data_8YDT
# 
_entry.id   8YDT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YDT         pdb_00008ydt 10.2210/pdb8ydt/pdb 
WWPDB D_1300045362 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YDT 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              yoshi.cesp@tmd.ac.jp 
_pdbx_contact_author.name_first         Yoshinori 
_pdbx_contact_author.name_last          Fujiyoshi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8070-1493 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nakamura, S.'  1 0000-0003-2253-6976 
'Numoto, N.'    2 0000-0001-6113-9792 
'Fujiyoshi, Y.' 3 0000-0002-8070-1493 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Development of a short-peptide inhibiting any SARS-CoV-2 variants based on structural biology' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nakamura, S.'  1  0000-0003-2253-6976 
primary 'Tanimura, Y.'  2  ?                   
primary 'Nomura, R.'    3  ?                   
primary 'Suzuki, H.'    4  ?                   
primary 'Nishikawa, K.' 5  ?                   
primary 'Kamegawa, A.'  6  ?                   
primary 'Numoto, N.'    7  ?                   
primary 'Tanaka, A.'    8  ?                   
primary 'Kawabata, S.'  9  ?                   
primary 'Sakaguchi, S.' 10 ?                   
primary 'Emi, A.'       11 ?                   
primary 'Suzuki, Y.'    12 ?                   
primary 'Fujiyoshi, Y.' 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     syn 'SARS-CoV-2 inhibiting peptide Ce41'     4793.477  2 ? ? ? ? 
2 polymer     man 'Spike protein S1'                       26247.141 2 ? ? ? ? 
3 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   2 ? ? ? ? 
# 
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 DKEWILQKIYEIMRRLDEEGHGEASLRVSDLIYEFMKKD DKEWILQKIYEIMRRLDEEGHGEASLRVSDLIYEFMKKD A,C ? 
2 'polypeptide(L)' no no 
;TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAP
GQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPL
QSYGFQPTYGVGYQPYRVVVLSFELLHAPATVCGSNSENLYFQGSHHHHHHHHHHGLNDIFEAQKIEWHE
;
;TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAP
GQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPL
QSYGFQPTYGVGYQPYRVVVLSFELLHAPATVCGSNSENLYFQGSHHHHHHHHHHGLNDIFEAQKIEWHE
;
B,D ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   LYS n 
1 3   GLU n 
1 4   TRP n 
1 5   ILE n 
1 6   LEU n 
1 7   GLN n 
1 8   LYS n 
1 9   ILE n 
1 10  TYR n 
1 11  GLU n 
1 12  ILE n 
1 13  MET n 
1 14  ARG n 
1 15  ARG n 
1 16  LEU n 
1 17  ASP n 
1 18  GLU n 
1 19  GLU n 
1 20  GLY n 
1 21  HIS n 
1 22  GLY n 
1 23  GLU n 
1 24  ALA n 
1 25  SER n 
1 26  LEU n 
1 27  ARG n 
1 28  VAL n 
1 29  SER n 
1 30  ASP n 
1 31  LEU n 
1 32  ILE n 
1 33  TYR n 
1 34  GLU n 
1 35  PHE n 
1 36  MET n 
1 37  LYS n 
1 38  LYS n 
1 39  ASP n 
2 1   THR n 
2 2   ASN n 
2 3   LEU n 
2 4   CYS n 
2 5   PRO n 
2 6   PHE n 
2 7   GLY n 
2 8   GLU n 
2 9   VAL n 
2 10  PHE n 
2 11  ASN n 
2 12  ALA n 
2 13  THR n 
2 14  ARG n 
2 15  PHE n 
2 16  ALA n 
2 17  SER n 
2 18  VAL n 
2 19  TYR n 
2 20  ALA n 
2 21  TRP n 
2 22  ASN n 
2 23  ARG n 
2 24  LYS n 
2 25  ARG n 
2 26  ILE n 
2 27  SER n 
2 28  ASN n 
2 29  CYS n 
2 30  VAL n 
2 31  ALA n 
2 32  ASP n 
2 33  TYR n 
2 34  SER n 
2 35  VAL n 
2 36  LEU n 
2 37  TYR n 
2 38  ASN n 
2 39  SER n 
2 40  ALA n 
2 41  SER n 
2 42  PHE n 
2 43  SER n 
2 44  THR n 
2 45  PHE n 
2 46  LYS n 
2 47  CYS n 
2 48  TYR n 
2 49  GLY n 
2 50  VAL n 
2 51  SER n 
2 52  PRO n 
2 53  THR n 
2 54  LYS n 
2 55  LEU n 
2 56  ASN n 
2 57  ASP n 
2 58  LEU n 
2 59  CYS n 
2 60  PHE n 
2 61  THR n 
2 62  ASN n 
2 63  VAL n 
2 64  TYR n 
2 65  ALA n 
2 66  ASP n 
2 67  SER n 
2 68  PHE n 
2 69  VAL n 
2 70  ILE n 
2 71  ARG n 
2 72  GLY n 
2 73  ASP n 
2 74  GLU n 
2 75  VAL n 
2 76  ARG n 
2 77  GLN n 
2 78  ILE n 
2 79  ALA n 
2 80  PRO n 
2 81  GLY n 
2 82  GLN n 
2 83  THR n 
2 84  GLY n 
2 85  LYS n 
2 86  ILE n 
2 87  ALA n 
2 88  ASP n 
2 89  TYR n 
2 90  ASN n 
2 91  TYR n 
2 92  LYS n 
2 93  LEU n 
2 94  PRO n 
2 95  ASP n 
2 96  ASP n 
2 97  PHE n 
2 98  THR n 
2 99  GLY n 
2 100 CYS n 
2 101 VAL n 
2 102 ILE n 
2 103 ALA n 
2 104 TRP n 
2 105 ASN n 
2 106 SER n 
2 107 ASN n 
2 108 ASN n 
2 109 LEU n 
2 110 ASP n 
2 111 SER n 
2 112 LYS n 
2 113 VAL n 
2 114 GLY n 
2 115 GLY n 
2 116 ASN n 
2 117 TYR n 
2 118 ASN n 
2 119 TYR n 
2 120 LEU n 
2 121 TYR n 
2 122 ARG n 
2 123 LEU n 
2 124 PHE n 
2 125 ARG n 
2 126 LYS n 
2 127 SER n 
2 128 ASN n 
2 129 LEU n 
2 130 LYS n 
2 131 PRO n 
2 132 PHE n 
2 133 GLU n 
2 134 ARG n 
2 135 ASP n 
2 136 ILE n 
2 137 SER n 
2 138 THR n 
2 139 GLU n 
2 140 ILE n 
2 141 TYR n 
2 142 GLN n 
2 143 ALA n 
2 144 GLY n 
2 145 SER n 
2 146 THR n 
2 147 PRO n 
2 148 CYS n 
2 149 ASN n 
2 150 GLY n 
2 151 VAL n 
2 152 GLU n 
2 153 GLY n 
2 154 PHE n 
2 155 ASN n 
2 156 CYS n 
2 157 TYR n 
2 158 PHE n 
2 159 PRO n 
2 160 LEU n 
2 161 GLN n 
2 162 SER n 
2 163 TYR n 
2 164 GLY n 
2 165 PHE n 
2 166 GLN n 
2 167 PRO n 
2 168 THR n 
2 169 TYR n 
2 170 GLY n 
2 171 VAL n 
2 172 GLY n 
2 173 TYR n 
2 174 GLN n 
2 175 PRO n 
2 176 TYR n 
2 177 ARG n 
2 178 VAL n 
2 179 VAL n 
2 180 VAL n 
2 181 LEU n 
2 182 SER n 
2 183 PHE n 
2 184 GLU n 
2 185 LEU n 
2 186 LEU n 
2 187 HIS n 
2 188 ALA n 
2 189 PRO n 
2 190 ALA n 
2 191 THR n 
2 192 VAL n 
2 193 CYS n 
2 194 GLY n 
2 195 SER n 
2 196 ASN n 
2 197 SER n 
2 198 GLU n 
2 199 ASN n 
2 200 LEU n 
2 201 TYR n 
2 202 PHE n 
2 203 GLN n 
2 204 GLY n 
2 205 SER n 
2 206 HIS n 
2 207 HIS n 
2 208 HIS n 
2 209 HIS n 
2 210 HIS n 
2 211 HIS n 
2 212 HIS n 
2 213 HIS n 
2 214 HIS n 
2 215 HIS n 
2 216 GLY n 
2 217 LEU n 
2 218 ASN n 
2 219 ASP n 
2 220 ILE n 
2 221 PHE n 
2 222 GLU n 
2 223 ALA n 
2 224 GLN n 
2 225 LYS n 
2 226 ILE n 
2 227 GLU n 
2 228 TRP n 
2 229 HIS n 
2 230 GLU n 
# 
_entity_src_gen.entity_id                          2 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   230 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'S, 2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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            Expi293F 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              1 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       39 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   ASP 1   1   1   ASP ASP A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  TYR 10  10  10  TYR TYR A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  HIS 21  21  21  HIS HIS A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  MET 36  36  36  MET MET A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
B 2 1   THR 1   333 ?   ?   ?   B . n 
B 2 2   ASN 2   334 334 ASN ASN B . n 
B 2 3   LEU 3   335 335 LEU LEU B . n 
B 2 4   CYS 4   336 336 CYS CYS B . n 
B 2 5   PRO 5   337 337 PRO PRO B . n 
B 2 6   PHE 6   338 338 PHE PHE B . n 
B 2 7   GLY 7   339 339 GLY GLY B . n 
B 2 8   GLU 8   340 340 GLU GLU B . n 
B 2 9   VAL 9   341 341 VAL VAL B . n 
B 2 10  PHE 10  342 342 PHE PHE B . n 
B 2 11  ASN 11  343 343 ASN ASN B . n 
B 2 12  ALA 12  344 344 ALA ALA B . n 
B 2 13  THR 13  345 345 THR THR B . n 
B 2 14  ARG 14  346 346 ARG ARG B . n 
B 2 15  PHE 15  347 347 PHE PHE B . n 
B 2 16  ALA 16  348 348 ALA ALA B . n 
B 2 17  SER 17  349 349 SER SER B . n 
B 2 18  VAL 18  350 350 VAL VAL B . n 
B 2 19  TYR 19  351 351 TYR TYR B . n 
B 2 20  ALA 20  352 352 ALA ALA B . n 
B 2 21  TRP 21  353 353 TRP TRP B . n 
B 2 22  ASN 22  354 354 ASN ASN B . n 
B 2 23  ARG 23  355 355 ARG ARG B . n 
B 2 24  LYS 24  356 356 LYS LYS B . n 
B 2 25  ARG 25  357 357 ARG ARG B . n 
B 2 26  ILE 26  358 358 ILE ILE B . n 
B 2 27  SER 27  359 359 SER SER B . n 
B 2 28  ASN 28  360 360 ASN ASN B . n 
B 2 29  CYS 29  361 361 CYS CYS B . n 
B 2 30  VAL 30  362 362 VAL VAL B . n 
B 2 31  ALA 31  363 363 ALA ALA B . n 
B 2 32  ASP 32  364 364 ASP ASP B . n 
B 2 33  TYR 33  365 365 TYR TYR B . n 
B 2 34  SER 34  366 366 SER SER B . n 
B 2 35  VAL 35  367 367 VAL VAL B . n 
B 2 36  LEU 36  368 368 LEU LEU B . n 
B 2 37  TYR 37  369 369 TYR TYR B . n 
B 2 38  ASN 38  370 370 ASN ASN B . n 
B 2 39  SER 39  371 371 SER SER B . n 
B 2 40  ALA 40  372 372 ALA ALA B . n 
B 2 41  SER 41  373 373 SER SER B . n 
B 2 42  PHE 42  374 374 PHE PHE B . n 
B 2 43  SER 43  375 375 SER SER B . n 
B 2 44  THR 44  376 376 THR THR B . n 
B 2 45  PHE 45  377 377 PHE PHE B . n 
B 2 46  LYS 46  378 378 LYS LYS B . n 
B 2 47  CYS 47  379 379 CYS CYS B . n 
B 2 48  TYR 48  380 380 TYR TYR B . n 
B 2 49  GLY 49  381 381 GLY GLY B . n 
B 2 50  VAL 50  382 382 VAL VAL B . n 
B 2 51  SER 51  383 383 SER SER B . n 
B 2 52  PRO 52  384 384 PRO PRO B . n 
B 2 53  THR 53  385 385 THR THR B . n 
B 2 54  LYS 54  386 386 LYS LYS B . n 
B 2 55  LEU 55  387 387 LEU LEU B . n 
B 2 56  ASN 56  388 388 ASN ASN B . n 
B 2 57  ASP 57  389 389 ASP ASP B . n 
B 2 58  LEU 58  390 390 LEU LEU B . n 
B 2 59  CYS 59  391 391 CYS CYS B . n 
B 2 60  PHE 60  392 392 PHE PHE B . n 
B 2 61  THR 61  393 393 THR THR B . n 
B 2 62  ASN 62  394 394 ASN ASN B . n 
B 2 63  VAL 63  395 395 VAL VAL B . n 
B 2 64  TYR 64  396 396 TYR TYR B . n 
B 2 65  ALA 65  397 397 ALA ALA B . n 
B 2 66  ASP 66  398 398 ASP ASP B . n 
B 2 67  SER 67  399 399 SER SER B . n 
B 2 68  PHE 68  400 400 PHE PHE B . n 
B 2 69  VAL 69  401 401 VAL VAL B . n 
B 2 70  ILE 70  402 402 ILE ILE B . n 
B 2 71  ARG 71  403 403 ARG ARG B . n 
B 2 72  GLY 72  404 404 GLY GLY B . n 
B 2 73  ASP 73  405 405 ASP ASP B . n 
B 2 74  GLU 74  406 406 GLU GLU B . n 
B 2 75  VAL 75  407 407 VAL VAL B . n 
B 2 76  ARG 76  408 408 ARG ARG B . n 
B 2 77  GLN 77  409 409 GLN GLN B . n 
B 2 78  ILE 78  410 410 ILE ILE B . n 
B 2 79  ALA 79  411 411 ALA ALA B . n 
B 2 80  PRO 80  412 412 PRO PRO B . n 
B 2 81  GLY 81  413 413 GLY GLY B . n 
B 2 82  GLN 82  414 414 GLN GLN B . n 
B 2 83  THR 83  415 415 THR THR B . n 
B 2 84  GLY 84  416 416 GLY GLY B . n 
B 2 85  LYS 85  417 417 LYS LYS B . n 
B 2 86  ILE 86  418 418 ILE ILE B . n 
B 2 87  ALA 87  419 419 ALA ALA B . n 
B 2 88  ASP 88  420 420 ASP ASP B . n 
B 2 89  TYR 89  421 421 TYR TYR B . n 
B 2 90  ASN 90  422 422 ASN ASN B . n 
B 2 91  TYR 91  423 423 TYR TYR B . n 
B 2 92  LYS 92  424 424 LYS LYS B . n 
B 2 93  LEU 93  425 425 LEU LEU B . n 
B 2 94  PRO 94  426 426 PRO PRO B . n 
B 2 95  ASP 95  427 427 ASP ASP B . n 
B 2 96  ASP 96  428 428 ASP ASP B . n 
B 2 97  PHE 97  429 429 PHE PHE B . n 
B 2 98  THR 98  430 430 THR THR B . n 
B 2 99  GLY 99  431 431 GLY GLY B . n 
B 2 100 CYS 100 432 432 CYS CYS B . n 
B 2 101 VAL 101 433 433 VAL VAL B . n 
B 2 102 ILE 102 434 434 ILE ILE B . n 
B 2 103 ALA 103 435 435 ALA ALA B . n 
B 2 104 TRP 104 436 436 TRP TRP B . n 
B 2 105 ASN 105 437 437 ASN ASN B . n 
B 2 106 SER 106 438 438 SER SER B . n 
B 2 107 ASN 107 439 439 ASN ASN B . n 
B 2 108 ASN 108 440 440 ASN ASN B . n 
B 2 109 LEU 109 441 441 LEU LEU B . n 
B 2 110 ASP 110 442 442 ASP ASP B . n 
B 2 111 SER 111 443 443 SER SER B . n 
B 2 112 LYS 112 444 444 LYS LYS B . n 
B 2 113 VAL 113 445 445 VAL VAL B . n 
B 2 114 GLY 114 446 446 GLY GLY B . n 
B 2 115 GLY 115 447 447 GLY GLY B . n 
B 2 116 ASN 116 448 448 ASN ASN B . n 
B 2 117 TYR 117 449 449 TYR TYR B . n 
B 2 118 ASN 118 450 450 ASN ASN B . n 
B 2 119 TYR 119 451 451 TYR TYR B . n 
B 2 120 LEU 120 452 452 LEU LEU B . n 
B 2 121 TYR 121 453 453 TYR TYR B . n 
B 2 122 ARG 122 454 454 ARG ARG B . n 
B 2 123 LEU 123 455 455 LEU LEU B . n 
B 2 124 PHE 124 456 456 PHE PHE B . n 
B 2 125 ARG 125 457 457 ARG ARG B . n 
B 2 126 LYS 126 458 458 LYS LYS B . n 
B 2 127 SER 127 459 459 SER SER B . n 
B 2 128 ASN 128 460 460 ASN ASN B . n 
B 2 129 LEU 129 461 461 LEU LEU B . n 
B 2 130 LYS 130 462 462 LYS LYS B . n 
B 2 131 PRO 131 463 463 PRO PRO B . n 
B 2 132 PHE 132 464 464 PHE PHE B . n 
B 2 133 GLU 133 465 465 GLU GLU B . n 
B 2 134 ARG 134 466 466 ARG ARG B . n 
B 2 135 ASP 135 467 467 ASP ASP B . n 
B 2 136 ILE 136 468 468 ILE ILE B . n 
B 2 137 SER 137 469 469 SER SER B . n 
B 2 138 THR 138 470 470 THR THR B . n 
B 2 139 GLU 139 471 471 GLU GLU B . n 
B 2 140 ILE 140 472 472 ILE ILE B . n 
B 2 141 TYR 141 473 473 TYR TYR B . n 
B 2 142 GLN 142 474 474 GLN GLN B . n 
B 2 143 ALA 143 475 475 ALA ALA B . n 
B 2 144 GLY 144 476 476 GLY GLY B . n 
B 2 145 SER 145 477 477 SER SER B . n 
B 2 146 THR 146 478 478 THR THR B . n 
B 2 147 PRO 147 479 479 PRO PRO B . n 
B 2 148 CYS 148 480 480 CYS CYS B . n 
B 2 149 ASN 149 481 481 ASN ASN B . n 
B 2 150 GLY 150 482 482 GLY GLY B . n 
B 2 151 VAL 151 483 483 VAL VAL B . n 
B 2 152 GLU 152 484 484 GLU GLU B . n 
B 2 153 GLY 153 485 485 GLY GLY B . n 
B 2 154 PHE 154 486 486 PHE PHE B . n 
B 2 155 ASN 155 487 487 ASN ASN B . n 
B 2 156 CYS 156 488 488 CYS CYS B . n 
B 2 157 TYR 157 489 489 TYR TYR B . n 
B 2 158 PHE 158 490 490 PHE PHE B . n 
B 2 159 PRO 159 491 491 PRO PRO B . n 
B 2 160 LEU 160 492 492 LEU LEU B . n 
B 2 161 GLN 161 493 493 GLN GLN B . n 
B 2 162 SER 162 494 494 SER SER B . n 
B 2 163 TYR 163 495 495 TYR TYR B . n 
B 2 164 GLY 164 496 496 GLY GLY B . n 
B 2 165 PHE 165 497 497 PHE PHE B . n 
B 2 166 GLN 166 498 498 GLN GLN B . n 
B 2 167 PRO 167 499 499 PRO PRO B . n 
B 2 168 THR 168 500 500 THR THR B . n 
B 2 169 TYR 169 501 501 TYR TYR B . n 
B 2 170 GLY 170 502 502 GLY GLY B . n 
B 2 171 VAL 171 503 503 VAL VAL B . n 
B 2 172 GLY 172 504 504 GLY GLY B . n 
B 2 173 TYR 173 505 505 TYR TYR B . n 
B 2 174 GLN 174 506 506 GLN GLN B . n 
B 2 175 PRO 175 507 507 PRO PRO B . n 
B 2 176 TYR 176 508 508 TYR TYR B . n 
B 2 177 ARG 177 509 509 ARG ARG B . n 
B 2 178 VAL 178 510 510 VAL VAL B . n 
B 2 179 VAL 179 511 511 VAL VAL B . n 
B 2 180 VAL 180 512 512 VAL VAL B . n 
B 2 181 LEU 181 513 513 LEU LEU B . n 
B 2 182 SER 182 514 514 SER SER B . n 
B 2 183 PHE 183 515 515 PHE PHE B . n 
B 2 184 GLU 184 516 516 GLU GLU B . n 
B 2 185 LEU 185 517 517 LEU LEU B . n 
B 2 186 LEU 186 518 518 LEU LEU B . n 
B 2 187 HIS 187 519 519 HIS HIS B . n 
B 2 188 ALA 188 520 520 ALA ALA B . n 
B 2 189 PRO 189 521 521 PRO PRO B . n 
B 2 190 ALA 190 522 522 ALA ALA B . n 
B 2 191 THR 191 523 523 THR THR B . n 
B 2 192 VAL 192 524 524 VAL VAL B . n 
B 2 193 CYS 193 525 525 CYS CYS B . n 
B 2 194 GLY 194 526 526 GLY GLY B . n 
B 2 195 SER 195 527 527 SER SER B . n 
B 2 196 ASN 196 528 528 ASN ASN B . n 
B 2 197 SER 197 529 529 SER SER B . n 
B 2 198 GLU 198 530 ?   ?   ?   B . n 
B 2 199 ASN 199 531 ?   ?   ?   B . n 
B 2 200 LEU 200 532 ?   ?   ?   B . n 
B 2 201 TYR 201 533 ?   ?   ?   B . n 
B 2 202 PHE 202 534 ?   ?   ?   B . n 
B 2 203 GLN 203 535 ?   ?   ?   B . n 
B 2 204 GLY 204 536 ?   ?   ?   B . n 
B 2 205 SER 205 537 ?   ?   ?   B . n 
B 2 206 HIS 206 538 ?   ?   ?   B . n 
B 2 207 HIS 207 539 ?   ?   ?   B . n 
B 2 208 HIS 208 540 ?   ?   ?   B . n 
B 2 209 HIS 209 541 ?   ?   ?   B . n 
B 2 210 HIS 210 542 ?   ?   ?   B . n 
B 2 211 HIS 211 543 ?   ?   ?   B . n 
B 2 212 HIS 212 544 ?   ?   ?   B . n 
B 2 213 HIS 213 545 ?   ?   ?   B . n 
B 2 214 HIS 214 546 ?   ?   ?   B . n 
B 2 215 HIS 215 547 ?   ?   ?   B . n 
B 2 216 GLY 216 548 ?   ?   ?   B . n 
B 2 217 LEU 217 549 ?   ?   ?   B . n 
B 2 218 ASN 218 550 ?   ?   ?   B . n 
B 2 219 ASP 219 551 ?   ?   ?   B . n 
B 2 220 ILE 220 552 ?   ?   ?   B . n 
B 2 221 PHE 221 553 ?   ?   ?   B . n 
B 2 222 GLU 222 554 ?   ?   ?   B . n 
B 2 223 ALA 223 555 ?   ?   ?   B . n 
B 2 224 GLN 224 556 ?   ?   ?   B . n 
B 2 225 LYS 225 557 ?   ?   ?   B . n 
B 2 226 ILE 226 558 ?   ?   ?   B . n 
B 2 227 GLU 227 559 ?   ?   ?   B . n 
B 2 228 TRP 228 560 ?   ?   ?   B . n 
B 2 229 HIS 229 561 ?   ?   ?   B . n 
B 2 230 GLU 230 562 ?   ?   ?   B . n 
C 1 1   ASP 1   1   1   ASP ASP C . n 
C 1 2   LYS 2   2   2   LYS LYS C . n 
C 1 3   GLU 3   3   3   GLU GLU C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   ILE 5   5   5   ILE ILE C . n 
C 1 6   LEU 6   6   6   LEU LEU C . n 
C 1 7   GLN 7   7   7   GLN GLN C . n 
C 1 8   LYS 8   8   8   LYS LYS C . n 
C 1 9   ILE 9   9   9   ILE ILE C . n 
C 1 10  TYR 10  10  10  TYR TYR C . n 
C 1 11  GLU 11  11  11  GLU GLU C . n 
C 1 12  ILE 12  12  12  ILE ILE C . n 
C 1 13  MET 13  13  13  MET MET C . n 
C 1 14  ARG 14  14  14  ARG ARG C . n 
C 1 15  ARG 15  15  15  ARG ARG C . n 
C 1 16  LEU 16  16  16  LEU LEU C . n 
C 1 17  ASP 17  17  17  ASP ASP C . n 
C 1 18  GLU 18  18  18  GLU GLU C . n 
C 1 19  GLU 19  19  19  GLU GLU C . n 
C 1 20  GLY 20  20  20  GLY GLY C . n 
C 1 21  HIS 21  21  21  HIS HIS C . n 
C 1 22  GLY 22  22  22  GLY GLY C . n 
C 1 23  GLU 23  23  23  GLU GLU C . n 
C 1 24  ALA 24  24  24  ALA ALA C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  ARG 27  27  27  ARG ARG C . n 
C 1 28  VAL 28  28  28  VAL VAL C . n 
C 1 29  SER 29  29  29  SER SER C . n 
C 1 30  ASP 30  30  30  ASP ASP C . n 
C 1 31  LEU 31  31  31  LEU LEU C . n 
C 1 32  ILE 32  32  32  ILE ILE C . n 
C 1 33  TYR 33  33  33  TYR TYR C . n 
C 1 34  GLU 34  34  34  GLU GLU C . n 
C 1 35  PHE 35  35  35  PHE PHE C . n 
C 1 36  MET 36  36  36  MET MET C . n 
C 1 37  LYS 37  37  37  LYS LYS C . n 
C 1 38  LYS 38  38  38  LYS LYS C . n 
C 1 39  ASP 39  39  39  ASP ASP C . n 
D 2 1   THR 1   333 ?   ?   ?   D . n 
D 2 2   ASN 2   334 334 ASN ASN D . n 
D 2 3   LEU 3   335 335 LEU LEU D . n 
D 2 4   CYS 4   336 336 CYS CYS D . n 
D 2 5   PRO 5   337 337 PRO PRO D . n 
D 2 6   PHE 6   338 338 PHE PHE D . n 
D 2 7   GLY 7   339 339 GLY GLY D . n 
D 2 8   GLU 8   340 340 GLU GLU D . n 
D 2 9   VAL 9   341 341 VAL VAL D . n 
D 2 10  PHE 10  342 342 PHE PHE D . n 
D 2 11  ASN 11  343 343 ASN ASN D . n 
D 2 12  ALA 12  344 344 ALA ALA D . n 
D 2 13  THR 13  345 345 THR THR D . n 
D 2 14  ARG 14  346 346 ARG ARG D . n 
D 2 15  PHE 15  347 347 PHE PHE D . n 
D 2 16  ALA 16  348 348 ALA ALA D . n 
D 2 17  SER 17  349 349 SER SER D . n 
D 2 18  VAL 18  350 350 VAL VAL D . n 
D 2 19  TYR 19  351 351 TYR TYR D . n 
D 2 20  ALA 20  352 352 ALA ALA D . n 
D 2 21  TRP 21  353 353 TRP TRP D . n 
D 2 22  ASN 22  354 354 ASN ASN D . n 
D 2 23  ARG 23  355 355 ARG ARG D . n 
D 2 24  LYS 24  356 356 LYS LYS D . n 
D 2 25  ARG 25  357 357 ARG ARG D . n 
D 2 26  ILE 26  358 358 ILE ILE D . n 
D 2 27  SER 27  359 359 SER SER D . n 
D 2 28  ASN 28  360 360 ASN ASN D . n 
D 2 29  CYS 29  361 361 CYS CYS D . n 
D 2 30  VAL 30  362 362 VAL VAL D . n 
D 2 31  ALA 31  363 363 ALA ALA D . n 
D 2 32  ASP 32  364 364 ASP ASP D . n 
D 2 33  TYR 33  365 365 TYR TYR D . n 
D 2 34  SER 34  366 366 SER SER D . n 
D 2 35  VAL 35  367 367 VAL VAL D . n 
D 2 36  LEU 36  368 368 LEU LEU D . n 
D 2 37  TYR 37  369 369 TYR TYR D . n 
D 2 38  ASN 38  370 370 ASN ASN D . n 
D 2 39  SER 39  371 371 SER SER D . n 
D 2 40  ALA 40  372 372 ALA ALA D . n 
D 2 41  SER 41  373 373 SER SER D . n 
D 2 42  PHE 42  374 374 PHE PHE D . n 
D 2 43  SER 43  375 375 SER SER D . n 
D 2 44  THR 44  376 376 THR THR D . n 
D 2 45  PHE 45  377 377 PHE PHE D . n 
D 2 46  LYS 46  378 378 LYS LYS D . n 
D 2 47  CYS 47  379 379 CYS CYS D . n 
D 2 48  TYR 48  380 380 TYR TYR D . n 
D 2 49  GLY 49  381 381 GLY GLY D . n 
D 2 50  VAL 50  382 382 VAL VAL D . n 
D 2 51  SER 51  383 383 SER SER D . n 
D 2 52  PRO 52  384 384 PRO PRO D . n 
D 2 53  THR 53  385 385 THR THR D . n 
D 2 54  LYS 54  386 386 LYS LYS D . n 
D 2 55  LEU 55  387 387 LEU LEU D . n 
D 2 56  ASN 56  388 388 ASN ASN D . n 
D 2 57  ASP 57  389 389 ASP ASP D . n 
D 2 58  LEU 58  390 390 LEU LEU D . n 
D 2 59  CYS 59  391 391 CYS CYS D . n 
D 2 60  PHE 60  392 392 PHE PHE D . n 
D 2 61  THR 61  393 393 THR THR D . n 
D 2 62  ASN 62  394 394 ASN ASN D . n 
D 2 63  VAL 63  395 395 VAL VAL D . n 
D 2 64  TYR 64  396 396 TYR TYR D . n 
D 2 65  ALA 65  397 397 ALA ALA D . n 
D 2 66  ASP 66  398 398 ASP ASP D . n 
D 2 67  SER 67  399 399 SER SER D . n 
D 2 68  PHE 68  400 400 PHE PHE D . n 
D 2 69  VAL 69  401 401 VAL VAL D . n 
D 2 70  ILE 70  402 402 ILE ILE D . n 
D 2 71  ARG 71  403 403 ARG ARG D . n 
D 2 72  GLY 72  404 404 GLY GLY D . n 
D 2 73  ASP 73  405 405 ASP ASP D . n 
D 2 74  GLU 74  406 406 GLU GLU D . n 
D 2 75  VAL 75  407 407 VAL VAL D . n 
D 2 76  ARG 76  408 408 ARG ARG D . n 
D 2 77  GLN 77  409 409 GLN GLN D . n 
D 2 78  ILE 78  410 410 ILE ILE D . n 
D 2 79  ALA 79  411 411 ALA ALA D . n 
D 2 80  PRO 80  412 412 PRO PRO D . n 
D 2 81  GLY 81  413 413 GLY GLY D . n 
D 2 82  GLN 82  414 414 GLN GLN D . n 
D 2 83  THR 83  415 415 THR THR D . n 
D 2 84  GLY 84  416 416 GLY GLY D . n 
D 2 85  LYS 85  417 417 LYS LYS D . n 
D 2 86  ILE 86  418 418 ILE ILE D . n 
D 2 87  ALA 87  419 419 ALA ALA D . n 
D 2 88  ASP 88  420 420 ASP ASP D . n 
D 2 89  TYR 89  421 421 TYR TYR D . n 
D 2 90  ASN 90  422 422 ASN ASN D . n 
D 2 91  TYR 91  423 423 TYR TYR D . n 
D 2 92  LYS 92  424 424 LYS LYS D . n 
D 2 93  LEU 93  425 425 LEU LEU D . n 
D 2 94  PRO 94  426 426 PRO PRO D . n 
D 2 95  ASP 95  427 427 ASP ASP D . n 
D 2 96  ASP 96  428 428 ASP ASP D . n 
D 2 97  PHE 97  429 429 PHE PHE D . n 
D 2 98  THR 98  430 430 THR THR D . n 
D 2 99  GLY 99  431 431 GLY GLY D . n 
D 2 100 CYS 100 432 432 CYS CYS D . n 
D 2 101 VAL 101 433 433 VAL VAL D . n 
D 2 102 ILE 102 434 434 ILE ILE D . n 
D 2 103 ALA 103 435 435 ALA ALA D . n 
D 2 104 TRP 104 436 436 TRP TRP D . n 
D 2 105 ASN 105 437 437 ASN ASN D . n 
D 2 106 SER 106 438 438 SER SER D . n 
D 2 107 ASN 107 439 439 ASN ASN D . n 
D 2 108 ASN 108 440 440 ASN ASN D . n 
D 2 109 LEU 109 441 441 LEU LEU D . n 
D 2 110 ASP 110 442 442 ASP ASP D . n 
D 2 111 SER 111 443 443 SER SER D . n 
D 2 112 LYS 112 444 444 LYS LYS D . n 
D 2 113 VAL 113 445 445 VAL VAL D . n 
D 2 114 GLY 114 446 446 GLY GLY D . n 
D 2 115 GLY 115 447 447 GLY GLY D . n 
D 2 116 ASN 116 448 448 ASN ASN D . n 
D 2 117 TYR 117 449 449 TYR TYR D . n 
D 2 118 ASN 118 450 450 ASN ASN D . n 
D 2 119 TYR 119 451 451 TYR TYR D . n 
D 2 120 LEU 120 452 452 LEU LEU D . n 
D 2 121 TYR 121 453 453 TYR TYR D . n 
D 2 122 ARG 122 454 454 ARG ARG D . n 
D 2 123 LEU 123 455 455 LEU LEU D . n 
D 2 124 PHE 124 456 456 PHE PHE D . n 
D 2 125 ARG 125 457 457 ARG ARG D . n 
D 2 126 LYS 126 458 458 LYS LYS D . n 
D 2 127 SER 127 459 459 SER SER D . n 
D 2 128 ASN 128 460 460 ASN ASN D . n 
D 2 129 LEU 129 461 461 LEU LEU D . n 
D 2 130 LYS 130 462 462 LYS LYS D . n 
D 2 131 PRO 131 463 463 PRO PRO D . n 
D 2 132 PHE 132 464 464 PHE PHE D . n 
D 2 133 GLU 133 465 465 GLU GLU D . n 
D 2 134 ARG 134 466 466 ARG ARG D . n 
D 2 135 ASP 135 467 467 ASP ASP D . n 
D 2 136 ILE 136 468 468 ILE ILE D . n 
D 2 137 SER 137 469 469 SER SER D . n 
D 2 138 THR 138 470 470 THR THR D . n 
D 2 139 GLU 139 471 471 GLU GLU D . n 
D 2 140 ILE 140 472 472 ILE ILE D . n 
D 2 141 TYR 141 473 473 TYR TYR D . n 
D 2 142 GLN 142 474 474 GLN GLN D . n 
D 2 143 ALA 143 475 475 ALA ALA D . n 
D 2 144 GLY 144 476 476 GLY GLY D . n 
D 2 145 SER 145 477 477 SER SER D . n 
D 2 146 THR 146 478 478 THR THR D . n 
D 2 147 PRO 147 479 479 PRO PRO D . n 
D 2 148 CYS 148 480 480 CYS CYS D . n 
D 2 149 ASN 149 481 481 ASN ASN D . n 
D 2 150 GLY 150 482 482 GLY GLY D . n 
D 2 151 VAL 151 483 483 VAL VAL D . n 
D 2 152 GLU 152 484 484 GLU GLU D . n 
D 2 153 GLY 153 485 485 GLY GLY D . n 
D 2 154 PHE 154 486 486 PHE PHE D . n 
D 2 155 ASN 155 487 487 ASN ASN D . n 
D 2 156 CYS 156 488 488 CYS CYS D . n 
D 2 157 TYR 157 489 489 TYR TYR D . n 
D 2 158 PHE 158 490 490 PHE PHE D . n 
D 2 159 PRO 159 491 491 PRO PRO D . n 
D 2 160 LEU 160 492 492 LEU LEU D . n 
D 2 161 GLN 161 493 493 GLN GLN D . n 
D 2 162 SER 162 494 494 SER SER D . n 
D 2 163 TYR 163 495 495 TYR TYR D . n 
D 2 164 GLY 164 496 496 GLY GLY D . n 
D 2 165 PHE 165 497 497 PHE PHE D . n 
D 2 166 GLN 166 498 498 GLN GLN D . n 
D 2 167 PRO 167 499 499 PRO PRO D . n 
D 2 168 THR 168 500 500 THR THR D . n 
D 2 169 TYR 169 501 501 TYR TYR D . n 
D 2 170 GLY 170 502 502 GLY GLY D . n 
D 2 171 VAL 171 503 503 VAL VAL D . n 
D 2 172 GLY 172 504 504 GLY GLY D . n 
D 2 173 TYR 173 505 505 TYR TYR D . n 
D 2 174 GLN 174 506 506 GLN GLN D . n 
D 2 175 PRO 175 507 507 PRO PRO D . n 
D 2 176 TYR 176 508 508 TYR TYR D . n 
D 2 177 ARG 177 509 509 ARG ARG D . n 
D 2 178 VAL 178 510 510 VAL VAL D . n 
D 2 179 VAL 179 511 511 VAL VAL D . n 
D 2 180 VAL 180 512 512 VAL VAL D . n 
D 2 181 LEU 181 513 513 LEU LEU D . n 
D 2 182 SER 182 514 514 SER SER D . n 
D 2 183 PHE 183 515 515 PHE PHE D . n 
D 2 184 GLU 184 516 516 GLU GLU D . n 
D 2 185 LEU 185 517 517 LEU LEU D . n 
D 2 186 LEU 186 518 518 LEU LEU D . n 
D 2 187 HIS 187 519 519 HIS HIS D . n 
D 2 188 ALA 188 520 520 ALA ALA D . n 
D 2 189 PRO 189 521 521 PRO PRO D . n 
D 2 190 ALA 190 522 522 ALA ALA D . n 
D 2 191 THR 191 523 523 THR THR D . n 
D 2 192 VAL 192 524 524 VAL VAL D . n 
D 2 193 CYS 193 525 525 CYS CYS D . n 
D 2 194 GLY 194 526 526 GLY GLY D . n 
D 2 195 SER 195 527 527 SER SER D . n 
D 2 196 ASN 196 528 528 ASN ASN D . n 
D 2 197 SER 197 529 529 SER SER D . n 
D 2 198 GLU 198 530 ?   ?   ?   D . n 
D 2 199 ASN 199 531 ?   ?   ?   D . n 
D 2 200 LEU 200 532 ?   ?   ?   D . n 
D 2 201 TYR 201 533 ?   ?   ?   D . n 
D 2 202 PHE 202 534 ?   ?   ?   D . n 
D 2 203 GLN 203 535 ?   ?   ?   D . n 
D 2 204 GLY 204 536 ?   ?   ?   D . n 
D 2 205 SER 205 537 ?   ?   ?   D . n 
D 2 206 HIS 206 538 ?   ?   ?   D . n 
D 2 207 HIS 207 539 ?   ?   ?   D . n 
D 2 208 HIS 208 540 ?   ?   ?   D . n 
D 2 209 HIS 209 541 ?   ?   ?   D . n 
D 2 210 HIS 210 542 ?   ?   ?   D . n 
D 2 211 HIS 211 543 ?   ?   ?   D . n 
D 2 212 HIS 212 544 ?   ?   ?   D . n 
D 2 213 HIS 213 545 ?   ?   ?   D . n 
D 2 214 HIS 214 546 ?   ?   ?   D . n 
D 2 215 HIS 215 547 ?   ?   ?   D . n 
D 2 216 GLY 216 548 ?   ?   ?   D . n 
D 2 217 LEU 217 549 ?   ?   ?   D . n 
D 2 218 ASN 218 550 ?   ?   ?   D . n 
D 2 219 ASP 219 551 ?   ?   ?   D . n 
D 2 220 ILE 220 552 ?   ?   ?   D . n 
D 2 221 PHE 221 553 ?   ?   ?   D . n 
D 2 222 GLU 222 554 ?   ?   ?   D . n 
D 2 223 ALA 223 555 ?   ?   ?   D . n 
D 2 224 GLN 224 556 ?   ?   ?   D . n 
D 2 225 LYS 225 557 ?   ?   ?   D . n 
D 2 226 ILE 226 558 ?   ?   ?   D . n 
D 2 227 GLU 227 559 ?   ?   ?   D . n 
D 2 228 TRP 228 560 ?   ?   ?   D . n 
D 2 229 HIS 229 561 ?   ?   ?   D . n 
D 2 230 GLU 230 562 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 NAG 1 601 601 NAG NAG B . 
F 3 NAG 1 601 601 NAG NAG D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YDT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     73.307 
_cell.length_a_esd                 ? 
_cell.length_b                     73.307 
_cell.length_b_esd                 ? 
_cell.length_c                     99.799 
_cell.length_c_esd                 ? 
_cell.volume                       464459.355 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         8YDT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                144 
_symmetry.space_group_name_Hall            'P 31' 
_symmetry.space_group_name_H-M             'P 31' 
_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                   8YDT 
_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             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.68 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M magnesium formate dihydrate' 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-08-18 
_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   1 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YDT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.46 
_reflns.d_resolution_low                               50 
_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                                     21629 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.65 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.082 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.46 
_reflns_shell.d_res_low                                     2.61 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3501 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.764 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               87.37 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YDT 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             39.23 
_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                     20669 
_refine.ls_number_reflns_R_free                  1040 
_refine.ls_number_reflns_R_work                  19629 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2306 
_refine.ls_R_factor_R_free                       0.2680 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2286 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.98 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 40.3264 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4263 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        39.23 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               3806 
_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        3778 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_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' ? 0.0087  ? 3904 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0114  ? 5292 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0558  ? 556  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 688  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.8029 ? 1410 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.50 2.63  . . 149 2804 99.46  . . . . 0.3561 . . . . . . . . . . . 0.3887 
'X-RAY DIFFRACTION' 2.63 2.80  . . 151 2810 99.80  . . . . 0.3306 . . . . . . . . . . . 0.4066 
'X-RAY DIFFRACTION' 2.80 3.01  . . 144 2802 99.80  . . . . 0.2989 . . . . . . . . . . . 0.3759 
'X-RAY DIFFRACTION' 3.01 3.32  . . 145 2822 99.97  . . . . 0.2945 . . . . . . . . . . . 0.4052 
'X-RAY DIFFRACTION' 3.32 3.80  . . 148 2775 99.12  . . . . 0.2659 . . . . . . . . . . . 0.2900 
'X-RAY DIFFRACTION' 3.80 4.78  . . 149 2829 100.00 . . . . 0.2152 . . . . . . . . . . . 0.2230 
'X-RAY DIFFRACTION' 4.79 39.23 . . 154 2787 99.32  . . . . 0.1837 . . . . . . . . . . . 0.2273 
# 
_struct.entry_id                     8YDT 
_struct.title                        
'Crystal structure of the receptor binding domain of SARS-CoV-2 Alpha variant spike protein in complex with Ce41' 
_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        8YDT 
_struct_keywords.text            'RBD, VIRAL PROTEIN-INHIBITOR COMPLEX' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/INHIBITOR' 
# 
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 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 8YDT        8YDT   ? 1 ? 1   
2 UNP SPIKE_SARS2 P0DTC2 ? 2 
;TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAP
GQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPL
QSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCG
;
333 
# 
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 8YDT A 1 ? 39  ? 8YDT   1   ? 39  ? 1   39  
2 2 8YDT B 1 ? 194 ? P0DTC2 333 ? 526 ? 333 526 
3 1 8YDT C 1 ? 39  ? 8YDT   1   ? 39  ? 1   39  
4 2 8YDT D 1 ? 194 ? P0DTC2 333 ? 526 ? 333 526 
# 
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 
2 8YDT TYR B 169 ? UNP P0DTC2 ASN 501 variant          501 1  
2 8YDT SER B 195 ? UNP P0DTC2 ?   ?   'expression tag' 527 2  
2 8YDT ASN B 196 ? UNP P0DTC2 ?   ?   'expression tag' 528 3  
2 8YDT SER B 197 ? UNP P0DTC2 ?   ?   'expression tag' 529 4  
2 8YDT GLU B 198 ? UNP P0DTC2 ?   ?   'expression tag' 530 5  
2 8YDT ASN B 199 ? UNP P0DTC2 ?   ?   'expression tag' 531 6  
2 8YDT LEU B 200 ? UNP P0DTC2 ?   ?   'expression tag' 532 7  
2 8YDT TYR B 201 ? UNP P0DTC2 ?   ?   'expression tag' 533 8  
2 8YDT PHE B 202 ? UNP P0DTC2 ?   ?   'expression tag' 534 9  
2 8YDT GLN B 203 ? UNP P0DTC2 ?   ?   'expression tag' 535 10 
2 8YDT GLY B 204 ? UNP P0DTC2 ?   ?   'expression tag' 536 11 
2 8YDT SER B 205 ? UNP P0DTC2 ?   ?   'expression tag' 537 12 
2 8YDT HIS B 206 ? UNP P0DTC2 ?   ?   'expression tag' 538 13 
2 8YDT HIS B 207 ? UNP P0DTC2 ?   ?   'expression tag' 539 14 
2 8YDT HIS B 208 ? UNP P0DTC2 ?   ?   'expression tag' 540 15 
2 8YDT HIS B 209 ? UNP P0DTC2 ?   ?   'expression tag' 541 16 
2 8YDT HIS B 210 ? UNP P0DTC2 ?   ?   'expression tag' 542 17 
2 8YDT HIS B 211 ? UNP P0DTC2 ?   ?   'expression tag' 543 18 
2 8YDT HIS B 212 ? UNP P0DTC2 ?   ?   'expression tag' 544 19 
2 8YDT HIS B 213 ? UNP P0DTC2 ?   ?   'expression tag' 545 20 
2 8YDT HIS B 214 ? UNP P0DTC2 ?   ?   'expression tag' 546 21 
2 8YDT HIS B 215 ? UNP P0DTC2 ?   ?   'expression tag' 547 22 
2 8YDT GLY B 216 ? UNP P0DTC2 ?   ?   'expression tag' 548 23 
2 8YDT LEU B 217 ? UNP P0DTC2 ?   ?   'expression tag' 549 24 
2 8YDT ASN B 218 ? UNP P0DTC2 ?   ?   'expression tag' 550 25 
2 8YDT ASP B 219 ? UNP P0DTC2 ?   ?   'expression tag' 551 26 
2 8YDT ILE B 220 ? UNP P0DTC2 ?   ?   'expression tag' 552 27 
2 8YDT PHE B 221 ? UNP P0DTC2 ?   ?   'expression tag' 553 28 
2 8YDT GLU B 222 ? UNP P0DTC2 ?   ?   'expression tag' 554 29 
2 8YDT ALA B 223 ? UNP P0DTC2 ?   ?   'expression tag' 555 30 
2 8YDT GLN B 224 ? UNP P0DTC2 ?   ?   'expression tag' 556 31 
2 8YDT LYS B 225 ? UNP P0DTC2 ?   ?   'expression tag' 557 32 
2 8YDT ILE B 226 ? UNP P0DTC2 ?   ?   'expression tag' 558 33 
2 8YDT GLU B 227 ? UNP P0DTC2 ?   ?   'expression tag' 559 34 
2 8YDT TRP B 228 ? UNP P0DTC2 ?   ?   'expression tag' 560 35 
2 8YDT HIS B 229 ? UNP P0DTC2 ?   ?   'expression tag' 561 36 
2 8YDT GLU B 230 ? UNP P0DTC2 ?   ?   'expression tag' 562 37 
4 8YDT TYR D 169 ? UNP P0DTC2 ASN 501 variant          501 38 
4 8YDT SER D 195 ? UNP P0DTC2 ?   ?   'expression tag' 527 39 
4 8YDT ASN D 196 ? UNP P0DTC2 ?   ?   'expression tag' 528 40 
4 8YDT SER D 197 ? UNP P0DTC2 ?   ?   'expression tag' 529 41 
4 8YDT GLU D 198 ? UNP P0DTC2 ?   ?   'expression tag' 530 42 
4 8YDT ASN D 199 ? UNP P0DTC2 ?   ?   'expression tag' 531 43 
4 8YDT LEU D 200 ? UNP P0DTC2 ?   ?   'expression tag' 532 44 
4 8YDT TYR D 201 ? UNP P0DTC2 ?   ?   'expression tag' 533 45 
4 8YDT PHE D 202 ? UNP P0DTC2 ?   ?   'expression tag' 534 46 
4 8YDT GLN D 203 ? UNP P0DTC2 ?   ?   'expression tag' 535 47 
4 8YDT GLY D 204 ? UNP P0DTC2 ?   ?   'expression tag' 536 48 
4 8YDT SER D 205 ? UNP P0DTC2 ?   ?   'expression tag' 537 49 
4 8YDT HIS D 206 ? UNP P0DTC2 ?   ?   'expression tag' 538 50 
4 8YDT HIS D 207 ? UNP P0DTC2 ?   ?   'expression tag' 539 51 
4 8YDT HIS D 208 ? UNP P0DTC2 ?   ?   'expression tag' 540 52 
4 8YDT HIS D 209 ? UNP P0DTC2 ?   ?   'expression tag' 541 53 
4 8YDT HIS D 210 ? UNP P0DTC2 ?   ?   'expression tag' 542 54 
4 8YDT HIS D 211 ? UNP P0DTC2 ?   ?   'expression tag' 543 55 
4 8YDT HIS D 212 ? UNP P0DTC2 ?   ?   'expression tag' 544 56 
4 8YDT HIS D 213 ? UNP P0DTC2 ?   ?   'expression tag' 545 57 
4 8YDT HIS D 214 ? UNP P0DTC2 ?   ?   'expression tag' 546 58 
4 8YDT HIS D 215 ? UNP P0DTC2 ?   ?   'expression tag' 547 59 
4 8YDT GLY D 216 ? UNP P0DTC2 ?   ?   'expression tag' 548 60 
4 8YDT LEU D 217 ? UNP P0DTC2 ?   ?   'expression tag' 549 61 
4 8YDT ASN D 218 ? UNP P0DTC2 ?   ?   'expression tag' 550 62 
4 8YDT ASP D 219 ? UNP P0DTC2 ?   ?   'expression tag' 551 63 
4 8YDT ILE D 220 ? UNP P0DTC2 ?   ?   'expression tag' 552 64 
4 8YDT PHE D 221 ? UNP P0DTC2 ?   ?   'expression tag' 553 65 
4 8YDT GLU D 222 ? UNP P0DTC2 ?   ?   'expression tag' 554 66 
4 8YDT ALA D 223 ? UNP P0DTC2 ?   ?   'expression tag' 555 67 
4 8YDT GLN D 224 ? UNP P0DTC2 ?   ?   'expression tag' 556 68 
4 8YDT LYS D 225 ? UNP P0DTC2 ?   ?   'expression tag' 557 69 
4 8YDT ILE D 226 ? UNP P0DTC2 ?   ?   'expression tag' 558 70 
4 8YDT GLU D 227 ? UNP P0DTC2 ?   ?   'expression tag' 559 71 
4 8YDT TRP D 228 ? UNP P0DTC2 ?   ?   'expression tag' 560 72 
4 8YDT HIS D 229 ? UNP P0DTC2 ?   ?   'expression tag' 561 73 
4 8YDT GLU D 230 ? UNP P0DTC2 ?   ?   'expression tag' 562 74 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2170  ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  11880 ? 
2 'ABSA (A^2)' 2250  ? 
2 MORE         -3    ? 
2 'SSA (A^2)'  11820 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E 
2 1 C,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 2   ? GLU A 19  ? LYS A 2   GLU A 19  1 ? 18 
HELX_P HELX_P2  AA2 HIS A 21  ? LYS A 38  ? HIS A 21  LYS A 38  1 ? 18 
HELX_P HELX_P3  AA3 PHE B 6   ? ASN B 11  ? PHE B 338 ASN B 343 1 ? 6  
HELX_P HELX_P4  AA4 SER B 17  ? TRP B 21  ? SER B 349 TRP B 353 5 ? 5  
HELX_P HELX_P5  AA5 ASP B 32  ? ALA B 40  ? ASP B 364 ALA B 372 1 ? 9  
HELX_P HELX_P6  AA6 ASP B 73  ? ILE B 78  ? ASP B 405 ILE B 410 5 ? 6  
HELX_P HELX_P7  AA7 GLY B 84  ? ASN B 90  ? GLY B 416 ASN B 422 1 ? 7  
HELX_P HELX_P8  AA8 SER B 106 ? SER B 111 ? SER B 438 SER B 443 1 ? 6  
HELX_P HELX_P9  AA9 GLY B 170 ? TYR B 173 ? GLY B 502 TYR B 505 5 ? 4  
HELX_P HELX_P10 AB1 LYS C 2   ? GLY C 20  ? LYS C 2   GLY C 20  1 ? 19 
HELX_P HELX_P11 AB2 HIS C 21  ? MET C 36  ? HIS C 21  MET C 36  1 ? 16 
HELX_P HELX_P12 AB3 PRO D 5   ? ASN D 11  ? PRO D 337 ASN D 343 1 ? 7  
HELX_P HELX_P13 AB4 ASP D 32  ? ASN D 38  ? ASP D 364 ASN D 370 1 ? 7  
HELX_P HELX_P14 AB5 SER D 51  ? ASN D 56  ? SER D 383 ASN D 388 1 ? 6  
HELX_P HELX_P15 AB6 GLY D 72  ? ARG D 76  ? GLY D 404 ARG D 408 1 ? 5  
HELX_P HELX_P16 AB7 GLY D 84  ? ASN D 90  ? GLY D 416 ASN D 422 1 ? 7  
HELX_P HELX_P17 AB8 SER D 106 ? SER D 111 ? SER D 438 SER D 443 1 ? 6  
HELX_P HELX_P18 AB9 GLY D 170 ? TYR D 173 ? GLY D 502 TYR D 505 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?   ? B CYS 4   SG  ? ? ? 1_555 B CYS 29  SG ? ? B CYS 336 B CYS 361 1_555 ? ? ? ? ? ? ? 2.035 ? ?               
disulf2 disulf ?   ? B CYS 47  SG  ? ? ? 1_555 B CYS 100 SG ? ? B CYS 379 B CYS 432 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf3 disulf ?   ? B CYS 59  SG  ? ? ? 1_555 B CYS 193 SG ? ? B CYS 391 B CYS 525 1_555 ? ? ? ? ? ? ? 2.040 ? ?               
disulf4 disulf ?   ? B CYS 148 SG  ? ? ? 1_555 B CYS 156 SG ? ? B CYS 480 B CYS 488 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf5 disulf ?   ? D CYS 4   SG  ? ? ? 1_555 D CYS 29  SG ? ? D CYS 336 D CYS 361 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf6 disulf ?   ? D CYS 47  SG  ? ? ? 1_555 D CYS 100 SG ? ? D CYS 379 D CYS 432 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf7 disulf ?   ? D CYS 59  SG  ? ? ? 1_555 D CYS 193 SG ? ? D CYS 391 D CYS 525 1_555 ? ? ? ? ? ? ? 2.014 ? ?               
disulf8 disulf ?   ? D CYS 148 SG  ? ? ? 1_555 D CYS 156 SG ? ? D CYS 480 D CYS 488 1_555 ? ? ? ? ? ? ? 2.027 ? ?               
covale1 covale one ? B ASN 11  ND2 ? ? ? 1_555 E NAG .   C1 ? ? B ASN 343 B NAG 601 1_555 ? ? ? ? ? ? ? 1.461 ? N-Glycosylation 
covale2 covale one ? D ASN 11  ND2 ? ? ? 1_555 F NAG .   C1 ? ? D ASN 343 D NAG 601 1_555 ? ? ? ? ? ? ? 1.454 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG E .   ? ASN B 11  ? NAG B 601 ? 1_555 ASN B 343 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG F .   ? ASN D 11  ? NAG D 601 ? 1_555 ASN D 343 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  CYS B 4   ? CYS B 29  ? CYS B 336 ? 1_555 CYS B 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4  CYS B 47  ? CYS B 100 ? CYS B 379 ? 1_555 CYS B 432 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5  CYS B 59  ? CYS B 193 ? CYS B 391 ? 1_555 CYS B 525 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6  CYS B 148 ? CYS B 156 ? CYS B 480 ? 1_555 CYS B 488 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7  CYS D 4   ? CYS D 29  ? CYS D 336 ? 1_555 CYS D 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS D 47  ? CYS D 100 ? CYS D 379 ? 1_555 CYS D 432 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS D 59  ? CYS D 193 ? CYS D 391 ? 1_555 CYS D 525 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS D 148 ? CYS D 156 ? CYS D 480 ? 1_555 CYS D 488 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? 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 ASN B 22  ? ILE B 26  ? ASN B 354 ILE B 358 
AA1 2 ASN B 62  ? ARG B 71  ? ASN B 394 ARG B 403 
AA1 3 PRO B 175 ? GLU B 184 ? PRO B 507 GLU B 516 
AA1 4 GLY B 99  ? ASN B 105 ? GLY B 431 ASN B 437 
AA1 5 THR B 44  ? TYR B 48  ? THR B 376 TYR B 380 
AA2 1 CYS B 29  ? ALA B 31  ? CYS B 361 ALA B 363 
AA2 2 VAL B 192 ? GLY B 194 ? VAL B 524 GLY B 526 
AA2 3 CYS B 59  ? PHE B 60  ? CYS B 391 PHE B 392 
AA3 1 LEU B 120 ? ARG B 122 ? LEU B 452 ARG B 454 
AA3 2 LEU B 160 ? SER B 162 ? LEU B 492 SER B 494 
AA4 1 TYR B 141 ? GLN B 142 ? TYR B 473 GLN B 474 
AA4 2 CYS B 156 ? TYR B 157 ? CYS B 488 TYR B 489 
AA5 1 ASN D 22  ? ILE D 26  ? ASN D 354 ILE D 358 
AA5 2 ASN D 62  ? ARG D 71  ? ASN D 394 ARG D 403 
AA5 3 PRO D 175 ? GLU D 184 ? PRO D 507 GLU D 516 
AA5 4 GLY D 99  ? ASN D 105 ? GLY D 431 ASN D 437 
AA5 5 THR D 44  ? TYR D 48  ? THR D 376 TYR D 380 
AA6 1 CYS D 29  ? ALA D 31  ? CYS D 361 ALA D 363 
AA6 2 VAL D 192 ? GLY D 194 ? VAL D 524 GLY D 526 
AA6 3 CYS D 59  ? PHE D 60  ? CYS D 391 PHE D 392 
AA7 1 LEU D 120 ? ARG D 122 ? LEU D 452 ARG D 454 
AA7 2 LEU D 160 ? SER D 162 ? LEU D 492 SER D 494 
AA8 1 TYR D 141 ? GLN D 142 ? TYR D 473 GLN D 474 
AA8 2 CYS D 156 ? TYR D 157 ? CYS D 488 TYR D 489 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE B 26  ? N ILE B 358 O VAL B 63  ? O VAL B 395 
AA1 2 3 N ILE B 70  ? N ILE B 402 O TYR B 176 ? O TYR B 508 
AA1 3 4 O VAL B 179 ? O VAL B 511 N ILE B 102 ? N ILE B 434 
AA1 4 5 O VAL B 101 ? O VAL B 433 N LYS B 46  ? N LYS B 378 
AA2 1 2 N ALA B 31  ? N ALA B 363 O CYS B 193 ? O CYS B 525 
AA2 2 3 O VAL B 192 ? O VAL B 524 N PHE B 60  ? N PHE B 392 
AA3 1 2 N TYR B 121 ? N TYR B 453 O GLN B 161 ? O GLN B 493 
AA4 1 2 N TYR B 141 ? N TYR B 473 O TYR B 157 ? O TYR B 489 
AA5 1 2 N ILE D 26  ? N ILE D 358 O VAL D 63  ? O VAL D 395 
AA5 2 3 N ASP D 66  ? N ASP D 398 O VAL D 180 ? O VAL D 512 
AA5 3 4 O VAL D 179 ? O VAL D 511 N ILE D 102 ? N ILE D 434 
AA5 4 5 O GLY D 99  ? O GLY D 431 N TYR D 48  ? N TYR D 380 
AA6 1 2 N ALA D 31  ? N ALA D 363 O CYS D 193 ? O CYS D 525 
AA6 2 3 O VAL D 192 ? O VAL D 524 N PHE D 60  ? N PHE D 392 
AA7 1 2 N TYR D 121 ? N TYR D 453 O GLN D 161 ? O GLN D 493 
AA8 1 2 N TYR D 141 ? N TYR D 473 O TYR D 157 ? O TYR D 489 
# 
_pdbx_entry_details.entry_id                   8YDT 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 LYS A 38  ? ? -55.64  109.08  
2  1 TRP B 353 ? ? -47.16  156.18  
3  1 ASP B 364 ? ? -68.14  98.49   
4  1 PHE B 377 ? ? -154.06 51.79   
5  1 PRO B 384 ? ? -66.24  4.27    
6  1 PHE B 400 ? ? 175.88  174.05  
7  1 PRO B 412 ? ? -41.88  151.72  
8  1 ASP B 428 ? ? -76.69  43.97   
9  1 ASN B 481 ? ? 51.84   18.66   
10 1 HIS B 519 ? ? -69.71  88.39   
11 1 ALA B 522 ? ? 80.00   100.19  
12 1 HIS C 21  ? ? -96.13  55.75   
13 1 MET C 36  ? ? -67.64  10.07   
14 1 ALA D 352 ? ? -107.01 51.97   
15 1 ASN D 360 ? ? 61.01   71.78   
16 1 ALA D 372 ? ? -164.99 -148.72 
17 1 PHE D 377 ? ? -144.93 49.77   
18 1 ASN D 388 ? ? -69.93  3.81    
19 1 ALA D 411 ? ? -173.54 146.41  
20 1 ASN D 422 ? ? -124.21 -53.70  
21 1 ASP D 428 ? ? -87.40  33.09   
22 1 THR D 470 ? ? -103.32 43.35   
23 1 PRO D 499 ? ? -73.24  28.10   
24 1 LEU D 517 ? ? -101.46 48.89   
25 1 HIS D 519 ? ? -69.21  87.92   
26 1 ALA D 522 ? ? 74.81   115.27  
27 1 SER D 527 ? ? -70.49  44.02   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z         
2 -y,x-y,z+1/3  
3 -x+y,-x,z+2/3 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B THR 333 ? B THR 1   
2  1 Y 1 B GLU 530 ? B GLU 198 
3  1 Y 1 B ASN 531 ? B ASN 199 
4  1 Y 1 B LEU 532 ? B LEU 200 
5  1 Y 1 B TYR 533 ? B TYR 201 
6  1 Y 1 B PHE 534 ? B PHE 202 
7  1 Y 1 B GLN 535 ? B GLN 203 
8  1 Y 1 B GLY 536 ? B GLY 204 
9  1 Y 1 B SER 537 ? B SER 205 
10 1 Y 1 B HIS 538 ? B HIS 206 
11 1 Y 1 B HIS 539 ? B HIS 207 
12 1 Y 1 B HIS 540 ? B HIS 208 
13 1 Y 1 B HIS 541 ? B HIS 209 
14 1 Y 1 B HIS 542 ? B HIS 210 
15 1 Y 1 B HIS 543 ? B HIS 211 
16 1 Y 1 B HIS 544 ? B HIS 212 
17 1 Y 1 B HIS 545 ? B HIS 213 
18 1 Y 1 B HIS 546 ? B HIS 214 
19 1 Y 1 B HIS 547 ? B HIS 215 
20 1 Y 1 B GLY 548 ? B GLY 216 
21 1 Y 1 B LEU 549 ? B LEU 217 
22 1 Y 1 B ASN 550 ? B ASN 218 
23 1 Y 1 B ASP 551 ? B ASP 219 
24 1 Y 1 B ILE 552 ? B ILE 220 
25 1 Y 1 B PHE 553 ? B PHE 221 
26 1 Y 1 B GLU 554 ? B GLU 222 
27 1 Y 1 B ALA 555 ? B ALA 223 
28 1 Y 1 B GLN 556 ? B GLN 224 
29 1 Y 1 B LYS 557 ? B LYS 225 
30 1 Y 1 B ILE 558 ? B ILE 226 
31 1 Y 1 B GLU 559 ? B GLU 227 
32 1 Y 1 B TRP 560 ? B TRP 228 
33 1 Y 1 B HIS 561 ? B HIS 229 
34 1 Y 1 B GLU 562 ? B GLU 230 
35 1 Y 1 D THR 333 ? D THR 1   
36 1 Y 1 D GLU 530 ? D GLU 198 
37 1 Y 1 D ASN 531 ? D ASN 199 
38 1 Y 1 D LEU 532 ? D LEU 200 
39 1 Y 1 D TYR 533 ? D TYR 201 
40 1 Y 1 D PHE 534 ? D PHE 202 
41 1 Y 1 D GLN 535 ? D GLN 203 
42 1 Y 1 D GLY 536 ? D GLY 204 
43 1 Y 1 D SER 537 ? D SER 205 
44 1 Y 1 D HIS 538 ? D HIS 206 
45 1 Y 1 D HIS 539 ? D HIS 207 
46 1 Y 1 D HIS 540 ? D HIS 208 
47 1 Y 1 D HIS 541 ? D HIS 209 
48 1 Y 1 D HIS 542 ? D HIS 210 
49 1 Y 1 D HIS 543 ? D HIS 211 
50 1 Y 1 D HIS 544 ? D HIS 212 
51 1 Y 1 D HIS 545 ? D HIS 213 
52 1 Y 1 D HIS 546 ? D HIS 214 
53 1 Y 1 D HIS 547 ? D HIS 215 
54 1 Y 1 D GLY 548 ? D GLY 216 
55 1 Y 1 D LEU 549 ? D LEU 217 
56 1 Y 1 D ASN 550 ? D ASN 218 
57 1 Y 1 D ASP 551 ? D ASP 219 
58 1 Y 1 D ILE 552 ? D ILE 220 
59 1 Y 1 D PHE 553 ? D PHE 221 
60 1 Y 1 D GLU 554 ? D GLU 222 
61 1 Y 1 D ALA 555 ? D ALA 223 
62 1 Y 1 D GLN 556 ? D GLN 224 
63 1 Y 1 D LYS 557 ? D LYS 225 
64 1 Y 1 D ILE 558 ? D ILE 226 
65 1 Y 1 D GLU 559 ? D GLU 227 
66 1 Y 1 D TRP 560 ? D TRP 228 
67 1 Y 1 D HIS 561 ? D HIS 229 
68 1 Y 1 D GLU 562 ? D GLU 230 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
NAG C1   C N R 247 
NAG C2   C N R 248 
NAG C3   C N R 249 
NAG C4   C N S 250 
NAG C5   C N R 251 
NAG C6   C N N 252 
NAG C7   C N N 253 
NAG C8   C N N 254 
NAG N2   N N N 255 
NAG O1   O N N 256 
NAG O3   O N N 257 
NAG O4   O N N 258 
NAG O5   O N N 259 
NAG O6   O N N 260 
NAG O7   O N N 261 
NAG H1   H N N 262 
NAG H2   H N N 263 
NAG H3   H N N 264 
NAG H4   H N N 265 
NAG H5   H N N 266 
NAG H61  H N N 267 
NAG H62  H N N 268 
NAG H81  H N N 269 
NAG H82  H N N 270 
NAG H83  H N N 271 
NAG HN2  H N N 272 
NAG HO1  H N N 273 
NAG HO3  H N N 274 
NAG HO4  H N N 275 
NAG HO6  H N N 276 
PHE N    N N N 277 
PHE CA   C N S 278 
PHE C    C N N 279 
PHE O    O N N 280 
PHE CB   C N N 281 
PHE CG   C Y N 282 
PHE CD1  C Y N 283 
PHE CD2  C Y N 284 
PHE CE1  C Y N 285 
PHE CE2  C Y N 286 
PHE CZ   C Y N 287 
PHE OXT  O N N 288 
PHE H    H N N 289 
PHE H2   H N N 290 
PHE HA   H N N 291 
PHE HB2  H N N 292 
PHE HB3  H N N 293 
PHE HD1  H N N 294 
PHE HD2  H N N 295 
PHE HE1  H N N 296 
PHE HE2  H N N 297 
PHE HZ   H N N 298 
PHE HXT  H N N 299 
PRO N    N N N 300 
PRO CA   C N S 301 
PRO C    C N N 302 
PRO O    O N N 303 
PRO CB   C N N 304 
PRO CG   C N N 305 
PRO CD   C N N 306 
PRO OXT  O N N 307 
PRO H    H N N 308 
PRO HA   H N N 309 
PRO HB2  H N N 310 
PRO HB3  H N N 311 
PRO HG2  H N N 312 
PRO HG3  H N N 313 
PRO HD2  H N N 314 
PRO HD3  H N N 315 
PRO HXT  H N N 316 
SER N    N N N 317 
SER CA   C N S 318 
SER C    C N N 319 
SER O    O N N 320 
SER CB   C N N 321 
SER OG   O N N 322 
SER OXT  O N N 323 
SER H    H N N 324 
SER H2   H N N 325 
SER HA   H N N 326 
SER HB2  H N N 327 
SER HB3  H N N 328 
SER HG   H N N 329 
SER HXT  H N N 330 
THR N    N N N 331 
THR CA   C N S 332 
THR C    C N N 333 
THR O    O N N 334 
THR CB   C N R 335 
THR OG1  O N N 336 
THR CG2  C N N 337 
THR OXT  O N N 338 
THR H    H N N 339 
THR H2   H N N 340 
THR HA   H N N 341 
THR HB   H N N 342 
THR HG1  H N N 343 
THR HG21 H N N 344 
THR HG22 H N N 345 
THR HG23 H N N 346 
THR HXT  H N N 347 
TRP N    N N N 348 
TRP CA   C N S 349 
TRP C    C N N 350 
TRP O    O N N 351 
TRP CB   C N N 352 
TRP CG   C Y N 353 
TRP CD1  C Y N 354 
TRP CD2  C Y N 355 
TRP NE1  N Y N 356 
TRP CE2  C Y N 357 
TRP CE3  C Y N 358 
TRP CZ2  C Y N 359 
TRP CZ3  C Y N 360 
TRP CH2  C Y N 361 
TRP OXT  O N N 362 
TRP H    H N N 363 
TRP H2   H N N 364 
TRP HA   H N N 365 
TRP HB2  H N N 366 
TRP HB3  H N N 367 
TRP HD1  H N N 368 
TRP HE1  H N N 369 
TRP HE3  H N N 370 
TRP HZ2  H N N 371 
TRP HZ3  H N N 372 
TRP HH2  H N N 373 
TRP HXT  H N N 374 
TYR N    N N N 375 
TYR CA   C N S 376 
TYR C    C N N 377 
TYR O    O N N 378 
TYR CB   C N N 379 
TYR CG   C Y N 380 
TYR CD1  C Y N 381 
TYR CD2  C Y N 382 
TYR CE1  C Y N 383 
TYR CE2  C Y N 384 
TYR CZ   C Y N 385 
TYR OH   O N N 386 
TYR OXT  O N N 387 
TYR H    H N N 388 
TYR H2   H N N 389 
TYR HA   H N N 390 
TYR HB2  H N N 391 
TYR HB3  H N N 392 
TYR HD1  H N N 393 
TYR HD2  H N N 394 
TYR HE1  H N N 395 
TYR HE2  H N N 396 
TYR HH   H N N 397 
TYR HXT  H N N 398 
VAL N    N N N 399 
VAL CA   C N S 400 
VAL C    C N N 401 
VAL O    O N N 402 
VAL CB   C N N 403 
VAL CG1  C N N 404 
VAL CG2  C N N 405 
VAL OXT  O N N 406 
VAL H    H N N 407 
VAL H2   H N N 408 
VAL HA   H N N 409 
VAL HB   H N N 410 
VAL HG11 H N N 411 
VAL HG12 H N N 412 
VAL HG13 H N N 413 
VAL HG21 H N N 414 
VAL HG22 H N N 415 
VAL HG23 H N N 416 
VAL HXT  H N N 417 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
NAG C1  C2   sing N N 235 
NAG C1  O1   sing N N 236 
NAG C1  O5   sing N N 237 
NAG C1  H1   sing N N 238 
NAG C2  C3   sing N N 239 
NAG C2  N2   sing N N 240 
NAG C2  H2   sing N N 241 
NAG C3  C4   sing N N 242 
NAG C3  O3   sing N N 243 
NAG C3  H3   sing N N 244 
NAG C4  C5   sing N N 245 
NAG C4  O4   sing N N 246 
NAG C4  H4   sing N N 247 
NAG C5  C6   sing N N 248 
NAG C5  O5   sing N N 249 
NAG C5  H5   sing N N 250 
NAG C6  O6   sing N N 251 
NAG C6  H61  sing N N 252 
NAG C6  H62  sing N N 253 
NAG C7  C8   sing N N 254 
NAG C7  N2   sing N N 255 
NAG C7  O7   doub N N 256 
NAG C8  H81  sing N N 257 
NAG C8  H82  sing N N 258 
NAG C8  H83  sing N N 259 
NAG N2  HN2  sing N N 260 
NAG O1  HO1  sing N N 261 
NAG O3  HO3  sing N N 262 
NAG O4  HO4  sing N N 263 
NAG O6  HO6  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Agency for Medical Research and Development (AMED)' Japan 'JP21fk0108462, JP21fk0108585, JP21ae0121028, JP18ae0101046' 1 
'Japan Society for the Promotion of Science (JSPS)'        Japan 20H00451                                                     2 
# 
_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   7jzu 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 31' 
_space_group.name_Hall        'P 31' 
_space_group.IT_number        144 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YDT 
_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]   0.013641 
_atom_sites.fract_transf_matrix[1][2]   0.007876 
_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]   0.015752 
_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]   0.010020 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP A 1 1   ? 15.40900 -6.46700  15.36100  1.000 117.43000 ? 1   ASP A N   1 
ATOM   2    C CA  . ASP A 1 1   ? 15.80700 -5.05700  15.30700  1.000 119.29000 ? 1   ASP A CA  1 
ATOM   3    C C   . ASP A 1 1   ? 17.29500 -4.90500  14.95300  1.000 115.14000 ? 1   ASP A C   1 
ATOM   4    O O   . ASP A 1 1   ? 17.66100 -4.67300  13.79400  1.000 113.89000 ? 1   ASP A O   1 
ATOM   5    C CB  . ASP A 1 1   ? 15.51400 -4.36500  16.64800  1.000 119.61000 ? 1   ASP A CB  1 
ATOM   6    C CG  . ASP A 1 1   ? 14.93200 -2.95800  16.47700  1.000 121.17000 ? 1   ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 1   ? 14.43500 -2.63900  15.37000  1.000 118.82000 ? 1   ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 1   ? 14.98400 -2.16900  17.45400  1.000 120.65000 ? 1   ASP A OD2 1 
ATOM   9    N N   . LYS A 1 2   ? 18.15500 -5.03100  15.96100  1.000 110.83000 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 19.59200 -4.94200  15.74400  1.000 106.36000 ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 20.20000 -6.25900  15.23200  1.000 103.00000 ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 21.42500 -6.31400  15.06800  1.000 99.33000  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 20.28100 -4.49500  17.04300  1.000 105.15000 ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 19.52100 -3.42600  17.83600  1.000 102.22000 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 20.24700 -3.01200  19.10600  1.000 92.51000  ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 20.27700 -4.11400  20.17000  1.000 91.31000  ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 20.63000 -3.58300  21.54100  1.000 86.12000  ? 2   LYS A NZ  1 
ATOM   18   N N   . GLU A 1 3   ? 19.36700 -7.27800  14.94600  1.000 104.16000 ? 3   GLU A N   1 
ATOM   19   C CA  . GLU A 1 3   ? 19.83900 -8.64500  14.68400  1.000 99.65000  ? 3   GLU A CA  1 
ATOM   20   C C   . GLU A 1 3   ? 20.96000 -8.65500  13.64900  1.000 93.87000  ? 3   GLU A C   1 
ATOM   21   O O   . GLU A 1 3   ? 22.00000 -9.29300  13.83700  1.000 89.02000  ? 3   GLU A O   1 
ATOM   22   C CB  . GLU A 1 3   ? 18.66900 -9.54900  14.22400  1.000 100.19000 ? 3   GLU A CB  1 
ATOM   23   C CG  . GLU A 1 3   ? 17.55400 -9.88000  15.28200  1.000 101.95000 ? 3   GLU A CG  1 
ATOM   24   C CD  . GLU A 1 3   ? 16.46700 -10.88100 14.78700  1.000 103.62000 ? 3   GLU A CD  1 
ATOM   25   O OE1 . GLU A 1 3   ? 16.63200 -11.48300 13.70100  1.000 99.33000  ? 3   GLU A OE1 1 
ATOM   26   O OE2 . GLU A 1 3   ? 15.43900 -11.07000 15.49100  1.000 97.49000  ? 3   GLU A OE2 1 
