data_9KNF
# 
_entry.id   9KNF 
# 
_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   9KNF         pdb_00009knf 10.2210/pdb9knf/pdb 
WWPDB D_1300053808 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-04-23 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KNF 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              liu_jinsong@gibh.ac.cn 
_pdbx_contact_author.name_first         Jinsong 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2317-0558 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, T.'   1 0000-0002-1826-2012 
'Wang, N.' 2 0009-0000-4095-3963 
'Liu, J.'  3 0000-0003-2317-0558 
# 
_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                   CN 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acta Pharmacol.Sin.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1745-7254 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Identification of indoles as potential endogenous ligands of ERR gamma and their modulation on drug binding.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41401-025-01550-6 
_citation.pdbx_database_id_PubMed   40200124 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Shuai, Y.Y.' 1  ? 
primary 'Zhang, H.Y.' 2  ? 
primary 'Chen, R.'    3  ? 
primary 'Wang, B.L.'  4  ? 
primary 'Ding, P.'    5  ? 
primary 'Dong, Y.'    6  ? 
primary 'Sun, M.Z.'   7  ? 
primary 'Wu, X.S.'    8  ? 
primary 'Xu, Y.'      9  ? 
primary 'Zhang, Y.'   10 ? 
primary 'Liu, J.S.'   11 ? 
primary 'Wang, N.'    12 ? 
primary 'Xu, T.T.'    13 ? 
# 
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 'Estrogen-related receptor gamma'        28386.941 1   ? ? ? ? 
2 polymer     man 'Nuclear receptor-interacting protein 1' 1692.997  1   ? ? ? ? 
3 non-polymer syn '5-chloranyl-2~{H}-indazole'             152.581   1   ? ? ? ? 
4 water       nat water                                    18.015    121 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'ERR gamma-2,Estrogen receptor-related protein 3,Nuclear receptor subfamily 3 group B member 3' 
2 'Nuclear factor RIP140,Receptor-interacting protein 140'                                        
# 
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 
;MGSSHHHHHHSSGLVPRGSHMPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIP
GFSTLSLADQMSLLQSAWMEILILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFV
TLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHMEDPRRAGKMLMTLPLLRQTSTKAVQHFYNIKLEGKVPMH
KLFLEMLEAKV
;
;MGSSHHHHHHSSGLVPRGSHMPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIP
GFSTLSLADQMSLLQSAWMEILILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFV
TLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHMEDPRRAGKMLMTLPLLRQTSTKAVQHFYNIKLEGKVPMH
KLFLEMLEAKV
;
A ? 
2 'polypeptide(L)' no no NNSLLLHLLKSQTIP NNSLLLHLLKSQTIP C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '5-chloranyl-2~{H}-indazole' A1EGB 
4 water                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  PRO n 
1 23  ALA n 
1 24  LYS n 
1 25  LYS n 
1 26  PRO n 
1 27  TYR n 
1 28  ASN n 
1 29  LYS n 
1 30  ILE n 
1 31  VAL n 
1 32  SER n 
1 33  HIS n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  ALA n 
1 38  GLU n 
1 39  PRO n 
1 40  GLU n 
1 41  LYS n 
1 42  ILE n 
1 43  TYR n 
1 44  ALA n 
1 45  MET n 
1 46  PRO n 
1 47  ASP n 
1 48  PRO n 
1 49  THR n 
1 50  VAL n 
1 51  PRO n 
1 52  ASP n 
1 53  SER n 
1 54  ASP n 
1 55  ILE n 
1 56  LYS n 
1 57  ALA n 
1 58  LEU n 
1 59  THR n 
1 60  THR n 
1 61  LEU n 
1 62  CYS n 
1 63  ASP n 
1 64  LEU n 
1 65  ALA n 
1 66  ASP n 
1 67  ARG n 
1 68  GLU n 
1 69  LEU n 
1 70  VAL n 
1 71  VAL n 
1 72  ILE n 
1 73  ILE n 
1 74  GLY n 
1 75  TRP n 
1 76  ALA n 
1 77  LYS n 
1 78  HIS n 
1 79  ILE n 
1 80  PRO n 
1 81  GLY n 
1 82  PHE n 
1 83  SER n 
1 84  THR n 
1 85  LEU n 
1 86  SER n 
1 87  LEU n 
1 88  ALA n 
1 89  ASP n 
1 90  GLN n 
1 91  MET n 
1 92  SER n 
1 93  LEU n 
1 94  LEU n 
1 95  GLN n 
1 96  SER n 
1 97  ALA n 
1 98  TRP n 
1 99  MET n 
1 100 GLU n 
1 101 ILE n 
1 102 LEU n 
1 103 ILE n 
1 104 LEU n 
1 105 GLY n 
1 106 VAL n 
1 107 VAL n 
1 108 TYR n 
1 109 ARG n 
1 110 SER n 
1 111 LEU n 
1 112 SER n 
1 113 PHE n 
1 114 GLU n 
1 115 ASP n 
1 116 GLU n 
1 117 LEU n 
1 118 VAL n 
1 119 TYR n 
1 120 ALA n 
1 121 ASP n 
1 122 ASP n 
1 123 TYR n 
1 124 ILE n 
1 125 MET n 
1 126 ASP n 
1 127 GLU n 
1 128 ASP n 
1 129 GLN n 
1 130 SER n 
1 131 LYS n 
1 132 LEU n 
1 133 ALA n 
1 134 GLY n 
1 135 LEU n 
1 136 LEU n 
1 137 ASP n 
1 138 LEU n 
1 139 ASN n 
1 140 ASN n 
1 141 ALA n 
1 142 ILE n 
1 143 LEU n 
1 144 GLN n 
1 145 LEU n 
1 146 VAL n 
1 147 LYS n 
1 148 LYS n 
1 149 TYR n 
1 150 LYS n 
1 151 SER n 
1 152 MET n 
1 153 LYS n 
1 154 LEU n 
1 155 GLU n 
1 156 LYS n 
1 157 GLU n 
1 158 GLU n 
1 159 PHE n 
1 160 VAL n 
1 161 THR n 
1 162 LEU n 
1 163 LYS n 
1 164 ALA n 
1 165 ILE n 
1 166 ALA n 
1 167 LEU n 
1 168 ALA n 
1 169 ASN n 
1 170 SER n 
1 171 ASP n 
1 172 SER n 
1 173 MET n 
1 174 HIS n 
1 175 ILE n 
1 176 GLU n 
1 177 ASP n 
1 178 VAL n 
1 179 GLU n 
1 180 ALA n 
1 181 VAL n 
1 182 GLN n 
1 183 LYS n 
1 184 LEU n 
1 185 GLN n 
1 186 ASP n 
1 187 VAL n 
1 188 LEU n 
1 189 HIS n 
1 190 GLU n 
1 191 ALA n 
1 192 LEU n 
1 193 GLN n 
1 194 ASP n 
1 195 TYR n 
1 196 GLU n 
1 197 ALA n 
1 198 GLY n 
1 199 GLN n 
1 200 HIS n 
1 201 MET n 
1 202 GLU n 
1 203 ASP n 
1 204 PRO n 
1 205 ARG n 
1 206 ARG n 
1 207 ALA n 
1 208 GLY n 
1 209 LYS n 
1 210 MET n 
1 211 LEU n 
1 212 MET n 
1 213 THR n 
1 214 LEU n 
1 215 PRO n 
1 216 LEU n 
1 217 LEU n 
1 218 ARG n 
1 219 GLN n 
1 220 THR n 
1 221 SER n 
1 222 THR n 
1 223 LYS n 
1 224 ALA n 
1 225 VAL n 
1 226 GLN n 
1 227 HIS n 
1 228 PHE n 
1 229 TYR n 
1 230 ASN n 
1 231 ILE n 
1 232 LYS n 
1 233 LEU n 
1 234 GLU n 
1 235 GLY n 
1 236 LYS n 
1 237 VAL n 
1 238 PRO n 
1 239 MET n 
1 240 HIS n 
1 241 LYS n 
1 242 LEU n 
1 243 PHE n 
1 244 LEU n 
1 245 GLU n 
1 246 MET n 
1 247 LEU n 
1 248 GLU n 
1 249 ALA n 
1 250 LYS n 
1 251 VAL n 
2 1   ASN n 
2 2   ASN n 
2 3   SER n 
2 4   LEU n 
2 5   LEU n 
2 6   LEU n 
2 7   HIS n 
2 8   LEU n 
2 9   LEU n 
2 10  LYS n 
2 11  SER n 
2 12  GLN n 
2 13  THR n 
2 14  ILE n 
2 15  PRO n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 251 human ? 'ESRRG, ERR3, ERRG2, KIAA0832, NR3B3' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 
? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 15  human ? NRIP1                                 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 
? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1EGB non-polymer         . '5-chloranyl-2~{H}-indazole' ? 'C7 H5 Cl N2'    152.581 
ALA   'L-peptide linking' y ALANINE                      ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                     ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                   ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'              ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                     ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                    ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'              ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                      ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                    ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                        ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                   ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                      ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                       ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                   ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                      ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                       ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                    ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                   ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                     ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                       ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   208 ?   ?   ?   A . n 
A 1 2   GLY 2   209 ?   ?   ?   A . n 
A 1 3   SER 3   210 ?   ?   ?   A . n 
A 1 4   SER 4   211 ?   ?   ?   A . n 
A 1 5   HIS 5   212 ?   ?   ?   A . n 
A 1 6   HIS 6   213 ?   ?   ?   A . n 
A 1 7   HIS 7   214 ?   ?   ?   A . n 
A 1 8   HIS 8   215 ?   ?   ?   A . n 
A 1 9   HIS 9   216 ?   ?   ?   A . n 
A 1 10  HIS 10  217 ?   ?   ?   A . n 
A 1 11  SER 11  218 ?   ?   ?   A . n 
A 1 12  SER 12  219 ?   ?   ?   A . n 
A 1 13  GLY 13  220 ?   ?   ?   A . n 
A 1 14  LEU 14  221 ?   ?   ?   A . n 
A 1 15  VAL 15  222 ?   ?   ?   A . n 
A 1 16  PRO 16  223 ?   ?   ?   A . n 
A 1 17  ARG 17  224 ?   ?   ?   A . n 
A 1 18  GLY 18  225 ?   ?   ?   A . n 
A 1 19  SER 19  226 ?   ?   ?   A . n 
A 1 20  HIS 20  227 ?   ?   ?   A . n 
A 1 21  MET 21  228 ?   ?   ?   A . n 
A 1 22  PRO 22  229 ?   ?   ?   A . n 
A 1 23  ALA 23  230 ?   ?   ?   A . n 
A 1 24  LYS 24  231 ?   ?   ?   A . n 
A 1 25  LYS 25  232 ?   ?   ?   A . n 
A 1 26  PRO 26  233 233 PRO PRO A . n 
A 1 27  TYR 27  234 234 TYR TYR A . n 
A 1 28  ASN 28  235 235 ASN ASN A . n 
A 1 29  LYS 29  236 236 LYS LYS A . n 
A 1 30  ILE 30  237 237 ILE ILE A . n 
A 1 31  VAL 31  238 238 VAL VAL A . n 
A 1 32  SER 32  239 239 SER SER A . n 
A 1 33  HIS 33  240 240 HIS HIS A . n 
A 1 34  LEU 34  241 241 LEU LEU A . n 
A 1 35  LEU 35  242 242 LEU LEU A . n 
A 1 36  VAL 36  243 243 VAL VAL A . n 
A 1 37  ALA 37  244 244 ALA ALA A . n 
A 1 38  GLU 38  245 245 GLU GLU A . n 
A 1 39  PRO 39  246 246 PRO PRO A . n 
A 1 40  GLU 40  247 247 GLU GLU A . n 
A 1 41  LYS 41  248 248 LYS LYS A . n 
A 1 42  ILE 42  249 249 ILE ILE A . n 
A 1 43  TYR 43  250 250 TYR TYR A . n 
A 1 44  ALA 44  251 251 ALA ALA A . n 
A 1 45  MET 45  252 252 MET MET A . n 
A 1 46  PRO 46  253 253 PRO PRO A . n 
A 1 47  ASP 47  254 254 ASP ASP A . n 
A 1 48  PRO 48  255 255 PRO PRO A . n 
A 1 49  THR 49  256 256 THR THR A . n 
A 1 50  VAL 50  257 257 VAL VAL A . n 
A 1 51  PRO 51  258 258 PRO PRO A . n 
A 1 52  ASP 52  259 259 ASP ASP A . n 
A 1 53  SER 53  260 260 SER SER A . n 
A 1 54  ASP 54  261 261 ASP ASP A . n 
A 1 55  ILE 55  262 262 ILE ILE A . n 
A 1 56  LYS 56  263 263 LYS LYS A . n 
A 1 57  ALA 57  264 264 ALA ALA A . n 
A 1 58  LEU 58  265 265 LEU LEU A . n 
A 1 59  THR 59  266 266 THR THR A . n 
A 1 60  THR 60  267 267 THR THR A . n 
A 1 61  LEU 61  268 268 LEU LEU A . n 
A 1 62  CYS 62  269 269 CYS CYS A . n 
A 1 63  ASP 63  270 270 ASP ASP A . n 
A 1 64  LEU 64  271 271 LEU LEU A . n 
A 1 65  ALA 65  272 272 ALA ALA A . n 
A 1 66  ASP 66  273 273 ASP ASP A . n 
A 1 67  ARG 67  274 274 ARG ARG A . n 
A 1 68  GLU 68  275 275 GLU GLU A . n 
A 1 69  LEU 69  276 276 LEU LEU A . n 
A 1 70  VAL 70  277 277 VAL VAL A . n 
A 1 71  VAL 71  278 278 VAL VAL A . n 
A 1 72  ILE 72  279 279 ILE ILE A . n 
A 1 73  ILE 73  280 280 ILE ILE A . n 
A 1 74  GLY 74  281 281 GLY GLY A . n 
A 1 75  TRP 75  282 282 TRP TRP A . n 
A 1 76  ALA 76  283 283 ALA ALA A . n 
A 1 77  LYS 77  284 284 LYS LYS A . n 
A 1 78  HIS 78  285 285 HIS HIS A . n 
A 1 79  ILE 79  286 286 ILE ILE A . n 
A 1 80  PRO 80  287 287 PRO PRO A . n 
A 1 81  GLY 81  288 288 GLY GLY A . n 
A 1 82  PHE 82  289 289 PHE PHE A . n 
A 1 83  SER 83  290 290 SER SER A . n 
A 1 84  THR 84  291 291 THR THR A . n 
A 1 85  LEU 85  292 292 LEU LEU A . n 
A 1 86  SER 86  293 293 SER SER A . n 
A 1 87  LEU 87  294 294 LEU LEU A . n 
A 1 88  ALA 88  295 295 ALA ALA A . n 
A 1 89  ASP 89  296 296 ASP ASP A . n 
A 1 90  GLN 90  297 297 GLN GLN A . n 
A 1 91  MET 91  298 298 MET MET A . n 
A 1 92  SER 92  299 299 SER SER A . n 
A 1 93  LEU 93  300 300 LEU LEU A . n 
A 1 94  LEU 94  301 301 LEU LEU A . n 
A 1 95  GLN 95  302 302 GLN GLN A . n 
A 1 96  SER 96  303 303 SER SER A . n 
A 1 97  ALA 97  304 304 ALA ALA A . n 
A 1 98  TRP 98  305 305 TRP TRP A . n 
A 1 99  MET 99  306 306 MET MET A . n 
A 1 100 GLU 100 307 307 GLU GLU A . n 
A 1 101 ILE 101 308 308 ILE ILE A . n 
A 1 102 LEU 102 309 309 LEU LEU A . n 
A 1 103 ILE 103 310 310 ILE ILE A . n 
A 1 104 LEU 104 311 311 LEU LEU A . n 
A 1 105 GLY 105 312 312 GLY GLY A . n 
A 1 106 VAL 106 313 313 VAL VAL A . n 
A 1 107 VAL 107 314 314 VAL VAL A . n 
A 1 108 TYR 108 315 315 TYR TYR A . n 
A 1 109 ARG 109 316 316 ARG ARG A . n 
A 1 110 SER 110 317 317 SER SER A . n 
A 1 111 LEU 111 318 318 LEU LEU A . n 
A 1 112 SER 112 319 319 SER SER A . n 
A 1 113 PHE 113 320 320 PHE PHE A . n 
A 1 114 GLU 114 321 321 GLU GLU A . n 
A 1 115 ASP 115 322 322 ASP ASP A . n 
A 1 116 GLU 116 323 323 GLU GLU A . n 
A 1 117 LEU 117 324 324 LEU LEU A . n 
A 1 118 VAL 118 325 325 VAL VAL A . n 
A 1 119 TYR 119 326 326 TYR TYR A . n 
A 1 120 ALA 120 327 327 ALA ALA A . n 
A 1 121 ASP 121 328 328 ASP ASP A . n 
A 1 122 ASP 122 329 329 ASP ASP A . n 
A 1 123 TYR 123 330 330 TYR TYR A . n 
A 1 124 ILE 124 331 331 ILE ILE A . n 
A 1 125 MET 125 332 332 MET MET A . n 
A 1 126 ASP 126 333 333 ASP ASP A . n 
A 1 127 GLU 127 334 334 GLU GLU A . n 
A 1 128 ASP 128 335 335 ASP ASP A . n 
A 1 129 GLN 129 336 336 GLN GLN A . n 
A 1 130 SER 130 337 337 SER SER A . n 
A 1 131 LYS 131 338 338 LYS LYS A . n 
A 1 132 LEU 132 339 339 LEU LEU A . n 
A 1 133 ALA 133 340 340 ALA ALA A . n 
A 1 134 GLY 134 341 341 GLY GLY A . n 
A 1 135 LEU 135 342 342 LEU LEU A . n 
A 1 136 LEU 136 343 343 LEU LEU A . n 
A 1 137 ASP 137 344 344 ASP ASP A . n 
A 1 138 LEU 138 345 345 LEU LEU A . n 
A 1 139 ASN 139 346 346 ASN ASN A . n 
A 1 140 ASN 140 347 347 ASN ASN A . n 
A 1 141 ALA 141 348 348 ALA ALA A . n 
A 1 142 ILE 142 349 349 ILE ILE A . n 
A 1 143 LEU 143 350 350 LEU LEU A . n 
A 1 144 GLN 144 351 351 GLN GLN A . n 
A 1 145 LEU 145 352 352 LEU LEU A . n 
A 1 146 VAL 146 353 353 VAL VAL A . n 
A 1 147 LYS 147 354 354 LYS LYS A . n 
A 1 148 LYS 148 355 355 LYS LYS A . n 
A 1 149 TYR 149 356 356 TYR TYR A . n 
A 1 150 LYS 150 357 357 LYS LYS A . n 
A 1 151 SER 151 358 358 SER SER A . n 
A 1 152 MET 152 359 359 MET MET A . n 
A 1 153 LYS 153 360 360 LYS LYS A . n 
A 1 154 LEU 154 361 361 LEU LEU A . n 
A 1 155 GLU 155 362 362 GLU GLU A . n 
A 1 156 LYS 156 363 363 LYS LYS A . n 
A 1 157 GLU 157 364 364 GLU GLU A . n 
A 1 158 GLU 158 365 365 GLU GLU A . n 
A 1 159 PHE 159 366 366 PHE PHE A . n 
A 1 160 VAL 160 367 367 VAL VAL A . n 
A 1 161 THR 161 368 368 THR THR A . n 
A 1 162 LEU 162 369 369 LEU LEU A . n 
A 1 163 LYS 163 370 370 LYS LYS A . n 
A 1 164 ALA 164 371 371 ALA ALA A . n 
A 1 165 ILE 165 372 372 ILE ILE A . n 
A 1 166 ALA 166 373 373 ALA ALA A . n 
A 1 167 LEU 167 374 374 LEU LEU A . n 
A 1 168 ALA 168 375 375 ALA ALA A . n 
A 1 169 ASN 169 376 376 ASN ASN A . n 
A 1 170 SER 170 377 377 SER SER A . n 
A 1 171 ASP 171 378 378 ASP ASP A . n 
A 1 172 SER 172 379 379 SER SER A . n 
A 1 173 MET 173 380 380 MET MET A . n 
A 1 174 HIS 174 381 381 HIS HIS A . n 
A 1 175 ILE 175 382 382 ILE ILE A . n 
A 1 176 GLU 176 383 383 GLU GLU A . n 
A 1 177 ASP 177 384 384 ASP ASP A . n 
A 1 178 VAL 178 385 385 VAL VAL A . n 
A 1 179 GLU 179 386 386 GLU GLU A . n 
A 1 180 ALA 180 387 387 ALA ALA A . n 
A 1 181 VAL 181 388 388 VAL VAL A . n 
A 1 182 GLN 182 389 389 GLN GLN A . n 
A 1 183 LYS 183 390 390 LYS LYS A . n 
A 1 184 LEU 184 391 391 LEU LEU A . n 
A 1 185 GLN 185 392 392 GLN GLN A . n 
A 1 186 ASP 186 393 393 ASP ASP A . n 
A 1 187 VAL 187 394 394 VAL VAL A . n 
A 1 188 LEU 188 395 395 LEU LEU A . n 
A 1 189 HIS 189 396 396 HIS HIS A . n 
A 1 190 GLU 190 397 397 GLU GLU A . n 
A 1 191 ALA 191 398 398 ALA ALA A . n 
A 1 192 LEU 192 399 399 LEU LEU A . n 
A 1 193 GLN 193 400 400 GLN GLN A . n 
A 1 194 ASP 194 401 401 ASP ASP A . n 
A 1 195 TYR 195 402 402 TYR TYR A . n 
A 1 196 GLU 196 403 403 GLU GLU A . n 
A 1 197 ALA 197 404 404 ALA ALA A . n 
A 1 198 GLY 198 405 405 GLY GLY A . n 
A 1 199 GLN 199 406 406 GLN GLN A . n 
A 1 200 HIS 200 407 407 HIS HIS A . n 
A 1 201 MET 201 408 408 MET MET A . n 
A 1 202 GLU 202 409 409 GLU GLU A . n 
A 1 203 ASP 203 410 410 ASP ASP A . n 
A 1 204 PRO 204 411 411 PRO PRO A . n 
A 1 205 ARG 205 412 412 ARG ARG A . n 
A 1 206 ARG 206 413 413 ARG ARG A . n 
A 1 207 ALA 207 414 414 ALA ALA A . n 
A 1 208 GLY 208 415 415 GLY GLY A . n 
A 1 209 LYS 209 416 416 LYS LYS A . n 
A 1 210 MET 210 417 417 MET MET A . n 
A 1 211 LEU 211 418 418 LEU LEU A . n 
A 1 212 MET 212 419 419 MET MET A . n 
A 1 213 THR 213 420 420 THR THR A . n 
A 1 214 LEU 214 421 421 LEU LEU A . n 
A 1 215 PRO 215 422 422 PRO PRO A . n 
A 1 216 LEU 216 423 423 LEU LEU A . n 
A 1 217 LEU 217 424 424 LEU LEU A . n 
A 1 218 ARG 218 425 425 ARG ARG A . n 
A 1 219 GLN 219 426 426 GLN GLN A . n 
A 1 220 THR 220 427 427 THR THR A . n 
A 1 221 SER 221 428 428 SER SER A . n 
A 1 222 THR 222 429 429 THR THR A . n 
A 1 223 LYS 223 430 430 LYS LYS A . n 
A 1 224 ALA 224 431 431 ALA ALA A . n 
A 1 225 VAL 225 432 432 VAL VAL A . n 
A 1 226 GLN 226 433 433 GLN GLN A . n 
A 1 227 HIS 227 434 434 HIS HIS A . n 
A 1 228 PHE 228 435 435 PHE PHE A . n 
A 1 229 TYR 229 436 436 TYR TYR A . n 
A 1 230 ASN 230 437 437 ASN ASN A . n 
A 1 231 ILE 231 438 438 ILE ILE A . n 
A 1 232 LYS 232 439 439 LYS LYS A . n 
A 1 233 LEU 233 440 440 LEU LEU A . n 
A 1 234 GLU 234 441 441 GLU GLU A . n 
A 1 235 GLY 235 442 442 GLY GLY A . n 
A 1 236 LYS 236 443 443 LYS LYS A . n 
A 1 237 VAL 237 444 444 VAL VAL A . n 
A 1 238 PRO 238 445 445 PRO PRO A . n 
A 1 239 MET 239 446 446 MET MET A . n 
A 1 240 HIS 240 447 447 HIS HIS A . n 
A 1 241 LYS 241 448 448 LYS LYS A . n 
A 1 242 LEU 242 449 449 LEU LEU A . n 
A 1 243 PHE 243 450 450 PHE PHE A . n 
A 1 244 LEU 244 451 451 LEU LEU A . n 
A 1 245 GLU 245 452 452 GLU GLU A . n 
A 1 246 MET 246 453 453 MET MET A . n 
A 1 247 LEU 247 454 454 LEU LEU A . n 
A 1 248 GLU 248 455 455 GLU GLU A . n 
A 1 249 ALA 249 456 456 ALA ALA A . n 
A 1 250 LYS 250 457 457 LYS LYS A . n 
A 1 251 VAL 251 458 ?   ?   ?   A . n 
B 2 1   ASN 1   376 376 ASN ASN C . n 
B 2 2   ASN 2   377 377 ASN ASN C . n 
B 2 3   SER 3   378 378 SER SER C . n 
B 2 4   LEU 4   379 379 LEU LEU C . n 
B 2 5   LEU 5   380 380 LEU LEU C . n 
B 2 6   LEU 6   381 381 LEU LEU C . n 
B 2 7   HIS 7   382 382 HIS HIS C . n 
B 2 8   LEU 8   383 383 LEU LEU C . n 
B 2 9   LEU 9   384 384 LEU LEU C . n 
B 2 10  LYS 10  385 385 LYS LYS C . n 
B 2 11  SER 11  386 386 SER SER C . n 
B 2 12  GLN 12  387 387 GLN GLN C . n 
B 2 13  THR 13  388 ?   ?   ?   C . n 
B 2 14  ILE 14  389 ?   ?   ?   C . n 
B 2 15  PRO 15  390 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EGB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EGB 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1EGB 1   501 501 A1EGB XT9 A . 
D 4 HOH   1   601 13  HOH   HOH A . 
D 4 HOH   2   602 51  HOH   HOH A . 
D 4 HOH   3   603 61  HOH   HOH A . 
D 4 HOH   4   604 109 HOH   HOH A . 
D 4 HOH   5   605 35  HOH   HOH A . 
D 4 HOH   6   606 99  HOH   HOH A . 
D 4 HOH   7   607 79  HOH   HOH A . 
D 4 HOH   8   608 12  HOH   HOH A . 
D 4 HOH   9   609 96  HOH   HOH A . 
D 4 HOH   10  610 59  HOH   HOH A . 
D 4 HOH   11  611 25  HOH   HOH A . 
D 4 HOH   12  612 81  HOH   HOH A . 
D 4 HOH   13  613 33  HOH   HOH A . 
D 4 HOH   14  614 57  HOH   HOH A . 
D 4 HOH   15  615 63  HOH   HOH A . 
D 4 HOH   16  616 1   HOH   HOH A . 
D 4 HOH   17  617 19  HOH   HOH A . 
D 4 HOH   18  618 120 HOH   HOH A . 
D 4 HOH   19  619 18  HOH   HOH A . 
D 4 HOH   20  620 72  HOH   HOH A . 
D 4 HOH   21  621 8   HOH   HOH A . 
D 4 HOH   22  622 7   HOH   HOH A . 
D 4 HOH   23  623 49  HOH   HOH A . 
D 4 HOH   24  624 11  HOH   HOH A . 
D 4 HOH   25  625 121 HOH   HOH A . 
D 4 HOH   26  626 14  HOH   HOH A . 
D 4 HOH   27  627 65  HOH   HOH A . 
D 4 HOH   28  628 28  HOH   HOH A . 
D 4 HOH   29  629 108 HOH   HOH A . 
D 4 HOH   30  630 6   HOH   HOH A . 
D 4 HOH   31  631 86  HOH   HOH A . 
D 4 HOH   32  632 75  HOH   HOH A . 
D 4 HOH   33  633 62  HOH   HOH A . 
D 4 HOH   34  634 20  HOH   HOH A . 
D 4 HOH   35  635 103 HOH   HOH A . 
D 4 HOH   36  636 21  HOH   HOH A . 
D 4 HOH   37  637 9   HOH   HOH A . 
D 4 HOH   38  638 41  HOH   HOH A . 
D 4 HOH   39  639 2   HOH   HOH A . 
D 4 HOH   40  640 113 HOH   HOH A . 
D 4 HOH   41  641 17  HOH   HOH A . 
D 4 HOH   42  642 70  HOH   HOH A . 
D 4 HOH   43  643 30  HOH   HOH A . 
D 4 HOH   44  644 68  HOH   HOH A . 
D 4 HOH   45  645 50  HOH   HOH A . 
D 4 HOH   46  646 39  HOH   HOH A . 
D 4 HOH   47  647 4   HOH   HOH A . 
D 4 HOH   48  648 88  HOH   HOH A . 
D 4 HOH   49  649 34  HOH   HOH A . 
D 4 HOH   50  650 64  HOH   HOH A . 
D 4 HOH   51  651 29  HOH   HOH A . 
D 4 HOH   52  652 76  HOH   HOH A . 
D 4 HOH   53  653 95  HOH   HOH A . 
D 4 HOH   54  654 111 HOH   HOH A . 
D 4 HOH   55  655 23  HOH   HOH A . 
D 4 HOH   56  656 110 HOH   HOH A . 
D 4 HOH   57  657 5   HOH   HOH A . 
D 4 HOH   58  658 90  HOH   HOH A . 
D 4 HOH   59  659 37  HOH   HOH A . 
D 4 HOH   60  660 66  HOH   HOH A . 
D 4 HOH   61  661 31  HOH   HOH A . 
D 4 HOH   62  662 83  HOH   HOH A . 
D 4 HOH   63  663 54  HOH   HOH A . 
D 4 HOH   64  664 71  HOH   HOH A . 
D 4 HOH   65  665 92  HOH   HOH A . 
D 4 HOH   66  666 16  HOH   HOH A . 
D 4 HOH   67  667 32  HOH   HOH A . 
D 4 HOH   68  668 52  HOH   HOH A . 
D 4 HOH   69  669 60  HOH   HOH A . 
D 4 HOH   70  670 10  HOH   HOH A . 
D 4 HOH   71  671 55  HOH   HOH A . 
D 4 HOH   72  672 46  HOH   HOH A . 
D 4 HOH   73  673 24  HOH   HOH A . 
D 4 HOH   74  674 93  HOH   HOH A . 
D 4 HOH   75  675 107 HOH   HOH A . 
D 4 HOH   76  676 67  HOH   HOH A . 
D 4 HOH   77  677 97  HOH   HOH A . 
D 4 HOH   78  678 53  HOH   HOH A . 
D 4 HOH   79  679 26  HOH   HOH A . 
D 4 HOH   80  680 27  HOH   HOH A . 
D 4 HOH   81  681 116 HOH   HOH A . 
D 4 HOH   82  682 15  HOH   HOH A . 
D 4 HOH   83  683 3   HOH   HOH A . 
D 4 HOH   84  684 43  HOH   HOH A . 
D 4 HOH   85  685 69  HOH   HOH A . 
D 4 HOH   86  686 100 HOH   HOH A . 
D 4 HOH   87  687 22  HOH   HOH A . 
D 4 HOH   88  688 87  HOH   HOH A . 
D 4 HOH   89  689 84  HOH   HOH A . 
D 4 HOH   90  690 101 HOH   HOH A . 
D 4 HOH   91  691 56  HOH   HOH A . 
D 4 HOH   92  692 114 HOH   HOH A . 
D 4 HOH   93  693 123 HOH   HOH A . 
D 4 HOH   94  694 38  HOH   HOH A . 
D 4 HOH   95  695 82  HOH   HOH A . 
D 4 HOH   96  696 40  HOH   HOH A . 
D 4 HOH   97  697 91  HOH   HOH A . 
D 4 HOH   98  698 126 HOH   HOH A . 
D 4 HOH   99  699 115 HOH   HOH A . 
D 4 HOH   100 700 119 HOH   HOH A . 
D 4 HOH   101 701 77  HOH   HOH A . 
D 4 HOH   102 702 122 HOH   HOH A . 
D 4 HOH   103 703 125 HOH   HOH A . 
D 4 HOH   104 704 118 HOH   HOH A . 
D 4 HOH   105 705 42  HOH   HOH A . 
D 4 HOH   106 706 80  HOH   HOH A . 
D 4 HOH   107 707 48  HOH   HOH A . 
D 4 HOH   108 708 104 HOH   HOH A . 
D 4 HOH   109 709 124 HOH   HOH A . 
D 4 HOH   110 710 85  HOH   HOH A . 
D 4 HOH   111 711 117 HOH   HOH A . 
D 4 HOH   112 712 36  HOH   HOH A . 
D 4 HOH   113 713 98  HOH   HOH A . 
D 4 HOH   114 714 112 HOH   HOH A . 
D 4 HOH   115 715 105 HOH   HOH A . 
D 4 HOH   116 716 106 HOH   HOH A . 
D 4 HOH   117 717 94  HOH   HOH A . 
D 4 HOH   118 718 58  HOH   HOH A . 
D 4 HOH   119 719 78  HOH   HOH A . 
D 4 HOH   120 720 44  HOH   HOH A . 
D 4 HOH   121 721 89  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0258 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KNF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.200 
_cell.length_a_esd                 ? 
_cell.length_b                     64.200 
_cell.length_b_esd                 ? 
_cell.length_c                     138.870 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9KNF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   9KNF 
_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             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.29 
_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    '1.0 M K/Na tartrate, 0.1 M Tris pH 7.0, 0.2 M Li2SO4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-01-09 
_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   0.97875 
_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 BL17U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97875 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KNF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.62 
_reflns.d_resolution_low                               64.20 
_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                                     34901 
_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                           91.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                23.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.03 
_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                                0.098 
_reflns.pdbx_Rpim_I_all                                0.020 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       820062 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.096 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.62 
_reflns_shell.d_res_low                                     1.64 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           45703 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1866 
_reflns_shell.percent_possible_obs                          99.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               24.5 
_reflns_shell.pdbx_chi_squared                              0.86 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.9 
_reflns_shell.pdbx_Rrim_I_all                               1.318 
_reflns_shell.pdbx_Rpim_I_all                               0.261 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.815 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.292 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            2.17 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            2.17 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -4.34 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.376 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9KNF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.62 
_refine.ls_d_res_low                             58.27 
_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                     32711 
_refine.ls_number_reflns_R_free                  1681 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.49 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17491 
_refine.ls_R_factor_R_free                       0.22770 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17200 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.110 
_refine.pdbx_overall_ESU_R_Free                  0.096 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             6.734 
_refine.overall_SU_ML                            0.097 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.62 
_refine_hist.d_res_low                        58.27 
_refine_hist.number_atoms_solvent             121 
_refine_hist.number_atoms_total               2016 
_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        1885 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_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' ? 0.014  0.013  1945 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  1877 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.804  1.637  2633 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.480  1.580  4378 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.340  5.000  241  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.149 25.114 88   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.260 15.000 376  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.778 15.000 5    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.104  0.200  254  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  2101 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  345  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.919  2.472  952  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.731  2.466  951  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.504  3.718  1188 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.526  3.725  1189 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.051  3.151  993  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 6.047  3.141  991  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.100  4.493  1442 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.730  30.077 2216 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.734  29.932 2197 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 6.257  3.000  3822 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.62 
_refine_ls_shell.d_res_low                        1.659 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             128 
_refine_ls_shell.number_reflns_R_work             2613 
_refine_ls_shell.percent_reflns_obs               99.67 
_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                  0.201 
_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                  0.331 
# 
_struct.entry_id                     9KNF 
_struct.title                        'Crystal structure of human ERRg LBD in complex with 4028691' 
_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        9KNF 
_struct_keywords.text            'EsRRG, LBD, nuclear receptor, complex structure, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 ? 
# 
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 ERR3_HUMAN  P62508 ? 1 
;PAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIPGFSTLSLADQMSLLQSAWMEI
LILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFVTLKAIALANSDSMHIEDVEAV
QKLQDVLHEALQDYEAGQHMEDPRRAGKMLMTLPLLRQTSTKAVQHFYNIKLEGKVPMHKLFLEMLEAKV
;
229 
2 UNP NRIP1_HUMAN P48552 ? 2 NNSLLLHLLKSQTIP 376 
# 
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 9KNF A 22 ? 251 ? P62508 229 ? 458 ? 229 458 
2 2 9KNF C 1  ? 15  ? P48552 376 ? 390 ? 376 390 
# 
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 9KNF MET A 1  ? UNP P62508 ? ? 'initiating methionine' 208 1  
1 9KNF GLY A 2  ? UNP P62508 ? ? 'expression tag'        209 2  
1 9KNF SER A 3  ? UNP P62508 ? ? 'expression tag'        210 3  
1 9KNF SER A 4  ? UNP P62508 ? ? 'expression tag'        211 4  
1 9KNF HIS A 5  ? UNP P62508 ? ? 'expression tag'        212 5  
1 9KNF HIS A 6  ? UNP P62508 ? ? 'expression tag'        213 6  
1 9KNF HIS A 7  ? UNP P62508 ? ? 'expression tag'        214 7  
1 9KNF HIS A 8  ? UNP P62508 ? ? 'expression tag'        215 8  
1 9KNF HIS A 9  ? UNP P62508 ? ? 'expression tag'        216 9  
1 9KNF HIS A 10 ? UNP P62508 ? ? 'expression tag'        217 10 
1 9KNF SER A 11 ? UNP P62508 ? ? 'expression tag'        218 11 
1 9KNF SER A 12 ? UNP P62508 ? ? 'expression tag'        219 12 
1 9KNF GLY A 13 ? UNP P62508 ? ? 'expression tag'        220 13 
1 9KNF LEU A 14 ? UNP P62508 ? ? 'expression tag'        221 14 
1 9KNF VAL A 15 ? UNP P62508 ? ? 'expression tag'        222 15 
1 9KNF PRO A 16 ? UNP P62508 ? ? 'expression tag'        223 16 
1 9KNF ARG A 17 ? UNP P62508 ? ? 'expression tag'        224 17 
1 9KNF GLY A 18 ? UNP P62508 ? ? 'expression tag'        225 18 
1 9KNF SER A 19 ? UNP P62508 ? ? 'expression tag'        226 19 
1 9KNF HIS A 20 ? UNP P62508 ? ? 'expression tag'        227 20 
1 9KNF MET A 21 ? UNP P62508 ? ? 'expression tag'        228 21 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 4270  ? 
1 MORE         -28   ? 
1 'SSA (A^2)'  22010 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z        1.0000000000 0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 8_554 -y,-x,-z-1/2 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -69.4350000000 
# 
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 ASN A 28  ? GLU A 38  ? ASN A 235 GLU A 245 1 ? 11 
HELX_P HELX_P2  AA2 SER A 53  ? LYS A 77  ? SER A 260 LYS A 284 1 ? 25 
HELX_P HELX_P3  AA3 GLY A 81  ? LEU A 85  ? GLY A 288 LEU A 292 5 ? 5  
HELX_P HELX_P4  AA4 SER A 86  ? SER A 110 ? SER A 293 SER A 317 1 ? 25 
HELX_P HELX_P5  AA5 ASP A 126 ? GLY A 134 ? ASP A 333 GLY A 341 1 ? 9  
HELX_P HELX_P6  AA6 LEU A 135 ? MET A 152 ? LEU A 342 MET A 359 1 ? 18 
HELX_P HELX_P7  AA7 GLU A 155 ? ASN A 169 ? GLU A 362 ASN A 376 1 ? 15 
HELX_P HELX_P8  AA8 ASP A 177 ? HIS A 200 ? ASP A 384 HIS A 407 1 ? 24 
HELX_P HELX_P9  AA9 ARG A 205 ? MET A 212 ? ARG A 412 MET A 419 1 ? 8  
HELX_P HELX_P10 AB1 THR A 213 ? GLY A 235 ? THR A 420 GLY A 442 1 ? 23 
HELX_P HELX_P11 AB2 HIS A 240 ? GLU A 248 ? HIS A 447 GLU A 455 1 ? 9  
HELX_P HELX_P12 AB3 SER B 3   ? SER B 11  ? SER C 378 SER C 386 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 117 ? ALA A 120 ? LEU A 324 ALA A 327 
AA1 2 TYR A 123 ? MET A 125 ? TYR A 330 MET A 332 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   LEU 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    117 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    LEU 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     324 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   MET 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    125 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    MET 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     332 
# 
_pdbx_entry_details.entry_id                   9KNF 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  A SER 377 ? ? O A HOH 601 ? ? 1.99 
2 1 ND2 A ASN 235 ? ? O A HOH 602 ? ? 2.14 
# 
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 TYR A 234 ? ? -137.79 -61.71 
2 1 ASN A 235 ? ? -171.22 130.67 
3 1 TYR A 330 ? ? -150.63 80.41  
4 1 ASN A 376 ? ? -97.45  30.42  
5 1 ASP A 384 ? ? -100.92 79.18  
6 1 ASN C 377 ? ? -91.75  35.26  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 208 ? A MET 1   
2  1 Y 1 A GLY 209 ? A GLY 2   
3  1 Y 1 A SER 210 ? A SER 3   
4  1 Y 1 A SER 211 ? A SER 4   
5  1 Y 1 A HIS 212 ? A HIS 5   
6  1 Y 1 A HIS 213 ? A HIS 6   
7  1 Y 1 A HIS 214 ? A HIS 7   
8  1 Y 1 A HIS 215 ? A HIS 8   
9  1 Y 1 A HIS 216 ? A HIS 9   
10 1 Y 1 A HIS 217 ? A HIS 10  
11 1 Y 1 A SER 218 ? A SER 11  
12 1 Y 1 A SER 219 ? A SER 12  
13 1 Y 1 A GLY 220 ? A GLY 13  
14 1 Y 1 A LEU 221 ? A LEU 14  
15 1 Y 1 A VAL 222 ? A VAL 15  
16 1 Y 1 A PRO 223 ? A PRO 16  
17 1 Y 1 A ARG 224 ? A ARG 17  
18 1 Y 1 A GLY 225 ? A GLY 18  
19 1 Y 1 A SER 226 ? A SER 19  
20 1 Y 1 A HIS 227 ? A HIS 20  
21 1 Y 1 A MET 228 ? A MET 21  
22 1 Y 1 A PRO 229 ? A PRO 22  
23 1 Y 1 A ALA 230 ? A ALA 23  
24 1 Y 1 A LYS 231 ? A LYS 24  
25 1 Y 1 A LYS 232 ? A LYS 25  
26 1 Y 1 A VAL 458 ? A VAL 251 
27 1 Y 1 C THR 388 ? B THR 13  
28 1 Y 1 C ILE 389 ? B ILE 14  
29 1 Y 1 C PRO 390 ? B PRO 15  
# 
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 
A1EGB CLAJ CL N N 1   
A1EGB CAE  C  Y N 2   
A1EGB CAD  C  Y N 3   
A1EGB CAB  C  Y N 4   
A1EGB CAA  C  Y N 5   
A1EGB NAH  N  Y N 6   
A1EGB NAI  N  Y N 7   
A1EGB CAC  C  Y N 8   
A1EGB CAG  C  Y N 9   
A1EGB CAF  C  Y N 10  
A1EGB H1   H  N N 11  
A1EGB H2   H  N N 12  
A1EGB H3   H  N N 13  
A1EGB H4   H  N N 14  
A1EGB H5   H  N N 15  
ALA   N    N  N N 16  
ALA   CA   C  N S 17  
ALA   C    C  N N 18  
ALA   O    O  N N 19  
ALA   CB   C  N N 20  
ALA   OXT  O  N N 21  
ALA   H    H  N N 22  
ALA   H2   H  N N 23  
ALA   HA   H  N N 24  
ALA   HB1  H  N N 25  
ALA   HB2  H  N N 26  
ALA   HB3  H  N N 27  
ALA   HXT  H  N N 28  
ARG   N    N  N N 29  
ARG   CA   C  N S 30  
ARG   C    C  N N 31  
ARG   O    O  N N 32  
ARG   CB   C  N N 33  
ARG   CG   C  N N 34  
ARG   CD   C  N N 35  
ARG   NE   N  N N 36  
ARG   CZ   C  N N 37  
ARG   NH1  N  N N 38  
ARG   NH2  N  N N 39  
ARG   OXT  O  N N 40  
ARG   H    H  N N 41  
ARG   H2   H  N N 42  
ARG   HA   H  N N 43  
ARG   HB2  H  N N 44  
ARG   HB3  H  N N 45  
ARG   HG2  H  N N 46  
ARG   HG3  H  N N 47  
ARG   HD2  H  N N 48  
ARG   HD3  H  N N 49  
ARG   HE   H  N N 50  
ARG   HH11 H  N N 51  
ARG   HH12 H  N N 52  
ARG   HH21 H  N N 53  
ARG   HH22 H  N N 54  
ARG   HXT  H  N N 55  
ASN   N    N  N N 56  
ASN   CA   C  N S 57  
ASN   C    C  N N 58  
ASN   O    O  N N 59  
ASN   CB   C  N N 60  
ASN   CG   C  N N 61  
ASN   OD1  O  N N 62  
ASN   ND2  N  N N 63  
ASN   OXT  O  N N 64  
ASN   H    H  N N 65  
ASN   H2   H  N N 66  
ASN   HA   H  N N 67  
ASN   HB2  H  N N 68  
ASN   HB3  H  N N 69  
ASN   HD21 H  N N 70  
ASN   HD22 H  N N 71  
ASN   HXT  H  N N 72  
ASP   N    N  N N 73  
ASP   CA   C  N S 74  
ASP   C    C  N N 75  
ASP   O    O  N N 76  
ASP   CB   C  N N 77  
ASP   CG   C  N N 78  
ASP   OD1  O  N N 79  
ASP   OD2  O  N N 80  
ASP   OXT  O  N N 81  
ASP   H    H  N N 82  
ASP   H2   H  N N 83  
ASP   HA   H  N N 84  
ASP   HB2  H  N N 85  
ASP   HB3  H  N N 86  
ASP   HD2  H  N N 87  
ASP   HXT  H  N N 88  
CYS   N    N  N N 89  
CYS   CA   C  N R 90  
CYS   C    C  N N 91  
CYS   O    O  N N 92  
CYS   CB   C  N N 93  
CYS   SG   S  N N 94  
CYS   OXT  O  N N 95  
CYS   H    H  N N 96  
CYS   H2   H  N N 97  
CYS   HA   H  N N 98  
CYS   HB2  H  N N 99  
CYS   HB3  H  N N 100 
CYS   HG   H  N N 101 
CYS   HXT  H  N N 102 
GLN   N    N  N N 103 
GLN   CA   C  N S 104 
GLN   C    C  N N 105 
GLN   O    O  N N 106 
GLN   CB   C  N N 107 
GLN   CG   C  N N 108 
GLN   CD   C  N N 109 
GLN   OE1  O  N N 110 
GLN   NE2  N  N N 111 
GLN   OXT  O  N N 112 
GLN   H    H  N N 113 
GLN   H2   H  N N 114 
GLN   HA   H  N N 115 
GLN   HB2  H  N N 116 
GLN   HB3  H  N N 117 
GLN   HG2  H  N N 118 
GLN   HG3  H  N N 119 
GLN   HE21 H  N N 120 
GLN   HE22 H  N N 121 
GLN   HXT  H  N N 122 
GLU   N    N  N N 123 
GLU   CA   C  N S 124 
GLU   C    C  N N 125 
GLU   O    O  N N 126 
GLU   CB   C  N N 127 
GLU   CG   C  N N 128 
GLU   CD   C  N N 129 
GLU   OE1  O  N N 130 
GLU   OE2  O  N N 131 
GLU   OXT  O  N N 132 
GLU   H    H  N N 133 
GLU   H2   H  N N 134 
GLU   HA   H  N N 135 
GLU   HB2  H  N N 136 
GLU   HB3  H  N N 137 
GLU   HG2  H  N N 138 
GLU   HG3  H  N N 139 
GLU   HE2  H  N N 140 
GLU   HXT  H  N N 141 
GLY   N    N  N N 142 
GLY   CA   C  N N 143 
GLY   C    C  N N 144 
GLY   O    O  N N 145 
GLY   OXT  O  N N 146 
GLY   H    H  N N 147 
GLY   H2   H  N N 148 
GLY   HA2  H  N N 149 
GLY   HA3  H  N N 150 
GLY   HXT  H  N N 151 
HIS   N    N  N N 152 
HIS   CA   C  N S 153 
HIS   C    C  N N 154 
HIS   O    O  N N 155 
HIS   CB   C  N N 156 
HIS   CG   C  Y N 157 
HIS   ND1  N  Y N 158 
HIS   CD2  C  Y N 159 
HIS   CE1  C  Y N 160 
HIS   NE2  N  Y N 161 
HIS   OXT  O  N N 162 
HIS   H    H  N N 163 
HIS   H2   H  N N 164 
HIS   HA   H  N N 165 
HIS   HB2  H  N N 166 
HIS   HB3  H  N N 167 
HIS   HD1  H  N N 168 
HIS   HD2  H  N N 169 
HIS   HE1  H  N N 170 
HIS   HE2  H  N N 171 
HIS   HXT  H  N N 172 
HOH   O    O  N N 173 
HOH   H1   H  N N 174 
HOH   H2   H  N N 175 
ILE   N    N  N N 176 
ILE   CA   C  N S 177 
ILE   C    C  N N 178 
ILE   O    O  N N 179 
ILE   CB   C  N S 180 
ILE   CG1  C  N N 181 
ILE   CG2  C  N N 182 
ILE   CD1  C  N N 183 
ILE   OXT  O  N N 184 
ILE   H    H  N N 185 
ILE   H2   H  N N 186 
ILE   HA   H  N N 187 
ILE   HB   H  N N 188 
ILE   HG12 H  N N 189 
ILE   HG13 H  N N 190 
ILE   HG21 H  N N 191 
ILE   HG22 H  N N 192 
ILE   HG23 H  N N 193 
ILE   HD11 H  N N 194 
ILE   HD12 H  N N 195 
ILE   HD13 H  N N 196 
ILE   HXT  H  N N 197 
LEU   N    N  N N 198 
LEU   CA   C  N S 199 
LEU   C    C  N N 200 
LEU   O    O  N N 201 
LEU   CB   C  N N 202 
LEU   CG   C  N N 203 
LEU   CD1  C  N N 204 
LEU   CD2  C  N N 205 
LEU   OXT  O  N N 206 
LEU   H    H  N N 207 
LEU   H2   H  N N 208 
LEU   HA   H  N N 209 
LEU   HB2  H  N N 210 
LEU   HB3  H  N N 211 
LEU   HG   H  N N 212 
LEU   HD11 H  N N 213 
LEU   HD12 H  N N 214 
LEU   HD13 H  N N 215 
LEU   HD21 H  N N 216 
LEU   HD22 H  N N 217 
LEU   HD23 H  N N 218 
LEU   HXT  H  N N 219 
LYS   N    N  N N 220 
LYS   CA   C  N S 221 
LYS   C    C  N N 222 
LYS   O    O  N N 223 
LYS   CB   C  N N 224 
LYS   CG   C  N N 225 
LYS   CD   C  N N 226 
LYS   CE   C  N N 227 
LYS   NZ   N  N N 228 
LYS   OXT  O  N N 229 
LYS   H    H  N N 230 
LYS   H2   H  N N 231 
LYS   HA   H  N N 232 
LYS   HB2  H  N N 233 
LYS   HB3  H  N N 234 
LYS   HG2  H  N N 235 
LYS   HG3  H  N N 236 
LYS   HD2  H  N N 237 
LYS   HD3  H  N N 238 
LYS   HE2  H  N N 239 
LYS   HE3  H  N N 240 
LYS   HZ1  H  N N 241 
LYS   HZ2  H  N N 242 
LYS   HZ3  H  N N 243 
LYS   HXT  H  N N 244 
MET   N    N  N N 245 
MET   CA   C  N S 246 
MET   C    C  N N 247 
MET   O    O  N N 248 
MET   CB   C  N N 249 
MET   CG   C  N N 250 
MET   SD   S  N N 251 
MET   CE   C  N N 252 
MET   OXT  O  N N 253 
MET   H    H  N N 254 
MET   H2   H  N N 255 
MET   HA   H  N N 256 
MET   HB2  H  N N 257 
MET   HB3  H  N N 258 
MET   HG2  H  N N 259 
MET   HG3  H  N N 260 
MET   HE1  H  N N 261 
MET   HE2  H  N N 262 
MET   HE3  H  N N 263 
MET   HXT  H  N N 264 
PHE   N    N  N N 265 
PHE   CA   C  N S 266 
PHE   C    C  N N 267 
PHE   O    O  N N 268 
PHE   CB   C  N N 269 
PHE   CG   C  Y N 270 
PHE   CD1  C  Y N 271 
PHE   CD2  C  Y N 272 
PHE   CE1  C  Y N 273 
PHE   CE2  C  Y N 274 
PHE   CZ   C  Y N 275 
PHE   OXT  O  N N 276 
PHE   H    H  N N 277 
PHE   H2   H  N N 278 
PHE   HA   H  N N 279 
PHE   HB2  H  N N 280 
PHE   HB3  H  N N 281 
PHE   HD1  H  N N 282 
PHE   HD2  H  N N 283 
PHE   HE1  H  N N 284 
PHE   HE2  H  N N 285 
PHE   HZ   H  N N 286 
PHE   HXT  H  N N 287 
PRO   N    N  N N 288 
PRO   CA   C  N S 289 
PRO   C    C  N N 290 
PRO   O    O  N N 291 
PRO   CB   C  N N 292 
PRO   CG   C  N N 293 
PRO   CD   C  N N 294 
PRO   OXT  O  N N 295 
PRO   H    H  N N 296 
PRO   HA   H  N N 297 
PRO   HB2  H  N N 298 
PRO   HB3  H  N N 299 
PRO   HG2  H  N N 300 
PRO   HG3  H  N N 301 
PRO   HD2  H  N N 302 
PRO   HD3  H  N N 303 
PRO   HXT  H  N N 304 
SER   N    N  N N 305 
SER   CA   C  N S 306 
SER   C    C  N N 307 
SER   O    O  N N 308 
SER   CB   C  N N 309 
SER   OG   O  N N 310 
SER   OXT  O  N N 311 
SER   H    H  N N 312 
SER   H2   H  N N 313 
SER   HA   H  N N 314 
SER   HB2  H  N N 315 
SER   HB3  H  N N 316 
SER   HG   H  N N 317 
SER   HXT  H  N N 318 
THR   N    N  N N 319 
THR   CA   C  N S 320 
THR   C    C  N N 321 
THR   O    O  N N 322 
THR   CB   C  N R 323 
THR   OG1  O  N N 324 
THR   CG2  C  N N 325 
THR   OXT  O  N N 326 
THR   H    H  N N 327 
THR   H2   H  N N 328 
THR   HA   H  N N 329 
THR   HB   H  N N 330 
THR   HG1  H  N N 331 
THR   HG21 H  N N 332 
THR   HG22 H  N N 333 
THR   HG23 H  N N 334 
THR   HXT  H  N N 335 
TRP   N    N  N N 336 
TRP   CA   C  N S 337 
TRP   C    C  N N 338 
TRP   O    O  N N 339 
TRP   CB   C  N N 340 
TRP   CG   C  Y N 341 
TRP   CD1  C  Y N 342 
TRP   CD2  C  Y N 343 
TRP   NE1  N  Y N 344 
TRP   CE2  C  Y N 345 
TRP   CE3  C  Y N 346 
TRP   CZ2  C  Y N 347 
TRP   CZ3  C  Y N 348 
TRP   CH2  C  Y N 349 
TRP   OXT  O  N N 350 
TRP   H    H  N N 351 
TRP   H2   H  N N 352 
TRP   HA   H  N N 353 
TRP   HB2  H  N N 354 
TRP   HB3  H  N N 355 
TRP   HD1  H  N N 356 
TRP   HE1  H  N N 357 
TRP   HE3  H  N N 358 
TRP   HZ2  H  N N 359 
TRP   HZ3  H  N N 360 
TRP   HH2  H  N N 361 
TRP   HXT  H  N N 362 
TYR   N    N  N N 363 
TYR   CA   C  N S 364 
TYR   C    C  N N 365 
TYR   O    O  N N 366 
TYR   CB   C  N N 367 
TYR   CG   C  Y N 368 
TYR   CD1  C  Y N 369 
TYR   CD2  C  Y N 370 
TYR   CE1  C  Y N 371 
TYR   CE2  C  Y N 372 
TYR   CZ   C  Y N 373 
TYR   OH   O  N N 374 
TYR   OXT  O  N N 375 
TYR   H    H  N N 376 
TYR   H2   H  N N 377 
TYR   HA   H  N N 378 
TYR   HB2  H  N N 379 
TYR   HB3  H  N N 380 
TYR   HD1  H  N N 381 
TYR   HD2  H  N N 382 
TYR   HE1  H  N N 383 
TYR   HE2  H  N N 384 
TYR   HH   H  N N 385 
TYR   HXT  H  N N 386 
VAL   N    N  N N 387 
VAL   CA   C  N S 388 
VAL   C    C  N N 389 
VAL   O    O  N N 390 
VAL   CB   C  N N 391 
VAL   CG1  C  N N 392 
VAL   CG2  C  N N 393 
VAL   OXT  O  N N 394 
VAL   H    H  N N 395 
VAL   H2   H  N N 396 
VAL   HA   H  N N 397 
VAL   HB   H  N N 398 
VAL   HG11 H  N N 399 
VAL   HG12 H  N N 400 
VAL   HG13 H  N N 401 
VAL   HG21 H  N N 402 
VAL   HG22 H  N N 403 
VAL   HG23 H  N N 404 
VAL   HXT  H  N N 405 
# 
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 
A1EGB CLAJ CAE  sing N N 1   
A1EGB CAF  CAG  doub Y N 2   
A1EGB CAF  CAE  sing Y N 3   
A1EGB CAG  CAC  sing Y N 4   
A1EGB CAE  CAD  doub Y N 5   
A1EGB CAC  CAB  sing Y N 6   
A1EGB CAC  NAI  doub Y N 7   
A1EGB CAD  CAB  sing Y N 8   
A1EGB CAB  CAA  doub Y N 9   
A1EGB NAI  NAH  sing Y N 10  
A1EGB CAA  NAH  sing Y N 11  
A1EGB CAD  H1   sing N N 12  
A1EGB CAA  H2   sing N N 13  
A1EGB NAH  H3   sing N N 14  
A1EGB CAG  H4   sing N N 15  
A1EGB CAF  H5   sing N N 16  
ALA   N    CA   sing N N 17  
ALA   N    H    sing N N 18  
ALA   N    H2   sing N N 19  
ALA   CA   C    sing N N 20  
ALA   CA   CB   sing N N 21  
ALA   CA   HA   sing N N 22  
ALA   C    O    doub N N 23  
ALA   C    OXT  sing N N 24  
ALA   CB   HB1  sing N N 25  
ALA   CB   HB2  sing N N 26  
ALA   CB   HB3  sing N N 27  
ALA   OXT  HXT  sing N N 28  
ARG   N    CA   sing N N 29  
ARG   N    H    sing N N 30  
ARG   N    H2   sing N N 31  
ARG   CA   C    sing N N 32  
ARG   CA   CB   sing N N 33  
ARG   CA   HA   sing N N 34  
ARG   C    O    doub N N 35  
ARG   C    OXT  sing N N 36  
ARG   CB   CG   sing N N 37  
ARG   CB   HB2  sing N N 38  
ARG   CB   HB3  sing N N 39  
ARG   CG   CD   sing N N 40  
ARG   CG   HG2  sing N N 41  
ARG   CG   HG3  sing N N 42  
ARG   CD   NE   sing N N 43  
ARG   CD   HD2  sing N N 44  
ARG   CD   HD3  sing N N 45  
ARG   NE   CZ   sing N N 46  
ARG   NE   HE   sing N N 47  
ARG   CZ   NH1  sing N N 48  
ARG   CZ   NH2  doub N N 49  
ARG   NH1  HH11 sing N N 50  
ARG   NH1  HH12 sing N N 51  
ARG   NH2  HH21 sing N N 52  
ARG   NH2  HH22 sing N N 53  
ARG   OXT  HXT  sing N N 54  
ASN   N    CA   sing N N 55  
ASN   N    H    sing N N 56  
ASN   N    H2   sing N N 57  
ASN   CA   C    sing N N 58  
ASN   CA   CB   sing N N 59  
ASN   CA   HA   sing N N 60  
ASN   C    O    doub N N 61  
ASN   C    OXT  sing N N 62  
ASN   CB   CG   sing N N 63  
ASN   CB   HB2  sing N N 64  
ASN   CB   HB3  sing N N 65  
ASN   CG   OD1  doub N N 66  
ASN   CG   ND2  sing N N 67  
ASN   ND2  HD21 sing N N 68  
ASN   ND2  HD22 sing N N 69  
ASN   OXT  HXT  sing N N 70  
ASP   N    CA   sing N N 71  
ASP   N    H    sing N N 72  
ASP   N    H2   sing N N 73  
ASP   CA   C    sing N N 74  
ASP   CA   CB   sing N N 75  
ASP   CA   HA   sing N N 76  
ASP   C    O    doub N N 77  
ASP   C    OXT  sing N N 78  
ASP   CB   CG   sing N N 79  
ASP   CB   HB2  sing N N 80  
ASP   CB   HB3  sing N N 81  
ASP   CG   OD1  doub N N 82  
ASP   CG   OD2  sing N N 83  
ASP   OD2  HD2  sing N N 84  
ASP   OXT  HXT  sing N N 85  
CYS   N    CA   sing N N 86  
CYS   N    H    sing N N 87  
CYS   N    H2   sing N N 88  
CYS   CA   C    sing N N 89  
CYS   CA   CB   sing N N 90  
CYS   CA   HA   sing N N 91  
CYS   C    O    doub N N 92  
CYS   C    OXT  sing N N 93  
CYS   CB   SG   sing N N 94  
CYS   CB   HB2  sing N N 95  
CYS   CB   HB3  sing N N 96  
CYS   SG   HG   sing N N 97  
CYS   OXT  HXT  sing N N 98  
GLN   N    CA   sing N N 99  
GLN   N    H    sing N N 100 
GLN   N    H2   sing N N 101 
GLN   CA   C    sing N N 102 
GLN   CA   CB   sing N N 103 
GLN   CA   HA   sing N N 104 
GLN   C    O    doub N N 105 
GLN   C    OXT  sing N N 106 
GLN   CB   CG   sing N N 107 
GLN   CB   HB2  sing N N 108 
GLN   CB   HB3  sing N N 109 
GLN   CG   CD   sing N N 110 
GLN   CG   HG2  sing N N 111 
GLN   CG   HG3  sing N N 112 
GLN   CD   OE1  doub N N 113 
GLN   CD   NE2  sing N N 114 
GLN   NE2  HE21 sing N N 115 
GLN   NE2  HE22 sing N N 116 
GLN   OXT  HXT  sing N N 117 
GLU   N    CA   sing N N 118 
GLU   N    H    sing N N 119 
GLU   N    H2   sing N N 120 
GLU   CA   C    sing N N 121 
GLU   CA   CB   sing N N 122 
GLU   CA   HA   sing N N 123 
GLU   C    O    doub N N 124 
GLU   C    OXT  sing N N 125 
GLU   CB   CG   sing N N 126 
GLU   CB   HB2  sing N N 127 
GLU   CB   HB3  sing N N 128 
GLU   CG   CD   sing N N 129 
GLU   CG   HG2  sing N N 130 
GLU   CG   HG3  sing N N 131 
GLU   CD   OE1  doub N N 132 
GLU   CD   OE2  sing N N 133 
GLU   OE2  HE2  sing N N 134 
GLU   OXT  HXT  sing N N 135 
GLY   N    CA   sing N N 136 
GLY   N    H    sing N N 137 
GLY   N    H2   sing N N 138 
GLY   CA   C    sing N N 139 
GLY   CA   HA2  sing N N 140 
GLY   CA   HA3  sing N N 141 
GLY   C    O    doub N N 142 
GLY   C    OXT  sing N N 143 
GLY   OXT  HXT  sing N N 144 
HIS   N    CA   sing N N 145 
HIS   N    H    sing N N 146 
HIS   N    H2   sing N N 147 
HIS   CA   C    sing N N 148 
HIS   CA   CB   sing N N 149 
HIS   CA   HA   sing N N 150 
HIS   C    O    doub N N 151 
HIS   C    OXT  sing N N 152 
HIS   CB   CG   sing N N 153 
HIS   CB   HB2  sing N N 154 
HIS   CB   HB3  sing N N 155 
HIS   CG   ND1  sing Y N 156 
HIS   CG   CD2  doub Y N 157 
HIS   ND1  CE1  doub Y N 158 
HIS   ND1  HD1  sing N N 159 
HIS   CD2  NE2  sing Y N 160 
HIS   CD2  HD2  sing N N 161 
HIS   CE1  NE2  sing Y N 162 
HIS   CE1  HE1  sing N N 163 
HIS   NE2  HE2  sing N N 164 
HIS   OXT  HXT  sing N N 165 
HOH   O    H1   sing N N 166 
HOH   O    H2   sing N N 167 
ILE   N    CA   sing N N 168 
ILE   N    H    sing N N 169 
ILE   N    H2   sing N N 170 
ILE   CA   C    sing N N 171 
ILE   CA   CB   sing N N 172 
ILE   CA   HA   sing N N 173 
ILE   C    O    doub N N 174 
ILE   C    OXT  sing N N 175 
ILE   CB   CG1  sing N N 176 
ILE   CB   CG2  sing N N 177 
ILE   CB   HB   sing N N 178 
ILE   CG1  CD1  sing N N 179 
ILE   CG1  HG12 sing N N 180 
ILE   CG1  HG13 sing N N 181 
ILE   CG2  HG21 sing N N 182 
ILE   CG2  HG22 sing N N 183 
ILE   CG2  HG23 sing N N 184 
ILE   CD1  HD11 sing N N 185 
ILE   CD1  HD12 sing N N 186 
ILE   CD1  HD13 sing N N 187 
ILE   OXT  HXT  sing N N 188 
LEU   N    CA   sing N N 189 
LEU   N    H    sing N N 190 
LEU   N    H2   sing N N 191 
LEU   CA   C    sing N N 192 
LEU   CA   CB   sing N N 193 
LEU   CA   HA   sing N N 194 
LEU   C    O    doub N N 195 
LEU   C    OXT  sing N N 196 
LEU   CB   CG   sing N N 197 
LEU   CB   HB2  sing N N 198 
LEU   CB   HB3  sing N N 199 
LEU   CG   CD1  sing N N 200 
LEU   CG   CD2  sing N N 201 
LEU   CG   HG   sing N N 202 
LEU   CD1  HD11 sing N N 203 
LEU   CD1  HD12 sing N N 204 
LEU   CD1  HD13 sing N N 205 
LEU   CD2  HD21 sing N N 206 
LEU   CD2  HD22 sing N N 207 
LEU   CD2  HD23 sing N N 208 
LEU   OXT  HXT  sing N N 209 
LYS   N    CA   sing N N 210 
LYS   N    H    sing N N 211 
LYS   N    H2   sing N N 212 
LYS   CA   C    sing N N 213 
LYS   CA   CB   sing N N 214 
LYS   CA   HA   sing N N 215 
LYS   C    O    doub N N 216 
LYS   C    OXT  sing N N 217 
LYS   CB   CG   sing N N 218 
LYS   CB   HB2  sing N N 219 
LYS   CB   HB3  sing N N 220 
LYS   CG   CD   sing N N 221 
LYS   CG   HG2  sing N N 222 
LYS   CG   HG3  sing N N 223 
LYS   CD   CE   sing N N 224 
LYS   CD   HD2  sing N N 225 
LYS   CD   HD3  sing N N 226 
LYS   CE   NZ   sing N N 227 
LYS   CE   HE2  sing N N 228 
LYS   CE   HE3  sing N N 229 
LYS   NZ   HZ1  sing N N 230 
LYS   NZ   HZ2  sing N N 231 
LYS   NZ   HZ3  sing N N 232 
LYS   OXT  HXT  sing N N 233 
MET   N    CA   sing N N 234 
MET   N    H    sing N N 235 
MET   N    H2   sing N N 236 
MET   CA   C    sing N N 237 
MET   CA   CB   sing N N 238 
MET   CA   HA   sing N N 239 
MET   C    O    doub N N 240 
MET   C    OXT  sing N N 241 
MET   CB   CG   sing N N 242 
MET   CB   HB2  sing N N 243 
MET   CB   HB3  sing N N 244 
MET   CG   SD   sing N N 245 
MET   CG   HG2  sing N N 246 
MET   CG   HG3  sing N N 247 
MET   SD   CE   sing N N 248 
MET   CE   HE1  sing N N 249 
MET   CE   HE2  sing N N 250 
MET   CE   HE3  sing N N 251 
MET   OXT  HXT  sing N N 252 
PHE   N    CA   sing N N 253 
PHE   N    H    sing N N 254 
PHE   N    H2   sing N N 255 
PHE   CA   C    sing N N 256 
PHE   CA   CB   sing N N 257 
PHE   CA   HA   sing N N 258 
PHE   C    O    doub N N 259 
PHE   C    OXT  sing N N 260 
PHE   CB   CG   sing N N 261 
PHE   CB   HB2  sing N N 262 
PHE   CB   HB3  sing N N 263 
PHE   CG   CD1  doub Y N 264 
PHE   CG   CD2  sing Y N 265 
PHE   CD1  CE1  sing Y N 266 
PHE   CD1  HD1  sing N N 267 
PHE   CD2  CE2  doub Y N 268 
PHE   CD2  HD2  sing N N 269 
PHE   CE1  CZ   doub Y N 270 
PHE   CE1  HE1  sing N N 271 
PHE   CE2  CZ   sing Y N 272 
PHE   CE2  HE2  sing N N 273 
PHE   CZ   HZ   sing N N 274 
PHE   OXT  HXT  sing N N 275 
PRO   N    CA   sing N N 276 
PRO   N    CD   sing N N 277 
PRO   N    H    sing N N 278 
PRO   CA   C    sing N N 279 
PRO   CA   CB   sing N N 280 
PRO   CA   HA   sing N N 281 
PRO   C    O    doub N N 282 
PRO   C    OXT  sing N N 283 
PRO   CB   CG   sing N N 284 
PRO   CB   HB2  sing N N 285 
PRO   CB   HB3  sing N N 286 
PRO   CG   CD   sing N N 287 
PRO   CG   HG2  sing N N 288 
PRO   CG   HG3  sing N N 289 
PRO   CD   HD2  sing N N 290 
PRO   CD   HD3  sing N N 291 
PRO   OXT  HXT  sing N N 292 
SER   N    CA   sing N N 293 
SER   N    H    sing N N 294 
SER   N    H2   sing N N 295 
SER   CA   C    sing N N 296 
SER   CA   CB   sing N N 297 
SER   CA   HA   sing N N 298 
SER   C    O    doub N N 299 
SER   C    OXT  sing N N 300 
SER   CB   OG   sing N N 301 
SER   CB   HB2  sing N N 302 
SER   CB   HB3  sing N N 303 
SER   OG   HG   sing N N 304 
SER   OXT  HXT  sing N N 305 
THR   N    CA   sing N N 306 
THR   N    H    sing N N 307 
THR   N    H2   sing N N 308 
THR   CA   C    sing N N 309 
THR   CA   CB   sing N N 310 
THR   CA   HA   sing N N 311 
THR   C    O    doub N N 312 
THR   C    OXT  sing N N 313 
THR   CB   OG1  sing N N 314 
THR   CB   CG2  sing N N 315 
THR   CB   HB   sing N N 316 
THR   OG1  HG1  sing N N 317 
THR   CG2  HG21 sing N N 318 
THR   CG2  HG22 sing N N 319 
THR   CG2  HG23 sing N N 320 
THR   OXT  HXT  sing N N 321 
TRP   N    CA   sing N N 322 
TRP   N    H    sing N N 323 
TRP   N    H2   sing N N 324 
TRP   CA   C    sing N N 325 
TRP   CA   CB   sing N N 326 
TRP   CA   HA   sing N N 327 
TRP   C    O    doub N N 328 
TRP   C    OXT  sing N N 329 
TRP   CB   CG   sing N N 330 
TRP   CB   HB2  sing N N 331 
TRP   CB   HB3  sing N N 332 
TRP   CG   CD1  doub Y N 333 
TRP   CG   CD2  sing Y N 334 
TRP   CD1  NE1  sing Y N 335 
TRP   CD1  HD1  sing N N 336 
TRP   CD2  CE2  doub Y N 337 
TRP   CD2  CE3  sing Y N 338 
TRP   NE1  CE2  sing Y N 339 
TRP   NE1  HE1  sing N N 340 
TRP   CE2  CZ2  sing Y N 341 
TRP   CE3  CZ3  doub Y N 342 
TRP   CE3  HE3  sing N N 343 
TRP   CZ2  CH2  doub Y N 344 
TRP   CZ2  HZ2  sing N N 345 
TRP   CZ3  CH2  sing Y N 346 
TRP   CZ3  HZ3  sing N N 347 
TRP   CH2  HH2  sing N N 348 
TRP   OXT  HXT  sing N N 349 
TYR   N    CA   sing N N 350 
TYR   N    H    sing N N 351 
TYR   N    H2   sing N N 352 
TYR   CA   C    sing N N 353 
TYR   CA   CB   sing N N 354 
TYR   CA   HA   sing N N 355 
TYR   C    O    doub N N 356 
TYR   C    OXT  sing N N 357 
TYR   CB   CG   sing N N 358 
TYR   CB   HB2  sing N N 359 
TYR   CB   HB3  sing N N 360 
TYR   CG   CD1  doub Y N 361 
TYR   CG   CD2  sing Y N 362 
