data_9EIB
# 
_entry.id   9EIB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EIB         pdb_00009eib 10.2210/pdb9eib/pdb 
WWPDB D_1000290535 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EIB 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Macro amylo with His-ADPR' 8R66 unspecified 
PDB 'ModTad2 apo'               8V3E unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              philip.kranzusch@gmail.com 
_pdbx_contact_author.name_first         Philip 
_pdbx_contact_author.name_last          Kranzusch 
_pdbx_contact_author.name_mi            J 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4943-733X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chang, R.B.'     1 0000-0001-6298-7005 
'Kranzusch, P.J.' 2 0000-0002-4943-733X 
# 
_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                     'TIR domains produce histidine-ADPR conjugates as immune signaling molecules in bacteria' 
_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 'Chang, R.B.'     1 0000-0001-6298-7005 
primary 'Kranzusch, P.J.' 2 0000-0002-4943-733X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Prophage anti-Thoeris 2 (ModTad2)' 9993.230 2   ? ? ? ? 
2 non-polymer syn 
;(2~{S})-3-[1-[(2~{R},3~{R},4~{S},5~{R})-5-[[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxymethyl]-3,4-bis(oxidanyl)oxolan-2-yl]imidazol-4-yl]-2-azanyl-propanoic acid
;
696.455  1   ? ? ? ? 
3 water       nat water 18.015   162 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMDSLNFGKALEALKEGKKVSREGWNGKGMFAYYVPGGVYKSQTDVIKNTFGEEVKYRPYLALKTVDNDIATWTPSVSDI
LAEDWNIVE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMDSLNFGKALEALKEGKKVSREGWNGKGMFAYYVPGGVYKSQTDVIKNTFGEEVKYRPYLALKTVDNDIATWTPSVSDI
LAEDWNIVE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(2~{S})-3-[1-[(2~{R},3~{R},4~{S},5~{R})-5-[[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxymethyl]-3,4-bis(oxidanyl)oxolan-2-yl]imidazol-4-yl]-2-azanyl-propanoic acid
;
Y65 
3 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  SER n 
1 2  MET n 
1 3  ASP n 
1 4  SER n 
1 5  LEU n 
1 6  ASN n 
1 7  PHE n 
1 8  GLY n 
1 9  LYS n 
1 10 ALA n 
1 11 LEU n 
1 12 GLU n 
1 13 ALA n 
1 14 LEU n 
1 15 LYS n 
1 16 GLU n 
1 17 GLY n 
1 18 LYS n 
1 19 LYS n 
1 20 VAL n 
1 21 SER n 
1 22 ARG n 
1 23 GLU n 
1 24 GLY n 
1 25 TRP n 
1 26 ASN n 
1 27 GLY n 
1 28 LYS n 
1 29 GLY n 
1 30 MET n 
1 31 PHE n 
1 32 ALA n 
1 33 TYR n 
1 34 TYR n 
1 35 VAL n 
1 36 PRO n 
1 37 GLY n 
1 38 GLY n 
1 39 VAL n 
1 40 TYR n 
1 41 LYS n 
1 42 SER n 
1 43 GLN n 
1 44 THR n 
1 45 ASP n 
1 46 VAL n 
1 47 ILE n 
1 48 LYS n 
1 49 ASN n 
1 50 THR n 
1 51 PHE n 
1 52 GLY n 
1 53 GLU n 
1 54 GLU n 
1 55 VAL n 
1 56 LYS n 
1 57 TYR n 
1 58 ARG n 
1 59 PRO n 
1 60 TYR n 
1 61 LEU n 
1 62 ALA n 
1 63 LEU n 
1 64 LYS n 
1 65 THR n 
1 66 VAL n 
1 67 ASP n 
1 68 ASN n 
1 69 ASP n 
1 70 ILE n 
1 71 ALA n 
1 72 THR n 
1 73 TRP n 
1 74 THR n 
1 75 PRO n 
1 76 SER n 
1 77 VAL n 
1 78 SER n 
1 79 ASP n 
1 80 ILE n 
1 81 LEU n 
1 82 ALA n 
1 83 GLU n 
1 84 ASP n 
1 85 TRP n 
1 86 ASN n 
1 87 ILE n 
1 88 VAL n 
1 89 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   89 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Myroides odoratus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     256 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'        133.103 
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  
HOH non-polymer         . WATER ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'       117.146 
Y65 non-polymer         . 
;(2~{S})-3-[1-[(2~{R},3~{R},4~{S},5~{R})-5-[[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxymethyl]-3,4-bis(oxidanyl)oxolan-2-yl]imidazol-4-yl]-2-azanyl-propanoic acid
;
? 'C21 H30 N8 O15 P2' 696.455 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  SER 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  ?  ?   ?   A . n 
A 1 3  ASP 3  2  ?  ?   ?   A . n 
A 1 4  SER 4  3  3  SER SER A . n 
A 1 5  LEU 5  4  4  LEU LEU A . n 
A 1 6  ASN 6  5  5  ASN ASN A . n 
A 1 7  PHE 7  6  6  PHE PHE A . n 
A 1 8  GLY 8  7  7  GLY GLY A . n 
A 1 9  LYS 9  8  8  LYS LYS A . n 
A 1 10 ALA 10 9  9  ALA ALA A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 GLU 12 11 11 GLU GLU A . n 
A 1 13 ALA 13 12 12 ALA ALA A . n 
A 1 14 LEU 14 13 13 LEU LEU A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 GLU 16 15 15 GLU GLU A . n 
A 1 17 GLY 17 16 16 GLY GLY A . n 
A 1 18 LYS 18 17 17 LYS LYS A . n 
A 1 19 LYS 19 18 18 LYS LYS A . n 
A 1 20 VAL 20 19 19 VAL VAL A . n 
A 1 21 SER 21 20 20 SER SER A . n 
A 1 22 ARG 22 21 21 ARG ARG A . n 
A 1 23 GLU 23 22 22 GLU GLU A . n 
A 1 24 GLY 24 23 23 GLY GLY A . n 
A 1 25 TRP 25 24 24 TRP TRP A . n 
A 1 26 ASN 26 25 25 ASN ASN A . n 
A 1 27 GLY 27 26 26 GLY GLY A . n 
A 1 28 LYS 28 27 27 LYS LYS A . n 
A 1 29 GLY 29 28 28 GLY GLY A . n 
A 1 30 MET 30 29 29 MET MET A . n 
A 1 31 PHE 31 30 30 PHE PHE A . n 
A 1 32 ALA 32 31 31 ALA ALA A . n 
A 1 33 TYR 33 32 32 TYR TYR A . n 
A 1 34 TYR 34 33 33 TYR TYR A . n 
A 1 35 VAL 35 34 34 VAL VAL A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 GLY 37 36 36 GLY GLY A . n 
A 1 38 GLY 38 37 37 GLY GLY A . n 
A 1 39 VAL 39 38 38 VAL VAL A . n 
A 1 40 TYR 40 39 39 TYR TYR A . n 
A 1 41 LYS 41 40 40 LYS LYS A . n 
A 1 42 SER 42 41 41 SER SER A . n 
A 1 43 GLN 43 42 42 GLN GLN A . n 
A 1 44 THR 44 43 43 THR THR A . n 
A 1 45 ASP 45 44 44 ASP ASP A . n 
A 1 46 VAL 46 45 45 VAL VAL A . n 
A 1 47 ILE 47 46 46 ILE ILE A . n 
A 1 48 LYS 48 47 47 LYS LYS A . n 
A 1 49 ASN 49 48 48 ASN ASN A . n 
A 1 50 THR 50 49 49 THR THR A . n 
A 1 51 PHE 51 50 50 PHE PHE A . n 
A 1 52 GLY 52 51 51 GLY GLY A . n 
A 1 53 GLU 53 52 52 GLU GLU A . n 
A 1 54 GLU 54 53 53 GLU GLU A . n 
A 1 55 VAL 55 54 54 VAL VAL A . n 
A 1 56 LYS 56 55 55 LYS LYS A . n 
A 1 57 TYR 57 56 56 TYR TYR A . n 
A 1 58 ARG 58 57 57 ARG ARG A . n 
A 1 59 PRO 59 58 58 PRO PRO A . n 
A 1 60 TYR 60 59 59 TYR TYR A . n 
A 1 61 LEU 61 60 60 LEU LEU A . n 
A 1 62 ALA 62 61 61 ALA ALA A . n 
A 1 63 LEU 63 62 62 LEU LEU A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 THR 65 64 64 THR THR A . n 
A 1 66 VAL 66 65 65 VAL VAL A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 ASN 68 67 67 ASN ASN A . n 
A 1 69 ASP 69 68 68 ASP ASP A . n 
A 1 70 ILE 70 69 69 ILE ILE A . n 
A 1 71 ALA 71 70 70 ALA ALA A . n 
A 1 72 THR 72 71 71 THR THR A . n 
A 1 73 TRP 73 72 72 TRP TRP A . n 
A 1 74 THR 74 73 73 THR THR A . n 
A 1 75 PRO 75 74 74 PRO PRO A . n 
A 1 76 SER 76 75 75 SER SER A . n 
A 1 77 VAL 77 76 76 VAL VAL A . n 
A 1 78 SER 78 77 77 SER SER A . n 
A 1 79 ASP 79 78 78 ASP ASP A . n 
A 1 80 ILE 80 79 79 ILE ILE A . n 
A 1 81 LEU 81 80 80 LEU LEU A . n 
A 1 82 ALA 82 81 81 ALA ALA A . n 
A 1 83 GLU 83 82 82 GLU GLU A . n 
A 1 84 ASP 84 83 83 ASP ASP A . n 
A 1 85 TRP 85 84 84 TRP TRP A . n 
A 1 86 ASN 86 85 85 ASN ASN A . n 
A 1 87 ILE 87 86 86 ILE ILE A . n 
A 1 88 VAL 88 87 87 VAL VAL A . n 
A 1 89 GLU 89 88 88 GLU GLU A . n 
B 1 1  SER 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  ?  ?   ?   B . n 
B 1 3  ASP 3  2  2  ASP ASP B . n 
B 1 4  SER 4  3  3  SER SER B . n 
B 1 5  LEU 5  4  4  LEU LEU B . n 
B 1 6  ASN 6  5  5  ASN ASN B . n 
B 1 7  PHE 7  6  6  PHE PHE B . n 
B 1 8  GLY 8  7  7  GLY GLY B . n 
B 1 9  LYS 9  8  8  LYS LYS B . n 
B 1 10 ALA 10 9  9  ALA ALA B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 GLU 12 11 11 GLU GLU B . n 
B 1 13 ALA 13 12 12 ALA ALA B . n 
B 1 14 LEU 14 13 13 LEU LEU B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 GLU 16 15 15 GLU GLU B . n 
B 1 17 GLY 17 16 16 GLY GLY B . n 
B 1 18 LYS 18 17 17 LYS LYS B . n 
B 1 19 LYS 19 18 18 LYS LYS B . n 
B 1 20 VAL 20 19 19 VAL VAL B . n 
B 1 21 SER 21 20 20 SER SER B . n 
B 1 22 ARG 22 21 21 ARG ARG B . n 
B 1 23 GLU 23 22 22 GLU GLU B . n 
B 1 24 GLY 24 23 23 GLY GLY B . n 
B 1 25 TRP 25 24 24 TRP TRP B . n 
B 1 26 ASN 26 25 25 ASN ASN B . n 
B 1 27 GLY 27 26 26 GLY GLY B . n 
B 1 28 LYS 28 27 27 LYS LYS B . n 
B 1 29 GLY 29 28 28 GLY GLY B . n 
B 1 30 MET 30 29 29 MET MET B . n 
B 1 31 PHE 31 30 30 PHE PHE B . n 
B 1 32 ALA 32 31 31 ALA ALA B . n 
B 1 33 TYR 33 32 32 TYR TYR B . n 
B 1 34 TYR 34 33 33 TYR TYR B . n 
B 1 35 VAL 35 34 34 VAL VAL B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 GLY 37 36 36 GLY GLY B . n 
B 1 38 GLY 38 37 37 GLY GLY B . n 
B 1 39 VAL 39 38 38 VAL VAL B . n 
B 1 40 TYR 40 39 39 TYR TYR B . n 
B 1 41 LYS 41 40 40 LYS LYS B . n 
B 1 42 SER 42 41 41 SER SER B . n 
B 1 43 GLN 43 42 42 GLN GLN B . n 
B 1 44 THR 44 43 43 THR THR B . n 
B 1 45 ASP 45 44 44 ASP ASP B . n 
B 1 46 VAL 46 45 45 VAL VAL B . n 
B 1 47 ILE 47 46 46 ILE ILE B . n 
B 1 48 LYS 48 47 47 LYS LYS B . n 
B 1 49 ASN 49 48 48 ASN ASN B . n 
B 1 50 THR 50 49 49 THR THR B . n 
B 1 51 PHE 51 50 50 PHE PHE B . n 
B 1 52 GLY 52 51 51 GLY GLY B . n 
B 1 53 GLU 53 52 52 GLU GLU B . n 
B 1 54 GLU 54 53 53 GLU GLU B . n 
B 1 55 VAL 55 54 54 VAL VAL B . n 
B 1 56 LYS 56 55 55 LYS LYS B . n 
B 1 57 TYR 57 56 56 TYR TYR B . n 
B 1 58 ARG 58 57 57 ARG ARG B . n 
B 1 59 PRO 59 58 58 PRO PRO B . n 
B 1 60 TYR 60 59 59 TYR TYR B . n 
B 1 61 LEU 61 60 60 LEU LEU B . n 
B 1 62 ALA 62 61 61 ALA ALA B . n 
B 1 63 LEU 63 62 62 LEU LEU B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 THR 65 64 64 THR THR B . n 
B 1 66 VAL 66 65 65 VAL VAL B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 ASN 68 67 67 ASN ASN B . n 
B 1 69 ASP 69 68 68 ASP ASP B . n 
B 1 70 ILE 70 69 69 ILE ILE B . n 
B 1 71 ALA 71 70 70 ALA ALA B . n 
B 1 72 THR 72 71 71 THR THR B . n 
B 1 73 TRP 73 72 72 TRP TRP B . n 
B 1 74 THR 74 73 73 THR THR B . n 
B 1 75 PRO 75 74 74 PRO PRO B . n 
B 1 76 SER 76 75 75 SER SER B . n 
B 1 77 VAL 77 76 76 VAL VAL B . n 
B 1 78 SER 78 77 77 SER SER B . n 
B 1 79 ASP 79 78 78 ASP ASP B . n 
B 1 80 ILE 80 79 79 ILE ILE B . n 
B 1 81 LEU 81 80 80 LEU LEU B . n 
B 1 82 ALA 82 81 81 ALA ALA B . n 
B 1 83 GLU 83 82 82 GLU GLU B . n 
B 1 84 ASP 84 83 83 ASP ASP B . n 
B 1 85 TRP 85 84 84 TRP TRP B . n 
B 1 86 ASN 86 85 85 ASN ASN B . n 
B 1 87 ILE 87 86 86 ILE ILE B . n 
B 1 88 VAL 88 87 87 VAL VAL B . n 
B 1 89 GLU 89 88 88 GLU GLU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        Y65 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   Y65 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 Y65 1  101 101  Y65 XMO B . 
D 3 HOH 1  101 2023 HOH HOH A . 
D 3 HOH 2  102 1799 HOH HOH A . 
D 3 HOH 3  103 1520 HOH HOH A . 
D 3 HOH 4  104 1486 HOH HOH A . 
D 3 HOH 5  105 33   HOH HOH A . 
D 3 HOH 6  106 9    HOH HOH A . 
D 3 HOH 7  107 971  HOH HOH A . 
D 3 HOH 8  108 981  HOH HOH A . 
D 3 HOH 9  109 571  HOH HOH A . 
D 3 HOH 10 110 179  HOH HOH A . 
D 3 HOH 11 111 2029 HOH HOH A . 
D 3 HOH 12 112 113  HOH HOH A . 
D 3 HOH 13 113 83   HOH HOH A . 
D 3 HOH 14 114 6    HOH HOH A . 
D 3 HOH 15 115 510  HOH HOH A . 
D 3 HOH 16 116 35   HOH HOH A . 
D 3 HOH 17 117 521  HOH HOH A . 
D 3 HOH 18 118 87   HOH HOH A . 
D 3 HOH 19 119 519  HOH HOH A . 
D 3 HOH 20 120 1476 HOH HOH A . 
D 3 HOH 21 121 26   HOH HOH A . 
D 3 HOH 22 122 658  HOH HOH A . 
D 3 HOH 23 123 40   HOH HOH A . 
D 3 HOH 24 124 36   HOH HOH A . 
D 3 HOH 25 125 564  HOH HOH A . 
D 3 HOH 26 126 89   HOH HOH A . 
D 3 HOH 27 127 398  HOH HOH A . 
D 3 HOH 28 128 1984 HOH HOH A . 
D 3 HOH 29 129 42   HOH HOH A . 
D 3 HOH 30 130 515  HOH HOH A . 
D 3 HOH 31 131 527  HOH HOH A . 
D 3 HOH 32 132 90   HOH HOH A . 
D 3 HOH 33 133 73   HOH HOH A . 
D 3 HOH 34 134 1059 HOH HOH A . 
D 3 HOH 35 135 13   HOH HOH A . 
D 3 HOH 36 136 605  HOH HOH A . 
D 3 HOH 37 137 1153 HOH HOH A . 
D 3 HOH 38 138 890  HOH HOH A . 
D 3 HOH 39 139 60   HOH HOH A . 
D 3 HOH 40 140 37   HOH HOH A . 
D 3 HOH 41 141 1286 HOH HOH A . 
D 3 HOH 42 142 39   HOH HOH A . 
D 3 HOH 43 143 32   HOH HOH A . 
D 3 HOH 44 144 509  HOH HOH A . 
D 3 HOH 45 145 18   HOH HOH A . 
D 3 HOH 46 146 504  HOH HOH A . 
D 3 HOH 47 147 342  HOH HOH A . 
D 3 HOH 48 148 1525 HOH HOH A . 
D 3 HOH 49 149 64   HOH HOH A . 
D 3 HOH 50 150 38   HOH HOH A . 
D 3 HOH 51 151 236  HOH HOH A . 
D 3 HOH 52 152 783  HOH HOH A . 
D 3 HOH 53 153 486  HOH HOH A . 
D 3 HOH 54 154 232  HOH HOH A . 
D 3 HOH 55 155 133  HOH HOH A . 
D 3 HOH 56 156 54   HOH HOH A . 
D 3 HOH 57 157 2012 HOH HOH A . 
D 3 HOH 58 158 1289 HOH HOH A . 
D 3 HOH 59 159 41   HOH HOH A . 
D 3 HOH 60 160 2070 HOH HOH A . 
D 3 HOH 61 161 1912 HOH HOH A . 
D 3 HOH 62 162 447  HOH HOH A . 
D 3 HOH 63 163 118  HOH HOH A . 
D 3 HOH 64 164 75   HOH HOH A . 
D 3 HOH 65 165 957  HOH HOH A . 
D 3 HOH 66 166 1714 HOH HOH A . 
D 3 HOH 67 167 989  HOH HOH A . 
D 3 HOH 68 168 94   HOH HOH A . 
D 3 HOH 69 169 910  HOH HOH A . 
D 3 HOH 70 170 57   HOH HOH A . 
D 3 HOH 71 171 2074 HOH HOH A . 
D 3 HOH 72 172 818  HOH HOH A . 
D 3 HOH 73 173 991  HOH HOH A . 
E 3 HOH 1  201 2017 HOH HOH B . 
E 3 HOH 2  202 1970 HOH HOH B . 
E 3 HOH 3  203 1632 HOH HOH B . 
E 3 HOH 4  204 12   HOH HOH B . 
E 3 HOH 5  205 1795 HOH HOH B . 
E 3 HOH 6  206 148  HOH HOH B . 
E 3 HOH 7  207 562  HOH HOH B . 
E 3 HOH 8  208 390  HOH HOH B . 
E 3 HOH 9  209 1367 HOH HOH B . 
E 3 HOH 10 210 1445 HOH HOH B . 
E 3 HOH 11 211 25   HOH HOH B . 
E 3 HOH 12 212 575  HOH HOH B . 
E 3 HOH 13 213 14   HOH HOH B . 
E 3 HOH 14 214 213  HOH HOH B . 
E 3 HOH 15 215 55   HOH HOH B . 
E 3 HOH 16 216 76   HOH HOH B . 
E 3 HOH 17 217 77   HOH HOH B . 
E 3 HOH 18 218 58   HOH HOH B . 
E 3 HOH 19 219 131  HOH HOH B . 
E 3 HOH 20 220 1097 HOH HOH B . 
E 3 HOH 21 221 1173 HOH HOH B . 
E 3 HOH 22 222 1    HOH HOH B . 
E 3 HOH 23 223 16   HOH HOH B . 
E 3 HOH 24 224 678  HOH HOH B . 
E 3 HOH 25 225 52   HOH HOH B . 
E 3 HOH 26 226 1164 HOH HOH B . 
E 3 HOH 27 227 157  HOH HOH B . 
E 3 HOH 28 228 502  HOH HOH B . 
E 3 HOH 29 229 169  HOH HOH B . 
E 3 HOH 30 230 203  HOH HOH B . 
E 3 HOH 31 231 352  HOH HOH B . 
E 3 HOH 32 232 503  HOH HOH B . 
E 3 HOH 33 233 80   HOH HOH B . 
E 3 HOH 34 234 1825 HOH HOH B . 
E 3 HOH 35 235 10   HOH HOH B . 
E 3 HOH 36 236 205  HOH HOH B . 
E 3 HOH 37 237 139  HOH HOH B . 
E 3 HOH 38 238 43   HOH HOH B . 
E 3 HOH 39 239 22   HOH HOH B . 
E 3 HOH 40 240 508  HOH HOH B . 
E 3 HOH 41 241 30   HOH HOH B . 
E 3 HOH 42 242 354  HOH HOH B . 
E 3 HOH 43 243 331  HOH HOH B . 
E 3 HOH 44 244 15   HOH HOH B . 
E 3 HOH 45 245 1123 HOH HOH B . 
E 3 HOH 46 246 217  HOH HOH B . 
E 3 HOH 47 247 182  HOH HOH B . 
E 3 HOH 48 248 66   HOH HOH B . 
E 3 HOH 49 249 4    HOH HOH B . 
E 3 HOH 50 250 84   HOH HOH B . 
E 3 HOH 51 251 576  HOH HOH B . 
E 3 HOH 52 252 329  HOH HOH B . 
E 3 HOH 53 253 45   HOH HOH B . 
E 3 HOH 54 254 3    HOH HOH B . 
E 3 HOH 55 255 5    HOH HOH B . 
E 3 HOH 56 256 558  HOH HOH B . 
E 3 HOH 57 257 255  HOH HOH B . 
E 3 HOH 58 258 46   HOH HOH B . 
E 3 HOH 59 259 756  HOH HOH B . 
E 3 HOH 60 260 28   HOH HOH B . 
E 3 HOH 61 261 778  HOH HOH B . 
E 3 HOH 62 262 144  HOH HOH B . 
E 3 HOH 63 263 385  HOH HOH B . 
E 3 HOH 64 264 29   HOH HOH B . 
E 3 HOH 65 265 1328 HOH HOH B . 
E 3 HOH 66 266 135  HOH HOH B . 
E 3 HOH 67 267 222  HOH HOH B . 
E 3 HOH 68 268 552  HOH HOH B . 
E 3 HOH 69 269 1837 HOH HOH B . 
E 3 HOH 70 270 372  HOH HOH B . 
E 3 HOH 71 271 506  HOH HOH B . 
E 3 HOH 72 272 404  HOH HOH B . 
E 3 HOH 73 273 514  HOH HOH B . 
E 3 HOH 74 274 2065 HOH HOH B . 
E 3 HOH 75 275 618  HOH HOH B . 
E 3 HOH 76 276 675  HOH HOH B . 
E 3 HOH 77 277 156  HOH HOH B . 
E 3 HOH 78 278 107  HOH HOH B . 
E 3 HOH 79 279 1348 HOH HOH B . 
E 3 HOH 80 280 572  HOH HOH B . 
E 3 HOH 81 281 1315 HOH HOH B . 
E 3 HOH 82 282 597  HOH HOH B . 
E 3 HOH 83 283 19   HOH HOH B . 
E 3 HOH 84 284 1913 HOH HOH B . 
E 3 HOH 85 285 719  HOH HOH B . 
E 3 HOH 86 286 1417 HOH HOH B . 
E 3 HOH 87 287 1345 HOH HOH B . 
E 3 HOH 88 288 694  HOH HOH B . 
E 3 HOH 89 289 730  HOH HOH B . 
# 
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  ? ? ? 1.21_5207 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .         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                     9EIB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.692 
_cell.length_a_esd                 ? 
_cell.length_b                     92.692 
_cell.length_b_esd                 ? 
_cell.length_c                     78.079 
_cell.length_c_esd                 ? 
_cell.volume                       580964.212 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9EIB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                182 
_symmetry.space_group_name_Hall            'P 6c 2c' 
_symmetry.space_group_name_H-M             'P 63 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EIB 
_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             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.22 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M CH3COONa pH 4.4 and 24% PEG-4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_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         2024-06-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97934 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97934 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          21.57 
_reflns.entry_id                                       9EIB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.668 
_reflns.d_resolution_low                               30.341 
_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                                     16652 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                38.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15 
_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                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.668 
_reflns_shell.d_res_low                                     1.783 
_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                             834 
_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                                  0.783 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          58.9 
_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                               31.33 
_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                                 9EIB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.67 
_refine.ls_d_res_low                             30.34 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     16636 
_refine.ls_number_reflns_R_free                  855 
_refine.ls_number_reflns_R_work                  15781 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    70.46 
_refine.ls_percent_reflns_R_free                 5.14 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2093 
_refine.ls_R_factor_R_free                       0.2372 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2077 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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             1.1000 
_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                 31.4206 
_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                            0.1767 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.67 
_refine_hist.d_res_low                        30.34 
_refine_hist.number_atoms_solvent             162 
_refine_hist.number_atoms_total               1580 
_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        1372 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         46 
_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' ? 0.0073  ? 1516 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0112  ? 2071 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0572  ? 222  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0064  ? 250  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.3824 ? 524  ? 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' 1.67 1.77  . . 30  656  17.88 . . . . 0.3136 . . . . . . . . . . . 0.4062 
'X-RAY DIFFRACTION' 1.77 1.91  . . 87  1790 48.61 . . . . 0.2618 . . . . . . . . . . . 0.3161 
'X-RAY DIFFRACTION' 1.91 2.10  . . 131 2507 68.11 . . . . 0.2443 . . . . . . . . . . . 0.2943 
'X-RAY DIFFRACTION' 2.10 2.41  . . 175 3158 85.44 . . . . 0.2312 . . . . . . . . . . . 0.2574 
'X-RAY DIFFRACTION' 2.41 3.03  . . 225 3720 99.40 . . . . 0.2199 . . . . . . . . . . . 0.2641 
'X-RAY DIFFRACTION' 3.03 30.34 . . 207 3950 99.83 . . . . 0.1819 . . . . . . . . . . . 0.2002 
# 
_struct.entry_id                     9EIB 
_struct.title                        'Structure of Myroides odoratus prophage anti-Thoeris 2 (ModTad2) in complex with hisADPR' 
_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        9EIB 
_struct_keywords.text            'anti-thoeris, immune evasion, viral sponge, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9EIB 
_struct_ref.pdbx_db_accession          9EIB 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
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 9EIB A 1 ? 89 ? 9EIB 0 ? 88 ? 0 88 
2 1 9EIB B 1 ? 89 ? 9EIB 0 ? 88 ? 0 88 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 8170  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  16600 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z        1.0000000000 0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 10_555 -y,-x,-z+1/2 0.5000000000 -0.8660254038 0.0000000000 0.0000000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 39.0395000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASN A 6  ? GLU A 16 ? ASN A 5  GLU A 15 1 ? 11 
HELX_P HELX_P2 AA2 THR A 44 ? GLY A 52 ? THR A 43 GLY A 51 1 ? 9  
HELX_P HELX_P3 AA3 SER A 76 ? ALA A 82 ? SER A 75 ALA A 81 1 ? 7  
HELX_P HELX_P4 AA4 ASN B 6  ? GLU B 16 ? ASN B 5  GLU B 15 1 ? 11 
HELX_P HELX_P5 AA5 THR B 44 ? GLY B 52 ? THR B 43 GLY B 51 1 ? 9  
HELX_P HELX_P6 AA6 SER B 76 ? ALA B 82 ? SER B 75 ALA B 81 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 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 
AA2 1 2 ? anti-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 
AA6 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 LYS A 19 ? ARG A 22 ? LYS A 18 ARG A 21 
AA1 2 TRP A 85 ? VAL A 88 ? TRP A 84 VAL A 87 
AA2 1 PHE A 31 ? VAL A 35 ? PHE A 30 VAL A 34 
AA2 2 TYR A 60 ? LYS A 64 ? TYR A 59 LYS A 63 
AA2 3 ILE A 70 ? THR A 72 ? ILE A 69 THR A 71 
AA3 1 GLY A 38 ? LYS A 41 ? GLY A 37 LYS A 40 
AA3 2 GLU A 54 ? TYR A 57 ? GLU A 53 TYR A 56 
AA4 1 LYS B 19 ? ARG B 22 ? LYS B 18 ARG B 21 
AA4 2 TRP B 85 ? VAL B 88 ? TRP B 84 VAL B 87 
AA5 1 PHE B 31 ? VAL B 35 ? PHE B 30 VAL B 34 
AA5 2 TYR B 60 ? LYS B 64 ? TYR B 59 LYS B 63 
AA5 3 ILE B 70 ? THR B 72 ? ILE B 69 THR B 71 
AA6 1 GLY B 38 ? LYS B 41 ? GLY B 37 LYS B 40 
AA6 2 GLU B 54 ? TYR B 57 ? GLU B 53 TYR B 56 
# 
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 LYS A 19 ? N LYS A 18 O VAL A 88 ? O VAL A 87 
AA2 1 2 N PHE A 31 ? N PHE A 30 O LYS A 64 ? O LYS A 63 
AA2 2 3 N LEU A 63 ? N LEU A 62 O ALA A 71 ? O ALA A 70 
AA3 1 2 N TYR A 40 ? N TYR A 39 O VAL A 55 ? O VAL A 54 
AA4 1 2 N SER B 21 ? N SER B 20 O ASN B 86 ? O ASN B 85 
AA5 1 2 N TYR B 33 ? N TYR B 32 O ALA B 62 ? O ALA B 61 
AA5 2 3 N LEU B 63 ? N LEU B 62 O ALA B 71 ? O ALA B 70 
AA6 1 2 N GLY B 38 ? N GLY B 37 O TYR B 57 ? O TYR B 56 
# 
_pdbx_entry_details.entry_id                   9EIB 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 151 ? ? O A HOH 154 ? ? 1.61 
2  1 O   A HOH 159 ? ? O A HOH 163 ? ? 1.74 
3  1 O   B HOH 266 ? ? O B HOH 272 ? ? 1.82 
4  1 O   A HOH 103 ? ? O A HOH 104 ? ? 1.92 
5  1 O   B HOH 271 ? ? O B HOH 282 ? ? 1.93 
6  1 O   A HOH 160 ? ? O A HOH 166 ? ? 2.00 
7  1 O   B HOH 212 ? ? O B HOH 275 ? ? 2.02 
8  1 O   B HOH 202 ? ? O B HOH 221 ? ? 2.05 
9  1 O   B HOH 286 ? ? O B HOH 288 ? ? 2.10 
10 1 O   A HOH 172 ? ? O A HOH 173 ? ? 2.10 
11 1 OE1 B GLU 15  ? ? O B HOH 201 ? ? 2.12 
12 1 O   B HOH 212 ? ? O B HOH 231 ? ? 2.12 
13 1 O   B HOH 209 ? ? O B HOH 236 ? ? 2.12 
14 1 O   A PRO 74  ? ? O A HOH 101 ? ? 2.13 
15 1 OE2 A GLU 15  ? ? O A HOH 102 ? ? 2.15 
16 1 O   B SER 41  ? ? O B HOH 202 ? ? 2.17 
17 1 O   A HOH 156 ? ? O A HOH 168 ? ? 2.17 
18 1 O   A HOH 158 ? ? O A HOH 167 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 113 ? ? 1_555 O A HOH 113 ? ? 8_556  1.53 
2 1 O A HOH 139 ? ? 1_555 O A HOH 161 ? ? 10_555 1.89 
3 1 O B HOH 210 ? ? 1_555 O B HOH 242 ? ? 5_554  1.94 
4 1 O A HOH 101 ? ? 1_555 O A HOH 101 ? ? 10_555 2.14 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 273 ? E HOH . 
