data_9IT4
# 
_entry.id   9IT4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9IT4         pdb_00009it4 10.2210/pdb9it4/pdb 
WWPDB D_1300049521 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IT4 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              lliu@mail.tsinghua.edu.cn 
_pdbx_contact_author.name_first         Lei 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6290-8602 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Du, Y.X.' 1 0000-0003-3061-724X 
'Liu, L.'  2 0000-0001-6290-8602 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Mechanism of Histone H3K9 Methyltransferase Clr4 Regulation by Proximal H3K14 Ubiquitination in-cis' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Du, Y.X.' 1 0000-0003-3061-724X 
primary 'Liu, L.'  2 0000-0001-6290-8602 
# 
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 'Histone-lysine N-methyltransferase, H3 lysine-9 specific' 34078.062 1   2.1.1.355,2.1.1.366,2.1.1.367 ? ? ? 
2 polymer     syn 'Histone H3.1/H3.2'                                        1807.084  1   ?                             
'K9L, K14C' ? ? 
3 non-polymer syn S-ADENOSYLMETHIONINE                                       398.437   1   ?                             ? ? ? 
4 non-polymer syn 'ZINC ION'                                                 65.409    4   ?                             ? ? ? 
5 water       nat water                                                      18.015    142 ?                             ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Cryptic loci regulator 4,Histone H3-K9 methyltransferase,H3-K9-HMTase,HKMT,Lysine N-methyltransferase 1,Protein lysine methyltransferase clr4,PKMT
;
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GPSKLDSYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRLTQGVIPPDPNFQSGCNCSSLGGCD
LNNPSRCECLDDLDEPTHFAYDAQGRVRADTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFAP
AGTFITCYLGEVITSAEAAKRDKNYDDDGITYLFDLDMFDDASEYTVDAQNYGDVSRFFNHSCSPNIAIYSAVRNHGFRT
IYDLAFFAIKDIQPLEELTFDYAGAKDFSPVQSQKSQQNRISKLRRQCKCGSANCRGWLFG
;
;GPSKLDSYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRLTQGVIPPDPNFQSGCNCSSLGGCD
LNNPSRCECLDDLDEPTHFAYDAQGRVRADTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFAP
AGTFITCYLGEVITSAEAAKRDKNYDDDGITYLFDLDMFDDASEYTVDAQNYGDVSRFFNHSCSPNIAIYSAVRNHGFRT
IYDLAFFAIKDIQPLEELTFDYAGAKDFSPVQSQKSQQNRISKLRRQCKCGSANCRGWLFG
;
B ? 
2 'polypeptide(L)' no yes 'TKQTAR(NLE)STGGCAPRKQ' TKQTARLSTGGCAPRKQ F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 S-ADENOSYLMETHIONINE SAM 
4 'ZINC ION'           ZN  
5 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   SER n 
1 4   LYS n 
1 5   LEU n 
1 6   ASP n 
1 7   SER n 
1 8   TYR n 
1 9   THR n 
1 10  HIS n 
1 11  LEU n 
1 12  SER n 
1 13  PHE n 
1 14  TYR n 
1 15  GLU n 
1 16  LYS n 
1 17  ARG n 
1 18  GLU n 
1 19  LEU n 
1 20  PHE n 
1 21  ARG n 
1 22  LYS n 
1 23  LYS n 
1 24  LEU n 
1 25  ARG n 
1 26  GLU n 
1 27  ILE n 
1 28  GLU n 
1 29  GLY n 
1 30  PRO n 
1 31  GLU n 
1 32  VAL n 
1 33  THR n 
1 34  LEU n 
1 35  VAL n 
1 36  ASN n 
1 37  GLU n 
1 38  VAL n 
1 39  ASP n 
1 40  ASP n 
1 41  GLU n 
1 42  PRO n 
1 43  CYS n 
1 44  PRO n 
1 45  SER n 
1 46  LEU n 
1 47  ASP n 
1 48  PHE n 
1 49  GLN n 
1 50  PHE n 
1 51  ILE n 
1 52  SER n 
1 53  GLN n 
1 54  TYR n 
1 55  ARG n 
1 56  LEU n 
1 57  THR n 
1 58  GLN n 
1 59  GLY n 
1 60  VAL n 
1 61  ILE n 
1 62  PRO n 
1 63  PRO n 
1 64  ASP n 
1 65  PRO n 
1 66  ASN n 
1 67  PHE n 
1 68  GLN n 
1 69  SER n 
1 70  GLY n 
1 71  CYS n 
1 72  ASN n 
1 73  CYS n 
1 74  SER n 
1 75  SER n 
1 76  LEU n 
1 77  GLY n 
1 78  GLY n 
1 79  CYS n 
1 80  ASP n 
1 81  LEU n 
1 82  ASN n 
1 83  ASN n 
1 84  PRO n 
1 85  SER n 
1 86  ARG n 
1 87  CYS n 
1 88  GLU n 
1 89  CYS n 
1 90  LEU n 
1 91  ASP n 
1 92  ASP n 
1 93  LEU n 
1 94  ASP n 
1 95  GLU n 
1 96  PRO n 
1 97  THR n 
1 98  HIS n 
1 99  PHE n 
1 100 ALA n 
1 101 TYR n 
1 102 ASP n 
1 103 ALA n 
1 104 GLN n 
1 105 GLY n 
1 106 ARG n 
1 107 VAL n 
1 108 ARG n 
1 109 ALA n 
1 110 ASP n 
1 111 THR n 
1 112 GLY n 
1 113 ALA n 
1 114 VAL n 
1 115 ILE n 
1 116 TYR n 
1 117 GLU n 
1 118 CYS n 
1 119 ASN n 
1 120 SER n 
1 121 PHE n 
1 122 CYS n 
1 123 SER n 
1 124 CYS n 
1 125 SER n 
1 126 MET n 
1 127 GLU n 
1 128 CYS n 
1 129 PRO n 
1 130 ASN n 
1 131 ARG n 
1 132 VAL n 
1 133 VAL n 
1 134 GLN n 
1 135 ARG n 
1 136 GLY n 
1 137 ARG n 
1 138 THR n 
1 139 LEU n 
1 140 PRO n 
1 141 LEU n 
1 142 GLU n 
1 143 ILE n 
1 144 PHE n 
1 145 LYS n 
1 146 THR n 
1 147 LYS n 
1 148 GLU n 
1 149 LYS n 
1 150 GLY n 
1 151 TRP n 
1 152 GLY n 
1 153 VAL n 
1 154 ARG n 
1 155 SER n 
1 156 LEU n 
1 157 ARG n 
1 158 PHE n 
1 159 ALA n 
1 160 PRO n 
1 161 ALA n 
1 162 GLY n 
1 163 THR n 
1 164 PHE n 
1 165 ILE n 
1 166 THR n 
1 167 CYS n 
1 168 TYR n 
1 169 LEU n 
1 170 GLY n 
1 171 GLU n 
1 172 VAL n 
1 173 ILE n 
1 174 THR n 
1 175 SER n 
1 176 ALA n 
1 177 GLU n 
1 178 ALA n 
1 179 ALA n 
1 180 LYS n 
1 181 ARG n 
1 182 ASP n 
1 183 LYS n 
1 184 ASN n 
1 185 TYR n 
1 186 ASP n 
1 187 ASP n 
1 188 ASP n 
1 189 GLY n 
1 190 ILE n 
1 191 THR n 
1 192 TYR n 
1 193 LEU n 
1 194 PHE n 
1 195 ASP n 
1 196 LEU n 
1 197 ASP n 
1 198 MET n 
1 199 PHE n 
1 200 ASP n 
1 201 ASP n 
1 202 ALA n 
1 203 SER n 
1 204 GLU n 
1 205 TYR n 
1 206 THR n 
1 207 VAL n 
1 208 ASP n 
1 209 ALA n 
1 210 GLN n 
1 211 ASN n 
1 212 TYR n 
1 213 GLY n 
1 214 ASP n 
1 215 VAL n 
1 216 SER n 
1 217 ARG n 
1 218 PHE n 
1 219 PHE n 
1 220 ASN n 
1 221 HIS n 
1 222 SER n 
1 223 CYS n 
1 224 SER n 
1 225 PRO n 
1 226 ASN n 
1 227 ILE n 
1 228 ALA n 
1 229 ILE n 
1 230 TYR n 
1 231 SER n 
1 232 ALA n 
1 233 VAL n 
1 234 ARG n 
1 235 ASN n 
1 236 HIS n 
1 237 GLY n 
1 238 PHE n 
1 239 ARG n 
1 240 THR n 
1 241 ILE n 
1 242 TYR n 
1 243 ASP n 
1 244 LEU n 
1 245 ALA n 
1 246 PHE n 
1 247 PHE n 
1 248 ALA n 
1 249 ILE n 
1 250 LYS n 
1 251 ASP n 
1 252 ILE n 
1 253 GLN n 
1 254 PRO n 
1 255 LEU n 
1 256 GLU n 
1 257 GLU n 
1 258 LEU n 
1 259 THR n 
1 260 PHE n 
1 261 ASP n 
1 262 TYR n 
1 263 ALA n 
1 264 GLY n 
1 265 ALA n 
1 266 LYS n 
1 267 ASP n 
1 268 PHE n 
1 269 SER n 
1 270 PRO n 
1 271 VAL n 
1 272 GLN n 
1 273 SER n 
1 274 GLN n 
1 275 LYS n 
1 276 SER n 
1 277 GLN n 
1 278 GLN n 
1 279 ASN n 
1 280 ARG n 
1 281 ILE n 
1 282 SER n 
1 283 LYS n 
1 284 LEU n 
1 285 ARG n 
1 286 ARG n 
1 287 GLN n 
1 288 CYS n 
1 289 LYS n 
1 290 CYS n 
1 291 GLY n 
1 292 SER n 
1 293 ALA n 
1 294 ASN n 
1 295 CYS n 
1 296 ARG n 
1 297 GLY n 
1 298 TRP n 
1 299 LEU n 
1 300 PHE n 
1 301 GLY n 
2 1   THR n 
2 2   LYS n 
2 3   GLN n 
2 4   THR n 
2 5   ALA n 
2 6   ARG n 
2 7   NLE n 
2 8   SER n 
2 9   THR n 
2 10  GLY n 
2 11  GLY n 
2 12  CYS n 
2 13  ALA n 
2 14  PRO n 
2 15  ARG n 
2 16  LYS n 
2 17  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                   301 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'clr4, kmt1, SPBC428.08c' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    972 
_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      'Schizosaccharomyces pombe 972h-' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     284812 
_entity_src_gen.pdbx_gene_src_variant              '972 / ATCC 24843' 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 24843 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pGEX-6p-1 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       17 
_pdbx_entity_src_syn.organism_scientific    'Schizosaccharomyces pombe 972h-' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       284812 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE              ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE             ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE           ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'      ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE             ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'   149.211 
NLE 'L-peptide linking' n NORLEUCINE           ? 'C6 H13 N O2'     131.173 
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'      115.130 
SAM non-polymer         . S-ADENOSYLMETHIONINE ? 'C15 H22 N6 O5 S' 398.437 
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 
ZN  non-polymer         . 'ZINC ION'           ? 'Zn 2'            65.409  
# 
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   GLY 1   190 ?   ?   ?   B . n 
A 1 2   PRO 2   191 ?   ?   ?   B . n 
A 1 3   SER 3   192 ?   ?   ?   B . n 
A 1 4   LYS 4   193 ?   ?   ?   B . n 
A 1 5   LEU 5   194 ?   ?   ?   B . n 
A 1 6   ASP 6   195 195 ASP ASP B . n 
A 1 7   SER 7   196 196 SER SER B . n 
A 1 8   TYR 8   197 197 TYR TYR B . n 
A 1 9   THR 9   198 198 THR THR B . n 
A 1 10  HIS 10  199 199 HIS HIS B . n 
A 1 11  LEU 11  200 200 LEU LEU B . n 
A 1 12  SER 12  201 201 SER SER B . n 
A 1 13  PHE 13  202 202 PHE PHE B . n 
A 1 14  TYR 14  203 203 TYR TYR B . n 
A 1 15  GLU 15  204 204 GLU GLU B . n 
A 1 16  LYS 16  205 205 LYS LYS B . n 
A 1 17  ARG 17  206 206 ARG ARG B . n 
A 1 18  GLU 18  207 207 GLU GLU B . n 
A 1 19  LEU 19  208 208 LEU LEU B . n 
A 1 20  PHE 20  209 209 PHE PHE B . n 
A 1 21  ARG 21  210 210 ARG ARG B . n 
A 1 22  LYS 22  211 211 LYS LYS B . n 
A 1 23  LYS 23  212 212 LYS LYS B . n 
A 1 24  LEU 24  213 213 LEU LEU B . n 
A 1 25  ARG 25  214 214 ARG ARG B . n 
A 1 26  GLU 26  215 215 GLU GLU B . n 
A 1 27  ILE 27  216 216 ILE ILE B . n 
A 1 28  GLU 28  217 217 GLU GLU B . n 
A 1 29  GLY 29  218 218 GLY GLY B . n 
A 1 30  PRO 30  219 219 PRO PRO B . n 
A 1 31  GLU 31  220 220 GLU GLU B . n 
A 1 32  VAL 32  221 221 VAL VAL B . n 
A 1 33  THR 33  222 222 THR THR B . n 
A 1 34  LEU 34  223 223 LEU LEU B . n 
A 1 35  VAL 35  224 224 VAL VAL B . n 
A 1 36  ASN 36  225 225 ASN ASN B . n 
A 1 37  GLU 37  226 226 GLU GLU B . n 
A 1 38  VAL 38  227 227 VAL VAL B . n 
A 1 39  ASP 39  228 228 ASP ASP B . n 
A 1 40  ASP 40  229 229 ASP ASP B . n 
A 1 41  GLU 41  230 230 GLU GLU B . n 
A 1 42  PRO 42  231 231 PRO PRO B . n 
A 1 43  CYS 43  232 232 CYS CYS B . n 
A 1 44  PRO 44  233 233 PRO PRO B . n 
A 1 45  SER 45  234 234 SER SER B . n 
A 1 46  LEU 46  235 235 LEU LEU B . n 
A 1 47  ASP 47  236 236 ASP ASP B . n 
A 1 48  PHE 48  237 237 PHE PHE B . n 
A 1 49  GLN 49  238 238 GLN GLN B . n 
A 1 50  PHE 50  239 239 PHE PHE B . n 
A 1 51  ILE 51  240 240 ILE ILE B . n 
A 1 52  SER 52  241 241 SER SER B . n 
A 1 53  GLN 53  242 242 GLN GLN B . n 
A 1 54  TYR 54  243 243 TYR TYR B . n 
A 1 55  ARG 55  244 244 ARG ARG B . n 
A 1 56  LEU 56  245 245 LEU LEU B . n 
A 1 57  THR 57  246 246 THR THR B . n 
A 1 58  GLN 58  247 247 GLN GLN B . n 
A 1 59  GLY 59  248 248 GLY GLY B . n 
A 1 60  VAL 60  249 249 VAL VAL B . n 
A 1 61  ILE 61  250 250 ILE ILE B . n 
A 1 62  PRO 62  251 251 PRO PRO B . n 
A 1 63  PRO 63  252 252 PRO PRO B . n 
A 1 64  ASP 64  253 253 ASP ASP B . n 
A 1 65  PRO 65  254 254 PRO PRO B . n 
A 1 66  ASN 66  255 255 ASN ASN B . n 
A 1 67  PHE 67  256 256 PHE PHE B . n 
A 1 68  GLN 68  257 257 GLN GLN B . n 
A 1 69  SER 69  258 258 SER SER B . n 
A 1 70  GLY 70  259 259 GLY GLY B . n 
A 1 71  CYS 71  260 260 CYS CYS B . n 
A 1 72  ASN 72  261 261 ASN ASN B . n 
A 1 73  CYS 73  262 262 CYS CYS B . n 
A 1 74  SER 74  263 263 SER SER B . n 
A 1 75  SER 75  264 ?   ?   ?   B . n 
A 1 76  LEU 76  265 ?   ?   ?   B . n 
A 1 77  GLY 77  266 ?   ?   ?   B . n 
A 1 78  GLY 78  267 267 GLY GLY B . n 
A 1 79  CYS 79  268 268 CYS CYS B . n 
A 1 80  ASP 80  269 269 ASP ASP B . n 
A 1 81  LEU 81  270 270 LEU LEU B . n 
A 1 82  ASN 82  271 271 ASN ASN B . n 
A 1 83  ASN 83  272 272 ASN ASN B . n 
A 1 84  PRO 84  273 273 PRO PRO B . n 
A 1 85  SER 85  274 274 SER SER B . n 
A 1 86  ARG 86  275 275 ARG ARG B . n 
A 1 87  CYS 87  276 276 CYS CYS B . n 
A 1 88  GLU 88  277 277 GLU GLU B . n 
A 1 89  CYS 89  278 278 CYS CYS B . n 
A 1 90  LEU 90  279 279 LEU LEU B . n 
A 1 91  ASP 91  280 280 ASP ASP B . n 
A 1 92  ASP 92  281 281 ASP ASP B . n 
A 1 93  LEU 93  282 282 LEU LEU B . n 
A 1 94  ASP 94  283 283 ASP ASP B . n 
A 1 95  GLU 95  284 284 GLU GLU B . n 
A 1 96  PRO 96  285 285 PRO PRO B . n 
A 1 97  THR 97  286 286 THR THR B . n 
A 1 98  HIS 98  287 287 HIS HIS B . n 
A 1 99  PHE 99  288 288 PHE PHE B . n 
A 1 100 ALA 100 289 289 ALA ALA B . n 
A 1 101 TYR 101 290 290 TYR TYR B . n 
A 1 102 ASP 102 291 291 ASP ASP B . n 
A 1 103 ALA 103 292 292 ALA ALA B . n 
A 1 104 GLN 104 293 293 GLN GLN B . n 
A 1 105 GLY 105 294 294 GLY GLY B . n 
A 1 106 ARG 106 295 295 ARG ARG B . n 
A 1 107 VAL 107 296 296 VAL VAL B . n 
A 1 108 ARG 108 297 297 ARG ARG B . n 
A 1 109 ALA 109 298 298 ALA ALA B . n 
A 1 110 ASP 110 299 299 ASP ASP B . n 
A 1 111 THR 111 300 300 THR THR B . n 
A 1 112 GLY 112 301 301 GLY GLY B . n 
A 1 113 ALA 113 302 302 ALA ALA B . n 
A 1 114 VAL 114 303 303 VAL VAL B . n 
A 1 115 ILE 115 304 304 ILE ILE B . n 
A 1 116 TYR 116 305 305 TYR TYR B . n 
A 1 117 GLU 117 306 306 GLU GLU B . n 
A 1 118 CYS 118 307 307 CYS CYS B . n 
A 1 119 ASN 119 308 308 ASN ASN B . n 
A 1 120 SER 120 309 309 SER SER B . n 
A 1 121 PHE 121 310 310 PHE PHE B . n 
A 1 122 CYS 122 311 311 CYS CYS B . n 
A 1 123 SER 123 312 312 SER SER B . n 
A 1 124 CYS 124 313 313 CYS CYS B . n 
A 1 125 SER 125 314 314 SER SER B . n 
A 1 126 MET 126 315 315 MET MET B . n 
A 1 127 GLU 127 316 316 GLU GLU B . n 
A 1 128 CYS 128 317 317 CYS CYS B . n 
A 1 129 PRO 129 318 318 PRO PRO B . n 
A 1 130 ASN 130 319 319 ASN ASN B . n 
A 1 131 ARG 131 320 320 ARG ARG B . n 
A 1 132 VAL 132 321 321 VAL VAL B . n 
A 1 133 VAL 133 322 322 VAL VAL B . n 
A 1 134 GLN 134 323 323 GLN GLN B . n 
A 1 135 ARG 135 324 324 ARG ARG B . n 
A 1 136 GLY 136 325 325 GLY GLY B . n 
A 1 137 ARG 137 326 326 ARG ARG B . n 
A 1 138 THR 138 327 327 THR THR B . n 
A 1 139 LEU 139 328 328 LEU LEU B . n 
A 1 140 PRO 140 329 329 PRO PRO B . n 
A 1 141 LEU 141 330 330 LEU LEU B . n 
A 1 142 GLU 142 331 331 GLU GLU B . n 
A 1 143 ILE 143 332 332 ILE ILE B . n 
A 1 144 PHE 144 333 333 PHE PHE B . n 
A 1 145 LYS 145 334 334 LYS LYS B . n 
A 1 146 THR 146 335 335 THR THR B . n 
A 1 147 LYS 147 336 336 LYS LYS B . n 
A 1 148 GLU 148 337 337 GLU GLU B . n 
A 1 149 LYS 149 338 338 LYS LYS B . n 
A 1 150 GLY 150 339 339 GLY GLY B . n 
A 1 151 TRP 151 340 340 TRP TRP B . n 
A 1 152 GLY 152 341 341 GLY GLY B . n 
A 1 153 VAL 153 342 342 VAL VAL B . n 
A 1 154 ARG 154 343 343 ARG ARG B . n 
A 1 155 SER 155 344 344 SER SER B . n 
A 1 156 LEU 156 345 345 LEU LEU B . n 
A 1 157 ARG 157 346 346 ARG ARG B . n 
A 1 158 PHE 158 347 347 PHE PHE B . n 
A 1 159 ALA 159 348 348 ALA ALA B . n 
A 1 160 PRO 160 349 349 PRO PRO B . n 
A 1 161 ALA 161 350 350 ALA ALA B . n 
A 1 162 GLY 162 351 351 GLY GLY B . n 
A 1 163 THR 163 352 352 THR THR B . n 
A 1 164 PHE 164 353 353 PHE PHE B . n 
A 1 165 ILE 165 354 354 ILE ILE B . n 
A 1 166 THR 166 355 355 THR THR B . n 
A 1 167 CYS 167 356 356 CYS CYS B . n 
A 1 168 TYR 168 357 357 TYR TYR B . n 
A 1 169 LEU 169 358 358 LEU LEU B . n 
A 1 170 GLY 170 359 359 GLY GLY B . n 
A 1 171 GLU 171 360 360 GLU GLU B . n 
A 1 172 VAL 172 361 361 VAL VAL B . n 
A 1 173 ILE 173 362 362 ILE ILE B . n 
A 1 174 THR 174 363 363 THR THR B . n 
A 1 175 SER 175 364 364 SER SER B . n 
A 1 176 ALA 176 365 365 ALA ALA B . n 
A 1 177 GLU 177 366 366 GLU GLU B . n 
A 1 178 ALA 178 367 367 ALA ALA B . n 
A 1 179 ALA 179 368 368 ALA ALA B . n 
A 1 180 LYS 180 369 369 LYS LYS B . n 
A 1 181 ARG 181 370 370 ARG ARG B . n 
A 1 182 ASP 182 371 371 ASP ASP B . n 
A 1 183 LYS 183 372 372 LYS LYS B . n 
A 1 184 ASN 184 373 ?   ?   ?   B . n 
A 1 185 TYR 185 374 ?   ?   ?   B . n 
A 1 186 ASP 186 375 375 ASP ASP B . n 
A 1 187 ASP 187 376 376 ASP ASP B . n 
A 1 188 ASP 188 377 377 ASP ASP B . n 
A 1 189 GLY 189 378 378 GLY GLY B . n 
A 1 190 ILE 190 379 379 ILE ILE B . n 
A 1 191 THR 191 380 380 THR THR B . n 
A 1 192 TYR 192 381 381 TYR TYR B . n 
A 1 193 LEU 193 382 382 LEU LEU B . n 
A 1 194 PHE 194 383 383 PHE PHE B . n 
A 1 195 ASP 195 384 384 ASP ASP B . n 
A 1 196 LEU 196 385 385 LEU LEU B . n 
A 1 197 ASP 197 386 386 ASP ASP B . n 
A 1 198 MET 198 387 387 MET MET B . n 
A 1 199 PHE 199 388 388 PHE PHE B . n 
A 1 200 ASP 200 389 389 ASP ASP B . n 
A 1 201 ASP 201 390 390 ASP ASP B . n 
A 1 202 ALA 202 391 391 ALA ALA B . n 
A 1 203 SER 203 392 392 SER SER B . n 
A 1 204 GLU 204 393 393 GLU GLU B . n 
A 1 205 TYR 205 394 394 TYR TYR B . n 
A 1 206 THR 206 395 395 THR THR B . n 
A 1 207 VAL 207 396 396 VAL VAL B . n 
A 1 208 ASP 208 397 397 ASP ASP B . n 
A 1 209 ALA 209 398 398 ALA ALA B . n 
A 1 210 GLN 210 399 399 GLN GLN B . n 
A 1 211 ASN 211 400 400 ASN ASN B . n 
A 1 212 TYR 212 401 401 TYR TYR B . n 
A 1 213 GLY 213 402 402 GLY GLY B . n 
A 1 214 ASP 214 403 403 ASP ASP B . n 
A 1 215 VAL 215 404 404 VAL VAL B . n 
A 1 216 SER 216 405 405 SER SER B . n 
A 1 217 ARG 217 406 406 ARG ARG B . n 
A 1 218 PHE 218 407 407 PHE PHE B . n 
A 1 219 PHE 219 408 408 PHE PHE B . n 
A 1 220 ASN 220 409 409 ASN ASN B . n 
A 1 221 HIS 221 410 410 HIS HIS B . n 
A 1 222 SER 222 411 411 SER SER B . n 
A 1 223 CYS 223 412 412 CYS CYS B . n 
A 1 224 SER 224 413 413 SER SER B . n 
A 1 225 PRO 225 414 414 PRO PRO B . n 
A 1 226 ASN 226 415 415 ASN ASN B . n 
A 1 227 ILE 227 416 416 ILE ILE B . n 
A 1 228 ALA 228 417 417 ALA ALA B . n 
A 1 229 ILE 229 418 418 ILE ILE B . n 
A 1 230 TYR 230 419 419 TYR TYR B . n 
A 1 231 SER 231 420 420 SER SER B . n 
A 1 232 ALA 232 421 421 ALA ALA B . n 
A 1 233 VAL 233 422 422 VAL VAL B . n 
A 1 234 ARG 234 423 423 ARG ARG B . n 
A 1 235 ASN 235 424 424 ASN ASN B . n 
A 1 236 HIS 236 425 425 HIS HIS B . n 
A 1 237 GLY 237 426 426 GLY GLY B . n 
A 1 238 PHE 238 427 427 PHE PHE B . n 
A 1 239 ARG 239 428 428 ARG ARG B . n 
A 1 240 THR 240 429 429 THR THR B . n 
A 1 241 ILE 241 430 430 ILE ILE B . n 
A 1 242 TYR 242 431 431 TYR TYR B . n 
A 1 243 ASP 243 432 432 ASP ASP B . n 
A 1 244 LEU 244 433 433 LEU LEU B . n 
A 1 245 ALA 245 434 434 ALA ALA B . n 
A 1 246 PHE 246 435 435 PHE PHE B . n 
A 1 247 PHE 247 436 436 PHE PHE B . n 
A 1 248 ALA 248 437 437 ALA ALA B . n 
A 1 249 ILE 249 438 438 ILE ILE B . n 
A 1 250 LYS 250 439 439 LYS LYS B . n 
A 1 251 ASP 251 440 440 ASP ASP B . n 
A 1 252 ILE 252 441 441 ILE ILE B . n 
A 1 253 GLN 253 442 442 GLN GLN B . n 
A 1 254 PRO 254 443 443 PRO PRO B . n 
A 1 255 LEU 255 444 444 LEU LEU B . n 
A 1 256 GLU 256 445 445 GLU GLU B . n 
A 1 257 GLU 257 446 446 GLU GLU B . n 
A 1 258 LEU 258 447 447 LEU LEU B . n 
A 1 259 THR 259 448 448 THR THR B . n 
A 1 260 PHE 260 449 449 PHE PHE B . n 
A 1 261 ASP 261 450 450 ASP ASP B . n 
A 1 262 TYR 262 451 451 TYR TYR B . n 
A 1 263 ALA 263 452 452 ALA ALA B . n 
A 1 264 GLY 264 453 453 GLY GLY B . n 
A 1 265 ALA 265 454 454 ALA ALA B . n 
A 1 266 LYS 266 455 ?   ?   ?   B . n 
A 1 267 ASP 267 456 ?   ?   ?   B . n 
A 1 268 PHE 268 457 ?   ?   ?   B . n 
A 1 269 SER 269 458 ?   ?   ?   B . n 
A 1 270 PRO 270 459 ?   ?   ?   B . n 
A 1 271 VAL 271 460 ?   ?   ?   B . n 
A 1 272 GLN 272 461 ?   ?   ?   B . n 
A 1 273 SER 273 462 ?   ?   ?   B . n 
A 1 274 GLN 274 463 ?   ?   ?   B . n 
A 1 275 LYS 275 464 ?   ?   ?   B . n 
A 1 276 SER 276 465 ?   ?   ?   B . n 
A 1 277 GLN 277 466 ?   ?   ?   B . n 
A 1 278 GLN 278 467 ?   ?   ?   B . n 
A 1 279 ASN 279 468 ?   ?   ?   B . n 
A 1 280 ARG 280 469 ?   ?   ?   B . n 
A 1 281 ILE 281 470 ?   ?   ?   B . n 
A 1 282 SER 282 471 ?   ?   ?   B . n 
A 1 283 LYS 283 472 ?   ?   ?   B . n 
A 1 284 LEU 284 473 ?   ?   ?   B . n 
A 1 285 ARG 285 474 474 ARG ARG B . n 
A 1 286 ARG 286 475 475 ARG ARG B . n 
A 1 287 GLN 287 476 476 GLN GLN B . n 
A 1 288 CYS 288 477 477 CYS CYS B . n 
A 1 289 LYS 289 478 478 LYS LYS B . n 
A 1 290 CYS 290 479 479 CYS CYS B . n 
A 1 291 GLY 291 480 480 GLY GLY B . n 
A 1 292 SER 292 481 481 SER SER B . n 
A 1 293 ALA 293 482 482 ALA ALA B . n 
A 1 294 ASN 294 483 483 ASN ASN B . n 
A 1 295 CYS 295 484 484 CYS CYS B . n 
A 1 296 ARG 296 485 485 ARG ARG B . n 
A 1 297 GLY 297 486 486 GLY GLY B . n 
A 1 298 TRP 298 487 487 TRP TRP B . n 
A 1 299 LEU 299 488 488 LEU LEU B . n 
A 1 300 PHE 300 489 489 PHE PHE B . n 
A 1 301 GLY 301 490 490 GLY GLY B . n 
B 2 1   THR 1   3   ?   ?   ?   F . n 
B 2 2   LYS 2   4   ?   ?   ?   F . n 
B 2 3   GLN 3   5   5   GLN GLN F . n 
B 2 4   THR 4   6   6   THR THR F . n 
B 2 5   ALA 5   7   7   ALA ALA F . n 
B 2 6   ARG 6   8   8   ARG ARG F . n 
B 2 7   NLE 7   9   9   NLE NLE F . n 
B 2 8   SER 8   10  10  SER SER F . n 
B 2 9   THR 9   11  11  THR THR F . n 
B 2 10  GLY 10  12  12  GLY GLY F . n 
B 2 11  GLY 11  13  13  GLY GLY F . n 
B 2 12  CYS 12  14  14  CYS CYS F . n 
B 2 13  ALA 13  15  15  ALA ALA F . n 
B 2 14  PRO 14  16  16  PRO PRO F . n 
B 2 15  ARG 15  17  17  ARG ARG F . n 
B 2 16  LYS 16  18  18  LYS LYS F . n 
B 2 17  GLN 17  19  19  GLN GLN F . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 NLE ? ? NLE ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SAM ? ? SAM ? ? 'SUBJECT OF INVESTIGATION' ? 
3 ZN  ? ? ZN  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
C 3 SAM 1   501 501 SAM SAM B . 
D 4 ZN  1   502 502 ZN  ZN  B . 
E 4 ZN  1   503 503 ZN  ZN  B . 
F 4 ZN  1   504 504 ZN  ZN  B . 
G 4 ZN  1   505 505 ZN  ZN  B . 
H 5 HOH 1   601 601 HOH HOH B . 
H 5 HOH 2   602 602 HOH HOH B . 
H 5 HOH 3   603 603 HOH HOH B . 
H 5 HOH 4   604 604 HOH HOH B . 
H 5 HOH 5   605 605 HOH HOH B . 
H 5 HOH 6   606 606 HOH HOH B . 
H 5 HOH 7   607 607 HOH HOH B . 
H 5 HOH 8   608 608 HOH HOH B . 
H 5 HOH 9   609 609 HOH HOH B . 
H 5 HOH 10  610 610 HOH HOH B . 
H 5 HOH 11  611 611 HOH HOH B . 
H 5 HOH 12  612 612 HOH HOH B . 
H 5 HOH 13  613 613 HOH HOH B . 
H 5 HOH 14  614 614 HOH HOH B . 
H 5 HOH 15  615 615 HOH HOH B . 
H 5 HOH 16  616 616 HOH HOH B . 
H 5 HOH 17  617 1   HOH HOH B . 
H 5 HOH 18  618 617 HOH HOH B . 
H 5 HOH 19  619 618 HOH HOH B . 
H 5 HOH 20  620 619 HOH HOH B . 
H 5 HOH 21  621 620 HOH HOH B . 
H 5 HOH 22  622 621 HOH HOH B . 
H 5 HOH 23  623 622 HOH HOH B . 
H 5 HOH 24  624 623 HOH HOH B . 
H 5 HOH 25  625 624 HOH HOH B . 
H 5 HOH 26  626 713 HOH HOH B . 
H 5 HOH 27  627 625 HOH HOH B . 
H 5 HOH 28  628 626 HOH HOH B . 
H 5 HOH 29  629 627 HOH HOH B . 
H 5 HOH 30  630 628 HOH HOH B . 
H 5 HOH 31  631 629 HOH HOH B . 
H 5 HOH 32  632 630 HOH HOH B . 
H 5 HOH 33  633 631 HOH HOH B . 
H 5 HOH 34  634 632 HOH HOH B . 
H 5 HOH 35  635 633 HOH HOH B . 
H 5 HOH 36  636 635 HOH HOH B . 
H 5 HOH 37  637 636 HOH HOH B . 
H 5 HOH 38  638 637 HOH HOH B . 
H 5 HOH 39  639 638 HOH HOH B . 
H 5 HOH 40  640 639 HOH HOH B . 
H 5 HOH 41  641 640 HOH HOH B . 
H 5 HOH 42  642 641 HOH HOH B . 
H 5 HOH 43  643 642 HOH HOH B . 
H 5 HOH 44  644 643 HOH HOH B . 
H 5 HOH 45  645 644 HOH HOH B . 
H 5 HOH 46  646 645 HOH HOH B . 
H 5 HOH 47  647 646 HOH HOH B . 
H 5 HOH 48  648 647 HOH HOH B . 
H 5 HOH 49  649 648 HOH HOH B . 
H 5 HOH 50  650 649 HOH HOH B . 
H 5 HOH 51  651 650 HOH HOH B . 
H 5 HOH 52  652 651 HOH HOH B . 
H 5 HOH 53  653 652 HOH HOH B . 
H 5 HOH 54  654 653 HOH HOH B . 
H 5 HOH 55  655 654 HOH HOH B . 
H 5 HOH 56  656 655 HOH HOH B . 
H 5 HOH 57  657 656 HOH HOH B . 
H 5 HOH 58  658 657 HOH HOH B . 
H 5 HOH 59  659 658 HOH HOH B . 
H 5 HOH 60  660 659 HOH HOH B . 
H 5 HOH 61  661 660 HOH HOH B . 
H 5 HOH 62  662 661 HOH HOH B . 
H 5 HOH 63  663 662 HOH HOH B . 
H 5 HOH 64  664 663 HOH HOH B . 
H 5 HOH 65  665 664 HOH HOH B . 
H 5 HOH 66  666 665 HOH HOH B . 
H 5 HOH 67  667 666 HOH HOH B . 
H 5 HOH 68  668 667 HOH HOH B . 
H 5 HOH 69  669 668 HOH HOH B . 
H 5 HOH 70  670 669 HOH HOH B . 
H 5 HOH 71  671 670 HOH HOH B . 
H 5 HOH 72  672 671 HOH HOH B . 
H 5 HOH 73  673 672 HOH HOH B . 
H 5 HOH 74  674 673 HOH HOH B . 
H 5 HOH 75  675 674 HOH HOH B . 
H 5 HOH 76  676 675 HOH HOH B . 
H 5 HOH 77  677 676 HOH HOH B . 
H 5 HOH 78  678 677 HOH HOH B . 
H 5 HOH 79  679 678 HOH HOH B . 
H 5 HOH 80  680 679 HOH HOH B . 
H 5 HOH 81  681 680 HOH HOH B . 
H 5 HOH 82  682 681 HOH HOH B . 
H 5 HOH 83  683 682 HOH HOH B . 
H 5 HOH 84  684 683 HOH HOH B . 
H 5 HOH 85  685 684 HOH HOH B . 
H 5 HOH 86  686 685 HOH HOH B . 
H 5 HOH 87  687 686 HOH HOH B . 
H 5 HOH 88  688 687 HOH HOH B . 
H 5 HOH 89  689 688 HOH HOH B . 
H 5 HOH 90  690 689 HOH HOH B . 
H 5 HOH 91  691 690 HOH HOH B . 
H 5 HOH 92  692 691 HOH HOH B . 
H 5 HOH 93  693 692 HOH HOH B . 
H 5 HOH 94  694 693 HOH HOH B . 
H 5 HOH 95  695 694 HOH HOH B . 
H 5 HOH 96  696 695 HOH HOH B . 
H 5 HOH 97  697 696 HOH HOH B . 
H 5 HOH 98  698 697 HOH HOH B . 
H 5 HOH 99  699 698 HOH HOH B . 
H 5 HOH 100 700 699 HOH HOH B . 
H 5 HOH 101 701 700 HOH HOH B . 
H 5 HOH 102 702 701 HOH HOH B . 
H 5 HOH 103 703 702 HOH HOH B . 
H 5 HOH 104 704 703 HOH HOH B . 
H 5 HOH 105 705 704 HOH HOH B . 
H 5 HOH 106 706 705 HOH HOH B . 
H 5 HOH 107 707 706 HOH HOH B . 
H 5 HOH 108 708 707 HOH HOH B . 
H 5 HOH 109 709 708 HOH HOH B . 
H 5 HOH 110 710 709 HOH HOH B . 
H 5 HOH 111 711 710 HOH HOH B . 
H 5 HOH 112 712 711 HOH HOH B . 
H 5 HOH 113 713 712 HOH HOH B . 
H 5 HOH 114 714 715 HOH HOH B . 
H 5 HOH 115 715 716 HOH HOH B . 
H 5 HOH 116 716 717 HOH HOH B . 
H 5 HOH 117 717 718 HOH HOH B . 
H 5 HOH 118 718 719 HOH HOH B . 
H 5 HOH 119 719 720 HOH HOH B . 
H 5 HOH 120 720 732 HOH HOH B . 
H 5 HOH 121 721 721 HOH HOH B . 
H 5 HOH 122 722 722 HOH HOH B . 
H 5 HOH 123 723 723 HOH HOH B . 
H 5 HOH 124 724 724 HOH HOH B . 
H 5 HOH 125 725 714 HOH HOH B . 
H 5 HOH 126 726 725 HOH HOH B . 
H 5 HOH 127 727 726 HOH HOH B . 
H 5 HOH 128 728 727 HOH HOH B . 
H 5 HOH 129 729 728 HOH HOH B . 
H 5 HOH 130 730 729 HOH HOH B . 
H 5 HOH 131 731 730 HOH HOH B . 
H 5 HOH 132 732 731 HOH HOH B . 
H 5 HOH 133 733 733 HOH HOH B . 
H 5 HOH 134 734 735 HOH HOH B . 
H 5 HOH 135 735 736 HOH HOH B . 
H 5 HOH 136 736 737 HOH HOH B . 
H 5 HOH 137 737 738 HOH HOH B . 
H 5 HOH 138 738 739 HOH HOH B . 
H 5 HOH 139 739 740 HOH HOH B . 
H 5 HOH 140 740 734 HOH HOH B . 
I 5 HOH 1   101 741 HOH HOH F . 
I 5 HOH 2   102 742 HOH HOH F . 
# 
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 B ASN 272 ? CG  ? A ASN 83  CG  
2 1 Y 1 B ASN 272 ? OD1 ? A ASN 83  OD1 
3 1 Y 1 B ASN 272 ? ND2 ? A ASN 83  ND2 
4 1 Y 1 B ARG 475 ? CG  ? A ARG 286 CG  
5 1 Y 1 B ARG 475 ? CD  ? A ARG 286 CD  
6 1 Y 1 B ARG 475 ? NE  ? A ARG 286 NE  
7 1 Y 1 B ARG 475 ? CZ  ? A ARG 286 CZ  
8 1 Y 1 B ARG 475 ? NH1 ? A ARG 286 NH1 
9 1 Y 1 B ARG 475 ? NH2 ? A ARG 286 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   ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? 0.7.4       3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.19.2_4158 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IT4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.130 
_cell.length_a_esd                 ? 
_cell.length_b                     70.384 
_cell.length_b_esd                 ? 
_cell.length_c                     110.466 
_cell.length_c_esd                 ? 
_cell.volume                       304237.274 
_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                         9IT4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (z,x,y)' 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_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                   9IT4 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.43 
_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              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Magnesium chloride hexahydrate, 0.1 M MES, pH 6.0, 8 % w/v PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979176 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979176 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          30.07 
_reflns.entry_id                                       9IT4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.29 
_reflns.d_resolution_low                               36.88 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     14058 
_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                           97.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.56 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.922 
_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                                0.169 
_reflns.pdbx_Rpim_I_all                                0.053 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.925 
_reflns.pdbx_CC_star                                   0.980 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.29 2.34  ? ? ? ? ? ? 565 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1  1 0.955 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.34 2.38  ? ? ? ? ? ? 617 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2  1 0.954 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.38 2.43  ? ? ? ? ? ? 644 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 3  1 0.965 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.43 2.48  ? ? ? ? ? ? 682 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 4  1 0.979 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.48 2.53  ? ? ? ? ? ? 697 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 5  1 0.974 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.53 2.59  ? ? ? ? ? ? 704 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 6  1 0.976 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.59 2.66  ? ? ? ? ? ? 695 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 7  1 0.980 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.66 2.73  ? ? ? ? ? ? 704 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 8  1 0.985 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.73 2.81  ? ? ? ? ? ? 719 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 9  1 0.990 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.81 2.90  ? ? ? ? ? ? 695 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 10 1 0.991 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2.90 3.00  ? ? ? ? ? ? 720 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 11 1 0.991 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3.00 3.12  ? ? ? ? ? ? 707 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 12 1 0.992 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3.12 3.26  ? ? ? ? ? ? 731 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 13 1 0.995 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3.26 3.44  ? ? ? ? ? ? 690 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 14 1 0.995 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3.44 3.65  ? ? ? ? ? ? 732 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 15 1 0.993 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3.65 3.93  ? ? ? ? ? ? 732 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 16 1 0.991 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3.93 4.33  ? ? ? ? ? ? 712 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 17 1 0.996 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4.33 4.95  ? ? ? ? ? ? 742 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 18 1 0.994 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4.95 6.24  ? ? ? ? ? ? 756 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 19 1 0.994 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
6.24 36.88 ? ? ? ? ? ? 814 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 20 1 0.994 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_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                               42.60 
_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                                 9IT4 
_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                            2.39 
_refine.ls_d_res_low                             36.88 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     11408 
_refine.ls_number_reflns_R_free                  1142 
_refine.ls_number_reflns_R_work                  10266 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.03 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2254 
_refine.ls_R_factor_R_free                       0.2653 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2210 
_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                          0.42 
_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                      6BP4 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.2182 
_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                            0.2617 
_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                       2.39 
_refine_hist.d_res_low                        36.88 
_refine_hist.number_atoms_solvent             142 
_refine_hist.number_atoms_total               2435 
_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        2262 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.0050  ? 2339 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8845  ? 3161 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0520  ? 333  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0044  ? 419  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.7538 ? 862  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.39 2.50  . . 108 980  70.51 . . . . 0.2622 . . . . . . . . . . . 0.3369 
'X-RAY DIFFRACTION' 2.50 2.63  . . 116 1075 76.20 . . . . 0.2670 . . . . . . . . . . . 0.3396 
'X-RAY DIFFRACTION' 2.63 2.79  . . 132 1186 84.76 . . . . 0.2539 . . . . . . . . . . . 0.3394 
'X-RAY DIFFRACTION' 2.80 3.01  . . 153 1343 96.52 . . . . 0.2434 . . . . . . . . . . . 0.2783 
'X-RAY DIFFRACTION' 3.01 3.31  . . 156 1394 98.98 . . . . 0.2300 . . . . . . . . . . . 0.2947 
'X-RAY DIFFRACTION' 3.31 3.79  . . 149 1351 95.30 . . . . 0.2206 . . . . . . . . . . . 0.2870 
'X-RAY DIFFRACTION' 3.79 4.78  . . 160 1430 98.82 . . . . 0.1871 . . . . . . . . . . . 0.1936 
'X-RAY DIFFRACTION' 4.78 36.88 . . 168 1507 98.13 . . . . 0.2102 . . . . . . . . . . . 0.2422 
# 
_struct.entry_id                     9IT4 
_struct.title                        'Structure of Clr4 catalyzing histone H3 K9 methylation' 
_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        9IT4 
_struct_keywords.text            'Epigenetics, Methylation, Crosstalk, Histone, GENE REGULATION' 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
# 
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 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CLR4_SCHPO O60016 ? 1 
;PSKLDSYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRLTQGVIPPDPNFQSGCNCSSLGGCDL
NNPSRCECLDDLDEPTHFAYDAQGRVRADTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFAPA
GTFITCYLGEVITSAEAAKRDKNYDDDGITYLFDLDMFDDASEYTVDAQNYGDVSRFFNHSCSPNIAIYSAVRNHGFRTI
YDLAFFAIKDIQPLEELTFDYAGAKDFSPVQSQKSQQNRISKLRRQCKCGSANCRGWLFG
;
191 
2 UNP H31_SCHPO  P09988 ? 2 TKQTARKSTGGKAPRKQ 4   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9IT4 B 2 ? 301 ? O60016 191 ? 490 ? 191 490 
2 2 9IT4 F 1 ? 17  ? P09988 4   ? 20  ? 3   19  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9IT4 GLY B 1  ? UNP O60016 ?   ?  'expression tag'      190 1 
2 9IT4 NLE F 7  ? UNP P09988 LYS 10 'engineered mutation' 9   2 
2 9IT4 CYS F 12 ? UNP P09988 LYS 15 'engineered mutation' 14  3 
# 
_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)' 1800  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  14320 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            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 12  ? GLU A 26  ? SER B 201 GLU B 215 1 ? 15 
HELX_P HELX_P2 AA2 ASP A 64  ? GLN A 68  ? ASP B 253 GLN B 257 5 ? 5  
HELX_P HELX_P3 AA3 CYS A 87  ? ASP A 91  ? CYS B 276 ASP B 280 5 ? 5  
HELX_P HELX_P4 AA4 ARG A 131 ? GLY A 136 ? ARG B 320 GLY B 325 1 ? 6  
HELX_P HELX_P5 AA5 THR A 174 ? ASP A 182 ? THR B 363 ASP B 371 1 ? 9  
HELX_P HELX_P6 AA6 VAL A 215 ? PHE A 219 ? VAL B 404 PHE B 408 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? B ARG 6   C  ? ? ? 1_555 B NLE 7 N  ? ? F ARG 8   F NLE 9   1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale2  covale both ? B NLE 7   C  ? ? ? 1_555 B SER 8 N  ? ? F NLE 9   F SER 10  1_555 ? ? ? ? ? ? ? 1.328 ? ? 
metalc1  metalc ?    ? A CYS 71  SG ? ? ? 1_555 D ZN  . ZN ? ? B CYS 260 B ZN  502 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc2  metalc ?    ? A CYS 71  SG ? ? ? 1_555 E ZN  . ZN ? ? B CYS 260 B ZN  503 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc3  metalc ?    ? A CYS 73  SG ? ? ? 1_555 E ZN  . ZN ? ? B CYS 262 B ZN  503 1_555 ? ? ? ? ? ? ? 2.321 ? ? 
metalc4  metalc ?    ? A CYS 79  SG ? ? ? 1_555 E ZN  . ZN ? ? B CYS 268 B ZN  503 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc5  metalc ?    ? A CYS 79  SG ? ? ? 1_555 F ZN  . ZN ? ? B CYS 268 B ZN  504 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc6  metalc ?    ? A CYS 87  SG ? ? ? 1_555 E ZN  . ZN ? ? B CYS 276 B ZN  503 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc7  metalc ?    ? A CYS 89  SG ? ? ? 1_555 D ZN  . ZN ? ? B CYS 278 B ZN  502 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc8  metalc ?    ? A CYS 118 SG ? ? ? 1_555 D ZN  . ZN ? ? B CYS 307 B ZN  502 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc9  metalc ?    ? A CYS 118 SG ? ? ? 1_555 F ZN  . ZN ? ? B CYS 307 B ZN  504 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc10 metalc ?    ? A CYS 122 SG ? ? ? 1_555 D ZN  . ZN ? ? B CYS 311 B ZN  502 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc11 metalc ?    ? A CYS 124 SG ? ? ? 1_555 F ZN  . ZN ? ? B CYS 313 B ZN  504 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc12 metalc ?    ? A CYS 128 SG ? ? ? 1_555 F ZN  . ZN ? ? B CYS 317 B ZN  504 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc13 metalc ?    ? A CYS 223 SG ? ? ? 1_555 G ZN  . ZN ? ? B CYS 412 B ZN  505 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc14 metalc ?    ? A CYS 288 SG ? ? ? 1_555 G ZN  . ZN ? ? B CYS 477 B ZN  505 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc15 metalc ?    ? A CYS 290 SG ? ? ? 1_555 G ZN  . ZN ? ? B CYS 479 B ZN  505 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc16 metalc ?    ? A CYS 295 SG ? ? ? 1_555 G ZN  . ZN ? ? B CYS 484 B ZN  505 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 71  ? B CYS 260 ? 1_555 ZN ? D ZN . ? B ZN 502 ? 1_555 SG ? A CYS 89  ? B CYS 278 ? 1_555 113.7 ? 
2  SG ? A CYS 71  ? B CYS 260 ? 1_555 ZN ? D ZN . ? B ZN 502 ? 1_555 SG ? A CYS 118 ? B CYS 307 ? 1_555 111.5 ? 
3  SG ? A CYS 89  ? B CYS 278 ? 1_555 ZN ? D ZN . ? B ZN 502 ? 1_555 SG ? A CYS 118 ? B CYS 307 ? 1_555 110.9 ? 
4  SG ? A CYS 71  ? B CYS 260 ? 1_555 ZN ? D ZN . ? B ZN 502 ? 1_555 SG ? A CYS 122 ? B CYS 311 ? 1_555 105.7 ? 
5  SG ? A CYS 89  ? B CYS 278 ? 1_555 ZN ? D ZN . ? B ZN 502 ? 1_555 SG ? A CYS 122 ? B CYS 311 ? 1_555 100.1 ? 
6  SG ? A CYS 118 ? B CYS 307 ? 1_555 ZN ? D ZN . ? B ZN 502 ? 1_555 SG ? A CYS 122 ? B CYS 311 ? 1_555 114.3 ? 
7  SG ? A CYS 71  ? B CYS 260 ? 1_555 ZN ? E ZN . ? B ZN 503 ? 1_555 SG ? A CYS 73  ? B CYS 262 ? 1_555 110.7 ? 
8  SG ? A CYS 71  ? B CYS 260 ? 1_555 ZN ? E ZN . ? B ZN 503 ? 1_555 SG ? A CYS 79  ? B CYS 268 ? 1_555 106.5 ? 
9  SG ? A CYS 73  ? B CYS 262 ? 1_555 ZN ? E ZN . ? B ZN 503 ? 1_555 SG ? A CYS 79  ? B CYS 268 ? 1_555 104.9 ? 
10 SG ? A CYS 71  ? B CYS 260 ? 1_555 ZN ? E ZN . ? B ZN 503 ? 1_555 SG ? A CYS 87  ? B CYS 276 ? 1_555 106.6 ? 
11 SG ? A CYS 73  ? B CYS 262 ? 1_555 ZN ? E ZN . ? B ZN 503 ? 1_555 SG ? A CYS 87  ? B CYS 276 ? 1_555 117.1 ? 
12 SG ? A CYS 79  ? B CYS 268 ? 1_555 ZN ? E ZN . ? B ZN 503 ? 1_555 SG ? A CYS 87  ? B CYS 276 ? 1_555 110.6 ? 
13 SG ? A CYS 79  ? B CYS 268 ? 1_555 ZN ? F ZN . ? B ZN 504 ? 1_555 SG ? A CYS 118 ? B CYS 307 ? 1_555 107.1 ? 
14 SG ? A CYS 79  ? B CYS 268 ? 1_555 ZN ? F ZN . ? B ZN 504 ? 1_555 SG ? A CYS 124 ? B CYS 313 ? 1_555 104.7 ? 
15 SG ? A CYS 118 ? B CYS 307 ? 1_555 ZN ? F ZN . ? B ZN 504 ? 1_555 SG ? A CYS 124 ? B CYS 313 ? 1_555 111.1 ? 
16 SG ? A CYS 79  ? B CYS 268 ? 1_555 ZN ? F ZN . ? B ZN 504 ? 1_555 SG ? A CYS 128 ? B CYS 317 ? 1_555 104.6 ? 
17 SG ? A CYS 118 ? B CYS 307 ? 1_555 ZN ? F ZN . ? B ZN 504 ? 1_555 SG ? A CYS 128 ? B CYS 317 ? 1_555 113.6 ? 
18 SG ? A CYS 124 ? B CYS 313 ? 1_555 ZN ? F ZN . ? B ZN 504 ? 1_555 SG ? A CYS 128 ? B CYS 317 ? 1_555 114.8 ? 
19 SG ? A CYS 223 ? B CYS 412 ? 1_555 ZN ? G ZN . ? B ZN 505 ? 1_555 SG ? A CYS 288 ? B CYS 477 ? 1_555 113.6 ? 
20 SG ? A CYS 223 ? B CYS 412 ? 1_555 ZN ? G ZN . ? B ZN 505 ? 1_555 SG ? A CYS 290 ? B CYS 479 ? 1_555 109.1 ? 
21 SG ? A CYS 288 ? B CYS 477 ? 1_555 ZN ? G ZN . ? B ZN 505 ? 1_555 SG ? A CYS 290 ? B CYS 479 ? 1_555 105.8 ? 
22 SG ? A CYS 223 ? B CYS 412 ? 1_555 ZN ? G ZN . ? B ZN 505 ? 1_555 SG ? A CYS 295 ? B CYS 484 ? 1_555 109.0 ? 
23 SG ? A CYS 288 ? B CYS 477 ? 1_555 ZN ? G ZN . ? B ZN 505 ? 1_555 SG ? A CYS 295 ? B CYS 484 ? 1_555 109.3 ? 
24 SG ? A CYS 290 ? B CYS 479 ? 1_555 ZN ? G ZN . ? B ZN 505 ? 1_555 SG ? A CYS 295 ? B CYS 484 ? 1_555 110.0 ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      NLE 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       7 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       NLE 
_pdbx_modification_feature.auth_asym_id                       F 
_pdbx_modification_feature.auth_seq_id                        9 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                LEU 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        NLE 
_pdbx_modification_feature.type                               Norleucine 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           95 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            284 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    96 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     285 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.10 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
# 
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 ? parallel      
AA1 2 3 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? 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 32  ? VAL A 35  ? VAL B 221 VAL B 224 
AA1 2 LEU A 141 ? LYS A 145 ? LEU B 330 LYS B 334 
AA1 3 TRP A 151 ? SER A 155 ? TRP B 340 SER B 344 
AA2 1 GLN A 49  ? PHE A 50  ? GLN B 238 PHE B 239 
AA2 2 THR A 206 ? GLY A 213 ? THR B 395 GLY B 402 
AA2 3 GLY A 170 ? ILE A 173 ? GLY B 359 ILE B 362 
AA2 4 ARG A 55  ? LEU A 56  ? ARG B 244 LEU B 245 
AA3 1 GLN A 49  ? PHE A 50  ? GLN B 238 PHE B 239 
AA3 2 THR A 206 ? GLY A 213 ? THR B 395 GLY B 402 
AA3 3 LEU A 193 ? ASP A 195 ? LEU B 382 ASP B 384 
AA4 1 VAL A 114 ? TYR A 116 ? VAL B 303 TYR B 305 
AA4 2 ILE A 227 ? VAL A 233 ? ILE B 416 VAL B 422 
AA4 3 ASP A 243 ? ALA A 248 ? ASP B 432 ALA B 437 
AA4 4 PHE A 164 ? CYS A 167 ? PHE B 353 CYS B 356 
AA5 1 ASN A 220 ? HIS A 221 ? ASN B 409 HIS B 410 
AA5 2 THR A 259 ? PHE A 260 ? THR B 448 PHE B 449 
# 
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 N THR A 33  ? N THR B 222 O ILE A 143 ? O ILE B 332 
AA1 2 3 N PHE A 144 ? N PHE B 333 O GLY A 152 ? O GLY B 341 
AA2 1 2 N GLN A 49  ? N GLN B 238 O ASN A 211 ? O ASN B 400 
AA2 2 3 O ASP A 208 ? O ASP B 397 N GLU A 171 ? N GLU B 360 
AA2 3 4 O GLY A 170 ? O GLY B 359 N ARG A 55  ? N ARG B 244 
AA3 1 2 N GLN A 49  ? N GLN B 238 O ASN A 211 ? O ASN B 400 
AA3 2 3 O VAL A 207 ? O VAL B 396 N PHE A 194 ? N PHE B 383 
AA4 1 2 N ILE A 115 ? N ILE B 304 O VAL A 233 ? O VAL B 422 
AA4 2 3 N ALA A 228 ? N ALA B 417 O PHE A 247 ? O PHE B 436 
AA4 3 4 O PHE A 246 ? O PHE B 435 N THR A 166 ? N THR B 355 
AA5 1 2 N ASN A 220 ? N ASN B 409 O PHE A 260 ? O PHE B 449 
# 
_pdbx_entry_details.entry_id                   9IT4 
_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   Y 
# 
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 PRO B 233 ? ? -67.66  -176.00 
2 1 ASN B 261 ? ? -109.70 73.76   
3 1 ILE B 354 ? ? -94.75  -65.32  
4 1 ASP B 371 ? ? -66.64  0.68    
5 1 ARG B 475 ? ? 53.09   -127.47 
6 1 ALA F 7   ? ? -92.12  55.63   
7 1 ARG F 17  ? ? -154.88 13.44   
8 1 LYS F 18  ? ? 68.92   92.29   
# 
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 B HOH 681 ? H HOH . 
2 1 B HOH 714 ? H HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x,-y,-z         
3 -x,y+1/2,-z+1/2 
4 -x,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 22.9072548828  18.4813687557  4.07866056676 0.554064502527 ? 0.106923638209   ? 0.0702598625322  ? 
0.260347291818 ? -0.0379436757869  ? 0.354111086832 ? 4.25603628999  ? 2.06688381436   ? 2.51455856228   ? 3.27175540425 ? 
-2.89192556437  ? 9.06097171667 ? 0.16450117952    ? 0.30117306722    ? -0.141438413618  ? -0.189090629219 ? -0.398140666247  ? 
-0.0569020309743 ? -0.158318370804  ? 0.0412398138159 ? 0.120190485424  ? 
2 'X-RAY DIFFRACTION' ? refined 21.3395174906  5.36679645298  29.0779692932 0.138226908635 ? -0.0207083998104 ? 0.0291300699486  ? 
0.167432830318 ? -0.00225306289437 ? 0.210732673198 ? 0.924273155578 ? -0.500981602914 ? 0.348780533254  ? 3.40140446612 ? 
-0.492654185265 ? 2.86156727645 ? -0.0749320197717 ? 0.00352263170737 ? -0.0258182543912 ? 0.160862750837  ? -0.117969963216  ? 
-0.225339746102  ? 0.0368386652889  ? 0.20806555664   ? 0.171790483415  ? 
3 'X-RAY DIFFRACTION' ? refined 9.08661666578  9.28593365791  25.7285869603 0.126814894158 ? -0.0268107334139 ? -0.0182388580007 ? 
0.213685359416 ? -0.0227781200692  ? 0.265998253061 ? 1.25223335249  ? -1.12104322749  ? -0.361877799371 ? 6.90843992764 ? 
0.819971145871  ? 2.55225952887 ? -0.0555784485891 ? -0.0963868189386 ? -0.0658433370809 ? 0.0139763937047 ? -0.114508449307  ? 
0.765101747055   ? -0.0173449740966 ? -0.447863264499 ? 0.0745465047658 ? 
4 'X-RAY DIFFRACTION' ? refined 14.464677328   -3.74172093794 17.4796107347 0.413079285562 ? -0.138933636215  ? 0.00120503617291 ? 
0.127542471594 ? -0.0900595650485  ? 0.277700974578 ? 5.65179659586  ? -1.32808004866  ? -2.39290683992  ? 4.87108250144 ? 
-0.080964010889 ? 3.59100660281 ? -0.494063228801  ? 0.328651909319   ? -0.692323713911  ? -0.690884294826 ? -0.0575544352501 ? 
0.522696777592   ? 0.486181111279   ? -0.214590623791 ? 0.210510067949  ? 
5 'X-RAY DIFFRACTION' ? refined 2.44377454527  -4.5708565985  13.4059857923 0.351073342789 ? -0.11106703496   ? -0.151888815275  ? 
0.44029891428  ? 0.0094346266213   ? 0.694551615291 ? 4.0675169519   ? -1.17300030153  ? 3.11046398138   ? 6.55974497191 ? 
-1.25639504151  ? 5.34152058315 ? 0.132047108109   ? -0.713686092265  ? -0.0741759959799 ? -0.222592343629 ? 0.495990541545   ? 
1.64554183898    ? 0.314892467716   ? -0.882406161863 ? -0.44254088328  ? 
6 'X-RAY DIFFRACTION' ? refined -1.57274632188 7.33031037404  23.2361469678 0.470600449859 ? -0.23550044125   ? 0.27828629121    ? 
0.891600647817 ? -0.131888348157   ? 0.527947098986 ? 7.29368285668  ? -9.9142176626   ? 4.90279968424   ? 2.00072796735 ? 
-5.29360964203  ? 4.48863429421 ? 0.110852557725   ? -0.662428628614  ? -1.11499472551   ? 2.10360906524   ? -0.166663567368  ? 
2.49759028418    ? 1.2826466697     ? -2.69910308116  ? 0.0409736581891 ? 
7 'X-RAY DIFFRACTION' ? refined 6.77771635454  -4.25428136447 32.884563147  0.788650264601 ? 0.170425869816   ? 0.00449603632141 ? 
0.487870363872 ? 0.124528704353    ? 0.964296164532 ? 1.69982163171  ? -2.40904155391  ? -0.645361258711 ? 7.472821777   ? 
6.18503617889   ? 7.11584161624 ? -0.0462643791159 ? -0.395722733561  ? -2.28098906931   ? 1.39655631686   ? -0.28612594219   ? 
-0.0709299574665 ? 2.95669645212    ? 1.34272522639   ? 0.16235249478   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   B 195 ? A 20  B 214 ? ? 
;chain 'B' and (resid 195 through 214 )
;
2 'X-RAY DIFFRACTION' 2 A 21  B 215 ? A 162 B 359 ? ? 
;chain 'B' and (resid 215 through 359 )
;
3 'X-RAY DIFFRACTION' 3 A 163 B 360 ? A 238 B 437 ? ? 
;chain 'B' and (resid 360 through 437 )
;
4 'X-RAY DIFFRACTION' 4 A 239 B 438 ? A 257 B 475 ? ? 
;chain 'B' and (resid 438 through 475 )
;
5 'X-RAY DIFFRACTION' 5 A 258 B 476 ? A 272 B 490 ? ? 
;chain 'B' and (resid 476 through 490 )
;
6 'X-RAY DIFFRACTION' 6 H 1   F 5   ? H 4   F 8   ? ? 
;chain 'F' and (resid 5 through 8 )
;
7 'X-RAY DIFFRACTION' 7 H 6   F 10  ? H 14  F 18  ? ? 
;chain 'F' and (resid 10 through 18 )
;
# 
_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                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       740 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.90 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B GLY 190 ? A GLY 1   
2  1 Y 1 B PRO 191 ? A PRO 2   
3  1 Y 1 B SER 192 ? A SER 3   
4  1 Y 1 B LYS 193 ? A LYS 4   
5  1 Y 1 B LEU 194 ? A LEU 5   
6  1 Y 1 B SER 264 ? A SER 75  
7  1 Y 1 B LEU 265 ? A LEU 76  
8  1 Y 1 B GLY 266 ? A GLY 77  
9  1 Y 1 B ASN 373 ? A ASN 184 
10 1 Y 1 B TYR 374 ? A TYR 185 
11 1 Y 1 B LYS 455 ? A LYS 266 
12 1 Y 1 B ASP 456 ? A ASP 267 
13 1 Y 1 B PHE 457 ? A PHE 268 
14 1 Y 1 B SER 458 ? A SER 269 
15 1 Y 1 B PRO 459 ? A PRO 270 
16 1 Y 1 B VAL 460 ? A VAL 271 
17 1 Y 1 B GLN 461 ? A GLN 272 
18 1 Y 1 B SER 462 ? A SER 273 
19 1 Y 1 B GLN 463 ? A GLN 274 
20 1 Y 1 B LYS 464 ? A LYS 275 
21 1 Y 1 B SER 465 ? A SER 276 
22 1 Y 1 B GLN 466 ? A GLN 277 
23 1 Y 1 B GLN 467 ? A GLN 278 
24 1 Y 1 B ASN 468 ? A ASN 279 
25 1 Y 1 B ARG 469 ? A ARG 280 
26 1 Y 1 B ILE 470 ? A ILE 281 
27 1 Y 1 B SER 471 ? A SER 282 
28 1 Y 1 B LYS 472 ? A LYS 283 
29 1 Y 1 B LEU 473 ? A LEU 284 
30 1 Y 1 F THR 3   ? B THR 1   
31 1 Y 1 F LYS 4   ? B LYS 2   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
HIS N      N  N N 137 
HIS CA     C  N S 138 
HIS C      C  N N 139 
HIS O      O  N N 140 
HIS CB     C  N N 141 
HIS CG     C  Y N 142 
HIS ND1    N  Y N 143 
HIS CD2    C  Y N 144 
HIS CE1    C  Y N 145 
HIS NE2    N  Y N 146 
HIS OXT    O  N N 147 
HIS H      H  N N 148 
HIS H2     H  N N 149 
HIS HA     H  N N 150 
HIS HB2    H  N N 151 
HIS HB3    H  N N 152 
HIS HD1    H  N N 153 
HIS HD2    H  N N 154 
HIS HE1    H  N N 155 
HIS HE2    H  N N 156 
HIS HXT    H  N N 157 
HOH O      O  N N 158 
HOH H1     H  N N 159 
HOH H2     H  N N 160 
ILE N      N  N N 161 
ILE CA     C  N S 162 
ILE C      C  N N 163 
ILE O      O  N N 164 
ILE CB     C  N S 165 
ILE CG1    C  N N 166 
ILE CG2    C  N N 167 
ILE CD1    C  N N 168 
ILE OXT    O  N N 169 
ILE H      H  N N 170 
ILE H2     H  N N 171 
ILE HA     H  N N 172 
ILE HB     H  N N 173 
ILE HG12   H  N N 174 
ILE HG13   H  N N 175 
ILE HG21   H  N N 176 
ILE HG22   H  N N 177 
ILE HG23   H  N N 178 
ILE HD11   H  N N 179 
ILE HD12   H  N N 180 
ILE HD13   H  N N 181 
ILE HXT    H  N N 182 
LEU N      N  N N 183 
LEU CA     C  N S 184 
LEU C      C  N N 185 
LEU O      O  N N 186 
LEU CB     C  N N 187 
LEU CG     C  N N 188 
LEU CD1    C  N N 189 
LEU CD2    C  N N 190 
LEU OXT    O  N N 191 
LEU H      H  N N 192 
LEU H2     H  N N 193 
LEU HA     H  N N 194 
LEU HB2    H  N N 195 
LEU HB3    H  N N 196 
LEU HG     H  N N 197 
LEU HD11   H  N N 198 
LEU HD12   H  N N 199 
LEU HD13   H  N N 200 
LEU HD21   H  N N 201 
LEU HD22   H  N N 202 
LEU HD23   H  N N 203 
LEU HXT    H  N N 204 
LYS N      N  N N 205 
LYS CA     C  N S 206 
LYS C      C  N N 207 
LYS O      O  N N 208 
LYS CB     C  N N 209 
LYS CG     C  N N 210 
LYS CD     C  N N 211 
LYS CE     C  N N 212 
LYS NZ     N  N N 213 
LYS OXT    O  N N 214 
LYS H      H  N N 215 
LYS H2     H  N N 216 
LYS HA     H  N N 217 
LYS HB2    H  N N 218 
LYS HB3    H  N N 219 
LYS HG2    H  N N 220 
LYS HG3    H  N N 221 
LYS HD2    H  N N 222 
LYS HD3    H  N N 223 
LYS HE2    H  N N 224 
LYS HE3    H  N N 225 
LYS HZ1    H  N N 226 
LYS HZ2    H  N N 227 
LYS HZ3    H  N N 228 
LYS HXT    H  N N 229 
MET N      N  N N 230 
MET CA     C  N S 231 
MET C      C  N N 232 
MET O      O  N N 233 
MET CB     C  N N 234 
MET CG     C  N N 235 
MET SD     S  N N 236 
MET CE     C  N N 237 
MET OXT    O  N N 238 
MET H      H  N N 239 
MET H2     H  N N 240 
MET HA     H  N N 241 
MET HB2    H  N N 242 
MET HB3    H  N N 243 
MET HG2    H  N N 244 
MET HG3    H  N N 245 
MET HE1    H  N N 246 
MET HE2    H  N N 247 
MET HE3    H  N N 248 
MET HXT    H  N N 249 
NLE N      N  N N 250 
NLE CA     C  N S 251 
NLE C      C  N N 252 
NLE O      O  N N 253 
NLE OXT    O  N N 254 
NLE CB     C  N N 255 
NLE CG     C  N N 256 
NLE CD     C  N N 257 
NLE CE     C  N N 258 
NLE H      H  N N 259 
NLE H2     H  N N 260 
NLE HA     H  N N 261 
NLE HXT    H  N N 262 
NLE HB2    H  N N 263 
NLE HB3    H  N N 264 
NLE HG2    H  N N 265 
NLE HG3    H  N N 266 
NLE HD2    H  N N 267 
NLE HD3    H  N N 268 
NLE HE1    H  N N 269 
NLE HE2    H  N N 270 
NLE HE3    H  N N 271 
PHE N      N  N N 272 
PHE CA     C  N S 273 
PHE C      C  N N 274 
PHE O      O  N N 275 
PHE CB     C  N N 276 
PHE CG     C  Y N 277 
PHE CD1    C  Y N 278 
PHE CD2    C  Y N 279 
PHE CE1    C  Y N 280 
PHE CE2    C  Y N 281 
PHE CZ     C  Y N 282 
PHE OXT    O  N N 283 
PHE H      H  N N 284 
PHE H2     H  N N 285 
PHE HA     H  N N 286 
PHE HB2    H  N N 287 
PHE HB3    H  N N 288 
PHE HD1    H  N N 289 
PHE HD2    H  N N 290 
PHE HE1    H  N N 291 
PHE HE2    H  N N 292 
PHE HZ     H  N N 293 
PHE HXT    H  N N 294 
PRO N      N  N N 295 
PRO CA     C  N S 296 
PRO C      C  N N 297 
PRO O      O  N N 298 
PRO CB     C  N N 299 
PRO CG     C  N N 300 
PRO CD     C  N N 301 
PRO OXT    O  N N 302 
PRO H      H  N N 303 
PRO HA     H  N N 304 
PRO HB2    H  N N 305 
PRO HB3    H  N N 306 
PRO HG2    H  N N 307 
PRO HG3    H  N N 308 
PRO HD2    H  N N 309 
PRO HD3    H  N N 310 
PRO HXT    H  N N 311 
SAM N      N  N N 312 
SAM CA     C  N S 313 
SAM C      C  N N 314 
SAM O      O  N N 315 
SAM OXT    O  N N 316 
SAM CB     C  N N 317 
SAM CG     C  N N 318 
SAM SD     S  N S 319 
SAM CE     C  N N 320 
SAM "C5'"  C  N N 321 
SAM "C4'"  C  N S 322 
SAM "O4'"  O  N N 323 
SAM "C3'"  C  N S 324 
SAM "O3'"  O  N N 325 
SAM "C2'"  C  N R 326 
SAM "O2'"  O  N N 327 
SAM "C1'"  C  N R 328 
SAM N9     N  Y N 329 
SAM C8     C  Y N 330 
SAM N7     N  Y N 331 
SAM C5     C  Y N 332 
SAM C6     C  Y N 333 
SAM N6     N  N N 334 
SAM N1     N  Y N 335 
SAM C2     C  Y N 336 
SAM N3     N  Y N 337 
SAM C4     C  Y N 338 
SAM HN1    H  N N 339 
SAM HN2    H  N N 340 
SAM HA     H  N N 341 
SAM HB1    H  N N 342 
SAM HB2    H  N N 343 
SAM HG1    H  N N 344 
SAM HG2    H  N N 345 
SAM HE1    H  N N 346 
SAM HE2    H  N N 347 
SAM HE3    H  N N 348 
SAM "H5'1" H  N N 349 
SAM "H5'2" H  N N 350 
SAM "H4'"  H  N N 351 
SAM "H3'"  H  N N 352 
SAM "HO3'" H  N N 353 
SAM "H2'"  H  N N 354 
SAM "HO2'" H  N N 355 
SAM "H1'"  H  N N 356 
SAM H8     H  N N 357 
SAM HN61   H  N N 358 
SAM HN62   H  N N 359 
SAM H2     H  N N 360 
SER N      N  N N 361 
SER CA     C  N S 362 
SER C      C  N N 363 
SER O      O  N N 364 
SER CB     C  N N 365 
SER OG     O  N N 366 
SER OXT    O  N N 367 
SER H      H  N N 368 
SER H2     H  N N 369 
SER HA     H  N N 370 
SER HB2    H  N N 371 
SER HB3    H  N N 372 
SER HG     H  N N 373 
SER HXT    H  N N 374 
THR N      N  N N 375 
THR CA     C  N S 376 
THR C      C  N N 377 
THR O      O  N N 378 
THR CB     C  N R 379 
THR OG1    O  N N 380 
THR CG2    C  N N 381 
THR OXT    O  N N 382 
THR H      H  N N 383 
THR H2     H  N N 384 
THR HA     H  N N 385 
THR HB     H  N N 386 
THR HG1    H  N N 387 
THR HG21   H  N N 388 
THR HG22   H  N N 389 
THR HG23   H  N N 390 
THR HXT    H  N N 391 
TRP N      N  N N 392 
TRP CA     C  N S 393 
TRP C      C  N N 394 
TRP O      O  N N 395 
TRP CB     C  N N 396 
TRP CG     C  Y N 397 
TRP CD1    C  Y N 398 
TRP CD2    C  Y N 399 
TRP NE1    N  Y N 400 
TRP CE2    C  Y N 401 
TRP CE3    C  Y N 402 
TRP CZ2    C  Y N 403 
TRP CZ3    C  Y N 404 
TRP CH2    C  Y N 405 
TRP OXT    O  N N 406 
TRP H      H  N N 407 
TRP H2     H  N N 408 
TRP HA     H  N N 409 
TRP HB2    H  N N 410 
TRP HB3    H  N N 411 
TRP HD1    H  N N 412 
TRP HE1    H  N N 413 
TRP HE3    H  N N 414 
TRP HZ2    H  N N 415 
TRP HZ3    H  N N 416 
TRP HH2    H  N N 417 
TRP HXT    H  N N 418 
TYR N      N  N N 419 
TYR CA     C  N S 420 
TYR C      C  N N 421 
TYR O      O  N N 422 
TYR CB     C  N N 423 
TYR CG     C  Y N 424 
TYR CD1    C  Y N 425 
TYR CD2    C  Y N 426 
TYR CE1    C  Y N 427 
TYR CE2    C  Y N 428 
TYR CZ     C  Y N 429 
TYR OH     O  N N 430 
TYR OXT    O  N N 431 
TYR H      H  N N 432 
TYR H2     H  N N 433 
TYR HA     H  N N 434 
TYR HB2    H  N N 435 
TYR HB3    H  N N 436 
TYR HD1    H  N N 437 
TYR HD2    H  N N 438 
TYR HE1    H  N N 439 
TYR HE2    H  N N 440 
TYR HH     H  N N 441 
TYR HXT    H  N N 442 
VAL N      N  N N 443 
VAL CA     C  N S 444 
VAL C      C  N N 445 
VAL O      O  N N 446 
VAL CB     C  N N 447 
VAL CG1    C  N N 448 
VAL CG2    C  N N 449 
VAL OXT    O  N N 450 
VAL H      H  N N 451 
VAL H2     H  N N 452 
VAL HA     H  N N 453 
VAL HB     H  N N 454 
VAL HG11   H  N N 455 
VAL HG12   H  N N 456 
VAL HG13   H  N N 457 
VAL HG21   H  N N 458 
VAL HG22   H  N N 459 
VAL HG23   H  N N 460 
VAL HXT    H  N N 461 
ZN  ZN     ZN N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
NLE N     CA     sing N N 237 
NLE N     H      sing N N 238 
NLE N     H2     sing N N 239 
NLE CA    C      sing N N 240 
NLE CA    CB     sing N N 241 
NLE CA    HA     sing N N 242 
NLE C     O      doub N N 243 
NLE C     OXT    sing N N 244 
NLE OXT   HXT    sing N N 245 
NLE CB    CG     sing N N 246 
NLE CB    HB2    sing N N 247 
NLE CB    HB3    sing N N 248 
NLE CG    CD     sing N N 249 
NLE CG    HG2    sing N N 250 
NLE CG    HG3    sing N N 251 
NLE CD    CE     sing N N 252 
NLE CD    HD2    sing N N 253 
NLE CD    HD3    sing N N 254 
NLE CE    HE1    sing N N 255 
NLE CE    HE2    sing N N 256 
NLE CE    HE3    sing N N 257 
PHE N     CA     sing N N 258 
PHE N     H      sing N N 259 
PHE N     H2     sing N N 260 
PHE CA    C      sing N N 261 
PHE CA    CB     sing N N 262 
PHE CA    HA     sing N N 263 
PHE C     O      doub N N 264 
PHE C     OXT    sing N N 265 
PHE CB    CG     sing N N 266 
PHE CB    HB2    sing N N 267 
PHE CB    HB3    sing N N 268 
PHE CG    CD1    doub Y N 269 
PHE CG    CD2    sing Y N 270 
PHE CD1   CE1    sing Y N 271 
PHE CD1   HD1    sing N N 272 
PHE CD2   CE2    doub Y N 273 
PHE CD2   HD2    sing N N 274 
PHE CE1   CZ     doub Y N 275 
PHE CE1   HE1    sing N N 276 
PHE CE2   CZ     sing Y N 277 
PHE CE2   HE2    sing N N 278 
PHE CZ    HZ     sing N N 279 
PHE OXT   HXT    sing N N 280 
PRO N     CA     sing N N 281 
PRO N     CD     sing N N 282 
PRO N     H      sing N N 283 
PRO CA    C      sing N N 284 
PRO CA    CB     sing N N 285 
PRO CA    HA     sing N N 286 
PRO C     O      doub N N 287 
PRO C     OXT    sing N N 288 
PRO CB    CG     sing N N 289 
PRO CB    HB2    sing N N 290 
PRO CB    HB3    sing N N 291 
PRO CG    CD     sing N N 292 
PRO CG    HG2    sing N N 293 
PRO CG    HG3    sing N N 294 
PRO CD    HD2    sing N N 295 
PRO CD    HD3    sing N N 296 
PRO OXT   HXT    sing N N 297 
SAM N     CA     sing N N 298 
SAM N     HN1    sing N N 299 
SAM N     HN2    sing N N 300 
SAM CA    C      sing N N 301 
SAM CA    CB     sing N N 302 
SAM CA    HA     sing N N 303 
SAM C     O      doub N N 304 
SAM C     OXT    sing N N 305 
SAM CB    CG     sing N N 306 
SAM CB    HB1    sing N N 307 
SAM CB    HB2    sing N N 308 
SAM CG    SD     sing N N 309 
SAM CG    HG1    sing N N 310 
SAM CG    HG2    sing N N 311 
SAM SD    CE     sing N N 312 
SAM SD    "C5'"  sing N N 313 
SAM CE    HE1    sing N N 314 
SAM CE    HE2    sing N N 315 
SAM CE    HE3    sing N N 316 
SAM "C5'" "C4'"  sing N N 317 
SAM "C5'" "H5'1" sing N N 318 
SAM "C5'" "H5'2" sing N N 319 
SAM "C4'" "O4'"  sing N N 320 
SAM "C4'" "C3'"  sing N N 321 
SAM "C4'" "H4'"  sing N N 322 
SAM "O4'" "C1'"  sing N N 323 
SAM "C3'" "O3'"  sing N N 324 
SAM "C3'" "C2'"  sing N N 325 
SAM "C3'" "H3'"  sing N N 326 
SAM "O3'" "HO3'" sing N N 327 
SAM "C2'" "O2'"  sing N N 328 
SAM "C2'" "C1'"  sing N N 329 
SAM "C2'" "H2'"  sing N N 330 
SAM "O2'" "HO2'" sing N N 331 
SAM "C1'" N9     sing N N 332 
SAM "C1'" "H1'"  sing N N 333 
SAM N9    C8     sing Y N 334 
SAM N9    C4     sing Y N 335 
SAM C8    N7     doub Y N 336 
SAM C8    H8     sing N N 337 
SAM N7    C5     sing Y N 338 
SAM C5    C6     sing Y N 339 
SAM C5    C4     doub Y N 340 
SAM C6    N6     sing N N 341 
SAM C6    N1     doub Y N 342 
SAM N6    HN61   sing N N 343 
SAM N6    HN62   sing N N 344 
SAM N1    C2     sing Y N 345 
SAM C2    N3     doub Y N 346 
SAM C2    H2     sing N N 347 
SAM N3    C4     sing Y N 348 
SER N     CA     sing N N 349 
SER N     H      sing N N 350 
SER N     H2     sing N N 351 
SER CA    C      sing N N 352 
SER CA    CB     sing N N 353 
SER CA    HA     sing N N 354 
SER C     O      doub N N 355 
SER C     OXT    sing N N 356 
SER CB    OG     sing N N 357 
SER CB    HB2    sing N N 358 
SER CB    HB3    sing N N 359 
SER OG    HG     sing N N 360 
SER OXT   HXT    sing N N 361 
THR N     CA     sing N N 362 
THR N     H      sing N N 363 
THR N     H2     sing N N 364 
THR CA    C      sing N N 365 
THR CA    CB     sing N N 366 
THR CA    HA     sing N N 367 
THR C     O      doub N N 368 
THR C     OXT    sing N N 369 
THR CB    OG1    sing N N 370 
THR CB    CG2    sing N N 371 
THR CB    HB     sing N N 372 
THR OG1   HG1    sing N N 373 
THR CG2   HG21   sing N N 374 
THR CG2   HG22   sing N N 375 
THR CG2   HG23   sing N N 376 
THR OXT   HXT    sing N N 377 
TRP N     CA     sing N N 378 
TRP N     H      sing N N 379 
TRP N     H2     sing N N 380 
TRP CA    C      sing N N 381 
TRP CA    CB     sing N N 382 
TRP CA    HA     sing N N 383 
TRP C     O      doub N N 384 
TRP C     OXT    sing N N 385 
TRP CB    CG     sing N N 386 
TRP CB    HB2    sing N N 387 
TRP CB    HB3    sing N N 388 
TRP CG    CD1    doub Y N 389 
TRP CG    CD2    sing Y N 390 
TRP CD1   NE1    sing Y N 391 
TRP CD1   HD1    sing N N 392 
TRP CD2   CE2    doub Y N 393 
TRP CD2   CE3    sing Y N 394 
TRP NE1   CE2    sing Y N 395 
TRP NE1   HE1    sing N N 396 
TRP CE2   CZ2    sing Y N 397 
TRP CE3   CZ3    doub Y N 398 
TRP CE3   HE3    sing N N 399 
TRP CZ2   CH2    doub Y N 400 
TRP CZ2   HZ2    sing N N 401 
TRP CZ3   CH2    sing Y N 402 
TRP CZ3   HZ3    sing N N 403 
TRP CH2   HH2    sing N N 404 
TRP OXT   HXT    sing N N 405 
TYR N     CA     sing N N 406 
TYR N     H      sing N N 407 
TYR N     H2     sing N N 408 
TYR CA    C      sing N N 409 
TYR CA    CB     sing N N 410 
TYR CA    HA     sing N N 411 
TYR C     O      doub N N 412 
TYR C     OXT    sing N N 413 
TYR CB    CG     sing N N 414 
TYR CB    HB2    sing N N 415 
TYR CB    HB3    sing N N 416 
TYR CG    CD1    doub Y N 417 
TYR CG    CD2    sing Y N 418 
TYR CD1   CE1    sing Y N 419 
TYR CD1   HD1    sing N N 420 
TYR CD2   CE2    doub Y N 421 
TYR CD2   HD2    sing N N 422 
TYR CE1   CZ     doub Y N 423 
TYR CE1   HE1    sing N N 424 
TYR CE2   CZ     sing Y N 425 
TYR CE2   HE2    sing N N 426 
TYR CZ    OH     sing N N 427 
TYR OH    HH     sing N N 428 
TYR OXT   HXT    sing N N 429 
VAL N     CA     sing N N 430 
VAL N     H      sing N N 431 
VAL N     H2     sing N N 432 
VAL CA    C      sing N N 433 
VAL CA    CB     sing N N 434 
VAL CA    HA     sing N N 435 
VAL C     O      doub N N 436 
VAL C     OXT    sing N N 437 
VAL CB    CG1    sing N N 438 
VAL CB    CG2    sing N N 439 
VAL CB    HB     sing N N 440 
VAL CG1   HG11   sing N N 441 
VAL CG1   HG12   sing N N 442 
VAL CG1   HG13   sing N N 443 
VAL CG2   HG21   sing N N 444 
VAL CG2   HG22   sing N N 445 
VAL CG2   HG23   sing N N 446 
VAL OXT   HXT    sing N N 447 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22137005 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6BP4 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 2 21 21' 
_space_group.name_Hall        'P 2 2ab (z,x,y)' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9IT4 
_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]   0.025556 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014208 
_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]   0.009053 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . ASP A 1 6   ? 9.19900  21.67500  0.93800  1.000 101.41835 ? 195 ASP B N     1 
ATOM   2    C  CA    . ASP A 1 6   ? 10.54600 21.64300  1.49800  1.000 109.70261 ? 195 ASP B CA    1 
ATOM   3    C  C     . ASP A 1 6   ? 11.19600 23.02700  1.37200  1.000 102.83059 ? 195 ASP B C     1 
ATOM   4    O  O     . ASP A 1 6   ? 11.38600 23.53300  0.26400  1.000 101.06499 ? 195 ASP B O     1 
ATOM   5    C  CB    . ASP A 1 6   ? 11.40400 20.58100  0.81200  1.000 98.83935  ? 195 ASP B CB    1 
ATOM   6    C  CG    . ASP A 1 6   ? 12.52500 20.07200  1.70800  1.000 95.23693  ? 195 ASP B CG    1 
ATOM   7    O  OD1   . ASP A 1 6   ? 12.61300 20.50600  2.87000  1.000 90.87958  ? 195 ASP B OD1   1 
ATOM   8    O  OD2   . ASP A 1 6   ? 13.32100 19.22600  1.24900  1.000 87.09533  ? 195 ASP B OD2   1 
ATOM   9    N  N     . SER A 1 7   ? 11.51600 23.63100  2.52300  1.000 116.86425 ? 196 SER B N     1 
