data_9CDM
# 
_entry.id   9CDM 
# 
_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   9CDM         pdb_00009cdm 10.2210/pdb9cdm/pdb 
WWPDB D_1000285288 ?            ?                   
# 
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                        9CDM 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'different mutant with the same inhibitor' 9CDK unspecified 
PDB 'different mutant with the same inhibitor' 9CDL unspecified 
# 
_pdbx_contact_author.id                 4 
_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   0000-0002-6993-1212 
# 
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 
'Huynh, K.'      3 0000-0003-2501-8189 
'Anderson, K.S.' 4 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' 33859.562 1   3.4.22.69 L50F ? ? 
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    1   ?         ?    ? ? 
4 water       nat water 18.015    237 ?         ?    ? ? 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMFNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMFNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
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 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  PHE n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
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, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli 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 
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  PHE 50  50  50  PHE PHE A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
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 4 HOH 1   501 138 HOH HOH A . 
D 4 HOH 2   502 154 HOH HOH A . 
D 4 HOH 3   503 188 HOH HOH A . 
D 4 HOH 4   504 224 HOH HOH A . 
D 4 HOH 5   505 131 HOH HOH A . 
D 4 HOH 6   506 40  HOH HOH A . 
D 4 HOH 7   507 203 HOH HOH A . 
D 4 HOH 8   508 118 HOH HOH A . 
D 4 HOH 9   509 47  HOH HOH A . 
D 4 HOH 10  510 51  HOH HOH A . 
D 4 HOH 11  511 135 HOH HOH A . 
D 4 HOH 12  512 92  HOH HOH A . 
D 4 HOH 13  513 184 HOH HOH A . 
D 4 HOH 14  514 167 HOH HOH A . 
D 4 HOH 15  515 31  HOH HOH A . 
D 4 HOH 16  516 42  HOH HOH A . 
D 4 HOH 17  517 44  HOH HOH A . 
D 4 HOH 18  518 11  HOH HOH A . 
D 4 HOH 19  519 234 HOH HOH A . 
D 4 HOH 20  520 93  HOH HOH A . 
D 4 HOH 21  521 90  HOH HOH A . 
D 4 HOH 22  522 13  HOH HOH A . 
D 4 HOH 23  523 74  HOH HOH A . 
D 4 HOH 24  524 159 HOH HOH A . 
D 4 HOH 25  525 23  HOH HOH A . 
D 4 HOH 26  526 53  HOH HOH A . 
D 4 HOH 27  527 123 HOH HOH A . 
D 4 HOH 28  528 16  HOH HOH A . 
D 4 HOH 29  529 57  HOH HOH A . 
D 4 HOH 30  530 80  HOH HOH A . 
D 4 HOH 31  531 177 HOH HOH A . 
D 4 HOH 32  532 169 HOH HOH A . 
D 4 HOH 33  533 157 HOH HOH A . 
D 4 HOH 34  534 162 HOH HOH A . 
D 4 HOH 35  535 237 HOH HOH A . 
D 4 HOH 36  536 163 HOH HOH A . 
D 4 HOH 37  537 149 HOH HOH A . 
D 4 HOH 38  538 180 HOH HOH A . 
D 4 HOH 39  539 29  HOH HOH A . 
D 4 HOH 40  540 112 HOH HOH A . 
D 4 HOH 41  541 86  HOH HOH A . 
D 4 HOH 42  542 232 HOH HOH A . 
D 4 HOH 43  543 191 HOH HOH A . 
D 4 HOH 44  544 1   HOH HOH A . 
D 4 HOH 45  545 109 HOH HOH A . 
D 4 HOH 46  546 111 HOH HOH A . 
D 4 HOH 47  547 45  HOH HOH A . 
D 4 HOH 48  548 5   HOH HOH A . 
D 4 HOH 49  549 34  HOH HOH A . 
D 4 HOH 50  550 33  HOH HOH A . 
D 4 HOH 51  551 96  HOH HOH A . 
D 4 HOH 52  552 52  HOH HOH A . 
D 4 HOH 53  553 151 HOH HOH A . 
D 4 HOH 54  554 46  HOH HOH A . 
D 4 HOH 55  555 202 HOH HOH A . 
D 4 HOH 56  556 8   HOH HOH A . 
D 4 HOH 57  557 143 HOH HOH A . 
D 4 HOH 58  558 18  HOH HOH A . 
D 4 HOH 59  559 117 HOH HOH A . 
D 4 HOH 60  560 27  HOH HOH A . 
D 4 HOH 61  561 231 HOH HOH A . 
D 4 HOH 62  562 71  HOH HOH A . 
D 4 HOH 63  563 54  HOH HOH A . 
D 4 HOH 64  564 147 HOH HOH A . 
D 4 HOH 65  565 12  HOH HOH A . 
D 4 HOH 66  566 218 HOH HOH A . 
D 4 HOH 67  567 89  HOH HOH A . 
D 4 HOH 68  568 15  HOH HOH A . 
D 4 HOH 69  569 223 HOH HOH A . 
D 4 HOH 70  570 77  HOH HOH A . 
D 4 HOH 71  571 30  HOH HOH A . 
D 4 HOH 72  572 160 HOH HOH A . 
D 4 HOH 73  573 55  HOH HOH A . 
D 4 HOH 74  574 206 HOH HOH A . 
D 4 HOH 75  575 132 HOH HOH A . 
D 4 HOH 76  576 65  HOH HOH A . 
D 4 HOH 77  577 217 HOH HOH A . 
D 4 HOH 78  578 127 HOH HOH A . 
D 4 HOH 79  579 171 HOH HOH A . 
D 4 HOH 80  580 116 HOH HOH A . 
D 4 HOH 81  581 115 HOH HOH A . 
D 4 HOH 82  582 205 HOH HOH A . 
D 4 HOH 83  583 9   HOH HOH A . 
D 4 HOH 84  584 61  HOH HOH A . 
D 4 HOH 85  585 72  HOH HOH A . 
D 4 HOH 86  586 60  HOH HOH A . 
D 4 HOH 87  587 174 HOH HOH A . 
D 4 HOH 88  588 36  HOH HOH A . 
D 4 HOH 89  589 129 HOH HOH A . 
D 4 HOH 90  590 63  HOH HOH A . 
D 4 HOH 91  591 50  HOH HOH A . 
D 4 HOH 92  592 126 HOH HOH A . 
D 4 HOH 93  593 120 HOH HOH A . 
D 4 HOH 94  594 25  HOH HOH A . 
D 4 HOH 95  595 176 HOH HOH A . 
D 4 HOH 96  596 2   HOH HOH A . 
D 4 HOH 97  597 62  HOH HOH A . 
D 4 HOH 98  598 49  HOH HOH A . 
D 4 HOH 99  599 150 HOH HOH A . 
D 4 HOH 100 600 7   HOH HOH A . 
D 4 HOH 101 601 102 HOH HOH A . 
D 4 HOH 102 602 73  HOH HOH A . 
D 4 HOH 103 603 41  HOH HOH A . 
D 4 HOH 104 604 107 HOH HOH A . 
D 4 HOH 105 605 103 HOH HOH A . 
D 4 HOH 106 606 59  HOH HOH A . 
D 4 HOH 107 607 181 HOH HOH A . 
D 4 HOH 108 608 43  HOH HOH A . 
D 4 HOH 109 609 122 HOH HOH A . 
D 4 HOH 110 610 164 HOH HOH A . 
D 4 HOH 111 611 6   HOH HOH A . 
D 4 HOH 112 612 4   HOH HOH A . 
D 4 HOH 113 613 64  HOH HOH A . 
D 4 HOH 114 614 100 HOH HOH A . 
D 4 HOH 115 615 148 HOH HOH A . 
D 4 HOH 116 616 17  HOH HOH A . 
D 4 HOH 117 617 22  HOH HOH A . 
D 4 HOH 118 618 19  HOH HOH A . 
D 4 HOH 119 619 190 HOH HOH A . 
D 4 HOH 120 620 136 HOH HOH A . 
D 4 HOH 121 621 220 HOH HOH A . 
D 4 HOH 122 622 37  HOH HOH A . 
D 4 HOH 123 623 104 HOH HOH A . 
D 4 HOH 124 624 219 HOH HOH A . 
D 4 HOH 125 625 88  HOH HOH A . 
D 4 HOH 126 626 35  HOH HOH A . 
D 4 HOH 127 627 38  HOH HOH A . 
D 4 HOH 128 628 28  HOH HOH A . 
D 4 HOH 129 629 197 HOH HOH A . 
D 4 HOH 130 630 24  HOH HOH A . 
D 4 HOH 131 631 156 HOH HOH A . 
D 4 HOH 132 632 82  HOH HOH A . 
D 4 HOH 133 633 187 HOH HOH A . 
D 4 HOH 134 634 79  HOH HOH A . 
D 4 HOH 135 635 133 HOH HOH A . 
D 4 HOH 136 636 20  HOH HOH A . 
D 4 HOH 137 637 207 HOH HOH A . 
D 4 HOH 138 638 134 HOH HOH A . 
D 4 HOH 139 639 91  HOH HOH A . 
D 4 HOH 140 640 110 HOH HOH A . 
D 4 HOH 141 641 227 HOH HOH A . 
D 4 HOH 142 642 26  HOH HOH A . 
D 4 HOH 143 643 198 HOH HOH A . 
D 4 HOH 144 644 119 HOH HOH A . 
D 4 HOH 145 645 222 HOH HOH A . 
D 4 HOH 146 646 105 HOH HOH A . 
D 4 HOH 147 647 10  HOH HOH A . 
D 4 HOH 148 648 175 HOH HOH A . 
D 4 HOH 149 649 99  HOH HOH A . 
D 4 HOH 150 650 144 HOH HOH A . 
D 4 HOH 151 651 140 HOH HOH A . 
D 4 HOH 152 652 58  HOH HOH A . 
D 4 HOH 153 653 75  HOH HOH A . 
D 4 HOH 154 654 48  HOH HOH A . 
D 4 HOH 155 655 161 HOH HOH A . 
D 4 HOH 156 656 125 HOH HOH A . 
D 4 HOH 157 657 94  HOH HOH A . 
D 4 HOH 158 658 141 HOH HOH A . 
D 4 HOH 159 659 21  HOH HOH A . 
D 4 HOH 160 660 95  HOH HOH A . 
D 4 HOH 161 661 139 HOH HOH A . 
D 4 HOH 162 662 185 HOH HOH A . 
D 4 HOH 163 663 137 HOH HOH A . 
D 4 HOH 164 664 225 HOH HOH A . 
D 4 HOH 165 665 153 HOH HOH A . 
D 4 HOH 166 666 56  HOH HOH A . 
D 4 HOH 167 667 76  HOH HOH A . 
D 4 HOH 168 668 215 HOH HOH A . 
D 4 HOH 169 669 87  HOH HOH A . 
D 4 HOH 170 670 70  HOH HOH A . 
D 4 HOH 171 671 146 HOH HOH A . 
D 4 HOH 172 672 200 HOH HOH A . 
D 4 HOH 173 673 3   HOH HOH A . 
D 4 HOH 174 674 221 HOH HOH A . 
D 4 HOH 175 675 32  HOH HOH A . 
D 4 HOH 176 676 193 HOH HOH A . 
D 4 HOH 177 677 14  HOH HOH A . 
D 4 HOH 178 678 213 HOH HOH A . 
D 4 HOH 179 679 97  HOH HOH A . 
D 4 HOH 180 680 186 HOH HOH A . 
D 4 HOH 181 681 199 HOH HOH A . 
D 4 HOH 182 682 113 HOH HOH A . 
D 4 HOH 183 683 108 HOH HOH A . 
D 4 HOH 184 684 142 HOH HOH A . 
D 4 HOH 185 685 168 HOH HOH A . 
D 4 HOH 186 686 204 HOH HOH A . 
D 4 HOH 187 687 85  HOH HOH A . 
D 4 HOH 188 688 229 HOH HOH A . 
D 4 HOH 189 689 194 HOH HOH A . 
D 4 HOH 190 690 196 HOH HOH A . 
D 4 HOH 191 691 226 HOH HOH A . 
D 4 HOH 192 692 130 HOH HOH A . 
D 4 HOH 193 693 210 HOH HOH A . 
D 4 HOH 194 694 114 HOH HOH A . 
D 4 HOH 195 695 233 HOH HOH A . 
D 4 HOH 196 696 81  HOH HOH A . 
D 4 HOH 197 697 179 HOH HOH A . 
D 4 HOH 198 698 165 HOH HOH A . 
D 4 HOH 199 699 128 HOH HOH A . 
D 4 HOH 200 700 158 HOH HOH A . 
D 4 HOH 201 701 230 HOH HOH A . 
D 4 HOH 202 702 211 HOH HOH A . 
D 4 HOH 203 703 66  HOH HOH A . 
D 4 HOH 204 704 209 HOH HOH A . 
D 4 HOH 205 705 124 HOH HOH A . 
D 4 HOH 206 706 178 HOH HOH A . 
D 4 HOH 207 707 68  HOH HOH A . 
D 4 HOH 208 708 152 HOH HOH A . 
D 4 HOH 209 709 192 HOH HOH A . 
D 4 HOH 210 710 67  HOH HOH A . 
D 4 HOH 211 711 189 HOH HOH A . 
D 4 HOH 212 712 155 HOH HOH A . 
D 4 HOH 213 713 170 HOH HOH A . 
D 4 HOH 214 714 195 HOH HOH A . 
D 4 HOH 215 715 183 HOH HOH A . 
D 4 HOH 216 716 236 HOH HOH A . 
D 4 HOH 217 717 84  HOH HOH A . 
D 4 HOH 218 718 173 HOH HOH A . 
D 4 HOH 219 719 216 HOH HOH A . 
D 4 HOH 220 720 166 HOH HOH A . 
D 4 HOH 221 721 83  HOH HOH A . 
D 4 HOH 222 722 145 HOH HOH A . 
D 4 HOH 223 723 212 HOH HOH A . 
D 4 HOH 224 724 121 HOH HOH A . 
D 4 HOH 225 725 78  HOH HOH A . 
D 4 HOH 226 726 201 HOH HOH A . 
D 4 HOH 227 727 69  HOH HOH A . 
D 4 HOH 228 728 98  HOH HOH A . 
D 4 HOH 229 729 208 HOH HOH A . 
D 4 HOH 230 730 172 HOH HOH A . 
D 4 HOH 231 731 182 HOH HOH A . 
D 4 HOH 232 732 106 HOH HOH A . 
D 4 HOH 233 733 101 HOH HOH A . 
D 4 HOH 234 734 228 HOH HOH A . 
D 4 HOH 235 735 39  HOH HOH A . 
D 4 HOH 236 736 214 HOH HOH A . 
D 4 HOH 237 737 235 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 GLU 47  ? CG  ? A GLU 47  CG  
2  1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
3  1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
4  1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
5  1 Y 1 A ARG 217 ? CG  ? A ARG 217 CG  
6  1 Y 1 A ARG 217 ? CD  ? A ARG 217 CD  
7  1 Y 1 A ARG 217 ? NE  ? A ARG 217 NE  
8  1 Y 1 A ARG 217 ? CZ  ? A ARG 217 CZ  
9  1 Y 1 A ARG 217 ? NH1 ? A ARG 217 NH1 
10 1 Y 1 A ARG 217 ? NH2 ? A ARG 217 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                   101.11 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CDM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     115.665 
_cell.length_a_esd                 ? 
_cell.length_b                     54.346 
_cell.length_b_esd                 ? 
_cell.length_c                     44.524 
_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                         9CDM 
_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                   9CDM 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.04 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.63 
_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    
'0.2 M Ammonium citrate tribasic pH 7.0, 0.1 M Imidazole pH 7.0, 20% w/v Polyethylene glycol monomethyl ether 2,000' 
_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   0.920 
_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        0.920 
_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                                       9CDM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.05 
_reflns.d_resolution_low                               31.34 
_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                                     17132 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.68 
_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                                0.529 
_reflns.pdbx_Rpim_I_all                                0.232 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       89092 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.822 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.473 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.05 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           13074 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2500 
_reflns_shell.percent_possible_obs                          99.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.2 
_reflns_shell.pdbx_chi_squared                              0.80 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.367 
_reflns_shell.pdbx_Rpim_I_all                               0.599 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.408 
_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                                  1.222 
_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                                 9CDM 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.05 
_refine.ls_d_res_low                             31.34 
_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                     17087 
_refine.ls_number_reflns_R_free                  848 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.14 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1963 
_refine.ls_R_factor_R_free                       0.2370 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1942 
_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                          1.35 
_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                 22.35 
_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                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.05 
_refine_hist.d_res_low                        31.34 
_refine_hist.number_atoms_solvent             237 
_refine_hist.number_atoms_total               2631 
_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        2351 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.906  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.396 ? 334 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052  ? 369 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 430 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.05 2.18  . . 146 2667 99.00 . . . . 0.2254 . . . . . . . . . . . 0.2616 
'X-RAY DIFFRACTION' 2.18 2.34  . . 148 2702 99.00 . . . . 0.2095 . . . . . . . . . . . 0.2597 
'X-RAY DIFFRACTION' 2.34 2.58  . . 143 2674 99.00 . . . . 0.2110 . . . . . . . . . . . 0.2662 
'X-RAY DIFFRACTION' 2.58 2.95  . . 154 2689 99.00 . . . . 0.2075 . . . . . . . . . . . 0.2694 
'X-RAY DIFFRACTION' 2.95 3.72  . . 129 2725 99.00 . . . . 0.1744 . . . . . . . . . . . 0.1952 
'X-RAY DIFFRACTION' 3.72 31.34 . . 128 2782 99.00 . . . . 0.1555 . . . . . . . . . . . 0.1850 
# 
_struct.entry_id                     9CDM 
_struct.title                        'SARS-CoV-2 Mpro L50F 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        9CDM 
_struct_keywords.text            
'SARS-CoV-2, main protease, Mpro, 3CL, mutant, L50F, antiviral, small molecule inhibitor, 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 4 ? 
# 
_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              9CDM 
_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             9CDM 
_struct_ref_seq_dif.mon_id                       PHE 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      50 
_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                    LEU 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          3313 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            50 
_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)' 3560  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  24450 ? 
# 
_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 
# 
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 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 LYS A 61  ? HIS A 64  ? LYS A 61  HIS A 64  5 ? 4  
HELX_P HELX_P5  AA5 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P7  AA7 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
# 
_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 32  ? N LEU A 32  O VAL A 35  ? O VAL A 35  
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 162 ? N MET A 162 O THR A 175 ? O THR A 175 
# 
_pdbx_entry_details.entry_id                   9CDM 
_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 577 ? ? O A HOH 624 ? ? 1.92 
2  1 O   A HOH 579 ? ? O A HOH 682 ? ? 1.92 
3  1 O   A HOH 609 ? ? O A HOH 714 ? ? 2.02 
4  1 O   A HOH 557 ? ? O A HOH 695 ? ? 2.03 
5  1 O   A HOH 529 ? ? O A HOH 534 ? ? 2.04 
6  1 O   A HOH 610 ? ? O A HOH 725 ? ? 2.11 
7  1 NZ  A LYS 90  ? ? O A HOH 501 ? ? 2.12 
8  1 OE1 A GLU 290 ? ? O A HOH 502 ? ? 2.13 
9  1 OD1 A ASP 229 ? ? O A HOH 503 ? ? 2.15 
10 1 OD2 A ASP 48  ? ? O A HOH 504 ? ? 2.16 
11 1 NZ  A LYS 269 ? ? O A HOH 505 ? ? 2.17 
12 1 O   A HOH 645 ? ? O A HOH 661 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     523 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     657 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              1.74 
# 
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  ? ? 49.59   -130.82 
2 1 HIS A 41  ? ? -69.35  1.31    
3 1 ASP A 48  ? ? 56.25   6.50    
4 1 ASN A 51  ? ? -151.94 68.04   
5 1 ASN A 84  ? ? 52.53   -123.50 
6 1 TYR A 154 ? ? 63.60   -101.05 
7 1 SER A 301 ? ? -131.55 -37.99  
# 
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 673 ? D HOH . 
2 1 A HOH 734 ? D HOH . 
3 1 A HOH 736 ? D HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         12.2280 
_pdbx_refine_tls.origin_y         0.5197 
_pdbx_refine_tls.origin_z         4.7337 
_pdbx_refine_tls.T[1][1]          0.0148 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0002 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0002 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0606 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.1039 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0854 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.0245 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0008 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0074 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.0596 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0245 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.0200 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0407 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0153 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0052 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0019 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0340 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0321 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0136 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0085 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0041 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       737 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.98 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
_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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
XEK C1   C  N N 401 
XEK C2   C  N N 402 
XEK C3   C  Y N 403 
XEK C4   C  Y N 404 
XEK C5   C  Y N 405 
XEK C6   C  Y N 406 
XEK C7   C  Y N 407 
XEK C8   C  N N 408 
XEK C9   C  Y N 409 
XEK C10  C  Y N 410 
XEK C11  C  Y N 411 
XEK C12  C  Y N 412 
XEK C13  C  Y N 413 
XEK C14  C  Y N 414 
XEK C15  C  Y N 415 
XEK C17  C  N N 416 
XEK C21  C  N N 417 
XEK C22  C  N N 418 
XEK C24  C  Y N 419 
XEK C25  C  Y N 420 
XEK C27  C  Y N 421 
XEK C16  C  N N 422 
XEK C18  C  N N 423 
XEK C19  C  N N 424 
XEK C20  C  N N 425 
XEK C23  C  N N 426 
XEK C26  C  Y N 427 
XEK C28  C  Y N 428 
XEK F1   F  N N 429 
XEK N1   N  N N 430 
XEK N2   N  N N 431 
XEK N3   N  N N 432 
XEK N4   N  Y N 433 
XEK O1   O  N N 434 
XEK O2   O  N N 435 
XEK O3   O  N N 436 
XEK O4   O  N N 437 
XEK CL1  CL N N 438 
XEK CL2  CL N N 439 
XEK H1   H  N N 440 
XEK H2   H  N N 441 
XEK H3   H  N N 442 
XEK H4   H  N N 443 
XEK H5   H  N N 444 
XEK H6   H  N N 445 
XEK H7   H  N N 446 
XEK H8   H  N N 447 
XEK H13  H  N N 448 
XEK H14  H  N N 449 
XEK H12  H  N N 450 
XEK H16  H  N N 451 
XEK H18  H  N N 452 
XEK H9   H  N N 453 
XEK H11  H  N N 454 
XEK H15  H  N N 455 
XEK H17  H  N N 456 
XEK H19  H  N N 457 
XEK H10  H  N N 458 
# 
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                    9CDM 
_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]   0.008646 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001698 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018401 
_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]   0.022889 
_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   ? -3.045 4.775   -16.633 1.00 10.75 ? 1   SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? -2.394 5.912   -15.998 1.00 16.79 ? 1   SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? -2.848 6.102   -14.544 1.00 11.90 ? 1   SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? -3.616 5.305   -14.009 1.00 12.28 ? 1   SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? -2.652 7.187   -16.809 1.00 18.48 ? 1   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? -3.948 7.684   -16.549 1.00 19.14 ? 1   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2   ? -2.376 7.174   -13.916 1.00 13.54 ? 2   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2   ? -2.538 7.391   -12.496 1.00 9.98  ? 2   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2   ? -1.263 7.045   -11.753 1.00 12.03 ? 2   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2   ? -0.388 6.341   -12.258 1.00 16.89 ? 2   GLY A O   1 
ATOM   11   N  N   . PHE A 1 3   ? -1.135 7.565   -10.533 1.00 13.60 ? 3   PHE A N   1 
ATOM   12   C  CA  . PHE A 1 3   ? 0.101  7.338   -9.787  1.00 11.34 ? 3   PHE A CA  1 
ATOM   13   C  C   . PHE A 1 3   ? -0.185 7.213   -8.301  1.00 11.89 ? 3   PHE A C   1 
ATOM   14   O  O   . PHE A 1 3   ? -0.663 8.160   -7.670  1.00 13.31 ? 3   PHE A O   1 
ATOM   15   C  CB  . PHE A 1 3   ? 1.136  8.443   -10.038 1.00 9.04  ? 3   PHE A CB  1 
ATOM   16   C  CG  . PHE A 1 3   ? 2.546  7.964   -9.846  1.00 11.55 ? 3   PHE A CG  1 
ATOM   17   C  CD1 . PHE A 1 3   ? 3.125  7.109   -10.778 1.00 11.34 ? 3   PHE A CD1 1 
ATOM   18   C  CD2 . PHE A 1 3   ? 3.265  8.295   -8.706  1.00 10.46 ? 3   PHE A CD2 1 
ATOM   19   C  CE1 . PHE A 1 3   ? 4.410  6.626   -10.609 1.00 11.92 ? 3   PHE A CE1 1 
ATOM   20   C  CE2 . PHE A 1 3   ? 4.559  7.811   -8.523  1.00 12.11 ? 3   PHE A CE2 1 
ATOM   21   C  CZ  . PHE A 1 3   ? 5.129  6.973   -9.476  1.00 11.71 ? 3   PHE A CZ  1 
ATOM   22   N  N   . ARG A 1 4   ? 0.158  6.050   -7.744  1.00 11.75 ? 4   ARG A N   1 
ATOM   23   C  CA  . ARG A 1 4   ? -0.158 5.705   -6.371  1.00 9.85  ? 4   ARG A CA  1 
ATOM   24   C  C   . ARG A 1 4   ? 1.095  5.316   -5.610  1.00 10.74 ? 4   ARG A C   1 
ATOM   25   O  O   . ARG A 1 4   ? 2.081  4.859   -6.196  1.00 7.88  ? 4   ARG A O   1 
ATOM   26   C  CB  . ARG A 1 4   ? -1.157 4.539   -6.311  1.00 11.72 ? 4   ARG A CB  1 
ATOM   27   C  CG  . ARG A 1 4   ? -2.572 4.961   -6.647  1.00 13.98 ? 4   ARG A CG  1 
ATOM   28   C  CD  . ARG A 1 4   ? -3.292 5.363   -5.359  1.00 17.07 ? 4   ARG A CD  1 
ATOM   29   N  NE  . ARG A 1 4   ? -4.568 6.025   -5.616  1.00 18.63 ? 4   ARG A NE  1 
ATOM   30   C  CZ  . ARG A 1 4   ? -5.251 6.700   -4.701  1.00 18.09 ? 4   ARG A CZ  1 
ATOM   31   N  NH1 . ARG A 1 4   ? -4.800 6.835   -3.465  1.00 17.57 ? 4   ARG A NH1 1 
ATOM   32   N  NH2 . ARG A 1 4   ? -6.418 7.244   -5.031  1.00 13.98 ? 4   ARG A NH2 1 
ATOM   33   N  N   . LYS A 1 5   ? 1.037  5.493   -4.290  1.00 9.95  ? 5   LYS A N   1 
ATOM   34   C  CA  . LYS A 1 5   ? 2.013  4.911   -3.371  1.00 13.38 ? 5   LYS A CA  1 
ATOM   35   C  C   . LYS A 1 5   ? 1.744  3.408   -3.278  1.00 8.54  ? 5   LYS A C   1 
ATOM   36   O  O   . LYS A 1 5   ? 0.904  2.954   -2.502  1.00 15.76 ? 5   LYS A O   1 
ATOM   37   C  CB  . LYS A 1 5   ? 1.917  5.596   -2.007  1.00 12.62 ? 5   LYS A CB  1 
ATOM   38   C  CG  . LYS A 1 5   ? 3.190  5.523   -1.199  1.00 14.44 ? 5   LYS A CG  1 
ATOM   39   C  CD  . LYS A 1 5   ? 3.423  6.788   -0.329  1.00 18.53 ? 5   LYS A CD  1 
ATOM   40   C  CE  . LYS A 1 5   ? 4.434  7.700   -1.000  1.00 18.67 ? 5   LYS A CE  1 
ATOM   41   N  NZ  . LYS A 1 5   ? 5.559  6.835   -1.504  1.00 14.67 ? 5   LYS A NZ  1 
ATOM   42   N  N   . MET A 1 6   ? 2.467  2.622   -4.061  1.00 10.39 ? 6   MET A N   1 
ATOM   43   C  CA  . MET A 1 6   ? 2.163  1.215   -4.280  1.00 9.88  ? 6   MET A CA  1 
ATOM   44   C  C   . MET A 1 6   ? 3.175  0.321   -3.579  1.00 6.38  ? 6   MET A C   1 
ATOM   45   O  O   . MET A 1 6   ? 4.386  0.506   -3.728  1.00 2.83  ? 6   MET A O   1 
ATOM   46   C  CB  . MET A 1 6   ? 2.173  0.902   -5.776  1.00 8.03  ? 6   MET A CB  1 
ATOM   47   C  CG  . MET A 1 6   ? 1.063  0.009   -6.245  1.00 19.97 ? 6   MET A CG  1 
ATOM   48   S  SD  . MET A 1 6   ? 1.206  -0.093  -8.047  1.00 20.76 ? 6   MET A SD  1 
ATOM   49   C  CE  . MET A 1 6   ? 2.769  -0.922  -8.175  1.00 13.00 ? 6   MET A CE  1 
ATOM   50   N  N   . ALA A 1 7   ? 2.678  -0.685  -2.877  1.00 10.58 ? 7   ALA A N   1 
ATOM   51   C  CA  . ALA A 1 7   ? 3.531  -1.673  -2.235  1.00 7.21  ? 7   ALA A CA  1 
ATOM   52   C  C   . ALA A 1 7   ? 3.563  -2.968  -3.045  1.00 11.27 ? 7   ALA A C   1 
ATOM   53   O  O   . ALA A 1 7   ? 2.671  -3.241  -3.860  1.00 6.29  ? 7   ALA A O   1 
ATOM   54   C  CB  . ALA A 1 7   ? 3.042  -1.953  -0.817  1.00 8.57  ? 7   ALA A CB  1 
ATOM   55   N  N   . PHE A 1 8   ? 4.610  -3.771  -2.809  1.00 8.48  ? 8   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 8   ? 4.682  -5.085  -3.432  1.00 8.57  ? 8   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 8   ? 3.595  -5.992  -2.872  1.00 6.86  ? 8   PHE A C   1 
ATOM   58   O  O   . PHE A 1 8   ? 3.212  -5.863  -1.706  1.00 6.27  ? 8   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 8   ? 6.044  -5.746  -3.213  1.00 4.94  ? 8   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 8   ? 7.128  -5.141  -4.034  1.00 9.18  ? 8   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 8   ? 7.221  -5.410  -5.383  1.00 12.43 ? 8   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 8   ? 8.025  -4.254  -3.469  1.00 8.79  ? 8   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 8   ? 8.211  -4.832  -6.150  1.00 19.18 ? 8   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 8   ? 9.024  -3.654  -4.245  1.00 10.30 ? 8   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 8   ? 9.118  -3.955  -5.578  1.00 16.56 ? 8   PHE A CZ  1 
ATOM   66   N  N   . PRO A 1 9   ? 3.096  -6.929  -3.680  1.00 5.26  ? 9   PRO A N   1 
ATOM   67   C  CA  . PRO A 1 9   ? 2.221  -7.971  -3.137  1.00 6.08  ? 9   PRO A CA  1 
ATOM   68   C  C   . PRO A 1 9   ? 2.939  -8.686  -1.999  1.00 6.37  ? 9   PRO A C   1 
ATOM   69   O  O   . PRO A 1 9   ? 4.085  -9.123  -2.135  1.00 6.43  ? 9   PRO A O   1 
ATOM   70   C  CB  . PRO A 1 9   ? 1.959  -8.891  -4.337  1.00 6.14  ? 9   PRO A CB  1 
ATOM   71   C  CG  . PRO A 1 9   ? 2.307  -8.059  -5.559  1.00 10.83 ? 9   PRO A CG  1 
ATOM   72   C  CD  . PRO A 1 9   ? 3.438  -7.161  -5.091  1.00 9.49  ? 9   PRO A CD  1 
ATOM   73   N  N   . SER A 1 10  ? 2.264  -8.758  -0.860  1.00 7.11  ? 10  SER A N   1 
ATOM   74   C  CA  . SER A 1 10  ? 2.842  -9.188  0.409   1.00 8.99  ? 10  SER A CA  1 
ATOM   75   C  C   . SER A 1 10  ? 2.663  -10.674 0.667   1.00 5.83  ? 10  SER A C   1 
ATOM   76   O  O   . SER A 1 10  ? 3.030  -11.144 1.748   1.00 7.14  ? 10  SER A O   1 
ATOM   77   C  CB  . SER A 1 10  ? 2.211  -8.400  1.569   1.00 6.99  ? 10  SER A CB  1 
ATOM   78   O  OG  . SER A 1 10  ? 0.822  -8.693  1.726   1.00 5.14  ? 10  SER A OG  1 
ATOM   79   N  N   . GLY A 1 11  ? 2.112  -11.416 -0.298  1.00 5.59  ? 11  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 11  ? 1.825  -12.828 -0.075  1.00 5.52  ? 11  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 11  ? 3.053  -13.644 0.293   1.00 6.07  ? 11  GLY A C   1 
ATOM   82   O  O   . GLY A 1 11  ? 3.030  -14.418 1.251   1.00 6.16  ? 11  GLY A O   1 
ATOM   83   N  N   . LYS A 1 12  ? 4.139  -13.498 -0.475  1.00 3.14  ? 12  LYS A N   1 
ATOM   84   C  CA  . LYS A 1 12  ? 5.336  -14.285 -0.209  1.00 4.95  ? 12  LYS A CA  1 
ATOM   85   C  C   . LYS A 1 12  ? 5.867  -14.058 1.202   1.00 7.23  ? 12  LYS A C   1 
ATOM   86   O  O   . LYS A 1 12  ? 6.506  -14.949 1.768   1.00 7.42  ? 12  LYS A O   1 
ATOM   87   C  CB  . LYS A 1 12  ? 6.413  -13.961 -1.240  1.00 9.77  ? 12  LYS A CB  1 
ATOM   88   C  CG  . LYS A 1 12  ? 6.179  -14.656 -2.578  1.00 11.58 ? 12  LYS A CG  1 
ATOM   89   C  CD  . LYS A 1 12  ? 6.417  -13.730 -3.734  1.00 16.93 ? 12  LYS A CD  1 
ATOM   90   C  CE  . LYS A 1 12  ? 6.129  -14.429 -5.053  1.00 25.83 ? 12  LYS A CE  1 
ATOM   91   N  NZ  . LYS A 1 12  ? 7.208  -15.407 -5.367  1.00 29.30 ? 12  LYS A NZ  1 
ATOM   92   N  N   . VAL A 1 13  ? 5.598  -12.895 1.795   1.00 4.45  ? 13  VAL A N   1 
ATOM   93   C  CA  . VAL A 1 13  ? 6.077  -12.634 3.150   1.00 4.04  ? 13  VAL A CA  1 
ATOM   94   C  C   . VAL A 1 13  ? 5.063  -13.050 4.217   1.00 4.05  ? 13  VAL A C   1 
ATOM   95   O  O   . VAL A 1 13  ? 5.461  -13.520 5.287   1.00 4.26  ? 13  VAL A O   1 
ATOM   96   C  CB  . VAL A 1 13  ? 6.471  -11.156 3.303   1.00 5.15  ? 13  VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 13  ? 7.070  -10.880 4.730   1.00 3.42  ? 13  VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 13  ? 7.433  -10.760 2.188   1.00 4.73  ? 13  VAL A CG2 1 
ATOM   99   N  N   . GLU A 1 14  ? 3.760  -12.899 3.954   1.00 3.44  ? 14  GLU A N   1 
ATOM   100  C  CA  . GLU A 1 14  ? 2.760  -13.309 4.941   1.00 4.85  ? 14  GLU A CA  1 
ATOM   101  C  C   . GLU A 1 14  ? 3.001  -14.738 5.408   1.00 4.93  ? 14  GLU A C   1 
ATOM   102  O  O   . GLU A 1 14  ? 2.824  -15.054 6.591   1.00 2.17  ? 14  GLU A O   1 
ATOM   103  C  CB  . GLU A 1 14  ? 1.341  -13.189 4.361   1.00 5.19  ? 14  GLU A CB  1 
ATOM   104  C  CG  . GLU A 1 14  ? 0.802  -11.775 4.198   1.00 5.31  ? 14  GLU A CG  1 
ATOM   105  C  CD  . GLU A 1 14  ? -0.384 -11.754 3.240   1.00 6.70  ? 14  GLU A CD  1 
ATOM   106  O  OE1 . GLU A 1 14  ? -1.323 -12.533 3.446   1.00 5.69  ? 14  GLU A OE1 1 
ATOM   107  O  OE2 . GLU A 1 14  ? -0.376 -10.990 2.257   1.00 5.62  ? 14  GLU A OE2 1 
ATOM   108  N  N   . GLY A 1 15  ? 3.398  -15.620 4.488   1.00 4.27  ? 15  GLY A N   1 
ATOM   109  C  CA  . GLY A 1 15  ? 3.624  -17.009 4.822   1.00 6.29  ? 15  GLY A CA  1 
ATOM   110  C  C   . GLY A 1 15  ? 4.865  -17.280 5.635   1.00 6.57  ? 15  GLY A C   1 
ATOM   111  O  O   . GLY A 1 15  ? 5.117  -18.433 5.991   1.00 4.79  ? 15  GLY A O   1 
ATOM   112  N  N   . CYS A 1 16  ? 5.667  -16.260 5.921   1.00 6.39  ? 16  CYS A N   1 
ATOM   113  C  CA  . CYS A 1 16  ? 6.857  -16.424 6.735   1.00 6.00  ? 16  CYS A CA  1 
ATOM   114  C  C   . CYS A 1 16  ? 6.695  -15.840 8.126   1.00 5.54  ? 16  CYS A C   1 
ATOM   115  O  O   . CYS A 1 16  ? 7.621  -15.944 8.932   1.00 5.50  ? 16  CYS A O   1 
ATOM   116  C  CB  . CYS A 1 16  ? 8.074  -15.773 6.059   1.00 2.79  ? 16  CYS A CB  1 
ATOM   117  S  SG  . CYS A 1 16  ? 8.472  -16.333 4.388   1.00 9.29  ? 16  CYS A SG  1 
ATOM   118  N  N   . MET A 1 17  ? 5.562  -15.211 8.426   1.00 5.58  ? 17  MET A N   1 
ATOM   119  C  CA  . MET A 1 17  ? 5.410  -14.518 9.692   1.00 5.25  ? 17  MET A CA  1 
ATOM   120  C  C   . MET A 1 17  ? 5.002  -15.498 10.782  1.00 8.88  ? 17  MET A C   1 
ATOM   121  O  O   . MET A 1 17  ? 4.082  -16.304 10.596  1.00 6.98  ? 17  MET A O   1 
ATOM   122  C  CB  . MET A 1 17  ? 4.385  -13.390 9.566   1.00 7.84  ? 17  MET A CB  1 
ATOM   123  C  CG  . MET A 1 17  ? 4.795  -12.293 8.579   1.00 5.57  ? 17  MET A CG  1 
ATOM   124  S  SD  . MET A 1 17  ? 6.516  -11.730 8.672   1.00 5.48  ? 17  MET A SD  1 
ATOM   125  C  CE  . MET A 1 17  ? 6.626  -11.072 10.356  1.00 6.82  ? 17  MET A CE  1 
ATOM   126  N  N   . VAL A 1 18  ? 5.695  -15.435 11.920  1.00 6.40  ? 18  VAL A N   1 
ATOM   127  C  CA  . VAL A 1 18  ? 5.357  -16.251 13.076  1.00 5.88  ? 18  VAL A CA  1 
ATOM   128  C  C   . VAL A 1 18  ? 5.334  -15.382 14.322  1.00 7.37  ? 18  VAL A C   1 
ATOM   129  O  O   . VAL A 1 18  ? 5.763  -14.228 14.324  1.00 5.74  ? 18  VAL A O   1 
ATOM   130  C  CB  . VAL A 1 18  ? 6.323  -17.438 13.269  1.00 6.06  ? 18  VAL A CB  1 
ATOM   131  C  CG1 . VAL A 1 18  ? 6.350  -18.323 12.015  1.00 6.37  ? 18  VAL A CG1 1 
ATOM   132  C  CG2 . VAL A 1 18  ? 7.707  -16.952 13.618  1.00 4.60  ? 18  VAL A CG2 1 
ATOM   133  N  N   . GLN A 1 19  ? 4.813  -15.962 15.396  1.00 10.42 ? 19  GLN A N   1 
ATOM   134  C  CA  . GLN A 1 19  ? 4.751  -15.313 16.696  1.00 11.16 ? 19  GLN A CA  1 
ATOM   135  C  C   . GLN A 1 19  ? 5.810  -15.947 17.585  1.00 8.91  ? 19  GLN A C   1 
ATOM   136  O  O   . GLN A 1 19  ? 5.809  -17.167 17.771  1.00 9.82  ? 19  GLN A O   1 
ATOM   137  C  CB  . GLN A 1 19  ? 3.362  -15.466 17.311  1.00 12.61 ? 19  GLN A CB  1 
ATOM   138  C  CG  . GLN A 1 19  ? 3.254  -14.997 18.746  1.00 14.81 ? 19  GLN A CG  1 
ATOM   139  C  CD  . GLN A 1 19  ? 2.001  -15.518 19.421  1.00 22.50 ? 19  GLN A CD  1 
ATOM   140  O  OE1 . GLN A 1 19  ? 0.971  -14.838 19.452  1.00 30.80 ? 19  GLN A OE1 1 
ATOM   141  N  NE2 . GLN A 1 19  ? 2.076  -16.731 19.961  1.00 22.64 ? 19  GLN A NE2 1 
ATOM   142  N  N   . VAL A 1 20  ? 6.708  -15.123 18.122  1.00 9.78  ? 20  VAL A N   1 
ATOM   143  C  CA  . VAL A 1 20  ? 7.802  -15.575 18.982  1.00 11.37 ? 20  VAL A CA  1 
ATOM   144  C  C   . VAL A 1 20  ? 7.524  -15.073 20.393  1.00 11.93 ? 20  VAL A C   1 
ATOM   145  O  O   . VAL A 1 20  ? 7.357  -13.864 20.606  1.00 13.68 ? 20  VAL A O   1 
ATOM   146  C  CB  . VAL A 1 20  ? 9.170  -15.068 18.487  1.00 10.68 ? 20  VAL A CB  1 
ATOM   147  C  CG1 . VAL A 1 20  ? 10.259 -15.411 19.497  1.00 6.78  ? 20  VAL A CG1 1 
ATOM   148  C  CG2 . VAL A 1 20  ? 9.509  -15.611 17.088  1.00 5.77  ? 20  VAL A CG2 1 
ATOM   149  N  N   . THR A 1 21  ? 7.519  -15.987 21.365  1.00 14.59 ? 21  THR A N   1 
ATOM   150  C  CA  . THR A 1 21  ? 7.277  -15.659 22.768  1.00 12.21 ? 21  THR A CA  1 
ATOM   151  C  C   . THR A 1 21  ? 8.474  -16.102 23.604  1.00 14.11 ? 21  THR A C   1 
ATOM   152  O  O   . THR A 1 21  ? 8.960  -17.229 23.454  1.00 14.93 ? 21  THR A O   1 
ATOM   153  C  CB  . THR A 1 21  ? 5.989  -16.336 23.283  1.00 15.13 ? 21  THR A CB  1 
ATOM   154  O  OG1 . THR A 1 21  ? 4.840  -15.722 22.690  1.00 10.81 ? 21  THR A OG1 1 
ATOM   155  C  CG2 . THR A 1 21  ? 5.872  -16.254 24.796  1.00 10.77 ? 21  THR A CG2 1 
ATOM   156  N  N   . CYS A 1 22  ? 8.959  -15.211 24.469  1.00 15.36 ? 22  CYS A N   1 
ATOM   157  C  CA  . CYS A 1 22  ? 10.024 -15.535 25.416  1.00 15.38 ? 22  CYS A CA  1 
ATOM   158  C  C   . CYS A 1 22  ? 9.618  -14.948 26.756  1.00 12.64 ? 22  CYS A C   1 
ATOM   159  O  O   . CYS A 1 22  ? 9.639  -13.730 26.924  1.00 14.56 ? 22  CYS A O   1 
ATOM   160  C  CB  . CYS A 1 22  ? 11.377 -14.976 24.967  1.00 11.00 ? 22  CYS A CB  1 
ATOM   161  S  SG  . CYS A 1 22  ? 12.779 -15.609 25.936  1.00 20.26 ? 22  CYS A SG  1 
ATOM   162  N  N   . GLY A 1 23  ? 9.256  -15.797 27.707  1.00 19.39 ? 23  GLY A N   1 
ATOM   163  C  CA  . GLY A 1 23  ? 8.737  -15.262 28.957  1.00 17.24 ? 23  GLY A CA  1 
ATOM   164  C  C   . GLY A 1 23  ? 7.437  -14.534 28.704  1.00 15.61 ? 23  GLY A C   1 
ATOM   165  O  O   . GLY A 1 23  ? 6.501  -15.082 28.112  1.00 19.23 ? 23  GLY A O   1 
ATOM   166  N  N   . THR A 1 24  ? 7.373  -13.275 29.130  1.00 23.95 ? 24  THR A N   1 
ATOM   167  C  CA  . THR A 1 24  ? 6.163  -12.486 28.938  1.00 25.07 ? 24  THR A CA  1 
ATOM   168  C  C   . THR A 1 24  ? 6.104  -11.818 27.572  1.00 20.61 ? 24  THR A C   1 
ATOM   169  O  O   . THR A 1 24  ? 5.010  -11.478 27.116  1.00 24.79 ? 24  THR A O   1 
ATOM   170  C  CB  . THR A 1 24  ? 6.061  -11.411 30.016  1.00 29.00 ? 24  THR A CB  1 
ATOM   171  O  OG1 . THR A 1 24  ? 7.316  -10.721 30.114  1.00 32.27 ? 24  THR A OG1 1 
ATOM   172  C  CG2 . THR A 1 24  ? 5.724  -12.054 31.356  1.00 33.55 ? 24  THR A CG2 1 
ATOM   173  N  N   . THR A 1 25  ? 7.241  -11.632 26.909  1.00 22.39 ? 25  THR A N   1 
ATOM   174  C  CA  . THR A 1 25  ? 7.265  -10.925 25.635  1.00 20.80 ? 25  THR A CA  1 
ATOM   175  C  C   . THR A 1 25  ? 6.814  -11.825 24.488  1.00 14.68 ? 25  THR A C   1 
ATOM   176  O  O   . THR A 1 25  ? 7.335  -12.928 24.314  1.00 14.11 ? 25  THR A O   1 
ATOM   177  C  CB  . THR A 1 25  ? 8.668  -10.407 25.338  1.00 21.89 ? 25  THR A CB  1 
ATOM   178  O  OG1 . THR A 1 25  ? 9.080  -9.489  26.361  1.00 18.43 ? 25  THR A OG1 1 
ATOM   179  C  CG2 . THR A 1 25  ? 8.675  -9.726  23.967  1.00 18.15 ? 25  THR A CG2 1 
ATOM   180  N  N   . THR A 1 26  ? 5.831  -11.353 23.722  1.00 12.94 ? 26  THR A N   1 
ATOM   181  C  CA  . THR A 1 26  ? 5.489  -11.887 22.408  1.00 14.40 ? 26  THR A CA  1 
ATOM   182  C  C   . THR A 1 26  ? 5.700  -10.797 21.369  1.00 14.49 ? 26  THR A C   1 
ATOM   183  O  O   . THR A 1 26  ? 5.284  -9.652  21.577  1.00 16.84 ? 26  THR A O   1 
ATOM   184  C  CB  . THR A 1 26  ? 4.038  -12.365 22.334  1.00 13.79 ? 26  THR A CB  1 
ATOM   185  O  OG1 . THR A 1 26  ? 3.828  -13.424 23.274  1.00 18.77 ? 26  THR A OG1 1 
ATOM   186  C  CG2 . THR A 1 26  ? 3.729  -12.877 20.948  1.00 15.27 ? 26  THR A CG2 1 
ATOM   187  N  N   . LEU A 1 27  ? 6.345  -11.148 20.261  1.00 9.70  ? 27  LEU A N   1 
ATOM   188  C  CA  . LEU A 1 27  ? 6.502  -10.221 19.142  1.00 8.50  ? 27  LEU A CA  1 
ATOM   189  C  C   . LEU A 1 27  ? 6.629  -11.050 17.865  1.00 5.19  ? 27  LEU A C   1 
ATOM   190  O  O   . LEU A 1 27  ? 6.427  -12.266 17.881  1.00 6.00  ? 27  LEU A O   1 
ATOM   191  C  CB  . LEU A 1 27  ? 7.687  -9.273  19.390  1.00 9.26  ? 27  LEU A CB  1 
ATOM   192  C  CG  . LEU A 1 27  ? 8.978  -9.843  19.983  1.00 7.95  ? 27  LEU A CG  1 
ATOM   193  C  CD1 . LEU A 1 27  ? 9.529  -10.945 19.094  1.00 11.02 ? 27  LEU A CD1 1 
ATOM   194  C  CD2 . LEU A 1 27  ? 10.001 -8.741  20.155  1.00 8.53  ? 27  LEU A CD2 1 
ATOM   195  N  N   . ASN A 1 28  ? 6.942  -10.397 16.745  1.00 5.35  ? 28  ASN A N   1 
ATOM   196  C  CA  . ASN A 1 28  ? 6.876  -11.065 15.443  1.00 4.11  ? 28  ASN A CA  1 
ATOM   197  C  C   . ASN A 1 28  ? 8.227  -11.653 15.032  1.00 5.17  ? 28  ASN A C   1 
ATOM   198  O  O   . ASN A 1 28  ? 9.285  -11.154 15.420  1.00 3.08  ? 28  ASN A O   1 
ATOM   199  C  CB  . ASN A 1 28  ? 6.367  -10.100 14.365  1.00 5.57  ? 28  ASN A CB  1 
ATOM   200  C  CG  . ASN A 1 28  ? 5.015  -9.454  14.740  1.00 6.91  ? 28  ASN A CG  1 
ATOM   201  O  OD1 . ASN A 1 28  ? 3.961  -10.089 14.661  1.00 5.52  ? 28  ASN A OD1 1 
ATOM   202  N  ND2 . ASN A 1 28  ? 5.056  -8.192  15.162  1.00 7.59  ? 28  ASN A ND2 1 
ATOM   203  N  N   . GLY A 1 29  ? 8.174  -12.739 14.243  1.00 2.69  ? 29  GLY A N   1 
ATOM   204  C  CA  . GLY A 1 29  ? 9.379  -13.393 13.772  1.00 2.23  ? 29  GLY A CA  1 
ATOM   205  C  C   . GLY A 1 29  ? 9.253  -13.780 12.311  1.00 3.32  ? 29  GLY A C   1 
ATOM   206  O  O   . GLY A 1 29  ? 8.154  -13.843 11.756  1.00 3.32  ? 29  GLY A O   1 
ATOM   207  N  N   . LEU A 1 30  ? 10.406 -14.046 11.692  1.00 3.21  ? 30  LEU A N   1 
ATOM   208  C  CA  . LEU A 1 30  ? 10.495 -14.322 10.255  1.00 5.94  ? 30  LEU A CA  1 
ATOM   209  C  C   . LEU A 1 30  ? 11.067 -15.721 10.034  1.00 3.82  ? 30  LEU A C   1 
ATOM   210  O  O   . LEU A 1 30  ? 12.252 -15.970 10.291  1.00 3.89  ? 30  LEU A O   1 
ATOM   211  C  CB  . LEU A 1 30  ? 11.337 -13.261 9.537   1.00 1.97  ? 30  LEU A CB  1 
ATOM   212  C  CG  . LEU A 1 30  ? 11.401 -13.371 8.002   1.00 6.59  ? 30  LEU A CG  1 
ATOM   213  C  CD1 . LEU A 1 30  ? 10.082 -12.964 7.336   1.00 5.32  ? 30  LEU A CD1 1 
ATOM   214  C  CD2 . LEU A 1 30  ? 12.521 -12.516 7.454   1.00 5.36  ? 30  LEU A CD2 1 
ATOM   215  N  N   . TRP A 1 31  ? 10.225 -16.624 9.541   1.00 4.73  ? 31  TRP A N   1 
ATOM   216  C  CA  . TRP A 1 31  ? 10.555 -18.038 9.418   1.00 6.90  ? 31  TRP A CA  1 
ATOM   217  C  C   . TRP A 1 31  ? 10.922 -18.329 7.962   1.00 6.02  ? 31  TRP A C   1 
ATOM   218  O  O   . TRP A 1 31  ? 10.077 -18.235 7.073   1.00 5.47  ? 31  TRP A O   1 
ATOM   219  C  CB  . TRP A 1 31  ? 9.376  -18.883 9.894   1.00 5.60  ? 31  TRP A CB  1 
ATOM   220  C  CG  . TRP A 1 31  ? 9.586  -20.350 9.820   1.00 7.25  ? 31  TRP A CG  1 
ATOM   221  C  CD1 . TRP A 1 31  ? 10.785 -21.020 9.800   1.00 6.11  ? 31  TRP A CD1 1 
ATOM   222  C  CD2 . TRP A 1 31  ? 8.564  -21.354 9.762   1.00 9.35  ? 31  TRP A CD2 1 
ATOM   223  N  NE1 . TRP A 1 31  ? 10.563 -22.373 9.717   1.00 9.03  ? 31  TRP A NE1 1 
ATOM   224  C  CE2 . TRP A 1 31  ? 9.211  -22.607 9.710   1.00 9.37  ? 31  TRP A CE2 1 
ATOM   225  C  CE3 . TRP A 1 31  ? 7.164  -21.314 9.765   1.00 7.92  ? 31  TRP A CE3 1 
ATOM   226  C  CZ2 . TRP A 1 31  ? 8.507  -23.812 9.643   1.00 9.19  ? 31  TRP A CZ2 1 
ATOM   227  C  CZ3 . TRP A 1 31  ? 6.466  -22.515 9.696   1.00 11.70 ? 31  TRP A CZ3 1 
ATOM   228  C  CH2 . TRP A 1 31  ? 7.144  -23.745 9.641   1.00 7.83  ? 31  TRP A CH2 1 
ATOM   229  N  N   . LEU A 1 32  ? 12.190 -18.671 7.733   1.00 6.84  ? 32  LEU A N   1 
ATOM   230  C  CA  . LEU A 1 32  ? 12.758 -18.904 6.413   1.00 8.13  ? 32  LEU A CA  1 
ATOM   231  C  C   . LEU A 1 32  ? 13.646 -20.139 6.490   1.00 10.45 ? 32  LEU A C   1 
ATOM   232  O  O   . LEU A 1 32  ? 14.530 -20.213 7.353   1.00 8.84  ? 32  LEU A O   1 
ATOM   233  C  CB  . LEU A 1 32  ? 13.585 -17.706 5.947   1.00 6.30  ? 32  LEU A CB  1 
ATOM   234  C  CG  . LEU A 1 32  ? 12.859 -16.372 5.802   1.00 7.92  ? 32  LEU A CG  1 
ATOM   235  C  CD1 . LEU A 1 32  ? 13.859 -15.229 5.618   1.00 3.77  ? 32  LEU A CD1 1 
ATOM   236  C  CD2 . LEU A 1 32  ? 11.948 -16.485 4.610   1.00 5.08  ? 32  LEU A CD2 1 
ATOM   237  N  N   . ASP A 1 33  ? 13.417 -21.102 5.596   1.00 8.69  ? 33  ASP A N   1 
ATOM   238  C  CA  . ASP A 1 33  ? 14.052 -22.423 5.735   1.00 11.49 ? 33  ASP A CA  1 
ATOM   239  C  C   . ASP A 1 33  ? 13.802 -22.875 7.178   1.00 9.09  ? 33  ASP A C   1 
ATOM   240  O  O   . ASP A 1 33  ? 12.651 -22.816 7.633   1.00 9.61  ? 33  ASP A O   1 
ATOM   241  C  CB  . ASP A 1 33  ? 15.514 -22.339 5.304   1.00 10.73 ? 33  ASP A CB  1 
ATOM   242  C  CG  . ASP A 1 33  ? 15.664 -21.905 3.852   1.00 14.29 ? 33  ASP A CG  1 
ATOM   243  O  OD1 . ASP A 1 33  ? 14.842 -22.348 3.027   1.00 14.04 ? 33  ASP A OD1 1 
ATOM   244  O  OD2 . ASP A 1 33  ? 16.592 -21.125 3.534   1.00 13.18 ? 33  ASP A OD2 1 
ATOM   245  N  N   . ASP A 1 34  ? 14.810 -23.328 7.921   1.00 8.16  ? 34  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 34  ? 14.630 -23.804 9.295   1.00 8.49  ? 34  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 34  ? 15.170 -22.818 10.326  1.00 7.71  ? 34  ASP A C   1 
ATOM   248  O  O   . ASP A 1 34  ? 15.685 -23.233 11.376  1.00 8.35  ? 34  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 34  ? 15.277 -25.184 9.477   1.00 9.37  ? 34  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 34  ? 16.774 -25.195 9.148   1.00 14.14 ? 34  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 34  ? 17.326 -24.149 8.726   1.00 11.88 ? 34  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 34  ? 17.405 -26.265 9.297   1.00 21.10 ? 34  ASP A OD2 1 
ATOM   253  N  N   . VAL A 1 35  ? 15.043 -21.512 10.072  1.00 5.16  ? 35  VAL A N   1 
ATOM   254  C  CA  . VAL A 1 35  ? 15.534 -20.476 10.977  1.00 6.48  ? 35  VAL A CA  1 
ATOM   255  C  C   . VAL A 1 35  ? 14.456 -19.414 11.166  1.00 6.59  ? 35  VAL A C   1 
ATOM   256  O  O   . VAL A 1 35  ? 13.785 -19.013 10.206  1.00 4.86  ? 35  VAL A O   1 
ATOM   257  C  CB  . VAL A 1 35  ? 16.844 -19.841 10.464  1.00 3.46  ? 35  VAL A CB  1 
ATOM   258  C  CG1 . VAL A 1 35  ? 17.306 -18.733 11.418  1.00 5.68  ? 35  VAL A CG1 1 
ATOM   259  C  CG2 . VAL A 1 35  ? 17.935 -20.906 10.336  1.00 4.70  ? 35  VAL A CG2 1 
ATOM   260  N  N   . VAL A 1 36  ? 14.274 -18.975 12.413  1.00 4.27  ? 36  VAL A N   1 
ATOM   261  C  CA  . VAL A 1 36  ? 13.378 -17.866 12.730  1.00 6.26  ? 36  VAL A CA  1 
ATOM   262  C  C   . VAL A 1 36  ? 14.219 -16.702 13.251  1.00 6.34  ? 36  VAL A C   1 
ATOM   263  O  O   . VAL A 1 36  ? 15.092 -16.893 14.105  1.00 4.66  ? 36  VAL A O   1 
ATOM   264  C  CB  . VAL A 1 36  ? 12.290 -18.288 13.733  1.00 7.53  ? 36  VAL A CB  1 
ATOM   265  C  CG1 . VAL A 1 36  ? 11.435 -17.088 14.141  1.00 3.58  ? 36  VAL A CG1 1 
ATOM   266  C  CG2 . VAL A 1 36  ? 11.415 -19.414 13.130  1.00 5.82  ? 36  VAL A CG2 1 
ATOM   267  N  N   . TYR A 1 37  ? 13.969 -15.505 12.709  1.00 3.98  ? 37  TYR A N   1 
ATOM   268  C  CA  . TYR A 1 37  ? 14.706 -14.274 12.993  1.00 3.74  ? 37  TYR A CA  1 
ATOM   269  C  C   . TYR A 1 37  ? 13.773 -13.309 13.715  1.00 3.44  ? 37  TYR A C   1 
ATOM   270  O  O   . TYR A 1 37  ? 12.644 -13.100 13.278  1.00 4.56  ? 37  TYR A O   1 
ATOM   271  C  CB  . TYR A 1 37  ? 15.203 -13.615 11.690  1.00 6.49  ? 37  TYR A CB  1 
ATOM   272  C  CG  . TYR A 1 37  ? 16.069 -14.496 10.806  1.00 7.18  ? 37  TYR A CG  1 
ATOM   273  C  CD1 . TYR A 1 37  ? 15.504 -15.450 9.961   1.00 3.67  ? 37  TYR A CD1 1 
ATOM   274  C  CD2 . TYR A 1 37  ? 17.463 -14.362 10.811  1.00 5.91  ? 37  TYR A CD2 1 
ATOM   275  C  CE1 . TYR A 1 37  ? 16.301 -16.260 9.161   1.00 3.67  ? 37  TYR A CE1 1 
ATOM   276  C  CE2 . TYR A 1 37  ? 18.267 -15.164 10.002  1.00 4.64  ? 37  TYR A CE2 1 
ATOM   277  C  CZ  . TYR A 1 37  ? 17.676 -16.110 9.189   1.00 4.27  ? 37  TYR A CZ  1 
ATOM   278  O  OH  . TYR A 1 37  ? 18.480 -16.894 8.400   1.00 7.96  ? 37  TYR A OH  1 
ATOM   279  N  N   . CYS A 1 38  ? 14.239 -12.685 14.789  1.00 5.86  ? 38  CYS A N   1 
ATOM   280  C  CA  . CYS A 1 38  ? 13.408 -11.700 15.468  1.00 3.76  ? 38  CYS A CA  1 
ATOM   281  C  C   . CYS A 1 38  ? 14.318 -10.746 16.221  1.00 5.06  ? 38  CYS A C   1 
ATOM   282  O  O   . CYS A 1 38  ? 15.535 -10.987 16.330  1.00 4.86  ? 38  CYS A O   1 
ATOM   283  C  CB  . CYS A 1 38  ? 12.388 -12.374 16.409  1.00 3.77  ? 38  CYS A CB  1 
ATOM   284  S  SG  . CYS A 1 38  ? 13.069 -13.162 17.892  1.00 7.11  ? 38  CYS A SG  1 
ATOM   285  N  N   . PRO A 1 39  ? 13.778 -9.625  16.709  1.00 2.61  ? 39  PRO A N   1 
ATOM   286  C  CA  . PRO A 1 39  ? 14.611 -8.703  17.489  1.00 5.18  ? 39  PRO A CA  1 
ATOM   287  C  C   . PRO A 1 39  ? 15.046 -9.390  18.772  1.00 4.62  ? 39  PRO A C   1 
ATOM   288  O  O   . PRO A 1 39  ? 14.261 -10.090 19.413  1.00 1.27  ? 39  PRO A O   1 
ATOM   289  C  CB  . PRO A 1 39  ? 13.678 -7.514  17.772  1.00 5.14  ? 39  PRO A CB  1 
ATOM   290  C  CG  . PRO A 1 39  ? 12.490 -7.696  16.806  1.00 3.79  ? 39  PRO A CG  1 
ATOM   291  C  CD  . PRO A 1 39  ? 12.382 -9.161  16.583  1.00 3.69  ? 39  PRO A CD  1 
ATOM   292  N  N   . ARG A 1 40  ? 16.309 -9.193  19.136  1.00 4.29  ? 40  ARG A N   1 
ATOM   293  C  CA  . ARG A 1 40  ? 16.829 -9.850  20.330  1.00 5.46  ? 40  ARG A CA  1 
ATOM   294  C  C   . ARG A 1 40  ? 16.232 -9.271  21.607  1.00 4.83  ? 40  ARG A C   1 
ATOM   295  O  O   . ARG A 1 40  ? 16.303 -9.925  22.655  1.00 4.72  ? 40  ARG A O   1 
ATOM   296  C  CB  . ARG A 1 40  ? 18.356 -9.753  20.372  1.00 6.21  ? 40  ARG A CB  1 
ATOM   297  C  CG  . ARG A 1 40  ? 18.892 -8.339  20.564  1.00 3.85  ? 40  ARG A CG  1 
ATOM   298  C  CD  . ARG A 1 40  ? 20.398 -8.346  20.735  1.00 4.43  ? 40  ARG A CD  1 
ATOM   299  N  NE  . ARG A 1 40  ? 20.876 -6.987  20.902  1.00 6.58  ? 40  ARG A NE  1 
ATOM   300  C  CZ  . ARG A 1 40  ? 22.125 -6.660  21.185  1.00 7.50  ? 40  ARG A CZ  1 
ATOM   301  N  NH1 . ARG A 1 40  ? 23.069 -7.580  21.323  1.00 4.34  ? 40  ARG A NH1 1 
ATOM   302  N  NH2 . ARG A 1 40  ? 22.431 -5.377  21.354  1.00 9.04  ? 40  ARG A NH2 1 
ATOM   303  N  N   . HIS A 1 41  ? 15.605 -8.087  21.548  1.00 4.80  ? 41  HIS A N   1 
ATOM   304  C  CA  . HIS A 1 41  ? 14.978 -7.592  22.774  1.00 7.20  ? 41  HIS A CA  1 
ATOM   305  C  C   . HIS A 1 41  ? 13.764 -8.418  23.163  1.00 8.23  ? 41  HIS A C   1 
ATOM   306  O  O   . HIS A 1 41  ? 13.133 -8.129  24.192  1.00 12.08 ? 41  HIS A O   1 
ATOM   307  C  CB  . HIS A 1 41  ? 14.618 -6.094  22.668  1.00 7.81  ? 41  HIS A CB  1 
ATOM   308  C  CG  . HIS A 1 41  ? 13.515 -5.764  21.693  1.00 8.98  ? 41  HIS A CG  1 
ATOM   309  N  ND1 . HIS A 1 41  ? 13.738 -5.074  20.516  1.00 4.91  ? 41  HIS A ND1 1 
ATOM   310  C  CD2 . HIS A 1 41  ? 12.176 -5.966  21.756  1.00 9.49  ? 41  HIS A CD2 1 
ATOM   311  C  CE1 . HIS A 1 41  ? 12.589 -4.894  19.883  1.00 5.46  ? 41  HIS A CE1 1 
ATOM   312  N  NE2 . HIS A 1 41  ? 11.626 -5.427  20.613  1.00 8.28  ? 41  HIS A NE2 1 
ATOM   313  N  N   . VAL A 1 42  ? 13.447 -9.464  22.391  1.00 7.63  ? 42  VAL A N   1 
ATOM   314  C  CA  . VAL A 1 42  ? 12.416 -10.402 22.810  1.00 7.13  ? 42  VAL A CA  1 
ATOM   315  C  C   . VAL A 1 42  ? 12.747 -11.018 24.161  1.00 10.02 ? 42  VAL A C   1 
ATOM   316  O  O   . VAL A 1 42  ? 11.842 -11.487 24.862  1.00 14.40 ? 42  VAL A O   1 
ATOM   317  C  CB  . VAL A 1 42  ? 12.195 -11.504 21.743  1.00 7.11  ? 42  VAL A CB  1 
ATOM   318  C  CG1 . VAL A 1 42  ? 13.444 -12.351 21.555  1.00 7.07  ? 42  VAL A CG1 1 
ATOM   319  C  CG2 . VAL A 1 42  ? 11.005 -12.394 22.127  1.00 7.26  ? 42  VAL A CG2 1 
ATOM   320  N  N   . ILE A 1 43  ? 14.018 -11.004 24.568  1.00 9.48  ? 43  ILE A N   1 
ATOM   321  C  CA  . ILE A 1 43  ? 14.420 -11.663 25.811  1.00 9.33  ? 43  ILE A CA  1 
ATOM   322  C  C   . ILE A 1 43  ? 14.458 -10.696 26.997  1.00 16.16 ? 43  ILE A C   1 
ATOM   323  O  O   . ILE A 1 43  ? 14.910 -11.065 28.084  1.00 17.78 ? 43  ILE A O   1 
ATOM   324  C  CB  . ILE A 1 43  ? 15.785 -12.355 25.641  1.00 5.91  ? 43  ILE A CB  1 
ATOM   325  C  CG1 . ILE A 1 43  ? 16.898 -11.310 25.477  1.00 6.29  ? 43  ILE A CG1 1 
ATOM   326  C  CG2 . ILE A 1 43  ? 15.763 -13.340 24.464  1.00 9.73  ? 43  ILE A CG2 1 
ATOM   327  C  CD1 . ILE A 1 43  ? 18.288 -11.889 25.524  1.00 6.60  ? 43  ILE A CD1 1 
ATOM   328  N  N   . CYS A 1 44  ? 13.976 -9.469  26.819  1.00 17.06 ? 44  CYS A N   1 
ATOM   329  C  CA  . CYS A 1 44  ? 14.083 -8.430  27.838  1.00 19.71 ? 44  CYS A CA  1 
ATOM   330  C  C   . CYS A 1 44  ? 12.800 -8.278  28.643  1.00 22.70 ? 44  CYS A C   1 
ATOM   331  O  O   . CYS A 1 44  ? 11.700 -8.546  28.155  1.00 23.67 ? 44  CYS A O   1 
ATOM   332  C  CB  . CYS A 1 44  ? 14.411 -7.078  27.206  1.00 21.38 ? 44  CYS A CB  1 
ATOM   333  S  SG  . CYS A 1 44  ? 16.062 -6.921  26.559  1.00 18.93 ? 44  CYS A SG  1 
ATOM   334  N  N   . THR A 1 45  ? 12.955 -7.806  29.879  1.00 30.34 ? 45  THR A N   1 
ATOM   335  C  CA  . THR A 1 45  ? 11.849 -7.366  30.717  1.00 32.19 ? 45  THR A CA  1 
ATOM   336  C  C   . THR A 1 45  ? 11.795 -5.836  30.711  1.00 32.69 ? 45  THR A C   1 
ATOM   337  O  O   . THR A 1 45  ? 12.605 -5.169  30.065  1.00 30.26 ? 45  THR A O   1 
ATOM   338  C  CB  . THR A 1 45  ? 12.000 -7.911  32.138  1.00 28.45 ? 45  THR A CB  1 
ATOM   339  O  OG1 . THR A 1 45  ? 13.147 -7.308  32.748  1.00 31.57 ? 45  THR A OG1 1 
ATOM   340  C  CG2 . THR A 1 45  ? 12.191 -9.418  32.117  1.00 25.59 ? 45  THR A CG2 1 
ATOM   341  N  N   . SER A 1 46  ? 10.832 -5.270  31.447  1.00 33.57 ? 46  SER A N   1 
ATOM   342  C  CA  . SER A 1 46  ? 10.653 -3.819  31.457  1.00 32.15 ? 46  SER A CA  1 
ATOM   343  C  C   . SER A 1 46  ? 11.918 -3.132  31.953  1.00 34.02 ? 46  SER A C   1 
ATOM   344  O  O   . SER A 1 46  ? 12.535 -2.340  31.231  1.00 31.75 ? 46  SER A O   1 
ATOM   345  C  CB  . SER A 1 46  ? 9.466  -3.415  32.332  1.00 33.23 ? 46  SER A CB  1 
ATOM   346  O  OG  . SER A 1 46  ? 9.577  -3.997  33.623  1.00 44.43 ? 46  SER A OG  1 
ATOM   347  N  N   . GLU A 1 47  ? 12.304 -3.411  33.194  1.00 34.17 ? 47  GLU A N   1 
ATOM   348  C  CA  . GLU A 1 47  ? 13.616 -2.981  33.653  1.00 31.97 ? 47  GLU A CA  1 
ATOM   349  C  C   . GLU A 1 47  ? 14.675 -3.720  32.845  1.00 36.96 ? 47  GLU A C   1 
ATOM   350  O  O   . GLU A 1 47  ? 14.350 -4.610  32.049  1.00 33.12 ? 47  GLU A O   1 
ATOM   351  C  CB  . GLU A 1 47  ? 13.779 -3.238  35.150  1.00 35.04 ? 47  GLU A CB  1 
ATOM   352  N  N   . ASP A 1 48  ? 15.940 -3.364  33.030  1.00 35.22 ? 48  ASP A N   1 
ATOM   353  C  CA  . ASP A 1 48  ? 17.040 -3.863  32.212  1.00 33.84 ? 48  ASP A CA  1 
ATOM   354  C  C   . ASP A 1 48  ? 16.830 -3.592  30.719  1.00 30.38 ? 48  ASP A C   1 
ATOM   355  O  O   . ASP A 1 48  ? 17.632 -4.049  29.898  1.00 30.77 ? 48  ASP A O   1 
ATOM   356  C  CB  . ASP A 1 48  ? 17.334 -5.364  32.490  1.00 32.81 ? 48  ASP A CB  1 
ATOM   357  C  CG  . ASP A 1 48  ? 16.365 -6.359  31.775  1.00 37.39 ? 48  ASP A CG  1 
ATOM   358  O  OD1 . ASP A 1 48  ? 15.849 -6.082  30.659  1.00 30.71 ? 48  ASP A OD1 1 
ATOM   359  O  OD2 . ASP A 1 48  ? 16.128 -7.456  32.351  1.00 27.89 ? 48  ASP A OD2 1 
ATOM   360  N  N   . MET A 1 49  ? 15.784 -2.843  30.342  1.00 31.04 ? 49  MET A N   1 
ATOM   361  C  CA  . MET A 1 49  ? 15.707 -2.267  29.002  1.00 32.42 ? 49  MET A CA  1 
ATOM   362  C  C   . MET A 1 49  ? 16.440 -0.936  28.899  1.00 27.86 ? 49  MET A C   1 
ATOM   363  O  O   . MET A 1 49  ? 16.569 -0.400  27.792  1.00 24.99 ? 49  MET A O   1 
ATOM   364  C  CB  . MET A 1 49  ? 14.246 -2.086  28.559  1.00 32.99 ? 49  MET A CB  1 
ATOM   365  C  CG  . MET A 1 49  ? 13.659 -3.271  27.777  1.00 28.19 ? 49  MET A CG  1 
ATOM   366  S  SD  . MET A 1 49  ? 14.332 -3.499  26.110  1.00 40.51 ? 49  MET A SD  1 
ATOM   367  C  CE  . MET A 1 49  ? 12.857 -4.015  25.219  1.00 24.64 ? 49  MET A CE  1 
ATOM   368  N  N   . PHE A 1 50  ? 16.948 -0.409  30.015  1.00 26.60 ? 50  PHE A N   1 
ATOM   369  C  CA  . PHE A 1 50  ? 17.701 0.835   29.982  1.00 26.94 ? 50  PHE A CA  1 
ATOM   370  C  C   . PHE A 1 50  ? 19.195 0.630   29.807  1.00 30.99 ? 50  PHE A C   1 
ATOM   371  O  O   . PHE A 1 50  ? 19.866 1.526   29.274  1.00 31.76 ? 50  PHE A O   1 
ATOM   372  C  CB  . PHE A 1 50  ? 17.407 1.651   31.238  1.00 27.56 ? 50  PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 50  ? 16.064 2.296   31.185  1.00 32.52 ? 50  PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 50  ? 15.899 3.515   30.546  1.00 25.40 ? 50  PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 50  ? 14.951 1.645   31.696  1.00 31.48 ? 50  PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 50  ? 14.662 4.095   30.448  1.00 23.93 ? 50  PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 50  ? 13.706 2.222   31.615  1.00 31.56 ? 50  PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 50  ? 13.557 3.449   30.985  1.00 28.03 ? 50  PHE A CZ  1 
ATOM   379  N  N   . ASN A 1 51  ? 19.726 -0.528  30.207  1.00 25.25 ? 51  ASN A N   1 
ATOM   380  C  CA  . ASN A 1 51  ? 21.046 -0.970  29.754  1.00 26.57 ? 51  ASN A CA  1 
ATOM   381  C  C   . ASN A 1 51  ? 21.090 -2.489  29.765  1.00 26.35 ? 51  ASN A C   1 
ATOM   382  O  O   . ASN A 1 51  ? 21.812 -3.104  30.556  1.00 29.02 ? 51  ASN A O   1 
ATOM   383  C  CB  . ASN A 1 51  ? 22.158 -0.373  30.613  1.00 32.55 ? 51  ASN A CB  1 
ATOM   384  C  CG  . ASN A 1 51  ? 23.433 -0.125  29.818  1.00 38.10 ? 51  ASN A CG  1 
ATOM   385  O  OD1 . ASN A 1 51  ? 23.564 -0.560  28.667  1.00 31.71 ? 51  ASN A OD1 1 
ATOM   386  N  ND2 . ASN A 1 51  ? 24.376 0.585   30.426  1.00 38.20 ? 51  ASN A ND2 1 
ATOM   387  N  N   . PRO A 1 52  ? 20.330 -3.129  28.881  1.00 27.24 ? 52  PRO A N   1 
ATOM   388  C  CA  . PRO A 1 52  ? 20.303 -4.598  28.855  1.00 21.51 ? 52  PRO A CA  1 
ATOM   389  C  C   . PRO A 1 52  ? 21.678 -5.179  28.548  1.00 21.87 ? 52  PRO A C   1 
ATOM   390  O  O   . PRO A 1 52  ? 22.384 -4.726  27.640  1.00 18.37 ? 52  PRO A O   1 
ATOM   391  C  CB  . PRO A 1 52  ? 19.299 -4.922  27.740  1.00 21.40 ? 52  PRO A CB  1 
ATOM   392  C  CG  . PRO A 1 52  ? 18.999 -3.630  27.062  1.00 23.59 ? 52  PRO A CG  1 
ATOM   393  C  CD  . PRO A 1 52  ? 19.306 -2.531  28.012  1.00 23.93 ? 52  PRO A CD  1 
ATOM   394  N  N   . ASN A 1 53  ? 22.055 -6.198  29.309  1.00 15.55 ? 53  ASN A N   1 
ATOM   395  C  CA  . ASN A 1 53  ? 23.237 -6.988  28.979  1.00 16.06 ? 53  ASN A CA  1 
ATOM   396  C  C   . ASN A 1 53  ? 22.713 -8.209  28.229  1.00 13.21 ? 53  ASN A C   1 
ATOM   397  O  O   . ASN A 1 53  ? 22.375 -9.231  28.826  1.00 11.38 ? 53  ASN A O   1 
ATOM   398  C  CB  . ASN A 1 53  ? 24.034 -7.370  30.219  1.00 17.16 ? 53  ASN A CB  1 
ATOM   399  C  CG  . ASN A 1 53  ? 25.364 -7.978  29.869  1.00 22.02 ? 53  ASN A CG  1 
ATOM   400  O  OD1 . ASN A 1 53  ? 25.441 -8.876  29.019  1.00 19.56 ? 53  ASN A OD1 1 
ATOM   401  N  ND2 . ASN A 1 53  ? 26.425 -7.506  30.519  1.00 21.95 ? 53  ASN A ND2 1 
ATOM   402  N  N   . TYR A 1 54  ? 22.645 -8.089  26.899  1.00 11.47 ? 54  TYR A N   1 
ATOM   403  C  CA  . TYR A 1 54  ? 21.994 -9.117  26.095  1.00 11.57 ? 54  TYR A CA  1 
ATOM   404  C  C   . TYR A 1 54  ? 22.711 -10.456 26.188  1.00 9.35  ? 54  TYR A C   1 
ATOM   405  O  O   . TYR A 1 54  ? 22.059 -11.506 26.170  1.00 8.96  ? 54  TYR A O   1 
ATOM   406  C  CB  . TYR A 1 54  ? 21.887 -8.668  24.643  1.00 8.21  ? 54  TYR A CB  1 
ATOM   407  C  CG  . TYR A 1 54  ? 20.774 -7.655  24.414  1.00 10.83 ? 54  TYR A CG  1 
ATOM   408  C  CD1 . TYR A 1 54  ? 19.450 -8.053  24.309  1.00 6.69  ? 54  TYR A CD1 1 
ATOM   409  C  CD2 . TYR A 1 54  ? 21.058 -6.298  24.316  1.00 8.32  ? 54  TYR A CD2 1 
ATOM   410  C  CE1 . TYR A 1 54  ? 18.437 -7.120  24.097  1.00 8.25  ? 54  TYR A CE1 1 
ATOM   411  C  CE2 . TYR A 1 54  ? 20.058 -5.363  24.102  1.00 10.09 ? 54  TYR A CE2 1 
ATOM   412  C  CZ  . TYR A 1 54  ? 18.749 -5.783  23.999  1.00 7.30  ? 54  TYR A CZ  1 
ATOM   413  O  OH  . TYR A 1 54  ? 17.765 -4.853  23.786  1.00 10.29 ? 54  TYR A OH  1 
ATOM   414  N  N   . GLU A 1 55  ? 24.046 -10.454 26.269  1.00 11.69 ? 55  GLU A N   1 
ATOM   415  C  CA  . GLU A 1 55  ? 24.758 -11.713 26.481  1.00 15.50 ? 55  GLU A CA  1 
ATOM   416  C  C   . GLU A 1 55  ? 24.290 -12.394 27.766  1.00 13.30 ? 55  GLU A C   1 
ATOM   417  O  O   . GLU A 1 55  ? 23.889 -13.564 27.751  1.00 16.91 ? 55  GLU A O   1 