2 1 B HOH 279 ? E HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z         
2  x-y,x,z+1/2   
3  y,-x+y,z+1/2  
4  -y,x-y,z      
5  -x+y,-x,z     
6  x-y,-y,-z     
7  -x,-x+y,-z    
8  -x,-y,z+1/2   
9  y,x,-z        
10 -y,-x,-z+1/2  
11 -x+y,y,-z+1/2 
12 x,x-y,-z+1/2  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 12.0416251129 -0.827207369232 25.6827935057 0.198812438725 ? 0.0537968411064   ? -0.0536572965859 
? 0.269621656697 ? -0.24768449111    ? 0.540967521316  ? 0.0507117516428 ? -0.117220662035 ? -0.12708049082  ? 0.295575550131   ? 
0.336928253549  ? 0.391786266884 ? 0.0164277536956   ? -0.0254341764994  ? 0.0740442931258  ? -0.00675494150848 ? -0.0500883239769 
? 0.159354861713   ? -0.115234972576  ? -0.0829845766694  ? 0.0513186622158  ? 
2  'X-RAY DIFFRACTION' ? refined 20.0555111229 -4.2855305578   31.4105722362 0.206433954031 ? 0.00636112802419  ? 0.011336941595   
? 0.219573954659 ? -0.212307766695   ? 0.392541533328  ? 0.039156404218  ? 0.0318370835955 ? -0.092854185231 ? 1.91590267699    ? 
0.183468728747  ? 0.714755180337 ? -0.0421226287405  ? -0.00150243012889 ? 0.0276723520318  ? 0.167020584299    ? -0.0452174283943 
? 0.168239184628   ? 0.00326199974002 ? -0.110112265811   ? -0.186652874312  ? 
3  'X-RAY DIFFRACTION' ? refined 39.2171538302 4.93370002281   8.45177958507 0.560462794605 ? 0.0225920766174   ? -0.195606883642  
? 0.408681281534 ? -0.00444582667114 ? 0.548934301146  ? 4.94610992086   ? -0.585676802244 ? -0.870104391748 ? 0.070287214565   ? 
0.09713457214   ? 0.174249320118 ? 0.00225193294313  ? 0.113072636753    ? 0.272557878576   ? -0.131872050908   ? -0.0546936307016 
? -0.120694233825  ? -0.189458256261  ? 0.375163863033    ? 0.0106310373972  ? 
4  'X-RAY DIFFRACTION' ? refined 33.6867393135 6.28725392382   7.72894060808 0.48929964106  ? -0.0676976907356  ? -0.219459215952  
? 0.341935924178 ? 0.140603136819    ? 0.558530487991  ? 9.46348230394   ? -0.967268770901 ? -5.41436837672  ? 4.47315275666    ? 
0.62864923931   ? 3.3182200886   ? 0.0679265254349   ? 0.365200663276    ? 0.815287310774   ? -0.39040819989    ? -0.114741640754  
? -0.215454382351  ? -0.604459707306  ? 0.38652052604     ? 0.00811385982232 ? 
5  'X-RAY DIFFRACTION' ? refined 20.4345952123 -4.99569386644  26.5510115624 0.203639552665 ? 0.00271987762922  ? -0.0269229296315 
? 0.24729279307  ? -0.210336304666   ? 0.341707759018  ? 0.459529500569  ? 0.187836051214  ? -0.068759481726 ? 0.959130487      ? 
0.131433301107  ? 0.199768862811 ? -0.0974531762888  ? -0.068422930516   ? 0.0898312699911  ? 0.0140123043111   ? -0.0950198613125 
? 0.198806053916   ? 0.025319486938   ? -0.171122140859   ? -0.211169932869  ? 
6  'X-RAY DIFFRACTION' ? refined 36.4885440835 -25.2107808821  24.6596756347 0.164474625006 ? 0.0427274617829   ? 0.0403502003603  
? 0.195624702156 ? -0.0251207479347  ? 0.0419677766467 ? 3.3814039098    ? 1.67547301616   ? 0.365643519699  ? 4.07622189763    ? 
0.716551004406  ? 4.16847157835  ? 0.0211434229273   ? -0.206112450739   ? -0.0892355899208 ? 0.310970435913    ? 0.0669697345071  
? -0.184862863279  ? 0.0812210917149  ? 0.365782249367    ? -0.144616995704  ? 
7  'X-RAY DIFFRACTION' ? refined 27.9853023291 -24.7315921566  30.2485753796 0.209472801798 ? -0.00741096033243 ? 0.0681696933636  
? 0.199384020189 ? -0.0766857706312  ? 0.107882717732  ? 0.650517288131  ? -0.611318466704 ? -0.657539859286 ? 2.55045098057    ? 
1.68891306765   ? 2.74571091951  ? -0.026890596223   ? -0.205059517177   ? 0.0871850903274  ? 0.267746164667    ? 0.0236903629671  
? 0.00717756895307 ? 0.124590971367   ? 0.147475325877    ? -0.0260152319825 ? 
8  'X-RAY DIFFRACTION' ? refined 9.13375030136 -31.4429702528  8.02861814134 0.343874051452 ? -0.0364789383225  ? -0.136653251522  
? 0.383313933327 ? -0.145537418862   ? 0.380196490145  ? 4.53549414927   ? -0.220471622567 ? 2.5088961166    ? 0.00999316932168 ? 
-0.120948750575 ? 1.38681608514  ? 0.061237449957    ? 0.0917035455001   ? -0.382102026317  ? -0.00165969853011 ? -0.0413561013409 
? 0.18280002296    ? 0.33543373385    ? -0.360700979191   ? -0.137516874574  ? 
9  'X-RAY DIFFRACTION' ? refined 23.0224581846 -21.4614107102  25.5157191761 0.197993295383 ? -0.00801588136311 ? 0.0539410879319  
? 0.218466420029 ? -0.0886310142985  ? 0.162746723943  ? 1.29269861669   ? 0.192150479082  ? 0.845406900735  ? 2.06590088158    ? 
0.998745496518  ? 0.92545084921  ? -0.00950636073865 ? -0.149199664656   ? 0.0883989092412  ? 0.0827841313675   ? -0.0471509224473 
? 0.36658478953    ? -0.0482450453852 ? -0.111789031535   ? -0.038243464937  ? 
10 'X-RAY DIFFRACTION' ? refined 34.8206208214 -23.7534954308  31.4316207765 0.288017739512 ? 0.00595948837763  ? 0.021904352541   
? 0.232979740982 ? -0.0779945813721  ? 0.0989607360492 ? 4.01126989125   ? 1.51879298169   ? 0.0463751974514 ? 4.65802025856    ? 
1.42833259858   ? 4.26121170868  ? -0.00241742275484 ? -0.250814280954   ? -0.177057274889  ? 0.363266032709    ? -0.0626638889822 
? -0.0740095486963 ? 0.335828618641   ? 0.000660492468048 ? 0.136981181437   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1  A 3  ? A 19 A 21 ? ? 
;chain 'A' and (resid 3 through 21 )
;
2  'X-RAY DIFFRACTION' 2  A 20 A 22 ? A 32 A 34 ? ? 
;chain 'A' and (resid 22 through 34 )
;
3  'X-RAY DIFFRACTION' 3  A 33 A 35 ? A 48 A 50 ? ? 
;chain 'A' and (resid 35 through 50 )
;
4  'X-RAY DIFFRACTION' 4  A 49 A 51 ? A 54 A 56 ? ? 
;chain 'A' and (resid 51 through 56 )
;
5  'X-RAY DIFFRACTION' 5  A 55 A 57 ? A 86 A 88 ? ? 
;chain 'A' and (resid 57 through 88 )
;
6  'X-RAY DIFFRACTION' 6  B 1  B 2  ? B 13 B 14 ? ? 
;chain 'B' and (resid 2 through 14 )
;
7  'X-RAY DIFFRACTION' 7  B 14 B 15 ? B 33 B 34 ? ? 
;chain 'B' and (resid 15 through 34 )
;
8  'X-RAY DIFFRACTION' 8  B 34 B 35 ? B 55 B 56 ? ? 
;chain 'B' and (resid 35 through 56 )
;
9  'X-RAY DIFFRACTION' 9  B 56 B 57 ? B 79 B 80 ? ? 
;chain 'B' and (resid 57 through 80 )
;
10 'X-RAY DIFFRACTION' 10 B 80 B 81 ? B 87 B 88 ? ? 
;chain 'B' and (resid 81 through 88 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       289 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.95 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 0 ? A SER 1 
2 1 Y 1 A MET 1 ? A MET 2 
3 1 Y 1 A ASP 2 ? A ASP 3 
4 1 Y 1 B SER 0 ? B SER 1 
5 1 Y 1 B MET 1 ? B MET 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HOH O    O N N 123 
HOH H1   H N N 124 
HOH H2   H N N 125 
ILE N    N N N 126 
ILE CA   C N S 127 
ILE C    C N N 128 
ILE O    O N N 129 
ILE CB   C N S 130 
ILE CG1  C N N 131 
ILE CG2  C N N 132 
ILE CD1  C N N 133 
ILE OXT  O N N 134 
ILE H    H N N 135 
ILE H2   H N N 136 
ILE HA   H N N 137 
ILE HB   H N N 138 
ILE HG12 H N N 139 
ILE HG13 H N N 140 
ILE HG21 H N N 141 
ILE HG22 H N N 142 
ILE HG23 H N N 143 
ILE HD11 H N N 144 
ILE HD12 H N N 145 
ILE HD13 H N N 146 
ILE HXT  H N N 147 
LEU N    N N N 148 
LEU CA   C N S 149 
LEU C    C N N 150 
LEU O    O N N 151 
LEU CB   C N N 152 
LEU CG   C N N 153 
LEU CD1  C N N 154 
LEU CD2  C N N 155 
LEU OXT  O N N 156 
LEU H    H N N 157 
LEU H2   H N N 158 
LEU HA   H N N 159 
LEU HB2  H N N 160 
LEU HB3  H N N 161 
LEU HG   H N N 162 
LEU HD11 H N N 163 
LEU HD12 H N N 164 
LEU HD13 H N N 165 
LEU HD21 H N N 166 
LEU HD22 H N N 167 
LEU HD23 H N N 168 
LEU HXT  H N N 169 
LYS N    N N N 170 
LYS CA   C N S 171 
LYS C    C N N 172 
LYS O    O N N 173 
LYS CB   C N N 174 
LYS CG   C N N 175 
LYS CD   C N N 176 
LYS CE   C N N 177 
LYS NZ   N N N 178 
LYS OXT  O N N 179 
LYS H    H N N 180 
LYS H2   H N N 181 
LYS HA   H N N 182 
LYS HB2  H N N 183 
LYS HB3  H N N 184 
LYS HG2  H N N 185 
LYS HG3  H N N 186 
LYS HD2  H N N 187 
LYS HD3  H N N 188 
LYS HE2  H N N 189 
LYS HE3  H N N 190 
LYS HZ1  H N N 191 
LYS HZ2  H N N 192 
LYS HZ3  H N N 193 
LYS HXT  H N N 194 
MET N    N N N 195 
MET CA   C N S 196 
MET C    C N N 197 
MET O    O N N 198 
MET CB   C N N 199 
MET CG   C N N 200 
MET SD   S N N 201 
MET CE   C N N 202 
MET OXT  O N N 203 
MET H    H N N 204 
MET H2   H N N 205 
MET HA   H N N 206 
MET HB2  H N N 207 
MET HB3  H N N 208 
MET HG2  H N N 209 
MET HG3  H N N 210 
MET HE1  H N N 211 
MET HE2  H N N 212 
MET HE3  H N N 213 
MET HXT  H N N 214 
PHE N    N N N 215 
PHE CA   C N S 216 
PHE C    C N N 217 
PHE O    O N N 218 
PHE CB   C N N 219 
PHE CG   C Y N 220 
PHE CD1  C Y N 221 
PHE CD2  C Y N 222 
PHE CE1  C Y N 223 
PHE CE2  C Y N 224 
PHE CZ   C Y N 225 
PHE OXT  O N N 226 
PHE H    H N N 227 
PHE H2   H N N 228 
PHE HA   H N N 229 
PHE HB2  H N N 230 
PHE HB3  H N N 231 
PHE HD1  H N N 232 
PHE HD2  H N N 233 
PHE HE1  H N N 234 
PHE HE2  H N N 235 
PHE HZ   H N N 236 
PHE HXT  H N N 237 
PRO N    N N N 238 
PRO CA   C N S 239 
PRO C    C N N 240 
PRO O    O N N 241 
PRO CB   C N N 242 
PRO CG   C N N 243 
PRO CD   C N N 244 
PRO OXT  O N N 245 
PRO H    H N N 246 
PRO HA   H N N 247 
PRO HB2  H N N 248 
PRO HB3  H N N 249 
PRO HG2  H N N 250 
PRO HG3  H N N 251 
PRO HD2  H N N 252 
PRO HD3  H N N 253 
PRO HXT  H N N 254 
SER N    N N N 255 
SER CA   C N S 256 
SER C    C N N 257 
SER O    O N N 258 
SER CB   C N N 259 
SER OG   O N N 260 
SER OXT  O N N 261 
SER H    H N N 262 
SER H2   H N N 263 
SER HA   H N N 264 
SER HB2  H N N 265 
SER HB3  H N N 266 
SER HG   H N N 267 
SER HXT  H N N 268 
THR N    N N N 269 
THR CA   C N S 270 
THR C    C N N 271 
THR O    O N N 272 
THR CB   C N R 273 
THR OG1  O N N 274 
THR CG2  C N N 275 
THR OXT  O N N 276 
THR H    H N N 277 
THR H2   H N N 278 
THR HA   H N N 279 
THR HB   H N N 280 
THR HG1  H N N 281 
THR HG21 H N N 282 
THR HG22 H N N 283 
THR HG23 H N N 284 
THR HXT  H N N 285 
TRP N    N N N 286 
TRP CA   C N S 287 
TRP C    C N N 288 
TRP O    O N N 289 
TRP CB   C N N 290 
TRP CG   C Y N 291 
TRP CD1  C Y N 292 
TRP CD2  C Y N 293 
TRP NE1  N Y N 294 
TRP CE2  C Y N 295 
TRP CE3  C Y N 296 
TRP CZ2  C Y N 297 
TRP CZ3  C Y N 298 
TRP CH2  C Y N 299 
TRP OXT  O N N 300 
TRP H    H N N 301 
TRP H2   H N N 302 
TRP HA   H N N 303 
TRP HB2  H N N 304 
TRP HB3  H N N 305 
TRP HD1  H N N 306 
TRP HE1  H N N 307 
TRP HE3  H N N 308 
TRP HZ2  H N N 309 
TRP HZ3  H N N 310 
TRP HH2  H N N 311 
TRP HXT  H N N 312 
TYR N    N N N 313 
TYR CA   C N S 314 
TYR C    C N N 315 
TYR O    O N N 316 
TYR CB   C N N 317 
TYR CG   C Y N 318 
TYR CD1  C Y N 319 
TYR CD2  C Y N 320 
TYR CE1  C Y N 321 
TYR CE2  C Y N 322 
TYR CZ   C Y N 323 
TYR OH   O N N 324 
TYR OXT  O N N 325 
TYR H    H N N 326 
TYR H2   H N N 327 
TYR HA   H N N 328 
TYR HB2  H N N 329 
TYR HB3  H N N 330 
TYR HD1  H N N 331 
TYR HD2  H N N 332 
TYR HE1  H N N 333 
TYR HE2  H N N 334 
TYR HH   H N N 335 
TYR HXT  H N N 336 
VAL N    N N N 337 
VAL CA   C N S 338 
VAL C    C N N 339 
VAL O    O N N 340 
VAL CB   C N N 341 
VAL CG1  C N N 342 
VAL CG2  C N N 343 
VAL OXT  O N N 344 
VAL H    H N N 345 
VAL H2   H N N 346 
VAL HA   H N N 347 
VAL HB   H N N 348 
VAL HG11 H N N 349 
VAL HG12 H N N 350 
VAL HG13 H N N 351 
VAL HG21 H N N 352 
VAL HG22 H N N 353 
VAL HG23 H N N 354 
VAL HXT  H N N 355 
Y65 C01  C N R 356 
Y65 C02  C N R 357 
Y65 C03  C N S 358 
Y65 C04  C N R 359 
Y65 C16  C N N 360 
Y65 C18  C N S 361 
Y65 O05  O N N 362 
Y65 O21  O N N 363 
Y65 C06  C N N 364 
Y65 C17  C N R 365 
Y65 C19  C N R 366 
Y65 C20  C N R 367 
Y65 C23  C Y N 368 
Y65 C25  C Y N 369 
Y65 C26  C Y N 370 
Y65 C28  C Y N 371 
Y65 C30  C Y N 372 
Y65 C37  C Y N 373 
Y65 C39  C Y N 374 
Y65 C40  C Y N 375 
Y65 C41  C N N 376 
Y65 C42  C N S 377 
Y65 C44  C N N 378 
Y65 N22  N Y N 379 
Y65 N24  N Y N 380 
Y65 N27  N Y N 381 
Y65 N29  N Y N 382 
Y65 N31  N N N 383 
Y65 N36  N Y N 384 
Y65 N38  N Y N 385 
Y65 N43  N N N 386 
Y65 O07  O N N 387 
Y65 O09  O N N 388 
Y65 O10  O N N 389 
Y65 O11  O N N 390 
Y65 O13  O N N 391 
Y65 O14  O N N 392 
Y65 O15  O N N 393 
Y65 O32  O N N 394 
Y65 O33  O N N 395 
Y65 O34  O N N 396 
Y65 O35  O N N 397 
Y65 O45  O N N 398 
Y65 O46  O N N 399 
Y65 P08  P N N 400 
Y65 P12  P N N 401 
Y65 H1   H N N 402 
Y65 H2   H N N 403 
Y65 H3   H N N 404 
Y65 H4   H N N 405 
Y65 H5   H N N 406 
Y65 H6   H N N 407 
Y65 H7   H N N 408 
Y65 H8   H N N 409 
Y65 H9   H N N 410 
Y65 H10  H N N 411 
Y65 H11  H N N 412 
Y65 H12  H N N 413 
Y65 H13  H N N 414 
Y65 H14  H N N 415 
Y65 H15  H N N 416 
Y65 H16  H N N 417 
Y65 H17  H N N 418 
Y65 H18  H N N 419 
Y65 H19  H N N 420 
Y65 H20  H N N 421 
Y65 H21  H N N 422 
Y65 H22  H N N 423 
Y65 H23  H N N 424 
Y65 H25  H N N 425 
Y65 H26  H N N 426 
Y65 H27  H N N 427 
Y65 H28  H N N 428 
Y65 H29  H N N 429 
Y65 H30  H N N 430 
Y65 H31  H N N 431 
# 
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  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HOH O   H1   sing N N 116 
HOH O   H2   sing N N 117 
ILE N   CA   sing N N 118 
ILE N   H    sing N N 119 
ILE N   H2   sing N N 120 
ILE CA  C    sing N N 121 
ILE CA  CB   sing N N 122 
ILE CA  HA   sing N N 123 
ILE C   O    doub N N 124 
ILE C   OXT  sing N N 125 
ILE CB  CG1  sing N N 126 
ILE CB  CG2  sing N N 127 
ILE CB  HB   sing N N 128 
ILE CG1 CD1  sing N N 129 
ILE CG1 HG12 sing N N 130 
ILE CG1 HG13 sing N N 131 
ILE CG2 HG21 sing N N 132 
ILE CG2 HG22 sing N N 133 
ILE CG2 HG23 sing N N 134 
ILE CD1 HD11 sing N N 135 
ILE CD1 HD12 sing N N 136 
ILE CD1 HD13 sing N N 137 
ILE OXT HXT  sing N N 138 
LEU N   CA   sing N N 139 
LEU N   H    sing N N 140 
LEU N   H2   sing N N 141 
LEU CA  C    sing N N 142 
LEU CA  CB   sing N N 143 
LEU CA  HA   sing N N 144 
LEU C   O    doub N N 145 
LEU C   OXT  sing N N 146 
LEU CB  CG   sing N N 147 
LEU CB  HB2  sing N N 148 
LEU CB  HB3  sing N N 149 
LEU CG  CD1  sing N N 150 
LEU CG  CD2  sing N N 151 
LEU CG  HG   sing N N 152 
LEU CD1 HD11 sing N N 153 
LEU CD1 HD12 sing N N 154 
LEU CD1 HD13 sing N N 155 
LEU CD2 HD21 sing N N 156 
LEU CD2 HD22 sing N N 157 
LEU CD2 HD23 sing N N 158 
LEU OXT HXT  sing N N 159 
LYS N   CA   sing N N 160 
LYS N   H    sing N N 161 
LYS N   H2   sing N N 162 
LYS CA  C    sing N N 163 
LYS CA  CB   sing N N 164 
LYS CA  HA   sing N N 165 
LYS C   O    doub N N 166 
LYS C   OXT  sing N N 167 
LYS CB  CG   sing N N 168 
LYS CB  HB2  sing N N 169 
LYS CB  HB3  sing N N 170 
LYS CG  CD   sing N N 171 
LYS CG  HG2  sing N N 172 
LYS CG  HG3  sing N N 173 
LYS CD  CE   sing N N 174 
LYS CD  HD2  sing N N 175 
LYS CD  HD3  sing N N 176 
LYS CE  NZ   sing N N 177 
LYS CE  HE2  sing N N 178 
LYS CE  HE3  sing N N 179 
LYS NZ  HZ1  sing N N 180 
LYS NZ  HZ2  sing N N 181 
LYS NZ  HZ3  sing N N 182 
LYS OXT HXT  sing N N 183 
MET N   CA   sing N N 184 
MET N   H    sing N N 185 
MET N   H2   sing N N 186 
MET CA  C    sing N N 187 
MET CA  CB   sing N N 188 
MET CA  HA   sing N N 189 
MET C   O    doub N N 190 
MET C   OXT  sing N N 191 
MET CB  CG   sing N N 192 
MET CB  HB2  sing N N 193 
MET CB  HB3  sing N N 194 
MET CG  SD   sing N N 195 
MET CG  HG2  sing N N 196 
MET CG  HG3  sing N N 197 
MET SD  CE   sing N N 198 
MET CE  HE1  sing N N 199 
MET CE  HE2  sing N N 200 
MET CE  HE3  sing N N 201 
MET OXT HXT  sing N N 202 
PHE N   CA   sing N N 203 
PHE N   H    sing N N 204 
PHE N   H2   sing N N 205 
PHE CA  C    sing N N 206 
PHE CA  CB   sing N N 207 
PHE CA  HA   sing N N 208 
PHE C   O    doub N N 209 
PHE C   OXT  sing N N 210 
PHE CB  CG   sing N N 211 
PHE CB  HB2  sing N N 212 
PHE CB  HB3  sing N N 213 
PHE CG  CD1  doub Y N 214 
PHE CG  CD2  sing Y N 215 
PHE CD1 CE1  sing Y N 216 
PHE CD1 HD1  sing N N 217 
PHE CD2 CE2  doub Y N 218 
PHE CD2 HD2  sing N N 219 
PHE CE1 CZ   doub Y N 220 
PHE CE1 HE1  sing N N 221 
PHE CE2 CZ   sing Y N 222 
PHE CE2 HE2  sing N N 223 
PHE CZ  HZ   sing N N 224 
PHE OXT HXT  sing N N 225 
PRO N   CA   sing N N 226 
PRO N   CD   sing N N 227 
PRO N   H    sing N N 228 
PRO CA  C    sing N N 229 
PRO CA  CB   sing N N 230 
PRO CA  HA   sing N N 231 
PRO C   O    doub N N 232 
PRO C   OXT  sing N N 233 
PRO CB  CG   sing N N 234 
PRO CB  HB2  sing N N 235 
PRO CB  HB3  sing N N 236 
PRO CG  CD   sing N N 237 
PRO CG  HG2  sing N N 238 
PRO CG  HG3  sing N N 239 
PRO CD  HD2  sing N N 240 
PRO CD  HD3  sing N N 241 
PRO OXT HXT  sing N N 242 
SER N   CA   sing N N 243 
SER N   H    sing N N 244 
SER N   H2   sing N N 245 
SER CA  C    sing N N 246 
SER CA  CB   sing N N 247 
SER CA  HA   sing N N 248 
SER C   O    doub N N 249 
SER C   OXT  sing N N 250 
SER CB  OG   sing N N 251 
SER CB  HB2  sing N N 252 
SER CB  HB3  sing N N 253 
SER OG  HG   sing N N 254 
SER OXT HXT  sing N N 255 
THR N   CA   sing N N 256 
THR N   H    sing N N 257 
THR N   H2   sing N N 258 
THR CA  C    sing N N 259 
THR CA  CB   sing N N 260 
THR CA  HA   sing N N 261 
THR C   O    doub N N 262 
THR C   OXT  sing N N 263 
THR CB  OG1  sing N N 264 
THR CB  CG2  sing N N 265 
THR CB  HB   sing N N 266 
THR OG1 HG1  sing N N 267 
THR CG2 HG21 sing N N 268 
THR CG2 HG22 sing N N 269 
THR CG2 HG23 sing N N 270 
THR OXT HXT  sing N N 271 
TRP N   CA   sing N N 272 
TRP N   H    sing N N 273 
TRP N   H2   sing N N 274 
TRP CA  C    sing N N 275 
TRP CA  CB   sing N N 276 
TRP CA  HA   sing N N 277 
TRP C   O    doub N N 278 
TRP C   OXT  sing N N 279 
TRP CB  CG   sing N N 280 
TRP CB  HB2  sing N N 281 
TRP CB  HB3  sing N N 282 
TRP CG  CD1  doub Y N 283 
TRP CG  CD2  sing Y N 284 
TRP CD1 NE1  sing Y N 285 
TRP CD1 HD1  sing N N 286 
TRP CD2 CE2  doub Y N 287 
TRP CD2 CE3  sing Y N 288 
TRP NE1 CE2  sing Y N 289 
TRP NE1 HE1  sing N N 290 
TRP CE2 CZ2  sing Y N 291 
TRP CE3 CZ3  doub Y N 292 
TRP CE3 HE3  sing N N 293 
TRP CZ2 CH2  doub Y N 294 
TRP CZ2 HZ2  sing N N 295 
TRP CZ3 CH2  sing Y N 296 
TRP CZ3 HZ3  sing N N 297 
TRP CH2 HH2  sing N N 298 
TRP OXT HXT  sing N N 299 
TYR N   CA   sing N N 300 
TYR N   H    sing N N 301 
TYR N   H2   sing N N 302 
TYR CA  C    sing N N 303 
TYR CA  CB   sing N N 304 
TYR CA  HA   sing N N 305 
TYR C   O    doub N N 306 
TYR C   OXT  sing N N 307 
TYR CB  CG   sing N N 308 
TYR CB  HB2  sing N N 309 
TYR CB  HB3  sing N N 310 
TYR CG  CD1  doub Y N 311 
TYR CG  CD2  sing Y N 312 
TYR CD1 CE1  sing Y N 313 
TYR CD1 HD1  sing N N 314 
TYR CD2 CE2  doub Y N 315 
TYR CD2 HD2  sing N N 316 
TYR CE1 CZ   doub Y N 317 
TYR CE1 HE1  sing N N 318 
TYR CE2 CZ   sing Y N 319 
TYR CE2 HE2  sing N N 320 
TYR CZ  OH   sing N N 321 
TYR OH  HH   sing N N 322 
TYR OXT HXT  sing N N 323 
VAL N   CA   sing N N 324 
VAL N   H    sing N N 325 
VAL N   H2   sing N N 326 