TYR   CD1  CE1  sing Y N 363 
TYR   CD1  HD1  sing N N 364 
TYR   CD2  CE2  doub Y N 365 
TYR   CD2  HD2  sing N N 366 
TYR   CE1  CZ   doub Y N 367 
TYR   CE1  HE1  sing N N 368 
TYR   CE2  CZ   sing Y N 369 
TYR   CE2  HE2  sing N N 370 
TYR   CZ   OH   sing N N 371 
TYR   OH   HH   sing N N 372 
TYR   OXT  HXT  sing N N 373 
VAL   N    CA   sing N N 374 
VAL   N    H    sing N N 375 
VAL   N    H2   sing N N 376 
VAL   CA   C    sing N N 377 
VAL   CA   CB   sing N N 378 
VAL   CA   HA   sing N N 379 
VAL   C    O    doub N N 380 
VAL   C    OXT  sing N N 381 
VAL   CB   CG1  sing N N 382 
VAL   CB   CG2  sing N N 383 
VAL   CB   HB   sing N N 384 
VAL   CG1  HG11 sing N N 385 
VAL   CG1  HG12 sing N N 386 
VAL   CG1  HG13 sing N N 387 
VAL   CG2  HG21 sing N N 388 
VAL   CG2  HG22 sing N N 389 
VAL   CG2  HG23 sing N N 390 
VAL   OXT  HXT  sing N N 391 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2GPO 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KNF 
_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]   0.015576 
_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]   0.015576 
_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]   0.007201 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . PRO   A 1 26  ? 6.075   -29.785 -24.359 1.00 115.24 ? 233 PRO   A N    1 
ATOM   2    C  CA   . PRO   A 1 26  ? 7.264   -28.961 -24.081 1.00 99.61  ? 233 PRO   A CA   1 
ATOM   3    C  C    . PRO   A 1 26  ? 7.364   -27.790 -25.065 1.00 111.06 ? 233 PRO   A C    1 
ATOM   4    O  O    . PRO   A 1 26  ? 7.649   -28.076 -26.220 1.00 114.25 ? 233 PRO   A O    1 
ATOM   5    C  CB   . PRO   A 1 26  ? 8.440   -29.926 -24.316 1.00 103.25 ? 233 PRO   A CB   1 
ATOM   6    C  CG   . PRO   A 1 26  ? 7.877   -31.272 -23.944 1.00 87.12  ? 233 PRO   A CG   1 
ATOM   7    C  CD   . PRO   A 1 26  ? 6.373   -31.161 -23.947 1.00 103.91 ? 233 PRO   A CD   1 
ATOM   8    N  N    . TYR   A 1 27  ? 7.121   -26.540 -24.637 1.00 98.69  ? 234 TYR   A N    1 
ATOM   9    C  CA   . TYR   A 1 27  ? 7.361   -25.363 -25.519 1.00 72.06  ? 234 TYR   A CA   1 
ATOM   10   C  C    . TYR   A 1 27  ? 8.024   -24.179 -24.803 1.00 70.45  ? 234 TYR   A C    1 
ATOM   11   O  O    . TYR   A 1 27  ? 9.134   -23.735 -25.253 1.00 72.44  ? 234 TYR   A O    1 
ATOM   12   C  CB   . TYR   A 1 27  ? 6.106   -24.896 -26.259 1.00 82.21  ? 234 TYR   A CB   1 
ATOM   13   C  CG   . TYR   A 1 27  ? 4.727   -25.251 -25.759 1.00 93.56  ? 234 TYR   A CG   1 
ATOM   14   C  CD1  . TYR   A 1 27  ? 4.096   -24.494 -24.784 1.00 57.24  ? 234 TYR   A CD1  1 
ATOM   15   C  CD2  . TYR   A 1 27  ? 3.969   -26.218 -26.404 1.00 84.24  ? 234 TYR   A CD2  1 
ATOM   16   C  CE1  . TYR   A 1 27  ? 2.796   -24.733 -24.392 1.00 73.29  ? 234 TYR   A CE1  1 
ATOM   17   C  CE2  . TYR   A 1 27  ? 2.656   -26.460 -26.044 1.00 94.22  ? 234 TYR   A CE2  1 
ATOM   18   C  CZ   . TYR   A 1 27  ? 2.063   -25.727 -25.020 1.00 80.64  ? 234 TYR   A CZ   1 
ATOM   19   O  OH   . TYR   A 1 27  ? 0.758   -25.919 -24.628 1.00 73.16  ? 234 TYR   A OH   1 
ATOM   20   N  N    . ASN   A 1 28  ? 7.341   -23.637 -23.795 1.00 55.24  ? 235 ASN   A N    1 
ATOM   21   C  CA   . ASN   A 1 28  ? 7.766   -22.437 -23.027 1.00 47.31  ? 235 ASN   A CA   1 
ATOM   22   C  C    . ASN   A 1 28  ? 6.812   -22.303 -21.839 1.00 41.18  ? 235 ASN   A C    1 
ATOM   23   O  O    . ASN   A 1 28  ? 5.588   -22.368 -22.076 1.00 62.30  ? 235 ASN   A O    1 
ATOM   24   C  CB   . ASN   A 1 28  ? 7.702   -21.159 -23.865 1.00 51.64  ? 235 ASN   A CB   1 
ATOM   25   C  CG   . ASN   A 1 28  ? 8.350   -19.988 -23.168 1.00 54.76  ? 235 ASN   A CG   1 
ATOM   26   O  OD1  . ASN   A 1 28  ? 7.865   -19.514 -22.144 1.00 65.65  ? 235 ASN   A OD1  1 
ATOM   27   N  ND2  . ASN   A 1 28  ? 9.442   -19.500 -23.719 1.00 67.41  ? 235 ASN   A ND2  1 
ATOM   28   N  N    . LYS   A 1 29  ? 7.319   -22.129 -20.620 1.00 28.85  ? 236 LYS   A N    1 
ATOM   29   C  CA   . LYS   A 1 29  ? 6.467   -22.220 -19.420 1.00 21.29  ? 236 LYS   A CA   1 
ATOM   30   C  C    . LYS   A 1 29  ? 5.543   -20.995 -19.355 1.00 21.72  ? 236 LYS   A C    1 
ATOM   31   O  O    . LYS   A 1 29  ? 4.454   -21.097 -18.818 1.00 20.66  ? 236 LYS   A O    1 
ATOM   32   C  CB   . LYS   A 1 29  ? 7.273   -22.382 -18.138 1.00 24.30  ? 236 LYS   A CB   1 
ATOM   33   C  CG   . LYS   A 1 29  ? 6.439   -22.442 -16.855 1.00 24.70  ? 236 LYS   A CG   1 
ATOM   34   C  CD   . LYS   A 1 29  ? 5.690   -23.735 -16.692 1.00 27.16  ? 236 LYS   A CD   1 
ATOM   35   C  CE   . LYS   A 1 29  ? 4.954   -23.923 -15.376 1.00 36.96  ? 236 LYS   A CE   1 
ATOM   36   N  NZ   . LYS   A 1 29  ? 5.824   -23.991 -14.179 1.00 34.67  ? 236 LYS   A NZ   1 
ATOM   37   N  N    . ILE   A 1 30  ? 6.004   -19.875 -19.879 1.00 20.77  ? 237 ILE   A N    1 
ATOM   38   C  CA   . ILE   A 1 30  ? 5.196   -18.630 -19.894 1.00 20.09  ? 237 ILE   A CA   1 
ATOM   39   C  C    . ILE   A 1 30  ? 3.959   -18.906 -20.752 1.00 18.15  ? 237 ILE   A C    1 
ATOM   40   O  O    . ILE   A 1 30  ? 2.840   -18.574 -20.348 1.00 20.41  ? 237 ILE   A O    1 
ATOM   41   C  CB   . ILE   A 1 30  ? 6.029   -17.426 -20.360 1.00 23.27  ? 237 ILE   A CB   1 
ATOM   42   C  CG1  . ILE   A 1 30  ? 7.091   -17.120 -19.305 1.00 24.58  ? 237 ILE   A CG1  1 
ATOM   43   C  CG2  . ILE   A 1 30  ? 5.106   -16.259 -20.665 1.00 25.17  ? 237 ILE   A CG2  1 
ATOM   44   C  CD1  . ILE   A 1 30  ? 7.986   -15.922 -19.646 1.00 27.94  ? 237 ILE   A CD1  1 
ATOM   45   N  N    . VAL   A 1 31  ? 4.159   -19.529 -21.885 1.00 20.37  ? 238 VAL   A N    1 
ATOM   46   C  CA   . VAL   A 1 31  ? 3.026   -19.873 -22.754 1.00 20.79  ? 238 VAL   A CA   1 
ATOM   47   C  C    . VAL   A 1 31  ? 2.059   -20.783 -21.959 1.00 18.54  ? 238 VAL   A C    1 
ATOM   48   O  O    . VAL   A 1 31  ? 0.860   -20.499 -22.005 1.00 19.14  ? 238 VAL   A O    1 
ATOM   49   C  CB   . VAL   A 1 31  ? 3.450   -20.455 -24.107 1.00 22.31  ? 238 VAL   A CB   1 
ATOM   50   C  CG1  . VAL   A 1 31  ? 2.240   -20.895 -24.956 1.00 23.12  ? 238 VAL   A CG1  1 
ATOM   51   C  CG2  . VAL   A 1 31  ? 4.282   -19.430 -24.832 1.00 21.91  ? 238 VAL   A CG2  1 
ATOM   52   N  N    . SER   A 1 32  ? 2.547   -21.870 -21.374 1.00 21.35  ? 239 SER   A N    1 
ATOM   53   C  CA   . SER   A 1 32  ? 1.742   -22.797 -20.530 1.00 21.62  ? 239 SER   A CA   1 
ATOM   54   C  C    . SER   A 1 32  ? 0.963   -21.994 -19.506 1.00 20.00  ? 239 SER   A C    1 
ATOM   55   O  O    . SER   A 1 32  ? -0.258  -22.257 -19.331 1.00 20.44  ? 239 SER   A O    1 
ATOM   56   C  CB   . SER   A 1 32  ? 2.592   -23.849 -19.831 1.00 29.12  ? 239 SER   A CB   1 
ATOM   57   O  OG   . SER   A 1 32  ? 3.080   -24.708 -20.808 1.00 33.67  ? 239 SER   A OG   1 
ATOM   58   N  N    . HIS   A 1 33  ? 1.633   -21.061 -18.845 1.00 18.67  ? 240 HIS   A N    1 
ATOM   59   C  CA   . HIS   A 1 33  ? 1.059   -20.324 -17.704 1.00 17.68  ? 240 HIS   A CA   1 
ATOM   60   C  C    . HIS   A 1 33  ? -0.046  -19.418 -18.270 1.00 16.72  ? 240 HIS   A C    1 
ATOM   61   O  O    . HIS   A 1 33  ? -1.147  -19.367 -17.676 1.00 20.38  ? 240 HIS   A O    1 
ATOM   62   C  CB   . HIS   A 1 33  ? 2.171   -19.505 -17.020 1.00 19.17  ? 240 HIS   A CB   1 
ATOM   63   C  CG   . HIS   A 1 33  ? 1.717   -18.854 -15.756 1.00 18.91  ? 240 HIS   A CG   1 
ATOM   64   N  ND1  . HIS   A 1 33  ? 1.314   -19.582 -14.648 1.00 28.09  ? 240 HIS   A ND1  1 
ATOM   65   C  CD2  . HIS   A 1 33  ? 1.508   -17.555 -15.457 1.00 24.15  ? 240 HIS   A CD2  1 
ATOM   66   C  CE1  . HIS   A 1 33  ? 0.913   -18.749 -13.697 1.00 24.97  ? 240 HIS   A CE1  1 
ATOM   67   N  NE2  . HIS   A 1 33  ? 1.036   -17.503 -14.171 1.00 29.45  ? 240 HIS   A NE2  1 
ATOM   68   N  N    . LEU   A 1 34  ? 0.192   -18.760 -19.408 1.00 17.22  ? 241 LEU   A N    1 
ATOM   69   C  CA   . LEU   A 1 34  ? -0.835  -17.885 -19.991 1.00 18.73  ? 241 LEU   A CA   1 
ATOM   70   C  C    . LEU   A 1 34  ? -2.064  -18.733 -20.379 1.00 19.61  ? 241 LEU   A C    1 
ATOM   71   O  O    . LEU   A 1 34  ? -3.231  -18.270 -20.207 1.00 19.65  ? 241 LEU   A O    1 
ATOM   72   C  CB   . LEU   A 1 34  ? -0.280  -17.103 -21.184 1.00 18.09  ? 241 LEU   A CB   1 
ATOM   73   C  CG   . LEU   A 1 34  ? 0.716   -16.030 -20.808 1.00 20.94  ? 241 LEU   A CG   1 
ATOM   74   C  CD1  . LEU   A 1 34  ? 1.312   -15.383 -22.056 1.00 19.34  ? 241 LEU   A CD1  1 
ATOM   75   C  CD2  . LEU   A 1 34  ? 0.088   -15.017 -19.868 1.00 25.38  ? 241 LEU   A CD2  1 
ATOM   76   N  N    . LEU   A 1 35  ? -1.855  -19.953 -20.862 1.00 18.00  ? 242 LEU   A N    1 
ATOM   77   C  CA   . LEU   A 1 35  ? -3.014  -20.744 -21.292 1.00 21.62  ? 242 LEU   A CA   1 
ATOM   78   C  C    . LEU   A 1 35  ? -3.853  -21.037 -20.067 1.00 18.92  ? 242 LEU   A C    1 
ATOM   79   O  O    . LEU   A 1 35  ? -5.104  -21.035 -20.225 1.00 23.30  ? 242 LEU   A O    1 
ATOM   80   C  CB   . LEU   A 1 35  ? -2.561  -22.028 -21.954 1.00 21.32  ? 242 LEU   A CB   1 
ATOM   81   C  CG   . LEU   A 1 35  ? -2.090  -21.908 -23.396 1.00 26.62  ? 242 LEU   A CG   1 
ATOM   82   C  CD1  . LEU   A 1 35  ? -1.430  -23.229 -23.816 1.00 29.74  ? 242 LEU   A CD1  1 
ATOM   83   C  CD2  . LEU   A 1 35  ? -3.218  -21.522 -24.339 1.00 26.17  ? 242 LEU   A CD2  1 
ATOM   84   N  N    . VAL   A 1 36  ? -3.289  -21.346 -18.916 1.00 21.14  ? 243 VAL   A N    1 
ATOM   85   C  CA   . VAL   A 1 36  ? -4.128  -21.745 -17.739 1.00 25.45  ? 243 VAL   A CA   1 
ATOM   86   C  C    . VAL   A 1 36  ? -4.697  -20.478 -17.133 1.00 24.88  ? 243 VAL   A C    1 
ATOM   87   O  O    . VAL   A 1 36  ? -5.686  -20.585 -16.425 1.00 30.32  ? 243 VAL   A O    1 
ATOM   88   C  CB   . VAL   A 1 36  ? -3.435  -22.586 -16.654 1.00 27.12  ? 243 VAL   A CB   1 
ATOM   89   C  CG1  . VAL   A 1 36  ? -3.029  -23.920 -17.218 1.00 30.97  ? 243 VAL   A CG1  1 
ATOM   90   C  CG2  . VAL   A 1 36  ? -2.274  -21.893 -15.989 1.00 30.42  ? 243 VAL   A CG2  1 
ATOM   91   N  N    . ALA   A 1 37  ? -4.090  -19.322 -17.399 1.00 27.17  ? 244 ALA   A N    1 
ATOM   92   C  CA   . ALA   A 1 37  ? -4.615  -18.047 -16.879 1.00 23.99  ? 244 ALA   A CA   1 
ATOM   93   C  C    . ALA   A 1 37  ? -5.791  -17.580 -17.737 1.00 23.32  ? 244 ALA   A C    1 
ATOM   94   O  O    . ALA   A 1 37  ? -6.430  -16.576 -17.317 1.00 23.42  ? 244 ALA   A O    1 
ATOM   95   C  CB   . ALA   A 1 37  ? -3.542  -17.028 -16.829 1.00 27.68  ? 244 ALA   A CB   1 
ATOM   96   N  N    . GLU   A 1 38  ? -6.029  -18.188 -18.896 1.00 22.26  ? 245 GLU   A N    1 
ATOM   97   C  CA   . GLU   A 1 38  ? -7.061  -17.698 -19.850 1.00 24.49  ? 245 GLU   A CA   1 
ATOM   98   C  C    . GLU   A 1 38  ? -8.418  -17.678 -19.135 1.00 28.54  ? 245 GLU   A C    1 
ATOM   99   O  O    . GLU   A 1 38  ? -8.822  -18.628 -18.519 1.00 28.22  ? 245 GLU   A O    1 
ATOM   100  C  CB   . GLU   A 1 38  ? -7.064  -18.490 -21.157 1.00 25.77  ? 245 GLU   A CB   1 
ATOM   101  C  CG   . GLU   A 1 38  ? -8.063  -17.959 -22.145 1.00 32.53  ? 245 GLU   A CG   1 
ATOM   102  C  CD   . GLU   A 1 38  ? -7.643  -16.668 -22.823 1.00 38.12  ? 245 GLU   A CD   1 
ATOM   103  O  OE1  . GLU   A 1 38  ? -6.582  -16.098 -22.452 1.00 30.03  ? 245 GLU   A OE1  1 
ATOM   104  O  OE2  . GLU   A 1 38  ? -8.383  -16.224 -23.705 1.00 46.54  ? 245 GLU   A OE2  1 
ATOM   105  N  N    . PRO   A 1 39  ? -9.095  -16.522 -19.061 1.00 27.44  ? 246 PRO   A N    1 
ATOM   106  C  CA   . PRO   A 1 39  ? -10.435 -16.416 -18.455 1.00 24.08  ? 246 PRO   A CA   1 
ATOM   107  C  C    . PRO   A 1 39  ? -11.499 -17.279 -19.139 1.00 26.43  ? 246 PRO   A C    1 
ATOM   108  O  O    . PRO   A 1 39  ? -11.362 -17.476 -20.326 1.00 24.81  ? 246 PRO   A O    1 
ATOM   109  C  CB   . PRO   A 1 39  ? -10.793 -14.952 -18.647 1.00 29.33  ? 246 PRO   A CB   1 
ATOM   110  C  CG   . PRO   A 1 39  ? -9.443  -14.248 -18.765 1.00 36.31  ? 246 PRO   A CG   1 
ATOM   111  C  CD   . PRO   A 1 39  ? -8.608  -15.229 -19.557 1.00 35.60  ? 246 PRO   A CD   1 
ATOM   112  N  N    . GLU   A 1 40  ? -12.500 -17.714 -18.368 1.00 26.97  ? 247 GLU   A N    1 
ATOM   113  C  CA   . GLU   A 1 40  ? -13.706 -18.435 -18.835 1.00 29.15  ? 247 GLU   A CA   1 
ATOM   114  C  C    . GLU   A 1 40  ? -14.530 -17.522 -19.764 1.00 21.39  ? 247 GLU   A C    1 
ATOM   115  O  O    . GLU   A 1 40  ? -14.401 -16.277 -19.717 1.00 25.56  ? 247 GLU   A O    1 
ATOM   116  C  CB   . GLU   A 1 40  ? -14.513 -18.911 -17.617 1.00 33.77  ? 247 GLU   A CB   1 
ATOM   117  C  CG   . GLU   A 1 40  ? -13.748 -19.944 -16.765 1.00 37.34  ? 247 GLU   A CG   1 
ATOM   118  C  CD   . GLU   A 1 40  ? -13.519 -21.256 -17.500 1.00 43.06  ? 247 GLU   A CD   1 
ATOM   119  O  OE1  . GLU   A 1 40  ? -14.442 -21.601 -18.253 1.00 51.57  ? 247 GLU   A OE1  1 
ATOM   120  O  OE2  . GLU   A 1 40  ? -12.404 -21.898 -17.381 1.00 60.33  ? 247 GLU   A OE2  1 
ATOM   121  N  N    . LYS   A 1 41  ? -15.195 -18.167 -20.710 1.00 27.50  ? 248 LYS   A N    1 
ATOM   122  C  CA   . LYS   A 1 41  ? -16.244 -17.591 -21.606 1.00 27.97  ? 248 LYS   A CA   1 
ATOM   123  C  C    . LYS   A 1 41  ? -17.264 -16.766 -20.805 1.00 27.14  ? 248 LYS   A C    1 
ATOM   124  O  O    . LYS   A 1 41  ? -17.582 -17.162 -19.709 1.00 31.88  ? 248 LYS   A O    1 
ATOM   125  C  CB   . LYS   A 1 41  ? -16.910 -18.720 -22.391 1.00 38.96  ? 248 LYS   A CB   1 
ATOM   126  C  CG   . LYS   A 1 41  ? -16.188 -19.028 -23.687 1.00 44.76  ? 248 LYS   A CG   1 
ATOM   127  C  CD   . LYS   A 1 41  ? -16.661 -20.268 -24.403 1.00 57.31  ? 248 LYS   A CD   1 
ATOM   128  C  CE   . LYS   A 1 41  ? -15.900 -20.466 -25.697 1.00 76.00  ? 248 LYS   A CE   1 
ATOM   129  N  NZ   . LYS   A 1 41  ? -16.499 -21.532 -26.536 1.00 70.65  ? 248 LYS   A NZ   1 
ATOM   130  N  N    . ILE   A 1 42  ? -17.648 -15.599 -21.349 1.00 23.37  ? 249 ILE   A N    1 
ATOM   131  C  CA   . ILE   A 1 42  ? -18.640 -14.597 -20.828 1.00 30.57  ? 249 ILE   A CA   1 
ATOM   132  C  C    . ILE   A 1 42  ? -19.761 -14.542 -21.871 1.00 25.76  ? 249 ILE   A C    1 
ATOM   133  O  O    . ILE   A 1 42  ? -19.460 -14.459 -23.089 1.00 32.98  ? 249 ILE   A O    1 
ATOM   134  C  CB   . ILE   A 1 42  ? -17.993 -13.195 -20.570 1.00 30.58  ? 249 ILE   A CB   1 
ATOM   135  C  CG1  . ILE   A 1 42  ? -16.909 -13.253 -19.483 1.00 34.15  ? 249 ILE   A CG1  1 
ATOM   136  C  CG2  . ILE   A 1 42  ? -19.037 -12.173 -20.181 1.00 35.35  ? 249 ILE   A CG2  1 
ATOM   137  C  CD1  . ILE   A 1 42  ? -15.970 -12.019 -19.414 1.00 47.22  ? 249 ILE   A CD1  1 
ATOM   138  N  N    . TYR   A 1 43  ? -21.006 -14.639 -21.414 1.00 26.47  ? 250 TYR   A N    1 
ATOM   139  C  CA   . TYR   A 1 43  ? -22.221 -14.487 -22.254 1.00 29.12  ? 250 TYR   A CA   1 
ATOM   140  C  C    . TYR   A 1 43  ? -22.598 -12.995 -22.336 1.00 25.06  ? 250 TYR   A C    1 
ATOM   141  O  O    . TYR   A 1 43  ? -22.557 -12.286 -21.285 1.00 25.65  ? 250 TYR   A O    1 
ATOM   142  C  CB   . TYR   A 1 43  ? -23.368 -15.341 -21.701 1.00 34.25  ? 250 TYR   A CB   1 
ATOM   143  C  CG   . TYR   A 1 43  ? -23.209 -16.832 -21.911 1.00 46.47  ? 250 TYR   A CG   1 
ATOM   144  C  CD1  . TYR   A 1 43  ? -23.559 -17.431 -23.122 1.00 41.29  ? 250 TYR   A CD1  1 
ATOM   145  C  CD2  . TYR   A 1 43  ? -22.678 -17.650 -20.914 1.00 54.14  ? 250 TYR   A CD2  1 
ATOM   146  C  CE1  . TYR   A 1 43  ? -23.390 -18.794 -23.338 1.00 58.77  ? 250 TYR   A CE1  1 
ATOM   147  C  CE2  . TYR   A 1 43  ? -22.520 -19.017 -21.108 1.00 64.63  ? 250 TYR   A CE2  1 
ATOM   148  C  CZ   . TYR   A 1 43  ? -22.879 -19.587 -22.323 1.00 68.45  ? 250 TYR   A CZ   1 
ATOM   149  O  OH   . TYR   A 1 43  ? -22.724 -20.929 -22.537 1.00 88.75  ? 250 TYR   A OH   1 
ATOM   150  N  N    . ALA   A 1 44  ? -22.988 -12.554 -23.536 1.00 22.49  ? 251 ALA   A N    1 
ATOM   151  C  CA   . ALA   A 1 44  ? -23.551 -11.203 -23.803 1.00 22.80  ? 251 ALA   A CA   1 
ATOM   152  C  C    . ALA   A 1 44  ? -24.888 -11.004 -23.073 1.00 21.46  ? 251 ALA   A C    1 
ATOM   153  O  O    . ALA   A 1 44  ? -25.045 -9.965  -22.435 1.00 20.49  ? 251 ALA   A O    1 
ATOM   154  C  CB   . ALA   A 1 44  ? -23.709 -10.998 -25.265 1.00 21.63  ? 251 ALA   A CB   1 
ATOM   155  N  N    . MET   A 1 45  ? -25.751 -12.012 -23.086 1.00 19.72  ? 252 MET   A N    1 
ATOM   156  C  CA   . MET   A 1 45  ? -27.132 -11.964 -22.507 1.00 20.31  ? 252 MET   A CA   1 
ATOM   157  C  C    . MET   A 1 45  ? -27.833 -10.666 -22.894 1.00 20.48  ? 252 MET   A C    1 
ATOM   158  O  O    . MET   A 1 45  ? -28.291 -9.914  -22.041 1.00 22.01  ? 252 MET   A O    1 
ATOM   159  C  CB   . MET   A 1 45  ? -27.118 -12.093 -20.974 1.00 25.53  ? 252 MET   A CB   1 
ATOM   160  C  CG   . MET   A 1 45  ? -26.887 -13.521 -20.525 1.00 24.92  ? 252 MET   A CG   1 
ATOM   161  S  SD   . MET   A 1 45  ? -26.505 -13.684 -18.770 1.00 26.43  ? 252 MET   A SD   1 
ATOM   162  C  CE   . MET   A 1 45  ? -24.760 -13.323 -18.829 1.00 28.95  ? 252 MET   A CE   1 
ATOM   163  N  N    . PRO   A 1 46  ? -28.058 -10.429 -24.189 1.00 18.58  ? 253 PRO   A N    1 
ATOM   164  C  CA   . PRO   A 1 46  ? -28.893 -9.319  -24.629 1.00 19.96  ? 253 PRO   A CA   1 
ATOM   165  C  C    . PRO   A 1 46  ? -30.326 -9.528  -24.095 1.00 21.19  ? 253 PRO   A C    1 
ATOM   166  O  O    . PRO   A 1 46  ? -30.814 -10.635 -24.031 1.00 23.64  ? 253 PRO   A O    1 
ATOM   167  C  CB   . PRO   A 1 46  ? -28.845 -9.407  -26.158 1.00 21.16  ? 253 PRO   A CB   1 
ATOM   168  C  CG   . PRO   A 1 46  ? -28.598 -10.871 -26.423 1.00 20.28  ? 253 PRO   A CG   1 
ATOM   169  C  CD   . PRO   A 1 46  ? -27.651 -11.266 -25.314 1.00 23.38  ? 253 PRO   A CD   1 
ATOM   170  N  N    . ASP   A 1 47  ? -30.948 -8.432  -23.673 1.00 23.01  ? 254 ASP   A N    1 
ATOM   171  C  CA   . ASP   A 1 47  ? -32.247 -8.414  -22.974 1.00 19.11  ? 254 ASP   A CA   1 
ATOM   172  C  C    . ASP   A 1 47  ? -33.287 -8.815  -23.999 1.00 20.81  ? 254 ASP   A C    1 
ATOM   173  O  O    . ASP   A 1 47  ? -33.562 -8.112  -24.960 1.00 21.27  ? 254 ASP   A O    1 
ATOM   174  C  CB   . ASP   A 1 47  ? -32.500 -7.049  -22.339 1.00 21.75  ? 254 ASP   A CB   1 
ATOM   175  C  CG   . ASP   A 1 47  ? -33.776 -7.018  -21.533 1.00 20.87  ? 254 ASP   A CG   1 
ATOM   176  O  OD1  . ASP   A 1 47  ? -34.648 -7.798  -21.861 1.00 25.30  ? 254 ASP   A OD1  1 
ATOM   177  O  OD2  . ASP   A 1 47  ? -33.810 -6.331  -20.523 1.00 23.91  ? 254 ASP   A OD2  1 
ATOM   178  N  N    . PRO   A 1 48  ? -33.938 -9.974  -23.809 1.00 21.33  ? 255 PRO   A N    1 
ATOM   179  C  CA   . PRO   A 1 48  ? -34.855 -10.471 -24.819 1.00 22.30  ? 255 PRO   A CA   1 
ATOM   180  C  C    . PRO   A 1 48  ? -36.139 -9.657  -24.776 1.00 21.35  ? 255 PRO   A C    1 
ATOM   181  O  O    . PRO   A 1 48  ? -36.894 -9.745  -25.717 1.00 30.08  ? 255 PRO   A O    1 
ATOM   182  C  CB   . PRO   A 1 48  ? -35.075 -11.931 -24.418 1.00 21.60  ? 255 PRO   A CB   1 
ATOM   183  C  CG   . PRO   A 1 48  ? -34.783 -11.977 -22.932 1.00 26.27  ? 255 PRO   A CG   1 
ATOM   184  C  CD   . PRO   A 1 48  ? -33.768 -10.890 -22.671 1.00 24.69  ? 255 PRO   A CD   1 
ATOM   185  N  N    . THR   A 1 49  ? -36.326 -8.840  -23.739 1.00 21.67  ? 256 THR   A N    1 
ATOM   186  C  CA   . THR   A 1 49  ? -37.575 -8.026  -23.647 1.00 22.30  ? 256 THR   A CA   1 
ATOM   187  C  C    . THR   A 1 49  ? -37.397 -6.724  -24.449 1.00 20.76  ? 256 THR   A C    1 
ATOM   188  O  O    . THR   A 1 49  ? -38.407 -6.019  -24.687 1.00 29.13  ? 256 THR   A O    1 
ATOM   189  C  CB   . THR   A 1 49  ? -37.989 -7.764  -22.191 1.00 22.99  ? 256 THR   A CB   1 
ATOM   190  O  OG1  . THR   A 1 49  ? -37.069 -6.846  -21.579 1.00 26.14  ? 256 THR   A OG1  1 
ATOM   191  C  CG2  . THR   A 1 49  ? -38.094 -9.047  -21.398 1.00 26.50  ? 256 THR   A CG2  1 
ATOM   192  N  N    . VAL   A 1 50  ? -36.162 -6.415  -24.857 1.00 24.59  ? 257 VAL   A N    1 
ATOM   193  C  CA   . VAL   A 1 50  ? -35.908 -5.090  -25.474 1.00 20.98  ? 257 VAL   A CA   1 
ATOM   194  C  C    . VAL   A 1 50  ? -35.987 -5.213  -26.987 1.00 22.19  ? 257 VAL   A C    1 
ATOM   195  O  O    . VAL   A 1 50  ? -35.430 -6.128  -27.578 1.00 22.45  ? 257 VAL   A O    1 
ATOM   196  C  CB   . VAL   A 1 50  ? -34.583 -4.508  -24.987 1.00 24.43  ? 257 VAL   A CB   1 
ATOM   197  C  CG1  . VAL   A 1 50  ? -34.231 -3.256  -25.750 1.00 22.11  ? 257 VAL   A CG1  1 
ATOM   198  C  CG2  . VAL   A 1 50  ? -34.616 -4.261  -23.484 1.00 27.22  ? 257 VAL   A CG2  1 
ATOM   199  N  N    . PRO   A 1 51  ? -36.686 -4.299  -27.700 1.00 22.09  ? 258 PRO   A N    1 
ATOM   200  C  CA   . PRO   A 1 51  ? -36.710 -4.366  -29.152 1.00 24.47  ? 258 PRO   A CA   1 
ATOM   201  C  C    . PRO   A 1 51  ? -35.297 -4.202  -29.730 1.00 23.51  ? 258 PRO   A C    1 
ATOM   202  O  O    . PRO   A 1 51  ? -34.543 -3.406  -29.195 1.00 26.57  ? 258 PRO   A O    1 
ATOM   203  C  CB   . PRO   A 1 51  ? -37.581 -3.199  -29.614 1.00 22.66  ? 258 PRO   A CB   1 
ATOM   204  C  CG   . PRO   A 1 51  ? -38.295 -2.752  -28.375 1.00 26.39  ? 258 PRO   A CG   1 
ATOM   205  C  CD   . PRO   A 1 51  ? -37.514 -3.213  -27.165 1.00 25.24  ? 258 PRO   A CD   1 
ATOM   206  N  N    . ASP   A 1 52  ? -35.014 -4.887  -30.826 1.00 19.59  ? 259 ASP   A N    1 
ATOM   207  C  CA   . ASP   A 1 52  ? -33.703 -4.797  -31.527 1.00 23.23  ? 259 ASP   A CA   1 
ATOM   208  C  C    . ASP   A 1 52  ? -33.501 -3.377  -32.073 1.00 25.92  ? 259 ASP   A C    1 
ATOM   209  O  O    . ASP   A 1 52  ? -34.435 -2.795  -32.611 1.00 31.41  ? 259 ASP   A O    1 
ATOM   210  C  CB   . ASP   A 1 52  ? -33.545 -5.867  -32.625 1.00 31.76  ? 259 ASP   A CB   1 
ATOM   211  C  CG   . ASP   A 1 52  ? -33.056 -7.235  -32.138 1.00 37.09  ? 259 ASP   A CG   1 
ATOM   212  O  OD1  . ASP   A 1 52  ? -32.602 -7.369  -30.959 1.00 32.15  ? 259 ASP   A OD1  1 
ATOM   213  O  OD2  . ASP   A 1 52  ? -33.146 -8.190  -32.933 1.00 53.20  ? 259 ASP   A OD2  1 
ATOM   214  N  N    . SER   A 1 53  ? -32.360 -2.775  -31.800 1.00 27.94  ? 260 SER   A N    1 
ATOM   215  C  CA   . SER   A 1 53  ? -32.031 -1.387  -32.198 1.00 25.97  ? 260 SER   A CA   1 
ATOM   216  C  C    . SER   A 1 53  ? -30.533 -1.195  -32.056 1.00 23.20  ? 260 SER   A C    1 
ATOM   217  O  O    . SER   A 1 53  ? -29.883 -2.017  -31.350 1.00 26.20  ? 260 SER   A O    1 
ATOM   218  C  CB   . SER   A 1 53  ? -32.760 -0.349  -31.380 1.00 29.31  ? 260 SER   A CB   1 
ATOM   219  O  OG   . SER   A 1 53  ? -32.351 -0.349  -30.005 1.00 30.99  ? 260 SER   A OG   1 
ATOM   220  N  N    . ASP   A 1 54  ? -30.056 -0.094  -32.646 1.00 23.31  ? 261 ASP   A N    1 
ATOM   221  C  CA   . ASP   A 1 54  ? -28.627 0.273   -32.567 1.00 27.67  ? 261 ASP   A CA   1 
ATOM   222  C  C    . ASP   A 1 54  ? -28.325 0.463   -31.079 1.00 26.09  ? 261 ASP   A C    1 
ATOM   223  O  O    . ASP   A 1 54  ? -27.301 -0.030  -30.637 1.00 29.09  ? 261 ASP   A O    1 
ATOM   224  C  CB   . ASP   A 1 54  ? -28.342 1.448   -33.508 1.00 34.32  ? 261 ASP   A CB   1 
ATOM   225  C  CG   . ASP   A 1 54  ? -29.098 2.741   -33.215 1.00 35.35  ? 261 ASP   A CG   1 
ATOM   226  O  OD1  . ASP   A 1 54  ? -30.201 2.688   -32.621 1.00 39.20  ? 261 ASP   A OD1  1 
ATOM   227  O  OD2  . ASP   A 1 54  ? -28.513 3.796   -33.516 1.00 46.75  ? 261 ASP   A OD2  1 
ATOM   228  N  N    . ILE   A 1 55  ? -29.240 1.071   -30.315 1.00 27.47  ? 262 ILE   A N    1 
ATOM   229  C  CA   . ILE   A 1 55  ? -29.031 1.351   -28.870 1.00 25.61  ? 262 ILE   A CA   1 
ATOM   230  C  C    . ILE   A 1 55  ? -28.953 0.024   -28.133 1.00 25.22  ? 262 ILE   A C    1 
ATOM   231  O  O    . ILE   A 1 55  ? -28.179 -0.080  -27.221 1.00 27.15  ? 262 ILE   A O    1 
ATOM   232  C  CB   . ILE   A 1 55  ? -30.098 2.305   -28.304 1.00 31.25  ? 262 ILE   A CB   1 
ATOM   233  C  CG1  . ILE   A 1 55  ? -29.994 3.702   -28.943 1.00 41.11  ? 262 ILE   A CG1  1 
ATOM   234  C  CG2  . ILE   A 1 55  ? -30.021 2.376   -26.782 1.00 33.23  ? 262 ILE   A CG2  1 
ATOM   235  C  CD1  . ILE   A 1 55  ? -31.223 4.538   -28.798 1.00 46.39  ? 262 ILE   A CD1  1 
ATOM   236  N  N    . LYS   A 1 56  ? -29.839 -0.942  -28.421 1.00 25.80  ? 263 LYS   A N    1 
ATOM   237  C  CA   . LYS   A 1 56  ? -29.733 -2.263  -27.751 1.00 25.90  ? 263 LYS   A CA   1 
ATOM   238  C  C    . LYS   A 1 56  ? -28.359 -2.926  -28.025 1.00 22.31  ? 263 LYS   A C    1 
ATOM   239  O  O    . LYS   A 1 56  ? -27.740 -3.454  -27.087 1.00 24.13  ? 263 LYS   A O    1 
ATOM   240  C  CB   . LYS   A 1 56  ? -30.882 -3.179  -28.163 1.00 25.27  ? 263 LYS   A CB   1 
ATOM   241  C  CG   . LYS   A 1 56  ? -30.802 -4.523  -27.486 1.00 24.34  ? 263 LYS   A CG   1 
ATOM   242  C  CD   . LYS   A 1 56  ? -31.873 -5.441  -27.913 1.00 21.56  ? 263 LYS   A CD   1 
ATOM   243  C  CE   . LYS   A 1 56  ? -31.784 -6.756  -27.223 1.00 24.14  ? 263 LYS   A CE   1 
ATOM   244  N  NZ   . LYS   A 1 56  ? -32.854 -7.569  -27.791 1.00 25.57  ? 263 LYS   A NZ   1 
ATOM   245  N  N    . ALA   A 1 57  ? -27.961 -2.995  -29.289 1.00 22.47  ? 264 ALA   A N    1 
ATOM   246  C  CA   . ALA   A 1 57  ? -26.698 -3.625  -29.725 1.00 24.13  ? 264 ALA   A CA   1 
ATOM   247  C  C    . ALA   A 1 57  ? -25.511 -2.978  -28.994 1.00 26.10  ? 264 ALA   A C    1 
ATOM   248  O  O    . ALA   A 1 57  ? -24.718 -3.690  -28.377 1.00 23.18  ? 264 ALA   A O    1 
ATOM   249  C  CB   . ALA   A 1 57  ? -26.561 -3.526  -31.217 1.00 25.08  ? 264 ALA   A CB   1 
ATOM   250  N  N    . LEU   A 1 58  ? -25.455 -1.650  -29.005 1.00 26.35  ? 265 LEU   A N    1 
ATOM   251  C  CA   . LEU   A 1 58  ? -24.362 -0.881  -28.377 1.00 23.75  ? 265 LEU   A CA   1 
ATOM   252  C  C    . LEU   A 1 58  ? -24.413 -1.023  -26.855 1.00 22.73  ? 265 LEU   A C    1 
ATOM   253  O  O    . LEU   A 1 58  ? -23.320 -1.262  -26.263 1.00 24.06  ? 265 LEU   A O    1 
ATOM   254  C  CB   . LEU   A 1 58  ? -24.431 0.569   -28.854 1.00 22.56  ? 265 LEU   A CB   1 
ATOM   255  C  CG   . LEU   A 1 58  ? -24.128 0.764   -30.340 1.00 25.94  ? 265 LEU   A CG   1 
ATOM   256  C  CD1  . LEU   A 1 58  ? -24.485 2.192   -30.821 1.00 29.51  ? 265 LEU   A CD1  1 
ATOM   257  C  CD2  . LEU   A 1 58  ? -22.668 0.480   -30.634 1.00 24.51  ? 265 LEU   A CD2  1 
ATOM   258  N  N    . THR   A 1 59  ? -25.604 -0.997  -26.246 1.00 21.51  ? 266 THR   A N    1 
ATOM   259  C  CA   . THR   A 1 59  ? -25.767 -1.261  -24.795 1.00 23.36  ? 266 THR   A CA   1 
ATOM   260  C  C    . THR   A 1 59  ? -25.225 -2.676  -24.498 1.00 24.54  ? 266 THR   A C    1 
ATOM   261  O  O    . THR   A 1 59  ? -24.424 -2.851  -23.508 1.00 23.79  ? 266 THR   A O    1 
ATOM   262  C  CB   . THR   A 1 59  ? -27.212 -1.029  -24.322 1.00 26.77  ? 266 THR   A CB   1 
ATOM   263  O  OG1  . THR   A 1 59  ? -27.616 0.314   -24.626 1.00 28.43  ? 266 THR   A OG1  1 
ATOM   264  C  CG2  . THR   A 1 59  ? -27.340 -1.258  -22.834 1.00 26.26  ? 266 THR   A CG2  1 
ATOM   265  N  N    . THR   A 1 60  ? -25.585 -3.670  -25.308 1.00 23.52  ? 267 THR   A N    1 
ATOM   266  C  CA   . THR   A 1 60  ? -25.141 -5.069  -25.054 1.00 20.29  ? 267 THR   A CA   1 
ATOM   267  C  C    . THR   A 1 60  ? -23.620 -5.182  -25.136 1.00 19.82  ? 267 THR   A C    1 
ATOM   268  O  O    . THR   A 1 60  ? -23.028 -5.767  -24.217 1.00 20.16  ? 267 THR   A O    1 
ATOM   269  C  CB   . THR   A 1 60  ? -25.740 -6.046  -26.046 1.00 22.78  ? 267 THR   A CB   1 
ATOM   270  O  OG1  . THR   A 1 60  ? -27.151 -5.844  -25.976 1.00 21.54  ? 267 THR   A OG1  1 
ATOM   271  C  CG2  . THR   A 1 60  ? -25.429 -7.493  -25.730 1.00 25.83  ? 267 THR   A CG2  1 
ATOM   272  N  N    . LEU   A 1 61  ? -23.041 -4.586  -26.176 1.00 19.93  ? 268 LEU   A N    1 
ATOM   273  C  CA   . LEU   A 1 61  ? -21.570 -4.591  -26.357 1.00 20.64  ? 268 LEU   A CA   1 
ATOM   274  C  C    . LEU   A 1 61  ? -20.879 -3.883  -25.196 1.00 19.39  ? 268 LEU   A C    1 
ATOM   275  O  O    . LEU   A 1 61  ? -19.851 -4.464  -24.689 1.00 19.03  ? 268 LEU   A O    1 
ATOM   276  C  CB   . LEU   A 1 61  ? -21.193 -4.047  -27.719 1.00 20.14  ? 268 LEU   A CB   1 
ATOM   277  C  CG   . LEU   A 1 61  ? -21.567 -4.931  -28.900 1.00 26.32  ? 268 LEU   A CG   1 
ATOM   278  C  CD1  . LEU   A 1 61  ? -21.292 -4.219  -30.194 1.00 27.63  ? 268 LEU   A CD1  1 
ATOM   279  C  CD2  . LEU   A 1 61  ? -20.840 -6.278  -28.898 1.00 28.10  ? 268 LEU   A CD2  1 
ATOM   280  N  N    . CYS   A 1 62  ? -21.324 -2.702  -24.789 1.00 20.53  ? 269 CYS   A N    1 
ATOM   281  C  CA   . CYS   A 1 62  ? -20.638 -1.960  -23.711 1.00 20.76  ? 269 CYS   A CA   1 
ATOM   282  C  C    . CYS   A 1 62  ? -20.752 -2.723  -22.398 1.00 21.83  ? 269 CYS   A C    1 
ATOM   283  O  O    . CYS   A 1 62  ? -19.805 -2.698  -21.615 1.00 23.45  ? 269 CYS   A O    1 
ATOM   284  C  CB   . CYS   A 1 62  ? -21.180 -0.542  -23.610 1.00 22.88  ? 269 CYS   A CB   1 
ATOM   285  S  SG   . CYS   A 1 62  ? -20.638 0.379   -25.056 1.00 29.62  ? 269 CYS   A SG   1 
ATOM   286  N  N    . ASP   A 1 63  ? -21.922 -3.326  -22.142 1.00 27.63  ? 270 ASP   A N    1 
ATOM   287  C  CA   . ASP   A 1 63  ? -22.134 -4.152  -20.916 1.00 24.84  ? 270 ASP   A CA   1 
ATOM   288  C  C    . ASP   A 1 63  ? -21.156 -5.348  -20.900 1.00 20.51  ? 270 ASP   A C    1 
ATOM   289  O  O    . ASP   A 1 63  ? -20.543 -5.645  -19.804 1.00 22.62  ? 270 ASP   A O    1 
ATOM   290  C  CB   . ASP   A 1 63  ? -23.601 -4.548  -20.847 1.00 24.44  ? 270 ASP   A CB   1 
ATOM   291  C  CG   . ASP   A 1 63  ? -23.971 -5.353  -19.619 1.00 36.31  ? 270 ASP   A CG   1 
ATOM   292  O  OD1  . ASP   A 1 63  ? -23.470 -6.480  -19.453 1.00 43.81  ? 270 ASP   A OD1  1 
ATOM   293  O  OD2  . ASP   A 1 63  ? -24.786 -4.863  -18.867 1.00 62.45  ? 270 ASP   A OD2  1 
ATOM   294  N  N    . LEU   A 1 64  ? -21.086 -6.069  -22.021 1.00 21.97  ? 271 LEU   A N    1 
ATOM   295  C  CA   . LEU   A 1 64  ? -20.143 -7.198  -22.209 1.00 21.17  ? 271 LEU   A CA   1 
ATOM   296  C  C    . LEU   A 1 64  ? -18.700 -6.725  -21.964 1.00 19.61  ? 271 LEU   A C    1 
ATOM   297  O  O    . LEU   A 1 64  ? -17.951 -7.399  -21.230 1.00 20.75  ? 271 LEU   A O    1 
ATOM   298  C  CB   . LEU   A 1 64  ? -20.292 -7.721  -23.636 1.00 21.51  ? 271 LEU   A CB   1 
ATOM   299  C  CG   . LEU   A 1 64  ? -19.337 -8.846  -23.991 1.00 21.25  ? 271 LEU   A CG   1 
ATOM   300  C  CD1  . LEU   A 1 64  ? -19.472 -9.986  -22.993 1.00 25.81  ? 271 LEU   A CD1  1 
ATOM   301  C  CD2  . LEU   A 1 64  ? -19.637 -9.315  -25.406 1.00 21.40  ? 271 LEU   A CD2  1 
ATOM   302  N  N    . ALA   A 1 65  ? -18.331 -5.587  -22.517 1.00 21.71  ? 272 ALA   A N    1 
ATOM   303  C  CA   . ALA   A 1 65  ? -16.961 -5.023  -22.341 1.00 20.03  ? 272 ALA   A CA   1 
ATOM   304  C  C    . ALA   A 1 65  ? -16.678 -4.712  -20.878 1.00 22.15  ? 272 ALA   A C    1 
ATOM   305  O  O    . ALA   A 1 65  ? -15.603 -5.084  -20.359 1.00 22.67  ? 272 ALA   A O    1 
ATOM   306  C  CB   . ALA   A 1 65  ? -16.732 -3.796  -23.212 1.00 24.77  ? 272 ALA   A CB   1 
ATOM   307  N  N    . ASP   A 1 66  ? -17.591 -4.019  -20.205 1.00 22.56  ? 273 ASP   A N    1 
ATOM   308  C  CA   . ASP   A 1 66  ? -17.489 -3.776  -18.744 1.00 25.00  ? 273 ASP   A CA   1 
ATOM   309  C  C    . ASP   A 1 66  ? -17.130 -5.076  -17.985 1.00 24.83  ? 273 ASP   A C    1 
ATOM   310  O  O    . ASP   A 1 66  ? -16.230 -5.067  -17.117 1.00 23.55  ? 273 ASP   A O    1 
ATOM   311  C  CB   . ASP   A 1 66  ? -18.778 -3.118  -18.248 1.00 26.39  ? 273 ASP   A CB   1 
ATOM   312  C  CG   . ASP   A 1 66  ? -18.592 -2.487  -16.889 1.00 32.63  ? 273 ASP   A CG   1 
ATOM   313  O  OD1  . ASP   A 1 66  ? -17.863 -1.485  -16.801 1.00 39.15  ? 273 ASP   A OD1  1 
ATOM   314  O  OD2  . ASP   A 1 66  ? -19.156 -3.026  -15.928 1.00 41.19  ? 273 ASP   A OD2  1 
ATOM   315  N  N    . ARG   A 1 67  ? -17.853 -6.163  -18.256 1.00 20.22  ? 274 ARG   A N    1 
ATOM   316  C  CA   . ARG   A 1 67  ? -17.688 -7.450  -17.519 1.00 20.52  ? 274 ARG   A CA   1 
ATOM   317  C  C    . ARG   A 1 67  ? -16.321 -8.045  -17.891 1.00 20.43  ? 274 ARG   A C    1 
ATOM   318  O  O    . ARG   A 1 67  ? -15.602 -8.520  -16.960 1.00 27.84  ? 274 ARG   A O    1 
ATOM   319  C  CB   . ARG   A 1 67  ? -18.889 -8.359  -17.787 1.00 25.19  ? 274 ARG   A CB   1 
ATOM   320  C  CG   . ARG   A 1 67  ? -20.103 -7.908  -16.992 1.00 27.19  ? 274 ARG   A CG   1 
ATOM   321  C  CD   . ARG   A 1 67  ? -21.301 -8.787  -17.157 1.00 27.28  ? 274 ARG   A CD   1 
ATOM   322  N  NE   . ARG   A 1 67  ? -21.845 -8.634  -18.489 1.00 32.99  ? 274 ARG   A NE   1 
ATOM   323  C  CZ   . ARG   A 1 67  ? -22.099 -9.649  -19.347 1.00 32.25  ? 274 ARG   A CZ   1 
ATOM   324  N  NH1  . ARG   A 1 67  ? -21.875 -10.935 -19.021 1.00 34.22  ? 274 ARG   A NH1  1 
ATOM   325  N  NH2  . ARG   A 1 67  ? -22.579 -9.340  -20.542 1.00 29.05  ? 274 ARG   A NH2  1 
ATOM   326  N  N    . GLU   A 1 68  ? -15.968 -8.053  -19.168 1.00 21.78  ? 275 GLU   A N    1 
ATOM   327  C  CA   A GLU   A 1 68  ? -14.664 -8.585  -19.660 0.50 21.26  ? 275 GLU   A CA   1 
ATOM   328  C  CA   B GLU   A 1 68  ? -14.663 -8.661  -19.556 0.50 21.08  ? 275 GLU   A CA   1 
ATOM   329  C  C    . GLU   A 1 68  ? -13.528 -7.792  -19.010 1.00 21.90  ? 275 GLU   A C    1 
ATOM   330  O  O    . GLU   A 1 68  ? -12.487 -8.412  -18.648 1.00 22.03  ? 275 GLU   A O    1 
ATOM   331  C  CB   A GLU   A 1 68  ? -14.605 -8.538  -21.186 0.50 23.21  ? 275 GLU   A CB   1 
ATOM   332  C  CB   B GLU   A 1 68  ? -14.452 -8.929  -21.043 0.50 22.71  ? 275 GLU   A CB   1 
ATOM   333  C  CG   A GLU   A 1 68  ? -15.238 -9.765  -21.802 0.50 28.74  ? 275 GLU   A CG   1 
ATOM   334  C  CG   B GLU   A 1 68  ? -13.245 -9.861  -21.267 0.50 24.14  ? 275 GLU   A CG   1 
ATOM   335  C  CD   A GLU   A 1 68  ? -15.018 -10.001 -23.274 0.50 33.00  ? 275 GLU   A CD   1 
ATOM   336  C  CD   B GLU   A 1 68  ? -12.795 -9.976  -22.700 0.50 26.86  ? 275 GLU   A CD   1 
ATOM   337  O  OE1  A GLU   A 1 68  ? -13.873 -10.342 -23.635 0.50 31.03  ? 275 GLU   A OE1  1 
ATOM   338  O  OE1  B GLU   A 1 68  ? -13.589 -9.590  -23.576 0.50 32.56  ? 275 GLU   A OE1  1 
ATOM   339  O  OE2  A GLU   A 1 68  ? -15.991 -9.862  -24.040 0.50 35.47  ? 275 GLU   A OE2  1 
ATOM   340  O  OE2  B GLU   A 1 68  ? -11.640 -10.411 -22.935 0.50 22.73  ? 275 GLU   A OE2  1 
ATOM   341  N  N    . LEU   A 1 69  ? -13.725 -6.480  -18.809 1.00 21.91  ? 276 LEU   A N    1 
ATOM   342  C  CA   . LEU   A 1 69  ? -12.596 -5.705  -18.238 1.00 21.10  ? 276 LEU   A CA   1 
ATOM   343  C  C    . LEU   A 1 69  ? -12.247 -6.178  -16.822 1.00 21.89  ? 276 LEU   A C    1 
ATOM   344  O  O    . LEU   A 1 69  ? -11.084 -6.138  -16.452 1.00 21.65  ? 276 LEU   A O    1 
ATOM   345  C  CB   . LEU   A 1 69  ? -12.940 -4.216  -18.233 1.00 23.22  ? 276 LEU   A CB   1 
ATOM   346  C  CG   . LEU   A 1 69  ? -12.828 -3.534  -19.586 1.00 24.09  ? 276 LEU   A CG   1 
ATOM   347  C  CD1  . LEU   A 1 69  ? -13.536 -2.192  -19.543 1.00 26.64  ? 276 LEU   A CD1  1 
ATOM   348  C  CD2  . LEU   A 1 69  ? -11.378 -3.335  -19.950 1.00 30.26  ? 276 LEU   A CD2  1 
ATOM   349  N  N    . VAL   A 1 70  ? -13.209 -6.590  -16.013 1.00 22.37  ? 277 VAL   A N    1 
ATOM   350  C  CA   . VAL   A 1 70  ? -12.949 -7.123  -14.650 1.00 24.07  ? 277 VAL   A CA   1 
ATOM   351  C  C    . VAL   A 1 70  ? -12.028 -8.345  -14.784 1.00 21.09  ? 277 VAL   A C    1 
ATOM   352  O  O    . VAL   A 1 70  ? -11.105 -8.466  -14.029 1.00 25.26  ? 277 VAL   A O    1 
ATOM   353  C  CB   . VAL   A 1 70  ? -14.252 -7.486  -13.933 1.00 26.73  ? 277 VAL   A CB   1 
ATOM   354  C  CG1  . VAL   A 1 70  ? -13.990 -8.220  -12.625 1.00 28.34  ? 277 VAL   A CG1  1 
ATOM   355  C  CG2  . VAL   A 1 70  ? -15.119 -6.258  -13.693 1.00 27.98  ? 277 VAL   A CG2  1 
ATOM   356  N  N    . VAL   A 1 71  ? -12.347 -9.227  -15.712 1.00 23.61  ? 278 VAL   A N    1 
ATOM   357  C  CA   . VAL   A 1 71  ? -11.632 -10.516 -15.943 1.00 25.92  ? 278 VAL   A CA   1 
ATOM   358  C  C    . VAL   A 1 71  ? -10.247 -10.199 -16.524 1.00 23.09  ? 278 VAL   A C    1 
ATOM   359  O  O    . VAL   A 1 71  ? -9.232  -10.828 -16.067 1.00 24.12  ? 278 VAL   A O    1 
ATOM   360  C  CB   . VAL   A 1 71  ? -12.598 -11.375 -16.772 1.00 34.49  ? 278 VAL   A CB   1 
ATOM   361  C  CG1  . VAL   A 1 71  ? -11.991 -12.071 -17.949 1.00 32.88  ? 278 VAL   A CG1  1 
ATOM   362  C  CG2  . VAL   A 1 71  ? -13.375 -12.294 -15.846 1.00 40.78  ? 278 VAL   A CG2  1 
ATOM   363  N  N    . ILE   A 1 72  ? -10.146 -9.195  -17.390 1.00 21.49  ? 279 ILE   A N    1 
ATOM   364  C  CA   . ILE   A 1 72  ? -8.808  -8.761  -17.932 1.00 23.47  ? 279 ILE   A CA   1 
ATOM   365  C  C    . ILE   A 1 72  ? -7.878  -8.274  -16.822 1.00 22.10  ? 279 ILE   A C    1 
ATOM   366  O  O    . ILE   A 1 72  ? -6.635  -8.634  -16.829 1.00 21.34  ? 279 ILE   A O    1 
ATOM   367  C  CB   . ILE   A 1 72  ? -8.992  -7.715  -19.022 1.00 21.95  ? 279 ILE   A CB   1 
ATOM   368  C  CG1  . ILE   A 1 72  ? -9.608  -8.369  -20.254 1.00 20.20  ? 279 ILE   A CG1  1 
ATOM   369  C  CG2  . ILE   A 1 72  ? -7.690  -7.003  -19.341 1.00 24.17  ? 279 ILE   A CG2  1 
ATOM   370  C  CD1  . ILE   A 1 72  ? -10.163 -7.390  -21.243 1.00 23.84  ? 279 ILE   A CD1  1 
ATOM   371  N  N    . ILE   A 1 73  ? -8.395  -7.494  -15.901 1.00 19.68  ? 280 ILE   A N    1 
ATOM   372  C  CA   . ILE   A 1 73  ? -7.569  -7.029  -14.764 1.00 22.00  ? 280 ILE   A CA   1 
ATOM   373  C  C    . ILE   A 1 73  ? -7.028  -8.252  -13.997 1.00 22.87  ? 280 ILE   A C    1 
ATOM   374  O  O    . ILE   A 1 73  ? -5.806  -8.296  -13.727 1.00 26.56  ? 280 ILE   A O    1 
ATOM   375  C  CB   . ILE   A 1 73  ? -8.354  -6.033  -13.899 1.00 27.15  ? 280 ILE   A CB   1 
ATOM   376  C  CG1  . ILE   A 1 73  ? -8.672  -4.765  -14.693 1.00 23.43  ? 280 ILE   A CG1  1 
ATOM   377  C  CG2  . ILE   A 1 73  ? -7.568  -5.690  -12.637 1.00 29.48  ? 280 ILE   A CG2  1 
ATOM   378  C  CD1  . ILE   A 1 73  ? -9.796  -3.976  -14.104 1.00 27.74  ? 280 ILE   A CD1  1 
ATOM   379  N  N    . GLY   A 1 74  ? -7.864  -9.232  -13.667 1.00 23.57  ? 281 GLY   A N    1 
ATOM   380  C  CA   . GLY   A 1 74  ? -7.423  -10.439 -12.926 1.00 25.59  ? 281 GLY   A CA   1 
ATOM   381  C  C    . GLY   A 1 74  ? -6.350  -11.212 -13.698 1.00 25.53  ? 281 GLY   A C    1 
ATOM   382  O  O    . GLY   A 1 74  ? -5.303  -11.643 -13.072 1.00 29.41  ? 281 GLY   A O    1 
ATOM   383  N  N    . TRP   A 1 75  ? -6.578  -11.364 -15.002 1.00 21.37  ? 282 TRP   A N    1 
ATOM   384  C  CA   . TRP   A 1 75  ? -5.668  -12.069 -15.935 1.00 21.41  ? 282 TRP   A CA   1 
ATOM   385  C  C    . TRP   A 1 75  ? -4.283  -11.397 -15.970 1.00 22.02  ? 282 TRP   A C    1 
ATOM   386  O  O    . TRP   A 1 75  ? -3.238  -12.093 -15.933 1.00 25.40  ? 282 TRP   A O    1 
ATOM   387  C  CB   . TRP   A 1 75  ? -6.326  -12.083 -17.294 1.00 23.00  ? 282 TRP   A CB   1 
ATOM   388  C  CG   . TRP   A 1 75  ? -5.416  -12.387 -18.422 1.00 19.34  ? 282 TRP   A CG   1 
ATOM   389  C  CD1  . TRP   A 1 75  ? -5.013  -13.616 -18.846 1.00 24.40  ? 282 TRP   A CD1  1 
ATOM   390  C  CD2  . TRP   A 1 75  ? -4.770  -11.444 -19.272 1.00 21.29  ? 282 TRP   A CD2  1 
ATOM   391  N  NE1  . TRP   A 1 75  ? -4.171  -13.499 -19.922 1.00 24.89  ? 282 TRP   A NE1  1 
ATOM   392  C  CE2  . TRP   A 1 75  ? -4.019  -12.181 -20.215 1.00 25.91  ? 282 TRP   A CE2  1 
ATOM   393  C  CE3  . TRP   A 1 75  ? -4.807  -10.042 -19.375 1.00 23.14  ? 282 TRP   A CE3  1 
ATOM   394  C  CZ2  . TRP   A 1 75  ? -3.278  -11.570 -21.220 1.00 29.90  ? 282 TRP   A CZ2  1 
ATOM   395  C  CZ3  . TRP   A 1 75  ? -4.008  -9.442  -20.329 1.00 23.95  ? 282 TRP   A CZ3  1 
ATOM   396  C  CH2  . TRP   A 1 75  ? -3.301  -10.197 -21.264 1.00 28.19  ? 282 TRP   A CH2  1 
ATOM   397  N  N    . ALA   A 1 76  ? -4.243  -10.078 -15.992 1.00 20.43  ? 283 ALA   A N    1 
ATOM   398  C  CA   . ALA   A 1 76  ? -2.965  -9.347  -16.087 1.00 20.79  ? 283 ALA   A CA   1 
ATOM   399  C  C    . ALA   A 1 76  ? -2.062  -9.709  -14.897 1.00 23.95  ? 283 ALA   A C    1 
ATOM   400  O  O    . ALA   A 1 76  ? -0.828  -9.779  -15.065 1.00 22.78  ? 283 ALA   A O    1 
ATOM   401  C  CB   . ALA   A 1 76  ? -3.205  -7.858  -16.197 1.00 20.45  ? 283 ALA   A CB   1 
ATOM   402  N  N    . LYS   A 1 77  ? -2.653  -9.915  -13.734 1.00 26.06  ? 284 LYS   A N    1 
ATOM   403  C  CA   . LYS   A 1 77  ? -1.938  -10.209 -12.478 1.00 24.98  ? 284 LYS   A CA   1 
ATOM   404  C  C    . LYS   A 1 77  ? -1.195  -11.545 -12.588 1.00 25.79  ? 284 LYS   A C    1 
ATOM   405  O  O    . LYS   A 1 77  ? -0.303  -11.759 -11.767 1.00 31.87  ? 284 LYS   A O    1 
ATOM   406  C  CB   . LYS   A 1 77  ? -2.954  -10.220 -11.345 1.00 27.80  ? 284 LYS   A CB   1 
ATOM   407  C  CG   . LYS   A 1 77  ? -3.504  -8.840  -11.023 1.00 30.23  ? 284 LYS   A CG   1 
ATOM   408  C  CD   . LYS   A 1 77  ? -4.692  -8.875  -10.129 1.00 35.94  ? 284 LYS   A CD   1 
ATOM   409  C  CE   . LYS   A 1 77  ? -4.933  -7.597  -9.371  1.00 42.53  ? 284 LYS   A CE   1 
ATOM   410  N  NZ   . LYS   A 1 77  ? -6.013  -7.777  -8.371  1.00 42.58  ? 284 LYS   A NZ   1 
ATOM   411  N  N    . HIS   A 1 78  ? -1.632  -12.440 -13.479 1.00 24.93  ? 285 HIS   A N    1 
ATOM   412  C  CA   . HIS   A 1 78  ? -0.983  -13.750 -13.737 1.00 27.99  ? 285 HIS   A CA   1 
ATOM   413  C  C    . HIS   A 1 78  ? 0.252   -13.587 -14.608 1.00 26.01  ? 285 HIS   A C    1 
ATOM   414  O  O    . HIS   A 1 78  ? 0.993   -14.587 -14.734 1.00 31.11  ? 285 HIS   A O    1 
ATOM   415  C  CB   . HIS   A 1 78  ? -1.948  -14.733 -14.390 1.00 28.46  ? 285 HIS   A CB   1 
ATOM   416  C  CG   . HIS   A 1 78  ? -2.938  -15.214 -13.407 1.00 37.15  ? 285 HIS   A CG   1 
ATOM   417  N  ND1  . HIS   A 1 78  ? -2.579  -16.103 -12.411 1.00 38.27  ? 285 HIS   A ND1  1 
ATOM   418  C  CD2  . HIS   A 1 78  ? -4.251  -14.897 -13.231 1.00 38.15  ? 285 HIS   A CD2  1 
ATOM   419  C  CE1  . HIS   A 1 78  ? -3.648  -16.329 -11.664 1.00 33.13  ? 285 HIS   A CE1  1 
ATOM   420  N  NE2  . HIS   A 1 78  ? -4.696  -15.611 -12.159 1.00 35.74  ? 285 HIS   A NE2  1 
ATOM   421  N  N    . ILE   A 1 79  ? 0.424   -12.431 -15.251 1.00 23.84  ? 286 ILE   A N    1 
ATOM   422  C  CA   . ILE   A 1 79  ? 1.504   -12.303 -16.264 1.00 21.78  ? 286 ILE   A CA   1 
ATOM   423  C  C    . ILE   A 1 79  ? 2.770   -12.091 -15.459 1.00 24.78  ? 286 ILE   A C    1 
ATOM   424  O  O    . ILE   A 1 79  ? 2.823   -11.186 -14.636 1.00 28.62  ? 286 ILE   A O    1 
ATOM   425  C  CB   . ILE   A 1 79  ? 1.283   -11.168 -17.273 1.00 22.21  ? 286 ILE   A CB   1 
ATOM   426  C  CG1  . ILE   A 1 79  ? 0.080   -11.427 -18.177 1.00 26.34  ? 286 ILE   A CG1  1 
ATOM   427  C  CG2  . ILE   A 1 79  ? 2.559   -10.950 -18.076 1.00 26.15  ? 286 ILE   A CG2  1 
ATOM   428  C  CD1  . ILE   A 1 79  ? -0.429  -10.202 -18.853 1.00 28.86  ? 286 ILE   A CD1  1 
ATOM   429  N  N    . PRO   A 1 80  ? 3.807   -12.945 -15.612 1.00 29.18  ? 287 PRO   A N    1 
ATOM   430  C  CA   . PRO   A 1 80  ? 5.008   -12.796 -14.800 1.00 30.47  ? 287 PRO   A CA   1 
ATOM   431  C  C    . PRO   A 1 80  ? 5.592   -11.370 -14.886 1.00 27.14  ? 287 PRO   A C    1 
ATOM   432  O  O    . PRO   A 1 80  ? 5.807   -10.852 -15.971 1.00 31.39  ? 287 PRO   A O    1 
ATOM   433  C  CB   . PRO   A 1 80  ? 5.985   -13.873 -15.310 1.00 34.75  ? 287 PRO   A CB   1 
ATOM   434  C  CG   . PRO   A 1 80  ? 5.101   -14.853 -16.049 1.00 37.13  ? 287 PRO   A CG   1 
ATOM   435  C  CD   . PRO   A 1 80  ? 3.906   -14.070 -16.547 1.00 31.04  ? 287 PRO   A CD   1 
ATOM   436  N  N    . GLY   A 1 81  ? 5.815   -10.788 -13.708 1.00 24.50  ? 288 GLY   A N    1 
ATOM   437  C  CA   . GLY   A 1 81  ? 6.389   -9.450  -13.505 1.00 27.81  ? 288 GLY   A CA   1 
ATOM   438  C  C    . GLY   A 1 81  ? 5.352   -8.349  -13.501 1.00 25.40  ? 288 GLY   A C    1 
ATOM   439  O  O    . GLY   A 1 81  ? 5.620   -7.298  -12.941 1.00 32.51  ? 288 GLY   A O    1 
ATOM   440  N  N    . PHE   A 1 82  ? 4.187   -8.567  -14.070 1.00 25.27  ? 289 PHE   A N    1 
ATOM   441  C  CA   . PHE   A 1 82  ? 3.180   -7.475  -14.170 1.00 27.05  ? 289 PHE   A CA   1 
ATOM   442  C  C    . PHE   A 1 82  ? 2.898   -6.909  -12.758 1.00 28.10  ? 289 PHE   A C    1 
ATOM   443  O  O    . PHE   A 1 82  ? 2.896   -5.656  -12.554 1.00 31.30  ? 289 PHE   A O    1 
ATOM   444  C  CB   . PHE   A 1 82  ? 1.879   -7.947  -14.820 1.00 23.42  ? 289 PHE   A CB   1 
ATOM   445  C  CG   . PHE   A 1 82  ? 0.861   -6.833  -14.939 1.00 22.94  ? 289 PHE   A CG   1 
ATOM   446  C  CD1  . PHE   A 1 82  ? 0.934   -5.907  -15.970 1.00 24.33  ? 289 PHE   A CD1  1 
ATOM   447  C  CD2  . PHE   A 1 82  ? -0.147  -6.681  -14.000 1.00 19.64  ? 289 PHE   A CD2  1 
ATOM   448  C  CE1  . PHE   A 1 82  ? 0.010   -4.887  -16.066 1.00 22.40  ? 289 PHE   A CE1  1 
ATOM   449  C  CE2  . PHE   A 1 82  ? -1.043  -5.628  -14.069 1.00 20.34  ? 289 PHE   A CE2  1 
ATOM   450  C  CZ   . PHE   A 1 82  ? -0.993  -4.762  -15.120 1.00 23.23  ? 289 PHE   A CZ   1 
ATOM   451  N  N    . SER   A 1 83  ? 2.680   -7.796  -11.783 1.00 27.60  ? 290 SER   A N    1 
ATOM   452  C  CA   . SER   A 1 83  ? 2.362   -7.456  -10.381 1.00 30.13  ? 290 SER   A CA   1 
ATOM   453  C  C    . SER   A 1 83  ? 3.456   -6.680  -9.693  1.00 30.15  ? 290 SER   A C    1 
ATOM   454  O  O    . SER   A 1 83  ? 3.124   -6.035  -8.699  1.00 36.36  ? 290 SER   A O    1 
ATOM   455  C  CB   . SER   A 1 83  ? 2.069   -8.648  -9.598  1.00 37.39  ? 290 SER   A CB   1 
ATOM   456  O  OG   . SER   A 1 83  ? 0.749   -8.930  -9.886  1.00 43.28  ? 290 SER   A OG   1 
ATOM   457  N  N    . THR   A 1 84  ? 4.677   -6.765  -10.184 1.00 31.01  ? 291 THR   A N    1 
ATOM   458  C  CA   . THR   A 1 84  ? 5.834   -6.169  -9.484  1.00 32.52  ? 291 THR   A CA   1 
ATOM   459  C  C    . THR   A 1 84  ? 6.018   -4.740  -9.948  1.00 33.62  ? 291 THR   A C    1 
ATOM   460  O  O    . THR   A 1 84  ? 6.817   -4.067  -9.311  1.00 35.69  ? 291 THR   A O    1 
ATOM   461  C  CB   . THR   A 1 84  ? 7.099   -7.005  -9.686  1.00 41.21  ? 291 THR   A CB   1 
ATOM   462  O  OG1  . THR   A 1 84  ? 7.615   -6.691  -10.984 1.00 49.82  ? 291 THR   A OG1  1 
ATOM   463  C  CG2  . THR   A 1 84  ? 6.813   -8.482  -9.533  1.00 38.35  ? 291 THR   A CG2  1 
ATOM   464  N  N    . LEU   A 1 85  ? 5.331   -4.329  -11.018 1.00 28.22  ? 292 LEU   A N    1 
ATOM   465  C  CA   . LEU   A 1 85  ? 5.256   -2.913  -11.434 1.00 27.15  ? 292 LEU   A CA   1 
ATOM   466  C  C    . LEU   A 1 85  ? 4.482   -2.147  -10.376 1.00 26.96  ? 292 LEU   A C    1 
ATOM   467  O  O    . LEU   A 1 85  ? 3.704   -2.763  -9.687  1.00 29.52  ? 292 LEU   A O    1 
ATOM   468  C  CB   . LEU   A 1 85  ? 4.525   -2.818  -12.761 1.00 23.93  ? 292 LEU   A CB   1 
ATOM   469  C  CG   . LEU   A 1 85  ? 5.240   -3.404  -13.969 1.00 25.68  ? 292 LEU   A CG   1 
ATOM   470  C  CD1  . LEU   A 1 85  ? 4.279   -3.366  -15.160 1.00 24.06  ? 292 LEU   A CD1  1 
ATOM   471  C  CD2  . LEU   A 1 85  ? 6.537   -2.641  -14.229 1.00 32.35  ? 292 LEU   A CD2  1 
ATOM   472  N  N    . SER   A 1 86  ? 4.725   -0.835  -10.274 1.00 26.63  ? 293 SER   A N    1 
ATOM   473  C  CA   . SER   A 1 86  ? 3.894   0.078   -9.457  1.00 29.57  ? 293 SER   A CA   1 
ATOM   474  C  C    . SER   A 1 86  ? 2.442   -0.048  -9.913  1.00 28.03  ? 293 SER   A C    1 
ATOM   475  O  O    . SER   A 1 86  ? 2.184   -0.361  -11.106 1.00 29.83  ? 293 SER   A O    1 
ATOM   476  C  CB   . SER   A 1 86  ? 4.334   1.499   -9.550  1.00 32.85  ? 293 SER   A CB   1 
ATOM   477  O  OG   . SER   A 1 86  ? 4.028   2.017   -10.837 1.00 34.66  ? 293 SER   A OG   1 
ATOM   478  N  N    . LEU   A 1 87  ? 1.520   0.225   -9.003  1.00 30.93  ? 294 LEU   A N    1 
ATOM   479  C  CA   . LEU   A 1 87  ? 0.075   0.304   -9.343  1.00 29.94  ? 294 LEU   A CA   1 
ATOM   480  C  C    . LEU   A 1 87  ? -0.096  1.353   -10.459 1.00 28.36  ? 294 LEU   A C    1 
ATOM   481  O  O    . LEU   A 1 87  ? -0.825  1.076   -11.404 1.00 26.48  ? 294 LEU   A O    1 
ATOM   482  C  CB   . LEU   A 1 87  ? -0.728  0.558   -8.057  1.00 33.01  ? 294 LEU   A CB   1 
ATOM   483  C  CG   . LEU   A 1 87  ? -0.850  -0.683  -7.154  1.00 29.54  ? 294 LEU   A CG   1 
ATOM   484  C  CD1  . LEU   A 1 87  ? -1.289  -0.372  -5.728  1.00 34.29  ? 294 LEU   A CD1  1 
ATOM   485  C  CD2  . LEU   A 1 87  ? -1.784  -1.738  -7.762  1.00 32.93  ? 294 LEU   A CD2  1 
ATOM   486  N  N    . ALA   A 1 88  ? 0.640   2.467   -10.441 1.00 26.63  ? 295 ALA   A N    1 
ATOM   487  C  CA   . ALA   A 1 88  ? 0.523   3.496   -11.511 1.00 29.21  ? 295 ALA   A CA   1 
ATOM   488  C  C    . ALA   A 1 88  ? 0.839   2.868   -12.872 1.00 25.81  ? 295 ALA   A C    1 
ATOM   489  O  O    . ALA   A 1 88  ? 0.122   3.119   -13.863 1.00 22.38  ? 295 ALA   A O    1 
ATOM   490  C  CB   . ALA   A 1 88  ? 1.445   4.656   -11.260 1.00 27.69  ? 295 ALA   A CB   1 
ATOM   491  N  N    . ASP   A 1 89  ? 1.901   2.068   -12.925 1.00 27.97  ? 296 ASP   A N    1 
ATOM   492  C  CA   . ASP   A 1 89  ? 2.410   1.448   -14.176 1.00 27.47  ? 296 ASP   A CA   1 
ATOM   493  C  C    . ASP   A 1 89  ? 1.433   0.333   -14.592 1.00 19.61  ? 296 ASP   A C    1 
ATOM   494  O  O    . ASP   A 1 89  ? 1.054   0.299   -15.778 1.00 21.21  ? 296 ASP   A O    1 
ATOM   495  C  CB   . ASP   A 1 89  ? 3.870   1.016   -14.004 1.00 28.46  ? 296 ASP   A CB   1 
ATOM   496  C  CG   . ASP   A 1 89  ? 4.890   2.123   -14.256 1.00 32.76  ? 296 ASP   A CG   1 
ATOM   497  O  OD1  . ASP   A 1 89  ? 4.462   3.218   -14.702 1.00 33.10  ? 296 ASP   A OD1  1 
ATOM   498  O  OD2  . ASP   A 1 89  ? 6.126   1.874   -14.061 1.00 33.06  ? 296 ASP   A OD2  1 
ATOM   499  N  N    . GLN   A 1 90  ? 0.940   -0.445  -13.639 1.00 20.42  ? 297 GLN   A N    1 
ATOM   500  C  CA   . GLN   A 1 90  ? -0.133  -1.445  -13.954 1.00 21.80  ? 297 GLN   A CA   1 
ATOM   501  C  C    . GLN   A 1 90  ? -1.368  -0.748  -14.574 1.00 21.62  ? 297 GLN   A C    1 
ATOM   502  O  O    . GLN   A 1 90  ? -1.857  -1.182  -15.609 1.00 21.29  ? 297 GLN   A O    1 
ATOM   503  C  CB   . GLN   A 1 90  ? -0.495  -2.237  -12.700 1.00 22.82  ? 297 GLN   A CB   1 
ATOM   504  C  CG   . GLN   A 1 90  ? 0.641   -3.115  -12.174 1.00 22.51  ? 297 GLN   A CG   1 
ATOM   505  C  CD   . GLN   A 1 90  ? 0.207   -3.830  -10.917 1.00 23.39  ? 297 GLN   A CD   1 
ATOM   506  O  OE1  . GLN   A 1 90  ? -0.884  -4.411  -10.884 1.00 26.85  ? 297 GLN   A OE1  1 
ATOM   507  N  NE2  . GLN   A 1 90  ? 1.047   -3.836  -9.901  1.00 27.39  ? 297 GLN   A NE2  1 
ATOM   508  N  N    . MET   A 1 91  ? -1.794  0.376   -14.006 1.00 21.40  ? 298 MET   A N    1 
ATOM   509  C  CA   . MET   A 1 91  ? -2.964  1.158   -14.499 1.00 18.68  ? 298 MET   A CA   1 
ATOM   510  C  C    . MET   A 1 91  ? -2.651  1.703   -15.898 1.00 19.49  ? 298 MET   A C    1 
ATOM   511  O  O    . MET   A 1 91  ? -3.453  1.566   -16.785 1.00 19.21  ? 298 MET   A O    1 
ATOM   512  C  CB   . MET   A 1 91  ? -3.283  2.311   -13.557 1.00 20.99  ? 298 MET   A CB   1 
ATOM   513  C  CG   . MET   A 1 91  ? -3.751  1.871   -12.189 1.00 26.31  ? 298 MET   A CG   1 
ATOM   514  S  SD   . MET   A 1 91  ? -4.229  3.246   -11.102 1.00 35.29  ? 298 MET   A SD   1 
ATOM   515  C  CE   . MET   A 1 91  ? -5.554  4.004   -12.055 1.00 36.57  ? 298 MET   A CE   1 
ATOM   516  N  N    . SER   A 1 92  ? -1.445  2.251   -16.111 1.00 21.13  ? 299 SER   A N    1 
ATOM   517  C  CA   . SER   A 1 92  ? -1.077  2.859   -17.405 1.00 19.95  ? 299 SER   A CA   1 
ATOM   518  C  C    . SER   A 1 92  ? -1.111  1.817   -18.516 1.00 18.22  ? 299 SER   A C    1 
ATOM   519  O  O    . SER   A 1 92  ? -1.608  2.139   -19.619 1.00 17.50  ? 299 SER   A O    1 
ATOM   520  C  CB   . SER   A 1 92  ? 0.266   3.496   -17.301 1.00 21.57  ? 299 SER   A CB   1 
ATOM   521  O  OG   . SER   A 1 92  ? 0.244   4.558   -16.366 1.00 24.17  ? 299 SER   A OG   1 
ATOM   522  N  N    . LEU   A 1 93  ? -0.528  0.643   -18.281 1.00 17.92  ? 300 LEU   A N    1 
ATOM   523  C  CA   . LEU   A 1 93  ? -0.504  -0.386  -19.340 1.00 18.56  ? 300 LEU   A CA   1 
ATOM   524  C  C    . LEU   A 1 93  ? -1.949  -0.817  -19.684 1.00 15.81  ? 300 LEU   A C    1 
ATOM   525  O  O    . LEU   A 1 93  ? -2.280  -0.891  -20.857 1.00 16.41  ? 300 LEU   A O    1 
ATOM   526  C  CB   . LEU   A 1 93  ? 0.282   -1.597  -18.842 1.00 19.81  ? 300 LEU   A CB   1 
ATOM   527  C  CG   . LEU   A 1 93  ? 1.786   -1.441  -18.616 1.00 22.23  ? 300 LEU   A CG   1 
ATOM   528  C  CD1  . LEU   A 1 93  ? 2.434   -2.774  -18.429 1.00 19.56  ? 300 LEU   A CD1  1 
ATOM   529  C  CD2  . LEU   A 1 93  ? 2.440   -0.718  -19.710 1.00 28.16  ? 300 LEU   A CD2  1 
ATOM   530  N  N    . LEU   A 1 94  ? -2.780  -1.029  -18.668 1.00 16.33  ? 301 LEU   A N    1 
ATOM   531  C  CA   . LEU   A 1 94  ? -4.191  -1.445  -18.898 1.00 17.46  ? 301 LEU   A CA   1 
ATOM   532  C  C    . LEU   A 1 94  ? -5.004  -0.303  -19.547 1.00 18.26  ? 301 LEU   A C    1 
ATOM   533  O  O    . LEU   A 1 94  ? -5.768  -0.572  -20.497 1.00 19.91  ? 301 LEU   A O    1 
ATOM   534  C  CB   . LEU   A 1 94  ? -4.779  -1.901  -17.578 1.00 19.84  ? 301 LEU   A CB   1 
ATOM   535  C  CG   . LEU   A 1 94  ? -4.345  -3.291  -17.147 1.00 19.00  ? 301 LEU   A CG   1 
ATOM   536  C  CD1  . LEU   A 1 94  ? -4.664  -3.493  -15.694 1.00 20.58  ? 301 LEU   A CD1  1 
ATOM   537  C  CD2  . LEU   A 1 94  ? -4.979  -4.370  -18.021 1.00 20.05  ? 301 LEU   A CD2  1 
ATOM   538  N  N    . GLN   A 1 95  ? -4.733  0.950   -19.177 1.00 19.24  ? 302 GLN   A N    1 
ATOM   539  C  CA   . GLN   A 1 95  ? -5.442  2.126   -19.757 1.00 18.76  ? 302 GLN   A CA   1 
ATOM   540  C  C    . GLN   A 1 95  ? -5.073  2.243   -21.232 1.00 18.28  ? 302 GLN   A C    1 
ATOM   541  O  O    . GLN   A 1 95  ? -5.941  2.612   -22.020 1.00 20.75  ? 302 GLN   A O    1 
ATOM   542  C  CB   . GLN   A 1 95  ? -5.178  3.394   -18.956 1.00 21.33  ? 302 GLN   A CB   1 
ATOM   543  C  CG   . GLN   A 1 95  ? -5.933  3.361   -17.639 1.00 27.64  ? 302 GLN   A CG   1 
ATOM   544  C  CD   . GLN   A 1 95  ? -5.643  4.539   -16.745 1.00 31.83  ? 302 GLN   A CD   1 
ATOM   545  O  OE1  . GLN   A 1 95  ? -4.540  5.066   -16.747 1.00 43.26  ? 302 GLN   A OE1  1 
ATOM   546  N  NE2  . GLN   A 1 95  ? -6.653  4.988   -16.006 1.00 35.08  ? 302 GLN   A NE2  1 
ATOM   547  N  N    . SER   A 1 96  ? -3.855  1.860   -21.620 1.00 17.17  ? 303 SER   A N    1 
ATOM   548  C  CA   . SER   A 1 96  ? -3.485  1.935   -23.056 1.00 18.94  ? 303 SER   A CA   1 
ATOM   549  C  C    . SER   A 1 96  ? -3.953  0.678   -23.823 1.00 14.91  ? 303 SER   A C    1 
ATOM   550  O  O    . SER   A 1 96  ? -4.246  0.802   -25.025 1.00 19.28  ? 303 SER   A O    1 
ATOM   551  C  CB   . SER   A 1 96  ? -2.015  2.191   -23.211 1.00 19.92  ? 303 SER   A CB   1 
ATOM   552  O  OG   . SER   A 1 96  ? -1.721  3.516   -22.753 1.00 23.82  ? 303 SER   A OG   1 
ATOM   553  N  N    . ALA   A 1 97  ? -3.925  -0.524  -23.212 1.00 16.63  ? 304 ALA   A N    1 
ATOM   554  C  CA   . ALA   A 1 97  ? -4.073  -1.770  -23.977 1.00 16.63  ? 304 ALA   A CA   1 
ATOM   555  C  C    . ALA   A 1 97  ? -5.467  -2.396  -23.895 1.00 14.53  ? 304 ALA   A C    1 
ATOM   556  O  O    . ALA   A 1 97  ? -5.669  -3.302  -24.713 1.00 16.53  ? 304 ALA   A O    1 
ATOM   557  C  CB   . ALA   A 1 97  ? -3.053  -2.750  -23.462 1.00 16.48  ? 304 ALA   A CB   1 