ATOM   418  C  CB  . GLU A 1 55  ? 26.274 -11.486 26.515  1.00 15.00 ? 55  GLU A CB  1 
ATOM   419  C  CG  . GLU A 1 55  ? 26.892 -11.165 25.160  1.00 13.60 ? 55  GLU A CG  1 
ATOM   420  C  CD  . GLU A 1 55  ? 26.572 -9.735  24.675  1.00 22.32 ? 55  GLU A CD  1 
ATOM   421  O  OE1 . GLU A 1 55  ? 26.093 -8.899  25.481  1.00 17.87 ? 55  GLU A OE1 1 
ATOM   422  O  OE2 . GLU A 1 55  ? 26.767 -9.457  23.466  1.00 25.79 ? 55  GLU A OE2 1 
ATOM   423  N  N   . ASP A 1 56  ? 24.312 -11.665 28.890  1.00 10.69 ? 56  ASP A N   1 
ATOM   424  C  CA  . ASP A 1 56  ? 23.926 -12.255 30.171  1.00 14.79 ? 56  ASP A CA  1 
ATOM   425  C  C   . ASP A 1 56  ? 22.457 -12.663 30.170  1.00 16.30 ? 56  ASP A C   1 
ATOM   426  O  O   . ASP A 1 56  ? 22.079 -13.660 30.791  1.00 14.05 ? 56  ASP A O   1 
ATOM   427  C  CB  . ASP A 1 56  ? 24.186 -11.272 31.319  1.00 14.70 ? 56  ASP A CB  1 
ATOM   428  C  CG  . ASP A 1 56  ? 25.662 -10.937 31.497  1.00 21.10 ? 56  ASP A CG  1 
ATOM   429  O  OD1 . ASP A 1 56  ? 25.970 -10.090 32.366  1.00 26.17 ? 56  ASP A OD1 1 
ATOM   430  O  OD2 . ASP A 1 56  ? 26.519 -11.505 30.783  1.00 21.09 ? 56  ASP A OD2 1 
ATOM   431  N  N   . LEU A 1 57  ? 21.611 -11.880 29.505  1.00 11.87 ? 57  LEU A N   1 
ATOM   432  C  CA  . LEU A 1 57  ? 20.197 -12.223 29.406  1.00 13.97 ? 57  LEU A CA  1 
ATOM   433  C  C   . LEU A 1 57  ? 19.999 -13.487 28.571  1.00 13.13 ? 57  LEU A C   1 
ATOM   434  O  O   . LEU A 1 57  ? 19.260 -14.398 28.961  1.00 14.10 ? 57  LEU A O   1 
ATOM   435  C  CB  . LEU A 1 57  ? 19.434 -11.039 28.809  1.00 9.29  ? 57  LEU A CB  1 
ATOM   436  C  CG  . LEU A 1 57  ? 19.304 -9.800  29.706  1.00 14.77 ? 57  LEU A CG  1 
ATOM   437  C  CD1 . LEU A 1 57  ? 18.695 -8.643  28.917  1.00 17.20 ? 57  LEU A CD1 1 
ATOM   438  C  CD2 . LEU A 1 57  ? 18.457 -10.068 30.942  1.00 18.89 ? 57  LEU A CD2 1 
ATOM   439  N  N   . LEU A 1 58  ? 20.679 -13.574 27.429  1.00 12.33 ? 58  LEU A N   1 
ATOM   440  C  CA  . LEU A 1 58  ? 20.512 -14.737 26.560  1.00 12.70 ? 58  LEU A CA  1 
ATOM   441  C  C   . LEU A 1 58  ? 21.030 -16.005 27.227  1.00 12.91 ? 58  LEU A C   1 
ATOM   442  O  O   . LEU A 1 58  ? 20.542 -17.106 26.945  1.00 10.25 ? 58  LEU A O   1 
ATOM   443  C  CB  . LEU A 1 58  ? 21.222 -14.488 25.230  1.00 9.57  ? 58  LEU A CB  1 
ATOM   444  C  CG  . LEU A 1 58  ? 21.059 -15.556 24.154  1.00 12.60 ? 58  LEU A CG  1 
ATOM   445  C  CD1 . LEU A 1 58  ? 19.586 -15.831 23.901  1.00 8.34  ? 58  LEU A CD1 1 
ATOM   446  C  CD2 . LEU A 1 58  ? 21.748 -15.056 22.893  1.00 9.95  ? 58  LEU A CD2 1 
ATOM   447  N  N   . ILE A 1 59  ? 21.997 -15.864 28.133  1.00 14.75 ? 59  ILE A N   1 
ATOM   448  C  CA  . ILE A 1 59  ? 22.549 -17.022 28.832  1.00 15.15 ? 59  ILE A CA  1 
ATOM   449  C  C   . ILE A 1 59  ? 21.531 -17.642 29.793  1.00 14.54 ? 59  ILE A C   1 
ATOM   450  O  O   . ILE A 1 59  ? 21.567 -18.852 30.049  1.00 16.33 ? 59  ILE A O   1 
ATOM   451  C  CB  . ILE A 1 59  ? 23.845 -16.600 29.548  1.00 13.30 ? 59  ILE A CB  1 
ATOM   452  C  CG1 . ILE A 1 59  ? 24.995 -16.571 28.522  1.00 14.43 ? 59  ILE A CG1 1 
ATOM   453  C  CG2 . ILE A 1 59  ? 24.117 -17.523 30.741  1.00 16.46 ? 59  ILE A CG2 1 
ATOM   454  C  CD1 . ILE A 1 59  ? 26.186 -15.681 28.875  1.00 11.56 ? 59  ILE A CD1 1 
ATOM   455  N  N   . ARG A 1 60  ? 20.618 -16.850 30.350  1.00 15.51 ? 60  ARG A N   1 
ATOM   456  C  CA  . ARG A 1 60  ? 19.607 -17.474 31.202  1.00 16.12 ? 60  ARG A CA  1 
ATOM   457  C  C   . ARG A 1 60  ? 18.539 -18.243 30.423  1.00 15.54 ? 60  ARG A C   1 
ATOM   458  O  O   . ARG A 1 60  ? 17.657 -18.827 31.061  1.00 16.85 ? 60  ARG A O   1 
ATOM   459  C  CB  . ARG A 1 60  ? 18.933 -16.421 32.093  1.00 17.85 ? 60  ARG A CB  1 
ATOM   460  C  CG  . ARG A 1 60  ? 19.860 -15.749 33.108  1.00 22.57 ? 60  ARG A CG  1 
ATOM   461  C  CD  . ARG A 1 60  ? 19.626 -14.253 33.202  1.00 25.90 ? 60  ARG A CD  1 
ATOM   462  N  NE  . ARG A 1 60  ? 18.211 -13.913 33.293  1.00 34.28 ? 60  ARG A NE  1 
ATOM   463  C  CZ  . ARG A 1 60  ? 17.747 -12.750 33.733  1.00 42.83 ? 60  ARG A CZ  1 
ATOM   464  N  NH1 . ARG A 1 60  ? 18.563 -11.791 34.140  1.00 42.86 ? 60  ARG A NH1 1 
ATOM   465  N  NH2 . ARG A 1 60  ? 16.432 -12.542 33.758  1.00 45.04 ? 60  ARG A NH2 1 
ATOM   466  N  N   . LYS A 1 61  ? 18.575 -18.264 29.090  1.00 11.95 ? 61  LYS A N   1 
ATOM   467  C  CA  . LYS A 1 61  ? 17.511 -18.845 28.278  1.00 15.39 ? 61  LYS A CA  1 
ATOM   468  C  C   . LYS A 1 61  ? 17.948 -20.167 27.662  1.00 14.41 ? 61  LYS A C   1 
ATOM   469  O  O   . LYS A 1 61  ? 19.114 -20.339 27.299  1.00 12.98 ? 61  LYS A O   1 
ATOM   470  C  CB  . LYS A 1 61  ? 17.094 -17.889 27.148  1.00 17.07 ? 61  LYS A CB  1 
ATOM   471  C  CG  . LYS A 1 61  ? 16.524 -16.552 27.616  1.00 16.89 ? 61  LYS A CG  1 
ATOM   472  C  CD  . LYS A 1 61  ? 15.331 -16.732 28.536  1.00 15.10 ? 61  LYS A CD  1 
ATOM   473  C  CE  . LYS A 1 61  ? 14.779 -15.372 28.932  1.00 19.50 ? 61  LYS A CE  1 
ATOM   474  N  NZ  . LYS A 1 61  ? 13.787 -15.451 30.028  1.00 22.32 ? 61  LYS A NZ  1 
ATOM   475  N  N   . SER A 1 62  ? 16.990 -21.090 27.520  1.00 16.67 ? 62  SER A N   1 
ATOM   476  C  CA  . SER A 1 62  ? 17.178 -22.381 26.861  1.00 15.69 ? 62  SER A CA  1 
ATOM   477  C  C   . SER A 1 62  ? 16.316 -22.467 25.602  1.00 12.76 ? 62  SER A C   1 
ATOM   478  O  O   . SER A 1 62  ? 15.405 -21.665 25.391  1.00 9.70  ? 62  SER A O   1 
ATOM   479  C  CB  . SER A 1 62  ? 16.838 -23.543 27.805  1.00 18.14 ? 62  SER A CB  1 
ATOM   480  O  OG  . SER A 1 62  ? 17.827 -23.695 28.816  1.00 26.45 ? 62  SER A OG  1 
ATOM   481  N  N   . ASN A 1 63  ? 16.615 -23.461 24.749  1.00 14.21 ? 63  ASN A N   1 
ATOM   482  C  CA  . ASN A 1 63  ? 15.815 -23.649 23.540  1.00 12.25 ? 63  ASN A CA  1 
ATOM   483  C  C   . ASN A 1 63  ? 14.327 -23.646 23.856  1.00 17.50 ? 63  ASN A C   1 
ATOM   484  O  O   . ASN A 1 63  ? 13.529 -23.020 23.140  1.00 14.21 ? 63  ASN A O   1 
ATOM   485  C  CB  . ASN A 1 63  ? 16.192 -24.953 22.839  1.00 12.66 ? 63  ASN A CB  1 
ATOM   486  C  CG  . ASN A 1 63  ? 17.515 -24.859 22.115  1.00 15.56 ? 63  ASN A CG  1 
ATOM   487  O  OD1 . ASN A 1 63  ? 18.045 -23.763 21.918  1.00 15.79 ? 63  ASN A OD1 1 
ATOM   488  N  ND2 . ASN A 1 63  ? 18.061 -26.005 21.715  1.00 11.40 ? 63  ASN A ND2 1 
ATOM   489  N  N   . HIS A 1 64  ? 13.938 -24.331 24.941  1.00 13.28 ? 64  HIS A N   1 
ATOM   490  C  CA  . HIS A 1 64  ? 12.535 -24.493 25.293  1.00 14.43 ? 64  HIS A CA  1 
ATOM   491  C  C   . HIS A 1 64  ? 11.900 -23.240 25.883  1.00 12.88 ? 64  HIS A C   1 
ATOM   492  O  O   . HIS A 1 64  ? 10.680 -23.217 26.050  1.00 13.95 ? 64  HIS A O   1 
ATOM   493  C  CB  . HIS A 1 64  ? 12.358 -25.660 26.273  1.00 15.23 ? 64  HIS A CB  1 
ATOM   494  C  CG  . HIS A 1 64  ? 12.891 -25.392 27.648  1.00 12.83 ? 64  HIS A CG  1 
ATOM   495  N  ND1 . HIS A 1 64  ? 14.058 -25.956 28.114  1.00 15.12 ? 64  HIS A ND1 1 
ATOM   496  C  CD2 . HIS A 1 64  ? 12.421 -24.616 28.654  1.00 13.97 ? 64  HIS A CD2 1 
ATOM   497  C  CE1 . HIS A 1 64  ? 14.278 -25.554 29.355  1.00 13.96 ? 64  HIS A CE1 1 
ATOM   498  N  NE2 . HIS A 1 64  ? 13.304 -24.732 29.704  1.00 14.06 ? 64  HIS A NE2 1 
ATOM   499  N  N   . ASN A 1 65  ? 12.670 -22.200 26.197  1.00 11.13 ? 65  ASN A N   1 
ATOM   500  C  CA  . ASN A 1 65  ? 12.037 -20.956 26.612  1.00 12.91 ? 65  ASN A CA  1 
ATOM   501  C  C   . ASN A 1 65  ? 11.547 -20.108 25.439  1.00 12.86 ? 65  ASN A C   1 
ATOM   502  O  O   . ASN A 1 65  ? 10.866 -19.101 25.660  1.00 11.20 ? 65  ASN A O   1 
ATOM   503  C  CB  . ASN A 1 65  ? 12.997 -20.131 27.461  1.00 12.63 ? 65  ASN A CB  1 
ATOM   504  C  CG  . ASN A 1 65  ? 13.460 -20.874 28.710  1.00 17.66 ? 65  ASN A CG  1 
ATOM   505  O  OD1 . ASN A 1 65  ? 14.656 -21.098 28.900  1.00 17.32 ? 65  ASN A OD1 1 
ATOM   506  N  ND2 . ASN A 1 65  ? 12.507 -21.274 29.558  1.00 12.61 ? 65  ASN A ND2 1 
ATOM   507  N  N   . PHE A 1 66  ? 11.859 -20.472 24.205  1.00 13.24 ? 66  PHE A N   1 
ATOM   508  C  CA  . PHE A 1 66  ? 11.439 -19.684 23.049  1.00 15.58 ? 66  PHE A CA  1 
ATOM   509  C  C   . PHE A 1 66  ? 10.276 -20.414 22.391  1.00 14.20 ? 66  PHE A C   1 
ATOM   510  O  O   . PHE A 1 66  ? 10.474 -21.468 21.782  1.00 16.51 ? 66  PHE A O   1 
ATOM   511  C  CB  . PHE A 1 66  ? 12.589 -19.494 22.062  1.00 13.84 ? 66  PHE A CB  1 
ATOM   512  C  CG  . PHE A 1 66  ? 13.703 -18.614 22.569  1.00 11.21 ? 66  PHE A CG  1 
ATOM   513  C  CD1 . PHE A 1 66  ? 13.590 -17.236 22.531  1.00 10.67 ? 66  PHE A CD1 1 
ATOM   514  C  CD2 . PHE A 1 66  ? 14.873 -19.169 23.054  1.00 10.51 ? 66  PHE A CD2 1 
ATOM   515  C  CE1 . PHE A 1 66  ? 14.613 -16.427 22.972  1.00 10.89 ? 66  PHE A CE1 1 
ATOM   516  C  CE2 . PHE A 1 66  ? 15.893 -18.362 23.504  1.00 11.54 ? 66  PHE A CE2 1 
ATOM   517  C  CZ  . PHE A 1 66  ? 15.761 -16.982 23.465  1.00 6.84  ? 66  PHE A CZ  1 
ATOM   518  N  N   . LEU A 1 67  ? 9.071  -19.857 22.500  1.00 10.56 ? 67  LEU A N   1 
ATOM   519  C  CA  . LEU A 1 67  ? 7.883  -20.465 21.911  1.00 13.18 ? 67  LEU A CA  1 
ATOM   520  C  C   . LEU A 1 67  ? 7.632  -19.815 20.552  1.00 14.44 ? 67  LEU A C   1 
ATOM   521  O  O   . LEU A 1 67  ? 7.330  -18.616 20.483  1.00 11.32 ? 67  LEU A O   1 
ATOM   522  C  CB  . LEU A 1 67  ? 6.661  -20.302 22.814  1.00 14.55 ? 67  LEU A CB  1 
ATOM   523  C  CG  . LEU A 1 67  ? 6.510  -21.036 24.152  1.00 12.26 ? 67  LEU A CG  1 
ATOM   524  C  CD1 . LEU A 1 67  ? 7.209  -22.404 24.126  1.00 15.52 ? 67  LEU A CD1 1 
ATOM   525  C  CD2 . LEU A 1 67  ? 6.936  -20.180 25.339  1.00 18.85 ? 67  LEU A CD2 1 
ATOM   526  N  N   . VAL A 1 68  ? 7.748  -20.605 19.481  1.00 10.62 ? 68  VAL A N   1 
ATOM   527  C  CA  . VAL A 1 68  ? 7.481  -20.145 18.121  1.00 10.81 ? 68  VAL A CA  1 
ATOM   528  C  C   . VAL A 1 68  ? 6.197  -20.813 17.631  1.00 14.29 ? 68  VAL A C   1 
ATOM   529  O  O   . VAL A 1 68  ? 6.104  -22.048 17.604  1.00 12.93 ? 68  VAL A O   1 
ATOM   530  C  CB  . VAL A 1 68  ? 8.664  -20.421 17.176  1.00 14.97 ? 68  VAL A CB  1 
ATOM   531  C  CG1 . VAL A 1 68  ? 8.373  -19.863 15.772  1.00 11.04 ? 68  VAL A CG1 1 
ATOM   532  C  CG2 . VAL A 1 68  ? 9.958  -19.795 17.735  1.00 11.41 ? 68  VAL A CG2 1 
ATOM   533  N  N   . GLN A 1 69  ? 5.202  -19.982 17.276  1.00 13.23 ? 69  GLN A N   1 
ATOM   534  C  CA  . GLN A 1 69  ? 3.916  -20.399 16.719  1.00 20.21 ? 69  GLN A CA  1 
ATOM   535  C  C   . GLN A 1 69  ? 3.718  -19.827 15.321  1.00 19.24 ? 69  GLN A C   1 
ATOM   536  O  O   . GLN A 1 69  ? 3.783  -18.609 15.129  1.00 12.91 ? 69  GLN A O   1 
ATOM   537  C  CB  . GLN A 1 69  ? 2.740  -19.923 17.575  1.00 16.99 ? 69  GLN A CB  1 
ATOM   538  C  CG  . GLN A 1 69  ? 2.175  -20.933 18.520  1.00 28.26 ? 69  GLN A CG  1 
ATOM   539  C  CD  . GLN A 1 69  ? 1.375  -20.285 19.636  1.00 26.19 ? 69  GLN A CD  1 
ATOM   540  O  OE1 . GLN A 1 69  ? 0.225  -19.893 19.436  1.00 27.99 ? 69  GLN A OE1 1 
ATOM   541  N  NE2 . GLN A 1 69  ? 1.977  -20.185 20.826  1.00 34.40 ? 69  GLN A NE2 1 
ATOM   542  N  N   . ALA A 1 70  ? 3.403  -20.695 14.369  1.00 20.14 ? 70  ALA A N   1 
ATOM   543  C  CA  . ALA A 1 70  ? 2.992  -20.289 13.028  1.00 26.83 ? 70  ALA A CA  1 
ATOM   544  C  C   . ALA A 1 70  ? 1.538  -20.738 12.865  1.00 32.60 ? 70  ALA A C   1 
ATOM   545  O  O   . ALA A 1 70  ? 1.267  -21.925 12.647  1.00 26.41 ? 70  ALA A O   1 
ATOM   546  C  CB  . ALA A 1 70  ? 3.921  -20.887 11.967  1.00 21.32 ? 70  ALA A CB  1 
ATOM   547  N  N   . GLY A 1 71  ? 0.604  -19.793 12.994  1.00 34.17 ? 71  GLY A N   1 
ATOM   548  C  CA  . GLY A 1 71  ? -0.812 -20.112 13.047  1.00 31.88 ? 71  GLY A CA  1 
ATOM   549  C  C   . GLY A 1 71  ? -1.147 -20.786 14.357  1.00 33.72 ? 71  GLY A C   1 
ATOM   550  O  O   . GLY A 1 71  ? -1.157 -20.145 15.412  1.00 44.34 ? 71  GLY A O   1 
ATOM   551  N  N   . ASN A 1 72  ? -1.427 -22.084 14.304  1.00 36.44 ? 72  ASN A N   1 
ATOM   552  C  CA  . ASN A 1 72  ? -1.409 -22.925 15.490  1.00 43.56 ? 72  ASN A CA  1 
ATOM   553  C  C   . ASN A 1 72  ? -0.344 -24.011 15.422  1.00 44.23 ? 72  ASN A C   1 
ATOM   554  O  O   . ASN A 1 72  ? -0.168 -24.743 16.403  1.00 45.08 ? 72  ASN A O   1 
ATOM   555  C  CB  . ASN A 1 72  ? -2.785 -23.567 15.728  1.00 54.87 ? 72  ASN A CB  1 
ATOM   556  C  CG  . ASN A 1 72  ? -3.656 -22.752 16.679  1.00 58.68 ? 72  ASN A CG  1 
ATOM   557  O  OD1 . ASN A 1 72  ? -4.150 -23.267 17.683  1.00 48.29 ? 72  ASN A OD1 1 
ATOM   558  N  ND2 . ASN A 1 72  ? -3.846 -21.473 16.364  1.00 62.16 ? 72  ASN A ND2 1 
ATOM   559  N  N   . VAL A 1 73  ? 0.365  -24.133 14.296  1.00 37.01 ? 73  VAL A N   1 
ATOM   560  C  CA  . VAL A 1 73  ? 1.547  -24.984 14.226  1.00 33.79 ? 73  VAL A CA  1 
ATOM   561  C  C   . VAL A 1 73  ? 2.576  -24.489 15.234  1.00 30.60 ? 73  VAL A C   1 
ATOM   562  O  O   . VAL A 1 73  ? 3.036  -23.344 15.164  1.00 22.43 ? 73  VAL A O   1 
ATOM   563  C  CB  . VAL A 1 73  ? 2.128  -24.984 12.809  1.00 35.74 ? 73  VAL A CB  1 
ATOM   564  C  CG1 . VAL A 1 73  ? 3.490  -25.656 12.790  1.00 29.55 ? 73  VAL A CG1 1 
ATOM   565  C  CG2 . VAL A 1 73  ? 1.172  -25.656 11.830  1.00 42.35 ? 73  VAL A CG2 1 
ATOM   566  N  N   . GLN A 1 74  ? 2.951  -25.351 16.169  1.00 31.67 ? 74  GLN A N   1 
ATOM   567  C  CA  . GLN A 1 74  ? 3.991  -25.043 17.139  1.00 22.19 ? 74  GLN A CA  1 
ATOM   568  C  C   . GLN A 1 74  ? 5.311  -25.617 16.633  1.00 18.61 ? 74  GLN A C   1 
ATOM   569  O  O   . GLN A 1 74  ? 5.402  -26.817 16.363  1.00 23.47 ? 74  GLN A O   1 
ATOM   570  C  CB  . GLN A 1 74  ? 3.623  -25.605 18.512  1.00 22.99 ? 74  GLN A CB  1 
ATOM   571  C  CG  . GLN A 1 74  ? 4.404  -24.991 19.667  1.00 26.97 ? 74  GLN A CG  1 
ATOM   572  C  CD  . GLN A 1 74  ? 3.901  -23.607 20.051  1.00 24.11 ? 74  GLN A CD  1 
ATOM   573  O  OE1 . GLN A 1 74  ? 2.701  -23.327 20.007  1.00 23.81 ? 74  GLN A OE1 1 
ATOM   574  N  NE2 . GLN A 1 74  ? 4.820  -22.737 20.436  1.00 20.56 ? 74  GLN A NE2 1 
ATOM   575  N  N   . LEU A 1 75  ? 6.321  -24.763 16.487  1.00 15.60 ? 75  LEU A N   1 
ATOM   576  C  CA  . LEU A 1 75  ? 7.634  -25.192 16.024  1.00 14.36 ? 75  LEU A CA  1 
ATOM   577  C  C   . LEU A 1 75  ? 8.495  -25.635 17.197  1.00 13.39 ? 75  LEU A C   1 
ATOM   578  O  O   . LEU A 1 75  ? 8.410  -25.093 18.300  1.00 17.74 ? 75  LEU A O   1 
ATOM   579  C  CB  . LEU A 1 75  ? 8.345  -24.071 15.257  1.00 16.05 ? 75  LEU A CB  1 
ATOM   580  C  CG  . LEU A 1 75  ? 7.611  -23.535 14.021  1.00 15.20 ? 75  LEU A CG  1 
ATOM   581  C  CD1 . LEU A 1 75  ? 8.511  -22.638 13.183  1.00 11.93 ? 75  LEU A CD1 1 
ATOM   582  C  CD2 . LEU A 1 75  ? 7.090  -24.699 13.203  1.00 17.42 ? 75  LEU A CD2 1 
ATOM   583  N  N   . ARG A 1 76  ? 9.342  -26.622 16.945  1.00 13.93 ? 76  ARG A N   1 
ATOM   584  C  CA  . ARG A 1 76  ? 10.227 -27.170 17.959  1.00 13.37 ? 76  ARG A CA  1 
ATOM   585  C  C   . ARG A 1 76  ? 11.591 -26.515 17.777  1.00 14.00 ? 76  ARG A C   1 
ATOM   586  O  O   . ARG A 1 76  ? 12.181 -26.600 16.696  1.00 11.54 ? 76  ARG A O   1 
ATOM   587  C  CB  . ARG A 1 76  ? 10.311 -28.693 17.834  1.00 13.07 ? 76  ARG A CB  1 
ATOM   588  C  CG  . ARG A 1 76  ? 11.214 -29.371 18.864  1.00 16.57 ? 76  ARG A CG  1 
ATOM   589  C  CD  . ARG A 1 76  ? 11.297 -30.893 18.662  1.00 15.42 ? 76  ARG A CD  1 
ATOM   590  N  NE  . ARG A 1 76  ? 10.001 -31.539 18.861  1.00 13.72 ? 76  ARG A NE  1 
ATOM   591  C  CZ  . ARG A 1 76  ? 9.414  -31.721 20.037  1.00 15.54 ? 76  ARG A CZ  1 
ATOM   592  N  NH1 . ARG A 1 76  ? 10.003 -31.364 21.170  1.00 12.02 ? 76  ARG A NH1 1 
ATOM   593  N  NH2 . ARG A 1 76  ? 8.214  -32.297 20.081  1.00 16.86 ? 76  ARG A NH2 1 
ATOM   594  N  N   . VAL A 1 77  ? 12.077 -25.846 18.822  1.00 17.97 ? 77  VAL A N   1 
ATOM   595  C  CA  . VAL A 1 77  ? 13.311 -25.070 18.751  1.00 10.47 ? 77  VAL A CA  1 
ATOM   596  C  C   . VAL A 1 77  ? 14.482 -25.969 19.129  1.00 11.59 ? 77  VAL A C   1 
ATOM   597  O  O   . VAL A 1 77  ? 14.503 -26.550 20.218  1.00 16.68 ? 77  VAL A O   1 
ATOM   598  C  CB  . VAL A 1 77  ? 13.248 -23.835 19.664  1.00 11.93 ? 77  VAL A CB  1 
ATOM   599  C  CG1 . VAL A 1 77  ? 14.589 -23.076 19.623  1.00 8.32  ? 77  VAL A CG1 1 
ATOM   600  C  CG2 . VAL A 1 77  ? 12.075 -22.913 19.272  1.00 15.03 ? 77  VAL A CG2 1 
ATOM   601  N  N   . ILE A 1 78  ? 15.478 -26.052 18.249  1.00 13.31 ? 78  ILE A N   1 
ATOM   602  C  CA  . ILE A 1 78  ? 16.620 -26.939 18.426  1.00 11.25 ? 78  ILE A CA  1 
ATOM   603  C  C   . ILE A 1 78  ? 17.938 -26.183 18.514  1.00 14.41 ? 78  ILE A C   1 
ATOM   604  O  O   . ILE A 1 78  ? 18.992 -26.813 18.606  1.00 14.63 ? 78  ILE A O   1 
ATOM   605  C  CB  . ILE A 1 78  ? 16.680 -27.993 17.301  1.00 10.93 ? 78  ILE A CB  1 
ATOM   606  C  CG1 . ILE A 1 78  ? 16.932 -27.322 15.943  1.00 17.02 ? 78  ILE A CG1 1 
ATOM   607  C  CG2 . ILE A 1 78  ? 15.371 -28.720 17.205  1.00 10.71 ? 78  ILE A CG2 1 
ATOM   608  C  CD1 . ILE A 1 78  ? 17.160 -28.322 14.782  1.00 14.37 ? 78  ILE A CD1 1 
ATOM   609  N  N   . GLY A 1 79  ? 17.914 -24.857 18.499  1.00 11.32 ? 79  GLY A N   1 
ATOM   610  C  CA  . GLY A 1 79  ? 19.141 -24.089 18.626  1.00 12.65 ? 79  GLY A CA  1 
ATOM   611  C  C   . GLY A 1 79  ? 18.811 -22.616 18.695  1.00 11.95 ? 79  GLY A C   1 
ATOM   612  O  O   . GLY A 1 79  ? 17.733 -22.177 18.276  1.00 12.14 ? 79  GLY A O   1 
ATOM   613  N  N   . HIS A 1 80  ? 19.749 -21.855 19.249  1.00 7.68  ? 80  HIS A N   1 
ATOM   614  C  CA  . HIS A 1 80  ? 19.537 -20.413 19.306  1.00 12.59 ? 80  HIS A CA  1 
ATOM   615  C  C   . HIS A 1 80  ? 20.872 -19.686 19.394  1.00 12.48 ? 80  HIS A C   1 
ATOM   616  O  O   . HIS A 1 80  ? 21.782 -20.116 20.109  1.00 11.08 ? 80  HIS A O   1 
ATOM   617  C  CB  . HIS A 1 80  ? 18.625 -20.023 20.477  1.00 7.56  ? 80  HIS A CB  1 
ATOM   618  C  CG  . HIS A 1 80  ? 19.260 -20.182 21.821  1.00 10.80 ? 80  HIS A CG  1 
ATOM   619  N  ND1 . HIS A 1 80  ? 19.240 -21.372 22.519  1.00 12.28 ? 80  HIS A ND1 1 
ATOM   620  C  CD2 . HIS A 1 80  ? 19.949 -19.303 22.592  1.00 11.84 ? 80  HIS A CD2 1 
ATOM   621  C  CE1 . HIS A 1 80  ? 19.874 -21.214 23.670  1.00 13.73 ? 80  HIS A CE1 1 
ATOM   622  N  NE2 . HIS A 1 80  ? 20.315 -19.967 23.738  1.00 12.52 ? 80  HIS A NE2 1 
ATOM   623  N  N   . SER A 1 81  ? 20.988 -18.597 18.635  1.00 12.28 ? 81  SER A N   1 
ATOM   624  C  CA  . SER A 1 81  ? 22.189 -17.775 18.621  1.00 9.53  ? 81  SER A CA  1 
ATOM   625  C  C   . SER A 1 81  ? 21.759 -16.324 18.481  1.00 12.19 ? 81  SER A C   1 
ATOM   626  O  O   . SER A 1 81  ? 20.609 -16.021 18.155  1.00 7.49  ? 81  SER A O   1 
ATOM   627  C  CB  . SER A 1 81  ? 23.159 -18.175 17.496  1.00 7.53  ? 81  SER A CB  1 
ATOM   628  O  OG  . SER A 1 81  ? 22.508 -18.264 16.227  1.00 12.65 ? 81  SER A OG  1 
ATOM   629  N  N   . MET A 1 82  ? 22.685 -15.418 18.754  1.00 6.57  ? 82  MET A N   1 
ATOM   630  C  CA  . MET A 1 82  ? 22.443 -13.998 18.600  1.00 9.01  ? 82  MET A CA  1 
ATOM   631  C  C   . MET A 1 82  ? 23.461 -13.465 17.608  1.00 13.09 ? 82  MET A C   1 
ATOM   632  O  O   . MET A 1 82  ? 24.646 -13.810 17.692  1.00 11.40 ? 82  MET A O   1 
ATOM   633  C  CB  . MET A 1 82  ? 22.532 -13.302 19.965  1.00 11.37 ? 82  MET A CB  1 
ATOM   634  C  CG  . MET A 1 82  ? 22.273 -11.826 19.967  1.00 10.52 ? 82  MET A CG  1 
ATOM   635  S  SD  . MET A 1 82  ? 22.299 -11.131 21.641  1.00 10.56 ? 82  MET A SD  1 
ATOM   636  C  CE  . MET A 1 82  ? 23.891 -11.688 22.279  1.00 14.62 ? 82  MET A CE  1 
ATOM   637  N  N   . GLN A 1 83  ? 22.991 -12.691 16.627  1.00 7.57  ? 83  GLN A N   1 
ATOM   638  C  CA  . GLN A 1 83  ? 23.868 -12.062 15.643  1.00 8.23  ? 83  GLN A CA  1 
ATOM   639  C  C   . GLN A 1 83  ? 23.564 -10.574 15.663  1.00 5.93  ? 83  GLN A C   1 
ATOM   640  O  O   . GLN A 1 83  ? 22.472 -10.158 15.263  1.00 4.73  ? 83  GLN A O   1 
ATOM   641  C  CB  . GLN A 1 83  ? 23.658 -12.643 14.241  1.00 5.79  ? 83  GLN A CB  1 
ATOM   642  C  CG  . GLN A 1 83  ? 24.308 -11.807 13.142  1.00 4.76  ? 83  GLN A CG  1 
ATOM   643  C  CD  . GLN A 1 83  ? 24.323 -12.496 11.787  1.00 11.21 ? 83  GLN A CD  1 
ATOM   644  O  OE1 . GLN A 1 83  ? 23.413 -13.253 11.455  1.00 10.60 ? 83  GLN A OE1 1 
ATOM   645  N  NE2 . GLN A 1 83  ? 25.350 -12.218 10.987  1.00 10.85 ? 83  GLN A NE2 1 
ATOM   646  N  N   . ASN A 1 84  ? 24.514 -9.774  16.134  1.00 9.50  ? 84  ASN A N   1 
ATOM   647  C  CA  . ASN A 1 84  ? 24.258 -8.351  16.279  1.00 6.22  ? 84  ASN A CA  1 
ATOM   648  C  C   . ASN A 1 84  ? 22.978 -8.141  17.085  1.00 5.89  ? 84  ASN A C   1 
ATOM   649  O  O   . ASN A 1 84  ? 22.884 -8.648  18.204  1.00 6.27  ? 84  ASN A O   1 
ATOM   650  C  CB  . ASN A 1 84  ? 24.221 -7.713  14.893  1.00 8.98  ? 84  ASN A CB  1 
ATOM   651  C  CG  . ASN A 1 84  ? 25.556 -7.873  14.156  1.00 9.41  ? 84  ASN A CG  1 
ATOM   652  O  OD1 . ASN A 1 84  ? 26.604 -7.563  14.710  1.00 12.70 ? 84  ASN A OD1 1 
ATOM   653  N  ND2 . ASN A 1 84  ? 25.518 -8.335  12.911  1.00 8.63  ? 84  ASN A ND2 1 
ATOM   654  N  N   . CYS A 1 85  ? 21.972 -7.426  16.571  1.00 5.08  ? 85  CYS A N   1 
ATOM   655  C  CA  . CYS A 1 85  ? 20.753 -7.210  17.357  1.00 4.58  ? 85  CYS A CA  1 
ATOM   656  C  C   . CYS A 1 85  ? 19.606 -8.142  16.968  1.00 5.52  ? 85  CYS A C   1 
ATOM   657  O  O   . CYS A 1 85  ? 18.441 -7.823  17.219  1.00 6.62  ? 85  CYS A O   1 
ATOM   658  C  CB  . CYS A 1 85  ? 20.309 -5.754  17.261  1.00 5.40  ? 85  CYS A CB  1 
ATOM   659  S  SG  . CYS A 1 85  ? 21.621 -4.658  17.792  1.00 5.15  ? 85  CYS A SG  1 
ATOM   660  N  N   . VAL A 1 86  ? 19.906 -9.282  16.369  1.00 4.20  ? 86  VAL A N   1 
ATOM   661  C  CA  . VAL A 1 86  ? 18.897 -10.231 15.936  1.00 4.51  ? 86  VAL A CA  1 
ATOM   662  C  C   . VAL A 1 86  ? 19.136 -11.553 16.652  1.00 7.92  ? 86  VAL A C   1 
ATOM   663  O  O   . VAL A 1 86  ? 20.285 -11.994 16.802  1.00 5.48  ? 86  VAL A O   1 
ATOM   664  C  CB  . VAL A 1 86  ? 18.946 -10.407 14.404  1.00 5.94  ? 86  VAL A CB  1 
ATOM   665  C  CG1 . VAL A 1 86  ? 18.762 -11.845 14.035  1.00 9.69  ? 86  VAL A CG1 1 
ATOM   666  C  CG2 . VAL A 1 86  ? 17.899 -9.511  13.713  1.00 2.69  ? 86  VAL A CG2 1 
ATOM   667  N  N   . LEU A 1 87  ? 18.048 -12.180 17.086  1.00 3.96  ? 87  LEU A N   1 
ATOM   668  C  CA  . LEU A 1 87  ? 18.069 -13.556 17.570  1.00 7.22  ? 87  LEU A CA  1 
ATOM   669  C  C   . LEU A 1 87  ? 17.741 -14.519 16.431  1.00 8.21  ? 87  LEU A C   1 
ATOM   670  O  O   . LEU A 1 87  ? 16.780 -14.306 15.693  1.00 4.50  ? 87  LEU A O   1 
ATOM   671  C  CB  . LEU A 1 87  ? 17.039 -13.715 18.688  1.00 7.97  ? 87  LEU A CB  1 
ATOM   672  C  CG  . LEU A 1 87  ? 17.106 -14.851 19.686  1.00 13.70 ? 87  LEU A CG  1 
ATOM   673  C  CD1 . LEU A 1 87  ? 18.277 -14.638 20.642  1.00 12.29 ? 87  LEU A CD1 1 
ATOM   674  C  CD2 . LEU A 1 87  ? 15.762 -14.932 20.420  1.00 7.65  ? 87  LEU A CD2 1 
ATOM   675  N  N   . LYS A 1 88  ? 18.525 -15.596 16.308  1.00 6.54  ? 88  LYS A N   1 
ATOM   676  C  CA  . LYS A 1 88  ? 18.298 -16.629 15.300  1.00 10.42 ? 88  LYS A CA  1 
ATOM   677  C  C   . LYS A 1 88  ? 17.975 -17.948 16.001  1.00 11.80 ? 88  LYS A C   1 
ATOM   678  O  O   . LYS A 1 88  ? 18.857 -18.548 16.631  1.00 5.81  ? 88  LYS A O   1 
ATOM   679  C  CB  . LYS A 1 88  ? 19.513 -16.788 14.391  1.00 9.06  ? 88  LYS A CB  1 
ATOM   680  C  CG  . LYS A 1 88  ? 19.661 -15.701 13.333  1.00 13.01 ? 88  LYS A CG  1 
ATOM   681  C  CD  . LYS A 1 88  ? 21.107 -15.269 13.262  1.00 15.29 ? 88  LYS A CD  1 
ATOM   682  C  CE  . LYS A 1 88  ? 21.906 -16.075 12.254  1.00 12.72 ? 88  LYS A CE  1 
ATOM   683  N  NZ  . LYS A 1 88  ? 23.345 -16.033 12.649  1.00 10.09 ? 88  LYS A NZ  1 
ATOM   684  N  N   . LEU A 1 89  ? 16.725 -18.409 15.858  1.00 7.83  ? 89  LEU A N   1 
ATOM   685  C  CA  . LEU A 1 89  ? 16.247 -19.656 16.460  1.00 7.26  ? 89  LEU A CA  1 
ATOM   686  C  C   . LEU A 1 89  ? 16.204 -20.763 15.409  1.00 9.25  ? 89  LEU A C   1 
ATOM   687  O  O   . LEU A 1 89  ? 15.454 -20.673 14.427  1.00 6.66  ? 89  LEU A O   1 
ATOM   688  C  CB  . LEU A 1 89  ? 14.863 -19.464 17.078  1.00 4.99  ? 89  LEU A CB  1 
ATOM   689  C  CG  . LEU A 1 89  ? 14.776 -18.277 18.041  1.00 8.38  ? 89  LEU A CG  1 
ATOM   690  C  CD1 . LEU A 1 89  ? 13.318 -18.015 18.506  1.00 10.29 ? 89  LEU A CD1 1 
ATOM   691  C  CD2 . LEU A 1 89  ? 15.711 -18.538 19.228  1.00 5.42  ? 89  LEU A CD2 1 
ATOM   692  N  N   . LYS A 1 90  ? 16.995 -21.810 15.621  1.00 7.16  ? 90  LYS A N   1 
ATOM   693  C  CA  . LYS A 1 90  ? 16.973 -22.960 14.724  1.00 8.36  ? 90  LYS A CA  1 
ATOM   694  C  C   . LYS A 1 90  ? 15.799 -23.871 15.075  1.00 6.76  ? 90  LYS A C   1 
ATOM   695  O  O   . LYS A 1 90  ? 15.639 -24.277 16.231  1.00 7.90  ? 90  LYS A O   1 
ATOM   696  C  CB  . LYS A 1 90  ? 18.290 -23.724 14.819  1.00 9.06  ? 90  LYS A CB  1 
ATOM   697  C  CG  . LYS A 1 90  ? 18.237 -25.097 14.195  1.00 14.16 ? 90  LYS A CG  1 
ATOM   698  C  CD  . LYS A 1 90  ? 18.878 -25.124 12.828  1.00 23.05 ? 90  LYS A CD  1 
ATOM   699  C  CE  . LYS A 1 90  ? 19.056 -26.563 12.353  1.00 20.51 ? 90  LYS A CE  1 
ATOM   700  N  NZ  . LYS A 1 90  ? 17.920 -26.966 11.462  1.00 22.46 ? 90  LYS A NZ  1 
ATOM   701  N  N   . VAL A 1 91  ? 14.962 -24.175 14.087  1.00 6.20  ? 91  VAL A N   1 
ATOM   702  C  CA  . VAL A 1 91  ? 13.776 -25.000 14.311  1.00 10.72 ? 91  VAL A CA  1 
ATOM   703  C  C   . VAL A 1 91  ? 13.921 -26.298 13.520  1.00 8.63  ? 91  VAL A C   1 
ATOM   704  O  O   . VAL A 1 91  ? 14.678 -26.378 12.550  1.00 8.03  ? 91  VAL A O   1 
ATOM   705  C  CB  . VAL A 1 91  ? 12.457 -24.255 13.954  1.00 7.62  ? 91  VAL A CB  1 
ATOM   706  C  CG1 . VAL A 1 91  ? 12.249 -23.093 14.897  1.00 7.59  ? 91  VAL A CG1 1 
ATOM   707  C  CG2 . VAL A 1 91  ? 12.386 -23.769 12.483  1.00 7.92  ? 91  VAL A CG2 1 
ATOM   708  N  N   . ASP A 1 92  ? 13.205 -27.340 13.952  1.00 10.20 ? 92  ASP A N   1 
ATOM   709  C  CA  . ASP A 1 92  ? 13.425 -28.633 13.299  1.00 13.13 ? 92  ASP A CA  1 
ATOM   710  C  C   . ASP A 1 92  ? 12.657 -28.801 11.988  1.00 13.80 ? 92  ASP A C   1 
ATOM   711  O  O   . ASP A 1 92  ? 12.812 -29.832 11.325  1.00 10.89 ? 92  ASP A O   1 
ATOM   712  C  CB  . ASP A 1 92  ? 13.086 -29.795 14.237  1.00 14.97 ? 92  ASP A CB  1 
ATOM   713  C  CG  . ASP A 1 92  ? 11.610 -29.988 14.429  1.00 14.29 ? 92  ASP A CG  1 
ATOM   714  O  OD1 . ASP A 1 92  ? 10.808 -29.160 13.935  1.00 17.88 ? 92  ASP A OD1 1 
ATOM   715  O  OD2 . ASP A 1 92  ? 11.248 -30.993 15.082  1.00 23.97 ? 92  ASP A OD2 1 
ATOM   716  N  N   . THR A 1 93  ? 11.842 -27.833 11.588  1.00 10.92 ? 93  THR A N   1 
ATOM   717  C  CA  . THR A 1 93  ? 11.068 -27.935 10.363  1.00 10.54 ? 93  THR A CA  1 
ATOM   718  C  C   . THR A 1 93  ? 11.375 -26.738 9.470   1.00 14.64 ? 93  THR A C   1 
ATOM   719  O  O   . THR A 1 93  ? 11.376 -25.594 9.941   1.00 12.13 ? 93  THR A O   1 
ATOM   720  C  CB  . THR A 1 93  ? 9.570  -27.999 10.681  1.00 13.84 ? 93  THR A CB  1 
ATOM   721  O  OG1 . THR A 1 93  ? 9.315  -29.104 11.567  1.00 13.39 ? 93  THR A OG1 1 
ATOM   722  C  CG2 . THR A 1 93  ? 8.760  -28.156 9.392   1.00 13.64 ? 93  THR A CG2 1 
ATOM   723  N  N   . ALA A 1 94  ? 11.653 -27.007 8.195   1.00 11.09 ? 94  ALA A N   1 
ATOM   724  C  CA  . ALA A 1 94  ? 11.803 -25.959 7.193   1.00 9.55  ? 94  ALA A CA  1 
ATOM   725  C  C   . ALA A 1 94  ? 10.439 -25.401 6.820   1.00 8.64  ? 94  ALA A C   1 
ATOM   726  O  O   . ALA A 1 94  ? 9.499  -26.166 6.572   1.00 9.87  ? 94  ALA A O   1 
ATOM   727  C  CB  . ALA A 1 94  ? 12.492 -26.509 5.941   1.00 10.39 ? 94  ALA A CB  1 
ATOM   728  N  N   . ASN A 1 95  ? 10.329 -24.077 6.751   1.00 7.15  ? 95  ASN A N   1 
ATOM   729  C  CA  . ASN A 1 95  ? 9.055  -23.467 6.382   1.00 8.10  ? 95  ASN A CA  1 
ATOM   730  C  C   . ASN A 1 95  ? 8.664  -23.880 4.961   1.00 8.71  ? 95  ASN A C   1 
ATOM   731  O  O   . ASN A 1 95  ? 9.365  -23.522 4.007   1.00 5.02  ? 95  ASN A O   1 
ATOM   732  C  CB  . ASN A 1 95  ? 9.123  -21.943 6.492   1.00 7.99  ? 95  ASN A CB  1 
ATOM   733  C  CG  . ASN A 1 95  ? 7.783  -21.268 6.168   1.00 11.06 ? 95  ASN A CG  1 
ATOM   734  O  OD1 . ASN A 1 95  ? 6.807  -21.941 5.807   1.00 9.44  ? 95  ASN A OD1 1 
ATOM   735  N  ND2 . ASN A 1 95  ? 7.734  -19.932 6.294   1.00 9.29  ? 95  ASN A ND2 1 
ATOM   736  N  N   . PRO A 1 96  ? 7.551  -24.598 4.766   1.00 8.88  ? 96  PRO A N   1 
ATOM   737  C  CA  . PRO A 1 96  ? 7.184  -25.006 3.401   1.00 13.21 ? 96  PRO A CA  1 
ATOM   738  C  C   . PRO A 1 96  ? 6.765  -23.843 2.500   1.00 9.49  ? 96  PRO A C   1 
ATOM   739  O  O   . PRO A 1 96  ? 6.635  -24.040 1.281   1.00 6.25  ? 96  PRO A O   1 
ATOM   740  C  CB  . PRO A 1 96  ? 6.037  -26.009 3.625   1.00 9.27  ? 96  PRO A CB  1 
ATOM   741  C  CG  . PRO A 1 96  ? 5.475  -25.673 4.943   1.00 10.90 ? 96  PRO A CG  1 
ATOM   742  C  CD  . PRO A 1 96  ? 6.602  -25.096 5.772   1.00 9.27  ? 96  PRO A CD  1 
ATOM   743  N  N   . LYS A 1 97  ? 6.584  -22.637 3.040   1.00 9.97  ? 97  LYS A N   1 
ATOM   744  C  CA  . LYS A 1 97  ? 6.246  -21.473 2.227   1.00 8.47  ? 97  LYS A CA  1 
ATOM   745  C  C   . LYS A 1 97  ? 7.426  -20.527 2.042   1.00 11.67 ? 97  LYS A C   1 
ATOM   746  O  O   . LYS A 1 97  ? 7.235  -19.370 1.647   1.00 11.41 ? 97  LYS A O   1 
ATOM   747  C  CB  . LYS A 1 97  ? 5.050  -20.741 2.834   1.00 13.09 ? 97  LYS A CB  1 
ATOM   748  C  CG  . LYS A 1 97  ? 3.880  -21.672 3.091   1.00 9.94  ? 97  LYS A CG  1 
ATOM   749  C  CD  . LYS A 1 97  ? 2.551  -20.956 3.113   1.00 18.60 ? 97  LYS A CD  1 
ATOM   750  C  CE  . LYS A 1 97  ? 2.032  -20.826 4.533   1.00 22.65 ? 97  LYS A CE  1 
ATOM   751  N  NZ  . LYS A 1 97  ? 0.655  -21.402 4.665   1.00 26.24 ? 97  LYS A NZ  1 
ATOM   752  N  N   . THR A 1 98  ? 8.636  -20.990 2.309   1.00 10.75 ? 98  THR A N   1 
ATOM   753  C  CA  . THR A 1 98  ? 9.804  -20.145 2.132   1.00 11.44 ? 98  THR A CA  1 
ATOM   754  C  C   . THR A 1 98  ? 9.905  -19.737 0.667   1.00 13.22 ? 98  THR A C   1 
ATOM   755  O  O   . THR A 1 98  ? 10.015 -20.610 -0.208  1.00 10.08 ? 98  THR A O   1 
ATOM   756  C  CB  . THR A 1 98  ? 11.085 -20.851 2.552   1.00 11.73 ? 98  THR A CB  1 
ATOM   757  O  OG1 . THR A 1 98  ? 10.987 -21.294 3.923   1.00 10.88 ? 98  THR A OG1 1 
ATOM   758  C  CG2 . THR A 1 98  ? 12.265 -19.897 2.386   1.00 8.17  ? 98  THR A CG2 1 
ATOM   759  N  N   . PRO A 1 99  ? 9.855  -18.453 0.352   1.00 11.81 ? 99  PRO A N   1 
ATOM   760  C  CA  . PRO A 1 99  ? 10.067 -18.028 -1.031  1.00 12.22 ? 99  PRO A CA  1 
ATOM   761  C  C   . PRO A 1 99  ? 11.555 -18.040 -1.337  1.00 12.50 ? 99  PRO A C   1 
ATOM   762  O  O   . PRO A 1 99  ? 12.398 -18.168 -0.447  1.00 6.86  ? 99  PRO A O   1 
ATOM   763  C  CB  . PRO A 1 99  ? 9.514  -16.601 -1.040  1.00 10.38 ? 99  PRO A CB  1 
ATOM   764  C  CG  . PRO A 1 99  ? 9.890  -16.086 0.336   1.00 12.93 ? 99  PRO A CG  1 
ATOM   765  C  CD  . PRO A 1 99  ? 9.718  -17.306 1.269   1.00 9.43  ? 99  PRO A CD  1 
ATOM   766  N  N   . LYS A 1 100 ? 11.874 -17.885 -2.618  1.00 13.81 ? 100 LYS A N   1 
ATOM   767  C  CA  . LYS A 1 100 ? 13.220 -17.460 -2.956  1.00 12.77 ? 100 LYS A CA  1 
ATOM   768  C  C   . LYS A 1 100 ? 13.476 -16.113 -2.275  1.00 12.17 ? 100 LYS A C   1 
ATOM   769  O  O   . LYS A 1 100 ? 12.623 -15.217 -2.292  1.00 9.30  ? 100 LYS A O   1 
ATOM   770  C  CB  . LYS A 1 100 ? 13.385 -17.368 -4.476  1.00 14.77 ? 100 LYS A CB  1 
ATOM   771  C  CG  . LYS A 1 100 ? 14.823 -17.200 -4.949  1.00 19.22 ? 100 LYS A CG  1 
ATOM   772  C  CD  . LYS A 1 100 ? 14.967 -17.509 -6.456  1.00 24.16 ? 100 LYS A CD  1 
ATOM   773  C  CE  . LYS A 1 100 ? 16.273 -16.962 -7.041  1.00 30.36 ? 100 LYS A CE  1 
ATOM   774  N  NZ  . LYS A 1 100 ? 17.492 -17.598 -6.432  1.00 30.75 ? 100 LYS A NZ  1 
ATOM   775  N  N   . TYR A 1 101 ? 14.628 -15.981 -1.627  1.00 7.79  ? 101 TYR A N   1 
ATOM   776  C  CA  . TYR A 1 101 ? 14.874 -14.770 -0.859  1.00 11.07 ? 101 TYR A CA  1 
ATOM   777  C  C   . TYR A 1 101 ? 16.369 -14.539 -0.724  1.00 9.51  ? 101 TYR A C   1 
ATOM   778  O  O   . TYR A 1 101 ? 17.180 -15.448 -0.925  1.00 10.45 ? 101 TYR A O   1 
ATOM   779  C  CB  . TYR A 1 101 ? 14.219 -14.847 0.524   1.00 8.60  ? 101 TYR A CB  1 
ATOM   780  C  CG  . TYR A 1 101 ? 14.951 -15.734 1.517   1.00 7.24  ? 101 TYR A CG  1 
ATOM   781  C  CD1 . TYR A 1 101 ? 14.757 -17.115 1.512   1.00 10.92 ? 101 TYR A CD1 1 
ATOM   782  C  CD2 . TYR A 1 101 ? 15.822 -15.196 2.466   1.00 6.98  ? 101 TYR A CD2 1 
ATOM   783  C  CE1 . TYR A 1 101 ? 15.416 -17.946 2.411   1.00 9.87  ? 101 TYR A CE1 1 
ATOM   784  C  CE2 . TYR A 1 101 ? 16.490 -16.025 3.399   1.00 7.81  ? 101 TYR A CE2 1 
ATOM   785  C  CZ  . TYR A 1 101 ? 16.277 -17.403 3.356   1.00 12.81 ? 101 TYR A CZ  1 
ATOM   786  O  OH  . TYR A 1 101 ? 16.911 -18.252 4.251   1.00 10.12 ? 101 TYR A OH  1 
ATOM   787  N  N   . LYS A 1 102 ? 16.719 -13.296 -0.395  1.00 8.75  ? 102 LYS A N   1 
ATOM   788  C  CA  . LYS A 1 102 ? 18.061 -12.954 0.051   1.00 8.48  ? 102 LYS A CA  1 
ATOM   789  C  C   . LYS A 1 102 ? 17.954 -11.826 1.063   1.00 5.77  ? 102 LYS A C   1 
ATOM   790  O  O   . LYS A 1 102 ? 16.931 -11.149 1.155   1.00 6.18  ? 102 LYS A O   1 
ATOM   791  C  CB  . LYS A 1 102 ? 18.986 -12.535 -1.102  1.00 13.48 ? 102 LYS A CB  1 
ATOM   792  C  CG  . LYS A 1 102 ? 18.303 -11.994 -2.313  1.00 13.62 ? 102 LYS A CG  1 
ATOM   793  C  CD  . LYS A 1 102 ? 19.340 -11.486 -3.315  1.00 25.19 ? 102 LYS A CD  1 
ATOM   794  C  CE  . LYS A 1 102 ? 18.741 -10.449 -4.265  1.00 27.39 ? 102 LYS A CE  1 
ATOM   795  N  NZ  . LYS A 1 102 ? 19.762 -9.901  -5.204  1.00 21.46 ? 102 LYS A NZ  1 
ATOM   796  N  N   . PHE A 1 103 ? 19.011 -11.657 1.847   1.00 4.49  ? 103 PHE A N   1 
ATOM   797  C  CA  . PHE A 1 103 ? 19.112 -10.559 2.798   1.00 7.44  ? 103 PHE A CA  1 
ATOM   798  C  C   . PHE A 1 103 ? 19.954 -9.479  2.145   1.00 11.13 ? 103 PHE A C   1 
ATOM   799  O  O   . PHE A 1 103 ? 21.043 -9.771  1.635   1.00 7.45  ? 103 PHE A O   1 
ATOM   800  C  CB  . PHE A 1 103 ? 19.771 -10.999 4.114   1.00 5.10  ? 103 PHE A CB  1 
ATOM   801  C  CG  . PHE A 1 103 ? 18.952 -11.962 4.934   1.00 5.03  ? 103 PHE A CG  1 
ATOM   802  C  CD1 . PHE A 1 103 ? 17.631 -12.233 4.616   1.00 7.75  ? 103 PHE A CD1 1 
ATOM   803  C  CD2 . PHE A 1 103 ? 19.512 -12.587 6.043   1.00 7.09  ? 103 PHE A CD2 1 
ATOM   804  C  CE1 . PHE A 1 103 ? 16.878 -13.122 5.387   1.00 6.15  ? 103 PHE A CE1 1 
ATOM   805  C  CE2 . PHE A 1 103 ? 18.768 -13.466 6.828   1.00 5.64  ? 103 PHE A CE2 1 
ATOM   806  C  CZ  . PHE A 1 103 ? 17.454 -13.733 6.498   1.00 6.66  ? 103 PHE A CZ  1 
ATOM   807  N  N   . VAL A 1 104 ? 19.460 -8.239  2.157   1.00 10.95 ? 104 VAL A N   1 
ATOM   808  C  CA  . VAL A 1 104 ? 20.182 -7.125  1.553   1.00 6.51  ? 104 VAL A CA  1 
ATOM   809  C  C   . VAL A 1 104 ? 20.120 -5.921  2.479   1.00 10.13 ? 104 VAL A C   1 
ATOM   810  O  O   . VAL A 1 104 ? 19.090 -5.655  3.105   1.00 14.70 ? 104 VAL A O   1 
ATOM   811  C  CB  . VAL A 1 104 ? 19.628 -6.768  0.154   1.00 11.14 ? 104 VAL A CB  1 
ATOM   812  C  CG1 . VAL A 1 104 ? 19.446 -8.037  -0.686  1.00 13.36 ? 104 VAL A CG1 1 
ATOM   813  C  CG2 . VAL A 1 104 ? 18.329 -6.008  0.267   1.00 15.11 ? 104 VAL A CG2 1 
ATOM   814  N  N   . ARG A 1 105 ? 21.221 -5.182  2.556   1.00 7.49  ? 105 ARG A N   1 
ATOM   815  C  CA  . ARG A 1 105 ? 21.222 -3.882  3.210   1.00 9.55  ? 105 ARG A CA  1 
ATOM   816  C  C   . ARG A 1 105 ? 20.981 -2.824  2.139   1.00 12.51 ? 105 ARG A C   1 
ATOM   817  O  O   . ARG A 1 105 ? 21.723 -2.757  1.155   1.00 13.13 ? 105 ARG A O   1 
ATOM   818  C  CB  . ARG A 1 105 ? 22.541 -3.621  3.942   1.00 9.19  ? 105 ARG A CB  1 
ATOM   819  C  CG  . ARG A 1 105 ? 22.449 -2.451  4.933   1.00 10.33 ? 105 ARG A CG  1 
ATOM   820  C  CD  . ARG A 1 105 ? 23.673 -2.350  5.788   1.00 10.60 ? 105 ARG A CD  1 
ATOM   821  N  NE  . ARG A 1 105 ? 23.690 -1.143  6.612   1.00 13.05 ? 105 ARG A NE  1 
ATOM   822  C  CZ  . ARG A 1 105 ? 23.261 -1.080  7.869   1.00 8.28  ? 105 ARG A CZ  1 
ATOM   823  N  NH1 . ARG A 1 105 ? 22.639 -2.100  8.442   1.00 6.09  ? 105 ARG A NH1 1 
ATOM   824  N  NH2 . ARG A 1 105 ? 23.448 0.040   8.565   1.00 7.02  ? 105 ARG A NH2 1 
ATOM   825  N  N   . ILE A 1 106 ? 19.942 -2.025  2.310   1.00 14.58 ? 106 ILE A N   1 
ATOM   826  C  CA  . ILE A 1 106 ? 19.614 -1.010  1.327   1.00 13.22 ? 106 ILE A CA  1 
ATOM   827  C  C   . ILE A 1 106 ? 20.311 0.291   1.704   1.00 15.47 ? 106 ILE A C   1 
ATOM   828  O  O   . ILE A 1 106 ? 20.769 0.490   2.837   1.00 10.73 ? 106 ILE A O   1 
ATOM   829  C  CB  . ILE A 1 106 ? 18.093 -0.801  1.179   1.00 11.98 ? 106 ILE A CB  1 
ATOM   830  C  CG1 . ILE A 1 106 ? 17.413 -0.778  2.546   1.00 12.28 ? 106 ILE A CG1 1 
ATOM   831  C  CG2 . ILE A 1 106 ? 17.482 -1.892  0.309   1.00 13.90 ? 106 ILE A CG2 1 
ATOM   832  C  CD1 . ILE A 1 106 ? 17.452 0.552   3.227   1.00 12.40 ? 106 ILE A CD1 1 
ATOM   833  N  N   . GLN A 1 107 ? 20.395 1.163   0.750   1.00 13.68 ? 107 GLN A N   1 
ATOM   834  C  CA  . GLN A 1 107 ? 20.991 2.481   0.868   1.00 12.37 ? 107 GLN A CA  1 
ATOM   835  C  C   . GLN A 1 107 ? 19.929 3.509   1.236   1.00 11.43 ? 107 GLN A C   1 
ATOM   836  O  O   . GLN A 1 107 ? 18.750 3.333   0.902   1.00 10.84 ? 107 GLN A O   1 
ATOM   837  C  CB  . GLN A 1 107 ? 21.648 2.874   -0.450  1.00 19.08 ? 107 GLN A CB  1 
ATOM   838  C  CG  . GLN A 1 107 ? 22.830 1.987   -0.829  1.00 18.00 ? 107 GLN A CG  1 
ATOM   839  C  CD  . GLN A 1 107 ? 23.921 2.006   0.232   1.00 23.20 ? 107 GLN A CD  1 
ATOM   840  O  OE1 . GLN A 1 107 ? 24.658 2.991   0.369   1.00 26.77 ? 107 GLN A OE1 1 
ATOM   841  N  NE2 . GLN A 1 107 ? 24.020 0.923   1.003   1.00 24.93 ? 107 GLN A NE2 1 
ATOM   842  N  N   . PRO A 1 108 ? 20.326 4.575   1.941   1.00 9.22  ? 108 PRO A N   1 
ATOM   843  C  CA  . PRO A 1 108 ? 19.401 5.691   2.188   1.00 9.92  ? 108 PRO A CA  1 
ATOM   844  C  C   . PRO A 1 108 ? 18.803 6.187   0.880   1.00 10.80 ? 108 PRO A C   1 
ATOM   845  O  O   . PRO A 1 108 ? 19.479 6.243   -0.143  1.00 8.05  ? 108 PRO A O   1 
ATOM   846  C  CB  . PRO A 1 108 ? 20.284 6.770   2.837   1.00 11.59 ? 108 PRO A CB  1 
ATOM   847  C  CG  . PRO A 1 108 ? 21.604 6.177   3.065   1.00 13.60 ? 108 PRO A CG  1 
ATOM   848  C  CD  . PRO A 1 108 ? 21.704 4.854   2.380   1.00 10.58 ? 108 PRO A CD  1 
ATOM   849  N  N   . GLY A 1 109 ? 17.522 6.562   0.919   1.00 9.62  ? 109 GLY A N   1 
ATOM   850  C  CA  . GLY A 1 109 ? 16.831 7.030   -0.253  1.00 7.63  ? 109 GLY A CA  1 
ATOM   851  C  C   . GLY A 1 109 ? 16.120 5.949   -1.039  1.00 11.61 ? 109 GLY A C   1 
ATOM   852  O  O   . GLY A 1 109 ? 15.242 6.270   -1.836  1.00 10.16 ? 109 GLY A O   1 
ATOM   853  N  N   . GLN A 1 110 ? 16.473 4.678   -0.838  1.00 13.11 ? 110 GLN A N   1 
ATOM   854  C  CA  . GLN A 1 110 ? 15.772 3.580   -1.489  1.00 14.19 ? 110 GLN A CA  1 
ATOM   855  C  C   . GLN A 1 110 ? 14.470 3.272   -0.754  1.00 11.71 ? 110 GLN A C   1 
ATOM   856  O  O   . GLN A 1 110 ? 14.293 3.593   0.428   1.00 11.39 ? 110 GLN A O   1 
ATOM   857  C  CB  . GLN A 1 110 ? 16.643 2.316   -1.554  1.00 10.47 ? 110 GLN A CB  1 
ATOM   858  C  CG  . GLN A 1 110 ? 17.965 2.460   -2.315  1.00 14.23 ? 110 GLN A CG  1 
ATOM   859  C  CD  . GLN A 1 110 ? 18.598 1.097   -2.650  1.00 25.35 ? 110 GLN A CD  1 
ATOM   860  O  OE1 . GLN A 1 110 ? 19.378 0.536   -1.859  1.00 18.96 ? 110 GLN A OE1 1 
ATOM   861  N  NE2 . GLN A 1 110 ? 18.238 0.546   -3.818  1.00 27.27 ? 110 GLN A NE2 1 
ATOM   862  N  N   . THR A 1 111 ? 13.549 2.637   -1.470  1.00 10.40 ? 111 THR A N   1 
ATOM   863  C  CA  . THR A 1 111 ? 12.228 2.357   -0.939  1.00 9.70  ? 111 THR A CA  1 
ATOM   864  C  C   . THR A 1 111 ? 12.046 0.861   -0.733  1.00 7.21  ? 111 THR A C   1 
ATOM   865  O  O   . THR A 1 111 ? 12.786 0.039   -1.282  1.00 7.28  ? 111 THR A O   1 
ATOM   866  C  CB  . THR A 1 111 ? 11.137 2.885   -1.874  1.00 7.31  ? 111 THR A CB  1 
ATOM   867  O  OG1 . THR A 1 111 ? 11.300 2.283   -3.161  1.00 8.00  ? 111 THR A OG1 1 
ATOM   868  C  CG2 . THR A 1 111 ? 11.227 4.402   -1.997  1.00 7.92  ? 111 THR A CG2 1 
ATOM   869  N  N   . PHE A 1 112 ? 11.042 0.525   0.074   1.00 6.27  ? 112 PHE A N   1 
ATOM   870  C  CA  . PHE A 1 112 ? 10.691 -0.859  0.330   1.00 6.60  ? 112 PHE A CA  1 
ATOM   871  C  C   . PHE A 1 112 ? 9.284  -0.908  0.902   1.00 5.08  ? 112 PHE A C   1 
ATOM   872  O  O   . PHE A 1 112 ? 8.752  0.099   1.385   1.00 4.08  ? 112 PHE A O   1 
ATOM   873  C  CB  . PHE A 1 112 ? 11.690 -1.534  1.278   1.00 4.75  ? 112 PHE A CB  1 
ATOM   874  C  CG  . PHE A 1 112 ? 11.784 -0.893  2.655   1.00 6.63  ? 112 PHE A CG  1 
ATOM   875  C  CD1 . PHE A 1 112 ? 12.689 0.138   2.899   1.00 6.97  ? 112 PHE A CD1 1 
ATOM   876  C  CD2 . PHE A 1 112 ? 10.994 -1.338  3.701   1.00 5.36  ? 112 PHE A CD2 1 
ATOM   877  C  CE1 . PHE A 1 112 ? 12.814 0.707   4.172   1.00 9.46  ? 112 PHE A CE1 1 
ATOM   878  C  CE2 . PHE A 1 112 ? 11.102 -0.762  4.988   1.00 5.04  ? 112 PHE A CE2 1 
ATOM   879  C  CZ  . PHE A 1 112 ? 12.007 0.252   5.221   1.00 7.03  ? 112 PHE A CZ  1 
ATOM   880  N  N   . SER A 1 113 ? 8.704  -2.099  0.851   1.00 1.30  ? 113 SER A N   1 
ATOM   881  C  CA  . SER A 1 113 ? 7.394  -2.375  1.413   1.00 3.38  ? 113 SER A CA  1 
ATOM   882  C  C   . SER A 1 113 ? 7.514  -2.904  2.840   1.00 4.37  ? 113 SER A C   1 
ATOM   883  O  O   . SER A 1 113 ? 8.460  -3.623  3.189   1.00 2.82  ? 113 SER A O   1 
ATOM   884  C  CB  . SER A 1 113 ? 6.655  -3.384  0.539   1.00 4.56  ? 113 SER A CB  1 
ATOM   885  O  OG  . SER A 1 113 ? 6.531  -2.882  -0.785  1.00 8.42  ? 113 SER A OG  1 
ATOM   886  N  N   . VAL A 1 114 ? 6.537  -2.542  3.669   1.00 4.87  ? 114 VAL A N   1 
ATOM   887  C  CA  . VAL A 1 114 ? 6.481  -2.978  5.060   1.00 3.43  ? 114 VAL A CA  1 
ATOM   888  C  C   . VAL A 1 114 ? 5.199  -3.764  5.252   1.00 3.79  ? 114 VAL A C   1 
ATOM   889  O  O   . VAL A 1 114 ? 4.112  -3.293  4.893   1.00 3.60  ? 114 VAL A O   1 
ATOM   890  C  CB  . VAL A 1 114 ? 6.525  -1.806  6.056   1.00 4.34  ? 114 VAL A CB  1 
ATOM   891  C  CG1 . VAL A 1 114 ? 6.405  -2.339  7.494   1.00 1.98  ? 114 VAL A CG1 1 
ATOM   892  C  CG2 . VAL A 1 114 ? 7.777  -0.944  5.865   1.00 5.09  ? 114 VAL A CG2 1 
ATOM   893  N  N   . LEU A 1 115 ? 5.319  -4.940  5.834   1.00 3.10  ? 115 LEU A N   1 
ATOM   894  C  CA  . LEU A 1 115 ? 4.166  -5.745  6.221   1.00 6.05  ? 115 LEU A CA  1 
ATOM   895  C  C   . LEU A 1 115 ? 4.066  -5.643  7.736   1.00 6.65  ? 115 LEU A C   1 
ATOM   896  O  O   . LEU A 1 115 ? 4.786  -6.335  8.462   1.00 5.82  ? 115 LEU A O   1 
ATOM   897  C  CB  . LEU A 1 115 ? 4.315  -7.188  5.762   1.00 5.43  ? 115 LEU A CB  1 
ATOM   898  C  CG  . LEU A 1 115 ? 3.165  -8.126  6.151   1.00 8.15  ? 115 LEU A CG  1 
ATOM   899  C  CD1 . LEU A 1 115 ? 1.860  -7.731  5.457   1.00 7.18  ? 115 LEU A CD1 1 
ATOM   900  C  CD2 . LEU A 1 115 ? 3.506  -9.587  5.894   1.00 3.98  ? 115 LEU A CD2 1 
ATOM   901  N  N   . ALA A 1 116 ? 3.199  -4.756  8.209   1.00 3.55  ? 116 ALA A N   1 
ATOM   902  C  CA  . ALA A 1 116 ? 3.000  -4.603  9.643   1.00 7.77  ? 116 ALA A CA  1 
ATOM   903  C  C   . ALA A 1 116 ? 2.257  -5.817  10.172  1.00 10.74 ? 116 ALA A C   1 
ATOM   904  O  O   . ALA A 1 116 ? 1.308  -6.296  9.539   1.00 7.76  ? 116 ALA A O   1 
ATOM   905  C  CB  . ALA A 1 116 ? 2.228  -3.321  9.945   1.00 7.96  ? 116 ALA A CB  1 
ATOM   906  N  N   . CYS A 1 117 ? 2.723  -6.337  11.308  1.00 8.77  ? 117 CYS A N   1 
ATOM   907  C  CA  . CYS A 1 117 ? 2.200  -7.556  11.902  1.00 10.86 ? 117 CYS A CA  1 
ATOM   908  C  C   . CYS A 1 117 ? 2.074  -7.384  13.413  1.00 10.19 ? 117 CYS A C   1 
ATOM   909  O  O   . CYS A 1 117 ? 2.835  -6.644  14.041  1.00 6.92  ? 117 CYS A O   1 
ATOM   910  C  CB  . CYS A 1 117 ? 3.101  -8.777  11.608  1.00 9.50  ? 117 CYS A CB  1 
ATOM   911  S  SG  . CYS A 1 117 ? 3.336  -9.155  9.865   1.00 14.70 ? 117 CYS A SG  1 
ATOM   912  N  N   . TYR A 1 118 ? 1.116  -8.106  13.991  1.00 12.52 ? 118 TYR A N   1 
ATOM   913  C  CA  . TYR A 1 118 ? 0.868  -8.090  15.425  1.00 12.12 ? 118 TYR A CA  1 
ATOM   914  C  C   . TYR A 1 118 ? 0.557  -9.509  15.858  1.00 14.72 ? 118 TYR A C   1 
ATOM   915  O  O   . TYR A 1 118 ? -0.327 -10.153 15.283  1.00 13.36 ? 118 TYR A O   1 
ATOM   916  C  CB  . TYR A 1 118 ? -0.279 -7.119  15.771  1.00 13.80 ? 118 TYR A CB  1 
ATOM   917  C  CG  . TYR A 1 118 ? 0.107  -5.707  15.396  1.00 12.52 ? 118 TYR A CG  1 
ATOM   918  C  CD1 . TYR A 1 118 ? -0.149 -5.213  14.122  1.00 12.43 ? 118 TYR A CD1 1 
ATOM   919  C  CD2 . TYR A 1 118 ? 0.813  -4.898  16.286  1.00 11.48 ? 118 TYR A CD2 1 
ATOM   920  C  CE1 . TYR A 1 118 ? 0.249  -3.931  13.751  1.00 14.96 ? 118 TYR A CE1 1 
ATOM   921  C  CE2 . TYR A 1 118 ? 1.204  -3.604  15.929  1.00 8.59  ? 118 TYR A CE2 1 
ATOM   922  C  CZ  . TYR A 1 118 ? 0.921  -3.136  14.652  1.00 11.32 ? 118 TYR A CZ  1 
ATOM   923  O  OH  . TYR A 1 118 ? 1.302  -1.877  14.264  1.00 8.72  ? 118 TYR A OH  1 
ATOM   924  N  N   . ASN A 1 119 ? 1.301  -10.003 16.848  1.00 15.02 ? 119 ASN A N   1 
ATOM   925  C  CA  . ASN A 1 119 ? 1.141  -11.380 17.310  1.00 18.69 ? 119 ASN A CA  1 
ATOM   926  C  C   . ASN A 1 119 ? 1.345  -12.375 16.165  1.00 12.23 ? 119 ASN A C   1 
ATOM   927  O  O   . ASN A 1 119 ? 0.658  -13.392 16.071  1.00 13.59 ? 119 ASN A O   1 
ATOM   928  C  CB  . ASN A 1 119 ? -0.228 -11.578 17.961  1.00 22.00 ? 119 ASN A CB  1 
ATOM   929  C  CG  . ASN A 1 119 ? -0.201 -11.326 19.442  1.00 31.99 ? 119 ASN A CG  1 
ATOM   930  O  OD1 . ASN A 1 119 ? 0.459  -12.047 20.197  1.00 30.36 ? 119 ASN A OD1 1 
ATOM   931  N  ND2 . ASN A 1 119 ? -0.904 -10.280 19.876  1.00 38.25 ? 119 ASN A ND2 1 
ATOM   932  N  N   . GLY A 1 120 ? 2.298  -12.078 15.286  1.00 10.40 ? 120 GLY A N   1 
ATOM   933  C  CA  . GLY A 1 120 ? 2.568  -12.920 14.138  1.00 9.55  ? 120 GLY A CA  1 
ATOM   934  C  C   . GLY A 1 120 ? 1.537  -12.866 13.032  1.00 11.26 ? 120 GLY A C   1 
ATOM   935  O  O   . GLY A 1 120 ? 1.634  -13.655 12.086  1.00 11.14 ? 120 GLY A O   1 
ATOM   936  N  N   . SER A 1 121 ? 0.543  -11.973 13.129  1.00 10.72 ? 121 SER A N   1 
ATOM   937  C  CA  . SER A 1 121 ? -0.550 -11.875 12.160  1.00 17.07 ? 121 SER A CA  1 
ATOM   938  C  C   . SER A 1 121 ? -0.388 -10.634 11.291  1.00 14.13 ? 121 SER A C   1 
ATOM   939  O  O   . SER A 1 121 ? -0.358 -9.513  11.820  1.00 13.68 ? 121 SER A O   1 
ATOM   940  C  CB  . SER A 1 121 ? -1.900 -11.832 12.875  1.00 23.70 ? 121 SER A CB  1 
ATOM   941  O  OG  . SER A 1 121 ? -2.451 -13.123 13.020  1.00 29.76 ? 121 SER A OG  1 
ATOM   942  N  N   . PRO A 1 122 ? -0.307 -10.771 9.971   1.00 16.53 ? 122 PRO A N   1 
ATOM   943  C  CA  . PRO A 1 122 ? -0.194 -9.579  9.113   1.00 14.48 ? 122 PRO A CA  1 
ATOM   944  C  C   . PRO A 1 122 ? -1.414 -8.672  9.243   1.00 17.36 ? 122 PRO A C   1 
ATOM   945  O  O   . PRO A 1 122 ? -2.555 -9.136  9.291   1.00 20.52 ? 122 PRO A O   1 
ATOM   946  C  CB  . PRO A 1 122 ? -0.075 -10.168 7.701   1.00 15.28 ? 122 PRO A CB  1 
ATOM   947  C  CG  . PRO A 1 122 ? 0.427  -11.614 7.929   1.00 17.16 ? 122 PRO A CG  1 
ATOM   948  C  CD  . PRO A 1 122 ? -0.253 -12.034 9.212   1.00 11.91 ? 122 PRO A CD  1 
ATOM   949  N  N   . SER A 1 123 ? -1.167 -7.365  9.299   1.00 15.78 ? 123 SER A N   1 
ATOM   950  C  CA  . SER A 1 123 ? -2.241 -6.387  9.477   1.00 21.61 ? 123 SER A CA  1 
ATOM   951  C  C   . SER A 1 123 ? -2.381 -5.399  8.328   1.00 16.58 ? 123 SER A C   1 
ATOM   952  O  O   . SER A 1 123 ? -3.506 -5.025  7.982   1.00 15.09 ? 123 SER A O   1 
ATOM   953  C  CB  . SER A 1 123 ? -2.032 -5.608  10.791  1.00 20.49 ? 123 SER A CB  1 
ATOM   954  O  OG  . SER A 1 123 ? -2.709 -4.363  10.765  1.00 29.18 ? 123 SER A OG  1 
ATOM   955  N  N   . GLY A 1 124 ? -1.277 -4.942  7.742   1.00 8.85  ? 124 GLY A N   1 
ATOM   956  C  CA  . GLY A 1 124 ? -1.344 -3.964  6.672   1.00 9.71  ? 124 GLY A CA  1 
ATOM   957  C  C   . GLY A 1 124 ? -0.041 -3.922  5.909   1.00 11.44 ? 124 GLY A C   1 
ATOM   958  O  O   . GLY A 1 124 ? 1.006  -4.375  6.393   1.00 9.12  ? 124 GLY A O   1 
ATOM   959  N  N   . VAL A 1 125 ? -0.115 -3.387  4.695   1.00 8.02  ? 125 VAL A N   1 
ATOM   960  C  CA  . VAL A 1 125 ? 1.064  -3.255  3.858   1.00 6.16  ? 125 VAL A CA  1 
ATOM   961  C  C   . VAL A 1 125 ? 1.125  -1.832  3.323   1.00 8.09  ? 125 VAL A C   1 
ATOM   962  O  O   . VAL A 1 125 ? 0.104  -1.259  2.923   1.00 6.85  ? 125 VAL A O   1 
ATOM   963  C  CB  . VAL A 1 125 ? 1.071  -4.316  2.732   1.00 8.25  ? 125 VAL A CB  1 
ATOM   964  C  CG1 . VAL A 1 125 ? -0.211 -4.265  1.914   1.00 9.73  ? 125 VAL A CG1 1 
ATOM   965  C  CG2 . VAL A 1 125 ? 2.314  -4.181  1.864   1.00 6.82  ? 125 VAL A CG2 1 
ATOM   966  N  N   . TYR A 1 126 ? 2.316  -1.244  3.356   1.00 7.62  ? 126 TYR A N   1 
ATOM   967  C  CA  . TYR A 1 126 ? 2.485  0.124   2.892   1.00 9.38  ? 126 TYR A CA  1 
ATOM   968  C  C   . TYR A 1 126 ? 3.915  0.291   2.410   1.00 7.80  ? 126 TYR A C   1 
ATOM   969  O  O   . TYR A 1 126 ? 4.795  -0.502  2.745   1.00 5.72  ? 126 TYR A O   1 
ATOM   970  C  CB  . TYR A 1 126 ? 2.129  1.150   3.983   1.00 8.62  ? 126 TYR A CB  1 
ATOM   971  C  CG  . TYR A 1 126 ? 2.928  1.072   5.284   1.00 7.88  ? 126 TYR A CG  1 
ATOM   972  C  CD1 . TYR A 1 126 ? 4.163  1.700   5.400   1.00 8.75  ? 126 TYR A CD1 1 
ATOM   973  C  CD2 . TYR A 1 126 ? 2.427  0.412   6.400   1.00 13.43 ? 126 TYR A CD2 1 
ATOM   974  C  CE1 . TYR A 1 126 ? 4.883  1.654   6.584   1.00 9.91  ? 126 TYR A CE1 1 
ATOM   975  C  CE2 . TYR A 1 126 ? 3.143  0.361   7.601   1.00 9.50  ? 126 TYR A CE2 1 
ATOM   976  C  CZ  . TYR A 1 126 ? 4.375  0.983   7.673   1.00 6.49  ? 126 TYR A CZ  1 
ATOM   977  O  OH  . TYR A 1 126 ? 5.083  0.955   8.849   1.00 9.67  ? 126 TYR A OH  1 
ATOM   978  N  N   . GLN A 1 127 ? 4.130  1.323   1.602   1.00 5.46  ? 127 GLN A N   1 
ATOM   979  C  CA  . GLN A 1 127 ? 5.425  1.623   1.018   1.00 6.93  ? 127 GLN A CA  1 
ATOM   980  C  C   . GLN A 1 127 ? 6.089  2.776   1.762   1.00 12.79 ? 127 GLN A C   1 
ATOM   981  O  O   . GLN A 1 127 ? 5.410  3.652   2.312   1.00 12.23 ? 127 GLN A O   1 
ATOM   982  C  CB  . GLN A 1 127 ? 5.252  1.971   -0.462  1.00 9.62  ? 127 GLN A CB  1 
ATOM   983  C  CG  . GLN A 1 127 ? 6.530  2.164   -1.199  1.00 11.34 ? 127 GLN A CG  1 
ATOM   984  C  CD  . GLN A 1 127 ? 7.114  0.863   -1.681  1.00 10.86 ? 127 GLN A CD  1 
ATOM   985  O  OE1 . GLN A 1 127 ? 6.658  -0.214  -1.297  1.00 10.39 ? 127 GLN A OE1 1 
ATOM   986  N  NE2 . GLN A 1 127 ? 8.145  0.950   -2.511  1.00 10.44 ? 127 GLN A NE2 1 
ATOM   987  N  N   . CYS A 1 128 ? 7.424  2.775   1.795   1.00 12.45 ? 128 CYS A N   1 
ATOM   988  C  CA  . CYS A 1 128 ? 8.113  3.916   2.394   1.00 13.78 ? 128 CYS A CA  1 
ATOM   989  C  C   . CYS A 1 128 ? 9.598  3.874   2.063   1.00 10.86 ? 128 CYS A C   1 
ATOM   990  O  O   . CYS A 1 128 ? 10.103 2.928   1.456   1.00 11.01 ? 128 CYS A O   1 
ATOM   991  C  CB  . CYS A 1 128 ? 7.899  3.982   3.913   1.00 16.45 ? 128 CYS A CB  1 
ATOM   992  S  SG  . CYS A 1 128 ? 8.643  2.641   4.859   1.00 15.78 ? 128 CYS A SG  1 
ATOM   993  N  N   . ALA A 1 129 ? 10.294 4.929   2.473   1.00 8.85  ? 129 ALA A N   1 
ATOM   994  C  CA  . ALA A 1 129 ? 11.681 5.138   2.096   1.00 9.96  ? 129 ALA A CA  1 
ATOM   995  C  C   . ALA A 1 129 ? 12.577 5.136   3.328   1.00 8.10  ? 129 ALA A C   1 
ATOM   996  O  O   . ALA A 1 129 ? 12.216 5.669   4.376   1.00 10.32 ? 129 ALA A O   1 
ATOM   997  C  CB  . ALA A 1 129 ? 11.834 6.457   1.332   1.00 9.63  ? 129 ALA A CB  1 
ATOM   998  N  N   . MET A 1 130 ? 13.745 4.526   3.201   1.00 10.10 ? 130 MET A N   1 
ATOM   999  C  CA  . MET A 1 130 ? 14.812 4.750   4.170   1.00 10.90 ? 130 MET A CA  1 
ATOM   1000 C  C   . MET A 1 130 ? 15.220 6.216   4.077   1.00 7.83  ? 130 MET A C   1 
ATOM   1001 O  O   . MET A 1 130 ? 15.662 6.671   3.019   1.00 5.58  ? 130 MET A O   1 
ATOM   1002 C  CB  . MET A 1 130 ? 15.971 3.809   3.859   1.00 7.13  ? 130 MET A CB  1 
ATOM   1003 C  CG  . MET A 1 130 ? 17.183 3.873   4.770   1.00 10.65 ? 130 MET A CG  1 
ATOM   1004 S  SD  . MET A 1 130 ? 16.726 3.414   6.449   1.00 11.78 ? 130 MET A SD  1 
ATOM   1005 C  CE  . MET A 1 130 ? 16.929 1.634   6.338   1.00 12.83 ? 130 MET A CE  1 
ATOM   1006 N  N   . ARG A 1 131 ? 15.017 6.982   5.146   1.00 5.90  ? 131 ARG A N   1 
ATOM   1007 C  CA  . ARG A 1 131 ? 15.373 8.396   5.087   1.00 10.13 ? 131 ARG A CA  1 
ATOM   1008 C  C   . ARG A 1 131 ? 16.894 8.551   5.007   1.00 6.62  ? 131 ARG A C   1 
ATOM   1009 O  O   . ARG A 1 131 ? 17.640 7.678   5.455   1.00 6.43  ? 131 ARG A O   1 
ATOM   1010 C  CB  . ARG A 1 131 ? 14.842 9.161   6.307   1.00 7.19  ? 131 ARG A CB  1 
ATOM   1011 C  CG  . ARG A 1 131 ? 13.325 9.193   6.481   1.00 10.18 ? 131 ARG A CG  1 
ATOM   1012 C  CD  . ARG A 1 131 ? 12.547 9.828   5.309   1.00 8.35  ? 131 ARG A CD  1 
ATOM   1013 N  NE  . ARG A 1 131 ? 13.131 11.022  4.703   1.00 8.88  ? 131 ARG A NE  1 
ATOM   1014 C  CZ  . ARG A 1 131 ? 12.778 11.474  3.502   1.00 12.83 ? 131 ARG A CZ  1 
ATOM   1015 N  NH1 . ARG A 1 131 ? 11.874 10.841  2.769   1.00 5.38  ? 131 ARG A NH1 1 
ATOM   1016 N  NH2 . ARG A 1 131 ? 13.352 12.576  3.018   1.00 5.40  ? 131 ARG A NH2 1 
ATOM   1017 N  N   . PRO A 1 132 ? 17.382 9.651   4.434   1.00 8.24  ? 132 PRO A N   1 
ATOM   1018 C  CA  . PRO A 1 132 ? 18.832 9.900   4.471   1.00 8.89  ? 132 PRO A CA  1 
ATOM   1019 C  C   . PRO A 1 132 ? 19.418 9.751   5.860   1.00 9.52  ? 132 PRO A C   1 
ATOM   1020 O  O   . PRO A 1 132 ? 20.582 9.351   5.994   1.00 8.42  ? 132 PRO A O   1 
ATOM   1021 C  CB  . PRO A 1 132 ? 18.947 11.339  3.951   1.00 10.42 ? 132 PRO A CB  1 
ATOM   1022 C  CG  . PRO A 1 132 ? 17.814 11.469  3.012   1.00 8.40  ? 132 PRO A CG  1 
ATOM   1023 C  CD  . PRO A 1 132 ? 16.685 10.619  3.567   1.00 10.35 ? 132 PRO A CD  1 
ATOM   1024 N  N   . ASN A 1 133 ? 18.639 10.015  6.908   1.00 8.00  ? 133 ASN A N   1 
ATOM   1025 C  CA  . ASN A 1 133 ? 19.126 9.851   8.277   1.00 9.33  ? 133 ASN A CA  1 
ATOM   1026 C  C   . ASN A 1 133 ? 18.837 8.469   8.858   1.00 8.14  ? 133 ASN A C   1 
ATOM   1027 O  O   . ASN A 1 133 ? 18.910 8.296   10.074  1.00 6.37  ? 133 ASN A O   1 
ATOM   1028 C  CB  . ASN A 1 133 ? 18.561 10.949  9.187   1.00 9.41  ? 133 ASN A CB  1 
ATOM   1029 C  CG  . ASN A 1 133 ? 17.105 10.727  9.589   1.00 10.27 ? 133 ASN A CG  1 
ATOM   1030 O  OD1 . ASN A 1 133 ? 16.425 9.794   9.143   1.00 8.01  ? 133 ASN A OD1 1 
ATOM   1031 N  ND2 . ASN A 1 133 ? 16.617 11.609  10.440  1.00 11.48 ? 133 ASN A ND2 1 
ATOM   1032 N  N   . PHE A 1 134 ? 18.529 7.482   8.020   1.00 6.66  ? 134 PHE A N   1 
ATOM   1033 C  CA  . PHE A 1 134 ? 18.448 6.074   8.418   1.00 10.53 ? 134 PHE A CA  1 
ATOM   1034 C  C   . PHE A 1 134 ? 17.301 5.777   9.378   1.00 8.98  ? 134 PHE A C   1 
ATOM   1035 O  O   . PHE A 1 134 ? 17.323 4.749   10.058  1.00 10.68 ? 134 PHE A O   1 
ATOM   1036 C  CB  . PHE A 1 134 ? 19.776 5.589   9.019   1.00 6.05  ? 134 PHE A CB  1 
ATOM   1037 C  CG  . PHE A 1 134 ? 20.856 5.412   7.996   1.00 9.81  ? 134 PHE A CG  1 
ATOM   1038 C  CD1 . PHE A 1 134 ? 20.726 4.462   6.999   1.00 7.59  ? 134 PHE A CD1 1 
ATOM   1039 C  CD2 . PHE A 1 134 ? 21.966 6.235   7.993   1.00 12.28 ? 134 PHE A CD2 1 
ATOM   1040 C  CE1 . PHE A 1 134 ? 21.703 4.306   6.048   1.00 15.12 ? 134 PHE A CE1 1 
ATOM   1041 C  CE2 . PHE A 1 134 ? 22.946 6.089   7.056   1.00 11.06 ? 134 PHE A CE2 1 
ATOM   1042 C  CZ  . PHE A 1 134 ? 22.819 5.130   6.072   1.00 18.17 ? 134 PHE A CZ  1 
ATOM   1043 N  N   . THR A 1 135 ? 16.327 6.679   9.480   1.00 6.72  ? 135 THR A N   1 
ATOM   1044 C  CA  . THR A 1 135 ? 15.024 6.382   10.049  1.00 5.82  ? 135 THR A CA  1 
ATOM   1045 C  C   . THR A 1 135 ? 14.060 6.025   8.919   1.00 9.48  ? 135 THR A C   1 
ATOM   1046 O  O   . THR A 1 135 ? 14.352 6.206   7.730   1.00 6.02  ? 135 THR A O   1 
ATOM   1047 C  CB  . THR A 1 135 ? 14.476 7.577   10.845  1.00 8.79  ? 135 THR A CB  1 
ATOM   1048 O  OG1 . THR A 1 135 ? 14.297 8.704   9.977   1.00 10.28 ? 135 THR A OG1 1 
ATOM   1049 C  CG2 . THR A 1 135 ? 15.424 7.955   11.986  1.00 6.12  ? 135 THR A CG2 1 
ATOM   1050 N  N   . ILE A 1 136 ? 12.906 5.484   9.298   1.00 6.65  ? 136 ILE A N   1 
ATOM   1051 C  CA  . ILE A 1 136 ? 11.781 5.376   8.381   1.00 7.36  ? 136 ILE A CA  1 
ATOM   1052 C  C   . ILE A 1 136 ? 10.589 6.027   9.066   1.00 8.55  ? 136 ILE A C   1 
ATOM   1053 O  O   . ILE A 1 136 ? 10.460 5.969   10.293  1.00 7.72  ? 136 ILE A O   1 
ATOM   1054 C  CB  . ILE A 1 136 ? 11.483 3.915   7.955   1.00 11.56 ? 136 ILE A CB  1 
ATOM   1055 C  CG1 . ILE A 1 136 ? 10.576 3.198   8.947   1.00 8.98  ? 136 ILE A CG1 1 
ATOM   1056 C  CG2 . ILE A 1 136 ? 12.788 3.098   7.700   1.00 7.01  ? 136 ILE A CG2 1 
ATOM   1057 C  CD1 . ILE A 1 136 ? 10.134 1.839   8.449   1.00 12.85 ? 136 ILE A CD1 1 
ATOM   1058 N  N   . LYS A 1 137 ? 9.760  6.716   8.283   1.00 9.61  ? 137 LYS A N   1 
ATOM   1059 C  CA  . LYS A 1 137 ? 8.514  7.280   8.802   1.00 8.78  ? 137 LYS A CA  1 
ATOM   1060 C  C   . LYS A 1 137 ? 7.449  6.218   8.575   1.00 11.29 ? 137 LYS A C   1 
ATOM   1061 O  O   . LYS A 1 137 ? 6.817  6.154   7.518   1.00 10.93 ? 137 LYS A O   1 
ATOM   1062 C  CB  . LYS A 1 137 ? 8.181  8.598   8.115   1.00 12.26 ? 137 LYS A CB  1 
ATOM   1063 C  CG  . LYS A 1 137 ? 9.357  9.578   8.008   1.00 13.89 ? 137 LYS A CG  1 
ATOM   1064 C  CD  . LYS A 1 137 ? 8.862  11.029  8.006   1.00 20.05 ? 137 LYS A CD  1 
ATOM   1065 C  CE  . LYS A 1 137 ? 9.944  12.009  7.536   1.00 18.43 ? 137 LYS A CE  1 
ATOM   1066 N  NZ  . LYS A 1 137 ? 10.640 12.635  8.702   1.00 19.61 ? 137 LYS A NZ  1 
ATOM   1067 N  N   . GLY A 1 138 ? 7.264  5.349   9.569   1.00 8.85  ? 138 GLY A N   1 