ATOM   27   N N   . TRP A 1 4   ? 20.76200 -7.92800  12.55500  1.000 100.09000 ? 4   TRP A N   1 
ATOM   28   C CA  . TRP A 1 4   ? 21.75200 -7.88700  11.48800  1.000 95.90000  ? 4   TRP A CA  1 
ATOM   29   C C   . TRP A 1 4   ? 22.99300 -7.11400  11.91500  1.000 92.17000  ? 4   TRP A C   1 
ATOM   30   O O   . TRP A 1 4   ? 24.12000 -7.57900  11.70900  1.000 91.15000  ? 4   TRP A O   1 
ATOM   31   C CB  . TRP A 1 4   ? 21.10900 -7.27100  10.24400  1.000 102.21000 ? 4   TRP A CB  1 
ATOM   32   C CG  . TRP A 1 4   ? 22.01600 -6.91500  9.11700   1.000 104.90000 ? 4   TRP A CG  1 
ATOM   33   C CD1 . TRP A 1 4   ? 22.59900 -5.70000  8.88400   1.000 102.80000 ? 4   TRP A CD1 1 
ATOM   34   C CD2 . TRP A 1 4   ? 22.39700 -7.76400  8.02100   1.000 108.67000 ? 4   TRP A CD2 1 
ATOM   35   N NE1 . TRP A 1 4   ? 23.33700 -5.74800  7.71800   1.000 108.99000 ? 4   TRP A NE1 1 
ATOM   36   C CE2 . TRP A 1 4   ? 23.23300 -7.00300  7.17400   1.000 108.52000 ? 4   TRP A CE2 1 
ATOM   37   C CE3 . TRP A 1 4   ? 22.12100 -9.09700  7.68200   1.000 108.82000 ? 4   TRP A CE3 1 
ATOM   38   C CZ2 . TRP A 1 4   ? 23.80100 -7.53300  6.00900   1.000 113.04000 ? 4   TRP A CZ2 1 
ATOM   39   C CZ3 . TRP A 1 4   ? 22.68700 -9.62400  6.52200   1.000 117.17000 ? 4   TRP A CZ3 1 
ATOM   40   C CH2 . TRP A 1 4   ? 23.51500 -8.84200  5.70000   1.000 116.77000 ? 4   TRP A CH2 1 
ATOM   41   N N   . ILE A 1 5   ? 22.80500 -5.94500  12.53300  1.000 85.49000  ? 5   ILE A N   1 
ATOM   42   C CA  . ILE A 1 5   ? 23.93200 -5.05900  12.81100  1.000 83.76000  ? 5   ILE A CA  1 
ATOM   43   C C   . ILE A 1 5   ? 24.94100 -5.75100  13.70900  1.000 85.47000  ? 5   ILE A C   1 
ATOM   44   O O   . ILE A 1 5   ? 26.15300 -5.70100  13.46300  1.000 87.39000  ? 5   ILE A O   1 
ATOM   45   C CB  . ILE A 1 5   ? 23.45600 -3.74500  13.44400  1.000 85.95000  ? 5   ILE A CB  1 
ATOM   46   C CG1 . ILE A 1 5   ? 22.41500 -3.05900  12.57000  1.000 93.74000  ? 5   ILE A CG1 1 
ATOM   47   C CG2 . ILE A 1 5   ? 24.64200 -2.86200  13.70400  1.000 85.40000  ? 5   ILE A CG2 1 
ATOM   48   C CD1 . ILE A 1 5   ? 20.99300 -3.50400  12.85100  1.000 99.23000  ? 5   ILE A CD1 1 
ATOM   49   N N   . LEU A 1 6   ? 24.46000 -6.38500  14.78100  1.000 88.26000  ? 6   LEU A N   1 
ATOM   50   C CA  . LEU A 1 6   ? 25.34500 -7.10700  15.67900  1.000 83.64000  ? 6   LEU A CA  1 
ATOM   51   C C   . LEU A 1 6   ? 26.24400 -8.05900  14.90400  1.000 80.29000  ? 6   LEU A C   1 
ATOM   52   O O   . LEU A 1 6   ? 27.47100 -7.94300  14.94900  1.000 82.46000  ? 6   LEU A O   1 
ATOM   53   C CB  . LEU A 1 6   ? 24.53200 -7.87300  16.72000  1.000 87.45000  ? 6   LEU A CB  1 
ATOM   54   C CG  . LEU A 1 6   ? 25.32400 -8.50000  17.87500  1.000 83.15000  ? 6   LEU A CG  1 
ATOM   55   C CD1 . LEU A 1 6   ? 25.81400 -7.42600  18.82500  1.000 80.47000  ? 6   LEU A CD1 1 
ATOM   56   C CD2 . LEU A 1 6   ? 24.49600 -9.52900  18.63800  1.000 81.62000  ? 6   LEU A CD2 1 
ATOM   57   N N   . GLN A 1 7   ? 25.64600 -9.00800  14.18400  1.000 79.42000  ? 7   GLN A N   1 
ATOM   58   C CA  . GLN A 1 7   ? 26.45500 -9.96600  13.44000  1.000 82.26000  ? 7   GLN A CA  1 
ATOM   59   C C   . GLN A 1 7   ? 27.57900 -9.26600  12.69300  1.000 84.79000  ? 7   GLN A C   1 
ATOM   60   O O   . GLN A 1 7   ? 28.75400 -9.63500  12.82600  1.000 85.94000  ? 7   GLN A O   1 
ATOM   61   C CB  . GLN A 1 7   ? 25.60400 -10.76000 12.46500  1.000 77.40000  ? 7   GLN A CB  1 
ATOM   62   C CG  . GLN A 1 7   ? 26.45500 -11.73400 11.69300  1.000 80.95000  ? 7   GLN A CG  1 
ATOM   63   C CD  . GLN A 1 7   ? 27.01500 -12.81100 12.57700  1.000 80.42000  ? 7   GLN A CD  1 
ATOM   64   O OE1 . GLN A 1 7   ? 26.28000 -13.46700 13.30900  1.000 83.90000  ? 7   GLN A OE1 1 
ATOM   65   N NE2 . GLN A 1 7   ? 28.31600 -12.99800 12.53100  1.000 79.04000  ? 7   GLN A NE2 1 
ATOM   66   N N   . LYS A 1 8   ? 27.24300 -8.19300  11.96800  1.000 82.14000  ? 8   LYS A N   1 
ATOM   67   C CA  . LYS A 1 8   ? 28.24200 -7.49800  11.16500  1.000 80.68000  ? 8   LYS A CA  1 
ATOM   68   C C   . LYS A 1 8   ? 29.29200 -6.82800  12.03900  1.000 80.17000  ? 8   LYS A C   1 
ATOM   69   O O   . LYS A 1 8   ? 30.47600 -6.80000  11.68200  1.000 78.01000  ? 8   LYS A O   1 
ATOM   70   C CB  . LYS A 1 8   ? 27.56100 -6.48500  10.24600  1.000 88.22000  ? 8   LYS A CB  1 
ATOM   71   C CG  . LYS A 1 8   ? 26.67800 -7.13200  9.17200   1.000 89.59000  ? 8   LYS A CG  1 
ATOM   72   C CD  . LYS A 1 8   ? 27.50300 -7.63800  7.98100   1.000 92.43000  ? 8   LYS A CD  1 
ATOM   73   C CE  . LYS A 1 8   ? 27.72500 -9.15300  7.99900   1.000 91.29000  ? 8   LYS A CE  1 
ATOM   74   N NZ  . LYS A 1 8   ? 28.62400 -9.61500  6.89000   1.000 92.01000  ? 8   LYS A NZ  1 
ATOM   75   N N   . ILE A 1 9   ? 28.89300 -6.30400  13.19700  1.000 83.30000  ? 9   ILE A N   1 
ATOM   76   C CA  . ILE A 1 9   ? 29.89300 -5.74300  14.10600  1.000 81.38000  ? 9   ILE A CA  1 
ATOM   77   C C   . ILE A 1 9   ? 30.78100 -6.84000  14.66300  1.000 75.71000  ? 9   ILE A C   1 
ATOM   78   O O   . ILE A 1 9   ? 32.00900 -6.69100  14.73300  1.000 77.06000  ? 9   ILE A O   1 
ATOM   79   C CB  . ILE A 1 9   ? 29.22800 -4.96100  15.24100  1.000 78.99000  ? 9   ILE A CB  1 
ATOM   80   C CG1 . ILE A 1 9   ? 28.37100 -3.84600  14.67300  1.000 83.01000  ? 9   ILE A CG1 1 
ATOM   81   C CG2 . ILE A 1 9   ? 30.29400 -4.39200  16.13700  1.000 79.90000  ? 9   ILE A CG2 1 
ATOM   82   C CD1 . ILE A 1 9   ? 27.66900 -3.04200  15.74300  1.000 86.26000  ? 9   ILE A CD1 1 
ATOM   83   N N   . TYR A 1 10  ? 30.17600 -7.93900  15.10100  1.000 74.46000  ? 10  TYR A N   1 
ATOM   84   C CA  . TYR A 1 10  ? 30.97200 -9.06900  15.55000  1.000 78.62000  ? 10  TYR A CA  1 
ATOM   85   C C   . TYR A 1 10  ? 31.98500 -9.44300  14.48000  1.000 77.46000  ? 10  TYR A C   1 
ATOM   86   O O   . TYR A 1 10  ? 33.19000 -9.49300  14.74700  1.000 78.96000  ? 10  TYR A O   1 
ATOM   87   C CB  . TYR A 1 10  ? 30.05600 -10.24500 15.90500  1.000 80.79000  ? 10  TYR A CB  1 
ATOM   88   C CG  . TYR A 1 10  ? 30.78000 -11.50400 16.33500  1.000 75.13000  ? 10  TYR A CG  1 
ATOM   89   C CD1 . TYR A 1 10  ? 31.41800 -11.58000 17.57100  1.000 80.63000  ? 10  TYR A CD1 1 
ATOM   90   C CD2 . TYR A 1 10  ? 30.81200 -12.62000 15.50900  1.000 78.97000  ? 10  TYR A CD2 1 
ATOM   91   C CE1 . TYR A 1 10  ? 32.08000 -12.72600 17.95800  1.000 82.11000  ? 10  TYR A CE1 1 
ATOM   92   C CE2 . TYR A 1 10  ? 31.47200 -13.76300 15.88500  1.000 81.83000  ? 10  TYR A CE2 1 
ATOM   93   C CZ  . TYR A 1 10  ? 32.10600 -13.81100 17.10800  1.000 75.37000  ? 10  TYR A CZ  1 
ATOM   94   O OH  . TYR A 1 10  ? 32.76000 -14.95700 17.47400  1.000 72.97000  ? 10  TYR A OH  1 
ATOM   95   N N   . GLU A 1 11  ? 31.51500 -9.61400  13.23900  1.000 82.38000  ? 11  GLU A N   1 
ATOM   96   C CA  . GLU A 1 11  ? 32.39000 -10.02900 12.14000  1.000 76.29000  ? 11  GLU A CA  1 
ATOM   97   C C   . GLU A 1 11  ? 33.56300 -9.08200  11.95300  1.000 73.00000  ? 11  GLU A C   1 
ATOM   98   O O   . GLU A 1 11  ? 34.67400 -9.52000  11.63200  1.000 76.83000  ? 11  GLU A O   1 
ATOM   99   C CB  . GLU A 1 11  ? 31.58700 -10.14500 10.84500  1.000 78.09000  ? 11  GLU A CB  1 
ATOM   100  C CG  . GLU A 1 11  ? 30.67000 -11.34800 10.85800  1.000 78.88000  ? 11  GLU A CG  1 
ATOM   101  C CD  . GLU A 1 11  ? 30.05600 -11.67000 9.52200   1.000 88.10000  ? 11  GLU A CD  1 
ATOM   102  O OE1 . GLU A 1 11  ? 30.33300 -10.96800 8.52200   1.000 94.86000  ? 11  GLU A OE1 1 
ATOM   103  O OE2 . GLU A 1 11  ? 29.28700 -12.65100 9.46900   1.000 89.38000  ? 11  GLU A OE2 1 
ATOM   104  N N   . ILE A 1 12  ? 33.34500 -7.78600  12.16500  1.000 71.32000  ? 12  ILE A N   1 
ATOM   105  C CA  . ILE A 1 12  ? 34.44300 -6.83400  12.05700  1.000 69.87000  ? 12  ILE A CA  1 
ATOM   106  C C   . ILE A 1 12  ? 35.57900 -7.22500  12.97800  1.000 75.31000  ? 12  ILE A C   1 
ATOM   107  O O   . ILE A 1 12  ? 36.69600 -7.50000  12.52100  1.000 80.30000  ? 12  ILE A O   1 
ATOM   108  C CB  . ILE A 1 12  ? 33.96000 -5.41300  12.35900  1.000 73.12000  ? 12  ILE A CB  1 
ATOM   109  C CG1 . ILE A 1 12  ? 32.99400 -4.96900  11.27400  1.000 80.94000  ? 12  ILE A CG1 1 
ATOM   110  C CG2 . ILE A 1 12  ? 35.14400 -4.46100  12.46000  1.000 67.14000  ? 12  ILE A CG2 1 
ATOM   111  C CD1 . ILE A 1 12  ? 32.75600 -3.50800  11.26700  1.000 78.41000  ? 12  ILE A CD1 1 
ATOM   112  N N   . MET A 1 13  ? 35.31900 -7.24000  14.29700  1.000 77.32000  ? 13  MET A N   1 
ATOM   113  C CA  . MET A 1 13  ? 36.40700 -7.50300  15.22900  1.000 74.75000  ? 13  MET A CA  1 
ATOM   114  C C   . MET A 1 13  ? 37.01900 -8.87700  14.99200  1.000 74.90000  ? 13  MET A C   1 
ATOM   115  O O   . MET A 1 13  ? 38.23900 -9.03000  15.08300  1.000 80.32000  ? 13  MET A O   1 
ATOM   116  C CB  . MET A 1 13  ? 35.94600 -7.36900  16.68400  1.000 82.67000  ? 13  MET A CB  1 
ATOM   117  C CG  . MET A 1 13  ? 35.23600 -8.57400  17.21700  1.000 83.16000  ? 13  MET A CG  1 
ATOM   118  S SD  . MET A 1 13  ? 35.22500 -8.75100  18.99900  1.000 71.08000  ? 13  MET A SD  1 
ATOM   119  C CE  . MET A 1 13  ? 34.08800 -10.11500 19.05300  1.000 76.69000  ? 13  MET A CE  1 
ATOM   120  N N   . ARG A 1 14  ? 36.20800 -9.88600  14.66000  1.000 75.43000  ? 14  ARG A N   1 
ATOM   121  C CA  . ARG A 1 14  ? 36.80500 -11.17300 14.30200  1.000 82.32000  ? 14  ARG A CA  1 
ATOM   122  C C   . ARG A 1 14  ? 37.77100 -11.01300 13.13400  1.000 86.04000  ? 14  ARG A C   1 
ATOM   123  O O   . ARG A 1 14  ? 38.89100 -11.53500 13.17800  1.000 87.53000  ? 14  ARG A O   1 
ATOM   124  C CB  . ARG A 1 14  ? 35.74100 -12.22900 13.97500  1.000 79.47000  ? 14  ARG A CB  1 
ATOM   125  C CG  . ARG A 1 14  ? 35.13000 -12.98100 15.20700  1.000 92.27000  ? 14  ARG A CG  1 
ATOM   126  C CD  . ARG A 1 14  ? 36.15300 -13.42300 16.29700  1.000 84.09000  ? 14  ARG A CD  1 
ATOM   127  N NE  . ARG A 1 14  ? 36.89300 -14.63700 15.94000  1.000 94.43000  ? 14  ARG A NE  1 
ATOM   128  C CZ  . ARG A 1 14  ? 38.21700 -14.69500 15.79000  1.000 99.20000  ? 14  ARG A CZ  1 
ATOM   129  N NH1 . ARG A 1 14  ? 38.96300 -13.61200 15.98400  1.000 97.70000  ? 14  ARG A NH1 1 
ATOM   130  N NH2 . ARG A 1 14  ? 38.80400 -15.84100 15.46600  1.000 102.34000 ? 14  ARG A NH2 1 
ATOM   131  N N   . ARG A 1 15  ? 37.37000 -10.24800 12.12800  1.000 79.49000  ? 15  ARG A N   1 
ATOM   132  C CA  . ARG A 1 15  ? 38.23500 -10.08100 10.93900  1.000 81.26000  ? 15  ARG A CA  1 
ATOM   133  C C   . ARG A 1 15  ? 39.47700 -9.29200  11.34900  1.000 83.26000  ? 15  ARG A C   1 
ATOM   134  O O   . ARG A 1 15  ? 40.59000 -9.72300  11.02400  1.000 83.21000  ? 15  ARG A O   1 
ATOM   135  C CB  . ARG A 1 15  ? 37.45800 -9.38000  9.82600   1.000 83.70000  ? 15  ARG A CB  1 
ATOM   136  C CG  . ARG A 1 15  ? 36.80100 -10.33000 8.83700   1.000 86.34000  ? 15  ARG A CG  1 
ATOM   137  C CD  . ARG A 1 15  ? 35.86600 -11.30700 9.51900   1.000 92.45000  ? 15  ARG A CD  1 
ATOM   138  N NE  . ARG A 1 15  ? 36.46200 -12.62400 9.67100   1.000 95.92000  ? 15  ARG A NE  1 
ATOM   139  C CZ  . ARG A 1 15  ? 35.91900 -13.74300 9.21300   1.000 102.21000 ? 15  ARG A CZ  1 
ATOM   140  N NH1 . ARG A 1 15  ? 34.76200 -13.70200 8.57600   1.000 109.12000 ? 15  ARG A NH1 1 
ATOM   141  N NH2 . ARG A 1 15  ? 36.53200 -14.89800 9.39100   1.000 101.40000 ? 15  ARG A NH2 1 
ATOM   142  N N   . LEU A 1 16  ? 39.28200 -8.18200  12.04600  1.000 75.73000  ? 16  LEU A N   1 
ATOM   143  C CA  . LEU A 1 16  ? 40.41200 -7.36900  12.47400  1.000 76.80000  ? 16  LEU A CA  1 
ATOM   144  C C   . LEU A 1 16  ? 41.46500 -8.19600  13.21600  1.000 83.08000  ? 16  LEU A C   1 
ATOM   145  O O   . LEU A 1 16  ? 42.67100 -8.03000  12.98400  1.000 79.81000  ? 16  LEU A O   1 
ATOM   146  C CB  . LEU A 1 16  ? 39.91000 -6.23800  13.35200  1.000 75.31000  ? 16  LEU A CB  1 
ATOM   147  C CG  . LEU A 1 16  ? 39.06600 -5.21400  12.64500  1.000 78.76000  ? 16  LEU A CG  1 
ATOM   148  C CD1 . LEU A 1 16  ? 38.50700 -4.23500  13.64900  1.000 74.67000  ? 16  LEU A CD1 1 
ATOM   149  C CD2 . LEU A 1 16  ? 39.96100 -4.51700  11.67500  1.000 82.39000  ? 16  LEU A CD2 1 
ATOM   150  N N   . ASP A 1 17  ? 41.03000 -9.07400  14.13500  1.000 85.05000  ? 17  ASP A N   1 
ATOM   151  C CA  . ASP A 1 17  ? 41.97300 -9.93400  14.85600  1.000 81.59000  ? 17  ASP A CA  1 
ATOM   152  C C   . ASP A 1 17  ? 42.76100 -10.79600 13.88300  1.000 82.33000  ? 17  ASP A C   1 
ATOM   153  O O   . ASP A 1 17  ? 43.99100 -10.88300 13.96600  1.000 74.82000  ? 17  ASP A O   1 
ATOM   154  C CB  . ASP A 1 17  ? 41.22100 -10.80900 15.86100  1.000 85.05000  ? 17  ASP A CB  1 
ATOM   155  C CG  . ASP A 1 17  ? 42.14100 -11.44600 16.91600  1.000 89.20000  ? 17  ASP A CG  1 
ATOM   156  O OD1 . ASP A 1 17  ? 43.08300 -12.18100 16.54900  1.000 91.10000  ? 17  ASP A OD1 1 
ATOM   157  O OD2 . ASP A 1 17  ? 41.91200 -11.22200 18.12900  1.000 92.68000  ? 17  ASP A OD2 1 
ATOM   158  N N   . GLU A 1 18  ? 42.05500 -11.43400 12.94300  1.000 84.83000  ? 18  GLU A N   1 
ATOM   159  C CA  . GLU A 1 18  ? 42.68800 -12.21100 11.87900  1.000 79.00000  ? 18  GLU A CA  1 
ATOM   160  C C   . GLU A 1 18  ? 43.71700 -11.39700 11.10700  1.000 81.84000  ? 18  GLU A C   1 
ATOM   161  O O   . GLU A 1 18  ? 44.74900 -11.92800 10.69500  1.000 83.67000  ? 18  GLU A O   1 
ATOM   162  C CB  . GLU A 1 18  ? 41.61700 -12.73500 10.91900  1.000 82.05000  ? 18  GLU A CB  1 
ATOM   163  C CG  . GLU A 1 18  ? 40.62300 -13.68500 11.54300  1.000 83.46000  ? 18  GLU A CG  1 
ATOM   164  C CD  . GLU A 1 18  ? 39.32100 -13.77100 10.76400  1.000 90.10000  ? 18  GLU A CD  1 
ATOM   165  O OE1 . GLU A 1 18  ? 39.13700 -13.00400 9.79100   1.000 92.52000  ? 18  GLU A OE1 1 
ATOM   166  O OE2 . GLU A 1 18  ? 38.47100 -14.60900 11.13600  1.000 94.05000  ? 18  GLU A OE2 1 
ATOM   167  N N   . GLU A 1 19  ? 43.45700 -10.12200 10.89200  1.000 82.17000  ? 19  GLU A N   1 
ATOM   168  C CA  . GLU A 1 19  ? 44.40900 -9.27100  10.20100  1.000 76.99000  ? 19  GLU A CA  1 
ATOM   169  C C   . GLU A 1 19  ? 45.48500 -8.70500  11.11700  1.000 82.57000  ? 19  GLU A C   1 
ATOM   170  O O   . GLU A 1 19  ? 46.37800 -8.00500  10.63100  1.000 88.46000  ? 19  GLU A O   1 
ATOM   171  C CB  . GLU A 1 19  ? 43.66600 -8.14100  9.50300   1.000 82.55000  ? 19  GLU A CB  1 
ATOM   172  C CG  . GLU A 1 19  ? 42.70900 -8.66200  8.43600   1.000 89.13000  ? 19  GLU A CG  1 
ATOM   173  C CD  . GLU A 1 19  ? 41.98200 -7.54500  7.71300   1.000 100.07000 ? 19  GLU A CD  1 
ATOM   174  O OE1 . GLU A 1 19  ? 42.45500 -6.38400  7.77300   1.000 96.38000  ? 19  GLU A OE1 1 
ATOM   175  O OE2 . GLU A 1 19  ? 40.93600 -7.82900  7.08500   1.000 101.26000 ? 19  GLU A OE2 1 
ATOM   176  N N   . GLY A 1 20  ? 45.42800 -8.98300  12.42100  1.000 85.43000  ? 20  GLY A N   1 
ATOM   177  C CA  . GLY A 1 20  ? 46.47800 -8.60600  13.33800  1.000 81.41000  ? 20  GLY A CA  1 
ATOM   178  C C   . GLY A 1 20  ? 46.15600 -7.43700  14.25100  1.000 83.27000  ? 20  GLY A C   1 
ATOM   179  O O   . GLY A 1 20  ? 46.74700 -7.33100  15.33700  1.000 89.20000  ? 20  GLY A O   1 
ATOM   180  N N   . HIS A 1 21  ? 45.23400 -6.56600  13.85400  1.000 82.14000  ? 21  HIS A N   1 
ATOM   181  C CA  . HIS A 1 21  ? 44.95500 -5.34800  14.60700  1.000 82.82000  ? 21  HIS A CA  1 
ATOM   182  C C   . HIS A 1 21  ? 44.22200 -5.71200  15.89700  1.000 83.13000  ? 21  HIS A C   1 
ATOM   183  O O   . HIS A 1 21  ? 42.99300 -5.68000  15.99400  1.000 85.78000  ? 21  HIS A O   1 
ATOM   184  C CB  . HIS A 1 21  ? 44.16500 -4.38100  13.73700  1.000 90.11000  ? 21  HIS A CB  1 
ATOM   185  C CG  . HIS A 1 21  ? 44.88900 -3.98600  12.48700  1.000 88.94000  ? 21  HIS A CG  1 
ATOM   186  N ND1 . HIS A 1 21  ? 44.31300 -4.03600  11.23700  1.000 86.12000  ? 21  HIS A ND1 1 
ATOM   187  C CD2 . HIS A 1 21  ? 46.15900 -3.55300  12.30100  1.000 91.59000  ? 21  HIS A CD2 1 
ATOM   188  C CE1 . HIS A 1 21  ? 45.20100 -3.65400  10.33600  1.000 97.13000  ? 21  HIS A CE1 1 
ATOM   189  N NE2 . HIS A 1 21  ? 46.32700 -3.34800  10.95600  1.000 100.09000 ? 21  HIS A NE2 1 
ATOM   190  N N   . GLY A 1 22  ? 45.00800 -6.06300  16.91300  1.000 83.30000  ? 22  GLY A N   1 
ATOM   191  C CA  . GLY A 1 22  ? 44.47700 -6.57600  18.15900  1.000 78.02000  ? 22  GLY A CA  1 
ATOM   192  C C   . GLY A 1 22  ? 43.83100 -5.50900  19.00600  1.000 78.04000  ? 22  GLY A C   1 
ATOM   193  O O   . GLY A 1 22  ? 42.71000 -5.69100  19.48500  1.000 77.87000  ? 22  GLY A O   1 
ATOM   194  N N   . GLU A 1 23  ? 44.52800 -4.39300  19.21000  1.000 73.52000  ? 23  GLU A N   1 
ATOM   195  C CA  . GLU A 1 23  ? 43.92200 -3.28500  19.93100  1.000 71.14000  ? 23  GLU A CA  1 
ATOM   196  C C   . GLU A 1 23  ? 42.60100 -2.87600  19.31700  1.000 73.27000  ? 23  GLU A C   1 
ATOM   197  O O   . GLU A 1 23  ? 41.65100 -2.55700  20.03600  1.000 77.47000  ? 23  GLU A O   1 
ATOM   198  C CB  . GLU A 1 23  ? 44.87100 -2.10700  19.96100  1.000 71.71000  ? 23  GLU A CB  1 
ATOM   199  C CG  . GLU A 1 23  ? 46.18500 -2.50000  20.51700  1.000 79.68000  ? 23  GLU A CG  1 
ATOM   200  C CD  . GLU A 1 23  ? 47.24900 -1.50300  20.21900  1.000 86.18000  ? 23  GLU A CD  1 
ATOM   201  O OE1 . GLU A 1 23  ? 47.41000 -0.56000  21.04000  1.000 75.79000  ? 23  GLU A OE1 1 
ATOM   202  O OE2 . GLU A 1 23  ? 47.90300 -1.67800  19.15600  1.000 94.13000  ? 23  GLU A OE2 1 
ATOM   203  N N   . ALA A 1 24  ? 42.51300 -2.89500  17.98800  1.000 69.53000  ? 24  ALA A N   1 
ATOM   204  C CA  . ALA A 1 24  ? 41.26400 -2.51300  17.35100  1.000 71.19000  ? 24  ALA A CA  1 
ATOM   205  C C   . ALA A 1 24  ? 40.21100 -3.60500  17.49900  1.000 67.99000  ? 24  ALA A C   1 
ATOM   206  O O   . ALA A 1 24  ? 39.02100 -3.30700  17.64100  1.000 69.07000  ? 24  ALA A O   1 
ATOM   207  C CB  . ALA A 1 24  ? 41.50600 -2.18200  15.87700  1.000 83.27000  ? 24  ALA A CB  1 
ATOM   208  N N   . SER A 1 25  ? 40.61800 -4.87700  17.45000  1.000 71.52000  ? 25  SER A N   1 
ATOM   209  C CA  . SER A 1 25  ? 39.67400 -5.95300  17.75500  1.000 74.90000  ? 25  SER A CA  1 
ATOM   210  C C   . SER A 1 25  ? 39.14600 -5.83200  19.17700  1.000 76.06000  ? 25  SER A C   1 
ATOM   211  O O   . SER A 1 25  ? 37.95900 -6.07100  19.43300  1.000 77.46000  ? 25  SER A O   1 
ATOM   212  C CB  . SER A 1 25  ? 40.32800 -7.31900  17.54900  1.000 79.00000  ? 25  SER A CB  1 
ATOM   213  O OG  . SER A 1 25  ? 40.26400 -7.69400  16.17800  1.000 83.46000  ? 25  SER A OG  1 
ATOM   214  N N   . LEU A 1 26  ? 40.00700 -5.42400  20.10900  1.000 71.87000  ? 26  LEU A N   1 
ATOM   215  C CA  . LEU A 1 26  ? 39.57700 -5.30000  21.49400  1.000 76.66000  ? 26  LEU A CA  1 
ATOM   216  C C   . LEU A 1 26  ? 38.70900 -4.07000  21.69800  1.000 78.50000  ? 26  LEU A C   1 
ATOM   217  O O   . LEU A 1 26  ? 37.81700 -4.08400  22.55600  1.000 80.95000  ? 26  LEU A O   1 
ATOM   218  C CB  . LEU A 1 26  ? 40.77900 -5.26500  22.43800  1.000 75.91000  ? 26  LEU A CB  1 
ATOM   219  C CG  . LEU A 1 26  ? 41.47100 -6.60100  22.70800  1.000 70.32000  ? 26  LEU A CG  1 
ATOM   220  C CD1 . LEU A 1 26  ? 42.66400 -6.39200  23.63300  1.000 75.74000  ? 26  LEU A CD1 1 
ATOM   221  C CD2 . LEU A 1 26  ? 40.50400 -7.61400  23.29700  1.000 72.24000  ? 26  LEU A CD2 1 
ATOM   222  N N   . ARG A 1 27  ? 38.94200 -3.00400  20.92700  1.000 72.15000  ? 27  ARG A N   1 
ATOM   223  C CA  . ARG A 1 27  ? 38.10800 -1.82000  21.08900  1.000 72.57000  ? 27  ARG A CA  1 
ATOM   224  C C   . ARG A 1 27  ? 36.72100 -2.03900  20.50800  1.000 70.88000  ? 27  ARG A C   1 
ATOM   225  O O   . ARG A 1 27  ? 35.79300 -1.30300  20.84400  1.000 75.30000  ? 27  ARG A O   1 
ATOM   226  C CB  . ARG A 1 27  ? 38.77500 -0.60800  20.45400  1.000 73.70000  ? 27  ARG A CB  1 
ATOM   227  C CG  . ARG A 1 27  ? 38.04700 0.67300   20.69700  1.000 75.77000  ? 27  ARG A CG  1 
ATOM   228  C CD  . ARG A 1 27  ? 37.79700 0.82000   22.17400  1.000 84.63000  ? 27  ARG A CD  1 
ATOM   229  N NE  . ARG A 1 27  ? 36.80600 1.84300   22.45000  1.000 86.71000  ? 27  ARG A NE  1 
ATOM   230  C CZ  . ARG A 1 27  ? 36.33600 2.11000   23.65700  1.000 90.78000  ? 27  ARG A CZ  1 
ATOM   231  N NH1 . ARG A 1 27  ? 36.77400 1.42100   24.71400  1.000 91.05000  ? 27  ARG A NH1 1 
ATOM   232  N NH2 . ARG A 1 27  ? 35.42900 3.06800   23.80100  1.000 93.90000  ? 27  ARG A NH2 1 
ATOM   233  N N   . VAL A 1 28  ? 36.54900 -3.06600  19.68500  1.000 66.28000  ? 28  VAL A N   1 
ATOM   234  C CA  . VAL A 1 28  ? 35.23800 -3.37200  19.13200  1.000 72.87000  ? 28  VAL A CA  1 
ATOM   235  C C   . VAL A 1 28  ? 34.48000 -4.28000  20.07500  1.000 71.50000  ? 28  VAL A C   1 
ATOM   236  O O   . VAL A 1 28  ? 33.26700 -4.12800  20.26800  1.000 67.98000  ? 28  VAL A O   1 
ATOM   237  C CB  . VAL A 1 28  ? 35.38700 -4.02400  17.74400  1.000 71.61000  ? 28  VAL A CB  1 
ATOM   238  C CG1 . VAL A 1 28  ? 34.05300 -4.55400  17.26900  1.000 67.90000  ? 28  VAL A CG1 1 
ATOM   239  C CG2 . VAL A 1 28  ? 35.98600 -3.05600  16.77400  1.000 67.63000  ? 28  VAL A CG2 1 
ATOM   240  N N   . SER A 1 29  ? 35.18500 -5.28300  20.60900  1.000 76.31000  ? 29  SER A N   1 
ATOM   241  C CA  . SER A 1 29  ? 34.70500 -6.06700  21.74200  1.000 75.72000  ? 29  SER A CA  1 
ATOM   242  C C   . SER A 1 29  ? 34.06500 -5.17600  22.78900  1.000 70.04000  ? 29  SER A C   1 
ATOM   243  O O   . SER A 1 29  ? 32.89700 -5.35500  23.15100  1.000 74.97000  ? 29  SER A O   1 
ATOM   244  C CB  . SER A 1 29  ? 35.86900 -6.84000  22.35700  1.000 75.42000  ? 29  SER A CB  1 
ATOM   245  O OG  . SER A 1 29  ? 35.37400 -7.83700  23.21200  1.000 80.46000  ? 29  SER A OG  1 
ATOM   246  N N   . ASP A 1 30  ? 34.83600 -4.19700  23.27100  1.000 62.70000  ? 30  ASP A N   1 
ATOM   247  C CA  . ASP A 1 30  ? 34.30700 -3.20300  24.20100  1.000 69.93000  ? 30  ASP A CA  1 
ATOM   248  C C   . ASP A 1 30  ? 33.01000 -2.59900  23.70700  1.000 68.11000  ? 30  ASP A C   1 
ATOM   249  O O   . ASP A 1 30  ? 32.08200 -2.37100  24.48600  1.000 68.97000  ? 30  ASP A O   1 
ATOM   250  C CB  . ASP A 1 30  ? 35.32300 -2.08800  24.40700  1.000 75.70000  ? 30  ASP A CB  1 
ATOM   251  C CG  . ASP A 1 30  ? 36.56900 -2.56200  25.10000  1.000 84.03000  ? 30  ASP A CG  1 
ATOM   252  O OD1 . ASP A 1 30  ? 36.64000 -3.77000  25.43400  1.000 84.12000  ? 30  ASP A OD1 1 
ATOM   253  O OD2 . ASP A 1 30  ? 37.47200 -1.72300  25.30800  1.000 86.42000  ? 30  ASP A OD2 1 
ATOM   254  N N   . LEU A 1 31  ? 32.93200 -2.30700  22.41200  1.000 78.73000  ? 31  LEU A N   1 
ATOM   255  C CA  . LEU A 1 31  ? 31.77000 -1.59700  21.90000  1.000 70.36000  ? 31  LEU A CA  1 
ATOM   256  C C   . LEU A 1 31  ? 30.59200 -2.52800  21.69900  1.000 68.98000  ? 31  LEU A C   1 
ATOM   257  O O   . LEU A 1 31  ? 29.44300 -2.10000  21.86700  1.000 70.16000  ? 31  LEU A O   1 
ATOM   258  C CB  . LEU A 1 31  ? 32.14100 -0.87200  20.61300  1.000 76.93000  ? 31  LEU A CB  1 
ATOM   259  C CG  . LEU A 1 31  ? 33.15700 0.24500   20.86800  1.000 77.59000  ? 31  LEU A CG  1 
ATOM   260  C CD1 . LEU A 1 31  ? 33.54600 0.90500   19.54600  1.000 81.19000  ? 31  LEU A CD1 1 
ATOM   261  C CD2 . LEU A 1 31  ? 32.63100 1.28000   21.87700  1.000 80.82000  ? 31  LEU A CD2 1 
ATOM   262  N N   . ILE A 1 32  ? 30.85500 -3.80000  21.39400  1.000 67.93000  ? 32  ILE A N   1 
ATOM   263  C CA  . ILE A 1 32  ? 29.79000 -4.80300  21.37900  1.000 69.79000  ? 32  ILE A CA  1 
ATOM   264  C C   . ILE A 1 32  ? 29.18000 -4.96800  22.77400  1.000 70.65000  ? 32  ILE A C   1 
ATOM   265  O O   . ILE A 1 32  ? 27.95400 -5.05800  22.92500  1.000 68.05000  ? 32  ILE A O   1 
ATOM   266  C CB  . ILE A 1 32  ? 30.32400 -6.13600  20.83500  1.000 69.55000  ? 32  ILE A CB  1 
ATOM   267  C CG1 . ILE A 1 32  ? 30.91100 -5.91000  19.43200  1.000 78.71000  ? 32  ILE A CG1 1 
ATOM   268  C CG2 . ILE A 1 32  ? 29.23400 -7.19100  20.84100  1.000 67.16000  ? 32  ILE A CG2 1 
ATOM   269  C CD1 . ILE A 1 32  ? 31.38600 -7.15000  18.69600  1.000 74.50000  ? 32  ILE A CD1 1 
ATOM   270  N N   . TYR A 1 33  ? 30.02100 -5.03500  23.81300  1.000 71.49000  ? 33  TYR A N   1 
ATOM   271  C CA  . TYR A 1 33  ? 29.48200 -5.06800  25.17500  1.000 75.51000  ? 33  TYR A CA  1 
ATOM   272  C C   . TYR A 1 33  ? 28.58800 -3.86800  25.43300  1.000 75.98000  ? 33  TYR A C   1 
ATOM   273  O O   . TYR A 1 33  ? 27.46500 -4.00800  25.92400  1.000 78.39000  ? 33  TYR A O   1 
ATOM   274  C CB  . TYR A 1 33  ? 30.59300 -5.09800  26.21400  1.000 74.95000  ? 33  TYR A CB  1 
ATOM   275  C CG  . TYR A 1 33  ? 30.12300 -4.64300  27.58400  1.000 72.81000  ? 33  TYR A CG  1 
ATOM   276  C CD1 . TYR A 1 33  ? 29.41000 -5.50100  28.41200  1.000 76.39000  ? 33  TYR A CD1 1 
ATOM   277  C CD2 . TYR A 1 33  ? 30.39500 -3.35900  28.05400  1.000 76.32000  ? 33  TYR A CD2 1 
ATOM   278  C CE1 . TYR A 1 33  ? 28.97200 -5.09200  29.66200  1.000 80.10000  ? 33  TYR A CE1 1 
ATOM   279  C CE2 . TYR A 1 33  ? 29.96200 -2.94900  29.30900  1.000 82.47000  ? 33  TYR A CE2 1 
ATOM   280  C CZ  . TYR A 1 33  ? 29.25700 -3.82600  30.10200  1.000 80.36000  ? 33  TYR A CZ  1 
ATOM   281  O OH  . TYR A 1 33  ? 28.81900 -3.44600  31.33600  1.000 74.93000  ? 33  TYR A OH  1 
ATOM   282  N N   . GLU A 1 34  ? 29.08000 -2.67100  25.11400  1.000 71.35000  ? 34  GLU A N   1 
ATOM   283  C CA  . GLU A 1 34  ? 28.28400 -1.47700  25.36300  1.000 71.58000  ? 34  GLU A CA  1 
ATOM   284  C C   . GLU A 1 34  ? 27.03500 -1.45400  24.48400  1.000 81.19000  ? 34  GLU A C   1 
ATOM   285  O O   . GLU A 1 34  ? 25.97400 -1.00900  24.93500  1.000 87.02000  ? 34  GLU A O   1 
ATOM   286  C CB  . GLU A 1 34  ? 29.15300 -0.23000  25.16200  1.000 66.90000  ? 34  GLU A CB  1 
ATOM   287  C CG  . GLU A 1 34  ? 28.97900 0.86600   26.21300  1.000 79.47000  ? 34  GLU A CG  1 
ATOM   288  C CD  . GLU A 1 34  ? 29.30200 0.41800   27.65300  1.000 94.87000  ? 34  GLU A CD  1 
ATOM   289  O OE1 . GLU A 1 34  ? 30.46800 0.02500   27.93100  1.000 93.60000  ? 34  GLU A OE1 1 
ATOM   290  O OE2 . GLU A 1 34  ? 28.38000 0.46900   28.51000  1.000 98.23000  ? 34  GLU A OE2 1 
ATOM   291  N N   . PHE A 1 35  ? 27.13400 -1.97400  23.24500  1.000 79.47000  ? 35  PHE A N   1 
ATOM   292  C CA  . PHE A 1 35  ? 26.01300 -1.98600  22.30400  1.000 78.41000  ? 35  PHE A CA  1 
ATOM   293  C C   . PHE A 1 35  ? 24.88800 -2.90600  22.75100  1.000 79.41000  ? 35  PHE A C   1 
ATOM   294  O O   . PHE A 1 35  ? 23.72000 -2.61800  22.48600  1.000 84.57000  ? 35  PHE A O   1 
ATOM   295  C CB  . PHE A 1 35  ? 26.52200 -2.40300  20.91000  1.000 81.87000  ? 35  PHE A CB  1 
ATOM   296  C CG  . PHE A 1 35  ? 25.45500 -2.49500  19.84000  1.000 73.94000  ? 35  PHE A CG  1 
ATOM   297  C CD1 . PHE A 1 35  ? 25.08400 -1.38300  19.10900  1.000 77.75000  ? 35  PHE A CD1 1 
ATOM   298  C CD2 . PHE A 1 35  ? 24.86400 -3.71300  19.54100  1.000 81.52000  ? 35  PHE A CD2 1 
ATOM   299  C CE1 . PHE A 1 35  ? 24.11200 -1.47900  18.11700  1.000 87.69000  ? 35  PHE A CE1 1 
ATOM   300  C CE2 . PHE A 1 35  ? 23.89600 -3.82100  18.55100  1.000 84.16000  ? 35  PHE A CE2 1 
ATOM   301  C CZ  . PHE A 1 35  ? 23.51900 -2.70300  17.83800  1.000 88.03000  ? 35  PHE A CZ  1 
ATOM   302  N N   . MET A 1 36  ? 25.21100 -4.01800  23.39500  1.000 83.61000  ? 36  MET A N   1 
ATOM   303  C CA  . MET A 1 36  ? 24.21000 -4.95900  23.88200  1.000 83.41000  ? 36  MET A CA  1 
ATOM   304  C C   . MET A 1 36  ? 23.66300 -4.59300  25.25700  1.000 83.63000  ? 36  MET A C   1 
ATOM   305  O O   . MET A 1 36  ? 22.77500 -5.28300  25.76100  1.000 86.58000  ? 36  MET A O   1 
ATOM   306  C CB  . MET A 1 36  ? 24.80000 -6.37200  23.90900  1.000 82.80000  ? 36  MET A CB  1 
ATOM   307  C CG  . MET A 1 36  ? 25.16400 -6.89500  22.55700  1.000 77.58000  ? 36  MET A CG  1 
ATOM   308  S SD  . MET A 1 36  ? 25.85000 -8.53600  22.65300  1.000 78.11000  ? 36  MET A SD  1 
ATOM   309  C CE  . MET A 1 36  ? 24.37900 -9.54600  22.57000  1.000 71.92000  ? 36  MET A CE  1 
ATOM   310  N N   . LYS A 1 37  ? 24.33200 -3.70100  25.97100  1.000 87.91000  ? 37  LYS A N   1 
ATOM   311  C CA  . LYS A 1 37  ? 23.73900 -3.21600  27.20500  1.000 92.91000  ? 37  LYS A CA  1 
ATOM   312  C C   . LYS A 1 37  ? 22.70700 -2.14300  26.89300  1.000 105.09000 ? 37  LYS A C   1 
ATOM   313  O O   . LYS A 1 37  ? 21.62400 -2.13100  27.49500  1.000 108.81000 ? 37  LYS A O   1 
ATOM   314  C CB  . LYS A 1 37  ? 24.81500 -2.67200  28.15000  1.000 91.26000  ? 37  LYS A CB  1 
ATOM   315  C CG  . LYS A 1 37  ? 25.57600 -3.70300  28.95700  1.000 90.46000  ? 37  LYS A CG  1 
ATOM   316  C CD  . LYS A 1 37  ? 24.62500 -4.63400  29.67900  1.000 93.24000  ? 37  LYS A CD  1 
ATOM   317  C CE  . LYS A 1 37  ? 25.35400 -5.48500  30.70900  1.000 82.78000  ? 37  LYS A CE  1 
ATOM   318  N NZ  . LYS A 1 37  ? 25.56400 -4.74400  31.96500  1.000 85.46000  ? 37  LYS A NZ  1 
ATOM   319  N N   . LYS A 1 38  ? 23.02800 -1.24800  25.93900  1.000 100.21000 ? 38  LYS A N   1 
ATOM   320  C CA  . LYS A 1 38  ? 22.18000 -0.12500  25.54300  1.000 106.61000 ? 38  LYS A CA  1 
ATOM   321  C C   . LYS A 1 38  ? 20.81100 -0.64800  25.13600  1.000 116.42000 ? 38  LYS A C   1 
ATOM   322  O O   . LYS A 1 38  ? 20.68100 -1.29500  24.09100  1.000 117.22000 ? 38  LYS A O   1 
ATOM   323  C CB  . LYS A 1 38  ? 22.81300 0.67800   24.39200  1.000 108.50000 ? 38  LYS A CB  1 
ATOM   324  C CG  . LYS A 1 38  ? 23.60500 1.95900   24.78300  1.000 105.17000 ? 38  LYS A CG  1 
ATOM   325  C CD  . LYS A 1 38  ? 24.35000 2.53000   23.54800  1.000 102.67000 ? 38  LYS A CD  1 
ATOM   326  C CE  . LYS A 1 38  ? 24.70300 4.02000   23.67700  1.000 102.06000 ? 38  LYS A CE  1 
ATOM   327  N NZ  . LYS A 1 38  ? 25.23300 4.58100   22.39200  1.000 101.66000 ? 38  LYS A NZ  1 
ATOM   328  N N   . ASP A 1 39  ? 19.79600 -0.38400  25.96500  1.000 128.53000 ? 39  ASP A N   1 
ATOM   329  C CA  . ASP A 1 39  ? 18.43700 -0.91900  25.77300  1.000 131.04000 ? 39  ASP A CA  1 
ATOM   330  C C   . ASP A 1 39  ? 17.61100 -0.16000  24.72900  1.000 132.42000 ? 39  ASP A C   1 
ATOM   331  O O   . ASP A 1 39  ? 16.45600 0.21100   24.98800  1.000 134.12000 ? 39  ASP A O   1 
ATOM   332  C CB  . ASP A 1 39  ? 17.67200 -0.92500  27.10400  1.000 129.46000 ? 39  ASP A CB  1 
ATOM   333  C CG  . ASP A 1 39  ? 17.75600 -2.25800  27.82000  1.000 131.58000 ? 39  ASP A CG  1 
ATOM   334  O OD1 . ASP A 1 39  ? 18.86000 -2.60600  28.30300  1.000 128.66000 ? 39  ASP A OD1 1 
ATOM   335  O OD2 . ASP A 1 39  ? 16.71500 -2.95300  27.89300  1.000 131.75000 ? 39  ASP A OD2 1 
ATOM   336  O OXT . ASP A 1 39  ? 18.07300 0.08700   23.61000  1.000 128.89000 ? 39  ASP A OXT 1 
ATOM   337  N N   . ASN B 2 2   ? 55.30000 -19.03900 61.19200  1.000 98.71000  ? 334 ASN B N   1 
ATOM   338  C CA  . ASN B 2 2   ? 54.23900 -19.61800 60.37300  1.000 102.72000 ? 334 ASN B CA  1 
ATOM   339  C C   . ASN B 2 2   ? 53.63400 -18.61700 59.35600  1.000 95.24000  ? 334 ASN B C   1 
ATOM   340  O O   . ASN B 2 2   ? 52.57400 -18.04700 59.59000  1.000 90.50000  ? 334 ASN B O   1 
ATOM   341  C CB  . ASN B 2 2   ? 53.16100 -20.17300 61.29400  1.000 98.05000  ? 334 ASN B CB  1 
ATOM   342  C CG  . ASN B 2 2   ? 52.84200 -21.61400 60.99400  1.000 107.52000 ? 334 ASN B CG  1 
ATOM   343  O OD1 . ASN B 2 2   ? 52.85100 -22.03400 59.83000  1.000 109.23000 ? 334 ASN B OD1 1 
ATOM   344  N ND2 . ASN B 2 2   ? 52.54400 -22.38800 62.03400  1.000 100.37000 ? 334 ASN B ND2 1 
ATOM   345  N N   . LEU B 2 3   ? 54.32600 -18.43100 58.23000  1.000 93.87000  ? 335 LEU B N   1 
ATOM   346  C CA  . LEU B 2 3   ? 54.05800 -17.33300 57.30400  1.000 93.98000  ? 335 LEU B CA  1 
ATOM   347  C C   . LEU B 2 3   ? 52.93300 -17.64800 56.31100  1.000 91.25000  ? 335 LEU B C   1 
ATOM   348  O O   . LEU B 2 3   ? 52.76700 -18.78500 55.86000  1.000 93.19000  ? 335 LEU B O   1 
ATOM   349  C CB  . LEU B 2 3   ? 55.34600 -16.97700 56.55100  1.000 96.49000  ? 335 LEU B CB  1 
ATOM   350  C CG  . LEU B 2 3   ? 55.35300 -15.90400 55.46100  1.000 100.58000 ? 335 LEU B CG  1 
ATOM   351  C CD1 . LEU B 2 3   ? 54.98900 -14.54600 56.04600  1.000 99.40000  ? 335 LEU B CD1 1 
ATOM   352  C CD2 . LEU B 2 3   ? 56.72800 -15.84700 54.79200  1.000 107.28000 ? 335 LEU B CD2 1 
ATOM   353  N N   . CYS B 2 4   ? 52.14400 -16.62500 55.98900  1.000 86.80000  ? 336 CYS B N   1 
ATOM   354  C CA  . CYS B 2 4   ? 51.14400 -16.76200 54.93500  1.000 92.08000  ? 336 CYS B CA  1 
ATOM   355  C C   . CYS B 2 4   ? 51.82600 -16.87900 53.57300  1.000 88.91000  ? 336 CYS B C   1 
ATOM   356  O O   . CYS B 2 4   ? 52.62900 -16.01200 53.21200  1.000 85.62000  ? 336 CYS B O   1 
ATOM   357  C CB  . CYS B 2 4   ? 50.18400 -15.57700 54.93000  1.000 85.55000  ? 336 CYS B CB  1 
ATOM   358  S SG  . CYS B 2 4   ? 49.17700 -15.42600 56.37600  1.000 87.07000  ? 336 CYS B SG  1 
ATOM   359  N N   . PRO B 2 5   ? 51.52400 -17.91600 52.79100  1.000 85.00000  ? 337 PRO B N   1 
ATOM   360  C CA  . PRO B 2 5   ? 52.15800 -18.14300 51.47700  1.000 90.49000  ? 337 PRO B CA  1 
ATOM   361  C C   . PRO B 2 5   ? 51.51700 -17.29300 50.38200  1.000 89.62000  ? 337 PRO B C   1 
ATOM   362  O O   . PRO B 2 5   ? 50.62400 -17.70700 49.64200  1.000 87.30000  ? 337 PRO B O   1 
ATOM   363  C CB  . PRO B 2 5   ? 51.92700 -19.63900 51.25400  1.000 94.86000  ? 337 PRO B CB  1 
ATOM   364  C CG  . PRO B 2 5   ? 50.58700 -19.87800 51.89100  1.000 93.06000  ? 337 PRO B CG  1 
ATOM   365  C CD  . PRO B 2 5   ? 50.48500 -18.92200 53.07300  1.000 87.46000  ? 337 PRO B CD  1 
ATOM   366  N N   . PHE B 2 6   ? 51.97200 -16.04400 50.30800  1.000 89.80000  ? 338 PHE B N   1 
ATOM   367  C CA  . PHE B 2 6   ? 51.53100 -15.11800 49.28100  1.000 89.45000  ? 338 PHE B CA  1 
ATOM   368  C C   . PHE B 2 6   ? 52.37100 -15.20100 48.02200  1.000 84.93000  ? 338 PHE B C   1 
ATOM   369  O O   . PHE B 2 6   ? 51.90800 -14.78300 46.95600  1.000 87.20000  ? 338 PHE B O   1 
ATOM   370  C CB  . PHE B 2 6   ? 51.57200 -13.68900 49.81000  1.000 88.40000  ? 338 PHE B CB  1 
ATOM   371  C CG  . PHE B 2 6   ? 50.43800 -13.34900 50.70500  1.000 87.43000  ? 338 PHE B CG  1 
ATOM   372  C CD1 . PHE B 2 6   ? 49.15700 -13.21900 50.19800  1.000 90.68000  ? 338 PHE B CD1 1 
ATOM   373  C CD2 . PHE B 2 6   ? 50.64900 -13.14600 52.05800  1.000 89.34000  ? 338 PHE B CD2 1 
ATOM   374  C CE1 . PHE B 2 6   ? 48.10900 -12.89000 51.03300  1.000 88.53000  ? 338 PHE B CE1 1 
ATOM   375  C CE2 . PHE B 2 6   ? 49.60600 -12.82700 52.89100  1.000 86.71000  ? 338 PHE B CE2 1 
ATOM   376  C CZ  . PHE B 2 6   ? 48.33700 -12.70100 52.38300  1.000 82.24000  ? 338 PHE B CZ  1 
ATOM   377  N N   . GLY B 2 7   ? 53.60100 -15.69500 48.12800  1.000 86.79000  ? 339 GLY B N   1 
ATOM   378  C CA  . GLY B 2 7   ? 54.40100 -15.89700 46.93800  1.000 91.94000  ? 339 GLY B CA  1 
ATOM   379  C C   . GLY B 2 7   ? 53.72600 -16.83000 45.96000  1.000 94.77000  ? 339 GLY B C   1 
ATOM   380  O O   . GLY B 2 7   ? 53.77400 -16.62000 44.75100  1.000 93.47000  ? 339 GLY B O   1 
ATOM   381  N N   . GLU B 2 8   ? 53.06400 -17.86500 46.47400  1.000 94.80000  ? 340 GLU B N   1 
ATOM   382  C CA  . GLU B 2 8   ? 52.29200 -18.73400 45.59700  1.000 86.81000  ? 340 GLU B CA  1 
ATOM   383  C C   . GLU B 2 8   ? 51.22200 -17.97100 44.85200  1.000 88.19000  ? 340 GLU B C   1 
ATOM   384  O O   . GLU B 2 8   ? 50.76900 -18.41600 43.79600  1.000 96.55000  ? 340 GLU B O   1 
ATOM   385  C CB  . GLU B 2 8   ? 51.61800 -19.82300 46.39400  1.000 86.81000  ? 340 GLU B CB  1 
ATOM   386  C CG  . GLU B 2 8   ? 52.52900 -20.60100 47.21600  1.000 87.27000  ? 340 GLU B CG  1 
ATOM   387  C CD  . GLU B 2 8   ? 51.77300 -21.70500 47.83800  1.000 91.81000  ? 340 GLU B CD  1 
ATOM   388  O OE1 . GLU B 2 8   ? 50.76000 -22.10000 47.21100  1.000 85.94000  ? 340 GLU B OE1 1 
ATOM   389  O OE2 . GLU B 2 8   ? 52.15900 -22.14300 48.94500  1.000 92.79000  ? 340 GLU B OE2 1 
ATOM   390  N N   . VAL B 2 9   ? 50.75700 -16.86200 45.40600  1.000 86.36000  ? 341 VAL B N   1 
ATOM   391  C CA  . VAL B 2 9   ? 49.74100 -16.08700 44.72600  1.000 86.46000  ? 341 VAL B CA  1 
ATOM   392  C C   . VAL B 2 9   ? 50.36700 -15.01700 43.85000  1.000 88.32000  ? 341 VAL B C   1 
ATOM   393  O O   . VAL B 2 9   ? 50.11200 -14.97000 42.64200  1.000 88.41000  ? 341 VAL B O   1 
ATOM   394  C CB  . VAL B 2 9   ? 48.76200 -15.50100 45.75300  1.000 82.95000  ? 341 VAL B CB  1 
ATOM   395  C CG1 . VAL B 2 9   ? 47.82900 -14.54200 45.06800  1.000 79.21000  ? 341 VAL B CG1 1 
ATOM   396  C CG2 . VAL B 2 9   ? 47.98000 -16.63100 46.39100  1.000 78.60000  ? 341 VAL B CG2 1 
ATOM   397  N N   . PHE B 2 10  ? 51.22000 -14.16700 44.42900  1.000 87.79000  ? 342 PHE B N   1 
ATOM   398  C CA  . PHE B 2 10  ? 51.83100 -13.09500 43.64400  1.000 88.96000  ? 342 PHE B CA  1 
ATOM   399  C C   . PHE B 2 10  ? 52.95400 -13.62600 42.76500  1.000 92.51000  ? 342 PHE B C   1 
ATOM   400  O O   . PHE B 2 10  ? 52.98600 -13.36500 41.55800  1.000 86.77000  ? 342 PHE B O   1 
ATOM   401  C CB  . PHE B 2 10  ? 52.34400 -11.98600 44.56000  1.000 86.32000  ? 342 PHE B CB  1 
ATOM   402  C CG  . PHE B 2 10  ? 51.26100 -11.30600 45.34800  1.000 84.07000  ? 342 PHE B CG  1 
ATOM   403  C CD1 . PHE B 2 10  ? 50.71800 -11.90500 46.47500  1.000 85.66000  ? 342 PHE B CD1 1 
ATOM   404  C CD2 . PHE B 2 10  ? 50.78200 -10.06900 44.96400  1.000 83.14000  ? 342 PHE B CD2 1 
ATOM   405  C CE1 . PHE B 2 10  ? 49.71900 -11.27900 47.19300  1.000 87.28000  ? 342 PHE B CE1 1 
ATOM   406  C CE2 . PHE B 2 10  ? 49.78400 -9.43900  45.68300  1.000 83.19000  ? 342 PHE B CE2 1 
ATOM   407  C CZ  . PHE B 2 10  ? 49.25300 -10.03800 46.79300  1.000 85.55000  ? 342 PHE B CZ  1 
ATOM   408  N N   . ASN B 2 11  ? 53.86900 -14.39500 43.34500  1.000 96.55000  ? 343 ASN B N   1 
ATOM   409  C CA  . ASN B 2 11  ? 55.02500 -14.87400 42.60000  1.000 99.94000  ? 343 ASN B CA  1 
ATOM   410  C C   . ASN B 2 11  ? 54.71400 -16.16500 41.83600  1.000 94.80000  ? 343 ASN B C   1 
ATOM   411  O O   . ASN B 2 11  ? 55.61600 -16.96400 41.58100  1.000 101.23000 ? 343 ASN B O   1 
ATOM   412  C CB  . ASN B 2 11  ? 56.21700 -15.05600 43.56900  1.000 101.81000 ? 343 ASN B CB  1 
ATOM   413  C CG  . ASN B 2 11  ? 56.89800 -13.72000 43.93200  1.000 105.14000 ? 343 ASN B CG  1 
ATOM   414  O OD1 . ASN B 2 11  ? 56.85300 -12.77400 43.14600  1.000 113.13000 ? 343 ASN B OD1 1 
ATOM   415  N ND2 . ASN B 2 11  ? 57.53000 -13.64200 45.11100  1.000 108.37000 ? 343 ASN B ND2 1 
ATOM   416  N N   . ALA B 2 12  ? 53.46300 -16.39100 41.44500  1.000 87.71000  ? 344 ALA B N   1 
ATOM   417  C CA  . ALA B 2 12  ? 53.11700 -17.62400 40.74600  1.000 84.47000  ? 344 ALA B CA  1 
ATOM   418  C C   . ALA B 2 12  ? 53.34500 -17.50200 39.24100  1.000 88.62000  ? 344 ALA B C   1 
ATOM   419  O O   . ALA B 2 12  ? 53.34200 -16.40900 38.67500  1.000 90.53000  ? 344 ALA B O   1 
ATOM   420  C CB  . ALA B 2 12  ? 51.66700 -18.01200 41.00200  1.000 85.83000  ? 344 ALA B CB  1 
ATOM   421  N N   . THR B 2 13  ? 53.49200 -18.66100 38.59100  1.000 85.93000  ? 345 THR B N   1 
ATOM   422  C CA  . THR B 2 13  ? 53.97600 -18.73400 37.21200  1.000 86.67000  ? 345 THR B CA  1 
ATOM   423  C C   . THR B 2 13  ? 52.85900 -18.50600 36.19900  1.000 89.26000  ? 345 THR B C   1 
ATOM   424  O O   . THR B 2 13  ? 52.94500 -17.62200 35.33600  1.000 87.54000  ? 345 THR B O   1 
ATOM   425  C CB  . THR B 2 13  ? 54.61600 -20.10400 36.96400  1.000 90.98000  ? 345 THR B CB  1 
ATOM   426  O OG1 . THR B 2 13  ? 55.91300 -20.15300 37.56600  1.000 91.96000  ? 345 THR B OG1 1 
ATOM   427  C CG2 . THR B 2 13  ? 54.72600 -20.38900 35.45300  1.000 92.10000  ? 345 THR B CG2 1 
ATOM   428  N N   . ARG B 2 14  ? 51.83300 -19.34500 36.25700  1.000 86.22000  ? 346 ARG B N   1 
ATOM   429  C CA  . ARG B 2 14  ? 50.66700 -19.21300 35.41400  1.000 87.31000  ? 346 ARG B CA  1 
ATOM   430  C C   . ARG B 2 14  ? 49.54100 -18.56100 36.20800  1.000 81.46000  ? 346 ARG B C   1 
ATOM   431  O O   . ARG B 2 14  ? 49.28700 -18.93000 37.35600  1.000 81.05000  ? 346 ARG B O   1 
ATOM   432  C CB  . ARG B 2 14  ? 50.25800 -20.58200 34.86300  1.000 92.64000  ? 346 ARG B CB  1 
ATOM   433  C CG  . ARG B 2 14  ? 51.36800 -21.19600 33.98100  1.000 101.60000 ? 346 ARG B CG  1 
ATOM   434  C CD  . ARG B 2 14  ? 51.04300 -22.58600 33.40800  1.000 101.77000 ? 346 ARG B CD  1 
ATOM   435  N NE  . ARG B 2 14  ? 49.95300 -22.57300 32.43300  1.000 98.77000  ? 346 ARG B NE  1 
ATOM   436  C CZ  . ARG B 2 14  ? 48.76500 -23.14500 32.63300  1.000 100.55000 ? 346 ARG B CZ  1 
ATOM   437  N NH1 . ARG B 2 14  ? 48.52400 -23.78700 33.77300  1.000 109.90000 ? 346 ARG B NH1 1 
ATOM   438  N NH2 . ARG B 2 14  ? 47.82100 -23.08100 31.69200  1.000 93.10000  ? 346 ARG B NH2 1 
ATOM   439  N N   . PHE B 2 15  ? 48.91000 -17.55900 35.61100  1.000 82.84000  ? 347 PHE B N   1 
ATOM   440  C CA  . PHE B 2 15  ? 47.71200 -16.93900 36.15300  1.000 79.68000  ? 347 PHE B CA  1 
ATOM   441  C C   . PHE B 2 15  ? 46.48700 -17.40500 35.38300  1.000 78.17000  ? 347 PHE B C   1 
ATOM   442  O O   . PHE B 2 15  ? 46.57300 -17.86100 34.24100  1.000 79.17000  ? 347 PHE B O   1 
ATOM   443  C CB  . PHE B 2 15  ? 47.81300 -15.41800 36.08900  1.000 78.39000  ? 347 PHE B CB  1 
ATOM   444  C CG  . PHE B 2 15  ? 48.41700 -14.80400 37.30700  1.000 80.63000  ? 347 PHE B CG  1 
ATOM   445  C CD1 . PHE B 2 15  ? 49.63100 -15.25700 37.79600  1.000 83.65000  ? 347 PHE B CD1 1 
ATOM   446  C CD2 . PHE B 2 15  ? 47.78300 -13.77200 37.95700  1.000 75.63000  ? 347 PHE B CD2 1 
ATOM   447  C CE1 . PHE B 2 15  ? 50.19100 -14.69800 38.91500  1.000 76.72000  ? 347 PHE B CE1 1 
ATOM   448  C CE2 . PHE B 2 15  ? 48.34300 -13.20800 39.07800  1.000 75.91000  ? 347 PHE B CE2 1 
ATOM   449  C CZ  . PHE B 2 15  ? 49.54700 -13.67500 39.55700  1.000 77.54000  ? 347 PHE B CZ  1 
ATOM   450  N N   . ALA B 2 16  ? 45.33400 -17.26300 36.01200  1.000 78.00000  ? 348 ALA B N   1 
ATOM   451  C CA  . ALA B 2 16  ? 44.09800 -17.65800 35.36400  1.000 76.80000  ? 348 ALA B CA  1 
ATOM   452  C C   . ALA B 2 16  ? 43.59400 -16.55200 34.44900  1.000 73.52000  ? 348 ALA B C   1 
ATOM   453  O O   . ALA B 2 16  ? 43.79900 -15.36400 34.70700  1.000 75.84000  ? 348 ALA B O   1 
ATOM   454  C CB  . ALA B 2 16  ? 43.03000 -17.99500 36.40600  1.000 75.24000  ? 348 ALA B CB  1 
ATOM   455  N N   . SER B 2 17  ? 42.95200 -16.95600 33.35500  1.000 68.56000  ? 349 SER B N   1 
ATOM   456  C CA  . SER B 2 17  ? 42.04500 -16.05100 32.66500  1.000 72.23000  ? 349 SER B CA  1 
ATOM   457  C C   . SER B 2 17  ? 41.02900 -15.51900 33.66100  1.000 69.88000  ? 349 SER B C   1 
ATOM   458  O O   . SER B 2 17  ? 40.64700 -16.20600 34.61500  1.000 76.76000  ? 349 SER B O   1 
ATOM   459  C CB  . SER B 2 17  ? 41.32000 -16.76900 31.51300  1.000 66.52000  ? 349 SER B CB  1 
ATOM   460  O OG  . SER B 2 17  ? 42.24000 -17.24500 30.55600  1.000 70.88000  ? 349 SER B OG  1 
ATOM   461  N N   . VAL B 2 18  ? 40.57800 -14.28700 33.43600  1.000 68.19000  ? 350 VAL B N   1 
ATOM   462  C CA  . VAL B 2 18  ? 39.71200 -13.62100 34.40900  1.000 69.06000  ? 350 VAL B CA  1 
ATOM   463  C C   . VAL B 2 18  ? 38.35000 -14.29700 34.50200  1.000 69.58000  ? 350 VAL B C   1 
ATOM   464  O O   . VAL B 2 18  ? 37.74100 -14.33200 35.57700  1.000 73.87000  ? 350 VAL B O   1 
ATOM   465  C CB  . VAL B 2 18  ? 39.57300 -12.12900 34.06100  1.000 69.51000  ? 350 VAL B CB  1 
ATOM   466  C CG1 . VAL B 2 18  ? 38.88300 -11.93600 32.68600  1.000 68.97000  ? 350 VAL B CG1 1 
ATOM   467  C CG2 . VAL B 2 18  ? 38.83200 -11.39900 35.14400  1.000 65.25000  ? 350 VAL B CG2 1 
ATOM   468  N N   . TYR B 2 19  ? 37.83900 -14.84200 33.39700  1.000 70.72000  ? 351 TYR B N   1 
ATOM   469  C CA  . TYR B 2 19  ? 36.53200 -15.48600 33.49100  1.000 72.15000  ? 351 TYR B CA  1 
ATOM   470  C C   . TYR B 2 19  ? 36.60900 -16.73800 34.37500  1.000 71.47000  ? 351 TYR B C   1 
ATOM   471  O O   . TYR B 2 19  ? 35.62700 -17.07700 35.05400  1.000 75.08000  ? 351 TYR B O   1 
ATOM   472  C CB  . TYR B 2 19  ? 35.97900 -15.78100 32.08800  1.000 61.80000  ? 351 TYR B CB  1 
ATOM   473  C CG  . TYR B 2 19  ? 36.36700 -17.12200 31.57200  1.000 62.57000  ? 351 TYR B CG  1 
ATOM   474  C CD1 . TYR B 2 19  ? 37.63600 -17.35500 31.09800  1.000 60.37000  ? 351 TYR B CD1 1 
ATOM   475  C CD2 . TYR B 2 19  ? 35.45800 -18.15700 31.54700  1.000 67.20000  ? 351 TYR B CD2 1 
ATOM   476  C CE1 . TYR B 2 19  ? 37.99900 -18.59400 30.64800  1.000 60.35000  ? 351 TYR B CE1 1 
ATOM   477  C CE2 . TYR B 2 19  ? 35.81100 -19.41300 31.08700  1.000 61.46000  ? 351 TYR B CE2 1 
ATOM   478  C CZ  . TYR B 2 19  ? 37.08300 -19.62400 30.65200  1.000 59.97000  ? 351 TYR B CZ  1 
ATOM   479  O OH  . TYR B 2 19  ? 37.43300 -20.87200 30.20700  1.000 68.35000  ? 351 TYR B OH  1 
ATOM   480  N N   . ALA B 2 20  ? 37.78400 -17.38500 34.43600  1.000 69.62000  ? 352 ALA B N   1 
ATOM   481  C CA  . ALA B 2 20  ? 38.02700 -18.52800 35.31400  1.000 71.71000  ? 352 ALA B CA  1 
ATOM   482  C C   . ALA B 2 20  ? 39.02700 -18.17000 36.40300  1.000 69.49000  ? 352 ALA B C   1 
ATOM   483  O O   . ALA B 2 20  ? 39.96200 -18.93600 36.65500  1.000 65.13000  ? 352 ALA B O   1 
ATOM   484  C CB  . ALA B 2 20  ? 38.56900 -19.72800 34.54200  1.000 67.51000  ? 352 ALA B CB  1 
ATOM   485  N N   . TRP B 2 21  ? 38.83500 -17.01400 37.04200  1.000 66.86000  ? 353 TRP B N   1 
ATOM   486  C CA  . TRP B 2 21  ? 39.74700 -16.52400 38.06200  1.000 72.32000  ? 353 TRP B CA  1 
ATOM   487  C C   . TRP B 2 21  ? 40.09200 -17.61200 39.06000  1.000 72.73000  ? 353 TRP B C   1 
ATOM   488  O O   . TRP B 2 21  ? 39.33700 -18.57800 39.22700  1.000 73.97000  ? 353 TRP B O   1 
ATOM   489  C CB  . TRP B 2 21  ? 39.15700 -15.31600 38.79700  1.000 74.83000  ? 353 TRP B CB  1 
ATOM   490  C CG  . TRP B 2 21  ? 37.68800 -15.38800 39.17600  1.000 74.20000  ? 353 TRP B CG  1 
ATOM   491  C CD1 . TRP B 2 21  ? 36.62200 -15.24400 38.34200  1.000 67.40000  ? 353 TRP B CD1 1 
ATOM   492  C CD2 . TRP B 2 21  ? 37.14000 -15.55800 40.49800  1.000 70.03000  ? 353 TRP B CD2 1 
ATOM   493  N NE1 . TRP B 2 21  ? 35.44100 -15.33000 39.04800  1.000 63.21000  ? 353 TRP B NE1 1 
ATOM   494  C CE2 . TRP B 2 21  ? 35.73300 -15.52900 40.37500  1.000 71.20000  ? 353 TRP B CE2 1 
ATOM   495  C CE3 . TRP B 2 21  ? 37.69900 -15.74600 41.76100  1.000 73.05000  ? 353 TRP B CE3 1 
ATOM   496  C CZ2 . TRP B 2 21  ? 34.88200 -15.67900 41.47400  1.000 67.40000  ? 353 TRP B CZ2 1 
ATOM   497  C CZ3 . TRP B 2 21  ? 36.85400 -15.89000 42.84200  1.000 74.90000  ? 353 TRP B CZ3 1 
ATOM   498  C CH2 . TRP B 2 21  ? 35.45900 -15.85400 42.69300  1.000 63.41000  ? 353 TRP B CH2 1 
ATOM   499  N N   . ASN B 2 22  ? 41.23800 -17.45800 39.71100  1.000 69.23000  ? 354 ASN B N   1 
ATOM   500  C CA  . ASN B 2 22  ? 41.79200 -18.42500 40.65100  1.000 78.60000  ? 354 ASN B CA  1 
ATOM   501  C C   . ASN B 2 22  ? 41.64500 -17.90400 42.08300  1.000 70.98000  ? 354 ASN B C   1 
ATOM   502  O O   . ASN B 2 22  ? 41.92700 -16.73100 42.35100  1.000 66.94000  ? 354 ASN B O   1 
ATOM   503  C CB  . ASN B 2 22  ? 43.26100 -18.65800 40.31900  1.000 75.91000  ? 354 ASN B CB  1 
ATOM   504  C CG  . ASN B 2 22  ? 43.82900 -19.82500 41.03400  1.000 93.85000  ? 354 ASN B CG  1 
ATOM   505  O OD1 . ASN B 2 22  ? 43.11300 -20.79500 41.32000  1.000 98.39000  ? 354 ASN B OD1 1 
ATOM   506  N ND2 . ASN B 2 22  ? 45.12100 -19.76200 41.34000  1.000 104.26000 ? 354 ASN B ND2 1 
ATOM   507  N N   . ARG B 2 23  ? 41.22200 -18.76900 43.00700  1.000 68.06000  ? 355 ARG B N   1 
ATOM   508  C CA  . ARG B 2 23  ? 40.96700 -18.37100 44.39600  1.000 76.07000  ? 355 ARG B CA  1 
ATOM   509  C C   . ARG B 2 23  ? 41.77800 -19.22600 45.35500  1.000 72.74000  ? 355 ARG B C   1 
ATOM   510  O O   . ARG B 2 23  ? 41.62800 -20.45400 45.37600  1.000 75.21000  ? 355 ARG B O   1 
ATOM   511  C CB  . ARG B 2 23  ? 39.48700 -18.48200 44.76100  1.000 66.32000  ? 355 ARG B CB  1 
ATOM   512  C CG  . ARG B 2 23  ? 39.25600 -18.53700 46.26000  1.000 67.27000  ? 355 ARG B CG  1 
ATOM   513  C CD  . ARG B 2 23  ? 37.82700 -18.19700 46.65300  1.000 68.77000  ? 355 ARG B CD  1 
ATOM   514  N NE  . ARG B 2 23  ? 37.59100 -16.76300 46.55100  1.000 69.37000  ? 355 ARG B NE  1 
ATOM   515  C CZ  . ARG B 2 23  ? 36.43200 -16.17700 46.80200  1.000 63.54000  ? 355 ARG B CZ  1 
ATOM   516  N NH1 . ARG B 2 23  ? 35.39200 -16.90600 47.16100  1.000 58.34000  ? 355 ARG B NH1 1 
ATOM   517  N NH2 . ARG B 2 23  ? 36.31500 -14.86200 46.66400  1.000 68.42000  ? 355 ARG B NH2 1 
ATOM   518  N N   . LYS B 2 24  ? 42.59800 -18.57100 46.18100  1.000 70.37000  ? 356 LYS B N   1 
ATOM   519  C CA  . LYS B 2 24  ? 43.40900 -19.23200 47.19200  1.000 72.26000  ? 356 LYS B CA  1 
ATOM   520  C C   . LYS B 2 24  ? 42.92500 -18.83600 48.57900  1.000 65.69000  ? 356 LYS B C   1 
ATOM   521  O O   . LYS B 2 24  ? 42.72100 -17.65300 48.86700  1.000 63.39000  ? 356 LYS B O   1 
ATOM   522  C CB  . LYS B 2 24  ? 44.89000 -18.88500 47.03500  1.000 75.09000  ? 356 LYS B CB  1 
ATOM   523  C CG  . LYS B 2 24  ? 45.76100 -19.60900 48.02000  1.000 76.34000  ? 356 LYS B CG  1 
ATOM   524  C CD  . LYS B 2 24  ? 47.18500 -19.09800 48.03600  1.000 90.87000  ? 356 LYS B CD  1 
ATOM   525  C CE  . LYS B 2 24  ? 48.01700 -19.93100 49.00400  1.000 99.24000  ? 356 LYS B CE  1 
ATOM   526  N NZ  . LYS B 2 24  ? 48.22200 -21.31800 48.50500  1.000 88.55000  ? 356 LYS B NZ  1 
ATOM   527  N N   . ARG B 2 25  ? 42.73200 -19.84100 49.42800  1.000 70.54000  ? 357 ARG B N   1 
ATOM   528  C CA  . ARG B 2 25  ? 42.31200 -19.55600 50.81800  1.000 74.82000  ? 357 ARG B CA  1 
ATOM   529  C C   . ARG B 2 25  ? 43.55500 -19.39500 51.67500  1.000 70.31000  ? 357 ARG B C   1 
ATOM   530  O O   . ARG B 2 25  ? 44.51100 -20.15300 51.48400  1.000 72.32000  ? 357 ARG B O   1 
ATOM   531  C CB  . ARG B 2 25  ? 41.44900 -20.67000 51.40800  1.000 72.07000  ? 357 ARG B CB  1 
ATOM   532  C CG  . ARG B 2 25  ? 40.87200 -20.32700 52.77300  1.000 69.08000  ? 357 ARG B CG  1 
ATOM   533  C CD  . ARG B 2 25  ? 40.38600 -21.55700 53.50800  1.000 72.04000  ? 357 ARG B CD  1 
ATOM   534  N NE  . ARG B 2 25  ? 39.30800 -22.21500 52.79000  1.000 72.05000  ? 357 ARG B NE  1 
ATOM   535  C CZ  . ARG B 2 25  ? 38.04800 -21.80400 52.78500  1.000 74.13000  ? 357 ARG B CZ  1 
ATOM   536  N NH1 . ARG B 2 25  ? 37.69900 -20.72600 53.46400  1.000 75.41000  ? 357 ARG B NH1 1 
ATOM   537  N NH2 . ARG B 2 25  ? 37.13800 -22.47100 52.10200  1.000 82.59000  ? 357 ARG B NH2 1 
ATOM   538  N N   . ILE B 2 26  ? 43.52600 -18.42100 52.56700  1.000 63.74000  ? 358 ILE B N   1 
ATOM   539  C CA  . ILE B 2 26  ? 44.63800 -18.19100 53.46800  1.000 69.45000  ? 358 ILE B CA  1 
ATOM   540  C C   . ILE B 2 26  ? 44.12100 -18.24000 54.89700  1.000 71.07000  ? 358 ILE B C   1 
ATOM   541  O O   . ILE B 2 26  ? 43.22800 -17.47100 55.28000  1.000 67.66000  ? 358 ILE B O   1 
ATOM   542  C CB  . ILE B 2 26  ? 45.34700 -16.86800 53.17500  1.000 73.04000  ? 358 ILE B CB  1 
ATOM   543  C CG1 . ILE B 2 26  ? 46.19900 -17.02700 51.93000  1.000 73.54000  ? 358 ILE B CG1 1 
ATOM   544  C CG2 . ILE B 2 26  ? 46.20600 -16.46200 54.37700  1.000 69.42000  ? 358 ILE B CG2 1 
ATOM   545  C CD1 . ILE B 2 26  ? 46.49500 -15.74100 51.25300  1.000 71.49000  ? 358 ILE B CD1 1 
ATOM   546  N N   . SER B 2 27  ? 44.66500 -19.16000 55.67400  1.000 74.04000  ? 359 SER B N   1 
ATOM   547  C CA  . SER B 2 27  ? 44.34600 -19.23800 57.08100  1.000 74.08000  ? 359 SER B CA  1 
ATOM   548  C C   . SER B 2 27  ? 45.62100 -19.55800 57.83800  1.000 78.08000  ? 359 SER B C   1 
ATOM   549  O O   . SER B 2 27  ? 46.63500 -19.95600 57.25300  1.000 77.68000  ? 359 SER B O   1 
ATOM   550  C CB  . SER B 2 27  ? 43.25400 -20.27800 57.33900  1.000 78.01000  ? 359 SER B CB  1 
ATOM   551  O OG  . SER B 2 27  ? 43.70500 -21.57300 57.01000  1.000 77.83000  ? 359 SER B OG  1 
ATOM   552  N N   . ASN B 2 28  ? 45.56600 -19.34300 59.15000  1.000 84.16000  ? 360 ASN B N   1 
ATOM   553  C CA  . ASN B 2 28  ? 46.54900 -19.86300 60.09900  1.000 80.60000  ? 360 ASN B CA  1 
ATOM   554  C C   . ASN B 2 28  ? 47.98000 -19.52300 59.69200  1.000 79.19000  ? 360 ASN B C   1 
ATOM   555  O O   . ASN B 2 28  ? 48.78300 -20.39100 59.34800  1.000 81.71000  ? 360 ASN B O   1 
ATOM   556  C CB  . ASN B 2 28  ? 46.38200 -21.37200 60.26800  1.000 83.41000  ? 360 ASN B CB  1 
ATOM   557  C CG  . ASN B 2 28  ? 45.36000 -21.71700 61.33200  1.000 91.47000  ? 360 ASN B CG  1 
ATOM   558  O OD1 . ASN B 2 28  ? 45.63000 -21.60400 62.54600  1.000 87.12000  ? 360 ASN B OD1 1 
ATOM   559  N ND2 . ASN B 2 28  ? 44.15900 -22.11600 60.88500  1.000 87.03000  ? 360 ASN B ND2 1 
ATOM   560  N N   . CYS B 2 29  ? 48.28000 -18.23100 59.80100  1.000 75.66000  ? 361 CYS B N   1 
ATOM   561  C CA  . CYS B 2 29  ? 49.59200 -17.71300 59.44000  1.000 76.78000  ? 361 CYS B CA  1 
ATOM   562  C C   . CYS B 2 29  ? 49.66100 -16.23600 59.80900  1.000 77.99000  ? 361 CYS B C   1 
ATOM   563  O O   . CYS B 2 29  ? 48.65100 -15.62200 60.16900  1.000 78.88000  ? 361 CYS B O   1 
ATOM   564  C CB  . CYS B 2 29  ? 49.87000 -17.92900 57.94700  1.000 91.26000  ? 361 CYS B CB  1 
ATOM   565  S SG  . CYS B 2 29  ? 48.59900 -17.33000 56.80100  1.000 88.86000  ? 361 CYS B SG  1 
ATOM   566  N N   . VAL B 2 30  ? 50.87700 -15.67900 59.73300  1.000 79.54000  ? 362 VAL B N   1 