ATOM   558  N  N    . TRP   A 1 98  ? -6.345  -1.952  -22.998 1.00 15.61  ? 305 TRP   A N    1 
ATOM   559  C  CA   . TRP   A 1 98  ? -7.617  -2.671  -22.708 1.00 17.50  ? 305 TRP   A CA   1 
ATOM   560  C  C    . TRP   A 1 98  ? -8.336  -3.008  -24.000 1.00 16.66  ? 305 TRP   A C    1 
ATOM   561  O  O    . TRP   A 1 98  ? -8.870  -4.160  -24.088 1.00 17.75  ? 305 TRP   A O    1 
ATOM   562  C  CB   . TRP   A 1 98  ? -8.494  -1.919  -21.721 1.00 20.85  ? 305 TRP   A CB   1 
ATOM   563  C  CG   . TRP   A 1 98  ? -9.026  -0.619  -22.205 1.00 22.42  ? 305 TRP   A CG   1 
ATOM   564  C  CD1  . TRP   A 1 98  ? -8.353  0.565   -22.216 1.00 21.38  ? 305 TRP   A CD1  1 
ATOM   565  C  CD2  . TRP   A 1 98  ? -10.332 -0.343  -22.741 1.00 23.31  ? 305 TRP   A CD2  1 
ATOM   566  N  NE1  . TRP   A 1 98  ? -9.150  1.544   -22.737 1.00 22.45  ? 305 TRP   A NE1  1 
ATOM   567  C  CE2  . TRP   A 1 98  ? -10.385 1.036   -23.020 1.00 22.61  ? 305 TRP   A CE2  1 
ATOM   568  C  CE3  . TRP   A 1 98  ? -11.473 -1.108  -22.979 1.00 23.09  ? 305 TRP   A CE3  1 
ATOM   569  C  CZ2  . TRP   A 1 98  ? -11.528 1.666   -23.544 1.00 24.96  ? 305 TRP   A CZ2  1 
ATOM   570  C  CZ3  . TRP   A 1 98  ? -12.596 -0.504  -23.501 1.00 24.99  ? 305 TRP   A CZ3  1 
ATOM   571  C  CH2  . TRP   A 1 98  ? -12.632 0.877   -23.780 1.00 24.12  ? 305 TRP   A CH2  1 
ATOM   572  N  N    . MET   A 1 99  ? -8.512  -2.066  -24.898 1.00 15.26  ? 306 MET   A N    1 
ATOM   573  C  CA   . MET   A 1 99  ? -9.371  -2.312  -26.071 1.00 14.47  ? 306 MET   A CA   1 
ATOM   574  C  C    . MET   A 1 99  ? -8.653  -3.310  -27.009 1.00 14.25  ? 306 MET   A C    1 
ATOM   575  O  O    . MET   A 1 99  ? -9.297  -4.086  -27.676 1.00 18.32  ? 306 MET   A O    1 
ATOM   576  C  CB   . MET   A 1 99  ? -9.719  -1.008  -26.787 1.00 15.46  ? 306 MET   A CB   1 
ATOM   577  C  CG   . MET   A 1 99  ? -10.573 -1.196  -28.052 1.00 16.91  ? 306 MET   A CG   1 
ATOM   578  S  SD   . MET   A 1 99  ? -12.219 -1.892  -27.719 1.00 19.77  ? 306 MET   A SD   1 
ATOM   579  C  CE   . MET   A 1 99  ? -13.010 -0.346  -27.298 1.00 26.44  ? 306 MET   A CE   1 
ATOM   580  N  N    . GLU   A 1 100 ? -7.330  -3.257  -27.143 1.00 14.13  ? 307 GLU   A N    1 
ATOM   581  C  CA   . GLU   A 1 100 ? -6.561  -4.254  -27.935 1.00 15.26  ? 307 GLU   A CA   1 
ATOM   582  C  C    . GLU   A 1 100 ? -6.820  -5.657  -27.365 1.00 14.73  ? 307 GLU   A C    1 
ATOM   583  O  O    . GLU   A 1 100 ? -6.984  -6.592  -28.159 1.00 16.49  ? 307 GLU   A O    1 
ATOM   584  C  CB   . GLU   A 1 100 ? -5.044  -3.956  -27.952 1.00 14.35  ? 307 GLU   A CB   1 
ATOM   585  C  CG   . GLU   A 1 100 ? -4.664  -2.716  -28.731 1.00 17.06  ? 307 GLU   A CG   1 
ATOM   586  C  CD   . GLU   A 1 100 ? -3.171  -2.441  -28.909 1.00 19.60  ? 307 GLU   A CD   1 
ATOM   587  O  OE1  . GLU   A 1 100 ? -2.446  -3.384  -29.121 1.00 23.56  ? 307 GLU   A OE1  1 
ATOM   588  O  OE2  . GLU   A 1 100 ? -2.740  -1.249  -28.957 1.00 23.63  ? 307 GLU   A OE2  1 
ATOM   589  N  N    . ILE   A 1 101 ? -6.818  -5.784  -26.056 1.00 15.06  ? 308 ILE   A N    1 
ATOM   590  C  CA   . ILE   A 1 101 ? -7.080  -7.088  -25.406 1.00 15.57  ? 308 ILE   A CA   1 
ATOM   591  C  C    . ILE   A 1 101 ? -8.510  -7.535  -25.742 1.00 16.22  ? 308 ILE   A C    1 
ATOM   592  O  O    . ILE   A 1 101 ? -8.671  -8.740  -26.144 1.00 16.78  ? 308 ILE   A O    1 
ATOM   593  C  CB   . ILE   A 1 101 ? -6.795  -7.047  -23.917 1.00 15.68  ? 308 ILE   A CB   1 
ATOM   594  C  CG1  . ILE   A 1 101 ? -5.311  -6.713  -23.725 1.00 19.04  ? 308 ILE   A CG1  1 
ATOM   595  C  CG2  . ILE   A 1 101 ? -7.127  -8.413  -23.287 1.00 19.82  ? 308 ILE   A CG2  1 
ATOM   596  C  CD1  . ILE   A 1 101 ? -4.996  -6.058  -22.418 1.00 23.29  ? 308 ILE   A CD1  1 
ATOM   597  N  N    . LEU   A 1 102 ? -9.517  -6.648  -25.631 1.00 16.92  ? 309 LEU   A N    1 
ATOM   598  C  CA   . LEU   A 1 102 ? -10.932 -7.017  -25.937 1.00 16.62  ? 309 LEU   A CA   1 
ATOM   599  C  C    . LEU   A 1 102 ? -10.991 -7.481  -27.401 1.00 15.29  ? 309 LEU   A C    1 
ATOM   600  O  O    . LEU   A 1 102 ? -11.653 -8.496  -27.714 1.00 17.63  ? 309 LEU   A O    1 
ATOM   601  C  CB   . LEU   A 1 102 ? -11.833 -5.781  -25.719 1.00 18.17  ? 309 LEU   A CB   1 
ATOM   602  C  CG   . LEU   A 1 102 ? -12.121 -5.410  -24.257 1.00 19.45  ? 309 LEU   A CG   1 
ATOM   603  C  CD1  . LEU   A 1 102 ? -12.956 -4.136  -24.129 1.00 21.61  ? 309 LEU   A CD1  1 
ATOM   604  C  CD2  . LEU   A 1 102 ? -12.802 -6.525  -23.526 1.00 23.33  ? 309 LEU   A CD2  1 
ATOM   605  N  N    . ILE   A 1 103 ? -10.419 -6.688  -28.310 1.00 14.84  ? 310 ILE   A N    1 
ATOM   606  C  CA   . ILE   A 1 103 ? -10.514 -6.932  -29.755 1.00 15.91  ? 310 ILE   A CA   1 
ATOM   607  C  C    . ILE   A 1 103 ? -9.837  -8.278  -30.070 1.00 16.27  ? 310 ILE   A C    1 
ATOM   608  O  O    . ILE   A 1 103 ? -10.416 -9.048  -30.864 1.00 17.44  ? 310 ILE   A O    1 
ATOM   609  C  CB   . ILE   A 1 103 ? -10.003 -5.761  -30.589 1.00 17.16  ? 310 ILE   A CB   1 
ATOM   610  C  CG1  . ILE   A 1 103 ? -11.014 -4.599  -30.539 1.00 19.66  ? 310 ILE   A CG1  1 
ATOM   611  C  CG2  . ILE   A 1 103 ? -9.716  -6.242  -31.993 1.00 19.60  ? 310 ILE   A CG2  1 
ATOM   612  C  CD1  . ILE   A 1 103 ? -10.549 -3.342  -31.172 1.00 24.37  ? 310 ILE   A CD1  1 
ATOM   613  N  N    . LEU   A 1 104 ? -8.673  -8.552  -29.491 1.00 17.76  ? 311 LEU   A N    1 
ATOM   614  C  CA   . LEU   A 1 104 ? -7.940  -9.809  -29.813 1.00 20.43  ? 311 LEU   A CA   1 
ATOM   615  C  C    . LEU   A 1 104 ? -8.790  -11.017 -29.427 1.00 18.18  ? 311 LEU   A C    1 
ATOM   616  O  O    . LEU   A 1 104 ? -8.811  -11.946 -30.234 1.00 15.65  ? 311 LEU   A O    1 
ATOM   617  C  CB   . LEU   A 1 104 ? -6.597  -9.863  -29.102 1.00 22.91  ? 311 LEU   A CB   1 
ATOM   618  C  CG   . LEU   A 1 104 ? -5.364  -9.730  -29.964 1.00 28.60  ? 311 LEU   A CG   1 
ATOM   619  C  CD1  . LEU   A 1 104 ? -4.173  -9.961  -29.041 1.00 43.11  ? 311 LEU   A CD1  1 
ATOM   620  C  CD2  . LEU   A 1 104 ? -5.331  -10.710 -31.128 1.00 30.80  ? 311 LEU   A CD2  1 
ATOM   621  N  N    . GLY   A 1 105 ? -9.516  -10.935 -28.300 1.00 17.66  ? 312 GLY   A N    1 
ATOM   622  C  CA   . GLY   A 1 105 ? -10.548 -11.915 -27.885 1.00 17.21  ? 312 GLY   A CA   1 
ATOM   623  C  C    . GLY   A 1 105 ? -11.585 -12.124 -28.983 1.00 17.82  ? 312 GLY   A C    1 
ATOM   624  O  O    . GLY   A 1 105 ? -11.857 -13.307 -29.383 1.00 19.88  ? 312 GLY   A O    1 
ATOM   625  N  N    . VAL   A 1 106 ? -12.189 -11.037 -29.471 1.00 16.32  ? 313 VAL   A N    1 
ATOM   626  C  CA   . VAL   A 1 106 ? -13.271 -11.165 -30.497 1.00 19.23  ? 313 VAL   A CA   1 
ATOM   627  C  C    . VAL   A 1 106 ? -12.646 -11.793 -31.744 1.00 19.05  ? 313 VAL   A C    1 
ATOM   628  O  O    . VAL   A 1 106 ? -13.238 -12.740 -32.312 1.00 17.69  ? 313 VAL   A O    1 
ATOM   629  C  CB   . VAL   A 1 106 ? -13.945 -9.835  -30.851 1.00 21.55  ? 313 VAL   A CB   1 
ATOM   630  C  CG1  . VAL   A 1 106 ? -15.000 -10.019 -31.938 1.00 23.99  ? 313 VAL   A CG1  1 
ATOM   631  C  CG2  . VAL   A 1 106 ? -14.530 -9.173  -29.616 1.00 20.62  ? 313 VAL   A CG2  1 
ATOM   632  N  N    . VAL   A 1 107 ? -11.420 -11.389 -32.086 1.00 16.98  ? 314 VAL   A N    1 
ATOM   633  C  CA   . VAL   A 1 107 ? -10.775 -11.916 -33.308 1.00 17.32  ? 314 VAL   A CA   1 
ATOM   634  C  C    . VAL   A 1 107 ? -10.536 -13.451 -33.144 1.00 17.38  ? 314 VAL   A C    1 
ATOM   635  O  O    . VAL   A 1 107 ? -10.844 -14.216 -34.067 1.00 18.88  ? 314 VAL   A O    1 
ATOM   636  C  CB   . VAL   A 1 107 ? -9.487  -11.126 -33.604 1.00 19.69  ? 314 VAL   A CB   1 
ATOM   637  C  CG1  . VAL   A 1 107 ? -8.646  -11.778 -34.670 1.00 20.05  ? 314 VAL   A CG1  1 
ATOM   638  C  CG2  . VAL   A 1 107 ? -9.779  -9.665  -33.975 1.00 21.24  ? 314 VAL   A CG2  1 
ATOM   639  N  N    . TYR   A 1 108 ? -10.017 -13.894 -32.018 1.00 15.61  ? 315 TYR   A N    1 
ATOM   640  C  CA   . TYR   A 1 108 ? -9.667  -15.302 -31.806 1.00 19.14  ? 315 TYR   A CA   1 
ATOM   641  C  C    . TYR   A 1 108 ? -10.960 -16.142 -31.864 1.00 17.59  ? 315 TYR   A C    1 
ATOM   642  O  O    . TYR   A 1 108 ? -10.972 -17.198 -32.514 1.00 17.75  ? 315 TYR   A O    1 
ATOM   643  C  CB   . TYR   A 1 108 ? -8.907  -15.509 -30.500 1.00 18.34  ? 315 TYR   A CB   1 
ATOM   644  C  CG   . TYR   A 1 108 ? -8.524  -16.953 -30.375 1.00 19.01  ? 315 TYR   A CG   1 
ATOM   645  C  CD1  . TYR   A 1 108 ? -7.492  -17.476 -31.157 1.00 23.15  ? 315 TYR   A CD1  1 
ATOM   646  C  CD2  . TYR   A 1 108 ? -9.146  -17.811 -29.493 1.00 22.54  ? 315 TYR   A CD2  1 
ATOM   647  C  CE1  . TYR   A 1 108 ? -7.192  -18.830 -31.153 1.00 23.76  ? 315 TYR   A CE1  1 
ATOM   648  C  CE2  . TYR   A 1 108 ? -8.801  -19.156 -29.433 1.00 26.84  ? 315 TYR   A CE2  1 
ATOM   649  C  CZ   . TYR   A 1 108 ? -7.792  -19.674 -30.243 1.00 22.36  ? 315 TYR   A CZ   1 
ATOM   650  O  OH   . TYR   A 1 108 ? -7.500  -21.039 -30.250 1.00 28.55  ? 315 TYR   A OH   1 
ATOM   651  N  N    . ARG   A 1 109 ? -12.052 -15.643 -31.258 1.00 16.43  ? 316 ARG   A N    1 
ATOM   652  C  CA   . ARG   A 1 109 ? -13.328 -16.413 -31.181 1.00 18.04  ? 316 ARG   A CA   1 
ATOM   653  C  C    . ARG   A 1 109 ? -13.913 -16.550 -32.586 1.00 19.97  ? 316 ARG   A C    1 
ATOM   654  O  O    . ARG   A 1 109 ? -14.791 -17.447 -32.809 1.00 21.10  ? 316 ARG   A O    1 
ATOM   655  C  CB   . ARG   A 1 109 ? -14.289 -15.775 -30.181 1.00 20.72  ? 316 ARG   A CB   1 
ATOM   656  C  CG   . ARG   A 1 109 ? -13.821 -15.916 -28.737 1.00 19.56  ? 316 ARG   A CG   1 
ATOM   657  C  CD   . ARG   A 1 109 ? -14.867 -15.424 -27.762 1.00 22.25  ? 316 ARG   A CD   1 
ATOM   658  N  NE   . ARG   A 1 109 ? -15.192 -13.992 -27.842 1.00 21.27  ? 316 ARG   A NE   1 
ATOM   659  C  CZ   . ARG   A 1 109 ? -14.583 -13.014 -27.196 1.00 20.65  ? 316 ARG   A CZ   1 
ATOM   660  N  NH1  . ARG   A 1 109 ? -13.451 -13.227 -26.539 1.00 22.02  ? 316 ARG   A NH1  1 
ATOM   661  N  NH2  . ARG   A 1 109 ? -15.075 -11.783 -27.289 1.00 20.39  ? 316 ARG   A NH2  1 
ATOM   662  N  N    . SER   A 1 110 ? -13.520 -15.686 -33.507 1.00 18.49  ? 317 SER   A N    1 
ATOM   663  C  CA   . SER   A 1 110 ? -14.065 -15.564 -34.869 1.00 19.23  ? 317 SER   A CA   1 
ATOM   664  C  C    . SER   A 1 110 ? -13.322 -16.381 -35.913 1.00 17.73  ? 317 SER   A C    1 
ATOM   665  O  O    . SER   A 1 110 ? -13.810 -16.396 -37.070 1.00 20.20  ? 317 SER   A O    1 
ATOM   666  C  CB   . SER   A 1 110 ? -14.135 -14.120 -35.228 1.00 16.34  ? 317 SER   A CB   1 
ATOM   667  O  OG   . SER   A 1 110 ? -14.981 -13.491 -34.288 1.00 17.54  ? 317 SER   A OG   1 
ATOM   668  N  N    . LEU   A 1 111 ? -12.181 -17.011 -35.574 1.00 18.83  ? 318 LEU   A N    1 
ATOM   669  C  CA   . LEU   A 1 111 ? -11.317 -17.578 -36.646 1.00 21.07  ? 318 LEU   A CA   1 
ATOM   670  C  C    . LEU   A 1 111 ? -12.031 -18.693 -37.451 1.00 20.42  ? 318 LEU   A C    1 
ATOM   671  O  O    . LEU   A 1 111 ? -11.767 -18.844 -38.667 1.00 22.43  ? 318 LEU   A O    1 
ATOM   672  C  CB   . LEU   A 1 111 ? -10.057 -18.114 -35.982 1.00 20.49  ? 318 LEU   A CB   1 
ATOM   673  C  CG   . LEU   A 1 111 ? -9.128  -17.055 -35.371 1.00 26.04  ? 318 LEU   A CG   1 
ATOM   674  C  CD1  . LEU   A 1 111 ? -7.867  -17.711 -34.801 1.00 28.61  ? 318 LEU   A CD1  1 
ATOM   675  C  CD2  . LEU   A 1 111 ? -8.742  -16.015 -36.404 1.00 27.95  ? 318 LEU   A CD2  1 
ATOM   676  N  N    . SER   A 1 112 ? -12.913 -19.473 -36.845 1.00 23.09  ? 319 SER   A N    1 
ATOM   677  C  CA   A SER   A 1 112 ? -13.578 -20.599 -37.557 0.50 25.76  ? 319 SER   A CA   1 
ATOM   678  C  CA   B SER   A 1 112 ? -13.602 -20.603 -37.532 0.50 26.07  ? 319 SER   A CA   1 
ATOM   679  C  C    . SER   A 1 112 ? -14.851 -20.130 -38.273 1.00 25.48  ? 319 SER   A C    1 
ATOM   680  O  O    . SER   A 1 112 ? -15.536 -20.995 -38.862 1.00 32.04  ? 319 SER   A O    1 
ATOM   681  C  CB   A SER   A 1 112 ? -13.872 -21.713 -36.608 0.50 26.74  ? 319 SER   A CB   1 
ATOM   682  C  CB   B SER   A 1 112 ? -13.970 -21.673 -36.559 0.50 24.62  ? 319 SER   A CB   1 
ATOM   683  O  OG   A SER   A 1 112 ? -14.919 -21.339 -35.729 0.50 24.88  ? 319 SER   A OG   1 
ATOM   684  O  OG   B SER   A 1 112 ? -12.816 -22.210 -35.956 0.50 27.17  ? 319 SER   A OG   1 
ATOM   685  N  N    . PHE   A 1 113 ? -15.177 -18.844 -38.178 1.00 25.42  ? 320 PHE   A N    1 
ATOM   686  C  CA   . PHE   A 1 113 ? -16.404 -18.246 -38.781 1.00 25.45  ? 320 PHE   A CA   1 
ATOM   687  C  C    . PHE   A 1 113 ? -16.003 -17.500 -40.051 1.00 24.38  ? 320 PHE   A C    1 
ATOM   688  O  O    . PHE   A 1 113 ? -14.822 -17.267 -40.280 1.00 27.84  ? 320 PHE   A O    1 
ATOM   689  C  CB   . PHE   A 1 113 ? -17.097 -17.326 -37.774 1.00 25.62  ? 320 PHE   A CB   1 
ATOM   690  C  CG   . PHE   A 1 113 ? -17.717 -18.091 -36.638 1.00 25.19  ? 320 PHE   A CG   1 
ATOM   691  C  CD1  . PHE   A 1 113 ? -16.954 -18.649 -35.628 1.00 24.72  ? 320 PHE   A CD1  1 
ATOM   692  C  CD2  . PHE   A 1 113 ? -19.088 -18.277 -36.608 1.00 28.06  ? 320 PHE   A CD2  1 
ATOM   693  C  CE1  . PHE   A 1 113 ? -17.554 -19.372 -34.608 1.00 29.47  ? 320 PHE   A CE1  1 
ATOM   694  C  CE2  . PHE   A 1 113 ? -19.692 -19.014 -35.596 1.00 32.01  ? 320 PHE   A CE2  1 
ATOM   695  C  CZ   . PHE   A 1 113 ? -18.917 -19.603 -34.616 1.00 28.73  ? 320 PHE   A CZ   1 
ATOM   696  N  N    . GLU   A 1 114 ? -16.988 -17.152 -40.850 1.00 29.39  ? 321 GLU   A N    1 
ATOM   697  C  CA   . GLU   A 1 114 ? -16.814 -16.448 -42.137 1.00 33.10  ? 321 GLU   A CA   1 
ATOM   698  C  C    . GLU   A 1 114 ? -17.681 -15.189 -42.078 1.00 28.88  ? 321 GLU   A C    1 
ATOM   699  O  O    . GLU   A 1 114 ? -18.900 -15.291 -41.994 1.00 32.53  ? 321 GLU   A O    1 
ATOM   700  C  CB   . GLU   A 1 114 ? -17.161 -17.391 -43.287 1.00 39.42  ? 321 GLU   A CB   1 
ATOM   701  C  CG   . GLU   A 1 114 ? -16.097 -18.456 -43.515 1.00 46.40  ? 321 GLU   A CG   1 
ATOM   702  C  CD   . GLU   A 1 114 ? -16.132 -19.074 -44.901 1.00 65.17  ? 321 GLU   A CD   1 
ATOM   703  O  OE1  . GLU   A 1 114 ? -16.631 -20.204 -45.030 1.00 79.08  ? 321 GLU   A OE1  1 
ATOM   704  O  OE2  . GLU   A 1 114 ? -15.655 -18.415 -45.847 1.00 78.31  ? 321 GLU   A OE2  1 
ATOM   705  N  N    . ASP   A 1 115 ? -17.028 -14.047 -42.043 1.00 27.38  ? 322 ASP   A N    1 
ATOM   706  C  CA   . ASP   A 1 115 ? -17.638 -12.687 -42.123 1.00 27.91  ? 322 ASP   A CA   1 
ATOM   707  C  C    . ASP   A 1 115 ? -18.594 -12.482 -40.940 1.00 25.89  ? 322 ASP   A C    1 
ATOM   708  O  O    . ASP   A 1 115 ? -19.593 -11.733 -41.069 1.00 28.08  ? 322 ASP   A O    1 
ATOM   709  C  CB   . ASP   A 1 115 ? -18.315 -12.472 -43.480 1.00 36.00  ? 322 ASP   A CB   1 
ATOM   710  C  CG   . ASP   A 1 115 ? -17.425 -12.737 -44.676 1.00 38.61  ? 322 ASP   A CG   1 
ATOM   711  O  OD1  . ASP   A 1 115 ? -16.258 -12.411 -44.611 1.00 41.36  ? 322 ASP   A OD1  1 
ATOM   712  O  OD2  . ASP   A 1 115 ? -17.911 -13.309 -45.649 1.00 54.65  ? 322 ASP   A OD2  1 
ATOM   713  N  N    . GLU   A 1 116 ? -18.318 -13.133 -39.827 1.00 25.61  ? 323 GLU   A N    1 
ATOM   714  C  CA   . GLU   A 1 116 ? -19.086 -12.944 -38.580 1.00 30.15  ? 323 GLU   A CA   1 
ATOM   715  C  C    . GLU   A 1 116 ? -18.101 -12.756 -37.441 1.00 23.05  ? 323 GLU   A C    1 
ATOM   716  O  O    . GLU   A 1 116 ? -16.965 -13.334 -37.501 1.00 26.88  ? 323 GLU   A O    1 
ATOM   717  C  CB   . GLU   A 1 116 ? -20.020 -14.119 -38.278 1.00 31.68  ? 323 GLU   A CB   1 
ATOM   718  C  CG   . GLU   A 1 116 ? -21.042 -14.395 -39.362 1.00 36.31  ? 323 GLU   A CG   1 
ATOM   719  C  CD   . GLU   A 1 116 ? -21.924 -15.590 -39.080 1.00 41.54  ? 323 GLU   A CD   1 
ATOM   720  O  OE1  . GLU   A 1 116 ? -21.379 -16.650 -38.750 1.00 44.52  ? 323 GLU   A OE1  1 
ATOM   721  O  OE2  . GLU   A 1 116 ? -23.145 -15.464 -39.211 1.00 59.26  ? 323 GLU   A OE2  1 
ATOM   722  N  N    . LEU   A 1 117 ? -18.499 -11.953 -36.459 1.00 20.78  ? 324 LEU   A N    1 
ATOM   723  C  CA   . LEU   A 1 117 ? -17.661 -11.676 -35.273 1.00 18.52  ? 324 LEU   A CA   1 
ATOM   724  C  C    . LEU   A 1 117 ? -18.342 -12.198 -34.021 1.00 19.72  ? 324 LEU   A C    1 
ATOM   725  O  O    . LEU   A 1 117 ? -19.492 -11.837 -33.721 1.00 22.09  ? 324 LEU   A O    1 
ATOM   726  C  CB   . LEU   A 1 117 ? -17.458 -10.178 -35.159 1.00 19.58  ? 324 LEU   A CB   1 
ATOM   727  C  CG   . LEU   A 1 117 ? -16.616 -9.565  -36.266 1.00 22.93  ? 324 LEU   A CG   1 
ATOM   728  C  CD1  . LEU   A 1 117 ? -16.534 -8.035  -36.097 1.00 20.29  ? 324 LEU   A CD1  1 
ATOM   729  C  CD2  . LEU   A 1 117 ? -15.282 -10.249 -36.243 1.00 24.32  ? 324 LEU   A CD2  1 
ATOM   730  N  N    . VAL   A 1 118 ? -17.642 -13.090 -33.348 1.00 18.68  ? 325 VAL   A N    1 
ATOM   731  C  CA   . VAL   A 1 118 ? -18.152 -13.771 -32.148 1.00 20.15  ? 325 VAL   A CA   1 
ATOM   732  C  C    . VAL   A 1 118 ? -17.810 -12.936 -30.925 1.00 21.29  ? 325 VAL   A C    1 
ATOM   733  O  O    . VAL   A 1 118 ? -16.764 -13.197 -30.246 1.00 19.17  ? 325 VAL   A O    1 
ATOM   734  C  CB   . VAL   A 1 118 ? -17.617 -15.201 -32.078 1.00 20.36  ? 325 VAL   A CB   1 
ATOM   735  C  CG1  . VAL   A 1 118 ? -18.199 -15.960 -30.889 1.00 23.67  ? 325 VAL   A CG1  1 
ATOM   736  C  CG2  . VAL   A 1 118 ? -17.862 -15.932 -33.387 1.00 21.88  ? 325 VAL   A CG2  1 
ATOM   737  N  N    . TYR   A 1 119 ? -18.599 -11.886 -30.679 1.00 20.24  ? 326 TYR   A N    1 
ATOM   738  C  CA   . TYR   A 1 119 ? -18.452 -11.095 -29.438 1.00 19.81  ? 326 TYR   A CA   1 
ATOM   739  C  C    . TYR   A 1 119 ? -18.636 -12.012 -28.233 1.00 20.45  ? 326 TYR   A C    1 
ATOM   740  O  O    . TYR   A 1 119 ? -17.888 -11.919 -27.229 1.00 21.55  ? 326 TYR   A O    1 
ATOM   741  C  CB   . TYR   A 1 119 ? -19.355 -9.866  -29.474 1.00 20.02  ? 326 TYR   A CB   1 
ATOM   742  C  CG   . TYR   A 1 119 ? -18.814 -8.740  -30.329 1.00 19.80  ? 326 TYR   A CG   1 
ATOM   743  C  CD1  . TYR   A 1 119 ? -17.911 -7.836  -29.798 1.00 22.74  ? 326 TYR   A CD1  1 
ATOM   744  C  CD2  . TYR   A 1 119 ? -19.092 -8.622  -31.674 1.00 25.74  ? 326 TYR   A CD2  1 
ATOM   745  C  CE1  . TYR   A 1 119 ? -17.419 -6.773  -30.537 1.00 24.06  ? 326 TYR   A CE1  1 
ATOM   746  C  CE2  . TYR   A 1 119 ? -18.541 -7.599  -32.451 1.00 30.24  ? 326 TYR   A CE2  1 
ATOM   747  C  CZ   . TYR   A 1 119 ? -17.697 -6.659  -31.881 1.00 26.69  ? 326 TYR   A CZ   1 
ATOM   748  O  OH   . TYR   A 1 119 ? -17.113 -5.618  -32.581 1.00 31.17  ? 326 TYR   A OH   1 
ATOM   749  N  N    . ALA   A 1 120 ? -19.586 -12.938 -28.364 1.00 20.45  ? 327 ALA   A N    1 
ATOM   750  C  CA   . ALA   A 1 120 ? -19.869 -13.960 -27.350 1.00 25.43  ? 327 ALA   A CA   1 
ATOM   751  C  C    . ALA   A 1 120 ? -20.622 -15.091 -28.040 1.00 19.66  ? 327 ALA   A C    1 
ATOM   752  O  O    . ALA   A 1 120 ? -21.042 -14.939 -29.192 1.00 18.94  ? 327 ALA   A O    1 
ATOM   753  C  CB   . ALA   A 1 120 ? -20.640 -13.362 -26.189 1.00 19.87  ? 327 ALA   A CB   1 
ATOM   754  N  N    . ASP   A 1 121 ? -20.700 -16.237 -27.383 1.00 22.69  ? 328 ASP   A N    1 
ATOM   755  C  CA   . ASP   A 1 121 ? -21.310 -17.412 -28.026 1.00 24.31  ? 328 ASP   A CA   1 
ATOM   756  C  C    . ASP   A 1 121 ? -22.771 -17.118 -28.342 1.00 24.60  ? 328 ASP   A C    1 
ATOM   757  O  O    . ASP   A 1 121 ? -23.261 -17.652 -29.340 1.00 26.06  ? 328 ASP   A O    1 
ATOM   758  C  CB   . ASP   A 1 121 ? -21.224 -18.668 -27.161 1.00 32.39  ? 328 ASP   A CB   1 
ATOM   759  C  CG   . ASP   A 1 121 ? -19.824 -19.198 -27.021 1.00 34.73  ? 328 ASP   A CG   1 
ATOM   760  O  OD1  . ASP   A 1 121 ? -19.021 -19.010 -27.946 1.00 35.75  ? 328 ASP   A OD1  1 
ATOM   761  O  OD2  . ASP   A 1 121 ? -19.554 -19.775 -25.967 1.00 58.06  ? 328 ASP   A OD2  1 
ATOM   762  N  N    . ASP   A 1 122 ? -23.399 -16.231 -27.558 1.00 25.45  ? 329 ASP   A N    1 
ATOM   763  C  CA   . ASP   A 1 122 ? -24.801 -15.778 -27.772 1.00 25.75  ? 329 ASP   A CA   1 
ATOM   764  C  C    . ASP   A 1 122 ? -24.844 -14.388 -28.423 1.00 24.23  ? 329 ASP   A C    1 
ATOM   765  O  O    . ASP   A 1 122 ? -25.833 -13.762 -28.254 1.00 24.29  ? 329 ASP   A O    1 
ATOM   766  C  CB   . ASP   A 1 122 ? -25.541 -15.716 -26.437 1.00 23.39  ? 329 ASP   A CB   1 
ATOM   767  C  CG   . ASP   A 1 122 ? -24.990 -14.734 -25.410 1.00 22.44  ? 329 ASP   A CG   1 
ATOM   768  O  OD1  . ASP   A 1 122 ? -23.800 -14.300 -25.561 1.00 23.90  ? 329 ASP   A OD1  1 
ATOM   769  O  OD2  . ASP   A 1 122 ? -25.730 -14.478 -24.391 1.00 23.41  ? 329 ASP   A OD2  1 
ATOM   770  N  N    . TYR   A 1 123 ? -23.756 -13.896 -29.052 1.00 25.22  ? 330 TYR   A N    1 
ATOM   771  C  CA   . TYR   A 1 123 ? -23.754 -12.561 -29.699 1.00 22.30  ? 330 TYR   A CA   1 
ATOM   772  C  C    . TYR   A 1 123 ? -22.771 -12.574 -30.875 1.00 21.05  ? 330 TYR   A C    1 
ATOM   773  O  O    . TYR   A 1 123 ? -21.590 -12.150 -30.783 1.00 21.93  ? 330 TYR   A O    1 
ATOM   774  C  CB   . TYR   A 1 123 ? -23.515 -11.473 -28.650 1.00 21.66  ? 330 TYR   A CB   1 
ATOM   775  C  CG   . TYR   A 1 123 ? -24.210 -10.189 -29.016 1.00 22.88  ? 330 TYR   A CG   1 
ATOM   776  C  CD1  . TYR   A 1 123 ? -25.563 -10.060 -28.825 1.00 23.42  ? 330 TYR   A CD1  1 
ATOM   777  C  CD2  . TYR   A 1 123 ? -23.572 -9.147  -29.662 1.00 26.99  ? 330 TYR   A CD2  1 
ATOM   778  C  CE1  . TYR   A 1 123 ? -26.271 -8.947  -29.221 1.00 26.50  ? 330 TYR   A CE1  1 
ATOM   779  C  CE2  . TYR   A 1 123 ? -24.263 -7.996  -30.032 1.00 27.56  ? 330 TYR   A CE2  1 
ATOM   780  C  CZ   . TYR   A 1 123 ? -25.617 -7.896  -29.804 1.00 27.11  ? 330 TYR   A CZ   1 
ATOM   781  O  OH   . TYR   A 1 123 ? -26.333 -6.796  -30.197 1.00 24.59  ? 330 TYR   A OH   1 
ATOM   782  N  N    . ILE   A 1 124 ? -23.255 -13.120 -31.971 1.00 21.06  ? 331 ILE   A N    1 
ATOM   783  C  CA   . ILE   A 1 124 ? -22.500 -13.246 -33.240 1.00 24.98  ? 331 ILE   A CA   1 
ATOM   784  C  C    . ILE   A 1 124 ? -23.059 -12.225 -34.201 1.00 20.23  ? 331 ILE   A C    1 
ATOM   785  O  O    . ILE   A 1 124 ? -24.244 -12.318 -34.530 1.00 25.62  ? 331 ILE   A O    1 
ATOM   786  C  CB   . ILE   A 1 124 ? -22.495 -14.691 -33.771 1.00 25.68  ? 331 ILE   A CB   1 
ATOM   787  C  CG1  . ILE   A 1 124 ? -21.923 -15.621 -32.696 1.00 26.54  ? 331 ILE   A CG1  1 
ATOM   788  C  CG2  . ILE   A 1 124 ? -21.686 -14.768 -35.065 1.00 28.23  ? 331 ILE   A CG2  1 
ATOM   789  C  CD1  . ILE   A 1 124 ? -22.020 -17.083 -33.028 1.00 30.25  ? 331 ILE   A CD1  1 
ATOM   790  N  N    . MET   A 1 125 ? -22.212 -11.267 -34.570 1.00 24.74  ? 332 MET   A N    1 
ATOM   791  C  CA   . MET   A 1 125 ? -22.598 -10.152 -35.467 1.00 24.50  ? 332 MET   A CA   1 
ATOM   792  C  C    . MET   A 1 125 ? -22.164 -10.416 -36.909 1.00 22.31  ? 332 MET   A C    1 
ATOM   793  O  O    . MET   A 1 125 ? -21.020 -10.583 -37.141 1.00 27.23  ? 332 MET   A O    1 
ATOM   794  C  CB   . MET   A 1 125 ? -22.054 -8.792  -35.048 1.00 25.98  ? 332 MET   A CB   1 
ATOM   795  C  CG   . MET   A 1 125 ? -22.362 -8.408  -33.635 1.00 26.41  ? 332 MET   A CG   1 
ATOM   796  S  SD   . MET   A 1 125 ? -22.024 -6.655  -33.355 1.00 31.51  ? 332 MET   A SD   1 
ATOM   797  C  CE   . MET   A 1 125 ? -22.793 -6.018  -34.826 1.00 27.32  ? 332 MET   A CE   1 
ATOM   798  N  N    . ASP   A 1 126 ? -23.112 -10.342 -37.832 1.00 28.10  ? 333 ASP   A N    1 
ATOM   799  C  CA   . ASP   A 1 126 ? -22.903 -10.418 -39.294 1.00 32.43  ? 333 ASP   A CA   1 
ATOM   800  C  C    . ASP   A 1 126 ? -22.927 -8.974  -39.828 1.00 28.01  ? 333 ASP   A C    1 
ATOM   801  O  O    . ASP   A 1 126 ? -23.025 -8.005  -39.035 1.00 29.48  ? 333 ASP   A O    1 
ATOM   802  C  CB   . ASP   A 1 126 ? -23.924 -11.396 -39.912 1.00 35.15  ? 333 ASP   A CB   1 
ATOM   803  C  CG   . ASP   A 1 126 ? -25.343 -10.872 -40.047 1.00 44.07  ? 333 ASP   A CG   1 
ATOM   804  O  OD1  . ASP   A 1 126 ? -25.615 -9.748  -39.567 1.00 43.33  ? 333 ASP   A OD1  1 
ATOM   805  O  OD2  . ASP   A 1 126 ? -26.186 -11.612 -40.616 1.00 57.29  ? 333 ASP   A OD2  1 
ATOM   806  N  N    . GLU   A 1 127 ? -22.777 -8.823  -41.127 1.00 31.08  ? 334 GLU   A N    1 
ATOM   807  C  CA   . GLU   A 1 127 ? -22.679 -7.509  -41.799 1.00 36.11  ? 334 GLU   A CA   1 
ATOM   808  C  C    . GLU   A 1 127 ? -23.929 -6.637  -41.529 1.00 36.64  ? 334 GLU   A C    1 
ATOM   809  O  O    . GLU   A 1 127 ? -23.780 -5.434  -41.193 1.00 31.65  ? 334 GLU   A O    1 
ATOM   810  C  CB   . GLU   A 1 127 ? -22.462 -7.806  -43.275 1.00 41.92  ? 334 GLU   A CB   1 
ATOM   811  C  CG   . GLU   A 1 127 ? -22.505 -6.560  -44.134 1.00 48.10  ? 334 GLU   A CG   1 
ATOM   812  C  CD   . GLU   A 1 127 ? -21.791 -6.729  -45.456 1.00 63.49  ? 334 GLU   A CD   1 
ATOM   813  O  OE1  . GLU   A 1 127 ? -22.445 -7.178  -46.413 1.00 62.77  ? 334 GLU   A OE1  1 
ATOM   814  O  OE2  . GLU   A 1 127 ? -20.567 -6.456  -45.504 1.00 79.40  ? 334 GLU   A OE2  1 
ATOM   815  N  N    . ASP   A 1 128 ? -25.132 -7.199  -41.670 1.00 34.65  ? 335 ASP   A N    1 
ATOM   816  C  CA   . ASP   A 1 128 ? -26.387 -6.436  -41.476 1.00 35.19  ? 335 ASP   A CA   1 
ATOM   817  C  C    . ASP   A 1 128 ? -26.472 -5.920  -40.037 1.00 34.07  ? 335 ASP   A C    1 
ATOM   818  O  O    . ASP   A 1 128 ? -26.788 -4.722  -39.844 1.00 43.95  ? 335 ASP   A O    1 
ATOM   819  C  CB   . ASP   A 1 128 ? -27.614 -7.273  -41.832 1.00 36.77  ? 335 ASP   A CB   1 
ATOM   820  C  CG   . ASP   A 1 128 ? -27.673 -7.648  -43.300 1.00 46.94  ? 335 ASP   A CG   1 
ATOM   821  O  OD1  . ASP   A 1 128 ? -27.166 -6.865  -44.133 1.00 59.32  ? 335 ASP   A OD1  1 
ATOM   822  O  OD2  . ASP   A 1 128 ? -28.197 -8.721  -43.599 1.00 56.52  ? 335 ASP   A OD2  1 
ATOM   823  N  N    . GLN   A 1 129 ? -26.205 -6.772  -39.051 1.00 30.39  ? 336 GLN   A N    1 
ATOM   824  C  CA   . GLN   A 1 129 ? -26.238 -6.351  -37.635 1.00 29.82  ? 336 GLN   A CA   1 
ATOM   825  C  C    . GLN   A 1 129 ? -25.141 -5.302  -37.448 1.00 27.96  ? 336 GLN   A C    1 
ATOM   826  O  O    . GLN   A 1 129 ? -25.313 -4.351  -36.694 1.00 30.03  ? 336 GLN   A O    1 
ATOM   827  C  CB   . GLN   A 1 129 ? -25.998 -7.539  -36.712 1.00 34.11  ? 336 GLN   A CB   1 
ATOM   828  C  CG   . GLN   A 1 129 ? -27.089 -8.605  -36.741 1.00 38.28  ? 336 GLN   A CG   1 
ATOM   829  C  CD   . GLN   A 1 129 ? -26.500 -9.857  -36.132 1.00 50.20  ? 336 GLN   A CD   1 
ATOM   830  O  OE1  . GLN   A 1 129 ? -26.423 -10.896 -36.821 1.00 59.35  ? 336 GLN   A OE1  1 
ATOM   831  N  NE2  . GLN   A 1 129 ? -26.075 -9.733  -34.859 1.00 56.64  ? 336 GLN   A NE2  1 
ATOM   832  N  N    . SER   A 1 130 ? -24.045 -5.424  -38.157 1.00 25.15  ? 337 SER   A N    1 
ATOM   833  C  CA   . SER   A 1 130 ? -22.997 -4.381  -38.035 1.00 27.16  ? 337 SER   A CA   1 
ATOM   834  C  C    . SER   A 1 130 ? -23.549 -3.062  -38.589 1.00 29.31  ? 337 SER   A C    1 
ATOM   835  O  O    . SER   A 1 130 ? -23.386 -2.039  -37.897 1.00 31.22  ? 337 SER   A O    1 
ATOM   836  C  CB   . SER   A 1 130 ? -21.641 -4.782  -38.651 1.00 25.55  ? 337 SER   A CB   1 
ATOM   837  O  OG   . SER   A 1 130 ? -21.163 -6.009  -38.084 1.00 30.33  ? 337 SER   A OG   1 
ATOM   838  N  N    . LYS   A 1 131 ? -24.218 -3.081  -39.745 1.00 31.99  ? 338 LYS   A N    1 
ATOM   839  C  CA   . LYS   A 1 131 ? -24.825 -1.848  -40.320 1.00 34.13  ? 338 LYS   A CA   1 
ATOM   840  C  C    . LYS   A 1 131 ? -25.847 -1.290  -39.330 1.00 35.29  ? 338 LYS   A C    1 
ATOM   841  O  O    . LYS   A 1 131 ? -25.885 -0.075  -39.115 1.00 35.48  ? 338 LYS   A O    1 
ATOM   842  C  CB   . LYS   A 1 131 ? -25.639 -2.081  -41.589 1.00 45.23  ? 338 LYS   A CB   1 
ATOM   843  C  CG   . LYS   A 1 131 ? -24.839 -2.215  -42.865 1.00 55.97  ? 338 LYS   A CG   1 
ATOM   844  C  CD   . LYS   A 1 131 ? -25.638 -1.884  -44.104 1.00 69.14  ? 338 LYS   A CD   1 
ATOM   845  C  CE   . LYS   A 1 131 ? -24.782 -1.858  -45.355 1.00 83.99  ? 338 LYS   A CE   1 
ATOM   846  N  NZ   . LYS   A 1 131 ? -24.292 -3.215  -45.699 1.00 76.62  ? 338 LYS   A NZ   1 
ATOM   847  N  N    . LEU   A 1 132 ? -26.695 -2.146  -38.771 1.00 35.58  ? 339 LEU   A N    1 
ATOM   848  C  CA   . LEU   A 1 132 ? -27.820 -1.667  -37.936 1.00 40.09  ? 339 LEU   A CA   1 
ATOM   849  C  C    . LEU   A 1 132 ? -27.251 -1.007  -36.680 1.00 36.86  ? 339 LEU   A C    1 
ATOM   850  O  O    . LEU   A 1 132 ? -27.830 -0.008  -36.265 1.00 46.27  ? 339 LEU   A O    1 
ATOM   851  C  CB   . LEU   A 1 132 ? -28.778 -2.821  -37.637 1.00 45.47  ? 339 LEU   A CB   1 
ATOM   852  C  CG   . LEU   A 1 132 ? -29.623 -3.264  -38.838 1.00 56.85  ? 339 LEU   A CG   1 
ATOM   853  C  CD1  . LEU   A 1 132 ? -30.344 -4.590  -38.571 1.00 61.31  ? 339 LEU   A CD1  1 
ATOM   854  C  CD2  . LEU   A 1 132 ? -30.622 -2.179  -39.226 1.00 62.81  ? 339 LEU   A CD2  1 
ATOM   855  N  N    . ALA   A 1 133 ? -26.077 -1.436  -36.197 1.00 30.21  ? 340 ALA   A N    1 
ATOM   856  C  CA   . ALA   A 1 133 ? -25.444 -0.935  -34.955 1.00 33.09  ? 340 ALA   A CA   1 
ATOM   857  C  C    . ALA   A 1 133 ? -24.531 0.284   -35.229 1.00 30.83  ? 340 ALA   A C    1 
ATOM   858  O  O    . ALA   A 1 133 ? -24.045 0.885   -34.230 1.00 31.49  ? 340 ALA   A O    1 
ATOM   859  C  CB   . ALA   A 1 133 ? -24.682 -2.056  -34.298 1.00 29.76  ? 340 ALA   A CB   1 
ATOM   860  N  N    . GLY   A 1 134 ? -24.337 0.681   -36.495 1.00 32.83  ? 341 GLY   A N    1 
ATOM   861  C  CA   . GLY   A 1 134 ? -23.385 1.757   -36.891 1.00 32.70  ? 341 GLY   A CA   1 
ATOM   862  C  C    . GLY   A 1 134 ? -21.936 1.308   -36.779 1.00 29.74  ? 341 GLY   A C    1 
ATOM   863  O  O    . GLY   A 1 134 ? -21.047 2.183   -36.627 1.00 29.75  ? 341 GLY   A O    1 
ATOM   864  N  N    . LEU   A 1 135 ? -21.698 -0.017  -36.842 1.00 28.34  ? 342 LEU   A N    1 
ATOM   865  C  CA   . LEU   A 1 135 ? -20.362 -0.620  -36.603 1.00 24.74  ? 342 LEU   A CA   1 
ATOM   866  C  C    . LEU   A 1 135 ? -19.783 -1.250  -37.876 1.00 28.54  ? 342 LEU   A C    1 
ATOM   867  O  O    . LEU   A 1 135 ? -18.810 -2.047  -37.763 1.00 27.55  ? 342 LEU   A O    1 
ATOM   868  C  CB   . LEU   A 1 135 ? -20.451 -1.671  -35.498 1.00 29.70  ? 342 LEU   A CB   1 
ATOM   869  C  CG   . LEU   A 1 135 ? -20.803 -1.161  -34.100 1.00 28.09  ? 342 LEU   A CG   1 
ATOM   870  C  CD1  . LEU   A 1 135 ? -20.905 -2.325  -33.131 1.00 33.73  ? 342 LEU   A CD1  1 
ATOM   871  C  CD2  . LEU   A 1 135 ? -19.821 -0.130  -33.585 1.00 30.30  ? 342 LEU   A CD2  1 
ATOM   872  N  N    . LEU   A 1 136 ? -20.298 -0.917  -39.050 1.00 25.67  ? 343 LEU   A N    1 
ATOM   873  C  CA   . LEU   A 1 136 ? -19.792 -1.560  -40.285 1.00 32.38  ? 343 LEU   A CA   1 
ATOM   874  C  C    . LEU   A 1 136 ? -18.292 -1.239  -40.462 1.00 27.95  ? 343 LEU   A C    1 
ATOM   875  O  O    . LEU   A 1 136 ? -17.539 -2.180  -40.779 1.00 31.61  ? 343 LEU   A O    1 
ATOM   876  C  CB   . LEU   A 1 136 ? -20.617 -1.135  -41.500 1.00 37.49  ? 343 LEU   A CB   1 
ATOM   877  C  CG   . LEU   A 1 136 ? -20.239 -1.870  -42.787 1.00 45.98  ? 343 LEU   A CG   1 
ATOM   878  C  CD1  . LEU   A 1 136 ? -20.354 -3.385  -42.633 1.00 47.75  ? 343 LEU   A CD1  1 
ATOM   879  C  CD2  . LEU   A 1 136 ? -21.099 -1.397  -43.949 1.00 56.83  ? 343 LEU   A CD2  1 
ATOM   880  N  N    . ASP   A 1 137 ? -17.838 0.014   -40.283 1.00 28.48  ? 344 ASP   A N    1 
ATOM   881  C  CA   . ASP   A 1 137 ? -16.395 0.328   -40.542 1.00 30.79  ? 344 ASP   A CA   1 
ATOM   882  C  C    . ASP   A 1 137 ? -15.499 -0.364  -39.496 1.00 26.34  ? 344 ASP   A C    1 
ATOM   883  O  O    . ASP   A 1 137 ? -14.432 -0.937  -39.877 1.00 28.64  ? 344 ASP   A O    1 
ATOM   884  C  CB   . ASP   A 1 137 ? -16.176 1.832   -40.619 1.00 34.71  ? 344 ASP   A CB   1 
ATOM   885  C  CG   . ASP   A 1 137 ? -16.821 2.445   -41.852 1.00 44.09  ? 344 ASP   A CG   1 
ATOM   886  O  OD1  . ASP   A 1 137 ? -17.212 1.676   -42.770 1.00 47.43  ? 344 ASP   A OD1  1 
ATOM   887  O  OD2  . ASP   A 1 137 ? -16.932 3.682   -41.891 1.00 55.15  ? 344 ASP   A OD2  1 
ATOM   888  N  N    . LEU   A 1 138 ? -15.893 -0.311  -38.225 1.00 26.86  ? 345 LEU   A N    1 
ATOM   889  C  CA   . LEU   A 1 138 ? -15.115 -0.923  -37.114 1.00 22.60  ? 345 LEU   A CA   1 
ATOM   890  C  C    . LEU   A 1 138 ? -15.112 -2.450  -37.263 1.00 22.18  ? 345 LEU   A C    1 
ATOM   891  O  O    . LEU   A 1 138 ? -14.028 -3.045  -37.229 1.00 24.69  ? 345 LEU   A O    1 
ATOM   892  C  CB   . LEU   A 1 138 ? -15.676 -0.516  -35.760 1.00 28.47  ? 345 LEU   A CB   1 
ATOM   893  C  CG   . LEU   A 1 138 ? -15.053 -1.274  -34.600 1.00 26.90  ? 345 LEU   A CG   1 
ATOM   894  C  CD1  . LEU   A 1 138 ? -13.548 -1.025  -34.532 1.00 33.57  ? 345 LEU   A CD1  1 
ATOM   895  C  CD2  . LEU   A 1 138 ? -15.740 -0.872  -33.311 1.00 33.49  ? 345 LEU   A CD2  1 
ATOM   896  N  N    . ASN   A 1 139 ? -16.252 -3.060  -37.538 1.00 23.17  ? 346 ASN   A N    1 
ATOM   897  C  CA   . ASN   A 1 139 ? -16.322 -4.540  -37.635 1.00 24.40  ? 346 ASN   A CA   1 
ATOM   898  C  C    . ASN   A 1 139 ? -15.586 -5.003  -38.888 1.00 19.66  ? 346 ASN   A C    1 
ATOM   899  O  O    . ASN   A 1 139 ? -14.952 -6.092  -38.783 1.00 23.45  ? 346 ASN   A O    1 
ATOM   900  C  CB   . ASN   A 1 139 ? -17.749 -5.094  -37.493 1.00 25.40  ? 346 ASN   A CB   1 
ATOM   901  C  CG   . ASN   A 1 139 ? -18.220 -5.151  -36.050 1.00 22.50  ? 346 ASN   A CG   1 
ATOM   902  O  OD1  . ASN   A 1 139 ? -17.442 -4.887  -35.116 1.00 28.42  ? 346 ASN   A OD1  1 
ATOM   903  N  ND2  . ASN   A 1 139 ? -19.502 -5.462  -35.853 1.00 27.24  ? 346 ASN   A ND2  1 
ATOM   904  N  N    . ASN   A 1 140 ? -15.602 -4.252  -39.982 1.00 19.92  ? 347 ASN   A N    1 
ATOM   905  C  CA   . ASN   A 1 140 ? -14.816 -4.567  -41.205 1.00 21.25  ? 347 ASN   A CA   1 
ATOM   906  C  C    . ASN   A 1 140 ? -13.311 -4.603  -40.855 1.00 21.17  ? 347 ASN   A C    1 
ATOM   907  O  O    . ASN   A 1 140 ? -12.583 -5.512  -41.352 1.00 23.64  ? 347 ASN   A O    1 
ATOM   908  C  CB   . ASN   A 1 140 ? -15.142 -3.616  -42.363 1.00 29.49  ? 347 ASN   A CB   1 
ATOM   909  C  CG   . ASN   A 1 140 ? -16.337 -4.077  -43.171 1.00 34.98  ? 347 ASN   A CG   1 
ATOM   910  O  OD1  . ASN   A 1 140 ? -16.791 -5.217  -43.024 1.00 48.13  ? 347 ASN   A OD1  1 
ATOM   911  N  ND2  . ASN   A 1 140 ? -16.867 -3.215  -44.027 1.00 36.61  ? 347 ASN   A ND2  1 
ATOM   912  N  N    . ALA   A 1 141 ? -12.846 -3.699  -40.008 1.00 21.54  ? 348 ALA   A N    1 
ATOM   913  C  CA   . ALA   A 1 141 ? -11.412 -3.655  -39.634 1.00 26.47  ? 348 ALA   A CA   1 
ATOM   914  C  C    . ALA   A 1 141 ? -11.089 -4.866  -38.756 1.00 20.83  ? 348 ALA   A C    1 
ATOM   915  O  O    . ALA   A 1 141 ? -9.997  -5.437  -38.875 1.00 21.75  ? 348 ALA   A O    1 
ATOM   916  C  CB   . ALA   A 1 141 ? -11.067 -2.335  -38.984 1.00 24.57  ? 348 ALA   A CB   1 
ATOM   917  N  N    . ILE   A 1 142 ? -11.985 -5.234  -37.857 1.00 20.59  ? 349 ILE   A N    1 
ATOM   918  C  CA   . ILE   A 1 142 ? -11.772 -6.431  -37.003 1.00 18.12  ? 349 ILE   A CA   1 
ATOM   919  C  C    . ILE   A 1 142 ? -11.738 -7.678  -37.906 1.00 19.84  ? 349 ILE   A C    1 
ATOM   920  O  O    . ILE   A 1 142 ? -10.878 -8.568  -37.672 1.00 20.26  ? 349 ILE   A O    1 
ATOM   921  C  CB   . ILE   A 1 142 ? -12.844 -6.477  -35.917 1.00 20.19  ? 349 ILE   A CB   1 
ATOM   922  C  CG1  . ILE   A 1 142 ? -12.738 -5.284  -34.967 1.00 22.64  ? 349 ILE   A CG1  1 
ATOM   923  C  CG2  . ILE   A 1 142 ? -12.750 -7.768  -35.150 1.00 22.71  ? 349 ILE   A CG2  1 
ATOM   924  C  CD1  . ILE   A 1 142 ? -13.878 -5.231  -33.938 1.00 25.64  ? 349 ILE   A CD1  1 
ATOM   925  N  N    . LEU   A 1 143 ? -12.580 -7.748  -38.913 1.00 19.92  ? 350 LEU   A N    1 
ATOM   926  C  CA   . LEU   A 1 143 ? -12.592 -8.880  -39.874 1.00 19.01  ? 350 LEU   A CA   1 
ATOM   927  C  C    . LEU   A 1 143 ? -11.284 -8.916  -40.666 1.00 19.03  ? 350 LEU   A C    1 
ATOM   928  O  O    . LEU   A 1 143 ? -10.877 -9.967  -41.035 1.00 20.32  ? 350 LEU   A O    1 
ATOM   929  C  CB   . LEU   A 1 143 ? -13.847 -8.786  -40.762 1.00 20.09  ? 350 LEU   A CB   1 
ATOM   930  C  CG   . LEU   A 1 143 ? -15.096 -9.270  -40.054 1.00 21.92  ? 350 LEU   A CG   1 
ATOM   931  C  CD1  . LEU   A 1 143 ? -16.332 -8.814  -40.833 1.00 25.79  ? 350 LEU   A CD1  1 
ATOM   932  C  CD2  . LEU   A 1 143 ? -15.085 -10.792 -39.871 1.00 21.92  ? 350 LEU   A CD2  1 
ATOM   933  N  N    . GLN   A 1 144 ? -10.629 -7.780  -40.854 1.00 17.62  ? 351 GLN   A N    1 
ATOM   934  C  CA   . GLN   A 1 144 ? -9.307  -7.724  -41.536 1.00 20.50  ? 351 GLN   A CA   1 
ATOM   935  C  C    . GLN   A 1 144 ? -8.271  -8.385  -40.616 1.00 20.15  ? 351 GLN   A C    1 
ATOM   936  O  O    . GLN   A 1 144 ? -7.434  -9.174  -41.125 1.00 21.54  ? 351 GLN   A O    1 
ATOM   937  C  CB   . GLN   A 1 144 ? -9.047  -6.268  -41.881 1.00 22.63  ? 351 GLN   A CB   1 
ATOM   938  C  CG   . GLN   A 1 144 ? -7.893  -6.034  -42.789 1.00 25.47  ? 351 GLN   A CG   1 
ATOM   939  C  CD   . GLN   A 1 144 ? -7.681  -4.549  -43.095 1.00 32.86  ? 351 GLN   A CD   1 
ATOM   940  O  OE1  . GLN   A 1 144 ? -8.406  -3.613  -42.656 1.00 37.12  ? 351 GLN   A OE1  1 
ATOM   941  N  NE2  . GLN   A 1 144 ? -6.681  -4.314  -43.926 1.00 29.34  ? 351 GLN   A NE2  1 
ATOM   942  N  N    . LEU   A 1 145 ? -8.375  -8.190  -39.310 1.00 17.84  ? 352 LEU   A N    1 
ATOM   943  C  CA   . LEU   A 1 145 ? -7.482  -8.881  -38.363 1.00 17.08  ? 352 LEU   A CA   1 
ATOM   944  C  C    . LEU   A 1 145 ? -7.793  -10.366 -38.445 1.00 17.80  ? 352 LEU   A C    1 
ATOM   945  O  O    . LEU   A 1 145 ? -6.854  -11.153 -38.454 1.00 19.58  ? 352 LEU   A O    1 
ATOM   946  C  CB   . LEU   A 1 145 ? -7.681  -8.411  -36.925 1.00 20.86  ? 352 LEU   A CB   1 
ATOM   947  C  CG   . LEU   A 1 145 ? -7.086  -7.073  -36.564 1.00 22.19  ? 352 LEU   A CG   1 
ATOM   948  C  CD1  . LEU   A 1 145 ? -7.727  -6.535  -35.313 1.00 25.36  ? 352 LEU   A CD1  1 
ATOM   949  C  CD2  . LEU   A 1 145 ? -5.604  -7.303  -36.334 1.00 28.24  ? 352 LEU   A CD2  1 
ATOM   950  N  N    . VAL   A 1 146 ? -9.071  -10.720 -38.523 1.00 16.95  ? 353 VAL   A N    1 
ATOM   951  C  CA   . VAL   A 1 146 ? -9.457  -12.145 -38.551 1.00 16.54  ? 353 VAL   A CA   1 
ATOM   952  C  C    . VAL   A 1 146 ? -8.831  -12.784 -39.793 1.00 16.67  ? 353 VAL   A C    1 
ATOM   953  O  O    . VAL   A 1 146 ? -8.300  -13.953 -39.691 1.00 20.81  ? 353 VAL   A O    1 
ATOM   954  C  CB   . VAL   A 1 146 ? -10.977 -12.324 -38.450 1.00 18.12  ? 353 VAL   A CB   1 
ATOM   955  C  CG1  . VAL   A 1 146 ? -11.421 -13.733 -38.731 1.00 21.27  ? 353 VAL   A CG1  1 
ATOM   956  C  CG2  . VAL   A 1 146 ? -11.495 -11.901 -37.086 1.00 20.94  ? 353 VAL   A CG2  1 
ATOM   957  N  N    . LYS   A 1 147 ? -8.975  -12.141 -40.938 1.00 19.87  ? 354 LYS   A N    1 
ATOM   958  C  CA   . LYS   A 1 147 ? -8.543  -12.714 -42.241 1.00 19.04  ? 354 LYS   A CA   1 
ATOM   959  C  C    . LYS   A 1 147 ? -7.040  -13.011 -42.123 1.00 22.27  ? 354 LYS   A C    1 
ATOM   960  O  O    . LYS   A 1 147 ? -6.595  -14.078 -42.602 1.00 20.19  ? 354 LYS   A O    1 
ATOM   961  C  CB   . LYS   A 1 147 ? -8.864  -11.761 -43.392 1.00 25.30  ? 354 LYS   A CB   1 
ATOM   962  C  CG   . LYS   A 1 147 ? -8.389  -12.152 -44.794 1.00 31.48  ? 354 LYS   A CG   1 
ATOM   963  C  CD   . LYS   A 1 147 ? -8.619  -11.054 -45.834 1.00 48.18  ? 354 LYS   A CD   1 
ATOM   964  C  CE   . LYS   A 1 147 ? -9.617  -11.452 -46.910 1.00 63.82  ? 354 LYS   A CE   1 
ATOM   965  N  NZ   . LYS   A 1 147 ? -9.065  -12.509 -47.794 1.00 76.09  ? 354 LYS   A NZ   1 
ATOM   966  N  N    . LYS   A 1 148 ? -6.268  -12.073 -41.591 1.00 20.54  ? 355 LYS   A N    1 
ATOM   967  C  CA   . LYS   A 1 148 ? -4.812  -12.283 -41.534 1.00 17.41  ? 355 LYS   A CA   1 
ATOM   968  C  C    . LYS   A 1 148 ? -4.523  -13.459 -40.605 1.00 18.17  ? 355 LYS   A C    1 
ATOM   969  O  O    . LYS   A 1 148 ? -3.664  -14.279 -40.956 1.00 19.87  ? 355 LYS   A O    1 
ATOM   970  C  CB   . LYS   A 1 148 ? -4.133  -11.001 -41.098 1.00 17.94  ? 355 LYS   A CB   1 
ATOM   971  C  CG   . LYS   A 1 148 ? -2.644  -11.035 -41.390 1.00 20.59  ? 355 LYS   A CG   1 
ATOM   972  C  CD   . LYS   A 1 148 ? -1.929  -9.932  -40.741 1.00 24.54  ? 355 LYS   A CD   1 
ATOM   973  C  CE   . LYS   A 1 148 ? -2.306  -8.547  -41.274 1.00 22.93  ? 355 LYS   A CE   1 
ATOM   974  N  NZ   . LYS   A 1 148 ? -1.541  -7.435  -40.596 1.00 21.60  ? 355 LYS   A NZ   1 
ATOM   975  N  N    . TYR   A 1 149 ? -5.172  -13.533 -39.448 1.00 18.76  ? 356 TYR   A N    1 
ATOM   976  C  CA   . TYR   A 1 149 ? -4.850  -14.598 -38.478 1.00 18.11  ? 356 TYR   A CA   1 
ATOM   977  C  C    . TYR   A 1 149 ? -5.358  -15.921 -39.035 1.00 17.05  ? 356 TYR   A C    1 
ATOM   978  O  O    . TYR   A 1 149 ? -4.689  -16.931 -38.776 1.00 19.96  ? 356 TYR   A O    1 
ATOM   979  C  CB   . TYR   A 1 149 ? -5.367  -14.299 -37.085 1.00 16.06  ? 356 TYR   A CB   1 
ATOM   980  C  CG   . TYR   A 1 149 ? -4.616  -13.239 -36.325 1.00 15.36  ? 356 TYR   A CG   1 
ATOM   981  C  CD1  . TYR   A 1 149 ? -3.226  -13.248 -36.206 1.00 17.82  ? 356 TYR   A CD1  1 
ATOM   982  C  CD2  . TYR   A 1 149 ? -5.292  -12.296 -35.581 1.00 14.86  ? 356 TYR   A CD2  1 
ATOM   983  C  CE1  . TYR   A 1 149 ? -2.541  -12.329 -35.431 1.00 16.90  ? 356 TYR   A CE1  1 
ATOM   984  C  CE2  . TYR   A 1 149 ? -4.623  -11.352 -34.797 1.00 15.88  ? 356 TYR   A CE2  1 
ATOM   985  C  CZ   . TYR   A 1 149 ? -3.238  -11.357 -34.722 1.00 15.58  ? 356 TYR   A CZ   1 
ATOM   986  O  OH   . TYR   A 1 149 ? -2.609  -10.431 -33.937 1.00 17.80  ? 356 TYR   A OH   1 
ATOM   987  N  N    . LYS   A 1 150 ? -6.431  -15.942 -39.834 1.00 20.02  ? 357 LYS   A N    1 
ATOM   988  C  CA   . LYS   A 1 150 ? -6.837  -17.233 -40.445 1.00 22.27  ? 357 LYS   A CA   1 
ATOM   989  C  C    . LYS   A 1 150 ? -5.756  -17.724 -41.418 1.00 21.07  ? 357 LYS   A C    1 
ATOM   990  O  O    . LYS   A 1 150 ? -5.394  -18.929 -41.337 1.00 24.52  ? 357 LYS   A O    1 
ATOM   991  C  CB   . LYS   A 1 150 ? -8.200  -17.158 -41.138 1.00 25.05  ? 357 LYS   A CB   1 
ATOM   992  C  CG   . LYS   A 1 150 ? -9.359  -16.755 -40.216 1.00 27.72  ? 357 LYS   A CG   1 
ATOM   993  C  CD   . LYS   A 1 150 ? -10.697 -16.560 -40.916 1.00 35.63  ? 357 LYS   A CD   1 
ATOM   994  C  CE   . LYS   A 1 150 ? -11.182 -17.795 -41.626 1.00 39.40  ? 357 LYS   A CE   1 
ATOM   995  N  NZ   . LYS   A 1 150 ? -12.666 -17.877 -41.638 1.00 53.44  ? 357 LYS   A NZ   1 
ATOM   996  N  N    . SER   A 1 151 ? -5.226  -16.871 -42.283 1.00 24.85  ? 358 SER   A N    1 
ATOM   997  C  CA   . SER   A 1 151 ? -4.173  -17.239 -43.274 1.00 24.53  ? 358 SER   A CA   1 
ATOM   998  C  C    . SER   A 1 151 ? -2.893  -17.683 -42.554 1.00 21.55  ? 358 SER   A C    1 
ATOM   999  O  O    . SER   A 1 151 ? -2.223  -18.561 -43.090 1.00 26.46  ? 358 SER   A O    1 
ATOM   1000 C  CB   . SER   A 1 151 ? -3.832  -16.131 -44.220 1.00 27.87  ? 358 SER   A CB   1 
ATOM   1001 O  OG   . SER   A 1 151 ? -3.310  -15.050 -43.492 1.00 40.12  ? 358 SER   A OG   1 
ATOM   1002 N  N    . MET   A 1 152 ? -2.580  -17.129 -41.395 1.00 20.73  ? 359 MET   A N    1 
ATOM   1003 C  CA   . MET   A 1 152 ? -1.393  -17.539 -40.603 1.00 21.79  ? 359 MET   A CA   1 
ATOM   1004 C  C    . MET   A 1 152 ? -1.658  -18.790 -39.761 1.00 17.96  ? 359 MET   A C    1 
ATOM   1005 O  O    . MET   A 1 152 ? -0.729  -19.254 -39.108 1.00 25.23  ? 359 MET   A O    1 
ATOM   1006 C  CB   . MET   A 1 152 ? -0.955  -16.419 -39.668 1.00 25.01  ? 359 MET   A CB   1 
ATOM   1007 C  CG   . MET   A 1 152 ? -0.650  -15.168 -40.444 1.00 29.48  ? 359 MET   A CG   1 
ATOM   1008 S  SD   . MET   A 1 152 ? -0.294  -13.816 -39.365 1.00 29.24  ? 359 MET   A SD   1 
ATOM   1009 C  CE   . MET   A 1 152 ? 1.357   -14.338 -38.889 1.00 31.58  ? 359 MET   A CE   1 
ATOM   1010 N  N    . LYS   A 1 153 ? -2.894  -19.274 -39.725 1.00 21.72  ? 360 LYS   A N    1 
ATOM   1011 C  CA   . LYS   A 1 153 ? -3.349  -20.366 -38.823 1.00 23.29  ? 360 LYS   A CA   1 
ATOM   1012 C  C    . LYS   A 1 153 ? -2.928  -20.069 -37.374 1.00 18.35  ? 360 LYS   A C    1 
ATOM   1013 O  O    . LYS   A 1 153 ? -2.264  -20.896 -36.728 1.00 19.53  ? 360 LYS   A O    1 
ATOM   1014 C  CB   . LYS   A 1 153 ? -2.816  -21.714 -39.311 1.00 24.88  ? 360 LYS   A CB   1 
ATOM   1015 C  CG   . LYS   A 1 153 ? -3.212  -22.109 -40.739 1.00 29.82  ? 360 LYS   A CG   1 
ATOM   1016 C  CD   . LYS   A 1 153 ? -2.559  -23.426 -41.232 1.00 37.87  ? 360 LYS   A CD   1 
ATOM   1017 C  CE   . LYS   A 1 153 ? -2.758  -23.689 -42.704 1.00 46.39  ? 360 LYS   A CE   1 
ATOM   1018 N  NZ   . LYS   A 1 153 ? -4.114  -24.231 -42.947 1.00 60.59  ? 360 LYS   A NZ   1 
ATOM   1019 N  N    . LEU   A 1 154 ? -3.345  -18.929 -36.847 1.00 16.35  ? 361 LEU   A N    1 
ATOM   1020 C  CA   . LEU   A 1 154 ? -3.088  -18.531 -35.441 1.00 17.26  ? 361 LEU   A CA   1 
ATOM   1021 C  C    . LEU   A 1 154 ? -3.518  -19.639 -34.487 1.00 18.39  ? 361 LEU   A C    1 
ATOM   1022 O  O    . LEU   A 1 154 ? -4.664  -20.082 -34.612 1.00 20.73  ? 361 LEU   A O    1 
ATOM   1023 C  CB   . LEU   A 1 154 ? -3.836  -17.218 -35.128 1.00 18.65  ? 361 LEU   A CB   1 
ATOM   1024 C  CG   . LEU   A 1 154 ? -3.568  -16.601 -33.754 1.00 18.11  ? 361 LEU   A CG   1 
ATOM   1025 C  CD1  . LEU   A 1 154 ? -2.116  -16.168 -33.661 1.00 18.68  ? 361 LEU   A CD1  1 
ATOM   1026 C  CD2  . LEU   A 1 154 ? -4.460  -15.418 -33.427 1.00 19.91  ? 361 LEU   A CD2  1 
ATOM   1027 N  N    . GLU   A 1 155 ? -2.651  -20.031 -33.552 1.00 17.69  ? 362 GLU   A N    1 
ATOM   1028 C  CA   . GLU   A 1 155 ? -2.862  -21.089 -32.543 1.00 17.93  ? 362 GLU   A CA   1 
ATOM   1029 C  C    . GLU   A 1 155 ? -3.231  -20.407 -31.233 1.00 16.83  ? 362 GLU   A C    1 
ATOM   1030 O  O    . GLU   A 1 155 ? -2.867  -19.206 -31.029 1.00 15.71  ? 362 GLU   A O    1 
ATOM   1031 C  CB   . GLU   A 1 155 ? -1.593  -21.910 -32.370 1.00 19.41  ? 362 GLU   A CB   1 
ATOM   1032 C  CG   . GLU   A 1 155 ? -1.229  -22.633 -33.646 1.00 19.67  ? 362 GLU   A CG   1 
ATOM   1033 C  CD   . GLU   A 1 155 ? 0.197   -23.115 -33.790 1.00 23.85  ? 362 GLU   A CD   1 
ATOM   1034 O  OE1  . GLU   A 1 155 ? 0.990   -22.854 -32.878 1.00 26.84  ? 362 GLU   A OE1  1 
ATOM   1035 O  OE2  . GLU   A 1 155 ? 0.496   -23.709 -34.835 1.00 28.12  ? 362 GLU   A OE2  1 
ATOM   1036 N  N    . LYS   A 1 156 ? -3.988  -21.056 -30.369 1.00 18.58  ? 363 LYS   A N    1 
ATOM   1037 C  CA   . LYS   A 1 156 ? -4.285  -20.491 -29.025 1.00 17.26  ? 363 LYS   A CA   1 
ATOM   1038 C  C    . LYS   A 1 156 ? -3.014  -19.995 -28.289 1.00 17.25  ? 363 LYS   A C    1 
ATOM   1039 O  O    . LYS   A 1 156 ? -3.084  -18.985 -27.562 1.00 16.95  ? 363 LYS   A O    1 
ATOM   1040 C  CB   . LYS   A 1 156 ? -5.072  -21.509 -28.196 1.00 19.39  ? 363 LYS   A CB   1 
ATOM   1041 C  CG   . LYS   A 1 156 ? -5.652  -20.909 -26.933 1.00 28.04  ? 363 LYS   A CG   1 
ATOM   1042 C  CD   . LYS   A 1 156 ? -6.763  -21.664 -26.279 1.00 36.81  ? 363 LYS   A CD   1 
ATOM   1043 C  CE   . LYS   A 1 156 ? -7.384  -20.810 -25.198 1.00 45.25  ? 363 LYS   A CE   1 
ATOM   1044 N  NZ   . LYS   A 1 156 ? -8.359  -21.582 -24.388 1.00 50.67  ? 363 LYS   A NZ   1 
ATOM   1045 N  N    . GLU   A 1 157 ? -1.949  -20.781 -28.327 1.00 17.97  ? 364 GLU   A N    1 
ATOM   1046 C  CA   . GLU   A 1 157 ? -0.678  -20.456 -27.649 1.00 17.41  ? 364 GLU   A CA   1 
ATOM   1047 C  C    . GLU   A 1 157 ? -0.214  -19.061 -28.109 1.00 14.68  ? 364 GLU   A C    1 
ATOM   1048 O  O    . GLU   A 1 157 ? 0.340   -18.302 -27.263 1.00 20.44  ? 364 GLU   A O    1 
ATOM   1049 C  CB   . GLU   A 1 157 ? 0.376   -21.489 -27.990 1.00 20.19  ? 364 GLU   A CB   1 
ATOM   1050 C  CG   . GLU   A 1 157 ? 0.157   -22.888 -27.358 1.00 23.86  ? 364 GLU   A CG   1 
ATOM   1051 C  CD   . GLU   A 1 157 ? -0.879  -23.821 -27.963 1.00 25.94  ? 364 GLU   A CD   1 
ATOM   1052 O  OE1  . GLU   A 1 157 ? -1.495  -23.483 -29.028 1.00 23.55  ? 364 GLU   A OE1  1 
ATOM   1053 O  OE2  . GLU   A 1 157 ? -1.072  -24.902 -27.370 1.00 27.37  ? 364 GLU   A OE2  1 
ATOM   1054 N  N    . GLU   A 1 158 ? -0.323  -18.811 -29.401 1.00 14.32  ? 365 GLU   A N    1 
ATOM   1055 C  CA   . GLU   A 1 158 ? 0.180   -17.587 -30.058 1.00 14.79  ? 365 GLU   A CA   1 
ATOM   1056 C  C    . GLU   A 1 158 ? -0.758  -16.433 -29.681 1.00 14.14  ? 365 GLU   A C    1 
ATOM   1057 O  O    . GLU   A 1 158 ? -0.330  -15.329 -29.352 1.00 16.85  ? 365 GLU   A O    1 
ATOM   1058 C  CB   . GLU   A 1 158 ? 0.269   -17.772 -31.565 1.00 15.85  ? 365 GLU   A CB   1 
ATOM   1059 C  CG   . GLU   A 1 158 ? 1.227   -18.876 -31.946 1.00 16.91  ? 365 GLU   A CG   1 
ATOM   1060 C  CD   . GLU   A 1 158 ? 1.218   -19.291 -33.392 1.00 20.86  ? 365 GLU   A CD   1 
ATOM   1061 O  OE1  . GLU   A 1 158 ? 0.130   -19.377 -34.009 1.00 17.69  ? 365 GLU   A OE1  1 
ATOM   1062 O  OE2  . GLU   A 1 158 ? 2.303   -19.421 -33.928 1.00 20.78  ? 365 GLU   A OE2  1 
ATOM   1063 N  N    . PHE   A 1 159 ? -2.045  -16.729 -29.624 1.00 15.10  ? 366 PHE   A N    1 
ATOM   1064 C  CA   . PHE   A 1 159 ? -3.020  -15.699 -29.244 1.00 14.73  ? 366 PHE   A CA   1 
ATOM   1065 C  C    . PHE   A 1 159 ? -2.781  -15.203 -27.822 1.00 15.98  ? 366 PHE   A C    1 
ATOM   1066 O  O    . PHE   A 1 159 ? -2.758  -13.991 -27.617 1.00 18.45  ? 366 PHE   A O    1 
ATOM   1067 C  CB   . PHE   A 1 159 ? -4.375  -16.359 -29.381 1.00 15.38  ? 366 PHE   A CB   1 
ATOM   1068 C  CG   . PHE   A 1 159 ? -5.463  -15.712 -28.587 1.00 19.14  ? 366 PHE   A CG   1 
ATOM   1069 C  CD1  . PHE   A 1 159 ? -5.871  -14.410 -28.845 1.00 20.37  ? 366 PHE   A CD1  1 
ATOM   1070 C  CD2  . PHE   A 1 159 ? -6.070  -16.396 -27.566 1.00 21.00  ? 366 PHE   A CD2  1 
ATOM   1071 C  CE1  . PHE   A 1 159 ? -6.868  -13.825 -28.092 1.00 19.92  ? 366 PHE   A CE1  1 
ATOM   1072 C  CE2  . PHE   A 1 159 ? -7.116  -15.828 -26.854 1.00 22.40  ? 366 PHE   A CE2  1 
ATOM   1073 C  CZ   . PHE   A 1 159 ? -7.504  -14.543 -27.114 1.00 22.96  ? 366 PHE   A CZ   1 
ATOM   1074 N  N    . VAL   A 1 160 ? -2.635  -16.097 -26.836 1.00 15.49  ? 367 VAL   A N    1 
ATOM   1075 C  CA   . VAL   A 1 160 ? -2.507  -15.694 -25.413 1.00 15.29  ? 367 VAL   A CA   1 
ATOM   1076 C  C    . VAL   A 1 160 ? -1.176  -14.936 -25.265 1.00 14.81  ? 367 VAL   A C    1 
ATOM   1077 O  O    . VAL   A 1 160 ? -1.084  -14.007 -24.458 1.00 16.61  ? 367 VAL   A O    1 
ATOM   1078 C  CB   . VAL   A 1 160 ? -2.632  -16.867 -24.447 1.00 16.48  ? 367 VAL   A CB   1 
ATOM   1079 C  CG1  . VAL   A 1 160 ? -4.077  -17.384 -24.481 1.00 16.39  ? 367 VAL   A CG1  1 
ATOM   1080 C  CG2  . VAL   A 1 160 ? -1.570  -17.922 -24.715 1.00 21.44  ? 367 VAL   A CG2  1 
ATOM   1081 N  N    . THR   A 1 161 ? -0.159  -15.365 -25.983 1.00 16.92  ? 368 THR   A N    1 
ATOM   1082 C  CA   . THR   A 1 161 ? 1.163   -14.685 -25.923 1.00 15.95  ? 368 THR   A CA   1 
ATOM   1083 C  C    . THR   A 1 161 ? 1.078   -13.286 -26.550 1.00 14.02  ? 368 THR   A C    1 
ATOM   1084 O  O    . THR   A 1 161 ? 1.573   -12.347 -25.901 1.00 15.16  ? 368 THR   A O    1 
ATOM   1085 C  CB   . THR   A 1 161 ? 2.267   -15.554 -26.506 1.00 15.55  ? 368 THR   A CB   1 
ATOM   1086 O  OG1  . THR   A 1 161 ? 2.168   -16.839 -25.900 1.00 17.33  ? 368 THR   A OG1  1 
ATOM   1087 C  CG2  . THR   A 1 161 ? 3.611   -14.962 -26.174 1.00 18.62  ? 368 THR   A CG2  1 
ATOM   1088 N  N    . LEU   A 1 162 ? 0.421   -13.137 -27.698 1.00 14.65  ? 369 LEU   A N    1 
ATOM   1089 C  CA   . LEU   A 1 162 ? 0.234   -11.803 -28.323 1.00 14.85  ? 369 LEU   A CA   1 
ATOM   1090 C  C    . LEU   A 1 162 ? -0.603  -10.908 -27.394 1.00 14.35  ? 369 LEU   A C    1 
ATOM   1091 O  O    . LEU   A 1 162 ? -0.333  -9.725  -27.376 1.00 15.79  ? 369 LEU   A O    1 
ATOM   1092 C  CB   . LEU   A 1 162 ? -0.413  -11.939 -29.695 1.00 14.35  ? 369 LEU   A CB   1 
ATOM   1093 C  CG   . LEU   A 1 162 ? 0.499   -12.389 -30.819 1.00 16.71  ? 369 LEU   A CG   1 
ATOM   1094 C  CD1  . LEU   A 1 162 ? -0.276  -12.723 -32.104 1.00 21.31  ? 369 LEU   A CD1  1 
ATOM   1095 C  CD2  . LEU   A 1 162 ? 1.513   -11.328 -31.121 1.00 18.75  ? 369 LEU   A CD2  1 
ATOM   1096 N  N    . LYS   A 1 163 ? -1.635  -11.408 -26.706 1.00 15.16  ? 370 LYS   A N    1 
ATOM   1097 C  CA   . LYS   A 1 163 ? -2.480  -10.575 -25.775 1.00 17.22  ? 370 LYS   A CA   1 
ATOM   1098 C  C    . LYS   A 1 163 ? -1.559  -10.008 -24.707 1.00 15.42  ? 370 LYS   A C    1 
ATOM   1099 O  O    . LYS   A 1 163 ? -1.636  -8.806  -24.437 1.00 17.92  ? 370 LYS   A O    1 
ATOM   1100 C  CB   . LYS   A 1 163 ? -3.619  -11.340 -25.077 1.00 19.46  ? 370 LYS   A CB   1 
ATOM   1101 C  CG   . LYS   A 1 163 ? -4.923  -11.467 -25.811 1.00 24.25  ? 370 LYS   A CG   1 
ATOM   1102 C  CD   . LYS   A 1 163 ? -6.023  -11.931 -24.902 1.00 23.76  ? 370 LYS   A CD   1 
ATOM   1103 C  CE   . LYS   A 1 163 ? -5.756  -13.215 -24.166 1.00 28.88  ? 370 LYS   A CE   1 
ATOM   1104 N  NZ   . LYS   A 1 163 ? -6.971  -13.590 -23.429 1.00 32.08  ? 370 LYS   A NZ   1 
ATOM   1105 N  N    . ALA   A 1 164 ? -0.646  -10.827 -24.170 1.00 15.94  ? 371 ALA   A N    1 
ATOM   1106 C  CA   . ALA   A 1 164 ? 0.299   -10.393 -23.114 1.00 14.55  ? 371 ALA   A CA   1 
ATOM   1107 C  C    . ALA   A 1 164 ? 1.254   -9.367  -23.730 1.00 13.25  ? 371 ALA   A C    1 
ATOM   1108 O  O    . ALA   A 1 164 ? 1.512   -8.330  -23.032 1.00 15.76  ? 371 ALA   A O    1 
ATOM   1109 C  CB   . ALA   A 1 164 ? 0.983   -11.594 -22.510 1.00 15.60  ? 371 ALA   A CB   1 
ATOM   1110 N  N    . ILE   A 1 165 ? 1.778   -9.624  -24.915 1.00 14.80  ? 372 ILE   A N    1 
ATOM   1111 C  CA   . ILE   A 1 165 ? 2.714   -8.670  -25.575 1.00 16.28  ? 372 ILE   A CA   1 
ATOM   1112 C  C    . ILE   A 1 165 ? 1.998   -7.353  -25.846 1.00 13.49  ? 372 ILE   A C    1 
ATOM   1113 O  O    . ILE   A 1 165 ? 2.619   -6.312  -25.578 1.00 16.37  ? 372 ILE   A O    1 
ATOM   1114 C  CB   . ILE   A 1 165 ? 3.308   -9.276  -26.848 1.00 14.86  ? 372 ILE   A CB   1 
ATOM   1115 C  CG1  . ILE   A 1 165 ? 4.284   -10.403 -26.470 1.00 15.57  ? 372 ILE   A CG1  1 
ATOM   1116 C  CG2  . ILE   A 1 165 ? 3.934   -8.211  -27.705 1.00 17.82  ? 372 ILE   A CG2  1 
ATOM   1117 C  CD1  . ILE   A 1 165 ? 4.706   -11.232 -27.657 1.00 17.09  ? 372 ILE   A CD1  1 
ATOM   1118 N  N    . ALA   A 1 166 ? 0.728   -7.377  -26.266 1.00 15.55  ? 373 ALA   A N    1 
ATOM   1119 C  CA   . ALA   A 1 166 ? -0.028  -6.126  -26.543 1.00 16.89  ? 373 ALA   A CA   1 
ATOM   1120 C  C    . ALA   A 1 166 ? -0.170  -5.315  -25.261 1.00 17.06  ? 373 ALA   A C    1 
ATOM   1121 O  O    . ALA   A 1 166 ? -0.035  -4.066  -25.314 1.00 16.68  ? 373 ALA   A O    1 
ATOM   1122 C  CB   . ALA   A 1 166 ? -1.373  -6.422  -27.112 1.00 18.12  ? 373 ALA   A CB   1 
ATOM   1123 N  N    . LEU   A 1 167 ? -0.375  -5.957  -24.134 1.00 15.38  ? 374 LEU   A N    1 
ATOM   1124 C  CA   . LEU   A 1 167 ? -0.399  -5.272  -22.821 1.00 14.96  ? 374 LEU   A CA   1 
ATOM   1125 C  C    . LEU   A 1 167 ? 0.976   -4.636  -22.558 1.00 16.52  ? 374 LEU   A C    1 
ATOM   1126 O  O    . LEU   A 1 167 ? 1.035   -3.463  -22.200 1.00 17.81  ? 374 LEU   A O    1 
ATOM   1127 C  CB   . LEU   A 1 167 ? -0.809  -6.232  -21.698 1.00 17.10  ? 374 LEU   A CB   1 