ATOM   1068 C  CA  . GLY A 1 138 ? 6.360  4.230   9.453   1.00 5.50  ? 138 GLY A CA  1 
ATOM   1069 C  C   . GLY A 1 138 ? 4.996  4.505   10.056  1.00 9.68  ? 138 GLY A C   1 
ATOM   1070 O  O   . GLY A 1 138 ? 4.655  5.624   10.447  1.00 16.54 ? 138 GLY A O   1 
ATOM   1071 N  N   . SER A 1 139 ? 4.198  3.450   10.118  1.00 8.46  ? 139 SER A N   1 
ATOM   1072 C  CA  . SER A 1 139 ? 2.989  3.423   10.933  1.00 9.56  ? 139 SER A CA  1 
ATOM   1073 C  C   . SER A 1 139 ? 3.076  2.117   11.712  1.00 8.34  ? 139 SER A C   1 
ATOM   1074 O  O   . SER A 1 139 ? 2.854  1.044   11.151  1.00 9.24  ? 139 SER A O   1 
ATOM   1075 C  CB  . SER A 1 139 ? 1.721  3.513   10.090  1.00 7.50  ? 139 SER A CB  1 
ATOM   1076 O  OG  . SER A 1 139 ? 0.605  2.989   10.808  1.00 13.71 ? 139 SER A OG  1 
ATOM   1077 N  N   . PHE A 1 140 ? 3.424  2.216   12.996  1.00 8.53  ? 140 PHE A N   1 
ATOM   1078 C  CA  . PHE A 1 140 ? 3.737  1.083   13.854  1.00 11.62 ? 140 PHE A CA  1 
ATOM   1079 C  C   . PHE A 1 140 ? 3.182  1.346   15.248  1.00 11.22 ? 140 PHE A C   1 
ATOM   1080 O  O   . PHE A 1 140 ? 3.359  2.442   15.785  1.00 12.90 ? 140 PHE A O   1 
ATOM   1081 C  CB  . PHE A 1 140 ? 5.263  0.872   13.972  1.00 7.82  ? 140 PHE A CB  1 
ATOM   1082 C  CG  . PHE A 1 140 ? 5.896  0.217   12.778  1.00 11.46 ? 140 PHE A CG  1 
ATOM   1083 C  CD1 . PHE A 1 140 ? 5.436  -1.004  12.314  1.00 5.98  ? 140 PHE A CD1 1 
ATOM   1084 C  CD2 . PHE A 1 140 ? 6.978  0.809   12.140  1.00 11.51 ? 140 PHE A CD2 1 
ATOM   1085 C  CE1 . PHE A 1 140 ? 6.037  -1.618  11.241  1.00 7.71  ? 140 PHE A CE1 1 
ATOM   1086 C  CE2 . PHE A 1 140 ? 7.578  0.193   11.046  1.00 5.74  ? 140 PHE A CE2 1 
ATOM   1087 C  CZ  . PHE A 1 140 ? 7.115  -1.016  10.609  1.00 5.09  ? 140 PHE A CZ  1 
ATOM   1088 N  N   . LEU A 1 141 ? 2.525  0.349   15.832  1.00 10.80 ? 141 LEU A N   1 
ATOM   1089 C  CA  . LEU A 1 141 ? 2.078  0.410   17.219  1.00 11.58 ? 141 LEU A CA  1 
ATOM   1090 C  C   . LEU A 1 141 ? 2.858  -0.593  18.060  1.00 11.29 ? 141 LEU A C   1 
ATOM   1091 O  O   . LEU A 1 141 ? 3.594  -1.431  17.538  1.00 11.82 ? 141 LEU A O   1 
ATOM   1092 C  CB  . LEU A 1 141 ? 0.569  0.152   17.313  1.00 13.66 ? 141 LEU A CB  1 
ATOM   1093 C  CG  . LEU A 1 141 ? -0.320 1.099   16.480  1.00 16.95 ? 141 LEU A CG  1 
ATOM   1094 C  CD1 . LEU A 1 141 ? -1.762 0.640   16.513  1.00 19.44 ? 141 LEU A CD1 1 
ATOM   1095 C  CD2 . LEU A 1 141 ? -0.217 2.534   16.992  1.00 15.00 ? 141 LEU A CD2 1 
ATOM   1096 N  N   . ASN A 1 142 ? 2.716  -0.497  19.385  1.00 13.73 ? 142 ASN A N   1 
ATOM   1097 C  CA  . ASN A 1 142 ? 3.355  -1.490  20.244  1.00 12.19 ? 142 ASN A CA  1 
ATOM   1098 C  C   . ASN A 1 142 ? 2.908  -2.886  19.839  1.00 14.05 ? 142 ASN A C   1 
ATOM   1099 O  O   . ASN A 1 142 ? 1.715  -3.131  19.625  1.00 12.00 ? 142 ASN A O   1 
ATOM   1100 C  CB  . ASN A 1 142 ? 3.016  -1.250  21.719  1.00 13.70 ? 142 ASN A CB  1 
ATOM   1101 C  CG  . ASN A 1 142 ? 3.753  -2.200  22.644  1.00 13.92 ? 142 ASN A CG  1 
ATOM   1102 O  OD1 . ASN A 1 142 ? 3.782  -3.413  22.420  1.00 22.50 ? 142 ASN A OD1 1 
ATOM   1103 N  ND2 . ASN A 1 142 ? 4.333  -1.659  23.707  1.00 28.03 ? 142 ASN A ND2 1 
ATOM   1104 N  N   . GLY A 1 143 ? 3.873  -3.812  19.754  1.00 7.69  ? 143 GLY A N   1 
ATOM   1105 C  CA  . GLY A 1 143 ? 3.613  -5.147  19.256  1.00 8.92  ? 143 GLY A CA  1 
ATOM   1106 C  C   . GLY A 1 143 ? 4.033  -5.388  17.816  1.00 7.07  ? 143 GLY A C   1 
ATOM   1107 O  O   . GLY A 1 143 ? 4.007  -6.537  17.362  1.00 10.96 ? 143 GLY A O   1 
ATOM   1108 N  N   . SER A 1 144 ? 4.433  -4.353  17.096  1.00 4.47  ? 144 SER A N   1 
ATOM   1109 C  CA  . SER A 1 144 ? 4.821  -4.489  15.702  1.00 9.32  ? 144 SER A CA  1 
ATOM   1110 C  C   . SER A 1 144 ? 6.275  -4.894  15.516  1.00 7.66  ? 144 SER A C   1 
ATOM   1111 O  O   . SER A 1 144 ? 6.687  -5.141  14.377  1.00 6.63  ? 144 SER A O   1 
ATOM   1112 C  CB  . SER A 1 144 ? 4.582  -3.176  14.966  1.00 6.45  ? 144 SER A CB  1 
ATOM   1113 O  OG  . SER A 1 144 ? 5.399  -2.184  15.543  1.00 10.08 ? 144 SER A OG  1 
ATOM   1114 N  N   . CYS A 1 145 ? 7.054  -4.987  16.594  1.00 4.25  ? 145 CYS A N   1 
ATOM   1115 C  CA  . CYS A 1 145 ? 8.456  -5.365  16.468  1.00 4.43  ? 145 CYS A CA  1 
ATOM   1116 C  C   . CYS A 1 145 ? 8.601  -6.732  15.808  1.00 4.03  ? 145 CYS A C   1 
ATOM   1117 O  O   . CYS A 1 145 ? 7.821  -7.656  16.060  1.00 4.78  ? 145 CYS A O   1 
ATOM   1118 C  CB  . CYS A 1 145 ? 9.131  -5.344  17.839  1.00 7.86  ? 145 CYS A CB  1 
ATOM   1119 S  SG  . CYS A 1 145 ? 9.220  -3.669  18.502  1.00 16.46 ? 145 CYS A SG  1 
ATOM   1120 N  N   . GLY A 1 146 ? 9.601  -6.848  14.934  1.00 4.18  ? 146 GLY A N   1 
ATOM   1121 C  CA  . GLY A 1 146 ? 9.777  -8.028  14.110  1.00 4.44  ? 146 GLY A CA  1 
ATOM   1122 C  C   . GLY A 1 146 ? 9.100  -7.970  12.756  1.00 4.49  ? 146 GLY A C   1 
ATOM   1123 O  O   . GLY A 1 146 ? 9.381  -8.822  11.904  1.00 5.45  ? 146 GLY A O   1 
ATOM   1124 N  N   . SER A 1 147 ? 8.211  -7.006  12.529  1.00 4.72  ? 147 SER A N   1 
ATOM   1125 C  CA  . SER A 1 147 ? 7.738  -6.759  11.178  1.00 5.55  ? 147 SER A CA  1 
ATOM   1126 C  C   . SER A 1 147 ? 8.922  -6.427  10.281  1.00 6.42  ? 147 SER A C   1 
ATOM   1127 O  O   . SER A 1 147 ? 9.946  -5.910  10.737  1.00 5.32  ? 147 SER A O   1 
ATOM   1128 C  CB  . SER A 1 147 ? 6.727  -5.615  11.176  1.00 6.32  ? 147 SER A CB  1 
ATOM   1129 O  OG  . SER A 1 147 ? 5.747  -5.834  12.170  1.00 5.95  ? 147 SER A OG  1 
ATOM   1130 N  N   . VAL A 1 148 ? 8.783  -6.714  8.987   1.00 4.10  ? 148 VAL A N   1 
ATOM   1131 C  CA  . VAL A 1 148 ? 9.917  -6.608  8.082   1.00 4.49  ? 148 VAL A CA  1 
ATOM   1132 C  C   . VAL A 1 148 ? 9.530  -5.791  6.859   1.00 5.34  ? 148 VAL A C   1 
ATOM   1133 O  O   . VAL A 1 148 ? 8.361  -5.728  6.464   1.00 3.71  ? 148 VAL A O   1 
ATOM   1134 C  CB  . VAL A 1 148 ? 10.459 -8.003  7.676   1.00 4.83  ? 148 VAL A CB  1 
ATOM   1135 C  CG1 . VAL A 1 148 ? 10.674 -8.860  8.899   1.00 5.40  ? 148 VAL A CG1 1 
ATOM   1136 C  CG2 . VAL A 1 148 ? 9.541  -8.707  6.651   1.00 7.31  ? 148 VAL A CG2 1 
ATOM   1137 N  N   . GLY A 1 149 ? 10.535 -5.129  6.284   1.00 5.49  ? 149 GLY A N   1 
ATOM   1138 C  CA  . GLY A 1 149 ? 10.431 -4.529  4.977   1.00 4.46  ? 149 GLY A CA  1 
ATOM   1139 C  C   . GLY A 1 149 ? 11.162 -5.359  3.941   1.00 5.95  ? 149 GLY A C   1 
ATOM   1140 O  O   . GLY A 1 149 ? 12.049 -6.162  4.254   1.00 2.95  ? 149 GLY A O   1 
ATOM   1141 N  N   . PHE A 1 150 ? 10.789 -5.145  2.683   1.00 4.88  ? 150 PHE A N   1 
ATOM   1142 C  CA  . PHE A 1 150 ? 11.218 -6.061  1.638   1.00 4.51  ? 150 PHE A CA  1 
ATOM   1143 C  C   . PHE A 1 150 ? 10.934 -5.425  0.290   1.00 4.83  ? 150 PHE A C   1 
ATOM   1144 O  O   . PHE A 1 150 ? 10.058 -4.562  0.158   1.00 3.86  ? 150 PHE A O   1 
ATOM   1145 C  CB  . PHE A 1 150 ? 10.487 -7.405  1.740   1.00 4.17  ? 150 PHE A CB  1 
ATOM   1146 C  CG  . PHE A 1 150 ? 9.010  -7.274  1.621   1.00 3.83  ? 150 PHE A CG  1 
ATOM   1147 C  CD1 . PHE A 1 150 ? 8.242  -6.984  2.737   1.00 6.19  ? 150 PHE A CD1 1 
ATOM   1148 C  CD2 . PHE A 1 150 ? 8.389  -7.370  0.395   1.00 5.11  ? 150 PHE A CD2 1 
ATOM   1149 C  CE1 . PHE A 1 150 ? 6.867  -6.838  2.638   1.00 5.55  ? 150 PHE A CE1 1 
ATOM   1150 C  CE2 . PHE A 1 150 ? 7.006  -7.229  0.279   1.00 4.82  ? 150 PHE A CE2 1 
ATOM   1151 C  CZ  . PHE A 1 150 ? 6.250  -6.965  1.405   1.00 7.68  ? 150 PHE A CZ  1 
ATOM   1152 N  N   . ASN A 1 151 ? 11.693 -5.867  -0.703  1.00 5.31  ? 151 ASN A N   1 
ATOM   1153 C  CA  . ASN A 1 151 ? 11.398 -5.644  -2.108  1.00 8.63  ? 151 ASN A CA  1 
ATOM   1154 C  C   . ASN A 1 151 ? 11.307 -7.009  -2.792  1.00 11.51 ? 151 ASN A C   1 
ATOM   1155 O  O   . ASN A 1 151 ? 11.814 -8.011  -2.274  1.00 11.61 ? 151 ASN A O   1 
ATOM   1156 C  CB  . ASN A 1 151 ? 12.476 -4.770  -2.759  1.00 11.23 ? 151 ASN A CB  1 
ATOM   1157 C  CG  . ASN A 1 151 ? 12.363 -3.296  -2.374  1.00 11.95 ? 151 ASN A CG  1 
ATOM   1158 O  OD1 . ASN A 1 151 ? 11.512 -2.560  -2.894  1.00 10.66 ? 151 ASN A OD1 1 
ATOM   1159 N  ND2 . ASN A 1 151 ? 13.236 -2.853  -1.474  1.00 10.15 ? 151 ASN A ND2 1 
ATOM   1160 N  N   . ILE A 1 152 ? 10.646 -7.060  -3.950  1.00 11.89 ? 152 ILE A N   1 
ATOM   1161 C  CA  . ILE A 1 152 ? 10.430 -8.311  -4.674  1.00 16.78 ? 152 ILE A CA  1 
ATOM   1162 C  C   . ILE A 1 152 ? 10.734 -8.093  -6.145  1.00 21.07 ? 152 ILE A C   1 
ATOM   1163 O  O   . ILE A 1 152 ? 10.244 -7.134  -6.748  1.00 18.98 ? 152 ILE A O   1 
ATOM   1164 C  CB  . ILE A 1 152 ? 8.994  -8.844  -4.518  1.00 18.81 ? 152 ILE A CB  1 
ATOM   1165 C  CG1 . ILE A 1 152 ? 8.606  -8.973  -3.048  1.00 13.28 ? 152 ILE A CG1 1 
ATOM   1166 C  CG2 . ILE A 1 152 ? 8.855  -10.209 -5.236  1.00 19.57 ? 152 ILE A CG2 1 
ATOM   1167 C  CD1 . ILE A 1 152 ? 7.276  -9.711  -2.841  1.00 9.37  ? 152 ILE A CD1 1 
ATOM   1168 N  N   . ASP A 1 153 ? 11.517 -8.998  -6.727  1.00 24.70 ? 153 ASP A N   1 
ATOM   1169 C  CA  . ASP A 1 153 ? 11.931 -8.920  -8.129  1.00 26.27 ? 153 ASP A CA  1 
ATOM   1170 C  C   . ASP A 1 153 ? 11.617 -10.274 -8.762  1.00 24.59 ? 153 ASP A C   1 
ATOM   1171 O  O   . ASP A 1 153 ? 12.324 -11.259 -8.530  1.00 24.81 ? 153 ASP A O   1 
ATOM   1172 C  CB  . ASP A 1 153 ? 13.415 -8.558  -8.245  1.00 24.74 ? 153 ASP A CB  1 
ATOM   1173 C  CG  . ASP A 1 153 ? 13.753 -7.222  -7.558  1.00 32.32 ? 153 ASP A CG  1 
ATOM   1174 O  OD1 . ASP A 1 153 ? 14.281 -7.245  -6.418  1.00 32.91 ? 153 ASP A OD1 1 
ATOM   1175 O  OD2 . ASP A 1 153 ? 13.463 -6.145  -8.141  1.00 35.75 ? 153 ASP A OD2 1 
ATOM   1176 N  N   . TYR A 1 154 ? 10.545 -10.324 -9.548  1.00 29.93 ? 154 TYR A N   1 
ATOM   1177 C  CA  . TYR A 1 154 ? 10.007 -11.575 -10.064 1.00 32.79 ? 154 TYR A CA  1 
ATOM   1178 C  C   . TYR A 1 154 ? 9.517  -12.456 -8.925  1.00 32.36 ? 154 TYR A C   1 
ATOM   1179 O  O   . TYR A 1 154 ? 8.424  -12.253 -8.384  1.00 40.92 ? 154 TYR A O   1 
ATOM   1180 C  CB  . TYR A 1 154 ? 11.053 -12.330 -10.884 1.00 39.29 ? 154 TYR A CB  1 
ATOM   1181 C  CG  . TYR A 1 154 ? 10.469 -13.422 -11.767 1.00 47.36 ? 154 TYR A CG  1 
ATOM   1182 C  CD1 . TYR A 1 154 ? 9.170  -13.326 -12.257 1.00 50.52 ? 154 TYR A CD1 1 
ATOM   1183 C  CD2 . TYR A 1 154 ? 11.212 -14.559 -12.092 1.00 47.92 ? 154 TYR A CD2 1 
ATOM   1184 C  CE1 . TYR A 1 154 ? 8.632  -14.317 -13.060 1.00 56.93 ? 154 TYR A CE1 1 
ATOM   1185 C  CE2 . TYR A 1 154 ? 10.681 -15.560 -12.891 1.00 53.84 ? 154 TYR A CE2 1 
ATOM   1186 C  CZ  . TYR A 1 154 ? 9.388  -15.433 -13.375 1.00 63.66 ? 154 TYR A CZ  1 
ATOM   1187 O  OH  . TYR A 1 154 ? 8.843  -16.416 -14.176 1.00 60.80 ? 154 TYR A OH  1 
ATOM   1188 N  N   . ASP A 1 155 ? 10.326 -13.441 -8.561  1.00 25.28 ? 155 ASP A N   1 
ATOM   1189 C  CA  . ASP A 1 155 ? 9.984  -14.379 -7.503  1.00 29.43 ? 155 ASP A CA  1 
ATOM   1190 C  C   . ASP A 1 155 ? 10.901 -14.279 -6.285  1.00 22.15 ? 155 ASP A C   1 
ATOM   1191 O  O   . ASP A 1 155 ? 10.705 -15.030 -5.323  1.00 18.81 ? 155 ASP A O   1 
ATOM   1192 C  CB  . ASP A 1 155 ? 9.994  -15.808 -8.067  1.00 28.45 ? 155 ASP A CB  1 
ATOM   1193 C  CG  . ASP A 1 155 ? 11.373 -16.222 -8.587  1.00 31.65 ? 155 ASP A CG  1 
ATOM   1194 O  OD1 . ASP A 1 155 ? 11.902 -15.525 -9.485  1.00 32.10 ? 155 ASP A OD1 1 
ATOM   1195 O  OD2 . ASP A 1 155 ? 11.918 -17.242 -8.113  1.00 26.66 ? 155 ASP A OD2 1 
ATOM   1196 N  N   . CYS A 1 156 ? 11.881 -13.369 -6.284  1.00 18.47 ? 156 CYS A N   1 
ATOM   1197 C  CA  . CYS A 1 156 ? 12.865 -13.292 -5.207  1.00 17.66 ? 156 CYS A CA  1 
ATOM   1198 C  C   . CYS A 1 156 ? 12.530 -12.142 -4.258  1.00 19.86 ? 156 CYS A C   1 
ATOM   1199 O  O   . CYS A 1 156 ? 12.532 -10.967 -4.664  1.00 11.90 ? 156 CYS A O   1 
ATOM   1200 C  CB  . CYS A 1 156 ? 14.288 -13.131 -5.746  1.00 13.49 ? 156 CYS A CB  1 
ATOM   1201 S  SG  . CYS A 1 156 ? 15.548 -13.204 -4.407  1.00 18.16 ? 156 CYS A SG  1 
ATOM   1202 N  N   . VAL A 1 157 ? 12.247 -12.488 -2.992  1.00 13.81 ? 157 VAL A N   1 
ATOM   1203 C  CA  . VAL A 1 157 ? 12.044 -11.491 -1.948  1.00 10.06 ? 157 VAL A CA  1 
ATOM   1204 C  C   . VAL A 1 157 ? 13.402 -11.064 -1.410  1.00 10.36 ? 157 VAL A C   1 
ATOM   1205 O  O   . VAL A 1 157 ? 14.203 -11.906 -0.994  1.00 10.70 ? 157 VAL A O   1 
ATOM   1206 C  CB  . VAL A 1 157 ? 11.159 -12.043 -0.817  1.00 8.75  ? 157 VAL A CB  1 
ATOM   1207 C  CG1 . VAL A 1 157 ? 10.915 -10.945 0.256   1.00 5.27  ? 157 VAL A CG1 1 
ATOM   1208 C  CG2 . VAL A 1 157 ? 9.835  -12.587 -1.370  1.00 9.19  ? 157 VAL A CG2 1 
ATOM   1209 N  N   . SER A 1 158 ? 13.668 -9.756  -1.411  1.00 10.66 ? 158 SER A N   1 
ATOM   1210 C  CA  . SER A 1 158 ? 14.879 -9.205  -0.799  1.00 7.97  ? 158 SER A CA  1 
ATOM   1211 C  C   . SER A 1 158 ? 14.468 -8.529  0.499   1.00 5.76  ? 158 SER A C   1 
ATOM   1212 O  O   . SER A 1 158 ? 13.956 -7.408  0.481   1.00 4.03  ? 158 SER A O   1 
ATOM   1213 C  CB  . SER A 1 158 ? 15.582 -8.222  -1.725  1.00 9.13  ? 158 SER A CB  1 
ATOM   1214 O  OG  . SER A 1 158 ? 16.359 -8.890  -2.683  1.00 15.29 ? 158 SER A OG  1 
ATOM   1215 N  N   . PHE A 1 159 ? 14.675 -9.223  1.623   1.00 6.37  ? 159 PHE A N   1 
ATOM   1216 C  CA  . PHE A 1 159 ? 14.412 -8.648  2.937   1.00 6.80  ? 159 PHE A CA  1 
ATOM   1217 C  C   . PHE A 1 159 ? 15.502 -7.647  3.284   1.00 5.27  ? 159 PHE A C   1 
ATOM   1218 O  O   . PHE A 1 159 ? 16.691 -7.986  3.302   1.00 6.10  ? 159 PHE A O   1 
ATOM   1219 C  CB  . PHE A 1 159 ? 14.358 -9.734  4.020   1.00 6.48  ? 159 PHE A CB  1 
ATOM   1220 C  CG  . PHE A 1 159 ? 13.252 -10.732 3.831   1.00 6.77  ? 159 PHE A CG  1 
ATOM   1221 C  CD1 . PHE A 1 159 ? 11.970 -10.452 4.274   1.00 4.52  ? 159 PHE A CD1 1 
ATOM   1222 C  CD2 . PHE A 1 159 ? 13.497 -11.945 3.208   1.00 4.38  ? 159 PHE A CD2 1 
ATOM   1223 C  CE1 . PHE A 1 159 ? 10.955 -11.377 4.106   1.00 5.13  ? 159 PHE A CE1 1 
ATOM   1224 C  CE2 . PHE A 1 159 ? 12.480 -12.875 3.029   1.00 7.43  ? 159 PHE A CE2 1 
ATOM   1225 C  CZ  . PHE A 1 159 ? 11.209 -12.589 3.475   1.00 4.99  ? 159 PHE A CZ  1 
ATOM   1226 N  N   . CYS A 1 160 ? 15.095 -6.427  3.610   1.00 4.40  ? 160 CYS A N   1 
ATOM   1227 C  CA  . CYS A 1 160 ? 16.044 -5.384  3.957   1.00 5.88  ? 160 CYS A CA  1 
ATOM   1228 C  C   . CYS A 1 160 ? 15.806 -4.745  5.317   1.00 5.77  ? 160 CYS A C   1 
ATOM   1229 O  O   . CYS A 1 160 ? 16.672 -4.000  5.782   1.00 8.33  ? 160 CYS A O   1 
ATOM   1230 C  CB  . CYS A 1 160 ? 16.038 -4.278  2.889   1.00 4.74  ? 160 CYS A CB  1 
ATOM   1231 S  SG  . CYS A 1 160 ? 14.417 -3.491  2.688   1.00 7.62  ? 160 CYS A SG  1 
ATOM   1232 N  N   . TYR A 1 161 ? 14.683 -5.001  5.978   1.00 4.59  ? 161 TYR A N   1 
ATOM   1233 C  CA  . TYR A 1 161 ? 14.405 -4.241  7.185   1.00 4.17  ? 161 TYR A CA  1 
ATOM   1234 C  C   . TYR A 1 161 ? 13.635 -5.094  8.171   1.00 3.51  ? 161 TYR A C   1 
ATOM   1235 O  O   . TYR A 1 161 ? 12.680 -5.769  7.793   1.00 4.91  ? 161 TYR A O   1 
ATOM   1236 C  CB  . TYR A 1 161 ? 13.607 -2.962  6.870   1.00 4.42  ? 161 TYR A CB  1 
ATOM   1237 C  CG  . TYR A 1 161 ? 13.269 -2.125  8.081   1.00 4.55  ? 161 TYR A CG  1 
ATOM   1238 C  CD1 . TYR A 1 161 ? 14.187 -1.204  8.592   1.00 4.32  ? 161 TYR A CD1 1 
ATOM   1239 C  CD2 . TYR A 1 161 ? 12.022 -2.227  8.701   1.00 3.25  ? 161 TYR A CD2 1 
ATOM   1240 C  CE1 . TYR A 1 161 ? 13.880 -0.425  9.693   1.00 2.97  ? 161 TYR A CE1 1 
ATOM   1241 C  CE2 . TYR A 1 161 ? 11.710 -1.470  9.800   1.00 1.20  ? 161 TYR A CE2 1 
ATOM   1242 C  CZ  . TYR A 1 161 ? 12.633 -0.566  10.296  1.00 4.57  ? 161 TYR A CZ  1 
ATOM   1243 O  OH  . TYR A 1 161 ? 12.325 0.218   11.393  1.00 4.40  ? 161 TYR A OH  1 
ATOM   1244 N  N   . MET A 1 162 ? 14.042 -5.035  9.443   1.00 4.23  ? 162 MET A N   1 
ATOM   1245 C  CA  . MET A 1 162 ? 13.248 -5.585  10.532  1.00 4.01  ? 162 MET A CA  1 
ATOM   1246 C  C   . MET A 1 162 ? 13.063 -4.494  11.584  1.00 4.31  ? 162 MET A C   1 
ATOM   1247 O  O   . MET A 1 162 ? 14.013 -3.761  11.926  1.00 1.56  ? 162 MET A O   1 
ATOM   1248 C  CB  . MET A 1 162 ? 13.895 -6.861  11.110  1.00 2.71  ? 162 MET A CB  1 
ATOM   1249 C  CG  . MET A 1 162 ? 13.410 -7.243  12.511  1.00 2.98  ? 162 MET A CG  1 
ATOM   1250 S  SD  . MET A 1 162 ? 13.854 -8.910  13.000  1.00 8.78  ? 162 MET A SD  1 
ATOM   1251 C  CE  . MET A 1 162 ? 13.083 -9.862  11.703  1.00 8.12  ? 162 MET A CE  1 
ATOM   1252 N  N   . HIS A 1 163 ? 11.823 -4.334  12.034  1.00 2.46  ? 163 HIS A N   1 
ATOM   1253 C  CA  . HIS A 1 163 ? 11.461 -3.198  12.878  1.00 4.01  ? 163 HIS A CA  1 
ATOM   1254 C  C   . HIS A 1 163 ? 11.796 -3.463  14.343  1.00 2.94  ? 163 HIS A C   1 
ATOM   1255 O  O   . HIS A 1 163 ? 11.397 -4.495  14.902  1.00 1.22  ? 163 HIS A O   1 
ATOM   1256 C  CB  . HIS A 1 163 ? 9.971  -2.891  12.729  1.00 3.86  ? 163 HIS A CB  1 
ATOM   1257 C  CG  . HIS A 1 163 ? 9.534  -1.698  13.510  1.00 4.82  ? 163 HIS A CG  1 
ATOM   1258 N  ND1 . HIS A 1 163 ? 10.229 -0.511  13.491  1.00 5.16  ? 163 HIS A ND1 1 
ATOM   1259 C  CD2 . HIS A 1 163 ? 8.497  -1.513  14.358  1.00 7.10  ? 163 HIS A CD2 1 
ATOM   1260 C  CE1 . HIS A 1 163 ? 9.626  0.363   14.275  1.00 4.95  ? 163 HIS A CE1 1 
ATOM   1261 N  NE2 . HIS A 1 163 ? 8.571  -0.219  14.811  1.00 6.82  ? 163 HIS A NE2 1 
ATOM   1262 N  N   . HIS A 1 164 ? 12.522 -2.517  14.971  1.00 2.62  ? 164 HIS A N   1 
ATOM   1263 C  CA  . HIS A 1 164 ? 12.948 -2.659  16.362  1.00 5.67  ? 164 HIS A CA  1 
ATOM   1264 C  C   . HIS A 1 164 ? 12.353 -1.644  17.316  1.00 6.82  ? 164 HIS A C   1 
ATOM   1265 O  O   . HIS A 1 164 ? 12.120 -1.993  18.468  1.00 9.00  ? 164 HIS A O   1 
ATOM   1266 C  CB  . HIS A 1 164 ? 14.481 -2.574  16.513  1.00 3.06  ? 164 HIS A CB  1 
ATOM   1267 C  CG  . HIS A 1 164 ? 15.198 -3.851  16.183  1.00 2.79  ? 164 HIS A CG  1 
ATOM   1268 N  ND1 . HIS A 1 164 ? 15.231 -4.376  14.907  1.00 3.70  ? 164 HIS A ND1 1 
ATOM   1269 C  CD2 . HIS A 1 164 ? 15.914 -4.699  16.957  1.00 2.21  ? 164 HIS A CD2 1 
ATOM   1270 C  CE1 . HIS A 1 164 ? 15.933 -5.497  14.914  1.00 4.80  ? 164 HIS A CE1 1 
ATOM   1271 N  NE2 . HIS A 1 164 ? 16.354 -5.714  16.147  1.00 5.61  ? 164 HIS A NE2 1 
ATOM   1272 N  N   . MET A 1 165 ? 12.116 -0.403  16.908  1.00 7.41  ? 165 MET A N   1 
ATOM   1273 C  CA  . MET A 1 165 ? 11.709 0.530   17.946  1.00 9.67  ? 165 MET A CA  1 
ATOM   1274 C  C   . MET A 1 165 ? 11.178 1.822   17.344  1.00 8.94  ? 165 MET A C   1 
ATOM   1275 O  O   . MET A 1 165 ? 11.363 2.119   16.161  1.00 4.96  ? 165 MET A O   1 
ATOM   1276 C  CB  . MET A 1 165 ? 12.861 0.809   18.924  1.00 8.92  ? 165 MET A CB  1 
ATOM   1277 C  CG  . MET A 1 165 ? 14.092 1.436   18.316  1.00 9.80  ? 165 MET A CG  1 
ATOM   1278 S  SD  . MET A 1 165 ? 15.472 1.477   19.515  1.00 17.59 ? 165 MET A SD  1 
ATOM   1279 C  CE  . MET A 1 165 ? 16.709 2.296   18.507  1.00 10.81 ? 165 MET A CE  1 
ATOM   1280 N  N   . GLU A 1 166 ? 10.496 2.580   18.196  1.00 7.30  ? 166 GLU A N   1 
ATOM   1281 C  CA  . GLU A 1 166 ? 10.035 3.921   17.882  1.00 8.45  ? 166 GLU A CA  1 
ATOM   1282 C  C   . GLU A 1 166 ? 10.765 4.907   18.786  1.00 10.13 ? 166 GLU A C   1 
ATOM   1283 O  O   . GLU A 1 166 ? 10.816 4.717   20.007  1.00 7.43  ? 166 GLU A O   1 
ATOM   1284 C  CB  . GLU A 1 166 ? 8.524  4.024   18.064  1.00 7.64  ? 166 GLU A CB  1 
ATOM   1285 C  CG  . GLU A 1 166 ? 7.920  5.353   17.607  1.00 9.15  ? 166 GLU A CG  1 
ATOM   1286 C  CD  . GLU A 1 166 ? 6.401  5.340   17.633  1.00 13.17 ? 166 GLU A CD  1 
ATOM   1287 O  OE1 . GLU A 1 166 ? 5.780  4.673   16.779  1.00 9.43  ? 166 GLU A OE1 1 
ATOM   1288 O  OE2 . GLU A 1 166 ? 5.819  6.002   18.515  1.00 21.26 ? 166 GLU A OE2 1 
ATOM   1289 N  N   . LEU A 1 167 ? 11.346 5.930   18.184  1.00 8.50  ? 167 LEU A N   1 
ATOM   1290 C  CA  . LEU A 1 167 ? 12.076 6.949   18.913  1.00 11.19 ? 167 LEU A CA  1 
ATOM   1291 C  C   . LEU A 1 167 ? 11.096 7.918   19.561  1.00 12.93 ? 167 LEU A C   1 
ATOM   1292 O  O   . LEU A 1 167 ? 9.926  7.990   19.168  1.00 8.19  ? 167 LEU A O   1 
ATOM   1293 C  CB  . LEU A 1 167 ? 13.012 7.703   17.971  1.00 10.65 ? 167 LEU A CB  1 
ATOM   1294 C  CG  . LEU A 1 167 ? 13.894 6.833   17.081  1.00 13.53 ? 167 LEU A CG  1 
ATOM   1295 C  CD1 . LEU A 1 167 ? 14.909 7.665   16.294  1.00 16.99 ? 167 LEU A CD1 1 
ATOM   1296 C  CD2 . LEU A 1 167 ? 14.583 5.787   17.926  1.00 15.36 ? 167 LEU A CD2 1 
ATOM   1297 N  N   . PRO A 1 168 ? 11.541 8.658   20.582  1.00 13.45 ? 168 PRO A N   1 
ATOM   1298 C  CA  . PRO A 1 168 ? 10.636 9.617   21.231  1.00 9.30  ? 168 PRO A CA  1 
ATOM   1299 C  C   . PRO A 1 168 ? 9.995  10.599  20.259  1.00 11.85 ? 168 PRO A C   1 
ATOM   1300 O  O   . PRO A 1 168 ? 8.926  11.136  20.561  1.00 16.47 ? 168 PRO A O   1 
ATOM   1301 C  CB  . PRO A 1 168 ? 11.530 10.327  22.260  1.00 17.67 ? 168 PRO A CB  1 
ATOM   1302 C  CG  . PRO A 1 168 ? 12.826 9.530   22.326  1.00 16.50 ? 168 PRO A CG  1 
ATOM   1303 C  CD  . PRO A 1 168 ? 12.736 8.362   21.390  1.00 12.60 ? 168 PRO A CD  1 
ATOM   1304 N  N   . THR A 1 169 ? 10.590 10.806  19.080  1.00 12.65 ? 169 THR A N   1 
ATOM   1305 C  CA  . THR A 1 169 ? 10.025 11.684  18.057  1.00 10.75 ? 169 THR A CA  1 
ATOM   1306 C  C   . THR A 1 169 ? 8.961  11.012  17.188  1.00 14.09 ? 169 THR A C   1 
ATOM   1307 O  O   . THR A 1 169 ? 8.398  11.674  16.312  1.00 15.46 ? 169 THR A O   1 
ATOM   1308 C  CB  . THR A 1 169 ? 11.135 12.221  17.160  1.00 12.99 ? 169 THR A CB  1 
ATOM   1309 O  OG1 . THR A 1 169 ? 11.905 11.126  16.640  1.00 16.28 ? 169 THR A OG1 1 
ATOM   1310 C  CG2 . THR A 1 169 ? 12.062 13.090  17.982  1.00 16.09 ? 169 THR A CG2 1 
ATOM   1311 N  N   . GLY A 1 170 ? 8.649  9.737   17.402  1.00 12.90 ? 170 GLY A N   1 
ATOM   1312 C  CA  . GLY A 1 170 ? 7.626  9.084   16.614  1.00 11.23 ? 170 GLY A CA  1 
ATOM   1313 C  C   . GLY A 1 170 ? 8.110  8.484   15.316  1.00 12.45 ? 170 GLY A C   1 
ATOM   1314 O  O   . GLY A 1 170 ? 7.284  8.031   14.518  1.00 13.01 ? 170 GLY A O   1 
ATOM   1315 N  N   . VAL A 1 171 ? 9.416  8.455   15.080  1.00 13.50 ? 171 VAL A N   1 
ATOM   1316 C  CA  . VAL A 1 171 ? 9.967  7.847   13.886  1.00 14.08 ? 171 VAL A CA  1 
ATOM   1317 C  C   . VAL A 1 171 ? 10.567 6.498   14.276  1.00 11.45 ? 171 VAL A C   1 
ATOM   1318 O  O   . VAL A 1 171 ? 10.695 6.168   15.451  1.00 10.13 ? 171 VAL A O   1 
ATOM   1319 C  CB  . VAL A 1 171 ? 11.008 8.759   13.195  1.00 12.37 ? 171 VAL A CB  1 
ATOM   1320 C  CG1 . VAL A 1 171 ? 10.357 10.067  12.773  1.00 16.81 ? 171 VAL A CG1 1 
ATOM   1321 C  CG2 . VAL A 1 171 ? 12.157 9.015   14.109  1.00 8.34  ? 171 VAL A CG2 1 
ATOM   1322 N  N   . HIS A 1 172 ? 10.917 5.702   13.274  1.00 6.87  ? 172 HIS A N   1 
ATOM   1323 C  CA  . HIS A 1 172 ? 11.165 4.290   13.499  1.00 5.90  ? 172 HIS A CA  1 
ATOM   1324 C  C   . HIS A 1 172 ? 12.570 3.899   13.060  1.00 5.14  ? 172 HIS A C   1 
ATOM   1325 O  O   . HIS A 1 172 ? 13.123 4.437   12.091  1.00 7.00  ? 172 HIS A O   1 
ATOM   1326 C  CB  . HIS A 1 172 ? 10.088 3.456   12.785  1.00 4.72  ? 172 HIS A CB  1 
ATOM   1327 C  CG  . HIS A 1 172 ? 8.698  3.824   13.196  1.00 6.11  ? 172 HIS A CG  1 
ATOM   1328 N  ND1 . HIS A 1 172 ? 7.813  4.473   12.359  1.00 5.48  ? 172 HIS A ND1 1 
ATOM   1329 C  CD2 . HIS A 1 172 ? 8.058  3.683   14.384  1.00 8.77  ? 172 HIS A CD2 1 
ATOM   1330 C  CE1 . HIS A 1 172 ? 6.676  4.682   13.000  1.00 8.57  ? 172 HIS A CE1 1 
ATOM   1331 N  NE2 . HIS A 1 172 ? 6.806  4.232   14.237  1.00 8.95  ? 172 HIS A NE2 1 
ATOM   1332 N  N   . ALA A 1 173 ? 13.132 2.946   13.798  1.00 2.65  ? 173 ALA A N   1 
ATOM   1333 C  CA  . ALA A 1 173 ? 14.498 2.491   13.647  1.00 3.97  ? 173 ALA A CA  1 
ATOM   1334 C  C   . ALA A 1 173 ? 14.488 0.974   13.664  1.00 5.58  ? 173 ALA A C   1 
ATOM   1335 O  O   . ALA A 1 173 ? 13.686 0.356   14.377  1.00 5.58  ? 173 ALA A O   1 
ATOM   1336 C  CB  . ALA A 1 173 ? 15.404 3.020   14.774  1.00 5.89  ? 173 ALA A CB  1 
ATOM   1337 N  N   . GLY A 1 174 ? 15.364 0.382   12.865  1.00 1.92  ? 174 GLY A N   1 
ATOM   1338 C  CA  . GLY A 1 174 ? 15.460 -1.055  12.828  1.00 5.78  ? 174 GLY A CA  1 
ATOM   1339 C  C   . GLY A 1 174 ? 16.771 -1.489  12.226  1.00 3.82  ? 174 GLY A C   1 
ATOM   1340 O  O   . GLY A 1 174 ? 17.671 -0.673  12.002  1.00 4.33  ? 174 GLY A O   1 
ATOM   1341 N  N   . THR A 1 175 ? 16.862 -2.792  11.954  1.00 1.75  ? 175 THR A N   1 
ATOM   1342 C  CA  . THR A 1 175 ? 18.108 -3.425  11.523  1.00 4.79  ? 175 THR A CA  1 
ATOM   1343 C  C   . THR A 1 175 ? 17.935 -4.044  10.135  1.00 3.71  ? 175 THR A C   1 
ATOM   1344 O  O   . THR A 1 175 ? 16.814 -4.233  9.645   1.00 1.34  ? 175 THR A O   1 
ATOM   1345 C  CB  . THR A 1 175 ? 18.572 -4.515  12.523  1.00 3.80  ? 175 THR A CB  1 
ATOM   1346 O  OG1 . THR A 1 175 ? 17.710 -5.652  12.444  1.00 3.36  ? 175 THR A OG1 1 
ATOM   1347 C  CG2 . THR A 1 175 ? 18.605 -4.015  13.993  1.00 3.69  ? 175 THR A CG2 1 
ATOM   1348 N  N   . ASP A 1 176 ? 19.059 -4.360  9.485   1.00 5.08  ? 176 ASP A N   1 
ATOM   1349 C  CA  . ASP A 1 176 ? 18.974 -5.316  8.387   1.00 4.72  ? 176 ASP A CA  1 
ATOM   1350 C  C   . ASP A 1 176 ? 18.770 -6.701  8.991   1.00 4.55  ? 176 ASP A C   1 
ATOM   1351 O  O   . ASP A 1 176 ? 18.593 -6.845  10.202  1.00 5.27  ? 176 ASP A O   1 
ATOM   1352 C  CB  . ASP A 1 176 ? 20.190 -5.224  7.461   1.00 7.61  ? 176 ASP A CB  1 
ATOM   1353 C  CG  . ASP A 1 176 ? 21.519 -5.534  8.144   1.00 10.94 ? 176 ASP A CG  1 
ATOM   1354 O  OD1 . ASP A 1 176 ? 21.562 -6.328  9.107   1.00 9.68  ? 176 ASP A OD1 1 
ATOM   1355 O  OD2 . ASP A 1 176 ? 22.551 -4.990  7.674   1.00 9.49  ? 176 ASP A OD2 1 
ATOM   1356 N  N   . LEU A 1 177 ? 18.751 -7.738  8.159   1.00 4.24  ? 177 LEU A N   1 
ATOM   1357 C  CA  . LEU A 1 177 ? 18.377 -9.054  8.670   1.00 9.11  ? 177 LEU A CA  1 
ATOM   1358 C  C   . LEU A 1 177 ? 19.570 -9.834  9.209   1.00 7.67  ? 177 LEU A C   1 
ATOM   1359 O  O   . LEU A 1 177 ? 19.394 -10.972 9.662   1.00 5.32  ? 177 LEU A O   1 
ATOM   1360 C  CB  . LEU A 1 177 ? 17.646 -9.878  7.595   1.00 6.33  ? 177 LEU A CB  1 
ATOM   1361 C  CG  . LEU A 1 177 ? 16.108 -9.834  7.630   1.00 5.89  ? 177 LEU A CG  1 
ATOM   1362 C  CD1 . LEU A 1 177 ? 15.567 -10.381 8.968   1.00 7.93  ? 177 LEU A CD1 1 
ATOM   1363 C  CD2 . LEU A 1 177 ? 15.572 -8.416  7.381   1.00 6.53  ? 177 LEU A CD2 1 
ATOM   1364 N  N   . GLU A 1 178 ? 20.770 -9.253  9.158   1.00 5.41  ? 178 GLU A N   1 
ATOM   1365 C  CA  . GLU A 1 178 ? 21.901 -9.714  9.955   1.00 10.17 ? 178 GLU A CA  1 
ATOM   1366 C  C   . GLU A 1 178 ? 21.977 -8.994  11.300  1.00 9.03  ? 178 GLU A C   1 
ATOM   1367 O  O   . GLU A 1 178 ? 22.978 -9.141  12.017  1.00 11.75 ? 178 GLU A O   1 
ATOM   1368 C  CB  . GLU A 1 178 ? 23.224 -9.522  9.193   1.00 12.87 ? 178 GLU A CB  1 
ATOM   1369 C  CG  . GLU A 1 178 ? 23.280 -10.183 7.821   1.00 16.41 ? 178 GLU A CG  1 
ATOM   1370 C  CD  . GLU A 1 178 ? 24.705 -10.308 7.273   1.00 28.00 ? 178 GLU A CD  1 
ATOM   1371 O  OE1 . GLU A 1 178 ? 25.085 -11.418 6.831   1.00 30.93 ? 178 GLU A OE1 1 
ATOM   1372 O  OE2 . GLU A 1 178 ? 25.446 -9.297  7.274   1.00 29.13 ? 178 GLU A OE2 1 
ATOM   1373 N  N   . GLY A 1 179 ? 20.958 -8.202  11.642  1.00 4.95  ? 179 GLY A N   1 
ATOM   1374 C  CA  . GLY A 1 179 ? 20.883 -7.558  12.940  1.00 6.80  ? 179 GLY A CA  1 
ATOM   1375 C  C   . GLY A 1 179 ? 21.636 -6.251  13.098  1.00 6.50  ? 179 GLY A C   1 
ATOM   1376 O  O   . GLY A 1 179 ? 21.730 -5.747  14.225  1.00 5.02  ? 179 GLY A O   1 
ATOM   1377 N  N   . ASN A 1 180 ? 22.182 -5.679  12.024  1.00 6.68  ? 180 ASN A N   1 
ATOM   1378 C  CA  . ASN A 1 180 ? 22.938 -4.426  12.114  1.00 4.89  ? 180 ASN A CA  1 
ATOM   1379 C  C   . ASN A 1 180 ? 21.986 -3.245  11.937  1.00 6.59  ? 180 ASN A C   1 
ATOM   1380 O  O   . ASN A 1 180 ? 21.316 -3.130  10.900  1.00 5.56  ? 180 ASN A O   1 
ATOM   1381 C  CB  . ASN A 1 180 ? 24.032 -4.364  11.049  1.00 8.75  ? 180 ASN A CB  1 
ATOM   1382 C  CG  . ASN A 1 180 ? 25.029 -5.508  11.154  1.00 10.61 ? 180 ASN A CG  1 
ATOM   1383 O  OD1 . ASN A 1 180 ? 25.906 -5.509  12.006  1.00 6.79  ? 180 ASN A OD1 1 
ATOM   1384 N  ND2 . ASN A 1 180 ? 24.898 -6.478  10.271  1.00 14.91 ? 180 ASN A ND2 1 
ATOM   1385 N  N   . PHE A 1 181 ? 21.944 -2.354  12.923  1.00 5.68  ? 181 PHE A N   1 
ATOM   1386 C  CA  . PHE A 1 181 ? 21.014 -1.231  12.847  1.00 4.63  ? 181 PHE A CA  1 
ATOM   1387 C  C   . PHE A 1 181 ? 21.347 -0.372  11.638  1.00 6.47  ? 181 PHE A C   1 
ATOM   1388 O  O   . PHE A 1 181 ? 22.505 -0.255  11.229  1.00 7.34  ? 181 PHE A O   1 
ATOM   1389 C  CB  . PHE A 1 181 ? 21.058 -0.380  14.134  1.00 6.71  ? 181 PHE A CB  1 
ATOM   1390 C  CG  . PHE A 1 181 ? 19.910 -0.650  15.084  1.00 5.54  ? 181 PHE A CG  1 
ATOM   1391 C  CD1 . PHE A 1 181 ? 18.693 0.002   14.928  1.00 3.61  ? 181 PHE A CD1 1 
ATOM   1392 C  CD2 . PHE A 1 181 ? 20.041 -1.579  16.113  1.00 6.55  ? 181 PHE A CD2 1 
ATOM   1393 C  CE1 . PHE A 1 181 ? 17.639 -0.266  15.787  1.00 5.14  ? 181 PHE A CE1 1 
ATOM   1394 C  CE2 . PHE A 1 181 ? 18.992 -1.852  16.979  1.00 3.45  ? 181 PHE A CE2 1 
ATOM   1395 C  CZ  . PHE A 1 181 ? 17.788 -1.203  16.820  1.00 5.39  ? 181 PHE A CZ  1 
ATOM   1396 N  N   . TYR A 1 182 ? 20.312 0.194   11.032  1.00 5.79  ? 182 TYR A N   1 
ATOM   1397 C  CA  . TYR A 1 182 ? 20.509 1.293   10.102  1.00 7.66  ? 182 TYR A CA  1 
ATOM   1398 C  C   . TYR A 1 182 ? 20.708 2.556   10.919  1.00 6.73  ? 182 TYR A C   1 
ATOM   1399 O  O   . TYR A 1 182 ? 19.923 2.842   11.823  1.00 7.51  ? 182 TYR A O   1 
ATOM   1400 C  CB  . TYR A 1 182 ? 19.305 1.455   9.171   1.00 6.90  ? 182 TYR A CB  1 
ATOM   1401 C  CG  . TYR A 1 182 ? 19.170 0.379   8.106   1.00 9.21  ? 182 TYR A CG  1 
ATOM   1402 C  CD1 . TYR A 1 182 ? 19.899 0.447   6.929   1.00 7.90  ? 182 TYR A CD1 1 
ATOM   1403 C  CD2 . TYR A 1 182 ? 18.292 -0.689  8.275   1.00 6.39  ? 182 TYR A CD2 1 
ATOM   1404 C  CE1 . TYR A 1 182 ? 19.770 -0.517  5.965   1.00 10.92 ? 182 TYR A CE1 1 
ATOM   1405 C  CE2 . TYR A 1 182 ? 18.157 -1.670  7.307   1.00 6.06  ? 182 TYR A CE2 1 
ATOM   1406 C  CZ  . TYR A 1 182 ? 18.897 -1.583  6.158   1.00 9.49  ? 182 TYR A CZ  1 
ATOM   1407 O  OH  . TYR A 1 182 ? 18.770 -2.542  5.165   1.00 8.33  ? 182 TYR A OH  1 
ATOM   1408 N  N   . GLY A 1 183 ? 21.760 3.304   10.615  1.00 7.34  ? 183 GLY A N   1 
ATOM   1409 C  CA  . GLY A 1 183 ? 22.032 4.534   11.314  1.00 9.41  ? 183 GLY A CA  1 
ATOM   1410 C  C   . GLY A 1 183 ? 22.634 4.321   12.690  1.00 11.48 ? 183 GLY A C   1 
ATOM   1411 O  O   . GLY A 1 183 ? 23.092 3.222   13.025  1.00 10.29 ? 183 GLY A O   1 
ATOM   1412 N  N   . PRO A 1 184 ? 22.624 5.357   13.516  1.00 11.72 ? 184 PRO A N   1 
ATOM   1413 C  CA  . PRO A 1 184 ? 23.406 5.344   14.764  1.00 14.77 ? 184 PRO A CA  1 
ATOM   1414 C  C   . PRO A 1 184 ? 22.725 4.677   15.951  1.00 11.01 ? 184 PRO A C   1 
ATOM   1415 O  O   . PRO A 1 184 ? 23.248 4.779   17.060  1.00 16.68 ? 184 PRO A O   1 
ATOM   1416 C  CB  . PRO A 1 184 ? 23.595 6.844   15.033  1.00 11.52 ? 184 PRO A CB  1 
ATOM   1417 C  CG  . PRO A 1 184 ? 22.295 7.423   14.608  1.00 9.84  ? 184 PRO A CG  1 
ATOM   1418 C  CD  . PRO A 1 184 ? 21.927 6.649   13.339  1.00 10.25 ? 184 PRO A CD  1 
ATOM   1419 N  N   . PHE A 1 185 ? 21.601 3.999   15.772  1.00 7.15  ? 185 PHE A N   1 
ATOM   1420 C  CA  . PHE A 1 185 ? 20.769 3.646   16.914  1.00 11.94 ? 185 PHE A CA  1 
ATOM   1421 C  C   . PHE A 1 185 ? 21.240 2.364   17.598  1.00 11.68 ? 185 PHE A C   1 
ATOM   1422 O  O   . PHE A 1 185 ? 21.900 1.520   16.985  1.00 7.25  ? 185 PHE A O   1 
ATOM   1423 C  CB  . PHE A 1 185 ? 19.321 3.523   16.452  1.00 11.95 ? 185 PHE A CB  1 
ATOM   1424 C  CG  . PHE A 1 185 ? 18.858 4.725   15.685  1.00 12.28 ? 185 PHE A CG  1 
ATOM   1425 C  CD1 . PHE A 1 185 ? 18.655 5.942   16.343  1.00 9.91  ? 185 PHE A CD1 1 
ATOM   1426 C  CD2 . PHE A 1 185 ? 18.711 4.675   14.304  1.00 7.30  ? 185 PHE A CD2 1 
ATOM   1427 C  CE1 . PHE A 1 185 ? 18.253 7.068   15.629  1.00 13.01 ? 185 PHE A CE1 1 
ATOM   1428 C  CE2 . PHE A 1 185 ? 18.316 5.801   13.591  1.00 7.69  ? 185 PHE A CE2 1 
ATOM   1429 C  CZ  . PHE A 1 185 ? 18.084 6.993   14.251  1.00 8.94  ? 185 PHE A CZ  1 
ATOM   1430 N  N   . VAL A 1 186 ? 20.905 2.242   18.896  1.00 8.52  ? 186 VAL A N   1 
ATOM   1431 C  CA  . VAL A 1 186 ? 21.149 1.040   19.692  1.00 8.84  ? 186 VAL A CA  1 
ATOM   1432 C  C   . VAL A 1 186 ? 19.831 0.564   20.301  1.00 10.18 ? 186 VAL A C   1 
ATOM   1433 O  O   . VAL A 1 186 ? 18.921 1.367   20.543  1.00 9.97  ? 186 VAL A O   1 
ATOM   1434 C  CB  . VAL A 1 186 ? 22.190 1.309   20.791  1.00 12.62 ? 186 VAL A CB  1 
ATOM   1435 C  CG1 . VAL A 1 186 ? 23.567 1.545   20.167  1.00 10.76 ? 186 VAL A CG1 1 
ATOM   1436 C  CG2 . VAL A 1 186 ? 21.742 2.488   21.657  1.00 13.01 ? 186 VAL A CG2 1 
ATOM   1437 N  N   . ASP A 1 187 ? 19.721 -0.750  20.559  1.00 6.73  ? 187 ASP A N   1 
ATOM   1438 C  CA  . ASP A 1 187 ? 18.487 -1.284  21.155  1.00 9.60  ? 187 ASP A CA  1 
ATOM   1439 C  C   . ASP A 1 187 ? 18.555 -1.227  22.692  1.00 9.68  ? 187 ASP A C   1 
ATOM   1440 O  O   . ASP A 1 187 ? 18.586 -2.235  23.408  1.00 11.21 ? 187 ASP A O   1 
ATOM   1441 C  CB  . ASP A 1 187 ? 18.176 -2.684  20.629  1.00 4.99  ? 187 ASP A CB  1 
ATOM   1442 C  CG  . ASP A 1 187 ? 19.368 -3.645  20.692  1.00 7.12  ? 187 ASP A CG  1 
ATOM   1443 O  OD1 . ASP A 1 187 ? 20.522 -3.209  20.934  1.00 6.39  ? 187 ASP A OD1 1 
ATOM   1444 O  OD2 . ASP A 1 187 ? 19.140 -4.857  20.486  1.00 3.32  ? 187 ASP A OD2 1 
ATOM   1445 N  N   . ARG A 1 188 ? 18.546 0.013   23.190  1.00 9.57  ? 188 ARG A N   1 
ATOM   1446 C  CA  . ARG A 1 188 ? 18.387 0.349   24.604  1.00 15.04 ? 188 ARG A CA  1 
ATOM   1447 C  C   . ARG A 1 188 ? 17.487 1.575   24.718  1.00 16.58 ? 188 ARG A C   1 
ATOM   1448 O  O   . ARG A 1 188 ? 17.437 2.416   23.812  1.00 15.22 ? 188 ARG A O   1 
ATOM   1449 C  CB  . ARG A 1 188 ? 19.721 0.667   25.306  1.00 13.66 ? 188 ARG A CB  1 
ATOM   1450 C  CG  . ARG A 1 188 ? 20.880 -0.231  24.919  1.00 24.85 ? 188 ARG A CG  1 
ATOM   1451 C  CD  . ARG A 1 188 ? 22.245 0.279   25.441  1.00 27.95 ? 188 ARG A CD  1 
ATOM   1452 N  NE  . ARG A 1 188 ? 22.676 1.503   24.771  1.00 25.92 ? 188 ARG A NE  1 
ATOM   1453 C  CZ  . ARG A 1 188 ? 23.937 1.820   24.504  1.00 28.26 ? 188 ARG A CZ  1 
ATOM   1454 N  NH1 . ARG A 1 188 ? 24.931 0.977   24.739  1.00 30.48 ? 188 ARG A NH1 1 
ATOM   1455 N  NH2 . ARG A 1 188 ? 24.206 3.006   23.962  1.00 32.53 ? 188 ARG A NH2 1 
ATOM   1456 N  N   . GLN A 1 189 ? 16.788 1.688   25.845  1.00 11.75 ? 189 GLN A N   1 
ATOM   1457 C  CA  . GLN A 1 189 ? 15.969 2.877   26.090  1.00 19.73 ? 189 GLN A CA  1 
ATOM   1458 C  C   . GLN A 1 189 ? 16.843 3.979   26.692  1.00 21.98 ? 189 GLN A C   1 
ATOM   1459 O  O   . GLN A 1 189 ? 16.794 4.274   27.891  1.00 16.42 ? 189 GLN A O   1 
ATOM   1460 C  CB  . GLN A 1 189 ? 14.785 2.559   26.997  1.00 20.12 ? 189 GLN A CB  1 
ATOM   1461 C  CG  . GLN A 1 189 ? 13.905 3.783   27.196  1.00 22.78 ? 189 GLN A CG  1 
ATOM   1462 C  CD  . GLN A 1 189 ? 12.485 3.452   27.592  1.00 26.26 ? 189 GLN A CD  1 
ATOM   1463 O  OE1 . GLN A 1 189 ? 12.128 2.283   27.780  1.00 22.28 ? 189 GLN A OE1 1 
ATOM   1464 N  NE2 . GLN A 1 189 ? 11.650 4.489   27.694  1.00 19.66 ? 189 GLN A NE2 1 
ATOM   1465 N  N   . THR A 1 190 ? 17.670 4.584   25.835  1.00 18.48 ? 190 THR A N   1 
ATOM   1466 C  CA  . THR A 1 190 ? 18.518 5.727   26.176  1.00 18.19 ? 190 THR A CA  1 
ATOM   1467 C  C   . THR A 1 190 ? 18.159 6.891   25.258  1.00 21.77 ? 190 THR A C   1 
ATOM   1468 O  O   . THR A 1 190 ? 17.453 6.724   24.270  1.00 21.95 ? 190 THR A O   1 
ATOM   1469 C  CB  . THR A 1 190 ? 20.004 5.390   26.025  1.00 21.57 ? 190 THR A CB  1 
ATOM   1470 O  OG1 . THR A 1 190 ? 20.223 4.027   26.385  1.00 33.58 ? 190 THR A OG1 1 
ATOM   1471 C  CG2 . THR A 1 190 ? 20.838 6.266   26.942  1.00 20.38 ? 190 THR A CG2 1 
ATOM   1472 N  N   . ALA A 1 191 ? 18.678 8.078   25.560  1.00 21.07 ? 191 ALA A N   1 
ATOM   1473 C  CA  . ALA A 1 191 ? 18.372 9.267   24.757  1.00 23.80 ? 191 ALA A CA  1 
ATOM   1474 C  C   . ALA A 1 191 ? 19.230 9.247   23.498  1.00 22.67 ? 191 ALA A C   1 
ATOM   1475 O  O   . ALA A 1 191 ? 20.434 9.511   23.543  1.00 37.47 ? 191 ALA A O   1 
ATOM   1476 C  CB  . ALA A 1 191 ? 18.610 10.540  25.566  1.00 22.65 ? 191 ALA A CB  1 
ATOM   1477 N  N   . GLN A 1 192 ? 18.602 8.942   22.357  1.00 16.80 ? 192 GLN A N   1 
ATOM   1478 C  CA  . GLN A 1 192 ? 19.276 8.913   21.063  1.00 21.80 ? 192 GLN A CA  1 
ATOM   1479 C  C   . GLN A 1 192 ? 18.430 9.617   20.015  1.00 23.90 ? 192 GLN A C   1 
ATOM   1480 O  O   . GLN A 1 192 ? 17.231 9.348   19.883  1.00 25.86 ? 192 GLN A O   1 
ATOM   1481 C  CB  . GLN A 1 192 ? 19.569 7.481   20.608  1.00 22.34 ? 192 GLN A CB  1 
ATOM   1482 C  CG  . GLN A 1 192 ? 18.428 6.506   20.793  1.00 19.21 ? 192 GLN A CG  1 
ATOM   1483 C  CD  . GLN A 1 192 ? 18.880 5.054   20.726  1.00 18.61 ? 192 GLN A CD  1 
ATOM   1484 O  OE1 . GLN A 1 192 ? 19.614 4.672   19.815  1.00 14.44 ? 192 GLN A OE1 1 
ATOM   1485 N  NE2 . GLN A 1 192 ? 18.424 4.235   21.673  1.00 12.53 ? 192 GLN A NE2 1 
ATOM   1486 N  N   . ALA A 1 193 ? 19.057 10.495  19.255  1.00 16.96 ? 193 ALA A N   1 
ATOM   1487 C  CA  . ALA A 1 193 ? 18.333 11.261  18.261  1.00 26.18 ? 193 ALA A CA  1 
ATOM   1488 C  C   . ALA A 1 193 ? 18.835 10.939  16.857  1.00 20.10 ? 193 ALA A C   1 
ATOM   1489 O  O   . ALA A 1 193 ? 20.002 10.591  16.648  1.00 15.51 ? 193 ALA A O   1 
ATOM   1490 C  CB  . ALA A 1 193 ? 18.446 12.763  18.546  1.00 27.16 ? 193 ALA A CB  1 
ATOM   1491 N  N   . ALA A 1 194 ? 17.921 11.016  15.899  1.00 18.76 ? 194 ALA A N   1 
ATOM   1492 C  CA  . ALA A 1 194 ? 18.304 10.908  14.504  1.00 17.35 ? 194 ALA A CA  1 
ATOM   1493 C  C   . ALA A 1 194 ? 19.061 12.162  14.088  1.00 18.05 ? 194 ALA A C   1 
ATOM   1494 O  O   . ALA A 1 194 ? 18.848 13.253  14.625  1.00 18.46 ? 194 ALA A O   1 
ATOM   1495 C  CB  . ALA A 1 194 ? 17.067 10.720  13.627  1.00 12.16 ? 194 ALA A CB  1 
ATOM   1496 N  N   . GLY A 1 195 ? 19.969 12.001  13.142  1.00 19.99 ? 195 GLY A N   1 
ATOM   1497 C  CA  . GLY A 1 195 ? 20.616 13.159  12.571  1.00 15.78 ? 195 GLY A CA  1 
ATOM   1498 C  C   . GLY A 1 195 ? 19.656 14.002  11.743  1.00 19.16 ? 195 GLY A C   1 
ATOM   1499 O  O   . GLY A 1 195 ? 18.490 13.650  11.511  1.00 12.19 ? 195 GLY A O   1 
ATOM   1500 N  N   . THR A 1 196 ? 20.164 15.163  11.317  1.00 11.88 ? 196 THR A N   1 
ATOM   1501 C  CA  . THR A 1 196 ? 19.439 16.002  10.370  1.00 18.50 ? 196 THR A CA  1 
ATOM   1502 C  C   . THR A 1 196 ? 19.040 15.180  9.152   1.00 13.80 ? 196 THR A C   1 
ATOM   1503 O  O   . THR A 1 196 ? 19.886 14.543  8.509   1.00 17.24 ? 196 THR A O   1 
ATOM   1504 C  CB  . THR A 1 196 ? 20.299 17.192  9.923   1.00 15.63 ? 196 THR A CB  1 
ATOM   1505 O  OG1 . THR A 1 196 ? 20.907 17.815  11.054  1.00 16.61 ? 196 THR A OG1 1 
ATOM   1506 C  CG2 . THR A 1 196 ? 19.465 18.213  9.176   1.00 13.55 ? 196 THR A CG2 1 
ATOM   1507 N  N   . ASP A 1 197 ? 17.754 15.185  8.838   1.00 9.54  ? 197 ASP A N   1 
ATOM   1508 C  CA  . ASP A 1 197 ? 17.344 14.535  7.607   1.00 11.75 ? 197 ASP A CA  1 
ATOM   1509 C  C   . ASP A 1 197 ? 17.378 15.524  6.443   1.00 14.27 ? 197 ASP A C   1 
ATOM   1510 O  O   . ASP A 1 197 ? 17.610 16.725  6.612   1.00 16.05 ? 197 ASP A O   1 
ATOM   1511 C  CB  . ASP A 1 197 ? 15.956 13.929  7.747   1.00 9.57  ? 197 ASP A CB  1 
ATOM   1512 C  CG  . ASP A 1 197 ? 15.720 12.814  6.750   1.00 11.43 ? 197 ASP A CG  1 
ATOM   1513 O  OD1 . ASP A 1 197 ? 16.698 12.092  6.420   1.00 11.03 ? 197 ASP A OD1 1 
ATOM   1514 O  OD2 . ASP A 1 197 ? 14.572 12.672  6.290   1.00 8.43  ? 197 ASP A OD2 1 
ATOM   1515 N  N   . THR A 1 198 ? 17.159 15.001  5.237   1.00 14.89 ? 198 THR A N   1 
ATOM   1516 C  CA  . THR A 1 198 ? 17.099 15.837  4.045   1.00 11.61 ? 198 THR A CA  1 
ATOM   1517 C  C   . THR A 1 198 ? 16.105 15.200  3.088   1.00 10.09 ? 198 THR A C   1 
ATOM   1518 O  O   . THR A 1 198 ? 15.660 14.068  3.289   1.00 9.78  ? 198 THR A O   1 
ATOM   1519 C  CB  . THR A 1 198 ? 18.483 16.010  3.379   1.00 13.46 ? 198 THR A CB  1 
ATOM   1520 O  OG1 . THR A 1 198 ? 19.028 14.732  3.011   1.00 18.02 ? 198 THR A OG1 1 
ATOM   1521 C  CG2 . THR A 1 198 ? 19.459 16.682  4.320   1.00 15.00 ? 198 THR A CG2 1 
ATOM   1522 N  N   . THR A 1 199 ? 15.752 15.946  2.048   1.00 9.89  ? 199 THR A N   1 
ATOM   1523 C  CA  . THR A 1 199 ? 14.863 15.453  1.008   1.00 8.44  ? 199 THR A CA  1 
ATOM   1524 C  C   . THR A 1 199 ? 15.677 14.747  -0.068  1.00 6.30  ? 199 THR A C   1 
ATOM   1525 O  O   . THR A 1 199 ? 16.802 15.145  -0.380  1.00 6.17  ? 199 THR A O   1 
ATOM   1526 C  CB  . THR A 1 199 ? 14.069 16.615  0.421   1.00 9.05  ? 199 THR A CB  1 
ATOM   1527 O  OG1 . THR A 1 199 ? 13.340 17.242  1.478   1.00 6.66  ? 199 THR A OG1 1 
ATOM   1528 C  CG2 . THR A 1 199 ? 13.097 16.159  -0.664  1.00 5.53  ? 199 THR A CG2 1 
ATOM   1529 N  N   . ILE A 1 200 ? 15.094 13.691  -0.637  1.00 3.77  ? 200 ILE A N   1 
ATOM   1530 C  CA  . ILE A 1 200 ? 15.804 12.824  -1.586  1.00 3.55  ? 200 ILE A CA  1 
ATOM   1531 C  C   . ILE A 1 200 ? 15.618 13.416  -2.982  1.00 5.44  ? 200 ILE A C   1 
ATOM   1532 O  O   . ILE A 1 200 ? 14.669 13.099  -3.717  1.00 2.29  ? 200 ILE A O   1 
ATOM   1533 C  CB  . ILE A 1 200 ? 15.339 11.373  -1.476  1.00 4.08  ? 200 ILE A CB  1 
ATOM   1534 C  CG1 . ILE A 1 200 ? 15.432 10.942  -0.010  1.00 5.10  ? 200 ILE A CG1 1 
ATOM   1535 C  CG2 . ILE A 1 200 ? 16.244 10.438  -2.293  1.00 5.32  ? 200 ILE A CG2 1 
ATOM   1536 C  CD1 . ILE A 1 200 ? 14.523 9.786   0.367   1.00 4.54  ? 200 ILE A CD1 1 
ATOM   1537 N  N   . THR A 1 201 ? 16.569 14.274  -3.373  1.00 4.34  ? 201 THR A N   1 
ATOM   1538 C  CA  . THR A 1 201 ? 16.462 15.021  -4.628  1.00 7.21  ? 201 THR A CA  1 
ATOM   1539 C  C   . THR A 1 201 ? 16.182 14.113  -5.820  1.00 5.14  ? 201 THR A C   1 
ATOM   1540 O  O   . THR A 1 201 ? 15.296 14.406  -6.624  1.00 4.97  ? 201 THR A O   1 
ATOM   1541 C  CB  . THR A 1 201 ? 17.738 15.832  -4.879  1.00 4.69  ? 201 THR A CB  1 
ATOM   1542 O  OG1 . THR A 1 201 ? 18.084 16.548  -3.688  1.00 4.73  ? 201 THR A OG1 1 
ATOM   1543 C  CG2 . THR A 1 201 ? 17.541 16.829  -6.032  1.00 6.27  ? 201 THR A CG2 1 
ATOM   1544 N  N   . VAL A 1 202 ? 16.944 13.020  -5.978  1.00 3.40  ? 202 VAL A N   1 
ATOM   1545 C  CA  . VAL A 1 202 ? 16.756 12.201  -7.178  1.00 4.46  ? 202 VAL A CA  1 
ATOM   1546 C  C   . VAL A 1 202 ? 15.359 11.598  -7.208  1.00 4.25  ? 202 VAL A C   1 
ATOM   1547 O  O   . VAL A 1 202 ? 14.790 11.399  -8.286  1.00 3.73  ? 202 VAL A O   1 
ATOM   1548 C  CB  . VAL A 1 202 ? 17.831 11.097  -7.304  1.00 4.87  ? 202 VAL A CB  1 
ATOM   1549 C  CG1 . VAL A 1 202 ? 17.622 9.998   -6.249  1.00 9.61  ? 202 VAL A CG1 1 
ATOM   1550 C  CG2 . VAL A 1 202 ? 17.788 10.493  -8.706  1.00 2.78  ? 202 VAL A CG2 1 
ATOM   1551 N  N   . ASN A 1 203 ? 14.792 11.290  -6.038  1.00 4.26  ? 203 ASN A N   1 
ATOM   1552 C  CA  . ASN A 1 203 ? 13.411 10.805  -5.975  1.00 3.89  ? 203 ASN A CA  1 
ATOM   1553 C  C   . ASN A 1 203 ? 12.412 11.905  -6.309  1.00 3.07  ? 203 ASN A C   1 
ATOM   1554 O  O   . ASN A 1 203 ? 11.377 11.638  -6.934  1.00 2.32  ? 203 ASN A O   1 
ATOM   1555 C  CB  . ASN A 1 203 ? 13.108 10.249  -4.586  1.00 2.88  ? 203 ASN A CB  1 
ATOM   1556 C  CG  . ASN A 1 203 ? 13.839 8.955   -4.308  1.00 7.52  ? 203 ASN A CG  1 
ATOM   1557 O  OD1 . ASN A 1 203 ? 14.621 8.494   -5.135  1.00 5.35  ? 203 ASN A OD1 1 
ATOM   1558 N  ND2 . ASN A 1 203 ? 13.605 8.371   -3.124  1.00 6.43  ? 203 ASN A ND2 1 
ATOM   1559 N  N   . VAL A 1 204 ? 12.673 13.143  -5.877  1.00 1.35  ? 204 VAL A N   1 
ATOM   1560 C  CA  . VAL A 1 204 ? 11.750 14.220  -6.220  1.00 2.76  ? 204 VAL A CA  1 
ATOM   1561 C  C   . VAL A 1 204 ? 11.720 14.407  -7.731  1.00 3.06  ? 204 VAL A C   1 
ATOM   1562 O  O   . VAL A 1 204 ? 10.656 14.606  -8.323  1.00 2.38  ? 204 VAL A O   1 
ATOM   1563 C  CB  . VAL A 1 204 ? 12.127 15.529  -5.509  1.00 4.94  ? 204 VAL A CB  1 
ATOM   1564 C  CG1 . VAL A 1 204 ? 11.352 16.683  -6.134  1.00 2.16  ? 204 VAL A CG1 1 
ATOM   1565 C  CG2 . VAL A 1 204 ? 11.899 15.441  -3.976  1.00 1.95  ? 204 VAL A CG2 1 
ATOM   1566 N  N   . LEU A 1 205 ? 12.889 14.325  -8.378  1.00 2.67  ? 205 LEU A N   1 
ATOM   1567 C  CA  . LEU A 1 205 ? 12.953 14.472  -9.835  1.00 6.78  ? 205 LEU A CA  1 
ATOM   1568 C  C   . LEU A 1 205 ? 12.265 13.313  -10.547 1.00 4.06  ? 205 LEU A C   1 
ATOM   1569 O  O   . LEU A 1 205 ? 11.560 13.527  -11.543 1.00 5.09  ? 205 LEU A O   1 
ATOM   1570 C  CB  . LEU A 1 205 ? 14.411 14.601  -10.292 1.00 2.22  ? 205 LEU A CB  1 
ATOM   1571 C  CG  . LEU A 1 205 ? 15.098 15.856  -9.748  1.00 6.60  ? 205 LEU A CG  1 
ATOM   1572 C  CD1 . LEU A 1 205 ? 16.608 15.744  -9.898  1.00 5.45  ? 205 LEU A CD1 1 
ATOM   1573 C  CD2 . LEU A 1 205 ? 14.592 17.064  -10.522 1.00 3.60  ? 205 LEU A CD2 1 
ATOM   1574 N  N   . ALA A 1 206 ? 12.468 12.073  -10.077 1.00 3.46  ? 206 ALA A N   1 
ATOM   1575 C  CA  . ALA A 1 206 ? 11.778 10.950  -10.707 1.00 4.55  ? 206 ALA A CA  1 
ATOM   1576 C  C   . ALA A 1 206 ? 10.268 11.141  -10.633 1.00 6.72  ? 206 ALA A C   1 
ATOM   1577 O  O   . ALA A 1 206 ? 9.537  10.782  -11.566 1.00 5.41  ? 206 ALA A O   1 
ATOM   1578 C  CB  . ALA A 1 206 ? 12.196 9.628   -10.058 1.00 5.92  ? 206 ALA A CB  1 
ATOM   1579 N  N   . TRP A 1 207 ? 9.788  11.746  -9.546  1.00 3.73  ? 207 TRP A N   1 
ATOM   1580 C  CA  . TRP A 1 207 ? 8.352  11.925  -9.358  1.00 5.19  ? 207 TRP A CA  1 
ATOM   1581 C  C   . TRP A 1 207 ? 7.805  13.006  -10.288 1.00 5.65  ? 207 TRP A C   1 
ATOM   1582 O  O   . TRP A 1 207 ? 6.669  12.903  -10.765 1.00 5.11  ? 207 TRP A O   1 
ATOM   1583 C  CB  . TRP A 1 207 ? 8.088  12.248  -7.886  1.00 6.24  ? 207 TRP A CB  1 
ATOM   1584 C  CG  . TRP A 1 207 ? 6.665  12.637  -7.487  1.00 7.49  ? 207 TRP A CG  1 
ATOM   1585 C  CD1 . TRP A 1 207 ? 5.590  11.796  -7.309  1.00 8.51  ? 207 TRP A CD1 1 
ATOM   1586 C  CD2 . TRP A 1 207 ? 6.206  13.952  -7.127  1.00 5.88  ? 207 TRP A CD2 1 
ATOM   1587 N  NE1 . TRP A 1 207 ? 4.495  12.517  -6.900  1.00 8.16  ? 207 TRP A NE1 1 
ATOM   1588 C  CE2 . TRP A 1 207 ? 4.846  13.840  -6.778  1.00 5.05  ? 207 TRP A CE2 1 
ATOM   1589 C  CE3 . TRP A 1 207 ? 6.815  15.215  -7.081  1.00 5.30  ? 207 TRP A CE3 1 
ATOM   1590 C  CZ2 . TRP A 1 207 ? 4.080  14.941  -6.388  1.00 7.56  ? 207 TRP A CZ2 1 
ATOM   1591 C  CZ3 . TRP A 1 207 ? 6.056  16.311  -6.703  1.00 4.96  ? 207 TRP A CZ3 1 
ATOM   1592 C  CH2 . TRP A 1 207 ? 4.701  16.168  -6.353  1.00 6.90  ? 207 TRP A CH2 1 
ATOM   1593 N  N   . LEU A 1 208 ? 8.595  14.052  -10.554 1.00 4.53  ? 208 LEU A N   1 
ATOM   1594 C  CA  . LEU A 1 208 ? 8.206  15.052  -11.546 1.00 6.25  ? 208 LEU A CA  1 
ATOM   1595 C  C   . LEU A 1 208 ? 8.146  14.455  -12.946 1.00 4.69  ? 208 LEU A C   1 
ATOM   1596 O  O   . LEU A 1 208 ? 7.318  14.868  -13.761 1.00 5.42  ? 208 LEU A O   1 
ATOM   1597 C  CB  . LEU A 1 208 ? 9.179  16.240  -11.513 1.00 6.24  ? 208 LEU A CB  1 
ATOM   1598 C  CG  . LEU A 1 208 ? 9.092  17.106  -10.256 1.00 5.21  ? 208 LEU A CG  1 
ATOM   1599 C  CD1 . LEU A 1 208 ? 10.187 18.181  -10.207 1.00 6.93  ? 208 LEU A CD1 1 
ATOM   1600 C  CD2 . LEU A 1 208 ? 7.691  17.740  -10.110 1.00 5.69  ? 208 LEU A CD2 1 
ATOM   1601 N  N   . TYR A 1 209 ? 9.019  13.492  -13.247 1.00 4.96  ? 209 TYR A N   1 
ATOM   1602 C  CA  . TYR A 1 209 ? 8.896  12.743  -14.493 1.00 6.41  ? 209 TYR A CA  1 
ATOM   1603 C  C   . TYR A 1 209 ? 7.614  11.927  -14.507 1.00 7.40  ? 209 TYR A C   1 
ATOM   1604 O  O   . TYR A 1 209 ? 6.916  11.871  -15.528 1.00 7.16  ? 209 TYR A O   1 
ATOM   1605 C  CB  . TYR A 1 209 ? 10.100 11.825  -14.681 1.00 2.89  ? 209 TYR A CB  1 
ATOM   1606 C  CG  . TYR A 1 209 ? 11.310 12.537  -15.230 1.00 5.60  ? 209 TYR A CG  1 
ATOM   1607 C  CD1 . TYR A 1 209 ? 11.342 12.949  -16.554 1.00 6.02  ? 209 TYR A CD1 1 
ATOM   1608 C  CD2 . TYR A 1 209 ? 12.411 12.804  -14.432 1.00 4.07  ? 209 TYR A CD2 1 
ATOM   1609 C  CE1 . TYR A 1 209 ? 12.437 13.596  -17.064 1.00 7.24  ? 209 TYR A CE1 1 
ATOM   1610 C  CE2 . TYR A 1 209 ? 13.524 13.457  -14.941 1.00 6.35  ? 209 TYR A CE2 1 
ATOM   1611 C  CZ  . TYR A 1 209 ? 13.517 13.858  -16.268 1.00 6.56  ? 209 TYR A CZ  1 
ATOM   1612 O  OH  . TYR A 1 209 ? 14.597 14.510  -16.821 1.00 4.95  ? 209 TYR A OH  1 
ATOM   1613 N  N   . ALA A 1 210 ? 7.296  11.283  -13.382 1.00 2.62  ? 210 ALA A N   1 
ATOM   1614 C  CA  . ALA A 1 210 ? 6.048  10.545  -13.278 1.00 6.89  ? 210 ALA A CA  1 
ATOM   1615 C  C   . ALA A 1 210 ? 4.867  11.473  -13.501 1.00 8.51  ? 210 ALA A C   1 
ATOM   1616 O  O   . ALA A 1 210 ? 3.879  11.093  -14.141 1.00 9.85  ? 210 ALA A O   1 
ATOM   1617 C  CB  . ALA A 1 210 ? 5.958  9.861   -11.905 1.00 4.10  ? 210 ALA A CB  1 
ATOM   1618 N  N   . ALA A 1 211 ? 4.954  12.706  -12.990 1.00 3.95  ? 211 ALA A N   1 
ATOM   1619 C  CA  . ALA A 1 211 ? 3.853  13.641  -13.181 1.00 8.88  ? 211 ALA A CA  1 
ATOM   1620 C  C   . ALA A 1 211 ? 3.687  14.017  -14.652 1.00 9.72  ? 211 ALA A C   1 
ATOM   1621 O  O   . ALA A 1 211 ? 2.557  14.110  -15.138 1.00 10.67 ? 211 ALA A O   1 
ATOM   1622 C  CB  . ALA A 1 211 ? 4.051  14.888  -12.323 1.00 6.33  ? 211 ALA A CB  1 
ATOM   1623 N  N   . VAL A 1 212 ? 4.789  14.239  -15.376 1.00 6.46  ? 212 VAL A N   1 
ATOM   1624 C  CA  . VAL A 1 212 ? 4.663  14.618  -16.787 1.00 11.98 ? 212 VAL A CA  1 
ATOM   1625 C  C   . VAL A 1 212 ? 4.065  13.473  -17.605 1.00 10.85 ? 212 VAL A C   1 
ATOM   1626 O  O   . VAL A 1 212 ? 3.258  13.696  -18.516 1.00 16.45 ? 212 VAL A O   1 
ATOM   1627 C  CB  . VAL A 1 212 ? 6.023  15.055  -17.351 1.00 8.35  ? 212 VAL A CB  1 
ATOM   1628 C  CG1 . VAL A 1 212 ? 5.939  15.202  -18.889 1.00 13.34 ? 212 VAL A CG1 1 
ATOM   1629 C  CG2 . VAL A 1 212 ? 6.490  16.343  -16.687 1.00 9.84  ? 212 VAL A CG2 1 
ATOM   1630 N  N   . ILE A 1 213 ? 4.466  12.239  -17.301 1.00 8.05  ? 213 ILE A N   1 
ATOM   1631 C  CA  . ILE A 1 213 ? 3.987  11.050  -18.003 1.00 12.85 ? 213 ILE A CA  1 
ATOM   1632 C  C   . ILE A 1 213 ? 2.489  10.898  -17.857 1.00 14.79 ? 213 ILE A C   1 
ATOM   1633 O  O   . ILE A 1 213 ? 1.827  10.330  -18.733 1.00 17.54 ? 213 ILE A O   1 
ATOM   1634 C  CB  . ILE A 1 213 ? 4.715  9.795   -17.475 1.00 9.23  ? 213 ILE A CB  1 
ATOM   1635 C  CG1 . ILE A 1 213 ? 6.158  9.762   -17.987 1.00 10.21 ? 213 ILE A CG1 1 
ATOM   1636 C  CG2 . ILE A 1 213 ? 3.945  8.543   -17.863 1.00 12.32 ? 213 ILE A CG2 1 
ATOM   1637 C  CD1 . ILE A 1 213 ? 6.994  8.601   -17.471 1.00 10.13 ? 213 ILE A CD1 1 
ATOM   1638 N  N   . ASN A 1 214 ? 1.932  11.381  -16.750 1.00 13.26 ? 214 ASN A N   1 
ATOM   1639 C  CA  . ASN A 1 214 ? 0.508  11.285  -16.473 1.00 16.38 ? 214 ASN A CA  1 
ATOM   1640 C  C   . ASN A 1 214 ? -0.255 12.546  -16.853 1.00 13.99 ? 214 ASN A C   1 
ATOM   1641 O  O   . ASN A 1 214 ? -1.473 12.588  -16.692 1.00 16.26 ? 214 ASN A O   1 
ATOM   1642 C  CB  . ASN A 1 214 ? 0.296  10.959  -14.996 1.00 12.19 ? 214 ASN A CB  1 
ATOM   1643 C  CG  . ASN A 1 214 ? 0.597  9.511   -14.688 1.00 14.73 ? 214 ASN A CG  1 
ATOM   1644 O  OD1 . ASN A 1 214 ? -0.297 8.670   -14.707 1.00 21.44 ? 214 ASN A OD1 1 
ATOM   1645 N  ND2 . ASN A 1 214 ? 1.868  9.201   -14.442 1.00 13.73 ? 214 ASN A ND2 1 
ATOM   1646 N  N   . GLY A 1 215 ? 0.427  13.567  -17.362 1.00 12.89 ? 215 GLY A N   1 
ATOM   1647 C  CA  . GLY A 1 215 ? -0.231 14.768  -17.831 1.00 14.83 ? 215 GLY A CA  1 
ATOM   1648 C  C   . GLY A 1 215 ? -0.215 15.949  -16.884 1.00 13.15 ? 215 GLY A C   1 
ATOM   1649 O  O   . GLY A 1 215 ? -0.798 16.983  -17.219 1.00 12.54 ? 215 GLY A O   1 
ATOM   1650 N  N   . ASP A 1 216 ? 0.411  15.828  -15.711 1.00 11.03 ? 216 ASP A N   1 
ATOM   1651 C  CA  . ASP A 1 216 ? 0.519  16.938  -14.757 1.00 14.46 ? 216 ASP A CA  1 
ATOM   1652 C  C   . ASP A 1 216 ? 1.748  17.739  -15.156 1.00 14.20 ? 216 ASP A C   1 
ATOM   1653 O  O   . ASP A 1 216 ? 2.859  17.441  -14.724 1.00 17.45 ? 216 ASP A O   1 
ATOM   1654 C  CB  . ASP A 1 216 ? 0.665  16.419  -13.331 1.00 16.80 ? 216 ASP A CB  1 
ATOM   1655 C  CG  . ASP A 1 216 ? -0.649 16.156  -12.664 1.00 19.66 ? 216 ASP A CG  1 
ATOM   1656 O  OD1 . ASP A 1 216 ? -0.806 16.541  -11.483 1.00 25.37 ? 216 ASP A OD1 1 
ATOM   1657 O  OD2 . ASP A 1 216 ? -1.524 15.545  -13.322 1.00 36.31 ? 216 ASP A OD2 1 
ATOM   1658 N  N   . ARG A 1 217 ? 1.569  18.766  -15.984 1.00 10.70 ? 217 ARG A N   1 
ATOM   1659 C  CA  . ARG A 1 217 ? 2.718  19.358  -16.655 1.00 10.36 ? 217 ARG A CA  1 
ATOM   1660 C  C   . ARG A 1 217 ? 2.833  20.863  -16.471 1.00 11.26 ? 217 ARG A C   1 
ATOM   1661 O  O   . ARG A 1 217 ? 3.735  21.470  -17.055 1.00 13.24 ? 217 ARG A O   1 
ATOM   1662 C  CB  . ARG A 1 217 ? 2.689  19.014  -18.152 1.00 16.62 ? 217 ARG A CB  1 
ATOM   1663 N  N   . TRP A 1 218 ? 1.971  21.479  -15.655 1.00 13.58 ? 218 TRP A N   1 
ATOM   1664 C  CA  . TRP A 1 218 ? 2.010  22.928  -15.457 1.00 13.89 ? 218 TRP A CA  1 
ATOM   1665 C  C   . TRP A 1 218 ? 3.355  23.435  -14.921 1.00 13.06 ? 218 TRP A C   1 
ATOM   1666 O  O   . TRP A 1 218 ? 3.712  24.600  -15.147 1.00 12.78 ? 218 TRP A O   1 
ATOM   1667 C  CB  . TRP A 1 218 ? 0.878  23.345  -14.508 1.00 17.59 ? 218 TRP A CB  1 
ATOM   1668 C  CG  . TRP A 1 218 ? 0.951  22.752  -13.102 1.00 17.35 ? 218 TRP A CG  1 
ATOM   1669 C  CD1 . TRP A 1 218 ? 0.322  21.619  -12.650 1.00 19.61 ? 218 TRP A CD1 1 
ATOM   1670 C  CD2 . TRP A 1 218 ? 1.687  23.270  -11.982 1.00 13.52 ? 218 TRP A CD2 1 
ATOM   1671 N  NE1 . TRP A 1 218 ? 0.626  21.405  -11.325 1.00 16.53 ? 218 TRP A NE1 1 
ATOM   1672 C  CE2 . TRP A 1 218 ? 1.456  22.405  -10.891 1.00 16.14 ? 218 TRP A CE2 1 
ATOM   1673 C  CE3 . TRP A 1 218 ? 2.519  24.377  -11.798 1.00 14.32 ? 218 TRP A CE3 1 
ATOM   1674 C  CZ2 . TRP A 1 218 ? 2.026  22.615  -9.640  1.00 13.98 ? 218 TRP A CZ2 1 
ATOM   1675 C  CZ3 . TRP A 1 218 ? 3.077  24.586  -10.562 1.00 16.82 ? 218 TRP A CZ3 1 
ATOM   1676 C  CH2 . TRP A 1 218 ? 2.826  23.708  -9.491  1.00 14.49 ? 218 TRP A CH2 1 
ATOM   1677 N  N   . PHE A 1 219 ? 4.112  22.597  -14.218 1.00 13.72 ? 219 PHE A N   1 
ATOM   1678 C  CA  . PHE A 1 219 ? 5.345  23.051  -13.592 1.00 13.44 ? 219 PHE A CA  1 
ATOM   1679 C  C   . PHE A 1 219 ? 6.512  23.145  -14.567 1.00 13.05 ? 219 PHE A C   1 
ATOM   1680 O  O   . PHE A 1 219 ? 7.538  23.732  -14.211 1.00 14.55 ? 219 PHE A O   1 
ATOM   1681 C  CB  . PHE A 1 219 ? 5.722  22.122  -12.422 1.00 9.28  ? 219 PHE A CB  1 
ATOM   1682 C  CG  . PHE A 1 219 ? 5.740  20.679  -12.803 1.00 10.94 ? 219 PHE A CG  1 
ATOM   1683 C  CD1 . PHE A 1 219 ? 6.880  20.109  -13.358 1.00 9.86  ? 219 PHE A CD1 1 
ATOM   1684 C  CD2 . PHE A 1 219 ? 4.608  19.895  -12.641 1.00 13.01 ? 219 PHE A CD2 1 
ATOM   1685 C  CE1 . PHE A 1 219 ? 6.888  18.797  -13.742 1.00 8.70  ? 219 PHE A CE1 1 
ATOM   1686 C  CE2 . PHE A 1 219 ? 4.610  18.577  -13.032 1.00 8.72  ? 219 PHE A CE2 1 
ATOM   1687 C  CZ  . PHE A 1 219 ? 5.747  18.025  -13.579 1.00 9.91  ? 219 PHE A CZ  1 
ATOM   1688 N  N   . LEU A 1 220 ? 6.408  22.578  -15.767 1.00 12.47 ? 220 LEU A N   1 
ATOM   1689 C  CA  . LEU A 1 220 ? 7.494  22.724  -16.732 1.00 12.07 ? 220 LEU A CA  1 
ATOM   1690 C  C   . LEU A 1 220 ? 7.667  24.186  -17.135 1.00 16.39 ? 220 LEU A C   1 
ATOM   1691 O  O   . LEU A 1 220 ? 6.692  24.911  -17.347 1.00 14.32 ? 220 LEU A O   1 
ATOM   1692 C  CB  . LEU A 1 220 ? 7.227  21.882  -17.976 1.00 15.40 ? 220 LEU A CB  1 
ATOM   1693 C  CG  . LEU A 1 220 ? 7.085  20.369  -17.820 1.00 14.99 ? 220 LEU A CG  1 
ATOM   1694 C  CD1 . LEU A 1 220 ? 6.867  19.726  -19.182 1.00 12.33 ? 220 LEU A CD1 1 
ATOM   1695 C  CD2 . LEU A 1 220 ? 8.277  19.762  -17.103 1.00 10.81 ? 220 LEU A CD2 1 
ATOM   1696 N  N   . ASN A 1 221 ? 8.915  24.624  -17.247 1.00 17.07 ? 221 ASN A N   1 
ATOM   1697 C  CA  . ASN A 1 221 ? 9.211  25.979  -17.693 1.00 21.29 ? 221 ASN A CA  1 
ATOM   1698 C  C   . ASN A 1 221 ? 10.221 25.914  -18.838 1.00 23.93 ? 221 ASN A C   1 
ATOM   1699 O  O   . ASN A 1 221 ? 10.689 24.838  -19.231 1.00 19.22 ? 221 ASN A O   1 
ATOM   1700 C  CB  . ASN A 1 221 ? 9.745  26.834  -16.544 1.00 19.62 ? 221 ASN A CB  1 
ATOM   1701 C  CG  . ASN A 1 221 ? 10.986 26.251  -15.926 1.00 18.73 ? 221 ASN A CG  1 
ATOM   1702 O  OD1 . ASN A 1 221 ? 11.904 25.827  -16.630 1.00 14.97 ? 221 ASN A OD1 1 
ATOM   1703 N  ND2 . ASN A 1 221 ? 11.017 26.200  -14.596 1.00 20.08 ? 221 ASN A ND2 1 
ATOM   1704 N  N   . ARG A 1 222 ? 10.575 27.079  -19.369 1.00 28.91 ? 222 ARG A N   1 
ATOM   1705 C  CA  . ARG A 1 222 ? 11.538 27.146  -20.462 1.00 32.78 ? 222 ARG A CA  1 
ATOM   1706 C  C   . ARG A 1 222 ? 12.946 27.498  -19.987 1.00 26.26 ? 222 ARG A C   1 
ATOM   1707 O  O   . ARG A 1 222 ? 13.793 27.859  -20.810 1.00 35.44 ? 222 ARG A O   1 
ATOM   1708 C  CB  . ARG A 1 222 ? 11.072 28.149  -21.519 1.00 34.34 ? 222 ARG A CB  1 
ATOM   1709 C  CG  . ARG A 1 222 ? 10.928 29.540  -20.983 1.00 34.19 ? 222 ARG A CG  1 
ATOM   1710 C  CD  . ARG A 1 222 ? 9.630  30.195  -21.404 1.00 41.02 ? 222 ARG A CD  1 
ATOM   1711 N  NE  . ARG A 1 222 ? 9.620  31.585  -20.959 1.00 44.65 ? 222 ARG A NE  1 
ATOM   1712 C  CZ  . ARG A 1 222 ? 9.488  31.965  -19.692 1.00 51.29 ? 222 ARG A CZ  1 
ATOM   1713 N  NH1 . ARG A 1 222 ? 9.298  31.084  -18.718 1.00 54.55 ? 222 ARG A NH1 1 
ATOM   1714 N  NH2 . ARG A 1 222 ? 9.552  33.260  -19.390 1.00 43.32 ? 222 ARG A NH2 1 
ATOM   1715 N  N   . PHE A 1 223 ? 13.215 27.387  -18.688 1.00 18.50 ? 223 PHE A N   1 
ATOM   1716 C  CA  . PHE A 1 223 ? 14.545 27.612  -18.146 1.00 18.67 ? 223 PHE A CA  1 
ATOM   1717 C  C   . PHE A 1 223 ? 15.337 26.307  -18.101 1.00 17.39 ? 223 PHE A C   1 