ATOM   567  C CA  . VAL B 2 30  ? 51.11200 -14.23800 59.82300  1.000 84.41000  ? 362 VAL B CA  1 
ATOM   568  C C   . VAL B 2 30  ? 51.67000 -13.73300 58.48900  1.000 89.40000  ? 362 VAL B C   1 
ATOM   569  O O   . VAL B 2 30  ? 52.22100 -14.49100 57.68100  1.000 90.00000  ? 362 VAL B O   1 
ATOM   570  C CB  . VAL B 2 30  ? 52.05900 -13.85400 60.98100  1.000 89.11000  ? 362 VAL B CB  1 
ATOM   571  C CG1 . VAL B 2 30  ? 51.65700 -14.57000 62.28100  1.000 86.16000  ? 362 VAL B CG1 1 
ATOM   572  C CG2 . VAL B 2 30  ? 53.50500 -14.13800 60.59700  1.000 91.66000  ? 362 VAL B CG2 1 
ATOM   573  N N   . ALA B 2 31  ? 51.51600 -12.43400 58.25100  1.000 90.51000  ? 363 ALA B N   1 
ATOM   574  C CA  . ALA B 2 31  ? 51.74500 -11.89400 56.91300  1.000 90.10000  ? 363 ALA B CA  1 
ATOM   575  C C   . ALA B 2 31  ? 52.31200 -10.48900 57.00700  1.000 93.88000  ? 363 ALA B C   1 
ATOM   576  O O   . ALA B 2 31  ? 51.59300 -9.54500  57.34200  1.000 99.14000  ? 363 ALA B O   1 
ATOM   577  C CB  . ALA B 2 31  ? 50.45400 -11.89400 56.10000  1.000 88.04000  ? 363 ALA B CB  1 
ATOM   578  N N   . ASP B 2 32  ? 53.58800 -10.34200 56.68200  1.000 90.72000  ? 364 ASP B N   1 
ATOM   579  C CA  . ASP B 2 32  ? 54.16200 -9.01400  56.53400  1.000 91.42000  ? 364 ASP B CA  1 
ATOM   580  C C   . ASP B 2 32  ? 53.53700 -8.37200  55.30600  1.000 93.41000  ? 364 ASP B C   1 
ATOM   581  O O   . ASP B 2 32  ? 53.95000 -8.62700  54.17100  1.000 93.15000  ? 364 ASP B O   1 
ATOM   582  C CB  . ASP B 2 32  ? 55.67500 -9.08800  56.40600  1.000 93.63000  ? 364 ASP B CB  1 
ATOM   583  C CG  . ASP B 2 32  ? 56.31100 -7.71800  56.35300  1.000 99.06000  ? 364 ASP B CG  1 
ATOM   584  O OD1 . ASP B 2 32  ? 55.56300 -6.71300  56.31400  1.000 98.04000  ? 364 ASP B OD1 1 
ATOM   585  O OD2 . ASP B 2 32  ? 57.55800 -7.64700  56.35600  1.000 100.85000 ? 364 ASP B OD2 1 
ATOM   586  N N   . TYR B 2 33  ? 52.53200 -7.53300  55.53100  1.000 92.03000  ? 365 TYR B N   1 
ATOM   587  C CA  . TYR B 2 33  ? 51.94000 -6.82200  54.40900  1.000 96.48000  ? 365 TYR B CA  1 
ATOM   588  C C   . TYR B 2 33  ? 52.85200 -5.72200  53.90600  1.000 99.44000  ? 365 TYR B C   1 
ATOM   589  O O   . TYR B 2 33  ? 52.92100 -5.49100  52.69700  1.000 102.15000 ? 365 TYR B O   1 
ATOM   590  C CB  . TYR B 2 33  ? 50.57900 -6.26000  54.79700  1.000 92.86000  ? 365 TYR B CB  1 
ATOM   591  C CG  . TYR B 2 33  ? 49.55500 -7.34900  54.82900  1.000 92.88000  ? 365 TYR B CG  1 
ATOM   592  C CD1 . TYR B 2 33  ? 49.08900 -7.91600  53.64200  1.000 92.64000  ? 365 TYR B CD1 1 
ATOM   593  C CD2 . TYR B 2 33  ? 49.09000 -7.85000  56.03200  1.000 90.30000  ? 365 TYR B CD2 1 
ATOM   594  C CE1 . TYR B 2 33  ? 48.16800 -8.93800  53.65600  1.000 91.25000  ? 365 TYR B CE1 1 
ATOM   595  C CE2 . TYR B 2 33  ? 48.16100 -8.86600  56.06500  1.000 94.31000  ? 365 TYR B CE2 1 
ATOM   596  C CZ  . TYR B 2 33  ? 47.70300 -9.40900  54.86800  1.000 95.36000  ? 365 TYR B CZ  1 
ATOM   597  O OH  . TYR B 2 33  ? 46.78000 -10.43000 54.87600  1.000 93.10000  ? 365 TYR B OH  1 
ATOM   598  N N   . SER B 2 34  ? 53.56900 -5.05100  54.81300  1.000 101.41000 ? 366 SER B N   1 
ATOM   599  C CA  . SER B 2 34  ? 54.48400 -3.99400  54.40600  1.000 101.03000 ? 366 SER B CA  1 
ATOM   600  C C   . SER B 2 34  ? 55.46500 -4.47700  53.34700  1.000 105.14000 ? 366 SER B C   1 
ATOM   601  O O   . SER B 2 34  ? 55.90300 -3.68200  52.51200  1.000 113.23000 ? 366 SER B O   1 
ATOM   602  C CB  . SER B 2 34  ? 55.22900 -3.46100  55.62300  1.000 107.62000 ? 366 SER B CB  1 
ATOM   603  O OG  . SER B 2 34  ? 54.31100 -2.84100  56.50000  1.000 109.58000 ? 366 SER B OG  1 
ATOM   604  N N   . VAL B 2 35  ? 55.80600 -5.77200  53.34700  1.000 101.85000 ? 367 VAL B N   1 
ATOM   605  C CA  . VAL B 2 35  ? 56.52400 -6.35800  52.21300  1.000 103.52000 ? 367 VAL B CA  1 
ATOM   606  C C   . VAL B 2 35  ? 55.77800 -6.09000  50.90800  1.000 104.96000 ? 367 VAL B C   1 
ATOM   607  O O   . VAL B 2 35  ? 56.35900 -5.62700  49.91900  1.000 107.62000 ? 367 VAL B O   1 
ATOM   608  C CB  . VAL B 2 35  ? 56.73100 -7.86800  52.42200  1.000 105.50000 ? 367 VAL B CB  1 
ATOM   609  C CG1 . VAL B 2 35  ? 56.99500 -8.56400  51.07200  1.000 107.03000 ? 367 VAL B CG1 1 
ATOM   610  C CG2 . VAL B 2 35  ? 57.87100 -8.12500  53.37400  1.000 103.14000 ? 367 VAL B CG2 1 
ATOM   611  N N   . LEU B 2 36  ? 54.48300 -6.39700  50.88000  1.000 102.32000 ? 368 LEU B N   1 
ATOM   612  C CA  . LEU B 2 36  ? 53.70200 -6.16800  49.67300  1.000 98.99000  ? 368 LEU B CA  1 
ATOM   613  C C   . LEU B 2 36  ? 53.63900 -4.68600  49.34400  1.000 104.67000 ? 368 LEU B C   1 
ATOM   614  O O   . LEU B 2 36  ? 54.00100 -4.26900  48.23900  1.000 104.20000 ? 368 LEU B O   1 
ATOM   615  C CB  . LEU B 2 36  ? 52.30200 -6.74500  49.84000  1.000 95.89000  ? 368 LEU B CB  1 
ATOM   616  C CG  . LEU B 2 36  ? 52.31200 -8.24200  50.13500  1.000 95.55000  ? 368 LEU B CG  1 
ATOM   617  C CD1 . LEU B 2 36  ? 50.90100 -8.80100  50.25000  1.000 91.20000  ? 368 LEU B CD1 1 
ATOM   618  C CD2 . LEU B 2 36  ? 53.10600 -8.97700  49.06900  1.000 93.65000  ? 368 LEU B CD2 1 
ATOM   619  N N   . TYR B 2 37  ? 53.19000 -3.86700  50.29800  1.000 101.76000 ? 369 TYR B N   1 
ATOM   620  C CA  . TYR B 2 37  ? 53.04800 -2.44300  50.01200  1.000 105.65000 ? 369 TYR B CA  1 
ATOM   621  C C   . TYR B 2 37  ? 54.38600 -1.80700  49.66100  1.000 112.65000 ? 369 TYR B C   1 
ATOM   622  O O   . TYR B 2 37  ? 54.43900 -0.88100  48.84200  1.000 112.69000 ? 369 TYR B O   1 
ATOM   623  C CB  . TYR B 2 37  ? 52.42200 -1.71700  51.19900  1.000 105.66000 ? 369 TYR B CB  1 
ATOM   624  C CG  . TYR B 2 37  ? 51.83300 -0.36500  50.84800  1.000 109.53000 ? 369 TYR B CG  1 
ATOM   625  C CD1 . TYR B 2 37  ? 52.64700 0.71000   50.49400  1.000 110.75000 ? 369 TYR B CD1 1 
ATOM   626  C CD2 . TYR B 2 37  ? 50.46100 -0.16300  50.87600  1.000 108.47000 ? 369 TYR B CD2 1 
ATOM   627  C CE1 . TYR B 2 37  ? 52.10800 1.94400   50.17300  1.000 111.44000 ? 369 TYR B CE1 1 
ATOM   628  C CE2 . TYR B 2 37  ? 49.91200 1.06900   50.56700  1.000 109.92000 ? 369 TYR B CE2 1 
ATOM   629  C CZ  . TYR B 2 37  ? 50.73500 2.12000   50.21500  1.000 113.81000 ? 369 TYR B CZ  1 
ATOM   630  O OH  . TYR B 2 37  ? 50.17600 3.34200   49.90100  1.000 116.49000 ? 369 TYR B OH  1 
ATOM   631  N N   . ASN B 2 38  ? 55.47700 -2.28400  50.25500  1.000 110.74000 ? 370 ASN B N   1 
ATOM   632  C CA  . ASN B 2 38  ? 56.77500 -1.65500  50.05800  1.000 112.29000 ? 370 ASN B CA  1 
ATOM   633  C C   . ASN B 2 38  ? 57.72300 -2.49300  49.20300  1.000 111.21000 ? 370 ASN B C   1 
ATOM   634  O O   . ASN B 2 38  ? 58.90500 -2.14600  49.08600  1.000 109.96000 ? 370 ASN B O   1 
ATOM   635  C CB  . ASN B 2 38  ? 57.40500 -1.31500  51.41400  1.000 113.96000 ? 370 ASN B CB  1 
ATOM   636  C CG  . ASN B 2 38  ? 56.49400 -0.44400  52.28100  1.000 109.85000 ? 370 ASN B CG  1 
ATOM   637  O OD1 . ASN B 2 38  ? 55.92800 0.54900   51.81200  1.000 112.92000 ? 370 ASN B OD1 1 
ATOM   638  N ND2 . ASN B 2 38  ? 56.34400 -0.82300  53.54800  1.000 111.07000 ? 370 ASN B ND2 1 
ATOM   639  N N   . SER B 2 39  ? 57.24100 -3.58400  48.59300  1.000 114.17000 ? 371 SER B N   1 
ATOM   640  C CA  . SER B 2 39  ? 57.90700 -4.08200  47.39200  1.000 114.74000 ? 371 SER B CA  1 
ATOM   641  C C   . SER B 2 39  ? 57.55500 -3.23700  46.17400  1.000 114.73000 ? 371 SER B C   1 
ATOM   642  O O   . SER B 2 39  ? 58.19000 -3.39600  45.12500  1.000 112.62000 ? 371 SER B O   1 
ATOM   643  C CB  . SER B 2 39  ? 57.56800 -5.55400  47.11900  1.000 111.08000 ? 371 SER B CB  1 
ATOM   644  O OG  . SER B 2 39  ? 58.43300 -6.09500  46.12600  1.000 108.75000 ? 371 SER B OG  1 
ATOM   645  N N   . ALA B 2 40  ? 56.53700 -2.37100  46.30400  1.000 115.02000 ? 372 ALA B N   1 
ATOM   646  C CA  . ALA B 2 40  ? 56.28200 -1.22300  45.42200  1.000 110.44000 ? 372 ALA B CA  1 
ATOM   647  C C   . ALA B 2 40  ? 56.44800 -1.56300  43.94600  1.000 113.70000 ? 372 ALA B C   1 
ATOM   648  O O   . ALA B 2 40  ? 56.97200 -0.75800  43.17200  1.000 115.54000 ? 372 ALA B O   1 
ATOM   649  C CB  . ALA B 2 40  ? 57.17300 -0.03200  45.79600  1.000 111.51000 ? 372 ALA B CB  1 
ATOM   650  N N   . SER B 2 41  ? 55.99900 -2.75600  43.54500  1.000 113.57000 ? 373 SER B N   1 
ATOM   651  C CA  . SER B 2 41  ? 55.99100 -3.18100  42.14600  1.000 111.33000 ? 373 SER B CA  1 
ATOM   652  C C   . SER B 2 41  ? 54.58700 -3.13600  41.53200  1.000 103.36000 ? 373 SER B C   1 
ATOM   653  O O   . SER B 2 41  ? 54.28400 -3.91600  40.62400  1.000 97.96000  ? 373 SER B O   1 
ATOM   654  C CB  . SER B 2 41  ? 56.56500 -4.59900  42.01100  1.000 111.90000 ? 373 SER B CB  1 
ATOM   655  O OG  . SER B 2 41  ? 57.73500 -4.79700  42.79000  1.000 112.83000 ? 373 SER B OG  1 
ATOM   656  N N   . PHE B 2 42  ? 53.71900 -2.24400  42.00900  1.000 101.25000 ? 374 PHE B N   1 
ATOM   657  C CA  . PHE B 2 42  ? 52.28100 -2.36800  41.80500  1.000 95.32000  ? 374 PHE B CA  1 
ATOM   658  C C   . PHE B 2 42  ? 51.72200 -1.10100  41.17600  1.000 92.75000  ? 374 PHE B C   1 
ATOM   659  O O   . PHE B 2 42  ? 51.70500 -0.04500  41.81300  1.000 94.48000  ? 374 PHE B O   1 
ATOM   660  C CB  . PHE B 2 42  ? 51.56600 -2.64700  43.13300  1.000 99.17000  ? 374 PHE B CB  1 
ATOM   661  C CG  . PHE B 2 42  ? 52.00900 -3.92100  43.81900  1.000 100.12000 ? 374 PHE B CG  1 
ATOM   662  C CD1 . PHE B 2 42  ? 52.39100 -5.03900  43.08000  1.000 100.95000 ? 374 PHE B CD1 1 
ATOM   663  C CD2 . PHE B 2 42  ? 52.03100 -4.00200  45.19800  1.000 92.62000  ? 374 PHE B CD2 1 
ATOM   664  C CE1 . PHE B 2 42  ? 52.78700 -6.20200  43.70700  1.000 97.30000  ? 374 PHE B CE1 1 
ATOM   665  C CE2 . PHE B 2 42  ? 52.42700 -5.16600  45.82800  1.000 99.27000  ? 374 PHE B CE2 1 
ATOM   666  C CZ  . PHE B 2 42  ? 52.80700 -6.26300  45.08400  1.000 91.94000  ? 374 PHE B CZ  1 
ATOM   667  N N   . SER B 2 43  ? 51.22200 -1.21500  39.94800  1.000 88.85000  ? 375 SER B N   1 
ATOM   668  C CA  . SER B 2 43  ? 50.53600 -0.08100  39.34900  1.000 87.62000  ? 375 SER B CA  1 
ATOM   669  C C   . SER B 2 43  ? 49.22500 0.24500   40.05100  1.000 91.71000  ? 375 SER B C   1 
ATOM   670  O O   . SER B 2 43  ? 48.64200 1.30100   39.77700  1.000 92.39000  ? 375 SER B O   1 
ATOM   671  C CB  . SER B 2 43  ? 50.29200 -0.34400  37.85700  1.000 88.23000  ? 375 SER B CB  1 
ATOM   672  O OG  . SER B 2 43  ? 49.51000 -1.50700  37.65000  1.000 90.61000  ? 375 SER B OG  1 
ATOM   673  N N   . THR B 2 44  ? 48.75300 -0.61900  40.95100  1.000 89.95000  ? 376 THR B N   1 
ATOM   674  C CA  . THR B 2 44  ? 47.52000 -0.38000  41.68700  1.000 89.13000  ? 376 THR B CA  1 
ATOM   675  C C   . THR B 2 44  ? 47.64300 -1.02700  43.05500  1.000 93.55000  ? 376 THR B C   1 
ATOM   676  O O   . THR B 2 44  ? 48.26900 -2.08000  43.19300  1.000 96.31000  ? 376 THR B O   1 
ATOM   677  C CB  . THR B 2 44  ? 46.29900 -0.95000  40.95200  1.000 91.06000  ? 376 THR B CB  1 
ATOM   678  O OG1 . THR B 2 44  ? 46.28600 -0.49100  39.58300  1.000 88.65000  ? 376 THR B OG1 1 
ATOM   679  C CG2 . THR B 2 44  ? 45.00900 -0.53200  41.66400  1.000 89.46000  ? 376 THR B CG2 1 
ATOM   680  N N   . PHE B 2 45  ? 47.06100 -0.37800  44.07100  1.000 92.03000  ? 377 PHE B N   1 
ATOM   681  C CA  . PHE B 2 45  ? 46.96200 -0.96000  45.40600  1.000 89.26000  ? 377 PHE B CA  1 
ATOM   682  C C   . PHE B 2 45  ? 45.76800 -0.37000  46.15700  1.000 91.35000  ? 377 PHE B C   1 
ATOM   683  O O   . PHE B 2 45  ? 45.90800 0.10100   47.28800  1.000 92.60000  ? 377 PHE B O   1 
ATOM   684  C CB  . PHE B 2 45  ? 48.26100 -0.74500  46.18900  1.000 95.74000  ? 377 PHE B CB  1 
ATOM   685  C CG  . PHE B 2 45  ? 48.54700 -1.81200  47.23500  1.000 94.54000  ? 377 PHE B CG  1 
ATOM   686  C CD1 . PHE B 2 45  ? 47.79000 -1.90200  48.39800  1.000 96.43000  ? 377 PHE B CD1 1 
ATOM   687  C CD2 . PHE B 2 45  ? 49.60400 -2.69700  47.06800  1.000 91.48000  ? 377 PHE B CD2 1 
ATOM   688  C CE1 . PHE B 2 45  ? 48.06500 -2.86600  49.35500  1.000 96.54000  ? 377 PHE B CE1 1 
ATOM   689  C CE2 . PHE B 2 45  ? 49.88900 -3.66200  48.02800  1.000 92.72000  ? 377 PHE B CE2 1 
ATOM   690  C CZ  . PHE B 2 45  ? 49.11700 -3.74700  49.16500  1.000 100.17000 ? 377 PHE B CZ  1 
ATOM   691  N N   . LYS B 2 46  ? 44.58800 -0.39800  45.53200  1.000 93.95000  ? 378 LYS B N   1 
ATOM   692  C CA  . LYS B 2 46  ? 43.36300 0.09200   46.16200  1.000 95.55000  ? 378 LYS B CA  1 
ATOM   693  C C   . LYS B 2 46  ? 42.89700 -0.86000  47.26500  1.000 92.58000  ? 378 LYS B C   1 
ATOM   694  O O   . LYS B 2 46  ? 42.76300 -2.06800  47.03500  1.000 89.26000  ? 378 LYS B O   1 
ATOM   695  C CB  . LYS B 2 46  ? 42.25900 0.25000   45.10400  1.000 99.41000  ? 378 LYS B CB  1 
ATOM   696  C CG  . LYS B 2 46  ? 41.76600 1.68600   44.84000  1.000 102.16000 ? 378 LYS B CG  1 
ATOM   697  C CD  . LYS B 2 46  ? 40.88600 2.23600   45.98500  1.000 98.18000  ? 378 LYS B CD  1 
ATOM   698  C CE  . LYS B 2 46  ? 40.07100 3.46900   45.53700  1.000 99.93000  ? 378 LYS B CE  1 
ATOM   699  N NZ  . LYS B 2 46  ? 39.19500 4.06100   46.59900  1.000 98.16000  ? 378 LYS B NZ  1 
ATOM   700  N N   . CYS B 2 47  ? 42.63300 -0.30700  48.46200  1.000 92.37000  ? 379 CYS B N   1 
ATOM   701  C CA  . CYS B 2 47  ? 42.09100 -1.03700  49.60700  1.000 85.38000  ? 379 CYS B CA  1 
ATOM   702  C C   . CYS B 2 47  ? 40.78600 -0.40000  50.06600  1.000 83.18000  ? 379 CYS B C   1 
ATOM   703  O O   . CYS B 2 47  ? 40.58700 0.80700   49.91400  1.000 83.70000  ? 379 CYS B O   1 
ATOM   704  C CB  . CYS B 2 47  ? 43.06500 -1.05100  50.77000  1.000 89.60000  ? 379 CYS B CB  1 
ATOM   705  S SG  . CYS B 2 47  ? 44.59200 -1.88500  50.41400  1.000 101.24000 ? 379 CYS B SG  1 
ATOM   706  N N   . TYR B 2 48  ? 39.89400 -1.21600  50.64000  1.000 81.33000  ? 380 TYR B N   1 
ATOM   707  C CA  . TYR B 2 48  ? 38.55200 -0.75300  50.97600  1.000 81.26000  ? 380 TYR B CA  1 
ATOM   708  C C   . TYR B 2 48  ? 38.14600 -1.27000  52.34500  1.000 84.30000  ? 380 TYR B C   1 
ATOM   709  O O   . TYR B 2 48  ? 38.52500 -2.37700  52.73700  1.000 90.83000  ? 380 TYR B O   1 
ATOM   710  C CB  . TYR B 2 48  ? 37.52300 -1.19700  49.93200  1.000 84.18000  ? 380 TYR B CB  1 
ATOM   711  C CG  . TYR B 2 48  ? 37.89800 -0.85000  48.51600  1.000 80.47000  ? 380 TYR B CG  1 
ATOM   712  C CD1 . TYR B 2 48  ? 38.80000 -1.62700  47.80500  1.000 82.86000  ? 380 TYR B CD1 1 
ATOM   713  C CD2 . TYR B 2 48  ? 37.33900 0.24000   47.87500  1.000 86.72000  ? 380 TYR B CD2 1 
ATOM   714  C CE1 . TYR B 2 48  ? 39.15200 -1.31300  46.49900  1.000 84.64000  ? 380 TYR B CE1 1 
ATOM   715  C CE2 . TYR B 2 48  ? 37.68400 0.55800   46.55600  1.000 87.96000  ? 380 TYR B CE2 1 
ATOM   716  C CZ  . TYR B 2 48  ? 38.59200 -0.22600  45.87500  1.000 84.45000  ? 380 TYR B CZ  1 
ATOM   717  O OH  . TYR B 2 48  ? 38.95000 0.07500   44.57100  1.000 87.15000  ? 380 TYR B OH  1 
ATOM   718  N N   . GLY B 2 49  ? 37.38500 -0.46400  53.07800  1.000 89.10000  ? 381 GLY B N   1 
ATOM   719  C CA  . GLY B 2 49  ? 37.02600 -0.82300  54.44100  1.000 89.41000  ? 381 GLY B CA  1 
ATOM   720  C C   . GLY B 2 49  ? 38.20400 -1.06700  55.37100  1.000 85.96000  ? 381 GLY B C   1 
ATOM   721  O O   . GLY B 2 49  ? 38.00900 -1.53000  56.49600  1.000 87.27000  ? 381 GLY B O   1 
ATOM   722  N N   . VAL B 2 50  ? 39.42300 -0.75500  54.92100  1.000 89.47000  ? 382 VAL B N   1 
ATOM   723  C CA  . VAL B 2 50  ? 40.64700 -0.98700  55.69500  1.000 87.00000  ? 382 VAL B CA  1 
ATOM   724  C C   . VAL B 2 50  ? 41.76000 -0.13800  55.08600  1.000 91.06000  ? 382 VAL B C   1 
ATOM   725  O O   . VAL B 2 50  ? 41.75400 0.14400   53.88200  1.000 86.25000  ? 382 VAL B O   1 
ATOM   726  C CB  . VAL B 2 50  ? 41.02400 -2.49100  55.70900  1.000 85.92000  ? 382 VAL B CB  1 
ATOM   727  C CG1 . VAL B 2 50  ? 41.36400 -2.97600  54.29100  1.000 84.30000  ? 382 VAL B CG1 1 
ATOM   728  C CG2 . VAL B 2 50  ? 42.17700 -2.75500  56.63800  1.000 83.66000  ? 382 VAL B CG2 1 
ATOM   729  N N   . SER B 2 51  ? 42.76600 0.29000   55.96300  1.000 88.02000  ? 383 SER B N   1 
ATOM   730  C CA  . SER B 2 51  ? 43.93700 1.10500   55.61100  1.000 91.12000  ? 383 SER B CA  1 
ATOM   731  C C   . SER B 2 51  ? 45.15300 0.22700   55.33000  1.000 92.59000  ? 383 SER B C   1 
ATOM   732  O O   . SER B 2 51  ? 45.56300 -0.55800  56.19500  1.000 94.04000  ? 383 SER B O   1 
ATOM   733  C CB  . SER B 2 51  ? 44.27100 2.09000   56.73100  1.000 97.30000  ? 383 SER B CB  1 
ATOM   734  O OG  . SER B 2 51  ? 45.22700 1.56700   57.64900  1.000 98.74000  ? 383 SER B OG  1 
ATOM   735  N N   . PRO B 2 52  ? 45.78900 0.37000   54.16200  1.000 97.78000  ? 384 PRO B N   1 
ATOM   736  C CA  . PRO B 2 52  ? 46.90600 -0.51900  53.78600  1.000 96.99000  ? 384 PRO B CA  1 
ATOM   737  C C   . PRO B 2 52  ? 48.14600 -0.37300  54.65100  1.000 96.56000  ? 384 PRO B C   1 
ATOM   738  O O   . PRO B 2 52  ? 49.16900 -1.01400  54.37400  1.000 95.06000  ? 384 PRO B O   1 
ATOM   739  C CB  . PRO B 2 52  ? 47.19800 -0.10500  52.33600  1.000 99.92000  ? 384 PRO B CB  1 
ATOM   740  C CG  . PRO B 2 52  ? 46.68600 1.30300   52.23700  1.000 98.35000  ? 384 PRO B CG  1 
ATOM   741  C CD  . PRO B 2 52  ? 45.48900 1.36800   53.12100  1.000 95.45000  ? 384 PRO B CD  1 
ATOM   742  N N   . THR B 2 53  ? 48.08700 0.44700   55.68600  1.000 96.35000  ? 385 THR B N   1 
ATOM   743  C CA  . THR B 2 53  ? 49.19900 0.63400   56.59800  1.000 100.62000 ? 385 THR B CA  1 
ATOM   744  C C   . THR B 2 53  ? 48.95300 -0.02300  57.94700  1.000 98.68000  ? 385 THR B C   1 
ATOM   745  O O   . THR B 2 53  ? 49.88200 -0.57400  58.54100  1.000 97.90000  ? 385 THR B O   1 
ATOM   746  C CB  . THR B 2 53  ? 49.44900 2.13000   56.76100  1.000 101.87000 ? 385 THR B CB  1 
ATOM   747  O OG1 . THR B 2 53  ? 48.18500 2.79300   56.89400  1.000 98.70000  ? 385 THR B OG1 1 
ATOM   748  C CG2 . THR B 2 53  ? 50.16700 2.66500   55.51900  1.000 96.03000  ? 385 THR B CG2 1 
ATOM   749  N N   . LYS B 2 54  ? 47.70800 0.00000   58.42300  1.000 96.84000  ? 386 LYS B N   1 
ATOM   750  C CA  . LYS B 2 54  ? 47.29200 -0.75400  59.60000  1.000 99.91000  ? 386 LYS B CA  1 
ATOM   751  C C   . LYS B 2 54  ? 47.01500 -2.22000  59.29700  1.000 99.68000  ? 386 LYS B C   1 
ATOM   752  O O   . LYS B 2 54  ? 46.45000 -2.91700  60.14700  1.000 99.77000  ? 386 LYS B O   1 
ATOM   753  C CB  . LYS B 2 54  ? 46.03800 -0.13000  60.21600  1.000 98.72000  ? 386 LYS B CB  1 
ATOM   754  C CG  . LYS B 2 54  ? 46.29000 0.81500   61.36700  1.000 100.57000 ? 386 LYS B CG  1 
ATOM   755  C CD  . LYS B 2 54  ? 45.26600 1.93100   61.34900  1.000 103.26000 ? 386 LYS B CD  1 
ATOM   756  C CE  . LYS B 2 54  ? 43.90200 1.39900   60.93500  1.000 102.94000 ? 386 LYS B CE  1 
ATOM   757  N NZ  . LYS B 2 54  ? 42.86300 2.47200   60.82700  1.000 102.93000 ? 386 LYS B NZ  1 
ATOM   758  N N   . LEU B 2 55  ? 47.37000 -2.71100  58.11200  1.000 94.78000  ? 387 LEU B N   1 
ATOM   759  C CA  . LEU B 2 55  ? 47.12700 -4.11800  57.82700  1.000 96.24000  ? 387 LEU B CA  1 
ATOM   760  C C   . LEU B 2 55  ? 47.95400 -5.00800  58.74100  1.000 98.96000  ? 387 LEU B C   1 
ATOM   761  O O   . LEU B 2 55  ? 47.47400 -6.05100  59.20400  1.000 100.18000 ? 387 LEU B O   1 
ATOM   762  C CB  . LEU B 2 55  ? 47.43500 -4.42600  56.36800  1.000 97.38000  ? 387 LEU B CB  1 
ATOM   763  C CG  . LEU B 2 55  ? 46.49900 -3.88100  55.29200  1.000 95.15000  ? 387 LEU B CG  1 
ATOM   764  C CD1 . LEU B 2 55  ? 47.05700 -4.31600  53.97700  1.000 88.37000  ? 387 LEU B CD1 1 
ATOM   765  C CD2 . LEU B 2 55  ? 45.07300 -4.38100  55.46900  1.000 90.77000  ? 387 LEU B CD2 1 
ATOM   766  N N   . ASN B 2 56  ? 49.20000 -4.61500  59.01100  1.000 100.50000 ? 388 ASN B N   1 
ATOM   767  C CA  . ASN B 2 56  ? 50.01700 -5.34900  59.96700  1.000 102.38000 ? 388 ASN B CA  1 
ATOM   768  C C   . ASN B 2 56  ? 49.38700 -5.38900  61.35500  1.000 102.56000 ? 388 ASN B C   1 
ATOM   769  O O   . ASN B 2 56  ? 49.63800 -6.33500  62.10900  1.000 101.94000 ? 388 ASN B O   1 
ATOM   770  C CB  . ASN B 2 56  ? 51.41400 -4.72800  60.04900  1.000 103.01000 ? 388 ASN B CB  1 
ATOM   771  C CG  . ASN B 2 56  ? 52.24900 -4.99700  58.81400  1.000 103.85000 ? 388 ASN B CG  1 
ATOM   772  O OD1 . ASN B 2 56  ? 51.94800 -5.89400  58.03600  1.000 104.65000 ? 388 ASN B OD1 1 
ATOM   773  N ND2 . ASN B 2 56  ? 53.31200 -4.22200  58.63300  1.000 107.79000 ? 388 ASN B ND2 1 
ATOM   774  N N   . ASP B 2 57  ? 48.57000 -4.39400  61.71000  1.000 103.29000 ? 389 ASP B N   1 
ATOM   775  C CA  . ASP B 2 57  ? 48.01900 -4.33700  63.06300  1.000 103.04000 ? 389 ASP B CA  1 
ATOM   776  C C   . ASP B 2 57  ? 46.81400 -5.25200  63.23700  1.000 95.91000  ? 389 ASP B C   1 
ATOM   777  O O   . ASP B 2 57  ? 46.51300 -5.66700  64.36200  1.000 99.10000  ? 389 ASP B O   1 
ATOM   778  C CB  . ASP B 2 57  ? 47.60800 -2.90000  63.42300  1.000 104.20000 ? 389 ASP B CB  1 
ATOM   779  C CG  . ASP B 2 57  ? 48.73600 -1.88000  63.23400  1.000 107.12000 ? 389 ASP B CG  1 
ATOM   780  O OD1 . ASP B 2 57  ? 49.90000 -2.28700  62.99400  1.000 105.37000 ? 389 ASP B OD1 1 
ATOM   781  O OD2 . ASP B 2 57  ? 48.43800 -0.66100  63.32600  1.000 102.75000 ? 389 ASP B OD2 1 
ATOM   782  N N   . LEU B 2 58  ? 46.12000 -5.57000  62.15400  1.000 91.51000  ? 390 LEU B N   1 
ATOM   783  C CA  . LEU B 2 58  ? 44.82500 -6.22100  62.21600  1.000 87.24000  ? 390 LEU B CA  1 
ATOM   784  C C   . LEU B 2 58  ? 44.97000 -7.73500  62.09500  1.000 85.27000  ? 390 LEU B C   1 
ATOM   785  O O   . LEU B 2 58  ? 46.03800 -8.26200  61.78000  1.000 82.33000  ? 390 LEU B O   1 
ATOM   786  C CB  . LEU B 2 58  ? 43.91600 -5.66300  61.12100  1.000 87.63000  ? 390 LEU B CB  1 
ATOM   787  C CG  . LEU B 2 58  ? 43.56100 -4.18900  61.33200  1.000 91.00000  ? 390 LEU B CG  1 
ATOM   788  C CD1 . LEU B 2 58  ? 43.38000 -3.43200  60.02700  1.000 87.90000  ? 390 LEU B CD1 1 
ATOM   789  C CD2 . LEU B 2 58  ? 42.30500 -4.08200  62.18600  1.000 90.42000  ? 390 LEU B CD2 1 
ATOM   790  N N   . CYS B 2 59  ? 43.87300 -8.43500  62.40200  1.000 84.28000  ? 391 CYS B N   1 
ATOM   791  C CA  . CYS B 2 59  ? 43.72700 -9.87100  62.19500  1.000 86.18000  ? 391 CYS B CA  1 
ATOM   792  C C   . CYS B 2 59  ? 42.36200 -10.13400 61.57200  1.000 84.44000  ? 391 CYS B C   1 
ATOM   793  O O   . CYS B 2 59  ? 41.44100 -9.32900  61.70600  1.000 83.72000  ? 391 CYS B O   1 
ATOM   794  C CB  . CYS B 2 59  ? 43.82900 -10.69100 63.49400  1.000 82.68000  ? 391 CYS B CB  1 
ATOM   795  S SG  . CYS B 2 59  ? 45.37800 -10.63300 64.45900  1.000 103.71000 ? 391 CYS B SG  1 
ATOM   796  N N   . PHE B 2 60  ? 42.23100 -11.27200 60.89100  1.000 83.18000  ? 392 PHE B N   1 
ATOM   797  C CA  . PHE B 2 60  ? 40.97000 -11.63600 60.26400  1.000 82.66000  ? 392 PHE B CA  1 
ATOM   798  C C   . PHE B 2 60  ? 40.71800 -13.13500 60.41500  1.000 83.43000  ? 392 PHE B C   1 
ATOM   799  O O   . PHE B 2 60  ? 41.65900 -13.93600 60.49600  1.000 84.92000  ? 392 PHE B O   1 
ATOM   800  C CB  . PHE B 2 60  ? 40.95600 -11.22100 58.77700  1.000 79.33000  ? 392 PHE B CB  1 
ATOM   801  C CG  . PHE B 2 60  ? 41.19100 -9.74500  58.55500  1.000 77.89000  ? 392 PHE B CG  1 
ATOM   802  C CD1 . PHE B 2 60  ? 42.48100 -9.23800  58.46500  1.000 78.10000  ? 392 PHE B CD1 1 
ATOM   803  C CD2 . PHE B 2 60  ? 40.12400 -8.86800  58.44000  1.000 77.89000  ? 392 PHE B CD2 1 
ATOM   804  C CE1 . PHE B 2 60  ? 42.70700 -7.88800  58.27100  1.000 74.15000  ? 392 PHE B CE1 1 
ATOM   805  C CE2 . PHE B 2 60  ? 40.34400 -7.51400  58.23800  1.000 80.75000  ? 392 PHE B CE2 1 
ATOM   806  C CZ  . PHE B 2 60  ? 41.64000 -7.02700  58.15200  1.000 77.24000  ? 392 PHE B CZ  1 
ATOM   807  N N   . THR B 2 61  ? 39.42600 -13.49000 60.49000  1.000 81.22000  ? 393 THR B N   1 
ATOM   808  C CA  . THR B 2 61  ? 38.98200 -14.88200 60.40600  1.000 80.58000  ? 393 THR B CA  1 
ATOM   809  C C   . THR B 2 61  ? 39.61700 -15.61500 59.23200  1.000 78.36000  ? 393 THR B C   1 
ATOM   810  O O   . THR B 2 61  ? 40.29000 -16.63900 59.40300  1.000 74.73000  ? 393 THR B O   1 
ATOM   811  C CB  . THR B 2 61  ? 37.46500 -14.94900 60.23600  1.000 82.53000  ? 393 THR B CB  1 
ATOM   812  O OG1 . THR B 2 61  ? 36.79200 -14.43200 61.39200  1.000 79.90000  ? 393 THR B OG1 1 
ATOM   813  C CG2 . THR B 2 61  ? 37.04300 -16.38800 59.94300  1.000 76.76000  ? 393 THR B CG2 1 
ATOM   814  N N   . ASN B 2 62  ? 39.35400 -15.13700 58.01500  1.000 81.76000  ? 394 ASN B N   1 
ATOM   815  C CA  . ASN B 2 62  ? 39.79300 -15.80700 56.79500  1.000 79.30000  ? 394 ASN B CA  1 
ATOM   816  C C   . ASN B 2 62  ? 40.30000 -14.78500 55.79800  1.000 73.24000  ? 394 ASN B C   1 
ATOM   817  O O   . ASN B 2 62  ? 39.86300 -13.63400 55.78100  1.000 75.68000  ? 394 ASN B O   1 
ATOM   818  C CB  . ASN B 2 62  ? 38.67500 -16.62400 56.12800  1.000 76.18000  ? 394 ASN B CB  1 
ATOM   819  C CG  . ASN B 2 62  ? 39.17400 -17.94600 55.58800  1.000 73.39000  ? 394 ASN B CG  1 
ATOM   820  O OD1 . ASN B 2 62  ? 38.44300 -18.67300 54.89400  1.000 84.55000  ? 394 ASN B OD1 1 
ATOM   821  N ND2 . ASN B 2 62  ? 40.42600 -18.26600 55.88800  1.000 64.86000  ? 394 ASN B ND2 1 
ATOM   822  N N   . VAL B 2 63  ? 41.23200 -15.22500 54.97100  1.000 68.04000  ? 395 VAL B N   1 
ATOM   823  C CA  . VAL B 2 63  ? 41.66000 -14.46800 53.80800  1.000 73.51000  ? 395 VAL B CA  1 
ATOM   824  C C   . VAL B 2 63  ? 41.52400 -15.34900 52.58100  1.000 70.01000  ? 395 VAL B C   1 
ATOM   825  O O   . VAL B 2 63  ? 41.92300 -16.52200 52.60300  1.000 68.74000  ? 395 VAL B O   1 
ATOM   826  C CB  . VAL B 2 63  ? 43.10900 -13.98100 53.94400  1.000 72.20000  ? 395 VAL B CB  1 
ATOM   827  C CG1 . VAL B 2 63  ? 43.58500 -13.40400 52.62200  1.000 74.78000  ? 395 VAL B CG1 1 
ATOM   828  C CG2 . VAL B 2 63  ? 43.18900 -12.96600 55.03100  1.000 81.48000  ? 395 VAL B CG2 1 
ATOM   829  N N   . TYR B 2 64  ? 40.95300 -14.78100 51.52600  1.000 69.90000  ? 396 TYR B N   1 
ATOM   830  C CA  . TYR B 2 64  ? 41.00000 -15.31900 50.17500  1.000 68.99000  ? 396 TYR B CA  1 
ATOM   831  C C   . TYR B 2 64  ? 41.87300 -14.41200 49.32400  1.000 68.73000  ? 396 TYR B C   1 
ATOM   832  O O   . TYR B 2 64  ? 41.87500 -13.19300 49.51500  1.000 74.85000  ? 396 TYR B O   1 
ATOM   833  C CB  . TYR B 2 64  ? 39.61700 -15.36200 49.54900  1.000 61.10000  ? 396 TYR B CB  1 
ATOM   834  C CG  . TYR B 2 64  ? 38.62500 -16.27400 50.19100  1.000 63.25000  ? 396 TYR B CG  1 
ATOM   835  C CD1 . TYR B 2 64  ? 38.82700 -17.64800 50.22800  1.000 65.06000  ? 396 TYR B CD1 1 
ATOM   836  C CD2 . TYR B 2 64  ? 37.44900 -15.76500 50.71900  1.000 62.29000  ? 396 TYR B CD2 1 
ATOM   837  C CE1 . TYR B 2 64  ? 37.88900 -18.48900 50.79700  1.000 67.48000  ? 396 TYR B CE1 1 
ATOM   838  C CE2 . TYR B 2 64  ? 36.50400 -16.59500 51.28500  1.000 64.92000  ? 396 TYR B CE2 1 
ATOM   839  C CZ  . TYR B 2 64  ? 36.72900 -17.95900 51.32200  1.000 72.97000  ? 396 TYR B CZ  1 
ATOM   840  O OH  . TYR B 2 64  ? 35.78200 -18.78600 51.89700  1.000 87.71000  ? 396 TYR B OH  1 
ATOM   841  N N   . ALA B 2 65  ? 42.58900 -15.00600 48.37200  1.000 65.62000  ? 397 ALA B N   1 
ATOM   842  C CA  . ALA B 2 65  ? 43.43400 -14.28900 47.41500  1.000 68.98000  ? 397 ALA B CA  1 
ATOM   843  C C   . ALA B 2 65  ? 42.95400 -14.67900 46.01800  1.000 74.72000  ? 397 ALA B C   1 
ATOM   844  O O   . ALA B 2 65  ? 43.20900 -15.79000 45.55000  1.000 70.89000  ? 397 ALA B O   1 
ATOM   845  C CB  . ALA B 2 65  ? 44.92000 -14.61300 47.60100  1.000 63.76000  ? 397 ALA B CB  1 
ATOM   846  N N   . ASP B 2 66  ? 42.24800 -13.77900 45.35100  1.000 74.46000  ? 398 ASP B N   1 
ATOM   847  C CA  . ASP B 2 66  ? 41.73700 -14.04600 44.01600  1.000 74.50000  ? 398 ASP B CA  1 
ATOM   848  C C   . ASP B 2 66  ? 42.67200 -13.40400 42.98700  1.000 71.56000  ? 398 ASP B C   1 
ATOM   849  O O   . ASP B 2 66  ? 43.07900 -12.25400 43.15200  1.000 78.16000  ? 398 ASP B O   1 
ATOM   850  C CB  . ASP B 2 66  ? 40.29600 -13.53100 43.89500  1.000 72.37000  ? 398 ASP B CB  1 
ATOM   851  C CG  . ASP B 2 66  ? 39.33500 -14.22800 44.87900  1.000 75.43000  ? 398 ASP B CG  1 
ATOM   852  O OD1 . ASP B 2 66  ? 39.62000 -15.36700 45.30600  1.000 76.08000  ? 398 ASP B OD1 1 
ATOM   853  O OD2 . ASP B 2 66  ? 38.29000 -13.64700 45.23100  1.000 77.85000  ? 398 ASP B OD2 1 
ATOM   854  N N   . SER B 2 67  ? 43.04800 -14.15700 41.96000  1.000 69.43000  ? 399 SER B N   1 
ATOM   855  C CA  . SER B 2 67  ? 44.04900 -13.70300 41.00600  1.000 75.18000  ? 399 SER B CA  1 
ATOM   856  C C   . SER B 2 67  ? 43.63400 -14.06200 39.58300  1.000 70.29000  ? 399 SER B C   1 
ATOM   857  O O   . SER B 2 67  ? 42.86900 -15.00300 39.37600  1.000 72.76000  ? 399 SER B O   1 
ATOM   858  C CB  . SER B 2 67  ? 45.41500 -14.29700 41.31900  1.000 67.04000  ? 399 SER B CB  1 
ATOM   859  O OG  . SER B 2 67  ? 45.30100 -15.63000 41.76100  1.000 74.76000  ? 399 SER B OG  1 
ATOM   860  N N   . PHE B 2 68  ? 44.14900 -13.30000 38.60800  1.000 70.60000  ? 400 PHE B N   1 
ATOM   861  C CA  . PHE B 2 68  ? 43.79400 -13.40500 37.18400  1.000 73.34000  ? 400 PHE B CA  1 
ATOM   862  C C   . PHE B 2 68  ? 44.50700 -12.30900 36.40200  1.000 74.01000  ? 400 PHE B C   1 
ATOM   863  O O   . PHE B 2 68  ? 45.11900 -11.40700 36.97700  1.000 80.37000  ? 400 PHE B O   1 
ATOM   864  C CB  . PHE B 2 68  ? 42.30500 -13.26300 36.94200  1.000 68.62000  ? 400 PHE B CB  1 
ATOM   865  C CG  . PHE B 2 68  ? 41.71100 -12.02600 37.57600  1.000 74.70000  ? 400 PHE B CG  1 
ATOM   866  C CD1 . PHE B 2 68  ? 41.77400 -10.79400 36.94200  1.000 72.37000  ? 400 PHE B CD1 1 
ATOM   867  C CD2 . PHE B 2 68  ? 41.10000 -12.09400 38.82100  1.000 70.75000  ? 400 PHE B CD2 1 
ATOM   868  C CE1 . PHE B 2 68  ? 41.22600 -9.66700  37.53700  1.000 70.09000  ? 400 PHE B CE1 1 
ATOM   869  C CE2 . PHE B 2 68  ? 40.54500 -10.96900 39.40000  1.000 67.82000  ? 400 PHE B CE2 1 
ATOM   870  C CZ  . PHE B 2 68  ? 40.61000 -9.76200  38.76100  1.000 70.86000  ? 400 PHE B CZ  1 
ATOM   871  N N   . VAL B 2 69  ? 44.36700 -12.36900 35.07600  1.000 74.45000  ? 401 VAL B N   1 
ATOM   872  C CA  . VAL B 2 69  ? 44.94100 -11.39600 34.14400  1.000 74.85000  ? 401 VAL B CA  1 
ATOM   873  C C   . VAL B 2 69  ? 43.82500 -10.61000 33.47200  1.000 74.76000  ? 401 VAL B C   1 
ATOM   874  O O   . VAL B 2 69  ? 42.80000 -11.18400 33.09000  1.000 71.22000  ? 401 VAL B O   1 
ATOM   875  C CB  . VAL B 2 69  ? 45.82100 -12.08800 33.08600  1.000 74.69000  ? 401 VAL B CB  1 
ATOM   876  C CG1 . VAL B 2 69  ? 45.89800 -11.25200 31.81600  1.000 75.16000  ? 401 VAL B CG1 1 
ATOM   877  C CG2 . VAL B 2 69  ? 47.22700 -12.34600 33.64800  1.000 78.41000  ? 401 VAL B CG2 1 
ATOM   878  N N   . ILE B 2 70  ? 44.01600 -9.29300  33.35100  1.000 75.92000  ? 402 ILE B N   1 
ATOM   879  C CA  . ILE B 2 70  ? 43.19800 -8.44100  32.48500  1.000 81.19000  ? 402 ILE B CA  1 
ATOM   880  C C   . ILE B 2 70  ? 44.07500 -7.35400  31.86400  1.000 81.93000  ? 402 ILE B C   1 
ATOM   881  O O   . ILE B 2 70  ? 45.12400 -6.98500  32.40000  1.000 80.22000  ? 402 ILE B O   1 
ATOM   882  C CB  . ILE B 2 70  ? 42.02700 -7.77300  33.23500  1.000 72.14000  ? 402 ILE B CB  1 
ATOM   883  C CG1 . ILE B 2 70  ? 42.53700 -7.17800  34.53900  1.000 71.18000  ? 402 ILE B CG1 1 
ATOM   884  C CG2 . ILE B 2 70  ? 40.91400 -8.76300  33.45600  1.000 70.66000  ? 402 ILE B CG2 1 
ATOM   885  C CD1 . ILE B 2 70  ? 41.56500 -6.26100  35.21800  1.000 74.04000  ? 402 ILE B CD1 1 
ATOM   886  N N   . ARG B 2 71  ? 43.63000 -6.81800  30.72500  1.000 82.79000  ? 403 ARG B N   1 
ATOM   887  C CA  . ARG B 2 71  ? 44.31300 -5.64300  30.19700  1.000 87.53000  ? 403 ARG B CA  1 
ATOM   888  C C   . ARG B 2 71  ? 44.15400 -4.45500  31.15600  1.000 87.69000  ? 403 ARG B C   1 
ATOM   889  O O   . ARG B 2 71  ? 43.33900 -4.46500  32.09200  1.000 77.76000  ? 403 ARG B O   1 
ATOM   890  C CB  . ARG B 2 71  ? 43.82300 -5.28600  28.79200  1.000 73.07000  ? 403 ARG B CB  1 
ATOM   891  C CG  . ARG B 2 71  ? 42.36300 -5.40900  28.57600  1.000 77.33000  ? 403 ARG B CG  1 
ATOM   892  C CD  . ARG B 2 71  ? 42.00600 -5.03800  27.15500  1.000 78.62000  ? 403 ARG B CD  1 
ATOM   893  N NE  . ARG B 2 71  ? 41.40100 -3.71100  27.09500  1.000 82.10000  ? 403 ARG B NE  1 
ATOM   894  C CZ  . ARG B 2 71  ? 40.18700 -3.46300  26.61300  1.000 80.49000  ? 403 ARG B CZ  1 
ATOM   895  N NH1 . ARG B 2 71  ? 39.44900 -4.44900  26.11300  1.000 80.68000  ? 403 ARG B NH1 1 
ATOM   896  N NH2 . ARG B 2 71  ? 39.72100 -2.22000  26.60900  1.000 78.13000  ? 403 ARG B NH2 1 
ATOM   897  N N   . GLY B 2 72  ? 44.96600 -3.42300  30.90900  1.000 86.99000  ? 404 GLY B N   1 
ATOM   898  C CA  . GLY B 2 72  ? 45.12700 -2.36100  31.89000  1.000 81.20000  ? 404 GLY B CA  1 
ATOM   899  C C   . GLY B 2 72  ? 43.92300 -1.44600  31.99800  1.000 83.62000  ? 404 GLY B C   1 
ATOM   900  O O   . GLY B 2 72  ? 43.63800 -0.92000  33.08000  1.000 84.09000  ? 404 GLY B O   1 
ATOM   901  N N   . ASP B 2 73  ? 43.21300 -1.22300  30.88100  1.000 83.81000  ? 405 ASP B N   1 
ATOM   902  C CA  . ASP B 2 73  ? 42.00000 -0.40600  30.92300  1.000 85.32000  ? 405 ASP B CA  1 
ATOM   903  C C   . ASP B 2 73  ? 41.05400 -0.90700  31.99900  1.000 85.04000  ? 405 ASP B C   1 
ATOM   904  O O   . ASP B 2 73  ? 40.52600 -0.12700  32.79900  1.000 79.59000  ? 405 ASP B O   1 
ATOM   905  C CB  . ASP B 2 73  ? 41.25500 -0.43200  29.58100  1.000 86.39000  ? 405 ASP B CB  1 
ATOM   906  C CG  . ASP B 2 73  ? 42.16600 -0.38100  28.38600  1.000 91.55000  ? 405 ASP B CG  1 
ATOM   907  O OD1 . ASP B 2 73  ? 43.00500 0.54700   28.30700  1.000 94.89000  ? 405 ASP B OD1 1 
ATOM   908  O OD2 . ASP B 2 73  ? 42.02600 -1.28000  27.52200  1.000 86.26000  ? 405 ASP B OD2 1 
ATOM   909  N N   . GLU B 2 74  ? 40.83100 -2.22500  32.01300  1.000 87.10000  ? 406 GLU B N   1 
ATOM   910  C CA  . GLU B 2 74  ? 39.78600 -2.89100  32.77600  1.000 81.11000  ? 406 GLU B CA  1 
ATOM   911  C C   . GLU B 2 74  ? 40.11500 -2.96600  34.25400  1.000 77.30000  ? 406 GLU B C   1 
ATOM   912  O O   . GLU B 2 74  ? 39.22700 -3.27100  35.06500  1.000 82.69000  ? 406 GLU B O   1 
ATOM   913  C CB  . GLU B 2 74  ? 39.55100 -4.29200  32.17900  1.000 79.21000  ? 406 GLU B CB  1 
ATOM   914  C CG  . GLU B 2 74  ? 39.02700 -4.27700  30.73300  1.000 75.35000  ? 406 GLU B CG  1 
ATOM   915  C CD  . GLU B 2 74  ? 39.25400 -5.59100  29.94700  1.000 78.94000  ? 406 GLU B CD  1 
ATOM   916  O OE1 . GLU B 2 74  ? 40.05600 -6.44700  30.37400  1.000 76.35000  ? 406 GLU B OE1 1 
ATOM   917  O OE2 . GLU B 2 74  ? 38.63300 -5.76400  28.86600  1.000 81.55000  ? 406 GLU B OE2 1 
ATOM   918  N N   . VAL B 2 75  ? 41.34900 -2.65700  34.63500  1.000 79.19000  ? 407 VAL B N   1 
ATOM   919  C CA  . VAL B 2 75  ? 41.70200 -2.68000  36.04900  1.000 75.91000  ? 407 VAL B CA  1 
ATOM   920  C C   . VAL B 2 75  ? 40.80700 -1.74600  36.85800  1.000 76.70000  ? 407 VAL B C   1 
ATOM   921  O O   . VAL B 2 75  ? 40.46700 -2.05000  38.00400  1.000 80.37000  ? 407 VAL B O   1 
ATOM   922  C CB  . VAL B 2 75  ? 43.19800 -2.35200  36.21400  1.000 76.64000  ? 407 VAL B CB  1 
ATOM   923  C CG1 . VAL B 2 75  ? 43.54500 -2.16700  37.66200  1.000 76.02000  ? 407 VAL B CG1 1 
ATOM   924  C CG2 . VAL B 2 75  ? 44.04000 -3.46700  35.62300  1.000 73.96000  ? 407 VAL B CG2 1 
ATOM   925  N N   . ARG B 2 76  ? 40.36500 -0.62600  36.27600  1.000 80.50000  ? 408 ARG B N   1 
ATOM   926  C CA  . ARG B 2 76  ? 39.43700 0.24500   36.99900  1.000 82.31000  ? 408 ARG B CA  1 
ATOM   927  C C   . ARG B 2 76  ? 38.18600 -0.49200  37.47100  1.000 81.15000  ? 408 ARG B C   1 
ATOM   928  O O   . ARG B 2 76  ? 37.57600 -0.07900  38.46200  1.000 78.20000  ? 408 ARG B O   1 
ATOM   929  C CB  . ARG B 2 76  ? 39.02100 1.45200   36.13800  1.000 86.25000  ? 408 ARG B CB  1 
ATOM   930  C CG  . ARG B 2 76  ? 38.22500 1.11200   34.87000  1.000 89.05000  ? 408 ARG B CG  1 
ATOM   931  C CD  . ARG B 2 76  ? 37.30400 2.25800   34.40300  1.000 90.11000  ? 408 ARG B CD  1 
ATOM   932  N NE  . ARG B 2 76  ? 38.01000 3.28600   33.64100  1.000 93.93000  ? 408 ARG B NE  1 
ATOM   933  C CZ  . ARG B 2 76  ? 37.47000 4.44500   33.26500  1.000 99.43000  ? 408 ARG B CZ  1 
ATOM   934  N NH1 . ARG B 2 76  ? 36.21200 4.73800   33.59200  1.000 93.74000  ? 408 ARG B NH1 1 
ATOM   935  N NH2 . ARG B 2 76  ? 38.19300 5.31800   32.56800  1.000 94.43000  ? 408 ARG B NH2 1 
ATOM   936  N N   . GLN B 2 77  ? 37.79500 -1.58100  36.79200  1.000 83.06000  ? 409 GLN B N   1 
ATOM   937  C CA  . GLN B 2 77  ? 36.54300 -2.26100  37.11500  1.000 77.66000  ? 409 GLN B CA  1 
ATOM   938  C C   . GLN B 2 77  ? 36.67500 -3.20000  38.31100  1.000 76.75000  ? 409 GLN B C   1 
ATOM   939  O O   . GLN B 2 77  ? 35.65400 -3.60300  38.87500  1.000 75.25000  ? 409 GLN B O   1 
ATOM   940  C CB  . GLN B 2 77  ? 36.03500 -3.02600  35.89100  1.000 71.44000  ? 409 GLN B CB  1 
ATOM   941  C CG  . GLN B 2 77  ? 35.78300 -2.11700  34.68400  1.000 78.21000  ? 409 GLN B CG  1 
ATOM   942  C CD  . GLN B 2 77  ? 35.46300 -2.87200  33.38200  1.000 70.98000  ? 409 GLN B CD  1 
ATOM   943  O OE1 . GLN B 2 77  ? 34.92300 -3.97200  33.40000  1.000 66.92000  ? 409 GLN B OE1 1 
ATOM   944  N NE2 . GLN B 2 77  ? 35.80000 -2.26700  32.25500  1.000 73.01000  ? 409 GLN B NE2 1 
ATOM   945  N N   . ILE B 2 78  ? 37.90000 -3.54100  38.71700  1.000 75.35000  ? 410 ILE B N   1 
ATOM   946  C CA  . ILE B 2 78  ? 38.11900 -4.43900  39.84600  1.000 77.45000  ? 410 ILE B CA  1 
ATOM   947  C C   . ILE B 2 78  ? 38.07000 -3.59500  41.11000  1.000 77.03000  ? 410 ILE B C   1 
ATOM   948  O O   . ILE B 2 78  ? 39.04100 -3.51000  41.87300  1.000 71.55000  ? 410 ILE B O   1 
ATOM   949  C CB  . ILE B 2 78  ? 39.44500 -5.21000  39.71200  1.000 76.46000  ? 410 ILE B CB  1 
ATOM   950  C CG1 . ILE B 2 78  ? 39.56500 -5.80700  38.31100  1.000 68.69000  ? 410 ILE B CG1 1 
ATOM   951  C CG2 . ILE B 2 78  ? 39.53000 -6.33100  40.73600  1.000 70.31000  ? 410 ILE B CG2 1 
ATOM   952  C CD1 . ILE B 2 78  ? 38.50300 -6.85500  38.01600  1.000 66.38000  ? 410 ILE B CD1 1 
ATOM   953  N N   . ALA B 2 79  ? 36.93600 -2.94100  41.31100  1.000 75.35000  ? 411 ALA B N   1 
ATOM   954  C CA  . ALA B 2 79  ? 36.67600 -2.12200  42.47200  1.000 76.01000  ? 411 ALA B CA  1 
ATOM   955  C C   . ALA B 2 79  ? 35.17300 -2.18800  42.69700  1.000 76.49000  ? 411 ALA B C   1 
ATOM   956  O O   . ALA B 2 79  ? 34.42600 -2.31200  41.73000  1.000 82.03000  ? 411 ALA B O   1 
ATOM   957  C CB  . ALA B 2 79  ? 37.12400 -0.67200  42.26600  1.000 76.92000  ? 411 ALA B CB  1 
ATOM   958  N N   . PRO B 2 80  ? 34.74100 -2.16100  43.94900  1.000 76.81000  ? 412 PRO B N   1 
ATOM   959  C CA  . PRO B 2 80  ? 33.29800 -2.13700  44.24600  1.000 77.69000  ? 412 PRO B CA  1 
ATOM   960  C C   . PRO B 2 80  ? 32.51600 -1.21400  43.33700  1.000 76.38000  ? 412 PRO B C   1 
ATOM   961  O O   . PRO B 2 80  ? 33.03900 -0.20900  42.84200  1.000 79.39000  ? 412 PRO B O   1 
ATOM   962  C CB  . PRO B 2 80  ? 33.24700 -1.61900  45.69300  1.000 71.89000  ? 412 PRO B CB  1 
ATOM   963  C CG  . PRO B 2 80  ? 34.58500 -1.89600  46.24900  1.000 75.89000  ? 412 PRO B CG  1 
ATOM   964  C CD  . PRO B 2 80  ? 35.57400 -1.95700  45.13800  1.000 75.11000  ? 412 PRO B CD  1 
ATOM   965  N N   . GLY B 2 81  ? 31.25100 -1.54000  43.12700  1.000 75.72000  ? 413 GLY B N   1 
ATOM   966  C CA  . GLY B 2 81  ? 30.35000 -0.62900  42.46400  1.000 77.44000  ? 413 GLY B CA  1 
ATOM   967  C C   . GLY B 2 81  ? 30.55600 -0.43500  40.97700  1.000 81.12000  ? 413 GLY B C   1 
ATOM   968  O O   . GLY B 2 81  ? 29.77800 0.30300   40.36600  1.000 84.25000  ? 413 GLY B O   1 
ATOM   969  N N   . GLN B 2 82  ? 31.54800 -1.07400  40.36300  1.000 81.66000  ? 414 GLN B N   1 
ATOM   970  C CA  . GLN B 2 82  ? 31.88000 -0.79500  38.96800  1.000 75.15000  ? 414 GLN B CA  1 
ATOM   971  C C   . GLN B 2 82  ? 31.04100 -1.62800  38.00200  1.000 76.17000  ? 414 GLN B C   1 
ATOM   972  O O   . GLN B 2 82  ? 30.80300 -2.81000  38.23400  1.000 81.63000  ? 414 GLN B O   1 
ATOM   973  C CB  . GLN B 2 82  ? 33.36400 -1.06700  38.74600  1.000 75.32000  ? 414 GLN B CB  1 
ATOM   974  C CG  . GLN B 2 82  ? 34.24000 -0.11500  39.51300  1.000 75.28000  ? 414 GLN B CG  1 
ATOM   975  C CD  . GLN B 2 82  ? 34.11800 1.29700   38.97800  1.000 81.64000  ? 414 GLN B CD  1 
ATOM   976  O OE1 . GLN B 2 82  ? 34.29200 1.53700   37.78000  1.000 88.41000  ? 414 GLN B OE1 1 
ATOM   977  N NE2 . GLN B 2 82  ? 33.78600 2.23400   39.85300  1.000 86.81000  ? 414 GLN B NE2 1 
ATOM   978  N N   . THR B 2 83  ? 30.59500 -1.01600  36.91200  1.000 81.55000  ? 415 THR B N   1 
ATOM   979  C CA  . THR B 2 83  ? 30.01800 -1.78100  35.81300  1.000 80.56000  ? 415 THR B CA  1 
ATOM   980  C C   . THR B 2 83  ? 31.02900 -1.86700  34.68600  1.000 67.63000  ? 415 THR B C   1 
ATOM   981  O O   . THR B 2 83  ? 32.05900 -1.19400  34.68900  1.000 75.93000  ? 415 THR B O   1 
ATOM   982  C CB  . THR B 2 83  ? 28.71500 -1.17100  35.28900  1.000 77.89000  ? 415 THR B CB  1 
ATOM   983  O OG1 . THR B 2 83  ? 28.95600 0.16200   34.83700  1.000 81.62000  ? 415 THR B OG1 1 
ATOM   984  C CG2 . THR B 2 83  ? 27.65500 -1.13100  36.36800  1.000 78.48000  ? 415 THR B CG2 1 
ATOM   985  N N   . GLY B 2 84  ? 30.72900 -2.71200  33.71800  1.000 70.35000  ? 416 GLY B N   1 
ATOM   986  C CA  . GLY B 2 84  ? 31.63200 -2.89000  32.60000  1.000 77.34000  ? 416 GLY B CA  1 
ATOM   987  C C   . GLY B 2 84  ? 31.81800 -4.34800  32.24600  1.000 77.24000  ? 416 GLY B C   1 
ATOM   988  O O   . GLY B 2 84  ? 31.40600 -5.23200  33.00200  1.000 76.31000  ? 416 GLY B O   1 
ATOM   989  N N   . LYS B 2 85  ? 32.46400 -4.61800  31.11100  1.000 71.14000  ? 417 LYS B N   1 
ATOM   990  C CA  . LYS B 2 85  ? 32.45600 -5.97600  30.58300  1.000 67.35000  ? 417 LYS B CA  1 
ATOM   991  C C   . LYS B 2 85  ? 33.10100 -6.96300  31.54800  1.000 68.16000  ? 417 LYS B C   1 
ATOM   992  O O   . LYS B 2 85  ? 32.66600 -8.11300  31.64500  1.000 71.35000  ? 417 LYS B O   1 
ATOM   993  C CB  . LYS B 2 85  ? 33.13700 -5.98800  29.21500  1.000 70.16000  ? 417 LYS B CB  1 
ATOM   994  C CG  . LYS B 2 85  ? 33.26900 -7.34100  28.56500  1.000 64.83000  ? 417 LYS B CG  1 
ATOM   995  C CD  . LYS B 2 85  ? 33.82300 -7.21900  27.15800  1.000 80.65000  ? 417 LYS B CD  1 
ATOM   996  C CE  . LYS B 2 85  ? 35.04900 -6.32000  27.04600  1.000 78.76000  ? 417 LYS B CE  1 
ATOM   997  N NZ  . LYS B 2 85  ? 35.58200 -6.38800  25.63000  1.000 72.73000  ? 417 LYS B NZ  1 
ATOM   998  N N   . ILE B 2 86  ? 34.09200 -6.52600  32.31000  1.000 65.76000  ? 418 ILE B N   1 
ATOM   999  C CA  . ILE B 2 86  ? 34.75700 -7.42600  33.25000  1.000 74.34000  ? 418 ILE B CA  1 
ATOM   1000 C C   . ILE B 2 86  ? 33.95100 -7.57800  34.54600  1.000 74.25000  ? 418 ILE B C   1 
ATOM   1001 O O   . ILE B 2 86  ? 33.74100 -8.69500  35.03000  1.000 77.33000  ? 418 ILE B O   1 
ATOM   1002 C CB  . ILE B 2 86  ? 36.19100 -6.93200  33.53400  1.000 75.42000  ? 418 ILE B CB  1 
ATOM   1003 C CG1 . ILE B 2 86  ? 36.97800 -6.77200  32.23300  1.000 71.84000  ? 418 ILE B CG1 1 
ATOM   1004 C CG2 . ILE B 2 86  ? 36.90800 -7.86900  34.47200  1.000 64.57000  ? 418 ILE B CG2 1 
ATOM   1005 C CD1 . ILE B 2 86  ? 36.83900 -7.91500  31.23600  1.000 71.95000  ? 418 ILE B CD1 1 
ATOM   1006 N N   . ALA B 2 87  ? 33.50600 -6.46900  35.14000  1.000 71.21000  ? 419 ALA B N   1 
ATOM   1007 C CA  . ALA B 2 87  ? 32.74400 -6.54300  36.37500  1.000 67.79000  ? 419 ALA B CA  1 
ATOM   1008 C C   . ALA B 2 87  ? 31.34700 -7.09100  36.16800  1.000 72.47000  ? 419 ALA B C   1 
ATOM   1009 O O   . ALA B 2 87  ? 30.70400 -7.48900  37.15400  1.000 67.45000  ? 419 ALA B O   1 
ATOM   1010 C CB  . ALA B 2 87  ? 32.64400 -5.16600  37.01800  1.000 68.09000  ? 419 ALA B CB  1 
ATOM   1011 N N   . ASP B 2 88  ? 30.84900 -7.09200  34.92600  1.000 62.34000  ? 420 ASP B N   1 
ATOM   1012 C CA  . ASP B 2 88  ? 29.53600 -7.64600  34.63100  1.000 66.31000  ? 420 ASP B CA  1 
ATOM   1013 C C   . ASP B 2 88  ? 29.60400 -9.14900  34.41000  1.000 69.28000  ? 420 ASP B C   1 
ATOM   1014 O O   . ASP B 2 88  ? 28.81500 -9.89800  35.00400  1.000 67.07000  ? 420 ASP B O   1 
ATOM   1015 C CB  . ASP B 2 88  ? 28.91800 -7.00900  33.36900  1.000 75.91000  ? 420 ASP B CB  1 
ATOM   1016 C CG  . ASP B 2 88  ? 28.54700 -5.53800  33.52700  1.000 72.98000  ? 420 ASP B CG  1 
ATOM   1017 O OD1 . ASP B 2 88  ? 29.10700 -4.80700  34.36200  1.000 76.29000  ? 420 ASP B OD1 1 
ATOM   1018 O OD2 . ASP B 2 88  ? 27.67000 -5.10500  32.77400  1.000 77.70000  ? 420 ASP B OD2 1 
ATOM   1019 N N   . TYR B 2 89  ? 30.53100 -9.60000  33.54300  1.000 74.03000  ? 421 TYR B N   1 
ATOM   1020 C CA  . TYR B 2 89  ? 30.52900 -10.95300 32.98700  1.000 72.76000  ? 421 TYR B CA  1 
ATOM   1021 C C   . TYR B 2 89  ? 31.69200 -11.84400 33.43000  1.000 65.88000  ? 421 TYR B C   1 
ATOM   1022 O O   . TYR B 2 89  ? 31.64400 -13.05700 33.17300  1.000 63.86000  ? 421 TYR B O   1 
ATOM   1023 C CB  . TYR B 2 89  ? 30.52400 -10.89700 31.45000  1.000 70.37000  ? 421 TYR B CB  1 
ATOM   1024 C CG  . TYR B 2 89  ? 29.33400 -10.19100 30.85100  1.000 70.13000  ? 421 TYR B CG  1 
ATOM   1025 C CD1 . TYR B 2 89  ? 28.18500 -10.01200 31.58300  1.000 63.54000  ? 421 TYR B CD1 1 
ATOM   1026 C CD2 . TYR B 2 89  ? 29.34800 -9.72700  29.52300  1.000 73.55000  ? 421 TYR B CD2 1 
ATOM   1027 C CE1 . TYR B 2 89  ? 27.07500 -9.37900  31.03600  1.000 66.76000  ? 421 TYR B CE1 1 
ATOM   1028 C CE2 . TYR B 2 89  ? 28.23500 -9.06800  28.96700  1.000 66.33000  ? 421 TYR B CE2 1 
ATOM   1029 C CZ  . TYR B 2 89  ? 27.09700 -8.90100  29.73400  1.000 72.20000  ? 421 TYR B CZ  1 
ATOM   1030 O OH  . TYR B 2 89  ? 25.96400 -8.26700  29.24000  1.000 67.75000  ? 421 TYR B OH  1 
ATOM   1031 N N   . ASN B 2 90  ? 32.70800 -11.30500 34.10600  1.000 65.06000  ? 422 ASN B N   1 
ATOM   1032 C CA  . ASN B 2 90  ? 33.91100 -12.07600 34.40500  1.000 66.31000  ? 422 ASN B CA  1 
ATOM   1033 C C   . ASN B 2 90  ? 34.25800 -12.11600 35.89100  1.000 71.73000  ? 422 ASN B C   1 
ATOM   1034 O O   . ASN B 2 90  ? 34.52500 -13.20300 36.43000  1.000 67.86000  ? 422 ASN B O   1 
ATOM   1035 C CB  . ASN B 2 90  ? 35.08100 -11.52700 33.58200  1.000 61.14000  ? 422 ASN B CB  1 
ATOM   1036 C CG  . ASN B 2 90  ? 34.86800 -11.71200 32.08800  1.000 73.33000  ? 422 ASN B CG  1 
ATOM   1037 O OD1 . ASN B 2 90  ? 35.27600 -12.72100 31.50300  1.000 71.85000  ? 422 ASN B OD1 1 
ATOM   1038 N ND2 . ASN B 2 90  ? 34.23100 -10.72800 31.45800  1.000 70.37000  ? 422 ASN B ND2 1 
ATOM   1039 N N   . TYR B 2 91  ? 34.23200 -10.98300 36.58900  1.000 66.67000  ? 423 TYR B N   1 
ATOM   1040 C CA  . TYR B 2 91  ? 34.62700 -10.92500 37.99600  1.000 64.99000  ? 423 TYR B CA  1 
ATOM   1041 C C   . TYR B 2 91  ? 33.97600 -9.70900  38.63300  1.000 68.79000  ? 423 TYR B C   1 
ATOM   1042 O O   . TYR B 2 91  ? 34.35500 -8.58200  38.29900  1.000 74.25000  ? 423 TYR B O   1 
ATOM   1043 C CB  . TYR B 2 91  ? 36.14000 -10.84300 38.14200  1.000 63.14000  ? 423 TYR B CB  1 
ATOM   1044 C CG  . TYR B 2 91  ? 36.61800 -10.97600 39.57200  1.000 72.65000  ? 423 TYR B CG  1 
ATOM   1045 C CD1 . TYR B 2 91  ? 36.88500 -12.22800 40.12800  1.000 69.41000  ? 423 TYR B CD1 1 
ATOM   1046 C CD2 . TYR B 2 91  ? 36.82100 -9.85700  40.36800  1.000 71.46000  ? 423 TYR B CD2 1 
ATOM   1047 C CE1 . TYR B 2 91  ? 37.33500 -12.35800 41.44700  1.000 71.46000  ? 423 TYR B CE1 1 
ATOM   1048 C CE2 . TYR B 2 91  ? 37.29100 -9.97300  41.66600  1.000 72.03000  ? 423 TYR B CE2 1 
ATOM   1049 C CZ  . TYR B 2 91  ? 37.53400 -11.22100 42.22500  1.000 79.44000  ? 423 TYR B CZ  1 
ATOM   1050 O OH  . TYR B 2 91  ? 37.99100 -11.34200 43.54100  1.000 71.66000  ? 423 TYR B OH  1 
ATOM   1051 N N   . LYS B 2 92  ? 33.02400 -9.93500  39.55000  1.000 63.56000  ? 424 LYS B N   1 
ATOM   1052 C CA  . LYS B 2 92  ? 32.25900 -8.88000  40.21500  1.000 64.11000  ? 424 LYS B CA  1 
ATOM   1053 C C   . LYS B 2 92  ? 32.61000 -8.80600  41.69900  1.000 71.30000  ? 424 LYS B C   1 
ATOM   1054 O O   . LYS B 2 92  ? 32.62900 -9.82800  42.39500  1.000 73.99000  ? 424 LYS B O   1 
ATOM   1055 C CB  . LYS B 2 92  ? 30.75700 -9.11400  40.06900  1.000 68.52000  ? 424 LYS B CB  1 
ATOM   1056 C CG  . LYS B 2 92  ? 29.87700 -8.13400  40.85400  1.000 64.14000  ? 424 LYS B CG  1 
ATOM   1057 C CD  . LYS B 2 92  ? 30.13300 -6.70500  40.41800  1.000 60.23000  ? 424 LYS B CD  1 
ATOM   1058 C CE  . LYS B 2 92  ? 28.96300 -5.80100  40.75300  1.000 50.00000  ? 424 LYS B CE  1 
ATOM   1059 N NZ  . LYS B 2 92  ? 29.31800 -4.35000  40.53700  1.000 57.11000  ? 424 LYS B NZ  1 
ATOM   1060 N N   . LEU B 2 93  ? 32.83700 -7.60000  42.18400  1.000 69.88000  ? 425 LEU B N   1 
ATOM   1061 C CA  . LEU B 2 93  ? 33.09100 -7.19000  43.55600  1.000 70.82000  ? 425 LEU B CA  1 
ATOM   1062 C C   . LEU B 2 93  ? 31.80600 -6.64600  44.18300  1.000 72.55000  ? 425 LEU B C   1 
ATOM   1063 O O   . LEU B 2 93  ? 31.04900 -5.93500  43.50500  1.000 71.61000  ? 425 LEU B O   1 
ATOM   1064 C CB  . LEU B 2 93  ? 34.17400 -6.13000  43.59300  1.000 71.37000  ? 425 LEU B CB  1 
ATOM   1065 C CG  . LEU B 2 93  ? 35.56200 -6.55300  43.14300  1.000 71.51000  ? 425 LEU B CG  1 
ATOM   1066 C CD1 . LEU B 2 93  ? 36.40100 -5.35200  43.12100  1.000 77.08000  ? 425 LEU B CD1 1 
ATOM   1067 C CD2 . LEU B 2 93  ? 36.15400 -7.59300  44.06200  1.000 72.52000  ? 425 LEU B CD2 1 
ATOM   1068 N N   . PRO B 2 94  ? 31.52100 -6.96400  45.44600  1.000 69.80000  ? 426 PRO B N   1 
ATOM   1069 C CA  . PRO B 2 94  ? 30.27300 -6.50600  46.07200  1.000 72.58000  ? 426 PRO B CA  1 
ATOM   1070 C C   . PRO B 2 94  ? 30.38100 -5.06300  46.54700  1.000 72.03000  ? 426 PRO B C   1 
ATOM   1071 O O   . PRO B 2 94  ? 31.46900 -4.53500  46.76400  1.000 75.74000  ? 426 PRO B O   1 
ATOM   1072 C CB  . PRO B 2 94  ? 30.09400 -7.46100  47.26500  1.000 72.91000  ? 426 PRO B CB  1 
ATOM   1073 C CG  . PRO B 2 94  ? 31.48600 -7.86700  47.62600  1.000 68.64000  ? 426 PRO B CG  1 
ATOM   1074 C CD  . PRO B 2 94  ? 32.23700 -7.93600  46.28300  1.000 67.13000  ? 426 PRO B CD  1 
ATOM   1075 N N   . ASP B 2 95  ? 29.22300 -4.41500  46.70100  1.000 69.38000  ? 427 ASP B N   1 
ATOM   1076 C CA  . ASP B 2 95  ? 29.23000 -3.04400  47.21100  1.000 73.39000  ? 427 ASP B CA  1 
ATOM   1077 C C   . ASP B 2 95  ? 29.95900 -2.97900  48.54900  1.000 74.31000  ? 427 ASP B C   1 
ATOM   1078 O O   . ASP B 2 95  ? 30.91300 -2.21600  48.72400  1.000 73.42000  ? 427 ASP B O   1 
ATOM   1079 C CB  . ASP B 2 95  ? 27.80000 -2.51700  47.34300  1.000 73.78000  ? 427 ASP B CB  1 
ATOM   1080 C CG  . ASP B 2 95  ? 26.92900 -2.89000  46.15500  1.000 76.76000  ? 427 ASP B CG  1 
ATOM   1081 O OD1 . ASP B 2 95  ? 27.30800 -3.82700  45.42300  1.000 84.53000  ? 427 ASP B OD1 1 
ATOM   1082 O OD2 . ASP B 2 95  ? 25.86400 -2.26400  45.95100  1.000 79.32000  ? 427 ASP B OD2 1 
ATOM   1083 N N   . ASP B 2 96  ? 29.55600 -3.81400  49.49000  1.000 71.89000  ? 428 ASP B N   1 
ATOM   1084 C CA  . ASP B 2 96  ? 30.23800 -3.86200  50.77800  1.000 77.88000  ? 428 ASP B CA  1 
ATOM   1085 C C   . ASP B 2 96  ? 31.56500 -4.61100  50.69500  1.000 78.44000  ? 428 ASP B C   1 
ATOM   1086 O O   . ASP B 2 96  ? 31.86700 -5.42000  51.57000  1.000 90.31000  ? 428 ASP B O   1 
ATOM   1087 C CB  . ASP B 2 96  ? 29.31900 -4.49100  51.82300  1.000 81.37000  ? 428 ASP B CB  1 
ATOM   1088 C CG  . ASP B 2 96  ? 29.15300 -5.99000  51.62900  1.000 86.09000  ? 428 ASP B CG  1 
ATOM   1089 O OD1 . ASP B 2 96  ? 29.38500 -6.44400  50.48900  1.000 87.45000  ? 428 ASP B OD1 1 
ATOM   1090 O OD2 . ASP B 2 96  ? 28.80800 -6.71600  52.60200  1.000 92.97000  ? 428 ASP B OD2 1 
ATOM   1091 N N   . PHE B 2 97  ? 32.39800 -4.39500  49.68200  1.000 65.23000  ? 429 PHE B N   1 
ATOM   1092 C CA  . PHE B 2 97  ? 33.66500 -5.11400  49.68300  1.000 70.11000  ? 429 PHE B CA  1 
ATOM   1093 C C   . PHE B 2 97  ? 34.52000 -4.68500  50.86800  1.000 77.04000  ? 429 PHE B C   1 
ATOM   1094 O O   . PHE B 2 97  ? 34.37200 -3.58500  51.40400  1.000 82.20000  ? 429 PHE B O   1 
ATOM   1095 C CB  . PHE B 2 97  ? 34.43500 -4.89500  48.38400  1.000 78.03000  ? 429 PHE B CB  1 
ATOM   1096 C CG  . PHE B 2 97  ? 35.78500 -5.58300  48.34400  1.000 73.11000  ? 429 PHE B CG  1 
ATOM   1097 C CD1 . PHE B 2 97  ? 35.89400 -6.96400  48.39700  1.000 73.71000  ? 429 PHE B CD1 1 
ATOM   1098 C CD2 . PHE B 2 97  ? 36.94300 -4.84000  48.25300  1.000 76.53000  ? 429 PHE B CD2 1 
ATOM   1099 C CE1 . PHE B 2 97  ? 37.14600 -7.58400  48.35900  1.000 76.02000  ? 429 PHE B CE1 1 
ATOM   1100 C CE2 . PHE B 2 97  ? 38.18300 -5.45400  48.22300  1.000 75.81000  ? 429 PHE B CE2 1 
ATOM   1101 C CZ  . PHE B 2 97  ? 38.28400 -6.82500  48.26700  1.000 73.86000  ? 429 PHE B CZ  1 
ATOM   1102 N N   . THR B 2 98  ? 35.40000 -5.59300  51.29000  1.000 76.44000  ? 430 THR B N   1 
ATOM   1103 C CA  . THR B 2 98  ? 36.37000 -5.34700  52.34700  1.000 79.51000  ? 430 THR B CA  1 
ATOM   1104 C C   . THR B 2 98  ? 37.63100 -6.11100  51.97900  1.000 77.27000  ? 430 THR B C   1 
ATOM   1105 O O   . THR B 2 98  ? 37.66600 -7.34800  52.07000  1.000 76.12000  ? 430 THR B O   1 
ATOM   1106 C CB  . THR B 2 98  ? 35.86600 -5.79700  53.73100  1.000 76.24000  ? 430 THR B CB  1 