ATOM   1128 C  CG   . LEU   A 1 167 ? -0.873  -5.630  -20.287 1.00 20.10  ? 374 LEU   A CG   1 
ATOM   1129 C  CD1  . LEU   A 1 167 ? -1.930  -4.541  -20.163 1.00 21.10  ? 374 LEU   A CD1  1 
ATOM   1130 C  CD2  . LEU   A 1 167 ? -1.114  -6.690  -19.223 1.00 22.41  ? 374 LEU   A CD2  1 
ATOM   1131 N  N    . ALA   A 1 168 ? 2.044   -5.433  -22.618 1.00 16.89  ? 375 ALA   A N    1 
ATOM   1132 C  CA   . ALA   A 1 168 ? 3.385   -4.951  -22.234 1.00 19.45  ? 375 ALA   A CA   1 
ATOM   1133 C  C    . ALA   A 1 168 ? 3.835   -3.860  -23.192 1.00 14.84  ? 375 ALA   A C    1 
ATOM   1134 O  O    . ALA   A 1 168 ? 4.550   -2.940  -22.723 1.00 20.10  ? 375 ALA   A O    1 
ATOM   1135 C  CB   . ALA   A 1 168 ? 4.337   -6.111  -22.230 1.00 19.54  ? 375 ALA   A CB   1 
ATOM   1136 N  N    . ASN   A 1 169 ? 3.483   -3.959  -24.455 1.00 14.82  ? 376 ASN   A N    1 
ATOM   1137 C  CA   . ASN   A 1 169 ? 3.943   -3.047  -25.538 1.00 14.97  ? 376 ASN   A CA   1 
ATOM   1138 C  C    . ASN   A 1 169 ? 2.935   -1.938  -25.856 1.00 14.31  ? 376 ASN   A C    1 
ATOM   1139 O  O    . ASN   A 1 169 ? 2.915   -1.497  -27.029 1.00 17.66  ? 376 ASN   A O    1 
ATOM   1140 C  CB   . ASN   A 1 169 ? 4.180   -3.844  -26.812 1.00 15.80  ? 376 ASN   A CB   1 
ATOM   1141 C  CG   . ASN   A 1 169 ? 5.071   -3.177  -27.817 1.00 15.99  ? 376 ASN   A CG   1 
ATOM   1142 O  OD1  . ASN   A 1 169 ? 6.042   -2.539  -27.400 1.00 18.74  ? 376 ASN   A OD1  1 
ATOM   1143 N  ND2  . ASN   A 1 169 ? 4.747   -3.325  -29.089 1.00 17.45  ? 376 ASN   A ND2  1 
ATOM   1144 N  N    . SER   A 1 170 ? 2.148   -1.481  -24.887 1.00 17.80  ? 377 SER   A N    1 
ATOM   1145 C  CA   . SER   A 1 170 ? 0.996   -0.600  -25.201 1.00 18.22  ? 377 SER   A CA   1 
ATOM   1146 C  C    . SER   A 1 170 ? 1.393   0.859   -25.355 1.00 16.44  ? 377 SER   A C    1 
ATOM   1147 O  O    . SER   A 1 170 ? 0.466   1.629   -25.704 1.00 17.02  ? 377 SER   A O    1 
ATOM   1148 C  CB   . SER   A 1 170 ? -0.094  -0.830  -24.169 1.00 23.43  ? 377 SER   A CB   1 
ATOM   1149 O  OG   . SER   A 1 170 ? 0.413   -0.615  -22.865 1.00 30.35  ? 377 SER   A OG   1 
ATOM   1150 N  N    . ASP   A 1 171 ? 2.662   1.245   -25.146 1.00 17.18  ? 378 ASP   A N    1 
ATOM   1151 C  CA   . ASP   A 1 171 ? 3.133   2.617   -25.510 1.00 18.43  ? 378 ASP   A CA   1 
ATOM   1152 C  C    . ASP   A 1 171 ? 2.380   3.705   -24.723 1.00 17.84  ? 378 ASP   A C    1 
ATOM   1153 O  O    . ASP   A 1 171 ? 2.264   4.856   -25.220 1.00 21.33  ? 378 ASP   A O    1 
ATOM   1154 C  CB   . ASP   A 1 171 ? 3.044   2.860   -27.006 1.00 18.57  ? 378 ASP   A CB   1 
ATOM   1155 C  CG   . ASP   A 1 171 ? 4.000   1.976   -27.764 1.00 18.05  ? 378 ASP   A CG   1 
ATOM   1156 O  OD1  . ASP   A 1 171 ? 5.213   2.022   -27.434 1.00 19.31  ? 378 ASP   A OD1  1 
ATOM   1157 O  OD2  . ASP   A 1 171 ? 3.555   1.368   -28.758 1.00 16.21  ? 378 ASP   A OD2  1 
ATOM   1158 N  N    . SER   A 1 172 ? 2.064   3.433   -23.470 1.00 18.12  ? 379 SER   A N    1 
ATOM   1159 C  CA   . SER   A 1 172 ? 1.568   4.470   -22.533 1.00 18.95  ? 379 SER   A CA   1 
ATOM   1160 C  C    . SER   A 1 172 ? 2.585   5.630   -22.425 1.00 17.95  ? 379 SER   A C    1 
ATOM   1161 O  O    . SER   A 1 172 ? 3.830   5.397   -22.366 1.00 21.32  ? 379 SER   A O    1 
ATOM   1162 C  CB   . SER   A 1 172 ? 1.274   3.922   -21.172 1.00 21.48  ? 379 SER   A CB   1 
ATOM   1163 O  OG   . SER   A 1 172 ? 0.928   4.984   -20.305 1.00 28.56  ? 379 SER   A OG   1 
ATOM   1164 N  N    . MET   A 1 173 ? 2.078   6.860   -22.433 1.00 20.66  ? 380 MET   A N    1 
ATOM   1165 C  CA   . MET   A 1 173 ? 2.858   8.110   -22.222 1.00 27.42  ? 380 MET   A CA   1 
ATOM   1166 C  C    . MET   A 1 173 ? 3.317   8.268   -20.769 1.00 27.43  ? 380 MET   A C    1 
ATOM   1167 O  O    . MET   A 1 173 ? 4.039   9.287   -20.478 1.00 31.78  ? 380 MET   A O    1 
ATOM   1168 C  CB   . MET   A 1 173 ? 1.950   9.312   -22.474 1.00 36.13  ? 380 MET   A CB   1 
ATOM   1169 C  CG   . MET   A 1 173 ? 1.951   9.820   -23.842 1.00 44.51  ? 380 MET   A CG   1 
ATOM   1170 S  SD   . MET   A 1 173 ? 0.765   11.213  -23.827 1.00 69.91  ? 380 MET   A SD   1 
ATOM   1171 C  CE   . MET   A 1 173 ? 1.567   12.420  -22.763 1.00 76.07  ? 380 MET   A CE   1 
ATOM   1172 N  N    . HIS   A 1 174 ? 2.797   7.465   -19.844 1.00 26.85  ? 381 HIS   A N    1 
ATOM   1173 C  CA   . HIS   A 1 174 ? 2.765   7.809   -18.400 1.00 30.43  ? 381 HIS   A CA   1 
ATOM   1174 C  C    . HIS   A 1 174 ? 3.652   6.848   -17.600 1.00 25.02  ? 381 HIS   A C    1 
ATOM   1175 O  O    . HIS   A 1 174 ? 3.546   6.843   -16.350 1.00 31.97  ? 381 HIS   A O    1 
ATOM   1176 C  CB   . HIS   A 1 174 ? 1.315   7.824   -17.870 1.00 32.04  ? 381 HIS   A CB   1 
ATOM   1177 C  CG   . HIS   A 1 174 ? 0.368   8.696   -18.637 1.00 31.93  ? 381 HIS   A CG   1 
ATOM   1178 N  ND1  . HIS   A 1 174 ? 0.350   10.075  -18.533 1.00 33.47  ? 381 HIS   A ND1  1 
ATOM   1179 C  CD2  . HIS   A 1 174 ? -0.625  8.389   -19.510 1.00 40.78  ? 381 HIS   A CD2  1 
ATOM   1180 C  CE1  . HIS   A 1 174 ? -0.583  10.586  -19.330 1.00 42.92  ? 381 HIS   A CE1  1 
ATOM   1181 N  NE2  . HIS   A 1 174 ? -1.205  9.572   -19.934 1.00 40.79  ? 381 HIS   A NE2  1 
ATOM   1182 N  N    . ILE   A 1 175 ? 4.486   6.062   -18.272 1.00 27.98  ? 382 ILE   A N    1 
ATOM   1183 C  CA   . ILE   A 1 175 ? 5.219   4.955   -17.598 1.00 27.61  ? 382 ILE   A CA   1 
ATOM   1184 C  C    . ILE   A 1 175 ? 6.246   5.549   -16.640 1.00 25.58  ? 382 ILE   A C    1 
ATOM   1185 O  O    . ILE   A 1 175 ? 6.957   6.475   -17.063 1.00 37.15  ? 382 ILE   A O    1 
ATOM   1186 C  CB   . ILE   A 1 175 ? 5.869   3.989   -18.610 1.00 26.83  ? 382 ILE   A CB   1 
ATOM   1187 C  CG1  . ILE   A 1 175 ? 4.850   3.288   -19.524 1.00 29.44  ? 382 ILE   A CG1  1 
ATOM   1188 C  CG2  . ILE   A 1 175 ? 6.671   2.986   -17.819 1.00 27.50  ? 382 ILE   A CG2  1 
ATOM   1189 C  CD1  . ILE   A 1 175 ? 3.793   2.618   -18.748 1.00 32.47  ? 382 ILE   A CD1  1 
ATOM   1190 N  N    . GLU   A 1 176 ? 6.270   5.086   -15.379 1.00 28.97  ? 383 GLU   A N    1 
ATOM   1191 C  CA   . GLU   A 1 176 ? 7.281   5.488   -14.359 1.00 31.62  ? 383 GLU   A CA   1 
ATOM   1192 C  C    . GLU   A 1 176 ? 8.572   4.707   -14.610 1.00 31.93  ? 383 GLU   A C    1 
ATOM   1193 O  O    . GLU   A 1 176 ? 9.612   5.376   -14.708 1.00 34.21  ? 383 GLU   A O    1 
ATOM   1194 C  CB   . GLU   A 1 176 ? 6.825   5.256   -12.915 1.00 27.35  ? 383 GLU   A CB   1 
ATOM   1195 C  CG   . GLU   A 1 176 ? 5.632   6.116   -12.465 1.00 39.04  ? 383 GLU   A CG   1 
ATOM   1196 C  CD   . GLU   A 1 176 ? 4.990   5.730   -11.120 1.00 45.60  ? 383 GLU   A CD   1 
ATOM   1197 O  OE1  . GLU   A 1 176 ? 5.358   4.633   -10.564 1.00 41.53  ? 383 GLU   A OE1  1 
ATOM   1198 O  OE2  . GLU   A 1 176 ? 4.097   6.509   -10.622 1.00 53.04  ? 383 GLU   A OE2  1 
ATOM   1199 N  N    . ASP   A 1 177 ? 8.533   3.378   -14.578 1.00 33.14  ? 384 ASP   A N    1 
ATOM   1200 C  CA   . ASP   A 1 177 ? 9.713   2.472   -14.649 1.00 31.14  ? 384 ASP   A CA   1 
ATOM   1201 C  C    . ASP   A 1 177 ? 9.852   1.910   -16.060 1.00 31.10  ? 384 ASP   A C    1 
ATOM   1202 O  O    . ASP   A 1 177 ? 9.432   0.735   -16.352 1.00 31.53  ? 384 ASP   A O    1 
ATOM   1203 C  CB   . ASP   A 1 177 ? 9.607   1.352   -13.616 1.00 30.40  ? 384 ASP   A CB   1 
ATOM   1204 C  CG   . ASP   A 1 177 ? 10.939  0.649   -13.411 1.00 27.57  ? 384 ASP   A CG   1 
ATOM   1205 O  OD1  . ASP   A 1 177 ? 11.775  0.651   -14.342 1.00 34.46  ? 384 ASP   A OD1  1 
ATOM   1206 O  OD2  . ASP   A 1 177 ? 11.138  0.127   -12.321 1.00 31.23  ? 384 ASP   A OD2  1 
ATOM   1207 N  N    . VAL   A 1 178 ? 10.399  2.728   -16.926 1.00 28.11  ? 385 VAL   A N    1 
ATOM   1208 C  CA   . VAL   A 1 178 ? 10.533  2.389   -18.366 1.00 29.24  ? 385 VAL   A CA   1 
ATOM   1209 C  C    . VAL   A 1 178 ? 11.347  1.103   -18.540 1.00 26.39  ? 385 VAL   A C    1 
ATOM   1210 O  O    . VAL   A 1 178 ? 10.948  0.266   -19.353 1.00 28.05  ? 385 VAL   A O    1 
ATOM   1211 C  CB   . VAL   A 1 178 ? 11.126  3.586   -19.121 1.00 28.88  ? 385 VAL   A CB   1 
ATOM   1212 C  CG1  . VAL   A 1 178 ? 11.520  3.205   -20.539 1.00 37.00  ? 385 VAL   A CG1  1 
ATOM   1213 C  CG2  . VAL   A 1 178 ? 10.127  4.738   -19.142 1.00 31.51  ? 385 VAL   A CG2  1 
ATOM   1214 N  N    . GLU   A 1 179 ? 12.458  0.946   -17.821 1.00 28.43  ? 386 GLU   A N    1 
ATOM   1215 C  CA   . GLU   A 1 179 ? 13.287  -0.274  -17.896 1.00 28.78  ? 386 GLU   A CA   1 
ATOM   1216 C  C    . GLU   A 1 179 ? 12.465  -1.488  -17.465 1.00 23.91  ? 386 GLU   A C    1 
ATOM   1217 O  O    . GLU   A 1 179 ? 12.629  -2.520  -18.098 1.00 29.15  ? 386 GLU   A O    1 
ATOM   1218 C  CB   . GLU   A 1 179 ? 14.534  -0.152  -17.022 1.00 35.32  ? 386 GLU   A CB   1 
ATOM   1219 C  CG   . GLU   A 1 179 ? 15.720  0.457   -17.746 1.00 50.94  ? 386 GLU   A CG   1 
ATOM   1220 C  CD   . GLU   A 1 179 ? 16.956  0.684   -16.879 1.00 67.77  ? 386 GLU   A CD   1 
ATOM   1221 O  OE1  . GLU   A 1 179 ? 17.081  0.038   -15.786 1.00 71.09  ? 386 GLU   A OE1  1 
ATOM   1222 O  OE2  . GLU   A 1 179 ? 17.815  1.508   -17.295 1.00 83.12  ? 386 GLU   A OE2  1 
ATOM   1223 N  N    . ALA   A 1 180 ? 11.635  -1.401  -16.423 1.00 26.85  ? 387 ALA   A N    1 
ATOM   1224 C  CA   . ALA   A 1 180 ? 10.877  -2.588  -15.948 1.00 27.01  ? 387 ALA   A CA   1 
ATOM   1225 C  C    . ALA   A 1 180 ? 9.887   -3.011  -17.031 1.00 27.13  ? 387 ALA   A C    1 
ATOM   1226 O  O    . ALA   A 1 180 ? 9.691   -4.220  -17.256 1.00 26.20  ? 387 ALA   A O    1 
ATOM   1227 C  CB   . ALA   A 1 180 ? 10.172  -2.311  -14.646 1.00 27.21  ? 387 ALA   A CB   1 
ATOM   1228 N  N    . VAL   A 1 181 ? 9.262   -2.023  -17.676 1.00 24.37  ? 388 VAL   A N    1 
ATOM   1229 C  CA   . VAL   A 1 181 ? 8.221   -2.285  -18.703 1.00 22.32  ? 388 VAL   A CA   1 
ATOM   1230 C  C    . VAL   A 1 181 ? 8.927   -2.920  -19.923 1.00 20.48  ? 388 VAL   A C    1 
ATOM   1231 O  O    . VAL   A 1 181 ? 8.436   -3.912  -20.509 1.00 22.21  ? 388 VAL   A O    1 
ATOM   1232 C  CB   . VAL   A 1 181 ? 7.363   -1.039  -19.023 1.00 21.41  ? 388 VAL   A CB   1 
ATOM   1233 C  CG1  . VAL   A 1 181 ? 6.493   -1.264  -20.253 1.00 24.82  ? 388 VAL   A CG1  1 
ATOM   1234 C  CG2  . VAL   A 1 181 ? 6.422   -0.671  -17.863 1.00 26.67  ? 388 VAL   A CG2  1 
ATOM   1235 N  N    . GLN   A 1 182 ? 10.102  -2.419  -20.261 1.00 23.04  ? 389 GLN   A N    1 
ATOM   1236 C  CA   . GLN   A 1 182 ? 10.941  -2.993  -21.340 1.00 23.56  ? 389 GLN   A CA   1 
ATOM   1237 C  C    . GLN   A 1 182 ? 11.319  -4.448  -20.979 1.00 20.90  ? 389 GLN   A C    1 
ATOM   1238 O  O    . GLN   A 1 182 ? 11.300  -5.249  -21.876 1.00 22.29  ? 389 GLN   A O    1 
ATOM   1239 C  CB   . GLN   A 1 182 ? 12.164  -2.130  -21.626 1.00 28.39  ? 389 GLN   A CB   1 
ATOM   1240 C  CG   . GLN   A 1 182 ? 13.144  -2.797  -22.604 1.00 32.56  ? 389 GLN   A CG   1 
ATOM   1241 C  CD   . GLN   A 1 182 ? 12.624  -2.822  -24.027 1.00 35.88  ? 389 GLN   A CD   1 
ATOM   1242 O  OE1  . GLN   A 1 182 ? 12.346  -1.759  -24.603 1.00 63.63  ? 389 GLN   A OE1  1 
ATOM   1243 N  NE2  . GLN   A 1 182 ? 12.492  -4.016  -24.623 1.00 28.81  ? 389 GLN   A NE2  1 
ATOM   1244 N  N    . LYS   A 1 183 ? 11.648  -4.766  -19.726 1.00 23.96  ? 390 LYS   A N    1 
ATOM   1245 C  CA   . LYS   A 1 183 ? 12.004  -6.155  -19.307 1.00 26.05  ? 390 LYS   A CA   1 
ATOM   1246 C  C    . LYS   A 1 183 ? 10.764  -7.051  -19.421 1.00 24.81  ? 390 LYS   A C    1 
ATOM   1247 O  O    . LYS   A 1 183 ? 10.927  -8.201  -19.888 1.00 24.32  ? 390 LYS   A O    1 
ATOM   1248 C  CB   . LYS   A 1 183 ? 12.582  -6.233  -17.895 1.00 32.48  ? 390 LYS   A CB   1 
ATOM   1249 C  CG   . LYS   A 1 183 ? 13.099  -7.603  -17.453 1.00 48.24  ? 390 LYS   A CG   1 
ATOM   1250 C  CD   . LYS   A 1 183 ? 13.418  -7.695  -15.947 1.00 70.44  ? 390 LYS   A CD   1 
ATOM   1251 C  CE   . LYS   A 1 183 ? 12.443  -8.547  -15.144 1.00 76.85  ? 390 LYS   A CE   1 
ATOM   1252 N  NZ   . LYS   A 1 183 ? 13.150  -9.430  -14.191 1.00 91.68  ? 390 LYS   A NZ   1 
ATOM   1253 N  N    . LEU   A 1 184 ? 9.566   -6.544  -19.101 1.00 21.12  ? 391 LEU   A N    1 
ATOM   1254 C  CA   . LEU   A 1 184 ? 8.328   -7.343  -19.272 1.00 20.00  ? 391 LEU   A CA   1 
ATOM   1255 C  C    . LEU   A 1 184 ? 8.107   -7.627  -20.772 1.00 19.39  ? 391 LEU   A C    1 
ATOM   1256 O  O    . LEU   A 1 184 ? 7.868   -8.819  -21.165 1.00 20.93  ? 391 LEU   A O    1 
ATOM   1257 C  CB   . LEU   A 1 184 ? 7.164   -6.599  -18.642 1.00 20.91  ? 391 LEU   A CB   1 
ATOM   1258 C  CG   . LEU   A 1 184 ? 5.808   -7.239  -18.888 1.00 23.72  ? 391 LEU   A CG   1 
ATOM   1259 C  CD1  . LEU   A 1 184 ? 5.754   -8.602  -18.251 1.00 23.95  ? 391 LEU   A CD1  1 
ATOM   1260 C  CD2  . LEU   A 1 184 ? 4.721   -6.367  -18.308 1.00 24.00  ? 391 LEU   A CD2  1 
ATOM   1261 N  N    . GLN   A 1 185 ? 8.263   -6.634  -21.636 1.00 17.91  ? 392 GLN   A N    1 
ATOM   1262 C  CA   . GLN   A 1 185 ? 8.228   -6.834  -23.106 1.00 18.21  ? 392 GLN   A CA   1 
ATOM   1263 C  C    . GLN   A 1 185 ? 9.205   -7.949  -23.482 1.00 16.30  ? 392 GLN   A C    1 
ATOM   1264 O  O    . GLN   A 1 185 ? 8.796   -8.824  -24.266 1.00 18.86  ? 392 GLN   A O    1 
ATOM   1265 C  CB   . GLN   A 1 185 ? 8.574   -5.537  -23.833 1.00 21.51  ? 392 GLN   A CB   1 
ATOM   1266 C  CG   . GLN   A 1 185 ? 7.441   -4.490  -23.773 1.00 20.30  ? 392 GLN   A CG   1 
ATOM   1267 C  CD   . GLN   A 1 185 ? 7.894   -3.137  -24.292 1.00 21.07  ? 392 GLN   A CD   1 
ATOM   1268 O  OE1  . GLN   A 1 185 ? 8.838   -3.021  -25.100 1.00 21.84  ? 392 GLN   A OE1  1 
ATOM   1269 N  NE2  . GLN   A 1 185 ? 7.177   -2.100  -23.858 1.00 19.97  ? 392 GLN   A NE2  1 
ATOM   1270 N  N    . ASP   A 1 186 ? 10.454  -7.879  -22.996 1.00 17.97  ? 393 ASP   A N    1 
ATOM   1271 C  CA   . ASP   A 1 186 ? 11.530  -8.790  -23.448 1.00 22.09  ? 393 ASP   A CA   1 
ATOM   1272 C  C    . ASP   A 1 186 ? 11.127  -10.203 -23.048 1.00 19.99  ? 393 ASP   A C    1 
ATOM   1273 O  O    . ASP   A 1 186 ? 11.374  -11.085 -23.842 1.00 18.30  ? 393 ASP   A O    1 
ATOM   1274 C  CB   . ASP   A 1 186 ? 12.898  -8.367  -22.881 1.00 24.04  ? 393 ASP   A CB   1 
ATOM   1275 C  CG   . ASP   A 1 186 ? 13.413  -7.036  -23.440 1.00 37.66  ? 393 ASP   A CG   1 
ATOM   1276 O  OD1  . ASP   A 1 186 ? 12.895  -6.557  -24.495 1.00 41.01  ? 393 ASP   A OD1  1 
ATOM   1277 O  OD2  . ASP   A 1 186 ? 14.353  -6.474  -22.807 1.00 49.80  ? 393 ASP   A OD2  1 
ATOM   1278 N  N    . VAL   A 1 187 ? 10.629  -10.380 -21.827 1.00 21.23  ? 394 VAL   A N    1 
ATOM   1279 C  CA   . VAL   A 1 187 ? 10.299  -11.725 -21.266 1.00 23.65  ? 394 VAL   A CA   1 
ATOM   1280 C  C    . VAL   A 1 187 ? 9.252   -12.382 -22.164 1.00 19.95  ? 394 VAL   A C    1 
ATOM   1281 O  O    . VAL   A 1 187 ? 9.359   -13.598 -22.554 1.00 21.16  ? 394 VAL   A O    1 
ATOM   1282 C  CB   . VAL   A 1 187 ? 9.870   -11.549 -19.808 1.00 25.02  ? 394 VAL   A CB   1 
ATOM   1283 C  CG1  . VAL   A 1 187 ? 9.127   -12.732 -19.267 1.00 30.36  ? 394 VAL   A CG1  1 
ATOM   1284 C  CG2  . VAL   A 1 187 ? 11.075  -11.263 -18.926 1.00 25.14  ? 394 VAL   A CG2  1 
ATOM   1285 N  N    . LEU   A 1 188 ? 8.220   -11.606 -22.472 1.00 16.97  ? 395 LEU   A N    1 
ATOM   1286 C  CA   . LEU   A 1 188 ? 7.118   -12.128 -23.320 1.00 16.66  ? 395 LEU   A CA   1 
ATOM   1287 C  C    . LEU   A 1 188 ? 7.535   -12.367 -24.774 1.00 15.77  ? 395 LEU   A C    1 
ATOM   1288 O  O    . LEU   A 1 188 ? 7.042   -13.320 -25.454 1.00 18.18  ? 395 LEU   A O    1 
ATOM   1289 C  CB   . LEU   A 1 188 ? 5.897   -11.209 -23.217 1.00 18.06  ? 395 LEU   A CB   1 
ATOM   1290 C  CG   . LEU   A 1 188 ? 5.394   -11.020 -21.802 1.00 18.15  ? 395 LEU   A CG   1 
ATOM   1291 C  CD1  . LEU   A 1 188 ? 4.360   -9.901  -21.778 1.00 18.52  ? 395 LEU   A CD1  1 
ATOM   1292 C  CD2  . LEU   A 1 188 ? 4.779   -12.303 -21.281 1.00 20.78  ? 395 LEU   A CD2  1 
ATOM   1293 N  N    . HIS   A 1 189 ? 8.269   -11.442 -25.348 1.00 15.89  ? 396 HIS   A N    1 
ATOM   1294 C  CA   . HIS   A 1 189 ? 8.812   -11.609 -26.713 1.00 13.71  ? 396 HIS   A CA   1 
ATOM   1295 C  C    . HIS   A 1 189 ? 9.653   -12.914 -26.756 1.00 12.58  ? 396 HIS   A C    1 
ATOM   1296 O  O    . HIS   A 1 189 ? 9.562   -13.600 -27.782 1.00 16.81  ? 396 HIS   A O    1 
ATOM   1297 C  CB   . HIS   A 1 189 ? 9.626   -10.380 -27.054 1.00 17.79  ? 396 HIS   A CB   1 
ATOM   1298 C  CG   . HIS   A 1 189 ? 10.342  -10.423 -28.355 1.00 16.25  ? 396 HIS   A CG   1 
ATOM   1299 N  ND1  . HIS   A 1 189 ? 11.314  -9.490  -28.644 1.00 19.16  ? 396 HIS   A ND1  1 
ATOM   1300 C  CD2  . HIS   A 1 189 ? 10.195  -11.167 -29.465 1.00 17.08  ? 396 HIS   A CD2  1 
ATOM   1301 C  CE1  . HIS   A 1 189 ? 11.768  -9.732  -29.856 1.00 20.48  ? 396 HIS   A CE1  1 
ATOM   1302 N  NE2  . HIS   A 1 189 ? 11.124  -10.788 -30.374 1.00 17.57  ? 396 HIS   A NE2  1 
ATOM   1303 N  N    . GLU   A 1 190 ? 10.516  -13.107 -25.764 1.00 16.50  ? 397 GLU   A N    1 
ATOM   1304 C  CA   . GLU   A 1 190 ? 11.359  -14.317 -25.653 1.00 17.21  ? 397 GLU   A CA   1 
ATOM   1305 C  C    . GLU   A 1 190 ? 10.444  -15.550 -25.655 1.00 17.62  ? 397 GLU   A C    1 
ATOM   1306 O  O    . GLU   A 1 190 ? 10.755  -16.535 -26.381 1.00 19.62  ? 397 GLU   A O    1 
ATOM   1307 C  CB   . GLU   A 1 190 ? 12.220  -14.281 -24.399 1.00 20.60  ? 397 GLU   A CB   1 
ATOM   1308 C  CG   . GLU   A 1 190 ? 13.161  -15.479 -24.311 1.00 25.99  ? 397 GLU   A CG   1 
ATOM   1309 C  CD   . GLU   A 1 190 ? 14.017  -15.545 -23.063 1.00 27.39  ? 397 GLU   A CD   1 
ATOM   1310 O  OE1  . GLU   A 1 190 ? 13.629  -15.024 -22.027 1.00 29.88  ? 397 GLU   A OE1  1 
ATOM   1311 O  OE2  . GLU   A 1 190 ? 15.072  -16.140 -23.117 1.00 32.36  ? 397 GLU   A OE2  1 
ATOM   1312 N  N    . ALA   A 1 191 ? 9.353   -15.496 -24.902 1.00 15.33  ? 398 ALA   A N    1 
ATOM   1313 C  CA   . ALA   A 1 191 ? 8.417   -16.633 -24.811 1.00 18.11  ? 398 ALA   A CA   1 
ATOM   1314 C  C    . ALA   A 1 191 ? 7.887   -16.946 -26.217 1.00 17.73  ? 398 ALA   A C    1 
ATOM   1315 O  O    . ALA   A 1 191 ? 7.838   -18.126 -26.608 1.00 18.26  ? 398 ALA   A O    1 
ATOM   1316 C  CB   . ALA   A 1 191 ? 7.315   -16.324 -23.817 1.00 20.51  ? 398 ALA   A CB   1 
ATOM   1317 N  N    . LEU   A 1 192 ? 7.407   -15.926 -26.937 1.00 16.21  ? 399 LEU   A N    1 
ATOM   1318 C  CA   . LEU   A 1 192 ? 6.909   -16.101 -28.318 1.00 15.27  ? 399 LEU   A CA   1 
ATOM   1319 C  C    . LEU   A 1 192 ? 7.980   -16.731 -29.213 1.00 16.75  ? 399 LEU   A C    1 
ATOM   1320 O  O    . LEU   A 1 192 ? 7.626   -17.620 -30.009 1.00 16.92  ? 399 LEU   A O    1 
ATOM   1321 C  CB   . LEU   A 1 192 ? 6.355   -14.772 -28.825 1.00 17.07  ? 399 LEU   A CB   1 
ATOM   1322 C  CG   . LEU   A 1 192 ? 5.855   -14.754 -30.263 1.00 15.85  ? 399 LEU   A CG   1 
ATOM   1323 C  CD1  . LEU   A 1 192 ? 4.604   -15.590 -30.381 1.00 18.44  ? 399 LEU   A CD1  1 
ATOM   1324 C  CD2  . LEU   A 1 192 ? 5.624   -13.345 -30.800 1.00 18.08  ? 399 LEU   A CD2  1 
ATOM   1325 N  N    . GLN   A 1 193 ? 9.210   -16.199 -29.175 1.00 17.23  ? 400 GLN   A N    1 
ATOM   1326 C  CA   . GLN   A 1 193 ? 10.297  -16.640 -30.057 1.00 15.88  ? 400 GLN   A CA   1 
ATOM   1327 C  C    . GLN   A 1 193 ? 10.615  -18.111 -29.723 1.00 16.08  ? 400 GLN   A C    1 
ATOM   1328 O  O    . GLN   A 1 193 ? 10.784  -18.924 -30.677 1.00 18.79  ? 400 GLN   A O    1 
ATOM   1329 C  CB   . GLN   A 1 193 ? 11.556  -15.767 -29.891 1.00 22.60  ? 400 GLN   A CB   1 
ATOM   1330 C  CG   . GLN   A 1 193 ? 12.630  -16.087 -30.910 1.00 24.83  ? 400 GLN   A CG   1 
ATOM   1331 C  CD   . GLN   A 1 193 ? 12.056  -16.079 -32.308 1.00 25.69  ? 400 GLN   A CD   1 
ATOM   1332 O  OE1  . GLN   A 1 193 ? 11.890  -14.982 -32.868 1.00 24.75  ? 400 GLN   A OE1  1 
ATOM   1333 N  NE2  . GLN   A 1 193 ? 11.668  -17.263 -32.828 1.00 34.05  ? 400 GLN   A NE2  1 
ATOM   1334 N  N    . ASP   A 1 194 ? 10.713  -18.432 -28.433 1.00 19.69  ? 401 ASP   A N    1 
ATOM   1335 C  CA   A ASP   A 1 194 ? 11.040  -19.819 -28.012 0.50 21.67  ? 401 ASP   A CA   1 
ATOM   1336 C  CA   B ASP   A 1 194 ? 10.950  -19.802 -27.919 0.50 19.90  ? 401 ASP   A CA   1 
ATOM   1337 C  C    . ASP   A 1 194 ? 9.873   -20.738 -28.453 1.00 21.04  ? 401 ASP   A C    1 
ATOM   1338 O  O    . ASP   A 1 194 ? 10.188  -21.828 -28.938 1.00 24.17  ? 401 ASP   A O    1 
ATOM   1339 C  CB   A ASP   A 1 194 ? 11.497  -19.854 -26.543 0.50 21.99  ? 401 ASP   A CB   1 
ATOM   1340 C  CB   B ASP   A 1 194 ? 10.867  -19.824 -26.401 0.50 20.75  ? 401 ASP   A CB   1 
ATOM   1341 C  CG   A ASP   A 1 194 ? 11.841  -21.239 -25.991 0.50 23.13  ? 401 ASP   A CG   1 
ATOM   1342 C  CG   B ASP   A 1 194 ? 12.142  -19.331 -25.775 0.50 17.63  ? 401 ASP   A CG   1 
ATOM   1343 O  OD1  A ASP   A 1 194 ? 13.005  -21.763 -26.215 0.50 25.05  ? 401 ASP   A OD1  1 
ATOM   1344 O  OD1  B ASP   A 1 194 ? 13.130  -19.177 -26.536 0.50 21.16  ? 401 ASP   A OD1  1 
ATOM   1345 O  OD2  A ASP   A 1 194 ? 10.974  -21.783 -25.318 0.50 23.10  ? 401 ASP   A OD2  1 
ATOM   1346 O  OD2  B ASP   A 1 194 ? 12.136  -19.125 -24.571 0.50 20.46  ? 401 ASP   A OD2  1 
ATOM   1347 N  N    . TYR   A 1 195 ? 8.615   -20.318 -28.327 1.00 21.94  ? 402 TYR   A N    1 
ATOM   1348 C  CA   . TYR   A 1 195 ? 7.447   -21.129 -28.784 1.00 18.62  ? 402 TYR   A CA   1 
ATOM   1349 C  C    . TYR   A 1 195 ? 7.595   -21.406 -30.288 1.00 18.26  ? 402 TYR   A C    1 
ATOM   1350 O  O    . TYR   A 1 195 ? 7.457   -22.558 -30.774 1.00 23.17  ? 402 TYR   A O    1 
ATOM   1351 C  CB   . TYR   A 1 195 ? 6.108   -20.411 -28.561 1.00 20.09  ? 402 TYR   A CB   1 
ATOM   1352 C  CG   . TYR   A 1 195 ? 4.954   -21.244 -29.045 1.00 20.04  ? 402 TYR   A CG   1 
ATOM   1353 C  CD1  . TYR   A 1 195 ? 4.559   -22.377 -28.351 1.00 20.47  ? 402 TYR   A CD1  1 
ATOM   1354 C  CD2  . TYR   A 1 195 ? 4.358   -20.978 -30.262 1.00 21.08  ? 402 TYR   A CD2  1 
ATOM   1355 C  CE1  . TYR   A 1 195 ? 3.505   -23.160 -28.817 1.00 24.62  ? 402 TYR   A CE1  1 
ATOM   1356 C  CE2  . TYR   A 1 195 ? 3.319   -21.748 -30.741 1.00 18.89  ? 402 TYR   A CE2  1 
ATOM   1357 C  CZ   . TYR   A 1 195 ? 2.882   -22.837 -30.017 1.00 20.60  ? 402 TYR   A CZ   1 
ATOM   1358 O  OH   . TYR   A 1 195 ? 1.858   -23.550 -30.564 1.00 25.34  ? 402 TYR   A OH   1 
ATOM   1359 N  N    . GLU   A 1 196 ? 7.857   -20.361 -31.060 1.00 16.86  ? 403 GLU   A N    1 
ATOM   1360 C  CA   . GLU   A 1 196 ? 7.901   -20.461 -32.541 1.00 18.03  ? 403 GLU   A CA   1 
ATOM   1361 C  C    . GLU   A 1 196 ? 9.127   -21.302 -32.966 1.00 18.67  ? 403 GLU   A C    1 
ATOM   1362 O  O    . GLU   A 1 196 ? 9.047   -22.012 -33.989 1.00 18.30  ? 403 GLU   A O    1 
ATOM   1363 C  CB   . GLU   A 1 196 ? 7.940   -19.074 -33.188 1.00 18.97  ? 403 GLU   A CB   1 
ATOM   1364 C  CG   . GLU   A 1 196 ? 6.636   -18.252 -33.022 1.00 16.85  ? 403 GLU   A CG   1 
ATOM   1365 C  CD   . GLU   A 1 196 ? 5.364   -18.954 -33.476 1.00 16.80  ? 403 GLU   A CD   1 
ATOM   1366 O  OE1  . GLU   A 1 196 ? 5.462   -19.874 -34.294 1.00 21.15  ? 403 GLU   A OE1  1 
ATOM   1367 O  OE2  . GLU   A 1 196 ? 4.267   -18.469 -33.116 1.00 21.29  ? 403 GLU   A OE2  1 
ATOM   1368 N  N    . ALA   A 1 197 ? 10.225  -21.186 -32.248 1.00 18.14  ? 404 ALA   A N    1 
ATOM   1369 C  CA   . ALA   A 1 197 ? 11.455  -21.910 -32.601 1.00 20.12  ? 404 ALA   A CA   1 
ATOM   1370 C  C    . ALA   A 1 197 ? 11.196  -23.409 -32.439 1.00 21.28  ? 404 ALA   A C    1 
ATOM   1371 O  O    . ALA   A 1 197 ? 11.690  -24.184 -33.276 1.00 29.81  ? 404 ALA   A O    1 
ATOM   1372 C  CB   . ALA   A 1 197 ? 12.632  -21.399 -31.785 1.00 22.27  ? 404 ALA   A CB   1 
ATOM   1373 N  N    . GLY   A 1 198 ? 10.428  -23.789 -31.426 1.00 26.05  ? 405 GLY   A N    1 
ATOM   1374 C  CA   . GLY   A 1 198 ? 10.122  -25.210 -31.122 1.00 20.75  ? 405 GLY   A CA   1 
ATOM   1375 C  C    . GLY   A 1 198 ? 8.974   -25.722 -31.953 1.00 27.26  ? 405 GLY   A C    1 
ATOM   1376 O  O    . GLY   A 1 198 ? 9.042   -26.859 -32.427 1.00 32.79  ? 405 GLY   A O    1 
ATOM   1377 N  N    . GLN   A 1 199 ? 7.934   -24.935 -32.155 1.00 26.01  ? 406 GLN   A N    1 
ATOM   1378 C  CA   . GLN   A 1 199 ? 6.684   -25.452 -32.799 1.00 23.03  ? 406 GLN   A CA   1 
ATOM   1379 C  C    . GLN   A 1 199 ? 6.735   -25.259 -34.322 1.00 23.25  ? 406 GLN   A C    1 
ATOM   1380 O  O    . GLN   A 1 199 ? 5.963   -25.908 -35.016 1.00 24.00  ? 406 GLN   A O    1 
ATOM   1381 C  CB   . GLN   A 1 199 ? 5.502   -24.733 -32.153 1.00 25.24  ? 406 GLN   A CB   1 
ATOM   1382 C  CG   . GLN   A 1 199 ? 4.125   -25.285 -32.511 1.00 30.69  ? 406 GLN   A CG   1 
ATOM   1383 C  CD   . GLN   A 1 199 ? 3.782   -26.674 -31.971 1.00 32.58  ? 406 GLN   A CD   1 
ATOM   1384 O  OE1  . GLN   A 1 199 ? 4.399   -27.211 -31.052 1.00 39.46  ? 406 GLN   A OE1  1 
ATOM   1385 N  NE2  . GLN   A 1 199 ? 2.718   -27.252 -32.506 1.00 41.76  ? 406 GLN   A NE2  1 
ATOM   1386 N  N    . HIS   A 1 200 ? 7.457   -24.236 -34.840 1.00 20.86  ? 407 HIS   A N    1 
ATOM   1387 C  CA   . HIS   A 1 200 ? 7.339   -23.870 -36.273 1.00 22.49  ? 407 HIS   A CA   1 
ATOM   1388 C  C    . HIS   A 1 200 ? 8.701   -23.741 -36.946 1.00 24.05  ? 407 HIS   A C    1 
ATOM   1389 O  O    . HIS   A 1 200 ? 9.005   -22.647 -37.519 1.00 25.14  ? 407 HIS   A O    1 
ATOM   1390 C  CB   . HIS   A 1 200 ? 6.547   -22.558 -36.365 1.00 19.79  ? 407 HIS   A CB   1 
ATOM   1391 C  CG   . HIS   A 1 200 ? 5.093   -22.813 -36.228 1.00 21.83  ? 407 HIS   A CG   1 
ATOM   1392 N  ND1  . HIS   A 1 200 ? 4.363   -23.292 -37.290 1.00 21.76  ? 407 HIS   A ND1  1 
ATOM   1393 C  CD2  . HIS   A 1 200 ? 4.271   -22.704 -35.159 1.00 20.45  ? 407 HIS   A CD2  1 
ATOM   1394 C  CE1  . HIS   A 1 200 ? 3.099   -23.430 -36.900 1.00 24.29  ? 407 HIS   A CE1  1 
ATOM   1395 N  NE2  . HIS   A 1 200 ? 3.028   -23.109 -35.565 1.00 22.73  ? 407 HIS   A NE2  1 
ATOM   1396 N  N    . MET   A 1 201 ? 9.482   -24.824 -36.934 1.00 24.29  ? 408 MET   A N    1 
ATOM   1397 C  CA   . MET   A 1 201 ? 10.843  -24.808 -37.513 1.00 27.71  ? 408 MET   A CA   1 
ATOM   1398 C  C    . MET   A 1 201 ? 10.738  -24.559 -39.027 1.00 26.07  ? 408 MET   A C    1 
ATOM   1399 O  O    . MET   A 1 201 ? 11.739  -24.060 -39.602 1.00 30.69  ? 408 MET   A O    1 
ATOM   1400 C  CB   . MET   A 1 201 ? 11.619  -26.093 -37.184 1.00 37.01  ? 408 MET   A CB   1 
ATOM   1401 C  CG   . MET   A 1 201 ? 11.902  -26.270 -35.681 1.00 49.16  ? 408 MET   A CG   1 
ATOM   1402 S  SD   . MET   A 1 201 ? 12.956  -27.725 -35.344 1.00 65.41  ? 408 MET   A SD   1 
ATOM   1403 C  CE   . MET   A 1 201 ? 12.886  -27.919 -33.556 1.00 54.81  ? 408 MET   A CE   1 
ATOM   1404 N  N    . GLU   A 1 202 ? 9.567   -24.795 -39.641 1.00 23.76  ? 409 GLU   A N    1 
ATOM   1405 C  CA   . GLU   A 1 202 ? 9.374   -24.610 -41.094 1.00 23.79  ? 409 GLU   A CA   1 
ATOM   1406 C  C    . GLU   A 1 202 ? 9.447   -23.118 -41.375 1.00 22.78  ? 409 GLU   A C    1 
ATOM   1407 O  O    . GLU   A 1 202 ? 9.745   -22.788 -42.489 1.00 23.90  ? 409 GLU   A O    1 
ATOM   1408 C  CB   . GLU   A 1 202 ? 8.073   -25.240 -41.611 1.00 25.92  ? 409 GLU   A CB   1 
ATOM   1409 C  CG   . GLU   A 1 202 ? 6.806   -24.430 -41.356 1.00 26.51  ? 409 GLU   A CG   1 
ATOM   1410 C  CD   . GLU   A 1 202 ? 6.271   -24.408 -39.929 1.00 26.71  ? 409 GLU   A CD   1 
ATOM   1411 O  OE1  . GLU   A 1 202 ? 6.797   -25.167 -39.073 1.00 27.74  ? 409 GLU   A OE1  1 
ATOM   1412 O  OE2  . GLU   A 1 202 ? 5.286   -23.686 -39.674 1.00 25.19  ? 409 GLU   A OE2  1 
ATOM   1413 N  N    . ASP   A 1 203 ? 9.147   -22.268 -40.414 1.00 21.10  ? 410 ASP   A N    1 
ATOM   1414 C  CA   . ASP   A 1 203 ? 9.147   -20.806 -40.698 1.00 21.93  ? 410 ASP   A CA   1 
ATOM   1415 C  C    . ASP   A 1 203 ? 9.961   -20.125 -39.615 1.00 17.73  ? 410 ASP   A C    1 
ATOM   1416 O  O    . ASP   A 1 203 ? 9.481   -19.772 -38.551 1.00 18.19  ? 410 ASP   A O    1 
ATOM   1417 C  CB   . ASP   A 1 203 ? 7.728   -20.245 -40.877 1.00 21.32  ? 410 ASP   A CB   1 
ATOM   1418 C  CG   . ASP   A 1 203 ? 7.709   -18.749 -41.105 1.00 20.37  ? 410 ASP   A CG   1 
ATOM   1419 O  OD1  . ASP   A 1 203 ? 8.795   -18.178 -41.343 1.00 23.68  ? 410 ASP   A OD1  1 
ATOM   1420 O  OD2  . ASP   A 1 203 ? 6.601   -18.201 -41.144 1.00 24.99  ? 410 ASP   A OD2  1 
ATOM   1421 N  N    . PRO   A 1 204 ? 11.262  -19.938 -39.819 1.00 22.69  ? 411 PRO   A N    1 
ATOM   1422 C  CA   . PRO   A 1 204 ? 12.050  -19.316 -38.770 1.00 22.87  ? 411 PRO   A CA   1 
ATOM   1423 C  C    . PRO   A 1 204 ? 11.693  -17.862 -38.497 1.00 21.87  ? 411 PRO   A C    1 
ATOM   1424 O  O    . PRO   A 1 204 ? 12.179  -17.397 -37.509 1.00 25.22  ? 411 PRO   A O    1 
ATOM   1425 C  CB   . PRO   A 1 204 ? 13.484  -19.413 -39.283 1.00 22.75  ? 411 PRO   A CB   1 
ATOM   1426 C  CG   . PRO   A 1 204 ? 13.346  -19.658 -40.781 1.00 33.02  ? 411 PRO   A CG   1 
ATOM   1427 C  CD   . PRO   A 1 204 ? 12.023  -20.371 -40.987 1.00 26.58  ? 411 PRO   A CD   1 
ATOM   1428 N  N    . ARG   A 1 205 ? 10.882  -17.214 -39.335 1.00 22.17  ? 412 ARG   A N    1 
ATOM   1429 C  CA   . ARG   A 1 205 ? 10.450  -15.787 -39.138 1.00 21.58  ? 412 ARG   A CA   1 
ATOM   1430 C  C    . ARG   A 1 205 ? 9.005   -15.686 -38.634 1.00 18.98  ? 412 ARG   A C    1 
ATOM   1431 O  O    . ARG   A 1 205 ? 8.406   -14.609 -38.683 1.00 17.90  ? 412 ARG   A O    1 
ATOM   1432 C  CB   . ARG   A 1 205 ? 10.726  -15.004 -40.420 1.00 28.23  ? 412 ARG   A CB   1 
ATOM   1433 C  CG   . ARG   A 1 205 ? 12.229  -14.838 -40.579 1.00 32.40  ? 412 ARG   A CG   1 
ATOM   1434 C  CD   . ARG   A 1 205 ? 12.711  -13.930 -41.660 1.00 41.99  ? 412 ARG   A CD   1 
ATOM   1435 N  NE   . ARG   A 1 205 ? 12.403  -14.465 -42.962 1.00 44.75  ? 412 ARG   A NE   1 
ATOM   1436 C  CZ   . ARG   A 1 205 ? 13.127  -15.382 -43.564 1.00 43.20  ? 412 ARG   A CZ   1 
ATOM   1437 N  NH1  . ARG   A 1 205 ? 14.180  -15.922 -42.961 1.00 45.05  ? 412 ARG   A NH1  1 
ATOM   1438 N  NH2  . ARG   A 1 205 ? 12.769  -15.784 -44.766 1.00 47.09  ? 412 ARG   A NH2  1 
ATOM   1439 N  N    . ARG   A 1 206 ? 8.441   -16.773 -38.169 1.00 16.13  ? 413 ARG   A N    1 
ATOM   1440 C  CA   . ARG   A 1 206 ? 7.012   -16.769 -37.777 1.00 15.11  ? 413 ARG   A CA   1 
ATOM   1441 C  C    . ARG   A 1 206 ? 6.822   -15.809 -36.596 1.00 13.35  ? 413 ARG   A C    1 
ATOM   1442 O  O    . ARG   A 1 206 ? 5.762   -15.147 -36.507 1.00 13.75  ? 413 ARG   A O    1 
ATOM   1443 C  CB   . ARG   A 1 206 ? 6.469   -18.183 -37.520 1.00 16.07  ? 413 ARG   A CB   1 
ATOM   1444 C  CG   . ARG   A 1 206 ? 4.959   -18.179 -37.218 1.00 18.11  ? 413 ARG   A CG   1 
ATOM   1445 C  CD   . ARG   A 1 206 ? 4.452   -19.630 -37.201 1.00 18.07  ? 413 ARG   A CD   1 
ATOM   1446 N  NE   . ARG   A 1 206 ? 3.151   -19.741 -36.604 1.00 19.05  ? 413 ARG   A NE   1 
ATOM   1447 C  CZ   . ARG   A 1 206 ? 2.034   -19.769 -37.302 1.00 17.91  ? 413 ARG   A CZ   1 
ATOM   1448 N  NH1  . ARG   A 1 206 ? 2.067   -19.635 -38.623 1.00 18.71  ? 413 ARG   A NH1  1 
ATOM   1449 N  NH2  . ARG   A 1 206 ? 0.877   -19.862 -36.664 1.00 19.91  ? 413 ARG   A NH2  1 
ATOM   1450 N  N    . ALA   A 1 207 ? 7.674   -15.824 -35.591 1.00 13.47  ? 414 ALA   A N    1 
ATOM   1451 C  CA   . ALA   A 1 207 ? 7.559   -14.894 -34.430 1.00 12.26  ? 414 ALA   A CA   1 
ATOM   1452 C  C    . ALA   A 1 207 ? 7.475   -13.454 -34.949 1.00 14.86  ? 414 ALA   A C    1 
ATOM   1453 O  O    . ALA   A 1 207 ? 6.525   -12.718 -34.467 1.00 15.62  ? 414 ALA   A O    1 
ATOM   1454 C  CB   . ALA   A 1 207 ? 8.612   -15.083 -33.389 1.00 16.25  ? 414 ALA   A CB   1 
ATOM   1455 N  N    . GLY   A 1 208 ? 8.345   -13.095 -35.896 1.00 15.36  ? 415 GLY   A N    1 
ATOM   1456 C  CA   . GLY   A 1 208 ? 8.353   -11.728 -36.441 1.00 16.45  ? 415 GLY   A CA   1 
ATOM   1457 C  C    . GLY   A 1 208 ? 7.051   -11.432 -37.140 1.00 13.04  ? 415 GLY   A C    1 
ATOM   1458 O  O    . GLY   A 1 208 ? 6.509   -10.320 -37.021 1.00 15.33  ? 415 GLY   A O    1 
ATOM   1459 N  N    . LYS   A 1 209 ? 6.547   -12.384 -37.892 1.00 15.22  ? 416 LYS   A N    1 
ATOM   1460 C  CA   . LYS   A 1 209 ? 5.300   -12.239 -38.647 1.00 13.42  ? 416 LYS   A CA   1 
ATOM   1461 C  C    . LYS   A 1 209 ? 4.159   -12.005 -37.644 1.00 17.43  ? 416 LYS   A C    1 
ATOM   1462 O  O    . LYS   A 1 209 ? 3.352   -11.157 -37.921 1.00 14.85  ? 416 LYS   A O    1 
ATOM   1463 C  CB   . LYS   A 1 209 ? 5.033   -13.484 -39.474 1.00 18.09  ? 416 LYS   A CB   1 
ATOM   1464 C  CG   . LYS   A 1 209 ? 5.827   -13.688 -40.741 1.00 18.76  ? 416 LYS   A CG   1 
ATOM   1465 C  CD   . LYS   A 1 209 ? 5.789   -15.065 -41.375 1.00 27.73  ? 416 LYS   A CD   1 
ATOM   1466 C  CE   . LYS   A 1 209 ? 7.036   -15.180 -42.220 1.00 26.82  ? 416 LYS   A CE   1 
ATOM   1467 N  NZ   . LYS   A 1 209 ? 6.891   -16.155 -43.292 1.00 35.15  ? 416 LYS   A NZ   1 
ATOM   1468 N  N    . MET   A 1 210 ? 4.128   -12.653 -36.497 1.00 13.68  ? 417 MET   A N    1 
ATOM   1469 C  CA   . MET   A 1 210 ? 3.161   -12.463 -35.411 1.00 15.84  ? 417 MET   A CA   1 
ATOM   1470 C  C    . MET   A 1 210 ? 3.298   -11.061 -34.845 1.00 12.87  ? 417 MET   A C    1 
ATOM   1471 O  O    . MET   A 1 210 ? 2.305   -10.360 -34.758 1.00 15.37  ? 417 MET   A O    1 
ATOM   1472 C  CB   . MET   A 1 210 ? 3.353   -13.517 -34.308 1.00 17.04  ? 417 MET   A CB   1 
ATOM   1473 C  CG   . MET   A 1 210 ? 2.962   -14.908 -34.790 1.00 17.27  ? 417 MET   A CG   1 
ATOM   1474 S  SD   . MET   A 1 210 ? 1.132   -15.029 -35.061 1.00 20.27  ? 417 MET   A SD   1 
ATOM   1475 C  CE   . MET   A 1 210 ? 1.009   -16.633 -35.858 1.00 24.47  ? 417 MET   A CE   1 
ATOM   1476 N  N    . LEU   A 1 211 ? 4.528   -10.583 -34.614 1.00 13.31  ? 418 LEU   A N    1 
ATOM   1477 C  CA   . LEU   A 1 211 ? 4.715   -9.199  -34.132 1.00 13.06  ? 418 LEU   A CA   1 
ATOM   1478 C  C    . LEU   A 1 211 ? 4.175   -8.224  -35.179 1.00 12.26  ? 418 LEU   A C    1 
ATOM   1479 O  O    . LEU   A 1 211 ? 3.685   -7.124  -34.736 1.00 16.45  ? 418 LEU   A O    1 
ATOM   1480 C  CB   . LEU   A 1 211 ? 6.206   -9.006  -33.843 1.00 13.44  ? 418 LEU   A CB   1 
ATOM   1481 C  CG   . LEU   A 1 211 ? 6.716   -9.784  -32.625 1.00 15.28  ? 418 LEU   A CG   1 
ATOM   1482 C  CD1  . LEU   A 1 211 ? 8.229   -9.638  -32.474 1.00 15.16  ? 418 LEU   A CD1  1 
ATOM   1483 C  CD2  . LEU   A 1 211 ? 5.999   -9.546  -31.301 1.00 14.46  ? 418 LEU   A CD2  1 
ATOM   1484 N  N    . MET   A 1 212 ? 4.328   -8.512  -36.457 1.00 12.06  ? 419 MET   A N    1 
ATOM   1485 C  CA   . MET   A 1 212 ? 3.918   -7.628  -37.571 1.00 15.13  ? 419 MET   A CA   1 
ATOM   1486 C  C    . MET   A 1 212 ? 2.400   -7.452  -37.658 1.00 12.34  ? 419 MET   A C    1 
ATOM   1487 O  O    . MET   A 1 212 ? 1.956   -6.600  -38.469 1.00 15.92  ? 419 MET   A O    1 
ATOM   1488 C  CB   . MET   A 1 212 ? 4.535   -8.098  -38.866 1.00 15.90  ? 419 MET   A CB   1 
ATOM   1489 C  CG   . MET   A 1 212 ? 6.012   -7.619  -38.950 1.00 16.46  ? 419 MET   A CG   1 
ATOM   1490 S  SD   . MET   A 1 212 ? 6.967   -8.324  -40.333 1.00 21.29  ? 419 MET   A SD   1 
ATOM   1491 C  CE   . MET   A 1 212 ? 6.189   -7.406  -41.654 1.00 21.91  ? 419 MET   A CE   1 
ATOM   1492 N  N    . THR   A 1 213 ? 1.656   -8.260  -36.906 1.00 14.29  ? 420 THR   A N    1 
ATOM   1493 C  CA   . THR   A 1 213 ? 0.194   -8.115  -36.827 1.00 14.98  ? 420 THR   A CA   1 
ATOM   1494 C  C    . THR   A 1 213 ? -0.246  -7.096  -35.799 1.00 15.67  ? 420 THR   A C    1 
ATOM   1495 O  O    . THR   A 1 213 ? -1.461  -6.717  -35.844 1.00 16.82  ? 420 THR   A O    1 
ATOM   1496 C  CB   . THR   A 1 213 ? -0.526  -9.440  -36.506 1.00 12.83  ? 420 THR   A CB   1 
ATOM   1497 O  OG1  . THR   A 1 213 ? -0.317  -9.872  -35.168 1.00 15.32  ? 420 THR   A OG1  1 
ATOM   1498 C  CG2  . THR   A 1 213 ? -0.189  -10.482 -37.540 1.00 14.99  ? 420 THR   A CG2  1 
ATOM   1499 N  N    . LEU   A 1 214 ? 0.651   -6.592  -34.953 1.00 13.51  ? 421 LEU   A N    1 
ATOM   1500 C  CA   . LEU   A 1 214 ? 0.300   -5.718  -33.809 1.00 12.31  ? 421 LEU   A CA   1 
ATOM   1501 C  C    . LEU   A 1 214 ? -0.054  -4.317  -34.334 1.00 13.26  ? 421 LEU   A C    1 
ATOM   1502 O  O    . LEU   A 1 214 ? -0.935  -3.693  -33.753 1.00 15.74  ? 421 LEU   A O    1 
ATOM   1503 C  CB   . LEU   A 1 214 ? 1.418   -5.715  -32.764 1.00 14.91  ? 421 LEU   A CB   1 
ATOM   1504 C  CG   . LEU   A 1 214 ? 1.594   -7.023  -31.984 1.00 15.54  ? 421 LEU   A CG   1 
ATOM   1505 C  CD1  . LEU   A 1 214 ? 2.820   -6.958  -31.103 1.00 16.62  ? 421 LEU   A CD1  1 
ATOM   1506 C  CD2  . LEU   A 1 214 ? 0.390   -7.305  -31.097 1.00 17.08  ? 421 LEU   A CD2  1 
ATOM   1507 N  N    . PRO   A 1 215 ? 0.477   -3.800  -35.457 1.00 13.99  ? 422 PRO   A N    1 
ATOM   1508 C  CA   . PRO   A 1 215 ? 0.077   -2.448  -35.908 1.00 13.43  ? 422 PRO   A CA   1 
ATOM   1509 C  C    . PRO   A 1 215 ? -1.407  -2.373  -36.249 1.00 14.04  ? 422 PRO   A C    1 
ATOM   1510 O  O    . PRO   A 1 215 ? -2.064  -1.400  -35.841 1.00 12.72  ? 422 PRO   A O    1 
ATOM   1511 C  CB   . PRO   A 1 215 ? 0.959   -2.196  -37.137 1.00 13.85  ? 422 PRO   A CB   1 
ATOM   1512 C  CG   . PRO   A 1 215 ? 2.245   -2.909  -36.721 1.00 14.52  ? 422 PRO   A CG   1 
ATOM   1513 C  CD   . PRO   A 1 215 ? 1.676   -4.231  -36.183 1.00 13.50  ? 422 PRO   A CD   1 
ATOM   1514 N  N    . LEU   A 1 216 ? -1.888  -3.406  -36.927 1.00 11.95  ? 423 LEU   A N    1 
ATOM   1515 C  CA   . LEU   A 1 216 ? -3.315  -3.467  -37.294 1.00 13.22  ? 423 LEU   A CA   1 
ATOM   1516 C  C    . LEU   A 1 216 ? -4.158  -3.568  -36.025 1.00 14.50  ? 423 LEU   A C    1 
ATOM   1517 O  O    . LEU   A 1 216 ? -5.254  -2.883  -36.000 1.00 15.60  ? 423 LEU   A O    1 
ATOM   1518 C  CB   . LEU   A 1 216 ? -3.625  -4.568  -38.303 1.00 15.90  ? 423 LEU   A CB   1 
ATOM   1519 C  CG   . LEU   A 1 216 ? -5.085  -4.556  -38.788 1.00 16.65  ? 423 LEU   A CG   1 
ATOM   1520 C  CD1  . LEU   A 1 216 ? -5.547  -3.217  -39.374 1.00 20.25  ? 423 LEU   A CD1  1 
ATOM   1521 C  CD2  . LEU   A 1 216 ? -5.269  -5.689  -39.797 1.00 22.34  ? 423 LEU   A CD2  1 
ATOM   1522 N  N    . LEU   A 1 217 ? -3.723  -4.277  -35.003 1.00 15.49  ? 424 LEU   A N    1 
ATOM   1523 C  CA   . LEU   A 1 217 ? -4.519  -4.369  -33.752 1.00 13.03  ? 424 LEU   A CA   1 
ATOM   1524 C  C    . LEU   A 1 217 ? -4.585  -2.982  -33.084 1.00 12.45  ? 424 LEU   A C    1 
ATOM   1525 O  O    . LEU   A 1 217 ? -5.595  -2.610  -32.538 1.00 15.02  ? 424 LEU   A O    1 
ATOM   1526 C  CB   . LEU   A 1 217 ? -3.874  -5.430  -32.874 1.00 15.43  ? 424 LEU   A CB   1 
ATOM   1527 C  CG   . LEU   A 1 217 ? -4.483  -5.606  -31.494 1.00 17.08  ? 424 LEU   A CG   1 
ATOM   1528 C  CD1  . LEU   A 1 217 ? -5.931  -6.087  -31.640 1.00 16.97  ? 424 LEU   A CD1  1 
ATOM   1529 C  CD2  . LEU   A 1 217 ? -3.638  -6.522  -30.623 1.00 20.71  ? 424 LEU   A CD2  1 
ATOM   1530 N  N    . ARG   A 1 218 ? -3.456  -2.276  -33.085 1.00 15.29  ? 425 ARG   A N    1 
ATOM   1531 C  CA   . ARG   A 1 218 ? -3.343  -0.917  -32.531 1.00 16.58  ? 425 ARG   A CA   1 
ATOM   1532 C  C    . ARG   A 1 218 ? -4.317  -0.000  -33.287 1.00 14.93  ? 425 ARG   A C    1 
ATOM   1533 O  O    . ARG   A 1 218 ? -5.009  0.748   -32.599 1.00 16.45  ? 425 ARG   A O    1 
ATOM   1534 C  CB   . ARG   A 1 218 ? -1.882  -0.450  -32.609 1.00 16.19  ? 425 ARG   A CB   1 
ATOM   1535 C  CG   . ARG   A 1 218 ? -1.639  0.975   -32.105 1.00 16.04  ? 425 ARG   A CG   1 
ATOM   1536 C  CD   . ARG   A 1 218 ? -1.800  1.169   -30.603 1.00 15.92  ? 425 ARG   A CD   1 
ATOM   1537 N  NE   . ARG   A 1 218 ? -0.922  0.352   -29.809 1.00 16.78  ? 425 ARG   A NE   1 
ATOM   1538 C  CZ   . ARG   A 1 218 ? 0.357   0.596   -29.524 1.00 16.25  ? 425 ARG   A CZ   1 
ATOM   1539 N  NH1  . ARG   A 1 218 ? 0.975   1.714   -29.883 1.00 19.68  ? 425 ARG   A NH1  1 
ATOM   1540 N  NH2  . ARG   A 1 218 ? 1.046   -0.326  -28.880 1.00 17.24  ? 425 ARG   A NH2  1 
ATOM   1541 N  N    . GLN   A 1 219 ? -4.269  -0.006  -34.603 1.00 14.46  ? 426 GLN   A N    1 
ATOM   1542 C  CA   . GLN   A 1 219 ? -5.060  0.869   -35.478 1.00 16.00  ? 426 GLN   A CA   1 
ATOM   1543 C  C    . GLN   A 1 219 ? -6.528  0.594   -35.128 1.00 17.35  ? 426 GLN   A C    1 
ATOM   1544 O  O    . GLN   A 1 219 ? -7.281  1.555   -34.923 1.00 18.71  ? 426 GLN   A O    1 
ATOM   1545 C  CB   . GLN   A 1 219 ? -4.749  0.571   -36.931 1.00 17.80  ? 426 GLN   A CB   1 
ATOM   1546 C  CG   . GLN   A 1 219 ? -5.450  1.436   -37.961 1.00 20.93  ? 426 GLN   A CG   1 
ATOM   1547 C  CD   . GLN   A 1 219 ? -5.375  0.725   -39.300 1.00 30.28  ? 426 GLN   A CD   1 
ATOM   1548 O  OE1  . GLN   A 1 219 ? -4.333  0.295   -39.752 1.00 23.00  ? 426 GLN   A OE1  1 
ATOM   1549 N  NE2  . GLN   A 1 219 ? -6.524  0.400   -39.889 1.00 39.64  ? 426 GLN   A NE2  1 
ATOM   1550 N  N    . THR   A 1 220 ? -6.901  -0.684  -35.087 1.00 19.08  ? 427 THR   A N    1 
ATOM   1551 C  CA   . THR   A 1 220 ? -8.318  -1.098  -34.946 1.00 17.24  ? 427 THR   A CA   1 
ATOM   1552 C  C    . THR   A 1 220 ? -8.801  -0.657  -33.557 1.00 16.59  ? 427 THR   A C    1 
ATOM   1553 O  O    . THR   A 1 220 ? -9.995  -0.167  -33.429 1.00 22.48  ? 427 THR   A O    1 
ATOM   1554 C  CB   . THR   A 1 220 ? -8.471  -2.581  -35.288 1.00 19.39  ? 427 THR   A CB   1 
ATOM   1555 O  OG1  . THR   A 1 220 ? -7.947  -2.866  -36.596 1.00 23.08  ? 427 THR   A OG1  1 
ATOM   1556 C  CG2  . THR   A 1 220 ? -9.927  -2.974  -35.249 1.00 22.60  ? 427 THR   A CG2  1 
ATOM   1557 N  N    . SER   A 1 221 ? -7.986  -0.859  -32.531 1.00 18.07  ? 428 SER   A N    1 
ATOM   1558 C  CA   . SER   A 1 221 ? -8.252  -0.521  -31.118 1.00 19.30  ? 428 SER   A CA   1 
ATOM   1559 C  C    . SER   A 1 221 ? -8.466  0.994   -31.009 1.00 17.75  ? 428 SER   A C    1 
ATOM   1560 O  O    . SER   A 1 221 ? -9.460  1.438   -30.355 1.00 21.14  ? 428 SER   A O    1 
ATOM   1561 C  CB   . SER   A 1 221 ? -7.140  -0.944  -30.226 1.00 29.13  ? 428 SER   A CB   1 
ATOM   1562 O  OG   . SER   A 1 221 ? -7.214  -0.228  -28.985 1.00 33.19  ? 428 SER   A OG   1 
ATOM   1563 N  N    . THR   A 1 222 ? -7.627  1.769   -31.669 1.00 20.62  ? 429 THR   A N    1 
ATOM   1564 C  CA   . THR   A 1 222 ? -7.734  3.246   -31.623 1.00 26.07  ? 429 THR   A CA   1 
ATOM   1565 C  C    . THR   A 1 222 ? -9.095  3.659   -32.170 1.00 23.09  ? 429 THR   A C    1 
ATOM   1566 O  O    . THR   A 1 222 ? -9.727  4.510   -31.544 1.00 26.99  ? 429 THR   A O    1 
ATOM   1567 C  CB   . THR   A 1 222 ? -6.581  3.956   -32.366 1.00 26.09  ? 429 THR   A CB   1 
ATOM   1568 O  OG1  . THR   A 1 222 ? -5.475  3.609   -31.538 1.00 28.38  ? 429 THR   A OG1  1 
ATOM   1569 C  CG2  . THR   A 1 222 ? -6.787  5.453   -32.504 1.00 32.72  ? 429 THR   A CG2  1 
ATOM   1570 N  N    . LYS   A 1 223 ? -9.483  3.104   -33.321 1.00 19.15  ? 430 LYS   A N    1 
ATOM   1571 C  CA   . LYS   A 1 223 ? -10.775 3.432   -33.997 1.00 25.41  ? 430 LYS   A CA   1 
ATOM   1572 C  C    . LYS   A 1 223 ? -11.939 3.026   -33.071 1.00 22.29  ? 430 LYS   A C    1 
ATOM   1573 O  O    . LYS   A 1 223 ? -12.865 3.860   -32.898 1.00 28.83  ? 430 LYS   A O    1 
ATOM   1574 C  CB   . LYS   A 1 223 ? -10.684 2.824   -35.404 1.00 30.93  ? 430 LYS   A CB   1 
ATOM   1575 C  CG   . LYS   A 1 223 ? -11.941 2.700   -36.230 1.00 44.01  ? 430 LYS   A CG   1 
ATOM   1576 C  CD   . LYS   A 1 223 ? -11.634 1.974   -37.533 1.00 61.50  ? 430 LYS   A CD   1 
ATOM   1577 C  CE   . LYS   A 1 223 ? -12.839 1.849   -38.446 1.00 60.50  ? 430 LYS   A CE   1 
ATOM   1578 N  NZ   . LYS   A 1 223 ? -13.183 3.144   -39.074 1.00 57.57  ? 430 LYS   A NZ   1 
ATOM   1579 N  N    . ALA   A 1 224 ? -11.876 1.847   -32.444 1.00 21.89  ? 431 ALA   A N    1 
ATOM   1580 C  CA   . ALA   A 1 224 ? -12.908 1.366   -31.494 1.00 19.91  ? 431 ALA   A CA   1 
ATOM   1581 C  C    . ALA   A 1 224 ? -13.065 2.346   -30.326 1.00 20.63  ? 431 ALA   A C    1 
ATOM   1582 O  O    . ALA   A 1 224 ? -14.212 2.781   -30.061 1.00 21.79  ? 431 ALA   A O    1 
ATOM   1583 C  CB   . ALA   A 1 224 ? -12.591 0.007   -30.955 1.00 22.04  ? 431 ALA   A CB   1 
ATOM   1584 N  N    . VAL   A 1 225 ? -11.957 2.733   -29.674 1.00 20.95  ? 432 VAL   A N    1 
ATOM   1585 C  CA   . VAL   A 1 225 ? -11.980 3.681   -28.523 1.00 19.95  ? 432 VAL   A CA   1 
ATOM   1586 C  C    . VAL   A 1 225 ? -12.643 4.980   -28.995 1.00 22.91  ? 432 VAL   A C    1 
ATOM   1587 O  O    . VAL   A 1 225 ? -13.610 5.439   -28.296 1.00 24.51  ? 432 VAL   A O    1 
ATOM   1588 C  CB   . VAL   A 1 225 ? -10.571 3.888   -27.940 1.00 20.31  ? 432 VAL   A CB   1 
ATOM   1589 C  CG1  . VAL   A 1 225 ? -10.538 5.022   -26.950 1.00 28.07  ? 432 VAL   A CG1  1 
ATOM   1590 C  CG2  . VAL   A 1 225 ? -10.095 2.629   -27.240 1.00 26.49  ? 432 VAL   A CG2  1 
ATOM   1591 N  N    . GLN   A 1 226 ? -12.242 5.501   -30.149 1.00 23.10  ? 433 GLN   A N    1 
ATOM   1592 C  CA   . GLN   A 1 226 ? -12.769 6.802   -30.653 1.00 24.33  ? 433 GLN   A CA   1 
ATOM   1593 C  C    . GLN   A 1 226 ? -14.275 6.681   -30.923 1.00 24.27  ? 433 GLN   A C    1 
ATOM   1594 O  O    . GLN   A 1 226 ? -15.023 7.557   -30.531 1.00 29.46  ? 433 GLN   A O    1 
ATOM   1595 C  CB   . GLN   A 1 226 ? -12.028 7.266   -31.894 1.00 31.95  ? 433 GLN   A CB   1 
ATOM   1596 C  CG   . GLN   A 1 226 ? -10.670 7.843   -31.533 1.00 42.43  ? 433 GLN   A CG   1 
ATOM   1597 C  CD   . GLN   A 1 226 ? -9.797  8.222   -32.712 1.00 50.42  ? 433 GLN   A CD   1 
ATOM   1598 O  OE1  . GLN   A 1 226 ? -10.009 7.809   -33.850 1.00 60.20  ? 433 GLN   A OE1  1 
ATOM   1599 N  NE2  . GLN   A 1 226 ? -8.781  9.002   -32.424 1.00 62.26  ? 433 GLN   A NE2  1 
ATOM   1600 N  N    . HIS   A 1 227 ? -14.694 5.578   -31.528 1.00 26.64  ? 434 HIS   A N    1 
ATOM   1601 C  CA   . HIS   A 1 227 ? -16.119 5.345   -31.868 1.00 29.30  ? 434 HIS   A CA   1 
ATOM   1602 C  C    . HIS   A 1 227 ? -16.965 5.300   -30.589 1.00 31.50  ? 434 HIS   A C    1 
ATOM   1603 O  O    . HIS   A 1 227 ? -17.999 6.020   -30.518 1.00 32.02  ? 434 HIS   A O    1 
ATOM   1604 C  CB   . HIS   A 1 227 ? -16.238 4.101   -32.738 1.00 27.79  ? 434 HIS   A CB   1 
ATOM   1605 C  CG   . HIS   A 1 227 ? -17.624 3.891   -33.210 1.00 29.04  ? 434 HIS   A CG   1 
ATOM   1606 N  ND1  . HIS   A 1 227 ? -18.059 4.458   -34.374 1.00 37.91  ? 434 HIS   A ND1  1 
ATOM   1607 C  CD2  . HIS   A 1 227 ? -18.667 3.228   -32.679 1.00 27.61  ? 434 HIS   A CD2  1 
ATOM   1608 C  CE1  . HIS   A 1 227 ? -19.331 4.170   -34.551 1.00 39.98  ? 434 HIS   A CE1  1 
ATOM   1609 N  NE2  . HIS   A 1 227 ? -19.729 3.418   -33.527 1.00 35.45  ? 434 HIS   A NE2  1 
ATOM   1610 N  N    . PHE   A 1 228 ? -16.513 4.553   -29.584 1.00 26.95  ? 435 PHE   A N    1 
ATOM   1611 C  CA   . PHE   A 1 228 ? -17.242 4.384   -28.307 1.00 24.80  ? 435 PHE   A CA   1 
ATOM   1612 C  C    . PHE   A 1 228 ? -17.159 5.662   -27.476 1.00 26.88  ? 435 PHE   A C    1 
ATOM   1613 O  O    . PHE   A 1 228 ? -18.150 5.970   -26.793 1.00 29.94  ? 435 PHE   A O    1 
ATOM   1614 C  CB   . PHE   A 1 228 ? -16.848 3.078   -27.608 1.00 23.98  ? 435 PHE   A CB   1 
ATOM   1615 C  CG   . PHE   A 1 228 ? -17.567 1.929   -28.270 1.00 21.03  ? 435 PHE   A CG   1 
ATOM   1616 C  CD1  . PHE   A 1 228 ? -18.869 1.648   -27.915 1.00 25.59  ? 435 PHE   A CD1  1 
ATOM   1617 C  CD2  . PHE   A 1 228 ? -17.017 1.184   -29.301 1.00 24.34  ? 435 PHE   A CD2  1 
ATOM   1618 C  CE1  . PHE   A 1 228 ? -19.608 0.676   -28.557 1.00 27.76  ? 435 PHE   A CE1  1 
ATOM   1619 C  CE2  . PHE   A 1 228 ? -17.759 0.176   -29.932 1.00 22.19  ? 435 PHE   A CE2  1 
ATOM   1620 C  CZ   . PHE   A 1 228 ? -19.059 -0.058  -29.561 1.00 22.98  ? 435 PHE   A CZ   1 
ATOM   1621 N  N    . TYR   A 1 229 ? -16.057 6.399   -27.536 1.00 29.50  ? 436 TYR   A N    1 
ATOM   1622 C  CA   . TYR   A 1 229 ? -15.993 7.713   -26.853 1.00 32.44  ? 436 TYR   A CA   1 
ATOM   1623 C  C    . TYR   A 1 229 ? -17.063 8.649   -27.425 1.00 33.48  ? 436 TYR   A C    1 
ATOM   1624 O  O    . TYR   A 1 229 ? -17.726 9.366   -26.645 1.00 31.80  ? 436 TYR   A O    1 
ATOM   1625 C  CB   . TYR   A 1 229 ? -14.613 8.358   -26.999 1.00 31.68  ? 436 TYR   A CB   1 
ATOM   1626 C  CG   . TYR   A 1 229 ? -14.457 9.511   -26.055 1.00 31.73  ? 436 TYR   A CG   1 
ATOM   1627 C  CD1  . TYR   A 1 229 ? -14.271 9.299   -24.699 1.00 37.59  ? 436 TYR   A CD1  1 
ATOM   1628 C  CD2  . TYR   A 1 229 ? -14.570 10.815  -26.508 1.00 38.51  ? 436 TYR   A CD2  1 
ATOM   1629 C  CE1  . TYR   A 1 229 ? -14.189 10.362  -23.819 1.00 49.11  ? 436 TYR   A CE1  1 
ATOM   1630 C  CE2  . TYR   A 1 229 ? -14.452 11.894  -25.644 1.00 38.95  ? 436 TYR   A CE2  1 
ATOM   1631 C  CZ   . TYR   A 1 229 ? -14.279 11.660  -24.293 1.00 49.55  ? 436 TYR   A CZ   1 
ATOM   1632 O  OH   . TYR   A 1 229 ? -14.183 12.692  -23.407 1.00 58.91  ? 436 TYR   A OH   1 
ATOM   1633 N  N    . ASN   A 1 230 ? -17.207 8.675   -28.752 1.00 28.96  ? 437 ASN   A N    1 
ATOM   1634 C  CA   . ASN   A 1 230 ? -18.255 9.491   -29.439 1.00 31.71  ? 437 ASN   A CA   1 
ATOM   1635 C  C    . ASN   A 1 230 ? -19.661 9.044   -29.019 1.00 31.84  ? 437 ASN   A C    1 
ATOM   1636 O  O    . ASN   A 1 230 ? -20.497 9.892   -28.832 1.00 34.12  ? 437 ASN   A O    1 
ATOM   1637 C  CB   . ASN   A 1 230 ? -18.161 9.429   -30.959 1.00 34.08  ? 437 ASN   A CB   1 
ATOM   1638 C  CG   . ASN   A 1 230 ? -16.920 10.108  -31.480 1.00 44.65  ? 437 ASN   A CG   1 
ATOM   1639 O  OD1  . ASN   A 1 230 ? -16.329 10.948  -30.784 1.00 47.54  ? 437 ASN   A OD1  1 
ATOM   1640 N  ND2  . ASN   A 1 230 ? -16.506 9.725   -32.688 1.00 51.58  ? 437 ASN   A ND2  1 
ATOM   1641 N  N    . ILE   A 1 231 ? -19.900 7.748   -28.840 1.00 30.52  ? 438 ILE   A N    1 
ATOM   1642 C  CA   . ILE   A 1 231 ? -21.226 7.250   -28.390 1.00 27.48  ? 438 ILE   A CA   1 
ATOM   1643 C  C    . ILE   A 1 231 ? -21.441 7.756   -26.953 1.00 31.29  ? 438 ILE   A C    1 
ATOM   1644 O  O    . ILE   A 1 231 ? -22.565 8.202   -26.651 1.00 33.82  ? 438 ILE   A O    1 
ATOM   1645 C  CB   . ILE   A 1 231 ? -21.344 5.716   -28.581 1.00 33.11  ? 438 ILE   A CB   1 
ATOM   1646 C  CG1  . ILE   A 1 231 ? -21.319 5.403   -30.086 1.00 39.23  ? 438 ILE   A CG1  1 
ATOM   1647 C  CG2  . ILE   A 1 231 ? -22.591 5.187   -27.898 1.00 38.28  ? 438 ILE   A CG2  1 
ATOM   1648 C  CD1  . ILE   A 1 231 ? -21.034 3.990   -30.459 1.00 44.88  ? 438 ILE   A CD1  1 
ATOM   1649 N  N    . LYS   A 1 232 ? -20.405 7.709   -26.109 1.00 29.58  ? 439 LYS   A N    1 
ATOM   1650 C  CA   . LYS   A 1 232 ? -20.447 8.228   -24.718 1.00 34.36  ? 439 LYS   A CA   1 
ATOM   1651 C  C    . LYS   A 1 232 ? -20.917 9.683   -24.764 1.00 32.87  ? 439 LYS   A C    1 
ATOM   1652 O  O    . LYS   A 1 232 ? -21.907 9.979   -24.091 1.00 41.94  ? 439 LYS   A O    1 
ATOM   1653 C  CB   . LYS   A 1 232 ? -19.082 8.115   -24.030 1.00 31.21  ? 439 LYS   A CB   1 
ATOM   1654 C  CG   . LYS   A 1 232 ? -19.019 8.735   -22.638 1.00 36.40  ? 439 LYS   A CG   1 
ATOM   1655 C  CD   . LYS   A 1 232 ? -17.649 9.230   -22.282 1.00 46.22  ? 439 LYS   A CD   1 
ATOM   1656 C  CE   . LYS   A 1 232 ? -17.739 10.548  -21.549 1.00 52.35  ? 439 LYS   A CE   1 
ATOM   1657 N  NZ   . LYS   A 1 232 ? -16.411 11.177  -21.380 1.00 69.15  ? 439 LYS   A NZ   1 
ATOM   1658 N  N    . LEU   A 1 233 ? -20.290 10.505  -25.610 1.00 37.19  ? 440 LEU   A N    1 
ATOM   1659 C  CA   . LEU   A 1 233 ? -20.590 11.956  -25.768 1.00 36.25  ? 440 LEU   A CA   1 
ATOM   1660 C  C    . LEU   A 1 233 ? -22.054 12.127  -26.166 1.00 34.41  ? 440 LEU   A C    1 
ATOM   1661 O  O    . LEU   A 1 233 ? -22.648 13.074  -25.691 1.00 44.36  ? 440 LEU   A O    1 
ATOM   1662 C  CB   . LEU   A 1 233 ? -19.675 12.593  -26.816 1.00 45.72  ? 440 LEU   A CB   1 
ATOM   1663 C  CG   . LEU   A 1 233 ? -18.226 12.756  -26.354 1.00 46.36  ? 440 LEU   A CG   1 
ATOM   1664 C  CD1  . LEU   A 1 233 ? -17.412 13.604  -27.338 1.00 52.99  ? 440 LEU   A CD1  1 
ATOM   1665 C  CD2  . LEU   A 1 233 ? -18.180 13.394  -24.961 1.00 57.42  ? 440 LEU   A CD2  1 
ATOM   1666 N  N    . GLU   A 1 234 ? -22.572 11.299  -27.065 1.00 36.36  ? 441 GLU   A N    1 
ATOM   1667 C  CA   . GLU   A 1 234 ? -23.947 11.449  -27.596 1.00 44.58  ? 441 GLU   A CA   1 
ATOM   1668 C  C    . GLU   A 1 234 ? -24.995 11.094  -26.535 1.00 48.52  ? 441 GLU   A C    1 
ATOM   1669 O  O    . GLU   A 1 234 ? -26.149 11.493  -26.751 1.00 59.20  ? 441 GLU   A O    1 
ATOM   1670 C  CB   . GLU   A 1 234 ? -24.183 10.568  -28.808 1.00 46.88  ? 441 GLU   A CB   1 
ATOM   1671 C  CG   . GLU   A 1 234 ? -23.613 11.158  -30.060 1.00 62.60  ? 441 GLU   A CG   1 
ATOM   1672 C  CD   . GLU   A 1 234 ? -23.358 10.109  -31.122 1.00 81.09  ? 441 GLU   A CD   1 
ATOM   1673 O  OE1  . GLU   A 1 234 ? -23.662 8.911   -30.864 1.00 82.26  ? 441 GLU   A OE1  1 
ATOM   1674 O  OE2  . GLU   A 1 234 ? -22.850 10.488  -32.200 1.00 88.83  ? 441 GLU   A OE2  1 
ATOM   1675 N  N    . GLY   A 1 235 ? -24.615 10.405  -25.453 1.00 42.44  ? 442 GLY   A N    1 
ATOM   1676 C  CA   . GLY   A 1 235 ? -25.415 10.254  -24.218 1.00 39.08  ? 442 GLY   A CA   1 
ATOM   1677 C  C    . GLY   A 1 235 ? -26.608 9.307   -24.379 1.00 37.65  ? 442 GLY   A C    1 
ATOM   1678 O  O    . GLY   A 1 235 ? -27.395 9.246   -23.439 1.00 42.50  ? 442 GLY   A O    1 
ATOM   1679 N  N    . LYS   A 1 236 ? -26.718 8.518   -25.465 1.00 39.62  ? 443 LYS   A N    1 
ATOM   1680 C  CA   . LYS   A 1 236 ? -27.945 7.707   -25.760 1.00 41.31  ? 443 LYS   A CA   1 
ATOM   1681 C  C    . LYS   A 1 236 ? -27.774 6.259   -25.300 1.00 42.48  ? 443 LYS   A C    1 
ATOM   1682 O  O    . LYS   A 1 236 ? -28.745 5.492   -25.291 1.00 40.51  ? 443 LYS   A O    1 
ATOM   1683 C  CB   . LYS   A 1 236 ? -28.281 7.745   -27.254 1.00 42.75  ? 443 LYS   A CB   1 
ATOM   1684 C  CG   . LYS   A 1 236 ? -28.780 9.098   -27.741 1.00 48.82  ? 443 LYS   A CG   1 
ATOM   1685 C  CD   . LYS   A 1 236 ? -29.345 9.087   -29.144 1.00 52.26  ? 443 LYS   A CD   1 
ATOM   1686 C  CE   . LYS   A 1 236 ? -30.239 10.275  -29.412 1.00 54.41  ? 443 LYS   A CE   1 
ATOM   1687 N  NZ   . LYS   A 1 236 ? -29.937 10.875  -30.731 1.00 72.90  ? 443 LYS   A NZ   1 
ATOM   1688 N  N    . VAL   A 1 237 ? -26.557 5.875   -24.941 1.00 38.07  ? 444 VAL   A N    1 
ATOM   1689 C  CA   . VAL   A 1 237 ? -26.241 4.484   -24.551 1.00 29.73  ? 444 VAL   A CA   1 
ATOM   1690 C  C    . VAL   A 1 237 ? -25.710 4.497   -23.121 1.00 33.46  ? 444 VAL   A C    1 
ATOM   1691 O  O    . VAL   A 1 237 ? -24.675 5.085   -22.804 1.00 33.66  ? 444 VAL   A O    1 
ATOM   1692 C  CB   . VAL   A 1 237 ? -25.228 3.872   -25.531 1.00 30.91  ? 444 VAL   A CB   1 
ATOM   1693 C  CG1  . VAL   A 1 237 ? -24.819 2.466   -25.127 1.00 29.17  ? 444 VAL   A CG1  1 
ATOM   1694 C  CG2  . VAL   A 1 237 ? -25.747 3.888   -26.966 1.00 31.07  ? 444 VAL   A CG2  1 
ATOM   1695 N  N    . PRO   A 1 238 ? -26.391 3.814   -22.191 1.00 31.39  ? 445 PRO   A N    1 
ATOM   1696 C  CA   . PRO   A 1 238 ? -25.898 3.718   -20.825 1.00 35.23  ? 445 PRO   A CA   1 
ATOM   1697 C  C    . PRO   A 1 238 ? -24.646 2.839   -20.829 1.00 35.68  ? 445 PRO   A C    1 