ATOM   1718 O  O   . PHE A 1 223 ? 14.799 25.205  -18.235 1.00 16.44 ? 223 PHE A O   1 
ATOM   1719 C  CB  . PHE A 1 223 ? 14.465 28.209  -16.740 1.00 20.49 ? 223 PHE A CB  1 
ATOM   1720 C  CG  . PHE A 1 223 ? 13.585 29.421  -16.641 1.00 24.25 ? 223 PHE A CG  1 
ATOM   1721 C  CD1 . PHE A 1 223 ? 13.259 30.157  -17.768 1.00 27.63 ? 223 PHE A CD1 1 
ATOM   1722 C  CD2 . PHE A 1 223 ? 13.089 29.826  -15.424 1.00 24.40 ? 223 PHE A CD2 1 
ATOM   1723 C  CE1 . PHE A 1 223 ? 12.449 31.271  -17.673 1.00 31.49 ? 223 PHE A CE1 1 
ATOM   1724 C  CE2 . PHE A 1 223 ? 12.280 30.943  -15.327 1.00 30.71 ? 223 PHE A CE2 1 
ATOM   1725 C  CZ  . PHE A 1 223 ? 11.962 31.662  -16.454 1.00 28.85 ? 223 PHE A CZ  1 
ATOM   1726 N  N   . THR A 1 224 ? 16.638 26.443  -17.902 1.00 12.43 ? 224 THR A N   1 
ATOM   1727 C  CA  . THR A 1 224 ? 17.496 25.311  -17.602 1.00 15.84 ? 224 THR A CA  1 
ATOM   1728 C  C   . THR A 1 224 ? 18.488 25.752  -16.534 1.00 13.11 ? 224 THR A C   1 
ATOM   1729 O  O   . THR A 1 224 ? 18.491 26.908  -16.098 1.00 14.70 ? 224 THR A O   1 
ATOM   1730 C  CB  . THR A 1 224 ? 18.193 24.794  -18.865 1.00 16.42 ? 224 THR A CB  1 
ATOM   1731 O  OG1 . THR A 1 224 ? 18.772 23.512  -18.597 1.00 12.67 ? 224 THR A OG1 1 
ATOM   1732 C  CG2 . THR A 1 224 ? 19.274 25.776  -19.335 1.00 12.75 ? 224 THR A CG2 1 
ATOM   1733 N  N   . THR A 1 225 ? 19.321 24.831  -16.085 1.00 8.26  ? 225 THR A N   1 
ATOM   1734 C  CA  . THR A 1 225 ? 20.340 25.189  -15.114 1.00 12.27 ? 225 THR A CA  1 
ATOM   1735 C  C   . THR A 1 225 ? 21.528 24.250  -15.260 1.00 12.32 ? 225 THR A C   1 
ATOM   1736 O  O   . THR A 1 225 ? 21.577 23.396  -16.147 1.00 13.18 ? 225 THR A O   1 
ATOM   1737 C  CB  . THR A 1 225 ? 19.810 25.156  -13.679 1.00 7.02  ? 225 THR A CB  1 
ATOM   1738 O  OG1 . THR A 1 225 ? 20.893 25.440  -12.791 1.00 14.73 ? 225 THR A OG1 1 
ATOM   1739 C  CG2 . THR A 1 225 ? 19.252 23.779  -13.336 1.00 10.36 ? 225 THR A CG2 1 
ATOM   1740 N  N   . THR A 1 226 ? 22.495 24.433  -14.380 1.00 12.20 ? 226 THR A N   1 
ATOM   1741 C  CA  . THR A 1 226 ? 23.662 23.581  -14.283 1.00 14.39 ? 226 THR A CA  1 
ATOM   1742 C  C   . THR A 1 226 ? 23.578 22.786  -12.985 1.00 14.45 ? 226 THR A C   1 
ATOM   1743 O  O   . THR A 1 226 ? 22.944 23.219  -12.020 1.00 12.13 ? 226 THR A O   1 
ATOM   1744 C  CB  . THR A 1 226 ? 24.941 24.419  -14.305 1.00 11.71 ? 226 THR A CB  1 
ATOM   1745 O  OG1 . THR A 1 226 ? 25.020 25.180  -13.093 1.00 13.25 ? 226 THR A OG1 1 
ATOM   1746 C  CG2 . THR A 1 226 ? 24.938 25.368  -15.494 1.00 15.85 ? 226 THR A CG2 1 
ATOM   1747 N  N   . LEU A 1 227 ? 24.206 21.608  -12.981 1.00 11.69 ? 227 LEU A N   1 
ATOM   1748 C  CA  . LEU A 1 227 ? 24.340 20.842  -11.748 1.00 9.57  ? 227 LEU A CA  1 
ATOM   1749 C  C   . LEU A 1 227 ? 24.792 21.746  -10.614 1.00 13.66 ? 227 LEU A C   1 
ATOM   1750 O  O   . LEU A 1 227 ? 24.163 21.802  -9.551  1.00 13.74 ? 227 LEU A O   1 
ATOM   1751 C  CB  . LEU A 1 227 ? 25.341 19.700  -11.960 1.00 14.91 ? 227 LEU A CB  1 
ATOM   1752 C  CG  . LEU A 1 227 ? 25.191 18.363  -11.239 1.00 15.46 ? 227 LEU A CG  1 
ATOM   1753 C  CD1 . LEU A 1 227 ? 23.762 17.860  -11.353 1.00 16.49 ? 227 LEU A CD1 1 
ATOM   1754 C  CD2 . LEU A 1 227 ? 26.180 17.348  -11.822 1.00 14.35 ? 227 LEU A CD2 1 
ATOM   1755 N  N   . ASN A 1 228 ? 25.876 22.491  -10.843 1.00 14.88 ? 228 ASN A N   1 
ATOM   1756 C  CA  . ASN A 1 228 ? 26.409 23.375  -9.813  1.00 15.09 ? 228 ASN A CA  1 
ATOM   1757 C  C   . ASN A 1 228 ? 25.375 24.406  -9.370  1.00 11.71 ? 228 ASN A C   1 
ATOM   1758 O  O   . ASN A 1 228 ? 25.135 24.588  -8.171  1.00 14.56 ? 228 ASN A O   1 
ATOM   1759 C  CB  . ASN A 1 228 ? 27.688 24.046  -10.322 1.00 17.74 ? 228 ASN A CB  1 
ATOM   1760 C  CG  . ASN A 1 228 ? 28.859 23.067  -10.423 1.00 20.13 ? 228 ASN A CG  1 
ATOM   1761 O  OD1 . ASN A 1 228 ? 29.102 22.287  -9.499  1.00 26.44 ? 228 ASN A OD1 1 
ATOM   1762 N  ND2 . ASN A 1 228 ? 29.578 23.099  -11.544 1.00 21.74 ? 228 ASN A ND2 1 
ATOM   1763 N  N   . ASP A 1 229 ? 24.753 25.101  -10.313 1.00 11.43 ? 229 ASP A N   1 
ATOM   1764 C  CA  . ASP A 1 229 ? 23.737 26.073  -9.923  1.00 12.41 ? 229 ASP A CA  1 
ATOM   1765 C  C   . ASP A 1 229 ? 22.599 25.409  -9.138  1.00 12.96 ? 229 ASP A C   1 
ATOM   1766 O  O   . ASP A 1 229 ? 22.205 25.887  -8.066  1.00 11.56 ? 229 ASP A O   1 
ATOM   1767 C  CB  . ASP A 1 229 ? 23.191 26.785  -11.153 1.00 12.27 ? 229 ASP A CB  1 
ATOM   1768 C  CG  . ASP A 1 229 ? 22.031 27.685  -10.816 1.00 16.55 ? 229 ASP A CG  1 
ATOM   1769 O  OD1 . ASP A 1 229 ? 22.303 28.768  -10.271 1.00 17.83 ? 229 ASP A OD1 1 
ATOM   1770 O  OD2 . ASP A 1 229 ? 20.859 27.322  -11.093 1.00 17.85 ? 229 ASP A OD2 1 
ATOM   1771 N  N   . PHE A 1 230 ? 22.060 24.297  -9.660  1.00 11.85 ? 230 PHE A N   1 
ATOM   1772 C  CA  . PHE A 1 230 ? 20.970 23.617  -8.964  1.00 9.80  ? 230 PHE A CA  1 
ATOM   1773 C  C   . PHE A 1 230 ? 21.385 23.194  -7.554  1.00 10.79 ? 230 PHE A C   1 
ATOM   1774 O  O   . PHE A 1 230 ? 20.588 23.285  -6.610  1.00 11.88 ? 230 PHE A O   1 
ATOM   1775 C  CB  . PHE A 1 230 ? 20.480 22.410  -9.772  1.00 5.78  ? 230 PHE A CB  1 
ATOM   1776 C  CG  . PHE A 1 230 ? 19.499 21.562  -9.022  1.00 8.57  ? 230 PHE A CG  1 
ATOM   1777 C  CD1 . PHE A 1 230 ? 18.157 21.911  -8.982  1.00 6.85  ? 230 PHE A CD1 1 
ATOM   1778 C  CD2 . PHE A 1 230 ? 19.927 20.448  -8.296  1.00 11.33 ? 230 PHE A CD2 1 
ATOM   1779 C  CE1 . PHE A 1 230 ? 17.241 21.148  -8.255  1.00 9.88  ? 230 PHE A CE1 1 
ATOM   1780 C  CE2 . PHE A 1 230 ? 19.022 19.677  -7.557  1.00 10.22 ? 230 PHE A CE2 1 
ATOM   1781 C  CZ  . PHE A 1 230 ? 17.670 20.031  -7.542  1.00 8.60  ? 230 PHE A CZ  1 
ATOM   1782 N  N   . ASN A 1 231 ? 22.630 22.737  -7.379  1.00 10.52 ? 231 ASN A N   1 
ATOM   1783 C  CA  . ASN A 1 231 ? 23.043 22.260  -6.063  1.00 10.91 ? 231 ASN A CA  1 
ATOM   1784 C  C   . ASN A 1 231 ? 23.153 23.399  -5.061  1.00 14.85 ? 231 ASN A C   1 
ATOM   1785 O  O   . ASN A 1 231 ? 23.011 23.176  -3.849  1.00 11.55 ? 231 ASN A O   1 
ATOM   1786 C  CB  . ASN A 1 231 ? 24.365 21.497  -6.162  1.00 13.49 ? 231 ASN A CB  1 
ATOM   1787 C  CG  . ASN A 1 231 ? 24.152 20.059  -6.535  1.00 12.15 ? 231 ASN A CG  1 
ATOM   1788 O  OD1 . ASN A 1 231 ? 23.047 19.542  -6.380  1.00 14.08 ? 231 ASN A OD1 1 
ATOM   1789 N  ND2 . ASN A 1 231 ? 25.196 19.395  -7.014  1.00 15.02 ? 231 ASN A ND2 1 
ATOM   1790 N  N   . LEU A 1 232 ? 23.410 24.616  -5.547  1.00 10.73 ? 232 LEU A N   1 
ATOM   1791 C  CA  . LEU A 1 232 ? 23.257 25.804  -4.714  1.00 13.18 ? 232 LEU A CA  1 
ATOM   1792 C  C   . LEU A 1 232 ? 21.849 25.893  -4.135  1.00 10.16 ? 232 LEU A C   1 
ATOM   1793 O  O   . LEU A 1 232 ? 21.664 26.171  -2.940  1.00 9.17  ? 232 LEU A O   1 
ATOM   1794 C  CB  . LEU A 1 232 ? 23.554 27.050  -5.548  1.00 15.42 ? 232 LEU A CB  1 
ATOM   1795 C  CG  . LEU A 1 232 ? 24.974 27.596  -5.580  1.00 14.77 ? 232 LEU A CG  1 
ATOM   1796 C  CD1 . LEU A 1 232 ? 24.874 29.072  -5.890  1.00 17.06 ? 232 LEU A CD1 1 
ATOM   1797 C  CD2 . LEU A 1 232 ? 25.716 27.336  -4.261  1.00 16.68 ? 232 LEU A CD2 1 
ATOM   1798 N  N   . VAL A 1 233 ? 20.840 25.672  -4.974  1.00 8.51  ? 233 VAL A N   1 
ATOM   1799 C  CA  . VAL A 1 233 ? 19.463 25.772  -4.508  1.00 9.79  ? 233 VAL A CA  1 
ATOM   1800 C  C   . VAL A 1 233 ? 19.126 24.597  -3.606  1.00 11.61 ? 233 VAL A C   1 
ATOM   1801 O  O   . VAL A 1 233 ? 18.486 24.765  -2.559  1.00 10.06 ? 233 VAL A O   1 
ATOM   1802 C  CB  . VAL A 1 233 ? 18.497 25.869  -5.700  1.00 10.20 ? 233 VAL A CB  1 
ATOM   1803 C  CG1 . VAL A 1 233 ? 17.072 26.096  -5.195  1.00 9.63  ? 233 VAL A CG1 1 
ATOM   1804 C  CG2 . VAL A 1 233 ? 18.932 26.995  -6.645  1.00 9.99  ? 233 VAL A CG2 1 
ATOM   1805 N  N   . ALA A 1 234 ? 19.580 23.395  -3.975  1.00 9.15  ? 234 ALA A N   1 
ATOM   1806 C  CA  . ALA A 1 234 ? 19.295 22.225  -3.153  1.00 12.53 ? 234 ALA A CA  1 
ATOM   1807 C  C   . ALA A 1 234 ? 19.780 22.425  -1.717  1.00 9.57  ? 234 ALA A C   1 
ATOM   1808 O  O   . ALA A 1 234 ? 19.086 22.057  -0.767  1.00 7.32  ? 234 ALA A O   1 
ATOM   1809 C  CB  . ALA A 1 234 ? 19.914 20.976  -3.783  1.00 7.81  ? 234 ALA A CB  1 
ATOM   1810 N  N   . MET A 1 235 ? 20.949 23.045  -1.537  1.00 10.34 ? 235 MET A N   1 
ATOM   1811 C  CA  . MET A 1 235 ? 21.490 23.213  -0.188  1.00 13.65 ? 235 MET A CA  1 
ATOM   1812 C  C   . MET A 1 235 ? 20.689 24.227  0.622   1.00 12.84 ? 235 MET A C   1 
ATOM   1813 O  O   . MET A 1 235 ? 20.479 24.042  1.826   1.00 13.71 ? 235 MET A O   1 
ATOM   1814 C  CB  . MET A 1 235 ? 22.956 23.634  -0.248  1.00 15.56 ? 235 MET A CB  1 
ATOM   1815 C  CG  . MET A 1 235 ? 23.619 23.650  1.130   1.00 23.57 ? 235 MET A CG  1 
ATOM   1816 S  SD  . MET A 1 235 ? 25.376 23.315  1.032   1.00 50.08 ? 235 MET A SD  1 
ATOM   1817 C  CE  . MET A 1 235 ? 25.889 24.672  -0.019  1.00 27.54 ? 235 MET A CE  1 
ATOM   1818 N  N   . LYS A 1 236 ? 20.257 25.316  -0.013  1.00 16.08 ? 236 LYS A N   1 
ATOM   1819 C  CA  . LYS A 1 236 ? 19.433 26.296  0.685   1.00 12.94 ? 236 LYS A CA  1 
ATOM   1820 C  C   . LYS A 1 236 ? 18.152 25.679  1.218   1.00 12.45 ? 236 LYS A C   1 
ATOM   1821 O  O   . LYS A 1 236 ? 17.654 26.095  2.268   1.00 12.62 ? 236 LYS A O   1 
ATOM   1822 C  CB  . LYS A 1 236 ? 19.100 27.463  -0.244  1.00 15.95 ? 236 LYS A CB  1 
ATOM   1823 C  CG  . LYS A 1 236 ? 18.331 28.574  0.452   1.00 16.48 ? 236 LYS A CG  1 
ATOM   1824 C  CD  . LYS A 1 236 ? 18.515 29.915  -0.235  1.00 21.81 ? 236 LYS A CD  1 
ATOM   1825 C  CE  . LYS A 1 236 ? 17.491 30.941  0.251   1.00 21.36 ? 236 LYS A CE  1 
ATOM   1826 N  NZ  . LYS A 1 236 ? 16.861 31.653  -0.917  1.00 19.01 ? 236 LYS A NZ  1 
ATOM   1827 N  N   . TYR A 1 237 ? 17.595 24.697  0.513   1.00 11.55 ? 237 TYR A N   1 
ATOM   1828 C  CA  . TYR A 1 237 ? 16.297 24.133  0.864   1.00 7.93  ? 237 TYR A CA  1 
ATOM   1829 C  C   . TYR A 1 237 ? 16.418 22.738  1.463   1.00 7.69  ? 237 TYR A C   1 
ATOM   1830 O  O   . TYR A 1 237 ? 15.422 22.006  1.555   1.00 8.61  ? 237 TYR A O   1 
ATOM   1831 C  CB  . TYR A 1 237 ? 15.398 24.136  -0.367  1.00 11.50 ? 237 TYR A CB  1 
ATOM   1832 C  CG  . TYR A 1 237 ? 14.945 25.539  -0.760  1.00 13.90 ? 237 TYR A CG  1 
ATOM   1833 C  CD1 . TYR A 1 237 ? 13.790 26.098  -0.215  1.00 14.66 ? 237 TYR A CD1 1 
ATOM   1834 C  CD2 . TYR A 1 237 ? 15.686 26.310  -1.657  1.00 14.45 ? 237 TYR A CD2 1 
ATOM   1835 C  CE1 . TYR A 1 237 ? 13.368 27.377  -0.566  1.00 17.05 ? 237 TYR A CE1 1 
ATOM   1836 C  CE2 . TYR A 1 237 ? 15.274 27.587  -2.009  1.00 15.64 ? 237 TYR A CE2 1 
ATOM   1837 C  CZ  . TYR A 1 237 ? 14.115 28.113  -1.463  1.00 16.82 ? 237 TYR A CZ  1 
ATOM   1838 O  OH  . TYR A 1 237 ? 13.707 29.380  -1.809  1.00 18.84 ? 237 TYR A OH  1 
ATOM   1839 N  N   . ASN A 1 238 ? 17.623 22.353  1.870   1.00 6.36  ? 238 ASN A N   1 
ATOM   1840 C  CA  . ASN A 1 238 ? 17.854 21.095  2.577   1.00 9.94  ? 238 ASN A CA  1 
ATOM   1841 C  C   . ASN A 1 238 ? 17.473 19.897  1.716   1.00 7.95  ? 238 ASN A C   1 
ATOM   1842 O  O   . ASN A 1 238 ? 16.780 18.977  2.154   1.00 10.61 ? 238 ASN A O   1 
ATOM   1843 C  CB  . ASN A 1 238 ? 17.118 21.065  3.918   1.00 11.06 ? 238 ASN A CB  1 
ATOM   1844 C  CG  . ASN A 1 238 ? 17.548 19.899  4.756   1.00 22.59 ? 238 ASN A CG  1 
ATOM   1845 O  OD1 . ASN A 1 238 ? 18.517 19.218  4.402   1.00 17.57 ? 238 ASN A OD1 1 
ATOM   1846 N  ND2 . ASN A 1 238 ? 16.864 19.664  5.889   1.00 20.38 ? 238 ASN A ND2 1 
ATOM   1847 N  N   . TYR A 1 239 ? 17.968 19.912  0.487   1.00 5.16  ? 239 TYR A N   1 
ATOM   1848 C  CA  . TYR A 1 239 ? 17.837 18.830  -0.460  1.00 6.60  ? 239 TYR A CA  1 
ATOM   1849 C  C   . TYR A 1 239 ? 19.197 18.164  -0.606  1.00 9.18  ? 239 TYR A C   1 
ATOM   1850 O  O   . TYR A 1 239 ? 20.229 18.845  -0.591  1.00 10.35 ? 239 TYR A O   1 
ATOM   1851 C  CB  . TYR A 1 239 ? 17.357 19.367  -1.817  1.00 6.51  ? 239 TYR A CB  1 
ATOM   1852 C  CG  . TYR A 1 239 ? 15.857 19.313  -2.026  1.00 6.37  ? 239 TYR A CG  1 
ATOM   1853 C  CD1 . TYR A 1 239 ? 14.983 20.050  -1.225  1.00 8.20  ? 239 TYR A CD1 1 
ATOM   1854 C  CD2 . TYR A 1 239 ? 15.316 18.505  -3.019  1.00 5.96  ? 239 TYR A CD2 1 
ATOM   1855 C  CE1 . TYR A 1 239 ? 13.591 19.985  -1.426  1.00 9.84  ? 239 TYR A CE1 1 
ATOM   1856 C  CE2 . TYR A 1 239 ? 13.954 18.432  -3.233  1.00 7.56  ? 239 TYR A CE2 1 
ATOM   1857 C  CZ  . TYR A 1 239 ? 13.090 19.166  -2.442  1.00 7.31  ? 239 TYR A CZ  1 
ATOM   1858 O  OH  . TYR A 1 239 ? 11.740 19.072  -2.675  1.00 3.78  ? 239 TYR A OH  1 
ATOM   1859 N  N   . GLU A 1 240 ? 19.197 16.843  -0.730  1.00 7.60  ? 240 GLU A N   1 
ATOM   1860 C  CA  . GLU A 1 240 ? 20.422 16.104  -1.020  1.00 10.84 ? 240 GLU A CA  1 
ATOM   1861 C  C   . GLU A 1 240 ? 21.103 16.704  -2.244  1.00 10.69 ? 240 GLU A C   1 
ATOM   1862 O  O   . GLU A 1 240 ? 20.418 17.080  -3.202  1.00 9.09  ? 240 GLU A O   1 
ATOM   1863 C  CB  . GLU A 1 240 ? 20.108 14.633  -1.305  1.00 10.23 ? 240 GLU A CB  1 
ATOM   1864 C  CG  . GLU A 1 240 ? 20.846 13.609  -0.486  1.00 18.93 ? 240 GLU A CG  1 
ATOM   1865 C  CD  . GLU A 1 240 ? 20.131 12.260  -0.520  1.00 26.15 ? 240 GLU A CD  1 
ATOM   1866 O  OE1 . GLU A 1 240 ? 20.238 11.539  -1.557  1.00 30.35 ? 240 GLU A OE1 1 
ATOM   1867 O  OE2 . GLU A 1 240 ? 19.437 11.938  0.476   1.00 20.42 ? 240 GLU A OE2 1 
ATOM   1868 N  N   . PRO A 1 241 ? 22.430 16.809  -2.255  1.00 10.43 ? 241 PRO A N   1 
ATOM   1869 C  CA  . PRO A 1 241 ? 23.117 17.288  -3.461  1.00 9.15  ? 241 PRO A CA  1 
ATOM   1870 C  C   . PRO A 1 241 ? 22.892 16.310  -4.601  1.00 12.37 ? 241 PRO A C   1 
ATOM   1871 O  O   . PRO A 1 241 ? 22.778 15.099  -4.386  1.00 10.10 ? 241 PRO A O   1 
ATOM   1872 C  CB  . PRO A 1 241 ? 24.590 17.347  -3.038  1.00 12.83 ? 241 PRO A CB  1 
ATOM   1873 C  CG  . PRO A 1 241 ? 24.515 17.521  -1.488  1.00 11.30 ? 241 PRO A CG  1 
ATOM   1874 C  CD  . PRO A 1 241 ? 23.339 16.665  -1.101  1.00 11.12 ? 241 PRO A CD  1 
ATOM   1875 N  N   . LEU A 1 242 ? 22.800 16.849  -5.816  1.00 9.03  ? 242 LEU A N   1 
ATOM   1876 C  CA  . LEU A 1 242 ? 22.590 16.041  -7.010  1.00 10.50 ? 242 LEU A CA  1 
ATOM   1877 C  C   . LEU A 1 242 ? 23.937 15.709  -7.649  1.00 9.72  ? 242 LEU A C   1 
ATOM   1878 O  O   . LEU A 1 242 ? 24.776 16.595  -7.842  1.00 11.92 ? 242 LEU A O   1 
ATOM   1879 C  CB  . LEU A 1 242 ? 21.695 16.783  -8.000  1.00 9.43  ? 242 LEU A CB  1 
ATOM   1880 C  CG  . LEU A 1 242 ? 21.185 15.935  -9.165  1.00 9.56  ? 242 LEU A CG  1 
ATOM   1881 C  CD1 . LEU A 1 242 ? 20.173 14.921  -8.649  1.00 10.35 ? 242 LEU A CD1 1 
ATOM   1882 C  CD2 . LEU A 1 242 ? 20.554 16.802  -10.234 1.00 14.89 ? 242 LEU A CD2 1 
ATOM   1883 N  N   . THR A 1 243 ? 24.149 14.439  -7.963  1.00 7.01  ? 243 THR A N   1 
ATOM   1884 C  CA  . THR A 1 243 ? 25.410 13.989  -8.532  1.00 9.63  ? 243 THR A CA  1 
ATOM   1885 C  C   . THR A 1 243 ? 25.224 13.512  -9.966  1.00 10.32 ? 243 THR A C   1 
ATOM   1886 O  O   . THR A 1 243 ? 24.112 13.283  -10.437 1.00 7.90  ? 243 THR A O   1 
ATOM   1887 C  CB  . THR A 1 243 ? 26.010 12.858  -7.709  1.00 8.82  ? 243 THR A CB  1 
ATOM   1888 O  OG1 . THR A 1 243 ? 25.275 11.662  -7.993  1.00 10.96 ? 243 THR A OG1 1 
ATOM   1889 C  CG2 . THR A 1 243 ? 25.951 13.182  -6.208  1.00 6.40  ? 243 THR A CG2 1 
ATOM   1890 N  N   . GLN A 1 244 ? 26.352 13.325  -10.654 1.00 14.51 ? 244 GLN A N   1 
ATOM   1891 C  CA  . GLN A 1 244 ? 26.299 12.766  -12.002 1.00 14.73 ? 244 GLN A CA  1 
ATOM   1892 C  C   . GLN A 1 244 ? 25.665 11.373  -11.994 1.00 10.99 ? 244 GLN A C   1 
ATOM   1893 O  O   . GLN A 1 244 ? 24.938 11.009  -12.925 1.00 7.20  ? 244 GLN A O   1 
ATOM   1894 C  CB  . GLN A 1 244 ? 27.710 12.733  -12.594 1.00 14.50 ? 244 GLN A CB  1 
ATOM   1895 C  CG  . GLN A 1 244 ? 27.754 12.283  -14.035 1.00 12.17 ? 244 GLN A CG  1 
ATOM   1896 C  CD  . GLN A 1 244 ? 26.904 13.154  -14.911 1.00 14.24 ? 244 GLN A CD  1 
ATOM   1897 O  OE1 . GLN A 1 244 ? 27.028 14.385  -14.897 1.00 17.93 ? 244 GLN A OE1 1 
ATOM   1898 N  NE2 . GLN A 1 244 ? 26.007 12.531  -15.669 1.00 13.40 ? 244 GLN A NE2 1 
ATOM   1899 N  N   . ASP A 1 245 ? 25.917 10.587  -10.937 1.00 9.35  ? 245 ASP A N   1 
ATOM   1900 C  CA  . ASP A 1 245 ? 25.297 9.264   -10.820 1.00 9.02  ? 245 ASP A CA  1 
ATOM   1901 C  C   . ASP A 1 245 ? 23.773 9.357   -10.752 1.00 9.07  ? 245 ASP A C   1 
ATOM   1902 O  O   . ASP A 1 245 ? 23.068 8.499   -11.296 1.00 9.75  ? 245 ASP A O   1 
ATOM   1903 C  CB  . ASP A 1 245 ? 25.823 8.532   -9.583  1.00 10.95 ? 245 ASP A CB  1 
ATOM   1904 C  CG  . ASP A 1 245 ? 27.229 7.993   -9.771  1.00 17.16 ? 245 ASP A CG  1 
ATOM   1905 O  OD1 . ASP A 1 245 ? 27.753 8.038   -10.918 1.00 19.93 ? 245 ASP A OD1 1 
ATOM   1906 O  OD2 . ASP A 1 245 ? 27.816 7.538   -8.758  1.00 17.06 ? 245 ASP A OD2 1 
ATOM   1907 N  N   . HIS A 1 246 ? 23.248 10.357  -10.039 1.00 8.80  ? 246 HIS A N   1 
ATOM   1908 C  CA  . HIS A 1 246 ? 21.807 10.592  -10.026 1.00 7.49  ? 246 HIS A CA  1 
ATOM   1909 C  C   . HIS A 1 246 ? 21.289 10.936  -11.417 1.00 6.79  ? 246 HIS A C   1 
ATOM   1910 O  O   . HIS A 1 246 ? 20.221 10.464  -11.818 1.00 4.80  ? 246 HIS A O   1 
ATOM   1911 C  CB  . HIS A 1 246 ? 21.461 11.725  -9.063  1.00 7.31  ? 246 HIS A CB  1 
ATOM   1912 C  CG  . HIS A 1 246 ? 21.798 11.435  -7.634  1.00 7.04  ? 246 HIS A CG  1 
ATOM   1913 N  ND1 . HIS A 1 246 ? 22.131 12.424  -6.734  1.00 11.26 ? 246 HIS A ND1 1 
ATOM   1914 C  CD2 . HIS A 1 246 ? 21.833 10.272  -6.945  1.00 11.35 ? 246 HIS A CD2 1 
ATOM   1915 C  CE1 . HIS A 1 246 ? 22.381 11.881  -5.557  1.00 11.61 ? 246 HIS A CE1 1 
ATOM   1916 N  NE2 . HIS A 1 246 ? 22.205 10.576  -5.657  1.00 15.11 ? 246 HIS A NE2 1 
ATOM   1917 N  N   . VAL A 1 247 ? 22.010 11.792  -12.147 1.00 5.23  ? 247 VAL A N   1 
ATOM   1918 C  CA  . VAL A 1 247 ? 21.591 12.163  -13.502 1.00 7.10  ? 247 VAL A CA  1 
ATOM   1919 C  C   . VAL A 1 247 ? 21.478 10.921  -14.382 1.00 8.47  ? 247 VAL A C   1 
ATOM   1920 O  O   . VAL A 1 247 ? 20.489 10.737  -15.110 1.00 7.08  ? 247 VAL A O   1 
ATOM   1921 C  CB  . VAL A 1 247 ? 22.572 13.185  -14.110 1.00 9.17  ? 247 VAL A CB  1 
ATOM   1922 C  CG1 . VAL A 1 247 ? 22.348 13.305  -15.622 1.00 7.20  ? 247 VAL A CG1 1 
ATOM   1923 C  CG2 . VAL A 1 247 ? 22.452 14.559  -13.421 1.00 6.21  ? 247 VAL A CG2 1 
ATOM   1924 N  N   . ASP A 1 248 ? 22.519 10.074  -14.355 1.00 4.96  ? 248 ASP A N   1 
ATOM   1925 C  CA  . ASP A 1 248 ? 22.537 8.834   -15.129 1.00 8.14  ? 248 ASP A CA  1 
ATOM   1926 C  C   . ASP A 1 248 ? 21.337 7.940   -14.803 1.00 9.85  ? 248 ASP A C   1 
ATOM   1927 O  O   . ASP A 1 248 ? 20.710 7.369   -15.702 1.00 10.53 ? 248 ASP A O   1 
ATOM   1928 C  CB  . ASP A 1 248 ? 23.842 8.080   -14.859 1.00 7.78  ? 248 ASP A CB  1 
ATOM   1929 C  CG  . ASP A 1 248 ? 25.074 8.846   -15.309 1.00 11.32 ? 248 ASP A CG  1 
ATOM   1930 O  OD1 . ASP A 1 248 ? 24.912 9.882   -15.983 1.00 11.45 ? 248 ASP A OD1 1 
ATOM   1931 O  OD2 . ASP A 1 248 ? 26.204 8.414   -14.976 1.00 12.31 ? 248 ASP A OD2 1 
ATOM   1932 N  N   . ILE A 1 249 ? 21.022 7.782   -13.517 1.00 5.07  ? 249 ILE A N   1 
ATOM   1933 C  CA  . ILE A 1 249 ? 19.882 6.960   -13.114 1.00 6.88  ? 249 ILE A CA  1 
ATOM   1934 C  C   . ILE A 1 249 ? 18.584 7.522   -13.669 1.00 4.75  ? 249 ILE A C   1 
ATOM   1935 O  O   . ILE A 1 249 ? 17.636 6.774   -13.935 1.00 8.59  ? 249 ILE A O   1 
ATOM   1936 C  CB  . ILE A 1 249 ? 19.850 6.842   -11.568 1.00 8.11  ? 249 ILE A CB  1 
ATOM   1937 C  CG1 . ILE A 1 249 ? 20.869 5.792   -11.109 1.00 7.72  ? 249 ILE A CG1 1 
ATOM   1938 C  CG2 . ILE A 1 249 ? 18.425 6.533   -11.056 1.00 10.08 ? 249 ILE A CG2 1 
ATOM   1939 C  CD1 . ILE A 1 249 ? 21.545 6.085   -9.789  1.00 17.60 ? 249 ILE A CD1 1 
ATOM   1940 N  N   . LEU A 1 250 ? 18.508 8.837   -13.843 1.00 4.53  ? 250 LEU A N   1 
ATOM   1941 C  CA  . LEU A 1 250 ? 17.336 9.458   -14.441 1.00 6.10  ? 250 LEU A CA  1 
ATOM   1942 C  C   . LEU A 1 250 ? 17.347 9.391   -15.971 1.00 9.09  ? 250 LEU A C   1 
ATOM   1943 O  O   . LEU A 1 250 ? 16.422 9.914   -16.605 1.00 4.41  ? 250 LEU A O   1 
ATOM   1944 C  CB  . LEU A 1 250 ? 17.242 10.921  -13.993 1.00 4.47  ? 250 LEU A CB  1 
ATOM   1945 C  CG  . LEU A 1 250 ? 16.872 11.173  -12.524 1.00 7.61  ? 250 LEU A CG  1 
ATOM   1946 C  CD1 . LEU A 1 250 ? 17.204 12.616  -12.105 1.00 4.26  ? 250 LEU A CD1 1 
ATOM   1947 C  CD2 . LEU A 1 250 ? 15.405 10.862  -12.282 1.00 4.06  ? 250 LEU A CD2 1 
ATOM   1948 N  N   . GLY A 1 251 ? 18.376 8.797   -16.569 1.00 5.44  ? 251 GLY A N   1 
ATOM   1949 C  CA  . GLY A 1 251 ? 18.511 8.720   -18.010 1.00 7.37  ? 251 GLY A CA  1 
ATOM   1950 C  C   . GLY A 1 251 ? 17.305 8.134   -18.721 1.00 8.56  ? 251 GLY A C   1 
ATOM   1951 O  O   . GLY A 1 251 ? 16.768 8.726   -19.660 1.00 8.40  ? 251 GLY A O   1 
ATOM   1952 N  N   . PRO A 1 252 ? 16.863 6.947   -18.292 1.00 8.49  ? 252 PRO A N   1 
ATOM   1953 C  CA  . PRO A 1 252 ? 15.662 6.351   -18.902 1.00 8.73  ? 252 PRO A CA  1 
ATOM   1954 C  C   . PRO A 1 252 ? 14.467 7.275   -18.928 1.00 9.65  ? 252 PRO A C   1 
ATOM   1955 O  O   . PRO A 1 252 ? 13.858 7.466   -19.986 1.00 10.50 ? 252 PRO A O   1 
ATOM   1956 C  CB  . PRO A 1 252 ? 15.413 5.127   -18.011 1.00 13.41 ? 252 PRO A CB  1 
ATOM   1957 C  CG  . PRO A 1 252 ? 16.784 4.718   -17.610 1.00 15.42 ? 252 PRO A CG  1 
ATOM   1958 C  CD  . PRO A 1 252 ? 17.527 6.008   -17.370 1.00 11.36 ? 252 PRO A CD  1 
ATOM   1959 N  N   . LEU A 1 253 ? 14.101 7.847   -17.778 1.00 7.66  ? 253 LEU A N   1 
ATOM   1960 C  CA  . LEU A 1 253 ? 12.953 8.745   -17.723 1.00 7.75  ? 253 LEU A CA  1 
ATOM   1961 C  C   . LEU A 1 253 ? 13.175 9.985   -18.579 1.00 8.82  ? 253 LEU A C   1 
ATOM   1962 O  O   . LEU A 1 253 ? 12.229 10.508  -19.186 1.00 8.46  ? 253 LEU A O   1 
ATOM   1963 C  CB  . LEU A 1 253 ? 12.677 9.131   -16.268 1.00 4.96  ? 253 LEU A CB  1 
ATOM   1964 C  CG  . LEU A 1 253 ? 12.078 8.013   -15.410 1.00 5.79  ? 253 LEU A CG  1 
ATOM   1965 C  CD1 . LEU A 1 253 ? 12.174 8.377   -13.920 1.00 4.14  ? 253 LEU A CD1 1 
ATOM   1966 C  CD2 . LEU A 1 253 ? 10.628 7.720   -15.866 1.00 7.01  ? 253 LEU A CD2 1 
ATOM   1967 N  N   . SER A 1 254 ? 14.411 10.478  -18.628 1.00 6.15  ? 254 SER A N   1 
ATOM   1968 C  CA  . SER A 1 254 ? 14.722 11.598  -19.503 1.00 8.41  ? 254 SER A CA  1 
ATOM   1969 C  C   . SER A 1 254 ? 14.444 11.232  -20.959 1.00 11.96 ? 254 SER A C   1 
ATOM   1970 O  O   . SER A 1 254 ? 13.822 12.007  -21.700 1.00 12.31 ? 254 SER A O   1 
ATOM   1971 C  CB  . SER A 1 254 ? 16.187 12.007  -19.295 1.00 8.10  ? 254 SER A CB  1 
ATOM   1972 O  OG  . SER A 1 254 ? 16.512 13.169  -20.041 1.00 10.74 ? 254 SER A OG  1 
ATOM   1973 N  N   . ALA A 1 255 ? 14.861 10.028  -21.365 1.00 8.96  ? 255 ALA A N   1 
ATOM   1974 C  CA  . ALA A 1 255 ? 14.699 9.576   -22.745 1.00 13.27 ? 255 ALA A CA  1 
ATOM   1975 C  C   . ALA A 1 255 ? 13.231 9.343   -23.091 1.00 16.02 ? 255 ALA A C   1 
ATOM   1976 O  O   . ALA A 1 255 ? 12.797 9.657   -24.202 1.00 17.00 ? 255 ALA A O   1 
ATOM   1977 C  CB  . ALA A 1 255 ? 15.506 8.295   -22.964 1.00 8.10  ? 255 ALA A CB  1 
ATOM   1978 N  N   . GLN A 1 256 ? 12.461 8.781   -22.157 1.00 12.97 ? 256 GLN A N   1 
ATOM   1979 C  CA  . GLN A 1 256 ? 11.036 8.551   -22.382 1.00 14.73 ? 256 GLN A CA  1 
ATOM   1980 C  C   . GLN A 1 256 ? 10.253 9.851   -22.503 1.00 19.66 ? 256 GLN A C   1 
ATOM   1981 O  O   . GLN A 1 256 ? 9.332  9.949   -23.320 1.00 20.18 ? 256 GLN A O   1 
ATOM   1982 C  CB  . GLN A 1 256 ? 10.454 7.719   -21.248 1.00 19.66 ? 256 GLN A CB  1 
ATOM   1983 C  CG  . GLN A 1 256 ? 8.940  7.652   -21.266 1.00 24.38 ? 256 GLN A CG  1 
ATOM   1984 C  CD  . GLN A 1 256 ? 8.416  6.334   -20.743 1.00 30.50 ? 256 GLN A CD  1 
ATOM   1985 O  OE1 . GLN A 1 256 ? 7.433  5.802   -21.257 1.00 39.37 ? 256 GLN A OE1 1 
ATOM   1986 N  NE2 . GLN A 1 256 ? 9.073  5.797   -19.707 1.00 28.07 ? 256 GLN A NE2 1 
ATOM   1987 N  N   . THR A 1 257 ? 10.556 10.848  -21.673 1.00 15.79 ? 257 THR A N   1 
ATOM   1988 C  CA  . THR A 1 257 ? 9.774  12.074  -21.729 1.00 12.70 ? 257 THR A CA  1 
ATOM   1989 C  C   . THR A 1 257 ? 10.350 13.086  -22.697 1.00 15.71 ? 257 THR A C   1 
ATOM   1990 O  O   . THR A 1 257 ? 9.648  14.032  -23.070 1.00 11.86 ? 257 THR A O   1 
ATOM   1991 C  CB  . THR A 1 257 ? 9.663  12.721  -20.338 1.00 14.02 ? 257 THR A CB  1 
ATOM   1992 O  OG1 . THR A 1 257 ? 10.967 13.107  -19.862 1.00 8.58  ? 257 THR A OG1 1 
ATOM   1993 C  CG2 . THR A 1 257 ? 8.989  11.763  -19.322 1.00 12.78 ? 257 THR A CG2 1 
ATOM   1994 N  N   . GLY A 1 258 ? 11.605 12.911  -23.112 1.00 12.26 ? 258 GLY A N   1 
ATOM   1995 C  CA  . GLY A 1 258 ? 12.263 13.938  -23.877 1.00 11.26 ? 258 GLY A CA  1 
ATOM   1996 C  C   . GLY A 1 258 ? 12.584 15.195  -23.107 1.00 13.59 ? 258 GLY A C   1 
ATOM   1997 O  O   . GLY A 1 258 ? 12.829 16.229  -23.723 1.00 14.53 ? 258 GLY A O   1 
ATOM   1998 N  N   . ILE A 1 259 ? 12.591 15.155  -21.772 1.00 9.64  ? 259 ILE A N   1 
ATOM   1999 C  CA  . ILE A 1 259 ? 12.943 16.326  -20.971 1.00 11.83 ? 259 ILE A CA  1 
ATOM   2000 C  C   . ILE A 1 259 ? 14.310 16.075  -20.346 1.00 11.17 ? 259 ILE A C   1 
ATOM   2001 O  O   . ILE A 1 259 ? 14.467 15.145  -19.542 1.00 8.10  ? 259 ILE A O   1 
ATOM   2002 C  CB  . ILE A 1 259 ? 11.877 16.637  -19.908 1.00 14.74 ? 259 ILE A CB  1 
ATOM   2003 C  CG1 . ILE A 1 259 ? 10.531 16.925  -20.585 1.00 17.19 ? 259 ILE A CG1 1 
ATOM   2004 C  CG2 . ILE A 1 259 ? 12.308 17.797  -19.029 1.00 11.12 ? 259 ILE A CG2 1 
ATOM   2005 C  CD1 . ILE A 1 259 ? 9.483  17.481  -19.645 1.00 15.63 ? 259 ILE A CD1 1 
ATOM   2006 N  N   . ALA A 1 260 ? 15.302 16.887  -20.733 1.00 9.02  ? 260 ALA A N   1 
ATOM   2007 C  CA  . ALA A 1 260 ? 16.658 16.749  -20.198 1.00 10.26 ? 260 ALA A CA  1 
ATOM   2008 C  C   . ALA A 1 260 ? 16.653 16.892  -18.679 1.00 7.61  ? 260 ALA A C   1 
ATOM   2009 O  O   . ALA A 1 260 ? 15.878 17.657  -18.114 1.00 7.19  ? 260 ALA A O   1 
ATOM   2010 C  CB  . ALA A 1 260 ? 17.586 17.809  -20.801 1.00 11.33 ? 260 ALA A CB  1 
ATOM   2011 N  N   . VAL A 1 261 ? 17.561 16.182  -18.010 1.00 9.51  ? 261 VAL A N   1 
ATOM   2012 C  CA  . VAL A 1 261 ? 17.548 16.193  -16.548 1.00 7.01  ? 261 VAL A CA  1 
ATOM   2013 C  C   . VAL A 1 261 ? 17.800 17.595  -16.017 1.00 9.87  ? 261 VAL A C   1 
ATOM   2014 O  O   . VAL A 1 261 ? 17.194 18.014  -15.025 1.00 7.99  ? 261 VAL A O   1 
ATOM   2015 C  CB  . VAL A 1 261 ? 18.570 15.188  -15.987 1.00 10.90 ? 261 VAL A CB  1 
ATOM   2016 C  CG1 . VAL A 1 261 ? 18.810 15.453  -14.506 1.00 6.73  ? 261 VAL A CG1 1 
ATOM   2017 C  CG2 . VAL A 1 261 ? 18.071 13.767  -16.203 1.00 8.79  ? 261 VAL A CG2 1 
ATOM   2018 N  N   . LEU A 1 262 ? 18.704 18.346  -16.661 1.00 10.80 ? 262 LEU A N   1 
ATOM   2019 C  CA  . LEU A 1 262 ? 18.980 19.696  -16.183 1.00 10.63 ? 262 LEU A CA  1 
ATOM   2020 C  C   . LEU A 1 262 ? 17.796 20.626  -16.427 1.00 9.58  ? 262 LEU A C   1 
ATOM   2021 O  O   . LEU A 1 262 ? 17.612 21.607  -15.696 1.00 7.95  ? 262 LEU A O   1 
ATOM   2022 C  CB  . LEU A 1 262 ? 20.242 20.239  -16.844 1.00 12.48 ? 262 LEU A CB  1 
ATOM   2023 C  CG  . LEU A 1 262 ? 21.527 19.523  -16.438 1.00 10.06 ? 262 LEU A CG  1 
ATOM   2024 C  CD1 . LEU A 1 262 ? 22.714 20.214  -17.066 1.00 15.41 ? 262 LEU A CD1 1 
ATOM   2025 C  CD2 . LEU A 1 262 ? 21.671 19.456  -14.914 1.00 15.24 ? 262 LEU A CD2 1 
ATOM   2026 N  N   . ASP A 1 263 ? 16.983 20.332  -17.442 1.00 8.90  ? 263 ASP A N   1 
ATOM   2027 C  CA  . ASP A 1 263 ? 15.736 21.068  -17.624 1.00 12.06 ? 263 ASP A CA  1 
ATOM   2028 C  C   . ASP A 1 263 ? 14.769 20.765  -16.483 1.00 11.35 ? 263 ASP A C   1 
ATOM   2029 O  O   . ASP A 1 263 ? 14.175 21.676  -15.899 1.00 8.41  ? 263 ASP A O   1 
ATOM   2030 C  CB  . ASP A 1 263 ? 15.111 20.731  -18.987 1.00 9.94  ? 263 ASP A CB  1 
ATOM   2031 C  CG  . ASP A 1 263 ? 15.879 21.359  -20.168 1.00 13.49 ? 263 ASP A CG  1 
ATOM   2032 O  OD1 . ASP A 1 263 ? 17.001 21.873  -19.972 1.00 13.42 ? 263 ASP A OD1 1 
ATOM   2033 O  OD2 . ASP A 1 263 ? 15.388 21.297  -21.314 1.00 18.06 ? 263 ASP A OD2 1 
ATOM   2034 N  N   . MET A 1 264 ? 14.615 19.490  -16.124 1.00 6.40  ? 264 MET A N   1 
ATOM   2035 C  CA  . MET A 1 264 ? 13.726 19.199  -15.010 1.00 6.81  ? 264 MET A CA  1 
ATOM   2036 C  C   . MET A 1 264 ? 14.277 19.762  -13.704 1.00 7.54  ? 264 MET A C   1 
ATOM   2037 O  O   . MET A 1 264 ? 13.499 20.140  -12.820 1.00 6.43  ? 264 MET A O   1 
ATOM   2038 C  CB  . MET A 1 264 ? 13.476 17.696  -14.894 1.00 7.61  ? 264 MET A CB  1 
ATOM   2039 C  CG  . MET A 1 264 ? 12.350 17.368  -13.935 1.00 8.13  ? 264 MET A CG  1 
ATOM   2040 S  SD  . MET A 1 264 ? 10.738 17.846  -14.605 1.00 8.39  ? 264 MET A SD  1 
ATOM   2041 C  CE  . MET A 1 264 ? 10.209 16.348  -15.414 1.00 5.22  ? 264 MET A CE  1 
ATOM   2042 N  N   . CYS A 1 265 ? 15.602 19.856  -13.570 1.00 5.54  ? 265 CYS A N   1 
ATOM   2043 C  CA  . CYS A 1 265 ? 16.153 20.523  -12.397 1.00 7.20  ? 265 CYS A CA  1 
ATOM   2044 C  C   . CYS A 1 265 ? 15.772 21.997  -12.363 1.00 8.69  ? 265 CYS A C   1 
ATOM   2045 O  O   . CYS A 1 265 ? 15.600 22.559  -11.278 1.00 8.51  ? 265 CYS A O   1 
ATOM   2046 C  CB  . CYS A 1 265 ? 17.678 20.375  -12.339 1.00 6.47  ? 265 CYS A CB  1 
ATOM   2047 S  SG  . CYS A 1 265 ? 18.305 18.687  -11.989 1.00 8.63  ? 265 CYS A SG  1 
ATOM   2048 N  N   . ALA A 1 266 ? 15.640 22.646  -13.526 1.00 7.48  ? 266 ALA A N   1 
ATOM   2049 C  CA  . ALA A 1 266 ? 15.234 24.049  -13.526 1.00 9.20  ? 266 ALA A CA  1 
ATOM   2050 C  C   . ALA A 1 266 ? 13.776 24.187  -13.103 1.00 9.52  ? 266 ALA A C   1 
ATOM   2051 O  O   . ALA A 1 266 ? 13.405 25.144  -12.410 1.00 12.81 ? 266 ALA A O   1 
ATOM   2052 C  CB  . ALA A 1 266 ? 15.476 24.675  -14.901 1.00 9.71  ? 266 ALA A CB  1 
ATOM   2053 N  N   . SER A 1 267 ? 12.939 23.228  -13.490 1.00 8.36  ? 267 SER A N   1 
ATOM   2054 C  CA  . SER A 1 267 ? 11.586 23.176  -12.958 1.00 8.01  ? 267 SER A CA  1 
ATOM   2055 C  C   . SER A 1 267 ? 11.593 23.044  -11.434 1.00 8.64  ? 267 SER A C   1 
ATOM   2056 O  O   . SER A 1 267 ? 10.863 23.758  -10.734 1.00 7.04  ? 267 SER A O   1 
ATOM   2057 C  CB  . SER A 1 267 ? 10.829 22.015  -13.597 1.00 9.33  ? 267 SER A CB  1 
ATOM   2058 O  OG  . SER A 1 267 ? 10.334 22.377  -14.866 1.00 14.48 ? 267 SER A OG  1 
ATOM   2059 N  N   . LEU A 1 268 ? 12.391 22.112  -10.901 1.00 5.21  ? 268 LEU A N   1 
ATOM   2060 C  CA  . LEU A 1 268 ? 12.401 21.898  -9.458  1.00 6.41  ? 268 LEU A CA  1 
ATOM   2061 C  C   . LEU A 1 268 ? 12.907 23.139  -8.724  1.00 7.33  ? 268 LEU A C   1 
ATOM   2062 O  O   . LEU A 1 268 ? 12.355 23.528  -7.688  1.00 8.50  ? 268 LEU A O   1 
ATOM   2063 C  CB  . LEU A 1 268 ? 13.247 20.667  -9.113  1.00 4.09  ? 268 LEU A CB  1 
ATOM   2064 C  CG  . LEU A 1 268 ? 13.452 20.414  -7.614  1.00 4.23  ? 268 LEU A CG  1 
ATOM   2065 C  CD1 . LEU A 1 268 ? 12.101 20.344  -6.914  1.00 4.30  ? 268 LEU A CD1 1 
ATOM   2066 C  CD2 . LEU A 1 268 ? 14.250 19.156  -7.352  1.00 6.68  ? 268 LEU A CD2 1 
ATOM   2067 N  N   . LYS A 1 269 ? 13.956 23.774  -9.250  1.00 9.92  ? 269 LYS A N   1 
ATOM   2068 C  CA  . LYS A 1 269 ? 14.455 25.028  -8.684  1.00 7.68  ? 269 LYS A CA  1 
ATOM   2069 C  C   . LYS A 1 269 ? 13.364 26.091  -8.616  1.00 10.47 ? 269 LYS A C   1 
ATOM   2070 O  O   . LYS A 1 269 ? 13.227 26.789  -7.601  1.00 11.13 ? 269 LYS A O   1 
ATOM   2071 C  CB  . LYS A 1 269 ? 15.638 25.517  -9.520  1.00 10.43 ? 269 LYS A CB  1 
ATOM   2072 C  CG  . LYS A 1 269 ? 16.126 26.922  -9.241  1.00 14.45 ? 269 LYS A CG  1 
ATOM   2073 C  CD  . LYS A 1 269 ? 17.283 27.250  -10.182 1.00 15.80 ? 269 LYS A CD  1 
ATOM   2074 C  CE  . LYS A 1 269 ? 17.608 28.726  -10.203 1.00 20.22 ? 269 LYS A CE  1 
ATOM   2075 N  NZ  . LYS A 1 269 ? 18.520 29.033  -11.361 1.00 19.01 ? 269 LYS A NZ  1 
ATOM   2076 N  N   . GLU A 1 270 ? 12.560 26.219  -9.678  1.00 11.41 ? 270 GLU A N   1 
ATOM   2077 C  CA  . GLU A 1 270 ? 11.455 27.176  -9.654  1.00 13.68 ? 270 GLU A CA  1 
ATOM   2078 C  C   . GLU A 1 270 ? 10.459 26.836  -8.548  1.00 13.77 ? 270 GLU A C   1 
ATOM   2079 O  O   . GLU A 1 270 ? 9.939  27.737  -7.875  1.00 14.51 ? 270 GLU A O   1 
ATOM   2080 C  CB  . GLU A 1 270 ? 10.749 27.226  -11.020 1.00 15.63 ? 270 GLU A CB  1 
ATOM   2081 C  CG  . GLU A 1 270 ? 9.848  28.482  -11.242 1.00 21.89 ? 270 GLU A CG  1 
ATOM   2082 C  CD  . GLU A 1 270 ? 9.527  28.763  -12.720 1.00 26.70 ? 270 GLU A CD  1 
ATOM   2083 O  OE1 . GLU A 1 270 ? 9.112  27.818  -13.439 1.00 26.82 ? 270 GLU A OE1 1 
ATOM   2084 O  OE2 . GLU A 1 270 ? 9.700  29.923  -13.169 1.00 27.53 ? 270 GLU A OE2 1 
ATOM   2085 N  N   . LEU A 1 271 ? 10.182 25.538  -8.346  1.00 12.42 ? 271 LEU A N   1 
ATOM   2086 C  CA  . LEU A 1 271 ? 9.223  25.112  -7.322  1.00 12.08 ? 271 LEU A CA  1 
ATOM   2087 C  C   . LEU A 1 271 ? 9.770  25.327  -5.918  1.00 12.42 ? 271 LEU A C   1 
ATOM   2088 O  O   . LEU A 1 271 ? 9.023  25.679  -4.999  1.00 13.29 ? 271 LEU A O   1 
ATOM   2089 C  CB  . LEU A 1 271 ? 8.853  23.634  -7.510  1.00 11.77 ? 271 LEU A CB  1 
ATOM   2090 C  CG  . LEU A 1 271 ? 8.016  23.237  -8.734  1.00 10.33 ? 271 LEU A CG  1 
ATOM   2091 C  CD1 . LEU A 1 271 ? 8.175  21.739  -9.091  1.00 7.64  ? 271 LEU A CD1 1 
ATOM   2092 C  CD2 . LEU A 1 271 ? 6.549  23.597  -8.508  1.00 11.29 ? 271 LEU A CD2 1 
ATOM   2093 N  N   . LEU A 1 272 ? 11.060 25.083  -5.720  1.00 11.60 ? 272 LEU A N   1 
ATOM   2094 C  CA  . LEU A 1 272 ? 11.639 25.316  -4.407  1.00 13.35 ? 272 LEU A CA  1 
ATOM   2095 C  C   . LEU A 1 272 ? 11.646 26.796  -4.067  1.00 13.86 ? 272 LEU A C   1 
ATOM   2096 O  O   . LEU A 1 272 ? 11.352 27.168  -2.926  1.00 15.16 ? 272 LEU A O   1 
ATOM   2097 C  CB  . LEU A 1 272 ? 13.048 24.743  -4.344  1.00 12.23 ? 272 LEU A CB  1 
ATOM   2098 C  CG  . LEU A 1 272 ? 13.021 23.218  -4.348  1.00 9.27  ? 272 LEU A CG  1 
ATOM   2099 C  CD1 . LEU A 1 272 ? 14.433 22.703  -4.516  1.00 6.71  ? 272 LEU A CD1 1 
ATOM   2100 C  CD2 . LEU A 1 272 ? 12.352 22.685  -3.068  1.00 10.54 ? 272 LEU A CD2 1 
ATOM   2101 N  N   . GLN A 1 273 ? 11.955 27.654  -5.048  1.00 15.14 ? 273 GLN A N   1 
ATOM   2102 C  CA  . GLN A 1 273 ? 12.027 29.099  -4.820  1.00 18.23 ? 273 GLN A CA  1 
ATOM   2103 C  C   . GLN A 1 273 ? 10.659 29.775  -4.757  1.00 15.43 ? 273 GLN A C   1 
ATOM   2104 O  O   . GLN A 1 273 ? 10.524 30.804  -4.093  1.00 18.37 ? 273 GLN A O   1 
ATOM   2105 C  CB  . GLN A 1 273 ? 12.879 29.770  -5.904  1.00 15.27 ? 273 GLN A CB  1 
ATOM   2106 C  CG  . GLN A 1 273 ? 14.381 29.545  -5.755  1.00 15.62 ? 273 GLN A CG  1 
ATOM   2107 C  CD  . GLN A 1 273 ? 15.174 29.985  -6.972  1.00 15.78 ? 273 GLN A CD  1 
ATOM   2108 O  OE1 . GLN A 1 273 ? 14.611 30.380  -8.001  1.00 22.95 ? 273 GLN A OE1 1 
ATOM   2109 N  NE2 . GLN A 1 273 ? 16.485 29.916  -6.867  1.00 14.01 ? 273 GLN A NE2 1 
ATOM   2110 N  N   . ASN A 1 274 ? 9.635  29.238  -5.412  1.00 17.75 ? 274 ASN A N   1 
ATOM   2111 C  CA  . ASN A 1 274 ? 8.348  29.925  -5.473  1.00 17.77 ? 274 ASN A CA  1 
ATOM   2112 C  C   . ASN A 1 274 ? 7.201  29.121  -4.885  1.00 17.21 ? 274 ASN A C   1 
ATOM   2113 O  O   . ASN A 1 274 ? 6.074  29.625  -4.837  1.00 14.14 ? 274 ASN A O   1 
ATOM   2114 C  CB  . ASN A 1 274 ? 7.986  30.306  -6.924  1.00 13.74 ? 274 ASN A CB  1 
ATOM   2115 C  CG  . ASN A 1 274 ? 9.107  31.042  -7.648  1.00 19.83 ? 274 ASN A CG  1 
ATOM   2116 O  OD1 . ASN A 1 274 ? 9.689  31.986  -7.123  1.00 26.78 ? 274 ASN A OD1 1 
ATOM   2117 N  ND2 . ASN A 1 274 ? 9.391  30.624  -8.879  1.00 22.10 ? 274 ASN A ND2 1 
ATOM   2118 N  N   . GLY A 1 275 ? 7.446  27.897  -4.432  1.00 20.24 ? 275 GLY A N   1 
ATOM   2119 C  CA  . GLY A 1 275 ? 6.361  27.072  -3.947  1.00 13.57 ? 275 GLY A CA  1 
ATOM   2120 C  C   . GLY A 1 275 ? 5.465  26.644  -5.095  1.00 14.63 ? 275 GLY A C   1 
ATOM   2121 O  O   . GLY A 1 275 ? 5.766  26.829  -6.269  1.00 15.79 ? 275 GLY A O   1 
ATOM   2122 N  N   . MET A 1 276 ? 4.321  26.076  -4.720  1.00 18.01 ? 276 MET A N   1 
ATOM   2123 C  CA  . MET A 1 276 ? 3.377  25.508  -5.669  1.00 16.23 ? 276 MET A CA  1 
ATOM   2124 C  C   . MET A 1 276 ? 2.213  26.429  -6.011  1.00 22.09 ? 276 MET A C   1 
ATOM   2125 O  O   . MET A 1 276 ? 1.510  26.160  -6.993  1.00 23.29 ? 276 MET A O   1 
ATOM   2126 C  CB  . MET A 1 276 ? 2.839  24.173  -5.137  1.00 19.62 ? 276 MET A CB  1 
ATOM   2127 C  CG  . MET A 1 276 ? 3.850  23.045  -5.252  1.00 15.87 ? 276 MET A CG  1 
ATOM   2128 S  SD  . MET A 1 276 ? 3.080  21.477  -5.701  1.00 29.15 ? 276 MET A SD  1 
ATOM   2129 C  CE  . MET A 1 276 ? 3.953  20.435  -4.551  1.00 16.43 ? 276 MET A CE  1 
ATOM   2130 N  N   . ASN A 1 277 ? 1.992  27.506  -5.253  1.00 19.86 ? 277 ASN A N   1 
ATOM   2131 C  CA  . ASN A 1 277 ? 0.939  28.460  -5.580  1.00 22.45 ? 277 ASN A CA  1 
ATOM   2132 C  C   . ASN A 1 277 ? -0.448 27.861  -5.369  1.00 25.81 ? 277 ASN A C   1 
ATOM   2133 O  O   . ASN A 1 277 ? -1.411 28.228  -6.053  1.00 28.15 ? 277 ASN A O   1 
ATOM   2134 C  CB  . ASN A 1 277 ? 1.091  28.957  -7.019  1.00 26.22 ? 277 ASN A CB  1 
ATOM   2135 C  CG  . ASN A 1 277 ? 0.836  30.435  -7.152  1.00 33.52 ? 277 ASN A CG  1 
ATOM   2136 O  OD1 . ASN A 1 277 ? 1.264  31.227  -6.311  1.00 35.34 ? 277 ASN A OD1 1 
ATOM   2137 N  ND2 . ASN A 1 277 ? 0.141  30.822  -8.217  1.00 37.27 ? 277 ASN A ND2 1 
ATOM   2138 N  N   . GLY A 1 278 ? -0.564 26.923  -4.436  1.00 19.84 ? 278 GLY A N   1 
ATOM   2139 C  CA  . GLY A 1 278 ? -1.851 26.318  -4.194  1.00 19.81 ? 278 GLY A CA  1 
ATOM   2140 C  C   . GLY A 1 278 ? -2.307 25.336  -5.245  1.00 23.38 ? 278 GLY A C   1 
ATOM   2141 O  O   . GLY A 1 278 ? -3.476 24.934  -5.229  1.00 23.57 ? 278 GLY A O   1 
ATOM   2142 N  N   . ARG A 1 279 ? -1.428 24.938  -6.161  1.00 20.16 ? 279 ARG A N   1 
ATOM   2143 C  CA  . ARG A 1 279 ? -1.754 23.919  -7.141  1.00 20.59 ? 279 ARG A CA  1 
ATOM   2144 C  C   . ARG A 1 279 ? -1.299 22.550  -6.630  1.00 16.74 ? 279 ARG A C   1 
ATOM   2145 O  O   . ARG A 1 279 ? -0.754 22.410  -5.532  1.00 13.83 ? 279 ARG A O   1 
ATOM   2146 C  CB  . ARG A 1 279 ? -1.118 24.275  -8.480  1.00 22.34 ? 279 ARG A CB  1 
ATOM   2147 C  CG  . ARG A 1 279 ? -0.913 25.774  -8.625  1.00 25.27 ? 279 ARG A CG  1 
ATOM   2148 C  CD  . ARG A 1 279 ? -0.563 26.167  -10.035 1.00 20.46 ? 279 ARG A CD  1 
ATOM   2149 N  NE  . ARG A 1 279 ? -1.296 25.399  -11.032 1.00 25.95 ? 279 ARG A NE  1 
ATOM   2150 C  CZ  . ARG A 1 279 ? -1.014 25.413  -12.330 1.00 31.01 ? 279 ARG A CZ  1 
ATOM   2151 N  NH1 . ARG A 1 279 ? 0.017  26.098  -12.808 1.00 28.11 ? 279 ARG A NH1 1 
ATOM   2152 N  NH2 . ARG A 1 279 ? -1.788 24.729  -13.170 1.00 30.12 ? 279 ARG A NH2 1 
ATOM   2153 N  N   . THR A 1 280 ? -1.535 21.517  -7.425  1.00 16.14 ? 280 THR A N   1 
ATOM   2154 C  CA  . THR A 1 280 ? -1.187 20.170  -7.019  1.00 12.75 ? 280 THR A CA  1 
ATOM   2155 C  C   . THR A 1 280 ? -0.465 19.443  -8.144  1.00 12.73 ? 280 THR A C   1 
ATOM   2156 O  O   . THR A 1 280 ? -0.644 19.743  -9.329  1.00 13.48 ? 280 THR A O   1 
ATOM   2157 C  CB  . THR A 1 280 ? -2.436 19.384  -6.584  1.00 14.97 ? 280 THR A CB  1 
ATOM   2158 O  OG1 . THR A 1 280 ? -3.442 19.465  -7.608  1.00 14.47 ? 280 THR A OG1 1 
ATOM   2159 C  CG2 . THR A 1 280 ? -2.975 19.923  -5.228  1.00 9.60  ? 280 THR A CG2 1 
ATOM   2160 N  N   . ILE A 1 281 ? 0.353  18.474  -7.741  1.00 10.09 ? 281 ILE A N   1 
ATOM   2161 C  CA  . ILE A 1 281 ? 1.103  17.603  -8.636  1.00 7.49  ? 281 ILE A CA  1 
ATOM   2162 C  C   . ILE A 1 281 ? 0.769  16.163  -8.270  1.00 10.83 ? 281 ILE A C   1 
ATOM   2163 O  O   . ILE A 1 281 ? 1.037  15.725  -7.143  1.00 9.04  ? 281 ILE A O   1 
ATOM   2164 C  CB  . ILE A 1 281 ? 2.620  17.846  -8.534  1.00 8.98  ? 281 ILE A CB  1 
ATOM   2165 C  CG1 . ILE A 1 281 ? 2.948  19.314  -8.865  1.00 10.03 ? 281 ILE A CG1 1 
ATOM   2166 C  CG2 . ILE A 1 281 ? 3.375  16.866  -9.436  1.00 9.11  ? 281 ILE A CG2 1 
ATOM   2167 C  CD1 . ILE A 1 281 ? 4.432  19.642  -9.051  1.00 9.00  ? 281 ILE A CD1 1 
ATOM   2168 N  N   . LEU A 1 282 ? 0.197  15.420  -9.214  1.00 10.55 ? 282 LEU A N   1 
ATOM   2169 C  CA  . LEU A 1 282 ? -0.186 14.036  -8.935  1.00 14.44 ? 282 LEU A CA  1 
ATOM   2170 C  C   . LEU A 1 282 ? -0.938 13.940  -7.605  1.00 15.18 ? 282 LEU A C   1 
ATOM   2171 O  O   . LEU A 1 282 ? -0.688 13.048  -6.793  1.00 9.94  ? 282 LEU A O   1 
ATOM   2172 C  CB  . LEU A 1 282 ? 1.042  13.118  -8.920  1.00 9.27  ? 282 LEU A CB  1 
ATOM   2173 C  CG  . LEU A 1 282 ? 1.715  12.810  -10.261 1.00 10.77 ? 282 LEU A CG  1 
ATOM   2174 C  CD1 . LEU A 1 282 ? 2.869  11.809  -10.077 1.00 7.59  ? 282 LEU A CD1 1 
ATOM   2175 C  CD2 . LEU A 1 282 ? 0.692  12.288  -11.283 1.00 9.43  ? 282 LEU A CD2 1 
ATOM   2176 N  N   . GLY A 1 283 ? -1.830 14.902  -7.356  1.00 11.03 ? 283 GLY A N   1 
ATOM   2177 C  CA  . GLY A 1 283 ? -2.651 14.885  -6.162  1.00 11.02 ? 283 GLY A CA  1 
ATOM   2178 C  C   . GLY A 1 283 ? -1.968 15.301  -4.878  1.00 13.84 ? 283 GLY A C   1 
ATOM   2179 O  O   . GLY A 1 283 ? -2.521 15.055  -3.798  1.00 15.53 ? 283 GLY A O   1 
ATOM   2180 N  N   . SER A 1 284 ? -0.796 15.930  -4.946  1.00 7.65  ? 284 SER A N   1 
ATOM   2181 C  CA  . SER A 1 284 ? -0.056 16.313  -3.751  1.00 10.51 ? 284 SER A CA  1 
ATOM   2182 C  C   . SER A 1 284 ? 0.205  17.815  -3.764  1.00 12.32 ? 284 SER A C   1 
ATOM   2183 O  O   . SER A 1 284 ? 0.449  18.405  -4.827  1.00 4.93  ? 284 SER A O   1 
ATOM   2184 C  CB  . SER A 1 284 ? 1.267  15.524  -3.647  1.00 11.28 ? 284 SER A CB  1 
ATOM   2185 O  OG  . SER A 1 284 ? 1.983  15.850  -2.467  1.00 10.36 ? 284 SER A OG  1 
ATOM   2186 N  N   . ALA A 1 285 ? 0.129  18.435  -2.581  1.00 8.52  ? 285 ALA A N   1 
ATOM   2187 C  CA  . ALA A 1 285 ? 0.412  19.857  -2.428  1.00 7.08  ? 285 ALA A CA  1 
ATOM   2188 C  C   . ALA A 1 285 ? 1.844  20.112  -1.988  1.00 10.27 ? 285 ALA A C   1 
ATOM   2189 O  O   . ALA A 1 285 ? 2.197  21.254  -1.662  1.00 8.40  ? 285 ALA A O   1 
ATOM   2190 C  CB  . ALA A 1 285 ? -0.564 20.490  -1.439  1.00 10.83 ? 285 ALA A CB  1 
ATOM   2191 N  N   . LEU A 1 286 ? 2.673  19.075  -1.960  1.00 10.27 ? 286 LEU A N   1 
ATOM   2192 C  CA  . LEU A 1 286 ? 4.084  19.227  -1.645  1.00 12.41 ? 286 LEU A CA  1 
ATOM   2193 C  C   . LEU A 1 286 ? 4.884  18.265  -2.510  1.00 11.52 ? 286 LEU A C   1 
ATOM   2194 O  O   . LEU A 1 286 ? 4.330  17.402  -3.203  1.00 8.31  ? 286 LEU A O   1 
ATOM   2195 C  CB  . LEU A 1 286 ? 4.360  19.034  -0.142  1.00 10.56 ? 286 LEU A CB  1 
ATOM   2196 C  CG  . LEU A 1 286 ? 3.680  17.915  0.647   1.00 16.48 ? 286 LEU A CG  1 
ATOM   2197 C  CD1 . LEU A 1 286 ? 4.124  16.544  0.155   1.00 16.33 ? 286 LEU A CD1 1 
ATOM   2198 C  CD2 . LEU A 1 286 ? 3.926  18.097  2.171   1.00 13.45 ? 286 LEU A CD2 1 
ATOM   2199 N  N   . LEU A 1 287 ? 6.202  18.448  -2.496  1.00 8.51  ? 287 LEU A N   1 
ATOM   2200 C  CA  . LEU A 1 287 ? 7.087  17.675  -3.355  1.00 9.22  ? 287 LEU A CA  1 
ATOM   2201 C  C   . LEU A 1 287 ? 7.321  16.304  -2.729  1.00 5.63  ? 287 LEU A C   1 
ATOM   2202 O  O   . LEU A 1 287 ? 7.857  16.222  -1.628  1.00 4.65  ? 287 LEU A O   1 
ATOM   2203 C  CB  . LEU A 1 287 ? 8.398  18.439  -3.551  1.00 8.87  ? 287 LEU A CB  1 
ATOM   2204 C  CG  . LEU A 1 287 ? 8.150  19.808  -4.206  1.00 10.87 ? 287 LEU A CG  1 
ATOM   2205 C  CD1 . LEU A 1 287 ? 9.336  20.760  -4.091  1.00 10.99 ? 287 LEU A CD1 1 
ATOM   2206 C  CD2 . LEU A 1 287 ? 7.725  19.648  -5.671  1.00 11.15 ? 287 LEU A CD2 1 
ATOM   2207 N  N   . GLU A 1 288 ? 6.926  15.226  -3.416  1.00 5.99  ? 288 GLU A N   1 
ATOM   2208 C  CA  . GLU A 1 288 ? 7.114  13.876  -2.882  1.00 7.03  ? 288 GLU A CA  1 
ATOM   2209 C  C   . GLU A 1 288 ? 8.501  13.314  -3.190  1.00 5.78  ? 288 GLU A C   1 
ATOM   2210 O  O   . GLU A 1 288 ? 8.980  13.385  -4.326  1.00 3.53  ? 288 GLU A O   1 
ATOM   2211 C  CB  . GLU A 1 288 ? 6.063  12.904  -3.429  1.00 5.79  ? 288 GLU A CB  1 
ATOM   2212 C  CG  . GLU A 1 288 ? 4.629  13.349  -3.258  1.00 10.53 ? 288 GLU A CG  1 
ATOM   2213 C  CD  . GLU A 1 288 ? 4.137  13.080  -1.828  1.00 22.73 ? 288 GLU A CD  1 
ATOM   2214 O  OE1 . GLU A 1 288 ? 3.371  13.914  -1.288  1.00 20.55 ? 288 GLU A OE1 1 
ATOM   2215 O  OE2 . GLU A 1 288 ? 4.578  12.059  -1.238  1.00 16.22 ? 288 GLU A OE2 1 
ATOM   2216 N  N   . ASP A 1 289 ? 9.125  12.690  -2.184  1.00 5.56  ? 289 ASP A N   1 
ATOM   2217 C  CA  . ASP A 1 289 ? 10.462 12.138  -2.378  1.00 4.97  ? 289 ASP A CA  1 
ATOM   2218 C  C   . ASP A 1 289 ? 10.554 10.664  -2.018  1.00 5.09  ? 289 ASP A C   1 
ATOM   2219 O  O   . ASP A 1 289 ? 11.658 10.173  -1.777  1.00 6.26  ? 289 ASP A O   1 
ATOM   2220 C  CB  . ASP A 1 289 ? 11.525 12.928  -1.594  1.00 5.11  ? 289 ASP A CB  1 
ATOM   2221 C  CG  . ASP A 1 289 ? 11.557 12.584  -0.094  1.00 8.29  ? 289 ASP A CG  1 
ATOM   2222 O  OD1 . ASP A 1 289 ? 10.586 11.980  0.421   1.00 3.14  ? 289 ASP A OD1 1 
ATOM   2223 O  OD2 . ASP A 1 289 ? 12.562 12.929  0.582   1.00 6.21  ? 289 ASP A OD2 1 
ATOM   2224 N  N   . GLU A 1 290 ? 9.443  9.927   -1.998  1.00 4.27  ? 290 GLU A N   1 
ATOM   2225 C  CA  . GLU A 1 290 ? 9.504  8.515   -1.641  1.00 8.06  ? 290 GLU A CA  1 
ATOM   2226 C  C   . GLU A 1 290 ? 9.175  7.600   -2.822  1.00 8.76  ? 290 GLU A C   1 
ATOM   2227 O  O   . GLU A 1 290 ? 8.764  6.457   -2.617  1.00 9.79  ? 290 GLU A O   1 
ATOM   2228 C  CB  . GLU A 1 290 ? 8.599  8.213   -0.438  1.00 8.52  ? 290 GLU A CB  1 
ATOM   2229 C  CG  . GLU A 1 290 ? 8.944  9.076   0.789   1.00 9.61  ? 290 GLU A CG  1 
ATOM   2230 C  CD  . GLU A 1 290 ? 8.836  8.364   2.151   1.00 19.69 ? 290 GLU A CD  1 
ATOM   2231 O  OE1 . GLU A 1 290 ? 7.882  7.567   2.373   1.00 11.13 ? 290 GLU A OE1 1 
ATOM   2232 O  OE2 . GLU A 1 290 ? 9.709  8.645   3.025   1.00 17.19 ? 290 GLU A OE2 1 
ATOM   2233 N  N   . PHE A 1 291 ? 9.382  8.065   -4.062  1.00 4.48  ? 291 PHE A N   1 
ATOM   2234 C  CA  . PHE A 1 291 ? 9.438  7.178   -5.230  1.00 6.64  ? 291 PHE A CA  1 
ATOM   2235 C  C   . PHE A 1 291 ? 10.820 7.256   -5.858  1.00 6.21  ? 291 PHE A C   1 
ATOM   2236 O  O   . PHE A 1 291 ? 11.240 8.333   -6.294  1.00 4.28  ? 291 PHE A O   1 
ATOM   2237 C  CB  . PHE A 1 291 ? 8.408  7.544   -6.297  1.00 6.12  ? 291 PHE A CB  1 
ATOM   2238 C  CG  . PHE A 1 291 ? 6.997  7.519   -5.827  1.00 10.38 ? 291 PHE A CG  1 
ATOM   2239 C  CD1 . PHE A 1 291 ? 6.260  6.341   -5.869  1.00 10.95 ? 291 PHE A CD1 1 
ATOM   2240 C  CD2 . PHE A 1 291 ? 6.386  8.686   -5.373  1.00 8.10  ? 291 PHE A CD2 1 
ATOM   2241 C  CE1 . PHE A 1 291 ? 4.925  6.325   -5.457  1.00 10.09 ? 291 PHE A CE1 1 
ATOM   2242 C  CE2 . PHE A 1 291 ? 5.056  8.682   -4.959  1.00 9.12  ? 291 PHE A CE2 1 
ATOM   2243 C  CZ  . PHE A 1 291 ? 4.326  7.495   -4.994  1.00 9.82  ? 291 PHE A CZ  1 
ATOM   2244 N  N   . THR A 1 292 ? 11.518 6.120   -5.937  1.00 5.45  ? 292 THR A N   1 
ATOM   2245 C  CA  . THR A 1 292 ? 12.774 6.105   -6.669  1.00 7.23  ? 292 THR A CA  1 
ATOM   2246 C  C   . THR A 1 292 ? 12.520 6.143   -8.179  1.00 8.15  ? 292 THR A C   1 
ATOM   2247 O  O   . THR A 1 292 ? 11.412 5.860   -8.647  1.00 8.04  ? 292 THR A O   1 
ATOM   2248 C  CB  . THR A 1 292 ? 13.577 4.852   -6.355  1.00 7.59  ? 292 THR A CB  1 
ATOM   2249 O  OG1 . THR A 1 292 ? 12.896 3.729   -6.920  1.00 8.66  ? 292 THR A OG1 1 
ATOM   2250 C  CG2 . THR A 1 292 ? 13.728 4.659   -4.869  1.00 8.82  ? 292 THR A CG2 1 
ATOM   2251 N  N   . PRO A 1 293 ? 13.539 6.459   -8.968  1.00 5.53  ? 293 PRO A N   1 
ATOM   2252 C  CA  . PRO A 1 293 ? 13.394 6.290   -10.424 1.00 5.40  ? 293 PRO A CA  1 
ATOM   2253 C  C   . PRO A 1 293 ? 12.924 4.896   -10.818 1.00 8.77  ? 293 PRO A C   1 
ATOM   2254 O  O   . PRO A 1 293 ? 12.102 4.766   -11.728 1.00 6.08  ? 293 PRO A O   1 
ATOM   2255 C  CB  . PRO A 1 293 ? 14.803 6.590   -10.945 1.00 4.35  ? 293 PRO A CB  1 
ATOM   2256 C  CG  . PRO A 1 293 ? 15.346 7.556   -9.959  1.00 6.03  ? 293 PRO A CG  1 
ATOM   2257 C  CD  . PRO A 1 293 ? 14.829 7.074   -8.613  1.00 7.72  ? 293 PRO A CD  1 
ATOM   2258 N  N   . PHE A 1 294 ? 13.405 3.847   -10.144 1.00 9.42  ? 294 PHE A N   1 
ATOM   2259 C  CA  . PHE A 1 294 ? 12.935 2.502   -10.463 1.00 11.35 ? 294 PHE A CA  1 
ATOM   2260 C  C   . PHE A 1 294 ? 11.439 2.364   -10.195 1.00 12.60 ? 294 PHE A C   1 
ATOM   2261 O  O   . PHE A 1 294 ? 10.699 1.797   -11.011 1.00 14.02 ? 294 PHE A O   1 
ATOM   2262 C  CB  . PHE A 1 294 ? 13.752 1.475   -9.674  1.00 18.47 ? 294 PHE A CB  1 
ATOM   2263 C  CG  . PHE A 1 294 ? 13.611 0.063   -10.177 1.00 27.42 ? 294 PHE A CG  1 
ATOM   2264 C  CD1 . PHE A 1 294 ? 12.390 -0.604  -10.105 1.00 28.02 ? 294 PHE A CD1 1 
ATOM   2265 C  CD2 . PHE A 1 294 ? 14.690 -0.590  -10.758 1.00 33.17 ? 294 PHE A CD2 1 
ATOM   2266 C  CE1 . PHE A 1 294 ? 12.256 -1.909  -10.578 1.00 31.51 ? 294 PHE A CE1 1 
ATOM   2267 C  CE2 . PHE A 1 294 ? 14.563 -1.895  -11.230 1.00 35.24 ? 294 PHE A CE2 1 
ATOM   2268 C  CZ  . PHE A 1 294 ? 13.344 -2.552  -11.141 1.00 34.54 ? 294 PHE A CZ  1 
ATOM   2269 N  N   . ASP A 1 295 ? 10.972 2.901   -9.069  1.00 10.77 ? 295 ASP A N   1 
ATOM   2270 C  CA  . ASP A 1 295 ? 9.547  2.859   -8.747  1.00 12.17 ? 295 ASP A CA  1 
ATOM   2271 C  C   . ASP A 1 295 ? 8.706  3.539   -9.830  1.00 10.77 ? 295 ASP A C   1 
ATOM   2272 O  O   . ASP A 1 295 ? 7.612  3.067   -10.169 1.00 9.14  ? 295 ASP A O   1 
ATOM   2273 C  CB  . ASP A 1 295 ? 9.287  3.521   -7.386  1.00 6.15  ? 295 ASP A CB  1 
ATOM   2274 C  CG  . ASP A 1 295 ? 10.012 2.834   -6.226  1.00 12.86 ? 295 ASP A CG  1 
ATOM   2275 O  OD1 . ASP A 1 295 ? 10.454 1.677   -6.389  1.00 11.57 ? 295 ASP A OD1 1 
ATOM   2276 O  OD2 . ASP A 1 295 ? 10.133 3.455   -5.127  1.00 12.56 ? 295 ASP A OD2 1 
ATOM   2277 N  N   . VAL A 1 296 ? 9.185  4.659   -10.370 1.00 6.65  ? 296 VAL A N   1 
ATOM   2278 C  CA  . VAL A 1 296 ? 8.403  5.396   -11.361 1.00 6.92  ? 296 VAL A CA  1 
ATOM   2279 C  C   . VAL A 1 296 ? 8.258  4.582   -12.652 1.00 12.25 ? 296 VAL A C   1 
ATOM   2280 O  O   . VAL A 1 296 ? 7.164  4.472   -13.220 1.00 13.07 ? 296 VAL A O   1 
ATOM   2281 C  CB  . VAL A 1 296 ? 9.048  6.771   -11.625 1.00 8.36  ? 296 VAL A CB  1 
ATOM   2282 C  CG1 . VAL A 1 296 ? 8.376  7.440   -12.820 1.00 8.13  ? 296 VAL A CG1 1 
ATOM   2283 C  CG2 . VAL A 1 296 ? 8.966  7.648   -10.397 1.00 6.32  ? 296 VAL A CG2 1 
ATOM   2284 N  N   . VAL A 1 297 ? 9.361  3.995   -13.129 1.00 11.51 ? 297 VAL A N   1 
ATOM   2285 C  CA  . VAL A 1 297 ? 9.337  3.192   -14.350 1.00 18.01 ? 297 VAL A CA  1 
ATOM   2286 C  C   . VAL A 1 297 ? 8.521  1.912   -14.156 1.00 18.35 ? 297 VAL A C   1 
ATOM   2287 O  O   . VAL A 1 297 ? 7.768  1.502   -15.048 1.00 18.25 ? 297 VAL A O   1 
ATOM   2288 C  CB  . VAL A 1 297 ? 10.774 2.875   -14.798 1.00 11.36 ? 297 VAL A CB  1 
ATOM   2289 C  CG1 . VAL A 1 297 ? 10.760 1.760   -15.826 1.00 14.14 ? 297 VAL A CG1 1 
ATOM   2290 C  CG2 . VAL A 1 297 ? 11.444 4.108   -15.355 1.00 13.69 ? 297 VAL A CG2 1 
ATOM   2291 N  N   . ARG A 1 298 ? 8.676  1.242   -13.012 1.00 16.58 ? 298 ARG A N   1 
ATOM   2292 C  CA  . ARG A 1 298 ? 7.848  0.074   -12.733 1.00 23.47 ? 298 ARG A CA  1 
ATOM   2293 C  C   . ARG A 1 298 ? 6.364  0.429   -12.824 1.00 23.79 ? 298 ARG A C   1 
ATOM   2294 O  O   . ARG A 1 298 ? 5.590  -0.256  -13.504 1.00 28.19 ? 298 ARG A O   1 
ATOM   2295 C  CB  . ARG A 1 298 ? 8.201  -0.509  -11.360 1.00 20.62 ? 298 ARG A CB  1 
ATOM   2296 C  CG  . ARG A 1 298 ? 7.390  -1.754  -10.962 1.00 34.59 ? 298 ARG A CG  1 
ATOM   2297 C  CD  . ARG A 1 298 ? 7.444  -2.073  -9.448  1.00 33.90 ? 298 ARG A CD  1 
ATOM   2298 N  NE  . ARG A 1 298 ? 6.983  -0.969  -8.601  1.00 35.48 ? 298 ARG A NE  1 
ATOM   2299 C  CZ  . ARG A 1 298 ? 6.364  -1.105  -7.431  1.00 22.29 ? 298 ARG A CZ  1 
ATOM   2300 N  NH1 . ARG A 1 298 ? 6.096  -2.293  -6.916  1.00 23.44 ? 298 ARG A NH1 1 
ATOM   2301 N  NH2 . ARG A 1 298 ? 5.997  -0.023  -6.767  1.00 16.55 ? 298 ARG A NH2 1 
ATOM   2302 N  N   . GLN A 1 299 ? 5.954  1.519   -12.168 1.00 19.74 ? 299 GLN A N   1 
ATOM   2303 C  CA  . GLN A 1 299 ? 4.542  1.892   -12.143 1.00 17.51 ? 299 GLN A CA  1 
ATOM   2304 C  C   . GLN A 1 299 ? 4.081  2.567   -13.426 1.00 25.37 ? 299 GLN A C   1 
ATOM   2305 O  O   . GLN A 1 299 ? 2.870  2.636   -13.669 1.00 30.19 ? 299 GLN A O   1 
ATOM   2306 C  CB  . GLN A 1 299 ? 4.242  2.808   -10.950 1.00 19.98 ? 299 GLN A CB  1 
ATOM   2307 C  CG  . GLN A 1 299 ? 2.755  3.127   -10.746 1.00 17.67 ? 299 GLN A CG  1 
ATOM   2308 C  CD  . GLN A 1 299 ? 2.444  3.755   -9.381  1.00 16.47 ? 299 GLN A CD  1 
ATOM   2309 O  OE1 . GLN A 1 299 ? 1.288  4.069   -9.077  1.00 16.27 ? 299 GLN A OE1 1 
ATOM   2310 N  NE2 . GLN A 1 299 ? 3.470  3.934   -8.558  1.00 12.86 ? 299 GLN A NE2 1 
ATOM   2311 N  N   . CYS A 1 300 ? 4.999  3.075   -14.248 1.00 22.63 ? 300 CYS A N   1 
ATOM   2312 C  CA  . CYS A 1 300 ? 4.635  3.658   -15.535 1.00 29.47 ? 300 CYS A CA  1 
ATOM   2313 C  C   . CYS A 1 300 ? 4.966  2.731   -16.705 1.00 31.29 ? 300 CYS A C   1 
ATOM   2314 O  O   . CYS A 1 300 ? 5.078  3.194   -17.844 1.00 41.97 ? 300 CYS A O   1 
ATOM   2315 C  CB  . CYS A 1 300 ? 5.308  5.027   -15.722 1.00 26.07 ? 300 CYS A CB  1 
ATOM   2316 S  SG  . CYS A 1 300 ? 4.889  6.342   -14.483 1.00 23.32 ? 300 CYS A SG  1 
ATOM   2317 N  N   . SER A 1 301 ? 5.115  1.428   -16.444 1.00 39.77 ? 301 SER A N   1 
ATOM   2318 C  CA  . SER A 1 301 ? 5.433  0.385   -17.419 1.00 40.37 ? 301 SER A CA  1 
ATOM   2319 C  C   . SER A 1 301 ? 4.519  -0.826  -17.309 1.00 48.18 ? 301 SER A C   1 
ATOM   2320 O  O   . SER A 1 301 ? 4.142  -1.400  -18.338 1.00 47.55 ? 301 SER A O   1 
ATOM   2321 C  CB  . SER A 1 301 ? 6.893  -0.053  -17.256 1.00 38.71 ? 301 SER A CB  1 
ATOM   2322 O  OG  . SER A 1 301 ? 7.758  0.928   -17.804 1.00 41.22 ? 301 SER A OG  1 
ATOM   2323 N  N   . GLY A 1 302 ? 4.144  -1.224  -16.092 1.00 54.01 ? 302 GLY A N   1 
ATOM   2324 C  CA  . GLY A 1 302 ? 3.233  -2.340  -15.904 1.00 51.42 ? 302 GLY A CA  1 
ATOM   2325 C  C   . GLY A 1 302 ? 3.948  -3.633  -15.572 1.00 59.53 ? 302 GLY A C   1 
ATOM   2326 O  O   . GLY A 1 302 ? 3.551  -4.711  -16.027 1.00 61.29 ? 302 GLY A O   1 
ATOM   2327 N  N   . VAL A 1 303 ? 5.005  -3.530  -14.778 1.00 61.94 ? 303 VAL A N   1 
ATOM   2328 C  CA  . VAL A 1 303 ? 5.845  -4.675  -14.456 1.00 72.98 ? 303 VAL A CA  1 
ATOM   2329 C  C   . VAL A 1 303 ? 5.186  -5.516  -13.368 1.00 77.30 ? 303 VAL A C   1 
ATOM   2330 O  O   . VAL A 1 303 ? 4.530  -4.999  -12.455 1.00 76.61 ? 303 VAL A O   1 
ATOM   2331 C  CB  . VAL A 1 303 ? 7.250  -4.196  -14.036 1.00 76.70 ? 303 VAL A CB  1 
ATOM   2332 C  CG1 . VAL A 1 303 ? 8.042  -5.337  -13.398 1.00 86.09 ? 303 VAL A CG1 1 
ATOM   2333 C  CG2 . VAL A 1 303 ? 7.993  -3.603  -15.233 1.00 74.39 ? 303 VAL A CG2 1 
ATOM   2334 N  N   . THR A 1 304 ? 5.371  -6.831  -13.462 1.00 78.41 ? 304 THR A N   1 
ATOM   2335 C  CA  . THR A 1 304 ? 4.741  -7.799  -12.574 1.00 68.46 ? 304 THR A CA  1 
ATOM   2336 C  C   . THR A 1 304 ? 5.795  -8.633  -11.852 1.00 77.09 ? 304 THR A C   1 
ATOM   2337 O  O   . THR A 1 304 ? 6.970  -8.664  -12.231 1.00 77.87 ? 304 THR A O   1 
ATOM   2338 C  CB  . THR A 1 304 ? 3.778  -8.709  -13.350 1.00 56.91 ? 304 THR A CB  1 
ATOM   2339 O  OG1 . THR A 1 304 ? 4.462  -9.305  -14.460 1.00 69.28 ? 304 THR A OG1 1 
ATOM   2340 C  CG2 . THR A 1 304 ? 2.586  -7.921  -13.856 1.00 51.52 ? 304 THR A CG2 1 
ATOM   2341 N  N   . PHE A 1 305 ? 5.354  -9.308  -10.792 1.00 70.80 ? 305 PHE A N   1 
ATOM   2342 C  CA  . PHE A 1 305 ? 6.235  -10.128 -9.960  1.00 75.47 ? 305 PHE A CA  1 
ATOM   2343 C  C   . PHE A 1 305 ? 5.589  -11.475 -9.644  1.00 70.08 ? 305 PHE A C   1 
ATOM   2344 O  O   . PHE A 1 305 ? 4.684  -11.927 -10.353 1.00 62.90 ? 305 PHE A O   1 
ATOM   2345 C  CB  . PHE A 1 305 ? 6.588  -9.389  -8.664  1.00 68.57 ? 305 PHE A CB  1 
ATOM   2346 C  CG  . PHE A 1 305 ? 7.066  -7.985  -8.885  1.00 80.89 ? 305 PHE A CG  1 
ATOM   2347 C  CD1 . PHE A 1 305 ? 8.389  -7.732  -9.211  1.00 86.50 ? 305 PHE A CD1 1 
ATOM   2348 C  CD2 . PHE A 1 305 ? 6.188  -6.917  -8.793  1.00 88.82 ? 305 PHE A CD2 1 
ATOM   2349 C  CE1 . PHE A 1 305 ? 8.831  -6.437  -9.427  1.00 92.35 ? 305 PHE A CE1 1 
ATOM   2350 C  CE2 . PHE A 1 305 ? 6.623  -5.619  -9.011  1.00 92.64 ? 305 PHE A CE2 1 
ATOM   2351 C  CZ  . PHE A 1 305 ? 7.946  -5.380  -9.328  1.00 92.43 ? 305 PHE A CZ  1 
HETATM 2352 C  C1  . XEK B 2 .   ? 9.384  -0.360  20.729  0.80 9.42  ? 401 XEK A C1  1 
HETATM 2353 C  C2  . XEK B 2 .   ? 10.101 -1.180  21.599  0.80 8.60  ? 401 XEK A C2  1 
HETATM 2354 C  C3  . XEK B 2 .   ? 11.419 -0.707  22.087  0.80 11.76 ? 401 XEK A C3  1 
HETATM 2355 C  C4  . XEK B 2 .   ? 12.549 -1.514  21.973  0.80 8.57  ? 401 XEK A C4  1 
HETATM 2356 C  C5  . XEK B 2 .   ? 13.773 -1.062  22.423  0.80 11.39 ? 401 XEK A C5  1 
HETATM 2357 C  C6  . XEK B 2 .   ? 13.884 0.192   22.993  0.80 16.70 ? 401 XEK A C6  1 
HETATM 2358 C  C7  . XEK B 2 .   ? 12.784 1.025   23.099  0.80 15.15 ? 401 XEK A C7  1 
HETATM 2359 C  C8  . XEK B 2 .   ? 12.330 3.417   23.023  0.80 17.62 ? 401 XEK A C8  1 
HETATM 2360 C  C9  . XEK B 2 .   ? 13.441 4.411   22.832  0.80 16.96 ? 401 XEK A C9  1 
HETATM 2361 C  C10 . XEK B 2 .   ? 14.344 4.272   21.786  0.80 17.08 ? 401 XEK A C10 1 
HETATM 2362 C  C11 . XEK B 2 .   ? 15.376 5.172   21.606  0.80 16.90 ? 401 XEK A C11 1 
HETATM 2363 C  C12 . XEK B 2 .   ? 15.523 6.233   22.466  0.80 22.74 ? 401 XEK A C12 1 
HETATM 2364 C  C13 . XEK B 2 .   ? 14.656 6.398   23.519  0.80 22.03 ? 401 XEK A C13 1 
HETATM 2365 C  C14 . XEK B 2 .   ? 13.625 5.492   23.695  0.80 22.59 ? 401 XEK A C14 1 
HETATM 2366 C  C15 . XEK B 2 .   ? 11.550 0.568   22.648  0.80 11.84 ? 401 XEK A C15 1 
HETATM 2367 C  C17 . XEK B 2 .   ? 8.347  -2.878  21.553  0.80 13.56 ? 401 XEK A C17 1 
HETATM 2368 C  C21 . XEK B 2 .   ? 8.141  -6.487  24.891  0.80 23.81 ? 401 XEK A C21 1 