VAL CA  C    sing N N 327 
VAL CA  CB   sing N N 328 
VAL CA  HA   sing N N 329 
VAL C   O    doub N N 330 
VAL C   OXT  sing N N 331 
VAL CB  CG1  sing N N 332 
VAL CB  CG2  sing N N 333 
VAL CB  HB   sing N N 334 
VAL CG1 HG11 sing N N 335 
VAL CG1 HG12 sing N N 336 
VAL CG1 HG13 sing N N 337 
VAL CG2 HG21 sing N N 338 
VAL CG2 HG22 sing N N 339 
VAL CG2 HG23 sing N N 340 
VAL OXT HXT  sing N N 341 
Y65 N43 C42  sing N N 342 
Y65 C42 C44  sing N N 343 
Y65 C42 C41  sing N N 344 
Y65 C44 O45  doub N N 345 
Y65 C44 O46  sing N N 346 
Y65 C41 C39  sing N N 347 
Y65 C39 N38  sing Y N 348 
Y65 C39 C40  doub Y N 349 
Y65 N38 C37  doub Y N 350 
Y65 C40 N36  sing Y N 351 
Y65 O35 C02  sing N N 352 
Y65 C37 N36  sing Y N 353 
Y65 N36 C01  sing N N 354 
Y65 C01 C02  sing N N 355 
Y65 C01 O05  sing N N 356 
Y65 C02 C03  sing N N 357 
Y65 O34 C03  sing N N 358 
Y65 O05 C04  sing N N 359 
Y65 C03 C04  sing N N 360 
Y65 C04 C06  sing N N 361 
Y65 C06 O07  sing N N 362 
Y65 O07 P08  sing N N 363 
Y65 P08 O10  doub N N 364 
Y65 P08 O11  sing N N 365 
Y65 P08 O09  sing N N 366 
Y65 O13 P12  doub N N 367 
Y65 O14 P12  sing N N 368 
Y65 O11 P12  sing N N 369 
Y65 P12 O15  sing N N 370 
Y65 O15 C16  sing N N 371 
Y65 C16 C17  sing N N 372 
Y65 C17 C18  sing N N 373 
Y65 C17 O21  sing N N 374 
Y65 C23 N24  doub Y N 375 
Y65 C23 N22  sing Y N 376 
Y65 C18 C19  sing N N 377 
Y65 C18 O33  sing N N 378 
Y65 N24 C25  sing Y N 379 
Y65 C19 C20  sing N N 380 
Y65 C19 O32  sing N N 381 
Y65 O21 C20  sing N N 382 
Y65 N31 C26  sing N N 383 
Y65 N22 C20  sing N N 384 
Y65 N22 C30  sing Y N 385 
Y65 C25 C26  doub Y N 386 
Y65 C25 C30  sing Y N 387 
Y65 C26 N27  sing Y N 388 
Y65 C30 N29  doub Y N 389 
Y65 N27 C28  doub Y N 390 
Y65 N29 C28  sing Y N 391 
Y65 C01 H1   sing N N 392 
Y65 C02 H2   sing N N 393 
Y65 C03 H3   sing N N 394 
Y65 C04 H4   sing N N 395 
Y65 C16 H5   sing N N 396 
Y65 C16 H6   sing N N 397 
Y65 C18 H7   sing N N 398 
Y65 C06 H8   sing N N 399 
Y65 C06 H9   sing N N 400 
Y65 C17 H10  sing N N 401 
Y65 C19 H11  sing N N 402 
Y65 C20 H12  sing N N 403 
Y65 C23 H13  sing N N 404 
Y65 C28 H14  sing N N 405 
Y65 C37 H15  sing N N 406 
Y65 C40 H16  sing N N 407 
Y65 C41 H17  sing N N 408 
Y65 C41 H18  sing N N 409 
Y65 C42 H19  sing N N 410 
Y65 N31 H20  sing N N 411 
Y65 N31 H21  sing N N 412 
Y65 N43 H22  sing N N 413 
Y65 N43 H23  sing N N 414 
Y65 O09 H25  sing N N 415 
Y65 O14 H26  sing N N 416 
Y65 O32 H27  sing N N 417 
Y65 O33 H28  sing N N 418 
Y65 O34 H29  sing N N 419 
Y65 O35 H30  sing N N 420 
Y65 O46 H31  sing N N 421 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1DP2GM146250-01 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8V3E 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 63 2 2' 
_space_group.name_Hall        'P 6c 2c' 
_space_group.IT_number        182 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EIB 
_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]   0.010788 
_atom_sites.fract_transf_matrix[1][2]   0.006229 
_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]   0.012457 
_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]   0.012808 
_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.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P   ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 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   . SER A 1 4  ? 5.14345  -4.10161  33.51778 1.000 44.09097  ?  3   SER A N   1 
ATOM   2    C CA  . SER A 1 4  ? 6.10622  -4.99508  32.86728 1.000 40.24608  ?  3   SER A CA  1 
ATOM   3    C C   . SER A 1 4  ? 5.76053  -5.19262  31.38991 1.000 41.47761  ?  3   SER A C   1 
ATOM   4    O O   . SER A 1 4  ? 4.70450  -5.71734  31.03108 1.000 46.20306  ?  3   SER A O   1 
ATOM   5    C CB  . SER A 1 4  ? 6.17026  -6.34953  33.58451 1.000 50.08872  ?  3   SER A CB  1 
ATOM   6    O OG  . SER A 1 4  ? 4.87956  -6.91295  33.75364 1.000 57.46145  ?  3   SER A OG  1 
ATOM   7    N N   . LEU A 1 5  ? 6.68156  -4.77761  30.53812 1.000 34.40159  ?  4   LEU A N   1 
ATOM   8    C CA  . LEU A 1 5  ? 6.47492  -4.67828  29.10294 1.000 32.74214  ?  4   LEU A CA  1 
ATOM   9    C C   . LEU A 1 5  ? 7.03374  -5.88906  28.36285 1.000 31.16341  ?  4   LEU A C   1 
ATOM   10   O O   . LEU A 1 5  ? 7.90586  -6.61398  28.85379 1.000 28.48045  ?  4   LEU A O   1 
ATOM   11   C CB  . LEU A 1 5  ? 7.14797  -3.40567  28.58398 1.000 34.87606  ?  4   LEU A CB  1 
ATOM   12   C CG  . LEU A 1 5  ? 7.01785  -2.22044  29.55042 1.000 35.01674  ?  4   LEU A CG  1 
ATOM   13   C CD1 . LEU A 1 5  ? 7.90817  -1.06281  29.12291 1.000 37.11423  ?  4   LEU A CD1 1 
ATOM   14   C CD2 . LEU A 1 5  ? 5.57053  -1.79117  29.61089 1.000 36.87652  ?  4   LEU A CD2 1 
ATOM   15   N N   . ASN A 1 6  ? 6.52184  -6.08946  27.15463 1.000 28.10384  ?  5   ASN A N   1 
ATOM   16   C CA  . ASN A 1 6  ? 7.15004  -7.00094  26.22632 1.000 29.89215  ?  5   ASN A CA  1 
ATOM   17   C C   . ASN A 1 6  ? 8.32519  -6.29455  25.54983 1.000 26.72342  ?  5   ASN A C   1 
ATOM   18   O O   . ASN A 1 6  ? 8.59355  -5.10675  25.77886 1.000 26.75141  ?  5   ASN A O   1 
ATOM   19   C CB  . ASN A 1 6  ? 6.11552  -7.54403  25.23385 1.000 31.21010  ?  5   ASN A CB  1 
ATOM   20   C CG  . ASN A 1 6  ? 5.47177  -6.47099  24.38939 1.000 34.40792  ?  5   ASN A CG  1 
ATOM   21   O OD1 . ASN A 1 6  ? 6.11651  -5.51968  23.96903 1.000 32.03425  ?  5   ASN A OD1 1 
ATOM   22   N ND2 . ASN A 1 6  ? 4.18097  -6.63862  24.11135 1.000 30.94507  ?  5   ASN A ND2 1 
ATOM   23   N N   . PHE A 1 7  ? 9.05811  -7.04537  24.71997 1.000 31.50436  ?  6   PHE A N   1 
ATOM   24   C CA  . PHE A 1 7  ? 10.25109 -6.47618  24.11385 1.000 27.84605  ?  6   PHE A CA  1 
ATOM   25   C C   . PHE A 1 7  ? 9.90794  -5.39606  23.10211 1.000 26.78359  ?  6   PHE A C   1 
ATOM   26   O O   . PHE A 1 7  ? 10.70493 -4.47469  22.90280 1.000 30.63173  ?  6   PHE A O   1 
ATOM   27   C CB  . PHE A 1 7  ? 11.09681 -7.56313  23.45100 1.000 25.68195  ?  6   PHE A CB  1 
ATOM   28   C CG  . PHE A 1 7  ? 12.37746 -7.03466  22.85725 1.000 25.42266  ?  6   PHE A CG  1 
ATOM   29   C CD1 . PHE A 1 7  ? 13.39270 -6.59080  23.68140 1.000 25.28564  ?  6   PHE A CD1 1 
ATOM   30   C CD2 . PHE A 1 7  ? 12.54135 -6.94854  21.48390 1.000 25.35307  ?  6   PHE A CD2 1 
ATOM   31   C CE1 . PHE A 1 7  ? 14.58418 -6.08438  23.14646 1.000 25.08392  ?  6   PHE A CE1 1 
ATOM   32   C CE2 . PHE A 1 7  ? 13.70388 -6.46474  20.94304 1.000 25.14705  ?  6   PHE A CE2 1 
ATOM   33   C CZ  . PHE A 1 7  ? 14.73658 -6.02771  21.77661 1.000 25.26440  ?  6   PHE A CZ  1 
ATOM   34   N N   . GLY A 1 8  ? 8.75005  -5.49910  22.44217 1.000 26.56642  ?  7   GLY A N   1 
ATOM   35   C CA  . GLY A 1 8  ? 8.35872  -4.47757  21.47677 1.000 29.69928  ?  7   GLY A CA  1 
ATOM   36   C C   . GLY A 1 8  ? 8.29347  -3.08869  22.08601 1.000 27.60453  ?  7   GLY A C   1 
ATOM   37   O O   . GLY A 1 8  ? 8.79157  -2.11252  21.50560 1.000 27.11389  ?  7   GLY A O   1 
ATOM   38   N N   . LYS A 1 9  ? 7.70155  -2.97981  23.27819 1.000 27.42613  ?  8   LYS A N   1 
ATOM   39   C CA  . LYS A 1 9  ? 7.66553  -1.69558  23.96486 1.000 27.49107  ?  8   LYS A CA  1 
ATOM   40   C C   . LYS A 1 9  ? 9.04150  -1.31017  24.48255 1.000 29.45251  ?  8   LYS A C   1 
ATOM   41   O O   . LYS A 1 9  ? 9.41491  -0.13028  24.44289 1.000 28.24815  ?  8   LYS A O   1 
ATOM   42   C CB  . LYS A 1 9  ? 6.64997  -1.73926  25.10637 1.000 27.77517  ?  8   LYS A CB  1 
ATOM   43   C CG  . LYS A 1 9  ? 5.19657  -2.06441  24.66678 1.000 36.99406  ?  8   LYS A CG  1 
ATOM   44   C CD  . LYS A 1 9  ? 4.56173  -0.92988  23.84326 1.000 50.64984  ?  8   LYS A CD  1 
ATOM   45   C CE  . LYS A 1 9  ? 4.25671  0.30352   24.69897 1.000 62.75024  ?  8   LYS A CE  1 
ATOM   46   N NZ  . LYS A 1 9  ? 3.41662  1.32265   23.98974 1.000 52.01307  ?  8   LYS A NZ  1 
ATOM   47   N N   . ALA A 1 10 ? 9.81559  -2.28210  24.98122 1.000 27.70563  ?  9   ALA A N   1 
ATOM   48   C CA  . ALA A 1 10 ? 11.18250 -1.97403  25.38753 1.000 26.56276  ?  9   ALA A CA  1 
ATOM   49   C C   . ALA A 1 10 ? 12.01044 -1.48887  24.20590 1.000 26.43547  ?  9   ALA A C   1 
ATOM   50   O O   . ALA A 1 10 ? 12.85930 -0.60779  24.37185 1.000 26.45760  ?  9   ALA A O   1 
ATOM   51   C CB  . ALA A 1 10 ? 11.83534 -3.19325  26.03966 1.000 26.23286  ?  9   ALA A CB  1 
ATOM   52   N N   . LEU A 1 11 ? 11.75298 -2.01844  23.00284 1.000 26.38800  ?  10  LEU A N   1 
ATOM   53   C CA  . LEU A 1 11 ? 12.47489 -1.55786  21.81781 1.000 26.30176  ?  10  LEU A CA  1 
ATOM   54   C C   . LEU A 1 11 ? 12.13752 -0.10012  21.48952 1.000 26.66612  ?  10  LEU A C   1 
ATOM   55   O O   . LEU A 1 11 ? 13.04042 0.71972   21.26692 1.000 26.63626  ?  10  LEU A O   1 
ATOM   56   C CB  . LEU A 1 11 ? 12.17440 -2.47755  20.63363 1.000 26.19702  ?  10  LEU A CB  1 
ATOM   57   C CG  . LEU A 1 11 ? 12.90440 -2.11768  19.33908 1.000 26.10537  ?  10  LEU A CG  1 
ATOM   58   C CD1 . LEU A 1 11 ? 14.41619 -2.09377  19.52097 1.000 25.77635  ?  10  LEU A CD1 1 
ATOM   59   C CD2 . LEU A 1 11 ? 12.51598 -3.09866  18.22342 1.000 32.32358  ?  10  LEU A CD2 1 
ATOM   60   N N   . GLU A 1 12 ? 10.85160 0.25147   21.46842 1.000 27.04027  ?  11  GLU A N   1 
ATOM   61   C CA  . GLU A 1 12 ? 10.49016 1.64849   21.24429 1.000 27.42209  ?  11  GLU A CA  1 
ATOM   62   C C   . GLU A 1 12 ? 11.16031 2.55282   22.26937 1.000 27.43188  ?  11  GLU A C   1 
ATOM   63   O O   . GLU A 1 12 ? 11.69386 3.60800   21.91182 1.000 31.02532  ?  11  GLU A O   1 
ATOM   64   C CB  . GLU A 1 12 ? 8.97402  1.83942   21.26779 1.000 27.84440  ?  11  GLU A CB  1 
ATOM   65   C CG  . GLU A 1 12 ? 8.35797  1.71268   19.90156 1.000 36.07611  ?  11  GLU A CG  1 
ATOM   66   C CD  . GLU A 1 12 ? 6.86466  2.01489   19.89871 1.000 72.07950  ?  11  GLU A CD  1 
ATOM   67   O OE1 . GLU A 1 12 ? 6.35034  2.50721   20.93788 1.000 56.24454  ?  11  GLU A OE1 1 
ATOM   68   O OE2 . GLU A 1 12 ? 6.21197  1.75340   18.85417 1.000 50.83099  ?  11  GLU A OE2 1 
ATOM   69   N N   . ALA A 1 13 ? 11.16711 2.14167   23.54270 1.000 27.32216  ?  12  ALA A N   1 
ATOM   70   C CA  . ALA A 1 13 ? 11.85493 2.90799   24.57800 1.000 27.31307  ?  12  ALA A CA  1 
ATOM   71   C C   . ALA A 1 13 ? 13.33736 3.09384   24.25233 1.000 29.79348  ?  12  ALA A C   1 
ATOM   72   O O   . ALA A 1 13 ? 13.87681 4.20134   24.35901 1.000 27.17108  ?  12  ALA A O   1 
ATOM   73   C CB  . ALA A 1 13 ? 11.66904 2.22252   25.92856 1.000 27.21151  ?  12  ALA A CB  1 
ATOM   74   N N   . LEU A 1 14 ? 14.01632 2.01786   23.86723 1.000 26.68091  ?  13  LEU A N   1 
ATOM   75   C CA  . LEU A 1 14 ? 15.41558 2.10793   23.45782 1.000 26.43314  ?  13  LEU A CA  1 
ATOM   76   C C   . LEU A 1 14 ? 15.61734 3.14524   22.35729 1.000 26.63506  ?  13  LEU A C   1 
ATOM   77   O O   . LEU A 1 14 ? 16.53439 3.97193   22.42597 1.000 26.66238  ?  13  LEU A O   1 
ATOM   78   C CB  . LEU A 1 14 ? 15.88477 0.74001   22.97639 1.000 26.06040  ?  13  LEU A CB  1 
ATOM   79   C CG  . LEU A 1 14 ? 16.27395 -0.28370  24.03296 1.000 25.79264  ?  13  LEU A CG  1 
ATOM   80   C CD1 . LEU A 1 14 ? 16.44673 -1.67013  23.37243 1.000 25.48553  ?  13  LEU A CD1 1 
ATOM   81   C CD2 . LEU A 1 14 ? 17.57517 0.14803   24.68162 1.000 25.66592  ?  13  LEU A CD2 1 
ATOM   82   N N   . LYS A 1 15 ? 14.78374 3.09612   21.31422 1.000 26.80066  ?  14  LYS A N   1 
ATOM   83   C CA  . LYS A 1 15 ? 14.97512 3.98086   20.17171 1.000 29.07733  ?  14  LYS A CA  1 
ATOM   84   C C   . LYS A 1 15 ? 14.72545 5.43887   20.52441 1.000 30.82615  ?  14  LYS A C   1 
ATOM   85   O O   . LYS A 1 15 ? 15.22178 6.32721   19.81851 1.000 29.94072  ?  14  LYS A O   1 
ATOM   86   C CB  . LYS A 1 15 ? 14.05995 3.57204   19.02078 1.000 27.12972  ?  14  LYS A CB  1 
ATOM   87   C CG  . LYS A 1 15 ? 14.45169 2.25714   18.32830 1.000 26.75635  ?  14  LYS A CG  1 
ATOM   88   C CD  . LYS A 1 15 ? 13.45397 1.94408   17.23393 1.000 26.93489  ?  14  LYS A CD  1 
ATOM   89   C CE  . LYS A 1 15 ? 13.83037 0.68051   16.47846 1.000 27.90056  ?  14  LYS A CE  1 
ATOM   90   N NZ  . LYS A 1 15 ? 12.68258 0.17166   15.63012 1.000 27.63171  ?  14  LYS A NZ  1 
ATOM   91   N N   . GLU A 1 16 ? 13.97463 5.69857   21.59836 1.000 27.57039  ?  15  GLU A N   1 
ATOM   92   C CA  . GLU A 1 16 ? 13.74215 7.04213   22.10003 1.000 27.95330  ?  15  GLU A CA  1 
ATOM   93   C C   . GLU A 1 16 ? 14.77160 7.47090   23.12395 1.000 42.25052  ?  15  GLU A C   1 
ATOM   94   O O   . GLU A 1 16 ? 14.62412 8.54167   23.71876 1.000 35.78586  ?  15  GLU A O   1 
ATOM   95   C CB  . GLU A 1 16 ? 12.34284 7.14274   22.71396 1.000 28.21520  ?  15  GLU A CB  1 
ATOM   96   C CG  . GLU A 1 16 ? 11.26016 6.92492   21.68857 1.000 28.44304  ?  15  GLU A CG  1 
ATOM   97   C CD  . GLU A 1 16 ? 9.88041  7.02029   22.27200 1.000 40.33885  ?  15  GLU A CD  1 
ATOM   98   O OE1 . GLU A 1 16 ? 9.76566  7.42925   23.44906 1.000 52.39719  ?  15  GLU A OE1 1 
ATOM   99   O OE2 . GLU A 1 16 ? 8.91540  6.69285   21.54244 1.000 38.60404  ?  15  GLU A OE2 1 
ATOM   100  N N   . GLY A 1 17 ? 15.78812 6.65921   23.35873 1.000 27.50211  ?  16  GLY A N   1 
ATOM   101  C CA  . GLY A 1 17 ? 16.87219 7.03920   24.23242 1.000 35.51233  ?  16  GLY A CA  1 
ATOM   102  C C   . GLY A 1 17 ? 16.74399 6.60838   25.67480 1.000 31.23616  ?  16  GLY A C   1 
ATOM   103  O O   . GLY A 1 17 ? 17.55040 7.04019   26.49565 1.000 34.99723  ?  16  GLY A O   1 
ATOM   104  N N   . LYS A 1 18 ? 15.77535 5.76939   26.01625 1.000 27.15646  ?  17  LYS A N   1 
ATOM   105  C CA  . LYS A 1 18 ? 15.65634 5.33119   27.39882 1.000 27.07415  ?  17  LYS A CA  1 
ATOM   106  C C   . LYS A 1 18 ? 16.47942 4.06371   27.67867 1.000 37.89625  ?  17  LYS A C   1 
ATOM   107  O O   . LYS A 1 18 ? 16.97848 3.38195   26.77094 1.000 26.44365  ?  17  LYS A O   1 
ATOM   108  C CB  . LYS A 1 18 ? 14.18830 5.09910   27.73698 1.000 27.70578  ?  17  LYS A CB  1 
ATOM   109  C CG  . LYS A 1 18 ? 13.30869 6.32262   27.48585 1.000 29.34571  ?  17  LYS A CG  1 
ATOM   110  C CD  . LYS A 1 18 ? 11.84258 5.92739   27.37370 1.000 38.13267  ?  17  LYS A CD  1 
ATOM   111  C CE  . LYS A 1 18 ? 10.92797 7.14449   27.37985 1.000 36.32991  ?  17  LYS A CE  1 
ATOM   112  N NZ  . LYS A 1 18 ? 9.51472  6.71540   27.59538 1.000 46.74380  ?  17  LYS A NZ  1 
ATOM   113  N N   . LYS A 1 19 ? 16.61811 3.76591   28.97394 1.000 26.61161  ?  18  LYS A N   1 
ATOM   114  C CA  . LYS A 1 19 ? 17.28836 2.57258   29.48252 1.000 26.29189  ?  18  LYS A CA  1 
ATOM   115  C C   . LYS A 1 19 ? 16.24873 1.52906   29.87245 1.000 28.60214  ?  18  LYS A C   1 
ATOM   116  O O   . LYS A 1 19 ? 15.18974 1.87493   30.39162 1.000 27.50756  ?  18  LYS A O   1 
ATOM   117  C CB  . LYS A 1 19 ? 18.13405 2.92003   30.70504 1.000 26.27583  ?  18  LYS A CB  1 
ATOM   118  C CG  . LYS A 1 19 ? 19.15040 4.02442   30.45772 1.000 29.45662  ?  18  LYS A CG  1 
ATOM   119  C CD  . LYS A 1 19 ? 20.01044 4.28151   31.69374 1.000 26.33488  ?  18  LYS A CD  1 
ATOM   120  C CE  . LYS A 1 19 ? 19.19149 4.91061   32.79563 1.000 32.84113  ?  18  LYS A CE  1 
ATOM   121  N NZ  . LYS A 1 19 ? 20.07914 5.39873   33.90932 1.000 37.31682  ?  18  LYS A NZ  1 
ATOM   122  N N   . VAL A 1 20 ? 16.54668 0.25252   29.63572 1.000 26.00079  ?  19  VAL A N   1 
ATOM   123  C CA  . VAL A 1 20 ? 15.60361 -0.82505  29.94194 1.000 25.99805  ?  19  VAL A CA  1 
ATOM   124  C C   . VAL A 1 20 ? 16.34124 -1.97114  30.61655 1.000 30.16076  ?  19  VAL A C   1 
ATOM   125  O O   . VAL A 1 20 ? 17.53665 -2.17669  30.39525 1.000 27.21067  ?  19  VAL A O   1 
ATOM   126  C CB  . VAL A 1 20 ? 14.88229 -1.34814  28.68088 1.000 25.98828  ?  19  VAL A CB  1 
ATOM   127  C CG1 . VAL A 1 20 ? 14.02948 -0.27001  28.06990 1.000 26.78462  ?  19  VAL A CG1 1 
ATOM   128  C CG2 . VAL A 1 20 ? 15.89650 -1.86266  27.66120 1.000 25.67778  ?  19  VAL A CG2 1 
ATOM   129  N N   . SER A 1 21 ? 15.61177 -2.75291  31.41401 1.000 25.79808  ?  20  SER A N   1 
ATOM   130  C CA  . SER A 1 21 ? 16.15846 -4.00075  31.93715 1.000 25.57824  ?  20  SER A CA  1 
ATOM   131  C C   . SER A 1 21 ? 15.02505 -4.99250  32.12531 1.000 27.70657  ?  20  SER A C   1 
ATOM   132  O O   . SER A 1 21 ? 13.85034 -4.66030  31.96525 1.000 27.96817  ?  20  SER A O   1 
ATOM   133  C CB  . SER A 1 21 ? 16.90047 -3.80549  33.25947 1.000 26.45282  ?  20  SER A CB  1 
ATOM   134  O OG  . SER A 1 21 ? 15.99465 -3.40628  34.26473 1.000 37.61301  ?  20  SER A OG  1 
ATOM   135  N N   . ARG A 1 22 ? 15.39799 -6.22260  32.46547 1.000 25.50052  ?  21  ARG A N   1 
ATOM   136  C CA  . ARG A 1 22 ? 14.45597 -7.31471  32.65140 1.000 25.58574  ?  21  ARG A CA  1 
ATOM   137  C C   . ARG A 1 22 ? 14.46911 -7.76370  34.10168 1.000 27.21154  ?  21  ARG A C   1 
ATOM   138  O O   . ARG A 1 22 ? 15.53832 -7.88800  34.70643 1.000 25.54741  ?  21  ARG A O   1 
ATOM   139  C CB  . ARG A 1 22 ? 14.80578 -8.50377  31.76141 1.000 25.32067  ?  21  ARG A CB  1 
ATOM   140  C CG  . ARG A 1 22 ? 14.25309 -8.41027  30.36998 1.000 26.98281  ?  21  ARG A CG  1 
ATOM   141  C CD  . ARG A 1 22 ? 14.46954 -9.74447  29.66972 1.000 28.21993  ?  21  ARG A CD  1 
ATOM   142  N NE  . ARG A 1 22 ? 13.73770 -10.78667 30.38411 1.000 25.20422  ?  21  ARG A NE  1 
ATOM   143  C CZ  . ARG A 1 22 ? 14.15976 -12.02658 30.56398 1.000 28.57397  ?  21  ARG A CZ  1 
ATOM   144  N NH1 . ARG A 1 22 ? 15.26608 -12.47477 29.98505 1.000 24.71536  ?  21  ARG A NH1 1 
ATOM   145  N NH2 . ARG A 1 22 ? 13.46178 -12.83444 31.35621 1.000 27.09641  ?  21  ARG A NH2 1 
ATOM   146  N N   . GLU A 1 23 ? 13.27200 -8.00980  34.65599 1.000 30.36266  ?  22  GLU A N   1 
ATOM   147  C CA  . GLU A 1 23 ? 13.18990 -8.56816  36.00222 1.000 30.97252  ?  22  GLU A CA  1 
ATOM   148  C C   . GLU A 1 23 ? 13.80421 -9.96260  36.06763 1.000 25.11099  ?  22  GLU A C   1 
ATOM   149  O O   . GLU A 1 23 ? 14.40156 -10.33007 37.08494 1.000 31.37541  ?  22  GLU A O   1 
ATOM   150  C CB  . GLU A 1 23 ? 11.72993 -8.59855  36.47940 1.000 38.43139  ?  22  GLU A CB  1 
ATOM   151  C CG  . GLU A 1 23 ? 11.16729 -7.21611  36.80039 1.000 52.73436  ?  22  GLU A CG  1 
ATOM   152  C CD  . GLU A 1 23 ? 9.74723  -7.25906  37.32690 1.000 68.95125  ?  22  GLU A CD  1 
ATOM   153  O OE1 . GLU A 1 23 ? 9.29030  -8.35504  37.72196 1.000 80.65790  ?  22  GLU A OE1 1 
ATOM   154  O OE2 . GLU A 1 23 ? 9.08699  -6.19582  37.34123 1.000 63.63979  ?  22  GLU A OE2 1 
ATOM   155  N N   . GLY A 1 24 ? 13.68126 -10.75334 35.00170 1.000 25.85145  ?  23  GLY A N   1 