ATOM   1107 O OG1 . THR B 2 98  ? 34.71500 -5.04400  54.10800  1.000 75.40000  ? 430 THR B OG1 1 
ATOM   1108 C CG2 . THR B 2 98  ? 36.94500 -5.61300  54.76200  1.000 68.02000  ? 430 THR B CG2 1 
ATOM   1109 N N   . GLY B 2 99  ? 38.66300 -5.38100  51.60800  1.000 76.33000  ? 431 GLY B N   1 
ATOM   1110 C CA  . GLY B 2 99  ? 39.91200 -5.97400  51.19100  1.000 76.84000  ? 431 GLY B CA  1 
ATOM   1111 C C   . GLY B 2 99  ? 40.63600 -5.02300  50.26300  1.000 79.83000  ? 431 GLY B C   1 
ATOM   1112 O O   . GLY B 2 99  ? 40.22600 -3.87900  50.06100  1.000 83.33000  ? 431 GLY B O   1 
ATOM   1113 N N   . CYS B 2 100 ? 41.72300 -5.51800  49.69200  1.000 81.68000  ? 432 CYS B N   1 
ATOM   1114 C CA  . CYS B 2 100 ? 42.55300 -4.72100  48.80800  1.000 81.45000  ? 432 CYS B CA  1 
ATOM   1115 C C   . CYS B 2 100 ? 42.50900 -5.28900  47.40400  1.000 78.89000  ? 432 CYS B C   1 
ATOM   1116 O O   . CYS B 2 100 ? 42.11200 -6.43700  47.18200  1.000 80.05000  ? 432 CYS B O   1 
ATOM   1117 C CB  . CYS B 2 100 ? 44.00100 -4.66800  49.28700  1.000 79.64000  ? 432 CYS B CB  1 
ATOM   1118 S SG  . CYS B 2 100 ? 44.17000 -3.82000  50.86800  1.000 97.00000  ? 432 CYS B SG  1 
ATOM   1119 N N   . VAL B 2 101 ? 42.92600 -4.46300  46.45300  1.000 82.57000  ? 433 VAL B N   1 
ATOM   1120 C CA  . VAL B 2 101 ? 43.04300 -4.87000  45.06500  1.000 80.46000  ? 433 VAL B CA  1 
ATOM   1121 C C   . VAL B 2 101 ? 44.40400 -4.40100  44.58400  1.000 82.60000  ? 433 VAL B C   1 
ATOM   1122 O O   . VAL B 2 101 ? 44.79100 -3.25700  44.83500  1.000 88.37000  ? 433 VAL B O   1 
ATOM   1123 C CB  . VAL B 2 101 ? 41.90900 -4.29300  44.20100  1.000 74.67000  ? 433 VAL B CB  1 
ATOM   1124 C CG1 . VAL B 2 101 ? 42.14000 -4.62600  42.76400  1.000 77.43000  ? 433 VAL B CG1 1 
ATOM   1125 C CG2 . VAL B 2 101 ? 40.59800 -4.87100  44.64300  1.000 75.56000  ? 433 VAL B CG2 1 
ATOM   1126 N N   . ILE B 2 102 ? 45.14100 -5.29400  43.93600  1.000 79.59000  ? 434 ILE B N   1 
ATOM   1127 C CA  . ILE B 2 102 ? 46.53300 -5.06600  43.58600  1.000 81.97000  ? 434 ILE B CA  1 
ATOM   1128 C C   . ILE B 2 102 ? 46.72100 -5.51700  42.15200  1.000 82.08000  ? 434 ILE B C   1 
ATOM   1129 O O   . ILE B 2 102 ? 46.26700 -6.60400  41.78200  1.000 82.74000  ? 434 ILE B O   1 
ATOM   1130 C CB  . ILE B 2 102 ? 47.49300 -5.83600  44.51000  1.000 84.26000  ? 434 ILE B CB  1 
ATOM   1131 C CG1 . ILE B 2 102 ? 47.05100 -5.75000  45.97400  1.000 85.10000  ? 434 ILE B CG1 1 
ATOM   1132 C CG2 . ILE B 2 102 ? 48.88800 -5.29200  44.38700  1.000 88.84000  ? 434 ILE B CG2 1 
ATOM   1133 C CD1 . ILE B 2 102 ? 47.84200 -6.64800  46.88000  1.000 85.44000  ? 434 ILE B CD1 1 
ATOM   1134 N N   . ALA B 2 103 ? 47.38000 -4.69200  41.34500  1.000 80.89000  ? 435 ALA B N   1 
ATOM   1135 C CA  . ALA B 2 103 ? 47.64300 -5.05100  39.96200  1.000 83.38000  ? 435 ALA B CA  1 
ATOM   1136 C C   . ALA B 2 103 ? 49.05100 -4.61500  39.60500  1.000 82.55000  ? 435 ALA B C   1 
ATOM   1137 O O   . ALA B 2 103 ? 49.56900 -3.63600  40.14600  1.000 86.52000  ? 435 ALA B O   1 
ATOM   1138 C CB  . ALA B 2 103 ? 46.63500 -4.41000  38.99300  1.000 78.55000  ? 435 ALA B CB  1 
ATOM   1139 N N   . TRP B 2 104 ? 49.66900 -5.35300  38.69000  1.000 81.79000  ? 436 TRP B N   1 
ATOM   1140 C CA  . TRP B 2 104 ? 50.93000 -4.91600  38.11400  1.000 82.72000  ? 436 TRP B CA  1 
ATOM   1141 C C   . TRP B 2 104 ? 50.97800 -5.27000  36.62400  1.000 82.45000  ? 436 TRP B C   1 
ATOM   1142 O O   . TRP B 2 104 ? 50.34300 -6.22500  36.17200  1.000 83.57000  ? 436 TRP B O   1 
ATOM   1143 C CB  . TRP B 2 104 ? 52.12300 -5.49700  38.89800  1.000 81.16000  ? 436 TRP B CB  1 
ATOM   1144 C CG  . TRP B 2 104 ? 52.28300 -6.98800  38.90800  1.000 73.95000  ? 436 TRP B CG  1 
ATOM   1145 C CD1 . TRP B 2 104 ? 53.14000 -7.72500  38.14100  1.000 79.50000  ? 436 TRP B CD1 1 
ATOM   1146 C CD2 . TRP B 2 104 ? 51.60000 -7.92200  39.75500  1.000 76.53000  ? 436 TRP B CD2 1 
ATOM   1147 N NE1 . TRP B 2 104 ? 53.02100 -9.05900  38.44900  1.000 78.56000  ? 436 TRP B NE1 1 
ATOM   1148 C CE2 . TRP B 2 104 ? 52.08100 -9.20400  39.43600  1.000 74.44000  ? 436 TRP B CE2 1 
ATOM   1149 C CE3 . TRP B 2 104 ? 50.61500 -7.79800  40.73800  1.000 79.43000  ? 436 TRP B CE3 1 
ATOM   1150 C CZ2 . TRP B 2 104 ? 51.61000 -10.35000 40.05700  1.000 77.61000  ? 436 TRP B CZ2 1 
ATOM   1151 C CZ3 . TRP B 2 104 ? 50.15800 -8.93700  41.36200  1.000 80.87000  ? 436 TRP B CZ3 1 
ATOM   1152 C CH2 . TRP B 2 104 ? 50.65700 -10.19600 41.02200  1.000 79.21000  ? 436 TRP B CH2 1 
ATOM   1153 N N   . ASN B 2 105 ? 51.71900 -4.47000  35.86300  1.000 81.28000  ? 437 ASN B N   1 
ATOM   1154 C CA  . ASN B 2 105 ? 51.84500 -4.70200  34.42600  1.000 80.85000  ? 437 ASN B CA  1 
ATOM   1155 C C   . ASN B 2 105 ? 52.69900 -5.92900  34.17900  1.000 79.76000  ? 437 ASN B C   1 
ATOM   1156 O O   . ASN B 2 105 ? 53.84600 -5.98900  34.62200  1.000 80.81000  ? 437 ASN B O   1 
ATOM   1157 C CB  . ASN B 2 105 ? 52.46900 -3.48400  33.73400  1.000 80.82000  ? 437 ASN B CB  1 
ATOM   1158 C CG  . ASN B 2 105 ? 52.54000 -3.62700  32.21600  1.000 85.10000  ? 437 ASN B CG  1 
ATOM   1159 O OD1 . ASN B 2 105 ? 53.27900 -4.46900  31.69200  1.000 83.50000  ? 437 ASN B OD1 1 
ATOM   1160 N ND2 . ASN B 2 105 ? 51.79000 -2.77900  31.50000  1.000 83.67000  ? 437 ASN B ND2 1 
ATOM   1161 N N   . SER B 2 106 ? 52.14700 -6.90100  33.46300  1.000 83.21000  ? 438 SER B N   1 
ATOM   1162 C CA  . SER B 2 106 ? 52.88200 -8.09800  33.08100  1.000 81.64000  ? 438 SER B CA  1 
ATOM   1163 C C   . SER B 2 106 ? 53.06200 -8.17400  31.57800  1.000 84.71000  ? 438 SER B C   1 
ATOM   1164 O O   . SER B 2 106 ? 52.84700 -9.22300  30.96800  1.000 92.02000  ? 438 SER B O   1 
ATOM   1165 C CB  . SER B 2 106 ? 52.18400 -9.35700  33.58300  1.000 88.11000  ? 438 SER B CB  1 
ATOM   1166 O OG  . SER B 2 106 ? 51.09300 -9.72000  32.74900  1.000 81.07000  ? 438 SER B OG  1 
ATOM   1167 N N   . ASN B 2 107 ? 53.45100 -7.06100  30.95000  1.000 89.96000  ? 439 ASN B N   1 
ATOM   1168 C CA  . ASN B 2 107 ? 53.71100 -7.09400  29.51300  1.000 83.60000  ? 439 ASN B CA  1 
ATOM   1169 C C   . ASN B 2 107 ? 54.84900 -8.04900  29.18800  1.000 82.38000  ? 439 ASN B C   1 
ATOM   1170 O O   . ASN B 2 107 ? 54.78000 -8.79500  28.20400  1.000 90.09000  ? 439 ASN B O   1 
ATOM   1171 C CB  . ASN B 2 107 ? 54.04200 -5.69700  28.99800  1.000 83.08000  ? 439 ASN B CB  1 
ATOM   1172 C CG  . ASN B 2 107 ? 53.85000 -5.57000  27.50100  1.000 94.24000  ? 439 ASN B CG  1 
ATOM   1173 O OD1 . ASN B 2 107 ? 53.37200 -6.49200  26.84400  1.000 92.70000  ? 439 ASN B OD1 1 
ATOM   1174 N ND2 . ASN B 2 107 ? 54.22900 -4.42600  26.95200  1.000 97.97000  ? 439 ASN B ND2 1 
ATOM   1175 N N   . ASN B 2 108 ? 55.90500 -8.03100  30.00200  1.000 81.59000  ? 440 ASN B N   1 
ATOM   1176 C CA  . ASN B 2 108 ? 57.04300 -8.92300  29.80200  1.000 90.39000  ? 440 ASN B CA  1 
ATOM   1177 C C   . ASN B 2 108 ? 56.61700 -10.38500 29.78400  1.000 91.68000  ? 440 ASN B C   1 
ATOM   1178 O O   . ASN B 2 108 ? 57.14200 -11.19000 29.00000  1.000 90.72000  ? 440 ASN B O   1 
ATOM   1179 C CB  . ASN B 2 108 ? 58.07900 -8.69000  30.90400  1.000 84.68000  ? 440 ASN B CB  1 
ATOM   1180 C CG  . ASN B 2 108 ? 57.44400 -8.58500  32.30200  1.000 92.13000  ? 440 ASN B CG  1 
ATOM   1181 O OD1 . ASN B 2 108 ? 56.25100 -8.28900  32.43800  1.000 96.96000  ? 440 ASN B OD1 1 
ATOM   1182 N ND2 . ASN B 2 108 ? 58.24500 -8.81400  33.34300  1.000 92.07000  ? 440 ASN B ND2 1 
ATOM   1183 N N   . LEU B 2 109 ? 55.66000 -10.74500 30.63300  1.000 89.89000  ? 441 LEU B N   1 
ATOM   1184 C CA  . LEU B 2 109 ? 55.34400 -12.13900 30.89500  1.000 83.83000  ? 441 LEU B CA  1 
ATOM   1185 C C   . LEU B 2 109 ? 54.27100 -12.67000 29.96000  1.000 84.88000  ? 441 LEU B C   1 
ATOM   1186 O O   . LEU B 2 109 ? 54.44200 -13.73900 29.36900  1.000 89.15000  ? 441 LEU B O   1 
ATOM   1187 C CB  . LEU B 2 109 ? 54.90700 -12.30100 32.35400  1.000 90.69000  ? 441 LEU B CB  1 
ATOM   1188 C CG  . LEU B 2 109 ? 55.92900 -11.76900 33.36600  1.000 94.31000  ? 441 LEU B CG  1 
ATOM   1189 C CD1 . LEU B 2 109 ? 55.37600 -11.71300 34.80700  1.000 81.94000  ? 441 LEU B CD1 1 
ATOM   1190 C CD2 . LEU B 2 109 ? 57.18700 -12.62400 33.27900  1.000 92.67000  ? 441 LEU B CD2 1 
ATOM   1191 N N   . ASP B 2 110 ? 53.17800 -11.92900 29.79000  1.000 85.37000  ? 442 ASP B N   1 
ATOM   1192 C CA  . ASP B 2 110 ? 51.97300 -12.47700 29.17500  1.000 87.93000  ? 442 ASP B CA  1 
ATOM   1193 C C   . ASP B 2 110 ? 51.70200 -11.94700 27.76000  1.000 85.19000  ? 442 ASP B C   1 
ATOM   1194 O O   . ASP B 2 110 ? 50.65100 -12.25700 27.17900  1.000 78.58000  ? 442 ASP B O   1 
ATOM   1195 C CB  . ASP B 2 110 ? 50.78200 -12.22600 30.10500  1.000 81.95000  ? 442 ASP B CB  1 
ATOM   1196 C CG  . ASP B 2 110 ? 50.98700 -12.84300 31.48300  1.000 83.49000  ? 442 ASP B CG  1 
ATOM   1197 O OD1 . ASP B 2 110 ? 51.15100 -14.08100 31.56300  1.000 87.02000  ? 442 ASP B OD1 1 
ATOM   1198 O OD2 . ASP B 2 110 ? 51.01700 -12.08700 32.47700  1.000 80.46000  ? 442 ASP B OD2 1 
ATOM   1199 N N   . SER B 2 111 ? 52.62400 -11.17700 27.18500  1.000 86.14000  ? 443 SER B N   1 
ATOM   1200 C CA  . SER B 2 111 ? 52.53500 -10.73900 25.80000  1.000 88.41000  ? 443 SER B CA  1 
ATOM   1201 C C   . SER B 2 111 ? 53.45600 -11.57600 24.93300  1.000 87.56000  ? 443 SER B C   1 
ATOM   1202 O O   . SER B 2 111 ? 54.58800 -11.87500 25.32000  1.000 88.30000  ? 443 SER B O   1 
ATOM   1203 C CB  . SER B 2 111 ? 52.92600 -9.27400  25.65000  1.000 85.72000  ? 443 SER B CB  1 
ATOM   1204 O OG  . SER B 2 111 ? 51.96000 -8.41400  26.22700  1.000 86.02000  ? 443 SER B OG  1 
ATOM   1205 N N   . LYS B 2 112 ? 52.98100 -11.93400 23.75100  1.000 87.29000  ? 444 LYS B N   1 
ATOM   1206 C CA  . LYS B 2 112 ? 53.81400 -12.65500 22.80700  1.000 91.71000  ? 444 LYS B CA  1 
ATOM   1207 C C   . LYS B 2 112 ? 53.79000 -11.95200 21.45900  1.000 89.69000  ? 444 LYS B C   1 
ATOM   1208 O O   . LYS B 2 112 ? 52.79400 -11.32300 21.08300  1.000 87.15000  ? 444 LYS B O   1 
ATOM   1209 C CB  . LYS B 2 112 ? 53.36800 -14.12400 22.67700  1.000 96.08000  ? 444 LYS B CB  1 
ATOM   1210 C CG  . LYS B 2 112 ? 54.25800 -14.96300 21.74400  1.000 106.39000 ? 444 LYS B CG  1 
ATOM   1211 C CD  . LYS B 2 112 ? 53.65800 -16.35400 21.43500  1.000 111.02000 ? 444 LYS B CD  1 
ATOM   1212 C CE  . LYS B 2 112 ? 54.58900 -17.21000 20.56300  1.000 116.72000 ? 444 LYS B CE  1 
ATOM   1213 N NZ  . LYS B 2 112 ? 55.84500 -17.66300 21.25500  1.000 122.65000 ? 444 LYS B NZ  1 
ATOM   1214 N N   . VAL B 2 113 ? 54.92600 -12.01800 20.76300  1.000 94.81000  ? 445 VAL B N   1 
ATOM   1215 C CA  . VAL B 2 113 ? 54.96200 -11.65200 19.35500  1.000 95.35000  ? 445 VAL B CA  1 
ATOM   1216 C C   . VAL B 2 113 ? 53.97000 -12.53200 18.61200  1.000 93.41000  ? 445 VAL B C   1 
ATOM   1217 O O   . VAL B 2 113 ? 53.93700 -13.75600 18.79400  1.000 91.91000  ? 445 VAL B O   1 
ATOM   1218 C CB  . VAL B 2 113 ? 56.39200 -11.79700 18.80500  1.000 96.74000  ? 445 VAL B CB  1 
ATOM   1219 C CG1 . VAL B 2 113 ? 56.47900 -11.33400 17.35000  1.000 96.87000  ? 445 VAL B CG1 1 
ATOM   1220 C CG2 . VAL B 2 113 ? 57.39200 -11.04200 19.68200  1.000 91.06000  ? 445 VAL B CG2 1 
ATOM   1221 N N   . GLY B 2 114 ? 53.13300 -11.91200 17.79100  1.000 93.85000  ? 446 GLY B N   1 
ATOM   1222 C CA  . GLY B 2 114 ? 52.07400 -12.64700 17.13500  1.000 92.09000  ? 446 GLY B CA  1 
ATOM   1223 C C   . GLY B 2 114 ? 50.85200 -12.89200 17.98800  1.000 86.63000  ? 446 GLY B C   1 
ATOM   1224 O O   . GLY B 2 114 ? 49.97600 -13.66900 17.58300  1.000 83.91000  ? 446 GLY B O   1 
ATOM   1225 N N   . GLY B 2 115 ? 50.76300 -12.25700 19.15100  1.000 88.64000  ? 447 GLY B N   1 
ATOM   1226 C CA  . GLY B 2 115 ? 49.56300 -12.35100 19.95100  1.000 89.25000  ? 447 GLY B CA  1 
ATOM   1227 C C   . GLY B 2 115 ? 49.60500 -13.50300 20.91900  1.000 88.05000  ? 447 GLY B C   1 
ATOM   1228 O O   . GLY B 2 115 ? 49.90500 -14.63000 20.53100  1.000 91.98000  ? 447 GLY B O   1 
ATOM   1229 N N   . ASN B 2 116 ? 49.32200 -13.23900 22.18100  1.000 91.82000  ? 448 ASN B N   1 
ATOM   1230 C CA  . ASN B 2 116 ? 49.22500 -14.29500 23.17600  1.000 90.43000  ? 448 ASN B CA  1 
ATOM   1231 C C   . ASN B 2 116 ? 47.75300 -14.57400 23.44300  1.000 87.34000  ? 448 ASN B C   1 
ATOM   1232 O O   . ASN B 2 116 ? 47.04000 -13.71400 23.97500  1.000 84.91000  ? 448 ASN B O   1 
ATOM   1233 C CB  . ASN B 2 116 ? 49.94600 -13.91600 24.46400  1.000 86.28000  ? 448 ASN B CB  1 
ATOM   1234 C CG  . ASN B 2 116 ? 49.76800 -14.95300 25.53500  1.000 87.13000  ? 448 ASN B CG  1 
ATOM   1235 O OD1 . ASN B 2 116 ? 49.41000 -16.09700 25.25300  1.000 82.05000  ? 448 ASN B OD1 1 
ATOM   1236 N ND2 . ASN B 2 116 ? 49.99300 -14.55600 26.78400  1.000 88.11000  ? 448 ASN B ND2 1 
ATOM   1237 N N   . TYR B 2 117 ? 47.31400 -15.78500 23.09300  1.000 85.56000  ? 449 TYR B N   1 
ATOM   1238 C CA  . TYR B 2 117 ? 45.90900 -16.16800 23.15400  1.000 85.53000  ? 449 TYR B CA  1 
ATOM   1239 C C   . TYR B 2 117 ? 45.59500 -17.11800 24.30900  1.000 81.02000  ? 449 TYR B C   1 
ATOM   1240 O O   . TYR B 2 117 ? 44.49900 -17.68600 24.35600  1.000 80.21000  ? 449 TYR B O   1 
ATOM   1241 C CB  . TYR B 2 117 ? 45.48000 -16.77300 21.81400  1.000 75.79000  ? 449 TYR B CB  1 
ATOM   1242 C CG  . TYR B 2 117 ? 45.40900 -15.70300 20.75000  1.000 91.85000  ? 449 TYR B CG  1 
ATOM   1243 C CD1 . TYR B 2 117 ? 46.57500 -15.20500 20.16800  1.000 92.09000  ? 449 TYR B CD1 1 
ATOM   1244 C CD2 . TYR B 2 117 ? 44.19200 -15.14800 20.35600  1.000 93.24000  ? 449 TYR B CD2 1 
ATOM   1245 C CE1 . TYR B 2 117 ? 46.53300 -14.20500 19.20900  1.000 89.50000  ? 449 TYR B CE1 1 
ATOM   1246 C CE2 . TYR B 2 117 ? 44.14600 -14.13700 19.39900  1.000 93.50000  ? 449 TYR B CE2 1 
ATOM   1247 C CZ  . TYR B 2 117 ? 45.32400 -13.67500 18.82700  1.000 87.94000  ? 449 TYR B CZ  1 
ATOM   1248 O OH  . TYR B 2 117 ? 45.31500 -12.68200 17.86900  1.000 84.80000  ? 449 TYR B OH  1 
ATOM   1249 N N   . ASN B 2 118 ? 46.51800 -17.28900 25.25800  1.000 78.86000  ? 450 ASN B N   1 
ATOM   1250 C CA  . ASN B 2 118 ? 46.18800 -18.11600 26.41600  1.000 84.37000  ? 450 ASN B CA  1 
ATOM   1251 C C   . ASN B 2 118 ? 45.17800 -17.46300 27.34000  1.000 77.88000  ? 450 ASN B C   1 
ATOM   1252 O O   . ASN B 2 118 ? 44.64700 -18.14200 28.22400  1.000 78.02000  ? 450 ASN B O   1 
ATOM   1253 C CB  . ASN B 2 118 ? 47.42700 -18.44600 27.24500  1.000 79.44000  ? 450 ASN B CB  1 
ATOM   1254 C CG  . ASN B 2 118 ? 48.40200 -19.30400 26.50900  1.000 82.12000  ? 450 ASN B CG  1 
ATOM   1255 O OD1 . ASN B 2 118 ? 48.02900 -20.09400 25.63200  1.000 88.04000  ? 450 ASN B OD1 1 
ATOM   1256 N ND2 . ASN B 2 118 ? 49.67700 -19.15500 26.84900  1.000 80.72000  ? 450 ASN B ND2 1 
ATOM   1257 N N   . TYR B 2 119 ? 44.91500 -16.18000 27.17300  1.000 74.47000  ? 451 TYR B N   1 
ATOM   1258 C CA  . TYR B 2 119 ? 44.07600 -15.42200 28.08200  1.000 72.29000  ? 451 TYR B CA  1 
ATOM   1259 C C   . TYR B 2 119 ? 42.75800 -15.06200 27.40400  1.000 70.40000  ? 451 TYR B C   1 
ATOM   1260 O O   . TYR B 2 119 ? 42.74200 -14.32800 26.41500  1.000 77.06000  ? 451 TYR B O   1 
ATOM   1261 C CB  . TYR B 2 119 ? 44.82400 -14.17600 28.55100  1.000 77.18000  ? 451 TYR B CB  1 
ATOM   1262 C CG  . TYR B 2 119 ? 45.98200 -14.49900 29.48400  1.000 81.14000  ? 451 TYR B CG  1 
ATOM   1263 C CD1 . TYR B 2 119 ? 45.74600 -14.87800 30.81100  1.000 74.04000  ? 451 TYR B CD1 1 
ATOM   1264 C CD2 . TYR B 2 119 ? 47.30100 -14.44300 29.04700  1.000 78.64000  ? 451 TYR B CD2 1 
ATOM   1265 C CE1 . TYR B 2 119 ? 46.78300 -15.18100 31.67000  1.000 74.71000  ? 451 TYR B CE1 1 
ATOM   1266 C CE2 . TYR B 2 119 ? 48.35000 -14.74400 29.91100  1.000 79.65000  ? 451 TYR B CE2 1 
ATOM   1267 C CZ  . TYR B 2 119 ? 48.07800 -15.11200 31.22300  1.000 82.13000  ? 451 TYR B CZ  1 
ATOM   1268 O OH  . TYR B 2 119 ? 49.10300 -15.41600 32.09600  1.000 75.85000  ? 451 TYR B OH  1 
ATOM   1269 N N   . LEU B 2 120 ? 41.66000 -15.57500 27.94300  1.000 70.59000  ? 452 LEU B N   1 
ATOM   1270 C CA  . LEU B 2 120 ? 40.31200 -15.29700 27.48000  1.000 66.75000  ? 452 LEU B CA  1 
ATOM   1271 C C   . LEU B 2 120 ? 39.56000 -14.41100 28.47400  1.000 70.42000  ? 452 LEU B C   1 
ATOM   1272 O O   . LEU B 2 120 ? 39.95300 -14.25800 29.63800  1.000 66.25000  ? 452 LEU B O   1 
ATOM   1273 C CB  . LEU B 2 120 ? 39.53900 -16.60100 27.28500  1.000 63.16000  ? 452 LEU B CB  1 
ATOM   1274 C CG  . LEU B 2 120 ? 40.30700 -17.70400 26.55000  1.000 70.91000  ? 452 LEU B CG  1 
ATOM   1275 C CD1 . LEU B 2 120 ? 39.72900 -19.07100 26.86000  1.000 64.47000  ? 452 LEU B CD1 1 
ATOM   1276 C CD2 . LEU B 2 120 ? 40.26000 -17.46300 25.06900  1.000 71.03000  ? 452 LEU B CD2 1 
ATOM   1277 N N   . TYR B 2 121 ? 38.46500 -13.82900 27.97700  1.000 70.62000  ? 453 TYR B N   1 
ATOM   1278 C CA  . TYR B 2 121 ? 37.46500 -13.11200 28.75700  1.000 69.10000  ? 453 TYR B CA  1 
ATOM   1279 C C   . TYR B 2 121 ? 36.09900 -13.49500 28.20400  1.000 66.99000  ? 453 TYR B C   1 
ATOM   1280 O O   . TYR B 2 121 ? 35.97400 -13.92300 27.04800  1.000 74.79000  ? 453 TYR B O   1 
ATOM   1281 C CB  . TYR B 2 121 ? 37.65300 -11.57400 28.69200  1.000 69.24000  ? 453 TYR B CB  1 
ATOM   1282 C CG  . TYR B 2 121 ? 37.54100 -10.99700 27.27900  1.000 75.80000  ? 453 TYR B CG  1 
ATOM   1283 C CD1 . TYR B 2 121 ? 38.65200 -10.92700 26.44800  1.000 77.66000  ? 453 TYR B CD1 1 
ATOM   1284 C CD2 . TYR B 2 121 ? 36.32400 -10.54300 26.77700  1.000 76.31000  ? 453 TYR B CD2 1 
ATOM   1285 C CE1 . TYR B 2 121 ? 38.55300 -10.43400 25.17200  1.000 77.55000  ? 453 TYR B CE1 1 
ATOM   1286 C CE2 . TYR B 2 121 ? 36.21700 -10.05300 25.47400  1.000 73.81000  ? 453 TYR B CE2 1 
ATOM   1287 C CZ  . TYR B 2 121 ? 37.34100 -9.99800  24.68300  1.000 77.88000  ? 453 TYR B CZ  1 
ATOM   1288 O OH  . TYR B 2 121 ? 37.28500 -9.51300  23.38800  1.000 82.78000  ? 453 TYR B OH  1 
ATOM   1289 N N   . ARG B 2 122 ? 35.06700 -13.34600 29.02000  1.000 66.22000  ? 454 ARG B N   1 
ATOM   1290 C CA  . ARG B 2 122 ? 33.71000 -13.58900 28.55600  1.000 68.23000  ? 454 ARG B CA  1 
ATOM   1291 C C   . ARG B 2 122 ? 33.12600 -12.27400 28.06100  1.000 67.40000  ? 454 ARG B C   1 
ATOM   1292 O O   . ARG B 2 122 ? 33.15300 -11.27200 28.78200  1.000 69.77000  ? 454 ARG B O   1 
ATOM   1293 C CB  . ARG B 2 122 ? 32.82800 -14.17900 29.65300  1.000 64.52000  ? 454 ARG B CB  1 
ATOM   1294 C CG  . ARG B 2 122 ? 31.39600 -14.44500 29.20900  1.000 68.25000  ? 454 ARG B CG  1 
ATOM   1295 C CD  . ARG B 2 122 ? 30.60100 -15.12600 30.32800  1.000 64.67000  ? 454 ARG B CD  1 
ATOM   1296 N NE  . ARG B 2 122 ? 31.33400 -16.32000 30.70000  1.000 66.32000  ? 454 ARG B NE  1 
ATOM   1297 C CZ  . ARG B 2 122 ? 31.03500 -17.53600 30.27600  1.000 68.26000  ? 454 ARG B CZ  1 
ATOM   1298 N NH1 . ARG B 2 122 ? 29.97200 -17.74700 29.51600  1.000 70.18000  ? 454 ARG B NH1 1 
ATOM   1299 N NH2 . ARG B 2 122 ? 31.79500 -18.54400 30.64000  1.000 66.41000  ? 454 ARG B NH2 1 
ATOM   1300 N N   . LEU B 2 123 ? 32.59400 -12.26800 26.83600  1.000 64.04000  ? 455 LEU B N   1 
ATOM   1301 C CA  . LEU B 2 123 ? 32.03200 -11.03500 26.22200  1.000 68.33000  ? 455 LEU B CA  1 
ATOM   1302 C C   . LEU B 2 123 ? 30.51800 -11.07100 26.34200  1.000 67.05000  ? 455 LEU B C   1 
ATOM   1303 O O   . LEU B 2 123 ? 29.91200 -10.00900 26.50100  1.000 73.37000  ? 455 LEU B O   1 
ATOM   1304 C CB  . LEU B 2 123 ? 32.40700 -11.03600 24.73900  1.000 77.43000  ? 455 LEU B CB  1 
ATOM   1305 C CG  . LEU B 2 123 ? 32.47800 -9.68300  24.03400  1.000 71.84000  ? 455 LEU B CG  1 
ATOM   1306 C CD1 . LEU B 2 123 ? 33.17400 -9.83500  22.69400  1.000 76.11000  ? 455 LEU B CD1 1 
ATOM   1307 C CD2 . LEU B 2 123 ? 31.09300 -9.09600  23.82800  1.000 76.55000  ? 455 LEU B CD2 1 
ATOM   1308 N N   . PHE B 2 124 ? 29.94100 -12.25800 26.23100  1.000 68.91000  ? 456 PHE B N   1 
ATOM   1309 C CA  . PHE B 2 124 ? 28.49900 -12.40600 26.28700  1.000 70.62000  ? 456 PHE B CA  1 
ATOM   1310 C C   . PHE B 2 124 ? 28.06200 -13.13000 27.56600  1.000 73.40000  ? 456 PHE B C   1 
ATOM   1311 O O   . PHE B 2 124 ? 28.74500 -14.02600 28.07200  1.000 75.80000  ? 456 PHE B O   1 
ATOM   1312 C CB  . PHE B 2 124 ? 28.01400 -13.14500 25.05400  1.000 68.66000  ? 456 PHE B CB  1 
ATOM   1313 C CG  . PHE B 2 124 ? 28.48300 -12.52500 23.77100  1.000 75.90000  ? 456 PHE B CG  1 
ATOM   1314 C CD1 . PHE B 2 124 ? 27.92600 -11.34000 23.31600  1.000 76.59000  ? 456 PHE B CD1 1 
ATOM   1315 C CD2 . PHE B 2 124 ? 29.48300 -13.12600 23.01400  1.000 73.47000  ? 456 PHE B CD2 1 
ATOM   1316 C CE1 . PHE B 2 124 ? 28.34500 -10.77500 22.13300  1.000 79.50000  ? 456 PHE B CE1 1 
ATOM   1317 C CE2 . PHE B 2 124 ? 29.91000 -12.56000 21.82900  1.000 77.04000  ? 456 PHE B CE2 1 
ATOM   1318 C CZ  . PHE B 2 124 ? 29.33800 -11.38500 21.38500  1.000 76.01000  ? 456 PHE B CZ  1 
ATOM   1319 N N   . ARG B 2 125 ? 26.91000 -12.74400 28.08000  1.000 63.08000  ? 457 ARG B N   1 
ATOM   1320 C CA  . ARG B 2 125 ? 26.35700 -13.39500 29.24600  1.000 65.80000  ? 457 ARG B CA  1 
ATOM   1321 C C   . ARG B 2 125 ? 24.94600 -12.88300 29.35500  1.000 69.38000  ? 457 ARG B C   1 
ATOM   1322 O O   . ARG B 2 125 ? 24.72300 -11.67700 29.23100  1.000 68.86000  ? 457 ARG B O   1 
ATOM   1323 C CB  . ARG B 2 125 ? 27.14900 -13.07600 30.52000  1.000 71.95000  ? 457 ARG B CB  1 
ATOM   1324 C CG  . ARG B 2 125 ? 27.00300 -14.12600 31.55000  1.000 66.03000  ? 457 ARG B CG  1 
ATOM   1325 C CD  . ARG B 2 125 ? 27.62500 -13.76400 32.88200  1.000 72.27000  ? 457 ARG B CD  1 
ATOM   1326 N NE  . ARG B 2 125 ? 27.46900 -14.92500 33.73400  1.000 69.20000  ? 457 ARG B NE  1 
ATOM   1327 C CZ  . ARG B 2 125 ? 26.43700 -15.11300 34.54500  1.000 67.20000  ? 457 ARG B CZ  1 
ATOM   1328 N NH1 . ARG B 2 125 ? 25.50800 -14.17500 34.65200  1.000 69.72000  ? 457 ARG B NH1 1 
ATOM   1329 N NH2 . ARG B 2 125 ? 26.33900 -16.23500 35.25000  1.000 65.61000  ? 457 ARG B NH2 1 
ATOM   1330 N N   . LYS B 2 126 ? 23.99800 -13.79600 29.56600  1.000 73.71000  ? 458 LYS B N   1 
ATOM   1331 C CA  . LYS B 2 126 ? 22.60000 -13.38000 29.56300  1.000 75.87000  ? 458 LYS B CA  1 
ATOM   1332 C C   . LYS B 2 126 ? 22.24100 -12.44100 30.71600  1.000 74.79000  ? 458 LYS B C   1 
ATOM   1333 O O   . LYS B 2 126 ? 21.12700 -11.90700 30.69900  1.000 75.73000  ? 458 LYS B O   1 
ATOM   1334 C CB  . LYS B 2 126 ? 21.67000 -14.60200 29.57100  1.000 74.04000  ? 458 LYS B CB  1 
ATOM   1335 C CG  . LYS B 2 126 ? 21.65000 -15.39200 28.26500  1.000 77.54000  ? 458 LYS B CG  1 
ATOM   1336 C CD  . LYS B 2 126 ? 21.08000 -14.55500 27.08100  1.000 87.40000  ? 458 LYS B CD  1 
ATOM   1337 C CE  . LYS B 2 126 ? 20.91600 -15.39600 25.79600  1.000 75.80000  ? 458 LYS B CE  1 
ATOM   1338 N NZ  . LYS B 2 126 ? 20.09900 -14.72600 24.73600  1.000 82.75000  ? 458 LYS B NZ  1 
ATOM   1339 N N   . SER B 2 127 ? 23.14400 -12.18000 31.67000  1.000 76.75000  ? 459 SER B N   1 
ATOM   1340 C CA  . SER B 2 127 ? 22.86300 -11.30200 32.81700  1.000 76.41000  ? 459 SER B CA  1 
ATOM   1341 C C   . SER B 2 127 ? 24.14000 -11.08700 33.62100  1.000 74.47000  ? 459 SER B C   1 
ATOM   1342 O O   . SER B 2 127 ? 25.10700 -11.84700 33.50100  1.000 74.19000  ? 459 SER B O   1 
ATOM   1343 C CB  . SER B 2 127 ? 21.79000 -11.88000 33.73900  1.000 70.38000  ? 459 SER B CB  1 
ATOM   1344 O OG  . SER B 2 127 ? 22.32000 -13.00700 34.42000  1.000 78.68000  ? 459 SER B OG  1 
ATOM   1345 N N   . ASN B 2 128 ? 24.11700 -10.07000 34.47200  1.000 75.20000  ? 460 ASN B N   1 
ATOM   1346 C CA  . ASN B 2 128 ? 25.33700 -9.69400  35.17700  1.000 73.37000  ? 460 ASN B CA  1 
ATOM   1347 C C   . ASN B 2 128 ? 25.71400 -10.74500 36.21600  1.000 72.99000  ? 460 ASN B C   1 
ATOM   1348 O O   . ASN B 2 128 ? 24.87900 -11.49400 36.71400  1.000 73.50000  ? 460 ASN B O   1 
ATOM   1349 C CB  . ASN B 2 128 ? 25.18700 -8.30800  35.81700  1.000 71.07000  ? 460 ASN B CB  1 
ATOM   1350 C CG  . ASN B 2 128 ? 25.05200 -7.20300  34.77300  1.000 78.78000  ? 460 ASN B CG  1 
ATOM   1351 O OD1 . ASN B 2 128 ? 25.60200 -7.30200  33.65900  1.000 85.35000  ? 460 ASN B OD1 1 
ATOM   1352 N ND2 . ASN B 2 128 ? 24.30200 -6.16000  35.10800  1.000 75.05000  ? 460 ASN B ND2 1 
ATOM   1353 N N   . LEU B 2 129 ? 27.00300 -10.83100 36.49400  1.000 75.57000  ? 461 LEU B N   1 
ATOM   1354 C CA  . LEU B 2 129 ? 27.48000 -11.68800 37.56100  1.000 70.35000  ? 461 LEU B CA  1 
ATOM   1355 C C   . LEU B 2 129 ? 27.02200 -11.18400 38.93000  1.000 75.14000  ? 461 LEU B C   1 
ATOM   1356 O O   . LEU B 2 129 ? 26.92400 -9.98100  39.17500  1.000 72.83000  ? 461 LEU B O   1 
ATOM   1357 C CB  . LEU B 2 129 ? 29.00100 -11.74500 37.53800  1.000 70.68000  ? 461 LEU B CB  1 
ATOM   1358 C CG  . LEU B 2 129 ? 29.63800 -12.64100 36.50400  1.000 69.00000  ? 461 LEU B CG  1 
ATOM   1359 C CD1 . LEU B 2 129 ? 31.13500 -12.66800 36.73300  1.000 66.87000  ? 461 LEU B CD1 1 
ATOM   1360 C CD2 . LEU B 2 129 ? 29.07000 -14.01400 36.66000  1.000 70.88000  ? 461 LEU B CD2 1 
ATOM   1361 N N   . LYS B 2 130 ? 26.73700 -12.12200 39.82000  1.000 71.59000  ? 462 LYS B N   1 
ATOM   1362 C CA  . LYS B 2 130 ? 26.62600 -11.80400 41.22800  1.000 68.54000  ? 462 LYS B CA  1 
ATOM   1363 C C   . LYS B 2 130 ? 28.03400 -11.69900 41.81200  1.000 75.87000  ? 462 LYS B C   1 
ATOM   1364 O O   . LYS B 2 130 ? 29.00400 -12.12500 41.18100  1.000 72.65000  ? 462 LYS B O   1 
ATOM   1365 C CB  . LYS B 2 130 ? 25.82700 -12.88200 41.95800  1.000 75.91000  ? 462 LYS B CB  1 
ATOM   1366 C CG  . LYS B 2 130 ? 24.41500 -13.24000 41.44600  1.000 75.89000  ? 462 LYS B CG  1 
ATOM   1367 C CD  . LYS B 2 130 ? 23.96500 -14.48200 42.26300  1.000 82.91000  ? 462 LYS B CD  1 
ATOM   1368 C CE  . LYS B 2 130 ? 22.54200 -14.97400 42.02000  1.000 89.35000  ? 462 LYS B CE  1 
ATOM   1369 N NZ  . LYS B 2 130 ? 22.30100 -16.16500 42.89500  1.000 87.88000  ? 462 LYS B NZ  1 
ATOM   1370 N N   . PRO B 2 131 ? 28.19100 -11.13100 43.01100  1.000 70.82000  ? 463 PRO B N   1 
ATOM   1371 C CA  . PRO B 2 131 ? 29.54600 -10.95200 43.54100  1.000 69.65000  ? 463 PRO B CA  1 
ATOM   1372 C C   . PRO B 2 131 ? 30.20100 -12.28500 43.86600  1.000 73.01000  ? 463 PRO B C   1 
ATOM   1373 O O   . PRO B 2 131 ? 29.60500 -13.14600 44.51300  1.000 77.57000  ? 463 PRO B O   1 
ATOM   1374 C CB  . PRO B 2 131 ? 29.32000 -10.10700 44.79400  1.000 71.23000  ? 463 PRO B CB  1 
ATOM   1375 C CG  . PRO B 2 131 ? 28.12800 -9.31100  44.44400  1.000 74.85000  ? 463 PRO B CG  1 
ATOM   1376 C CD  . PRO B 2 131 ? 27.23200 -10.33200 43.78700  1.000 72.99000  ? 463 PRO B CD  1 
ATOM   1377 N N   . PHE B 2 132 ? 31.43600 -12.44600 43.39400  1.000 68.89000  ? 464 PHE B N   1 
ATOM   1378 C CA  . PHE B 2 132 ? 32.24200 -13.64400 43.57900  1.000 62.21000  ? 464 PHE B CA  1 
ATOM   1379 C C   . PHE B 2 132 ? 31.67500 -14.84200 42.82600  1.000 63.11000  ? 464 PHE B C   1 
ATOM   1380 O O   . PHE B 2 132 ? 32.20800 -15.94800 42.93200  1.000 66.91000  ? 464 PHE B O   1 
ATOM   1381 C CB  . PHE B 2 132 ? 32.41200 -13.93300 45.06300  1.000 66.76000  ? 464 PHE B CB  1 
ATOM   1382 C CG  . PHE B 2 132 ? 33.19400 -12.87500 45.78300  1.000 65.38000  ? 464 PHE B CG  1 
ATOM   1383 C CD1 . PHE B 2 132 ? 34.39600 -12.43900 45.26500  1.000 71.04000  ? 464 PHE B CD1 1 
ATOM   1384 C CD2 . PHE B 2 132 ? 32.73300 -12.31300 46.96600  1.000 61.79000  ? 464 PHE B CD2 1 
ATOM   1385 C CE1 . PHE B 2 132 ? 35.15600 -11.46600 45.90500  1.000 70.06000  ? 464 PHE B CE1 1 
ATOM   1386 C CE2 . PHE B 2 132 ? 33.49500 -11.31700 47.62600  1.000 66.17000  ? 464 PHE B CE2 1 
ATOM   1387 C CZ  . PHE B 2 132 ? 34.70400 -10.89500 47.07900  1.000 67.36000  ? 464 PHE B CZ  1 
ATOM   1388 N N   . GLU B 2 133 ? 30.61600 -14.64100 42.04400  1.000 70.73000  ? 465 GLU B N   1 
ATOM   1389 C CA  . GLU B 2 133 ? 30.16600 -15.65500 41.09800  1.000 70.12000  ? 465 GLU B CA  1 
ATOM   1390 C C   . GLU B 2 133 ? 31.23000 -15.89500 40.03300  1.000 71.39000  ? 465 GLU B C   1 
ATOM   1391 O O   . GLU B 2 133 ? 31.87500 -14.96100 39.54300  1.000 69.16000  ? 465 GLU B O   1 
ATOM   1392 C CB  . GLU B 2 133 ? 28.84900 -15.23500 40.44000  1.000 71.72000  ? 465 GLU B CB  1 
ATOM   1393 C CG  . GLU B 2 133 ? 28.11600 -16.36300 39.75000  1.000 67.58000  ? 465 GLU B CG  1 
ATOM   1394 C CD  . GLU B 2 133 ? 26.77600 -15.93400 39.12400  1.000 73.03000  ? 465 GLU B CD  1 
ATOM   1395 O OE1 . GLU B 2 133 ? 26.38400 -14.75600 39.26600  1.000 74.78000  ? 465 GLU B OE1 1 
ATOM   1396 O OE2 . GLU B 2 133 ? 26.10300 -16.78000 38.48600  1.000 72.57000  ? 465 GLU B OE2 1 
ATOM   1397 N N   . ARG B 2 134 ? 31.46600 -17.17800 39.75500  1.000 71.98000  ? 466 ARG B N   1 
ATOM   1398 C CA  . ARG B 2 134 ? 32.43400 -17.57600 38.70600  1.000 65.88000  ? 466 ARG B CA  1 
ATOM   1399 C C   . ARG B 2 134 ? 31.66600 -18.40400 37.68500  1.000 76.67000  ? 466 ARG B C   1 
ATOM   1400 O O   . ARG B 2 134 ? 31.13600 -19.45700 38.06600  1.000 79.84000  ? 466 ARG B O   1 
ATOM   1401 C CB  . ARG B 2 134 ? 33.58500 -18.40000 39.27600  1.000 70.02000  ? 466 ARG B CB  1 
ATOM   1402 C CG  . ARG B 2 134 ? 34.70900 -18.66200 38.28500  1.000 68.17000  ? 466 ARG B CG  1 
ATOM   1403 C CD  . ARG B 2 134 ? 36.02500 -18.80800 39.02100  1.000 69.39000  ? 466 ARG B CD  1 
ATOM   1404 N NE  . ARG B 2 134 ? 36.96600 -19.71800 38.38900  1.000 72.34000  ? 466 ARG B NE  1 
ATOM   1405 C CZ  . ARG B 2 134 ? 36.78900 -21.02700 38.27500  1.000 66.09000  ? 466 ARG B CZ  1 
ATOM   1406 N NH1 . ARG B 2 134 ? 35.69200 -21.59400 38.74600  1.000 71.27000  ? 466 ARG B NH1 1 
ATOM   1407 N NH2 . ARG B 2 134 ? 37.71000 -21.76700 37.68800  1.000 76.19000  ? 466 ARG B NH2 1 
ATOM   1408 N N   . ASP B 2 135 ? 31.59900 -17.93200 36.44700  1.000 76.70000  ? 467 ASP B N   1 
ATOM   1409 C CA  . ASP B 2 135 ? 30.86000 -18.59000 35.38400  1.000 67.77000  ? 467 ASP B CA  1 
ATOM   1410 C C   . ASP B 2 135 ? 31.88700 -19.08300 34.37200  1.000 70.92000  ? 467 ASP B C   1 
ATOM   1411 O O   . ASP B 2 135 ? 32.31000 -18.33700 33.49300  1.000 72.45000  ? 467 ASP B O   1 
ATOM   1412 C CB  . ASP B 2 135 ? 29.84700 -17.62200 34.75800  1.000 69.12000  ? 467 ASP B CB  1 
ATOM   1413 C CG  . ASP B 2 135 ? 29.04400 -18.26000 33.63000  1.000 76.52000  ? 467 ASP B CG  1 
ATOM   1414 O OD1 . ASP B 2 135 ? 29.28200 -19.46200 33.34500  1.000 72.91000  ? 467 ASP B OD1 1 
ATOM   1415 O OD2 . ASP B 2 135 ? 28.17100 -17.56700 33.03600  1.000 75.86000  ? 467 ASP B OD2 1 
ATOM   1416 N N   . ILE B 2 136 ? 32.27300 -20.35500 34.48600  1.000 75.57000  ? 468 ILE B N   1 
ATOM   1417 C CA  . ILE B 2 136 ? 33.20300 -20.93100 33.52500  1.000 70.19000  ? 468 ILE B CA  1 
ATOM   1418 C C   . ILE B 2 136 ? 32.44800 -21.73500 32.47000  1.000 61.83000  ? 468 ILE B C   1 
ATOM   1419 O O   . ILE B 2 136 ? 32.99700 -22.66700 31.86500  1.000 61.34000  ? 468 ILE B O   1 
ATOM   1420 C CB  . ILE B 2 136 ? 34.28100 -21.78700 34.21500  1.000 70.79000  ? 468 ILE B CB  1 
ATOM   1421 C CG1 . ILE B 2 136 ? 33.65700 -22.89800 35.05800  1.000 66.60000  ? 468 ILE B CG1 1 
ATOM   1422 C CG2 . ILE B 2 136 ? 35.23600 -20.90200 34.98000  1.000 64.15000  ? 468 ILE B CG2 1 
ATOM   1423 C CD1 . ILE B 2 136 ? 34.70800 -23.83900 35.67100  1.000 60.27000  ? 468 ILE B CD1 1 
ATOM   1424 N N   . SER B 2 137 ? 31.20200 -21.36000 32.21500  1.000 65.78000  ? 469 SER B N   1 
ATOM   1425 C CA  . SER B 2 137 ? 30.43500 -22.04600 31.18500  1.000 72.11000  ? 469 SER B CA  1 
ATOM   1426 C C   . SER B 2 137 ? 30.94900 -21.68300 29.78600  1.000 71.20000  ? 469 SER B C   1 
ATOM   1427 O O   . SER B 2 137 ? 31.54200 -20.62100 29.57100  1.000 65.19000  ? 469 SER B O   1 
ATOM   1428 C CB  . SER B 2 137 ? 28.95400 -21.70200 31.31500  1.000 64.40000  ? 469 SER B CB  1 
ATOM   1429 O OG  . SER B 2 137 ? 28.24500 -22.12200 30.17100  1.000 85.91000  ? 469 SER B OG  1 
ATOM   1430 N N   . THR B 2 138 ? 30.73700 -22.59400 28.83100  1.000 70.00000  ? 470 THR B N   1 
ATOM   1431 C CA  . THR B 2 138 ? 31.13200 -22.38000 27.44500  1.000 72.93000  ? 470 THR B CA  1 
ATOM   1432 C C   . THR B 2 138 ? 29.98200 -22.68100 26.51400  1.000 72.30000  ? 470 THR B C   1 
ATOM   1433 O O   . THR B 2 138 ? 30.17100 -23.25300 25.43900  1.000 76.05000  ? 470 THR B O   1 
ATOM   1434 C CB  . THR B 2 138 ? 32.34000 -23.23300 27.05400  1.000 77.64000  ? 470 THR B CB  1 
ATOM   1435 O OG1 . THR B 2 138 ? 31.92500 -24.59100 26.89300  1.000 75.04000  ? 470 THR B OG1 1 
ATOM   1436 C CG2 . THR B 2 138 ? 33.42600 -23.17400 28.12200  1.000 77.72000  ? 470 THR B CG2 1 
ATOM   1437 N N   . GLU B 2 139 ? 28.76700 -22.31500 26.89300  1.000 75.04000  ? 471 GLU B N   1 
ATOM   1438 C CA  . GLU B 2 139 ? 27.66200 -22.52500 25.97000  1.000 77.19000  ? 471 GLU B CA  1 
ATOM   1439 C C   . GLU B 2 139 ? 27.60500 -21.40900 24.93000  1.000 79.13000  ? 471 GLU B C   1 
ATOM   1440 O O   . GLU B 2 139 ? 27.97100 -20.25800 25.19400  1.000 83.45000  ? 471 GLU B O   1 
ATOM   1441 C CB  . GLU B 2 139 ? 26.32900 -22.61700 26.71400  1.000 81.77000  ? 471 GLU B CB  1 
ATOM   1442 C CG  . GLU B 2 139 ? 25.93900 -24.02600 27.15800  1.000 91.12000  ? 471 GLU B CG  1 
ATOM   1443 C CD  . GLU B 2 139 ? 25.44400 -24.03800 28.59400  1.000 100.34000 ? 471 GLU B CD  1 
ATOM   1444 O OE1 . GLU B 2 139 ? 25.00400 -22.96500 29.06300  1.000 99.49000  ? 471 GLU B OE1 1 
ATOM   1445 O OE2 . GLU B 2 139 ? 25.51200 -25.10100 29.25700  1.000 99.95000  ? 471 GLU B OE2 1 
ATOM   1446 N N   . ILE B 2 140 ? 27.12200 -21.76600 23.73900  1.000 74.25000  ? 472 ILE B N   1 
ATOM   1447 C CA  . ILE B 2 140 ? 27.02300 -20.82800 22.63000  1.000 79.67000  ? 472 ILE B CA  1 
ATOM   1448 C C   . ILE B 2 140 ? 25.92600 -19.81200 22.91400  1.000 79.07000  ? 472 ILE B C   1 
ATOM   1449 O O   . ILE B 2 140 ? 24.79500 -20.17300 23.26700  1.000 72.98000  ? 472 ILE B O   1 
ATOM   1450 C CB  . ILE B 2 140 ? 26.75100 -21.57800 21.31700  1.000 79.86000  ? 472 ILE B CB  1 
ATOM   1451 C CG1 . ILE B 2 140 ? 27.83500 -22.62600 21.06600  1.000 80.86000  ? 472 ILE B CG1 1 
ATOM   1452 C CG2 . ILE B 2 140 ? 26.63700 -20.60200 20.13100  1.000 71.85000  ? 472 ILE B CG2 1 
ATOM   1453 C CD1 . ILE B 2 140 ? 27.60500 -23.94600 21.80200  1.000 88.14000  ? 472 ILE B CD1 1 
ATOM   1454 N N   . TYR B 2 141 ? 26.24600 -18.53600 22.73400  1.000 74.12000  ? 473 TYR B N   1 
ATOM   1455 C CA  . TYR B 2 141 ? 25.38100 -17.46300 23.19800  1.000 73.38000  ? 473 TYR B CA  1 
ATOM   1456 C C   . TYR B 2 141 ? 24.37700 -17.11700 22.10900  1.000 77.90000  ? 473 TYR B C   1 
ATOM   1457 O O   . TYR B 2 141 ? 24.76500 -16.72400 21.00700  1.000 79.64000  ? 473 TYR B O   1 
ATOM   1458 C CB  . TYR B 2 141 ? 26.20900 -16.24200 23.58700  1.000 72.30000  ? 473 TYR B CB  1 
ATOM   1459 C CG  . TYR B 2 141 ? 25.39300 -15.11300 24.13300  1.000 74.95000  ? 473 TYR B CG  1 
ATOM   1460 C CD1 . TYR B 2 141 ? 25.07700 -15.05500 25.46700  1.000 72.03000  ? 473 TYR B CD1 1 
ATOM   1461 C CD2 . TYR B 2 141 ? 24.92400 -14.10700 23.30700  1.000 79.18000  ? 473 TYR B CD2 1 
ATOM   1462 C CE1 . TYR B 2 141 ? 24.32800 -14.02100 25.98400  1.000 73.64000  ? 473 TYR B CE1 1 
ATOM   1463 C CE2 . TYR B 2 141 ? 24.16600 -13.06600 23.80900  1.000 77.68000  ? 473 TYR B CE2 1 
ATOM   1464 C CZ  . TYR B 2 141 ? 23.87500 -13.02600 25.15800  1.000 70.82000  ? 473 TYR B CZ  1 
ATOM   1465 O OH  . TYR B 2 141 ? 23.12700 -11.98600 25.67500  1.000 77.53000  ? 473 TYR B OH  1 
ATOM   1466 N N   . GLN B 2 142 ? 23.09200 -17.26100 22.42200  1.000 79.19000  ? 474 GLN B N   1 
ATOM   1467 C CA  . GLN B 2 142 ? 22.01700 -16.91000 21.50600  1.000 76.94000  ? 474 GLN B CA  1 
ATOM   1468 C C   . GLN B 2 142 ? 21.69800 -15.42900 21.66600  1.000 78.89000  ? 474 GLN B C   1 
ATOM   1469 O O   . GLN B 2 142 ? 21.12300 -15.01500 22.67900  1.000 75.00000  ? 474 GLN B O   1 
ATOM   1470 C CB  . GLN B 2 142 ? 20.78300 -17.76700 21.76200  1.000 70.46000  ? 474 GLN B CB  1 
ATOM   1471 C CG  . GLN B 2 142 ? 19.53900 -17.24900 21.07100  1.000 78.66000  ? 474 GLN B CG  1 
ATOM   1472 C CD  . GLN B 2 142 ? 18.45200 -18.27900 21.04700  1.000 79.35000  ? 474 GLN B CD  1 
ATOM   1473 O OE1 . GLN B 2 142 ? 18.68500 -19.42700 21.39100  1.000 83.45000  ? 474 GLN B OE1 1 
ATOM   1474 N NE2 . GLN B 2 142 ? 17.25900 -17.88400 20.64700  1.000 78.42000  ? 474 GLN B NE2 1 
ATOM   1475 N N   . ALA B 2 143 ? 22.05000 -14.63500 20.64900  1.000 87.21000  ? 475 ALA B N   1 
ATOM   1476 C CA  . ALA B 2 143 ? 21.82500 -13.19200 20.64300  1.000 84.62000  ? 475 ALA B CA  1 
ATOM   1477 C C   . ALA B 2 143 ? 20.53900 -12.77700 19.93100  1.000 85.89000  ? 475 ALA B C   1 
ATOM   1478 O O   . ALA B 2 143 ? 19.97400 -11.72300 20.24800  1.000 85.46000  ? 475 ALA B O   1 
ATOM   1479 C CB  . ALA B 2 143 ? 23.01300 -12.48600 19.98500  1.000 80.58000  ? 475 ALA B CB  1 
ATOM   1480 N N   . GLY B 2 144 ? 20.06400 -13.56800 18.97500  1.000 82.31000  ? 476 GLY B N   1 
ATOM   1481 C CA  . GLY B 2 144 ? 18.84900 -13.23400 18.27200  1.000 84.48000  ? 476 GLY B CA  1 
ATOM   1482 C C   . GLY B 2 144 ? 17.77900 -14.28200 18.45000  1.000 85.30000  ? 476 GLY B C   1 
ATOM   1483 O O   . GLY B 2 144 ? 17.85500 -15.11700 19.35400  1.000 87.38000  ? 476 GLY B O   1 
ATOM   1484 N N   . SER B 2 145 ? 16.76000 -14.22800 17.60900  1.000 85.57000  ? 477 SER B N   1 
ATOM   1485 C CA  . SER B 2 145 ? 15.63600 -15.13500 17.73900  1.000 86.84000  ? 477 SER B CA  1 
ATOM   1486 C C   . SER B 2 145 ? 15.88500 -16.46600 17.06700  1.000 85.98000  ? 477 SER B C   1 
ATOM   1487 O O   . SER B 2 145 ? 14.93700 -17.23400 16.90700  1.000 93.09000  ? 477 SER B O   1 
ATOM   1488 C CB  . SER B 2 145 ? 14.35600 -14.49400 17.18200  1.000 86.93000  ? 477 SER B CB  1 
ATOM   1489 O OG  . SER B 2 145 ? 14.60500 -13.79800 15.97300  1.000 94.63000  ? 477 SER B OG  1 
ATOM   1490 N N   . THR B 2 146 ? 17.11000 -16.77400 16.66100  1.000 84.76000  ? 478 THR B N   1 
ATOM   1491 C CA  . THR B 2 146 ? 17.24300 -18.04000 15.95000  1.000 89.07000  ? 478 THR B CA  1 
ATOM   1492 C C   . THR B 2 146 ? 18.06600 -19.02400 16.75800  1.000 84.32000  ? 478 THR B C   1 
ATOM   1493 O O   . THR B 2 146 ? 19.21300 -18.72900 17.11700  1.000 83.88000  ? 478 THR B O   1 
ATOM   1494 C CB  . THR B 2 146 ? 17.87400 -17.86700 14.54200  1.000 93.46000  ? 478 THR B CB  1 
ATOM   1495 O OG1 . THR B 2 146 ? 19.06300 -17.05900 14.62300  1.000 90.19000  ? 478 THR B OG1 1 
ATOM   1496 C CG2 . THR B 2 146 ? 16.86100 -17.26800 13.53200  1.000 87.52000  ? 478 THR B CG2 1 
ATOM   1497 N N   . PRO B 2 147 ? 17.52400 -20.21700 16.98300  1.000 84.55000  ? 479 PRO B N   1 
ATOM   1498 C CA  . PRO B 2 147 ? 18.20100 -21.21800 17.81000  1.000 83.11000  ? 479 PRO B CA  1 
ATOM   1499 C C   . PRO B 2 147 ? 19.60900 -21.51300 17.32300  1.000 85.64000  ? 479 PRO B C   1 
ATOM   1500 O O   . PRO B 2 147 ? 19.87900 -21.55600 16.12400  1.000 90.99000  ? 479 PRO B O   1 
ATOM   1501 C CB  . PRO B 2 147 ? 17.30700 -22.45300 17.66100  1.000 87.07000  ? 479 PRO B CB  1 
ATOM   1502 C CG  . PRO B 2 147 ? 16.01300 -21.94200 17.16300  1.000 88.90000  ? 479 PRO B CG  1 
ATOM   1503 C CD  . PRO B 2 147 ? 16.33100 -20.76300 16.32400  1.000 91.96000  ? 479 PRO B CD  1 
ATOM   1504 N N   . CYS B 2 148 ? 20.50900 -21.75400 18.27200  1.000 81.34000  ? 480 CYS B N   1 
ATOM   1505 C CA  . CYS B 2 148 ? 21.90400 -21.98200 17.94000  1.000 75.89000  ? 480 CYS B CA  1 
ATOM   1506 C C   . CYS B 2 148 ? 22.27700 -23.44600 17.90200  1.000 80.70000  ? 480 CYS B C   1 
ATOM   1507 O O   . CYS B 2 148 ? 23.36200 -23.78200 17.40800  1.000 82.41000  ? 480 CYS B O   1 
ATOM   1508 C CB  . CYS B 2 148 ? 22.78900 -21.25800 18.93300  1.000 75.61000  ? 480 CYS B CB  1 
ATOM   1509 S SG  . CYS B 2 148 ? 22.27600 -19.56500 19.06800  1.000 88.39000  ? 480 CYS B SG  1 
ATOM   1510 N N   . ASN B 2 149 ? 21.41700 -24.31700 18.42500  1.000 84.63000  ? 481 ASN B N   1 
ATOM   1511 C CA  . ASN B 2 149 ? 21.60600 -25.76200 18.35700  1.000 86.11000  ? 481 ASN B CA  1 
ATOM   1512 C C   . ASN B 2 149 ? 22.98600 -26.19700 18.85500  1.000 88.19000  ? 481 ASN B C   1 
ATOM   1513 O O   . ASN B 2 149 ? 23.43000 -27.32000 18.58900  1.000 89.96000  ? 481 ASN B O   1 
ATOM   1514 C CB  . ASN B 2 149 ? 21.34700 -26.25200 16.93900  1.000 79.21000  ? 481 ASN B CB  1 
ATOM   1515 C CG  . ASN B 2 149 ? 19.94800 -25.94200 16.49000  1.000 84.57000  ? 481 ASN B CG  1 
ATOM   1516 O OD1 . ASN B 2 149 ? 18.98500 -26.15400 17.22600  1.000 75.84000  ? 481 ASN B OD1 1 
ATOM   1517 N ND2 . ASN B 2 149 ? 19.82100 -25.41300 15.27600  1.000 93.52000  ? 481 ASN B ND2 1 
ATOM   1518 N N   . GLY B 2 150 ? 23.65900 -25.33400 19.61200  1.000 85.03000  ? 482 GLY B N   1 
ATOM   1519 C CA  . GLY B 2 150 ? 24.97500 -25.65500 20.11500  1.000 81.50000  ? 482 GLY B CA  1 
ATOM   1520 C C   . GLY B 2 150 ? 26.11500 -25.43400 19.14700  1.000 83.90000  ? 482 GLY B C   1 
ATOM   1521 O O   . GLY B 2 150 ? 27.19200 -26.01100 19.34400  1.000 86.78000  ? 482 GLY B O   1 
ATOM   1522 N N   . VAL B 2 151 ? 25.93400 -24.61200 18.11100  1.000 78.92000  ? 483 VAL B N   1 
ATOM   1523 C CA  . VAL B 2 151 ? 27.00300 -24.33900 17.16000  1.000 74.16000  ? 483 VAL B CA  1 
ATOM   1524 C C   . VAL B 2 151 ? 26.95900 -22.86900 16.76700  1.000 75.99000  ? 483 VAL B C   1 
ATOM   1525 O O   . VAL B 2 151 ? 25.88100 -22.27100 16.64800  1.000 74.09000  ? 483 VAL B O   1 
ATOM   1526 C CB  . VAL B 2 151 ? 26.92200 -25.25000 15.91100  1.000 76.07000  ? 483 VAL B CB  1 
ATOM   1527 C CG1 . VAL B 2 151 ? 27.19100 -26.70800 16.28400  1.000 73.82000  ? 483 VAL B CG1 1 
ATOM   1528 C CG2 . VAL B 2 151 ? 25.57300 -25.12100 15.23000  1.000 78.98000  ? 483 VAL B CG2 1 
ATOM   1529 N N   . GLU B 2 152 ? 28.14400 -22.28800 16.57300  1.000 70.52000  ? 484 GLU B N   1 
ATOM   1530 C CA  . GLU B 2 152 ? 28.27100 -20.87200 16.27500  1.000 69.33000  ? 484 GLU B CA  1 
ATOM   1531 C C   . GLU B 2 152 ? 27.83600 -20.58000 14.84400  1.000 72.67000  ? 484 GLU B C   1 
ATOM   1532 O O   . GLU B 2 152 ? 27.83800 -21.45300 13.97400  1.000 72.07000  ? 484 GLU B O   1 
ATOM   1533 C CB  . GLU B 2 152 ? 29.71100 -20.40500 16.49700  1.000 69.97000  ? 484 GLU B CB  1 
ATOM   1534 C CG  . GLU B 2 152 ? 30.51100 -21.39200 17.27400  1.000 61.79000  ? 484 GLU B CG  1 
ATOM   1535 C CD  . GLU B 2 152 ? 31.99100 -21.09400 17.26700  1.000 67.53000  ? 484 GLU B CD  1 
ATOM   1536 O OE1 . GLU B 2 152 ? 32.40400 -19.89500 17.20400  1.000 65.11000  ? 484 GLU B OE1 1 
ATOM   1537 O OE2 . GLU B 2 152 ? 32.74600 -22.09600 17.33900  1.000 71.13000  ? 484 GLU B OE2 1 
ATOM   1538 N N   . GLY B 2 153 ? 27.50500 -19.31500 14.60400  1.000 67.81000  ? 485 GLY B N   1 
ATOM   1539 C CA  . GLY B 2 153 ? 26.60300 -18.96100 13.52200  1.000 62.43000  ? 485 GLY B CA  1 
ATOM   1540 C C   . GLY B 2 153 ? 26.06500 -17.56200 13.71900  1.000 71.96000  ? 485 GLY B C   1 
ATOM   1541 O O   . GLY B 2 153 ? 26.74100 -16.69800 14.28100  1.000 77.72000  ? 485 GLY B O   1 
ATOM   1542 N N   . PHE B 2 154 ? 24.83900 -17.35000 13.26000  1.000 76.76000  ? 486 PHE B N   1 
ATOM   1543 C CA  . PHE B 2 154 ? 24.28100 -16.00700 13.14000  1.000 81.51000  ? 486 PHE B CA  1 
ATOM   1544 C C   . PHE B 2 154 ? 23.57500 -15.62900 14.44100  1.000 84.16000  ? 486 PHE B C   1 
ATOM   1545 O O   . PHE B 2 154 ? 22.55600 -16.23100 14.78600  1.000 85.19000  ? 486 PHE B O   1 
ATOM   1546 C CB  . PHE B 2 154 ? 23.31700 -15.92800 11.95200  1.000 83.30000  ? 486 PHE B CB  1 
ATOM   1547 C CG  . PHE B 2 154 ? 22.74400 -14.55700 11.72900  1.000 87.40000  ? 486 PHE B CG  1 
ATOM   1548 C CD1 . PHE B 2 154 ? 23.48500 -13.58700 11.07300  1.000 93.38000  ? 486 PHE B CD1 1 
ATOM   1549 C CD2 . PHE B 2 154 ? 21.46600 -14.23100 12.17100  1.000 80.90000  ? 486 PHE B CD2 1 
ATOM   1550 C CE1 . PHE B 2 154 ? 22.96800 -12.32100 10.85800  1.000 92.55000  ? 486 PHE B CE1 1 
ATOM   1551 C CE2 . PHE B 2 154 ? 20.94300 -12.96300 11.96500  1.000 85.53000  ? 486 PHE B CE2 1 
ATOM   1552 C CZ  . PHE B 2 154 ? 21.69900 -12.00700 11.31300  1.000 93.75000  ? 486 PHE B CZ  1 
ATOM   1553 N N   . ASN B 2 155 ? 24.09000 -14.61300 15.13600  1.000 85.44000  ? 487 ASN B N   1 
ATOM   1554 C CA  . ASN B 2 155 ? 23.66400 -14.30900 16.51100  1.000 84.22000  ? 487 ASN B CA  1 
ATOM   1555 C C   . ASN B 2 155 ? 23.85000 -15.50500 17.43700  1.000 81.86000  ? 487 ASN B C   1 
ATOM   1556 O O   . ASN B 2 155 ? 23.08600 -15.69700 18.38500  1.000 85.09000  ? 487 ASN B O   1 
ATOM   1557 C CB  . ASN B 2 155 ? 22.21900 -13.82500 16.57100  1.000 85.12000  ? 487 ASN B CB  1 
ATOM   1558 C CG  . ASN B 2 155 ? 22.00000 -12.60600 15.75300  1.000 85.56000  ? 487 ASN B CG  1 
ATOM   1559 O OD1 . ASN B 2 155 ? 20.93500 -12.42700 15.16400  1.000 90.08000  ? 487 ASN B OD1 1 
ATOM   1560 N ND2 . ASN B 2 155 ? 23.01800 -11.75200 15.69300  1.000 85.09000  ? 487 ASN B ND2 1 
ATOM   1561 N N   . CYS B 2 156 ? 24.87400 -16.31300 17.16300  1.000 76.59000  ? 488 CYS B N   1 
ATOM   1562 C CA  . CYS B 2 156 ? 25.16000 -17.49800 17.97000  1.000 75.80000  ? 488 CYS B CA  1 
ATOM   1563 C C   . CYS B 2 156 ? 26.67900 -17.56400 18.14800  1.000 74.32000  ? 488 CYS B C   1 
ATOM   1564 O O   . CYS B 2 156 ? 27.37500 -18.20200 17.36600  1.000 72.86000  ? 488 CYS B O   1 
ATOM   1565 C CB  . CYS B 2 156 ? 24.59400 -18.75100 17.32000  1.000 75.16000  ? 488 CYS B CB  1 
ATOM   1566 S SG  . CYS B 2 156 ? 22.78100 -18.73600 17.27800  1.000 81.98000  ? 488 CYS B SG  1 
ATOM   1567 N N   . TYR B 2 157 ? 27.17100 -16.90900 19.20200  1.000 74.70000  ? 489 TYR B N   1 
ATOM   1568 C CA  . TYR B 2 157 ? 28.57600 -16.56200 19.35300  1.000 71.36000  ? 489 TYR B CA  1 
ATOM   1569 C C   . TYR B 2 157 ? 29.19300 -17.33100 20.50900  1.000 74.72000  ? 489 TYR B C   1 
ATOM   1570 O O   . TYR B 2 157 ? 28.56800 -17.48100 21.56300  1.000 79.79000  ? 489 TYR B O   1 
ATOM   1571 C CB  . TYR B 2 157 ? 28.71400 -15.05600 19.59300  1.000 72.13000  ? 489 TYR B CB  1 
ATOM   1572 C CG  . TYR B 2 157 ? 27.93000 -14.24800 18.59800  1.000 73.99000  ? 489 TYR B CG  1 
ATOM   1573 C CD1 . TYR B 2 157 ? 27.91200 -14.61800 17.24900  1.000 79.15000  ? 489 TYR B CD1 1 
ATOM   1574 C CD2 . TYR B 2 157 ? 27.20000 -13.13700 18.98300  1.000 74.35000  ? 489 TYR B CD2 1 
ATOM   1575 C CE1 . TYR B 2 157 ? 27.20100 -13.90900 16.31600  1.000 77.72000  ? 489 TYR B CE1 1 
ATOM   1576 C CE2 . TYR B 2 157 ? 26.48400 -12.40500 18.04500  1.000 82.38000  ? 489 TYR B CE2 1 
ATOM   1577 C CZ  . TYR B 2 157 ? 26.49500 -12.80100 16.70400  1.000 79.62000  ? 489 TYR B CZ  1 
ATOM   1578 O OH  . TYR B 2 157 ? 25.77800 -12.11700 15.73900  1.000 74.84000  ? 489 TYR B OH  1 
ATOM   1579 N N   . PHE B 2 158 ? 30.41300 -17.81100 20.31400  1.000 68.78000  ? 490 PHE B N   1 
ATOM   1580 C CA  . PHE B 2 158 ? 31.18100 -18.38600 21.41000  1.000 71.72000  ? 490 PHE B CA  1 
ATOM   1581 C C   . PHE B 2 158 ? 31.45000 -17.29200 22.44400  1.000 70.50000  ? 490 PHE B C   1 
ATOM   1582 O O   . PHE B 2 158 ? 32.02600 -16.24700 22.09400  1.000 73.72000  ? 490 PHE B O   1 
ATOM   1583 C CB  . PHE B 2 158 ? 32.48700 -18.98600 20.88000  1.000 71.50000  ? 490 PHE B CB  1 
ATOM   1584 C CG  . PHE B 2 158 ? 33.24400 -19.81600 21.89300  1.000 69.97000  ? 490 PHE B CG  1 
ATOM   1585 C CD1 . PHE B 2 158 ? 32.88400 -21.12700 22.14300  1.000 70.39000  ? 490 PHE B CD1 1 
ATOM   1586 C CD2 . PHE B 2 158 ? 34.32100 -19.28500 22.58900  1.000 68.76000  ? 490 PHE B CD2 1 
ATOM   1587 C CE1 . PHE B 2 158 ? 33.58400 -21.89500 23.06300  1.000 69.80000  ? 490 PHE B CE1 1 
ATOM   1588 C CE2 . PHE B 2 158 ? 35.02400 -20.05200 23.51800  1.000 71.78000  ? 490 PHE B CE2 1 
ATOM   1589 C CZ  . PHE B 2 158 ? 34.65500 -21.35500 23.75300  1.000 71.75000  ? 490 PHE B CZ  1 
ATOM   1590 N N   . PRO B 2 159 ? 31.05000 -17.47600 23.70700  1.000 63.76000  ? 491 PRO B N   1 
ATOM   1591 C CA  . PRO B 2 159 ? 31.00200 -16.33500 24.63300  1.000 64.99000  ? 491 PRO B CA  1 
ATOM   1592 C C   . PRO B 2 159 ? 32.37000 -15.87300 25.10100  1.000 67.88000  ? 491 PRO B C   1 
ATOM   1593 O O   . PRO B 2 159 ? 32.50100 -14.74100 25.59400  1.000 71.00000  ? 491 PRO B O   1 
ATOM   1594 C CB  . PRO B 2 159 ? 30.16000 -16.87200 25.78500  1.000 71.73000  ? 491 PRO B CB  1 
ATOM   1595 C CG  . PRO B 2 159 ? 30.42900 -18.33600 25.78400  1.000 69.54000  ? 491 PRO B CG  1 
ATOM   1596 C CD  . PRO B 2 159 ? 30.62000 -18.72900 24.35000  1.000 70.93000  ? 491 PRO B CD  1 
ATOM   1597 N N   . LEU B 2 160 ? 33.39900 -16.69000 24.93000  1.000 65.37000  ? 492 LEU B N   1 
ATOM   1598 C CA  . LEU B 2 160 ? 34.75300 -16.32200 25.29800  1.000 60.93000  ? 492 LEU B CA  1 
ATOM   1599 C C   . LEU B 2 160 ? 35.49600 -15.78800 24.08500  1.000 76.80000  ? 492 LEU B C   1 
ATOM   1600 O O   . LEU B 2 160 ? 35.50500 -16.40700 23.00800  1.000 77.45000  ? 492 LEU B O   1 
ATOM   1601 C CB  . LEU B 2 160 ? 35.49700 -17.51400 25.89100  1.000 69.12000  ? 492 LEU B CB  1 
ATOM   1602 C CG  . LEU B 2 160 ? 34.77100 -18.13500 27.09100  1.000 68.74000  ? 492 LEU B CG  1 
ATOM   1603 C CD1 . LEU B 2 160 ? 35.66500 -19.15900 27.71300  1.000 70.87000  ? 492 LEU B CD1 1 
ATOM   1604 C CD2 . LEU B 2 160 ? 34.33600 -17.10600 28.09800  1.000 67.37000  ? 492 LEU B CD2 1 
ATOM   1605 N N   . GLN B 2 161 ? 36.10100 -14.63100 24.26800  1.000 75.19000  ? 493 GLN B N   1 
ATOM   1606 C CA  . GLN B 2 161 ? 36.95300 -13.99800 23.28700  1.000 72.32000  ? 493 GLN B CA  1 
ATOM   1607 C C   . GLN B 2 161 ? 38.32500 -13.88900 23.93300  1.000 73.88000  ? 493 GLN B C   1 
ATOM   1608 O O   . GLN B 2 161 ? 38.42100 -13.69600 25.14800  1.000 78.48000  ? 493 GLN B O   1 
ATOM   1609 C CB  . GLN B 2 161 ? 36.37700 -12.62800 22.91000  1.000 76.96000  ? 493 GLN B CB  1 
ATOM   1610 C CG  . GLN B 2 161 ? 36.52700 -12.23600 21.43900  1.000 78.41000  ? 493 GLN B CG  1 
ATOM   1611 C CD  . GLN B 2 161 ? 35.94100 -13.26600 20.48600  1.000 73.28000  ? 493 GLN B CD  1 
ATOM   1612 O OE1 . GLN B 2 161 ? 36.65900 -13.84700 19.68500  1.000 77.17000  ? 493 GLN B OE1 1 
ATOM   1613 N NE2 . GLN B 2 161 ? 34.63500 -13.49600 20.57400  1.000 78.66000  ? 493 GLN B NE2 1 
ATOM   1614 N N   . SER B 2 162 ? 39.38800 -14.06100 23.16200  1.000 68.16000  ? 494 SER B N   1 
ATOM   1615 C CA  . SER B 2 162 ? 40.71200 -14.02300 23.75000  1.000 61.80000  ? 494 SER B CA  1 
ATOM   1616 C C   . SER B 2 162 ? 41.30300 -12.63200 23.66200  1.000 67.67000  ? 494 SER B C   1 
ATOM   1617 O O   . SER B 2 162 ? 40.98400 -11.86000 22.76400  1.000 71.53000  ? 494 SER B O   1 
ATOM   1618 C CB  . SER B 2 162 ? 41.66100 -14.99700 23.08800  1.000 71.79000  ? 494 SER B CB  1 
ATOM   1619 O OG  . SER B 2 162 ? 42.98100 -14.55600 23.33500  1.000 77.43000  ? 494 SER B OG  1 
ATOM   1620 N N   . TYR B 2 163 ? 42.12900 -12.29700 24.64200  1.000 73.84000  ? 495 TYR B N   1 
ATOM   1621 C CA  . TYR B 2 163 ? 42.96500 -11.12800 24.49200  1.000 75.50000  ? 495 TYR B CA  1 
ATOM   1622 C C   . TYR B 2 163 ? 44.00900 -11.42800 23.44000  1.000 81.55000  ? 495 TYR B C   1 
ATOM   1623 O O   . TYR B 2 163 ? 44.30500 -12.58600 23.13500  1.000 92.78000  ? 495 TYR B O   1 
ATOM   1624 C CB  . TYR B 2 163 ? 43.65700 -10.76400 25.80100  1.000 81.40000  ? 495 TYR B CB  1 
ATOM   1625 C CG  . TYR B 2 163 ? 42.74000 -10.27200 26.89500  1.000 76.46000  ? 495 TYR B CG  1 
ATOM   1626 C CD1 . TYR B 2 163 ? 42.19500 -9.00300  26.84500  1.000 74.47000  ? 495 TYR B CD1 1 
ATOM   1627 C CD2 . TYR B 2 163 ? 42.43700 -11.07000 27.97900  1.000 80.08000  ? 495 TYR B CD2 1 
ATOM   1628 C CE1 . TYR B 2 163 ? 41.37100 -8.54500  27.82700  1.000 77.94000  ? 495 TYR B CE1 1 
ATOM   1629 C CE2 . TYR B 2 163 ? 41.60800 -10.60800 28.97900  1.000 78.38000  ? 495 TYR B CE2 1 
ATOM   1630 C CZ  . TYR B 2 163 ? 41.08400 -9.34700  28.89300  1.000 77.45000  ? 495 TYR B CZ  1 
ATOM   1631 O OH  . TYR B 2 163 ? 40.26000 -8.89100  29.88600  1.000 80.96000  ? 495 TYR B OH  1 
ATOM   1632 N N   . GLY B 2 164 ? 44.58700 -10.38800 22.89200  1.000 80.19000  ? 496 GLY B N   1 
ATOM   1633 C CA  . GLY B 2 164 ? 45.53200 -10.67700 21.84000  1.000 85.95000  ? 496 GLY B CA  1 
ATOM   1634 C C   . GLY B 2 164 ? 46.90500 -10.22700 22.24900  1.000 88.21000  ? 496 GLY B C   1 
ATOM   1635 O O   . GLY B 2 164 ? 47.65400 -9.70300  21.42000  1.000 94.89000  ? 496 GLY B O   1 
ATOM   1636 N N   . PHE B 2 165 ? 47.22800 -10.42300 23.52200  1.000 80.16000  ? 497 PHE B N   1 
ATOM   1637 C CA  . PHE B 2 165 ? 48.34600 -9.72100  24.13100  1.000 85.05000  ? 497 PHE B CA  1 
ATOM   1638 C C   . PHE B 2 165 ? 49.56100 -9.77100  23.22700  1.000 84.85000  ? 497 PHE B C   1 
ATOM   1639 O O   . PHE B 2 165 ? 50.00800 -10.85000 22.83100  1.000 86.17000  ? 497 PHE B O   1 
ATOM   1640 C CB  . PHE B 2 165 ? 48.66400 -10.31900 25.50400  1.000 86.35000  ? 497 PHE B CB  1 
ATOM   1641 C CG  . PHE B 2 165 ? 47.59000 -10.09300 26.52100  1.000 80.71000  ? 497 PHE B CG  1 
ATOM   1642 C CD1 . PHE B 2 165 ? 46.97800 -8.86000  26.62800  1.000 85.84000  ? 497 PHE B CD1 1 
ATOM   1643 C CD2 . PHE B 2 165 ? 47.17000 -11.11300 27.35900  1.000 82.25000  ? 497 PHE B CD2 1 
ATOM   1644 C CE1 . PHE B 2 165 ? 45.97500 -8.63300  27.56800  1.000 80.18000  ? 497 PHE B CE1 1 
ATOM   1645 C CE2 . PHE B 2 165 ? 46.15900 -10.89600 28.30000  1.000 78.44000  ? 497 PHE B CE2 1 
ATOM   1646 C CZ  . PHE B 2 165 ? 45.56900 -9.65500  28.39900  1.000 79.33000  ? 497 PHE B CZ  1 