ATOM   1698 O  O    . PRO   A 1 238 ? -24.571 1.912   -21.613 1.00 38.74  ? 445 PRO   A O    1 
ATOM   1699 C  CB   . PRO   A 1 238 ? -27.059 3.123   -20.031 1.00 41.96  ? 445 PRO   A CB   1 
ATOM   1700 C  CG   . PRO   A 1 238 ? -27.888 2.399   -21.079 1.00 46.25  ? 445 PRO   A CG   1 
ATOM   1701 C  CD   . PRO   A 1 238 ? -27.696 3.168   -22.371 1.00 33.69  ? 445 PRO   A CD   1 
ATOM   1702 N  N    . MET   A 1 239 ? -23.701 3.198   -19.970 1.00 32.49  ? 446 MET   A N    1 
ATOM   1703 C  CA   . MET   A 1 239 ? -22.376 2.572   -19.877 1.00 27.12  ? 446 MET   A CA   1 
ATOM   1704 C  C    . MET   A 1 239 ? -22.032 2.431   -18.393 1.00 34.46  ? 446 MET   A C    1 
ATOM   1705 O  O    . MET   A 1 239 ? -22.345 3.367   -17.603 1.00 34.95  ? 446 MET   A O    1 
ATOM   1706 C  CB   . MET   A 1 239 ? -21.343 3.445   -20.581 1.00 28.41  ? 446 MET   A CB   1 
ATOM   1707 C  CG   . MET   A 1 239 ? -21.507 3.501   -22.097 1.00 31.18  ? 446 MET   A CG   1 
ATOM   1708 S  SD   . MET   A 1 239 ? -20.254 4.569   -22.855 1.00 30.79  ? 446 MET   A SD   1 
ATOM   1709 C  CE   . MET   A 1 239 ? -20.697 4.422   -24.589 1.00 28.55  ? 446 MET   A CE   1 
ATOM   1710 N  N    . HIS   A 1 240 ? -21.442 1.306   -18.004 1.00 32.35  ? 447 HIS   A N    1 
ATOM   1711 C  CA   . HIS   A 1 240 ? -21.073 1.070   -16.588 1.00 30.45  ? 447 HIS   A CA   1 
ATOM   1712 C  C    . HIS   A 1 240 ? -19.766 1.792   -16.252 1.00 28.08  ? 447 HIS   A C    1 
ATOM   1713 O  O    . HIS   A 1 240 ? -19.083 2.250   -17.167 1.00 31.88  ? 447 HIS   A O    1 
ATOM   1714 C  CB   . HIS   A 1 240 ? -21.033 -0.427  -16.283 1.00 37.49  ? 447 HIS   A CB   1 
ATOM   1715 C  CG   . HIS   A 1 240 ? -22.404 -1.009  -16.266 1.00 50.49  ? 447 HIS   A CG   1 
ATOM   1716 N  ND1  . HIS   A 1 240 ? -23.140 -1.183  -15.084 1.00 47.44  ? 447 HIS   A ND1  1 
ATOM   1717 C  CD2  . HIS   A 1 240 ? -23.202 -1.419  -17.278 1.00 52.63  ? 447 HIS   A CD2  1 
ATOM   1718 C  CE1  . HIS   A 1 240 ? -24.324 -1.665  -15.384 1.00 59.21  ? 447 HIS   A CE1  1 
ATOM   1719 N  NE2  . HIS   A 1 240 ? -24.381 -1.827  -16.718 1.00 60.00  ? 447 HIS   A NE2  1 
ATOM   1720 N  N    . LYS   A 1 241 ? -19.453 1.806   -14.958 1.00 35.17  ? 448 LYS   A N    1 
ATOM   1721 C  CA   . LYS   A 1 241 ? -18.402 2.610   -14.275 1.00 38.59  ? 448 LYS   A CA   1 
ATOM   1722 C  C    . LYS   A 1 241 ? -17.044 2.219   -14.867 1.00 35.51  ? 448 LYS   A C    1 
ATOM   1723 O  O    . LYS   A 1 241 ? -16.312 3.118   -15.331 1.00 29.74  ? 448 LYS   A O    1 
ATOM   1724 C  CB   . LYS   A 1 241 ? -18.453 2.328   -12.769 1.00 40.93  ? 448 LYS   A CB   1 
ATOM   1725 C  CG   . LYS   A 1 241 ? -19.837 2.339   -12.119 1.00 64.17  ? 448 LYS   A CG   1 
ATOM   1726 C  CD   . LYS   A 1 241 ? -20.805 1.204   -12.571 1.00 72.99  ? 448 LYS   A CD   1 
ATOM   1727 C  CE   . LYS   A 1 241 ? -21.768 0.716   -11.514 1.00 74.30  ? 448 LYS   A CE   1 
ATOM   1728 N  NZ   . LYS   A 1 241 ? -22.623 1.807   -10.969 1.00 89.17  ? 448 LYS   A NZ   1 
ATOM   1729 N  N    . LEU   A 1 242 ? -16.717 0.925   -14.893 1.00 33.98  ? 449 LEU   A N    1 
ATOM   1730 C  CA   . LEU   A 1 242 ? -15.349 0.503   -15.329 1.00 28.94  ? 449 LEU   A CA   1 
ATOM   1731 C  C    . LEU   A 1 242 ? -15.129 0.823   -16.799 1.00 28.17  ? 449 LEU   A C    1 
ATOM   1732 O  O    . LEU   A 1 242 ? -14.057 1.338   -17.141 1.00 29.97  ? 449 LEU   A O    1 
ATOM   1733 C  CB   . LEU   A 1 242 ? -15.123 -0.984  -15.069 1.00 31.25  ? 449 LEU   A CB   1 
ATOM   1734 C  CG   . LEU   A 1 242 ? -13.702 -1.476  -15.322 1.00 29.23  ? 449 LEU   A CG   1 
ATOM   1735 C  CD1  . LEU   A 1 242 ? -12.687 -0.631  -14.568 1.00 30.89  ? 449 LEU   A CD1  1 
ATOM   1736 C  CD2  . LEU   A 1 242 ? -13.570 -2.947  -14.969 1.00 34.08  ? 449 LEU   A CD2  1 
ATOM   1737 N  N    . PHE   A 1 243 ? -16.106 0.532   -17.641 1.00 31.57  ? 450 PHE   A N    1 
ATOM   1738 C  CA   . PHE   A 1 243 ? -16.002 0.795   -19.093 1.00 28.29  ? 450 PHE   A CA   1 
ATOM   1739 C  C    . PHE   A 1 243 ? -15.770 2.289   -19.326 1.00 28.00  ? 450 PHE   A C    1 
ATOM   1740 O  O    . PHE   A 1 243 ? -14.878 2.694   -20.128 1.00 27.42  ? 450 PHE   A O    1 
ATOM   1741 C  CB   . PHE   A 1 243 ? -17.235 0.299   -19.813 1.00 27.28  ? 450 PHE   A CB   1 
ATOM   1742 C  CG   . PHE   A 1 243 ? -17.168 0.480   -21.302 1.00 25.70  ? 450 PHE   A CG   1 
ATOM   1743 C  CD1  . PHE   A 1 243 ? -16.473 -0.427  -22.084 1.00 26.33  ? 450 PHE   A CD1  1 
ATOM   1744 C  CD2  . PHE   A 1 243 ? -17.874 1.490   -21.932 1.00 27.95  ? 450 PHE   A CD2  1 
ATOM   1745 C  CE1  . PHE   A 1 243 ? -16.402 -0.277  -23.460 1.00 23.82  ? 450 PHE   A CE1  1 
ATOM   1746 C  CE2  . PHE   A 1 243 ? -17.843 1.602   -23.313 1.00 27.46  ? 450 PHE   A CE2  1 
ATOM   1747 C  CZ   . PHE   A 1 243 ? -17.078 0.749   -24.075 1.00 24.47  ? 450 PHE   A CZ   1 
ATOM   1748 N  N    . LEU   A 1 244 ? -16.576 3.090   -18.639 1.00 29.73  ? 451 LEU   A N    1 
ATOM   1749 C  CA   . LEU   A 1 244 ? -16.485 4.562   -18.700 1.00 30.81  ? 451 LEU   A CA   1 
ATOM   1750 C  C    . LEU   A 1 244 ? -15.104 5.033   -18.275 1.00 28.28  ? 451 LEU   A C    1 
ATOM   1751 O  O    . LEU   A 1 244 ? -14.613 5.915   -18.944 1.00 27.24  ? 451 LEU   A O    1 
ATOM   1752 C  CB   . LEU   A 1 244 ? -17.577 5.206   -17.852 1.00 33.20  ? 451 LEU   A CB   1 
ATOM   1753 C  CG   . LEU   A 1 244 ? -18.877 5.314   -18.630 1.00 38.87  ? 451 LEU   A CG   1 
ATOM   1754 C  CD1  . LEU   A 1 244 ? -20.056 5.625   -17.716 1.00 51.61  ? 451 LEU   A CD1  1 
ATOM   1755 C  CD2  . LEU   A 1 244 ? -18.709 6.330   -19.763 1.00 38.74  ? 451 LEU   A CD2  1 
ATOM   1756 N  N    . GLU   A 1 245 ? -14.529 4.439   -17.221 1.00 28.41  ? 452 GLU   A N    1 
ATOM   1757 C  CA   . GLU   A 1 245 ? -13.244 4.878   -16.632 1.00 32.01  ? 452 GLU   A CA   1 
ATOM   1758 C  C    . GLU   A 1 245 ? -12.137 4.628   -17.666 1.00 31.74  ? 452 GLU   A C    1 
ATOM   1759 O  O    . GLU   A 1 245 ? -11.294 5.536   -17.850 1.00 36.04  ? 452 GLU   A O    1 
ATOM   1760 C  CB   . GLU   A 1 245 ? -13.011 4.180   -15.294 1.00 38.36  ? 452 GLU   A CB   1 
ATOM   1761 C  CG   . GLU   A 1 245 ? -11.772 4.673   -14.579 1.00 43.34  ? 452 GLU   A CG   1 
ATOM   1762 C  CD   . GLU   A 1 245 ? -11.566 3.945   -13.270 1.00 52.13  ? 452 GLU   A CD   1 
ATOM   1763 O  OE1  . GLU   A 1 245 ? -12.581 3.809   -12.519 1.00 56.06  ? 452 GLU   A OE1  1 
ATOM   1764 O  OE2  . GLU   A 1 245 ? -10.425 3.472   -13.033 1.00 63.88  ? 452 GLU   A OE2  1 
ATOM   1765 N  N    . MET   A 1 246 ? -12.186 3.483   -18.361 1.00 24.37  ? 453 MET   A N    1 
ATOM   1766 C  CA   . MET   A 1 246 ? -11.155 3.162   -19.372 1.00 26.43  ? 453 MET   A CA   1 
ATOM   1767 C  C    . MET   A 1 246 ? -11.414 4.012   -20.625 1.00 24.32  ? 453 MET   A C    1 
ATOM   1768 O  O    . MET   A 1 246 ? -10.417 4.411   -21.245 1.00 27.94  ? 453 MET   A O    1 
ATOM   1769 C  CB   . MET   A 1 246 ? -11.092 1.676   -19.740 1.00 24.47  ? 453 MET   A CB   1 
ATOM   1770 C  CG   . MET   A 1 246 ? -11.147 0.781   -18.523 1.00 25.43  ? 453 MET   A CG   1 
ATOM   1771 S  SD   . MET   A 1 246 ? -9.695  0.996   -17.487 1.00 31.25  ? 453 MET   A SD   1 
ATOM   1772 C  CE   . MET   A 1 246 ? -8.539  0.187   -18.577 1.00 29.93  ? 453 MET   A CE   1 
ATOM   1773 N  N    . LEU   A 1 247 ? -12.676 4.325   -20.969 1.00 27.46  ? 454 LEU   A N    1 
ATOM   1774 C  CA   . LEU   A 1 247 ? -12.922 5.238   -22.119 1.00 25.21  ? 454 LEU   A CA   1 
ATOM   1775 C  C    . LEU   A 1 247 ? -12.372 6.617   -21.802 1.00 25.93  ? 454 LEU   A C    1 
ATOM   1776 O  O    . LEU   A 1 247 ? -11.885 7.267   -22.738 1.00 36.89  ? 454 LEU   A O    1 
ATOM   1777 C  CB   . LEU   A 1 247 ? -14.402 5.394   -22.450 1.00 31.34  ? 454 LEU   A CB   1 
ATOM   1778 C  CG   . LEU   A 1 247 ? -14.961 4.478   -23.512 1.00 28.27  ? 454 LEU   A CG   1 
ATOM   1779 C  CD1  . LEU   A 1 247 ? -16.419 4.826   -23.728 1.00 33.57  ? 454 LEU   A CD1  1 
ATOM   1780 C  CD2  . LEU   A 1 247 ? -14.197 4.527   -24.820 1.00 32.22  ? 454 LEU   A CD2  1 
ATOM   1781 N  N    . GLU   A 1 248 ? -12.470 7.064   -20.555 1.00 32.90  ? 455 GLU   A N    1 
ATOM   1782 C  CA   . GLU   A 1 248 ? -12.056 8.448   -20.183 1.00 34.64  ? 455 GLU   A CA   1 
ATOM   1783 C  C    . GLU   A 1 248 ? -10.542 8.507   -19.914 1.00 37.87  ? 455 GLU   A C    1 
ATOM   1784 O  O    . GLU   A 1 248 ? -10.074 9.597   -19.667 1.00 43.87  ? 455 GLU   A O    1 
ATOM   1785 C  CB   . GLU   A 1 248 ? -12.903 8.928   -19.006 1.00 41.58  ? 455 GLU   A CB   1 
ATOM   1786 C  CG   . GLU   A 1 248 ? -14.304 9.423   -19.427 1.00 50.89  ? 455 GLU   A CG   1 
ATOM   1787 C  CD   . GLU   A 1 248 ? -15.421 9.400   -18.385 1.00 56.59  ? 455 GLU   A CD   1 
ATOM   1788 O  OE1  . GLU   A 1 248 ? -15.120 9.424   -17.171 1.00 71.86  ? 455 GLU   A OE1  1 
ATOM   1789 O  OE2  . GLU   A 1 248 ? -16.600 9.360   -18.788 1.00 70.11  ? 455 GLU   A OE2  1 
ATOM   1790 N  N    . ALA   A 1 249 ? -9.773  7.413   -19.984 1.00 35.76  ? 456 ALA   A N    1 
ATOM   1791 C  CA   . ALA   A 1 249 ? -8.312  7.478   -19.699 1.00 34.75  ? 456 ALA   A CA   1 
ATOM   1792 C  C    . ALA   A 1 249 ? -7.590  8.330   -20.767 1.00 45.41  ? 456 ALA   A C    1 
ATOM   1793 O  O    . ALA   A 1 249 ? -8.011  8.318   -21.932 1.00 45.39  ? 456 ALA   A O    1 
ATOM   1794 C  CB   . ALA   A 1 249 ? -7.734  6.083   -19.563 1.00 36.75  ? 456 ALA   A CB   1 
ATOM   1795 N  N    . LYS   A 1 250 ? -6.512  9.031   -20.383 1.00 59.32  ? 457 LYS   A N    1 
ATOM   1796 C  CA   . LYS   A 1 250 ? -5.888  10.140  -21.171 1.00 54.13  ? 457 LYS   A CA   1 
ATOM   1797 C  C    . LYS   A 1 250 ? -4.831  9.592   -22.138 1.00 54.19  ? 457 LYS   A C    1 
ATOM   1798 O  O    . LYS   A 1 250 ? -3.987  8.842   -21.658 1.00 55.15  ? 457 LYS   A O    1 
ATOM   1799 C  CB   . LYS   A 1 250 ? -5.379  11.222  -20.205 1.00 77.65  ? 457 LYS   A CB   1 
ATOM   1800 C  CG   . LYS   A 1 250 ? -6.516  12.013  -19.554 1.00 77.34  ? 457 LYS   A CG   1 
ATOM   1801 C  CD   . LYS   A 1 250 ? -6.171  12.924  -18.401 1.00 80.03  ? 457 LYS   A CD   1 
ATOM   1802 C  CE   . LYS   A 1 250 ? -7.425  13.507  -17.776 1.00 83.66  ? 457 LYS   A CE   1 
ATOM   1803 N  NZ   . LYS   A 1 250 ? -7.127  14.682  -16.928 1.00 84.34  ? 457 LYS   A NZ   1 
ATOM   1804 N  N    . ASN   B 2 1   ? -7.356  7.516   -7.933  1.00 62.89  ? 376 ASN   C N    1 
ATOM   1805 C  CA   . ASN   B 2 1   ? -7.727  8.040   -6.575  1.00 67.43  ? 376 ASN   C CA   1 
ATOM   1806 C  C    . ASN   B 2 1   ? -8.806  7.130   -5.987  1.00 49.77  ? 376 ASN   C C    1 
ATOM   1807 O  O    . ASN   B 2 1   ? -8.436  6.148   -5.335  1.00 64.73  ? 376 ASN   C O    1 
ATOM   1808 C  CB   . ASN   B 2 1   ? -8.197  9.501   -6.606  1.00 75.50  ? 376 ASN   C CB   1 
ATOM   1809 C  CG   . ASN   B 2 1   ? -7.150  10.475  -6.116  1.00 67.16  ? 376 ASN   C CG   1 
ATOM   1810 O  OD1  . ASN   B 2 1   ? -5.957  10.173  -6.129  1.00 84.32  ? 376 ASN   C OD1  1 
ATOM   1811 N  ND2  . ASN   B 2 1   ? -7.596  11.641  -5.673  1.00 65.10  ? 376 ASN   C ND2  1 
ATOM   1812 N  N    . ASN   B 2 2   ? -10.081 7.442   -6.257  1.00 64.84  ? 377 ASN   C N    1 
ATOM   1813 C  CA   . ASN   B 2 2   ? -11.266 6.576   -5.986  1.00 65.82  ? 377 ASN   C CA   1 
ATOM   1814 C  C    . ASN   B 2 2   ? -11.555 5.724   -7.228  1.00 53.11  ? 377 ASN   C C    1 
ATOM   1815 O  O    . ASN   B 2 2   ? -12.742 5.487   -7.513  1.00 73.82  ? 377 ASN   C O    1 
ATOM   1816 C  CB   . ASN   B 2 2   ? -12.505 7.412   -5.639  1.00 78.65  ? 377 ASN   C CB   1 
ATOM   1817 C  CG   . ASN   B 2 2   ? -13.503 6.717   -4.734  1.00 87.87  ? 377 ASN   C CG   1 
ATOM   1818 O  OD1  . ASN   B 2 2   ? -13.375 5.522   -4.448  1.00 102.14 ? 377 ASN   C OD1  1 
ATOM   1819 N  ND2  . ASN   B 2 2   ? -14.505 7.467   -4.282  1.00 94.09  ? 377 ASN   C ND2  1 
ATOM   1820 N  N    . SER   B 2 3   ? -10.518 5.295   -7.950  1.00 56.13  ? 378 SER   C N    1 
ATOM   1821 C  CA   . SER   B 2 3   ? -10.639 4.656   -9.286  1.00 47.07  ? 378 SER   C CA   1 
ATOM   1822 C  C    . SER   B 2 3   ? -11.051 3.181   -9.113  1.00 38.87  ? 378 SER   C C    1 
ATOM   1823 O  O    . SER   B 2 3   ? -10.558 2.509   -8.197  1.00 42.38  ? 378 SER   C O    1 
ATOM   1824 C  CB   . SER   B 2 3   ? -9.363  4.900   -10.081 1.00 47.80  ? 378 SER   C CB   1 
ATOM   1825 O  OG   . SER   B 2 3   ? -8.753  3.706   -10.502 1.00 41.56  ? 378 SER   C OG   1 
ATOM   1826 N  N    . LEU   B 2 4   ? -11.999 2.707   -9.916  1.00 35.71  ? 379 LEU   C N    1 
ATOM   1827 C  CA   . LEU   B 2 4   ? -12.429 1.282   -9.886  1.00 42.97  ? 379 LEU   C CA   1 
ATOM   1828 C  C    . LEU   B 2 4   ? -11.279 0.411   -10.410 1.00 37.33  ? 379 LEU   C C    1 
ATOM   1829 O  O    . LEU   B 2 4   ? -11.049 -0.702  -9.858  1.00 36.53  ? 379 LEU   C O    1 
ATOM   1830 C  CB   . LEU   B 2 4   ? -13.708 1.119   -10.715 1.00 47.16  ? 379 LEU   C CB   1 
ATOM   1831 C  CG   . LEU   B 2 4   ? -14.441 -0.234  -10.644 1.00 54.23  ? 379 LEU   C CG   1 
ATOM   1832 C  CD1  . LEU   B 2 4   ? -14.465 -0.844  -9.243  1.00 52.27  ? 379 LEU   C CD1  1 
ATOM   1833 C  CD2  . LEU   B 2 4   ? -15.868 -0.087  -11.163 1.00 54.31  ? 379 LEU   C CD2  1 
ATOM   1834 N  N    . LEU   B 2 5   ? -10.550 0.889   -11.421 1.00 31.19  ? 380 LEU   C N    1 
ATOM   1835 C  CA   . LEU   B 2 5   ? -9.364  0.173   -11.963 1.00 32.69  ? 380 LEU   C CA   1 
ATOM   1836 C  C    . LEU   B 2 5   ? -8.383  -0.069  -10.805 1.00 31.36  ? 380 LEU   C C    1 
ATOM   1837 O  O    . LEU   B 2 5   ? -7.941  -1.194  -10.614 1.00 32.70  ? 380 LEU   C O    1 
ATOM   1838 C  CB   . LEU   B 2 5   ? -8.700  0.994   -13.076 1.00 32.03  ? 380 LEU   C CB   1 
ATOM   1839 C  CG   . LEU   B 2 5   ? -7.403  0.403   -13.647 1.00 26.29  ? 380 LEU   C CG   1 
ATOM   1840 C  CD1  . LEU   B 2 5   ? -7.583  -1.065  -14.027 1.00 32.66  ? 380 LEU   C CD1  1 
ATOM   1841 C  CD2  . LEU   B 2 5   ? -6.946  1.206   -14.860 1.00 28.99  ? 380 LEU   C CD2  1 
ATOM   1842 N  N    . LEU   B 2 6   ? -8.043  0.968   -10.058 1.00 32.75  ? 381 LEU   C N    1 
ATOM   1843 C  CA   . LEU   B 2 6   ? -7.085  0.845   -8.925  1.00 36.71  ? 381 LEU   C CA   1 
ATOM   1844 C  C    . LEU   B 2 6   ? -7.618  -0.180  -7.915  1.00 37.82  ? 381 LEU   C C    1 
ATOM   1845 O  O    . LEU   B 2 6   ? -6.868  -1.139  -7.554  1.00 44.83  ? 381 LEU   C O    1 
ATOM   1846 C  CB   . LEU   B 2 6   ? -6.889  2.209   -8.259  1.00 39.27  ? 381 LEU   C CB   1 
ATOM   1847 C  CG   . LEU   B 2 6   ? -5.966  2.180   -7.044  1.00 36.72  ? 381 LEU   C CG   1 
ATOM   1848 C  CD1  . LEU   B 2 6   ? -4.561  1.714   -7.442  1.00 41.98  ? 381 LEU   C CD1  1 
ATOM   1849 C  CD2  . LEU   B 2 6   ? -5.945  3.534   -6.361  1.00 46.29  ? 381 LEU   C CD2  1 
ATOM   1850 N  N    . HIS   B 2 7   ? -8.861  0.002   -7.478  1.00 37.42  ? 382 HIS   C N    1 
ATOM   1851 C  CA   . HIS   B 2 7   ? -9.506  -0.847  -6.450  1.00 36.94  ? 382 HIS   C CA   1 
ATOM   1852 C  C    . HIS   B 2 7   ? -9.421  -2.310  -6.899  1.00 35.36  ? 382 HIS   C C    1 
ATOM   1853 O  O    . HIS   B 2 7   ? -9.050  -3.176  -6.083  1.00 33.08  ? 382 HIS   C O    1 
ATOM   1854 C  CB   . HIS   B 2 7   ? -10.933 -0.360  -6.208  1.00 37.87  ? 382 HIS   C CB   1 
ATOM   1855 C  CG   . HIS   B 2 7   ? -11.700 -1.231  -5.281  1.00 47.36  ? 382 HIS   C CG   1 
ATOM   1856 N  ND1  . HIS   B 2 7   ? -11.445 -1.268  -3.928  1.00 47.85  ? 382 HIS   C ND1  1 
ATOM   1857 C  CD2  . HIS   B 2 7   ? -12.716 -2.097  -5.507  1.00 62.70  ? 382 HIS   C CD2  1 
ATOM   1858 C  CE1  . HIS   B 2 7   ? -12.274 -2.129  -3.352  1.00 57.78  ? 382 HIS   C CE1  1 
ATOM   1859 N  NE2  . HIS   B 2 7   ? -13.069 -2.651  -4.302  1.00 58.03  ? 382 HIS   C NE2  1 
ATOM   1860 N  N    . LEU   B 2 8   ? -9.672  -2.578  -8.169  1.00 35.17  ? 383 LEU   C N    1 
ATOM   1861 C  CA   . LEU   B 2 8   ? -9.650  -3.973  -8.674  1.00 32.60  ? 383 LEU   C CA   1 
ATOM   1862 C  C    . LEU   B 2 8   ? -8.206  -4.483  -8.707  1.00 32.11  ? 383 LEU   C C    1 
ATOM   1863 O  O    . LEU   B 2 8   ? -8.016  -5.677  -8.388  1.00 37.95  ? 383 LEU   C O    1 
ATOM   1864 C  CB   . LEU   B 2 8   ? -10.326 -4.057  -10.042 1.00 30.99  ? 383 LEU   C CB   1 
ATOM   1865 C  CG   . LEU   B 2 8   ? -11.834 -3.829  -10.030 1.00 34.13  ? 383 LEU   C CG   1 
ATOM   1866 C  CD1  . LEU   B 2 8   ? -12.330 -3.595  -11.450 1.00 36.57  ? 383 LEU   C CD1  1 
ATOM   1867 C  CD2  . LEU   B 2 8   ? -12.562 -5.007  -9.391  1.00 38.51  ? 383 LEU   C CD2  1 
ATOM   1868 N  N    . LEU   B 2 9   ? -7.234  -3.630  -9.036  1.00 30.44  ? 384 LEU   C N    1 
ATOM   1869 C  CA   . LEU   B 2 9   ? -5.798  -4.020  -9.060  1.00 30.84  ? 384 LEU   C CA   1 
ATOM   1870 C  C    . LEU   B 2 9   ? -5.310  -4.326  -7.652  1.00 29.35  ? 384 LEU   C C    1 
ATOM   1871 O  O    . LEU   B 2 9   ? -4.408  -5.158  -7.539  1.00 34.53  ? 384 LEU   C O    1 
ATOM   1872 C  CB   . LEU   B 2 9   ? -4.959  -2.917  -9.697  1.00 29.57  ? 384 LEU   C CB   1 
ATOM   1873 C  CG   . LEU   B 2 9   ? -4.969  -2.924  -11.219 1.00 29.37  ? 384 LEU   C CG   1 
ATOM   1874 C  CD1  . LEU   B 2 9   ? -4.274  -1.699  -11.778 1.00 31.26  ? 384 LEU   C CD1  1 
ATOM   1875 C  CD2  . LEU   B 2 9   ? -4.361  -4.211  -11.752 1.00 25.50  ? 384 LEU   C CD2  1 
ATOM   1876 N  N    . LYS   B 2 10  ? -5.863  -3.672  -6.633  1.00 37.77  ? 385 LYS   C N    1 
ATOM   1877 C  CA   . LYS   B 2 10  ? -5.383  -3.784  -5.236  1.00 39.34  ? 385 LYS   C CA   1 
ATOM   1878 C  C    . LYS   B 2 10  ? -5.971  -5.017  -4.579  1.00 44.51  ? 385 LYS   C C    1 
ATOM   1879 O  O    . LYS   B 2 10  ? -5.346  -5.483  -3.650  1.00 58.72  ? 385 LYS   C O    1 
ATOM   1880 C  CB   . LYS   B 2 10  ? -5.709  -2.520  -4.443  1.00 43.49  ? 385 LYS   C CB   1 
ATOM   1881 C  CG   . LYS   B 2 10  ? -4.735  -1.377  -4.691  1.00 44.43  ? 385 LYS   C CG   1 
ATOM   1882 C  CD   . LYS   B 2 10  ? -5.255  -0.024  -4.249  1.00 48.19  ? 385 LYS   C CD   1 
ATOM   1883 C  CE   . LYS   B 2 10  ? -4.764  0.433   -2.894  1.00 54.28  ? 385 LYS   C CE   1 
ATOM   1884 N  NZ   . LYS   B 2 10  ? -5.346  1.750   -2.544  1.00 64.91  ? 385 LYS   C NZ   1 
ATOM   1885 N  N    . SER   B 2 11  ? -7.099  -5.534  -5.070  1.00 47.99  ? 386 SER   C N    1 
ATOM   1886 C  CA   . SER   B 2 11  ? -7.928  -6.528  -4.339  1.00 57.27  ? 386 SER   C CA   1 
ATOM   1887 C  C    . SER   B 2 11  ? -7.523  -7.941  -4.769  1.00 62.24  ? 386 SER   C C    1 
ATOM   1888 O  O    . SER   B 2 11  ? -6.890  -8.061  -5.823  1.00 72.52  ? 386 SER   C O    1 
ATOM   1889 C  CB   . SER   B 2 11  ? -9.372  -6.264  -4.564  1.00 64.35  ? 386 SER   C CB   1 
ATOM   1890 O  OG   . SER   B 2 11  ? -9.621  -6.158  -5.949  1.00 71.38  ? 386 SER   C OG   1 
ATOM   1891 N  N    . GLN   B 2 12  ? -7.838  -8.952  -3.952  1.00 76.44  ? 387 GLN   C N    1 
ATOM   1892 C  CA   . GLN   B 2 12  ? -7.428  -10.377 -4.139  1.00 78.27  ? 387 GLN   C CA   1 
ATOM   1893 C  C    . GLN   B 2 12  ? -6.095  -10.470 -4.895  1.00 80.79  ? 387 GLN   C C    1 
ATOM   1894 O  O    . GLN   B 2 12  ? -5.094  -9.853  -4.534  1.00 93.86  ? 387 GLN   C O    1 
ATOM   1895 C  CB   . GLN   B 2 12  ? -8.492  -11.147 -4.912  1.00 76.38  ? 387 GLN   C CB   1 
ATOM   1896 C  CG   . GLN   B 2 12  ? -9.838  -11.165 -4.207  1.00 80.84  ? 387 GLN   C CG   1 
ATOM   1897 C  CD   . GLN   B 2 12  ? -10.978 -11.395 -5.166  1.00 79.08  ? 387 GLN   C CD   1 
ATOM   1898 O  OE1  . GLN   B 2 12  ? -10.779 -11.769 -6.323  1.00 82.88  ? 387 GLN   C OE1  1 
ATOM   1899 N  NE2  . GLN   B 2 12  ? -12.192 -11.175 -4.680  1.00 91.16  ? 387 GLN   C NE2  1 
HETATM 1900 CL CLAJ . A1EGB C 3 .   ? -16.272 -2.398  -28.722 1.00 82.72  ? 501 A1EGB A CLAJ 1 
HETATM 1901 C  CAE  . A1EGB C 3 .   ? -16.068 -3.829  -28.141 1.00 42.44  ? 501 A1EGB A CAE  1 
HETATM 1902 C  CAD  . A1EGB C 3 .   ? -16.915 -4.432  -27.200 1.00 42.07  ? 501 A1EGB A CAD  1 
HETATM 1903 C  CAB  . A1EGB C 3 .   ? -16.657 -5.698  -26.809 1.00 40.25  ? 501 A1EGB A CAB  1 
HETATM 1904 C  CAA  . A1EGB C 3 .   ? -17.211 -6.509  -25.911 1.00 43.66  ? 501 A1EGB A CAA  1 
HETATM 1905 N  NAH  . A1EGB C 3 .   ? -16.533 -7.670  -25.875 1.00 45.26  ? 501 A1EGB A NAH  1 
HETATM 1906 N  NAI  . A1EGB C 3 .   ? -15.529 -7.581  -26.727 1.00 51.98  ? 501 A1EGB A NAI  1 
HETATM 1907 C  CAC  . A1EGB C 3 .   ? -15.593 -6.374  -27.301 1.00 43.55  ? 501 A1EGB A CAC  1 
HETATM 1908 C  CAG  . A1EGB C 3 .   ? -14.765 -5.805  -28.203 1.00 44.82  ? 501 A1EGB A CAG  1 
HETATM 1909 C  CAF  . A1EGB C 3 .   ? -15.005 -4.508  -28.665 1.00 36.05  ? 501 A1EGB A CAF  1 
HETATM 1910 O  O    . HOH   D 4 .   ? 1.655   0.800   -22.212 1.00 32.49  ? 601 HOH   A O    1 
HETATM 1911 O  O    . HOH   D 4 .   ? 10.375  -18.131 -22.358 1.00 37.22  ? 602 HOH   A O    1 
HETATM 1912 O  O    . HOH   D 4 .   ? -9.935  -10.683 -24.636 1.00 33.21  ? 603 HOH   A O    1 
HETATM 1913 O  O    . HOH   D 4 .   ? -30.496 -13.079 -24.126 1.00 35.72  ? 604 HOH   A O    1 
HETATM 1914 O  O    . HOH   D 4 .   ? -28.677 -6.470  -29.485 1.00 27.62  ? 605 HOH   A O    1 
HETATM 1915 O  O    . HOH   D 4 .   ? -35.676 -5.033  -19.457 1.00 37.73  ? 606 HOH   A O    1 
HETATM 1916 O  O    . HOH   D 4 .   ? -8.417  -0.360  -38.399 1.00 44.93  ? 607 HOH   A O    1 
HETATM 1917 O  O    . HOH   D 4 .   ? 9.887   -20.212 -36.086 1.00 23.27  ? 608 HOH   A O    1 
HETATM 1918 O  O    . HOH   D 4 .   ? -3.781  0.829   -27.868 1.00 27.10  ? 609 HOH   A O    1 
HETATM 1919 O  O    . HOH   D 4 .   ? -10.202 -11.715 -21.253 1.00 34.30  ? 610 HOH   A O    1 
HETATM 1920 O  O    . HOH   D 4 .   ? -13.260 -9.941  -26.108 1.00 31.72  ? 611 HOH   A O    1 
HETATM 1921 O  O    . HOH   D 4 .   ? -20.954 -12.412 -17.104 1.00 36.34  ? 612 HOH   A O    1 
HETATM 1922 O  O    . HOH   D 4 .   ? 2.502   4.923   -14.719 1.00 31.13  ? 613 HOH   A O    1 
HETATM 1923 O  O    . HOH   D 4 .   ? 15.221  -18.099 -25.424 1.00 43.50  ? 614 HOH   A O    1 
HETATM 1924 O  O    . HOH   D 4 .   ? -22.521 2.889   -33.527 1.00 32.50  ? 615 HOH   A O    1 
HETATM 1925 O  O    . HOH   D 4 .   ? 4.283   -19.289 -40.582 1.00 20.39  ? 616 HOH   A O    1 
HETATM 1926 O  O    . HOH   D 4 .   ? 2.471   -10.442 -40.288 1.00 19.53  ? 617 HOH   A O    1 
HETATM 1927 O  O    . HOH   D 4 .   ? -6.562  -21.729 -22.295 1.00 43.52  ? 618 HOH   A O    1 
HETATM 1928 O  O    . HOH   D 4 .   ? -6.442  -0.236  -26.031 1.00 25.99  ? 619 HOH   A O    1 
HETATM 1929 O  O    . HOH   D 4 .   ? -1.726  5.173   -20.702 1.00 33.12  ? 620 HOH   A O    1 
HETATM 1930 O  O    . HOH   D 4 .   ? -15.024 -14.457 -38.889 1.00 22.87  ? 621 HOH   A O    1 
HETATM 1931 O  O    . HOH   D 4 .   ? 6.067   -0.053  -26.039 1.00 24.25  ? 622 HOH   A O    1 
HETATM 1932 O  O    . HOH   D 4 .   ? -14.366 -14.986 -17.407 1.00 29.56  ? 623 HOH   A O    1 
HETATM 1933 O  O    . HOH   D 4 .   ? -0.487  -3.430  -30.900 1.00 16.97  ? 624 HOH   A O    1 
HETATM 1934 O  O    . HOH   D 4 .   ? 1.320   -26.224 -34.737 1.00 38.83  ? 625 HOH   A O    1 
HETATM 1935 O  O    . HOH   D 4 .   ? 4.097   -21.937 -41.272 1.00 24.54  ? 626 HOH   A O    1 
HETATM 1936 O  O    . HOH   D 4 .   ? 5.705   3.829   -23.398 1.00 26.66  ? 627 HOH   A O    1 
HETATM 1937 O  O    . HOH   D 4 .   ? -34.343 -0.934  -28.249 1.00 29.85  ? 628 HOH   A O    1 
HETATM 1938 O  O    . HOH   D 4 .   ? 4.198   -0.304  -22.881 1.00 39.74  ? 629 HOH   A O    1 
HETATM 1939 O  O    . HOH   D 4 .   ? -0.210  -2.656  -27.569 1.00 20.36  ? 630 HOH   A O    1 
HETATM 1940 O  O    . HOH   D 4 .   ? -19.403 -16.548 -24.745 1.00 31.48  ? 631 HOH   A O    1 
HETATM 1941 O  O    . HOH   D 4 .   ? -24.083 7.195   -24.324 1.00 31.30  ? 632 HOH   A O    1 
HETATM 1942 O  O    . HOH   D 4 .   ? -11.043 -19.871 -32.530 1.00 34.14  ? 633 HOH   A O    1 
HETATM 1943 O  O    . HOH   D 4 .   ? -7.685  -15.486 -44.602 1.00 31.48  ? 634 HOH   A O    1 
HETATM 1944 O  O    . HOH   D 4 .   ? -21.936 -11.029 -42.397 1.00 42.20  ? 635 HOH   A O    1 
HETATM 1945 O  O    . HOH   D 4 .   ? -13.739 -19.594 -34.033 1.00 28.81  ? 636 HOH   A O    1 
HETATM 1946 O  O    . HOH   D 4 .   ? 2.203   -10.515 -12.106 1.00 26.32  ? 637 HOH   A O    1 
HETATM 1947 O  O    . HOH   D 4 .   ? -17.344 -12.912 -24.786 1.00 30.21  ? 638 HOH   A O    1 
HETATM 1948 O  O    . HOH   D 4 .   ? -0.364  -5.241  -38.691 1.00 18.22  ? 639 HOH   A O    1 
HETATM 1949 O  O    . HOH   D 4 .   ? -19.027 -6.710  -42.783 1.00 43.25  ? 640 HOH   A O    1 
HETATM 1950 O  O    . HOH   D 4 .   ? -1.037  -23.302 -37.022 1.00 23.17  ? 641 HOH   A O    1 
HETATM 1951 O  O    . HOH   D 4 .   ? -12.694 -6.879  -43.680 1.00 33.72  ? 642 HOH   A O    1 
HETATM 1952 O  O    . HOH   D 4 .   ? 8.867   -1.191  -11.664 1.00 38.68  ? 643 HOH   A O    1 
HETATM 1953 O  O    . HOH   D 4 .   ? -15.834 -19.215 -31.026 1.00 30.47  ? 644 HOH   A O    1 
HETATM 1954 O  O    . HOH   D 4 .   ? -12.970 -0.709  -42.171 1.00 32.27  ? 645 HOH   A O    1 
HETATM 1955 O  O    . HOH   D 4 .   ? 1.617   -22.294 -14.531 1.00 25.70  ? 646 HOH   A O    1 
HETATM 1956 O  O    . HOH   D 4 .   ? -4.069  -15.864 -21.407 1.00 23.03  ? 647 HOH   A O    1 
HETATM 1957 O  O    . HOH   D 4 .   ? -16.876 -9.910  -14.971 1.00 29.23  ? 648 HOH   A O    1 
HETATM 1958 O  O    . HOH   D 4 .   ? 11.020  -15.426 -21.248 1.00 32.16  ? 649 HOH   A O    1 
HETATM 1959 O  O    . HOH   D 4 .   ? 7.574   2.990   -10.660 1.00 41.78  ? 650 HOH   A O    1 
HETATM 1960 O  O    . HOH   D 4 .   ? 6.879   0.259   -11.946 1.00 30.54  ? 651 HOH   A O    1 
HETATM 1961 O  O    . HOH   D 4 .   ? 6.275   4.116   -25.954 1.00 34.35  ? 652 HOH   A O    1 
HETATM 1962 O  O    . HOH   D 4 .   ? -0.684  7.131   -22.628 1.00 33.49  ? 653 HOH   A O    1 
HETATM 1963 O  O    . HOH   D 4 .   ? -9.379  -13.251 -14.676 1.00 38.61  ? 654 HOH   A O    1 
HETATM 1964 O  O    . HOH   D 4 .   ? -29.222 -6.041  -24.104 1.00 26.42  ? 655 HOH   A O    1 
HETATM 1965 O  O    . HOH   D 4 .   ? -7.342  -11.874 -21.245 1.00 35.52  ? 656 HOH   A O    1 
HETATM 1966 O  O    . HOH   D 4 .   ? 1.118   -8.208  -41.061 1.00 19.65  ? 657 HOH   A O    1 
HETATM 1967 O  O    . HOH   D 4 .   ? -12.404 -11.985 -42.264 1.00 29.68  ? 658 HOH   A O    1 
HETATM 1968 O  O    . HOH   D 4 .   ? 11.109  -6.983  -26.631 1.00 27.67  ? 659 HOH   A O    1 
HETATM 1969 O  O    . HOH   D 4 .   ? -30.066 0.780   -23.313 1.00 32.20  ? 660 HOH   A O    1 
HETATM 1970 O  O    . HOH   D 4 .   ? -32.302 -10.277 -27.237 1.00 30.74  ? 661 HOH   A O    1 
HETATM 1971 O  O    . HOH   D 4 .   ? -19.390 2.236   -39.506 1.00 52.72  ? 662 HOH   A O    1 
HETATM 1972 O  O    . HOH   D 4 .   ? -4.689  -23.704 -31.073 1.00 37.74  ? 663 HOH   A O    1 
HETATM 1973 O  O    . HOH   D 4 .   ? -27.234 -4.981  -34.715 1.00 39.13  ? 664 HOH   A O    1 
HETATM 1974 O  O    . HOH   D 4 .   ? 9.857   -13.750 -43.981 1.00 47.51  ? 665 HOH   A O    1 
HETATM 1975 O  O    . HOH   D 4 .   ? -2.885  -7.770  -38.111 1.00 26.01  ? 666 HOH   A O    1 
HETATM 1976 O  O    . HOH   D 4 .   ? -19.507 -18.286 -40.149 1.00 31.43  ? 667 HOH   A O    1 
HETATM 1977 O  O    . HOH   D 4 .   ? -6.267  -21.025 -36.773 1.00 36.24  ? 668 HOH   A O    1 
HETATM 1978 O  O    . HOH   D 4 .   ? 8.483   -27.339 -35.989 1.00 40.46  ? 669 HOH   A O    1 
HETATM 1979 O  O    . HOH   D 4 .   ? -4.266  -10.180 -37.692 1.00 28.31  ? 670 HOH   A O    1 
HETATM 1980 O  O    . HOH   D 4 .   ? -21.339 -0.563  -20.178 1.00 34.27  ? 671 HOH   A O    1 
HETATM 1981 O  O    . HOH   D 4 .   ? -25.083 7.443   -27.799 1.00 42.82  ? 672 HOH   A O    1 
HETATM 1982 O  O    . HOH   D 4 .   ? 10.894  -14.449 -36.069 1.00 24.12  ? 673 HOH   A O    1 
HETATM 1983 O  O    . HOH   D 4 .   ? -1.210  -24.910 -19.977 1.00 32.21  ? 674 HOH   A O    1 
HETATM 1984 O  O    . HOH   D 4 .   ? 7.499   -25.451 -21.542 1.00 45.73  ? 675 HOH   A O    1 
HETATM 1985 O  O    . HOH   D 4 .   ? -31.987 1.081   -34.464 1.00 37.75  ? 676 HOH   A O    1 
HETATM 1986 O  O    . HOH   D 4 .   ? -11.379 -15.236 -26.242 1.00 38.65  ? 677 HOH   A O    1 
HETATM 1987 O  O    . HOH   D 4 .   ? -6.516  -21.711 -33.080 1.00 29.15  ? 678 HOH   A O    1 
HETATM 1988 O  O    . HOH   D 4 .   ? -14.209 -13.945 -41.332 1.00 30.46  ? 679 HOH   A O    1 
HETATM 1989 O  O    . HOH   D 4 .   ? -9.603  -13.455 -24.671 1.00 31.14  ? 680 HOH   A O    1 
HETATM 1990 O  O    . HOH   D 4 .   ? -7.076  3.614   -24.521 1.00 38.05  ? 681 HOH   A O    1 
HETATM 1991 O  O    . HOH   D 4 .   ? 1.875   -3.865  -29.313 1.00 18.55  ? 682 HOH   A O    1 
HETATM 1992 O  O    . HOH   D 4 .   ? 10.152  -17.532 -35.394 1.00 17.73  ? 683 HOH   A O    1 
HETATM 1993 O  O    . HOH   D 4 .   ? -19.606 -8.806  -39.046 1.00 36.88  ? 684 HOH   A O    1 
HETATM 1994 O  O    . HOH   D 4 .   ? 13.628  2.822   -15.845 1.00 42.36  ? 685 HOH   A O    1 
HETATM 1995 O  O    . HOH   D 4 .   ? -25.997 -14.280 -31.935 1.00 38.60  ? 686 HOH   A O    1 
HETATM 1996 O  O    . HOH   D 4 .   ? 4.968   -4.717  -35.966 1.00 40.00  ? 687 HOH   A O    1 
HETATM 1997 O  O    . HOH   D 4 .   ? -30.230 -4.996  -31.410 1.00 32.37  ? 688 HOH   A O    1 
HETATM 1998 O  O    . HOH   D 4 .   ? -11.257 -2.771  -43.116 1.00 38.18  ? 689 HOH   A O    1 
HETATM 1999 O  O    . HOH   D 4 .   ? 2.620   0.741   -6.245  1.00 39.06  ? 690 HOH   A O    1 
HETATM 2000 O  O    . HOH   D 4 .   ? -17.864 1.756   -37.258 1.00 37.40  ? 691 HOH   A O    1 
HETATM 2001 O  O    . HOH   D 4 .   ? 10.334  -22.229 -20.492 1.00 40.09  ? 692 HOH   A O    1 
HETATM 2002 O  O    . HOH   D 4 .   ? -25.239 -9.881  -43.065 1.00 50.75  ? 693 HOH   A O    1 
HETATM 2003 O  O    . HOH   D 4 .   ? 1.900   3.189   -7.755  1.00 35.72  ? 694 HOH   A O    1 
HETATM 2004 O  O    . HOH   D 4 .   ? -22.376 1.207   -39.780 1.00 38.12  ? 695 HOH   A O    1 
HETATM 2005 O  O    . HOH   D 4 .   ? -16.253 -15.318 -24.069 1.00 32.27  ? 696 HOH   A O    1 
HETATM 2006 O  O    . HOH   D 4 .   ? -18.340 -1.250  -13.373 1.00 45.61  ? 697 HOH   A O    1 
HETATM 2007 O  O    . HOH   D 4 .   ? -19.397 -7.025  -40.481 1.00 39.66  ? 698 HOH   A O    1 
HETATM 2008 O  O    . HOH   D 4 .   ? -15.025 -0.333  -43.821 1.00 46.44  ? 699 HOH   A O    1 
HETATM 2009 O  O    . HOH   D 4 .   ? -9.612  -21.623 -21.167 1.00 44.60  ? 700 HOH   A O    1 
HETATM 2010 O  O    . HOH   D 4 .   ? 2.109   -17.770 -41.569 1.00 37.27  ? 701 HOH   A O    1 
HETATM 2011 O  O    . HOH   D 4 .   ? -0.384  -27.100 -30.071 1.00 50.60  ? 702 HOH   A O    1 
HETATM 2012 O  O    . HOH   D 4 .   ? -23.354 6.783   -19.789 1.00 39.59  ? 703 HOH   A O    1 
HETATM 2013 O  O    . HOH   D 4 .   ? 1.779   -23.987 -16.540 1.00 37.55  ? 704 HOH   A O    1 
HETATM 2014 O  O    . HOH   D 4 .   ? 1.353   -22.245 -41.265 1.00 27.23  ? 705 HOH   A O    1 
HETATM 2015 O  O    . HOH   D 4 .   ? -31.200 -1.041  -24.783 1.00 32.59  ? 706 HOH   A O    1 
HETATM 2016 O  O    . HOH   D 4 .   ? 0.399   -9.470  -43.273 1.00 28.96  ? 707 HOH   A O    1 
HETATM 2017 O  O    . HOH   D 4 .   ? -10.554 -8.413  -44.697 1.00 52.06  ? 708 HOH   A O    1 
HETATM 2018 O  O    . HOH   D 4 .   ? -26.081 5.617   -30.974 1.00 35.76  ? 709 HOH   A O    1 
HETATM 2019 O  O    . HOH   D 4 .   ? -33.137 0.052   -26.071 1.00 38.18  ? 710 HOH   A O    1 
HETATM 2020 O  O    . HOH   D 4 .   ? -6.533  3.697   -26.708 1.00 48.03  ? 711 HOH   A O    1 
HETATM 2021 O  O    . HOH   D 4 .   ? 0.617   -23.863 -39.055 1.00 24.69  ? 712 HOH   A O    1 
HETATM 2022 O  O    . HOH   D 4 .   ? -10.959 -17.415 -26.886 1.00 50.36  ? 713 HOH   A O    1 
HETATM 2023 O  O    . HOH   D 4 .   ? -18.224 -8.074  -13.612 1.00 38.92  ? 714 HOH   A O    1 
HETATM 2024 O  O    . HOH   D 4 .   ? 11.461  -15.545 -18.259 1.00 36.22  ? 715 HOH   A O    1 
HETATM 2025 O  O    . HOH   D 4 .   ? -18.112 -12.248 -16.248 1.00 38.54  ? 716 HOH   A O    1 
HETATM 2026 O  O    . HOH   D 4 .   ? -30.113 0.099   -20.698 1.00 40.46  ? 717 HOH   A O    1 
HETATM 2027 O  O    . HOH   D 4 .   ? -30.903 -3.710  -23.633 1.00 29.97  ? 718 HOH   A O    1 
HETATM 2028 O  O    . HOH   D 4 .   ? 2.261   -15.404 -42.883 1.00 43.74  ? 719 HOH   A O    1 
HETATM 2029 O  O    . HOH   D 4 .   ? 4.322   -10.346 -42.471 1.00 27.74  ? 720 HOH   A O    1 
HETATM 2030 O  O    . HOH   D 4 .   ? -16.566 -14.040 -15.888 1.00 40.38  ? 721 HOH   A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N    . PRO   A 26  ? 1.2104 1.6499 1.5182 -0.1472 0.1670  -0.1338 233 PRO   A N    
2    C  CA   . PRO   A 26  ? 0.9238 1.4549 1.4058 0.1183  0.0334  0.0157  233 PRO   A CA   
3    C  C    . PRO   A 26  ? 1.5548 1.3505 1.3145 -0.1549 -0.0637 -0.0125 233 PRO   A C    
4    O  O    . PRO   A 26  ? 1.4279 1.2344 1.6784 -0.2404 -0.0449 -0.7364 233 PRO   A O    
5    C  CB   . PRO   A 26  ? 1.4248 1.3025 1.1956 0.4310  -0.1357 -0.1281 233 PRO   A CB   
6    C  CG   . PRO   A 26  ? 0.9322 1.1299 1.2481 0.7955  -0.0236 -0.1545 233 PRO   A CG   
7    C  CD   . PRO   A 26  ? 0.8489 1.6507 1.4483 0.3598  0.0244  -0.2215 233 PRO   A CD   
8    N  N    . TYR   A 27  ? 1.2129 1.4820 1.0547 0.0257  -0.2544 -0.2403 234 TYR   A N    
9    C  CA   . TYR   A 27  ? 0.4942 1.1430 1.1007 0.4080  -0.4362 -0.2356 234 TYR   A CA   
10   C  C    . TYR   A 27  ? 1.0493 0.8698 0.7576 0.3514  0.0308  -0.3339 234 TYR   A C    
11   O  O    . TYR   A 27  ? 0.4703 1.0479 1.2343 0.4882  0.0994  0.2116  234 TYR   A O    
12   C  CB   . TYR   A 27  ? 0.4749 1.6713 0.9774 0.2537  -0.3945 0.1152  234 TYR   A CB   
13   C  CG   . TYR   A 27  ? 0.6242 1.7483 1.1821 0.1346  -0.1058 0.0098  234 TYR   A CG   
14   C  CD1  . TYR   A 27  ? 0.5626 0.7052 0.9071 -0.5176 -0.2402 0.1157  234 TYR   A CD1  
15   C  CD2  . TYR   A 27  ? 0.5027 1.2969 1.4009 -0.2156 0.5774  0.1752  234 TYR   A CD2  
16   C  CE1  . TYR   A 27  ? 0.6705 0.9574 1.1568 -0.3806 0.0038  0.1995  234 TYR   A CE1  
17   C  CE2  . TYR   A 27  ? 0.5492 1.2517 1.7787 -0.3780 0.5464  0.3451  234 TYR   A CE2  
18   C  CZ   . TYR   A 27  ? 1.0164 0.7003 1.3471 -0.5373 0.1124  0.3454  234 TYR   A CZ   
19   O  OH   . TYR   A 27  ? 0.7152 0.2195 1.8449 0.1588  0.1726  0.0101  234 TYR   A OH   
20   N  N    . ASN   A 28  ? 0.2071 0.9713 0.9203 0.1607  0.2774  -0.0041 235 ASN   A N    
21   C  CA   . ASN   A 28  ? 0.4659 0.6800 0.6515 0.2386  -0.0483 0.2300  235 ASN   A CA   
22   C  C    . ASN   A 28  ? 0.6397 0.3239 0.6008 0.2303  -0.0152 0.0796  235 ASN   A C    
23   O  O    . ASN   A 28  ? 0.5688 0.9524 0.8456 0.5668  -0.0142 0.2146  235 ASN   A O    
24   C  CB   . ASN   A 28  ? 0.5536 0.6307 0.7776 0.1114  -0.0060 0.2071  235 ASN   A CB   
25   C  CG   . ASN   A 28  ? 0.9287 0.2546 0.8973 0.0137  0.0366  0.3596  235 ASN   A CG   
26   O  OD1  . ASN   A 28  ? 0.9219 0.7468 0.8257 0.1646  0.1083  0.3654  235 ASN   A OD1  
27   N  ND2  . ASN   A 28  ? 0.5984 1.0311 0.9315 0.5420  0.2168  0.2133  235 ASN   A ND2  
28   N  N    . LYS   A 29  ? 0.1028 0.3820 0.6112 0.1234  0.0504  0.0691  236 LYS   A N    
29   C  CA   . LYS   A 29  ? 0.0521 0.1988 0.5580 -0.0006 0.0289  0.1488  236 LYS   A CA   
30   C  C    . LYS   A 29  ? 0.1001 0.2392 0.4861 0.0398  0.1099  0.1730  236 LYS   A C    
31   O  O    . LYS   A 29  ? 0.0123 0.1585 0.6139 0.0183  0.0549  0.1202  236 LYS   A O    
32   C  CB   . LYS   A 29  ? 0.0829 0.2270 0.6134 -0.0433 -0.0065 0.1955  236 LYS   A CB   
33   C  CG   . LYS   A 29  ? 0.1123 0.2332 0.5930 0.0167  -0.0408 0.1908  236 LYS   A CG   
34   C  CD   . LYS   A 29  ? 0.0851 0.2138 0.7330 -0.0008 0.0258  0.1097  236 LYS   A CD   
35   C  CE   . LYS   A 29  ? 0.1866 0.5560 0.6617 0.0835  -0.0083 0.1779  236 LYS   A CE   
36   N  NZ   . LYS   A 29  ? 0.1109 0.4955 0.7107 0.0156  0.0532  0.1518  236 LYS   A NZ   
37   N  N    . ILE   A 30  ? 0.0526 0.2053 0.5312 0.0152  -0.0101 0.1532  237 ILE   A N    
38   C  CA   . ILE   A 30  ? 0.1478 0.1047 0.5109 -0.0314 -0.0484 0.1053  237 ILE   A CA   
39   C  C    . ILE   A 30  ? 0.0864 0.1349 0.4681 0.0010  0.0020  0.0747  237 ILE   A C    
40   O  O    . ILE   A 30  ? 0.0284 0.1984 0.5486 -0.0257 -0.0373 0.1144  237 ILE   A O    
41   C  CB   . ILE   A 30  ? 0.2583 0.1315 0.4941 -0.0766 -0.0061 0.0839  237 ILE   A CB   
42   C  CG1  . ILE   A 30  ? 0.1758 0.1920 0.5660 -0.0502 -0.0008 0.0057  237 ILE   A CG1  
43   C  CG2  . ILE   A 30  ? 0.1756 0.2128 0.5680 -0.0246 0.0568  0.0902  237 ILE   A CG2  
44   C  CD1  . ILE   A 30  ? 0.1123 0.2402 0.7091 -0.0850 -0.0706 -0.0051 237 ILE   A CD1  
45   N  N    . VAL   A 31  ? 0.1007 0.2240 0.4489 0.0053  -0.0448 0.0350  238 VAL   A N    
46   C  CA   . VAL   A 31  ? 0.0212 0.2798 0.4887 0.0429  -0.0430 0.1072  238 VAL   A CA   
47   C  C    . VAL   A 31  ? 0.0382 0.1823 0.4837 0.0429  -0.0719 0.0957  238 VAL   A C    
48   O  O    . VAL   A 31  ? 0.0204 0.1910 0.5158 0.0177  -0.0689 0.0808  238 VAL   A O    
49   C  CB   . VAL   A 31  ? 0.0105 0.3228 0.5140 0.0346  -0.0022 0.1151  238 VAL   A CB   
50   C  CG1  . VAL   A 31  ? 0.0655 0.2686 0.5444 0.0063  -0.0661 0.1453  238 VAL   A CG1  
51   C  CG2  . VAL   A 31  ? 0.0631 0.2467 0.5225 0.0407  -0.0153 0.1183  238 VAL   A CG2  
52   N  N    . SER   A 32  ? 0.0893 0.2124 0.5095 0.0911  0.0060  0.1459  239 SER   A N    
53   C  CA   . SER   A 32  ? 0.1047 0.2066 0.5101 0.0310  -0.0016 0.1116  239 SER   A CA   
54   C  C    . SER   A 32  ? 0.0601 0.2063 0.4934 -0.0016 -0.0194 0.0853  239 SER   A C    
55   O  O    . SER   A 32  ? 0.0617 0.1698 0.5451 0.0107  0.0114  0.0935  239 SER   A O    
56   C  CB   . SER   A 32  ? 0.2544 0.1754 0.6764 0.1690  0.0482  0.0862  239 SER   A CB   
57   O  OG   . SER   A 32  ? 0.2983 0.2163 0.7646 0.0475  0.1032  0.0504  239 SER   A OG   
58   N  N    . HIS   A 33  ? 0.0448 0.1639 0.5004 0.0328  -0.0571 0.0801  240 HIS   A N    
59   C  CA   . HIS   A 33  ? 0.0816 0.1251 0.4649 -0.0205 -0.0451 0.1026  240 HIS   A CA   
60   C  C    . HIS   A 33  ? 0.0298 0.1596 0.4460 -0.0300 -0.0144 0.1156  240 HIS   A C    
61   O  O    . HIS   A 33  ? 0.0352 0.1956 0.5435 0.0334  -0.0030 0.0654  240 HIS   A O    
62   C  CB   . HIS   A 33  ? 0.0142 0.2642 0.4497 -0.0081 -0.0260 0.0832  240 HIS   A CB   
63   C  CG   . HIS   A 33  ? 0.0302 0.2101 0.4780 0.0409  0.0184  0.0635  240 HIS   A CG   
64   N  ND1  . HIS   A 33  ? 0.1408 0.4983 0.4279 -0.0702 0.0679  0.0602  240 HIS   A ND1  
65   C  CD2  . HIS   A 33  ? 0.1999 0.1609 0.5565 0.0510  -0.0313 0.1330  240 HIS   A CD2  
66   C  CE1  . HIS   A 33  ? 0.1520 0.3755 0.4212 -0.1182 0.0937  0.1109  240 HIS   A CE1  
67   N  NE2  . HIS   A 33  ? 0.2339 0.3262 0.5589 -0.1009 0.0450  0.0624  240 HIS   A NE2  
68   N  N    . LEU   A 34  ? 0.0083 0.1533 0.4928 -0.0021 -0.0137 0.1379  241 LEU   A N    
69   C  CA   . LEU   A 34  ? 0.0222 0.2553 0.4341 0.0614  -0.0040 0.0550  241 LEU   A CA   
70   C  C    . LEU   A 34  ? 0.0954 0.1427 0.5066 0.0399  0.0061  0.0295  241 LEU   A C    
71   O  O    . LEU   A 34  ? 0.0620 0.1725 0.5120 0.0222  0.0246  0.0855  241 LEU   A O    
72   C  CB   . LEU   A 34  ? 0.0389 0.1896 0.4584 0.0255  -0.0201 0.0655  241 LEU   A CB   
73   C  CG   . LEU   A 34  ? 0.0658 0.2773 0.4524 0.0042  -0.0332 0.0439  241 LEU   A CG   
74   C  CD1  . LEU   A 34  ? 0.1166 0.1524 0.4658 0.0632  0.0192  0.0686  241 LEU   A CD1  
75   C  CD2  . LEU   A 34  ? 0.1072 0.3044 0.5525 -0.0655 0.0979  -0.0023 241 LEU   A CD2  
76   N  N    . LEU   A 35  ? 0.0526 0.1118 0.5195 0.0092  -0.0355 0.0278  242 LEU   A N    
77   C  CA   . LEU   A 35  ? 0.0065 0.2412 0.5736 0.0046  -0.0063 0.0196  242 LEU   A CA   
78   C  C    . LEU   A 35  ? 0.0262 0.2100 0.4826 -0.0423 -0.0802 0.0390  242 LEU   A C    
79   O  O    . LEU   A 35  ? 0.0131 0.2858 0.5862 -0.0419 -0.0316 0.1013  242 LEU   A O    
80   C  CB   . LEU   A 35  ? 0.0064 0.2104 0.5932 -0.0025 0.0075  0.0524  242 LEU   A CB   
81   C  CG   . LEU   A 35  ? 0.2027 0.2040 0.6047 -0.0253 0.0030  0.0324  242 LEU   A CG   
82   C  CD1  . LEU   A 35  ? 0.3223 0.2033 0.6042 -0.0519 0.0522  -0.0483 242 LEU   A CD1  
83   C  CD2  . LEU   A 35  ? 0.1847 0.1153 0.6941 -0.0025 -0.0222 0.0466  242 LEU   A CD2  
84   N  N    . VAL   A 36  ? 0.0863 0.2042 0.5126 -0.0070 -0.0912 0.1018  243 VAL   A N    
85   C  CA   . VAL   A 36  ? 0.0801 0.3338 0.5530 0.0128  -0.0435 0.0812  243 VAL   A CA   
86   C  C    . VAL   A 36  ? 0.0467 0.3891 0.5096 -0.0430 0.0332  0.0491  243 VAL   A C    
87   O  O    . VAL   A 36  ? 0.0490 0.5019 0.6011 0.0093  0.0699  0.1502  243 VAL   A O    
88   C  CB   . VAL   A 36  ? 0.2137 0.1848 0.6316 0.0946  -0.0657 0.0371  243 VAL   A CB   
89   C  CG1  . VAL   A 36  ? 0.3243 0.1622 0.6900 0.0872  -0.0867 0.0222  243 VAL   A CG1  
90   C  CG2  . VAL   A 36  ? 0.2807 0.2740 0.6008 -0.0431 -0.0127 0.0860  243 VAL   A CG2  
91   N  N    . ALA   A 37  ? 0.1622 0.3164 0.5535 -0.0095 0.0411  0.0548  244 ALA   A N    
92   C  CA   . ALA   A 37  ? 0.1270 0.2690 0.5151 -0.0605 0.0321  0.0595  244 ALA   A CA   
93   C  C    . ALA   A 37  ? 0.1121 0.2766 0.4970 0.0053  0.0628  0.0326  244 ALA   A C    
94   O  O    . ALA   A 37  ? 0.0237 0.2880 0.5780 0.0254  0.0382  0.0702  244 ALA   A O    
95   C  CB   . ALA   A 37  ? 0.0143 0.3862 0.6509 -0.0460 0.0010  -0.1421 244 ALA   A CB   
96   N  N    . GLU   A 38  ? 0.0853 0.2513 0.5090 0.0443  -0.0340 0.0407  245 GLU   A N    
97   C  CA   . GLU   A 38  ? 0.0864 0.2708 0.5731 0.1058  -0.0012 0.1208  245 GLU   A CA   
98   C  C    . GLU   A 38  ? 0.1366 0.3512 0.5965 0.0040  0.0584  0.1385  245 GLU   A C    
99   O  O    . GLU   A 38  ? 0.0363 0.4192 0.6165 -0.0376 0.0234  0.1508  245 GLU   A O    
100  C  CB   . GLU   A 38  ? 0.0885 0.2043 0.6863 0.1193  -0.0459 0.0607  245 GLU   A CB   
101  C  CG   . GLU   A 38  ? 0.2914 0.3485 0.5959 0.1191  -0.1093 0.0931  245 GLU   A CG   
102  C  CD   . GLU   A 38  ? 0.3536 0.4777 0.6169 0.0255  -0.0518 0.1911  245 GLU   A CD   
103  O  OE1  . GLU   A 38  ? 0.1927 0.3743 0.5739 0.1536  0.0882  0.0910  245 GLU   A OE1  
104  O  OE2  . GLU   A 38  ? 0.2103 0.8282 0.7297 0.0363  -0.1014 0.1407  245 GLU   A OE2  
105  N  N    . PRO   A 39  ? 0.0071 0.3679 0.6673 -0.0086 0.0083  0.0553  246 PRO   A N    
106  C  CA   . PRO   A 39  ? 0.0380 0.2595 0.6171 -0.0273 0.0291  0.0957  246 PRO   A CA   
107  C  C    . PRO   A 39  ? 0.1192 0.3346 0.5503 -0.0357 -0.0044 0.0260  246 PRO   A C    
108  O  O    . PRO   A 39  ? 0.0947 0.2664 0.5813 0.0548  -0.0129 -0.0062 246 PRO   A O    
109  C  CB   . PRO   A 39  ? 0.1066 0.3062 0.7015 0.0453  0.0303  0.1263  246 PRO   A CB   
110  C  CG   . PRO   A 39  ? 0.1823 0.4359 0.7612 -0.0483 0.0884  0.1389  246 PRO   A CG   
111  C  CD   . PRO   A 39  ? 0.0278 0.5490 0.7757 -0.0109 0.1161  0.2185  246 PRO   A CD   
112  N  N    . GLU   A 40  ? 0.1073 0.2992 0.6180 0.1014  0.0288  0.0807  247 GLU   A N    
113  C  CA   . GLU   A 40  ? 0.2310 0.2728 0.6034 0.0299  -0.0883 0.1871  247 GLU   A CA   
114  C  C    . GLU   A 40  ? 0.0411 0.1530 0.6183 0.0327  -0.0019 0.1438  247 GLU   A C    
115  O  O    . GLU   A 40  ? 0.1465 0.1431 0.6815 0.0362  0.0064  0.1303  247 GLU   A O    
116  C  CB   . GLU   A 40  ? 0.1935 0.4519 0.6374 0.0079  -0.1046 0.2008  247 GLU   A CB   
117  C  CG   . GLU   A 40  ? 0.1771 0.3752 0.8663 0.0439  -0.0708 0.2362  247 GLU   A CG   
118  C  CD   . GLU   A 40  ? 0.0403 0.4013 1.1944 0.1157  0.0465  0.1278  247 GLU   A CD   
119  O  OE1  . GLU   A 40  ? 0.3438 0.3599 1.2557 -0.0580 0.0868  -0.0991 247 GLU   A OE1  
120  O  OE2  . GLU   A 40  ? 0.2619 0.7202 1.3099 0.4235  -0.0474 0.0466  247 GLU   A OE2  
121  N  N    . LYS   A 41  ? 0.1114 0.3245 0.6089 0.0192  -0.0466 0.1158  248 LYS   A N    
122  C  CA   . LYS   A 41  ? 0.1992 0.2611 0.6021 0.0801  -0.0281 0.1447  248 LYS   A CA   
123  C  C    . LYS   A 41  ? 0.1404 0.2921 0.5987 0.0392  0.0135  0.1714  248 LYS   A C    
124  O  O    . LYS   A 41  ? 0.1002 0.4884 0.6226 0.0171  -0.0463 0.2382  248 LYS   A O    
125  C  CB   . LYS   A 41  ? 0.4747 0.3314 0.6743 0.1174  -0.1519 0.0293  248 LYS   A CB   
126  C  CG   . LYS   A 41  ? 0.5553 0.3571 0.7882 0.2272  -0.1399 -0.1241 248 LYS   A CG   
127  C  CD   . LYS   A 41  ? 0.8405 0.4087 0.9282 0.3132  -0.1175 -0.3158 248 LYS   A CD   
128  C  CE   . LYS   A 41  ? 1.2068 0.7622 0.9186 0.2322  -0.0344 -0.3659 248 LYS   A CE   
129  N  NZ   . LYS   A 41  ? 1.2584 0.6260 0.7999 0.2728  -0.1564 -0.2120 248 LYS   A NZ   
130  N  N    . ILE   A 42  ? 0.0183 0.1989 0.6705 -0.0436 -0.0117 0.1349  249 ILE   A N    
131  C  CA   . ILE   A 42  ? 0.1886 0.2997 0.6730 0.0215  0.0051  0.0313  249 ILE   A CA   
132  C  C    . ILE   A 42  ? 0.0656 0.2106 0.7023 -0.0787 0.0461  0.0657  249 ILE   A C    
133  O  O    . ILE   A 42  ? 0.0974 0.4806 0.6748 0.0444  -0.0001 0.0629  249 ILE   A O    
134  C  CB   . ILE   A 42  ? 0.1138 0.3039 0.7439 0.0435  -0.0508 0.0342  249 ILE   A CB   
135  C  CG1  . ILE   A 42  ? 0.2860 0.1456 0.8659 -0.0187 -0.1478 -0.1213 249 ILE   A CG1  
136  C  CG2  . ILE   A 42  ? 0.3594 0.2285 0.7552 0.1269  -0.0758 0.0364  249 ILE   A CG2  
137  C  CD1  . ILE   A 42  ? 0.4242 0.2964 1.0733 -0.1597 -0.1846 -0.1251 249 ILE   A CD1  
138  N  N    . TYR   A 43  ? 0.0367 0.2818 0.6872 -0.0057 0.0034  0.1160  250 TYR   A N    
139  C  CA   . TYR   A 43  ? 0.0733 0.3698 0.6632 -0.0345 -0.0162 0.1910  250 TYR   A CA   
140  C  C    . TYR   A 43  ? 0.0750 0.3383 0.5386 -0.0538 0.0529  0.1417  250 TYR   A C    
141  O  O    . TYR   A 43  ? 0.0851 0.3219 0.5672 0.0518  -0.0396 0.1534  250 TYR   A O    
142  C  CB   . TYR   A 43  ? 0.0802 0.3637 0.8572 -0.0331 0.1255  0.0970  250 TYR   A CB   
143  C  CG   . TYR   A 43  ? 0.2503 0.4220 1.0934 0.0315  0.2008  -0.0043 250 TYR   A CG   
144  C  CD1  . TYR   A 43  ? 0.0381 0.3648 1.1657 0.0050  0.0256  0.0108  250 TYR   A CD1  
145  C  CD2  . TYR   A 43  ? 0.3612 0.4638 1.2318 0.2286  0.1545  -0.0187 250 TYR   A CD2  
146  C  CE1  . TYR   A 43  ? 0.3674 0.4231 1.4422 0.2695  -0.0949 -0.0791 250 TYR   A CE1  
147  C  CE2  . TYR   A 43  ? 0.4508 0.4256 1.5791 0.2576  0.1713  0.0711  250 TYR   A CE2  
148  C  CZ   . TYR   A 43  ? 0.5218 0.5313 1.5474 0.2823  0.1536  0.0996  250 TYR   A CZ   
149  O  OH   . TYR   A 43  ? 0.8729 0.5849 1.9142 0.0977  0.6283  -0.0354 250 TYR   A OH   
150  N  N    . ALA   A 44  ? 0.0291 0.2729 0.5522 -0.0309 0.0166  0.1078  251 ALA   A N    
151  C  CA   . ALA   A 44  ? 0.0315 0.2920 0.5427 -0.0109 0.0042  0.0767  251 ALA   A CA   
152  C  C    . ALA   A 44  ? 0.0109 0.2690 0.5354 -0.0233 -0.0384 0.0198  251 ALA   A C    
153  O  O    . ALA   A 44  ? 0.0529 0.1879 0.5374 -0.0249 0.0219  0.0796  251 ALA   A O    
154  C  CB   . ALA   A 44  ? 0.0075 0.2953 0.5189 -0.0100 0.0172  0.0878  251 ALA   A CB   
155  N  N    . MET   A 45  ? 0.0640 0.1669 0.5181 -0.0047 0.0263  0.0733  252 MET   A N    
156  C  CA   . MET   A 45  ? 0.0094 0.1868 0.5751 0.0020  -0.0296 0.1323  252 MET   A CA   
157  C  C    . MET   A 45  ? 0.0805 0.1892 0.5082 0.0260  -0.0399 0.1129  252 MET   A C    
158  O  O    . MET   A 45  ? 0.0603 0.1885 0.5871 0.0005  -0.0267 0.1175  252 MET   A O    
159  C  CB   . MET   A 45  ? 0.0867 0.2924 0.5909 -0.0229 -0.0332 0.1760  252 MET   A CB   
160  C  CG   . MET   A 45  ? 0.0833 0.2561 0.6075 -0.0829 0.0265  0.1462  252 MET   A CG   
161  S  SD   . MET   A 45  ? 0.1096 0.3116 0.5829 0.0203  0.0056  0.1703  252 MET   A SD   
162  C  CE   . MET   A 45  ? 0.1325 0.3155 0.6521 0.0108  0.0797  0.1425  252 MET   A CE   
163  N  N    . PRO   A 46  ? 0.0108 0.1865 0.5086 0.0063  0.0058  0.1280  253 PRO   A N    
164  C  CA   . PRO   A 46  ? 0.0102 0.2344 0.5136 0.0287  0.0052  0.1319  253 PRO   A CA   
165  C  C    . PRO   A 46  ? 0.0258 0.2743 0.5050 0.0150  0.0546  0.0260  253 PRO   A C    
166  O  O    . PRO   A 46  ? 0.0548 0.2875 0.5559 0.0040  -0.0004 0.0898  253 PRO   A O    
167  C  CB   . PRO   A 46  ? 0.0871 0.1717 0.5453 -0.0219 0.0643  0.1095  253 PRO   A CB   
168  C  CG   . PRO   A 46  ? 0.0365 0.1534 0.5804 -0.0604 0.0114  0.0989  253 PRO   A CG   
169  C  CD   . PRO   A 46  ? 0.0795 0.2675 0.5413 -0.0144 0.0164  0.0781  253 PRO   A CD   
170  N  N    . ASP   A 47  ? 0.0686 0.2185 0.5872 0.0572  0.0373  0.0995  254 ASP   A N    
171  C  CA   . ASP   A 47  ? 0.0298 0.1887 0.5073 0.0039  -0.0046 0.1263  254 ASP   A CA   
172  C  C    . ASP   A 47  ? 0.1676 0.1893 0.4337 -0.0346 0.0134  0.0435  254 ASP   A C    
173  O  O    . ASP   A 47  ? 0.0653 0.3153 0.4274 -0.0402 0.0139  0.0506  254 ASP   A O    
174  C  CB   . ASP   A 47  ? 0.0190 0.2454 0.5620 0.0119  -0.0079 0.0499  254 ASP   A CB   
175  C  CG   . ASP   A 47  ? 0.1091 0.2344 0.4493 0.0186  0.0192  0.0505  254 ASP   A CG   
176  O  OD1  . ASP   A 47  ? 0.1002 0.2095 0.6515 -0.0130 -0.0068 0.1070  254 ASP   A OD1  
177  O  OD2  . ASP   A 47  ? 0.2251 0.2278 0.4555 0.0308  -0.0053 0.0545  254 ASP   A OD2  
178  N  N    . PRO   A 48  ? 0.1200 0.1700 0.5203 0.0230  0.0171  0.1151  255 PRO   A N    
179  C  CA   . PRO   A 48  ? 0.1679 0.1945 0.4847 0.0220  0.0137  0.0845  255 PRO   A CA   
180  C  C    . PRO   A 48  ? 0.1067 0.1718 0.5328 -0.0347 0.0144  0.0380  255 PRO   A C    
181  O  O    . PRO   A 48  ? 0.2900 0.2536 0.5991 0.0418  -0.0778 0.0551  255 PRO   A O    
182  C  CB   . PRO   A 48  ? 0.0855 0.1805 0.5547 0.0023  0.0290  0.0428  255 PRO   A CB   
183  C  CG   . PRO   A 48  ? 0.1819 0.2546 0.5616 0.0065  0.0168  0.0691  255 PRO   A CG   
184  C  CD   . PRO   A 48  ? 0.1056 0.2962 0.5360 0.0040  0.0107  0.1453  255 PRO   A CD   
185  N  N    . THR   A 49  ? 0.0402 0.2994 0.4838 0.0600  0.0778  0.0847  256 THR   A N    
186  C  CA   . THR   A 49  ? 0.1062 0.2197 0.5212 0.0955  0.0020  0.1330  256 THR   A CA   
187  C  C    . THR   A 49  ? 0.0078 0.2177 0.5630 -0.0153 -0.0241 0.1316  256 THR   A C    
188  O  O    . THR   A 49  ? 0.0784 0.3153 0.7130 0.1130  -0.0338 0.0292  256 THR   A O    
189  C  CB   . THR   A 49  ? 0.0897 0.2732 0.5104 0.0596  -0.0349 0.0869  256 THR   A CB   
190  O  OG1  . THR   A 49  ? 0.1677 0.2768 0.5487 0.0456  0.0061  -0.0212 256 THR   A OG1  
191  C  CG2  . THR   A 49  ? 0.0451 0.3562 0.6053 -0.1083 0.0201  0.1115  256 THR   A CG2  
192  N  N    . VAL   A 50  ? 0.0393 0.2744 0.6203 -0.0920 -0.0259 0.1567  257 VAL   A N    
193  C  CA   . VAL   A 50  ? 0.0109 0.2063 0.5798 0.0260  0.0430  0.1438  257 VAL   A CA   
194  C  C    . VAL   A 50  ? 0.0442 0.2050 0.5937 -0.0096 0.0004  0.1271  257 VAL   A C    
195  O  O    . VAL   A 50  ? 0.0424 0.2403 0.5703 -0.0297 -0.0137 0.1257  257 VAL   A O    
196  C  CB   . VAL   A 50  ? 0.0356 0.2830 0.6096 0.0787  -0.0368 0.0737  257 VAL   A CB   
197  C  CG1  . VAL   A 50  ? 0.0254 0.2588 0.5559 0.0636  -0.0308 0.0391  257 VAL   A CG1  
198  C  CG2  . VAL   A 50  ? 0.1806 0.1973 0.6564 0.1020  0.0060  0.0960  257 VAL   A CG2  
199  N  N    . PRO   A 51  ? 0.0423 0.2425 0.5545 0.0258  -0.0190 0.0975  258 PRO   A N    
200  C  CA   . PRO   A 51  ? 0.1123 0.2640 0.5533 0.0174  -0.0034 0.1356  258 PRO   A CA   
201  C  C    . PRO   A 51  ? 0.1077 0.3172 0.4685 0.0835  -0.0049 0.0905  258 PRO   A C    
202  O  O    . PRO   A 51  ? 0.0542 0.3694 0.5858 0.0235  -0.0092 0.1588  258 PRO   A O    
203  C  CB   . PRO   A 51  ? 0.0862 0.2363 0.5384 0.0053  0.0007  0.1260  258 PRO   A CB   
204  C  CG   . PRO   A 51  ? 0.1171 0.2909 0.5946 0.0125  0.0180  0.1018  258 PRO   A CG   
205  C  CD   . PRO   A 51  ? 0.1028 0.2192 0.6370 0.0199  0.0345  0.1157  258 PRO   A CD   
206  N  N    . ASP   A 52  ? 0.0171 0.2647 0.4624 -0.0361 -0.0151 0.0688  259 ASP   A N    
207  C  CA   . ASP   A 52  ? 0.0250 0.3150 0.5424 0.0299  0.0201  0.1427  259 ASP   A CA   
208  C  C    . ASP   A 52  ? 0.1068 0.2572 0.6207 0.0500  -0.0475 0.1087  259 ASP   A C    
209  O  O    . ASP   A 52  ? 0.1311 0.3690 0.6933 -0.0157 -0.1091 0.2293  259 ASP   A O    
210  C  CB   . ASP   A 52  ? 0.3423 0.3011 0.5631 -0.1118 -0.0824 0.0602  259 ASP   A CB   
211  C  CG   . ASP   A 52  ? 0.4304 0.3210 0.6579 0.0167  -0.1133 -0.0358 259 ASP   A CG   
212  O  OD1  . ASP   A 52  ? 0.2299 0.3212 0.6702 0.0236  -0.0330 0.0091  259 ASP   A OD1  
213  O  OD2  . ASP   A 52  ? 0.7839 0.4292 0.8083 -0.1956 -0.0522 -0.0987 259 ASP   A OD2  
214  N  N    . SER   A 53  ? 0.0432 0.3382 0.6802 0.0392  0.0152  0.1736  260 SER   A N    
215  C  CA   . SER   A 53  ? 0.0626 0.3189 0.6050 0.0014  -0.0162 0.1263  260 SER   A CA   
216  C  C    . SER   A 53  ? 0.0757 0.3059 0.4997 -0.0561 0.0010  0.1702  260 SER   A C    
217  O  O    . SER   A 53  ? 0.1087 0.2753 0.6115 -0.0221 -0.0222 0.1671  260 SER   A O    
218  C  CB   . SER   A 53  ? 0.0458 0.3994 0.6682 0.0392  0.0733  0.1537  260 SER   A CB   
219  O  OG   . SER   A 53  ? 0.0826 0.3648 0.7299 0.0554  -0.0228 0.1448  260 SER   A OG   
220  N  N    . ASP   A 54  ? 0.0975 0.2252 0.5630 -0.0263 0.0216  0.1494  261 ASP   A N    
221  C  CA   . ASP   A 54  ? 0.1136 0.2742 0.6634 -0.0584 0.0579  0.1023  261 ASP   A CA   
222  C  C    . ASP   A 54  ? 0.2141 0.1494 0.6275 -0.0393 0.0220  0.1208  261 ASP   A C    
223  O  O    . ASP   A 54  ? 0.2093 0.2017 0.6941 -0.0332 0.0442  0.1332  261 ASP   A O    
224  C  CB   . ASP   A 54  ? 0.2540 0.1981 0.8519 -0.0606 0.0457  0.1300  261 ASP   A CB   
225  C  CG   . ASP   A 54  ? 0.1341 0.2124 0.9963 -0.0267 -0.0558 0.1462  261 ASP   A CG   
226  O  OD1  . ASP   A 54  ? 0.3509 0.2477 0.8905 0.1042  0.0705  0.0986  261 ASP   A OD1  
227  O  OD2  . ASP   A 54  ? 0.6280 0.1587 0.9894 -0.0958 0.2777  -0.0044 261 ASP   A OD2  
228  N  N    . ILE   A 55  ? 0.0670 0.3115 0.6652 0.0539  -0.0195 0.1488  262 ILE   A N    
229  C  CA   . ILE   A 55  ? 0.0371 0.2665 0.6692 -0.0377 -0.0201 0.1215  262 ILE   A CA   
230  C  C    . ILE   A 55  ? 0.0884 0.2195 0.6500 -0.0620 0.0332  0.0876  262 ILE   A C    
231  O  O    . ILE   A 55  ? 0.1143 0.2606 0.6564 -0.0619 0.0308  0.1021  262 ILE   A O    
232  C  CB   . ILE   A 55  ? 0.1289 0.3612 0.6973 0.0630  0.0124  0.2161  262 ILE   A CB   
233  C  CG1  . ILE   A 55  ? 0.4192 0.3786 0.7641 0.1322  0.0656  0.2562  262 ILE   A CG1  
234  C  CG2  . ILE   A 55  ? 0.2078 0.3185 0.7362 0.0855  -0.0633 0.2095  262 ILE   A CG2  
235  C  CD1  . ILE   A 55  ? 0.4496 0.4682 0.8445 0.1721  -0.0140 0.1623  262 ILE   A CD1  
236  N  N    . LYS   A 56  ? 0.0223 0.2073 0.7507 -0.0345 -0.0064 0.1681  263 LYS   A N    
237  C  CA   . LYS   A 56  ? 0.0132 0.2548 0.7159 0.0182  -0.0134 0.1826  263 LYS   A CA   
238  C  C    . LYS   A 56  ? 0.0481 0.2159 0.5834 0.0185  0.0298  0.0874  263 LYS   A C    
239  O  O    . LYS   A 56  ? 0.0457 0.2930 0.5779 -0.0481 -0.0248 0.0753  263 LYS   A O    
240  C  CB   . LYS   A 56  ? 0.0306 0.2391 0.6903 0.0306  -0.0107 0.1576  263 LYS   A CB   
241  C  CG   . LYS   A 56  ? 0.1048 0.2173 0.6027 -0.0743 -0.0153 0.1069  263 LYS   A CG   
242  C  CD   . LYS   A 56  ? 0.0101 0.1724 0.6366 0.0183  -0.0184 0.1162  263 LYS   A CD   
243  C  CE   . LYS   A 56  ? 0.1003 0.2092 0.6075 0.0193  0.0239  0.1594  263 LYS   A CE   
244  N  NZ   . LYS   A 56  ? 0.1914 0.1723 0.6078 0.0186  0.0202  0.1004  263 LYS   A NZ   
245  N  N    . ALA   A 57  ? 0.0799 0.1954 0.5783 -0.0290 0.0289  0.1366  264 ALA   A N    
246  C  CA   . ALA   A 57  ? 0.0633 0.2040 0.6493 -0.0252 -0.0134 0.1128  264 ALA   A CA   