ATOM   156  C CA  . GLY A 1 24 ? 14.22120 -12.09772 35.01489 1.000 24.81463  ?  23  GLY A CA  1 
ATOM   157  C C   . GLY A 1 24 ? 15.71636 -12.25204 34.78214 1.000 24.07233  ?  23  GLY A C   1 
ATOM   158  O O   . GLY A 1 24 ? 16.20065 -13.38451 34.73308 1.000 28.28410  ?  23  GLY A O   1 
ATOM   159  N N   . TRP A 1 25 ? 16.46490 -11.16333 34.62748 1.000 23.56077  ?  24  TRP A N   1 
ATOM   160  C CA  . TRP A 1 25 ? 17.91136 -11.26401 34.49180 1.000 22.99819  ?  24  TRP A CA  1 
ATOM   161  C C   . TRP A 1 25 ? 18.54094 -11.75888 35.78971 1.000 23.64347  ?  24  TRP A C   1 
ATOM   162  O O   . TRP A 1 25 ? 18.13450 -11.36480 36.88650 1.000 28.03715  ?  24  TRP A O   1 
ATOM   163  C CB  . TRP A 1 25 ? 18.48939 -9.90574  34.11493 1.000 22.62778  ?  24  TRP A CB  1 
ATOM   164  C CG  . TRP A 1 25 ? 18.32985 -9.55675  32.66802 1.000 22.32836  ?  24  TRP A CG  1 
ATOM   165  C CD1 . TRP A 1 25 ? 17.90693 -10.38168 31.65430 1.000 22.31372  ?  24  TRP A CD1 1 
ATOM   166  C CD2 . TRP A 1 25 ? 18.60338 -8.28836  32.06755 1.000 22.07816  ?  24  TRP A CD2 1 
ATOM   167  N NE1 . TRP A 1 25 ? 17.91407 -9.68902  30.45974 1.000 22.09204  ?  24  TRP A NE1 1 
ATOM   168  C CE2 . TRP A 1 25 ? 18.33117 -8.40544  30.69065 1.000 21.94346  ?  24  TRP A CE2 1 
ATOM   169  C CE3 . TRP A 1 25 ? 19.04871 -7.06079  32.56618 1.000 22.01272  ?  24  TRP A CE3 1 
ATOM   170  C CZ2 . TRP A 1 25 ? 18.50303 -7.34400  29.80517 1.000 21.75791  ?  24  TRP A CZ2 1 
ATOM   171  C CZ3 . TRP A 1 25 ? 19.19796 -5.99842  31.68588 1.000 21.80166  ?  24  TRP A CZ3 1 
ATOM   172  C CH2 . TRP A 1 25 ? 18.93946 -6.15565  30.31725 1.000 21.67851  ?  24  TRP A CH2 1 
ATOM   173  N N   . ASN A 1 26 ? 19.57058 -12.60133 35.65848 1.000 23.79266  ?  25  ASN A N   1 
ATOM   174  C CA  . ASN A 1 26 ? 20.23726 -13.16352 36.83187 1.000 23.21885  ?  25  ASN A CA  1 
ATOM   175  C C   . ASN A 1 26 ? 21.07124 -12.10753 37.54671 1.000 31.94959  ?  25  ASN A C   1 
ATOM   176  O O   . ASN A 1 26 ? 20.99019 -11.96292 38.77465 1.000 28.01392  ?  25  ASN A O   1 
ATOM   177  C CB  . ASN A 1 26 ? 21.10048 -14.35523 36.41798 1.000 23.01608  ?  25  ASN A CB  1 
ATOM   178  C CG  . ASN A 1 26 ? 20.27337 -15.56137 35.98054 1.000 23.19356  ?  25  ASN A CG  1 
ATOM   179  O OD1 . ASN A 1 26 ? 19.21305 -15.83854 36.54519 1.000 28.38962  ?  25  ASN A OD1 1 
ATOM   180  N ND2 . ASN A 1 26 ? 20.75065 -16.27443 34.96530 1.000 24.65439  ?  25  ASN A ND2 1 
ATOM   181  N N   . GLY A 1 27 ? 21.87895 -11.35530 36.79517 1.000 26.46562  ?  26  GLY A N   1 
ATOM   182  C CA  . GLY A 1 27 ? 22.56079 -10.20846 37.36856 1.000 22.99284  ?  26  GLY A CA  1 
ATOM   183  C C   . GLY A 1 27 ? 21.60326 -9.06171  37.64108 1.000 30.36286  ?  26  GLY A C   1 
ATOM   184  O O   . GLY A 1 27 ? 20.60580 -8.87146  36.94488 1.000 26.15101  ?  26  GLY A O   1 
ATOM   185  N N   . LYS A 1 28 ? 21.90884 -8.28804  38.68239 1.000 23.21317  ?  27  LYS A N   1 
ATOM   186  C CA  . LYS A 1 28 ? 21.04263 -7.20574  39.13687 1.000 28.53580  ?  27  LYS A CA  1 
ATOM   187  C C   . LYS A 1 28 ? 21.66980 -5.84970  38.84885 1.000 23.80278  ?  27  LYS A C   1 
ATOM   188  O O   . LYS A 1 28 ? 22.89282 -5.69831  38.83107 1.000 23.04421  ?  27  LYS A O   1 
ATOM   189  C CB  . LYS A 1 28 ? 20.74523 -7.30534  40.63820 1.000 29.35171  ?  27  LYS A CB  1 
ATOM   190  C CG  . LYS A 1 28 ? 20.07485 -8.60686  41.08181 1.000 34.37832  ?  27  LYS A CG  1 
ATOM   191  C CD  . LYS A 1 28 ? 18.86604 -8.90953  40.21980 1.000 31.79871  ?  27  LYS A CD  1 
ATOM   192  C CE  . LYS A 1 28 ? 18.31017 -10.28950 40.49970 1.000 35.95783  ?  27  LYS A CE  1 
ATOM   193  N NZ  . LYS A 1 28 ? 17.16445 -10.55683 39.57596 1.000 43.41847  ?  27  LYS A NZ  1 
ATOM   194  N N   . GLY A 1 29 ? 20.81735 -4.84654  38.66495 1.000 23.31861  ?  28  GLY A N   1 
ATOM   195  C CA  . GLY A 1 29 ? 21.30894 -3.49541  38.43653 1.000 23.13533  ?  28  GLY A CA  1 
ATOM   196  C C   . GLY A 1 29 ? 21.81816 -3.21943  37.03790 1.000 28.23754  ?  28  GLY A C   1 
ATOM   197  O O   . GLY A 1 29 ? 22.45364 -2.17778  36.82339 1.000 24.76022  ?  28  GLY A O   1 
ATOM   198  N N   . MET A 1 30 ? 21.54366 -4.10273  36.07386 1.000 22.28441  ?  29  MET A N   1 
ATOM   199  C CA  . MET A 1 30 ? 21.99860 -3.92763  34.70124 1.000 22.66150  ?  29  MET A CA  1 
ATOM   200  C C   . MET A 1 30 ? 20.94397 -3.17872  33.88228 1.000 25.12993  ?  29  MET A C   1 
ATOM   201  O O   . MET A 1 30 ? 19.75500 -3.16166  34.21258 1.000 25.65086  ?  29  MET A O   1 
ATOM   202  C CB  . MET A 1 30 ? 22.31773 -5.29197  34.06943 1.000 21.59687  ?  29  MET A CB  1 
ATOM   203  C CG  . MET A 1 30 ? 23.40124 -6.09391  34.80197 1.000 21.64652  ?  29  MET A CG  1 
ATOM   204  S SD  . MET A 1 30 ? 23.81783 -7.67592  33.99735 1.000 24.89312  ?  29  MET A SD  1 
ATOM   205  C CE  . MET A 1 30 ? 22.26191 -8.50876  34.14269 1.000 21.68265  ?  29  MET A CE  1 
ATOM   206  N N   . PHE A 1 31 ? 21.38665 -2.54886  32.79704 1.000 21.63419  ?  30  PHE A N   1 
ATOM   207  C CA  . PHE A 1 31 ? 20.41660 -1.96621  31.87718 1.000 23.79452  ?  30  PHE A CA  1 
ATOM   208  C C   . PHE A 1 31 ? 21.03887 -1.91369  30.49321 1.000 27.99385  ?  30  PHE A C   1 
ATOM   209  O O   . PHE A 1 31 ? 22.26603 -1.89406  30.34990 1.000 23.39942  ?  30  PHE A O   1 
ATOM   210  C CB  . PHE A 1 31 ? 19.94820 -0.55739  32.31853 1.000 21.88233  ?  30  PHE A CB  1 
ATOM   211  C CG  . PHE A 1 31 ? 21.06023 0.42954   32.45721 1.000 21.71176  ?  30  PHE A CG  1 
ATOM   212  C CD1 . PHE A 1 31 ? 21.50014 1.15661   31.36280 1.000 21.50837  ?  30  PHE A CD1 1 
ATOM   213  C CD2 . PHE A 1 31 ? 21.69080 0.60781   33.68359 1.000 21.83775  ?  30  PHE A CD2 1 
ATOM   214  C CE1 . PHE A 1 31 ? 22.57264 2.04797   31.47685 1.000 22.80366  ?  30  PHE A CE1 1 
ATOM   215  C CE2 . PHE A 1 31 ? 22.76069 1.47794   33.81250 1.000 21.75932  ?  30  PHE A CE2 1 
ATOM   216  C CZ  . PHE A 1 31 ? 23.19936 2.21702   32.70428 1.000 21.54673  ?  30  PHE A CZ  1 
ATOM   217  N N   . ALA A 1 32 ? 20.17463 -1.88185  29.47458 1.000 21.37431  ?  31  ALA A N   1 
ATOM   218  C CA  . ALA A 1 32 ? 20.59664 -1.72314  28.09197 1.000 21.18884  ?  31  ALA A CA  1 
ATOM   219  C C   . ALA A 1 32 ? 20.17722 -0.35381  27.56233 1.000 21.37412  ?  31  ALA A C   1 
ATOM   220  O O   . ALA A 1 32 ? 19.23552 0.27085   28.05713 1.000 21.70300  ?  31  ALA A O   1 
ATOM   221  C CB  . ALA A 1 32 ? 20.02285 -2.83668  27.20376 1.000 21.24123  ?  31  ALA A CB  1 
ATOM   222  N N   . TYR A 1 33 ? 20.88170 0.11416   26.53113 1.000 22.42376  ?  32  TYR A N   1 
ATOM   223  C CA  . TYR A 1 33 ? 20.57834 1.42011   25.96042 1.000 21.44772  ?  32  TYR A CA  1 
ATOM   224  C C   . TYR A 1 33 ? 21.09303 1.46320   24.52735 1.000 27.88027  ?  32  TYR A C   1 
ATOM   225  O O   . TYR A 1 33 ? 21.93678 0.65564   24.11957 1.000 22.41015  ?  32  TYR A O   1 
ATOM   226  C CB  . TYR A 1 33 ? 21.16820 2.55907   26.80309 1.000 21.42232  ?  32  TYR A CB  1 
ATOM   227  C CG  . TYR A 1 33 ? 22.67394 2.54806   26.93268 1.000 21.13839  ?  32  TYR A CG  1 
ATOM   228  C CD1 . TYR A 1 33 ? 23.30453 1.76550   27.88944 1.000 22.61965  ?  32  TYR A CD1 1 
ATOM   229  C CD2 . TYR A 1 33 ? 23.46938 3.33864   26.10631 1.000 21.39195  ?  32  TYR A CD2 1 
ATOM   230  C CE1 . TYR A 1 33 ? 24.68614 1.76497   28.02092 1.000 20.84644  ?  32  TYR A CE1 1 
ATOM   231  C CE2 . TYR A 1 33 ? 24.84617 3.35336   26.23752 1.000 26.12320  ?  32  TYR A CE2 1 
ATOM   232  C CZ  . TYR A 1 33 ? 25.45099 2.55751   27.18763 1.000 28.61106  ?  32  TYR A CZ  1 
ATOM   233  O OH  . TYR A 1 33 ? 26.82483 2.56668   27.29198 1.000 29.42848  ?  32  TYR A OH  1 
ATOM   234  N N   . TYR A 1 34 ? 20.55665 2.42000   23.77034 1.000 22.59281  ?  33  TYR A N   1 
ATOM   235  C CA  . TYR A 1 34 ? 20.81111 2.57444   22.33932 1.000 21.85610  ?  33  TYR A CA  1 
ATOM   236  C C   . TYR A 1 34 ? 21.95875 3.54982   22.11381 1.000 24.10698  ?  33  TYR A C   1 
ATOM   237  O O   . TYR A 1 34 ? 22.06721 4.55554   22.82505 1.000 24.60991  ?  33  TYR A O   1 
ATOM   238  C CB  . TYR A 1 34 ? 19.51427 3.09324   21.67995 1.000 23.91303  ?  33  TYR A CB  1 
ATOM   239  C CG  . TYR A 1 34 ? 19.57719 3.43838   20.19443 1.000 22.74332  ?  33  TYR A CG  1 
ATOM   240  C CD1 . TYR A 1 34 ? 19.96608 4.70969   19.76268 1.000 33.49531  ?  33  TYR A CD1 1 
ATOM   241  C CD2 . TYR A 1 34 ? 19.24221 2.49659   19.23156 1.000 22.89536  ?  33  TYR A CD2 1 
ATOM   242  C CE1 . TYR A 1 34 ? 20.02353 5.01545   18.40645 1.000 24.29567  ?  33  TYR A CE1 1 
ATOM   243  C CE2 . TYR A 1 34 ? 19.29597 2.79840   17.87371 1.000 24.46806  ?  33  TYR A CE2 1 
ATOM   244  C CZ  . TYR A 1 34 ? 19.66065 4.06370   17.47895 1.000 29.20114  ?  33  TYR A CZ  1 
ATOM   245  O OH  . TYR A 1 34 ? 19.71537 4.33263   16.13577 1.000 27.21970  ?  33  TYR A OH  1 
ATOM   246  N N   . VAL A 1 35 ? 22.80351 3.27274   21.12425 1.000 21.75670  ?  34  VAL A N   1 
ATOM   247  C CA  . VAL A 1 35 ? 23.89385 4.16334   20.74543 1.000 27.72557  ?  34  VAL A CA  1 
ATOM   248  C C   . VAL A 1 35 ? 23.77233 4.47142   19.25679 1.000 22.71130  ?  34  VAL A C   1 
ATOM   249  O O   . VAL A 1 35 ? 23.76367 3.54736   18.44606 1.000 22.52516  ?  34  VAL A O   1 
ATOM   250  C CB  . VAL A 1 35 ? 25.28353 3.57768   21.05433 1.000 28.64606  ?  34  VAL A CB  1 
ATOM   251  C CG1 . VAL A 1 35 ? 26.33567 4.61542   20.72695 1.000 27.06971  ?  34  VAL A CG1 1 
ATOM   252  C CG2 . VAL A 1 35 ? 25.38270 3.15809   22.51156 1.000 29.46280  ?  34  VAL A CG2 1 
ATOM   253  N N   . PRO A 1 36 ? 23.70260 5.73748   18.85028 1.000 33.35404  ?  35  PRO A N   1 
ATOM   254  C CA  . PRO A 1 36 ? 23.51497 6.04239   17.42693 1.000 32.88042  ?  35  PRO A CA  1 
ATOM   255  C C   . PRO A 1 36 ? 24.75509 5.71095   16.60935 1.000 33.21012  ?  35  PRO A C   1 
ATOM   256  O O   . PRO A 1 36 ? 25.86666 5.59435   17.12675 1.000 33.88716  ?  35  PRO A O   1 
ATOM   257  C CB  . PRO A 1 36 ? 23.24686 7.55626   17.40739 1.000 36.33172  ?  35  PRO A CB  1 
ATOM   258  C CG  . PRO A 1 36 ? 23.11649 7.97988   18.83781 1.000 38.53485  ?  35  PRO A CG  1 
ATOM   259  C CD  . PRO A 1 36 ? 23.80634 6.95228   19.66814 1.000 34.22024  ?  35  PRO A CD  1 
ATOM   260  N N   . GLY A 1 37 ? 24.54906 5.57997   15.29492 1.000 32.83265  ?  36  GLY A N   1 
ATOM   261  C CA  . GLY A 1 37 ? 25.64930 5.40205   14.36829 1.000 33.23467  ?  36  GLY A CA  1 
ATOM   262  C C   . GLY A 1 37 ? 26.35179 6.71361   14.04322 1.000 34.06851  ?  36  GLY A C   1 
ATOM   263  O O   . GLY A 1 37 ? 25.98464 7.79061   14.50796 1.000 34.42944  ?  36  GLY A O   1 
ATOM   264  N N   . GLY A 1 38 ? 27.39780 6.61795   13.23153 1.000 34.53080  ?  37  GLY A N   1 
ATOM   265  C CA  . GLY A 1 38 ? 28.13124 7.81994   12.88393 1.000 35.49888  ?  37  GLY A CA  1 
ATOM   266  C C   . GLY A 1 38 ? 29.15264 7.59324   11.79163 1.000 38.62221  ?  37  GLY A C   1 
ATOM   267  O O   . GLY A 1 38 ? 29.12273 6.58718   11.07663 1.000 37.15284  ?  37  GLY A O   1 
ATOM   268  N N   . VAL A 1 39 ? 30.04773 8.57638   11.66639 1.000 36.98196  ?  38  VAL A N   1 
ATOM   269  C CA  . VAL A 1 39 ? 31.17207 8.55279   10.73699 1.000 37.90278  ?  38  VAL A CA  1 
ATOM   270  C C   . VAL A 1 39 ? 32.42693 8.99410   11.48506 1.000 44.72431  ?  38  VAL A C   1 
ATOM   271  O O   . VAL A 1 39 ? 32.37242 9.90970   12.31241 1.000 60.77434  ?  38  VAL A O   1 
ATOM   272  C CB  . VAL A 1 39 ? 30.91513 9.46754   9.51692  1.000 43.37767  ?  38  VAL A CB  1 
ATOM   273  C CG1 . VAL A 1 39 ? 32.08690 9.43487   8.55550  1.000 60.97287  ?  38  VAL A CG1 1 
ATOM   274  C CG2 . VAL A 1 39 ? 29.64375 9.05951   8.80157  1.000 44.70593  ?  38  VAL A CG2 1 
ATOM   275  N N   . TYR A 1 40 ? 33.55517 8.33974   11.20393 1.000 49.83459  ?  39  TYR A N   1 
ATOM   276  C CA  . TYR A 1 40 ? 34.85099 8.78755   11.69905 1.000 56.78060  ?  39  TYR A CA  1 
ATOM   277  C C   . TYR A 1 40 ? 35.89208 8.64621   10.59260 1.000 71.09195  ?  39  TYR A C   1 
ATOM   278  O O   . TYR A 1 40 ? 35.73699 7.84743   9.66109  1.000 62.37911  ?  39  TYR A O   1 
ATOM   279  C CB  . TYR A 1 40 ? 35.28842 8.02099   12.96005 1.000 58.25782  ?  39  TYR A CB  1 
ATOM   280  C CG  . TYR A 1 40 ? 35.53794 6.54079   12.75502 1.000 71.98958  ?  39  TYR A CG  1 
ATOM   281  C CD1 . TYR A 1 40 ? 34.50372 5.62026   12.89270 1.000 72.78824  ?  39  TYR A CD1 1 
ATOM   282  C CD2 . TYR A 1 40 ? 36.81175 6.05933   12.43754 1.000 62.94953  ?  39  TYR A CD2 1 
ATOM   283  C CE1 . TYR A 1 40 ? 34.72376 4.25801   12.71895 1.000 69.55452  ?  39  TYR A CE1 1 
ATOM   284  C CE2 . TYR A 1 40 ? 37.04333 4.69775   12.25312 1.000 58.77046  ?  39  TYR A CE2 1 
ATOM   285  C CZ  . TYR A 1 40 ? 35.99254 3.80217   12.40097 1.000 67.55252  ?  39  TYR A CZ  1 
ATOM   286  O OH  . TYR A 1 40 ? 36.19531 2.44808   12.23507 1.000 57.24470  ?  39  TYR A OH  1 
ATOM   287  N N   . LYS A 1 41 ? 36.96672 9.43266   10.71375 1.000 63.25629  ?  40  LYS A N   1 
ATOM   288  C CA  . LYS A 1 41 ? 37.98378 9.51639   9.66947  1.000 72.25375  ?  40  LYS A CA  1 
ATOM   289  C C   . LYS A 1 41 ? 39.00344 8.38976   9.78660  1.000 60.60669  ?  40  LYS A C   1 
ATOM   290  O O   . LYS A 1 41 ? 39.44808 8.04688   10.88542 1.000 65.94558  ?  40  LYS A O   1 
ATOM   291  C CB  . LYS A 1 41 ? 38.70934 10.86046  9.73773  1.000 75.79292  ?  40  LYS A CB  1 
ATOM   292  C CG  . LYS A 1 41 ? 37.80312 12.07289  9.64732  1.000 78.90117  ?  40  LYS A CG  1 
ATOM   293  C CD  . LYS A 1 41 ? 38.59278 13.35177  9.86458  1.000 87.87825  ?  40  LYS A CD  1 
ATOM   294  C CE  . LYS A 1 41 ? 39.65602 13.52107  8.79825  1.000 80.75998  ?  40  LYS A CE  1 
ATOM   295  N NZ  . LYS A 1 41 ? 39.04390 13.53848  7.44457  1.000 72.85793  ?  40  LYS A NZ  1 
ATOM   296  N N   . SER A 1 42 ? 39.37303 7.81471   8.64159  1.000 61.92299  ?  41  SER A N   1 
ATOM   297  C CA  . SER A 1 42 ? 40.48305 6.86993   8.60684  1.000 75.63449  ?  41  SER A CA  1 
ATOM   298  C C   . SER A 1 42 ? 41.77975 7.61551   8.88350  1.000 74.77338  ?  41  SER A C   1 
ATOM   299  O O   . SER A 1 42 ? 42.07989 8.61858   8.22677  1.000 64.14537  ?  41  SER A O   1 
ATOM   300  C CB  . SER A 1 42 ? 40.55817 6.16184   7.25190  1.000 68.45307  ?  41  SER A CB  1 
ATOM   301  O OG  . SER A 1 42 ? 39.65500 5.06918   7.17346  1.000 62.73327  ?  41  SER A OG  1 
ATOM   302  N N   . GLN A 1 43 ? 42.54874 7.13460   9.86175  1.000 66.91955  ?  42  GLN A N   1 
ATOM   303  C CA  . GLN A 1 43 ? 43.70193 7.89465   10.32351 1.000 73.26266  ?  42  GLN A CA  1 
ATOM   304  C C   . GLN A 1 43 ? 45.02764 7.41375   9.75182  1.000 64.97601  ?  42  GLN A C   1 
ATOM   305  O O   . GLN A 1 43 ? 45.97723 8.20303   9.69096  1.000 67.13843  ?  42  GLN A O   1 
ATOM   306  C CB  . GLN A 1 43 ? 43.76283 7.88813   11.85459 1.000 66.03149  ?  42  GLN A CB  1 
ATOM   307  C CG  . GLN A 1 43 ? 42.73204 8.81507   12.49661 1.000 76.09864  ?  42  GLN A CG  1 
ATOM   308  C CD  . GLN A 1 43 ? 42.80103 10.24571  11.95993 1.000 77.92002  ?  42  GLN A CD  1 
ATOM   309  O OE1 . GLN A 1 43 ? 43.88411 10.78692  11.73226 1.000 91.27558  ?  42  GLN A OE1 1 
ATOM   310  N NE2 . GLN A 1 43 ? 41.63876 10.85874  11.75208 1.000 74.38834  ?  42  GLN A NE2 1 
ATOM   311  N N   . THR A 1 44 ? 45.11801 6.16438   9.31855  1.000 55.41436  ?  43  THR A N   1 
ATOM   312  C CA  . THR A 1 44 ? 46.31353 5.66692   8.65961  1.000 60.85613  ?  43  THR A CA  1 
ATOM   313  C C   . THR A 1 44 ? 45.96344 5.18982   7.25757  1.000 58.43482  ?  43  THR A C   1 
ATOM   314  O O   . THR A 1 44 ? 44.82105 4.80950   6.97944  1.000 61.49861  ?  43  THR A O   1 
ATOM   315  C CB  . THR A 1 44 ? 46.96165 4.51917   9.44516  1.000 62.26231  ?  43  THR A CB  1 
ATOM   316  O OG1 . THR A 1 44 ? 46.06872 3.40112   9.47508  1.000 56.77405  ?  43  THR A OG1 1 
ATOM   317  C CG2 . THR A 1 44 ? 47.28724 4.94742   10.87184 1.000 55.56131  ?  43  THR A CG2 1 
ATOM   318  N N   . ASP A 1 45 ? 46.96199 5.21512   6.37123  1.000 57.15282  ?  44  ASP A N   1 
ATOM   319  C CA  . ASP A 1 45 ? 46.75768 4.69351   5.02405  1.000 63.64696  ?  44  ASP A CA  1 
ATOM   320  C C   . ASP A 1 45 ? 46.43437 3.20720   5.04739  1.000 61.20005  ?  44  ASP A C   1 
ATOM   321  O O   . ASP A 1 45 ? 45.78055 2.70385   4.12742  1.000 54.56844  ?  44  ASP A O   1 
ATOM   322  C CB  . ASP A 1 45 ? 47.98960 4.94751   4.15476  1.000 50.99816  ?  44  ASP A CB  1 
ATOM   323  C CG  . ASP A 1 45 ? 48.39117 6.40335   4.12680  1.000 66.86487  ?  44  ASP A CG  1 
ATOM   324  O OD1 . ASP A 1 45 ? 47.52998 7.27000   4.40418  1.000 69.45571  ?  44  ASP A OD1 1 
ATOM   325  O OD2 . ASP A 1 45 ? 49.57401 6.67787   3.83236  1.000 73.52994  ?  44  ASP A OD2 1 
ATOM   326  N N   . VAL A 1 46 ? 46.89137 2.48527   6.07518  1.000 50.56526  ?  45  VAL A N   1 
ATOM   327  C CA  . VAL A 1 46 ? 46.49968 1.08477   6.21782  1.000 58.52503  ?  45  VAL A CA  1 
ATOM   328  C C   . VAL A 1 46 ? 44.99671 0.98419   6.44489  1.000 70.53966  ?  45  VAL A C   1 
ATOM   329  O O   . VAL A 1 46 ? 44.30371 0.17978   5.80737  1.000 62.56303  ?  45  VAL A O   1 
ATOM   330  C CB  . VAL A 1 46 ? 47.28186 0.40864   7.35770  1.000 47.49683  ?  45  VAL A CB  1 
ATOM   331  C CG1 . VAL A 1 46 ? 46.84409 -1.04521  7.48652  1.000 42.70935  ?  45  VAL A CG1 1 
ATOM   332  C CG2 . VAL A 1 46 ? 48.78852 0.50813   7.12291  1.000 43.25544  ?  45  VAL A CG2 1 
ATOM   333  N N   . ILE A 1 47 ? 44.47311 1.80577   7.35983  1.000 62.26416  ?  46  ILE A N   1 
ATOM   334  C CA  . ILE A 1 47 ? 43.03160 1.87360   7.57490  1.000 61.98863  ?  46  ILE A CA  1 
ATOM   335  C C   . ILE A 1 47 ? 42.34121 2.48721   6.36418  1.000 58.40421  ?  46  ILE A C   1 
ATOM   336  O O   . ILE A 1 47 ? 41.26490 2.03776   5.95192  1.000 62.91767  ?  46  ILE A O   1 
ATOM   337  C CB  . ILE A 1 47 ? 42.72764 2.65993   8.86343  1.000 56.00969  ?  46  ILE A CB  1 
ATOM   338  C CG1 . ILE A 1 47 ? 43.35476 1.95371   10.07369 1.000 53.36803  ?  46  ILE A CG1 1 
ATOM   339  C CG2 . ILE A 1 47 ? 41.21985 2.83985   9.03020  1.000 52.19489  ?  46  ILE A CG2 1 
ATOM   340  C CD1 . ILE A 1 47 ? 43.44457 2.81324   11.33169 1.000 46.51739  ?  46  ILE A CD1 1 
ATOM   341  N N   . LYS A 1 48 ? 42.95481 3.51536   5.77032  1.000 56.15293  ?  47  LYS A N   1 
ATOM   342  C CA  . LYS A 1 48 ? 42.38010 4.15829   4.59192  1.000 52.79858  ?  47  LYS A CA  1 
ATOM   343  C C   . LYS A 1 48 ? 42.19723 3.16664   3.44728  1.000 55.82518  ?  47  LYS A C   1 
ATOM   344  O O   . LYS A 1 48 ? 41.20469 3.22900   2.71513  1.000 70.47405  ?  47  LYS A O   1 