ATOM   10   C  CA    . SER A 1 7   ? 12.15700 24.93500  2.51100  1.000 117.62210 ? 196 SER B CA    1 
ATOM   11   C  C     . SER A 1 7   ? 13.62300 24.82500  2.11900  1.000 114.21604 ? 196 SER B C     1 
ATOM   12   O  O     . SER A 1 7   ? 14.18400 25.79800  1.61800  1.000 114.95315 ? 196 SER B O     1 
ATOM   13   C  CB    . SER A 1 7   ? 11.97200 25.65900  3.86100  1.000 120.14543 ? 196 SER B CB    1 
ATOM   14   O  OG    . SER A 1 7   ? 13.02000 26.62300  4.04500  1.000 119.69110 ? 196 SER B OG    1 
ATOM   15   N  N     . TYR A 1 8   ? 14.26400 23.67500  2.34300  1.000 91.03067  ? 197 TYR B N     1 
ATOM   16   C  CA    . TYR A 1 8   ? 15.61300 23.43700  1.83100  1.000 78.70161  ? 197 TYR B CA    1 
ATOM   17   C  C     . TYR A 1 8   ? 15.49800 22.84500  0.43100  1.000 70.35532  ? 197 TYR B C     1 
ATOM   18   O  O     . TYR A 1 8   ? 15.52200 21.62900  0.22900  1.000 69.16412  ? 197 TYR B O     1 
ATOM   19   C  CB    . TYR A 1 8   ? 16.38800 22.49900  2.74100  1.000 74.09205  ? 197 TYR B CB    1 
ATOM   20   C  CG    . TYR A 1 8   ? 16.56100 22.93400  4.17400  1.000 85.88738  ? 197 TYR B CG    1 
ATOM   21   C  CD1   . TYR A 1 8   ? 17.66400 23.68300  4.56700  1.000 83.05104  ? 197 TYR B CD1   1 
ATOM   22   C  CD2   . TYR A 1 8   ? 15.66300 22.51700  5.15700  1.000 96.95844  ? 197 TYR B CD2   1 
ATOM   23   C  CE1   . TYR A 1 8   ? 17.84400 24.04500  5.89600  1.000 70.88728  ? 197 TYR B CE1   1 
ATOM   24   C  CE2   . TYR A 1 8   ? 15.82800 22.87700  6.48400  1.000 76.23236  ? 197 TYR B CE2   1 
ATOM   25   C  CZ    . TYR A 1 8   ? 16.91900 23.63600  6.85300  1.000 74.60755  ? 197 TYR B CZ    1 
ATOM   26   O  OH    . TYR A 1 8   ? 17.07200 23.97900  8.18500  1.000 83.68051  ? 197 TYR B OH    1 
ATOM   27   N  N     . THR A 1 9   ? 15.32900 23.72700  -0.55000 1.000 68.83255  ? 198 THR B N     1 
ATOM   28   C  CA    . THR A 1 9   ? 15.37800 23.33500  -1.94900 1.000 68.54573  ? 198 THR B CA    1 
ATOM   29   C  C     . THR A 1 9   ? 16.48900 24.03500  -2.71000 1.000 53.73500  ? 198 THR B C     1 
ATOM   30   O  O     . THR A 1 9   ? 16.68100 23.74200  -3.89400 1.000 50.33728  ? 198 THR B O     1 
ATOM   31   C  CB    . THR A 1 9   ? 14.04000 23.60700  -2.65200 1.000 74.08384  ? 198 THR B CB    1 
ATOM   32   O  OG1   . THR A 1 9   ? 13.60700 24.94500  -2.38100 1.000 77.95228  ? 198 THR B OG1   1 
ATOM   33   C  CG2   . THR A 1 9   ? 12.98900 22.62200  -2.19200 1.000 70.04295  ? 198 THR B CG2   1 
ATOM   34   N  N     . HIS A 1 10  ? 17.20600 24.92000  -2.03300 1.000 55.23799  ? 199 HIS B N     1 
ATOM   35   C  CA    . HIS A 1 10  ? 18.30900 25.64000  -2.62300 1.000 49.43970  ? 199 HIS B CA    1 
ATOM   36   C  C     . HIS A 1 10  ? 19.56700 25.00000  -2.17700 1.000 46.78733  ? 199 HIS B C     1 
ATOM   37   O  O     . HIS A 1 10  ? 20.65600 25.43300  -2.52300 1.000 39.71482  ? 199 HIS B O     1 
ATOM   38   C  CB    . HIS A 1 10  ? 18.30900 27.08500  -2.15500 1.000 51.20157  ? 199 HIS B CB    1 
ATOM   39   C  CG    . HIS A 1 10  ? 18.32000 27.23200  -0.66900 1.000 53.18663  ? 199 HIS B CG    1 
ATOM   40   N  ND1   . HIS A 1 10  ? 17.17500 27.17500  0.09000  1.000 56.81197  ? 199 HIS B ND1   1 
ATOM   41   C  CD2   . HIS A 1 10  ? 19.33900 27.42500  0.19800  1.000 49.79161  ? 199 HIS B CD2   1 
ATOM   42   C  CE1   . HIS A 1 10  ? 17.48600 27.33000  1.36200  1.000 57.28577  ? 199 HIS B CE1   1 
ATOM   43   N  NE2   . HIS A 1 10  ? 18.79300 27.48200  1.45400  1.000 52.43779  ? 199 HIS B NE2   1 
ATOM   44   N  N     . LEU A 1 11  ? 19.42800 23.98300  -1.36300 1.000 46.17458  ? 200 LEU B N     1 
ATOM   45   C  CA    . LEU A 1 11  ? 20.59000 23.23600  -0.99700 1.000 46.59338  ? 200 LEU B CA    1 
ATOM   46   C  C     . LEU A 1 11  ? 20.56900 21.97500  -1.84100 1.000 46.00201  ? 200 LEU B C     1 
ATOM   47   O  O     . LEU A 1 11  ? 19.52300 21.52300  -2.25800 1.000 44.74344  ? 200 LEU B O     1 
ATOM   48   C  CB    . LEU A 1 11  ? 20.59500 22.94700  0.48500  1.000 44.13321  ? 200 LEU B CB    1 
ATOM   49   C  CG    . LEU A 1 11  ? 20.87000 24.16200  1.35400  1.000 51.29661  ? 200 LEU B CG    1 
ATOM   50   C  CD1   . LEU A 1 11  ? 21.19800 23.72900  2.77200  1.000 48.17251  ? 200 LEU B CD1   1 
ATOM   51   C  CD2   . LEU A 1 11  ? 22.02000 24.94500  0.75000  1.000 52.76167  ? 200 LEU B CD2   1 
ATOM   52   N  N     . SER A 1 12  ? 21.72400 21.42100  -2.11100 1.000 45.39351  ? 201 SER B N     1 
ATOM   53   C  CA    . SER A 1 12  ? 21.81600 20.24400  -2.94600 1.000 40.17935  ? 201 SER B CA    1 
ATOM   54   C  C     . SER A 1 12  ? 21.77900 18.99500  -2.14700 1.000 40.24307  ? 201 SER B C     1 
ATOM   55   O  O     . SER A 1 12  ? 22.04800 19.02200  -0.95900 1.000 38.99760  ? 201 SER B O     1 
ATOM   56   C  CB    . SER A 1 12  ? 23.13900 20.24800  -3.68900 1.000 37.70391  ? 201 SER B CB    1 
ATOM   57   O  OG    . SER A 1 12  ? 24.17900 19.73300  -2.89600 1.000 37.54205  ? 201 SER B OG    1 
ATOM   58   N  N     . PHE A 1 13  ? 21.45400 17.89500  -2.79600 1.000 36.56432  ? 202 PHE B N     1 
ATOM   59   C  CA    . PHE A 1 13  ? 21.49900 16.63000  -2.15300 1.000 36.40592  ? 202 PHE B CA    1 
ATOM   60   C  C     . PHE A 1 13  ? 22.84700 16.49900  -1.52500 1.000 38.37749  ? 202 PHE B C     1 
ATOM   61   O  O     . PHE A 1 13  ? 22.93100 16.09900  -0.38400 1.000 36.47197  ? 202 PHE B O     1 
ATOM   62   C  CB    . PHE A 1 13  ? 21.26900 15.52300  -3.18400 1.000 38.57099  ? 202 PHE B CB    1 
ATOM   63   C  CG    . PHE A 1 13  ? 21.51300 14.13900  -2.67900 1.000 39.34660  ? 202 PHE B CG    1 
ATOM   64   C  CD1   . PHE A 1 13  ? 22.78300 13.60000  -2.68500 1.000 42.33393  ? 202 PHE B CD1   1 
ATOM   65   C  CD2   . PHE A 1 13  ? 20.46300 13.36200  -2.24200 1.000 39.56422  ? 202 PHE B CD2   1 
ATOM   66   C  CE1   . PHE A 1 13  ? 23.00700 12.32200  -2.23000 1.000 46.51923  ? 202 PHE B CE1   1 
ATOM   67   C  CE2   . PHE A 1 13  ? 20.67700 12.08100  -1.78700 1.000 45.13741  ? 202 PHE B CE2   1 
ATOM   68   C  CZ    . PHE A 1 13  ? 21.95100 11.56000  -1.78200 1.000 44.56766  ? 202 PHE B CZ    1 
ATOM   69   N  N     . TYR A 1 14  ? 23.91300 16.87700  -2.17900 1.000 37.14954  ? 203 TYR B N     1 
ATOM   70   C  CA    . TYR A 1 14  ? 25.18100 16.67700  -1.52600 1.000 39.52485  ? 203 TYR B CA    1 
ATOM   71   C  C     . TYR A 1 14  ? 25.35100 17.52600  -0.26500 1.000 41.98285  ? 203 TYR B C     1 
ATOM   72   O  O     . TYR A 1 14  ? 25.74200 17.02100  0.76700  1.000 44.75529  ? 203 TYR B O     1 
ATOM   73   C  CB    . TYR A 1 14  ? 26.33400 16.92000  -2.48200 1.000 42.14225  ? 203 TYR B CB    1 
ATOM   74   C  CG    . TYR A 1 14  ? 27.69700 16.54300  -1.96000 1.000 62.18783  ? 203 TYR B CG    1 
ATOM   75   C  CD1   . TYR A 1 14  ? 28.31300 17.28000  -0.95900 1.000 67.80386  ? 203 TYR B CD1   1 
ATOM   76   C  CD2   . TYR A 1 14  ? 28.38300 15.46000  -2.48400 1.000 65.90376  ? 203 TYR B CD2   1 
ATOM   77   C  CE1   . TYR A 1 14  ? 29.56200 16.94200  -0.48200 1.000 68.52373  ? 203 TYR B CE1   1 
ATOM   78   C  CE2   . TYR A 1 14  ? 29.63700 15.11300  -2.01400 1.000 69.47739  ? 203 TYR B CE2   1 
ATOM   79   C  CZ    . TYR A 1 14  ? 30.22100 15.85900  -1.01700 1.000 70.97150  ? 203 TYR B CZ    1 
ATOM   80   O  OH    . TYR A 1 14  ? 31.46700 15.51800  -0.54800 1.000 72.39883  ? 203 TYR B OH    1 
ATOM   81   N  N     . GLU A 1 15  ? 25.05300 18.80000  -0.34200 1.000 37.34571  ? 204 GLU B N     1 
ATOM   82   C  CA    . GLU A 1 15  ? 25.29200 19.66000  0.79300  1.000 46.76117  ? 204 GLU B CA    1 
ATOM   83   C  C     . GLU A 1 15  ? 24.39200 19.34700  1.98200  1.000 37.11430  ? 204 GLU B C     1 
ATOM   84   O  O     . GLU A 1 15  ? 24.82600 19.42700  3.10100  1.000 36.79290  ? 204 GLU B O     1 
ATOM   85   C  CB    . GLU A 1 15  ? 25.20400 21.13000  0.35900  1.000 45.44410  ? 204 GLU B CB    1 
ATOM   86   C  CG    . GLU A 1 15  ? 25.72800 22.12700  1.38700  1.000 55.16438  ? 204 GLU B CG    1 
ATOM   87   C  CD    . GLU A 1 15  ? 27.15600 21.86300  1.85600  1.000 65.41047  ? 204 GLU B CD    1 
ATOM   88   O  OE1   . GLU A 1 15  ? 27.83800 20.98400  1.30500  1.000 63.89635  ? 204 GLU B OE1   1 
ATOM   89   O  OE2   . GLU A 1 15  ? 27.61200 22.55000  2.78900  1.000 55.32849  ? 204 GLU B OE2   1 
ATOM   90   N  N     . LYS A 1 16  ? 23.17200 18.93600  1.71800  1.000 32.99576  ? 205 LYS B N     1 
ATOM   91   C  CA    . LYS A 1 16  ? 22.26100 18.57700  2.78500  1.000 39.20846  ? 205 LYS B CA    1 
ATOM   92   C  C     . LYS A 1 16  ? 22.74700 17.34000  3.52800  1.000 34.80213  ? 205 LYS B C     1 
ATOM   93   O  O     . LYS A 1 16  ? 22.69800 17.29300  4.73500  1.000 30.56368  ? 205 LYS B O     1 
ATOM   94   C  CB    . LYS A 1 16  ? 20.84700 18.41300  2.23400  1.000 36.94030  ? 205 LYS B CB    1 
ATOM   95   C  CG    . LYS A 1 16  ? 20.22200 19.71600  1.78500  1.000 42.08172  ? 205 LYS B CG    1 
ATOM   96   C  CD    . LYS A 1 16  ? 19.15700 19.47800  0.73800  1.000 43.47846  ? 205 LYS B CD    1 
ATOM   97   C  CE    . LYS A 1 16  ? 17.88500 18.95600  1.37100  1.000 47.41792  ? 205 LYS B CE    1 
ATOM   98   N  NZ    . LYS A 1 16  ? 16.68900 19.20500  0.52700  1.000 52.39489  ? 205 LYS B NZ    1 
ATOM   99   N  N     . ARG A 1 17  ? 23.26700 16.37400  2.79700  1.000 33.87687  ? 206 ARG B N     1 
ATOM   100  C  CA    . ARG A 1 17  ? 23.79800 15.17600  3.39400  1.000 38.07653  ? 206 ARG B CA    1 
ATOM   101  C  C     . ARG A 1 17  ? 25.08000 15.50700  4.09900  1.000 36.51940  ? 206 ARG B C     1 
ATOM   102  O  O     . ARG A 1 17  ? 25.34200 15.01700  5.17200  1.000 39.12761  ? 206 ARG B O     1 
ATOM   103  C  CB    . ARG A 1 17  ? 24.02400 14.11000  2.32400  1.000 35.64649  ? 206 ARG B CB    1 
ATOM   104  C  CG    . ARG A 1 17  ? 24.87200 12.93000  2.75500  1.000 43.21624  ? 206 ARG B CG    1 
ATOM   105  C  CD    . ARG A 1 17  ? 24.95300 11.89400  1.64700  1.000 41.33791  ? 206 ARG B CD    1 
ATOM   106  N  NE    . ARG A 1 17  ? 23.70000 11.16000  1.50300  1.000 55.24967  ? 206 ARG B NE    1 
ATOM   107  C  CZ    . ARG A 1 17  ? 23.55400 10.05400  0.78000  1.000 60.50289  ? 206 ARG B CZ    1 
ATOM   108  N  NH1   . ARG A 1 17  ? 24.58400 9.54600   0.12200  1.000 52.07029  ? 206 ARG B NH1   1 
ATOM   109  N  NH2   . ARG A 1 17  ? 22.37400 9.45700   0.71000  1.000 51.52879  ? 206 ARG B NH2   1 
ATOM   110  N  N     . GLU A 1 18  ? 25.86800 16.37200  3.51600  1.000 34.53824  ? 207 GLU B N     1 
ATOM   111  C  CA    . GLU A 1 18  ? 27.06900 16.77400  4.20100  1.000 39.79477  ? 207 GLU B CA    1 
ATOM   112  C  C     . GLU A 1 18  ? 26.78200 17.57400  5.46700  1.000 36.16150  ? 207 GLU B C     1 
ATOM   113  O  O     . GLU A 1 18  ? 27.44800 17.42400  6.47000  1.000 33.07178  ? 207 GLU B O     1 
ATOM   114  C  CB    . GLU A 1 18  ? 27.96000 17.56600  3.24200  1.000 48.10683  ? 207 GLU B CB    1 
ATOM   115  C  CG    . GLU A 1 18  ? 29.29400 17.99400  3.80500  1.000 51.97965  ? 207 GLU B CG    1 
ATOM   116  C  CD    . GLU A 1 18  ? 30.19200 16.82100  4.12700  1.000 65.28253  ? 207 GLU B CD    1 
ATOM   117  O  OE1   . GLU A 1 18  ? 29.89100 15.68900  3.69300  1.000 61.10605  ? 207 GLU B OE1   1 
ATOM   118  O  OE2   . GLU A 1 18  ? 31.20900 17.03900  4.81300  1.000 71.73002  ? 207 GLU B OE2   1 
ATOM   119  N  N     . LEU A 1 19  ? 25.79100 18.43000  5.39900  1.000 31.87856  ? 208 LEU B N     1 
ATOM   120  C  CA    . LEU A 1 19  ? 25.42200 19.21700  6.57300  1.000 32.24827  ? 208 LEU B CA    1 
ATOM   121  C  C     . LEU A 1 19  ? 24.89400 18.33000  7.69400  1.000 37.11353  ? 208 LEU B C     1 
ATOM   122  O  O     . LEU A 1 19  ? 25.22200 18.54000  8.86800  1.000 32.14048  ? 208 LEU B O     1 
ATOM   123  C  CB    . LEU A 1 19  ? 24.38900 20.27800  6.19600  1.000 31.15873  ? 208 LEU B CB    1 
ATOM   124  C  CG    . LEU A 1 19  ? 24.93700 21.51000  5.47400  1.000 39.14266  ? 208 LEU B CG    1 
ATOM   125  C  CD1   . LEU A 1 19  ? 23.81200 22.46500  5.12300  1.000 42.33096  ? 208 LEU B CD1   1 
ATOM   126  C  CD2   . LEU A 1 19  ? 25.98800 22.20200  6.32700  1.000 43.83514  ? 208 LEU B CD2   1 
ATOM   127  N  N     . PHE A 1 20  ? 24.06900 17.33800  7.35500  1.000 35.06588  ? 209 PHE B N     1 
ATOM   128  C  CA    . PHE A 1 20  ? 23.60800 16.39900  8.37100  1.000 34.35224  ? 209 PHE B CA    1 
ATOM   129  C  C     . PHE A 1 20  ? 24.75000 15.53500  8.88600  1.000 35.38724  ? 209 PHE B C     1 
ATOM   130  O  O     . PHE A 1 20  ? 24.77500 15.18400  10.07200 1.000 34.17656  ? 209 PHE B O     1 
ATOM   131  C  CB    . PHE A 1 20  ? 22.48500 15.52500  7.81700  1.000 30.29067  ? 209 PHE B CB    1 
ATOM   132  C  CG    . PHE A 1 20  ? 21.68600 14.82300  8.87700  1.000 33.49166  ? 209 PHE B CG    1 
ATOM   133  C  CD1   . PHE A 1 20  ? 22.05800 13.56800  9.33000  1.000 31.39450  ? 209 PHE B CD1   1 
ATOM   134  C  CD2   . PHE A 1 20  ? 20.56400 15.42200  9.42800  1.000 30.86439  ? 209 PHE B CD2   1 
ATOM   135  C  CE1   . PHE A 1 20  ? 21.32500 12.92300  10.30900 1.000 33.18168  ? 209 PHE B CE1   1 
ATOM   136  C  CE2   . PHE A 1 20  ? 19.82700 14.78200  10.40600 1.000 31.70760  ? 209 PHE B CE2   1 
ATOM   137  C  CZ    . PHE A 1 20  ? 20.20800 13.53200  10.84800 1.000 32.22696  ? 209 PHE B CZ    1 
ATOM   138  N  N     . ARG A 1 21  ? 25.69500 15.17700  8.01300  1.000 32.83133  ? 210 ARG B N     1 
ATOM   139  C  CA    . ARG A 1 21  ? 26.86500 14.42400  8.45200  1.000 36.98037  ? 210 ARG B CA    1 
ATOM   140  C  C     . ARG A 1 21  ? 27.69200 15.22800  9.44800  1.000 37.45123  ? 210 ARG B C     1 
ATOM   141  O  O     . ARG A 1 21  ? 28.13700 14.69400  10.47000 1.000 40.06384  ? 210 ARG B O     1 
ATOM   142  C  CB    . ARG A 1 21  ? 27.71800 14.02900  7.24700  1.000 38.15136  ? 210 ARG B CB    1 
ATOM   143  C  CG    . ARG A 1 21  ? 28.15100 12.57400  7.24500  1.000 49.92052  ? 210 ARG B CG    1 
ATOM   144  C  CD    . ARG A 1 21  ? 27.23300 11.72800  6.38000  1.000 50.84022  ? 210 ARG B CD    1 
ATOM   145  N  NE    . ARG A 1 21  ? 27.46700 11.95700  4.95900  1.000 46.91269  ? 210 ARG B NE    1 
ATOM   146  C  CZ    . ARG A 1 21  ? 28.34300 11.28100  4.22800  1.000 55.04607  ? 210 ARG B CZ    1 
ATOM   147  N  NH1   . ARG A 1 21  ? 29.08300 10.31700  4.75100  1.000 57.41571  ? 210 ARG B NH1   1 
ATOM   148  N  NH2   . ARG A 1 21  ? 28.48000 11.57900  2.93900  1.000 44.96018  ? 210 ARG B NH2   1 
ATOM   149  N  N     . LYS A 1 22  ? 27.90600 16.51700  9.16600  1.000 36.26612  ? 211 LYS B N     1 
ATOM   150  C  CA    . LYS A 1 22  ? 28.62600 17.37300  10.10200 1.000 38.24673  ? 211 LYS B CA    1 
ATOM   151  C  C     . LYS A 1 22  ? 27.85000 17.54300  11.40100 1.000 38.41862  ? 211 LYS B C     1 
ATOM   152  O  O     . LYS A 1 22  ? 28.45400 17.69800  12.46900 1.000 37.54483  ? 211 LYS B O     1 
ATOM   153  C  CB    . LYS A 1 22  ? 28.91300 18.73000  9.45300  1.000 40.68246  ? 211 LYS B CB    1 
ATOM   154  C  CG    . LYS A 1 22  ? 28.80400 19.92200  10.39300 1.000 42.96781  ? 211 LYS B CG    1 
ATOM   155  C  CD    . LYS A 1 22  ? 28.80500 21.24000  9.63400  1.000 49.00431  ? 211 LYS B CD    1 
ATOM   156  C  CE    . LYS A 1 22  ? 30.21200 21.70700  9.30500  1.000 52.93605  ? 211 LYS B CE    1 
ATOM   157  N  NZ    . LYS A 1 22  ? 30.21200 22.67700  8.17400  1.000 53.36872  ? 211 LYS B NZ    1 
ATOM   158  N  N     . LYS A 1 23  ? 26.51700 17.52300  11.33000 1.000 37.40276  ? 212 LYS B N     1 
ATOM   159  C  CA    . LYS A 1 23  ? 25.71100 17.53500  12.54500 1.000 37.25252  ? 212 LYS B CA    1 
ATOM   160  C  C     . LYS A 1 23  ? 25.95700 16.28000  13.37300 1.000 36.64621  ? 212 LYS B C     1 
ATOM   161  O  O     . LYS A 1 23  ? 26.04100 16.34600  14.60500 1.000 36.40209  ? 212 LYS B O     1 
ATOM   162  C  CB    . LYS A 1 23  ? 24.23100 17.66300  12.18900 1.000 32.36110  ? 212 LYS B CB    1 
ATOM   163  C  CG    . LYS A 1 23  ? 23.35300 18.09600  13.34700 1.000 31.50741  ? 212 LYS B CG    1 
ATOM   164  C  CD    . LYS A 1 23  ? 21.92600 17.60700  13.17200 1.000 31.89352  ? 212 LYS B CD    1 
ATOM   165  C  CE    . LYS A 1 23  ? 21.29200 18.19100  11.92300 1.000 31.44143  ? 212 LYS B CE    1 
ATOM   166  N  NZ    . LYS A 1 23  ? 20.28000 19.22800  12.26000 1.000 32.84064  ? 212 LYS B NZ    1 
ATOM   167  N  N     . LEU A 1 24  ? 26.07200 15.12600  12.71100 1.000 32.22978  ? 213 LEU B N     1 
ATOM   168  C  CA    . LEU A 1 24  ? 26.37300 13.88900  13.42400 1.000 35.53475  ? 213 LEU B CA    1 
ATOM   169  C  C     . LEU A 1 24  ? 27.75500 13.94000  14.06200 1.000 36.89191  ? 213 LEU B C     1 
ATOM   170  O  O     . LEU A 1 24  ? 27.95200 13.43900  15.17500 1.000 38.03076  ? 213 LEU B O     1 
ATOM   171  C  CB    . LEU A 1 24  ? 26.26600 12.69300  12.47700 1.000 33.72116  ? 213 LEU B CB    1 
ATOM   172  C  CG    . LEU A 1 24  ? 24.87000 12.35000  11.95200 1.000 32.96308  ? 213 LEU B CG    1 
ATOM   173  C  CD1   . LEU A 1 24  ? 24.91100 11.07000  11.13500 1.000 34.40538  ? 213 LEU B CD1   1 
ATOM   174  C  CD2   . LEU A 1 24  ? 23.88100 12.22600  13.09700 1.000 33.09502  ? 213 LEU B CD2   1 
ATOM   175  N  N     . ARG A 1 25  ? 28.72800 14.53800  13.36800 1.000 36.05421  ? 214 ARG B N     1 
ATOM   176  C  CA    . ARG A 1 25  ? 30.08600 14.59900  13.89900 1.000 42.81287  ? 214 ARG B CA    1 
ATOM   177  C  C     . ARG A 1 25  ? 30.16100 15.43300  15.17300 1.000 45.20793  ? 214 ARG B C     1 
ATOM   178  O  O     . ARG A 1 25  ? 31.04500 15.20900  16.00800 1.000 49.20976  ? 214 ARG B O     1 
ATOM   179  C  CB    . ARG A 1 25  ? 31.04000 15.15100  12.83700 1.000 39.67845  ? 214 ARG B CB    1 
ATOM   180  C  CG    . ARG A 1 25  ? 30.88200 14.48700  11.47500 1.000 43.70802  ? 214 ARG B CG    1 
ATOM   181  C  CD    . ARG A 1 25  ? 32.11900 14.65600  10.60600 1.000 42.32140  ? 214 ARG B CD    1 
ATOM   182  N  NE    . ARG A 1 25  ? 31.92400 15.61800  9.52900  1.000 46.04252  ? 214 ARG B NE    1 
ATOM   183  C  CZ    . ARG A 1 25  ? 31.46300 15.30800  8.32400  1.000 45.34066  ? 214 ARG B CZ    1 
ATOM   184  N  NH1   . ARG A 1 25  ? 31.11500 14.07100  8.01400  1.000 43.34438  ? 214 ARG B NH1   1 
ATOM   185  N  NH2   . ARG A 1 25  ? 31.34900 16.26500  7.40700  1.000 48.39968  ? 214 ARG B NH2   1 
ATOM   186  N  N     . GLU A 1 26  ? 29.24700 16.38900  15.34600 1.000 41.63376  ? 215 GLU B N     1 
ATOM   187  C  CA    . GLU A 1 26  ? 29.24400 17.21700  16.54700 1.000 45.99950  ? 215 GLU B CA    1 
ATOM   188  C  C     . GLU A 1 26  ? 28.75100 16.47600  17.78300 1.000 48.68868  ? 215 GLU B C     1 
ATOM   189  O  O     . GLU A 1 26  ? 28.89500 16.99800  18.89300 1.000 49.07709  ? 215 GLU B O     1 
ATOM   190  C  CB    . GLU A 1 26  ? 28.39100 18.46600  16.32100 1.000 47.98306  ? 215 GLU B CB    1 
ATOM   191  C  CG    . GLU A 1 26  ? 29.20100 19.71400  16.01300 1.000 61.03551  ? 215 GLU B CG    1 
ATOM   192  C  CD    . GLU A 1 26  ? 30.55700 19.70900  16.69500 1.000 70.69827  ? 215 GLU B CD    1 
ATOM   193  O  OE1   . GLU A 1 26  ? 30.60900 19.95100  17.91900 1.000 73.13645  ? 215 GLU B OE1   1 
ATOM   194  O  OE2   . GLU A 1 26  ? 31.56900 19.45200  16.00900 1.000 80.42460  ? 215 GLU B OE2   1 
ATOM   195  N  N     . ILE A 1 27  ? 28.17900 15.28300  17.62300 1.000 42.88093  ? 216 ILE B N     1 
ATOM   196  C  CA    . ILE A 1 27  ? 27.65800 14.54000  18.76300 1.000 43.21688  ? 216 ILE B CA    1 
ATOM   197  C  C     . ILE A 1 27  ? 28.81500 14.01400  19.60100 1.000 45.63656  ? 216 ILE B C     1 
ATOM   198  O  O     . ILE A 1 27  ? 29.76200 13.41400  19.07500 1.000 45.63671  ? 216 ILE B O     1 
ATOM   199  C  CB    . ILE A 1 27  ? 26.75200 13.39500  18.28700 1.000 43.51950  ? 216 ILE B CB    1 
ATOM   200  C  CG1   . ILE A 1 27  ? 25.53200 13.95500  17.55300 1.000 35.96662  ? 216 ILE B CG1   1 
ATOM   201  C  CG2   . ILE A 1 27  ? 26.32300 12.52800  19.46300 1.000 43.15110  ? 216 ILE B CG2   1 
ATOM   202  C  CD1   . ILE A 1 27  ? 25.00500 13.04400  16.46900 1.000 31.94923  ? 216 ILE B CD1   1 
ATOM   203  N  N     . GLU A 1 28  ? 28.74900 14.24300  20.91000 1.000 45.74423  ? 217 GLU B N     1 
ATOM   204  C  CA    . GLU A 1 28  ? 29.75000 13.70800  21.82000 1.000 48.37452  ? 217 GLU B CA    1 
ATOM   205  C  C     . GLU A 1 28  ? 29.46500 12.24100  22.11500 1.000 48.47833  ? 217 GLU B C     1 
ATOM   206  O  O     . GLU A 1 28  ? 28.31600 11.84700  22.33500 1.000 45.87866  ? 217 GLU B O     1 
ATOM   207  C  CB    . GLU A 1 28  ? 29.78500 14.50700  23.12400 1.000 53.77206  ? 217 GLU B CB    1 
ATOM   208  C  CG    . GLU A 1 28  ? 30.32000 15.92400  22.97500 1.000 60.69310  ? 217 GLU B CG    1 
ATOM   209  C  CD    . GLU A 1 28  ? 29.21800 16.96300  22.89000 1.000 73.58362  ? 217 GLU B CD    1 
ATOM   210  O  OE1   . GLU A 1 28  ? 28.28000 16.90800  23.71300 1.000 68.48828  ? 217 GLU B OE1   1 
ATOM   211  O  OE2   . GLU A 1 28  ? 29.29000 17.83500  21.99800 1.000 79.68859  ? 217 GLU B OE2   1 
ATOM   212  N  N     . GLY A 1 29  ? 30.52100 11.43300  22.11700 1.000 43.29275  ? 218 GLY B N     1 
ATOM   213  C  CA    . GLY A 1 29  ? 30.39500 10.01300  22.33600 1.000 37.49409  ? 218 GLY B CA    1 
ATOM   214  C  C     . GLY A 1 29  ? 30.79700 9.22000   21.11000 1.000 41.13586  ? 218 GLY B C     1 
ATOM   215  O  O     . GLY A 1 29  ? 31.45400 9.73400   20.19900 1.000 40.24934  ? 218 GLY B O     1 
ATOM   216  N  N     . PRO A 1 30  ? 30.41300 7.94500   21.06700 1.000 35.85468  ? 219 PRO B N     1 
ATOM   217  C  CA    . PRO A 1 30  ? 30.73300 7.12100   19.89600 1.000 38.39323  ? 219 PRO B CA    1 
ATOM   218  C  C     . PRO A 1 30  ? 30.09000 7.68200   18.63700 1.000 34.01761  ? 219 PRO B C     1 
ATOM   219  O  O     . PRO A 1 30  ? 29.00100 8.26000   18.67000 1.000 33.27110  ? 219 PRO B O     1 
ATOM   220  C  CB    . PRO A 1 30  ? 30.16500 5.74300   20.25900 1.000 34.49628  ? 219 PRO B CB    1 
ATOM   221  C  CG    . PRO A 1 30  ? 29.16400 6.00700   21.33500 1.000 33.60700  ? 219 PRO B CG    1 
ATOM   222  C  CD    . PRO A 1 30  ? 29.67000 7.19400   22.09100 1.000 35.53923  ? 219 PRO B CD    1 
ATOM   223  N  N     . GLU A 1 31  ? 30.78700 7.51000   17.51800 1.000 30.79724  ? 220 GLU B N     1 
ATOM   224  C  CA    . GLU A 1 31  ? 30.38600 8.15000   16.27500 1.000 41.82315  ? 220 GLU B CA    1 
ATOM   225  C  C     . GLU A 1 31  ? 29.05200 7.60600   15.77300 1.000 36.12816  ? 220 GLU B C     1 
ATOM   226  O  O     . GLU A 1 31  ? 28.71300 6.43700   15.97200 1.000 39.25561  ? 220 GLU B O     1 
ATOM   227  C  CB    . GLU A 1 31  ? 31.46000 7.95800   15.20500 1.000 40.95392  ? 220 GLU B CB    1 
ATOM   228  C  CG    . GLU A 1 31  ? 31.58100 6.53600   14.68900 1.000 46.74180  ? 220 GLU B CG    1 
ATOM   229  C  CD    . GLU A 1 31  ? 32.63400 6.40100   13.60800 1.000 64.78673  ? 220 GLU B CD    1 
ATOM   230  O  OE1   . GLU A 1 31  ? 33.12700 7.44200   13.12500 1.000 62.44572  ? 220 GLU B OE1   1 
ATOM   231  O  OE2   . GLU A 1 31  ? 32.96900 5.25400   13.24100 1.000 71.09649  ? 220 GLU B OE2   1 
ATOM   232  N  N     . VAL A 1 32  ? 28.28900 8.48400   15.12700 1.000 35.68810  ? 221 VAL B N     1 
ATOM   233  C  CA    . VAL A 1 32  ? 27.03800 8.13200   14.46800 1.000 33.06835  ? 221 VAL B CA    1 
ATOM   234  C  C     . VAL A 1 32  ? 27.18800 8.44500   12.98800 1.000 31.45112  ? 221 VAL B C     1 
ATOM   235  O  O     . VAL A 1 32  ? 27.59700 9.55400   12.62200 1.000 34.30568  ? 221 VAL B O     1 
ATOM   236  C  CB    . VAL A 1 32  ? 25.84000 8.89000   15.06800 1.000 29.78225  ? 221 VAL B CB    1 
ATOM   237  C  CG1   . VAL A 1 32  ? 24.54300 8.43700   14.41000 1.000 29.44227  ? 221 VAL B CG1   1 
ATOM   238  C  CG2   . VAL A 1 32  ? 25.78100 8.68400   16.57100 1.000 28.27734  ? 221 VAL B CG2   1 
ATOM   239  N  N     . THR A 1 33  ? 26.86300 7.47500   12.14300 1.000 33.70333  ? 222 THR B N     1 
ATOM   240  C  CA    . THR A 1 33  ? 27.01100 7.61100   10.70300 1.000 28.07126  ? 222 THR B CA    1 
ATOM   241  C  C     . THR A 1 33  ? 25.65000 7.58000   10.02100 1.000 30.44840  ? 222 THR B C     1 
ATOM   242  O  O     . THR A 1 33  ? 24.66600 7.06300   10.55800 1.000 28.58799  ? 222 THR B O     1 
ATOM   243  C  CB    . THR A 1 33  ? 27.90700 6.50400   10.13800 1.000 34.32254  ? 222 THR B CB    1 
ATOM   244  O  OG1   . THR A 1 33  ? 27.66800 5.28400   10.85100 1.000 36.68053  ? 222 THR B OG1   1 
ATOM   245  C  CG2   . THR A 1 33  ? 29.37100 6.88500   10.27700 1.000 40.23703  ? 222 THR B CG2   1 
ATOM   246  N  N     . LEU A 1 34  ? 25.60800 8.15400   8.82100  1.000 34.61059  ? 223 LEU B N     1 
ATOM   247  C  CA    . LEU A 1 34  ? 24.39300 8.23700   8.02000  1.000 33.88099  ? 223 LEU B CA    1 
ATOM   248  C  C     . LEU A 1 34  ? 24.67500 7.65100   6.64600  1.000 37.36283  ? 223 LEU B C     1 
ATOM   249  O  O     . LEU A 1 34  ? 25.59400 8.10300   5.95600  1.000 42.19564  ? 223 LEU B O     1 
ATOM   250  C  CB    . LEU A 1 34  ? 23.91800 9.68600   7.89100  1.000 27.44600  ? 223 LEU B CB    1 
ATOM   251  C  CG    . LEU A 1 34  ? 22.65800 9.93200   7.06000  1.000 30.91471  ? 223 LEU B CG    1 
ATOM   252  C  CD1   . LEU A 1 34  ? 21.41000 9.58700   7.85800  1.000 31.52783  ? 223 LEU B CD1   1 
ATOM   253  C  CD2   . LEU A 1 34  ? 22.61500 11.37100  6.57500  1.000 28.39236  ? 223 LEU B CD2   1 
ATOM   254  N  N     . VAL A 1 35  ? 23.89300 6.64700   6.25200  1.000 38.09487  ? 224 VAL B N     1 
ATOM   255  C  CA    . VAL A 1 35  ? 23.96900 6.08200   4.91200  1.000 45.87185  ? 224 VAL B CA    1 
ATOM   256  C  C     . VAL A 1 35  ? 22.56000 5.98400   4.34500  1.000 38.46068  ? 224 VAL B C     1 
ATOM   257  O  O     . VAL A 1 35  ? 21.57800 5.85900   5.08400  1.000 31.51703  ? 224 VAL B O     1 
ATOM   258  C  CB    . VAL A 1 35  ? 24.65800 4.69500   4.88700  1.000 43.00391  ? 224 VAL B CB    1 
ATOM   259  C  CG1   . VAL A 1 35  ? 25.91100 4.69000   5.75200  1.000 37.96370  ? 224 VAL B CG1   1 
ATOM   260  C  CG2   . VAL A 1 35  ? 23.69300 3.60200   5.32000  1.000 39.92652  ? 224 VAL B CG2   1 
ATOM   261  N  N     . ASN A 1 36  ? 22.46500 6.04900   3.01700  1.000 40.93288  ? 225 ASN B N     1 
ATOM   262  C  CA    . ASN A 1 36  ? 21.18600 5.87200   2.33200  1.000 43.44297  ? 225 ASN B CA    1 
ATOM   263  C  C     . ASN A 1 36  ? 21.48000 5.23100   0.98100  1.000 37.42645  ? 225 ASN B C     1 
ATOM   264  O  O     . ASN A 1 36  ? 21.78700 5.93000   0.01000  1.000 38.80276  ? 225 ASN B O     1 
ATOM   265  C  CB    . ASN A 1 36  ? 20.44600 7.19400   2.17900  1.000 40.41589  ? 225 ASN B CB    1 
ATOM   266  C  CG    . ASN A 1 36  ? 19.01300 7.01000   1.70200  1.000 38.05239  ? 225 ASN B CG    1 
ATOM   267  O  OD1   . ASN A 1 36  ? 18.65300 5.96300   1.16100  1.000 38.27666  ? 225 ASN B OD1   1 
ATOM   268  N  ND2   . ASN A 1 36  ? 18.18900 8.03300   1.89700  1.000 41.26310  ? 225 ASN B ND2   1 
ATOM   269  N  N     . GLU A 1 37  ? 21.38100 3.90400   0.92700  1.000 41.31534  ? 226 GLU B N     1 
ATOM   270  C  CA    . GLU A 1 37  ? 21.53500 3.14900   -0.30700 1.000 47.85704  ? 226 GLU B CA    1 
ATOM   271  C  C     . GLU A 1 37  ? 20.19800 2.61500   -0.80600 1.000 43.08207  ? 226 GLU B C     1 
ATOM   272  O  O     . GLU A 1 37  ? 20.15800 1.61700   -1.53200 1.000 42.64265  ? 226 GLU B O     1 
ATOM   273  C  CB    . GLU A 1 37  ? 22.53100 2.00700   -0.10100 1.000 40.91846  ? 226 GLU B CB    1 
ATOM   274  C  CG    . GLU A 1 37  ? 23.82900 2.44000   0.56900  1.000 44.18171  ? 226 GLU B CG    1 
ATOM   275  C  CD    . GLU A 1 37  ? 24.61400 1.27300   1.14200  1.000 61.05269  ? 226 GLU B CD    1 
ATOM   276  O  OE1   . GLU A 1 37  ? 24.01900 0.45900   1.87900  1.000 57.10227  ? 226 GLU B OE1   1 
ATOM   277  O  OE2   . GLU A 1 37  ? 25.82700 1.17300   0.85900  1.000 61.28688  ? 226 GLU B OE2   1 
ATOM   278  N  N     . VAL A 1 38  ? 19.09900 3.27100   -0.42900 1.000 44.34176  ? 227 VAL B N     1 
ATOM   279  C  CA    . VAL A 1 38  ? 17.75000 2.76600   -0.64300 1.000 41.29007  ? 227 VAL B CA    1 
ATOM   280  C  C     . VAL A 1 38  ? 16.93000 3.70800   -1.52300 1.000 40.74721  ? 227 VAL B C     1 
ATOM   281  O  O     . VAL A 1 38  ? 16.32600 3.27900   -2.50900 1.000 42.86420  ? 227 VAL B O     1 
ATOM   282  C  CB    . VAL A 1 38  ? 17.03200 2.50500   0.70000  1.000 40.13971  ? 227 VAL B CB    1 
ATOM   283  C  CG1   . VAL A 1 38  ? 15.55000 2.35000   0.49500  1.000 37.51600  ? 227 VAL B CG1   1 
ATOM   284  C  CG2   . VAL A 1 38  ? 17.60100 1.25800   1.35800  1.000 43.49651  ? 227 VAL B CG2   1 
ATOM   285  N  N     . ASP A 1 39  ? 16.90000 4.99300   -1.17900 1.000 39.56539  ? 228 ASP B N     1 
ATOM   286  C  CA    . ASP A 1 39  ? 16.19000 5.98700   -1.98100 1.000 42.38508  ? 228 ASP B CA    1 
ATOM   287  C  C     . ASP A 1 39  ? 17.07200 7.22600   -2.10500 1.000 40.87778  ? 228 ASP B C     1 
ATOM   288  O  O     . ASP A 1 39  ? 18.24700 7.21900   -1.72500 1.000 40.26042  ? 228 ASP B O     1 
ATOM   289  C  CB    . ASP A 1 39  ? 14.80700 6.29600   -1.38600 1.000 39.50127  ? 228 ASP B CB    1 
ATOM   290  C  CG    . ASP A 1 39  ? 14.87000 6.77800   0.05600  1.000 46.81564  ? 228 ASP B CG    1 
ATOM   291  O  OD1   . ASP A 1 39  ? 15.96400 7.14000   0.53800  1.000 47.28503  ? 228 ASP B OD1   1 
ATOM   292  O  OD2   . ASP A 1 39  ? 13.80800 6.79000   0.71400  1.000 50.00257  ? 228 ASP B OD2   1 
ATOM   293  N  N     . ASP A 1 40  ? 16.49900 8.30400   -2.63900 1.000 43.79865  ? 229 ASP B N     1 
ATOM   294  C  CA    . ASP A 1 40  ? 17.24600 9.51600   -2.94200 1.000 53.64590  ? 229 ASP B CA    1 
ATOM   295  C  C     . ASP A 1 40  ? 17.10900 10.59100  -1.86900 1.000 42.43116  ? 229 ASP B C     1 
ATOM   296  O  O     . ASP A 1 40  ? 17.58600 11.71200  -2.07100 1.000 48.25200  ? 229 ASP B O     1 
ATOM   297  C  CB    . ASP A 1 40  ? 16.81300 10.07600  -4.30000 1.000 49.38303  ? 229 ASP B CB    1 
ATOM   298  C  CG    . ASP A 1 40  ? 15.31100 10.26500  -4.40500 1.000 57.40005  ? 229 ASP B CG    1 
ATOM   299  O  OD1   . ASP A 1 40  ? 14.59000 9.86500   -3.46700 1.000 57.41053  ? 229 ASP B OD1   1 
ATOM   300  O  OD2   . ASP A 1 40  ? 14.85000 10.81400  -5.42900 1.000 66.09978  ? 229 ASP B OD2   1 
ATOM   301  N  N     . GLU A 1 41  ? 16.47600 10.28400  -0.74500 1.000 38.23475  ? 230 GLU B N     1 
ATOM   302  C  CA    . GLU A 1 41  ? 16.36700 11.26000  0.33400  1.000 42.12864  ? 230 GLU B CA    1 
ATOM   303  C  C     . GLU A 1 41  ? 17.74900 11.52000  0.91900  1.000 42.76223  ? 230 GLU B C     1 
ATOM   304  O  O     . GLU A 1 41  ? 18.42200 10.57000  1.33900  1.000 41.61114  ? 230 GLU B O     1 
ATOM   305  C  CB    . GLU A 1 41  ? 15.41100 10.76400  1.41500  1.000 41.27604  ? 230 GLU B CB    1 
ATOM   306  C  CG    . GLU A 1 41  ? 15.17100 11.76500  2.53600  1.000 42.98126  ? 230 GLU B CG    1 
ATOM   307  C  CD    . GLU A 1 41  ? 14.19100 11.25600  3.57800  1.000 45.13789  ? 230 GLU B CD    1 
ATOM   308  O  OE1   . GLU A 1 41  ? 13.69500 10.11900  3.42600  1.000 45.80605  ? 230 GLU B OE1   1 
ATOM   309  O  OE2   . GLU A 1 41  ? 13.91700 11.99400  4.54900  1.000 43.52678  ? 230 GLU B OE2   1 
ATOM   310  N  N     . PRO A 1 42  ? 18.21200 12.77300  0.96700  1.000 39.92018  ? 231 PRO B N     1 
ATOM   311  C  CA    . PRO A 1 42  ? 19.60400 13.00900  1.38700  1.000 38.21083  ? 231 PRO B CA    1 
ATOM   312  C  C     . PRO A 1 42  ? 19.85200 12.72400  2.85600  1.000 35.43348  ? 231 PRO B C     1 
ATOM   313  O  O     . PRO A 1 42  ? 20.89500 12.15600  3.20100  1.000 37.09366  ? 231 PRO B O     1 
ATOM   314  C  CB    . PRO A 1 42  ? 19.82000 14.49000  1.04700  1.000 43.65821  ? 231 PRO B CB    1 
ATOM   315  C  CG    . PRO A 1 42  ? 18.45100 15.08800  1.10600  1.000 46.76769  ? 231 PRO B CG    1 
ATOM   316  C  CD    . PRO A 1 42  ? 17.51400 14.02000  0.61300  1.000 42.10347  ? 231 PRO B CD    1 
ATOM   317  N  N     . CYS A 1 43  ? 18.91900 13.09300  3.73000  1.000 36.76059  ? 232 CYS B N     1 
ATOM   318  C  CA    . CYS A 1 43  ? 19.11300 12.96500  5.16800  1.000 32.26530  ? 232 CYS B CA    1 
ATOM   319  C  C     . CYS A 1 43  ? 17.79900 13.22400  5.89300  1.000 30.66949  ? 232 CYS B C     1 
ATOM   320  O  O     . CYS A 1 43  ? 16.81800 13.64200  5.26400  1.000 33.22251  ? 232 CYS B O     1 
ATOM   321  C  CB    . CYS A 1 43  ? 20.19200 13.94000  5.64400  1.000 32.52006  ? 232 CYS B CB    1 
ATOM   322  S  SG    . CYS A 1 43  ? 19.88900 15.66600  5.20300  1.000 34.14709  ? 232 CYS B SG    1 
ATOM   323  N  N     . PRO A 1 44  ? 17.72700 12.98200  7.20900  1.000 31.29523  ? 233 PRO B N     1 
ATOM   324  C  CA    . PRO A 1 44  ? 16.55700 13.44200  7.96900  1.000 34.38632  ? 233 PRO B CA    1 
ATOM   325  C  C     . PRO A 1 44  ? 16.50600 14.96100  8.05000  1.000 35.14688  ? 233 PRO B C     1 
ATOM   326  O  O     . PRO A 1 44  ? 17.33800 15.64500  7.44400  1.000 26.67055  ? 233 PRO B O     1 
ATOM   327  C  CB    . PRO A 1 44  ? 16.76100 12.80600  9.35100  1.000 30.69584  ? 233 PRO B CB    1 
ATOM   328  C  CG    . PRO A 1 44  ? 17.64000 11.63000  9.09900  1.000 31.58719  ? 233 PRO B CG    1 
ATOM   329  C  CD    . PRO A 1 44  ? 18.56000 12.05400  7.99500  1.000 29.97260  ? 233 PRO B CD    1 
ATOM   330  N  N     . SER A 1 45  ? 15.53300 15.49600  8.78500  1.000 32.41711  ? 234 SER B N     1 
ATOM   331  C  CA    . SER A 1 45  ? 15.33900 16.94000  8.84400  1.000 34.43523  ? 234 SER B CA    1 
ATOM   332  C  C     . SER A 1 45  ? 16.60300 17.64600  9.31900  1.000 32.93849  ? 234 SER B C     1 
ATOM   333  O  O     . SER A 1 45  ? 17.18400 17.28700  10.34800 1.000 32.17418  ? 234 SER B O     1 
ATOM   334  C  CB    . SER A 1 45  ? 14.17100 17.27300  9.77200  1.000 34.38176  ? 234 SER B CB    1 
ATOM   335  O  OG    . SER A 1 45  ? 14.10200 18.66500  10.02800 1.000 31.37243  ? 234 SER B OG    1 
ATOM   336  N  N     . LEU A 1 46  ? 17.02700 18.65800  8.55900  1.000 33.67101  ? 235 LEU B N     1 
ATOM   337  C  CA    . LEU A 1 46  ? 18.18800 19.45700  8.93200  1.000 38.68880  ? 235 LEU B CA    1 
ATOM   338  C  C     . LEU A 1 46  ? 17.91500 20.37000  10.11700 1.000 33.04168  ? 235 LEU B C     1 
ATOM   339  O  O     . LEU A 1 46  ? 18.86700 20.90000  10.70100 1.000 33.49058  ? 235 LEU B O     1 
ATOM   340  C  CB    . LEU A 1 46  ? 18.66200 20.29300  7.74000  1.000 44.66957  ? 235 LEU B CB    1 
ATOM   341  C  CG    . LEU A 1 46  ? 19.39200 19.55100  6.61900  1.000 41.83517  ? 235 LEU B CG    1 
ATOM   342  C  CD1   . LEU A 1 46  ? 19.60700 20.46500  5.42400  1.000 45.63106  ? 235 LEU B CD1   1 
ATOM   343  C  CD2   . LEU A 1 46  ? 20.71800 19.00500  7.12200  1.000 36.60069  ? 235 LEU B CD2   1 
ATOM   344  N  N     . ASP A 1 47  ? 16.64900 20.57000  10.48200 1.000 31.29535  ? 236 ASP B N     1 
ATOM   345  C  CA    . ASP A 1 47  ? 16.31000 21.40400  11.62600 1.000 36.30722  ? 236 ASP B CA    1 
ATOM   346  C  C     . ASP A 1 47  ? 16.40200 20.65900  12.95100 1.000 30.13565  ? 236 ASP B C     1 
ATOM   347  O  O     . ASP A 1 47  ? 16.35200 21.30000  14.00600 1.000 31.94987  ? 236 ASP B O     1 
ATOM   348  C  CB    . ASP A 1 47  ? 14.90200 21.98000  11.44900 1.000 34.27071  ? 236 ASP B CB    1 
ATOM   349  C  CG    . ASP A 1 47  ? 14.63300 23.15300  12.37000 1.000 41.06260  ? 236 ASP B CG    1 
ATOM   350  O  OD1   . ASP A 1 47  ? 15.32600 24.18400  12.23800 1.000 39.83412  ? 236 ASP B OD1   1 
ATOM   351  O  OD2   . ASP A 1 47  ? 13.72800 23.04500  13.22400 1.000 43.38800  ? 236 ASP B OD2   1 
ATOM   352  N  N     . PHE A 1 48  ? 16.54000 19.33400  12.92400 1.000 25.19062  ? 237 PHE B N     1 
ATOM   353  C  CA    . PHE A 1 48  ? 16.61300 18.55900  14.15500 1.000 27.79986  ? 237 PHE B CA    1 
ATOM   354  C  C     . PHE A 1 48  ? 17.89800 18.86800  14.91500 1.000 23.29672  ? 237 PHE B C     1 
ATOM   355  O  O     . PHE A 1 48  ? 18.95500 19.09000  14.31800 1.000 25.25820  ? 237 PHE B O     1 
ATOM   356  C  CB    . PHE A 1 48  ? 16.52800 17.06500  13.84400 1.000 23.57279  ? 237 PHE B CB    1 
ATOM   357  C  CG    . PHE A 1 48  ? 16.78500 16.18300  15.03200 1.000 26.77263  ? 237 PHE B CG    1 
ATOM   358  C  CD1   . PHE A 1 48  ? 15.81900 16.01800  16.01100 1.000 25.43611  ? 237 PHE B CD1   1 
ATOM   359  C  CD2   . PHE A 1 48  ? 17.99000 15.51300  15.16600 1.000 24.37343  ? 237 PHE B CD2   1 
ATOM   360  C  CE1   . PHE A 1 48  ? 16.05400 15.20700  17.10500 1.000 23.44732  ? 237 PHE B CE1   1 
ATOM   361  C  CE2   . PHE A 1 48  ? 18.22900 14.70000  16.25800 1.000 26.75166  ? 237 PHE B CE2   1 
ATOM   362  C  CZ    . PHE A 1 48  ? 17.26000 14.54700  17.22700 1.000 25.12510  ? 237 PHE B CZ    1 
ATOM   363  N  N     . GLN A 1 49  ? 17.80100 18.88300  16.24400 1.000 23.90435  ? 238 GLN B N     1 
ATOM   364  C  CA    . GLN A 1 49  ? 18.92900 19.16800  17.12100 1.000 23.54121  ? 238 GLN B CA    1 
ATOM   365  C  C     . GLN A 1 49  ? 19.19300 17.97200  18.02400 1.000 23.07039  ? 238 GLN B C     1 
ATOM   366  O  O     . GLN A 1 49  ? 18.28400 17.49800  18.71300 1.000 22.05303  ? 238 GLN B O     1 
ATOM   367  C  CB    . GLN A 1 49  ? 18.66700 20.40900  17.97800 1.000 23.02878  ? 238 GLN B CB    1 
ATOM   368  C  CG    . GLN A 1 49  ? 18.41300 21.68100  17.19800 1.000 22.51099  ? 238 GLN B CG    1 
ATOM   369  C  CD    . GLN A 1 49  ? 18.12400 22.86000  18.10600 1.000 29.69328  ? 238 GLN B CD    1 
ATOM   370  O  OE1   . GLN A 1 49  ? 17.03400 23.43200  18.07400 1.000 23.67772  ? 238 GLN B OE1   1 
ATOM   371  N  NE2   . GLN A 1 49  ? 19.10300 23.22900  18.92600 1.000 27.58781  ? 238 GLN B NE2   1 
ATOM   372  N  N     . PHE A 1 50  ? 20.43600 17.49800  18.02900 1.000 20.79201  ? 239 PHE B N     1 
ATOM   373  C  CA    . PHE A 1 50  ? 20.83900 16.43800  18.94000 1.000 21.18833  ? 239 PHE B CA    1 
ATOM   374  C  C     . PHE A 1 50  ? 21.15100 17.01200  20.31600 1.000 24.66964  ? 239 PHE B C     1 
ATOM   375  O  O     . PHE A 1 50  ? 21.79500 18.05800  20.43800 1.000 25.68940  ? 239 PHE B O     1 
ATOM   376  C  CB    . PHE A 1 50  ? 22.05400 15.69100  18.39100 1.000 22.23007  ? 239 PHE B CB    1 
ATOM   377  C  CG    . PHE A 1 50  ? 21.74500 14.82500  17.20400 1.000 30.26953  ? 239 PHE B CG    1 
ATOM   378  C  CD1   . PHE A 1 50  ? 21.19000 13.56600  17.37100 1.000 28.94607  ? 239 PHE B CD1   1 
ATOM   379  C  CD2   . PHE A 1 50  ? 22.01500 15.26900  15.91900 1.000 26.23220  ? 239 PHE B CD2   1 
ATOM   380  C  CE1   . PHE A 1 50  ? 20.90900 12.76800  16.27800 1.000 22.76130  ? 239 PHE B CE1   1 
ATOM   381  C  CE2   . PHE A 1 50  ? 21.73400 14.47400  14.82200 1.000 24.03421  ? 239 PHE B CE2   1 
ATOM   382  C  CZ    . PHE A 1 50  ? 21.18200 13.22300  15.00200 1.000 23.67348  ? 239 PHE B CZ    1 
ATOM   383  N  N     . ILE A 1 51  ? 20.68700 16.31900  21.35700 1.000 25.42954  ? 240 ILE B N     1 
ATOM   384  C  CA    . ILE A 1 51  ? 20.85600 16.75900  22.73400 1.000 25.30682  ? 240 ILE B CA    1 
ATOM   385  C  C     . ILE A 1 51  ? 21.39100 15.60200  23.56800 1.000 20.49088  ? 240 ILE B C     1 
ATOM   386  O  O     . ILE A 1 51  ? 21.28600 14.43200  23.19500 1.000 23.02596  ? 240 ILE B O     1 
ATOM   387  C  CB    . ILE A 1 51  ? 19.53900 17.29000  23.34100 1.000 21.16821  ? 240 ILE B CB    1 
ATOM   388  C  CG1   . ILE A 1 51  ? 18.45000 16.21800  23.26700 1.000 28.13137  ? 240 ILE B CG1   1 
ATOM   389  C  CG2   . ILE A 1 51  ? 19.09700 18.56100  22.63200 1.000 28.19214  ? 240 ILE B CG2   1 
ATOM   390  C  CD1   . ILE A 1 51  ? 17.10000 16.68000  23.77100 1.000 26.50726  ? 240 ILE B CD1   1 
ATOM   391  N  N     . SER A 1 52  ? 21.97800 15.95100  24.71300 1.000 24.46043  ? 241 SER B N     1 
ATOM   392  C  CA    . SER A 1 52  ? 22.49500 14.96900  25.65500 1.000 24.83330  ? 241 SER B CA    1 
ATOM   393  C  C     . SER A 1 52  ? 21.66900 14.86200  26.92900 1.000 24.08544  ? 241 SER B C     1 
ATOM   394  O  O     . SER A 1 52  ? 21.95000 13.98800  27.75600 1.000 30.55404  ? 241 SER B O     1 
ATOM   395  C  CB    . SER A 1 52  ? 23.95100 15.29500  26.02400 1.000 23.18901  ? 241 SER B CB    1 
ATOM   396  O  OG    . SER A 1 52  ? 24.04800 16.53900  26.69500 1.000 20.38041  ? 241 SER B OG    1 
ATOM   397  N  N     . GLN A 1 53  ? 20.67100 15.72400  27.11400 1.000 24.33538  ? 242 GLN B N     1 
ATOM   398  C  CA    . GLN A 1 53  ? 19.79000 15.65200  28.27100 1.000 25.55022  ? 242 GLN B CA    1 
ATOM   399  C  C     . GLN A 1 53  ? 18.42000 16.18300  27.87200 1.000 25.23636  ? 242 GLN B C     1 
ATOM   400  O  O     . GLN A 1 53  ? 18.24500 16.76600  26.79900 1.000 24.00626  ? 242 GLN B O     1 
ATOM   401  C  CB    . GLN A 1 53  ? 20.36200 16.42800  29.46300 1.000 34.44379  ? 242 GLN B CB    1 
ATOM   402  C  CG    . GLN A 1 53  ? 20.64700 17.89200  29.17700 1.000 33.59222  ? 242 GLN B CG    1 
ATOM   403  C  CD    . GLN A 1 53  ? 21.20600 18.62100  30.38400 1.000 49.57844  ? 242 GLN B CD    1 
ATOM   404  O  OE1   . GLN A 1 53  ? 20.49200 19.35800  31.06400 1.000 60.32433  ? 242 GLN B OE1   1 
ATOM   405  N  NE2   . GLN A 1 53  ? 22.49200 18.42200  30.65200 1.000 47.95561  ? 242 GLN B NE2   1 
ATOM   406  N  N     . TYR A 1 54  ? 17.44600 15.97700  28.75700 1.000 20.89471  ? 243 TYR B N     1 
ATOM   407  C  CA    . TYR A 1 54  ? 16.07400 16.38100  28.47900 1.000 26.48010  ? 243 TYR B CA    1 
ATOM   408  C  C     . TYR A 1 54  ? 15.97800 17.88700  28.25700 1.000 26.14940  ? 243 TYR B C     1 
ATOM   409  O  O     . TYR A 1 54  ? 16.69600 18.67900  28.87300 1.000 27.78360  ? 243 TYR B O     1 
ATOM   410  C  CB    . TYR A 1 54  ? 15.15400 15.97100  29.63000 1.000 20.76822  ? 243 TYR B CB    1 
ATOM   411  C  CG    . TYR A 1 54  ? 14.72900 14.52100  29.60400 1.000 24.22447  ? 243 TYR B CG    1 
ATOM   412  C  CD1   . TYR A 1 54  ? 14.38900 13.89500  28.41200 1.000 25.15632  ? 243 TYR B CD1   1 
ATOM   413  C  CD2   . TYR A 1 54  ? 14.66700 13.77700  30.77400 1.000 20.41239  ? 243 TYR B CD2   1 
ATOM   414  C  CE1   . TYR A 1 54  ? 13.99700 12.56800  28.38800 1.000 24.27714  ? 243 TYR B CE1   1 
ATOM   415  C  CE2   . TYR A 1 54  ? 14.27800 12.45200  30.76100 1.000 23.72450  ? 243 TYR B CE2   1 
ATOM   416  C  CZ    . TYR A 1 54  ? 13.94500 11.85300  29.56700 1.000 26.06682  ? 243 TYR B CZ    1 
ATOM   417  O  OH    . TYR A 1 54  ? 13.55900 10.53200  29.55700 1.000 29.32099  ? 243 TYR B OH    1 
ATOM   418  N  N     . ARG A 1 55  ? 15.07800 18.27700  27.35800 1.000 28.77526  ? 244 ARG B N     1 
ATOM   419  C  CA    . ARG A 1 55  ? 14.81300 19.67700  27.03000 1.000 30.20782  ? 244 ARG B CA    1 
ATOM   420  C  C     . ARG A 1 55  ? 13.48200 20.05800  27.67700 1.000 32.32489  ? 244 ARG B C     1 
ATOM   421  O  O     . ARG A 1 55  ? 12.42000 19.93400  27.06500 1.000 37.22234  ? 244 ARG B O     1 
ATOM   422  C  CB    . ARG A 1 55  ? 14.78700 19.88400  25.51400 1.000 28.33796  ? 244 ARG B CB    1 
ATOM   423  C  CG    . ARG A 1 55  ? 14.82900 21.33700  25.06100 1.000 27.33404  ? 244 ARG B CG    1 
ATOM   424  C  CD    . ARG A 1 55  ? 15.94300 22.09400  25.76500 1.000 37.87536  ? 244 ARG B CD    1 
ATOM   425  N  NE    . ARG A 1 55  ? 16.69300 22.95700  24.86100 1.000 33.83657  ? 244 ARG B NE    1 
ATOM   426  C  CZ    . ARG A 1 55  ? 16.29700 24.16000  24.46600 1.000 27.89396  ? 244 ARG B CZ    1 
ATOM   427  N  NH1   . ARG A 1 55  ? 15.13500 24.66400  24.84700 1.000 33.87119  ? 244 ARG B NH1   1 
ATOM   428  N  NH2   . ARG A 1 55  ? 17.08500 24.87300  23.66700 1.000 26.27653  ? 244 ARG B NH2   1 
ATOM   429  N  N     . LEU A 1 56  ? 13.54600 20.52500  28.92200 1.000 31.20926  ? 245 LEU B N     1 
ATOM   430  C  CA    . LEU A 1 56  ? 12.33400 20.89100  29.64300 1.000 34.21939  ? 245 LEU B CA    1 
ATOM   431  C  C     . LEU A 1 56  ? 11.66800 22.11000  29.00700 1.000 33.13814  ? 245 LEU B C     1 
ATOM   432  O  O     . LEU A 1 56  ? 12.32700 22.98500  28.43800 1.000 36.77733  ? 245 LEU B O     1 
ATOM   433  C  CB    . LEU A 1 56  ? 12.64900 21.17000  31.11500 1.000 32.73853  ? 245 LEU B CB    1 
ATOM   434  C  CG    . LEU A 1 56  ? 13.30500 20.04400  31.91900 1.000 35.24278  ? 245 LEU B CG    1 
ATOM   435  C  CD1   . LEU A 1 56  ? 13.29200 20.37500  33.40500 1.000 32.33702  ? 245 LEU B CD1   1 
ATOM   436  C  CD2   . LEU A 1 56  ? 12.62100 18.71100  31.65900 1.000 26.17754  ? 245 LEU B CD2   1 
ATOM   437  N  N     . THR A 1 57  ? 10.34200 22.15000  29.10000 1.000 31.14018  ? 246 THR B N     1 
ATOM   438  C  CA    . THR A 1 57  ? 9.52600  23.24000  28.58500 1.000 32.94715  ? 246 THR B CA    1 
ATOM   439  C  C     . THR A 1 57  ? 8.74200  23.86300  29.73800 1.000 38.93721  ? 246 THR B C     1 
ATOM   440  O  O     . THR A 1 57  ? 8.92200  23.50800  30.90700 1.000 41.30987  ? 246 THR B O     1 
ATOM   441  C  CB    . THR A 1 57  ? 8.58200  22.75100  27.48000 1.000 35.88971  ? 246 THR B CB    1 
ATOM   442  O  OG1   . THR A 1 57  ? 7.73500  21.71100  27.98900 1.000 34.64657  ? 246 THR B OG1   1 
ATOM   443  C  CG2   . THR A 1 57  ? 9.37400  22.21600  26.29200 1.000 32.42118  ? 246 THR B CG2   1 
ATOM   444  N  N     . GLN A 1 58  ? 7.86900  24.81100  29.40100 1.000 42.52256  ? 247 GLN B N     1 
ATOM   445  C  CA    . GLN A 1 58  ? 7.06300  25.46900  30.42100 1.000 48.95996  ? 247 GLN B CA    1 
ATOM   446  C  C     . GLN A 1 58  ? 5.98800  24.52200  30.94500 1.000 42.33120  ? 247 GLN B C     1 
ATOM   447  O  O     . GLN A 1 58  ? 5.42500  23.71600  30.19700 1.000 45.67970  ? 247 GLN B O     1 
ATOM   448  C  CB    . GLN A 1 58  ? 6.41900  26.73400  29.85900 1.000 40.85020  ? 247 GLN B CB    1 
ATOM   449  C  CG    . GLN A 1 58  ? 6.25800  27.84500  30.87600 1.000 47.35080  ? 247 GLN B CG    1 
ATOM   450  C  CD    . GLN A 1 58  ? 7.58600  28.43500  31.30300 1.000 52.42992  ? 247 GLN B CD    1 
ATOM   451  O  OE1   . GLN A 1 58  ? 8.49500  28.60400  30.49100 1.000 52.08377  ? 247 GLN B OE1   1 
ATOM   452  N  NE2   . GLN A 1 58  ? 7.70900  28.74300  32.58500 1.000 61.13256  ? 247 GLN B NE2   1 
ATOM   453  N  N     . GLY A 1 59  ? 5.70500  24.61800  32.24300 1.000 36.97406  ? 248 GLY B N     1 
ATOM   454  C  CA    . GLY A 1 59  ? 4.71700  23.77000  32.87100 1.000 40.31214  ? 248 GLY B CA    1 
ATOM   455  C  C     . GLY A 1 59  ? 5.23500  22.44200  33.37200 1.000 39.45256  ? 248 GLY B C     1 
ATOM   456  O  O     . GLY A 1 59  ? 4.48300  21.71600  34.03100 1.000 41.22547  ? 248 GLY B O     1 
ATOM   457  N  N     . VAL A 1 60  ? 6.49000  22.10500  33.09600 1.000 33.55867  ? 249 VAL B N     1 
ATOM   458  C  CA    . VAL A 1 60  ? 7.08300  20.84900  33.53900 1.000 35.27320  ? 249 VAL B CA    1 
ATOM   459  C  C     . VAL A 1 60  ? 7.88000  21.13200  34.80600 1.000 38.79835  ? 249 VAL B C     1 
ATOM   460  O  O     . VAL A 1 60  ? 8.94200  21.76200  34.76000 1.000 43.24010  ? 249 VAL B O     1 
ATOM   461  C  CB    . VAL A 1 60  ? 7.96200  20.22000  32.45100 1.000 37.24293  ? 249 VAL B CB    1 
ATOM   462  C  CG1   . VAL A 1 60  ? 8.71900  19.02600  33.00900 1.000 33.97601  ? 249 VAL B CG1   1 
ATOM   463  C  CG2   . VAL A 1 60  ? 7.11000  19.80100  31.26100 1.000 31.01582  ? 249 VAL B CG2   1 
ATOM   464  N  N     . ILE A 1 61  ? 7.37000  20.66400  35.93900 1.000 40.30350  ? 250 ILE B N     1 
ATOM   465  C  CA    . ILE A 1 61  ? 8.02400  20.86900  37.22800 1.000 43.87247  ? 250 ILE B CA    1 
ATOM   466  C  C     . ILE A 1 61  ? 9.20800  19.91600  37.34500 1.000 44.81421  ? 250 ILE B C     1 
ATOM   467  O  O     . ILE A 1 61  ? 9.02700  18.69200  37.27000 1.000 47.26683  ? 250 ILE B O     1 
ATOM   468  C  CB    . ILE A 1 61  ? 7.03400  20.67200  38.38600 1.000 50.57775  ? 250 ILE B CB    1 
ATOM   469  C  CG1   . ILE A 1 61  ? 5.90700  21.70400  38.29700 1.000 47.74891  ? 250 ILE B CG1   1 
ATOM   470  C  CG2   . ILE A 1 61  ? 7.75500  20.75400  39.72700 1.000 54.79706  ? 250 ILE B CG2   1 
ATOM   471  C  CD1   . ILE A 1 61  ? 4.53100  21.12900  38.54700 1.000 49.56748  ? 250 ILE B CD1   1 
ATOM   472  N  N     . PRO A 1 62  ? 10.42400 20.42100  37.52800 1.000 46.16851  ? 251 PRO B N     1 
ATOM   473  C  CA    . PRO A 1 62  ? 11.58000 19.53800  37.68500 1.000 41.14114  ? 251 PRO B CA    1 
ATOM   474  C  C     . PRO A 1 62  ? 11.66300 19.01400  39.10600 1.000 42.42997  ? 251 PRO B C     1 
ATOM   475  O  O     . PRO A 1 62  ? 11.02900 19.57000  40.01700 1.000 41.54192  ? 251 PRO B O     1 
ATOM   476  C  CB    . PRO A 1 62  ? 12.77400 20.45100  37.35200 1.000 41.18969  ? 251 PRO B CB    1 
ATOM   477  C  CG    . PRO A 1 62  ? 12.20100 21.84300  37.14900 1.000 45.34498  ? 251 PRO B CG    1 
ATOM   478  C  CD    . PRO A 1 62  ? 10.80000 21.83500  37.66500 1.000 47.28508  ? 251 PRO B CD    1 
ATOM   479  N  N     . PRO A 1 63  ? 12.41500 17.93900  39.33800 1.000 41.79576  ? 252 PRO B N     1 
ATOM   480  C  CA    . PRO A 1 63  ? 12.56100 17.43000  40.70800 1.000 40.86564  ? 252 PRO B CA    1 
ATOM   481  C  C     . PRO A 1 63  ? 13.23900 18.45100  41.61100 1.000 41.91031  ? 252 PRO B C     1 
ATOM   482  O  O     . PRO A 1 63  ? 14.15300 19.16600  41.19700 1.000 43.34794  ? 252 PRO B O     1 
ATOM   483  C  CB    . PRO A 1 63  ? 13.41800 16.17200  40.53100 1.000 43.39006  ? 252 PRO B CB    1 
ATOM   484  C  CG    . PRO A 1 63  ? 14.13000 16.37400  39.22900 1.000 41.89774  ? 252 PRO B CG    1 
ATOM   485  C  CD    . PRO A 1 63  ? 13.17300 17.13400  38.36400 1.000 41.73602  ? 252 PRO B CD    1 
ATOM   486  N  N     . ASP A 1 64  ? 12.77900 18.51100  42.85500 1.000 43.44299  ? 253 ASP B N     1 
ATOM   487  C  CA    . ASP A 1 64  ? 13.34300 19.43800  43.82900 1.000 41.40214  ? 253 ASP B CA    1 
ATOM   488  C  C     . ASP A 1 64  ? 14.64500 18.87200  44.37500 1.000 43.87270  ? 253 ASP B C     1 
ATOM   489  O  O     . ASP A 1 64  ? 14.64800 17.75500  44.91100 1.000 48.57405  ? 253 ASP B O     1 
ATOM   490  C  CB    . ASP A 1 64  ? 12.35100 19.68200  44.96200 1.000 43.98814  ? 253 ASP B CB    1 
ATOM   491  C  CG    . ASP A 1 64  ? 12.67100 20.93100  45.76800 1.000 48.83356  ? 253 ASP B CG    1 
ATOM   492  O  OD1   . ASP A 1 64  ? 13.86600 21.24000  45.96100 1.000 48.72739  ? 253 ASP B OD1   1 
ATOM   493  O  OD2   . ASP A 1 64  ? 11.71900 21.60500  46.21400 1.000 43.36900  ? 253 ASP B OD2   1 
ATOM   494  N  N     . PRO A 1 65  ? 15.76900 19.58500  44.26100 1.000 44.51551  ? 254 PRO B N     1 
ATOM   495  C  CA    . PRO A 1 65  ? 17.02700 19.06900  44.82300 1.000 45.91238  ? 254 PRO B CA    1 
ATOM   496  C  C     . PRO A 1 65  ? 17.00700 18.92900  46.33500 1.000 39.84828  ? 254 PRO B C     1 
ATOM   497  O  O     . PRO A 1 65  ? 17.82900 18.18500  46.88300 1.000 41.23699  ? 254 PRO B O     1 
ATOM   498  C  CB    . PRO A 1 65  ? 18.06800 20.10200  44.36700 1.000 48.96828  ? 254 PRO B CB    1 
ATOM   499  C  CG    . PRO A 1 65  ? 17.28100 21.34400  44.10200 1.000 48.16543  ? 254 PRO B CG    1 
ATOM   500  C  CD    . PRO A 1 65  ? 15.95600 20.87700  43.57800 1.000 46.59202  ? 254 PRO B CD    1 
ATOM   501  N  N     . ASN A 1 66  ? 16.10100 19.62100  47.02800 1.000 41.63524  ? 255 ASN B N     1 
ATOM   502  C  CA    . ASN A 1 66  ? 16.00400 19.49700  48.47600 1.000 48.17548  ? 255 ASN B CA    1 
ATOM   503  C  C     . ASN A 1 66  ? 15.39300 18.17400  48.91700 1.000 35.81237  ? 255 ASN B C     1 
ATOM   504  O  O     . ASN A 1 66  ? 15.46800 17.84300  50.10500 1.000 37.53739  ? 255 ASN B O     1 
ATOM   505  C  CB    . ASN A 1 66  ? 15.19400 20.66300  49.04400 1.000 39.42552  ? 255 ASN B CB    1 
ATOM   506  C  CG    . ASN A 1 66  ? 15.87900 22.00000  48.83600 1.000 46.47123  ? 255 ASN B CG    1 
ATOM   507  O  OD1   . ASN A 1 66  ? 17.10800 22.08600  48.84200 1.000 43.95876  ? 255 ASN B OD1   1 
ATOM   508  N  ND2   . ASN A 1 66  ? 15.08800 23.05000  48.64700 1.000 40.17607  ? 255 ASN B ND2   1 
ATOM   509  N  N     . PHE A 1 67  ? 14.79100 17.41900  48.00100 1.000 43.60293  ? 256 PHE B N     1 
ATOM   510  C  CA    . PHE A 1 67  ? 14.26500 16.09200  48.29200 1.000 50.59808  ? 256 PHE B CA    1 
ATOM   511  C  C     . PHE A 1 67  ? 15.23900 14.97300  47.94400 1.000 48.96963  ? 256 PHE B C     1 
ATOM   512  O  O     . PHE A 1 67  ? 14.91200 13.80100  48.15000 1.000 53.10751  ? 256 PHE B O     1 
ATOM   513  C  CB    . PHE A 1 67  ? 12.95100 15.87100  47.53500 1.000 46.94298  ? 256 PHE B CB    1 
ATOM   514  C  CG    . PHE A 1 67  ? 11.73600 16.41100  48.23400 1.000 53.97205  ? 256 PHE B CG    1 
ATOM   515  C  CD1   . PHE A 1 67  ? 11.35900 15.93100  49.47700 1.000 53.50358  ? 256 PHE B CD1   1 
ATOM   516  C  CD2   . PHE A 1 67  ? 10.96400 17.39600  47.63900 1.000 50.32784  ? 256 PHE B CD2   1 
ATOM   517  C  CE1   . PHE A 1 67  ? 10.23600 16.42700  50.11300 1.000 54.09329  ? 256 PHE B CE1   1 
ATOM   518  C  CE2   . PHE A 1 67  ? 9.84200  17.89600  48.27300 1.000 60.21129  ? 256 PHE B CE2   1 
ATOM   519  C  CZ    . PHE A 1 67  ? 9.47700  17.41000  49.51100 1.000 60.69736  ? 256 PHE B CZ    1 
ATOM   520  N  N     . GLN A 1 68  ? 16.42500 15.30100  47.43400 1.000 43.46980  ? 257 GLN B N     1 
ATOM   521  C  CA    . GLN A 1 68  ? 17.32400 14.31100  46.85200 1.000 46.79986  ? 257 GLN B CA    1 
ATOM   522  C  C     . GLN A 1 68  ? 18.28800 13.75000  47.88900 1.000 42.63950  ? 257 GLN B C     1 
ATOM   523  O  O     . GLN A 1 68  ? 18.83900 14.48900  48.71000 1.000 48.50781  ? 257 GLN B O     1 
ATOM   524  C  CB    . GLN A 1 68  ? 18.11200 14.92800  45.69500 1.000 48.52386  ? 257 GLN B CB    1 
ATOM   525  C  CG    . GLN A 1 68  ? 19.13500 13.99900  45.06100 1.000 46.88401  ? 257 GLN B CG    1 
ATOM   526  C  CD    . GLN A 1 68  ? 18.49900 12.89400  44.23900 1.000 56.18496  ? 257 GLN B CD    1 
ATOM   527  O  OE1   . GLN A 1 68  ? 18.55500 12.90500  43.00800 1.000 55.97678  ? 257 GLN B OE1   1 
ATOM   528  N  NE2   . GLN A 1 68  ? 17.88800 11.93200  44.91900 1.000 57.35430  ? 257 GLN B NE2   1 
ATOM   529  N  N     . SER A 1 69  ? 18.50500 12.43600  47.83100 1.000 47.74224  ? 258 SER B N     1 
ATOM   530  C  CA    . SER A 1 69  ? 19.41000 11.74000  48.73400 1.000 49.68845  ? 258 SER B CA    1 
ATOM   531  C  C     . SER A 1 69  ? 20.40300 10.90700  47.93400 1.000 42.07016  ? 258 SER B C     1 
ATOM   532  O  O     . SER A 1 69  ? 20.14500 10.52000  46.79200 1.000 40.98689  ? 258 SER B O     1 
ATOM   533  C  CB    . SER A 1 69  ? 18.64700 10.83400  49.71100 1.000 45.00694  ? 258 SER B CB    1 
ATOM   534  O  OG    . SER A 1 69  ? 18.38700 11.50200  50.93100 1.000 50.05996  ? 258 SER B OG    1 
ATOM   535  N  N     . GLY A 1 70  ? 21.54900 10.63600  48.55400 1.000 43.13905  ? 259 GLY B N     1 
ATOM   536  C  CA    . GLY A 1 70  ? 22.56600 9.79900   47.94600 1.000 46.01438  ? 259 GLY B CA    1 
ATOM   537  C  C     . GLY A 1 70  ? 22.93300 8.60600   48.80600 1.000 47.11148  ? 259 GLY B C     1 
ATOM   538  O  O     . GLY A 1 70  ? 22.26200 8.32800   49.80400 1.000 49.42711  ? 259 GLY B O     1 
ATOM   539  N  N     . CYS A 1 71  ? 23.99300 7.89200   48.43500 1.000 49.70117  ? 260 CYS B N     1 
ATOM   540  C  CA    . CYS A 1 71  ? 24.46600 6.74400   49.19300 1.000 53.14972  ? 260 CYS B CA    1 
ATOM   541  C  C     . CYS A 1 71  ? 25.81100 7.05400   49.83900 1.000 52.96110  ? 260 CYS B C     1 
ATOM   542  O  O     . CYS A 1 71  ? 26.56000 7.92500   49.38700 1.000 56.44580  ? 260 CYS B O     1 
ATOM   543  C  CB    . CYS A 1 71  ? 24.58100 5.49900   48.30300 1.000 44.73225  ? 260 CYS B CB    1 
ATOM   544  S  SG    . CYS A 1 71  ? 25.76600 5.62900   46.94200 1.000 41.95507  ? 260 CYS B SG    1 
ATOM   545  N  N     . ASN A 1 72  ? 26.09600 6.31100   50.89000 1.000 50.85616  ? 261 ASN B N     1 
ATOM   546  C  CA    . ASN A 1 72  ? 27.30200 6.51700   51.64600 1.000 63.77048  ? 261 ASN B CA    1 
ATOM   547  C  C     . ASN A 1 72  ? 28.18700 5.34100   51.37300 1.000 66.58306  ? 261 ASN B C     1 
ATOM   548  O  O     . ASN A 1 72  ? 28.35100 4.47600   52.22800 1.000 72.18586  ? 261 ASN B O     1 
ATOM   549  C  CB    . ASN A 1 72  ? 26.92800 6.57200   53.12200 1.000 61.91979  ? 261 ASN B CB    1 
ATOM   550  C  CG    . ASN A 1 72  ? 25.76500 7.50900   53.40100 1.000 68.85996  ? 261 ASN B CG    1 
ATOM   551  O  OD1   . ASN A 1 72  ? 24.70100 7.40000   52.79600 1.000 65.30736  ? 261 ASN B OD1   1 
ATOM   552  N  ND2   . ASN A 1 72  ? 25.96600 8.43700   54.32700 1.000 71.29459  ? 261 ASN B ND2   1 
ATOM   553  N  N     . CYS A 1 73  ? 28.76500 5.29000   50.19500 1.000 63.35912  ? 262 CYS B N     1 
ATOM   554  C  CA    . CYS A 1 73  ? 29.54800 4.11400   49.77300 1.000 65.96390  ? 262 CYS B CA    1 
ATOM   555  C  C     . CYS A 1 73  ? 31.01300 4.51900   49.70300 1.000 72.60330  ? 262 CYS B C     1 
ATOM   556  O  O     . CYS A 1 73  ? 31.79800 3.90900   48.99900 1.000 72.91581  ? 262 CYS B O     1 
ATOM   557  C  CB    . CYS A 1 73  ? 29.00100 3.47900   48.48800 1.000 56.60077  ? 262 CYS B CB    1 
ATOM   558  S  SG    . CYS A 1 73  ? 27.41600 2.65700   48.71100 1.000 52.13263  ? 262 CYS B SG    1 
ATOM   559  N  N     . SER A 1 74  ? 31.36700 5.57200   50.41600 1.000 74.63341  ? 263 SER B N     1 
ATOM   560  C  CA    . SER A 1 74  ? 32.76100 6.00600   50.47500 1.000 78.94017  ? 263 SER B CA    1 
ATOM   561  C  C     . SER A 1 74  ? 33.30600 6.40400   49.09500 1.000 79.03287  ? 263 SER B C     1 
ATOM   562  O  O     . SER A 1 74  ? 34.51700 6.43500   48.86600 1.000 76.49578  ? 263 SER B O     1 
ATOM   563  C  CB    . SER A 1 74  ? 33.61900 4.92300   51.13400 1.000 76.64028  ? 263 SER B CB    1 
ATOM   564  O  OG    . SER A 1 74  ? 33.08000 4.53500   52.38200 1.000 74.70210  ? 263 SER B OG    1 
ATOM   565  N  N     . GLY A 1 78  ? 33.53900 2.80400   43.11900 1.000 58.16990  ? 267 GLY B N     1 
ATOM   566  C  CA    . GLY A 1 78  ? 32.43000 3.45100   43.78900 1.000 55.68626  ? 267 GLY B CA    1 
ATOM   567  C  C     . GLY A 1 78  ? 31.68400 2.47900   44.65100 1.000 59.70759  ? 267 GLY B C     1 
ATOM   568  O  O     . GLY A 1 78  ? 32.24100 1.93000   45.59700 1.000 59.29088  ? 267 GLY B O     1 
ATOM   569  N  N     . CYS A 1 79  ? 30.41000 2.27200   44.35500 1.000 56.42823  ? 268 CYS B N     1 
ATOM   570  C  CA    . CYS A 1 79  ? 29.70700 1.23400   45.08800 1.000 47.76502  ? 268 CYS B CA    1 
ATOM   571  C  C     . CYS A 1 79  ? 30.26200 -0.14500  44.74100 1.000 41.76057  ? 268 CYS B C     1 
ATOM   572  O  O     . CYS A 1 79  ? 30.86200 -0.35900  43.68400 1.000 42.67516  ? 268 CYS B O     1 
ATOM   573  C  CB    . CYS A 1 79  ? 28.21200 1.29300   44.78800 1.000 44.98826  ? 268 CYS B CB    1 
ATOM   574  S  SG    . CYS A 1 79  ? 27.50000 2.92700   45.04700 1.000 35.38400  ? 268 CYS B SG    1 
ATOM   575  N  N     . ASP A 1 80  ? 30.05600 -1.08600  45.65600 1.000 44.13326  ? 269 ASP B N     1 
ATOM   576  C  CA    . ASP A 1 80  ? 30.54100 -2.45000  45.49700 1.000 50.83281  ? 269 ASP B CA    1 
ATOM   577  C  C     . ASP A 1 80  ? 29.40500 -3.33800  45.01000 1.000 45.33689  ? 269 ASP B C     1 
ATOM   578  O  O     . ASP A 1 80  ? 28.32400 -3.36000  45.60800 1.000 42.69373  ? 269 ASP B O     1 
ATOM   579  C  CB    . ASP A 1 80  ? 31.11600 -2.97900  46.81200 1.000 53.88577  ? 269 ASP B CB    1 
ATOM   580  C  CG    . ASP A 1 80  ? 31.72500 -4.36100  46.67000 1.000 55.81051  ? 269 ASP B CG    1 
ATOM   581  O  OD1   . ASP A 1 80  ? 30.96300 -5.33800  46.51900 1.000 57.85676  ? 269 ASP B OD1   1 
ATOM   582  O  OD2   . ASP A 1 80  ? 32.97000 -4.46900  46.69900 1.000 62.48198  ? 269 ASP B OD2   1 
ATOM   583  N  N     . LEU A 1 81  ? 29.65600 -4.06500  43.91900 1.000 43.85993  ? 270 LEU B N     1 
ATOM   584  C  CA    . LEU A 1 81  ? 28.61800 -4.90300  43.32800 1.000 46.24960  ? 270 LEU B CA    1 
ATOM   585  C  C     . LEU A 1 81  ? 28.34800 -6.14700  44.16400 1.000 45.74646  ? 270 LEU B C     1 
ATOM   586  O  O     . LEU A 1 81  ? 27.21800 -6.64900  44.17800 1.000 40.13783  ? 270 LEU B O     1 
ATOM   587  C  CB    . LEU A 1 81  ? 29.01900 -5.29300  41.90600 1.000 41.46218  ? 270 LEU B CB    1 
ATOM   588  C  CG    . LEU A 1 81  ? 27.90200 -5.40400  40.87100 1.000 40.45374  ? 270 LEU B CG    1 
ATOM   589  C  CD1   . LEU A 1 81  ? 27.18000 -4.07500  40.71700 1.000 29.06618  ? 270 LEU B CD1   1 
ATOM   590  C  CD2   . LEU A 1 81  ? 28.47900 -5.85300  39.54700 1.000 36.06272  ? 270 LEU B CD2   1 
ATOM   591  N  N     . ASN A 1 82  ? 29.36300 -6.66100  44.86000 1.000 43.20215  ? 271 ASN B N     1 
ATOM   592  C  CA    . ASN A 1 82  ? 29.20200 -7.85700  45.67800 1.000 51.14177  ? 271 ASN B CA    1 
ATOM   593  C  C     . ASN A 1 82  ? 28.58700 -7.56800  47.04200 1.000 52.54963  ? 271 ASN B C     1 
ATOM   594  O  O     . ASN A 1 82  ? 28.28300 -8.51300  47.77700 1.000 58.68479  ? 271 ASN B O     1 
ATOM   595  C  CB    . ASN A 1 82  ? 30.55400 -8.55200  45.86300 1.000 55.05897  ? 271 ASN B CB    1 
ATOM   596  C  CG    . ASN A 1 82  ? 31.28400 -8.76900  44.54900 1.000 54.46245  ? 271 ASN B CG    1 
ATOM   597  O  OD1   . ASN A 1 82  ? 30.66500 -8.90700  43.49500 1.000 56.23323  ? 271 ASN B OD1   1 
ATOM   598  N  ND2   . ASN A 1 82  ? 32.61100 -8.80000  44.60900 1.000 62.28349  ? 271 ASN B ND2   1 
ATOM   599  N  N     . ASN A 1 83  ? 28.41700 -6.29100  47.36300 1.000 50.46380  ? 272 ASN B N     1 
ATOM   600  C  CA    . ASN A 1 83  ? 27.72300 -5.91300  48.57600 1.000 54.61374  ? 272 ASN B CA    1 
ATOM   601  C  C     . ASN A 1 83  ? 26.69500 -4.86100  48.31800 1.000 49.08936  ? 272 ASN B C     1 
ATOM   602  O  O     . ASN A 1 83  ? 26.90400 -3.70200  48.61500 1.000 52.84370  ? 272 ASN B O     1 
ATOM   603  C  CB    . ASN A 1 83  ? 28.65900 -5.34700  49.60100 1.000 64.99572  ? 272 ASN B CB    1 
ATOM   604  N  N     . PRO A 1 84  ? 25.55600 -5.27100  47.78600 1.000 48.82923  ? 273 PRO B N     1 
ATOM   605  C  CA    . PRO A 1 84  ? 24.49000 -4.30500  47.48100 1.000 43.09407  ? 273 PRO B CA    1 
ATOM   606  C  C     . PRO A 1 84  ? 23.71200 -3.82700  48.69500 1.000 48.94733  ? 273 PRO B C     1 
ATOM   607  O  O     . PRO A 1 84  ? 22.92600 -2.87800  48.56700 1.000 48.17405  ? 273 PRO B O     1 
ATOM   608  C  CB    . PRO A 1 84  ? 23.58200 -5.08900  46.52700 1.000 39.84891  ? 273 PRO B CB    1 
ATOM   609  C  CG    . PRO A 1 84  ? 23.76200 -6.50600  46.94400 1.000 36.75331  ? 273 PRO B CG    1 
ATOM   610  C  CD    . PRO A 1 84  ? 25.19700 -6.63900  47.37300 1.000 43.42465  ? 273 PRO B CD    1 
ATOM   611  N  N     . SER A 1 85  ? 23.89600 -4.45100  49.86100 1.000 45.86346  ? 274 SER B N     1 
ATOM   612  C  CA    . SER A 1 85  ? 23.12500 -4.06600  51.03900 1.000 51.70760  ? 274 SER B CA    1 
ATOM   613  C  C     . SER A 1 85  ? 23.51200 -2.68300  51.54900 1.000 51.97245  ? 274 SER B C     1 
ATOM   614  O  O     . SER A 1 85  ? 22.65200 -1.94500  52.04300 1.000 50.73262  ? 274 SER B O     1 
ATOM   615  C  CB    . SER A 1 85  ? 23.30900 -5.10600  52.14500 1.000 57.37868  ? 274 SER B CB    1 
ATOM   616  O  OG    . SER A 1 85  ? 23.01900 -6.41000  51.67200 1.000 61.72874  ? 274 SER B OG    1 
ATOM   617  N  N     . ARG A 1 86  ? 24.79200 -2.31700  51.44200 1.000 61.10608  ? 275 ARG B N     1 
ATOM   618  C  CA    . ARG A 1 86  ? 25.26100 -1.06200  52.02200 1.000 59.02140  ? 275 ARG B CA    1 
ATOM   619  C  C     . ARG A 1 86  ? 24.71900 0.15600   51.28000 1.000 56.84971  ? 275 ARG B C     1 
ATOM   620  O  O     . ARG A 1 86  ? 24.52000 1.21100   51.89200 1.000 48.26650  ? 275 ARG B O     1 
ATOM   621  C  CB    . ARG A 1 86  ? 26.79100 -1.03900  52.04100 1.000 66.62597  ? 275 ARG B CB    1 
ATOM   622  C  CG    . ARG A 1 86  ? 27.43200 -1.55800  50.76100 1.000 72.63109  ? 275 ARG B CG    1 
ATOM   623  C  CD    . ARG A 1 86  ? 28.95000 -1.63600  50.85500 1.000 82.88431  ? 275 ARG B CD    1 
ATOM   624  N  NE    . ARG A 1 86  ? 29.42500 -2.93600  51.31800 1.000 91.40880  ? 275 ARG B NE    1 
ATOM   625  C  CZ    . ARG A 1 86  ? 30.65900 -3.38600  51.14200 1.000 88.11088  ? 275 ARG B CZ    1 
ATOM   626  N  NH1   . ARG A 1 86  ? 31.56900 -2.67400  50.49800 1.000 90.76054  ? 275 ARG B NH1   1 
ATOM   627  N  NH2   . ARG A 1 86  ? 30.98700 -4.58500  51.61600 1.000 89.36713  ? 275 ARG B NH2   1 
ATOM   628  N  N     . CYS A 1 87  ? 24.47500 0.03700   49.97700 1.000 48.11893  ? 276 CYS B N     1 
ATOM   629  C  CA    . CYS A 1 87  ? 24.07800 1.18600   49.17200 1.000 52.50181  ? 276 CYS B CA    1 
ATOM   630  C  C     . CYS A 1 87  ? 22.62100 1.55300   49.43100 1.000 44.36052  ? 276 CYS B C     1 
ATOM   631  O  O     . CYS A 1 87  ? 21.73000 0.70200   49.34200 1.000 43.72503  ? 276 CYS B O     1 
ATOM   632  C  CB    . CYS A 1 87  ? 24.29400 0.88800   47.68900 1.000 41.34566  ? 276 CYS B CB    1 
ATOM   633  S  SG    . CYS A 1 87  ? 24.07100 2.31300   46.60800 1.000 29.92720  ? 276 CYS B SG    1 
ATOM   634  N  N     . GLU A 1 88  ? 22.37900 2.83100   49.73500 1.000 38.82787  ? 277 GLU B N     1 
ATOM   635  C  CA    . GLU A 1 88  ? 21.03200 3.31200   50.02000 1.000 47.92592  ? 277 GLU B CA    1 
ATOM   636  C  C     . GLU A 1 88  ? 20.22100 3.61400   48.76700 1.000 44.51866  ? 277 GLU B C     1 
ATOM   637  O  O     . GLU A 1 88  ? 19.00800 3.83000   48.87500 1.000 33.72676  ? 277 GLU B O     1 
ATOM   638  C  CB    . GLU A 1 88  ? 21.08600 4.56900   50.89400 1.000 47.39699  ? 277 GLU B CB    1 
ATOM   639  C  CG    . GLU A 1 88  ? 21.38600 4.31300   52.36300 1.000 49.90469  ? 277 GLU B CG    1 
ATOM   640  C  CD    . GLU A 1 88  ? 22.83400 4.58500   52.72600 1.000 58.99585  ? 277 GLU B CD    1 
ATOM   641  O  OE1   . GLU A 1 88  ? 23.67100 4.67100   51.80100 1.000 57.78855  ? 277 GLU B OE1   1 
ATOM   642  O  OE2   . GLU A 1 88  ? 23.13600 4.70600   53.93100 1.000 58.20510  ? 277 GLU B OE2   1 