ATOM   1647 N N   . GLN B 2 166 ? 50.03300 -8.59000  22.83400  1.000 85.81000  ? 498 GLN B N   1 
ATOM   1648 C CA  . GLN B 2 166 ? 51.27100 -8.43900  22.09600  1.000 88.64000  ? 498 GLN B CA  1 
ATOM   1649 C C   . GLN B 2 166 ? 52.08700 -7.32000  22.71400  1.000 89.64000  ? 498 GLN B C   1 
ATOM   1650 O O   . GLN B 2 166 ? 51.53300 -6.28100  23.09500  1.000 89.06000  ? 498 GLN B O   1 
ATOM   1651 C CB  . GLN B 2 166 ? 51.02900 -8.11200  20.63400  1.000 87.15000  ? 498 GLN B CB  1 
ATOM   1652 C CG  . GLN B 2 166 ? 50.32600 -9.17000  19.89500  1.000 85.34000  ? 498 GLN B CG  1 
ATOM   1653 C CD  . GLN B 2 166 ? 49.62800 -8.59200  18.72300  1.000 90.90000  ? 498 GLN B CD  1 
ATOM   1654 O OE1 . GLN B 2 166 ? 49.81800 -7.41900  18.42200  1.000 93.19000  ? 498 GLN B OE1 1 
ATOM   1655 N NE2 . GLN B 2 166 ? 48.79800 -9.38800  18.05500  1.000 95.12000  ? 498 GLN B NE2 1 
ATOM   1656 N N   . PRO B 2 167 ? 53.40900 -7.49400  22.78000  1.000 87.35000  ? 499 PRO B N   1 
ATOM   1657 C CA  . PRO B 2 167 ? 54.25400 -6.54600  23.52800  1.000 86.44000  ? 499 PRO B CA  1 
ATOM   1658 C C   . PRO B 2 167 ? 54.17000 -5.13300  23.00400  1.000 90.84000  ? 499 PRO B C   1 
ATOM   1659 O O   . PRO B 2 167 ? 54.33100 -4.17200  23.77400  1.000 91.78000  ? 499 PRO B O   1 
ATOM   1660 C CB  . PRO B 2 167 ? 55.66100 -7.12800  23.35900  1.000 83.36000  ? 499 PRO B CB  1 
ATOM   1661 C CG  . PRO B 2 167 ? 55.56600 -8.01200  22.13400  1.000 88.65000  ? 499 PRO B CG  1 
ATOM   1662 C CD  . PRO B 2 167 ? 54.17800 -8.53300  22.07300  1.000 88.00000  ? 499 PRO B CD  1 
ATOM   1663 N N   . THR B 2 168 ? 53.90500 -4.99100  21.70800  1.000 87.55000  ? 500 THR B N   1 
ATOM   1664 C CA  . THR B 2 168 ? 53.67400 -3.78600  20.93400  1.000 90.22000  ? 500 THR B CA  1 
ATOM   1665 C C   . THR B 2 168 ? 52.32500 -3.22500  21.13000  1.000 91.50000  ? 500 THR B C   1 
ATOM   1666 O O   . THR B 2 168 ? 51.90400 -2.41000  20.29600  1.000 92.27000  ? 500 THR B O   1 
ATOM   1667 C CB  . THR B 2 168 ? 53.88000 -4.10800  19.46000  1.000 90.98000  ? 500 THR B CB  1 
ATOM   1668 O OG1 . THR B 2 168 ? 52.96400 -5.14000  19.08900  1.000 88.09000  ? 500 THR B OG1 1 
ATOM   1669 C CG2 . THR B 2 168 ? 55.27600 -4.61500  19.25900  1.000 93.38000  ? 500 THR B CG2 1 
ATOM   1670 N N   . TYR B 2 169 ? 51.58500 -3.64000  22.15000  1.000 90.69000  ? 501 TYR B N   1 
ATOM   1671 C CA  . TYR B 2 169 ? 50.32700 -2.98000  22.42100  1.000 87.42000  ? 501 TYR B CA  1 
ATOM   1672 C C   . TYR B 2 169 ? 50.60100 -1.68900  23.16000  1.000 80.11000  ? 501 TYR B C   1 
ATOM   1673 O O   . TYR B 2 169 ? 51.68700 -1.48200  23.69300  1.000 84.12000  ? 501 TYR B O   1 
ATOM   1674 C CB  . TYR B 2 169 ? 49.39400 -3.86900  23.24400  1.000 91.10000  ? 501 TYR B CB  1 
ATOM   1675 C CG  . TYR B 2 169 ? 48.61900 -4.87800  22.41700  1.000 87.37000  ? 501 TYR B CG  1 
ATOM   1676 C CD1 . TYR B 2 169 ? 48.88800 -5.04600  21.07200  1.000 87.19000  ? 501 TYR B CD1 1 
ATOM   1677 C CD2 . TYR B 2 169 ? 47.59900 -5.64000  22.98600  1.000 88.65000  ? 501 TYR B CD2 1 
ATOM   1678 C CE1 . TYR B 2 169 ? 48.17400 -5.95200  20.31500  1.000 92.27000  ? 501 TYR B CE1 1 
ATOM   1679 C CE2 . TYR B 2 169 ? 46.88400 -6.55500  22.24400  1.000 82.94000  ? 501 TYR B CE2 1 
ATOM   1680 C CZ  . TYR B 2 169 ? 47.17900 -6.71000  20.90900  1.000 92.45000  ? 501 TYR B CZ  1 
ATOM   1681 O OH  . TYR B 2 169 ? 46.48100 -7.62000  20.14900  1.000 97.33000  ? 501 TYR B OH  1 
ATOM   1682 N N   . GLY B 2 170 ? 49.62000 -0.79700  23.13700  1.000 80.64000  ? 502 GLY B N   1 
ATOM   1683 C CA  . GLY B 2 170 ? 49.65400 0.34800   24.01400  1.000 79.47000  ? 502 GLY B CA  1 
ATOM   1684 C C   . GLY B 2 170 ? 49.47600 -0.08300  25.45100  1.000 82.16000  ? 502 GLY B C   1 
ATOM   1685 O O   . GLY B 2 170 ? 49.07700 -1.20700  25.73500  1.000 87.53000  ? 502 GLY B O   1 
ATOM   1686 N N   . VAL B 2 171 ? 49.78900 0.81900   26.38300  1.000 80.65000  ? 503 VAL B N   1 
ATOM   1687 C CA  . VAL B 2 171 ? 49.83100 0.40400   27.78100  1.000 81.78000  ? 503 VAL B CA  1 
ATOM   1688 C C   . VAL B 2 171 ? 48.46300 -0.02000  28.28200  1.000 88.74000  ? 503 VAL B C   1 
ATOM   1689 O O   . VAL B 2 171 ? 48.37000 -0.81100  29.22900  1.000 88.46000  ? 503 VAL B O   1 
ATOM   1690 C CB  . VAL B 2 171 ? 50.41300 1.52100   28.66500  1.000 87.59000  ? 503 VAL B CB  1 
ATOM   1691 C CG1 . VAL B 2 171 ? 51.76500 1.97100   28.11900  1.000 94.87000  ? 503 VAL B CG1 1 
ATOM   1692 C CG2 . VAL B 2 171 ? 49.43700 2.68600   28.78300  1.000 85.49000  ? 503 VAL B CG2 1 
ATOM   1693 N N   . GLY B 2 172 ? 47.39000 0.47600   27.65700  1.000 89.91000  ? 504 GLY B N   1 
ATOM   1694 C CA  . GLY B 2 172 ? 46.05000 0.11000   28.07100  1.000 84.24000  ? 504 GLY B CA  1 
ATOM   1695 C C   . GLY B 2 172 ? 45.63300 -1.27100  27.64200  1.000 82.39000  ? 504 GLY B C   1 
ATOM   1696 O O   . GLY B 2 172 ? 44.77100 -1.87400  28.29200  1.000 87.38000  ? 504 GLY B O   1 
ATOM   1697 N N   . TYR B 2 173 ? 46.25600 -1.79200  26.58900  1.000 83.91000  ? 505 TYR B N   1 
ATOM   1698 C CA  . TYR B 2 173 ? 45.94200 -3.08200  25.98600  1.000 87.08000  ? 505 TYR B CA  1 
ATOM   1699 C C   . TYR B 2 173 ? 46.91300 -4.17200  26.40200  1.000 88.98000  ? 505 TYR B C   1 
ATOM   1700 O O   . TYR B 2 173 ? 46.82400 -5.29500  25.89200  1.000 90.13000  ? 505 TYR B O   1 
ATOM   1701 C CB  . TYR B 2 173 ? 45.94700 -2.96000  24.45000  1.000 80.23000  ? 505 TYR B CB  1 
ATOM   1702 C CG  . TYR B 2 173 ? 44.81600 -2.11400  23.96700  1.000 76.63000  ? 505 TYR B CG  1 
ATOM   1703 C CD1 . TYR B 2 173 ? 44.92800 -0.73000  23.92900  1.000 76.61000  ? 505 TYR B CD1 1 
ATOM   1704 C CD2 . TYR B 2 173 ? 43.60500 -2.69000  23.60500  1.000 78.91000  ? 505 TYR B CD2 1 
ATOM   1705 C CE1 . TYR B 2 173 ? 43.87000 0.05800   23.51600  1.000 77.77000  ? 505 TYR B CE1 1 
ATOM   1706 C CE2 . TYR B 2 173 ? 42.53400 -1.91300  23.19400  1.000 77.36000  ? 505 TYR B CE2 1 
ATOM   1707 C CZ  . TYR B 2 173 ? 42.67300 -0.53900  23.14900  1.000 80.19000  ? 505 TYR B CZ  1 
ATOM   1708 O OH  . TYR B 2 173 ? 41.61300 0.23900   22.73000  1.000 83.41000  ? 505 TYR B OH  1 
ATOM   1709 N N   . GLN B 2 174 ? 47.82800 -3.86300  27.25400  1.000 85.30000  ? 506 GLN B N   1 
ATOM   1710 C CA  . GLN B 2 174 ? 48.85400 -4.76600  27.73500  1.000 86.92000  ? 506 GLN B CA  1 
ATOM   1711 C C   . GLN B 2 174 ? 48.34200 -5.49400  28.97200  1.000 82.85000  ? 506 GLN B C   1 
ATOM   1712 O O   . GLN B 2 174 ? 47.52800 -4.94600  29.71400  1.000 82.62000  ? 506 GLN B O   1 
ATOM   1713 C CB  . GLN B 2 174 ? 50.12300 -3.98700  28.07100  1.000 86.86000  ? 506 GLN B CB  1 
ATOM   1714 C CG  . GLN B 2 174 ? 51.00000 -3.64500  26.89200  1.000 83.14000  ? 506 GLN B CG  1 
ATOM   1715 C CD  . GLN B 2 174 ? 52.05700 -2.61400  27.23900  1.000 83.63000  ? 506 GLN B CD  1 
ATOM   1716 O OE1 . GLN B 2 174 ? 52.65500 -2.66200  28.31400  1.000 80.32000  ? 506 GLN B OE1 1 
ATOM   1717 N NE2 . GLN B 2 174 ? 52.30100 -1.68100  26.32400  1.000 85.76000  ? 506 GLN B NE2 1 
ATOM   1718 N N   . PRO B 2 175 ? 48.79900 -6.71900  29.23200  1.000 79.63000  ? 507 PRO B N   1 
ATOM   1719 C CA  . PRO B 2 175 ? 48.15300 -7.52700  30.26500  1.000 80.36000  ? 507 PRO B CA  1 
ATOM   1720 C C   . PRO B 2 175 ? 48.58700 -7.09000  31.64700  1.000 81.18000  ? 507 PRO B C   1 
ATOM   1721 O O   . PRO B 2 175 ? 49.75400 -6.77200  31.88900  1.000 84.75000  ? 507 PRO B O   1 
ATOM   1722 C CB  . PRO B 2 175 ? 48.64800 -8.94000  29.95200  1.000 77.76000  ? 507 PRO B CB  1 
ATOM   1723 C CG  . PRO B 2 175 ? 50.04600 -8.69500  29.49900  1.000 80.34000  ? 507 PRO B CG  1 
ATOM   1724 C CD  . PRO B 2 175 ? 50.04200 -7.35900  28.77400  1.000 82.17000  ? 507 PRO B CD  1 
ATOM   1725 N N   . TYR B 2 176 ? 47.63100 -7.06600  32.56000  1.000 81.87000  ? 508 TYR B N   1 
ATOM   1726 C CA  . TYR B 2 176 ? 47.92100 -6.83300  33.96100  1.000 80.24000  ? 508 TYR B CA  1 
ATOM   1727 C C   . TYR B 2 176 ? 47.55200 -8.07600  34.74400  1.000 77.19000  ? 508 TYR B C   1 
ATOM   1728 O O   . TYR B 2 176 ? 46.58300 -8.76300  34.41000  1.000 80.78000  ? 508 TYR B O   1 
ATOM   1729 C CB  . TYR B 2 176 ? 47.16600 -5.61300  34.47800  1.000 78.05000  ? 508 TYR B CB  1 
ATOM   1730 C CG  . TYR B 2 176 ? 47.91600 -4.34800  34.17100  1.000 85.22000  ? 508 TYR B CG  1 
ATOM   1731 C CD1 . TYR B 2 176 ? 48.03700 -3.89000  32.86700  1.000 81.52000  ? 508 TYR B CD1 1 
ATOM   1732 C CD2 . TYR B 2 176 ? 48.54100 -3.62800  35.18400  1.000 85.50000  ? 508 TYR B CD2 1 
ATOM   1733 C CE1 . TYR B 2 176 ? 48.74000 -2.73600  32.58000  1.000 82.93000  ? 508 TYR B CE1 1 
ATOM   1734 C CE2 . TYR B 2 176 ? 49.24800 -2.47600  34.90800  1.000 85.83000  ? 508 TYR B CE2 1 
ATOM   1735 C CZ  . TYR B 2 176 ? 49.34800 -2.03200  33.60300  1.000 86.61000  ? 508 TYR B CZ  1 
ATOM   1736 O OH  . TYR B 2 176 ? 50.05800 -0.87500  33.34900  1.000 88.25000  ? 508 TYR B OH  1 
ATOM   1737 N N   . ARG B 2 177 ? 48.35200 -8.38000  35.75800  1.000 81.84000  ? 509 ARG B N   1 
ATOM   1738 C CA  . ARG B 2 177 ? 48.06700 -9.45900  36.69300  1.000 79.49000  ? 509 ARG B CA  1 
ATOM   1739 C C   . ARG B 2 177 ? 47.43300 -8.82600  37.92300  1.000 80.82000  ? 509 ARG B C   1 
ATOM   1740 O O   . ARG B 2 177 ? 48.00600 -7.89800  38.50300  1.000 84.73000  ? 509 ARG B O   1 
ATOM   1741 C CB  . ARG B 2 177 ? 49.34500 -10.23400 37.03400  1.000 74.98000  ? 509 ARG B CB  1 
ATOM   1742 C CG  . ARG B 2 177 ? 49.93300 -11.01700 35.84300  1.000 76.05000  ? 509 ARG B CG  1 
ATOM   1743 C CD  . ARG B 2 177 ? 51.20200 -11.79700 36.19000  1.000 76.27000  ? 509 ARG B CD  1 
ATOM   1744 N NE  . ARG B 2 177 ? 51.55700 -12.75100 35.14400  1.000 82.14000  ? 509 ARG B NE  1 
ATOM   1745 C CZ  . ARG B 2 177 ? 52.25300 -13.87600 35.32200  1.000 84.45000  ? 509 ARG B CZ  1 
ATOM   1746 N NH1 . ARG B 2 177 ? 52.68600 -14.23300 36.52800  1.000 79.52000  ? 509 ARG B NH1 1 
ATOM   1747 N NH2 . ARG B 2 177 ? 52.50900 -14.66200 34.28500  1.000 77.90000  ? 509 ARG B NH2 1 
ATOM   1748 N N   . VAL B 2 178 ? 46.22900 -9.27600  38.28300  1.000 74.30000  ? 510 VAL B N   1 
ATOM   1749 C CA  . VAL B 2 178 ? 45.51000 -8.72300  39.42600  1.000 78.12000  ? 510 VAL B CA  1 
ATOM   1750 C C   . VAL B 2 178 ? 45.54900 -9.70600  40.58300  1.000 76.53000  ? 510 VAL B C   1 
ATOM   1751 O O   . VAL B 2 178 ? 45.48000 -10.92300 40.38800  1.000 78.71000  ? 510 VAL B O   1 
ATOM   1752 C CB  . VAL B 2 178 ? 44.05200 -8.38700  39.07000  1.000 78.28000  ? 510 VAL B CB  1 
ATOM   1753 C CG1 . VAL B 2 178 ? 43.37600 -7.68200  40.26800  1.000 75.59000  ? 510 VAL B CG1 1 
ATOM   1754 C CG2 . VAL B 2 178 ? 43.98400 -7.55800  37.81700  1.000 74.14000  ? 510 VAL B CG2 1 
ATOM   1755 N N   . VAL B 2 179 ? 45.65300 -9.18300  41.79400  1.000 79.09000  ? 511 VAL B N   1 
ATOM   1756 C CA  . VAL B 2 179 ? 45.45200 -9.97100  42.99900  1.000 69.77000  ? 511 VAL B CA  1 
ATOM   1757 C C   . VAL B 2 179 ? 44.52700 -9.17400  43.88100  1.000 72.25000  ? 511 VAL B C   1 
ATOM   1758 O O   . VAL B 2 179 ? 44.86100 -8.05700  44.28100  1.000 77.61000  ? 511 VAL B O   1 
ATOM   1759 C CB  . VAL B 2 179 ? 46.75900 -10.27300 43.73600  1.000 72.47000  ? 511 VAL B CB  1 
ATOM   1760 C CG1 . VAL B 2 179 ? 46.46000 -11.08000 44.99600  1.000 71.60000  ? 511 VAL B CG1 1 
ATOM   1761 C CG2 . VAL B 2 179 ? 47.70700 -11.02500 42.82100  1.000 75.72000  ? 511 VAL B CG2 1 
ATOM   1762 N N   . VAL B 2 180 ? 43.38100 -9.79300  44.17300  1.000 70.07000  ? 512 VAL B N   1 
ATOM   1763 C CA  . VAL B 2 180 ? 42.35500 -9.17700  45.05000  1.000 74.09000  ? 512 VAL B CA  1 
ATOM   1764 C C   . VAL B 2 180 ? 42.32300 -9.98700  46.33700  1.000 72.07000  ? 512 VAL B C   1 
ATOM   1765 O O   . VAL B 2 180 ? 41.96000 -11.16800 46.27400  1.000 71.30000  ? 512 VAL B O   1 
ATOM   1766 C CB  . VAL B 2 180 ? 40.97500 -9.21300  44.37900  1.000 73.82000  ? 512 VAL B CB  1 
ATOM   1767 C CG1 . VAL B 2 180 ? 39.93500 -8.45100  45.18200  1.000 78.25000  ? 512 VAL B CG1 1 
ATOM   1768 C CG2 . VAL B 2 180 ? 41.02800 -8.71500  42.94500  1.000 78.93000  ? 512 VAL B CG2 1 
ATOM   1769 N N   . LEU B 2 181 ? 42.69100 -9.37200  47.45000  1.000 73.29000  ? 513 LEU B N   1 
ATOM   1770 C CA  . LEU B 2 181 ? 42.72200 -10.03500 48.74600  1.000 68.23000  ? 513 LEU B CA  1 
ATOM   1771 C C   . LEU B 2 181 ? 41.44500 -9.70000  49.48900  1.000 68.17000  ? 513 LEU B C   1 
ATOM   1772 O O   . LEU B 2 181 ? 41.04900 -8.53300  49.54100  1.000 71.19000  ? 513 LEU B O   1 
ATOM   1773 C CB  . LEU B 2 181 ? 43.93500 -9.57300  49.54600  1.000 69.67000  ? 513 LEU B CB  1 
ATOM   1774 C CG  . LEU B 2 181 ? 45.26100 -9.79300  48.81200  1.000 78.62000  ? 513 LEU B CG  1 
ATOM   1775 C CD1 . LEU B 2 181 ? 46.42100 -9.19900  49.56200  1.000 81.07000  ? 513 LEU B CD1 1 
ATOM   1776 C CD2 . LEU B 2 181 ? 45.50300 -11.27200 48.56100  1.000 76.16000  ? 513 LEU B CD2 1 
ATOM   1777 N N   . SER B 2 182 ? 40.77800 -10.70700 50.02900  1.000 65.72000  ? 514 SER B N   1 
ATOM   1778 C CA  . SER B 2 182 ? 39.56500 -10.46300 50.78700  1.000 73.53000  ? 514 SER B CA  1 
ATOM   1779 C C   . SER B 2 182 ? 39.85600 -10.69600 52.26400  1.000 75.10000  ? 514 SER B C   1 
ATOM   1780 O O   . SER B 2 182 ? 40.38600 -11.74600 52.64500  1.000 76.40000  ? 514 SER B O   1 
ATOM   1781 C CB  . SER B 2 182 ? 38.42900 -11.33700 50.28200  1.000 69.64000  ? 514 SER B CB  1 
ATOM   1782 O OG  . SER B 2 182 ? 38.03000 -10.87400 49.01200  1.000 76.18000  ? 514 SER B OG  1 
ATOM   1783 N N   . PHE B 2 183 ? 39.53000 -9.70700  53.07500  1.000 71.40000  ? 515 PHE B N   1 
ATOM   1784 C CA  . PHE B 2 183 ? 39.76400 -9.77300  54.50800  1.000 75.09000  ? 515 PHE B CA  1 
ATOM   1785 C C   . PHE B 2 183 ? 38.44300 -10.11400 55.16000  1.000 76.56000  ? 515 PHE B C   1 
ATOM   1786 O O   . PHE B 2 183 ? 37.58600 -9.24800  55.35000  1.000 79.08000  ? 515 PHE B O   1 
ATOM   1787 C CB  . PHE B 2 183 ? 40.35700 -8.46700  55.00200  1.000 74.03000  ? 515 PHE B CB  1 
ATOM   1788 C CG  . PHE B 2 183 ? 41.67100 -8.18700  54.39300  1.000 74.90000  ? 515 PHE B CG  1 
ATOM   1789 C CD1 . PHE B 2 183 ? 42.51900 -9.23800  54.10900  1.000 75.95000  ? 515 PHE B CD1 1 
ATOM   1790 C CD2 . PHE B 2 183 ? 42.05100 -6.91100  54.05300  1.000 78.48000  ? 515 PHE B CD2 1 
ATOM   1791 C CE1 . PHE B 2 183 ? 43.73700 -9.02700  53.52100  1.000 76.80000  ? 515 PHE B CE1 1 
ATOM   1792 C CE2 . PHE B 2 183 ? 43.28300 -6.69200  53.45800  1.000 83.35000  ? 515 PHE B CE2 1 
ATOM   1793 C CZ  . PHE B 2 183 ? 44.12100 -7.75600  53.18800  1.000 77.72000  ? 515 PHE B CZ  1 
ATOM   1794 N N   . GLU B 2 184 ? 38.26200 -11.39100 55.46000  1.000 76.51000  ? 516 GLU B N   1 
ATOM   1795 C CA  . GLU B 2 184 ? 37.00100 -11.86300 56.00600  1.000 76.49000  ? 516 GLU B CA  1 
ATOM   1796 C C   . GLU B 2 184 ? 37.02800 -11.66200 57.51500  1.000 82.03000  ? 516 GLU B C   1 
ATOM   1797 O O   . GLU B 2 184 ? 37.76900 -12.34300 58.23100  1.000 81.71000  ? 516 GLU B O   1 
ATOM   1798 C CB  . GLU B 2 184 ? 36.78800 -13.32800 55.64000  1.000 82.05000  ? 516 GLU B CB  1 
ATOM   1799 C CG  . GLU B 2 184 ? 35.34700 -13.75700 55.66800  1.000 86.01000  ? 516 GLU B CG  1 
ATOM   1800 C CD  . GLU B 2 184 ? 34.84800 -14.11000 54.28100  1.000 86.46000  ? 516 GLU B CD  1 
ATOM   1801 O OE1 . GLU B 2 184 ? 35.60300 -14.79600 53.56500  1.000 86.68000  ? 516 GLU B OE1 1 
ATOM   1802 O OE2 . GLU B 2 184 ? 33.72600 -13.68900 53.91000  1.000 81.64000  ? 516 GLU B OE2 1 
ATOM   1803 N N   . LEU B 2 185 ? 36.25600 -10.70300 57.99700  1.000 77.46000  ? 517 LEU B N   1 
ATOM   1804 C CA  . LEU B 2 185 ? 36.10700 -10.48300 59.42000  1.000 75.18000  ? 517 LEU B CA  1 
ATOM   1805 C C   . LEU B 2 185 ? 34.67900 -10.88400 59.74300  1.000 80.86000  ? 517 LEU B C   1 
ATOM   1806 O O   . LEU B 2 185 ? 33.73700 -10.09600 59.64400  1.000 85.13000  ? 517 LEU B O   1 
ATOM   1807 C CB  . LEU B 2 185 ? 36.39700 -9.05300  59.82600  1.000 80.48000  ? 517 LEU B CB  1 
ATOM   1808 C CG  . LEU B 2 185 ? 36.51700 -8.85800  61.34400  1.000 79.27000  ? 517 LEU B CG  1 
ATOM   1809 C CD1 . LEU B 2 185 ? 35.16200 -8.72300  62.04000  1.000 82.27000  ? 517 LEU B CD1 1 
ATOM   1810 C CD2 . LEU B 2 185 ? 37.33700 -9.99100  61.96000  1.000 73.90000  ? 517 LEU B CD2 1 
ATOM   1811 N N   . LEU B 2 186 ? 34.53700 -12.11300 60.14900  1.000 77.22000  ? 518 LEU B N   1 
ATOM   1812 C CA  . LEU B 2 186 ? 33.27400 -12.64700 60.63200  1.000 81.15000  ? 518 LEU B CA  1 
ATOM   1813 C C   . LEU B 2 186 ? 33.46400 -13.22800 62.03100  1.000 84.19000  ? 518 LEU B C   1 
ATOM   1814 O O   . LEU B 2 186 ? 34.56400 -13.22300 62.58800  1.000 85.65000  ? 518 LEU B O   1 
ATOM   1815 C CB  . LEU B 2 186 ? 32.71400 -13.67700 59.64400  1.000 85.23000  ? 518 LEU B CB  1 
ATOM   1816 C CG  . LEU B 2 186 ? 33.52000 -14.90900 59.22100  1.000 79.44000  ? 518 LEU B CG  1 
ATOM   1817 C CD1 . LEU B 2 186 ? 33.45300 -16.00000 60.27500  1.000 89.39000  ? 518 LEU B CD1 1 
ATOM   1818 C CD2 . LEU B 2 186 ? 33.02100 -15.44200 57.88500  1.000 77.76000  ? 518 LEU B CD2 1 
ATOM   1819 N N   . HIS B 2 187 ? 32.37100 -13.72900 62.60300  1.000 81.63000  ? 519 HIS B N   1 
ATOM   1820 C CA  . HIS B 2 187 ? 32.38700 -14.19900 63.98300  1.000 71.92000  ? 519 HIS B CA  1 
ATOM   1821 C C   . HIS B 2 187 ? 33.21400 -15.47700 64.10400  1.000 74.64000  ? 519 HIS B C   1 
ATOM   1822 O O   . HIS B 2 187 ? 32.66300 -16.57800 63.99800  1.000 80.40000  ? 519 HIS B O   1 
ATOM   1823 C CB  . HIS B 2 187 ? 30.95900 -14.44000 64.49100  1.000 71.09000  ? 519 HIS B CB  1 
ATOM   1824 C CG  . HIS B 2 187 ? 30.03800 -13.26700 64.32000  1.000 73.52000  ? 519 HIS B CG  1 
ATOM   1825 N ND1 . HIS B 2 187 ? 30.45500 -12.04700 63.83500  1.000 74.72000  ? 519 HIS B ND1 1 
ATOM   1826 C CD2 . HIS B 2 187 ? 28.71300 -13.13700 64.57200  1.000 79.69000  ? 519 HIS B CD2 1 
ATOM   1827 C CE1 . HIS B 2 187 ? 29.42800 -11.21600 63.79300  1.000 80.38000  ? 519 HIS B CE1 1 
ATOM   1828 N NE2 . HIS B 2 187 ? 28.36000 -11.85400 64.23600  1.000 80.16000  ? 519 HIS B NE2 1 
ATOM   1829 N N   . ALA B 2 188 ? 34.51600 -15.34200 64.32800  1.000 76.30000  ? 520 ALA B N   1 
ATOM   1830 C CA  . ALA B 2 188 ? 35.42600 -16.48900 64.40500  1.000 78.86000  ? 520 ALA B CA  1 
ATOM   1831 C C   . ALA B 2 188 ? 36.74800 -16.02200 65.03100  1.000 83.10000  ? 520 ALA B C   1 
ATOM   1832 O O   . ALA B 2 188 ? 37.04900 -14.82500 65.03400  1.000 88.10000  ? 520 ALA B O   1 
ATOM   1833 C CB  . ALA B 2 188 ? 35.66300 -17.10200 63.01700  1.000 83.78000  ? 520 ALA B CB  1 
ATOM   1834 N N   . PRO B 2 189 ? 37.57400 -16.98000 65.55300  1.000 83.32000  ? 521 PRO B N   1 
ATOM   1835 C CA  . PRO B 2 189 ? 38.77600 -16.60000 66.32000  1.000 87.75000  ? 521 PRO B CA  1 
ATOM   1836 C C   . PRO B 2 189 ? 39.65100 -15.56400 65.62600  1.000 93.30000  ? 521 PRO B C   1 
ATOM   1837 O O   . PRO B 2 189 ? 40.29500 -14.76100 66.30900  1.000 104.27000 ? 521 PRO B O   1 
ATOM   1838 C CB  . PRO B 2 189 ? 39.44200 -17.95400 66.59800  1.000 87.07000  ? 521 PRO B CB  1 
ATOM   1839 C CG  . PRO B 2 189 ? 38.32300 -18.91200 66.64900  1.000 81.77000  ? 521 PRO B CG  1 
ATOM   1840 C CD  . PRO B 2 189 ? 37.32100 -18.43300 65.63100  1.000 82.67000  ? 521 PRO B CD  1 
ATOM   1841 N N   . ALA B 2 190 ? 39.68500 -15.57600 64.29200  1.000 83.99000  ? 522 ALA B N   1 
ATOM   1842 C CA  . ALA B 2 190 ? 40.57100 -14.72500 63.50000  1.000 90.47000  ? 522 ALA B CA  1 
ATOM   1843 C C   . ALA B 2 190 ? 41.97100 -15.32600 63.46200  1.000 89.96000  ? 522 ALA B C   1 
ATOM   1844 O O   . ALA B 2 190 ? 42.75100 -15.17000 64.40600  1.000 84.59000  ? 522 ALA B O   1 
ATOM   1845 C CB  . ALA B 2 190 ? 40.68200 -13.27500 63.98500  1.000 80.41000  ? 522 ALA B CB  1 
ATOM   1846 N N   . THR B 2 191 ? 42.30300 -16.00400 62.36200  1.000 89.80000  ? 523 THR B N   1 
ATOM   1847 C CA  . THR B 2 191 ? 43.50800 -16.81400 62.27000  1.000 80.65000  ? 523 THR B CA  1 
ATOM   1848 C C   . THR B 2 191 ? 44.60300 -16.19200 61.41400  1.000 80.94000  ? 523 THR B C   1 
ATOM   1849 O O   . THR B 2 191 ? 45.72600 -16.70700 61.41200  1.000 86.44000  ? 523 THR B O   1 
ATOM   1850 C CB  . THR B 2 191 ? 43.16200 -18.20900 61.72200  1.000 89.77000  ? 523 THR B CB  1 
ATOM   1851 O OG1 . THR B 2 191 ? 44.25800 -19.10300 61.94400  1.000 94.78000  ? 523 THR B OG1 1 
ATOM   1852 C CG2 . THR B 2 191 ? 42.85800 -18.14200 60.23300  1.000 83.39000  ? 523 THR B CG2 1 
ATOM   1853 N N   . VAL B 2 192 ? 44.31900 -15.09500 60.71400  1.000 72.61000  ? 524 VAL B N   1 
ATOM   1854 C CA  . VAL B 2 192 ? 45.30400 -14.44700 59.85900  1.000 79.27000  ? 524 VAL B CA  1 
ATOM   1855 C C   . VAL B 2 192 ? 45.55900 -13.06600 60.42700  1.000 76.20000  ? 524 VAL B C   1 
ATOM   1856 O O   . VAL B 2 192 ? 44.62400 -12.27000 60.56500  1.000 77.65000  ? 524 VAL B O   1 
ATOM   1857 C CB  . VAL B 2 192 ? 44.84000 -14.37500 58.39000  1.000 81.92000  ? 524 VAL B CB  1 
ATOM   1858 C CG1 . VAL B 2 192 ? 45.82000 -13.56700 57.55200  1.000 80.15000  ? 524 VAL B CG1 1 
ATOM   1859 C CG2 . VAL B 2 192 ? 44.70400 -15.77000 57.80800  1.000 82.09000  ? 524 VAL B CG2 1 
ATOM   1860 N N   . CYS B 2 193 ? 46.82800 -12.78600 60.75100  1.000 84.01000  ? 525 CYS B N   1 
ATOM   1861 C CA  . CYS B 2 193 ? 47.26500 -11.58600 61.46000  1.000 87.73000  ? 525 CYS B CA  1 
ATOM   1862 C C   . CYS B 2 193 ? 48.49200 -10.98400 60.78300  1.000 88.88000  ? 525 CYS B C   1 
ATOM   1863 O O   . CYS B 2 193 ? 49.32600 -11.70700 60.23300  1.000 84.96000  ? 525 CYS B O   1 
ATOM   1864 C CB  . CYS B 2 193 ? 47.63700 -11.90300 62.92000  1.000 90.38000  ? 525 CYS B CB  1 
ATOM   1865 S SG  . CYS B 2 193 ? 46.30900 -12.39600 64.02800  1.000 93.62000  ? 525 CYS B SG  1 
ATOM   1866 N N   . GLY B 2 194 ? 48.52200 -9.65300  60.77300  1.000 93.46000  ? 526 GLY B N   1 
ATOM   1867 C CA  . GLY B 2 194 ? 49.64300 -8.91300  60.25600  1.000 98.52000  ? 526 GLY B CA  1 
ATOM   1868 C C   . GLY B 2 194 ? 50.83900 -9.03700  61.17300  1.000 100.18000 ? 526 GLY B C   1 
ATOM   1869 O O   . GLY B 2 194 ? 50.82300 -9.71500  62.19600  1.000 100.16000 ? 526 GLY B O   1 
ATOM   1870 N N   . SER B 2 195 ? 51.90900 -8.33800  60.80000  1.000 109.86000 ? 527 SER B N   1 
ATOM   1871 C CA  . SER B 2 195 ? 53.19000 -8.53500  61.47000  1.000 109.14000 ? 527 SER B CA  1 
ATOM   1872 C C   . SER B 2 195 ? 53.18400 -8.06700  62.92500  1.000 106.40000 ? 527 SER B C   1 
ATOM   1873 O O   . SER B 2 195 ? 54.16200 -8.32100  63.63200  1.000 114.77000 ? 527 SER B O   1 
ATOM   1874 C CB  . SER B 2 195 ? 54.30000 -7.81900  60.68800  1.000 110.12000 ? 527 SER B CB  1 
ATOM   1875 O OG  . SER B 2 195 ? 55.56900 -7.94200  61.32700  1.000 129.16000 ? 527 SER B OG  1 
ATOM   1876 N N   . ASN B 2 196 ? 52.09700 -7.42800  63.40100  1.000 107.45000 ? 528 ASN B N   1 
ATOM   1877 C CA  . ASN B 2 196 ? 52.02200 -6.78200  64.72600  1.000 109.50000 ? 528 ASN B CA  1 
ATOM   1878 C C   . ASN B 2 196 ? 50.76800 -7.25100  65.48600  1.000 105.22000 ? 528 ASN B C   1 
ATOM   1879 O O   . ASN B 2 196 ? 49.66300 -6.77100  65.22100  1.000 107.13000 ? 528 ASN B O   1 
ATOM   1880 C CB  . ASN B 2 196 ? 52.01700 -5.25700  64.55200  1.000 109.99000 ? 528 ASN B CB  1 
ATOM   1881 C CG  . ASN B 2 196 ? 53.02400 -4.53800  65.45100  1.000 112.56000 ? 528 ASN B CG  1 
ATOM   1882 O OD1 . ASN B 2 196 ? 53.34300 -4.98500  66.55800  1.000 113.31000 ? 528 ASN B OD1 1 
ATOM   1883 N ND2 . ASN B 2 196 ? 53.51800 -3.39700  64.96900  1.000 112.17000 ? 528 ASN B ND2 1 
ATOM   1884 N N   . SER B 2 197 ? 50.95300 -8.13600  66.47500  1.000 106.31000 ? 529 SER B N   1 
ATOM   1885 C CA  . SER B 2 197 ? 49.85300 -8.81500  67.20100  1.000 104.51000 ? 529 SER B CA  1 
ATOM   1886 C C   . SER B 2 197 ? 48.67000 -9.11500  66.28800  1.000 106.93000 ? 529 SER B C   1 
ATOM   1887 O O   . SER B 2 197 ? 48.85700 -9.50100  65.12700  1.000 100.82000 ? 529 SER B O   1 
ATOM   1888 C CB  . SER B 2 197 ? 49.35500 -8.00800  68.40200  1.000 98.52000  ? 529 SER B CB  1 
ATOM   1889 O OG  . SER B 2 197 ? 48.23200 -8.66000  68.99000  1.000 90.48000  ? 529 SER B OG  1 
ATOM   1890 N N   . ASP C 1 1   ? 12.71400 2.60300   16.38700  1.000 116.41000 ? 1   ASP C N   1 
ATOM   1891 C CA  . ASP C 1 1   ? 13.63000 1.48600   16.59600  1.000 113.77000 ? 1   ASP C CA  1 
ATOM   1892 C C   . ASP C 1 1   ? 14.85700 1.66000   15.71400  1.000 114.96000 ? 1   ASP C C   1 
ATOM   1893 O O   . ASP C 1 1   ? 15.99300 1.63000   16.19000  1.000 112.28000 ? 1   ASP C O   1 
ATOM   1894 C CB  . ASP C 1 1   ? 12.94300 0.15200   16.28700  1.000 110.69000 ? 1   ASP C CB  1 
ATOM   1895 C CG  . ASP C 1 1   ? 11.60000 0.00800   16.98200  1.000 116.46000 ? 1   ASP C CG  1 
ATOM   1896 O OD1 . ASP C 1 1   ? 11.53300 0.21900   18.21400  1.000 123.73000 ? 1   ASP C OD1 1 
ATOM   1897 O OD2 . ASP C 1 1   ? 10.60600 -0.30900  16.29500  1.000 117.14000 ? 1   ASP C OD2 1 
ATOM   1898 N N   . LYS C 1 2   ? 14.59800 1.86600   14.41800  1.000 114.80000 ? 2   LYS C N   1 
ATOM   1899 C CA  . LYS C 1 2   ? 15.67100 1.95300   13.43300  1.000 116.45000 ? 2   LYS C CA  1 
ATOM   1900 C C   . LYS C 1 2   ? 16.50800 3.21700   13.61400  1.000 115.30000 ? 2   LYS C C   1 
ATOM   1901 O O   . LYS C 1 2   ? 17.74300 3.15300   13.57600  1.000 112.65000 ? 2   LYS C O   1 
ATOM   1902 C CB  . LYS C 1 2   ? 15.08100 1.90000   12.02600  1.000 112.94000 ? 2   LYS C CB  1 
ATOM   1903 C CG  . LYS C 1 2   ? 16.07100 1.56700   10.94100  1.000 108.17000 ? 2   LYS C CG  1 
ATOM   1904 C CD  . LYS C 1 2   ? 15.42600 0.61300   9.96000   1.000 117.44000 ? 2   LYS C CD  1 
ATOM   1905 C CE  . LYS C 1 2   ? 15.03700 -0.68800  10.65400  1.000 119.59000 ? 2   LYS C CE  1 
ATOM   1906 N NZ  . LYS C 1 2   ? 13.75800 -1.28300  10.16800  1.000 115.46000 ? 2   LYS C NZ  1 
ATOM   1907 N N   . GLU C 1 3   ? 15.86000 4.37700   13.77800  1.000 114.36000 ? 3   GLU C N   1 
ATOM   1908 C CA  . GLU C 1 3   ? 16.60600 5.59800   14.06800  1.000 113.40000 ? 3   GLU C CA  1 
ATOM   1909 C C   . GLU C 1 3   ? 17.53900 5.38100   15.25000  1.000 108.56000 ? 3   GLU C C   1 
ATOM   1910 O O   . GLU C 1 3   ? 18.70400 5.79900   15.22200  1.000 102.84000 ? 3   GLU C O   1 
ATOM   1911 C CB  . GLU C 1 3   ? 15.64900 6.76700   14.34500  1.000 115.44000 ? 3   GLU C CB  1 
ATOM   1912 C CG  . GLU C 1 3   ? 14.86400 7.28500   13.12300  1.000 113.71000 ? 3   GLU C CG  1 
ATOM   1913 C CD  . GLU C 1 3   ? 14.11000 8.59600   13.38900  1.000 115.20000 ? 3   GLU C CD  1 
ATOM   1914 O OE1 . GLU C 1 3   ? 14.49300 9.34400   14.31200  1.000 119.27000 ? 3   GLU C OE1 1 
ATOM   1915 O OE2 . GLU C 1 3   ? 13.13100 8.88400   12.67100  1.000 111.10000 ? 3   GLU C OE2 1 
ATOM   1916 N N   . TRP C 1 4   ? 17.04600 4.69800   16.28800  1.000 109.21000 ? 4   TRP C N   1 
ATOM   1917 C CA  . TRP C 1 4   ? 17.88800 4.39400   17.43800  1.000 108.06000 ? 4   TRP C CA  1 
ATOM   1918 C C   . TRP C 1 4   ? 19.06300 3.50900   17.03300  1.000 105.02000 ? 4   TRP C C   1 
ATOM   1919 O O   . TRP C 1 4   ? 20.22000 3.85100   17.29100  1.000 100.13000 ? 4   TRP C O   1 
ATOM   1920 C CB  . TRP C 1 4   ? 17.05600 3.73400   18.53900  1.000 107.81000 ? 4   TRP C CB  1 
ATOM   1921 C CG  . TRP C 1 4   ? 17.84000 3.42000   19.77400  1.000 107.37000 ? 4   TRP C CG  1 
ATOM   1922 C CD1 . TRP C 1 4   ? 18.39600 2.22000   20.10400  1.000 106.40000 ? 4   TRP C CD1 1 
ATOM   1923 C CD2 . TRP C 1 4   ? 18.16000 4.32000   20.84400  1.000 107.63000 ? 4   TRP C CD2 1 
ATOM   1924 N NE1 . TRP C 1 4   ? 19.04300 2.31400   21.31300  1.000 107.92000 ? 4   TRP C NE1 1 
ATOM   1925 C CE2 . TRP C 1 4   ? 18.91400 3.59300   21.78900  1.000 111.22000 ? 4   TRP C CE2 1 
ATOM   1926 C CE3 . TRP C 1 4   ? 17.88300 5.66900   21.09600  1.000 110.38000 ? 4   TRP C CE3 1 
ATOM   1927 C CZ2 . TRP C 1 4   ? 19.39400 4.16900   22.97200  1.000 115.31000 ? 4   TRP C CZ2 1 
ATOM   1928 C CZ3 . TRP C 1 4   ? 18.36500 6.24400   22.27700  1.000 116.98000 ? 4   TRP C CZ3 1 
ATOM   1929 C CH2 . TRP C 1 4   ? 19.11100 5.49000   23.19800  1.000 116.65000 ? 4   TRP C CH2 1 
ATOM   1930 N N   . ILE C 1 5   ? 18.77800 2.38400   16.36600  1.000 108.33000 ? 5   ILE C N   1 
ATOM   1931 C CA  . ILE C 1 5   ? 19.83600 1.47400   15.90900  1.000 109.86000 ? 5   ILE C CA  1 
ATOM   1932 C C   . ILE C 1 5   ? 20.91500 2.23500   15.15100  1.000 106.51000 ? 5   ILE C C   1 
ATOM   1933 O O   . ILE C 1 5   ? 22.11600 1.99900   15.34500  1.000 107.80000 ? 5   ILE C O   1 
ATOM   1934 C CB  . ILE C 1 5   ? 19.26300 0.34300   15.02700  1.000 111.63000 ? 5   ILE C CB  1 
ATOM   1935 C CG1 . ILE C 1 5   ? 18.31200 -0.57000  15.79400  1.000 114.81000 ? 5   ILE C CG1 1 
ATOM   1936 C CG2 . ILE C 1 5   ? 20.38800 -0.50900  14.47800  1.000 106.59000 ? 5   ILE C CG2 1 
ATOM   1937 C CD1 . ILE C 1 5   ? 17.66300 -1.61000  14.90100  1.000 110.66000 ? 5   ILE C CD1 1 
ATOM   1938 N N   . LEU C 1 6   ? 20.50700 3.15000   14.26300  1.000 106.45000 ? 6   LEU C N   1 
ATOM   1939 C CA  . LEU C 1 6   ? 21.47800 3.81400   13.39800  1.000 105.93000 ? 6   LEU C CA  1 
ATOM   1940 C C   . LEU C 1 6   ? 22.45600 4.66500   14.19900  1.000 102.27000 ? 6   LEU C C   1 
ATOM   1941 O O   . LEU C 1 6   ? 23.66600 4.61000   13.95400  1.000 100.67000 ? 6   LEU C O   1 
ATOM   1942 C CB  . LEU C 1 6   ? 20.77000 4.67400   12.34600  1.000 107.61000 ? 6   LEU C CB  1 
ATOM   1943 C CG  . LEU C 1 6   ? 21.66300 5.39800   11.31700  1.000 104.53000 ? 6   LEU C CG  1 
ATOM   1944 C CD1 . LEU C 1 6   ? 22.08700 4.46300   10.19500  1.000 108.01000 ? 6   LEU C CD1 1 
ATOM   1945 C CD2 . LEU C 1 6   ? 20.99800 6.65200   10.75500  1.000 103.56000 ? 6   LEU C CD2 1 
ATOM   1946 N N   . GLN C 1 7   ? 21.95400 5.46300   15.15100  1.000 99.14000  ? 7   GLN C N   1 
ATOM   1947 C CA  . GLN C 1 7   ? 22.81900 6.39500   15.87400  1.000 99.19000  ? 7   GLN C CA  1 
ATOM   1948 C C   . GLN C 1 7   ? 24.01400 5.68700   16.49800  1.000 96.95000  ? 7   GLN C C   1 
ATOM   1949 O O   . GLN C 1 7   ? 25.13900 6.20800   16.49100  1.000 93.27000  ? 7   GLN C O   1 
ATOM   1950 C CB  . GLN C 1 7   ? 22.01900 7.12400   16.95300  1.000 97.03000  ? 7   GLN C CB  1 
ATOM   1951 C CG  . GLN C 1 7   ? 22.87700 7.99800   17.84200  1.000 99.33000  ? 7   GLN C CG  1 
ATOM   1952 C CD  . GLN C 1 7   ? 23.49700 9.15400   17.08800  1.000 97.45000  ? 7   GLN C CD  1 
ATOM   1953 O OE1 . GLN C 1 7   ? 22.82400 9.82900   16.31800  1.000 96.92000  ? 7   GLN C OE1 1 
ATOM   1954 N NE2 . GLN C 1 7   ? 24.78600 9.39000   17.30700  1.000 96.59000  ? 7   GLN C NE2 1 
ATOM   1955 N N   . LYS C 1 8   ? 23.79000 4.48000   17.00800  1.000 93.47000  ? 8   LYS C N   1 
ATOM   1956 C CA  . LYS C 1 8   ? 24.78200 3.81600   17.84000  1.000 96.05000  ? 8   LYS C CA  1 
ATOM   1957 C C   . LYS C 1 8   ? 26.03400 3.49500   17.03900  1.000 94.86000  ? 8   LYS C C   1 
ATOM   1958 O O   . LYS C 1 8   ? 27.15100 3.87000   17.42100  1.000 93.91000  ? 8   LYS C O   1 
ATOM   1959 C CB  . LYS C 1 8   ? 24.17300 2.54800   18.43500  1.000 98.94000  ? 8   LYS C CB  1 
ATOM   1960 C CG  . LYS C 1 8   ? 22.65900 2.61800   18.66100  1.000 99.53000  ? 8   LYS C CG  1 
ATOM   1961 C CD  . LYS C 1 8   ? 22.20900 3.87400   19.44900  1.000 107.44000 ? 8   LYS C CD  1 
ATOM   1962 C CE  . LYS C 1 8   ? 22.58400 3.83500   20.91200  1.000 108.74000 ? 8   LYS C CE  1 
ATOM   1963 N NZ  . LYS C 1 8   ? 22.37800 5.16100   21.56800  1.000 106.29000 ? 8   LYS C NZ  1 
ATOM   1964 N N   . ILE C 1 9   ? 25.85000 2.81200   15.90600  1.000 103.57000 ? 9   ILE C N   1 
ATOM   1965 C CA  . ILE C 1 9   ? 26.95600 2.46400   15.01900  1.000 94.46000  ? 9   ILE C CA  1 
ATOM   1966 C C   . ILE C 1 9   ? 27.78800 3.69400   14.68700  1.000 89.28000  ? 9   ILE C C   1 
ATOM   1967 O O   . ILE C 1 9   ? 29.02600 3.65600   14.71200  1.000 89.22000  ? 9   ILE C O   1 
ATOM   1968 C CB  . ILE C 1 9   ? 26.40700 1.78400   13.74900  1.000 94.56000  ? 9   ILE C CB  1 
ATOM   1969 C CG1 . ILE C 1 9   ? 25.47000 2.71100   12.97400  1.000 93.15000  ? 9   ILE C CG1 1 
ATOM   1970 C CG2 . ILE C 1 9   ? 25.62500 0.55000   14.10600  1.000 99.48000  ? 9   ILE C CG2 1 
ATOM   1971 C CD1 . ILE C 1 9   ? 24.82400 2.00400   11.77900  1.000 88.35000  ? 9   ILE C CD1 1 
ATOM   1972 N N   . TYR C 1 10  ? 27.11800 4.81600   14.39600  1.000 92.49000  ? 10  TYR C N   1 
ATOM   1973 C CA  . TYR C 1 10  ? 27.81400 6.06600   14.09100  1.000 94.31000  ? 10  TYR C CA  1 
ATOM   1974 C C   . TYR C 1 10  ? 28.74200 6.45100   15.22600  1.000 95.46000  ? 10  TYR C C   1 
ATOM   1975 O O   . TYR C 1 10  ? 29.93200 6.71200   15.01300  1.000 92.63000  ? 10  TYR C O   1 
ATOM   1976 C CB  . TYR C 1 10  ? 26.81200 7.19900   13.82500  1.000 101.03000 ? 10  TYR C CB  1 
ATOM   1977 C CG  . TYR C 1 10  ? 27.42900 8.59800   13.67300  1.000 102.09000 ? 10  TYR C CG  1 
ATOM   1978 C CD1 . TYR C 1 10  ? 27.93700 9.03100   12.44900  1.000 105.01000 ? 10  TYR C CD1 1 
ATOM   1979 C CD2 . TYR C 1 10  ? 27.48400 9.48700   14.74500  1.000 101.11000 ? 10  TYR C CD2 1 
ATOM   1980 C CE1 . TYR C 1 10  ? 28.49400 10.31000  12.30100  1.000 104.93000 ? 10  TYR C CE1 1 
ATOM   1981 C CE2 . TYR C 1 10  ? 28.04000 10.76000  14.60700  1.000 103.16000 ? 10  TYR C CE2 1 
ATOM   1982 C CZ  . TYR C 1 10  ? 28.54100 11.16700  13.38600  1.000 108.79000 ? 10  TYR C CZ  1 
ATOM   1983 O OH  . TYR C 1 10  ? 29.08700 12.43000  13.25200  1.000 111.88000 ? 10  TYR C OH  1 
ATOM   1984 N N   . GLU C 1 11  ? 28.19500 6.51100   16.44900  1.000 101.28000 ? 11  GLU C N   1 
ATOM   1985 C CA  . GLU C 1 11  ? 29.01200 6.78900   17.62800  1.000 102.14000 ? 11  GLU C CA  1 
ATOM   1986 C C   . GLU C 1 11  ? 30.08800 5.72700   17.80100  1.000 95.38000  ? 11  GLU C C   1 
ATOM   1987 O O   . GLU C 1 11  ? 31.18700 6.01300   18.29200  1.000 92.26000  ? 11  GLU C O   1 
ATOM   1988 C CB  . GLU C 1 11  ? 28.12300 6.88200   18.87200  1.000 102.91000 ? 11  GLU C CB  1 
ATOM   1989 C CG  . GLU C 1 11  ? 27.36400 8.20500   18.99100  1.000 105.31000 ? 11  GLU C CG  1 
ATOM   1990 C CD  . GLU C 1 11  ? 26.52000 8.30900   20.25600  1.000 102.42000 ? 11  GLU C CD  1 
ATOM   1991 O OE1 . GLU C 1 11  ? 25.96500 7.28200   20.71200  1.000 101.47000 ? 11  GLU C OE1 1 
ATOM   1992 O OE2 . GLU C 1 11  ? 26.40800 9.43400   20.78700  1.000 104.61000 ? 11  GLU C OE2 1 
ATOM   1993 N N   . ILE C 1 12  ? 29.79900 4.50000   17.36500  1.000 93.18000  ? 12  ILE C N   1 
ATOM   1994 C CA  . ILE C 1 12  ? 30.81700 3.45600   17.37400  1.000 97.39000  ? 12  ILE C CA  1 
ATOM   1995 C C   . ILE C 1 12  ? 31.92000 3.77400   16.36800  1.000 93.38000  ? 12  ILE C C   1 
ATOM   1996 O O   . ILE C 1 12  ? 33.11600 3.67800   16.68100  1.000 90.28000  ? 12  ILE C O   1 
ATOM   1997 C CB  . ILE C 1 12  ? 30.17400 2.08600   17.10700  1.000 94.29000  ? 12  ILE C CB  1 
ATOM   1998 C CG1 . ILE C 1 12  ? 29.50600 1.57900   18.38500  1.000 91.86000  ? 12  ILE C CG1 1 
ATOM   1999 C CG2 . ILE C 1 12  ? 31.21200 1.09900   16.61700  1.000 89.24000  ? 12  ILE C CG2 1 
ATOM   2000 C CD1 . ILE C 1 12  ? 29.15000 0.11600   18.35500  1.000 82.20000  ? 12  ILE C CD1 1 
ATOM   2001 N N   . MET C 1 13  ? 31.53000 4.16000   15.14400  1.000 92.32000  ? 13  MET C N   1 
ATOM   2002 C CA  . MET C 1 13  ? 32.50000 4.58700   14.14100  1.000 88.53000  ? 13  MET C CA  1 
ATOM   2003 C C   . MET C 1 13  ? 33.27200 5.81800   14.59900  1.000 89.01000  ? 13  MET C C   1 
ATOM   2004 O O   . MET C 1 13  ? 34.47800 5.93300   14.34600  1.000 91.04000  ? 13  MET C O   1 
ATOM   2005 C CB  . MET C 1 13  ? 31.79100 4.86300   12.81500  1.000 92.63000  ? 13  MET C CB  1 
ATOM   2006 C CG  . MET C 1 13  ? 32.59600 5.67700   11.81100  1.000 90.06000  ? 13  MET C CG  1 
ATOM   2007 S SD  . MET C 1 13  ? 31.75500 5.75700   10.21600  1.000 98.99000  ? 13  MET C SD  1 
ATOM   2008 C CE  . MET C 1 13  ? 30.21700 6.49700   10.72000  1.000 101.42000 ? 13  MET C CE  1 
ATOM   2009 N N   . ARG C 1 14  ? 32.59800 6.75200   15.27400  1.000 90.90000  ? 14  ARG C N   1 
ATOM   2010 C CA  . ARG C 1 14  ? 33.28800 7.96000   15.70800  1.000 95.03000  ? 14  ARG C CA  1 
ATOM   2011 C C   . ARG C 1 14  ? 34.18500 7.70300   16.91800  1.000 94.62000  ? 14  ARG C C   1 
ATOM   2012 O O   . ARG C 1 14  ? 35.19500 8.39600   17.09100  1.000 100.13000 ? 14  ARG C O   1 
ATOM   2013 C CB  . ARG C 1 14  ? 32.27600 9.07400   15.99600  1.000 99.44000  ? 14  ARG C CB  1 
ATOM   2014 C CG  . ARG C 1 14  ? 31.54700 9.63200   14.75500  1.000 101.24000 ? 14  ARG C CG  1 
ATOM   2015 C CD  . ARG C 1 14  ? 31.97900 11.06700  14.38800  1.000 103.75000 ? 14  ARG C CD  1 
ATOM   2016 N NE  . ARG C 1 14  ? 33.37100 11.13000  13.94000  1.000 104.60000 ? 14  ARG C NE  1 
ATOM   2017 C CZ  . ARG C 1 14  ? 34.04600 12.25400  13.70200  1.000 108.72000 ? 14  ARG C CZ  1 
ATOM   2018 N NH1 . ARG C 1 14  ? 33.46800 13.43900  13.86700  1.000 113.66000 ? 14  ARG C NH1 1 
ATOM   2019 N NH2 . ARG C 1 14  ? 35.30900 12.19200  13.30100  1.000 108.11000 ? 14  ARG C NH2 1 
ATOM   2020 N N   . ARG C 1 15  ? 33.86000 6.72200   17.76500  1.000 85.66000  ? 15  ARG C N   1 
ATOM   2021 C CA  . ARG C 1 15  ? 34.85800 6.27700   18.73100  1.000 92.68000  ? 15  ARG C CA  1 
ATOM   2022 C C   . ARG C 1 15  ? 36.11500 5.80900   18.00700  1.000 91.88000  ? 15  ARG C C   1 
ATOM   2023 O O   . ARG C 1 15  ? 37.21600 6.32500   18.24000  1.000 93.90000  ? 15  ARG C O   1 
ATOM   2024 C CB  . ARG C 1 15  ? 34.31300 5.15200   19.61600  1.000 94.79000  ? 15  ARG C CB  1 
ATOM   2025 C CG  . ARG C 1 15  ? 33.13400 5.49900   20.50400  1.000 94.80000  ? 15  ARG C CG  1 
ATOM   2026 C CD  . ARG C 1 15  ? 33.49400 6.37500   21.67400  1.000 92.96000  ? 15  ARG C CD  1 
ATOM   2027 N NE  . ARG C 1 15  ? 32.52000 6.19400   22.75000  1.000 103.73000 ? 15  ARG C NE  1 
ATOM   2028 C CZ  . ARG C 1 15  ? 32.42800 6.97000   23.82700  1.000 107.23000 ? 15  ARG C CZ  1 
ATOM   2029 N NH1 . ARG C 1 15  ? 33.25000 8.00700   23.97000  1.000 103.05000 ? 15  ARG C NH1 1 
ATOM   2030 N NH2 . ARG C 1 15  ? 31.50700 6.71500   24.75800  1.000 106.29000 ? 15  ARG C NH2 1 
ATOM   2031 N N   . LEU C 1 16  ? 35.95600 4.83000   17.10600  1.000 83.79000  ? 16  LEU C N   1 
ATOM   2032 C CA  . LEU C 1 16  ? 37.09200 4.27600   16.37500  1.000 89.12000  ? 16  LEU C CA  1 
ATOM   2033 C C   . LEU C 1 16  ? 37.85400 5.35900   15.62700  1.000 95.45000  ? 16  LEU C C   1 
ATOM   2034 O O   . LEU C 1 16  ? 39.09300 5.38000   15.65100  1.000 93.88000  ? 16  LEU C O   1 
ATOM   2035 C CB  . LEU C 1 16  ? 36.61900 3.20700   15.39200  1.000 89.63000  ? 16  LEU C CB  1 
ATOM   2036 C CG  . LEU C 1 16  ? 35.78900 2.05100   15.94000  1.000 84.63000  ? 16  LEU C CG  1 
ATOM   2037 C CD1 . LEU C 1 16  ? 35.35100 1.13100   14.81800  1.000 82.25000  ? 16  LEU C CD1 1 
ATOM   2038 C CD2 . LEU C 1 16  ? 36.60100 1.28700   16.97200  1.000 92.26000  ? 16  LEU C CD2 1 
ATOM   2039 N N   . ASP C 1 17  ? 37.12100 6.24000   14.92900  1.000 95.06000  ? 17  ASP C N   1 
ATOM   2040 C CA  . ASP C 1 17  ? 37.70200 7.42300   14.30100  1.000 95.79000  ? 17  ASP C CA  1 
ATOM   2041 C C   . ASP C 1 17  ? 38.66600 8.12300   15.24800  1.000 98.39000  ? 17  ASP C C   1 
ATOM   2042 O O   . ASP C 1 17  ? 39.86700 8.23700   14.97200  1.000 98.03000  ? 17  ASP C O   1 
ATOM   2043 C CB  . ASP C 1 17  ? 36.58600 8.38900   13.86300  1.000 99.61000  ? 17  ASP C CB  1 
ATOM   2044 C CG  . ASP C 1 17  ? 36.18600 8.23200   12.37400  1.000 105.74000 ? 17  ASP C CG  1 
ATOM   2045 O OD1 . ASP C 1 17  ? 35.59800 7.19400   11.99400  1.000 100.14000 ? 17  ASP C OD1 1 
ATOM   2046 O OD2 . ASP C 1 17  ? 36.44000 9.16800   11.58100  1.000 111.97000 ? 17  ASP C OD2 1 
ATOM   2047 N N   . GLU C 1 18  ? 38.15100 8.57000   16.39600  1.000 94.40000  ? 18  GLU C N   1 
ATOM   2048 C CA  . GLU C 1 18  ? 38.96800 9.33200   17.32800  1.000 99.89000  ? 18  GLU C CA  1 
ATOM   2049 C C   . GLU C 1 18  ? 40.20800 8.56300   17.75100  1.000 101.37000 ? 18  GLU C C   1 
ATOM   2050 O O   . GLU C 1 18  ? 41.29500 9.14200   17.86200  1.000 107.12000 ? 18  GLU C O   1 
ATOM   2051 C CB  . GLU C 1 18  ? 38.14900 9.71400   18.55200  1.000 106.22000 ? 18  GLU C CB  1 
ATOM   2052 C CG  . GLU C 1 18  ? 38.91400 10.57800  19.54100  1.000 110.08000 ? 18  GLU C CG  1 
ATOM   2053 C CD  . GLU C 1 18  ? 38.03700 11.02900  20.68400  1.000 118.72000 ? 18  GLU C CD  1 
ATOM   2054 O OE1 . GLU C 1 18  ? 36.89100 10.53400  20.77200  1.000 119.24000 ? 18  GLU C OE1 1 
ATOM   2055 O OE2 . GLU C 1 18  ? 38.48500 11.87800  21.48500  1.000 123.73000 ? 18  GLU C OE2 1 
ATOM   2056 N N   . GLU C 1 19  ? 40.07600 7.25700   17.97400  1.000 94.16000  ? 19  GLU C N   1 
ATOM   2057 C CA  . GLU C 1 19  ? 41.18200 6.50700   18.54900  1.000 97.02000  ? 19  GLU C CA  1 
ATOM   2058 C C   . GLU C 1 19  ? 42.25200 6.11600   17.53200  1.000 93.88000  ? 19  GLU C C   1 
ATOM   2059 O O   . GLU C 1 19  ? 43.35100 5.72500   17.93500  1.000 95.52000  ? 19  GLU C O   1 
ATOM   2060 C CB  . GLU C 1 19  ? 40.63100 5.27900   19.27700  1.000 101.80000 ? 19  GLU C CB  1 
ATOM   2061 C CG  . GLU C 1 19  ? 39.66300 5.63900   20.42400  1.000 92.54000  ? 19  GLU C CG  1 
ATOM   2062 C CD  . GLU C 1 19  ? 39.16700 4.41800   21.18000  1.000 92.22000  ? 19  GLU C CD  1 
ATOM   2063 O OE1 . GLU C 1 19  ? 39.90100 3.40000   21.20200  1.000 89.52000  ? 19  GLU C OE1 1 
ATOM   2064 O OE2 . GLU C 1 19  ? 38.04600 4.47300   21.74200  1.000 88.51000  ? 19  GLU C OE2 1 
ATOM   2065 N N   . GLY C 1 20  ? 41.99700 6.25800   16.23800  1.000 96.74000  ? 20  GLY C N   1 
ATOM   2066 C CA  . GLY C 1 20  ? 43.01200 5.99300   15.24200  1.000 94.86000  ? 20  GLY C CA  1 
ATOM   2067 C C   . GLY C 1 20  ? 42.92800 4.62500   14.61600  1.000 96.03000  ? 20  GLY C C   1 
ATOM   2068 O O   . GLY C 1 20  ? 43.92800 4.14500   14.05800  1.000 98.15000  ? 20  GLY C O   1 
ATOM   2069 N N   . HIS C 1 21  ? 41.77500 3.98200   14.71200  1.000 94.53000  ? 21  HIS C N   1 
ATOM   2070 C CA  . HIS C 1 21  ? 41.53500 2.68200   14.10400  1.000 95.91000  ? 21  HIS C CA  1 
ATOM   2071 C C   . HIS C 1 21  ? 40.85100 2.86700   12.75500  1.000 91.71000  ? 21  HIS C C   1 
ATOM   2072 O O   . HIS C 1 21  ? 39.76700 2.34500   12.48900  1.000 87.92000  ? 21  HIS C O   1 
ATOM   2073 C CB  . HIS C 1 21  ? 40.70300 1.81700   15.04900  1.000 94.64000  ? 21  HIS C CB  1 
ATOM   2074 C CG  . HIS C 1 21  ? 41.30800 1.66000   16.41000  1.000 97.93000  ? 21  HIS C CG  1 
ATOM   2075 N ND1 . HIS C 1 21  ? 42.54900 1.09400   16.61300  1.000 98.77000  ? 21  HIS C ND1 1 
ATOM   2076 C CD2 . HIS C 1 21  ? 40.84500 1.99900   17.63700  1.000 97.30000  ? 21  HIS C CD2 1 
ATOM   2077 C CE1 . HIS C 1 21  ? 42.82100 1.08500   17.90700  1.000 96.05000  ? 21  HIS C CE1 1 
ATOM   2078 N NE2 . HIS C 1 21  ? 41.80400 1.63000   18.55000  1.000 90.70000  ? 21  HIS C NE2 1 
ATOM   2079 N N   . GLY C 1 22  ? 41.52000 3.65800   11.91400  1.000 95.02000  ? 22  GLY C N   1 
ATOM   2080 C CA  . GLY C 1 22  ? 40.92100 4.08100   10.65600  1.000 84.88000  ? 22  GLY C CA  1 
ATOM   2081 C C   . GLY C 1 22  ? 40.29900 2.94100   9.88400   1.000 82.22000  ? 22  GLY C C   1 
ATOM   2082 O O   . GLY C 1 22  ? 39.11000 2.97400   9.56600   1.000 83.28000  ? 22  GLY C O   1 
ATOM   2083 N N   . GLU C 1 23  ? 41.08900 1.89400   9.60500   1.000 80.67000  ? 23  GLU C N   1 
ATOM   2084 C CA  . GLU C 1 23  ? 40.57800 0.73600   8.87200   1.000 81.28000  ? 23  GLU C CA  1 
ATOM   2085 C C   . GLU C 1 23  ? 39.28900 0.20800   9.47800   1.000 78.69000  ? 23  GLU C C   1 
ATOM   2086 O O   . GLU C 1 23  ? 38.34600 -0.14300  8.75400   1.000 70.74000  ? 23  GLU C O   1 
ATOM   2087 C CB  . GLU C 1 23  ? 41.61800 -0.38400  8.84500   1.000 84.34000  ? 23  GLU C CB  1 
ATOM   2088 C CG  . GLU C 1 23  ? 41.10800 -1.65400  8.14100   1.000 82.94000  ? 23  GLU C CG  1 
ATOM   2089 C CD  . GLU C 1 23  ? 42.11800 -2.78300  8.14300   1.000 83.56000  ? 23  GLU C CD  1 
ATOM   2090 O OE1 . GLU C 1 23  ? 43.09400 -2.70000  8.89300   1.000 92.21000  ? 23  GLU C OE1 1 
ATOM   2091 O OE2 . GLU C 1 23  ? 41.94600 -3.75700  7.39800   1.000 80.68000  ? 23  GLU C OE2 1 
ATOM   2092 N N   . ALA C 1 24  ? 39.24600 0.12500   10.81400  1.000 82.01000  ? 24  ALA C N   1 
ATOM   2093 C CA  . ALA C 1 24  ? 38.04600 -0.32500  11.50700  1.000 80.73000  ? 24  ALA C CA  1 
ATOM   2094 C C   . ALA C 1 24  ? 36.93200 0.70000   11.39600  1.000 79.69000  ? 24  ALA C C   1 
ATOM   2095 O O   . ALA C 1 24  ? 35.75800 0.32900   11.34700  1.000 77.73000  ? 24  ALA C O   1 
ATOM   2096 C CB  . ALA C 1 24  ? 38.35900 -0.60500  12.98000  1.000 88.92000  ? 24  ALA C CB  1 
ATOM   2097 N N   . SER C 1 25  ? 37.27800 1.98800   11.38600  1.000 82.88000  ? 25  SER C N   1 
ATOM   2098 C CA  . SER C 1 25  ? 36.28700 3.01600   11.09400  1.000 82.80000  ? 25  SER C CA  1 
ATOM   2099 C C   . SER C 1 25  ? 35.66600 2.77300   9.73600   1.000 80.69000  ? 25  SER C C   1 
ATOM   2100 O O   . SER C 1 25  ? 34.44100 2.68200   9.60300   1.000 77.29000  ? 25  SER C O   1 
ATOM   2101 C CB  . SER C 1 25  ? 36.93100 4.40100   11.14500  1.000 89.34000  ? 25  SER C CB  1 
ATOM   2102 O OG  . SER C 1 25  ? 36.01100 5.38500   10.71700  1.000 91.49000  ? 25  SER C OG  1 
ATOM   2103 N N   . LEU C 1 26  ? 36.51700 2.64500   8.71300   1.000 82.78000  ? 26  LEU C N   1 
ATOM   2104 C CA  . LEU C 1 26  ? 36.04500 2.39500   7.35900   1.000 75.45000  ? 26  LEU C CA  1 
ATOM   2105 C C   . LEU C 1 26  ? 35.16100 1.16000   7.31100   1.000 77.88000  ? 26  LEU C C   1 
ATOM   2106 O O   . LEU C 1 26  ? 34.14200 1.14100   6.59700   1.000 79.86000  ? 26  LEU C O   1 
ATOM   2107 C CB  . LEU C 1 26  ? 37.23700 2.25500   6.41900   1.000 77.58000  ? 26  LEU C CB  1 
ATOM   2108 C CG  . LEU C 1 26  ? 37.93500 3.48700   5.82500   1.000 80.43000  ? 26  LEU C CG  1 
ATOM   2109 C CD1 . LEU C 1 26  ? 38.57000 4.39700   6.85400   1.000 86.77000  ? 26  LEU C CD1 1 
ATOM   2110 C CD2 . LEU C 1 26  ? 38.99500 3.02400   4.83800   1.000 82.89000  ? 26  LEU C CD2 1 
ATOM   2111 N N   . ARG C 1 27  ? 35.50800 0.12500   8.08900   1.000 69.22000  ? 27  ARG C N   1 
ATOM   2112 C CA  . ARG C 1 27  ? 34.69700 -1.08600  8.05500   1.000 71.67000  ? 27  ARG C CA  1 
ATOM   2113 C C   . ARG C 1 27  ? 33.30100 -0.83600  8.58600   1.000 75.71000  ? 27  ARG C C   1 
ATOM   2114 O O   . ARG C 1 27  ? 32.34900 -1.49600  8.14800   1.000 70.78000  ? 27  ARG C O   1 
ATOM   2115 C CB  . ARG C 1 27  ? 35.36100 -2.21000  8.84400   1.000 71.91000  ? 27  ARG C CB  1 
ATOM   2116 C CG  . ARG C 1 27  ? 36.56900 -2.82600  8.16600   1.000 72.85000  ? 27  ARG C CG  1 
ATOM   2117 C CD  . ARG C 1 27  ? 36.94600 -4.12200  8.82700   1.000 74.84000  ? 27  ARG C CD  1 
ATOM   2118 N NE  . ARG C 1 27  ? 37.36000 -5.16900  7.89500   1.000 76.53000  ? 27  ARG C NE  1 
ATOM   2119 C CZ  . ARG C 1 27  ? 38.62500 -5.46200  7.62900   1.000 80.01000  ? 27  ARG C CZ  1 
ATOM   2120 N NH1 . ARG C 1 27  ? 39.60300 -4.77000  8.20500   1.000 78.50000  ? 27  ARG C NH1 1 
ATOM   2121 N NH2 . ARG C 1 27  ? 38.91300 -6.44400  6.79100   1.000 81.32000  ? 27  ARG C NH2 1 
ATOM   2122 N N   . VAL C 1 28  ? 33.15700 0.12800   9.49600   1.000 79.96000  ? 28  VAL C N   1 
ATOM   2123 C CA  . VAL C 1 28  ? 31.83300 0.49800   9.98300   1.000 81.35000  ? 28  VAL C CA  1 
ATOM   2124 C C   . VAL C 1 28  ? 31.13000 1.41800   8.98900   1.000 80.40000  ? 28  VAL C C   1 
ATOM   2125 O O   . VAL C 1 28  ? 29.93700 1.23700   8.70200   1.000 80.49000  ? 28  VAL C O   1 
ATOM   2126 C CB  . VAL C 1 28  ? 31.94200 1.12100   11.38800  1.000 89.71000  ? 28  VAL C CB  1 
ATOM   2127 C CG1 . VAL C 1 28  ? 30.57100 1.51300   11.91500  1.000 89.13000  ? 28  VAL C CG1 1 
ATOM   2128 C CG2 . VAL C 1 28  ? 32.64300 0.14800   12.36100  1.000 78.78000  ? 28  VAL C CG2 1 
ATOM   2129 N N   . SER C 1 29  ? 31.85600 2.39300   8.41900   1.000 84.34000  ? 29  SER C N   1 
ATOM   2130 C CA  . SER C 1 29  ? 31.30700 3.14400   7.29100   1.000 80.80000  ? 29  SER C CA  1 
ATOM   2131 C C   . SER C 1 29  ? 30.63700 2.19900   6.31400   1.000 75.89000  ? 29  SER C C   1 
ATOM   2132 O O   . SER C 1 29  ? 29.47600 2.39400   5.95000   1.000 83.20000  ? 29  SER C O   1 
ATOM   2133 C CB  . SER C 1 29  ? 32.38200 3.93800   6.54900   1.000 74.09000  ? 29  SER C CB  1 
ATOM   2134 O OG  . SER C 1 29  ? 33.23800 4.63900   7.42800   1.000 87.14000  ? 29  SER C OG  1 
ATOM   2135 N N   . ASP C 1 30  ? 31.34700 1.14100   5.91400   1.000 68.97000  ? 30  ASP C N   1 
ATOM   2136 C CA  . ASP C 1 30  ? 30.79600 0.22900   4.91700   1.000 77.71000  ? 30  ASP C CA  1 
ATOM   2137 C C   . ASP C 1 30  ? 29.43400 -0.30600  5.33600   1.000 81.24000  ? 30  ASP C C   1 
ATOM   2138 O O   . ASP C 1 30  ? 28.56200 -0.53400  4.48700   1.000 90.01000  ? 30  ASP C O   1 
ATOM   2139 C CB  . ASP C 1 30  ? 31.75300 -0.93300  4.66500   1.000 73.95000  ? 30  ASP C CB  1 
ATOM   2140 C CG  . ASP C 1 30  ? 33.01700 -0.51300  3.93100   1.000 80.86000  ? 30  ASP C CG  1 
ATOM   2141 O OD1 . ASP C 1 30  ? 33.42700 0.67300   3.98100   1.000 77.72000  ? 30  ASP C OD1 1 
ATOM   2142 O OD2 . ASP C 1 30  ? 33.60600 -1.40500  3.29000   1.000 87.04000  ? 30  ASP C OD2 1 
ATOM   2143 N N   . LEU C 1 31  ? 29.22200 -0.52400  6.63600   1.000 86.18000  ? 31  LEU C N   1 
ATOM   2144 C CA  . LEU C 1 31  ? 27.92600 -1.02800  7.06600   1.000 85.51000  ? 31  LEU C CA  1 
ATOM   2145 C C   . LEU C 1 31  ? 26.96800 0.07300   7.51300   1.000 90.12000  ? 31  LEU C C   1 
ATOM   2146 O O   . LEU C 1 31  ? 25.75300 -0.16000  7.50200   1.000 96.50000  ? 31  LEU C O   1 
ATOM   2147 C CB  . LEU C 1 31  ? 28.07800 -2.08000  8.17200   1.000 89.76000  ? 31  LEU C CB  1 
ATOM   2148 C CG  . LEU C 1 31  ? 27.57700 -1.72600  9.57700   1.000 90.26000  ? 31  LEU C CG  1 
ATOM   2149 C CD1 . LEU C 1 31  ? 26.94700 -2.91900  10.28200  1.000 83.48000  ? 31  LEU C CD1 1 
ATOM   2150 C CD2 . LEU C 1 31  ? 28.73000 -1.20000  10.39300  1.000 90.02000  ? 31  LEU C CD2 1 
ATOM   2151 N N   . ILE C 1 32  ? 27.45700 1.26200   7.89200   1.000 80.52000  ? 32  ILE C N   1 
ATOM   2152 C CA  . ILE C 1 32  ? 26.57900 2.43600   7.85800   1.000 80.35000  ? 32  ILE C CA  1 
ATOM   2153 C C   . ILE C 1 32  ? 25.84700 2.47400   6.52700   1.000 88.12000  ? 32  ILE C C   1 
ATOM   2154 O O   . ILE C 1 32  ? 24.61500 2.40100   6.46400   1.000 88.18000  ? 32  ILE C O   1 
ATOM   2155 C CB  . ILE C 1 32  ? 27.37400 3.73600   8.04700   1.000 82.47000  ? 32  ILE C CB  1 
ATOM   2156 C CG1 . ILE C 1 32  ? 28.03800 3.77400   9.40800   1.000 90.28000  ? 32  ILE C CG1 1 
ATOM   2157 C CG2 . ILE C 1 32  ? 26.44900 4.93000   7.84300   1.000 79.00000  ? 32  ILE C CG2 1 
ATOM   2158 C CD1 . ILE C 1 32  ? 27.25800 3.03000   10.45200  1.000 87.62000  ? 32  ILE C CD1 1 
ATOM   2159 N N   . TYR C 1 33  ? 26.62800 2.58200   5.44000   1.000 83.61000  ? 33  TYR C N   1 
ATOM   2160 C CA  . TYR C 1 33  ? 26.07800 2.65800   4.09900   1.000 85.27000  ? 33  TYR C CA  1 
ATOM   2161 C C   . TYR C 1 33  ? 25.20900 1.44800   3.79500   1.000 94.51000  ? 33  TYR C C   1 
ATOM   2162 O O   . TYR C 1 33  ? 24.12200 1.58400   3.21800   1.000 96.12000  ? 33  TYR C O   1 
ATOM   2163 C CB  . TYR C 1 33  ? 27.20700 2.77700   3.06500   1.000 87.24000  ? 33  TYR C CB  1 
ATOM   2164 C CG  . TYR C 1 33  ? 26.73400 2.47200   1.65600   1.000 83.13000  ? 33  TYR C CG  1 
ATOM   2165 C CD1 . TYR C 1 33  ? 26.17000 3.46200   0.86800   1.000 88.08000  ? 33  TYR C CD1 1 
ATOM   2166 C CD2 . TYR C 1 33  ? 26.83000 1.18700   1.12500   1.000 87.39000  ? 33  TYR C CD2 1 
ATOM   2167 C CE1 . TYR C 1 33  ? 25.72700 3.18400   -0.41400  1.000 87.98000  ? 33  TYR C CE1 1 
ATOM   2168 C CE2 . TYR C 1 33  ? 26.38200 0.90300   -0.15300  1.000 86.17000  ? 33  TYR C CE2 1 
ATOM   2169 C CZ  . TYR C 1 33  ? 25.82800 1.90800   -0.90500  1.000 87.37000  ? 33  TYR C CZ  1 
ATOM   2170 O OH  . TYR C 1 33  ? 25.37600 1.64100   -2.16300  1.000 90.90000  ? 33  TYR C OH  1 
ATOM   2171 N N   . GLU C 1 34  ? 25.68600 0.24600   4.15000   1.000 94.84000  ? 34  GLU C N   1 
ATOM   2172 C CA  . GLU C 1 34  ? 24.92800 -0.96500  3.83400   1.000 94.09000  ? 34  GLU C CA  1 
ATOM   2173 C C   . GLU C 1 34  ? 23.56800 -0.97700  4.52500   1.000 98.37000  ? 34  GLU C C   1 
ATOM   2174 O O   . GLU C 1 34  ? 22.56500 -1.39900  3.93400   1.000 99.64000  ? 34  GLU C O   1 
ATOM   2175 C CB  . GLU C 1 34  ? 25.71500 -2.21700  4.21800   1.000 84.55000  ? 34  GLU C CB  1 
ATOM   2176 C CG  . GLU C 1 34  ? 24.84900 -3.47300  4.16600   1.000 87.08000  ? 34  GLU C CG  1 
ATOM   2177 C CD  . GLU C 1 34  ? 25.63800 -4.73500  3.92200   1.000 93.28000  ? 34  GLU C CD  1 
ATOM   2178 O OE1 . GLU C 1 34  ? 26.81300 -4.79400  4.35000   1.000 94.73000  ? 34  GLU C OE1 1 
ATOM   2179 O OE2 . GLU C 1 34  ? 25.08100 -5.67000  3.30300   1.000 96.86000  ? 34  GLU C OE2 1 
ATOM   2180 N N   . PHE C 1 35  ? 23.51500 -0.50500  5.77200   1.000 91.58000  ? 35  PHE C N   1 
ATOM   2181 C CA  . PHE C 1 35  ? 22.29900 -0.60800  6.57100   1.000 99.53000  ? 35  PHE C CA  1 
ATOM   2182 C C   . PHE C 1 35  ? 21.23100 0.36100   6.08200   1.000 96.56000  ? 35  PHE C C   1 
ATOM   2183 O O   . PHE C 1 35  ? 20.05200 0.00100   5.98000   1.000 96.25000  ? 35  PHE C O   1 
ATOM   2184 C CB  . PHE C 1 35  ? 22.65300 -0.36400  8.03800   1.000 96.61000  ? 35  PHE C CB  1 
ATOM   2185 C CG  . PHE C 1 35  ? 21.48200 -0.26500  8.94400   1.000 94.60000  ? 35  PHE C CG  1 
ATOM   2186 C CD1 . PHE C 1 35  ? 20.70700 -1.37700  9.22800   1.000 99.66000  ? 35  PHE C CD1 1 