247  C  C    . ALA   A 57  ? 0.1404 0.2825 0.5688 -0.0381 -0.0701 0.1122  264 ALA   A C    
248  O  O    . ALA   A 57  ? 0.1011 0.2551 0.5242 -0.0602 -0.0304 0.1110  264 ALA   A O    
249  C  CB   . ALA   A 57  ? 0.1449 0.1659 0.6417 -0.0252 -0.0813 0.1151  264 ALA   A CB   
250  N  N    . LEU   A 58  ? 0.0801 0.2809 0.6401 -0.0011 -0.0403 0.1102  265 LEU   A N    
251  C  CA   . LEU   A 58  ? 0.0973 0.2075 0.5975 -0.0009 0.0188  0.1019  265 LEU   A CA   
252  C  C    . LEU   A 58  ? 0.0337 0.2267 0.6032 0.0628  0.0471  0.0774  265 LEU   A C    
253  O  O    . LEU   A 58  ? 0.0384 0.2582 0.6176 0.0275  0.0275  0.1045  265 LEU   A O    
254  C  CB   . LEU   A 58  ? 0.0455 0.1959 0.6155 0.0252  0.0165  0.1014  265 LEU   A CB   
255  C  CG   . LEU   A 58  ? 0.1207 0.2144 0.6504 0.0739  0.0592  0.0702  265 LEU   A CG   
256  C  CD1  . LEU   A 58  ? 0.1759 0.2381 0.7070 0.0396  0.0337  0.1418  265 LEU   A CD1  
257  C  CD2  . LEU   A 58  ? 0.0918 0.2406 0.5987 0.0674  0.0022  0.0708  265 LEU   A CD2  
258  N  N    . THR   A 59  ? 0.0417 0.1706 0.6048 0.0062  0.0608  0.0425  266 THR   A N    
259  C  CA   . THR   A 59  ? 0.1156 0.1597 0.6120 0.0383  0.0622  0.0780  266 THR   A CA   
260  C  C    . THR   A 59  ? 0.1180 0.1621 0.6520 0.0626  0.0631  0.0434  266 THR   A C    
261  O  O    . THR   A 59  ? 0.1388 0.1811 0.5838 0.0168  0.0626  -0.0135 266 THR   A O    
262  C  CB   . THR   A 59  ? 0.1416 0.2363 0.6389 -0.0058 0.1230  0.0684  266 THR   A CB   
263  O  OG1  . THR   A 59  ? 0.1612 0.2685 0.6501 0.0008  -0.0085 0.0525  266 THR   A OG1  
264  C  CG2  . THR   A 59  ? 0.0684 0.2606 0.6686 0.0231  0.0870  0.0294  266 THR   A CG2  
265  N  N    . THR   A 60  ? 0.0189 0.2916 0.5831 0.0316  0.0568  0.0525  267 THR   A N    
266  C  CA   . THR   A 60  ? 0.0261 0.2407 0.5041 0.0282  0.0915  0.0090  267 THR   A CA   
267  C  C    . THR   A 60  ? 0.0102 0.2681 0.4746 -0.0263 0.0200  0.0392  267 THR   A C    
268  O  O    . THR   A 60  ? 0.0851 0.1780 0.5025 -0.0082 0.0375  0.0830  267 THR   A O    
269  C  CB   . THR   A 60  ? 0.0546 0.2341 0.5767 0.0030  -0.0103 0.0543  267 THR   A CB   
270  O  OG1  . THR   A 60  ? 0.0550 0.1526 0.6106 0.0078  -0.0318 0.1098  267 THR   A OG1  
271  C  CG2  . THR   A 60  ? 0.0986 0.2363 0.6462 0.0400  -0.0208 0.0407  267 THR   A CG2  
272  N  N    . LEU   A 61  ? 0.0150 0.2312 0.5109 0.0335  0.0401  0.0379  268 LEU   A N    
273  C  CA   . LEU   A 61  ? 0.0076 0.2202 0.5561 0.0167  0.0101  0.0839  268 LEU   A CA   
274  C  C    . LEU   A 61  ? 0.0152 0.1434 0.5779 0.0121  0.0376  0.0594  268 LEU   A C    
275  O  O    . LEU   A 61  ? 0.0361 0.1712 0.5154 0.0118  0.0076  0.0786  268 LEU   A O    
276  C  CB   . LEU   A 61  ? 0.0065 0.1737 0.5851 -0.0021 0.0066  0.1309  268 LEU   A CB   
277  C  CG   . LEU   A 61  ? 0.1479 0.2211 0.6310 -0.0856 -0.0419 0.1055  268 LEU   A CG   
278  C  CD1  . LEU   A 61  ? 0.1814 0.2165 0.6518 -0.1007 -0.0724 0.0952  268 LEU   A CD1  
279  C  CD2  . LEU   A 61  ? 0.1624 0.2131 0.6921 -0.1016 -0.0217 0.0836  268 LEU   A CD2  
280  N  N    . CYS   A 62  ? 0.0103 0.1758 0.5938 0.0225  0.0289  0.0395  269 CYS   A N    
281  C  CA   . CYS   A 62  ? 0.0639 0.1453 0.5796 -0.0003 0.0454  0.0456  269 CYS   A CA   
282  C  C    . CYS   A 62  ? 0.0270 0.2649 0.5373 -0.0246 0.0971  0.0161  269 CYS   A C    
283  O  O    . CYS   A 62  ? 0.0733 0.2322 0.5854 -0.0079 0.0068  0.0040  269 CYS   A O    
284  C  CB   . CYS   A 62  ? 0.0964 0.1201 0.6527 -0.0230 -0.0651 0.0288  269 CYS   A CB   
285  S  SG   . CYS   A 62  ? 0.1512 0.1905 0.7835 -0.0295 0.0071  0.0919  269 CYS   A SG   
286  N  N    . ASP   A 63  ? 0.0271 0.3958 0.6269 0.0171  0.1134  0.0642  270 ASP   A N    
287  C  CA   . ASP   A 63  ? 0.0424 0.2791 0.6222 -0.0245 0.0621  -0.0094 270 ASP   A CA   
288  C  C    . ASP   A 63  ? 0.0681 0.2730 0.4379 -0.0374 0.0662  0.0867  270 ASP   A C    
289  O  O    . ASP   A 63  ? 0.0894 0.2672 0.5026 0.0093  0.0095  0.0653  270 ASP   A O    
290  C  CB   . ASP   A 63  ? 0.0539 0.2400 0.6347 -0.0526 0.0043  -0.0395 270 ASP   A CB   
291  C  CG   . ASP   A 63  ? 0.1783 0.4944 0.7068 -0.0121 0.1210  0.0584  270 ASP   A CG   
292  O  OD1  . ASP   A 63  ? 0.1637 0.6154 0.8853 0.0375  0.0995  0.2633  270 ASP   A OD1  
293  O  OD2  . ASP   A 63  ? 0.7475 0.9184 0.7067 0.2853  0.1833  -0.0752 270 ASP   A OD2  
294  N  N    . LEU   A 64  ? 0.0505 0.2794 0.5049 -0.0096 0.0438  0.0269  271 LEU   A N    
295  C  CA   . LEU   A 64  ? 0.0271 0.2168 0.5604 -0.0540 0.0385  0.0338  271 LEU   A CA   
296  C  C    . LEU   A 64  ? 0.0155 0.2469 0.4823 -0.0221 -0.0221 0.0740  271 LEU   A C    
297  O  O    . LEU   A 64  ? 0.0728 0.1354 0.5802 0.0028  -0.0423 0.0733  271 LEU   A O    
298  C  CB   . LEU   A 64  ? 0.0789 0.1794 0.5590 -0.0254 0.0189  0.0249  271 LEU   A CB   
299  C  CG   . LEU   A 64  ? 0.0373 0.2744 0.4956 0.0229  0.0266  0.0525  271 LEU   A CG   
300  C  CD1  . LEU   A 64  ? 0.1326 0.3810 0.4669 0.0593  -0.0003 0.0525  271 LEU   A CD1  
301  C  CD2  . LEU   A 64  ? 0.0810 0.2086 0.5233 -0.1172 0.0247  0.0545  271 LEU   A CD2  
302  N  N    . ALA   A 65  ? 0.0127 0.2096 0.6023 0.0066  0.0323  0.0531  272 ALA   A N    
303  C  CA   . ALA   A 65  ? 0.0121 0.2640 0.4849 0.0047  0.0525  0.0189  272 ALA   A CA   
304  C  C    . ALA   A 65  ? 0.1537 0.2350 0.4528 0.0391  0.0159  0.0948  272 ALA   A C    
305  O  O    . ALA   A 65  ? 0.0684 0.3217 0.4712 0.0128  0.0265  0.0139  272 ALA   A O    
306  C  CB   . ALA   A 65  ? 0.0405 0.3554 0.5450 -0.0769 0.0754  0.0862  272 ALA   A CB   
307  N  N    . ASP   A 66  ? 0.0115 0.2947 0.5508 -0.0378 0.0081  0.0334  273 ASP   A N    
308  C  CA   . ASP   A 66  ? 0.0370 0.2970 0.6156 -0.0684 0.0823  0.0098  273 ASP   A CA   
309  C  C    . ASP   A 66  ? 0.1366 0.2978 0.5091 -0.1143 0.0052  -0.0123 273 ASP   A C    
310  O  O    . ASP   A 66  ? 0.1298 0.2470 0.5180 -0.0425 0.0010  0.0261  273 ASP   A O    
311  C  CB   . ASP   A 66  ? 0.0715 0.3459 0.5853 0.0222  0.0408  0.0238  273 ASP   A CB   
312  C  CG   . ASP   A 66  ? 0.2150 0.4416 0.5830 0.0951  0.1536  -0.0077 273 ASP   A CG   
313  O  OD1  . ASP   A 66  ? 0.1822 0.6073 0.6980 0.0219  0.1018  -0.0338 273 ASP   A OD1  
314  O  OD2  . ASP   A 66  ? 0.2579 0.5693 0.7378 0.1220  0.1544  0.1709  273 ASP   A OD2  
315  N  N    . ARG   A 67  ? 0.0697 0.2272 0.4710 -0.0765 0.0568  0.0326  274 ARG   A N    
316  C  CA   . ARG   A 67  ? 0.0596 0.2302 0.4896 -0.0595 0.1102  0.0363  274 ARG   A CA   
317  C  C    . ARG   A 67  ? 0.0700 0.2222 0.4838 -0.0622 0.1023  -0.0073 274 ARG   A C    
318  O  O    . ARG   A 67  ? 0.1622 0.3351 0.5601 -0.0466 0.0415  0.0506  274 ARG   A O    
319  C  CB   . ARG   A 67  ? 0.1099 0.3758 0.4714 -0.1269 0.0585  0.0286  274 ARG   A CB   
320  C  CG   . ARG   A 67  ? 0.1731 0.3455 0.5145 -0.0648 0.0696  0.0668  274 ARG   A CG   
321  C  CD   . ARG   A 67  ? 0.1579 0.3584 0.5201 -0.0779 0.1427  -0.0056 274 ARG   A CD   
322  N  NE   . ARG   A 67  ? 0.2286 0.4946 0.5301 -0.0591 0.1469  0.0586  274 ARG   A NE   
323  C  CZ   . ARG   A 67  ? 0.1264 0.5497 0.5491 -0.0360 0.0992  0.0270  274 ARG   A CZ   
324  N  NH1  . ARG   A 67  ? 0.0169 0.5063 0.7770 -0.0297 0.0392  0.0467  274 ARG   A NH1  
325  N  NH2  . ARG   A 67  ? 0.0783 0.4259 0.5995 -0.0222 0.0709  0.0949  274 ARG   A NH2  
326  N  N    . GLU   A 68  ? 0.0586 0.2723 0.4967 0.0231  0.0575  0.0080  275 GLU   A N    
327  C  CA   A GLU   A 68  ? 0.0144 0.2383 0.5547 -0.0229 0.0505  -0.0020 275 GLU   A CA   
328  C  CA   B GLU   A 68  ? 0.0124 0.2328 0.5558 -0.0183 0.0450  0.0176  275 GLU   A CA   
329  C  C    . GLU   A 68  ? 0.0516 0.2449 0.5356 0.0075  0.0065  -0.0415 275 GLU   A C    
330  O  O    . GLU   A 68  ? 0.0154 0.2375 0.5839 -0.0388 0.0378  0.0047  275 GLU   A O    
331  C  CB   A GLU   A 68  ? 0.0137 0.3005 0.5675 -0.0019 0.0644  -0.0262 275 GLU   A CB   
332  C  CB   B GLU   A 68  ? 0.0130 0.2918 0.5578 -0.0395 0.0242  0.0118  275 GLU   A CB   
333  C  CG   A GLU   A 68  ? 0.1420 0.3517 0.5981 -0.0859 0.1136  -0.0334 275 GLU   A CG   
334  C  CG   B GLU   A 68  ? 0.0322 0.3150 0.5700 0.0021  0.0649  -0.0066 275 GLU   A CG   
335  C  CD   A GLU   A 68  ? 0.1786 0.4870 0.5883 -0.0626 0.0836  -0.0423 275 GLU   A CD   
336  C  CD   B GLU   A 68  ? 0.0727 0.3595 0.5882 0.0007  0.0601  -0.0339 275 GLU   A CD   
337  O  OE1  A GLU   A 68  ? 0.2069 0.2781 0.6937 -0.1689 0.2061  0.0627  275 GLU   A OE1  
338  O  OE1  B GLU   A 68  ? 0.1345 0.3486 0.7538 0.1815  0.0222  -0.0730 275 GLU   A OE1  
339  O  OE2  A GLU   A 68  ? 0.1989 0.5532 0.5956 0.1847  0.1244  0.1193  275 GLU   A OE2  
340  O  OE2  B GLU   A 68  ? 0.1575 0.1686 0.5375 0.0944  0.0448  0.0408  275 GLU   A OE2  
341  N  N    . LEU   A 69  ? 0.0833 0.2371 0.5118 0.0031  0.0529  -0.0276 276 LEU   A N    
342  C  CA   . LEU   A 69  ? 0.0901 0.1917 0.5198 0.0068  0.0508  -0.0147 276 LEU   A CA   
343  C  C    . LEU   A 69  ? 0.0065 0.3116 0.5136 -0.0045 0.0102  -0.0342 276 LEU   A C    
344  O  O    . LEU   A 69  ? 0.0098 0.2823 0.5302 -0.0278 -0.0209 0.0113  276 LEU   A O    
345  C  CB   . LEU   A 69  ? 0.0869 0.2005 0.5948 -0.0020 0.0302  -0.0252 276 LEU   A CB   
346  C  CG   . LEU   A 69  ? 0.0113 0.3288 0.5750 -0.0144 -0.0177 0.0529  276 LEU   A CG   
347  C  CD1  . LEU   A 69  ? 0.0064 0.3653 0.6403 0.0074  0.0016  0.0685  276 LEU   A CD1  
348  C  CD2  . LEU   A 69  ? 0.0493 0.5327 0.5676 -0.1363 0.0183  0.0333  276 LEU   A CD2  
349  N  N    . VAL   A 70  ? 0.0718 0.2981 0.4799 -0.0459 0.0188  -0.0156 277 VAL   A N    
350  C  CA   . VAL   A 70  ? 0.0788 0.3563 0.4793 0.0227  0.0483  -0.0283 277 VAL   A CA   
351  C  C    . VAL   A 70  ? 0.0483 0.3356 0.4173 -0.0015 0.0322  -0.0013 277 VAL   A C    
352  O  O    . VAL   A 70  ? 0.0623 0.4119 0.4855 -0.0990 -0.0262 0.0139  277 VAL   A O    
353  C  CB   . VAL   A 70  ? 0.1283 0.3465 0.5409 0.0164  0.0906  0.0108  277 VAL   A CB   
354  C  CG1  . VAL   A 70  ? 0.0807 0.4460 0.5501 -0.1105 0.1377  0.0771  277 VAL   A CG1  
355  C  CG2  . VAL   A 70  ? 0.1624 0.2898 0.6108 0.0194  0.1342  0.0685  277 VAL   A CG2  
356  N  N    . VAL   A 71  ? 0.0539 0.3184 0.5246 -0.0091 0.1070  -0.0349 278 VAL   A N    
357  C  CA   . VAL   A 71  ? 0.0512 0.3781 0.5556 0.0206  0.1088  -0.0365 278 VAL   A CA   
358  C  C    . VAL   A 71  ? 0.0483 0.3419 0.4870 -0.0767 0.0230  0.0227  278 VAL   A C    
359  O  O    . VAL   A 71  ? 0.1225 0.2429 0.5509 -0.0484 0.0063  -0.0508 278 VAL   A O    
360  C  CB   . VAL   A 71  ? 0.2636 0.2040 0.8427 -0.1370 0.1108  -0.0547 278 VAL   A CB   
361  C  CG1  . VAL   A 71  ? 0.2059 0.2661 0.7772 -0.1378 0.0834  0.0419  278 VAL   A CG1  
362  C  CG2  . VAL   A 71  ? 0.2292 0.5488 0.7715 -0.2240 0.0855  0.0145  278 VAL   A CG2  
363  N  N    . ILE   A 72  ? 0.0275 0.3329 0.4558 -0.0710 0.0512  -0.0013 279 ILE   A N    
364  C  CA   . ILE   A 72  ? 0.0286 0.3796 0.4833 -0.0748 0.0455  0.0635  279 ILE   A CA   
365  C  C    . ILE   A 72  ? 0.0370 0.3316 0.4710 -0.0428 0.0660  0.0330  279 ILE   A C    
366  O  O    . ILE   A 72  ? 0.0325 0.3057 0.4725 -0.0404 -0.0197 -0.0065 279 ILE   A O    
367  C  CB   . ILE   A 72  ? 0.0391 0.3694 0.4255 0.0006  0.0360  0.0209  279 ILE   A CB   
368  C  CG1  . ILE   A 72  ? 0.0411 0.3081 0.4181 -0.0427 0.0168  0.0231  279 ILE   A CG1  
369  C  CG2  . ILE   A 72  ? 0.0431 0.3736 0.5016 0.0100  0.0454  0.0583  279 ILE   A CG2  
370  C  CD1  . ILE   A 72  ? 0.1174 0.3600 0.4281 -0.0861 -0.0189 0.0465  279 ILE   A CD1  
371  N  N    . ILE   A 73  ? 0.0498 0.2437 0.4539 -0.0308 0.0428  0.0359  280 ILE   A N    
372  C  CA   . ILE   A 73  ? 0.0767 0.3062 0.4528 -0.0437 0.0232  0.0512  280 ILE   A CA   
373  C  C    . ILE   A 73  ? 0.0982 0.3284 0.4420 -0.0444 0.0372  0.0705  280 ILE   A C    
374  O  O    . ILE   A 73  ? 0.0971 0.3625 0.5495 -0.0694 0.0215  -0.0204 280 ILE   A O    
375  C  CB   . ILE   A 73  ? 0.1409 0.3939 0.4967 0.0048  0.0317  0.0372  280 ILE   A CB   
376  C  CG1  . ILE   A 73  ? 0.0499 0.3184 0.5217 -0.0185 -0.0049 -0.0326 280 ILE   A CG1  
377  C  CG2  . ILE   A 73  ? 0.2333 0.3835 0.5031 -0.0442 0.0690  0.0522  280 ILE   A CG2  
378  C  CD1  . ILE   A 73  ? 0.0074 0.4029 0.6436 -0.0065 0.0243  0.0088  280 ILE   A CD1  
379  N  N    . GLY   A 74  ? 0.0241 0.3637 0.5074 -0.0188 0.0883  0.0530  281 GLY   A N    
380  C  CA   . GLY   A 74  ? 0.1075 0.3488 0.5157 -0.0748 0.0736  0.0644  281 GLY   A CA   
381  C  C    . GLY   A 74  ? 0.1384 0.3678 0.4635 -0.0713 0.0767  0.0461  281 GLY   A C    
382  O  O    . GLY   A 74  ? 0.2760 0.3898 0.4515 -0.1124 -0.0544 0.0708  281 GLY   A O    
383  N  N    . TRP   A 75  ? 0.0693 0.2969 0.4456 -0.0099 0.0368  0.0506  282 TRP   A N    
384  C  CA   . TRP   A 75  ? 0.1315 0.2410 0.4408 -0.0557 0.0140  -0.0093 282 TRP   A CA   
385  C  C    . TRP   A 75  ? 0.1105 0.2046 0.5216 -0.0272 0.0183  0.0042  282 TRP   A C    
386  O  O    . TRP   A 75  ? 0.1939 0.2456 0.5255 0.0398  -0.0396 0.0679  282 TRP   A O    
387  C  CB   . TRP   A 75  ? 0.1895 0.2059 0.4783 -0.0354 -0.0231 -0.0124 282 TRP   A CB   
388  C  CG   . TRP   A 75  ? 0.0750 0.1560 0.5036 0.0128  -0.0162 0.0231  282 TRP   A CG   
389  C  CD1  . TRP   A 75  ? 0.2453 0.2240 0.4576 0.0501  -0.0454 -0.0480 282 TRP   A CD1  
390  C  CD2  . TRP   A 75  ? 0.0950 0.1926 0.5210 -0.0150 -0.0065 0.0476  282 TRP   A CD2  
391  N  NE1  . TRP   A 75  ? 0.0914 0.3152 0.5389 0.0548  -0.0481 0.0323  282 TRP   A NE1  
392  C  CE2  . TRP   A 75  ? 0.1153 0.3274 0.5415 -0.0032 -0.0176 0.0302  282 TRP   A CE2  
393  C  CE3  . TRP   A 75  ? 0.1910 0.2008 0.4873 -0.0348 -0.0477 0.0582  282 TRP   A CE3  
394  C  CZ2  . TRP   A 75  ? 0.0717 0.4494 0.6147 0.0681  -0.0369 0.1739  282 TRP   A CZ2  
395  C  CZ3  . TRP   A 75  ? 0.1557 0.2353 0.5187 -0.0396 -0.0403 0.1021  282 TRP   A CZ3  
396  C  CH2  . TRP   A 75  ? 0.0245 0.4071 0.6392 -0.0467 -0.0125 0.0560  282 TRP   A CH2  
397  N  N    . ALA   A 76  ? 0.0729 0.1965 0.5068 0.0006  0.0428  -0.0132 283 ALA   A N    
398  C  CA   . ALA   A 76  ? 0.0528 0.2416 0.4955 0.0029  0.0242  0.0365  283 ALA   A CA   
399  C  C    . ALA   A 76  ? 0.1063 0.3174 0.4863 -0.0035 0.0314  0.0783  283 ALA   A C    
400  O  O    . ALA   A 76  ? 0.0912 0.2719 0.5022 -0.0882 0.0215  -0.0219 283 ALA   A O    
401  C  CB   . ALA   A 76  ? 0.0107 0.2353 0.5306 0.0235  -0.0116 0.0183  283 ALA   A CB   
402  N  N    . LYS   A 77  ? 0.1435 0.3417 0.5049 -0.0530 0.0593  0.0677  284 LYS   A N    
403  C  CA   . LYS   A 77  ? 0.1551 0.3008 0.4928 -0.0954 0.0183  0.0413  284 LYS   A CA   
404  C  C    . LYS   A 77  ? 0.1371 0.3815 0.4612 -0.0671 -0.0311 0.0197  284 LYS   A C    
405  O  O    . LYS   A 77  ? 0.1403 0.4794 0.5909 -0.0712 -0.0743 0.1066  284 LYS   A O    
406  C  CB   . LYS   A 77  ? 0.1605 0.3937 0.5020 -0.0289 -0.0105 0.0335  284 LYS   A CB   
407  C  CG   . LYS   A 77  ? 0.0664 0.3776 0.7045 -0.0229 0.0035  0.0579  284 LYS   A CG   
408  C  CD   . LYS   A 77  ? 0.2026 0.3691 0.7938 -0.0756 0.1038  0.0474  284 LYS   A CD   
409  C  CE   . LYS   A 77  ? 0.2993 0.4879 0.8287 0.0542  0.0429  -0.0365 284 LYS   A CE   
410  N  NZ   . LYS   A 77  ? 0.3066 0.5158 0.7954 -0.0512 0.0154  -0.0704 284 LYS   A NZ   
411  N  N    . HIS   A 78  ? 0.1619 0.3178 0.4675 -0.0550 -0.0154 0.0277  285 HIS   A N    
412  C  CA   . HIS   A 78  ? 0.2247 0.3110 0.5277 -0.0317 0.0293  0.0850  285 HIS   A CA   
413  C  C    . HIS   A 78  ? 0.2507 0.1609 0.5763 -0.0555 0.0589  0.0829  285 HIS   A C    
414  O  O    . HIS   A 78  ? 0.3313 0.2403 0.6104 0.0371  0.0757  0.1405  285 HIS   A O    
415  C  CB   . HIS   A 78  ? 0.2326 0.2466 0.6019 0.0375  -0.0128 0.0731  285 HIS   A CB   
416  C  CG   . HIS   A 78  ? 0.3315 0.4192 0.6608 -0.0141 0.0418  0.1019  285 HIS   A CG   
417  N  ND1  . HIS   A 78  ? 0.1598 0.5579 0.7362 -0.0079 0.0574  0.1821  285 HIS   A ND1  
418  C  CD2  . HIS   A 78  ? 0.3338 0.4441 0.6714 -0.0519 0.1214  0.1136  285 HIS   A CD2  
419  C  CE1  . HIS   A 78  ? 0.2619 0.1801 0.8168 -0.0776 0.1446  0.0871  285 HIS   A CE1  
420  N  NE2  . HIS   A 78  ? 0.3221 0.4320 0.6038 -0.0351 0.0581  0.1113  285 HIS   A NE2  
421  N  N    . ILE   A 79  ? 0.2430 0.1485 0.5141 -0.0787 0.0624  0.0606  286 ILE   A N    
422  C  CA   . ILE   A 79  ? 0.1735 0.1288 0.5250 -0.0415 0.0468  0.0126  286 ILE   A CA   
423  C  C    . ILE   A 79  ? 0.1835 0.2109 0.5469 0.0550  -0.0228 0.0426  286 ILE   A C    
424  O  O    . ILE   A 79  ? 0.1867 0.3146 0.5859 -0.0427 -0.0440 -0.0130 286 ILE   A O    
425  C  CB   . ILE   A 79  ? 0.1508 0.1655 0.5273 -0.0385 0.0029  0.0086  286 ILE   A CB   
426  C  CG1  . ILE   A 79  ? 0.1689 0.2789 0.5529 -0.0692 -0.0263 0.0194  286 ILE   A CG1  
427  C  CG2  . ILE   A 79  ? 0.2332 0.1229 0.6374 -0.0224 0.0932  0.0188  286 ILE   A CG2  
428  C  CD1  . ILE   A 79  ? 0.3050 0.1975 0.5940 -0.1244 0.0062  -0.0030 286 ILE   A CD1  
429  N  N    . PRO   A 80  ? 0.2078 0.2534 0.6473 0.0680  0.0202  0.0222  287 PRO   A N    
430  C  CA   . PRO   A 80  ? 0.2790 0.1951 0.6835 0.1394  -0.0610 0.0558  287 PRO   A CA   
431  C  C    . PRO   A 80  ? 0.1631 0.2777 0.5901 0.0402  -0.0598 -0.0046 287 PRO   A C    
432  O  O    . PRO   A 80  ? 0.1721 0.3821 0.6385 0.0814  -0.0636 0.0621  287 PRO   A O    
433  C  CB   . PRO   A 80  ? 0.3427 0.2565 0.7210 0.1870  -0.0511 0.0199  287 PRO   A CB   
434  C  CG   . PRO   A 80  ? 0.3505 0.2601 0.8000 0.1959  -0.0103 -0.0454 287 PRO   A CG   
435  C  CD   . PRO   A 80  ? 0.0781 0.3905 0.7108 0.0389  0.0254  -0.0379 287 PRO   A CD   
436  N  N    . GLY   A 81  ? 0.0352 0.3274 0.5682 0.0459  0.0198  -0.0007 288 GLY   A N    
437  C  CA   . GLY   A 81  ? 0.0532 0.3673 0.6361 -0.0023 0.0492  0.0184  288 GLY   A CA   
438  C  C    . GLY   A 81  ? 0.0412 0.3377 0.5859 -0.0113 -0.0514 -0.0251 288 GLY   A C    
439  O  O    . GLY   A 81  ? 0.1440 0.3087 0.7823 -0.0924 -0.0565 0.0026  288 GLY   A O    
440  N  N    . PHE   A 82  ? 0.0310 0.3829 0.5462 -0.0611 -0.0224 0.0030  289 PHE   A N    
441  C  CA   . PHE   A 82  ? 0.0968 0.3195 0.6115 -0.0323 -0.0252 -0.0545 289 PHE   A CA   
442  C  C    . PHE   A 82  ? 0.1053 0.3760 0.5863 0.0575  -0.0751 0.0104  289 PHE   A C    
443  O  O    . PHE   A 82  ? 0.1942 0.4005 0.5945 -0.0477 0.0176  -0.0700 289 PHE   A O    
444  C  CB   . PHE   A 82  ? 0.1285 0.2008 0.5606 -0.0667 -0.0180 -0.0116 289 PHE   A CB   
445  C  CG   . PHE   A 82  ? 0.0792 0.2881 0.5043 -0.0297 -0.0186 0.0145  289 PHE   A CG   
446  C  CD1  . PHE   A 82  ? 0.1262 0.2612 0.5368 0.0255  0.0458  -0.0187 289 PHE   A CD1  
447  C  CD2  . PHE   A 82  ? 0.1857 0.0697 0.4907 0.0076  -0.0059 0.0038  289 PHE   A CD2  
448  C  CE1  . PHE   A 82  ? 0.1673 0.1378 0.5459 -0.0504 0.0184  0.1176  289 PHE   A CE1  
449  C  CE2  . PHE   A 82  ? 0.0179 0.2193 0.5353 0.0204  0.0000  0.0090  289 PHE   A CE2  
450  C  CZ   . PHE   A 82  ? 0.1427 0.2207 0.5192 -0.0389 -0.0075 -0.0085 289 PHE   A CZ   
451  N  N    . SER   A 83  ? 0.0741 0.3868 0.5877 -0.0253 0.0155  0.0027  290 SER   A N    
452  C  CA   . SER   A 83  ? 0.2055 0.3906 0.5484 0.0297  -0.0214 0.0495  290 SER   A CA   
453  C  C    . SER   A 83  ? 0.2368 0.4293 0.4792 0.0015  -0.0025 0.0350  290 SER   A C    
454  O  O    . SER   A 83  ? 0.2510 0.6477 0.4826 -0.0499 0.0061  -0.0574 290 SER   A O    
455  C  CB   . SER   A 83  ? 0.3686 0.4510 0.6008 -0.0588 0.1069  0.0753  290 SER   A CB   
456  O  OG   . SER   A 83  ? 0.4316 0.4386 0.7740 -0.1787 0.1792  -0.0173 290 SER   A OG   
457  N  N    . THR   A 84  ? 0.1548 0.4534 0.5700 0.0706  -0.0717 0.0563  291 THR   A N    
458  C  CA   . THR   A 84  ? 0.2520 0.4370 0.5464 0.0703  -0.1053 0.0220  291 THR   A CA   
459  C  C    . THR   A 84  ? 0.2496 0.4858 0.5419 -0.0388 -0.0780 -0.0090 291 THR   A C    
460  O  O    . THR   A 84  ? 0.2514 0.5022 0.6022 -0.0443 -0.1583 0.0554  291 THR   A O    
461  C  CB   . THR   A 84  ? 0.1888 0.6033 0.7737 0.0914  -0.0931 0.0391  291 THR   A CB   
462  O  OG1  . THR   A 84  ? 0.3004 0.7134 0.8790 0.1732  -0.1120 0.0219  291 THR   A OG1  
463  C  CG2  . THR   A 84  ? 0.2033 0.5542 0.6994 0.1459  -0.1024 0.1476  291 THR   A CG2  
464  N  N    . LEU   A 85  ? 0.2865 0.2873 0.4982 -0.0467 -0.0400 -0.0283 292 LEU   A N    
465  C  CA   . LEU   A 85  ? 0.2059 0.3154 0.5100 -0.0759 -0.0520 0.0086  292 LEU   A CA   
466  C  C    . LEU   A 85  ? 0.1848 0.3433 0.4961 -0.1585 -0.0518 -0.0750 292 LEU   A C    
467  O  O    . LEU   A 85  ? 0.2196 0.4239 0.4780 -0.0193 -0.0027 0.0613  292 LEU   A O    
468  C  CB   . LEU   A 85  ? 0.1369 0.2790 0.4930 0.0318  -0.0249 0.0379  292 LEU   A CB   
469  C  CG   . LEU   A 85  ? 0.1653 0.2726 0.5378 -0.0274 -0.0105 -0.0395 292 LEU   A CG   
470  C  CD1  . LEU   A 85  ? 0.2444 0.1479 0.5217 0.0505  -0.0159 -0.0710 292 LEU   A CD1  
471  C  CD2  . LEU   A 85  ? 0.2244 0.3639 0.6407 -0.0493 0.0790  0.0104  292 LEU   A CD2  
472  N  N    . SER   A 86  ? 0.1916 0.3183 0.5018 -0.0504 -0.0520 -0.0248 293 SER   A N    
473  C  CA   . SER   A 86  ? 0.1875 0.4334 0.5025 -0.0297 -0.0685 -0.1072 293 SER   A CA   
474  C  C    . SER   A 86  ? 0.1360 0.3677 0.5611 -0.1667 0.0358  -0.0340 293 SER   A C    
475  O  O    . SER   A 86  ? 0.2435 0.3850 0.5046 -0.0441 0.0007  0.0150  293 SER   A O    
476  C  CB   . SER   A 86  ? 0.2085 0.4235 0.6160 -0.0303 -0.0995 -0.0957 293 SER   A CB   
477  O  OG   . SER   A 86  ? 0.2655 0.4491 0.6021 -0.0320 -0.0769 -0.0993 293 SER   A OG   
478  N  N    . LEU   A 87  ? 0.2523 0.3790 0.5437 -0.0780 0.0369  -0.0481 294 LEU   A N    
479  C  CA   . LEU   A 87  ? 0.2703 0.3080 0.5590 0.0030  0.0041  -0.0262 294 LEU   A CA   
480  C  C    . LEU   A 87  ? 0.2625 0.3741 0.4408 -0.1313 0.0080  -0.0388 294 LEU   A C    
481  O  O    . LEU   A 87  ? 0.1367 0.3811 0.4881 -0.0393 -0.0002 -0.0939 294 LEU   A O    
482  C  CB   . LEU   A 87  ? 0.4098 0.3196 0.5247 -0.0035 0.0064  -0.0590 294 LEU   A CB   
483  C  CG   . LEU   A 87  ? 0.2649 0.1961 0.6611 0.1205  -0.0197 -0.0934 294 LEU   A CG   
484  C  CD1  . LEU   A 87  ? 0.3055 0.3420 0.6551 0.0356  -0.0672 -0.1337 294 LEU   A CD1  
485  C  CD2  . LEU   A 87  ? 0.3293 0.3476 0.5743 0.0014  0.0526  -0.0838 294 LEU   A CD2  
486  N  N    . ALA   A 88  ? 0.2097 0.2937 0.5084 -0.0613 -0.0286 -0.0960 295 ALA   A N    
487  C  CA   . ALA   A 88  ? 0.2260 0.3944 0.4893 -0.0995 0.0130  -0.0268 295 ALA   A CA   
488  C  C    . ALA   A 88  ? 0.2296 0.2951 0.4560 -0.0964 -0.0414 0.0136  295 ALA   A C    
489  O  O    . ALA   A 88  ? 0.1424 0.2495 0.4581 -0.0109 -0.0344 -0.0477 295 ALA   A O    
490  C  CB   . ALA   A 88  ? 0.2645 0.3111 0.4764 -0.0304 -0.0317 -0.1101 295 ALA   A CB   
491  N  N    . ASP   A 89  ? 0.1985 0.3489 0.5151 -0.0948 -0.0054 -0.0259 296 ASP   A N    
492  C  CA   . ASP   A 89  ? 0.1633 0.3517 0.5288 -0.1146 -0.0534 -0.0761 296 ASP   A CA   
493  C  C    . ASP   A 89  ? 0.0996 0.2338 0.4115 -0.0474 0.0315  -0.0790 296 ASP   A C    
494  O  O    . ASP   A 89  ? 0.1235 0.2230 0.4593 -0.0813 0.0157  -0.0364 296 ASP   A O    
495  C  CB   . ASP   A 89  ? 0.1786 0.3531 0.5494 -0.0462 -0.0456 -0.1143 296 ASP   A CB   
496  C  CG   . ASP   A 89  ? 0.1713 0.3979 0.6755 -0.0575 -0.0083 -0.1041 296 ASP   A CG   
497  O  OD1  . ASP   A 89  ? 0.2606 0.3414 0.6555 -0.1703 -0.0399 -0.1135 296 ASP   A OD1  
498  O  OD2  . ASP   A 89  ? 0.1619 0.4185 0.6756 -0.0063 0.0349  0.0027  296 ASP   A OD2  
499  N  N    . GLN   A 90  ? 0.0959 0.1972 0.4825 -0.0503 0.0239  -0.0357 297 GLN   A N    
500  C  CA   . GLN   A 90  ? 0.1051 0.2454 0.4778 -0.0486 -0.0132 -0.0899 297 GLN   A CA   
501  C  C    . GLN   A 90  ? 0.1162 0.2979 0.4073 -0.0262 0.0018  -0.1005 297 GLN   A C    
502  O  O    . GLN   A 90  ? 0.1758 0.1956 0.4372 -0.0492 -0.0258 -0.0718 297 GLN   A O    
503  C  CB   . GLN   A 90  ? 0.1127 0.3000 0.4540 -0.0268 -0.0362 -0.0562 297 GLN   A CB   
504  C  CG   . GLN   A 90  ? 0.0648 0.3041 0.4862 -0.0704 -0.0464 -0.0226 297 GLN   A CG   
505  C  CD   . GLN   A 90  ? 0.1038 0.3497 0.4351 -0.1009 -0.0139 -0.0656 297 GLN   A CD   
506  O  OE1  . GLN   A 90  ? 0.0689 0.3888 0.5623 -0.0750 -0.0176 0.0083  297 GLN   A OE1  
507  N  NE2  . GLN   A 90  ? 0.3043 0.3433 0.3928 -0.1362 -0.0648 -0.0110 297 GLN   A NE2  
508  N  N    . MET   A 91  ? 0.0773 0.2629 0.4729 -0.0428 -0.0094 -0.0670 298 MET   A N    
509  C  CA   . MET   A 91  ? 0.0505 0.1672 0.4918 -0.0599 0.0063  -0.0853 298 MET   A CA   
510  C  C    . MET   A 91  ? 0.0786 0.1895 0.4723 -0.0641 0.0128  -0.0523 298 MET   A C    
511  O  O    . MET   A 91  ? 0.1362 0.1858 0.4079 -0.0560 0.0346  -0.0604 298 MET   A O    
512  C  CB   . MET   A 91  ? 0.1309 0.2750 0.3916 -0.0203 -0.0363 -0.1177 298 MET   A CB   
513  C  CG   . MET   A 91  ? 0.2076 0.3452 0.4467 -0.0250 -0.0091 -0.0828 298 MET   A CG   
514  S  SD   . MET   A 91  ? 0.2806 0.4272 0.6330 -0.0031 0.0468  -0.1635 298 MET   A SD   
515  C  CE   . MET   A 91  ? 0.3818 0.4408 0.5667 -0.1601 -0.0503 -0.1099 298 MET   A CE   
516  N  N    . SER   A 92  ? 0.0960 0.2193 0.4874 -0.0888 0.0302  -0.0921 299 SER   A N    
517  C  CA   . SER   A 92  ? 0.0719 0.1789 0.5071 -0.0656 0.0620  -0.0778 299 SER   A CA   
518  C  C    . SER   A 92  ? 0.1070 0.1810 0.4040 -0.0337 0.0171  -0.0094 299 SER   A C    
519  O  O    . SER   A 92  ? 0.0916 0.1387 0.4344 -0.0577 -0.0288 0.0089  299 SER   A O    
520  C  CB   . SER   A 92  ? 0.1178 0.2745 0.4271 -0.1274 0.0162  -0.0875 299 SER   A CB   
521  O  OG   . SER   A 92  ? 0.2081 0.2047 0.5053 -0.0361 0.0152  -0.0794 299 SER   A OG   
522  N  N    . LEU   A 93  ? 0.0317 0.2115 0.4375 0.0141  -0.0243 -0.0164 300 LEU   A N    
523  C  CA   . LEU   A 93  ? 0.0646 0.1699 0.4706 -0.0260 -0.0205 -0.0236 300 LEU   A CA   
524  C  C    . LEU   A 93  ? 0.0668 0.1344 0.3992 -0.0011 -0.0129 -0.0917 300 LEU   A C    
525  O  O    . LEU   A 93  ? 0.0226 0.1747 0.4259 -0.0139 -0.0404 -0.0633 300 LEU   A O    
526  C  CB   . LEU   A 93  ? 0.0607 0.1782 0.5137 0.0657  0.0300  -0.0815 300 LEU   A CB   
527  C  CG   . LEU   A 93  ? 0.0968 0.1586 0.5889 0.0205  -0.0459 0.0092  300 LEU   A CG   
528  C  CD1  . LEU   A 93  ? 0.0097 0.1395 0.5938 -0.0102 0.0077  0.0016  300 LEU   A CD1  
529  C  CD2  . LEU   A 93  ? 0.0514 0.3711 0.6471 0.1282  0.0277  0.0903  300 LEU   A CD2  
530  N  N    . LEU   A 94  ? 0.0791 0.0963 0.4449 -0.0018 -0.0070 -0.0625 301 LEU   A N    
531  C  CA   . LEU   A 94  ? 0.0644 0.1661 0.4325 -0.0209 0.0336  -0.0284 301 LEU   A CA   
532  C  C    . LEU   A 94  ? 0.1483 0.1358 0.4097 0.0188  0.0265  -0.0922 301 LEU   A C    
533  O  O    . LEU   A 94  ? 0.0783 0.2167 0.4612 0.0074  0.0195  -0.0947 301 LEU   A O    
534  C  CB   . LEU   A 94  ? 0.1134 0.2035 0.4367 0.0442  0.0523  -0.0337 301 LEU   A CB   
535  C  CG   . LEU   A 94  ? 0.0532 0.2230 0.4455 0.0169  -0.0315 -0.0078 301 LEU   A CG   
536  C  CD1  . LEU   A 94  ? 0.1145 0.1954 0.4721 0.0052  0.0225  -0.0641 301 LEU   A CD1  
537  C  CD2  . LEU   A 94  ? 0.0619 0.1847 0.5150 -0.0935 0.0190  0.0273  301 LEU   A CD2  
538  N  N    . GLN   A 95  ? 0.1044 0.1265 0.5000 -0.0055 0.0225  -0.0684 302 GLN   A N    
539  C  CA   . GLN   A 95  ? 0.0896 0.1349 0.4882 0.0257  0.0651  -0.0875 302 GLN   A CA   
540  C  C    . GLN   A 95  ? 0.0418 0.1802 0.4723 -0.0164 0.0509  -0.0620 302 GLN   A C    
541  O  O    . GLN   A 95  ? 0.0797 0.1706 0.5379 -0.0079 -0.0042 -0.0366 302 GLN   A O    
542  C  CB   . GLN   A 95  ? 0.1520 0.1718 0.4866 0.0141  0.0273  -0.1210 302 GLN   A CB   
543  C  CG   . GLN   A 95  ? 0.2404 0.2653 0.5445 0.1131  0.0839  -0.1289 302 GLN   A CG   
544  C  CD   . GLN   A 95  ? 0.2648 0.2779 0.6665 0.1946  -0.0089 -0.1760 302 GLN   A CD   
545  O  OE1  . GLN   A 95  ? 0.5603 0.2759 0.8074 -0.0055 0.0359  -0.2173 302 GLN   A OE1  
546  N  NE2  . GLN   A 95  ? 0.3292 0.2505 0.7531 0.1619  0.1002  -0.1155 302 GLN   A NE2  
547  N  N    . SER   A 96  ? 0.0240 0.1455 0.4828 -0.0194 0.0124  -0.1098 303 SER   A N    
548  C  CA   . SER   A 96  ? 0.0521 0.1892 0.4783 -0.0093 -0.0087 -0.0707 303 SER   A CA   
549  C  C    . SER   A 96  ? 0.0109 0.1717 0.3836 -0.0137 -0.0119 -0.0194 303 SER   A C    
550  O  O    . SER   A 96  ? 0.1079 0.1914 0.4330 -0.0515 -0.0102 -0.0094 303 SER   A O    
551  C  CB   . SER   A 96  ? 0.0709 0.1272 0.5586 -0.0398 0.0237  -0.0541 303 SER   A CB   
552  O  OG   . SER   A 96  ? 0.1840 0.1590 0.5619 -0.1077 0.0512  -0.0746 303 SER   A OG   
553  N  N    . ALA   A 97  ? 0.0507 0.1692 0.4119 -0.0201 0.0134  -0.0341 304 ALA   A N    
554  C  CA   . ALA   A 97  ? 0.0167 0.1798 0.4351 -0.0011 0.0341  -0.0388 304 ALA   A CA   
555  C  C    . ALA   A 97  ? 0.0354 0.1756 0.3409 -0.0188 0.0314  -0.0074 304 ALA   A C    
556  O  O    . ALA   A 97  ? 0.0108 0.1789 0.4383 0.0275  -0.0170 -0.0622 304 ALA   A O    
557  C  CB   . ALA   A 97  ? 0.0598 0.1616 0.4046 0.0264  0.0066  -0.0868 304 ALA   A CB   
558  N  N    . TRP   A 98  ? 0.0091 0.1474 0.4364 -0.0160 0.0241  -0.0362 305 TRP   A N    
559  C  CA   . TRP   A 98  ? 0.0565 0.1530 0.4552 -0.0435 0.0438  0.0175  305 TRP   A CA   
560  C  C    . TRP   A 98  ? 0.0162 0.1491 0.4674 -0.0321 0.0333  0.0097  305 TRP   A C    
561  O  O    . TRP   A 98  ? 0.0079 0.1328 0.5336 -0.0134 -0.0114 0.0199  305 TRP   A O    
562  C  CB   . TRP   A 98  ? 0.0553 0.2212 0.5158 -0.0309 0.0275  -0.0084 305 TRP   A CB   
563  C  CG   . TRP   A 98  ? 0.1160 0.2118 0.5238 0.0170  0.0118  -0.0175 305 TRP   A CG   
564  C  CD1  . TRP   A 98  ? 0.0180 0.2186 0.5755 0.0344  -0.0152 -0.0829 305 TRP   A CD1  
565  C  CD2  . TRP   A 98  ? 0.0780 0.2087 0.5988 0.0196  0.0424  0.0374  305 TRP   A CD2  
566  N  NE1  . TRP   A 98  ? 0.1085 0.1248 0.6196 -0.0092 0.0013  -0.0291 305 TRP   A NE1  
567  C  CE2  . TRP   A 98  ? 0.0608 0.1785 0.6198 0.0215  0.0368  -0.0530 305 TRP   A CE2  
568  C  CE3  . TRP   A 98  ? 0.1710 0.1259 0.5802 0.0141  -0.0007 -0.0048 305 TRP   A CE3  
569  C  CZ2  . TRP   A 98  ? 0.1876 0.1257 0.6351 0.0250  0.0101  0.0847  305 TRP   A CZ2  
570  C  CZ3  . TRP   A 98  ? 0.1591 0.1909 0.5995 0.0371  0.0517  0.0793  305 TRP   A CZ3  
571  C  CH2  . TRP   A 98  ? 0.0435 0.1915 0.6814 0.0691  0.1171  0.0853  305 TRP   A CH2  
572  N  N    . MET   A 99  ? 0.0520 0.1245 0.4033 -0.0123 0.0227  -0.0196 306 MET   A N    
573  C  CA   . MET   A 99  ? 0.0509 0.0761 0.4227 -0.0307 -0.0070 -0.0063 306 MET   A CA   
574  C  C    . MET   A 99  ? 0.0244 0.1083 0.4085 -0.0177 0.0137  0.0064  306 MET   A C    
575  O  O    . MET   A 99  ? 0.0285 0.1648 0.5024 -0.0488 -0.0001 -0.0091 306 MET   A O    
576  C  CB   . MET   A 99  ? 0.0457 0.0862 0.4552 -0.0053 -0.0015 -0.0057 306 MET   A CB   
577  C  CG   . MET   A 99  ? 0.0186 0.1241 0.4997 0.0037  -0.0090 -0.0097 306 MET   A CG   
578  S  SD   . MET   A 99  ? 0.0126 0.2061 0.5325 -0.0034 -0.0088 0.0215  306 MET   A SD   
579  C  CE   . MET   A 99  ? 0.1176 0.2473 0.6395 0.0272  0.0576  -0.0343 306 MET   A CE   
580  N  N    . GLU   A 100 ? 0.0242 0.0928 0.4198 -0.0357 0.0077  -0.0349 307 GLU   A N    
581  C  CA   . GLU   A 100 ? 0.0176 0.1059 0.4563 -0.0240 0.0276  -0.0407 307 GLU   A CA   
582  C  C    . GLU   A 100 ? 0.0104 0.1698 0.3793 -0.0220 0.0234  -0.0229 307 GLU   A C    
583  O  O    . GLU   A 100 ? 0.0525 0.1341 0.4399 0.0046  -0.0491 -0.0390 307 GLU   A O    
584  C  CB   . GLU   A 100 ? 0.0235 0.0615 0.4603 -0.0189 0.0795  -0.0339 307 GLU   A CB   
585  C  CG   . GLU   A 100 ? 0.0940 0.0875 0.4665 -0.0227 0.0430  -0.0099 307 GLU   A CG   
586  C  CD   . GLU   A 100 ? 0.0800 0.1026 0.5619 0.0005  0.0281  0.0485  307 GLU   A CD   
587  O  OE1  . GLU   A 100 ? 0.0399 0.1919 0.6632 0.0118  0.0323  -0.0213 307 GLU   A OE1  
588  O  OE2  . GLU   A 100 ? 0.1278 0.1376 0.6323 -0.0444 -0.0417 0.0831  307 GLU   A OE2  
589  N  N    . ILE   A 101 ? 0.0188 0.1444 0.4088 0.0027  0.0153  0.0264  308 ILE   A N    
590  C  CA   . ILE   A 101 ? 0.0229 0.1344 0.4341 -0.0455 -0.0215 0.0243  308 ILE   A CA   
591  C  C    . ILE   A 101 ? 0.0123 0.1497 0.4542 -0.0183 -0.0414 0.0055  308 ILE   A C    
592  O  O    . ILE   A 101 ? 0.0434 0.1187 0.4754 -0.0115 -0.0367 0.0440  308 ILE   A O    
593  C  CB   . ILE   A 101 ? 0.0107 0.1411 0.4439 -0.0169 -0.0319 0.0048  308 ILE   A CB   
594  C  CG1  . ILE   A 101 ? 0.0159 0.2541 0.4534 -0.0354 -0.0519 0.0512  308 ILE   A CG1  
595  C  CG2  . ILE   A 101 ? 0.0459 0.2108 0.4963 -0.0458 -0.0685 0.0654  308 ILE   A CG2  
596  C  CD1  . ILE   A 101 ? 0.0468 0.3470 0.4910 0.0199  0.0198  0.0340  308 ILE   A CD1  
597  N  N    . LEU   A 102 ? 0.0349 0.1627 0.4450 -0.0031 -0.0496 0.0485  309 LEU   A N    
598  C  CA   . LEU   A 102 ? 0.0093 0.1640 0.4579 0.0177  -0.0113 0.0220  309 LEU   A CA   
599  C  C    . LEU   A 102 ? 0.0207 0.1123 0.4477 -0.0024 0.0032  0.0365  309 LEU   A C    
600  O  O    . LEU   A 102 ? 0.0353 0.1543 0.4801 -0.0413 -0.0096 0.0191  309 LEU   A O    
601  C  CB   . LEU   A 102 ? 0.0613 0.1439 0.4852 0.0119  0.0379  0.0138  309 LEU   A CB   
602  C  CG   . LEU   A 102 ? 0.0974 0.1112 0.5303 -0.0323 0.0145  -0.0335 309 LEU   A CG   
603  C  CD1  . LEU   A 102 ? 0.0579 0.1676 0.5956 0.0068  -0.1000 0.0103  309 LEU   A CD1  
604  C  CD2  . LEU   A 102 ? 0.0553 0.2090 0.6221 0.0008  0.0656  0.0480  309 LEU   A CD2  
605  N  N    . ILE   A 103 ? 0.0118 0.1256 0.4263 -0.0254 -0.0117 0.0203  310 ILE   A N    
606  C  CA   . ILE   A 103 ? 0.0524 0.1378 0.4140 -0.0022 0.0152  0.0526  310 ILE   A CA   
607  C  C    . ILE   A 103 ? 0.0606 0.1726 0.3850 0.0116  -0.0138 0.0154  310 ILE   A C    
608  O  O    . ILE   A 103 ? 0.0502 0.1326 0.4796 -0.0640 0.0080  0.0134  310 ILE   A O    
609  C  CB   . ILE   A 103 ? 0.0419 0.1512 0.4586 -0.0097 -0.0171 0.0727  310 ILE   A CB   
610  C  CG1  . ILE   A 103 ? 0.0717 0.1702 0.5049 0.0140  -0.0073 0.0407  310 ILE   A CG1  
611  C  CG2  . ILE   A 103 ? 0.1012 0.1837 0.4597 -0.0199 -0.0631 0.0773  310 ILE   A CG2  
612  C  CD1  . ILE   A 103 ? 0.2758 0.1452 0.5046 0.0523  0.0189  0.0410  310 ILE   A CD1  
613  N  N    . LEU   A 104 ? 0.0409 0.1653 0.4684 -0.0667 -0.0532 -0.0045 311 LEU   A N    
614  C  CA   . LEU   A 104 ? 0.0985 0.1975 0.4801 -0.0358 -0.0390 -0.0229 311 LEU   A CA   
615  C  C    . LEU   A 104 ? 0.1057 0.1623 0.4225 0.0022  -0.0047 -0.0152 311 LEU   A C    
616  O  O    . LEU   A 104 ? 0.0456 0.1120 0.4369 0.0047  -0.0185 -0.0232 311 LEU   A O    
617  C  CB   . LEU   A 104 ? 0.0683 0.2975 0.5045 -0.0633 -0.0293 -0.0393 311 LEU   A CB   
618  C  CG   . LEU   A 104 ? 0.1286 0.4936 0.4642 -0.1569 -0.0537 0.0224  311 LEU   A CG   
619  C  CD1  . LEU   A 104 ? 0.0550 0.7166 0.8662 -0.1774 0.0426  0.0746  311 LEU   A CD1  
620  C  CD2  . LEU   A 104 ? 0.1904 0.4129 0.5667 -0.0683 -0.1180 -0.0534 311 LEU   A CD2  
621  N  N    . GLY   A 105 ? 0.0917 0.1179 0.4612 0.0007  -0.0011 0.0232  312 GLY   A N    
622  C  CA   . GLY   A 105 ? 0.0300 0.1055 0.5180 0.0423  -0.0251 0.0619  312 GLY   A CA   
623  C  C    . GLY   A 105 ? 0.0944 0.1299 0.4525 0.0332  -0.0254 0.0634  312 GLY   A C    
624  O  O    . GLY   A 105 ? 0.0346 0.1530 0.5677 -0.0285 -0.0377 0.0183  312 GLY   A O    
625  N  N    . VAL   A 106 ? 0.0943 0.0514 0.4741 -0.0184 -0.0473 0.0420  313 VAL   A N    
626  C  CA   . VAL   A 106 ? 0.0688 0.1819 0.4797 -0.0527 -0.0348 0.0458  313 VAL   A CA   
627  C  C    . VAL   A 106 ? 0.0217 0.2152 0.4869 -0.0412 -0.0540 -0.0256 313 VAL   A C    
628  O  O    . VAL   A 106 ? 0.0590 0.1469 0.4662 -0.0161 -0.0934 0.0242  313 VAL   A O    
629  C  CB   . VAL   A 106 ? 0.1137 0.2216 0.4835 -0.0258 -0.0293 0.0943  313 VAL   A CB   
630  C  CG1  . VAL   A 106 ? 0.0793 0.2541 0.5780 0.0095  -0.0605 0.0543  313 VAL   A CG1  
631  C  CG2  . VAL   A 106 ? 0.1222 0.1230 0.5383 -0.0250 -0.0354 0.0718  313 VAL   A CG2  
632  N  N    . VAL   A 107 ? 0.0118 0.1754 0.4577 -0.0218 -0.0378 0.0272  314 VAL   A N    
633  C  CA   . VAL   A 107 ? 0.0693 0.1152 0.4734 -0.0436 -0.0363 -0.0275 314 VAL   A CA   
634  C  C    . VAL   A 107 ? 0.0942 0.1361 0.4298 -0.0225 -0.0244 0.0095  314 VAL   A C    
635  O  O    . VAL   A 107 ? 0.0874 0.1676 0.4622 -0.0961 0.0463  0.0003  314 VAL   A O    
636  C  CB   . VAL   A 107 ? 0.0939 0.1681 0.4861 -0.0481 0.0131  0.0196  314 VAL   A CB   
637  C  CG1  . VAL   A 107 ? 0.0612 0.1984 0.5022 0.0048  -0.0249 -0.0257 314 VAL   A CG1  
638  C  CG2  . VAL   A 107 ? 0.1167 0.1940 0.4962 -0.0608 0.0463  0.0636  314 VAL   A CG2  
639  N  N    . TYR   A 108 ? 0.0136 0.1220 0.4573 -0.0204 -0.0396 -0.0052 315 TYR   A N    
640  C  CA   . TYR   A 108 ? 0.1500 0.0950 0.4820 -0.0513 -0.0444 -0.0043 315 TYR   A CA   
641  C  C    . TYR   A 108 ? 0.0526 0.1742 0.4413 0.0015  -0.0323 -0.0244 315 TYR   A C    
642  O  O    . TYR   A 108 ? 0.0360 0.1035 0.5349 -0.0257 -0.0208 -0.0116 315 TYR   A O    
643  C  CB   . TYR   A 108 ? 0.1144 0.0593 0.5231 -0.0285 -0.0654 -0.0067 315 TYR   A CB   
644  C  CG   . TYR   A 108 ? 0.1548 0.0408 0.5265 -0.0321 -0.0060 -0.0582 315 TYR   A CG   
645  C  CD1  . TYR   A 108 ? 0.1881 0.1662 0.5251 0.0492  0.0180  -0.0195 315 TYR   A CD1  
646  C  CD2  . TYR   A 108 ? 0.1851 0.1459 0.5255 0.0366  0.0103  0.0188  315 TYR   A CD2  
647  C  CE1  . TYR   A 108 ? 0.1934 0.1664 0.5429 0.0352  -0.0103 0.0036  315 TYR   A CE1  
648  C  CE2  . TYR   A 108 ? 0.2575 0.1148 0.6474 0.0078  -0.0240 0.0008  315 TYR   A CE2  
649  C  CZ   . TYR   A 108 ? 0.2741 0.0187 0.5567 0.0017  -0.0604 0.0275  315 TYR   A CZ   
650  O  OH   . TYR   A 108 ? 0.3333 0.0324 0.7189 0.0379  -0.0863 -0.0298 315 TYR   A OH   
651  N  N    . ARG   A 109 ? 0.0197 0.1016 0.5030 -0.0341 0.0082  0.0431  316 ARG   A N    
652  C  CA   . ARG   A 109 ? 0.1064 0.1008 0.4781 -0.0898 0.0408  0.0428  316 ARG   A CA   
653  C  C    . ARG   A 109 ? 0.0692 0.1845 0.5049 -0.0812 -0.0122 0.0545  316 ARG   A C    
654  O  O    . ARG   A 109 ? 0.0874 0.1157 0.5987 -0.0458 0.0048  -0.0032 316 ARG   A O    
655  C  CB   . ARG   A 109 ? 0.1241 0.1716 0.4917 -0.0212 0.0081  -0.0113 316 ARG   A CB   
656  C  CG   . ARG   A 109 ? 0.2028 0.0704 0.4697 -0.0347 0.0487  0.0353  316 ARG   A CG   
657  C  CD   . ARG   A 109 ? 0.1022 0.2129 0.5301 0.0097  0.0037  0.0315  316 ARG   A CD   
658  N  NE   . ARG   A 109 ? 0.0532 0.2008 0.5540 -0.0193 -0.0298 -0.0290 316 ARG   A NE   
659  C  CZ   . ARG   A 109 ? 0.0770 0.1043 0.6033 -0.0322 -0.0508 0.0532  316 ARG   A CZ   
660  N  NH1  . ARG   A 109 ? 0.0681 0.2249 0.5434 -0.0219 -0.0388 0.0255  316 ARG   A NH1  
661  N  NH2  . ARG   A 109 ? 0.0581 0.0849 0.6315 -0.0481 -0.0450 0.0545  316 ARG   A NH2  
662  N  N    . SER   A 110 ? 0.0132 0.1493 0.5397 -0.0315 -0.0130 0.0580  317 SER   A N    
663  C  CA   . SER   A 110 ? 0.0843 0.1144 0.5319 -0.0837 -0.0038 0.0558  317 SER   A CA   
664  C  C    . SER   A 110 ? 0.0787 0.0816 0.5130 -0.0550 -0.0608 0.0536  317 SER   A C    
665  O  O    . SER   A 110 ? 0.1035 0.1675 0.4962 -0.0546 -0.0420 0.0164  317 SER   A O    
666  C  CB   . SER   A 110 ? 0.0528 0.0995 0.4682 -0.0317 -0.0175 0.0166  317 SER   A CB   
667  O  OG   . SER   A 110 ? 0.0552 0.1087 0.5025 -0.0433 -0.0035 -0.0019 317 SER   A OG   
668  N  N    . LEU   A 111 ? 0.1337 0.0787 0.5030 -0.0299 -0.1130 0.0259  318 LEU   A N    
669  C  CA   . LEU   A 111 ? 0.1877 0.0829 0.5298 -0.0675 -0.0706 -0.0154 318 LEU   A CA   
670  C  C    . LEU   A 111 ? 0.1495 0.1708 0.4554 -0.1084 -0.0379 -0.0218 318 LEU   A C    
671  O  O    . LEU   A 111 ? 0.2074 0.1567 0.4880 -0.0232 -0.0264 -0.0664 318 LEU   A O    
672  C  CB   . LEU   A 111 ? 0.1548 0.0890 0.5347 -0.0906 -0.0823 0.0176  318 LEU   A CB   
673  C  CG   . LEU   A 111 ? 0.3153 0.0286 0.6453 -0.0701 -0.0877 -0.0425 318 LEU   A CG   
674  C  CD1  . LEU   A 111 ? 0.3171 0.1700 0.5999 -0.0895 -0.1117 0.0049  318 LEU   A CD1  
675  C  CD2  . LEU   A 111 ? 0.3254 0.2085 0.5279 -0.0485 -0.0966 0.0283  318 LEU   A CD2  
676  N  N    . SER   A 112 ? 0.2067 0.0950 0.5756 -0.0976 0.0163  -0.0056 319 SER   A N    
677  C  CA   A SER   A 112 ? 0.1883 0.1898 0.6007 -0.1147 -0.0347 -0.0390 319 SER   A CA   
678  C  CA   B SER   A 112 ? 0.2068 0.1875 0.5962 -0.1060 -0.0524 -0.0398 319 SER   A CA   
679  C  C    . SER   A 112 ? 0.2168 0.1582 0.5931 -0.1189 -0.0617 -0.0768 319 SER   A C    
680  O  O    . SER   A 112 ? 0.2532 0.1370 0.8270 -0.1497 -0.0825 -0.1059 319 SER   A O    
681  C  CB   A SER   A 112 ? 0.1248 0.2115 0.6797 -0.1424 0.0432  -0.0205 319 SER   A CB   
682  C  CB   B SER   A 112 ? 0.1231 0.1630 0.6491 -0.0888 -0.0531 -0.0225 319 SER   A CB   
683  O  OG   A SER   A 112 ? 0.0841 0.1841 0.6771 -0.0621 0.0053  0.0381  319 SER   A OG   
684  O  OG   B SER   A 112 ? 0.1853 0.1788 0.6683 -0.0788 -0.1196 0.0161  319 SER   A OG   
685  N  N    . PHE   A 113 ? 0.1247 0.1841 0.6570 -0.0640 -0.0831 -0.0949 320 PHE   A N    
686  C  CA   . PHE   A 113 ? 0.0921 0.2949 0.5800 -0.1074 -0.0484 -0.0366 320 PHE   A CA   
687  C  C    . PHE   A 113 ? 0.1463 0.1939 0.5861 -0.0851 0.0101  -0.0956 320 PHE   A C    
688  O  O    . PHE   A 113 ? 0.1356 0.3089 0.6132 -0.1410 -0.0236 -0.0806 320 PHE   A O    
689  C  CB   . PHE   A 113 ? 0.1122 0.2504 0.6108 -0.0752 -0.0489 -0.0353 320 PHE   A CB   
690  C  CG   . PHE   A 113 ? 0.0940 0.1899 0.6729 -0.1118 -0.0654 0.0037  320 PHE   A CG   
691  C  CD1  . PHE   A 113 ? 0.1599 0.1433 0.6357 -0.1390 -0.0744 -0.0138 320 PHE   A CD1  
692  C  CD2  . PHE   A 113 ? 0.0850 0.2648 0.7163 -0.0940 -0.1168 0.0659  320 PHE   A CD2  
693  C  CE1  . PHE   A 113 ? 0.2565 0.2114 0.6516 -0.0327 0.0079  0.0093  320 PHE   A CE1  
694  C  CE2  . PHE   A 113 ? 0.2860 0.2291 0.7011 -0.0683 -0.0571 0.0290  320 PHE   A CE2  
695  C  CZ   . PHE   A 113 ? 0.2843 0.1267 0.6806 -0.1658 -0.0926 0.0023  320 PHE   A CZ   
696  N  N    . GLU   A 114 ? 0.1605 0.3272 0.6287 -0.1311 -0.0377 -0.0885 321 GLU   A N    
697  C  CA   . GLU   A 114 ? 0.3442 0.2285 0.6850 -0.1609 0.0285  -0.1138 321 GLU   A CA   
698  C  C    . GLU   A 114 ? 0.1545 0.3239 0.6187 -0.1517 -0.0463 -0.0389 321 GLU   A C    
699  O  O    . GLU   A 114 ? 0.1361 0.3867 0.7130 -0.1431 -0.0982 -0.0421 321 GLU   A O    
700  C  CB   . GLU   A 114 ? 0.4540 0.3562 0.6873 -0.1121 0.0448  -0.1646 321 GLU   A CB   
701  C  CG   . GLU   A 114 ? 0.5739 0.4215 0.7672 -0.0637 0.1035  -0.1460 321 GLU   A CG   
702  C  CD   . GLU   A 114 ? 0.9194 0.6550 0.9015 -0.1678 0.2195  -0.3252 321 GLU   A CD   
703  O  OE1  . GLU   A 114 ? 1.2844 0.7749 0.9454 -0.4137 0.1621  -0.1720 321 GLU   A OE1  
704  O  OE2  . GLU   A 114 ? 0.8590 0.8585 1.2579 -0.6361 0.1780  -0.1320 321 GLU   A OE2  
705  N  N    . ASP   A 115 ? 0.2200 0.2477 0.5723 -0.1154 0.0095  0.0023  322 ASP   A N    
706  C  CA   . ASP   A 115 ? 0.1955 0.2295 0.6353 -0.1273 -0.0786 -0.0528 322 ASP   A CA   
707  C  C    . ASP   A 115 ? 0.1683 0.2522 0.5632 0.0277  -0.0879 0.0736  322 ASP   A C    
708  O  O    . ASP   A 115 ? 0.2061 0.2114 0.6493 0.0536  -0.0833 0.0253  322 ASP   A O    
709  C  CB   . ASP   A 115 ? 0.3280 0.3830 0.6565 -0.1064 -0.1384 -0.0569 322 ASP   A CB   
710  C  CG   . ASP   A 115 ? 0.2869 0.5170 0.6628 -0.1393 -0.1298 -0.0236 322 ASP   A CG   
711  O  OD1  . ASP   A 115 ? 0.3091 0.5733 0.6890 -0.2001 0.0597  0.0619  322 ASP   A OD1  
712  O  OD2  . ASP   A 115 ? 0.5859 0.8613 0.6292 0.0271  -0.0954 -0.1724 322 ASP   A OD2  
713  N  N    . GLU   A 116 ? 0.1297 0.3241 0.5191 -0.0633 -0.0801 0.0741  323 GLU   A N    
714  C  CA   . GLU   A 116 ? 0.2476 0.3413 0.5565 -0.0762 -0.0033 0.0580  323 GLU   A CA   
715  C  C    . GLU   A 116 ? 0.1281 0.2310 0.5167 -0.1183 0.0529  0.0284  323 GLU   A C    
716  O  O    . GLU   A 116 ? 0.1624 0.1873 0.6714 -0.0937 -0.0762 0.0083  323 GLU   A O    
717  C  CB   . GLU   A 116 ? 0.1223 0.4153 0.6659 -0.1113 -0.0465 0.0163  323 GLU   A CB   
718  C  CG   . GLU   A 116 ? 0.2500 0.4949 0.6346 -0.0919 -0.0841 0.0607  323 GLU   A CG   
719  C  CD   . GLU   A 116 ? 0.3758 0.5287 0.6738 -0.1425 -0.0526 0.0881  323 GLU   A CD   
720  O  OE1  . GLU   A 116 ? 0.4580 0.4831 0.7502 -0.2413 -0.1662 0.0537  323 GLU   A OE1  
721  O  OE2  . GLU   A 116 ? 0.4021 0.9269 0.9224 -0.0260 -0.0228 -0.0133 323 GLU   A OE2  
722  N  N    . LEU   A 117 ? 0.1201 0.1620 0.5074 -0.0458 -0.0298 0.0503  324 LEU   A N    
723  C  CA   . LEU   A 117 ? 0.1180 0.0799 0.5057 -0.0321 -0.0496 0.0464  324 LEU   A CA   
724  C  C    . LEU   A 117 ? 0.1116 0.1272 0.5102 -0.0468 -0.0416 0.0196  324 LEU   A C    
725  O  O    . LEU   A 117 ? 0.0842 0.2062 0.5486 -0.0441 -0.0714 0.0054  324 LEU   A O    
726  C  CB   . LEU   A 117 ? 0.0973 0.0712 0.5752 0.0030  0.0265  0.0502  324 LEU   A CB   
727  C  CG   . LEU   A 117 ? 0.1120 0.1607 0.5983 -0.0630 -0.0032 0.0890  324 LEU   A CG   
728  C  CD1  . LEU   A 117 ? 0.0533 0.1494 0.5681 -0.0274 -0.0300 0.1196  324 LEU   A CD1  
729  C  CD2  . LEU   A 117 ? 0.0413 0.3090 0.5736 -0.1028 -0.0343 0.1179  324 LEU   A CD2  
730  N  N    . VAL   A 118 ? 0.0682 0.1410 0.5005 -0.0317 -0.0304 0.0060  325 VAL   A N    
731  C  CA   . VAL   A 118 ? 0.0483 0.2125 0.5048 -0.0014 -0.0188 0.0503  325 VAL   A CA   
732  C  C    . VAL   A 118 ? 0.1075 0.1590 0.5422 0.0376  -0.0766 0.0409  325 VAL   A C    
733  O  O    . VAL   A 118 ? 0.0546 0.1525 0.5212 0.0188  -0.0459 -0.0144 325 VAL   A O    
734  C  CB   . VAL   A 118 ? 0.0499 0.2071 0.5166 -0.0020 -0.0339 0.0018  325 VAL   A CB   
735  C  CG1  . VAL   A 118 ? 0.1753 0.1492 0.5747 -0.0676 0.0125  0.0159  325 VAL   A CG1  
736  C  CG2  . VAL   A 118 ? 0.1204 0.2268 0.4839 0.0244  -0.0606 0.0456  325 VAL   A CG2  
737  N  N    . TYR   A 119 ? 0.0570 0.1700 0.5418 0.0081  -0.0378 0.0123  326 TYR   A N    
738  C  CA   . TYR   A 119 ? 0.0134 0.1951 0.5440 -0.0173 0.0016  -0.0182 326 TYR   A CA   
739  C  C    . TYR   A 119 ? 0.0516 0.1796 0.5455 -0.0323 -0.0417 -0.0343 326 TYR   A C    
740  O  O    . TYR   A 119 ? 0.0641 0.2167 0.5381 -0.0243 -0.0259 -0.0016 326 TYR   A O    
741  C  CB   . TYR   A 119 ? 0.0904 0.1327 0.5375 -0.0222 -0.0230 -0.0561 326 TYR   A CB   
742  C  CG   . TYR   A 119 ? 0.0820 0.1737 0.4965 0.0404  0.0043  -0.0183 326 TYR   A CG   
743  C  CD1  . TYR   A 119 ? 0.0517 0.2723 0.5399 -0.0074 -0.0025 0.0157  326 TYR   A CD1  
744  C  CD2  . TYR   A 119 ? 0.1983 0.2322 0.5473 0.0749  -0.0930 -0.0328 326 TYR   A CD2  
745  C  CE1  . TYR   A 119 ? 0.0514 0.3178 0.5447 -0.0191 -0.0204 0.0642  326 TYR   A CE1  
746  C  CE2  . TYR   A 119 ? 0.0209 0.4289 0.6989 0.0121  -0.0817 0.0181  326 TYR   A CE2  
747  C  CZ   . TYR   A 119 ? 0.1377 0.3525 0.5236 -0.0714 -0.0014 0.0816  326 TYR   A CZ   
748  O  OH   . TYR   A 119 ? 0.1850 0.3474 0.6518 -0.0085 0.0727  0.1385  326 TYR   A OH   
749  N  N    . ALA   A 120 ? 0.0208 0.2481 0.5079 -0.0590 -0.0067 0.0616  327 ALA   A N    
750  C  CA   . ALA   A 120 ? 0.1989 0.2678 0.4993 -0.0058 0.0248  0.0529  327 ALA   A CA   
751  C  C    . ALA   A 120 ? 0.1304 0.2095 0.4067 0.0602  0.0277  0.0735  327 ALA   A C    
752  O  O    . ALA   A 120 ? 0.0664 0.2131 0.4399 -0.0420 0.0125  0.0242  327 ALA   A O    
753  C  CB   . ALA   A 120 ? 0.0747 0.2075 0.4725 -0.0183 -0.0103 0.0892  327 ALA   A CB   
754  N  N    . ASP   A 121 ? 0.1420 0.1591 0.5610 0.0060  -0.0181 0.0727  328 ASP   A N    
755  C  CA   . ASP   A 121 ? 0.1694 0.1068 0.6473 0.0819  -0.0407 0.0158  328 ASP   A CA   
756  C  C    . ASP   A 121 ? 0.1685 0.1739 0.5919 0.0200  -0.1037 0.0653  328 ASP   A C    
757  O  O    . ASP   A 121 ? 0.1627 0.2234 0.6038 -0.1138 -0.0048 0.0466  328 ASP   A O    
758  C  CB   . ASP   A 121 ? 0.3086 0.2024 0.7195 0.0007  -0.0082 0.1479  328 ASP   A CB   
759  C  CG   . ASP   A 121 ? 0.3098 0.3089 0.7006 0.0321  0.1225  0.0994  328 ASP   A CG   
760  O  OD1  . ASP   A 121 ? 0.2984 0.4127 0.6471 0.0807  0.1228  0.0388  328 ASP   A OD1  
761  O  OD2  . ASP   A 121 ? 0.5856 0.6807 0.9395 0.3013  -0.0342 0.2084  328 ASP   A OD2  
762  N  N    . ASP   A 122 ? 0.0683 0.2340 0.6645 -0.0635 -0.0017 0.0910  329 ASP   A N    
763  C  CA   . ASP   A 122 ? 0.0936 0.2579 0.6266 -0.0532 -0.0403 0.1195  329 ASP   A CA   
764  C  C    . ASP   A 122 ? 0.0465 0.2134 0.6604 -0.0421 0.0259  0.1076  329 ASP   A C    
765  O  O    . ASP   A 122 ? 0.0718 0.2225 0.6283 0.0016  -0.0307 0.1213  329 ASP   A O    
766  C  CB   . ASP   A 122 ? 0.0725 0.2403 0.5757 -0.0556 -0.0328 0.1543  329 ASP   A CB   
767  C  CG   . ASP   A 122 ? 0.0376 0.2641 0.5507 -0.0145 -0.0148 0.1149  329 ASP   A CG   
768  O  OD1  . ASP   A 122 ? 0.0194 0.2368 0.6519 0.0076  -0.0027 0.0458  329 ASP   A OD1  
769  O  OD2  . ASP   A 122 ? 0.1008 0.1892 0.5992 0.0235  0.0104  0.0939  329 ASP   A OD2  
770  N  N    . TYR   A 123 ? 0.0757 0.2770 0.6056 -0.1053 -0.0052 0.1012  330 TYR   A N    
771  C  CA   . TYR   A 123 ? 0.0146 0.3088 0.5236 -0.0494 -0.0278 0.1051  330 TYR   A CA   
772  C  C    . TYR   A 123 ? 0.0859 0.2371 0.4769 -0.0545 -0.0078 0.0825  330 TYR   A C    
773  O  O    . TYR   A 123 ? 0.0634 0.2129 0.5569 -0.0145 -0.0506 0.0973  330 TYR   A O    
774  C  CB   . TYR   A 123 ? 0.0367 0.2604 0.5255 0.0280  -0.0135 0.0601  330 TYR   A CB   
775  C  CG   . TYR   A 123 ? 0.0676 0.2831 0.5184 -0.0175 -0.0246 0.1697  330 TYR   A CG   
776  C  CD1  . TYR   A 123 ? 0.0633 0.2426 0.5839 -0.0891 0.0108  0.1187  330 TYR   A CD1  
777  C  CD2  . TYR   A 123 ? 0.0655 0.3135 0.6465 -0.0894 -0.0175 0.1778  330 TYR   A CD2  
778  C  CE1  . TYR   A 123 ? 0.1505 0.3117 0.5445 -0.0108 -0.0570 0.1009  330 TYR   A CE1  
779  C  CE2  . TYR   A 123 ? 0.0828 0.3426 0.6215 -0.0200 -0.0096 0.1232  330 TYR   A CE2  
780  C  CZ   . TYR   A 123 ? 0.0934 0.3203 0.6162 0.0349  -0.0143 0.1373  330 TYR   A CZ   
781  O  OH   . TYR   A 123 ? 0.1135 0.2142 0.6066 0.0094  -0.0369 0.0324  330 TYR   A OH   
782  N  N    . ILE   A 124 ? 0.0608 0.2425 0.4966 -0.0363 -0.0506 0.0935  331 ILE   A N    
783  C  CA   . ILE   A 124 ? 0.1582 0.2668 0.5240 -0.0078 -0.0452 0.0682  331 ILE   A CA   
784  C  C    . ILE   A 124 ? 0.0516 0.1947 0.5221 -0.0878 -0.0738 0.0584  331 ILE   A C    
785  O  O    . ILE   A 124 ? 0.0587 0.3497 0.5647 -0.0768 -0.1115 0.0352  331 ILE   A O    
786  C  CB   . ILE   A 124 ? 0.1997 0.2246 0.5512 -0.0845 -0.0135 0.0681  331 ILE   A CB   
787  C  CG1  . ILE   A 124 ? 0.1332 0.2841 0.5911 0.0343  -0.0281 0.0282  331 ILE   A CG1  
788  C  CG2  . ILE   A 124 ? 0.2243 0.2095 0.6385 -0.0898 0.0811  0.0614  331 ILE   A CG2  
789  C  CD1  . ILE   A 124 ? 0.1738 0.3224 0.6528 0.0096  0.0031  -0.0388 331 ILE   A CD1  
790  N  N    . MET   A 125 ? 0.1051 0.2281 0.6067 -0.1126 -0.0071 0.0770  332 MET   A N    
791  C  CA   . MET   A 125 ? 0.0452 0.3081 0.5773 -0.0546 -0.0435 0.0764  332 MET   A CA   
792  C  C    . MET   A 125 ? 0.1165 0.1725 0.5586 -0.0424 -0.0467 0.1097  332 MET   A C    
793  O  O    . MET   A 125 ? 0.1168 0.2976 0.6200 -0.0282 -0.0754 0.0291  332 MET   A O    
794  C  CB   . MET   A 125 ? 0.1293 0.3345 0.5230 -0.0687 -0.0512 0.0308  332 MET   A CB   
795  C  CG   . MET   A 125 ? 0.2277 0.1968 0.5789 0.0524  0.0463  0.1258  332 MET   A CG   
796  S  SD   . MET   A 125 ? 0.2359 0.2307 0.7304 -0.0250 0.0463  0.0793  332 MET   A SD   
797  C  CE   . MET   A 125 ? 0.2327 0.1981 0.6071 -0.0103 0.0072  0.0642  332 MET   A CE   
798  N  N    . ASP   A 126 ? 0.1738 0.2953 0.5984 -0.0999 -0.0989 0.0216  333 ASP   A N    
799  C  CA   . ASP   A 126 ? 0.2341 0.4205 0.5774 -0.1019 -0.1382 0.0969  333 ASP   A CA   
800  C  C    . ASP   A 126 ? 0.1142 0.4011 0.5488 -0.0787 -0.0963 0.0625  333 ASP   A C    
801  O  O    . ASP   A 126 ? 0.1388 0.4041 0.5771 0.0067  -0.0961 0.0667  333 ASP   A O    
802  C  CB   . ASP   A 126 ? 0.3381 0.3357 0.6615 -0.2014 -0.0193 0.1261  333 ASP   A CB   
803  C  CG   . ASP   A 126 ? 0.3179 0.5834 0.7730 -0.1895 -0.1352 0.1087  333 ASP   A CG   
804  O  OD1  . ASP   A 126 ? 0.1533 0.7036 0.7895 0.0284  -0.1220 0.0487  333 ASP   A OD1  
805  O  OD2  . ASP   A 126 ? 0.2834 0.9771 0.9163 -0.2215 -0.1639 -0.0180 333 ASP   A OD2  
806  N  N    . GLU   A 127 ? 0.2624 0.3324 0.5859 -0.0886 -0.1030 0.0659  334 GLU   A N    
807  C  CA   . GLU   A 127 ? 0.2974 0.4381 0.6365 -0.0272 0.0058  0.2087  334 GLU   A CA   
808  C  C    . GLU   A 127 ? 0.2503 0.4684 0.6734 -0.0716 -0.0339 0.1511  334 GLU   A C    
809  O  O    . GLU   A 127 ? 0.1812 0.4315 0.5899 -0.0170 -0.0311 0.1423  334 GLU   A O    
810  C  CB   . GLU   A 127 ? 0.3627 0.5538 0.6761 -0.1424 0.0406  0.0897  334 GLU   A CB   
811  C  CG   . GLU   A 127 ? 0.4792 0.5929 0.7552 -0.1549 0.0786  0.1037  334 GLU   A CG   
812  C  CD   . GLU   A 127 ? 0.8072 0.9435 0.6613 -0.1807 0.0566  -0.0076 334 GLU   A CD   
813  O  OE1  . GLU   A 127 ? 0.3363 1.2972 0.7513 -0.1311 -0.0564 0.1505  334 GLU   A OE1  
814  O  OE2  . GLU   A 127 ? 0.9825 1.2151 0.8192 -0.4339 0.3279  -0.0464 334 GLU   A OE2  
815  N  N    . ASP   A 128 ? 0.2050 0.2744 0.8370 0.0286  -0.0411 0.0924  335 ASP   A N    
816  C  CA   . ASP   A 128 ? 0.2198 0.3904 0.7266 0.0836  -0.0860 0.0822  335 ASP   A CA   
817  C  C    . ASP   A 128 ? 0.1605 0.4639 0.6700 -0.0580 -0.1120 0.1839  335 ASP   A C    
818  O  O    . ASP   A 128 ? 0.2720 0.6008 0.7969 0.0386  -0.1502 -0.0092 335 ASP   A O    
819  C  CB   . ASP   A 128 ? 0.3470 0.3026 0.7474 -0.0166 0.0251  0.0266  335 ASP   A CB   
820  C  CG   . ASP   A 128 ? 0.5470 0.4633 0.7731 -0.1079 -0.0035 0.0706  335 ASP   A CG   
821  O  OD1  . ASP   A 128 ? 0.5275 0.8033 0.9230 -0.2530 -0.2650 0.3443  335 ASP   A OD1  
822  O  OD2  . ASP   A 128 ? 0.6791 0.3525 1.1156 0.0293  0.0407  -0.0607 335 ASP   A OD2  
823  N  N    . GLN   A 129 ? 0.1176 0.4065 0.6305 -0.0366 -0.0182 0.1419  336 GLN   A N    
824  C  CA   . GLN   A 129 ? 0.0200 0.4874 0.6253 -0.0483 -0.0838 0.1112  336 GLN   A CA   
825  C  C    . GLN   A 129 ? 0.0344 0.4153 0.6125 -0.0467 0.0050  0.0598  336 GLN   A C    
826  O  O    . GLN   A 129 ? 0.1490 0.3543 0.6374 0.0180  -0.0326 0.0964  336 GLN   A O    
827  C  CB   . GLN   A 129 ? 0.1719 0.3584 0.7653 -0.0400 -0.0176 0.0882  336 GLN   A CB   
828  C  CG   . GLN   A 129 ? 0.2425 0.4498 0.7619 -0.1221 0.1111  0.1561  336 GLN   A CG   
829  C  CD   . GLN   A 129 ? 0.5875 0.4254 0.8945 -0.1386 -0.0735 0.1142  336 GLN   A CD   
830  O  OE1  . GLN   A 129 ? 0.8433 0.2901 1.1215 -0.2663 -0.1452 0.0497  336 GLN   A OE1  
831  N  NE2  . GLN   A 129 ? 0.0674 1.1087 0.9759 -0.0517 -0.0599 0.3996  336 GLN   A NE2  
832  N  N    . SER   A 130 ? 0.1013 0.3692 0.4851 -0.0143 0.0217  0.1202  337 SER   A N    
833  C  CA   . SER   A 130 ? 0.0596 0.3409 0.6313 0.0122  -0.0190 0.1165  337 SER   A CA   
834  C  C    . SER   A 130 ? 0.1667 0.4026 0.5442 0.0686  -0.0208 0.1454  337 SER   A C    
835  O  O    . SER   A 130 ? 0.1272 0.3946 0.6641 0.0283  0.0607  0.0781  337 SER   A O    
836  C  CB   . SER   A 130 ? 0.1007 0.2433 0.6267 0.0344  0.0014  0.0586  337 SER   A CB   
837  O  OG   . SER   A 130 ? 0.2033 0.2501 0.6990 -0.0647 -0.0255 0.1451  337 SER   A OG   
838  N  N    . LYS   A 131 ? 0.1211 0.4904 0.6037 0.0451  -0.0565 0.1307  338 LYS   A N    
839  C  CA   . LYS   A 131 ? 0.1740 0.3875 0.7352 0.0772  -0.0271 0.0684  338 LYS   A CA   
840  C  C    . LYS   A 131 ? 0.3291 0.3016 0.7100 0.1153  -0.0212 0.0885  338 LYS   A C    
841  O  O    . LYS   A 131 ? 0.2889 0.2739 0.7853 0.1488  0.0330  0.1083  338 LYS   A O    