HETATM 2369 C  C22 . XEK B 2 .   ? 6.734  -6.615  22.905  0.80 19.01 ? 401 XEK A C22 1 
HETATM 2370 C  C24 . XEK B 2 .   ? 7.334  -0.037  19.381  0.80 8.70  ? 401 XEK A C24 1 
HETATM 2371 C  C25 . XEK B 2 .   ? 6.232  0.672   19.796  0.80 9.58  ? 401 XEK A C25 1 
HETATM 2372 C  C27 . XEK B 2 .   ? 5.931  1.394   17.556  0.80 8.67  ? 401 XEK A C27 1 
HETATM 2373 C  C16 . XEK B 2 .   ? 9.586  -2.408  22.005  0.80 10.20 ? 401 XEK A C16 1 
HETATM 2374 C  C18 . XEK B 2 .   ? 7.797  -4.182  21.997  0.80 13.43 ? 401 XEK A C18 1 
HETATM 2375 C  C19 . XEK B 2 .   ? 6.789  -4.868  21.198  0.80 11.92 ? 401 XEK A C19 1 
HETATM 2376 C  C20 . XEK B 2 .   ? 8.193  -4.742  23.174  0.80 12.01 ? 401 XEK A C20 1 
HETATM 2377 C  C23 . XEK B 2 .   ? 7.603  -2.067  20.697  0.80 11.39 ? 401 XEK A C23 1 
HETATM 2378 C  C26 . XEK B 2 .   ? 5.520  1.409   18.867  0.80 10.81 ? 401 XEK A C26 1 
HETATM 2379 C  C28 . XEK B 2 .   ? 7.689  0.004   18.038  0.80 8.36  ? 401 XEK A C28 1 
HETATM 2380 F  F1  . XEK B 2 .   ? 15.101 0.598   23.421  0.80 11.36 ? 401 XEK A F1  1 
HETATM 2381 N  N1  . XEK B 2 .   ? 6.325  -6.056  21.719  0.80 12.85 ? 401 XEK A N1  1 
HETATM 2382 N  N2  . XEK B 2 .   ? 7.681  -5.912  23.620  0.80 21.72 ? 401 XEK A N2  1 
HETATM 2383 N  N3  . XEK B 2 .   ? 8.102  -0.843  20.299  0.80 7.57  ? 401 XEK A N3  1 
HETATM 2384 N  N4  . XEK B 2 .   ? 7.000  0.711   17.140  0.80 8.48  ? 401 XEK A N4  1 
HETATM 2385 O  O1  . XEK B 2 .   ? 9.750  0.739   20.335  0.80 7.32  ? 401 XEK A O1  1 
HETATM 2386 O  O2  . XEK B 2 .   ? 12.917 2.270   23.660  0.80 17.98 ? 401 XEK A O2  1 
HETATM 2387 O  O3  . XEK B 2 .   ? 6.335  -4.490  20.121  0.80 14.42 ? 401 XEK A O3  1 
HETATM 2388 O  O4  . XEK B 2 .   ? 6.282  -7.677  23.300  0.80 17.25 ? 401 XEK A O4  1 
HETATM 2389 CL CL1 . XEK B 2 .   ? 15.163 -2.078  22.312  0.80 13.34 ? 401 XEK A CL1 1 
HETATM 2390 CL CL2 . XEK B 2 .   ? 12.547 5.749   25.047  0.80 34.43 ? 401 XEK A CL2 1 
HETATM 2391 H  H1  . XEK B 2 .   ? 12.474 -2.372  21.587  0.80 10.99 ? 401 XEK A H1  1 
HETATM 2392 H  H2  . XEK B 2 .   ? 11.622 3.797   23.584  0.80 21.85 ? 401 XEK A H2  1 
HETATM 2393 H  H3  . XEK B 2 .   ? 11.940 3.168   22.159  0.80 21.85 ? 401 XEK A H3  1 
HETATM 2394 H  H4  . XEK B 2 .   ? 14.248 3.547   21.189  0.80 21.21 ? 401 XEK A H4  1 
HETATM 2395 H  H5  . XEK B 2 .   ? 15.980 5.058   20.890  0.80 20.99 ? 401 XEK A H5  1 
HETATM 2396 H  H6  . XEK B 2 .   ? 16.220 6.850   22.336  0.80 27.99 ? 401 XEK A H6  1 
HETATM 2397 H  H7  . XEK B 2 .   ? 14.760 7.117   24.113  0.80 27.14 ? 401 XEK A H7  1 
HETATM 2398 H  H8  . XEK B 2 .   ? 10.790 1.126   22.722  0.80 14.92 ? 401 XEK A H8  1 
HETATM 2399 H  H13 . XEK B 2 .   ? 8.618  -5.810  25.397  0.80 29.28 ? 401 XEK A H13 1 
HETATM 2400 H  H14 . XEK B 2 .   ? 8.733  -7.235  24.711  0.80 29.28 ? 401 XEK A H14 1 
HETATM 2401 H  H12 . XEK B 2 .   ? 7.375  -6.795  25.401  0.80 29.28 ? 401 XEK A H12 1 
HETATM 2402 H  H16 . XEK B 2 .   ? 5.965  0.657   20.695  0.80 12.20 ? 401 XEK A H16 1 
HETATM 2403 H  H18 . XEK B 2 .   ? 5.440  1.887   16.921  0.80 11.12 ? 401 XEK A H18 1 
HETATM 2404 H  H9  . XEK B 2 .   ? 10.089 -2.944  22.605  0.80 12.95 ? 401 XEK A H9  1 
HETATM 2405 H  H11 . XEK B 2 .   ? 8.844  -4.313  23.705  0.80 15.12 ? 401 XEK A H11 1 
HETATM 2406 H  H15 . XEK B 2 .   ? 6.757  -2.346  20.383  0.80 14.38 ? 401 XEK A H15 1 
HETATM 2407 H  H17 . XEK B 2 .   ? 4.768  1.910   19.134  0.80 13.68 ? 401 XEK A H17 1 
HETATM 2408 H  H19 . XEK B 2 .   ? 8.444  -0.487  17.752  0.80 10.74 ? 401 XEK A H19 1 
HETATM 2409 H  H10 . XEK B 2 .   ? 5.718  -6.486  21.249  0.80 16.13 ? 401 XEK A H10 1 
HETATM 2410 S  S   . DMS C 3 .   ? 7.769  -28.653 20.722  1.00 17.41 ? 402 DMS A S   1 
HETATM 2411 O  O   . DMS C 3 .   ? 8.691  -28.051 21.722  1.00 16.89 ? 402 DMS A O   1 
HETATM 2412 C  C1  . DMS C 3 .   ? 6.612  -27.374 20.159  1.00 18.08 ? 402 DMS A C1  1 
HETATM 2413 C  C2  . DMS C 3 .   ? 6.640  -29.783 21.578  1.00 18.49 ? 402 DMS A C2  1 
HETATM 2414 H  H11 . DMS C 3 .   ? 6.718  -27.237 19.114  1.00 22.40 ? 402 DMS A H11 1 
HETATM 2415 H  H12 . DMS C 3 .   ? 6.822  -26.463 20.657  1.00 22.40 ? 402 DMS A H12 1 
HETATM 2416 H  H13 . DMS C 3 .   ? 5.620  -27.674 20.376  1.00 22.40 ? 402 DMS A H13 1 
HETATM 2417 H  H21 . DMS C 3 .   ? 6.132  -29.260 22.346  1.00 22.89 ? 402 DMS A H21 1 
HETATM 2418 H  H22 . DMS C 3 .   ? 7.193  -30.582 22.001  1.00 22.89 ? 402 DMS A H22 1 
HETATM 2419 H  H23 . DMS C 3 .   ? 5.935  -30.168 20.888  1.00 22.89 ? 402 DMS A H23 1 
HETATM 2420 O  O   . HOH D 4 .   ? 16.647 -28.121 10.221  1.00 40.64 ? 501 HOH A O   1 
HETATM 2421 O  O   . HOH D 4 .   ? 6.353  6.468   1.384   1.00 28.78 ? 502 HOH A O   1 
HETATM 2422 O  O   . HOH D 4 .   ? 21.371 29.220  -8.388  1.00 18.06 ? 503 HOH A O   1 
HETATM 2423 O  O   . HOH D 4 .   ? 14.899 -8.920  31.349  1.00 41.98 ? 504 HOH A O   1 
HETATM 2424 O  O   . HOH D 4 .   ? 18.135 31.170  -11.460 1.00 18.04 ? 505 HOH A O   1 
HETATM 2425 O  O   . HOH D 4 .   ? 12.628 23.798  -19.352 1.00 19.16 ? 506 HOH A O   1 
HETATM 2426 O  O   . HOH D 4 .   ? 13.046 -4.562  -6.512  1.00 21.01 ? 507 HOH A O   1 
HETATM 2427 O  O   . HOH D 4 .   ? 0.613  26.243  -2.542  1.00 18.56 ? 508 HOH A O   1 
HETATM 2428 O  O   . HOH D 4 .   ? 6.471  10.698  -1.228  1.00 12.39 ? 509 HOH A O   1 
HETATM 2429 O  O   . HOH D 4 .   ? 18.400 -23.821 6.645   1.00 16.51 ? 510 HOH A O   1 
HETATM 2430 O  O   . HOH D 4 .   ? 26.208 -6.038  32.381  1.00 27.26 ? 511 HOH A O   1 
HETATM 2431 O  O   . HOH D 4 .   ? 19.587 5.789   -2.489  1.00 15.38 ? 512 HOH A O   1 
HETATM 2432 O  O   . HOH D 4 .   ? 15.732 -20.260 31.155  1.00 24.13 ? 513 HOH A O   1 
HETATM 2433 O  O   . HOH D 4 .   ? 28.583 8.577   -15.383 1.00 22.10 ? 514 HOH A O   1 
HETATM 2434 O  O   . HOH D 4 .   ? 22.966 -14.529 32.901  1.00 18.80 ? 515 HOH A O   1 
HETATM 2435 O  O   . HOH D 4 .   ? 25.398 -0.951  26.180  1.00 22.13 ? 516 HOH A O   1 
HETATM 2436 O  O   . HOH D 4 .   ? 26.188 -7.730  21.800  1.00 14.44 ? 517 HOH A O   1 
HETATM 2437 O  O   . HOH D 4 .   ? 7.639  -23.551 20.110  1.00 11.81 ? 518 HOH A O   1 
HETATM 2438 O  O   . HOH D 4 .   ? 13.600 -24.500 2.718   1.00 28.93 ? 519 HOH A O   1 
HETATM 2439 O  O   . HOH D 4 .   ? 29.268 15.307  -14.256 1.00 21.48 ? 520 HOH A O   1 
HETATM 2440 O  O   . HOH D 4 .   ? 26.814 6.943   -12.971 1.00 13.41 ? 521 HOH A O   1 
HETATM 2441 O  O   . HOH D 4 .   ? 10.341 20.212  -0.925  1.00 11.07 ? 522 HOH A O   1 
HETATM 2442 O  O   . HOH D 4 .   ? -1.848 4.989   -18.844 1.00 17.48 ? 523 HOH A O   1 
HETATM 2443 O  O   . HOH D 4 .   ? 10.619 17.461  -23.731 1.00 21.62 ? 524 HOH A O   1 
HETATM 2444 O  O   . HOH D 4 .   ? 10.464 -0.339  -3.517  1.00 10.41 ? 525 HOH A O   1 
HETATM 2445 O  O   . HOH D 4 .   ? 6.214  -8.419  8.705   1.00 12.36 ? 526 HOH A O   1 
HETATM 2446 O  O   . HOH D 4 .   ? 13.104 13.278  8.654   1.00 31.75 ? 527 HOH A O   1 
HETATM 2447 O  O   . HOH D 4 .   ? 23.836 10.429  -18.227 1.00 20.14 ? 528 HOH A O   1 
HETATM 2448 O  O   . HOH D 4 .   ? 22.948 1.312   3.873   1.00 12.80 ? 529 HOH A O   1 
HETATM 2449 O  O   . HOH D 4 .   ? 15.779 30.653  -2.998  1.00 20.50 ? 530 HOH A O   1 
HETATM 2450 O  O   . HOH D 4 .   ? 19.080 32.766  -1.501  1.00 20.00 ? 531 HOH A O   1 
HETATM 2451 O  O   . HOH D 4 .   ? 17.464 29.455  -4.543  1.00 17.66 ? 532 HOH A O   1 
HETATM 2452 O  O   . HOH D 4 .   ? 16.164 28.753  -21.256 1.00 29.37 ? 533 HOH A O   1 
HETATM 2453 O  O   . HOH D 4 .   ? 23.583 1.303   5.814   1.00 26.30 ? 534 HOH A O   1 
HETATM 2454 O  O   . HOH D 4 .   ? 9.061  -4.719  36.051  1.00 31.33 ? 535 HOH A O   1 
HETATM 2455 O  O   . HOH D 4 .   ? 16.755 2.361   -4.919  1.00 18.53 ? 536 HOH A O   1 
HETATM 2456 O  O   . HOH D 4 .   ? 1.812  14.681  0.638   1.00 15.88 ? 537 HOH A O   1 
HETATM 2457 O  O   . HOH D 4 .   ? 16.234 -22.444 30.461  1.00 22.70 ? 538 HOH A O   1 
HETATM 2458 O  O   . HOH D 4 .   ? 19.033 -7.604  5.572   1.00 9.36  ? 539 HOH A O   1 
HETATM 2459 O  O   . HOH D 4 .   ? 9.543  -18.703 27.870  1.00 25.82 ? 540 HOH A O   1 
HETATM 2460 O  O   . HOH D 4 .   ? 24.028 1.929   15.087  1.00 11.18 ? 541 HOH A O   1 
HETATM 2461 O  O   . HOH D 4 .   ? 24.413 -6.779  7.261   1.00 31.32 ? 542 HOH A O   1 
HETATM 2462 O  O   . HOH D 4 .   ? -5.128 14.826  -3.765  1.00 20.97 ? 543 HOH A O   1 
HETATM 2463 O  O   . HOH D 4 .   ? 10.067 6.728   5.436   1.00 2.08  ? 544 HOH A O   1 
HETATM 2464 O  O   . HOH D 4 .   ? 4.719  -18.632 8.575   1.00 16.11 ? 545 HOH A O   1 
HETATM 2465 O  O   . HOH D 4 .   ? 13.300 -27.755 22.219  1.00 12.14 ? 546 HOH A O   1 
HETATM 2466 O  O   . HOH D 4 .   ? 7.425  20.164  -0.926  1.00 16.28 ? 547 HOH A O   1 
HETATM 2467 O  O   . HOH D 4 .   ? 27.802 22.134  -13.238 1.00 13.20 ? 548 HOH A O   1 
HETATM 2468 O  O   . HOH D 4 .   ? 18.974 -24.627 24.964  1.00 16.97 ? 549 HOH A O   1 
HETATM 2469 O  O   . HOH D 4 .   ? 14.224 0.251   -3.489  1.00 11.89 ? 550 HOH A O   1 
HETATM 2470 O  O   . HOH D 4 .   ? 22.567 20.060  -0.387  1.00 12.27 ? 551 HOH A O   1 
HETATM 2471 O  O   . HOH D 4 .   ? 23.022 23.385  -18.366 1.00 14.41 ? 552 HOH A O   1 
HETATM 2472 O  O   . HOH D 4 .   ? 14.460 18.726  3.411   1.00 13.00 ? 553 HOH A O   1 
HETATM 2473 O  O   . HOH D 4 .   ? 20.752 -20.237 15.847  1.00 15.47 ? 554 HOH A O   1 
HETATM 2474 O  O   . HOH D 4 .   ? 8.010  25.283  -12.105 1.00 19.49 ? 555 HOH A O   1 
HETATM 2475 O  O   . HOH D 4 .   ? 21.971 -19.150 26.014  1.00 10.97 ? 556 HOH A O   1 
HETATM 2476 O  O   . HOH D 4 .   ? 14.853 -9.393  -4.820  1.00 20.48 ? 557 HOH A O   1 
HETATM 2477 O  O   . HOH D 4 .   ? 17.511 28.272  -13.705 1.00 14.31 ? 558 HOH A O   1 
HETATM 2478 O  O   . HOH D 4 .   ? 22.453 14.356  9.202   1.00 26.47 ? 559 HOH A O   1 
HETATM 2479 O  O   . HOH D 4 .   ? 22.700 -2.251  19.718  1.00 8.55  ? 560 HOH A O   1 
HETATM 2480 O  O   . HOH D 4 .   ? 22.612 -4.296  32.810  1.00 24.43 ? 561 HOH A O   1 
HETATM 2481 O  O   . HOH D 4 .   ? 11.099 22.614  -17.421 1.00 16.40 ? 562 HOH A O   1 
HETATM 2482 O  O   . HOH D 4 .   ? 0.624  -0.692  11.960  1.00 12.84 ? 563 HOH A O   1 
HETATM 2483 O  O   . HOH D 4 .   ? 11.515 30.379  -0.638  1.00 21.87 ? 564 HOH A O   1 
HETATM 2484 O  O   . HOH D 4 .   ? 5.861  2.459   -7.765  1.00 12.66 ? 565 HOH A O   1 
HETATM 2485 O  O   . HOH D 4 .   ? 19.083 -26.036 28.437  1.00 27.97 ? 566 HOH A O   1 
HETATM 2486 O  O   . HOH D 4 .   ? 12.864 -23.393 31.993  1.00 16.71 ? 567 HOH A O   1 
HETATM 2487 O  O   . HOH D 4 .   ? 16.847 7.033   -4.737  1.00 10.06 ? 568 HOH A O   1 
HETATM 2488 O  O   . HOH D 4 .   ? -3.897 11.486  -17.157 1.00 28.90 ? 569 HOH A O   1 
HETATM 2489 O  O   . HOH D 4 .   ? -0.471 4.344   -14.087 1.00 14.89 ? 570 HOH A O   1 
HETATM 2490 O  O   . HOH D 4 .   ? 24.516 13.755  -2.799  1.00 13.47 ? 571 HOH A O   1 
HETATM 2491 O  O   . HOH D 4 .   ? -3.290 29.498  -7.539  1.00 18.50 ? 572 HOH A O   1 
HETATM 2492 O  O   . HOH D 4 .   ? 9.055  -25.193 25.143  1.00 15.85 ? 573 HOH A O   1 
HETATM 2493 O  O   . HOH D 4 .   ? 24.594 -17.470 14.587  1.00 18.70 ? 574 HOH A O   1 
HETATM 2494 O  O   . HOH D 4 .   ? 24.419 -8.243  33.624  1.00 23.29 ? 575 HOH A O   1 
HETATM 2495 O  O   . HOH D 4 .   ? 27.467 17.045  -7.791  1.00 16.47 ? 576 HOH A O   1 
HETATM 2496 O  O   . HOH D 4 .   ? 29.036 -7.838  13.503  1.00 23.59 ? 577 HOH A O   1 
HETATM 2497 O  O   . HOH D 4 .   ? 10.897 -25.029 2.322   1.00 13.34 ? 578 HOH A O   1 
HETATM 2498 O  O   . HOH D 4 .   ? 22.278 2.441   28.377  1.00 27.03 ? 579 HOH A O   1 
HETATM 2499 O  O   . HOH D 4 .   ? 12.892 22.169  -21.999 1.00 18.84 ? 580 HOH A O   1 
HETATM 2500 O  O   . HOH D 4 .   ? 9.984  -24.133 22.185  1.00 17.08 ? 581 HOH A O   1 
HETATM 2501 O  O   . HOH D 4 .   ? 0.680  9.015   -5.434  1.00 21.41 ? 582 HOH A O   1 
HETATM 2502 O  O   . HOH D 4 .   ? 9.566  10.604  -5.149  1.00 5.77  ? 583 HOH A O   1 
HETATM 2503 O  O   . HOH D 4 .   ? 24.967 -15.006 25.676  1.00 14.00 ? 584 HOH A O   1 
HETATM 2504 O  O   . HOH D 4 .   ? 17.066 -18.883 7.134   1.00 9.13  ? 585 HOH A O   1 
HETATM 2505 O  O   . HOH D 4 .   ? 1.705  1.823   20.464  1.00 15.55 ? 586 HOH A O   1 
HETATM 2506 O  O   . HOH D 4 .   ? -2.616 17.245  -9.009  1.00 21.30 ? 587 HOH A O   1 
HETATM 2507 O  O   . HOH D 4 .   ? 25.225 -9.541  19.349  1.00 10.58 ? 588 HOH A O   1 
HETATM 2508 O  O   . HOH D 4 .   ? 13.061 0.857   -6.025  1.00 13.58 ? 589 HOH A O   1 
HETATM 2509 O  O   . HOH D 4 .   ? 25.022 -13.781 8.252   1.00 12.52 ? 590 HOH A O   1 
HETATM 2510 O  O   . HOH D 4 .   ? 4.171  -22.197 6.592   1.00 12.31 ? 591 HOH A O   1 
HETATM 2511 O  O   . HOH D 4 .   ? 22.133 9.386   3.707   1.00 20.62 ? 592 HOH A O   1 
HETATM 2512 O  O   . HOH D 4 .   ? 4.618  -17.618 20.585  1.00 15.98 ? 593 HOH A O   1 
HETATM 2513 O  O   . HOH D 4 .   ? 5.142  -17.565 1.691   1.00 10.78 ? 594 HOH A O   1 
HETATM 2514 O  O   . HOH D 4 .   ? 24.257 -6.349  25.474  1.00 15.62 ? 595 HOH A O   1 
HETATM 2515 O  O   . HOH D 4 .   ? 4.016  -11.771 -2.936  1.00 5.47  ? 596 HOH A O   1 
HETATM 2516 O  O   . HOH D 4 .   ? 12.821 22.890  1.895   1.00 14.38 ? 597 HOH A O   1 
HETATM 2517 O  O   . HOH D 4 .   ? 23.683 -2.543  15.070  1.00 7.29  ? 598 HOH A O   1 
HETATM 2518 O  O   . HOH D 4 .   ? 22.069 -2.113  22.959  1.00 14.80 ? 599 HOH A O   1 
HETATM 2519 O  O   . HOH D 4 .   ? 16.895 2.398   11.721  1.00 5.85  ? 600 HOH A O   1 
HETATM 2520 O  O   . HOH D 4 .   ? 17.229 -13.446 30.603  1.00 24.54 ? 601 HOH A O   1 
HETATM 2521 O  O   . HOH D 4 .   ? 25.091 16.354  -15.232 1.00 14.95 ? 602 HOH A O   1 
HETATM 2522 O  O   . HOH D 4 .   ? 10.446 25.591  -0.807  1.00 11.39 ? 603 HOH A O   1 
HETATM 2523 O  O   . HOH D 4 .   ? 22.120 5.855   19.456  1.00 15.15 ? 604 HOH A O   1 
HETATM 2524 O  O   . HOH D 4 .   ? 8.657  16.806  0.987   1.00 18.03 ? 605 HOH A O   1 
HETATM 2525 O  O   . HOH D 4 .   ? 1.813  2.407   0.453   1.00 9.68  ? 606 HOH A O   1 
HETATM 2526 O  O   . HOH D 4 .   ? 19.934 9.191   0.750   1.00 27.79 ? 607 HOH A O   1 
HETATM 2527 O  O   . HOH D 4 .   ? 21.102 22.247  -19.518 1.00 16.77 ? 608 HOH A O   1 
HETATM 2528 O  O   . HOH D 4 .   ? 23.701 20.626  -2.891  1.00 13.60 ? 609 HOH A O   1 
HETATM 2529 O  O   . HOH D 4 .   ? 18.546 -29.223 19.981  1.00 27.20 ? 610 HOH A O   1 
HETATM 2530 O  O   . HOH D 4 .   ? 20.807 10.863  -17.909 1.00 7.57  ? 611 HOH A O   1 
HETATM 2531 O  O   . HOH D 4 .   ? 16.406 -5.723  19.861  1.00 4.00  ? 612 HOH A O   1 
HETATM 2532 O  O   . HOH D 4 .   ? 24.894 -16.255 20.309  1.00 16.29 ? 613 HOH A O   1 
HETATM 2533 O  O   . HOH D 4 .   ? -2.065 -1.617  11.033  1.00 17.64 ? 614 HOH A O   1 
HETATM 2534 O  O   . HOH D 4 .   ? 12.199 31.446  -9.037  1.00 19.25 ? 615 HOH A O   1 
HETATM 2535 O  O   . HOH D 4 .   ? 21.029 9.444   11.564  1.00 9.37  ? 616 HOH A O   1 
HETATM 2536 O  O   . HOH D 4 .   ? 19.438 12.799  -4.649  1.00 8.81  ? 617 HOH A O   1 
HETATM 2537 O  O   . HOH D 4 .   ? 15.892 -26.459 26.011  1.00 12.78 ? 618 HOH A O   1 
HETATM 2538 O  O   . HOH D 4 .   ? 4.739  13.778  1.203   1.00 19.73 ? 619 HOH A O   1 
HETATM 2539 O  O   . HOH D 4 .   ? 22.599 10.292  7.779   1.00 19.86 ? 620 HOH A O   1 
HETATM 2540 O  O   . HOH D 4 .   ? 6.874  -15.561 -8.197  1.00 31.90 ? 621 HOH A O   1 
HETATM 2541 O  O   . HOH D 4 .   ? 14.911 18.858  -22.765 1.00 10.49 ? 622 HOH A O   1 
HETATM 2542 O  O   . HOH D 4 .   ? 3.494  29.541  -3.607  1.00 23.07 ? 623 HOH A O   1 
HETATM 2543 O  O   . HOH D 4 .   ? 28.305 -7.063  11.904  1.00 24.11 ? 624 HOH A O   1 
HETATM 2544 O  O   . HOH D 4 .   ? 20.929 -13.368 9.949   1.00 14.07 ? 625 HOH A O   1 
HETATM 2545 O  O   . HOH D 4 .   ? 11.055 -26.369 21.444  1.00 14.04 ? 626 HOH A O   1 
HETATM 2546 O  O   . HOH D 4 .   ? 27.109 -10.698 16.957  1.00 13.27 ? 627 HOH A O   1 
HETATM 2547 O  O   . HOH D 4 .   ? 5.267  2.902   -5.055  1.00 11.38 ? 628 HOH A O   1 
HETATM 2548 O  O   . HOH D 4 .   ? 14.816 -11.470 30.932  1.00 36.98 ? 629 HOH A O   1 
HETATM 2549 O  O   . HOH D 4 .   ? 27.918 -11.117 11.683  1.00 13.97 ? 630 HOH A O   1 
HETATM 2550 O  O   . HOH D 4 .   ? 26.933 3.748   23.404  1.00 19.44 ? 631 HOH A O   1 
HETATM 2551 O  O   . HOH D 4 .   ? 27.620 20.958  -6.849  1.00 19.92 ? 632 HOH A O   1 
HETATM 2552 O  O   . HOH D 4 .   ? 17.310 15.684  14.904  1.00 22.88 ? 633 HOH A O   1 
HETATM 2553 O  O   . HOH D 4 .   ? 25.907 21.087  -15.262 1.00 18.10 ? 634 HOH A O   1 
HETATM 2554 O  O   . HOH D 4 .   ? 19.506 14.772  -19.625 1.00 23.21 ? 635 HOH A O   1 
HETATM 2555 O  O   . HOH D 4 .   ? 23.505 -0.861  17.354  1.00 6.64  ? 636 HOH A O   1 
HETATM 2556 O  O   . HOH D 4 .   ? 19.109 4.288   29.736  1.00 24.75 ? 637 HOH A O   1 
HETATM 2557 O  O   . HOH D 4 .   ? 27.099 23.485  -6.334  1.00 14.26 ? 638 HOH A O   1 
HETATM 2558 O  O   . HOH D 4 .   ? 17.735 3.872   -14.076 1.00 15.27 ? 639 HOH A O   1 
HETATM 2559 O  O   . HOH D 4 .   ? 8.229  30.043  -15.680 1.00 25.32 ? 640 HOH A O   1 
HETATM 2560 O  O   . HOH D 4 .   ? 10.217 14.042  2.445   1.00 31.74 ? 641 HOH A O   1 
HETATM 2561 O  O   . HOH D 4 .   ? 9.617  -17.648 -4.453  1.00 16.29 ? 642 HOH A O   1 
HETATM 2562 O  O   . HOH D 4 .   ? 14.082 -22.896 0.262   1.00 27.55 ? 643 HOH A O   1 
HETATM 2563 O  O   . HOH D 4 .   ? 1.663  -16.575 12.208  1.00 15.45 ? 644 HOH A O   1 
HETATM 2564 O  O   . HOH D 4 .   ? 23.090 11.472  -2.199  1.00 29.96 ? 645 HOH A O   1 
HETATM 2565 O  O   . HOH D 4 .   ? 27.483 19.841  -9.613  1.00 17.54 ? 646 HOH A O   1 
HETATM 2566 O  O   . HOH D 4 .   ? 7.705  3.844   -3.518  1.00 6.67  ? 647 HOH A O   1 
HETATM 2567 O  O   . HOH D 4 .   ? 15.520 27.389  3.823   1.00 26.58 ? 648 HOH A O   1 
HETATM 2568 O  O   . HOH D 4 .   ? 1.954  11.709  -5.658  1.00 9.46  ? 649 HOH A O   1 
HETATM 2569 O  O   . HOH D 4 .   ? 6.662  -8.563  28.224  1.00 28.01 ? 650 HOH A O   1 
HETATM 2570 O  O   . HOH D 4 .   ? 12.248 19.098  -23.407 1.00 20.02 ? 651 HOH A O   1 
HETATM 2571 O  O   . HOH D 4 .   ? 15.304 -4.804  -0.697  1.00 14.17 ? 652 HOH A O   1 
HETATM 2572 O  O   . HOH D 4 .   ? 28.311 11.062  -9.271  1.00 12.73 ? 653 HOH A O   1 
HETATM 2573 O  O   . HOH D 4 .   ? 6.848  8.238   11.588  1.00 15.66 ? 654 HOH A O   1 
HETATM 2574 O  O   . HOH D 4 .   ? 28.945 14.572  -9.901  1.00 23.50 ? 655 HOH A O   1 
HETATM 2575 O  O   . HOH D 4 .   ? 14.825 27.669  -13.100 1.00 15.70 ? 656 HOH A O   1 
HETATM 2576 O  O   . HOH D 4 .   ? 3.354  4.826   19.706  1.00 17.41 ? 657 HOH A O   1 
HETATM 2577 O  O   . HOH D 4 .   ? 17.052 -28.570 22.861  1.00 15.18 ? 658 HOH A O   1 
HETATM 2578 O  O   . HOH D 4 .   ? 13.755 11.419  11.271  1.00 11.76 ? 659 HOH A O   1 
HETATM 2579 O  O   . HOH D 4 .   ? 12.814 -30.499 21.801  1.00 19.27 ? 660 HOH A O   1 
HETATM 2580 O  O   . HOH D 4 .   ? 23.258 9.479   -3.061  1.00 21.09 ? 661 HOH A O   1 
HETATM 2581 O  O   . HOH D 4 .   ? 3.834  22.373  -19.935 1.00 23.30 ? 662 HOH A O   1 
HETATM 2582 O  O   . HOH D 4 .   ? 0.210  1.590   13.458  1.00 22.54 ? 663 HOH A O   1 
HETATM 2583 O  O   . HOH D 4 .   ? 27.525 -7.767  9.406   1.00 32.06 ? 664 HOH A O   1 
HETATM 2584 O  O   . HOH D 4 .   ? 26.356 -11.975 19.429  1.00 26.68 ? 665 HOH A O   1 
HETATM 2585 O  O   . HOH D 4 .   ? 22.881 -5.582  0.023   1.00 15.47 ? 666 HOH A O   1 
HETATM 2586 O  O   . HOH D 4 .   ? 18.758 31.239  -8.455  1.00 16.38 ? 667 HOH A O   1 
HETATM 2587 O  O   . HOH D 4 .   ? 2.705  12.620  -21.361 1.00 18.90 ? 668 HOH A O   1 
HETATM 2588 O  O   . HOH D 4 .   ? 3.984  25.447  -1.703  1.00 14.84 ? 669 HOH A O   1 
HETATM 2589 O  O   . HOH D 4 .   ? 16.188 3.673   -8.730  1.00 7.95  ? 670 HOH A O   1 
HETATM 2590 O  O   . HOH D 4 .   ? 12.922 32.802  -3.832  1.00 16.10 ? 671 HOH A O   1 
HETATM 2591 O  O   . HOH D 4 .   ? 10.405 -19.165 30.562  1.00 27.41 ? 672 HOH A O   1 
HETATM 2592 O  O   . HOH D 4 .   ? 0.000  16.638  0.000   0.50 9.44  ? 673 HOH A O   1 
HETATM 2593 O  O   . HOH D 4 .   ? 1.573  27.613  -10.525 1.00 29.08 ? 674 HOH A O   1 
HETATM 2594 O  O   . HOH D 4 .   ? 24.790 -4.013  30.001  1.00 21.81 ? 675 HOH A O   1 
HETATM 2595 O  O   . HOH D 4 .   ? 11.605 -6.715  35.457  1.00 30.57 ? 676 HOH A O   1 
HETATM 2596 O  O   . HOH D 4 .   ? 24.762 14.043  -18.174 1.00 13.56 ? 677 HOH A O   1 
HETATM 2597 O  O   . HOH D 4 .   ? 8.681  3.531   22.056  1.00 21.70 ? 678 HOH A O   1 
HETATM 2598 O  O   . HOH D 4 .   ? 14.494 17.571  5.415   1.00 18.20 ? 679 HOH A O   1 
HETATM 2599 O  O   . HOH D 4 .   ? 21.421 13.745  5.798   1.00 27.94 ? 680 HOH A O   1 
HETATM 2600 O  O   . HOH D 4 .   ? 10.419 18.602  1.214   1.00 20.05 ? 681 HOH A O   1 
HETATM 2601 O  O   . HOH D 4 .   ? 24.023 2.553   27.579  1.00 30.55 ? 682 HOH A O   1 
HETATM 2602 O  O   . HOH D 4 .   ? 21.107 17.245  -18.622 1.00 12.71 ? 683 HOH A O   1 
HETATM 2603 O  O   . HOH D 4 .   ? 16.254 -25.625 5.959   1.00 21.98 ? 684 HOH A O   1 
HETATM 2604 O  O   . HOH D 4 .   ? 13.189 -2.307  -5.743  1.00 19.70 ? 685 HOH A O   1 
HETATM 2605 O  O   . HOH D 4 .   ? 25.289 -4.775  22.953  1.00 21.76 ? 686 HOH A O   1 
HETATM 2606 O  O   . HOH D 4 .   ? -3.518 9.566   -9.303  1.00 20.07 ? 687 HOH A O   1 
HETATM 2607 O  O   . HOH D 4 .   ? 25.857 -14.344 32.562  1.00 29.65 ? 688 HOH A O   1 
HETATM 2608 O  O   . HOH D 4 .   ? 10.853 21.499  -20.077 1.00 17.29 ? 689 HOH A O   1 
HETATM 2609 O  O   . HOH D 4 .   ? 13.616 29.121  -11.323 1.00 21.30 ? 690 HOH A O   1 
HETATM 2610 O  O   . HOH D 4 .   ? 29.164 -9.318  16.387  1.00 30.46 ? 691 HOH A O   1 
HETATM 2611 O  O   . HOH D 4 .   ? 2.815  -17.964 1.080   1.00 13.82 ? 692 HOH A O   1 
HETATM 2612 O  O   . HOH D 4 .   ? 18.298 4.089   -4.361  1.00 37.30 ? 693 HOH A O   1 
HETATM 2613 O  O   . HOH D 4 .   ? 23.415 -18.182 22.661  1.00 12.89 ? 694 HOH A O   1 
HETATM 2614 O  O   . HOH D 4 .   ? 16.098 -10.522 -5.960  1.00 32.64 ? 695 HOH A O   1 
HETATM 2615 O  O   . HOH D 4 .   ? 15.719 -29.143 7.696   1.00 26.61 ? 696 HOH A O   1 
HETATM 2616 O  O   . HOH D 4 .   ? 11.834 24.833  -22.761 1.00 29.05 ? 697 HOH A O   1 
HETATM 2617 O  O   . HOH D 4 .   ? 21.856 -22.887 16.367  1.00 19.00 ? 698 HOH A O   1 
HETATM 2618 O  O   . HOH D 4 .   ? 22.328 -14.840 8.274   1.00 19.00 ? 699 HOH A O   1 
HETATM 2619 O  O   . HOH D 4 .   ? 25.108 -3.111  32.287  1.00 24.09 ? 700 HOH A O   1 
HETATM 2620 O  O   . HOH D 4 .   ? 27.562 -12.753 21.920  1.00 30.51 ? 701 HOH A O   1 
HETATM 2621 O  O   . HOH D 4 .   ? 2.798  28.607  -12.330 1.00 36.48 ? 702 HOH A O   1 
HETATM 2622 O  O   . HOH D 4 .   ? -4.371 9.533   -7.261  1.00 19.38 ? 703 HOH A O   1 
HETATM 2623 O  O   . HOH D 4 .   ? 14.701 4.111   -21.628 1.00 21.83 ? 704 HOH A O   1 
HETATM 2624 O  O   . HOH D 4 .   ? 16.129 -4.841  -3.102  1.00 22.07 ? 705 HOH A O   1 
HETATM 2625 O  O   . HOH D 4 .   ? -4.558 -11.615 5.452   1.00 19.06 ? 706 HOH A O   1 
HETATM 2626 O  O   . HOH D 4 .   ? 24.014 -17.865 25.228  1.00 13.51 ? 707 HOH A O   1 
HETATM 2627 O  O   . HOH D 4 .   ? 24.466 7.110   10.467  1.00 18.77 ? 708 HOH A O   1 
HETATM 2628 O  O   . HOH D 4 .   ? 20.743 6.783   -6.003  1.00 24.29 ? 709 HOH A O   1 
HETATM 2629 O  O   . HOH D 4 .   ? 19.488 7.837   -3.908  1.00 19.40 ? 710 HOH A O   1 
HETATM 2630 O  O   . HOH D 4 .   ? 22.752 12.321  4.181   1.00 21.32 ? 711 HOH A O   1 
HETATM 2631 O  O   . HOH D 4 .   ? 18.562 -26.862 26.247  1.00 16.99 ? 712 HOH A O   1 
HETATM 2632 O  O   . HOH D 4 .   ? 15.779 3.202   -15.048 1.00 15.79 ? 713 HOH A O   1 
HETATM 2633 O  O   . HOH D 4 .   ? 25.527 20.235  -2.120  1.00 27.27 ? 714 HOH A O   1 
HETATM 2634 O  O   . HOH D 4 .   ? 23.103 9.110   10.153  1.00 21.01 ? 715 HOH A O   1 
HETATM 2635 O  O   . HOH D 4 .   ? 24.976 -1.455  21.225  1.00 25.40 ? 716 HOH A O   1 
HETATM 2636 O  O   . HOH D 4 .   ? 14.972 -28.478 24.359  1.00 9.51  ? 717 HOH A O   1 
HETATM 2637 O  O   . HOH D 4 .   ? 21.314 3.756   -3.985  1.00 23.14 ? 718 HOH A O   1 
HETATM 2638 O  O   . HOH D 4 .   ? 14.363 12.462  20.953  1.00 15.51 ? 719 HOH A O   1 
HETATM 2639 O  O   . HOH D 4 .   ? 12.918 25.092  3.506   1.00 20.47 ? 720 HOH A O   1 
HETATM 2640 O  O   . HOH D 4 .   ? 26.563 18.741  -15.575 1.00 17.00 ? 721 HOH A O   1 
HETATM 2641 O  O   . HOH D 4 .   ? 6.555  22.808  -1.758  1.00 20.82 ? 722 HOH A O   1 
HETATM 2642 O  O   . HOH D 4 .   ? -4.654 27.768  -9.208  1.00 21.56 ? 723 HOH A O   1 
HETATM 2643 O  O   . HOH D 4 .   ? -0.868 19.558  -20.919 1.00 18.19 ? 724 HOH A O   1 
HETATM 2644 O  O   . HOH D 4 .   ? 16.936 -30.370 20.727  1.00 15.07 ? 725 HOH A O   1 
HETATM 2645 O  O   . HOH D 4 .   ? 26.835 2.159   15.500  1.00 25.99 ? 726 HOH A O   1 
HETATM 2646 O  O   . HOH D 4 .   ? 25.658 22.060  -17.999 1.00 18.05 ? 727 HOH A O   1 
HETATM 2647 O  O   . HOH D 4 .   ? 26.325 0.074   17.469  1.00 21.47 ? 728 HOH A O   1 
HETATM 2648 O  O   . HOH D 4 .   ? 24.972 -4.880  -1.535  1.00 24.81 ? 729 HOH A O   1 
HETATM 2649 O  O   . HOH D 4 .   ? 17.723 5.304   -6.794  1.00 24.50 ? 730 HOH A O   1 
HETATM 2650 O  O   . HOH D 4 .   ? 23.687 16.183  -17.774 1.00 19.69 ? 731 HOH A O   1 
HETATM 2651 O  O   . HOH D 4 .   ? 23.443 12.537  21.389  1.00 18.10 ? 732 HOH A O   1 
HETATM 2652 O  O   . HOH D 4 .   ? 27.800 23.758  -3.836  1.00 22.34 ? 733 HOH A O   1 
HETATM 2653 O  O   . HOH D 4 .   ? 4.290  21.401  -21.845 0.50 28.54 ? 734 HOH A O   1 
HETATM 2654 O  O   . HOH D 4 .   ? 10.841 23.029  0.102   1.00 18.61 ? 735 HOH A O   1 
HETATM 2655 O  O   . HOH D 4 .   ? 4.290  18.469  -21.845 0.50 26.35 ? 736 HOH A O   1 
HETATM 2656 O  O   . HOH D 4 .   ? 14.765 14.746  20.738  1.00 22.78 ? 737 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   ? 0.1317 0.1431 0.1337 -0.0122 -0.0087 0.0129 1   SER A N   
2    C  CA  . SER A 1   ? 0.2079 0.2195 0.2107 -0.0116 -0.0084 0.0128 1   SER A CA  
3    C  C   . SER A 1   ? 0.1456 0.1576 0.1492 -0.0109 -0.0081 0.0127 1   SER A C   
4    O  O   . SER A 1   ? 0.1504 0.1624 0.1539 -0.0110 -0.0081 0.0128 1   SER A O   
5    C  CB  . SER A 1   ? 0.2291 0.2411 0.2322 -0.0116 -0.0085 0.0128 1   SER A CB  
6    O  OG  . SER A 1   ? 0.2371 0.2495 0.2406 -0.0116 -0.0085 0.0129 1   SER A OG  
7    N  N   . GLY A 2   ? 0.1660 0.1782 0.1702 -0.0104 -0.0078 0.0126 2   GLY A N   
8    C  CA  . GLY A 2   ? 0.1207 0.1331 0.1256 -0.0098 -0.0074 0.0125 2   GLY A CA  
9    C  C   . GLY A 2   ? 0.1467 0.1588 0.1517 -0.0094 -0.0072 0.0124 2   GLY A C   
10   O  O   . GLY A 2   ? 0.2085 0.2203 0.2129 -0.0096 -0.0073 0.0124 2   GLY A O   
11   N  N   . PHE A 3   ? 0.1663 0.1786 0.1719 -0.0088 -0.0068 0.0123 3   PHE A N   
12   C  CA  . PHE A 3   ? 0.1376 0.1497 0.1433 -0.0084 -0.0066 0.0122 3   PHE A CA  
13   C  C   . PHE A 3   ? 0.1445 0.1568 0.1506 -0.0079 -0.0062 0.0122 3   PHE A C   
14   O  O   . PHE A 3   ? 0.1622 0.1747 0.1688 -0.0076 -0.0060 0.0121 3   PHE A O   
15   C  CB  . PHE A 3   ? 0.1085 0.1205 0.1144 -0.0082 -0.0065 0.0120 3   PHE A CB  
16   C  CG  . PHE A 3   ? 0.1404 0.1522 0.1461 -0.0081 -0.0064 0.0120 3   PHE A CG  
17   C  CD1 . PHE A 3   ? 0.1381 0.1496 0.1433 -0.0085 -0.0066 0.0121 3   PHE A CD1 
18   C  CD2 . PHE A 3   ? 0.1265 0.1383 0.1327 -0.0076 -0.0060 0.0118 3   PHE A CD2 
19   C  CE1 . PHE A 3   ? 0.1455 0.1568 0.1506 -0.0084 -0.0066 0.0120 3   PHE A CE1 
20   C  CE2 . PHE A 3   ? 0.1475 0.1591 0.1536 -0.0074 -0.0059 0.0118 3   PHE A CE2 
21   C  CZ  . PHE A 3   ? 0.1426 0.1540 0.1483 -0.0078 -0.0062 0.0119 3   PHE A CZ  
22   N  N   . ARG A 4   ? 0.1427 0.1549 0.1487 -0.0078 -0.0061 0.0122 4   ARG A N   
23   C  CA  . ARG A 4   ? 0.1185 0.1309 0.1249 -0.0074 -0.0058 0.0123 4   ARG A CA  
24   C  C   . ARG A 4   ? 0.1297 0.1419 0.1362 -0.0070 -0.0056 0.0122 4   ARG A C   
25   O  O   . ARG A 4   ? 0.0940 0.1055 0.0998 -0.0070 -0.0055 0.0121 4   ARG A O   
26   C  CB  . ARG A 4   ? 0.1422 0.1547 0.1484 -0.0076 -0.0060 0.0125 4   ARG A CB  
27   C  CG  . ARG A 4   ? 0.1708 0.1835 0.1770 -0.0078 -0.0061 0.0126 4   ARG A CG  
28   C  CD  . ARG A 4   ? 0.2095 0.2227 0.2164 -0.0073 -0.0058 0.0127 4   ARG A CD  
29   N  NE  . ARG A 4   ? 0.2292 0.2426 0.2362 -0.0075 -0.0059 0.0128 4   ARG A NE  
30   C  CZ  . ARG A 4   ? 0.2219 0.2358 0.2295 -0.0071 -0.0056 0.0129 4   ARG A CZ  
31   N  NH1 . ARG A 4   ? 0.2152 0.2291 0.2231 -0.0065 -0.0052 0.0128 4   ARG A NH1 
32   N  NH2 . ARG A 4   ? 0.1697 0.1839 0.1774 -0.0073 -0.0057 0.0130 4   ARG A NH2 
33   N  N   . LYS A 5   ? 0.1198 0.1318 0.1264 -0.0063 -0.0051 0.0121 5   LYS A N   
34   C  CA  . LYS A 5   ? 0.1639 0.1748 0.1698 -0.0056 -0.0044 0.0118 5   LYS A CA  
35   C  C   . LYS A 5   ? 0.1033 0.1130 0.1080 -0.0053 -0.0041 0.0117 5   LYS A C   
36   O  O   . LYS A 5   ? 0.1949 0.2044 0.1994 -0.0050 -0.0038 0.0117 5   LYS A O   
37   C  CB  . LYS A 5   ? 0.1540 0.1651 0.1604 -0.0050 -0.0041 0.0118 5   LYS A CB  
38   C  CG  . LYS A 5   ? 0.1776 0.1878 0.1834 -0.0044 -0.0036 0.0115 5   LYS A CG  
39   C  CD  . LYS A 5   ? 0.2289 0.2396 0.2355 -0.0042 -0.0035 0.0115 5   LYS A CD  
40   C  CE  . LYS A 5   ? 0.2303 0.2416 0.2375 -0.0046 -0.0038 0.0115 5   LYS A CE  
41   N  NZ  . LYS A 5   ? 0.1801 0.1906 0.1866 -0.0045 -0.0037 0.0114 5   LYS A NZ  
42   N  N   . MET A 6   ? 0.1273 0.1363 0.1312 -0.0054 -0.0041 0.0115 6   MET A N   
43   C  CA  . MET A 6   ? 0.1216 0.1295 0.1243 -0.0054 -0.0039 0.0114 6   MET A CA  
44   C  C   . MET A 6   ? 0.0780 0.0846 0.0797 -0.0046 -0.0033 0.0111 6   MET A C   
45   O  O   . MET A 6   ? 0.0332 0.0395 0.0348 -0.0045 -0.0032 0.0110 6   MET A O   
46   C  CB  . MET A 6   ? 0.0984 0.1062 0.1007 -0.0061 -0.0044 0.0115 6   MET A CB  
47   C  CG  . MET A 6   ? 0.2498 0.2575 0.2516 -0.0065 -0.0046 0.0116 6   MET A CG  
48   S  SD  . MET A 6   ? 0.2600 0.2677 0.2613 -0.0074 -0.0052 0.0118 6   MET A SD  
49   C  CE  . MET A 6   ? 0.1625 0.1687 0.1626 -0.0069 -0.0047 0.0114 6   MET A CE  
50   N  N   . ALA A 7   ? 0.1317 0.1374 0.1327 -0.0042 -0.0029 0.0110 7   ALA A N   
51   C  CA  . ALA A 7   ? 0.0898 0.0942 0.0898 -0.0035 -0.0023 0.0107 7   ALA A CA  
52   C  C   . ALA A 7   ? 0.1420 0.1454 0.1408 -0.0037 -0.0022 0.0107 7   ALA A C   
53   O  O   . ALA A 7   ? 0.0790 0.0825 0.0776 -0.0043 -0.0026 0.0108 7   ALA A O   
54   C  CB  . ALA A 7   ? 0.1072 0.1113 0.1070 -0.0029 -0.0018 0.0106 7   ALA A CB  
55   N  N   . PHE A 8   ? 0.1074 0.1095 0.1052 -0.0032 -0.0017 0.0104 8   PHE A N   
56   C  CA  . PHE A 8   ? 0.1093 0.1103 0.1059 -0.0032 -0.0015 0.0103 8   PHE A CA  
57   C  C   . PHE A 8   ? 0.0881 0.0885 0.0841 -0.0031 -0.0013 0.0103 8   PHE A C   
58   O  O   . PHE A 8   ? 0.0805 0.0811 0.0768 -0.0026 -0.0011 0.0103 8   PHE A O   
59   C  CB  . PHE A 8   ? 0.0640 0.0638 0.0597 -0.0027 -0.0010 0.0101 8   PHE A CB  
60   C  CG  . PHE A 8   ? 0.1176 0.1176 0.1135 -0.0030 -0.0012 0.0102 8   PHE A CG  
61   C  CD1 . PHE A 8   ? 0.1589 0.1587 0.1544 -0.0035 -0.0014 0.0103 8   PHE A CD1 
62   C  CD2 . PHE A 8   ? 0.1122 0.1127 0.1089 -0.0027 -0.0011 0.0101 8   PHE A CD2 
63   C  CE1 . PHE A 8   ? 0.2444 0.2444 0.2401 -0.0037 -0.0016 0.0103 8   PHE A CE1 
64   C  CE2 . PHE A 8   ? 0.1312 0.1320 0.1282 -0.0029 -0.0013 0.0102 8   PHE A CE2 
65   C  CZ  . PHE A 8   ? 0.2107 0.2113 0.2072 -0.0034 -0.0015 0.0103 8   PHE A CZ  
66   N  N   . PRO A 9   ? 0.0682 0.0681 0.0634 -0.0034 -0.0013 0.0104 9   PRO A N   
67   C  CA  . PRO A 9   ? 0.0790 0.0782 0.0736 -0.0031 -0.0010 0.0104 9   PRO A CA  
68   C  C   . PRO A 9   ? 0.0834 0.0814 0.0771 -0.0023 -0.0004 0.0101 9   PRO A C   
69   O  O   . PRO A 9   ? 0.0847 0.0818 0.0777 -0.0021 -0.0001 0.0099 9   PRO A O   
70   C  CB  . PRO A 9   ? 0.0803 0.0789 0.0740 -0.0036 -0.0012 0.0104 9   PRO A CB  
71   C  CG  . PRO A 9   ? 0.1394 0.1388 0.1335 -0.0044 -0.0017 0.0106 9   PRO A CG  
72   C  CD  . PRO A 9   ? 0.1221 0.1217 0.1168 -0.0040 -0.0016 0.0105 9   PRO A CD  
73   N  N   . SER A 10  ? 0.0928 0.0908 0.0867 -0.0019 -0.0002 0.0100 10  SER A N   
74   C  CA  . SER A 10  ? 0.1170 0.1142 0.1104 -0.0013 0.0003  0.0098 10  SER A CA  
75   C  C   . SER A 10  ? 0.0779 0.0737 0.0699 -0.0011 0.0006  0.0096 10  SER A C   
76   O  O   . SER A 10  ? 0.0947 0.0900 0.0865 -0.0007 0.0009  0.0094 10  SER A O   
77   C  CB  . SER A 10  ? 0.0910 0.0891 0.0854 -0.0010 0.0002  0.0098 10  SER A CB  
78   O  OG  . SER A 10  ? 0.0675 0.0659 0.0619 -0.0011 0.0002  0.0100 10  SER A OG  
79   N  N   . GLY A 11  ? 0.0752 0.0706 0.0667 -0.0014 0.0006  0.0097 11  GLY A N   
80   C  CA  . GLY A 11  ? 0.0751 0.0692 0.0653 -0.0012 0.0010  0.0096 11  GLY A CA  
81   C  C   . GLY A 11  ? 0.0830 0.0757 0.0721 -0.0010 0.0012  0.0093 11  GLY A C   
82   O  O   . GLY A 11  ? 0.0842 0.0766 0.0731 -0.0010 0.0012  0.0091 11  GLY A O   
83   N  N   . LYS A 12  ? 0.0460 0.0384 0.0349 -0.0011 0.0013  0.0092 12  LYS A N   
84   C  CA  . LYS A 12  ? 0.0693 0.0610 0.0577 -0.0012 0.0013  0.0088 12  LYS A CA  
85   C  C   . LYS A 12  ? 0.0976 0.0902 0.0870 -0.0010 0.0011  0.0090 12  LYS A C   
86   O  O   . LYS A 12  ? 0.0997 0.0926 0.0895 -0.0008 0.0013  0.0090 12  LYS A O   
87   C  CB  . LYS A 12  ? 0.1305 0.1219 0.1187 -0.0012 0.0014  0.0088 12  LYS A CB  
88   C  CG  . LYS A 12  ? 0.1538 0.1448 0.1416 -0.0010 0.0019  0.0089 12  LYS A CG  
89   C  CD  . LYS A 12  ? 0.2209 0.2128 0.2093 -0.0012 0.0018  0.0095 12  LYS A CD  
90   C  CE  . LYS A 12  ? 0.3338 0.3258 0.3220 -0.0015 0.0019  0.0099 12  LYS A CE  
91   N  NZ  . LYS A 12  ? 0.3777 0.3695 0.3660 -0.0010 0.0024  0.0098 12  LYS A NZ  
92   N  N   . VAL A 13  ? 0.0618 0.0552 0.0521 -0.0006 0.0011  0.0090 13  VAL A N   
93   C  CA  . VAL A 13  ? 0.0560 0.0503 0.0474 -0.0001 0.0013  0.0089 13  VAL A CA  
94   C  C   . VAL A 13  ? 0.0558 0.0505 0.0476 0.0003  0.0015  0.0089 13  VAL A C   
95   O  O   . VAL A 13  ? 0.0582 0.0532 0.0504 0.0009  0.0019  0.0088 13  VAL A O   
96   C  CB  . VAL A 13  ? 0.0694 0.0646 0.0617 0.0001  0.0012  0.0089 13  VAL A CB  
97   C  CG1 . VAL A 13  ? 0.0470 0.0428 0.0402 0.0007  0.0015  0.0088 13  VAL A CG1 
98   C  CG2 . VAL A 13  ? 0.0643 0.0591 0.0563 -0.0002 0.0011  0.0089 13  VAL A CG2 
99   N  N   . GLU A 14  ? 0.0482 0.0428 0.0397 0.0000  0.0013  0.0091 14  GLU A N   
100  C  CA  . GLU A 14  ? 0.0658 0.0608 0.0576 0.0004  0.0015  0.0091 14  GLU A CA  
101  C  C   . GLU A 14  ? 0.0671 0.0617 0.0586 0.0007  0.0018  0.0090 14  GLU A C   
102  O  O   . GLU A 14  ? 0.0318 0.0268 0.0238 0.0014  0.0023  0.0089 14  GLU A O   
103  C  CB  . GLU A 14  ? 0.0703 0.0652 0.0617 0.0000  0.0013  0.0093 14  GLU A CB  
104  C  CG  . GLU A 14  ? 0.0712 0.0671 0.0635 -0.0001 0.0011  0.0095 14  GLU A CG  
105  C  CD  . GLU A 14  ? 0.0888 0.0848 0.0809 -0.0005 0.0009  0.0097 14  GLU A CD  
106  O  OE1 . GLU A 14  ? 0.0762 0.0720 0.0680 -0.0005 0.0009  0.0098 14  GLU A OE1 
107  O  OE2 . GLU A 14  ? 0.0747 0.0714 0.0674 -0.0009 0.0006  0.0099 14  GLU A OE2 
108  N  N   . GLY A 15  ? 0.0592 0.0531 0.0499 0.0003  0.0017  0.0090 15  GLY A N   
109  C  CA  . GLY A 15  ? 0.0850 0.0786 0.0756 0.0006  0.0021  0.0090 15  GLY A CA  
110  C  C   . GLY A 15  ? 0.0883 0.0820 0.0793 0.0015  0.0027  0.0086 15  GLY A C   
111  O  O   . GLY A 15  ? 0.0660 0.0592 0.0568 0.0020  0.0032  0.0085 15  GLY A O   
112  N  N   . CYS A 16  ? 0.0857 0.0798 0.0773 0.0017  0.0027  0.0086 16  CYS A N   
113  C  CA  . CYS A 16  ? 0.0807 0.0748 0.0726 0.0025  0.0033  0.0083 16  CYS A CA  
114  C  C   . CYS A 16  ? 0.0745 0.0691 0.0670 0.0032  0.0036  0.0081 16  CYS A C   
115  O  O   . CYS A 16  ? 0.0739 0.0685 0.0666 0.0039  0.0041  0.0078 16  CYS A O   
116  C  CB  . CYS A 16  ? 0.0399 0.0341 0.0320 0.0023  0.0031  0.0083 16  CYS A CB  
117  S  SG  . CYS A 16  ? 0.1227 0.1163 0.1140 0.0015  0.0027  0.0085 16  CYS A SG  
118  N  N   . MET A 17  ? 0.0747 0.0697 0.0674 0.0031  0.0034  0.0082 17  MET A N   
119  C  CA  . MET A 17  ? 0.0702 0.0658 0.0635 0.0036  0.0037  0.0081 17  MET A CA  
120  C  C   . MET A 17  ? 0.1163 0.1116 0.1094 0.0044  0.0043  0.0079 17  MET A C   
121  O  O   . MET A 17  ? 0.0925 0.0875 0.0853 0.0043  0.0043  0.0080 17  MET A O   
122  C  CB  . MET A 17  ? 0.1027 0.0988 0.0963 0.0032  0.0032  0.0084 17  MET A CB  
123  C  CG  . MET A 17  ? 0.0738 0.0702 0.0676 0.0025  0.0027  0.0085 17  MET A CG  
124  S  SD  . MET A 17  ? 0.0726 0.0691 0.0667 0.0027  0.0028  0.0084 17  MET A SD  
125  C  CE  . MET A 17  ? 0.0892 0.0861 0.0838 0.0035  0.0032  0.0082 17  MET A CE  
126  N  N   . VAL A 18  ? 0.0849 0.0802 0.0781 0.0052  0.0048  0.0076 18  VAL A N   
127  C  CA  . VAL A 18  ? 0.0785 0.0734 0.0715 0.0060  0.0055  0.0074 18  VAL A CA  
128  C  C   . VAL A 18  ? 0.0972 0.0925 0.0905 0.0065  0.0057  0.0072 18  VAL A C   
129  O  O   . VAL A 18  ? 0.0762 0.0719 0.0698 0.0062  0.0054  0.0073 18  VAL A O   
130  C  CB  . VAL A 18  ? 0.0811 0.0754 0.0737 0.0065  0.0060  0.0071 18  VAL A CB  
131  C  CG1 . VAL A 18  ? 0.0853 0.0792 0.0775 0.0060  0.0057  0.0072 18  VAL A CG1 
132  C  CG2 . VAL A 18  ? 0.0625 0.0569 0.0552 0.0068  0.0061  0.0069 18  VAL A CG2 
133  N  N   . GLN A 19  ? 0.1360 0.1310 0.1290 0.0072  0.0062  0.0070 19  GLN A N   
134  C  CA  . GLN A 19  ? 0.1453 0.1404 0.1383 0.0077  0.0066  0.0069 19  GLN A CA  
135  C  C   . GLN A 19  ? 0.1170 0.1117 0.1097 0.0085  0.0072  0.0065 19  GLN A C   
136  O  O   . GLN A 19  ? 0.1289 0.1230 0.1211 0.0089  0.0076  0.0063 19  GLN A O   
137  C  CB  . GLN A 19  ? 0.1635 0.1588 0.1566 0.0080  0.0068  0.0070 19  GLN A CB  
138  C  CG  . GLN A 19  ? 0.1915 0.1867 0.1844 0.0087  0.0072  0.0068 19  GLN A CG  
139  C  CD  . GLN A 19  ? 0.2890 0.2842 0.2817 0.0092  0.0076  0.0068 19  GLN A CD  
140  O  OE1 . GLN A 19  ? 0.3938 0.3895 0.3869 0.0090  0.0074  0.0070 19  GLN A OE1 
141  N  NE2 . GLN A 19  ? 0.2911 0.2857 0.2833 0.0098  0.0082  0.0065 19  GLN A NE2 
142  N  N   . VAL A 20  ? 0.1281 0.1228 0.1207 0.0086  0.0072  0.0064 20  VAL A N   
143  C  CA  . VAL A 20  ? 0.1485 0.1428 0.1407 0.0092  0.0077  0.0061 20  VAL A CA  
144  C  C   . VAL A 20  ? 0.1557 0.1498 0.1476 0.0097  0.0080  0.0059 20  VAL A C   
145  O  O   . VAL A 20  ? 0.1778 0.1723 0.1699 0.0095  0.0078  0.0060 20  VAL A O   
146  C  CB  . VAL A 20  ? 0.1396 0.1340 0.1320 0.0088  0.0074  0.0061 20  VAL A CB  
147  C  CG1 . VAL A 20  ? 0.0906 0.0845 0.0825 0.0094  0.0079  0.0059 20  VAL A CG1 
148  C  CG2 . VAL A 20  ? 0.0774 0.0718 0.0700 0.0083  0.0071  0.0063 20  VAL A CG2 
149  N  N   . THR A 21  ? 0.1898 0.1835 0.1812 0.0097  0.0080  0.0057 21  THR A N   
150  C  CA  . THR A 21  ? 0.1598 0.1533 0.1508 0.0099  0.0080  0.0055 21  THR A CA  
151  C  C   . THR A 21  ? 0.1841 0.1771 0.1747 0.0099  0.0080  0.0053 21  THR A C   
152  O  O   . THR A 21  ? 0.1946 0.1874 0.1851 0.0099  0.0080  0.0052 21  THR A O   
153  C  CB  . THR A 21  ? 0.1968 0.1902 0.1877 0.0100  0.0081  0.0055 21  THR A CB  
154  O  OG1 . THR A 21  ? 0.1419 0.1357 0.1332 0.0100  0.0081  0.0058 21  THR A OG1 
155  C  CG2 . THR A 21  ? 0.1419 0.1350 0.1323 0.0102  0.0081  0.0053 21  THR A CG2 
156  N  N   . CYS A 22  ? 0.2001 0.1930 0.1904 0.0100  0.0079  0.0052 22  CYS A N   
157  C  CA  . CYS A 22  ? 0.2006 0.1932 0.1905 0.0101  0.0079  0.0051 22  CYS A CA  
158  C  C   . CYS A 22  ? 0.1662 0.1585 0.1556 0.0103  0.0079  0.0050 22  CYS A C   
159  O  O   . CYS A 22  ? 0.1906 0.1829 0.1799 0.0104  0.0079  0.0050 22  CYS A O   
160  C  CB  . CYS A 22  ? 0.1451 0.1377 0.1350 0.0100  0.0079  0.0051 22  CYS A CB  
161  S  SG  . CYS A 22  ? 0.2627 0.2548 0.2521 0.0101  0.0079  0.0050 22  CYS A SG  
162  N  N   . GLY A 23  ? 0.2520 0.2439 0.2410 0.0104  0.0080  0.0048 23  GLY A N   
163  C  CA  . GLY A 23  ? 0.2250 0.2167 0.2135 0.0106  0.0080  0.0047 23  GLY A CA  
164  C  C   . GLY A 23  ? 0.2042 0.1961 0.1929 0.0107  0.0080  0.0049 23  GLY A C   
165  O  O   . GLY A 23  ? 0.2497 0.2419 0.2389 0.0106  0.0080  0.0049 23  GLY A O   
166  N  N   . THR A 24  ? 0.3099 0.3017 0.2983 0.0108  0.0079  0.0049 24  THR A N   
167  C  CA  . THR A 24  ? 0.3239 0.3160 0.3126 0.0108  0.0080  0.0050 24  THR A CA  
168  C  C   . THR A 24  ? 0.2670 0.2597 0.2563 0.0106  0.0079  0.0053 24  THR A C   
169  O  O   . THR A 24  ? 0.3197 0.3128 0.3094 0.0106  0.0080  0.0054 24  THR A O   
170  C  CB  . THR A 24  ? 0.3740 0.3658 0.3621 0.0111  0.0080  0.0050 24  THR A CB  
171  O  OG1 . THR A 24  ? 0.4156 0.4071 0.4033 0.0111  0.0079  0.0049 24  THR A OG1 
172  C  CG2 . THR A 24  ? 0.4321 0.4233 0.4195 0.0113  0.0080  0.0048 24  THR A CG2 
173  N  N   . THR A 25  ? 0.2895 0.2822 0.2789 0.0105  0.0079  0.0053 25  THR A N   
174  C  CA  . THR A 25  ? 0.2690 0.2623 0.2591 0.0104  0.0078  0.0055 25  THR A CA  
175  C  C   . THR A 25  ? 0.1911 0.1848 0.1818 0.0102  0.0079  0.0057 25  THR A C   
176  O  O   . THR A 25  ? 0.1840 0.1775 0.1746 0.0101  0.0079  0.0055 25  THR A O   
177  C  CB  . THR A 25  ? 0.2827 0.2760 0.2728 0.0103  0.0078  0.0055 25  THR A CB  
178  O  OG1 . THR A 25  ? 0.2393 0.2321 0.2287 0.0105  0.0078  0.0055 25  THR A OG1 
179  C  CG2 . THR A 25  ? 0.2349 0.2289 0.2258 0.0099  0.0076  0.0059 25  THR A CG2 
180  N  N   . THR A 26  ? 0.1687 0.1630 0.1599 0.0101  0.0079  0.0059 26  THR A N   
181  C  CA  . THR A 26  ? 0.1868 0.1816 0.1787 0.0099  0.0078  0.0061 26  THR A CA  
182  C  C   . THR A 26  ? 0.1876 0.1829 0.1801 0.0091  0.0072  0.0064 26  THR A C   
183  O  O   . THR A 26  ? 0.2172 0.2128 0.2099 0.0089  0.0069  0.0066 26  THR A O   
184  C  CB  . THR A 26  ? 0.1790 0.1739 0.1710 0.0101  0.0080  0.0063 26  THR A CB  
185  O  OG1 . THR A 26  ? 0.2425 0.2369 0.2340 0.0102  0.0081  0.0060 26  THR A OG1 
186  C  CG2 . THR A 26  ? 0.1974 0.1927 0.1900 0.0094  0.0076  0.0065 26  THR A CG2 
187  N  N   . LEU A 27  ? 0.1268 0.1223 0.1196 0.0086  0.0068  0.0065 27  LEU A N   
188  C  CA  . LEU A 27  ? 0.1111 0.1072 0.1046 0.0078  0.0062  0.0068 27  LEU A CA  
189  C  C   . LEU A 27  ? 0.0691 0.0652 0.0628 0.0074  0.0060  0.0070 27  LEU A C   
190  O  O   . LEU A 27  ? 0.0795 0.0753 0.0730 0.0077  0.0063  0.0068 27  LEU A O   
191  C  CB  . LEU A 27  ? 0.1208 0.1169 0.1143 0.0076  0.0060  0.0068 27  LEU A CB  
192  C  CG  . LEU A 27  ? 0.1046 0.1001 0.0976 0.0081  0.0063  0.0065 27  LEU A CG  
193  C  CD1 . LEU A 27  ? 0.1433 0.1388 0.1365 0.0079  0.0064  0.0065 27  LEU A CD1 
194  C  CD2 . LEU A 27  ? 0.1119 0.1074 0.1049 0.0078  0.0060  0.0066 27  LEU A CD2 
195  N  N   . ASN A 28  ? 0.0709 0.0674 0.0651 0.0066  0.0054  0.0072 28  ASN A N   
196  C  CA  . ASN A 28  ? 0.0551 0.0517 0.0494 0.0061  0.0051  0.0074 28  ASN A CA  
197  C  C   . ASN A 28  ? 0.0687 0.0650 0.0629 0.0062  0.0052  0.0072 28  ASN A C   
198  O  O   . ASN A 28  ? 0.0422 0.0385 0.0364 0.0063  0.0052  0.0071 28  ASN A O   
199  C  CB  . ASN A 28  ? 0.0732 0.0703 0.0680 0.0053  0.0044  0.0077 28  ASN A CB  
200  C  CG  . ASN A 28  ? 0.0900 0.0875 0.0850 0.0053  0.0043  0.0079 28  ASN A CG  
201  O  OD1 . ASN A 28  ? 0.0724 0.0699 0.0673 0.0053  0.0044  0.0079 28  ASN A OD1 
202  N  ND2 . ASN A 28  ? 0.0985 0.0963 0.0937 0.0052  0.0042  0.0079 28  ASN A ND2 
203  N  N   . GLY A 29  ? 0.0374 0.0334 0.0314 0.0060  0.0052  0.0072 29  GLY A N   
204  C  CA  . GLY A 29  ? 0.0317 0.0274 0.0256 0.0061  0.0053  0.0071 29  GLY A CA  
205  C  C   . GLY A 29  ? 0.0456 0.0412 0.0394 0.0054  0.0049  0.0073 29  GLY A C   
206  O  O   . GLY A 29  ? 0.0456 0.0413 0.0394 0.0050  0.0046  0.0075 29  GLY A O   
207  N  N   . LEU A 30  ? 0.0443 0.0397 0.0381 0.0053  0.0049  0.0073 30  LEU A N   
208  C  CA  . LEU A 30  ? 0.0790 0.0742 0.0726 0.0047  0.0045  0.0075 30  LEU A CA  
209  C  C   . LEU A 30  ? 0.0525 0.0471 0.0457 0.0050  0.0049  0.0074 30  LEU A C   
210  O  O   . LEU A 30  ? 0.0534 0.0479 0.0466 0.0054  0.0053  0.0072 30  LEU A O   
211  C  CB  . LEU A 30  ? 0.0284 0.0240 0.0223 0.0042  0.0041  0.0077 30  LEU A CB  
212  C  CG  . LEU A 30  ? 0.0870 0.0825 0.0808 0.0035  0.0036  0.0079 30  LEU A CG  
213  C  CD1 . LEU A 30  ? 0.0709 0.0665 0.0646 0.0028  0.0031  0.0081 30  LEU A CD1 
214  C  CD2 . LEU A 30  ? 0.0713 0.0670 0.0653 0.0032  0.0034  0.0080 30  LEU A CD2 
215  N  N   . TRP A 31  ? 0.0643 0.0585 0.0570 0.0049  0.0049  0.0074 31  TRP A N   
216  C  CA  . TRP A 31  ? 0.0922 0.0856 0.0843 0.0052  0.0054  0.0072 31  TRP A CA  
217  C  C   . TRP A 31  ? 0.0813 0.0744 0.0731 0.0046  0.0050  0.0074 31  TRP A C   
218  O  O   . TRP A 31  ? 0.0743 0.0674 0.0659 0.0039  0.0046  0.0076 31  TRP A O   
219  C  CB  . TRP A 31  ? 0.0759 0.0690 0.0677 0.0055  0.0056  0.0071 31  TRP A CB  
220  C  CG  . TRP A 31  ? 0.0973 0.0896 0.0885 0.0059  0.0061  0.0069 31  TRP A CG  
221  C  CD1 . TRP A 31  ? 0.0831 0.0750 0.0741 0.0063  0.0065  0.0067 31  TRP A CD1 
222  C  CD2 . TRP A 31  ? 0.1243 0.1161 0.1150 0.0059  0.0062  0.0069 31  TRP A CD2 
223  N  NE1 . TRP A 31  ? 0.1206 0.1116 0.1110 0.0065  0.0069  0.0066 31  TRP A NE1 
224  C  CE2 . TRP A 31  ? 0.1250 0.1160 0.1152 0.0063  0.0067  0.0067 31  TRP A CE2 
225  C  CE3 . TRP A 31  ? 0.1060 0.0980 0.0967 0.0055  0.0059  0.0071 31  TRP A CE3 
226  C  CZ2 . TRP A 31  ? 0.1230 0.1134 0.1127 0.0064  0.0069  0.0066 31  TRP A CZ2 
227  C  CZ3 . TRP A 31  ? 0.1544 0.1457 0.1445 0.0056  0.0061  0.0071 31  TRP A CZ3 
228  C  CH2 . TRP A 31  ? 0.1058 0.0963 0.0954 0.0061  0.0066  0.0068 31  TRP A CH2 
229  N  N   . LEU A 32  ? 0.0918 0.0846 0.0835 0.0048  0.0053  0.0073 32  LEU A N   
230  C  CA  . LEU A 32  ? 0.1083 0.1008 0.0997 0.0043  0.0051  0.0074 32  LEU A CA  
231  C  C   . LEU A 32  ? 0.1381 0.1298 0.1291 0.0049  0.0058  0.0072 32  LEU A C   
232  O  O   . LEU A 32  ? 0.1177 0.1095 0.1089 0.0056  0.0062  0.0070 32  LEU A O   
233  C  CB  . LEU A 32  ? 0.0849 0.0779 0.0768 0.0039  0.0047  0.0076 32  LEU A CB  
234  C  CG  . LEU A 32  ? 0.1049 0.0986 0.0972 0.0033  0.0041  0.0079 32  LEU A CG  
235  C  CD1 . LEU A 32  ? 0.0520 0.0462 0.0449 0.0032  0.0039  0.0080 32  LEU A CD1 
236  C  CD2 . LEU A 32  ? 0.0692 0.0627 0.0610 0.0025  0.0036  0.0081 32  LEU A CD2 
237  N  N   . ASP A 33  ? 0.1163 0.1072 0.1065 0.0046  0.0058  0.0072 33  ASP A N   
238  C  CA  . ASP A 33  ? 0.1522 0.1423 0.1420 0.0052  0.0065  0.0069 33  ASP A CA  
239  C  C   . ASP A 33  ? 0.1218 0.1119 0.1117 0.0061  0.0070  0.0066 33  ASP A C   
240  O  O   . ASP A 33  ? 0.1283 0.1187 0.1183 0.0060  0.0068  0.0067 33  ASP A O   
241  C  CB  . ASP A 33  ? 0.1425 0.1326 0.1324 0.0054  0.0067  0.0069 33  ASP A CB  
242  C  CG  . ASP A 33  ? 0.1878 0.1777 0.1774 0.0045  0.0062  0.0072 33  ASP A CG  
243  O  OD1 . ASP A 33  ? 0.1850 0.1745 0.1740 0.0040  0.0059  0.0073 33  ASP A OD1 
244  O  OD2 . ASP A 33  ? 0.1735 0.1639 0.1635 0.0044  0.0060  0.0074 33  ASP A OD2 
245  N  N   . ASP A 34  ? 0.1100 0.1000 0.0999 0.0068  0.0076  0.0064 34  ASP A N   
246  C  CA  . ASP A 34  ? 0.1141 0.1041 0.1041 0.0076  0.0081  0.0061 34  ASP A CA  
247  C  C   . ASP A 34  ? 0.1038 0.0945 0.0944 0.0079  0.0082  0.0061 34  ASP A C   
248  O  O   . ASP A 34  ? 0.1120 0.1027 0.1026 0.0086  0.0087  0.0059 34  ASP A O   
249  C  CB  . ASP A 34  ? 0.1258 0.1150 0.1153 0.0082  0.0089  0.0059 34  ASP A CB  
250  C  CG  . ASP A 34  ? 0.1862 0.1753 0.1759 0.0084  0.0091  0.0059 34  ASP A CG  
251  O  OD1 . ASP A 34  ? 0.1572 0.1469 0.1473 0.0080  0.0087  0.0061 34  ASP A OD1 
252  O  OD2 . ASP A 34  ? 0.2746 0.2631 0.2639 0.0089  0.0097  0.0057 34  ASP A OD2 
253  N  N   . VAL A 35  ? 0.0711 0.0626 0.0623 0.0074  0.0076  0.0063 35  VAL A N   
254  C  CA  . VAL A 35  ? 0.0874 0.0796 0.0792 0.0076  0.0076  0.0064 35  VAL A CA  
255  C  C   . VAL A 35  ? 0.0886 0.0813 0.0806 0.0071  0.0071  0.0065 35  VAL A C   
256  O  O   . VAL A 35  ? 0.0665 0.0594 0.0586 0.0065  0.0065  0.0067 35  VAL A O   
257  C  CB  . VAL A 35  ? 0.0489 0.0415 0.0411 0.0073  0.0074  0.0065 35  VAL A CB  
258  C  CG1 . VAL A 35  ? 0.0766 0.0698 0.0692 0.0075  0.0073  0.0065 35  VAL A CG1 
259  C  CG2 . VAL A 35  ? 0.0650 0.0570 0.0568 0.0078  0.0080  0.0064 35  VAL A CG2 
260  N  N   . VAL A 36  ? 0.0590 0.0521 0.0512 0.0076  0.0072  0.0064 36  VAL A N   
261  C  CA  . VAL A 36  ? 0.0839 0.0775 0.0765 0.0073  0.0068  0.0065 36  VAL A CA  
262  C  C   . VAL A 36  ? 0.0846 0.0788 0.0776 0.0072  0.0067  0.0066 36  VAL A C   
263  O  O   . VAL A 36  ? 0.0634 0.0574 0.0563 0.0077  0.0071  0.0064 36  VAL A O   
264  C  CB  . VAL A 36  ? 0.1001 0.0935 0.0924 0.0077  0.0072  0.0063 36  VAL A CB  
265  C  CG1 . VAL A 36  ? 0.0497 0.0437 0.0424 0.0075  0.0068  0.0065 36  VAL A CG1 
266  C  CG2 . VAL A 36  ? 0.0788 0.0717 0.0707 0.0076  0.0072  0.0063 36  VAL A CG2 
267  N  N   . TYR A 37  ? 0.0544 0.0491 0.0478 0.0066  0.0061  0.0068 37  TYR A N   
268  C  CA  . TYR A 37  ? 0.0510 0.0462 0.0449 0.0064  0.0058  0.0069 37  TYR A CA  
269  C  C   . TYR A 37  ? 0.0471 0.0425 0.0410 0.0064  0.0056  0.0069 37  TYR A C   
270  O  O   . TYR A 37  ? 0.0612 0.0569 0.0553 0.0060  0.0054  0.0071 37  TYR A O   
271  C  CB  . TYR A 37  ? 0.0857 0.0811 0.0798 0.0057  0.0053  0.0072 37  TYR A CB  
272  C  CG  . TYR A 37  ? 0.0946 0.0897 0.0886 0.0057  0.0055  0.0072 37  TYR A CG  
273  C  CD1 . TYR A 37  ? 0.0504 0.0450 0.0440 0.0056  0.0055  0.0072 37  TYR A CD1 
274  C  CD2 . TYR A 37  ? 0.0784 0.0736 0.0726 0.0059  0.0056  0.0072 37  TYR A CD2 
275  C  CE1 . TYR A 37  ? 0.0507 0.0449 0.0440 0.0056  0.0057  0.0072 37  TYR A CE1 
276  C  CE2 . TYR A 37  ? 0.0625 0.0573 0.0565 0.0059  0.0058  0.0073 37  TYR A CE2 
277  C  CZ  . TYR A 37  ? 0.0581 0.0524 0.0517 0.0058  0.0058  0.0072 37  TYR A CZ  
278  O  OH  . TYR A 37  ? 0.1050 0.0989 0.0984 0.0058  0.0061  0.0073 37  TYR A OH  
279  N  N   . CYS A 38  ? 0.0777 0.0733 0.0717 0.0067  0.0058  0.0069 38  CYS A N   
280  C  CA  . CYS A 38  ? 0.0510 0.0468 0.0451 0.0066  0.0056  0.0069 38  CYS A CA  
281  C  C   . CYS A 38  ? 0.0674 0.0633 0.0615 0.0067  0.0055  0.0069 38  CYS A C   
282  O  O   . CYS A 38  ? 0.0650 0.0608 0.0591 0.0068  0.0057  0.0069 38  CYS A O   
283  C  CB  . CYS A 38  ? 0.0514 0.0469 0.0450 0.0072  0.0061  0.0067 38  CYS A CB  
284  S  SG  . CYS A 38  ? 0.0941 0.0889 0.0870 0.0081  0.0068  0.0063 38  CYS A SG  
285  N  N   . PRO A 39  ? 0.0363 0.0324 0.0305 0.0065  0.0053  0.0070 39  PRO A N   
286  C  CA  . PRO A 39  ? 0.0689 0.0649 0.0630 0.0065  0.0052  0.0070 39  PRO A CA  
287  C  C   . PRO A 39  ? 0.0622 0.0577 0.0557 0.0072  0.0057  0.0067 39  PRO A C   
288  O  O   . PRO A 39  ? 0.0201 0.0153 0.0131 0.0077  0.0061  0.0065 39  PRO A O   
289  C  CB  . PRO A 39  ? 0.0682 0.0645 0.0624 0.0063  0.0049  0.0071 39  PRO A CB  
290  C  CG  . PRO A 39  ? 0.0510 0.0476 0.0455 0.0060  0.0047  0.0072 39  PRO A CG  
291  C  CD  . PRO A 39  ? 0.0498 0.0461 0.0441 0.0063  0.0051  0.0071 39  PRO A CD  
292  N  N   . ARG A 40  ? 0.0581 0.0534 0.0514 0.0072  0.0057  0.0067 40  ARG A N   
293  C  CA  . ARG A 40  ? 0.0733 0.0681 0.0660 0.0078  0.0062  0.0065 40  ARG A CA  
294  C  C   . ARG A 40  ? 0.0657 0.0601 0.0577 0.0082  0.0062  0.0064 40  ARG A C   
295  O  O   . ARG A 40  ? 0.0647 0.0586 0.0560 0.0087  0.0067  0.0061 40  ARG A O   
296  C  CB  . ARG A 40  ? 0.0828 0.0775 0.0755 0.0077  0.0060  0.0066 40  ARG A CB  
297  C  CG  . ARG A 40  ? 0.0528 0.0477 0.0457 0.0073  0.0055  0.0068 40  ARG A CG  
298  C  CD  . ARG A 40  ? 0.0602 0.0550 0.0531 0.0072  0.0054  0.0070 40  ARG A CD  
299  N  NE  . ARG A 40  ? 0.0874 0.0823 0.0804 0.0067  0.0048  0.0072 40  ARG A NE  
300  C  CZ  . ARG A 40  ? 0.0991 0.0938 0.0921 0.0066  0.0046  0.0074 40  ARG A CZ  
301  N  NH1 . ARG A 40  ? 0.0591 0.0537 0.0520 0.0068  0.0049  0.0074 40  ARG A NH1 
302  N  NH2 . ARG A 40  ? 0.1185 0.1132 0.1116 0.0061  0.0040  0.0076 40  ARG A NH2 
303  N  N   . HIS A 41  ? 0.0651 0.0598 0.0574 0.0078  0.0058  0.0065 41  HIS A N   
304  C  CA  . HIS A 41  ? 0.0959 0.0901 0.0875 0.0082  0.0060  0.0063 41  HIS A CA  
305  C  C   . HIS A 41  ? 0.1091 0.1031 0.1003 0.0087  0.0065  0.0061 41  HIS A C   
306  O  O   . HIS A 41  ? 0.1583 0.1518 0.1489 0.0091  0.0067  0.0060 41  HIS A O   
307  C  CB  . HIS A 41  ? 0.1035 0.0979 0.0953 0.0077  0.0054  0.0065 41  HIS A CB  
308  C  CG  . HIS A 41  ? 0.1179 0.1129 0.1104 0.0073  0.0052  0.0067 41  HIS A CG  
309  N  ND1 . HIS A 41  ? 0.0659 0.0615 0.0591 0.0066  0.0047  0.0070 41  HIS A ND1 
310  C  CD2 . HIS A 41  ? 0.1244 0.1195 0.1169 0.0075  0.0054  0.0067 41  HIS A CD2 
311  C  CE1 . HIS A 41  ? 0.0726 0.0687 0.0663 0.0064  0.0046  0.0071 41  HIS A CE1 
312  N  NE2 . HIS A 41  ? 0.1085 0.1043 0.1017 0.0069  0.0050  0.0069 41  HIS A NE2 
313  N  N   . VAL A 42  ? 0.1014 0.0956 0.0929 0.0087  0.0067  0.0061 42  VAL A N   
314  C  CA  . VAL A 42  ? 0.0952 0.0892 0.0865 0.0093  0.0072  0.0059 42  VAL A CA  
315  C  C   . VAL A 42  ? 0.1324 0.1256 0.1227 0.0100  0.0077  0.0056 42  VAL A C   
316  O  O   . VAL A 42  ? 0.1881 0.1810 0.1781 0.0101  0.0078  0.0054 42  VAL A O   
317  C  CB  . VAL A 42  ? 0.0947 0.0889 0.0864 0.0092  0.0073  0.0059 42  VAL A CB  
318  C  CG1 . VAL A 42  ? 0.0944 0.0884 0.0859 0.0093  0.0075  0.0059 42  VAL A CG1 
319  C  CG2 . VAL A 42  ? 0.0969 0.0908 0.0883 0.0097  0.0078  0.0058 42  VAL A CG2 
320  N  N   . ILE A 43  ? 0.1257 0.1186 0.1157 0.0101  0.0077  0.0056 43  ILE A N   
321  C  CA  . ILE A 43  ? 0.1243 0.1166 0.1136 0.0103  0.0078  0.0053 43  ILE A CA  
322  C  C   . ILE A 43  ? 0.2112 0.2030 0.1996 0.0106  0.0078  0.0053 43  ILE A C   
323  O  O   . ILE A 43  ? 0.2323 0.2234 0.2200 0.0108  0.0078  0.0051 43  ILE A O   
324  C  CB  . ILE A 43  ? 0.0810 0.0732 0.0703 0.0103  0.0079  0.0054 43  ILE A CB  
325  C  CG1 . ILE A 43  ? 0.0858 0.0781 0.0751 0.0102  0.0077  0.0056 43  ILE A CG1 
326  C  CG2 . ILE A 43  ? 0.1291 0.1217 0.1190 0.0101  0.0079  0.0054 43  ILE A CG2 
327  C  CD1 . ILE A 43  ? 0.0898 0.0820 0.0791 0.0102  0.0078  0.0056 43  ILE A CD1 
328  N  N   . CYS A 44  ? 0.2226 0.2145 0.2111 0.0105  0.0076  0.0054 44  CYS A N   
329  C  CA  . CYS A 44  ? 0.2565 0.2479 0.2443 0.0106  0.0074  0.0053 44  CYS A CA  
330  C  C   . CYS A 44  ? 0.2947 0.2858 0.2820 0.0110  0.0077  0.0052 44  CYS A C   
331  O  O   . CYS A 44  ? 0.3066 0.2982 0.2945 0.0109  0.0077  0.0052 44  CYS A O   
332  C  CB  . CYS A 44  ? 0.2773 0.2691 0.2657 0.0098  0.0067  0.0057 44  CYS A CB  
333  S  SG  . CYS A 44  ? 0.2460 0.2381 0.2350 0.0093  0.0063  0.0059 44  CYS A SG  
334  N  N   . THR A 45  ? 0.3921 0.3823 0.3783 0.0113  0.0077  0.0050 45  THR A N   
335  C  CA  . THR A 45  ? 0.4158 0.4058 0.4016 0.0115  0.0076  0.0049 45  THR A CA  
336  C  C   . THR A 45  ? 0.4222 0.4121 0.4078 0.0114  0.0074  0.0050 45  THR A C   
337  O  O   . THR A 45  ? 0.3911 0.3813 0.3773 0.0108  0.0069  0.0053 45  THR A O   
338  C  CB  . THR A 45  ? 0.3690 0.3581 0.3538 0.0117  0.0076  0.0047 45  THR A CB  
339  O  OG1 . THR A 45  ? 0.4091 0.3975 0.3930 0.0120  0.0076  0.0046 45  THR A OG1 
340  C  CG2 . THR A 45  ? 0.3325 0.3219 0.3177 0.0116  0.0077  0.0047 45  THR A CG2 
341  N  N   . SER A 46  ? 0.4337 0.4232 0.4187 0.0118  0.0076  0.0049 46  SER A N   
342  C  CA  . SER A 46  ? 0.4157 0.4052 0.4008 0.0114  0.0071  0.0051 46  SER A CA  
343  C  C   . SER A 46  ? 0.4398 0.4286 0.4242 0.0112  0.0066  0.0051 46  SER A C   
344  O  O   . SER A 46  ? 0.4106 0.3999 0.3957 0.0105  0.0060  0.0054 46  SER A O   
345  C  CB  . SER A 46  ? 0.4298 0.4188 0.4141 0.0120  0.0074  0.0049 46  SER A CB  
346  O  OG  . SER A 46  ? 0.5723 0.5605 0.5556 0.0124  0.0075  0.0047 46  SER A OG  
347  N  N   . GLU A 47  ? 0.4424 0.4302 0.4255 0.0117  0.0068  0.0048 47  GLU A N   
348  C  CA  . GLU A 47  ? 0.4150 0.4022 0.3976 0.0115  0.0063  0.0049 47  GLU A CA  
349  C  C   . GLU A 47  ? 0.4778 0.4655 0.4611 0.0111  0.0062  0.0050 47  GLU A C   
350  O  O   . GLU A 47  ? 0.4287 0.4171 0.4128 0.0111  0.0065  0.0051 47  GLU A O   
351  C  CB  . GLU A 47  ? 0.4548 0.4407 0.4357 0.0122  0.0065  0.0045 47  GLU A CB  
352  N  N   . ASP A 48  ? 0.4559 0.4433 0.4391 0.0108  0.0057  0.0052 48  ASP A N   
353  C  CA  . ASP A 48  ? 0.4379 0.4259 0.4220 0.0103  0.0055  0.0054 48  ASP A CA  
354  C  C   . ASP A 48  ? 0.3932 0.3823 0.3787 0.0097  0.0053  0.0057 48  ASP A C   
355  O  O   . ASP A 48  ? 0.3977 0.3874 0.3839 0.0093  0.0052  0.0059 48  ASP A O   
356  C  CB  . ASP A 48  ? 0.4251 0.4129 0.4088 0.0108  0.0061  0.0052 48  ASP A CB  
357  C  CG  . ASP A 48  ? 0.4826 0.4711 0.4669 0.0111  0.0067  0.0051 48  ASP A CG  
358  O  OD1 . ASP A 48  ? 0.3973 0.3867 0.3828 0.0106  0.0066  0.0053 48  ASP A OD1 
359  O  OD2 . ASP A 48  ? 0.3626 0.3507 0.3463 0.0117  0.0073  0.0049 48  ASP A OD2 
360  N  N   . MET A 49  ? 0.4013 0.3908 0.3871 0.0095  0.0052  0.0058 49  MET A N   
361  C  CA  . MET A 49  ? 0.4181 0.4086 0.4052 0.0088  0.0048  0.0061 49  MET A CA  
362  C  C   . MET A 49  ? 0.3603 0.3507 0.3476 0.0082  0.0041  0.0064 49  MET A C   
363  O  O   . MET A 49  ? 0.3234 0.3146 0.3117 0.0076  0.0037  0.0067 49  MET A O   
364  C  CB  . MET A 49  ? 0.4249 0.4159 0.4125 0.0089  0.0051  0.0061 49  MET A CB  
365  C  CG  . MET A 49  ? 0.3637 0.3553 0.3519 0.0090  0.0055  0.0060 49  MET A CG  
366  S  SD  . MET A 49  ? 0.5190 0.5116 0.5085 0.0083  0.0052  0.0063 49  MET A SD  
367  C  CE  . MET A 49  ? 0.3175 0.3108 0.3077 0.0083  0.0055  0.0063 49  MET A CE  
368  N  N   . PHE A 50  ? 0.3450 0.3345 0.3313 0.0084  0.0039  0.0063 50  PHE A N   
369  C  CA  . PHE A 50  ? 0.3493 0.3387 0.3357 0.0078  0.0031  0.0066 50  PHE A CA  
370  C  C   . PHE A 50  ? 0.4004 0.3898 0.3872 0.0075  0.0027  0.0068 50  PHE A C   
371  O  O   . PHE A 50  ? 0.4099 0.3996 0.3973 0.0069  0.0021  0.0072 50  PHE A O   
372  C  CB  . PHE A 50  ? 0.3579 0.3462 0.3431 0.0082  0.0030  0.0064 50  PHE A CB  
373  C  CG  . PHE A 50  ? 0.4206 0.4091 0.4059 0.0083  0.0031  0.0063 50  PHE A CG  
374  C  CD1 . PHE A 50  ? 0.3300 0.3190 0.3159 0.0077  0.0026  0.0066 50  PHE A CD1 