ATOM   2187 C CD2 . PHE C 1 35  ? 21.17600 0.94000   9.54800   1.000 101.06000 ? 35  PHE C CD2 1 
ATOM   2188 C CE1 . PHE C 1 35  ? 19.63000 -1.27900  10.08200  1.000 103.04000 ? 35  PHE C CE1 1 
ATOM   2189 C CE2 . PHE C 1 35  ? 20.10900 1.04500   10.40800  1.000 103.85000 ? 35  PHE C CE2 1 
ATOM   2190 C CZ  . PHE C 1 35  ? 19.33100 -0.06400  10.67300  1.000 106.18000 ? 35  PHE C CZ  1 
ATOM   2191 N N   . MET C 1 36  ? 21.63000 1.58300   5.75900   1.000 93.76000  ? 36  MET C N   1 
ATOM   2192 C CA  . MET C 1 36  ? 20.76000 2.59900   5.19500   1.000 93.51000  ? 36  MET C CA  1 
ATOM   2193 C C   . MET C 1 36  ? 20.28300 2.26000   3.77400   1.000 96.05000  ? 36  MET C C   1 
ATOM   2194 O O   . MET C 1 36  ? 19.72100 3.11800   3.10600   1.000 98.05000  ? 36  MET C O   1 
ATOM   2195 C CB  . MET C 1 36  ? 21.48300 3.94600   5.21200   1.000 87.77000  ? 36  MET C CB  1 
ATOM   2196 C CG  . MET C 1 36  ? 22.10000 4.27000   6.53000   1.000 87.34000  ? 36  MET C CG  1 
ATOM   2197 S SD  . MET C 1 36  ? 22.69100 5.95300   6.64000   1.000 97.10000  ? 36  MET C SD  1 
ATOM   2198 C CE  . MET C 1 36  ? 21.33300 6.83700   5.88100   1.000 96.46000  ? 36  MET C CE  1 
ATOM   2199 N N   . LYS C 1 37  ? 20.49900 1.05400   3.25800   1.000 98.22000  ? 37  LYS C N   1 
ATOM   2200 C CA  . LYS C 1 37  ? 19.86800 0.60800   2.02500   1.000 101.12000 ? 37  LYS C CA  1 
ATOM   2201 C C   . LYS C 1 37  ? 18.99500 -0.61800  2.24200   1.000 111.66000 ? 37  LYS C C   1 
ATOM   2202 O O   . LYS C 1 37  ? 18.29700 -1.03400  1.30900   1.000 116.77000 ? 37  LYS C O   1 
ATOM   2203 C CB  . LYS C 1 37  ? 20.91600 0.29700   0.94300   1.000 103.28000 ? 37  LYS C CB  1 
ATOM   2204 C CG  . LYS C 1 37  ? 21.90000 1.42600   0.62800   1.000 97.17000  ? 37  LYS C CG  1 
ATOM   2205 C CD  . LYS C 1 37  ? 21.24300 2.65400   0.01700   1.000 92.09000  ? 37  LYS C CD  1 
ATOM   2206 C CE  . LYS C 1 37  ? 22.30100 3.72400   -0.24800  1.000 91.13000  ? 37  LYS C CE  1 
ATOM   2207 N NZ  . LYS C 1 37  ? 21.85100 4.92500   -1.03000  1.000 91.94000  ? 37  LYS C NZ  1 
ATOM   2208 N N   . LYS C 1 38  ? 19.03200 -1.22100  3.43400   1.000 115.24000 ? 38  LYS C N   1 
ATOM   2209 C CA  . LYS C 1 38  ? 18.14500 -2.31900  3.79200   1.000 117.37000 ? 38  LYS C CA  1 
ATOM   2210 C C   . LYS C 1 38  ? 16.87500 -1.85200  4.49000   1.000 123.96000 ? 38  LYS C C   1 
ATOM   2211 O O   . LYS C 1 38  ? 15.84500 -2.52700  4.37800   1.000 128.66000 ? 38  LYS C O   1 
ATOM   2212 C CB  . LYS C 1 38  ? 18.87200 -3.33000  4.70100   1.000 113.46000 ? 38  LYS C CB  1 
ATOM   2213 C CG  . LYS C 1 38  ? 20.00800 -4.09800  4.03100   1.000 114.44000 ? 38  LYS C CG  1 
ATOM   2214 C CD  . LYS C 1 38  ? 20.46100 -5.28500  4.86800   1.000 109.02000 ? 38  LYS C CD  1 
ATOM   2215 C CE  . LYS C 1 38  ? 19.32200 -6.26900  5.10000   1.000 105.19000 ? 38  LYS C CE  1 
ATOM   2216 N NZ  . LYS C 1 38  ? 19.80200 -7.68100  5.14700   1.000 106.32000 ? 38  LYS C NZ  1 
ATOM   2217 N N   . ASP C 1 39  ? 16.92600 -0.71200  5.18500   1.000 124.93000 ? 39  ASP C N   1 
ATOM   2218 C CA  . ASP C 1 39  ? 15.83600 -0.21500  6.04200   1.000 130.14000 ? 39  ASP C CA  1 
ATOM   2219 C C   . ASP C 1 39  ? 15.53600 -1.17300  7.20900   1.000 133.52000 ? 39  ASP C C   1 
ATOM   2220 O O   . ASP C 1 39  ? 16.44600 -1.63800  7.90200   1.000 132.64000 ? 39  ASP C O   1 
ATOM   2221 C CB  . ASP C 1 39  ? 14.56400 0.04200   5.22200   1.000 127.07000 ? 39  ASP C CB  1 
ATOM   2222 C CG  . ASP C 1 39  ? 14.69000 1.24900   4.30900   1.000 131.74000 ? 39  ASP C CG  1 
ATOM   2223 O OD1 . ASP C 1 39  ? 15.62900 2.05000   4.50600   1.000 132.23000 ? 39  ASP C OD1 1 
ATOM   2224 O OD2 . ASP C 1 39  ? 13.85400 1.38800   3.38800   1.000 134.18000 ? 39  ASP C OD2 1 
ATOM   2225 O OXT . ASP C 1 39  ? 14.38600 -1.49500  7.52900   1.000 135.91000 ? 39  ASP C OXT 1 
ATOM   2226 N N   . ASN D 2 2   ? 54.44500 18.02500  -30.10800 1.000 97.74000  ? 334 ASN D N   1 
ATOM   2227 C CA  . ASN D 2 2   ? 53.52900 18.44000  -29.05800 1.000 100.14000 ? 334 ASN D CA  1 
ATOM   2228 C C   . ASN D 2 2   ? 52.66700 17.26200  -28.63800 1.000 101.71000 ? 334 ASN D C   1 
ATOM   2229 O O   . ASN D 2 2   ? 51.72100 16.89100  -29.33200 1.000 99.95000  ? 334 ASN D O   1 
ATOM   2230 C CB  . ASN D 2 2   ? 52.64200 19.60400  -29.50700 1.000 101.26000 ? 334 ASN D CB  1 
ATOM   2231 C CG  . ASN D 2 2   ? 52.06000 20.39000  -28.32200 1.000 106.30000 ? 334 ASN D CG  1 
ATOM   2232 O OD1 . ASN D 2 2   ? 51.80600 19.83200  -27.24800 1.000 106.28000 ? 334 ASN D OD1 1 
ATOM   2233 N ND2 . ASN D 2 2   ? 51.83200 21.68700  -28.52300 1.000 101.26000 ? 334 ASN D ND2 1 
ATOM   2234 N N   . LEU D 2 3   ? 53.00600 16.69600  -27.48600 1.000 102.15000 ? 335 LEU D N   1 
ATOM   2235 C CA  . LEU D 2 3   ? 52.35300 15.52500  -26.92600 1.000 101.15000 ? 335 LEU D CA  1 
ATOM   2236 C C   . LEU D 2 3   ? 51.34800 15.94800  -25.86300 1.000 98.29000  ? 335 LEU D C   1 
ATOM   2237 O O   . LEU D 2 3   ? 51.40300 17.05700  -25.32900 1.000 102.71000 ? 335 LEU D O   1 
ATOM   2238 C CB  . LEU D 2 3   ? 53.38900 14.57500  -26.31500 1.000 102.96000 ? 335 LEU D CB  1 
ATOM   2239 C CG  . LEU D 2 3   ? 54.65600 14.30700  -27.13800 1.000 100.47000 ? 335 LEU D CG  1 
ATOM   2240 C CD1 . LEU D 2 3   ? 55.80000 15.25000  -26.77000 1.000 95.49000  ? 335 LEU D CD1 1 
ATOM   2241 C CD2 . LEU D 2 3   ? 55.08300 12.87000  -26.97000 1.000 105.69000 ? 335 LEU D CD2 1 
ATOM   2242 N N   . CYS D 2 4   ? 50.42500 15.05000  -25.56400 1.000 97.10000  ? 336 CYS D N   1 
ATOM   2243 C CA  . CYS D 2 4   ? 49.40700 15.33400  -24.55800 1.000 93.26000  ? 336 CYS D CA  1 
ATOM   2244 C C   . CYS D 2 4   ? 50.00600 15.14200  -23.16900 1.000 97.95000  ? 336 CYS D C   1 
ATOM   2245 O O   . CYS D 2 4   ? 50.61600 14.10500  -22.91400 1.000 99.41000  ? 336 CYS D O   1 
ATOM   2246 C CB  . CYS D 2 4   ? 48.20600 14.41300  -24.74100 1.000 94.94000  ? 336 CYS D CB  1 
ATOM   2247 S SG  . CYS D 2 4   ? 47.34200 14.55400  -26.35700 1.000 99.29000  ? 336 CYS D SG  1 
ATOM   2248 N N   . PRO D 2 5   ? 49.82900 16.13400  -22.23900 1.000 97.56000  ? 337 PRO D N   1 
ATOM   2249 C CA  . PRO D 2 5   ? 50.55500 16.11500  -20.93400 1.000 93.16000  ? 337 PRO D CA  1 
ATOM   2250 C C   . PRO D 2 5   ? 49.94400 15.15200  -19.92500 1.000 100.41000 ? 337 PRO D C   1 
ATOM   2251 O O   . PRO D 2 5   ? 49.64400 15.53300  -18.78100 1.000 100.41000 ? 337 PRO D O   1 
ATOM   2252 C CB  . PRO D 2 5   ? 50.44300 17.56700  -20.48500 1.000 96.16000  ? 337 PRO D CB  1 
ATOM   2253 C CG  . PRO D 2 5   ? 49.10000 17.97500  -20.97300 1.000 98.43000  ? 337 PRO D CG  1 
ATOM   2254 C CD  . PRO D 2 5   ? 48.93700 17.29600  -22.32800 1.000 99.75000  ? 337 PRO D CD  1 
ATOM   2255 N N   . PHE D 2 6   ? 49.78400 13.88700  -20.32200 1.000 100.33000 ? 338 PHE D N   1 
ATOM   2256 C CA  . PHE D 2 6   ? 49.29100 12.87000  -19.39900 1.000 97.99000  ? 338 PHE D CA  1 
ATOM   2257 C C   . PHE D 2 6   ? 50.10000 12.82900  -18.10800 1.000 96.56000  ? 338 PHE D C   1 
ATOM   2258 O O   . PHE D 2 6   ? 49.56900 12.44000  -17.06400 1.000 98.32000  ? 338 PHE D O   1 
ATOM   2259 C CB  . PHE D 2 6   ? 49.30800 11.49400  -20.06900 1.000 96.79000  ? 338 PHE D CB  1 
ATOM   2260 C CG  . PHE D 2 6   ? 48.23800 11.30400  -21.11600 1.000 100.82000 ? 338 PHE D CG  1 
ATOM   2261 C CD1 . PHE D 2 6   ? 46.91700 11.64900  -20.86100 1.000 101.08000 ? 338 PHE D CD1 1 
ATOM   2262 C CD2 . PHE D 2 6   ? 48.55900 10.76900  -22.36300 1.000 100.51000 ? 338 PHE D CD2 1 
ATOM   2263 C CE1 . PHE D 2 6   ? 45.93000 11.46800  -21.83800 1.000 97.90000  ? 338 PHE D CE1 1 
ATOM   2264 C CE2 . PHE D 2 6   ? 47.58200 10.58600  -23.34100 1.000 98.62000  ? 338 PHE D CE2 1 
ATOM   2265 C CZ  . PHE D 2 6   ? 46.26800 10.93600  -23.08100 1.000 98.27000  ? 338 PHE D CZ  1 
ATOM   2266 N N   . GLY D 2 7   ? 51.37600 13.22700  -18.15600 1.000 95.70000  ? 339 GLY D N   1 
ATOM   2267 C CA  . GLY D 2 7   ? 52.17700 13.28200  -16.94500 1.000 92.24000  ? 339 GLY D CA  1 
ATOM   2268 C C   . GLY D 2 7   ? 51.59900 14.19700  -15.88600 1.000 93.21000  ? 339 GLY D C   1 
ATOM   2269 O O   . GLY D 2 7   ? 51.70300 13.91100  -14.69200 1.000 95.98000  ? 339 GLY D O   1 
ATOM   2270 N N   . GLU D 2 8   ? 50.97500 15.30400  -16.29800 1.000 93.80000  ? 340 GLU D N   1 
ATOM   2271 C CA  . GLU D 2 8   ? 50.35700 16.20800  -15.33400 1.000 93.54000  ? 340 GLU D CA  1 
ATOM   2272 C C   . GLU D 2 8   ? 49.19700 15.55900  -14.59500 1.000 98.77000  ? 340 GLU D C   1 
ATOM   2273 O O   . GLU D 2 8   ? 48.86500 15.99600  -13.48500 1.000 99.92000  ? 340 GLU D O   1 
ATOM   2274 C CB  . GLU D 2 8   ? 49.86600 17.48200  -16.02500 1.000 98.81000  ? 340 GLU D CB  1 
ATOM   2275 C CG  . GLU D 2 8   ? 50.96000 18.47900  -16.35900 1.000 102.56000 ? 340 GLU D CG  1 
ATOM   2276 C CD  . GLU D 2 8   ? 50.40900 19.79700  -16.87200 1.000 104.31000 ? 340 GLU D CD  1 
ATOM   2277 O OE1 . GLU D 2 8   ? 49.17700 20.00600  -16.77700 1.000 102.71000 ? 340 GLU D OE1 1 
ATOM   2278 O OE2 . GLU D 2 8   ? 51.20600 20.62100  -17.36900 1.000 106.38000 ? 340 GLU D OE2 1 
ATOM   2279 N N   . VAL D 2 9   ? 48.57400 14.53800  -15.18800 1.000 98.80000  ? 341 VAL D N   1 
ATOM   2280 C CA  . VAL D 2 9   ? 47.46200 13.83100  -14.56800 1.000 91.16000  ? 341 VAL D CA  1 
ATOM   2281 C C   . VAL D 2 9   ? 48.02200 12.65300  -13.78300 1.000 91.45000  ? 341 VAL D C   1 
ATOM   2282 O O   . VAL D 2 9   ? 47.81200 12.54200  -12.57100 1.000 90.13000  ? 341 VAL D O   1 
ATOM   2283 C CB  . VAL D 2 9   ? 46.43100 13.37200  -15.62100 1.000 88.86000  ? 341 VAL D CB  1 
ATOM   2284 C CG1 . VAL D 2 9   ? 45.20000 12.81000  -14.94100 1.000 82.07000  ? 341 VAL D CG1 1 
ATOM   2285 C CG2 . VAL D 2 9   ? 46.05000 14.53100  -16.53500 1.000 86.97000  ? 341 VAL D CG2 1 
ATOM   2286 N N   . PHE D 2 10  ? 48.75700 11.78000  -14.46700 1.000 92.81000  ? 342 PHE D N   1 
ATOM   2287 C CA  . PHE D 2 10  ? 49.21100 10.54200  -13.84300 1.000 89.75000  ? 342 PHE D CA  1 
ATOM   2288 C C   . PHE D 2 10  ? 50.33300 10.80000  -12.84800 1.000 92.44000  ? 342 PHE D C   1 
ATOM   2289 O O   . PHE D 2 10  ? 50.31300 10.27800  -11.72500 1.000 88.15000  ? 342 PHE D O   1 
ATOM   2290 C CB  . PHE D 2 10  ? 49.66500 9.55500   -14.91800 1.000 92.68000  ? 342 PHE D CB  1 
ATOM   2291 C CG  . PHE D 2 10  ? 48.53400 8.91800   -15.64900 1.000 90.25000  ? 342 PHE D CG  1 
ATOM   2292 C CD1 . PHE D 2 10  ? 47.92600 7.78200   -15.15200 1.000 89.93000  ? 342 PHE D CD1 1 
ATOM   2293 C CD2 . PHE D 2 10  ? 48.05600 9.46800   -16.81800 1.000 89.65000  ? 342 PHE D CD2 1 
ATOM   2294 C CE1 . PHE D 2 10  ? 46.87400 7.19600   -15.81400 1.000 86.49000  ? 342 PHE D CE1 1 
ATOM   2295 C CE2 . PHE D 2 10  ? 47.00700 8.88900   -17.47900 1.000 85.58000  ? 342 PHE D CE2 1 
ATOM   2296 C CZ  . PHE D 2 10  ? 46.41400 7.75200   -16.97400 1.000 82.94000  ? 342 PHE D CZ  1 
ATOM   2297 N N   . ASN D 2 11  ? 51.32500 11.60100  -13.24700 1.000 94.81000  ? 343 ASN D N   1 
ATOM   2298 C CA  . ASN D 2 11  ? 52.50100 11.87300  -12.43000 1.000 93.25000  ? 343 ASN D CA  1 
ATOM   2299 C C   . ASN D 2 11  ? 52.34200 13.12900  -11.55900 1.000 94.56000  ? 343 ASN D C   1 
ATOM   2300 O O   . ASN D 2 11  ? 53.34200 13.74100  -11.16400 1.000 94.48000  ? 343 ASN D O   1 
ATOM   2301 C CB  . ASN D 2 11  ? 53.74200 11.97700  -13.32500 1.000 90.56000  ? 343 ASN D CB  1 
ATOM   2302 C CG  . ASN D 2 11  ? 54.27600 10.60700  -13.77300 1.000 95.80000  ? 343 ASN D CG  1 
ATOM   2303 O OD1 . ASN D 2 11  ? 54.13900 9.62000   -13.06000 1.000 96.10000  ? 343 ASN D OD1 1 
ATOM   2304 N ND2 . ASN D 2 11  ? 54.89400 10.55500  -14.96100 1.000 102.97000 ? 343 ASN D ND2 1 
ATOM   2305 N N   . ALA D 2 12  ? 51.11600 13.53000  -11.23500 1.000 91.31000  ? 344 ALA D N   1 
ATOM   2306 C CA  . ALA D 2 12  ? 50.92100 14.68600  -10.37000 1.000 91.43000  ? 344 ALA D CA  1 
ATOM   2307 C C   . ALA D 2 12  ? 51.11500 14.30700  -8.90600  1.000 89.81000  ? 344 ALA D C   1 
ATOM   2308 O O   . ALA D 2 12  ? 50.71200 13.22700  -8.46300  1.000 88.51000  ? 344 ALA D O   1 
ATOM   2309 C CB  . ALA D 2 12  ? 49.53100 15.28900  -10.56400 1.000 92.46000  ? 344 ALA D CB  1 
ATOM   2310 N N   . THR D 2 13  ? 51.73600 15.21000  -8.14800  1.000 87.21000  ? 345 THR D N   1 
ATOM   2311 C CA  . THR D 2 13  ? 52.00600 14.91500  -6.74500  1.000 89.93000  ? 345 THR D CA  1 
ATOM   2312 C C   . THR D 2 13  ? 50.71000 14.72700  -5.96600  1.000 88.02000  ? 345 THR D C   1 
ATOM   2313 O O   . THR D 2 13  ? 50.54000 13.73100  -5.25000  1.000 86.13000  ? 345 THR D O   1 
ATOM   2314 C CB  . THR D 2 13  ? 52.84700 16.02800  -6.11900  1.000 88.78000  ? 345 THR D CB  1 
ATOM   2315 O OG1 . THR D 2 13  ? 54.04700 16.22200  -6.88000  1.000 90.96000  ? 345 THR D OG1 1 
ATOM   2316 C CG2 . THR D 2 13  ? 53.22200 15.65000  -4.70400  1.000 92.76000  ? 345 THR D CG2 1 
ATOM   2317 N N   . ARG D 2 14  ? 49.76900 15.65500  -6.12200  1.000 87.17000  ? 346 ARG D N   1 
ATOM   2318 C CA  . ARG D 2 14  ? 48.58900 15.72600  -5.27300  1.000 86.98000  ? 346 ARG D CA  1 
ATOM   2319 C C   . ARG D 2 14  ? 47.34300 15.33600  -6.06800  1.000 84.39000  ? 346 ARG D C   1 
ATOM   2320 O O   . ARG D 2 14  ? 46.90000 16.07100  -6.95400  1.000 89.30000  ? 346 ARG D O   1 
ATOM   2321 C CB  . ARG D 2 14  ? 48.46700 17.12600  -4.67500  1.000 95.72000  ? 346 ARG D CB  1 
ATOM   2322 C CG  . ARG D 2 14  ? 49.57700 17.46800  -3.63600  1.000 99.45000  ? 346 ARG D CG  1 
ATOM   2323 C CD  . ARG D 2 14  ? 49.40000 18.87900  -3.02500  1.000 97.39000  ? 346 ARG D CD  1 
ATOM   2324 N NE  . ARG D 2 14  ? 48.02900 19.09700  -2.55600  1.000 98.70000  ? 346 ARG D NE  1 
ATOM   2325 C CZ  . ARG D 2 14  ? 47.47700 20.28400  -2.31400  1.000 99.43000  ? 346 ARG D CZ  1 
ATOM   2326 N NH1 . ARG D 2 14  ? 48.17700 21.40300  -2.48600  1.000 100.50000 ? 346 ARG D NH1 1 
ATOM   2327 N NH2 . ARG D 2 14  ? 46.21800 20.34700  -1.89600  1.000 98.01000  ? 346 ARG D NH2 1 
ATOM   2328 N N   . PHE D 2 15  ? 46.77900 14.18700  -5.74200  1.000 80.47000  ? 347 PHE D N   1 
ATOM   2329 C CA  . PHE D 2 15  ? 45.47100 13.79800  -6.22500  1.000 79.65000  ? 347 PHE D CA  1 
ATOM   2330 C C   . PHE D 2 15  ? 44.37300 14.26800  -5.26500  1.000 80.43000  ? 347 PHE D C   1 
ATOM   2331 O O   . PHE D 2 15  ? 44.62000 14.62400  -4.11000  1.000 82.08000  ? 347 PHE D O   1 
ATOM   2332 C CB  . PHE D 2 15  ? 45.40600 12.28700  -6.39900  1.000 85.94000  ? 347 PHE D CB  1 
ATOM   2333 C CG  . PHE D 2 15  ? 45.90800 11.80000  -7.73200  1.000 82.31000  ? 347 PHE D CG  1 
ATOM   2334 C CD1 . PHE D 2 15  ? 47.17400 12.13800  -8.18300  1.000 81.11000  ? 347 PHE D CD1 1 
ATOM   2335 C CD2 . PHE D 2 15  ? 45.11600 10.96600  -8.52100  1.000 79.26000  ? 347 PHE D CD2 1 
ATOM   2336 C CE1 . PHE D 2 15  ? 47.63700 11.67000  -9.39600  1.000 79.97000  ? 347 PHE D CE1 1 
ATOM   2337 C CE2 . PHE D 2 15  ? 45.57600 10.49100  -9.74200  1.000 81.72000  ? 347 PHE D CE2 1 
ATOM   2338 C CZ  . PHE D 2 15  ? 46.83700 10.84400  -10.17600 1.000 82.33000  ? 347 PHE D CZ  1 
ATOM   2339 N N   . ALA D 2 16  ? 43.13900 14.23400  -5.75500  1.000 83.20000  ? 348 ALA D N   1 
ATOM   2340 C CA  . ALA D 2 16  ? 41.99200 14.83000  -5.08900  1.000 82.82000  ? 348 ALA D CA  1 
ATOM   2341 C C   . ALA D 2 16  ? 41.16700 13.80400  -4.31600  1.000 77.90000  ? 348 ALA D C   1 
ATOM   2342 O O   . ALA D 2 16  ? 41.24400 12.59900  -4.53300  1.000 80.59000  ? 348 ALA D O   1 
ATOM   2343 C CB  . ALA D 2 16  ? 41.09700 15.52300  -6.11400  1.000 77.96000  ? 348 ALA D CB  1 
ATOM   2344 N N   . SER D 2 17  ? 40.33900 14.30000  -3.42200  1.000 70.38000  ? 349 SER D N   1 
ATOM   2345 C CA  . SER D 2 17  ? 39.41200 13.40100  -2.77000  1.000 77.82000  ? 349 SER D CA  1 
ATOM   2346 C C   . SER D 2 17  ? 38.29900 13.05900  -3.74700  1.000 76.44000  ? 349 SER D C   1 
ATOM   2347 O O   . SER D 2 17  ? 37.86700 13.89600  -4.53700  1.000 76.36000  ? 349 SER D O   1 
ATOM   2348 C CB  . SER D 2 17  ? 38.84300 14.03000  -1.48700  1.000 80.86000  ? 349 SER D CB  1 
ATOM   2349 O OG  . SER D 2 17  ? 39.85200 14.19500  -0.50400  1.000 79.89000  ? 349 SER D OG  1 
ATOM   2350 N N   . VAL D 2 18  ? 37.81800 11.82100  -3.66200  1.000 73.42000  ? 350 VAL D N   1 
ATOM   2351 C CA  . VAL D 2 18  ? 36.78100 11.33300  -4.56300  1.000 72.73000  ? 350 VAL D CA  1 
ATOM   2352 C C   . VAL D 2 18  ? 35.51500 12.19700  -4.53100  1.000 75.92000  ? 350 VAL D C   1 
ATOM   2353 O O   . VAL D 2 18  ? 34.77400 12.25900  -5.52100  1.000 78.93000  ? 350 VAL D O   1 
ATOM   2354 C CB  . VAL D 2 18  ? 36.47400 9.86800   -4.22000  1.000 72.40000  ? 350 VAL D CB  1 
ATOM   2355 C CG1 . VAL D 2 18  ? 35.92400 9.77300   -2.81900  1.000 83.04000  ? 350 VAL D CG1 1 
ATOM   2356 C CG2 . VAL D 2 18  ? 35.50200 9.28800   -5.20700  1.000 74.15000  ? 350 VAL D CG2 1 
ATOM   2357 N N   . TYR D 2 19  ? 35.23300 12.87600  -3.42200  1.000 82.74000  ? 351 TYR D N   1 
ATOM   2358 C CA  . TYR D 2 19  ? 34.02700 13.70000  -3.43900  1.000 81.81000  ? 351 TYR D CA  1 
ATOM   2359 C C   . TYR D 2 19  ? 34.27800 15.01000  -4.17100  1.000 80.24000  ? 351 TYR D C   1 
ATOM   2360 O O   . TYR D 2 19  ? 33.40900 15.48400  -4.91100  1.000 84.22000  ? 351 TYR D O   1 
ATOM   2361 C CB  . TYR D 2 19  ? 33.50100 13.93800  -2.01800  1.000 77.48000  ? 351 TYR D CB  1 
ATOM   2362 C CG  . TYR D 2 19  ? 34.01900 15.17400  -1.32300  1.000 77.71000  ? 351 TYR D CG  1 
ATOM   2363 C CD1 . TYR D 2 19  ? 35.30800 15.22800  -0.82000  1.000 78.91000  ? 351 TYR D CD1 1 
ATOM   2364 C CD2 . TYR D 2 19  ? 33.19800 16.27300  -1.12600  1.000 82.18000  ? 351 TYR D CD2 1 
ATOM   2365 C CE1 . TYR D 2 19  ? 35.77200 16.35500  -0.16800  1.000 81.56000  ? 351 TYR D CE1 1 
ATOM   2366 C CE2 . TYR D 2 19  ? 33.65200 17.40500  -0.46500  1.000 80.33000  ? 351 TYR D CE2 1 
ATOM   2367 C CZ  . TYR D 2 19  ? 34.94000 17.43600  0.00200   1.000 81.46000  ? 351 TYR D CZ  1 
ATOM   2368 O OH  . TYR D 2 19  ? 35.39300 18.56600  0.63000   1.000 86.21000  ? 351 TYR D OH  1 
ATOM   2369 N N   . ALA D 2 20  ? 35.48054 15.55779  -4.04387  1.000 75.40244  ? 352 ALA D N   1 
ATOM   2370 C CA  . ALA D 2 20  ? 35.84138 16.77198  -4.75902  1.000 76.26660  ? 352 ALA D CA  1 
ATOM   2371 C C   . ALA D 2 20  ? 36.80275 16.47907  -5.89552  1.000 75.86060  ? 352 ALA D C   1 
ATOM   2372 O O   . ALA D 2 20  ? 37.84342 17.12734  -6.03413  1.000 73.65157  ? 352 ALA D O   1 
ATOM   2373 C CB  . ALA D 2 20  ? 36.46227 17.78159  -3.81039  1.000 80.79000  ? 352 ALA D CB  1 
ATOM   2374 N N   . TRP D 2 21  ? 36.41600 15.52600  -6.72800  1.000 76.60000  ? 353 TRP D N   1 
ATOM   2375 C CA  . TRP D 2 21  ? 37.26000 14.97800  -7.78900  1.000 82.76000  ? 353 TRP D CA  1 
ATOM   2376 C C   . TRP D 2 21  ? 37.59000 16.01300  -8.86200  1.000 78.62000  ? 353 TRP D C   1 
ATOM   2377 O O   . TRP D 2 21  ? 36.73900 16.81200  -9.25500  1.000 81.53000  ? 353 TRP D O   1 
ATOM   2378 C CB  . TRP D 2 21  ? 36.55600 13.78400  -8.43400  1.000 82.33000  ? 353 TRP D CB  1 
ATOM   2379 C CG  . TRP D 2 21  ? 35.15700 14.07400  -8.91500  1.000 81.82000  ? 353 TRP D CG  1 
ATOM   2380 C CD1 . TRP D 2 21  ? 33.98900 13.92600  -8.21000  1.000 78.99000  ? 353 TRP D CD1 1 
ATOM   2381 C CD2 . TRP D 2 21  ? 34.77800 14.53800  -10.21500 1.000 82.41000  ? 353 TRP D CD2 1 
ATOM   2382 N NE1 . TRP D 2 21  ? 32.90600 14.28400  -8.99300  1.000 77.21000  ? 353 TRP D NE1 1 
ATOM   2383 C CE2 . TRP D 2 21  ? 33.36700 14.65800  -10.22900 1.000 85.67000  ? 353 TRP D CE2 1 
ATOM   2384 C CE3 . TRP D 2 21  ? 35.49200 14.85900  -11.37100 1.000 80.33000  ? 353 TRP D CE3 1 
ATOM   2385 C CZ2 . TRP D 2 21  ? 32.66500 15.09000  -11.36200 1.000 85.29000  ? 353 TRP D CZ2 1 
ATOM   2386 C CZ3 . TRP D 2 21  ? 34.79300 15.29000  -12.48800 1.000 79.47000  ? 353 TRP D CZ3 1 
ATOM   2387 C CH2 . TRP D 2 21  ? 33.39700 15.40700  -12.47300 1.000 79.08000  ? 353 TRP D CH2 1 
ATOM   2388 N N   . ASN D 2 22  ? 38.82300 15.96900  -9.36000  1.000 73.76000  ? 354 ASN D N   1 
ATOM   2389 C CA  . ASN D 2 22  ? 39.35900 16.97700  -10.27000 1.000 81.22000  ? 354 ASN D CA  1 
ATOM   2390 C C   . ASN D 2 22  ? 39.36700 16.49800  -11.72300 1.000 84.38000  ? 354 ASN D C   1 
ATOM   2391 O O   . ASN D 2 22  ? 39.59600 15.31800  -12.00300 1.000 81.61000  ? 354 ASN D O   1 
ATOM   2392 C CB  . ASN D 2 22  ? 40.77900 17.35700  -9.85600  1.000 81.89000  ? 354 ASN D CB  1 
ATOM   2393 C CG  . ASN D 2 22  ? 41.47100 18.19700  -10.89300 1.000 89.68000  ? 354 ASN D CG  1 
ATOM   2394 O OD1 . ASN D 2 22  ? 42.26200 17.69300  -11.70100 1.000 92.31000  ? 354 ASN D OD1 1 
ATOM   2395 N ND2 . ASN D 2 22  ? 41.15300 19.48500  -10.90600 1.000 93.65000  ? 354 ASN D ND2 1 
ATOM   2396 N N   . ARG D 2 23  ? 39.15700 17.44200  -12.65000 1.000 84.29000  ? 355 ARG D N   1 
ATOM   2397 C CA  . ARG D 2 23  ? 39.02600 17.16800  -14.07900 1.000 83.41000  ? 355 ARG D CA  1 
ATOM   2398 C C   . ARG D 2 23  ? 39.99800 18.00900  -14.89800 1.000 78.31000  ? 355 ARG D C   1 
ATOM   2399 O O   . ARG D 2 23  ? 40.01900 19.23600  -14.78000 1.000 84.79000  ? 355 ARG D O   1 
ATOM   2400 C CB  . ARG D 2 23  ? 37.59800 17.45200  -14.54100 1.000 84.71000  ? 355 ARG D CB  1 
ATOM   2401 C CG  . ARG D 2 23  ? 37.39600 17.51600  -16.05200 1.000 78.74000  ? 355 ARG D CG  1 
ATOM   2402 C CD  . ARG D 2 23  ? 35.90200 17.50400  -16.33700 1.000 79.03000  ? 355 ARG D CD  1 
ATOM   2403 N NE  . ARG D 2 23  ? 35.38900 16.14400  -16.47700 1.000 83.02000  ? 355 ARG D NE  1 
ATOM   2404 C CZ  . ARG D 2 23  ? 34.10100 15.83200  -16.62400 1.000 83.09000  ? 355 ARG D CZ  1 
ATOM   2405 N NH1 . ARG D 2 23  ? 33.17900 16.78400  -16.64400 1.000 85.88000  ? 355 ARG D NH1 1 
ATOM   2406 N NH2 . ARG D 2 23  ? 33.73300 14.56200  -16.75000 1.000 80.00000  ? 355 ARG D NH2 1 
ATOM   2407 N N   . LYS D 2 24  ? 40.76800 17.36000  -15.75900 1.000 75.39000  ? 356 LYS D N   1 
ATOM   2408 C CA  . LYS D 2 24  ? 41.68900 18.05200  -16.64900 1.000 83.83000  ? 356 LYS D CA  1 
ATOM   2409 C C   . LYS D 2 24  ? 41.26700 17.83500  -18.10900 1.000 81.65000  ? 356 LYS D C   1 
ATOM   2410 O O   . LYS D 2 24  ? 40.97200 16.70300  -18.52200 1.000 78.63000  ? 356 LYS D O   1 
ATOM   2411 C CB  . LYS D 2 24  ? 43.11900 17.56900  -16.38800 1.000 80.58000  ? 356 LYS D CB  1 
ATOM   2412 C CG  . LYS D 2 24  ? 44.14100 17.97100  -17.42900 1.000 85.43000  ? 356 LYS D CG  1 
ATOM   2413 C CD  . LYS D 2 24  ? 45.00000 19.13100  -16.96700 1.000 83.69000  ? 356 LYS D CD  1 
ATOM   2414 C CE  . LYS D 2 24  ? 46.20000 19.28900  -17.89800 1.000 86.04000  ? 356 LYS D CE  1 
ATOM   2415 N NZ  . LYS D 2 24  ? 46.98900 20.52900  -17.62300 1.000 88.58000  ? 356 LYS D NZ  1 
ATOM   2416 N N   . ARG D 2 25  ? 41.21800 18.92200  -18.88500 1.000 80.01000  ? 357 ARG D N   1 
ATOM   2417 C CA  . ARG D 2 25  ? 40.80100 18.86100  -20.28400 1.000 82.38000  ? 357 ARG D CA  1 
ATOM   2418 C C   . ARG D 2 25  ? 42.02400 18.78700  -21.18000 1.000 78.25000  ? 357 ARG D C   1 
ATOM   2419 O O   . ARG D 2 25  ? 42.84400 19.71200  -21.19700 1.000 80.47000  ? 357 ARG D O   1 
ATOM   2420 C CB  . ARG D 2 25  ? 39.96100 20.06500  -20.70000 1.000 81.03000  ? 357 ARG D CB  1 
ATOM   2421 C CG  . ARG D 2 25  ? 39.54200 19.96700  -22.17300 1.000 87.64000  ? 357 ARG D CG  1 
ATOM   2422 C CD  . ARG D 2 25  ? 38.78000 21.18200  -22.66100 1.000 87.79000  ? 357 ARG D CD  1 
ATOM   2423 N NE  . ARG D 2 25  ? 37.34300 20.95900  -22.65100 1.000 98.39000  ? 357 ARG D NE  1 
ATOM   2424 C CZ  . ARG D 2 25  ? 36.46100 21.79600  -22.11800 1.000 100.44000 ? 357 ARG D CZ  1 
ATOM   2425 N NH1 . ARG D 2 25  ? 36.87500 22.91400  -21.54900 1.000 102.59000 ? 357 ARG D NH1 1 
ATOM   2426 N NH2 . ARG D 2 25  ? 35.17200 21.51300  -22.15600 1.000 91.34000  ? 357 ARG D NH2 1 
ATOM   2427 N N   . ILE D 2 26  ? 42.11500 17.71300  -21.95000 1.000 73.08000  ? 358 ILE D N   1 
ATOM   2428 C CA  . ILE D 2 26  ? 43.25700 17.43400  -22.80900 1.000 79.38000  ? 358 ILE D CA  1 
ATOM   2429 C C   . ILE D 2 26  ? 42.79500 17.60300  -24.24900 1.000 83.47000  ? 358 ILE D C   1 
ATOM   2430 O O   . ILE D 2 26  ? 41.92200 16.86400  -24.73000 1.000 76.81000  ? 358 ILE D O   1 
ATOM   2431 C CB  . ILE D 2 26  ? 43.81200 16.03000  -22.55200 1.000 81.78000  ? 358 ILE D CB  1 
ATOM   2432 C CG1 . ILE D 2 26  ? 44.50300 15.99200  -21.19000 1.000 83.34000  ? 358 ILE D CG1 1 
ATOM   2433 C CG2 . ILE D 2 26  ? 44.73900 15.60400  -23.67800 1.000 77.50000  ? 358 ILE D CG2 1 
ATOM   2434 C CD1 . ILE D 2 26  ? 45.00800 14.63600  -20.81900 1.000 86.00000  ? 358 ILE D CD1 1 
ATOM   2435 N N   . SER D 2 27  ? 43.36200 18.59100  -24.93600 1.000 84.58000  ? 359 SER D N   1 
ATOM   2436 C CA  . SER D 2 27  ? 42.96100 18.88200  -26.30500 1.000 89.62000  ? 359 SER D CA  1 
ATOM   2437 C C   . SER D 2 27  ? 44.16400 19.35100  -27.10500 1.000 89.14000  ? 359 SER D C   1 
ATOM   2438 O O   . SER D 2 27  ? 45.13300 19.87600  -26.55100 1.000 87.86000  ? 359 SER D O   1 
ATOM   2439 C CB  . SER D 2 27  ? 41.86800 19.94200  -26.36100 1.000 89.34000  ? 359 SER D CB  1 
ATOM   2440 O OG  . SER D 2 27  ? 42.28400 21.10500  -25.68200 1.000 89.19000  ? 359 SER D OG  1 
ATOM   2441 N N   . ASN D 2 28  ? 44.07800 19.15900  -28.42400 1.000 87.80000  ? 360 ASN D N   1 
ATOM   2442 C CA  . ASN D 2 28  ? 45.05600 19.67800  -29.38100 1.000 88.03000  ? 360 ASN D CA  1 
ATOM   2443 C C   . ASN D 2 28  ? 46.45200 19.10800  -29.11800 1.000 88.47000  ? 360 ASN D C   1 
ATOM   2444 O O   . ASN D 2 28  ? 47.37300 19.80000  -28.66800 1.000 90.91000  ? 360 ASN D O   1 
ATOM   2445 C CB  . ASN D 2 28  ? 45.07000 21.21100  -29.35700 1.000 87.83000  ? 360 ASN D CB  1 
ATOM   2446 C CG  . ASN D 2 28  ? 44.06400 21.80800  -30.31500 1.000 95.37000  ? 360 ASN D CG  1 
ATOM   2447 O OD1 . ASN D 2 28  ? 44.10400 21.54100  -31.52400 1.000 97.23000  ? 360 ASN D OD1 1 
ATOM   2448 N ND2 . ASN D 2 28  ? 43.13800 22.59900  -29.78300 1.000 94.90000  ? 360 ASN D ND2 1 
ATOM   2449 N N   . CYS D 2 29  ? 46.58700 17.82300  -29.44100 1.000 82.04000  ? 361 CYS D N   1 
ATOM   2450 C CA  . CYS D 2 29  ? 47.83500 17.10900  -29.19000 1.000 86.53000  ? 361 CYS D CA  1 
ATOM   2451 C C   . CYS D 2 29  ? 47.68400 15.67600  -29.68700 1.000 85.34000  ? 361 CYS D C   1 
ATOM   2452 O O   . CYS D 2 29  ? 46.58700 15.22200  -30.02700 1.000 82.07000  ? 361 CYS D O   1 
ATOM   2453 C CB  . CYS D 2 29  ? 48.23400 17.13300  -27.69800 1.000 96.15000  ? 361 CYS D CB  1 
ATOM   2454 S SG  . CYS D 2 29  ? 46.95200 16.54400  -26.51200 1.000 96.14000  ? 361 CYS D SG  1 
ATOM   2455 N N   . VAL D 2 30  ? 48.81300 14.97600  -29.73600 1.000 90.94000  ? 362 VAL D N   1 
ATOM   2456 C CA  . VAL D 2 30  ? 48.87200 13.57100  -30.12200 1.000 92.47000  ? 362 VAL D CA  1 
ATOM   2457 C C   . VAL D 2 30  ? 49.22100 12.75400  -28.88800 1.000 89.85000  ? 362 VAL D C   1 
ATOM   2458 O O   . VAL D 2 30  ? 49.99100 13.19900  -28.02600 1.000 91.46000  ? 362 VAL D O   1 
ATOM   2459 C CB  . VAL D 2 30  ? 49.88600 13.31600  -31.25500 1.000 90.41000  ? 362 VAL D CB  1 
ATOM   2460 C CG1 . VAL D 2 30  ? 51.27500 13.82900  -30.85600 1.000 93.90000  ? 362 VAL D CG1 1 
ATOM   2461 C CG2 . VAL D 2 30  ? 49.92400 11.83100  -31.62200 1.000 87.66000  ? 362 VAL D CG2 1 
ATOM   2462 N N   . ALA D 2 31  ? 48.65000 11.55700  -28.79100 1.000 90.43000  ? 363 ALA D N   1 
ATOM   2463 C CA  . ALA D 2 31  ? 48.83400 10.75200  -27.58900 1.000 94.02000  ? 363 ALA D CA  1 
ATOM   2464 C C   . ALA D 2 31  ? 49.12700 9.31500   -27.97100 1.000 89.99000  ? 363 ALA D C   1 
ATOM   2465 O O   . ALA D 2 31  ? 48.39600 8.72500   -28.77100 1.000 92.72000  ? 363 ALA D O   1 
ATOM   2466 C CB  . ALA D 2 31  ? 47.59700 10.82200  -26.68800 1.000 99.16000  ? 363 ALA D CB  1 
ATOM   2467 N N   . ASP D 2 32  ? 50.18000 8.75100   -27.38700 1.000 95.74000  ? 364 ASP D N   1 
ATOM   2468 C CA  . ASP D 2 32  ? 50.39800 7.30800   -27.47200 1.000 98.32000  ? 364 ASP D CA  1 
ATOM   2469 C C   . ASP D 2 32  ? 49.77500 6.65500   -26.23900 1.000 100.96000 ? 364 ASP D C   1 
ATOM   2470 O O   . ASP D 2 32  ? 50.28500 6.76900   -25.11900 1.000 94.92000  ? 364 ASP D O   1 
ATOM   2471 C CB  . ASP D 2 32  ? 51.87800 6.97200   -27.59900 1.000 96.56000  ? 364 ASP D CB  1 
ATOM   2472 C CG  . ASP D 2 32  ? 52.11000 5.59700   -28.22900 1.000 103.93000 ? 364 ASP D CG  1 
ATOM   2473 O OD1 . ASP D 2 32  ? 51.26900 4.69400   -28.02300 1.000 102.89000 ? 364 ASP D OD1 1 
ATOM   2474 O OD2 . ASP D 2 32  ? 53.12100 5.42300   -28.94300 1.000 110.12000 ? 364 ASP D OD2 1 
ATOM   2475 N N   . TYR D 2 33  ? 48.65100 5.97100   -26.45300 1.000 99.34000  ? 365 TYR D N   1 
ATOM   2476 C CA  . TYR D 2 33  ? 47.96500 5.29900   -25.36100 1.000 98.34000  ? 365 TYR D CA  1 
ATOM   2477 C C   . TYR D 2 33  ? 48.69000 4.01600   -24.97700 1.000 100.51000 ? 365 TYR D C   1 
ATOM   2478 O O   . TYR D 2 33  ? 48.82800 3.70700   -23.79000 1.000 102.43000 ? 365 TYR D O   1 
ATOM   2479 C CB  . TYR D 2 33  ? 46.50600 5.03400   -25.75300 1.000 95.87000  ? 365 TYR D CB  1 
ATOM   2480 C CG  . TYR D 2 33  ? 45.67700 6.30500   -25.86400 1.000 96.03000  ? 365 TYR D CG  1 
ATOM   2481 C CD1 . TYR D 2 33  ? 45.17100 6.94200   -24.73600 1.000 93.45000  ? 365 TYR D CD1 1 
ATOM   2482 C CD2 . TYR D 2 33  ? 45.43500 6.88500   -27.09000 1.000 96.36000  ? 365 TYR D CD2 1 
ATOM   2483 C CE1 . TYR D 2 33  ? 44.42400 8.10100   -24.84700 1.000 93.56000  ? 365 TYR D CE1 1 
ATOM   2484 C CE2 . TYR D 2 33  ? 44.69800 8.03800   -27.20800 1.000 95.33000  ? 365 TYR D CE2 1 
ATOM   2485 C CZ  . TYR D 2 33  ? 44.19900 8.64000   -26.09500 1.000 94.19000  ? 365 TYR D CZ  1 
ATOM   2486 O OH  . TYR D 2 33  ? 43.46900 9.78500   -26.26700 1.000 92.61000  ? 365 TYR D OH  1 
ATOM   2487 N N   . SER D 2 34  ? 49.19700 3.27300   -25.95500 1.000 102.02000 ? 366 SER D N   1 
ATOM   2488 C CA  . SER D 2 34  ? 49.98700 2.09700   -25.61800 1.000 100.44000 ? 366 SER D CA  1 
ATOM   2489 C C   . SER D 2 34  ? 51.26200 2.46400   -24.85600 1.000 99.75000  ? 366 SER D C   1 
ATOM   2490 O O   . SER D 2 34  ? 51.73200 1.65500   -24.04900 1.000 102.54000 ? 366 SER D O   1 
ATOM   2491 C CB  . SER D 2 34  ? 50.29200 1.29600   -26.89200 1.000 102.57000 ? 366 SER D CB  1 
ATOM   2492 O OG  . SER D 2 34  ? 49.09500 0.84400   -27.51400 1.000 103.77000 ? 366 SER D OG  1 
ATOM   2493 N N   . VAL D 2 35  ? 51.81300 3.66900   -25.04900 1.000 95.89000  ? 367 VAL D N   1 
ATOM   2494 C CA  . VAL D 2 35  ? 52.90900 4.09200   -24.17400 1.000 96.59000  ? 367 VAL D CA  1 
ATOM   2495 C C   . VAL D 2 35  ? 52.39500 4.33900   -22.77600 1.000 100.20000 ? 367 VAL D C   1 
ATOM   2496 O O   . VAL D 2 35  ? 52.99000 3.87900   -21.79800 1.000 102.84000 ? 367 VAL D O   1 
ATOM   2497 C CB  . VAL D 2 35  ? 53.63000 5.33900   -24.70500 1.000 97.96000  ? 367 VAL D CB  1 
ATOM   2498 C CG1 . VAL D 2 35  ? 54.69600 5.82100   -23.68600 1.000 95.42000  ? 367 VAL D CG1 1 
ATOM   2499 C CG2 . VAL D 2 35  ? 54.28700 5.00900   -26.03100 1.000 104.88000 ? 367 VAL D CG2 1 
ATOM   2500 N N   . LEU D 2 36  ? 51.30600 5.09700   -22.65200 1.000 99.00000  ? 368 LEU D N   1 
ATOM   2501 C CA  . LEU D 2 36  ? 50.65500 5.23500   -21.35900 1.000 101.77000 ? 368 LEU D CA  1 
ATOM   2502 C C   . LEU D 2 36  ? 50.41400 3.86900   -20.73400 1.000 98.86000  ? 368 LEU D C   1 
ATOM   2503 O O   . LEU D 2 36  ? 50.79300 3.63000   -19.58200 1.000 96.51000  ? 368 LEU D O   1 
ATOM   2504 C CB  . LEU D 2 36  ? 49.33700 5.99600   -21.50700 1.000 98.52000  ? 368 LEU D CB  1 
ATOM   2505 C CG  . LEU D 2 36  ? 48.64000 6.39000   -20.21400 1.000 92.50000  ? 368 LEU D CG  1 
ATOM   2506 C CD1 . LEU D 2 36  ? 49.67600 6.79000   -19.17600 1.000 97.88000  ? 368 LEU D CD1 1 
ATOM   2507 C CD2 . LEU D 2 36  ? 47.71200 7.53100   -20.48800 1.000 89.08000  ? 368 LEU D CD2 1 
ATOM   2508 N N   . TYR D 2 37  ? 49.81100 2.95700   -21.50600 1.000 94.90000  ? 369 TYR D N   1 
ATOM   2509 C CA  . TYR D 2 37  ? 49.56900 1.59400   -21.03900 1.000 97.91000  ? 369 TYR D CA  1 
ATOM   2510 C C   . TYR D 2 37  ? 50.81400 1.01100   -20.37800 1.000 103.58000 ? 369 TYR D C   1 
ATOM   2511 O O   . TYR D 2 37  ? 50.82700 0.74400   -19.16900 1.000 102.15000 ? 369 TYR D O   1 
ATOM   2512 C CB  . TYR D 2 37  ? 49.11000 0.70300   -22.20200 1.000 101.50000 ? 369 TYR D CB  1 
ATOM   2513 C CG  . TYR D 2 37  ? 48.63400 -0.68400  -21.77900 1.000 102.53000 ? 369 TYR D CG  1 
ATOM   2514 C CD1 . TYR D 2 37  ? 48.60200 -1.04200  -20.43700 1.000 101.22000 ? 369 TYR D CD1 1 
ATOM   2515 C CD2 . TYR D 2 37  ? 48.21200 -1.63500  -22.71500 1.000 107.12000 ? 369 TYR D CD2 1 
ATOM   2516 C CE1 . TYR D 2 37  ? 48.18100 -2.28800  -20.02200 1.000 100.64000 ? 369 TYR D CE1 1 
ATOM   2517 C CE2 . TYR D 2 37  ? 47.78300 -2.90000  -22.30200 1.000 107.00000 ? 369 TYR D CE2 1 
ATOM   2518 C CZ  . TYR D 2 37  ? 47.77700 -3.21200  -20.94500 1.000 101.61000 ? 369 TYR D CZ  1 
ATOM   2519 O OH  . TYR D 2 37  ? 47.35900 -4.43300  -20.46700 1.000 98.68000  ? 369 TYR D OH  1 
ATOM   2520 N N   . ASN D 2 38  ? 51.87700 0.81500   -21.14900 1.000 105.07000 ? 370 ASN D N   1 
ATOM   2521 C CA  . ASN D 2 38  ? 53.07800 0.19400   -20.61600 1.000 102.22000 ? 370 ASN D CA  1 
ATOM   2522 C C   . ASN D 2 38  ? 54.00900 1.21000   -19.92200 1.000 103.51000 ? 370 ASN D C   1 
ATOM   2523 O O   . ASN D 2 38  ? 55.21300 0.94700   -19.81000 1.000 102.27000 ? 370 ASN D O   1 
ATOM   2524 C CB  . ASN D 2 38  ? 53.79100 -0.57400  -21.74000 1.000 103.68000 ? 370 ASN D CB  1 
ATOM   2525 C CG  . ASN D 2 38  ? 52.79700 -1.26600  -22.74500 1.000 109.39000 ? 370 ASN D CG  1 
ATOM   2526 O OD1 . ASN D 2 38  ? 52.28900 -2.36900  -22.48700 1.000 112.96000 ? 370 ASN D OD1 1 
ATOM   2527 N ND2 . ASN D 2 38  ? 52.55500 -0.62100  -23.89600 1.000 100.68000 ? 370 ASN D ND2 1 
ATOM   2528 N N   . SER D 2 39  ? 53.47100 2.34800   -19.43300 1.000 101.45000 ? 371 SER D N   1 
ATOM   2529 C CA  . SER D 2 39  ? 54.26400 3.39100   -18.77400 1.000 100.97000 ? 371 SER D CA  1 
ATOM   2530 C C   . SER D 2 39  ? 54.32400 3.23700   -17.26000 1.000 104.01000 ? 371 SER D C   1 
ATOM   2531 O O   . SER D 2 39  ? 54.92100 4.08900   -16.58600 1.000 111.16000 ? 371 SER D O   1 
ATOM   2532 C CB  . SER D 2 39  ? 53.73600 4.79500   -19.11000 1.000 103.08000 ? 371 SER D CB  1 
ATOM   2533 O OG  . SER D 2 39  ? 52.53400 5.10500   -18.43200 1.000 102.24000 ? 371 SER D OG  1 
ATOM   2534 N N   . ALA D 2 40  ? 53.69500 2.19900   -16.71400 1.000 102.59000 ? 372 ALA D N   1 
ATOM   2535 C CA  . ALA D 2 40  ? 54.02400 1.68600   -15.39400 1.000 96.76000  ? 372 ALA D CA  1 
ATOM   2536 C C   . ALA D 2 40  ? 53.37700 0.31700   -15.29900 1.000 99.32000  ? 372 ALA D C   1 
ATOM   2537 O O   . ALA D 2 40  ? 53.23600 -0.38900  -16.30900 1.000 99.73000  ? 372 ALA D O   1 
ATOM   2538 C CB  . ALA D 2 40  ? 53.54400 2.61300   -14.28100 1.000 93.98000  ? 372 ALA D CB  1 
ATOM   2539 N N   . SER D 2 41  ? 52.97700 -0.06900  -14.09700 1.000 103.79000 ? 373 SER D N   1 
ATOM   2540 C CA  . SER D 2 41  ? 52.15000 -1.25400  -13.90400 1.000 107.07000 ? 373 SER D CA  1 
ATOM   2541 C C   . SER D 2 41  ? 50.88800 -0.81800  -13.17400 1.000 105.37000 ? 373 SER D C   1 
ATOM   2542 O O   . SER D 2 41  ? 50.94000 -0.41700  -12.00000 1.000 96.92000  ? 373 SER D O   1 
ATOM   2543 C CB  . SER D 2 41  ? 52.88900 -2.35300  -13.13500 1.000 107.86000 ? 373 SER D CB  1 
ATOM   2544 O OG  . SER D 2 41  ? 52.16000 -3.58700  -13.14500 1.000 102.90000 ? 373 SER D OG  1 
ATOM   2545 N N   . PHE D 2 42  ? 49.76900 -0.89900  -13.88000 1.000 100.58000 ? 374 PHE D N   1 
ATOM   2546 C CA  . PHE D 2 42  ? 48.47000 -0.56700  -13.33200 1.000 93.28000  ? 374 PHE D CA  1 
ATOM   2547 C C   . PHE D 2 42  ? 47.78000 -1.81600  -12.80100 1.000 91.81000  ? 374 PHE D C   1 
ATOM   2548 O O   . PHE D 2 42  ? 48.11600 -2.95000  -13.15300 1.000 95.46000  ? 374 PHE D O   1 
ATOM   2549 C CB  . PHE D 2 42  ? 47.63100 0.12400   -14.40200 1.000 85.52000  ? 374 PHE D CB  1 
ATOM   2550 C CG  . PHE D 2 42  ? 48.29700 1.32500   -14.95000 1.000 91.30000  ? 374 PHE D CG  1 
ATOM   2551 C CD1 . PHE D 2 42  ? 48.25800 2.51600   -14.25700 1.000 89.21000  ? 374 PHE D CD1 1 
ATOM   2552 C CD2 . PHE D 2 42  ? 49.04300 1.25200   -16.10700 1.000 92.20000  ? 374 PHE D CD2 1 
ATOM   2553 C CE1 . PHE D 2 42  ? 48.90000 3.63200   -14.74300 1.000 90.33000  ? 374 PHE D CE1 1 
ATOM   2554 C CE2 . PHE D 2 42  ? 49.69900 2.36400   -16.59100 1.000 91.11000  ? 374 PHE D CE2 1 
ATOM   2555 C CZ  . PHE D 2 42  ? 49.63200 3.55400   -15.90800 1.000 88.30000  ? 374 PHE D CZ  1 
ATOM   2556 N N   . SER D 2 43  ? 46.82500 -1.58800  -11.91000 1.000 87.61000  ? 375 SER D N   1 
ATOM   2557 C CA  . SER D 2 43  ? 45.94500 -2.62000  -11.39400 1.000 82.48000  ? 375 SER D CA  1 
ATOM   2558 C C   . SER D 2 43  ? 44.69800 -2.74200  -12.24800 1.000 81.37000  ? 375 SER D C   1 
ATOM   2559 O O   . SER D 2 43  ? 44.19900 -3.84800  -12.46700 1.000 83.60000  ? 375 SER D O   1 
ATOM   2560 C CB  . SER D 2 43  ? 45.56100 -2.29400  -9.94200  1.000 88.16000  ? 375 SER D CB  1 
ATOM   2561 O OG  . SER D 2 43  ? 46.70000 -1.88000  -9.16400  1.000 87.92000  ? 375 SER D OG  1 
ATOM   2562 N N   . THR D 2 44  ? 44.19200 -1.62400  -12.74600 1.000 82.39000  ? 376 THR D N   1 
ATOM   2563 C CA  . THR D 2 44  ? 42.97200 -1.60900  -13.53500 1.000 79.14000  ? 376 THR D CA  1 
ATOM   2564 C C   . THR D 2 44  ? 43.18200 -0.74100  -14.76100 1.000 85.69000  ? 376 THR D C   1 
ATOM   2565 O O   . THR D 2 44  ? 43.69700 0.37700   -14.66200 1.000 86.45000  ? 376 THR D O   1 
ATOM   2566 C CB  . THR D 2 44  ? 41.77700 -1.09900  -12.74200 1.000 79.48000  ? 376 THR D CB  1 
ATOM   2567 O OG1 . THR D 2 44  ? 41.40000 -2.09100  -11.78200 1.000 93.19000  ? 376 THR D OG1 1 
ATOM   2568 C CG2 . THR D 2 44  ? 40.59300 -0.83900  -13.65000 1.000 74.57000  ? 376 THR D CG2 1 
ATOM   2569 N N   . PHE D 2 45  ? 42.78800 -1.26300  -15.91200 1.000 87.46000  ? 377 PHE D N   1 
ATOM   2570 C CA  . PHE D 2 45  ? 42.82000 -0.49900  -17.14200 1.000 81.07000  ? 377 PHE D CA  1 
ATOM   2571 C C   . PHE D 2 45  ? 41.62200 -0.92500  -17.98000 1.000 83.24000  ? 377 PHE D C   1 
ATOM   2572 O O   . PHE D 2 45  ? 41.74800 -1.29500  -19.14600 1.000 90.75000  ? 377 PHE D O   1 
ATOM   2573 C CB  . PHE D 2 45  ? 44.14500 -0.71600  -17.87000 1.000 85.43000  ? 377 PHE D CB  1 
ATOM   2574 C CG  . PHE D 2 45  ? 44.64700 0.48200   -18.63700 1.000 87.52000  ? 377 PHE D CG  1 
ATOM   2575 C CD1 . PHE D 2 45  ? 43.97700 0.95200   -19.76100 1.000 89.06000  ? 377 PHE D CD1 1 
ATOM   2576 C CD2 . PHE D 2 45  ? 45.83700 1.10000   -18.26900 1.000 89.27000  ? 377 PHE D CD2 1 
ATOM   2577 C CE1 . PHE D 2 45  ? 44.46800 2.04000   -20.47900 1.000 88.77000  ? 377 PHE D CE1 1 
ATOM   2578 C CE2 . PHE D 2 45  ? 46.33400 2.19200   -18.98400 1.000 89.12000  ? 377 PHE D CE2 1 
ATOM   2579 C CZ  . PHE D 2 45  ? 45.64600 2.65600   -20.09200 1.000 90.84000  ? 377 PHE D CZ  1 
ATOM   2580 N N   . LYS D 2 46  ? 40.43800 -0.93800  -17.37000 1.000 80.10000  ? 378 LYS D N   1 
ATOM   2581 C CA  . LYS D 2 46  ? 39.23500 -1.16100  -18.15800 1.000 85.35000  ? 378 LYS D CA  1 
ATOM   2582 C C   . LYS D 2 46  ? 39.03100 0.00300   -19.11800 1.000 86.61000  ? 378 LYS D C   1 
ATOM   2583 O O   . LYS D 2 46  ? 39.20000 1.16800   -18.74500 1.000 86.83000  ? 378 LYS D O   1 
ATOM   2584 C CB  . LYS D 2 46  ? 37.99800 -1.31400  -17.27300 1.000 84.71000  ? 378 LYS D CB  1 
ATOM   2585 C CG  . LYS D 2 46  ? 38.08700 -2.38600  -16.19000 1.000 91.50000  ? 378 LYS D CG  1 
ATOM   2586 C CD  . LYS D 2 46  ? 36.68700 -2.80300  -15.68200 1.000 97.79000  ? 378 LYS D CD  1 
ATOM   2587 C CE  . LYS D 2 46  ? 36.63400 -2.99500  -14.16100 1.000 87.52000  ? 378 LYS D CE  1 
ATOM   2588 N NZ  . LYS D 2 46  ? 35.96700 -4.27000  -13.73500 1.000 77.36000  ? 378 LYS D NZ  1 
ATOM   2589 N N   . CYS D 2 47  ? 38.68500 -0.31800  -20.36600 1.000 89.21000  ? 379 CYS D N   1 
ATOM   2590 C CA  . CYS D 2 47  ? 38.16600 0.65200   -21.32000 1.000 83.84000  ? 379 CYS D CA  1 
ATOM   2591 C C   . CYS D 2 47  ? 36.73900 0.27900   -21.67500 1.000 87.70000  ? 379 CYS D C   1 
ATOM   2592 O O   . CYS D 2 47  ? 36.44600 -0.89800  -21.89200 1.000 92.13000  ? 379 CYS D O   1 
ATOM   2593 C CB  . CYS D 2 47  ? 39.01600 0.69700   -22.56400 1.000 87.05000  ? 379 CYS D CB  1 
ATOM   2594 S SG  . CYS D 2 47  ? 40.53800 1.55800   -22.28100 1.000 102.53000 ? 379 CYS D SG  1 
ATOM   2595 N N   . TYR D 2 48  ? 35.85600 1.27100   -21.70700 1.000 88.70000  ? 380 TYR D N   1 
ATOM   2596 C CA  . TYR D 2 48  ? 34.46300 1.08000   -22.08600 1.000 89.79000  ? 380 TYR D CA  1 
ATOM   2597 C C   . TYR D 2 48  ? 34.20300 1.82600   -23.38700 1.000 99.64000  ? 380 TYR D C   1 
ATOM   2598 O O   . TYR D 2 48  ? 34.61100 2.98400   -23.53900 1.000 100.97000 ? 380 TYR D O   1 
ATOM   2599 C CB  . TYR D 2 48  ? 33.51500 1.58000   -20.99400 1.000 91.18000  ? 380 TYR D CB  1 
ATOM   2600 C CG  . TYR D 2 48  ? 33.72000 0.94900   -19.61900 1.000 91.39000  ? 380 TYR D CG  1 
ATOM   2601 C CD1 . TYR D 2 48  ? 33.20900 -0.31100  -19.32600 1.000 94.83000  ? 380 TYR D CD1 1 
ATOM   2602 C CD2 . TYR D 2 48  ? 34.40300 1.61900   -18.61400 1.000 82.93000  ? 380 TYR D CD2 1 
ATOM   2603 C CE1 . TYR D 2 48  ? 33.38500 -0.89100  -18.07800 1.000 93.62000  ? 380 TYR D CE1 1 
ATOM   2604 C CE2 . TYR D 2 48  ? 34.58400 1.03900   -17.35800 1.000 92.89000  ? 380 TYR D CE2 1 
ATOM   2605 C CZ  . TYR D 2 48  ? 34.07200 -0.21700  -17.10400 1.000 92.95000  ? 380 TYR D CZ  1 
ATOM   2606 O OH  . TYR D 2 48  ? 34.22700 -0.80800  -15.87300 1.000 91.48000  ? 380 TYR D OH  1 
ATOM   2607 N N   . GLY D 2 49  ? 33.53500 1.15700   -24.32700 1.000 105.34000 ? 381 GLY D N   1 
ATOM   2608 C CA  . GLY D 2 49  ? 33.20100 1.72000   -25.62300 1.000 110.47000 ? 381 GLY D CA  1 
ATOM   2609 C C   . GLY D 2 49  ? 34.29100 1.61000   -26.67400 1.000 111.48000 ? 381 GLY D C   1 
ATOM   2610 O O   . GLY D 2 49  ? 33.98100 1.49700   -27.86400 1.000 111.63000 ? 381 GLY D O   1 
ATOM   2611 N N   . VAL D 2 50  ? 35.55700 1.63900   -26.26000 1.000 109.20000 ? 382 VAL D N   1 
ATOM   2612 C CA  . VAL D 2 50  ? 36.69700 1.67500   -27.16100 1.000 107.21000 ? 382 VAL D CA  1 
ATOM   2613 C C   . VAL D 2 50  ? 37.70700 0.64100   -26.68100 1.000 107.93000 ? 382 VAL D C   1 
ATOM   2614 O O   . VAL D 2 50  ? 37.60100 0.10200   -25.58100 1.000 106.21000 ? 382 VAL D O   1 
ATOM   2615 C CB  . VAL D 2 50  ? 37.34000 3.07800   -27.22400 1.000 108.17000 ? 382 VAL D CB  1 
ATOM   2616 C CG1 . VAL D 2 50  ? 36.37200 4.08400   -27.83100 1.000 98.76000  ? 382 VAL D CG1 1 
ATOM   2617 C CG2 . VAL D 2 50  ? 37.77000 3.52900   -25.81700 1.000 105.43000 ? 382 VAL D CG2 1 
ATOM   2618 N N   . SER D 2 51  ? 38.69500 0.37800   -27.51300 1.000 110.17000 ? 383 SER D N   1 
ATOM   2619 C CA  . SER D 2 51  ? 39.71500 -0.58000  -27.12200 1.000 110.83000 ? 383 SER D CA  1 
ATOM   2620 C C   . SER D 2 51  ? 41.07000 0.10800   -26.96700 1.000 110.70000 ? 383 SER D C   1 
ATOM   2621 O O   . SER D 2 51  ? 41.37900 1.05600   -27.69600 1.000 110.83000 ? 383 SER D O   1 
ATOM   2622 C CB  . SER D 2 51  ? 39.83300 -1.70500  -28.15600 1.000 113.36000 ? 383 SER D CB  1 
ATOM   2623 O OG  . SER D 2 51  ? 38.64400 -2.47500  -28.20600 1.000 124.97000 ? 383 SER D OG  1 
ATOM   2624 N N   . PRO D 2 52  ? 41.91200 -0.36300  -26.04300 1.000 113.65000 ? 384 PRO D N   1 
ATOM   2625 C CA  . PRO D 2 52  ? 43.17400 0.35200   -25.77500 1.000 113.66000 ? 384 PRO D CA  1 
ATOM   2626 C C   . PRO D 2 52  ? 44.20000 0.25500   -26.89400 1.000 110.53000 ? 384 PRO D C   1 
ATOM   2627 O O   . PRO D 2 52  ? 45.00600 1.18100   -27.05600 1.000 106.17000 ? 384 PRO D O   1 
ATOM   2628 C CB  . PRO D 2 52  ? 43.68700 -0.31700  -24.49400 1.000 111.11000 ? 384 PRO D CB  1 
ATOM   2629 C CG  . PRO D 2 52  ? 43.12600 -1.70800  -24.57100 1.000 114.95000 ? 384 PRO D CG  1 
ATOM   2630 C CD  . PRO D 2 52  ? 41.76800 -1.56900  -25.21300 1.000 112.19000 ? 384 PRO D CD  1 
ATOM   2631 N N   . THR D 2 53  ? 44.21900 -0.84200  -27.65600 1.000 114.81000 ? 385 THR D N   1 
ATOM   2632 C CA  . THR D 2 53  ? 45.14000 -0.92800  -28.78600 1.000 113.93000 ? 385 THR D CA  1 
ATOM   2633 C C   . THR D 2 53  ? 44.65200 -0.10500  -29.97000 1.000 108.91000 ? 385 THR D C   1 
ATOM   2634 O O   . THR D 2 53  ? 45.46200 0.34600   -30.78800 1.000 105.37000 ? 385 THR D O   1 
ATOM   2635 C CB  . THR D 2 53  ? 45.34700 -2.38700  -29.21300 1.000 115.65000 ? 385 THR D CB  1 
ATOM   2636 O OG1 . THR D 2 53  ? 46.29800 -2.43800  -30.28500 1.000 111.21000 ? 385 THR D OG1 1 
ATOM   2637 C CG2 . THR D 2 53  ? 44.03400 -3.01800  -29.68300 1.000 113.38000 ? 385 THR D CG2 1 
ATOM   2638 N N   . LYS D 2 54  ? 43.34200 0.10700   -30.06600 1.000 107.79000 ? 386 LYS D N   1 
ATOM   2639 C CA  . LYS D 2 54  ? 42.76900 0.95000   -31.10000 1.000 105.63000 ? 386 LYS D CA  1 
ATOM   2640 C C   . LYS D 2 54  ? 42.74400 2.41900   -30.71700 1.000 105.26000 ? 386 LYS D C   1 
ATOM   2641 O O   . LYS D 2 54  ? 42.42000 3.25700   -31.56500 1.000 102.68000 ? 386 LYS D O   1 
ATOM   2642 C CB  . LYS D 2 54  ? 41.35000 0.48700   -31.43700 1.000 105.74000 ? 386 LYS D CB  1 
ATOM   2643 C CG  . LYS D 2 54  ? 41.28800 -0.86700  -32.13800 1.000 106.55000 ? 386 LYS D CG  1 
ATOM   2644 C CD  . LYS D 2 54  ? 40.02100 -0.97600  -32.96400 1.000 108.97000 ? 386 LYS D CD  1 
ATOM   2645 C CE  . LYS D 2 54  ? 38.83000 -0.39100  -32.21600 1.000 106.70000 ? 386 LYS D CE  1 
ATOM   2646 N NZ  . LYS D 2 54  ? 37.65600 -0.13600  -33.09300 1.000 100.95000 ? 386 LYS D NZ  1 
ATOM   2647 N N   . LEU D 2 55  ? 43.08100 2.75100   -29.46800 1.000 106.36000 ? 387 LEU D N   1 
ATOM   2648 C CA  . LEU D 2 55  ? 43.14300 4.15300   -29.07600 1.000 102.69000 ? 387 LEU D CA  1 
ATOM   2649 C C   . LEU D 2 55  ? 44.25700 4.88200   -29.81500 1.000 102.35000 ? 387 LEU D C   1 
ATOM   2650 O O   . LEU D 2 55  ? 44.10600 6.05700   -30.16600 1.000 101.59000 ? 387 LEU D O   1 
ATOM   2651 C CB  . LEU D 2 55  ? 43.32800 4.27000   -27.56700 1.000 108.36000 ? 387 LEU D CB  1 
ATOM   2652 C CG  . LEU D 2 55  ? 42.12300 3.92500   -26.68800 1.000 106.25000 ? 387 LEU D CG  1 
ATOM   2653 C CD1 . LEU D 2 55  ? 42.53000 3.89900   -25.21600 1.000 100.83000 ? 387 LEU D CD1 1 
ATOM   2654 C CD2 . LEU D 2 55  ? 40.95600 4.88900   -26.92400 1.000 97.67000  ? 387 LEU D CD2 1 
ATOM   2655 N N   . ASN D 2 56  ? 45.37000 4.20100   -30.08300 1.000 102.03000 ? 388 ASN D N   1 
ATOM   2656 C CA  . ASN D 2 56  ? 46.41100 4.81700   -30.89700 1.000 103.41000 ? 388 ASN D CA  1 
ATOM   2657 C C   . ASN D 2 56  ? 46.01300 4.98200   -32.36700 1.000 100.28000 ? 388 ASN D C   1 
ATOM   2658 O O   . ASN D 2 56  ? 46.84000 5.44300   -33.16400 1.000 100.55000 ? 388 ASN D O   1 
ATOM   2659 C CB  . ASN D 2 56  ? 47.70800 4.02000   -30.77100 1.000 101.50000 ? 388 ASN D CB  1 
ATOM   2660 C CG  . ASN D 2 56  ? 48.64900 4.63900   -29.76100 1.000 103.49000 ? 388 ASN D CG  1 
ATOM   2661 O OD1 . ASN D 2 56  ? 48.52600 5.82300   -29.45100 1.000 101.84000 ? 388 ASN D OD1 1 
ATOM   2662 N ND2 . ASN D 2 56  ? 49.58400 3.85000   -29.23500 1.000 106.24000 ? 388 ASN D ND2 1 
ATOM   2663 N N   . ASP D 2 57  ? 44.77800 4.63600   -32.72900 1.000 97.39000  ? 389 ASP D N   1 
ATOM   2664 C CA  . ASP D 2 57  ? 44.21900 4.92100   -34.04400 1.000 99.48000  ? 389 ASP D CA  1 
ATOM   2665 C C   . ASP D 2 57  ? 43.27800 6.11700   -34.05300 1.000 100.48000 ? 389 ASP D C   1 
ATOM   2666 O O   . ASP D 2 57  ? 43.28200 6.88300   -35.02300 1.000 103.16000 ? 389 ASP D O   1 
ATOM   2667 C CB  . ASP D 2 57  ? 43.44600 3.70600   -34.58000 1.000 99.11000  ? 389 ASP D CB  1 
ATOM   2668 C CG  . ASP D 2 57  ? 44.34600 2.55200   -34.98200 1.000 97.63000  ? 389 ASP D CG  1 
ATOM   2669 O OD1 . ASP D 2 57  ? 45.57500 2.72200   -35.00300 1.000 99.70000  ? 389 ASP D OD1 1 
ATOM   2670 O OD2 . ASP D 2 57  ? 43.81200 1.46300   -35.27400 1.000 96.26000  ? 389 ASP D OD2 1 
ATOM   2671 N N   . LEU D 2 58  ? 42.46500 6.29400   -33.01200 1.000 98.98000  ? 390 LEU D N   1 
ATOM   2672 C CA  . LEU D 2 58  ? 41.28400 7.14300   -33.09300 1.000 90.48000  ? 390 LEU D CA  1 
ATOM   2673 C C   . LEU D 2 58  ? 41.61300 8.59900   -32.76200 1.000 85.99000  ? 390 LEU D C   1 
ATOM   2674 O O   . LEU D 2 58  ? 42.74800 8.95700   -32.43100 1.000 89.29000  ? 390 LEU D O   1 
ATOM   2675 C CB  . LEU D 2 58  ? 40.18300 6.61200   -32.17100 1.000 89.44000  ? 390 LEU D CB  1 
ATOM   2676 C CG  . LEU D 2 58  ? 39.72400 5.14700   -32.27500 1.000 92.62000  ? 390 LEU D CG  1 
ATOM   2677 C CD1 . LEU D 2 58  ? 39.19200 4.64000   -30.93500 1.000 95.12000  ? 390 LEU D CD1 1 
ATOM   2678 C CD2 . LEU D 2 58  ? 38.66400 4.98700   -33.32900 1.000 91.18000  ? 390 LEU D CD2 1 
ATOM   2679 N N   . CYS D 2 59  ? 40.58800 9.44900   -32.85200 1.000 82.68000  ? 391 CYS D N   1 
ATOM   2680 C CA  . CYS D 2 59  ? 40.70300 10.88800  -32.64200 1.000 83.46000  ? 391 CYS D CA  1 
ATOM   2681 C C   . CYS D 2 59  ? 39.44700 11.40300  -31.94600 1.000 80.61000  ? 391 CYS D C   1 
ATOM   2682 O O   . CYS D 2 59  ? 38.35600 10.85600  -32.12500 1.000 82.72000  ? 391 CYS D O   1 
ATOM   2683 C CB  . CYS D 2 59  ? 40.88700 11.65400  -33.97400 1.000 90.35000  ? 391 CYS D CB  1 
ATOM   2684 S SG  . CYS D 2 59  ? 42.44500 11.44000  -34.84100 1.000 87.46000  ? 391 CYS D SG  1 
ATOM   2685 N N   . PHE D 2 60  ? 39.59200 12.47000  -31.16300 1.000 76.23000  ? 392 PHE D N   1 
ATOM   2686 C CA  . PHE D 2 60  ? 38.47400 12.91200  -30.33700 1.000 76.02000  ? 392 PHE D CA  1 
ATOM   2687 C C   . PHE D 2 60  ? 38.53700 14.42500  -30.16900 1.000 81.33000  ? 392 PHE D C   1 
ATOM   2688 O O   . PHE D 2 60  ? 39.59700 15.03600  -30.31100 1.000 83.17000  ? 392 PHE D O   1 
ATOM   2689 C CB  . PHE D 2 60  ? 38.48700 12.21700  -28.96400 1.000 74.20000  ? 392 PHE D CB  1 
ATOM   2690 C CG  . PHE D 2 60  ? 38.36200 10.69600  -29.01500 1.000 70.47000  ? 392 PHE D CG  1 
ATOM   2691 C CD1 . PHE D 2 60  ? 37.12600 10.08600  -29.04800 1.000 68.68000  ? 392 PHE D CD1 1 
ATOM   2692 C CD2 . PHE D 2 60  ? 39.47800 9.89000   -28.96400 1.000 70.98000  ? 392 PHE D CD2 1 
ATOM   2693 C CE1 . PHE D 2 60  ? 37.00600 8.72000   -29.07400 1.000 66.27000  ? 392 PHE D CE1 1 
ATOM   2694 C CE2 . PHE D 2 60  ? 39.35600 8.51000   -28.98800 1.000 72.41000  ? 392 PHE D CE2 1 
ATOM   2695 C CZ  . PHE D 2 60  ? 38.11900 7.93300   -29.03800 1.000 71.46000  ? 392 PHE D CZ  1 
ATOM   2696 N N   . THR D 2 61  ? 37.38900 15.03500  -29.85900 1.000 77.26000  ? 393 THR D N   1 
ATOM   2697 C CA  . THR D 2 61  ? 37.36600 16.49400  -29.75700 1.000 80.14000  ? 393 THR D CA  1 
ATOM   2698 C C   . THR D 2 61  ? 38.19100 16.98000  -28.57200 1.000 84.81000  ? 393 THR D C   1 
ATOM   2699 O O   . THR D 2 61  ? 39.01800 17.89400  -28.70800 1.000 84.26000  ? 393 THR D O   1 
ATOM   2700 C CB  . THR D 2 61  ? 35.94000 17.01500  -29.63700 1.000 83.08000  ? 393 THR D CB  1 
ATOM   2701 O OG1 . THR D 2 61  ? 35.12500 16.49900  -30.69900 1.000 85.57000  ? 393 THR D OG1 1 
ATOM   2702 C CG2 . THR D 2 61  ? 35.95600 18.53900  -29.68000 1.000 84.52000  ? 393 THR D CG2 1 
ATOM   2703 N N   . ASN D 2 62  ? 37.93300 16.42100  -27.39000 1.000 85.18000  ? 394 ASN D N   1 
ATOM   2704 C CA  . ASN D 2 62  ? 38.79500 16.57300  -26.22600 1.000 80.60000  ? 394 ASN D CA  1 
ATOM   2705 C C   . ASN D 2 62  ? 38.79100 15.26200  -25.46600 1.000 79.48000  ? 394 ASN D C   1 
ATOM   2706 O O   . ASN D 2 62  ? 37.87800 14.44400  -25.59500 1.000 79.26000  ? 394 ASN D O   1 
ATOM   2707 C CB  . ASN D 2 62  ? 38.34800 17.69200  -25.29200 1.000 79.63000  ? 394 ASN D CB  1 
ATOM   2708 C CG  . ASN D 2 62  ? 38.08500 18.99400  -26.01100 1.000 87.78000  ? 394 ASN D CG  1 
ATOM   2709 O OD1 . ASN D 2 62  ? 38.98900 19.80200  -26.21100 1.000 85.95000  ? 394 ASN D OD1 1 
ATOM   2710 N ND2 . ASN D 2 62  ? 36.82500 19.22500  -26.37300 1.000 91.84000  ? 394 ASN D ND2 1 
ATOM   2711 N N   . VAL D 2 63  ? 39.83100 15.05600  -24.68100 1.000 79.74000  ? 395 VAL D N   1 
ATOM   2712 C CA  . VAL D 2 63  ? 39.82100 14.01200  -23.67200 1.000 80.74000  ? 395 VAL D CA  1 
ATOM   2713 C C   . VAL D 2 63  ? 39.79500 14.68200  -22.30900 1.000 80.44000  ? 395 VAL D C   1 
ATOM   2714 O O   . VAL D 2 63  ? 40.43800 15.72000  -22.10800 1.000 79.93000  ? 395 VAL D O   1 
ATOM   2715 C CB  . VAL D 2 63  ? 41.01800 13.06000  -23.82000 1.000 75.62000  ? 395 VAL D CB  1 
ATOM   2716 C CG1 . VAL D 2 63  ? 40.91600 11.93700  -22.78000 1.000 70.39000  ? 395 VAL D CG1 1 
ATOM   2717 C CG2 . VAL D 2 63  ? 41.00800 12.48800  -25.19500 1.000 67.67000  ? 395 VAL D CG2 1 
ATOM   2718 N N   . TYR D 2 64  ? 39.01000 14.12600  -21.39300 1.000 82.98000  ? 396 TYR D N   1 
ATOM   2719 C CA  . TYR D 2 64  ? 38.96000 14.60700  -20.01700 1.000 77.73000  ? 396 TYR D CA  1 
ATOM   2720 C C   . TYR D 2 64  ? 39.62900 13.59500  -19.10400 1.000 77.78000  ? 396 TYR D C   1 
ATOM   2721 O O   . TYR D 2 64  ? 39.36300 12.39200  -19.19400 1.000 76.65000  ? 396 TYR D O   1 
ATOM   2722 C CB  . TYR D 2 64  ? 37.52100 14.84500  -19.56300 1.000 76.95000  ? 396 TYR D CB  1 
ATOM   2723 C CG  . TYR D 2 64  ? 36.84700 15.93200  -20.33700 1.000 80.89000  ? 396 TYR D CG  1 
ATOM   2724 C CD1 . TYR D 2 64  ? 37.19700 17.25600  -20.14800 1.000 83.17000  ? 396 TYR D CD1 1 
ATOM   2725 C CD2 . TYR D 2 64  ? 35.87800 15.63500  -21.28700 1.000 86.65000  ? 396 TYR D CD2 1 
ATOM   2726 C CE1 . TYR D 2 64  ? 36.58400 18.25800  -20.87300 1.000 92.62000  ? 396 TYR D CE1 1 