ATOM   345  C CB  . LYS A 1 48 ? 43.26476 5.33033   4.16500  1.000 59.68172  ?  47  LYS A CB  1 
ATOM   346  C CG  . LYS A 1 48 ? 42.81601 6.05192   2.90861  1.000 61.25821  ?  47  LYS A CG  1 
ATOM   347  C CD  . LYS A 1 48 ? 43.72333 7.24619   2.62328  1.000 69.31283  ?  47  LYS A CD  1 
ATOM   348  C CE  . LYS A 1 48 ? 43.45718 7.83321   1.24148  1.000 59.75659  ?  47  LYS A CE  1 
ATOM   349  N NZ  . LYS A 1 48 ? 42.04359 8.26582   1.09502  1.000 59.27856  ?  47  LYS A NZ  1 
ATOM   350  N N   . ASN A 1 49 ? 43.13905 2.23852   3.27887  1.000 57.66477  ?  48  ASN A N   1 
ATOM   351  C CA  . ASN A 1 49 ? 43.00089 1.23973   2.22391  1.000 68.37370  ?  48  ASN A CA  1 
ATOM   352  C C   . ASN A 1 49 ? 41.89975 0.23795   2.55045  1.000 67.65418  ?  48  ASN A C   1 
ATOM   353  O O   . ASN A 1 49 ? 41.09433 -0.11194  1.67782  1.000 68.28512  ?  48  ASN A O   1 
ATOM   354  C CB  . ASN A 1 49 ? 44.33303 0.51766   1.99646  1.000 74.28972  ?  48  ASN A CB  1 
ATOM   355  C CG  . ASN A 1 49 ? 45.34278 1.36792   1.23233  1.000 74.74441  ?  48  ASN A CG  1 
ATOM   356  O OD1 . ASN A 1 49 ? 44.97206 2.17999   0.38425  1.000 80.81871  ?  48  ASN A OD1 1 
ATOM   357  N ND2 . ASN A 1 49 ? 46.62570 1.17983   1.53115  1.000 69.64247  ?  48  ASN A ND2 1 
ATOM   358  N N   . THR A 1 50 ? 41.84169 -0.22502  3.80380  1.000 64.79230  ?  49  THR A N   1 
ATOM   359  C CA  . THR A 1 50 ? 40.88222 -1.26484  4.16944  1.000 59.15798  ?  49  THR A CA  1 
ATOM   360  C C   . THR A 1 50 ? 39.44637 -0.73990  4.12547  1.000 62.35561  ?  49  THR A C   1 
ATOM   361  O O   . THR A 1 50 ? 38.55539 -1.39794  3.57499  1.000 65.33413  ?  49  THR A O   1 
ATOM   362  C CB  . THR A 1 50 ? 41.20809 -1.83976  5.55707  1.000 51.96015  ?  49  THR A CB  1 
ATOM   363  O OG1 . THR A 1 50 ? 42.58193 -2.24021  5.61991  1.000 45.72116  ?  49  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 50 ? 40.35709 -3.06433  5.83760  1.000 54.05446  ?  49  THR A CG2 1 
ATOM   365  N N   . PHE A 1 51 ? 39.20120 0.45000   4.68431  1.000 54.66625  ?  50  PHE A N   1 
ATOM   366  C CA  . PHE A 1 51 ? 37.84008 0.94522   4.88168  1.000 54.85690  ?  50  PHE A CA  1 
ATOM   367  C C   . PHE A 1 51 ? 37.51710 2.21335   4.10274  1.000 56.83181  ?  50  PHE A C   1 
ATOM   368  O O   . PHE A 1 51 ? 36.42543 2.76339   4.28593  1.000 62.06069  ?  50  PHE A O   1 
ATOM   369  C CB  . PHE A 1 51 ? 37.57082 1.22032   6.36333  1.000 46.27664  ?  50  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 51 ? 37.85148 0.06000   7.26912  1.000 61.07464  ?  50  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 51 ? 39.09611 -0.07447  7.88339  1.000 71.23644  ?  50  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 51 ? 36.86759 -0.87814  7.53828  1.000 39.97682  ?  50  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 51 ? 39.36873 -1.13855  8.73935  1.000 55.03923  ?  50  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 51 ? 37.12787 -1.94673  8.39311  1.000 47.14419  ?  50  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 51 ? 38.38696 -2.07288  8.99811  1.000 49.78055  ?  50  PHE A CZ  1 
ATOM   376  N N   . GLY A 1 52 ? 38.42399 2.70753   3.26454  1.000 58.02811  ?  51  GLY A N   1 
ATOM   377  C CA  . GLY A 1 52 ? 38.20688 3.99489   2.62206  1.000 54.39254  ?  51  GLY A CA  1 
ATOM   378  C C   . GLY A 1 52 ? 38.63601 5.15412   3.50739  1.000 63.06940  ?  51  GLY A C   1 
ATOM   379  O O   . GLY A 1 52 ? 39.17890 4.97508   4.60128  1.000 68.14056  ?  51  GLY A O   1 
ATOM   380  N N   . GLU A 1 53 ? 38.36471 6.37164   3.02399  1.000 62.23359  ?  52  GLU A N   1 
ATOM   381  C CA  . GLU A 1 53 ? 38.86916 7.56322   3.70383  1.000 76.65361  ?  52  GLU A CA  1 
ATOM   382  C C   . GLU A 1 53 ? 38.08029 7.88706   4.97136  1.000 69.97500  ?  52  GLU A C   1 
ATOM   383  O O   . GLU A 1 53 ? 38.66498 8.33420   5.96765  1.000 69.13925  ?  52  GLU A O   1 
ATOM   384  C CB  . GLU A 1 53 ? 38.86686 8.76316   2.74965  1.000 71.04750  ?  52  GLU A CB  1 
ATOM   385  C CG  . GLU A 1 53 ? 39.63749 9.96931   3.28428  1.000 89.76564  ?  52  GLU A CG  1 
ATOM   386  C CD  . GLU A 1 53 ? 40.31945 10.77956  2.18838  1.000 103.30196 ?  52  GLU A CD  1 
ATOM   387  O OE1 . GLU A 1 53 ? 40.11735 10.46165  0.99692  1.000 106.32088 ?  52  GLU A OE1 1 
ATOM   388  O OE2 . GLU A 1 53 ? 41.06390 11.73143  2.51953  1.000 99.66304  ?  52  GLU A OE2 1 
ATOM   389  N N   . GLU A 1 54 ? 36.76022 7.69315   4.95359  1.000 70.08882  ?  53  GLU A N   1 
ATOM   390  C CA  . GLU A 1 54 ? 35.93190 7.85497   6.14227  1.000 63.18531  ?  53  GLU A CA  1 
ATOM   391  C C   . GLU A 1 54 ? 34.97290 6.68362   6.26854  1.000 62.74856  ?  53  GLU A C   1 
ATOM   392  O O   . GLU A 1 54 ? 34.49414 6.13608   5.27116  1.000 50.41598  ?  53  GLU A O   1 
ATOM   393  C CB  . GLU A 1 54 ? 35.14909 9.15542   6.12969  1.000 51.29479  ?  53  GLU A CB  1 
ATOM   394  C CG  . GLU A 1 54 ? 35.97959 10.32832  6.60387  1.000 70.63633  ?  53  GLU A CG  1 
ATOM   395  C CD  . GLU A 1 54 ? 35.15871 11.57699  6.79508  1.000 82.00722  ?  53  GLU A CD  1 
ATOM   396  O OE1 . GLU A 1 54 ? 33.92410 11.50159  6.60750  1.000 80.29689  ?  53  GLU A OE1 1 
ATOM   397  O OE2 . GLU A 1 54 ? 35.74956 12.62786  7.13300  1.000 82.95735  ?  53  GLU A OE2 1 
ATOM   398  N N   . VAL A 1 55 ? 34.69263 6.31214   7.51449  1.000 54.94247  ?  54  VAL A N   1 
ATOM   399  C CA  . VAL A 1 55 ? 34.03962 5.04864   7.83327  1.000 63.80595  ?  54  VAL A CA  1 
ATOM   400  C C   . VAL A 1 55 ? 32.71037 5.32757   8.51656  1.000 35.97235  ?  54  VAL A C   1 
ATOM   401  O O   . VAL A 1 55 ? 32.66808 5.99753   9.55733  1.000 46.04974  ?  54  VAL A O   1 
ATOM   402  C CB  . VAL A 1 55 ? 34.92560 4.16818   8.72356  1.000 52.58178  ?  54  VAL A CB  1 
ATOM   403  C CG1 . VAL A 1 55 ? 34.63343 2.70464   8.44913  1.000 51.75707  ?  54  VAL A CG1 1 
ATOM   404  C CG2 . VAL A 1 55 ? 36.39332 4.49712   8.50501  1.000 59.39494  ?  54  VAL A CG2 1 
ATOM   405  N N   . LYS A 1 56 ? 31.63570 4.78862   7.95008  1.000 33.84475  ?  55  LYS A N   1 
ATOM   406  C CA  . LYS A 1 56 ? 30.32159 4.83409   8.57550  1.000 35.11979  ?  55  LYS A CA  1 
ATOM   407  C C   . LYS A 1 56 ? 30.14375 3.62158   9.48500  1.000 34.86726  ?  55  LYS A C   1 
ATOM   408  O O   . LYS A 1 56 ? 30.45684 2.49274   9.08468  1.000 31.09483  ?  55  LYS A O   1 
ATOM   409  C CB  . LYS A 1 56 ? 29.23969 4.85181   7.50466  1.000 34.03571  ?  55  LYS A CB  1 
ATOM   410  C CG  . LYS A 1 56 ? 27.92856 5.45490   7.94557  1.000 54.33105  ?  55  LYS A CG  1 
ATOM   411  C CD  . LYS A 1 56 ? 27.01342 5.69583   6.74926  1.000 57.38193  ?  55  LYS A CD  1 
ATOM   412  C CE  . LYS A 1 56 ? 26.52847 4.38346   6.14967  1.000 53.56733  ?  55  LYS A CE  1 
ATOM   413  N NZ  . LYS A 1 56 ? 25.55717 4.59224   5.03698  1.000 68.87672  ?  55  LYS A NZ  1 
ATOM   414  N N   . TYR A 1 57 ? 29.64272 3.84165   10.70187 1.000 30.89204  ?  56  TYR A N   1 
ATOM   415  C CA  . TYR A 1 57 ? 29.34207 2.72916   11.59672 1.000 29.91614  ?  56  TYR A CA  1 
ATOM   416  C C   . TYR A 1 57 ? 27.87504 2.76268   12.01038 1.000 29.53443  ?  56  TYR A C   1 
ATOM   417  O O   . TYR A 1 57 ? 27.31270 3.83183   12.25292 1.000 30.00276  ?  56  TYR A O   1 
ATOM   418  C CB  . TYR A 1 57 ? 30.25651 2.72134   12.81939 1.000 33.54038  ?  56  TYR A CB  1 
ATOM   419  C CG  . TYR A 1 57 ? 30.15440 3.90972   13.71718 1.000 34.29820  ?  56  TYR A CG  1 
ATOM   420  C CD1 . TYR A 1 57 ? 29.20759 3.94811   14.73244 1.000 31.64357  ?  56  TYR A CD1 1 
ATOM   421  C CD2 . TYR A 1 57 ? 31.03099 4.99209   13.57825 1.000 32.57515  ?  56  TYR A CD2 1 
ATOM   422  C CE1 . TYR A 1 57 ? 29.11272 5.05759   15.58212 1.000 48.60263  ?  56  TYR A CE1 1 
ATOM   423  C CE2 . TYR A 1 57 ? 30.94072 6.10823   14.41472 1.000 44.14127  ?  56  TYR A CE2 1 
ATOM   424  C CZ  . TYR A 1 57 ? 29.97635 6.13143   15.41751 1.000 46.94324  ?  56  TYR A CZ  1 
ATOM   425  O OH  . TYR A 1 57 ? 29.86959 7.22365   16.25776 1.000 46.73821  ?  56  TYR A OH  1 
ATOM   426  N N   A ARG A 1 58 ? 27.25704 1.57893   12.06207 0.462 22.04067  ?  57  ARG A N   1 
ATOM   427  N N   B ARG A 1 58 ? 27.26294 1.58299   12.07688 0.538 22.03103  ?  57  ARG A N   1 
ATOM   428  C CA  A ARG A 1 58 ? 25.83210 1.45599   12.34033 0.462 21.12462  ?  57  ARG A CA  1 
ATOM   429  C CA  B ARG A 1 58 ? 25.84132 1.47906   12.35076 0.538 21.12268  ?  57  ARG A CA  1 
ATOM   430  C C   A ARG A 1 58 ? 25.53491 1.72045   13.81635 0.462 20.89184  ?  57  ARG A C   1 
ATOM   431  C C   B ARG A 1 58 ? 25.54000 1.74149   13.82225 0.538 20.89209  ?  57  ARG A C   1 
ATOM   432  O O   A ARG A 1 58 ? 26.41257 1.57422   14.66956 0.462 22.62909  ?  57  ARG A O   1 
ATOM   433  O O   B ARG A 1 58 ? 26.41668 1.60745   14.67822 0.538 22.66555  ?  57  ARG A O   1 
ATOM   434  C CB  A ARG A 1 58 ? 25.34233 0.05739   11.96446 0.462 21.48767  ?  57  ARG A CB  1 
ATOM   435  C CB  B ARG A 1 58 ? 25.34028 0.09319   11.97485 0.538 21.48808  ?  57  ARG A CB  1 
ATOM   436  C CG  A ARG A 1 58 ? 25.36466 -0.26428  10.48061 0.462 26.10722  ?  57  ARG A CG  1 
ATOM   437  C CG  B ARG A 1 58 ? 25.39040 -0.20265  10.51216 0.538 26.07837  ?  57  ARG A CG  1 
ATOM   438  C CD  A ARG A 1 58 ? 24.86047 -1.68313  10.24009 0.462 30.27265  ?  57  ARG A CD  1 
ATOM   439  C CD  B ARG A 1 58 ? 24.49966 -1.37170  10.24848 0.538 33.05022  ?  57  ARG A CD  1 
ATOM   440  N NE  A ARG A 1 58 ? 24.95385 -2.06945  8.83783  0.462 29.17266  ?  57  ARG A NE  1 
ATOM   441  N NE  B ARG A 1 58 ? 24.75708 -1.97373  8.95161  0.538 29.33395  ?  57  ARG A NE  1 
ATOM   442  C CZ  A ARG A 1 58 ? 24.65698 -3.27094  8.36280  0.462 29.85225  ?  57  ARG A CZ  1 
ATOM   443  C CZ  B ARG A 1 58 ? 24.02864 -2.95311  8.44775  0.538 31.93077  ?  57  ARG A CZ  1 
ATOM   444  N NH1 A ARG A 1 58 ? 24.22985 -4.24785  9.15317  0.462 27.14834  ?  57  ARG A NH1 1 
ATOM   445  N NH1 B ARG A 1 58 ? 22.98990 -3.44439  9.10534  0.538 33.76119  ?  57  ARG A NH1 1 
ATOM   446  N NH2 A ARG A 1 58 ? 24.79427 -3.50146  7.06046  0.462 35.54848  ?  57  ARG A NH2 1 
ATOM   447  N NH2 B ARG A 1 58 ? 24.34819 -3.45099  7.25618  0.538 37.82134  ?  57  ARG A NH2 1 
ATOM   448  N N   . PRO A 1 59 ? 24.29917 2.10120   14.14709 1.000 21.95978  ?  58  PRO A N   1 
ATOM   449  C CA  . PRO A 1 59 ? 23.90676 2.16371   15.55572 1.000 21.08003  ?  58  PRO A CA  1 
ATOM   450  C C   . PRO A 1 59 ? 23.94565 0.76237   16.15377 1.000 21.85827  ?  58  PRO A C   1 
ATOM   451  O O   . PRO A 1 59 ? 23.95850 -0.24839  15.44581 1.000 22.32100  ?  58  PRO A O   1 
ATOM   452  C CB  . PRO A 1 59 ? 22.48303 2.72170   15.51492 1.000 22.00299  ?  58  PRO A CB  1 
ATOM   453  C CG  . PRO A 1 59 ? 21.96699 2.32851   14.18485 1.000 25.82051  ?  58  PRO A CG  1 
ATOM   454  C CD  . PRO A 1 59 ? 23.15658 2.37700   13.25169 1.000 25.47404  ?  58  PRO A CD  1 
ATOM   455  N N   . TYR A 1 60 ? 24.00302 0.70387   17.47899 1.000 22.65820  ?  59  TYR A N   1 
ATOM   456  C CA  . TYR A 1 60 ? 24.10554 -0.58179  18.16291 1.000 21.80848  ?  59  TYR A CA  1 
ATOM   457  C C   . TYR A 1 60 ? 23.45927 -0.43862  19.53778 1.000 20.46274  ?  59  TYR A C   1 
ATOM   458  O O   . TYR A 1 60 ? 22.95630 0.62808   19.89314 1.000 21.58397  ?  59  TYR A O   1 
ATOM   459  C CB  . TYR A 1 60 ? 25.57509 -1.04970  18.22998 1.000 19.86510  ?  59  TYR A CB  1 
ATOM   460  C CG  . TYR A 1 60 ? 26.47933 -0.11997  18.99657 1.000 22.46340  ?  59  TYR A CG  1 
ATOM   461  C CD1 . TYR A 1 60 ? 27.04029 1.01128   18.38950 1.000 27.55137  ?  59  TYR A CD1 1 
ATOM   462  C CD2 . TYR A 1 60 ? 26.77716 -0.35998  20.33322 1.000 20.89896  ?  59  TYR A CD2 1 
ATOM   463  C CE1 . TYR A 1 60 ? 27.87887 1.87244   19.10485 1.000 25.39971  ?  59  TYR A CE1 1 
ATOM   464  C CE2 . TYR A 1 60 ? 27.61183 0.48418   21.04567 1.000 26.45372  ?  59  TYR A CE2 1 
ATOM   465  C CZ  . TYR A 1 60 ? 28.15534 1.59801   20.43144 1.000 28.67287  ?  59  TYR A CZ  1 
ATOM   466  O OH  . TYR A 1 60 ? 28.97371 2.42424   21.16099 1.000 28.28875  ?  59  TYR A OH  1 
ATOM   467  N N   . LEU A 1 61 ? 23.42879 -1.53806  20.28863 1.000 21.87130  ?  60  LEU A N   1 
ATOM   468  C CA  . LEU A 1 61 ? 22.93239 -1.55251  21.65757 1.000 20.23523  ?  60  LEU A CA  1 
ATOM   469  C C   . LEU A 1 61 ? 24.06287 -1.91174  22.61875 1.000 20.14093  ?  60  LEU A C   1 
ATOM   470  O O   . LEU A 1 61 ? 24.96820 -2.67650  22.27964 1.000 19.52949  ?  60  LEU A O   1 
ATOM   471  C CB  . LEU A 1 61 ? 21.79882 -2.55550  21.82014 1.000 20.49474  ?  60  LEU A CB  1 
ATOM   472  C CG  . LEU A 1 61 ? 20.57439 -2.31953  20.94450 1.000 20.97320  ?  60  LEU A CG  1 
ATOM   473  C CD1 . LEU A 1 61 ? 19.52502 -3.42088  21.15113 1.000 21.23513  ?  60  LEU A CD1 1 
ATOM   474  C CD2 . LEU A 1 61 ? 19.99013 -0.95972  21.25235 1.000 21.31083  ?  60  LEU A CD2 1 
ATOM   475  N N   . ALA A 1 62 ? 23.99589 -1.36453  23.83065 1.000 21.45022  ?  61  ALA A N   1 
ATOM   476  C CA  . ALA A 1 62 ? 25.01067 -1.58763  24.85629 1.000 23.21544  ?  61  ALA A CA  1 
ATOM   477  C C   . ALA A 1 62 ? 24.34430 -1.98948  26.16566 1.000 24.90314  ?  61  ALA A C   1 
ATOM   478  O O   . ALA A 1 62 ? 23.18128 -1.66517  26.41223 1.000 20.21688  ?  61  ALA A O   1 
ATOM   479  C CB  . ALA A 1 62 ? 25.87557 -0.32748  25.08730 1.000 19.52194  ?  61  ALA A CB  1 
ATOM   480  N N   . LEU A 1 63 ? 25.09700 -2.71017  26.99599 1.000 20.49255  ?  62  LEU A N   1 
ATOM   481  C CA  . LEU A 1 63 ? 24.64378 -3.17824  28.29892 1.000 19.86631  ?  62  LEU A CA  1 
ATOM   482  C C   . LEU A 1 63 ? 25.63803 -2.73541  29.36534 1.000 19.77619  ?  62  LEU A C   1 
ATOM   483  O O   . LEU A 1 63 ? 26.84353 -2.96999  29.22946 1.000 19.45963  ?  62  LEU A O   1 
ATOM   484  C CB  . LEU A 1 63 ? 24.50803 -4.71040  28.32112 1.000 19.82174  ?  62  LEU A CB  1 
ATOM   485  C CG  . LEU A 1 63 ? 23.85182 -5.28680  29.57737 1.000 20.14148  ?  62  LEU A CG  1 
ATOM   486  C CD1 . LEU A 1 63 ? 22.34758 -5.23617  29.45868 1.000 20.55681  ?  62  LEU A CD1 1 
ATOM   487  C CD2 . LEU A 1 63 ? 24.33047 -6.68686  29.84810 1.000 22.29936  ?  62  LEU A CD2 1 
ATOM   488  N N   . LYS A 1 64 ? 25.13245 -2.07581  30.41008 1.000 20.68216  ?  63  LYS A N   1 
ATOM   489  C CA  . LYS A 1 64 ? 25.87799 -1.83301  31.64502 1.000 20.15288  ?  63  LYS A CA  1 
ATOM   490  C C   . LYS A 1 64 ? 25.82402 -3.11436  32.46733 1.000 21.09056  ?  63  LYS A C   1 
ATOM   491  O O   . LYS A 1 64 ? 24.75653 -3.48789  32.96024 1.000 25.12419  ?  63  LYS A O   1 
ATOM   492  C CB  . LYS A 1 64 ? 25.26216 -0.64423  32.39311 1.000 23.28647  ?  63  LYS A CB  1 
ATOM   493  C CG  . LYS A 1 64 ? 26.20704 0.10905   33.31196 1.000 28.76931  ?  63  LYS A CG  1 
ATOM   494  C CD  . LYS A 1 64 ? 26.49509 -0.64809  34.60495 1.000 29.26438  ?  63  LYS A CD  1 
ATOM   495  C CE  . LYS A 1 64 ? 25.23623 -0.88064  35.40785 1.000 33.40757  ?  63  LYS A CE  1 
ATOM   496  N NZ  . LYS A 1 64 ? 25.47617 -1.90279  36.47052 1.000 31.48082  ?  63  LYS A NZ  1 
ATOM   497  N N   . THR A 1 65 ? 26.96320 -3.80790  32.59890 1.000 19.99570  ?  64  THR A N   1 
ATOM   498  C CA  . THR A 1 65 ? 27.01344 -5.14023  33.19350 1.000 20.07732  ?  64  THR A CA  1 
ATOM   499  C C   . THR A 1 65 ? 27.11909 -5.05415  34.71337 1.000 21.11968  ?  64  THR A C   1 
ATOM   500  O O   . THR A 1 65 ? 27.24217 -3.97402  35.28347 1.000 24.90412  ?  64  THR A O   1 
ATOM   501  C CB  . THR A 1 65 ? 28.19761 -5.94272  32.65029 1.000 19.88363  ?  64  THR A CB  1 
ATOM   502  O OG1 . THR A 1 65 ? 29.42093 -5.41704  33.19351 1.000 24.26940  ?  64  THR A OG1 1 
ATOM   503  C CG2 . THR A 1 65 ? 28.26242 -5.85918  31.14796 1.000 20.62224  ?  64  THR A CG2 1 
ATOM   504  N N   . VAL A 1 66 ? 27.08037 -6.21710  35.38260 1.000 20.61664  ?  65  VAL A N   1 
ATOM   505  C CA  . VAL A 1 66 ? 27.26000 -6.25196  36.83876 1.000 27.49341  ?  65  VAL A CA  1 
ATOM   506  C C   . VAL A 1 66 ? 28.66332 -5.85227  37.24931 1.000 30.18350  ?  65  VAL A C   1 
ATOM   507  O O   . VAL A 1 66 ? 28.87851 -5.49729  38.41298 1.000 29.77036  ?  65  VAL A O   1 
ATOM   508  C CB  . VAL A 1 66 ? 26.92418 -7.63580  37.44205 1.000 21.29171  ?  65  VAL A CB  1 
ATOM   509  C CG1 . VAL A 1 66 ? 25.53619 -8.05400  37.04348 1.000 29.45574  ?  65  VAL A CG1 1 
ATOM   510  C CG2 . VAL A 1 66 ? 27.94291 -8.68848  37.02890 1.000 30.11189  ?  65  VAL A CG2 1 
ATOM   511  N N   . ASP A 1 67 ? 29.63094 -5.89675  36.32881 1.000 20.44333  ?  66  ASP A N   1 
ATOM   512  C CA  . ASP A 1 67 ? 30.98792 -5.44711  36.60602 1.000 27.29858  ?  66  ASP A CA  1 
ATOM   513  C C   . ASP A 1 67 ? 31.14509 -3.94903  36.42235 1.000 29.39524  ?  66  ASP A C   1 
ATOM   514  O O   . ASP A 1 67 ? 32.25281 -3.43857  36.59912 1.000 28.94682  ?  66  ASP A O   1 
ATOM   515  C CB  . ASP A 1 67 ? 31.98643 -6.18952  35.70664 1.000 23.29517  ?  66  ASP A CB  1 
ATOM   516  C CG  . ASP A 1 67 ? 31.93636 -7.68722  35.89996 1.000 36.52572  ?  66  ASP A CG  1 
ATOM   517  O OD1 . ASP A 1 67 ? 31.85785 -8.13839  37.06589 1.000 38.16199  ?  66  ASP A OD1 1 
ATOM   518  O OD2 . ASP A 1 67 ? 31.94866 -8.41452  34.88174 1.000 32.07630  ?  66  ASP A OD2 1 
ATOM   519  N N   . ASN A 1 68 ? 30.07138 -3.24786  36.06175 1.000 24.60867  ?  67  ASN A N   1 
ATOM   520  C CA  . ASN A 1 68 ? 30.06345 -1.80628  35.84803 1.000 25.01737  ?  67  ASN A CA  1 
ATOM   521  C C   . ASN A 1 68 ? 30.88093 -1.38001  34.63056 1.000 24.73659  ?  67  ASN A C   1 
ATOM   522  O O   . ASN A 1 68 ? 31.31984 -0.23525  34.55046 1.000 36.44448  ?  67  ASN A O   1 
ATOM   523  C CB  . ASN A 1 68 ? 30.54642 -1.04671  37.09330 1.000 29.41313  ?  67  ASN A CB  1 
ATOM   524  C CG  . ASN A 1 68 ? 30.11211 0.39414   37.07888 1.000 30.20740  ?  67  ASN A CG  1 
ATOM   525  O OD1 . ASN A 1 68 ? 29.01132 0.70659   36.63130 1.000 51.14731  ?  67  ASN A OD1 1 
ATOM   526  N ND2 . ASN A 1 68 ? 30.97457 1.29115   37.55914 1.000 44.73957  ?  67  ASN A ND2 1 
ATOM   527  N N   . ASP A 1 69 ? 31.09731 -2.26226  33.66752 1.000 22.27714  ?  68  ASP A N   1 
ATOM   528  C CA  . ASP A 1 69 ? 31.65928 -1.85616  32.38856 1.000 27.49857  ?  68  ASP A CA  1 
ATOM   529  C C   . ASP A 1 69 ? 30.60441 -2.05544  31.30532 1.000 25.36716  ?  68  ASP A C   1 
ATOM   530  O O   . ASP A 1 69 ? 29.53261 -2.61194  31.55222 1.000 25.90148  ?  68  ASP A O   1 
ATOM   531  C CB  . ASP A 1 69 ? 32.96609 -2.61540  32.07851 1.000 23.02950  ?  68  ASP A CB  1 
ATOM   532  C CG  . ASP A 1 69 ? 32.84604 -4.11658  32.26461 1.000 35.49634  ?  68  ASP A CG  1 