375  C  CD2 . PHE A 50  ? 0.4077 0.3960 0.3924 0.0090  0.0038  0.0060 50  PHE A CD2 
376  C  CE1 . PHE A 50  ? 0.3114 0.3005 0.2974 0.0078  0.0028  0.0066 50  PHE A CE1 
377  C  CE2 . PHE A 50  ? 0.4086 0.3971 0.3933 0.0091  0.0040  0.0060 50  PHE A CE2 
378  C  CZ  . PHE A 50  ? 0.3636 0.3525 0.3490 0.0085  0.0035  0.0063 50  PHE A CZ  
379  N  N   . ASN A 51  ? 0.3280 0.3171 0.3143 0.0079  0.0031  0.0067 51  ASN A N   
380  C  CA  . ASN A 51  ? 0.3444 0.3338 0.3312 0.0075  0.0028  0.0069 51  ASN A CA  
381  C  C   . ASN A 51  ? 0.3416 0.3311 0.3283 0.0080  0.0035  0.0067 51  ASN A C   
382  O  O   . ASN A 51  ? 0.3759 0.3648 0.3620 0.0083  0.0036  0.0067 51  ASN A O   
383  C  CB  . ASN A 51  ? 0.4206 0.4092 0.4069 0.0074  0.0022  0.0071 51  ASN A CB  
384  C  CG  . ASN A 51  ? 0.4904 0.4795 0.4776 0.0067  0.0017  0.0076 51  ASN A CG  
385  O  OD1 . ASN A 51  ? 0.4088 0.3988 0.3971 0.0064  0.0018  0.0077 51  ASN A OD1 
386  N  ND2 . ASN A 51  ? 0.4919 0.4805 0.4789 0.0065  0.0010  0.0078 51  ASN A ND2 
387  N  N   . PRO A 52  ? 0.3524 0.3426 0.3398 0.0081  0.0040  0.0066 52  PRO A N   
388  C  CA  . PRO A 52  ? 0.2798 0.2701 0.2672 0.0086  0.0046  0.0064 52  PRO A CA  
389  C  C   . PRO A 52  ? 0.2843 0.2748 0.2720 0.0084  0.0045  0.0066 52  PRO A C   
390  O  O   . PRO A 52  ? 0.2395 0.2305 0.2281 0.0078  0.0041  0.0070 52  PRO A O   
391  C  CB  . PRO A 52  ? 0.2780 0.2691 0.2662 0.0085  0.0049  0.0064 52  PRO A CB  
392  C  CG  . PRO A 52  ? 0.3053 0.2969 0.2941 0.0079  0.0044  0.0066 52  PRO A CG  
393  C  CD  . PRO A 52  ? 0.3101 0.3010 0.2982 0.0078  0.0039  0.0067 52  PRO A CD  
394  N  N   . ASN A 53  ? 0.2046 0.1946 0.1917 0.0089  0.0049  0.0065 53  ASN A N   
395  C  CA  . ASN A 53  ? 0.2108 0.2010 0.1982 0.0088  0.0049  0.0067 53  ASN A CA  
396  C  C   . ASN A 53  ? 0.1744 0.1651 0.1623 0.0091  0.0056  0.0065 53  ASN A C   
397  O  O   . ASN A 53  ? 0.1516 0.1420 0.1389 0.0097  0.0062  0.0062 53  ASN A O   
398  C  CB  . ASN A 53  ? 0.2254 0.2147 0.2118 0.0092  0.0049  0.0066 53  ASN A CB  
399  C  CG  . ASN A 53  ? 0.2867 0.2763 0.2736 0.0090  0.0048  0.0070 53  ASN A CG  
400  O  OD1 . ASN A 53  ? 0.2551 0.2453 0.2427 0.0090  0.0053  0.0070 53  ASN A OD1 
401  N  ND2 . ASN A 53  ? 0.2861 0.2752 0.2727 0.0088  0.0043  0.0072 53  ASN A ND2 
402  N  N   . TYR A 54  ? 0.1517 0.1433 0.1407 0.0087  0.0055  0.0067 54  TYR A N   
403  C  CA  . TYR A 54  ? 0.1527 0.1447 0.1421 0.0089  0.0061  0.0065 54  TYR A CA  
404  C  C   . TYR A 54  ? 0.1247 0.1166 0.1139 0.0093  0.0066  0.0064 54  TYR A C   
405  O  O   . TYR A 54  ? 0.1199 0.1118 0.1090 0.0098  0.0071  0.0062 54  TYR A O   
406  C  CB  . TYR A 54  ? 0.1096 0.1024 0.1000 0.0083  0.0058  0.0067 54  TYR A CB  
407  C  CG  . TYR A 54  ? 0.1426 0.1356 0.1332 0.0080  0.0055  0.0067 54  TYR A CG  
408  C  CD1 . TYR A 54  ? 0.0902 0.0833 0.0808 0.0083  0.0058  0.0065 54  TYR A CD1 
409  C  CD2 . TYR A 54  ? 0.1107 0.1038 0.1016 0.0075  0.0048  0.0069 54  TYR A CD2 
410  C  CE1 . TYR A 54  ? 0.1098 0.1032 0.1006 0.0081  0.0056  0.0065 54  TYR A CE1 
411  C  CE2 . TYR A 54  ? 0.1330 0.1263 0.1241 0.0073  0.0046  0.0069 54  TYR A CE2 
412  C  CZ  . TYR A 54  ? 0.0976 0.0911 0.0886 0.0076  0.0050  0.0067 54  TYR A CZ  
413  O  OH  . TYR A 54  ? 0.1354 0.1290 0.1265 0.0073  0.0047  0.0068 54  TYR A OH  
414  N  N   . GLU A 55  ? 0.1543 0.1462 0.1437 0.0091  0.0063  0.0067 55  GLU A N   
415  C  CA  . GLU A 55  ? 0.2027 0.1944 0.1919 0.0095  0.0068  0.0067 55  GLU A CA  
416  C  C   . GLU A 55  ? 0.1755 0.1665 0.1636 0.0102  0.0073  0.0064 55  GLU A C   
417  O  O   . GLU A 55  ? 0.2212 0.2121 0.2091 0.0107  0.0079  0.0061 55  GLU A O   
418  C  CB  . GLU A 55  ? 0.1963 0.1881 0.1857 0.0092  0.0064  0.0071 55  GLU A CB  
419  C  CG  . GLU A 55  ? 0.1778 0.1704 0.1685 0.0086  0.0061  0.0074 55  GLU A CG  
420  C  CD  . GLU A 55  ? 0.2881 0.2809 0.2791 0.0080  0.0055  0.0075 55  GLU A CD  
421  O  OE1 . GLU A 55  ? 0.2320 0.2244 0.2225 0.0080  0.0052  0.0075 55  GLU A OE1 
422  O  OE2 . GLU A 55  ? 0.3314 0.3250 0.3234 0.0076  0.0053  0.0077 55  GLU A OE2 
423  N  N   . ASP A 56  ? 0.1429 0.1332 0.1301 0.0102  0.0069  0.0063 56  ASP A N   
424  C  CA  . ASP A 56  ? 0.1955 0.1850 0.1815 0.0109  0.0073  0.0060 56  ASP A CA  
425  C  C   . ASP A 56  ? 0.2146 0.2041 0.2005 0.0113  0.0079  0.0056 56  ASP A C   
426  O  O   . ASP A 56  ? 0.1865 0.1756 0.1717 0.0119  0.0084  0.0054 56  ASP A O   
427  C  CB  . ASP A 56  ? 0.1949 0.1836 0.1801 0.0108  0.0068  0.0061 56  ASP A CB  
428  C  CG  . ASP A 56  ? 0.2760 0.2646 0.2613 0.0104  0.0062  0.0065 56  ASP A CG  
429  O  OD1 . ASP A 56  ? 0.3406 0.3285 0.3253 0.0103  0.0056  0.0066 56  ASP A OD1 
430  O  OD2 . ASP A 56  ? 0.2753 0.2644 0.2614 0.0102  0.0063  0.0067 56  ASP A OD2 
431  N  N   . LEU A 57  ? 0.1583 0.1482 0.1447 0.0110  0.0076  0.0056 57  LEU A N   
432  C  CA  . LEU A 57  ? 0.1848 0.1748 0.1711 0.0113  0.0081  0.0054 57  LEU A CA  
433  C  C   . LEU A 57  ? 0.1738 0.1643 0.1609 0.0111  0.0082  0.0053 57  LEU A C   
434  O  O   . LEU A 57  ? 0.1861 0.1765 0.1732 0.0111  0.0082  0.0052 57  LEU A O   
435  C  CB  . LEU A 57  ? 0.1253 0.1156 0.1121 0.0109  0.0076  0.0054 57  LEU A CB  
436  C  CG  . LEU A 57  ? 0.1950 0.1849 0.1812 0.0108  0.0072  0.0055 57  LEU A CG  
437  C  CD1 . LEU A 57  ? 0.2254 0.2157 0.2123 0.0102  0.0068  0.0056 57  LEU A CD1 
438  C  CD2 . LEU A 57  ? 0.2479 0.2369 0.2329 0.0115  0.0076  0.0051 57  LEU A CD2 
439  N  N   . LEU A 58  ? 0.1632 0.1543 0.1511 0.0110  0.0083  0.0055 58  LEU A N   
440  C  CA  . LEU A 58  ? 0.1674 0.1589 0.1560 0.0107  0.0083  0.0055 58  LEU A CA  
441  C  C   . LEU A 58  ? 0.1704 0.1615 0.1587 0.0108  0.0084  0.0054 58  LEU A C   
442  O  O   . LEU A 58  ? 0.1365 0.1278 0.1251 0.0107  0.0085  0.0053 58  LEU A O   
443  C  CB  . LEU A 58  ? 0.1274 0.1195 0.1168 0.0105  0.0084  0.0058 58  LEU A CB  
444  C  CG  . LEU A 58  ? 0.1655 0.1579 0.1555 0.0103  0.0084  0.0058 58  LEU A CG  
445  C  CD1 . LEU A 58  ? 0.1114 0.1039 0.1016 0.0101  0.0083  0.0056 58  LEU A CD1 
446  C  CD2 . LEU A 58  ? 0.1314 0.1244 0.1222 0.0101  0.0084  0.0060 58  LEU A CD2 
447  N  N   . ILE A 59  ? 0.1941 0.1848 0.1817 0.0111  0.0085  0.0055 59  ILE A N   
448  C  CA  . ILE A 59  ? 0.1993 0.1897 0.1866 0.0113  0.0087  0.0055 59  ILE A CA  
449  C  C   . ILE A 59  ? 0.1919 0.1820 0.1787 0.0114  0.0086  0.0052 59  ILE A C   
450  O  O   . ILE A 59  ? 0.2145 0.2045 0.2014 0.0114  0.0087  0.0052 59  ILE A O   
451  C  CB  . ILE A 59  ? 0.1762 0.1662 0.1628 0.0117  0.0088  0.0057 59  ILE A CB  
452  C  CG1 . ILE A 59  ? 0.1901 0.1806 0.1775 0.0116  0.0090  0.0060 59  ILE A CG1 
453  C  CG2 . ILE A 59  ? 0.2167 0.2061 0.2026 0.0120  0.0089  0.0056 59  ILE A CG2 
454  C  CD1 . ILE A 59  ? 0.1539 0.1443 0.1411 0.0114  0.0085  0.0063 59  ILE A CD1 
455  N  N   . ARG A 60  ? 0.2043 0.1941 0.1907 0.0114  0.0085  0.0051 60  ARG A N   
456  C  CA  . ARG A 60  ? 0.2122 0.2018 0.1983 0.0115  0.0084  0.0049 60  ARG A CA  
457  C  C   . ARG A 60  ? 0.2045 0.1946 0.1914 0.0111  0.0084  0.0048 60  ARG A C   
458  O  O   . ARG A 60  ? 0.2211 0.2111 0.2078 0.0112  0.0084  0.0047 60  ARG A O   
459  C  CB  . ARG A 60  ? 0.2346 0.2237 0.2200 0.0116  0.0083  0.0048 60  ARG A CB  
460  C  CG  . ARG A 60  ? 0.2949 0.2833 0.2792 0.0120  0.0083  0.0048 60  ARG A CG  
461  C  CD  . ARG A 60  ? 0.3373 0.3254 0.3213 0.0121  0.0082  0.0048 60  ARG A CD  
462  N  NE  . ARG A 60  ? 0.4433 0.4316 0.4274 0.0120  0.0081  0.0047 60  ARG A NE  
463  C  CZ  . ARG A 60  ? 0.5520 0.5399 0.5356 0.0121  0.0080  0.0046 60  ARG A CZ  
464  N  NH1 . ARG A 60  ? 0.5528 0.5400 0.5355 0.0124  0.0079  0.0047 60  ARG A NH1 
465  N  NH2 . ARG A 60  ? 0.5798 0.5679 0.5636 0.0120  0.0079  0.0045 60  ARG A NH2 
466  N  N   . LYS A 61  ? 0.1586 0.1492 0.1463 0.0109  0.0084  0.0049 61  LYS A N   
467  C  CA  . LYS A 61  ? 0.2019 0.1928 0.1901 0.0106  0.0083  0.0048 61  LYS A CA  
468  C  C   . LYS A 61  ? 0.1894 0.1804 0.1779 0.0105  0.0084  0.0048 61  LYS A C   
469  O  O   . LYS A 61  ? 0.1712 0.1623 0.1598 0.0105  0.0085  0.0049 61  LYS A O   
470  C  CB  . LYS A 61  ? 0.2229 0.2142 0.2116 0.0104  0.0082  0.0049 61  LYS A CB  
471  C  CG  . LYS A 61  ? 0.2207 0.2120 0.2091 0.0105  0.0081  0.0049 61  LYS A CG  
472  C  CD  . LYS A 61  ? 0.1982 0.1892 0.1863 0.0106  0.0081  0.0048 61  LYS A CD  
473  C  CE  . LYS A 61  ? 0.2541 0.2451 0.2419 0.0107  0.0080  0.0048 61  LYS A CE  
474  N  NZ  . LYS A 61  ? 0.2901 0.2807 0.2774 0.0109  0.0080  0.0046 61  LYS A NZ  
475  N  N   . SER A 62  ? 0.2179 0.2090 0.2066 0.0104  0.0084  0.0047 62  SER A N   
476  C  CA  . SER A 62  ? 0.2053 0.1965 0.1944 0.0103  0.0085  0.0047 62  SER A CA  
477  C  C   . SER A 62  ? 0.1680 0.1594 0.1575 0.0101  0.0085  0.0047 62  SER A C   
478  O  O   . SER A 62  ? 0.1291 0.1207 0.1187 0.0100  0.0084  0.0047 62  SER A O   
479  C  CB  . SER A 62  ? 0.2365 0.2274 0.2252 0.0104  0.0086  0.0046 62  SER A CB  
480  O  OG  . SER A 62  ? 0.3420 0.3327 0.3303 0.0106  0.0087  0.0046 62  SER A OG  
481  N  N   . ASN A 63  ? 0.1862 0.1776 0.1759 0.0100  0.0085  0.0047 63  ASN A N   
482  C  CA  . ASN A 63  ? 0.1613 0.1529 0.1513 0.0098  0.0085  0.0047 63  ASN A CA  
483  C  C   . ASN A 63  ? 0.2278 0.2194 0.2178 0.0098  0.0085  0.0047 63  ASN A C   
484  O  O   . ASN A 63  ? 0.1861 0.1777 0.1762 0.0097  0.0084  0.0047 63  ASN A O   
485  C  CB  . ASN A 63  ? 0.1666 0.1579 0.1566 0.0098  0.0087  0.0047 63  ASN A CB  
486  C  CG  . ASN A 63  ? 0.2032 0.1947 0.1935 0.0097  0.0087  0.0048 63  ASN A CG  
487  O  OD1 . ASN A 63  ? 0.2060 0.1977 0.1964 0.0097  0.0087  0.0050 63  ASN A OD1 
488  N  ND2 . ASN A 63  ? 0.1506 0.1418 0.1408 0.0097  0.0089  0.0048 63  ASN A ND2 
489  N  N   . HIS A 64  ? 0.1745 0.1659 0.1642 0.0099  0.0085  0.0045 64  HIS A N   
490  C  CA  . HIS A 64  ? 0.1891 0.1805 0.1787 0.0100  0.0085  0.0045 64  HIS A CA  
491  C  C   . HIS A 64  ? 0.1695 0.1609 0.1590 0.0100  0.0084  0.0045 64  HIS A C   
492  O  O   . HIS A 64  ? 0.1831 0.1745 0.1726 0.0101  0.0084  0.0045 64  HIS A O   
493  C  CB  . HIS A 64  ? 0.1994 0.1904 0.1887 0.0101  0.0086  0.0044 64  HIS A CB  
494  C  CG  . HIS A 64  ? 0.1691 0.1601 0.1581 0.0103  0.0086  0.0043 64  HIS A CG  
495  N  ND1 . HIS A 64  ? 0.1983 0.1891 0.1871 0.0103  0.0087  0.0043 64  HIS A ND1 
496  C  CD2 . HIS A 64  ? 0.1837 0.1746 0.1724 0.0104  0.0085  0.0043 64  HIS A CD2 
497  C  CE1 . HIS A 64  ? 0.1839 0.1745 0.1723 0.0105  0.0087  0.0043 64  HIS A CE1 
498  N  NE2 . HIS A 64  ? 0.1851 0.1758 0.1734 0.0106  0.0086  0.0043 64  HIS A NE2 
499  N  N   . ASN A 65  ? 0.1473 0.1388 0.1367 0.0101  0.0083  0.0046 65  ASN A N   
500  C  CA  . ASN A 65  ? 0.1699 0.1615 0.1593 0.0101  0.0082  0.0046 65  ASN A CA  
501  C  C   . ASN A 65  ? 0.1690 0.1609 0.1587 0.0100  0.0082  0.0047 65  ASN A C   
502  O  O   . ASN A 65  ? 0.1479 0.1399 0.1376 0.0100  0.0081  0.0048 65  ASN A O   
503  C  CB  . ASN A 65  ? 0.1665 0.1579 0.1554 0.0103  0.0082  0.0046 65  ASN A CB  
504  C  CG  . ASN A 65  ? 0.2305 0.2216 0.2190 0.0104  0.0083  0.0045 65  ASN A CG  
505  O  OD1 . ASN A 65  ? 0.2263 0.2172 0.2146 0.0105  0.0083  0.0045 65  ASN A OD1 
506  N  ND2 . ASN A 65  ? 0.1666 0.1575 0.1548 0.0106  0.0083  0.0044 65  ASN A ND2 
507  N  N   . PHE A 66  ? 0.1736 0.1657 0.1637 0.0098  0.0082  0.0048 66  PHE A N   
508  C  CA  . PHE A 66  ? 0.2031 0.1955 0.1935 0.0097  0.0081  0.0050 66  PHE A CA  
509  C  C   . PHE A 66  ? 0.1856 0.1779 0.1761 0.0097  0.0082  0.0050 66  PHE A C   
510  O  O   . PHE A 66  ? 0.2149 0.2070 0.2054 0.0096  0.0083  0.0050 66  PHE A O   
511  C  CB  . PHE A 66  ? 0.1809 0.1734 0.1715 0.0096  0.0081  0.0051 66  PHE A CB  
512  C  CG  . PHE A 66  ? 0.1477 0.1402 0.1382 0.0097  0.0081  0.0051 66  PHE A CG  
513  C  CD1 . PHE A 66  ? 0.1407 0.1334 0.1314 0.0097  0.0080  0.0052 66  PHE A CD1 
514  C  CD2 . PHE A 66  ? 0.1389 0.1312 0.1293 0.0097  0.0082  0.0050 66  PHE A CD2 
515  C  CE1 . PHE A 66  ? 0.1435 0.1363 0.1341 0.0098  0.0080  0.0053 66  PHE A CE1 
516  C  CE2 . PHE A 66  ? 0.1519 0.1442 0.1422 0.0098  0.0082  0.0051 66  PHE A CE2 
517  C  CZ  . PHE A 66  ? 0.0923 0.0848 0.0826 0.0098  0.0081  0.0052 66  PHE A CZ  
518  N  N   . LEU A 67  ? 0.1394 0.1318 0.1299 0.0097  0.0082  0.0051 67  LEU A N   
519  C  CA  . LEU A 67  ? 0.1725 0.1650 0.1631 0.0098  0.0083  0.0052 67  LEU A CA  
520  C  C   . LEU A 67  ? 0.1883 0.1810 0.1793 0.0097  0.0083  0.0054 67  LEU A C   
521  O  O   . LEU A 67  ? 0.1486 0.1418 0.1399 0.0097  0.0082  0.0056 67  LEU A O   
522  C  CB  . LEU A 67  ? 0.1899 0.1824 0.1804 0.0099  0.0083  0.0052 67  LEU A CB  
523  C  CG  . LEU A 67  ? 0.1611 0.1534 0.1514 0.0100  0.0083  0.0050 67  LEU A CG  
524  C  CD1 . LEU A 67  ? 0.2025 0.1944 0.1926 0.0100  0.0084  0.0049 67  LEU A CD1 
525  C  CD2 . LEU A 67  ? 0.2447 0.2369 0.2347 0.0101  0.0082  0.0049 67  LEU A CD2 
526  N  N   . VAL A 68  ? 0.1400 0.1326 0.1310 0.0096  0.0084  0.0055 68  VAL A N   
527  C  CA  . VAL A 68  ? 0.1423 0.1350 0.1335 0.0096  0.0084  0.0057 68  VAL A CA  
528  C  C   . VAL A 68  ? 0.1864 0.1790 0.1775 0.0097  0.0086  0.0059 68  VAL A C   
529  O  O   . VAL A 68  ? 0.1694 0.1615 0.1602 0.0097  0.0087  0.0058 68  VAL A O   
530  C  CB  . VAL A 68  ? 0.1950 0.1875 0.1862 0.0095  0.0085  0.0057 68  VAL A CB  
531  C  CG1 . VAL A 68  ? 0.1451 0.1379 0.1366 0.0088  0.0079  0.0061 68  VAL A CG1 
532  C  CG2 . VAL A 68  ? 0.1499 0.1426 0.1412 0.0094  0.0084  0.0056 68  VAL A CG2 
533  N  N   . GLN A 69  ? 0.1727 0.1658 0.1642 0.0093  0.0082  0.0062 69  GLN A N   
534  C  CA  . GLN A 69  ? 0.2610 0.2542 0.2525 0.0089  0.0079  0.0064 69  GLN A CA  
535  C  C   . GLN A 69  ? 0.2486 0.2421 0.2404 0.0079  0.0072  0.0068 69  GLN A C   
536  O  O   . GLN A 69  ? 0.1681 0.1621 0.1603 0.0075  0.0067  0.0069 69  GLN A O   
537  C  CB  . GLN A 69  ? 0.2201 0.2136 0.2118 0.0092  0.0080  0.0065 69  GLN A CB  
538  C  CG  . GLN A 69  ? 0.3632 0.3562 0.3545 0.0100  0.0087  0.0063 69  GLN A CG  
539  C  CD  . GLN A 69  ? 0.3367 0.3301 0.3281 0.0102  0.0087  0.0063 69  GLN A CD  
540  O  OE1 . GLN A 69  ? 0.3593 0.3532 0.3511 0.0101  0.0086  0.0066 69  GLN A OE1 
541  N  NE2 . GLN A 69  ? 0.4409 0.4341 0.4321 0.0102  0.0086  0.0060 69  GLN A NE2 
542  N  N   . ALA A 70  ? 0.2602 0.2533 0.2517 0.0075  0.0070  0.0069 70  ALA A N   
543  C  CA  . ALA A 70  ? 0.3448 0.3382 0.3365 0.0065  0.0062  0.0073 70  ALA A CA  
544  C  C   . ALA A 70  ? 0.4179 0.4113 0.4094 0.0062  0.0060  0.0075 70  ALA A C   
545  O  O   . ALA A 70  ? 0.3399 0.3327 0.3309 0.0063  0.0062  0.0075 70  ALA A O   
546  C  CB  . ALA A 70  ? 0.2754 0.2682 0.2666 0.0061  0.0061  0.0073 70  ALA A CB  
547  N  N   . GLY A 71  ? 0.4374 0.4315 0.4293 0.0060  0.0057  0.0078 71  GLY A N   
548  C  CA  . GLY A 71  ? 0.4084 0.4026 0.4003 0.0058  0.0056  0.0081 71  GLY A CA  
549  C  C   . GLY A 71  ? 0.4318 0.4258 0.4236 0.0068  0.0063  0.0078 71  GLY A C   
550  O  O   . GLY A 71  ? 0.5660 0.5604 0.5582 0.0074  0.0067  0.0077 71  GLY A O   
551  N  N   . ASN A 72  ? 0.4667 0.4600 0.4580 0.0070  0.0066  0.0078 72  ASN A N   
552  C  CA  . ASN A 72  ? 0.5570 0.5500 0.5481 0.0079  0.0074  0.0074 72  ASN A CA  
553  C  C   . ASN A 72  ? 0.5660 0.5581 0.5565 0.0083  0.0078  0.0071 72  ASN A C   
554  O  O   . ASN A 72  ? 0.5769 0.5686 0.5672 0.0091  0.0084  0.0068 72  ASN A O   
555  C  CB  . ASN A 72  ? 0.7002 0.6932 0.6912 0.0080  0.0074  0.0077 72  ASN A CB  
556  C  CG  . ASN A 72  ? 0.7481 0.7418 0.7396 0.0084  0.0076  0.0078 72  ASN A CG  
557  O  OD1 . ASN A 72  ? 0.6166 0.6101 0.6080 0.0091  0.0082  0.0076 72  ASN A OD1 
558  N  ND2 . ASN A 72  ? 0.7918 0.7862 0.7838 0.0079  0.0071  0.0080 72  ASN A ND2 
559  N  N   . VAL A 73  ? 0.4747 0.4666 0.4650 0.0077  0.0074  0.0071 73  VAL A N   
560  C  CA  . VAL A 73  ? 0.4343 0.4254 0.4242 0.0081  0.0078  0.0068 73  VAL A CA  
561  C  C   . VAL A 73  ? 0.3937 0.3850 0.3839 0.0088  0.0083  0.0065 73  VAL A C   
562  O  O   . VAL A 73  ? 0.2900 0.2818 0.2805 0.0086  0.0080  0.0065 73  VAL A O   
563  C  CB  . VAL A 73  ? 0.4591 0.4501 0.4488 0.0072  0.0073  0.0069 73  VAL A CB  
564  C  CG1 . VAL A 73  ? 0.3810 0.3713 0.3703 0.0077  0.0077  0.0066 73  VAL A CG1 
565  C  CG2 . VAL A 73  ? 0.5431 0.5337 0.5324 0.0065  0.0069  0.0073 73  VAL A CG2 
566  N  N   . GLN A 74  ? 0.4076 0.3984 0.3974 0.0096  0.0090  0.0061 74  GLN A N   
567  C  CA  . GLN A 74  ? 0.2874 0.2783 0.2773 0.0100  0.0091  0.0058 74  GLN A CA  
568  C  C   . GLN A 74  ? 0.2424 0.2328 0.2320 0.0099  0.0092  0.0056 74  GLN A C   
569  O  O   . GLN A 74  ? 0.3042 0.2941 0.2935 0.0099  0.0093  0.0056 74  GLN A O   
570  C  CB  . GLN A 74  ? 0.2975 0.2885 0.2874 0.0100  0.0091  0.0056 74  GLN A CB  
571  C  CG  . GLN A 74  ? 0.3478 0.3391 0.3378 0.0100  0.0089  0.0054 74  GLN A CG  
572  C  CD  . GLN A 74  ? 0.3113 0.3031 0.3017 0.0100  0.0088  0.0056 74  GLN A CD  
573  O  OE1 . GLN A 74  ? 0.3073 0.2994 0.2979 0.0101  0.0089  0.0058 74  GLN A OE1 
574  N  NE2 . GLN A 74  ? 0.2662 0.2583 0.2567 0.0099  0.0086  0.0055 74  GLN A NE2 
575  N  N   . LEU A 75  ? 0.2041 0.1948 0.1940 0.0097  0.0090  0.0056 75  LEU A N   
576  C  CA  . LEU A 75  ? 0.1885 0.1789 0.1783 0.0096  0.0090  0.0055 75  LEU A CA  
577  C  C   . LEU A 75  ? 0.1761 0.1667 0.1660 0.0096  0.0089  0.0053 75  LEU A C   
578  O  O   . LEU A 75  ? 0.2309 0.2219 0.2210 0.0096  0.0088  0.0052 75  LEU A O   
579  C  CB  . LEU A 75  ? 0.2097 0.2004 0.1997 0.0096  0.0090  0.0056 75  LEU A CB  
580  C  CG  . LEU A 75  ? 0.1987 0.1898 0.1890 0.0087  0.0083  0.0060 75  LEU A CG  
581  C  CD1 . LEU A 75  ? 0.1571 0.1485 0.1477 0.0081  0.0078  0.0061 75  LEU A CD1 
582  C  CD2 . LEU A 75  ? 0.2272 0.2176 0.2170 0.0084  0.0083  0.0061 75  LEU A CD2 
583  N  N   . ARG A 76  ? 0.1832 0.1734 0.1728 0.0096  0.0090  0.0052 76  ARG A N   
584  C  CA  . ARG A 76  ? 0.1760 0.1662 0.1657 0.0096  0.0090  0.0050 76  ARG A CA  
585  C  C   . ARG A 76  ? 0.1839 0.1744 0.1738 0.0095  0.0089  0.0050 76  ARG A C   
586  O  O   . ARG A 76  ? 0.1528 0.1431 0.1427 0.0094  0.0090  0.0050 76  ARG A O   
587  C  CB  . ARG A 76  ? 0.1725 0.1622 0.1619 0.0096  0.0092  0.0049 76  ARG A CB  
588  C  CG  . ARG A 76  ? 0.2168 0.2066 0.2062 0.0096  0.0091  0.0047 76  ARG A CG  
589  C  CD  . ARG A 76  ? 0.2026 0.1918 0.1917 0.0097  0.0093  0.0046 76  ARG A CD  
590  N  NE  . ARG A 76  ? 0.1811 0.1702 0.1700 0.0097  0.0094  0.0047 76  ARG A NE  
591  C  CZ  . ARG A 76  ? 0.2040 0.1933 0.1930 0.0098  0.0094  0.0046 76  ARG A CZ  
592  N  NH1 . ARG A 76  ? 0.1593 0.1489 0.1484 0.0099  0.0092  0.0045 76  ARG A NH1 
593  N  NH2 . ARG A 76  ? 0.2209 0.2100 0.2097 0.0099  0.0095  0.0046 76  ARG A NH2 
594  N  N   . VAL A 77  ? 0.2340 0.2248 0.2241 0.0095  0.0088  0.0049 77  VAL A N   
595  C  CA  . VAL A 77  ? 0.1388 0.1300 0.1292 0.0095  0.0087  0.0050 77  VAL A CA  
596  C  C   . VAL A 77  ? 0.1530 0.1440 0.1433 0.0095  0.0088  0.0049 77  VAL A C   
597  O  O   . VAL A 77  ? 0.2176 0.2085 0.2078 0.0096  0.0088  0.0047 77  VAL A O   
598  C  CB  . VAL A 77  ? 0.1571 0.1487 0.1476 0.0095  0.0086  0.0050 77  VAL A CB  
599  C  CG1 . VAL A 77  ? 0.1112 0.1030 0.1019 0.0095  0.0085  0.0050 77  VAL A CG1 
600  C  CG2 . VAL A 77  ? 0.1962 0.1880 0.1868 0.0095  0.0085  0.0051 77  VAL A CG2 
601  N  N   . ILE A 78  ? 0.1748 0.1657 0.1651 0.0094  0.0089  0.0049 78  ILE A N   
602  C  CA  . ILE A 78  ? 0.1488 0.1396 0.1391 0.0095  0.0090  0.0049 78  ILE A CA  
603  C  C   . ILE A 78  ? 0.1887 0.1797 0.1792 0.0095  0.0090  0.0050 78  ILE A C   
604  O  O   . ILE A 78  ? 0.1914 0.1824 0.1820 0.0096  0.0092  0.0050 78  ILE A O   
605  C  CB  . ILE A 78  ? 0.1450 0.1353 0.1351 0.0095  0.0092  0.0049 78  ILE A CB  
606  C  CG1 . ILE A 78  ? 0.2221 0.2123 0.2122 0.0094  0.0093  0.0051 78  ILE A CG1 
607  C  CG2 . ILE A 78  ? 0.1424 0.1323 0.1322 0.0095  0.0093  0.0048 78  ILE A CG2 
608  C  CD1 . ILE A 78  ? 0.1888 0.1784 0.1787 0.0094  0.0095  0.0051 78  ILE A CD1 
609  N  N   . GLY A 79  ? 0.1493 0.1407 0.1401 0.0095  0.0089  0.0051 79  GLY A N   
610  C  CA  . GLY A 79  ? 0.1659 0.1576 0.1569 0.0095  0.0089  0.0052 79  GLY A CA  
611  C  C   . GLY A 79  ? 0.1569 0.1489 0.1480 0.0095  0.0087  0.0053 79  GLY A C   
612  O  O   . GLY A 79  ? 0.1593 0.1514 0.1505 0.0094  0.0087  0.0053 79  GLY A O   
613  N  N   . HIS A 80  ? 0.1028 0.0951 0.0941 0.0095  0.0087  0.0054 80  HIS A N   
614  C  CA  . HIS A 80  ? 0.1648 0.1575 0.1563 0.0095  0.0086  0.0055 80  HIS A CA  
615  C  C   . HIS A 80  ? 0.1632 0.1561 0.1549 0.0096  0.0087  0.0057 80  HIS A C   
616  O  O   . HIS A 80  ? 0.1455 0.1383 0.1370 0.0097  0.0088  0.0057 80  HIS A O   
617  C  CB  . HIS A 80  ? 0.1012 0.0937 0.0923 0.0096  0.0085  0.0054 80  HIS A CB  
618  C  CG  . HIS A 80  ? 0.1424 0.1347 0.1331 0.0097  0.0085  0.0053 80  HIS A CG  
619  N  ND1 . HIS A 80  ? 0.1614 0.1535 0.1519 0.0098  0.0086  0.0052 80  HIS A ND1 
620  C  CD2 . HIS A 80  ? 0.1556 0.1480 0.1462 0.0099  0.0085  0.0054 80  HIS A CD2 
621  C  CE1 . HIS A 80  ? 0.1799 0.1718 0.1701 0.0100  0.0086  0.0052 80  HIS A CE1 
622  N  NE2 . HIS A 80  ? 0.1645 0.1566 0.1547 0.0101  0.0086  0.0053 80  HIS A NE2 
623  N  N   . SER A 81  ? 0.1604 0.1537 0.1525 0.0095  0.0086  0.0059 81  SER A N   
624  C  CA  . SER A 81  ? 0.1254 0.1190 0.1177 0.0096  0.0087  0.0062 81  SER A CA  
625  C  C   . SER A 81  ? 0.1588 0.1528 0.1514 0.0093  0.0083  0.0063 81  SER A C   
626  O  O   . SER A 81  ? 0.0992 0.0933 0.0919 0.0091  0.0081  0.0063 81  SER A O   
627  C  CB  . SER A 81  ? 0.0998 0.0937 0.0927 0.0096  0.0088  0.0064 81  SER A CB  
628  O  OG  . SER A 81  ? 0.1646 0.1585 0.1577 0.0094  0.0088  0.0064 81  SER A OG  
629  N  N   . MET A 82  ? 0.0875 0.0818 0.0804 0.0090  0.0080  0.0066 82  MET A N   
630  C  CA  . MET A 82  ? 0.1182 0.1128 0.1114 0.0085  0.0074  0.0067 82  MET A CA  
631  C  C   . MET A 82  ? 0.1695 0.1646 0.1634 0.0080  0.0070  0.0071 82  MET A C   
632  O  O   . MET A 82  ? 0.1480 0.1431 0.1420 0.0081  0.0072  0.0072 82  MET A O   
633  C  CB  . MET A 82  ? 0.1483 0.1427 0.1411 0.0086  0.0072  0.0067 82  MET A CB  
634  C  CG  . MET A 82  ? 0.1374 0.1320 0.1303 0.0081  0.0066  0.0069 82  MET A CG  
635  S  SD  . MET A 82  ? 0.1383 0.1324 0.1305 0.0083  0.0065  0.0068 82  MET A SD  
636  C  CE  . MET A 82  ? 0.1900 0.1838 0.1819 0.0085  0.0067  0.0069 82  MET A CE  
637  N  N   . GLN A 83  ? 0.0992 0.0948 0.0936 0.0075  0.0065  0.0072 83  GLN A N   
638  C  CA  . GLN A 83  ? 0.1072 0.1032 0.1022 0.0070  0.0061  0.0075 83  GLN A CA  
639  C  C   . GLN A 83  ? 0.0779 0.0742 0.0731 0.0064  0.0055  0.0077 83  GLN A C   
640  O  O   . GLN A 83  ? 0.0627 0.0591 0.0580 0.0062  0.0053  0.0076 83  GLN A O   
641  C  CB  . GLN A 83  ? 0.0762 0.0723 0.0714 0.0068  0.0062  0.0075 83  GLN A CB  
642  C  CG  . GLN A 83  ? 0.0628 0.0593 0.0587 0.0062  0.0057  0.0079 83  GLN A CG  
643  C  CD  . GLN A 83  ? 0.1445 0.1410 0.1405 0.0061  0.0058  0.0079 83  GLN A CD  
644  O  OE1 . GLN A 83  ? 0.1370 0.1331 0.1325 0.0063  0.0060  0.0077 83  GLN A OE1 
645  N  NE2 . GLN A 83  ? 0.1397 0.1365 0.1361 0.0059  0.0057  0.0082 83  GLN A NE2 
646  N  N   . ASN A 84  ? 0.1230 0.1194 0.1184 0.0062  0.0052  0.0079 84  ASN A N   
647  C  CA  . ASN A 84  ? 0.0814 0.0779 0.0769 0.0058  0.0047  0.0080 84  ASN A CA  
648  C  C   . ASN A 84  ? 0.0775 0.0737 0.0725 0.0059  0.0047  0.0078 84  ASN A C   
649  O  O   . ASN A 84  ? 0.0827 0.0785 0.0771 0.0064  0.0050  0.0076 84  ASN A O   
650  C  CB  . ASN A 84  ? 0.1160 0.1131 0.1122 0.0052  0.0043  0.0082 84  ASN A CB  
651  C  CG  . ASN A 84  ? 0.1211 0.1185 0.1178 0.0051  0.0043  0.0084 84  ASN A CG  
652  O  OD1 . ASN A 84  ? 0.1628 0.1601 0.1596 0.0051  0.0042  0.0086 84  ASN A OD1 
653  N  ND2 . ASN A 84  ? 0.1111 0.1087 0.1081 0.0050  0.0043  0.0085 84  ASN A ND2 
654  N  N   . CYS A 85  ? 0.0671 0.0637 0.0624 0.0056  0.0044  0.0078 85  CYS A N   
655  C  CA  . CYS A 85  ? 0.0610 0.0573 0.0558 0.0058  0.0044  0.0076 85  CYS A CA  
656  C  C   . CYS A 85  ? 0.0730 0.0692 0.0676 0.0060  0.0048  0.0074 85  CYS A C   
657  O  O   . CYS A 85  ? 0.0869 0.0831 0.0814 0.0060  0.0047  0.0073 85  CYS A O   
658  C  CB  . CYS A 85  ? 0.0712 0.0677 0.0662 0.0053  0.0039  0.0077 85  CYS A CB  
659  S  SG  . CYS A 85  ? 0.0681 0.0645 0.0632 0.0050  0.0034  0.0079 85  CYS A SG  
660  N  N   . VAL A 86  ? 0.0562 0.0524 0.0509 0.0062  0.0051  0.0073 86  VAL A N   
661  C  CA  . VAL A 86  ? 0.0603 0.0563 0.0549 0.0064  0.0054  0.0072 86  VAL A CA  
662  C  C   . VAL A 86  ? 0.1037 0.0993 0.0978 0.0071  0.0060  0.0069 86  VAL A C   
663  O  O   . VAL A 86  ? 0.0729 0.0683 0.0669 0.0073  0.0062  0.0070 86  VAL A O   
664  C  CB  . VAL A 86  ? 0.0782 0.0745 0.0732 0.0060  0.0051  0.0074 86  VAL A CB  
665  C  CG1 . VAL A 86  ? 0.1258 0.1218 0.1205 0.0063  0.0056  0.0072 86  VAL A CG1 
666  C  CG2 . VAL A 86  ? 0.0368 0.0335 0.0321 0.0054  0.0046  0.0075 86  VAL A CG2 
667  N  N   . LEU A 87  ? 0.0538 0.0491 0.0475 0.0075  0.0063  0.0067 87  LEU A N   
668  C  CA  . LEU A 87  ? 0.0955 0.0903 0.0887 0.0081  0.0070  0.0065 87  LEU A CA  
669  C  C   . LEU A 87  ? 0.1079 0.1026 0.1012 0.0080  0.0070  0.0065 87  LEU A C   
670  O  O   . LEU A 87  ? 0.0609 0.0558 0.0544 0.0076  0.0067  0.0065 87  LEU A O   
671  C  CB  . LEU A 87  ? 0.1052 0.0997 0.0979 0.0085  0.0072  0.0062 87  LEU A CB  
672  C  CG  . LEU A 87  ? 0.1782 0.1721 0.1702 0.0093  0.0079  0.0059 87  LEU A CG  
673  C  CD1 . LEU A 87  ? 0.1605 0.1542 0.1522 0.0095  0.0080  0.0059 87  LEU A CD1 
674  C  CD2 . LEU A 87  ? 0.1018 0.0955 0.0935 0.0095  0.0080  0.0058 87  LEU A CD2 
675  N  N   . LYS A 88  ? 0.0870 0.0814 0.0801 0.0084  0.0075  0.0064 88  LYS A N   
676  C  CA  . LYS A 88  ? 0.1362 0.1303 0.1293 0.0083  0.0076  0.0064 88  LYS A CA  
677  C  C   . LYS A 88  ? 0.1542 0.1477 0.1467 0.0090  0.0083  0.0061 88  LYS A C   
678  O  O   . LYS A 88  ? 0.0783 0.0717 0.0706 0.0093  0.0085  0.0060 88  LYS A O   
679  C  CB  . LYS A 88  ? 0.1189 0.1131 0.1122 0.0081  0.0076  0.0065 88  LYS A CB  
680  C  CG  . LYS A 88  ? 0.1685 0.1632 0.1624 0.0074  0.0069  0.0068 88  LYS A CG  
681  C  CD  . LYS A 88  ? 0.1973 0.1923 0.1915 0.0073  0.0069  0.0070 88  LYS A CD  
682  C  CE  . LYS A 88  ? 0.1647 0.1595 0.1590 0.0074  0.0071  0.0071 88  LYS A CE  
683  N  NZ  . LYS A 88  ? 0.1313 0.1263 0.1259 0.0076  0.0073  0.0072 88  LYS A NZ  
684  N  N   . LEU A 89  ? 0.1040 0.0973 0.0963 0.0091  0.0083  0.0060 89  LEU A N   
685  C  CA  . LEU A 89  ? 0.0971 0.0899 0.0889 0.0093  0.0085  0.0057 89  LEU A CA  
686  C  C   . LEU A 89  ? 0.1225 0.1148 0.1141 0.0092  0.0087  0.0057 89  LEU A C   
687  O  O   . LEU A 89  ? 0.0897 0.0820 0.0814 0.0091  0.0086  0.0058 89  LEU A O   
688  C  CB  . LEU A 89  ? 0.0684 0.0612 0.0601 0.0093  0.0084  0.0056 89  LEU A CB  
689  C  CG  . LEU A 89  ? 0.1111 0.1043 0.1029 0.0093  0.0082  0.0057 89  LEU A CG  
690  C  CD1 . LEU A 89  ? 0.1353 0.1285 0.1270 0.0094  0.0082  0.0056 89  LEU A CD1 
691  C  CD2 . LEU A 89  ? 0.0738 0.0667 0.0653 0.0094  0.0082  0.0055 89  LEU A CD2 
692  N  N   . LYS A 90  ? 0.0962 0.0883 0.0876 0.0093  0.0088  0.0056 90  LYS A N   
693  C  CA  . LYS A 90  ? 0.1116 0.1031 0.1028 0.0093  0.0089  0.0056 90  LYS A CA  
694  C  C   . LYS A 90  ? 0.0917 0.0828 0.0825 0.0093  0.0090  0.0054 90  LYS A C   
695  O  O   . LYS A 90  ? 0.1062 0.0973 0.0968 0.0093  0.0089  0.0053 90  LYS A O   
696  C  CB  . LYS A 90  ? 0.1206 0.1120 0.1118 0.0093  0.0091  0.0055 90  LYS A CB  
697  C  CG  . LYS A 90  ? 0.1855 0.1762 0.1763 0.0093  0.0093  0.0054 90  LYS A CG  
698  C  CD  . LYS A 90  ? 0.2982 0.2887 0.2889 0.0093  0.0095  0.0056 90  LYS A CD  
699  C  CE  . LYS A 90  ? 0.2665 0.2562 0.2567 0.0093  0.0097  0.0055 90  LYS A CE  
700  N  NZ  . LYS A 90  ? 0.2916 0.2806 0.2812 0.0093  0.0098  0.0054 90  LYS A NZ  
701  N  N   . VAL A 91  ? 0.0848 0.0755 0.0753 0.0093  0.0091  0.0055 91  VAL A N   
702  C  CA  . VAL A 91  ? 0.1422 0.1326 0.1324 0.0093  0.0091  0.0054 91  VAL A CA  
703  C  C   . VAL A 91  ? 0.1162 0.1058 0.1059 0.0093  0.0093  0.0053 91  VAL A C   
704  O  O   . VAL A 91  ? 0.1088 0.0981 0.0983 0.0093  0.0095  0.0054 91  VAL A O   
705  C  CB  . VAL A 91  ? 0.1030 0.0935 0.0932 0.0093  0.0091  0.0055 91  VAL A CB  
706  C  CG1 . VAL A 91  ? 0.1023 0.0934 0.0929 0.0093  0.0088  0.0055 91  VAL A CG1 
707  C  CG2 . VAL A 91  ? 0.1067 0.0972 0.0969 0.0087  0.0087  0.0058 91  VAL A CG2 
708  N  N   . ASP A 92  ? 0.1363 0.1255 0.1256 0.0094  0.0094  0.0052 92  ASP A N   
709  C  CA  . ASP A 92  ? 0.1739 0.1624 0.1627 0.0094  0.0096  0.0051 92  ASP A CA  
710  C  C   . ASP A 92  ? 0.1829 0.1705 0.1711 0.0094  0.0099  0.0052 92  ASP A C   
711  O  O   . ASP A 92  ? 0.1465 0.1333 0.1341 0.0094  0.0101  0.0051 92  ASP A O   
712  C  CB  . ASP A 92  ? 0.1972 0.1855 0.1859 0.0094  0.0097  0.0050 92  ASP A CB  
713  C  CG  . ASP A 92  ? 0.1887 0.1769 0.1772 0.0095  0.0097  0.0050 92  ASP A CG  
714  O  OD1 . ASP A 92  ? 0.2342 0.2225 0.2227 0.0095  0.0096  0.0051 92  ASP A OD1 
715  O  OD2 . ASP A 92  ? 0.3114 0.2994 0.2998 0.0096  0.0097  0.0049 92  ASP A OD2 
716  N  N   . THR A 93  ? 0.1463 0.1342 0.1346 0.0093  0.0097  0.0054 93  THR A N   
717  C  CA  . THR A 93  ? 0.1416 0.1292 0.1296 0.0085  0.0092  0.0056 93  THR A CA  
718  C  C   . THR A 93  ? 0.1932 0.1814 0.1816 0.0078  0.0085  0.0059 93  THR A C   
719  O  O   . THR A 93  ? 0.1609 0.1499 0.1499 0.0077  0.0083  0.0060 93  THR A O   
720  C  CB  . THR A 93  ? 0.1834 0.1711 0.1713 0.0083  0.0090  0.0057 93  THR A CB  
721  O  OG1 . THR A 93  ? 0.1781 0.1652 0.1656 0.0091  0.0096  0.0054 93  THR A OG1 
722  C  CG2 . THR A 93  ? 0.1812 0.1686 0.1686 0.0074  0.0084  0.0060 93  THR A CG2 
723  N  N   . ALA A 94  ? 0.1486 0.1363 0.1366 0.0072  0.0083  0.0060 94  ALA A N   
724  C  CA  . ALA A 94  ? 0.1289 0.1170 0.1170 0.0064  0.0077  0.0063 94  ALA A CA  
725  C  C   . ALA A 94  ? 0.1171 0.1057 0.1054 0.0056  0.0070  0.0066 94  ALA A C   
726  O  O   . ALA A 94  ? 0.1330 0.1212 0.1208 0.0054  0.0069  0.0067 94  ALA A O   
727  C  CB  . ALA A 94  ? 0.1399 0.1273 0.1274 0.0060  0.0077  0.0064 94  ALA A CB  
728  N  N   . ASN A 95  ? 0.0977 0.0872 0.0866 0.0052  0.0065  0.0069 95  ASN A N   
729  C  CA  . ASN A 95  ? 0.1096 0.0996 0.0986 0.0045  0.0058  0.0072 95  ASN A CA  
730  C  C   . ASN A 95  ? 0.1177 0.1072 0.1061 0.0036  0.0054  0.0074 95  ASN A C   
731  O  O   . ASN A 95  ? 0.0710 0.0604 0.0592 0.0032  0.0051  0.0076 95  ASN A O   
732  C  CB  . ASN A 95  ? 0.1077 0.0986 0.0974 0.0042  0.0054  0.0074 95  ASN A CB  
733  C  CG  . ASN A 95  ? 0.1463 0.1377 0.1362 0.0035  0.0047  0.0077 95  ASN A CG  
734  O  OD1 . ASN A 95  ? 0.1260 0.1172 0.1155 0.0031  0.0046  0.0078 95  ASN A OD1 
735  N  ND2 . ASN A 95  ? 0.1233 0.1156 0.1139 0.0032  0.0043  0.0079 95  ASN A ND2 
736  N  N   . PRO A 96  ? 0.1202 0.1094 0.1080 0.0033  0.0053  0.0076 96  PRO A N   
737  C  CA  . PRO A 96  ? 0.1753 0.1641 0.1625 0.0024  0.0049  0.0078 96  PRO A CA  
738  C  C   . PRO A 96  ? 0.1278 0.1174 0.1153 0.0015  0.0041  0.0083 96  PRO A C   
739  O  O   . PRO A 96  ? 0.0870 0.0765 0.0741 0.0007  0.0037  0.0086 96  PRO A O   
740  C  CB  . PRO A 96  ? 0.1257 0.1141 0.1124 0.0024  0.0050  0.0079 96  PRO A CB  
741  C  CG  . PRO A 96  ? 0.1460 0.1349 0.1333 0.0030  0.0052  0.0077 96  PRO A CG  
742  C  CD  . PRO A 96  ? 0.1250 0.1142 0.1129 0.0038  0.0056  0.0074 96  PRO A CD  
743  N  N   . LYS A 97  ? 0.1334 0.1238 0.1216 0.0015  0.0038  0.0084 97  LYS A N   
744  C  CA  . LYS A 97  ? 0.1140 0.1052 0.1025 0.0005  0.0030  0.0088 97  LYS A CA  
745  C  C   . LYS A 97  ? 0.1544 0.1458 0.1433 0.0006  0.0029  0.0088 97  LYS A C   
746  O  O   . LYS A 97  ? 0.1507 0.1427 0.1399 0.0000  0.0024  0.0090 97  LYS A O   
747  C  CB  . LYS A 97  ? 0.1723 0.1641 0.1612 0.0004  0.0027  0.0090 97  LYS A CB  
748  C  CG  . LYS A 97  ? 0.1325 0.1241 0.1211 0.0004  0.0028  0.0090 97  LYS A CG  
749  C  CD  . LYS A 97  ? 0.2419 0.2340 0.2306 -0.0002 0.0022  0.0094 97  LYS A CD  
750  C  CE  . LYS A 97  ? 0.2930 0.2853 0.2822 0.0006  0.0026  0.0091 97  LYS A CE  
751  N  NZ  . LYS A 97  ? 0.3386 0.3308 0.3275 0.0004  0.0025  0.0093 97  LYS A NZ  
752  N  N   . THR A 98  ? 0.1429 0.1339 0.1317 0.0013  0.0035  0.0084 98  THR A N   
753  C  CA  . THR A 98  ? 0.1514 0.1426 0.1406 0.0013  0.0035  0.0084 98  THR A CA  
754  C  C   . THR A 98  ? 0.1739 0.1653 0.1629 0.0004  0.0029  0.0088 98  THR A C   
755  O  O   . THR A 98  ? 0.1346 0.1254 0.1230 0.0001  0.0030  0.0089 98  THR A O   
756  C  CB  . THR A 98  ? 0.1552 0.1460 0.1444 0.0022  0.0042  0.0080 98  THR A CB  
757  O  OG1 . THR A 98  ? 0.1444 0.1351 0.1338 0.0031  0.0047  0.0077 98  THR A OG1 
758  C  CG2 . THR A 98  ? 0.1099 0.1011 0.0996 0.0022  0.0041  0.0081 98  THR A CG2 
759  N  N   . PRO A 99  ? 0.1558 0.1478 0.1451 -0.0002 0.0023  0.0090 99  PRO A N   
760  C  CA  . PRO A 99  ? 0.1611 0.1531 0.1501 -0.0011 0.0018  0.0094 99  PRO A CA  
761  C  C   . PRO A 99  ? 0.1647 0.1565 0.1538 -0.0007 0.0022  0.0092 99  PRO A C   
762  O  O   . PRO A 99  ? 0.0931 0.0848 0.0826 0.0001  0.0027  0.0089 99  PRO A O   
763  C  CB  . PRO A 99  ? 0.1376 0.1300 0.1268 -0.0015 0.0013  0.0093 99  PRO A CB  
764  C  CG  . PRO A 99  ? 0.1697 0.1623 0.1595 -0.0007 0.0016  0.0091 99  PRO A CG  
765  C  CD  . PRO A 99  ? 0.1253 0.1178 0.1152 0.0001  0.0022  0.0089 99  PRO A CD  
766  N  N   . LYS A 100 ? 0.1812 0.1732 0.1702 -0.0014 0.0019  0.0096 100 LYS A N   
767  C  CA  . LYS A 100 ? 0.1681 0.1599 0.1572 -0.0012 0.0020  0.0095 100 LYS A CA  
768  C  C   . LYS A 100 ? 0.1603 0.1523 0.1497 -0.0011 0.0018  0.0093 100 LYS A C   
769  O  O   . LYS A 100 ? 0.1240 0.1162 0.1133 -0.0015 0.0013  0.0092 100 LYS A O   
770  C  CB  . LYS A 100 ? 0.1934 0.1855 0.1824 -0.0018 0.0018  0.0099 100 LYS A CB  
771  C  CG  . LYS A 100 ? 0.2499 0.2417 0.2388 -0.0017 0.0020  0.0100 100 LYS A CG  
772  C  CD  . LYS A 100 ? 0.3124 0.3043 0.3012 -0.0020 0.0021  0.0103 100 LYS A CD  
773  C  CE  . LYS A 100 ? 0.3910 0.3828 0.3798 -0.0021 0.0021  0.0104 100 LYS A CE  
774  N  NZ  . LYS A 100 ? 0.3964 0.3871 0.3847 -0.0014 0.0028  0.0100 100 LYS A NZ  
775  N  N   . TYR A 101 ? 0.1047 0.0968 0.0946 -0.0004 0.0022  0.0091 101 TYR A N   
776  C  CA  . TYR A 101 ? 0.1457 0.1385 0.1363 -0.0001 0.0021  0.0090 101 TYR A CA  
777  C  C   . TYR A 101 ? 0.1258 0.1187 0.1169 0.0004  0.0025  0.0089 101 TYR A C   
778  O  O   . TYR A 101 ? 0.1378 0.1303 0.1288 0.0007  0.0029  0.0089 101 TYR A O   
779  C  CB  . TYR A 101 ? 0.1142 0.1073 0.1053 0.0005  0.0024  0.0088 101 TYR A CB  
780  C  CG  . TYR A 101 ? 0.0969 0.0900 0.0884 0.0014  0.0031  0.0085 101 TYR A CG  
781  C  CD1 . TYR A 101 ? 0.1439 0.1363 0.1348 0.0017  0.0035  0.0084 101 TYR A CD1 
782  C  CD2 . TYR A 101 ? 0.0932 0.0867 0.0853 0.0021  0.0034  0.0084 101 TYR A CD2 
783  C  CE1 . TYR A 101 ? 0.1307 0.1228 0.1217 0.0026  0.0042  0.0081 101 TYR A CE1 
784  C  CE2 . TYR A 101 ? 0.1037 0.0971 0.0960 0.0029  0.0041  0.0081 101 TYR A CE2 
785  C  CZ  . TYR A 101 ? 0.1675 0.1601 0.1591 0.0032  0.0045  0.0080 101 TYR A CZ  
786  O  OH  . TYR A 101 ? 0.1335 0.1259 0.1252 0.0040  0.0052  0.0077 101 TYR A OH  
787  N  N   . LYS A 102 ? 0.1158 0.1092 0.1075 0.0004  0.0023  0.0089 102 LYS A N   
788  C  CA  . LYS A 102 ? 0.1119 0.1058 0.1043 0.0010  0.0026  0.0089 102 LYS A CA  
789  C  C   . LYS A 102 ? 0.0771 0.0718 0.0703 0.0012  0.0025  0.0088 102 LYS A C   
790  O  O   . LYS A 102 ? 0.0822 0.0771 0.0755 0.0009  0.0021  0.0088 102 LYS A O   
791  C  CB  . LYS A 102 ? 0.1754 0.1691 0.1677 0.0006  0.0025  0.0091 102 LYS A CB  
792  C  CG  . LYS A 102 ? 0.1777 0.1709 0.1691 -0.0002 0.0019  0.0092 102 LYS A CG  
793  C  CD  . LYS A 102 ? 0.3243 0.3174 0.3156 -0.0005 0.0019  0.0094 102 LYS A CD  
794  C  CE  . LYS A 102 ? 0.3524 0.3451 0.3431 -0.0010 0.0016  0.0094 102 LYS A CE  
795  N  NZ  . LYS A 102 ? 0.2774 0.2700 0.2681 -0.0011 0.0016  0.0095 102 LYS A NZ  
796  N  N   . PHE A 103 ? 0.0605 0.0556 0.0544 0.0017  0.0028  0.0088 103 PHE A N   
797  C  CA  . PHE A 103 ? 0.0973 0.0932 0.0920 0.0019  0.0027  0.0087 103 PHE A CA  
798  C  C   . PHE A 103 ? 0.1438 0.1401 0.1389 0.0016  0.0025  0.0089 103 PHE A C   
799  O  O   . PHE A 103 ? 0.0972 0.0934 0.0924 0.0017  0.0026  0.0090 103 PHE A O   
800  C  CB  . PHE A 103 ? 0.0675 0.0636 0.0626 0.0027  0.0032  0.0086 103 PHE A CB  
801  C  CG  . PHE A 103 ? 0.0669 0.0626 0.0616 0.0031  0.0036  0.0084 103 PHE A CG  
802  C  CD1 . PHE A 103 ? 0.1016 0.0971 0.0959 0.0027  0.0034  0.0083 103 PHE A CD1 
803  C  CD2 . PHE A 103 ? 0.0930 0.0887 0.0878 0.0038  0.0041  0.0082 103 PHE A CD2 
804  C  CE1 . PHE A 103 ? 0.0815 0.0767 0.0755 0.0032  0.0037  0.0081 103 PHE A CE1 
805  C  CE2 . PHE A 103 ? 0.0747 0.0701 0.0693 0.0042  0.0045  0.0079 103 PHE A CE2 
806  C  CZ  . PHE A 103 ? 0.0880 0.0831 0.0821 0.0039  0.0043  0.0079 103 PHE A CZ  
807  N  N   . VAL A 104 ? 0.1413 0.1381 0.1368 0.0013  0.0021  0.0090 104 VAL A N   
808  C  CA  . VAL A 104 ? 0.0846 0.0819 0.0806 0.0011  0.0018  0.0092 104 VAL A CA  
809  C  C   . VAL A 104 ? 0.1300 0.1281 0.1269 0.0012  0.0017  0.0092 104 VAL A C   
810  O  O   . VAL A 104 ? 0.1878 0.1861 0.1847 0.0012  0.0016  0.0091 104 VAL A O   
811  C  CB  . VAL A 104 ? 0.1435 0.1406 0.1391 0.0006  0.0015  0.0093 104 VAL A CB  
812  C  CG1 . VAL A 104 ? 0.1724 0.1684 0.1668 0.0004  0.0016  0.0092 104 VAL A CG1 
813  C  CG2 . VAL A 104 ? 0.1935 0.1910 0.1894 0.0003  0.0012  0.0093 104 VAL A CG2 
814  N  N   . ARG A 105 ? 0.0962 0.0948 0.0937 0.0013  0.0016  0.0093 105 ARG A N   
815  C  CA  . ARG A 105 ? 0.1217 0.1211 0.1200 0.0012  0.0014  0.0093 105 ARG A CA  
816  C  C   . ARG A 105 ? 0.1588 0.1588 0.1576 0.0007  0.0010  0.0095 105 ARG A C   
817  O  O   . ARG A 105 ? 0.1665 0.1667 0.1655 0.0006  0.0010  0.0097 105 ARG A O   
818  C  CB  . ARG A 105 ? 0.1168 0.1166 0.1157 0.0015  0.0016  0.0094 105 ARG A CB  
819  C  CG  . ARG A 105 ? 0.1310 0.1312 0.1304 0.0014  0.0014  0.0094 105 ARG A CG  
820  C  CD  . ARG A 105 ? 0.1343 0.1347 0.1340 0.0017  0.0016  0.0094 105 ARG A CD  
821  N  NE  . ARG A 105 ? 0.1649 0.1657 0.1650 0.0016  0.0013  0.0095 105 ARG A NE  
822  C  CZ  . ARG A 105 ? 0.1049 0.1053 0.1046 0.0018  0.0014  0.0093 105 ARG A CZ  
823  N  NH1 . ARG A 105 ? 0.0775 0.0774 0.0766 0.0021  0.0017  0.0091 105 ARG A NH1 
824  N  NH2 . ARG A 105 ? 0.0887 0.0893 0.0887 0.0017  0.0012  0.0094 105 ARG A NH2 
825  N  N   . ILE A 106 ? 0.1847 0.1852 0.1839 0.0005  0.0007  0.0095 106 ILE A N   
826  C  CA  . ILE A 106 ? 0.1670 0.1683 0.1668 0.0000  0.0003  0.0097 106 ILE A CA  
827  C  C   . ILE A 106 ? 0.1948 0.1971 0.1957 -0.0001 0.0001  0.0098 106 ILE A C   
828  O  O   . ILE A 106 ? 0.1348 0.1370 0.1358 0.0002  0.0003  0.0098 106 ILE A O   
829  C  CB  . ILE A 106 ? 0.1513 0.1528 0.1510 -0.0002 0.0001  0.0097 106 ILE A CB  
830  C  CG1 . ILE A 106 ? 0.1552 0.1565 0.1548 0.0000  0.0003  0.0095 106 ILE A CG1 
831  C  CG2 . ILE A 106 ? 0.1763 0.1769 0.1750 -0.0003 0.0002  0.0096 106 ILE A CG2 
832  C  CD1 . ILE A 106 ? 0.1562 0.1583 0.1567 0.0000  0.0001  0.0096 106 ILE A CD1 
833  N  N   . GLN A 107 ? 0.1718 0.1748 0.1733 -0.0005 -0.0002 0.0100 107 GLN A N   
834  C  CA  . GLN A 107 ? 0.1544 0.1584 0.1571 -0.0007 -0.0005 0.0102 107 GLN A CA  
835  C  C   . GLN A 107 ? 0.1421 0.1467 0.1453 -0.0010 -0.0009 0.0102 107 GLN A C   
836  O  O   . GLN A 107 ? 0.1348 0.1394 0.1378 -0.0012 -0.0010 0.0102 107 GLN A O   
837  C  CB  . GLN A 107 ? 0.2391 0.2436 0.2423 -0.0010 -0.0008 0.0105 107 GLN A CB  
838  C  CG  . GLN A 107 ? 0.2258 0.2297 0.2285 -0.0008 -0.0005 0.0105 107 GLN A CG  
839  C  CD  . GLN A 107 ? 0.2916 0.2955 0.2946 -0.0004 -0.0002 0.0105 107 GLN A CD  
840  O  OE1 . GLN A 107 ? 0.3362 0.3408 0.3401 -0.0006 -0.0004 0.0107 107 GLN A OE1 
841  N  NE2 . GLN A 107 ? 0.3140 0.3170 0.3161 0.0000  0.0002  0.0103 107 GLN A NE2 
842  N  N   . PRO A 108 ? 0.1137 0.1189 0.1176 -0.0010 -0.0010 0.0103 108 PRO A N   
843  C  CA  . PRO A 108 ? 0.1222 0.1281 0.1267 -0.0014 -0.0013 0.0103 108 PRO A CA  
844  C  C   . PRO A 108 ? 0.1328 0.1395 0.1379 -0.0019 -0.0017 0.0105 108 PRO A C   
845  O  O   . PRO A 108 ? 0.0978 0.1048 0.1032 -0.0021 -0.0019 0.0107 108 PRO A O   
846  C  CB  . PRO A 108 ? 0.1430 0.1493 0.1482 -0.0014 -0.0014 0.0104 108 PRO A CB  
847  C  CG  . PRO A 108 ? 0.1687 0.1746 0.1736 -0.0011 -0.0012 0.0104 108 PRO A CG  
848  C  CD  . PRO A 108 ? 0.1309 0.1361 0.1351 -0.0009 -0.0009 0.0104 108 PRO A CD  
849  N  N   . GLY A 109 ? 0.1177 0.1247 0.1229 -0.0021 -0.0019 0.0105 109 GLY A N   
850  C  CA  . GLY A 109 ? 0.0921 0.0999 0.0979 -0.0026 -0.0024 0.0107 109 GLY A CA  
851  C  C   . GLY A 109 ? 0.1430 0.1503 0.1480 -0.0027 -0.0023 0.0106 109 GLY A C   
852  O  O   . GLY A 109 ? 0.1243 0.1322 0.1297 -0.0031 -0.0027 0.0108 109 GLY A O   
853  N  N   . GLN A 110 ? 0.1626 0.1688 0.1666 -0.0023 -0.0019 0.0105 110 GLN A N   
854  C  CA  . GLN A 110 ? 0.1768 0.1823 0.1799 -0.0023 -0.0018 0.0104 110 GLN A CA  
855  C  C   . GLN A 110 ? 0.1456 0.1509 0.1484 -0.0022 -0.0017 0.0103 110 GLN A C   
856  O  O   . GLN A 110 ? 0.1414 0.1468 0.1444 -0.0019 -0.0015 0.0102 110 GLN A O   
857  C  CB  . GLN A 110 ? 0.1304 0.1348 0.1325 -0.0019 -0.0014 0.0103 110 GLN A CB  
858  C  CG  . GLN A 110 ? 0.1779 0.1825 0.1803 -0.0019 -0.0014 0.0104 110 GLN A CG  
859  C  CD  . GLN A 110 ? 0.3196 0.3229 0.3208 -0.0016 -0.0010 0.0103 110 GLN A CD  
860  O  OE1 . GLN A 110 ? 0.2390 0.2417 0.2399 -0.0012 -0.0006 0.0102 110 GLN A OE1 
861  N  NE2 . GLN A 110 ? 0.3442 0.3471 0.3448 -0.0019 -0.0010 0.0104 110 GLN A NE2 
862  N  N   . THR A 111 ? 0.1292 0.1344 0.1316 -0.0024 -0.0018 0.0103 111 THR A N   
863  C  CA  . THR A 111 ? 0.1205 0.1255 0.1226 -0.0023 -0.0017 0.0103 111 THR A CA  
864  C  C   . THR A 111 ? 0.0898 0.0935 0.0907 -0.0020 -0.0013 0.0101 111 THR A C   
865  O  O   . THR A 111 ? 0.0912 0.0942 0.0914 -0.0019 -0.0011 0.0100 111 THR A O   
866  C  CB  . THR A 111 ? 0.0897 0.0956 0.0925 -0.0030 -0.0023 0.0105 111 THR A CB  
867  O  OG1 . THR A 111 ? 0.0987 0.1043 0.1009 -0.0033 -0.0024 0.0106 111 THR A OG1 
868  C  CG2 . THR A 111 ? 0.0966 0.1037 0.1006 -0.0033 -0.0027 0.0107 111 THR A CG2 
869  N  N   . PHE A 112 ? 0.0780 0.0816 0.0787 -0.0017 -0.0012 0.0100 112 PHE A N   
870  C  CA  . PHE A 112 ? 0.0829 0.0853 0.0824 -0.0014 -0.0008 0.0098 112 PHE A CA  
871  C  C   . PHE A 112 ? 0.0637 0.0662 0.0632 -0.0014 -0.0008 0.0099 112 PHE A C   
872  O  O   . PHE A 112 ? 0.0504 0.0538 0.0508 -0.0015 -0.0010 0.0100 112 PHE A O   
873  C  CB  . PHE A 112 ? 0.0600 0.0615 0.0589 -0.0008 -0.0003 0.0096 112 PHE A CB  
874  C  CG  . PHE A 112 ? 0.0837 0.0854 0.0829 -0.0005 -0.0002 0.0095 112 PHE A CG  
875  C  CD1 . PHE A 112 ? 0.0875 0.0899 0.0875 -0.0005 -0.0003 0.0096 112 PHE A CD1 
876  C  CD2 . PHE A 112 ? 0.0678 0.0691 0.0667 -0.0001 0.0001  0.0094 112 PHE A CD2 
877  C  CE1 . PHE A 112 ? 0.1189 0.1213 0.1191 -0.0002 -0.0001 0.0095 112 PHE A CE1 
878  C  CE2 . PHE A 112 ? 0.0637 0.0651 0.0628 0.0002  0.0002  0.0093 112 PHE A CE2 
879  C  CZ  . PHE A 112 ? 0.0886 0.0905 0.0882 0.0002  0.0001  0.0093 112 PHE A CZ  
880  N  N   . SER A 113 ? 0.0164 0.0181 0.0150 -0.0013 -0.0006 0.0098 113 SER A N   
881  C  CA  . SER A 113 ? 0.0427 0.0445 0.0413 -0.0012 -0.0005 0.0098 113 SER A CA  
882  C  C   . SER A 113 ? 0.0556 0.0566 0.0536 -0.0006 -0.0001 0.0096 113 SER A C   
883  O  O   . SER A 113 ? 0.0365 0.0367 0.0339 -0.0002 0.0002  0.0094 113 SER A O   
884  C  CB  . SER A 113 ? 0.0580 0.0593 0.0559 -0.0015 -0.0006 0.0099 113 SER A CB  
885  O  OG  . SER A 113 ? 0.1066 0.1086 0.1049 -0.0021 -0.0011 0.0101 113 SER A OG  
886  N  N   . VAL A 114 ? 0.0618 0.0632 0.0601 -0.0004 0.0000  0.0096 114 VAL A N   
887  C  CA  . VAL A 114 ? 0.0438 0.0446 0.0417 0.0002  0.0004  0.0094 114 VAL A CA  
888  C  C   . VAL A 114 ? 0.0487 0.0492 0.0461 0.0002  0.0005  0.0095 114 VAL A C   
889  O  O   . VAL A 114 ? 0.0459 0.0471 0.0439 -0.0001 0.0002  0.0097 114 VAL A O   
890  C  CB  . VAL A 114 ? 0.0550 0.0564 0.0535 0.0004  0.0004  0.0094 114 VAL A CB  
891  C  CG1 . VAL A 114 ? 0.0255 0.0263 0.0235 0.0010  0.0008  0.0092 114 VAL A CG1 
892  C  CG2 . VAL A 114 ? 0.0643 0.0659 0.0632 0.0003  0.0003  0.0094 114 VAL A CG2 
893  N  N   . LEU A 115 ? 0.0405 0.0402 0.0372 0.0006  0.0008  0.0093 115 LEU A N   
894  C  CA  . LEU A 115 ? 0.0781 0.0775 0.0744 0.0007  0.0009  0.0093 115 LEU A CA  
895  C  C   . LEU A 115 ? 0.0856 0.0850 0.0820 0.0013  0.0013  0.0092 115 LEU A C   
896  O  O   . LEU A 115 ? 0.0754 0.0743 0.0715 0.0017  0.0016  0.0090 115 LEU A O   
897  C  CB  . LEU A 115 ? 0.0708 0.0692 0.0662 0.0007  0.0010  0.0092 115 LEU A CB  
898  C  CG  . LEU A 115 ? 0.1055 0.1036 0.1005 0.0008  0.0012  0.0092 115 LEU A CG  
899  C  CD1 . LEU A 115 ? 0.0930 0.0916 0.0882 0.0004  0.0009  0.0095 115 LEU A CD1 
900  C  CD2 . LEU A 115 ? 0.0534 0.0505 0.0475 0.0008  0.0013  0.0091 115 LEU A CD2 
901  N  N   . ALA A 116 ? 0.0459 0.0460 0.0429 0.0013  0.0012  0.0093 116 ALA A N   
902  C  CA  . ALA A 116 ? 0.0994 0.0994 0.0964 0.0019  0.0016  0.0092 116 ALA A CA  
903  C  C   . ALA A 116 ? 0.1372 0.1369 0.1338 0.0022  0.0019  0.0092 116 ALA A C   
904  O  O   . ALA A 116 ? 0.0996 0.0993 0.0961 0.0019  0.0017  0.0093 116 ALA A O   
905  C  CB  . ALA A 116 ? 0.1013 0.1021 0.0990 0.0018  0.0015  0.0094 116 ALA A CB  
906  N  N   . CYS A 117 ? 0.1126 0.1119 0.1089 0.0028  0.0024  0.0089 117 CYS A N   
907  C  CA  . CYS A 117 ? 0.1393 0.1382 0.1353 0.0033  0.0028  0.0088 117 CYS A CA  
908  C  C   . CYS A 117 ? 0.1307 0.1296 0.1267 0.0040  0.0033  0.0087 117 CYS A C   
909  O  O   . CYS A 117 ? 0.0894 0.0882 0.0854 0.0043  0.0034  0.0085 117 CYS A O   
910  C  CB  . CYS A 117 ? 0.1224 0.1206 0.1179 0.0034  0.0029  0.0086 117 CYS A CB  
911  S  SG  . CYS A 117 ? 0.1884 0.1864 0.1836 0.0026  0.0024  0.0088 117 CYS A SG  
912  N  N   . TYR A 118 ? 0.1604 0.1592 0.1562 0.0044  0.0036  0.0087 118 TYR A N   
913  C  CA  . TYR A 118 ? 0.1554 0.1541 0.1511 0.0052  0.0042  0.0085 118 TYR A CA  
914  C  C   . TYR A 118 ? 0.1886 0.1868 0.1839 0.0057  0.0046  0.0083 118 TYR A C   
915  O  O   . TYR A 118 ? 0.1713 0.1696 0.1666 0.0055  0.0045  0.0085 118 TYR A O   
916  C  CB  . TYR A 118 ? 0.1764 0.1756 0.1725 0.0052  0.0041  0.0087 118 TYR A CB  
917  C  CG  . TYR A 118 ? 0.1599 0.1595 0.1563 0.0048  0.0037  0.0088 118 TYR A CG  
918  C  CD1 . TYR A 118 ? 0.1585 0.1585 0.1553 0.0040  0.0031  0.0091 118 TYR A CD1 
919  C  CD2 . TYR A 118 ? 0.1468 0.1463 0.1431 0.0051  0.0038  0.0087 118 TYR A CD2 
920  C  CE1 . TYR A 118 ? 0.1903 0.1907 0.1875 0.0036  0.0027  0.0092 118 TYR A CE1 
921  C  CE2 . TYR A 118 ? 0.1101 0.1098 0.1067 0.0047  0.0035  0.0088 118 TYR A CE2 
922  C  CZ  . TYR A 118 ? 0.1443 0.1445 0.1414 0.0039  0.0029  0.0091 118 TYR A CZ  
923  O  OH  . TYR A 118 ? 0.1111 0.1117 0.1085 0.0035  0.0026  0.0092 118 TYR A OH  
924  N  N   . ASN A 119 ? 0.1927 0.1904 0.1876 0.0064  0.0052  0.0080 119 ASN A N   
925  C  CA  . ASN A 119 ? 0.2394 0.2367 0.2339 0.0070  0.0057  0.0078 119 ASN A CA  
926  C  C   . ASN A 119 ? 0.1578 0.1548 0.1522 0.0065  0.0054  0.0078 119 ASN A C   
927  O  O   . ASN A 119 ? 0.1751 0.1719 0.1692 0.0066  0.0056  0.0079 119 ASN A O   
928  C  CB  . ASN A 119 ? 0.2814 0.2788 0.2759 0.0074  0.0059  0.0079 119 ASN A CB  
929  C  CG  . ASN A 119 ? 0.4081 0.4052 0.4022 0.0082  0.0065  0.0076 119 ASN A CG  
930  O  OD1 . ASN A 119 ? 0.3879 0.3844 0.3814 0.0088  0.0070  0.0073 119 ASN A OD1 
931  N  ND2 . ASN A 119 ? 0.4872 0.4846 0.4815 0.0082  0.0065  0.0078 119 ASN A ND2 
932  N  N   . GLY A 120 ? 0.1346 0.1316 0.1290 0.0060  0.0050  0.0079 120 GLY A N   
933  C  CA  . GLY A 120 ? 0.1240 0.1208 0.1183 0.0055  0.0048  0.0079 120 GLY A CA  
934  C  C   . GLY A 120 ? 0.1455 0.1425 0.1399 0.0048  0.0042  0.0083 120 GLY A C   
935  O  O   . GLY A 120 ? 0.1442 0.1408 0.1382 0.0044  0.0040  0.0084 120 GLY A O   
936  N  N   . SER A 121 ? 0.1383 0.1359 0.1330 0.0046  0.0040  0.0086 121 SER A N   
937  C  CA  . SER A 121 ? 0.2187 0.2165 0.2135 0.0039  0.0035  0.0089 121 SER A CA  
938  C  C   . SER A 121 ? 0.1812 0.1794 0.1763 0.0032  0.0029  0.0091 121 SER A C   
939  O  O   . SER A 121 ? 0.1752 0.1739 0.1708 0.0034  0.0029  0.0091 121 SER A O   
940  C  CB  . SER A 121 ? 0.3024 0.3005 0.2974 0.0042  0.0037  0.0091 121 SER A CB  
941  O  OG  . SER A 121 ? 0.3795 0.3772 0.3741 0.0044  0.0039  0.0090 121 SER A OG  
942  N  N   . PRO A 122 ? 0.2117 0.2097 0.2065 0.0025  0.0025  0.0092 122 PRO A N   
943  C  CA  . PRO A 122 ? 0.1855 0.1839 0.1806 0.0019  0.0020  0.0094 122 PRO A CA  
944  C  C   . PRO A 122 ? 0.2216 0.2208 0.2173 0.0018  0.0018  0.0096 122 PRO A C   
945  O  O   . PRO A 122 ? 0.2616 0.2609 0.2573 0.0018  0.0019  0.0098 122 PRO A O   
946  C  CB  . PRO A 122 ? 0.1960 0.1939 0.1905 0.0013  0.0016  0.0094 122 PRO A CB  
947  C  CG  . PRO A 122 ? 0.2204 0.2175 0.2142 0.0015  0.0019  0.0093 122 PRO A CG  
948  C  CD  . PRO A 122 ? 0.1537 0.1510 0.1478 0.0022  0.0024  0.0092 122 PRO A CD  
949  N  N   . SER A 123 ? 0.2011 0.2009 0.1974 0.0018  0.0017  0.0097 123 SER A N   
950  C  CA  . SER A 123 ? 0.2745 0.2751 0.2715 0.0017  0.0016  0.0099 123 SER A CA  
951  C  C   . SER A 123 ? 0.2103 0.2117 0.2079 0.0011  0.0011  0.0102 123 SER A C   
952  O  O   . SER A 123 ? 0.1910 0.1931 0.1891 0.0008  0.0009  0.0105 123 SER A O   
953  C  CB  . SER A 123 ? 0.2601 0.2609 0.2574 0.0023  0.0019  0.0098 123 SER A CB  
954  O  OG  . SER A 123 ? 0.3697 0.3714 0.3677 0.0021  0.0017  0.0101 123 SER A OG  
955  N  N   . GLY A 124 ? 0.1124 0.1137 0.1100 0.0008  0.0009  0.0101 124 GLY A N   
956  C  CA  . GLY A 124 ? 0.1228 0.1250 0.1212 0.0003  0.0005  0.0103 124 GLY A CA  
957  C  C   . GLY A 124 ? 0.1448 0.1468 0.1431 0.0000  0.0003  0.0101 124 GLY A C   
958  O  O   . GLY A 124 ? 0.1159 0.1171 0.1136 0.0004  0.0006  0.0099 124 GLY A O   
959  N  N   . VAL A 125 ? 0.1011 0.1038 0.0999 -0.0006 -0.0001 0.0103 125 VAL A N   
960  C  CA  . VAL A 125 ? 0.0776 0.0801 0.0763 -0.0008 -0.0003 0.0103 125 VAL A CA  
961  C  C   . VAL A 125 ? 0.1013 0.1051 0.1012 -0.0013 -0.0007 0.0105 125 VAL A C   
962  O  O   . VAL A 125 ? 0.0850 0.0897 0.0856 -0.0017 -0.0011 0.0107 125 VAL A O   
963  C  CB  . VAL A 125 ? 0.1045 0.1065 0.1025 -0.0012 -0.0004 0.0103 125 VAL A CB  
964  C  CG1 . VAL A 125 ? 0.1229 0.1256 0.1213 -0.0018 -0.0009 0.0106 125 VAL A CG1 
965  C  CG2 . VAL A 125 ? 0.0865 0.0883 0.0844 -0.0014 -0.0006 0.0102 125 VAL A CG2 
966  N  N   . TYR A 126 ? 0.0952 0.0990 0.0953 -0.0012 -0.0007 0.0103 126 TYR A N   
967  C  CA  . TYR A 126 ? 0.1167 0.1216 0.1179 -0.0016 -0.0011 0.0105 126 TYR A CA  
968  C  C   . TYR A 126 ? 0.0969 0.1016 0.0979 -0.0017 -0.0012 0.0104 126 TYR A C   
969  O  O   . TYR A 126 ? 0.0712 0.0748 0.0714 -0.0013 -0.0008 0.0101 126 TYR A O   
970  C  CB  . TYR A 126 ? 0.1068 0.1122 0.1085 -0.0013 -0.0010 0.0105 126 TYR A CB  
971  C  CG  . TYR A 126 ? 0.0979 0.1025 0.0990 -0.0007 -0.0005 0.0103 126 TYR A CG  
972  C  CD1 . TYR A 126 ? 0.1089 0.1134 0.1101 -0.0006 -0.0005 0.0101 126 TYR A CD1 
973  C  CD2 . TYR A 126 ? 0.1687 0.1725 0.1691 -0.0001 -0.0001 0.0101 126 TYR A CD2 
974  C  CE1 . TYR A 126 ? 0.1241 0.1278 0.1248 -0.0001 -0.0001 0.0099 126 TYR A CE1 
975  C  CE2 . TYR A 126 ? 0.1193 0.1224 0.1192 0.0004  0.0003  0.0099 126 TYR A CE2 
976  C  CZ  . TYR A 126 ? 0.0811 0.0842 0.0812 0.0004  0.0003  0.0098 126 TYR A CZ  
977  O  OH  . TYR A 126 ? 0.1218 0.1242 0.1214 0.0009  0.0006  0.0095 126 TYR A OH  
978  N  N   . GLN A 127 ? 0.0666 0.0723 0.0685 -0.0022 -0.0016 0.0105 127 GLN A N   
979  C  CA  . GLN A 127 ? 0.0851 0.0908 0.0872 -0.0023 -0.0018 0.0105 127 GLN A CA  
980  C  C   . GLN A 127 ? 0.1590 0.1651 0.1617 -0.0022 -0.0017 0.0105 127 GLN A C   
981  O  O   . GLN A 127 ? 0.1515 0.1583 0.1548 -0.0022 -0.0018 0.0106 127 GLN A O   
982  C  CB  . GLN A 127 ? 0.1189 0.1253 0.1214 -0.0031 -0.0023 0.0107 127 GLN A CB  
983  C  CG  . GLN A 127 ? 0.1406 0.1470 0.1432 -0.0033 -0.0025 0.0107 127 GLN A CG  
984  C  CD  . GLN A 127 ? 0.1353 0.1406 0.1368 -0.0031 -0.0022 0.0105 127 GLN A CD  
985  O  OE1 . GLN A 127 ? 0.1299 0.1343 0.1305 -0.0028 -0.0019 0.0104 127 GLN A OE1 
986  N  NE2 . GLN A 127 ? 0.1300 0.1352 0.1314 -0.0033 -0.0023 0.0105 127 GLN A NE2 
987  N  N   . CYS A 128 ? 0.1550 0.1607 0.1575 -0.0020 -0.0016 0.0103 128 CYS A N   
988  C  CA  . CYS A 128 ? 0.1714 0.1776 0.1746 -0.0019 -0.0016 0.0103 128 CYS A CA  
989  C  C   . CYS A 128 ? 0.1346 0.1404 0.1376 -0.0019 -0.0016 0.0102 128 CYS A C   
990  O  O   . CYS A 128 ? 0.1369 0.1422 0.1393 -0.0018 -0.0015 0.0102 128 CYS A O   
991  C  CB  . CYS A 128 ? 0.2056 0.2112 0.2084 -0.0013 -0.0012 0.0102 128 CYS A CB  
992  S  SG  . CYS A 128 ? 0.1980 0.2022 0.1995 -0.0006 -0.0006 0.0098 128 CYS A SG  
993  N  N   . ALA A 129 ? 0.1087 0.1150 0.1124 -0.0019 -0.0016 0.0103 129 ALA A N   
994  C  CA  . ALA A 129 ? 0.1227 0.1290 0.1265 -0.0019 -0.0017 0.0102 129 ALA A CA  
995  C  C   . ALA A 129 ? 0.0995 0.1052 0.1029 -0.0014 -0.0013 0.0101 129 ALA A C   
996  O  O   . ALA A 129 ? 0.1278 0.1334 0.1311 -0.0012 -0.0012 0.0100 129 ALA A O   
997  C  CB  . ALA A 129 ? 0.1178 0.1253 0.1228 -0.0025 -0.0022 0.0105 129 ALA A CB  
998  N  N   . MET A 130 ? 0.1252 0.1303 0.1282 -0.0012 -0.0011 0.0100 130 MET A N   
999  C  CA  . MET A 130 ? 0.1355 0.1403 0.1384 -0.0009 -0.0009 0.0099 130 MET A CA  
1000 C  C   . MET A 130 ? 0.0959 0.1016 0.0998 -0.0012 -0.0013 0.0101 130 MET A C   
1001 O  O   . MET A 130 ? 0.0671 0.0735 0.0716 -0.0017 -0.0016 0.0102 130 MET A O   
1002 C  CB  . MET A 130 ? 0.0881 0.0923 0.0905 -0.0007 -0.0007 0.0098 130 MET A CB  
1003 C  CG  . MET A 130 ? 0.1329 0.1367 0.1351 -0.0004 -0.0005 0.0097 130 MET A CG  
1004 S  SD  . MET A 130 ? 0.1478 0.1507 0.1491 0.0002  -0.0001 0.0095 130 MET A SD  
1005 C  CE  . MET A 130 ? 0.1618 0.1637 0.1622 0.0005  0.0003  0.0093 130 MET A CE  
1006 N  N   . ARG A 131 ? 0.0716 0.0772 0.0755 -0.0011 -0.0012 0.0100 131 ARG A N   
1007 C  CA  . ARG A 131 ? 0.1245 0.1309 0.1293 -0.0015 -0.0016 0.0102 131 ARG A CA  
1008 C  C   . ARG A 131 ? 0.0801 0.0864 0.0850 -0.0015 -0.0016 0.0102 131 ARG A C   
1009 O  O   . ARG A 131 ? 0.0782 0.0838 0.0825 -0.0011 -0.0013 0.0101 131 ARG A O   
1010 C  CB  . ARG A 131 ? 0.0875 0.0936 0.0920 -0.0013 -0.0015 0.0101 131 ARG A CB  
1011 C  CG  . ARG A 131 ? 0.1254 0.1316 0.1298 -0.0013 -0.0014 0.0101 131 ARG A CG  
1012 C  CD  . ARG A 131 ? 0.1014 0.1088 0.1069 -0.0018 -0.0019 0.0104 131 ARG A CD  
1013 N  NE  . ARG A 131 ? 0.1076 0.1159 0.1140 -0.0023 -0.0023 0.0106 131 ARG A NE  
1014 C  CZ  . ARG A 131 ? 0.1569 0.1662 0.1642 -0.0029 -0.0027 0.0108 131 ARG A CZ  
1015 N  NH1 . ARG A 131 ? 0.0625 0.0721 0.0699 -0.0030 -0.0028 0.0108 131 ARG A NH1 
1016 N  NH2 . ARG A 131 ? 0.0623 0.0725 0.0706 -0.0033 -0.0031 0.0109 131 ARG A NH2 
1017 N  N   . PRO A 132 ? 0.0999 0.1072 0.1059 -0.0019 -0.0020 0.0104 132 PRO A N   
1018 C  CA  . PRO A 132 ? 0.1081 0.1154 0.1143 -0.0019 -0.0020 0.0105 132 PRO A CA  
1019 C  C   . PRO A 132 ? 0.1166 0.1230 0.1221 -0.0015 -0.0017 0.0103 132 PRO A C   
1020 O  O   . PRO A 132 ? 0.1029 0.1089 0.1082 -0.0013 -0.0016 0.0103 132 PRO A O   
1021 C  CB  . PRO A 132 ? 0.1268 0.1351 0.1341 -0.0025 -0.0025 0.0107 132 PRO A CB  
1022 C  CG  . PRO A 132 ? 0.1008 0.1098 0.1086 -0.0028 -0.0027 0.0108 132 PRO A CG  
1023 C  CD  . PRO A 132 ? 0.1260 0.1343 0.1329 -0.0025 -0.0024 0.0106 132 PRO A CD  
1024 N  N   . ASN A 133 ? 0.0978 0.1036 0.1026 -0.0013 -0.0016 0.0102 133 ASN A N   
1025 C  CA  . ASN A 133 ? 0.1153 0.1201 0.1192 -0.0009 -0.0014 0.0100 133 ASN A CA  
1026 C  C   . ASN A 133 ? 0.1010 0.1047 0.1038 -0.0003 -0.0009 0.0098 133 ASN A C   
1027 O  O   . ASN A 133 ? 0.0792 0.0820 0.0810 0.0000  -0.0007 0.0097 133 ASN A O   
1028 C  CB  . ASN A 133 ? 0.1165 0.1210 0.1201 -0.0009 -0.0015 0.0100 133 ASN A CB  
1029 C  CG  . ASN A 133 ? 0.1276 0.1318 0.1308 -0.0007 -0.0013 0.0099 133 ASN A CG  
1030 O  OD1 . ASN A 133 ? 0.0990 0.1032 0.1020 -0.0006 -0.0011 0.0099 133 ASN A OD1 
1031 N  ND2 . ASN A 133 ? 0.1433 0.1470 0.1460 -0.0006 -0.0013 0.0099 133 ASN A ND2 
1032 N  N   . PHE A 134 ? 0.0821 0.0860 0.0849 -0.0003 -0.0008 0.0098 134 PHE A N   
1033 C  CA  . PHE A 134 ? 0.1318 0.1348 0.1337 0.0001  -0.0004 0.0096 134 PHE A CA  
1034 C  C   . PHE A 134 ? 0.1126 0.1150 0.1137 0.0004  -0.0002 0.0094 134 PHE A C   
1035 O  O   . PHE A 134 ? 0.1347 0.1362 0.1349 0.0009  0.0001  0.0092 134 PHE A O   
1036 C  CB  . PHE A 134 ? 0.0754 0.0778 0.0768 0.0004  -0.0002 0.0095 134 PHE A CB  
1037 C  CG  . PHE A 134 ? 0.1225 0.1255 0.1247 0.0002  -0.0003 0.0097 134 PHE A CG  
1038 C  CD1 . PHE A 134 ? 0.0944 0.0975 0.0965 0.0002  -0.0002 0.0097 134 PHE A CD1 
1039 C  CD2 . PHE A 134 ? 0.1535 0.1568 0.1562 0.0000  -0.0005 0.0099 134 PHE A CD2 
1040 C  CE1 . PHE A 134 ? 0.1895 0.1930 0.1921 0.0001  -0.0002 0.0099 134 PHE A CE1 
1041 C  CE2 . PHE A 134 ? 0.1377 0.1416 0.1411 -0.0002 -0.0006 0.0101 134 PHE A CE2 
1042 C  CZ  . PHE A 134 ? 0.2277 0.2316 0.2310 -0.0001 -0.0004 0.0101 134 PHE A CZ  
1043 N  N   . THR A 135 ? 0.0838 0.0865 0.0851 0.0003  -0.0003 0.0095 135 THR A N   
1044 C  CA  . THR A 135 ? 0.0727 0.0750 0.0735 0.0005  -0.0002 0.0094 135 THR A CA  
1045 C  C   . THR A 135 ? 0.1186 0.1216 0.1199 0.0003  -0.0003 0.0095 135 THR A C   
1046 O  O   . THR A 135 ? 0.0743 0.0781 0.0764 -0.0001 -0.0005 0.0096 135 THR A O   
1047 C  CB  . THR A 135 ? 0.1103 0.1125 0.1110 0.0005  -0.0003 0.0094 135 THR A CB  
1048 O  OG1 . THR A 135 ? 0.1284 0.1318 0.1302 0.0000  -0.0006 0.0096 135 THR A OG1 