842  C  CB   . LYS   A 131 ? 0.4460 0.5428 0.7295 -0.0438 -0.0540 0.0237  338 LYS   A CB   
843  C  CG   . LYS   A 131 ? 0.5895 0.6965 0.8406 -0.1597 0.0113  0.1146  338 LYS   A CG   
844  C  CD   . LYS   A 131 ? 0.7219 1.0209 0.8841 -0.2249 -0.1175 -0.0542 338 LYS   A CD   
845  C  CE   . LYS   A 131 ? 0.8723 1.3270 0.9915 -0.0887 0.0607  -0.2646 338 LYS   A CE   
846  N  NZ   . LYS   A 131 ? 0.6140 1.3641 0.9329 -0.0637 0.0729  -0.2450 338 LYS   A NZ   
847  N  N    . LEU   A 132 ? 0.2135 0.4189 0.7193 0.1157  -0.1191 0.1358  339 LEU   A N    
848  C  CA   . LEU   A 132 ? 0.0676 0.5510 0.9046 0.0265  -0.0504 0.1013  339 LEU   A CA   
849  C  C    . LEU   A 132 ? 0.1648 0.4709 0.7645 0.1837  -0.0253 0.1917  339 LEU   A C    
850  O  O    . LEU   A 132 ? 0.3302 0.5903 0.8374 0.2470  -0.0044 0.1138  339 LEU   A O    
851  C  CB   . LEU   A 132 ? 0.2345 0.5897 0.9031 0.0182  0.0249  0.2116  339 LEU   A CB   
852  C  CG   . LEU   A 132 ? 0.2285 0.8881 1.0432 -0.0243 -0.0604 0.2148  339 LEU   A CG   
853  C  CD1  . LEU   A 132 ? 0.2872 1.0627 0.9796 -0.2402 0.0149  0.2714  339 LEU   A CD1  
854  C  CD2  . LEU   A 132 ? 0.4717 1.0172 0.8976 0.1304  -0.0957 0.2989  339 LEU   A CD2  
855  N  N    . ALA   A 133 ? 0.0956 0.2530 0.7991 0.0630  -0.0430 0.1072  340 ALA   A N    
856  C  CA   . ALA   A 133 ? 0.2253 0.2794 0.7523 0.0629  -0.0152 0.0960  340 ALA   A CA   
857  C  C    . ALA   A 133 ? 0.1080 0.3913 0.6718 0.0550  0.1017  0.1508  340 ALA   A C    
858  O  O    . ALA   A 133 ? 0.1387 0.3853 0.6723 0.1901  0.0305  0.0832  340 ALA   A O    
859  C  CB   . ALA   A 133 ? 0.1711 0.2317 0.7279 -0.0256 0.0145  0.1527  340 ALA   A CB   
860  N  N    . GLY   A 134 ? 0.1256 0.4512 0.6703 0.1037  0.0715  0.1551  341 GLY   A N    
861  C  CA   . GLY   A 134 ? 0.2356 0.3273 0.6796 0.1759  0.1374  0.2247  341 GLY   A CA   
862  C  C    . GLY   A 134 ? 0.1541 0.2568 0.7189 0.0162  0.0865  0.2297  341 GLY   A C    
863  O  O    . GLY   A 134 ? 0.1766 0.2637 0.6898 0.0513  0.0751  0.1247  341 GLY   A O    
864  N  N    . LEU   A 135 ? 0.0743 0.2671 0.7352 -0.0138 -0.0293 0.1520  342 LEU   A N    
865  C  CA   . LEU   A 135 ? 0.0682 0.1950 0.6766 0.0000  0.0542  0.1136  342 LEU   A CA   
866  C  C    . LEU   A 135 ? 0.1159 0.3741 0.5944 0.0785  0.0136  0.1187  342 LEU   A C    
867  O  O    . LEU   A 135 ? 0.1068 0.3684 0.5713 0.0779  0.0018  0.1266  342 LEU   A O    
868  C  CB   . LEU   A 135 ? 0.1604 0.3195 0.6483 0.1634  0.0959  0.1792  342 LEU   A CB   
869  C  CG   . LEU   A 135 ? 0.0916 0.3050 0.6706 0.0990  0.0556  0.1243  342 LEU   A CG   
870  C  CD1  . LEU   A 135 ? 0.1333 0.4657 0.6824 0.1473  -0.0130 0.2197  342 LEU   A CD1  
871  C  CD2  . LEU   A 135 ? 0.0533 0.4018 0.6959 0.0812  0.0615  0.1310  342 LEU   A CD2  
872  N  N    . LEU   A 136 ? 0.1533 0.2156 0.6064 0.0454  0.0045  0.1208  343 LEU   A N    
873  C  CA   . LEU   A 136 ? 0.2453 0.3885 0.5965 0.0498  0.0753  0.0679  343 LEU   A CA   
874  C  C    . LEU   A 136 ? 0.2886 0.2327 0.5405 -0.0054 0.0972  0.0189  343 LEU   A C    
875  O  O    . LEU   A 136 ? 0.3209 0.2898 0.5901 0.0968  0.0603  0.0587  343 LEU   A O    
876  C  CB   . LEU   A 136 ? 0.4319 0.3937 0.5988 0.0431  0.0536  0.1318  343 LEU   A CB   
877  C  CG   . LEU   A 136 ? 0.5733 0.5118 0.6618 -0.0902 0.0230  0.0727  343 LEU   A CG   
878  C  CD1  . LEU   A 136 ? 0.6344 0.4837 0.6960 -0.0395 0.0844  0.0102  343 LEU   A CD1  
879  C  CD2  . LEU   A 136 ? 0.7425 0.6072 0.8093 -0.0991 -0.0574 0.2077  343 LEU   A CD2  
880  N  N    . ASP   A 137 ? 0.1892 0.1817 0.7110 0.0510  0.0558  0.1060  344 ASP   A N    
881  C  CA   . ASP   A 137 ? 0.2182 0.2759 0.6757 0.0542  0.1135  0.0844  344 ASP   A CA   
882  C  C    . ASP   A 137 ? 0.1845 0.1985 0.6175 0.0712  0.1197  0.0567  344 ASP   A C    
883  O  O    . ASP   A 137 ? 0.1582 0.2515 0.6783 0.0893  0.0823  0.0400  344 ASP   A O    
884  C  CB   . ASP   A 137 ? 0.3114 0.2864 0.7207 -0.0022 0.0191  0.1589  344 ASP   A CB   
885  C  CG   . ASP   A 137 ? 0.4949 0.4296 0.7506 0.1086  -0.0378 0.1275  344 ASP   A CG   
886  O  OD1  . ASP   A 137 ? 0.4922 0.5757 0.7342 0.0577  -0.0641 0.1137  344 ASP   A OD1  
887  O  OD2  . ASP   A 137 ? 0.6663 0.4755 0.9534 0.2286  0.2242  0.2457  344 ASP   A OD2  
888  N  N    . LEU   A 138 ? 0.2312 0.2386 0.5504 0.0206  0.0212  0.0861  345 LEU   A N    
889  C  CA   . LEU   A 138 ? 0.2439 0.1155 0.4991 -0.0681 0.0441  0.1027  345 LEU   A CA   
890  C  C    . LEU   A 138 ? 0.1047 0.1161 0.6217 -0.0472 0.0049  0.0886  345 LEU   A C    
891  O  O    . LEU   A 138 ? 0.1042 0.2629 0.5710 0.0037  0.0204  0.0649  345 LEU   A O    
892  C  CB   . LEU   A 138 ? 0.2146 0.3255 0.5414 -0.0464 0.0521  0.0301  345 LEU   A CB   
893  C  CG   . LEU   A 138 ? 0.0920 0.3763 0.5535 0.0304  -0.0363 -0.0427 345 LEU   A CG   
894  C  CD1  . LEU   A 138 ? 0.0946 0.5999 0.5807 0.0357  -0.0643 -0.0491 345 LEU   A CD1  
895  C  CD2  . LEU   A 138 ? 0.2173 0.4787 0.5763 -0.0225 -0.0758 -0.1075 345 LEU   A CD2  
896  N  N    . ASN   A 139 ? 0.1002 0.2100 0.5699 -0.0138 -0.0439 -0.0213 346 ASN   A N    
897  C  CA   . ASN   A 139 ? 0.1698 0.1824 0.5749 0.0425  -0.0033 -0.0126 346 ASN   A CA   
898  C  C    . ASN   A 139 ? 0.0825 0.1720 0.4923 -0.0925 -0.0133 0.0557  346 ASN   A C    
899  O  O    . ASN   A 139 ? 0.1977 0.1246 0.5685 -0.0819 -0.0446 0.0469  346 ASN   A O    
900  C  CB   . ASN   A 139 ? 0.1960 0.2207 0.5480 0.0049  -0.0363 0.0078  346 ASN   A CB   
901  C  CG   . ASN   A 139 ? 0.1332 0.1805 0.5412 0.0786  -0.0742 0.0699  346 ASN   A CG   
902  O  OD1  . ASN   A 139 ? 0.2522 0.3113 0.5161 0.0674  -0.0963 0.0087  346 ASN   A OD1  
903  N  ND2  . ASN   A 139 ? 0.1450 0.2448 0.6451 0.0981  0.0466  0.0501  346 ASN   A ND2  
904  N  N    . ASN   A 140 ? 0.1590 0.1377 0.4600 -0.0149 -0.0022 0.0242  347 ASN   A N    
905  C  CA   . ASN   A 140 ? 0.1237 0.1895 0.4941 0.0031  -0.0238 0.0238  347 ASN   A CA   
906  C  C    . ASN   A 140 ? 0.1219 0.2335 0.4490 -0.0983 -0.0256 -0.0173 347 ASN   A C    
907  O  O    . ASN   A 140 ? 0.1836 0.1430 0.5715 -0.0632 -0.0075 0.0252  347 ASN   A O    
908  C  CB   . ASN   A 140 ? 0.3008 0.2175 0.6019 0.1070  -0.0362 0.0757  347 ASN   A CB   
909  C  CG   . ASN   A 140 ? 0.3193 0.3472 0.6624 0.0864  -0.0584 0.0170  347 ASN   A CG   
910  O  OD1  . ASN   A 140 ? 0.6684 0.2967 0.8633 0.1529  -0.1504 -0.1046 347 ASN   A OD1  
911  N  ND2  . ASN   A 140 ? 0.4713 0.1769 0.7425 0.0815  0.0410  0.0029  347 ASN   A ND2  
912  N  N    . ALA   A 141 ? 0.2572 0.1134 0.4477 -0.0488 -0.0213 0.0128  348 ALA   A N    
913  C  CA   . ALA   A 141 ? 0.2820 0.2271 0.4964 -0.0866 -0.0460 0.0077  348 ALA   A CA   
914  C  C    . ALA   A 141 ? 0.1083 0.1353 0.5478 -0.1105 -0.0341 -0.0022 348 ALA   A C    
915  O  O    . ALA   A 141 ? 0.1120 0.1905 0.5237 -0.0577 -0.0302 0.0294  348 ALA   A O    
916  C  CB   . ALA   A 141 ? 0.2338 0.1546 0.5448 -0.0778 -0.0597 0.0484  348 ALA   A CB   
917  N  N    . ILE   A 142 ? 0.0956 0.2064 0.4803 0.0432  -0.0276 0.0675  349 ILE   A N    
918  C  CA   . ILE   A 142 ? 0.0696 0.1553 0.4636 -0.0159 -0.0280 0.0459  349 ILE   A CA   
919  C  C    . ILE   A 142 ? 0.1477 0.2035 0.4026 0.0010  -0.0443 0.0497  349 ILE   A C    
920  O  O    . ILE   A 142 ? 0.1404 0.1586 0.4706 -0.0208 -0.0574 0.0486  349 ILE   A O    
921  C  CB   . ILE   A 142 ? 0.1553 0.2167 0.3950 -0.0016 -0.0315 0.0072  349 ILE   A CB   
922  C  CG1  . ILE   A 142 ? 0.2152 0.2061 0.4390 0.0844  -0.0274 -0.0043 349 ILE   A CG1  
923  C  CG2  . ILE   A 142 ? 0.1456 0.2862 0.4311 0.0370  -0.0309 0.0722  349 ILE   A CG2  
924  C  CD1  . ILE   A 142 ? 0.3158 0.2013 0.4570 0.0649  0.0435  0.0201  349 ILE   A CD1  
925  N  N    . LEU   A 143 ? 0.1448 0.1898 0.4221 -0.0582 -0.0440 -0.0044 350 LEU   A N    
926  C  CA   . LEU   A 143 ? 0.1194 0.1112 0.4917 -0.0946 -0.0360 0.0181  350 LEU   A CA   
927  C  C    . LEU   A 143 ? 0.1120 0.1051 0.5057 -0.0876 -0.0502 -0.0012 350 LEU   A C    
928  O  O    . LEU   A 143 ? 0.0484 0.1643 0.5592 -0.0429 -0.0075 -0.0137 350 LEU   A O    
929  C  CB   . LEU   A 143 ? 0.0867 0.1090 0.5676 -0.0517 -0.0264 -0.0001 350 LEU   A CB   
930  C  CG   . LEU   A 143 ? 0.1272 0.1349 0.5707 0.0425  0.0802  -0.0348 350 LEU   A CG   
931  C  CD1  . LEU   A 143 ? 0.1193 0.2412 0.6192 0.0680  0.0679  -0.0012 350 LEU   A CD1  
932  C  CD2  . LEU   A 143 ? 0.0574 0.1333 0.6422 0.0133  0.0076  -0.0205 350 LEU   A CD2  
933  N  N    . GLN   A 144 ? 0.0557 0.0978 0.5159 -0.0649 -0.0394 -0.0021 351 GLN   A N    
934  C  CA   . GLN   A 144 ? 0.1529 0.0624 0.5633 -0.0440 0.0408  0.0061  351 GLN   A CA   
935  C  C    . GLN   A 144 ? 0.1423 0.1280 0.4953 -0.1286 0.0239  -0.0311 351 GLN   A C    
936  O  O    . GLN   A 144 ? 0.1524 0.1680 0.4980 -0.0640 0.0102  -0.0031 351 GLN   A O    
937  C  CB   . GLN   A 144 ? 0.2240 0.0759 0.5596 -0.0939 0.0418  0.0023  351 GLN   A CB   
938  C  CG   . GLN   A 144 ? 0.1866 0.2138 0.5671 -0.0405 -0.0068 0.0442  351 GLN   A CG   
939  C  CD   . GLN   A 144 ? 0.4283 0.1898 0.6303 0.0142  -0.0344 0.0709  351 GLN   A CD   
940  O  OE1  . GLN   A 144 ? 0.5176 0.1608 0.7317 -0.0683 0.1317  0.0473  351 GLN   A OE1  
941  N  NE2  . GLN   A 144 ? 0.2829 0.1822 0.6497 0.0415  -0.0562 0.0316  351 GLN   A NE2  
942  N  N    . LEU   A 145 ? 0.0849 0.1455 0.4472 -0.0584 -0.0077 0.0025  352 LEU   A N    
943  C  CA   . LEU   A 145 ? 0.0362 0.1372 0.4752 -0.0622 0.0089  0.0096  352 LEU   A CA   
944  C  C    . LEU   A 145 ? 0.0499 0.1330 0.4934 -0.0627 0.0052  0.0316  352 LEU   A C    
945  O  O    . LEU   A 145 ? 0.1522 0.0940 0.4976 -0.0132 -0.0284 0.0339  352 LEU   A O    
946  C  CB   . LEU   A 145 ? 0.0711 0.1639 0.5574 -0.0333 0.0383  -0.0184 352 LEU   A CB   
947  C  CG   . LEU   A 145 ? 0.0828 0.1481 0.6122 -0.0466 0.0091  0.0219  352 LEU   A CG   
948  C  CD1  . LEU   A 145 ? 0.1388 0.1767 0.6478 -0.0313 0.0146  0.0136  352 LEU   A CD1  
949  C  CD2  . LEU   A 145 ? 0.1311 0.2757 0.6659 -0.0195 -0.1423 0.0492  352 LEU   A CD2  
950  N  N    . VAL   A 146 ? 0.0650 0.0944 0.4844 -0.0698 -0.0374 -0.0030 353 VAL   A N    
951  C  CA   . VAL   A 146 ? 0.0792 0.0673 0.4819 -0.0262 -0.0380 -0.0071 353 VAL   A CA   
952  C  C    . VAL   A 146 ? 0.0262 0.1361 0.4709 -0.0507 -0.0188 0.0341  353 VAL   A C    
953  O  O    . VAL   A 146 ? 0.1410 0.0859 0.5636 -0.0495 -0.0503 -0.0108 353 VAL   A O    
954  C  CB   . VAL   A 146 ? 0.0788 0.1048 0.5048 -0.0436 -0.0783 -0.0053 353 VAL   A CB   
955  C  CG1  . VAL   A 146 ? 0.1296 0.0828 0.5957 -0.0328 -0.0066 -0.0036 353 VAL   A CG1  
956  C  CG2  . VAL   A 146 ? 0.1363 0.1730 0.4861 -0.0880 -0.0451 0.0549  353 VAL   A CG2  
957  N  N    . LYS   A 147 ? 0.2020 0.0355 0.5173 -0.0184 -0.0661 0.0450  354 LYS   A N    
958  C  CA   . LYS   A 147 ? 0.0886 0.1273 0.5075 -0.0156 -0.0300 0.0141  354 LYS   A CA   
959  C  C    . LYS   A 147 ? 0.1032 0.2232 0.5197 0.0220  -0.0387 -0.0643 354 LYS   A C    
960  O  O    . LYS   A 147 ? 0.1787 0.1025 0.4857 -0.0137 -0.0224 0.0170  354 LYS   A O    
961  C  CB   . LYS   A 147 ? 0.2232 0.1749 0.5629 -0.0457 0.0184  0.0707  354 LYS   A CB   
962  C  CG   . LYS   A 147 ? 0.2983 0.3486 0.5490 0.0308  -0.0500 0.0723  354 LYS   A CG   
963  C  CD   . LYS   A 147 ? 0.7284 0.5834 0.5189 0.1525  -0.0478 0.1619  354 LYS   A CD   
964  C  CE   . LYS   A 147 ? 1.1054 0.7502 0.5690 0.1231  -0.0815 0.0200  354 LYS   A CE   
965  N  NZ   . LYS   A 147 ? 1.3085 0.8566 0.7257 0.3197  -0.0047 0.0736  354 LYS   A NZ   
966  N  N    . LYS   A 148 ? 0.0958 0.1912 0.4933 -0.0327 0.0063  0.0058  355 LYS   A N    
967  C  CA   . LYS   A 148 ? 0.0855 0.1014 0.4744 -0.0755 0.0080  0.0155  355 LYS   A CA   
968  C  C    . LYS   A 148 ? 0.0291 0.2075 0.4539 -0.0257 -0.0116 0.0289  355 LYS   A C    
969  O  O    . LYS   A 148 ? 0.1003 0.1604 0.4940 -0.0214 -0.0283 -0.0259 355 LYS   A O    
970  C  CB   . LYS   A 148 ? 0.0853 0.0919 0.5042 -0.0795 -0.0103 0.0628  355 LYS   A CB   
971  C  CG   . LYS   A 148 ? 0.0857 0.0909 0.6056 0.0069  -0.0087 0.0454  355 LYS   A CG   
972  C  CD   . LYS   A 148 ? 0.1870 0.1061 0.6393 -0.0142 -0.0842 0.0600  355 LYS   A CD   
973  C  CE   . LYS   A 148 ? 0.1321 0.1030 0.6357 -0.0870 -0.0571 0.1169  355 LYS   A CE   
974  N  NZ   . LYS   A 148 ? 0.1700 0.1123 0.5384 -0.0679 -0.0055 0.0704  355 LYS   A NZ   
975  N  N    . TYR   A 149 ? 0.1647 0.1300 0.4181 -0.0493 -0.0305 -0.0125 356 TYR   A N    
976  C  CA   . TYR   A 149 ? 0.1051 0.1685 0.4142 -0.0504 -0.0644 -0.0334 356 TYR   A CA   
977  C  C    . TYR   A 149 ? 0.1422 0.0546 0.4511 -0.0145 -0.0113 0.0280  356 TYR   A C    
978  O  O    . TYR   A 149 ? 0.1879 0.0506 0.5197 0.0230  -0.0477 -0.0443 356 TYR   A O    
979  C  CB   . TYR   A 149 ? 0.0848 0.0777 0.4474 -0.0538 -0.0305 -0.0410 356 TYR   A CB   
980  C  CG   . TYR   A 149 ? 0.1141 0.0607 0.4086 -0.0647 -0.0211 -0.0245 356 TYR   A CG   
981  C  CD1  . TYR   A 149 ? 0.1096 0.0803 0.4872 0.0188  0.0319  -0.0560 356 TYR   A CD1  
982  C  CD2  . TYR   A 149 ? 0.0697 0.0518 0.4430 -0.0174 0.0076  0.0253  356 TYR   A CD2  
983  C  CE1  . TYR   A 149 ? 0.0614 0.0984 0.4822 -0.0551 0.0485  -0.0099 356 TYR   A CE1  
984  C  CE2  . TYR   A 149 ? 0.0412 0.1131 0.4488 -0.0274 0.0138  -0.0017 356 TYR   A CE2  
985  C  CZ   . TYR   A 149 ? 0.0444 0.0997 0.4479 -0.0188 -0.0020 0.0152  356 TYR   A CZ   
986  O  OH   . TYR   A 149 ? 0.0942 0.1058 0.4763 -0.0361 -0.0259 0.0004  356 TYR   A OH   
987  N  N    . LYS   A 150 ? 0.1735 0.0854 0.5015 -0.0036 -0.0420 -0.0200 357 LYS   A N    
988  C  CA   . LYS   A 150 ? 0.2599 0.0518 0.5342 -0.0253 -0.0601 0.0131  357 LYS   A CA   
989  C  C    . LYS   A 150 ? 0.2149 0.1160 0.4694 -0.0441 -0.1170 -0.0041 357 LYS   A C    
990  O  O    . LYS   A 150 ? 0.2674 0.1036 0.5605 -0.0486 -0.0518 0.0103  357 LYS   A O    
991  C  CB   . LYS   A 150 ? 0.2526 0.1735 0.5255 0.0091  -0.0590 -0.0390 357 LYS   A CB   
992  C  CG   . LYS   A 150 ? 0.2644 0.2217 0.5670 -0.0211 -0.0536 -0.0641 357 LYS   A CG   
993  C  CD   . LYS   A 150 ? 0.4396 0.2384 0.6758 0.0195  -0.1826 0.0486  357 LYS   A CD   
994  C  CE   . LYS   A 150 ? 0.2765 0.5228 0.6976 -0.1056 -0.1784 -0.0821 357 LYS   A CE   
995  N  NZ   . LYS   A 150 ? 0.2617 0.9451 0.8236 0.0409  -0.1668 -0.1635 357 LYS   A NZ   
996  N  N    . SER   A 151 ? 0.3042 0.1900 0.4498 -0.0391 -0.0557 0.0034  358 SER   A N    
997  C  CA   . SER   A 151 ? 0.2817 0.1815 0.4686 0.0032  -0.0764 0.0268  358 SER   A CA   
998  C  C    . SER   A 151 ? 0.2050 0.1496 0.4642 0.0559  -0.0263 -0.0684 358 SER   A C    
999  O  O    . SER   A 151 ? 0.2331 0.1721 0.6001 0.0705  -0.0040 -0.1058 358 SER   A O    
1000 C  CB   . SER   A 151 ? 0.3615 0.0760 0.6212 -0.0457 -0.1192 0.0739  358 SER   A CB   
1001 O  OG   . SER   A 151 ? 0.4636 0.3928 0.6676 -0.2309 -0.0510 -0.0112 358 SER   A OG   
1002 N  N    . MET   A 152 ? 0.2310 0.0939 0.4624 -0.0977 -0.0170 -0.0252 359 MET   A N    
1003 C  CA   . MET   A 152 ? 0.1558 0.1647 0.5072 -0.0320 0.0403  -0.0084 359 MET   A CA   
1004 C  C    . MET   A 152 ? 0.0748 0.1756 0.4318 -0.0651 0.0437  -0.0444 359 MET   A C    
1005 O  O    . MET   A 152 ? 0.2567 0.1785 0.5233 -0.0332 -0.0459 -0.0063 359 MET   A O    
1006 C  CB   . MET   A 152 ? 0.1446 0.2829 0.5225 0.0110  -0.0080 -0.0620 359 MET   A CB   
1007 C  CG   . MET   A 152 ? 0.2791 0.2446 0.5962 -0.0123 0.0159  -0.0692 359 MET   A CG   
1008 S  SD   . MET   A 152 ? 0.2638 0.1854 0.6618 -0.0230 0.0105  -0.0497 359 MET   A SD   
1009 C  CE   . MET   A 152 ? 0.1686 0.2006 0.8304 -0.0925 0.0719  0.0654  359 MET   A CE   
1010 N  N    . LYS   A 153 ? 0.0682 0.1927 0.5640 -0.0626 0.0082  -0.0220 360 LYS   A N    
1011 C  CA   . LYS   A 153 ? 0.2126 0.1625 0.5096 -0.0019 -0.0129 -0.0096 360 LYS   A CA   
1012 C  C    . LYS   A 153 ? 0.1361 0.0688 0.4922 -0.0019 -0.0002 -0.0466 360 LYS   A C    
1013 O  O    . LYS   A 153 ? 0.1231 0.1002 0.5185 -0.0162 -0.0258 -0.0071 360 LYS   A O    
1014 C  CB   . LYS   A 153 ? 0.0667 0.2373 0.6412 -0.0147 0.0118  -0.1178 360 LYS   A CB   
1015 C  CG   . LYS   A 153 ? 0.2327 0.2426 0.6576 0.0507  -0.0957 -0.0585 360 LYS   A CG   
1016 C  CD   . LYS   A 153 ? 0.3114 0.3781 0.7492 0.0313  -0.0211 -0.2484 360 LYS   A CD   
1017 C  CE   . LYS   A 153 ? 0.5283 0.4742 0.7600 -0.0116 -0.1707 -0.2052 360 LYS   A CE   
1018 N  NZ   . LYS   A 153 ? 0.6746 0.6890 0.9383 -0.1889 -0.1945 -0.1159 360 LYS   A NZ   
1019 N  N    . LEU   A 154 ? 0.0875 0.0573 0.4762 -0.0162 0.0186  -0.0377 361 LEU   A N    
1020 C  CA   . LEU   A 154 ? 0.0991 0.0898 0.4667 -0.0231 -0.0233 -0.0157 361 LEU   A CA   
1021 C  C    . LEU   A 154 ? 0.1439 0.0931 0.4617 -0.0370 -0.0272 -0.0254 361 LEU   A C    
1022 O  O    . LEU   A 154 ? 0.1083 0.1243 0.5551 -0.0096 -0.0123 0.0247  361 LEU   A O    
1023 C  CB   . LEU   A 154 ? 0.1094 0.1241 0.4749 0.0160  -0.0009 0.0033  361 LEU   A CB   
1024 C  CG   . LEU   A 154 ? 0.1520 0.0309 0.5052 -0.0089 -0.0448 -0.0147 361 LEU   A CG   
1025 C  CD1  . LEU   A 154 ? 0.1560 0.0302 0.5236 -0.0077 -0.0123 0.0344  361 LEU   A CD1  
1026 C  CD2  . LEU   A 154 ? 0.1669 0.0491 0.5403 -0.0206 0.0348  -0.0243 361 LEU   A CD2  
1027 N  N    . GLU   A 155 ? 0.0879 0.1363 0.4476 -0.0615 0.0023  0.0042  362 GLU   A N    
1028 C  CA   . GLU   A 155 ? 0.1675 0.0352 0.4785 0.0184  0.0116  0.0136  362 GLU   A CA   
1029 C  C    . GLU   A 155 ? 0.2009 0.0152 0.4234 -0.0389 -0.0518 0.0087  362 GLU   A C    
1030 O  O    . GLU   A 155 ? 0.0674 0.0073 0.5221 -0.0076 0.0035  -0.0072 362 GLU   A O    
1031 C  CB   . GLU   A 155 ? 0.1128 0.1141 0.5105 -0.0088 0.0401  0.0144  362 GLU   A CB   
1032 C  CG   . GLU   A 155 ? 0.1166 0.0579 0.5728 -0.0046 0.1149  0.0017  362 GLU   A CG   
1033 C  CD   . GLU   A 155 ? 0.1236 0.1889 0.5936 0.0623  0.0242  0.0129  362 GLU   A CD   
1034 O  OE1  . GLU   A 155 ? 0.1459 0.2615 0.6121 -0.0254 0.0418  0.0694  362 GLU   A OE1  
1035 O  OE2  . GLU   A 155 ? 0.2419 0.1269 0.6995 -0.0424 0.0568  -0.0363 362 GLU   A OE2  
1036 N  N    . LYS   A 156 ? 0.1349 0.1229 0.4479 -0.0020 -0.0437 0.0588  363 LYS   A N    
1037 C  CA   . LYS   A 156 ? 0.0605 0.1062 0.4888 -0.0112 -0.0315 0.0544  363 LYS   A CA   
1038 C  C    . LYS   A 156 ? 0.0671 0.1916 0.3964 -0.0412 0.0228  -0.0196 363 LYS   A C    
1039 O  O    . LYS   A 156 ? 0.0577 0.1028 0.4835 0.0030  -0.0383 0.0306  363 LYS   A O    
1040 C  CB   . LYS   A 156 ? 0.0801 0.1137 0.5430 -0.0632 -0.0331 0.0460  363 LYS   A CB   
1041 C  CG   . LYS   A 156 ? 0.2455 0.3132 0.5066 -0.1660 0.0105  -0.0049 363 LYS   A CG   
1042 C  CD   . LYS   A 156 ? 0.3216 0.3631 0.7138 -0.1941 0.1120  0.0083  363 LYS   A CD   
1043 C  CE   . LYS   A 156 ? 0.2382 0.7338 0.7473 -0.1335 0.1110  -0.0597 363 LYS   A CE   
1044 N  NZ   . LYS   A 156 ? 0.1345 0.9140 0.8766 -0.1486 0.0787  0.0631  363 LYS   A NZ   
1045 N  N    . GLU   A 157 ? 0.1018 0.1185 0.4622 -0.0522 -0.0076 0.0443  364 GLU   A N    
1046 C  CA   . GLU   A 157 ? 0.0933 0.1012 0.4669 -0.0506 0.0011  0.0166  364 GLU   A CA   
1047 C  C    . GLU   A 157 ? 0.0923 0.0887 0.3767 0.0205  -0.0249 0.0629  364 GLU   A C    
1048 O  O    . GLU   A 157 ? 0.1276 0.1458 0.5032 -0.0168 0.0097  0.0046  364 GLU   A O    
1049 C  CB   . GLU   A 157 ? 0.1550 0.1429 0.4689 0.0044  0.0017  -0.0025 364 GLU   A CB   
1050 C  CG   . GLU   A 157 ? 0.1158 0.2337 0.5570 -0.0465 0.0109  0.0723  364 GLU   A CG   
1051 C  CD   . GLU   A 157 ? 0.2809 0.1015 0.6032 -0.0905 -0.0140 0.1189  364 GLU   A CD   
1052 O  OE1  . GLU   A 157 ? 0.2179 0.1251 0.5518 -0.0503 0.0088  -0.0233 364 GLU   A OE1  
1053 O  OE2  . GLU   A 157 ? 0.2683 0.0699 0.7016 -0.0486 0.0062  0.1197  364 GLU   A OE2  
1054 N  N    . GLU   A 158 ? 0.0731 0.0914 0.3796 -0.0491 -0.0110 -0.0080 365 GLU   A N    
1055 C  CA   . GLU   A 158 ? 0.0241 0.0714 0.4664 -0.0120 0.0068  0.0082  365 GLU   A CA   
1056 C  C    . GLU   A 158 ? 0.0630 0.0267 0.4473 -0.0171 -0.0029 0.0151  365 GLU   A C    
1057 O  O    . GLU   A 158 ? 0.0838 0.0576 0.4988 -0.0622 0.0456  -0.0125 365 GLU   A O    
1058 C  CB   . GLU   A 158 ? 0.0800 0.0426 0.4795 -0.0099 -0.0134 -0.0342 365 GLU   A CB   
1059 C  CG   . GLU   A 158 ? 0.1006 0.0845 0.4572 0.0254  0.0648  0.0369  365 GLU   A CG   
1060 C  CD   . GLU   A 158 ? 0.1078 0.2309 0.4538 0.0066  -0.0028 0.0855  365 GLU   A CD   
1061 O  OE1  . GLU   A 158 ? 0.0873 0.1086 0.4762 0.0156  -0.0023 0.0245  365 GLU   A OE1  
1062 O  OE2  . GLU   A 158 ? 0.0599 0.2121 0.5175 -0.0565 -0.0061 0.0247  365 GLU   A OE2  
1063 N  N    . PHE   A 159 ? 0.0638 0.0654 0.4445 -0.0168 -0.0063 0.0386  366 PHE   A N    
1064 C  CA   . PHE   A 159 ? 0.0174 0.0854 0.4569 -0.0136 -0.0498 0.0353  366 PHE   A CA   
1065 C  C    . PHE   A 159 ? 0.0503 0.1331 0.4238 -0.0004 -0.0434 0.0639  366 PHE   A C    
1066 O  O    . PHE   A 159 ? 0.0660 0.1577 0.4772 -0.0106 -0.0324 0.0107  366 PHE   A O    
1067 C  CB   . PHE   A 159 ? 0.0644 0.0711 0.4489 -0.0606 -0.0050 0.0314  366 PHE   A CB   
1068 C  CG   . PHE   A 159 ? 0.2089 0.0762 0.4421 -0.0292 0.0375  -0.0371 366 PHE   A CG   
1069 C  CD1  . PHE   A 159 ? 0.0957 0.1086 0.5696 -0.0313 0.0310  0.0165  366 PHE   A CD1  
1070 C  CD2  . PHE   A 159 ? 0.2353 0.1022 0.4602 0.0356  0.0291  0.0075  366 PHE   A CD2  
1071 C  CE1  . PHE   A 159 ? 0.0687 0.1197 0.5682 0.0384  -0.0347 0.0118  366 PHE   A CE1  
1072 C  CE2  . PHE   A 159 ? 0.1423 0.1621 0.5466 -0.0119 0.0279  -0.0096 366 PHE   A CE2  
1073 C  CZ   . PHE   A 159 ? 0.1077 0.2206 0.5440 0.1288  0.0527  -0.0158 366 PHE   A CZ   
1074 N  N    . VAL   A 160 ? 0.0412 0.1166 0.4306 0.0029  -0.0156 0.0567  367 VAL   A N    
1075 C  CA   . VAL   A 160 ? 0.0313 0.1063 0.4434 0.0062  -0.0383 0.0640  367 VAL   A CA   
1076 C  C    . VAL   A 160 ? 0.0341 0.1576 0.3709 -0.0071 -0.0365 0.0233  367 VAL   A C    
1077 O  O    . VAL   A 160 ? 0.0782 0.1104 0.4425 0.0045  -0.0017 0.0273  367 VAL   A O    
1078 C  CB   . VAL   A 160 ? 0.0776 0.0842 0.4640 -0.0388 0.0183  0.0350  367 VAL   A CB   
1079 C  CG1  . VAL   A 160 ? 0.0789 0.0717 0.4720 -0.0378 0.0061  0.0236  367 VAL   A CG1  
1080 C  CG2  . VAL   A 160 ? 0.1510 0.1772 0.4864 0.0391  0.0377  0.0471  367 VAL   A CG2  
1081 N  N    . THR   A 161 ? 0.0776 0.0960 0.4692 -0.0446 0.0345  0.0299  368 THR   A N    
1082 C  CA   . THR   A 161 ? 0.0782 0.0846 0.4431 -0.0401 0.0034  0.0363  368 THR   A CA   
1083 C  C    . THR   A 161 ? 0.0924 0.0988 0.3412 0.0069  -0.0055 0.0277  368 THR   A C    
1084 O  O    . THR   A 161 ? 0.0257 0.1387 0.4116 -0.0079 -0.0190 0.0227  368 THR   A O    
1085 C  CB   . THR   A 161 ? 0.0596 0.0982 0.4328 -0.0424 -0.0020 0.0435  368 THR   A CB   
1086 O  OG1  . THR   A 161 ? 0.0526 0.0965 0.5092 -0.0260 -0.0269 0.0693  368 THR   A OG1  
1087 C  CG2  . THR   A 161 ? 0.0435 0.0955 0.5683 -0.0498 0.0673  0.0092  368 THR   A CG2  
1088 N  N    . LEU   A 162 ? 0.1177 0.0595 0.3794 0.0094  0.0017  0.0568  369 LEU   A N    
1089 C  CA   . LEU   A 162 ? 0.1198 0.0494 0.3948 -0.0637 0.0145  0.0453  369 LEU   A CA   
1090 C  C    . LEU   A 162 ? 0.0655 0.0977 0.3819 -0.0687 0.0237  0.0376  369 LEU   A C    
1091 O  O    . LEU   A 162 ? 0.0266 0.0735 0.4996 -0.0140 -0.0035 0.0118  369 LEU   A O    
1092 C  CB   . LEU   A 162 ? 0.1135 0.0675 0.3641 -0.0327 0.0147  0.0142  369 LEU   A CB   
1093 C  CG   . LEU   A 162 ? 0.1473 0.1279 0.3597 -0.0248 0.0534  0.0707  369 LEU   A CG   
1094 C  CD1  . LEU   A 162 ? 0.0556 0.2516 0.5024 -0.0050 -0.0007 0.0449  369 LEU   A CD1  
1095 C  CD2  . LEU   A 162 ? 0.1613 0.1094 0.4416 -0.0449 -0.0061 0.0469  369 LEU   A CD2  
1096 N  N    . LYS   A 163 ? 0.0231 0.1458 0.4069 -0.0446 0.0315  -0.0001 370 LYS   A N    
1097 C  CA   . LYS   A 163 ? 0.1449 0.1706 0.3387 -0.0116 0.0508  0.0259  370 LYS   A CA   
1098 C  C    . LYS   A 163 ? 0.0706 0.1150 0.4003 0.0245  0.0002  0.0582  370 LYS   A C    
1099 O  O    . LYS   A 163 ? 0.0753 0.1435 0.4620 -0.0207 -0.0054 -0.0068 370 LYS   A O    
1100 C  CB   . LYS   A 163 ? 0.1105 0.1279 0.5010 -0.0669 0.0044  0.0293  370 LYS   A CB   
1101 C  CG   . LYS   A 163 ? 0.1931 0.2296 0.4984 0.0060  -0.0143 0.0381  370 LYS   A CG   
1102 C  CD   . LYS   A 163 ? 0.1535 0.1834 0.5658 -0.0091 0.0227  0.0016  370 LYS   A CD   
1103 C  CE   . LYS   A 163 ? 0.2187 0.2223 0.6562 -0.0602 0.0989  0.0750  370 LYS   A CE   
1104 N  NZ   . LYS   A 163 ? 0.2730 0.2621 0.6838 -0.0942 0.1363  -0.0298 370 LYS   A NZ   
1105 N  N    . ALA   A 164 ? 0.0526 0.1582 0.3949 0.0049  -0.0515 0.0483  371 ALA   A N    
1106 C  CA   . ALA   A 164 ? 0.0620 0.1383 0.3523 0.0214  -0.0120 0.0508  371 ALA   A CA   
1107 C  C    . ALA   A 164 ? 0.1011 0.0791 0.3231 0.0128  -0.0273 0.0239  371 ALA   A C    
1108 O  O    . ALA   A 164 ? 0.0476 0.1351 0.4162 -0.0012 -0.0093 -0.0494 371 ALA   A O    
1109 C  CB   . ALA   A 164 ? 0.0540 0.0989 0.4398 -0.0500 -0.0618 0.0929  371 ALA   A CB   
1110 N  N    . ILE   A 165 ? 0.1115 0.0821 0.3686 0.0216  -0.0083 0.0489  372 ILE   A N    
1111 C  CA   . ILE   A 165 ? 0.0946 0.1417 0.3821 0.0154  0.0032  0.0568  372 ILE   A CA   
1112 C  C    . ILE   A 165 ? 0.0460 0.1010 0.3654 -0.0181 -0.0490 -0.0124 372 ILE   A C    
1113 O  O    . ILE   A 165 ? 0.1140 0.0769 0.4308 -0.0458 0.0252  -0.0047 372 ILE   A O    
1114 C  CB   . ILE   A 165 ? 0.0375 0.1267 0.4003 0.0421  0.0001  0.0501  372 ILE   A CB   
1115 C  CG1  . ILE   A 165 ? 0.0157 0.1456 0.4302 0.0338  -0.0068 0.0616  372 ILE   A CG1  
1116 C  CG2  . ILE   A 165 ? 0.0801 0.1335 0.4634 0.0286  0.0469  0.0432  372 ILE   A CG2  
1117 C  CD1  . ILE   A 165 ? 0.0591 0.1356 0.4546 -0.0094 0.0229  0.0649  372 ILE   A CD1  
1118 N  N    . ALA   A 166 ? 0.0545 0.1237 0.4123 0.0241  -0.0695 0.0479  373 ALA   A N    
1119 C  CA   . ALA   A 166 ? 0.1400 0.0758 0.4257 0.0156  -0.0432 0.0485  373 ALA   A CA   
1120 C  C    . ALA   A 166 ? 0.1422 0.0882 0.4175 -0.0075 -0.0501 0.0344  373 ALA   A C    
1121 O  O    . ALA   A 166 ? 0.0262 0.0894 0.5181 -0.0405 -0.0094 -0.0007 373 ALA   A O    
1122 C  CB   . ALA   A 166 ? 0.1477 0.1040 0.4367 0.0193  -0.0608 0.0172  373 ALA   A CB   
1123 N  N    . LEU   A 167 ? 0.0579 0.1492 0.3771 0.0386  -0.0127 0.0159  374 LEU   A N    
1124 C  CA   . LEU   A 167 ? 0.0232 0.1366 0.4086 0.0420  -0.0364 0.0015  374 LEU   A CA   
1125 C  C    . LEU   A 167 ? 0.0431 0.1516 0.4329 0.0121  -0.0345 -0.0146 374 LEU   A C    
1126 O  O    . LEU   A 167 ? 0.0890 0.1568 0.4306 -0.0107 0.0216  -0.0322 374 LEU   A O    
1127 C  CB   . LEU   A 167 ? 0.0189 0.1959 0.4347 0.0181  0.0012  0.0169  374 LEU   A CB   
1128 C  CG   . LEU   A 167 ? 0.1298 0.1855 0.4482 0.0264  0.0046  0.0040  374 LEU   A CG   
1129 C  CD1  . LEU   A 167 ? 0.0537 0.2607 0.4873 0.0270  -0.0122 -0.0423 374 LEU   A CD1  
1130 C  CD2  . LEU   A 167 ? 0.1409 0.2182 0.4923 -0.1118 0.0402  -0.0240 374 LEU   A CD2  
1131 N  N    . ALA   A 168 ? 0.0232 0.1494 0.4689 -0.0015 0.0073  0.0378  375 ALA   A N    
1132 C  CA   . ALA   A 168 ? 0.0680 0.2287 0.4421 -0.0289 -0.0227 -0.0252 375 ALA   A CA   
1133 C  C    . ALA   A 168 ? 0.0622 0.1331 0.3682 0.0460  -0.0420 -0.0522 375 ALA   A C    
1134 O  O    . ALA   A 168 ? 0.0954 0.1991 0.4692 -0.0411 -0.0001 -0.0602 375 ALA   A O    
1135 C  CB   . ALA   A 168 ? 0.0313 0.2024 0.5085 -0.0653 -0.0342 -0.0179 375 ALA   A CB   
1136 N  N    . ASN   A 169 ? 0.0246 0.1746 0.3637 0.0332  -0.0134 0.0181  376 ASN   A N    
1137 C  CA   . ASN   A 169 ? 0.0297 0.1399 0.3989 -0.0484 -0.0085 0.0153  376 ASN   A CA   
1138 C  C    . ASN   A 169 ? 0.0154 0.1785 0.3498 -0.0362 0.0226  0.0002  376 ASN   A C    
1139 O  O    . ASN   A 169 ? 0.1229 0.1603 0.3879 0.0034  -0.0160 -0.0165 376 ASN   A O    
1140 C  CB   . ASN   A 169 ? 0.0388 0.1410 0.4204 -0.0161 -0.0148 0.0225  376 ASN   A CB   
1141 C  CG   . ASN   A 169 ? 0.0893 0.1496 0.3686 0.0164  0.0331  -0.0292 376 ASN   A CG   
1142 O  OD1  . ASN   A 169 ? 0.0976 0.1192 0.4951 -0.0061 0.0459  -0.0278 376 ASN   A OD1  
1143 N  ND2  . ASN   A 169 ? 0.1902 0.0870 0.3857 0.0209  0.0048  0.0034  376 ASN   A ND2  
1144 N  N    . SER   A 170 ? 0.0604 0.1543 0.4615 0.0068  0.0450  -0.0474 377 SER   A N    
1145 C  CA   . SER   A 170 ? 0.1598 0.0697 0.4627 0.0187  0.0626  -0.0114 377 SER   A CA   
1146 C  C    . SER   A 170 ? 0.0754 0.0515 0.4975 0.0219  -0.0214 -0.0816 377 SER   A C    
1147 O  O    . SER   A 170 ? 0.0631 0.0749 0.5086 0.0118  0.0260  0.0068  377 SER   A O    
1148 C  CB   . SER   A 170 ? 0.2635 0.1107 0.5161 0.0041  0.1331  0.0460  377 SER   A CB   
1149 O  OG   . SER   A 170 ? 0.3268 0.2918 0.5342 0.0499  0.1183  -0.0091 377 SER   A OG   
1150 N  N    . ASP   A 171 ? 0.0815 0.0916 0.4795 -0.0159 0.0098  -0.0172 378 ASP   A N    
1151 C  CA   . ASP   A 171 ? 0.1279 0.0929 0.4792 -0.0199 -0.0017 -0.0215 378 ASP   A CA   
1152 C  C    . ASP   A 171 ? 0.1238 0.1379 0.4162 -0.0522 0.0172  -0.0499 378 ASP   A C    
1153 O  O    . ASP   A 171 ? 0.1663 0.1300 0.5141 -0.0486 -0.0085 -0.0313 378 ASP   A O    
1154 C  CB   . ASP   A 171 ? 0.1070 0.1302 0.4684 0.0174  0.0490  -0.0171 378 ASP   A CB   
1155 C  CG   . ASP   A 171 ? 0.1256 0.1392 0.4209 0.0623  -0.0225 -0.0244 378 ASP   A CG   
1156 O  OD1  . ASP   A 171 ? 0.1188 0.0705 0.5444 -0.0113 -0.0274 -0.0211 378 ASP   A OD1  
1157 O  OD2  . ASP   A 171 ? 0.0356 0.1030 0.4770 0.0128  0.0181  -0.0422 378 ASP   A OD2  
1158 N  N    . SER   A 172 ? 0.1180 0.1688 0.4016 -0.0725 -0.0120 -0.0899 379 SER   A N    
1159 C  CA   . SER   A 172 ? 0.1417 0.0837 0.4945 -0.0863 0.0451  -0.0940 379 SER   A CA   
1160 C  C    . SER   A 172 ? 0.0754 0.1127 0.4936 -0.0794 0.0906  -0.0829 379 SER   A C    
1161 O  O    . SER   A 172 ? 0.0836 0.1660 0.5605 -0.0637 0.0350  -0.0547 379 SER   A O    
1162 C  CB   . SER   A 172 ? 0.1305 0.1927 0.4926 -0.0985 0.0093  -0.0939 379 SER   A CB   
1163 O  OG   . SER   A 172 ? 0.3838 0.1574 0.5439 -0.1414 0.1004  -0.0664 379 SER   A OG   
1164 N  N    . MET   A 173 ? 0.1658 0.1188 0.5003 -0.0408 0.0362  -0.0497 380 MET   A N    
1165 C  CA   . MET   A 173 ? 0.3143 0.1456 0.5818 -0.0952 0.0003  -0.0860 380 MET   A CA   
1166 C  C    . MET   A 173 ? 0.2719 0.2033 0.5668 -0.1363 0.0248  -0.0171 380 MET   A C    
1167 O  O    . MET   A 173 ? 0.1817 0.2519 0.7737 -0.1112 0.0796  -0.1210 380 MET   A O    
1168 C  CB   . MET   A 173 ? 0.5081 0.1263 0.7382 -0.1016 -0.1562 0.0906  380 MET   A CB   
1169 C  CG   . MET   A 173 ? 0.6696 0.2923 0.7290 -0.0335 -0.1126 -0.0001 380 MET   A CG   
1170 S  SD   . MET   A 173 ? 0.9850 0.5123 1.1589 0.2113  -0.1062 0.3160  380 MET   A SD   
1171 C  CE   . MET   A 173 ? 0.8719 0.8369 1.1813 0.3103  -0.0070 -0.0530 380 MET   A CE   
1172 N  N    . HIS   A 174 ? 0.2547 0.2071 0.5581 -0.0472 0.0331  -0.0001 381 HIS   A N    
1173 C  CA   . HIS   A 174 ? 0.4006 0.1835 0.5721 0.0046  0.0350  0.0044  381 HIS   A CA   
1174 C  C    . HIS   A 174 ? 0.2373 0.1792 0.5338 -0.0095 -0.0081 -0.1173 381 HIS   A C    
1175 O  O    . HIS   A 174 ? 0.2464 0.3922 0.5762 -0.0745 0.0353  -0.1573 381 HIS   A O    
1176 C  CB   . HIS   A 174 ? 0.3482 0.2991 0.5700 0.0355  0.0211  -0.0607 381 HIS   A CB   
1177 C  CG   . HIS   A 174 ? 0.4924 0.0913 0.6295 0.0496  -0.0310 -0.1120 381 HIS   A CG   
1178 N  ND1  . HIS   A 174 ? 0.4896 0.0867 0.6954 0.0672  0.0477  -0.0761 381 HIS   A ND1  
1179 C  CD2  . HIS   A 174 ? 0.6077 0.2980 0.6435 0.0022  -0.1028 -0.0547 381 HIS   A CD2  
1180 C  CE1  . HIS   A 174 ? 0.6054 0.4566 0.5685 0.0449  -0.0575 -0.0884 381 HIS   A CE1  
1181 N  NE2  . HIS   A 174 ? 0.5964 0.3418 0.6116 0.1035  -0.0194 -0.0845 381 HIS   A NE2  
1182 N  N    . ILE   A 175 ? 0.3597 0.1778 0.5253 -0.0248 0.0546  -0.1286 382 ILE   A N    
1183 C  CA   . ILE   A 175 ? 0.2471 0.2116 0.5901 -0.0363 0.0105  -0.1184 382 ILE   A CA   
1184 C  C    . ILE   A 175 ? 0.3457 0.0703 0.5557 -0.0997 0.0189  -0.0827 382 ILE   A C    
1185 O  O    . ILE   A 175 ? 0.4682 0.0590 0.8842 -0.1183 0.1876  -0.1159 382 ILE   A O    
1186 C  CB   . ILE   A 175 ? 0.1709 0.2574 0.5911 -0.0182 -0.0400 -0.1343 382 ILE   A CB   
1187 C  CG1  . ILE   A 175 ? 0.0804 0.4084 0.6295 -0.0451 -0.0500 -0.0705 382 ILE   A CG1  
1188 C  CG2  . ILE   A 175 ? 0.0884 0.3048 0.6515 0.0555  -0.0464 -0.1399 382 ILE   A CG2  
1189 C  CD1  . ILE   A 175 ? 0.3541 0.2733 0.6061 -0.1449 0.0251  -0.1752 382 ILE   A CD1  
1190 N  N    . GLU   A 176 ? 0.2751 0.2585 0.5670 -0.1142 0.0611  -0.0950 383 GLU   A N    
1191 C  CA   . GLU   A 176 ? 0.3014 0.2583 0.6414 -0.0524 -0.0076 -0.1408 383 GLU   A CA   
1192 C  C    . GLU   A 176 ? 0.1235 0.3970 0.6926 -0.2013 -0.0162 -0.1471 383 GLU   A C    
1193 O  O    . GLU   A 176 ? 0.1609 0.3872 0.7514 -0.2370 -0.0338 -0.0618 383 GLU   A O    
1194 C  CB   . GLU   A 176 ? 0.2528 0.1336 0.6527 -0.0893 0.0233  -0.2273 383 GLU   A CB   
1195 C  CG   . GLU   A 176 ? 0.3230 0.4685 0.6919 0.0026  0.0634  -0.3400 383 GLU   A CG   
1196 C  CD   . GLU   A 176 ? 0.3732 0.6469 0.7123 -0.0664 0.0278  -0.2640 383 GLU   A CD   
1197 O  OE1  . GLU   A 176 ? 0.3861 0.6254 0.5664 -0.0139 -0.0255 -0.2217 383 GLU   A OE1  
1198 O  OE2  . GLU   A 176 ? 0.3490 0.7208 0.9455 -0.1681 0.1464  -0.4583 383 GLU   A OE2  
1199 N  N    . ASP   A 177 ? 0.1792 0.3970 0.6827 -0.0361 0.0300  -0.2208 384 ASP   A N    
1200 C  CA   . ASP   A 177 ? 0.2295 0.2747 0.6787 -0.0221 -0.1205 -0.1256 384 ASP   A CA   
1201 C  C    . ASP   A 177 ? 0.1692 0.4073 0.6050 -0.0593 -0.0258 -0.0481 384 ASP   A C    
1202 O  O    . ASP   A 177 ? 0.0910 0.4790 0.6281 -0.0855 -0.0741 -0.1376 384 ASP   A O    
1203 C  CB   . ASP   A 177 ? 0.1782 0.3388 0.6379 -0.0366 -0.1316 -0.0681 384 ASP   A CB   
1204 C  CG   . ASP   A 177 ? 0.1802 0.3759 0.4915 0.0075  -0.0864 -0.1875 384 ASP   A CG   
1205 O  OD1  . ASP   A 177 ? 0.2202 0.5257 0.5633 -0.0815 -0.0482 -0.1693 384 ASP   A OD1  
1206 O  OD2  . ASP   A 177 ? 0.1264 0.5195 0.5406 -0.0064 -0.0880 -0.1452 384 ASP   A OD2  
1207 N  N    . VAL   A 178 ? 0.1699 0.3033 0.5946 -0.1373 -0.0572 -0.1318 385 VAL   A N    
1208 C  CA   . VAL   A 178 ? 0.1536 0.3040 0.6533 -0.1455 -0.0170 -0.1832 385 VAL   A CA   
1209 C  C    . VAL   A 178 ? 0.1226 0.3313 0.5486 -0.1110 -0.0139 -0.0715 385 VAL   A C    
1210 O  O    . VAL   A 178 ? 0.2025 0.3060 0.5571 -0.1306 -0.0003 -0.0615 385 VAL   A O    
1211 C  CB   . VAL   A 178 ? 0.1695 0.2014 0.7264 -0.0145 0.1230  -0.2032 385 VAL   A CB   
1212 C  CG1  . VAL   A 178 ? 0.3373 0.3264 0.7420 0.0790  0.1239  -0.1180 385 VAL   A CG1  
1213 C  CG2  . VAL   A 178 ? 0.2345 0.2147 0.7478 0.0010  0.0581  -0.2163 385 VAL   A CG2  
1214 N  N    . GLU   A 179 ? 0.0960 0.3755 0.6087 -0.0665 -0.0002 -0.1272 386 GLU   A N    
1215 C  CA   . GLU   A 179 ? 0.0873 0.3351 0.6711 -0.1016 0.0069  -0.1636 386 GLU   A CA   
1216 C  C    . GLU   A 179 ? 0.1246 0.3067 0.4770 -0.0753 -0.0296 -0.1368 386 GLU   A C    
1217 O  O    . GLU   A 179 ? 0.1232 0.3746 0.6095 -0.0558 -0.0723 -0.2357 386 GLU   A O    
1218 C  CB   . GLU   A 179 ? 0.1564 0.4584 0.7272 -0.0142 -0.0867 -0.2030 386 GLU   A CB   
1219 C  CG   . GLU   A 179 ? 0.3480 0.7065 0.8806 -0.0258 0.0653  -0.0880 386 GLU   A CG   
1220 C  CD   . GLU   A 179 ? 0.7053 0.9078 0.9616 -0.2018 -0.0935 -0.1288 386 GLU   A CD   
1221 O  OE1  . GLU   A 179 ? 0.5777 1.1414 0.9817 -0.3428 -0.3218 -0.0300 386 GLU   A OE1  
1222 O  OE2  . GLU   A 179 ? 1.2762 0.8062 1.0756 0.0028  0.4969  0.2030  386 GLU   A OE2  
1223 N  N    . ALA   A 180 ? 0.1120 0.3554 0.5526 -0.0255 -0.0097 -0.0862 387 ALA   A N    
1224 C  CA   . ALA   A 180 ? 0.1617 0.3344 0.5301 0.0453  -0.0348 -0.0094 387 ALA   A CA   
1225 C  C    . ALA   A 180 ? 0.1289 0.3520 0.5499 0.0520  -0.0511 -0.0126 387 ALA   A C    
1226 O  O    . ALA   A 180 ? 0.0807 0.4033 0.5115 -0.0078 -0.0369 -0.0350 387 ALA   A O    
1227 C  CB   . ALA   A 180 ? 0.1305 0.3809 0.5225 0.0811  -0.1089 -0.1284 387 ALA   A CB   
1228 N  N    . VAL   A 181 ? 0.1078 0.2873 0.5305 -0.0417 -0.0434 0.0120  388 VAL   A N    
1229 C  CA   . VAL   A 181 ? 0.1108 0.2468 0.4904 -0.0276 -0.0335 -0.0077 388 VAL   A CA   
1230 C  C    . VAL   A 181 ? 0.0597 0.2155 0.5028 -0.0172 -0.0065 -0.0160 388 VAL   A C    
1231 O  O    . VAL   A 181 ? 0.1357 0.1865 0.5215 -0.0089 0.0193  -0.0443 388 VAL   A O    
1232 C  CB   . VAL   A 181 ? 0.0883 0.2103 0.5148 -0.0183 -0.0315 -0.0837 388 VAL   A CB   
1233 C  CG1  . VAL   A 181 ? 0.2069 0.2407 0.4951 0.0120  -0.0166 -0.0845 388 VAL   A CG1  
1234 C  CG2  . VAL   A 181 ? 0.2330 0.3048 0.4753 0.0369  -0.0267 -0.0443 388 VAL   A CG2  
1235 N  N    . GLN   A 182 ? 0.0902 0.2774 0.5076 -0.0760 -0.0112 -0.0270 389 GLN   A N    
1236 C  CA   . GLN   A 182 ? 0.1469 0.2356 0.5126 -0.0850 -0.0355 -0.0598 389 GLN   A CA   
1237 C  C    . GLN   A 182 ? 0.0733 0.2749 0.4457 -0.0163 -0.0025 -0.0492 389 GLN   A C    
1238 O  O    . GLN   A 182 ? 0.0767 0.2784 0.4918 -0.0416 0.0256  -0.0764 389 GLN   A O    
1239 C  CB   . GLN   A 182 ? 0.0801 0.3844 0.6138 -0.1032 -0.0444 -0.0673 389 GLN   A CB   
1240 C  CG   . GLN   A 182 ? 0.2450 0.3838 0.6081 -0.0998 0.0142  -0.0177 389 GLN   A CG   
1241 C  CD   . GLN   A 182 ? 0.3681 0.3785 0.6166 -0.1876 0.0077  -0.0870 389 GLN   A CD   
1242 O  OE1  . GLN   A 182 ? 0.6857 0.5449 1.1868 -0.4812 -0.2448 0.2937  389 GLN   A OE1  
1243 N  NE2  . GLN   A 182 ? 0.1872 0.3042 0.6030 -0.0878 0.0256  -0.0779 389 GLN   A NE2  
1244 N  N    . LYS   A 183 ? 0.0498 0.3532 0.5074 -0.0786 -0.0447 0.0069  390 LYS   A N    
1245 C  CA   . LYS   A 183 ? 0.1240 0.3003 0.5653 -0.0188 -0.0438 -0.0685 390 LYS   A CA   
1246 C  C    . LYS   A 183 ? 0.0648 0.3011 0.5765 0.0238  -0.0564 -0.0246 390 LYS   A C    
1247 O  O    . LYS   A 183 ? 0.0529 0.3183 0.5527 0.0388  -0.0869 -0.0319 390 LYS   A O    
1248 C  CB   . LYS   A 183 ? 0.0886 0.5139 0.6316 -0.1159 -0.0937 -0.0476 390 LYS   A CB   
1249 C  CG   . LYS   A 183 ? 0.3539 0.6711 0.8075 -0.1265 -0.2309 0.0800  390 LYS   A CG   
1250 C  CD   . LYS   A 183 ? 0.8047 0.9801 0.8916 0.0864  -0.2720 0.1287  390 LYS   A CD   
1251 C  CE   . LYS   A 183 ? 1.0127 1.0351 0.8719 0.2833  -0.1776 0.2552  390 LYS   A CE   
1252 N  NZ   . LYS   A 183 ? 1.1312 1.3186 1.0335 0.4032  -0.3087 0.2678  390 LYS   A NZ   
1253 N  N    . LEU   A 184 ? 0.0613 0.2220 0.5189 0.0094  -0.0684 -0.0125 391 LEU   A N    
1254 C  CA   . LEU   A 184 ? 0.0165 0.2492 0.4941 0.0223  -0.0197 0.0078  391 LEU   A CA   
1255 C  C    . LEU   A 184 ? 0.0534 0.2081 0.4750 0.0238  -0.0294 0.0601  391 LEU   A C    
1256 O  O    . LEU   A 184 ? 0.1099 0.2387 0.4464 0.0227  0.0110  0.0004  391 LEU   A O    
1257 C  CB   . LEU   A 184 ? 0.0690 0.2314 0.4939 0.0482  -0.0470 -0.0362 391 LEU   A CB   
1258 C  CG   . LEU   A 184 ? 0.1198 0.2370 0.5441 -0.0228 -0.0407 0.0280  391 LEU   A CG   
1259 C  CD1  . LEU   A 184 ? 0.1048 0.1788 0.6262 -0.0486 -0.0090 0.0018  391 LEU   A CD1  
1260 C  CD2  . LEU   A 184 ? 0.0740 0.2444 0.5935 -0.0565 -0.0313 0.0194  391 LEU   A CD2  
1261 N  N    . GLN   A 185 ? 0.0278 0.2042 0.4483 -0.0491 -0.0041 0.0453  392 GLN   A N    
1262 C  CA   . GLN   A 185 ? 0.0725 0.1391 0.4804 -0.0139 -0.0060 -0.0057 392 GLN   A CA   
1263 C  C    . GLN   A 185 ? 0.0087 0.1836 0.4269 -0.0116 -0.0269 0.0142  392 GLN   A C    
1264 O  O    . GLN   A 185 ? 0.0822 0.2071 0.4270 0.0032  0.0029  -0.0029 392 GLN   A O    
1265 C  CB   . GLN   A 185 ? 0.1450 0.1519 0.5204 0.0094  0.0021  0.0338  392 GLN   A CB   
1266 C  CG   . GLN   A 185 ? 0.1098 0.0933 0.5681 -0.0307 -0.0154 0.0070  392 GLN   A CG   
1267 C  CD   . GLN   A 185 ? 0.1603 0.1106 0.5295 -0.0695 0.0740  -0.0381 392 GLN   A CD   
1268 O  OE1  . GLN   A 185 ? 0.1053 0.1567 0.5677 0.0064  0.0625  -0.0090 392 GLN   A OE1  
1269 N  NE2  . GLN   A 185 ? 0.1321 0.1209 0.5056 -0.0173 -0.0126 -0.0253 392 GLN   A NE2  
1270 N  N    . ASP   A 186 ? 0.0299 0.2093 0.4436 0.0009  -0.0679 0.0010  393 ASP   A N    
1271 C  CA   . ASP   A 186 ? 0.1273 0.2126 0.4994 0.0014  0.0240  -0.0196 393 ASP   A CA   
1272 C  C    . ASP   A 186 ? 0.0652 0.2176 0.4766 -0.0565 -0.0207 -0.0559 393 ASP   A C    
1273 O  O    . ASP   A 186 ? 0.0964 0.1270 0.4717 -0.0023 -0.0141 -0.0097 393 ASP   A O    
1274 C  CB   . ASP   A 186 ? 0.0882 0.3162 0.5088 0.0200  0.0202  0.0090  393 ASP   A CB   
1275 C  CG   . ASP   A 186 ? 0.3347 0.4731 0.6231 -0.0517 0.0720  0.0766  393 ASP   A CG   
1276 O  OD1  . ASP   A 186 ? 0.2207 0.7932 0.5440 -0.1470 -0.0241 -0.0082 393 ASP   A OD1  
1277 O  OD2  . ASP   A 186 ? 0.2096 0.9564 0.7259 0.0311  0.0595  -0.0161 393 ASP   A OD2  
1278 N  N    . VAL   A 187 ? 0.0170 0.2693 0.5201 0.0329  -0.0564 0.0124  394 VAL   A N    
1279 C  CA   . VAL   A 187 ? 0.0415 0.3220 0.5351 0.0781  -0.0661 0.0933  394 VAL   A CA   
1280 C  C    . VAL   A 187 ? 0.0472 0.2203 0.4903 0.0770  -0.0493 0.0505  394 VAL   A C    
1281 O  O    . VAL   A 187 ? 0.0411 0.2402 0.5227 -0.0250 0.0259  -0.0030 394 VAL   A O    
1282 C  CB   . VAL   A 187 ? 0.1120 0.3570 0.4814 0.0152  -0.1124 0.0938  394 VAL   A CB   
1283 C  CG1  . VAL   A 187 ? 0.1913 0.5314 0.4306 -0.0886 -0.0424 0.1169  394 VAL   A CG1  
1284 C  CG2  . VAL   A 187 ? 0.0644 0.3909 0.4999 0.0025  -0.0558 0.0447  394 VAL   A CG2  
1285 N  N    . LEU   A 188 ? 0.0323 0.0976 0.5149 0.0485  -0.0037 0.0127  395 LEU   A N    
1286 C  CA   . LEU   A 188 ? 0.0812 0.0965 0.4552 0.0085  -0.0346 0.0528  395 LEU   A CA   
1287 C  C    . LEU   A 188 ? 0.0072 0.1460 0.4458 -0.0083 -0.0174 0.0661  395 LEU   A C    
1288 O  O    . LEU   A 188 ? 0.0895 0.1031 0.4981 -0.0115 -0.0545 0.0516  395 LEU   A O    
1289 C  CB   . LEU   A 188 ? 0.1088 0.0992 0.4781 0.0248  0.0084  0.0249  395 LEU   A CB   
1290 C  CG   . LEU   A 188 ? 0.1372 0.0948 0.4576 0.0334  0.0023  0.0072  395 LEU   A CG   
1291 C  CD1  . LEU   A 188 ? 0.0936 0.1217 0.4883 0.0282  0.0009  0.0449  395 LEU   A CD1  
1292 C  CD2  . LEU   A 188 ? 0.2368 0.0992 0.4534 0.0627  0.0684  0.0262  395 LEU   A CD2  
1293 N  N    . HIS   A 189 ? 0.0447 0.1278 0.4310 -0.0153 -0.0033 0.0832  396 HIS   A N    
1294 C  CA   . HIS   A 189 ? 0.0534 0.0636 0.4039 0.0027  -0.0298 0.0698  396 HIS   A CA   
1295 C  C    . HIS   A 189 ? 0.0608 0.0499 0.3670 -0.0050 0.0175  0.1120  396 HIS   A C    
1296 O  O    . HIS   A 189 ? 0.0538 0.1442 0.4406 0.0600  0.0008  0.0421  396 HIS   A O    
1297 C  CB   . HIS   A 189 ? 0.1027 0.1062 0.4670 -0.0721 -0.0406 0.0291  396 HIS   A CB   
1298 C  CG   . HIS   A 189 ? 0.0452 0.1254 0.4469 -0.0505 -0.0343 0.0545  396 HIS   A CG   
1299 N  ND1  . HIS   A 189 ? 0.0219 0.2343 0.4715 -0.0588 -0.0474 0.1333  396 HIS   A ND1  
1300 C  CD2  . HIS   A 189 ? 0.1124 0.0834 0.4532 -0.0718 0.0143  0.1029  396 HIS   A CD2  
1301 C  CE1  . HIS   A 189 ? 0.0688 0.2406 0.4688 -0.1179 -0.0132 0.0599  396 HIS   A CE1  
1302 N  NE2  . HIS   A 189 ? 0.0548 0.0979 0.5148 -0.0400 0.0524  0.0609  396 HIS   A NE2  
1303 N  N    . GLU   A 190 ? 0.0893 0.1063 0.4314 0.0014  -0.0267 0.0671  397 GLU   A N    
1304 C  CA   . GLU   A 190 ? 0.0995 0.1105 0.4437 0.0042  -0.0399 0.1021  397 GLU   A CA   
1305 C  C    . GLU   A 190 ? 0.1405 0.1010 0.4279 -0.0026 0.0265  0.0676  397 GLU   A C    
1306 O  O    . GLU   A 190 ? 0.1352 0.1278 0.4824 -0.0041 0.0284  0.0238  397 GLU   A O    
1307 C  CB   . GLU   A 190 ? 0.0844 0.2442 0.4538 0.0223  -0.0337 0.0203  397 GLU   A CB   
1308 C  CG   . GLU   A 190 ? 0.2114 0.2231 0.5529 0.0552  -0.0343 0.0093  397 GLU   A CG   
1309 C  CD   . GLU   A 190 ? 0.1382 0.3359 0.5664 0.1079  -0.0288 0.0442  397 GLU   A CD   
1310 O  OE1  . GLU   A 190 ? 0.1265 0.3907 0.6181 0.0728  -0.0052 0.0440  397 GLU   A OE1  
1311 O  OE2  . GLU   A 190 ? 0.0506 0.4310 0.7477 0.0593  -0.0285 0.1209  397 GLU   A OE2  
1312 N  N    . ALA   A 191 ? 0.0854 0.0435 0.4534 0.0087  -0.0011 0.0836  398 ALA   A N    
1313 C  CA   . ALA   A 191 ? 0.1813 0.0316 0.4750 -0.0109 0.0248  0.1054  398 ALA   A CA   
1314 C  C    . ALA   A 191 ? 0.1088 0.1079 0.4568 0.0574  0.0150  0.0690  398 ALA   A C    
1315 O  O    . ALA   A 191 ? 0.0737 0.1389 0.4809 0.0079  0.0182  0.0281  398 ALA   A O    
1316 C  CB   . ALA   A 191 ? 0.1348 0.1453 0.4990 -0.0520 0.0198  0.1136  398 ALA   A CB   
1317 N  N    . LEU   A 192 ? 0.0542 0.1119 0.4497 0.0537  -0.0013 0.0444  399 LEU   A N    
1318 C  CA   . LEU   A 192 ? 0.0345 0.1033 0.4421 0.0059  0.0127  0.0725  399 LEU   A CA   
1319 C  C    . LEU   A 192 ? 0.0469 0.0961 0.4933 -0.0252 0.0335  0.0256  399 LEU   A C    
1320 O  O    . LEU   A 192 ? 0.0395 0.1411 0.4620 0.0434  0.0325  0.0361  399 LEU   A O    
1321 C  CB   . LEU   A 192 ? 0.1552 0.0224 0.4709 -0.0380 0.0178  0.0500  399 LEU   A CB   
1322 C  CG   . LEU   A 192 ? 0.0970 0.0686 0.4364 -0.0489 0.0210  0.0450  399 LEU   A CG   
1323 C  CD1  . LEU   A 192 ? 0.1286 0.0947 0.4770 -0.0690 -0.0658 0.0431  399 LEU   A CD1  
1324 C  CD2  . LEU   A 192 ? 0.1036 0.0496 0.5337 -0.0203 -0.0553 0.0076  399 LEU   A CD2  
1325 N  N    . GLN   A 193 ? 0.0330 0.1463 0.4754 -0.0221 0.0350  0.0591  400 GLN   A N    
1326 C  CA   . GLN   A 193 ? 0.0516 0.0678 0.4840 -0.0269 0.0401  0.0405  400 GLN   A CA   
1327 C  C    . GLN   A 193 ? 0.0109 0.1136 0.4863 0.0110  0.0106  0.0809  400 GLN   A C    
1328 O  O    . GLN   A 193 ? 0.0873 0.1043 0.5222 -0.0003 0.0597  0.0613  400 GLN   A O    
1329 C  CB   . GLN   A 193 ? 0.0293 0.3060 0.5234 -0.0827 -0.0010 0.0430  400 GLN   A CB   
1330 C  CG   . GLN   A 193 ? 0.2068 0.2048 0.5319 0.0384  0.0309  0.0731  400 GLN   A CG   
1331 C  CD   . GLN   A 193 ? 0.1805 0.2498 0.5456 0.0899  0.0470  0.1229  400 GLN   A CD   
1332 O  OE1  . GLN   A 193 ? 0.0618 0.2465 0.6318 0.0052  -0.0256 0.1389  400 GLN   A OE1  
1333 N  NE2  . GLN   A 193 ? 0.3487 0.3886 0.5564 -0.0975 0.1105  0.0390  400 GLN   A NE2  
1334 N  N    . ASP   A 194 ? 0.0697 0.1636 0.5147 0.0604  0.0542  0.1088  401 ASP   A N    
1335 C  CA   A ASP   A 194 ? 0.1586 0.1022 0.5623 0.0478  0.0288  0.0311  401 ASP   A CA   
1336 C  CA   B ASP   A 194 ? 0.1342 0.1255 0.4962 0.0662  0.0207  0.0519  401 ASP   A CA   
1337 C  C    . ASP   A 194 ? 0.1092 0.1752 0.5148 0.0258  0.0770  0.0343  401 ASP   A C    
1338 O  O    . ASP   A 194 ? 0.1034 0.1933 0.6215 0.0549  0.0897  0.0250  401 ASP   A O    
1339 C  CB   A ASP   A 194 ? 0.1165 0.1692 0.5495 0.0458  0.0855  0.0560  401 ASP   A CB   
1340 C  CB   B ASP   A 194 ? 0.1141 0.1850 0.4890 0.1044  0.0097  0.0650  401 ASP   A CB   
1341 C  CG   A ASP   A 194 ? 0.1142 0.1960 0.5686 0.1081  0.0340  0.0434  401 ASP   A CG   
1342 C  CG   B ASP   A 194 ? 0.1077 0.1840 0.3779 0.0512  0.0501  0.1058  401 ASP   A CG   
1343 O  OD1  A ASP   A 194 ? 0.0432 0.2513 0.6572 0.0221  0.0746  0.0230  401 ASP   A OD1  
1344 O  OD1  B ASP   A 194 ? 0.0688 0.2731 0.4619 0.1008  0.0666  0.1065  401 ASP   A OD1  
1345 O  OD2  A ASP   A 194 ? 0.1223 0.1277 0.6275 0.0382  -0.0051 0.0326  401 ASP   A OD2  
1346 O  OD2  B ASP   A 194 ? 0.1265 0.2396 0.4110 -0.0119 0.0645  0.0424  401 ASP   A OD2  
1347 N  N    . TYR   A 195 ? 0.0969 0.1534 0.5833 0.0017  0.0668  0.0720  402 TYR   A N    
1348 C  CA   . TYR   A 195 ? 0.1395 0.0314 0.5366 0.0355  0.0540  0.0349  402 TYR   A CA   
1349 C  C    . TYR   A 195 ? 0.1262 0.0533 0.5142 0.0348  0.0166  0.0650  402 TYR   A C    
1350 O  O    . TYR   A 195 ? 0.1236 0.0905 0.6660 -0.0053 0.0626  -0.0139 402 TYR   A O    
1351 C  CB   . TYR   A 195 ? 0.1634 0.0908 0.5088 0.0784  0.0436  0.0658  402 TYR   A CB   
1352 C  CG   . TYR   A 195 ? 0.1635 0.0666 0.5313 0.0827  0.0489  0.0464  402 TYR   A CG   
1353 C  CD1  . TYR   A 195 ? 0.1763 0.1297 0.4716 0.0323  0.0035  0.0631  402 TYR   A CD1  
1354 C  CD2  . TYR   A 195 ? 0.1767 0.1044 0.5198 0.0234  0.0127  0.0246  402 TYR   A CD2  
1355 C  CE1  . TYR   A 195 ? 0.1316 0.2574 0.5465 -0.0093 0.0278  0.0375  402 TYR   A CE1  
1356 C  CE2  . TYR   A 195 ? 0.1037 0.0776 0.5361 0.0826  0.0324  0.0531  402 TYR   A CE2  
1357 C  CZ   . TYR   A 195 ? 0.1934 0.0093 0.5798 0.0210  -0.0322 0.0161  402 TYR   A CZ   
1358 O  OH   . TYR   A 195 ? 0.1977 0.1549 0.6098 -0.0195 -0.0156 -0.0757 402 TYR   A OH   
1359 N  N    . GLU   A 196 ? 0.1050 0.0225 0.5130 0.0092  0.0068  0.0503  403 GLU   A N    
1360 C  CA   . GLU   A 196 ? 0.1000 0.0917 0.4934 0.0138  0.0721  -0.0073 403 GLU   A CA   
1361 C  C    . GLU   A 196 ? 0.1529 0.1493 0.4069 0.0725  0.0370  -0.0263 403 GLU   A C    
1362 O  O    . GLU   A 196 ? 0.1939 0.0476 0.4535 0.0120  0.0486  -0.0336 403 GLU   A O    
1363 C  CB   . GLU   A 196 ? 0.1114 0.1181 0.4910 0.0308  0.0141  0.0151  403 GLU   A CB   
1364 C  CG   . GLU   A 196 ? 0.1070 0.0097 0.5236 -0.0042 -0.0693 0.0418  403 GLU   A CG   
1365 C  CD   . GLU   A 196 ? 0.0345 0.1583 0.4455 0.0093  0.0021  -0.0557 403 GLU   A CD   
1366 O  OE1  . GLU   A 196 ? 0.1919 0.0953 0.5162 0.1035  -0.0201 -0.0474 403 GLU   A OE1  
1367 O  OE2  . GLU   A 196 ? 0.0738 0.1914 0.5436 0.0505  0.0554  -0.0101 403 GLU   A OE2  
1368 N  N    . ALA   A 197 ? 0.1336 0.0509 0.5048 0.0246  0.0203  0.0297  404 ALA   A N    
1369 C  CA   . ALA   A 197 ? 0.1842 0.0835 0.4965 0.0645  0.0338  -0.0023 404 ALA   A CA   
1370 C  C    . ALA   A 197 ? 0.1558 0.1049 0.5477 0.0431  0.0264  0.0453  404 ALA   A C    
1371 O  O    . ALA   A 197 ? 0.2982 0.1301 0.7043 0.1344  0.0605  -0.0434 404 ALA   A O    
1372 C  CB   . ALA   A 197 ? 0.1492 0.1755 0.5212 0.1191  0.0042  -0.0298 404 ALA   A CB   
1373 N  N    . GLY   A 198 ? 0.3102 0.1468 0.5326 -0.0285 0.0223  0.0683  405 GLY   A N    
1374 C  CA   . GLY   A 198 ? 0.1278 0.1046 0.5559 0.0826  0.0343  0.0572  405 GLY   A CA   
1375 C  C    . GLY   A 198 ? 0.2584 0.1555 0.6215 0.0247  -0.0071 -0.0011 405 GLY   A C    
1376 O  O    . GLY   A 198 ? 0.3194 0.1256 0.8005 0.0194  -0.0288 0.0217  405 GLY   A O    
1377 N  N    . GLN   A 199 ? 0.2612 0.0813 0.6457 -0.0057 -0.0146 0.0312  406 GLN   A N    
1378 C  CA   . GLN   A 199 ? 0.2657 0.0067 0.6024 -0.0070 0.0218  0.0106  406 GLN   A CA   
1379 C  C    . GLN   A 199 ? 0.2799 0.0115 0.5919 -0.0378 0.0321  -0.0014 406 GLN   A C    
1380 O  O    . GLN   A 199 ? 0.2349 0.0116 0.6651 -0.0310 -0.0030 0.0267  406 GLN   A O    
1381 C  CB   . GLN   A 199 ? 0.2073 0.1459 0.6057 -0.0647 0.1203  0.0192  406 GLN   A CB   
1382 C  CG   . GLN   A 199 ? 0.3408 0.0714 0.7536 -0.1027 0.0078  0.0166  406 GLN   A CG   
1383 C  CD   . GLN   A 199 ? 0.2512 0.1644 0.8221 -0.1796 -0.0080 0.1096  406 GLN   A CD   
1384 O  OE1  . GLN   A 199 ? 0.6009 0.2338 0.6644 -0.1448 -0.0247 0.1225  406 GLN   A OE1  
1385 N  NE2  . GLN   A 199 ? 0.4628 0.3432 0.7806 -0.2998 -0.0785 -0.0159 406 GLN   A NE2  
1386 N  N    . HIS   A 200 ? 0.2231 0.0089 0.5605 0.0236  0.0898  0.0106  407 HIS   A N    
1387 C  CA   . HIS   A 200 ? 0.2983 0.0241 0.5320 0.0397  0.0993  -0.0646 407 HIS   A CA   
1388 C  C    . HIS   A 200 ? 0.2866 0.0402 0.5868 0.0833  0.1096  -0.0375 407 HIS   A C    
1389 O  O    . HIS   A 200 ? 0.2655 0.0786 0.6111 0.0551  0.0760  0.0194  407 HIS   A O    
1390 C  CB   . HIS   A 200 ? 0.2017 0.0480 0.5019 0.0815  0.0107  -0.0042 407 HIS   A CB   
1391 C  CG   . HIS   A 200 ? 0.1729 0.1494 0.5070 0.1127  0.0351  -0.0202 407 HIS   A CG   
1392 N  ND1  . HIS   A 200 ? 0.2384 0.0077 0.5804 0.0178  0.0591  0.0113  407 HIS   A ND1  
1393 C  CD2  . HIS   A 200 ? 0.1807 0.1110 0.4852 0.0771  0.0054  0.0443  407 HIS   A CD2  
1394 C  CE1  . HIS   A 200 ? 0.1834 0.1002 0.6392 0.0284  0.0140  0.0266  407 HIS   A CE1  
1395 N  NE2  . HIS   A 200 ? 0.1661 0.0869 0.6104 0.0324  0.0521  0.0812  407 HIS   A NE2  
1396 N  N    . MET   A 201 ? 0.2626 0.0564 0.6038 0.0853  0.0863  0.0175  408 MET   A N    
1397 C  CA   . MET   A 201 ? 0.2736 0.1300 0.6491 0.0726  0.1364  0.0702  408 MET   A CA   
1398 C  C    . MET   A 201 ? 0.1924 0.1464 0.6516 0.0212  0.0913  0.0097  408 MET   A C    
1399 O  O    . MET   A 201 ? 0.2349 0.1981 0.7330 0.0226  0.1955  -0.0536 408 MET   A O    
1400 C  CB   . MET   A 201 ? 0.4693 0.1653 0.7716 0.1265  0.1013  0.1442  408 MET   A CB   
1401 C  CG   . MET   A 201 ? 0.7704 0.3144 0.7830 0.2727  0.0774  -0.0462 408 MET   A CG   
1402 S  SD   . MET   A 201 ? 0.8744 0.3766 1.2342 0.3269  0.0915  0.1512  408 MET   A SD   
1403 C  CE   . MET   A 201 ? 0.3124 0.5937 1.1765 0.1103  0.2831  0.1327  408 MET   A CE   
1404 N  N    . GLU   A 202 ? 0.2359 0.0407 0.6260 0.0470  0.0595  0.0113  409 GLU   A N    
1405 C  CA   . GLU   A 202 ? 0.2611 0.0437 0.5991 0.0891  0.0938  -0.0261 409 GLU   A CA   
1406 C  C    . GLU   A 202 ? 0.3175 0.0224 0.5254 0.0657  0.1481  0.0366  409 GLU   A C    
1407 O  O    . GLU   A 202 ? 0.3117 0.0774 0.5188 0.0803  0.0885  0.0118  409 GLU   A O    
1408 C  CB   . GLU   A 202 ? 0.2749 0.0610 0.6490 0.1093  0.0592  0.0219  409 GLU   A CB   
1409 C  CG   . GLU   A 202 ? 0.2183 0.1377 0.6510 0.0796  0.0164  -0.0529 409 GLU   A CG   
1410 C  CD   . GLU   A 202 ? 0.1962 0.1642 0.6543 0.0261  0.0972  0.0191  409 GLU   A CD   
1411 O  OE1  . GLU   A 202 ? 0.3082 0.0711 0.6744 0.0190  0.0340  -0.0262 409 GLU   A OE1  
1412 O  OE2  . GLU   A 202 ? 0.1764 0.1375 0.6432 0.0168  0.0598  -0.0105 409 GLU   A OE2  
1413 N  N    . ASP   A 203 ? 0.2039 0.0668 0.5309 -0.0078 0.0737  -0.0278 410 ASP   A N    
1414 C  CA   . ASP   A 203 ? 0.2630 0.0715 0.4984 0.0536  0.0747  -0.0240 410 ASP   A CA   
1415 C  C    . ASP   A 203 ? 0.1022 0.0788 0.4925 0.0555  0.0654  0.0001  410 ASP   A C    
1416 O  O    . ASP   A 203 ? 0.1672 0.0133 0.5106 0.0020  0.0553  -0.0115 410 ASP   A O    
1417 C  CB   . ASP   A 203 ? 0.2384 0.0127 0.5590 0.0102  0.0732  -0.0321 410 ASP   A CB   
1418 C  CG   . ASP   A 203 ? 0.2225 0.0501 0.5012 0.0292  0.0096  0.0855  410 ASP   A CG   
1419 O  OD1  . ASP   A 203 ? 0.3016 0.0079 0.5903 -0.0110 0.1009  -0.0291 410 ASP   A OD1  
1420 O  OD2  . ASP   A 203 ? 0.2023 0.0739 0.6733 0.0188  0.0813  0.0624  410 ASP   A OD2  
1421 N  N    . PRO   A 204 ? 0.1007 0.1620 0.5991 0.0434  0.0643  -0.0221 411 PRO   A N    
1422 C  CA   . PRO   A 204 ? 0.1195 0.0892 0.6598 0.0280  0.0811  -0.0586 411 PRO   A CA   
1423 C  C    . PRO   A 204 ? 0.2224 0.0425 0.5661 -0.0199 0.0451  -0.0159 411 PRO   A C    
1424 O  O    . PRO   A 204 ? 0.1655 0.1851 0.6076 0.0005  0.0422  -0.0746 411 PRO   A O    
1425 C  CB   . PRO   A 204 ? 0.0603 0.0634 0.7407 0.0265  0.0097  -0.0914 411 PRO   A CB   
1426 C  CG   . PRO   A 204 ? 0.1771 0.3643 0.7130 -0.0442 0.0514  -0.0851 411 PRO   A CG   
1427 C  CD   . PRO   A 204 ? 0.1726 0.1630 0.6742 0.0099  0.0741  -0.0917 411 PRO   A CD   
1428 N  N    . ARG   A 205 ? 0.2136 0.0637 0.5648 0.0295  0.0764  -0.0223 412 ARG   A N    
1429 C  CA   . ARG   A 205 ? 0.1594 0.0462 0.6142 -0.0081 0.1339  -0.0126 412 ARG   A CA   
1430 C  C    . ARG   A 205 ? 0.1659 0.0512 0.5039 0.0030  0.1324  0.1129  412 ARG   A C    
1431 O  O    . ARG   A 205 ? 0.1822 0.0125 0.4851 -0.0155 0.0644  0.0038  412 ARG   A O    
1432 C  CB   . ARG   A 205 ? 0.3667 0.0679 0.6378 0.0950  0.2662  -0.0420 412 ARG   A CB   
1433 C  CG   . ARG   A 205 ? 0.3978 0.0413 0.7920 0.0199  0.2924  0.0074  412 ARG   A CG   
1434 C  CD   . ARG   A 205 ? 0.7253 0.0985 0.7713 0.1413  0.3007  0.0901  412 ARG   A CD   
1435 N  NE   . ARG   A 205 ? 0.8304 0.1478 0.7220 0.0238  0.3892  0.0375  412 ARG   A NE   