ATOM   533  O OD1 . ASP A 1 69 ? 31.72384 -4.65281  32.20267 1.000 27.62521  ?  68  ASP A OD1 1 
ATOM   534  O OD2 . ASP A 1 69 ? 33.89027 -4.78164  32.46215 1.000 28.75359  ?  68  ASP A OD2 1 
ATOM   535  N N   . ILE A 1 70 ? 30.89049 -1.56150  30.10186 1.000 20.19753  ?  69  ILE A N   1 
ATOM   536  C CA  . ILE A 1 70 ? 29.91594 -1.52736  29.01550 1.000 18.95788  ?  69  ILE A CA  1 
ATOM   537  C C   . ILE A 1 70 ? 30.25250 -2.60243  27.99771 1.000 21.68238  ?  69  ILE A C   1 
ATOM   538  O O   . ILE A 1 70 ? 31.34926 -2.60759  27.43163 1.000 22.90032  ?  69  ILE A O   1 
ATOM   539  C CB  . ILE A 1 70 ? 29.87458 -0.15646  28.31633 1.000 21.16654  ?  69  ILE A CB  1 
ATOM   540  C CG1 . ILE A 1 70 ? 29.62745 0.99829   29.29867 1.000 23.76184  ?  69  ILE A CG1 1 
ATOM   541  C CG2 . ILE A 1 70 ? 28.83812 -0.19905  27.19009 1.000 22.50890  ?  69  ILE A CG2 1 
ATOM   542  C CD1 . ILE A 1 70 ? 28.49594 0.80080   30.24679 1.000 26.57643  ?  69  ILE A CD1 1 
ATOM   543  N N   . ALA A 1 71 ? 29.28655 -3.46166  27.70568 1.000 18.75378  ?  70  ALA A N   1 
ATOM   544  C CA  . ALA A 1 71 ? 29.42029 -4.48808  26.68649 1.000 18.58727  ?  70  ALA A CA  1 
ATOM   545  C C   . ALA A 1 71 ? 28.52815 -4.15551  25.50473 1.000 18.67829  ?  70  ALA A C   1 
ATOM   546  O O   . ALA A 1 71 ? 27.45885 -3.58812  25.67875 1.000 20.49540  ?  70  ALA A O   1 
ATOM   547  C CB  . ALA A 1 71 ? 29.02224 -5.85556  27.23851 1.000 22.62693  ?  70  ALA A CB  1 
ATOM   548  N N   . THR A 1 72 ? 28.94652 -4.53392  24.29796 1.000 19.93684  ?  71  THR A N   1 
ATOM   549  C CA  . THR A 1 72 ? 27.99309 -4.53957  23.19935 1.000 18.75070  ?  71  THR A CA  1 
ATOM   550  C C   . THR A 1 72 ? 26.99521 -5.65708  23.44740 1.000 21.20856  ?  71  THR A C   1 
ATOM   551  O O   . THR A 1 72 ? 27.33992 -6.72732  23.95002 1.000 22.75703  ?  71  THR A O   1 
ATOM   552  C CB  . THR A 1 72 ? 28.68132 -4.73456  21.84455 1.000 19.65476  ?  71  THR A CB  1 
ATOM   553  O OG1 . THR A 1 72 ? 29.32450 -6.01361  21.80713 1.000 30.99163  ?  71  THR A OG1 1 
ATOM   554  C CG2 . THR A 1 72 ? 29.69338 -3.64566  21.59970 1.000 20.62634  ?  71  THR A CG2 1 
ATOM   555  N N   . TRP A 1 73 ? 25.74561 -5.41443  23.10152 1.000 20.45991  ?  72  TRP A N   1 
ATOM   556  C CA  . TRP A 1 73 ? 24.70446 -6.29064  23.59730 1.000 23.57606  ?  72  TRP A CA  1 
ATOM   557  C C   . TRP A 1 73 ? 23.72470 -6.61739  22.49268 1.000 23.27418  ?  72  TRP A C   1 
ATOM   558  O O   . TRP A 1 73 ? 23.32655 -5.73738  21.72805 1.000 19.79819  ?  72  TRP A O   1 
ATOM   559  C CB  . TRP A 1 73 ? 23.97532 -5.64297  24.77453 1.000 19.63743  ?  72  TRP A CB  1 
ATOM   560  C CG  . TRP A 1 73 ? 22.81353 -6.45204  25.30872 1.000 19.95735  ?  72  TRP A CG  1 
ATOM   561  C CD1 . TRP A 1 73 ? 22.87984 -7.57987  26.07337 1.000 19.94976  ?  72  TRP A CD1 1 
ATOM   562  C CD2 . TRP A 1 73 ? 21.42690 -6.15742  25.15022 1.000 20.38646  ?  72  TRP A CD2 1 
ATOM   563  N NE1 . TRP A 1 73 ? 21.61963 -8.01564  26.39063 1.000 20.33876  ?  72  TRP A NE1 1 
ATOM   564  C CE2 . TRP A 1 73 ? 20.70514 -7.16561  25.82701 1.000 20.61592  ?  72  TRP A CE2 1 
ATOM   565  C CE3 . TRP A 1 73 ? 20.72348 -5.15827  24.47660 1.000 20.64524  ?  72  TRP A CE3 1 
ATOM   566  C CZ2 . TRP A 1 73 ? 19.31937 -7.19286  25.86034 1.000 21.09079  ?  72  TRP A CZ2 1 
ATOM   567  C CZ3 . TRP A 1 73 ? 19.35652 -5.18078  24.51349 1.000 21.12187  ?  72  TRP A CZ3 1 
ATOM   568  C CH2 . TRP A 1 73 ? 18.66046 -6.19158  25.20314 1.000 21.89032  ?  72  TRP A CH2 1 
ATOM   569  N N   . THR A 1 74 ? 23.34960 -7.89205  22.44158 1.000 25.19172  ?  73  THR A N   1 
ATOM   570  C CA  . THR A 1 74 ? 22.29270 -8.45287  21.62193 1.000 36.26235  ?  73  THR A CA  1 
ATOM   571  C C   . THR A 1 74 ? 21.34157 -9.18403  22.56277 1.000 20.60533  ?  73  THR A C   1 
ATOM   572  O O   . THR A 1 74 ? 21.79842 -10.03854 23.34755 1.000 27.94400  ?  73  THR A O   1 
ATOM   573  C CB  . THR A 1 74 ? 22.89242 -9.44685  20.60965 1.000 33.55460  ?  73  THR A CB  1 
ATOM   574  O OG1 . THR A 1 74 ? 24.07782 -8.88488  20.02377 1.000 46.76164  ?  73  THR A OG1 1 
ATOM   575  C CG2 . THR A 1 74 ? 21.90660 -9.76850  19.53216 1.000 30.16839  ?  73  THR A CG2 1 
ATOM   576  N N   . PRO A 1 75 ? 20.04207 -8.90750  22.52870 1.000 30.49124  ?  74  PRO A N   1 
ATOM   577  C CA  . PRO A 1 75 ? 19.11971 -9.67736  23.37381 1.000 27.57104  ?  74  PRO A CA  1 
ATOM   578  C C   . PRO A 1 75 ? 19.22086 -11.16516 23.05393 1.000 27.95000  ?  74  PRO A C   1 
ATOM   579  O O   . PRO A 1 75 ? 19.52103 -11.55591 21.92711 1.000 29.85842  ?  74  PRO A O   1 
ATOM   580  C CB  . PRO A 1 75 ? 17.73737 -9.12315  23.00426 1.000 31.55778  ?  74  PRO A CB  1 
ATOM   581  C CG  . PRO A 1 75 ? 18.00362 -7.85402  22.28357 1.000 38.93715  ?  74  PRO A CG  1 
ATOM   582  C CD  . PRO A 1 75 ? 19.34138 -7.94154  21.67017 1.000 24.77716  ?  74  PRO A CD  1 
ATOM   583  N N   . SER A 1 76 ? 19.02536 -11.99966 24.07331 1.000 21.97531  ?  75  SER A N   1 
ATOM   584  C CA  . SER A 1 76 ? 18.89050 -13.42877 23.84400 1.000 23.32177  ?  75  SER A CA  1 
ATOM   585  C C   . SER A 1 76 ? 17.46368 -13.72863 23.40160 1.000 21.58726  ?  75  SER A C   1 
ATOM   586  O O   . SER A 1 76 ? 16.58967 -12.86101 23.42770 1.000 23.07638  ?  75  SER A O   1 
ATOM   587  C CB  . SER A 1 76 ? 19.21250 -14.20899 25.11173 1.000 22.01809  ?  75  SER A CB  1 
ATOM   588  O OG  . SER A 1 76 ? 18.17644 -13.97772 26.06051 1.000 21.46689  ?  75  SER A OG  1 
ATOM   589  N N   . VAL A 1 77 ? 17.21116 -14.97670 23.00150 1.000 23.26817  ?  76  VAL A N   1 
ATOM   590  C CA  . VAL A 1 77 ? 15.84709 -15.32407 22.60738 1.000 22.23749  ?  76  VAL A CA  1 
ATOM   591  C C   . VAL A 1 77 ? 14.91304 -15.23560 23.80489 1.000 22.63363  ?  76  VAL A C   1 
ATOM   592  O O   . VAL A 1 77 ? 13.75937 -14.81509 23.67990 1.000 23.11244  ?  76  VAL A O   1 
ATOM   593  C CB  . VAL A 1 77 ? 15.79440 -16.71535 21.95153 1.000 22.30840  ?  76  VAL A CB  1 
ATOM   594  C CG1 . VAL A 1 77 ? 14.41265 -16.96398 21.43392 1.000 23.64273  ?  76  VAL A CG1 1 
ATOM   595  C CG2 . VAL A 1 77 ? 16.78081 -16.78054 20.82132 1.000 36.25641  ?  76  VAL A CG2 1 
ATOM   596  N N   . SER A 1 78 ? 15.39574 -15.61770 24.98750 1.000 22.49863  ?  77  SER A N   1 
ATOM   597  C CA  . SER A 1 78 ? 14.59323 -15.43435 26.19151 1.000 22.90606  ?  77  SER A CA  1 
ATOM   598  C C   . SER A 1 78 ? 14.30709 -13.96143 26.44380 1.000 23.45855  ?  77  SER A C   1 
ATOM   599  O O   . SER A 1 78 ? 13.18216 -13.60760 26.81843 1.000 23.60494  ?  77  SER A O   1 
ATOM   600  C CB  . SER A 1 78 ? 15.28700 -16.06533 27.39134 1.000 29.69215  ?  77  SER A CB  1 
ATOM   601  O OG  . SER A 1 78 ? 15.38486 -17.47177 27.20319 1.000 36.59462  ?  77  SER A OG  1 
ATOM   602  N N   . ASP A 1 79 ? 15.29839 -13.08264 26.23314 1.000 22.56695  ?  78  ASP A N   1 
ATOM   603  C CA  . ASP A 1 79 ? 15.05674 -11.63794 26.33209 1.000 26.41937  ?  78  ASP A CA  1 
ATOM   604  C C   . ASP A 1 79 ? 13.99592 -11.18596 25.33649 1.000 23.06812  ?  78  ASP A C   1 
ATOM   605  O O   . ASP A 1 79 ? 13.08984 -10.41479 25.67744 1.000 23.51268  ?  78  ASP A O   1 
ATOM   606  C CB  . ASP A 1 79 ? 16.33576 -10.84516 26.06405 1.000 22.13461  ?  78  ASP A CB  1 
ATOM   607  C CG  . ASP A 1 79 ? 17.42225 -11.08248 27.07957 1.000 25.43221  ?  78  ASP A CG  1 
ATOM   608  O OD1 . ASP A 1 79 ? 17.13077 -11.36004 28.26496 1.000 22.03930  ?  78  ASP A OD1 1 
ATOM   609  O OD2 . ASP A 1 79 ? 18.59396 -10.94064 26.67946 1.000 25.04675  ?  78  ASP A OD2 1 
ATOM   610  N N   . ILE A 1 80 ? 14.12816 -11.61975 24.08221 1.000 23.05116  ?  79  ILE A N   1 
ATOM   611  C CA  . ILE A 1 80 ? 13.17788 -11.23963 23.03685 1.000 23.37276  ?  79  ILE A CA  1 
ATOM   612  C C   . ILE A 1 80 ? 11.75427 -11.64461 23.40786 1.000 31.80137  ?  79  ILE A C   1 
ATOM   613  O O   . ILE A 1 80 ? 10.79952 -10.89898 23.16193 1.000 27.15703  ?  79  ILE A O   1 
ATOM   614  C CB  . ILE A 1 80 ? 13.59936 -11.86950 21.69532 1.000 23.18613  ?  79  ILE A CB  1 
ATOM   615  C CG1 . ILE A 1 80 ? 14.96864 -11.35549 21.25511 1.000 25.18871  ?  79  ILE A CG1 1 
ATOM   616  C CG2 . ILE A 1 80 ? 12.56251 -11.61754 20.62636 1.000 23.71426  ?  79  ILE A CG2 1 
ATOM   617  C CD1 . ILE A 1 80 ? 14.97038 -9.94620  20.88405 1.000 23.69004  ?  79  ILE A CD1 1 
ATOM   618  N N   . LEU A 1 81 ? 11.57753 -12.84275 23.96386 1.000 24.11426  ?  80  LEU A N   1 
ATOM   619  C CA  . LEU A 1 81 ? 10.24817 -13.38429 24.18306 1.000 24.77410  ?  80  LEU A CA  1 
ATOM   620  C C   . LEU A 1 81 ? 9.65117  -12.98512 25.52165 1.000 27.08841  ?  80  LEU A C   1 
ATOM   621  O O   . LEU A 1 81 ? 8.45758  -13.22545 25.74491 1.000 30.55842  ?  80  LEU A O   1 
ATOM   622  C CB  . LEU A 1 81 ? 10.29011 -14.91107 24.06825 1.000 24.75236  ?  80  LEU A CB  1 
ATOM   623  C CG  . LEU A 1 81 ? 10.56716 -15.42546 22.65889 1.000 24.60087  ?  80  LEU A CG  1 
ATOM   624  C CD1 . LEU A 1 81 ? 10.55574 -16.96307 22.65405 1.000 24.63906  ?  80  LEU A CD1 1 
ATOM   625  C CD2 . LEU A 1 81 ? 9.49166  -14.89051 21.72778 1.000 25.15501  ?  80  LEU A CD2 1 
ATOM   626  N N   . ALA A 1 82 ? 10.44110 -12.37850 26.40403 1.000 29.48656  ?  81  ALA A N   1 
ATOM   627  C CA  . ALA A 1 82 ? 10.01418 -12.09997 27.77086 1.000 25.14815  ?  81  ALA A CA  1 
ATOM   628  C C   . ALA A 1 82 ? 9.02171  -10.94036 27.83694 1.000 32.11093  ?  81  ALA A C   1 
ATOM   629  O O   . ALA A 1 82 ? 8.94482  -10.08267 26.95302 1.000 32.19556  ?  81  ALA A O   1 
ATOM   630  C CB  . ALA A 1 82 ? 11.21374 -11.76698 28.65158 1.000 28.30298  ?  81  ALA A CB  1 
ATOM   631  N N   . GLU A 1 83 ? 8.25659  -10.91680 28.92071 1.000 26.23649  ?  82  GLU A N   1 
ATOM   632  C CA  . GLU A 1 83 ? 7.30800  -9.83369  29.14182 1.000 26.83079  ?  82  GLU A CA  1 
ATOM   633  C C   . GLU A 1 83 ? 7.50899  -9.21312  30.52013 1.000 41.01549  ?  82  GLU A C   1 
ATOM   634  O O   . GLU A 1 83 ? 6.54668  -8.78507  31.16611 1.000 31.99605  ?  82  GLU A O   1 
ATOM   635  C CB  . GLU A 1 83 ? 5.87394  -10.32788 28.95008 1.000 29.37411  ?  82  GLU A CB  1 
ATOM   636  C CG  . GLU A 1 83 ? 5.70096  -11.14270 27.67139 1.000 33.11408  ?  82  GLU A CG  1 
ATOM   637  C CD  . GLU A 1 83 ? 4.36341  -10.90758 26.99997 1.000 39.36493  ?  82  GLU A CD  1 
ATOM   638  O OE1 . GLU A 1 83 ? 3.56277  -10.12260 27.53815 1.000 53.50471  ?  82  GLU A OE1 1 
ATOM   639  O OE2 . GLU A 1 83 ? 4.12634  -11.49794 25.92509 1.000 36.88297  ?  82  GLU A OE2 1 
ATOM   640  N N   . ASP A 1 84 ? 8.76068  -9.15846  30.97902 1.000 26.92800  ?  83  ASP A N   1 
ATOM   641  C CA  . ASP A 1 84 ? 9.11652  -8.57461  32.26516 1.000 26.40772  ?  83  ASP A CA  1 
ATOM   642  C C   . ASP A 1 84 ? 10.08879 -7.40846  32.09956 1.000 26.18658  ?  83  ASP A C   1 
ATOM   643  O O   . ASP A 1 84 ? 10.90628 -7.15708  32.98198 1.000 27.17526  ?  83  ASP A O   1 
ATOM   644  C CB  . ASP A 1 84 ? 9.70884  -9.63988  33.19002 1.000 32.77700  ?  83  ASP A CB  1 
ATOM   645  C CG  . ASP A 1 84 ? 10.91098 -10.34113 32.57480 1.000 30.10411  ?  83  ASP A CG  1 
ATOM   646  O OD1 . ASP A 1 84 ? 11.22511 -10.05598 31.40048 1.000 25.11174  ?  83  ASP A OD1 1 
ATOM   647  O OD2 . ASP A 1 84 ? 11.55592 -11.17516 33.25298 1.000 29.37863  ?  83  ASP A OD2 1 
ATOM   648  N N   . TRP A 1 85 ? 10.00830 -6.68578  30.97728 1.000 25.79977  ?  84  TRP A N   1 
ATOM   649  C CA  . TRP A 1 85 ? 10.85243 -5.51396  30.75850 1.000 25.40706  ?  84  TRP A CA  1 
ATOM   650  C C   . TRP A 1 85 ? 10.33998 -4.31512  31.54259 1.000 32.19816  ?  84  TRP A C   1 
ATOM   651  O O   . TRP A 1 85 ? 9.12828  -4.13196  31.70004 1.000 33.35834  ?  84  TRP A O   1 
ATOM   652  C CB  . TRP A 1 85 ? 10.90931 -5.15535  29.27322 1.000 25.19060  ?  84  TRP A CB  1 
ATOM   653  C CG  . TRP A 1 85 ? 11.67156 -6.13639  28.44313 1.000 26.47667  ?  84  TRP A CG  1 
ATOM   654  C CD1 . TRP A 1 85 ? 11.16761 -7.20680  27.76028 1.000 24.83505  ?  84  TRP A CD1 1 
ATOM   655  C CD2 . TRP A 1 85 ? 13.08642 -6.14194  28.20615 1.000 23.92126  ?  84  TRP A CD2 1 
ATOM   656  N NE1 . TRP A 1 85 ? 12.17479 -7.86830  27.10665 1.000 24.14835  ?  84  TRP A NE1 1 
ATOM   657  C CE2 . TRP A 1 85 ? 13.36190 -7.23821  27.36015 1.000 23.64214  ?  84  TRP A CE2 1 
ATOM   658  C CE3 . TRP A 1 85 ? 14.14363 -5.32050  28.62208 1.000 23.53509  ?  84  TRP A CE3 1 
ATOM   659  C CZ2 . TRP A 1 85 ? 14.65130 -7.54222  26.93086 1.000 24.85005  ?  84  TRP A CZ2 1 
ATOM   660  C CZ3 . TRP A 1 85 ? 15.42651 -5.61513  28.19300 1.000 22.90065  ?  84  TRP A CZ3 1 
ATOM   661  C CH2 . TRP A 1 85 ? 15.66767 -6.73090  27.36003 1.000 22.64830  ?  84  TRP A CH2 1 
ATOM   662  N N   . ASN A 1 86 ? 11.27014 -3.48706  32.02423 1.000 26.81697  ?  85  ASN A N   1 
ATOM   663  C CA  . ASN A 1 86 ? 10.93108 -2.23750  32.68769 1.000 38.78543  ?  85  ASN A CA  1 
ATOM   664  C C   . ASN A 1 86 ? 11.86589 -1.14525  32.19917 1.000 39.06595  ?  85  ASN A C   1 
ATOM   665  O O   . ASN A 1 86 ? 13.04679 -1.39771  31.95227 1.000 31.45116  ?  85  ASN A O   1 
ATOM   666  C CB  . ASN A 1 86 ? 11.02539 -2.35380  34.22242 1.000 45.55774  ?  85  ASN A CB  1 
ATOM   667  C CG  . ASN A 1 86 ? 10.22002 -3.52536  34.77969 1.000 47.49088  ?  85  ASN A CG  1 
ATOM   668  O OD1 . ASN A 1 86 ? 10.76535 -4.38055  35.47545 1.000 64.55198  ?  85  ASN A OD1 1 
ATOM   669  N ND2 . ASN A 1 86 ? 8.92643  -3.56764  34.47498 1.000 59.26497  ?  85  ASN A ND2 1 
ATOM   670  N N   . ILE A 1 87 ? 11.32097 0.06061   32.03724 1.000 28.04491  ?  86  ILE A N   1 
ATOM   671  C CA  . ILE A 1 87 ? 12.13562 1.24387   31.80044 1.000 28.24166  ?  86  ILE A CA  1 
ATOM   672  C C   . ILE A 1 87 ? 12.85432 1.62648   33.08808 1.000 33.30284  ?  86  ILE A C   1 
ATOM   673  O O   . ILE A 1 87 ? 12.28458 1.56510   34.18446 1.000 34.57833  ?  86  ILE A O   1 
ATOM   674  C CB  . ILE A 1 87 ? 11.25286 2.38971   31.27602 1.000 34.32369  ?  86  ILE A CB  1 
ATOM   675  C CG1 . ILE A 1 87 ? 10.72390 2.02608   29.88658 1.000 34.01901  ?  86  ILE A CG1 1 
ATOM   676  C CG2 . ILE A 1 87 ? 12.00741 3.70612   31.24090 1.000 33.79819  ?  86  ILE A CG2 1 
ATOM   677  C CD1 . ILE A 1 87 ? 9.58684  2.92577   29.40543 1.000 54.05258  ?  86  ILE A CD1 1 
ATOM   678  N N   . VAL A 1 88 ? 14.12027 2.00294   32.95832 1.000 26.46632  ?  87  VAL A N   1 
ATOM   679  C CA  . VAL A 1 88 ? 14.98947 2.33376   34.07980 1.000 38.72254  ?  87  VAL A CA  1 
ATOM   680  C C   . VAL A 1 88 ? 15.21008 3.83851   34.07519 1.000 33.98544  ?  87  VAL A C   1 
ATOM   681  O O   . VAL A 1 88 ? 15.60963 4.40677   33.04942 1.000 33.92592  ?  87  VAL A O   1 
ATOM   682  C CB  . VAL A 1 88 ? 16.34193 1.60061   33.98634 1.000 36.97861  ?  87  VAL A CB  1 
ATOM   683  C CG1 . VAL A 1 88 ? 17.31620 2.16544   34.99483 1.000 39.15078  ?  87  VAL A CG1 1 
ATOM   684  C CG2 . VAL A 1 88 ? 16.18340 0.10748   34.18815 1.000 36.30642  ?  87  VAL A CG2 1 
ATOM   685  N N   . GLU A 1 89 ? 14.95833 4.47806   35.21788 1.000 42.24550  ?  88  GLU A N   1 
ATOM   686  C CA  . GLU A 1 89 ? 15.32948 5.88004   35.43278 1.000 42.04324  ?  88  GLU A CA  1 
ATOM   687  C C   . GLU A 1 89 ? 16.84133 6.00911   35.62715 1.000 50.67557  ?  88  GLU A C   1 
ATOM   688  O O   . GLU A 1 89 ? 17.53513 6.63234   34.82497 1.000 50.68437  ?  88  GLU A O   1 
ATOM   689  C CB  . GLU A 1 89 ? 14.60745 6.45771   36.65056 1.000 46.15733  ?  88  GLU A CB  1 
ATOM   690  C CG  . GLU A 1 89 ? 13.13213 6.78731   36.45394 1.000 56.76049  ?  88  GLU A CG  1 
ATOM   691  C CD  . GLU A 1 89 ? 12.54188 7.50424   37.67525 1.000 68.98676  ?  88  GLU A CD  1 
ATOM   692  O OE1 . GLU A 1 89 ? 13.24486 7.57979   38.70702 1.000 69.16862  ?  88  GLU A OE1 1 
ATOM   693  O OE2 . GLU A 1 89 ? 11.39162 7.99503   37.60956 1.000 58.85932  ?  88  GLU A OE2 1 
ATOM   694  N N   . ASP B 1 3  ? 38.32001 -24.48546 34.78744 1.000 52.06055  ?  2   ASP B N   1 
ATOM   695  C CA  . ASP B 1 3  ? 39.62648 -24.95738 34.33928 1.000 49.93279  ?  2   ASP B CA  1 
ATOM   696  C C   . ASP B 1 3  ? 40.37558 -23.84828 33.60148 1.000 48.94819  ?  2   ASP B C   1 
ATOM   697  O O   . ASP B 1 3  ? 41.50064 -24.06047 33.14430 1.000 49.70352  ?  2   ASP B O   1 
ATOM   698  C CB  . ASP B 1 3  ? 39.47794 -26.18009 33.43610 1.000 36.20466  ?  2   ASP B CB  1 
ATOM   699  C CG  . ASP B 1 3  ? 38.38468 -27.13468 33.90913 1.000 63.94158  ?  2   ASP B CG  1 
ATOM   700  O OD1 . ASP B 1 3  ? 38.19517 -27.25090 35.14447 1.000 79.84201  ?  2   ASP B OD1 1 
ATOM   701  O OD2 . ASP B 1 3  ? 37.71800 -27.76661 33.04433 1.000 36.72865  ?  2   ASP B OD2 1 
ATOM   702  N N   . SER B 1 4  ? 39.73494 -22.67826 33.49606 1.000 42.38968  ?  3   SER B N   1 
ATOM   703  C CA  . SER B 1 4  ? 40.26646 -21.50696 32.79328 1.000 34.31872  ?  3   SER B CA  1 
ATOM   704  C C   . SER B 1 4  ? 40.65975 -21.83600 31.34487 1.000 33.44038  ?  3   SER B C   1 
ATOM   705  O O   . SER B 1 4  ? 41.79937 -21.64536 30.91442 1.000 31.20278  ?  3   SER B O   1 
ATOM   706  C CB  . SER B 1 4  ? 41.44202 -20.90416 33.56219 1.000 42.26982  ?  3   SER B CB  1 
ATOM   707  O OG  . SER B 1 4  ? 42.52451 -21.81355 33.62715 1.000 57.65383  ?  3   SER B OG  1 
ATOM   708  N N   . LEU B 1 5  ? 39.67848 -22.32204 30.59004 1.000 17.61681  ?  4   LEU B N   1 
ATOM   709  C CA  . LEU B 1 5  ? 39.80668 -22.53638 29.15854 1.000 18.17383  ?  4   LEU B CA  1 
ATOM   710  C C   . LEU B 1 5  ? 39.29306 -21.32367 28.39309 1.000 18.34699  ?  4   LEU B C   1 
ATOM   711  O O   . LEU B 1 5  ? 38.41610 -20.58782 28.86390 1.000 16.36110  ?  4   LEU B O   1 
ATOM   712  C CB  . LEU B 1 5  ? 39.02015 -23.77424 28.72286 1.000 15.78739  ?  4   LEU B CB  1 
ATOM   713  C CG  . LEU B 1 5  ? 39.26680 -25.02835 29.57140 1.000 23.09094  ?  4   LEU B CG  1 
ATOM   714  C CD1 . LEU B 1 5  ? 38.31645 -26.12648 29.15977 1.000 20.11382  ?  4   LEU B CD1 1 
ATOM   715  C CD2 . LEU B 1 5  ? 40.69386 -25.49393 29.45212 1.000 24.37199  ?  4   LEU B CD2 1 
ATOM   716  N N   . ASN B 1 6  ? 39.85454 -21.11335 27.20131 1.000 18.33454  ?  5   ASN B N   1 
ATOM   717  C CA  . ASN B 1 6  ? 39.26366 -20.13637 26.30453 1.000 16.27196  ?  5   ASN B CA  1 
ATOM   718  C C   . ASN B 1 6  ? 38.09037 -20.78622 25.56559 1.000 16.59605  ?  5   ASN B C   1 
ATOM   719  O O   . ASN B 1 6  ? 37.77857 -21.97385 25.75395 1.000 13.23116  ?  5   ASN B O   1 
ATOM   720  C CB  . ASN B 1 6  ? 40.31906 -19.55146 25.36351 1.000 15.35624  ?  5   ASN B CB  1 
ATOM   721  C CG  . ASN B 1 6  ? 40.92807 -20.57517 24.43177 1.000 17.25582  ?  5   ASN B CG  1 