ATOM   2727 C CE2 . TYR D 2 64  ? 35.25800 16.62500  -22.02000 1.000 85.73000  ? 396 TYR D CE2 1 
ATOM   2728 C CZ  . TYR D 2 64  ? 35.61300 17.93400  -21.81600 1.000 90.11000  ? 396 TYR D CZ  1 
ATOM   2729 O OH  . TYR D 2 64  ? 34.99500 18.93100  -22.54600 1.000 90.20000  ? 396 TYR D OH  1 
ATOM   2730 N N   . ALA D 2 65  ? 40.50100 14.08200  -18.23600 1.000 81.16000  ? 397 ALA D N   1 
ATOM   2731 C CA  . ALA D 2 65  ? 41.11200 13.26100  -17.20100 1.000 77.81000  ? 397 ALA D CA  1 
ATOM   2732 C C   . ALA D 2 65  ? 40.46500 13.61800  -15.87600 1.000 76.28000  ? 397 ALA D C   1 
ATOM   2733 O O   . ALA D 2 65  ? 40.63200 14.73400  -15.37700 1.000 77.79000  ? 397 ALA D O   1 
ATOM   2734 C CB  . ALA D 2 65  ? 42.61900 13.47300  -17.14200 1.000 82.53000  ? 397 ALA D CB  1 
ATOM   2735 N N   . ASP D 2 66  ? 39.71400 12.68100  -15.32500 1.000 80.74000  ? 398 ASP D N   1 
ATOM   2736 C CA  . ASP D 2 66  ? 39.23900 12.76500  -13.95300 1.000 77.09000  ? 398 ASP D CA  1 
ATOM   2737 C C   . ASP D 2 66  ? 40.15600 11.95500  -13.04900 1.000 72.61000  ? 398 ASP D C   1 
ATOM   2738 O O   . ASP D 2 66  ? 40.45500 10.79500  -13.34300 1.000 69.10000  ? 398 ASP D O   1 
ATOM   2739 C CB  . ASP D 2 66  ? 37.81000 12.25700  -13.86300 1.000 73.49000  ? 398 ASP D CB  1 
ATOM   2740 C CG  . ASP D 2 66  ? 36.87600 13.13600  -14.59600 1.000 73.47000  ? 398 ASP D CG  1 
ATOM   2741 O OD1 . ASP D 2 66  ? 37.26500 14.28300  -14.83800 1.000 78.27000  ? 398 ASP D OD1 1 
ATOM   2742 O OD2 . ASP D 2 66  ? 35.77600 12.69500  -14.93800 1.000 78.26000  ? 398 ASP D OD2 1 
ATOM   2743 N N   . SER D 2 67  ? 40.62500 12.57600  -11.96400 1.000 83.10000  ? 399 SER D N   1 
ATOM   2744 C CA  . SER D 2 67  ? 41.59100 11.94500  -11.07000 1.000 80.76000  ? 399 SER D CA  1 
ATOM   2745 C C   . SER D 2 67  ? 41.18000 12.13900  -9.62000  1.000 71.49000  ? 399 SER D C   1 
ATOM   2746 O O   . SER D 2 67  ? 40.75700 13.22800  -9.23000  1.000 74.86000  ? 399 SER D O   1 
ATOM   2747 C CB  . SER D 2 67  ? 42.99800 12.49300  -11.29300 1.000 76.38000  ? 399 SER D CB  1 
ATOM   2748 O OG  . SER D 2 67  ? 42.97800 13.90400  -11.35200 1.000 87.04000  ? 399 SER D OG  1 
ATOM   2749 N N   . PHE D 2 68  ? 41.31600 11.07400  -8.83200  1.000 75.92000  ? 400 PHE D N   1 
ATOM   2750 C CA  . PHE D 2 68  ? 40.99500 11.07400  -7.40600  1.000 78.57000  ? 400 PHE D CA  1 
ATOM   2751 C C   . PHE D 2 68  ? 41.60700 9.83000   -6.76300  1.000 79.90000  ? 400 PHE D C   1 
ATOM   2752 O O   . PHE D 2 68  ? 42.27300 9.03000   -7.42500  1.000 79.55000  ? 400 PHE D O   1 
ATOM   2753 C CB  . PHE D 2 68  ? 39.48300 11.11800  -7.17800  1.000 78.04000  ? 400 PHE D CB  1 
ATOM   2754 C CG  . PHE D 2 68  ? 38.73500 10.11700  -7.98300  1.000 76.19000  ? 400 PHE D CG  1 
ATOM   2755 C CD1 . PHE D 2 68  ? 38.52000 8.83900   -7.50200  1.000 74.13000  ? 400 PHE D CD1 1 
ATOM   2756 C CD2 . PHE D 2 68  ? 38.26700 10.44600  -9.25100  1.000 76.28000  ? 400 PHE D CD2 1 
ATOM   2757 C CE1 . PHE D 2 68  ? 37.82700 7.91300   -8.26700  1.000 73.40000  ? 400 PHE D CE1 1 
ATOM   2758 C CE2 . PHE D 2 68  ? 37.58100 9.53100   -10.01200 1.000 74.01000  ? 400 PHE D CE2 1 
ATOM   2759 C CZ  . PHE D 2 68  ? 37.36200 8.27000   -9.53300  1.000 78.95000  ? 400 PHE D CZ  1 
ATOM   2760 N N   . VAL D 2 69  ? 41.37200 9.66800   -5.45200  1.000 81.51000  ? 401 VAL D N   1 
ATOM   2761 C CA  . VAL D 2 69  ? 41.91000 8.55100   -4.67800  1.000 78.26000  ? 401 VAL D CA  1 
ATOM   2762 C C   . VAL D 2 69  ? 40.79500 7.90100   -3.86400  1.000 75.55000  ? 401 VAL D C   1 
ATOM   2763 O O   . VAL D 2 69  ? 39.91200 8.58500   -3.33700  1.000 77.27000  ? 401 VAL D O   1 
ATOM   2764 C CB  . VAL D 2 69  ? 43.06500 8.99900   -3.76500  1.000 81.97000  ? 401 VAL D CB  1 
ATOM   2765 C CG1 . VAL D 2 69  ? 43.31500 7.97700   -2.64300  1.000 81.75000  ? 401 VAL D CG1 1 
ATOM   2766 C CG2 . VAL D 2 69  ? 44.32900 9.20600   -4.58500  1.000 81.76000  ? 401 VAL D CG2 1 
ATOM   2767 N N   . ILE D 2 70  ? 40.81500 6.56500   -3.81500  1.000 77.53000  ? 402 ILE D N   1 
ATOM   2768 C CA  . ILE D 2 70  ? 39.94700 5.74100   -2.97700  1.000 84.12000  ? 402 ILE D CA  1 
ATOM   2769 C C   . ILE D 2 70  ? 40.71700 4.49600   -2.53900  1.000 81.31000  ? 402 ILE D C   1 
ATOM   2770 O O   . ILE D 2 70  ? 41.94500 4.42600   -2.66500  1.000 77.87000  ? 402 ILE D O   1 
ATOM   2771 C CB  . ILE D 2 70  ? 38.66100 5.34000   -3.72500  1.000 78.99000  ? 402 ILE D CB  1 
ATOM   2772 C CG1 . ILE D 2 70  ? 39.02500 4.68300   -5.05200  1.000 77.42000  ? 402 ILE D CG1 1 
ATOM   2773 C CG2 . ILE D 2 70  ? 37.72600 6.53000   -3.90900  1.000 75.88000  ? 402 ILE D CG2 1 
ATOM   2774 C CD1 . ILE D 2 70  ? 37.85000 4.02300   -5.76200  1.000 75.01000  ? 402 ILE D CD1 1 
ATOM   2775 N N   . ARG D 2 71  ? 40.00100 3.48300   -2.06700  1.000 82.71000  ? 403 ARG D N   1 
ATOM   2776 C CA  . ARG D 2 71  ? 40.61600 2.21100   -1.73400  1.000 83.02000  ? 403 ARG D CA  1 
ATOM   2777 C C   . ARG D 2 71  ? 40.33000 1.17500   -2.81400  1.000 81.44000  ? 403 ARG D C   1 
ATOM   2778 O O   . ARG D 2 71  ? 39.26200 1.17500   -3.43300  1.000 81.08000  ? 403 ARG D O   1 
ATOM   2779 C CB  . ARG D 2 71  ? 40.13200 1.70200   -0.36700  1.000 80.48000  ? 403 ARG D CB  1 
ATOM   2780 C CG  . ARG D 2 71  ? 38.74700 2.17700   0.02300   1.000 85.39000  ? 403 ARG D CG  1 
ATOM   2781 C CD  . ARG D 2 71  ? 38.43300 1.97700   1.51400   1.000 80.46000  ? 403 ARG D CD  1 
ATOM   2782 N NE  . ARG D 2 71  ? 37.82600 0.66800   1.76500   1.000 84.01000  ? 403 ARG D NE  1 
ATOM   2783 C CZ  . ARG D 2 71  ? 36.53500 0.46500   2.01800   1.000 82.63000  ? 403 ARG D CZ  1 
ATOM   2784 N NH1 . ARG D 2 71  ? 35.69400 1.48900   2.07800   1.000 85.43000  ? 403 ARG D NH1 1 
ATOM   2785 N NH2 . ARG D 2 71  ? 36.08700 -0.76500  2.22900   1.000 75.06000  ? 403 ARG D NH2 1 
ATOM   2786 N N   . GLY D 2 72  ? 41.30500 0.28800   -3.02800  1.000 76.40000  ? 404 GLY D N   1 
ATOM   2787 C CA  . GLY D 2 72  ? 41.13000 -0.80200  -3.97100  1.000 73.26000  ? 404 GLY D CA  1 
ATOM   2788 C C   . GLY D 2 72  ? 39.78400 -1.48600  -3.85900  1.000 76.12000  ? 404 GLY D C   1 
ATOM   2789 O O   . GLY D 2 72  ? 39.21100 -1.89600  -4.87600  1.000 85.37000  ? 404 GLY D O   1 
ATOM   2790 N N   . ASP D 2 73  ? 39.27500 -1.62600  -2.63100  1.000 80.67000  ? 405 ASP D N   1 
ATOM   2791 C CA  . ASP D 2 73  ? 37.90900 -2.08100  -2.36900  1.000 81.83000  ? 405 ASP D CA  1 
ATOM   2792 C C   . ASP D 2 73  ? 36.92400 -1.49100  -3.34000  1.000 76.58000  ? 405 ASP D C   1 
ATOM   2793 O O   . ASP D 2 73  ? 36.06300 -2.19200  -3.87600  1.000 77.13000  ? 405 ASP D O   1 
ATOM   2794 C CB  . ASP D 2 73  ? 37.45300 -1.63100  -0.96900  1.000 82.49000  ? 405 ASP D CB  1 
ATOM   2795 C CG  . ASP D 2 73  ? 37.72200 -2.63300  0.10500   1.000 89.50000  ? 405 ASP D CG  1 
ATOM   2796 O OD1 . ASP D 2 73  ? 37.67100 -3.85600  -0.14300  1.000 97.63000  ? 405 ASP D OD1 1 
ATOM   2797 O OD2 . ASP D 2 73  ? 37.97000 -2.16300  1.23100   1.000 91.50000  ? 405 ASP D OD2 1 
ATOM   2798 N N   . GLU D 2 74  ? 37.00000 -0.18000  -3.51900  1.000 78.36000  ? 406 GLU D N   1 
ATOM   2799 C CA  . GLU D 2 74  ? 35.97100 0.62300   -4.15100  1.000 85.25000  ? 406 GLU D CA  1 
ATOM   2800 C C   . GLU D 2 74  ? 36.23700 0.89900   -5.62900  1.000 78.77000  ? 406 GLU D C   1 
ATOM   2801 O O   . GLU D 2 74  ? 35.35400 1.42800   -6.30600  1.000 78.90000  ? 406 GLU D O   1 
ATOM   2802 C CB  . GLU D 2 74  ? 35.83100 1.94300   -3.38000  1.000 80.14000  ? 406 GLU D CB  1 
ATOM   2803 C CG  . GLU D 2 74  ? 35.34400 1.74400   -1.96200  1.000 81.66000  ? 406 GLU D CG  1 
ATOM   2804 C CD  . GLU D 2 74  ? 35.63200 2.92600   -1.05500  1.000 85.62000  ? 406 GLU D CD  1 
ATOM   2805 O OE1 . GLU D 2 74  ? 36.59800 3.68800   -1.32500  1.000 80.22000  ? 406 GLU D OE1 1 
ATOM   2806 O OE2 . GLU D 2 74  ? 34.87400 3.08300   -0.07300  1.000 77.14000  ? 406 GLU D OE2 1 
ATOM   2807 N N   . VAL D 2 75  ? 37.42700 0.56700   -6.12800  1.000 75.79000  ? 407 VAL D N   1 
ATOM   2808 C CA  . VAL D 2 75  ? 37.74900 0.76200   -7.53900  1.000 73.98000  ? 407 VAL D CA  1 
ATOM   2809 C C   . VAL D 2 75  ? 36.67700 0.14300   -8.42400  1.000 73.93000  ? 407 VAL D C   1 
ATOM   2810 O O   . VAL D 2 75  ? 36.20200 0.76500   -9.38300  1.000 76.82000  ? 407 VAL D O   1 
ATOM   2811 C CB  . VAL D 2 75  ? 39.13600 0.17100   -7.84500  1.000 71.97000  ? 407 VAL D CB  1 
ATOM   2812 C CG1 . VAL D 2 75  ? 39.34200 0.09200   -9.32500  1.000 68.14000  ? 407 VAL D CG1 1 
ATOM   2813 C CG2 . VAL D 2 75  ? 40.24900 0.98600   -7.13700  1.000 65.62000  ? 407 VAL D CG2 1 
ATOM   2814 N N   . ARG D 2 76  ? 36.22300 -1.04100  -8.04200  1.000 74.29000  ? 408 ARG D N   1 
ATOM   2815 C CA  . ARG D 2 76  ? 35.14900 -1.69500  -8.81600  1.000 70.78000  ? 408 ARG D CA  1 
ATOM   2816 C C   . ARG D 2 76  ? 33.98200 -0.72800  -8.96200  1.000 78.07000  ? 408 ARG D C   1 
ATOM   2817 O O   . ARG D 2 76  ? 33.26800 -0.82800  -9.96300  1.000 87.68000  ? 408 ARG D O   1 
ATOM   2818 C CB  . ARG D 2 76  ? 34.67400 -2.94800  -8.08500  1.000 82.13000  ? 408 ARG D CB  1 
ATOM   2819 C CG  . ARG D 2 76  ? 34.44500 -2.73800  -6.59600  1.000 81.34000  ? 408 ARG D CG  1 
ATOM   2820 C CD  . ARG D 2 76  ? 33.51100 -3.78400  -6.02500  1.000 87.20000  ? 408 ARG D CD  1 
ATOM   2821 N NE  . ARG D 2 76  ? 32.11700 -3.46100  -6.28200  1.000 96.14000  ? 408 ARG D NE  1 
ATOM   2822 C CZ  . ARG D 2 76  ? 31.30800 -2.88900  -5.40000  1.000 98.53000  ? 408 ARG D CZ  1 
ATOM   2823 N NH1 . ARG D 2 76  ? 31.76000 -2.57700  -4.19700  1.000 91.76000  ? 408 ARG D NH1 1 
ATOM   2824 N NH2 . ARG D 2 76  ? 30.05400 -2.63200  -5.72100  1.000 96.85000  ? 408 ARG D NH2 1 
ATOM   2825 N N   . GLN D 2 77  ? 33.78900 0.16300   -7.99400  1.000 84.91000  ? 409 GLN D N   1 
ATOM   2826 C CA  . GLN D 2 77  ? 32.61000 1.01100   -8.06500  1.000 84.29000  ? 409 GLN D CA  1 
ATOM   2827 C C   . GLN D 2 77  ? 32.75100 2.13400   -9.07300  1.000 81.49000  ? 409 GLN D C   1 
ATOM   2828 O O   . GLN D 2 77  ? 31.73900 2.76300   -9.40900  1.000 88.03000  ? 409 GLN D O   1 
ATOM   2829 C CB  . GLN D 2 77  ? 32.27300 1.59600   -6.70000  1.000 79.00000  ? 409 GLN D CB  1 
ATOM   2830 C CG  . GLN D 2 77  ? 31.84700 0.57000   -5.69600  1.000 79.98000  ? 409 GLN D CG  1 
ATOM   2831 C CD  . GLN D 2 77  ? 31.49800 1.21600   -4.39100  1.000 86.55000  ? 409 GLN D CD  1 
ATOM   2832 O OE1 . GLN D 2 77  ? 30.99700 2.32900   -4.36500  1.000 83.54000  ? 409 GLN D OE1 1 
ATOM   2833 N NE2 . GLN D 2 77  ? 31.80000 0.54300   -3.29300  1.000 87.90000  ? 409 GLN D NE2 1 
ATOM   2834 N N   . ILE D 2 78  ? 33.95600 2.40600   -9.57400  1.000 75.47000  ? 410 ILE D N   1 
ATOM   2835 C CA  . ILE D 2 78  ? 34.10900 3.34600   -10.69400 1.000 81.00000  ? 410 ILE D CA  1 
ATOM   2836 C C   . ILE D 2 78  ? 33.88200 2.54200   -11.96400 1.000 80.87000  ? 410 ILE D C   1 
ATOM   2837 O O   . ILE D 2 78  ? 34.81800 2.03000   -12.59000 1.000 75.14000  ? 410 ILE D O   1 
ATOM   2838 C CB  . ILE D 2 78  ? 35.46500 4.03500   -10.69000 1.000 80.00000  ? 410 ILE D CB  1 
ATOM   2839 C CG1 . ILE D 2 78  ? 35.79600 4.55200   -9.30800  1.000 75.29000  ? 410 ILE D CG1 1 
ATOM   2840 C CG2 . ILE D 2 78  ? 35.44700 5.19500   -11.65400 1.000 82.14000  ? 410 ILE D CG2 1 
ATOM   2841 C CD1 . ILE D 2 78  ? 34.92300 5.68500   -8.88600  1.000 76.41000  ? 410 ILE D CD1 1 
ATOM   2842 N N   . ALA D 2 79  ? 32.62700 2.44600   -12.37000 1.000 78.03000  ? 411 ALA D N   1 
ATOM   2843 C CA  . ALA D 2 79  ? 32.24300 1.54900   -13.44400 1.000 84.12000  ? 411 ALA D CA  1 
ATOM   2844 C C   . ALA D 2 79  ? 30.77900 1.78700   -13.77800 1.000 82.31000  ? 411 ALA D C   1 
ATOM   2845 O O   . ALA D 2 79  ? 29.99200 2.10900   -12.88500 1.000 89.54000  ? 411 ALA D O   1 
ATOM   2846 C CB  . ALA D 2 79  ? 32.48600 0.09100   -13.03900 1.000 80.65000  ? 411 ALA D CB  1 
ATOM   2847 N N   . PRO D 2 80  ? 30.37200 1.65000   -15.03400 1.000 88.62000  ? 412 PRO D N   1 
ATOM   2848 C CA  . PRO D 2 80  ? 28.98200 1.96200   -15.38700 1.000 93.23000  ? 412 PRO D CA  1 
ATOM   2849 C C   . PRO D 2 80  ? 27.98900 1.15100   -14.56700 1.000 93.21000  ? 412 PRO D C   1 
ATOM   2850 O O   . PRO D 2 80  ? 28.19100 -0.03400  -14.29500 1.000 88.46000  ? 412 PRO D O   1 
ATOM   2851 C CB  . PRO D 2 80  ? 28.90500 1.61500   -16.87700 1.000 88.57000  ? 412 PRO D CB  1 
ATOM   2852 C CG  . PRO D 2 80  ? 30.30600 1.77900   -17.35700 1.000 91.56000  ? 412 PRO D CG  1 
ATOM   2853 C CD  . PRO D 2 80  ? 31.18400 1.32500   -16.21700 1.000 90.62000  ? 412 PRO D CD  1 
ATOM   2854 N N   . GLY D 2 81  ? 26.91400 1.81600   -14.15300 1.000 97.21000  ? 413 GLY D N   1 
ATOM   2855 C CA  . GLY D 2 81  ? 25.81600 1.12100   -13.50600 1.000 99.06000  ? 413 GLY D CA  1 
ATOM   2856 C C   . GLY D 2 81  ? 26.14600 0.43900   -12.19400 1.000 103.00000 ? 413 GLY D C   1 
ATOM   2857 O O   . GLY D 2 81  ? 25.33700 -0.35800  -11.70600 1.000 105.85000 ? 413 GLY D O   1 
ATOM   2858 N N   . GLN D 2 82  ? 27.30800 0.72400   -11.60400 1.000 96.05000  ? 414 GLN D N   1 
ATOM   2859 C CA  . GLN D 2 82  ? 27.67000 0.13100   -10.32700 1.000 91.38000  ? 414 GLN D CA  1 
ATOM   2860 C C   . GLN D 2 82  ? 26.92100 0.81200   -9.19100  1.000 98.07000  ? 414 GLN D C   1 
ATOM   2861 O O   . GLN D 2 82  ? 26.43300 1.93800   -9.30900  1.000 99.37000  ? 414 GLN D O   1 
ATOM   2862 C CB  . GLN D 2 82  ? 29.17400 0.24200   -10.06800 1.000 91.74000  ? 414 GLN D CB  1 
ATOM   2863 C CG  . GLN D 2 82  ? 29.97100 -0.96000  -10.49100 1.000 91.70000  ? 414 GLN D CG  1 
ATOM   2864 C CD  . GLN D 2 82  ? 29.85600 -2.11100  -9.52500  1.000 95.04000  ? 414 GLN D CD  1 
ATOM   2865 O OE1 . GLN D 2 82  ? 29.96400 -1.93000  -8.31100  1.000 97.79000  ? 414 GLN D OE1 1 
ATOM   2866 N NE2 . GLN D 2 82  ? 29.65000 -3.31200  -10.05500 1.000 90.75000  ? 414 GLN D NE2 1 
ATOM   2867 N N   . THR D 2 83  ? 26.85000 0.11200   -8.07100  1.000 96.11000  ? 415 THR D N   1 
ATOM   2868 C CA  . THR D 2 83  ? 26.25700 0.64700   -6.86500  1.000 91.98000  ? 415 THR D CA  1 
ATOM   2869 C C   . THR D 2 83  ? 27.25300 0.47700   -5.73400  1.000 91.06000  ? 415 THR D C   1 
ATOM   2870 O O   . THR D 2 83  ? 28.01000 -0.50000  -5.69700  1.000 94.81000  ? 415 THR D O   1 
ATOM   2871 C CB  . THR D 2 83  ? 24.93100 -0.05000  -6.54500  1.000 94.99000  ? 415 THR D CB  1 
ATOM   2872 O OG1 . THR D 2 83  ? 25.16800 -1.44600  -6.31000  1.000 96.16000  ? 415 THR D OG1 1 
ATOM   2873 C CG2 . THR D 2 83  ? 23.96500 0.10300   -7.73400  1.000 92.69000  ? 415 THR D CG2 1 
ATOM   2874 N N   . GLY D 2 84  ? 27.26700 1.44400   -4.83700  1.000 82.62000  ? 416 GLY D N   1 
ATOM   2875 C CA  . GLY D 2 84  ? 28.19800 1.41500   -3.73500  1.000 79.06000  ? 416 GLY D CA  1 
ATOM   2876 C C   . GLY D 2 84  ? 28.37200 2.78900   -3.13700  1.000 85.67000  ? 416 GLY D C   1 
ATOM   2877 O O   . GLY D 2 84  ? 28.00000 3.80700   -3.72200  1.000 87.01000  ? 416 GLY D O   1 
ATOM   2878 N N   . LYS D 2 85  ? 28.96600 2.80400   -1.93900  1.000 83.16000  ? 417 LYS D N   1 
ATOM   2879 C CA  . LYS D 2 85  ? 29.20400 4.05000   -1.21400  1.000 81.37000  ? 417 LYS D CA  1 
ATOM   2880 C C   . LYS D 2 85  ? 29.92500 5.08100   -2.07900  1.000 80.46000  ? 417 LYS D C   1 
ATOM   2881 O O   . LYS D 2 85  ? 29.72200 6.29100   -1.91500  1.000 78.92000  ? 417 LYS D O   1 
ATOM   2882 C CB  . LYS D 2 85  ? 29.99800 3.74600   0.07100   1.000 75.66000  ? 417 LYS D CB  1 
ATOM   2883 C CG  . LYS D 2 85  ? 30.35400 4.94900   0.91600   1.000 69.78000  ? 417 LYS D CG  1 
ATOM   2884 C CD  . LYS D 2 85  ? 30.37100 4.61100   2.41800   1.000 79.92000  ? 417 LYS D CD  1 
ATOM   2885 C CE  . LYS D 2 85  ? 31.31100 3.46700   2.80600   1.000 70.49000  ? 417 LYS D CE  1 
ATOM   2886 N NZ  . LYS D 2 85  ? 32.76200 3.84700   2.75900   1.000 75.32000  ? 417 LYS D NZ  1 
ATOM   2887 N N   . ILE D 2 86  ? 30.75500 4.63100   -3.01200  1.000 80.87000  ? 418 ILE D N   1 
ATOM   2888 C CA  . ILE D 2 86  ? 31.48200 5.57800   -3.85200  1.000 85.15000  ? 418 ILE D CA  1 
ATOM   2889 C C   . ILE D 2 86  ? 30.65800 5.96200   -5.07100  1.000 81.61000  ? 418 ILE D C   1 
ATOM   2890 O O   . ILE D 2 86  ? 30.48200 7.14900   -5.36700  1.000 77.56000  ? 418 ILE D O   1 
ATOM   2891 C CB  . ILE D 2 86  ? 32.84900 5.00100   -4.24500  1.000 84.63000  ? 418 ILE D CB  1 
ATOM   2892 C CG1 . ILE D 2 86  ? 33.66500 4.74200   -2.98000  1.000 80.55000  ? 418 ILE D CG1 1 
ATOM   2893 C CG2 . ILE D 2 86  ? 33.56900 5.95200   -5.20700  1.000 77.32000  ? 418 ILE D CG2 1 
ATOM   2894 C CD1 . ILE D 2 86  ? 33.57800 5.85700   -1.96200  1.000 76.96000  ? 418 ILE D CD1 1 
ATOM   2895 N N   . ALA D 2 87  ? 30.12700 4.96100   -5.77500  1.000 81.56000  ? 419 ALA D N   1 
ATOM   2896 C CA  . ALA D 2 87  ? 29.23500 5.23600   -6.89400  1.000 82.43000  ? 419 ALA D CA  1 
ATOM   2897 C C   . ALA D 2 87  ? 28.04600 6.08900   -6.46800  1.000 85.09000  ? 419 ALA D C   1 
ATOM   2898 O O   . ALA D 2 87  ? 27.63800 7.00100   -7.19500  1.000 84.79000  ? 419 ALA D O   1 
ATOM   2899 C CB  . ALA D 2 87  ? 28.75900 3.92500   -7.52000  1.000 85.26000  ? 419 ALA D CB  1 
ATOM   2900 N N   . ASP D 2 88  ? 27.48700 5.83300   -5.28600  1.000 81.82000  ? 420 ASP D N   1 
ATOM   2901 C CA  . ASP D 2 88  ? 26.22700 6.49200   -4.96900  1.000 83.32000  ? 420 ASP D CA  1 
ATOM   2902 C C   . ASP D 2 88  ? 26.39300 7.92200   -4.46900  1.000 83.24000  ? 420 ASP D C   1 
ATOM   2903 O O   . ASP D 2 88  ? 25.49400 8.74200   -4.67400  1.000 87.52000  ? 420 ASP D O   1 
ATOM   2904 C CB  . ASP D 2 88  ? 25.45200 5.69400   -3.92900  1.000 88.79000  ? 420 ASP D CB  1 
ATOM   2905 C CG  . ASP D 2 88  ? 25.08200 4.31900   -4.41200  1.000 93.61000  ? 420 ASP D CG  1 
ATOM   2906 O OD1 . ASP D 2 88  ? 25.38300 4.01000   -5.59200  1.000 94.32000  ? 420 ASP D OD1 1 
ATOM   2907 O OD2 . ASP D 2 88  ? 24.50900 3.54900   -3.60100  1.000 92.82000  ? 420 ASP D OD2 1 
ATOM   2908 N N   . TYR D 2 89  ? 27.49300 8.24600   -3.79300  1.000 77.51000  ? 421 TYR D N   1 
ATOM   2909 C CA  . TYR D 2 89  ? 27.59900 9.55100   -3.15400  1.000 82.17000  ? 421 TYR D CA  1 
ATOM   2910 C C   . TYR D 2 89  ? 28.86300 10.31300  -3.52200  1.000 77.35000  ? 421 TYR D C   1 
ATOM   2911 O O   . TYR D 2 89  ? 29.04300 11.43900  -3.05300  1.000 87.60000  ? 421 TYR D O   1 
ATOM   2912 C CB  . TYR D 2 89  ? 27.53900 9.42300   -1.61100  1.000 85.82000  ? 421 TYR D CB  1 
ATOM   2913 C CG  . TYR D 2 89  ? 26.34400 8.67300   -1.01100  1.000 84.99000  ? 421 TYR D CG  1 
ATOM   2914 C CD1 . TYR D 2 89  ? 25.06900 8.78200   -1.55400  1.000 89.70000  ? 421 TYR D CD1 1 
ATOM   2915 C CD2 . TYR D 2 89  ? 26.50100 7.86800   0.12000   1.000 89.33000  ? 421 TYR D CD2 1 
ATOM   2916 C CE1 . TYR D 2 89  ? 23.98400 8.10600   -0.99700  1.000 89.18000  ? 421 TYR D CE1 1 
ATOM   2917 C CE2 . TYR D 2 89  ? 25.41600 7.18600   0.68400   1.000 88.95000  ? 421 TYR D CE2 1 
ATOM   2918 C CZ  . TYR D 2 89  ? 24.16800 7.31500   0.11600   1.000 89.74000  ? 421 TYR D CZ  1 
ATOM   2919 O OH  . TYR D 2 89  ? 23.10200 6.65600   0.65800   1.000 87.27000  ? 421 TYR D OH  1 
ATOM   2920 N N   . ASN D 2 90  ? 29.74100 9.75300   -4.33900  1.000 75.68000  ? 422 ASN D N   1 
ATOM   2921 C CA  . ASN D 2 90  ? 31.02500 10.40200  -4.57300  1.000 76.52000  ? 422 ASN D CA  1 
ATOM   2922 C C   . ASN D 2 90  ? 31.31900 10.67600  -6.03900  1.000 79.82000  ? 422 ASN D C   1 
ATOM   2923 O O   . ASN D 2 90  ? 31.61400 11.82500  -6.39900  1.000 79.67000  ? 422 ASN D O   1 
ATOM   2924 C CB  . ASN D 2 90  ? 32.12100 9.54400   -3.96000  1.000 77.70000  ? 422 ASN D CB  1 
ATOM   2925 C CG  . ASN D 2 90  ? 32.00100 9.46800   -2.47000  1.000 81.58000  ? 422 ASN D CG  1 
ATOM   2926 O OD1 . ASN D 2 90  ? 32.60600 10.26800  -1.75600  1.000 81.74000  ? 422 ASN D OD1 1 
ATOM   2927 N ND2 . ASN D 2 90  ? 31.20200 8.51400   -1.98200  1.000 74.73000  ? 422 ASN D ND2 1 
ATOM   2928 N N   . TYR D 2 91  ? 31.24500 9.65900   -6.89600  1.000 72.16000  ? 423 TYR D N   1 
ATOM   2929 C CA  . TYR D 2 91  ? 31.62800 9.78200   -8.29300  1.000 71.02000  ? 423 TYR D CA  1 
ATOM   2930 C C   . TYR D 2 91  ? 30.94600 8.67500   -9.07000  1.000 78.23000  ? 423 TYR D C   1 
ATOM   2931 O O   . TYR D 2 91  ? 31.11400 7.50000   -8.73000  1.000 80.19000  ? 423 TYR D O   1 
ATOM   2932 C CB  . TYR D 2 91  ? 33.13300 9.68500   -8.46400  1.000 77.52000  ? 423 TYR D CB  1 
ATOM   2933 C CG  . TYR D 2 91  ? 33.56500 9.78700   -9.91900  1.000 79.86000  ? 423 TYR D CG  1 
ATOM   2934 C CD1 . TYR D 2 91  ? 33.62500 8.65500   -10.73100 1.000 81.63000  ? 423 TYR D CD1 1 
ATOM   2935 C CD2 . TYR D 2 91  ? 33.92100 11.01200  -10.47700 1.000 75.86000  ? 423 TYR D CD2 1 
ATOM   2936 C CE1 . TYR D 2 91  ? 34.02100 8.74300   -12.05400 1.000 83.48000  ? 423 TYR D CE1 1 
ATOM   2937 C CE2 . TYR D 2 91  ? 34.32600 11.10300  -11.78600 1.000 77.51000  ? 423 TYR D CE2 1 
ATOM   2938 C CZ  . TYR D 2 91  ? 34.36900 9.96800   -12.57100 1.000 82.88000  ? 423 TYR D CZ  1 
ATOM   2939 O OH  . TYR D 2 91  ? 34.77100 10.06200  -13.87700 1.000 80.25000  ? 423 TYR D OH  1 
ATOM   2940 N N   . LYS D 2 92  ? 30.22500 9.04000   -10.13600 1.000 76.05000  ? 424 LYS D N   1 
ATOM   2941 C CA  . LYS D 2 92  ? 29.27400 8.12800   -10.76400 1.000 78.01000  ? 424 LYS D CA  1 
ATOM   2942 C C   . LYS D 2 92  ? 29.40900 8.15400   -12.28100 1.000 87.14000  ? 424 LYS D C   1 
ATOM   2943 O O   . LYS D 2 92  ? 29.13600 9.17400   -12.91700 1.000 87.90000  ? 424 LYS D O   1 
ATOM   2944 C CB  . LYS D 2 92  ? 27.84100 8.48700   -10.34400 1.000 81.96000  ? 424 LYS D CB  1 
ATOM   2945 C CG  . LYS D 2 92  ? 26.77500 7.58700   -10.94600 1.000 85.52000  ? 424 LYS D CG  1 
ATOM   2946 C CD  . LYS D 2 92  ? 26.91700 6.15700   -10.46100 1.000 89.06000  ? 424 LYS D CD  1 
ATOM   2947 C CE  . LYS D 2 92  ? 26.02200 5.20900   -11.25600 1.000 94.23000  ? 424 LYS D CE  1 
ATOM   2948 N NZ  . LYS D 2 92  ? 25.98300 3.82600   -10.69100 1.000 92.97000  ? 424 LYS D NZ  1 
ATOM   2949 N N   . LEU D 2 93  ? 29.78700 7.02600   -12.85600 1.000 82.88000  ? 425 LEU D N   1 
ATOM   2950 C CA  . LEU D 2 93  ? 29.80800 6.85900   -14.29900 1.000 87.55000  ? 425 LEU D CA  1 
ATOM   2951 C C   . LEU D 2 93  ? 28.40600 6.54800   -14.81900 1.000 94.27000  ? 425 LEU D C   1 
ATOM   2952 O O   . LEU D 2 93  ? 27.68000 5.75200   -14.21500 1.000 97.44000  ? 425 LEU D O   1 
ATOM   2953 C CB  . LEU D 2 93  ? 30.75100 5.73400   -14.69500 1.000 85.41000  ? 425 LEU D CB  1 
ATOM   2954 C CG  . LEU D 2 93  ? 32.20200 5.94300   -14.28100 1.000 87.56000  ? 425 LEU D CG  1 
ATOM   2955 C CD1 . LEU D 2 93  ? 33.05500 4.78700   -14.74100 1.000 84.37000  ? 425 LEU D CD1 1 
ATOM   2956 C CD2 . LEU D 2 93  ? 32.72200 7.24200   -14.85200 1.000 88.21000  ? 425 LEU D CD2 1 
ATOM   2957 N N   . PRO D 2 94  ? 28.00600 7.14300   -15.93800 1.000 92.55000  ? 426 PRO D N   1 
ATOM   2958 C CA  . PRO D 2 94  ? 26.73500 6.76500   -16.55300 1.000 93.56000  ? 426 PRO D CA  1 
ATOM   2959 C C   . PRO D 2 94  ? 26.80400 5.34500   -17.08100 1.000 99.63000  ? 426 PRO D C   1 
ATOM   2960 O O   . PRO D 2 94  ? 27.87200 4.73900   -17.19800 1.000 98.37000  ? 426 PRO D O   1 
ATOM   2961 C CB  . PRO D 2 94  ? 26.56600 7.77500   -17.69300 1.000 96.67000  ? 426 PRO D CB  1 
ATOM   2962 C CG  . PRO D 2 94  ? 27.95200 8.20900   -18.00100 1.000 93.97000  ? 426 PRO D CG  1 
ATOM   2963 C CD  . PRO D 2 94  ? 28.71400 8.17200   -16.71700 1.000 88.45000  ? 426 PRO D CD  1 
ATOM   2964 N N   . ASP D 2 95  ? 25.62300 4.82100   -17.40900 1.000 102.75000 ? 427 ASP D N   1 
ATOM   2965 C CA  . ASP D 2 95  ? 25.53700 3.49100   -17.99800 1.000 99.97000  ? 427 ASP D CA  1 
ATOM   2966 C C   . ASP D 2 95  ? 26.17200 3.45300   -19.37900 1.000 96.34000  ? 427 ASP D C   1 
ATOM   2967 O O   . ASP D 2 95  ? 26.84500 2.47400   -19.72800 1.000 93.22000  ? 427 ASP D O   1 
ATOM   2968 C CB  . ASP D 2 95  ? 24.07500 3.06300   -18.06100 1.000 102.30000 ? 427 ASP D CB  1 
ATOM   2969 C CG  . ASP D 2 95  ? 23.32200 3.40500   -16.78500 1.000 105.18000 ? 427 ASP D CG  1 
ATOM   2970 O OD1 . ASP D 2 95  ? 23.97900 3.51000   -15.71600 1.000 101.07000 ? 427 ASP D OD1 1 
ATOM   2971 O OD2 . ASP D 2 95  ? 22.08500 3.57700   -16.85600 1.000 105.71000 ? 427 ASP D OD2 1 
ATOM   2972 N N   . ASP D 2 96  ? 25.98300 4.50900   -20.16700 1.000 98.65000  ? 428 ASP D N   1 
ATOM   2973 C CA  . ASP D 2 96  ? 26.53700 4.59500   -21.51200 1.000 98.76000  ? 428 ASP D CA  1 
ATOM   2974 C C   . ASP D 2 96  ? 27.95200 5.16700   -21.52900 1.000 100.27000 ? 428 ASP D C   1 
ATOM   2975 O O   . ASP D 2 96  ? 28.32400 5.85600   -22.49100 1.000 102.76000 ? 428 ASP D O   1 
ATOM   2976 C CB  . ASP D 2 96  ? 25.61400 5.43000   -22.40400 1.000 97.83000  ? 428 ASP D CB  1 
ATOM   2977 C CG  . ASP D 2 96  ? 25.72400 6.92700   -22.13100 1.000 104.72000 ? 428 ASP D CG  1 
ATOM   2978 O OD1 . ASP D 2 96  ? 25.90500 7.30900   -20.95600 1.000 106.78000 ? 428 ASP D OD1 1 
ATOM   2979 O OD2 . ASP D 2 96  ? 25.65500 7.71900   -23.10000 1.000 108.32000 ? 428 ASP D OD2 1 
ATOM   2980 N N   . PHE D 2 97  ? 28.75500 4.90600   -20.49900 1.000 94.53000  ? 429 PHE D N   1 
ATOM   2981 C CA  . PHE D 2 97  ? 30.06300 5.54900   -20.40900 1.000 97.79000  ? 429 PHE D CA  1 
ATOM   2982 C C   . PHE D 2 97  ? 31.03000 4.96500   -21.43400 1.000 96.03000  ? 429 PHE D C   1 
ATOM   2983 O O   . PHE D 2 97  ? 31.21300 3.74500   -21.50500 1.000 96.50000  ? 429 PHE D O   1 
ATOM   2984 C CB  . PHE D 2 97  ? 30.64800 5.41200   -18.99600 1.000 90.13000  ? 429 PHE D CB  1 
ATOM   2985 C CG  . PHE D 2 97  ? 32.10600 5.80500   -18.90200 1.000 81.72000  ? 429 PHE D CG  1 
ATOM   2986 C CD1 . PHE D 2 97  ? 32.49700 7.12400   -19.07300 1.000 83.97000  ? 429 PHE D CD1 1 
ATOM   2987 C CD2 . PHE D 2 97  ? 33.07900 4.85400   -18.65200 1.000 81.14000  ? 429 PHE D CD2 1 
ATOM   2988 C CE1 . PHE D 2 97  ? 33.83600 7.48800   -18.99600 1.000 82.11000  ? 429 PHE D CE1 1 
ATOM   2989 C CE2 . PHE D 2 97  ? 34.41800 5.20900   -18.57800 1.000 79.03000  ? 429 PHE D CE2 1 
ATOM   2990 C CZ  . PHE D 2 97  ? 34.79500 6.53000   -18.75000 1.000 79.41000  ? 429 PHE D CZ  1 
ATOM   2991 N N   . THR D 2 98  ? 31.66400 5.84600   -22.21800 1.000 91.52000  ? 430 THR D N   1 
ATOM   2992 C CA  . THR D 2 98  ? 32.73300 5.46900   -23.14100 1.000 96.52000  ? 430 THR D CA  1 
ATOM   2993 C C   . THR D 2 98  ? 34.03500 6.12900   -22.68100 1.000 94.04000  ? 430 THR D C   1 
ATOM   2994 O O   . THR D 2 98  ? 34.18400 7.35800   -22.74300 1.000 91.20000  ? 430 THR D O   1 
ATOM   2995 C CB  . THR D 2 98  ? 32.40200 5.85200   -24.59100 1.000 99.29000  ? 430 THR D CB  1 
ATOM   2996 O OG1 . THR D 2 98  ? 32.22100 7.27300   -24.70300 1.000 101.50000 ? 430 THR D OG1 1 
ATOM   2997 C CG2 . THR D 2 98  ? 31.14200 5.14600   -25.06200 1.000 97.72000  ? 430 THR D CG2 1 
ATOM   2998 N N   . GLY D 2 99  ? 34.97900 5.30800   -22.24400 1.000 88.97000  ? 431 GLY D N   1 
ATOM   2999 C CA  . GLY D 2 99  ? 36.24100 5.82500   -21.76400 1.000 84.56000  ? 431 GLY D CA  1 
ATOM   3000 C C   . GLY D 2 99  ? 37.03500 4.72400   -21.11300 1.000 80.09000  ? 431 GLY D C   1 
ATOM   3001 O O   . GLY D 2 99  ? 36.73200 3.54100   -21.26700 1.000 81.47000  ? 431 GLY D O   1 
ATOM   3002 N N   . CYS D 2 100 ? 38.06800 5.12200   -20.38700 1.000 73.40000  ? 432 CYS D N   1 
ATOM   3003 C CA  . CYS D 2 100 ? 38.94700 4.15600   -19.74600 1.000 79.64000  ? 432 CYS D CA  1 
ATOM   3004 C C   . CYS D 2 100 ? 39.19700 4.54300   -18.29200 1.000 78.73000  ? 432 CYS D C   1 
ATOM   3005 O O   . CYS D 2 100 ? 39.49400 5.70700   -17.99000 1.000 75.98000  ? 432 CYS D O   1 
ATOM   3006 C CB  . CYS D 2 100 ? 40.26000 4.04500   -20.51300 1.000 80.70000  ? 432 CYS D CB  1 
ATOM   3007 S SG  . CYS D 2 100 ? 40.03100 3.52900   -22.22700 1.000 95.99000  ? 432 CYS D SG  1 
ATOM   3008 N N   . VAL D 2 101 ? 39.06400 3.56600   -17.39300 1.000 77.82000  ? 433 VAL D N   1 
ATOM   3009 C CA  . VAL D 2 101 ? 39.36300 3.75600   -15.98100 1.000 78.56000  ? 433 VAL D CA  1 
ATOM   3010 C C   . VAL D 2 101 ? 40.73200 3.15300   -15.72300 1.000 77.04000  ? 433 VAL D C   1 
ATOM   3011 O O   . VAL D 2 101 ? 41.03700 2.06900   -16.22700 1.000 79.59000  ? 433 VAL D O   1 
ATOM   3012 C CB  . VAL D 2 101 ? 38.27900 3.11700   -15.08800 1.000 78.77000  ? 433 VAL D CB  1 
ATOM   3013 C CG1 . VAL D 2 101 ? 38.60500 3.31200   -13.59300 1.000 72.06000  ? 433 VAL D CG1 1 
ATOM   3014 C CG2 . VAL D 2 101 ? 36.90600 3.68900   -15.42200 1.000 75.82000  ? 433 VAL D CG2 1 
ATOM   3015 N N   . ILE D 2 102 ? 41.57000 3.85800   -14.95700 1.000 77.18000  ? 434 ILE D N   1 
ATOM   3016 C CA  . ILE D 2 102 ? 42.94300 3.43500   -14.68300 1.000 80.48000  ? 434 ILE D CA  1 
ATOM   3017 C C   . ILE D 2 102 ? 43.22800 3.60400   -13.19800 1.000 75.99000  ? 434 ILE D C   1 
ATOM   3018 O O   . ILE D 2 102 ? 42.91700 4.65000   -12.62100 1.000 74.39000  ? 434 ILE D O   1 
ATOM   3019 C CB  . ILE D 2 102 ? 43.96500 4.23900   -15.50700 1.000 75.32000  ? 434 ILE D CB  1 
ATOM   3020 C CG1 . ILE D 2 102 ? 43.74400 4.00400   -16.99200 1.000 82.68000  ? 434 ILE D CG1 1 
ATOM   3021 C CG2 . ILE D 2 102 ? 45.36500 3.84500   -15.14100 1.000 80.75000  ? 434 ILE D CG2 1 
ATOM   3022 C CD1 . ILE D 2 102 ? 44.14300 5.18300   -17.85400 1.000 88.97000  ? 434 ILE D CD1 1 
ATOM   3023 N N   . ALA D 2 103 ? 43.84200 2.59400   -12.58900 1.000 72.60000  ? 435 ALA D N   1 
ATOM   3024 C CA  . ALA D 2 103 ? 44.08300 2.60800   -11.15200 1.000 86.61000  ? 435 ALA D CA  1 
ATOM   3025 C C   . ALA D 2 103 ? 45.36900 1.87100   -10.82700 1.000 86.85000  ? 435 ALA D C   1 
ATOM   3026 O O   . ALA D 2 103 ? 45.74500 0.92300   -11.51600 1.000 90.02000  ? 435 ALA D O   1 
ATOM   3027 C CB  . ALA D 2 103 ? 42.93500 1.96300   -10.36600 1.000 85.54000  ? 435 ALA D CB  1 
ATOM   3028 N N   . TRP D 2 104 ? 46.02600 2.30200   -9.75300  1.000 82.99000  ? 436 TRP D N   1 
ATOM   3029 C CA  . TRP D 2 104 ? 47.25400 1.66400   -9.31100  1.000 81.44000  ? 436 TRP D CA  1 
ATOM   3030 C C   . TRP D 2 104 ? 47.47700 1.95400   -7.82900  1.000 89.32000  ? 436 TRP D C   1 
ATOM   3031 O O   . TRP D 2 104 ? 47.20300 3.06400   -7.35500  1.000 90.67000  ? 436 TRP D O   1 
ATOM   3032 C CB  . TRP D 2 104 ? 48.44500 2.13700   -10.15300 1.000 87.16000  ? 436 TRP D CB  1 
ATOM   3033 C CG  . TRP D 2 104 ? 48.87500 3.57300   -9.93500  1.000 86.56000  ? 436 TRP D CG  1 
ATOM   3034 C CD1 . TRP D 2 104 ? 49.84300 4.00700   -9.08700  1.000 85.98000  ? 436 TRP D CD1 1 
ATOM   3035 C CD2 . TRP D 2 104 ? 48.37800 4.74400   -10.60700 1.000 83.51000  ? 436 TRP D CD2 1 
ATOM   3036 N NE1 . TRP D 2 104 ? 49.98300 5.37200   -9.18000  1.000 87.57000  ? 436 TRP D NE1 1 
ATOM   3037 C CE2 . TRP D 2 104 ? 49.09400 5.85000   -10.10200 1.000 79.78000  ? 436 TRP D CE2 1 
ATOM   3038 C CE3 . TRP D 2 104 ? 47.39900 4.96200   -11.57900 1.000 82.59000  ? 436 TRP D CE3 1 
ATOM   3039 C CZ2 . TRP D 2 104 ? 48.85500 7.14800   -10.51700 1.000 81.13000  ? 436 TRP D CZ2 1 
ATOM   3040 C CZ3 . TRP D 2 104 ? 47.16900 6.25700   -12.00300 1.000 83.86000  ? 436 TRP D CZ3 1 
ATOM   3041 C CH2 . TRP D 2 104 ? 47.89600 7.33600   -11.47100 1.000 85.12000  ? 436 TRP D CH2 1 
ATOM   3042 N N   . ASN D 2 105 ? 47.97200 0.94700   -7.10900  1.000 83.33000  ? 437 ASN D N   1 
ATOM   3043 C CA  . ASN D 2 105 ? 48.20400 1.06300   -5.68000  1.000 81.18000  ? 437 ASN D CA  1 
ATOM   3044 C C   . ASN D 2 105 ? 49.15200 2.21800   -5.38100  1.000 82.61000  ? 437 ASN D C   1 
ATOM   3045 O O   . ASN D 2 105 ? 50.28100 2.25000   -5.88300  1.000 86.93000  ? 437 ASN D O   1 
ATOM   3046 C CB  . ASN D 2 105 ? 48.77700 -0.25100  -5.15500  1.000 83.95000  ? 437 ASN D CB  1 
ATOM   3047 C CG  . ASN D 2 105 ? 48.84800 -0.29400  -3.64200  1.000 85.09000  ? 437 ASN D CG  1 
ATOM   3048 O OD1 . ASN D 2 105 ? 49.65800 0.39800   -3.02400  1.000 82.86000  ? 437 ASN D OD1 1 
ATOM   3049 N ND2 . ASN D 2 105 ? 47.99800 -1.11000  -3.04000  1.000 87.42000  ? 437 ASN D ND2 1 
ATOM   3050 N N   . SER D 2 106 ? 48.68600 3.17400   -4.57100  1.000 82.55000  ? 438 SER D N   1 
ATOM   3051 C CA  . SER D 2 106 ? 49.50200 4.30000   -4.12900  1.000 83.34000  ? 438 SER D CA  1 
ATOM   3052 C C   . SER D 2 106 ? 49.59200 4.31100   -2.60300  1.000 88.19000  ? 438 SER D C   1 
ATOM   3053 O O   . SER D 2 106 ? 49.46300 5.35800   -1.95700  1.000 84.76000  ? 438 SER D O   1 
ATOM   3054 C CB  . SER D 2 106 ? 48.93000 5.62000   -4.65100  1.000 83.07000  ? 438 SER D CB  1 
ATOM   3055 O OG  . SER D 2 106 ? 47.61600 5.80900   -4.15300  1.000 80.80000  ? 438 SER D OG  1 
ATOM   3056 N N   . ASN D 2 107 ? 49.81600 3.13600   -2.01700  1.000 93.38000  ? 439 ASN D N   1 
ATOM   3057 C CA  . ASN D 2 107 ? 49.92200 3.04700   -0.56400  1.000 88.26000  ? 439 ASN D CA  1 
ATOM   3058 C C   . ASN D 2 107 ? 51.19000 3.71300   -0.04600  1.000 90.55000  ? 439 ASN D C   1 
ATOM   3059 O O   . ASN D 2 107 ? 51.20700 4.21800   1.08300   1.000 89.97000  ? 439 ASN D O   1 
ATOM   3060 C CB  . ASN D 2 107 ? 49.87100 1.58800   -0.11600  1.000 92.04000  ? 439 ASN D CB  1 
ATOM   3061 C CG  . ASN D 2 107 ? 49.99200 1.44100   1.37900   1.000 93.08000  ? 439 ASN D CG  1 
ATOM   3062 O OD1 . ASN D 2 107 ? 49.49000 2.26900   2.13300   1.000 91.91000  ? 439 ASN D OD1 1 
ATOM   3063 N ND2 . ASN D 2 107 ? 50.67500 0.39700   1.81600   1.000 91.91000  ? 439 ASN D ND2 1 
ATOM   3064 N N   . ASN D 2 108 ? 52.25600 3.71800   -0.84300  1.000 90.05000  ? 440 ASN D N   1 
ATOM   3065 C CA  . ASN D 2 108 ? 53.45900 4.44600   -0.46200  1.000 88.88000  ? 440 ASN D CA  1 
ATOM   3066 C C   . ASN D 2 108 ? 53.21900 5.94900   -0.48300  1.000 93.85000  ? 440 ASN D C   1 
ATOM   3067 O O   . ASN D 2 108 ? 53.59200 6.66300   0.45800   1.000 100.12000 ? 440 ASN D O   1 
ATOM   3068 C CB  . ASN D 2 108 ? 54.59300 4.08000   -1.40200  1.000 92.06000  ? 440 ASN D CB  1 
ATOM   3069 C CG  . ASN D 2 108 ? 54.15100 4.07600   -2.85600  1.000 102.09000 ? 440 ASN D CG  1 
ATOM   3070 O OD1 . ASN D 2 108 ? 53.06300 3.58000   -3.18900  1.000 97.95000  ? 440 ASN D OD1 1 
ATOM   3071 N ND2 . ASN D 2 108 ? 54.98400 4.64100   -3.73200  1.000 109.81000 ? 440 ASN D ND2 1 
ATOM   3072 N N   . LEU D 2 109 ? 52.58700 6.45000   -1.54900  1.000 93.60000  ? 441 LEU D N   1 
ATOM   3073 C CA  . LEU D 2 109 ? 52.40500 7.88900   -1.71300  1.000 89.25000  ? 441 LEU D CA  1 
ATOM   3074 C C   . LEU D 2 109 ? 51.41300 8.45500   -0.70300  1.000 90.47000  ? 441 LEU D C   1 
ATOM   3075 O O   . LEU D 2 109 ? 51.71000 9.43400   -0.00900  1.000 89.79000  ? 441 LEU D O   1 
ATOM   3076 C CB  . LEU D 2 109 ? 51.92500 8.19100   -3.12700  1.000 90.45000  ? 441 LEU D CB  1 
ATOM   3077 C CG  . LEU D 2 109 ? 52.76400 7.74600   -4.32300  1.000 91.92000  ? 441 LEU D CG  1 
ATOM   3078 C CD1 . LEU D 2 109 ? 52.07500 8.18800   -5.61800  1.000 89.74000  ? 441 LEU D CD1 1 
ATOM   3079 C CD2 . LEU D 2 109 ? 54.17700 8.30100   -4.24400  1.000 87.77000  ? 441 LEU D CD2 1 
ATOM   3080 N N   . ASP D 2 110 ? 50.22400 7.85200   -0.60700  1.000 90.89000  ? 442 ASP D N   1 
ATOM   3081 C CA  . ASP D 2 110 ? 49.08000 8.45400   0.06800   1.000 85.73000  ? 442 ASP D CA  1 
ATOM   3082 C C   . ASP D 2 110 ? 48.75600 7.83700   1.42900   1.000 86.97000  ? 442 ASP D C   1 
ATOM   3083 O O   . ASP D 2 110 ? 47.70400 8.15500   1.99200   1.000 86.27000  ? 442 ASP D O   1 
ATOM   3084 C CB  . ASP D 2 110 ? 47.84200 8.36100   -0.83000  1.000 90.19000  ? 442 ASP D CB  1 
ATOM   3085 C CG  . ASP D 2 110 ? 48.06400 8.94200   -2.22200  1.000 89.65000  ? 442 ASP D CG  1 
ATOM   3086 O OD1 . ASP D 2 110 ? 48.44400 10.13200  -2.33400  1.000 87.92000  ? 442 ASP D OD1 1 
ATOM   3087 O OD2 . ASP D 2 110 ? 47.84500 8.19700   -3.20100  1.000 83.42000  ? 442 ASP D OD2 1 
ATOM   3088 N N   . SER D 2 111 ? 49.59300 6.94500   1.95800   1.000 85.43000  ? 443 SER D N   1 
ATOM   3089 C CA  . SER D 2 111 ? 49.45300 6.49000   3.33800   1.000 91.72000  ? 443 SER D CA  1 
ATOM   3090 C C   . SER D 2 111 ? 50.47200 7.18600   4.22900   1.000 91.37000  ? 443 SER D C   1 
ATOM   3091 O O   . SER D 2 111 ? 51.56000 7.56700   3.77900   1.000 91.19000  ? 443 SER D O   1 
ATOM   3092 C CB  . SER D 2 111 ? 49.63800 4.97800   3.48300   1.000 92.78000  ? 443 SER D CB  1 
ATOM   3093 O OG  . SER D 2 111 ? 48.47800 4.26700   3.09600   1.000 93.76000  ? 443 SER D OG  1 
ATOM   3094 N N   . LYS D 2 112 ? 50.11100 7.34100   5.50000   1.000 86.02000  ? 444 LYS D N   1 
ATOM   3095 C CA  . LYS D 2 112 ? 51.00200 7.93900   6.48100   1.000 90.54000  ? 444 LYS D CA  1 
ATOM   3096 C C   . LYS D 2 112 ? 50.93700 7.10200   7.75200   1.000 96.65000  ? 444 LYS D C   1 
ATOM   3097 O O   . LYS D 2 112 ? 49.92200 6.45500   8.03100   1.000 95.15000  ? 444 LYS D O   1 
ATOM   3098 C CB  . LYS D 2 112 ? 50.62200 9.41400   6.74400   1.000 88.66000  ? 444 LYS D CB  1 
ATOM   3099 C CG  . LYS D 2 112 ? 51.44100 10.12700  7.84100   1.000 98.66000  ? 444 LYS D CG  1 
ATOM   3100 C CD  . LYS D 2 112 ? 50.71700 11.38300  8.40300   1.000 101.05000 ? 444 LYS D CD  1 
ATOM   3101 C CE  . LYS D 2 112 ? 50.75200 11.48100  9.95000   1.000 90.09000  ? 444 LYS D CE  1 
ATOM   3102 N NZ  . LYS D 2 112 ? 52.13500 11.41200  10.55400  1.000 90.00000  ? 444 LYS D NZ  1 
ATOM   3103 N N   . VAL D 2 113 ? 52.03600 7.08300   8.50800   1.000 102.52000 ? 445 VAL D N   1 
ATOM   3104 C CA  . VAL D 2 113 ? 52.00900 6.46000   9.83200   1.000 101.72000 ? 445 VAL D CA  1 
ATOM   3105 C C   . VAL D 2 113 ? 51.21500 7.34100   10.78500  1.000 94.95000  ? 445 VAL D C   1 
ATOM   3106 O O   . VAL D 2 113 ? 51.46500 8.54700   10.90600  1.000 97.10000  ? 445 VAL D O   1 
ATOM   3107 C CB  . VAL D 2 113 ? 53.42900 6.21400   10.35700  1.000 103.63000 ? 445 VAL D CB  1 
ATOM   3108 C CG1 . VAL D 2 113 ? 53.38600 5.68200   11.78000  1.000 102.12000 ? 445 VAL D CG1 1 
ATOM   3109 C CG2 . VAL D 2 113 ? 54.16200 5.23700   9.44000   1.000 102.81000 ? 445 VAL D CG2 1 
ATOM   3110 N N   . GLY D 2 114 ? 50.24300 6.74700   11.46000  1.000 92.39000  ? 446 GLY D N   1 
ATOM   3111 C CA  . GLY D 2 114 ? 49.29500 7.53200   12.21800  1.000 94.41000  ? 446 GLY D CA  1 
ATOM   3112 C C   . GLY D 2 114 ? 48.13800 8.06500   11.40800  1.000 94.87000  ? 446 GLY D C   1 
ATOM   3113 O O   . GLY D 2 114 ? 47.50700 9.04600   11.81900  1.000 96.68000  ? 446 GLY D O   1 
ATOM   3114 N N   . GLY D 2 115 ? 47.85200 7.46300   10.25900  1.000 95.26000  ? 447 GLY D N   1 
ATOM   3115 C CA  . GLY D 2 115 ? 46.69200 7.81800   9.47500   1.000 93.79000  ? 447 GLY D CA  1 
ATOM   3116 C C   . GLY D 2 115 ? 46.85300 9.06400   8.62900   1.000 92.96000  ? 447 GLY D C   1 
ATOM   3117 O O   . GLY D 2 115 ? 47.13800 10.14400  9.16600   1.000 86.61000  ? 447 GLY D O   1 
ATOM   3118 N N   . ASN D 2 116 ? 46.67300 8.91800   7.30200   1.000 93.77000  ? 448 ASN D N   1 
ATOM   3119 C CA  . ASN D 2 116 ? 46.47300 10.05500  6.40600   1.000 87.76000  ? 448 ASN D CA  1 
ATOM   3120 C C   . ASN D 2 116 ? 44.98100 10.36200  6.32200   1.000 85.01000  ? 448 ASN D C   1 
ATOM   3121 O O   . ASN D 2 116 ? 44.16300 9.47000   6.07400   1.000 81.98000  ? 448 ASN D O   1 
ATOM   3122 C CB  . ASN D 2 116 ? 47.04400 9.79100   5.01400   1.000 91.47000  ? 448 ASN D CB  1 
ATOM   3123 C CG  . ASN D 2 116 ? 47.04000 11.04700  4.12700   1.000 95.68000  ? 448 ASN D CG  1 
ATOM   3124 O OD1 . ASN D 2 116 ? 46.37900 12.04100  4.44300   1.000 92.32000  ? 448 ASN D OD1 1 
ATOM   3125 N ND2 . ASN D 2 116 ? 47.78600 11.00200  3.01600   1.000 86.54000  ? 448 ASN D ND2 1 
ATOM   3126 N N   . TYR D 2 117 ? 44.63800 11.63000  6.52500   1.000 85.88000  ? 449 TYR D N   1 
ATOM   3127 C CA  . TYR D 2 117 ? 43.26000 12.03300  6.75300   1.000 87.13000  ? 449 TYR D CA  1 
ATOM   3128 C C   . TYR D 2 117 ? 42.82600 13.15400  5.82200   1.000 86.28000  ? 449 TYR D C   1 
ATOM   3129 O O   . TYR D 2 117 ? 41.71200 13.66600  5.97300   1.000 87.39000  ? 449 TYR D O   1 
ATOM   3130 C CB  . TYR D 2 117 ? 43.07100 12.45400  8.22800   1.000 89.34000  ? 449 TYR D CB  1 
ATOM   3131 C CG  . TYR D 2 117 ? 43.06600 11.28900  9.21200   1.000 85.01000  ? 449 TYR D CG  1 
ATOM   3132 C CD1 . TYR D 2 117 ? 41.89800 10.57000  9.45600   1.000 85.63000  ? 449 TYR D CD1 1 
ATOM   3133 C CD2 . TYR D 2 117 ? 44.22100 10.90200  9.88200   1.000 82.63000  ? 449 TYR D CD2 1 
ATOM   3134 C CE1 . TYR D 2 117 ? 41.87400 9.50000   10.33300  1.000 85.76000  ? 449 TYR D CE1 1 
ATOM   3135 C CE2 . TYR D 2 117 ? 44.20600 9.82900   10.77200  1.000 86.40000  ? 449 TYR D CE2 1 
ATOM   3136 C CZ  . TYR D 2 117 ? 43.02900 9.13500   10.98900  1.000 89.14000  ? 449 TYR D CZ  1 
ATOM   3137 O OH  . TYR D 2 117 ? 43.00300 8.07700   11.86300  1.000 90.24000  ? 449 TYR D OH  1 
ATOM   3138 N N   . ASN D 2 118 ? 43.68200 13.53800  4.86800   1.000 87.06000  ? 450 ASN D N   1 
ATOM   3139 C CA  . ASN D 2 118 ? 43.43200 14.57300  3.87000   1.000 94.19000  ? 450 ASN D CA  1 
ATOM   3140 C C   . ASN D 2 118 ? 42.86300 14.03200  2.55200   1.000 92.74000  ? 450 ASN D C   1 
ATOM   3141 O O   . ASN D 2 118 ? 42.99100 14.69500  1.51400   1.000 89.28000  ? 450 ASN D O   1 
ATOM   3142 C CB  . ASN D 2 118 ? 44.72400 15.32200  3.56300   1.000 96.49000  ? 450 ASN D CB  1 
ATOM   3143 C CG  . ASN D 2 118 ? 45.25400 16.06700  4.75300   1.000 92.27000  ? 450 ASN D CG  1 
ATOM   3144 O OD1 . ASN D 2 118 ? 46.44100 15.97100  5.06900   1.000 100.59000 ? 450 ASN D OD1 1 
ATOM   3145 N ND2 . ASN D 2 118 ? 44.38400 16.82900  5.41700   1.000 98.37000  ? 450 ASN D ND2 1 
ATOM   3146 N N   . TYR D 2 119 ? 42.29400 12.83200  2.55900   1.000 87.89000  ? 451 TYR D N   1 
ATOM   3147 C CA  . TYR D 2 119 ? 41.51100 12.32200  1.44500   1.000 83.61000  ? 451 TYR D CA  1 
ATOM   3148 C C   . TYR D 2 119 ? 40.15400 11.96500  2.03000   1.000 84.82000  ? 451 TYR D C   1 
ATOM   3149 O O   . TYR D 2 119 ? 40.07200 11.09900  2.90700   1.000 88.09000  ? 451 TYR D O   1 
ATOM   3150 C CB  . TYR D 2 119 ? 42.18300 11.10500  0.79600   1.000 81.62000  ? 451 TYR D CB  1 
ATOM   3151 C CG  . TYR D 2 119 ? 43.34800 11.40500  -0.14600  1.000 81.51000  ? 451 TYR D CG  1 
ATOM   3152 C CD1 . TYR D 2 119 ? 43.13000 11.63400  -1.50200  1.000 84.93000  ? 451 TYR D CD1 1 
ATOM   3153 C CD2 . TYR D 2 119 ? 44.66400 11.41400  0.30400   1.000 84.55000  ? 451 TYR D CD2 1 
ATOM   3154 C CE1 . TYR D 2 119 ? 44.19200 11.88600  -2.38400  1.000 86.84000  ? 451 TYR D CE1 1 
ATOM   3155 C CE2 . TYR D 2 119 ? 45.73000 11.66600  -0.57100  1.000 83.06000  ? 451 TYR D CE2 1 
ATOM   3156 C CZ  . TYR D 2 119 ? 45.48500 11.89800  -1.91700  1.000 83.33000  ? 451 TYR D CZ  1 
ATOM   3157 O OH  . TYR D 2 119 ? 46.51600 12.15500  -2.80100  1.000 83.84000  ? 451 TYR D OH  1 
ATOM   3158 N N   . LEU D 2 120 ? 39.10200 12.65300  1.59500   1.000 83.90000  ? 452 LEU D N   1 
ATOM   3159 C CA  . LEU D 2 120 ? 37.80500 12.51600  2.24500   1.000 82.27000  ? 452 LEU D CA  1 
ATOM   3160 C C   . LEU D 2 120 ? 36.87100 11.69500  1.37800   1.000 75.61000  ? 452 LEU D C   1 
ATOM   3161 O O   . LEU D 2 120 ? 37.22800 11.29000  0.28400   1.000 79.99000  ? 452 LEU D O   1 
ATOM   3162 C CB  . LEU D 2 120 ? 37.18500 13.88400  2.55300   1.000 81.58000  ? 452 LEU D CB  1 
ATOM   3163 C CG  . LEU D 2 120 ? 37.98100 14.77400  3.51300   1.000 86.19000  ? 452 LEU D CG  1 
ATOM   3164 C CD1 . LEU D 2 120 ? 37.12900 15.89700  4.08000   1.000 85.73000  ? 452 LEU D CD1 1 
ATOM   3165 C CD2 . LEU D 2 120 ? 38.56900 13.94600  4.61900   1.000 91.27000  ? 452 LEU D CD2 1 
ATOM   3166 N N   . TYR D 2 121 ? 35.66700 11.44200  1.89000   1.000 76.64000  ? 453 TYR D N   1 
ATOM   3167 C CA  . TYR D 2 121 ? 34.64800 10.74500  1.11800   1.000 77.39000  ? 453 TYR D CA  1 
ATOM   3168 C C   . TYR D 2 121 ? 33.28600 10.98000  1.75300   1.000 78.57000  ? 453 TYR D C   1 
ATOM   3169 O O   . TYR D 2 121 ? 33.17300 11.23700  2.95200   1.000 79.53000  ? 453 TYR D O   1 
ATOM   3170 C CB  . TYR D 2 121 ? 34.94400 9.24400   0.98900   1.000 77.47000  ? 453 TYR D CB  1 
ATOM   3171 C CG  . TYR D 2 121 ? 34.73600 8.44300   2.25800   1.000 83.71000  ? 453 TYR D CG  1 
ATOM   3172 C CD1 . TYR D 2 121 ? 35.48600 8.70700   3.39300   1.000 84.45000  ? 453 TYR D CD1 1 
ATOM   3173 C CD2 . TYR D 2 121 ? 33.79600 7.41700   2.31100   1.000 81.64000  ? 453 TYR D CD2 1 
ATOM   3174 C CE1 . TYR D 2 121 ? 35.30200 7.99500   4.55400   1.000 85.15000  ? 453 TYR D CE1 1 
ATOM   3175 C CE2 . TYR D 2 121 ? 33.60700 6.69600   3.46300   1.000 85.89000  ? 453 TYR D CE2 1 
ATOM   3176 C CZ  . TYR D 2 121 ? 34.36300 6.99400   4.58700   1.000 84.40000  ? 453 TYR D CZ  1 
ATOM   3177 O OH  . TYR D 2 121 ? 34.19100 6.28900   5.74700   1.000 85.12000  ? 453 TYR D OH  1 
ATOM   3178 N N   . ARG D 2 122 ? 32.25100 10.86500  0.92800   1.000 75.79000  ? 454 ARG D N   1 
ATOM   3179 C CA  . ARG D 2 122 ? 30.87900 11.15900  1.31800   1.000 80.74000  ? 454 ARG D CA  1 
ATOM   3180 C C   . ARG D 2 122 ? 30.20200 9.88600   1.80400   1.000 81.52000  ? 454 ARG D C   1 
ATOM   3181 O O   . ARG D 2 122 ? 30.02500 8.94200   1.02500   1.000 81.82000  ? 454 ARG D O   1 
ATOM   3182 C CB  . ARG D 2 122 ? 30.09900 11.75900  0.14100   1.000 78.45000  ? 454 ARG D CB  1 
ATOM   3183 C CG  . ARG D 2 122 ? 28.64900 12.15600  0.47100   1.000 88.64000  ? 454 ARG D CG  1 
ATOM   3184 C CD  . ARG D 2 122 ? 28.05200 13.14700  -0.54200  1.000 84.58000  ? 454 ARG D CD  1 
ATOM   3185 N NE  . ARG D 2 122 ? 28.97500 14.25000  -0.76000  1.000 83.11000  ? 454 ARG D NE  1 
ATOM   3186 C CZ  . ARG D 2 122 ? 28.99900 15.37000  -0.04300  1.000 86.12000  ? 454 ARG D CZ  1 
ATOM   3187 N NH1 . ARG D 2 122 ? 28.12300 15.55800  0.93800   1.000 93.17000  ? 454 ARG D NH1 1 
ATOM   3188 N NH2 . ARG D 2 122 ? 29.90400 16.30600  -0.30700  1.000 78.76000  ? 454 ARG D NH2 1 
ATOM   3189 N N   . LEU D 2 123 ? 29.79600 9.87400   3.07800   1.000 80.82000  ? 455 LEU D N   1 
ATOM   3190 C CA  . LEU D 2 123 ? 29.06100 8.73400   3.61700   1.000 86.49000  ? 455 LEU D CA  1 
ATOM   3191 C C   . LEU D 2 123 ? 27.54300 8.86500   3.46500   1.000 86.29000  ? 455 LEU D C   1 
ATOM   3192 O O   . LEU D 2 123 ? 26.86400 7.85200   3.27100   1.000 85.34000  ? 455 LEU D O   1 
ATOM   3193 C CB  . LEU D 2 123 ? 29.43300 8.52900   5.08900   1.000 86.54000  ? 455 LEU D CB  1 
ATOM   3194 C CG  . LEU D 2 123 ? 28.77400 7.42100   5.92000   1.000 81.45000  ? 455 LEU D CG  1 
ATOM   3195 C CD1 . LEU D 2 123 ? 28.78100 6.10200   5.19900   1.000 82.00000  ? 455 LEU D CD1 1 
ATOM   3196 C CD2 . LEU D 2 123 ? 29.47700 7.27700   7.26600   1.000 89.14000  ? 455 LEU D CD2 1 
ATOM   3197 N N   . PHE D 2 124 ? 26.98500 10.07700  3.52600   1.000 90.00000  ? 456 PHE D N   1 
ATOM   3198 C CA  . PHE D 2 124 ? 25.53800 10.25400  3.44900   1.000 92.73000  ? 456 PHE D CA  1 
ATOM   3199 C C   . PHE D 2 124 ? 25.16100 11.25700  2.36800   1.000 89.14000  ? 456 PHE D C   1 
ATOM   3200 O O   . PHE D 2 124 ? 25.88600 12.21800  2.10800   1.000 86.18000  ? 456 PHE D O   1 
ATOM   3201 C CB  . PHE D 2 124 ? 24.92500 10.76400  4.75800   1.000 85.42000  ? 456 PHE D CB  1 
ATOM   3202 C CG  . PHE D 2 124 ? 25.33100 9.99600   5.96800   1.000 88.06000  ? 456 PHE D CG  1 
ATOM   3203 C CD1 . PHE D 2 124 ? 24.58400 8.91600   6.40300   1.000 87.84000  ? 456 PHE D CD1 1 
ATOM   3204 C CD2 . PHE D 2 124 ? 26.44200 10.37500  6.69300   1.000 87.92000  ? 456 PHE D CD2 1 
ATOM   3205 C CE1 . PHE D 2 124 ? 24.94600 8.22100   7.52500   1.000 81.14000  ? 456 PHE D CE1 1 
ATOM   3206 C CE2 . PHE D 2 124 ? 26.80900 9.68000   7.81000   1.000 87.19000  ? 456 PHE D CE2 1 
ATOM   3207 C CZ  . PHE D 2 124 ? 26.06000 8.59400   8.22100   1.000 83.79000  ? 456 PHE D CZ  1 
ATOM   3208 N N   . ARG D 2 125 ? 23.97800 11.05400  1.79700   1.000 85.09000  ? 457 ARG D N   1 
ATOM   3209 C CA  . ARG D 2 125 ? 23.39700 11.99700  0.86100   1.000 88.38000  ? 457 ARG D CA  1 
ATOM   3210 C C   . ARG D 2 125 ? 21.94300 11.61500  0.64700   1.000 93.97000  ? 457 ARG D C   1 
ATOM   3211 O O   . ARG D 2 125 ? 21.60400 10.42800  0.60600   1.000 94.15000  ? 457 ARG D O   1 
ATOM   3212 C CB  . ARG D 2 125 ? 24.15000 11.99000  -0.47400  1.000 96.06000  ? 457 ARG D CB  1 
ATOM   3213 C CG  . ARG D 2 125 ? 23.67900 13.02600  -1.45500  1.000 92.75000  ? 457 ARG D CG  1 
ATOM   3214 C CD  . ARG D 2 125 ? 24.63800 13.10600  -2.60100  1.000 95.77000  ? 457 ARG D CD  1 
ATOM   3215 N NE  . ARG D 2 125 ? 24.42100 14.28400  -3.43600  1.000 95.13000  ? 457 ARG D NE  1 
ATOM   3216 C CZ  . ARG D 2 125 ? 23.73600 14.27900  -4.56900  1.000 91.71000  ? 457 ARG D CZ  1 
ATOM   3217 N NH1 . ARG D 2 125 ? 23.20300 13.14600  -5.02100  1.000 93.81000  ? 457 ARG D NH1 1 
ATOM   3218 N NH2 . ARG D 2 125 ? 23.61400 15.40400  -5.25600  1.000 89.75000  ? 457 ARG D NH2 1 
ATOM   3219 N N   . LYS D 2 126 ? 21.09100 12.63100  0.48500   1.000 91.29000  ? 458 LYS D N   1 
ATOM   3220 C CA  . LYS D 2 126 ? 19.66400 12.37200  0.33200   1.000 94.69000  ? 458 LYS D CA  1 
ATOM   3221 C C   . LYS D 2 126 ? 19.33200 11.60500  -0.93500  1.000 95.18000  ? 458 LYS D C   1 
ATOM   3222 O O   . LYS D 2 126 ? 18.17500 11.20500  -1.10400  1.000 94.92000  ? 458 LYS D O   1 
ATOM   3223 C CB  . LYS D 2 126 ? 18.86500 13.67600  0.33700   1.000 100.97000 ? 458 LYS D CB  1 
ATOM   3224 C CG  . LYS D 2 126 ? 18.87500 14.41000  1.66500   1.000 112.80000 ? 458 LYS D CG  1 
ATOM   3225 C CD  . LYS D 2 126 ? 18.08100 15.72100  1.60800   1.000 119.88000 ? 458 LYS D CD  1 
ATOM   3226 C CE  . LYS D 2 126 ? 18.10700 16.39000  2.96000   1.000 121.65000 ? 458 LYS D CE  1 
ATOM   3227 N NZ  . LYS D 2 126 ? 17.35200 17.67100  2.87700   1.000 120.83000 ? 458 LYS D NZ  1 
ATOM   3228 N N   . SER D 2 127 ? 20.29600 11.39900  -1.82800  1.000 96.83000  ? 459 SER D N   1 
ATOM   3229 C CA  . SER D 2 127 ? 20.03100 10.69600  -3.07600  1.000 97.47000  ? 459 SER D CA  1 
ATOM   3230 C C   . SER D 2 127 ? 21.35100 10.39300  -3.77100  1.000 97.37000  ? 459 SER D C   1 
ATOM   3231 O O   . SER D 2 127 ? 22.39100 10.99200  -3.48200  1.000 98.94000  ? 459 SER D O   1 
ATOM   3232 C CB  . SER D 2 127 ? 19.10300 11.50100  -3.99900  1.000 95.29000  ? 459 SER D CB  1 
ATOM   3233 O OG  . SER D 2 127 ? 19.49800 12.86100  -4.07600  1.000 95.91000  ? 459 SER D OG  1 
ATOM   3234 N N   . ASN D 2 128 ? 21.28700 9.44300   -4.69300  1.000 96.30000  ? 460 ASN D N   1 
ATOM   3235 C CA  . ASN D 2 128 ? 22.44200 9.10100   -5.50200  1.000 94.36000  ? 460 ASN D CA  1 
ATOM   3236 C C   . ASN D 2 128 ? 22.84500 10.27800  -6.38700  1.000 94.94000  ? 460 ASN D C   1 
ATOM   3237 O O   . ASN D 2 128 ? 22.01600 11.10100  -6.78300  1.000 96.03000  ? 460 ASN D O   1 
ATOM   3238 C CB  . ASN D 2 128 ? 22.14000 7.87700   -6.37200  1.000 88.93000  ? 460 ASN D CB  1 
ATOM   3239 C CG  . ASN D 2 128 ? 21.82700 6.63500   -5.55300  1.000 85.97000  ? 460 ASN D CG  1 
ATOM   3240 O OD1 . ASN D 2 128 ? 22.42200 6.40100   -4.50300  1.000 87.84000  ? 460 ASN D OD1 1 
ATOM   3241 N ND2 . ASN D 2 128 ? 20.88400 5.83700   -6.02900  1.000 83.72000  ? 460 ASN D ND2 1 
ATOM   3242 N N   . LEU D 2 129 ? 24.14300 10.35800  -6.67000  1.000 95.01000  ? 461 LEU D N   1 
ATOM   3243 C CA  . LEU D 2 129 ? 24.65200 11.26500  -7.68600  1.000 87.60000  ? 461 LEU D CA  1 
ATOM   3244 C C   . LEU D 2 129 ? 24.17300 10.82500  -9.06300  1.000 92.12000  ? 461 LEU D C   1 
ATOM   3245 O O   . LEU D 2 129 ? 24.09300 9.62600   -9.35600  1.000 93.55000  ? 461 LEU D O   1 
ATOM   3246 C CB  . LEU D 2 129 ? 26.18100 11.28100  -7.65700  1.000 83.20000  ? 461 LEU D CB  1 
ATOM   3247 C CG  . LEU D 2 129 ? 26.92200 12.42500  -6.98100  1.000 82.11000  ? 461 LEU D CG  1 
ATOM   3248 C CD1 . LEU D 2 129 ? 26.31100 12.70300  -5.65000  1.000 88.94000  ? 461 LEU D CD1 1 
ATOM   3249 C CD2 . LEU D 2 129 ? 28.37200 12.04700  -6.79000  1.000 76.59000  ? 461 LEU D CD2 1 
ATOM   3250 N N   . LYS D 2 130 ? 23.84400 11.79500  -9.91200  1.000 93.74000  ? 462 LYS D N   1 
ATOM   3251 C CA  . LYS D 2 130 ? 23.67400 11.47600  -11.32100 1.000 97.71000  ? 462 LYS D CA  1 
ATOM   3252 C C   . LYS D 2 130 ? 25.04500 11.44500  -11.99400 1.000 91.97000  ? 462 LYS D C   1 
ATOM   3253 O O   . LYS D 2 130 ? 26.00900 12.02100  -11.47100 1.000 88.12000  ? 462 LYS D O   1 
ATOM   3254 C CB  . LYS D 2 130 ? 22.73700 12.48500  -11.99700 1.000 101.74000 ? 462 LYS D CB  1 
ATOM   3255 C CG  . LYS D 2 130 ? 21.27800 12.44000  -11.52600 1.000 105.68000 ? 462 LYS D CG  1 
ATOM   3256 C CD  . LYS D 2 130 ? 20.38400 13.48700  -12.21500 1.000 110.21000 ? 462 LYS D CD  1 
ATOM   3257 C CE  . LYS D 2 130 ? 18.92800 13.37500  -11.71800 1.000 114.68000 ? 462 LYS D CE  1 
ATOM   3258 N NZ  . LYS D 2 130 ? 17.96100 14.36200  -12.30200 1.000 120.27000 ? 462 LYS D NZ  1 
ATOM   3259 N N   . PRO D 2 131 ? 25.16900 10.74900  -13.13100 1.000 85.06000  ? 463 PRO D N   1 
ATOM   3260 C CA  . PRO D 2 131 ? 26.48000 10.59100  -13.77400 1.000 84.14000  ? 463 PRO D CA  1 
ATOM   3261 C C   . PRO D 2 131 ? 27.27600 11.88500  -13.82700 1.000 85.23000  ? 463 PRO D C   1 
ATOM   3262 O O   . PRO D 2 131 ? 26.75500 12.94500  -14.17400 1.000 90.46000  ? 463 PRO D O   1 
ATOM   3263 C CB  . PRO D 2 131 ? 26.11500 10.10000  -15.17000 1.000 88.51000  ? 463 PRO D CB  1 
ATOM   3264 C CG  . PRO D 2 131 ? 24.89100 9.29800   -14.94800 1.000 90.10000  ? 463 PRO D CG  1 
ATOM   3265 C CD  . PRO D 2 131 ? 24.12100 10.01300  -13.86600 1.000 86.61000  ? 463 PRO D CD  1 
ATOM   3266 N N   . PHE D 2 132 ? 28.53500 11.80400  -13.41300 1.000 81.78000  ? 464 PHE D N   1 