ATOM   643  N  N     . CYS A 1 89  ? 20.84800 3.64300   47.58900 1.000 34.46142  ? 278 CYS B N     1 
ATOM   644  C  CA    . CYS A 1 89  ? 20.11100 3.89200   46.35700 1.000 36.39566  ? 278 CYS B CA    1 
ATOM   645  C  C     . CYS A 1 89  ? 19.22100 2.72500   45.95700 1.000 38.79879  ? 278 CYS B C     1 
ATOM   646  O  O     . CYS A 1 89  ? 18.36200 2.89400   45.08500 1.000 44.40045  ? 278 CYS B O     1 
ATOM   647  C  CB    . CYS A 1 89  ? 21.08000 4.20800   45.21600 1.000 36.32709  ? 278 CYS B CB    1 
ATOM   648  S  SG    . CYS A 1 89  ? 22.13300 5.64600   45.51000 1.000 28.98665  ? 278 CYS B SG    1 
ATOM   649  N  N     . LEU A 1 90  ? 19.40100 1.55400   46.57000 1.000 42.88511  ? 279 LEU B N     1 
ATOM   650  C  CA    . LEU A 1 90  ? 18.63800 0.35900   46.23500 1.000 40.55583  ? 279 LEU B CA    1 
ATOM   651  C  C     . LEU A 1 90  ? 17.59000 0.02400   47.29300 1.000 40.73349  ? 279 LEU B C     1 
ATOM   652  O  O     . LEU A 1 90  ? 17.14300 -1.12400  47.37400 1.000 45.25040  ? 279 LEU B O     1 
ATOM   653  C  CB    . LEU A 1 90  ? 19.58200 -0.82700  46.03500 1.000 39.44356  ? 279 LEU B CB    1 
ATOM   654  C  CG    . LEU A 1 90  ? 20.74800 -0.62800  45.06400 1.000 39.29293  ? 279 LEU B CG    1 
ATOM   655  C  CD1   . LEU A 1 90  ? 21.65900 -1.84800  45.06600 1.000 36.16060  ? 279 LEU B CD1   1 
ATOM   656  C  CD2   . LEU A 1 90  ? 20.24200 -0.33400  43.66100 1.000 31.04158  ? 279 LEU B CD2   1 
ATOM   657  N  N     . ASP A 1 91  ? 17.19300 1.00400   48.11000 1.000 49.26751  ? 280 ASP B N     1 
ATOM   658  C  CA    . ASP A 1 91  ? 16.24800 0.72700   49.18700 1.000 58.31379  ? 280 ASP B CA    1 
ATOM   659  C  C     . ASP A 1 91  ? 14.84000 0.46400   48.66300 1.000 55.24720  ? 280 ASP B C     1 
ATOM   660  O  O     . ASP A 1 91  ? 14.07100 -0.26000  49.30500 1.000 48.58074  ? 280 ASP B O     1 
ATOM   661  C  CB    . ASP A 1 91  ? 16.23700 1.88300   50.18700 1.000 65.19070  ? 280 ASP B CB    1 
ATOM   662  C  CG    . ASP A 1 91  ? 17.44800 1.87200   51.10100 1.000 69.95778  ? 280 ASP B CG    1 
ATOM   663  O  OD1   . ASP A 1 91  ? 17.90500 0.76900   51.47100 1.000 70.18566  ? 280 ASP B OD1   1 
ATOM   664  O  OD2   . ASP A 1 91  ? 17.94100 2.96600   51.45100 1.000 66.86100  ? 280 ASP B OD2   1 
ATOM   665  N  N     . ASP A 1 92  ? 14.48300 1.03600   47.51100 1.000 42.95681  ? 281 ASP B N     1 
ATOM   666  C  CA    . ASP A 1 92  ? 13.17000 0.78600   46.92800 1.000 44.41204  ? 281 ASP B CA    1 
ATOM   667  C  C     . ASP A 1 92  ? 13.02000 -0.63200  46.39400 1.000 51.72566  ? 281 ASP B C     1 
ATOM   668  O  O     . ASP A 1 92  ? 11.89900 -1.03800  46.06900 1.000 50.63463  ? 281 ASP B O     1 
ATOM   669  C  CB    . ASP A 1 92  ? 12.88800 1.78400   45.80300 1.000 52.09743  ? 281 ASP B CB    1 
ATOM   670  C  CG    . ASP A 1 92  ? 12.60400 3.18100   46.31800 1.000 52.03019  ? 281 ASP B CG    1 
ATOM   671  O  OD1   . ASP A 1 92  ? 12.69600 3.39700   47.54500 1.000 60.98334  ? 281 ASP B OD1   1 
ATOM   672  O  OD2   . ASP A 1 92  ? 12.28600 4.06300   45.49200 1.000 60.28479  ? 281 ASP B OD2   1 
ATOM   673  N  N     . LEU A 1 93  ? 14.11100 -1.38700  46.29500 1.000 51.10017  ? 282 LEU B N     1 
ATOM   674  C  CA    . LEU A 1 93  ? 14.07000 -2.74600  45.77800 1.000 44.78174  ? 282 LEU B CA    1 
ATOM   675  C  C     . LEU A 1 93  ? 13.75000 -3.73400  46.89000 1.000 50.78762  ? 282 LEU B C     1 
ATOM   676  O  O     . LEU A 1 93  ? 14.16300 -3.55500  48.04000 1.000 50.91556  ? 282 LEU B O     1 
ATOM   677  C  CB    . LEU A 1 93  ? 15.40400 -3.11200  45.12700 1.000 42.96222  ? 282 LEU B CB    1 
ATOM   678  C  CG    . LEU A 1 93  ? 15.78800 -2.33600  43.86800 1.000 35.96485  ? 282 LEU B CG    1 
ATOM   679  C  CD1   . LEU A 1 93  ? 17.29600 -2.33300  43.69000 1.000 37.89383  ? 282 LEU B CD1   1 
ATOM   680  C  CD2   . LEU A 1 93  ? 15.10700 -2.92900  42.64500 1.000 35.47109  ? 282 LEU B CD2   1 
ATOM   681  N  N     . ASP A 1 94  ? 13.00600 -4.77800  46.54000 1.000 49.93323  ? 283 ASP B N     1 
ATOM   682  C  CA    . ASP A 1 94  ? 12.72100 -5.85200  47.47300 1.000 57.89207  ? 283 ASP B CA    1 
ATOM   683  C  C     . ASP A 1 94  ? 13.91600 -6.79500  47.57100 1.000 51.44975  ? 283 ASP B C     1 
ATOM   684  O  O     . ASP A 1 94  ? 14.76800 -6.85600  46.67900 1.000 53.38005  ? 283 ASP B O     1 
ATOM   685  C  CB    . ASP A 1 94  ? 11.47900 -6.62900  47.03600 1.000 60.37695  ? 283 ASP B CB    1 
ATOM   686  C  CG    . ASP A 1 94  ? 10.37500 -5.72400  46.52800 1.000 72.03806  ? 283 ASP B CG    1 
ATOM   687  O  OD1   . ASP A 1 94  ? 10.11800 -4.67800  47.16200 1.000 80.02107  ? 283 ASP B OD1   1 
ATOM   688  O  OD2   . ASP A 1 94  ? 9.76900  -6.05600  45.48600 1.000 73.26012  ? 283 ASP B OD2   1 
ATOM   689  N  N     . GLU A 1 95  ? 13.97500 -7.53300  48.67400 1.000 44.97781  ? 284 GLU B N     1 
ATOM   690  C  CA    . GLU A 1 95  ? 14.99600 -8.55500  48.81300 1.000 45.46355  ? 284 GLU B CA    1 
ATOM   691  C  C     . GLU A 1 95  ? 14.72700 -9.69700  47.83200 1.000 43.53652  ? 284 GLU B C     1 
ATOM   692  O  O     . GLU A 1 95  ? 13.57100 -10.00700 47.53200 1.000 47.63044  ? 284 GLU B O     1 
ATOM   693  C  CB    . GLU A 1 95  ? 15.03300 -9.08600  50.24400 1.000 48.33897  ? 284 GLU B CB    1 
ATOM   694  C  CG    . GLU A 1 95  ? 15.77900 -8.18900  51.22500 1.000 54.19274  ? 284 GLU B CG    1 
ATOM   695  C  CD    . GLU A 1 95  ? 17.28200 -8.18000  50.99100 1.000 57.79715  ? 284 GLU B CD    1 
ATOM   696  O  OE1   . GLU A 1 95  ? 17.83500 -9.22700  50.59600 1.000 66.59993  ? 284 GLU B OE1   1 
ATOM   697  O  OE2   . GLU A 1 95  ? 17.91200 -7.12300  51.20500 1.000 54.96663  ? 284 GLU B OE2   1 
ATOM   698  N  N     . PRO A 1 96  ? 15.78400 -10.33800 47.30300 1.000 43.97990  ? 285 PRO B N     1 
ATOM   699  C  CA    . PRO A 1 96  ? 17.20100 -10.05700 47.56600 1.000 45.82982  ? 285 PRO B CA    1 
ATOM   700  C  C     . PRO A 1 96  ? 17.70500 -8.79500  46.86800 1.000 44.91856  ? 285 PRO B C     1 
ATOM   701  O  O     . PRO A 1 96  ? 17.70300 -8.72300  45.63900 1.000 42.85853  ? 285 PRO B O     1 
ATOM   702  C  CB    . PRO A 1 96  ? 17.90800 -11.29800 47.01800 1.000 46.69855  ? 285 PRO B CB    1 
ATOM   703  C  CG    . PRO A 1 96  ? 17.01000 -11.78500 45.93800 1.000 40.60799  ? 285 PRO B CG    1 
ATOM   704  C  CD    . PRO A 1 96  ? 15.61100 -11.48600 46.39600 1.000 34.47744  ? 285 PRO B CD    1 
ATOM   705  N  N     . THR A 1 97  ? 18.12400 -7.81000  47.66100 1.000 44.09285  ? 286 THR B N     1 
ATOM   706  C  CA    . THR A 1 97  ? 18.59700 -6.54800  47.10900 1.000 42.90400  ? 286 THR B CA    1 
ATOM   707  C  C     . THR A 1 97  ? 19.84900 -6.76900  46.27000 1.000 33.80723  ? 286 THR B C     1 
ATOM   708  O  O     . THR A 1 97  ? 20.77100 -7.47700  46.68300 1.000 40.28826  ? 286 THR B O     1 
ATOM   709  C  CB    . THR A 1 97  ? 18.88300 -5.55400  48.23700 1.000 45.61784  ? 286 THR B CB    1 
ATOM   710  O  OG1   . THR A 1 97  ? 17.65400 -5.18800  48.87700 1.000 47.44097  ? 286 THR B OG1   1 
ATOM   711  C  CG2   . THR A 1 97  ? 19.56100 -4.30000  47.69900 1.000 44.25044  ? 286 THR B CG2   1 
ATOM   712  N  N     . HIS A 1 98  ? 19.86900 -6.17000  45.08100 1.000 30.31394  ? 287 HIS B N     1 
ATOM   713  C  CA    . HIS A 1 98  ? 21.03400 -6.23100  44.21200 1.000 33.31511  ? 287 HIS B CA    1 
ATOM   714  C  C     . HIS A 1 98  ? 20.99700 -5.04500  43.26100 1.000 32.18875  ? 287 HIS B C     1 
ATOM   715  O  O     . HIS A 1 98  ? 19.94400 -4.44500  43.02700 1.000 27.48655  ? 287 HIS B O     1 
ATOM   716  C  CB    . HIS A 1 98  ? 21.09200 -7.55000  43.43100 1.000 32.93757  ? 287 HIS B CB    1 
ATOM   717  C  CG    . HIS A 1 98  ? 19.87600 -7.81700  42.59800 1.000 34.91031  ? 287 HIS B CG    1 
ATOM   718  N  ND1   . HIS A 1 98  ? 19.56700 -7.08400  41.47200 1.000 31.30170  ? 287 HIS B ND1   1 
ATOM   719  C  CD2   . HIS A 1 98  ? 18.89400 -8.74100  42.72500 1.000 37.14641  ? 287 HIS B CD2   1 
ATOM   720  C  CE1   . HIS A 1 98  ? 18.44700 -7.54300  40.94300 1.000 35.20419  ? 287 HIS B CE1   1 
ATOM   721  N  NE2   . HIS A 1 98  ? 18.01800 -8.54900  41.68500 1.000 39.78712  ? 287 HIS B NE2   1 
ATOM   722  N  N     . PHE A 1 99  ? 22.16500 -4.71600  42.71600 1.000 32.83985  ? 288 PHE B N     1 
ATOM   723  C  CA    . PHE A 1 99  ? 22.24200 -3.69900  41.68200 1.000 25.53222  ? 288 PHE B CA    1 
ATOM   724  C  C     . PHE A 1 99  ? 21.62700 -4.21800  40.38600 1.000 27.91498  ? 288 PHE B C     1 
ATOM   725  O  O     . PHE A 1 99  ? 21.47100 -5.42300  40.17700 1.000 23.11765  ? 288 PHE B O     1 
ATOM   726  C  CB    . PHE A 1 99  ? 23.69100 -3.27900  41.44200 1.000 25.65943  ? 288 PHE B CB    1 
ATOM   727  C  CG    . PHE A 1 99  ? 24.26700 -2.43200  42.53900 1.000 35.48704  ? 288 PHE B CG    1 
ATOM   728  C  CD1   . PHE A 1 99  ? 24.09600 -1.05600  42.53000 1.000 31.11378  ? 288 PHE B CD1   1 
ATOM   729  C  CD2   . PHE A 1 99  ? 24.98200 -3.00800  43.57600 1.000 30.39545  ? 288 PHE B CD2   1 
ATOM   730  C  CE1   . PHE A 1 99  ? 24.62400 -0.27100  43.53700 1.000 29.19732  ? 288 PHE B CE1   1 
ATOM   731  C  CE2   . PHE A 1 99  ? 25.51400 -2.22900  44.58600 1.000 34.10716  ? 288 PHE B CE2   1 
ATOM   732  C  CZ    . PHE A 1 99  ? 25.33400 -0.85800  44.56600 1.000 37.58897  ? 288 PHE B CZ    1 
ATOM   733  N  N     . ALA A 1 100 ? 21.27300 -3.28300  39.50500 1.000 21.08665  ? 289 ALA B N     1 
ATOM   734  C  CA    . ALA A 1 100 ? 20.68100 -3.65900  38.22900 1.000 25.00275  ? 289 ALA B CA    1 
ATOM   735  C  C     . ALA A 1 100 ? 21.69000 -4.26700  37.26500 1.000 24.15175  ? 289 ALA B C     1 
ATOM   736  O  O     . ALA A 1 100 ? 21.28000 -4.82800  36.24400 1.000 25.64080  ? 289 ALA B O     1 
ATOM   737  C  CB    . ALA A 1 100 ? 20.01800 -2.44500  37.57700 1.000 26.72502  ? 289 ALA B CB    1 
ATOM   738  N  N     . TYR A 1 101 ? 22.98200 -4.18600  37.56400 1.000 24.82821  ? 290 TYR B N     1 
ATOM   739  C  CA    . TYR A 1 101 ? 24.02400 -4.57700  36.62900 1.000 23.66723  ? 290 TYR B CA    1 
ATOM   740  C  C     . TYR A 1 101 ? 24.87800 -5.69400  37.21200 1.000 31.21517  ? 290 TYR B C     1 
ATOM   741  O  O     . TYR A 1 101 ? 25.09100 -5.76900  38.42600 1.000 33.39619  ? 290 TYR B O     1 
ATOM   742  C  CB    . TYR A 1 101 ? 24.91000 -3.38100  36.26500 1.000 22.48018  ? 290 TYR B CB    1 
ATOM   743  C  CG    . TYR A 1 101 ? 24.12500 -2.16200  35.83900 1.000 24.23850  ? 290 TYR B CG    1 
ATOM   744  C  CD1   . TYR A 1 101 ? 23.57300 -2.07700  34.56700 1.000 25.16167  ? 290 TYR B CD1   1 
ATOM   745  C  CD2   . TYR A 1 101 ? 23.93300 -1.09700  36.71000 1.000 26.06170  ? 290 TYR B CD2   1 
ATOM   746  C  CE1   . TYR A 1 101 ? 22.85200 -0.96400  34.17400 1.000 25.75813  ? 290 TYR B CE1   1 
ATOM   747  C  CE2   . TYR A 1 101 ? 23.21400 0.02000   36.32700 1.000 22.48443  ? 290 TYR B CE2   1 
ATOM   748  C  CZ    . TYR A 1 101 ? 22.67600 0.08100   35.05900 1.000 22.50317  ? 290 TYR B CZ    1 
ATOM   749  O  OH    . TYR A 1 101 ? 21.96000 1.19000   34.67400 1.000 16.86959  ? 290 TYR B OH    1 
ATOM   750  N  N     . ASP A 1 102 ? 25.36300 -6.56200  36.32800 1.000 27.00498  ? 291 ASP B N     1 
ATOM   751  C  CA    . ASP A 1 102 ? 26.25600 -7.64400  36.71000 1.000 32.45855  ? 291 ASP B CA    1 
ATOM   752  C  C     . ASP A 1 102 ? 27.70600 -7.18400  36.56300 1.000 32.27295  ? 291 ASP B C     1 
ATOM   753  O  O     . ASP A 1 102 ? 27.98600 -6.01400  36.28800 1.000 27.30264  ? 291 ASP B O     1 
ATOM   754  C  CB    . ASP A 1 102 ? 25.95300 -8.89600  35.88600 1.000 27.37304  ? 291 ASP B CB    1 
ATOM   755  C  CG    . ASP A 1 102 ? 25.91800 -8.62600  34.39000 1.000 29.42011  ? 291 ASP B CG    1 
ATOM   756  O  OD1   . ASP A 1 102 ? 26.47000 -7.59900  33.94200 1.000 34.33670  ? 291 ASP B OD1   1 
ATOM   757  O  OD2   . ASP A 1 102 ? 25.32600 -9.44500  33.65700 1.000 29.62313  ? 291 ASP B OD2   1 
ATOM   758  N  N     . ALA A 1 103 ? 28.64900 -8.11200  36.74200 1.000 36.29468  ? 292 ALA B N     1 
ATOM   759  C  CA    . ALA A 1 103 ? 30.06800 -7.78000  36.71600 1.000 36.29079  ? 292 ALA B CA    1 
ATOM   760  C  C     . ALA A 1 103 ? 30.55600 -7.33600  35.34300 1.000 38.06512  ? 292 ALA B C     1 
ATOM   761  O  O     . ALA A 1 103 ? 31.66800 -6.80700  35.24500 1.000 41.58459  ? 292 ALA B O     1 
ATOM   762  C  CB    . ALA A 1 103 ? 30.89300 -8.97600  37.19400 1.000 30.05080  ? 292 ALA B CB    1 
ATOM   763  N  N     . GLN A 1 104 ? 29.76700 -7.53800  34.29000 1.000 33.11538  ? 293 GLN B N     1 
ATOM   764  C  CA    . GLN A 1 104 ? 30.13800 -7.12600  32.94300 1.000 38.38325  ? 293 GLN B CA    1 
ATOM   765  C  C     . GLN A 1 104 ? 29.54200 -5.77800  32.55500 1.000 32.66110  ? 293 GLN B C     1 
ATOM   766  O  O     . GLN A 1 104 ? 29.64700 -5.38000  31.39100 1.000 34.11743  ? 293 GLN B O     1 
ATOM   767  C  CB    . GLN A 1 104 ? 29.72100 -8.19300  31.92900 1.000 36.32831  ? 293 GLN B CB    1 
ATOM   768  C  CG    . GLN A 1 104 ? 30.68700 -9.36300  31.82500 1.000 42.90364  ? 293 GLN B CG    1 
ATOM   769  C  CD    . GLN A 1 104 ? 30.97100 -10.01200 33.16500 1.000 57.77059  ? 293 GLN B CD    1 
ATOM   770  O  OE1   . GLN A 1 104 ? 30.07000 -10.55300 33.81000 1.000 41.23302  ? 293 GLN B OE1   1 
ATOM   771  N  NE2   . GLN A 1 104 ? 32.22500 -9.95400  33.59700 1.000 60.22097  ? 293 GLN B NE2   1 
ATOM   772  N  N     . GLY A 1 105 ? 28.92100 -5.07200  33.49700 1.000 30.71718  ? 294 GLY B N     1 
ATOM   773  C  CA    . GLY A 1 105 ? 28.32700 -3.78700  33.18800 1.000 26.73692  ? 294 GLY B CA    1 
ATOM   774  C  C     . GLY A 1 105 ? 27.04200 -3.85700  32.39800 1.000 30.07241  ? 294 GLY B C     1 
ATOM   775  O  O     . GLY A 1 105 ? 26.62200 -2.84900  31.82500 1.000 37.29611  ? 294 GLY B O     1 
ATOM   776  N  N     . ARG A 1 106 ? 26.40300 -5.02200  32.34700 1.000 30.57149  ? 295 ARG B N     1 
ATOM   777  C  CA    . ARG A 1 106 ? 25.15000 -5.20800  31.63200 1.000 30.70182  ? 295 ARG B CA    1 
ATOM   778  C  C     . ARG A 1 106 ? 24.00700 -5.38200  32.62200 1.000 27.11460  ? 295 ARG B C     1 
ATOM   779  O  O     . ARG A 1 106 ? 24.20400 -5.85500  33.74400 1.000 27.26265  ? 295 ARG B O     1 
ATOM   780  C  CB    . ARG A 1 106 ? 25.21400 -6.42500  30.70400 1.000 27.56176  ? 295 ARG B CB    1 
ATOM   781  C  CG    . ARG A 1 106 ? 26.02500 -6.20200  29.44200 1.000 28.42619  ? 295 ARG B CG    1 
ATOM   782  C  CD    . ARG A 1 106 ? 25.89400 -7.38100  28.49200 1.000 31.22353  ? 295 ARG B CD    1 
ATOM   783  N  NE    . ARG A 1 106 ? 26.57500 -8.57000  28.98800 1.000 38.98863  ? 295 ARG B NE    1 
ATOM   784  C  CZ    . ARG A 1 106 ? 27.84400 -8.86400  28.73500 1.000 42.30809  ? 295 ARG B CZ    1 
ATOM   785  N  NH1   . ARG A 1 106 ? 28.60500 -8.06500  28.00500 1.000 39.08336  ? 295 ARG B NH1   1 
ATOM   786  N  NH2   . ARG A 1 106 ? 28.36100 -9.98700  29.22500 1.000 36.64013  ? 295 ARG B NH2   1 
ATOM   787  N  N     . VAL A 1 107 ? 22.80500 -4.98900  32.19700 1.000 22.94530  ? 296 VAL B N     1 
ATOM   788  C  CA    . VAL A 1 107 ? 21.63600 -5.15200  33.04900 1.000 26.59173  ? 296 VAL B CA    1 
ATOM   789  C  C     . VAL A 1 107 ? 21.37300 -6.63700  33.26300 1.000 31.14253  ? 296 VAL B C     1 
ATOM   790  O  O     . VAL A 1 107 ? 21.55300 -7.46200  32.35500 1.000 31.83754  ? 296 VAL B O     1 
ATOM   791  C  CB    . VAL A 1 107 ? 20.41200 -4.43500  32.44900 1.000 27.54167  ? 296 VAL B CB    1 
ATOM   792  C  CG1   . VAL A 1 107 ? 19.92000 -5.13500  31.19200 1.000 21.90517  ? 296 VAL B CG1   1 
ATOM   793  C  CG2   . VAL A 1 107 ? 19.29800 -4.32800  33.48000 1.000 25.52165  ? 296 VAL B CG2   1 
ATOM   794  N  N     . ARG A 1 108 ? 20.98300 -6.99000  34.48300 1.000 26.90300  ? 297 ARG B N     1 
ATOM   795  C  CA    . ARG A 1 108 ? 20.74500 -8.38300  34.82000 1.000 29.17747  ? 297 ARG B CA    1 
ATOM   796  C  C     . ARG A 1 108 ? 19.44000 -8.87200  34.20100 1.000 29.53129  ? 297 ARG B C     1 
ATOM   797  O  O     . ARG A 1 108 ? 18.52600 -8.09200  33.92100 1.000 28.68901  ? 297 ARG B O     1 
ATOM   798  C  CB    . ARG A 1 108 ? 20.70600 -8.56400  36.33600 1.000 27.78133  ? 297 ARG B CB    1 
ATOM   799  C  CG    . ARG A 1 108 ? 22.03200 -8.30400  37.03100 1.000 28.09822  ? 297 ARG B CG    1 
ATOM   800  C  CD    . ARG A 1 108 ? 21.83200 -8.10000  38.52200 1.000 26.38627  ? 297 ARG B CD    1 
ATOM   801  N  NE    . ARG A 1 108 ? 21.09600 -9.19800  39.13700 1.000 31.56347  ? 297 ARG B NE    1 
ATOM   802  C  CZ    . ARG A 1 108 ? 21.63300 -10.09900 39.94800 1.000 28.93817  ? 297 ARG B CZ    1 
ATOM   803  N  NH1   . ARG A 1 108 ? 22.91200 -10.05500 40.28200 1.000 31.67396  ? 297 ARG B NH1   1 
ATOM   804  N  NH2   . ARG A 1 108 ? 20.86500 -11.06700 40.44000 1.000 28.85363  ? 297 ARG B NH2   1 
ATOM   805  N  N     . ALA A 1 109 ? 19.36600 -10.18700 33.98600 1.000 25.68958  ? 298 ALA B N     1 
ATOM   806  C  CA    . ALA A 1 109 ? 18.14900 -10.78200 33.44600 1.000 30.42389  ? 298 ALA B CA    1 
ATOM   807  C  C     . ALA A 1 109 ? 16.98100 -10.62500 34.41200 1.000 27.54957  ? 298 ALA B C     1 
ATOM   808  O  O     . ALA A 1 109 ? 15.84500 -10.38000 33.98900 1.000 34.50699  ? 298 ALA B O     1 
ATOM   809  C  CB    . ALA A 1 109 ? 18.38500 -12.25800 33.12400 1.000 30.16311  ? 298 ALA B CB    1 
ATOM   810  N  N     . ASP A 1 110 ? 17.23900 -10.76100 35.71200 1.000 26.75597  ? 299 ASP B N     1 
ATOM   811  C  CA    . ASP A 1 110 ? 16.18400 -10.68100 36.71500 1.000 39.70660  ? 299 ASP B CA    1 
ATOM   812  C  C     . ASP A 1 110 ? 15.86400 -9.25200  37.13600 1.000 35.43622  ? 299 ASP B C     1 
ATOM   813  O  O     . ASP A 1 110 ? 14.97400 -9.05500  37.97000 1.000 44.47095  ? 299 ASP B O     1 
ATOM   814  C  CB    . ASP A 1 110 ? 16.56500 -11.51400 37.94500 1.000 36.57794  ? 299 ASP B CB    1 
ATOM   815  C  CG    . ASP A 1 110 ? 17.75800 -10.94800 38.69400 1.000 34.40188  ? 299 ASP B CG    1 
ATOM   816  O  OD1   . ASP A 1 110 ? 18.51200 -10.14300 38.11000 1.000 35.54395  ? 299 ASP B OD1   1 
ATOM   817  O  OD2   . ASP A 1 110 ? 17.94600 -11.31800 39.87200 1.000 43.39446  ? 299 ASP B OD2   1 
ATOM   818  N  N     . THR A 1 111 ? 16.56500 -8.25900  36.59400 1.000 32.58047  ? 300 THR B N     1 
ATOM   819  C  CA    . THR A 1 111 ? 16.24300 -6.86900  36.88200 1.000 36.41995  ? 300 THR B CA    1 
ATOM   820  C  C     . THR A 1 111 ? 14.88200 -6.50800  36.29800 1.000 35.25112  ? 300 THR B C     1 
ATOM   821  O  O     . THR A 1 111 ? 14.55300 -6.88200  35.16900 1.000 36.83093  ? 300 THR B O     1 
ATOM   822  C  CB    . THR A 1 111 ? 17.32200 -5.94400  36.31400 1.000 32.09402  ? 300 THR B CB    1 
ATOM   823  O  OG1   . THR A 1 111 ? 18.58200 -6.24300  36.92800 1.000 26.17624  ? 300 THR B OG1   1 
ATOM   824  C  CG2   . THR A 1 111 ? 16.97800 -4.48400  36.57100 1.000 31.23882  ? 300 THR B CG2   1 
ATOM   825  N  N     . GLY A 1 112 ? 14.08800 -5.77700  37.07600 1.000 38.45322  ? 301 GLY B N     1 
ATOM   826  C  CA    . GLY A 1 112 ? 12.78100 -5.33400  36.63900 1.000 41.10780  ? 301 GLY B CA    1 
ATOM   827  C  C     . GLY A 1 112 ? 12.86800 -4.16300  35.68100 1.000 42.49836  ? 301 GLY B C     1 
ATOM   828  O  O     . GLY A 1 112 ? 13.92000 -3.85800  35.11300 1.000 37.76997  ? 301 GLY B O     1 
ATOM   829  N  N     . ALA A 1 113 ? 11.72900 -3.49400  35.50300 1.000 47.08296  ? 302 ALA B N     1 
ATOM   830  C  CA    . ALA A 1 113 ? 11.64200 -2.37900  34.57000 1.000 46.43803  ? 302 ALA B CA    1 
ATOM   831  C  C     . ALA A 1 113 ? 12.19700 -1.07800  35.13500 1.000 44.34370  ? 302 ALA B C     1 
ATOM   832  O  O     . ALA A 1 113 ? 12.34500 -0.11000  34.38000 1.000 37.90505  ? 302 ALA B O     1 
ATOM   833  C  CB    . ALA A 1 113 ? 10.18800 -2.16900  34.13700 1.000 48.31326  ? 302 ALA B CB    1 
ATOM   834  N  N     . VAL A 1 114 ? 12.51400 -1.03000  36.42800 1.000 33.51974  ? 303 VAL B N     1 
ATOM   835  C  CA    . VAL A 1 114 ? 12.98600 0.18200   37.08500 1.000 35.51259  ? 303 VAL B CA    1 
ATOM   836  C  C     . VAL A 1 114 ? 14.42100 -0.03700  37.54200 1.000 28.76328  ? 303 VAL B C     1 
ATOM   837  O  O     . VAL A 1 114 ? 14.71100 -1.00200  38.25900 1.000 31.51242  ? 303 VAL B O     1 
ATOM   838  C  CB    . VAL A 1 114 ? 12.09000 0.56900   38.27600 1.000 35.14100  ? 303 VAL B CB    1 
ATOM   839  C  CG1   . VAL A 1 114 ? 12.76200 1.64300   39.11400 1.000 33.86062  ? 303 VAL B CG1   1 
ATOM   840  C  CG2   . VAL A 1 114 ? 10.73200 1.04000   37.78500 1.000 37.88157  ? 303 VAL B CG2   1 
ATOM   841  N  N     . ILE A 1 115 ? 15.31100 0.86500   37.13400 1.000 28.50235  ? 304 ILE B N     1 
ATOM   842  C  CA    . ILE A 1 115 ? 16.72100 0.82600   37.50400 1.000 29.48107  ? 304 ILE B CA    1 
ATOM   843  C  C     . ILE A 1 115 ? 17.01200 2.02700   38.39200 1.000 32.46249  ? 304 ILE B C     1 
ATOM   844  O  O     . ILE A 1 115 ? 16.71500 3.16800   38.01800 1.000 31.16069  ? 304 ILE B O     1 
ATOM   845  C  CB    . ILE A 1 115 ? 17.63000 0.83000   36.26300 1.000 25.47959  ? 304 ILE B CB    1 
ATOM   846  C  CG1   . ILE A 1 115 ? 17.41100 -0.43800  35.43400 1.000 28.03939  ? 304 ILE B CG1   1 
ATOM   847  C  CG2   . ILE A 1 115 ? 19.09000 0.97500   36.67000 1.000 25.56161  ? 304 ILE B CG2   1 
ATOM   848  C  CD1   . ILE A 1 115 ? 18.22700 -0.47900  34.15500 1.000 19.89283  ? 304 ILE B CD1   1 
ATOM   849  N  N     . TYR A 1 116 ? 17.58900 1.77000   39.56500 1.000 30.31471  ? 305 TYR B N     1 
ATOM   850  C  CA    . TYR A 1 116 ? 17.90700 2.81700   40.53500 1.000 29.15801  ? 305 TYR B CA    1 
ATOM   851  C  C     . TYR A 1 116 ? 19.40900 3.07400   40.49500 1.000 30.81590  ? 305 TYR B C     1 
ATOM   852  O  O     . TYR A 1 116 ? 20.19500 2.33800   41.09800 1.000 32.22171  ? 305 TYR B O     1 
ATOM   853  C  CB    . TYR A 1 116 ? 17.44400 2.42200   41.93300 1.000 28.96737  ? 305 TYR B CB    1 
ATOM   854  C  CG    . TYR A 1 116 ? 15.94200 2.34100   42.07500 1.000 31.24316  ? 305 TYR B CG    1 
ATOM   855  C  CD1   . TYR A 1 116 ? 15.16700 3.49300   42.10600 1.000 33.71262  ? 305 TYR B CD1   1 
ATOM   856  C  CD2   . TYR A 1 116 ? 15.30000 1.11500   42.18300 1.000 32.45520  ? 305 TYR B CD2   1 
ATOM   857  C  CE1   . TYR A 1 116 ? 13.79300 3.42700   42.23700 1.000 33.66894  ? 305 TYR B CE1   1 
ATOM   858  C  CE2   . TYR A 1 116 ? 13.92600 1.03800   42.31500 1.000 36.17628  ? 305 TYR B CE2   1 
ATOM   859  C  CZ    . TYR A 1 116 ? 13.17800 2.19700   42.34200 1.000 37.61054  ? 305 TYR B CZ    1 
ATOM   860  O  OH    . TYR A 1 116 ? 11.81000 2.12700   42.47400 1.000 40.58713  ? 305 TYR B OH    1 
ATOM   861  N  N     . GLU A 1 117 ? 19.80400 4.12800   39.79000 1.000 31.34803  ? 306 GLU B N     1 
ATOM   862  C  CA    . GLU A 1 117 ? 21.20500 4.49100   39.66900 1.000 30.17668  ? 306 GLU B CA    1 
ATOM   863  C  C     . GLU A 1 117 ? 21.58800 5.52500   40.72300 1.000 30.67319  ? 306 GLU B C     1 
ATOM   864  O  O     . GLU A 1 117 ? 20.74100 6.10400   41.40600 1.000 33.65979  ? 306 GLU B O     1 
ATOM   865  C  CB    . GLU A 1 117 ? 21.50200 5.02800   38.26900 1.000 23.85067  ? 306 GLU B CB    1 
ATOM   866  C  CG    . GLU A 1 117 ? 21.55900 3.95700   37.19700 1.000 24.32931  ? 306 GLU B CG    1 
ATOM   867  C  CD    . GLU A 1 117 ? 22.34500 4.40100   35.98100 1.000 25.36363  ? 306 GLU B CD    1 
ATOM   868  O  OE1   . GLU A 1 117 ? 22.67600 5.60300   35.89300 1.000 24.12924  ? 306 GLU B OE1   1 
ATOM   869  O  OE2   . GLU A 1 117 ? 22.64000 3.54600   35.12000 1.000 22.97425  ? 306 GLU B OE2   1 
ATOM   870  N  N     . CYS A 1 118 ? 22.89200 5.74700   40.85500 1.000 34.11859  ? 307 CYS B N     1 
ATOM   871  C  CA    . CYS A 1 118 ? 23.39100 6.79500   41.72600 1.000 34.29680  ? 307 CYS B CA    1 
ATOM   872  C  C     . CYS A 1 118 ? 23.21400 8.15700   41.05900 1.000 35.00148  ? 307 CYS B C     1 
ATOM   873  O  O     . CYS A 1 118 ? 22.93600 8.26500   39.86200 1.000 22.99932  ? 307 CYS B O     1 
ATOM   874  C  CB    . CYS A 1 118 ? 24.85700 6.55000   42.07900 1.000 32.56996  ? 307 CYS B CB    1 
ATOM   875  S  SG    . CYS A 1 118 ? 25.13000 5.12600   43.16600 1.000 31.18156  ? 307 CYS B SG    1 
ATOM   876  N  N     . ASN A 1 119 ? 23.36900 9.21100   41.86000 1.000 35.63190  ? 308 ASN B N     1 
ATOM   877  C  CA    . ASN A 1 119 ? 23.17000 10.57000  41.37400 1.000 35.72591  ? 308 ASN B CA    1 
ATOM   878  C  C     . ASN A 1 119 ? 24.30000 11.48400  41.83200 1.000 32.37506  ? 308 ASN B C     1 
ATOM   879  O  O     . ASN A 1 119 ? 25.29600 11.01800  42.39400 1.000 32.06465  ? 308 ASN B O     1 
ATOM   880  C  CB    . ASN A 1 119 ? 21.81600 11.11100  41.84400 1.000 36.90332  ? 308 ASN B CB    1 
ATOM   881  C  CG    . ASN A 1 119 ? 21.59400 10.91700  43.33100 1.000 39.86153  ? 308 ASN B CG    1 
ATOM   882  O  OD1   . ASN A 1 119 ? 22.20900 11.59400  44.15500 1.000 43.85857  ? 308 ASN B OD1   1 
ATOM   883  N  ND2   . ASN A 1 119 ? 20.70600 9.99300   43.68200 1.000 40.33588  ? 308 ASN B ND2   1 
ATOM   884  N  N     . SER A 1 120 ? 24.15100 12.78900  41.59400 1.000 34.36299  ? 309 SER B N     1 
ATOM   885  C  CA    . SER A 1 120 ? 25.19200 13.75300  41.93100 1.000 34.84759  ? 309 SER B CA    1 
ATOM   886  C  C     . SER A 1 120 ? 25.33000 13.98200  43.42900 1.000 35.57115  ? 309 SER B C     1 
ATOM   887  O  O     . SER A 1 120 ? 26.33800 14.55400  43.85800 1.000 38.79562  ? 309 SER B O     1 
ATOM   888  C  CB    . SER A 1 120 ? 24.91500 15.08400  41.23000 1.000 33.25703  ? 309 SER B CB    1 
ATOM   889  O  OG    . SER A 1 120 ? 23.63100 15.57700  41.56600 1.000 40.31591  ? 309 SER B OG    1 
ATOM   890  N  N     . PHE A 1 121 ? 24.35400 13.56200  44.23000 1.000 32.67172  ? 310 PHE B N     1 
ATOM   891  C  CA    . PHE A 1 121 ? 24.43300 13.70900  45.67600 1.000 38.68900  ? 310 PHE B CA    1 
ATOM   892  C  C     . PHE A 1 121 ? 25.13400 12.54000  46.35700 1.000 44.44666  ? 310 PHE B C     1 
ATOM   893  O  O     . PHE A 1 121 ? 25.50200 12.65900  47.53100 1.000 41.66959  ? 310 PHE B O     1 
ATOM   894  C  CB    . PHE A 1 121 ? 23.02900 13.88600  46.26700 1.000 42.08017  ? 310 PHE B CB    1 
ATOM   895  C  CG    . PHE A 1 121 ? 22.39500 15.21200  45.94200 1.000 41.35074  ? 310 PHE B CG    1 
ATOM   896  C  CD1   . PHE A 1 121 ? 21.86600 15.45100  44.68300 1.000 49.84753  ? 310 PHE B CD1   1 
ATOM   897  C  CD2   . PHE A 1 121 ? 22.32100 16.21100  46.89500 1.000 42.97827  ? 310 PHE B CD2   1 
ATOM   898  C  CE1   . PHE A 1 121 ? 21.27800 16.66700  44.38100 1.000 46.47929  ? 310 PHE B CE1   1 
ATOM   899  C  CE2   . PHE A 1 121 ? 21.73600 17.42900  46.60000 1.000 43.91287  ? 310 PHE B CE2   1 
ATOM   900  C  CZ    . PHE A 1 121 ? 21.21500 17.65900  45.34100 1.000 43.31622  ? 310 PHE B CZ    1 
ATOM   901  N  N     . CYS A 1 122 ? 25.33000 11.42500  45.65700 1.000 42.12538  ? 311 CYS B N     1 
ATOM   902  C  CA    . CYS A 1 122 ? 26.06900 10.30700  46.22600 1.000 46.72697  ? 311 CYS B CA    1 
ATOM   903  C  C     . CYS A 1 122 ? 27.53900 10.66800  46.38900 1.000 48.20452  ? 311 CYS B C     1 
ATOM   904  O  O     . CYS A 1 122 ? 28.08200 11.50800  45.66700 1.000 46.25154  ? 311 CYS B O     1 
ATOM   905  C  CB    . CYS A 1 122 ? 25.95100 9.06700   45.33800 1.000 43.29587  ? 311 CYS B CB    1 
ATOM   906  S  SG    . CYS A 1 122 ? 24.28000 8.46700   45.04000 1.000 35.90088  ? 311 CYS B SG    1 
ATOM   907  N  N     . SER A 1 123 ? 28.18900 10.01500  47.35400 1.000 61.09358  ? 312 SER B N     1 
ATOM   908  C  CA    . SER A 1 123 ? 29.64300 10.09000  47.48900 1.000 56.85959  ? 312 SER B CA    1 
ATOM   909  C  C     . SER A 1 123 ? 30.26400 9.07400   46.52900 1.000 59.13399  ? 312 SER B C     1 
ATOM   910  O  O     . SER A 1 123 ? 30.88500 8.08300   46.91800 1.000 70.44376  ? 312 SER B O     1 
ATOM   911  C  CB    . SER A 1 123 ? 30.06400 9.84600   48.93100 1.000 55.01631  ? 312 SER B CB    1 
ATOM   912  O  OG    . SER A 1 123 ? 29.57400 8.60300   49.40300 1.000 62.10313  ? 312 SER B OG    1 
ATOM   913  N  N     . CYS A 1 124 ? 30.07500 9.33900   45.23800 1.000 54.26677  ? 313 CYS B N     1 
ATOM   914  C  CA    . CYS A 1 124 ? 30.47500 8.42600   44.18000 1.000 50.76514  ? 313 CYS B CA    1 
ATOM   915  C  C     . CYS A 1 124 ? 31.30000 9.15400   43.13200 1.000 62.11525  ? 313 CYS B C     1 
ATOM   916  O  O     . CYS A 1 124 ? 31.11500 10.34900  42.88800 1.000 72.08085  ? 313 CYS B O     1 
ATOM   917  C  CB    . CYS A 1 124 ? 29.26100 7.78900   43.49100 1.000 54.79030  ? 313 CYS B CB    1 
ATOM   918  S  SG    . CYS A 1 124 ? 28.55600 6.38500   44.35300 1.000 57.65432  ? 313 CYS B SG    1 
ATOM   919  N  N     . SER A 1 125 ? 32.21300 8.41300   42.51200 1.000 59.54905  ? 314 SER B N     1 
ATOM   920  C  CA    . SER A 1 125 ? 32.90100 8.90300   41.33200 1.000 57.98547  ? 314 SER B CA    1 
ATOM   921  C  C     . SER A 1 125 ? 32.03500 8.66600   40.09800 1.000 57.15754  ? 314 SER B C     1 
ATOM   922  O  O     . SER A 1 125 ? 30.98600 8.01900   40.15400 1.000 56.80381  ? 314 SER B O     1 
ATOM   923  C  CB    . SER A 1 125 ? 34.25800 8.22000   41.17300 1.000 59.11780  ? 314 SER B CB    1 
ATOM   924  O  OG    . SER A 1 125 ? 34.17300 7.11700   40.28700 1.000 68.46926  ? 314 SER B OG    1 
ATOM   925  N  N     . MET A 1 126 ? 32.48800 9.20100   38.96400 1.000 59.78534  ? 315 MET B N     1 
ATOM   926  C  CA    . MET A 1 126 ? 31.72700 9.05800   37.73000 1.000 61.59979  ? 315 MET B CA    1 
ATOM   927  C  C     . MET A 1 126 ? 31.82700 7.65800   37.13300 1.000 64.99453  ? 315 MET B C     1 
ATOM   928  O  O     . MET A 1 126 ? 31.07500 7.34600   36.20300 1.000 60.44097  ? 315 MET B O     1 
ATOM   929  C  CB    . MET A 1 126 ? 32.18800 10.10200  36.71000 1.000 63.06977  ? 315 MET B CB    1 
ATOM   930  C  CG    . MET A 1 126 ? 31.20900 10.32100  35.56800 1.000 65.66064  ? 315 MET B CG    1 
ATOM   931  S  SD    . MET A 1 126 ? 29.50200 10.03800  36.07800 1.000 68.31029  ? 315 MET B SD    1 
ATOM   932  C  CE    . MET A 1 126 ? 29.09700 11.62800  36.80000 1.000 51.19102  ? 315 MET B CE    1 
ATOM   933  N  N     . GLU A 1 127 ? 32.71900 6.80800   37.64300 1.000 70.77596  ? 316 GLU B N     1 
ATOM   934  C  CA    . GLU A 1 127 ? 32.84800 5.43400   37.17400 1.000 78.03832  ? 316 GLU B CA    1 
ATOM   935  C  C     . GLU A 1 127 ? 32.30600 4.43300   38.19100 1.000 76.25310  ? 316 GLU B C     1 
ATOM   936  O  O     . GLU A 1 127 ? 32.80800 3.31200   38.30100 1.000 70.64929  ? 316 GLU B O     1 
ATOM   937  C  CB    . GLU A 1 127 ? 34.30200 5.11600   36.82700 1.000 84.97079  ? 316 GLU B CB    1 
ATOM   938  C  CG    . GLU A 1 127 ? 34.80200 5.82000   35.56900 1.000 83.85419  ? 316 GLU B CG    1 
ATOM   939  C  CD    . GLU A 1 127 ? 34.50800 7.31200   35.56100 1.000 84.30940  ? 316 GLU B CD    1 
ATOM   940  O  OE1   . GLU A 1 127 ? 35.30700 8.08800   36.12400 1.000 82.59357  ? 316 GLU B OE1   1 
ATOM   941  O  OE2   . GLU A 1 127 ? 33.46700 7.70800   34.99400 1.000 82.17807  ? 316 GLU B OE2   1 
ATOM   942  N  N     . CYS A 1 128 ? 31.28900 4.83400   38.94500 1.000 55.55783  ? 317 CYS B N     1 
ATOM   943  C  CA    . CYS A 1 128 ? 30.59400 3.90100   39.81500 1.000 46.23209  ? 317 CYS B CA    1 
ATOM   944  C  C     . CYS A 1 128 ? 29.85400 2.86500   38.97100 1.000 43.00850  ? 317 CYS B C     1 
ATOM   945  O  O     . CYS A 1 128 ? 29.31000 3.20200   37.91400 1.000 41.41993  ? 317 CYS B O     1 
ATOM   946  C  CB    . CYS A 1 128 ? 29.61600 4.65600   40.71800 1.000 46.73160  ? 317 CYS B CB    1 
ATOM   947  S  SG    . CYS A 1 128 ? 28.35700 3.65500   41.53600 1.000 30.44677  ? 317 CYS B SG    1 
ATOM   948  N  N     . PRO A 1 129 ? 29.82100 1.60000   39.40000 1.000 39.79719  ? 318 PRO B N     1 
ATOM   949  C  CA    . PRO A 1 129 ? 29.12800 0.57500   38.60000 1.000 36.71835  ? 318 PRO B CA    1 
ATOM   950  C  C     . PRO A 1 129 ? 27.64700 0.84800   38.41300 1.000 33.07375  ? 318 PRO B C     1 
ATOM   951  O  O     . PRO A 1 129 ? 27.04100 0.28700   37.49100 1.000 25.10302  ? 318 PRO B O     1 
ATOM   952  C  CB    . PRO A 1 129 ? 29.36100 -0.71300  39.40200 1.000 36.17521  ? 318 PRO B CB    1 
ATOM   953  C  CG    . PRO A 1 129 ? 30.59300 -0.44500  40.19900 1.000 39.00154  ? 318 PRO B CG    1 
ATOM   954  C  CD    . PRO A 1 129 ? 30.54400 1.01500   40.54200 1.000 40.88379  ? 318 PRO B CD    1 
ATOM   955  N  N     . ASN A 1 130 ? 27.04400 1.69000   39.25300 1.000 31.79942  ? 319 ASN B N     1 
ATOM   956  C  CA    . ASN A 1 130 ? 25.62600 2.01300   39.16500 1.000 31.36351  ? 319 ASN B CA    1 
ATOM   957  C  C     . ASN A 1 130 ? 25.34900 3.28700   38.37100 1.000 29.13568  ? 319 ASN B C     1 
ATOM   958  O  O     . ASN A 1 130 ? 24.34700 3.96500   38.61500 1.000 28.95549  ? 319 ASN B O     1 
ATOM   959  C  CB    . ASN A 1 130 ? 25.01800 2.09200   40.56600 1.000 30.56905  ? 319 ASN B CB    1 
ATOM   960  C  CG    . ASN A 1 130 ? 23.53900 1.75800   40.58000 1.000 28.14733  ? 319 ASN B CG    1 
ATOM   961  O  OD1   . ASN A 1 130 ? 23.05100 1.01900   39.72500 1.000 27.46573  ? 319 ASN B OD1   1 
ATOM   962  N  ND2   . ASN A 1 130 ? 22.81900 2.30000   41.55500 1.000 28.29612  ? 319 ASN B ND2   1 
ATOM   963  N  N     . ARG A 1 131 ? 26.22900 3.63000   37.42800 1.000 27.48679  ? 320 ARG B N     1 
ATOM   964  C  CA    . ARG A 1 131 ? 26.06500 4.81300   36.58800 1.000 31.58461  ? 320 ARG B CA    1 
ATOM   965  C  C     . ARG A 1 131 ? 26.20400 4.48900   35.10400 1.000 27.03848  ? 320 ARG B C     1 
ATOM   966  O  O     . ARG A 1 131 ? 26.71400 5.30500   34.33200 1.000 26.54042  ? 320 ARG B O     1 
ATOM   967  C  CB    . ARG A 1 131 ? 27.08000 5.88200   36.99200 1.000 36.14187  ? 320 ARG B CB    1 
ATOM   968  C  CG    . ARG A 1 131 ? 26.86800 6.47600   38.37500 1.000 38.51756  ? 320 ARG B CG    1 
ATOM   969  C  CD    . ARG A 1 131 ? 27.95600 7.49300   38.69500 1.000 48.97479  ? 320 ARG B CD    1 
ATOM   970  N  NE    . ARG A 1 131 ? 27.81800 8.05800   40.03200 1.000 44.58645  ? 320 ARG B NE    1 
ATOM   971  C  CZ    . ARG A 1 131 ? 27.21300 9.20500   40.30400 1.000 35.24190  ? 320 ARG B CZ    1 
ATOM   972  N  NH1   . ARG A 1 131 ? 26.66900 9.94300   39.34900 1.000 37.06129  ? 320 ARG B NH1   1 
ATOM   973  N  NH2   . ARG A 1 131 ? 27.15200 9.62500   41.56400 1.000 36.55975  ? 320 ARG B NH2   1 
ATOM   974  N  N     . VAL A 1 132 ? 25.75600 3.29900   34.69200 1.000 24.23391  ? 321 VAL B N     1 
ATOM   975  C  CA    . VAL A 1 132 ? 25.90400 2.88300   33.29800 1.000 26.44609  ? 321 VAL B CA    1 
ATOM   976  C  C     . VAL A 1 132 ? 25.12300 3.81200   32.37600 1.000 24.28640  ? 321 VAL B C     1 
ATOM   977  O  O     . VAL A 1 132 ? 25.62900 4.25900   31.34000 1.000 23.19657  ? 321 VAL B O     1 
ATOM   978  C  CB    . VAL A 1 132 ? 25.46000 1.41800   33.12800 1.000 23.76859  ? 321 VAL B CB    1 
ATOM   979  C  CG1   . VAL A 1 132 ? 25.54200 1.00300   31.66600 1.000 23.29311  ? 321 VAL B CG1   1 
ATOM   980  C  CG2   . VAL A 1 132 ? 26.30500 0.50300   33.99700 1.000 26.33901  ? 321 VAL B CG2   1 
ATOM   981  N  N     . VAL A 1 133 ? 23.87500 4.11500   32.74100 1.000 20.86483  ? 322 VAL B N     1 
ATOM   982  C  CA    . VAL A 1 133 ? 23.05700 5.00900   31.92800 1.000 24.82101  ? 322 VAL B CA    1 
ATOM   983  C  C     . VAL A 1 133 ? 23.65100 6.41200   31.91400 1.000 26.53970  ? 322 VAL B C     1 
ATOM   984  O  O     . VAL A 1 133 ? 23.67200 7.08400   30.87600 1.000 20.17083  ? 322 VAL B O     1 
ATOM   985  C  CB    . VAL A 1 133 ? 21.60400 5.01000   32.44100 1.000 22.52958  ? 322 VAL B CB    1 
ATOM   986  C  CG1   . VAL A 1 133 ? 20.77400 6.04700   31.70400 1.000 20.64581  ? 322 VAL B CG1   1 
ATOM   987  C  CG2   . VAL A 1 133 ? 20.99000 3.62700   32.29600 1.000 18.32608  ? 322 VAL B CG2   1 
ATOM   988  N  N     . GLN A 1 134 ? 24.15000 6.86900   33.06500 1.000 25.99697  ? 323 GLN B N     1 
ATOM   989  C  CA    . GLN A 1 134 ? 24.69500 8.21900   33.16300 1.000 28.46689  ? 323 GLN B CA    1 
ATOM   990  C  C     . GLN A 1 134 ? 25.91800 8.39300   32.26900 1.000 31.11257  ? 323 GLN B C     1 
ATOM   991  O  O     . GLN A 1 134 ? 26.10000 9.45000   31.65300 1.000 31.82751  ? 323 GLN B O     1 
ATOM   992  C  CB    . GLN A 1 134 ? 25.03600 8.53200   34.61900 1.000 24.36020  ? 323 GLN B CB    1 
ATOM   993  C  CG    . GLN A 1 134 ? 24.46300 9.83900   35.13200 1.000 29.83789  ? 323 GLN B CG    1 
ATOM   994  C  CD    . GLN A 1 134 ? 25.00200 10.20400  36.50200 1.000 39.33505  ? 323 GLN B CD    1 
ATOM   995  O  OE1   . GLN A 1 134 ? 25.53400 9.35400   37.21600 1.000 32.77546  ? 323 GLN B OE1   1 
ATOM   996  N  NE2   . GLN A 1 134 ? 24.87300 11.47600  36.86900 1.000 40.70867  ? 323 GLN B NE2   1 
ATOM   997  N  N     . ARG A 1 135 ? 26.77400 7.36900   32.18900 1.000 25.45598  ? 324 ARG B N     1 
ATOM   998  C  CA    . ARG A 1 135 ? 27.96400 7.46700   31.34700 1.000 34.20160  ? 324 ARG B CA    1 
ATOM   999  C  C     . ARG A 1 135 ? 27.60200 7.59400   29.87300 1.000 29.65689  ? 324 ARG B C     1 
ATOM   1000 O  O     . ARG A 1 135 ? 28.34100 8.22000   29.10500 1.000 30.61561  ? 324 ARG B O     1 
ATOM   1001 C  CB    . ARG A 1 135 ? 28.87700 6.26200   31.57800 1.000 34.24642  ? 324 ARG B CB    1 
ATOM   1002 C  CG    . ARG A 1 135 ? 29.64000 6.32400   32.89400 1.000 35.34019  ? 324 ARG B CG    1 
ATOM   1003 C  CD    . ARG A 1 135 ? 30.65000 5.19400   33.02300 1.000 42.65074  ? 324 ARG B CD    1 
ATOM   1004 N  NE    . ARG A 1 135 ? 30.02900 3.93200   33.40300 1.000 40.96800  ? 324 ARG B NE    1 
ATOM   1005 C  CZ    . ARG A 1 135 ? 29.77800 3.57100   34.65400 1.000 40.66547  ? 324 ARG B CZ    1 
ATOM   1006 N  NH1   . ARG A 1 135 ? 30.05900 4.36700   35.67200 1.000 38.75967  ? 324 ARG B NH1   1 
ATOM   1007 N  NH2   . ARG A 1 135 ? 29.22900 2.38200   34.89000 1.000 38.42226  ? 324 ARG B NH2   1 
ATOM   1008 N  N     . GLY A 1 136 ? 26.48400 7.01300   29.46100 1.000 27.03838  ? 325 GLY B N     1 
ATOM   1009 C  CA    . GLY A 1 136 ? 25.95600 7.23100   28.13300 1.000 28.64256  ? 325 GLY B CA    1 
ATOM   1010 C  C     . GLY A 1 136 ? 26.28600 6.12700   27.15000 1.000 30.05751  ? 325 GLY B C     1 
ATOM   1011 O  O     . GLY A 1 136 ? 26.69500 5.01900   27.50400 1.000 27.91943  ? 325 GLY B O     1 
ATOM   1012 N  N     . ARG A 1 137 ? 26.10200 6.45900   25.87500 1.000 35.45620  ? 326 ARG B N     1 
ATOM   1013 C  CA    . ARG A 1 137 ? 26.24800 5.48800   24.80000 1.000 33.96101  ? 326 ARG B CA    1 
ATOM   1014 C  C     . ARG A 1 137 ? 27.70200 5.05900   24.64200 1.000 38.43664  ? 326 ARG B C     1 
ATOM   1015 O  O     . ARG A 1 137 ? 28.62500 5.86900   24.76900 1.000 33.01445  ? 326 ARG B O     1 
ATOM   1016 C  CB    . ARG A 1 137 ? 25.72000 6.08200   23.49300 1.000 29.78959  ? 326 ARG B CB    1 
ATOM   1017 C  CG    . ARG A 1 137 ? 25.79600 5.16600   22.28300 1.000 29.68854  ? 326 ARG B CG    1 
ATOM   1018 C  CD    . ARG A 1 137 ? 25.00900 5.75100   21.11700 1.000 29.65539  ? 326 ARG B CD    1 
ATOM   1019 N  NE    . ARG A 1 137 ? 25.36400 7.14200   20.86500 1.000 32.56300  ? 326 ARG B NE    1 
ATOM   1020 C  CZ    . ARG A 1 137 ? 26.21200 7.54400   19.92800 1.000 29.87736  ? 326 ARG B CZ    1 
ATOM   1021 N  NH1   . ARG A 1 137 ? 26.79200 6.68400   19.10600 1.000 27.62424  ? 326 ARG B NH1   1 
ATOM   1022 N  NH2   . ARG A 1 137 ? 26.48300 8.84100   19.81200 1.000 28.07575  ? 326 ARG B NH2   1 
ATOM   1023 N  N     . THR A 1 138 ? 27.90100 3.76500   24.37800 1.000 40.42459  ? 327 THR B N     1 
ATOM   1024 C  CA    . THR A 1 138 ? 29.21200 3.21700   24.06400 1.000 37.18965  ? 327 THR B CA    1 
ATOM   1025 C  C     . THR A 1 138 ? 29.25900 2.49800   22.72400 1.000 35.46027  ? 327 THR B C     1 
ATOM   1026 O  O     . THR A 1 138 ? 30.35200 2.13200   22.27800 1.000 33.44525  ? 327 THR B O     1 
ATOM   1027 C  CB    . THR A 1 138 ? 29.67300 2.24000   25.15800 1.000 42.08842  ? 327 THR B CB    1 
ATOM   1028 O  OG1   . THR A 1 138 ? 29.19900 0.92100   24.85400 1.000 36.53678  ? 327 THR B OG1   1 
ATOM   1029 C  CG2   . THR A 1 138 ? 29.14200 2.66700   26.51800 1.000 40.55006  ? 327 THR B CG2   1 
ATOM   1030 N  N     . LEU A 1 139 ? 28.11400 2.28100   22.07700 1.000 34.18515  ? 328 LEU B N     1 
ATOM   1031 C  CA    . LEU A 1 139 ? 28.06100 1.57200   20.80800 1.000 34.08758  ? 328 LEU B CA    1 
ATOM   1032 C  C     . LEU A 1 139 ? 27.98000 2.56600   19.66200 1.000 35.64575  ? 328 LEU B C     1 
ATOM   1033 O  O     . LEU A 1 139 ? 27.07400 3.41400   19.65700 1.000 29.38245  ? 328 LEU B O     1 
ATOM   1034 C  CB    . LEU A 1 139 ? 26.86100 0.63300   20.77000 1.000 31.29072  ? 328 LEU B CB    1 
ATOM   1035 C  CG    . LEU A 1 139 ? 27.11200 -0.84100  21.09000 1.000 37.43688  ? 328 LEU B CG    1 
ATOM   1036 C  CD1   . LEU A 1 139 ? 27.83600 -0.99800  22.41700 1.000 40.37112  ? 328 LEU B CD1   1 
ATOM   1037 C  CD2   . LEU A 1 139 ? 25.79600 -1.60100  21.10000 1.000 39.99636  ? 328 LEU B CD2   1 
ATOM   1038 N  N     . PRO A 1 140 ? 28.89000 2.51600   18.69000 1.000 33.47546  ? 329 PRO B N     1 
ATOM   1039 C  CA    . PRO A 1 140 ? 28.72200 3.34500   17.48800 1.000 34.43148  ? 329 PRO B CA    1 
ATOM   1040 C  C     . PRO A 1 140 ? 27.53300 2.85700   16.67400 1.000 29.60865  ? 329 PRO B C     1 
ATOM   1041 O  O     . PRO A 1 140 ? 27.41800 1.66900   16.36600 1.000 34.28359  ? 329 PRO B O     1 
ATOM   1042 C  CB    . PRO A 1 140 ? 30.04400 3.15400   16.73600 1.000 37.35070  ? 329 PRO B CB    1 
ATOM   1043 C  CG    . PRO A 1 140 ? 30.54900 1.82800   17.20300 1.000 36.24630  ? 329 PRO B CG    1 
ATOM   1044 C  CD    . PRO A 1 140 ? 30.11700 1.70400   18.63800 1.000 34.48052  ? 329 PRO B CD    1 
ATOM   1045 N  N     . LEU A 1 141 ? 26.64300 3.78400   16.33300 1.000 26.72591  ? 330 LEU B N     1 
ATOM   1046 C  CA    . LEU A 1 141 ? 25.40800 3.46600   15.63500 1.000 27.42544  ? 330 LEU B CA    1 
ATOM   1047 C  C     . LEU A 1 141 ? 25.40700 4.11100   14.25600 1.000 28.64418  ? 330 LEU B C     1 
ATOM   1048 O  O     . LEU A 1 141 ? 26.17700 5.03400   13.97800 1.000 34.48201  ? 330 LEU B O     1 
ATOM   1049 C  CB    . LEU A 1 141 ? 24.18200 3.93200   16.43400 1.000 27.16822  ? 330 LEU B CB    1 
ATOM   1050 C  CG    . LEU A 1 141 ? 24.05900 3.40600   17.86700 1.000 29.01621  ? 330 LEU B CG    1 
ATOM   1051 C  CD1   . LEU A 1 141 ? 22.79800 3.93900   18.53000 1.000 26.48974  ? 330 LEU B CD1   1 
ATOM   1052 C  CD2   . LEU A 1 141 ? 24.07800 1.88600   17.89100 1.000 24.30255  ? 330 LEU B CD2   1 
ATOM   1053 N  N     . GLU A 1 142 ? 24.52900 3.61100   13.38900 1.000 26.17018  ? 331 GLU B N     1 
ATOM   1054 C  CA    . GLU A 1 142 ? 24.43500 4.08100   12.01300 1.000 26.95652  ? 331 GLU B CA    1 
ATOM   1055 C  C     . GLU A 1 142 ? 22.97500 4.29200   11.64800 1.000 30.86021  ? 331 GLU B C     1 
ATOM   1056 O  O     . GLU A 1 142 ? 22.16300 3.36800   11.76500 1.000 27.16892  ? 331 GLU B O     1 
ATOM   1057 C  CB    . GLU A 1 142 ? 25.09100 3.08900   11.04900 1.000 29.14163  ? 331 GLU B CB    1 
ATOM   1058 C  CG    . GLU A 1 142 ? 25.05900 3.52800   9.59400  1.000 32.37818  ? 331 GLU B CG    1 
ATOM   1059 C  CD    . GLU A 1 142 ? 25.92800 2.65900   8.70800  1.000 40.36890  ? 331 GLU B CD    1 
ATOM   1060 O  OE1   . GLU A 1 142 ? 27.15300 2.90100   8.64800  1.000 42.52658  ? 331 GLU B OE1   1 
ATOM   1061 O  OE2   . GLU A 1 142 ? 25.38300 1.73700   8.06300  1.000 45.96874  ? 331 GLU B OE2   1 
ATOM   1062 N  N     . ILE A 1 143 ? 22.64800 5.50000   11.19600 1.000 30.53518  ? 332 ILE B N     1 
ATOM   1063 C  CA    . ILE A 1 143 ? 21.31100 5.82400   10.71400 1.000 30.13410  ? 332 ILE B CA    1 
ATOM   1064 C  C     . ILE A 1 143 ? 21.23300 5.47600   9.23300  1.000 30.14524  ? 332 ILE B C     1 
ATOM   1065 O  O     . ILE A 1 143 ? 22.08200 5.90000   8.44000  1.000 33.46227  ? 332 ILE B O     1 
ATOM   1066 C  CB    . ILE A 1 143 ? 20.98400 7.30800   10.94900 1.000 27.66636  ? 332 ILE B CB    1 
ATOM   1067 C  CG1   . ILE A 1 143 ? 21.16700 7.66900   12.42500 1.000 26.20790  ? 332 ILE B CG1   1 
ATOM   1068 C  CG2   . ILE A 1 143 ? 19.56700 7.62000   10.49100 1.000 23.06766  ? 332 ILE B CG2   1 
ATOM   1069 C  CD1   . ILE A 1 143 ? 21.02700 9.14600   12.71400 1.000 25.77120  ? 332 ILE B CD1   1 
ATOM   1070 N  N     . PHE A 1 144 ? 20.21600 4.70300   8.85800  1.000 28.69648  ? 333 PHE B N     1 
ATOM   1071 C  CA    . PHE A 1 144 ? 20.06300 4.25400   7.48300  1.000 32.44174  ? 333 PHE B CA    1 
ATOM   1072 C  C     . PHE A 1 144 ? 18.59200 4.28200   7.09700  1.000 28.46345  ? 333 PHE B C     1 
ATOM   1073 O  O     . PHE A 1 144 ? 17.70100 4.24800   7.95000  1.000 25.24994  ? 333 PHE B O     1 
ATOM   1074 C  CB    . PHE A 1 144 ? 20.63700 2.84400   7.28300  1.000 37.29971  ? 333 PHE B CB    1 
ATOM   1075 C  CG    . PHE A 1 144 ? 19.78300 1.75500   7.86500  1.000 27.50251  ? 333 PHE B CG    1 
ATOM   1076 C  CD1   . PHE A 1 144 ? 19.71100 1.56900   9.23500  1.000 26.09647  ? 333 PHE B CD1   1 
ATOM   1077 C  CD2   . PHE A 1 144 ? 19.05800 0.91100   7.04100  1.000 28.03525  ? 333 PHE B CD2   1 
ATOM   1078 C  CE1   . PHE A 1 144 ? 18.92800 0.56700   9.77100  1.000 27.59882  ? 333 PHE B CE1   1 
ATOM   1079 C  CE2   . PHE A 1 144 ? 18.27200 -0.09300  7.57200  1.000 32.57290  ? 333 PHE B CE2   1 
ATOM   1080 C  CZ    . PHE A 1 144 ? 18.20700 -0.26500  8.93800  1.000 28.14047  ? 333 PHE B CZ    1 
ATOM   1081 N  N     . LYS A 1 145 ? 18.34800 4.34800   5.79100  1.000 28.20184  ? 334 LYS B N     1 
ATOM   1082 C  CA    . LYS A 1 145 ? 16.99500 4.31800   5.25200  1.000 36.58259  ? 334 LYS B CA    1 
ATOM   1083 C  C     . LYS A 1 145 ? 16.54700 2.87000   5.08700  1.000 35.20303  ? 334 LYS B C     1 
ATOM   1084 O  O     . LYS A 1 145 ? 17.29900 2.03800   4.57000  1.000 30.81607  ? 334 LYS B O     1 
ATOM   1085 C  CB    . LYS A 1 145 ? 16.93100 5.05300   3.91300  1.000 34.80016  ? 334 LYS B CB    1 
ATOM   1086 C  CG    . LYS A 1 145 ? 15.52600 5.43600   3.47700  1.000 37.29290  ? 334 LYS B CG    1 
ATOM   1087 C  CD    . LYS A 1 145 ? 15.11500 6.77600   4.06900  1.000 38.12351  ? 334 LYS B CD    1 
ATOM   1088 C  CE    . LYS A 1 145 ? 13.63600 7.05100   3.84600  1.000 37.92476  ? 334 LYS B CE    1 
ATOM   1089 N  NZ    . LYS A 1 145 ? 12.87000 7.05100   5.12400  1.000 46.89435  ? 334 LYS B NZ    1 
ATOM   1090 N  N     . THR A 1 146 ? 15.33000 2.57300   5.52900  1.000 42.16013  ? 335 THR B N     1 
ATOM   1091 C  CA    . THR A 1 146 ? 14.77300 1.23200   5.43400  1.000 36.31819  ? 335 THR B CA    1 
ATOM   1092 C  C     . THR A 1 146 ? 13.84600 1.12300   4.22600  1.000 34.67389  ? 335 THR B C     1 
ATOM   1093 O  O     . THR A 1 146 ? 13.56400 2.10300   3.53300  1.000 35.35945  ? 335 THR B O     1 
ATOM   1094 C  CB    . THR A 1 146 ? 14.02100 0.86200   6.71800  1.000 33.58718  ? 335 THR B CB    1 
ATOM   1095 O  OG1   . THR A 1 146 ? 12.84600 1.67200   6.84000  1.000 29.96909  ? 335 THR B OG1   1 
ATOM   1096 C  CG2   . THR A 1 146 ? 14.90600 1.08000   7.93300  1.000 27.53171  ? 335 THR B CG2   1 
ATOM   1097 N  N     . LYS A 1 147 ? 13.37600 -0.10100  3.97900  1.000 39.21110  ? 336 LYS B N     1 
ATOM   1098 C  CA    . LYS A 1 147 ? 12.48600 -0.38200  2.85700  1.000 45.45012  ? 336 LYS B CA    1 
ATOM   1099 C  C     . LYS A 1 147 ? 11.15100 0.34600   2.92800  1.000 39.36839  ? 336 LYS B C     1 
ATOM   1100 O  O     . LYS A 1 147 ? 10.83300 1.17200   2.06700  1.000 40.57762  ? 336 LYS B O     1 
ATOM   1101 C  CB    . LYS A 1 147 ? 12.18200 -1.88100  2.77900  1.000 43.50493  ? 336 LYS B CB    1 
ATOM   1102 C  CG    . LYS A 1 147 ? 13.26700 -2.72900  2.16300  1.000 43.02327  ? 336 LYS B CG    1 
ATOM   1103 C  CD    . LYS A 1 147 ? 12.88000 -3.16800  0.75800  1.000 44.15159  ? 336 LYS B CD    1 
ATOM   1104 C  CE    . LYS A 1 147 ? 11.76500 -4.19800  0.77800  1.000 44.05429  ? 336 LYS B CE    1 
ATOM   1105 N  NZ    . LYS A 1 147 ? 10.96100 -4.15200  -0.47500 1.000 47.91585  ? 336 LYS B NZ    1 
ATOM   1106 N  N     . GLU A 1 148 ? 10.37600 0.05200   3.97200  1.000 44.97631  ? 337 GLU B N     1 
ATOM   1107 C  CA    . GLU A 1 148 ? 8.98700  0.47100   4.05700  1.000 49.84101  ? 337 GLU B CA    1 
ATOM   1108 C  C     . GLU A 1 148 ? 8.74100  1.42800   5.21000  1.000 43.53194  ? 337 GLU B C     1 
ATOM   1109 O  O     . GLU A 1 148 ? 7.73300  2.14100   5.19400  1.000 55.23266  ? 337 GLU B O     1 
ATOM   1110 C  CB    . GLU A 1 148 ? 8.05300  -0.74000  4.19600  1.000 56.74267  ? 337 GLU B CB    1 
ATOM   1111 C  CG    . GLU A 1 148 ? 8.40300  -1.87300  3.23900  1.000 55.28803  ? 337 GLU B CG    1 
ATOM   1112 C  CD    . GLU A 1 148 ? 7.93600  -3.22800  3.73100  1.000 63.92257  ? 337 GLU B CD    1 
ATOM   1113 O  OE1   . GLU A 1 148 ? 6.71000  -3.44700  3.80500  1.000 77.56404  ? 337 GLU B OE1   1 
ATOM   1114 O  OE2   . GLU A 1 148 ? 8.79900  -4.07300  4.05200  1.000 68.33405  ? 337 GLU B OE2   1 
ATOM   1115 N  N     . LYS A 1 149 ? 9.62300  1.45700   6.20000  1.000 47.13239  ? 338 LYS B N     1 
ATOM   1116 C  CA    . LYS A 1 149 ? 9.56300  2.44800   7.25900  1.000 47.74491  ? 338 LYS B CA    1 
ATOM   1117 C  C     . LYS A 1 149 ? 10.38700 3.66300   6.83700  1.000 44.62102  ? 338 LYS B C     1 
ATOM   1118 O  O     . LYS A 1 149 ? 10.88600 3.74100   5.71100  1.000 47.68965  ? 338 LYS B O     1 
ATOM   1119 C  CB    . LYS A 1 149 ? 10.04700 1.84800   8.57600  1.000 39.28697  ? 338 LYS B CB    1 
ATOM   1120 C  CG    . LYS A 1 149 ? 9.25600  0.63100   9.02400  1.000 38.68626  ? 338 LYS B CG    1 
ATOM   1121 C  CD    . LYS A 1 149 ? 10.09700 -0.63200  8.98600  1.000 38.01728  ? 338 LYS B CD    1 
ATOM   1122 C  CE    . LYS A 1 149 ? 11.28100 -0.53100  9.93400  1.000 29.20012  ? 338 LYS B CE    1 
ATOM   1123 N  NZ    . LYS A 1 149 ? 12.03800 -1.81100  10.02600 1.000 29.05895  ? 338 LYS B NZ    1 
ATOM   1124 N  N     . GLY A 1 150 ? 10.54000 4.62600   7.73800  1.000 36.88341  ? 339 GLY B N     1 
ATOM   1125 C  CA    . GLY A 1 150 ? 11.36900 5.77600   7.44600  1.000 43.48624  ? 339 GLY B CA    1 
ATOM   1126 C  C     . GLY A 1 150 ? 12.81800 5.44600   7.73300  1.000 39.89802  ? 339 GLY B C     1 
ATOM   1127 O  O     . GLY A 1 150 ? 13.29900 4.36800   7.37100  1.000 37.31018  ? 339 GLY B O     1 
ATOM   1128 N  N     . TRP A 1 151 ? 13.52600 6.36800   8.37400  1.000 32.65346  ? 340 TRP B N     1 
ATOM   1129 C  CA    . TRP A 1 151 ? 14.88800 6.09500   8.79300  1.000 35.17978  ? 340 TRP B CA    1 
ATOM   1130 C  C     . TRP A 1 151 ? 14.93900 5.08600   9.93700  1.000 32.00925  ? 340 TRP B C     1 
ATOM   1131 O  O     . TRP A 1 151 ? 13.95500 4.85600   10.64700 1.000 24.62194  ? 340 TRP B O     1 
ATOM   1132 C  CB    . TRP A 1 151 ? 15.58900 7.39400   9.19300  1.000 37.89884  ? 340 TRP B CB    1 
ATOM   1133 C  CG    . TRP A 1 151 ? 15.68200 8.37900   8.06700  1.000 36.48725  ? 340 TRP B CG    1 
ATOM   1134 C  CD1   . TRP A 1 151 ? 14.76900 9.33900   7.74000  1.000 34.06405  ? 340 TRP B CD1   1 
ATOM   1135 C  CD2   . TRP A 1 151 ? 16.74500 8.49400   7.11300  1.000 34.74557  ? 340 TRP B CD2   1 
ATOM   1136 N  NE1   . TRP A 1 151 ? 15.20000 10.04800  6.64400  1.000 32.81467  ? 340 TRP B NE1   1 
ATOM   1137 C  CE2   . TRP A 1 151 ? 16.41100 9.54800   6.24000  1.000 30.87394  ? 340 TRP B CE2   1 
ATOM   1138 C  CE3   . TRP A 1 151 ? 17.94900 7.81000   6.91500  1.000 30.43091  ? 340 TRP B CE3   1 
ATOM   1139 C  CZ2   . TRP A 1 151 ? 17.23500 9.93400   5.18400  1.000 30.83874  ? 340 TRP B CZ2   1 
ATOM   1140 C  CZ3   . TRP A 1 151 ? 18.76700 8.19500   5.86600  1.000 32.53856  ? 340 TRP B CZ3   1 
ATOM   1141 C  CH2   . TRP A 1 151 ? 18.40600 9.24700   5.01500  1.000 35.24067  ? 340 TRP B CH2   1 
ATOM   1142 N  N     . GLY A 1 152 ? 16.11000 4.47100   10.10300 1.000 31.04426  ? 341 GLY B N     1 
ATOM   1143 C  CA    . GLY A 1 152 ? 16.31800 3.49800   11.15600 1.000 24.71411  ? 341 GLY B CA    1 
ATOM   1144 C  C     . GLY A 1 152 ? 17.75800 3.52900   11.61500 1.000 26.53105  ? 341 GLY B C     1 
ATOM   1145 O  O     . GLY A 1 152 ? 18.61800 4.15600   10.99300 1.000 28.88624  ? 341 GLY B O     1 
ATOM   1146 N  N     . VAL A 1 153 ? 18.01400 2.84200   12.72600 1.000 21.93284  ? 342 VAL B N     1 
ATOM   1147 C  CA    . VAL A 1 153 ? 19.34100 2.79000   13.32700 1.000 24.50509  ? 342 VAL B CA    1 
ATOM   1148 C  C     . VAL A 1 153 ? 19.74700 1.33400   13.49000 1.000 26.85834  ? 342 VAL B C     1 
ATOM   1149 O  O     . VAL A 1 153 ? 18.95800 0.51400   13.97500 1.000 28.69093  ? 342 VAL B O     1 
ATOM   1150 C  CB    . VAL A 1 153 ? 19.38900 3.51700   14.68500 1.000 25.19691  ? 342 VAL B CB    1 
ATOM   1151 C  CG1   . VAL A 1 153 ? 20.76400 3.36900   15.31700 1.000 23.93718  ? 342 VAL B CG1   1 
ATOM   1152 C  CG2   . VAL A 1 153 ? 19.04600 4.97900   14.51300 1.000 25.38945  ? 342 VAL B CG2   1 
ATOM   1153 N  N     . ARG A 1 154 ? 20.97200 1.01400   13.08300 1.000 25.20988  ? 343 ARG B N     1 
ATOM   1154 C  CA    . ARG A 1 154 ? 21.53800 -0.31200  13.26500 1.000 29.32776  ? 343 ARG B CA    1 
ATOM   1155 C  C     . ARG A 1 154 ? 22.89000 -0.19100  13.95200 1.000 30.88225  ? 343 ARG B C     1 
ATOM   1156 O  O     . ARG A 1 154 ? 23.60100 0.80500   13.79000 1.000 23.60824  ? 343 ARG B O     1 
ATOM   1157 C  CB    . ARG A 1 154 ? 21.68300 -1.05100  11.92800 1.000 29.43451  ? 343 ARG B CB    1 
ATOM   1158 C  CG    . ARG A 1 154 ? 22.50300 -0.31000  10.89100 1.000 29.92466  ? 343 ARG B CG    1 
ATOM   1159 C  CD    . ARG A 1 154 ? 22.31000 -0.91800  9.51400  1.000 30.07125  ? 343 ARG B CD    1 
ATOM   1160 N  NE    . ARG A 1 154 ? 23.03100 -0.17600  8.48700  1.000 35.19301  ? 343 ARG B NE    1 
ATOM   1161 C  CZ    . ARG A 1 154 ? 22.87000 -0.35500  7.18300  1.000 39.47949  ? 343 ARG B CZ    1 
ATOM   1162 N  NH1   . ARG A 1 154 ? 22.01100 -1.24300  6.70800  1.000 39.45141  ? 343 ARG B NH1   1 
ATOM   1163 N  NH2   . ARG A 1 154 ? 23.58600 0.37700   6.33500  1.000 42.67749  ? 343 ARG B NH2   1 
ATOM   1164 N  N     . SER A 1 155 ? 23.22900 -1.21000  14.73600 1.000 27.53108  ? 344 SER B N     1 
ATOM   1165 C  CA    . SER A 1 155 ? 24.50100 -1.23900  15.44000 1.000 28.15063  ? 344 SER B CA    1 
ATOM   1166 C  C     . SER A 1 155 ? 25.60400 -1.75600  14.52700 1.000 29.34596  ? 344 SER B C     1 
ATOM   1167 O  O     . SER A 1 155 ? 25.38600 -2.65400  13.70900 1.000 28.84459  ? 344 SER B O     1 
ATOM   1168 C  CB    . SER A 1 155 ? 24.40300 -2.11900  16.68600 1.000 31.38269  ? 344 SER B CB    1 
ATOM   1169 O  OG    . SER A 1 155 ? 25.68300 -2.34300  17.25200 1.000 37.71697  ? 344 SER B OG    1 
ATOM   1170 N  N     . LEU A 1 156 ? 26.79500 -1.18000  14.67100 1.000 33.09397  ? 345 LEU B N     1 
ATOM   1171 C  CA    . LEU A 1 156 ? 27.96100 -1.61600  13.91600 1.000 32.58662  ? 345 LEU B CA    1 
ATOM   1172 C  C     . LEU A 1 156 ? 28.81200 -2.63200  14.67000 1.000 30.64257  ? 345 LEU B C     1 
ATOM   1173 O  O     . LEU A 1 156 ? 29.78200 -3.14500  14.10300 1.000 39.23684  ? 345 LEU B O     1 
ATOM   1174 C  CB    . LEU A 1 156 ? 28.81700 -0.40500  13.53300 1.000 31.24758  ? 345 LEU B CB    1 
ATOM   1175 C  CG    . LEU A 1 156 ? 28.08100 0.68400   12.74700 1.000 36.25815  ? 345 LEU B CG    1 
ATOM   1176 C  CD1   . LEU A 1 156 ? 28.98800 1.87600   12.48600 1.000 35.46486  ? 345 LEU B CD1   1 
ATOM   1177 C  CD2   . LEU A 1 156 ? 27.53400 0.12800   11.44100 1.000 28.43711  ? 345 LEU B CD2   1 
ATOM   1178 N  N     . ARG A 1 157 ? 28.47000 -2.94000  15.92000 1.000 38.09608  ? 346 ARG B N     1 
ATOM   1179 C  CA    . ARG A 1 157 ? 29.20900 -3.89600  16.73300 1.000 38.86955  ? 346 ARG B CA    1 
ATOM   1180 C  C     . ARG A 1 157 ? 28.23500 -4.89200  17.34700 1.000 35.53112  ? 346 ARG B C     1 
ATOM   1181 O  O     . ARG A 1 157 ? 27.02400 -4.65800  17.39300 1.000 33.87133  ? 346 ARG B O     1 
ATOM   1182 C  CB    . ARG A 1 157 ? 30.00900 -3.20200  17.84800 1.000 35.94159  ? 346 ARG B CB    1 
ATOM   1183 C  CG    . ARG A 1 157 ? 30.80600 -1.99200  17.39300 1.000 39.36262  ? 346 ARG B CG    1 
ATOM   1184 C  CD    . ARG A 1 157 ? 31.89800 -2.37700  16.41000 1.000 48.65077  ? 346 ARG B CD    1 
ATOM   1185 N  NE    . ARG A 1 157 ? 32.15500 -1.30800  15.45300 1.000 56.97732  ? 346 ARG B NE    1 
ATOM   1186 C  CZ    . ARG A 1 157 ? 33.00200 -0.30800  15.65300 1.000 56.76211  ? 346 ARG B CZ    1 
ATOM   1187 N  NH1   . ARG A 1 157 ? 33.71100 -0.21400  16.76600 1.000 68.45576  ? 346 ARG B NH1   1 
ATOM   1188 N  NH2   . ARG A 1 157 ? 33.13800 0.62400   14.71400 1.000 56.53619  ? 346 ARG B NH2   1 
ATOM   1189 N  N     . PHE A 1 158 ? 28.77500 -6.01400  17.81600 1.000 36.60406  ? 347 PHE B N     1 
ATOM   1190 C  CA    . PHE A 1 158 ? 27.94800 -7.00200  18.49500 1.000 38.23249  ? 347 PHE B CA    1 
ATOM   1191 C  C     . PHE A 1 158 ? 27.43600 -6.43600  19.81300 1.000 32.19222  ? 347 PHE B C     1 
ATOM   1192 O  O     . PHE A 1 158 ? 28.19000 -5.82600  20.57700 1.000 40.05390  ? 347 PHE B O     1 
ATOM   1193 C  CB    . PHE A 1 158 ? 28.73400 -8.29000  18.73900 1.000 42.98464  ? 347 PHE B CB    1 
ATOM   1194 C  CG    . PHE A 1 158 ? 27.98400 -9.31200  19.55100 1.000 52.03080  ? 347 PHE B CG    1 
ATOM   1195 C  CD1   . PHE A 1 158 ? 26.67200 -9.62900  19.24900 1.000 46.90174  ? 347 PHE B CD1   1 
ATOM   1196 C  CD2   . PHE A 1 158 ? 28.58700 -9.94800  20.62300 1.000 52.65833  ? 347 PHE B CD2   1 
ATOM   1197 C  CE1   . PHE A 1 158 ? 25.97400 -10.56100 19.99000 1.000 44.43879  ? 347 PHE B CE1   1 
ATOM   1198 C  CE2   . PHE A 1 158 ? 27.89600 -10.88800 21.36600 1.000 48.37869  ? 347 PHE B CE2   1 
ATOM   1199 C  CZ    . PHE A 1 158 ? 26.58500 -11.19300 21.05000 1.000 41.03170  ? 347 PHE B CZ    1 
ATOM   1200 N  N     . ALA A 1 159 ? 26.14500 -6.63900  20.07700 1.000 37.32743  ? 348 ALA B N     1 
ATOM   1201 C  CA    . ALA A 1 159 ? 25.48300 -6.14200  21.28100 1.000 37.76679  ? 348 ALA B CA    1 
ATOM   1202 C  C     . ALA A 1 159 ? 24.83300 -7.31700  21.99900 1.000 37.07420  ? 348 ALA B C     1 
ATOM   1203 O  O     . ALA A 1 159 ? 23.67500 -7.66600  21.71700 1.000 32.20005  ? 348 ALA B O     1 
ATOM   1204 C  CB    . ALA A 1 159 ? 24.45300 -5.06600  20.94000 1.000 32.87308  ? 348 ALA B CB    1 
ATOM   1205 N  N     . PRO A 1 160 ? 25.53700 -7.95800  22.92800 1.000 38.25225  ? 349 PRO B N     1 
ATOM   1206 C  CA    . PRO A 1 160 ? 24.93400 -9.05900  23.68300 1.000 35.93298  ? 349 PRO B CA    1 
ATOM   1207 C  C     . PRO A 1 160 ? 23.78700 -8.56700  24.55100 1.000 28.58963  ? 349 PRO B C     1 
ATOM   1208 O  O     . PRO A 1 160 ? 23.68600 -7.38600  24.88900 1.000 32.29977  ? 349 PRO B O     1 
ATOM   1209 C  CB    . PRO A 1 160 ? 26.09200 -9.58600  24.53600 1.000 31.21507  ? 349 PRO B CB    1 
ATOM   1210 C  CG    . PRO A 1 160 ? 27.02700 -8.42800  24.65300 1.000 38.72252  ? 349 PRO B CG    1 
ATOM   1211 C  CD    . PRO A 1 160 ? 26.92300 -7.69100  23.34800 1.000 31.52698  ? 349 PRO B CD    1 
ATOM   1212 N  N     . ALA A 1 161 ? 22.90400 -9.50200  24.89700 1.000 26.81956  ? 350 ALA B N     1 
ATOM   1213 C  CA    . ALA A 1 161 ? 21.73200 -9.16900  25.69600 1.000 30.48403  ? 350 ALA B CA    1 
ATOM   1214 C  C     . ALA A 1 161 ? 22.14700 -8.50500  27.00300 1.000 23.03100  ? 350 ALA B C     1 
ATOM   1215 O  O     . ALA A 1 161 ? 23.06900 -8.96300  27.68500 1.000 24.28485  ? 350 ALA B O     1 
ATOM   1216 C  CB    . ALA A 1 161 ? 20.91000 -10.42600 25.97500 1.000 26.49239  ? 350 ALA B CB    1 
ATOM   1217 N  N     . GLY A 1 162 ? 21.46800 -7.41200  27.34300 1.000 27.52947  ? 351 GLY B N     1 
ATOM   1218 C  CA    . GLY A 1 162 ? 21.79300 -6.62600  28.51200 1.000 27.21679  ? 351 GLY B CA    1 
ATOM   1219 C  C     . GLY A 1 162 ? 22.64000 -5.39900  28.24100 1.000 29.22173  ? 351 GLY B C     1 
ATOM   1220 O  O     . GLY A 1 162 ? 22.85000 -4.59900  29.16100 1.000 27.24538  ? 351 GLY B O     1 
ATOM   1221 N  N     . THR A 1 163 ? 23.12800 -5.22600  27.01400 1.000 29.56540  ? 352 THR B N     1 
ATOM   1222 C  CA    . THR A 1 163 ? 23.97500 -4.08400  26.69600 1.000 31.35770  ? 352 THR B CA    1 
ATOM   1223 C  C     . THR A 1 163 ? 23.14600 -2.80700  26.62500 1.000 23.32540  ? 352 THR B C     1 
ATOM   1224 O  O     . THR A 1 163 ? 22.10600 -2.76300  25.96000 1.000 18.21626  ? 352 THR B O     1 
ATOM   1225 C  CB    . THR A 1 163 ? 24.70100 -4.31100  25.37000 1.000 29.31630  ? 352 THR B CB    1 
ATOM   1226 O  OG1   . THR A 1 163 ? 25.45900 -5.52600  25.43600 1.000 27.04273  ? 352 THR B OG1   1 
ATOM   1227 C  CG2   . THR A 1 163 ? 25.64000 -3.15100  25.06700 1.000 27.89259  ? 352 THR B CG2   1 
ATOM   1228 N  N     . PHE A 1 164 ? 23.60800 -1.76700  27.31400 1.000 22.42496  ? 353 PHE B N     1 
ATOM   1229 C  CA    . PHE A 1 164 ? 22.96200 -0.46500  27.22300 1.000 24.46983  ? 353 PHE B CA    1 
ATOM   1230 C  C     . PHE A 1 164 ? 23.24600 0.26400   25.91600 1.000 21.01410  ? 353 PHE B C     1 
ATOM   1231 O  O     . PHE A 1 164 ? 24.40100 0.42400   25.51500 1.000 29.91878  ? 353 PHE B O     1 
ATOM   1232 C  CB    . PHE A 1 164 ? 23.46500 0.45600   28.33400 1.000 22.50512  ? 353 PHE B CB    1 
ATOM   1233 C  CG    . PHE A 1 164 ? 22.94900 1.86000   28.23400 1.000 21.21293  ? 353 PHE B CG    1 
ATOM   1234 C  CD1   . PHE A 1 164 ? 21.59800 2.12700   28.38300 1.000 20.16013  ? 353 PHE B CD1   1 
ATOM   1235 C  CD2   . PHE A 1 164 ? 23.81400 2.91500   27.99700 1.000 26.38034  ? 353 PHE B CD2   1 
ATOM   1236 C  CE1   . PHE A 1 164 ? 21.11900 3.41900   28.29100 1.000 20.61958  ? 353 PHE B CE1   1 
ATOM   1237 C  CE2   . PHE A 1 164 ? 23.33900 4.21100   27.90400 1.000 27.17025  ? 353 PHE B CE2   1 
ATOM   1238 C  CZ    . PHE A 1 164 ? 21.99000 4.46200   28.05300 1.000 21.15142  ? 353 PHE B CZ    1 
ATOM   1239 N  N     . ILE A 1 165 ? 22.18200 0.70800   25.24800 1.000 19.25876  ? 354 ILE B N     1 
ATOM   1240 C  CA    . ILE A 1 165 ? 22.34100 1.40400   23.97500 1.000 27.37418  ? 354 ILE B CA    1 
ATOM   1241 C  C     . ILE A 1 165 ? 22.37500 2.92000   24.12000 1.000 23.49984  ? 354 ILE B C     1 
ATOM   1242 O  O     . ILE A 1 165 ? 23.41000 3.55000   23.86900 1.000 21.97816  ? 354 ILE B O     1 
ATOM   1243 C  CB    . ILE A 1 165 ? 21.20800 0.97000   23.02800 1.000 27.49011  ? 354 ILE B CB    1 
ATOM   1244 C  CG1   . ILE A 1 165 ? 21.21800 -0.54700  22.83900 1.000 25.34846  ? 354 ILE B CG1   1 
ATOM   1245 C  CG2   . ILE A 1 165 ? 21.33100 1.67600   21.68800 1.000 26.11692  ? 354 ILE B CG2   1 
ATOM   1246 C  CD1   . ILE A 1 165 ? 19.98400 -1.22400  23.37200 1.000 23.30772  ? 354 ILE B CD1   1 
ATOM   1247 N  N     . THR A 1 166 ? 21.26100 3.50300   24.55300 1.000 24.26681  ? 355 THR B N     1 
ATOM   1248 C  CA    . THR A 1 166 ? 21.10300 4.95200   24.64300 1.000 23.91695  ? 355 THR B CA    1 
ATOM   1249 C  C     . THR A 1 166 ? 19.73600 5.24400   25.25100 1.000 24.79402  ? 355 THR B C     1 
ATOM   1250 O  O     . THR A 1 166 ? 18.91000 4.34400   25.43600 1.000 21.34094  ? 355 THR B O     1 
ATOM   1251 C  CB    . THR A 1 166 ? 21.16400 5.61800   23.26500 1.000 26.43138  ? 355 THR B CB    1 
ATOM   1252 O  OG1   . THR A 1 166 ? 21.10600 7.04100   23.41900 1.000 31.87023  ? 355 THR B OG1   1 
ATOM   1253 C  CG2   . THR A 1 166 ? 19.99500 5.16000   22.40400 1.000 22.96764  ? 355 THR B CG2   1 
ATOM   1254 N  N     . CYS A 1 167 ? 19.50200 6.51800   25.55000 1.000 23.25402  ? 356 CYS B N     1 
ATOM   1255 C  CA    . CYS A 1 167 ? 18.24000 6.98800   26.10200 1.000 23.17572  ? 356 CYS B CA    1 
ATOM   1256 C  C     . CYS A 1 167 ? 17.39100 7.70600   25.06200 1.000 24.09120  ? 356 CYS B C     1 
ATOM   1257 O  O     . CYS A 1 167 ? 17.90700 8.24600   24.08000 1.000 28.09594  ? 356 CYS B O     1 
ATOM   1258 C  CB    . CYS A 1 167 ? 18.50400 7.93000   27.28100 1.000 20.49065  ? 356 CYS B CB    1 
ATOM   1259 S  SG    . CYS A 1 167 ? 19.07900 7.11100   28.77400 1.000 31.81577  ? 356 CYS B SG    1 
ATOM   1260 N  N     . TYR A 1 168 ? 16.07900 7.70500   25.28400 1.000 18.29941  ? 357 TYR B N     1 
ATOM   1261 C  CA    . TYR A 1 168 ? 15.15300 8.44500   24.42900 1.000 22.13311  ? 357 TYR B CA    1 
ATOM   1262 C  C     . TYR A 1 168 ? 15.03600 9.85800   24.98400 1.000 22.85058  ? 357 TYR B C     1 
ATOM   1263 O  O     . TYR A 1 168 ? 14.38900 10.08600  26.00700 1.000 24.28009  ? 357 TYR B O     1 
ATOM   1264 C  CB    . TYR A 1 168 ? 13.79800 7.75300   24.35400 1.000 21.45319  ? 357 TYR B CB    1 
ATOM   1265 C  CG    . TYR A 1 168 ? 12.92100 8.28800   23.24500 1.000 24.97576  ? 357 TYR B CG    1 
ATOM   1266 C  CD1   . TYR A 1 168 ? 13.00700 7.77300   21.95700 1.000 23.44229  ? 357 TYR B CD1   1 
ATOM   1267 C  CD2   . TYR A 1 168 ? 12.01600 9.31500   23.48000 1.000 20.83066  ? 357 TYR B CD2   1 
ATOM   1268 C  CE1   . TYR A 1 168 ? 12.21400 8.26100   20.93700 1.000 25.58397  ? 357 TYR B CE1   1 
ATOM   1269 C  CE2   . TYR A 1 168 ? 11.21800 9.80900   22.46500 1.000 24.05895  ? 357 TYR B CE2   1 
ATOM   1270 C  CZ    . TYR A 1 168 ? 11.32000 9.27800   21.19600 1.000 26.56772  ? 357 TYR B CZ    1 
ATOM   1271 O  OH    . TYR A 1 168 ? 10.52700 9.76600   20.18100 1.000 21.46302  ? 357 TYR B OH    1 
ATOM   1272 N  N     . LEU A 1 169 ? 15.66700 10.81100  24.30900 1.000 22.43592  ? 358 LEU B N     1 
ATOM   1273 C  CA    . LEU A 1 169 ? 15.68900 12.19500  24.74600 1.000 25.88502  ? 358 LEU B CA    1 
ATOM   1274 C  C     . LEU A 1 169 ? 14.71900 13.02400  23.90600 1.000 25.73416  ? 358 LEU B C     1 
ATOM   1275 O  O     . LEU A 1 169 ? 14.07700 12.53200  22.97500 1.000 21.60958  ? 358 LEU B O     1 