ATOM   722  O OD1 . ASN B 1 6  ? 40.25167 -21.46448 23.90585 1.000 19.05670  ?  5   ASN B OD1 1 
ATOM   723  N ND2 . ASN B 1 6  ? 42.22076 -20.43472 24.19484 1.000 18.14659  ?  5   ASN B ND2 1 
ATOM   724  N N   . PHE B 1 7  ? 37.41570 -20.00137 24.71881 1.000 18.98148  ?  6   PHE B N   1 
ATOM   725  C CA  . PHE B 1 7  ? 36.19936 -20.52067 24.10852 1.000 13.06633  ?  6   PHE B CA  1 
ATOM   726  C C   . PHE B 1 7  ? 36.52047 -21.54789 23.04368 1.000 13.94747  ?  6   PHE B C   1 
ATOM   727  O O   . PHE B 1 7  ? 35.69022 -22.42782 22.75691 1.000 12.16953  ?  6   PHE B O   1 
ATOM   728  C CB  . PHE B 1 7  ? 35.35286 -19.38766 23.53263 1.000 12.79382  ?  6   PHE B CB  1 
ATOM   729  C CG  . PHE B 1 7  ? 34.08033 -19.88014 22.89143 1.000 12.22879  ?  6   PHE B CG  1 
ATOM   730  C CD1 . PHE B 1 7  ? 33.02076 -20.28524 23.66877 1.000 12.23937  ?  6   PHE B CD1 1 
ATOM   731  C CD2 . PHE B 1 7  ? 33.96865 -19.96001 21.51866 1.000 12.35307  ?  6   PHE B CD2 1 
ATOM   732  C CE1 . PHE B 1 7  ? 31.84243 -20.75946 23.08370 1.000 14.90632  ?  6   PHE B CE1 1 
ATOM   733  C CE2 . PHE B 1 7  ? 32.82419 -20.42257 20.92895 1.000 12.42344  ?  6   PHE B CE2 1 
ATOM   734  C CZ  . PHE B 1 7  ? 31.74868 -20.82086 21.70726 1.000 15.24292  ?  6   PHE B CZ  1 
ATOM   735  N N   . GLY B 1 8  ? 37.70658 -21.46001 22.43462 1.000 14.08884  ?  7   GLY B N   1 
ATOM   736  C CA  . GLY B 1 8  ? 38.08048 -22.47219 21.46469 1.000 13.33061  ?  7   GLY B CA  1 
ATOM   737  C C   . GLY B 1 8  ? 38.13439 -23.84508 22.09391 1.000 12.91497  ?  7   GLY B C   1 
ATOM   738  O O   . GLY B 1 8  ? 37.65365 -24.82678 21.51696 1.000 14.63139  ?  7   GLY B O   1 
ATOM   739  N N   . LYS B 1 9  ? 38.67287 -23.92579 23.31093 1.000 16.25571  ?  8   LYS B N   1 
ATOM   740  C CA  . LYS B 1 9  ? 38.73621 -25.20386 24.01500 1.000 19.49034  ?  8   LYS B CA  1 
ATOM   741  C C   . LYS B 1 9  ? 37.37547 -25.60767 24.55648 1.000 21.14029  ?  8   LYS B C   1 
ATOM   742  O O   . LYS B 1 9  ? 37.04700 -26.80087 24.58205 1.000 15.67324  ?  8   LYS B O   1 
ATOM   743  C CB  . LYS B 1 9  ? 39.76439 -25.14248 25.14818 1.000 16.91511  ?  8   LYS B CB  1 
ATOM   744  C CG  . LYS B 1 9  ? 41.20926 -25.01290 24.68834 1.000 19.57422  ?  8   LYS B CG  1 
ATOM   745  C CD  . LYS B 1 9  ? 41.57801 -26.05547 23.66089 1.000 41.67105  ?  8   LYS B CD  1 
ATOM   746  C CE  . LYS B 1 9  ? 42.94702 -25.75934 23.04861 1.000 56.51953  ?  8   LYS B CE  1 
ATOM   747  N NZ  . LYS B 1 9  ? 43.28461 -26.72106 21.96364 1.000 56.83229  ?  8   LYS B NZ  1 
ATOM   748  N N   . ALA B 1 10 ? 36.57167 -24.64308 25.01359 1.000 11.11583  ?  9   ALA B N   1 
ATOM   749  C CA  . ALA B 1 10 ? 35.20699 -24.99540 25.38986 1.000 10.40123  ?  9   ALA B CA  1 
ATOM   750  C C   . ALA B 1 10 ? 34.41000 -25.47499 24.18143 1.000 11.92255  ?  9   ALA B C   1 
ATOM   751  O O   . ALA B 1 10 ? 33.57944 -26.39333 24.29280 1.000 13.05738  ?  9   ALA B O   1 
ATOM   752  C CB  . ALA B 1 10 ? 34.51748 -23.81026 26.04570 1.000 10.58230  ?  9   ALA B CB  1 
ATOM   753  N N   . LEU B 1 11 ? 34.66095 -24.88576 23.00874 1.000 10.65001  ?  10  LEU B N   1 
ATOM   754  C CA  . LEU B 1 11 ? 33.92439 -25.30358 21.81849 1.000 12.91546  ?  10  LEU B CA  1 
ATOM   755  C C   . LEU B 1 11 ? 34.30650 -26.72474 21.40216 1.000 10.24391  ?  10  LEU B C   1 
ATOM   756  O O   . LEU B 1 11 ? 33.44017 -27.51291 20.99164 1.000 12.34619  ?  10  LEU B O   1 
ATOM   757  C CB  . LEU B 1 11 ? 34.18255 -24.30682 20.67992 1.000 12.49591  ?  10  LEU B CB  1 
ATOM   758  C CG  . LEU B 1 11 ? 33.51968 -24.67881 19.34349 1.000 11.52899  ?  10  LEU B CG  1 
ATOM   759  C CD1 . LEU B 1 11 ? 32.00423 -24.75036 19.50696 1.000 12.48538  ?  10  LEU B CD1 1 
ATOM   760  C CD2 . LEU B 1 11 ? 33.90534 -23.63071 18.32974 1.000 14.60178  ?  10  LEU B CD2 1 
ATOM   761  N N   . GLU B 1 12 ? 35.59976 -27.06195 21.45225 1.000 9.64425   ?  11  GLU B N   1 
ATOM   762  C CA  . GLU B 1 12 ? 36.01927 -28.43866 21.19478 1.000 10.80897  ?  11  GLU B CA  1 
ATOM   763  C C   . GLU B 1 12 ? 35.31530 -29.39205 22.14937 1.000 13.17273  ?  11  GLU B C   1 
ATOM   764  O O   . GLU B 1 12 ? 34.82376 -30.45383 21.74020 1.000 15.41617  ?  11  GLU B O   1 
ATOM   765  C CB  . GLU B 1 12 ? 37.54141 -28.55798 21.33389 1.000 14.20662  ?  11  GLU B CB  1 
ATOM   766  C CG  . GLU B 1 12 ? 38.23246 -29.18051 20.16952 1.000 37.87559  ?  11  GLU B CG  1 
ATOM   767  C CD  . GLU B 1 12 ? 39.69772 -28.73868 20.07171 1.000 65.13605  ?  11  GLU B CD  1 
ATOM   768  O OE1 . GLU B 1 12 ? 40.33156 -28.52703 21.13114 1.000 42.19161  ?  11  GLU B OE1 1 
ATOM   769  O OE2 . GLU B 1 12 ? 40.21035 -28.58691 18.93720 1.000 62.94917  -1 11  GLU B OE2 1 
ATOM   770  N N   . ALA B 1 13 ? 35.23266 -29.01645 23.42420 1.000 11.13126  ?  12  ALA B N   1 
ATOM   771  C CA  . ALA B 1 13 ? 34.52234 -29.84636 24.39451 1.000 14.35638  ?  12  ALA B CA  1 
ATOM   772  C C   . ALA B 1 13 ? 33.05150 -29.99895 24.02180 1.000 16.00380  ?  12  ALA B C   1 
ATOM   773  O O   . ALA B 1 13 ? 32.50285 -31.10372 24.07666 1.000 13.42857  ?  12  ALA B O   1 
ATOM   774  C CB  . ALA B 1 13 ? 34.66487 -29.24023 25.79135 1.000 12.71949  ?  12  ALA B CB  1 
ATOM   775  N N   . LEU B 1 14 ? 32.39683 -28.90581 23.63399 1.000 10.12517  ?  13  LEU B N   1 
ATOM   776  C CA  . LEU B 1 14 ? 30.99292 -28.98301 23.23956 1.000 10.03201  ?  13  LEU B CA  1 
ATOM   777  C C   . LEU B 1 14 ? 30.80573 -29.97504 22.10346 1.000 11.10496  ?  13  LEU B C   1 
ATOM   778  O O   . LEU B 1 14 ? 29.93338 -30.85399 22.16562 1.000 13.54921  ?  13  LEU B O   1 
ATOM   779  C CB  . LEU B 1 14 ? 30.49986 -27.59896 22.83916 1.000 13.06026  ?  13  LEU B CB  1 
ATOM   780  C CG  . LEU B 1 14 ? 30.16112 -26.65565 23.99623 1.000 14.29533  ?  13  LEU B CG  1 
ATOM   781  C CD1 . LEU B 1 14 ? 30.09103 -25.19225 23.50700 1.000 9.54020   ?  13  LEU B CD1 1 
ATOM   782  C CD2 . LEU B 1 14 ? 28.83558 -27.09911 24.60409 1.000 13.06434  ?  13  LEU B CD2 1 
ATOM   783  N N   . LYS B 1 15 ? 31.62694 -29.85050 21.05572 1.000 10.62554  ?  14  LYS B N   1 
ATOM   784  C CA  . LYS B 1 15 ? 31.50807 -30.72051 19.89174 1.000 12.81194  ?  14  LYS B CA  1 
ATOM   785  C C   . LYS B 1 15 ? 31.78292 -32.18169 20.22271 1.000 12.94429  ?  14  LYS B C   1 
ATOM   786  O O   . LYS B 1 15 ? 31.30340 -33.07118 19.50950 1.000 14.28291  ?  14  LYS B O   1 
ATOM   787  C CB  . LYS B 1 15 ? 32.44322 -30.23867 18.79105 1.000 15.40826  ?  14  LYS B CB  1 
ATOM   788  C CG  . LYS B 1 15 ? 32.07204 -28.84876 18.19337 1.000 10.23460  ?  14  LYS B CG  1 
ATOM   789  C CD  . LYS B 1 15 ? 33.01058 -28.52510 17.03950 1.000 15.80863  ?  14  LYS B CD  1 
ATOM   790  C CE  . LYS B 1 15 ? 32.65063 -27.25345 16.30783 1.000 13.56406  ?  14  LYS B CE  1 
ATOM   791  N NZ  . LYS B 1 15 ? 33.77055 -26.79696 15.41131 1.000 12.19109  ?  14  LYS B NZ  1 
ATOM   792  N N   . GLU B 1 16 ? 32.53274 -32.45052 21.28582 1.000 13.23973  ?  15  GLU B N   1 
ATOM   793  C CA  . GLU B 1 16 ? 32.80402 -33.80944 21.74783 1.000 14.57175  ?  15  GLU B CA  1 
ATOM   794  C C   . GLU B 1 16 ? 31.72528 -34.31934 22.69324 1.000 19.16863  ?  15  GLU B C   1 
ATOM   795  O O   . GLU B 1 16 ? 31.81068 -35.46472 23.15950 1.000 17.38311  ?  15  GLU B O   1 
ATOM   796  C CB  . GLU B 1 16 ? 34.20284 -33.85516 22.40457 1.000 13.78646  ?  15  GLU B CB  1 
ATOM   797  C CG  . GLU B 1 16 ? 35.29005 -33.66777 21.34147 1.000 14.66106  ?  15  GLU B CG  1 
ATOM   798  C CD  . GLU B 1 16 ? 36.70819 -33.49602 21.85643 1.000 32.63150  ?  15  GLU B CD  1 
ATOM   799  O OE1 . GLU B 1 16 ? 36.92063 -33.48156 23.08461 1.000 25.55818  ?  15  GLU B OE1 1 
ATOM   800  O OE2 . GLU B 1 16 ? 37.60928 -33.33653 20.99753 1.000 28.81532  -1 15  GLU B OE2 1 
ATOM   801  N N   . GLY B 1 17 ? 30.69126 -33.51645 22.95030 1.000 15.20860  ?  16  GLY B N   1 
ATOM   802  C CA  . GLY B 1 17 ? 29.57419 -33.96602 23.76213 1.000 13.14374  ?  16  GLY B CA  1 
ATOM   803  C C   . GLY B 1 17 ? 29.70694 -33.69152 25.23828 1.000 21.79728  ?  16  GLY B C   1 
ATOM   804  O O   . GLY B 1 17 ? 28.96671 -34.28065 26.03214 1.000 22.07056  ?  16  GLY B O   1 
ATOM   805  N N   . LYS B 1 18 ? 30.61654 -32.81464 25.63604 1.000 18.18978  ?  17  LYS B N   1 
ATOM   806  C CA  . LYS B 1 18 ? 30.76840 -32.46351 27.04040 1.000 14.69953  ?  17  LYS B CA  1 
ATOM   807  C C   . LYS B 1 18 ? 29.92679 -31.24915 27.40704 1.000 17.89523  ?  17  LYS B C   1 
ATOM   808  O O   . LYS B 1 18 ? 29.49177 -30.48569 26.54383 1.000 18.32603  ?  17  LYS B O   1 
ATOM   809  C CB  . LYS B 1 18 ? 32.23566 -32.18522 27.34607 1.000 14.61284  ?  17  LYS B CB  1 
ATOM   810  C CG  . LYS B 1 18 ? 33.14765 -33.36017 27.05715 1.000 15.23986  ?  17  LYS B CG  1 
ATOM   811  C CD  . LYS B 1 18 ? 34.57946 -32.99713 27.38800 1.000 19.85499  ?  17  LYS B CD  1 
ATOM   812  C CE  . LYS B 1 18 ? 35.48404 -34.21789 27.25431 1.000 26.98066  ?  17  LYS B CE  1 
ATOM   813  N NZ  . LYS B 1 18 ? 36.90794 -33.81594 27.37882 1.000 45.25889  ?  17  LYS B NZ  1 
ATOM   814  N N   . LYS B 1 19 ? 29.72216 -31.06775 28.71775 1.000 16.87801  ?  18  LYS B N   1 
ATOM   815  C CA  . LYS B 1 19 ? 29.05520 -29.89724 29.27607 1.000 16.34668  ?  18  LYS B CA  1 
ATOM   816  C C   . LYS B 1 19 ? 30.09453 -28.85812 29.63260 1.000 14.24067  ?  18  LYS B C   1 
ATOM   817  O O   . LYS B 1 19 ? 31.20037 -29.20460 30.05584 1.000 15.55954  ?  18  LYS B O   1 
ATOM   818  C CB  . LYS B 1 19 ? 28.26208 -30.27415 30.53287 1.000 14.82000  ?  18  LYS B CB  1 
ATOM   819  C CG  . LYS B 1 19 ? 27.25239 -31.39347 30.31949 1.000 19.36638  ?  18  LYS B CG  1 
ATOM   820  C CD  . LYS B 1 19 ? 26.42157 -31.64527 31.57953 1.000 21.49769  ?  18  LYS B CD  1 
ATOM   821  C CE  . LYS B 1 19 ? 27.13115 -32.54328 32.56693 1.000 35.60369  ?  18  LYS B CE  1 
ATOM   822  N NZ  . LYS B 1 19 ? 27.04121 -33.97610 32.14768 1.000 65.00565  ?  18  LYS B NZ  1 
ATOM   823  N N   . VAL B 1 20 ? 29.75964 -27.58634 29.43363 1.000 14.18395  ?  19  VAL B N   1 
ATOM   824  C CA  . VAL B 1 20 ? 30.69222 -26.49721 29.72766 1.000 14.79030  ?  19  VAL B CA  1 
ATOM   825  C C   . VAL B 1 20 ? 29.95805 -25.37043 30.43298 1.000 15.34023  ?  19  VAL B C   1 
ATOM   826  O O   . VAL B 1 20 ? 28.74202 -25.21211 30.30006 1.000 15.15307  ?  19  VAL B O   1 
ATOM   827  C CB  . VAL B 1 20 ? 31.40218 -25.92929 28.46923 1.000 13.76290  ?  19  VAL B CB  1 
ATOM   828  C CG1 . VAL B 1 20 ? 32.22996 -27.00005 27.78052 1.000 14.15109  ?  19  VAL B CG1 1 
ATOM   829  C CG2 . VAL B 1 20 ? 30.37571 -25.28404 27.52556 1.000 14.78722  ?  19  VAL B CG2 1 
ATOM   830  N N   . SER B 1 21 ? 30.71777 -24.57955 31.19665 1.000 15.65640  ?  20  SER B N   1 
ATOM   831  C CA  . SER B 1 21 ? 30.17088 -23.38365 31.82179 1.000 19.84900  ?  20  SER B CA  1 
ATOM   832  C C   . SER B 1 21 ? 31.30266 -22.40561 32.09511 1.000 19.56126  ?  20  SER B C   1 
ATOM   833  O O   . SER B 1 21 ? 32.48601 -22.71019 31.89789 1.000 18.95385  ?  20  SER B O   1 
ATOM   834  C CB  . SER B 1 21 ? 29.42372 -23.69537 33.10976 1.000 24.16496  ?  20  SER B CB  1 
ATOM   835  O OG  . SER B 1 21 ? 30.29209 -24.30556 34.03562 1.000 33.21261  ?  20  SER B OG  1 
ATOM   836  N N   . ARG B 1 22 ? 30.91237 -21.21369 32.54334 1.000 16.87292  ?  21  ARG B N   1 
ATOM   837  C CA  . ARG B 1 22 ? 31.82150 -20.10377 32.78552 1.000 16.41872  ?  21  ARG B CA  1 
ATOM   838  C C   . ARG B 1 22 ? 31.74818 -19.69347 34.24633 1.000 18.56651  ?  21  ARG B C   1 
ATOM   839  O O   . ARG B 1 22 ? 30.64811 -19.54030 34.78399 1.000 18.82835  ?  21  ARG B O   1 
ATOM   840  C CB  . ARG B 1 22 ? 31.44951 -18.88440 31.92186 1.000 17.66761  ?  21  ARG B CB  1 
ATOM   841  C CG  . ARG B 1 22 ? 32.04864 -18.88565 30.55792 1.000 21.19827  ?  21  ARG B CG  1 
ATOM   842  C CD  . ARG B 1 22 ? 31.81110 -17.52945 29.90901 1.000 17.85306  ?  21  ARG B CD  1 
ATOM   843  N NE  . ARG B 1 22 ? 32.50265 -16.48587 30.64800 1.000 18.79488  ?  21  ARG B NE  1 
ATOM   844  C CZ  . ARG B 1 22 ? 32.06826 -15.23830 30.75720 1.000 20.21060  ?  21  ARG B CZ  1 
ATOM   845  N NH1 . ARG B 1 22 ? 30.95795 -14.83714 30.15890 1.000 16.95488  ?  21  ARG B NH1 1 
ATOM   846  N NH2 . ARG B 1 22 ? 32.73317 -14.38509 31.52726 1.000 18.51310  ?  21  ARG B NH2 1 
ATOM   847  N N   . GLU B 1 23 ? 32.91630 -19.46652 34.87547 1.000 21.22959  ?  22  GLU B N   1 
ATOM   848  C CA  . GLU B 1 23 ? 32.91516 -18.90967 36.22791 1.000 20.66113  ?  22  GLU B CA  1 
ATOM   849  C C   . GLU B 1 23 ? 32.21130 -17.56089 36.25912 1.000 25.40496  ?  22  GLU B C   1 
ATOM   850  O O   . GLU B 1 23 ? 31.53486 -17.22441 37.24096 1.000 23.12151  ?  22  GLU B O   1 
ATOM   851  C CB  . GLU B 1 23 ? 34.34569 -18.74858 36.75870 1.000 27.43888  ?  22  GLU B CB  1 
ATOM   852  C CG  . GLU B 1 23 ? 35.28440 -19.94311 36.52450 1.000 32.34372  ?  22  GLU B CG  1 
ATOM   853  C CD  . GLU B 1 23 ? 36.62535 -19.81213 37.25614 1.000 58.67016  ?  22  GLU B CD  1 
ATOM   854  O OE1 . GLU B 1 23 ? 36.78851 -18.85095 38.04322 1.000 70.64206  ?  22  GLU B OE1 1 
ATOM   855  O OE2 . GLU B 1 23 ? 37.51375 -20.67560 37.04506 1.000 61.85727  -1 22  GLU B OE2 1 
ATOM   856  N N   . GLY B 1 24 ? 32.36790 -16.76659 35.19063 1.000 21.07634  ?  23  GLY B N   1 
ATOM   857  C CA  . GLY B 1 24 ? 31.86898 -15.39815 35.13286 1.000 21.39632  ?  23  GLY B CA  1 
ATOM   858  C C   . GLY B 1 24 ? 30.39367 -15.23201 34.83100 1.000 17.97861  ?  23  GLY B C   1 
ATOM   859  O O   . GLY B 1 24 ? 29.89805 -14.10124 34.76760 1.000 23.08924  ?  23  GLY B O   1 
ATOM   860  N N   . TRP B 1 25 ? 29.67781 -16.32443 34.61499 1.000 17.38746  ?  24  TRP B N   1 
ATOM   861  C CA  . TRP B 1 25 ? 28.23205 -16.25673 34.45510 1.000 16.64619  ?  24  TRP B CA  1 
ATOM   862  C C   . TRP B 1 25 ? 27.61027 -15.81660 35.76618 1.000 17.20669  ?  24  TRP B C   1 
ATOM   863  O O   . TRP B 1 25 ? 28.10885 -16.15076 36.84130 1.000 22.48214  ?  24  TRP B O   1 
ATOM   864  C CB  . TRP B 1 25 ? 27.68070 -17.62261 34.03836 1.000 15.94830  ?  24  TRP B CB  1 
ATOM   865  C CG  . TRP B 1 25 ? 27.85257 -17.94854 32.58549 1.000 15.31730  ?  24  TRP B CG  1 
ATOM   866  C CD1 . TRP B 1 25 ? 28.21927 -17.09675 31.58635 1.000 15.32862  ?  24  TRP B CD1 1 
ATOM   867  C CD2 . TRP B 1 25 ? 27.59256 -19.20976 31.96598 1.000 16.38967  ?  24  TRP B CD2 1 
ATOM   868  N NE1 . TRP B 1 25 ? 28.22304 -17.75935 30.38802 1.000 14.76852  ?  24  TRP B NE1 1 
ATOM   869  C CE2 . TRP B 1 25 ? 27.84937 -19.06170 30.59750 1.000 14.35692  ?  24  TRP B CE2 1 
ATOM   870  C CE3 . TRP B 1 25 ? 27.18676 -20.45583 32.44744 1.000 14.64773  ?  24  TRP B CE3 1 
ATOM   871  C CZ2 . TRP B 1 25 ? 27.69705 -20.11189 29.69656 1.000 15.48439  ?  24  TRP B CZ2 1 
ATOM   872  C CZ3 . TRP B 1 25 ? 27.04726 -21.50658 31.55851 1.000 14.14496  ?  24  TRP B CZ3 1 
ATOM   873  C CH2 . TRP B 1 25 ? 27.29618 -21.32774 30.19715 1.000 15.13131  ?  24  TRP B CH2 1 
ATOM   874  N N   . ASN B 1 26 ? 26.51709 -15.04244 35.67291 1.000 18.78310  ?  25  ASN B N   1 
ATOM   875  C CA  . ASN B 1 26 ? 25.83162 -14.54742 36.87214 1.000 19.79108  ?  25  ASN B CA  1 
ATOM   876  C C   . ASN B 1 26 ? 24.98538 -15.64365 37.52220 1.000 23.03753  ?  25  ASN B C   1 
ATOM   877  O O   . ASN B 1 26 ? 25.05860 -15.85379 38.73494 1.000 31.61927  ?  25  ASN B O   1 
ATOM   878  C CB  . ASN B 1 26 ? 24.96581 -13.32963 36.52461 1.000 22.38888  ?  25  ASN B CB  1 
ATOM   879  C CG  . ASN B 1 26 ? 25.79531 -12.12406 36.09602 1.000 20.01066  ?  25  ASN B CG  1 
ATOM   880  O OD1 . ASN B 1 26 ? 26.83580 -11.83621 36.68373 1.000 22.81653  ?  25  ASN B OD1 1 
ATOM   881  N ND2 . ASN B 1 26 ? 25.33102 -11.40863 35.07707 1.000 18.40416  ?  25  ASN B ND2 1 
ATOM   882  N N   . GLY B 1 27 ? 24.18172 -16.35580 36.73653 1.000 27.91859  ?  26  GLY B N   1 
ATOM   883  C CA  . GLY B 1 27 ? 23.52611 -17.54762 37.24823 1.000 26.99586  ?  26  GLY B CA  1 
ATOM   884  C C   . GLY B 1 27 ? 24.52767 -18.65723 37.51114 1.000 27.18791  ?  26  GLY B C   1 
ATOM   885  O O   . GLY B 1 27 ? 25.55484 -18.77264 36.83989 1.000 30.73335  ?  26  GLY B O   1 
ATOM   886  N N   . LYS B 1 28 ? 24.24096 -19.47573 38.52305 1.000 25.78196  ?  27  LYS B N   1 
ATOM   887  C CA  . LYS B 1 28 ? 25.15277 -20.53890 38.93105 1.000 26.17180  ?  27  LYS B CA  1 
ATOM   888  C C   . LYS B 1 28 ? 24.52132 -21.90741 38.69541 1.000 29.04642  ?  27  LYS B C   1 
ATOM   889  O O   . LYS B 1 28 ? 23.29945 -22.04206 38.59861 1.000 27.70790  ?  27  LYS B O   1 
ATOM   890  C CB  . LYS B 1 28 ? 25.54582 -20.39335 40.40426 1.000 23.86772  ?  27  LYS B CB  1 
ATOM   891  C CG  . LYS B 1 28 ? 26.16230 -19.03115 40.75332 1.000 31.92115  ?  27  LYS B CG  1 
ATOM   892  C CD  . LYS B 1 28 ? 27.33573 -18.65629 39.82496 1.000 27.16634  ?  27  LYS B CD  1 
ATOM   893  C CE  . LYS B 1 28 ? 27.76743 -17.20590 40.07123 1.000 38.76595  ?  27  LYS B CE  1 
ATOM   894  N NZ  . LYS B 1 28 ? 28.92710 -16.81610 39.22365 1.000 40.66889  ?  27  LYS B NZ  1 
ATOM   895  N N   . GLY B 1 29 ? 25.37200 -22.92793 38.58808 1.000 23.09639  ?  28  GLY B N   1 
ATOM   896  C CA  . GLY B 1 29 ? 24.88022 -24.26731 38.30781 1.000 19.56140  ?  28  GLY B CA  1 
ATOM   897  C C   . GLY B 1 29 ? 24.37593 -24.48903 36.90077 1.000 28.73844  ?  28  GLY B C   1 
ATOM   898  O O   . GLY B 1 29 ? 23.69894 -25.49392 36.65497 1.000 25.30766  ?  28  GLY B O   1 
ATOM   899  N N   . MET B 1 30 ? 24.68444 -23.59186 35.96568 1.000 22.69263  ?  29  MET B N   1 
ATOM   900  C CA  . MET B 1 30 ? 24.27168 -23.74125 34.57759 1.000 17.24450  ?  29  MET B CA  1 
ATOM   901  C C   . MET B 1 30 ? 25.35453 -24.44045 33.76118 1.000 20.85574  ?  29  MET B C   1 
ATOM   902  O O   . MET B 1 30 ? 26.53199 -24.47575 34.12907 1.000 24.37585  ?  29  MET B O   1 
ATOM   903  C CB  . MET B 1 30 ? 23.95807 -22.37795 33.95633 1.000 19.21483  ?  29  MET B CB  1 
ATOM   904  C CG  . MET B 1 30 ? 22.91626 -21.55517 34.74612 1.000 17.87267  ?  29  MET B CG  1 
ATOM   905  S SD  . MET B 1 30 ? 22.41763 -20.05670 33.86522 1.000 25.16379  ?  29  MET B SD  1 
ATOM   906  C CE  . MET B 1 30 ? 23.97635 -19.20859 33.79681 1.000 17.87825  ?  29  MET B CE  1 
ATOM   907  N N   . PHE B 1 31 ? 24.94913 -24.98382 32.62326 1.000 20.72588  ?  30  PHE B N   1 
ATOM   908  C CA  . PHE B 1 31 ? 25.93230 -25.51310 31.68645 1.000 16.30614  ?  30  PHE B CA  1 
ATOM   909  C C   . PHE B 1 31 ? 25.32201 -25.53474 30.28989 1.000 17.24057  ?  30  PHE B C   1 
ATOM   910  O O   . PHE B 1 31 ? 24.10194 -25.67482 30.13134 1.000 18.38419  ?  30  PHE B O   1 