ATOM   3267 C CA  . PHE D 2 132 ? 29.50700 12.88900  -13.49200 1.000 79.28000  ? 464 PHE D CA  1 
ATOM   3268 C C   . PHE D 2 132 ? 29.12600 14.10100  -12.67800 1.000 72.61000  ? 464 PHE D C   1 
ATOM   3269 O O   . PHE D 2 132 ? 29.79400 15.13400  -12.77400 1.000 79.55000  ? 464 PHE D O   1 
ATOM   3270 C CB  . PHE D 2 132 ? 29.76600 13.31600  -14.94000 1.000 80.80000  ? 464 PHE D CB  1 
ATOM   3271 C CG  . PHE D 2 132 ? 30.48100 12.29000  -15.72800 1.000 77.32000  ? 464 PHE D CG  1 
ATOM   3272 C CD1 . PHE D 2 132 ? 31.68900 11.78400  -15.27700 1.000 80.36000  ? 464 PHE D CD1 1 
ATOM   3273 C CD2 . PHE D 2 132 ? 29.95100 11.81300  -16.91700 1.000 82.91000  ? 464 PHE D CD2 1 
ATOM   3274 C CE1 . PHE D 2 132 ? 32.36300 10.82600  -16.00800 1.000 88.06000  ? 464 PHE D CE1 1 
ATOM   3275 C CE2 . PHE D 2 132 ? 30.61600 10.85000  -17.65500 1.000 84.57000  ? 464 PHE D CE2 1 
ATOM   3276 C CZ  . PHE D 2 132 ? 31.82200 10.35600  -17.20900 1.000 85.26000  ? 464 PHE D CZ  1 
ATOM   3277 N N   . GLU D 2 133 ? 28.08500 14.01900  -11.86400 1.000 83.80000  ? 465 GLU D N   1 
ATOM   3278 C CA  . GLU D 2 133 ? 27.89100 15.07000  -10.88000 1.000 80.89000  ? 465 GLU D CA  1 
ATOM   3279 C C   . GLU D 2 133 ? 29.08600 15.10800  -9.94300  1.000 80.57000  ? 465 GLU D C   1 
ATOM   3280 O O   . GLU D 2 133 ? 29.77000 14.09900  -9.72700  1.000 80.71000  ? 465 GLU D O   1 
ATOM   3281 C CB  . GLU D 2 133 ? 26.60700 14.85400  -10.08700 1.000 83.53000  ? 465 GLU D CB  1 
ATOM   3282 C CG  . GLU D 2 133 ? 26.27800 16.03300  -9.19000  1.000 90.22000  ? 465 GLU D CG  1 
ATOM   3283 C CD  . GLU D 2 133 ? 24.85700 16.01600  -8.67300  1.000 94.83000  ? 465 GLU D CD  1 
ATOM   3284 O OE1 . GLU D 2 133 ? 24.09600 15.09800  -9.05300  1.000 92.14000  ? 465 GLU D OE1 1 
ATOM   3285 O OE2 . GLU D 2 133 ? 24.50700 16.93000  -7.88800  1.000 106.12000 ? 465 GLU D OE2 1 
ATOM   3286 N N   . ARG D 2 134 ? 29.35900 16.29900  -9.42100  1.000 86.22000  ? 466 ARG D N   1 
ATOM   3287 C CA  . ARG D 2 134 ? 30.37400 16.51200  -8.39600  1.000 80.13000  ? 466 ARG D CA  1 
ATOM   3288 C C   . ARG D 2 134 ? 29.72300 17.27900  -7.25600  1.000 77.81000  ? 466 ARG D C   1 
ATOM   3289 O O   . ARG D 2 134 ? 29.42500 18.46900  -7.39400  1.000 83.97000  ? 466 ARG D O   1 
ATOM   3290 C CB  . ARG D 2 134 ? 31.57800 17.26800  -8.95000  1.000 80.81000  ? 466 ARG D CB  1 
ATOM   3291 C CG  . ARG D 2 134 ? 32.48200 17.81600  -7.88200  1.000 77.36000  ? 466 ARG D CG  1 
ATOM   3292 C CD  . ARG D 2 134 ? 33.79000 18.28600  -8.45300  1.000 70.48000  ? 466 ARG D CD  1 
ATOM   3293 N NE  . ARG D 2 134 ? 34.12300 19.59800  -7.92500  1.000 75.63000  ? 466 ARG D NE  1 
ATOM   3294 C CZ  . ARG D 2 134 ? 35.36100 19.99900  -7.68300  1.000 78.79000  ? 466 ARG D CZ  1 
ATOM   3295 N NH1 . ARG D 2 134 ? 36.35900 19.16300  -7.91600  1.000 81.60000  ? 466 ARG D NH1 1 
ATOM   3296 N NH2 . ARG D 2 134 ? 35.60100 21.22300  -7.20700  1.000 80.25000  ? 466 ARG D NH2 1 
ATOM   3297 N N   . ASP D 2 135 ? 29.50300 16.59800  -6.13500  1.000 90.37000  ? 467 ASP D N   1 
ATOM   3298 C CA  . ASP D 2 135 ? 28.85100 17.16000  -4.95100  1.000 85.27000  ? 467 ASP D CA  1 
ATOM   3299 C C   . ASP D 2 135 ? 29.90900 17.43500  -3.89000  1.000 78.13000  ? 467 ASP D C   1 
ATOM   3300 O O   . ASP D 2 135 ? 30.50800 16.49800  -3.35300  1.000 82.17000  ? 467 ASP D O   1 
ATOM   3301 C CB  . ASP D 2 135 ? 27.79400 16.19100  -4.41900  1.000 84.49000  ? 467 ASP D CB  1 
ATOM   3302 C CG  . ASP D 2 135 ? 26.98400 16.76500  -3.27000  1.000 88.02000  ? 467 ASP D CG  1 
ATOM   3303 O OD1 . ASP D 2 135 ? 27.45200 17.73300  -2.62400  1.000 92.24000  ? 467 ASP D OD1 1 
ATOM   3304 O OD2 . ASP D 2 135 ? 25.87800 16.23100  -3.01500  1.000 87.73000  ? 467 ASP D OD2 1 
ATOM   3305 N N   . ILE D 2 136 ? 30.11600 18.71100  -3.56500  1.000 82.79000  ? 468 ILE D N   1 
ATOM   3306 C CA  . ILE D 2 136 ? 31.13100 19.07500  -2.57900  1.000 85.02000  ? 468 ILE D CA  1 
ATOM   3307 C C   . ILE D 2 136 ? 30.53100 19.90800  -1.45300  1.000 92.59000  ? 468 ILE D C   1 
ATOM   3308 O O   . ILE D 2 136 ? 31.20700 20.75100  -0.85200  1.000 98.41000  ? 468 ILE D O   1 
ATOM   3309 C CB  . ILE D 2 136 ? 32.31800 19.79000  -3.25200  1.000 84.80000  ? 468 ILE D CB  1 
ATOM   3310 C CG1 . ILE D 2 136 ? 31.93000 21.19100  -3.71900  1.000 93.19000  ? 468 ILE D CG1 1 
ATOM   3311 C CG2 . ILE D 2 136 ? 32.80500 18.96500  -4.42500  1.000 82.56000  ? 468 ILE D CG2 1 
ATOM   3312 C CD1 . ILE D 2 136 ? 33.12400 22.14000  -3.73400  1.000 91.96000  ? 468 ILE D CD1 1 
ATOM   3313 N N   . SER D 2 137 ? 29.27500 19.64200  -1.11900  1.000 91.65000  ? 469 SER D N   1 
ATOM   3314 C CA  . SER D 2 137 ? 28.65200 20.31100  0.01000   1.000 90.95000  ? 469 SER D CA  1 
ATOM   3315 C C   . SER D 2 137 ? 29.08600 19.70400  1.34200   1.000 89.46000  ? 469 SER D C   1 
ATOM   3316 O O   . SER D 2 137 ? 29.25300 18.48700  1.47300   1.000 88.42000  ? 469 SER D O   1 
ATOM   3317 C CB  . SER D 2 137 ? 27.13400 20.23100  -0.09800  1.000 93.89000  ? 469 SER D CB  1 
ATOM   3318 O OG  . SER D 2 137 ? 26.73200 18.87400  -0.01500  1.000 102.08000 ? 469 SER D OG  1 
ATOM   3319 N N   . THR D 2 138 ? 29.25300 20.56700  2.33900   1.000 96.84000  ? 470 THR D N   1 
ATOM   3320 C CA  . THR D 2 138 ? 29.39600 20.17000  3.73900   1.000 94.58000  ? 470 THR D CA  1 
ATOM   3321 C C   . THR D 2 138 ? 28.09900 20.41700  4.51000   1.000 94.28000  ? 470 THR D C   1 
ATOM   3322 O O   . THR D 2 138 ? 28.10300 20.92500  5.63800   1.000 92.35000  ? 470 THR D O   1 
ATOM   3323 C CB  . THR D 2 138 ? 30.57700 20.90400  4.38200   1.000 90.54000  ? 470 THR D CB  1 
ATOM   3324 O OG1 . THR D 2 138 ? 30.29000 22.29900  4.47600   1.000 90.61000  ? 470 THR D OG1 1 
ATOM   3325 C CG2 . THR D 2 138 ? 31.85300 20.73300  3.54600   1.000 85.93000  ? 470 THR D CG2 1 
ATOM   3326 N N   . GLU D 2 139 ? 26.96700 20.06100  3.89400   1.000 98.08000  ? 471 GLU D N   1 
ATOM   3327 C CA  . GLU D 2 139 ? 25.64000 20.29300  4.46200   1.000 96.87000  ? 471 GLU D CA  1 
ATOM   3328 C C   . GLU D 2 139 ? 25.28300 19.15200  5.39600   1.000 97.31000  ? 471 GLU D C   1 
ATOM   3329 O O   . GLU D 2 139 ? 25.27100 17.98600  4.98200   1.000 88.78000  ? 471 GLU D O   1 
ATOM   3330 C CB  . GLU D 2 139 ? 24.58800 20.40300  3.35900   1.000 97.41000  ? 471 GLU D CB  1 
ATOM   3331 C CG  . GLU D 2 139 ? 23.28100 21.06000  3.77500   1.000 99.19000  ? 471 GLU D CG  1 
ATOM   3332 C CD  . GLU D 2 139 ? 23.43800 22.55800  4.00600   1.000 109.30000 ? 471 GLU D CD  1 
ATOM   3333 O OE1 . GLU D 2 139 ? 23.83800 22.95000  5.12500   1.000 112.92000 ? 471 GLU D OE1 1 
ATOM   3334 O OE2 . GLU D 2 139 ? 23.18100 23.34200  3.06600   1.000 106.27000 ? 471 GLU D OE2 1 
ATOM   3335 N N   . ILE D 2 140 ? 24.95200 19.49400  6.64300   1.000 103.46000 ? 472 ILE D N   1 
ATOM   3336 C CA  . ILE D 2 140 ? 24.73400 18.47400  7.66000   1.000 96.04000  ? 472 ILE D CA  1 
ATOM   3337 C C   . ILE D 2 140 ? 23.52100 17.63300  7.30200   1.000 94.71000  ? 472 ILE D C   1 
ATOM   3338 O O   . ILE D 2 140 ? 22.49900 18.13300  6.81000   1.000 93.09000  ? 472 ILE D O   1 
ATOM   3339 C CB  . ILE D 2 140 ? 24.60100 19.10600  9.05200   1.000 98.11000  ? 472 ILE D CB  1 
ATOM   3340 C CG1 . ILE D 2 140 ? 25.98400 19.21400  9.69900   1.000 103.37000 ? 472 ILE D CG1 1 
ATOM   3341 C CG2 . ILE D 2 140 ? 23.65900 18.28400  9.91700   1.000 99.22000  ? 472 ILE D CG2 1 
ATOM   3342 C CD1 . ILE D 2 140 ? 26.98700 20.05600  8.92000   1.000 99.62000  ? 472 ILE D CD1 1 
ATOM   3343 N N   . TYR D 2 141 ? 23.65700 16.33600  7.51700   1.000 93.20000  ? 473 TYR D N   1 
ATOM   3344 C CA  . TYR D 2 141 ? 22.69200 15.35100  7.07300   1.000 90.84000  ? 473 TYR D CA  1 
ATOM   3345 C C   . TYR D 2 141 ? 21.79800 14.98100  8.24500   1.000 102.24000 ? 473 TYR D C   1 
ATOM   3346 O O   . TYR D 2 141 ? 22.28300 14.45300  9.24800   1.000 100.27000 ? 473 TYR D O   1 
ATOM   3347 C CB  . TYR D 2 141 ? 23.42700 14.12400  6.55000   1.000 88.18000  ? 473 TYR D CB  1 
ATOM   3348 C CG  . TYR D 2 141 ? 22.55100 13.10700  5.87600   1.000 92.85000  ? 473 TYR D CG  1 
ATOM   3349 C CD1 . TYR D 2 141 ? 22.14700 13.28200  4.54500   1.000 89.03000  ? 473 TYR D CD1 1 
ATOM   3350 C CD2 . TYR D 2 141 ? 22.15100 11.95300  6.54800   1.000 92.14000  ? 473 TYR D CD2 1 
ATOM   3351 C CE1 . TYR D 2 141 ? 21.35900 12.35100  3.91200   1.000 88.56000  ? 473 TYR D CE1 1 
ATOM   3352 C CE2 . TYR D 2 141 ? 21.36500 11.00700  5.91100   1.000 93.22000  ? 473 TYR D CE2 1 
ATOM   3353 C CZ  . TYR D 2 141 ? 20.96900 11.21800  4.59600   1.000 94.21000  ? 473 TYR D CZ  1 
ATOM   3354 O OH  . TYR D 2 141 ? 20.18100 10.28700  3.97000   1.000 95.10000  ? 473 TYR D OH  1 
ATOM   3355 N N   . GLN D 2 142 ? 20.50700 15.26900  8.13200   1.000 105.63000 ? 474 GLN D N   1 
ATOM   3356 C CA  . GLN D 2 142 ? 19.53500 14.71600  9.06200   1.000 104.30000 ? 474 GLN D CA  1 
ATOM   3357 C C   . GLN D 2 142 ? 18.96500 13.45200  8.42200   1.000 104.48000 ? 474 GLN D C   1 
ATOM   3358 O O   . GLN D 2 142 ? 18.41900 13.49600  7.31500   1.000 103.48000 ? 474 GLN D O   1 
ATOM   3359 C CB  . GLN D 2 142 ? 18.44800 15.73500  9.43500   1.000 104.59000 ? 474 GLN D CB  1 
ATOM   3360 C CG  . GLN D 2 142 ? 17.40400 16.07900  8.36400   1.000 109.36000 ? 474 GLN D CG  1 
ATOM   3361 C CD  . GLN D 2 142 ? 16.16100 15.19400  8.44100   1.000 109.18000 ? 474 GLN D CD  1 
ATOM   3362 O OE1 . GLN D 2 142 ? 16.17200 14.15100  9.09600   1.000 112.14000 ? 474 GLN D OE1 1 
ATOM   3363 N NE2 . GLN D 2 142 ? 15.08400 15.61200  7.77700   1.000 93.41000  ? 474 GLN D NE2 1 
ATOM   3364 N N   . ALA D 2 143 ? 19.15700 12.31600  9.09200   1.000 105.24000 ? 475 ALA D N   1 
ATOM   3365 C CA  . ALA D 2 143 ? 18.69300 11.02400  8.60000   1.000 105.10000 ? 475 ALA D CA  1 
ATOM   3366 C C   . ALA D 2 143 ? 17.53100 10.46400  9.40000   1.000 105.00000 ? 475 ALA D C   1 
ATOM   3367 O O   . ALA D 2 143 ? 17.02900 9.38800   9.06100   1.000 102.31000 ? 475 ALA D O   1 
ATOM   3368 C CB  . ALA D 2 143 ? 19.83300 9.99700   8.61200   1.000 102.32000 ? 475 ALA D CB  1 
ATOM   3369 N N   . GLY D 2 144 ? 17.11400 11.13600  10.45500  1.000 105.66000 ? 476 GLY D N   1 
ATOM   3370 C CA  . GLY D 2 144 ? 15.97600 10.69700  11.22300  1.000 110.62000 ? 476 GLY D CA  1 
ATOM   3371 C C   . GLY D 2 144 ? 14.75400 11.52500  10.90800  1.000 111.28000 ? 476 GLY D C   1 
ATOM   3372 O O   . GLY D 2 144 ? 14.51600 11.90500  9.75800   1.000 110.27000 ? 476 GLY D O   1 
ATOM   3373 N N   . SER D 2 145 ? 13.96900 11.80500  11.94300  1.000 113.43000 ? 477 SER D N   1 
ATOM   3374 C CA  . SER D 2 145 ? 12.88700 12.76100  11.83300  1.000 114.32000 ? 477 SER D CA  1 
ATOM   3375 C C   . SER D 2 145 ? 13.23600 14.11800  12.41800  1.000 116.27000 ? 477 SER D C   1 
ATOM   3376 O O   . SER D 2 145 ? 12.51800 15.08300  12.14800  1.000 114.98000 ? 477 SER D O   1 
ATOM   3377 C CB  . SER D 2 145 ? 11.63100 12.22000  12.52600  1.000 116.77000 ? 477 SER D CB  1 
ATOM   3378 O OG  . SER D 2 145 ? 11.29300 10.94600  12.01200  1.000 113.12000 ? 477 SER D OG  1 
ATOM   3379 N N   . THR D 2 146 ? 14.32000 14.21400  13.19200  1.000 118.17000 ? 478 THR D N   1 
ATOM   3380 C CA  . THR D 2 146 ? 14.69200 15.44000  13.88900  1.000 119.65000 ? 478 THR D CA  1 
ATOM   3381 C C   . THR D 2 146 ? 15.63800 16.32100  13.07700  1.000 122.29000 ? 478 THR D C   1 
ATOM   3382 O O   . THR D 2 146 ? 16.84400 16.04600  13.04000  1.000 122.27000 ? 478 THR D O   1 
ATOM   3383 C CB  . THR D 2 146 ? 15.35200 15.10000  15.22700  1.000 117.83000 ? 478 THR D CB  1 
ATOM   3384 O OG1 . THR D 2 146 ? 16.51400 14.29500  14.98900  1.000 120.76000 ? 478 THR D OG1 1 
ATOM   3385 C CG2 . THR D 2 146 ? 14.38700 14.33300  16.12400  1.000 115.47000 ? 478 THR D CG2 1 
ATOM   3386 N N   . PRO D 2 147 ? 15.15100 17.38600  12.42900  1.000 117.73000 ? 479 PRO D N   1 
ATOM   3387 C CA  . PRO D 2 147 ? 16.07400 18.39900  11.90200  1.000 115.68000 ? 479 PRO D CA  1 
ATOM   3388 C C   . PRO D 2 147 ? 16.89900 18.96900  13.04400  1.000 121.02000 ? 479 PRO D C   1 
ATOM   3389 O O   . PRO D 2 147 ? 16.44400 19.03400  14.19000  1.000 116.20000 ? 479 PRO D O   1 
ATOM   3390 C CB  . PRO D 2 147 ? 15.14200 19.45600  11.30300  1.000 110.99000 ? 479 PRO D CB  1 
ATOM   3391 C CG  . PRO D 2 147 ? 13.81900 18.77700  11.16200  1.000 105.98000 ? 479 PRO D CG  1 
ATOM   3392 C CD  . PRO D 2 147 ? 13.74900 17.80100  12.27500  1.000 109.76000 ? 479 PRO D CD  1 
ATOM   3393 N N   . CYS D 2 148 ? 18.13600 19.36900  12.73500  1.000 121.81000 ? 480 CYS D N   1 
ATOM   3394 C CA  . CYS D 2 148 ? 19.06300 19.70400  13.81100  1.000 118.49000 ? 480 CYS D CA  1 
ATOM   3395 C C   . CYS D 2 148 ? 19.73100 21.06100  13.64300  1.000 116.14000 ? 480 CYS D C   1 
ATOM   3396 O O   . CYS D 2 148 ? 20.81300 21.26700  14.19100  1.000 116.44000 ? 480 CYS D O   1 
ATOM   3397 C CB  . CYS D 2 148 ? 20.13400 18.62500  13.96300  1.000 120.49000 ? 480 CYS D CB  1 
ATOM   3398 S SG  . CYS D 2 148 ? 19.49100 16.98500  14.35300  1.000 130.00000 ? 480 CYS D SG  1 
ATOM   3399 N N   . ASN D 2 149 ? 19.12000 21.98900  12.90900  1.000 115.66000 ? 481 ASN D N   1 
ATOM   3400 C CA  . ASN D 2 149 ? 19.53400 23.39400  12.93500  1.000 113.44000 ? 481 ASN D CA  1 
ATOM   3401 C C   . ASN D 2 149 ? 21.01300 23.55800  12.57200  1.000 113.19000 ? 481 ASN D C   1 
ATOM   3402 O O   . ASN D 2 149 ? 21.75100 24.32000  13.20500  1.000 111.59000 ? 481 ASN D O   1 
ATOM   3403 C CB  . ASN D 2 149 ? 19.22600 24.01500  14.30200  1.000 110.48000 ? 481 ASN D CB  1 
ATOM   3404 C CG  . ASN D 2 149 ? 17.72900 24.21300  14.52400  1.000 109.67000 ? 481 ASN D CG  1 
ATOM   3405 O OD1 . ASN D 2 149 ? 16.93900 24.10800  13.57800  1.000 112.44000 ? 481 ASN D OD1 1 
ATOM   3406 N ND2 . ASN D 2 149 ? 17.32900 24.48500  15.77100  1.000 100.70000 ? 481 ASN D ND2 1 
ATOM   3407 N N   . GLY D 2 150 ? 21.44700 22.82700  11.54600  1.000 117.75000 ? 482 GLY D N   1 
ATOM   3408 C CA  . GLY D 2 150 ? 22.80400 22.93800  11.05200  1.000 113.23000 ? 482 GLY D CA  1 
ATOM   3409 C C   . GLY D 2 150 ? 23.86700 22.42600  11.99000  1.000 115.27000 ? 482 GLY D C   1 
ATOM   3410 O O   . GLY D 2 150 ? 25.02200 22.84700  11.89200  1.000 115.39000 ? 482 GLY D O   1 
ATOM   3411 N N   . VAL D 2 151 ? 23.50700 21.53900  12.91400  1.000 115.95000 ? 483 VAL D N   1 
ATOM   3412 C CA  . VAL D 2 151 ? 24.45400 20.96100  13.85600  1.000 112.36000 ? 483 VAL D CA  1 
ATOM   3413 C C   . VAL D 2 151 ? 24.29500 19.44600  13.83200  1.000 110.13000 ? 483 VAL D C   1 
ATOM   3414 O O   . VAL D 2 151 ? 23.20200 18.91800  13.60100  1.000 109.70000 ? 483 VAL D O   1 
ATOM   3415 C CB  . VAL D 2 151 ? 24.27200 21.53300  15.28900  1.000 116.47000 ? 483 VAL D CB  1 
ATOM   3416 C CG1 . VAL D 2 151 ? 24.05400 23.03500  15.24600  1.000 114.45000 ? 483 VAL D CG1 1 
ATOM   3417 C CG2 . VAL D 2 151 ? 23.13500 20.85700  16.02900  1.000 116.58000 ? 483 VAL D CG2 1 
ATOM   3418 N N   . GLU D 2 152 ? 25.40600 18.74300  14.04100  1.000 111.00000 ? 484 GLU D N   1 
ATOM   3419 C CA  . GLU D 2 152 ? 25.39000 17.28700  14.07100  1.000 107.64000 ? 484 GLU D CA  1 
ATOM   3420 C C   . GLU D 2 152 ? 24.97000 16.79000  15.45200  1.000 110.75000 ? 484 GLU D C   1 
ATOM   3421 O O   . GLU D 2 152 ? 25.30100 17.38900  16.48100  1.000 109.55000 ? 484 GLU D O   1 
ATOM   3422 C CB  . GLU D 2 152 ? 26.75800 16.69800  13.70700  1.000 101.01000 ? 484 GLU D CB  1 
ATOM   3423 C CG  . GLU D 2 152 ? 27.69900 17.64800  12.99200  1.000 100.99000 ? 484 GLU D CG  1 
ATOM   3424 C CD  . GLU D 2 152 ? 29.07200 17.04700  12.78000  1.000 104.63000 ? 484 GLU D CD  1 
ATOM   3425 O OE1 . GLU D 2 152 ? 29.17000 15.80000  12.74600  1.000 104.29000 ? 484 GLU D OE1 1 
ATOM   3426 O OE2 . GLU D 2 152 ? 30.05400 17.81500  12.64500  1.000 105.02000 ? 484 GLU D OE2 1 
ATOM   3427 N N   . GLY D 2 153 ? 24.23400 15.67800  15.45900  1.000 110.54000 ? 485 GLY D N   1 
ATOM   3428 C CA  . GLY D 2 153 ? 23.77100 15.05200  16.68200  1.000 102.98000 ? 485 GLY D CA  1 
ATOM   3429 C C   . GLY D 2 153 ? 22.98500 13.79400  16.38000  1.000 102.92000 ? 485 GLY D C   1 
ATOM   3430 O O   . GLY D 2 153 ? 23.32100 13.04600  15.45800  1.000 101.43000 ? 485 GLY D O   1 
ATOM   3431 N N   . PHE D 2 154 ? 21.92400 13.55500  17.13700  1.000 105.50000 ? 486 PHE D N   1 
ATOM   3432 C CA  . PHE D 2 154 ? 21.12500 12.35600  16.93600  1.000 103.86000 ? 486 PHE D CA  1 
ATOM   3433 C C   . PHE D 2 154 ? 20.44500 12.41000  15.57100  1.000 105.83000 ? 486 PHE D C   1 
ATOM   3434 O O   . PHE D 2 154 ? 19.65600 13.32100  15.29800  1.000 107.58000 ? 486 PHE D O   1 
ATOM   3435 C CB  . PHE D 2 154 ? 20.10100 12.21100  18.06000  1.000 102.32000 ? 486 PHE D CB  1 
ATOM   3436 C CG  . PHE D 2 154 ? 19.30500 10.93900  17.99500  1.000 105.12000 ? 486 PHE D CG  1 
ATOM   3437 C CD1 . PHE D 2 154 ? 19.85400 9.73500   18.41600  1.000 108.06000 ? 486 PHE D CD1 1 
ATOM   3438 C CD2 . PHE D 2 154 ? 18.00500 10.94400  17.51700  1.000 105.05000 ? 486 PHE D CD2 1 
ATOM   3439 C CE1 . PHE D 2 154 ? 19.12200 8.56100   18.35200  1.000 104.02000 ? 486 PHE D CE1 1 
ATOM   3440 C CE2 . PHE D 2 154 ? 17.26900 9.77500   17.45700  1.000 105.68000 ? 486 PHE D CE2 1 
ATOM   3441 C CZ  . PHE D 2 154 ? 17.82800 8.58300   17.87100  1.000 103.84000 ? 486 PHE D CZ  1 
ATOM   3442 N N   . ASN D 2 155 ? 20.76200 11.43500  14.71500  1.000 104.71000 ? 487 ASN D N   1 
ATOM   3443 C CA  . ASN D 2 155 ? 20.24300 11.33500  13.35000  1.000 104.58000 ? 487 ASN D CA  1 
ATOM   3444 C C   . ASN D 2 155 ? 20.63000 12.53400  12.48800  1.000 103.45000 ? 487 ASN D C   1 
ATOM   3445 O O   . ASN D 2 155 ? 19.96800 12.81500  11.48400  1.000 102.69000 ? 487 ASN D O   1 
ATOM   3446 C CB  . ASN D 2 155 ? 18.72200 11.15100  13.33400  1.000 106.03000 ? 487 ASN D CB  1 
ATOM   3447 C CG  . ASN D 2 155 ? 18.29000 9.76500   13.77400  1.000 105.68000 ? 487 ASN D CG  1 
ATOM   3448 O OD1 . ASN D 2 155 ? 17.21400 9.57400   14.33600  1.000 111.48000 ? 487 ASN D OD1 1 
ATOM   3449 N ND2 . ASN D 2 155 ? 19.14500 8.78800   13.52400  1.000 102.49000 ? 487 ASN D ND2 1 
ATOM   3450 N N   . CYS D 2 156 ? 21.70500 13.23300  12.86200  1.000 103.17000 ? 488 CYS D N   1 
ATOM   3451 C CA  . CYS D 2 156 ? 22.17500 14.41800  12.14900  1.000 103.74000 ? 488 CYS D CA  1 
ATOM   3452 C C   . CYS D 2 156 ? 23.69500 14.40600  12.13600  1.000 101.52000 ? 488 CYS D C   1 
ATOM   3453 O O   . CYS D 2 156 ? 24.32200 14.54700  13.19000  1.000 101.24000 ? 488 CYS D O   1 
ATOM   3454 C CB  . CYS D 2 156 ? 21.66100 15.69200  12.80100  1.000 103.55000 ? 488 CYS D CB  1 
ATOM   3455 S SG  . CYS D 2 156 ? 19.88700 15.90100  12.68700  1.000 111.75000 ? 488 CYS D SG  1 
ATOM   3456 N N   . TYR D 2 157 ? 24.29500 14.26000  10.95600  1.000 96.88000  ? 489 TYR D N   1 
ATOM   3457 C CA  . TYR D 2 157 ? 25.72600 14.00800  10.89700  1.000 98.69000  ? 489 TYR D CA  1 
ATOM   3458 C C   . TYR D 2 157 ? 26.38600 14.80200  9.77800   1.000 95.89000  ? 489 TYR D C   1 
ATOM   3459 O O   . TYR D 2 157 ? 25.77800 15.09600  8.74500   1.000 94.46000  ? 489 TYR D O   1 
ATOM   3460 C CB  . TYR D 2 157 ? 26.02500 12.51500  10.69700  1.000 100.55000 ? 489 TYR D CB  1 
ATOM   3461 C CG  . TYR D 2 157 ? 25.10700 11.56500  11.45000  1.000 99.23000  ? 489 TYR D CG  1 
ATOM   3462 C CD1 . TYR D 2 157 ? 25.23500 11.38100  12.82500  1.000 103.22000 ? 489 TYR D CD1 1 
ATOM   3463 C CD2 . TYR D 2 157 ? 24.12400 10.83300  10.78000  1.000 96.57000  ? 489 TYR D CD2 1 
ATOM   3464 C CE1 . TYR D 2 157 ? 24.40200 10.50200  13.52000  1.000 101.26000 ? 489 TYR D CE1 1 
ATOM   3465 C CE2 . TYR D 2 157 ? 23.28800 9.95300   11.46600  1.000 100.34000 ? 489 TYR D CE2 1 
ATOM   3466 C CZ  . TYR D 2 157 ? 23.43300 9.79800   12.84000  1.000 99.56000  ? 489 TYR D CZ  1 
ATOM   3467 O OH  . TYR D 2 157 ? 22.61700 8.93200   13.52700  1.000 94.63000  ? 489 TYR D OH  1 
ATOM   3468 N N   . PHE D 2 158 ? 27.64600 15.13200  10.01000  1.000 95.08000  ? 490 PHE D N   1 
ATOM   3469 C CA  . PHE D 2 158 ? 28.50800 15.64900  8.96400   1.000 93.72000  ? 490 PHE D CA  1 
ATOM   3470 C C   . PHE D 2 158 ? 28.62700 14.61200  7.83900   1.000 91.12000  ? 490 PHE D C   1 
ATOM   3471 O O   . PHE D 2 158 ? 28.91200 13.43800  8.11100   1.000 89.00000  ? 490 PHE D O   1 
ATOM   3472 C CB  . PHE D 2 158 ? 29.86300 15.98100  9.59500   1.000 92.16000  ? 490 PHE D CB  1 
ATOM   3473 C CG  . PHE D 2 158 ? 30.80600 16.67600  8.68600   1.000 97.31000  ? 490 PHE D CG  1 
ATOM   3474 C CD1 . PHE D 2 158 ? 30.43500 17.84200  8.04700   1.000 101.35000 ? 490 PHE D CD1 1 
ATOM   3475 C CD2 . PHE D 2 158 ? 32.07700 16.17800  8.48200   1.000 96.67000  ? 490 PHE D CD2 1 
ATOM   3476 C CE1 . PHE D 2 158 ? 31.30900 18.48800  7.19000   1.000 95.99000  ? 490 PHE D CE1 1 
ATOM   3477 C CE2 . PHE D 2 158 ? 32.95800 16.82200  7.63900   1.000 97.67000  ? 490 PHE D CE2 1 
ATOM   3478 C CZ  . PHE D 2 158 ? 32.57200 17.98100  6.99300   1.000 95.38000  ? 490 PHE D CZ  1 
ATOM   3479 N N   . PRO D 2 159 ? 28.38700 14.98700  6.57400   1.000 90.57000  ? 491 PRO D N   1 
ATOM   3480 C CA  . PRO D 2 159 ? 28.20500 13.96000  5.52500   1.000 88.92000  ? 491 PRO D CA  1 
ATOM   3481 C C   . PRO D 2 159 ? 29.49100 13.36100  4.98100   1.000 86.20000  ? 491 PRO D C   1 
ATOM   3482 O O   . PRO D 2 159 ? 29.43900 12.30500  4.33200   1.000 81.56000  ? 491 PRO D O   1 
ATOM   3483 C CB  . PRO D 2 159 ? 27.45500 14.71900  4.41900   1.000 94.01000  ? 491 PRO D CB  1 
ATOM   3484 C CG  . PRO D 2 159 ? 27.91400 16.14500  4.58800   1.000 96.10000  ? 491 PRO D CG  1 
ATOM   3485 C CD  . PRO D 2 159 ? 28.14300 16.35100  6.06800   1.000 93.95000  ? 491 PRO D CD  1 
ATOM   3486 N N   . LEU D 2 160 ? 30.62500 14.01300  5.19500   1.000 84.60000  ? 492 LEU D N   1 
ATOM   3487 C CA  . LEU D 2 160 ? 31.92200 13.49100  4.80300   1.000 83.17000  ? 492 LEU D CA  1 
ATOM   3488 C C   . LEU D 2 160 ? 32.58200 12.78900  5.98500   1.000 88.99000  ? 492 LEU D C   1 
ATOM   3489 O O   . LEU D 2 160 ? 32.35900 13.14200  7.14400   1.000 93.54000  ? 492 LEU D O   1 
ATOM   3490 C CB  . LEU D 2 160 ? 32.83700 14.61200  4.30600   1.000 85.46000  ? 492 LEU D CB  1 
ATOM   3491 C CG  . LEU D 2 160 ? 32.35800 15.57600  3.21200   1.000 85.45000  ? 492 LEU D CG  1 
ATOM   3492 C CD1 . LEU D 2 160 ? 33.37700 16.69600  3.01900   1.000 75.69000  ? 492 LEU D CD1 1 
ATOM   3493 C CD2 . LEU D 2 160 ? 32.08900 14.84400  1.89300   1.000 83.40000  ? 492 LEU D CD2 1 
ATOM   3494 N N   . GLN D 2 161 ? 33.44500 11.83700  5.62000   1.000 90.89000  ? 493 GLN D N   1 
ATOM   3495 C CA  . GLN D 2 161 ? 34.28200 11.12800  6.61000   1.000 83.73000  ? 493 GLN D CA  1 
ATOM   3496 C C   . GLN D 2 161 ? 35.65800 11.06100  5.93600   1.000 84.13000  ? 493 GLN D C   1 
ATOM   3497 O O   . GLN D 2 161 ? 35.72200 11.33300  4.72000   1.000 88.75000  ? 493 GLN D O   1 
ATOM   3498 C CB  . GLN D 2 161 ? 33.69800 9.74900   6.91500   1.000 90.33000  ? 493 GLN D CB  1 
ATOM   3499 C CG  . GLN D 2 161 ? 34.47000 8.97200   7.97100   1.000 96.08000  ? 493 GLN D CG  1 
ATOM   3500 C CD  . GLN D 2 161 ? 34.84400 9.83600   9.15000   1.000 100.85000 ? 493 GLN D CD  1 
ATOM   3501 O OE1 . GLN D 2 161 ? 35.92100 10.42800  9.19500   1.000 101.56000 ? 493 GLN D OE1 1 
ATOM   3502 N NE2 . GLN D 2 161 ? 33.95200 9.91000   10.12400  1.000 100.38000 ? 493 GLN D NE2 1 
ATOM   3503 N N   . SER D 2 162 ? 36.71900 10.74700  6.67500   1.000 87.48000  ? 494 SER D N   1 
ATOM   3504 C CA  . SER D 2 162 ? 38.06200 10.71500  6.12400   1.000 85.17000  ? 494 SER D CA  1 
ATOM   3505 C C   . SER D 2 162 ? 38.55500 9.28800   5.98600   1.000 85.43000  ? 494 SER D C   1 
ATOM   3506 O O   . SER D 2 162 ? 38.39200 8.47800   6.90000   1.000 85.32000  ? 494 SER D O   1 
ATOM   3507 C CB  . SER D 2 162 ? 39.04800 11.48800  6.98500   1.000 85.07000  ? 494 SER D CB  1 
ATOM   3508 O OG  . SER D 2 162 ? 40.33800 11.37500  6.42300   1.000 85.68000  ? 494 SER D OG  1 
ATOM   3509 N N   . TYR D 2 163 ? 39.15300 8.98500   4.83200   1.000 88.70000  ? 495 TYR D N   1 
ATOM   3510 C CA  . TYR D 2 163 ? 40.05100 7.84500   4.75600   1.000 86.14000  ? 495 TYR D CA  1 
ATOM   3511 C C   . TYR D 2 163 ? 41.15200 8.03600   5.79500   1.000 87.56000  ? 495 TYR D C   1 
ATOM   3512 O O   . TYR D 2 163 ? 41.57500 9.16200   6.08300   1.000 87.26000  ? 495 TYR D O   1 
ATOM   3513 C CB  . TYR D 2 163 ? 40.64500 7.71000   3.34100   1.000 88.07000  ? 495 TYR D CB  1 
ATOM   3514 C CG  . TYR D 2 163 ? 39.64500 7.29500   2.26400   1.000 80.88000  ? 495 TYR D CG  1 
ATOM   3515 C CD1 . TYR D 2 163 ? 38.97200 6.08600   2.34800   1.000 78.41000  ? 495 TYR D CD1 1 
ATOM   3516 C CD2 . TYR D 2 163 ? 39.39100 8.10500   1.16300   1.000 82.93000  ? 495 TYR D CD2 1 
ATOM   3517 C CE1 . TYR D 2 163 ? 38.05800 5.69900   1.38900   1.000 82.06000  ? 495 TYR D CE1 1 
ATOM   3518 C CE2 . TYR D 2 163 ? 38.47400 7.72200   0.17700   1.000 80.58000  ? 495 TYR D CE2 1 
ATOM   3519 C CZ  . TYR D 2 163 ? 37.81500 6.51900   0.29900   1.000 84.36000  ? 495 TYR D CZ  1 
ATOM   3520 O OH  . TYR D 2 163 ? 36.91000 6.11200   -0.64600  1.000 84.63000  ? 495 TYR D OH  1 
ATOM   3521 N N   . GLY D 2 164 ? 41.59200 6.94000   6.39100   1.000 88.41000  ? 496 GLY D N   1 
ATOM   3522 C CA  . GLY D 2 164 ? 42.59200 7.05700   7.43300   1.000 91.20000  ? 496 GLY D CA  1 
ATOM   3523 C C   . GLY D 2 164 ? 43.86800 6.37100   7.01800   1.000 92.98000  ? 496 GLY D C   1 
ATOM   3524 O O   . GLY D 2 164 ? 44.47200 5.65200   7.82300   1.000 92.09000  ? 496 GLY D O   1 
ATOM   3525 N N   . PHE D 2 165 ? 44.28700 6.60800   5.76600   1.000 85.58000  ? 497 PHE D N   1 
ATOM   3526 C CA  . PHE D 2 165 ? 45.26000 5.76100   5.07700   1.000 89.66000  ? 497 PHE D CA  1 
ATOM   3527 C C   . PHE D 2 165 ? 46.54400 5.55200   5.87100   1.000 89.24000  ? 497 PHE D C   1 
ATOM   3528 O O   . PHE D 2 165 ? 47.28600 6.50200   6.15000   1.000 89.34000  ? 497 PHE D O   1 
ATOM   3529 C CB  . PHE D 2 165 ? 45.57900 6.33000   3.68500   1.000 92.17000  ? 497 PHE D CB  1 
ATOM   3530 C CG  . PHE D 2 165 ? 44.48600 6.09000   2.66800   1.000 90.44000  ? 497 PHE D CG  1 
ATOM   3531 C CD1 . PHE D 2 165 ? 43.89500 4.83400   2.54200   1.000 86.59000  ? 497 PHE D CD1 1 
ATOM   3532 C CD2 . PHE D 2 165 ? 44.03100 7.12100   1.85800   1.000 86.20000  ? 497 PHE D CD2 1 
ATOM   3533 C CE1 . PHE D 2 165 ? 42.88300 4.61000   1.61900   1.000 78.70000  ? 497 PHE D CE1 1 
ATOM   3534 C CE2 . PHE D 2 165 ? 43.01800 6.90100   0.94500   1.000 83.26000  ? 497 PHE D CE2 1 
ATOM   3535 C CZ  . PHE D 2 165 ? 42.44600 5.64100   0.82800   1.000 80.31000  ? 497 PHE D CZ  1 
ATOM   3536 N N   . GLN D 2 166 ? 46.79200 4.29100   6.22800   1.000 89.28000  ? 498 GLN D N   1 
ATOM   3537 C CA  . GLN D 2 166 ? 48.04100 3.94100   6.94500   1.000 93.54000  ? 498 GLN D CA  1 
ATOM   3538 C C   . GLN D 2 166 ? 48.73700 2.84400   6.14500   1.000 93.93000  ? 498 GLN D C   1 
ATOM   3539 O O   . GLN D 2 166 ? 48.02500 2.04800   5.50100   1.000 93.70000  ? 498 GLN D O   1 
ATOM   3540 C CB  . GLN D 2 166 ? 47.72500 3.41400   8.34200   1.000 98.06000  ? 498 GLN D CB  1 
ATOM   3541 C CG  . GLN D 2 166 ? 47.31100 4.49500   9.32500   1.000 95.67000  ? 498 GLN D CG  1 
ATOM   3542 C CD  . GLN D 2 166 ? 47.05600 3.93000   10.70000  1.000 95.78000  ? 498 GLN D CD  1 
ATOM   3543 O OE1 . GLN D 2 166 ? 46.78200 2.74400   10.86700  1.000 96.66000  ? 498 GLN D OE1 1 
ATOM   3544 N NE2 . GLN D 2 166 ? 47.15400 4.78500   11.70600  1.000 101.64000 ? 498 GLN D NE2 1 
ATOM   3545 N N   . PRO D 2 167 ? 50.08800 2.73600   6.12700   1.000 93.09000  ? 499 PRO D N   1 
ATOM   3546 C CA  . PRO D 2 167 ? 50.74300 1.61800   5.44500   1.000 94.09000  ? 499 PRO D CA  1 
ATOM   3547 C C   . PRO D 2 167 ? 50.54200 0.35000   6.28500   1.000 94.86000  ? 499 PRO D C   1 
ATOM   3548 O O   . PRO D 2 167 ? 51.38000 -0.52900  6.21900   1.000 98.27000  ? 499 PRO D O   1 
ATOM   3549 C CB  . PRO D 2 167 ? 52.21900 2.02600   5.41600   1.000 97.44000  ? 499 PRO D CB  1 
ATOM   3550 C CG  . PRO D 2 167 ? 52.37400 2.90000   6.63900   1.000 93.64000  ? 499 PRO D CG  1 
ATOM   3551 C CD  . PRO D 2 167 ? 51.06700 3.65500   6.73400   1.000 91.81000  ? 499 PRO D CD  1 
ATOM   3552 N N   . THR D 2 168 ? 49.44700 0.29000   7.05000   1.000 100.55000 ? 500 THR D N   1 
ATOM   3553 C CA  . THR D 2 168 ? 49.17900 -0.86900  7.93900   1.000 98.17000  ? 500 THR D CA  1 
ATOM   3554 C C   . THR D 2 168 ? 47.75600 -1.38200  7.70400   1.000 98.89000  ? 500 THR D C   1 
ATOM   3555 O O   . THR D 2 168 ? 47.19300 -1.99200  8.63400   1.000 102.16000 ? 500 THR D O   1 
ATOM   3556 C CB  . THR D 2 168 ? 49.35900 -0.46900  9.40700   1.000 100.66000 ? 500 THR D CB  1 
ATOM   3557 O OG1 . THR D 2 168 ? 48.21100 0.28800   9.79200   1.000 105.76000 ? 500 THR D OG1 1 
ATOM   3558 C CG2 . THR D 2 168 ? 50.60900 0.34800   9.64800   1.000 97.39000  ? 500 THR D CG2 1 
ATOM   3559 N N   . TYR D 2 169 ? 47.19400 -1.13800  6.51600   1.000 98.71000  ? 501 TYR D N   1 
ATOM   3560 C CA  . TYR D 2 169 ? 45.79200 -1.54300  6.23700   1.000 94.43000  ? 501 TYR D CA  1 
ATOM   3561 C C   . TYR D 2 169 ? 45.76300 -2.64700  5.18200   1.000 92.11000  ? 501 TYR D C   1 
ATOM   3562 O O   . TYR D 2 169 ? 46.63900 -2.63800  4.29400   1.000 97.63000  ? 501 TYR D O   1 
ATOM   3563 C CB  . TYR D 2 169 ? 44.97800 -0.35200  5.72800   1.000 87.75000  ? 501 TYR D CB  1 
ATOM   3564 C CG  . TYR D 2 169 ? 44.65800 0.69900   6.76100   1.000 94.65000  ? 501 TYR D CG  1 
ATOM   3565 C CD1 . TYR D 2 169 ? 45.08100 0.56900   8.07300   1.000 99.19000  ? 501 TYR D CD1 1 
ATOM   3566 C CD2 . TYR D 2 169 ? 43.93000 1.82700   6.42400   1.000 89.95000  ? 501 TYR D CD2 1 
ATOM   3567 C CE1 . TYR D 2 169 ? 44.78800 1.53100   9.02400   1.000 99.97000  ? 501 TYR D CE1 1 
ATOM   3568 C CE2 . TYR D 2 169 ? 43.62600 2.79800   7.36200   1.000 93.53000  ? 501 TYR D CE2 1 
ATOM   3569 C CZ  . TYR D 2 169 ? 44.06000 2.65100   8.66700   1.000 97.11000  ? 501 TYR D CZ  1 
ATOM   3570 O OH  . TYR D 2 169 ? 43.76700 3.60400   9.59700   1.000 107.73000 ? 501 TYR D OH  1 
ATOM   3571 N N   . GLY D 2 170 ? 44.79400 -3.56600  5.26900   1.000 88.01000  ? 502 GLY D N   1 
ATOM   3572 C CA  . GLY D 2 170 ? 44.64900 -4.57400  4.23900   1.000 87.51000  ? 502 GLY D CA  1 
ATOM   3573 C C   . GLY D 2 170 ? 44.68900 -3.93300  2.86700   1.000 93.95000  ? 502 GLY D C   1 
ATOM   3574 O O   . GLY D 2 170 ? 44.29600 -2.77700  2.68400   1.000 93.48000  ? 502 GLY D O   1 
ATOM   3575 N N   . VAL D 2 171 ? 45.20000 -4.68000  1.89200   1.000 90.66000  ? 503 VAL D N   1 
ATOM   3576 C CA  . VAL D 2 171 ? 45.32500 -4.12200  0.55200   1.000 91.81000  ? 503 VAL D CA  1 
ATOM   3577 C C   . VAL D 2 171 ? 43.99900 -3.52200  0.10400   1.000 93.30000  ? 503 VAL D C   1 
ATOM   3578 O O   . VAL D 2 171 ? 43.96600 -2.43400  -0.47900  1.000 89.76000  ? 503 VAL D O   1 
ATOM   3579 C CB  . VAL D 2 171 ? 45.83000 -5.19700  -0.42400  1.000 98.40000  ? 503 VAL D CB  1 
ATOM   3580 C CG1 . VAL D 2 171 ? 45.92100 -4.64100  -1.84700  1.000 99.13000  ? 503 VAL D CG1 1 
ATOM   3581 C CG2 . VAL D 2 171 ? 47.18000 -5.72000  0.03500   1.000 101.69000 ? 503 VAL D CG2 1 
ATOM   3582 N N   . GLY D 2 172 ? 42.88500 -4.20200  0.41200   1.000 95.54000  ? 504 GLY D N   1 
ATOM   3583 C CA  . GLY D 2 172 ? 41.56400 -3.69500  0.06900   1.000 89.39000  ? 504 GLY D CA  1 
ATOM   3584 C C   . GLY D 2 172 ? 41.26200 -2.32800  0.64500   1.000 85.20000  ? 504 GLY D C   1 
ATOM   3585 O O   . GLY D 2 172 ? 40.36600 -1.63900  0.15600   1.000 85.31000  ? 504 GLY D O   1 
ATOM   3586 N N   . TYR D 2 173 ? 42.00000 -1.91200  1.65800   1.000 84.88000  ? 505 TYR D N   1 
ATOM   3587 C CA  . TYR D 2 173 ? 41.78800 -0.62900  2.30100   1.000 84.17000  ? 505 TYR D CA  1 
ATOM   3588 C C   . TYR D 2 173 ? 42.89600 0.35000   1.95400   1.000 81.22000  ? 505 TYR D C   1 
ATOM   3589 O O   . TYR D 2 173 ? 42.81800 1.52300   2.32900   1.000 78.40000  ? 505 TYR D O   1 
ATOM   3590 C CB  . TYR D 2 173 ? 41.65800 -0.83300  3.84000   1.000 91.58000  ? 505 TYR D CB  1 
ATOM   3591 C CG  . TYR D 2 173 ? 40.39800 -1.60800  4.20800   1.000 86.99000  ? 505 TYR D CG  1 
ATOM   3592 C CD1 . TYR D 2 173 ? 39.19300 -0.95200  4.38900   1.000 87.79000  ? 505 TYR D CD1 1 
ATOM   3593 C CD2 . TYR D 2 173 ? 40.39700 -2.99500  4.30400   1.000 84.14000  ? 505 TYR D CD2 1 
ATOM   3594 C CE1 . TYR D 2 173 ? 38.02500 -1.64200  4.67500   1.000 80.14000  ? 505 TYR D CE1 1 
ATOM   3595 C CE2 . TYR D 2 173 ? 39.21600 -3.70100  4.58700   1.000 75.84000  ? 505 TYR D CE2 1 
ATOM   3596 C CZ  . TYR D 2 173 ? 38.03800 -3.00800  4.76800   1.000 73.46000  ? 505 TYR D CZ  1 
ATOM   3597 O OH  . TYR D 2 173 ? 36.85900 -3.66500  5.04400   1.000 72.23000  ? 505 TYR D OH  1 
ATOM   3598 N N   . GLN D 2 174 ? 43.93100 -0.10100  1.25200   1.000 87.56000  ? 506 GLN D N   1 
ATOM   3599 C CA  . GLN D 2 174 ? 45.00700 0.79000   0.85400   1.000 87.50000  ? 506 GLN D CA  1 
ATOM   3600 C C   . GLN D 2 174 ? 44.51700 1.77400   -0.20900  1.000 83.84000  ? 506 GLN D C   1 
ATOM   3601 O O   . GLN D 2 174 ? 43.49700 1.53500   -0.86300  1.000 80.86000  ? 506 GLN D O   1 
ATOM   3602 C CB  . GLN D 2 174 ? 46.19000 -0.01700  0.33400   1.000 87.63000  ? 506 GLN D CB  1 
ATOM   3603 C CG  . GLN D 2 174 ? 46.71000 -1.00500  1.35700   1.000 93.65000  ? 506 GLN D CG  1 
ATOM   3604 C CD  . GLN D 2 174 ? 48.02700 -1.62400  0.95500   1.000 95.78000  ? 506 GLN D CD  1 
ATOM   3605 O OE1 . GLN D 2 174 ? 48.24600 -1.96000  -0.21300  1.000 92.18000  ? 506 GLN D OE1 1 
ATOM   3606 N NE2 . GLN D 2 174 ? 48.92000 -1.77500  1.92600   1.000 96.11000  ? 506 GLN D NE2 1 
ATOM   3607 N N   . PRO D 2 175 ? 45.21200 2.90300   -0.37900  1.000 83.68000  ? 507 PRO D N   1 
ATOM   3608 C CA  . PRO D 2 175 ? 44.76800 3.90200   -1.35600  1.000 81.92000  ? 507 PRO D CA  1 
ATOM   3609 C C   . PRO D 2 175 ? 45.20300 3.54700   -2.76300  1.000 83.50000  ? 507 PRO D C   1 
ATOM   3610 O O   . PRO D 2 175 ? 46.27800 2.98600   -2.98800  1.000 85.34000  ? 507 PRO D O   1 
ATOM   3611 C CB  . PRO D 2 175 ? 45.46300 5.18100   -0.88400  1.000 83.27000  ? 507 PRO D CB  1 
ATOM   3612 C CG  . PRO D 2 175 ? 46.75800 4.67700   -0.39700  1.000 87.60000  ? 507 PRO D CG  1 
ATOM   3613 C CD  . PRO D 2 175 ? 46.41900 3.36700   0.32800   1.000 87.21000  ? 507 PRO D CD  1 
ATOM   3614 N N   . TYR D 2 176 ? 44.35400 3.89600   -3.71600  1.000 85.23000  ? 508 TYR D N   1 
ATOM   3615 C CA  . TYR D 2 176 ? 44.65300 3.73800   -5.12900  1.000 81.79000  ? 508 TYR D CA  1 
ATOM   3616 C C   . TYR D 2 176 ? 44.36900 5.05500   -5.82300  1.000 80.65000  ? 508 TYR D C   1 
ATOM   3617 O O   . TYR D 2 176 ? 43.32300 5.66300   -5.58600  1.000 83.42000  ? 508 TYR D O   1 
ATOM   3618 C CB  . TYR D 2 176 ? 43.80500 2.62900   -5.74300  1.000 80.42000  ? 508 TYR D CB  1 
ATOM   3619 C CG  . TYR D 2 176 ? 44.27000 1.23500   -5.39700  1.000 88.55000  ? 508 TYR D CG  1 
ATOM   3620 C CD1 . TYR D 2 176 ? 44.23400 0.76200   -4.09300  1.000 81.05000  ? 508 TYR D CD1 1 
ATOM   3621 C CD2 . TYR D 2 176 ? 44.73300 0.38400   -6.38600  1.000 88.52000  ? 508 TYR D CD2 1 
ATOM   3622 C CE1 . TYR D 2 176 ? 44.64900 -0.53400  -3.79400  1.000 87.09000  ? 508 TYR D CE1 1 
ATOM   3623 C CE2 . TYR D 2 176 ? 45.15700 -0.90100  -6.09300  1.000 88.73000  ? 508 TYR D CE2 1 
ATOM   3624 C CZ  . TYR D 2 176 ? 45.11500 -1.35600  -4.81000  1.000 85.30000  ? 508 TYR D CZ  1 
ATOM   3625 O OH  . TYR D 2 176 ? 45.54000 -2.63900  -4.55800  1.000 84.46000  ? 508 TYR D OH  1 
ATOM   3626 N N   . ARG D 2 177 ? 45.29900 5.50400   -6.66000  1.000 84.49000  ? 509 ARG D N   1 
ATOM   3627 C CA  . ARG D 2 177 ? 45.03800 6.65900   -7.50900  1.000 82.28000  ? 509 ARG D CA  1 
ATOM   3628 C C   . ARG D 2 177 ? 44.27200 6.21600   -8.74600  1.000 78.06000  ? 509 ARG D C   1 
ATOM   3629 O O   . ARG D 2 177 ? 44.48900 5.12800   -9.28000  1.000 78.15000  ? 509 ARG D O   1 
ATOM   3630 C CB  . ARG D 2 177 ? 46.34200 7.36200   -7.88800  1.000 83.20000  ? 509 ARG D CB  1 
ATOM   3631 C CG  . ARG D 2 177 ? 47.07300 7.85400   -6.64900  1.000 80.04000  ? 509 ARG D CG  1 
ATOM   3632 C CD  . ARG D 2 177 ? 48.25400 8.72900   -6.95200  1.000 79.60000  ? 509 ARG D CD  1 
ATOM   3633 N NE  . ARG D 2 177 ? 48.54800 9.56100   -5.78800  1.000 83.04000  ? 509 ARG D NE  1 
ATOM   3634 C CZ  . ARG D 2 177 ? 49.47800 10.50600  -5.75700  1.000 82.82000  ? 509 ARG D CZ  1 
ATOM   3635 N NH1 . ARG D 2 177 ? 50.21300 10.74900  -6.83200  1.000 80.57000  ? 509 ARG D NH1 1 
ATOM   3636 N NH2 . ARG D 2 177 ? 49.65800 11.21800  -4.65500  1.000 82.25000  ? 509 ARG D NH2 1 
ATOM   3637 N N   . VAL D 2 178 ? 43.33200 7.03800   -9.16900  1.000 75.52000  ? 510 VAL D N   1 
ATOM   3638 C CA  . VAL D 2 178 ? 42.40000 6.66500   -10.21200 1.000 74.49000  ? 510 VAL D CA  1 
ATOM   3639 C C   . VAL D 2 178 ? 42.37400 7.78100   -11.23400 1.000 80.70000  ? 510 VAL D C   1 
ATOM   3640 O O   . VAL D 2 178 ? 42.24300 8.95300   -10.86300 1.000 82.46000  ? 510 VAL D O   1 
ATOM   3641 C CB  . VAL D 2 178 ? 40.99100 6.41800   -9.65400  1.000 77.75000  ? 510 VAL D CB  1 
ATOM   3642 C CG1 . VAL D 2 178 ? 39.99500 6.25200   -10.78600 1.000 71.95000  ? 510 VAL D CG1 1 
ATOM   3643 C CG2 . VAL D 2 178 ? 40.98500 5.18400   -8.79300  1.000 80.00000  ? 510 VAL D CG2 1 
ATOM   3644 N N   . VAL D 2 179 ? 42.53100 7.42200   -12.51300 1.000 75.24000  ? 511 VAL D N   1 
ATOM   3645 C CA  . VAL D 2 179 ? 42.37200 8.35800   -13.61600 1.000 69.24000  ? 511 VAL D CA  1 
ATOM   3646 C C   . VAL D 2 179 ? 41.31900 7.81000   -14.56400 1.000 72.18000  ? 511 VAL D C   1 
ATOM   3647 O O   . VAL D 2 179 ? 41.40200 6.65400   -14.99300 1.000 73.78000  ? 511 VAL D O   1 
ATOM   3648 C CB  . VAL D 2 179 ? 43.68600 8.61000   -14.36200 1.000 75.94000  ? 511 VAL D CB  1 
ATOM   3649 C CG1 . VAL D 2 179 ? 43.42300 9.49600   -15.57700 1.000 77.97000  ? 511 VAL D CG1 1 
ATOM   3650 C CG2 . VAL D 2 179 ? 44.67800 9.24900   -13.42300 1.000 75.19000  ? 511 VAL D CG2 1 
ATOM   3651 N N   . VAL D 2 180 ? 40.30100 8.61800   -14.83200 1.000 76.53000  ? 512 VAL D N   1 
ATOM   3652 C CA  . VAL D 2 180 ? 39.24500 8.29400   -15.78000 1.000 76.97000  ? 512 VAL D CA  1 
ATOM   3653 C C   . VAL D 2 180 ? 39.40500 9.22400   -16.97200 1.000 72.47000  ? 512 VAL D C   1 
ATOM   3654 O O   . VAL D 2 180 ? 39.64900 10.42700  -16.80500 1.000 72.45000  ? 512 VAL D O   1 
ATOM   3655 C CB  . VAL D 2 180 ? 37.84500 8.42300   -15.15600 1.000 77.12000  ? 512 VAL D CB  1 
ATOM   3656 C CG1 . VAL D 2 180 ? 36.78500 8.18500   -16.21100 1.000 73.90000  ? 512 VAL D CG1 1 
ATOM   3657 C CG2 . VAL D 2 180 ? 37.67400 7.43000   -14.01300 1.000 72.28000  ? 512 VAL D CG2 1 
ATOM   3658 N N   . LEU D 2 181 ? 39.31200 8.65800   -18.16700 1.000 77.29000  ? 513 LEU D N   1 
ATOM   3659 C CA  . LEU D 2 181 ? 39.43100 9.39600   -19.41700 1.000 67.89000  ? 513 LEU D CA  1 
ATOM   3660 C C   . LEU D 2 181 ? 38.09800 9.36100   -20.14500 1.000 69.74000  ? 513 LEU D C   1 
ATOM   3661 O O   . LEU D 2 181 ? 37.56200 8.28000   -20.40300 1.000 73.68000  ? 513 LEU D O   1 
ATOM   3662 C CB  . LEU D 2 181 ? 40.52100 8.79600   -20.29600 1.000 66.04000  ? 513 LEU D CB  1 
ATOM   3663 C CG  . LEU D 2 181 ? 41.88600 8.63700   -19.64100 1.000 67.50000  ? 513 LEU D CG  1 
ATOM   3664 C CD1 . LEU D 2 181 ? 42.74800 7.80800   -20.56600 1.000 68.78000  ? 513 LEU D CD1 1 
ATOM   3665 C CD2 . LEU D 2 181 ? 42.53800 9.97800   -19.34300 1.000 64.83000  ? 513 LEU D CD2 1 
ATOM   3666 N N   . SER D 2 182 ? 37.56100 10.53000  -20.46600 1.000 71.64000  ? 514 SER D N   1 
ATOM   3667 C CA  . SER D 2 182 ? 36.37800 10.62100  -21.31300 1.000 78.63000  ? 514 SER D CA  1 
ATOM   3668 C C   . SER D 2 182 ? 36.78000 11.00900  -22.74100 1.000 75.77000  ? 514 SER D C   1 
ATOM   3669 O O   . SER D 2 182 ? 37.59700 11.91100  -22.94700 1.000 75.07000  ? 514 SER D O   1 
ATOM   3670 C CB  . SER D 2 182 ? 35.38100 11.62700  -20.74100 1.000 71.31000  ? 514 SER D CB  1 
ATOM   3671 O OG  . SER D 2 182 ? 34.96600 11.24300  -19.45200 1.000 84.93000  ? 514 SER D OG  1 
ATOM   3672 N N   . PHE D 2 183 ? 36.21200 10.32300  -23.71700 1.000 76.81000  ? 515 PHE D N   1 
ATOM   3673 C CA  . PHE D 2 183 ? 36.53800 10.54900  -25.12800 1.000 80.17000  ? 515 PHE D CA  1 
ATOM   3674 C C   . PHE D 2 183 ? 35.36700 11.27200  -25.79300 1.000 77.34000  ? 515 PHE D C   1 
ATOM   3675 O O   . PHE D 2 183 ? 34.34100 10.66800  -26.10300 1.000 77.71000  ? 515 PHE D O   1 
ATOM   3676 C CB  . PHE D 2 183 ? 36.87200 9.22400   -25.79800 1.000 75.77000  ? 515 PHE D CB  1 
ATOM   3677 C CG  . PHE D 2 183 ? 38.05400 8.54500   -25.19000 1.000 80.89000  ? 515 PHE D CG  1 
ATOM   3678 C CD1 . PHE D 2 183 ? 39.27800 9.19600   -25.12500 1.000 80.41000  ? 515 PHE D CD1 1 
ATOM   3679 C CD2 . PHE D 2 183 ? 37.94200 7.27600   -24.64200 1.000 86.29000  ? 515 PHE D CD2 1 
ATOM   3680 C CE1 . PHE D 2 183 ? 40.38100 8.58200   -24.53300 1.000 83.14000  ? 515 PHE D CE1 1 
ATOM   3681 C CE2 . PHE D 2 183 ? 39.03600 6.65900   -24.05700 1.000 86.76000  ? 515 PHE D CE2 1 
ATOM   3682 C CZ  . PHE D 2 183 ? 40.25700 7.31800   -23.99800 1.000 79.10000  ? 515 PHE D CZ  1 
ATOM   3683 N N   . GLU D 2 184 ? 35.53200 12.57400  -26.00500 1.000 78.19000  ? 516 GLU D N   1 
ATOM   3684 C CA  . GLU D 2 184 ? 34.43900 13.46000  -26.38900 1.000 79.94000  ? 516 GLU D CA  1 
ATOM   3685 C C   . GLU D 2 184 ? 34.35700 13.52900  -27.91400 1.000 84.80000  ? 516 GLU D C   1 
ATOM   3686 O O   . GLU D 2 184 ? 35.16800 14.20600  -28.55700 1.000 81.58000  ? 516 GLU D O   1 
ATOM   3687 C CB  . GLU D 2 184 ? 34.67100 14.83600  -25.78200 1.000 80.74000  ? 516 GLU D CB  1 
ATOM   3688 C CG  . GLU D 2 184 ? 33.44000 15.68200  -25.58800 1.000 88.01000  ? 516 GLU D CG  1 
ATOM   3689 C CD  . GLU D 2 184 ? 33.80000 17.10900  -25.17800 1.000 91.36000  ? 516 GLU D CD  1 
ATOM   3690 O OE1 . GLU D 2 184 ? 34.95700 17.51900  -25.42900 1.000 86.10000  ? 516 GLU D OE1 1 
ATOM   3691 O OE2 . GLU D 2 184 ? 32.93200 17.82100  -24.61700 1.000 93.66000  ? 516 GLU D OE2 1 
ATOM   3692 N N   . LEU D 2 185 ? 33.38800 12.80800  -28.48700 1.000 88.66000  ? 517 LEU D N   1 
ATOM   3693 C CA  . LEU D 2 185 ? 33.10400 12.77500  -29.92200 1.000 85.15000  ? 517 LEU D CA  1 
ATOM   3694 C C   . LEU D 2 185 ? 31.90900 13.64500  -30.25800 1.000 89.68000  ? 517 LEU D C   1 
ATOM   3695 O O   . LEU D 2 185 ? 30.96400 13.18700  -30.90300 1.000 89.34000  ? 517 LEU D O   1 
ATOM   3696 C CB  . LEU D 2 185 ? 32.80400 11.35300  -30.39500 1.000 84.69000  ? 517 LEU D CB  1 
ATOM   3697 C CG  . LEU D 2 185 ? 33.99800 10.41700  -30.44500 1.000 91.26000  ? 517 LEU D CG  1 
ATOM   3698 C CD1 . LEU D 2 185 ? 33.55000 8.98400   -30.69500 1.000 93.20000  ? 517 LEU D CD1 1 
ATOM   3699 C CD2 . LEU D 2 185 ? 34.92900 10.91000  -31.54700 1.000 87.99000  ? 517 LEU D CD2 1 
ATOM   3700 N N   . LEU D 2 186 ? 31.90400 14.87100  -29.76600 1.000 88.05000  ? 518 LEU D N   1 
ATOM   3701 C CA  . LEU D 2 186 ? 30.89800 15.82600  -30.20100 1.000 91.03000  ? 518 LEU D CA  1 
ATOM   3702 C C   . LEU D 2 186 ? 31.17100 16.18100  -31.65800 1.000 100.15000 ? 518 LEU D C   1 
ATOM   3703 O O   . LEU D 2 186 ? 32.27600 15.98500  -32.17000 1.000 100.23000 ? 518 LEU D O   1 
ATOM   3704 C CB  . LEU D 2 186 ? 30.83100 17.03600  -29.26300 1.000 93.65000  ? 518 LEU D CB  1 
ATOM   3705 C CG  . LEU D 2 186 ? 31.93800 18.08300  -29.33000 1.000 92.02000  ? 518 LEU D CG  1 
ATOM   3706 C CD1 . LEU D 2 186 ? 31.36700 19.47400  -29.11100 1.000 94.03000  ? 518 LEU D CD1 1 
ATOM   3707 C CD2 . LEU D 2 186 ? 33.00400 17.79200  -28.29800 1.000 88.90000  ? 518 LEU D CD2 1 
ATOM   3708 N N   . HIS D 2 187 ? 30.13800 16.69200  -32.32900 1.000 97.81000  ? 519 HIS D N   1 
ATOM   3709 C CA  . HIS D 2 187 ? 30.25200 17.07500  -33.73200 1.000 91.86000  ? 519 HIS D CA  1 
ATOM   3710 C C   . HIS D 2 187 ? 31.15900 18.29700  -33.79600 1.000 91.17000  ? 519 HIS D C   1 
ATOM   3711 O O   . HIS D 2 187 ? 30.68500 19.43700  -33.75700 1.000 85.04000  ? 519 HIS D O   1 
ATOM   3712 C CB  . HIS D 2 187 ? 28.87300 17.37500  -34.32800 1.000 86.18000  ? 519 HIS D CB  1 
ATOM   3713 C CG  . HIS D 2 187 ? 28.00400 16.16200  -34.48100 1.000 90.14000  ? 519 HIS D CG  1 
ATOM   3714 N ND1 . HIS D 2 187 ? 26.63100 16.21300  -34.38400 1.000 93.10000  ? 519 HIS D ND1 1 
ATOM   3715 C CD2 . HIS D 2 187 ? 28.31400 14.86700  -34.72900 1.000 96.97000  ? 519 HIS D CD2 1 
ATOM   3716 C CE1 . HIS D 2 187 ? 26.13200 15.00300  -34.56200 1.000 94.57000  ? 519 HIS D CE1 1 
ATOM   3717 N NE2 . HIS D 2 187 ? 27.13300 14.16700  -34.77300 1.000 99.52000  ? 519 HIS D NE2 1 
ATOM   3718 N N   . ALA D 2 188 ? 32.46900 18.06100  -33.89500 1.000 92.38000  ? 520 ALA D N   1 
ATOM   3719 C CA  . ALA D 2 188 ? 33.47700 19.10100  -33.76200 1.000 87.76000  ? 520 ALA D CA  1 
ATOM   3720 C C   . ALA D 2 188 ? 34.75900 18.63500  -34.45900 1.000 80.73000  ? 520 ALA D C   1 
ATOM   3721 O O   . ALA D 2 188 ? 34.90400 17.44100  -34.74800 1.000 82.94000  ? 520 ALA D O   1 
ATOM   3722 C CB  . ALA D 2 188 ? 33.74700 19.41900  -32.28200 1.000 97.15000  ? 520 ALA D CB  1 
ATOM   3723 N N   . PRO D 2 189 ? 35.69100 19.55300  -34.74900 1.000 78.96000  ? 521 PRO D N   1 
ATOM   3724 C CA  . PRO D 2 189 ? 36.89000 19.18200  -35.53200 1.000 87.27000  ? 521 PRO D CA  1 
ATOM   3725 C C   . PRO D 2 189 ? 37.61000 17.93200  -35.04200 1.000 90.58000  ? 521 PRO D C   1 
ATOM   3726 O O   . PRO D 2 189 ? 38.16900 17.20800  -35.87600 1.000 99.56000  ? 521 PRO D O   1 
ATOM   3727 C CB  . PRO D 2 189 ? 37.76900 20.43700  -35.43300 1.000 83.84000  ? 521 PRO D CB  1 
ATOM   3728 C CG  . PRO D 2 189 ? 36.87500 21.55300  -34.97200 1.000 84.15000  ? 521 PRO D CG  1 
ATOM   3729 C CD  . PRO D 2 189 ? 35.50300 21.01500  -34.71500 1.000 84.38000  ? 521 PRO D CD  1 
ATOM   3730 N N   . ALA D 2 190 ? 37.63000 17.67600  -33.73000 1.000 82.05000  ? 522 ALA D N   1 
ATOM   3731 C CA  . ALA D 2 190 ? 38.44600 16.63700  -33.10100 1.000 83.83000  ? 522 ALA D CA  1 
ATOM   3732 C C   . ALA D 2 190 ? 39.91500 17.04000  -33.03200 1.000 84.64000  ? 522 ALA D C   1 
ATOM   3733 O O   . ALA D 2 190 ? 40.57200 17.19600  -34.06700 1.000 80.36000  ? 522 ALA D O   1 
ATOM   3734 C CB  . ALA D 2 190 ? 38.34500 15.27600  -33.80400 1.000 74.99000  ? 522 ALA D CB  1 
ATOM   3735 N N   . THR D 2 191 ? 40.44000 17.20900  -31.81000 1.000 89.53000  ? 523 THR D N   1 
ATOM   3736 C CA  . THR D 2 191 ? 41.75900 17.78800  -31.58600 1.000 86.40000  ? 523 THR D CA  1 
ATOM   3737 C C   . THR D 2 191 ? 42.77800 16.83100  -30.98000 1.000 86.84000  ? 523 THR D C   1 
ATOM   3738 O O   . THR D 2 191 ? 43.97500 17.14400  -31.00100 1.000 87.10000  ? 523 THR D O   1 
ATOM   3739 C CB  . THR D 2 191 ? 41.65900 19.01600  -30.66700 1.000 89.06000  ? 523 THR D CB  1 
ATOM   3740 O OG1 . THR D 2 191 ? 41.39100 18.58700  -29.32600 1.000 84.17000  ? 523 THR D OG1 1 
ATOM   3741 C CG2 . THR D 2 191 ? 40.54700 19.94200  -31.12500 1.000 88.06000  ? 523 THR D CG2 1 
ATOM   3742 N N   . VAL D 2 192 ? 42.36100 15.70300  -30.41400 1.000 86.02000  ? 524 VAL D N   1 
ATOM   3743 C CA  . VAL D 2 192 ? 43.27700 14.76800  -29.76500 1.000 86.12000  ? 524 VAL D CA  1 
ATOM   3744 C C   . VAL D 2 192 ? 43.27400 13.47300  -30.56600 1.000 82.46000  ? 524 VAL D C   1 
ATOM   3745 O O   . VAL D 2 192 ? 42.21600 12.85900  -30.75500 1.000 83.09000  ? 524 VAL D O   1 
ATOM   3746 C CB  . VAL D 2 192 ? 42.89300 14.51500  -28.29500 1.000 81.47000  ? 524 VAL D CB  1 
ATOM   3747 C CG1 . VAL D 2 192 ? 44.05700 13.90600  -27.52500 1.000 82.14000  ? 524 VAL D CG1 1 
ATOM   3748 C CG2 . VAL D 2 192 ? 42.46600 15.79800  -27.64900 1.000 79.53000  ? 524 VAL D CG2 1 
ATOM   3749 N N   . CYS D 2 193 ? 44.43300 13.13700  -31.12300 1.000 82.18000  ? 525 CYS D N   1 
ATOM   3750 C CA  . CYS D 2 193 ? 44.46700 11.97800  -32.04000 1.000 87.56000  ? 525 CYS D CA  1 
ATOM   3751 C C   . CYS D 2 193 ? 45.49000 10.95100  -31.57200 1.000 85.02000  ? 525 CYS D C   1 
ATOM   3752 O O   . CYS D 2 193 ? 46.52000 11.35300  -31.00300 1.000 81.16000  ? 525 CYS D O   1 
ATOM   3753 C CB  . CYS D 2 193 ? 44.84700 12.45800  -33.43400 1.000 89.09000  ? 525 CYS D CB  1 
ATOM   3754 S SG  . CYS D 2 193 ? 43.45600 13.12000  -34.38000 1.000 88.40000  ? 525 CYS D SG  1 
ATOM   3755 N N   . GLY D 2 194 ? 45.11700 9.68500   -31.63500 1.000 88.68000  ? 526 GLY D N   1 
ATOM   3756 C CA  . GLY D 2 194 ? 46.05600 8.63300   -31.38200 1.000 94.16000  ? 526 GLY D CA  1 
ATOM   3757 C C   . GLY D 2 194 ? 47.15700 8.68400   -32.40500 1.000 97.16000  ? 526 GLY D C   1 
ATOM   3758 O O   . GLY D 2 194 ? 47.02600 9.26300   -33.48800 1.000 101.28000 ? 526 GLY D O   1 
ATOM   3759 N N   . SER D 2 195 ? 48.26500 8.08200   -32.05600 1.000 96.60000  ? 527 SER D N   1 
ATOM   3760 C CA  . SER D 2 195 ? 49.43300 8.11600   -32.93100 1.000 102.96000 ? 527 SER D CA  1 
ATOM   3761 C C   . SER D 2 195 ? 49.24800 7.25500   -34.22900 1.000 103.98000 ? 527 SER D C   1 
ATOM   3762 O O   . SER D 2 195 ? 50.21800 6.56000   -34.58400 1.000 99.70000  ? 527 SER D O   1 
ATOM   3763 C CB  . SER D 2 195 ? 50.67500 7.65700   -32.15900 1.000 102.58000 ? 527 SER D CB  1 
ATOM   3764 O OG  . SER D 2 195 ? 50.40700 6.65200   -31.18600 1.000 98.70000  ? 527 SER D OG  1 
ATOM   3765 N N   . ASN D 2 196 ? 48.09400 7.31100   -34.92100 1.000 104.99000 ? 528 ASN D N   1 
ATOM   3766 C CA  . ASN D 2 196 ? 47.86700 6.69000   -36.24200 1.000 105.68000 ? 528 ASN D CA  1 
ATOM   3767 C C   . ASN D 2 196 ? 46.83100 7.52600   -37.01500 1.000 109.77000 ? 528 ASN D C   1 
ATOM   3768 O O   . ASN D 2 196 ? 45.88300 8.04200   -36.43000 1.000 109.73000 ? 528 ASN D O   1 
ATOM   3769 C CB  . ASN D 2 196 ? 47.38200 5.22200   -36.14400 1.000 100.15000 ? 528 ASN D CB  1 
ATOM   3770 C CG  . ASN D 2 196 ? 48.52200 4.20800   -35.91300 1.000 101.29000 ? 528 ASN D CG  1 
ATOM   3771 O OD1 . ASN D 2 196 ? 49.37600 4.39500   -35.06000 1.000 100.06000 ? 528 ASN D OD1 1 
ATOM   3772 N ND2 . ASN D 2 196 ? 48.50700 3.11200   -36.67100 1.000 102.57000 ? 528 ASN D ND2 1 
ATOM   3773 N N   . SER D 2 197 ? 47.01700 7.62300   -38.35600 1.000 111.28000 ? 529 SER D N   1 
ATOM   3774 C CA  . SER D 2 197 ? 46.24200 8.47900   -39.27800 1.000 110.87000 ? 529 SER D CA  1 
ATOM   3775 C C   . SER D 2 197 ? 46.30100 9.95400   -38.89400 1.000 112.47000 ? 529 SER D C   1 
ATOM   3776 O O   . SER D 2 197 ? 46.87600 10.77300  -39.61900 1.000 110.88000 ? 529 SER D O   1 
ATOM   3777 C CB  . SER D 2 197 ? 44.78300 8.02100   -39.37200 1.000 113.42000 ? 529 SER D CB  1 
ATOM   3778 O OG  . SER D 2 197 ? 44.05200 8.89400   -40.23200 1.000 123.96000 ? 529 SER D OG  1 
HETATM 3779 C C1  . NAG E 3 .   ? 58.18500 -12.38400 45.46300  1.000 112.37000 ? 601 NAG B C1  1 
HETATM 3780 C C2  . NAG E 3 .   ? 57.92700 -11.95100 46.90000  1.000 112.13000 ? 601 NAG B C2  1 
HETATM 3781 C C3  . NAG E 3 .   ? 58.53300 -10.56900 47.15000  1.000 115.66000 ? 601 NAG B C3  1 
HETATM 3782 C C4  . NAG E 3 .   ? 60.01800 -10.57100 46.80900  1.000 117.77000 ? 601 NAG B C4  1 
HETATM 3783 C C5  . NAG E 3 .   ? 60.23100 -11.05900 45.37700  1.000 117.90000 ? 601 NAG B C5  1 
HETATM 3784 C C6  . NAG E 3 .   ? 61.69100 -11.21200 45.01800  1.000 115.72000 ? 601 NAG B C6  1 
HETATM 3785 C C7  . NAG E 3 .   ? 56.01000 -12.23800 48.39800  1.000 110.03000 ? 601 NAG B C7  1 
HETATM 3786 C C8  . NAG E 3 .   ? 54.52200 -12.18800 48.52000  1.000 107.78000 ? 601 NAG B C8  1 
HETATM 3787 N N2  . NAG E 3 .   ? 56.50400 -11.95100 47.19100  1.000 105.97000 ? 601 NAG B N2  1 
HETATM 3788 O O3  . NAG E 3 .   ? 58.34800 -10.19300 48.51000  1.000 118.70000 ? 601 NAG B O3  1 
HETATM 3789 O O4  . NAG E 3 .   ? 60.55600 -9.25900  46.94900  1.000 115.84000 ? 601 NAG B O4  1 
HETATM 3790 O O5  . NAG E 3 .   ? 59.62000 -12.34900 45.19100  1.000 120.85000 ? 601 NAG B O5  1 
HETATM 3791 O O6  . NAG E 3 .   ? 61.90100 -12.33100 44.16800  1.000 111.07000 ? 601 NAG B O6  1 
HETATM 3792 O O7  . NAG E 3 .   ? 56.73400 -12.51900 49.35100  1.000 115.91000 ? 601 NAG B O7  1 
HETATM 3793 C C1  . NAG F 3 .   ? 55.46200 9.33200   -15.50600 1.000 104.68000 ? 601 NAG D C1  1 
HETATM 3794 C C2  . NAG F 3 .   ? 55.20700 9.21500   -17.01700 1.000 106.91000 ? 601 NAG D C2  1 
HETATM 3795 C C3  . NAG F 3 .   ? 55.93400 8.00000   -17.59500 1.000 112.28000 ? 601 NAG D C3  1 
HETATM 3796 C C4  . NAG F 3 .   ? 57.42300 8.11100   -17.29900 1.000 109.45000 ? 601 NAG D C4  1 
HETATM 3797 C C5  . NAG F 3 .   ? 57.62200 8.16300   -15.78800 1.000 114.85000 ? 601 NAG D C5  1 
HETATM 3798 C C6  . NAG F 3 .   ? 59.07100 8.31800   -15.38700 1.000 115.36000 ? 601 NAG D C6  1 
HETATM 3799 C C7  . NAG F 3 .   ? 53.28900 9.62000   -18.47700 1.000 103.91000 ? 601 NAG D C7  1 
HETATM 3800 C C8  . NAG F 3 .   ? 51.81100 9.50200   -18.64700 1.000 100.19000 ? 601 NAG D C8  1 
HETATM 3801 N N2  . NAG F 3 .   ? 53.78700 9.16300   -17.32400 1.000 103.31000 ? 601 NAG D N2  1 
HETATM 3802 O O3  . NAG F 3 .   ? 55.71000 7.91100   -19.00100 1.000 107.37000 ? 601 NAG D O3  1 
HETATM 3803 O O4  . NAG F 3 .   ? 58.15300 7.02800   -17.86900 1.000 111.87000 ? 601 NAG D O4  1 
HETATM 3804 O O5  . NAG F 3 .   ? 56.91400 9.29200   -15.24000 1.000 111.16000 ? 601 NAG D O5  1 
HETATM 3805 O O6  . NAG F 3 .   ? 59.19300 8.88200   -14.08900 1.000 104.34000 ? 601 NAG D O6  1 
HETATM 3806 O O7  . NAG F 3 .   ? 54.00500 10.10900  -19.34500 1.000 109.05000 ? 601 NAG D O7  1 
# 