1049 C  CG2 . THR A 135 ? 0.0770 0.0784 0.0770 0.0007  -0.0003 0.0093 135 THR A CG2 
1050 N  N   . ILE A 136 ? 0.0831 0.0857 0.0839 0.0005  -0.0001 0.0094 136 ILE A N   
1051 C  CA  . ILE A 136 ? 0.0917 0.0950 0.0930 0.0002  -0.0002 0.0095 136 ILE A CA  
1052 C  C   . ILE A 136 ? 0.1067 0.1101 0.1080 0.0003  -0.0002 0.0096 136 ILE A C   
1053 O  O   . ILE A 136 ? 0.0967 0.0994 0.0972 0.0007  0.0001  0.0094 136 ILE A O   
1054 C  CB  . ILE A 136 ? 0.1451 0.1480 0.1459 0.0003  0.0000  0.0094 136 ILE A CB  
1055 C  CG1 . ILE A 136 ? 0.1130 0.1153 0.1130 0.0008  0.0003  0.0093 136 ILE A CG1 
1056 C  CG2 . ILE A 136 ? 0.0878 0.0903 0.0883 0.0005  0.0001  0.0093 136 ILE A CG2 
1057 C  CD1 . ILE A 136 ? 0.1623 0.1641 0.1619 0.0008  0.0004  0.0092 136 ILE A CD1 
1058 N  N   . LYS A 137 ? 0.1196 0.1240 0.1217 -0.0002 -0.0005 0.0098 137 LYS A N   
1059 C  CA  . LYS A 137 ? 0.1089 0.1135 0.1111 -0.0001 -0.0005 0.0099 137 LYS A CA  
1060 C  C   . LYS A 137 ? 0.1408 0.1453 0.1427 0.0000  -0.0003 0.0099 137 LYS A C   
1061 O  O   . LYS A 137 ? 0.1359 0.1411 0.1384 -0.0004 -0.0006 0.0101 137 LYS A O   
1062 C  CB  . LYS A 137 ? 0.1522 0.1580 0.1556 -0.0006 -0.0009 0.0101 137 LYS A CB  
1063 C  CG  . LYS A 137 ? 0.1726 0.1786 0.1764 -0.0009 -0.0011 0.0102 137 LYS A CG  
1064 C  CD  . LYS A 137 ? 0.2501 0.2569 0.2547 -0.0012 -0.0014 0.0104 137 LYS A CD  
1065 C  CE  . LYS A 137 ? 0.2292 0.2365 0.2344 -0.0016 -0.0017 0.0105 137 LYS A CE  
1066 N  NZ  . LYS A 137 ? 0.2446 0.2511 0.2493 -0.0013 -0.0016 0.0104 137 LYS A NZ  
1067 N  N   . GLY A 138 ? 0.1105 0.1141 0.1115 0.0005  0.0001  0.0097 138 GLY A N   
1068 C  CA  . GLY A 138 ? 0.0683 0.0717 0.0690 0.0007  0.0002  0.0097 138 GLY A CA  
1069 C  C   . GLY A 138 ? 0.1212 0.1248 0.1219 0.0008  0.0003  0.0098 138 GLY A C   
1070 O  O   . GLY A 138 ? 0.2079 0.2117 0.2089 0.0008  0.0003  0.0099 138 GLY A O   
1071 N  N   . SER A 139 ? 0.1060 0.1092 0.1063 0.0010  0.0005  0.0098 139 SER A N   
1072 C  CA  . SER A 139 ? 0.1199 0.1231 0.1201 0.0013  0.0008  0.0098 139 SER A CA  
1073 C  C   . SER A 139 ? 0.1052 0.1074 0.1044 0.0019  0.0012  0.0096 139 SER A C   
1074 O  O   . SER A 139 ? 0.1166 0.1187 0.1157 0.0018  0.0012  0.0096 139 SER A O   
1075 C  CB  . SER A 139 ? 0.0933 0.0974 0.0942 0.0010  0.0005  0.0101 139 SER A CB  
1076 O  OG  . SER A 139 ? 0.1722 0.1761 0.1727 0.0013  0.0008  0.0102 139 SER A OG  
1077 N  N   . PHE A 140 ? 0.1080 0.1096 0.1066 0.0023  0.0015  0.0094 140 PHE A N   
1078 C  CA  . PHE A 140 ? 0.1476 0.1485 0.1455 0.0029  0.0019  0.0091 140 PHE A CA  
1079 C  C   . PHE A 140 ? 0.1427 0.1432 0.1402 0.0034  0.0022  0.0091 140 PHE A C   
1080 O  O   . PHE A 140 ? 0.1641 0.1646 0.1616 0.0035  0.0022  0.0091 140 PHE A O   
1081 C  CB  . PHE A 140 ? 0.0997 0.1001 0.0974 0.0029  0.0019  0.0089 140 PHE A CB  
1082 C  CG  . PHE A 140 ? 0.1457 0.1462 0.1435 0.0025  0.0017  0.0089 140 PHE A CG  
1083 C  CD1 . PHE A 140 ? 0.0764 0.0768 0.0741 0.0026  0.0018  0.0089 140 PHE A CD1 
1084 C  CD2 . PHE A 140 ? 0.1463 0.1469 0.1443 0.0022  0.0014  0.0090 140 PHE A CD2 
1085 C  CE1 . PHE A 140 ? 0.0983 0.0986 0.0959 0.0022  0.0016  0.0089 140 PHE A CE1 
1086 C  CE2 . PHE A 140 ? 0.0731 0.0738 0.0713 0.0019  0.0013  0.0090 140 PHE A CE2 
1087 C  CZ  . PHE A 140 ? 0.0650 0.0655 0.0629 0.0019  0.0014  0.0090 140 PHE A CZ  
1088 N  N   . LEU A 141 ? 0.1376 0.1380 0.1349 0.0039  0.0026  0.0090 141 LEU A N   
1089 C  CA  . LEU A 141 ? 0.1478 0.1477 0.1446 0.0045  0.0031  0.0089 141 LEU A CA  
1090 C  C   . LEU A 141 ? 0.1446 0.1438 0.1407 0.0051  0.0035  0.0085 141 LEU A C   
1091 O  O   . LEU A 141 ? 0.1513 0.1504 0.1474 0.0050  0.0035  0.0084 141 LEU A O   
1092 C  CB  . LEU A 141 ? 0.1739 0.1742 0.1709 0.0047  0.0032  0.0091 141 LEU A CB  
1093 C  CG  . LEU A 141 ? 0.2150 0.2162 0.2127 0.0042  0.0028  0.0094 141 LEU A CG  
1094 C  CD1 . LEU A 141 ? 0.2464 0.2480 0.2444 0.0043  0.0030  0.0096 141 LEU A CD1 
1095 C  CD2 . LEU A 141 ? 0.1903 0.1915 0.1881 0.0042  0.0028  0.0095 141 LEU A CD2 
1096 N  N   . ASN A 142 ? 0.1758 0.1745 0.1713 0.0057  0.0039  0.0084 142 ASN A N   
1097 C  CA  . ASN A 142 ? 0.1568 0.1548 0.1516 0.0063  0.0044  0.0080 142 ASN A CA  
1098 C  C   . ASN A 142 ? 0.1802 0.1784 0.1752 0.0065  0.0046  0.0080 142 ASN A C   
1099 O  O   . ASN A 142 ? 0.1540 0.1526 0.1493 0.0065  0.0047  0.0082 142 ASN A O   
1100 C  CB  . ASN A 142 ? 0.1763 0.1738 0.1704 0.0071  0.0049  0.0078 142 ASN A CB  
1101 C  CG  . ASN A 142 ? 0.1797 0.1764 0.1730 0.0077  0.0054  0.0074 142 ASN A CG  
1102 O  OD1 . ASN A 142 ? 0.2883 0.2850 0.2816 0.0079  0.0056  0.0073 142 ASN A OD1 
1103 N  ND2 . ASN A 142 ? 0.3588 0.3549 0.3513 0.0080  0.0055  0.0072 142 ASN A ND2 
1104 N  N   . GLY A 143 ? 0.0999 0.0977 0.0946 0.0066  0.0048  0.0078 143 GLY A N   
1105 C  CA  . GLY A 143 ? 0.1155 0.1133 0.1102 0.0067  0.0049  0.0077 143 GLY A CA  
1106 C  C   . GLY A 143 ? 0.0917 0.0898 0.0869 0.0060  0.0045  0.0079 143 GLY A C   
1107 O  O   . GLY A 143 ? 0.1410 0.1390 0.1362 0.0060  0.0046  0.0079 143 GLY A O   
1108 N  N   . SER A 144 ? 0.0585 0.0570 0.0542 0.0054  0.0040  0.0081 144 SER A N   
1109 C  CA  . SER A 144 ? 0.1198 0.1186 0.1158 0.0047  0.0035  0.0082 144 SER A CA  
1110 C  C   . SER A 144 ? 0.0989 0.0974 0.0948 0.0047  0.0035  0.0081 144 SER A C   
1111 O  O   . SER A 144 ? 0.0858 0.0843 0.0818 0.0042  0.0032  0.0082 144 SER A O   
1112 C  CB  . SER A 144 ? 0.0831 0.0823 0.0796 0.0041  0.0030  0.0085 144 SER A CB  
1113 O  OG  . SER A 144 ? 0.1292 0.1284 0.1256 0.0041  0.0029  0.0084 144 SER A OG  
1114 N  N   . CYS A 145 ? 0.0560 0.0540 0.0514 0.0052  0.0039  0.0078 145 CYS A N   
1115 C  CA  . CYS A 145 ? 0.0584 0.0561 0.0537 0.0052  0.0039  0.0077 145 CYS A CA  
1116 C  C   . CYS A 145 ? 0.0534 0.0510 0.0486 0.0053  0.0041  0.0076 145 CYS A C   
1117 O  O   . CYS A 145 ? 0.0631 0.0605 0.0581 0.0056  0.0044  0.0076 145 CYS A O   
1118 C  CB  . CYS A 145 ? 0.1022 0.0994 0.0969 0.0058  0.0043  0.0075 145 CYS A CB  
1119 S  SG  . CYS A 145 ? 0.2112 0.2084 0.2059 0.0057  0.0040  0.0075 145 CYS A SG  
1120 N  N   . GLY A 146 ? 0.0553 0.0528 0.0506 0.0049  0.0039  0.0077 146 GLY A N   
1121 C  CA  . GLY A 146 ? 0.0587 0.0561 0.0540 0.0049  0.0039  0.0077 146 GLY A CA  
1122 C  C   . GLY A 146 ? 0.0591 0.0568 0.0546 0.0042  0.0035  0.0079 146 GLY A C   
1123 O  O   . GLY A 146 ? 0.0714 0.0688 0.0667 0.0040  0.0034  0.0079 146 GLY A O   
1124 N  N   . SER A 147 ? 0.0618 0.0599 0.0576 0.0038  0.0031  0.0081 147 SER A N   
1125 C  CA  . SER A 147 ? 0.0722 0.0705 0.0682 0.0031  0.0026  0.0084 147 SER A CA  
1126 C  C   . SER A 147 ? 0.0832 0.0815 0.0792 0.0028  0.0024  0.0084 147 SER A C   
1127 O  O   . SER A 147 ? 0.0692 0.0676 0.0654 0.0029  0.0024  0.0083 147 SER A O   
1128 C  CB  . SER A 147 ? 0.0816 0.0805 0.0780 0.0029  0.0023  0.0085 147 SER A CB  
1129 O  OG  . SER A 147 ? 0.0770 0.0758 0.0732 0.0033  0.0027  0.0085 147 SER A OG  
1130 N  N   . VAL A 148 ? 0.0539 0.0521 0.0498 0.0023  0.0020  0.0085 148 VAL A N   
1131 C  CA  . VAL A 148 ? 0.0588 0.0570 0.0547 0.0020  0.0019  0.0086 148 VAL A CA  
1132 C  C   . VAL A 148 ? 0.0694 0.0679 0.0655 0.0014  0.0014  0.0088 148 VAL A C   
1133 O  O   . VAL A 148 ? 0.0487 0.0474 0.0448 0.0011  0.0012  0.0089 148 VAL A O   
1134 C  CB  . VAL A 148 ? 0.0636 0.0611 0.0590 0.0021  0.0021  0.0085 148 VAL A CB  
1135 C  CG1 . VAL A 148 ? 0.0708 0.0681 0.0661 0.0028  0.0026  0.0082 148 VAL A CG1 
1136 C  CG2 . VAL A 148 ? 0.0953 0.0924 0.0902 0.0017  0.0019  0.0086 148 VAL A CG2 
1137 N  N   . GLY A 149 ? 0.0711 0.0698 0.0676 0.0012  0.0012  0.0088 149 GLY A N   
1138 C  CA  . GLY A 149 ? 0.0579 0.0570 0.0546 0.0007  0.0009  0.0090 149 GLY A CA  
1139 C  C   . GLY A 149 ? 0.0771 0.0756 0.0732 0.0005  0.0009  0.0090 149 GLY A C   
1140 O  O   . GLY A 149 ? 0.0395 0.0375 0.0353 0.0008  0.0012  0.0088 149 GLY A O   
1141 N  N   . PHE A 150 ? 0.0636 0.0622 0.0597 0.0000  0.0006  0.0091 150 PHE A N   
1142 C  CA  . PHE A 150 ? 0.0594 0.0573 0.0547 -0.0002 0.0007  0.0091 150 PHE A CA  
1143 C  C   . PHE A 150 ? 0.0631 0.0615 0.0588 -0.0007 0.0003  0.0093 150 PHE A C   
1144 O  O   . PHE A 150 ? 0.0503 0.0496 0.0467 -0.0009 0.0000  0.0095 150 PHE A O   
1145 C  CB  . PHE A 150 ? 0.0558 0.0527 0.0501 -0.0001 0.0008  0.0090 150 PHE A CB  
1146 C  CG  . PHE A 150 ? 0.0513 0.0485 0.0457 -0.0003 0.0007  0.0091 150 PHE A CG  
1147 C  CD1 . PHE A 150 ? 0.0809 0.0786 0.0757 -0.0001 0.0007  0.0091 150 PHE A CD1 
1148 C  CD2 . PHE A 150 ? 0.0676 0.0648 0.0617 -0.0007 0.0005  0.0093 150 PHE A CD2 
1149 C  CE1 . PHE A 150 ? 0.0727 0.0707 0.0677 -0.0002 0.0006  0.0093 150 PHE A CE1 
1150 C  CE2 . PHE A 150 ? 0.0637 0.0614 0.0581 -0.0010 0.0003  0.0095 150 PHE A CE2 
1151 C  CZ  . PHE A 150 ? 0.0996 0.0977 0.0945 -0.0007 0.0003  0.0094 150 PHE A CZ  
1152 N  N   . ASN A 151 ? 0.0696 0.0674 0.0647 -0.0008 0.0004  0.0094 151 ASN A N   
1153 C  CA  . ASN A 151 ? 0.1116 0.1096 0.1067 -0.0013 0.0001  0.0096 151 ASN A CA  
1154 C  C   . ASN A 151 ? 0.1490 0.1457 0.1427 -0.0014 0.0004  0.0095 151 ASN A C   
1155 O  O   . ASN A 151 ? 0.1510 0.1465 0.1437 -0.0010 0.0007  0.0093 151 ASN A O   
1156 C  CB  . ASN A 151 ? 0.1441 0.1427 0.1398 -0.0015 -0.0001 0.0097 151 ASN A CB  
1157 C  CG  . ASN A 151 ? 0.1523 0.1524 0.1494 -0.0017 -0.0005 0.0098 151 ASN A CG  
1158 O  OD1 . ASN A 151 ? 0.1354 0.1365 0.1333 -0.0021 -0.0009 0.0100 151 ASN A OD1 
1159 N  ND2 . ASN A 151 ? 0.1293 0.1296 0.1269 -0.0013 -0.0003 0.0097 151 ASN A ND2 
1160 N  N   . ILE A 152 ? 0.1538 0.1506 0.1473 -0.0018 0.0001  0.0097 152 ILE A N   
1161 C  CA  . ILE A 152 ? 0.2166 0.2121 0.2088 -0.0019 0.0004  0.0097 152 ILE A CA  
1162 C  C   . ILE A 152 ? 0.2709 0.2666 0.2630 -0.0024 0.0002  0.0099 152 ILE A C   
1163 O  O   . ILE A 152 ? 0.2437 0.2406 0.2367 -0.0029 -0.0004 0.0101 152 ILE A O   
1164 C  CB  . ILE A 152 ? 0.2424 0.2380 0.2344 -0.0020 0.0004  0.0097 152 ILE A CB  
1165 C  CG1 . ILE A 152 ? 0.1724 0.1678 0.1645 -0.0016 0.0005  0.0095 152 ILE A CG1 
1166 C  CG2 . ILE A 152 ? 0.2529 0.2472 0.2435 -0.0020 0.0008  0.0097 152 ILE A CG2 
1167 C  CD1 . ILE A 152 ? 0.1230 0.1182 0.1147 -0.0016 0.0006  0.0096 152 ILE A CD1 
1168 N  N   . ASP A 153 ? 0.3177 0.3121 0.3087 -0.0022 0.0007  0.0098 153 ASP A N   
1169 C  CA  . ASP A 153 ? 0.3377 0.3321 0.3284 -0.0026 0.0006  0.0100 153 ASP A CA  
1170 C  C   . ASP A 153 ? 0.3172 0.3105 0.3068 -0.0026 0.0010  0.0101 153 ASP A C   
1171 O  O   . ASP A 153 ? 0.3205 0.3127 0.3093 -0.0020 0.0018  0.0101 153 ASP A O   
1172 C  CB  . ASP A 153 ? 0.3183 0.3125 0.3091 -0.0024 0.0008  0.0100 153 ASP A CB  
1173 C  CG  . ASP A 153 ? 0.4134 0.4089 0.4056 -0.0024 0.0004  0.0100 153 ASP A CG  
1174 O  OD1 . ASP A 153 ? 0.4210 0.4163 0.4133 -0.0019 0.0006  0.0098 153 ASP A OD1 
1175 O  OD2 . ASP A 153 ? 0.4562 0.4529 0.4493 -0.0029 -0.0002 0.0102 153 ASP A OD2 
1176 N  N   . TYR A 154 ? 0.3845 0.3784 0.3742 -0.0033 0.0006  0.0102 154 TYR A N   
1177 C  CA  . TYR A 154 ? 0.4214 0.4145 0.4101 -0.0034 0.0008  0.0103 154 TYR A CA  
1178 C  C   . TYR A 154 ? 0.4162 0.4088 0.4047 -0.0028 0.0013  0.0102 154 TYR A C   
1179 O  O   . TYR A 154 ? 0.5242 0.5174 0.5131 -0.0029 0.0009  0.0102 154 TYR A O   
1180 C  CB  . TYR A 154 ? 0.5043 0.4965 0.4923 -0.0032 0.0013  0.0104 154 TYR A CB  
1181 C  CG  . TYR A 154 ? 0.6068 0.5986 0.5940 -0.0037 0.0013  0.0105 154 TYR A CG  
1182 C  CD1 . TYR A 154 ? 0.6468 0.6388 0.6338 -0.0046 0.0007  0.0105 154 TYR A CD1 
1183 C  CD2 . TYR A 154 ? 0.6144 0.6054 0.6010 -0.0035 0.0019  0.0107 154 TYR A CD2 
1184 C  CE1 . TYR A 154 ? 0.7286 0.7200 0.7146 -0.0052 0.0006  0.0105 154 TYR A CE1 
1185 C  CE2 . TYR A 154 ? 0.6898 0.6802 0.6755 -0.0041 0.0018  0.0106 154 TYR A CE2 
1186 C  CZ  . TYR A 154 ? 0.8144 0.8048 0.7996 -0.0049 0.0012  0.0105 154 TYR A CZ  
1187 O  OH  . TYR A 154 ? 0.7788 0.7684 0.7629 -0.0056 0.0011  0.0104 154 TYR A OH  
1188 N  N   . ASP A 155 ? 0.3268 0.3187 0.3150 -0.0020 0.0021  0.0103 155 ASP A N   
1189 C  CA  . ASP A 155 ? 0.3793 0.3711 0.3676 -0.0014 0.0024  0.0101 155 ASP A CA  
1190 C  C   . ASP A 155 ? 0.2873 0.2786 0.2757 -0.0006 0.0028  0.0095 155 ASP A C   
1191 O  O   . ASP A 155 ? 0.2451 0.2361 0.2334 -0.0001 0.0031  0.0092 155 ASP A O   
1192 C  CB  . ASP A 155 ? 0.3669 0.3589 0.3553 -0.0015 0.0026  0.0105 155 ASP A CB  
1193 C  CG  . ASP A 155 ? 0.4071 0.3995 0.3959 -0.0015 0.0027  0.0107 155 ASP A CG  
1194 O  OD1 . ASP A 155 ? 0.4131 0.4050 0.4014 -0.0017 0.0027  0.0107 155 ASP A OD1 
1195 O  OD2 . ASP A 155 ? 0.3436 0.3365 0.3329 -0.0017 0.0025  0.0109 155 ASP A OD2 
1196 N  N   . CYS A 156 ? 0.2409 0.2317 0.2290 -0.0008 0.0026  0.0092 156 CYS A N   
1197 C  CA  . CYS A 156 ? 0.2313 0.2211 0.2184 -0.0016 0.0018  0.0086 156 CYS A CA  
1198 C  C   . CYS A 156 ? 0.2585 0.2495 0.2468 -0.0013 0.0016  0.0088 156 CYS A C   
1199 O  O   . CYS A 156 ? 0.1570 0.1489 0.1461 -0.0013 0.0016  0.0092 156 CYS A O   
1200 C  CB  . CYS A 156 ? 0.1786 0.1684 0.1658 -0.0020 0.0016  0.0086 156 CYS A CB  
1201 S  SG  . CYS A 156 ? 0.2364 0.2280 0.2254 -0.0019 0.0013  0.0091 156 CYS A SG  
1202 N  N   . VAL A 157 ? 0.1815 0.1730 0.1702 -0.0014 0.0013  0.0088 157 VAL A N   
1203 C  CA  . VAL A 157 ? 0.1333 0.1257 0.1230 -0.0011 0.0012  0.0089 157 VAL A CA  
1204 C  C   . VAL A 157 ? 0.1366 0.1298 0.1273 -0.0008 0.0013  0.0089 157 VAL A C   
1205 O  O   . VAL A 157 ? 0.1408 0.1340 0.1317 -0.0006 0.0014  0.0090 157 VAL A O   
1206 C  CB  . VAL A 157 ? 0.1166 0.1093 0.1066 -0.0009 0.0012  0.0089 157 VAL A CB  
1207 C  CG1 . VAL A 157 ? 0.0717 0.0656 0.0630 -0.0005 0.0012  0.0089 157 VAL A CG1 
1208 C  CG2 . VAL A 157 ? 0.1227 0.1147 0.1118 -0.0012 0.0012  0.0088 157 VAL A CG2 
1209 N  N   . SER A 158 ? 0.1399 0.1339 0.1315 -0.0007 0.0012  0.0090 158 SER A N   
1210 C  CA  . SER A 158 ? 0.1052 0.0999 0.0977 -0.0003 0.0012  0.0090 158 SER A CA  
1211 C  C   . SER A 158 ? 0.0765 0.0722 0.0700 0.0000  0.0012  0.0090 158 SER A C   
1212 O  O   . SER A 158 ? 0.0542 0.0506 0.0484 -0.0001 0.0010  0.0090 158 SER A O   
1213 C  CB  . SER A 158 ? 0.1196 0.1147 0.1125 -0.0005 0.0011  0.0092 158 SER A CB  
1214 O  OG  . SER A 158 ? 0.1982 0.1924 0.1903 -0.0007 0.0013  0.0092 158 SER A OG  
1215 N  N   . PHE A 159 ? 0.0843 0.0799 0.0779 0.0005  0.0015  0.0088 159 PHE A N   
1216 C  CA  . PHE A 159 ? 0.0892 0.0855 0.0836 0.0009  0.0016  0.0088 159 PHE A CA  
1217 C  C   . PHE A 159 ? 0.0693 0.0663 0.0645 0.0010  0.0016  0.0088 159 PHE A C   
1218 O  O   . PHE A 159 ? 0.0799 0.0768 0.0751 0.0013  0.0018  0.0088 159 PHE A O   
1219 C  CB  . PHE A 159 ? 0.0852 0.0813 0.0795 0.0014  0.0020  0.0086 159 PHE A CB  
1220 C  CG  . PHE A 159 ? 0.0892 0.0849 0.0830 0.0013  0.0020  0.0086 159 PHE A CG  
1221 C  CD1 . PHE A 159 ? 0.0607 0.0566 0.0545 0.0012  0.0019  0.0086 159 PHE A CD1 
1222 C  CD2 . PHE A 159 ? 0.0595 0.0545 0.0526 0.0012  0.0022  0.0086 159 PHE A CD2 
1223 C  CE1 . PHE A 159 ? 0.0688 0.0642 0.0620 0.0011  0.0019  0.0086 159 PHE A CE1 
1224 C  CE2 . PHE A 159 ? 0.0984 0.0929 0.0909 0.0010  0.0022  0.0086 159 PHE A CE2 
1225 C  CZ  . PHE A 159 ? 0.0674 0.0621 0.0600 0.0010  0.0020  0.0086 159 PHE A CZ  
1226 N  N   . CYS A 160 ? 0.0579 0.0556 0.0538 0.0009  0.0014  0.0088 160 CYS A N   
1227 C  CA  . CYS A 160 ? 0.0762 0.0745 0.0728 0.0010  0.0013  0.0089 160 CYS A CA  
1228 C  C   . CYS A 160 ? 0.0745 0.0732 0.0716 0.0013  0.0014  0.0088 160 CYS A C   
1229 O  O   . CYS A 160 ? 0.1067 0.1058 0.1042 0.0014  0.0014  0.0089 160 CYS A O   
1230 C  CB  . CYS A 160 ? 0.0613 0.0603 0.0584 0.0006  0.0009  0.0091 160 CYS A CB  
1231 S  SG  . CYS A 160 ? 0.0975 0.0971 0.0950 0.0002  0.0006  0.0092 160 CYS A SG  
1232 N  N   . TYR A 161 ? 0.0597 0.0583 0.0565 0.0014  0.0015  0.0087 161 TYR A N   
1233 C  CA  . TYR A 161 ? 0.0542 0.0531 0.0513 0.0017  0.0015  0.0087 161 TYR A CA  
1234 C  C   . TYR A 161 ? 0.0461 0.0446 0.0428 0.0021  0.0018  0.0085 161 TYR A C   
1235 O  O   . TYR A 161 ? 0.0639 0.0623 0.0603 0.0020  0.0018  0.0085 161 TYR A O   
1236 C  CB  . TYR A 161 ? 0.0569 0.0565 0.0545 0.0013  0.0012  0.0088 161 TYR A CB  
1237 C  CG  . TYR A 161 ? 0.0584 0.0582 0.0562 0.0015  0.0012  0.0088 161 TYR A CG  
1238 C  CD1 . TYR A 161 ? 0.0553 0.0553 0.0535 0.0016  0.0011  0.0088 161 TYR A CD1 
1239 C  CD2 . TYR A 161 ? 0.0420 0.0417 0.0396 0.0017  0.0013  0.0087 161 TYR A CD2 
1240 C  CE1 . TYR A 161 ? 0.0383 0.0383 0.0364 0.0017  0.0012  0.0088 161 TYR A CE1 
1241 C  CE2 . TYR A 161 ? 0.0161 0.0159 0.0138 0.0019  0.0013  0.0087 161 TYR A CE2 
1242 C  CZ  . TYR A 161 ? 0.0586 0.0585 0.0566 0.0019  0.0013  0.0087 161 TYR A CZ  
1243 O  OH  . TYR A 161 ? 0.0565 0.0564 0.0544 0.0021  0.0013  0.0087 161 TYR A OH  
1244 N  N   . MET A 162 ? 0.0551 0.0536 0.0519 0.0025  0.0021  0.0084 162 MET A N   
1245 C  CA  . MET A 162 ? 0.0526 0.0508 0.0490 0.0030  0.0025  0.0082 162 MET A CA  
1246 C  C   . MET A 162 ? 0.0563 0.0547 0.0529 0.0031  0.0024  0.0082 162 MET A C   
1247 O  O   . MET A 162 ? 0.0214 0.0199 0.0181 0.0031  0.0023  0.0082 162 MET A O   
1248 C  CB  . MET A 162 ? 0.0364 0.0342 0.0325 0.0035  0.0030  0.0081 162 MET A CB  
1249 C  CG  . MET A 162 ? 0.0399 0.0375 0.0357 0.0041  0.0034  0.0078 162 MET A CG  
1250 S  SD  . MET A 162 ? 0.1137 0.1107 0.1090 0.0048  0.0040  0.0076 162 MET A SD  
1251 C  CE  . MET A 162 ? 0.1055 0.1024 0.1007 0.0045  0.0039  0.0077 162 MET A CE  
1252 N  N   . HIS A 163 ? 0.0328 0.0313 0.0293 0.0032  0.0025  0.0082 163 HIS A N   
1253 C  CA  . HIS A 163 ? 0.0524 0.0510 0.0490 0.0032  0.0024  0.0082 163 HIS A CA  
1254 C  C   . HIS A 163 ? 0.0391 0.0374 0.0353 0.0039  0.0028  0.0080 163 HIS A C   
1255 O  O   . HIS A 163 ? 0.0176 0.0155 0.0134 0.0043  0.0032  0.0079 163 HIS A O   
1256 C  CB  . HIS A 163 ? 0.0503 0.0492 0.0470 0.0031  0.0023  0.0084 163 HIS A CB  
1257 C  CG  . HIS A 163 ? 0.0624 0.0615 0.0592 0.0031  0.0022  0.0084 163 HIS A CG  
1258 N  ND1 . HIS A 163 ? 0.0666 0.0658 0.0636 0.0029  0.0019  0.0085 163 HIS A ND1 
1259 C  CD2 . HIS A 163 ? 0.0914 0.0904 0.0880 0.0034  0.0024  0.0084 163 HIS A CD2 
1260 C  CE1 . HIS A 163 ? 0.0639 0.0632 0.0609 0.0030  0.0019  0.0085 163 HIS A CE1 
1261 N  NE2 . HIS A 163 ? 0.0877 0.0869 0.0844 0.0034  0.0022  0.0085 163 HIS A NE2 
1262 N  N   . HIS A 164 ? 0.0352 0.0333 0.0313 0.0038  0.0027  0.0080 164 HIS A N   
1263 C  CA  . HIS A 164 ? 0.0741 0.0717 0.0696 0.0044  0.0030  0.0079 164 HIS A CA  
1264 C  C   . HIS A 164 ? 0.0888 0.0863 0.0841 0.0045  0.0030  0.0079 164 HIS A C   
1265 O  O   . HIS A 164 ? 0.1167 0.1138 0.1115 0.0050  0.0033  0.0077 164 HIS A O   
1266 C  CB  . HIS A 164 ? 0.0411 0.0385 0.0366 0.0043  0.0029  0.0079 164 HIS A CB  
1267 C  CG  . HIS A 164 ? 0.0377 0.0350 0.0332 0.0046  0.0032  0.0078 164 HIS A CG  
1268 N  ND1 . HIS A 164 ? 0.0491 0.0467 0.0449 0.0043  0.0031  0.0079 164 HIS A ND1 
1269 C  CD2 . HIS A 164 ? 0.0306 0.0275 0.0257 0.0051  0.0037  0.0076 164 HIS A CD2 
1270 C  CE1 . HIS A 164 ? 0.0631 0.0605 0.0588 0.0046  0.0035  0.0077 164 HIS A CE1 
1271 N  NE2 . HIS A 164 ? 0.0737 0.0707 0.0689 0.0051  0.0038  0.0076 164 HIS A NE2 
1272 N  N   . MET A 165 ? 0.0960 0.0938 0.0917 0.0040  0.0025  0.0080 165 MET A N   
1273 C  CA  . MET A 165 ? 0.1249 0.1224 0.1202 0.0042  0.0025  0.0080 165 MET A CA  
1274 C  C   . MET A 165 ? 0.1153 0.1132 0.1110 0.0037  0.0021  0.0082 165 MET A C   
1275 O  O   . MET A 165 ? 0.0646 0.0630 0.0609 0.0032  0.0018  0.0084 165 MET A O   
1276 C  CB  . MET A 165 ? 0.1157 0.1126 0.1104 0.0044  0.0025  0.0079 165 MET A CB  
1277 C  CG  . MET A 165 ? 0.1268 0.1238 0.1218 0.0039  0.0021  0.0081 165 MET A CG  
1278 S  SD  . MET A 165 ? 0.2259 0.2221 0.2203 0.0041  0.0021  0.0080 165 MET A SD  
1279 C  CE  . MET A 165 ? 0.1398 0.1363 0.1347 0.0035  0.0015  0.0082 165 MET A CE  
1280 N  N   . GLU A 166 ? 0.0947 0.0924 0.0901 0.0039  0.0021  0.0082 166 GLU A N   
1281 C  CA  . GLU A 166 ? 0.1091 0.1071 0.1048 0.0035  0.0017  0.0084 166 GLU A CA  
1282 C  C   . GLU A 166 ? 0.1308 0.1282 0.1260 0.0035  0.0015  0.0084 166 GLU A C   
1283 O  O   . GLU A 166 ? 0.0971 0.0938 0.0915 0.0040  0.0018  0.0083 166 GLU A O   
1284 C  CB  . GLU A 166 ? 0.0987 0.0970 0.0945 0.0037  0.0019  0.0085 166 GLU A CB  
1285 C  CG  . GLU A 166 ? 0.1176 0.1163 0.1138 0.0033  0.0016  0.0087 166 GLU A CG  
1286 C  CD  . GLU A 166 ? 0.1683 0.1674 0.1647 0.0035  0.0018  0.0088 166 GLU A CD  
1287 O  OE1 . GLU A 166 ? 0.1206 0.1203 0.1175 0.0033  0.0018  0.0089 166 GLU A OE1 
1288 O  OE2 . GLU A 166 ? 0.2709 0.2698 0.2670 0.0037  0.0019  0.0088 166 GLU A OE2 
1289 N  N   . LEU A 167 ? 0.1100 0.1076 0.1055 0.0031  0.0011  0.0086 167 LEU A N   
1290 C  CA  . LEU A 167 ? 0.1444 0.1413 0.1394 0.0030  0.0008  0.0086 167 LEU A CA  
1291 C  C   . LEU A 167 ? 0.1666 0.1633 0.1612 0.0031  0.0008  0.0086 167 LEU A C   
1292 O  O   . LEU A 167 ? 0.1063 0.1035 0.1013 0.0031  0.0009  0.0087 167 LEU A O   
1293 C  CB  . LEU A 167 ? 0.1373 0.1345 0.1327 0.0025  0.0004  0.0087 167 LEU A CB  
1294 C  CG  . LEU A 167 ? 0.1735 0.1711 0.1695 0.0024  0.0005  0.0087 167 LEU A CG  
1295 C  CD1 . LEU A 167 ? 0.2170 0.2150 0.2135 0.0019  0.0001  0.0088 167 LEU A CD1 
1296 C  CD2 . LEU A 167 ? 0.1971 0.1941 0.1924 0.0027  0.0007  0.0085 167 LEU A CD2 
1297 N  N   . PRO A 168 ? 0.1737 0.1697 0.1677 0.0032  0.0006  0.0086 168 PRO A N   
1298 C  CA  . PRO A 168 ? 0.1214 0.1171 0.1150 0.0033  0.0005  0.0087 168 PRO A CA  
1299 C  C   . PRO A 168 ? 0.1532 0.1495 0.1475 0.0029  0.0003  0.0089 168 PRO A C   
1300 O  O   . PRO A 168 ? 0.2117 0.2081 0.2059 0.0031  0.0004  0.0089 168 PRO A O   
1301 C  CB  . PRO A 168 ? 0.2280 0.2227 0.2208 0.0033  0.0002  0.0087 168 PRO A CB  
1302 C  CG  . PRO A 168 ? 0.2133 0.2077 0.2059 0.0033  0.0001  0.0086 168 PRO A CG  
1303 C  CD  . PRO A 168 ? 0.1634 0.1585 0.1567 0.0033  0.0005  0.0085 168 PRO A CD  
1304 N  N   . THR A 169 ? 0.1629 0.1598 0.1579 0.0025  0.0001  0.0089 169 THR A N   
1305 C  CA  . THR A 169 ? 0.1383 0.1361 0.1342 0.0022  0.0000  0.0091 169 THR A CA  
1306 C  C   . THR A 169 ? 0.1799 0.1788 0.1767 0.0021  0.0002  0.0092 169 THR A C   
1307 O  O   . THR A 169 ? 0.1966 0.1965 0.1943 0.0018  0.0001  0.0094 169 THR A O   
1308 C  CB  . THR A 169 ? 0.1662 0.1646 0.1628 0.0017  -0.0003 0.0092 169 THR A CB  
1309 O  OG1 . THR A 169 ? 0.2077 0.2063 0.2046 0.0017  -0.0002 0.0091 169 THR A OG1 
1310 C  CG2 . THR A 169 ? 0.2061 0.2034 0.2018 0.0018  -0.0006 0.0092 169 THR A CG2 
1311 N  N   . GLY A 170 ? 0.1650 0.1637 0.1615 0.0024  0.0005  0.0091 170 GLY A N   
1312 C  CA  . GLY A 170 ? 0.1433 0.1429 0.1405 0.0023  0.0007  0.0092 170 GLY A CA  
1313 C  C   . GLY A 170 ? 0.1582 0.1586 0.1562 0.0020  0.0006  0.0092 170 GLY A C   
1314 O  O   . GLY A 170 ? 0.1648 0.1659 0.1635 0.0018  0.0006  0.0094 170 GLY A O   
1315 N  N   . VAL A 171 ? 0.1716 0.1718 0.1696 0.0018  0.0004  0.0092 171 VAL A N   
1316 C  CA  . VAL A 171 ? 0.1784 0.1793 0.1772 0.0015  0.0003  0.0092 171 VAL A CA  
1317 C  C   . VAL A 171 ? 0.1457 0.1458 0.1438 0.0019  0.0006  0.0090 171 VAL A C   
1318 O  O   . VAL A 171 ? 0.1295 0.1288 0.1267 0.0023  0.0008  0.0089 171 VAL A O   
1319 C  CB  . VAL A 171 ? 0.1564 0.1578 0.1558 0.0011  0.0000  0.0093 171 VAL A CB  
1320 C  CG1 . VAL A 171 ? 0.2121 0.2143 0.2123 0.0008  -0.0003 0.0096 171 VAL A CG1 
1321 C  CG2 . VAL A 171 ? 0.1060 0.1064 0.1046 0.0013  0.0000  0.0092 171 VAL A CG2 
1322 N  N   . HIS A 172 ? 0.0873 0.0879 0.0858 0.0017  0.0006  0.0090 172 HIS A N   
1323 C  CA  . HIS A 172 ? 0.0754 0.0755 0.0734 0.0020  0.0009  0.0089 172 HIS A CA  
1324 C  C   . HIS A 172 ? 0.0658 0.0658 0.0639 0.0019  0.0008  0.0088 172 HIS A C   
1325 O  O   . HIS A 172 ? 0.0889 0.0895 0.0877 0.0015  0.0006  0.0090 172 HIS A O   
1326 C  CB  . HIS A 172 ? 0.0602 0.0607 0.0585 0.0019  0.0010  0.0089 172 HIS A CB  
1327 C  CG  . HIS A 172 ? 0.0777 0.0783 0.0760 0.0020  0.0010  0.0090 172 HIS A CG  
1328 N  ND1 . HIS A 172 ? 0.0693 0.0707 0.0683 0.0017  0.0008  0.0092 172 HIS A ND1 
1329 C  CD2 . HIS A 172 ? 0.1118 0.1119 0.1095 0.0025  0.0013  0.0089 172 HIS A CD2 
1330 C  CE1 . HIS A 172 ? 0.1085 0.1099 0.1073 0.0019  0.0009  0.0093 172 HIS A CE1 
1331 N  NE2 . HIS A 172 ? 0.1138 0.1144 0.1119 0.0024  0.0013  0.0091 172 HIS A NE2 
1332 N  N   . ALA A 173 ? 0.0346 0.0340 0.0321 0.0023  0.0011  0.0087 173 ALA A N   
1333 C  CA  . ALA A 173 ? 0.0514 0.0506 0.0489 0.0023  0.0011  0.0086 173 ALA A CA  
1334 C  C   . ALA A 173 ? 0.0720 0.0709 0.0692 0.0026  0.0015  0.0085 173 ALA A C   
1335 O  O   . ALA A 173 ? 0.0723 0.0709 0.0690 0.0029  0.0018  0.0084 173 ALA A O   
1336 C  CB  . ALA A 173 ? 0.0761 0.0746 0.0730 0.0024  0.0011  0.0086 173 ALA A CB  
1337 N  N   . GLY A 174 ? 0.0255 0.0245 0.0228 0.0025  0.0015  0.0085 174 GLY A N   
1338 C  CA  . GLY A 174 ? 0.0746 0.0734 0.0717 0.0028  0.0018  0.0084 174 GLY A CA  
1339 C  C   . GLY A 174 ? 0.0497 0.0485 0.0470 0.0027  0.0018  0.0085 174 GLY A C   
1340 O  O   . GLY A 174 ? 0.0559 0.0549 0.0535 0.0025  0.0016  0.0086 174 GLY A O   
1341 N  N   . THR A 175 ? 0.0235 0.0221 0.0206 0.0029  0.0021  0.0084 175 THR A N   
1342 C  CA  . THR A 175 ? 0.0621 0.0607 0.0593 0.0030  0.0023  0.0084 175 THR A CA  
1343 C  C   . THR A 175 ? 0.0483 0.0469 0.0456 0.0027  0.0022  0.0085 175 THR A C   
1344 O  O   . THR A 175 ? 0.0183 0.0170 0.0155 0.0026  0.0021  0.0085 175 THR A O   
1345 C  CB  . THR A 175 ? 0.0498 0.0479 0.0465 0.0036  0.0027  0.0082 175 THR A CB  
1346 O  OG1 . THR A 175 ? 0.0445 0.0423 0.0409 0.0038  0.0031  0.0081 175 THR A OG1 
1347 C  CG2 . THR A 175 ? 0.0487 0.0465 0.0451 0.0039  0.0028  0.0081 175 THR A CG2 
1348 N  N   . ASP A 176 ? 0.0656 0.0643 0.0630 0.0027  0.0022  0.0086 176 ASP A N   
1349 C  CA  . ASP A 176 ? 0.0612 0.0597 0.0585 0.0026  0.0023  0.0086 176 ASP A CA  
1350 C  C   . ASP A 176 ? 0.0594 0.0574 0.0562 0.0031  0.0028  0.0084 176 ASP A C   
1351 O  O   . ASP A 176 ? 0.0686 0.0665 0.0652 0.0035  0.0030  0.0082 176 ASP A O   
1352 C  CB  . ASP A 176 ? 0.0976 0.0963 0.0952 0.0024  0.0022  0.0087 176 ASP A CB  
1353 C  CG  . ASP A 176 ? 0.1397 0.1384 0.1375 0.0028  0.0025  0.0087 176 ASP A CG  
1354 O  OD1 . ASP A 176 ? 0.1241 0.1224 0.1214 0.0033  0.0029  0.0086 176 ASP A OD1 
1355 O  OD2 . ASP A 176 ? 0.1212 0.1201 0.1193 0.0026  0.0024  0.0089 176 ASP A OD2 
1356 N  N   . LEU A 177 ? 0.0556 0.0533 0.0521 0.0031  0.0029  0.0084 177 LEU A N   
1357 C  CA  . LEU A 177 ? 0.1176 0.1148 0.1136 0.0036  0.0034  0.0082 177 LEU A CA  
1358 C  C   . LEU A 177 ? 0.0995 0.0965 0.0955 0.0041  0.0039  0.0081 177 LEU A C   
1359 O  O   . LEU A 177 ? 0.0699 0.0665 0.0655 0.0046  0.0044  0.0079 177 LEU A O   
1360 C  CB  . LEU A 177 ? 0.0827 0.0796 0.0783 0.0033  0.0033  0.0082 177 LEU A CB  
1361 C  CG  . LEU A 177 ? 0.0772 0.0740 0.0726 0.0031  0.0031  0.0082 177 LEU A CG  
1362 C  CD1 . LEU A 177 ? 0.1032 0.0999 0.0984 0.0037  0.0036  0.0080 177 LEU A CD1 
1363 C  CD2 . LEU A 177 ? 0.0851 0.0824 0.0808 0.0026  0.0026  0.0083 177 LEU A CD2 
1364 N  N   . GLU A 178 ? 0.0706 0.0679 0.0670 0.0040  0.0038  0.0082 178 GLU A N   
1365 C  CA  . GLU A 178 ? 0.1309 0.1282 0.1274 0.0045  0.0042  0.0082 178 GLU A CA  
1366 C  C   . GLU A 178 ? 0.1164 0.1138 0.1129 0.0047  0.0042  0.0081 178 GLU A C   
1367 O  O   . GLU A 178 ? 0.1509 0.1482 0.1474 0.0050  0.0044  0.0081 178 GLU A O   
1368 C  CB  . GLU A 178 ? 0.1649 0.1624 0.1617 0.0044  0.0042  0.0084 178 GLU A CB  
1369 C  CG  . GLU A 178 ? 0.2099 0.2071 0.2066 0.0042  0.0042  0.0085 178 GLU A CG  
1370 C  CD  . GLU A 178 ? 0.3564 0.3538 0.3535 0.0043  0.0043  0.0087 178 GLU A CD  
1371 O  OE1 . GLU A 178 ? 0.3938 0.3907 0.3905 0.0045  0.0047  0.0086 178 GLU A OE1 
1372 O  OE2 . GLU A 178 ? 0.3705 0.3683 0.3681 0.0040  0.0041  0.0089 178 GLU A OE2 
1373 N  N   . GLY A 179 ? 0.0647 0.0622 0.0612 0.0045  0.0039  0.0081 179 GLY A N   
1374 C  CA  . GLY A 179 ? 0.0883 0.0857 0.0845 0.0046  0.0039  0.0080 179 GLY A CA  
1375 C  C   . GLY A 179 ? 0.0842 0.0819 0.0809 0.0043  0.0035  0.0082 179 GLY A C   
1376 O  O   . GLY A 179 ? 0.0657 0.0632 0.0621 0.0044  0.0034  0.0082 179 GLY A O   
1377 N  N   . ASN A 180 ? 0.0862 0.0843 0.0834 0.0039  0.0031  0.0084 180 ASN A N   
1378 C  CA  . ASN A 180 ? 0.0634 0.0617 0.0609 0.0035  0.0027  0.0086 180 ASN A CA  
1379 C  C   . ASN A 180 ? 0.0848 0.0833 0.0824 0.0031  0.0023  0.0086 180 ASN A C   
1380 O  O   . ASN A 180 ? 0.0716 0.0704 0.0694 0.0029  0.0022  0.0087 180 ASN A O   
1381 C  CB  . ASN A 180 ? 0.1119 0.1106 0.1099 0.0033  0.0027  0.0088 180 ASN A CB  
1382 C  CG  . ASN A 180 ? 0.1356 0.1341 0.1335 0.0037  0.0031  0.0089 180 ASN A CG  
1383 O  OD1 . ASN A 180 ? 0.0873 0.0857 0.0852 0.0039  0.0032  0.0089 180 ASN A OD1 
1384 N  ND2 . ASN A 180 ? 0.1901 0.1886 0.1880 0.0038  0.0033  0.0088 180 ASN A ND2 
1385 N  N   . PHE A 181 ? 0.0734 0.0717 0.0708 0.0031  0.0021  0.0086 181 PHE A N   
1386 C  CA  . PHE A 181 ? 0.0600 0.0585 0.0575 0.0028  0.0018  0.0087 181 PHE A CA  
1387 C  C   . PHE A 181 ? 0.0828 0.0820 0.0811 0.0023  0.0015  0.0089 181 PHE A C   
1388 O  O   . PHE A 181 ? 0.0936 0.0931 0.0923 0.0022  0.0014  0.0090 181 PHE A O   
1389 C  CB  . PHE A 181 ? 0.0866 0.0847 0.0837 0.0029  0.0017  0.0086 181 PHE A CB  
1390 C  CG  . PHE A 181 ? 0.0721 0.0698 0.0686 0.0032  0.0019  0.0084 181 PHE A CG  
1391 C  CD1 . PHE A 181 ? 0.0475 0.0454 0.0441 0.0030  0.0017  0.0084 181 PHE A CD1 
1392 C  CD2 . PHE A 181 ? 0.0852 0.0825 0.0812 0.0037  0.0022  0.0083 181 PHE A CD2 
1393 C  CE1 . PHE A 181 ? 0.0672 0.0648 0.0633 0.0034  0.0019  0.0083 181 PHE A CE1 
1394 C  CE2 . PHE A 181 ? 0.0462 0.0432 0.0417 0.0041  0.0025  0.0081 181 PHE A CE2 
1395 C  CZ  . PHE A 181 ? 0.0707 0.0678 0.0662 0.0039  0.0024  0.0081 181 PHE A CZ  
1396 N  N   . TYR A 182 ? 0.0740 0.0736 0.0725 0.0021  0.0013  0.0089 182 TYR A N   
1397 C  CA  . TYR A 182 ? 0.0972 0.0975 0.0965 0.0016  0.0009  0.0091 182 TYR A CA  
1398 C  C   . TYR A 182 ? 0.0854 0.0856 0.0847 0.0015  0.0007  0.0091 182 TYR A C   
1399 O  O   . TYR A 182 ? 0.0956 0.0954 0.0944 0.0017  0.0007  0.0090 182 TYR A O   
1400 C  CB  . TYR A 182 ? 0.0874 0.0880 0.0869 0.0014  0.0008  0.0091 182 TYR A CB  
1401 C  CG  . TYR A 182 ? 0.1166 0.1173 0.1161 0.0013  0.0009  0.0091 182 TYR A CG  
1402 C  CD1 . TYR A 182 ? 0.0998 0.1009 0.0997 0.0011  0.0008  0.0093 182 TYR A CD1 
1403 C  CD2 . TYR A 182 ? 0.0812 0.0814 0.0801 0.0016  0.0011  0.0089 182 TYR A CD2 
1404 C  CE1 . TYR A 182 ? 0.1382 0.1391 0.1378 0.0011  0.0009  0.0093 182 TYR A CE1 
1405 C  CE2 . TYR A 182 ? 0.0772 0.0772 0.0758 0.0015  0.0012  0.0089 182 TYR A CE2 
1406 C  CZ  . TYR A 182 ? 0.1204 0.1207 0.1193 0.0013  0.0011  0.0091 182 TYR A CZ  
1407 O  OH  . TYR A 182 ? 0.1061 0.1060 0.1046 0.0012  0.0011  0.0091 182 TYR A OH  
1408 N  N   . GLY A 183 ? 0.0928 0.0934 0.0926 0.0013  0.0005  0.0093 183 GLY A N   
1409 C  CA  . GLY A 183 ? 0.1190 0.1196 0.1189 0.0011  0.0002  0.0094 183 GLY A CA  
1410 C  C   . GLY A 183 ? 0.1458 0.1454 0.1448 0.0015  0.0003  0.0093 183 GLY A C   
1411 O  O   . GLY A 183 ? 0.1310 0.1302 0.1296 0.0018  0.0005  0.0092 183 GLY A O   
1412 N  N   . PRO A 184 ? 0.1491 0.1484 0.1478 0.0014  0.0000  0.0093 184 PRO A N   
1413 C  CA  . PRO A 184 ? 0.1883 0.1866 0.1862 0.0016  0.0000  0.0092 184 PRO A CA  
1414 C  C   . PRO A 184 ? 0.1414 0.1387 0.1382 0.0020  0.0001  0.0090 184 PRO A C   
1415 O  O   . PRO A 184 ? 0.2138 0.2103 0.2098 0.0021  0.0000  0.0090 184 PRO A O   
1416 C  CB  . PRO A 184 ? 0.1472 0.1454 0.1452 0.0014  -0.0004 0.0094 184 PRO A CB  
1417 C  CG  . PRO A 184 ? 0.1256 0.1243 0.1239 0.0012  -0.0005 0.0093 184 PRO A CG  
1418 C  CD  . PRO A 184 ? 0.1302 0.1299 0.1293 0.0011  -0.0003 0.0094 184 PRO A CD  
1419 N  N   . PHE A 185 ? 0.0925 0.0900 0.0892 0.0022  0.0004  0.0089 185 PHE A N   
1420 C  CA  . PHE A 185 ? 0.1536 0.1504 0.1495 0.0025  0.0006  0.0087 185 PHE A CA  
1421 C  C   . PHE A 185 ? 0.1506 0.1470 0.1460 0.0029  0.0009  0.0086 185 PHE A C   
1422 O  O   . PHE A 185 ? 0.0943 0.0911 0.0901 0.0029  0.0011  0.0086 185 PHE A O   
1423 C  CB  . PHE A 185 ? 0.1535 0.1507 0.1496 0.0025  0.0007  0.0086 185 PHE A CB  
1424 C  CG  . PHE A 185 ? 0.1574 0.1551 0.1540 0.0021  0.0004  0.0087 185 PHE A CG  
1425 C  CD1 . PHE A 185 ? 0.1276 0.1250 0.1239 0.0020  0.0002  0.0088 185 PHE A CD1 
1426 C  CD2 . PHE A 185 ? 0.0936 0.0923 0.0912 0.0018  0.0004  0.0089 185 PHE A CD2 
1427 C  CE1 . PHE A 185 ? 0.1665 0.1645 0.1635 0.0017  0.0000  0.0089 185 PHE A CE1 
1428 C  CE2 . PHE A 185 ? 0.0981 0.0975 0.0964 0.0015  0.0002  0.0090 185 PHE A CE2 
1429 C  CZ  . PHE A 185 ? 0.1142 0.1133 0.1122 0.0014  0.0000  0.0090 185 PHE A CZ  
1430 N  N   . VAL A 186 ? 0.1111 0.1069 0.1058 0.0032  0.0010  0.0085 186 VAL A N   
1431 C  CA  . VAL A 186 ? 0.1154 0.1108 0.1097 0.0037  0.0014  0.0084 186 VAL A CA  
1432 C  C   . VAL A 186 ? 0.1326 0.1279 0.1265 0.0042  0.0018  0.0081 186 VAL A C   
1433 O  O   . VAL A 186 ? 0.1300 0.1252 0.1237 0.0041  0.0017  0.0081 186 VAL A O   
1434 C  CB  . VAL A 186 ? 0.1637 0.1584 0.1574 0.0038  0.0012  0.0084 186 VAL A CB  
1435 C  CG1 . VAL A 186 ? 0.1400 0.1349 0.1341 0.0034  0.0008  0.0087 186 VAL A CG1 
1436 C  CG2 . VAL A 186 ? 0.1690 0.1632 0.1622 0.0037  0.0008  0.0085 186 VAL A CG2 
1437 N  N   . ASP A 187 ? 0.0889 0.0842 0.0826 0.0047  0.0024  0.0079 187 ASP A N   
1438 C  CA  . ASP A 187 ? 0.1255 0.1206 0.1187 0.0052  0.0028  0.0077 187 ASP A CA  
1439 C  C   . ASP A 187 ? 0.1271 0.1214 0.1194 0.0056  0.0030  0.0075 187 ASP A C   
1440 O  O   . ASP A 187 ? 0.1468 0.1406 0.1385 0.0062  0.0035  0.0073 187 ASP A O   
1441 C  CB  . ASP A 187 ? 0.0670 0.0623 0.0604 0.0055  0.0034  0.0075 187 ASP A CB  
1442 C  CG  . ASP A 187 ? 0.0940 0.0892 0.0874 0.0057  0.0036  0.0075 187 ASP A CG  
1443 O  OD1 . ASP A 187 ? 0.0848 0.0798 0.0782 0.0055  0.0033  0.0077 187 ASP A OD1 
1444 O  OD2 . ASP A 187 ? 0.0459 0.0411 0.0392 0.0060  0.0041  0.0074 187 ASP A OD2 
1445 N  N   . ARG A 188 ? 0.1259 0.1198 0.1179 0.0054  0.0026  0.0076 188 ARG A N   
1446 C  CA  . ARG A 188 ? 0.1957 0.1888 0.1867 0.0058  0.0026  0.0075 188 ARG A CA  
1447 C  C   . ARG A 188 ? 0.2153 0.2084 0.2063 0.0056  0.0023  0.0075 188 ARG A C   
1448 O  O   . ARG A 188 ? 0.1977 0.1912 0.1893 0.0050  0.0019  0.0078 188 ARG A O   
1449 C  CB  . ARG A 188 ? 0.1787 0.1712 0.1692 0.0057  0.0022  0.0076 188 ARG A CB  
1450 C  CG  . ARG A 188 ? 0.3202 0.3129 0.3111 0.0057  0.0023  0.0077 188 ARG A CG  
1451 C  CD  . ARG A 188 ? 0.3597 0.3519 0.3504 0.0054  0.0017  0.0079 188 ARG A CD  
1452 N  NE  . ARG A 188 ? 0.3337 0.3261 0.3249 0.0047  0.0010  0.0083 188 ARG A NE  
1453 C  CZ  . ARG A 188 ? 0.3633 0.3557 0.3548 0.0043  0.0005  0.0086 188 ARG A CZ  
1454 N  NH1 . ARG A 188 ? 0.3914 0.3837 0.3829 0.0044  0.0007  0.0086 188 ARG A NH1 
1455 N  NH2 . ARG A 188 ? 0.4173 0.4097 0.4092 0.0037  -0.0001 0.0088 188 ARG A NH2 
1456 N  N   . GLN A 189 ? 0.1546 0.1470 0.1447 0.0061  0.0026  0.0073 189 GLN A N   
1457 C  CA  . GLN A 189 ? 0.2558 0.2482 0.2458 0.0060  0.0023  0.0074 189 GLN A CA  
1458 C  C   . GLN A 189 ? 0.2847 0.2764 0.2742 0.0058  0.0017  0.0076 189 GLN A C   
1459 O  O   . GLN A 189 ? 0.2149 0.2057 0.2034 0.0062  0.0018  0.0074 189 GLN A O   
1460 C  CB  . GLN A 189 ? 0.2612 0.2531 0.2503 0.0067  0.0029  0.0071 189 GLN A CB  
1461 C  CG  . GLN A 189 ? 0.2949 0.2868 0.2840 0.0066  0.0027  0.0072 189 GLN A CG  
1462 C  CD  . GLN A 189 ? 0.3391 0.3309 0.3278 0.0072  0.0032  0.0070 189 GLN A CD  
1463 O  OE1 . GLN A 189 ? 0.2887 0.2805 0.2772 0.0077  0.0038  0.0067 189 GLN A OE1 
1464 N  NE2 . GLN A 189 ? 0.2555 0.2473 0.2442 0.0071  0.0031  0.0071 189 GLN A NE2 
1465 N  N   . THR A 190 ? 0.2399 0.2320 0.2302 0.0051  0.0012  0.0079 190 THR A N   
1466 C  CA  . THR A 190 ? 0.2365 0.2282 0.2266 0.0047  0.0005  0.0081 190 THR A CA  
1467 C  C   . THR A 190 ? 0.2813 0.2735 0.2722 0.0040  0.0000  0.0084 190 THR A C   
1468 O  O   . THR A 190 ? 0.2833 0.2762 0.2747 0.0039  0.0002  0.0084 190 THR A O   
1469 C  CB  . THR A 190 ? 0.2792 0.2709 0.2696 0.0044  0.0002  0.0083 190 THR A CB  
1470 O  OG1 . THR A 190 ? 0.4315 0.4230 0.4215 0.0049  0.0007  0.0081 190 THR A OG1 
1471 C  CG2 . THR A 190 ? 0.2645 0.2554 0.2544 0.0043  -0.0004 0.0085 190 THR A CG2 
1472 N  N   . ALA A 191 ? 0.2727 0.2646 0.2635 0.0037  -0.0006 0.0086 191 ALA A N   
1473 C  CA  . ALA A 191 ? 0.3070 0.2991 0.2982 0.0031  -0.0011 0.0088 191 ALA A CA  
1474 C  C   . ALA A 191 ? 0.2924 0.2848 0.2841 0.0026  -0.0014 0.0089 191 ALA A C   
1475 O  O   . ALA A 191 ? 0.4801 0.4720 0.4716 0.0023  -0.0019 0.0090 191 ALA A O   
1476 C  CB  . ALA A 191 ? 0.2927 0.2842 0.2835 0.0030  -0.0017 0.0090 191 ALA A CB  
1477 N  N   . GLN A 192 ? 0.2177 0.2108 0.2100 0.0025  -0.0011 0.0087 192 GLN A N   
1478 C  CA  . GLN A 192 ? 0.2807 0.2742 0.2735 0.0023  -0.0011 0.0087 192 GLN A CA  
1479 C  C   . GLN A 192 ? 0.3068 0.3010 0.3002 0.0021  -0.0010 0.0088 192 GLN A C   
1480 O  O   . GLN A 192 ? 0.3314 0.3261 0.3251 0.0022  -0.0007 0.0087 192 GLN A O   
1481 C  CB  . GLN A 192 ? 0.2871 0.2812 0.2804 0.0024  -0.0006 0.0087 192 GLN A CB  
1482 C  CG  . GLN A 192 ? 0.2474 0.2419 0.2408 0.0028  -0.0001 0.0086 192 GLN A CG  
1483 C  CD  . GLN A 192 ? 0.2396 0.2343 0.2331 0.0031  0.0003  0.0085 192 GLN A CD  
1484 O  OE1 . GLN A 192 ? 0.1865 0.1816 0.1806 0.0029  0.0003  0.0085 192 GLN A OE1 
1485 N  NE2 . GLN A 192 ? 0.1629 0.1573 0.1559 0.0036  0.0008  0.0083 192 GLN A NE2 
1486 N  N   . ALA A 193 ? 0.2186 0.2132 0.2126 0.0019  -0.0011 0.0089 193 ALA A N   
1487 C  CA  . ALA A 193 ? 0.3347 0.3304 0.3297 0.0016  -0.0011 0.0090 193 ALA A CA  
1488 C  C   . ALA A 193 ? 0.2567 0.2538 0.2531 0.0013  -0.0010 0.0091 193 ALA A C   
1489 O  O   . ALA A 193 ? 0.1984 0.1957 0.1951 0.0012  -0.0010 0.0092 193 ALA A O   
1490 C  CB  . ALA A 193 ? 0.3473 0.3427 0.3421 0.0015  -0.0014 0.0091 193 ALA A CB  
1491 N  N   . ALA A 194 ? 0.2391 0.2373 0.2365 0.0011  -0.0009 0.0092 194 ALA A N   
1492 C  CA  . ALA A 194 ? 0.2202 0.2198 0.2190 0.0007  -0.0009 0.0094 194 ALA A CA  
1493 C  C   . ALA A 194 ? 0.2286 0.2289 0.2283 0.0003  -0.0013 0.0096 194 ALA A C   
1494 O  O   . ALA A 194 ? 0.2340 0.2339 0.2334 0.0002  -0.0015 0.0096 194 ALA A O   
1495 C  CB  . ALA A 194 ? 0.1539 0.1545 0.1535 0.0006  -0.0008 0.0094 194 ALA A CB  
1496 N  N   . GLY A 195 ? 0.2525 0.2537 0.2532 0.0000  -0.0014 0.0097 195 GLY A N   
1497 C  CA  . GLY A 195 ? 0.1985 0.2006 0.2004 -0.0006 -0.0018 0.0100 195 GLY A CA  
1498 C  C   . GLY A 195 ? 0.2406 0.2437 0.2435 -0.0010 -0.0020 0.0101 195 GLY A C   
1499 O  O   . GLY A 195 ? 0.1524 0.1556 0.1551 -0.0009 -0.0018 0.0100 195 GLY A O   
1500 N  N   . THR A 196 ? 0.1479 0.1517 0.1517 -0.0015 -0.0024 0.0103 196 THR A N   
1501 C  CA  . THR A 196 ? 0.2310 0.2361 0.2359 -0.0019 -0.0027 0.0105 196 THR A CA  
1502 C  C   . THR A 196 ? 0.1708 0.1768 0.1765 -0.0021 -0.0026 0.0105 196 THR A C   
1503 O  O   . THR A 196 ? 0.2142 0.2206 0.2203 -0.0021 -0.0026 0.0106 196 THR A O   
1504 C  CB  . THR A 196 ? 0.1940 0.1998 0.2000 -0.0025 -0.0031 0.0107 196 THR A CB  
1505 O  OG1 . THR A 196 ? 0.2070 0.2118 0.2123 -0.0023 -0.0032 0.0107 196 THR A OG1 
1506 C  CG2 . THR A 196 ? 0.1670 0.1739 0.1740 -0.0029 -0.0034 0.0109 196 THR A CG2 
1507 N  N   . ASP A 197 ? 0.1168 0.1232 0.1226 -0.0021 -0.0025 0.0105 197 ASP A N   
1508 C  CA  . ASP A 197 ? 0.1443 0.1515 0.1508 -0.0023 -0.0026 0.0106 197 ASP A CA  
1509 C  C   . ASP A 197 ? 0.1753 0.1839 0.1832 -0.0029 -0.0030 0.0109 197 ASP A C   
1510 O  O   . ASP A 197 ? 0.1976 0.2065 0.2059 -0.0032 -0.0033 0.0110 197 ASP A O   
1511 C  CB  . ASP A 197 ? 0.1169 0.1239 0.1229 -0.0021 -0.0023 0.0105 197 ASP A CB  
1512 C  CG  . ASP A 197 ? 0.1402 0.1476 0.1464 -0.0021 -0.0022 0.0105 197 ASP A CG  
1513 O  OD1 . ASP A 197 ? 0.1352 0.1424 0.1413 -0.0020 -0.0022 0.0104 197 ASP A OD1 
1514 O  OD2 . ASP A 197 ? 0.1020 0.1098 0.1084 -0.0022 -0.0023 0.0105 197 ASP A OD2 
1515 N  N   . THR A 198 ? 0.1826 0.1920 0.1911 -0.0032 -0.0031 0.0109 198 THR A N   
1516 C  CA  . THR A 198 ? 0.1404 0.1508 0.1499 -0.0037 -0.0036 0.0111 198 THR A CA  
1517 C  C   . THR A 198 ? 0.1212 0.1318 0.1305 -0.0038 -0.0036 0.0110 198 THR A C   
1518 O  O   . THR A 198 ? 0.1173 0.1278 0.1264 -0.0035 -0.0033 0.0111 198 THR A O   
1519 C  CB  . THR A 198 ? 0.1639 0.1742 0.1735 -0.0038 -0.0037 0.0111 198 THR A CB  
1520 O  OG1 . THR A 198 ? 0.2215 0.2320 0.2312 -0.0037 -0.0035 0.0112 198 THR A OG1 
1521 C  CG2 . THR A 198 ? 0.1833 0.1935 0.1931 -0.0038 -0.0037 0.0112 198 THR A CG2 
1522 N  N   . THR A 199 ? 0.1186 0.1291 0.1278 -0.0040 -0.0037 0.0109 199 THR A N   
1523 C  CA  . THR A 199 ? 0.1004 0.1110 0.1094 -0.0041 -0.0038 0.0108 199 THR A CA  
1524 C  C   . THR A 199 ? 0.0732 0.0838 0.0822 -0.0042 -0.0039 0.0109 199 THR A C   
1525 O  O   . THR A 199 ? 0.0716 0.0822 0.0807 -0.0042 -0.0039 0.0108 199 THR A O   
1526 C  CB  . THR A 199 ? 0.1081 0.1187 0.1171 -0.0043 -0.0040 0.0107 199 THR A CB  
1527 O  OG1 . THR A 199 ? 0.0777 0.0884 0.0868 -0.0042 -0.0039 0.0108 199 THR A OG1 
1528 C  CG2 . THR A 199 ? 0.0635 0.0743 0.0724 -0.0045 -0.0041 0.0107 199 THR A CG2 
1529 N  N   . ILE A 200 ? 0.0412 0.0520 0.0501 -0.0042 -0.0039 0.0109 200 ILE A N   
1530 C  CA  . ILE A 200 ? 0.0384 0.0492 0.0472 -0.0043 -0.0039 0.0110 200 ILE A CA  
1531 C  C   . ILE A 200 ? 0.0624 0.0732 0.0711 -0.0046 -0.0042 0.0110 200 ILE A C   
1532 O  O   . ILE A 200 ? 0.0225 0.0334 0.0310 -0.0048 -0.0043 0.0110 200 ILE A O   
1533 C  CB  . ILE A 200 ? 0.0451 0.0561 0.0539 -0.0042 -0.0038 0.0112 200 ILE A CB  
1534 C  CG1 . ILE A 200 ? 0.0583 0.0688 0.0668 -0.0037 -0.0034 0.0111 200 ILE A CG1 
1535 C  CG2 . ILE A 200 ? 0.0607 0.0717 0.0695 -0.0042 -0.0038 0.0113 200 ILE A CG2 
1536 C  CD1 . ILE A 200 ? 0.0517 0.0614 0.0592 -0.0034 -0.0031 0.0109 200 ILE A CD1 
1537 N  N   . THR A 201 ? 0.0484 0.0592 0.0572 -0.0046 -0.0042 0.0109 201 THR A N   
1538 C  CA  . THR A 201 ? 0.0848 0.0957 0.0936 -0.0049 -0.0044 0.0109 201 THR A CA  
1539 C  C   . THR A 201 ? 0.0586 0.0696 0.0672 -0.0051 -0.0046 0.0110 201 THR A C   
1540 O  O   . THR A 201 ? 0.0564 0.0675 0.0648 -0.0054 -0.0048 0.0110 201 THR A O   
1541 C  CB  . THR A 201 ? 0.0529 0.0637 0.0618 -0.0048 -0.0045 0.0109 201 THR A CB  
1542 O  OG1 . THR A 201 ? 0.0532 0.0639 0.0624 -0.0047 -0.0043 0.0108 201 THR A OG1 
1543 C  CG2 . THR A 201 ? 0.0728 0.0837 0.0817 -0.0051 -0.0047 0.0108 201 THR A CG2 
1544 N  N   . VAL A 202 ? 0.0365 0.0476 0.0451 -0.0051 -0.0046 0.0112 202 VAL A N   
1545 C  CA  . VAL A 202 ? 0.0499 0.0611 0.0583 -0.0054 -0.0048 0.0114 202 VAL A CA  
1546 C  C   . VAL A 202 ? 0.0474 0.0586 0.0554 -0.0055 -0.0049 0.0114 202 VAL A C   
1547 O  O   . VAL A 202 ? 0.0409 0.0522 0.0487 -0.0059 -0.0051 0.0115 202 VAL A O   
1548 C  CB  . VAL A 202 ? 0.0551 0.0664 0.0636 -0.0053 -0.0047 0.0117 202 VAL A CB  
1549 C  CG1 . VAL A 202 ? 0.1151 0.1264 0.1237 -0.0050 -0.0045 0.0117 202 VAL A CG1 
1550 C  CG2 . VAL A 202 ? 0.0286 0.0401 0.0369 -0.0057 -0.0050 0.0120 202 VAL A CG2 
1551 N  N   . ASN A 203 ? 0.0476 0.0587 0.0557 -0.0053 -0.0047 0.0113 203 ASN A N   
1552 C  CA  . ASN A 203 ? 0.0429 0.0541 0.0508 -0.0054 -0.0047 0.0113 203 ASN A CA  
1553 C  C   . ASN A 203 ? 0.0325 0.0437 0.0403 -0.0056 -0.0048 0.0112 203 ASN A C   
1554 O  O   . ASN A 203 ? 0.0231 0.0344 0.0307 -0.0059 -0.0050 0.0112 203 ASN A O   
1555 C  CB  . ASN A 203 ? 0.0301 0.0413 0.0382 -0.0051 -0.0045 0.0113 203 ASN A CB  
1556 C  CG  . ASN A 203 ? 0.0890 0.0998 0.0968 -0.0048 -0.0042 0.0114 203 ASN A CG  
1557 O  OD1 . ASN A 203 ? 0.0618 0.0723 0.0692 -0.0049 -0.0042 0.0114 203 ASN A OD1 
1558 N  ND2 . ASN A 203 ? 0.0756 0.0857 0.0828 -0.0043 -0.0038 0.0112 203 ASN A ND2 
1559 N  N   . VAL A 204 ? 0.0107 0.0218 0.0187 -0.0054 -0.0048 0.0110 204 VAL A N   
1560 C  CA  . VAL A 204 ? 0.0286 0.0397 0.0366 -0.0056 -0.0049 0.0109 204 VAL A CA  
1561 C  C   . VAL A 204 ? 0.0324 0.0436 0.0402 -0.0059 -0.0051 0.0110 204 VAL A C   
1562 O  O   . VAL A 204 ? 0.0237 0.0351 0.0315 -0.0061 -0.0053 0.0110 204 VAL A O   
1563 C  CB  . VAL A 204 ? 0.0561 0.0671 0.0643 -0.0054 -0.0047 0.0108 204 VAL A CB  
1564 C  CG1 . VAL A 204 ? 0.0208 0.0320 0.0291 -0.0055 -0.0049 0.0107 204 VAL A CG1 
1565 C  CG2 . VAL A 204 ? 0.0182 0.0292 0.0266 -0.0051 -0.0045 0.0107 204 VAL A CG2 
1566 N  N   . LEU A 205 ? 0.0275 0.0387 0.0354 -0.0060 -0.0052 0.0111 205 LEU A N   
1567 C  CA  . LEU A 205 ? 0.0795 0.0908 0.0872 -0.0063 -0.0055 0.0112 205 LEU A CA  
1568 C  C   . LEU A 205 ? 0.0452 0.0566 0.0526 -0.0067 -0.0057 0.0114 205 LEU A C   
1569 O  O   . LEU A 205 ? 0.0582 0.0697 0.0653 -0.0070 -0.0059 0.0115 205 LEU A O   
1570 C  CB  . LEU A 205 ? 0.0218 0.0331 0.0296 -0.0063 -0.0055 0.0113 205 LEU A CB  
1571 C  CG  . LEU A 205 ? 0.0771 0.0884 0.0853 -0.0060 -0.0053 0.0111 205 LEU A CG  
1572 C  CD1 . LEU A 205 ? 0.0624 0.0738 0.0708 -0.0059 -0.0053 0.0113 205 LEU A CD1 
1573 C  CD2 . LEU A 205 ? 0.0391 0.0504 0.0472 -0.0062 -0.0055 0.0111 205 LEU A CD2 
1574 N  N   . ALA A 206 ? 0.0377 0.0490 0.0449 -0.0066 -0.0056 0.0115 206 ALA A N   
1575 C  CA  . ALA A 206 ? 0.0516 0.0629 0.0584 -0.0070 -0.0058 0.0117 206 ALA A CA  
1576 C  C   . ALA A 206 ? 0.0791 0.0904 0.0857 -0.0071 -0.0059 0.0116 206 ALA A C   
1577 O  O   . ALA A 206 ? 0.0626 0.0739 0.0689 -0.0076 -0.0062 0.0117 206 ALA A O   
1578 C  CB  . ALA A 206 ? 0.0690 0.0803 0.0758 -0.0069 -0.0057 0.0118 206 ALA A CB  
1579 N  N   . TRP A 207 ? 0.0411 0.0525 0.0481 -0.0068 -0.0057 0.0114 207 TRP A N   
1580 C  CA  . TRP A 207 ? 0.0597 0.0711 0.0666 -0.0068 -0.0057 0.0114 207 TRP A CA  
1581 C  C   . TRP A 207 ? 0.0654 0.0769 0.0723 -0.0071 -0.0059 0.0114 207 TRP A C   
1582 O  O   . TRP A 207 ? 0.0585 0.0702 0.0653 -0.0073 -0.0060 0.0114 207 TRP A O   
1583 C  CB  . TRP A 207 ? 0.0728 0.0842 0.0801 -0.0064 -0.0054 0.0112 207 TRP A CB  
1584 C  CG  . TRP A 207 ? 0.0886 0.1002 0.0960 -0.0064 -0.0054 0.0112 207 TRP A CG  
1585 C  CD1 . TRP A 207 ? 0.1014 0.1131 0.1087 -0.0065 -0.0054 0.0113 207 TRP A CD1 
1586 C  CD2 . TRP A 207 ? 0.0681 0.0798 0.0757 -0.0063 -0.0053 0.0111 207 TRP A CD2 
1587 N  NE1 . TRP A 207 ? 0.0969 0.1088 0.1043 -0.0064 -0.0053 0.0113 207 TRP A NE1 
1588 C  CE2 . TRP A 207 ? 0.0574 0.0693 0.0651 -0.0063 -0.0053 0.0112 207 TRP A CE2 
1589 C  CE3 . TRP A 207 ? 0.0607 0.0723 0.0685 -0.0061 -0.0052 0.0110 207 TRP A CE3 
1590 C  CZ2 . TRP A 207 ? 0.0891 0.1011 0.0970 -0.0062 -0.0052 0.0112 207 TRP A CZ2 
1591 C  CZ3 . TRP A 207 ? 0.0562 0.0680 0.0643 -0.0060 -0.0051 0.0109 207 TRP A CZ3 
1592 C  CH2 . TRP A 207 ? 0.0807 0.0927 0.0888 -0.0061 -0.0051 0.0110 207 TRP A CH2 
1593 N  N   . LEU A 208 ? 0.0511 0.0626 0.0582 -0.0070 -0.0058 0.0113 208 LEU A N   
1594 C  CA  . LEU A 208 ? 0.0729 0.0846 0.0800 -0.0072 -0.0060 0.0113 208 LEU A CA  
1595 C  C   . LEU A 208 ? 0.0532 0.0650 0.0600 -0.0077 -0.0063 0.0115 208 LEU A C   
1596 O  O   . LEU A 208 ? 0.0625 0.0744 0.0691 -0.0080 -0.0065 0.0116 208 LEU A O   
1597 C  CB  . LEU A 208 ? 0.0727 0.0844 0.0801 -0.0070 -0.0059 0.0112 208 LEU A CB  
1598 C  CG  . LEU A 208 ? 0.0595 0.0711 0.0672 -0.0066 -0.0057 0.0110 208 LEU A CG  
1599 C  CD1 . LEU A 208 ? 0.0813 0.0929 0.0893 -0.0064 -0.0056 0.0109 208 LEU A CD1 
1600 C  CD2 . LEU A 208 ? 0.0656 0.0774 0.0734 -0.0067 -0.0057 0.0110 208 LEU A CD2 
1601 N  N   . TYR A 209 ? 0.0568 0.0685 0.0633 -0.0078 -0.0064 0.0116 209 TYR A N   
1602 C  CA  . TYR A 209 ? 0.0753 0.0870 0.0813 -0.0084 -0.0068 0.0119 209 TYR A CA  
1603 C  C   . TYR A 209 ? 0.0880 0.0996 0.0937 -0.0086 -0.0069 0.0119 209 TYR A C   
1604 O  O   . TYR A 209 ? 0.0850 0.0966 0.0903 -0.0091 -0.0072 0.0120 209 TYR A O   
1605 C  CB  . TYR A 209 ? 0.0309 0.0424 0.0367 -0.0085 -0.0068 0.0120 209 TYR A CB  
1606 C  CG  . TYR A 209 ? 0.0651 0.0766 0.0711 -0.0084 -0.0068 0.0121 209 TYR A CG  
1607 C  CD1 . TYR A 209 ? 0.0705 0.0821 0.0762 -0.0088 -0.0071 0.0123 209 TYR A CD1 
1608 C  CD2 . TYR A 209 ? 0.0456 0.0571 0.0520 -0.0080 -0.0065 0.0120 209 TYR A CD2 
1609 C  CE1 . TYR A 209 ? 0.0858 0.0976 0.0918 -0.0088 -0.0071 0.0124 209 TYR A CE1 
1610 C  CE2 . TYR A 209 ? 0.0743 0.0859 0.0809 -0.0079 -0.0066 0.0121 209 TYR A CE2 
1611 C  CZ  . TYR A 209 ? 0.0771 0.0888 0.0835 -0.0083 -0.0069 0.0123 209 TYR A CZ  
1612 O  OH  . TYR A 209 ? 0.0565 0.0684 0.0631 -0.0083 -0.0069 0.0124 209 TYR A OH  
1613 N  N   . ALA A 210 ? 0.0275 0.0390 0.0332 -0.0084 -0.0067 0.0118 210 ALA A N   
1614 C  CA  . ALA A 210 ? 0.0816 0.0931 0.0871 -0.0086 -0.0068 0.0119 210 ALA A CA  
1615 C  C   . ALA A 210 ? 0.1019 0.1137 0.1076 -0.0086 -0.0068 0.0119 210 ALA A C   
1616 O  O   . ALA A 210 ? 0.1191 0.1309 0.1244 -0.0090 -0.0071 0.0120 210 ALA A O   
1617 C  CB  . ALA A 210 ? 0.0462 0.0577 0.0519 -0.0082 -0.0065 0.0118 210 ALA A CB  
1618 N  N   . ALA A 211 ? 0.0440 0.0558 0.0501 -0.0083 -0.0066 0.0117 211 ALA A N   
1619 C  CA  . ALA A 211 ? 0.1064 0.1185 0.1127 -0.0083 -0.0067 0.0117 211 ALA A CA  
1620 C  C   . ALA A 211 ? 0.1170 0.1292 0.1231 -0.0088 -0.0070 0.0119 211 ALA A C   
1621 O  O   . ALA A 211 ? 0.1290 0.1414 0.1350 -0.0090 -0.0072 0.0120 211 ALA A O   
1622 C  CB  . ALA A 211 ? 0.0738 0.0860 0.0807 -0.0078 -0.0064 0.0115 211 ALA A CB  
1623 N  N   . VAL A 212 ? 0.0758 0.0880 0.0818 -0.0089 -0.0071 0.0119 212 VAL A N   
1624 C  CA  . VAL A 212 ? 0.1457 0.1580 0.1515 -0.0094 -0.0074 0.0121 212 VAL A CA  
1625 C  C   . VAL A 212 ? 0.1317 0.1439 0.1368 -0.0099 -0.0077 0.0123 212 VAL A C   
1626 O  O   . VAL A 212 ? 0.2026 0.2150 0.2075 -0.0103 -0.0080 0.0124 212 VAL A O   
1627 C  CB  . VAL A 212 ? 0.0998 0.1120 0.1055 -0.0093 -0.0074 0.0121 212 VAL A CB  
1628 C  CG1 . VAL A 212 ? 0.1631 0.1754 0.1685 -0.0099 -0.0078 0.0123 212 VAL A CG1 
1629 C  CG2 . VAL A 212 ? 0.1184 0.1307 0.1247 -0.0089 -0.0072 0.0119 212 VAL A CG2 
1630 N  N   . ILE A 213 ? 0.0964 0.1083 0.1012 -0.0100 -0.0077 0.0123 213 ILE A N   
1631 C  CA  . ILE A 213 ? 0.1575 0.1692 0.1615 -0.0106 -0.0080 0.0124 213 ILE A CA  
1632 C  C   . ILE A 213 ? 0.1820 0.1939 0.1860 -0.0107 -0.0081 0.0125 213 ILE A C   
1633 O  O   . ILE A 213 ? 0.2170 0.2288 0.2205 -0.0113 -0.0084 0.0126 213 ILE A O   
1634 C  CB  . ILE A 213 ? 0.1119 0.1233 0.1156 -0.0106 -0.0080 0.0124 213 ILE A CB  
1635 C  CG1 . ILE A 213 ? 0.1244 0.1356 0.1279 -0.0106 -0.0080 0.0125 213 ILE A CG1 
1636 C  CG2 . ILE A 213 ? 0.1513 0.1624 0.1543 -0.0111 -0.0082 0.0125 213 ILE A CG2 
1637 C  CD1 . ILE A 213 ? 0.1235 0.1345 0.1268 -0.0106 -0.0080 0.0125 213 ILE A CD1 
1638 N  N   . ASN A 214 ? 0.1623 0.1744 0.1670 -0.0102 -0.0078 0.0123 214 ASN A N   
1639 C  CA  . ASN A 214 ? 0.2018 0.2141 0.2065 -0.0103 -0.0078 0.0124 214 ASN A CA  
1640 C  C   . ASN A 214 ? 0.1713 0.1840 0.1764 -0.0103 -0.0079 0.0124 214 ASN A C   
1641 O  O   . ASN A 214 ? 0.1999 0.2128 0.2052 -0.0103 -0.0079 0.0125 214 ASN A O   
1642 C  CB  . ASN A 214 ? 0.1486 0.1609 0.1537 -0.0098 -0.0075 0.0123 214 ASN A CB  
1643 C  CG  . ASN A 214 ? 0.1810 0.1930 0.1857 -0.0099 -0.0075 0.0123 214 ASN A CG  
1644 O  OD1 . ASN A 214 ? 0.2660 0.2780 0.2704 -0.0102 -0.0077 0.0124 214 ASN A OD1 
1645 N  ND2 . ASN A 214 ? 0.1684 0.1802 0.1730 -0.0097 -0.0074 0.0122 214 ASN A ND2 
1646 N  N   . GLY A 215 ? 0.1572 0.1699 0.1625 -0.0102 -0.0079 0.0124 215 GLY A N   
1647 C  CA  . GLY A 215 ? 0.1815 0.1946 0.1872 -0.0102 -0.0079 0.0125 215 GLY A CA  
1648 C  C   . GLY A 215 ? 0.1600 0.1733 0.1663 -0.0097 -0.0076 0.0123 215 GLY A C   
1649 O  O   . GLY A 215 ? 0.1521 0.1656 0.1586 -0.0097 -0.0077 0.0123 215 GLY A O   
1650 N  N   . ASP A 216 ? 0.1332 0.1463 0.1397 -0.0092 -0.0073 0.0121 216 ASP A N   
1651 C  CA  . ASP A 216 ? 0.1764 0.1895 0.1834 -0.0087 -0.0070 0.0119 216 ASP A CA  
1652 C  C   . ASP A 216 ? 0.1732 0.1862 0.1803 -0.0086 -0.0070 0.0118 216 ASP A C   
1653 O  O   . ASP A 216 ? 0.2144 0.2272 0.2215 -0.0084 -0.0069 0.0117 216 ASP A O   
1654 C  CB  . ASP A 216 ? 0.2061 0.2191 0.2133 -0.0083 -0.0067 0.0118 216 ASP A CB  
1655 C  CG  . ASP A 216 ? 0.2422 0.2553 0.2495 -0.0083 -0.0067 0.0119 216 ASP A CG  
1656 O  OD1 . ASP A 216 ? 0.3143 0.3275 0.3220 -0.0079 -0.0064 0.0118 216 ASP A OD1 
1657 O  OD2 . ASP A 216 ? 0.4531 0.4664 0.4602 -0.0086 -0.0069 0.0121 216 ASP A OD2 
1658 N  N   . ARG A 217 ? 0.1281 0.1433 0.1352 -0.0112 -0.0088 0.0166 217 ARG A N   
1659 C  CA  . ARG A 217 ? 0.1238 0.1390 0.1309 -0.0112 -0.0088 0.0166 217 ARG A CA  
1660 C  C   . ARG A 217 ? 0.1358 0.1487 0.1435 -0.0093 -0.0065 0.0124 217 ARG A C   
1661 O  O   . ARG A 217 ? 0.1609 0.1738 0.1686 -0.0093 -0.0065 0.0125 217 ARG A O   
1662 C  CB  . ARG A 217 ? 0.2039 0.2171 0.2107 -0.0094 -0.0075 0.0121 217 ARG A CB  
1663 N  N   . TRP A 218 ? 0.1641 0.1798 0.1721 -0.0109 -0.0087 0.0170 218 TRP A N   
1664 C  CA  . TRP A 218 ? 0.1686 0.1820 0.1771 -0.0090 -0.0064 0.0127 218 TRP A CA  
1665 C  C   . TRP A 218 ? 0.1602 0.1712 0.1650 -0.0073 -0.0068 0.0137 218 TRP A C   
1666 O  O   . TRP A 218 ? 0.1545 0.1678 0.1633 -0.0087 -0.0063 0.0127 218 TRP A O   
1667 C  CB  . TRP A 218 ? 0.2144 0.2307 0.2233 -0.0106 -0.0086 0.0174 218 TRP A CB  
1668 C  CG  . TRP A 218 ? 0.2122 0.2260 0.2210 -0.0081 -0.0066 0.0123 218 TRP A CG  
1669 C  CD1 . TRP A 218 ? 0.2410 0.2543 0.2496 -0.0083 -0.0059 0.0123 218 TRP A CD1 
1670 C  CD2 . TRP A 218 ? 0.1629 0.1787 0.1722 -0.0096 -0.0079 0.0167 218 TRP A CD2 
1671 N  NE1 . TRP A 218 ? 0.2012 0.2168 0.2102 -0.0094 -0.0077 0.0164 218 TRP A NE1 
1672 C  CE2 . TRP A 218 ? 0.1969 0.2103 0.2058 -0.0073 -0.0061 0.0119 218 TRP A CE2 
1673 C  CE3 . TRP A 218 ? 0.1760 0.1865 0.1815 -0.0069 -0.0058 0.0136 218 TRP A CE3 
1674 C  CZ2 . TRP A 218 ? 0.1696 0.1828 0.1786 -0.0070 -0.0058 0.0116 218 TRP A CZ2 
1675 C  CZ3 . TRP A 218 ? 0.2077 0.2179 0.2134 -0.0066 -0.0055 0.0133 218 TRP A CZ3 
1676 C  CH2 . TRP A 218 ? 0.1783 0.1884 0.1840 -0.0063 -0.0053 0.0130 218 TRP A CH2 
1677 N  N   . PHE A 219 ? 0.1686 0.1793 0.1734 -0.0070 -0.0066 0.0133 219 PHE A N   
1678 C  CA  . PHE A 219 ? 0.1652 0.1752 0.1702 -0.0071 -0.0059 0.0133 219 PHE A CA  
1679 C  C   . PHE A 219 ? 0.1601 0.1706 0.1651 -0.0069 -0.0065 0.0132 219 PHE A C   
1680 O  O   . PHE A 219 ? 0.1764 0.1912 0.1854 -0.0096 -0.0080 0.0164 219 PHE A O   
1681 C  CB  . PHE A 219 ? 0.1105 0.1232 0.1190 -0.0074 -0.0061 0.0115 219 PHE A CB  
1682 C  CG  . PHE A 219 ? 0.1338 0.1434 0.1385 -0.0068 -0.0056 0.0127 219 PHE A CG  
1683 C  CD1 . PHE A 219 ? 0.1183 0.1302 0.1263 -0.0078 -0.0056 0.0114 219 PHE A CD1 
1684 C  CD2 . PHE A 219 ? 0.1598 0.1699 0.1644 -0.0065 -0.0062 0.0125 219 PHE A CD2 
1685 C  CE1 . PHE A 219 ? 0.1036 0.1159 0.1111 -0.0076 -0.0064 0.0113 219 PHE A CE1 
1686 C  CE2 . PHE A 219 ? 0.1038 0.1162 0.1114 -0.0076 -0.0063 0.0114 219 PHE A CE2 
1687 C  CZ  . PHE A 219 ? 0.1189 0.1312 0.1263 -0.0077 -0.0064 0.0114 219 PHE A CZ  
1688 N  N   . LEU A 220 ? 0.1502 0.1652 0.1585 -0.0103 -0.0084 0.0166 220 LEU A N   
1689 C  CA  . LEU A 220 ? 0.1478 0.1583 0.1523 -0.0073 -0.0069 0.0133 220 LEU A CA  
1690 C  C   . LEU A 220 ? 0.2005 0.2133 0.2089 -0.0089 -0.0064 0.0125 220 LEU A C   
1691 O  O   . LEU A 220 ? 0.1733 0.1890 0.1820 -0.0108 -0.0089 0.0174 220 LEU A O   
1692 C  CB  . LEU A 220 ? 0.1902 0.2007 0.1942 -0.0077 -0.0071 0.0134 220 LEU A CB  
1693 C  CG  . LEU A 220 ? 0.1831 0.1960 0.1904 -0.0087 -0.0072 0.0118 220 LEU A CG  
1694 C  CD1 . LEU A 220 ? 0.1496 0.1625 0.1564 -0.0092 -0.0075 0.0121 220 LEU A CD1 
1695 C  CD2 . LEU A 220 ? 0.1303 0.1428 0.1375 -0.0084 -0.0070 0.0117 220 LEU A CD2 
1696 N  N   . ASN A 221 ? 0.2111 0.2217 0.2160 -0.0073 -0.0069 0.0136 221 ASN A N   
1697 C  CA  . ASN A 221 ? 0.2643 0.2752 0.2695 -0.0074 -0.0071 0.0139 221 ASN A CA  
1698 C  C   . ASN A 221 ? 0.2978 0.3087 0.3028 -0.0076 -0.0072 0.0140 221 ASN A C   
1699 O  O   . ASN A 221 ? 0.2363 0.2491 0.2448 -0.0091 -0.0066 0.0127 221 ASN A O   
1700 C  CB  . ASN A 221 ? 0.2401 0.2556 0.2498 -0.0102 -0.0086 0.0173 221 ASN A CB  
1701 C  CG  . ASN A 221 ? 0.2321 0.2420 0.2376 -0.0072 -0.0061 0.0137 221 ASN A CG  
1702 O  OD1 . ASN A 221 ? 0.1844 0.1943 0.1899 -0.0072 -0.0062 0.0137 221 ASN A OD1 
1703 N  ND2 . ASN A 221 ? 0.2492 0.2589 0.2549 -0.0069 -0.0059 0.0135 221 ASN A ND2 
1704 N  N   . ARG A 222 ? 0.3587 0.3720 0.3678 -0.0092 -0.0067 0.0131 222 ARG A N   
1705 C  CA  . ARG A 222 ? 0.4078 0.4211 0.4168 -0.0094 -0.0068 0.0132 222 ARG A CA  
1706 C  C   . ARG A 222 ? 0.3251 0.3383 0.3343 -0.0091 -0.0067 0.0132 222 ARG A C   
1707 O  O   . ARG A 222 ? 0.4403 0.4562 0.4500 -0.0110 -0.0092 0.0181 222 ARG A O   
1708 C  CB  . ARG A 222 ? 0.4263 0.4427 0.4356 -0.0117 -0.0096 0.0186 222 ARG A CB  
1709 C  CG  . ARG A 222 ? 0.4252 0.4391 0.4348 -0.0096 -0.0071 0.0138 222 ARG A CG  
1710 C  CD  . ARG A 222 ? 0.5137 0.5256 0.5192 -0.0083 -0.0079 0.0154 222 ARG A CD  
1711 N  NE  . ARG A 222 ? 0.5574 0.5718 0.5674 -0.0098 -0.0072 0.0143 222 ARG A NE  
1712 C  CZ  . ARG A 222 ? 0.6437 0.6550 0.6499 -0.0083 -0.0071 0.0156 222 ARG A CZ  
1713 N  NH1 . ARG A 222 ? 0.6827 0.6973 0.6928 -0.0088 -0.0075 0.0137 222 ARG A NH1 
1714 N  NH2 . ARG A 222 ? 0.5428 0.5541 0.5492 -0.0083 -0.0071 0.0158 222 ARG A NH2 
1715 N  N   . PHE A 223 ? 0.2266 0.2402 0.2360 -0.0083 -0.0071 0.0127 223 PHE A N   
1716 C  CA  . PHE A 223 ? 0.2311 0.2412 0.2370 -0.0073 -0.0063 0.0141 223 PHE A CA  
1717 C  C   . PHE A 223 ? 0.2150 0.2249 0.2208 -0.0072 -0.0062 0.0139 223 PHE A C   
1718 O  O   . PHE A 223 ? 0.2001 0.2150 0.2096 -0.0099 -0.0084 0.0169 223 PHE A O   
1719 C  CB  . PHE A 223 ? 0.2541 0.2641 0.2603 -0.0071 -0.0062 0.0140 223 PHE A CB  
1720 C  CG  . PHE A 223 ? 0.3016 0.3117 0.3079 -0.0072 -0.0063 0.0143 223 PHE A CG  
1721 C  CD1 . PHE A 223 ? 0.3444 0.3548 0.3507 -0.0075 -0.0065 0.0146 223 PHE A CD1 