ATOM   1276 C  CB    . LEU A 1 169 ? 17.11100 12.75700  24.66300 1.000 28.26000  ? 358 LEU B CB    1 
ATOM   1277 C  CG    . LEU A 1 169 ? 18.18000 12.01500  25.46700 1.000 25.51997  ? 358 LEU B CG    1 
ATOM   1278 C  CD1   . LEU A 1 169 ? 19.54900 12.61900  25.21900 1.000 26.75197  ? 358 LEU B CD1   1 
ATOM   1279 C  CD2   . LEU A 1 169 ? 17.84900 12.03500  26.95100 1.000 25.27560  ? 358 LEU B CD2   1 
ATOM   1280 N  N     . GLY A 1 170 ? 14.61700 14.29900  24.24200 1.000 27.08751  ? 359 GLY B N     1 
ATOM   1281 C  CA    . GLY A 1 170 ? 13.76400 15.22000  23.53100 1.000 24.56604  ? 359 GLY B CA    1 
ATOM   1282 C  C     . GLY A 1 170 ? 13.16900 16.23200  24.48000 1.000 25.43074  ? 359 GLY B C     1 
ATOM   1283 O  O     . GLY A 1 170 ? 13.55700 16.33100  25.64400 1.000 25.40195  ? 359 GLY B O     1 
ATOM   1284 N  N     . GLU A 1 171 ? 12.21900 17.00500  23.96400 1.000 27.39454  ? 360 GLU B N     1 
ATOM   1285 C  CA    . GLU A 1 171 ? 11.49700 17.95200  24.79800 1.000 24.02557  ? 360 GLU B CA    1 
ATOM   1286 C  C     . GLU A 1 171 ? 10.56900 17.21500  25.75400 1.000 23.91894  ? 360 GLU B C     1 
ATOM   1287 O  O     . GLU A 1 171 ? 9.93700  16.22100  25.38800 1.000 21.48168  ? 360 GLU B O     1 
ATOM   1288 C  CB    . GLU A 1 171 ? 10.69200 18.92000  23.93200 1.000 24.15752  ? 360 GLU B CB    1 
ATOM   1289 C  CG    . GLU A 1 171 ? 11.53200 19.93000  23.17500 1.000 29.71981  ? 360 GLU B CG    1 
ATOM   1290 C  CD    . GLU A 1 171 ? 10.70400 20.77500  22.22800 1.000 32.13040  ? 360 GLU B CD    1 
ATOM   1291 O  OE1   . GLU A 1 171 ? 10.12700 20.20900  21.27500 1.000 32.42616  ? 360 GLU B OE1   1 
ATOM   1292 O  OE2   . GLU A 1 171 ? 10.62300 22.00400  22.44200 1.000 39.17926  ? 360 GLU B OE2   1 
ATOM   1293 N  N     . VAL A 1 172 ? 10.49200 17.70600  26.98600 1.000 28.94747  ? 361 VAL B N     1 
ATOM   1294 C  CA    . VAL A 1 172 ? 9.54700  17.20600  27.97700 1.000 26.93521  ? 361 VAL B CA    1 
ATOM   1295 C  C     . VAL A 1 172 ? 8.38800  18.19000  28.04300 1.000 25.38066  ? 361 VAL B C     1 
ATOM   1296 O  O     . VAL A 1 172 ? 8.58600  19.37500  28.33600 1.000 25.03782  ? 361 VAL B O     1 
ATOM   1297 C  CB    . VAL A 1 172 ? 10.21000 17.02800  29.35200 1.000 28.37555  ? 361 VAL B CB    1 
ATOM   1298 C  CG1   . VAL A 1 172 ? 9.20300  16.49200  30.35700 1.000 27.77094  ? 361 VAL B CG1   1 
ATOM   1299 C  CG2   . VAL A 1 172 ? 11.40600 16.09400  29.24600 1.000 21.73663  ? 361 VAL B CG2   1 
ATOM   1300 N  N     . ILE A 1 173 ? 7.17900  17.70200  27.76500 1.000 29.04901  ? 362 ILE B N     1 
ATOM   1301 C  CA    . ILE A 1 173 ? 6.00600  18.55300  27.62300 1.000 27.24911  ? 362 ILE B CA    1 
ATOM   1302 C  C     . ILE A 1 173 ? 4.87400  18.00300  28.47900 1.000 29.95687  ? 362 ILE B C     1 
ATOM   1303 O  O     . ILE A 1 173 ? 4.88700  16.84700  28.90700 1.000 27.37152  ? 362 ILE B O     1 
ATOM   1304 C  CB    . ILE A 1 173 ? 5.55200  18.67600  26.15200 1.000 26.27598  ? 362 ILE B CB    1 
ATOM   1305 C  CG1   . ILE A 1 173 ? 5.20900  17.29800  25.58400 1.000 24.84571  ? 362 ILE B CG1   1 
ATOM   1306 C  CG2   . ILE A 1 173 ? 6.63000  19.35200  25.31500 1.000 27.33578  ? 362 ILE B CG2   1 
ATOM   1307 C  CD1   . ILE A 1 173 ? 4.80800  17.31800  24.12600 1.000 33.80896  ? 362 ILE B CD1   1 
ATOM   1308 N  N     . THR A 1 174 ? 3.88400  18.85800  28.72100 1.000 36.49203  ? 363 THR B N     1 
ATOM   1309 C  CA    . THR A 1 174 ? 2.73500  18.50900  29.53900 1.000 39.31682  ? 363 THR B CA    1 
ATOM   1310 C  C     . THR A 1 174 ? 1.67300  17.79500  28.70500 1.000 37.33622  ? 363 THR B C     1 
ATOM   1311 O  O     . THR A 1 174 ? 1.78400  17.66100  27.48300 1.000 35.89173  ? 363 THR B O     1 
ATOM   1312 C  CB    . THR A 1 174 ? 2.14300  19.75800  30.18800 1.000 38.48560  ? 363 THR B CB    1 
ATOM   1313 O  OG1   . THR A 1 174 ? 1.83000  20.71900  29.17200 1.000 41.13531  ? 363 THR B OG1   1 
ATOM   1314 C  CG2   . THR A 1 174 ? 3.13400  20.37000  31.17000 1.000 36.32012  ? 363 THR B CG2   1 
ATOM   1315 N  N     . SER A 1 175 ? 0.62400  17.33300  29.39100 1.000 37.68354  ? 364 SER B N     1 
ATOM   1316 C  CA    . SER A 1 175 ? -0.46500 16.64000  28.70700 1.000 41.26307  ? 364 SER B CA    1 
ATOM   1317 C  C     . SER A 1 175 ? -1.17500 17.56200  27.72400 1.000 41.81867  ? 364 SER B C     1 
ATOM   1318 O  O     . SER A 1 175 ? -1.53800 17.14100  26.61900 1.000 42.14459  ? 364 SER B O     1 
ATOM   1319 C  CB    . SER A 1 175 ? -1.45500 16.08000  29.72800 1.000 42.97540  ? 364 SER B CB    1 
ATOM   1320 O  OG    . SER A 1 175 ? -0.83300 15.13000  30.57500 1.000 51.66701  ? 364 SER B OG    1 
ATOM   1321 N  N     . ALA A 1 176 ? -1.39100 18.82100  28.11200 1.000 40.55941  ? 365 ALA B N     1 
ATOM   1322 C  CA    . ALA A 1 176 ? -2.02600 19.77400  27.20800 1.000 47.12696  ? 365 ALA B CA    1 
ATOM   1323 C  C     . ALA A 1 176 ? -1.17900 20.00200  25.96200 1.000 45.83597  ? 365 ALA B C     1 
ATOM   1324 O  O     . ALA A 1 176 ? -1.70600 20.05600  24.84500 1.000 49.02169  ? 365 ALA B O     1 
ATOM   1325 C  CB    . ALA A 1 176 ? -2.28100 21.09500  27.93300 1.000 45.25140  ? 365 ALA B CB    1 
ATOM   1326 N  N     . GLU A 1 177 ? 0.13800  20.13900  26.13300 1.000 51.47836  ? 366 GLU B N     1 
ATOM   1327 C  CA    . GLU A 1 177 ? 1.01300  20.33000  24.98100 1.000 47.45180  ? 366 GLU B CA    1 
ATOM   1328 C  C     . GLU A 1 177 ? 1.12700  19.05300  24.15700 1.000 42.20223  ? 366 GLU B C     1 
ATOM   1329 O  O     . GLU A 1 177 ? 1.21700  19.10900  22.92500 1.000 43.49690  ? 366 GLU B O     1 
ATOM   1330 C  CB    . GLU A 1 177 ? 2.39300  20.80600  25.44000 1.000 36.62250  ? 366 GLU B CB    1 
ATOM   1331 C  CG    . GLU A 1 177 ? 3.33800  21.17700  24.30400 1.000 45.17392  ? 366 GLU B CG    1 
ATOM   1332 C  CD    . GLU A 1 177 ? 2.87800  22.39400  23.51700 1.000 56.92917  ? 366 GLU B CD    1 
ATOM   1333 O  OE1   . GLU A 1 177 ? 2.08200  23.19600  24.05200 1.000 57.13817  ? 366 GLU B OE1   1 
ATOM   1334 O  OE2   . GLU A 1 177 ? 3.31700  22.54900  22.35800 1.000 56.11807  ? 366 GLU B OE2   1 
ATOM   1335 N  N     . ALA A 1 178 ? 1.12600  17.89200  24.81900 1.000 40.44981  ? 367 ALA B N     1 
ATOM   1336 C  CA    . ALA A 1 178 ? 1.18200  16.62700  24.09000 1.000 43.01878  ? 367 ALA B CA    1 
ATOM   1337 C  C     . ALA A 1 178 ? -0.04000 16.44900  23.19800 1.000 44.50231  ? 367 ALA B C     1 
ATOM   1338 O  O     . ALA A 1 178 ? 0.07900  16.01100  22.04800 1.000 48.21624  ? 367 ALA B O     1 
ATOM   1339 C  CB    . ALA A 1 178 ? 1.30700  15.45900  25.06800 1.000 42.81926  ? 367 ALA B CB    1 
ATOM   1340 N  N     . ALA A 1 179 ? -1.22600 16.78200  23.71300 1.000 47.42096  ? 368 ALA B N     1 
ATOM   1341 C  CA    . ALA A 1 179 ? -2.42600 16.75000  22.88300 1.000 48.30700  ? 368 ALA B CA    1 
ATOM   1342 C  C     . ALA A 1 179 ? -2.36200 17.80300  21.78400 1.000 50.96761  ? 368 ALA B C     1 
ATOM   1343 O  O     . ALA A 1 179 ? -2.78900 17.55400  20.65000 1.000 54.34410  ? 368 ALA B O     1 
ATOM   1344 C  CB    . ALA A 1 179 ? -3.67000 16.94700  23.74700 1.000 42.61520  ? 368 ALA B CB    1 
ATOM   1345 N  N     . LYS A 1 180 ? -1.83400 18.98800  22.10200 1.000 47.92614  ? 369 LYS B N     1 
ATOM   1346 C  CA    . LYS A 1 180 ? -1.71800 20.04100  21.10000 1.000 49.13759  ? 369 LYS B CA    1 
ATOM   1347 C  C     . LYS A 1 180 ? -0.72300 19.66800  20.00900 1.000 53.14525  ? 369 LYS B C     1 
ATOM   1348 O  O     . LYS A 1 180 ? -0.83100 20.15900  18.88000 1.000 56.72765  ? 369 LYS B O     1 
ATOM   1349 C  CB    . LYS A 1 180 ? -1.31800 21.35600  21.76800 1.000 54.89189  ? 369 LYS B CB    1 
ATOM   1350 C  CG    . LYS A 1 180 ? -2.38900 22.43400  21.70500 1.000 69.03336  ? 369 LYS B CG    1 
ATOM   1351 C  CD    . LYS A 1 180 ? -1.98400 23.66600  22.50400 1.000 68.79790  ? 369 LYS B CD    1 
ATOM   1352 C  CE    . LYS A 1 180 ? -2.78200 23.77500  23.79600 1.000 75.98717  ? 369 LYS B CE    1 
ATOM   1353 N  NZ    . LYS A 1 180 ? -2.15000 24.70400  24.77400 1.000 59.88268  ? 369 LYS B NZ    1 
ATOM   1354 N  N     . ARG A 1 181 ? 0.25300  18.81700  20.32200 1.000 49.42046  ? 370 ARG B N     1 
ATOM   1355 C  CA    . ARG A 1 181 ? 1.18300  18.30700  19.32600 1.000 52.60302  ? 370 ARG B CA    1 
ATOM   1356 C  C     . ARG A 1 181 ? 0.80200  16.93400  18.79000 1.000 56.92497  ? 370 ARG B C     1 
ATOM   1357 O  O     . ARG A 1 181 ? 1.49500  16.42100  17.90600 1.000 58.70793  ? 370 ARG B O     1 
ATOM   1358 C  CB    . ARG A 1 181 ? 2.59100  18.18500  19.92100 1.000 41.68465  ? 370 ARG B CB    1 
ATOM   1359 C  CG    . ARG A 1 181 ? 3.18100  19.49000  20.41300 1.000 39.31200  ? 370 ARG B CG    1 
ATOM   1360 C  CD    . ARG A 1 181 ? 4.62200  19.29900  20.84300 1.000 32.25433  ? 370 ARG B CD    1 
ATOM   1361 N  NE    . ARG A 1 181 ? 5.20800  20.52600  21.36600 1.000 40.55315  ? 370 ARG B NE    1 
ATOM   1362 C  CZ    . ARG A 1 181 ? 6.49900  20.68700  21.62300 1.000 35.23233  ? 370 ARG B CZ    1 
ATOM   1363 N  NH1   . ARG A 1 181 ? 7.37300  19.71900  21.39800 1.000 31.39290  ? 370 ARG B NH1   1 
ATOM   1364 N  NH2   . ARG A 1 181 ? 6.92300  21.84800  22.11300 1.000 39.14933  ? 370 ARG B NH2   1 
ATOM   1365 N  N     . ASP A 1 182 ? -0.23600 16.33500  19.34400 1.000 54.04615  ? 371 ASP B N     1 
ATOM   1366 C  CA    . ASP A 1 182 ? -0.71400 15.06900  18.85000 1.000 58.01106  ? 371 ASP B CA    1 
ATOM   1367 C  C     . ASP A 1 182 ? -1.24000 15.37300  17.48300 1.000 64.26272  ? 371 ASP B C     1 
ATOM   1368 O  O     . ASP A 1 182 ? -1.76500 14.48700  16.82700 1.000 69.57658  ? 371 ASP B O     1 
ATOM   1369 C  CB    . ASP A 1 182 ? -1.80200 14.52500  19.75000 1.000 56.51244  ? 371 ASP B CB    1 
ATOM   1370 C  CG    . ASP A 1 182 ? -1.43900 13.21200  20.38000 1.000 59.32259  ? 371 ASP B CG    1 
ATOM   1371 O  OD1   . ASP A 1 182 ? -0.80200 12.37900  19.70400 1.000 66.37125  ? 371 ASP B OD1   1 
ATOM   1372 O  OD2   . ASP A 1 182 ? -1.80900 13.00900  21.55000 1.000 57.68682  ? 371 ASP B OD2   1 
ATOM   1373 N  N     . LYS A 1 183 ? -1.14400 16.62500  17.06200 1.000 63.82493  ? 372 LYS B N     1 
ATOM   1374 C  CA    . LYS A 1 183 ? -1.51700 17.04200  15.71000 1.000 66.93209  ? 372 LYS B CA    1 
ATOM   1375 C  C     . LYS A 1 183 ? -3.02700 17.28800  15.78300 1.000 60.28491  ? 372 LYS B C     1 
ATOM   1376 O  O     . LYS A 1 183 ? -3.55700 17.66400  16.82600 1.000 55.65154  ? 372 LYS B O     1 
ATOM   1377 C  CB    . LYS A 1 183 ? -1.15000 16.07000  14.58200 1.000 71.66724  ? 372 LYS B CB    1 
ATOM   1378 C  CG    . LYS A 1 183 ? 0.28100  15.56200  14.66600 1.000 74.47795  ? 372 LYS B CG    1 
ATOM   1379 C  CD    . LYS A 1 183 ? 0.42200  14.18100  14.05500 1.000 78.57789  ? 372 LYS B CD    1 
ATOM   1380 C  CE    . LYS A 1 183 ? 1.41600  13.33700  14.83300 1.000 76.08122  ? 372 LYS B CE    1 
ATOM   1381 N  NZ    . LYS A 1 183 ? 1.06900  11.89000  14.79100 1.000 72.55897  ? 372 LYS B NZ    1 
ATOM   1382 N  N     . ASP A 1 186 ? 0.28300  19.29000  11.14300 1.000 110.67106 ? 375 ASP B N     1 
ATOM   1383 C  CA    . ASP A 1 186 ? 0.73400  18.27400  10.19700 1.000 113.77145 ? 375 ASP B CA    1 
ATOM   1384 C  C     . ASP A 1 186 ? 0.55200  16.86400  10.74700 1.000 118.36916 ? 375 ASP B C     1 
ATOM   1385 O  O     . ASP A 1 186 ? 0.71200  16.62300  11.94900 1.000 107.86524 ? 375 ASP B O     1 
ATOM   1386 C  CB    . ASP A 1 186 ? 2.19700  18.51100  9.80600  1.000 115.73141 ? 375 ASP B CB    1 
ATOM   1387 C  CG    . ASP A 1 186 ? 2.55200  17.89400  8.46900  1.000 121.52966 ? 375 ASP B CG    1 
ATOM   1388 O  OD1   . ASP A 1 186 ? 1.90800  16.89900  8.07600  1.000 118.98151 ? 375 ASP B OD1   1 
ATOM   1389 O  OD2   . ASP A 1 186 ? 3.47700  18.41000  7.80700  1.000 129.81291 ? 375 ASP B OD2   1 
ATOM   1390 N  N     . ASP A 1 187 ? 0.20700  15.92800  9.86600  1.000 116.74582 ? 376 ASP B N     1 
ATOM   1391 C  CA    . ASP A 1 187 ? 0.11600  14.51900  10.22000 1.000 107.54620 ? 376 ASP B CA    1 
ATOM   1392 C  C     . ASP A 1 187 ? 0.43300  13.68400  8.99100  1.000 102.17639 ? 376 ASP B C     1 
ATOM   1393 O  O     . ASP A 1 187 ? -0.19400 13.85800  7.94100  1.000 91.72905  ? 376 ASP B O     1 
ATOM   1394 C  CB    . ASP A 1 187 ? -1.27100 14.15400  10.75400 1.000 102.83577 ? 376 ASP B CB    1 
ATOM   1395 C  CG    . ASP A 1 187 ? -1.51300 12.65900  10.74600 1.000 101.33480 ? 376 ASP B CG    1 
ATOM   1396 O  OD1   . ASP A 1 187 ? -0.88000 11.94800  11.55400 1.000 93.06677  ? 376 ASP B OD1   1 
ATOM   1397 O  OD2   . ASP A 1 187 ? -2.33500 12.19500  9.92700  1.000 103.06065 ? 376 ASP B OD2   1 
ATOM   1398 N  N     . ASP A 1 188 ? 1.40500  12.78200  9.12700  1.000 105.11154 ? 377 ASP B N     1 
ATOM   1399 C  CA    . ASP A 1 188 ? 1.79700  11.89300  8.04200  1.000 91.73801  ? 377 ASP B CA    1 
ATOM   1400 C  C     . ASP A 1 188 ? 2.08400  10.48700  8.55600  1.000 74.64245  ? 377 ASP B C     1 
ATOM   1401 O  O     . ASP A 1 188 ? 2.85100  9.74100   7.93800  1.000 64.67117  ? 377 ASP B O     1 
ATOM   1402 C  CB    . ASP A 1 188 ? 3.01500  12.44400  7.29900  1.000 91.26419  ? 377 ASP B CB    1 
ATOM   1403 C  CG    . ASP A 1 188 ? 3.99200  13.14400  8.22600  1.000 95.26662  ? 377 ASP B CG    1 
ATOM   1404 O  OD1   . ASP A 1 188 ? 3.70600  13.23700  9.43800  1.000 89.98186  ? 377 ASP B OD1   1 
ATOM   1405 O  OD2   . ASP A 1 188 ? 5.04700  13.60300  7.73900  1.000 99.57880  ? 377 ASP B OD2   1 
ATOM   1406 N  N     . GLY A 1 189 ? 1.48200  10.11200  9.68200  1.000 70.31598  ? 378 GLY B N     1 
ATOM   1407 C  CA    . GLY A 1 189 ? 1.77400  8.83700   10.30000 1.000 64.72128  ? 378 GLY B CA    1 
ATOM   1408 C  C     . GLY A 1 189 ? 3.09500  8.77800   11.02900 1.000 62.15245  ? 378 GLY B C     1 
ATOM   1409 O  O     . GLY A 1 189 ? 3.52700  7.68300   11.40900 1.000 58.78560  ? 378 GLY B O     1 
ATOM   1410 N  N     . ILE A 1 190 ? 3.75300  9.91500   11.23600 1.000 58.88746  ? 379 ILE B N     1 
ATOM   1411 C  CA    . ILE A 1 190 ? 5.04900  9.97700   11.90100 1.000 45.71680  ? 379 ILE B CA    1 
ATOM   1412 C  C     . ILE A 1 190 ? 4.86100  10.69800  13.22700 1.000 45.74519  ? 379 ILE B C     1 
ATOM   1413 O  O     . ILE A 1 190 ? 4.36700  11.83200  13.26100 1.000 50.79814  ? 379 ILE B O     1 
ATOM   1414 C  CB    . ILE A 1 190 ? 6.10000  10.68200  11.03200 1.000 47.91434  ? 379 ILE B CB    1 
ATOM   1415 C  CG1   . ILE A 1 190 ? 6.11200  10.09600  9.62000  1.000 56.09715  ? 379 ILE B CG1   1 
ATOM   1416 C  CG2   . ILE A 1 190 ? 7.47800  10.55100  11.65500 1.000 47.65674  ? 379 ILE B CG2   1 
ATOM   1417 C  CD1   . ILE A 1 190 ? 7.17400  10.69800  8.72500  1.000 55.24874  ? 379 ILE B CD1   1 
ATOM   1418 N  N     . THR A 1 191 ? 5.24600  10.04000  14.31800 1.000 44.41549  ? 380 THR B N     1 
ATOM   1419 C  CA    . THR A 1 191 ? 5.18300  10.63900  15.64200 1.000 36.79307  ? 380 THR B CA    1 
ATOM   1420 C  C     . THR A 1 191 ? 6.46100  10.31600  16.40400 1.000 34.51590  ? 380 THR B C     1 
ATOM   1421 O  O     . THR A 1 191 ? 7.06700  9.25800   16.21600 1.000 29.36705  ? 380 THR B O     1 
ATOM   1422 C  CB    . THR A 1 191 ? 3.96000  10.15400  16.43900 1.000 37.38188  ? 380 THR B CB    1 
ATOM   1423 O  OG1   . THR A 1 191 ? 3.95300  10.77200  17.73200 1.000 27.31342  ? 380 THR B OG1   1 
ATOM   1424 C  CG2   . THR A 1 191 ? 3.98300  8.63900   16.60300 1.000 35.70097  ? 380 THR B CG2   1 
ATOM   1425 N  N     . TYR A 1 192 ? 6.86900  11.25300  17.25900 1.000 29.94007  ? 381 TYR B N     1 
ATOM   1426 C  CA    . TYR A 1 192 ? 8.03700  11.08200  18.11500 1.000 28.63871  ? 381 TYR B CA    1 
ATOM   1427 C  C     . TYR A 1 192 ? 7.68300  11.24500  19.58800 1.000 27.26072  ? 381 TYR B C     1 
ATOM   1428 O  O     . TYR A 1 192 ? 8.57400  11.43900  20.42100 1.000 24.12356  ? 381 TYR B O     1 
ATOM   1429 C  CB    . TYR A 1 192 ? 9.14200  12.06600  17.72100 1.000 31.35224  ? 381 TYR B CB    1 
ATOM   1430 C  CG    . TYR A 1 192 ? 9.59600  11.93600  16.28400 1.000 31.70319  ? 381 TYR B CG    1 
ATOM   1431 C  CD1   . TYR A 1 192 ? 10.46700 10.92500  15.90000 1.000 26.97238  ? 381 TYR B CD1   1 
ATOM   1432 C  CD2   . TYR A 1 192 ? 9.16000  12.82700  15.31400 1.000 33.44705  ? 381 TYR B CD2   1 
ATOM   1433 C  CE1   . TYR A 1 192 ? 10.88700 10.80400  14.58900 1.000 31.22276  ? 381 TYR B CE1   1 
ATOM   1434 C  CE2   . TYR A 1 192 ? 9.57400  12.71500  14.00200 1.000 34.25405  ? 381 TYR B CE2   1 
ATOM   1435 C  CZ    . TYR A 1 192 ? 10.43700 11.70100  13.64500 1.000 37.37163  ? 381 TYR B CZ    1 
ATOM   1436 O  OH    . TYR A 1 192 ? 10.85200 11.58500  12.33800 1.000 45.92594  ? 381 TYR B OH    1 
ATOM   1437 N  N     . LEU A 1 193 ? 6.39600  11.16900  19.92100 1.000 25.18599  ? 382 LEU B N     1 
ATOM   1438 C  CA    . LEU A 1 193 ? 5.94900  11.33200  21.29700 1.000 26.87065  ? 382 LEU B CA    1 
ATOM   1439 C  C     . LEU A 1 193 ? 6.11600  10.02800  22.06600 1.000 26.11520  ? 382 LEU B C     1 
ATOM   1440 O  O     . LEU A 1 193 ? 5.75000  8.95400   21.57700 1.000 21.45059  ? 382 LEU B O     1 
ATOM   1441 C  CB    . LEU A 1 193 ? 4.49000  11.78000  21.33000 1.000 27.02816  ? 382 LEU B CB    1 
ATOM   1442 C  CG    . LEU A 1 193 ? 4.14900  13.14200  20.72800 1.000 30.56590  ? 382 LEU B CG    1 
ATOM   1443 C  CD1   . LEU A 1 193 ? 2.64500  13.35400  20.71800 1.000 36.93802  ? 382 LEU B CD1   1 
ATOM   1444 C  CD2   . LEU A 1 193 ? 4.83900  14.24400  21.50700 1.000 27.45994  ? 382 LEU B CD2   1 
ATOM   1445 N  N     . PHE A 1 194 ? 6.66100  10.12900  23.27700 1.000 25.30029  ? 383 PHE B N     1 
ATOM   1446 C  CA    . PHE A 1 194 ? 6.91500  8.98100   24.14300 1.000 24.32596  ? 383 PHE B CA    1 
ATOM   1447 C  C     . PHE A 1 194 ? 6.38300  9.32800   25.52600 1.000 23.59756  ? 383 PHE B C     1 
ATOM   1448 O  O     . PHE A 1 194 ? 6.94100  10.19300  26.20900 1.000 24.16395  ? 383 PHE B O     1 
ATOM   1449 C  CB    . PHE A 1 194 ? 8.40900  8.65200   24.18700 1.000 22.29150  ? 383 PHE B CB    1 
ATOM   1450 C  CG    . PHE A 1 194 ? 8.72300  7.24000   24.61300 1.000 24.84337  ? 383 PHE B CG    1 
ATOM   1451 C  CD1   . PHE A 1 194 ? 8.09900  6.66400   25.70700 1.000 21.88154  ? 383 PHE B CD1   1 
ATOM   1452 C  CD2   . PHE A 1 194 ? 9.65600  6.49200   23.91500 1.000 27.43893  ? 383 PHE B CD2   1 
ATOM   1453 C  CE1   . PHE A 1 194 ? 8.39700  5.37100   26.09400 1.000 30.04862  ? 383 PHE B CE1   1 
ATOM   1454 C  CE2   . PHE A 1 194 ? 9.95800  5.19800   24.29600 1.000 25.58917  ? 383 PHE B CE2   1 
ATOM   1455 C  CZ    . PHE A 1 194 ? 9.32800  4.63700   25.38600 1.000 26.02210  ? 383 PHE B CZ    1 
ATOM   1456 N  N     . ASP A 1 195 ? 5.30600  8.66200   25.93600 1.000 22.77077  ? 384 ASP B N     1 
ATOM   1457 C  CA    . ASP A 1 195 ? 4.70800  8.94200   27.23400 1.000 27.64643  ? 384 ASP B CA    1 
ATOM   1458 C  C     . ASP A 1 195 ? 5.61100  8.47100   28.36700 1.000 30.86540  ? 384 ASP B C     1 
ATOM   1459 O  O     . ASP A 1 195 ? 6.17500  7.37400   28.32300 1.000 30.92841  ? 384 ASP B O     1 
ATOM   1460 C  CB    . ASP A 1 195 ? 3.33900  8.27100   27.34900 1.000 29.01863  ? 384 ASP B CB    1 
ATOM   1461 C  CG    . ASP A 1 195 ? 2.23600  9.08200   26.69800 1.000 34.30298  ? 384 ASP B CG    1 
ATOM   1462 O  OD1   . ASP A 1 195 ? 2.40000  10.31400  26.56500 1.000 31.61580  ? 384 ASP B OD1   1 
ATOM   1463 O  OD2   . ASP A 1 195 ? 1.20200  8.48800   26.32600 1.000 40.41736  ? 384 ASP B OD2   1 
ATOM   1464 N  N     . LEU A 1 196 ? 5.74800  9.31800   29.38700 1.000 27.32664  ? 385 LEU B N     1 
ATOM   1465 C  CA    . LEU A 1 196 ? 6.42800  8.94400   30.62700 1.000 29.90588  ? 385 LEU B CA    1 
ATOM   1466 C  C     . LEU A 1 196 ? 5.39300  8.31900   31.55700 1.000 30.21587  ? 385 LEU B C     1 
ATOM   1467 O  O     . LEU A 1 196 ? 4.92400  8.92700   32.52200 1.000 32.31451  ? 385 LEU B O     1 
ATOM   1468 C  CB    . LEU A 1 196 ? 7.10300  10.15500  31.25800 1.000 26.98636  ? 385 LEU B CB    1 
ATOM   1469 C  CG    . LEU A 1 196 ? 8.37200  10.65900  30.57200 1.000 32.02160  ? 385 LEU B CG    1 
ATOM   1470 C  CD1   . LEU A 1 196 ? 8.85300  11.94900  31.21600 1.000 29.91414  ? 385 LEU B CD1   1 
ATOM   1471 C  CD2   . LEU A 1 196 ? 9.45200  9.59500   30.63200 1.000 22.84695  ? 385 LEU B CD2   1 
ATOM   1472 N  N     . ASP A 1 197 ? 5.03200  7.07000   31.25300 1.000 28.58489  ? 386 ASP B N     1 
ATOM   1473 C  CA    . ASP A 1 197 ? 3.93600  6.39400   31.93900 1.000 31.27844  ? 386 ASP B CA    1 
ATOM   1474 C  C     . ASP A 1 197 ? 4.38800  5.15300   32.70100 1.000 34.79158  ? 386 ASP B C     1 
ATOM   1475 O  O     . ASP A 1 197 ? 3.55700  4.29400   33.01500 1.000 40.93174  ? 386 ASP B O     1 
ATOM   1476 C  CB    . ASP A 1 197 ? 2.83200  6.02900   30.94400 1.000 29.07686  ? 386 ASP B CB    1 
ATOM   1477 C  CG    . ASP A 1 197 ? 3.34900  5.24100   29.75200 1.000 32.91624  ? 386 ASP B CG    1 
ATOM   1478 O  OD1   . ASP A 1 197 ? 4.56600  4.96200   29.69200 1.000 32.40855  ? 386 ASP B OD1   1 
ATOM   1479 O  OD2   . ASP A 1 197 ? 2.53300  4.90200   28.87000 1.000 31.42324  ? 386 ASP B OD2   1 
ATOM   1480 N  N     . MET A 1 198 ? 5.68200  5.04100   33.01800 1.000 26.97564  ? 387 MET B N     1 
ATOM   1481 C  CA    . MET A 1 198 ? 6.15900  3.86400   33.74000 1.000 39.08275  ? 387 MET B CA    1 
ATOM   1482 C  C     . MET A 1 198 ? 5.47600  3.73700   35.09600 1.000 47.53573  ? 387 MET B C     1 
ATOM   1483 O  O     . MET A 1 198 ? 5.07800  2.63700   35.49900 1.000 46.99191  ? 387 MET B O     1 
ATOM   1484 C  CB    . MET A 1 198 ? 7.67600  3.91900   33.91400 1.000 35.22024  ? 387 MET B CB    1 
ATOM   1485 C  CG    . MET A 1 198 ? 8.24300  2.76800   34.73700 1.000 41.96159  ? 387 MET B CG    1 
ATOM   1486 S  SD    . MET A 1 198 ? 8.14600  1.17700   33.89600 1.000 42.87101  ? 387 MET B SD    1 
ATOM   1487 C  CE    . MET A 1 198 ? 9.52000  1.31500   32.75200 1.000 38.25008  ? 387 MET B CE    1 
ATOM   1488 N  N     . PHE A 1 199 ? 5.32300  4.84800   35.80700 1.000 44.53431  ? 388 PHE B N     1 
ATOM   1489 C  CA    . PHE A 1 199 ? 4.65700  4.86200   37.10200 1.000 46.65282  ? 388 PHE B CA    1 
ATOM   1490 C  C     . PHE A 1 199 ? 3.26500  5.45600   36.93200 1.000 55.38616  ? 388 PHE B C     1 
ATOM   1491 O  O     . PHE A 1 199 ? 3.12400  6.60200   36.49100 1.000 55.65563  ? 388 PHE B O     1 
ATOM   1492 C  CB    . PHE A 1 199 ? 5.46800  5.66000   38.12100 1.000 46.90379  ? 388 PHE B CB    1 
ATOM   1493 C  CG    . PHE A 1 199 ? 6.91700  5.27500   38.17100 1.000 42.37362  ? 388 PHE B CG    1 
ATOM   1494 C  CD1   . PHE A 1 199 ? 7.83500  5.87200   37.32500 1.000 37.53970  ? 388 PHE B CD1   1 
ATOM   1495 C  CD2   . PHE A 1 199 ? 7.36200  4.31900   39.06700 1.000 42.86339  ? 388 PHE B CD2   1 
ATOM   1496 C  CE1   . PHE A 1 199 ? 9.17000  5.52100   37.37000 1.000 39.46861  ? 388 PHE B CE1   1 
ATOM   1497 C  CE2   . PHE A 1 199 ? 8.69500  3.96200   39.11700 1.000 42.64455  ? 388 PHE B CE2   1 
ATOM   1498 C  CZ    . PHE A 1 199 ? 9.60000  4.56400   38.26600 1.000 42.52448  ? 388 PHE B CZ    1 
ATOM   1499 N  N     . ASP A 1 200 ? 2.24200  4.67700   37.27900 1.000 67.35486  ? 389 ASP B N     1 
ATOM   1500 C  CA    . ASP A 1 200 ? 0.87000  5.14200   37.13300 1.000 66.54372  ? 389 ASP B CA    1 
ATOM   1501 C  C     . ASP A 1 200 ? 0.47600  6.14400   38.20900 1.000 72.94156  ? 389 ASP B C     1 
ATOM   1502 O  O     . ASP A 1 200 ? -0.49400 6.88500   38.02000 1.000 77.56017  ? 389 ASP B O     1 
ATOM   1503 C  CB    . ASP A 1 200 ? -0.09400 3.95700   37.15300 1.000 69.34817  ? 389 ASP B CB    1 
ATOM   1504 C  CG    . ASP A 1 200 ? -1.22700 4.12000   36.16800 1.000 76.48073  ? 389 ASP B CG    1 
ATOM   1505 O  OD1   . ASP A 1 200 ? -1.67800 5.26900   35.97500 1.000 78.62161  ? 389 ASP B OD1   1 
ATOM   1506 O  OD2   . ASP A 1 200 ? -1.66100 3.10600   35.58300 1.000 76.22482  ? 389 ASP B OD2   1 
ATOM   1507 N  N     . ASP A 1 201 ? 1.17200  6.23300   39.30800 1.000 79.41929  ? 390 ASP B N     1 
ATOM   1508 C  CA    . ASP A 1 201 ? 0.77000  7.25200   40.25400 1.000 81.86060  ? 390 ASP B CA    1 
ATOM   1509 C  C     . ASP A 1 201 ? 1.15800  8.63200   39.74700 1.000 84.59380  ? 390 ASP B C     1 
ATOM   1510 O  O     . ASP A 1 201 ? 0.55300  9.62000   40.13900 1.000 83.52671  ? 390 ASP B O     1 
ATOM   1511 C  CB    . ASP A 1 201 ? 1.36600  7.00500   41.62900 1.000 85.01886  ? 390 ASP B CB    1 
ATOM   1512 C  CG    . ASP A 1 201 ? 2.85300  7.02200   41.61000 1.000 98.83078  ? 390 ASP B CG    1 
ATOM   1513 O  OD1   . ASP A 1 201 ? 3.42200  7.15200   40.50500 1.000 91.77198  ? 390 ASP B OD1   1 
ATOM   1514 O  OD2   . ASP A 1 201 ? 3.45900  6.90700   42.69600 1.000 105.34546 ? 390 ASP B OD2   1 
ATOM   1515 N  N     . ALA A 1 202 ? 2.15900  8.71300   38.88400 1.000 68.85545  ? 391 ALA B N     1 
ATOM   1516 C  CA    . ALA A 1 202 ? 2.50300  10.01500  38.31000 1.000 54.25670  ? 391 ALA B CA    1 
ATOM   1517 C  C     . ALA A 1 202 ? 2.88700  9.79000   36.84600 1.000 51.70651  ? 391 ALA B C     1 
ATOM   1518 O  O     . ALA A 1 202 ? 4.04200  9.49600   36.53000 1.000 50.11382  ? 391 ALA B O     1 
ATOM   1519 C  CB    . ALA A 1 202 ? 3.62300  10.68400  39.09100 1.000 53.34530  ? 391 ALA B CB    1 
ATOM   1520 N  N     . SER A 1 203 ? 1.90200  9.94400   35.96000 1.000 48.42465  ? 392 SER B N     1 
ATOM   1521 C  CA    . SER A 1 203 ? 2.09200  9.83800   34.51300 1.000 41.18669  ? 392 SER B CA    1 
ATOM   1522 C  C     . SER A 1 203 ? 1.52200  11.11600  33.90400 1.000 41.18971  ? 392 SER B C     1 
ATOM   1523 O  O     . SER A 1 203 ? 0.34700  11.16600  33.53200 1.000 46.48628  ? 392 SER B O     1 
ATOM   1524 C  CB    . SER A 1 203 ? 1.41900  8.58800   33.95400 1.000 45.34847  ? 392 SER B CB    1 
ATOM   1525 O  OG    . SER A 1 203 ? 1.53300  8.53600   32.54300 1.000 49.89952  ? 392 SER B OG    1 
ATOM   1526 N  N     . GLU A 1 204 ? 2.35700  12.14700  33.80800 1.000 39.35160  ? 393 GLU B N     1 
ATOM   1527 C  CA    . GLU A 1 204 ? 1.90600  13.47600  33.41900 1.000 41.32575  ? 393 GLU B CA    1 
ATOM   1528 C  C     . GLU A 1 204 ? 2.61500  14.04300  32.20200 1.000 35.05530  ? 393 GLU B C     1 
ATOM   1529 O  O     . GLU A 1 204 ? 1.99500  14.79000  31.44200 1.000 37.22431  ? 393 GLU B O     1 
ATOM   1530 C  CB    . GLU A 1 204 ? 2.08900  14.46000  34.58600 1.000 41.98147  ? 393 GLU B CB    1 
ATOM   1531 C  CG    . GLU A 1 204 ? 2.12400  13.80200  35.95400 1.000 54.36808  ? 393 GLU B CG    1 
ATOM   1532 C  CD    . GLU A 1 204 ? 2.17000  14.81100  37.08400 1.000 65.24110  ? 393 GLU B CD    1 
ATOM   1533 O  OE1   . GLU A 1 204 ? 1.66500  15.93800  36.89800 1.000 68.22410  ? 393 GLU B OE1   1 
ATOM   1534 O  OE2   . GLU A 1 204 ? 2.71400  14.47800  38.15700 1.000 72.33079  ? 393 GLU B OE2   1 
ATOM   1535 N  N     . TYR A 1 205 ? 3.88800  13.71800  31.99600 1.000 32.52100  ? 394 TYR B N     1 
ATOM   1536 C  CA    . TYR A 1 205 ? 4.70100  14.33800  30.96400 1.000 29.80559  ? 394 TYR B CA    1 
ATOM   1537 C  C     . TYR A 1 205 ? 4.94600  13.37500  29.80800 1.000 32.34858  ? 394 TYR B C     1 
ATOM   1538 O  O     . TYR A 1 205 ? 4.80200  12.15600  29.93600 1.000 25.82873  ? 394 TYR B O     1 
ATOM   1539 C  CB    . TYR A 1 205 ? 6.03900  14.81200  31.54100 1.000 28.30867  ? 394 TYR B CB    1 
ATOM   1540 C  CG    . TYR A 1 205 ? 5.89800  15.75500  32.71400 1.000 30.68949  ? 394 TYR B CG    1 
ATOM   1541 C  CD1   . TYR A 1 205 ? 4.92700  16.75000  32.72000 1.000 32.88915  ? 394 TYR B CD1   1 
ATOM   1542 C  CD2   . TYR A 1 205 ? 6.72800  15.64400  33.82000 1.000 31.54128  ? 394 TYR B CD2   1 
ATOM   1543 C  CE1   . TYR A 1 205 ? 4.79400  17.61200  33.79400 1.000 34.84809  ? 394 TYR B CE1   1 
ATOM   1544 C  CE2   . TYR A 1 205 ? 6.60300  16.50000  34.89700 1.000 36.73836  ? 394 TYR B CE2   1 
ATOM   1545 C  CZ    . TYR A 1 205 ? 5.63500  17.48100  34.88000 1.000 34.70783  ? 394 TYR B CZ    1 
ATOM   1546 O  OH    . TYR A 1 205 ? 5.51200  18.33200  35.95300 1.000 38.90728  ? 394 TYR B OH    1 
ATOM   1547 N  N     . THR A 1 206 ? 5.32400  13.95200  28.66900 1.000 31.24917  ? 395 THR B N     1 
ATOM   1548 C  CA    . THR A 1 206 ? 5.61700  13.21300  27.45100 1.000 25.62375  ? 395 THR B CA    1 
ATOM   1549 C  C     . THR A 1 206 ? 6.91300  13.74100  26.85400 1.000 25.55746  ? 395 THR B C     1 
ATOM   1550 O  O     . THR A 1 206 ? 7.18300  14.94500  26.90500 1.000 25.76040  ? 395 THR B O     1 
ATOM   1551 C  CB    . THR A 1 206 ? 4.46600  13.34400  26.43400 1.000 25.57434  ? 395 THR B CB    1 
ATOM   1552 O  OG1   . THR A 1 206 ? 3.25600  12.83700  27.01000 1.000 27.31043  ? 395 THR B OG1   1 
ATOM   1553 C  CG2   . THR A 1 206 ? 4.77200  12.57400  25.15600 1.000 26.53425  ? 395 THR B CG2   1 
ATOM   1554 N  N     . VAL A 1 207 ? 7.71800  12.84100  26.30000 1.000 23.32083  ? 396 VAL B N     1 
ATOM   1555 C  CA    . VAL A 1 207 ? 8.95300  13.21700  25.62300 1.000 23.70514  ? 396 VAL B CA    1 
ATOM   1556 C  C     . VAL A 1 207 ? 8.65800  13.35300  24.13500 1.000 19.62774  ? 396 VAL B C     1 
ATOM   1557 O  O     . VAL A 1 207 ? 8.15500  12.41700  23.50500 1.000 21.77137  ? 396 VAL B O     1 
ATOM   1558 C  CB    . VAL A 1 207 ? 10.06700 12.19000  25.87400 1.000 25.15656  ? 396 VAL B CB    1 
ATOM   1559 C  CG1   . VAL A 1 207 ? 11.32800 12.58500  25.11700 1.000 25.18118  ? 396 VAL B CG1   1 
ATOM   1560 C  CG2   . VAL A 1 207 ? 10.35300 12.06600  27.36400 1.000 19.67227  ? 396 VAL B CG2   1 
ATOM   1561 N  N     . ASP A 1 208 ? 8.96000  14.52300  23.57500 1.000 21.82285  ? 397 ASP B N     1 
ATOM   1562 C  CA    . ASP A 1 208 ? 8.74200  14.81100  22.16000 1.000 25.39948  ? 397 ASP B CA    1 
ATOM   1563 C  C     . ASP A 1 208 ? 10.10100 14.94200  21.48400 1.000 25.38387  ? 397 ASP B C     1 
ATOM   1564 O  O     . ASP A 1 208 ? 10.86100 15.87000  21.78200 1.000 22.73181  ? 397 ASP B O     1 
ATOM   1565 C  CB    . ASP A 1 208 ? 7.91300  16.08200  21.98300 1.000 23.36414  ? 397 ASP B CB    1 
ATOM   1566 C  CG    . ASP A 1 208 ? 7.53000  16.33300  20.53600 1.000 28.79346  ? 397 ASP B CG    1 
ATOM   1567 O  OD1   . ASP A 1 208 ? 7.64100  15.39700  19.71400 1.000 31.91990  ? 397 ASP B OD1   1 
ATOM   1568 O  OD2   . ASP A 1 208 ? 7.12100  17.46800  20.21700 1.000 30.65638  ? 397 ASP B OD2   1 
ATOM   1569 N  N     . ALA A 1 209 ? 10.39900 14.02300  20.56500 1.000 19.45211  ? 398 ALA B N     1 
ATOM   1570 C  CA    . ALA A 1 209 ? 11.68000 13.99600  19.87200 1.000 24.12316  ? 398 ALA B CA    1 
ATOM   1571 C  C     . ALA A 1 209 ? 11.60900 14.61900  18.48100 1.000 26.53675  ? 398 ALA B C     1 
ATOM   1572 O  O     . ALA A 1 209 ? 12.44800 14.30900  17.62800 1.000 25.83578  ? 398 ALA B O     1 
ATOM   1573 C  CB    . ALA A 1 209 ? 12.20400 12.56100  19.78600 1.000 25.82696  ? 398 ALA B CB    1 
ATOM   1574 N  N     . GLN A 1 210 ? 10.63100 15.49300  18.23700 1.000 27.00288  ? 399 GLN B N     1 
ATOM   1575 C  CA    . GLN A 1 210 ? 10.48300 16.10300  16.91800 1.000 28.43729  ? 399 GLN B CA    1 
ATOM   1576 C  C     . GLN A 1 210 ? 11.65500 17.02500  16.59800 1.000 32.18025  ? 399 GLN B C     1 
ATOM   1577 O  O     . GLN A 1 210 ? 12.36900 16.82400  15.60900 1.000 27.15276  ? 399 GLN B O     1 
ATOM   1578 C  CB    . GLN A 1 210 ? 9.16200  16.87100  16.84500 1.000 33.78427  ? 399 GLN B CB    1 
ATOM   1579 C  CG    . GLN A 1 210 ? 8.86200  17.49200  15.49100 1.000 45.14519  ? 399 GLN B CG    1 
ATOM   1580 C  CD    . GLN A 1 210 ? 8.56700  16.45800  14.42200 1.000 47.75012  ? 399 GLN B CD    1 
ATOM   1581 O  OE1   . GLN A 1 210 ? 9.22600  16.41400  13.38200 1.000 45.94863  ? 399 GLN B OE1   1 
ATOM   1582 N  NE2   . GLN A 1 210 ? 7.56500  15.62100  14.67100 1.000 50.63147  ? 399 GLN B NE2   1 
ATOM   1583 N  N     . ASN A 1 211 ? 11.86500 18.04700  17.42500 1.000 24.75528  ? 400 ASN B N     1 
ATOM   1584 C  CA    . ASN A 1 211 ? 12.88100 19.06200  17.17700 1.000 22.50704  ? 400 ASN B CA    1 
ATOM   1585 C  C     . ASN A 1 211 ? 14.17300 18.80900  17.93700 1.000 26.11150  ? 400 ASN B C     1 
ATOM   1586 O  O     . ASN A 1 211 ? 15.25900 19.07400  17.41200 1.000 25.62917  ? 400 ASN B O     1 
ATOM   1587 C  CB    . ASN A 1 211 ? 12.33300 20.44400  17.54300 1.000 31.35454  ? 400 ASN B CB    1 
ATOM   1588 C  CG    . ASN A 1 211 ? 10.91600 20.65500  17.04600 1.000 33.19118  ? 400 ASN B CG    1 
ATOM   1589 O  OD1   . ASN A 1 211 ? 10.00800 20.94100  17.82700 1.000 35.55125  ? 400 ASN B OD1   1 
ATOM   1590 N  ND2   . ASN A 1 211 ? 10.71800 20.50400  15.74100 1.000 28.49379  ? 400 ASN B ND2   1 
ATOM   1591 N  N     . TYR A 1 212 ? 14.07800 18.31000  19.16600 1.000 23.17143  ? 401 TYR B N     1 
ATOM   1592 C  CA    . TYR A 1 212 ? 15.22900 17.92600  19.96800 1.000 25.09394  ? 401 TYR B CA    1 
ATOM   1593 C  C     . TYR A 1 212 ? 15.11900 16.44300  20.28000 1.000 24.92422  ? 401 TYR B C     1 
ATOM   1594 O  O     . TYR A 1 212 ? 14.01400 15.92900  20.47200 1.000 25.75252  ? 401 TYR B O     1 
ATOM   1595 C  CB    . TYR A 1 212 ? 15.29800 18.72200  21.28000 1.000 24.62415  ? 401 TYR B CB    1 
ATOM   1596 C  CG    . TYR A 1 212 ? 15.35800 20.22700  21.12600 1.000 27.58625  ? 401 TYR B CG    1 
ATOM   1597 C  CD1   . TYR A 1 212 ? 14.20300 20.97500  20.92500 1.000 26.04749  ? 401 TYR B CD1   1 
ATOM   1598 C  CD2   . TYR A 1 212 ? 16.56900 20.90400  21.21100 1.000 27.79044  ? 401 TYR B CD2   1 
ATOM   1599 C  CE1   . TYR A 1 212 ? 14.25600 22.35200  20.79500 1.000 25.29948  ? 401 TYR B CE1   1 
ATOM   1600 C  CE2   . TYR A 1 212 ? 16.63100 22.27900  21.08300 1.000 24.27791  ? 401 TYR B CE2   1 
ATOM   1601 C  CZ    . TYR A 1 212 ? 15.47400 22.99800  20.87500 1.000 25.21210  ? 401 TYR B CZ    1 
ATOM   1602 O  OH    . TYR A 1 212 ? 15.53800 24.36700  20.74700 1.000 26.37135  ? 401 TYR B OH    1 
ATOM   1603 N  N     . GLY A 1 213 ? 16.25100 15.75300  20.33300 1.000 22.41264  ? 402 GLY B N     1 
ATOM   1604 C  CA    . GLY A 1 213 ? 16.21500 14.34800  20.68200 1.000 24.28802  ? 402 GLY B CA    1 
ATOM   1605 C  C     . GLY A 1 213 ? 17.57200 13.69500  20.52800 1.000 27.44351  ? 402 GLY B C     1 
ATOM   1606 O  O     . GLY A 1 213 ? 18.58300 14.35300  20.26700 1.000 25.87517  ? 402 GLY B O     1 
ATOM   1607 N  N     . ASP A 1 214 ? 17.56400 12.37900  20.69900 1.000 26.28016  ? 403 ASP B N     1 
ATOM   1608 C  CA    . ASP A 1 214 ? 18.73500 11.52300  20.61000 1.000 24.57103  ? 403 ASP B CA    1 
ATOM   1609 C  C     . ASP A 1 214 ? 18.64700 10.67700  19.34000 1.000 26.07649  ? 403 ASP B C     1 
ATOM   1610 O  O     . ASP A 1 214 ? 17.66800 10.73700  18.59200 1.000 23.56022  ? 403 ASP B O     1 
ATOM   1611 C  CB    . ASP A 1 214 ? 18.83900 10.65600  21.87000 1.000 26.77344  ? 403 ASP B CB    1 
ATOM   1612 C  CG    . ASP A 1 214 ? 20.14500 9.89100   21.95600 1.000 37.37758  ? 403 ASP B CG    1 
ATOM   1613 O  OD1   . ASP A 1 214 ? 21.20600 10.53200  22.11200 1.000 44.37669  ? 403 ASP B OD1   1 
ATOM   1614 O  OD2   . ASP A 1 214 ? 20.10700 8.64600   21.86300 1.000 32.56509  ? 403 ASP B OD2   1 
ATOM   1615 N  N     . VAL A 1 215 ? 19.69200 9.88200   19.09500 1.000 25.65885  ? 404 VAL B N     1 
ATOM   1616 C  CA    . VAL A 1 215 ? 19.68100 8.95000   17.97000 1.000 27.35054  ? 404 VAL B CA    1 
ATOM   1617 C  C     . VAL A 1 215 ? 18.54900 7.93900   18.11600 1.000 26.28814  ? 404 VAL B C     1 
ATOM   1618 O  O     . VAL A 1 215 ? 18.05900 7.39200   17.11900 1.000 31.29788  ? 404 VAL B O     1 
ATOM   1619 C  CB    . VAL A 1 215 ? 21.05500 8.26000   17.84800 1.000 27.50848  ? 404 VAL B CB    1 
ATOM   1620 C  CG1   . VAL A 1 215 ? 21.44700 7.61500   19.16900 1.000 30.75922  ? 404 VAL B CG1   1 
ATOM   1621 C  CG2   . VAL A 1 215 ? 21.05600 7.23700   16.71700 1.000 33.94228  ? 404 VAL B CG2   1 
ATOM   1622 N  N     . SER A 1 216 ? 18.09600 7.69500   19.34900 1.000 24.85309  ? 405 SER B N     1 
ATOM   1623 C  CA    . SER A 1 216 ? 16.97000 6.79500   19.58500 1.000 23.47383  ? 405 SER B CA    1 
ATOM   1624 C  C     . SER A 1 216 ? 15.69600 7.27200   18.90100 1.000 24.40660  ? 405 SER B C     1 
ATOM   1625 O  O     . SER A 1 216 ? 14.77100 6.47500   18.70800 1.000 19.05752  ? 405 SER B O     1 
ATOM   1626 C  CB    . SER A 1 216 ? 16.72900 6.65500   21.08700 1.000 26.11239  ? 405 SER B CB    1 
ATOM   1627 O  OG    . SER A 1 216 ? 16.62000 7.93300   21.69000 1.000 23.18523  ? 405 SER B OG    1 
ATOM   1628 N  N     . ARG A 1 217 ? 15.63500 8.55100   18.52800 1.000 23.44795  ? 406 ARG B N     1 
ATOM   1629 C  CA    . ARG A 1 217 ? 14.49200 9.09100   17.80200 1.000 24.39023  ? 406 ARG B CA    1 
ATOM   1630 C  C     . ARG A 1 217 ? 14.28000 8.39200   16.46300 1.000 27.68039  ? 406 ARG B C     1 
ATOM   1631 O  O     . ARG A 1 217 ? 13.17900 8.45800   15.90700 1.000 22.86777  ? 406 ARG B O     1 
ATOM   1632 C  CB    . ARG A 1 217 ? 14.70000 10.60100  17.62300 1.000 26.11858  ? 406 ARG B CB    1 
ATOM   1633 C  CG    . ARG A 1 217 ? 13.82300 11.30400  16.60700 1.000 30.65021  ? 406 ARG B CG    1 
ATOM   1634 C  CD    . ARG A 1 217 ? 14.66200 12.24100  15.75700 1.000 27.68408  ? 406 ARG B CD    1 
ATOM   1635 N  NE    . ARG A 1 217 ? 13.85700 13.25800  15.09600 1.000 30.34977  ? 406 ARG B NE    1 
ATOM   1636 C  CZ    . ARG A 1 217 ? 13.45800 13.19900  13.83300 1.000 31.88962  ? 406 ARG B CZ    1 
ATOM   1637 N  NH1   . ARG A 1 217 ? 13.76900 12.17300  13.05800 1.000 36.22021  ? 406 ARG B NH1   1 
ATOM   1638 N  NH2   . ARG A 1 217 ? 12.73200 14.19500  13.33500 1.000 36.84354  ? 406 ARG B NH2   1 
ATOM   1639 N  N     . PHE A 1 218 ? 15.29600 7.70600   15.94000 1.000 23.42087  ? 407 PHE B N     1 
ATOM   1640 C  CA    . PHE A 1 218 ? 15.17000 6.96400   14.69400 1.000 27.98141  ? 407 PHE B CA    1 
ATOM   1641 C  C     . PHE A 1 218 ? 14.94900 5.46900   14.90700 1.000 26.70400  ? 407 PHE B C     1 
ATOM   1642 O  O     . PHE A 1 218 ? 14.91200 4.71600   13.92900 1.000 20.53194  ? 407 PHE B O     1 
ATOM   1643 C  CB    . PHE A 1 218 ? 16.40100 7.19600   13.81900 1.000 21.44078  ? 407 PHE B CB    1 
ATOM   1644 C  CG    . PHE A 1 218 ? 16.65800 8.64200   13.51300 1.000 28.97078  ? 407 PHE B CG    1 
ATOM   1645 C  CD1   . PHE A 1 218 ? 15.88500 9.31200   12.57900 1.000 28.17032  ? 407 PHE B CD1   1 
ATOM   1646 C  CD2   . PHE A 1 218 ? 17.67100 9.33300   14.15800 1.000 26.73477  ? 407 PHE B CD2   1 
ATOM   1647 C  CE1   . PHE A 1 218 ? 16.11500 10.64400  12.29400 1.000 31.28079  ? 407 PHE B CE1   1 
ATOM   1648 C  CE2   . PHE A 1 218 ? 17.90700 10.66600  13.87700 1.000 25.81470  ? 407 PHE B CE2   1 
ATOM   1649 C  CZ    . PHE A 1 218 ? 17.12800 11.32200  12.94300 1.000 25.35351  ? 407 PHE B CZ    1 
ATOM   1650 N  N     . PHE A 1 219 ? 14.80200 5.02100   16.15300 1.000 25.27705  ? 408 PHE B N     1 
ATOM   1651 C  CA    . PHE A 1 219 ? 14.50000 3.61700   16.40700 1.000 26.64233  ? 408 PHE B CA    1 
ATOM   1652 C  C     . PHE A 1 219 ? 13.09900 3.28300   15.90700 1.000 27.68337  ? 408 PHE B C     1 
ATOM   1653 O  O     . PHE A 1 219 ? 12.13700 4.00500   16.18800 1.000 27.68978  ? 408 PHE B O     1 
ATOM   1654 C  CB    . PHE A 1 219 ? 14.61300 3.29900   17.89800 1.000 22.32310  ? 408 PHE B CB    1 
ATOM   1655 C  CG    . PHE A 1 219 ? 16.02400 3.28300   18.41600 1.000 24.73391  ? 408 PHE B CG    1 
ATOM   1656 C  CD1   . PHE A 1 219 ? 17.10100 3.24000   17.54600 1.000 26.66814  ? 408 PHE B CD1   1 
ATOM   1657 C  CD2   . PHE A 1 219 ? 16.27100 3.30100   19.77800 1.000 24.64774  ? 408 PHE B CD2   1 
ATOM   1658 C  CE1   . PHE A 1 219 ? 18.39800 3.22300   18.02700 1.000 22.57034  ? 408 PHE B CE1   1 
ATOM   1659 C  CE2   . PHE A 1 219 ? 17.56600 3.28400   20.26300 1.000 27.23037  ? 408 PHE B CE2   1 
ATOM   1660 C  CZ    . PHE A 1 219 ? 18.63000 3.24600   19.38500 1.000 21.52912  ? 408 PHE B CZ    1 
ATOM   1661 N  N     . ASN A 1 220 ? 12.98200 2.18300   15.17200 1.000 21.35047  ? 409 ASN B N     1 
ATOM   1662 C  CA    . ASN A 1 220 ? 11.70100 1.75900   14.63400 1.000 26.01818  ? 409 ASN B CA    1 
ATOM   1663 C  C     . ASN A 1 220 ? 11.02700 0.75300   15.56400 1.000 32.23258  ? 409 ASN B C     1 
ATOM   1664 O  O     . ASN A 1 220 ? 11.61800 0.24600   16.51900 1.000 25.83822  ? 409 ASN B O     1 
ATOM   1665 C  CB    . ASN A 1 220 ? 11.87900 1.16400   13.23700 1.000 30.00798  ? 409 ASN B CB    1 
ATOM   1666 C  CG    . ASN A 1 220 ? 12.10700 2.22500   12.18300 1.000 28.10288  ? 409 ASN B CG    1 
ATOM   1667 O  OD1   . ASN A 1 220 ? 11.45500 3.26800   12.19100 1.000 29.82885  ? 409 ASN B OD1   1 
ATOM   1668 N  ND2   . ASN A 1 220 ? 13.03900 1.97000   11.27300 1.000 30.93356  ? 409 ASN B ND2   1 
ATOM   1669 N  N     . HIS A 1 221 ? 9.76100  0.47500   15.27100 1.000 31.87238  ? 410 HIS B N     1 
ATOM   1670 C  CA    . HIS A 1 221 ? 8.97400  -0.48000  16.03500 1.000 34.25096  ? 410 HIS B CA    1 
ATOM   1671 C  C     . HIS A 1 221 ? 9.09600  -1.87200  15.43500 1.000 33.28762  ? 410 HIS B C     1 
ATOM   1672 O  O     . HIS A 1 221 ? 9.19300  -2.03200  14.21500 1.000 29.76311  ? 410 HIS B O     1 
ATOM   1673 C  CB    . HIS A 1 221 ? 7.50300  -0.06000  16.06900 1.000 33.24496  ? 410 HIS B CB    1 
ATOM   1674 C  CG    . HIS A 1 221 ? 6.57300  -1.15300  16.49300 1.000 31.05654  ? 410 HIS B CG    1 
ATOM   1675 N  ND1   . HIS A 1 221 ? 6.42600  -1.53700  17.80800 1.000 31.42837  ? 410 HIS B ND1   1 
ATOM   1676 C  CD2   . HIS A 1 221 ? 5.75200  -1.95400  15.77300 1.000 40.63003  ? 410 HIS B CD2   1 
ATOM   1677 C  CE1   . HIS A 1 221 ? 5.54800  -2.52200  17.88200 1.000 36.60428  ? 410 HIS B CE1   1 
ATOM   1678 N  NE2   . HIS A 1 221 ? 5.12500  -2.79400  16.66100 1.000 35.61059  ? 410 HIS B NE2   1 
ATOM   1679 N  N     . SER A 1 222 ? 9.09800  -2.87900  16.30400 1.000 28.75793  ? 411 SER B N     1 
ATOM   1680 C  CA    . SER A 1 222 ? 9.02200  -4.26800  15.87900 1.000 35.23845  ? 411 SER B CA    1 
ATOM   1681 C  C     . SER A 1 222 ? 8.18000  -5.04300  16.87700 1.000 37.19495  ? 411 SER B C     1 
ATOM   1682 O  O     . SER A 1 222 ? 8.30300  -4.84700  18.08900 1.000 30.63336  ? 411 SER B O     1 
ATOM   1683 C  CB    . SER A 1 222 ? 10.40800 -4.91100  15.75900 1.000 30.33386  ? 411 SER B CB    1 
ATOM   1684 O  OG    . SER A 1 222 ? 10.30900 -6.29300  15.45600 1.000 31.50250  ? 411 SER B OG    1 
ATOM   1685 N  N     . CYS A 1 223 ? 7.32500  -5.92400  16.35700 1.000 29.41624  ? 412 CYS B N     1 
ATOM   1686 C  CA    . CYS A 1 223 ? 6.55000  -6.80600  17.21600 1.000 37.75043  ? 412 CYS B CA    1 
ATOM   1687 C  C     . CYS A 1 223 ? 7.40300  -7.90400  17.83600 1.000 35.18334  ? 412 CYS B C     1 
ATOM   1688 O  O     . CYS A 1 223 ? 6.93800  -8.58400  18.75700 1.000 34.89416  ? 412 CYS B O     1 
ATOM   1689 C  CB    . CYS A 1 223 ? 5.38900  -7.40000  16.42100 1.000 45.89237  ? 412 CYS B CB    1 
ATOM   1690 S  SG    . CYS A 1 223 ? 4.35000  -6.13400  15.64400 1.000 40.30549  ? 412 CYS B SG    1 
ATOM   1691 N  N     . SER A 1 224 ? 8.63500  -8.08200  17.36300 1.000 36.88073  ? 413 SER B N     1 
ATOM   1692 C  CA    . SER A 1 224 ? 9.62400  -8.95700  17.99000 1.000 34.63254  ? 413 SER B CA    1 
ATOM   1693 C  C     . SER A 1 224 ? 10.89400 -8.14300  18.20800 1.000 33.64392  ? 413 SER B C     1 
ATOM   1694 O  O     . SER A 1 224 ? 11.90300 -8.33700  17.51900 1.000 34.62237  ? 413 SER B O     1 
ATOM   1695 C  CB    . SER A 1 224 ? 9.89600  -10.19500 17.13500 1.000 37.69875  ? 413 SER B CB    1 
ATOM   1696 O  OG    . SER A 1 224 ? 8.84900  -11.14100 17.26000 1.000 43.59305  ? 413 SER B OG    1 
ATOM   1697 N  N     . PRO A 1 225 ? 10.87100 -7.21500  19.16100 1.000 30.55040  ? 414 PRO B N     1 
ATOM   1698 C  CA    . PRO A 1 225 ? 11.98700 -6.27600  19.31000 1.000 31.00110  ? 414 PRO B CA    1 
ATOM   1699 C  C     . PRO A 1 225 ? 13.23000 -6.93900  19.88300 1.000 27.70370  ? 414 PRO B C     1 
ATOM   1700 O  O     . PRO A 1 225 ? 13.17600 -7.99200  20.52200 1.000 28.70556  ? 414 PRO B O     1 
ATOM   1701 C  CB    . PRO A 1 225 ? 11.43100 -5.22900  20.27700 1.000 30.04468  ? 414 PRO B CB    1 
ATOM   1702 C  CG    . PRO A 1 225 ? 10.43800 -5.97700  21.09200 1.000 26.11273  ? 414 PRO B CG    1 
ATOM   1703 C  CD    . PRO A 1 225 ? 9.81600  -6.98400  20.16400 1.000 30.33913  ? 414 PRO B CD    1 
ATOM   1704 N  N     . ASN A 1 226 ? 14.37100 -6.29000  19.64100 1.000 27.52251  ? 415 ASN B N     1 
ATOM   1705 C  CA    . ASN A 1 226 ? 15.64100 -6.72000  20.20600 1.000 28.39250  ? 415 ASN B CA    1 
ATOM   1706 C  C     . ASN A 1 226 ? 16.17500 -5.78600  21.28600 1.000 22.42156  ? 415 ASN B C     1 
ATOM   1707 O  O     . ASN A 1 226 ? 17.19000 -6.11100  21.91200 1.000 21.32574  ? 415 ASN B O     1 
ATOM   1708 C  CB    . ASN A 1 226 ? 16.69400 -6.87800  19.09900 1.000 25.71167  ? 415 ASN B CB    1 
ATOM   1709 C  CG    . ASN A 1 226 ? 16.79300 -5.66000  18.20200 1.000 28.16343  ? 415 ASN B CG    1 
ATOM   1710 O  OD1   . ASN A 1 226 ? 16.27500 -4.59000  18.52200 1.000 29.40950  ? 415 ASN B OD1   1 
ATOM   1711 N  ND2   . ASN A 1 226 ? 17.46800 -5.81700  17.06900 1.000 27.10971  ? 415 ASN B ND2   1 
ATOM   1712 N  N     . ILE A 1 227 ? 15.52700 -4.64200  21.52000 1.000 25.96053  ? 416 ILE B N     1 
ATOM   1713 C  CA    . ILE A 1 227 ? 15.86400 -3.75100  22.62300 1.000 24.73459  ? 416 ILE B CA    1 
ATOM   1714 C  C     . ILE A 1 227 ? 14.57700 -3.41000  23.36400 1.000 25.32132  ? 416 ILE B C     1 
ATOM   1715 O  O     . ILE A 1 227 ? 13.47200 -3.55600  22.83700 1.000 21.28002  ? 416 ILE B O     1 
ATOM   1716 C  CB    . ILE A 1 227 ? 16.58200 -2.46100  22.15900 1.000 23.75129  ? 416 ILE B CB    1 
ATOM   1717 C  CG1   . ILE A 1 227 ? 15.58600 -1.46200  21.57000 1.000 29.34402  ? 416 ILE B CG1   1 
ATOM   1718 C  CG2   . ILE A 1 227 ? 17.65800 -2.77900  21.13500 1.000 26.68775  ? 416 ILE B CG2   1 
ATOM   1719 C  CD1   . ILE A 1 227 ? 16.22900 -0.20700  21.00800 1.000 19.89760  ? 416 ILE B CD1   1 
ATOM   1720 N  N     . ALA A 1 228 ? 14.73200 -2.95500  24.60600 1.000 21.29684  ? 417 ALA B N     1 
ATOM   1721 C  CA    . ALA A 1 228 ? 13.58000 -2.65400  25.44500 1.000 26.47506  ? 417 ALA B CA    1 
ATOM   1722 C  C     . ALA A 1 228 ? 13.90300 -1.47700  26.35300 1.000 26.33051  ? 417 ALA B C     1 
ATOM   1723 O  O     . ALA A 1 228 ? 15.06900 -1.15200  26.59400 1.000 20.79980  ? 417 ALA B O     1 
ATOM   1724 C  CB    . ALA A 1 228 ? 13.15200 -3.86800  26.27700 1.000 25.35739  ? 417 ALA B CB    1 
ATOM   1725 N  N     . ILE A 1 229 ? 12.85200 -0.86700  26.85600 1.000 22.26012  ? 418 ILE B N     1 
ATOM   1726 C  CA    . ILE A 1 229 ? 13.01200 0.26700   27.71700 1.000 26.96919  ? 418 ILE B CA    1 
ATOM   1727 C  C     . ILE A 1 229 ? 13.07600 -0.01400  29.20200 1.000 28.76346  ? 418 ILE B C     1 
ATOM   1728 O  O     . ILE A 1 229 ? 12.38600 -0.85500  29.72200 1.000 31.29733  ? 418 ILE B O     1 
ATOM   1729 C  CB    . ILE A 1 229 ? 11.91900 1.33800   27.43500 1.000 29.02919  ? 418 ILE B CB    1 
ATOM   1730 C  CG1   . ILE A 1 229 ? 12.48000 2.74100   27.67200 1.000 31.77573  ? 418 ILE B CG1   1 
ATOM   1731 C  CG2   . ILE A 1 229 ? 10.67800 1.11800   28.27800 1.000 34.68930  ? 418 ILE B CG2   1 
ATOM   1732 C  CD1   . ILE A 1 229 ? 13.40700 3.21700   26.57900 1.000 26.15697  ? 418 ILE B CD1   1 
ATOM   1733 N  N     . TYR A 1 230 ? 14.01300 0.61900   29.83800 1.000 24.77010  ? 419 TYR B N     1 
ATOM   1734 C  CA    . TYR A 1 230 ? 14.12900 0.55400   31.28800 1.000 27.70158  ? 419 TYR B CA    1 
ATOM   1735 C  C     . TYR A 1 230 ? 14.05500 1.97000   31.83900 1.000 28.16913  ? 419 TYR B C     1 
ATOM   1736 O  O     . TYR A 1 230 ? 14.63400 2.89800   31.26600 1.000 27.74950  ? 419 TYR B O     1 
ATOM   1737 C  CB    . TYR A 1 230 ? 15.44700 -0.10400  31.72600 1.000 31.06172  ? 419 TYR B CB    1 
ATOM   1738 C  CG    . TYR A 1 230 ? 15.53600 -1.59300  31.46900 1.000 30.11576  ? 419 TYR B CG    1 
ATOM   1739 C  CD1   . TYR A 1 230 ? 15.61400 -2.09000  30.17700 1.000 24.14848  ? 419 TYR B CD1   1 
ATOM   1740 C  CD2   . TYR A 1 230 ? 15.56200 -2.50000  32.52200 1.000 32.38199  ? 419 TYR B CD2   1 
ATOM   1741 C  CE1   . TYR A 1 230 ? 15.70100 -3.44500  29.93600 1.000 25.02882  ? 419 TYR B CE1   1 
ATOM   1742 C  CE2   . TYR A 1 230 ? 15.65000 -3.86000  32.29100 1.000 29.56271  ? 419 TYR B CE2   1 
ATOM   1743 C  CZ    . TYR A 1 230 ? 15.72000 -4.32600  30.99400 1.000 32.64827  ? 419 TYR B CZ    1 
ATOM   1744 O  OH    . TYR A 1 230 ? 15.80800 -5.67900  30.75200 1.000 38.75837  ? 419 TYR B OH    1 
ATOM   1745 N  N     . SER A 1 231 ? 13.33500 2.14000   32.94600 1.000 26.54934  ? 420 SER B N     1 
ATOM   1746 C  CA    . SER A 1 231 ? 13.21500 3.44800   33.58700 1.000 32.40623  ? 420 SER B CA    1 
ATOM   1747 C  C     . SER A 1 231 ? 14.38300 3.60700   34.55100 1.000 30.32558  ? 420 SER B C     1 
ATOM   1748 O  O     . SER A 1 231 ? 14.37600 3.05300   35.65300 1.000 35.67706  ? 420 SER B O     1 
ATOM   1749 C  CB    . SER A 1 231 ? 11.87300 3.58800   34.29900 1.000 35.72459  ? 420 SER B CB    1 
ATOM   1750 O  OG    . SER A 1 231 ? 10.87900 4.10700   33.43300 1.000 51.34523  ? 420 SER B OG    1 
ATOM   1751 N  N     . ALA A 1 232 ? 15.39900 4.35600   34.13100 1.000 29.17622  ? 421 ALA B N     1 
ATOM   1752 C  CA    . ALA A 1 232 ? 16.56100 4.61600   34.97500 1.000 26.01314  ? 421 ALA B CA    1 
ATOM   1753 C  C     . ALA A 1 232 ? 16.24000 5.79100   35.89000 1.000 29.46459  ? 421 ALA B C     1 
ATOM   1754 O  O     . ALA A 1 232 ? 16.17100 6.93900   35.44000 1.000 30.16590  ? 421 ALA B O     1 
ATOM   1755 C  CB    . ALA A 1 232 ? 17.79500 4.89500   34.12300 1.000 22.42560  ? 421 ALA B CB    1 
ATOM   1756 N  N     . VAL A 1 233 ? 16.04700 5.50700   37.17400 1.000 31.30259  ? 422 VAL B N     1 
ATOM   1757 C  CA    . VAL A 1 233 ? 15.62300 6.50000   38.15200 1.000 32.77953  ? 422 VAL B CA    1 
ATOM   1758 C  C     . VAL A 1 233 ? 16.79700 6.79700   39.07300 1.000 31.83761  ? 422 VAL B C     1 
ATOM   1759 O  O     . VAL A 1 233 ? 17.28800 5.90600   39.77700 1.000 33.93673  ? 422 VAL B O     1 
ATOM   1760 C  CB    . VAL A 1 233 ? 14.40400 6.01700   38.95400 1.000 36.16038  ? 422 VAL B CB    1 
ATOM   1761 C  CG1   . VAL A 1 233 ? 14.10600 6.97500   40.09400 1.000 36.07866  ? 422 VAL B CG1   1 
ATOM   1762 C  CG2   . VAL A 1 233 ? 13.19500 5.87000   38.04300 1.000 35.94421  ? 422 VAL B CG2   1 
ATOM   1763 N  N     . ARG A 1 234 ? 17.24200 8.05100   39.07100 1.000 33.75534  ? 423 ARG B N     1 
ATOM   1764 C  CA    . ARG A 1 234 ? 18.28600 8.51200   39.97200 1.000 39.03212  ? 423 ARG B CA    1 
ATOM   1765 C  C     . ARG A 1 234 ? 17.77100 9.50700   40.99900 1.000 44.23917  ? 423 ARG B C     1 
ATOM   1766 O  O     . ARG A 1 234 ? 18.55500 9.99300   41.82200 1.000 43.78774  ? 423 ARG B O     1 
ATOM   1767 C  CB    . ARG A 1 234 ? 19.44000 9.13000   39.17200 1.000 42.63932  ? 423 ARG B CB    1 
ATOM   1768 C  CG    . ARG A 1 234 ? 18.99600 10.15700  38.14300 1.000 42.81609  ? 423 ARG B CG    1 
ATOM   1769 C  CD    . ARG A 1 234 ? 19.89400 10.13500  36.91500 1.000 42.64590  ? 423 ARG B CD    1 
ATOM   1770 N  NE    . ARG A 1 234 ? 19.32000 10.90000  35.81300 1.000 49.27481  ? 423 ARG B NE    1 
ATOM   1771 C  CZ    . ARG A 1 234 ? 19.56500 12.18200  35.58300 1.000 52.89204  ? 423 ARG B CZ    1 
ATOM   1772 N  NH1   . ARG A 1 234 ? 20.38500 12.87900  36.35300 1.000 54.02540  ? 423 ARG B NH1   1 
ATOM   1773 N  NH2   . ARG A 1 234 ? 18.97300 12.78200  34.55500 1.000 53.94352  ? 423 ARG B NH2   1 
ATOM   1774 N  N     . ASN A 1 235 ? 16.47800 9.81500   40.98200 1.000 51.60390  ? 424 ASN B N     1 
ATOM   1775 C  CA    . ASN A 1 235 ? 15.87500 10.73100  41.93600 1.000 59.20309  ? 424 ASN B CA    1 
ATOM   1776 C  C     . ASN A 1 235 ? 15.13800 9.89400   42.97700 1.000 74.98468  ? 424 ASN B C     1 
ATOM   1777 O  O     . ASN A 1 235 ? 14.96000 8.68200   42.82900 1.000 79.25816  ? 424 ASN B O     1 
ATOM   1778 C  CB    . ASN A 1 235 ? 15.05600 11.81000  41.21900 1.000 57.45357  ? 424 ASN B CB    1 
ATOM   1779 C  CG    . ASN A 1 235 ? 15.93000 12.77900  40.43600 1.000 50.92347  ? 424 ASN B CG    1 
ATOM   1780 O  OD1   . ASN A 1 235 ? 16.52800 13.69300  41.00500 1.000 55.46404  ? 424 ASN B OD1   1 
ATOM   1781 N  ND2   . ASN A 1 235 ? 16.00900 12.58100  39.12400 1.000 42.23586  ? 424 ASN B ND2   1 
ATOM   1782 N  N     . HIS A 1 236 ? 14.89400 10.54300  44.08600 1.000 102.55582 ? 425 HIS B N     1 
ATOM   1783 C  CA    . HIS A 1 236 ? 14.24700 9.89400   45.22400 1.000 109.16473 ? 425 HIS B CA    1 
ATOM   1784 C  C     . HIS A 1 236 ? 12.93300 9.17700   45.14200 1.000 109.18395 ? 425 HIS B C     1 
ATOM   1785 O  O     . HIS A 1 236 ? 12.83200 7.98700   45.39200 1.000 107.18973 ? 425 HIS B O     1 
ATOM   1786 C  CB    . HIS A 1 236 ? 13.95600 11.01100  46.18500 1.000 108.17636 ? 425 HIS B CB    1 
ATOM   1787 C  CG    . HIS A 1 236 ? 13.10500 12.09500  45.60000 1.000 109.74801 ? 425 HIS B CG    1 
ATOM   1788 N  ND1   . HIS A 1 236 ? 13.59400 13.02300  44.70600 1.000 112.18146 ? 425 HIS B ND1   1 
ATOM   1789 C  CD2   . HIS A 1 236 ? 11.80300 12.41200  45.79500 1.000 112.17200 ? 425 HIS B CD2   1 
ATOM   1790 C  CE1   . HIS A 1 236 ? 12.62900 13.85900  44.37200 1.000 111.45947 ? 425 HIS B CE1   1 
ATOM   1791 N  NE2   . HIS A 1 236 ? 11.53200 13.51000  45.01900 1.000 111.22013 ? 425 HIS B NE2   1 
ATOM   1792 N  N     . GLY A 1 237 ? 11.91800 9.91300   44.80300 1.000 87.82681  ? 426 GLY B N     1 
ATOM   1793 C  CA    . GLY A 1 237 ? 10.56500 9.38900   44.84000 1.000 78.17169  ? 426 GLY B CA    1 
ATOM   1794 C  C     . GLY A 1 237 ? 9.86300  10.10000  43.70600 1.000 71.62608  ? 426 GLY B C     1 
ATOM   1795 O  O     . GLY A 1 237 ? 8.65700  9.95100   43.48400 1.000 68.88698  ? 426 GLY B O     1 
ATOM   1796 N  N     . PHE A 1 238 ? 10.64500 10.91200  43.00500 1.000 68.13050  ? 427 PHE B N     1 
ATOM   1797 C  CA    . PHE A 1 238 ? 10.19200 11.63700  41.82700 1.000 64.04421  ? 427 PHE B CA    1 
ATOM   1798 C  C     . PHE A 1 238 ? 9.94100  10.64200  40.70300 1.000 48.79777  ? 427 PHE B C     1 
ATOM   1799 O  O     . PHE A 1 238 ? 10.88500 10.06600  40.15200 1.000 50.91519  ? 427 PHE B O     1 
ATOM   1800 C  CB    . PHE A 1 238 ? 11.25200 12.66200  41.44000 1.000 58.93428  ? 427 PHE B CB    1 
ATOM   1801 C  CG    . PHE A 1 238 ? 10.78600 13.67400  40.45000 1.000 51.22447  ? 427 PHE B CG    1 
ATOM   1802 C  CD1   . PHE A 1 238 ? 9.93300  14.69200  40.83500 1.000 48.02502  ? 427 PHE B CD1   1 
ATOM   1803 C  CD2   . PHE A 1 238 ? 11.21900 13.62300  39.13800 1.000 43.34003  ? 427 PHE B CD2   1 
ATOM   1804 C  CE1   . PHE A 1 238 ? 9.50800  15.63300  39.92500 1.000 46.82507  ? 427 PHE B CE1   1 
ATOM   1805 C  CE2   . PHE A 1 238 ? 10.79700 14.56200  38.22400 1.000 49.56427  ? 427 PHE B CE2   1 
ATOM   1806 C  CZ    . PHE A 1 238 ? 9.94300  15.57000  38.61800 1.000 47.92441  ? 427 PHE B CZ    1 
ATOM   1807 N  N     . ARG A 1 239 ? 8.68300  10.46900  40.31400 1.000 46.49716  ? 428 ARG B N     1 
ATOM   1808 C  CA    . ARG A 1 239 ? 8.33400  9.46200   39.30800 1.000 47.14337  ? 428 ARG B CA    1 
ATOM   1809 C  C     . ARG A 1 239 ? 7.62200  10.02000  38.12600 1.000 38.80644  ? 428 ARG B C     1 
ATOM   1810 O  O     . ARG A 1 239 ? 6.93300  9.31100   37.42700 1.000 35.05681  ? 428 ARG B O     1 
ATOM   1811 C  CB    . ARG A 1 239 ? 7.47400  8.38600   39.93600 1.000 49.65438  ? 428 ARG B CB    1 
ATOM   1812 C  CG    . ARG A 1 239 ? 6.72500  8.79800   41.18300 1.000 56.99479  ? 428 ARG B CG    1 
ATOM   1813 C  CD    . ARG A 1 239 ? 6.64400  7.62600   42.14100 1.000 66.72508  ? 428 ARG B CD    1 
ATOM   1814 N  NE    . ARG A 1 239 ? 5.71600  6.60800   41.66600 1.000 70.31378  ? 428 ARG B NE    1 
ATOM   1815 C  CZ    . ARG A 1 239 ? 5.84200  5.30500   41.89100 1.000 67.22994  ? 428 ARG B CZ    1 
ATOM   1816 N  NH1   . ARG A 1 239 ? 6.87500  4.84800   42.57700 1.000 60.98661  ? 428 ARG B NH1   1 
ATOM   1817 N  NH2   . ARG A 1 239 ? 4.93600  4.46000   41.42100 1.000 61.84283  ? 428 ARG B NH2   1 
ATOM   1818 N  N     . THR A 1 240 ? 7.77000  11.30300  37.91700 1.000 40.60473  ? 429 THR B N     1 
ATOM   1819 C  CA    . THR A 1 240 ? 7.21800  11.92600  36.72100 1.000 36.64343  ? 429 THR B CA    1 
ATOM   1820 C  C     . THR A 1 240 ? 8.23700  12.07000  35.60000 1.000 35.78456  ? 429 THR B C     1 
ATOM   1821 O  O     . THR A 1 240 ? 7.85500  12.04400  34.42600 1.000 35.73779  ? 429 THR B O     1 
ATOM   1822 C  CB    . THR A 1 240 ? 6.64400  13.31000  37.04500 1.000 35.32321  ? 429 THR B CB    1 
ATOM   1823 O  OG1   . THR A 1 240 ? 7.69900  14.27700  37.04600 1.000 35.05394  ? 429 THR B OG1   1 
ATOM   1824 C  CG2   . THR A 1 240 ? 5.97300  13.30600  38.40700 1.000 35.38378  ? 429 THR B CG2   1 
ATOM   1825 N  N     . ILE A 1 241 ? 9.51700  12.22200  35.93300 1.000 34.04845  ? 430 ILE B N     1 
ATOM   1826 C  CA    . ILE A 1 241 ? 10.58700 12.34900  34.95000 1.000 31.51523  ? 430 ILE B CA    1 
ATOM   1827 C  C     . ILE A 1 241 ? 11.67900 11.34900  35.30000 1.000 26.14702  ? 430 ILE B C     1 
ATOM   1828 O  O     . ILE A 1 241 ? 12.10900 11.27200  36.45600 1.000 36.62535  ? 430 ILE B O     1 
ATOM   1829 C  CB    . ILE A 1 241 ? 11.15900 13.77900  34.90200 1.000 33.12327  ? 430 ILE B CB    1 
ATOM   1830 C  CG1   . ILE A 1 241 ? 10.09100 14.76800  34.43200 1.000 32.55480  ? 430 ILE B CG1   1 
ATOM   1831 C  CG2   . ILE A 1 241 ? 12.38600 13.83700  34.00500 1.000 29.37641  ? 430 ILE B CG2   1 
ATOM   1832 C  CD1   . ILE A 1 241 ? 10.53300 16.21200  34.48700 1.000 27.68693  ? 430 ILE B CD1   1 
ATOM   1833 N  N     . TYR A 1 242 ? 12.12200 10.58600  34.30400 1.000 27.82754  ? 431 TYR B N     1 
ATOM   1834 C  CA    . TYR A 1 242 ? 13.16100 9.58400   34.49000 1.000 28.84088  ? 431 TYR B CA    1 
ATOM   1835 C  C     . TYR A 1 242 ? 13.77400 9.27800   33.13200 1.000 27.13401  ? 431 TYR B C     1 
ATOM   1836 O  O     . TYR A 1 242 ? 13.22500 9.63600   32.08700 1.000 26.65729  ? 431 TYR B O     1 
ATOM   1837 C  CB    . TYR A 1 242 ? 12.60300 8.31800   35.14700 1.000 26.37546  ? 431 TYR B CB    1 
ATOM   1838 C  CG    . TYR A 1 242 ? 11.22600 7.94900   34.65100 1.000 26.48868  ? 431 TYR B CG    1 
ATOM   1839 C  CD1   . TYR A 1 242 ? 11.06000 7.18500   33.50300 1.000 22.62700  ? 431 TYR B CD1   1 
ATOM   1840 C  CD2   . TYR A 1 242 ? 10.08900 8.37500   35.32500 1.000 27.86818  ? 431 TYR B CD2   1 
ATOM   1841 C  CE1   . TYR A 1 242 ? 9.80100  6.85200   33.04500 1.000 25.73372  ? 431 TYR B CE1   1 
ATOM   1842 C  CE2   . TYR A 1 242 ? 8.82800  8.04900   34.87400 1.000 33.14878  ? 431 TYR B CE2   1 
ATOM   1843 C  CZ    . TYR A 1 242 ? 8.69000  7.28700   33.73500 1.000 29.42487  ? 431 TYR B CZ    1 
ATOM   1844 O  OH    . TYR A 1 242 ? 7.43200  6.96200   33.28700 1.000 36.16203  ? 431 TYR B OH    1 
ATOM   1845 N  N     . ASP A 1 243 ? 14.92700 8.61600   33.15800 1.000 25.69320  ? 432 ASP B N     1 
ATOM   1846 C  CA    . ASP A 1 243 ? 15.62700 8.27000   31.92900 1.000 25.72699  ? 432 ASP B CA    1 
ATOM   1847 C  C     . ASP A 1 243 ? 14.95700 7.07900   31.25400 1.000 27.25708  ? 432 ASP B C     1 
ATOM   1848 O  O     . ASP A 1 243 ? 14.69000 6.05800   31.89600 1.000 21.35428  ? 432 ASP B O     1 
ATOM   1849 C  CB    . ASP A 1 243 ? 17.09300 7.95100   32.22000 1.000 26.77137  ? 432 ASP B CB    1 
ATOM   1850 C  CG    . ASP A 1 243 ? 17.81800 9.09800   32.89000 1.000 30.96025  ? 432 ASP B CG    1 
ATOM   1851 O  OD1   . ASP A 1 243 ? 17.44600 10.26600  32.64300 1.000 28.68042  ? 432 ASP B OD1   1 
ATOM   1852 O  OD2   . ASP A 1 243 ? 18.76300 8.83200   33.66200 1.000 38.76125  ? 432 ASP B OD2   1 
ATOM   1853 N  N     . LEU A 1 244 ? 14.68800 7.21300   29.95400 1.000 21.02337  ? 433 LEU B N     1 
ATOM   1854 C  CA    . LEU A 1 244 ? 14.14600 6.11400   29.15300 1.000 25.27838  ? 433 LEU B CA    1 
ATOM   1855 C  C     . LEU A 1 244 ? 15.31800 5.39900   28.48700 1.000 26.10520  ? 433 LEU B C     1 
ATOM   1856 O  O     . LEU A 1 244 ? 15.67900 5.65700   27.33700 1.000 23.36312  ? 433 LEU B O     1 
ATOM   1857 C  CB    . LEU A 1 244 ? 13.14400 6.63400   28.13100 1.000 22.95161  ? 433 LEU B CB    1 
ATOM   1858 C  CG    . LEU A 1 244 ? 11.92900 7.39500   28.66100 1.000 23.58596  ? 433 LEU B CG    1 
ATOM   1859 C  CD1   . LEU A 1 244 ? 11.14100 7.99900   27.50900 1.000 23.58647  ? 433 LEU B CD1   1 
ATOM   1860 C  CD2   . LEU A 1 244 ? 11.04500 6.48700   29.49900 1.000 21.67847  ? 433 LEU B CD2   1 
ATOM   1861 N  N     . ALA A 1 245 ? 15.91800 4.47600   29.23300 1.000 24.47878  ? 434 ALA B N     1 
ATOM   1862 C  CA    . ALA A 1 245 ? 17.13200 3.79800   28.79800 1.000 24.47739  ? 434 ALA B CA    1 
ATOM   1863 C  C     . ALA A 1 245 ? 16.78700 2.56200   27.97800 1.000 26.56903  ? 434 ALA B C     1 
ATOM   1864 O  O     . ALA A 1 245 ? 15.99000 1.72300   28.41000 1.000 24.80762  ? 434 ALA B O     1 
ATOM   1865 C  CB    . ALA A 1 245 ? 17.99000 3.40900   30.00200 1.000 24.61658  ? 434 ALA B CB    1 
ATOM   1866 N  N     . PHE A 1 246 ? 17.39200 2.45500   26.79800 1.000 24.47864  ? 435 PHE B N     1 
ATOM   1867 C  CA    . PHE A 1 246 ? 17.22400 1.29200   25.93800 1.000 23.58568  ? 435 PHE B CA    1 
ATOM   1868 C  C     . PHE A 1 246 ? 18.30400 0.26200   26.24400 1.000 23.16767  ? 435 PHE B C     1 
ATOM   1869 O  O     . PHE A 1 246 ? 19.50000 0.57200   26.19400 1.000 20.68244  ? 435 PHE B O     1 
ATOM   1870 C  CB    . PHE A 1 246 ? 17.29000 1.68700   24.46200 1.000 27.95076  ? 435 PHE B CB    1 
ATOM   1871 C  CG    . PHE A 1 246 ? 16.09100 2.45200   23.97900 1.000 27.59618  ? 435 PHE B CG    1 
ATOM   1872 C  CD1   . PHE A 1 246 ? 14.91700 1.79100   23.65800 1.000 25.26357  ? 435 PHE B CD1   1 
ATOM   1873 C  CD2   . PHE A 1 246 ? 16.14400 3.82800   23.82700 1.000 26.16119  ? 435 PHE B CD2   1 
ATOM   1874 C  CE1   . PHE A 1 246 ? 13.81400 2.48900   23.20400 1.000 26.54683  ? 435 PHE B CE1   1 
ATOM   1875 C  CE2   . PHE A 1 246 ? 15.04300 4.53200   23.37500 1.000 29.54551  ? 435 PHE B CE2   1 
ATOM   1876 C  CZ    . PHE A 1 246 ? 13.87600 3.86100   23.06300 1.000 30.14874  ? 435 PHE B CZ    1 
ATOM   1877 N  N     . PHE A 1 247 ? 17.88100 -0.96000  26.55100 1.000 22.57358  ? 436 PHE B N     1 
ATOM   1878 C  CA    . PHE A 1 247 ? 18.78700 -2.07100  26.79700 1.000 22.17804  ? 436 PHE B CA    1 
ATOM   1879 C  C     . PHE A 1 247 ? 18.47200 -3.20500  25.83400 1.000 21.32433  ? 436 PHE B C     1 
ATOM   1880 O  O     . PHE A 1 247 ? 17.30600 -3.45100  25.50900 1.000 25.87311  ? 436 PHE B O     1 
ATOM   1881 C  CB    . PHE A 1 247 ? 18.68400 -2.57000  28.24300 1.000 22.06518  ? 436 PHE B CB    1 
ATOM   1882 C  CG    . PHE A 1 247 ? 19.45300 -1.73800  29.22900 1.000 26.91366  ? 436 PHE B CG    1 
ATOM   1883 C  CD1   . PHE A 1 247 ? 18.88600 -0.61200  29.80100 1.000 22.29195  ? 436 PHE B CD1   1 
ATOM   1884 C  CD2   . PHE A 1 247 ? 20.74500 -2.08700  29.59000 1.000 24.95151  ? 436 PHE B CD2   1 
ATOM   1885 C  CE1   . PHE A 1 247 ? 19.59300 0.15200   30.71200 1.000 22.64936  ? 436 PHE B CE1   1 
ATOM   1886 C  CE2   . PHE A 1 247 ? 21.45600 -1.33000  30.50100 1.000 22.88736  ? 436 PHE B CE2   1 
ATOM   1887 C  CZ    . PHE A 1 247 ? 20.88000 -0.20800  31.06200 1.000 23.03982  ? 436 PHE B CZ    1 
ATOM   1888 N  N     . ALA A 1 248 ? 19.51700 -3.89100  25.38000 1.000 19.87972  ? 437 ALA B N     1 
ATOM   1889 C  CA    . ALA A 1 248 ? 19.34600 -4.99400  24.44500 1.000 21.96233  ? 437 ALA B CA    1 
ATOM   1890 C  C     . ALA A 1 248 ? 18.80100 -6.21500  25.17500 1.000 21.07830  ? 437 ALA B C     1 
ATOM   1891 O  O     . ALA A 1 248 ? 19.41400 -6.70100  26.13100 1.000 24.96040  ? 437 ALA B O     1 
ATOM   1892 C  CB    . ALA A 1 248 ? 20.67400 -5.32300  23.76900 1.000 23.21748  ? 437 ALA B CB    1 
ATOM   1893 N  N     . ILE A 1 249 ? 17.64400 -6.71000  24.72800 1.000 22.74995  ? 438 ILE B N     1 
ATOM   1894 C  CA    . ILE A 1 249 ? 17.06900 -7.93500  25.27100 1.000 28.83521  ? 438 ILE B CA    1 
ATOM   1895 C  C     . ILE A 1 249 ? 17.40200 -9.15400  24.42600 1.000 26.12365  ? 438 ILE B C     1 
ATOM   1896 O  O     . ILE A 1 249 ? 17.02400 -10.27500 24.78900 1.000 28.72566  ? 438 ILE B O     1 
ATOM   1897 C  CB    . ILE A 1 249 ? 15.54200 -7.80400  25.43900 1.000 29.54176  ? 438 ILE B CB    1 
ATOM   1898 C  CG1   . ILE A 1 249 ? 14.89700 -7.35300  24.12700 1.000 31.28933  ? 438 ILE B CG1   1 
ATOM   1899 C  CG2   . ILE A 1 249 ? 15.21300 -6.84100  26.57100 1.000 23.76852  ? 438 ILE B CG2   1 
ATOM   1900 C  CD1   . ILE A 1 249 ? 13.39600 -7.18200  24.21000 1.000 30.50296  ? 438 ILE B CD1   1 
ATOM   1901 N  N     . LYS A 1 250 ? 18.09600 -8.96700  23.30600 1.000 29.19967  ? 439 LYS B N     1 
ATOM   1902 C  CA    . LYS A 1 250 ? 18.53400 -10.06100 22.45400 1.000 30.79729  ? 439 LYS B CA    1 
ATOM   1903 C  C     . LYS A 1 250 ? 19.94300 -9.76600  21.96300 1.000 28.67584  ? 439 LYS B C     1 
ATOM   1904 O  O     . LYS A 1 250 ? 20.38600 -8.61400  21.93900 1.000 33.66776  ? 439 LYS B O     1 
ATOM   1905 C  CB    . LYS A 1 250 ? 17.58800 -10.26700 21.26200 1.000 29.17398  ? 439 LYS B CB    1 
ATOM   1906 C  CG    . LYS A 1 250 ? 16.14100 -10.54100 21.64400 1.000 29.10494  ? 439 LYS B CG    1 
ATOM   1907 C  CD    . LYS A 1 250 ? 15.29000 -10.79000 20.40900 1.000 31.04350  ? 439 LYS B CD    1 