1436 C  CZ   . ARG   A 205 ? 0.6199 0.3139 0.7073 0.1409  0.3178  0.1175  412 ARG   A CZ   
1437 N  NH1  . ARG   A 205 ? 0.5892 0.1537 0.9685 0.1900  0.3382  0.1808  412 ARG   A NH1  
1438 N  NH2  . ARG   A 205 ? 0.8360 0.2420 0.7109 0.0134  0.4178  0.0822  412 ARG   A NH2  
1439 N  N    . ARG   A 206 ? 0.1335 0.0192 0.4602 -0.0271 0.0877  0.0340  413 ARG   A N    
1440 C  CA   . ARG   A 206 ? 0.1034 0.0258 0.4447 -0.0218 0.0519  0.0455  413 ARG   A CA   
1441 C  C    . ARG   A 206 ? 0.0344 0.0558 0.4171 -0.0121 0.0387  0.0359  413 ARG   A C    
1442 O  O    . ARG   A 206 ? 0.0330 0.0453 0.4439 -0.0105 0.0056  -0.0050 413 ARG   A O    
1443 C  CB   . ARG   A 206 ? 0.1520 0.0064 0.4522 0.0043  0.0907  0.0037  413 ARG   A CB   
1444 C  CG   . ARG   A 206 ? 0.1595 0.0445 0.4841 0.0015  0.0718  -0.0052 413 ARG   A CG   
1445 C  CD   . ARG   A 206 ? 0.1460 0.0753 0.4650 -0.0448 0.0085  0.0316  413 ARG   A CD   
1446 N  NE   . ARG   A 206 ? 0.1906 0.0074 0.5257 0.0025  0.0277  -0.0227 413 ARG   A NE   
1447 C  CZ   . ARG   A 206 ? 0.1799 0.0108 0.4897 0.0087  0.0311  -0.0424 413 ARG   A CZ   
1448 N  NH1  . ARG   A 206 ? 0.1036 0.1129 0.4945 -0.0545 0.0510  -0.0511 413 ARG   A NH1  
1449 N  NH2  . ARG   A 206 ? 0.1172 0.0824 0.5566 -0.0064 0.0083  -0.0522 413 ARG   A NH2  
1450 N  N    . ALA   A 207 ? 0.0357 0.0613 0.4147 0.0275  0.0245  -0.0030 414 ALA   A N    
1451 C  CA   . ALA   A 207 ? 0.0234 0.0800 0.3623 -0.0112 0.0523  0.0304  414 ALA   A CA   
1452 C  C    . ALA   A 207 ? 0.1350 0.1057 0.3239 0.0230  0.0401  0.0554  414 ALA   A C    
1453 O  O    . ALA   A 207 ? 0.0993 0.1075 0.3866 -0.0172 0.0432  -0.0069 414 ALA   A O    
1454 C  CB   . ALA   A 207 ? 0.1124 0.0729 0.4320 -0.0101 -0.0281 -0.0071 414 ALA   A CB   
1455 N  N    . GLY   A 208 ? 0.0316 0.1127 0.4391 0.0478  0.0562  0.0367  415 GLY   A N    
1456 C  CA   . GLY   A 208 ? 0.0837 0.0728 0.4684 0.0603  0.0247  -0.0004 415 GLY   A CA   
1457 C  C    . GLY   A 208 ? 0.0767 0.0103 0.4081 0.0142  0.0288  -0.0155 415 GLY   A C    
1458 O  O    . GLY   A 208 ? 0.0534 0.0196 0.5092 0.0241  0.0277  0.0356  415 GLY   A O    
1459 N  N    . LYS   A 209 ? 0.1436 0.0403 0.3942 0.0400  -0.0521 -0.0223 416 LYS   A N    
1460 C  CA   . LYS   A 209 ? 0.1167 0.0205 0.3726 -0.0221 -0.0326 0.0170  416 LYS   A CA   
1461 C  C    . LYS   A 209 ? 0.1742 0.0972 0.3906 0.0456  -0.0039 0.0500  416 LYS   A C    
1462 O  O    . LYS   A 209 ? 0.0927 0.0094 0.4620 -0.0164 0.0013  -0.0008 416 LYS   A O    
1463 C  CB   . LYS   A 209 ? 0.2152 0.0305 0.4415 -0.0636 0.0121  0.0420  416 LYS   A CB   
1464 C  CG   . LYS   A 209 ? 0.1666 0.0791 0.4669 -0.0602 0.0013  0.0422  416 LYS   A CG   
1465 C  CD   . LYS   A 209 ? 0.4059 0.0910 0.5564 -0.0779 0.0528  0.0168  416 LYS   A CD   
1466 C  CE   . LYS   A 209 ? 0.4346 0.0866 0.4978 -0.0439 0.0523  0.0139  416 LYS   A CE   
1467 N  NZ   . LYS   A 209 ? 0.5161 0.1429 0.6764 -0.0540 -0.0671 -0.0337 416 LYS   A NZ   
1468 N  N    . MET   A 210 ? 0.1137 0.0151 0.3907 0.0301  -0.0011 0.0108  417 MET   A N    
1469 C  CA   . MET   A 210 ? 0.1197 0.0783 0.4037 -0.0148 -0.0109 -0.0328 417 MET   A CA   
1470 C  C    . MET   A 210 ? 0.0097 0.0557 0.4236 0.0114  -0.0212 -0.0163 417 MET   A C    
1471 O  O    . MET   A 210 ? 0.0168 0.0911 0.4761 0.0267  0.0473  0.0557  417 MET   A O    
1472 C  CB   . MET   A 210 ? 0.1203 0.1273 0.3997 -0.0013 0.0490  -0.0152 417 MET   A CB   
1473 C  CG   . MET   A 210 ? 0.0675 0.1174 0.4712 0.0236  0.0728  -0.0485 417 MET   A CG   
1474 S  SD   . MET   A 210 ? 0.0916 0.1138 0.5646 -0.0330 0.0334  -0.0538 417 MET   A SD   
1475 C  CE   . MET   A 210 ? 0.2264 0.0653 0.6378 -0.0060 0.0277  -0.0528 417 MET   A CE   
1476 N  N    . LEU   A 211 ? 0.0276 0.0353 0.4425 -0.0248 0.0056  -0.0004 418 LEU   A N    
1477 C  CA   . LEU   A 211 ? 0.0222 0.0477 0.4264 -0.0223 -0.0332 -0.0118 418 LEU   A CA   
1478 C  C    . LEU   A 211 ? 0.0487 0.0592 0.3577 -0.0282 -0.0440 -0.0324 418 LEU   A C    
1479 O  O    . LEU   A 211 ? 0.1632 0.0112 0.4505 -0.0261 -0.0063 -0.0154 418 LEU   A O    
1480 C  CB   . LEU   A 211 ? 0.0255 0.0653 0.4197 -0.0333 0.0218  -0.0592 418 LEU   A CB   
1481 C  CG   . LEU   A 211 ? 0.0661 0.0792 0.4351 -0.0591 -0.0291 -0.0484 418 LEU   A CG   
1482 C  CD1  . LEU   A 211 ? 0.0419 0.0740 0.4599 -0.0490 -0.0328 0.0394  418 LEU   A CD1  
1483 C  CD2  . LEU   A 211 ? 0.1205 0.0229 0.4059 -0.0435 -0.0493 0.0229  418 LEU   A CD2  
1484 N  N    . MET   A 212 ? 0.0541 0.0248 0.3791 -0.0286 -0.0155 -0.0129 419 MET   A N    
1485 C  CA   . MET   A 212 ? 0.0666 0.1004 0.4079 -0.0752 -0.0202 0.0327  419 MET   A CA   
1486 C  C    . MET   A 212 ? 0.0486 0.0917 0.3282 -0.0485 -0.0282 0.0318  419 MET   A C    
1487 O  O    . MET   A 212 ? 0.1044 0.1065 0.3937 -0.0405 -0.0442 0.0385  419 MET   A O    
1488 C  CB   . MET   A 212 ? 0.0950 0.0715 0.4375 -0.0755 -0.0305 0.0067  419 MET   A CB   
1489 C  CG   . MET   A 212 ? 0.0505 0.1169 0.4579 -0.0220 0.0305  0.0121  419 MET   A CG   
1490 S  SD   . MET   A 212 ? 0.0865 0.1948 0.5274 -0.0352 0.0469  -0.0305 419 MET   A SD   
1491 C  CE   . MET   A 212 ? 0.2012 0.0277 0.6033 -0.0499 0.0694  0.0504  419 MET   A CE   
1492 N  N    . THR   A 213 ? 0.0440 0.0903 0.4084 -0.0317 0.0492  0.0112  420 THR   A N    
1493 C  CA   . THR   A 213 ? 0.0532 0.1112 0.4045 -0.0678 0.0138  0.0317  420 THR   A CA   
1494 C  C    . THR   A 213 ? 0.0746 0.0943 0.4263 -0.0686 -0.0227 0.0203  420 THR   A C    
1495 O  O    . THR   A 213 ? 0.0696 0.0943 0.4749 -0.0559 -0.0366 0.0275  420 THR   A O    
1496 C  CB   . THR   A 213 ? 0.0359 0.0668 0.3847 -0.0395 0.0284  0.0137  420 THR   A CB   
1497 O  OG1  . THR   A 213 ? 0.1329 0.0234 0.4258 -0.0229 0.0351  0.0175  420 THR   A OG1  
1498 C  CG2  . THR   A 213 ? 0.0315 0.0873 0.4507 -0.0059 0.0075  -0.0039 420 THR   A CG2  
1499 N  N    . LEU   A 214 ? 0.0430 0.0802 0.3901 -0.0296 -0.0110 0.0304  421 LEU   A N    
1500 C  CA   . LEU   A 214 ? 0.0450 0.0696 0.3530 -0.0435 0.0087  0.0505  421 LEU   A CA   
1501 C  C    . LEU   A 214 ? 0.0886 0.0516 0.3636 -0.0183 0.0003  0.0128  421 LEU   A C    
1502 O  O    . LEU   A 214 ? 0.0960 0.0698 0.4320 0.0143  -0.0123 -0.0301 421 LEU   A O    
1503 C  CB   . LEU   A 214 ? 0.0392 0.1331 0.3939 0.0333  -0.0092 0.0573  421 LEU   A CB   
1504 C  CG   . LEU   A 214 ? 0.1279 0.0991 0.3634 0.0027  -0.0206 0.0235  421 LEU   A CG   
1505 C  CD1  . LEU   A 214 ? 0.1492 0.0104 0.4718 0.0239  -0.0616 -0.0059 421 LEU   A CD1  
1506 C  CD2  . LEU   A 214 ? 0.1946 0.0226 0.4316 0.0113  0.0170  0.0538  421 LEU   A CD2  
1507 N  N    . PRO   A 215 ? 0.0434 0.0733 0.4146 -0.0129 0.0239  0.0229  422 PRO   A N    
1508 C  CA   . PRO   A 215 ? 0.0129 0.0694 0.4279 -0.0079 -0.0108 0.0160  422 PRO   A CA   
1509 C  C    . PRO   A 215 ? 0.0108 0.0743 0.4484 0.0025  -0.0075 -0.0563 422 PRO   A C    
1510 O  O    . PRO   A 215 ? 0.0530 0.0123 0.4179 0.0042  -0.0012 0.0020  422 PRO   A O    
1511 C  CB   . PRO   A 215 ? 0.1099 0.0144 0.4017 0.0284  -0.0181 0.0059  422 PRO   A CB   
1512 C  CG   . PRO   A 215 ? 0.0710 0.0097 0.4708 -0.0135 -0.0417 0.0254  422 PRO   A CG   
1513 C  CD   . PRO   A 215 ? 0.0289 0.0488 0.4352 -0.0294 0.0238  0.0099  422 PRO   A CD   
1514 N  N    . LEU   A 216 ? 0.0375 0.0152 0.4013 0.0146  -0.0303 -0.0043 423 LEU   A N    
1515 C  CA   . LEU   A 216 ? 0.0396 0.0200 0.4424 0.0090  -0.0403 0.0167  423 LEU   A CA   
1516 C  C    . LEU   A 216 ? 0.0936 0.0950 0.3620 0.0456  -0.0753 -0.0414 423 LEU   A C    
1517 O  O    . LEU   A 216 ? 0.0599 0.0343 0.4984 0.0051  -0.0504 -0.0077 423 LEU   A O    
1518 C  CB   . LEU   A 216 ? 0.0824 0.0668 0.4548 -0.0423 -0.0473 0.0119  423 LEU   A CB   
1519 C  CG   . LEU   A 216 ? 0.0778 0.1490 0.4058 -0.0390 -0.0367 0.0053  423 LEU   A CG   
1520 C  CD1  . LEU   A 216 ? 0.1000 0.2437 0.4258 0.0243  -0.0152 0.0385  423 LEU   A CD1  
1521 C  CD2  . LEU   A 216 ? 0.2163 0.2286 0.4037 0.0141  -0.0712 -0.0174 423 LEU   A CD2  
1522 N  N    . LEU   A 217 ? 0.0379 0.1402 0.4101 -0.0045 -0.0541 0.0305  424 LEU   A N    
1523 C  CA   . LEU   A 217 ? 0.0488 0.0558 0.3904 -0.0323 -0.0534 -0.0166 424 LEU   A CA   
1524 C  C    . LEU   A 217 ? 0.0083 0.0697 0.3948 0.0106  0.0060  -0.0251 424 LEU   A C    
1525 O  O    . LEU   A 217 ? 0.0194 0.0655 0.4855 0.0232  0.0421  -0.0039 424 LEU   A O    
1526 C  CB   . LEU   A 217 ? 0.0358 0.1142 0.4361 -0.0148 -0.0693 0.0103  424 LEU   A CB   
1527 C  CG   . LEU   A 217 ? 0.0983 0.1018 0.4488 -0.0261 -0.0473 0.0138  424 LEU   A CG   
1528 C  CD1  . LEU   A 217 ? 0.0969 0.1019 0.4457 -0.0215 -0.0462 0.0357  424 LEU   A CD1  
1529 C  CD2  . LEU   A 217 ? 0.1037 0.1823 0.5005 -0.0314 -0.0546 0.0580  424 LEU   A CD2  
1530 N  N    . ARG   A 218 ? 0.0067 0.0987 0.4755 0.0036  0.0103  -0.0269 425 ARG   A N    
1531 C  CA   . ARG   A 218 ? 0.0555 0.1275 0.4468 0.0462  -0.0323 -0.0476 425 ARG   A CA   
1532 C  C    . ARG   A 218 ? 0.0685 0.1256 0.3729 0.0058  -0.0244 -0.0063 425 ARG   A C    
1533 O  O    . ARG   A 218 ? 0.0556 0.0983 0.4710 -0.0182 0.0278  0.0086  425 ARG   A O    
1534 C  CB   . ARG   A 218 ? 0.0682 0.0599 0.4871 0.0363  -0.0521 -0.0501 425 ARG   A CB   
1535 C  CG   . ARG   A 218 ? 0.0986 0.0336 0.4771 0.0461  -0.0468 -0.0200 425 ARG   A CG   
1536 C  CD   . ARG   A 218 ? 0.1123 0.0237 0.4689 0.0221  -0.0151 -0.0413 425 ARG   A CD   
1537 N  NE   . ARG   A 218 ? 0.0955 0.0810 0.4608 -0.0391 -0.0630 -0.0180 425 ARG   A NE   
1538 C  CZ   . ARG   A 218 ? 0.0974 0.0562 0.4636 -0.0338 -0.0724 -0.0192 425 ARG   A CZ   
1539 N  NH1  . ARG   A 218 ? 0.1470 0.1012 0.4992 -0.0518 -0.0158 0.0117  425 ARG   A NH1  
1540 N  NH2  . ARG   A 218 ? 0.0217 0.1361 0.4972 -0.0264 -0.0367 0.0294  425 ARG   A NH2  
1541 N  N    . GLN   A 219 ? 0.0782 0.0746 0.3963 0.0329  -0.0492 -0.0121 426 GLN   A N    
1542 C  CA   . GLN   A 219 ? 0.0101 0.1957 0.4020 0.0123  -0.0310 0.0457  426 GLN   A CA   
1543 C  C    . GLN   A 219 ? 0.0308 0.1443 0.4841 -0.0039 0.0251  0.0564  426 GLN   A C    
1544 O  O    . GLN   A 219 ? 0.0465 0.1708 0.4936 0.0474  -0.0202 0.0550  426 GLN   A O    
1545 C  CB   . GLN   A 219 ? 0.0509 0.1787 0.4466 0.0051  -0.0047 0.0694  426 GLN   A CB   
1546 C  CG   . GLN   A 219 ? 0.0717 0.2155 0.5079 0.0461  -0.0069 0.1070  426 GLN   A CG   
1547 C  CD   . GLN   A 219 ? 0.0974 0.5347 0.5183 0.0203  -0.0069 0.0382  426 GLN   A CD   
1548 O  OE1  . GLN   A 219 ? 0.1388 0.2733 0.4615 -0.0211 0.0229  0.0603  426 GLN   A OE1  
1549 N  NE2  . GLN   A 219 ? 0.2470 0.4954 0.7634 0.1067  -0.2433 0.0870  426 GLN   A NE2  
1550 N  N    . THR   A 220 ? 0.0401 0.1610 0.5237 -0.0367 -0.0024 0.0313  427 THR   A N    
1551 C  CA   . THR   A 220 ? 0.0175 0.1224 0.5149 0.0090  -0.0090 0.0760  427 THR   A CA   
1552 C  C    . THR   A 220 ? 0.0094 0.1261 0.4947 0.0178  -0.0058 0.0597  427 THR   A C    
1553 O  O    . THR   A 220 ? 0.0093 0.2495 0.5953 0.0267  -0.0018 0.0184  427 THR   A O    
1554 C  CB   . THR   A 220 ? 0.0498 0.1586 0.5282 0.0062  -0.0282 0.0137  427 THR   A CB   
1555 O  OG1  . THR   A 220 ? 0.1954 0.1797 0.5019 -0.0468 -0.0474 0.0365  427 THR   A OG1  
1556 C  CG2  . THR   A 220 ? 0.0824 0.1167 0.6595 -0.0432 -0.0730 0.0629  427 THR   A CG2  
1557 N  N    . SER   A 221 ? 0.0086 0.1865 0.4912 0.0202  0.0094  0.0477  428 SER   A N    
1558 C  CA   . SER   A 221 ? 0.0797 0.1469 0.5067 0.0581  -0.0239 0.0343  428 SER   A CA   
1559 C  C    . SER   A 221 ? 0.0851 0.1395 0.4498 0.0328  0.0420  0.0010  428 SER   A C    
1560 O  O    . SER   A 221 ? 0.0870 0.1869 0.5292 0.0443  0.0855  0.0192  428 SER   A O    
1561 C  CB   . SER   A 221 ? 0.1867 0.4563 0.4637 0.1837  0.0039  0.1124  428 SER   A CB   
1562 O  OG   . SER   A 221 ? 0.1776 0.5573 0.5262 0.0996  -0.0245 0.0696  428 SER   A OG   
1563 N  N    . THR   A 222 ? 0.0752 0.2109 0.4972 0.0351  0.0249  0.0666  429 THR   A N    
1564 C  CA   . THR   A 222 ? 0.0847 0.2105 0.6951 0.0437  0.0024  -0.0099 429 THR   A CA   
1565 C  C    . THR   A 222 ? 0.1074 0.2421 0.5276 0.0603  0.0322  0.0154  429 THR   A C    
1566 O  O    . THR   A 222 ? 0.2346 0.1775 0.6135 0.1462  0.0526  0.0339  429 THR   A O    
1567 C  CB   . THR   A 222 ? 0.1559 0.0915 0.7437 -0.0016 0.0184  -0.0712 429 THR   A CB   
1568 O  OG1  . THR   A 222 ? 0.1618 0.1577 0.7587 -0.0608 0.0583  0.0622  429 THR   A OG1  
1569 C  CG2  . THR   A 222 ? 0.2086 0.1358 0.8987 0.1368  -0.0095 -0.0504 429 THR   A CG2  
1570 N  N    . LYS   A 223 ? 0.0475 0.1647 0.5152 0.0237  0.0332  0.0764  430 LYS   A N    
1571 C  CA   . LYS   A 223 ? 0.0087 0.2429 0.7135 -0.0127 0.0256  0.1400  430 LYS   A CA   
1572 C  C    . LYS   A 223 ? 0.0829 0.1810 0.5831 0.0392  0.0653  0.0763  430 LYS   A C    
1573 O  O    . LYS   A 223 ? 0.1363 0.3026 0.6565 0.1464  0.0302  0.1453  430 LYS   A O    
1574 C  CB   . LYS   A 223 ? 0.1522 0.2402 0.7828 0.1527  -0.0953 0.1057  430 LYS   A CB   
1575 C  CG   . LYS   A 223 ? 0.4710 0.3868 0.8142 0.0050  -0.2992 0.1771  430 LYS   A CG   
1576 C  CD   . LYS   A 223 ? 0.8863 0.6548 0.7956 -0.0509 -0.2004 0.1846  430 LYS   A CD   
1577 C  CE   . LYS   A 223 ? 0.7836 0.4164 1.0987 -0.3437 -0.1894 0.3225  430 LYS   A CE   
1578 N  NZ   . LYS   A 223 ? 0.1961 0.7084 1.2826 -0.0489 -0.1851 0.4675  430 LYS   A NZ   
1579 N  N    . ALA   A 224 ? 0.0868 0.2079 0.5367 0.0336  0.0049  0.0872  431 ALA   A N    
1580 C  CA   . ALA   A 224 ? 0.0695 0.1925 0.4944 0.0590  0.0092  0.0560  431 ALA   A CA   
1581 C  C    . ALA   A 224 ? 0.1007 0.2004 0.4824 0.0871  0.0012  0.0805  431 ALA   A C    
1582 O  O    . ALA   A 224 ? 0.1295 0.1216 0.5766 0.0726  0.0757  0.0686  431 ALA   A O    
1583 C  CB   . ALA   A 224 ? 0.0399 0.1812 0.6162 0.0757  -0.0085 0.0317  431 ALA   A CB   
1584 N  N    . VAL   A 225 ? 0.0740 0.1791 0.5427 0.0764  0.0299  0.0019  432 VAL   A N    
1585 C  CA   . VAL   A 225 ? 0.0492 0.1587 0.5498 0.0665  -0.0034 0.0150  432 VAL   A CA   
1586 C  C    . VAL   A 225 ? 0.1470 0.2041 0.5193 0.1130  0.0384  0.0655  432 VAL   A C    
1587 O  O    . VAL   A 225 ? 0.1379 0.1142 0.6791 0.0674  0.0902  0.0315  432 VAL   A O    
1588 C  CB   . VAL   A 225 ? 0.0195 0.1616 0.5904 0.0391  0.0428  -0.0049 432 VAL   A CB   
1589 C  CG1  . VAL   A 225 ? 0.1575 0.1707 0.7380 0.0599  0.0564  -0.0688 432 VAL   A CG1  
1590 C  CG2  . VAL   A 225 ? 0.2688 0.1215 0.6159 0.1177  0.1428  -0.0068 432 VAL   A CG2  
1591 N  N    . GLN   A 226 ? 0.0864 0.1907 0.6006 0.0532  0.0578  0.0849  433 GLN   A N    
1592 C  CA   . GLN   A 226 ? 0.1305 0.1525 0.6412 0.0496  0.0460  0.0667  433 GLN   A CA   
1593 C  C    . GLN   A 226 ? 0.1187 0.1955 0.6078 0.0582  0.0614  0.0675  433 GLN   A C    
1594 O  O    . GLN   A 226 ? 0.1917 0.1694 0.7579 0.0723  0.0780  0.0318  433 GLN   A O    
1595 C  CB   . GLN   A 226 ? 0.1970 0.2892 0.7274 0.0206  0.1154  0.1445  433 GLN   A CB   
1596 C  CG   . GLN   A 226 ? 0.4579 0.3351 0.8190 -0.1600 0.0357  0.0837  433 GLN   A CG   
1597 C  CD   . GLN   A 226 ? 0.6323 0.5023 0.7809 -0.2896 0.0740  0.0785  433 GLN   A CD   
1598 O  OE1  . GLN   A 226 ? 1.0747 0.5763 0.6360 0.1005  0.2684  0.0125  433 GLN   A OE1  
1599 N  NE2  . GLN   A 226 ? 0.7524 0.3987 1.2145 -0.4587 0.3151  -0.0904 433 GLN   A NE2  
1600 N  N    . HIS   A 227 ? 0.1396 0.1907 0.6817 0.0697  0.0678  0.0580  434 HIS   A N    
1601 C  CA   . HIS   A 227 ? 0.1492 0.2626 0.7013 0.0449  0.0642  0.0749  434 HIS   A CA   
1602 C  C    . HIS   A 227 ? 0.1533 0.3282 0.7154 0.1336  0.0642  0.1382  434 HIS   A C    
1603 O  O    . HIS   A 227 ? 0.1045 0.2967 0.8154 0.0977  0.0088  0.2151  434 HIS   A O    
1604 C  CB   . HIS   A 227 ? 0.0823 0.2901 0.6834 0.1421  0.0701  0.0830  434 HIS   A CB   
1605 C  CG   . HIS   A 227 ? 0.1377 0.2736 0.6917 0.1554  -0.0418 0.1195  434 HIS   A CG   
1606 N  ND1  . HIS   A 227 ? 0.1662 0.4841 0.7899 -0.0085 -0.1909 0.2206  434 HIS   A ND1  
1607 C  CD2  . HIS   A 227 ? 0.2288 0.1750 0.6451 0.0480  -0.0422 0.0165  434 HIS   A CD2  
1608 C  CE1  . HIS   A 227 ? 0.1751 0.5718 0.7721 -0.1086 -0.0691 0.1321  434 HIS   A CE1  
1609 N  NE2  . HIS   A 227 ? 0.2047 0.2793 0.8630 0.0724  -0.0539 0.1750  434 HIS   A NE2  
1610 N  N    . PHE   A 228 ? 0.1657 0.2212 0.6368 0.0838  0.0620  0.0430  435 PHE   A N    
1611 C  CA   . PHE   A 228 ? 0.1156 0.1935 0.6330 0.0578  0.0803  0.0095  435 PHE   A CA   
1612 C  C    . PHE   A 228 ? 0.1485 0.2066 0.6661 -0.0247 0.0886  0.0162  435 PHE   A C    
1613 O  O    . PHE   A 228 ? 0.1491 0.2109 0.7772 0.0470  0.1070  0.0137  435 PHE   A O    
1614 C  CB   . PHE   A 228 ? 0.0929 0.1976 0.6203 0.1200  0.0152  -0.0709 435 PHE   A CB   
1615 C  CG   . PHE   A 228 ? 0.0213 0.2116 0.5661 0.0362  0.0487  -0.0180 435 PHE   A CG   
1616 C  CD1  . PHE   A 228 ? 0.0427 0.3117 0.6178 0.0771  0.0922  -0.0355 435 PHE   A CD1  
1617 C  CD2  . PHE   A 228 ? 0.1479 0.2322 0.5446 0.0555  0.0728  -0.0130 435 PHE   A CD2  
1618 C  CE1  . PHE   A 228 ? 0.1899 0.2601 0.6047 0.0549  0.0682  -0.0214 435 PHE   A CE1  
1619 C  CE2  . PHE   A 228 ? 0.1141 0.1487 0.5801 0.0666  0.0983  0.0437  435 PHE   A CE2  
1620 C  CZ   . PHE   A 228 ? 0.0877 0.2128 0.5726 0.1030  0.0584  0.0665  435 PHE   A CZ   
1621 N  N    . TYR   A 229 ? 0.0439 0.1461 0.9307 0.0724  -0.0207 -0.0218 436 TYR   A N    
1622 C  CA   . TYR   A 229 ? 0.1876 0.2121 0.8325 0.0531  0.0474  -0.0458 436 TYR   A CA   
1623 C  C    . TYR   A 229 ? 0.1448 0.3560 0.7711 0.1005  -0.0056 -0.0669 436 TYR   A C    
1624 O  O    . TYR   A 229 ? 0.1914 0.1797 0.8370 0.0616  0.0747  -0.0213 436 TYR   A O    
1625 C  CB   . TYR   A 229 ? 0.1201 0.2787 0.8048 0.0663  0.0543  -0.0968 436 TYR   A CB   
1626 C  CG   . TYR   A 229 ? 0.2450 0.1948 0.7658 -0.0424 0.2549  -0.0268 436 TYR   A CG   
1627 C  CD1  . TYR   A 229 ? 0.3562 0.2660 0.8059 -0.0105 0.0873  -0.0968 436 TYR   A CD1  
1628 C  CD2  . TYR   A 229 ? 0.4751 0.2276 0.7602 -0.1218 0.1378  0.0455  436 TYR   A CD2  
1629 C  CE1  . TYR   A 229 ? 0.6483 0.4115 0.8061 -0.0266 0.0772  -0.1624 436 TYR   A CE1  
1630 C  CE2  . TYR   A 229 ? 0.3325 0.3271 0.8202 -0.0806 -0.0055 -0.0688 436 TYR   A CE2  
1631 C  CZ   . TYR   A 229 ? 0.5700 0.4426 0.8700 -0.0475 0.0031  -0.0716 436 TYR   A CZ   
1632 O  OH   . TYR   A 229 ? 0.6151 0.3091 1.3140 -0.0956 -0.1320 -0.1163 436 TYR   A OH   
1633 N  N    . ASN   A 230 ? 0.1361 0.1731 0.7911 0.0515  0.0219  0.0923  437 ASN   A N    
1634 C  CA   . ASN   A 230 ? 0.1838 0.1647 0.8562 0.0845  -0.0048 0.0828  437 ASN   A CA   
1635 C  C    . ASN   A 230 ? 0.1947 0.1719 0.8429 0.0919  0.0357  0.0424  437 ASN   A C    
1636 O  O    . ASN   A 230 ? 0.1678 0.1377 0.9908 0.0677  0.0689  0.0816  437 ASN   A O    
1637 C  CB   . ASN   A 230 ? 0.2894 0.2104 0.7950 0.0164  -0.0616 0.2176  437 ASN   A CB   
1638 C  CG   . ASN   A 230 ? 0.3997 0.4214 0.8753 0.0316  0.1280  0.1932  437 ASN   A CG   
1639 O  OD1  . ASN   A 230 ? 0.2834 0.3211 1.2016 0.1165  0.1701  0.1123  437 ASN   A OD1  
1640 N  ND2  . ASN   A 230 ? 0.4543 0.6169 0.8886 0.4386  0.2794  0.2896  437 ASN   A ND2  
1641 N  N    . ILE   A 231 ? 0.0811 0.2333 0.8452 0.0080  0.0978  0.0977  438 ILE   A N    
1642 C  CA   . ILE   A 231 ? 0.0813 0.1792 0.7835 0.0692  0.1089  0.1813  438 ILE   A CA   
1643 C  C    . ILE   A 231 ? 0.1535 0.2623 0.7730 0.0271  0.1043  0.1446  438 ILE   A C    
1644 O  O    . ILE   A 231 ? 0.2380 0.2679 0.7788 0.1072  0.1715  0.1298  438 ILE   A O    
1645 C  CB   . ILE   A 231 ? 0.2006 0.1863 0.8710 0.0890  0.0490  0.2412  438 ILE   A CB   
1646 C  CG1  . ILE   A 231 ? 0.1977 0.3853 0.9074 0.0959  0.2307  0.1948  438 ILE   A CG1  
1647 C  CG2  . ILE   A 231 ? 0.1938 0.2324 1.0281 0.0680  0.1704  0.0708  438 ILE   A CG2  
1648 C  CD1  . ILE   A 231 ? 0.3052 0.3718 1.0279 0.0179  0.2112  0.1812  438 ILE   A CD1  
1649 N  N    . LYS   A 232 ? 0.1217 0.2163 0.7859 0.0681  0.0686  0.0364  439 LYS   A N    
1650 C  CA   . LYS   A 232 ? 0.2862 0.1795 0.8395 0.0681  0.1235  -0.0082 439 LYS   A CA   
1651 C  C    . LYS   A 232 ? 0.2194 0.1737 0.8556 0.0550  0.1446  -0.0652 439 LYS   A C    
1652 O  O    . LYS   A 232 ? 0.3025 0.3807 0.9101 0.1849  0.1989  -0.0297 439 LYS   A O    
1653 C  CB   . LYS   A 232 ? 0.2129 0.1208 0.8519 -0.0381 0.1991  -0.0816 439 LYS   A CB   
1654 C  CG   . LYS   A 232 ? 0.1611 0.3123 0.9096 0.0148  0.2018  -0.1017 439 LYS   A CG   
1655 C  CD   . LYS   A 232 ? 0.3706 0.4110 0.9744 -0.1138 0.1065  -0.2780 439 LYS   A CD   
1656 C  CE   . LYS   A 232 ? 0.5329 0.1342 1.3218 0.1211  0.1643  -0.1281 439 LYS   A CE   
1657 N  NZ   . LYS   A 232 ? 0.5099 0.7532 1.3639 -0.0175 0.3745  -0.1325 439 LYS   A NZ   
1658 N  N    . LEU   A 233 ? 0.2064 0.2102 0.9962 0.1194  0.1447  0.0470  440 LEU   A N    
1659 C  CA   . LEU   A 233 ? 0.1040 0.1710 1.1020 0.0369  0.1886  0.0239  440 LEU   A CA   
1660 C  C    . LEU   A 233 ? 0.1255 0.1663 1.0154 0.0201  0.1426  0.0451  440 LEU   A C    
1661 O  O    . LEU   A 233 ? 0.2741 0.1607 1.2505 0.1183  0.1532  0.0327  440 LEU   A O    
1662 C  CB   . LEU   A 233 ? 0.3068 0.2713 1.1589 -0.0110 0.2923  -0.0017 440 LEU   A CB   
1663 C  CG   . LEU   A 233 ? 0.3900 0.0451 1.3263 -0.0233 0.1633  0.0801  440 LEU   A CG   
1664 C  CD1  . LEU   A 233 ? 0.3304 0.2991 1.3837 -0.1423 0.3394  -0.0001 440 LEU   A CD1  
1665 C  CD2  . LEU   A 233 ? 0.4387 0.3874 1.3556 0.0937  0.2253  -0.0740 440 LEU   A CD2  
1666 N  N    . GLU   A 234 ? 0.2611 0.1652 0.9550 0.0966  0.1571  0.0111  441 GLU   A N    
1667 C  CA   . GLU   A 234 ? 0.2615 0.2914 1.1410 0.2061  0.1148  0.0020  441 GLU   A CA   
1668 C  C    . GLU   A 234 ? 0.1462 0.4618 1.2354 0.2079  0.0234  0.1448  441 GLU   A C    
1669 O  O    . GLU   A 234 ? 0.2177 0.4774 1.5541 0.2463  -0.1099 0.1970  441 GLU   A O    
1670 C  CB   . GLU   A 234 ? 0.3919 0.3564 1.0330 0.1316  0.2581  -0.0282 441 GLU   A CB   
1671 C  CG   . GLU   A 234 ? 0.7483 0.5670 1.0630 0.0286  0.1137  0.1523  441 GLU   A CG   
1672 C  CD   . GLU   A 234 ? 1.2041 0.7494 1.1275 -0.0567 0.0240  0.0231  441 GLU   A CD   
1673 O  OE1  . GLU   A 234 ? 0.9295 0.6027 1.5931 -0.0431 -0.3559 -0.1878 441 GLU   A OE1  
1674 O  OE2  . GLU   A 234 ? 0.9286 0.8868 1.5596 -0.1619 0.1596  0.4944  441 GLU   A OE2  
1675 N  N    . GLY   A 235 ? 0.1006 0.4787 1.0331 0.1989  0.0921  0.0549  442 GLY   A N    
1676 C  CA   . GLY   A 235 ? 0.1969 0.1698 1.1181 0.1719  0.2067  0.0996  442 GLY   A CA   
1677 C  C    . GLY   A 235 ? 0.3260 0.1544 0.9498 0.0958  0.1900  0.0650  442 GLY   A C    
1678 O  O    . GLY   A 235 ? 0.3056 0.3823 0.9269 0.0687  0.1321  0.0002  442 GLY   A O    
1679 N  N    . LYS   A 236 ? 0.2113 0.3416 0.9522 0.0694  0.0880  0.0411  443 LYS   A N    
1680 C  CA   . LYS   A 236 ? 0.1754 0.4502 0.9438 0.0604  0.1140  0.0499  443 LYS   A CA   
1681 C  C    . LYS   A 236 ? 0.0994 0.5216 0.9928 0.0449  0.1164  0.1604  443 LYS   A C    
1682 O  O    . LYS   A 236 ? 0.1180 0.4937 0.9272 0.0358  0.0284  -0.0595 443 LYS   A O    
1683 C  CB   . LYS   A 236 ? 0.3088 0.3380 0.9773 0.1737  0.0378  0.1261  443 LYS   A CB   
1684 C  CG   . LYS   A 236 ? 0.4498 0.3814 1.0234 0.2020  -0.0145 0.1573  443 LYS   A CG   
1685 C  CD   . LYS   A 236 ? 0.4344 0.5408 1.0104 0.2923  -0.0365 0.3043  443 LYS   A CD   
1686 C  CE   . LYS   A 236 ? 0.5940 0.3068 1.1665 0.2024  0.0792  0.3509  443 LYS   A CE   
1687 N  NZ   . LYS   A 236 ? 0.9511 0.7460 1.0726 0.0044  0.0846  0.3007  443 LYS   A NZ   
1688 N  N    . VAL   A 237 ? 0.1609 0.4100 0.8756 0.0474  0.0606  0.1008  444 VAL   A N    
1689 C  CA   . VAL   A 237 ? 0.0366 0.3373 0.7555 0.0188  0.1055  0.0036  444 VAL   A CA   
1690 C  C    . VAL   A 237 ? 0.1995 0.2739 0.7977 -0.0247 0.0689  0.0020  444 VAL   A C    
1691 O  O    . VAL   A 237 ? 0.2058 0.1817 0.8911 -0.0279 0.0996  -0.0445 444 VAL   A O    
1692 C  CB   . VAL   A 237 ? 0.1643 0.2200 0.7899 0.0636  0.1109  -0.0373 444 VAL   A CB   
1693 C  CG1  . VAL   A 237 ? 0.0355 0.3231 0.7494 0.0620  0.1212  0.0990  444 VAL   A CG1  
1694 C  CG2  . VAL   A 237 ? 0.2007 0.1767 0.8029 0.0559  0.1155  0.0679  444 VAL   A CG2  
1695 N  N    . PRO   A 238 ? 0.0693 0.3280 0.7952 0.0433  0.0822  0.0016  445 PRO   A N    
1696 C  CA   . PRO   A 238 ? 0.1916 0.3407 0.8060 0.0874  0.0653  -0.0434 445 PRO   A CA   
1697 C  C    . PRO   A 238 ? 0.1120 0.4029 0.8406 0.0549  -0.0263 -0.0508 445 PRO   A C    
1698 O  O    . PRO   A 238 ? 0.2506 0.4733 0.7477 0.1011  -0.0190 -0.0061 445 PRO   A O    
1699 C  CB   . PRO   A 238 ? 0.3169 0.4008 0.8765 0.0403  0.1630  -0.0293 445 PRO   A CB   
1700 C  CG   . PRO   A 238 ? 0.4260 0.4879 0.8434 0.0006  0.0961  0.0212  445 PRO   A CG   
1701 C  CD   . PRO   A 238 ? 0.1498 0.1952 0.9350 0.0094  0.0087  0.0300  445 PRO   A CD   
1702 N  N    . MET   A 239 ? 0.2243 0.3689 0.6414 0.1885  -0.0275 -0.0535 446 MET   A N    
1703 C  CA   . MET   A 239 ? 0.0861 0.3012 0.6432 0.0424  0.0580  -0.0650 446 MET   A CA   
1704 C  C    . MET   A 239 ? 0.2210 0.4114 0.6766 0.0620  0.0413  0.0167  446 MET   A C    
1705 O  O    . MET   A 239 ? 0.1139 0.4108 0.8031 0.0349  0.0341  0.0251  446 MET   A O    
1706 C  CB   . MET   A 239 ? 0.1103 0.3659 0.6033 0.0398  0.0913  -0.1017 446 MET   A CB   
1707 C  CG   . MET   A 239 ? 0.1586 0.4169 0.6091 0.0348  0.1391  -0.0473 446 MET   A CG   
1708 S  SD   . MET   A 239 ? 0.1912 0.2798 0.6989 0.0270  0.0528  -0.0360 446 MET   A SD   
1709 C  CE   . MET   A 239 ? 0.1729 0.1664 0.7453 0.0878  0.0300  -0.1054 446 MET   A CE   
1710 N  N    . HIS   A 240 ? 0.1461 0.4050 0.6777 0.0060  0.0555  0.0832  447 HIS   A N    
1711 C  CA   . HIS   A 240 ? 0.0403 0.4716 0.6449 -0.0013 0.0795  0.0563  447 HIS   A CA   
1712 C  C    . HIS   A 240 ? 0.1264 0.3477 0.5924 0.0035  0.0268  0.0032  447 HIS   A C    
1713 O  O    . HIS   A 240 ? 0.2537 0.3400 0.6176 0.0240  0.0967  0.0176  447 HIS   A O    
1714 C  CB   . HIS   A 240 ? 0.2163 0.4173 0.7908 -0.1030 0.0856  0.0079  447 HIS   A CB   
1715 C  CG   . HIS   A 240 ? 0.1067 0.7501 1.0616 -0.0607 0.1187  0.1276  447 HIS   A CG   
1716 N  ND1  . HIS   A 240 ? 0.1685 0.6427 0.9910 0.0637  0.0694  0.1062  447 HIS   A ND1  
1717 C  CD2  . HIS   A 240 ? 0.2000 0.7489 1.0508 0.0417  -0.0273 0.1588  447 HIS   A CD2  
1718 C  CE1  . HIS   A 240 ? 0.3149 0.7005 1.2343 -0.1459 0.0621  0.2294  447 HIS   A CE1  
1719 N  NE2  . HIS   A 240 ? 0.2654 0.8193 1.1949 -0.2228 -0.1554 0.3631  447 HIS   A NE2  
1720 N  N    . LYS   A 241 ? 0.1836 0.5496 0.6027 0.0772  0.0472  -0.0630 448 LYS   A N    
1721 C  CA   . LYS   A 241 ? 0.1827 0.5821 0.7012 0.0526  0.0510  -0.1207 448 LYS   A CA   
1722 C  C    . LYS   A 241 ? 0.1285 0.5224 0.6980 -0.0398 0.1104  0.0427  448 LYS   A C    
1723 O  O    . LYS   A 241 ? 0.0889 0.4208 0.6202 -0.0688 0.0449  -0.0724 448 LYS   A O    
1724 C  CB   . LYS   A 241 ? 0.2483 0.6297 0.6771 -0.0426 -0.0784 -0.1344 448 LYS   A CB   
1725 C  CG   . LYS   A 241 ? 0.4844 1.0780 0.8758 0.0929  0.1511  -0.1312 448 LYS   A CG   
1726 C  CD   . LYS   A 241 ? 0.7639 0.9799 1.0292 0.0189  0.1723  -0.0555 448 LYS   A CD   
1727 C  CE   . LYS   A 241 ? 0.5320 0.9452 1.3457 -0.1470 0.0984  -0.0594 448 LYS   A CE   
1728 N  NZ   . LYS   A 241 ? 0.7110 1.5579 1.1189 0.1311  0.0305  -0.2754 448 LYS   A NZ   
1729 N  N    . LEU   A 242 ? 0.0776 0.5232 0.6902 -0.1066 0.1443  -0.0751 449 LEU   A N    
1730 C  CA   . LEU   A 242 ? 0.1370 0.3279 0.6343 -0.0112 0.1094  -0.0889 449 LEU   A CA   
1731 C  C    . LEU   A 242 ? 0.1928 0.2707 0.6068 0.0685  0.0521  -0.0441 449 LEU   A C    
1732 O  O    . LEU   A 242 ? 0.1789 0.3425 0.6171 0.0385  0.0167  -0.1066 449 LEU   A O    
1733 C  CB   . LEU   A 242 ? 0.2284 0.3055 0.6532 -0.0324 0.0915  -0.0135 449 LEU   A CB   
1734 C  CG   . LEU   A 242 ? 0.1644 0.2803 0.6656 -0.0925 0.0031  -0.0232 449 LEU   A CG   
1735 C  CD1  . LEU   A 242 ? 0.1223 0.3621 0.6892 -0.1190 0.0346  -0.0306 449 LEU   A CD1  
1736 C  CD2  . LEU   A 242 ? 0.2655 0.3553 0.6740 0.0109  -0.0232 0.0105  449 LEU   A CD2  
1737 N  N    . PHE   A 243 ? 0.0911 0.4647 0.6434 0.0336  0.1313  -0.0908 450 PHE   A N    
1738 C  CA   . PHE   A 243 ? 0.0373 0.4053 0.6319 0.0297  0.1108  -0.0601 450 PHE   A CA   
1739 C  C    . PHE   A 243 ? 0.1230 0.3779 0.5627 0.0760  0.0938  -0.0404 450 PHE   A C    
1740 O  O    . PHE   A 243 ? 0.1026 0.3608 0.5782 0.0771  0.0505  0.0207  450 PHE   A O    
1741 C  CB   . PHE   A 243 ? 0.1141 0.2933 0.6290 -0.0790 0.1162  -0.0833 450 PHE   A CB   
1742 C  CG   . PHE   A 243 ? 0.0918 0.2561 0.6284 0.0319  0.1065  0.0153  450 PHE   A CG   
1743 C  CD1  . PHE   A 243 ? 0.0455 0.3023 0.6524 0.1073  -0.0113 0.0080  450 PHE   A CD1  
1744 C  CD2  . PHE   A 243 ? 0.1347 0.2354 0.6917 0.0107  0.0300  0.0445  450 PHE   A CD2  
1745 C  CE1  . PHE   A 243 ? 0.1345 0.1658 0.6045 0.0317  -0.0055 0.0284  450 PHE   A CE1  
1746 C  CE2  . PHE   A 243 ? 0.1997 0.1608 0.6828 0.1444  0.0684  0.0788  450 PHE   A CE2  
1747 C  CZ   . PHE   A 243 ? 0.1555 0.1095 0.6647 0.0320  -0.0360 -0.0191 450 PHE   A CZ   
1748 N  N    . LEU   A 244 ? 0.1083 0.3330 0.6883 0.0464  0.1395  -0.0359 451 LEU   A N    
1749 C  CA   . LEU   A 244 ? 0.1470 0.3213 0.7022 0.0670  0.1367  -0.0472 451 LEU   A CA   
1750 C  C    . LEU   A 244 ? 0.1587 0.1659 0.7499 0.0954  0.0790  0.0099  451 LEU   A C    
1751 O  O    . LEU   A 244 ? 0.2092 0.1181 0.7075 -0.0003 0.0428  -0.0324 451 LEU   A O    
1752 C  CB   . LEU   A 244 ? 0.1039 0.4455 0.7119 0.0772  0.1207  -0.0713 451 LEU   A CB   
1753 C  CG   . LEU   A 244 ? 0.3263 0.4143 0.7363 0.2217  -0.0142 -0.0150 451 LEU   A CG   
1754 C  CD1  . LEU   A 244 ? 0.5657 0.5770 0.8179 0.2246  0.1568  -0.0084 451 LEU   A CD1  
1755 C  CD2  . LEU   A 244 ? 0.2993 0.3944 0.7781 0.0514  0.0274  0.0136  451 LEU   A CD2  
1756 N  N    . GLU   A 245 ? 0.1269 0.2674 0.6849 0.0169  0.0629  -0.1299 452 GLU   A N    
1757 C  CA   . GLU   A 245 ? 0.2595 0.2601 0.6966 -0.0148 -0.0130 -0.1747 452 GLU   A CA   
1758 C  C    . GLU   A 245 ? 0.1860 0.2754 0.7443 -0.0371 0.0184  -0.2189 452 GLU   A C    
1759 O  O    . GLU   A 245 ? 0.1780 0.4214 0.7697 -0.0772 -0.0527 -0.0858 452 GLU   A O    
1760 C  CB   . GLU   A 245 ? 0.3541 0.4601 0.6431 0.0119  0.0178  -0.1165 452 GLU   A CB   
1761 C  CG   . GLU   A 245 ? 0.4476 0.5139 0.6850 -0.0211 -0.0424 -0.1083 452 GLU   A CG   
1762 C  CD   . GLU   A 245 ? 0.5020 0.7051 0.7735 0.0702  -0.0238 -0.0018 452 GLU   A CD   
1763 O  OE1  . GLU   A 245 ? 0.5338 0.5696 1.0267 -0.2831 0.0132  -0.0382 452 GLU   A OE1  
1764 O  OE2  . GLU   A 245 ? 0.8535 0.7539 0.8196 0.5227  -0.0205 -0.0916 452 GLU   A OE2  
1765 N  N    . MET   A 246 ? 0.1141 0.2368 0.5749 0.0543  -0.0259 -0.1156 453 MET   A N    
1766 C  CA   . MET   A 246 ? 0.1318 0.2408 0.6313 -0.0122 0.0417  -0.0970 453 MET   A CA   
1767 C  C    . MET   A 246 ? 0.0829 0.2289 0.6119 0.0468  0.0691  -0.1562 453 MET   A C    
1768 O  O    . MET   A 246 ? 0.0494 0.4091 0.6030 0.0305  0.0750  -0.1246 453 MET   A O    
1769 C  CB   . MET   A 246 ? 0.0973 0.2088 0.6236 -0.0163 -0.0052 -0.0351 453 MET   A CB   
1770 C  CG   . MET   A 246 ? 0.0778 0.2824 0.6058 0.0066  0.0812  0.0251  453 MET   A CG   
1771 S  SD   . MET   A 246 ? 0.1864 0.3214 0.6796 -0.0250 0.0427  -0.0595 453 MET   A SD   
1772 C  CE   . MET   A 246 ? 0.0264 0.4410 0.6696 -0.0933 0.0245  -0.0930 453 MET   A CE   
1773 N  N    . LEU   A 247 ? 0.1239 0.2605 0.6589 0.0658  0.0045  -0.0495 454 LEU   A N    
1774 C  CA   . LEU   A 247 ? 0.0109 0.3486 0.5983 0.0071  0.0135  -0.1039 454 LEU   A CA   
1775 C  C    . LEU   A 247 ? 0.1485 0.2481 0.5886 0.0298  -0.0012 -0.0187 454 LEU   A C    
1776 O  O    . LEU   A 247 ? 0.3734 0.4122 0.6158 0.0840  0.0468  0.0836  454 LEU   A O    
1777 C  CB   . LEU   A 247 ? 0.0158 0.4820 0.6930 -0.0636 0.0325  -0.0487 454 LEU   A CB   
1778 C  CG   . LEU   A 247 ? 0.1128 0.2486 0.7126 -0.0731 0.0923  -0.0405 454 LEU   A CG   
1779 C  CD1  . LEU   A 247 ? 0.0764 0.4508 0.7481 -0.0520 0.1084  -0.0829 454 LEU   A CD1  
1780 C  CD2  . LEU   A 247 ? 0.1948 0.3101 0.7192 0.0134  0.1226  0.0139  454 LEU   A CD2  
1781 N  N    . GLU   A 248 ? 0.3341 0.2715 0.6444 0.0209  0.1061  -0.0771 455 GLU   A N    
1782 C  CA   . GLU   A 248 ? 0.1798 0.2379 0.8982 0.0110  0.0613  -0.0132 455 GLU   A CA   
1783 C  C    . GLU   A 248 ? 0.2001 0.3753 0.8632 -0.0091 0.0203  -0.0826 455 GLU   A C    
1784 O  O    . GLU   A 248 ? 0.3802 0.3784 0.9081 -0.1032 0.0182  0.0084  455 GLU   A O    
1785 C  CB   . GLU   A 248 ? 0.3539 0.3282 0.8976 0.0883  0.1432  0.0144  455 GLU   A CB   
1786 C  CG   . GLU   A 248 ? 0.2614 0.5392 1.1327 0.1810  0.2597  -0.0401 455 GLU   A CG   
1787 C  CD   . GLU   A 248 ? 0.4044 0.5806 1.1652 0.0515  0.3018  -0.1496 455 GLU   A CD   
1788 O  OE1  . GLU   A 248 ? 0.9107 0.5619 1.2575 0.0508  0.3042  -0.5027 455 GLU   A OE1  
1789 O  OE2  . GLU   A 248 ? 0.4748 1.0945 1.0945 0.2520  0.2217  -0.1276 455 GLU   A OE2  
1790 N  N    . ALA   A 249 ? 0.1559 0.4263 0.7765 0.0071  -0.0184 -0.0998 456 ALA   A N    
1791 C  CA   . ALA   A 249 ? 0.1780 0.3065 0.8357 0.0794  -0.0855 -0.1111 456 ALA   A CA   
1792 C  C    . ALA   A 249 ? 0.3413 0.5178 0.8662 -0.0552 -0.1838 -0.0372 456 ALA   A C    
1793 O  O    . ALA   A 249 ? 0.2557 0.6931 0.7757 -0.0383 -0.0637 -0.0503 456 ALA   A O    
1794 C  CB   . ALA   A 249 ? 0.2930 0.2828 0.8203 0.0819  -0.0526 -0.1354 456 ALA   A CB   
1795 N  N    . LYS   A 250 ? 0.5507 0.3833 1.3198 -0.2130 -0.2185 0.0239  457 LYS   A N    
1796 C  CA   . LYS   A 250 ? 0.4803 0.3214 1.2548 -0.0220 -0.3453 0.1670  457 LYS   A CA   
1797 C  C    . LYS   A 250 ? 0.1672 0.3891 1.5025 -0.2194 -0.1143 0.2198  457 LYS   A C    
1798 O  O    . LYS   A 250 ? 0.2193 0.7062 1.1700 0.0428  0.1784  0.4134  457 LYS   A O    
1799 C  CB   . LYS   A 250 ? 1.0880 0.5003 1.3618 -0.1642 -0.3323 0.0086  457 LYS   A CB   
1800 C  CG   . LYS   A 250 ? 1.3223 0.2624 1.3537 -0.2323 -0.3138 -0.2090 457 LYS   A CG   
1801 C  CD   . LYS   A 250 ? 1.4543 0.3308 1.2553 -0.0100 -0.2003 -0.3355 457 LYS   A CD   
1802 C  CE   . LYS   A 250 ? 1.4156 0.7531 1.0099 -0.2043 0.0629  -0.1917 457 LYS   A CE   
1803 N  NZ   . LYS   A 250 ? 1.3939 0.8554 0.9550 -0.1410 -0.1156 -0.1753 457 LYS   A NZ   
1804 N  N    . ASN   B 1   ? 0.5317 0.6534 1.2042 -0.2060 0.1526  0.2588  376 ASN   C N    
1805 C  CA   . ASN   B 1   ? 0.9418 0.4087 1.2114 -0.3491 0.0463  0.0949  376 ASN   C CA   
1806 C  C    . ASN   B 1   ? 0.7746 0.2025 0.9137 -0.2665 -0.0882 -0.0487 376 ASN   C C    
1807 O  O    . ASN   B 1   ? 0.8974 0.3915 1.1703 0.0580  -0.2464 -0.0133 376 ASN   C O    
1808 C  CB   . ASN   B 1   ? 0.8575 0.6436 1.3676 -0.1225 -0.1203 0.1723  376 ASN   C CB   
1809 C  CG   . ASN   B 1   ? 0.1903 0.9341 1.4273 0.0989  -0.1496 0.1929  376 ASN   C CG   
1810 O  OD1  . ASN   B 1   ? 0.1870 1.3713 1.6452 0.1564  -0.1267 0.3198  376 ASN   C OD1  
1811 N  ND2  . ASN   B 1   ? 0.4661 0.9462 1.0609 -0.0647 -0.3016 0.1224  376 ASN   C ND2  
1812 N  N    . ASN   B 2   ? 0.6788 0.7927 0.9921 -0.3178 0.0358  -0.3223 377 ASN   C N    
1813 C  CA   . ASN   B 2   ? 1.0190 0.3461 1.1354 -0.3749 0.0746  -0.2407 377 ASN   C CA   
1814 C  C    . ASN   B 2   ? 0.7909 0.1618 1.0649 0.0592  0.0791  -0.2361 377 ASN   C C    
1815 O  O    . ASN   B 2   ? 0.8233 0.9124 1.0688 0.1040  0.0276  -0.3452 377 ASN   C O    
1816 C  CB   . ASN   B 2   ? 1.0281 0.4734 1.4866 -0.3872 0.1141  -0.3825 377 ASN   C CB   
1817 C  CG   . ASN   B 2   ? 1.0161 0.7736 1.5486 -0.2540 0.1705  -0.3026 377 ASN   C CG   
1818 O  OD1  . ASN   B 2   ? 1.1575 0.7736 1.9495 0.6232  -0.0463 -0.4565 377 ASN   C OD1  
1819 N  ND2  . ASN   B 2   ? 0.6113 0.5350 2.4285 0.1022  -0.4686 0.0114  377 ASN   C ND2  
1820 N  N    . SER   B 3   ? 0.7889 0.5077 0.8361 0.1149  -0.0129 -0.2760 378 SER   C N    
1821 C  CA   . SER   B 3   ? 0.4138 0.5887 0.7858 0.1913  0.1025  -0.2255 378 SER   C CA   
1822 C  C    . SER   B 3   ? 0.2144 0.6526 0.6096 0.0652  0.0671  -0.1818 378 SER   C C    
1823 O  O    . SER   B 3   ? 0.3500 0.6472 0.6130 0.0561  0.1009  -0.1172 378 SER   C O    
1824 C  CB   . SER   B 3   ? 0.4452 0.5844 0.7865 0.1269  0.1411  -0.2197 378 SER   C CB   
1825 O  OG   . SER   B 3   ? 0.3006 0.5089 0.7695 0.0236  0.1297  -0.2348 378 SER   C OG   
1826 N  N    . LEU   B 4   ? 0.1322 0.5617 0.6628 0.1431  0.0415  -0.0773 379 LEU   C N    
1827 C  CA   . LEU   B 4   ? 0.3085 0.5897 0.7343 -0.0057 0.0721  -0.0616 379 LEU   C CA   
1828 C  C    . LEU   B 4   ? 0.1804 0.5098 0.7281 -0.1483 0.1419  -0.0119 379 LEU   C C    
1829 O  O    . LEU   B 4   ? 0.3490 0.4203 0.6186 -0.0559 0.1361  -0.1090 379 LEU   C O    
1830 C  CB   . LEU   B 4   ? 0.2117 0.8998 0.6801 0.0475  0.1415  -0.1317 379 LEU   C CB   
1831 C  CG   . LEU   B 4   ? 0.2473 1.0637 0.7493 -0.0356 -0.1187 -0.1339 379 LEU   C CG   
1832 C  CD1  . LEU   B 4   ? 0.2424 0.9854 0.7579 0.0968  -0.0332 -0.1092 379 LEU   C CD1  
1833 C  CD2  . LEU   B 4   ? 0.2170 1.0403 0.8059 0.0961  -0.0625 -0.2245 379 LEU   C CD2  
1834 N  N    . LEU   B 5   ? 0.1703 0.3672 0.6475 -0.1229 0.0438  -0.0545 380 LEU   C N    
1835 C  CA   . LEU   B 5   ? 0.1838 0.4498 0.6085 -0.1104 0.0750  -0.0903 380 LEU   C CA   
1836 C  C    . LEU   B 5   ? 0.2076 0.4292 0.5548 0.0475  0.0821  -0.1421 380 LEU   C C    
1837 O  O    . LEU   B 5   ? 0.2526 0.3833 0.6063 0.0738  0.0914  -0.0734 380 LEU   C O    
1838 C  CB   . LEU   B 5   ? 0.1517 0.3620 0.7031 0.0079  0.1577  -0.0689 380 LEU   C CB   
1839 C  CG   . LEU   B 5   ? 0.0578 0.3309 0.6101 -0.0692 0.0721  -0.1310 380 LEU   C CG   
1840 C  CD1  . LEU   B 5   ? 0.3008 0.2666 0.6735 -0.0565 0.0633  -0.0511 380 LEU   C CD1  
1841 C  CD2  . LEU   B 5   ? 0.1114 0.3713 0.6186 0.0364  0.0813  -0.0101 380 LEU   C CD2  
1842 N  N    . LEU   B 6   ? 0.1402 0.5508 0.5531 0.0078  0.0252  -0.1636 381 LEU   C N    
1843 C  CA   . LEU   B 6   ? 0.2641 0.5233 0.6072 0.0096  -0.0694 -0.1374 381 LEU   C CA   
1844 C  C    . LEU   B 6   ? 0.2883 0.6490 0.4997 0.0755  0.0961  -0.1384 381 LEU   C C    
1845 O  O    . LEU   B 6   ? 0.2915 0.7375 0.6743 0.0811  0.0614  -0.0492 381 LEU   C O    
1846 C  CB   . LEU   B 6   ? 0.3424 0.4928 0.6567 -0.0281 0.0048  -0.1190 381 LEU   C CB   
1847 C  CG   . LEU   B 6   ? 0.2991 0.4006 0.6951 0.0895  0.0094  -0.1600 381 LEU   C CG   
1848 C  CD1  . LEU   B 6   ? 0.3118 0.4902 0.7927 0.0634  0.0626  -0.1649 381 LEU   C CD1  
1849 C  CD2  . LEU   B 6   ? 0.5946 0.4942 0.6700 -0.0466 0.0565  -0.2004 381 LEU   C CD2  
1850 N  N    . HIS   B 7   ? 0.2210 0.6349 0.5656 -0.0254 0.0518  -0.0918 382 HIS   C N    
1851 C  CA   . HIS   B 7   ? 0.3058 0.4993 0.5982 0.0339  0.1042  -0.0967 382 HIS   C CA   
1852 C  C    . HIS   B 7   ? 0.3624 0.4614 0.5196 -0.1188 0.0493  -0.0672 382 HIS   C C    
1853 O  O    . HIS   B 7   ? 0.1892 0.4317 0.6360 -0.0800 0.0022  -0.0991 382 HIS   C O    
1854 C  CB   . HIS   B 7   ? 0.2611 0.5698 0.6077 0.0283  0.0607  -0.0652 382 HIS   C CB   
1855 C  CG   . HIS   B 7   ? 0.3636 0.7955 0.6403 -0.0244 0.0778  0.0444  382 HIS   C CG   
1856 N  ND1  . HIS   B 7   ? 0.1891 0.9489 0.6799 0.0446  -0.0089 -0.0913 382 HIS   C ND1  
1857 C  CD2  . HIS   B 7   ? 0.6041 0.9941 0.7838 -0.1415 -0.0243 -0.0571 382 HIS   C CD2  
1858 C  CE1  . HIS   B 7   ? 0.2447 0.9647 0.9858 -0.1363 -0.1585 -0.0949 382 HIS   C CE1  
1859 N  NE2  . HIS   B 7   ? 0.5052 0.9139 0.7857 -0.2872 0.0332  -0.1366 382 HIS   C NE2  
1860 N  N    . LEU   B 8   ? 0.3502 0.4721 0.5136 -0.0785 0.0696  -0.0224 383 LEU   C N    
1861 C  CA   . LEU   B 8   ? 0.2949 0.3847 0.5591 0.0528  0.1173  0.0569  383 LEU   C CA   
1862 C  C    . LEU   B 8   ? 0.2722 0.3812 0.5664 0.0064  0.1202  0.0189  383 LEU   C C    
1863 O  O    . LEU   B 8   ? 0.3182 0.4217 0.7018 0.1058  0.0411  0.1092  383 LEU   C O    
1864 C  CB   . LEU   B 8   ? 0.1641 0.4363 0.5769 -0.0289 0.1249  -0.0113 383 LEU   C CB   
1865 C  CG   . LEU   B 8   ? 0.1658 0.5539 0.5770 -0.0086 0.1460  0.0111  383 LEU   C CG   
1866 C  CD1  . LEU   B 8   ? 0.3198 0.4753 0.5945 0.1446  0.1488  -0.0493 383 LEU   C CD1  
1867 C  CD2  . LEU   B 8   ? 0.3821 0.4878 0.5932 -0.0458 0.1228  0.0045  383 LEU   C CD2  
1868 N  N    . LEU   B 9   ? 0.2450 0.3022 0.6092 0.0047  0.0454  -0.0412 384 LEU   C N    
1869 C  CA   . LEU   B 9   ? 0.2282 0.3173 0.6262 -0.0186 -0.0678 -0.0055 384 LEU   C CA   
1870 C  C    . LEU   B 9   ? 0.1015 0.3714 0.6423 0.0432  -0.0369 0.0171  384 LEU   C C    
1871 O  O    . LEU   B 9   ? 0.1016 0.4608 0.7494 0.0933  -0.0265 -0.0487 384 LEU   C O    
1872 C  CB   . LEU   B 9   ? 0.2280 0.3329 0.5626 -0.0366 -0.0299 -0.0727 384 LEU   C CB   
1873 C  CG   . LEU   B 9   ? 0.1747 0.3781 0.5630 -0.0572 -0.0416 -0.1299 384 LEU   C CG   
1874 C  CD1  . LEU   B 9   ? 0.1928 0.4003 0.5943 -0.0671 0.0263  -0.1200 384 LEU   C CD1  
1875 C  CD2  . LEU   B 9   ? 0.1839 0.2899 0.4950 -0.0740 -0.0427 -0.0841 384 LEU   C CD2  
1876 N  N    . LYS   B 10  ? 0.1155 0.5837 0.7356 0.0171  -0.0430 -0.0938 385 LYS   C N    
1877 C  CA   . LYS   B 10  ? 0.2096 0.6204 0.6644 0.0118  0.0069  -0.0731 385 LYS   C CA   
1878 C  C    . LYS   B 10  ? 0.3570 0.8516 0.4823 -0.0503 0.0321  0.0606  385 LYS   C C    
1879 O  O    . LYS   B 10  ? 0.6798 1.0602 0.4909 -0.0389 -0.0712 0.0451  385 LYS   C O    
1880 C  CB   . LYS   B 10  ? 0.3747 0.6094 0.6683 -0.0212 0.0614  -0.0777 385 LYS   C CB   
1881 C  CG   . LYS   B 10  ? 0.2780 0.5782 0.8316 0.0035  -0.0529 -0.0071 385 LYS   C CG   
1882 C  CD   . LYS   B 10  ? 0.3994 0.6351 0.7964 0.0326  0.1441  0.0223  385 LYS   C CD   
1883 C  CE   . LYS   B 10  ? 0.5438 0.7024 0.8159 0.0080  0.1841  -0.0475 385 LYS   C CE   
1884 N  NZ   . LYS   B 10  ? 0.8365 0.6314 0.9983 -0.1684 0.2085  -0.1974 385 LYS   C NZ   
1885 N  N    . SER   B 11  ? 0.2494 0.9229 0.6509 0.0224  0.1135  -0.0393 386 SER   C N    
1886 C  CA   . SER   B 11  ? 0.4447 1.0691 0.6621 -0.2765 -0.0588 -0.0333 386 SER   C CA   
1887 C  C    . SER   B 11  ? 0.6940 1.0958 0.5748 -0.1704 -0.0099 0.0353  386 SER   C C    
1888 O  O    . SER   B 11  ? 1.0185 1.2932 0.4435 -0.1100 -0.0087 0.0356  386 SER   C O    
1889 C  CB   . SER   B 11  ? 0.4676 1.2969 0.6803 -0.1764 -0.0821 0.1260  386 SER   C CB   
1890 O  OG   . SER   B 11  ? 0.3965 1.5824 0.7333 -0.3377 -0.1522 -0.0301 386 SER   C OG   
1891 N  N    . GLN   B 12  ? 0.9118 1.2094 0.7831 -0.3440 0.0162  0.0978  387 GLN   C N    
1892 C  CA   . GLN   B 12  ? 0.7760 1.2131 0.9844 -0.4128 -0.2554 0.0135  387 GLN   C CA   
1893 C  C    . GLN   B 12  ? 0.6267 1.3604 1.0824 -0.3073 -0.3638 0.3088  387 GLN   C C    
1894 O  O    . GLN   B 12  ? 0.6934 1.7429 1.1299 -0.3337 -0.3461 -0.1370 387 GLN   C O    
1895 C  CB   . GLN   B 12  ? 1.0806 0.6744 1.1468 -0.7780 -0.0680 0.1036  387 GLN   C CB   
1896 C  CG   . GLN   B 12  ? 1.2483 0.8853 0.9377 -0.5165 0.0150  -0.1707 387 GLN   C CG   
1897 C  CD   . GLN   B 12  ? 1.2951 1.0272 0.6821 -0.2421 0.0103  -0.1201 387 GLN   C CD   
1898 O  OE1  . GLN   B 12  ? 1.8160 0.6925 0.6402 0.0194  -0.2117 -0.1964 387 GLN   C OE1  
1899 N  NE2  . GLN   B 12  ? 1.4851 1.2749 0.7033 -0.1245 0.3511  -0.0064 387 GLN   C NE2  
1900 CL CLAJ . A1EGB C .   ? 0.6737 0.3490 2.1200 -0.1426 -0.6121 0.3638  501 A1EGB A CLAJ 
1901 C  CAE  . A1EGB C .   ? 0.3769 0.3613 0.8740 -0.0088 0.0142  0.1555  501 A1EGB A CAE  
1902 C  CAD  . A1EGB C .   ? 0.2088 0.5691 0.8204 -0.0875 -0.0661 0.1314  501 A1EGB A CAD  
1903 C  CAB  . A1EGB C .   ? 0.1820 0.5242 0.8228 -0.2025 -0.0733 0.0417  501 A1EGB A CAB  
1904 C  CAA  . A1EGB C .   ? 0.4311 0.4761 0.7516 -0.2037 0.0223  -0.0168 501 A1EGB A CAA  
1905 N  NAH  . A1EGB C .   ? 0.1128 0.6076 0.9993 -0.2285 -0.0614 0.2462  501 A1EGB A NAH  
1906 N  NAI  . A1EGB C .   ? 0.4662 0.6289 0.8799 -0.1819 0.0683  0.1097  501 A1EGB A NAI  
1907 C  CAC  . A1EGB C .   ? 0.4170 0.4319 0.8056 -0.2526 0.0752  -0.0782 501 A1EGB A CAC  
1908 C  CAG  . A1EGB C .   ? 0.3750 0.4240 0.9037 -0.0636 0.1809  0.0083  501 A1EGB A CAG  
1909 C  CAF  . A1EGB C .   ? 0.2386 0.3469 0.7842 -0.2361 0.0293  -0.0086 501 A1EGB A CAF  
1910 O  O    . HOH   D .   ? 0.4792 0.1031 0.6520 0.0237  0.1161  0.0460  601 HOH   A O    
1911 O  O    . HOH   D .   ? 0.4002 0.4378 0.5763 0.2497  0.0884  0.0248  602 HOH   A O    
1912 O  O    . HOH   D .   ? 0.3489 0.2235 0.6892 -0.1344 -0.0401 -0.0285 603 HOH   A O    
1913 O  O    . HOH   D .   ? 0.2724 0.3827 0.7021 -0.0468 0.0830  0.1714  604 HOH   A O    
1914 O  O    . HOH   D .   ? 0.0754 0.2462 0.7276 -0.0723 0.0477  0.0289  605 HOH   A O    
1915 O  O    . HOH   D .   ? 0.2063 0.5204 0.7065 0.1777  -0.0630 -0.0346 606 HOH   A O    
1916 O  O    . HOH   D .   ? 0.3735 0.6850 0.6486 -0.3443 0.0356  0.0772  607 HOH   A O    
1917 O  O    . HOH   D .   ? 0.2054 0.0563 0.6222 0.0050  0.0549  -0.0077 608 HOH   A O    
1918 O  O    . HOH   D .   ? 0.2343 0.2109 0.5842 -0.0008 0.0909  0.0328  609 HOH   A O    
1919 O  O    . HOH   D .   ? 0.2897 0.3202 0.6933 0.1246  -0.1131 -0.2158 610 HOH   A O    
1920 O  O    . HOH   D .   ? 0.1792 0.3856 0.6403 -0.1985 0.1020  -0.1227 611 HOH   A O    
1921 O  O    . HOH   D .   ? 0.2832 0.3217 0.7758 0.0778  0.0917  0.0485  612 HOH   A O    
1922 O  O    . HOH   D .   ? 0.1648 0.3384 0.6792 0.0148  0.0791  -0.1283 613 HOH   A O    
1923 O  O    . HOH   D .   ? 0.2746 0.6294 0.7487 0.2419  -0.0416 -0.1981 614 HOH   A O    
1924 O  O    . HOH   D .   ? 0.2101 0.2837 0.7408 -0.0098 0.0555  0.0734  615 HOH   A O    
1925 O  O    . HOH   D .   ? 0.1101 0.1419 0.5224 0.0541  -0.0014 0.0215  616 HOH   A O    
1926 O  O    . HOH   D .   ? 0.0980 0.0942 0.5497 -0.0048 0.0180  0.0488  617 HOH   A O    
1927 O  O    . HOH   D .   ? 0.1923 0.6455 0.8155 -0.1220 -0.1556 -0.0750 618 HOH   A O    
1928 O  O    . HOH   D .   ? 0.1576 0.2450 0.5847 -0.1468 -0.0963 0.1463  619 HOH   A O    
1929 O  O    . HOH   D .   ? 0.2495 0.2858 0.7231 -0.0088 -0.0139 -0.1747 620 HOH   A O    
1930 O  O    . HOH   D .   ? 0.1459 0.2327 0.4904 -0.0481 0.0277  0.0054  621 HOH   A O    
1931 O  O    . HOH   D .   ? 0.1335 0.2047 0.5830 0.0166  -0.0234 -0.0059 622 HOH   A O    
1932 O  O    . HOH   D .   ? 0.0406 0.3032 0.7791 0.0811  -0.0220 -0.0344 623 HOH   A O    
1933 O  O    . HOH   D .   ? 0.0667 0.1364 0.4416 0.0314  0.0244  0.0067  624 HOH   A O    
1934 O  O    . HOH   D .   ? 0.5512 0.1165 0.8074 0.0001  0.0394  -0.0588 625 HOH   A O    
1935 O  O    . HOH   D .   ? 0.3046 0.0741 0.5533 0.0339  0.1072  0.0414  626 HOH   A O    
1936 O  O    . HOH   D .   ? 0.1723 0.1479 0.6926 -0.0127 0.0174  -0.1108 627 HOH   A O    
1937 O  O    . HOH   D .   ? 0.1872 0.2026 0.7440 0.1005  -0.0108 0.0556  628 HOH   A O    
1938 O  O    . HOH   D .   ? 0.2822 0.1759 1.0519 0.0954  -0.3332 -0.2219 629 HOH   A O    
1939 O  O    . HOH   D .   ? 0.1487 0.1533 0.4716 -0.0807 -0.0095 0.0780  630 HOH   A O    
1940 O  O    . HOH   D .   ? 0.2204 0.3661 0.6094 0.0565  0.0278  0.1056  631 HOH   A O    
1941 O  O    . HOH   D .   ? 0.1610 0.2768 0.7514 0.0839  0.1058  0.0313  632 HOH   A O    
1942 O  O    . HOH   D .   ? 0.5517 0.1196 0.6256 -0.0716 -0.0339 0.0112  633 HOH   A O    
1943 O  O    . HOH   D .   ? 0.2546 0.3193 0.6220 -0.0488 -0.0821 -0.1203 634 HOH   A O    
1944 O  O    . HOH   D .   ? 0.4762 0.3611 0.7660 -0.0044 -0.0445 -0.1431 635 HOH   A O    
1945 O  O    . HOH   D .   ? 0.2811 0.2016 0.6119 -0.1025 0.0413  -0.0611 636 HOH   A O    
1946 O  O    . HOH   D .   ? 0.1283 0.2585 0.6129 0.0517  -0.0296 0.0639  637 HOH   A O    
1947 O  O    . HOH   D .   ? 0.0835 0.3924 0.6719 0.0819  -0.0158 0.0863  638 HOH   A O    
1948 O  O    . HOH   D .   ? 0.0719 0.1484 0.4719 -0.0462 0.0058  0.0169  639 HOH   A O    
1949 O  O    . HOH   D .   ? 0.2647 0.5638 0.8147 -0.0133 -0.1984 -0.0040 640 HOH   A O    
1950 O  O    . HOH   D .   ? 0.1663 0.0671 0.6467 0.0116  0.0479  -0.0250 641 HOH   A O    
1951 O  O    . HOH   D .   ? 0.2374 0.4277 0.6161 -0.1592 -0.0076 -0.0075 642 HOH   A O    
1952 O  O    . HOH   D .   ? 0.1391 0.6360 0.6945 -0.1187 0.0346  -0.2301 643 HOH   A O    
1953 O  O    . HOH   D .   ? 0.3339 0.1378 0.6857 -0.0932 0.0903  0.0816  644 HOH   A O    
1954 O  O    . HOH   D .   ? 0.2233 0.2329 0.7697 0.0172  0.0417  0.1457  645 HOH   A O    
1955 O  O    . HOH   D .   ? 0.0847 0.2893 0.6023 -0.0367 -0.1015 0.1508  646 HOH   A O    
1956 O  O    . HOH   D .   ? 0.1113 0.2375 0.5260 0.0545  0.0303  0.0528  647 HOH   A O    
1957 O  O    . HOH   D .   ? 0.1394 0.4019 0.5692 -0.0355 0.0367  0.0548  648 HOH   A O    
1958 O  O    . HOH   D .   ? 0.1300 0.4723 0.6195 0.1092  0.0889  0.1902  649 HOH   A O    
1959 O  O    . HOH   D .   ? 0.3376 0.5277 0.7221 -0.1747 0.0411  -0.2902 650 HOH   A O    
1960 O  O    . HOH   D .   ? 0.2673 0.4590 0.4339 -0.0842 -0.0323 0.0229  651 HOH   A O    
1961 O  O    . HOH   D .   ? 0.2755 0.4269 0.6028 -0.2403 -0.0576 -0.0137 652 HOH   A O    
1962 O  O    . HOH   D .   ? 0.2520 0.2669 0.7533 0.0043  0.0229  -0.0059 653 HOH   A O    
1963 O  O    . HOH   D .   ? 0.4565 0.3786 0.6318 -0.1595 0.1074  0.0562  654 HOH   A O    
1964 O  O    . HOH   D .   ? 0.1072 0.3089 0.5877 0.0603  -0.0083 0.1169  655 HOH   A O    
1965 O  O    . HOH   D .   ? 0.2946 0.3965 0.6586 0.0193  -0.1527 -0.1273 656 HOH   A O    
1966 O  O    . HOH   D .   ? 0.1198 0.0506 0.5760 -0.0071 0.0250  -0.0089 657 HOH   A O    
1967 O  O    . HOH   D .   ? 0.2699 0.2481 0.6097 -0.0527 -0.0510 0.0009  658 HOH   A O    
1968 O  O    . HOH   D .   ? 0.1468 0.3181 0.5863 -0.0552 0.0398  -0.0409 659 HOH   A O    
1969 O  O    . HOH   D .   ? 0.1452 0.2567 0.8215 0.0674  0.0649  -0.0006 660 HOH   A O    
1970 O  O    . HOH   D .   ? 0.1388 0.1896 0.8395 -0.0185 -0.0399 0.1556  661 HOH   A O    
1971 O  O    . HOH   D .   ? 0.7831 0.2248 0.9950 0.1130  0.1310  -0.0273 662 HOH   A O    
1972 O  O    . HOH   D .   ? 0.5237 0.1251 0.7851 -0.1388 0.1757  0.0174  663 HOH   A O    
1973 O  O    . HOH   D .   ? 0.1215 0.6354 0.7297 -0.0427 0.0197  0.1553  664 HOH   A O    
1974 O  O    . HOH   D .   ? 0.6249 0.1834 0.9967 0.1762  0.2993  0.1946  665 HOH   A O    
1975 O  O    . HOH   D .   ? 0.1683 0.2525 0.5674 0.0613  0.0227  0.0156  666 HOH   A O    
1976 O  O    . HOH   D .   ? 0.1620 0.3651 0.6670 -0.1794 -0.0223 -0.0018 667 HOH   A O    
1977 O  O    . HOH   D .   ? 0.2246 0.4789 0.6732 -0.1202 0.0488  0.0537  668 HOH   A O    
1978 O  O    . HOH   D .   ? 0.6684 0.0526 0.8162 0.0960  0.4380  0.0411  669 HOH   A O    
1979 O  O    . HOH   D .   ? 0.2417 0.2643 0.5694 -0.0510 -0.0087 0.0337  670 HOH   A O    
1980 O  O    . HOH   D .   ? 0.1517 0.4216 0.7288 0.0007  0.0126  -0.1075 671 HOH   A O    
1981 O  O    . HOH   D .   ? 0.2222 0.3612 1.0434 0.2037  0.1533  0.1157  672 HOH   A O    
1982 O  O    . HOH   D .   ? 0.1039 0.1669 0.6456 0.0533  0.0720  0.0044  673 HOH   A O    
1983 O  O    . HOH   D .   ? 0.2402 0.2333 0.7501 -0.0448 0.0273  0.1635  674 HOH   A O    
1984 O  O    . HOH   D .   ? 0.6694 0.2505 0.8173 0.0771  0.2193  0.0289  675 HOH   A O    
1985 O  O    . HOH   D .   ? 0.2681 0.4802 0.6860 0.0849  0.0419  0.2097  676 HOH   A O    
1986 O  O    . HOH   D .   ? 0.1715 0.6448 0.6520 0.1603  -0.0179 0.0631  677 HOH   A O    
1987 O  O    . HOH   D .   ? 0.2462 0.1439 0.7175 -0.0898 -0.0135 -0.0922 678 HOH   A O    
1988 O  O    . HOH   D .   ? 0.1190 0.4654 0.5730 -0.1168 -0.0889 0.0605  679 HOH   A O    
1989 O  O    . HOH   D .   ? 0.1126 0.4788 0.5914 -0.0445 0.0379  0.0019  680 HOH   A O    
1990 O  O    . HOH   D .   ? 0.3825 0.3303 0.7328 -0.1031 -0.0792 0.0030  681 HOH   A O    
1991 O  O    . HOH   D .   ? 0.0973 0.1040 0.5035 0.0499  -0.0273 -0.0532 682 HOH   A O    
1992 O  O    . HOH   D .   ? 0.0207 0.1167 0.5361 0.0076  0.0157  0.0431  683 HOH   A O    
1993 O  O    . HOH   D .   ? 0.1519 0.5232 0.7258 -0.0856 -0.0831 0.1217  684 HOH   A O    
1994 O  O    . HOH   D .   ? 0.2270 0.2934 1.0890 -0.0729 -0.0995 -0.0423 685 HOH   A O    
1995 O  O    . HOH   D .   ? 0.1020 0.6881 0.6761 -0.1782 0.0155  -0.0274 686 HOH   A O    
1996 O  O    . HOH   D .   ? 0.1860 0.3129 1.0208 0.0689  0.0209  0.2021  687 HOH   A O    
1997 O  O    . HOH   D .   ? 0.0848 0.4075 0.7376 0.0483  -0.0556 0.1255  688 HOH   A O    
1998 O  O    . HOH   D .   ? 0.3659 0.3524 0.7323 -0.0026 -0.0064 0.1203  689 HOH   A O    
1999 O  O    . HOH   D .   ? 0.3583 0.5512 0.5745 -0.0851 -0.0687 -0.1593 690 HOH   A O    
2000 O  O    . HOH   D .   ? 0.2490 0.4524 0.7193 0.0943  0.1033  0.2363  691 HOH   A O    
2001 O  O    . HOH   D .   ? 0.2938 0.6152 0.6140 0.1602  0.0189  0.2073  692 HOH   A O    
2002 O  O    . HOH   D .   ? 0.3704 0.7149 0.8428 -0.0687 -0.2807 0.1690  693 HOH   A O    
2003 O  O    . HOH   D .   ? 0.2561 0.4834 0.6176 -0.0771 -0.0419 -0.1654 694 HOH   A O    
2004 O  O    . HOH   D .   ? 0.2714 0.3836 0.7933 0.2075  0.1118  0.1927  695 HOH   A O    
2005 O  O    . HOH   D .   ? 0.1864 0.4032 0.6363 0.0218  0.0458  0.1454  696 HOH   A O    
2006 O  O    . HOH   D .   ? 0.3300 0.5367 0.8659 -0.1648 0.2348  -0.2229 697 HOH   A O    
2007 O  O    . HOH   D .   ? 0.2257 0.5532 0.7280 0.0135  -0.0554 0.0283  698 HOH   A O    
2008 O  O    . HOH   D .   ? 0.7341 0.2325 0.7979 -0.0010 -0.1157 0.0869  699 HOH   A O    
2009 O  O    . HOH   D .   ? 0.3297 0.4750 0.8896 -0.1037 -0.0695 0.0370  700 HOH   A O    
2010 O  O    . HOH   D .   ? 0.2764 0.2608 0.8789 0.0522  -0.1565 0.1423  701 HOH   A O    
2011 O  O    . HOH   D .   ? 0.5562 0.6658 0.7005 -0.0506 0.0380  -0.1078 702 HOH   A O    
2012 O  O    . HOH   D .   ? 0.3270 0.3955 0.7814 0.1023  -0.1718 -0.1267 703 HOH   A O    
2013 O  O    . HOH   D .   ? 0.1541 0.5385 0.7340 -0.0855 -0.0434 0.1041  704 HOH   A O    
2014 O  O    . HOH   D .   ? 0.2781 0.0932 0.6631 0.0782  0.0424  -0.0142 705 HOH   A O    
2015 O  O    . HOH   D .   ? 0.1974 0.3481 0.6926 0.0328  -0.0551 -0.0553 706 HOH   A O    
2016 O  O    . HOH   D .   ? 0.3017 0.2213 0.5773 -0.0301 -0.0253 0.0395  707 HOH   A O    
2017 O  O    . HOH   D .   ? 0.6188 0.3408 1.0182 0.1658  -0.2698 -0.0958 708 HOH   A O    
2018 O  O    . HOH   D .   ? 0.2994 0.3657 0.6934 0.1199  -0.0327 0.1110  709 HOH   A O    
2019 O  O    . HOH   D .   ? 0.4384 0.2543 0.7577 0.0612  -0.1188 0.0203  710 HOH   A O    
2020 O  O    . HOH   D .   ? 0.6105 0.2238 0.9906 0.0895  0.1554  -0.2070 711 HOH   A O    
2021 O  O    . HOH   D .   ? 0.1354 0.1850 0.6177 0.0725  0.0334  -0.0003 712 HOH   A O    
2022 O  O    . HOH   D .   ? 0.2725 0.7437 0.8971 0.1872  0.0360  0.0453  713 HOH   A O    
2023 O  O    . HOH   D .   ? 0.2104 0.6616 0.6068 -0.0409 0.0908  0.0293  714 HOH   A O    
2024 O  O    . HOH   D .   ? 0.1302 0.5705 0.6756 0.0413  -0.0168 0.1358  715 HOH   A O    
2025 O  O    . HOH   D .   ? 0.2643 0.3792 0.8206 0.0117  -0.0297 0.0152  716 HOH   A O    
2026 O  O    . HOH   D .   ? 0.4306 0.4635 0.6431 -0.0784 0.0408  -0.0295 717 HOH   A O    
2027 O  O    . HOH   D .   ? 0.1622 0.3207 0.6557 -0.0358 0.0283  -0.0015 718 HOH   A O    
2028 O  O    . HOH   D .   ? 0.4867 0.2374 0.9378 0.2250  -0.0416 0.1267  719 HOH   A O    
2029 O  O    . HOH   D .   ? 0.2646 0.2429 0.5463 -0.0344 -0.0023 0.1091  720 HOH   A O    
2030 O  O    . HOH   D .   ? 0.2939 0.5534 0.6868 0.1709  0.0187  -0.0267 721 HOH   A O    
# 