1722 C  CD2 . PHE A 223 ? 0.3004 0.3156 0.3112 -0.0095 -0.0084 0.0175 223 PHE A CD2 
1723 C  CE1 . PHE A 223 ? 0.3907 0.4047 0.4011 -0.0082 -0.0072 0.0133 223 PHE A CE1 
1724 C  CE2 . PHE A 223 ? 0.3809 0.3945 0.3913 -0.0077 -0.0068 0.0129 223 PHE A CE2 
1725 C  CZ  . PHE A 223 ? 0.3564 0.3723 0.3675 -0.0100 -0.0088 0.0182 223 PHE A CZ  
1726 N  N   . THR A 224 ? 0.1521 0.1620 0.1581 -0.0070 -0.0061 0.0138 224 THR A N   
1727 C  CA  . THR A 224 ? 0.1954 0.2050 0.2013 -0.0068 -0.0060 0.0135 224 THR A CA  
1728 C  C   . THR A 224 ? 0.1577 0.1722 0.1682 -0.0089 -0.0079 0.0166 224 THR A C   
1729 O  O   . THR A 224 ? 0.1786 0.1914 0.1887 -0.0071 -0.0064 0.0122 224 THR A O   
1730 C  CB  . THR A 224 ? 0.2027 0.2125 0.2086 -0.0070 -0.0061 0.0136 224 THR A CB  
1731 O  OG1 . THR A 224 ? 0.1530 0.1659 0.1622 -0.0075 -0.0067 0.0123 224 THR A OG1 
1732 C  CG2 . THR A 224 ? 0.1538 0.1670 0.1636 -0.0076 -0.0067 0.0125 224 THR A CG2 
1733 N  N   . THR A 225 ? 0.0963 0.1106 0.1068 -0.0086 -0.0077 0.0163 225 THR A N   
1734 C  CA  . THR A 225 ? 0.1470 0.1611 0.1580 -0.0083 -0.0075 0.0163 225 THR A CA  
1735 C  C   . THR A 225 ? 0.1485 0.1609 0.1586 -0.0064 -0.0060 0.0118 225 THR A C   
1736 O  O   . THR A 225 ? 0.1594 0.1720 0.1693 -0.0066 -0.0061 0.0120 225 THR A O   
1737 C  CB  . THR A 225 ? 0.0807 0.0945 0.0916 -0.0080 -0.0073 0.0160 225 THR A CB  
1738 O  OG1 . THR A 225 ? 0.1782 0.1919 0.1895 -0.0077 -0.0071 0.0159 225 THR A OG1 
1739 C  CG2 . THR A 225 ? 0.1240 0.1360 0.1337 -0.0063 -0.0057 0.0113 225 THR A CG2 
1740 N  N   . THR A 226 ? 0.1470 0.1593 0.1573 -0.0061 -0.0058 0.0117 226 THR A N   
1741 C  CA  . THR A 226 ? 0.1747 0.1870 0.1852 -0.0060 -0.0057 0.0119 226 THR A CA  
1742 C  C   . THR A 226 ? 0.1755 0.1876 0.1859 -0.0058 -0.0055 0.0117 226 THR A C   
1743 O  O   . THR A 226 ? 0.1463 0.1581 0.1566 -0.0057 -0.0054 0.0114 226 THR A O   
1744 C  CB  . THR A 226 ? 0.1405 0.1530 0.1515 -0.0059 -0.0057 0.0120 226 THR A CB  
1745 O  OG1 . THR A 226 ? 0.1591 0.1729 0.1714 -0.0073 -0.0069 0.0162 226 THR A OG1 
1746 C  CG2 . THR A 226 ? 0.1928 0.2054 0.2038 -0.0061 -0.0059 0.0121 226 THR A CG2 
1747 N  N   . LEU A 227 ? 0.1406 0.1527 0.1510 -0.0057 -0.0055 0.0119 227 LEU A N   
1748 C  CA  . LEU A 227 ? 0.1137 0.1256 0.1242 -0.0055 -0.0053 0.0118 227 LEU A CA  
1749 C  C   . LEU A 227 ? 0.1655 0.1772 0.1761 -0.0053 -0.0052 0.0115 227 LEU A C   
1750 O  O   . LEU A 227 ? 0.1667 0.1781 0.1772 -0.0052 -0.0051 0.0113 227 LEU A O   
1751 C  CB  . LEU A 227 ? 0.1813 0.1934 0.1919 -0.0054 -0.0052 0.0121 227 LEU A CB  
1752 C  CG  . LEU A 227 ? 0.1883 0.2003 0.1988 -0.0053 -0.0051 0.0121 227 LEU A CG  
1753 C  CD1 . LEU A 227 ? 0.2015 0.2134 0.2116 -0.0055 -0.0052 0.0120 227 LEU A CD1 
1754 C  CD2 . LEU A 227 ? 0.1740 0.1863 0.1848 -0.0053 -0.0051 0.0125 227 LEU A CD2 
1755 N  N   . ASN A 228 ? 0.1809 0.1927 0.1919 -0.0053 -0.0052 0.0116 228 ASN A N   
1756 C  CA  . ASN A 228 ? 0.1835 0.1952 0.1947 -0.0052 -0.0051 0.0114 228 ASN A CA  
1757 C  C   . ASN A 228 ? 0.1408 0.1523 0.1518 -0.0052 -0.0051 0.0112 228 ASN A C   
1758 O  O   . ASN A 228 ? 0.1790 0.1872 0.1869 -0.0047 -0.0047 0.0122 228 ASN A O   
1759 C  CB  . ASN A 228 ? 0.2168 0.2286 0.2284 -0.0052 -0.0052 0.0116 228 ASN A CB  
1760 C  CG  . ASN A 228 ? 0.2470 0.2590 0.2589 -0.0051 -0.0051 0.0119 228 ASN A CG  
1761 O  OD1 . ASN A 228 ? 0.3269 0.3388 0.3388 -0.0049 -0.0050 0.0119 228 ASN A OD1 
1762 N  ND2 . ASN A 228 ? 0.2672 0.2795 0.2794 -0.0051 -0.0052 0.0123 228 ASN A ND2 
1763 N  N   . ASP A 229 ? 0.1373 0.1489 0.1483 -0.0055 -0.0053 0.0113 229 ASP A N   
1764 C  CA  . ASP A 229 ? 0.1517 0.1602 0.1595 -0.0051 -0.0050 0.0126 229 ASP A CA  
1765 C  C   . ASP A 229 ? 0.1589 0.1672 0.1663 -0.0050 -0.0049 0.0123 229 ASP A C   
1766 O  O   . ASP A 229 ? 0.1382 0.1509 0.1499 -0.0068 -0.0066 0.0151 229 ASP A O   
1767 C  CB  . ASP A 229 ? 0.1469 0.1603 0.1590 -0.0073 -0.0070 0.0160 229 ASP A CB  
1768 C  CG  . ASP A 229 ? 0.2011 0.2145 0.2131 -0.0075 -0.0071 0.0160 229 ASP A CG  
1769 O  OD1 . ASP A 229 ? 0.2181 0.2300 0.2292 -0.0060 -0.0058 0.0117 229 ASP A OD1 
1770 O  OD2 . ASP A 229 ? 0.2207 0.2295 0.2281 -0.0056 -0.0053 0.0129 229 ASP A OD2 
1771 N  N   . PHE A 230 ? 0.1429 0.1542 0.1531 -0.0055 -0.0052 0.0110 230 PHE A N   
1772 C  CA  . PHE A 230 ? 0.1171 0.1283 0.1270 -0.0054 -0.0051 0.0108 230 PHE A CA  
1773 C  C   . PHE A 230 ? 0.1296 0.1406 0.1396 -0.0052 -0.0050 0.0106 230 PHE A C   
1774 O  O   . PHE A 230 ? 0.1436 0.1544 0.1535 -0.0052 -0.0049 0.0105 230 PHE A O   
1775 C  CB  . PHE A 230 ? 0.0662 0.0775 0.0760 -0.0055 -0.0052 0.0109 230 PHE A CB  
1776 C  CG  . PHE A 230 ? 0.1016 0.1128 0.1111 -0.0055 -0.0051 0.0108 230 PHE A CG  
1777 C  CD1 . PHE A 230 ? 0.0799 0.0911 0.0893 -0.0055 -0.0051 0.0107 230 PHE A CD1 
1778 C  CD2 . PHE A 230 ? 0.1367 0.1478 0.1462 -0.0053 -0.0050 0.0108 230 PHE A CD2 
1779 C  CE1 . PHE A 230 ? 0.1184 0.1295 0.1276 -0.0055 -0.0051 0.0106 230 PHE A CE1 
1780 C  CE2 . PHE A 230 ? 0.1227 0.1337 0.1320 -0.0053 -0.0049 0.0108 230 PHE A CE2 
1781 C  CZ  . PHE A 230 ? 0.1022 0.1132 0.1113 -0.0053 -0.0049 0.0106 230 PHE A CZ  
1782 N  N   . ASN A 231 ? 0.1262 0.1371 0.1364 -0.0051 -0.0049 0.0108 231 ASN A N   
1783 C  CA  . ASN A 231 ? 0.1311 0.1419 0.1414 -0.0049 -0.0048 0.0107 231 ASN A CA  
1784 C  C   . ASN A 231 ? 0.1811 0.1917 0.1914 -0.0049 -0.0048 0.0106 231 ASN A C   
1785 O  O   . ASN A 231 ? 0.1394 0.1499 0.1497 -0.0048 -0.0047 0.0106 231 ASN A O   
1786 C  CB  . ASN A 231 ? 0.1637 0.1746 0.1742 -0.0049 -0.0047 0.0109 231 ASN A CB  
1787 C  CG  . ASN A 231 ? 0.1467 0.1577 0.1571 -0.0048 -0.0047 0.0111 231 ASN A CG  
1788 O  OD1 . ASN A 231 ? 0.1713 0.1823 0.1814 -0.0048 -0.0047 0.0110 231 ASN A OD1 
1789 N  ND2 . ASN A 231 ? 0.1829 0.1941 0.1935 -0.0048 -0.0047 0.0113 231 ASN A ND2 
1790 N  N   . LEU A 232 ? 0.1288 0.1395 0.1393 -0.0050 -0.0049 0.0106 232 LEU A N   
1791 C  CA  . LEU A 232 ? 0.1618 0.1695 0.1694 -0.0046 -0.0046 0.0117 232 LEU A CA  
1792 C  C   . LEU A 232 ? 0.1237 0.1313 0.1311 -0.0046 -0.0046 0.0116 232 LEU A C   
1793 O  O   . LEU A 232 ? 0.1093 0.1195 0.1195 -0.0050 -0.0049 0.0104 232 LEU A O   
1794 C  CB  . LEU A 232 ? 0.1872 0.1993 0.1994 -0.0065 -0.0066 0.0150 232 LEU A CB  
1795 C  CG  . LEU A 232 ? 0.1788 0.1909 0.1914 -0.0066 -0.0067 0.0152 232 LEU A CG  
1796 C  CD1 . LEU A 232 ? 0.2086 0.2196 0.2200 -0.0055 -0.0056 0.0113 232 LEU A CD1 
1797 C  CD2 . LEU A 232 ? 0.2031 0.2149 0.2158 -0.0064 -0.0066 0.0150 232 LEU A CD2 
1798 N  N   . VAL A 233 ? 0.1027 0.1105 0.1100 -0.0047 -0.0046 0.0116 233 VAL A N   
1799 C  CA  . VAL A 233 ? 0.1172 0.1278 0.1272 -0.0051 -0.0050 0.0104 233 VAL A CA  
1800 C  C   . VAL A 233 ? 0.1403 0.1507 0.1501 -0.0050 -0.0048 0.0103 233 VAL A C   
1801 O  O   . VAL A 233 ? 0.1207 0.1310 0.1305 -0.0050 -0.0047 0.0103 233 VAL A O   
1802 C  CB  . VAL A 233 ? 0.1242 0.1322 0.1312 -0.0049 -0.0047 0.0117 233 VAL A CB  
1803 C  CG1 . VAL A 233 ? 0.1142 0.1265 0.1251 -0.0067 -0.0063 0.0145 233 VAL A CG1 
1804 C  CG2 . VAL A 233 ? 0.1195 0.1306 0.1297 -0.0055 -0.0053 0.0109 233 VAL A CG2 
1805 N  N   . ALA A 234 ? 0.1092 0.1197 0.1190 -0.0050 -0.0047 0.0103 234 ALA A N   
1806 C  CA  . ALA A 234 ? 0.1521 0.1625 0.1617 -0.0048 -0.0046 0.0104 234 ALA A CA  
1807 C  C   . ALA A 234 ? 0.1145 0.1247 0.1243 -0.0048 -0.0046 0.0104 234 ALA A C   
1808 O  O   . ALA A 234 ? 0.0861 0.0962 0.0957 -0.0047 -0.0045 0.0104 234 ALA A O   
1809 C  CB  . ALA A 234 ? 0.0922 0.1026 0.1018 -0.0048 -0.0046 0.0105 234 ALA A CB  
1810 N  N   . MET A 235 ? 0.1243 0.1344 0.1343 -0.0048 -0.0046 0.0105 235 MET A N   
1811 C  CA  . MET A 235 ? 0.1662 0.1761 0.1762 -0.0047 -0.0046 0.0105 235 MET A CA  
1812 C  C   . MET A 235 ? 0.1561 0.1659 0.1661 -0.0048 -0.0047 0.0105 235 MET A C   
1813 O  O   . MET A 235 ? 0.1671 0.1768 0.1770 -0.0048 -0.0047 0.0106 235 MET A O   
1814 C  CB  . MET A 235 ? 0.1903 0.2002 0.2006 -0.0048 -0.0047 0.0106 235 MET A CB  
1815 C  CG  . MET A 235 ? 0.2919 0.3016 0.3023 -0.0047 -0.0048 0.0107 235 MET A CG  
1816 S  SD  . MET A 235 ? 0.6275 0.6372 0.6382 -0.0047 -0.0048 0.0109 235 MET A SD  
1817 C  CE  . MET A 235 ? 0.3419 0.3518 0.3528 -0.0048 -0.0049 0.0108 235 MET A CE  
1818 N  N   . LYS A 236 ? 0.1970 0.2069 0.2070 -0.0049 -0.0048 0.0104 236 LYS A N   
1819 C  CA  . LYS A 236 ? 0.1573 0.1671 0.1673 -0.0050 -0.0048 0.0105 236 LYS A CA  
1820 C  C   . LYS A 236 ? 0.1511 0.1610 0.1609 -0.0049 -0.0047 0.0105 236 LYS A C   
1821 O  O   . LYS A 236 ? 0.1533 0.1631 0.1631 -0.0049 -0.0048 0.0106 236 LYS A O   
1822 C  CB  . LYS A 236 ? 0.1953 0.2052 0.2054 -0.0051 -0.0049 0.0104 236 LYS A CB  
1823 C  CG  . LYS A 236 ? 0.2020 0.2119 0.2121 -0.0052 -0.0050 0.0104 236 LYS A CG  
1824 C  CD  . LYS A 236 ? 0.2695 0.2794 0.2797 -0.0053 -0.0051 0.0104 236 LYS A CD  
1825 C  CE  . LYS A 236 ? 0.2637 0.2737 0.2740 -0.0054 -0.0052 0.0105 236 LYS A CE  
1826 N  NZ  . LYS A 236 ? 0.2358 0.2432 0.2432 -0.0049 -0.0049 0.0119 236 LYS A NZ  
1827 N  N   . TYR A 237 ? 0.1397 0.1497 0.1494 -0.0048 -0.0046 0.0104 237 TYR A N   
1828 C  CA  . TYR A 237 ? 0.0939 0.1040 0.1035 -0.0048 -0.0045 0.0105 237 TYR A CA  
1829 C  C   . TYR A 237 ? 0.0908 0.1009 0.1004 -0.0046 -0.0044 0.0105 237 TYR A C   
1830 O  O   . TYR A 237 ? 0.1025 0.1127 0.1119 -0.0046 -0.0043 0.0106 237 TYR A O   
1831 C  CB  . TYR A 237 ? 0.1391 0.1494 0.1486 -0.0048 -0.0045 0.0104 237 TYR A CB  
1832 C  CG  . TYR A 237 ? 0.1694 0.1798 0.1790 -0.0050 -0.0046 0.0103 237 TYR A CG  
1833 C  CD1 . TYR A 237 ? 0.1790 0.1895 0.1887 -0.0050 -0.0046 0.0104 237 TYR A CD1 
1834 C  CD2 . TYR A 237 ? 0.1763 0.1866 0.1860 -0.0051 -0.0047 0.0103 237 TYR A CD2 
1835 C  CE1 . TYR A 237 ? 0.2092 0.2197 0.2189 -0.0051 -0.0047 0.0104 237 TYR A CE1 
1836 C  CE2 . TYR A 237 ? 0.1913 0.2019 0.2011 -0.0051 -0.0049 0.0103 237 TYR A CE2 
1837 C  CZ  . TYR A 237 ? 0.2063 0.2168 0.2161 -0.0052 -0.0048 0.0103 237 TYR A CZ  
1838 O  OH  . TYR A 237 ? 0.2317 0.2424 0.2417 -0.0053 -0.0051 0.0105 237 TYR A OH  
1839 N  N   . ASN A 238 ? 0.0740 0.0839 0.0836 -0.0046 -0.0044 0.0106 238 ASN A N   
1840 C  CA  . ASN A 238 ? 0.1194 0.1293 0.1289 -0.0044 -0.0043 0.0107 238 ASN A CA  
1841 C  C   . ASN A 238 ? 0.0942 0.1044 0.1037 -0.0044 -0.0042 0.0107 238 ASN A C   
1842 O  O   . ASN A 238 ? 0.1278 0.1381 0.1372 -0.0043 -0.0040 0.0107 238 ASN A O   
1843 C  CB  . ASN A 238 ? 0.1335 0.1435 0.1431 -0.0044 -0.0042 0.0109 238 ASN A CB  
1844 C  CG  . ASN A 238 ? 0.2796 0.2896 0.2892 -0.0042 -0.0041 0.0110 238 ASN A CG  
1845 O  OD1 . ASN A 238 ? 0.2159 0.2259 0.2256 -0.0041 -0.0041 0.0110 238 ASN A OD1 
1846 N  ND2 . ASN A 238 ? 0.2515 0.2616 0.2612 -0.0041 -0.0040 0.0112 238 ASN A ND2 
1847 N  N   . TYR A 239 ? 0.0588 0.0690 0.0683 -0.0045 -0.0042 0.0106 239 TYR A N   
1848 C  CA  . TYR A 239 ? 0.0771 0.0874 0.0864 -0.0044 -0.0042 0.0106 239 TYR A CA  
1849 C  C   . TYR A 239 ? 0.1096 0.1200 0.1191 -0.0044 -0.0042 0.0107 239 TYR A C   
1850 O  O   . TYR A 239 ? 0.1245 0.1347 0.1341 -0.0044 -0.0042 0.0107 239 TYR A O   
1851 C  CB  . TYR A 239 ? 0.0759 0.0863 0.0852 -0.0046 -0.0043 0.0105 239 TYR A CB  
1852 C  CG  . TYR A 239 ? 0.0741 0.0847 0.0833 -0.0047 -0.0044 0.0105 239 TYR A CG  
1853 C  CD1 . TYR A 239 ? 0.0972 0.1077 0.1064 -0.0047 -0.0043 0.0104 239 TYR A CD1 
1854 C  CD2 . TYR A 239 ? 0.0689 0.0796 0.0779 -0.0048 -0.0044 0.0105 239 TYR A CD2 
1855 C  CE1 . TYR A 239 ? 0.1181 0.1287 0.1272 -0.0047 -0.0043 0.0104 239 TYR A CE1 
1856 C  CE2 . TYR A 239 ? 0.0892 0.1000 0.0981 -0.0049 -0.0044 0.0105 239 TYR A CE2 
1857 C  CZ  . TYR A 239 ? 0.0861 0.0968 0.0950 -0.0048 -0.0044 0.0105 239 TYR A CZ  
1858 O  OH  . TYR A 239 ? 0.0413 0.0522 0.0501 -0.0049 -0.0044 0.0105 239 TYR A OH  
1859 N  N   . GLU A 240 ? 0.0897 0.1001 0.0991 -0.0043 -0.0041 0.0108 240 GLU A N   
1860 C  CA  . GLU A 240 ? 0.1306 0.1411 0.1402 -0.0042 -0.0040 0.0109 240 GLU A CA  
1861 C  C   . GLU A 240 ? 0.1286 0.1392 0.1383 -0.0043 -0.0041 0.0109 240 GLU A C   
1862 O  O   . GLU A 240 ? 0.1084 0.1191 0.1180 -0.0045 -0.0043 0.0108 240 GLU A O   
1863 C  CB  . GLU A 240 ? 0.1228 0.1335 0.1324 -0.0041 -0.0039 0.0110 240 GLU A CB  
1864 C  CG  . GLU A 240 ? 0.2330 0.2437 0.2427 -0.0039 -0.0037 0.0112 240 GLU A CG  
1865 C  CD  . GLU A 240 ? 0.3244 0.3352 0.3340 -0.0038 -0.0036 0.0113 240 GLU A CD  
1866 O  OE1 . GLU A 240 ? 0.3776 0.3886 0.3872 -0.0038 -0.0036 0.0114 240 GLU A OE1 
1867 O  OE2 . GLU A 240 ? 0.2520 0.2626 0.2614 -0.0036 -0.0034 0.0112 240 GLU A OE2 
1868 N  N   . PRO A 241 ? 0.1253 0.1358 0.1352 -0.0043 -0.0041 0.0110 241 PRO A N   
1869 C  CA  . PRO A 241 ? 0.1089 0.1196 0.1190 -0.0044 -0.0043 0.0110 241 PRO A CA  
1870 C  C   . PRO A 241 ? 0.1497 0.1606 0.1597 -0.0045 -0.0043 0.0112 241 PRO A C   
1871 O  O   . PRO A 241 ? 0.1209 0.1319 0.1309 -0.0044 -0.0042 0.0113 241 PRO A O   
1872 C  CB  . PRO A 241 ? 0.1555 0.1662 0.1659 -0.0043 -0.0042 0.0112 241 PRO A CB  
1873 C  CG  . PRO A 241 ? 0.1361 0.1466 0.1465 -0.0042 -0.0041 0.0111 241 PRO A CG  
1874 C  CD  . PRO A 241 ? 0.1340 0.1445 0.1442 -0.0041 -0.0040 0.0111 241 PRO A CD  
1875 N  N   . LEU A 242 ? 0.1074 0.1184 0.1173 -0.0047 -0.0044 0.0112 242 LEU A N   
1876 C  CA  . LEU A 242 ? 0.1260 0.1373 0.1358 -0.0048 -0.0045 0.0114 242 LEU A CA  
1877 C  C   . LEU A 242 ? 0.1159 0.1274 0.1261 -0.0048 -0.0045 0.0117 242 LEU A C   
1878 O  O   . LEU A 242 ? 0.1437 0.1552 0.1541 -0.0048 -0.0046 0.0117 242 LEU A O   
1879 C  CB  . LEU A 242 ? 0.1125 0.1237 0.1221 -0.0051 -0.0048 0.0113 242 LEU A CB  
1880 C  CG  . LEU A 242 ? 0.1142 0.1256 0.1236 -0.0053 -0.0049 0.0116 242 LEU A CG  
1881 C  CD1 . LEU A 242 ? 0.1242 0.1356 0.1334 -0.0053 -0.0049 0.0115 242 LEU A CD1 
1882 C  CD2 . LEU A 242 ? 0.1817 0.1932 0.1909 -0.0056 -0.0051 0.0115 242 LEU A CD2 
1883 N  N   . THR A 243 ? 0.0815 0.0931 0.0917 -0.0047 -0.0045 0.0120 243 THR A N   
1884 C  CA  . THR A 243 ? 0.1144 0.1263 0.1250 -0.0047 -0.0044 0.0123 243 THR A CA  
1885 C  C   . THR A 243 ? 0.1232 0.1353 0.1336 -0.0049 -0.0046 0.0127 243 THR A C   
1886 O  O   . THR A 243 ? 0.0926 0.1047 0.1027 -0.0052 -0.0048 0.0126 243 THR A O   
1887 C  CB  . THR A 243 ? 0.1041 0.1161 0.1149 -0.0044 -0.0042 0.0125 243 THR A CB  
1888 O  OG1 . THR A 243 ? 0.1313 0.1434 0.1419 -0.0044 -0.0042 0.0126 243 THR A OG1 
1889 C  CG2 . THR A 243 ? 0.0736 0.0853 0.0844 -0.0042 -0.0040 0.0122 243 THR A CG2 
1890 N  N   . GLN A 244 ? 0.1760 0.1885 0.1868 -0.0049 -0.0046 0.0130 244 GLN A N   
1891 C  CA  . GLN A 244 ? 0.1787 0.1915 0.1895 -0.0052 -0.0048 0.0134 244 GLN A CA  
1892 C  C   . GLN A 244 ? 0.1319 0.1441 0.1418 -0.0052 -0.0047 0.0134 244 GLN A C   
1893 O  O   . GLN A 244 ? 0.0842 0.0960 0.0933 -0.0054 -0.0048 0.0134 244 GLN A O   
1894 C  CB  . GLN A 244 ? 0.1754 0.1886 0.1868 -0.0051 -0.0048 0.0139 244 GLN A CB  
1895 C  CG  . GLN A 244 ? 0.1463 0.1591 0.1569 -0.0053 -0.0048 0.0142 244 GLN A CG  
1896 C  CD  . GLN A 244 ? 0.1722 0.1856 0.1831 -0.0059 -0.0054 0.0143 244 GLN A CD  
1897 O  OE1 . GLN A 244 ? 0.2190 0.2323 0.2299 -0.0058 -0.0054 0.0140 244 GLN A OE1 
1898 N  NE2 . GLN A 244 ? 0.1622 0.1749 0.1719 -0.0061 -0.0054 0.0142 244 GLN A NE2 
1899 N  N   . ASP A 245 ? 0.1113 0.1229 0.1209 -0.0047 -0.0042 0.0132 245 ASP A N   
1900 C  CA  . ASP A 245 ? 0.1081 0.1184 0.1162 -0.0044 -0.0038 0.0129 245 ASP A CA  
1901 C  C   . ASP A 245 ? 0.1087 0.1192 0.1167 -0.0048 -0.0041 0.0127 245 ASP A C   
1902 O  O   . ASP A 245 ? 0.1180 0.1276 0.1248 -0.0049 -0.0040 0.0126 245 ASP A O   
1903 C  CB  . ASP A 245 ? 0.1328 0.1425 0.1407 -0.0039 -0.0033 0.0127 245 ASP A CB  
1904 C  CG  . ASP A 245 ? 0.2117 0.2209 0.2195 -0.0034 -0.0029 0.0129 245 ASP A CG  
1905 O  OD1 . ASP A 245 ? 0.2469 0.2560 0.2544 -0.0035 -0.0029 0.0131 245 ASP A OD1 
1906 O  OD2 . ASP A 245 ? 0.2104 0.2194 0.2182 -0.0030 -0.0025 0.0128 245 ASP A OD2 
1907 N  N   . HIS A 246 ? 0.1046 0.1161 0.1137 -0.0050 -0.0045 0.0127 246 HIS A N   
1908 C  CA  . HIS A 246 ? 0.0879 0.0997 0.0970 -0.0054 -0.0048 0.0126 246 HIS A CA  
1909 C  C   . HIS A 246 ? 0.0790 0.0911 0.0879 -0.0059 -0.0052 0.0128 246 HIS A C   
1910 O  O   . HIS A 246 ? 0.0541 0.0660 0.0624 -0.0062 -0.0054 0.0127 246 HIS A O   
1911 C  CB  . HIS A 246 ? 0.0855 0.0973 0.0948 -0.0052 -0.0048 0.0122 246 HIS A CB  
1912 C  CG  . HIS A 246 ? 0.0822 0.0938 0.0917 -0.0048 -0.0044 0.0121 246 HIS A CG  
1913 N  ND1 . HIS A 246 ? 0.1355 0.1470 0.1452 -0.0047 -0.0043 0.0119 246 HIS A ND1 
1914 C  CD2 . HIS A 246 ? 0.1369 0.1483 0.1462 -0.0046 -0.0042 0.0122 246 HIS A CD2 
1915 C  CE1 . HIS A 246 ? 0.1399 0.1513 0.1497 -0.0044 -0.0041 0.0119 246 HIS A CE1 
1916 N  NE2 . HIS A 246 ? 0.1843 0.1959 0.1941 -0.0043 -0.0040 0.0121 246 HIS A NE2 
1917 N  N   . VAL A 247 ? 0.0591 0.0713 0.0682 -0.0060 -0.0053 0.0129 247 VAL A N   
1918 C  CA  . VAL A 247 ? 0.0829 0.0952 0.0917 -0.0065 -0.0057 0.0130 247 VAL A CA  
1919 C  C   . VAL A 247 ? 0.1007 0.1125 0.1086 -0.0067 -0.0057 0.0132 247 VAL A C   
1920 O  O   . VAL A 247 ? 0.0833 0.0950 0.0907 -0.0071 -0.0060 0.0132 247 VAL A O   
1921 C  CB  . VAL A 247 ? 0.1090 0.1214 0.1181 -0.0064 -0.0057 0.0132 247 VAL A CB  
1922 C  CG1 . VAL A 247 ? 0.0840 0.0966 0.0928 -0.0070 -0.0061 0.0135 247 VAL A CG1 
1923 C  CG2 . VAL A 247 ? 0.0715 0.0838 0.0808 -0.0062 -0.0056 0.0127 247 VAL A CG2 
1924 N  N   . ASP A 248 ? 0.0569 0.0677 0.0640 -0.0062 -0.0051 0.0132 248 ASP A N   
1925 C  CA  . ASP A 248 ? 0.0981 0.1074 0.1036 -0.0061 -0.0047 0.0131 248 ASP A CA  
1926 C  C   . ASP A 248 ? 0.1203 0.1290 0.1249 -0.0062 -0.0047 0.0129 248 ASP A C   
1927 O  O   . ASP A 248 ? 0.1295 0.1374 0.1330 -0.0065 -0.0047 0.0129 248 ASP A O   
1928 C  CB  . ASP A 248 ? 0.0941 0.1025 0.0991 -0.0055 -0.0041 0.0131 248 ASP A CB  
1929 C  CG  . ASP A 248 ? 0.1384 0.1474 0.1442 -0.0054 -0.0041 0.0135 248 ASP A CG  
1930 O  OD1 . ASP A 248 ? 0.1396 0.1495 0.1460 -0.0059 -0.0046 0.0137 248 ASP A OD1 
1931 O  OD2 . ASP A 248 ? 0.1513 0.1597 0.1569 -0.0049 -0.0036 0.0135 248 ASP A OD2 
1932 N  N   . ILE A 249 ? 0.0597 0.0685 0.0647 -0.0058 -0.0045 0.0126 249 ILE A N   
1933 C  CA  . ILE A 249 ? 0.0830 0.0912 0.0872 -0.0058 -0.0044 0.0124 249 ILE A CA  
1934 C  C   . ILE A 249 ? 0.0557 0.0646 0.0602 -0.0065 -0.0050 0.0125 249 ILE A C   
1935 O  O   . ILE A 249 ? 0.1048 0.1132 0.1085 -0.0067 -0.0050 0.0124 249 ILE A O   
1936 C  CB  . ILE A 249 ? 0.0983 0.1067 0.1031 -0.0054 -0.0042 0.0122 249 ILE A CB  
1937 C  CG1 . ILE A 249 ? 0.0941 0.1012 0.0980 -0.0047 -0.0035 0.0121 249 ILE A CG1 
1938 C  CG2 . ILE A 249 ? 0.1234 0.1317 0.1279 -0.0055 -0.0043 0.0120 249 ILE A CG2 
1939 C  CD1 . ILE A 249 ? 0.2188 0.2264 0.2236 -0.0042 -0.0033 0.0120 249 ILE A CD1 
1940 N  N   . LEU A 250 ? 0.0520 0.0623 0.0578 -0.0069 -0.0056 0.0127 250 LEU A N   
1941 C  CA  . LEU A 250 ? 0.0715 0.0826 0.0777 -0.0076 -0.0062 0.0128 250 LEU A CA  
1942 C  C   . LEU A 250 ? 0.1096 0.1205 0.1151 -0.0081 -0.0064 0.0130 250 LEU A C   
1943 O  O   . LEU A 250 ? 0.0501 0.0616 0.0558 -0.0087 -0.0070 0.0131 250 LEU A O   
1944 C  CB  . LEU A 250 ? 0.0503 0.0620 0.0574 -0.0074 -0.0062 0.0126 250 LEU A CB  
1945 C  CG  . LEU A 250 ? 0.0900 0.1016 0.0974 -0.0069 -0.0059 0.0123 250 LEU A CG  
1946 C  CD1 . LEU A 250 ? 0.0475 0.0591 0.0553 -0.0066 -0.0057 0.0121 250 LEU A CD1 
1947 C  CD2 . LEU A 250 ? 0.0452 0.0567 0.0522 -0.0071 -0.0060 0.0122 250 LEU A CD2 
1948 N  N   . GLY A 251 ? 0.0641 0.0739 0.0686 -0.0078 -0.0060 0.0130 251 GLY A N   
1949 C  CA  . GLY A 251 ? 0.0890 0.0983 0.0926 -0.0083 -0.0062 0.0132 251 GLY A CA  
1950 C  C   . GLY A 251 ? 0.1046 0.1134 0.1072 -0.0088 -0.0064 0.0132 251 GLY A C   
1951 O  O   . GLY A 251 ? 0.1023 0.1118 0.1050 -0.0095 -0.0069 0.0133 251 GLY A O   
1952 N  N   . PRO A 252 ? 0.1043 0.1122 0.1060 -0.0086 -0.0060 0.0129 252 PRO A N   
1953 C  CA  . PRO A 252 ? 0.1079 0.1153 0.1086 -0.0092 -0.0063 0.0128 252 PRO A CA  
1954 C  C   . PRO A 252 ? 0.1187 0.1275 0.1204 -0.0098 -0.0070 0.0130 252 PRO A C   
1955 O  O   . PRO A 252 ? 0.1295 0.1385 0.1309 -0.0105 -0.0075 0.0131 252 PRO A O   
1956 C  CB  . PRO A 252 ? 0.1678 0.1741 0.1677 -0.0086 -0.0057 0.0126 252 PRO A CB  
1957 C  CG  . PRO A 252 ? 0.1936 0.1992 0.1932 -0.0079 -0.0051 0.0125 252 PRO A CG  
1958 C  CD  . PRO A 252 ? 0.1413 0.1481 0.1424 -0.0078 -0.0053 0.0127 252 PRO A CD  
1959 N  N   . LEU A 253 ? 0.0927 0.1025 0.0958 -0.0095 -0.0071 0.0129 253 LEU A N   
1960 C  CA  . LEU A 253 ? 0.0932 0.1042 0.0972 -0.0100 -0.0077 0.0130 253 LEU A CA  
1961 C  C   . LEU A 253 ? 0.1065 0.1177 0.1107 -0.0101 -0.0078 0.0130 253 LEU A C   
1962 O  O   . LEU A 253 ? 0.1021 0.1134 0.1061 -0.0104 -0.0079 0.0130 253 LEU A O   
1963 C  CB  . LEU A 253 ? 0.0575 0.0686 0.0622 -0.0093 -0.0073 0.0127 253 LEU A CB  
1964 C  CG  . LEU A 253 ? 0.0682 0.0792 0.0727 -0.0092 -0.0072 0.0126 253 LEU A CG  
1965 C  CD1 . LEU A 253 ? 0.0469 0.0581 0.0522 -0.0085 -0.0068 0.0124 253 LEU A CD1 
1966 C  CD2 . LEU A 253 ? 0.0838 0.0946 0.0878 -0.0097 -0.0074 0.0126 253 LEU A CD2 
1967 N  N   . SER A 254 ? 0.0725 0.0840 0.0773 -0.0098 -0.0077 0.0132 254 SER A N   
1968 C  CA  . SER A 254 ? 0.1010 0.1127 0.1058 -0.0100 -0.0078 0.0133 254 SER A CA  
1969 C  C   . SER A 254 ? 0.1462 0.1578 0.1503 -0.0108 -0.0082 0.0135 254 SER A C   
1970 O  O   . SER A 254 ? 0.1507 0.1624 0.1546 -0.0110 -0.0084 0.0135 254 SER A O   
1971 C  CB  . SER A 254 ? 0.0968 0.1087 0.1023 -0.0096 -0.0076 0.0134 254 SER A CB  
1972 O  OG  . SER A 254 ? 0.1301 0.1422 0.1358 -0.0096 -0.0077 0.0135 254 SER A OG  
1973 N  N   . ALA A 255 ? 0.1087 0.1198 0.1119 -0.0111 -0.0083 0.0137 255 ALA A N   
1974 C  CA  . ALA A 255 ? 0.1641 0.1743 0.1659 -0.0117 -0.0084 0.0138 255 ALA A CA  
1975 C  C   . ALA A 255 ? 0.1989 0.2094 0.2004 -0.0124 -0.0089 0.0138 255 ALA A C   
1976 O  O   . ALA A 255 ? 0.2114 0.2221 0.2125 -0.0132 -0.0094 0.0140 255 ALA A O   
1977 C  CB  . ALA A 255 ? 0.0998 0.1082 0.0999 -0.0113 -0.0077 0.0136 255 ALA A CB  
1978 N  N   . GLN A 256 ? 0.1602 0.1707 0.1618 -0.0122 -0.0088 0.0136 256 GLN A N   
1979 C  CA  . GLN A 256 ? 0.1826 0.1931 0.1839 -0.0127 -0.0091 0.0135 256 GLN A CA  
1980 C  C   . GLN A 256 ? 0.2447 0.2556 0.2465 -0.0124 -0.0090 0.0134 256 GLN A C   
1981 O  O   . GLN A 256 ? 0.2515 0.2623 0.2529 -0.0129 -0.0092 0.0134 256 GLN A O   
1982 C  CB  . GLN A 256 ? 0.2451 0.2554 0.2464 -0.0124 -0.0089 0.0133 256 GLN A CB  
1983 C  CG  . GLN A 256 ? 0.3051 0.3153 0.3061 -0.0125 -0.0089 0.0131 256 GLN A CG  
1984 C  CD  . GLN A 256 ? 0.3828 0.3926 0.3833 -0.0127 -0.0090 0.0131 256 GLN A CD  
1985 O  OE1 . GLN A 256 ? 0.4955 0.5051 0.4953 -0.0132 -0.0092 0.0130 256 GLN A OE1 
1986 N  NE2 . GLN A 256 ? 0.3523 0.3616 0.3528 -0.0119 -0.0084 0.0129 256 GLN A NE2 
1987 N  N   . THR A 257 ? 0.1954 0.2066 0.1982 -0.0117 -0.0087 0.0132 257 THR A N   
1988 C  CA  . THR A 257 ? 0.1559 0.1674 0.1592 -0.0115 -0.0086 0.0131 257 THR A CA  
1989 C  C   . THR A 257 ? 0.1939 0.2056 0.1973 -0.0116 -0.0087 0.0133 257 THR A C   
1990 O  O   . THR A 257 ? 0.1449 0.1570 0.1486 -0.0116 -0.0088 0.0133 257 THR A O   
1991 C  CB  . THR A 257 ? 0.1723 0.1840 0.1765 -0.0107 -0.0082 0.0128 257 THR A CB  
1992 O  OG1 . THR A 257 ? 0.1032 0.1150 0.1079 -0.0102 -0.0080 0.0128 257 THR A OG1 
1993 C  CG2 . THR A 257 ? 0.1566 0.1682 0.1607 -0.0105 -0.0080 0.0127 257 THR A CG2 
1994 N  N   . GLY A 258 ? 0.1503 0.1620 0.1536 -0.0117 -0.0088 0.0135 258 GLY A N   
1995 C  CA  . GLY A 258 ? 0.1375 0.1495 0.1411 -0.0118 -0.0089 0.0137 258 GLY A CA  
1996 C  C   . GLY A 258 ? 0.1665 0.1788 0.1710 -0.0111 -0.0086 0.0135 258 GLY A C   
1997 O  O   . GLY A 258 ? 0.1782 0.1907 0.1830 -0.0111 -0.0086 0.0136 258 GLY A O   
1998 N  N   . ILE A 259 ? 0.1163 0.1286 0.1214 -0.0105 -0.0082 0.0132 259 ILE A N   
1999 C  CA  . ILE A 259 ? 0.1437 0.1561 0.1495 -0.0098 -0.0079 0.0130 259 ILE A CA  
2000 C  C   . ILE A 259 ? 0.1353 0.1476 0.1414 -0.0095 -0.0077 0.0130 259 ILE A C   
2001 O  O   . ILE A 259 ? 0.0965 0.1087 0.1026 -0.0093 -0.0075 0.0129 259 ILE A O   
2002 C  CB  . ILE A 259 ? 0.1805 0.1929 0.1866 -0.0095 -0.0076 0.0126 259 ILE A CB  
2003 C  CG1 . ILE A 259 ? 0.2116 0.2240 0.2174 -0.0098 -0.0079 0.0127 259 ILE A CG1 
2004 C  CG2 . ILE A 259 ? 0.1345 0.1469 0.1412 -0.0089 -0.0073 0.0124 259 ILE A CG2 
2005 C  CD1 . ILE A 259 ? 0.1918 0.2043 0.1980 -0.0095 -0.0076 0.0124 259 ILE A CD1 
2006 N  N   . ALA A 260 ? 0.1078 0.1204 0.1143 -0.0094 -0.0077 0.0131 260 ALA A N   
2007 C  CA  . ALA A 260 ? 0.1235 0.1361 0.1304 -0.0090 -0.0075 0.0132 260 ALA A CA  
2008 C  C   . ALA A 260 ? 0.0899 0.1023 0.0971 -0.0084 -0.0071 0.0128 260 ALA A C   
2009 O  O   . ALA A 260 ? 0.0845 0.0969 0.0919 -0.0082 -0.0069 0.0125 260 ALA A O   
2010 C  CB  . ALA A 260 ? 0.1368 0.1497 0.1441 -0.0090 -0.0075 0.0133 260 ALA A CB  
2011 N  N   . VAL A 261 ? 0.1138 0.1262 0.1213 -0.0082 -0.0069 0.0128 261 VAL A N   
2012 C  CA  . VAL A 261 ? 0.0822 0.0944 0.0899 -0.0077 -0.0066 0.0125 261 VAL A CA  
2013 C  C   . VAL A 261 ? 0.1182 0.1304 0.1263 -0.0073 -0.0064 0.0122 261 VAL A C   
2014 O  O   . VAL A 261 ? 0.0945 0.1065 0.1027 -0.0071 -0.0062 0.0119 261 VAL A O   
2015 C  CB  . VAL A 261 ? 0.1313 0.1435 0.1392 -0.0075 -0.0064 0.0126 261 VAL A CB  
2016 C  CG1 . VAL A 261 ? 0.0785 0.0905 0.0867 -0.0069 -0.0061 0.0123 261 VAL A CG1 
2017 C  CG2 . VAL A 261 ? 0.1048 0.1169 0.1122 -0.0078 -0.0066 0.0128 261 VAL A CG2 
2018 N  N   . LEU A 262 ? 0.1299 0.1422 0.1382 -0.0073 -0.0064 0.0124 262 LEU A N   
2019 C  CA  . LEU A 262 ? 0.1276 0.1399 0.1363 -0.0071 -0.0063 0.0122 262 LEU A CA  
2020 C  C   . LEU A 262 ? 0.1143 0.1267 0.1230 -0.0072 -0.0064 0.0120 262 LEU A C   
2021 O  O   . LEU A 262 ? 0.0937 0.1059 0.1026 -0.0069 -0.0062 0.0117 262 LEU A O   
2022 C  CB  . LEU A 262 ? 0.1508 0.1633 0.1599 -0.0071 -0.0063 0.0124 262 LEU A CB  
2023 C  CG  . LEU A 262 ? 0.1201 0.1327 0.1295 -0.0069 -0.0062 0.0126 262 LEU A CG  
2024 C  CD1 . LEU A 262 ? 0.1877 0.2005 0.1974 -0.0069 -0.0063 0.0128 262 LEU A CD1 
2025 C  CD2 . LEU A 262 ? 0.1858 0.1981 0.1953 -0.0065 -0.0059 0.0122 262 LEU A CD2 
2026 N  N   . ASP A 263 ? 0.1057 0.1182 0.1141 -0.0076 -0.0066 0.0122 263 ASP A N   
2027 C  CA  . ASP A 263 ? 0.1458 0.1583 0.1541 -0.0077 -0.0067 0.0120 263 ASP A CA  
2028 C  C   . ASP A 263 ? 0.1369 0.1492 0.1451 -0.0075 -0.0065 0.0117 263 ASP A C   
2029 O  O   . ASP A 263 ? 0.0996 0.1119 0.1080 -0.0073 -0.0064 0.0115 263 ASP A O   
2030 C  CB  . ASP A 263 ? 0.1190 0.1317 0.1269 -0.0082 -0.0070 0.0123 263 ASP A CB  
2031 C  CG  . ASP A 263 ? 0.1639 0.1769 0.1719 -0.0084 -0.0072 0.0126 263 ASP A CG  
2032 O  OD1 . ASP A 263 ? 0.1629 0.1759 0.1712 -0.0082 -0.0071 0.0126 263 ASP A OD1 
2033 O  OD2 . ASP A 263 ? 0.2219 0.2350 0.2295 -0.0089 -0.0075 0.0129 263 ASP A OD2 
2034 N  N   . MET A 264 ? 0.0743 0.0865 0.0823 -0.0075 -0.0065 0.0118 264 MET A N   
2035 C  CA  . MET A 264 ? 0.0796 0.0916 0.0875 -0.0073 -0.0063 0.0115 264 MET A CA  
2036 C  C   . MET A 264 ? 0.0888 0.1007 0.0971 -0.0069 -0.0060 0.0113 264 MET A C   
2037 O  O   . MET A 264 ? 0.0747 0.0865 0.0831 -0.0067 -0.0059 0.0111 264 MET A O   
2038 C  CB  . MET A 264 ? 0.0899 0.1018 0.0975 -0.0074 -0.0063 0.0116 264 MET A CB  
2039 C  CG  . MET A 264 ? 0.0965 0.1083 0.1041 -0.0073 -0.0062 0.0115 264 MET A CG  
2040 S  SD  . MET A 264 ? 0.0998 0.1118 0.1072 -0.0076 -0.0064 0.0115 264 MET A SD  
2041 C  CE  . MET A 264 ? 0.0599 0.0718 0.0667 -0.0081 -0.0067 0.0117 264 MET A CE  
2042 N  N   . CYS A 265 ? 0.0635 0.0753 0.0719 -0.0067 -0.0059 0.0113 265 CYS A N   
2043 C  CA  . CYS A 265 ? 0.0844 0.0961 0.0931 -0.0063 -0.0057 0.0111 265 CYS A CA  
2044 C  C   . CYS A 265 ? 0.1031 0.1148 0.1120 -0.0063 -0.0057 0.0110 265 CYS A C   
2045 O  O   . CYS A 265 ? 0.1029 0.1116 0.1088 -0.0057 -0.0050 0.0121 265 CYS A O   
2046 C  CB  . CYS A 265 ? 0.0751 0.0867 0.0840 -0.0062 -0.0056 0.0112 265 CYS A CB  
2047 S  SG  . CYS A 265 ? 0.1025 0.1141 0.1113 -0.0061 -0.0056 0.0114 265 CYS A SG  
2048 N  N   . ALA A 266 ? 0.0870 0.1007 0.0966 -0.0083 -0.0073 0.0154 266 ALA A N   
2049 C  CA  . ALA A 266 ? 0.1094 0.1215 0.1186 -0.0068 -0.0059 0.0114 266 ALA A CA  
2050 C  C   . ALA A 266 ? 0.1127 0.1266 0.1224 -0.0085 -0.0075 0.0157 266 ALA A C   
2051 O  O   . ALA A 266 ? 0.1572 0.1664 0.1632 -0.0062 -0.0055 0.0128 266 ALA A O   
2052 C  CB  . ALA A 266 ? 0.1157 0.1281 0.1250 -0.0071 -0.0062 0.0117 266 ALA A CB  
2053 N  N   . SER A 267 ? 0.0989 0.1110 0.1077 -0.0069 -0.0060 0.0113 267 SER A N   
2054 C  CA  . SER A 267 ? 0.0966 0.1058 0.1020 -0.0064 -0.0055 0.0126 267 SER A CA  
2055 C  C   . SER A 267 ? 0.1025 0.1144 0.1113 -0.0066 -0.0057 0.0111 267 SER A C   
2056 O  O   . SER A 267 ? 0.0842 0.0933 0.0900 -0.0060 -0.0052 0.0124 267 SER A O   
2057 C  CB  . SER A 267 ? 0.1113 0.1234 0.1197 -0.0071 -0.0061 0.0113 267 SER A CB  
2058 O  OG  . SER A 267 ? 0.1764 0.1889 0.1848 -0.0075 -0.0063 0.0115 267 SER A OG  
2059 N  N   . LEU A 268 ? 0.0612 0.0701 0.0668 -0.0058 -0.0051 0.0121 268 LEU A N   
2060 C  CA  . LEU A 268 ? 0.0737 0.0868 0.0831 -0.0075 -0.0067 0.0146 268 LEU A CA  
2061 C  C   . LEU A 268 ? 0.0880 0.0966 0.0940 -0.0054 -0.0049 0.0119 268 LEU A C   
2062 O  O   . LEU A 268 ? 0.1008 0.1122 0.1099 -0.0058 -0.0052 0.0106 268 LEU A O   
2063 C  CB  . LEU A 268 ? 0.0451 0.0565 0.0538 -0.0059 -0.0053 0.0106 268 LEU A CB  
2064 C  CG  . LEU A 268 ? 0.0470 0.0582 0.0557 -0.0056 -0.0050 0.0105 268 LEU A CG  
2065 C  CD1 . LEU A 268 ? 0.0478 0.0590 0.0565 -0.0056 -0.0050 0.0105 268 LEU A CD1 
2066 C  CD2 . LEU A 268 ? 0.0781 0.0891 0.0867 -0.0055 -0.0050 0.0106 268 LEU A CD2 
2067 N  N   . LYS A 269 ? 0.1207 0.1293 0.1268 -0.0055 -0.0049 0.0120 269 LYS A N   
2068 C  CA  . LYS A 269 ? 0.0903 0.1018 0.0998 -0.0059 -0.0054 0.0109 269 LYS A CA  
2069 C  C   . LYS A 269 ? 0.1275 0.1363 0.1340 -0.0056 -0.0050 0.0123 269 LYS A C   
2070 O  O   . LYS A 269 ? 0.1339 0.1455 0.1436 -0.0059 -0.0054 0.0110 269 LYS A O   
2071 C  CB  . LYS A 269 ? 0.1241 0.1374 0.1346 -0.0075 -0.0069 0.0152 269 LYS A CB  
2072 C  CG  . LYS A 269 ? 0.1749 0.1882 0.1858 -0.0076 -0.0070 0.0154 269 LYS A CG  
2073 C  CD  . LYS A 269 ? 0.1920 0.2054 0.2031 -0.0077 -0.0071 0.0157 269 LYS A CD  
2074 C  CE  . LYS A 269 ? 0.2477 0.2613 0.2592 -0.0078 -0.0073 0.0160 269 LYS A CE  
2075 N  NZ  . LYS A 269 ? 0.2332 0.2453 0.2437 -0.0064 -0.0060 0.0118 269 LYS A NZ  
2076 N  N   . GLU A 270 ? 0.1394 0.1484 0.1457 -0.0058 -0.0052 0.0125 270 GLU A N   
2077 C  CA  . GLU A 270 ? 0.1680 0.1772 0.1744 -0.0059 -0.0053 0.0128 270 GLU A CA  
2078 C  C   . GLU A 270 ? 0.1671 0.1792 0.1768 -0.0063 -0.0056 0.0113 270 GLU A C   
2079 O  O   . GLU A 270 ? 0.1764 0.1886 0.1863 -0.0062 -0.0056 0.0114 270 GLU A O   
2080 C  CB  . GLU A 270 ? 0.1906 0.2031 0.2002 -0.0068 -0.0060 0.0117 270 GLU A CB  
2081 C  CG  . GLU A 270 ? 0.2696 0.2825 0.2795 -0.0069 -0.0061 0.0120 270 GLU A CG  
2082 C  CD  . GLU A 270 ? 0.3327 0.3426 0.3390 -0.0067 -0.0059 0.0137 270 GLU A CD  
2083 O  OE1 . GLU A 270 ? 0.3321 0.3453 0.3417 -0.0075 -0.0065 0.0123 270 GLU A OE1 
2084 O  OE2 . GLU A 270 ? 0.3432 0.3533 0.3497 -0.0068 -0.0060 0.0140 270 GLU A OE2 
2085 N  N   . LEU A 271 ? 0.1522 0.1613 0.1584 -0.0057 -0.0050 0.0123 271 LEU A N   
2086 C  CA  . LEU A 271 ? 0.1480 0.1570 0.1541 -0.0055 -0.0049 0.0122 271 LEU A CA  
2087 C  C   . LEU A 271 ? 0.1495 0.1628 0.1597 -0.0071 -0.0064 0.0148 271 LEU A C   
2088 O  O   . LEU A 271 ? 0.1633 0.1721 0.1697 -0.0051 -0.0046 0.0119 271 LEU A O   
2089 C  CB  . LEU A 271 ? 0.1421 0.1539 0.1512 -0.0060 -0.0053 0.0108 271 LEU A CB  
2090 C  CG  . LEU A 271 ? 0.1258 0.1350 0.1316 -0.0058 -0.0050 0.0122 271 LEU A CG  
2091 C  CD1 . LEU A 271 ? 0.0899 0.1018 0.0986 -0.0063 -0.0054 0.0108 271 LEU A CD1 
2092 C  CD2 . LEU A 271 ? 0.1351 0.1492 0.1448 -0.0079 -0.0069 0.0153 271 LEU A CD2 
2093 N  N   . LEU A 272 ? 0.1391 0.1522 0.1494 -0.0070 -0.0063 0.0146 272 LEU A N   
2094 C  CA  . LEU A 272 ? 0.1614 0.1742 0.1718 -0.0067 -0.0061 0.0143 272 LEU A CA  
2095 C  C   . LEU A 272 ? 0.1706 0.1790 0.1772 -0.0050 -0.0046 0.0117 272 LEU A C   
2096 O  O   . LEU A 272 ? 0.1851 0.1963 0.1948 -0.0053 -0.0049 0.0105 272 LEU A O   
2097 C  CB  . LEU A 272 ? 0.1500 0.1582 0.1564 -0.0048 -0.0044 0.0114 272 LEU A CB  
2098 C  CG  . LEU A 272 ? 0.1108 0.1217 0.1200 -0.0052 -0.0047 0.0103 272 LEU A CG  
2099 C  CD1 . LEU A 272 ? 0.0783 0.0891 0.0875 -0.0052 -0.0047 0.0103 272 LEU A CD1 
2100 C  CD2 . LEU A 272 ? 0.1268 0.1376 0.1359 -0.0051 -0.0046 0.0103 272 LEU A CD2 
2101 N  N   . GLN A 273 ? 0.1838 0.1968 0.1945 -0.0070 -0.0065 0.0149 273 GLN A N   
2102 C  CA  . GLN A 273 ? 0.2258 0.2343 0.2327 -0.0052 -0.0049 0.0122 273 GLN A CA  
2103 C  C   . GLN A 273 ? 0.1881 0.1998 0.1982 -0.0058 -0.0054 0.0112 273 GLN A C   
2104 O  O   . GLN A 273 ? 0.2274 0.2361 0.2345 -0.0053 -0.0049 0.0125 273 GLN A O   
2105 C  CB  . GLN A 273 ? 0.1882 0.1968 0.1952 -0.0054 -0.0051 0.0125 273 GLN A CB  
2106 C  CG  . GLN A 273 ? 0.1907 0.2021 0.2009 -0.0058 -0.0055 0.0111 273 GLN A CG  
2107 C  CD  . GLN A 273 ? 0.1946 0.2032 0.2018 -0.0055 -0.0052 0.0126 273 GLN A CD  
2108 O  OE1 . GLN A 273 ? 0.2824 0.2959 0.2938 -0.0077 -0.0072 0.0160 273 GLN A OE1 
2109 N  NE2 . GLN A 273 ? 0.1722 0.1806 0.1794 -0.0054 -0.0052 0.0126 273 GLN A NE2 
2110 N  N   . ASN A 274 ? 0.2174 0.2294 0.2275 -0.0059 -0.0054 0.0112 274 ASN A N   
2111 C  CA  . ASN A 274 ? 0.2175 0.2298 0.2277 -0.0060 -0.0055 0.0114 274 ASN A CA  
2112 C  C   . ASN A 274 ? 0.2126 0.2219 0.2195 -0.0053 -0.0049 0.0126 274 ASN A C   
2113 O  O   . ASN A 274 ? 0.1715 0.1840 0.1817 -0.0059 -0.0053 0.0115 274 ASN A O   
2114 C  CB  . ASN A 274 ? 0.1685 0.1780 0.1755 -0.0057 -0.0052 0.0131 274 ASN A CB  
2115 C  CG  . ASN A 274 ? 0.2426 0.2570 0.2539 -0.0080 -0.0073 0.0164 274 ASN A CG  
2116 O  OD1 . ASN A 274 ? 0.3315 0.3440 0.3421 -0.0063 -0.0058 0.0119 274 ASN A OD1 
2117 N  ND2 . ASN A 274 ? 0.2713 0.2859 0.2826 -0.0082 -0.0075 0.0165 274 ASN A ND2 
2118 N  N   . GLY A 275 ? 0.2490 0.2611 0.2589 -0.0057 -0.0051 0.0111 275 GLY A N   
2119 C  CA  . GLY A 275 ? 0.1646 0.1767 0.1744 -0.0056 -0.0050 0.0110 275 GLY A CA  
2120 C  C   . GLY A 275 ? 0.1800 0.1894 0.1865 -0.0053 -0.0047 0.0124 275 GLY A C   
2121 O  O   . GLY A 275 ? 0.1947 0.2042 0.2012 -0.0055 -0.0049 0.0126 275 GLY A O   
2122 N  N   . MET A 276 ? 0.2227 0.2323 0.2293 -0.0053 -0.0046 0.0124 276 MET A N   
2123 C  CA  . MET A 276 ? 0.1980 0.2108 0.2077 -0.0060 -0.0052 0.0113 276 MET A CA  
2124 C  C   . MET A 276 ? 0.2721 0.2853 0.2821 -0.0061 -0.0053 0.0117 276 MET A C   
2125 O  O   . MET A 276 ? 0.2872 0.3007 0.2971 -0.0064 -0.0055 0.0119 276 MET A O   
2126 C  CB  . MET A 276 ? 0.2402 0.2549 0.2505 -0.0072 -0.0063 0.0153 276 MET A CB  
2127 C  CG  . MET A 276 ? 0.1938 0.2062 0.2031 -0.0057 -0.0050 0.0109 276 MET A CG  
2128 S  SD  . MET A 276 ? 0.3620 0.3744 0.3710 -0.0059 -0.0050 0.0110 276 MET A SD  
2129 C  CE  . MET A 276 ? 0.2011 0.2132 0.2100 -0.0056 -0.0048 0.0109 276 MET A CE  
2130 N  N   . ASN A 277 ? 0.2437 0.2570 0.2539 -0.0060 -0.0053 0.0117 277 ASN A N   
2131 C  CA  . ASN A 277 ? 0.2752 0.2910 0.2866 -0.0077 -0.0067 0.0166 277 ASN A CA  
2132 C  C   . ASN A 277 ? 0.3209 0.3317 0.3279 -0.0056 -0.0049 0.0135 277 ASN A C   
2133 O  O   . ASN A 277 ? 0.3505 0.3616 0.3576 -0.0058 -0.0050 0.0138 277 ASN A O   
2134 C  CB  . ASN A 277 ? 0.3230 0.3390 0.3343 -0.0081 -0.0071 0.0170 277 ASN A CB  
2135 C  CG  . ASN A 277 ? 0.4162 0.4304 0.4271 -0.0066 -0.0058 0.0126 277 ASN A CG  
2136 O  OD1 . ASN A 277 ? 0.4393 0.4534 0.4503 -0.0064 -0.0057 0.0125 277 ASN A OD1 
2137 N  ND2 . ASN A 277 ? 0.4635 0.4781 0.4745 -0.0069 -0.0060 0.0130 277 ASN A ND2 
2138 N  N   . GLY A 278 ? 0.2432 0.2570 0.2536 -0.0059 -0.0051 0.0119 278 GLY A N   
2139 C  CA  . GLY A 278 ? 0.2417 0.2579 0.2531 -0.0073 -0.0063 0.0164 278 GLY A CA  
2140 C  C   . GLY A 278 ? 0.2901 0.3011 0.2969 -0.0056 -0.0048 0.0133 278 GLY A C   
2141 O  O   . GLY A 278 ? 0.2892 0.3060 0.3005 -0.0077 -0.0065 0.0168 278 GLY A O   
2142 N  N   . ARG A 279 ? 0.2473 0.2613 0.2574 -0.0063 -0.0054 0.0120 279 ARG A N   
2143 C  CA  . ARG A 279 ? 0.2529 0.2669 0.2627 -0.0066 -0.0055 0.0120 279 ARG A CA  
2144 C  C   . ARG A 279 ? 0.2043 0.2179 0.2139 -0.0064 -0.0054 0.0117 279 ARG A C   
2145 O  O   . ARG A 279 ? 0.1676 0.1809 0.1771 -0.0060 -0.0051 0.0114 279 ARG A O   
2146 C  CB  . ARG A 279 ? 0.2741 0.2904 0.2845 -0.0086 -0.0072 0.0168 279 ARG A CB  
2147 C  CG  . ARG A 279 ? 0.3142 0.3252 0.3205 -0.0064 -0.0054 0.0138 279 ARG A CG  
2148 C  CD  . ARG A 279 ? 0.2510 0.2653 0.2609 -0.0073 -0.0062 0.0126 279 ARG A CD  
2149 N  NE  . ARG A 279 ? 0.3205 0.3351 0.3303 -0.0077 -0.0064 0.0128 279 ARG A NE  
2150 C  CZ  . ARG A 279 ? 0.3847 0.3993 0.3943 -0.0080 -0.0066 0.0129 279 ARG A CZ  
2151 N  NH1 . ARG A 279 ? 0.3504 0.3617 0.3562 -0.0074 -0.0061 0.0144 279 ARG A NH1 
2152 N  NH2 . ARG A 279 ? 0.3725 0.3897 0.3822 -0.0104 -0.0085 0.0180 279 ARG A NH2 
2153 N  N   . THR A 280 ? 0.1967 0.2103 0.2060 -0.0066 -0.0055 0.0117 280 THR A N   
2154 C  CA  . THR A 280 ? 0.1539 0.1673 0.1630 -0.0065 -0.0054 0.0115 280 THR A CA  
2155 C  C   . THR A 280 ? 0.1539 0.1671 0.1626 -0.0067 -0.0056 0.0115 280 THR A C   
2156 O  O   . THR A 280 ? 0.1634 0.1767 0.1721 -0.0071 -0.0058 0.0115 280 THR A O   
2157 C  CB  . THR A 280 ? 0.1820 0.1956 0.1911 -0.0065 -0.0054 0.0117 280 THR A CB  
2158 O  OG1 . THR A 280 ? 0.1756 0.1895 0.1847 -0.0068 -0.0056 0.0119 280 THR A OG1 
2159 C  CG2 . THR A 280 ? 0.1138 0.1276 0.1233 -0.0062 -0.0051 0.0118 280 THR A CG2 
2160 N  N   . ILE A 281 ? 0.1206 0.1335 0.1291 -0.0066 -0.0055 0.0114 281 ILE A N   
2161 C  CA  . ILE A 281 ? 0.0878 0.1006 0.0960 -0.0068 -0.0057 0.0114 281 ILE A CA  
2162 C  C   . ILE A 281 ? 0.1302 0.1429 0.1382 -0.0069 -0.0057 0.0115 281 ILE A C   
2163 O  O   . ILE A 281 ? 0.1075 0.1202 0.1156 -0.0066 -0.0054 0.0114 281 ILE A O   
2164 C  CB  . ILE A 281 ? 0.1068 0.1193 0.1150 -0.0067 -0.0056 0.0112 281 ILE A CB  
2165 C  CG1 . ILE A 281 ? 0.1200 0.1325 0.1284 -0.0066 -0.0056 0.0111 281 ILE A CG1 
2166 C  CG2 . ILE A 281 ? 0.1086 0.1209 0.1164 -0.0069 -0.0058 0.0112 281 ILE A CG2 
2167 C  CD1 . ILE A 281 ? 0.1071 0.1193 0.1154 -0.0066 -0.0056 0.0110 281 ILE A CD1 
2168 N  N   . LEU A 282 ? 0.1268 0.1396 0.1345 -0.0072 -0.0059 0.0116 282 LEU A N   
2169 C  CA  . LEU A 282 ? 0.1761 0.1889 0.1836 -0.0073 -0.0059 0.0117 282 LEU A CA  
2170 C  C   . LEU A 282 ? 0.1854 0.1983 0.1932 -0.0070 -0.0057 0.0118 282 LEU A C   
2171 O  O   . LEU A 282 ? 0.1190 0.1319 0.1268 -0.0068 -0.0056 0.0118 282 LEU A O   
2172 C  CB  . LEU A 282 ? 0.1108 0.1233 0.1181 -0.0073 -0.0059 0.0116 282 LEU A CB  
2173 C  CG  . LEU A 282 ? 0.1300 0.1423 0.1369 -0.0077 -0.0062 0.0117 282 LEU A CG  
2174 C  CD1 . LEU A 282 ? 0.0898 0.1019 0.0965 -0.0076 -0.0061 0.0116 282 LEU A CD1 
2175 C  CD2 . LEU A 282 ? 0.1131 0.1256 0.1196 -0.0082 -0.0065 0.0119 282 LEU A CD2 
2176 N  N   . GLY A 283 ? 0.1326 0.1458 0.1407 -0.0069 -0.0057 0.0118 283 GLY A N   
2177 C  CA  . GLY A 283 ? 0.1322 0.1457 0.1407 -0.0066 -0.0054 0.0119 283 GLY A CA  
2178 C  C   . GLY A 283 ? 0.1679 0.1813 0.1766 -0.0062 -0.0051 0.0118 283 GLY A C   
2179 O  O   . GLY A 283 ? 0.1893 0.2027 0.1981 -0.0059 -0.0049 0.0119 283 GLY A O   
2180 N  N   . SER A 284 ? 0.0897 0.1027 0.0983 -0.0061 -0.0051 0.0116 284 SER A N   
2181 C  CA  . SER A 284 ? 0.1258 0.1387 0.1346 -0.0057 -0.0048 0.0115 284 SER A CA  
2182 C  C   . SER A 284 ? 0.1488 0.1617 0.1577 -0.0057 -0.0048 0.0114 284 SER A C   
2183 O  O   . SER A 284 ? 0.0552 0.0680 0.0641 -0.0059 -0.0050 0.0114 284 SER A O   
2184 C  CB  . SER A 284 ? 0.1358 0.1483 0.1443 -0.0057 -0.0048 0.0114 284 SER A CB  
2185 O  OG  . SER A 284 ? 0.1242 0.1367 0.1329 -0.0053 -0.0045 0.0114 284 SER A OG  
2186 N  N   . ALA A 285 ? 0.1005 0.1134 0.1097 -0.0054 -0.0046 0.0115 285 ALA A N   
2187 C  CA  . ALA A 285 ? 0.0823 0.0952 0.0917 -0.0054 -0.0046 0.0114 285 ALA A CA  
2188 C  C   . ALA A 285 ? 0.1228 0.1354 0.1321 -0.0052 -0.0045 0.0113 285 ALA A C   
2189 O  O   . ALA A 285 ? 0.0991 0.1116 0.1085 -0.0052 -0.0044 0.0112 285 ALA A O   
2190 C  CB  . ALA A 285 ? 0.1295 0.1427 0.1392 -0.0052 -0.0044 0.0116 285 ALA A CB  
2191 N  N   . LEU A 286 ? 0.1229 0.1352 0.1320 -0.0052 -0.0044 0.0112 286 LEU A N   
2192 C  CA  . LEU A 286 ? 0.1501 0.1622 0.1592 -0.0051 -0.0044 0.0110 286 LEU A CA  
2193 C  C   . LEU A 286 ? 0.1390 0.1509 0.1479 -0.0052 -0.0045 0.0109 286 LEU A C   
2194 O  O   . LEU A 286 ? 0.0984 0.1104 0.1071 -0.0053 -0.0046 0.0110 286 LEU A O   
2195 C  CB  . LEU A 286 ? 0.1267 0.1387 0.1359 -0.0048 -0.0042 0.0111 286 LEU A CB  
2196 C  CG  . LEU A 286 ? 0.2016 0.2138 0.2108 -0.0046 -0.0040 0.0113 286 LEU A CG  
2197 C  CD1 . LEU A 286 ? 0.1998 0.2119 0.2088 -0.0046 -0.0040 0.0113 286 LEU A CD1 
2198 C  CD2 . LEU A 286 ? 0.1631 0.1753 0.1725 -0.0043 -0.0037 0.0114 286 LEU A CD2 
2199 N  N   . LEU A 287 ? 0.1010 0.1127 0.1098 -0.0051 -0.0045 0.0108 287 LEU A N   
2200 C  CA  . LEU A 287 ? 0.1101 0.1216 0.1187 -0.0052 -0.0046 0.0108 287 LEU A CA  
2201 C  C   . LEU A 287 ? 0.0646 0.0761 0.0731 -0.0051 -0.0044 0.0108 287 LEU A C   
2202 O  O   . LEU A 287 ? 0.0522 0.0636 0.0608 -0.0049 -0.0043 0.0109 287 LEU A O   
2203 C  CB  . LEU A 287 ? 0.1057 0.1170 0.1143 -0.0052 -0.0046 0.0106 287 LEU A CB  
2204 C  CG  . LEU A 287 ? 0.1310 0.1424 0.1397 -0.0053 -0.0047 0.0106 287 LEU A CG  
2205 C  CD1 . LEU A 287 ? 0.1325 0.1438 0.1414 -0.0053 -0.0047 0.0105 287 LEU A CD1 
2206 C  CD2 . LEU A 287 ? 0.1345 0.1461 0.1431 -0.0056 -0.0049 0.0106 287 LEU A CD2 
2207 N  N   . GLU A 288 ? 0.0692 0.0808 0.0776 -0.0053 -0.0046 0.0109 288 GLU A N   
2208 C  CA  . GLU A 288 ? 0.0825 0.0940 0.0907 -0.0051 -0.0044 0.0110 288 GLU A CA  
2209 C  C   . GLU A 288 ? 0.0667 0.0780 0.0748 -0.0051 -0.0044 0.0110 288 GLU A C   
2210 O  O   . GLU A 288 ? 0.0383 0.0496 0.0463 -0.0054 -0.0046 0.0110 288 GLU A O   
2211 C  CB  . GLU A 288 ? 0.0667 0.0784 0.0748 -0.0054 -0.0046 0.0112 288 GLU A CB  
2212 C  CG  . GLU A 288 ? 0.1267 0.1386 0.1349 -0.0054 -0.0046 0.0112 288 GLU A CG  
2213 C  CD  . GLU A 288 ? 0.2810 0.2931 0.2894 -0.0051 -0.0043 0.0113 288 GLU A CD  
2214 O  OE1 . GLU A 288 ? 0.2533 0.2656 0.2620 -0.0050 -0.0042 0.0114 288 GLU A OE1 
2215 O  OE2 . GLU A 288 ? 0.1986 0.2107 0.2070 -0.0049 -0.0042 0.0114 288 GLU A OE2 
2216 N  N   . ASP A 289 ? 0.0639 0.0752 0.0722 -0.0048 -0.0042 0.0110 289 ASP A N   
2217 C  CA  . ASP A 289 ? 0.0564 0.0676 0.0647 -0.0048 -0.0042 0.0111 289 ASP A CA  
2218 C  C   . ASP A 289 ? 0.0580 0.0693 0.0662 -0.0047 -0.0041 0.0112 289 ASP A C   
2219 O  O   . ASP A 289 ? 0.0727 0.0840 0.0811 -0.0045 -0.0040 0.0113 289 ASP A O   
2220 C  CB  . ASP A 289 ? 0.0582 0.0693 0.0667 -0.0046 -0.0041 0.0110 289 ASP A CB  
2221 C  CG  . ASP A 289 ? 0.0984 0.1095 0.1071 -0.0042 -0.0038 0.0111 289 ASP A CG  
2222 O  OD1 . ASP A 289 ? 0.0331 0.0444 0.0418 -0.0041 -0.0037 0.0112 289 ASP A OD1 
2223 O  OD2 . ASP A 289 ? 0.0721 0.0831 0.0809 -0.0041 -0.0037 0.0110 289 ASP A OD2 
2224 N  N   . GLU A 290 ? 0.0476 0.0590 0.0557 -0.0047 -0.0041 0.0113 290 GLU A N   
2225 C  CA  . GLU A 290 ? 0.0961 0.1067 0.1034 -0.0044 -0.0038 0.0112 290 GLU A CA  
2226 C  C   . GLU A 290 ? 0.1052 0.1156 0.1120 -0.0047 -0.0040 0.0113 290 GLU A C   
2227 O  O   . GLU A 290 ? 0.1189 0.1284 0.1248 -0.0044 -0.0037 0.0111 290 GLU A O   
2228 C  CB  . GLU A 290 ? 0.1022 0.1124 0.1092 -0.0039 -0.0034 0.0111 290 GLU A CB  
2229 C  CG  . GLU A 290 ? 0.1159 0.1260 0.1230 -0.0036 -0.0031 0.0110 290 GLU A CG  
2230 C  CD  . GLU A 290 ? 0.2443 0.2533 0.2505 -0.0029 -0.0026 0.0108 290 GLU A CD  
2231 O  OE1 . GLU A 290 ? 0.1362 0.1449 0.1419 -0.0027 -0.0024 0.0108 290 GLU A OE1 
2232 O  OE2 . GLU A 290 ? 0.2129 0.2214 0.2188 -0.0025 -0.0023 0.0107 290 GLU A OE2 
2233 N  N   . PHE A 291 ? 0.0507 0.0618 0.0580 -0.0053 -0.0045 0.0115 291 PHE A N   
2234 C  CA  . PHE A 291 ? 0.0784 0.0890 0.0849 -0.0055 -0.0046 0.0115 291 PHE A CA  
2235 C  C   . PHE A 291 ? 0.0730 0.0835 0.0795 -0.0056 -0.0046 0.0115 291 PHE A C   
2236 O  O   . PHE A 291 ? 0.0480 0.0593 0.0553 -0.0059 -0.0050 0.0116 291 PHE A O   
2237 C  CB  . PHE A 291 ? 0.0714 0.0828 0.0784 -0.0062 -0.0052 0.0117 291 PHE A CB  
2238 C  CG  . PHE A 291 ? 0.1253 0.1368 0.1322 -0.0062 -0.0051 0.0117 291 PHE A CG  
2239 C  CD1 . PHE A 291 ? 0.1328 0.1439 0.1391 -0.0063 -0.0051 0.0117 291 PHE A CD1 
2240 C  CD2 . PHE A 291 ? 0.0963 0.1079 0.1035 -0.0061 -0.0050 0.0116 291 PHE A CD2 
2241 C  CE1 . PHE A 291 ? 0.1217 0.1332 0.1283 -0.0063 -0.0051 0.0118 291 PHE A CE1 
2242 C  CE2 . PHE A 291 ? 0.1092 0.1209 0.1164 -0.0061 -0.0050 0.0116 291 PHE A CE2 
2243 C  CZ  . PHE A 291 ? 0.1180 0.1299 0.1251 -0.0062 -0.0051 0.0118 291 PHE A CZ  
2244 N  N   . THR A 292 ? 0.0642 0.0735 0.0696 -0.0052 -0.0042 0.0113 292 THR A N   
2245 C  CA  . THR A 292 ? 0.0868 0.0959 0.0921 -0.0052 -0.0042 0.0113 292 THR A CA  
2246 C  C   . THR A 292 ? 0.0984 0.1077 0.1035 -0.0058 -0.0047 0.0115 292 THR A C   
2247 O  O   . THR A 292 ? 0.0971 0.1064 0.1019 -0.0062 -0.0049 0.0116 292 THR A O   
2248 C  CB  . THR A 292 ? 0.0922 0.0999 0.0963 -0.0046 -0.0036 0.0111 292 THR A CB  
2249 O  OG1 . THR A 292 ? 0.1064 0.1133 0.1094 -0.0047 -0.0036 0.0111 292 THR A OG1 
2250 C  CG2 . THR A 292 ? 0.1079 0.1153 0.1120 -0.0040 -0.0032 0.0109 292 THR A CG2 
2251 N  N   . PRO A 293 ? 0.0652 0.0746 0.0704 -0.0060 -0.0048 0.0116 293 PRO A N   
2252 C  CA  . PRO A 293 ? 0.0638 0.0731 0.0685 -0.0065 -0.0051 0.0118 293 PRO A CA  
2253 C  C   . PRO A 293 ? 0.1074 0.1154 0.1105 -0.0065 -0.0049 0.0117 293 PRO A C   
2254 O  O   . PRO A 293 ? 0.0734 0.0815 0.0762 -0.0071 -0.0053 0.0118 293 PRO A O   
2255 C  CB  . PRO A 293 ? 0.0505 0.0597 0.0552 -0.0064 -0.0051 0.0119 293 PRO A CB  
2256 C  CG  . PRO A 293 ? 0.0711 0.0811 0.0770 -0.0061 -0.0050 0.0119 293 PRO A CG  
2257 C  CD  . PRO A 293 ? 0.0926 0.1022 0.0984 -0.0057 -0.0047 0.0117 293 PRO A CD  
2258 N  N   . PHE A 294 ? 0.1162 0.1231 0.1186 -0.0059 -0.0043 0.0115 294 PHE A N   
2259 C  CA  . PHE A 294 ? 0.1415 0.1471 0.1424 -0.0058 -0.0040 0.0113 294 PHE A CA  
2260 C  C   . PHE A 294 ? 0.1572 0.1632 0.1583 -0.0061 -0.0042 0.0113 294 PHE A C   
2261 O  O   . PHE A 294 ? 0.1756 0.1812 0.1759 -0.0066 -0.0044 0.0114 294 PHE A O   
2262 C  CB  . PHE A 294 ? 0.2324 0.2368 0.2325 -0.0051 -0.0033 0.0111 294 PHE A CB  
2263 C  CG  . PHE A 294 ? 0.3468 0.3497 0.3453 -0.0050 -0.0029 0.0110 294 PHE A CG  
2264 C  CD1 . PHE A 294 ? 0.3547 0.3574 0.3527 -0.0052 -0.0030 0.0110 294 PHE A CD1 
2265 C  CD2 . PHE A 294 ? 0.4202 0.4221 0.4179 -0.0048 -0.0025 0.0110 294 PHE A CD2 
2266 C  CE1 . PHE A 294 ? 0.3998 0.4011 0.3964 -0.0051 -0.0026 0.0109 294 PHE A CE1 
2267 C  CE2 . PHE A 294 ? 0.4475 0.4479 0.4436 -0.0047 -0.0021 0.0109 294 PHE A CE2 
2268 C  CZ  . PHE A 294 ? 0.4388 0.4390 0.4345 -0.0049 -0.0022 0.0109 294 PHE A CZ  
2269 N  N   . ASP A 295 ? 0.1335 0.1402 0.1355 -0.0059 -0.0042 0.0113 295 ASP A N   
2270 C  CA  . ASP A 295 ? 0.1510 0.1581 0.1532 -0.0061 -0.0044 0.0113 295 ASP A CA  
2271 C  C   . ASP A 295 ? 0.1329 0.1410 0.1356 -0.0069 -0.0051 0.0116 295 ASP A C   
2272 O  O   . ASP A 295 ? 0.1122 0.1203 0.1146 -0.0073 -0.0053 0.0116 295 ASP A O   
2273 C  CB  . ASP A 295 ? 0.0742 0.0820 0.0774 -0.0057 -0.0043 0.0113 295 ASP A CB  
2274 C  CG  . ASP A 295 ? 0.1597 0.1665 0.1623 -0.0049 -0.0036 0.0110 295 ASP A CG  
2275 O  OD1 . ASP A 295 ? 0.1442 0.1498 0.1456 -0.0046 -0.0033 0.0109 295 ASP A OD1 
2276 O  OD2 . ASP A 295 ? 0.1556 0.1628 0.1588 -0.0046 -0.0035 0.0110 295 ASP A OD2 
2277 N  N   . VAL A 296 ? 0.0800 0.0890 0.0835 -0.0073 -0.0055 0.0117 296 VAL A N   
2278 C  CA  . VAL A 296 ? 0.0829 0.0929 0.0870 -0.0081 -0.0062 0.0120 296 VAL A CA  
2279 C  C   . VAL A 296 ? 0.1511 0.1604 0.1540 -0.0086 -0.0064 0.0120 296 VAL A C   
2280 O  O   . VAL A 296 ? 0.1614 0.1709 0.1641 -0.0092 -0.0068 0.0121 296 VAL A O   
2281 C  CB  . VAL A 296 ? 0.1005 0.1115 0.1056 -0.0082 -0.0065 0.0121 296 VAL A CB  
2282 C  CG1 . VAL A 296 ? 0.0977 0.1087 0.1025 -0.0087 -0.0068 0.0121 296 VAL A CG1 
2283 C  CG2 . VAL A 296 ? 0.0744 0.0856 0.0802 -0.0076 -0.0061 0.0119 296 VAL A CG2 
2284 N  N   . VAL A 297 ? 0.1424 0.1506 0.1444 -0.0084 -0.0061 0.0119 297 VAL A N   
2285 C  CA  . VAL A 297 ? 0.2254 0.2327 0.2260 -0.0088 -0.0061 0.0119 297 VAL A CA  
2286 C  C   . VAL A 297 ? 0.2305 0.2368 0.2300 -0.0087 -0.0059 0.0118 297 VAL A C   
2287 O  O   . VAL A 297 ? 0.2295 0.2356 0.2283 -0.0094 -0.0062 0.0119 297 VAL A O   
2288 C  CB  . VAL A 297 ? 0.1419 0.1482 0.1417 -0.0085 -0.0057 0.0119 297 VAL A CB  
2289 C  CG1 . VAL A 297 ? 0.1780 0.1830 0.1762 -0.0087 -0.0055 0.0118 297 VAL A CG1 
2290 C  CG2 . VAL A 297 ? 0.1707 0.1779 0.1714 -0.0087 -0.0061 0.0121 297 VAL A CG2 
2291 N  N   . ARG A 298 ? 0.2083 0.2140 0.2076 -0.0080 -0.0053 0.0116 298 ARG A N   
2292 C  CA  . ARG A 298 ? 0.2961 0.3010 0.2946 -0.0079 -0.0051 0.0115 298 ARG A CA  
2293 C  C   . ARG A 298 ? 0.2997 0.3056 0.2988 -0.0085 -0.0056 0.0116 298 ARG A C   
2294 O  O   . ARG A 298 ? 0.3558 0.3613 0.3541 -0.0090 -0.0058 0.0117 298 ARG A O   
2295 C  CB  . ARG A 298 ? 0.2603 0.2646 0.2587 -0.0070 -0.0044 0.0113 298 ARG A CB  
2296 C  CG  . ARG A 298 ? 0.4379 0.4412 0.4353 -0.0069 -0.0041 0.0111 298 ARG A CG  
2297 C  CD  . ARG A 298 ? 0.4291 0.4322 0.4268 -0.0060 -0.0036 0.0110 298 ARG A CD  
2298 N  NE  . ARG A 298 ? 0.4483 0.4526 0.4473 -0.0060 -0.0038 0.0110 298 ARG A NE  
2299 C  CZ  . ARG A 298 ? 0.2811 0.2855 0.2804 -0.0055 -0.0035 0.0110 298 ARG A CZ  
2300 N  NH1 . ARG A 298 ? 0.2962 0.2996 0.2946 -0.0051 -0.0031 0.0108 298 ARG A NH1 
2301 N  NH2 . ARG A 298 ? 0.2076 0.2132 0.2081 -0.0055 -0.0037 0.0111 298 ARG A NH2 
2302 N  N   . GLN A 299 ? 0.2475 0.2546 0.2479 -0.0085 -0.0059 0.0117 299 GLN A N   
2303 C  CA  . GLN A 299 ? 0.2186 0.2268 0.2198 -0.0090 -0.0064 0.0119 299 GLN A CA  
2304 C  C   . GLN A 299 ? 0.3178 0.3268 0.3193 -0.0099 -0.0071 0.0122 299 GLN A C   
2305 O  O   . GLN A 299 ? 0.3786 0.3883 0.3803 -0.0105 -0.0075 0.0124 299 GLN A O   
2306 C  CB  . GLN A 299 ? 0.2491 0.2583 0.2517 -0.0086 -0.0063 0.0120 299 GLN A CB  
2307 C  CG  . GLN A 299 ? 0.2193 0.2295 0.2226 -0.0090 -0.0067 0.0122 299 GLN A CG  
2308 C  CD  . GLN A 299 ? 0.2036 0.2144 0.2079 -0.0084 -0.0064 0.0122 299 GLN A CD  
2309 O  OE1 . GLN A 299 ? 0.2005 0.2121 0.2054 -0.0086 -0.0066 0.0124 299 GLN A OE1 
2310 N  NE2 . GLN A 299 ? 0.1579 0.1683 0.1622 -0.0078 -0.0059 0.0120 299 GLN A NE2 
2311 N  N   . CYS A 300 ? 0.2831 0.2922 0.2845 -0.0102 -0.0073 0.0122 300 CYS A N   
2312 C  CA  . CYS A 300 ? 0.3695 0.3792 0.3710 -0.0111 -0.0080 0.0125 300 CYS A CA  
2313 C  C   . CYS A 300 ? 0.3935 0.4020 0.3934 -0.0115 -0.0079 0.0124 300 CYS A C   
2314 O  O   . CYS A 300 ? 0.5287 0.5374 0.5284 -0.0121 -0.0084 0.0125 300 CYS A O   
2315 C  CB  . CYS A 300 ? 0.3259 0.3362 0.3283 -0.0109 -0.0080 0.0125 300 CYS A CB  
2316 S  SG  . CYS A 300 ? 0.2905 0.3014 0.2940 -0.0100 -0.0075 0.0123 300 CYS A SG  
2317 N  N   . SER A 301 ? 0.5018 0.5089 0.5005 -0.0111 -0.0074 0.0122 301 SER A N   
2318 C  CA  . SER A 301 ? 0.5105 0.5161 0.5074 -0.0114 -0.0072 0.0121 301 SER A CA  
2319 C  C   . SER A 301 ? 0.6099 0.6148 0.6059 -0.0115 -0.0071 0.0120 301 SER A C   
2320 O  O   . SER A 301 ? 0.6025 0.6068 0.5975 -0.0122 -0.0073 0.0120 301 SER A O   
2321 C  CB  . SER A 301 ? 0.4900 0.4945 0.4863 -0.0106 -0.0065 0.0119 301 SER A CB  
2322 O  OG  . SER A 301 ? 0.5214 0.5265 0.5182 -0.0107 -0.0067 0.0120 301 SER A OG  
2323 N  N   . GLY A 302 ? 0.6837 0.6885 0.6801 -0.0109 -0.0067 0.0118 302 GLY A N   
2324 C  CA  . GLY A 302 ? 0.6513 0.6555 0.6469 -0.0109 -0.0066 0.0118 302 GLY A CA  
2325 C  C   . GLY A 302 ? 0.7551 0.7576 0.7494 -0.0103 -0.0058 0.0115 302 GLY A C   
2326 O  O   . GLY A 302 ? 0.7780 0.7796 0.7711 -0.0106 -0.0057 0.0114 302 GLY A O   
2327 N  N   . VAL A 303 ? 0.7855 0.7877 0.7801 -0.0094 -0.0053 0.0114 303 VAL A N   
2328 C  CA  . VAL A 303 ? 0.9263 0.9270 0.9197 -0.0087 -0.0045 0.0112 303 VAL A CA  
2329 C  C   . VAL A 303 ? 0.9812 0.9815 0.9745 -0.0082 -0.0041 0.0111 303 VAL A C   
2330 O  O   . VAL A 303 ? 0.9717 0.9730 0.9660 -0.0080 -0.0042 0.0111 303 VAL A O   
2331 C  CB  . VAL A 303 ? 0.9733 0.9739 0.9671 -0.0081 -0.0041 0.0111 303 VAL A CB  
2332 C  CG1 . VAL A 303 ? 1.0930 1.0922 1.0859 -0.0072 -0.0032 0.0109 303 VAL A CG1 
2333 C  CG2 . VAL A 303 ? 0.9441 0.9447 0.9377 -0.0085 -0.0043 0.0112 303 VAL A CG2 
2334 N  N   . THR A 304 ? 0.9961 0.9950 0.9880 -0.0080 -0.0036 0.0109 304 THR A N   
2335 C  CA  . THR A 304 ? 0.8704 0.8687 0.8620 -0.0076 -0.0032 0.0108 304 THR A CA  
2336 C  C   . THR A 304 ? 0.9803 0.9775 0.9713 -0.0066 -0.0023 0.0107 304 THR A C   
2337 O  O   . THR A 304 ? 0.9905 0.9871 0.9811 -0.0064 -0.0020 0.0106 304 THR A O   
2338 C  CB  . THR A 304 ? 0.7247 0.7225 0.7153 -0.0083 -0.0034 0.0109 304 THR A CB  
2339 O  OG1 . THR A 304 ? 0.8820 0.8788 0.8714 -0.0086 -0.0033 0.0108 304 THR A OG1 
2340 C  CG2 . THR A 304 ? 0.6557 0.6548 0.6470 -0.0092 -0.0043 0.0111 304 THR A CG2 
2341 N  N   . PHE A 305 ? 0.9008 0.8976 0.8917 -0.0060 -0.0019 0.0106 305 PHE A N   
2342 C  CA  . PHE A 305 ? 0.9604 0.9562 0.9508 -0.0051 -0.0011 0.0104 305 PHE A CA  
2343 C  C   . PHE A 305 ? 0.8927 0.8876 0.8822 -0.0048 -0.0007 0.0104 305 PHE A C   
2344 O  O   . PHE A 305 ? 0.8020 0.7969 0.7911 -0.0055 -0.0010 0.0105 305 PHE A O   
2345 C  CB  . PHE A 305 ? 0.8726 0.8689 0.8639 -0.0044 -0.0009 0.0103 305 PHE A CB  
2346 C  CG  . PHE A 305 ? 1.0279 1.0253 1.0202 -0.0047 -0.0014 0.0104 305 PHE A CG  
2347 C  CD1 . PHE A 305 ? 1.0991 1.0962 1.0914 -0.0044 -0.0012 0.0104 305 PHE A CD1 
2348 C  CD2 . PHE A 305 ? 1.1275 1.1263 1.1210 -0.0051 -0.0020 0.0105 305 PHE A CD2 
2349 C  CE1 . PHE A 305 ? 1.1725 1.1706 1.1657 -0.0047 -0.0016 0.0105 305 PHE A CE1 
2350 C  CE2 . PHE A 305 ? 1.1752 1.1751 1.1698 -0.0054 -0.0024 0.0106 305 PHE A CE2 
2351 C  CZ  . PHE A 305 ? 1.1726 1.1722 1.1670 -0.0052 -0.0022 0.0106 305 PHE A CZ  
2352 C  C1  . XEK B .   ? 0.1225 0.1191 0.1163 0.0057  0.0037  0.0076 401 XEK A C1  
2353 C  C2  . XEK B .   ? 0.1126 0.1085 0.1058 0.0063  0.0040  0.0073 401 XEK A C2  
2354 C  C3  . XEK B .   ? 0.1529 0.1484 0.1457 0.0062  0.0038  0.0073 401 XEK A C3  
2355 C  C4  . XEK B .   ? 0.1124 0.1078 0.1052 0.0062  0.0039  0.0072 401 XEK A C4  
2356 C  C5  . XEK B .   ? 0.1484 0.1434 0.1409 0.0061  0.0037  0.0072 401 XEK A C5  
2357 C  C6  . XEK B .   ? 0.2159 0.2106 0.2081 0.0060  0.0033  0.0073 401 XEK A C6  
2358 C  C7  . XEK B .   ? 0.1962 0.1910 0.1884 0.0059  0.0032  0.0074 401 XEK A C7  
2359 C  C8  . XEK B .   ? 0.2274 0.2222 0.2198 0.0053  0.0025  0.0077 401 XEK A C8  
2360 C  C9  . XEK B .   ? 0.2191 0.2138 0.2116 0.0048  0.0019  0.0079 401 XEK A C9  
2361 C  C10 . XEK B .   ? 0.2203 0.2154 0.2134 0.0043  0.0016  0.0081 401 XEK A C10 
2362 C  C11 . XEK B .   ? 0.2181 0.2130 0.2112 0.0038  0.0010  0.0082 401 XEK A C11 
2363 C  C12 . XEK B .   ? 0.2923 0.2866 0.2849 0.0038  0.0007  0.0083 401 XEK A C12 
2364 C  C13 . XEK B .   ? 0.2837 0.2776 0.2757 0.0042  0.0010  0.0082 401 XEK A C13 
2365 C  C14 . XEK B .   ? 0.2908 0.2849 0.2827 0.0047  0.0016  0.0080 401 XEK A C14 
2366 C  C15 . XEK B .   ? 0.1541 0.1493 0.1466 0.0060  0.0035  0.0074 401 XEK A C15 
2367 C  C17 . XEK B .   ? 0.1753 0.1715 0.1686 0.0069  0.0047  0.0072 401 XEK A C17 
2368 C  C21 . XEK B .   ? 0.3066 0.3007 0.2973 0.0095  0.0069  0.0061 401 XEK A C21 
2369 C  C22 . XEK B .   ? 0.2449 0.2402 0.2371 0.0087  0.0064  0.0066 401 XEK A C22 
2370 C  C24 . XEK B .   ? 0.1127 0.1104 0.1076 0.0053  0.0034  0.0080 401 XEK A C24 
2371 C  C25 . XEK B .   ? 0.1238 0.1216 0.1186 0.0054  0.0035  0.0081 401 XEK A C25 
2372 C  C27 . XEK B .   ? 0.1115 0.1104 0.1076 0.0042  0.0027  0.0085 401 XEK A C27 
2373 C  C16 . XEK B .   ? 0.1329 0.1287 0.1258 0.0068  0.0046  0.0071 401 XEK A C16 
2374 C  C18 . XEK B .   ? 0.1738 0.1697 0.1667 0.0075  0.0053  0.0070 401 XEK A C18 
2375 C  C19 . XEK B .   ? 0.1544 0.1508 0.1478 0.0074  0.0054  0.0071 401 XEK A C19 
2376 C  C20 . XEK B .   ? 0.1563 0.1515 0.1484 0.0082  0.0058  0.0067 401 XEK A C20 
2377 C  C23 . XEK B .   ? 0.1474 0.1442 0.1413 0.0063  0.0043  0.0075 401 XEK A C23 
2378 C  C26 . XEK B .   ? 0.1389 0.1374 0.1345 0.0048  0.0031  0.0083 401 XEK A C26 
2379 C  C28 . XEK B .   ? 0.1080 0.1061 0.1035 0.0046  0.0030  0.0081 401 XEK A C28 
2380 F  F1  . XEK B .   ? 0.1485 0.1427 0.1403 0.0058  0.0030  0.0074 401 XEK A F1  
2381 N  N1  . XEK B .   ? 0.1664 0.1624 0.1594 0.0080  0.0059  0.0069 401 XEK A N1  
2382 N  N2  . XEK B .   ? 0.2795 0.2744 0.2712 0.0088  0.0063  0.0065 401 XEK A N2  
2383 N  N3  . XEK B .   ? 0.0988 0.0958 0.0930 0.0058  0.0038  0.0077 401 XEK A N3  
2384 N  N4  . XEK B .   ? 0.1091 0.1079 0.1052 0.0042  0.0026  0.0084 401 XEK A N4  
2385 O  O1  . XEK B .   ? 0.0957 0.0924 0.0898 0.0053  0.0032  0.0078 401 XEK A O1  
2386 O  O2  . XEK B .   ? 0.2324 0.2268 0.2242 0.0058  0.0029  0.0075 401 XEK A O2  
2387 O  O3  . XEK B .   ? 0.1856 0.1825 0.1796 0.0068  0.0049  0.0074 401 XEK A O3  
2388 O  O4  . XEK B .   ? 0.2228 0.2179 0.2147 0.0092  0.0069  0.0064 401 XEK A O4  
2389 CL CL1 . XEK B .   ? 0.1732 0.1680 0.1656 0.0062  0.0038  0.0072 401 XEK A CL1 
2390 CL CL2 . XEK B .   ? 0.4413 0.4347 0.4322 0.0054  0.0019  0.0078 401 XEK A CL2 
2410 S  S   . DMS C .   ? 0.2272 0.2175 0.2167 0.0099  0.0090  0.0048 402 DMS A S   
2411 O  O   . DMS C .   ? 0.2205 0.2111 0.2101 0.0098  0.0089  0.0047 402 DMS A O   
2412 C  C1  . DMS C .   ? 0.2356 0.2261 0.2252 0.0099  0.0090  0.0050 402 DMS A C1  
2413 C  C2  . DMS C .   ? 0.2410 0.2311 0.2303 0.0100  0.0091  0.0047 402 DMS A C2  
# 