ATOM   1908 C  CE    . LYS A 1 250 ? 14.35400 -11.97300 20.60100 1.000 45.11391  ? 439 LYS B CE    1 
ATOM   1909 N  NZ    . LYS A 1 250 ? 15.09800 -13.26100 20.71000 1.000 57.95613  ? 439 LYS B NZ    1 
ATOM   1910 N  N     . ASP A 1 251 ? 20.64800 -10.82400 21.57000 1.000 28.90837  ? 440 ASP B N     1 
ATOM   1911 C  CA    . ASP A 1 251 ? 21.99100 -10.68300 21.01800 1.000 31.98550  ? 440 ASP B CA    1 
ATOM   1912 C  C     . ASP A 1 251 ? 21.90600 -10.00100 19.65700 1.000 32.29799  ? 440 ASP B C     1 
ATOM   1913 O  O     . ASP A 1 251 ? 21.44700 -10.60100 18.68000 1.000 41.63302  ? 440 ASP B O     1 
ATOM   1914 C  CB    . ASP A 1 251 ? 22.66400 -12.04800 20.90600 1.000 32.02218  ? 440 ASP B CB    1 
ATOM   1915 C  CG    . ASP A 1 251 ? 22.89100 -12.69700 22.25700 1.000 39.31149  ? 440 ASP B CG    1 
ATOM   1916 O  OD1   . ASP A 1 251 ? 23.19100 -11.96700 23.22500 1.000 35.54689  ? 440 ASP B OD1   1 
ATOM   1917 O  OD2   . ASP A 1 251 ? 22.76600 -13.93800 22.35300 1.000 43.47401  ? 440 ASP B OD2   1 
ATOM   1918 N  N     . ILE A 1 252 ? 22.34500 -8.74800  19.59100 1.000 34.82079  ? 441 ILE B N     1 
ATOM   1919 C  CA    . ILE A 1 252 ? 22.25900 -7.94000  18.38100 1.000 33.04674  ? 441 ILE B CA    1 
ATOM   1920 C  C     . ILE A 1 252 ? 23.60300 -7.99000  17.66700 1.000 35.26049  ? 441 ILE B C     1 
ATOM   1921 O  O     . ILE A 1 252 ? 24.63000 -7.58600  18.22600 1.000 38.44544  ? 441 ILE B O     1 
ATOM   1922 C  CB    . ILE A 1 252 ? 21.85700 -6.49300  18.70500 1.000 31.87095  ? 441 ILE B CB    1 
ATOM   1923 C  CG1   . ILE A 1 252 ? 20.42000 -6.45200  19.22700 1.000 33.18063  ? 441 ILE B CG1   1 
ATOM   1924 C  CG2   . ILE A 1 252 ? 22.02700 -5.60500  17.48100 1.000 31.71821  ? 441 ILE B CG2   1 
ATOM   1925 C  CD1   . ILE A 1 252 ? 20.06600 -5.17000  19.93500 1.000 31.39315  ? 441 ILE B CD1   1 
ATOM   1926 N  N     . GLN A 1 253 ? 23.59500 -8.48100  16.43500 1.000 32.17629  ? 442 GLN B N     1 
ATOM   1927 C  CA    . GLN A 1 253 ? 24.78000 -8.59000  15.60000 1.000 39.71123  ? 442 GLN B CA    1 
ATOM   1928 C  C     . GLN A 1 253 ? 25.01400 -7.29700  14.82900 1.000 35.63227  ? 442 GLN B C     1 
ATOM   1929 O  O     . GLN A 1 253 ? 24.11800 -6.45400  14.72300 1.000 32.66998  ? 442 GLN B O     1 
ATOM   1930 C  CB    . GLN A 1 253 ? 24.63100 -9.76900  14.63900 1.000 43.54325  ? 442 GLN B CB    1 
ATOM   1931 C  CG    . GLN A 1 253 ? 25.15900 -11.08200 15.20000 1.000 42.62346  ? 442 GLN B CG    1 
ATOM   1932 C  CD    . GLN A 1 253 ? 24.46800 -12.29100 14.61100 1.000 46.15479  ? 442 GLN B CD    1 
ATOM   1933 O  OE1   . GLN A 1 253 ? 23.50400 -12.16200 13.85500 1.000 59.56254  ? 442 GLN B OE1   1 
ATOM   1934 N  NE2   . GLN A 1 253 ? 24.95500 -13.47800 14.95300 1.000 49.81966  ? 442 GLN B NE2   1 
ATOM   1935 N  N     . PRO A 1 254 ? 26.22200 -7.09600  14.29800 1.000 37.78202  ? 443 PRO B N     1 
ATOM   1936 C  CA    . PRO A 1 254 ? 26.48300 -5.88500  13.50900 1.000 37.19416  ? 443 PRO B CA    1 
ATOM   1937 C  C     . PRO A 1 254 ? 25.55500 -5.77700  12.30700 1.000 38.49811  ? 443 PRO B C     1 
ATOM   1938 O  O     . PRO A 1 254 ? 25.16500 -6.77700  11.70000 1.000 33.60746  ? 443 PRO B O     1 
ATOM   1939 C  CB    . PRO A 1 254 ? 27.94200 -6.05500  13.07400 1.000 34.10127  ? 443 PRO B CB    1 
ATOM   1940 C  CG    . PRO A 1 254 ? 28.54400 -6.90600  14.13200 1.000 32.66885  ? 443 PRO B CG    1 
ATOM   1941 C  CD    . PRO A 1 254 ? 27.45800 -7.85600  14.55800 1.000 37.49233  ? 443 PRO B CD    1 
ATOM   1942 N  N     . LEU A 1 255 ? 25.19300 -4.53300  11.98500 1.000 34.78107  ? 444 LEU B N     1 
ATOM   1943 C  CA    . LEU A 1 255 ? 24.30500 -4.15000  10.88800 1.000 30.95893  ? 444 LEU B CA    1 
ATOM   1944 C  C     . LEU A 1 255 ? 22.86200 -4.58800  11.10200 1.000 28.80865  ? 444 LEU B C     1 
ATOM   1945 O  O     . LEU A 1 255 ? 22.03500 -4.43100  10.19600 1.000 33.19079  ? 444 LEU B O     1 
ATOM   1946 C  CB    . LEU A 1 255 ? 24.80300 -4.67900  9.53700  1.000 39.88839  ? 444 LEU B CB    1 
ATOM   1947 C  CG    . LEU A 1 255 ? 26.26600 -4.38500  9.20400  1.000 33.34661  ? 444 LEU B CG    1 
ATOM   1948 C  CD1   . LEU A 1 255 ? 26.64500 -4.99900  7.86700  1.000 36.82692  ? 444 LEU B CD1   1 
ATOM   1949 C  CD2   . LEU A 1 255 ? 26.52700 -2.88800  9.20700  1.000 32.32784  ? 444 LEU B CD2   1 
ATOM   1950 N  N     . GLU A 1 256 ? 22.52900 -5.12700  12.27200 1.000 32.01611  ? 445 GLU B N     1 
ATOM   1951 C  CA    . GLU A 1 256 ? 21.15100 -5.48100  12.58000 1.000 36.06514  ? 445 GLU B CA    1 
ATOM   1952 C  C     . GLU A 1 256 ? 20.40700 -4.25000  13.08200 1.000 32.31854  ? 445 GLU B C     1 
ATOM   1953 O  O     . GLU A 1 256 ? 20.92200 -3.50300  13.91900 1.000 23.79375  ? 445 GLU B O     1 
ATOM   1954 C  CB    . GLU A 1 256 ? 21.10600 -6.59700  13.62400 1.000 31.74482  ? 445 GLU B CB    1 
ATOM   1955 C  CG    . GLU A 1 256 ? 19.70500 -7.06200  13.99300 1.000 33.39907  ? 445 GLU B CG    1 
ATOM   1956 C  CD    . GLU A 1 256 ? 19.71500 -8.19300  15.00700 1.000 39.42665  ? 445 GLU B CD    1 
ATOM   1957 O  OE1   . GLU A 1 256 ? 20.60800 -9.06300  14.92300 1.000 41.77981  ? 445 GLU B OE1   1 
ATOM   1958 O  OE2   . GLU A 1 256 ? 18.83300 -8.21000  15.89100 1.000 39.07065  ? 445 GLU B OE2   1 
ATOM   1959 N  N     . GLU A 1 257 ? 19.19800 -4.03800  12.56600 1.000 28.64604  ? 446 GLU B N     1 
ATOM   1960 C  CA    . GLU A 1 257 ? 18.42400 -2.86100  12.93700 1.000 33.78391  ? 446 GLU B CA    1 
ATOM   1961 C  C     . GLU A 1 257 ? 17.96400 -2.95600  14.38800 1.000 32.69812  ? 446 GLU B C     1 
ATOM   1962 O  O     . GLU A 1 257 ? 17.48700 -4.00400  14.83400 1.000 27.14398  ? 446 GLU B O     1 
ATOM   1963 C  CB    . GLU A 1 257 ? 17.21900 -2.70200  12.01200 1.000 28.56756  ? 446 GLU B CB    1 
ATOM   1964 C  CG    . GLU A 1 257 ? 16.67700 -1.28200  11.95600 1.000 32.96030  ? 446 GLU B CG    1 
ATOM   1965 C  CD    . GLU A 1 257 ? 15.25200 -1.21600  11.44300 1.000 38.87937  ? 446 GLU B CD    1 
ATOM   1966 O  OE1   . GLU A 1 257 ? 14.74600 -2.24600  10.94600 1.000 39.73333  ? 446 GLU B OE1   1 
ATOM   1967 O  OE2   . GLU A 1 257 ? 14.63700 -0.13200  11.53900 1.000 29.31730  ? 446 GLU B OE2   1 
ATOM   1968 N  N     . LEU A 1 258 ? 18.10600 -1.85400  15.12100 1.000 28.19765  ? 447 LEU B N     1 
ATOM   1969 C  CA    . LEU A 1 258 ? 17.64700 -1.77300  16.50100 1.000 30.19722  ? 447 LEU B CA    1 
ATOM   1970 C  C     . LEU A 1 258 ? 16.17900 -1.36800  16.52100 1.000 30.70355  ? 447 LEU B C     1 
ATOM   1971 O  O     . LEU A 1 258 ? 15.80100 -0.34900  15.93400 1.000 24.78148  ? 447 LEU B O     1 
ATOM   1972 C  CB    . LEU A 1 258 ? 18.48400 -0.76700  17.29100 1.000 31.86512  ? 447 LEU B CB    1 
ATOM   1973 C  CG    . LEU A 1 258 ? 20.00100 -0.95600  17.24700 1.000 31.59450  ? 447 LEU B CG    1 
ATOM   1974 C  CD1   . LEU A 1 258 ? 20.70000 0.08200   18.11200 1.000 26.65618  ? 447 LEU B CD1   1 
ATOM   1975 C  CD2   . LEU A 1 258 ? 20.37500 -2.35800  17.68300 1.000 32.59006  ? 447 LEU B CD2   1 
ATOM   1976 N  N     . THR A 1 259 ? 15.35400 -2.17400  17.18700 1.000 29.61308  ? 448 THR B N     1 
ATOM   1977 C  CA    . THR A 1 259 ? 13.92100 -1.92500  17.25600 1.000 30.01217  ? 448 THR B CA    1 
ATOM   1978 C  C     . THR A 1 259 ? 13.41600 -2.22000  18.66000 1.000 27.49046  ? 448 THR B C     1 
ATOM   1979 O  O     . THR A 1 259 ? 13.95800 -3.07700  19.36300 1.000 28.38664  ? 448 THR B O     1 
ATOM   1980 C  CB    . THR A 1 259 ? 13.14300 -2.78400  16.24900 1.000 28.88713  ? 448 THR B CB    1 
ATOM   1981 O  OG1   . THR A 1 259 ? 13.43700 -4.16900  16.47400 1.000 27.64531  ? 448 THR B OG1   1 
ATOM   1982 C  CG2   . THR A 1 259 ? 13.50600 -2.41500  14.81500 1.000 34.26280  ? 448 THR B CG2   1 
ATOM   1983 N  N     . PHE A 1 260 ? 12.36400 -1.50800  19.06000 1.000 24.22821  ? 449 PHE B N     1 
ATOM   1984 C  CA    . PHE A 1 260 ? 11.70600 -1.76900  20.33100 1.000 28.26503  ? 449 PHE B CA    1 
ATOM   1985 C  C     . PHE A 1 260 ? 10.19900 -1.73500  20.13000 1.000 27.88968  ? 449 PHE B C     1 
ATOM   1986 O  O     . PHE A 1 260 ? 9.69000  -1.15300  19.16900 1.000 24.29655  ? 449 PHE B O     1 
ATOM   1987 C  CB    . PHE A 1 260 ? 12.13800 -0.77900  21.42800 1.000 23.00629  ? 449 PHE B CB    1 
ATOM   1988 C  CG    . PHE A 1 260 ? 11.57100 0.60500   21.27900 1.000 25.97321  ? 449 PHE B CG    1 
ATOM   1989 C  CD1   . PHE A 1 260 ? 12.12100 1.50400   20.37900 1.000 27.44348  ? 449 PHE B CD1   1 
ATOM   1990 C  CD2   . PHE A 1 260 ? 10.51300 1.02200   22.07200 1.000 28.84848  ? 449 PHE B CD2   1 
ATOM   1991 C  CE1   . PHE A 1 260 ? 11.61000 2.78500   20.25600 1.000 26.77526  ? 449 PHE B CE1   1 
ATOM   1992 C  CE2   . PHE A 1 260 ? 9.99800  2.30100   21.95200 1.000 25.54250  ? 449 PHE B CE2   1 
ATOM   1993 C  CZ    . PHE A 1 260 ? 10.54700 3.18400   21.04400 1.000 23.04151  ? 449 PHE B CZ    1 
ATOM   1994 N  N     . ASP A 1 261 ? 9.48900  -2.39400  21.04300 1.000 32.68209  ? 450 ASP B N     1 
ATOM   1995 C  CA    . ASP A 1 261 ? 8.03200  -2.44100  20.99600 1.000 28.78556  ? 450 ASP B CA    1 
ATOM   1996 C  C     . ASP A 1 261 ? 7.48000  -1.09700  21.45100 1.000 28.79082  ? 450 ASP B C     1 
ATOM   1997 O  O     . ASP A 1 261 ? 7.65600  -0.70600  22.60900 1.000 25.13599  ? 450 ASP B O     1 
ATOM   1998 C  CB    . ASP A 1 261 ? 7.51700  -3.57700  21.87500 1.000 33.14609  ? 450 ASP B CB    1 
ATOM   1999 C  CG    . ASP A 1 261 ? 6.05300  -3.89700  21.62700 1.000 36.59543  ? 450 ASP B CG    1 
ATOM   2000 O  OD1   . ASP A 1 261 ? 5.33600  -3.05500  21.04700 1.000 34.10407  ? 450 ASP B OD1   1 
ATOM   2001 O  OD2   . ASP A 1 261 ? 5.61600  -4.99900  22.02100 1.000 48.50951  ? 450 ASP B OD2   1 
ATOM   2002 N  N     . TYR A 1 262 ? 6.81000  -0.38500  20.53900 1.000 30.96373  ? 451 TYR B N     1 
ATOM   2003 C  CA    . TYR A 1 262 ? 6.24200  0.91300   20.88900 1.000 30.11823  ? 451 TYR B CA    1 
ATOM   2004 C  C     . TYR A 1 262 ? 5.17600  0.78400   21.96900 1.000 35.12532  ? 451 TYR B C     1 
ATOM   2005 O  O     . TYR A 1 262 ? 4.99500  1.70700   22.77400 1.000 30.05966  ? 451 TYR B O     1 
ATOM   2006 C  CB    . TYR A 1 262 ? 5.66000  1.59200   19.64800 1.000 30.92315  ? 451 TYR B CB    1 
ATOM   2007 C  CG    . TYR A 1 262 ? 6.69100  2.18300   18.70600 1.000 30.14302  ? 451 TYR B CG    1 
ATOM   2008 C  CD1   . TYR A 1 262 ? 8.05100  2.02000   18.93600 1.000 27.78940  ? 451 TYR B CD1   1 
ATOM   2009 C  CD2   . TYR A 1 262 ? 6.30100  2.91700   17.59100 1.000 32.17645  ? 451 TYR B CD2   1 
ATOM   2010 C  CE1   . TYR A 1 262 ? 8.99200  2.56100   18.07800 1.000 26.23718  ? 451 TYR B CE1   1 
ATOM   2011 C  CE2   . TYR A 1 262 ? 7.23600  3.46200   16.72900 1.000 30.37687  ? 451 TYR B CE2   1 
ATOM   2012 C  CZ    . TYR A 1 262 ? 8.58000  3.28100   16.97800 1.000 28.76988  ? 451 TYR B CZ    1 
ATOM   2013 O  OH    . TYR A 1 262 ? 9.51500  3.82200   16.12500 1.000 25.99209  ? 451 TYR B OH    1 
ATOM   2014 N  N     . ALA A 1 263 ? 4.45500  -0.34100  21.99800 1.000 34.71730  ? 452 ALA B N     1 
ATOM   2015 C  CA    . ALA A 1 263 ? 3.49600  -0.58000  23.07300 1.000 31.89329  ? 452 ALA B CA    1 
ATOM   2016 C  C     . ALA A 1 263 ? 4.19600  -0.68100  24.42200 1.000 34.24618  ? 452 ALA B C     1 
ATOM   2017 O  O     . ALA A 1 263 ? 3.71700  -0.13400  25.42200 1.000 37.85091  ? 452 ALA B O     1 
ATOM   2018 C  CB    . ALA A 1 263 ? 2.69100  -1.84700  22.78600 1.000 35.09697  ? 452 ALA B CB    1 
ATOM   2019 N  N     . GLY A 1 264 ? 5.24400  -1.49000  24.49100 1.000 41.11400  ? 453 GLY B N     1 
ATOM   2020 C  CA    . GLY A 1 264 ? 5.97600  -1.70500  25.72800 1.000 42.35552  ? 453 GLY B CA    1 
ATOM   2021 C  C     . GLY A 1 264 ? 5.55400  -2.96400  26.47300 1.000 60.24686  ? 453 GLY B C     1 
ATOM   2022 O  O     . GLY A 1 264 ? 4.65900  -2.91800  27.29600 1.000 66.95552  ? 453 GLY B O     1 
ATOM   2023 N  N     . ALA A 1 265 ? 6.18900  -4.09400  26.21000 1.000 60.08427  ? 454 ALA B N     1 
ATOM   2024 C  CA    . ALA A 1 265 ? 5.74100  -5.36100  26.82600 1.000 71.20049  ? 454 ALA B CA    1 
ATOM   2025 C  C     . ALA A 1 265 ? 6.74000  -6.03900  27.73600 1.000 66.53490  ? 454 ALA B C     1 
ATOM   2026 O  O     . ALA A 1 265 ? 6.42500  -7.05900  28.33200 1.000 73.90769  ? 454 ALA B O     1 
ATOM   2027 C  CB    . ALA A 1 265 ? 5.31000  -6.34200  25.74600 1.000 62.72451  ? 454 ALA B CB    1 
ATOM   2028 N  N     . ARG A 1 285 ? 1.10700  4.58500   11.38000 1.000 90.66740  ? 474 ARG B N     1 
ATOM   2029 C  CA    . ARG A 1 285 ? 0.49600  4.68400   10.05900 1.000 89.63992  ? 474 ARG B CA    1 
ATOM   2030 C  C     . ARG A 1 285 ? 0.09300  3.37200   9.38600  1.000 88.18530  ? 474 ARG B C     1 
ATOM   2031 O  O     . ARG A 1 285 ? 0.94500  2.59700   8.94900  1.000 86.27310  ? 474 ARG B O     1 
ATOM   2032 C  CB    . ARG A 1 285 ? 1.45400  5.36500   9.07700  1.000 88.79457  ? 474 ARG B CB    1 
ATOM   2033 C  CG    . ARG A 1 285 ? 2.84400  4.74700   9.01500  1.000 77.24793  ? 474 ARG B CG    1 
ATOM   2034 C  CD    . ARG A 1 285 ? 3.78300  5.56800   8.14700  1.000 73.37109  ? 474 ARG B CD    1 
ATOM   2035 N  NE    . ARG A 1 285 ? 5.01800  4.85200   7.85100  1.000 67.94965  ? 474 ARG B NE    1 
ATOM   2036 C  CZ    . ARG A 1 285 ? 6.00300  5.33600   7.10700  1.000 70.63179  ? 474 ARG B CZ    1 
ATOM   2037 N  NH1   . ARG A 1 285 ? 5.94100  6.54800   6.58100  1.000 74.32204  ? 474 ARG B NH1   1 
ATOM   2038 N  NH2   . ARG A 1 285 ? 7.07700  4.58500   6.88500  1.000 64.74844  ? 474 ARG B NH2   1 
ATOM   2039 N  N     . ARG A 1 286 ? -1.22200 3.14300   9.31900  1.000 94.87944  ? 475 ARG B N     1 
ATOM   2040 C  CA    . ARG A 1 286 ? -1.82100 1.97500   8.67600  1.000 92.50155  ? 475 ARG B CA    1 
ATOM   2041 C  C     . ARG A 1 286 ? -1.11700 0.78500   9.32100  1.000 89.72575  ? 475 ARG B C     1 
ATOM   2042 O  O     . ARG A 1 286 ? -1.07400 0.67600   10.55100 1.000 87.53824  ? 475 ARG B O     1 
ATOM   2043 C  CB    . ARG A 1 286 ? -1.60900 1.94200   7.15900  1.000 95.09693  ? 475 ARG B CB    1 
ATOM   2044 N  N     . GLN A 1 287 ? -0.56500 -0.11200  8.50600  1.000 75.01687  ? 476 GLN B N     1 
ATOM   2045 C  CA    . GLN A 1 287 ? -0.01700 -1.36900  8.99300  1.000 64.08371  ? 476 GLN B CA    1 
ATOM   2046 C  C     . GLN A 1 287 ? 1.44800  -1.36100  9.41200  1.000 59.21285  ? 476 GLN B C     1 
ATOM   2047 O  O     . GLN A 1 287 ? 2.23700  -0.50200  9.00900  1.000 53.76186  ? 476 GLN B O     1 
ATOM   2048 C  CB    . GLN A 1 287 ? -0.23300 -2.39900  7.87500  1.000 56.16473  ? 476 GLN B CB    1 
ATOM   2049 C  CG    . GLN A 1 287 ? -1.67200 -2.88700  7.71400  1.000 73.44305  ? 476 GLN B CG    1 
ATOM   2050 C  CD    . GLN A 1 287 ? -2.16300 -2.78200  6.27800  1.000 75.94840  ? 476 GLN B CD    1 
ATOM   2051 O  OE1   . GLN A 1 287 ? -2.52200 -1.70000  5.81200  1.000 65.70485  ? 476 GLN B OE1   1 
ATOM   2052 N  NE2   . GLN A 1 287 ? -2.18100 -3.90800  5.57200  1.000 81.15323  ? 476 GLN B NE2   1 
ATOM   2053 N  N     . CYS A 1 288 ? 1.79500  -2.34100  10.24400 1.000 55.87582  ? 477 CYS B N     1 
ATOM   2054 C  CA    . CYS A 1 288 ? 3.16100  -2.51200  10.71400 1.000 48.15282  ? 477 CYS B CA    1 
ATOM   2055 C  C     . CYS A 1 288 ? 3.98500  -3.26000  9.67200  1.000 45.18421  ? 477 CYS B C     1 
ATOM   2056 O  O     . CYS A 1 288 ? 3.56300  -4.30500  9.16700  1.000 47.27778  ? 477 CYS B O     1 
ATOM   2057 C  CB    . CYS A 1 288 ? 3.16600  -3.26700  12.04400 1.000 42.08673  ? 477 CYS B CB    1 
ATOM   2058 S  SG    . CYS A 1 288 ? 4.78900  -3.50200  12.79700 1.000 34.45856  ? 477 CYS B SG    1 
ATOM   2059 N  N     . LYS A 1 289 ? 5.16100  -2.72200  9.35200  1.000 40.44216  ? 478 LYS B N     1 
ATOM   2060 C  CA    . LYS A 1 289 ? 6.06400  -3.30700  8.36900  1.000 43.30904  ? 478 LYS B CA    1 
ATOM   2061 C  C     . LYS A 1 289 ? 7.28100  -3.95400  9.02600  1.000 45.19840  ? 478 LYS B C     1 
ATOM   2062 O  O     . LYS A 1 289 ? 8.35400  -4.02600  8.42200  1.000 39.16673  ? 478 LYS B O     1 
ATOM   2063 C  CB    . LYS A 1 289 ? 6.51400  -2.25200  7.35900  1.000 46.16191  ? 478 LYS B CB    1 
ATOM   2064 C  CG    . LYS A 1 289 ? 5.38700  -1.56200  6.60100  1.000 52.32225  ? 478 LYS B CG    1 
ATOM   2065 C  CD    . LYS A 1 289 ? 4.64100  -2.52900  5.69600  1.000 57.27757  ? 478 LYS B CD    1 
ATOM   2066 C  CE    . LYS A 1 289 ? 3.86000  -1.78300  4.62300  1.000 52.47493  ? 478 LYS B CE    1 
ATOM   2067 N  NZ    . LYS A 1 289 ? 3.07800  -0.64700  5.18500  1.000 55.73696  ? 478 LYS B NZ    1 
ATOM   2068 N  N     . CYS A 1 290 ? 7.13100  -4.42600  10.26800 1.000 38.85229  ? 479 CYS B N     1 
ATOM   2069 C  CA    . CYS A 1 290 ? 8.26000  -5.04000  10.95900 1.000 36.33939  ? 479 CYS B CA    1 
ATOM   2070 C  C     . CYS A 1 290 ? 8.65700  -6.36500  10.31900 1.000 44.56984  ? 479 CYS B C     1 
ATOM   2071 O  O     . CYS A 1 290 ? 9.84100  -6.72000  10.31900 1.000 48.56376  ? 479 CYS B O     1 
ATOM   2072 C  CB    . CYS A 1 290 ? 7.93300  -5.24100  12.44000 1.000 32.18045  ? 479 CYS B CB    1 
ATOM   2073 S  SG    . CYS A 1 290 ? 6.81700  -6.61800  12.79900 1.000 41.92099  ? 479 CYS B SG    1 
ATOM   2074 N  N     . GLY A 1 291 ? 7.69500  -7.10300  9.77300  1.000 41.09937  ? 480 GLY B N     1 
ATOM   2075 C  CA    . GLY A 1 291 ? 7.99300  -8.35200  9.10500  1.000 43.52960  ? 480 GLY B CA    1 
ATOM   2076 C  C     . GLY A 1 291 ? 8.19300  -9.54400  10.01200 1.000 41.38268  ? 480 GLY B C     1 
ATOM   2077 O  O     . GLY A 1 291 ? 8.61000  -10.60300 9.52900  1.000 42.83565  ? 480 GLY B O     1 
ATOM   2078 N  N     . SER A 1 292 ? 7.91800  -9.41100  11.30600 1.000 38.38168  ? 481 SER B N     1 
ATOM   2079 C  CA    . SER A 1 292 ? 8.00700  -10.55400 12.20100 1.000 46.49716  ? 481 SER B CA    1 
ATOM   2080 C  C     . SER A 1 292 ? 6.84600  -11.51300 11.95800 1.000 50.07445  ? 481 SER B C     1 
ATOM   2081 O  O     . SER A 1 292 ? 5.77700  -11.12400 11.48100 1.000 47.41186  ? 481 SER B O     1 
ATOM   2082 C  CB    . SER A 1 292 ? 8.01100  -10.09700 13.66000 1.000 43.17860  ? 481 SER B CB    1 
ATOM   2083 O  OG    . SER A 1 292 ? 9.18300  -9.35900  13.95900 1.000 44.34757  ? 481 SER B OG    1 
ATOM   2084 N  N     . ALA A 1 293 ? 7.06900  -12.78500 12.29100 1.000 48.77416  ? 482 ALA B N     1 
ATOM   2085 C  CA    . ALA A 1 293 ? 6.02800  -13.79200 12.13000 1.000 47.38407  ? 482 ALA B CA    1 
ATOM   2086 C  C     . ALA A 1 293 ? 4.88100  -13.61400 13.11500 1.000 48.93011  ? 482 ALA B C     1 
ATOM   2087 O  O     . ALA A 1 293 ? 3.82100  -14.21700 12.91800 1.000 53.44985  ? 482 ALA B O     1 
ATOM   2088 C  CB    . ALA A 1 293 ? 6.62600  -15.19200 12.27700 1.000 44.64824  ? 482 ALA B CB    1 
ATOM   2089 N  N     . ASN A 1 294 ? 5.06400  -12.81000 14.16300 1.000 52.49828  ? 483 ASN B N     1 
ATOM   2090 C  CA    . ASN A 1 294 ? 4.02800  -12.54800 15.15200 1.000 54.34126  ? 483 ASN B CA    1 
ATOM   2091 C  C     . ASN A 1 294 ? 3.56700  -11.09400 15.12000 1.000 47.95600  ? 483 ASN B C     1 
ATOM   2092 O  O     . ASN A 1 294 ? 3.14500  -10.54900 16.14300 1.000 43.72802  ? 483 ASN B O     1 
ATOM   2093 C  CB    . ASN A 1 294 ? 4.52200  -12.91400 16.55000 1.000 49.61497  ? 483 ASN B CB    1 
ATOM   2094 C  CG    . ASN A 1 294 ? 5.70800  -12.07600 16.98500 1.000 57.15665  ? 483 ASN B CG    1 
ATOM   2095 O  OD1   . ASN A 1 294 ? 6.56900  -11.73200 16.17600 1.000 55.36667  ? 483 ASN B OD1   1 
ATOM   2096 N  ND2   . ASN A 1 294 ? 5.75400  -11.73400 18.26900 1.000 67.40370  ? 483 ASN B ND2   1 
ATOM   2097 N  N     . CYS A 1 295 ? 3.64800  -10.45400 13.95500 1.000 55.20978  ? 484 CYS B N     1 
ATOM   2098 C  CA    . CYS A 1 295 ? 3.28000  -9.04800  13.84700 1.000 47.21682  ? 484 CYS B CA    1 
ATOM   2099 C  C     . CYS A 1 295 ? 1.79600  -8.86600  14.12900 1.000 53.21887  ? 484 CYS B C     1 
ATOM   2100 O  O     . CYS A 1 295 ? 0.94900  -9.50500  13.49600 1.000 46.57068  ? 484 CYS B O     1 
ATOM   2101 C  CB    . CYS A 1 295 ? 3.62900  -8.51600  12.45800 1.000 44.77241  ? 484 CYS B CB    1 
ATOM   2102 S  SG    . CYS A 1 295 ? 3.06300  -6.82500  12.14200 1.000 38.53155  ? 484 CYS B SG    1 
ATOM   2103 N  N     . ARG A 1 296 ? 1.48400  -7.99200  15.08700 1.000 45.68932  ? 485 ARG B N     1 
ATOM   2104 C  CA    . ARG A 1 296 ? 0.09900  -7.71800  15.44500 1.000 54.26181  ? 485 ARG B CA    1 
ATOM   2105 C  C     . ARG A 1 296 ? -0.60800 -6.85100  14.41300 1.000 49.07004  ? 485 ARG B C     1 
ATOM   2106 O  O     . ARG A 1 296 ? -1.84300 -6.79900  14.40800 1.000 52.87463  ? 485 ARG B O     1 
ATOM   2107 C  CB    . ARG A 1 296 ? 0.04100  -7.04800  16.82000 1.000 59.05376  ? 485 ARG B CB    1 
ATOM   2108 C  CG    . ARG A 1 296 ? 0.69500  -5.67600  16.87000 1.000 56.04384  ? 485 ARG B CG    1 
ATOM   2109 C  CD    . ARG A 1 296 ? 1.05500  -5.27600  18.29400 1.000 60.20980  ? 485 ARG B CD    1 
ATOM   2110 N  NE    . ARG A 1 296 ? 2.35600  -5.80000  18.69600 1.000 75.02145  ? 485 ARG B NE    1 
ATOM   2111 C  CZ    . ARG A 1 296 ? 2.91300  -5.59700  19.88200 1.000 66.12092  ? 485 ARG B CZ    1 
ATOM   2112 N  NH1   . ARG A 1 296 ? 2.29800  -4.90000  20.82400 1.000 65.90132  ? 485 ARG B NH1   1 
ATOM   2113 N  NH2   . ARG A 1 296 ? 4.11700  -6.10500  20.12900 1.000 50.62489  ? 485 ARG B NH2   1 
ATOM   2114 N  N     . GLY A 1 297 ? 0.14300  -6.17500  13.54400 1.000 48.00078  ? 486 GLY B N     1 
ATOM   2115 C  CA    . GLY A 1 297 ? -0.42600 -5.36000  12.49500 1.000 48.42202  ? 486 GLY B CA    1 
ATOM   2116 C  C     . GLY A 1 297 ? -0.62200 -3.90100  12.84300 1.000 50.53142  ? 486 GLY B C     1 
ATOM   2117 O  O     . GLY A 1 297 ? -0.87600 -3.09600  11.93700 1.000 55.95985  ? 486 GLY B O     1 
ATOM   2118 N  N     . TRP A 1 298 ? -0.50900 -3.53000  14.11700 1.000 48.20854  ? 487 TRP B N     1 
ATOM   2119 C  CA    . TRP A 1 298 ? -0.70800 -2.15500  14.55200 1.000 54.54459  ? 487 TRP B CA    1 
ATOM   2120 C  C     . TRP A 1 298 ? 0.45400  -1.71600  15.42800 1.000 58.17764  ? 487 TRP B C     1 
ATOM   2121 O  O     . TRP A 1 298 ? 0.90900  -2.46700  16.29700 1.000 58.76477  ? 487 TRP B O     1 
ATOM   2122 C  CB    . TRP A 1 298 ? -2.02300 -1.99800  15.32500 1.000 56.51360  ? 487 TRP B CB    1 
ATOM   2123 C  CG    . TRP A 1 298 ? -3.22200 -2.50100  14.58500 1.000 63.39548  ? 487 TRP B CG    1 
ATOM   2124 C  CD1   . TRP A 1 298 ? -3.88600 -3.67300  14.79900 1.000 58.52320  ? 487 TRP B CD1   1 
ATOM   2125 C  CD2   . TRP A 1 298 ? -3.90100 -1.84700  13.50500 1.000 59.93639  ? 487 TRP B CD2   1 
ATOM   2126 N  NE1   . TRP A 1 298 ? -4.93700 -3.79000  13.92300 1.000 61.56020  ? 487 TRP B NE1   1 
ATOM   2127 C  CE2   . TRP A 1 298 ? -4.96800 -2.68200  13.11700 1.000 64.52338  ? 487 TRP B CE2   1 
ATOM   2128 C  CE3   . TRP A 1 298 ? -3.71000 -0.63800  12.83000 1.000 64.71134  ? 487 TRP B CE3   1 
ATOM   2129 C  CZ2   . TRP A 1 298 ? -5.84100 -2.34600  12.08500 1.000 71.10250  ? 487 TRP B CZ2   1 
ATOM   2130 C  CZ3   . TRP A 1 298 ? -4.57800 -0.30600  11.80500 1.000 77.22324  ? 487 TRP B CZ3   1 
ATOM   2131 C  CH2   . TRP A 1 298 ? -5.63100 -1.15600  11.44300 1.000 66.54409  ? 487 TRP B CH2   1 
ATOM   2132 N  N     . LEU A 1 299 ? 0.93500  -0.49400  15.19200 1.000 58.86480  ? 488 LEU B N     1 
ATOM   2133 C  CA    . LEU A 1 299 ? 1.97800  0.07100   16.04100 1.000 58.70069  ? 488 LEU B CA    1 
ATOM   2134 C  C     . LEU A 1 299 ? 1.42600  0.56600   17.37000 1.000 60.65081  ? 488 LEU B C     1 
ATOM   2135 O  O     . LEU A 1 299 ? 2.11500  0.47500   18.39200 1.000 55.21640  ? 488 LEU B O     1 
ATOM   2136 C  CB    . LEU A 1 299 ? 2.68900  1.22000   15.32200 1.000 55.04917  ? 488 LEU B CB    1 
ATOM   2137 C  CG    . LEU A 1 299 ? 3.76300  0.89000   14.28100 1.000 47.92072  ? 488 LEU B CG    1 
ATOM   2138 C  CD1   . LEU A 1 299 ? 3.15700  0.32100   13.01100 1.000 49.24230  ? 488 LEU B CD1   1 
ATOM   2139 C  CD2   . LEU A 1 299 ? 4.57900  2.13100   13.97500 1.000 52.35161  ? 488 LEU B CD2   1 
ATOM   2140 N  N     . PHE A 1 300 ? 0.19700  1.09100   17.37100 1.000 74.15237  ? 489 PHE B N     1 
ATOM   2141 C  CA    . PHE A 1 300 ? -0.41000 1.72600   18.54300 1.000 71.48678  ? 489 PHE B CA    1 
ATOM   2142 C  C     . PHE A 1 300 ? 0.43300  2.89200   19.05500 1.000 65.63379  ? 489 PHE B C     1 
ATOM   2143 O  O     . PHE A 1 300 ? 0.38700  3.23200   20.23900 1.000 72.30851  ? 489 PHE B O     1 
ATOM   2144 C  CB    . PHE A 1 300 ? -0.66100 0.71600   19.66700 1.000 77.11128  ? 489 PHE B CB    1 
ATOM   2145 C  CG    . PHE A 1 300 ? -2.11200 0.38300   19.86700 1.000 87.99026  ? 489 PHE B CG    1 
ATOM   2146 C  CD1   . PHE A 1 300 ? -2.98000 1.31400   20.41500 1.000 89.14954  ? 489 PHE B CD1   1 
ATOM   2147 C  CD2   . PHE A 1 300 ? -2.60700 -0.86200  19.51500 1.000 90.10156  ? 489 PHE B CD2   1 
ATOM   2148 C  CE1   . PHE A 1 300 ? -4.31600 1.01300   20.60100 1.000 89.35459  ? 489 PHE B CE1   1 
ATOM   2149 C  CE2   . PHE A 1 300 ? -3.94200 -1.17000  19.70000 1.000 87.55873  ? 489 PHE B CE2   1 
ATOM   2150 C  CZ    . PHE A 1 300 ? -4.79700 -0.23100  20.24400 1.000 91.92403  ? 489 PHE B CZ    1 
ATOM   2151 N  N     . GLY A 1 301 ? 1.19800  3.51800   18.16500 1.000 55.86367  ? 490 GLY B N     1 
ATOM   2152 C  CA    . GLY A 1 301 ? 2.06200  4.62100   18.53900 1.000 50.22966  ? 490 GLY B CA    1 
ATOM   2153 C  C     . GLY A 1 301 ? 2.92500  5.11500   17.39500 1.000 45.88498  ? 490 GLY B C     1 
ATOM   2154 O  O     . GLY A 1 301 ? 2.49900  5.11200   16.24000 1.000 52.34608  ? 490 GLY B O     1 
ATOM   2155 N  N     . GLN B 2 3   ? -5.35200 4.03300   24.08300 1.000 96.62685  ? 5   GLN F N     1 
ATOM   2156 C  CA    . GLN B 2 3   ? -5.40100 5.32800   24.73400 1.000 97.44353  ? 5   GLN F CA    1 
ATOM   2157 C  C     . GLN B 2 3   ? -4.88900 6.45200   23.86800 1.000 82.93391  ? 5   GLN F C     1 
ATOM   2158 O  O     . GLN B 2 3   ? -5.52700 7.49500   23.77000 1.000 72.60542  ? 5   GLN F O     1 
ATOM   2159 C  CB    . GLN B 2 3   ? -4.53900 5.25300   25.98200 1.000 96.20065  ? 5   GLN F CB    1 
ATOM   2160 C  CG    . GLN B 2 3   ? -4.64100 3.92900   26.71200 1.000 101.79503 ? 5   GLN F CG    1 
ATOM   2161 C  CD    . GLN B 2 3   ? -3.90300 3.94700   28.02900 1.000 110.86015 ? 5   GLN F CD    1 
ATOM   2162 O  OE1   . GLN B 2 3   ? -3.36800 4.97700   28.43400 1.000 110.38324 ? 5   GLN F OE1   1 
ATOM   2163 N  NE2   . GLN B 2 3   ? -3.86600 2.80400   28.70500 1.000 108.02235 ? 5   GLN F NE2   1 
ATOM   2164 N  N     . THR B 2 4   ? -3.77500 6.23100   23.19100 1.000 83.88953  ? 6   THR F N     1 
ATOM   2165 C  CA    . THR B 2 4   ? -3.10200 7.28100   22.43700 1.000 79.47332  ? 6   THR F CA    1 
ATOM   2166 C  C     . THR B 2 4   ? -2.34000 6.64000   21.28700 1.000 78.85692  ? 6   THR F C     1 
ATOM   2167 O  O     . THR B 2 4   ? -2.07100 5.43700   21.28700 1.000 84.10514  ? 6   THR F O     1 
ATOM   2168 C  CB    . THR B 2 4   ? -2.11200 8.13000   23.25300 1.000 76.09154  ? 6   THR F CB    1 
ATOM   2169 O  OG1   . THR B 2 4   ? -1.24900 7.27300   24.01200 1.000 71.95494  ? 6   THR F OG1   1 
ATOM   2170 C  CG2   . THR B 2 4   ? -2.82500 9.10600   24.18600 1.000 69.83516  ? 6   THR F CG2   1 
ATOM   2171 N  N     . ALA B 2 5   ? -1.99400 7.46700   20.30600 1.000 64.81577  ? 7   ALA F N     1 
ATOM   2172 C  CA    . ALA B 2 5   ? -1.02700 7.08700   19.27700 1.000 57.25975  ? 7   ALA F CA    1 
ATOM   2173 C  C     . ALA B 2 5   ? 0.37700  7.51300   19.69400 1.000 52.78267  ? 7   ALA F C     1 
ATOM   2174 O  O     . ALA B 2 5   ? 1.07600  8.23300   18.98300 1.000 52.22760  ? 7   ALA F O     1 
ATOM   2175 C  CB    . ALA B 2 5   ? -1.41400 7.70900   17.94000 1.000 52.50224  ? 7   ALA F CB    1 
ATOM   2176 N  N     . ARG B 2 6   ? 0.79400  7.06000   20.87100 1.000 48.96717  ? 8   ARG F N     1 
ATOM   2177 C  CA    . ARG B 2 6   ? 2.06200  7.47600   21.45700 1.000 48.69474  ? 8   ARG F CA    1 
ATOM   2178 C  C     . ARG B 2 6   ? 2.82800  6.28100   22.01300 1.000 42.19627  ? 8   ARG F C     1 
ATOM   2179 O  O     . ARG B 2 6   ? 2.23100  5.31500   22.49100 1.000 41.84194  ? 8   ARG F O     1 
ATOM   2180 C  CB    . ARG B 2 6   ? 1.84000  8.52400   22.55400 1.000 44.76818  ? 8   ARG F CB    1 
ATOM   2181 C  CG    . ARG B 2 6   ? 1.63000  9.93000   22.01200 1.000 45.88061  ? 8   ARG F CG    1 
ATOM   2182 C  CD    . ARG B 2 6   ? 0.44000  10.64800  22.63500 1.000 48.15176  ? 8   ARG F CD    1 
ATOM   2183 N  NE    . ARG B 2 6   ? 0.66600  11.04300  24.02100 1.000 48.58529  ? 8   ARG F NE    1 
ATOM   2184 C  CZ    . ARG B 2 6   ? -0.03000 11.98300  24.64900 1.000 44.99657  ? 8   ARG F CZ    1 
ATOM   2185 N  NH1   . ARG B 2 6   ? -0.97900 12.66900  24.03300 1.000 44.00131  ? 8   ARG F NH1   1 
ATOM   2186 N  NH2   . ARG B 2 6   ? 0.23700  12.24400  25.92500 1.000 42.47474  ? 8   ARG F NH2   1 
HETATM 2187 N  N     . NLE B 2 7   ? 4.15300  6.35200   21.93800 1.000 31.85381  ? 9   NLE F N     1 
HETATM 2188 C  CA    . NLE B 2 7   ? 5.00800  5.29700   22.46600 1.000 34.97504  ? 9   NLE F CA    1 
HETATM 2189 C  C     . NLE B 2 7   ? 4.87900  5.22700   23.98300 1.000 29.70635  ? 9   NLE F C     1 
HETATM 2190 O  O     . NLE B 2 7   ? 4.79500  6.25300   24.65700 1.000 30.34218  ? 9   NLE F O     1 
HETATM 2191 C  CB    . NLE B 2 7   ? 6.46500  5.52500   22.05700 1.000 28.68708  ? 9   NLE F CB    1 
HETATM 2192 C  CG    . NLE B 2 7   ? 6.70400  5.44000   20.55600 1.000 30.91395  ? 9   NLE F CG    1 
HETATM 2193 C  CD    . NLE B 2 7   ? 8.13300  5.80800   20.19400 1.000 27.27631  ? 9   NLE F CD    1 
HETATM 2194 C  CE    . NLE B 2 7   ? 8.43000  7.25700   20.54000 1.000 27.48223  ? 9   NLE F CE    1 
ATOM   2195 N  N     . SER B 2 8   ? 4.85500  4.00800   24.51000 1.000 25.41635  ? 10  SER F N     1 
ATOM   2196 C  CA    . SER B 2 8   ? 4.68200  3.79200   25.94100 1.000 31.41269  ? 10  SER F CA    1 
ATOM   2197 C  C     . SER B 2 8   ? 5.77000  2.89500   26.51000 1.000 28.53136  ? 10  SER F C     1 
ATOM   2198 O  O     . SER B 2 8   ? 6.35100  2.07200   25.80100 1.000 28.94544  ? 10  SER F O     1 
ATOM   2199 C  CB    . SER B 2 8   ? 3.30400  3.18400   26.22600 1.000 33.95316  ? 10  SER F CB    1 
ATOM   2200 O  OG    . SER B 2 8   ? 3.20900  2.72100   27.56300 1.000 26.51567  ? 10  SER F OG    1 
ATOM   2201 N  N     . THR B 2 9   ? 6.04500  3.06100   27.80200 1.000 26.00573  ? 11  THR F N     1 
ATOM   2202 C  CA    . THR B 2 9   ? 6.97800  2.17200   28.47600 1.000 32.51200  ? 11  THR F CA    1 
ATOM   2203 C  C     . THR B 2 9   ? 6.34900  0.83200   28.83000 1.000 36.59791  ? 11  THR F C     1 
ATOM   2204 O  O     . THR B 2 9   ? 7.07700  -0.10200  29.18100 1.000 37.08559  ? 11  THR F O     1 
ATOM   2205 C  CB    . THR B 2 9   ? 7.52200  2.82400   29.75100 1.000 30.67455  ? 11  THR F CB    1 
ATOM   2206 O  OG1   . THR B 2 9   ? 6.54300  2.72600   30.79200 1.000 36.30897  ? 11  THR F OG1   1 
ATOM   2207 C  CG2   . THR B 2 9   ? 7.84400  4.29100   29.50600 1.000 32.89681  ? 11  THR F CG2   1 
ATOM   2208 N  N     . GLY B 2 10  ? 5.02500  0.71600   28.74200 1.000 37.47098  ? 12  GLY F N     1 
ATOM   2209 C  CA    . GLY B 2 10  ? 4.33000  -0.48800  29.13500 1.000 37.67372  ? 12  GLY F CA    1 
ATOM   2210 C  C     . GLY B 2 10  ? 4.06400  -0.61500  30.61700 1.000 38.48197  ? 12  GLY F C     1 
ATOM   2211 O  O     . GLY B 2 10  ? 3.46000  -1.61000  31.03700 1.000 44.92221  ? 12  GLY F O     1 
ATOM   2212 N  N     . GLY B 2 11  ? 4.49000  0.35500   31.42100 1.000 42.00900  ? 13  GLY F N     1 
ATOM   2213 C  CA    . GLY B 2 11  ? 4.29800  0.29900   32.85300 1.000 43.72210  ? 13  GLY F CA    1 
ATOM   2214 C  C     . GLY B 2 11  ? 5.30200  -0.61300  33.53200 1.000 53.93316  ? 13  GLY F C     1 
ATOM   2215 O  O     . GLY B 2 11  ? 6.06100  -1.34900  32.90000 1.000 54.64629  ? 13  GLY F O     1 
ATOM   2216 N  N     . CYS B 2 12  ? 5.28700  -0.59200  34.86100 1.000 63.71396  ? 14  CYS F N     1 
ATOM   2217 C  CA    . CYS B 2 12  ? 6.28000  -1.34500  35.64000 1.000 64.12961  ? 14  CYS F CA    1 
ATOM   2218 C  C     . CYS B 2 12  ? 5.87400  -2.74800  36.06300 1.000 68.68915  ? 14  CYS F C     1 
ATOM   2219 O  O     . CYS B 2 12  ? 6.57600  -3.37900  36.82700 1.000 72.19496  ? 14  CYS F O     1 
ATOM   2220 C  CB    . CYS B 2 12  ? 6.72000  -0.50600  36.85700 1.000 61.18726  ? 14  CYS F CB    1 
ATOM   2221 S  SG    . CYS B 2 12  ? 5.49900  -0.14500  38.13600 1.000 76.70601  ? 14  CYS F SG    1 
ATOM   2222 N  N     . ALA B 2 13  ? 4.73500  -3.20500  35.57400 1.000 73.56177  ? 15  ALA F N     1 
ATOM   2223 C  CA    . ALA B 2 13  ? 4.29100  -4.55300  35.84000 1.000 83.42661  ? 15  ALA F CA    1 
ATOM   2224 C  C     . ALA B 2 13  ? 5.41000  -5.45100  35.47200 1.000 94.36228  ? 15  ALA F C     1 
ATOM   2225 O  O     . ALA B 2 13  ? 5.85000  -5.47200  34.33100 1.000 96.46655  ? 15  ALA F O     1 
ATOM   2226 C  CB    . ALA B 2 13  ? 3.07400  -4.88100  35.01100 1.000 82.94359  ? 15  ALA F CB    1 
ATOM   2227 N  N     . PRO B 2 14  ? 5.85900  -6.24200  36.42500 1.000 105.28940 ? 16  PRO F N     1 
ATOM   2228 C  CA    . PRO B 2 14  ? 7.04800  -7.03100  36.16800 1.000 108.54730 ? 16  PRO F CA    1 
ATOM   2229 C  C     . PRO B 2 14  ? 6.91500  -8.29600  35.35900 1.000 120.09889 ? 16  PRO F C     1 
ATOM   2230 O  O     . PRO B 2 14  ? 5.99300  -9.07200  35.57400 1.000 125.44225 ? 16  PRO F O     1 
ATOM   2231 C  CB    . PRO B 2 14  ? 7.43700  -7.48600  37.57500 1.000 106.80630 ? 16  PRO F CB    1 
ATOM   2232 C  CG    . PRO B 2 14  ? 6.14300  -7.62200  38.28900 1.000 105.21052 ? 16  PRO F CG    1 
ATOM   2233 C  CD    . PRO B 2 14  ? 5.24200  -6.56100  37.72200 1.000 109.03823 ? 16  PRO F CD    1 
ATOM   2234 N  N     . ARG B 2 15  ? 7.81800  -8.48300  34.41200 1.000 130.08372 ? 17  ARG F N     1 
ATOM   2235 C  CA    . ARG B 2 15  ? 7.87500  -9.70100  33.62100 1.000 137.85459 ? 17  ARG F CA    1 
ATOM   2236 C  C     . ARG B 2 15  ? 9.33100  -9.70500  33.21400 1.000 131.01860 ? 17  ARG F C     1 
ATOM   2237 O  O     . ARG B 2 15  ? 9.73600  -10.47300 32.33900 1.000 121.86890 ? 17  ARG F O     1 
ATOM   2238 C  CB    . ARG B 2 15  ? 6.93200  -9.53400  32.45900 1.000 132.57142 ? 17  ARG F CB    1 
ATOM   2239 C  CG    . ARG B 2 15  ? 6.30400  -10.83100 31.97600 1.000 121.25404 ? 17  ARG F CG    1 
ATOM   2240 C  CD    . ARG B 2 15  ? 5.49000  -11.49500 33.07500 1.000 120.10426 ? 17  ARG F CD    1 
ATOM   2241 N  NE    . ARG B 2 15  ? 5.41600  -12.94200 32.90700 1.000 126.87298 ? 17  ARG F NE    1 
ATOM   2242 C  CZ    . ARG B 2 15  ? 6.46900  -13.75100 32.90600 1.000 135.74794 ? 17  ARG F CZ    1 
ATOM   2243 N  NH1   . ARG B 2 15  ? 7.68900  -13.26100 33.06800 1.000 139.25062 ? 17  ARG F NH1   1 
ATOM   2244 N  NH2   . ARG B 2 15  ? 6.30100  -15.05300 32.74200 1.000 138.73962 ? 17  ARG F NH2   1 
ATOM   2245 N  N     . LYS B 2 16  ? 10.12400 -8.86000  33.87000 1.000 125.49892 ? 18  LYS F N     1 
ATOM   2246 C  CA    . LYS B 2 16  ? 11.56100 -8.68300  33.57200 1.000 104.73098 ? 18  LYS F CA    1 
ATOM   2247 C  C     . LYS B 2 16  ? 11.75700 -8.00800  32.21300 1.000 89.11227  ? 18  LYS F C     1 
ATOM   2248 O  O     . LYS B 2 16  ? 11.83300 -8.67100  31.18600 1.000 88.88533  ? 18  LYS F O     1 
ATOM   2249 C  CB    . LYS B 2 16  ? 12.35900 -9.98300  33.72500 1.000 101.56221 ? 18  LYS F CB    1 
ATOM   2250 C  CG    . LYS B 2 16  ? 12.92700 -10.16300 35.11700 1.000 107.45574 ? 18  LYS F CG    1 
ATOM   2251 C  CD    . LYS B 2 16  ? 12.47800 -9.03900  36.03200 1.000 102.43979 ? 18  LYS F CD    1 
ATOM   2252 C  CE    . LYS B 2 16  ? 11.44200 -9.50600  37.03800 1.000 105.40529 ? 18  LYS F CE    1 
ATOM   2253 N  NZ    . LYS B 2 16  ? 11.49900 -8.70700  38.29100 1.000 104.51524 ? 18  LYS F NZ    1 
ATOM   2254 N  N     . GLN B 2 17  ? 11.85700 -6.68800  32.22400 1.000 71.28174  ? 19  GLN F N     1 
ATOM   2255 C  CA    . GLN B 2 17  ? 11.95400 -5.94900  30.97500 1.000 69.18033  ? 19  GLN F CA    1 
ATOM   2256 C  C     . GLN B 2 17  ? 13.07500 -6.47600  30.08500 1.000 60.76647  ? 19  GLN F C     1 
ATOM   2257 O  O     . GLN B 2 17  ? 12.91000 -6.54700  28.87500 1.000 59.00520  ? 19  GLN F O     1 
ATOM   2258 C  CB    . GLN B 2 17  ? 12.09000 -4.43700  31.24500 1.000 47.41684  ? 19  GLN F CB    1 
ATOM   2259 C  CG    . GLN B 2 17  ? 10.89400 -3.83500  31.94200 1.000 55.53646  ? 19  GLN F CG    1 
ATOM   2260 C  CD    . GLN B 2 17  ? 10.07400 -2.95400  31.02900 1.000 58.92949  ? 19  GLN F CD    1 
ATOM   2261 O  OE1   . GLN B 2 17  ? 10.33800 -2.87000  29.83100 1.000 59.75033  ? 19  GLN F OE1   1 
ATOM   2262 N  NE2   . GLN B 2 17  ? 9.07100  -2.28900  31.59200 1.000 60.19755  ? 19  GLN F NE2   1 
HETATM 2263 N  N     . SAM C 3 .   ? 12.68500 8.21000   13.04100 1.000 41.42258  ? 501 SAM B N     1 
HETATM 2264 C  CA    . SAM C 3 .   ? 12.38900 7.57900   11.76100 1.000 38.93843  ? 501 SAM B CA    1 
HETATM 2265 C  C     . SAM C 3 .   ? 11.90700 8.60200   10.74000 1.000 39.12435  ? 501 SAM B C     1 
HETATM 2266 O  O     . SAM C 3 .   ? 11.91700 8.34800   9.53500  1.000 42.01483  ? 501 SAM B O     1 
HETATM 2267 O  OXT   . SAM C 3 .   ? 11.50700 9.71000   11.09800 1.000 38.61004  ? 501 SAM B OXT   1 
HETATM 2268 C  CB    . SAM C 3 .   ? 11.35900 6.47000   11.95000 1.000 42.04735  ? 501 SAM B CB    1 
HETATM 2269 C  CG    . SAM C 3 .   ? 10.96900 6.19500   13.40100 1.000 38.01779  ? 501 SAM B CG    1 
HETATM 2270 S  SD    . SAM C 3 .   ? 9.87000  7.43500   14.12900 1.000 45.60936  ? 501 SAM B SD    1 
HETATM 2271 C  CE    . SAM C 3 .   ? 10.33400 7.33300   15.87400 1.000 43.62710  ? 501 SAM B CE    1 
HETATM 2272 C  "C5'" . SAM C 3 .   ? 8.33500  6.49100   14.25900 1.000 41.45610  ? 501 SAM B "C5'" 1 
HETATM 2273 C  "C4'" . SAM C 3 .   ? 7.54700  6.42900   12.96300 1.000 46.54526  ? 501 SAM B "C4'" 1 
HETATM 2274 O  "O4'" . SAM C 3 .   ? 8.12100  5.47300   12.08900 1.000 43.39435  ? 501 SAM B "O4'" 1 
HETATM 2275 C  "C3'" . SAM C 3 .   ? 6.12100  5.99800   13.24800 1.000 47.64849  ? 501 SAM B "C3'" 1 
HETATM 2276 O  "O3'" . SAM C 3 .   ? 5.25000  7.09500   13.15600 1.000 45.77114  ? 501 SAM B "O3'" 1 
HETATM 2277 C  "C2'" . SAM C 3 .   ? 5.79400  4.98400   12.18400 1.000 54.53004  ? 501 SAM B "C2'" 1 
HETATM 2278 O  "O2'" . SAM C 3 .   ? 5.00100  5.59500   11.20100 1.000 63.99724  ? 501 SAM B "O2'" 1 
HETATM 2279 C  "C1'" . SAM C 3 .   ? 7.12900  4.60400   11.57700 1.000 49.02745  ? 501 SAM B "C1'" 1 
HETATM 2280 N  N9    . SAM C 3 .   ? 7.42300  3.22000   11.98000 1.000 48.37746  ? 501 SAM B N9    1 
HETATM 2281 C  C8    . SAM C 3 .   ? 8.16800  2.83600   13.06600 1.000 41.15005  ? 501 SAM B C8    1 
HETATM 2282 N  N7    . SAM C 3 .   ? 8.19400  1.48700   13.10400 1.000 40.43864  ? 501 SAM B N7    1 
HETATM 2283 C  C5    . SAM C 3 .   ? 7.46900  1.00600   12.07500 1.000 43.19028  ? 501 SAM B C5    1 
HETATM 2284 C  C6    . SAM C 3 .   ? 7.17800  -0.28700  11.66900 1.000 42.08408  ? 501 SAM B C6    1 
HETATM 2285 N  N6    . SAM C 3 .   ? 7.65200  -1.32700  12.35100 1.000 39.32481  ? 501 SAM B N6    1 
HETATM 2286 N  N1    . SAM C 3 .   ? 6.39500  -0.48000  10.55300 1.000 43.67456  ? 501 SAM B N1    1 
HETATM 2287 C  C2    . SAM C 3 .   ? 5.90400  0.60300   9.85100  1.000 43.44104  ? 501 SAM B C2    1 
HETATM 2288 N  N3    . SAM C 3 .   ? 6.20000  1.88700   10.26100 1.000 46.95357  ? 501 SAM B N3    1 
HETATM 2289 C  C4    . SAM C 3 .   ? 6.97400  2.08400   11.35600 1.000 46.88158  ? 501 SAM B C4    1 
HETATM 2290 ZN ZN    . ZN  D 4 .   ? 24.37700 6.13400   45.13300 1.000 31.45643  ? 502 ZN  B ZN    1 
HETATM 2291 ZN ZN    . ZN  E 4 .   ? 26.14900 3.32500   46.88500 1.000 38.21817  ? 503 ZN  B ZN    1 
HETATM 2292 ZN ZN    . ZN  F 4 .   ? 27.38100 4.59700   43.43700 1.000 41.55119  ? 504 ZN  B ZN    1 
HETATM 2293 ZN ZN    . ZN  G 4 .   ? 4.72800  -5.76100  13.37400 1.000 35.88022  ? 505 ZN  B ZN    1 
HETATM 2294 O  O     . HOH H 5 .   ? 28.85900 -0.80300  47.47900 1.000 49.83583  ? 601 HOH B O     1 
HETATM 2295 O  O     . HOH H 5 .   ? 20.49000 7.80200   43.71200 1.000 38.02348  ? 602 HOH B O     1 
HETATM 2296 O  O     . HOH H 5 .   ? 13.13400 27.73100  1.83900  1.000 78.21926  ? 603 HOH B O     1 
HETATM 2297 O  O     . HOH H 5 .   ? 31.37900 -3.16200  42.81000 1.000 45.83656  ? 604 HOH B O     1 
HETATM 2298 O  O     . HOH H 5 .   ? 10.55900 -4.51900  8.26500  1.000 43.25609  ? 605 HOH B O     1 
HETATM 2299 O  O     . HOH H 5 .   ? 25.96100 -10.72400 31.88300 1.000 29.34533  ? 606 HOH B O     1 
HETATM 2300 O  O     . HOH H 5 .   ? 23.21300 -12.78700 25.35800 1.000 30.50951  ? 607 HOH B O     1 
HETATM 2301 O  O     . HOH H 5 .   ? 22.54100 -0.68000  3.20300  1.000 46.23683  ? 608 HOH B O     1 
HETATM 2302 O  O     . HOH H 5 .   ? 5.45600  21.59500  27.75600 1.000 33.36773  ? 609 HOH B O     1 
HETATM 2303 O  O     . HOH H 5 .   ? 17.73100 23.26100  0.01500  1.000 59.15652  ? 610 HOH B O     1 
HETATM 2304 O  O     . HOH H 5 .   ? 12.94500 23.70900  4.34900  1.000 88.01900  ? 611 HOH B O     1 
HETATM 2305 O  O     . HOH H 5 .   ? 17.36000 11.02700  30.44500 1.000 21.99932  ? 612 HOH B O     1 
HETATM 2306 O  O     . HOH H 5 .   ? 14.49000 23.76000  27.94900 1.000 30.68019  ? 613 HOH B O     1 
HETATM 2307 O  O     . HOH H 5 .   ? 16.20000 -2.90300  49.01500 1.000 46.48893  ? 614 HOH B O     1 
HETATM 2308 O  O     . HOH H 5 .   ? 22.83000 10.55700  20.40600 1.000 27.41969  ? 615 HOH B O     1 
HETATM 2309 O  O     . HOH H 5 .   ? 33.06700 -0.64000  42.85700 1.000 49.44989  ? 616 HOH B O     1 
HETATM 2310 O  O     . HOH H 5 .   ? 15.06700 11.70800  49.26400 1.000 50.95634  ? 617 HOH B O     1 
HETATM 2311 O  O     . HOH H 5 .   ? 15.07800 21.83200  15.95000 1.000 23.88897  ? 618 HOH B O     1 
HETATM 2312 O  O     . HOH H 5 .   ? 10.82600 21.50600  41.43000 1.000 39.48451  ? 619 HOH B O     1 
HETATM 2313 O  O     . HOH H 5 .   ? 16.39500 -7.48100  32.98500 1.000 30.69460  ? 620 HOH B O     1 
HETATM 2314 O  O     . HOH H 5 .   ? 25.48400 2.30600   23.91300 1.000 25.64308  ? 621 HOH B O     1 
HETATM 2315 O  O     . HOH H 5 .   ? 28.81200 20.15200  -0.75100 1.000 46.93905  ? 622 HOH B O     1 
HETATM 2316 O  O     . HOH H 5 .   ? 11.17400 -2.79100  12.06600 1.000 23.40545  ? 623 HOH B O     1 
HETATM 2317 O  O     . HOH H 5 .   ? 5.29600  -6.76500  9.49100  1.000 40.64904  ? 624 HOH B O     1 
HETATM 2318 O  O     . HOH H 5 .   ? 11.52400 14.93400  11.34900 1.000 36.37500  ? 625 HOH B O     1 
HETATM 2319 O  O     . HOH H 5 .   ? 9.67100  14.99000  44.41200 1.000 61.77872  ? 626 HOH B O     1 
HETATM 2320 O  O     . HOH H 5 .   ? 16.46100 18.55900  40.60200 1.000 42.79580  ? 627 HOH B O     1 
HETATM 2321 O  O     . HOH H 5 .   ? 2.29600  9.96000   30.67400 1.000 33.35845  ? 628 HOH B O     1 
HETATM 2322 O  O     . HOH H 5 .   ? 21.94400 18.74000  16.49400 1.000 26.63841  ? 629 HOH B O     1 
HETATM 2323 O  O     . HOH H 5 .   ? 2.32700  2.47800   31.80800 1.000 39.47230  ? 630 HOH B O     1 
HETATM 2324 O  O     . HOH H 5 .   ? 15.56900 10.18500  21.32300 1.000 22.91868  ? 631 HOH B O     1 
HETATM 2325 O  O     . HOH H 5 .   ? 21.65500 -15.35300 24.10700 1.000 37.83187  ? 632 HOH B O     1 
HETATM 2326 O  O     . HOH H 5 .   ? 9.22600  -2.57600  48.21600 1.000 51.78341  ? 633 HOH B O     1 
HETATM 2327 O  O     . HOH H 5 .   ? 17.64800 19.84700  -2.45600 1.000 37.19556  ? 634 HOH B O     1 
HETATM 2328 O  O     . HOH H 5 .   ? 5.47200  7.99500   35.08900 1.000 31.63747  ? 635 HOH B O     1 
HETATM 2329 O  O     . HOH H 5 .   ? 7.99100  -5.27500  43.85000 1.000 40.96437  ? 636 HOH B O     1 
HETATM 2330 O  O     . HOH H 5 .   ? 25.00800 9.64100   3.99800  1.000 39.35548  ? 637 HOH B O     1 
HETATM 2331 O  O     . HOH H 5 .   ? 5.43900  11.69400  33.62100 1.000 28.21135  ? 638 HOH B O     1 
HETATM 2332 O  O     . HOH H 5 .   ? 17.49400 -11.83700 42.35000 1.000 45.12838  ? 639 HOH B O     1 
HETATM 2333 O  O     . HOH H 5 .   ? 27.14700 3.22200   29.52000 1.000 25.63861  ? 640 HOH B O     1 
HETATM 2334 O  O     . HOH H 5 .   ? 28.21100 -0.84200  31.39500 1.000 23.78615  ? 641 HOH B O     1 
HETATM 2335 O  O     . HOH H 5 .   ? 10.99500 -3.46700  23.62900 1.000 28.89748  ? 642 HOH B O     1 
HETATM 2336 O  O     . HOH H 5 .   ? 24.60200 -8.04400  40.49500 1.000 28.79615  ? 643 HOH B O     1 
HETATM 2337 O  O     . HOH H 5 .   ? 11.06600 17.88900  20.10000 1.000 23.73765  ? 644 HOH B O     1 
HETATM 2338 O  O     . HOH H 5 .   ? 13.56900 14.18400  10.01700 1.000 36.30780  ? 645 HOH B O     1 
HETATM 2339 O  O     . HOH H 5 .   ? 15.71600 9.49600   28.38600 1.000 24.27993  ? 646 HOH B O     1 
HETATM 2340 O  O     . HOH H 5 .   ? 6.20600  14.05000  17.91500 1.000 25.62127  ? 647 HOH B O     1 
HETATM 2341 O  O     . HOH H 5 .   ? 28.49100 -1.07700  35.71500 1.000 36.44936  ? 648 HOH B O     1 
HETATM 2342 O  O     . HOH H 5 .   ? 26.21600 12.57000  39.02400 1.000 32.73881  ? 649 HOH B O     1 
HETATM 2343 O  O     . HOH H 5 .   ? 14.28900 -6.37100  15.16500 1.000 34.91158  ? 650 HOH B O     1 
HETATM 2344 O  O     . HOH H 5 .   ? 29.26500 13.85700  46.30300 1.000 46.43404  ? 651 HOH B O     1 
HETATM 2345 O  O     . HOH H 5 .   ? 11.25200 16.66400  44.11300 1.000 53.58457  ? 652 HOH B O     1 
HETATM 2346 O  O     . HOH H 5 .   ? 23.86800 8.79000   22.43000 1.000 34.39556  ? 653 HOH B O     1 
HETATM 2347 O  O     . HOH H 5 .   ? 0.03400  1.43700   13.44800 1.000 55.25546  ? 654 HOH B O     1 
HETATM 2348 O  O     . HOH H 5 .   ? -2.33600 14.56000  26.08600 1.000 42.68871  ? 655 HOH B O     1 
HETATM 2349 O  O     . HOH H 5 .   ? 28.83300 24.76500  7.01600  1.000 43.80583  ? 656 HOH B O     1 
HETATM 2350 O  O     . HOH H 5 .   ? 1.22100  23.40000  28.88600 1.000 38.66106  ? 657 HOH B O     1 
HETATM 2351 O  O     . HOH H 5 .   ? 20.63200 -0.70600  40.31200 1.000 25.39757  ? 658 HOH B O     1 
HETATM 2352 O  O     . HOH H 5 .   ? 25.01700 6.45100   1.96000  1.000 39.66517  ? 659 HOH B O     1 
HETATM 2353 O  O     . HOH H 5 .   ? 18.14300 -0.59400  4.15300  1.000 35.67707  ? 660 HOH B O     1 
HETATM 2354 O  O     . HOH H 5 .   ? 24.45500 -6.32100  42.87400 1.000 27.42496  ? 661 HOH B O     1 
HETATM 2355 O  O     . HOH H 5 .   ? 25.79500 -2.28700  28.98700 1.000 26.99871  ? 662 HOH B O     1 
HETATM 2356 O  O     . HOH H 5 .   ? 19.30800 19.37300  26.66000 1.000 28.98650  ? 663 HOH B O     1 
HETATM 2357 O  O     . HOH H 5 .   ? 19.79700 2.59300   3.24400  1.000 32.82377  ? 664 HOH B O     1 
HETATM 2358 O  O     . HOH H 5 .   ? 7.25900  12.74800  41.38200 1.000 43.36024  ? 665 HOH B O     1 
HETATM 2359 O  O     . HOH H 5 .   ? 13.59600 14.86600  4.70600  1.000 39.47614  ? 666 HOH B O     1 
HETATM 2360 O  O     . HOH H 5 .   ? 18.13900 -5.83100  10.55600 1.000 24.40472  ? 667 HOH B O     1 
HETATM 2361 O  O     . HOH H 5 .   ? 12.29700 22.27700  49.07500 1.000 38.87954  ? 668 HOH B O     1 
HETATM 2362 O  O     . HOH H 5 .   ? 12.79400 -3.13300  38.89500 1.000 32.81108  ? 669 HOH B O     1 
HETATM 2363 O  O     . HOH H 5 .   ? 18.09600 24.13400  11.25100 1.000 37.76796  ? 670 HOH B O     1 
HETATM 2364 O  O     . HOH H 5 .   ? 19.43500 -8.78800  30.74000 1.000 22.19273  ? 671 HOH B O     1 
HETATM 2365 O  O     . HOH H 5 .   ? 26.92800 0.54200   27.09800 1.000 33.33741  ? 672 HOH B O     1 
HETATM 2366 O  O     . HOH H 5 .   ? 3.65400  25.51600  22.28500 1.000 55.36888  ? 673 HOH B O     1 
HETATM 2367 O  O     . HOH H 5 .   ? -0.71500 -8.76900  11.10400 1.000 47.46291  ? 674 HOH B O     1 
HETATM 2368 O  O     . HOH H 5 .   ? 19.09100 17.32700  49.68800 1.000 40.58675  ? 675 HOH B O     1 
HETATM 2369 O  O     . HOH H 5 .   ? 13.25200 20.43900  7.74400  1.000 45.08407  ? 676 HOH B O     1 
HETATM 2370 O  O     . HOH H 5 .   ? 22.76400 20.60600  19.14300 1.000 26.99411  ? 677 HOH B O     1 
HETATM 2371 O  O     . HOH H 5 .   ? 10.23500 -1.45000  25.47000 1.000 21.11807  ? 678 HOH B O     1 
HETATM 2372 O  O     . HOH H 5 .   ? 13.19300 11.86200  9.81800  1.000 29.57242  ? 679 HOH B O     1 
HETATM 2373 O  O     . HOH H 5 .   ? 17.95900 21.43600  28.74000 1.000 26.95964  ? 680 HOH B O     1 
HETATM 2374 O  O     . HOH H 5 .   ? 8.93900  0.00000   0.00000  0.500 43.01333  ? 681 HOH B O     1 
HETATM 2375 O  O     . HOH H 5 .   ? 32.14900 12.88800  44.21900 1.000 41.12396  ? 682 HOH B O     1 
HETATM 2376 O  O     . HOH H 5 .   ? -4.46300 2.43200   34.57500 1.000 46.15416  ? 683 HOH B O     1 
HETATM 2377 O  O     . HOH H 5 .   ? 22.50900 11.00600  27.38200 1.000 26.78563  ? 684 HOH B O     1 
HETATM 2378 O  O     . HOH H 5 .   ? 28.13400 -5.24000  26.91600 1.000 27.28741  ? 685 HOH B O     1 
HETATM 2379 O  O     . HOH H 5 .   ? 11.31300 -9.89600  22.05200 1.000 34.56537  ? 686 HOH B O     1 
HETATM 2380 O  O     . HOH H 5 .   ? 20.81800 14.12600  39.14100 1.000 43.96065  ? 687 HOH B O     1 
HETATM 2381 O  O     . HOH H 5 .   ? 16.00100 19.14100  5.68900  1.000 40.78640  ? 688 HOH B O     1 
HETATM 2382 O  O     . HOH H 5 .   ? 21.34600 9.31400   25.50800 1.000 29.63077  ? 689 HOH B O     1 
HETATM 2383 O  O     . HOH H 5 .   ? 1.38600  -15.07300 11.16600 1.000 35.94375  ? 690 HOH B O     1 
HETATM 2384 O  O     . HOH H 5 .   ? 11.54900 -1.72900  6.25100  1.000 36.27628  ? 691 HOH B O     1 
HETATM 2385 O  O     . HOH H 5 .   ? 29.90100 2.40700   30.66000 1.000 33.53348  ? 692 HOH B O     1 
HETATM 2386 O  O     . HOH H 5 .   ? 0.74300  17.40000  32.66300 1.000 34.76697  ? 693 HOH B O     1 
HETATM 2387 O  O     . HOH H 5 .   ? -1.28400 12.52200  35.86900 1.000 46.16846  ? 694 HOH B O     1 
HETATM 2388 O  O     . HOH H 5 .   ? 15.68700 -6.09900  13.23100 1.000 38.13963  ? 695 HOH B O     1 
HETATM 2389 O  O     . HOH H 5 .   ? 24.45600 18.18300  16.68500 1.000 36.10623  ? 696 HOH B O     1 
HETATM 2390 O  O     . HOH H 5 .   ? 19.83800 20.86500  47.66500 1.000 44.28545  ? 697 HOH B O     1 
HETATM 2391 O  O     . HOH H 5 .   ? 17.43200 -1.39900  40.08300 1.000 28.72142  ? 698 HOH B O     1 
HETATM 2392 O  O     . HOH H 5 .   ? 17.92400 13.87600  31.23700 1.000 18.59335  ? 699 HOH B O     1 
HETATM 2393 O  O     . HOH H 5 .   ? 15.21800 5.51100   45.89400 1.000 45.97062  ? 700 HOH B O     1 
HETATM 2394 O  O     . HOH H 5 .   ? 16.84900 -14.35900 40.51200 1.000 23.57738  ? 701 HOH B O     1 
HETATM 2395 O  O     . HOH H 5 .   ? 12.92200 19.51500  13.40100 1.000 32.20831  ? 702 HOH B O     1 
HETATM 2396 O  O     . HOH H 5 .   ? 12.06000 -10.81800 12.94500 1.000 43.05733  ? 703 HOH B O     1 
HETATM 2397 O  O     . HOH H 5 .   ? 14.10400 12.85700  -1.96400 1.000 48.07040  ? 704 HOH B O     1 
HETATM 2398 O  O     . HOH H 5 .   ? 9.86700  8.82900   4.74000  1.000 50.98901  ? 705 HOH B O     1 
HETATM 2399 O  O     . HOH H 5 .   ? 27.53600 4.08200   1.91400  1.000 38.99006  ? 706 HOH B O     1 
HETATM 2400 O  O     . HOH H 5 .   ? 19.32600 -4.04600  7.87100  1.000 35.17469  ? 707 HOH B O     1 
HETATM 2401 O  O     . HOH H 5 .   ? 1.10300  -6.88400  8.70500  1.000 46.05938  ? 708 HOH B O     1 
HETATM 2402 O  O     . HOH H 5 .   ? 16.41300 26.21000  49.75200 1.000 37.37201  ? 709 HOH B O     1 
HETATM 2403 O  O     . HOH H 5 .   ? 23.08700 15.25000  36.07100 1.000 39.49779  ? 710 HOH B O     1 
HETATM 2404 O  O     . HOH H 5 .   ? 16.40800 6.38100   49.23500 1.000 48.77864  ? 711 HOH B O     1 
HETATM 2405 O  O     . HOH H 5 .   ? 4.47900  -12.86600 8.53200  1.000 42.67418  ? 712 HOH B O     1 
HETATM 2406 O  O     . HOH H 5 .   ? 12.25400 -9.49400  10.53400 1.000 38.08216  ? 713 HOH B O     1 
HETATM 2407 O  O     . HOH H 5 .   ? 22.43800 0.00000   55.23300 0.500 41.46817  ? 714 HOH B O     1 
HETATM 2408 O  O     . HOH H 5 .   ? 20.60400 10.84900  29.33900 1.000 39.11481  ? 715 HOH B O     1 
HETATM 2409 O  O     . HOH H 5 .   ? 35.87300 9.65700   32.72600 1.000 52.42025  ? 716 HOH B O     1 
HETATM 2410 O  O     . HOH H 5 .   ? 9.56400  22.61800  5.65000  1.000 52.86861  ? 717 HOH B O     1 
HETATM 2411 O  O     . HOH H 5 .   ? 30.85600 -2.65700  28.95900 1.000 45.68697  ? 718 HOH B O     1 
HETATM 2412 O  O     . HOH H 5 .   ? 29.83500 22.75300  -1.60300 1.000 45.26163  ? 719 HOH B O     1 
HETATM 2413 O  O     . HOH H 5 .   ? 8.18500  14.63000  46.95800 1.000 50.75879  ? 720 HOH B O     1 
HETATM 2414 O  O     . HOH H 5 .   ? -0.46000 10.41000  29.56900 1.000 37.14589  ? 721 HOH B O     1 
HETATM 2415 O  O     . HOH H 5 .   ? 4.33300  -11.72300 22.06100 1.000 43.23072  ? 722 HOH B O     1 
HETATM 2416 O  O     . HOH H 5 .   ? 18.44900 -12.38000 13.74400 1.000 43.51047  ? 723 HOH B O     1 
HETATM 2417 O  O     . HOH H 5 .   ? 12.68600 12.00200  -0.37400 1.000 41.98527  ? 724 HOH B O     1 
HETATM 2418 O  O     . HOH H 5 .   ? 10.86600 11.49800  48.79200 1.000 46.95513  ? 725 HOH B O     1 
HETATM 2419 O  O     . HOH H 5 .   ? -3.11700 19.96700  8.54600  1.000 36.97110  ? 726 HOH B O     1 
HETATM 2420 O  O     . HOH H 5 .   ? 3.26800  -18.59500 12.55800 1.000 37.99127  ? 727 HOH B O     1 
HETATM 2421 O  O     . HOH H 5 .   ? 30.64600 -0.39800  28.82700 1.000 37.36261  ? 728 HOH B O     1 
HETATM 2422 O  O     . HOH H 5 .   ? 22.07500 20.45000  25.45900 1.000 28.66833  ? 729 HOH B O     1 
HETATM 2423 O  O     . HOH H 5 .   ? 17.86500 5.81000   -6.41700 1.000 33.53180  ? 730 HOH B O     1 
HETATM 2424 O  O     . HOH H 5 .   ? 35.00500 -6.68600  31.51900 1.000 41.29478  ? 731 HOH B O     1 
HETATM 2425 O  O     . HOH H 5 .   ? 6.63600  -4.94700  50.42400 1.000 37.01428  ? 732 HOH B O     1 
HETATM 2426 O  O     . HOH H 5 .   ? 0.43800  21.70500  5.76200  1.000 31.56023  ? 733 HOH B O     1 
HETATM 2427 O  O     . HOH H 5 .   ? 5.99200  -0.67300  42.49400 1.000 39.89813  ? 734 HOH B O     1 
HETATM 2428 O  O     . HOH H 5 .   ? -0.38700 -17.64800 12.19100 1.000 43.54117  ? 735 HOH B O     1 
HETATM 2429 O  O     . HOH H 5 .   ? 26.62500 16.14100  34.30000 1.000 32.59950  ? 736 HOH B O     1 
HETATM 2430 O  O     . HOH H 5 .   ? -4.46000 -8.65600  7.62500  1.000 27.28752  ? 737 HOH B O     1 
HETATM 2431 O  O     . HOH H 5 .   ? 2.57600  -9.18900  6.43300  1.000 47.84058  ? 738 HOH B O     1 
HETATM 2432 O  O     . HOH H 5 .   ? 31.72400 16.06000  42.65400 1.000 35.28142  ? 739 HOH B O     1 
HETATM 2433 O  O     . HOH H 5 .   ? 36.34900 11.11500  51.95900 1.000 42.04239  ? 740 HOH B O     1 
HETATM 2434 O  O     . HOH I 5 .   ? 8.03900  1.02800   24.56100 1.000 29.12469  ? 101 HOH F O     1 
HETATM 2435 O  O     . HOH I 5 .   ? -4.96100 -1.35600  30.48300 1.000 37.02668  ? 102 HOH F 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   . ASP A 6   ? 1.25769 1.38407 1.21168 0.24236  0.00582  -0.00795 195 ASP B N   
2    C CA  . ASP A 6   ? 1.40181 1.44459 1.32180 0.23347  0.01805  -0.02866 195 ASP B CA  
3    C C   . ASP A 6   ? 1.34538 1.31712 1.24460 0.26757  0.02054  -0.03391 195 ASP B C   
4    O O   . ASP A 6   ? 1.33652 1.28016 1.22333 0.27059  0.00572  -0.02284 195 ASP B O   
5    C CB  . ASP A 6   ? 1.28760 1.28929 1.17856 0.19087  0.00914  -0.03119 195 ASP B CB  
6    C CG  . ASP A 6   ? 1.26430 1.21728 1.13699 0.17522  0.02214  -0.04722 195 ASP B CG  
7    O OD1 . ASP A 6   ? 1.20733 1.15920 1.08648 0.18955  0.03632  -0.05540 195 ASP B OD1 
8    O OD2 . ASP A 6   ? 1.18103 1.09714 1.03106 0.14981  0.01804  -0.05142 195 ASP B OD2 
9    N N   . SER A 7   ? 1.53693 1.47710 1.42628 0.28861  0.03665  -0.04940 196 SER B N   
10   C CA  . SER A 7   ? 1.58443 1.44247 1.44220 0.31473  0.03460  -0.05404 196 SER B CA  
11   C C   . SER A 7   ? 1.57687 1.36442 1.39840 0.28185  0.02901  -0.05342 196 SER B C   
12   O O   . SER A 7   ? 1.61613 1.34197 1.40959 0.28958  0.01758  -0.04674 196 SER B O   
13   C CB  . SER A 7   ? 1.62639 1.46510 1.47349 0.34743  0.05205  -0.07259 196 SER B CB  
14   O OG  . SER A 7   ? 1.66984 1.40804 1.46984 0.34491  0.04665  -0.07788 196 SER B OG  
15   N N   . TYR A 8   ? 1.27994 1.07742 1.10140 0.24600  0.03545  -0.05768 197 TYR B N   
16   C CA  . TYR A 8   ? 1.14732 0.89960 0.94338 0.21920  0.03212  -0.05393 197 TYR B CA  
17   C C   . TYR A 8   ? 1.03329 0.80866 0.83123 0.20494  0.02110  -0.04446 197 TYR B C   
18   O O   . TYR A 8   ? 1.00881 0.80756 0.81155 0.18337  0.02284  -0.04848 197 TYR B O   
19   C CB  . TYR A 8   ? 1.09007 0.83940 0.88570 0.19455  0.04386  -0.06218 197 TYR B CB  
20   C CG  . TYR A 8   ? 1.24904 0.97783 1.03646 0.19917  0.05442  -0.07138 197 TYR B CG  
21   C CD1 . TYR A 8   ? 1.24364 0.91243 0.99949 0.19220  0.05365  -0.06879 197 TYR B CD1 
22   C CD2 . TYR A 8   ? 1.36770 1.14158 1.17470 0.20362  0.06422  -0.08067 197 TYR B CD2 
23   C CE1 . TYR A 8   ? 1.10376 0.74749 0.84214 0.19059  0.06167  -0.07794 197 TYR B CE1 
24   C CE2 . TYR A 8   ? 1.11586 0.87244 0.90818 0.20505  0.07544  -0.09108 197 TYR B CE2 
25   C CZ  . TYR A 8   ? 1.13095 0.81747 0.88633 0.19846  0.07392  -0.09108 197 TYR B CZ  
26   O OH  . TYR A 8   ? 1.26131 0.92530 0.99286 0.19510  0.08349  -0.10218 197 TYR B OH  
27   N N   . THR A 9   ? 1.02160 0.78412 0.80960 0.21628  0.00721  -0.03165 198 THR B N   
28   C CA  . THR A 9   ? 1.01666 0.79322 0.79455 0.19903  -0.00396 -0.02188 198 THR B CA  
29   C C   . THR A 9   ? 0.85368 0.58866 0.59935 0.18943  -0.01027 -0.01098 198 THR B C   
30   O O   . THR A 9   ? 0.81190 0.55886 0.54183 0.17316  -0.01694 -0.00394 198 THR B O   
31   C CB  . THR A 9   ? 1.06624 0.88521 0.86339 0.21176  -0.01979 -0.00864 198 THR B CB  
32   O OG1 . THR A 9   ? 1.11930 0.91921 0.92333 0.24615  -0.02703 -0.00036 198 THR B OG1 
33   C CG2 . THR A 9   ? 0.98479 0.86489 0.81163 0.20685  -0.01653 -0.01300 198 THR B CG2 
34   N N   . HIS A 10  ? 0.89296 0.58181 0.62402 0.19502  -0.00917 -0.00858 199 HIS B N   
35   C CA  . HIS A 10  ? 0.84180 0.49582 0.54086 0.17897  -0.01807 0.00745  199 HIS B CA  
36   C C   . HIS A 10  ? 0.80987 0.46487 0.50297 0.15871  -0.00228 0.00322  199 HIS B C   
37   O O   . HIS A 10  ? 0.73202 0.37423 0.40273 0.14048  -0.00594 0.01881  199 HIS B O   
38   C CB  . HIS A 10  ? 0.89153 0.48431 0.56958 0.19305  -0.03329 0.01709  199 HIS B CB  
39   C CG  . HIS A 10  ? 0.92648 0.48969 0.60468 0.20552  -0.02188 0.00112  199 HIS B CG  
40   N ND1 . HIS A 10  ? 0.95953 0.53805 0.66102 0.23650  -0.01380 -0.01517 199 HIS B ND1 
41   C CD2 . HIS A 10  ? 0.90348 0.42920 0.55918 0.18827  -0.01726 0.00063  199 HIS B CD2 
42   C CE1 . HIS A 10  ? 0.98018 0.52739 0.66903 0.23858  -0.00314 -0.02833 199 HIS B CE1 
43   N NE2 . HIS A 10  ? 0.94040 0.45155 0.60045 0.20785  -0.00664 -0.01851 199 HIS B NE2 
44   N N   . LEU A 11  ? 0.78834 0.46299 0.50309 0.16059  0.01350  -0.01409 200 LEU B N   
45   C CA  . LEU A 11  ? 0.79133 0.47251 0.50650 0.14509  0.02739  -0.01605 200 LEU B CA  
46   C C   . LEU A 11  ? 0.77160 0.48551 0.49076 0.14145  0.03524  -0.02589 200 LEU B C   
47   O O   . LEU A 11  ? 0.74899 0.47761 0.47344 0.14579  0.03019  -0.03422 200 LEU B O   
48   C CB  . LEU A 11  ? 0.75861 0.43008 0.48817 0.14614  0.03624  -0.02600 200 LEU B CB  
49   C CG  . LEU A 11  ? 0.87104 0.49704 0.58096 0.14574  0.02959  -0.01892 200 LEU B CG  
50   C CD1 . LEU A 11  ? 0.83059 0.45175 0.54799 0.13716  0.03985  -0.02643 200 LEU B CD1 
51   C CD2 . LEU A 11  ? 0.90548 0.51135 0.58788 0.12718  0.01940  0.00409  200 LEU B CD2 
52   N N   . SER A 12  ? 0.76226 0.48715 0.47534 0.13395  0.04664  -0.02405 201 SER B N   
53   C CA  . SER A 12  ? 0.69328 0.43531 0.39804 0.13566  0.05539  -0.03760 201 SER B CA  
54   C C   . SER A 12  ? 0.69121 0.42667 0.41117 0.13937  0.06339  -0.05381 201 SER B C   
55   O O   . SER A 12  ? 0.67104 0.39982 0.41087 0.13778  0.06593  -0.05046 201 SER B O   
56   C CB  . SER A 12  ? 0.65967 0.42347 0.34943 0.13325  0.06701  -0.02826 201 SER B CB  
57   O OG  . SER A 12  ? 0.64887 0.42104 0.35652 0.13711  0.08061  -0.02618 201 SER B OG  
58   N N   . PHE A 13  ? 0.65135 0.38233 0.35560 0.14105  0.06457  -0.07044 202 PHE B N   
59   C CA  . PHE A 13  ? 0.65346 0.36621 0.36359 0.14280  0.06763  -0.08427 202 PHE B CA  
60   C C   . PHE A 13  ? 0.67123 0.38879 0.39815 0.15166  0.08156  -0.07696 202 PHE B C   
61   O O   . PHE A 13  ? 0.64278 0.35146 0.39153 0.14825  0.08015  -0.07511 202 PHE B O   
62   C CB  . PHE A 13  ? 0.70023 0.39191 0.37338 0.14429  0.06633  -0.10377 202 PHE B CB  
63   C CG  . PHE A 13  ? 0.72393 0.37952 0.39154 0.14898  0.06692  -0.11859 202 PHE B CG  
64   C CD1 . PHE A 13  ? 0.76452 0.41260 0.43137 0.17127  0.08362  -0.12347 202 PHE B CD1 
65   C CD2 . PHE A 13  ? 0.73666 0.36790 0.39871 0.13092  0.04853  -0.12478 202 PHE B CD2 
66   C CE1 . PHE A 13  ? 0.82933 0.44194 0.49625 0.17649  0.07933  -0.13352 202 PHE B CE1 
67   C CE2 . PHE A 13  ? 0.82612 0.41231 0.47658 0.13146  0.04309  -0.13578 202 PHE B CE2 
68   C CZ  . PHE A 13  ? 0.82297 0.39462 0.47578 0.15651  0.05805  -0.14097 202 PHE B CZ  
69   N N   . TYR A 14  ? 0.65032 0.39078 0.37041 0.15978  0.09377  -0.06806 203 TYR B N   
70   C CA  . TYR A 14  ? 0.66701 0.42487 0.40989 0.16750  0.10570  -0.05591 203 TYR B CA  
71   C C   . TYR A 14  ? 0.68895 0.44959 0.45662 0.15061  0.09834  -0.03533 203 TYR B C   
72   O O   . TYR A 14  ? 0.71797 0.47480 0.50772 0.14916  0.09908  -0.03081 203 TYR B O   
73   C CB  . TYR A 14  ? 0.68897 0.48946 0.42278 0.17832  0.12167  -0.04575 203 TYR B CB  
74   C CG  . TYR A 14  ? 0.92190 0.75698 0.68397 0.19150  0.13590  -0.03051 203 TYR B CG  
75   C CD1 . TYR A 14  ? 0.97705 0.83280 0.76639 0.17289  0.13012  -0.00131 203 TYR B CD1 
76   C CD2 . TYR A 14  ? 0.96606 0.81320 0.72478 0.22381  0.15438  -0.04424 203 TYR B CD2 
77   C CE1 . TYR A 14  ? 0.96186 0.86013 0.78160 0.18172  0.14049  0.01904  203 TYR B CE1 
78   C CE2 . TYR A 14  ? 0.98585 0.87575 0.77822 0.24162  0.16765  -0.02637 203 TYR B CE2 
79   C CZ  . TYR A 14  ? 0.98300 0.90424 0.80935 0.21830  0.15981  0.00798  203 TYR B CZ  
80   O OH  . TYR A 14  ? 0.97089 0.94490 0.83503 0.23276  0.17040  0.03185  203 TYR B OH  
81   N N   . GLU A 15  ? 0.63346 0.39367 0.39184 0.13726  0.08923  -0.02309 204 GLU B N   
82   C CA  . GLU A 15  ? 0.75327 0.50325 0.52019 0.12113  0.08180  -0.00631 204 GLU B CA  
83   C C   . GLU A 15  ? 0.63555 0.36069 0.41394 0.11782  0.07645  -0.01888 204 GLU B C   
84   O O   . GLU A 15  ? 0.62986 0.34998 0.41812 0.10588  0.07543  -0.00958 204 GLU B O   
85   C CB  . GLU A 15  ? 0.74804 0.48734 0.49128 0.10968  0.06992  0.00882  204 GLU B CB  
86   C CG  . GLU A 15  ? 0.88119 0.59829 0.61652 0.08916  0.05999  0.02851  204 GLU B CG  
87   C CD  . GLU A 15  ? 0.99518 0.74504 0.74509 0.07437  0.06567  0.05190  204 GLU B CD  
88   O OE1 . GLU A 15  ? 0.95421 0.74992 0.72364 0.08656  0.07986  0.05399  204 GLU B OE1 
89   O OE2 . GLU A 15  ? 0.87752 0.60758 0.61714 0.05110  0.05536  0.06928  204 GLU B OE2 
90   N N   . LYS A 16  ? 0.58666 0.30419 0.36284 0.12493  0.07261  -0.03731 205 LYS B N   
91   C CA  . LYS A 16  ? 0.66368 0.37413 0.45193 0.11963  0.06843  -0.04675 205 LYS B CA  
92   C C   . LYS A 16  ? 0.60266 0.31249 0.40717 0.11330  0.07080  -0.04767 205 LYS B C   
93   O O   . LYS A 16  ? 0.54612 0.25404 0.36112 0.10048  0.06870  -0.04372 205 LYS B O   
94   C CB  . LYS A 16  ? 0.63368 0.35127 0.41861 0.12500  0.06154  -0.05950 205 LYS B CB  
95   C CG  . LYS A 16  ? 0.70200 0.41939 0.47753 0.13422  0.05602  -0.05536 205 LYS B CG  
96   C CD  . LYS A 16  ? 0.71510 0.44965 0.48723 0.13908  0.04795  -0.06057 205 LYS B CD  
97   C CE  . LYS A 16  ? 0.75067 0.51032 0.54067 0.13605  0.04337  -0.06689 205 LYS B CE  
98   N NZ  . LYS A 16  ? 0.80390 0.59089 0.59598 0.14152  0.03233  -0.06362 205 LYS B NZ  
99   N N   . ARG A 17  ? 0.59221 0.30021 0.39475 0.12357  0.07469  -0.05248 206 ARG B N   
100  C CA  . ARG A 17  ? 0.64439 0.34202 0.46032 0.12367  0.07413  -0.05206 206 ARG B CA  
101  C C   . ARG A 17  ? 0.61251 0.32693 0.44813 0.12061  0.07983  -0.03026 206 ARG B C   
102  O O   . ARG A 17  ? 0.64101 0.35186 0.49380 0.10924  0.07459  -0.02126 206 ARG B O   
103  C CB  . ARG A 17  ? 0.62504 0.30506 0.42430 0.14335  0.07741  -0.06676 206 ARG B CB  
104  C CG  . ARG A 17  ? 0.72294 0.38506 0.53402 0.15541  0.07798  -0.06485 206 ARG B CG  
105  C CD  . ARG A 17  ? 0.72069 0.34878 0.50118 0.18002  0.08105  -0.08655 206 ARG B CD  
106  N NE  . ARG A 17  ? 0.92158 0.50521 0.67245 0.16338  0.06223  -0.10367 206 ARG B NE  
107  C CZ  . ARG A 17  ? 1.00921 0.55689 0.73273 0.16819  0.05384  -0.12019 206 ARG B CZ  
108  N NH1 . ARG A 17  ? 0.90170 0.45212 0.62462 0.19602  0.06635  -0.12628 206 ARG B NH1 
109  N NH2 . ARG A 17  ? 0.92017 0.42640 0.61129 0.14497  0.03261  -0.13046 206 ARG B NH2 
110  N N   . GLU A 18  ? 0.58115 0.31803 0.41312 0.12520  0.08764  -0.01742 207 GLU B N   
111  C CA  . GLU A 18  ? 0.63405 0.39463 0.48333 0.11445  0.08932  0.00968  207 GLU B CA  
112  C C   . GLU A 18  ? 0.59464 0.33981 0.43952 0.08602  0.07908  0.01899  207 GLU B C   
113  O O   . GLU A 18  ? 0.54809 0.30076 0.40772 0.06980  0.07511  0.03707  207 GLU B O   
114  C CB  . GLU A 18  ? 0.73011 0.52549 0.57224 0.11847  0.09700  0.02619  207 GLU B CB  
115  C CG  . GLU A 18  ? 0.76047 0.59411 0.62041 0.10250  0.09658  0.06152  207 GLU B CG  
116  C CD  . GLU A 18  ? 0.90659 0.77082 0.80303 0.12053  0.10440  0.07158  207 GLU B CD  
117  O OE1 . GLU A 18  ? 0.85760 0.70625 0.75790 0.15035  0.11163  0.04837  207 GLU B OE1 
118  O OE2 . GLU A 18  ? 0.96880 0.86930 0.88732 0.10434  0.10088  0.10458  207 GLU B OE2 
119  N N   . LEU A 19  ? 0.55535 0.27866 0.37723 0.08193  0.07482  0.00654  208 LEU B N   
120  C CA  . LEU A 19  ? 0.57222 0.27329 0.37978 0.06181  0.06805  0.00837  208 LEU B CA  
121  C C   . LEU A 19  ? 0.62931 0.32986 0.45097 0.05189  0.06615  0.00057  208 LEU B C   
122  O O   . LEU A 19  ? 0.56967 0.26440 0.38712 0.02909  0.06208  0.01115  208 LEU B O   
123  C CB  . LEU A 19  ? 0.57520 0.25239 0.35631 0.07072  0.06533  -0.00592 208 LEU B CB  
124  C CG  . LEU A 19  ? 0.69008 0.35194 0.44523 0.06798  0.05931  0.00844  208 LEU B CG  
125  C CD1 . LEU A 19  ? 0.74840 0.37989 0.48009 0.08302  0.05375  -0.00577 208 LEU B CD1 
126  C CD2 . LEU A 19  ? 0.76099 0.40650 0.49805 0.03914  0.05137  0.03179  208 LEU B CD2 
127  N N   . PHE A 20  ? 0.59794 0.30350 0.43089 0.06305  0.06624  -0.01563 209 PHE B N   
128  C CA  . PHE A 20  ? 0.58408 0.29214 0.42901 0.04727  0.06016  -0.01777 209 PHE B CA  
129  C C   . PHE A 20  ? 0.58957 0.29971 0.45528 0.03853  0.05551  0.00153  209 PHE B C   
130  O O   . PHE A 20  ? 0.57153 0.28334 0.44369 0.01467  0.04795  0.01114  209 PHE B O   
131  C CB  . PHE A 20  ? 0.53163 0.24147 0.37781 0.05419  0.05554  -0.03446 209 PHE B CB  
132  C CG  . PHE A 20  ? 0.56692 0.28687 0.41874 0.03070  0.04648  -0.03499 209 PHE B CG  
133  C CD1 . PHE A 20  ? 0.54091 0.24849 0.40345 0.01652  0.03420  -0.02570 209 PHE B CD1 
134  C CD2 . PHE A 20  ? 0.52737 0.27220 0.37314 0.02377  0.04961  -0.04300 209 PHE B CD2 
135  C CE1 . PHE A 20  ? 0.55877 0.27850 0.42348 -0.01244 0.02217  -0.02160 209 PHE B CE1 
136  C CE2 . PHE A 20  ? 0.52829 0.29735 0.37911 -0.00145 0.04244  -0.04057 209 PHE B CE2 
137  C CZ  . PHE A 20  ? 0.53629 0.29281 0.39538 -0.02382 0.02718  -0.02843 209 PHE B CZ  
138  N N   . ARG A 21  ? 0.55175 0.26697 0.42872 0.05902  0.06018  0.00869  210 ARG B N   
139  C CA  . ARG A 21  ? 0.59212 0.31769 0.49528 0.05940  0.05699  0.03057  210 ARG B CA  
140  C C   . ARG A 21  ? 0.59026 0.33445 0.49827 0.03212  0.05365  0.05804  210 ARG B C   
141  O O   . ARG A 21  ? 0.61584 0.36517 0.54123 0.01340  0.04365  0.07694  210 ARG B O   
142  C CB  . ARG A 21  ? 0.59917 0.33826 0.51214 0.09429  0.06797  0.03139  210 ARG B CB  
143  C CG  . ARG A 21  ? 0.74703 0.47122 0.67850 0.11583  0.06378  0.03184  210 ARG B CG  
144  C CD  . ARG A 21  ? 0.78204 0.46235 0.68731 0.13386  0.06149  0.00046  210 ARG B CD  
145  N NE  . ARG A 21  ? 0.73484 0.42439 0.62324 0.16406  0.07829  -0.01428 210 ARG B NE  
146  C CZ  . ARG A 21  ? 0.83573 0.52815 0.72762 0.20210  0.09002  -0.01753 210 ARG B CZ  
147  N NH1 . ARG A 21  ? 0.86127 0.54366 0.77661 0.22015  0.08559  -0.00639 210 ARG B NH1 
148  N NH2 . ARG A 21  ? 0.71019 0.41758 0.58051 0.22466  0.10679  -0.03189 210 ARG B NH2 
149  N N   . LYS A 22  ? 0.58042 0.32957 0.46796 0.02532  0.05813  0.06287  211 LYS B N   
150  C CA  . LYS A 22  ? 0.60741 0.36123 0.48455 -0.00804 0.05060  0.08846  211 LYS B CA  
151  C C   . LYS A 22  ? 0.62549 0.35317 0.48108 -0.03607 0.04345  0.07937  211 LYS B C   
152  O O   . LYS A 22  ? 0.61495 0.34534 0.46625 -0.06859 0.03402  0.10141  211 LYS B O   
153  C CB  . LYS A 22  ? 0.64976 0.39854 0.49745 -0.01234 0.05175  0.09436  211 LYS B CB  
154  C CG  . LYS A 22  ? 0.70594 0.41718 0.50946 -0.04680 0.04126  0.09903  211 LYS B CG  
155  C CD  . LYS A 22  ? 0.80408 0.48893 0.56893 -0.04737 0.03771  0.09917  211 LYS B CD  
156  C CE  . LYS A 22  ? 0.84253 0.55962 0.60918 -0.06986 0.02912  0.13969  211 LYS B CE  
157  N NZ  . LYS A 22  ? 0.86101 0.56622 0.60053 -0.06484 0.02576  0.14181  211 LYS B NZ  
158  N N   . LYS A 23  ? 0.62348 0.33323 0.46443 -0.02551 0.04801  0.04904  212 LYS B N   
159  C CA  . LYS A 23  ? 0.63020 0.33109 0.45414 -0.04814 0.04520  0.03912  212 LYS B CA  
160  C C   . LYS A 23  ? 0.60801 0.32530 0.45908 -0.06769 0.03482  0.05448  212 LYS B C   
161  O O   . LYS A 23  ? 0.60870 0.32692 0.44750 -0.10114 0.02810  0.06481  212 LYS B O   
162  C CB  . LYS A 23  ? 0.57253 0.27147 0.38557 -0.02875 0.05312  0.00845  212 LYS B CB  
163  C CG  . LYS A 23  ? 0.57049 0.26914 0.35751 -0.04503 0.05666  -0.00490 212 LYS B CG  
164  C CD  . LYS A 23  ? 0.56235 0.28949 0.35997 -0.03169 0.06159  -0.02472 212 LYS B CD  
165  C CE  . LYS A 23  ? 0.55823 0.28194 0.35446 0.00395  0.06821  -0.04028 212 LYS B CE  
166  N NZ  . LYS A 23  ? 0.58320 0.30931 0.35528 0.02019  0.07913  -0.05967 212 LYS B NZ  
167  N N   . LEU A 24  ? 0.53961 0.26331 0.42167 -0.04804 0.03145  0.05607  213 LEU B N   
168  C CA  . LEU A 24  ? 0.57219 0.29940 0.47857 -0.06358 0.01652  0.07362  213 LEU B CA  
169  C C   . LEU A 24  ? 0.57809 0.32095 0.50268 -0.08059 0.00864  0.10937  213 LEU B C   
170  O O   . LEU A 24  ? 0.58836 0.33616 0.52047 -0.11184 -0.00611 0.12929  213 LEU B O   
171  C CB  . LEU A 24  ? 0.54800 0.26049 0.47276 -0.03349 0.01273  0.06523  213 LEU B CB  
172  C CG  . LEU A 24  ? 0.54870 0.24773 0.45601 -0.02781 0.01233  0.03740  213 LEU B CG  
173  C CD1 . LEU A 24  ? 0.57563 0.24302 0.48860 -0.00545 0.00280  0.03148  213 LEU B CD1 
174  C CD2 . LEU A 24  ? 0.54964 0.26155 0.44627 -0.06517 0.00319  0.03701  213 LEU B CD2 
175  N N   . ARG A 25  ? 0.55966 0.31794 0.49229 -0.06421 0.01636  0.12224  214 ARG B N   
176  C CA  . ARG A 25  ? 0.62770 0.41608 0.58291 -0.08165 0.00763  0.16291  214 ARG B CA  
177  C C   . ARG A 25  ? 0.67052 0.45347 0.59370 -0.13313 -0.00228 0.17733  214 ARG B C   
178  O O   . ARG A 25  ? 0.70511 0.51732 0.64732 -0.15462 -0.01472 0.20469  214 ARG B O   
179  C CB  . ARG A 25  ? 0.57356 0.39290 0.54114 -0.05779 0.01843  0.17603  214 ARG B CB  
180  C CG  . ARG A 25  ? 0.61868 0.43917 0.60285 -0.00598 0.03251  0.15432  214 ARG B CG  
181  C CD  . ARG A 25  ? 0.57463 0.44825 0.58514 0.01847  0.04298  0.17763  214 ARG B CD  
182  N NE  . ARG A 25  ? 0.62981 0.50646 0.61313 0.02786  0.05572  0.16290  214 ARG B NE  
183  C CZ  . ARG A 25  ? 0.62634 0.49361 0.60278 0.06515  0.06963  0.13422  214 ARG B CZ  
184  N NH1 . ARG A 25  ? 0.60465 0.44972 0.59252 0.09719  0.07263  0.11355  214 ARG B NH1 
185  N NH2 . ARG A 25  ? 0.67119 0.54526 0.62251 0.06677  0.07756  0.12741  214 ARG B NH2 
186  N N   . GLU A 26  ? 0.48056 0.53498 0.56635 -0.09232 0.11903  0.11297  215 GLU B N   
187  C CA  . GLU A 26  ? 0.53097 0.58391 0.63290 -0.10785 0.09714  0.11197  215 GLU B CA  
188  C C   . GLU A 26  ? 0.55838 0.62000 0.67157 -0.10087 0.08123  0.09865  215 GLU B C   
189  O O   . GLU A 26  ? 0.55798 0.62093 0.68579 -0.11225 0.06385  0.09787  215 GLU B O   
190  C CB  . GLU A 26  ? 0.58260 0.59331 0.64723 -0.11410 0.08489  0.10912  215 GLU B CB  
191  C CG  . GLU A 26  ? 0.74867 0.75212 0.81828 -0.13471 0.08760  0.12510  215 GLU B CG  
192  C CD  . GLU A 26  ? 0.84494 0.88255 0.95872 -0.14572 0.08684  0.12924  215 GLU B CD  
193  O OE1 . GLU A 26  ? 0.86969 0.91018 0.99898 -0.15238 0.06689  0.12359  215 GLU B OE1 
194  O OE2 . GLU A 26  ? 0.95568 1.01551 1.08458 -0.14575 0.10470  0.13605  215 GLU B OE2 
195  N N   . ILE A 27  ? 0.48714 0.55129 0.59085 -0.08312 0.08651  0.08847  216 ILE B N   
196  C CA  . ILE A 27  ? 0.48711 0.55661 0.59832 -0.07677 0.07341  0.07668  216 ILE B CA  
197  C C   . ILE A 27  ? 0.49223 0.59664 0.64512 -0.08090 0.07326  0.08371  216 ILE B C   
198  O O   . ILE A 27  ? 0.47648 0.60655 0.65096 -0.07672 0.08973  0.09280  216 ILE B O   
199  C CB  . ILE A 27  ? 0.50106 0.56172 0.59076 -0.05882 0.07921  0.06506  216 ILE B CB  
200  C CG1 . ILE A 27  ? 0.42923 0.45684 0.48049 -0.05492 0.07447  0.05753  216 ILE B CG1 
201  C CG2 . ILE A 27  ? 0.49068 0.55850 0.59037 -0.05341 0.06883  0.05511  216 ILE B CG2 
202  C CD1 . ILE A 27  ? 0.38983 0.40712 0.41697 -0.04038 0.08472  0.05174  216 ILE B CD1 
203  N N   . GLU A 28  ? 0.49005 0.59481 0.65321 -0.08781 0.05449  0.07969  217 GLU B N   
204  C CA  . GLU A 28  ? 0.50103 0.63610 0.70089 -0.09052 0.04964  0.08505  217 GLU B CA  
205  C C   . GLU A 28  ? 0.49964 0.64282 0.69950 -0.07310 0.05409  0.07707  217 GLU B C   
206  O O   . GLU A 28  ? 0.48282 0.60435 0.65601 -0.06474 0.04993  0.06455  217 GLU B O   
207  C CB  . GLU A 28  ? 0.57112 0.69720 0.77477 -0.10411 0.02605  0.08335  217 GLU B CB  
208  C CG  . GLU A 28  ? 0.66308 0.77802 0.86496 -0.12054 0.01906  0.08928  217 GLU B CG  
209  C CD  . GLU A 28  ? 0.85024 0.92698 1.01863 -0.12721 0.01061  0.08508  217 GLU B CD  
210  O OE1 . GLU A 28  ? 0.80006 0.85595 0.94623 -0.12055 -0.00135 0.07255  217 GLU B OE1 
211  O OE2 . GLU A 28  ? 0.93564 0.99911 1.09306 -0.13467 0.01681  0.09140  217 GLU B OE2 
212  N N   . GLY A 29  ? 0.41534 0.58717 0.64242 -0.06672 0.06182  0.08321  218 GLY B N   
213  C CA  . GLY A 29  ? 0.33866 0.51799 0.56796 -0.05036 0.06755  0.07846  218 GLY B CA  
214  C C   . GLY A 29  ? 0.38432 0.56988 0.60878 -0.03591 0.08899  0.08019  218 GLY B C   
215  O O   . GLY A 29  ? 0.37035 0.56186 0.59708 -0.03887 0.09946  0.08690  218 GLY B O   
216  N N   . PRO A 30  ? 0.32210 0.50323 0.53699 -0.01995 0.09600  0.07401  219 PRO B N   
217  C CA  . PRO A 30  ? 0.35885 0.53844 0.56148 -0.00455 0.11521  0.07400  219 PRO B CA  
218  C C   . PRO A 30  ? 0.32024 0.47886 0.49341 -0.00563 0.12648  0.07300  219 PRO B C   
219  O O   . PRO A 30  ? 0.32533 0.46173 0.47709 -0.01249 0.11803  0.06662  219 PRO B O   
220  C CB  . PRO A 30  ? 0.31696 0.48580 0.50794 0.01031  0.11631  0.06550  219 PRO B CB  
221  C CG  . PRO A 30  ? 0.31388 0.46729 0.49574 0.00116  0.09736  0.05711  219 PRO B CG  
222  C CD  . PRO A 30  ? 0.32515 0.49424 0.53094 -0.01518 0.08430  0.06442  219 PRO B CD  
223  N N   . GLU A 31  ? 0.28074 0.44198 0.44743 0.00203  0.14252  0.07755  220 GLU B N   
224  C CA  . GLU A 31  ? 0.43675 0.57803 0.57432 0.00064  0.15353  0.07902  220 GLU B CA  
225  C C   . GLU A 31  ? 0.38883 0.49740 0.48648 0.01021  0.15621  0.06813  220 GLU B C   
226  O O   . GLU A 31  ? 0.43395 0.53482 0.52276 0.02234  0.15593  0.05961  220 GLU B O   
227  C CB  . GLU A 31  ? 0.42287 0.57291 0.56028 0.00855  0.17124  0.08606  220 GLU B CB  
228  C CG  . GLU A 31  ? 0.50434 0.64610 0.62553 0.02955  0.18229  0.08044  220 GLU B CG  
229  C CD  . GLU A 31  ? 0.73081 0.87996 0.85084 0.03799  0.20101  0.08788  220 GLU B CD  
230  O OE1 . GLU A 31  ? 0.69603 0.85363 0.82299 0.02708  0.20693  0.09693  220 GLU B OE1 
231  O OE2 . GLU A 31  ? 0.81510 0.96000 0.92624 0.05548  0.21028  0.08497  220 GLU B OE2 
232  N N   . VAL A 32  ? 0.40094 0.48510 0.46995 0.00367  0.15272  0.06595  221 VAL B N   
233  C CA  . VAL A 32  ? 0.39425 0.44262 0.41958 0.01093  0.14692  0.05288  221 VAL B CA  
234  C C   . VAL A 32  ? 0.39132 0.42035 0.38333 0.01663  0.16295  0.05777  221 VAL B C   
235  O O   . VAL A 32  ? 0.42595 0.45749 0.42001 0.00709  0.16812  0.06832  221 VAL B O   
236  C CB  . VAL A 32  ? 0.35999 0.39374 0.37786 0.00026  0.12429  0.04431  221 VAL B CB  
237  C CG1 . VAL A 32  ? 0.37876 0.38123 0.35868 0.00775  0.11655  0.03114  221 VAL B CG1 
238  C CG2 . VAL A 32  ? 0.32511 0.37643 0.37287 -0.00555 0.11085  0.04110  221 VAL B CG2 
239  N N   . THR A 33  ? 0.43883 0.44495 0.39679 0.03177  0.17052  0.05036  222 THR B N   
240  C CA  . THR A 33  ? 0.38884 0.37096 0.30678 0.04028  0.18681  0.05407  222 THR B CA  
241  C C   . THR A 33  ? 0.44876 0.38947 0.31867 0.04329  0.17123  0.04090  222 THR B C   
242  O O   . THR A 33  ? 0.42823 0.36089 0.29709 0.04251  0.15217  0.02806  222 THR B O   
243  C CB  . THR A 33  ? 0.46750 0.45331 0.38329 0.05589  0.20159  0.05487  222 THR B CB  
244  O OG1 . THR A 33  ? 0.49391 0.48172 0.41806 0.06373  0.19533  0.04544  222 THR B OG1 
245  C CG2 . THR A 33  ? 0.51617 0.53910 0.47356 0.05137  0.21223  0.06868  222 THR B CG2 
246  N N   . LEU A 34  ? 0.52321 0.43803 0.35381 0.04636  0.17938  0.04504  223 LEU B N   
247  C CA  . LEU A 34  ? 0.54375 0.41780 0.32578 0.04991  0.16362  0.03416  223 LEU B CA  
248  C C   . LEU A 34  ? 0.61581 0.45763 0.34617 0.06593  0.18096  0.03420  223 LEU B C   
249  O O   . LEU A 34  ? 0.67582 0.52182 0.40560 0.06699  0.19713  0.04585  223 LEU B O   
250  C CB  . LEU A 34  ? 0.46761 0.33255 0.24266 0.03845  0.15194  0.03874  223 LEU B CB  
251  C CG  . LEU A 34  ? 0.54076 0.36563 0.26823 0.04251  0.13298  0.02889  223 LEU B CG  
252  C CD1 . LEU A 34  ? 0.54179 0.37059 0.28553 0.03912  0.10594  0.01430  223 LEU B CD1 
253  C CD2 . LEU A 34  ? 0.51970 0.32955 0.22953 0.03577  0.13136  0.03838  223 LEU B CD2 
254  N N   . VAL A 35  ? 0.64594 0.45858 0.34291 0.07574  0.16994  0.01984  224 VAL B N   
255  C CA  . VAL A 35  ? 0.77101 0.54904 0.42287 0.08858  0.17388  0.01690  224 VAL B CA  
256  C C   . VAL A 35  ? 0.70664 0.44307 0.31162 0.08989  0.14910  0.00296  224 VAL B C   
257  O O   . VAL A 35  ? 0.61393 0.35336 0.23022 0.08304  0.12821  -0.00752 224 VAL B O   
258  C CB  . VAL A 35  ? 0.73030 0.51289 0.39076 0.10035  0.18401  0.01436  224 VAL B CB  
259  C CG1 . VAL A 35  ? 0.63165 0.46215 0.34865 0.09803  0.20093  0.02578  224 VAL B CG1 
260  C CG2 . VAL A 35  ? 0.70016 0.46612 0.35074 0.10213  0.16534  -0.00149 224 VAL B CG2 
261  N N   . ASN A 36  ? 0.76501 0.46578 0.32447 0.09758  0.14828  0.00315  225 ASN B N   
262  C CA  . ASN A 36  ? 0.82438 0.48533 0.34092 0.09940  0.12167  -0.00940 225 ASN B CA  
263  C C   . ASN A 36  ? 0.77469 0.39945 0.24790 0.11232  0.12770  -0.00957 225 ASN B C   
264  O O   . ASN A 36  ? 0.80788 0.41358 0.25287 0.11633  0.13596  -0.00180 225 ASN B O   
265  C CB  . ASN A 36  ? 0.79384 0.44527 0.29651 0.09218  0.10645  -0.00758 225 ASN B CB  
266  C CG  . ASN A 36  ? 0.78393 0.40472 0.25717 0.09245  0.07306  -0.02126 225 ASN B CG  
267  O OD1 . ASN A 36  ? 0.80072 0.39952 0.25410 0.09807  0.06336  -0.03001 225 ASN B OD1 
268  N ND2 . ASN A 36  ? 0.82485 0.44506 0.29791 0.08608  0.05390  -0.02234 225 ASN B ND2 
269  N N   . GLU A 37  ? 0.83036 0.44303 0.29640 0.11872  0.12361  -0.01821 226 GLU B N   
270  C CA  . GLU A 37  ? 0.94177 0.51447 0.36212 0.13150  0.12630  -0.02004 226 GLU B CA  
271  C C   . GLU A 37  ? 0.90490 0.44066 0.29136 0.12993  0.09441  -0.03352 226 GLU B C   
272  O O   . GLU A 37  ? 0.92107 0.42435 0.27481 0.13864  0.09140  -0.03826 226 GLU B O   
273  C CB  . GLU A 37  ? 0.84600 0.42869 0.28002 0.14120  0.14620  -0.01796 226 GLU B CB  
274  C CG  . GLU A 37  ? 0.85640 0.48512 0.33718 0.14102  0.17383  -0.00480 226 GLU B CG  
275  C CD  . GLU A 37  ? 1.05549 0.70227 0.56196 0.14863  0.18623  -0.00460 226 GLU B CD  
276  O OE1 . GLU A 37  ? 1.00185 0.64903 0.51874 0.14505  0.17118  -0.01449 226 GLU B OE1 
277  O OE2 . GLU A 37  ? 1.05029 0.71105 0.56728 0.15816  0.21057  0.00569  226 GLU B OE2 
278  N N   . VAL A 38  ? 0.91603 0.45713 0.31163 0.11879  0.06954  -0.03929 227 VAL B N   
279  C CA  . VAL A 38  ? 0.88918 0.40891 0.27075 0.11373  0.03592  -0.05202 227 VAL B CA  
280  C C   . VAL A 38  ? 0.90032 0.39579 0.25210 0.11338  0.01579  -0.05201 227 VAL B C   
281  O O   . VAL A 38  ? 0.95198 0.41044 0.26622 0.11773  -0.00157 -0.05712 227 VAL B O   
282  C CB  . VAL A 38  ? 0.84798 0.40049 0.27666 0.10056  0.02023  -0.06054 227 VAL B CB  
283  C CG1 . VAL A 38  ? 0.82009 0.36018 0.24517 0.09248  -0.01593 -0.07137 227 VAL B CG1 
284  C CG2 . VAL A 38  ? 0.88082 0.44365 0.32820 0.10206  0.03299  -0.06316 227 VAL B CG2 
285  N N   . ASP A 39  ? 0.87408 0.38811 0.24111 0.10862  0.01703  -0.04592 228 ASP B N   
286  C CA  . ASP A 39  ? 0.92647 0.41767 0.26630 0.10961  -0.00106 -0.04449 228 ASP B CA  
287  C C   . ASP A 39  ? 0.90708 0.40358 0.24251 0.11142  0.02233  -0.03073 228 ASP B C   
288  O O   . ASP A 39  ? 0.88695 0.40367 0.23910 0.11227  0.05243  -0.02209 228 ASP B O   
289  C CB  . ASP A 39  ? 0.87551 0.38285 0.24252 0.09978  -0.03494 -0.05341 228 ASP B CB  
290  C CG  . ASP A 39  ? 0.93657 0.48831 0.35390 0.09023  -0.03045 -0.05285 228 ASP B CG  
291  O OD1 . ASP A 39  ? 0.93320 0.50182 0.36159 0.09052  -0.00243 -0.04375 228 ASP B OD1 
292  O OD2 . ASP A 39  ? 0.96029 0.53114 0.40844 0.08227  -0.05519 -0.06124 228 ASP B OD2 
293  N N   . ASP A 40  ? 0.95628 0.43576 0.27212 0.11147  0.00778  -0.02800 229 ASP B N   
294  C CA  . ASP A 40  ? 1.08580 0.56199 0.39051 0.11230  0.02751  -0.01454 229 ASP B CA  
295  C C   . ASP A 40  ? 0.92126 0.42904 0.26189 0.10206  0.02462  -0.00986 229 ASP B C   
296  O O   . ASP A 40  ? 0.99890 0.50270 0.33176 0.10030  0.03662  0.00167  229 ASP B O   
297  C CB  . ASP A 40  ? 1.06407 0.49445 0.31780 0.12009  0.01577  -0.01313 229 ASP B CB  
298  C CG  . ASP A 40  ? 1.17007 0.58975 0.42112 0.11888  -0.02411 -0.02305 229 ASP B CG  
299  O OD1 . ASP A 40  ? 1.14777 0.59629 0.43728 0.11183  -0.04223 -0.03159 229 ASP B OD1 
300  O OD2 . ASP A 40  ? 1.30491 0.68878 0.51780 0.12518  -0.03718 -0.02216 229 ASP B OD2 
301  N N   . GLU A 41  ? 0.84573 0.38270 0.22431 0.09499  0.00912  -0.01830 230 GLU B N   
302  C CA  . GLU A 41  ? 0.87510 0.43989 0.28571 0.08631  0.00668  -0.01415 230 GLU B CA  
303  C C   . GLU A 41  ? 0.86838 0.45695 0.29945 0.08136  0.04130  -0.00091 230 GLU B C   
304  O O   . GLU A 41  ? 0.84084 0.44846 0.29173 0.08159  0.05864  -0.00207 230 GLU B O   
305  C CB  . GLU A 41  ? 0.84283 0.43427 0.29120 0.08050  -0.01602 -0.02732 230 GLU B CB  
306  C CG  . GLU A 41  ? 0.83544 0.46246 0.33519 0.07133  -0.02122 -0.02294 230 GLU B CG  
307  C CD  . GLU A 41  ? 0.83372 0.49489 0.38642 0.06508  -0.04136 -0.03451 230 GLU B CD  
308  O OE1 . GLU A 41  ? 0.84487 0.50151 0.39404 0.06609  -0.05226 -0.04569 230 GLU B OE1 
309  O OE2 . GLU A 41  ? 0.78916 0.47956 0.38510 0.05898  -0.04566 -0.03215 230 GLU B OE2 
310  N N   . PRO A 42  ? 0.83200 0.42150 0.26328 0.07625  0.05144  0.01255  231 PRO B N   
311  C CA  . PRO A 42  ? 0.79329 0.40807 0.25048 0.06958  0.08452  0.02719  231 PRO B CA  
312  C C   . PRO A 42  ? 0.71970 0.38355 0.24306 0.05944  0.08696  0.02585  231 PRO B C   
313  O O   . PRO A 42  ? 0.72442 0.41262 0.27235 0.05822  0.11086  0.03151  231 PRO B O   
314  C CB  . PRO A 42  ? 0.87068 0.47194 0.31619 0.06378  0.08727  0.04047  231 PRO B CB  
315  C CG  . PRO A 42  ? 0.92173 0.50384 0.35139 0.06573  0.05343  0.03221  231 PRO B CG  
316  C CD  . PRO A 42  ? 0.87325 0.44134 0.28515 0.07586  0.03257  0.01562  231 PRO B CD  
317  N N   . CYS A 43  ? 0.71959 0.40059 0.27655 0.05306  0.06228  0.01834  232 CYS B N   
318  C CA  . CYS A 43  ? 0.62661 0.35245 0.24688 0.04293  0.06287  0.01733  232 CYS B CA  
319  C C   . CYS A 43  ? 0.59543 0.33079 0.23908 0.04051  0.03389  0.00626  232 CYS B C   
320  O O   . CYS A 43  ? 0.64581 0.35594 0.26056 0.04629  0.01365  0.00114  232 CYS B O   
321  C CB  . CYS A 43  ? 0.61577 0.35942 0.26043 0.03202  0.08090  0.03310  232 CYS B CB  
322  S SG  . CYS A 43  ? 0.65516 0.36977 0.27250 0.02758  0.07157  0.04243  232 CYS B SG  
323  N N   . PRO A 44  ? 0.57417 0.34556 0.26934 0.03316  0.03121  0.00263  233 PRO B N   
324  C CA  . PRO A 44  ? 0.60151 0.38407 0.32094 0.03115  0.00811  -0.00530 233 PRO B CA  
325  C C   . PRO A 44  ? 0.61617 0.38870 0.33056 0.02835  0.00321  0.00251  233 PRO B C   
326  O O   . PRO A 44  ? 0.52295 0.27750 0.21291 0.02630  0.01659  0.01435  233 PRO B O   
327  C CB  . PRO A 44  ? 0.52557 0.34553 0.29520 0.02408  0.01284  -0.00846 233 PRO B CB  
328  C CG  . PRO A 44  ? 0.53694 0.36036 0.30287 0.02590  0.03064  -0.00740 233 PRO B CG  
329  C CD  . PRO A 44  ? 0.53624 0.33704 0.26554 0.02932  0.04743  0.00351  233 PRO B CD  
330  N N   . SER A 45  ? 0.57107 0.35344 0.30719 0.02861  -0.01490 -0.00358 234 SER B N   
331  C CA  . SER A 45  ? 0.60502 0.37182 0.33155 0.02852  -0.02242 0.00221  234 SER B CA  
332  C C   . SER A 45  ? 0.58178 0.35222 0.31752 0.01695  -0.00450 0.01512  234 SER B C   
333  O O   . SER A 45  ? 0.55056 0.34934 0.32258 0.00872  0.00450  0.01580  234 SER B O   
334  C CB  . SER A 45  ? 0.58937 0.37216 0.34482 0.03204  -0.04104 -0.00687 234 SER B CB  
335  O OG  . SER A 45  ? 0.55877 0.32624 0.30700 0.03233  -0.04633 -0.00137 234 SER B OG  
336  N N   . LEU A 46  ? 0.61233 0.35263 0.31439 0.01563  -0.00043 0.02590  235 LEU B N   
337  C CA  . LEU A 46  ? 0.67280 0.41389 0.38331 0.00219  0.01445  0.03944  235 LEU B CA  
338  C C   . LEU A 46  ? 0.59146 0.33820 0.32578 -0.00347 0.00311  0.03803  235 LEU B C   
339  O O   . LEU A 46  ? 0.58980 0.34267 0.34001 -0.01703 0.01235  0.04728  235 LEU B O   
340  C CB  . LEU A 46  ? 0.77644 0.47977 0.44103 0.00130  0.02253  0.05230  235 LEU B CB  
341  C CG  . LEU A 46  ? 0.75174 0.44755 0.39025 0.00405  0.04269  0.05858  235 LEU B CG  
342  C CD1 . LEU A 46  ? 0.83208 0.48404 0.41765 0.00521  0.04819  0.07058  235 LEU B CD1 
343  C CD2 . LEU A 46  ? 0.66214 0.39178 0.33674 -0.00705 0.06654  0.06670  235 LEU B CD2 
344  N N   . ASP A 47  ? 0.56918 0.31366 0.30624 0.00684  -0.01672 0.02687  236 ASP B N   
345  C CA  . ASP A 47  ? 0.62577 0.37261 0.38113 0.00481  -0.02653 0.02421  236 ASP B CA  
346  C C   . ASP A 47  ? 0.52078 0.30459 0.31965 0.00005  -0.02345 0.01755  236 ASP B C   
347  O O   . ASP A 47  ? 0.53882 0.32386 0.35127 -0.00331 -0.02836 0.01630  236 ASP B O   
348  C CB  . ASP A 47  ? 0.61059 0.34038 0.35116 0.02057  -0.04729 0.01589  236 ASP B CB  
349  C CG  . ASP A 47  ? 0.69963 0.41706 0.44350 0.02113  -0.05593 0.01557  236 ASP B CG  
350  O OD1 . ASP A 47  ? 0.70081 0.38964 0.42306 0.01279  -0.05292 0.02586  236 ASP B OD1 
351  O OD2 . ASP A 47  ? 0.71578 0.45031 0.48246 0.02987  -0.06506 0.00528  236 ASP B OD2 
352  N N   . PHE A 48  ? 0.44377 0.25314 0.26023 0.00027  -0.01572 0.01331  237 PHE B N   
353  C CA  . PHE A 48  ? 0.45367 0.29497 0.30763 -0.00361 -0.01275 0.00758  237 PHE B CA  
354  C C   . PHE A 48  ? 0.38833 0.23828 0.25856 -0.01783 -0.00233 0.01676  237 PHE B C   
355  O O   . PHE A 48  ? 0.41800 0.26195 0.27974 -0.02602 0.00907  0.02804  237 PHE B O   
356  C CB  . PHE A 48  ? 0.39049 0.25090 0.25427 -0.00029 -0.00697 0.00198  237 PHE B CB  
357  C CG  . PHE A 48  ? 0.40968 0.29956 0.30800 -0.00506 -0.00154 -0.00174 237 PHE B CG  
358  C CD1 . PHE A 48  ? 0.38177 0.28483 0.29986 -0.00142 -0.01050 -0.01094 237 PHE B CD1 
359  C CD2 . PHE A 48  ? 0.37045 0.27467 0.28096 -0.01209 0.01324  0.00463  237 PHE B CD2 
360  C CE1 . PHE A 48  ? 0.34011 0.26597 0.28481 -0.00565 -0.00501 -0.01354 237 PHE B CE1 
361  C CE2 . PHE A 48  ? 0.38311 0.31122 0.32211 -0.01528 0.01670  0.00164  237 PHE B CE2 
362  C CZ  . PHE A 48  ? 0.35470 0.29153 0.30841 -0.01250 0.00746  -0.00739 237 PHE B CZ  
363  N N   . GLN A 49  ? 0.38334 0.24767 0.27725 -0.02085 -0.00646 0.01230  238 GLN B N   
364  C CA  . GLN A 49  ? 0.37033 0.24294 0.28118 -0.03444 -0.00152 0.01953  238 GLN B CA  
365  C C   . GLN A 49  ? 0.34424 0.24758 0.28475 -0.03569 0.00357  0.01532  238 GLN B C   
366  O O   . GLN A 49  ? 0.32558 0.23747 0.27486 -0.02835 -0.00193 0.00528  238 GLN B O   
367  C CB  . GLN A 49  ? 0.37289 0.22555 0.27654 -0.03706 -0.01329 0.01845  238 GLN B CB  
368  C CG  . GLN A 49  ? 0.38894 0.20579 0.26058 -0.03556 -0.01975 0.02299  238 GLN B CG  
369  C CD  . GLN A 49  ? 0.49133 0.28417 0.35271 -0.03634 -0.03180 0.02066  238 GLN B CD  
370  O OE1 . GLN A 49  ? 0.42699 0.20121 0.27145 -0.02277 -0.04170 0.01380  238 GLN B OE1 
371  N NE2 . GLN A 49  ? 0.46161 0.25387 0.33274 -0.05151 -0.03192 0.02623  238 GLN B NE2 
372  N N   . PHE A 50  ? 0.30448 0.22454 0.26098 -0.04460 0.01453  0.02378  239 PHE B N   
373  C CA  . PHE A 50  ? 0.29182 0.23823 0.27501 -0.04579 0.01833  0.02142  239 PHE B CA  
374  C C   . PHE A 50  ? 0.33165 0.27891 0.32677 -0.05400 0.00946  0.02174  239 PHE B C   
375  O O   . PHE A 50  ? 0.34950 0.28511 0.34148 -0.06472 0.00534  0.02922  239 PHE B O   
376  C CB  . PHE A 50  ? 0.29426 0.25935 0.29103 -0.04929 0.03321  0.03053  239 PHE B CB  
377  C CG  . PHE A 50  ? 0.40166 0.36461 0.38384 -0.03891 0.04253  0.02796  239 PHE B CG  
378  C CD1 . PHE A 50  ? 0.38018 0.35246 0.36718 -0.03026 0.04314  0.01880  239 PHE B CD1 
379  C CD2 . PHE A 50  ? 0.36308 0.31069 0.32294 -0.03826 0.05037  0.03491  239 PHE B CD2 
380  C CE1 . PHE A 50  ? 0.31011 0.27520 0.27952 -0.02136 0.04949  0.01562  239 PHE B CE1 
381  C CE2 . PHE A 50  ? 0.34436 0.28459 0.28423 -0.02789 0.05781  0.03184  239 PHE B CE2 
382  C CZ  . PHE A 50  ? 0.33555 0.28392 0.28001 -0.01953 0.05641  0.02170  239 PHE B CZ  
383  N N   . ILE A 51  ? 0.33406 0.29206 0.34009 -0.04951 0.00614  0.01374  240 ILE B N   
384  C CA  . ILE A 51  ? 0.33213 0.28662 0.34280 -0.05482 -0.00293 0.01230  240 ILE B CA  
385  C C   . ILE A 51  ? 0.25661 0.23373 0.28821 -0.05548 0.00050  0.01215  240 ILE B C   
386  O O   . ILE A 51  ? 0.28078 0.27321 0.32089 -0.04925 0.00920  0.01028  240 ILE B O   
387  C CB  . ILE A 51  ? 0.29101 0.22779 0.28549 -0.04594 -0.01113 0.00201  240 ILE B CB  
388  C CG1 . ILE A 51  ? 0.37291 0.32294 0.37302 -0.03434 -0.00621 -0.00677 240 ILE B CG1 
389  C CG2 . ILE A 51  ? 0.39617 0.30678 0.36823 -0.04429 -0.01695 0.00284  240 ILE B CG2 
390  C CD1 . ILE A 51  ? 0.35902 0.29852 0.34962 -0.02418 -0.01153 -0.01588 240 ILE B CD1 
391  N N   . SER A 52  ? 0.30583 0.28112 0.34244 -0.06293 -0.00795 0.01411  241 SER B N   
392  C CA  . SER A 52  ? 0.29957 0.29182 0.35216 -0.06305 -0.00789 0.01430  241 SER B CA  
393  C C   . SER A 52  ? 0.29823 0.27866 0.33825 -0.05745 -0.01393 0.00535  241 SER B C   
394  O O   . SER A 52  ? 0.37433 0.36446 0.42212 -0.05604 -0.01380 0.00494  241 SER B O   
395  C CB  . SER A 52  ? 0.26952 0.27177 0.33979 -0.07599 -0.01407 0.02468  241 SER B CB  
396  O OG  . SER A 52  ? 0.24600 0.22559 0.30277 -0.08512 -0.02838 0.02485  241 SER B OG  
397  N N   . GLN A 53  ? 0.31549 0.27423 0.33491 -0.05301 -0.01830 -0.00127 242 GLN B N   
398  C CA  . GLN A 53  ? 0.33918 0.28661 0.34500 -0.04553 -0.02030 -0.00958 242 GLN B CA  
399  C C   . GLN A 53  ? 0.34316 0.27951 0.33620 -0.03512 -0.01784 -0.01691 242 GLN B C   
400  O O   . GLN A 53  ? 0.32999 0.26191 0.32022 -0.03466 -0.01836 -0.01544 242 GLN B O   
401  C CB  . GLN A 53  ? 0.46358 0.39058 0.45455 -0.05184 -0.03298 -0.00885 242 GLN B CB  
402  C CG  . GLN A 53  ? 0.46571 0.36873 0.44192 -0.05901 -0.04335 -0.00638 242 GLN B CG  
403  C CD  . GLN A 53  ? 0.68249 0.56071 0.64055 -0.06624 -0.05845 -0.00661 242 GLN B CD  
404  O OE1 . GLN A 53  ? 0.83804 0.68672 0.76729 -0.05941 -0.06322 -0.01381 242 GLN B OE1 
405  N NE2 . GLN A 53  ? 0.65273 0.54223 0.62714 -0.07938 -0.06671 0.00125  242 GLN B NE2 
406  N N   . TYR A 54  ? 0.29213 0.22430 0.27747 -0.02602 -0.01481 -0.02422 243 TYR B N   
407  C CA  . TYR A 54  ? 0.36612 0.29415 0.34585 -0.01421 -0.01166 -0.03104 243 TYR B CA  
408  C C   . TYR A 54  ? 0.37783 0.27896 0.33676 -0.01214 -0.02069 -0.03154 243 TYR B C   
409  O O   . TYR A 54  ? 0.41168 0.29036 0.35360 -0.01843 -0.02938 -0.02943 243 TYR B O   
410  C CB  . TYR A 54  ? 0.29475 0.22357 0.27077 -0.00525 -0.00470 -0.03727 243 TYR B CB  
411  C CG  . TYR A 54  ? 0.32321 0.27729 0.31991 -0.00477 0.00587  -0.03802 243 TYR B CG  
412  C CD1 . TYR A 54  ? 0.32269 0.29530 0.33783 -0.00521 0.00864  -0.03790 243 TYR B CD1 
413  C CD2 . TYR A 54  ? 0.27564 0.23057 0.26937 -0.00424 0.01233  -0.03874 243 TYR B CD2 
414  C CE1 . TYR A 54  ? 0.29999 0.29093 0.33150 -0.00619 0.01673  -0.03886 243 TYR B CE1 
415  C CE2 . TYR A 54  ? 0.30568 0.27957 0.31617 -0.00515 0.02189  -0.03875 243 TYR B CE2 
416  C CZ  . TYR A 54  ? 0.32289 0.31455 0.35297 -0.00666 0.02364  -0.03899 243 TYR B CZ  
417  O OH  . TYR A 54  ? 0.35458 0.36056 0.39892 -0.00894 0.03163  -0.03925 243 TYR B OH  
418  N N   . ARG A 55  ? 0.41101 0.31224 0.37008 -0.00338 -0.02022 -0.03430 244 ARG B N   
419  C CA  . ARG A 55  ? 0.44566 0.31903 0.38306 0.00160  -0.02850 -0.03503 244 ARG B CA  
420  C C   . ARG A 55  ? 0.47712 0.34423 0.40685 0.01903  -0.02585 -0.04350 244 ARG B C   
421  O O   . ARG A 55  ? 0.53062 0.41163 0.47202 0.03024  -0.02318 -0.04701 244 ARG B O   
422  C CB  . ARG A 55  ? 0.42042 0.29586 0.36043 0.00089  -0.03073 -0.03118 244 ARG B CB  
423  C CG  . ARG A 55  ? 0.42757 0.26923 0.34177 0.00248  -0.04025 -0.02902 244 ARG B CG  
424  C CD  . ARG A 55  ? 0.57489 0.39146 0.47275 -0.01064 -0.04713 -0.02434 244 ARG B CD  
425  N NE  . ARG A 55  ? 0.53483 0.33090 0.41990 -0.02127 -0.05306 -0.01583 244 ARG B NE  
426  C CZ  . ARG A 55  ? 0.47946 0.24199 0.33840 -0.01558 -0.06060 -0.01593 244 ARG B CZ  
427  N NH1 . ARG A 55  ? 0.56497 0.31258 0.40940 0.00289  -0.06335 -0.02460 244 ARG B NH1 
428  N NH2 . ARG A 55  ? 0.46933 0.21257 0.31649 -0.02807 -0.06454 -0.00647 244 ARG B NH2 
429  N N   . LEU A 56  ? 0.47662 0.32270 0.38649 0.02190  -0.02682 -0.04663 245 LEU B N   
430  C CA  . LEU A 56  ? 0.52006 0.35941 0.42071 0.04031  -0.02107 -0.05428 245 LEU B CA  
431  C C   . LEU A 56  ? 0.51838 0.33666 0.40406 0.05325  -0.02772 -0.05667 245 LEU B C   
432  O O   . LEU A 56  ? 0.57925 0.37141 0.44671 0.04641  -0.03881 -0.05274 245 LEU B O   
433  C CB  . LEU A 56  ? 0.51877 0.33260 0.39255 0.04121  -0.02085 -0.05714 245 LEU B CB  
434  C CG  . LEU A 56  ? 0.54301 0.37117 0.42489 0.03057  -0.01600 -0.05476 245 LEU B CG  
435  C CD1 . LEU A 56  ? 0.52681 0.32593 0.37592 0.03663  -0.01509 -0.05913 245 LEU B CD1 
436  C CD2 . LEU A 56  ? 0.40348 0.27217 0.31897 0.03275  -0.00232 -0.05479 245 LEU B CD2 
437  N N   . THR A 57  ? 0.48586 0.31648 0.38084 0.07222  -0.02057 -0.06241 246 THR B N   
438  C CA  . THR A 57  ? 0.51832 0.33195 0.40157 0.08944  -0.02626 -0.06537 246 THR B CA  
439  C C   . THR A 57  ? 0.60657 0.40217 0.47070 0.10925  -0.01919 -0.07228 246 THR B C   
440  O O   . THR A 57  ? 0.64098 0.43271 0.49589 0.10786  -0.01069 -0.07436 246 THR B O   
441  C CB  . THR A 57  ? 0.53298 0.38157 0.44909 0.09686  -0.02574 -0.06555 246 THR B CB  
442  O OG1 . THR A 57  ? 0.49357 0.38101 0.44184 0.10190  -0.01244 -0.06865 246 THR B OG1 
443  C CG2 . THR A 57  ? 0.48253 0.34097 0.40836 0.07944  -0.03236 -0.05920 246 THR B CG2 
444  N N   . GLN A 58  ? 0.65947 0.44156 0.51464 0.12943  -0.02253 -0.07570 247 GLN B N   
445  C CA  . GLN A 58  ? 0.75367 0.51736 0.58922 0.15229  -0.01416 -0.08245 247 GLN B CA  
446  C C   . GLN A 58  ? 0.64209 0.45203 0.51428 0.16342  0.00473  -0.08510 247 GLN B C   
447  O O   . GLN A 58  ? 0.65521 0.50996 0.57045 0.16118  0.00701  -0.08305 247 GLN B O   
448  C CB  . GLN A 58  ? 0.66206 0.40636 0.48371 0.16830  -0.02272 -0.08238 247 GLN B CB  
449  C CG  . GLN A 58  ? 0.76790 0.47820 0.55302 0.17726  -0.02097 -0.08358 247 GLN B CG  
450  C CD  . GLN A 58  ? 0.86124 0.52592 0.60494 0.15868  -0.03266 -0.08079 247 GLN B CD  
451  O OE1 . GLN A 58  ? 0.86426 0.51352 0.60116 0.14229  -0.04601 -0.07630 247 GLN B OE1 
452  N NE2 . GLN A 58  ? 0.98730 0.63128 0.70418 0.16036  -0.02791 -0.08265 247 GLN B NE2 
453  N N   . GLY A 59  ? 0.58229 0.38371 0.43884 0.17087  0.01799  -0.08744 248 GLY B N   
454  C CA  . GLY A 59  ? 0.60025 0.44249 0.48893 0.17930  0.03857  -0.08833 248 GLY B CA  
455  C C   . GLY A 59  ? 0.57962 0.43987 0.47953 0.16439  0.04839  -0.08703 248 GLY B C   
456  O O   . GLY A 59  ? 0.58476 0.47466 0.50695 0.16909  0.06724  -0.08666 248 GLY B O   
457  N N   . VAL A 60  ? 0.51234 0.36047 0.40228 0.14117  0.03587  -0.08313 249 VAL B N   
458  C CA  . VAL A 60  ? 0.52419 0.39015 0.42588 0.12287  0.04225  -0.07933 249 VAL B CA  
459  C C   . VAL A 60  ? 0.59794 0.42258 0.45364 0.12022  0.04223  -0.08075 249 VAL B C   
460  O O   . VAL A 60  ? 0.67547 0.46542 0.50203 0.11009  0.02567  -0.07996 249 VAL B O   
461  C CB  . VAL A 60  ? 0.53727 0.41871 0.45908 0.10125  0.02948  -0.07388 249 VAL B CB  
462  C CG1 . VAL A 60  ? 0.49094 0.38246 0.41754 0.08440  0.03451  -0.07008 249 VAL B CG1 
463  C CG2 . VAL A 60  ? 0.43150 0.35183 0.39513 0.10386  0.02909  -0.07315 249 VAL B CG2 
464  N N   . ILE A 61  ? 0.61841 0.44594 0.46700 0.12860  0.06036  -0.08236 250 ILE B N   
465  C CA  . ILE A 61  ? 0.69317 0.47973 0.49405 0.12761  0.06038  -0.08392 250 ILE B CA  
466  C C   . ILE A 61  ? 0.70330 0.49308 0.50635 0.10456  0.05222  -0.07868 250 ILE B C   
467  O O   . ILE A 61  ? 0.71197 0.53728 0.54667 0.09682  0.06280  -0.07457 250 ILE B O   
468  C CB  . ILE A 61  ? 0.77581 0.57185 0.57407 0.13988  0.08147  -0.08338 250 ILE B CB  
469  C CG1 . ILE A 61  ? 0.73737 0.53654 0.54033 0.15909  0.08634  -0.08571 250 ILE B CG1 
470  C CG2 . ILE A 61  ? 0.85800 0.61530 0.60874 0.13541  0.07871  -0.08244 250 ILE B CG2 
471  C CD1 . ILE A 61  ? 0.73351 0.57587 0.57395 0.16996  0.10959  -0.08456 250 ILE B CD1 
472  N N   . PRO A 62  ? 0.74239 0.49704 0.51477 0.09275  0.03291  -0.07806 251 PRO B N   
473  C CA  . PRO A 62  ? 0.67508 0.43555 0.45254 0.07252  0.02428  -0.07238 251 PRO B CA  
474  C C   . PRO A 62  ? 0.70780 0.44967 0.45467 0.07554  0.03275  -0.07310 251 PRO B C   
475  O O   . PRO A 62  ? 0.71727 0.43179 0.42934 0.09194  0.04222  -0.07824 251 PRO B O   
476  C CB  . PRO A 62  ? 0.69205 0.42253 0.45044 0.05976  -0.00027 -0.07111 251 PRO B CB  
477  C CG  . PRO A 62  ? 0.76261 0.46308 0.49721 0.07391  -0.00409 -0.07684 251 PRO B CG  
478  C CD  . PRO A 62  ? 0.78562 0.49318 0.51782 0.09695  0.01728  -0.08185 251 PRO B CD  
479  N N   . PRO A 63  ? 0.69222 0.44686 0.44897 0.06151  0.03030  -0.06759 252 PRO B N   
480  C CA  . PRO A 63  ? 0.69948 0.43156 0.42167 0.06428  0.03645  -0.06751 252 PRO B CA  
481  C C   . PRO A 63  ? 0.74975 0.42682 0.41583 0.06617  0.01930  -0.07184 252 PRO B C   
482  O O   . PRO A 63  ? 0.77452 0.43625 0.43625 0.05515  -0.00349 -0.07151 252 PRO B O   
483  C CB  . PRO A 63  ? 0.71524 0.47117 0.46222 0.04775  0.03137  -0.06008 252 PRO B CB  
484  C CG  . PRO A 63  ? 0.67812 0.45482 0.45898 0.03481  0.01581  -0.05704 252 PRO B CG  
485  C CD  . PRO A 63  ? 0.66726 0.45469 0.46383 0.04425  0.02214  -0.06105 252 PRO B CD  
486  N N   . ASP A 64  ? 0.78719 0.44336 0.42009 0.07726  0.02940  -0.07187 253 ASP B N   
487  C CA  . ASP A 64  ? 0.79093 0.40335 0.37881 0.07779  0.01245  -0.07151 253 ASP B CA  
488  C C   . ASP A 64  ? 0.83319 0.42943 0.40434 0.06292  -0.00687 -0.06801 253 ASP B C   
489  O O   . ASP A 64  ? 0.89157 0.49446 0.45957 0.06267  0.00306  -0.06544 253 ASP B O   
490  C CB  . ASP A 64  ? 0.83866 0.43490 0.39778 0.09572  0.03080  -0.07159 253 ASP B CB  
491  C CG  . ASP A 64  ? 0.93141 0.48011 0.44393 0.10046  0.01510  -0.07241 253 ASP B CG  
492  O OD1 . ASP A 64  ? 0.94464 0.46819 0.43859 0.08730  -0.01065 -0.07086 253 ASP B OD1 
493  O OD2 . ASP A 64  ? 0.87168 0.40876 0.36738 0.11734  0.02833  -0.07415 253 ASP B OD2 
494  N N   . PRO A 65  ? 0.85063 0.42746 0.41330 0.04990  -0.03474 -0.06669 254 PRO B N   
495  C CA  . PRO A 65  ? 0.87573 0.44116 0.42757 0.03606  -0.05553 -0.06242 254 PRO B CA  
496  C C   . PRO A 65  ? 0.82557 0.35702 0.33147 0.04454  -0.05492 -0.06084 254 PRO B C   
497  O O   . PRO A 65  ? 0.84775 0.37368 0.34538 0.03687  -0.06684 -0.05716 254 PRO B O   
498  C CB  . PRO A 65  ? 0.91591 0.47086 0.47379 0.02120  -0.08342 -0.06008 254 PRO B CB  
499  C CG  . PRO A 65  ? 0.91414 0.45463 0.46129 0.03170  -0.07747 -0.06349 254 PRO B CG  
500  C CD  . PRO A 65  ? 0.87885 0.44607 0.44536 0.04632  -0.04874 -0.06769 254 PRO B CD  
501  N N   . ASN A 66  ? 0.86640 0.37390 0.34165 0.06082  -0.04194 -0.06308 255 ASN B N   
502  C CA  . ASN A 66  ? 0.97666 0.44849 0.40530 0.07022  -0.03920 -0.06129 255 ASN B CA  
503  C C   . ASN A 66  ? 0.81385 0.30202 0.24484 0.07686  -0.01469 -0.05892 255 ASN B C   
504  O O   . ASN A 66  ? 0.85785 0.31706 0.25133 0.08231  -0.01347 -0.05613 255 ASN B O   
505  C CB  . ASN A 66  ? 0.88742 0.32819 0.28238 0.08638  -0.03162 -0.06402 255 ASN B CB  
506  C CG  . ASN A 66  ? 0.99011 0.40382 0.37176 0.07954  -0.05771 -0.06503 255 ASN B CG  
507  O OD1 . ASN A 66  ? 0.96159 0.36530 0.34334 0.06325  -0.08466 -0.06224 255 ASN B OD1 
508  N ND2 . ASN A 66  ? 0.91720 0.32007 0.28924 0.09170  -0.04992 -0.06827 255 ASN B ND2 
509  N N   . PHE A 67  ? 0.88404 0.41556 0.35711 0.07623  0.00467  -0.05937 256 PHE B N   
510  C CA  . PHE A 67  ? 0.96350 0.51409 0.44490 0.07921  0.02775  -0.05561 256 PHE B CA  
511  C C   . PHE A 67  ? 0.93313 0.49773 0.42977 0.06486  0.01607  -0.05246 256 PHE B C   
512  O O   . PHE A 67  ? 0.97911 0.55727 0.48147 0.06561  0.03359  -0.04828 256 PHE B O   
513  C CB  . PHE A 67  ? 0.89041 0.48158 0.41164 0.08689  0.05681  -0.05685 256 PHE B CB  
514  C CG  . PHE A 67  ? 0.98705 0.57035 0.49329 0.10401  0.07808  -0.05709 256 PHE B CG  
515  C CD1 . PHE A 67  ? 0.99813 0.56157 0.47319 0.11157  0.09251  -0.05258 256 PHE B CD1 
516  C CD2 . PHE A 67  ? 0.93130 0.52649 0.45445 0.11315  0.08361  -0.06150 256 PHE B CD2 
517  C CE1 . PHE A 67  ? 1.01197 0.56911 0.47422 0.12761  0.11304  -0.05255 256 PHE B CE1 
518  C CE2 . PHE A 67  ? 1.06241 0.65211 0.57323 0.12993  0.10301  -0.06167 256 PHE B CE2 
519  C CZ  . PHE A 67  ? 1.08457 0.65608 0.56558 0.13702  0.11829  -0.05720 256 PHE B CZ  
520  N N   . GLN A 68  ? 0.86157 0.42381 0.36628 0.05142  -0.01306 -0.05335 257 GLN B N   
521  C CA  . GLN A 68  ? 0.88904 0.47201 0.41713 0.03800  -0.02473 -0.05073 257 GLN B CA  
522  C C   . GLN A 68  ? 0.85446 0.41292 0.35273 0.03421  -0.04327 -0.04543 257 GLN B C   
523  O O   . GLN A 68  ? 0.94937 0.47527 0.41843 0.03421  -0.06288 -0.04488 257 GLN B O   
524  C CB  . GLN A 68  ? 0.88837 0.49582 0.45950 0.02398  -0.04561 -0.04995 257 GLN B CB  
525  C CG  . GLN A 68  ? 0.83943 0.48461 0.45733 0.01004  -0.05750 -0.04124 257 GLN B CG  
526  C CD  . GLN A 68  ? 0.92683 0.61719 0.59075 0.01105  -0.03331 -0.03699 257 GLN B CD  
527  O OE1 . GLN A 68  ? 0.89660 0.62287 0.60740 0.00455  -0.03180 -0.03533 257 GLN B OE1 
528  N NE2 . GLN A 68  ? 0.94865 0.63420 0.59636 0.01863  -0.01457 -0.03500 257 GLN B NE2 
529  N N   . SER A 69  ? 0.90604 0.48573 0.42222 0.03091  -0.03717 -0.03888 258 SER B N   
530  C CA  . SER A 69  ? 0.94765 0.50501 0.43528 0.02882  -0.05484 -0.03370 258 SER B CA  
531  C C   . SER A 69  ? 0.81872 0.41817 0.36158 0.01694  -0.06843 -0.02563 258 SER B C   
532  O O   . SER A 69  ? 0.77212 0.41605 0.36915 0.01263  -0.05518 -0.02335 258 SER B O   
533  C CB  . SER A 69  ? 0.90678 0.44436 0.35892 0.04016  -0.03044 -0.03037 258 SER B CB  
534  O OG  . SER A 69  ? 0.99815 0.49579 0.40811 0.04960  -0.03064 -0.03133 258 SER B OG  
535  N N   . GLY A 70  ? 0.84280 0.42649 0.36980 0.01288  -0.09569 -0.02141 259 GLY B N   
536  C CA  . GLY A 70  ? 0.85056 0.47164 0.42613 0.00481  -0.10888 -0.01310 259 GLY B CA  
537  C C   . GLY A 70  ? 0.87789 0.48316 0.42898 0.01070  -0.11229 -0.00638 259 GLY B C   
538  O O   . GLY A 70  ? 0.93773 0.50499 0.43528 0.02039  -0.09933 -0.00751 259 GLY B O   
539  N N   . CYS A 71  ? 0.88906 0.52197 0.47739 0.00611  -0.12862 0.00119  260 CYS B N   
540  C CA  . CYS A 71  ? 0.94462 0.56276 0.51207 0.01269  -0.13543 0.00839  260 CYS B CA  
541  C C   . CYS A 71  ? 0.95070 0.55489 0.50669 0.00944  -0.17593 0.01124  260 CYS B C   
542  O O   . CYS A 71  ? 0.97870 0.60127 0.56471 -0.00099 -0.19784 0.01008  260 CYS B O   
543  C CB  . CYS A 71  ? 0.80779 0.46664 0.42519 0.01340  -0.12122 0.01540  260 CYS B CB  
544  S SG  . CYS A 71  ? 0.72708 0.44427 0.42275 0.00409  -0.13761 0.01951  260 CYS B SG  
545  N N   . ASN A 72  ? 0.94927 0.52080 0.46223 0.01785  -0.18583 0.01568  261 ASN B N   
546  C CA  . ASN A 72  ? 1.11491 0.67846 0.62962 0.01541  -0.21777 0.01679  261 ASN B CA  
547  C C   . ASN A 72  ? 1.12990 0.72179 0.67816 0.01915  -0.22890 0.02698  261 ASN B C   
548  O O   . ASN A 72  ? 1.21763 0.78677 0.73834 0.02830  -0.23005 0.03027  261 ASN B O   
549  C CB  . ASN A 72  ? 1.13097 0.63941 0.58229 0.02356  -0.21445 0.01227  261 ASN B CB  
550  C CG  . ASN A 72  ? 1.24110 0.71962 0.65565 0.02552  -0.19339 0.00350  261 ASN B CG  
551  O OD1 . ASN A 72  ? 1.19236 0.68068 0.60834 0.02795  -0.16449 0.00216  261 ASN B OD1 
552  N ND2 . ASN A 72  ? 1.29493 0.73661 0.67733 0.02538  -0.20757 -0.00198 261 ASN B ND2 
553  N N   . CYS A 73  ? 1.05282 0.69363 0.66091 0.01330  -0.23631 0.03223  262 CYS B N   
554  C CA  . CYS A 73  ? 1.06061 0.73495 0.71077 0.01965  -0.24013 0.04193  262 CYS B CA  
555  C C   . CYS A 73  ? 1.11871 0.82477 0.81512 0.01281  -0.27323 0.04586  262 CYS B C   
556  O O   . CYS A 73  ? 1.09084 0.83953 0.84009 0.01559  -0.27901 0.05398  262 CYS B O   
557  C CB  . CYS A 73  ? 0.91279 0.62700 0.61078 0.02039  -0.20659 0.04284  262 CYS B CB  
558  S SG  . CYS A 73  ? 0.88119 0.56393 0.53569 0.02791  -0.16628 0.03996  262 CYS B SG  
559  N N   . SER A 74  ? 1.15594 0.84287 0.83692 0.00380  -0.29064 0.03984  263 SER B N   
560  C CA  . SER A 74  ? 1.18632 0.90150 0.91154 -0.00472 -0.31883 0.04352  263 SER B CA  
561  C C   . SER A 74  ? 1.14301 0.91765 0.94222 -0.01547 -0.31880 0.04821  263 SER B C   
562  O O   . SER A 74  ? 1.08076 0.89393 0.93180 -0.02023 -0.33529 0.05463  263 SER B O   
563  C CB  . SER A 74  ? 1.15556 0.87324 0.88318 0.00673  -0.33298 0.05037  263 SER B CB  
564  O OG  . SER A 74  ? 1.17303 0.83431 0.83101 0.01627  -0.33055 0.04634  263 SER B OG  
565  N N   . GLY A 78  ? 0.73022 0.71380 0.76617 0.01371  -0.21636 0.07311  267 GLY B N   
566  C CA  . GLY A 78  ? 0.73301 0.67039 0.71243 0.00640  -0.21286 0.06367  267 GLY B CA  
567  C C   . GLY A 78  ? 0.81690 0.71044 0.74127 0.01883  -0.20412 0.06168  267 GLY B C   
568  O O   . GLY A 78  ? 0.82475 0.70008 0.72795 0.02762  -0.22394 0.06648  267 GLY B O   
569  N N   . CYS A 79  ? 0.78943 0.66488 0.68971 0.01915  -0.17512 0.05518  268 CYS B N   
570  C CA  . CYS A 79  ? 0.70830 0.54522 0.56133 0.02978  -0.16334 0.05513  268 CYS B CA  
571  C C   . CYS A 79  ? 0.62059 0.47164 0.49448 0.04344  -0.15923 0.06258  268 CYS B C   
572  O O   . CYS A 79  ? 0.60134 0.49357 0.52655 0.04556  -0.15493 0.06578  268 CYS B O   
573  C CB  . CYS A 79  ? 0.68600 0.50648 0.51687 0.02577  -0.13257 0.04752  268 CYS B CB  
574  S SG  . CYS A 79  ? 0.57665 0.38209 0.38570 0.01323  -0.13393 0.03827  268 CYS B SG  
575  N N   . ASP A 80  ? 0.67800 0.49104 0.50783 0.05379  -0.15976 0.06561  269 ASP B N   
576  C CA  . ASP A 80  ? 0.75917 0.57448 0.59776 0.06879  -0.15739 0.07273  269 ASP B CA  
577  C C   . ASP A 80  ? 0.70032 0.49893 0.52334 0.07004  -0.12497 0.06989  269 ASP B C   
578  O O   . ASP A 80  ? 0.69371 0.45629 0.47216 0.06523  -0.11125 0.06640  269 ASP B O   
579  C CB  . ASP A 80  ? 0.82287 0.60346 0.62108 0.07994  -0.18126 0.07916  269 ASP B CB  
580  C CG  . ASP A 80  ? 0.84379 0.62552 0.65124 0.09777  -0.18182 0.08718  269 ASP B CG  
581  O OD1 . ASP A 80  ? 0.88582 0.64275 0.66972 0.10245  -0.15857 0.08707  269 ASP B OD1 
582  O OD2 . ASP A 80  ? 0.90888 0.71656 0.74859 0.10718  -0.20585 0.09385  269 ASP B OD2 
583  N N   . LEU A 81  ? 0.66061 0.48527 0.52060 0.07633  -0.11270 0.07160  270 LEU B N   
584  C CA  . LEU A 81  ? 0.69938 0.50937 0.54853 0.07559  -0.08446 0.06841  270 LEU B CA  
585  C C   . LEU A 81  ? 0.72379 0.48772 0.52664 0.08503  -0.08107 0.07343  270 LEU B C   
586  O O   . LEU A 81  ? 0.67028 0.40790 0.44687 0.07913  -0.05962 0.07093  270 LEU B O   
587  C CB  . LEU A 81  ? 0.61101 0.45697 0.50739 0.08046  -0.07404 0.06816  270 LEU B CB  
588  C CG  . LEU A 81  ? 0.59539 0.44389 0.49777 0.07149  -0.04785 0.06091  270 LEU B CG  
589  C CD1 . LEU A 81  ? 0.44512 0.30616 0.35310 0.05546  -0.04377 0.05393  270 LEU B CD1 
590  C CD2 . LEU A 81  ? 0.51699 0.39492 0.45832 0.07962  -0.04051 0.06131  270 LEU B CD2 
591  N N   . ASN A 82  ? 0.69825 0.45184 0.49140 0.09924  -0.10236 0.08118  271 ASN B N   
592  C CA  . ASN A 82  ? 0.83063 0.53636 0.57617 0.10967  -0.10112 0.08719  271 ASN B CA  
593  C C   . ASN A 82  ? 0.88329 0.54394 0.56941 0.10417  -0.10455 0.08784  271 ASN B C   
594  O O   . ASN A 82  ? 0.99182 0.60687 0.63106 0.11042  -0.09995 0.09325  271 ASN B O   
595  C CB  . ASN A 82  ? 0.87406 0.58578 0.63215 0.12991  -0.12363 0.09574  271 ASN B CB  
596  C CG  . ASN A 82  ? 0.83093 0.58977 0.64863 0.13814  -0.11973 0.09581  271 ASN B CG  
597  O OD1 . ASN A 82  ? 0.84371 0.61413 0.67877 0.13200  -0.09660 0.09029  271 ASN B OD1 
598  N ND2 . ASN A 82  ? 0.91035 0.69671 0.75943 0.15267  -0.14254 0.10236  271 ASN B ND2 
599  N N   . ASN A 83  ? 0.85407 0.52416 0.53916 0.09332  -0.11177 0.08269  272 ASN B N   
600  C CA  . ASN A 83  ? 0.94081 0.56730 0.56697 0.08845  -0.11086 0.08187  272 ASN B CA  
601  C C   . ASN A 83  ? 0.86651 0.50271 0.49595 0.07329  -0.09339 0.07301  272 ASN B C   
602  O O   . ASN A 83  ? 0.91190 0.55511 0.54082 0.06823  -0.10770 0.06876  272 ASN B O   
603  C CB  . ASN A 83  ? 1.08389 0.69761 0.68803 0.09422  -0.14457 0.08474  272 ASN B CB  
604  N N   . PRO A 84  ? 0.86306 0.49759 0.49464 0.06611  -0.06321 0.07030  273 PRO B N   
605  C CA  . PRO A 84  ? 0.78405 0.43076 0.42257 0.05325  -0.04516 0.06206  273 PRO B CA  
606  C C   . PRO A 84  ? 0.89016 0.49729 0.47233 0.05106  -0.03811 0.06110  273 PRO B C   
607  O O   . PRO A 84  ? 0.87618 0.49247 0.46174 0.04327  -0.02621 0.05414  273 PRO B O   
608  C CB  . PRO A 84  ? 0.73180 0.38951 0.39277 0.04724  -0.01771 0.06079  273 PRO B CB  
609  C CG  . PRO A 84  ? 0.71262 0.33749 0.34635 0.05530  -0.01557 0.06915  273 PRO B CG  
610  C CD  . PRO A 84  ? 0.79887 0.42136 0.42971 0.06915  -0.04550 0.07457  273 PRO B CD  
611  N N   . SER A 85  ? 0.88431 0.44591 0.41238 0.05912  -0.04428 0.06803  274 SER B N   
612  C CA  . SER A 85  ? 0.99259 0.51175 0.46031 0.05859  -0.03410 0.06778  274 SER B CA  
613  C C   . SER A 85  ? 1.00192 0.51814 0.45466 0.05880  -0.05495 0.06149  274 SER B C   
614  O O   . SER A 85  ? 1.00083 0.50109 0.42569 0.05570  -0.04032 0.05607  274 SER B O   
615  C CB  . SER A 85  ? 1.09120 0.57185 0.51707 0.06605  -0.03553 0.07271  274 SER B CB  
616  O OG  . SER A 85  ? 1.14277 0.62231 0.58033 0.06544  -0.01894 0.07850  274 SER B OG  
617  N N   . ARG A 86  ? 1.10503 0.63780 0.57893 0.06222  -0.08867 0.06165  275 ARG B N   
618  C CA  . ARG A 86  ? 1.08684 0.61166 0.54405 0.06076  -0.11283 0.05579  275 ARG B CA  
619  C C   . ARG A 86  ? 1.04014 0.59291 0.52698 0.05073  -0.10365 0.04673  275 ARG B C   
620  O O   . ARG A 86  ? 0.95018 0.48029 0.40343 0.04928  -0.11066 0.04076  275 ARG B O   
621  C CB  . ARG A 86  ? 1.16768 0.71134 0.65246 0.06429  -0.15074 0.05857  275 ARG B CB  
622  C CG  . ARG A 86  ? 1.20517 0.79809 0.75639 0.06482  -0.15361 0.06335  275 ARG B CG  
623  C CD  . ARG A 86  ? 1.32056 0.93152 0.89715 0.07101  -0.19081 0.06910  275 ARG B CD  
624  N NE  . ARG A 86  ? 1.43636 1.03406 1.00270 0.08335  -0.19352 0.07573  275 ARG B NE  
625  C CZ  . ARG A 86  ? 1.37294 0.99797 0.97691 0.09134  -0.21564 0.08131  275 ARG B CZ  
626  N NH1 . ARG A 86  ? 1.37307 1.04366 1.03176 0.08728  -0.23613 0.08186  275 ARG B NH1 
627  N NH2 . ARG A 86  ? 1.39960 1.00765 0.98829 0.10348  -0.21582 0.08669  275 ARG B NH2 
628  N N   . CYS A 87  ? 0.89413 0.49307 0.44110 0.04452  -0.08836 0.04491  276 CYS B N   
629  C CA  . CYS A 87  ? 0.92861 0.55718 0.50904 0.03556  -0.08238 0.03657  276 CYS B CA  
630  C C   . CYS A 87  ? 0.84073 0.45148 0.39328 0.03399  -0.05268 0.03124  276 CYS B C   
631  O O   . CYS A 87  ? 0.83464 0.44241 0.38430 0.03428  -0.02567 0.03395  276 CYS B O   
632  C CB  . CYS A 87  ? 0.74731 0.42751 0.39613 0.03076  -0.07582 0.03687  276 CYS B CB  
633  S SG  . CYS A 87  ? 0.57615 0.29306 0.26788 0.02026  -0.07439 0.02828  276 CYS B SG  
634  N N   . GLU A 88  ? 0.78066 0.38013 0.31449 0.03228  -0.05772 0.02389  277 GLU B N   
635  C CA  . GLU A 88  ? 0.90968 0.49360 0.41769 0.03360  -0.03007 0.01857  277 GLU B CA  
636  C C   . GLU A 88  ? 0.83449 0.46127 0.39574 0.02724  -0.00951 0.01392  277 GLU B C   
637  O O   . GLU A 88  ? 0.70270 0.32528 0.25349 0.02888  0.01668  0.01073  277 GLU B O   
638  C CB  . GLU A 88  ? 0.93113 0.47906 0.39068 0.03708  -0.04394 0.01193  277 GLU B CB  
639  C CG  . GLU A 88  ? 1.00245 0.49766 0.39604 0.04531  -0.05448 0.01459  277 GLU B CG  
640  C CD  . GLU A 88  ? 1.11937 0.60837 0.51384 0.04353  -0.09556 0.01504  277 GLU B CD  
641  O OE1 . GLU A 88  ? 1.07836 0.60140 0.51595 0.03683  -0.11582 0.01760  277 GLU B OE1 
642  O OE2 . GLU A 88  ? 1.13398 0.58666 0.49089 0.04853  -0.10691 0.01314  277 GLU B OE2 
643  N N   . CYS A 89  ? 0.67476 0.34253 0.29209 0.02086  -0.02038 0.01381  278 CYS B N   
644  C CA  . CYS A 89  ? 0.67099 0.37651 0.33537 0.01534  -0.00310 0.00961  278 CYS B CA  
645  C C   . CYS A 89  ? 0.69210 0.40950 0.37258 0.01407  0.02332  0.01298  278 CYS B C   
646  O O   . CYS A 89  ? 0.74364 0.48726 0.45612 0.00996  0.03976  0.00918  278 CYS B O   
647  C CB  . CYS A 89  ? 0.64121 0.38331 0.35575 0.00933  -0.02119 0.00949  278 CYS B CB  
648  S SG  . CYS A 89  ? 0.55387 0.28750 0.25999 0.00599  -0.05328 0.00631  278 CYS B SG  
649  N N   . LEU A 90  ? 0.75817 0.45497 0.41630 0.01701  0.02626  0.02018  279 LEU B N   
650  C CA  . LEU A 90  ? 0.72252 0.42523 0.39319 0.01381  0.04909  0.02431  279 LEU B CA  
651  C C   . LEU A 90  ? 0.74947 0.42079 0.37742 0.01568  0.07257  0.02734  279 LEU B C   
652  O O   . LEU A 90  ? 0.81038 0.47377 0.43515 0.01267  0.08841  0.03351  279 LEU B O   
653  C CB  . LEU A 90  ? 0.70627 0.40758 0.38483 0.01562  0.03752  0.03121  279 LEU B CB  
654  C CG  . LEU A 90  ? 0.68019 0.41258 0.40019 0.01582  0.01601  0.03023  279 LEU B CG  
655  C CD1 . LEU A 90  ? 0.64238 0.36826 0.36330 0.02168  0.00621  0.03771  279 LEU B CD1 
656  C CD2 . LEU A 90  ? 0.54674 0.31757 0.31512 0.00890  0.02638  0.02471  279 LEU B CD2 
657  N N   . ASP A 91  ? 0.87595 0.52698 0.46901 0.02070  0.07602  0.02348  280 ASP B N   
658  C CA  . ASP A 91  ? 1.01606 0.63539 0.56420 0.02433  0.10052  0.02719  280 ASP B CA  
659  C C   . ASP A 91  ? 0.95777 0.60339 0.53799 0.01787  0.13248  0.02719  280 ASP B C   
660  O O   . ASP A 91  ? 0.88446 0.51475 0.44663 0.01662  0.15516  0.03331  280 ASP B O   
661  C CB  . ASP A 91  ? 1.13048 0.71786 0.62860 0.03366  0.09559  0.02230  280 ASP B CB  
662  C CG  . ASP A 91  ? 1.22001 0.76797 0.67010 0.03978  0.06698  0.02481  280 ASP B CG  
663  O OD1 . ASP A 91  ? 1.23366 0.76469 0.66839 0.04029  0.06289  0.03298  280 ASP B OD1 
664  O OD2 . ASP A 91  ? 1.19333 0.72600 0.62109 0.04400  0.04705  0.01857  280 ASP B OD2 
665  N N   . ASP A 92  ? 0.77101 0.45813 0.40302 0.01322  0.13282  0.02056  281 ASP B N   
666  C CA  . ASP A 92  ? 0.76735 0.48390 0.43620 0.00647  0.15900  0.02045  281 ASP B CA  
667  C C   . ASP A 92  ? 0.84847 0.57467 0.54220 -0.00444 0.16623  0.02696  281 ASP B C   
668  O O   . ASP A 92  ? 0.81921 0.56495 0.53972 -0.01242 0.18812  0.02870  281 ASP B O   
669  C CB  . ASP A 92  ? 0.83655 0.59181 0.55111 0.00545  0.15352  0.01159  281 ASP B CB  
670  C CG  . ASP A 92  ? 0.84664 0.59205 0.53822 0.01597  0.15449  0.00506  281 ASP B CG  
671  O OD1 . ASP A 92  ? 0.99066 0.69783 0.62860 0.02431  0.15795  0.00667  281 ASP B OD1 
672  O OD2 . ASP A 92  ? 0.93162 0.70388 0.65504 0.01673  0.15138  -0.00180 281 ASP B OD2 
673  N N   . LEU A 93  ? 0.84754 0.56023 0.53380 -0.00476 0.14781  0.03063  282 LEU B N   
674  C CA  . LEU A 93  ? 0.76087 0.47573 0.46491 -0.01349 0.15240  0.03620  282 LEU B CA  
675  C C   . LEU A 93  ? 0.86415 0.54031 0.52524 -0.01464 0.16857  0.04629  282 LEU B C   
676  O O   . LEU A 93  ? 0.89380 0.53536 0.50541 -0.00557 0.16461  0.04941  282 LEU B O   
677  C CB  . LEU A 93  ? 0.73288 0.45076 0.44873 -0.01051 0.12659  0.03574  282 LEU B CB  
678  C CG  . LEU A 93  ? 0.61677 0.37261 0.37712 -0.01109 0.11229  0.02759  282 LEU B CG  
679  C CD1 . LEU A 93  ? 0.64208 0.39595 0.40176 -0.00397 0.08643  0.02837  282 LEU B CD1 
680  C CD2 . LEU A 93  ? 0.58767 0.36982 0.39026 -0.02103 0.12177  0.02545  282 LEU B CD2 
681  N N   . ASP A 94  ? 0.84351 0.52687 0.52686 -0.02588 0.18309  0.05000  283 ASP B N   
682  C CA  . ASP A 94  ? 0.96195 0.61762 0.62006 -0.02751 0.19149  0.05670  283 ASP B CA  
683  C C   . ASP A 94  ? 0.90027 0.52375 0.53084 -0.02312 0.17458  0.06229  283 ASP B C   
684  O O   . ASP A 94  ? 0.91838 0.54762 0.56220 -0.02176 0.15941  0.06185  283 ASP B O   
685  C CB  . ASP A 94  ? 0.97331 0.65119 0.66955 -0.04197 0.20867  0.05783  283 ASP B CB  
686  C CG  . ASP A 94  ? 1.09262 0.81311 0.83139 -0.04614 0.21987  0.05195  283 ASP B CG  
687  O OD1 . ASP A 94  ? 1.19725 0.91995 0.92324 -0.03698 0.22517  0.04931  283 ASP B OD1 
688  O OD2 . ASP A 94  ? 1.08310 0.83347 0.86699 -0.05757 0.22154  0.04966  283 ASP B OD2 
689  N N   . GLU A 95  ? 0.84244 0.43165 0.43487 -0.01956 0.17717  0.06791  284 GLU B N   
690  C CA  . GLU A 95  ? 0.86671 0.42580 0.43489 -0.01426 0.16165  0.07326  284 GLU B CA  
691  C C   . GLU A 95  ? 0.82928 0.39685 0.42806 -0.02529 0.16568  0.07469  284 GLU B C   
692  O O   . GLU A 95  ? 0.86614 0.45156 0.49204 -0.03868 0.18310  0.07386  284 GLU B O   
693  C CB  . GLU A 95  ? 0.93268 0.45212 0.45186 -0.00814 0.16441  0.07833  284 GLU B CB  
694  C CG  . GLU A 95  ? 1.02748 0.52589 0.50570 0.00613  0.14959  0.07682  284 GLU B CG  
695  C CD  . GLU A 95  ? 1.07935 0.56891 0.54777 0.01713  0.11909  0.07776  284 GLU B CD  
696  O OE1 . GLU A 95  ? 1.19173 0.67357 0.66519 0.01824  0.11085  0.08196  284 GLU B OE1 
697  O OE2 . GLU A 95  ? 1.04673 0.53773 0.50402 0.02511  0.10228  0.07431  284 GLU B OE2 
698  N N   . PRO A 96  ? 0.83988 0.39517 0.43598 -0.01915 0.14816  0.07667  285 PRO B N   
699  C CA  . PRO A 96  ? 0.87640 0.41609 0.44884 -0.00269 0.12414  0.07868  285 PRO B CA  
700  C C   . PRO A 96  ? 0.84654 0.41630 0.44386 0.00139  0.11198  0.07342  285 PRO B C   
701  O O   . PRO A 96  ? 0.79363 0.39763 0.43716 -0.00288 0.10930  0.06693  285 PRO B O   
702  C CB  . PRO A 96  ? 0.89137 0.41655 0.46640 0.00153  0.11366  0.08188  285 PRO B CB  
703  C CG  . PRO A 96  ? 0.79577 0.33968 0.40747 -0.01367 0.12805  0.07847  285 PRO B CG  
704  C CD  . PRO A 96  ? 0.71204 0.26781 0.33013 -0.02760 0.15003  0.07709  285 PRO B CD  
705  N N   . THR A 97  ? 0.84504 0.41059 0.41970 0.00983  0.10114  0.07198  286 THR B N   
706  C CA  . THR A 97  ? 0.80682 0.40980 0.41353 0.01298  0.08565  0.06289  286 THR B CA  
707  C C   . THR A 97  ? 0.67498 0.29770 0.31184 0.02051  0.06246  0.06157  286 THR B C   
708  O O   . THR A 97  ? 0.77148 0.37163 0.38766 0.03076  0.04778  0.06782  286 THR B O   
709  C CB  . THR A 97  ? 0.86028 0.44478 0.42821 0.02044  0.07572  0.06223  286 THR B CB  
710  O OG1 . THR A 97  ? 0.89503 0.46745 0.44007 0.01504  0.10077  0.06217  286 THR B OG1 
711  C CG2 . THR A 97  ? 0.82174 0.43947 0.42011 0.02304  0.05535  0.05393  286 THR B CG2 
712  N N   . HIS A 98  ? 0.60044 0.26534 0.28602 0.01643  0.06012  0.05397  287 HIS B N   
713  C CA  . HIS A 98  ? 0.61970 0.30860 0.33753 0.02375  0.04144  0.05271  287 HIS B CA  
714  C C   . HIS A 98  ? 0.57754 0.30865 0.33684 0.01886  0.03850  0.04435  287 HIS B C   
715  O O   . HIS A 98  ? 0.51116 0.25375 0.27945 0.00969  0.05283  0.03911  287 HIS B O   
716  C CB  . HIS A 98  ? 0.61257 0.29657 0.34234 0.02475  0.04752  0.05517  287 HIS B CB  
717  C CG  . HIS A 98  ? 0.62754 0.32171 0.37718 0.01118  0.06804  0.05066  287 HIS B CG  
718  N ND1 . HIS A 98  ? 0.55587 0.28775 0.34571 0.00516  0.07009  0.04257  287 HIS B ND1 
719  C CD2 . HIS A 98  ? 0.66834 0.33941 0.40365 0.00160  0.08591  0.05362  287 HIS B CD2 
720  C CE1 . HIS A 98  ? 0.60168 0.33425 0.40167 -0.00679 0.08656  0.04019  287 HIS B CE1 
721  N NE2 . HIS A 98  ? 0.68166 0.37894 0.45113 -0.01017 0.09657  0.04690  287 HIS B NE2 
722  N N   . PHE A 99  ? 0.56934 0.32382 0.35460 0.02553  0.02008  0.04397  288 PHE B N   
723  C CA  . PHE A 99  ? 0.45079 0.24364 0.27567 0.02085  0.01755  0.03745  288 PHE B CA  
724  C C   . PHE A 99  ? 0.46619 0.27561 0.31884 0.01570  0.03248  0.03355  288 PHE B C   
725  O O   . PHE A 99  ? 0.41277 0.20658 0.25902 0.01732  0.04015  0.03614  288 PHE B O   
726  C CB  . PHE A 99  ? 0.43772 0.25215 0.28507 0.02824  -0.00438 0.03988  288 PHE B CB  
727  C CG  . PHE A 99  ? 0.57252 0.37658 0.39925 0.02987  -0.02342 0.04162  288 PHE B CG  
728  C CD1 . PHE A 99  ? 0.51116 0.32711 0.34391 0.02259  -0.02845 0.03630  288 PHE B CD1 
729  C CD2 . PHE A 99  ? 0.52597 0.30471 0.32420 0.03900  -0.03803 0.04840  288 PHE B CD2 
730  C CE1 . PHE A 99  ? 0.49953 0.30070 0.30914 0.02327  -0.04797 0.03709  288 PHE B CE1 
731  C CE2 . PHE A 99  ? 0.58476 0.35055 0.36060 0.04002  -0.05855 0.04945  288 PHE B CE2 
732  C CZ  . PHE A 99  ? 0.62364 0.39990 0.40467 0.03159  -0.06367 0.04347  288 PHE B CZ  
733  N N   . ALA A 100 ? 0.36097 0.19870 0.24152 0.00944  0.03519  0.02711  289 ALA B N   
734  C CA  . ALA A 100 ? 0.39758 0.25014 0.30227 0.00450  0.04648  0.02261  289 ALA B CA  
735  C C   . ALA A 100 ? 0.37648 0.24056 0.30062 0.01271  0.04069  0.02417  289 ALA B C   
736  O O   . ALA A 100 ? 0.39052 0.25774 0.32597 0.01050  0.04923  0.02073  289 ALA B O   
737  C CB  . ALA A 100 ? 0.40436 0.28129 0.32978 -0.00292 0.04967  0.01569  289 ALA B CB  
738  N N   . TYR A 101 ? 0.38180 0.25179 0.30977 0.02263  0.02639  0.02933  290 TYR B N   
739  C CA  . TYR A 101 ? 0.35318 0.24106 0.30500 0.03241  0.02234  0.03140  290 TYR B CA  
740  C C   . TYR A 101 ? 0.45970 0.32894 0.39739 0.04596  0.01569  0.03859  290 TYR B C   
741  O O   . TYR A 101 ? 0.50126 0.35178 0.41586 0.04855  0.00653  0.04326  290 TYR B O   
742  C CB  . TYR A 101 ? 0.31730 0.23880 0.29804 0.03253  0.01130  0.03220  290 TYR B CB  
743  C CG  . TYR A 101 ? 0.33207 0.26716 0.32172 0.02037  0.01529  0.02584  290 TYR B CG  
744  C CD1 . TYR A 101 ? 0.33462 0.28195 0.33945 0.01655  0.02621  0.02050  290 TYR B CD1 
745  C CD2 . TYR A 101 ? 0.35966 0.29169 0.33888 0.01399  0.00714  0.02496  290 TYR B CD2 
746  C CE1 . TYR A 101 ? 0.33615 0.29447 0.34807 0.00715  0.02855  0.01509  290 TYR B CE1 
747  C CE2 . TYR A 101 ? 0.30911 0.25070 0.29450 0.00507  0.01065  0.01916  290 TYR B CE2 
748  C CZ  . TYR A 101 ? 0.29873 0.25453 0.30176 0.00191  0.02120  0.01457  290 TYR B CZ  
749  O OH  . TYR A 101 ? 0.22291 0.18691 0.23115 -0.00531 0.02341  0.00921  290 TYR B OH  
750  N N   . ASP A 102 ? 0.40197 0.27363 0.35047 0.05604  0.02014  0.03934  291 ASP B N   
751  C CA  . ASP A 102 ? 0.47970 0.33548 0.41809 0.07243  0.01402  0.04612  291 ASP B CA  
752  C C   . ASP A 102 ? 0.45518 0.34535 0.42570 0.08441  0.00070  0.05166  291 ASP B C   
753  O O   . ASP A 102 ? 0.37271 0.29501 0.36965 0.07744  -0.00423 0.05074  291 ASP B O   
754  C CB  . ASP A 102 ? 0.42597 0.26000 0.35409 0.07834  0.02661  0.04372  291 ASP B CB  
755  C CG  . ASP A 102 ? 0.43580 0.29323 0.38880 0.07766  0.03575  0.03768  291 ASP B CG  
756  O OD1 . ASP A 102 ? 0.47595 0.37001 0.45868 0.07717  0.03210  0.03781  291 ASP B OD1 
757  O OD2 . ASP A 102 ? 0.44979 0.28590 0.38985 0.07693  0.04616  0.03295  291 ASP B OD2 
758  N N   . ALA A 103 ? 0.50835 0.39232 0.47835 0.10264  -0.00532 0.05812  292 ALA B N   
759  C CA  . ALA A 103 ? 0.48483 0.40440 0.48966 0.11516  -0.01885 0.06508  292 ALA B CA  
760  C C   . ALA A 103 ? 0.48062 0.43986 0.52582 0.11756  -0.00926 0.06370  292 ALA B C   
761  O O   . ALA A 103 ? 0.50016 0.49744 0.58242 0.12338  -0.01863 0.06988  292 ALA B O   
762  C CB  . ALA A 103 ? 0.41487 0.31745 0.40947 0.13691  -0.02643 0.07244  292 ALA B CB  
763  N N   . GLN A 104 ? 0.42283 0.37384 0.46156 0.11287  0.00868  0.05637  293 GLN B N   
764  C CA  . GLN A 104 ? 0.46910 0.45140 0.53788 0.11527  0.01967  0.05480  293 GLN B CA  
765  C C   . GLN A 104 ? 0.38627 0.38760 0.46710 0.09556  0.02141  0.05008  293 GLN B C   
766  O O   . GLN A 104 ? 0.39209 0.41337 0.49084 0.09504  0.03196  0.04814  293 GLN B O   
767  C CB  . GLN A 104 ? 0.45756 0.41520 0.50755 0.12440  0.03643  0.04938  293 GLN B CB  
768  C CG  . GLN A 104 ? 0.54333 0.49375 0.59306 0.14975  0.03812  0.05475  293 GLN B CG  
769  C CD  . GLN A 104 ? 0.74473 0.67326 0.77703 0.15734  0.02381  0.06077  293 GLN B CD  
770  O OE1 . GLN A 104 ? 0.56145 0.44889 0.55633 0.14953  0.02305  0.05785  293 GLN B OE1 
771  N NE2 . GLN A 104 ? 0.75735 0.71359 0.81719 0.17229  0.01210  0.06995  293 GLN B NE2 
772  N N   . GLY A 105 ? 0.36883 0.36143 0.43685 0.08079  0.01189  0.04832  294 GLY B N   
773  C CA  . GLY A 105 ? 0.31101 0.31758 0.38729 0.06396  0.01282  0.04369  294 GLY B CA  
774  C C   . GLY A 105 ? 0.36383 0.35458 0.42420 0.05540  0.02709  0.03464  294 GLY B C   
775  O O   . GLY A 105 ? 0.44737 0.45209 0.51762 0.04487  0.02965  0.03086  294 GLY B O   
776  N N   . ARG A 106 ? 0.38830 0.34905 0.42422 0.05921  0.03508  0.03135  295 ARG B N   
777  C CA  . ARG A 106 ? 0.39981 0.34474 0.42198 0.05001  0.04602  0.02294  295 ARG B CA  
778  C C   . ARG A 106 ? 0.37069 0.29055 0.36900 0.03882  0.04599  0.02046  295 ARG B C   
779  O O   . ARG A 106 ? 0.38372 0.28636 0.36578 0.04215  0.04078  0.02522  295 ARG B O   
780  C CB  . ARG A 106 ? 0.36939 0.29655 0.38128 0.06063  0.05546  0.02061  295 ARG B CB  
781  C CG  . ARG A 106 ? 0.36644 0.31598 0.39765 0.07061  0.06141  0.02108  295 ARG B CG  
782  C CD  . ARG A 106 ? 0.41687 0.34062 0.42886 0.08081  0.07131  0.01666  295 ARG B CD  
783  N NE  . ARG A 106 ? 0.52577 0.42990 0.52572 0.09714  0.07054  0.02134  295 ARG B NE  
784  C CZ  . ARG A 106 ? 0.55784 0.47723 0.57245 0.11697  0.07268  0.02749  295 ARG B CZ  
785  N NH1 . ARG A 106 ? 0.49516 0.45123 0.53860 0.12149  0.07709  0.03054  295 ARG B NH1 
786  N NH2 . ARG A 106 ? 0.49797 0.39551 0.49868 0.13303  0.07102  0.03139  295 ARG B NH2 
787  N N   . VAL A 107 ? 0.31898 0.23739 0.31544 0.02609  0.05223  0.01357  296 VAL B N   
788  C CA  . VAL A 107 ? 0.37759 0.27665 0.35612 0.01521  0.05572  0.01176  296 VAL B CA  
789  C C   . VAL A 107 ? 0.45354 0.31977 0.40997 0.01743  0.06096  0.01316  296 VAL B C   
790  O O   . VAL A 107 ? 0.46628 0.32269 0.42071 0.02301  0.06423  0.01104  296 VAL B O   
791  C CB  . VAL A 107 ? 0.38310 0.29263 0.37072 0.00253  0.06101  0.00451  296 VAL B CB  
792  C CG1 . VAL A 107 ? 0.31349 0.21630 0.30251 0.00071  0.06644  -0.00105 296 VAL B CG1 
793  C CG2 . VAL A 107 ? 0.36521 0.26366 0.34083 -0.00760 0.06574  0.00417  296 VAL B CG2 
794  N N   . ARG A 108 ? 0.41377 0.25891 0.34951 0.01369  0.06194  0.01707  297 ARG B N   
795  C CA  . ARG A 108 ? 0.46272 0.27204 0.37385 0.01456  0.06676  0.01993  297 ARG B CA  
796  C C   . ARG A 108 ? 0.47114 0.26941 0.38150 0.00007  0.07649  0.01431  297 ARG B C   
797  O O   . ARG A 108 ? 0.44883 0.26627 0.37496 -0.01159 0.08003  0.00948  297 ARG B O   
798  C CB  . ARG A 108 ? 0.46067 0.24847 0.34643 0.01431  0.06574  0.02689  297 ARG B CB  
799  C CG  . ARG A 108 ? 0.46430 0.25656 0.34675 0.02893  0.05226  0.03308  297 ARG B CG  
800  C CD  . ARG A 108 ? 0.45805 0.23133 0.31318 0.02660  0.04987  0.03828  297 ARG B CD  
801  N NE  . ARG A 108 ? 0.54713 0.28140 0.37073 0.02162  0.06016  0.04207  297 ARG B NE  
802  C CZ  . ARG A 108 ? 0.53495 0.23622 0.32835 0.03113  0.05547  0.04966  297 ARG B CZ  
803  N NH1 . ARG A 108 ? 0.56870 0.27344 0.36133 0.04718  0.03923  0.05413  297 ARG B NH1 
804  N NH2 . ARG A 108 ? 0.55605 0.22004 0.32022 0.02400  0.06682  0.05354  297 ARG B NH2 
805  N N   . ALA A 109 ? 0.43935 0.20536 0.33138 0.00108  0.07945  0.01511  298 ALA B N   
806  C CA  . ALA A 109 ? 0.50468 0.25617 0.39512 -0.01480 0.08616  0.01040  298 ALA B CA  
807  C C   . ALA A 109 ? 0.46980 0.21889 0.35808 -0.03143 0.09462  0.01334  298 ALA B C   
808  O O   . ALA A 109 ? 0.54803 0.30982 0.45326 -0.04665 0.09928  0.00879  298 ALA B O   
809  C CB  . ALA A 109 ? 0.52331 0.23361 0.38914 -0.01032 0.08635  0.01120  298 ALA B CB  
810  N N   . ASP A 110 ? 0.47199 0.20522 0.33940 -0.02798 0.09690  0.02132  299 ASP B N   
811  C CA  . ASP A 110 ? 0.64049 0.36762 0.50056 -0.04181 0.10831  0.02552  299 ASP B CA  
812  C C   . ASP A 110 ? 0.57014 0.33012 0.44616 -0.04295 0.11012  0.02367  299 ASP B C   
813  O O   . ASP A 110 ? 0.68688 0.44516 0.55766 -0.05220 0.12179  0.02691  299 ASP B O   
814  C CB  . ASP A 110 ? 0.62653 0.31454 0.44872 -0.03694 0.11091  0.03539  299 ASP B CB  
815  C CG  . ASP A 110 ? 0.60230 0.29313 0.41169 -0.01931 0.10021  0.03920  299 ASP B CG  
816  O OD1 . ASP A 110 ? 0.59987 0.31996 0.43068 -0.00982 0.08975  0.03472  299 ASP B OD1 
817  O OD2 . ASP A 110 ? 0.73643 0.39889 0.51347 -0.01562 0.10156  0.04721  299 ASP B OD2 
818  N N   . THR A 111 ? 0.51888 0.30653 0.41250 -0.03353 0.09999  0.01903  300 THR B N   
819  C CA  . THR A 111 ? 0.55393 0.36890 0.46097 -0.03465 0.10046  0.01634  300 THR B CA  
820  C C   . THR A 111 ? 0.52411 0.35945 0.45583 -0.04816 0.10928  0.01089  300 THR B C   
821  O O   . THR A 111 ? 0.53631 0.37807 0.48503 -0.05369 0.10729  0.00597  300 THR B O   
822  C CB  . THR A 111 ? 0.48678 0.32453 0.40811 -0.02361 0.08702  0.01324  300 THR B CB  
823  O OG1 . THR A 111 ? 0.42230 0.24610 0.32618 -0.01115 0.07748  0.01911  300 THR B OG1 
824  C CG2 . THR A 111 ? 0.46482 0.32542 0.39670 -0.02519 0.08632  0.01004  300 THR B CG2 
825  N N   . GLY A 112 ? 0.56124 0.40595 0.49385 -0.05235 0.11850  0.01174  301 GLY B N   
826  C CA  . GLY A 112 ? 0.57771 0.44655 0.53765 -0.06302 0.12693  0.00744  301 GLY B CA  
827  C C   . GLY A 112 ? 0.57723 0.47603 0.56148 -0.05852 0.11729  -0.00023 301 GLY B C   
828  O O   . GLY A 112 ? 0.51677 0.41815 0.50016 -0.04981 0.10493  -0.00232 301 GLY B O   
829  N N   . ALA A 113 ? 0.61986 0.54213 0.62695 -0.06425 0.12381  -0.00369 302 ALA B N   
830  C CA  . ALA A 113 ? 0.59575 0.54405 0.62463 -0.06034 0.11499  -0.01067 302 ALA B CA  
831  C C   . ALA A 113 ? 0.57159 0.52380 0.58947 -0.04933 0.11118  -0.01128 302 ALA B C   
832  O O   . ALA A 113 ? 0.48039 0.44881 0.51101 -0.04516 0.10240  -0.01617 302 ALA B O   
833  C CB  . ALA A 113 ? 0.60126 0.57377 0.66065 -0.06924 0.12140  -0.01401 302 ALA B CB  
834  N N   . VAL A 114 ? 0.44942 0.38348 0.44070 -0.04490 0.11647  -0.00640 303 VAL B N   
835  C CA  . VAL A 114 ? 0.48072 0.41234 0.45626 -0.03561 0.11161  -0.00732 303 VAL B CA  
836  C C   . VAL A 114 ? 0.40977 0.32159 0.36152 -0.02962 0.09947  -0.00334 303 VAL B C   
837  O O   . VAL A 114 ? 0.45876 0.34877 0.38981 -0.02975 0.10274  0.00236  303 VAL B O   
838  C CB  . VAL A 114 ? 0.48323 0.40830 0.44367 -0.03383 0.12713  -0.00563 303 VAL B CB  
839  C CG1 . VAL A 114 ? 0.48152 0.39160 0.41342 -0.02376 0.11978  -0.00640 303 VAL B CG1 
840  C CG2 . VAL A 114 ? 0.49880 0.45092 0.48961 -0.03694 0.13746  -0.00969 303 VAL B CG2 
841  N N   . ILE A 115 ? 0.40252 0.32218 0.35826 -0.02461 0.08505  -0.00565 304 ILE B N   
842  C CA  . ILE A 115 ? 0.42350 0.33177 0.36487 -0.01919 0.07101  -0.00165 304 ILE B CA  
843  C C   . ILE A 115 ? 0.47093 0.37001 0.39249 -0.01497 0.06342  -0.00249 304 ILE B C   
844  O O   . ILE A 115 ? 0.44770 0.35799 0.37828 -0.01496 0.06103  -0.00732 304 ILE B O   
845  C CB  . ILE A 115 ? 0.35919 0.28494 0.32397 -0.01827 0.06037  -0.00232 304 ILE B CB  
846  C CG1 . ILE A 115 ? 0.38756 0.31428 0.36353 -0.02081 0.06680  -0.00212 304 ILE B CG1 
847  C CG2 . ILE A 115 ? 0.36406 0.28546 0.32171 -0.01270 0.04537  0.00250  304 ILE B CG2 
848  C CD1 . ILE A 115 ? 0.27317 0.21460 0.26807 -0.01800 0.05977  -0.00306 304 ILE B CD1 
849  N N   . TYR A 116 ? 0.46194 0.33678 0.35310 -0.01102 0.05834  0.00207  305 TYR B N   
850  C CA  . TYR A 116 ? 0.46198 0.31991 0.32598 -0.00706 0.04883  0.00105  305 TYR B CA  
851  C C   . TYR A 116 ? 0.48135 0.34092 0.34859 -0.00564 0.02597  0.00404  305 TYR B C   
852  O O   . TYR A 116 ? 0.50840 0.35440 0.36147 -0.00225 0.01754  0.00968  305 TYR B O   
853  C CB  . TYR A 116 ? 0.48383 0.31017 0.30663 -0.00346 0.05830  0.00402  305 TYR B CB  
854  C CG  . TYR A 116 ? 0.51215 0.34034 0.33460 -0.00506 0.08258  0.00202  305 TYR B CG  
855  C CD1 . TYR A 116 ? 0.54158 0.37528 0.36406 -0.00236 0.08892  -0.00390 305 TYR B CD1 
856  C CD2 . TYR A 116 ? 0.52832 0.35299 0.35184 -0.00921 0.09916  0.00659  305 TYR B CD2 
857  C CE1 . TYR A 116 ? 0.53680 0.37766 0.36481 -0.00254 0.11182  -0.00494 305 TYR B CE1 
858  C CE2 . TYR A 116 ? 0.57125 0.40250 0.40078 -0.01229 0.12174  0.00599  305 TYR B CE2 
859  C CZ  . TYR A 116 ? 0.58440 0.42631 0.41832 -0.00833 0.12833  0.00035  305 TYR B CZ  
860  O OH  . TYR A 116 ? 0.61431 0.46802 0.45980 -0.01011 0.15149  0.00049  305 TYR B OH  
861  N N   . GLU A 117 ? 0.47582 0.35243 0.36283 -0.00833 0.01572  0.00097  306 GLU B N   
862  C CA  . GLU A 117 ? 0.45488 0.33901 0.35269 -0.00933 -0.00526 0.00458  306 GLU B CA  
863  C C   . GLU A 117 ? 0.47879 0.33972 0.34693 -0.00945 -0.02139 0.00341  306 GLU B C   
864  O O   . GLU A 117 ? 0.53376 0.37282 0.37233 -0.00738 -0.01485 -0.00133 306 GLU B O   
865  C CB  . GLU A 117 ? 0.35227 0.26628 0.28767 -0.01389 -0.00697 0.00340  306 GLU B CB  
866  C CG  . GLU A 117 ? 0.34279 0.27681 0.30480 -0.01270 0.00291  0.00543  306 GLU B CG  
867  C CD  . GLU A 117 ? 0.33643 0.29673 0.33054 -0.01537 -0.00245 0.00712  306 GLU B CD  
868  O OE1 . GLU A 117 ? 0.31817 0.28232 0.31632 -0.02021 -0.01227 0.00654  306 GLU B OE1 
869  O OE2 . GLU A 117 ? 0.29532 0.26963 0.30797 -0.01251 0.00377  0.00931  306 GLU B OE2 
870  N N   . CYS A 118 ? 0.51820 0.38368 0.39447 -0.01155 -0.04306 0.00787  307 CYS B N   
871  C CA  . CYS A 118 ? 0.53615 0.37976 0.38720 -0.01419 -0.06335 0.00656  307 CYS B CA  
872  C C   . CYS A 118 ? 0.53872 0.38953 0.40164 -0.02111 -0.06628 0.00173  307 CYS B C   
873  O O   . CYS A 118 ? 0.36742 0.24418 0.26227 -0.02386 -0.05551 0.00089  307 CYS B O   
874  C CB  . CYS A 118 ? 0.50900 0.35836 0.37014 -0.01557 -0.08791 0.01375  307 CYS B CB  
875  S SG  . CYS A 118 ? 0.50791 0.33587 0.34098 -0.00527 -0.09047 0.01951  307 CYS B SG  
876  N N   . ASN A 119 ? 0.56636 0.38907 0.39843 -0.02350 -0.08193 -0.00159 308 ASN B N   
877  C CA  . ASN A 119 ? 0.56771 0.38760 0.40212 -0.02947 -0.08608 -0.00639 308 ASN B CA  
878  C C   . ASN A 119 ? 0.53226 0.33849 0.35936 -0.03894 -0.11566 -0.00456 308 ASN B C   
879  O O   . ASN A 119 ? 0.52746 0.33448 0.35637 -0.04103 -0.13359 0.00106  308 ASN B O   
880  C CB  . ASN A 119 ? 0.60423 0.39619 0.40174 -0.02149 -0.07068 -0.01481 308 ASN B CB  
881  C CG  . ASN A 119 ? 0.67269 0.42449 0.41738 -0.01377 -0.07290 -0.01677 308 ASN B CG  
882  O OD1 . ASN A 119 ? 0.74404 0.46542 0.45696 -0.01611 -0.09456 -0.01810 308 ASN B OD1 
883  N ND2 . ASN A 119 ? 0.68348 0.43268 0.41641 -0.00522 -0.05071 -0.01669 308 ASN B ND2 
884  N N   . SER A 120 ? 0.56464 0.35730 0.38370 -0.04495 -0.12230 -0.00902 309 SER B N   
885  C CA  . SER A 120 ? 0.57722 0.35554 0.39129 -0.05727 -0.15151 -0.00729 309 SER B CA  
886  C C   . SER A 120 ? 0.62027 0.35169 0.37958 -0.05420 -0.17004 -0.01111 309 SER B C   
887  O O   . SER A 120 ? 0.66642 0.38585 0.42178 -0.06531 -0.19911 -0.00878 309 SER B O   
888  C CB  . SER A 120 ? 0.55904 0.32972 0.37486 -0.06455 -0.15241 -0.01105 309 SER B CB  
889  O OG  . SER A 120 ? 0.67243 0.41143 0.44797 -0.05304 -0.13784 -0.02056 309 SER B OG  
890  N N   . PHE A 121 ? 0.60702 0.31088 0.32348 -0.04007 -0.15435 -0.01651 310 PHE B N   
891  C CA  . PHE A 121 ? 0.71965 0.37414 0.37622 -0.03493 -0.16943 -0.02012 310 PHE B CA  
892  C C   . PHE A 121 ? 0.79209 0.45020 0.44648 -0.03213 -0.17941 -0.01329 310 PHE B C   
893  O O   . PHE A 121 ? 0.78605 0.40408 0.39312 -0.03010 -0.19954 -0.01469 310 PHE B O   
894  C CB  . PHE A 121 ? 0.79064 0.41059 0.39762 -0.01973 -0.14535 -0.02852 310 PHE B CB  
895  C CG  . PHE A 121 ? 0.79253 0.39356 0.38505 -0.01914 -0.14182 -0.03651 310 PHE B CG  
896  C CD1 . PHE A 121 ? 0.87447 0.50979 0.50972 -0.02069 -0.12499 -0.03670 310 PHE B CD1 
897  C CD2 . PHE A 121 ? 0.84028 0.40010 0.39260 -0.01404 -0.14938 -0.03857 310 PHE B CD2 
898  C CE1 . PHE A 121 ? 0.84330 0.45907 0.46363 -0.01842 -0.12258 -0.04361 310 PHE B CE1 
899  C CE2 . PHE A 121 ? 0.85862 0.40567 0.40419 -0.01086 -0.14361 -0.04273 310 PHE B CE2 
900  C CZ  . PHE A 121 ? 0.83097 0.40550 0.40934 -0.01285 -0.13087 -0.04551 310 PHE B CZ  
901  N N   . CYS A 122 ? 0.73301 0.43414 0.43342 -0.03098 -0.16700 -0.00618 311 CYS B N   
902  C CA  . CYS A 122 ? 0.78970 0.49489 0.49082 -0.02715 -0.17774 0.00105  311 CYS B CA  
903  C C   . CYS A 122 ? 0.79866 0.51291 0.51999 -0.03825 -0.21426 0.00655  311 CYS B C   
904  O O   . CYS A 122 ? 0.75506 0.49070 0.51159 -0.05119 -0.22541 0.00765  311 CYS B O   
905  C CB  . CYS A 122 ? 0.71724 0.46450 0.46330 -0.02278 -0.15595 0.00694  311 CYS B CB  
906  S SG  . CYS A 122 ? 0.62820 0.37324 0.36263 -0.01292 -0.11497 0.00226  311 CYS B SG  
907  N N   . SER A 123 ? 0.97458 0.67257 0.67413 -0.03345 -0.23345 0.01083  312 SER B N   
908  C CA  . SER A 123 ? 0.90330 0.62120 0.63591 -0.04209 -0.26518 0.01804  312 SER B CA  
909  C C   . SER A 123 ? 0.89245 0.66624 0.68814 -0.04040 -0.25956 0.02775  312 SER B C   
910  O O   . SER A 123 ? 1.03089 0.81265 0.83300 -0.03227 -0.26904 0.03454  312 SER B O   
911  C CB  . SER A 123 ? 0.90600 0.58651 0.59786 -0.03539 -0.28028 0.01795  312 SER B CB  
912  O OG  . SER A 123 ? 1.01101 0.67659 0.67204 -0.02045 -0.26800 0.01992  312 SER B OG  
913  N N   . CYS A 124 ? 0.80264 0.61411 0.64514 -0.04641 -0.24047 0.02819  313 CYS B N   
914  C CA  . CYS A 124 ? 0.72222 0.58436 0.62226 -0.04264 -0.22540 0.03574  313 CYS B CA  
915  C C   . CYS A 124 ? 0.83216 0.73716 0.79078 -0.05671 -0.23216 0.04090  313 CYS B C   
916  O O   . CYS A 124 ? 0.96274 0.85852 0.91748 -0.06919 -0.23624 0.03686  313 CYS B O   
917  C CB  . CYS A 124 ? 0.77334 0.63859 0.66985 -0.03369 -0.18825 0.03157  313 CYS B CB  
918  S SG  . CYS A 124 ? 0.83398 0.66959 0.68703 -0.01693 -0.17377 0.03124  313 CYS B SG  
919  N N   . SER A 125 ? 0.76683 0.71731 0.77846 -0.05378 -0.23203 0.05043  314 SER B N   
920  C CA  . SER A 125 ? 0.71186 0.70846 0.78286 -0.06470 -0.22892 0.05680  314 SER B CA  
921  C C   . SER A 125 ? 0.69301 0.70354 0.77517 -0.06014 -0.19378 0.05364  314 SER B C   
922  O O   . SER A 125 ? 0.70564 0.69565 0.75700 -0.04895 -0.17369 0.04735  314 SER B O   
923  C CB  . SER A 125 ? 0.69325 0.73498 0.81798 -0.06144 -0.24160 0.06886  314 SER B CB  
924  O OG  . SER A 125 ? 0.79358 0.86356 0.94439 -0.04714 -0.21490 0.07216  314 SER B OG  
925  N N   . MET A 126 ? 0.69985 0.74521 0.82652 -0.06975 -0.18693 0.05863  315 MET B N   
926  C CA  . MET A 126 ? 0.71613 0.77289 0.85149 -0.06603 -0.15651 0.05579  315 MET B CA  
927  C C   . MET A 126 ? 0.74416 0.82510 0.90024 -0.05010 -0.13721 0.05939  315 MET B C   
928  O O   . MET A 126 ? 0.68607 0.76957 0.84085 -0.04495 -0.11281 0.05562  315 MET B O   
929  C CB  . MET A 126 ? 0.71514 0.79609 0.88514 -0.08114 -0.15487 0.06065  315 MET B CB  
930  C CG  . MET A 126 ? 0.75088 0.82937 0.91456 -0.07962 -0.12848 0.05551  315 MET B CG  
931  S SD  . MET A 126 ? 0.81820 0.85266 0.92461 -0.06854 -0.11539 0.04160  315 MET B SD  
932  C CE  . MET A 126 ? 0.62646 0.62179 0.69678 -0.08135 -0.13319 0.03514  315 MET B CE  
933  N N   . GLU A 127 ? 0.80687 0.90272 0.97958 -0.04147 -0.14879 0.06626  316 GLU B N   
934  C CA  . GLU A 127 ? 0.88856 1.00100 1.07554 -0.02423 -0.13207 0.06943  316 GLU B CA  
935  C C   . GLU A 127 ? 0.89149 0.96958 1.03620 -0.01141 -0.13394 0.06540  316 GLU B C   
936  O O   . GLU A 127 ? 0.81438 0.90131 0.96866 0.00284  -0.13335 0.07043  316 GLU B O   
937  C CB  . GLU A 127 ? 0.94244 1.10134 1.18473 -0.02057 -0.13986 0.08164  316 GLU B CB  
938  C CG  . GLU A 127 ? 0.90070 1.09757 1.18781 -0.03026 -0.12824 0.08743  316 GLU B CG  
939  C CD  . GLU A 127 ? 0.91355 1.09792 1.19191 -0.05156 -0.13706 0.08440  316 GLU B CD  
940  O OE1 . GLU A 127 ? 0.88303 1.07617 1.17898 -0.06517 -0.16186 0.08975  316 GLU B OE1 
941  O OE2 . GLU A 127 ? 0.90182 1.06578 1.15480 -0.05456 -0.12043 0.07660  316 GLU B OE2 
942  N N   . CYS A 128 ? 0.65895 0.69641 0.75559 -0.01560 -0.13527 0.05693  317 CYS B N   
943  C CA  . CYS A 128 ? 0.56708 0.56940 0.62013 -0.00467 -0.13097 0.05339  317 CYS B CA  
944  C C   . CYS A 128 ? 0.52525 0.52972 0.57915 0.00465  -0.10296 0.05098  317 CYS B C   
945  O O   . CYS A 128 ? 0.49654 0.51330 0.56393 -0.00001 -0.08584 0.04718  317 CYS B O   
946  C CB  . CYS A 128 ? 0.60399 0.56465 0.60695 -0.01108 -0.13429 0.04514  317 CYS B CB  
947  S SG  . CYS A 128 ? 0.43032 0.34789 0.37863 -0.00057 -0.11740 0.04011  317 CYS B SG  
948  N N   . PRO A 129 ? 0.49496 0.48470 0.53246 0.01751  -0.09916 0.05317  318 PRO B N   
949  C CA  . PRO A 129 ? 0.45722 0.44457 0.49334 0.02494  -0.07450 0.05067  318 PRO B CA  
950  C C   . PRO A 129 ? 0.42631 0.39322 0.43712 0.01757  -0.05663 0.04173  318 PRO B C   
951  O O   . PRO A 129 ? 0.32189 0.29276 0.33915 0.01939  -0.03779 0.03867  318 PRO B O   
952  C CB  . PRO A 129 ? 0.46525 0.43033 0.47891 0.03845  -0.07841 0.05506  318 PRO B CB  
953  C CG  . PRO A 129 ? 0.49437 0.46890 0.51861 0.04143  -0.10570 0.06224  318 PRO B CG  
954  C CD  . PRO A 129 ? 0.51865 0.49405 0.54069 0.02624  -0.11918 0.05899  318 PRO B CD  
955  N N   . ASN A 130 ? 0.42708 0.37196 0.40920 0.01007  -0.06244 0.03739  319 ASN B N   
956  C CA  . ASN A 130 ? 0.43403 0.36258 0.39506 0.00463  -0.04557 0.02950  319 ASN B CA  
957  C C   . ASN A 130 ? 0.39426 0.33955 0.37321 -0.00476 -0.04382 0.02484  319 ASN B C   
958  O O   . ASN A 130 ? 0.40381 0.33379 0.36258 -0.00902 -0.03752 0.01857  319 ASN B O   
959  C CB  . ASN A 130 ? 0.45209 0.34306 0.36633 0.00522  -0.04845 0.02757  319 ASN B CB  
960  C CG  . ASN A 130 ? 0.43356 0.30822 0.32768 0.00407  -0.02548 0.02235  319 ASN B CG  
961  O OD1 . ASN A 130 ? 0.41583 0.30135 0.32639 0.00432  -0.00993 0.02146  319 ASN B OD1 
962  N ND2 . ASN A 130 ? 0.45616 0.30438 0.31458 0.00288  -0.02336 0.01901  319 ASN B ND2 
963  N N   . ARG A 131 ? 0.35087 0.32672 0.36679 -0.00715 -0.04845 0.02847  320 ARG B N   
964  C CA  . ARG A 131 ? 0.39258 0.38265 0.42484 -0.01618 -0.04686 0.02556  320 ARG B CA  
965  C C   . ARG A 131 ? 0.31576 0.33250 0.37908 -0.01462 -0.03313 0.02692  320 ARG B C   
966  O O   . ARG A 131 ? 0.29513 0.33158 0.38170 -0.02074 -0.03549 0.02935  320 ARG B O   
967  C CB  . ARG A 131 ? 0.44484 0.44135 0.48703 -0.02424 -0.06869 0.02967  320 ARG B CB  
968  C CG  . ARG A 131 ? 0.49845 0.46222 0.50282 -0.02694 -0.08402 0.02649  320 ARG B CG  
969  C CD  . ARG A 131 ? 0.62495 0.59453 0.64134 -0.03692 -0.10885 0.03071  320 ARG B CD  
970  N NE  . ARG A 131 ? 0.59569 0.52835 0.57004 -0.03895 -0.12613 0.02702  320 ARG B NE  
971  C CZ  . ARG A 131 ? 0.49463 0.40220 0.44220 -0.04504 -0.12930 0.02029  320 ARG B CZ  
972  N NH1 . ARG A 131 ? 0.51084 0.42686 0.47046 -0.05000 -0.11739 0.01684  320 ARG B NH1 
973  N NH2 . ARG A 131 ? 0.53837 0.40824 0.44249 -0.04484 -0.14515 0.01683  320 ARG B NH2 
974  N N   . VAL A 132 ? 0.28200 0.29612 0.34266 -0.00676 -0.01869 0.02555  321 VAL B N   
975  C CA  . VAL A 132 ? 0.29618 0.32953 0.37912 -0.00333 -0.00598 0.02620  321 VAL B CA  
976  C C   . VAL A 132 ? 0.26698 0.30379 0.35201 -0.01074 0.00128  0.02073  321 VAL B C   
977  O O   . VAL A 132 ? 0.24005 0.29580 0.34551 -0.01243 0.00428  0.02345  321 VAL B O   
978  C CB  . VAL A 132 ? 0.27010 0.29100 0.34199 0.00572  0.00603  0.02446  321 VAL B CB  
979  C CG1 . VAL A 132 ? 0.25456 0.28865 0.34183 0.01007  0.01874  0.02367  321 VAL B CG1 
980  C CG2 . VAL A 132 ? 0.30566 0.32105 0.37405 0.01499  -0.00197 0.03075  321 VAL B CG2 
981  N N   . VAL A 133 ? 0.23687 0.25538 0.30051 -0.01435 0.00484  0.01358  322 VAL B N   
982  C CA  . VAL A 133 ? 0.28602 0.30648 0.35058 -0.01951 0.00993  0.00825  322 VAL B CA  
983  C C   . VAL A 133 ? 0.30347 0.32988 0.37504 -0.02670 -0.00112 0.01085  322 VAL B C   
984  O O   . VAL A 133 ? 0.21606 0.25201 0.29832 -0.03009 0.00175  0.01105  322 VAL B O   
985  C CB  . VAL A 133 ? 0.26963 0.27259 0.31380 -0.02022 0.01609  0.00088  322 VAL B CB  
986  C CG1 . VAL A 133 ? 0.24442 0.24978 0.29025 -0.02371 0.01848  -0.00437 322 VAL B CG1 
987  C CG2 . VAL A 133 ? 0.21943 0.21696 0.25992 -0.01641 0.02719  -0.00098 322 VAL B CG2 
988  N N   . GLN A 134 ? 0.30256 0.31997 0.36523 -0.02965 -0.01486 0.01312  323 GLN B N   
989  C CA  . GLN A 134 ? 0.33268 0.35020 0.39873 -0.03859 -0.02797 0.01530  323 GLN B CA  
990  C C   . GLN A 134 ? 0.34621 0.39085 0.44507 -0.04284 -0.03008 0.02388  323 GLN B C   
991  O O   . GLN A 134 ? 0.35133 0.40004 0.45794 -0.05106 -0.03244 0.02562  323 GLN B O   
992  C CB  . GLN A 134 ? 0.29348 0.29220 0.33990 -0.04071 -0.04456 0.01572  323 GLN B CB  
993  C CG  . GLN A 134 ? 0.37942 0.35359 0.40069 -0.04603 -0.05230 0.01014  323 GLN B CG  
994  C CD  . GLN A 134 ? 0.51429 0.46687 0.51339 -0.04879 -0.07176 0.01090  323 GLN B CD  
995  O OE1 . GLN A 134 ? 0.43193 0.38454 0.42885 -0.04475 -0.07781 0.01449  323 GLN B OE1 
996  N NE2 . GLN A 134 ? 0.54570 0.47613 0.52492 -0.05510 -0.08298 0.00737  323 GLN B NE2 
997  N N   . ARG A 135 ? 0.26204 0.32492 0.38025 -0.03671 -0.02825 0.03001  324 ARG B N   
998  C CA  . ARG A 135 ? 0.35119 0.44409 0.50422 -0.03887 -0.02707 0.03927  324 ARG B CA  
999  C C   . ARG A 135 ? 0.28903 0.38982 0.44797 -0.03799 -0.01004 0.03833  324 ARG B C   
1000 O O   . ARG A 135 ? 0.28784 0.40698 0.46843 -0.04402 -0.00804 0.04535  324 ARG B O   
1001 C CB  . ARG A 135 ? 0.33987 0.45006 0.51128 -0.02851 -0.02701 0.04556  324 ARG B CB  
1002 C CG  . ARG A 135 ? 0.35322 0.46249 0.52705 -0.03078 -0.04832 0.04988  324 ARG B CG  
1003 C CD  . ARG A 135 ? 0.43116 0.56131 0.62806 -0.01887 -0.04943 0.05745  324 ARG B CD  
1004 N NE  . ARG A 135 ? 0.42515 0.53459 0.59686 -0.00574 -0.04191 0.05277  324 ARG B NE  
1005 C CZ  . ARG A 135 ? 0.43840 0.52339 0.58332 -0.00312 -0.05339 0.05065  324 ARG B CZ  
1006 N NH1 . ARG A 135 ? 0.42026 0.49603 0.55640 -0.01152 -0.07398 0.05153  324 ARG B NH1 
1007 N NH2 . ARG A 135 ? 0.42368 0.48947 0.54672 0.00779  -0.04420 0.04771  324 ARG B NH2 
1008 N N   . GLY A 136 ? 0.26711 0.35359 0.40663 -0.03126 0.00179  0.03033  325 GLY B N   
1009 C CA  . GLY A 136 ? 0.28810 0.37498 0.42520 -0.03070 0.01430  0.02776  325 GLY B CA  
1010 C C   . GLY A 136 ? 0.29970 0.39736 0.44498 -0.02028 0.02875  0.02970  325 GLY B C   
1011 O O   . GLY A 136 ? 0.26993 0.37127 0.41961 -0.01149 0.03083  0.03131  325 GLY B O   
1012 N N   . ARG A 137 ? 0.36838 0.46724 0.51156 -0.02026 0.03868  0.02948  326 ARG B N   
1013 C CA  . ARG A 137 ? 0.34916 0.45052 0.49068 -0.00941 0.05335  0.02949  326 ARG B CA  
1014 C C   . ARG A 137 ? 0.38872 0.51514 0.55656 -0.00308 0.05947  0.04004  326 ARG B C   
1015 O O   . ARG A 137 ? 0.30532 0.45217 0.49690 -0.01049 0.05556  0.04912  326 ARG B O   
1016 C CB  . ARG A 137 ? 0.30358 0.39670 0.43159 -0.01102 0.06089  0.02711  326 ARG B CB  
1017 C CG  . ARG A 137 ? 0.30720 0.39596 0.42487 0.00051  0.07558  0.02597  326 ARG B CG  
1018 C CD  . ARG A 137 ? 0.31935 0.39230 0.41512 -0.00126 0.07885  0.02158  326 ARG B CD  
1019 N NE  . ARG A 137 ? 0.35166 0.43138 0.45421 -0.01092 0.07690  0.02833  326 ARG B NE  
1020 C CZ  . ARG A 137 ? 0.31305 0.40179 0.42037 -0.01051 0.08840  0.03730  326 ARG B CZ  
1021 N NH1 . ARG A 137 ? 0.28408 0.37666 0.38885 0.00118  0.10396  0.04014  326 ARG B NH1 
1022 N NH2 . ARG A 137 ? 0.28741 0.37915 0.40019 -0.02180 0.08522  0.04390  326 ARG B NH2 
1023 N N   . THR A 138 ? 0.41554 0.54023 0.58018 0.01082  0.06879  0.03906  327 THR B N   
1024 C CA  . THR A 138 ? 0.35856 0.50712 0.54735 0.02158  0.07810  0.04856  327 THR B CA  
1025 C C   . THR A 138 ? 0.34344 0.48519 0.51870 0.03503  0.09719  0.04722  327 THR B C   
1026 O O   . THR A 138 ? 0.30438 0.46711 0.49928 0.04594  0.10910  0.05563  327 THR B O   
1027 C CB  . THR A 138 ? 0.41660 0.56848 0.61409 0.03021  0.07061  0.05019  327 THR B CB  
1028 O OG1 . THR A 138 ? 0.36165 0.49103 0.53554 0.04382  0.07913  0.04355  327 THR B OG1 
1029 C CG2 . THR A 138 ? 0.40300 0.54403 0.59369 0.01913  0.05194  0.04676  327 THR B CG2 
1030 N N   . LEU A 139 ? 0.34792 0.46084 0.49012 0.03523  0.10004  0.03698  328 LEU B N   
1031 C CA  . LEU A 139 ? 0.35879 0.45700 0.47939 0.04795  0.11563  0.03397  328 LEU B CA  
1032 C C   . LEU A 139 ? 0.38144 0.47937 0.49357 0.04273  0.12333  0.03612  328 LEU B C   
1033 O O   . LEU A 139 ? 0.30966 0.39639 0.41035 0.03051  0.11365  0.03131  328 LEU B O   
1034 C CB  . LEU A 139 ? 0.34576 0.40955 0.43359 0.05065  0.11150  0.02140  328 LEU B CB  
1035 C CG  . LEU A 139 ? 0.43033 0.48154 0.51056 0.06471  0.11485  0.01935  328 LEU B CG  
1036 C CD1 . LEU A 139 ? 0.45199 0.52288 0.55905 0.06540  0.10711  0.02621  328 LEU B CD1 
1037 C CD2 . LEU A 139 ? 0.48465 0.50088 0.53415 0.06147  0.10842  0.00736  328 LEU B CD2 
1038 N N   . PRO A 140 ? 0.34894 0.45789 0.46508 0.05245  0.14123  0.04376  329 PRO B N   
1039 C CA  . PRO A 140 ? 0.36998 0.47028 0.46798 0.04884  0.15007  0.04543  329 PRO B CA  
1040 C C   . PRO A 140 ? 0.33720 0.39816 0.38963 0.05357  0.14877  0.03267  329 PRO B C   
1041 O O   . PRO A 140 ? 0.40944 0.45165 0.44153 0.06702  0.15415  0.02649  329 PRO B O   
1042 C CB  . PRO A 140 ? 0.39941 0.51403 0.50572 0.05751  0.16263  0.05378  329 PRO B CB  
1043 C CG  . PRO A 140 ? 0.38239 0.49960 0.49521 0.07192  0.16357  0.05207  329 PRO B CG  
1044 C CD  . PRO A 140 ? 0.35183 0.47576 0.48251 0.06564  0.14860  0.04958  329 PRO B CD  
1045 N N   . LEU A 141 ? 0.31088 0.35778 0.34681 0.04242  0.13971  0.02865  330 LEU B N   
1046 C CA  . LEU A 141 ? 0.34424 0.35656 0.34125 0.04415  0.13301  0.01646  330 LEU B CA  
1047 C C   . LEU A 141 ? 0.37433 0.37101 0.34301 0.04660  0.14210  0.01896  330 LEU B C   
1048 O O   . LEU A 141 ? 0.43873 0.45155 0.41988 0.04265  0.15164  0.03024  330 LEU B O   
1049 C CB  . LEU A 141 ? 0.34159 0.34896 0.34172 0.03110  0.11245  0.00854  330 LEU B CB  
1050 C CG  . LEU A 141 ? 0.35352 0.37242 0.37655 0.02732  0.10338  0.00634  330 LEU B CG  
1051 C CD1 . LEU A 141 ? 0.32330 0.33666 0.34653 0.01604  0.08693  -0.00098 330 LEU B CD1 
1052 C CD2 . LEU A 141 ? 0.30211 0.30729 0.31399 0.03824  0.10765  0.00117  330 LEU B CD2 
1053 N N   . GLU A 142 ? 0.36756 0.33051 0.29628 0.05238  0.13824  0.00869  331 GLU B N   
1054 C CA  . GLU A 142 ? 0.39762 0.33738 0.28922 0.05694  0.14537  0.00967  331 GLU B CA  
1055 C C   . GLU A 142 ? 0.46544 0.37768 0.32942 0.05150  0.12493  -0.00201 331 GLU B C   
1056 O O   . GLU A 142 ? 0.42815 0.32368 0.28047 0.05308  0.11357  -0.01335 331 GLU B O   
1057 C CB  . GLU A 142 ? 0.44119 0.36269 0.30337 0.07508  0.16469  0.00980  331 GLU B CB  
1058 C CG  . GLU A 142 ? 0.50688 0.39984 0.32350 0.08157  0.17420  0.01136  331 GLU B CG  
1059 C CD  . GLU A 142 ? 0.61714 0.49941 0.41728 0.09647  0.18778  0.01403  331 GLU B CD  
1060 O OE1 . GLU A 142 ? 0.62650 0.53584 0.45348 0.09856  0.20273  0.02641  331 GLU B OE1 
1061 O OE2 . GLU A 142 ? 0.71307 0.55934 0.47419 0.10525  0.18177  0.00365  331 GLU B OE2 
1062 N N   . ILE A 143 ? 0.46612 0.37349 0.32059 0.04499  0.11974  0.00131  332 ILE B N   
1063 C CA  . ILE A 143 ? 0.47790 0.36062 0.30645 0.04191  0.10002  -0.00837 332 ILE B CA  
1064 C C   . ILE A 143 ? 0.50805 0.35353 0.28380 0.05330  0.10511  -0.01148 332 ILE B C   
1065 O O   . ILE A 143 ? 0.55845 0.39756 0.31540 0.05912  0.12319  -0.00193 332 ILE B O   
1066 C CB  . ILE A 143 ? 0.44002 0.33118 0.28000 0.03168  0.09075  -0.00336 332 ILE B CB  
1067 C CG1 . ILE A 143 ? 0.39526 0.31877 0.28175 0.02149  0.08672  -0.00023 332 ILE B CG1 
1068 C CG2 . ILE A 143 ? 0.39664 0.26572 0.21410 0.03074  0.06899  -0.01330 332 ILE B CG2 
1069 C CD1 . ILE A 143 ? 0.38488 0.31362 0.28069 0.01222  0.07950  0.00543  332 ILE B CD1 
1070 N N   . PHE A 144 ? 0.50673 0.32630 0.25731 0.05593  0.08917  -0.02448 333 PHE B N   
1071 C CA  . PHE A 144 ? 0.58685 0.36465 0.28114 0.06708  0.09027  -0.02956 333 PHE B CA  
1072 C C   . PHE A 144 ? 0.55078 0.30575 0.22495 0.06258  0.06158  -0.04161 333 PHE B C   
1073 O O   . PHE A 144 ? 0.49331 0.26607 0.20001 0.05243  0.04367  -0.04755 333 PHE B O   
1074 C CB  . PHE A 144 ? 0.65920 0.42181 0.33621 0.07886  0.10342  -0.03360 333 PHE B CB  
1075 C CG  . PHE A 144 ? 0.53451 0.29067 0.21979 0.07430  0.08568  -0.04613 333 PHE B CG  
1076 C CD1 . PHE A 144 ? 0.48895 0.27845 0.22414 0.06480  0.08205  -0.04536 333 PHE B CD1 
1077 C CD2 . PHE A 144 ? 0.57017 0.28416 0.21089 0.07869  0.07232  -0.05829 333 PHE B CD2 
1078 C CE1 . PHE A 144 ? 0.50810 0.29041 0.25012 0.05933  0.06770  -0.05543 333 PHE B CE1 
1079 C CE2 . PHE A 144 ? 0.62683 0.33411 0.27668 0.07186  0.05589  -0.06886 333 PHE B CE2 
1080 C CZ  . PHE A 144 ? 0.54191 0.28408 0.24322 0.06196  0.05477  -0.06689 333 PHE B CZ  
1081 N N   . LYS A 145 ? 0.57868 0.29425 0.19862 0.07073  0.05751  -0.04468 334 LYS B N   
1082 C CA  . LYS A 145 ? 0.70099 0.39166 0.29732 0.06798  0.02807  -0.05614 334 LYS B CA  
1083 C C   . LYS A 145 ? 0.69761 0.36433 0.27561 0.06981  0.01788  -0.06891 334 LYS B C   
1084 O O   . LYS A 145 ? 0.65419 0.30497 0.21171 0.07889  0.03296  -0.06643 334 LYS B O   
1085 C CB  . LYS A 145 ? 0.70901 0.36325 0.25000 0.07613  0.02557  -0.05362 334 LYS B CB  
1086 C CG  . LYS A 145 ? 0.74980 0.38869 0.27847 0.07217  -0.00807 -0.06212 334 LYS B CG  
1087 C CD  . LYS A 145 ? 0.73942 0.40633 0.30277 0.06495  -0.01643 -0.05616 334 LYS B CD  
1088 C CE  . LYS A 145 ? 0.73909 0.39960 0.30228 0.06196  -0.05115 -0.06549 334 LYS B CE  
1089 N NZ  . LYS A 145 ? 0.81715 0.52055 0.44407 0.05099  -0.06297 -0.06925 334 LYS B NZ  
1090 N N   . THR A 146 ? 0.77613 0.44963 0.37613 0.05901  -0.00834 -0.07856 335 THR B N   
1091 C CA  . THR A 146 ? 0.71011 0.36618 0.30364 0.05572  -0.02153 -0.08846 335 THR B CA  
1092 C C   . THR A 146 ? 0.70897 0.33683 0.27165 0.05577  -0.04577 -0.09283 335 THR B C   
1093 O O   . THR A 146 ? 0.72607 0.34628 0.27115 0.05906  -0.05394 -0.08970 335 THR B O   
1094 C CB  . THR A 146 ? 0.64893 0.33422 0.29301 0.04145  -0.03335 -0.09411 335 THR B CB  
1095 O OG1 . THR A 146 ? 0.58898 0.29238 0.25734 0.03245  -0.05669 -0.09638 335 THR B OG1 
1096 C CG2 . THR A 146 ? 0.54408 0.26895 0.23305 0.04001  -0.01048 -0.08409 335 THR B CG2 
1097 N N   . LYS A 147 ? 0.77481 0.38513 0.32990 0.05214  -0.05763 -0.09958 336 LYS B N   
1098 C CA  . LYS A 147 ? 0.87302 0.45464 0.39924 0.05154  -0.08170 -0.10406 336 LYS B CA  
1099 C C   . LYS A 147 ? 0.78176 0.38090 0.33316 0.04155  -0.11021 -0.10794 336 LYS B C   
1100 O O   . LYS A 147 ? 0.80875 0.39517 0.33785 0.04719  -0.12083 -0.10538 336 LYS B O   
1101 C CB  . LYS A 147 ? 0.85716 0.41935 0.37648 0.04671  -0.08991 -0.11077 336 LYS B CB  
1102 C CG  . LYS A 147 ? 0.87558 0.40539 0.35371 0.06035  -0.06965 -0.10768 336 LYS B CG  
1103 C CD  . LYS A 147 ? 0.92176 0.40642 0.34938 0.06613  -0.08486 -0.11019 336 LYS B CD  
1104 C CE  . LYS A 147 ? 0.92203 0.39552 0.35632 0.05287  -0.11156 -0.11942 336 LYS B CE  
1105 N NZ  . LYS A 147 ? 0.99404 0.43437 0.39217 0.05404  -0.13626 -0.12239 336 LYS B NZ  
1106 N N   . GLU A 148 ? 0.82663 0.45589 0.42638 0.02738  -0.12172 -0.11322 337 GLU B N   
1107 C CA  . GLU A 148 ? 0.87087 0.52065 0.50222 0.01725  -0.14974 -0.11709 337 GLU B CA  
1108 C C   . GLU A 148 ? 0.76058 0.45295 0.44049 0.01202  -0.14839 -0.11549 337 GLU B C   
1109 O O   . GLU A 148 ? 0.89410 0.60606 0.59843 0.00881  -0.16827 -0.11622 337 GLU B O   
1110 C CB  . GLU A 148 ? 0.95173 0.60188 0.60235 0.00338  -0.16738 -0.12402 337 GLU B CB  
1111 C CG  . GLU A 148 ? 0.96440 0.56959 0.56670 0.00816  -0.16689 -0.12631 337 GLU B CG  
1112 C CD  . GLU A 148 ? 1.06789 0.67220 0.68867 -0.00568 -0.17347 -0.13187 337 GLU B CD  
1113 O OE1 . GLU A 148 ? 1.22610 0.84486 0.87612 -0.01947 -0.19672 -0.13583 337 GLU B OE1 
1114 O OE2 . GLU A 148 ? 1.13314 0.72289 0.74036 -0.00257 -0.15479 -0.13156 337 GLU B OE2 
1115 N N   . LYS A 149 ? 0.79662 0.50306 0.49114 0.01226  -0.12594 -0.11312 338 LYS B N   
1116 C CA  . LYS A 149 ? 0.77680 0.52244 0.51485 0.00960  -0.12037 -0.10884 338 LYS B CA  
1117 C C   . LYS A 149 ? 0.74657 0.48730 0.46153 0.02184  -0.10597 -0.09966 338 LYS B C   
1118 O O   . LYS A 149 ? 0.81617 0.51908 0.47674 0.03192  -0.10374 -0.09937 338 LYS B O   
1119 C CB  . LYS A 149 ? 0.64761 0.42027 0.42484 0.00264  -0.10025 -0.10526 338 LYS B CB  
1120 C CG  . LYS A 149 ? 0.63221 0.40691 0.43078 -0.01100 -0.11248 -0.11287 338 LYS B CG  
1121 C CD  . LYS A 149 ? 0.64296 0.38811 0.41341 -0.00934 -0.09863 -0.11495 338 LYS B CD  
1122 C CE  . LYS A 149 ? 0.51904 0.28398 0.30645 -0.00406 -0.06911 -0.10551 338 LYS B CE  
1123 N NZ  . LYS A 149 ? 0.53280 0.27246 0.29885 -0.00118 -0.05625 -0.10722 338 LYS B NZ  
1124 N N   . GLY A 150 ? 0.62394 0.40005 0.37741 0.02068  -0.09562 -0.09178 339 GLY B N   
1125 C CA  . GLY A 150 ? 0.71514 0.48682 0.45031 0.02930  -0.08124 -0.08201 339 GLY B CA  
1126 C C   . GLY A 150 ? 0.67195 0.44321 0.40078 0.03220  -0.05147 -0.07456 339 GLY B C   
1127 O O   . GLY A 150 ? 0.65410 0.40452 0.35899 0.03507  -0.04372 -0.07791 339 GLY B O   
1128 N N   . TRP A 151 ? 0.56578 0.35907 0.31583 0.03194  -0.03557 -0.06444 340 TRP B N   
1129 C CA  . TRP A 151 ? 0.59321 0.39484 0.34862 0.03342  -0.00908 -0.05642 340 TRP B CA  
1130 C C   . TRP A 151 ? 0.53374 0.35747 0.32500 0.02710  -0.00434 -0.05949 340 TRP B C   
1131 O O   . TRP A 151 ? 0.42507 0.26497 0.24548 0.01937  -0.01831 -0.06549 340 TRP B O   
1132 C CB  . TRP A 151 ? 0.61692 0.43575 0.38731 0.03223  0.00299  -0.04467 340 TRP B CB  
1133 C CG  . TRP A 151 ? 0.62062 0.41378 0.35195 0.03816  0.00166  -0.03956 340 TRP B CG  
1134 C CD1 . TRP A 151 ? 0.59533 0.38032 0.31863 0.03886  -0.01716 -0.04110 340 TRP B CD1 
1135 C CD2 . TRP A 151 ? 0.61864 0.38954 0.31199 0.04519  0.02083  -0.03131 340 TRP B CD2 
1136 N NE1 . TRP A 151 ? 0.60394 0.35954 0.28333 0.04523  -0.01198 -0.03423 340 TRP B NE1 
1137 C CE2 . TRP A 151 ? 0.58858 0.33552 0.24897 0.04862  0.01243  -0.02786 340 TRP B CE2 
1138 C CE3 . TRP A 151 ? 0.56750 0.33685 0.25189 0.05004  0.04541  -0.02586 340 TRP B CE3 
1139 C CZ2 . TRP A 151 ? 0.61166 0.33164 0.22843 0.05517  0.02891  -0.01871 340 TRP B CZ2 
1140 C CZ3 . TRP A 151 ? 0.61489 0.36149 0.25994 0.05743  0.06281  -0.01691 340 TRP B CZ3 
1141 C CH2 . TRP A 151 ? 0.66895 0.39040 0.27963 0.05916  0.05508  -0.01318 340 TRP B CH2 
1142 N N   . GLY A 152 ? 0.52220 0.34642 0.31091 0.03121  0.01643  -0.05456 341 GLY B N   
1143 C CA  . GLY A 152 ? 0.42715 0.26772 0.24415 0.02720  0.02231  -0.05607 341 GLY B CA  
1144 C C   . GLY A 152 ? 0.44081 0.29705 0.27020 0.03160  0.04541  -0.04562 341 GLY B C   
1145 O O   . GLY A 152 ? 0.47666 0.32967 0.29121 0.03750  0.05857  -0.03746 341 GLY B O   
1146 N N   . VAL A 153 ? 0.36711 0.24112 0.22512 0.02832  0.05000  -0.04519 342 VAL B N   
1147 C CA  . VAL A 153 ? 0.38697 0.28035 0.26376 0.03216  0.06845  -0.03544 342 VAL B CA  
1148 C C   . VAL A 153 ? 0.42258 0.30502 0.29290 0.03906  0.07575  -0.03859 342 VAL B C   
1149 O O   . VAL A 153 ? 0.44709 0.32207 0.32097 0.03385  0.06521  -0.04632 342 VAL B O   
1150 C CB  . VAL A 153 ? 0.37147 0.29678 0.28913 0.02265  0.06580  -0.03026 342 VAL B CB  
1151 C CG1 . VAL A 153 ? 0.34191 0.28732 0.28027 0.02614  0.08121  -0.02048 342 VAL B CG1 
1152 C CG2 . VAL A 153 ? 0.37108 0.30229 0.29131 0.01735  0.05904  -0.02709 342 VAL B CG2 
1153 N N   . ARG A 154 ? 0.40517 0.28630 0.26639 0.05104  0.09445  -0.03203 343 ARG B N   
1154 C CA  . ARG A 154 ? 0.46266 0.33370 0.31796 0.06107  0.10360  -0.03357 343 ARG B CA  
1155 C C   . ARG A 154 ? 0.46138 0.36378 0.34822 0.06671  0.11973  -0.02164 343 ARG B C   
1156 O O   . ARG A 154 ? 0.35733 0.28119 0.25849 0.06605  0.12875  -0.01184 343 ARG B O   
1157 C CB  . ARG A 154 ? 0.49321 0.32555 0.29961 0.07509  0.11088  -0.03882 343 ARG B CB  
1158 C CG  . ARG A 154 ? 0.50567 0.33740 0.29393 0.08470  0.12766  -0.03082 343 ARG B CG  
1159 C CD  . ARG A 154 ? 0.54157 0.32787 0.27313 0.09646  0.12949  -0.03801 343 ARG B CD  
1160 N NE  . ARG A 154 ? 0.61102 0.39818 0.32798 0.10283  0.14306  -0.02818 343 ARG B NE  
1161 C CZ  . ARG A 154 ? 0.69158 0.44440 0.36407 0.10965  0.14125  -0.03059 343 ARG B CZ  
1162 N NH1 . ARG A 154 ? 0.71464 0.43063 0.35370 0.11026  0.12457  -0.04233 343 ARG B NH1 
1163 N NH2 . ARG A 154 ? 0.73491 0.48974 0.39690 0.11496  0.15584  -0.02034 343 ARG B NH2 
1164 N N   . SER A 155 ? 0.41444 0.31885 0.31276 0.07147  0.12193  -0.02207 344 SER B N   
1165 C CA  . SER A 155 ? 0.40178 0.33616 0.33166 0.07819  0.13419  -0.01115 344 SER B CA  
1166 C C   . SER A 155 ? 0.42413 0.35259 0.33829 0.09794  0.15533  -0.00632 344 SER B C   
1167 O O   . SER A 155 ? 0.44150 0.33580 0.31866 0.10719  0.15623  -0.01334 344 SER B O   
1168 C CB  . SER A 155 ? 0.43659 0.37321 0.38260 0.07673  0.12692  -0.01303 344 SER B CB  
1169 O OG  . SER A 155 ? 0.49988 0.46123 0.47197 0.08689  0.13750  -0.00305 344 SER B OG  
1170 N N   . LEU A 156 ? 0.44915 0.41298 0.39528 0.09983  0.16524  0.00666  345 LEU B N   
1171 C CA  . LEU A 156 ? 0.44229 0.41012 0.38573 0.11316  0.17814  0.01364  345 LEU B CA  
1172 C C   . LEU A 156 ? 0.40675 0.38686 0.37067 0.12370  0.17986  0.01714  345 LEU B C   
1173 O O   . LEU A 156 ? 0.51545 0.49800 0.47736 0.13695  0.19108  0.02224  345 LEU B O   
1174 C CB  . LEU A 156 ? 0.40734 0.40574 0.37419 0.10782  0.18717  0.02590  345 LEU B CB  
1175 C CG  . LEU A 156 ? 0.48271 0.46768 0.42725 0.09848  0.18663  0.02441  345 LEU B CG  
1176 C CD1 . LEU A 156 ? 0.45443 0.46885 0.42423 0.09131  0.19530  0.03773  345 LEU B CD1 
1177 C CD2 . LEU A 156 ? 0.41606 0.35743 0.30699 0.10830  0.18952  0.01607  345 LEU B CD2 
1178 N N   . ARG A 157 ? 0.49323 0.47937 0.47487 0.11920  0.16962  0.01475  346 ARG B N   
1179 C CA  . ARG A 157 ? 0.49457 0.48928 0.49302 0.12968  0.16935  0.01812  346 ARG B CA  
1180 C C   . ARG A 157 ? 0.47077 0.43228 0.44697 0.13016  0.15994  0.00769  346 ARG B C   
1181 O O   . ARG A 157 ? 0.46184 0.40366 0.42145 0.11912  0.15237  -0.00112 346 ARG B O   
1182 C CB  . ARG A 157 ? 0.42595 0.46543 0.47424 0.12336  0.16525  0.02886  346 ARG B CB  
1183 C CG  . ARG A 157 ? 0.44988 0.52212 0.52361 0.11607  0.17105  0.03892  346 ARG B CG  
1184 C CD  . ARG A 157 ? 0.56686 0.64387 0.63778 0.13007  0.18605  0.04457  346 ARG B CD  
1185 N NE  . ARG A 157 ? 0.66891 0.75570 0.74027 0.12306  0.19482  0.04995  346 ARG B NE  
1186 C CZ  . ARG A 157 ? 0.64160 0.76498 0.75012 0.11354  0.19610  0.06063  346 ARG B CZ  
1187 N NH1 . ARG A 157 ? 0.76537 0.92078 0.91486 0.10983  0.18781  0.06696  346 ARG B NH1 
1188 N NH2 . ARG A 157 ? 0.63993 0.76556 0.74264 0.10710  0.20495  0.06513  346 ARG B NH2 
1189 N N   . PHE A 158 ? 0.48699 0.44112 0.46268 0.14280  0.16041  0.00884  347 PHE B N   
1190 C CA  . PHE A 158 ? 0.52558 0.44631 0.48077 0.14244  0.15156  0.00049  347 PHE B CA  
1191 C C   . PHE A 158 ? 0.43526 0.37211 0.41578 0.12895  0.14146  0.00169  347 PHE B C   
1192 O O   . PHE A 158 ? 0.50995 0.48429 0.52763 0.12744  0.13967  0.01139  347 PHE B O   
1193 C CB  . PHE A 158 ? 0.59199 0.50073 0.54050 0.15966  0.15412  0.00299  347 PHE B CB  
1194 C CG  . PHE A 158 ? 0.72520 0.59835 0.65339 0.15828  0.14470  -0.00361 347 PHE B CG  
1195 C CD1 . PHE A 158 ? 0.68438 0.51817 0.57950 0.14665  0.13759  -0.01508 347 PHE B CD1 
1196 C CD2 . PHE A 158 ? 0.72685 0.60490 0.66903 0.16744  0.14177  0.00213  347 PHE B CD2 
1197 C CE1 . PHE A 158 ? 0.67042 0.47034 0.54771 0.14200  0.12894  -0.02019 347 PHE B CE1 
1198 C CE2 . PHE A 158 ? 0.69239 0.53339 0.61239 0.16504  0.13352  -0.00286 347 PHE B CE2 
1199 C CZ  . PHE A 158 ? 0.62303 0.42494 0.51106 0.15113  0.12772  -0.01378 347 PHE B CZ  
1200 N N   . ALA A 159 ? 0.51558 0.42601 0.47669 0.11337  0.12883  -0.00746 348 ALA B N   
1201 C CA  . ALA A 159 ? 0.51085 0.43366 0.49045 0.09483  0.11482  -0.00682 348 ALA B CA  
1202 C C   . ALA A 159 ? 0.51957 0.40935 0.47973 0.09244  0.10793  -0.01165 348 ALA B C   
1203 O O   . ALA A 159 ? 0.47425 0.33657 0.41264 0.08122  0.10214  -0.02050 348 ALA B O   
1204 C CB  . ALA A 159 ? 0.44665 0.37525 0.42713 0.07654  0.10777  -0.01170 348 ALA B CB  
1205 N N   . PRO A 160 ? 0.53169 0.42248 0.49924 0.10210  0.10759  -0.00550 349 PRO B N   
1206 C CA  . PRO A 160 ? 0.52072 0.37710 0.46748 0.09886  0.10158  -0.00859 349 PRO B CA  
1207 C C   . PRO A 160 ? 0.42481 0.28379 0.37768 0.07608  0.09154  -0.01066 349 PRO B C   
1208 O O   . PRO A 160 ? 0.45385 0.34358 0.42981 0.06617  0.08787  -0.00809 349 PRO B O   
1209 C CB  . PRO A 160 ? 0.45480 0.31878 0.41245 0.11561  0.10246  0.00058  349 PRO B CB  
1210 C CG  . PRO A 160 ? 0.52103 0.43377 0.51648 0.11801  0.10337  0.00894  349 PRO B CG  
1211 C CD  . PRO A 160 ? 0.42580 0.34976 0.42233 0.11592  0.11159  0.00541  349 PRO B CD  
1212 N N   . ALA A 161 ? 0.42128 0.24569 0.35205 0.06796  0.08798  -0.01517 350 ALA B N   
1213 C CA  . ALA A 161 ? 0.46550 0.29113 0.40162 0.04701  0.08156  -0.01676 350 ALA B CA  
1214 C C   . ALA A 161 ? 0.35629 0.20673 0.31206 0.04547  0.07845  -0.00860 350 ALA B C   
1215 O O   . ALA A 161 ? 0.37331 0.22132 0.32809 0.05787  0.07809  -0.00181 350 ALA B O   
1216 C CB  . ALA A 161 ? 0.43722 0.22129 0.34808 0.03926  0.07999  -0.02020 350 ALA B CB  
1217 N N   . GLY A 162 ? 0.40061 0.27306 0.37233 0.03136  0.07507  -0.00950 351 GLY B N   
1218 C CA  . GLY A 162 ? 0.38509 0.27800 0.37103 0.02911  0.07091  -0.00320 351 GLY B CA  
1219 C C   . GLY A 162 ? 0.39143 0.31848 0.40038 0.03328  0.06864  0.00016  351 GLY B C   
1220 O O   . GLY A 162 ? 0.35773 0.30025 0.37722 0.02941  0.06285  0.00432  351 GLY B O   
1221 N N   . THR A 163 ? 0.39084 0.32724 0.40527 0.04050  0.07315  -0.00126 352 THR B N   
1222 C CA  . THR A 163 ? 0.39529 0.36365 0.43251 0.04301  0.07259  0.00341  352 THR B CA  
1223 C C   . THR A 163 ? 0.28695 0.26783 0.33149 0.02856  0.06856  -0.00011 352 THR B C   
1224 O O   . THR A 163 ? 0.22884 0.19951 0.26378 0.02162  0.06977  -0.00735 352 THR B O   
1225 C CB  . THR A 163 ? 0.36806 0.34023 0.40560 0.05552  0.08188  0.00376  352 THR B CB  
1226 O OG1 . THR A 163 ? 0.34649 0.30514 0.37587 0.07184  0.08643  0.00669  352 THR B OG1 
1227 C CG2 . THR A 163 ? 0.32977 0.33642 0.39359 0.05661  0.08310  0.01065  352 THR B CG2 
1228 N N   . PHE A 164 ? 0.26323 0.26471 0.32410 0.02450  0.06229  0.00494  353 PHE B N   
1229 C CA  . PHE A 164 ? 0.28392 0.29550 0.35032 0.01328  0.05841  0.00216  353 PHE B CA  
1230 C C   . PHE A 164 ? 0.23364 0.25764 0.30716 0.01405  0.06254  0.00224  353 PHE B C   
1231 O O   . PHE A 164 ? 0.33666 0.37652 0.42359 0.02052  0.06594  0.00895  353 PHE B O   
1232 C CB  . PHE A 164 ? 0.25122 0.27555 0.32832 0.00886  0.04913  0.00742  353 PHE B CB  
1233 C CG  . PHE A 164 ? 0.23124 0.26287 0.31188 -0.00076 0.04482  0.00505  353 PHE B CG  
1234 C CD1 . PHE A 164 ? 0.22518 0.24599 0.29482 -0.00719 0.04514  -0.00205 353 PHE B CD1 
1235 C CD2 . PHE A 164 ? 0.28569 0.33491 0.38173 -0.00325 0.04053  0.01047  353 PHE B CD2 
1236 C CE1 . PHE A 164 ? 0.22893 0.25431 0.30021 -0.01333 0.04107  -0.00433 353 PHE B CE1 
1237 C CE2 . PHE A 164 ? 0.29560 0.34595 0.39079 -0.01162 0.03597  0.00833  353 PHE B CE2 
1238 C CZ  . PHE A 164 ? 0.22828 0.26566 0.30972 -0.01536 0.03612  0.00060  353 PHE B CZ  
1239 N N   . ILE A 165 ? 0.21648 0.23376 0.28151 0.00767  0.06251  -0.00454 354 ILE B N   
1240 C CA  . ILE A 165 ? 0.31728 0.34050 0.38231 0.00851  0.06605  -0.00455 354 ILE B CA  
1241 C C   . ILE A 165 ? 0.26033 0.29698 0.33558 0.00059  0.06037  -0.00176 354 ILE B C   
1242 O O   . ILE A 165 ? 0.23190 0.28353 0.31963 0.00118  0.06224  0.00575  354 ILE B O   
1243 C CB  . ILE A 165 ? 0.33106 0.33576 0.37768 0.00751  0.06682  -0.01351 354 ILE B CB  
1244 C CG1 . ILE A 165 ? 0.31506 0.30050 0.34756 0.01450  0.07141  -0.01651 354 ILE B CG1 
1245 C CG2 . ILE A 165 ? 0.31570 0.32122 0.35541 0.00944  0.06979  -0.01354 354 ILE B CG2 
1246 C CD1 . ILE A 165 ? 0.29680 0.26667 0.32212 0.00666  0.06648  -0.02313 354 ILE B CD1 
1247 N N   . THR A 166 ? 0.27336 0.30448 0.34419 -0.00675 0.05381  -0.00724 355 THR B N   
1248 C CA  . THR A 166 ? 0.26587 0.30255 0.34031 -0.01307 0.04777  -0.00622 355 THR B CA  
1249 C C   . THR A 166 ? 0.28141 0.31050 0.35014 -0.01723 0.04280  -0.01335 355 THR B C   
1250 O O   . THR A 166 ? 0.24121 0.26358 0.30606 -0.01689 0.04484  -0.01839 355 THR B O   
1251 C CB  . THR A 166 ? 0.29957 0.33587 0.36884 -0.01248 0.05048  -0.00555 355 THR B CB  
1252 O OG1 . THR A 166 ? 0.36725 0.40539 0.43829 -0.01866 0.04405  -0.00353 355 THR B OG1 
1253 C CG2 . THR A 166 ? 0.26496 0.28804 0.31966 -0.01045 0.05057  -0.01403 355 THR B CG2 
1254 N N   . CYS A 167 ? 0.26168 0.29150 0.33037 -0.02108 0.03686  -0.01331 356 CYS B N   
1255 C CA  . CYS A 167 ? 0.26374 0.28849 0.32834 -0.02252 0.03361  -0.01945 356 CYS B CA  
1256 C C   . CYS A 167 ? 0.27719 0.29987 0.33830 -0.02159 0.03088  -0.02376 356 CYS B C   
1257 O O   . CYS A 167 ? 0.32953 0.35105 0.38694 -0.02129 0.02999  -0.02080 356 CYS B O   
1258 C CB  . CYS A 167 ? 0.23188 0.25324 0.29343 -0.02492 0.02799  -0.01734 356 CYS B CB  
1259 S SG  . CYS A 167 ? 0.37696 0.39548 0.43642 -0.02498 0.02816  -0.01416 356 CYS B SG  
1260 N N   . TYR A 168 ? 0.20328 0.22597 0.26605 -0.02075 0.02983  -0.03006 357 TYR B N   
1261 C CA  . TYR A 168 ? 0.25260 0.27448 0.31388 -0.01831 0.02463  -0.03436 357 TYR B CA  
1262 C C   . TYR A 168 ? 0.26489 0.28202 0.32131 -0.01659 0.02011  -0.03383 357 TYR B C   
1263 O O   . TYR A 168 ? 0.28212 0.29993 0.34049 -0.01472 0.02131  -0.03647 357 TYR B O   
1264 C CB  . TYR A 168 ? 0.23865 0.26685 0.30962 -0.01813 0.02463  -0.04079 357 TYR B CB  
1265 C CG  . TYR A 168 ? 0.28314 0.31177 0.35405 -0.01490 0.01656  -0.04505 357 TYR B CG  
1266 C CD1 . TYR A 168 ? 0.26848 0.29087 0.33136 -0.01496 0.01281  -0.04647 357 TYR B CD1 
1267 C CD2 . TYR A 168 ? 0.22759 0.26036 0.30351 -0.01015 0.01203  -0.04773 357 TYR B CD2 
1268 C CE1 . TYR A 168 ? 0.29764 0.31757 0.35687 -0.01149 0.00293  -0.05027 357 TYR B CE1 
1269 C CE2 . TYR A 168 ? 0.26836 0.30140 0.34437 -0.00568 0.00257  -0.05122 357 TYR B CE2 
1270 C CZ  . TYR A 168 ? 0.30521 0.33167 0.37258 -0.00692 -0.00289 -0.05240 357 TYR B CZ  
1271 O OH  . TYR A 168 ? 0.24249 0.26649 0.30652 -0.00201 -0.01471 -0.05583 357 TYR B OH  
1272 N N   . LEU A 169 ? 0.26519 0.27466 0.31261 -0.01697 0.01578  -0.03012 358 LEU B N   
1273 C CA  . LEU A 169 ? 0.31559 0.31410 0.35382 -0.01620 0.01010  -0.02916 358 LEU B CA  
1274 C C   . LEU A 169 ? 0.31789 0.31006 0.34982 -0.00996 0.00421  -0.03292 358 LEU B C   
1275 O O   . LEU A 169 ? 0.26271 0.26023 0.29812 -0.00707 0.00313  -0.03603 358 LEU B O   
1276 C CB  . LEU A 169 ? 0.34936 0.34179 0.38260 -0.02300 0.00834  -0.02103 358 LEU B CB  
1277 C CG  . LEU A 169 ? 0.30899 0.30963 0.35102 -0.02813 0.01142  -0.01633 358 LEU B CG  
1278 C CD1 . LEU A 169 ? 0.32399 0.32430 0.36816 -0.03572 0.00891  -0.00733 358 LEU B CD1 
1279 C CD2 . LEU A 169 ? 0.30873 0.30449 0.34714 -0.02721 0.00936  -0.01952 358 LEU B CD2 
1280 N N   . GLY A 170 ? 0.34365 0.32153 0.36402 -0.00739 -0.00129 -0.03275 359 GLY B N   
1281 C CA  . GLY A 170 ? 0.31776 0.28610 0.32953 0.00045  -0.00816 -0.03559 359 GLY B CA  
1282 C C   . GLY A 170 ? 0.33532 0.29188 0.33905 0.00770  -0.01116 -0.03907 359 GLY B C   
1283 O O   . GLY A 170 ? 0.33810 0.28932 0.33774 0.00522  -0.00868 -0.03881 359 GLY B O   
1284 N N   . GLU A 171 ? 0.34354 0.31961 0.37772 0.01678  -0.04408 -0.02027 360 GLU B N   
1285 C CA  . GLU A 171 ? 0.29683 0.27821 0.33783 0.02554  -0.04442 -0.02637 360 GLU B CA  
1286 C C   . GLU A 171 ? 0.27750 0.28940 0.34191 0.02554  -0.03977 -0.03066 360 GLU B C   
1287 O O   . GLU A 171 ? 0.23483 0.26496 0.31641 0.02313  -0.04212 -0.03044 360 GLU B O   
1288 C CB  . GLU A 171 ? 0.30637 0.27214 0.33937 0.04012  -0.05449 -0.02784 360 GLU B CB  
1289 C CG  . GLU A 171 ? 0.40053 0.32575 0.40293 0.04170  -0.05344 -0.02333 360 GLU B CG  
1290 C CD  . GLU A 171 ? 0.44497 0.34649 0.42935 0.05886  -0.06579 -0.02352 360 GLU B CD  
1291 O OE1 . GLU A 171 ? 0.45123 0.35099 0.42983 0.06498  -0.07863 -0.02249 360 GLU B OE1 
1292 O OE2 . GLU A 171 ? 0.54466 0.42584 0.51813 0.06736  -0.06498 -0.02539 360 GLU B OE2 
1293 N N   . VAL A 172 ? 0.34146 0.35425 0.40417 0.02790  -0.03152 -0.03496 361 VAL B N   
1294 C CA  . VAL A 172 ? 0.30370 0.33686 0.38285 0.02983  -0.01995 -0.03883 361 VAL B CA  
1295 C C   . VAL A 172 ? 0.27686 0.31537 0.37212 0.04461  -0.01868 -0.04531 361 VAL B C   
1296 O O   . VAL A 172 ? 0.28515 0.30344 0.36274 0.05254  -0.01931 -0.04834 361 VAL B O   
1297 C CB  . VAL A 172 ? 0.33342 0.35513 0.38959 0.02529  -0.00999 -0.03942 361 VAL B CB  
1298 C CG1 . VAL A 172 ? 0.31905 0.35256 0.38356 0.02784  0.00857  -0.04201 361 VAL B CG1 
1299 C CG2 . VAL A 172 ? 0.25442 0.27162 0.29985 0.01343  -0.01494 -0.03367 361 VAL B CG2 
1300 N N   . ILE A 173 ? 0.30159 0.36737 0.43477 0.04850  -0.01761 -0.04842 362 ILE B N   
1301 C CA  . ILE A 173 ? 0.26575 0.34253 0.42706 0.06464  -0.02007 -0.05542 362 ILE B CA  
1302 C C   . ILE A 173 ? 0.27616 0.38263 0.47943 0.06537  0.00058  -0.06078 362 ILE B C   
1303 O O   . ILE A 173 ? 0.23687 0.35488 0.44824 0.05245  0.01370  -0.05822 362 ILE B O   
1304 C CB  . ILE A 173 ? 0.24726 0.32743 0.42368 0.07228  -0.04549 -0.05611 362 ILE B CB  
1305 C CG1 . ILE A 173 ? 0.21219 0.31571 0.41612 0.06157  -0.05225 -0.05576 362 ILE B CG1 
1306 C CG2 . ILE A 173 ? 0.28929 0.33105 0.41830 0.07304  -0.05853 -0.04993 362 ILE B CG2 
1307 C CD1 . ILE A 173 ? 0.32566 0.42468 0.53424 0.06964  -0.08174 -0.05760 362 ILE B CD1 
1308 N N   . THR A 174 ? 0.34642 0.46269 0.57742 0.08124  0.00593  -0.06816 363 THR B N   
1309 C CA  . THR A 174 ? 0.35717 0.50115 0.63555 0.08387  0.03154  -0.07422 363 THR B CA  
1310 C C   . THR A 174 ? 0.29484 0.47999 0.64378 0.08265  0.01981  -0.07940 363 THR B C   
1311 O O   . THR A 174 ? 0.27466 0.46182 0.62724 0.08284  -0.01162 -0.07893 363 THR B O   
1312 C CB  . THR A 174 ? 0.34800 0.48438 0.62990 0.10300  0.04490  -0.08103 363 THR B CB  
1313 O OG1 . THR A 174 ? 0.37713 0.51348 0.67234 0.11918  0.01731  -0.08459 363 THR B OG1 
1314 C CG2 . THR A 174 ? 0.35838 0.45125 0.57037 0.10270  0.05685  -0.07826 363 THR B CG2 
1315 N N   . SER A 175 ? 0.27105 0.48554 0.67522 0.08125  0.04623  -0.08497 364 SER B N   
1316 C CA  . SER A 175 ? 0.29021 0.53249 0.74511 0.07371  0.03346  -0.08668 364 SER B CA  
1317 C C   . SER A 175 ? 0.28870 0.53667 0.76355 0.09013  0.00197  -0.09181 364 SER B C   
1318 O O   . SER A 175 ? 0.28506 0.54025 0.77599 0.08685  -0.02758 -0.09380 364 SER B O   
1319 C CB  . SER A 175 ? 0.29463 0.55287 0.78537 0.06592  0.06989  -0.08775 364 SER B CB  
1320 O OG  . SER A 175 ? 0.41875 0.66307 0.88129 0.05056  0.09804  -0.08154 364 SER B OG  
1321 N N   . ALA A 176 ? 0.27786 0.51702 0.74619 0.10883  0.00791  -0.09439 365 ALA B N   
1322 C CA  . ALA A 176 ? 0.35727 0.59583 0.83750 0.12633  -0.02154 -0.09830 365 ALA B CA  
1323 C C   . ALA A 176 ? 0.36552 0.57616 0.79988 0.12961  -0.05866 -0.09485 365 ALA B C   
1324 O O   . ALA A 176 ? 0.40327 0.61326 0.84607 0.13469  -0.08965 -0.09748 365 ALA B O   
1325 C CB  . ALA A 176 ? 0.33989 0.56709 0.81236 0.14610  -0.00526 -0.10050 365 ALA B CB  
1326 N N   . GLU A 177 ? 0.46362 0.64650 0.84582 0.12734  -0.05538 -0.08960 366 GLU B N   
1327 C CA  . GLU A 177 ? 0.43977 0.59023 0.77296 0.12966  -0.08535 -0.08470 366 GLU B CA  
1328 C C   . GLU A 177 ? 0.36951 0.52766 0.70632 0.11371  -0.10093 -0.08269 366 GLU B C   
1329 O O   . GLU A 177 ? 0.40274 0.53808 0.71186 0.11778  -0.12953 -0.08122 366 GLU B O   
1330 C CB  . GLU A 177 ? 0.33521 0.44920 0.60708 0.12639  -0.07339 -0.07782 366 GLU B CB  
1331 C CG  . GLU A 177 ? 0.47745 0.54850 0.69046 0.12709  -0.09563 -0.07003 366 GLU B CG  
1332 C CD  . GLU A 177 ? 0.63873 0.68486 0.83946 0.15137  -0.11827 -0.07250 366 GLU B CD  
1333 O OE1 . GLU A 177 ? 0.63037 0.68600 0.85462 0.16433  -0.11119 -0.07803 366 GLU B OE1 
1334 O OE2 . GLU A 177 ? 0.65461 0.66536 0.81227 0.15463  -0.13900 -0.06693 366 GLU B OE2 
1335 N N   . ALA A 178 ? 0.33001 0.51326 0.69363 0.09585  -0.08062 -0.08254 367 ALA B N   
1336 C CA  . ALA A 178 ? 0.36023 0.54775 0.72654 0.08013  -0.09335 -0.08116 367 ALA B CA  
1337 C C   . ALA A 178 ? 0.36478 0.56266 0.76345 0.08374  -0.11639 -0.08830 367 ALA B C   
1338 O O   . ALA A 178 ? 0.42543 0.60504 0.80153 0.08219  -0.14256 -0.08859 367 ALA B O   
1339 C CB  . ALA A 178 ? 0.34362 0.55184 0.73148 0.06075  -0.06382 -0.07931 367 ALA B CB  
1340 N N   . ALA A 179 ? 0.37534 0.60002 0.82643 0.08949  -0.10672 -0.09503 368 ALA B N   
1341 C CA  . ALA A 179 ? 0.37036 0.60620 0.85889 0.09551  -0.13179 -0.10404 368 ALA B CA  
1342 C C   . ALA A 179 ? 0.42767 0.63175 0.87711 0.11523  -0.16542 -0.10516 368 ALA B C   
1343 O O   . ALA A 179 ? 0.47585 0.66771 0.92127 0.11874  -0.19659 -0.11065 368 ALA B O   
1344 C CB  . ALA A 179 ? 0.26342 0.53548 0.82029 0.09817  -0.11120 -0.11082 368 ALA B CB  
1345 N N   . LYS A 180 ? 0.40682 0.59156 0.82259 0.12893  -0.15914 -0.10038 369 LYS B N   
1346 C CA  . LYS A 180 ? 0.45037 0.59663 0.82000 0.14762  -0.18716 -0.09983 369 LYS B CA  
1347 C C   . LYS A 180 ? 0.53760 0.64109 0.84059 0.14369  -0.20616 -0.09399 369 LYS B C   
1348 O O   . LYS A 180 ? 0.60802 0.67540 0.87197 0.15639  -0.23344 -0.09534 369 LYS B O   
1349 C CB  . LYS A 180 ? 0.53641 0.66685 0.88237 0.16156  -0.17200 -0.09540 369 LYS B CB  
1350 C CG  . LYS A 180 ? 0.70538 0.84066 1.07691 0.18170  -0.18138 -0.10148 369 LYS B CG  
1351 C CD  . LYS A 180 ? 0.71612 0.83383 1.06406 0.19424  -0.16155 -0.09726 369 LYS B CD  
1352 C CE  . LYS A 180 ? 0.77422 0.93127 1.18168 0.19621  -0.13095 -0.10200 369 LYS B CE  
1353 N NZ  . LYS A 180 ? 0.58798 0.72323 0.96406 0.20389  -0.10520 -0.09847 369 LYS B NZ  
1354 N N   . ARG A 181 ? 0.49625 0.59939 0.78211 0.12727  -0.19085 -0.08744 370 ARG B N   
1355 C CA  . ARG A 181 ? 0.56899 0.63359 0.79610 0.12227  -0.20454 -0.08159 370 ARG B CA  
1356 C C   . ARG A 181 ? 0.61334 0.68970 0.85986 0.10900  -0.21503 -0.08630 370 ARG B C   
1357 O O   . ARG A 181 ? 0.66381 0.70596 0.86087 0.10560  -0.22599 -0.08228 370 ARG B O   
1358 C CB  . ARG A 181 ? 0.44524 0.49874 0.63985 0.11305  -0.18325 -0.07130 370 ARG B CB  
1359 C CG  . ARG A 181 ? 0.43162 0.46355 0.59851 0.12514  -0.17262 -0.06626 370 ARG B CG  
1360 C CD  . ARG A 181 ? 0.36113 0.37448 0.48990 0.11158  -0.15114 -0.05625 370 ARG B CD  
1361 N NE  . ARG A 181 ? 0.48440 0.47247 0.58396 0.11674  -0.13564 -0.05199 370 ARG B NE  
1362 C CZ  . ARG A 181 ? 0.43840 0.40107 0.49920 0.10382  -0.11675 -0.04372 370 ARG B CZ  
1363 N NH1 . ARG A 181 ? 0.39597 0.35526 0.44156 0.08685  -0.10940 -0.03788 370 ARG B NH1 
1364 N NH2 . ARG A 181 ? 0.50217 0.44232 0.54301 0.10831  -0.10581 -0.04233 370 ARG B NH2 
1365 N N   . ASP A 182 ? 0.53950 0.65964 0.85436 0.10135  -0.20862 -0.09416 371 ASP B N   
1366 C CA  . ASP A 182 ? 0.57894 0.70863 0.91659 0.08933  -0.21907 -0.09976 371 ASP B CA  
1367 C C   . ASP A 182 ? 0.67683 0.77473 0.99013 0.10413  -0.25630 -0.10686 371 ASP B C   
1368 O O   . ASP A 182 ? 0.73949 0.83691 1.06720 0.09927  -0.27396 -0.11404 371 ASP B O   
1369 C CB  . ASP A 182 ? 0.51677 0.69602 0.93442 0.07955  -0.20236 -0.10685 371 ASP B CB  
1370 C CG  . ASP A 182 ? 0.54197 0.73786 0.97416 0.05743  -0.17870 -0.10296 371 ASP B CG  
1371 O OD1 . ASP A 182 ? 0.65059 0.82432 1.04690 0.04933  -0.18854 -0.09995 371 ASP B OD1 
1372 O OD2 . ASP A 182 ? 0.49615 0.72334 0.97235 0.04887  -0.14892 -0.10282 371 ASP B OD2 
1373 N N   . LYS A 183 ? 0.69369 0.76210 0.96926 0.12289  -0.26869 -0.10560 372 LYS B N   
1374 C CA  . LYS A 183 ? 0.76076 0.78607 0.99628 0.13964  -0.30412 -0.11158 372 LYS B CA  
1375 C C   . LYS A 183 ? 0.64182 0.70098 0.94775 0.14830  -0.32097 -0.12533 372 LYS B C   
1376 O O   . LYS A 183 ? 0.54950 0.65156 0.91344 0.14745  -0.30203 -0.12674 372 LYS B O   
1377 C CB  . LYS A 183 ? 0.84853 0.83605 1.03845 0.13518  -0.32221 -0.11234 372 LYS B CB  
1378 C CG  . LYS A 183 ? 0.90893 0.87438 1.04652 0.12289  -0.30077 -0.09926 372 LYS B CG  
1379 C CD  . LYS A 183 ? 0.96763 0.92262 1.09535 0.11123  -0.30850 -0.10114 372 LYS B CD  
1380 C CE  . LYS A 183 ? 0.92931 0.90259 1.05884 0.09140  -0.27902 -0.09142 372 LYS B CE  
1381 N NZ  . LYS A 183 ? 0.86730 0.86026 1.02935 0.07583  -0.28075 -0.09638 372 LYS B NZ  
1382 N N   . ASP A 186 ? 1.51401 1.27195 1.41903 0.19612  -0.36802 -0.10197 375 ASP B N   
1383 C CA  . ASP A 186 ? 1.58284 1.30018 1.43978 0.19136  -0.37524 -0.10186 375 ASP B CA  
1384 C C   . ASP A 186 ? 1.60195 1.37226 1.52328 0.17176  -0.37004 -0.10440 375 ASP B C   
1385 O O   . ASP A 186 ? 1.43110 1.25785 1.40944 0.15695  -0.34609 -0.09990 375 ASP B O   
1386 C CB  . ASP A 186 ? 1.65628 1.31576 1.42523 0.18879  -0.34963 -0.08742 375 ASP B CB  
1387 C CG  . ASP A 186 ? 1.77778 1.36866 1.47113 0.19362  -0.36052 -0.08877 375 ASP B CG  
1388 O OD1 . ASP A 186 ? 1.73434 1.33403 1.45238 0.19201  -0.38298 -0.09813 375 ASP B OD1 
1389 O OD2 . ASP A 186 ? 1.93278 1.45836 1.54116 0.19895  -0.34452 -0.08064 375 ASP B OD2 
1390 N N   . ASP A 187 ? 1.59274 1.34104 1.50203 0.17215  -0.39235 -0.11197 376 ASP B N   
1391 C CA  . ASP A 187 ? 1.44717 1.23441 1.40469 0.15333  -0.38739 -0.11376 376 ASP B CA  
1392 C C   . ASP A 187 ? 1.41996 1.14848 1.31379 0.15620  -0.40337 -0.11502 376 ASP B C   
1393 O O   . ASP A 187 ? 1.31235 0.99754 1.17540 0.17300  -0.43620 -0.12495 376 ASP B O   
1394 C CB  . ASP A 187 ? 1.33384 1.18369 1.38975 0.14931  -0.40245 -0.12740 376 ASP B CB  
1395 C CG  . ASP A 187 ? 1.29501 1.16763 1.38762 0.13278  -0.40514 -0.13196 376 ASP B CG  
1396 O OD1 . ASP A 187 ? 1.17407 1.07670 1.28534 0.11355  -0.37574 -0.12364 376 ASP B OD1 
1397 O OD2 . ASP A 187 ? 1.31879 1.17686 1.42019 0.13942  -0.43787 -0.14441 376 ASP B OD2 
1398 N N   . ASP A 188 ? 1.46570 1.19005 1.33801 0.14094  -0.38082 -0.10538 377 ASP B N   
1399 C CA  . ASP A 188 ? 1.33523 1.00401 1.14638 0.14241  -0.39072 -0.10512 377 ASP B CA  
1400 C C   . ASP A 188 ? 1.09433 0.79991 0.94184 0.12066  -0.37650 -0.10262 377 ASP B C   
1401 O O   . ASP A 188 ? 1.00097 0.66403 0.79221 0.11758  -0.37007 -0.09704 377 ASP B O   
1402 C CB  . ASP A 188 ? 1.38892 0.98160 1.09710 0.15148  -0.37330 -0.09354 377 ASP B CB  
1403 C CG  . ASP A 188 ? 1.43315 1.04559 1.14096 0.14330  -0.33694 -0.08056 377 ASP B CG  
1404 O OD1 . ASP A 188 ? 1.31802 0.99995 1.10093 0.13264  -0.32778 -0.08057 377 ASP B OD1 
1405 O OD2 . ASP A 188 ? 1.53192 1.08773 1.16389 0.14759  -0.31610 -0.07081 377 ASP B OD2 
1406 N N   . GLY A 189 ? 0.98440 0.76483 0.92246 0.10567  -0.36902 -0.10677 378 GLY B N   
1407 C CA  . GLY A 189 ? 0.89043 0.70587 0.86281 0.08385  -0.35146 -0.10440 378 GLY B CA  
1408 C C   . GLY A 189 ? 0.86364 0.68409 0.81378 0.07192  -0.31561 -0.09031 378 GLY B C   
1409 O O   . GLY A 189 ? 0.81186 0.64801 0.77371 0.05505  -0.30091 -0.08775 378 GLY B O   
1410 N N   . ILE A 190 ? 0.83780 0.64342 0.75624 0.08012  -0.30197 -0.08186 379 ILE B N   
1411 C CA  . ILE A 190 ? 0.67793 0.48469 0.57442 0.07042  -0.27070 -0.06923 379 ILE B CA  
1412 C C   . ILE A 190 ? 0.63980 0.50221 0.59611 0.06588  -0.25622 -0.06795 379 ILE B C   
1413 O O   . ILE A 190 ? 0.70118 0.56469 0.66423 0.07908  -0.26401 -0.07012 379 ILE B O   
1414 C CB  . ILE A 190 ? 0.75990 0.49601 0.56462 0.08278  -0.26240 -0.05953 379 ILE B CB  
1415 C CG1 . ILE A 190 ? 0.90608 0.57842 0.64694 0.09148  -0.27727 -0.06204 379 ILE B CG1 
1416 C CG2 . ILE A 190 ? 0.76370 0.49919 0.54785 0.07109  -0.23033 -0.04737 379 ILE B CG2 
1417 C CD1 . ILE A 190 ? 0.95213 0.54782 0.59926 0.10241  -0.26042 -0.05244 379 ILE B CD1 
1418 N N   . THR A 191 ? 0.59550 0.49991 0.59217 0.04803  -0.23472 -0.06488 380 THR B N   
1419 C CA  . THR A 191 ? 0.46638 0.41790 0.51369 0.04347  -0.21714 -0.06301 380 THR B CA  
1420 C C   . THR A 191 ? 0.44032 0.39582 0.47530 0.03045  -0.19278 -0.05386 380 THR B C   
1421 O O   . THR A 191 ? 0.38564 0.32836 0.40181 0.01899  -0.18517 -0.05138 380 THR B O   
1422 C CB  . THR A 191 ? 0.42849 0.43525 0.55661 0.03473  -0.21464 -0.07182 380 THR B CB  
1423 O OG1 . THR A 191 ? 0.27545 0.31943 0.44290 0.03204  -0.19331 -0.06930 380 THR B OG1 
1424 C CG2 . THR A 191 ? 0.39667 0.41626 0.54354 0.01630  -0.20673 -0.07326 380 THR B CG2 
1425 N N   . TYR A 192 ? 0.37506 0.34408 0.41845 0.03236  -0.17304 -0.04764 381 TYR B N   
1426 C CA  . TYR A 192 ? 0.35927 0.33296 0.39592 0.02014  -0.13899 -0.03734 381 TYR B CA  
1427 C C   . TYR A 192 ? 0.30900 0.32843 0.39836 0.01374  -0.12190 -0.03865 381 TYR B C   
1428 O O   . TYR A 192 ? 0.27105 0.29231 0.35323 0.00805  -0.09906 -0.03156 381 TYR B O   
1429 C CB  . TYR A 192 ? 0.42438 0.35796 0.40891 0.02726  -0.12671 -0.02776 381 TYR B CB  
1430 C CG  . TYR A 192 ? 0.46867 0.34629 0.38962 0.03443  -0.13514 -0.02458 381 TYR B CG  
1431 C CD1 . TYR A 192 ? 0.42379 0.28173 0.31930 0.02531  -0.12136 -0.01992 381 TYR B CD1 
1432 C CD2 . TYR A 192 ? 0.51729 0.35569 0.39786 0.05227  -0.15563 -0.02604 381 TYR B CD2 
1433 C CE1 . TYR A 192 ? 0.51873 0.31855 0.34905 0.03307  -0.12449 -0.01700 381 TYR B CE1 
1434 C CE2 . TYR A 192 ? 0.57195 0.34816 0.38139 0.06057  -0.16098 -0.02255 381 TYR B CE2 
1435 C CZ  . TYR A 192 ? 0.62646 0.38313 0.41036 0.05055  -0.14368 -0.01813 381 TYR B CZ  
1436 O OH  . TYR A 192 ? 0.78348 0.47161 0.48989 0.05996  -0.14468 -0.01468 381 TYR B OH  
1437 N N   . LEU A 193 ? 0.25360 0.30742 0.39593 0.01526  -0.13257 -0.04840 382 LEU B N   
1438 C CA  . LEU A 193 ? 0.24730 0.33834 0.43532 0.01086  -0.11202 -0.04994 382 LEU B CA  
1439 C C   . LEU A 193 ? 0.22672 0.33341 0.43213 -0.00703 -0.09180 -0.04763 382 LEU B C   
1440 O O   . LEU A 193 ? 0.16176 0.27167 0.38160 -0.01579 -0.10089 -0.05172 382 LEU B O   
1441 C CB  . LEU A 193 ? 0.22063 0.34184 0.46448 0.02032  -0.12615 -0.06138 382 LEU B CB  
1442 C CG  . LEU A 193 ? 0.27598 0.38093 0.50445 0.04097  -0.14499 -0.06376 382 LEU B CG  
1443 C CD1 . LEU A 193 ? 0.33251 0.46113 0.60984 0.04753  -0.15210 -0.07325 382 LEU B CD1 
1444 C CD2 . LEU A 193 ? 0.24711 0.34295 0.45329 0.04682  -0.12624 -0.05739 382 LEU B CD2 
1445 N N   . PHE A 194 ? 0.21680 0.32797 0.41653 -0.01161 -0.06595 -0.04155 383 PHE B N   
1446 C CA  . PHE A 194 ? 0.20115 0.31785 0.40528 -0.02576 -0.04492 -0.03749 383 PHE B CA  
1447 C C   . PHE A 194 ? 0.17859 0.31284 0.40517 -0.02521 -0.02163 -0.03851 383 PHE B C   
1448 O O   . PHE A 194 ? 0.19765 0.32143 0.39904 -0.01828 -0.01325 -0.03516 383 PHE B O   
1449 C CB  . PHE A 194 ? 0.20014 0.29023 0.35661 -0.02934 -0.03854 -0.02774 383 PHE B CB  
1450 C CG  . PHE A 194 ? 0.23480 0.32131 0.38783 -0.04185 -0.02597 -0.02355 383 PHE B CG  
1451 C CD1 . PHE A 194 ? 0.18594 0.28522 0.36025 -0.04900 -0.00662 -0.02386 383 PHE B CD1 
1452 C CD2 . PHE A 194 ? 0.28407 0.34933 0.40916 -0.04541 -0.03069 -0.01882 383 PHE B CD2 
1453 C CE1 . PHE A 194 ? 0.29620 0.38473 0.46078 -0.05954 0.00561  -0.01898 383 PHE B CE1 
1454 C CE2 . PHE A 194 ? 0.26477 0.32309 0.38441 -0.05504 -0.01990 -0.01482 383 PHE B CE2 
1455 C CZ  . PHE A 194 ? 0.26074 0.32949 0.39849 -0.06215 -0.00283 -0.01462 383 PHE B CZ  
1456 N N   . ASP A 195 ? 0.14483 0.30228 0.41808 -0.03276 -0.00976 -0.04378 384 ASP B N   
1457 C CA  . ASP A 195 ? 0.19623 0.36529 0.48892 -0.03171 0.01872  -0.04473 384 ASP B CA  
1458 C C   . ASP A 195 ? 0.26174 0.40481 0.50619 -0.03672 0.04186  -0.03502 384 ASP B C   
1459 O O   . ASP A 195 ? 0.27378 0.40280 0.49856 -0.04691 0.04403  -0.02930 384 ASP B O   
1460 C CB  . ASP A 195 ? 0.18342 0.37981 0.53935 -0.03983 0.03005  -0.05201 384 ASP B CB  
1461 C CG  . ASP A 195 ? 0.23118 0.44691 0.62526 -0.02787 0.01088  -0.06100 384 ASP B CG  
1462 O OD1 . ASP A 195 ? 0.19889 0.41567 0.58669 -0.01302 0.00038  -0.06331 384 ASP B OD1 
1463 O OD2 . ASP A 195 ? 0.29232 0.52035 0.72301 -0.03281 0.00583  -0.06627 384 ASP B OD2 
1464 N N   . LEU A 196 ? 0.22800 0.36054 0.44975 -0.02772 0.05694  -0.03386 385 LEU B N   
1465 C CA  . LEU A 196 ? 0.28676 0.38985 0.45967 -0.02930 0.07739  -0.02656 385 LEU B CA  
1466 C C   . LEU A 196 ? 0.28268 0.38843 0.47695 -0.03518 0.11252  -0.02710 385 LEU B C   
1467 O O   . LEU A 196 ? 0.31417 0.41228 0.50135 -0.02754 0.13564  -0.02895 385 LEU B O   
1468 C CB  . LEU A 196 ? 0.27017 0.35321 0.40198 -0.01659 0.07375  -0.02662 385 LEU B CB  
1469 C CG  . LEU A 196 ? 0.34631 0.41852 0.45184 -0.01367 0.04618  -0.02445 385 LEU B CG  
1470 C CD1 . LEU A 196 ? 0.33547 0.38983 0.41130 -0.00273 0.04294  -0.02719 385 LEU B CD1 
1471 C CD2 . LEU A 196 ? 0.24554 0.30038 0.32216 -0.02115 0.04168  -0.01708 385 LEU B CD2 
1472 N N   . ASP A 197 ? 0.25121 0.36402 0.47086 -0.04940 0.11935  -0.02562 386 ASP B N   
1473 C CA  . ASP A 197 ? 0.27171 0.39036 0.52637 -0.05866 0.15543  -0.02685 386 ASP B CA  
1474 C C   . ASP A 197 ? 0.34453 0.42510 0.55229 -0.06778 0.17632  -0.01653 386 ASP B C   
1475 O O   . ASP A 197 ? 0.41838 0.49416 0.64268 -0.07513 0.19258  -0.01590 386 ASP B O   
1476 C CB  . ASP A 197 ? 0.21141 0.36256 0.53082 -0.06444 0.13787  -0.03480 386 ASP B CB  
1477 C CG  . ASP A 197 ? 0.25929 0.41247 0.57891 -0.07296 0.10812  -0.03451 386 ASP B CG  
1478 O OD1 . ASP A 197 ? 0.27386 0.40675 0.55077 -0.07548 0.10296  -0.02790 386 ASP B OD1 
1479 O OD2 . ASP A 197 ? 0.22056 0.39252 0.58086 -0.07644 0.08995  -0.04140 386 ASP B OD2 
1480 N N   . MET A 198 ? 0.28002 0.32618 0.41875 -0.06234 0.16504  -0.00838 387 MET B N   
1481 C CA  . MET A 198 ? 0.46332 0.46864 0.55300 -0.06804 0.18221  0.00170  387 MET B CA  
1482 C C   . MET A 198 ? 0.58916 0.56406 0.65293 -0.06528 0.22136  0.00489  387 MET B C   
1483 O O   . MET A 198 ? 0.59139 0.54565 0.64843 -0.07195 0.23661  0.00898  387 MET B O   
1484 C CB  . MET A 198 ? 0.44660 0.42154 0.47006 -0.05780 0.15691  0.00802  387 MET B CB  
1485 C CG  . MET A 198 ? 0.56772 0.49434 0.53229 -0.05876 0.17003  0.01856  387 MET B CG  
1486 S SD  . MET A 198 ? 0.56921 0.49905 0.56065 -0.07608 0.17093  0.02240  387 MET B SD  
1487 C CE  . MET A 198 ? 0.50710 0.45069 0.49553 -0.07001 0.12569  0.02150  387 MET B CE  
1488 N N   . PHE A 199 ? 0.56019 0.52740 0.60451 -0.05276 0.23284  0.00203  388 PHE B N   
1489 C CA  . PHE A 199 ? 0.60891 0.54152 0.62217 -0.04622 0.26365  0.00389  388 PHE B CA  
1490 C C   . PHE A 199 ? 0.68247 0.65359 0.76836 -0.04701 0.27676  -0.00536 388 PHE B C   
1491 O O   . PHE A 199 ? 0.66564 0.66737 0.78165 -0.03946 0.26533  -0.01286 388 PHE B O   
1492 C CB  . PHE A 199 ? 0.65559 0.54175 0.58479 -0.02930 0.26466  0.00658  388 PHE B CB  
1493 C CG  . PHE A 199 ? 0.63192 0.48455 0.49354 -0.02541 0.24176  0.01358  388 PHE B CG  
1494 C CD1 . PHE A 199 ? 0.55710 0.43644 0.43279 -0.02171 0.19678  0.00927  388 PHE B CD1 
1495 C CD2 . PHE A 199 ? 0.67804 0.47630 0.47427 -0.02197 0.24579  0.02230  388 PHE B CD2 
1496 C CE1 . PHE A 199 ? 0.60506 0.46020 0.43437 -0.01664 0.16643  0.01377  388 PHE B CE1 
1497 C CE2 . PHE A 199 ? 0.70438 0.47291 0.44302 -0.01572 0.21864  0.02794  388 PHE B CE2 
1498 C CZ  . PHE A 199 ? 0.68377 0.48542 0.44654 -0.01308 0.17618  0.02271  388 PHE B CZ  
1499 N N   . ASP A 200 ? 0.82568 0.79338 0.94011 -0.05520 0.30029  -0.00534 389 ASP B N   
1500 C CA  . ASP A 200 ? 0.77914 0.78241 0.96682 -0.05623 0.31275  -0.01433 389 ASP B CA  
1501 C C   . ASP A 200 ? 0.87670 0.85723 1.03752 -0.04244 0.33830  -0.01522 389 ASP B C   
1502 O O   . ASP A 200 ? 0.90463 0.91824 1.12406 -0.03887 0.34338  -0.02340 389 ASP B O   
1503 C CB  . ASP A 200 ? 0.79982 0.80526 1.02983 -0.07035 0.33152  -0.01512 389 ASP B CB  
1504 C CG  . ASP A 200 ? 0.83859 0.90110 1.16622 -0.07658 0.31890  -0.02675 389 ASP B CG  
1505 O OD1 . ASP A 200 ? 0.84511 0.93575 1.20641 -0.06685 0.31245  -0.03374 389 ASP B OD1 
1506 O OD2 . ASP A 200 ? 0.81714 0.89377 1.18529 -0.08997 0.31336  -0.02941 389 ASP B OD2 
1507 N N   . ASP A 201 ? 1.00695 0.93041 1.08022 -0.03303 0.35163  -0.00781 390 ASP B N   
1508 C CA  . ASP A 201 ? 1.05450 0.95480 1.10103 -0.01913 0.37280  -0.00979 390 ASP B CA  
1509 C C   . ASP A 201 ? 1.07762 1.00510 1.13145 -0.00713 0.34881  -0.01692 390 ASP B C   
1510 O O   . ASP A 201 ? 1.06009 0.98992 1.12363 0.00343  0.36148  -0.02215 390 ASP B O   
1511 C CB  . ASP A 201 ? 1.15490 0.97779 1.09765 -0.01010 0.39007  -0.00088 390 ASP B CB  
1512 C CG  . ASP A 201 ? 1.36297 1.15886 1.23329 -0.00352 0.35919  0.00344  390 ASP B CG  
1513 O OD1 . ASP A 201 ? 1.24884 1.08642 1.15166 -0.00793 0.32967  0.00039  390 ASP B OD1 
1514 O OD2 . ASP A 201 ? 1.49703 1.22770 1.27792 0.00680  0.36287  0.00942  390 ASP B OD2 
1515 N N   . ALA A 202 ? 0.87409 0.81923 0.92287 -0.00811 0.31597  -0.01746 391 ALA B N   
1516 C CA  . ALA A 202 ? 0.67683 0.64691 0.73776 0.00330  0.29413  -0.02554 391 ALA B CA  
1517 C C   . ALA A 202 ? 0.61065 0.62830 0.72567 -0.00557 0.26251  -0.02850 391 ALA B C   
1518 O O   . ALA A 202 ? 0.60771 0.61223 0.68416 -0.00795 0.24004  -0.02427 391 ALA B O   
1519 C CB  . ALA A 202 ? 0.71396 0.63233 0.68058 0.01747  0.28709  -0.02424 391 ALA B CB  
1520 N N   . SER A 203 ? 0.52382 0.59219 0.72391 -0.00935 0.25313  -0.03559 392 SER B N   
1521 C CA  . SER A 203 ? 0.40092 0.51125 0.65274 -0.01550 0.21794  -0.03977 392 SER B CA  
1522 C C   . SER A 203 ? 0.37455 0.51744 0.67303 -0.00214 0.20085  -0.04980 392 SER B C   
1523 O O   . SER A 203 ? 0.41161 0.58381 0.77085 -0.00259 0.19814  -0.05534 392 SER B O   
1524 C CB  . SER A 203 ? 0.43181 0.56099 0.73024 -0.03197 0.21405  -0.03892 392 SER B CB  
1525 O OG  . SER A 203 ? 0.46529 0.62694 0.80373 -0.03566 0.17623  -0.04371 392 SER B OG  
1526 N N   . GLU A 204 ? 0.36864 0.49816 0.62839 0.01041  0.18264  -0.05117 393 GLU B N   
1527 C CA  . GLU A 204 ? 0.37845 0.52562 0.66613 0.02645  0.16933  -0.05965 393 GLU B CA  
1528 C C   . GLU A 204 ? 0.29962 0.45231 0.58001 0.03006  0.12350  -0.05999 393 GLU B C   
1529 O O   . GLU A 204 ? 0.30448 0.48140 0.62848 0.04039  0.10622  -0.06711 393 GLU B O   
1530 C CB  . GLU A 204 ? 0.41765 0.52757 0.64988 0.04105  0.19006  -0.06062 393 GLU B CB  
1531 C CG  . GLU A 204 ? 0.60392 0.67537 0.78645 0.03736  0.23067  -0.05515 393 GLU B CG  
1532 C CD  . GLU A 204 ? 0.77506 0.80456 0.89925 0.05375  0.24979  -0.05795 393 GLU B CD  
1533 O OE1 . GLU A 204 ? 0.79980 0.84272 0.94968 0.06721  0.24490  -0.06552 393 GLU B OE1 
1534 O OE2 . GLU A 204 ? 0.90758 0.88611 0.95455 0.05374  0.26461  -0.05222 393 GLU B OE2 
1535 N N   . TYR A 205 ? 0.29358 0.42182 0.52025 0.02309  0.10476  -0.05253 394 TYR B N   
1536 C CA  . TYR A 205 ? 0.26638 0.38985 0.47624 0.02656  0.06941  -0.05165 394 TYR B CA  
1537 C C   . TYR A 205 ? 0.28829 0.42541 0.51540 0.01500  0.04860  -0.04855 394 TYR B C   
1538 O O   . TYR A 205 ? 0.19958 0.34323 0.43856 0.00237  0.05934  -0.04573 394 TYR B O   
1539 C CB  . TYR A 205 ? 0.28257 0.36787 0.42516 0.02799  0.06382  -0.04720 394 TYR B CB  
1540 C CG  . TYR A 205 ? 0.33048 0.39233 0.44325 0.03969  0.08124  -0.05137 394 TYR B CG  
1541 C CD1 . TYR A 205 ? 0.34501 0.41808 0.48655 0.05342  0.08850  -0.05884 394 TYR B CD1 
1542 C CD2 . TYR A 205 ? 0.37351 0.39826 0.42665 0.03886  0.08865  -0.04873 394 TYR B CD2 
1543 C CE1 . TYR A 205 ? 0.38946 0.43586 0.49874 0.06523  0.10636  -0.06329 394 TYR B CE1 
1544 C CE2 . TYR A 205 ? 0.46143 0.45666 0.47780 0.05056  0.10298  -0.05373 394 TYR B CE2 
1545 C CZ  . TYR A 205 ? 0.42327 0.42872 0.46675 0.06331  0.11373  -0.06087 394 TYR B CZ  
1546 O OH  . TYR A 205 ? 0.50175 0.47279 0.50376 0.07598  0.12981  -0.06643 394 TYR B OH  
1547 N N   . THR A 206 ? 0.27662 0.41155 0.49915 0.02010  0.02018  -0.04899 395 THR B N   
1548 C CA  . THR A 206 ? 0.20297 0.34098 0.42963 0.01253  -0.00130 -0.04668 395 THR B CA  
1549 C C   . THR A 206 ? 0.22753 0.33695 0.40659 0.01431  -0.01702 -0.04097 395 THR B C   
1550 O O   . THR A 206 ? 0.24094 0.33589 0.40195 0.02435  -0.02108 -0.04189 395 THR B O   
1551 C CB  . THR A 206 ? 0.17765 0.33997 0.45409 0.01920  -0.02066 -0.05499 395 THR B CB  
1552 O OG1 . THR A 206 ? 0.16950 0.36348 0.50469 0.01568  -0.00330 -0.06163 395 THR B OG1 
1553 C CG2 . THR A 206 ? 0.19456 0.35035 0.46328 0.01275  -0.04469 -0.05361 395 THR B CG2 
1554 N N   . VAL A 207 ? 0.20845 0.30812 0.36952 0.00428  -0.02315 -0.03534 396 VAL B N   
1555 C CA  . VAL A 207 ? 0.23397 0.30802 0.35869 0.00453  -0.03341 -0.02997 396 VAL B CA  
1556 C C   . VAL A 207 ? 0.18525 0.25160 0.30891 0.00986  -0.05327 -0.03120 396 VAL B C   
1557 O O   . VAL A 207 ? 0.20481 0.27947 0.34294 0.00547  -0.06167 -0.03318 396 VAL B O   
1558 C CB  . VAL A 207 ? 0.26198 0.32658 0.36727 -0.00677 -0.02678 -0.02339 396 VAL B CB  
1559 C CG1 . VAL A 207 ? 0.27855 0.32011 0.35811 -0.00681 -0.03333 -0.01873 396 VAL B CG1 
1560 C CG2 . VAL A 207 ? 0.19605 0.25950 0.29190 -0.00895 -0.01184 -0.02252 396 VAL B CG2 
1561 N N   . ASP A 208 ? 0.22761 0.27222 0.32934 0.01979  -0.06146 -0.03041 397 ASP B N   
1562 C CA  . ASP A 208 ? 0.28576 0.30925 0.37006 0.02846  -0.08053 -0.03060 397 ASP B CA  
1563 C C   . ASP A 208 ? 0.31197 0.29929 0.35321 0.02472  -0.07522 -0.02239 397 ASP B C   
1564 O O   . ASP A 208 ? 0.28875 0.25993 0.31503 0.02553  -0.06600 -0.01935 397 ASP B O   
1565 C CB  . ASP A 208 ? 0.25954 0.27911 0.34908 0.04542  -0.09220 -0.03560 397 ASP B CB  
1566 C CG  . ASP A 208 ? 0.34532 0.33764 0.41106 0.05787  -0.11673 -0.03653 397 ASP B CG  
1567 O OD1 . ASP A 208 ? 0.39282 0.37510 0.44489 0.05303  -0.12611 -0.03565 397 ASP B OD1 
1568 O OD2 . ASP A 208 ? 0.37825 0.35352 0.43304 0.07396  -0.12762 -0.03833 397 ASP B OD2 
1569 N N   . ALA A 209 ? 0.24756 0.22043 0.27111 0.02041  -0.07953 -0.01963 398 ALA B N   
1570 C CA  . ALA A 209 ? 0.33045 0.26883 0.31730 0.01671  -0.06875 -0.01187 398 ALA B CA  
1571 C C   . ALA A 209 ? 0.39153 0.28388 0.33286 0.02874  -0.07847 -0.00963 398 ALA B C   
1572 O O   . ALA A 209 ? 0.40607 0.26382 0.31175 0.02673  -0.06882 -0.00370 398 ALA B O   
1573 C CB  . ALA A 209 ? 0.34974 0.29337 0.33820 0.00560  -0.06189 -0.00943 398 ALA B CB  
1574 N N   . GLN A 210 ? 0.40020 0.28704 0.33874 0.04289  -0.09623 -0.01412 399 GLN B N   
1575 C CA  . GLN A 210 ? 0.45359 0.28808 0.33882 0.05777  -0.10918 -0.01186 399 GLN B CA  
1576 C C   . GLN A 210 ? 0.52897 0.31919 0.37454 0.05724  -0.08622 -0.00241 399 GLN B C   
1577 O O   . GLN A 210 ? 0.49648 0.24069 0.29451 0.05737  -0.07547 0.00424  399 GLN B O   
1578 C CB  . GLN A 210 ? 0.51508 0.35612 0.41244 0.07536  -0.13585 -0.01951 399 GLN B CB  
1579 C CG  . GLN A 210 ? 0.69924 0.48084 0.53523 0.09499  -0.15640 -0.01801 399 GLN B CG  
1580 C CD  . GLN A 210 ? 0.74985 0.50872 0.55572 0.09800  -0.17728 -0.02115 399 GLN B CD  
1581 O OE1 . GLN A 210 ? 0.77018 0.46870 0.50695 0.10204  -0.17158 -0.01427 399 GLN B OE1 
1582 N NE2 . GLN A 210 ? 0.75440 0.55806 0.61131 0.09572  -0.19995 -0.03224 399 GLN B NE2 
1583 N N   . ASN A 211 ? 0.42521 0.22555 0.28983 0.05625  -0.07637 -0.00224 400 ASN B N   
1584 C CA  . ASN A 211 ? 0.42013 0.17914 0.25589 0.05450  -0.05523 0.00508  400 ASN B CA  
1585 C C   . ASN A 211 ? 0.44915 0.22753 0.31543 0.03546  -0.03020 0.00755  400 ASN B C   
1586 O O   . ASN A 211 ? 0.46068 0.20518 0.30793 0.02918  -0.00787 0.01426  400 ASN B O   
1587 C CB  . ASN A 211 ? 0.53533 0.28561 0.37039 0.06599  -0.06240 0.00246  400 ASN B CB  
1588 C CG  . ASN A 211 ? 0.56388 0.30970 0.38753 0.08692  -0.09283 -0.00285 400 ASN B CG  
1589 O OD1 . ASN A 211 ? 0.56858 0.35112 0.43109 0.09345  -0.10546 -0.01067 400 ASN B OD1 
1590 N ND2 . ASN A 211 ? 0.53790 0.23654 0.30819 0.09877  -0.10520 0.00060  400 ASN B ND2 
1591 N N   . TYR A 212 ? 0.37909 0.20863 0.29269 0.02700  -0.03325 0.00188  401 TYR B N   
1592 C CA  . TYR A 212 ? 0.38624 0.23673 0.33048 0.01151  -0.01775 0.00237  401 TYR B CA  
1593 C C   . TYR A 212 ? 0.36669 0.24984 0.33047 0.00557  -0.02174 0.00113  401 TYR B C   
1594 O O   . TYR A 212 ? 0.36758 0.27208 0.33882 0.01040  -0.03633 -0.00303 401 TYR B O   
1595 C CB  . TYR A 212 ? 0.36444 0.23531 0.33585 0.00856  -0.01938 -0.00356 401 TYR B CB  
1596 C CG  . TYR A 212 ? 0.41835 0.25680 0.37300 0.01378  -0.01605 -0.00364 401 TYR B CG  
1597 C CD1 . TYR A 212 ? 0.40888 0.23577 0.34504 0.02938  -0.02878 -0.00587 401 TYR B CD1 
1598 C CD2 . TYR A 212 ? 0.42464 0.24425 0.38702 0.00311  -0.00050 -0.00235 401 TYR B CD2 
1599 C CE1 . TYR A 212 ? 0.41737 0.20960 0.33429 0.03537  -0.02547 -0.00557 401 TYR B CE1 
1600 C CE2 . TYR A 212 ? 0.39676 0.18239 0.34330 0.00631  0.00417  -0.00253 401 TYR B CE2 
1601 C CZ  . TYR A 212 ? 0.42293 0.19255 0.34247 0.02297  -0.00805 -0.00357 401 TYR B CZ  
1602 O OH  . TYR A 212 ? 0.45718 0.18789 0.35692 0.02733  -0.00307 -0.00332 401 TYR B OH  
1603 N N   . GLY A 213 ? 0.32959 0.21630 0.30569 -0.00477 -0.00806 0.00431  402 GLY B N   
1604 C CA  . GLY A 213 ? 0.33944 0.25230 0.33109 -0.00974 -0.01104 0.00367  402 GLY B CA  
1605 C C   . GLY A 213 ? 0.37659 0.28625 0.37989 -0.01791 0.00506  0.00768  402 GLY B C   
1606 O O   . GLY A 213 ? 0.36021 0.25333 0.36960 -0.02159 0.02000  0.01003  402 GLY B O   
1607 N N   . ASP A 214 ? 0.35408 0.27976 0.36468 -0.02071 0.00299  0.00800  403 ASP B N   
1608 C CA  . ASP A 214 ? 0.32720 0.25388 0.35251 -0.02589 0.01603  0.01110  403 ASP B CA  
1609 C C   . ASP A 214 ? 0.36600 0.26552 0.35927 -0.02294 0.02374  0.01498  403 ASP B C   
1610 O O   . ASP A 214 ? 0.35171 0.23220 0.31127 -0.01717 0.01441  0.01430  403 ASP B O   
1611 C CB  . ASP A 214 ? 0.33590 0.29428 0.38709 -0.02921 0.00700  0.00856  403 ASP B CB  
1612 C CG  . ASP A 214 ? 0.46096 0.42366 0.53557 -0.03206 0.01659  0.01063  403 ASP B CG  
1613 O OD1 . ASP A 214 ? 0.53955 0.50433 0.64223 -0.03475 0.02332  0.00950  403 ASP B OD1 
1614 O OD2 . ASP A 214 ? 0.40142 0.36548 0.47042 -0.03150 0.01706  0.01264  403 ASP B OD2 
1615 N N   . VAL A 215 ? 0.35856 0.25405 0.36230 -0.02556 0.03926  0.01802  404 VAL B N   
1616 C CA  . VAL A 215 ? 0.40136 0.26713 0.37071 -0.02216 0.04811  0.02093  404 VAL B CA  
1617 C C   . VAL A 215 ? 0.38904 0.26449 0.34530 -0.02180 0.02821  0.01747  404 VAL B C   
1618 O O   . VAL A 215 ? 0.47507 0.32125 0.39287 -0.01804 0.02521  0.01701  404 VAL B O   
1619 C CB  . VAL A 215 ? 0.39611 0.26062 0.38847 -0.02404 0.07042  0.02404  404 VAL B CB  
1620 C CG1 . VAL A 215 ? 0.40817 0.31402 0.44652 -0.02758 0.05976  0.02151  404 VAL B CG1 
1621 C CG2 . VAL A 215 ? 0.50322 0.33193 0.45449 -0.01936 0.08160  0.02648  404 VAL B CG2 
1622 N N   . SER A 216 ? 0.34884 0.26088 0.33458 -0.02585 0.01483  0.01438  405 SER B N   
1623 C CA  . SER A 216 ? 0.32900 0.25189 0.31101 -0.02798 0.00009  0.01085  405 SER B CA  
1624 C C   . SER A 216 ? 0.35099 0.26352 0.31283 -0.02405 -0.01570 0.00631  405 SER B C   
1625 O O   . SER A 216 ? 0.28347 0.19810 0.24252 -0.02617 -0.02818 0.00191  405 SER B O   
1626 C CB  . SER A 216 ? 0.34105 0.29787 0.35323 -0.03213 -0.00550 0.00936  405 SER B CB  
1627 O OG  . SER A 216 ? 0.29599 0.26491 0.32003 -0.03022 -0.00886 0.00753  405 SER B OG  
1628 N N   . ARG A 217 ? 0.34688 0.24694 0.29709 -0.01805 -0.01682 0.00661  406 ARG B N   
1629 C CA  . ARG A 217 ? 0.37091 0.25635 0.29946 -0.01042 -0.03526 0.00215  406 ARG B CA  
1630 C C   . ARG A 217 ? 0.44062 0.28615 0.32496 -0.00585 -0.04235 0.00092  406 ARG B C   
1631 O O   . ARG A 217 ? 0.38715 0.22377 0.25795 0.00022  -0.06609 -0.00553 406 ARG B O   
1632 C CB  . ARG A 217 ? 0.40210 0.27170 0.31858 -0.00339 -0.03160 0.00450  406 ARG B CB  
1633 C CG  . ARG A 217 ? 0.48263 0.32019 0.36174 0.00913  -0.04911 0.00199  406 ARG B CG  
1634 C CD  . ARG A 217 ? 0.47592 0.26423 0.31172 0.01536  -0.03226 0.00913  406 ARG B CD  
1635 N NE  . ARG A 217 ? 0.53149 0.28916 0.33250 0.02959  -0.04940 0.00767  406 ARG B NE  
1636 C CZ  . ARG A 217 ? 0.58788 0.29424 0.32954 0.04185  -0.06228 0.00754  406 ARG B CZ  
1637 N NH1 . ARG A 217 ? 0.66342 0.34149 0.37129 0.04090  -0.05831 0.00831  406 ARG B NH1 
1638 N NH2 . ARG A 217 ? 0.67047 0.34832 0.38110 0.05717  -0.08098 0.00617  406 ARG B NH2 
1639 N N   . PHE A 218 ? 0.40259 0.22246 0.26484 -0.00751 -0.02379 0.00578  407 PHE B N   
1640 C CA  . PHE A 218 ? 0.49248 0.26670 0.30398 -0.00248 -0.02835 0.00413  407 PHE B CA  
1641 C C   . PHE A 218 ? 0.46784 0.25451 0.29228 -0.01030 -0.03372 0.00012  407 PHE B C   
1642 O O   . PHE A 218 ? 0.41731 0.16397 0.19884 -0.00703 -0.03734 -0.00235 407 PHE B O   
1643 C CB  . PHE A 218 ? 0.43933 0.16590 0.20941 0.00271  0.00066  0.01196  407 PHE B CB  
1644 C CG  . PHE A 218 ? 0.54816 0.25259 0.30001 0.00921  0.01011  0.01668  407 PHE B CG  
1645 C CD1 . PHE A 218 ? 0.57073 0.23160 0.26802 0.02148  -0.00730 0.01493  407 PHE B CD1 
1646 C CD2 . PHE A 218 ? 0.50107 0.22488 0.28985 0.00351  0.03429  0.02216  407 PHE B CD2 
1647 C CE1 . PHE A 218 ? 0.62668 0.26027 0.30157 0.02814  0.00282  0.02022  407 PHE B CE1 
1648 C CE2 . PHE A 218 ? 0.50270 0.20253 0.27561 0.00769  0.04474  0.02626  407 PHE B CE2 
1649 C CZ  . PHE A 218 ? 0.53237 0.18523 0.24572 0.02010  0.03085  0.02613  407 PHE B CZ  
1650 N N   . PHE A 219 ? 0.41677 0.25094 0.29270 -0.01994 -0.03356 -0.00058 408 PHE B N   
1651 C CA  . PHE A 219 ? 0.42764 0.26986 0.31478 -0.02807 -0.03768 -0.00393 408 PHE B CA  
1652 C C   . PHE A 219 ? 0.44313 0.28172 0.32699 -0.02952 -0.06597 -0.01443 408 PHE B C   
1653 O O   . PHE A 219 ? 0.42694 0.28935 0.33580 -0.02842 -0.08249 -0.01954 408 PHE B O   
1654 C CB  . PHE A 219 ? 0.34261 0.22829 0.27727 -0.03654 -0.02983 -0.00134 408 PHE B CB  
1655 C CG  . PHE A 219 ? 0.36929 0.25832 0.31216 -0.03519 -0.00860 0.00652  408 PHE B CG  
1656 C CD1 . PHE A 219 ? 0.41235 0.27046 0.33045 -0.02938 0.00739  0.01062  408 PHE B CD1 
1657 C CD2 . PHE A 219 ? 0.34662 0.26732 0.32256 -0.03873 -0.00487 0.00900  408 PHE B CD2 
1658 C CE1 . PHE A 219 ? 0.35030 0.21726 0.29001 -0.02801 0.02545  0.01607  408 PHE B CE1 
1659 C CE2 . PHE A 219 ? 0.37373 0.29854 0.36236 -0.03610 0.00793  0.01412  408 PHE B CE2 
1660 C CZ  . PHE A 219 ? 0.31292 0.21491 0.29017 -0.03118 0.02245  0.01716  408 PHE B CZ  
1661 N N   . ASN A 220 ? 0.38181 0.19067 0.23873 -0.03162 -0.07260 -0.01891 409 ASN B N   
1662 C CA  . ASN A 220 ? 0.44253 0.24568 0.30036 -0.03414 -0.10353 -0.03137 409 ASN B CA  
1663 C C   . ASN A 220 ? 0.49139 0.33113 0.40217 -0.04998 -0.10506 -0.03593 409 ASN B C   
1664 O O   . ASN A 220 ? 0.39759 0.25563 0.32851 -0.05701 -0.08231 -0.02845 409 ASN B O   
1665 C CB  . ASN A 220 ? 0.53589 0.27700 0.32728 -0.02727 -0.11337 -0.03584 409 ASN B CB  
1666 C CG  . ASN A 220 ? 0.54657 0.24248 0.27874 -0.01051 -0.11844 -0.03390 409 ASN B CG  
1667 O OD1 . ASN A 220 ? 0.56066 0.26928 0.30343 -0.00397 -0.13580 -0.03640 409 ASN B OD1 
1668 N ND2 . ASN A 220 ? 0.62325 0.26190 0.29018 -0.00241 -0.10062 -0.02900 409 ASN B ND2 
1669 N N   . HIS A 221 ? 0.47649 0.32412 0.41039 -0.05508 -0.13290 -0.04882 410 HIS B N   
1670 C CA  . HIS A 221 ? 0.47847 0.35662 0.46630 -0.07207 -0.13303 -0.05466 410 HIS B CA  
1671 C C   . HIS A 221 ? 0.48632 0.33025 0.44821 -0.07885 -0.13528 -0.05882 410 HIS B C   
1672 O O   . HIS A 221 ? 0.47146 0.27508 0.38432 -0.06888 -0.14954 -0.06268 410 HIS B O   
1673 C CB  . HIS A 221 ? 0.43553 0.35143 0.47620 -0.07157 -0.15157 -0.06464 410 HIS B CB  
1674 C CG  . HIS A 221 ? 0.38398 0.32352 0.47250 -0.08675 -0.14764 -0.07117 410 HIS B CG  
1675 N ND1 . HIS A 221 ? 0.36429 0.33449 0.49535 -0.10048 -0.12196 -0.06670 410 HIS B ND1 
1676 C CD2 . HIS A 221 ? 0.50511 0.43705 0.60160 -0.09062 -0.16479 -0.08144 410 HIS B CD2 
1677 C CE1 . HIS A 221 ? 0.41638 0.39582 0.57860 -0.11309 -0.12124 -0.07346 410 HIS B CE1 
1678 N NE2 . HIS A 221 ? 0.41585 0.37516 0.56204 -0.10819 -0.14828 -0.08330 410 HIS B NE2 
1679 N N   . SER A 222 ? 0.41493 0.27222 0.40552 -0.09377 -0.11784 -0.05643 411 SER B N   
1680 C CA  . SER A 222 ? 0.51009 0.34187 0.48694 -0.10103 -0.11763 -0.06105 411 SER B CA  
1681 C C   . SER A 222 ? 0.50418 0.36935 0.53971 -0.11845 -0.10560 -0.06386 411 SER B C   
1682 O O   . SER A 222 ? 0.40331 0.29363 0.46699 -0.12457 -0.08461 -0.05550 411 SER B O   
1683 C CB  . SER A 222 ? 0.48049 0.26865 0.40340 -0.09794 -0.09846 -0.05149 411 SER B CB  
1684 O OG  . SER A 222 ? 0.50635 0.27139 0.41921 -0.10436 -0.09645 -0.05563 411 SER B OG  
1685 N N   . CYS A 223 ? 0.40250 0.26337 0.45181 -0.12635 -0.11726 -0.07529 412 CYS B N   
1686 C CA  . CYS A 223 ? 0.48531 0.36744 0.58160 -0.14540 -0.10136 -0.07800 412 CYS B CA  
1687 C C   . CYS A 223 ? 0.46871 0.32341 0.54469 -0.15256 -0.07520 -0.06939 412 CYS B C   
1688 O O   . CYS A 223 ? 0.45291 0.31725 0.55566 -0.16857 -0.05472 -0.06721 412 CYS B O   
1689 C CB  . CYS A 223 ? 0.58092 0.46436 0.69842 -0.15269 -0.12362 -0.09293 412 CYS B CB  
1690 S SG  . CYS A 223 ? 0.49253 0.40365 0.63525 -0.13881 -0.15821 -0.10201 412 CYS B SG  
1691 N N   . SER A 224 ? 0.52144 0.33765 0.54221 -0.14047 -0.07416 -0.06159 413 SER B N   
1692 C CA  . SER A 224 ? 0.50982 0.30097 0.50509 -0.14033 -0.05002 -0.04868 413 SER B CA  
1693 C C   . SER A 224 ? 0.51139 0.29602 0.47090 -0.12668 -0.03976 -0.03541 413 SER B C   
1694 O O   . SER A 224 ? 0.55114 0.30145 0.46290 -0.11499 -0.03730 -0.03198 413 SER B O   
1695 C CB  . SER A 224 ? 0.57477 0.32315 0.53446 -0.13937 -0.05400 -0.05339 413 SER B CB  
1696 O OG  . SER A 224 ? 0.63457 0.38838 0.63338 -0.15502 -0.05560 -0.06380 413 SER B OG  
1697 N N   . PRO A 225 ? 0.45263 0.27073 0.43741 -0.12683 -0.03107 -0.02859 414 PRO B N   
1698 C CA  . PRO A 225 ? 0.46271 0.28827 0.42693 -0.10923 -0.02288 -0.01844 414 PRO B CA  
1699 C C   . PRO A 225 ? 0.43525 0.24220 0.37517 -0.10145 -0.00260 -0.00641 414 PRO B C   
1700 O O   . PRO A 225 ? 0.45284 0.24571 0.39213 -0.10879 0.00863  -0.00282 414 PRO B O   
1701 C CB  . PRO A 225 ? 0.42300 0.29230 0.42626 -0.11068 -0.01984 -0.01642 414 PRO B CB  
1702 C CG  . PRO A 225 ? 0.35866 0.23755 0.39595 -0.12775 -0.01082 -0.01875 414 PRO B CG  
1703 C CD  . PRO A 225 ? 0.41930 0.27555 0.45790 -0.13843 -0.02454 -0.03007 414 PRO B CD  
1704 N N   . ASN A 226 ? 0.43931 0.24500 0.36142 -0.08574 0.00203  -0.00041 415 ASN B N   
1705 C CA  . ASN A 226 ? 0.45738 0.25344 0.36797 -0.07504 0.01748  0.00984  415 ASN B CA  
1706 C C   . ASN A 226 ? 0.36468 0.19203 0.29521 -0.06765 0.02183  0.01712  415 ASN B C   
1707 O O   . ASN A 226 ? 0.35348 0.17619 0.28061 -0.05792 0.02945  0.02449  415 ASN B O   
1708 C CB  . ASN A 226 ? 0.44272 0.20993 0.32428 -0.06244 0.02267  0.01003  415 ASN B CB  
1709 C CG  . ASN A 226 ? 0.47424 0.24633 0.34951 -0.05623 0.01774  0.00675  415 ASN B CG  
1710 O OD1 . ASN A 226 ? 0.47323 0.27492 0.36927 -0.05872 0.00961  0.00562  415 ASN B OD1 
1711 N ND2 . ASN A 226 ? 0.48352 0.22100 0.32552 -0.04702 0.02517  0.00561  415 ASN B ND2 
1712 N N   . ILE A 227 ? 0.39292 0.24965 0.34381 -0.07075 0.01485  0.01423  416 ILE B N   
1713 C CA  . ILE A 227 ? 0.36363 0.24605 0.33012 -0.06531 0.01712  0.01926  416 ILE B CA  
1714 C C   . ILE A 227 ? 0.35792 0.26046 0.34372 -0.07573 0.01628  0.01627  416 ILE B C   
1715 O O   . ILE A 227 ? 0.30142 0.20728 0.29984 -0.08617 0.01078  0.00886  416 ILE B O   
1716 C CB  . ILE A 227 ? 0.34466 0.24069 0.31710 -0.05573 0.01374  0.01893  416 ILE B CB  
1717 C CG1 . ILE A 227 ? 0.40844 0.31785 0.38865 -0.05998 0.00388  0.01214  416 ILE B CG1 
1718 C CG2 . ILE A 227 ? 0.39443 0.26799 0.35159 -0.04733 0.02000  0.02017  416 ILE B CG2 
1719 C CD1 . ILE A 227 ? 0.28778 0.20131 0.26693 -0.05136 0.00302  0.01240  416 ILE B CD1 
1720 N N   . ALA A 228 ? 0.30185 0.21623 0.29110 -0.07199 0.02151  0.02115  417 ALA B N   
1721 C CA  . ALA A 228 ? 0.35729 0.28646 0.36219 -0.08016 0.02774  0.01932  417 ALA B CA  
1722 C C   . ALA A 228 ? 0.35036 0.29486 0.35522 -0.07111 0.02710  0.02143  417 ALA B C   
1723 O O   . ALA A 228 ? 0.28565 0.22626 0.27838 -0.06001 0.02157  0.02511  417 ALA B O   
1724 C CB  . ALA A 228 ? 0.35396 0.26151 0.34800 -0.08840 0.04339  0.02393  417 ALA B CB  
1725 N N   . ILE A 229 ? 0.28747 0.24877 0.30954 -0.07599 0.03268  0.01789  418 ILE B N   
1726 C CA  . ILE A 229 ? 0.34500 0.31638 0.36333 -0.06774 0.03270  0.01841  418 ILE B CA  
1727 C C   . ILE A 229 ? 0.38372 0.33511 0.37405 -0.06430 0.04594  0.02438  418 ILE B C   
1728 O O   . ILE A 229 ? 0.42281 0.35943 0.40691 -0.07197 0.06330  0.02718  418 ILE B O   
1729 C CB  . ILE A 229 ? 0.35163 0.35034 0.40101 -0.07035 0.03096  0.01062  418 ILE B CB  
1730 C CG1 . ILE A 229 ? 0.38510 0.39272 0.42951 -0.05939 0.02230  0.00949  418 ILE B CG1 
1731 C CG2 . ILE A 229 ? 0.41642 0.42009 0.48153 -0.07813 0.05027  0.00915  418 ILE B CG2 
1732 C CD1 . ILE A 229 ? 0.31395 0.32226 0.35764 -0.05431 0.00751  0.00881  418 ILE B CD1 
1733 N N   . TYR A 230 ? 0.34219 0.28716 0.31180 -0.05233 0.03675  0.02631  419 TYR B N   
1734 C CA  . TYR A 230 ? 0.40098 0.31947 0.33209 -0.04517 0.04415  0.03079  419 TYR B CA  
1735 C C   . TYR A 230 ? 0.40390 0.33272 0.33368 -0.03827 0.03916  0.02576  419 TYR B C   
1736 O O   . TYR A 230 ? 0.38562 0.33403 0.33470 -0.03452 0.02259  0.02111  419 TYR B O   
1737 C CB  . TYR A 230 ? 0.46312 0.35470 0.36238 -0.03385 0.03104  0.03644  419 TYR B CB  
1738 C CG  . TYR A 230 ? 0.46222 0.33188 0.35016 -0.03777 0.03863  0.04268  419 TYR B CG  
1739 C CD1 . TYR A 230 ? 0.37233 0.25638 0.28883 -0.04497 0.03627  0.04082  419 TYR B CD1 
1740 C CD2 . TYR A 230 ? 0.52071 0.34781 0.36185 -0.03298 0.04834  0.05048  419 TYR B CD2 
1741 C CE1 . TYR A 230 ? 0.39567 0.25583 0.29948 -0.04829 0.04303  0.04561  419 TYR B CE1 
1742 C CE2 . TYR A 230 ? 0.49746 0.29989 0.32589 -0.03625 0.05589  0.05643  419 TYR B CE2 
1743 C CZ  . TYR A 230 ? 0.51908 0.33993 0.38147 -0.04434 0.05291  0.05350  419 TYR B CZ  
1744 O OH  . TYR A 230 ? 0.61074 0.40346 0.45844 -0.04745 0.06032  0.05850  419 TYR B OH  
1745 N N   . SER A 231 ? 0.39768 0.30880 0.30227 -0.03664 0.05638  0.02668  420 SER B N   
1746 C CA  . SER A 231 ? 0.47438 0.38744 0.36946 -0.02879 0.05382  0.02140  420 SER B CA  
1747 C C   . SER A 231 ? 0.47488 0.35567 0.32169 -0.01472 0.03546  0.02269  420 SER B C   
1748 O O   . SER A 231 ? 0.57419 0.41321 0.36817 -0.00814 0.04425  0.02770  420 SER B O   
1749 C CB  . SER A 231 ? 0.52002 0.42654 0.41082 -0.03223 0.08400  0.02078  420 SER B CB  
1750 O OG  . SER A 231 ? 0.68557 0.63220 0.63311 -0.04042 0.08981  0.01442  420 SER B OG  
1751 N N   . ALA A 232 ? 0.44909 0.34587 0.31361 -0.00978 0.00927  0.01769  421 ALA B N   
1752 C CA  . ALA A 232 ? 0.42796 0.30024 0.26017 0.00327  -0.01521 0.01559  421 ALA B CA  
1753 C C   . ALA A 232 ? 0.48613 0.34319 0.29020 0.01002  -0.01627 0.00901  421 ALA B C   
1754 O O   . ALA A 232 ? 0.47680 0.35829 0.31108 0.00754  -0.02159 0.00202  421 ALA B O   
1755 C CB  . ALA A 232 ? 0.35996 0.25776 0.23436 0.00371  -0.03965 0.01188  421 ALA B CB  
1756 N N   . VAL A 233 ? 0.54651 0.35660 0.28625 0.01962  -0.01009 0.01140  422 VAL B N   
1757 C CA  . VAL A 233 ? 0.58751 0.37149 0.28647 0.02762  -0.00573 0.00546  422 VAL B CA  
1758 C C   . VAL A 233 ? 0.60353 0.35043 0.25572 0.04277  -0.04142 -0.00016 422 VAL B C   
1759 O O   . VAL A 233 ? 0.66037 0.36654 0.26253 0.05280  -0.05125 0.00481  422 VAL B O   
1760 C CB  . VAL A 233 ? 0.65668 0.40665 0.31060 0.02800  0.03355  0.01166  422 VAL B CB  
1761 C CG1 . VAL A 233 ? 0.68786 0.39817 0.28480 0.03999  0.03875  0.00558  422 VAL B CG1 
1762 C CG2 . VAL A 233 ? 0.61937 0.41242 0.33392 0.01255  0.06433  0.01363  422 VAL B CG2 
1763 N N   . ARG A 234 ? 0.61880 0.37687 0.28688 0.04496  -0.06290 -0.01123 423 ARG B N   
1764 C CA  . ARG A 234 ? 0.71001 0.43367 0.33936 0.05846  -0.10093 -0.02031 423 ARG B CA  
1765 C C   . ARG A 234 ? 0.80937 0.49202 0.37950 0.06747  -0.09706 -0.02809 423 ARG B C   
1766 O O   . ARG A 234 ? 0.82006 0.47561 0.36806 0.07757  -0.12641 -0.03619 423 ARG B O   
1767 C CB  . ARG A 234 ? 0.71836 0.48371 0.41803 0.05298  -0.13322 -0.02897 423 ARG B CB  
1768 C CG  . ARG A 234 ? 0.68589 0.49577 0.44515 0.03968  -0.11865 -0.03237 423 ARG B CG  
1769 C CD  . ARG A 234 ? 0.64297 0.49859 0.47878 0.02980  -0.13013 -0.03276 423 ARG B CD  
1770 N NE  . ARG A 234 ? 0.70041 0.59038 0.58143 0.01820  -0.11075 -0.03250 423 ARG B NE  
1771 C CZ  . ARG A 234 ? 0.73566 0.63386 0.64014 0.01473  -0.11915 -0.04120 423 ARG B CZ  
1772 N NH1 . ARG A 234 ? 0.75975 0.63863 0.65434 0.01969  -0.14736 -0.05241 423 ARG B NH1 
1773 N NH2 . ARG A 234 ? 0.73017 0.65266 0.66678 0.00657  -0.10075 -0.03920 423 ARG B NH2 
1774 N N   . ASN A 235 ? 0.90361 0.58875 0.46835 0.06308  -0.05745 -0.02508 424 ASN B N   
1775 C CA  . ASN A 235 ? 1.03262 0.67668 0.54015 0.07274  -0.04601 -0.03196 424 ASN B CA  
1776 C C   . ASN A 235 ? 1.26860 0.86442 0.71606 0.07998  -0.01368 -0.02154 424 ASN B C   
1777 O O   . ASN A 235 ? 1.32426 0.91801 0.76917 0.07617  0.00222  -0.01073 424 ASN B O   
1778 C CB  . ASN A 235 ? 0.97832 0.66414 0.54052 0.06419  -0.02626 -0.03662 424 ASN B CB  
1779 C CG  . ASN A 235 ? 0.86436 0.58653 0.48397 0.05805  -0.05931 -0.04606 424 ASN B CG  
1780 O OD1 . ASN A 235 ? 0.93902 0.63539 0.53297 0.06484  -0.08530 -0.05762 424 ASN B OD1 
1781 N ND2 . ASN A 235 ? 0.71089 0.48822 0.40565 0.04491  -0.05735 -0.04153 424 ASN B ND2 
1782 N N   . HIS A 236 ? 1.64730 1.20056 1.04880 0.09071  -0.00935 -0.02492 425 HIS B N   
1783 C CA  . HIS A 236 ? 1.76887 1.26743 1.11146 0.09890  0.02015  -0.01598 425 HIS B CA  
1784 C C   . HIS A 236 ? 1.76549 1.26750 1.11551 0.09102  0.07374  -0.00567 425 HIS B C   
1785 O O   . HIS A 236 ? 1.75292 1.23388 1.08592 0.08994  0.08775  0.00388  425 HIS B O   
1786 C CB  . HIS A 236 ? 1.78253 1.24331 1.08436 0.10961  0.02273  -0.02234 425 HIS B CB  
1787 C CG  . HIS A 236 ? 1.77719 1.27490 1.11784 0.10329  0.04438  -0.02852 425 HIS B CG  
1788 N ND1 . HIS A 236 ? 1.77806 1.31857 1.16576 0.09781  0.01811  -0.03947 425 HIS B ND1 
1789 C CD2 . HIS A 236 ? 1.80717 1.30414 1.15072 0.10260  0.08970  -0.02616 425 HIS B CD2 
1790 C CE1 . HIS A 236 ? 1.75389 1.31513 1.16593 0.09564  0.04549  -0.04381 425 HIS B CE1 
1791 N NE2 . HIS A 236 ? 1.76566 1.30456 1.15564 0.09867  0.08873  -0.03596 425 HIS B NE2 
1792 N N   . GLY A 237 ? 1.47521 1.00453 0.85727 0.08551  0.10359  -0.00870 426 GLY B N   
1793 C CA  . GLY A 237 ? 1.34357 0.87954 0.74706 0.07788  0.15573  -0.00108 426 GLY B CA  
1794 C C   . GLY A 237 ? 1.21404 0.81494 0.69249 0.06800  0.17012  -0.00742 426 GLY B C   
1795 O O   . GLY A 237 ? 1.15532 0.78186 0.68020 0.06025  0.20940  -0.00493 426 GLY B O   
1796 N N   . PHE A 238 ? 1.15618 0.78219 0.65027 0.06918  0.13539  -0.01711 427 PHE B N   
1797 C CA  . PHE A 238 ? 1.05843 0.74586 0.62909 0.06143  0.13809  -0.02385 427 PHE B CA  
1798 C C   . PHE A 238 ? 0.82253 0.56405 0.46751 0.04476  0.14281  -0.01603 427 PHE B C   
1799 O O   . PHE A 238 ? 0.84088 0.59559 0.49808 0.03910  0.11284  -0.01269 427 PHE B O   
1800 C CB  . PHE A 238 ? 0.98611 0.68575 0.56737 0.06403  0.09111  -0.03347 427 PHE B CB  
1801 C CG  . PHE A 238 ? 0.84701 0.59866 0.50063 0.05917  0.08993  -0.03953 427 PHE B CG  
1802 C CD1 . PHE A 238 ? 0.81184 0.55392 0.45897 0.06822  0.11156  -0.04651 427 PHE B CD1 
1803 C CD2 . PHE A 238 ? 0.70687 0.51081 0.42905 0.04760  0.06757  -0.03818 427 PHE B CD2 
1804 C CE1 . PHE A 238 ? 0.76142 0.54660 0.47113 0.06638  0.10798  -0.05180 427 PHE B CE1 
1805 C CE2 . PHE A 238 ? 0.75444 0.59659 0.53219 0.04543  0.06526  -0.04297 427 PHE B CE2 
1806 C CZ  . PHE A 238 ? 0.73848 0.57175 0.51068 0.05517  0.08373  -0.04973 427 PHE B CZ  
1807 N N   . ARG A 239 ? 0.76421 0.53845 0.46402 0.03720  0.17850  -0.01457 428 ARG B N   
1808 C CA  . ARG A 239 ? 0.73521 0.55444 0.50158 0.02108  0.18325  -0.00876 428 ARG B CA  
1809 C C   . ARG A 239 ? 0.57924 0.46120 0.43403 0.01440  0.17967  -0.01473 428 ARG B C   
1810 O O   . ARG A 239 ? 0.50088 0.41745 0.41367 0.00246  0.19131  -0.01273 428 ARG B O   
1811 C CB  . ARG A 239 ? 0.77936 0.57502 0.53226 0.01552  0.22845  -0.00106 428 ARG B CB  
1812 C CG  . ARG A 239 ? 0.89758 0.65407 0.61389 0.02535  0.25746  -0.00157 428 ARG B CG  
1813 C CD  . ARG A 239 ? 1.05301 0.75947 0.72277 0.02389  0.27414  0.00862  428 ARG B CD  
1814 N NE  . ARG A 239 ? 1.06683 0.80334 0.80144 0.00761  0.29840  0.01233  428 ARG B NE  
1815 C CZ  . ARG A 239 ? 1.04256 0.75344 0.75843 0.00093  0.30478  0.02032  428 ARG B CZ  
1816 N NH1 . ARG A 239 ? 1.00873 0.66465 0.64383 0.01057  0.28799  0.02622  428 ARG B NH1 
1817 N NH2 . ARG A 239 ? 0.94345 0.68300 0.72330 -0.01434 0.32464  0.02101  428 ARG B NH2 
1818 N N   . THR A 240 ? 0.59604 0.48830 0.45846 0.02290  0.16206  -0.02274 429 THR B N   
1819 C CA  . THR A 240 ? 0.50320 0.44838 0.44070 0.01985  0.15146  -0.02825 429 THR B CA  
1820 C C   . THR A 240 ? 0.47993 0.44532 0.43440 0.01505  0.11135  -0.02788 429 THR B C   
1821 O O   . THR A 240 ? 0.44779 0.45182 0.45827 0.00933  0.10168  -0.02904 429 THR B O   
1822 C CB  . THR A 240 ? 0.48633 0.42956 0.42623 0.03319  0.15957  -0.03701 429 THR B CB  
1823 O OG1 . THR A 240 ? 0.50108 0.42538 0.40544 0.03996  0.12834  -0.04096 429 THR B OG1 
1824 C CG2 . THR A 240 ? 0.51431 0.41867 0.41144 0.04166  0.20031  -0.03744 429 THR B CG2 
1825 N N   . ILE A 241 ? 0.48272 0.42040 0.39057 0.01788  0.08815  -0.02697 430 ILE B N   
1826 C CA  . ILE A 241 ? 0.43973 0.39293 0.36478 0.01300  0.05589  -0.02645 430 ILE B CA  
1827 C C   . ILE A 241 ? 0.38965 0.32169 0.28213 0.00983  0.04366  -0.02065 430 ILE B C   
1828 O O   . ILE A 241 ? 0.55369 0.44652 0.39139 0.01715  0.04288  -0.02092 430 ILE B O   
1829 C CB  . ILE A 241 ? 0.46525 0.41082 0.38246 0.01995  0.03653  -0.03381 430 ILE B CB  
1830 C CG1 . ILE A 241 ? 0.44026 0.40581 0.39086 0.02530  0.04614  -0.03905 430 ILE B CG1 
1831 C CG2 . ILE A 241 ? 0.40907 0.36459 0.34251 0.01364  0.00926  -0.03260 430 ILE B CG2 
1832 C CD1 . ILE A 241 ? 0.38806 0.33857 0.32535 0.03277  0.03150  -0.04627 430 ILE B CD1 
1833 N N   . TYR A 242 ? 0.39373 0.34748 0.31611 0.00093  0.03300  -0.01591 431 TYR B N   
1834 C CA  . TYR A 242 ? 0.41905 0.35700 0.31977 -0.00083 0.02089  -0.01044 431 TYR B CA  
1835 C C   . TYR A 242 ? 0.37485 0.34001 0.31610 -0.00849 0.00649  -0.00829 431 TYR B C   
1836 O O   . TYR A 242 ? 0.34819 0.33892 0.32575 -0.01286 0.00852  -0.00978 431 TYR B O   
1837 C CB  . TYR A 242 ? 0.40273 0.32110 0.27831 -0.00291 0.04316  -0.00341 431 TYR B CB  
1838 C CG  . TYR A 242 ? 0.38275 0.32590 0.29780 -0.01159 0.06904  -0.00245 431 TYR B CG  
1839 C CD1 . TYR A 242 ? 0.31078 0.28112 0.26783 -0.02233 0.06611  -0.00003 431 TYR B CD1 
1840 C CD2 . TYR A 242 ? 0.40231 0.34088 0.31568 -0.00858 0.09586  -0.00534 431 TYR B CD2 
1841 C CE1 . TYR A 242 ? 0.32804 0.32208 0.32764 -0.03068 0.08417  -0.00166 431 TYR B CE1 
1842 C CE2 . TYR A 242 ? 0.44321 0.40977 0.40652 -0.01684 0.11791  -0.00640 431 TYR B CE2 
1843 C CZ  . TYR A 242 ? 0.37159 0.36677 0.37965 -0.02831 0.10943  -0.00512 431 TYR B CZ  
1844 O OH  . TYR A 242 ? 0.42882 0.45267 0.49250 -0.03692 0.12612  -0.00854 431 TYR B OH  
1845 N N   . ASP A 243 ? 0.36297 0.31846 0.29479 -0.00818 -0.00836 -0.00511 432 ASP B N   
1846 C CA  . ASP A 243 ? 0.34566 0.32074 0.31111 -0.01399 -0.01777 -0.00285 432 ASP B CA  
1847 C C   . ASP A 243 ? 0.35811 0.34190 0.33563 -0.02158 -0.00399 0.00284  432 ASP B C   
1848 O O   . ASP A 243 ? 0.29615 0.26356 0.25165 -0.02220 0.00617  0.00752  432 ASP B O   
1849 C CB  . ASP A 243 ? 0.36436 0.32852 0.32431 -0.00971 -0.03714 -0.00258 432 ASP B CB  
1850 C CG  . ASP A 243 ? 0.42251 0.37759 0.37625 -0.00373 -0.05553 -0.01056 432 ASP B CG  
1851 O OD1 . ASP A 243 ? 0.38738 0.35020 0.35214 -0.00515 -0.05360 -0.01564 432 ASP B OD1 
1852 O OD2 . ASP A 243 ? 0.53228 0.47029 0.47019 0.00303  -0.07427 -0.01258 432 ASP B OD2 
1853 N N   . LEU A 244 ? 0.26232 0.26616 0.27031 -0.02705 -0.00426 0.00209  433 LEU B N   
1854 C CA  . LEU A 244 ? 0.31008 0.31989 0.33050 -0.03465 0.00310  0.00523  433 LEU B CA  
1855 C C   . LEU A 244 ? 0.32262 0.32612 0.34314 -0.03501 -0.00451 0.00907  433 LEU B C   
1856 O O   . LEU A 244 ? 0.28138 0.29052 0.31579 -0.03605 -0.00892 0.00831  433 LEU B O   
1857 C CB  . LEU A 244 ? 0.26574 0.29405 0.31227 -0.03777 0.00305  0.00077  433 LEU B CB  
1858 C CG  . LEU A 244 ? 0.26600 0.30577 0.32438 -0.03566 0.01108  -0.00427 433 LEU B CG  
1859 C CD1 . LEU A 244 ? 0.25118 0.30803 0.33697 -0.03502 0.00271  -0.00950 433 LEU B CD1 
1860 C CD2 . LEU A 244 ? 0.24231 0.27986 0.30152 -0.04104 0.03021  -0.00286 433 LEU B CD2 
1861 N N   . ALA A 245 ? 0.31390 0.30096 0.31523 -0.03250 -0.00445 0.01349  434 ALA B N   
1862 C CA  . ALA A 245 ? 0.31481 0.29576 0.31946 -0.02973 -0.01152 0.01664  434 ALA B CA  
1863 C C   . ALA A 245 ? 0.34290 0.31843 0.34817 -0.03604 -0.00283 0.02012  434 ALA B C   
1864 O O   . ALA A 245 ? 0.32834 0.29372 0.32052 -0.04087 0.00691  0.02258  434 ALA B O   
1865 C CB  . ALA A 245 ? 0.32994 0.29263 0.31275 -0.02065 -0.02095 0.01880  434 ALA B CB  
1866 N N   . PHE A 246 ? 0.31119 0.28912 0.32976 -0.03630 -0.00430 0.01997  435 PHE B N   
1867 C CA  . PHE A 246 ? 0.30538 0.27174 0.31903 -0.04078 0.00184  0.02202  435 PHE B CA  
1868 C C   . PHE A 246 ? 0.30791 0.25863 0.31373 -0.03421 0.00173  0.02688  435 PHE B C   
1869 O O   . PHE A 246 ? 0.27046 0.22509 0.29029 -0.02628 -0.00335 0.02695  435 PHE B O   
1870 C CB  . PHE A 246 ? 0.35828 0.32504 0.37867 -0.04203 0.00215  0.01924  435 PHE B CB  
1871 C CG  . PHE A 246 ? 0.34927 0.32558 0.37368 -0.04667 -0.00150 0.01415  435 PHE B CG  
1872 C CD1 . PHE A 246 ? 0.32024 0.29500 0.34466 -0.05432 -0.00241 0.01094  435 PHE B CD1 
1873 C CD2 . PHE A 246 ? 0.32544 0.31137 0.35720 -0.04297 -0.00550 0.01170  435 PHE B CD2 
1874 C CE1 . PHE A 246 ? 0.32886 0.31509 0.36471 -0.05649 -0.01001 0.00473  435 PHE B CE1 
1875 C CE2 . PHE A 246 ? 0.36480 0.35763 0.40016 -0.04418 -0.01130 0.00688  435 PHE B CE2 
1876 C CZ  . PHE A 246 ? 0.37044 0.36517 0.40991 -0.05008 -0.01495 0.00305  435 PHE B CZ  
1877 N N   . PHE A 247 ? 0.31244 0.24513 0.30012 -0.03739 0.00768  0.03045  436 PHE B N   
1878 C CA  . PHE A 247 ? 0.31818 0.23049 0.29399 -0.02965 0.00743  0.03547  436 PHE B CA  
1879 C C   . PHE A 247 ? 0.31597 0.21070 0.28355 -0.03586 0.01636  0.03606  436 PHE B C   
1880 O O   . PHE A 247 ? 0.37527 0.26804 0.33975 -0.04798 0.02157  0.03344  436 PHE B O   
1881 C CB  . PHE A 247 ? 0.33231 0.22542 0.28064 -0.02504 0.00616  0.04039  436 PHE B CB  
1882 C CG  . PHE A 247 ? 0.39228 0.29051 0.33982 -0.01337 -0.00894 0.03936  436 PHE B CG  
1883 C CD1 . PHE A 247 ? 0.33027 0.24023 0.27650 -0.01585 -0.01091 0.03568  436 PHE B CD1 
1884 C CD2 . PHE A 247 ? 0.36938 0.25939 0.31928 0.00105  -0.02333 0.04075  436 PHE B CD2 
1885 C CE1 . PHE A 247 ? 0.33657 0.24603 0.27797 -0.00533 -0.02769 0.03299  436 PHE B CE1 
1886 C CE2 . PHE A 247 ? 0.34147 0.23492 0.29323 0.01175  -0.04302 0.03743  436 PHE B CE2 
1887 C CZ  . PHE A 247 ? 0.34321 0.24442 0.28777 0.00798  -0.04561 0.03334  436 PHE B CZ  
1888 N N   . ALA A 248 ? 0.30209 0.18375 0.26950 -0.02713 0.01735  0.03826  437 ALA B N   
1889 C CA  . ALA A 248 ? 0.34089 0.19903 0.29455 -0.03106 0.02570  0.03809  437 ALA B CA  
1890 C C   . ALA A 248 ? 0.34656 0.17849 0.27582 -0.03546 0.03031  0.04251  437 ALA B C   
1891 O O   . ALA A 248 ? 0.40466 0.22255 0.32117 -0.02515 0.02797  0.04847  437 ALA B O   
1892 C CB  . ALA A 248 ? 0.35678 0.20685 0.31852 -0.01840 0.02956  0.03906  437 ALA B CB  
1893 N N   . ILE A 249 ? 0.38133 0.16273 0.32033 -0.02098 0.14053  0.04884  438 ILE B N   
1894 C CA  . ILE A 249 ? 0.45294 0.22761 0.41506 -0.00996 0.16587  0.05677  438 ILE B CA  
1895 C C   . ILE A 249 ? 0.42371 0.17443 0.39444 -0.01011 0.18398  0.04885  438 ILE B C   
1896 O O   . ILE A 249 ? 0.45355 0.19321 0.44469 -0.00147 0.20954  0.05446  438 ILE B O   
1897 C CB  . ILE A 249 ? 0.45548 0.22777 0.43920 -0.02573 0.16183  0.04321  438 ILE B CB  
1898 C CG1 . ILE A 249 ? 0.47862 0.24505 0.46518 -0.05290 0.13461  0.01199  438 ILE B CG1 
1899 C CG2 . ILE A 249 ? 0.37771 0.17125 0.35413 -0.01830 0.15731  0.05693  438 ILE B CG2 
1900 C CD1 . ILE A 249 ? 0.45646 0.23157 0.47095 -0.06663 0.12520  -0.00117 438 ILE B CD1 
1901 N N   . LYS A 250 ? 0.47142 0.21205 0.42598 -0.01929 0.17481  0.03602  439 LYS B N   
1902 C CA  . LYS A 250 ? 0.49917 0.21576 0.45523 -0.01862 0.19537  0.02836  439 LYS B CA  
1903 C C   . LYS A 250 ? 0.47849 0.19575 0.41531 -0.00918 0.19595  0.03534  439 LYS B C   
1904 O O   . LYS A 250 ? 0.54106 0.27528 0.46288 -0.01257 0.17435  0.03797  439 LYS B O   
1905 C CB  . LYS A 250 ? 0.48364 0.18471 0.44013 -0.04522 0.18416  -0.00178 439 LYS B CB  
1906 C CG  . LYS A 250 ? 0.47214 0.17753 0.45618 -0.05640 0.18133  -0.00998 439 LYS B CG  
1907 C CD  . LYS A 250 ? 0.49851 0.19536 0.48564 -0.07979 0.16557  -0.03830 439 LYS B CD  
1908 C CE  . LYS A 250 ? 0.66935 0.35401 0.69076 -0.08636 0.18664  -0.04506 439 LYS B CE  
1909 N NZ  . LYS A 250 ? 0.83873 0.49766 0.86568 -0.07397 0.22748  -0.03636 439 LYS B NZ  
1910 N N   . ASP A 251 ? 0.48638 0.18501 0.42700 0.00251  0.22386  0.03863  440 ASP B N   
1911 C CA  . ASP A 251 ? 0.52978 0.22739 0.45814 0.01287  0.23014  0.04520  440 ASP B CA  
1912 C C   . ASP A 251 ? 0.54840 0.23039 0.44838 -0.01182 0.21338  0.02023  440 ASP B C   
1913 O O   . ASP A 251 ? 0.67878 0.33482 0.56827 -0.02675 0.22104  -0.00065 440 ASP B O   
1914 C CB  . ASP A 251 ? 0.53230 0.21033 0.47407 0.03249  0.26891  0.05398  440 ASP B CB  
1915 C CG  . ASP A 251 ? 0.60961 0.30651 0.57754 0.06319  0.28546  0.08357  440 ASP B CG  
1916 O OD1 . ASP A 251 ? 0.54868 0.28319 0.51875 0.07685  0.26620  0.10419  440 ASP B OD1 
1917 O OD2 . ASP A 251 ? 0.66355 0.34030 0.64797 0.07327  0.31861  0.08707  440 ASP B OD2 
1918 N N   . ILE A 252 ? 0.57850 0.27918 0.46536 -0.01620 0.19027  0.02366  441 ILE B N   
1919 C CA  . ILE A 252 ? 0.56994 0.25860 0.42708 -0.03645 0.17281  0.00397  441 ILE B CA  
1920 C C   . ILE A 252 ? 0.60540 0.28384 0.45050 -0.02746 0.19163  0.01039  441 ILE B C   
1921 O O   . ILE A 252 ? 0.63028 0.33819 0.49228 -0.01282 0.19306  0.03191  441 ILE B O   
1922 C CB  . ILE A 252 ? 0.54858 0.26124 0.40113 -0.04773 0.13918  0.00343  441 ILE B CB  
1923 C CG1 . ILE A 252 ? 0.55804 0.27899 0.42368 -0.05665 0.12234  -0.00601 441 ILE B CG1 
1924 C CG2 . ILE A 252 ? 0.56005 0.26313 0.38197 -0.06195 0.12435  -0.00968 441 ILE B CG2 
1925 C CD1 . ILE A 252 ? 0.52656 0.27124 0.39500 -0.06157 0.09666  -0.00257 441 ILE B CD1 
1926 N N   . GLN A 253 ? 0.58705 0.23073 0.40478 -0.03644 0.20571  -0.00756 442 GLN B N   
1927 C CA  . GLN A 253 ? 0.69437 0.31911 0.49536 -0.02858 0.22973  -0.00434 442 GLN B CA  
1928 C C   . GLN A 253 ? 0.65208 0.27833 0.42345 -0.04163 0.21097  -0.00810 442 GLN B C   
1929 O O   . GLN A 253 ? 0.61736 0.25004 0.37391 -0.05815 0.18026  -0.01813 442 GLN B O   
1930 C CB  . GLN A 253 ? 0.76335 0.34799 0.54311 -0.03393 0.25749  -0.02056 442 GLN B CB  
1931 C CG  . GLN A 253 ? 0.74306 0.32211 0.55433 -0.01278 0.29422  -0.00709 442 GLN B CG  
1932 C CD  . GLN A 253 ? 0.79937 0.34906 0.60524 -0.02687 0.30948  -0.02389 442 GLN B CD  
1933 O OE1 . GLN A 253 ? 0.97938 0.51986 0.76387 -0.05019 0.28649  -0.04815 442 GLN B OE1 
1934 N NE2 . GLN A 253 ? 0.84146 0.37972 0.67174 -0.01089 0.34634  -0.01130 442 GLN B NE2 
1935 N N   . PRO A 254 ? 0.67956 0.30731 0.44868 -0.03196 0.22817  0.00191  443 PRO B N   
1936 C CA  . PRO A 254 ? 0.67847 0.31191 0.42283 -0.04272 0.21412  0.00106  443 PRO B CA  
1937 C C   . PRO A 254 ? 0.73343 0.31710 0.41222 -0.06260 0.20933  -0.02175 443 PRO B C   
1938 O O   . PRO A 254 ? 0.69115 0.23985 0.34594 -0.06571 0.22295  -0.03990 443 PRO B O   
1939 C CB  . PRO A 254 ? 0.63012 0.27346 0.39212 -0.02587 0.23934  0.01374  443 PRO B CB  
1940 C CG  . PRO A 254 ? 0.58697 0.25550 0.39880 -0.00490 0.25291  0.03038  443 PRO B CG  
1941 C CD  . PRO A 254 ? 0.66086 0.29978 0.46390 -0.00712 0.25639  0.01910  443 PRO B CD  
1942 N N   . LEU A 255 ? 0.68757 0.28502 0.34893 -0.07294 0.18126  -0.02154 444 LEU B N   
1943 C CA  . LEU A 255 ? 0.66649 0.23834 0.27147 -0.08557 0.16256  -0.04050 444 LEU B CA  
1944 C C   . LEU A 255 ? 0.63028 0.21523 0.24909 -0.09506 0.13353  -0.05549 444 LEU B C   
1945 O O   . LEU A 255 ? 0.69383 0.27948 0.28779 -0.10180 0.11190  -0.06692 444 LEU B O   
1946 C CB  . LEU A 255 ? 0.80271 0.34489 0.36797 -0.08187 0.18396  -0.04667 444 LEU B CB  
1947 C CG  . LEU A 255 ? 0.71473 0.26168 0.29061 -0.06777 0.21170  -0.02813 444 LEU B CG  
1948 C CD1 . LEU A 255 ? 0.78273 0.29744 0.31908 -0.06336 0.23152  -0.03677 444 LEU B CD1 
1949 C CD2 . LEU A 255 ? 0.68827 0.26497 0.27507 -0.06861 0.19472  -0.01111 444 LEU B CD2 
1950 N N   . GLU A 256 ? 0.64811 0.25439 0.31397 -0.09199 0.13249  -0.05285 445 GLU B N   
1951 C CA  . GLU A 256 ? 0.68303 0.31253 0.37475 -0.09817 0.10824  -0.06374 445 GLU B CA  
1952 C C   . GLU A 256 ? 0.61984 0.28117 0.32695 -0.10100 0.07468  -0.05800 445 GLU B C   
1953 O O   . GLU A 256 ? 0.50214 0.17711 0.22481 -0.09673 0.07306  -0.04427 445 GLU B O   
1954 C CB  . GLU A 256 ? 0.61287 0.24746 0.34583 -0.09118 0.12672  -0.06081 445 GLU B CB  
1955 C CG  . GLU A 256 ? 0.61731 0.27019 0.38151 -0.09764 0.10872  -0.07211 445 GLU B CG  
1956 C CD  . GLU A 256 ? 0.68265 0.33280 0.48258 -0.08984 0.13293  -0.06581 445 GLU B CD  
1957 O OE1 . GLU A 256 ? 0.72141 0.34837 0.51766 -0.08126 0.16597  -0.06092 445 GLU B OE1 
1958 O OE2 . GLU A 256 ? 0.66083 0.33084 0.49284 -0.09032 0.12173  -0.06370 445 GLU B OE2 
1959 N N   . GLU A 257 ? 0.56852 0.24365 0.27625 -0.10688 0.04840  -0.06941 446 GLU B N   
1960 C CA  . GLU A 257 ? 0.61848 0.32205 0.34311 -0.10648 0.01999  -0.06337 446 GLU B CA  
1961 C C   . GLU A 257 ? 0.57871 0.30993 0.35374 -0.10183 0.01744  -0.05817 446 GLU B C   
1962 O O   . GLU A 257 ? 0.49947 0.23221 0.29967 -0.10211 0.02583  -0.06542 446 GLU B O   
1963 C CB  . GLU A 257 ? 0.55184 0.26474 0.26886 -0.11056 -0.00459 -0.07779 446 GLU B CB  
1964 C CG  . GLU A 257 ? 0.60264 0.33168 0.31801 -0.10816 -0.02906 -0.06845 446 GLU B CG  
1965 C CD  . GLU A 257 ? 0.66647 0.41748 0.39329 -0.10956 -0.05411 -0.08328 446 GLU B CD  
1966 O OE1 . GLU A 257 ? 0.67532 0.42814 0.40623 -0.11434 -0.05473 -0.10434 446 GLU B OE1 
1967 O OE2 . GLU A 257 ? 0.53823 0.30426 0.27144 -0.10618 -0.07305 -0.07543 446 GLU B OE2 
1968 N N   . LEU A 258 ? 0.51136 0.26084 0.29919 -0.09783 0.00730  -0.04615 447 LEU B N   
1969 C CA  . LEU A 258 ? 0.51514 0.28954 0.34268 -0.09272 0.00379  -0.04209 447 LEU B CA  
1970 C C   . LEU A 258 ? 0.50625 0.30215 0.35820 -0.09285 -0.01649 -0.04946 447 LEU B C   
1971 O O   . LEU A 258 ? 0.43251 0.23394 0.27513 -0.09297 -0.03275 -0.04860 447 LEU B O   
1972 C CB  . LEU A 258 ? 0.53157 0.31630 0.36286 -0.08922 0.00228  -0.03047 447 LEU B CB  
1973 C CG  . LEU A 258 ? 0.53965 0.30667 0.35413 -0.08968 0.02141  -0.02318 447 LEU B CG  
1974 C CD1 . LEU A 258 ? 0.46621 0.25057 0.29603 -0.08993 0.01524  -0.01530 447 LEU B CD1 
1975 C CD2 . LEU A 258 ? 0.55505 0.30816 0.37506 -0.08481 0.04616  -0.02125 447 LEU B CD2 
1976 N N   . THR A 259 ? 0.47966 0.28304 0.36245 -0.09323 -0.01309 -0.05583 448 THR B N   
1977 C CA  . THR A 259 ? 0.46820 0.29110 0.38103 -0.09464 -0.02870 -0.06543 448 THR B CA  
1978 C C   . THR A 259 ? 0.42258 0.25353 0.36840 -0.09250 -0.02166 -0.06149 448 THR B C   
1979 O O   . THR A 259 ? 0.43949 0.25568 0.38339 -0.09213 -0.00272 -0.05427 448 THR B O   
1980 C CB  . THR A 259 ? 0.45440 0.27170 0.37148 -0.10271 -0.03476 -0.08394 448 THR B CB  
1981 O OG1 . THR A 259 ? 0.44428 0.24042 0.36570 -0.10637 -0.01625 -0.08624 448 THR B OG1 
1982 C CG2 . THR A 259 ? 0.53998 0.34726 0.41459 -0.10569 -0.04391 -0.08903 448 THR B CG2 
1983 N N   . PHE A 260 ? 0.36599 0.21692 0.33765 -0.09174 -0.03316 -0.06549 449 PHE B N   
1984 C CA  . PHE A 260 ? 0.40695 0.26029 0.40670 -0.09207 -0.02736 -0.06179 449 PHE B CA  
1985 C C   . PHE A 260 ? 0.38534 0.25398 0.42036 -0.09673 -0.03956 -0.07279 449 PHE B C   
1986 O O   . PHE A 260 ? 0.33520 0.22193 0.36602 -0.10195 -0.04581 -0.08666 449 PHE B O   
1987 C CB  . PHE A 260 ? 0.34096 0.20134 0.33184 -0.08598 -0.02512 -0.05253 449 PHE B CB  
1988 C CG  . PHE A 260 ? 0.37068 0.25020 0.36598 -0.08349 -0.03843 -0.05707 449 PHE B CG  
1989 C CD1 . PHE A 260 ? 0.39640 0.27731 0.36902 -0.08003 -0.04832 -0.05377 449 PHE B CD1 
1990 C CD2 . PHE A 260 ? 0.39737 0.28565 0.41308 -0.08642 -0.03872 -0.06063 449 PHE B CD2 
1991 C CE1 . PHE A 260 ? 0.38549 0.27342 0.35843 -0.07759 -0.06042 -0.05236 449 PHE B CE1 
1992 C CE2 . PHE A 260 ? 0.35315 0.25097 0.36638 -0.08368 -0.05225 -0.05991 449 PHE B CE2 
1993 C CZ  . PHE A 260 ? 0.32820 0.22488 0.32240 -0.07835 -0.06326 -0.05562 449 PHE B CZ  
1994 N N   . ASP A 261 ? 0.45082 0.30299 0.48796 -0.10676 -0.03590 -0.06223 450 ASP B N   
1995 C CA  . ASP A 261 ? 0.39453 0.25483 0.44436 -0.12323 -0.03978 -0.06853 450 ASP B CA  
1996 C C   . ASP A 261 ? 0.38387 0.26842 0.44163 -0.12055 -0.04320 -0.06994 450 ASP B C   
1997 O O   . ASP A 261 ? 0.33109 0.21897 0.40499 -0.11008 -0.03329 -0.06356 450 ASP B O   
1998 C CB  . ASP A 261 ? 0.43468 0.29697 0.52775 -0.12495 -0.01058 -0.06902 450 ASP B CB  
1999 C CG  . ASP A 261 ? 0.45868 0.33910 0.59268 -0.13784 -0.01438 -0.08053 450 ASP B CG  
2000 O OD1 . ASP A 261 ? 0.41960 0.32034 0.55585 -0.14277 -0.03774 -0.08745 450 ASP B OD1 
2001 O OD2 . ASP A 261 ? 0.59930 0.47620 0.76764 -0.14253 0.00899  -0.08273 450 ASP B OD2 
2002 N N   . TYR A 262 ? 0.40205 0.30943 0.46500 -0.12382 -0.05879 -0.08047 451 TYR B N   
2003 C CA  . TYR A 262 ? 0.37652 0.30438 0.46346 -0.11180 -0.07286 -0.07769 451 TYR B CA  
2004 C C   . TYR A 262 ? 0.41699 0.35885 0.55876 -0.11055 -0.06674 -0.07707 451 TYR B C   
2005 O O   . TYR A 262 ? 0.34385 0.29270 0.50558 -0.09946 -0.06742 -0.07379 451 TYR B O   
2006 C CB  . TYR A 262 ? 0.38028 0.32613 0.46853 -0.11082 -0.09903 -0.08317 451 TYR B CB  
2007 C CG  . TYR A 262 ? 0.38803 0.32263 0.43464 -0.10328 -0.10648 -0.07992 451 TYR B CG  
2008 C CD1 . TYR A 262 ? 0.37321 0.28955 0.39311 -0.09854 -0.08878 -0.07527 451 TYR B CD1 
2009 C CD2 . TYR A 262 ? 0.41400 0.35645 0.45211 -0.09909 -0.13369 -0.07905 451 TYR B CD2 
2010 C CE1 . TYR A 262 ? 0.36853 0.27250 0.35587 -0.09175 -0.09605 -0.06885 451 TYR B CE1 
2011 C CE2 . TYR A 262 ? 0.41093 0.33524 0.40801 -0.09252 -0.14109 -0.07169 451 TYR B CE2 
2012 C CZ  . TYR A 262 ? 0.40563 0.30936 0.37814 -0.09007 -0.12086 -0.06639 451 TYR B CZ  
2013 O OH  . TYR A 262 ? 0.39073 0.27308 0.32377 -0.08596 -0.12724 -0.05706 451 TYR B OH  
2014 N N   . ALA A 263 ? 0.39968 0.34664 0.57279 -0.12153 -0.05711 -0.08219 452 ALA B N   
2015 C CA  . ALA A 263 ? 0.33766 0.30111 0.57303 -0.11987 -0.03922 -0.08180 452 ALA B CA  
2016 C C   . ALA A 263 ? 0.37334 0.32082 0.60704 -0.11066 -0.00980 -0.07165 452 ALA B C   
2017 O O   . ALA A 263 ? 0.40287 0.36218 0.67311 -0.10336 0.00363  -0.06899 452 ALA B O   
2018 C CB  . ALA A 263 ? 0.36497 0.33436 0.63420 -0.13422 -0.02972 -0.08943 452 ALA B CB  
2019 N N   . GLY A 264 ? 0.48076 0.40266 0.67872 -0.11124 0.00494  -0.06569 453 GLY B N   
2020 C CA  . GLY A 264 ? 0.50341 0.41014 0.69576 -0.10207 0.03642  -0.05372 453 GLY B CA  
2021 C C   . GLY A 264 ? 0.72190 0.62208 0.94513 -0.10203 0.07589  -0.04293 453 GLY B C   
2022 O O   . GLY A 264 ? 0.78828 0.70162 1.05411 -0.09912 0.09717  -0.03752 453 GLY B O   
2023 N N   . ALA A 265 ? 0.73334 0.61295 0.93664 -0.10278 0.08909  -0.03772 454 ALA B N   
2024 C CA  . ALA A 265 ? 0.86714 0.73822 1.09993 -0.10010 0.12684  -0.02703 454 ALA B CA  
2025 C C   . ALA A 265 ? 0.82490 0.67381 1.02931 -0.08192 0.16200  -0.00221 454 ALA B C   
2026 O O   . ALA A 265 ? 0.91480 0.75485 1.13851 -0.07381 0.19487  0.01037  454 ALA B O   
2027 C CB  . ALA A 265 ? 0.75621 0.62317 1.00386 -0.11536 0.11731  -0.04313 454 ALA B CB  
2028 N N   . ARG A 285 ? 1.08855 1.21790 1.13850 -0.08210 -0.31813 -0.09512 474 ARG B N   
2029 C CA  . ARG A 285 ? 1.06834 1.24092 1.09665 -0.07777 -0.35037 -0.09779 474 ARG B CA  
2030 C C   . ARG A 285 ? 1.04132 1.24293 1.06639 -0.10598 -0.35475 -0.12858 474 ARG B C   
2031 O O   . ARG A 285 ? 1.04083 1.21570 1.02146 -0.11972 -0.33940 -0.14379 474 ARG B O   
2032 C CB  . ARG A 285 ? 1.09163 1.23739 1.04477 -0.05976 -0.35742 -0.08035 474 ARG B CB  
2033 C CG  . ARG A 285 ? 0.97911 1.07295 0.88301 -0.07054 -0.32965 -0.08870 474 ARG B CG  
2034 C CD  . ARG A 285 ? 0.96379 1.02654 0.79744 -0.05106 -0.33367 -0.06566 474 ARG B CD  
2035 N NE  . ARG A 285 ? 0.92383 0.94696 0.71098 -0.06170 -0.30993 -0.07627 474 ARG B NE  
2036 C CZ  . ARG A 285 ? 0.99033 0.98003 0.71332 -0.04961 -0.30540 -0.05888 474 ARG B CZ  
2037 N NH1 . ARG A 285 ? 1.04741 1.03509 0.74140 -0.02609 -0.32034 -0.02800 474 ARG B NH1 
2038 N NH2 . ARG A 285 ? 0.93805 0.89512 0.62698 -0.05985 -0.28234 -0.07025 474 ARG B NH2 
2039 N N   . ARG A 286 ? 1.09114 1.34679 1.16706 -0.11531 -0.37574 -0.13733 475 ARG B N   
2040 C CA  . ARG A 286 ? 1.05005 1.33472 1.12987 -0.14663 -0.38701 -0.16492 475 ARG B CA  
2041 C C   . ARG A 286 ? 1.03280 1.26721 1.10916 -0.17222 -0.34921 -0.18239 475 ARG B C   
2042 O O   . ARG A 286 ? 0.99897 1.21079 1.11630 -0.17204 -0.32316 -0.17649 475 ARG B O   
2043 C CB  . ARG A 286 ? 1.09962 1.40209 1.11154 -0.14788 -0.41299 -0.17083 475 ARG B CB  
2044 N N   . GLN A 287 ? 0.78401 0.80499 1.26130 -0.08372 -0.27608 0.01947  476 GLN B N   
2045 C CA  . GLN A 287 ? 0.65815 0.67906 1.09768 -0.09701 -0.26203 0.02107  476 GLN B CA  
2046 C C   . GLN A 287 ? 0.62664 0.62630 0.99689 -0.09524 -0.23979 -0.00437 476 GLN B C   
2047 O O   . GLN A 287 ? 0.58405 0.55110 0.90756 -0.08649 -0.23579 -0.02182 476 GLN B O   
2048 C CB  . GLN A 287 ? 0.59259 0.55990 0.98152 -0.10738 -0.29193 0.03640  476 GLN B CB  
2049 C CG  . GLN A 287 ? 0.78130 0.77089 1.23831 -0.11550 -0.31256 0.06519  476 GLN B CG  
2050 C CD  . GLN A 287 ? 0.84041 0.77313 1.27216 -0.11424 -0.35280 0.07416  476 GLN B CD  
2051 O OE1 . GLN A 287 ? 0.70469 0.63311 1.15869 -0.10461 -0.36422 0.07239  476 GLN B OE1 
2052 N NE2 . GLN A 287 ? 0.93805 0.82278 1.32263 -0.12260 -0.37747 0.08380  476 GLN B NE2 
2053 N N   . CYS A 288 ? 0.58264 0.59953 0.94085 -0.10192 -0.22138 -0.00291 477 CYS B N   
2054 C CA  . CYS A 288 ? 0.51420 0.51232 0.80306 -0.09684 -0.19785 -0.02461 477 CYS B CA  
2055 C C   . CYS A 288 ? 0.52166 0.46195 0.73318 -0.10274 -0.21804 -0.02945 477 CYS B C   
2056 O O   . CYS A 288 ? 0.55902 0.47962 0.75771 -0.10892 -0.23647 -0.01379 477 CYS B O   
2057 C CB  . CYS A 288 ? 0.42044 0.45714 0.72152 -0.09784 -0.17027 -0.01909 477 CYS B CB  
2058 S SG  . CYS A 288 ? 0.35510 0.37395 0.58022 -0.08960 -0.14504 -0.04488 477 CYS B SG  
2059 N N   . LYS A 289 ? 0.48822 0.40478 0.64361 -0.09427 -0.20591 -0.04893 478 LYS B N   
2060 C CA  . LYS A 289 ? 0.56234 0.43926 0.64395 -0.09016 -0.20929 -0.05308 478 LYS B CA  
2061 C C   . LYS A 289 ? 0.59725 0.47822 0.64187 -0.08594 -0.18937 -0.06863 478 LYS B C   
2062 O O   . LYS A 289 ? 0.54301 0.40717 0.53797 -0.07890 -0.18185 -0.07883 478 LYS B O   
2063 C CB  . LYS A 289 ? 0.61606 0.47002 0.66786 -0.08604 -0.21080 -0.05741 478 LYS B CB  
2064 C CG  . LYS A 289 ? 0.68859 0.53000 0.76941 -0.08784 -0.23551 -0.04211 478 LYS B CG  
2065 C CD  . LYS A 289 ? 0.76530 0.57853 0.83245 -0.08963 -0.26461 -0.02568 478 LYS B CD  
2066 C CE  . LYS A 289 ? 0.71184 0.49805 0.78393 -0.08927 -0.29294 -0.01254 478 LYS B CE  
2067 N NZ  . LYS A 289 ? 0.71915 0.53561 0.86299 -0.08872 -0.29350 -0.00923 478 LYS B NZ  
2068 N N   . CYS A 290 ? 0.49946 0.40531 0.57144 -0.09029 -0.18209 -0.06959 479 CYS B N   
2069 C CA  . CYS A 290 ? 0.47892 0.38593 0.51588 -0.08463 -0.16725 -0.08378 479 CYS B CA  
2070 C C   . CYS A 290 ? 0.60784 0.48466 0.60095 -0.07984 -0.17849 -0.07975 479 CYS B C   
2071 O O   . CYS A 290 ? 0.67224 0.54479 0.62818 -0.06884 -0.16673 -0.09307 479 CYS B O   
2072 C CB  . CYS A 290 ? 0.40476 0.34311 0.47484 -0.08839 -0.15585 -0.08202 479 CYS B CB  
2073 S SG  . CYS A 290 ? 0.51789 0.45817 0.61675 -0.10552 -0.17517 -0.05340 479 CYS B SG  
2074 N N   . GLY A 291 ? 0.56798 0.42410 0.56951 -0.08630 -0.20287 -0.06159 480 GLY B N   
2075 C CA  . GLY A 291 ? 0.62570 0.44317 0.58506 -0.07887 -0.21926 -0.05914 480 GLY B CA  
2076 C C   . GLY A 291 ? 0.60231 0.41355 0.55649 -0.08106 -0.22392 -0.05605 480 GLY B C   
2077 O O   . GLY A 291 ? 0.64532 0.42033 0.56191 -0.07086 -0.23769 -0.05722 480 GLY B O   
2078 N N   . SER A 292 ? 0.54282 0.38430 0.53122 -0.09365 -0.21539 -0.05186 481 SER B N   
2079 C CA  . SER A 292 ? 0.65159 0.48199 0.63311 -0.10032 -0.22484 -0.04386 481 SER B CA  
2080 C C   . SER A 292 ? 0.69690 0.50496 0.70073 -0.11755 -0.25551 -0.01478 481 SER B C   
2081 O O   . SER A 292 ? 0.64586 0.46555 0.69002 -0.12824 -0.26496 0.00137  481 SER B O   
2082 C CB  . SER A 292 ? 0.58824 0.45617 0.59618 -0.11228 -0.20970 -0.04508 481 SER B CB  
2083 O OG  . SER A 292 ? 0.60782 0.48837 0.58881 -0.09408 -0.18606 -0.07255 481 SER B OG  
2084 N N   . ALA A 293 ? 0.69987 0.47429 0.67904 -0.11954 -0.27346 -0.00663 482 ALA B N   
2085 C CA  . ALA A 293 ? 0.68416 0.43280 0.68342 -0.13801 -0.30661 0.02412  482 ALA B CA  
2086 C C   . ALA A 293 ? 0.66318 0.46129 0.73465 -0.17052 -0.30306 0.05576  482 ALA B C   
2087 O O   . ALA A 293 ? 0.70997 0.50396 0.81692 -0.18835 -0.32654 0.08642  482 ALA B O   
2088 C CB  . ALA A 293 ? 0.68314 0.37760 0.63569 -0.13137 -0.32955 0.02566  482 ALA B CB  
2089 N N   . ASN A 294 ? 0.68262 0.53172 0.78036 -0.17833 -0.27350 0.05144  483 ASN B N   
2090 C CA  . ASN A 294 ? 0.65880 0.57225 0.83367 -0.20673 -0.25742 0.08524  483 ASN B CA  
2091 C C   . ASN A 294 ? 0.54225 0.51669 0.76317 -0.19283 -0.22220 0.07758  483 ASN B C   
2092 O O   . ASN A 294 ? 0.45611 0.49333 0.71202 -0.18864 -0.18011 0.08949  483 ASN B O   
2093 C CB  . ASN A 294 ? 0.60231 0.53253 0.75030 -0.20378 -0.22720 0.09205  483 ASN B CB  
2094 C CG  . ASN A 294 ? 0.71218 0.64972 0.80979 -0.17146 -0.19372 0.05349  483 ASN B CG  
2095 O OD1 . ASN A 294 ? 0.71234 0.61827 0.77306 -0.15345 -0.20434 0.02031  483 ASN B OD1 
2096 N ND2 . ASN A 294 ? 0.82855 0.80856 0.92393 -0.16444 -0.15365 0.05915  483 ASN B ND2 
2097 N N   . CYS A 295 ? 0.64373 0.59622 0.85777 -0.18204 -0.23845 0.05730  484 CYS B N   
2098 C CA  . CYS A 295 ? 0.51428 0.51214 0.76760 -0.16847 -0.21296 0.04840  484 CYS B CA  
2099 C C   . CYS A 295 ? 0.53858 0.59771 0.88579 -0.18329 -0.20712 0.08339  484 CYS B C   
2100 O O   . CYS A 295 ? 0.45167 0.49567 0.82213 -0.19610 -0.23573 0.10592  484 CYS B O   
2101 C CB  . CYS A 295 ? 0.51035 0.46466 0.72613 -0.15334 -0.23126 0.02605  484 CYS B CB  
2102 S SG  . CYS A 295 ? 0.39984 0.39423 0.66996 -0.14371 -0.21831 0.01931  484 CYS B SG  
2103 N N   . ARG A 296 ? 0.41026 0.53415 0.79158 -0.16752 -0.15979 0.08422  485 ARG B N   
2104 C CA  . ARG A 296 ? 0.46266 0.65980 0.93924 -0.17424 -0.14455 0.11603  485 ARG B CA  
2105 C C   . ARG A 296 ? 0.37704 0.58162 0.90578 -0.16852 -0.16570 0.11311  485 ARG B C   
2106 O O   . ARG A 296 ? 0.37857 0.63664 0.99379 -0.17671 -0.16707 0.14207  485 ARG B O   
2107 C CB  . ARG A 296 ? 0.49994 0.76010 0.98374 -0.15113 -0.08471 0.11311  485 ARG B CB  
2108 C CG  . ARG A 296 ? 0.47648 0.72892 0.92401 -0.11586 -0.06228 0.07190  485 ARG B CG  
2109 C CD  . ARG A 296 ? 0.52981 0.81351 0.94437 -0.09223 -0.01230 0.06015  485 ARG B CD  
2110 N NE  . ARG A 296 ? 0.76305 0.99652 1.09091 -0.09304 -0.01483 0.04164  485 ARG B NE  
2111 C CZ  . ARG A 296 ? 0.66394 0.90522 0.94313 -0.07485 0.01780  0.02817  485 ARG B CZ  
2112 N NH1 . ARG A 296 ? 0.63691 0.93145 0.93559 -0.05213 0.05914  0.02946  485 ARG B NH1 
2113 N NH2 . ARG A 296 ? 0.50761 0.70115 0.71475 -0.07654 0.00731  0.01182  485 ARG B NH2 
2114 N N   . GLY A 297 ? 0.39869 0.55085 0.87427 -0.15363 -0.18128 0.08064  486 GLY B N   
2115 C CA  . GLY A 297 ? 0.39571 0.54030 0.90380 -0.14778 -0.20579 0.07765  486 GLY B CA  
2116 C C   . GLY A 297 ? 0.39946 0.58342 0.93709 -0.11874 -0.17404 0.06201  486 GLY B C   
2117 O O   . GLY A 297 ? 0.47040 0.63525 1.02057 -0.11111 -0.19657 0.05481  486 GLY B O   
2118 N N   . TRP A 298 ? 0.35360 0.58391 0.89419 -0.10006 -0.12505 0.05558  487 TRP B N   
2119 C CA  . TRP A 298 ? 0.41687 0.67758 0.97799 -0.06704 -0.09556 0.03710  487 TRP B CA  
2120 C C   . TRP A 298 ? 0.49455 0.73581 0.98012 -0.04748 -0.06325 0.00595  487 TRP B C   
2121 O O   . TRP A 298 ? 0.51118 0.75933 0.96228 -0.05304 -0.04318 0.00897  487 TRP B O   
2122 C CB  . TRP A 298 ? 0.38119 0.73036 1.03572 -0.05583 -0.06651 0.06119  487 TRP B CB  
2123 C CG  . TRP A 298 ? 0.42793 0.80795 1.17286 -0.07839 -0.09968 0.09687  487 TRP B CG  
2124 C CD1 . TRP A 298 ? 0.33653 0.75428 1.13281 -0.10868 -0.10598 0.13578  487 TRP B CD1 
2125 C CD2 . TRP A 298 ? 0.36950 0.74174 1.16607 -0.07474 -0.13682 0.09903  487 TRP B CD2 
2126 N NE1 . TRP A 298 ? 0.36316 0.77520 1.20065 -0.11831 -0.13916 0.15445  487 TRP B NE1 
2127 C CE2 . TRP A 298 ? 0.40851 0.79480 1.24828 -0.09780 -0.15837 0.13314  487 TRP B CE2 
2128 C CE3 . TRP A 298 ? 0.44846 0.78285 1.22743 -0.05198 -0.15183 0.07353  487 TRP B CE3 
2129 C CZ2 . TRP A 298 ? 0.48880 0.85541 1.35736 -0.09713 -0.19361 0.14111  487 TRP B CZ2 
2130 C CZ3 . TRP A 298 ? 0.59532 0.91952 1.41929 -0.05408 -0.19061 0.08562  487 TRP B CZ3 
2131 C CH2 . TRP A 298 ? 0.44450 0.78064 1.30323 -0.07511 -0.20849 0.11756  487 TRP B CH2 
2132 N N   . LEU A 299 ? 0.52130 0.73396 0.98133 -0.02615 -0.06298 -0.02245 488 LEU B N   
2133 C CA  . LEU A 299 ? 0.54655 0.74025 0.94355 -0.00734 -0.03795 -0.05252 488 LEU B CA  
2134 C C   . LEU A 299 ? 0.54732 0.79280 0.96433 0.02259  0.00393  -0.05780 488 LEU B C   
2135 O O   . LEU A 299 ? 0.49759 0.73908 0.86130 0.03256  0.02777  -0.07263 488 LEU B O   
2136 C CB  . LEU A 299 ? 0.52836 0.66967 0.89359 0.00097  -0.05631 -0.07757 488 LEU B CB  
2137 C CG  . LEU A 299 ? 0.47447 0.55957 0.78672 -0.02152 -0.08422 -0.08218 488 LEU B CG  
2138 C CD1 . LEU A 299 ? 0.48771 0.55962 0.82365 -0.04166 -0.11832 -0.06001 488 LEU B CD1 
2139 C CD2 . LEU A 299 ? 0.55488 0.59946 0.83478 -0.01252 -0.09017 -0.10505 488 LEU B CD2 
2140 N N   . PHE A 300 ? 0.67750 0.97157 1.16838 0.03996  0.01264  -0.04663 489 PHE B N   
2141 C CA  . PHE A 300 ? 0.61981 0.96577 1.13059 0.07778  0.05514  -0.05511 489 PHE B CA  
2142 C C   . PHE A 300 ? 0.58323 0.88203 1.02852 0.10881  0.06215  -0.09761 489 PHE B C   
2143 O O   . PHE A 300 ? 0.66934 0.98919 1.08886 0.13990  0.09736  -0.11319 489 PHE B O   
2144 C CB  . PHE A 300 ? 0.67414 1.07368 1.18205 0.07258  0.09282  -0.03334 489 PHE B CB  
2145 C CG  . PHE A 300 ? 0.74991 1.23851 1.35481 0.07446  0.11446  0.00289  489 PHE B CG  
2146 C CD1 . PHE A 300 ? 0.73027 1.27500 1.38200 0.11740  0.14703  -0.00490 489 PHE B CD1 
2147 C CD2 . PHE A 300 ? 0.75125 1.26839 1.40381 0.03419  0.10084  0.04520  489 PHE B CD2 
2148 C CE1 . PHE A 300 ? 0.66758 1.30728 1.42020 0.12008  0.17030  0.03113  489 PHE B CE1 
2149 C CE2 . PHE A 300 ? 0.65563 1.26187 1.40932 0.03135  0.11920  0.08337  489 PHE B CE2 
2150 C CZ  . PHE A 300 ? 0.67038 1.34410 1.47822 0.07432  0.15646  0.07749  489 PHE B CZ  
2151 N N   . GLY A 301 ? 0.49137 0.72405 0.90714 0.10012  0.02721  -0.11525 490 GLY B N   
2152 C CA  . GLY A 301 ? 0.45654 0.63667 0.81529 0.12158  0.02433  -0.15195 490 GLY B CA  
2153 C C   . GLY A 301 ? 0.43184 0.54551 0.76607 0.10006  -0.01528 -0.15954 490 GLY B C   
2154 O O   . GLY A 301 ? 0.50388 0.61051 0.87452 0.08430  -0.04099 -0.14214 490 GLY B O   
2155 N N   . GLN B 3   ? 0.93785 1.44471 1.28882 -0.39887 0.34875  -0.01346 5   GLN F N   
2156 C CA  . GLN B 3   ? 0.95966 1.49645 1.24630 -0.32922 0.38470  -0.01065 5   GLN F CA  
2157 C C   . GLN B 3   ? 0.78090 1.32575 1.04446 -0.27532 0.33792  -0.06326 5   GLN F C   
2158 O O   . GLN B 3   ? 0.62100 1.22590 0.91177 -0.22694 0.34286  -0.06562 5   GLN F O   
2159 C CB  . GLN B 3   ? 1.02344 1.46240 1.16935 -0.30930 0.41710  0.01323  5   GLN F CB  
2160 C CG  . GLN B 3   ? 1.10724 1.50307 1.25743 -0.36076 0.44596  0.06559  5   GLN F CG  
2161 C CD  . GLN B 3   ? 1.29582 1.60948 1.30688 -0.31809 0.47652  0.09192  5   GLN F CD  
2162 O OE1 . GLN B 3   ? 1.32955 1.61882 1.24569 -0.25020 0.47259  0.07033  5   GLN F OE1 
2163 N NE2 . GLN B 3   ? 1.27435 1.54796 1.28204 -0.35150 0.49676  0.13924  5   GLN F NE2 
2164 N N   . THR B 4   ? 0.82810 1.31216 1.04715 -0.28029 0.28927  -0.09657 6   THR F N   
2165 C CA  . THR B 4   ? 0.77621 1.26690 0.97651 -0.22037 0.24178  -0.12822 6   THR F CA  
2166 C C   . THR B 4   ? 0.76709 1.24618 0.98293 -0.23111 0.18315  -0.15414 6   THR F C   
2167 O O   . THR B 4   ? 0.85419 1.28407 1.05734 -0.28867 0.17601  -0.15103 6   THR F O   
2168 C CB  . THR B 4   ? 0.79591 1.21343 0.88179 -0.17466 0.24546  -0.12072 6   THR F CB  
2169 O OG1 . THR B 4   ? 0.81856 1.12277 0.79264 -0.20584 0.26071  -0.10334 6   THR F OG1 
2170 C CG2 . THR B 4   ? 0.71375 1.15350 0.78618 -0.13100 0.28368  -0.10341 6   THR F CG2 
2171 N N   . ALA B 5   ? 0.57441 1.08020 0.80809 -0.16608 0.13253  -0.16893 7   ALA F N   
2172 C CA  . ALA B 5   ? 0.48820 0.97789 0.70952 -0.13761 0.07057  -0.17788 7   ALA F CA  
2173 C C   . ALA B 5   ? 0.47493 0.92279 0.60778 -0.11311 0.05471  -0.16188 7   ALA F C   
2174 O O   . ALA B 5   ? 0.48404 0.90502 0.59536 -0.04024 0.01044  -0.14103 7   ALA F O   
2175 C CB  . ALA B 5   ? 0.41373 0.91099 0.67013 -0.07142 0.03354  -0.17458 7   ALA F CB  
2176 N N   . ARG B 6   ? 0.50239 0.83852 0.51963 -0.15605 0.09044  -0.14204 8   ARG F N   
2177 C CA  . ARG B 6   ? 0.58339 0.80126 0.46553 -0.11977 0.07126  -0.11188 8   ARG F CA  
2178 C C   . ARG B 6   ? 0.59678 0.65479 0.35169 -0.15286 0.06396  -0.08373 8   ARG F C   
2179 O O   . ARG B 6   ? 0.61057 0.63920 0.34003 -0.22271 0.10770  -0.09121 8   ARG F O   
2180 C CB  . ARG B 6   ? 0.54594 0.74499 0.41006 -0.09607 0.11069  -0.10519 8   ARG F CB  
2181 C CG  . ARG B 6   ? 0.49407 0.79194 0.45724 -0.03872 0.08517  -0.11393 8   ARG F CG  
2182 C CD  . ARG B 6   ? 0.49531 0.83416 0.50008 -0.03525 0.12772  -0.12391 8   ARG F CD  
2183 N NE  . ARG B 6   ? 0.56613 0.81391 0.46598 -0.01520 0.15749  -0.11366 8   ARG F NE  
2184 C CZ  . ARG B 6   ? 0.51234 0.78036 0.41697 0.01604  0.18034  -0.11930 8   ARG F CZ  
2185 N NH1 . ARG B 6   ? 0.43581 0.79692 0.43911 0.02354  0.17546  -0.12785 8   ARG F NH1 
2186 N NH2 . ARG B 6   ? 0.55072 0.72150 0.34163 0.04424  0.20262  -0.11437 8   ARG F NH2 
2195 N N   . SER B 8   ? 0.19812 0.38879 0.37879 0.01372  -0.01490 -0.18558 10  SER F N   
2196 C CA  . SER B 8   ? 0.27358 0.45872 0.46124 0.00507  -0.00542 -0.18750 10  SER F CA  
2197 C C   . SER B 8   ? 0.20358 0.42592 0.45457 0.03540  0.00172  -0.15436 10  SER F C   
2198 O O   . SER B 8   ? 0.20774 0.41148 0.48057 0.07198  0.00601  -0.16427 10  SER F O   
2199 C CB  . SER B 8   ? 0.30121 0.45879 0.53006 -0.00072 0.00366  -0.18864 10  SER F CB  
2200 O OG  . SER B 8   ? 0.20009 0.34919 0.45820 -0.02575 0.00386  -0.17085 10  SER F OG  
2201 N N   . THR B 9   ? 0.15522 0.41568 0.41720 0.02378  -0.00065 -0.10667 11  THR F N   
2202 C CA  . THR B 9   ? 0.20489 0.50005 0.53037 0.06400  -0.00405 -0.07821 11  THR F CA  
2203 C C   . THR B 9   ? 0.29161 0.47572 0.62323 0.07020  -0.00149 -0.06716 11  THR F C   
2204 O O   . THR B 9   ? 0.30610 0.45760 0.64538 0.11237  -0.00612 -0.04000 11  THR F O   
2205 C CB  . THR B 9   ? 0.17204 0.51687 0.47658 0.04888  -0.01414 -0.02569 11  THR F CB  
2206 O OG1 . THR B 9   ? 0.25728 0.57098 0.55132 0.01405  -0.01723 -0.00210 11  THR F OG1 
2207 C CG2 . THR B 9   ? 0.23567 0.55320 0.46106 0.01826  -0.00913 -0.02552 11  THR F CG2 
2208 N N   . GLY B 10  ? 0.32449 0.44746 0.65178 0.03005  0.00652  -0.09238 12  GLY F N   
2209 C CA  . GLY B 10  ? 0.36221 0.37432 0.69490 0.02192  0.01880  -0.08608 12  GLY F CA  
2210 C C   . GLY B 10  ? 0.39428 0.37066 0.69720 -0.00701 0.02544  -0.03235 12  GLY F C   
2211 O O   . GLY B 10  ? 0.51488 0.38275 0.80921 -0.02099 0.04465  -0.02408 12  GLY F O   
2212 N N   . GLY B 11  ? 0.41958 0.47585 0.70072 -0.01746 0.01325  0.00298  13  GLY F N   
2213 C CA  . GLY B 11  ? 0.46607 0.48798 0.70719 -0.03946 0.01762  0.05571  13  GLY F CA  
2214 C C   . GLY B 11  ? 0.62426 0.59125 0.83370 0.01592  0.00853  0.10566  13  GLY F C   
2215 O O   . GLY B 11  ? 0.63413 0.58205 0.86013 0.06977  0.00047  0.09677  13  GLY F O   
2216 N N   . CYS B 12  ? 0.77743 0.71070 0.93271 0.00713  0.00793  0.15713  14  CYS F N   
2217 C CA  . CYS B 12  ? 0.81738 0.69577 0.92348 0.06958  -0.00984 0.20543  14  CYS F CA  
2218 C C   . CYS B 12  ? 0.95581 0.65309 1.00097 0.07920  0.01354  0.22926  14  CYS F C   
2219 O O   . CYS B 12  ? 1.04571 0.67187 1.02550 0.13261  -0.00216 0.27201  14  CYS F O   
2220 C CB  . CYS B 12  ? 0.77182 0.71423 0.83878 0.07167  -0.03184 0.24866  14  CYS F CB  
2221 S SG  . CYS B 12  ? 1.01244 0.88950 1.01254 0.00089  -0.00512 0.28311  14  CYS F SG  
2222 N N   . ALA B 13  ? 1.03728 0.65751 1.10022 0.02821  0.05064  0.19743  15  ALA F N   
2223 C CA  . ALA B 13  ? 1.23981 0.68003 1.24999 0.02786  0.08222  0.21146  15  ALA F CA  
2224 C C   . ALA B 13  ? 1.39757 0.79490 1.39286 0.11237  0.05623  0.22139  15  ALA F C   
2225 O O   . ALA B 13  ? 1.37802 0.84536 1.44191 0.14194  0.04013  0.18056  15  ALA F O   
2226 C CB  . ALA B 13  ? 1.22844 0.62790 1.29514 -0.03121 0.11964  0.15370  15  ALA F CB  
2227 N N   . PRO B 14  ? 1.61095 0.88170 1.50787 0.15527  0.05243  0.27337  16  PRO F N   
2228 C CA  . PRO B 14  ? 1.66834 0.90942 1.54654 0.24870  0.01697  0.28142  16  PRO F CA  
2229 C C   . PRO B 14  ? 1.85471 0.97310 1.73540 0.27017  0.03353  0.25744  16  PRO F C   
2230 O O   . PRO B 14  ? 1.97634 0.97004 1.81986 0.21846  0.07011  0.25465  16  PRO F O   
2231 C CB  . PRO B 14  ? 1.72031 0.85982 1.47802 0.28118  0.00248  0.33814  16  PRO F CB  
2232 C CG  . PRO B 14  ? 1.74724 0.79329 1.45699 0.19304  0.05181  0.34916  16  PRO F CG  
2233 C CD  . PRO B 14  ? 1.73873 0.87445 1.52978 0.12099  0.08183  0.31986  16  PRO F CD  
2234 N N   . ARG B 15  ? 1.93592 1.12987 1.87680 0.33233  0.00155  0.22678  17  ARG F N   
2235 C CA  . ARG B 15  ? 2.06061 1.16620 2.01104 0.35832  0.00463  0.19916  17  ARG F CA  
2236 C C   . ARG B 15  ? 1.92246 1.14181 1.91384 0.44201  -0.04546 0.18734  17  ARG F C   
2237 O O   . ARG B 15  ? 1.79299 1.01133 1.82614 0.47250  -0.05317 0.15587  17  ARG F O   
2238 C CB  . ARG B 15  ? 1.95900 1.08567 1.99243 0.30425  0.03780  0.14413  17  ARG F CB  
2239 C CG  . ARG B 15  ? 1.85817 0.86743 1.88150 0.28141  0.05334  0.11531  17  ARG F CG  
2240 C CD  . ARG B 15  ? 1.91706 0.78960 1.85676 0.22894  0.08416  0.14851  17  ARG F CD  
2241 N NE  . ARG B 15  ? 2.05277 0.80560 1.96222 0.24063  0.08758  0.14270  17  ARG F NE  
2242 C CZ  . ARG B 15  ? 2.18740 0.90163 2.06878 0.31596  0.05720  0.16070  17  ARG F CZ  
2243 N NH1 . ARG B 15  ? 2.20177 1.00352 2.08560 0.38611  0.01810  0.18040  17  ARG F NH1 
2244 N NH2 . ARG B 15  ? 2.27200 0.87222 2.12725 0.31993  0.06603  0.15484  17  ARG F NH2 
2245 N N   . LYS B 16  ? 1.81585 1.14742 1.80512 0.47019  -0.07707 0.20783  18  LYS F N   
2246 C CA  . LYS B 16  ? 1.48351 0.96268 1.53311 0.52992  -0.11901 0.18580  18  LYS F CA  
2247 C C   . LYS B 16  ? 1.20086 0.82429 1.36071 0.51994  -0.11178 0.13216  18  LYS F C   
2248 O O   . LYS B 16  ? 1.19013 0.79810 1.38901 0.52940  -0.10093 0.09941  18  LYS F O   
2249 C CB  . LYS B 16  ? 1.48073 0.88487 1.49330 0.58673  -0.13957 0.18992  18  LYS F CB  
2250 C CG  . LYS B 16  ? 1.59700 0.96266 1.52317 0.61977  -0.16848 0.22932  18  LYS F CG  
2251 C CD  . LYS B 16  ? 1.52872 0.93490 1.42862 0.57960  -0.16603 0.25842  18  LYS F CD  
2252 C CE  . LYS B 16  ? 1.66476 0.89309 1.44707 0.54130  -0.13739 0.30563  18  LYS F CE  
2253 N NZ  . LYS B 16  ? 1.65789 0.92249 1.39072 0.52809  -0.15083 0.33860  18  LYS F NZ  
# 