ATOM   911  C CB  . PHE B 1 31 ? 26.42408 -26.91895 32.08396 1.000 19.48902  ?  30  PHE B CB  1 
ATOM   912  C CG  . PHE B 1 31 ? 25.32745 -27.95563 32.13564 1.000 20.47055  ?  30  PHE B CG  1 
ATOM   913  C CD1 . PHE B 1 31 ? 24.89537 -28.59755 30.98304 1.000 14.64998  ?  30  PHE B CD1 1 
ATOM   914  C CD2 . PHE B 1 31 ? 24.73553 -28.29052 33.33602 1.000 21.18141  ?  30  PHE B CD2 1 
ATOM   915  C CE1 . PHE B 1 31 ? 23.87787 -29.52885 31.02646 1.000 17.74950  ?  30  PHE B CE1 1 
ATOM   916  C CE2 . PHE B 1 31 ? 23.71813 -29.25165 33.39186 1.000 21.76341  ?  30  PHE B CE2 1 
ATOM   917  C CZ  . PHE B 1 31 ? 23.28996 -29.86617 32.24768 1.000 19.71858  ?  30  PHE B CZ  1 
ATOM   918  N N   . ALA B 1 32 ? 26.18780 -25.42369 29.28245 1.000 16.76237  ?  31  ALA B N   1 
ATOM   919  C CA  . ALA B 1 32 ? 25.78728 -25.54353 27.89047 1.000 12.70651  ?  31  ALA B CA  1 
ATOM   920  C C   . ALA B 1 32 ? 26.24589 -26.87869 27.30210 1.000 16.10284  ?  31  ALA B C   1 
ATOM   921  O O   . ALA B 1 32 ? 27.21066 -27.49169 27.77354 1.000 14.63802  ?  31  ALA B O   1 
ATOM   922  C CB  . ALA B 1 32 ? 26.33640 -24.36428 27.07822 1.000 13.28545  ?  31  ALA B CB  1 
ATOM   923  N N   . TYR B 1 33 ? 25.53090 -27.33966 26.27161 1.000 12.37758  ?  32  TYR B N   1 
ATOM   924  C CA  . TYR B 1 33 ? 25.84528 -28.59332 25.60099 1.000 12.29289  ?  32  TYR B CA  1 
ATOM   925  C C   . TYR B 1 33 ? 25.35232 -28.54485 24.15705 1.000 15.23535  ?  32  TYR B C   1 
ATOM   926  O O   . TYR B 1 33 ? 24.50624 -27.72149 23.77832 1.000 17.53954  ?  32  TYR B O   1 
ATOM   927  C CB  . TYR B 1 33 ? 25.26279 -29.81036 26.33500 1.000 17.42901  ?  32  TYR B CB  1 
ATOM   928  C CG  . TYR B 1 33 ? 23.75488 -29.84933 26.43566 1.000 17.38392  ?  32  TYR B CG  1 
ATOM   929  C CD1 . TYR B 1 33 ? 23.09546 -29.14377 27.42721 1.000 18.50885  ?  32  TYR B CD1 1 
ATOM   930  C CD2 . TYR B 1 33 ? 22.99177 -30.60898 25.55530 1.000 17.33385  ?  32  TYR B CD2 1 
ATOM   931  C CE1 . TYR B 1 33 ? 21.71327 -29.17627 27.54507 1.000 18.11650  ?  32  TYR B CE1 1 
ATOM   932  C CE2 . TYR B 1 33 ? 21.60115 -30.63962 25.66646 1.000 20.72968  ?  32  TYR B CE2 1 
ATOM   933  C CZ  . TYR B 1 33 ? 20.97669 -29.92715 26.67398 1.000 21.70845  ?  32  TYR B CZ  1 
ATOM   934  O OH  . TYR B 1 33 ? 19.59621 -29.93545 26.82166 1.000 26.61280  ?  32  TYR B OH  1 
ATOM   935  N N   . TYR B 1 34 ? 25.90724 -29.44680 23.36215 1.000 11.87639  ?  33  TYR B N   1 
ATOM   936  C CA  . TYR B 1 34 ? 25.65945 -29.55740 21.93042 1.000 11.71941  ?  33  TYR B CA  1 
ATOM   937  C C   . TYR B 1 34 ? 24.54528 -30.55383 21.64959 1.000 17.76012  ?  33  TYR B C   1 
ATOM   938  O O   . TYR B 1 34 ? 24.46896 -31.61054 22.28668 1.000 18.24177  ?  33  TYR B O   1 
ATOM   939  C CB  . TYR B 1 34 ? 26.95084 -30.02924 21.26218 1.000 11.48994  ?  33  TYR B CB  1 
ATOM   940  C CG  . TYR B 1 34 ? 26.93941 -30.28825 19.77239 1.000 12.22426  ?  33  TYR B CG  1 
ATOM   941  C CD1 . TYR B 1 34 ? 26.55022 -31.52093 19.25493 1.000 20.58265  ?  33  TYR B CD1 1 
ATOM   942  C CD2 . TYR B 1 34 ? 27.36535 -29.31427 18.88304 1.000 15.50598  ?  33  TYR B CD2 1 
ATOM   943  C CE1 . TYR B 1 34 ? 26.57331 -31.76226 17.88519 1.000 19.26730  ?  33  TYR B CE1 1 
ATOM   944  C CE2 . TYR B 1 34 ? 27.40432 -29.55946 17.50807 1.000 16.41626  ?  33  TYR B CE2 1 
ATOM   945  C CZ  . TYR B 1 34 ? 26.99138 -30.77087 17.02755 1.000 16.20019  ?  33  TYR B CZ  1 
ATOM   946  O OH  . TYR B 1 34 ? 27.03113 -31.00225 15.67249 1.000 23.72714  ?  33  TYR B OH  1 
ATOM   947  N N   . VAL B 1 35 ? 23.70632 -30.24037 20.66425 1.000 13.08859  ?  34  VAL B N   1 
ATOM   948  C CA  . VAL B 1 35 ? 22.64925 -31.13326 20.21201 1.000 15.22137  ?  34  VAL B CA  1 
ATOM   949  C C   . VAL B 1 35 ? 22.82902 -31.35738 18.71504 1.000 18.42422  ?  34  VAL B C   1 
ATOM   950  O O   . VAL B 1 35 ? 22.88473 -30.39049 17.95252 1.000 17.38048  ?  34  VAL B O   1 
ATOM   951  C CB  . VAL B 1 35 ? 21.24689 -30.58185 20.50984 1.000 17.50390  ?  34  VAL B CB  1 
ATOM   952  C CG1 . VAL B 1 35 ? 20.20235 -31.63505 20.14393 1.000 20.67360  ?  34  VAL B CG1 1 
ATOM   953  C CG2 . VAL B 1 35 ? 21.12830 -30.20489 21.97442 1.000 18.66070  ?  34  VAL B CG2 1 
ATOM   954  N N   . PRO B 1 36 ? 22.94583 -32.59945 18.24822 1.000 22.38253  ?  35  PRO B N   1 
ATOM   955  C CA  . PRO B 1 36 ? 23.15339 -32.84619 16.81772 1.000 22.37537  ?  35  PRO B CA  1 
ATOM   956  C C   . PRO B 1 36 ? 21.94004 -32.47097 15.98934 1.000 24.25784  ?  35  PRO B C   1 
ATOM   957  O O   . PRO B 1 36 ? 20.81275 -32.38061 16.48079 1.000 23.35431  ?  35  PRO B O   1 
ATOM   958  C CB  . PRO B 1 36 ? 23.40363 -34.36263 16.74235 1.000 23.45061  ?  35  PRO B CB  1 
ATOM   959  C CG  . PRO B 1 36 ? 23.80725 -34.75933 18.12504 1.000 31.60933  ?  35  PRO B CG  1 
ATOM   960  C CD  . PRO B 1 36 ? 23.03394 -33.83424 19.03995 1.000 23.36438  ?  35  PRO B CD  1 
ATOM   961  N N   . GLY B 1 37 ? 22.19244 -32.26869 14.69844 1.000 22.60762  ?  36  GLY B N   1 
ATOM   962  C CA  . GLY B 1 37 ? 21.13107 -32.02143 13.75276 1.000 23.07332  ?  36  GLY B CA  1 
ATOM   963  C C   . GLY B 1 37 ? 20.43925 -33.31333 13.38086 1.000 24.38709  ?  36  GLY B C   1 
ATOM   964  O O   . GLY B 1 37 ? 20.79932 -34.39915 13.83603 1.000 25.89045  ?  36  GLY B O   1 
ATOM   965  N N   . GLY B 1 38 ? 19.42772 -33.19165 12.53301 1.000 24.89870  ?  37  GLY B N   1 
ATOM   966  C CA  . GLY B 1 38 ? 18.66038 -34.35583 12.14751 1.000 27.05472  ?  37  GLY B CA  1 
ATOM   967  C C   . GLY B 1 38 ? 17.57238 -34.01665 11.15197 1.000 26.67519  ?  37  GLY B C   1 
ATOM   968  O O   . GLY B 1 38 ? 17.57669 -32.95113 10.53495 1.000 25.94034  ?  37  GLY B O   1 
ATOM   969  N N   . VAL B 1 39 ? 16.64257 -34.95646 10.99228 1.000 27.98680  ?  38  VAL B N   1 
ATOM   970  C CA  . VAL B 1 39 ? 15.62199 -34.89209 9.95212  1.000 28.59134  ?  38  VAL B CA  1 
ATOM   971  C C   . VAL B 1 39 ? 14.34230 -35.49901 10.49960 1.000 45.29617  ?  38  VAL B C   1 
ATOM   972  O O   . VAL B 1 39 ? 14.31372 -36.69291 10.81743 1.000 52.36248  ?  38  VAL B O   1 
ATOM   973  C CB  . VAL B 1 39 ? 16.04806 -35.66430 8.68435  1.000 31.77871  ?  38  VAL B CB  1 
ATOM   974  C CG1 . VAL B 1 39 ? 14.92915 -35.66411 7.67588  1.000 33.86538  ?  38  VAL B CG1 1 
ATOM   975  C CG2 . VAL B 1 39 ? 17.34126 -35.10913 8.06990  1.000 33.46017  ?  38  VAL B CG2 1 
ATOM   976  N N   . TYR B 1 40 ? 13.27145 -34.71497 10.59466 1.000 45.08146  ?  39  TYR B N   1 
ATOM   977  C CA  . TYR B 1 40 ? 11.97438 -35.25473 10.98822 1.000 51.66953  ?  39  TYR B CA  1 
ATOM   978  C C   . TYR B 1 40 ? 10.93768 -35.05180 9.88492  1.000 54.08067  ?  39  TYR B C   1 
ATOM   979  O O   . TYR B 1 40 ? 10.95796 -34.04090 9.17087  1.000 45.14984  ?  39  TYR B O   1 
ATOM   980  C CB  . TYR B 1 40 ? 11.48019 -34.63128 12.30723 1.000 43.35046  ?  39  TYR B CB  1 
ATOM   981  C CG  . TYR B 1 40 ? 11.15827 -33.14866 12.26174 1.000 63.71968  ?  39  TYR B CG  1 
ATOM   982  C CD1 . TYR B 1 40 ? 9.89314  -32.70044 11.88673 1.000 59.05820  ?  39  TYR B CD1 1 
ATOM   983  C CD2 . TYR B 1 40 ? 12.10324 -32.19802 12.63470 1.000 64.43682  ?  39  TYR B CD2 1 
ATOM   984  C CE1 . TYR B 1 40 ? 9.58022  -31.34969 11.86049 1.000 39.84494  ?  39  TYR B CE1 1 
ATOM   985  C CE2 . TYR B 1 40 ? 11.80091 -30.83915 12.61437 1.000 54.75941  ?  39  TYR B CE2 1 
ATOM   986  C CZ  . TYR B 1 40 ? 10.53872 -30.42520 12.22643 1.000 61.09940  ?  39  TYR B CZ  1 
ATOM   987  O OH  . TYR B 1 40 ? 10.23349 -29.08145 12.20936 1.000 67.50128  ?  39  TYR B OH  1 
ATOM   988  N N   . LYS B 1 41 ? 10.03642 -36.02723 9.75190  1.000 53.04713  ?  40  LYS B N   1 
ATOM   989  C CA  . LYS B 1 41 ? 8.92385  -35.92249 8.82120  1.000 33.25896  ?  40  LYS B CA  1 
ATOM   990  C C   . LYS B 1 41 ? 7.96805  -34.81616 9.25154  1.000 42.31627  ?  40  LYS B C   1 
ATOM   991  O O   . LYS B 1 41 ? 7.78386  -34.54822 10.44090 1.000 44.64062  ?  40  LYS B O   1 
ATOM   992  C CB  . LYS B 1 41 ? 8.17444  -37.25413 8.73719  1.000 52.44701  ?  40  LYS B CB  1 
ATOM   993  C CG  . LYS B 1 41 ? 9.00554  -38.41815 8.20468  1.000 50.70213  ?  40  LYS B CG  1 
ATOM   994  C CD  . LYS B 1 41 ? 9.14712  -38.34899 6.69008  1.000 63.33744  ?  40  LYS B CD  1 
ATOM   995  C CE  . LYS B 1 41 ? 10.27003 -39.24188 6.20486  1.000 56.96244  ?  40  LYS B CE  1 
ATOM   996  N NZ  . LYS B 1 41 ? 11.54619 -38.87891 6.88732  1.000 69.72531  ?  40  LYS B NZ  1 
ATOM   997  N N   . SER B 1 42 ? 7.34997  -34.17268 8.26648  1.000 49.35913  ?  41  SER B N   1 
ATOM   998  C CA  . SER B 1 42 ? 6.41963  -33.08390 8.54853  1.000 64.32194  ?  41  SER B CA  1 
ATOM   999  C C   . SER B 1 42 ? 5.13211  -33.61910 9.17907  1.000 52.02161  ?  41  SER B C   1 
ATOM   1000 O O   . SER B 1 42 ? 4.54599  -34.59135 8.69476  1.000 49.56570  ?  41  SER B O   1 
ATOM   1001 C CB  . SER B 1 42 ? 6.11455  -32.30974 7.26436  1.000 49.07405  ?  41  SER B CB  1 
ATOM   1002 O OG  . SER B 1 42 ? 7.26063  -31.58743 6.82616  1.000 38.40423  ?  41  SER B OG  1 
ATOM   1003 N N   . GLN B 1 43 ? 4.68414  -32.95884 10.25180 1.000 55.08829  ?  42  GLN B N   1 
ATOM   1004 C CA  . GLN B 1 43 ? 3.61956  -33.48743 11.10212 1.000 51.64676  ?  42  GLN B CA  1 
ATOM   1005 C C   . GLN B 1 43 ? 2.24538  -33.33133 10.46327 1.000 53.07528  ?  42  GLN B C   1 
ATOM   1006 O O   . GLN B 1 43 ? 1.43091  -34.26088 10.49470 1.000 54.05134  ?  42  GLN B O   1 
ATOM   1007 C CB  . GLN B 1 43 ? 3.63322  -32.79155 12.46720 1.000 55.56912  ?  42  GLN B CB  1 
ATOM   1008 C CG  . GLN B 1 43 ? 4.84525  -33.07807 13.34349 1.000 72.02961  ?  42  GLN B CG  1 
ATOM   1009 C CD  . GLN B 1 43 ? 6.14055  -32.54002 12.75728 1.000 90.32926  ?  42  GLN B CD  1 
ATOM   1010 O OE1 . GLN B 1 43 ? 6.35526  -31.32309 12.66968 1.000 68.35968  ?  42  GLN B OE1 1 
ATOM   1011 N NE2 . GLN B 1 43 ? 7.00583  -33.45261 12.33246 1.000 88.49839  ?  42  GLN B NE2 1 
ATOM   1012 N N   . THR B 1 44 ? 1.96098  -32.16186 9.89778  1.000 52.44057  ?  43  THR B N   1 
ATOM   1013 C CA  . THR B 1 44 ? 0.65418  -31.87452 9.32282  1.000 49.27080  ?  43  THR B CA  1 
ATOM   1014 C C   . THR B 1 44 ? 0.78468  -31.47672 7.85620  1.000 42.39368  ?  43  THR B C   1 
ATOM   1015 O O   . THR B 1 44 ? 1.86898  -31.15603 7.36136  1.000 41.48939  ?  43  THR B O   1 
ATOM   1016 C CB  . THR B 1 44 ? -0.05069 -30.75020 10.08625 1.000 50.07695  ?  43  THR B CB  1 
ATOM   1017 O OG1 . THR B 1 44 ? 0.67129  -29.52629 9.88175  1.000 41.81833  ?  43  THR B OG1 1 
ATOM   1018 C CG2 . THR B 1 44 ? -0.11658 -31.07157 11.57615 1.000 49.35903  ?  43  THR B CG2 1 
ATOM   1019 N N   . ASP B 1 45 ? -0.35686 -31.47970 7.16112  1.000 37.49200  ?  44  ASP B N   1 
ATOM   1020 C CA  . ASP B 1 45 ? -0.35959 -31.01021 5.78054  1.000 44.94918  ?  44  ASP B CA  1 
ATOM   1021 C C   . ASP B 1 45 ? -0.05636 -29.51841 5.69809  1.000 39.59194  ?  44  ASP B C   1 
ATOM   1022 O O   . ASP B 1 45 ? 0.56538  -29.06814 4.72756  1.000 36.86048  ?  44  ASP B O   1 
ATOM   1023 C CB  . ASP B 1 45 ? -1.69279 -31.33862 5.11241  1.000 48.23487  ?  44  ASP B CB  1 
ATOM   1024 C CG  . ASP B 1 45 ? -1.93081 -32.82754 5.01478  1.000 39.78688  ?  44  ASP B CG  1 
ATOM   1025 O OD1 . ASP B 1 45 ? -0.95050 -33.59323 5.15281  1.000 55.55872  ?  44  ASP B OD1 1 
ATOM   1026 O OD2 . ASP B 1 45 ? -3.09108 -33.23542 4.80325  1.000 56.86454  -1 44  ASP B OD2 1 
ATOM   1027 N N   . VAL B 1 46 ? -0.44697 -28.74111 6.71138  1.000 46.69234  ?  45  VAL B N   1 
ATOM   1028 C CA  . VAL B 1 46 ? -0.07022 -27.33124 6.72565  1.000 47.99753  ?  45  VAL B CA  1 
ATOM   1029 C C   . VAL B 1 46 ? 1.44379  -27.19561 6.81167  1.000 37.61389  ?  45  VAL B C   1 
ATOM   1030 O O   . VAL B 1 46 ? 2.04778  -26.34916 6.13748  1.000 43.09071  ?  45  VAL B O   1 
ATOM   1031 C CB  . VAL B 1 46 ? -0.78332 -26.58693 7.87104  1.000 36.31079  ?  45  VAL B CB  1 
ATOM   1032 C CG1 . VAL B 1 46 ? -0.28462 -25.16002 7.95624  1.000 38.63029  ?  45  VAL B CG1 1 
ATOM   1033 C CG2 . VAL B 1 46 ? -2.29406 -26.61666 7.65170  1.000 43.53272  ?  45  VAL B CG2 1 
ATOM   1034 N N   . ILE B 1 47 ? 2.08874  -28.04595 7.61289  1.000 34.86310  ?  46  ILE B N   1 
ATOM   1035 C CA  . ILE B 1 47 ? 3.55006  -28.03711 7.65493  1.000 33.08375  ?  46  ILE B CA  1 
ATOM   1036 C C   . ILE B 1 47 ? 4.12919  -28.45975 6.30996  1.000 36.30524  ?  46  ILE B C   1 
ATOM   1037 O O   . ILE B 1 47 ? 5.06759  -27.83655 5.80333  1.000 38.22965  ?  46  ILE B O   1 
ATOM   1038 C CB  . ILE B 1 47 ? 4.06250  -28.93097 8.79990  1.000 42.73396  ?  46  ILE B CB  1 
ATOM   1039 C CG1 . ILE B 1 47 ? 3.59464  -28.38149 10.15090 1.000 47.41517  ?  46  ILE B CG1 1 
ATOM   1040 C CG2 . ILE B 1 47 ? 5.57658  -29.02504 8.77243  1.000 32.48076  ?  46  ILE B CG2 1 
ATOM   1041 C CD1 . ILE B 1 47 ? 4.00149  -29.23470 11.32008 1.000 60.01467  ?  46  ILE B CD1 1 
ATOM   1042 N N   . LYS B 1 48 ? 3.58027  -29.52186 5.71075  1.000 31.00284  ?  47  LYS B N   1 
ATOM   1043 C CA  . LYS B 1 48 ? 4.05231  -29.97672 4.40435  1.000 31.11922  ?  47  LYS B CA  1 
ATOM   1044 C C   . LYS B 1 48 ? 3.95998  -28.88250 3.34647  1.000 30.94270  ?  47  LYS B C   1 
ATOM   1045 O O   . LYS B 1 48 ? 4.78264  -28.83624 2.42601  1.000 30.70948  ?  47  LYS B O   1 
ATOM   1046 C CB  . LYS B 1 48 ? 3.24973  -31.19252 3.94823  1.000 32.29254  ?  47  LYS B CB  1 
ATOM   1047 C CG  . LYS B 1 48 ? 3.58576  -32.48682 4.65921  1.000 36.07548  ?  47  LYS B CG  1 
ATOM   1048 C CD  . LYS B 1 48 ? 2.70273  -33.62853 4.12679  1.000 41.91683  ?  47  LYS B CD  1 
ATOM   1049 C CE  . LYS B 1 48 ? 3.02279  -34.95440 4.81444  1.000 53.22606  ?  47  LYS B CE  1 
ATOM   1050 N NZ  . LYS B 1 48 ? 2.00563  -36.00675 4.53705  1.000 43.60262  ?  47  LYS B NZ  1 
ATOM   1051 N N   . ASN B 1 49 ? 2.96965  -28.00120 3.44569  1.000 30.85869  ?  48  ASN B N   1 
ATOM   1052 C CA  . ASN B 1 49 ? 2.83933  -26.95663 2.43968  1.000 30.78413  ?  48  ASN B CA  1 
ATOM   1053 C C   . ASN B 1 49 ? 3.96230  -25.94894 2.51358  1.000 34.32660  ?  48  ASN B C   1 
ATOM   1054 O O   . ASN B 1 49 ? 4.24471  -25.29096 1.50582  1.000 31.10593  ?  48  ASN B O   1 
ATOM   1055 C CB  . ASN B 1 49 ? 1.50775  -26.22510 2.57649  1.000 31.13984  ?  48  ASN B CB  1 
ATOM   1056 C CG  . ASN B 1 49 ? 0.34643  -27.06536 2.12991  1.000 38.00689  ?  48  ASN B CG  1 
ATOM   1057 O OD1 . ASN B 1 49 ? 0.51690  -28.07460 1.43381  1.000 39.22878  ?  48  ASN B OD1 1 
ATOM   1058 N ND2 . ASN B 1 49 ? -0.84972 -26.65552 2.51646  1.000 38.24467  ?  48  ASN B ND2 1 
ATOM   1059 N N   . THR B 1 50 ? 4.59602  -25.80624 3.68036  1.000 31.71065  ?  49  THR B N   1 
ATOM   1060 C CA  . THR B 1 50 ? 5.71648  -24.89178 3.85146  1.000 33.32904  ?  49  THR B CA  1 
ATOM   1061 C C   . THR B 1 50 ? 7.06179  -25.58495 3.76540  1.000 31.14028  ?  49  THR B C   1 
ATOM   1062 O O   . THR B 1 50 ? 7.99936  -25.02214 3.19554  1.000 36.28327  ?  49  THR B O   1 
ATOM   1063 C CB  . THR B 1 50 ? 5.61270  -24.15316 5.19049  1.000 28.76403  ?  49  THR B CB  1 
ATOM   1064 O OG1 . THR B 1 50 ? 4.52121  -23.22333 5.14430  1.000 32.23615  ?  49  THR B OG1 1 
ATOM   1065 C CG2 . THR B 1 50 ? 6.90345  -23.38364 5.48602  1.000 28.20812  ?  49  THR B CG2 1 
ATOM   1066 N N   . PHE B 1 51 ? 7.18654  -26.80205 4.29316  1.000 28.59406  ?  50  PHE B N   1 
ATOM   1067 C CA  . PHE B 1 51 ? 8.49815  -27.42616 4.41392  1.000 39.19830  ?  50  PHE B CA  1 
ATOM   1068 C C   . PHE B 1 51 ? 8.70574  -28.63298 3.50488  1.000 31.49585  ?  50  PHE B C   1 
ATOM   1069 O O   . PHE B 1 51 ? 9.82995  -29.13566 3.42785  1.000 42.93129  ?  50  PHE B O   1 
ATOM   1070 C CB  . PHE B 1 51 ? 8.75368  -27.84257 5.87132  1.000 35.28228  ?  50  PHE B CB  1 
ATOM   1071 C CG  . PHE B 1 51 ? 8.72306  -26.69369 6.85670  1.000 37.91351  ?  50  PHE B CG  1 
ATOM   1072 C CD1 . PHE B 1 51 ? 7.52817  -26.32544 7.47722  1.000 42.63655  ?  50  PHE B CD1 1 
ATOM   1073 C CD2 . PHE B 1 51 ? 9.88535  -25.99006 7.16914  1.000 34.37536  ?  50  PHE B CD2 1 
ATOM   1074 C CE1 . PHE B 1 51 ? 7.48168  -25.27263 8.39088  1.000 37.55060  ?  50  PHE B CE1 1 
ATOM   1075 C CE2 . PHE B 1 51 ? 9.85671  -24.93841 8.09364  1.000 27.46192  ?  50  PHE B CE2 1 
ATOM   1076 C CZ  . PHE B 1 51 ? 8.65013  -24.57791 8.70197  1.000 38.57432  ?  50  PHE B CZ  1 
ATOM   1077 N N   . GLY B 1 52 ? 7.68508  -29.09035 2.80458  1.000 35.51528  ?  51  GLY B N   1 
ATOM   1078 C CA  . GLY B 1 52 ? 7.80788  -30.32506 2.05526  1.000 34.95870  ?  51  GLY B CA  1 
ATOM   1079 C C   . GLY B 1 52 ? 7.63171  -31.53915 2.95345  1.000 38.73725  ?  51  GLY B C   1 
ATOM   1080 O O   . GLY B 1 52 ? 7.15183  -31.45068 4.08802  1.000 37.15776  ?  51  GLY B O   1 
ATOM   1081 N N   . GLU B 1 53 ? 8.05105  -32.69491 2.43849  1.000 31.99188  ?  52  GLU B N   1 
ATOM   1082 C CA  . GLU B 1 53 ? 7.82142  -33.93635 3.16952  1.000 36.02620  ?  52  GLU B CA  1 
ATOM   1083 C C   . GLU B 1 53 ? 8.72792  -34.04808 4.39218  1.000 46.73815  ?  52  GLU B C   1 
ATOM   1084 O O   . GLU B 1 53 ? 8.29146  -34.50950 5.45421  1.000 36.88665  ?  52  GLU B O   1 
ATOM   1085 C CB  . GLU B 1 53 ? 8.00610  -35.13090 2.23845  1.000 37.54409  ?  52  GLU B CB  1 
ATOM   1086 C CG  . GLU B 1 53 ? 6.89531  -35.28348 1.19254  1.000 65.92109  ?  52  GLU B CG  1 
ATOM   1087 C CD  . GLU B 1 53 ? 5.56002  -35.75048 1.77921  1.000 59.98143  ?  52  GLU B CD  1 
ATOM   1088 O OE1 . GLU B 1 53 ? 5.56942  -36.50385 2.77747  1.000 73.46761  ?  52  GLU B OE1 1 
ATOM   1089 O OE2 . GLU B 1 53 ? 4.49819  -35.36451 1.23992  1.000 48.79516  -1 52  GLU B OE2 1 
ATOM   1090 N N   . GLU B 1 54 ? 9.98257  -33.62598 4.27635  1.000 43.40369  ?  53  GLU B N   1 
ATOM   1091 C CA  . GLU B 1 54 ? 10.91419 -33.71310 5.38933  1.000 37.70769  ?  53  GLU B CA  1 
ATOM   1092 C C   . GLU B 1 54 ? 11.47936 -32.34831 5.71657  1.000 36.02017  ?  53  GLU B C   1 
ATOM   1093 O O   . GLU B 1 54 ? 11.51439 -31.44008 4.88205  1.000 34.29484  ?  53  GLU B O   1 
ATOM   1094 C CB  . GLU B 1 54 ? 12.09449 -34.65302 5.11317  1.000 39.31904  ?  53  GLU B CB  1 
ATOM   1095 C CG  . GLU B 1 54 ? 11.75100 -36.10918 4.97102  1.000 56.56855  ?  53  GLU B CG  1 
ATOM   1096 C CD  . GLU B 1 54 ? 12.95674 -36.90260 4.53143  1.000 55.72946  ?  53  GLU B CD  1 
ATOM   1097 O OE1 . GLU B 1 54 ? 14.05330 -36.30639 4.48209  1.000 53.98519  ?  53  GLU B OE1 1 
ATOM   1098 O OE2 . GLU B 1 54 ? 12.81270 -38.10483 4.22979  1.000 90.21003  -1 53  GLU B OE2 1 
ATOM   1099 N N   . VAL B 1 55 ? 11.94937 -32.25487 6.95530  1.000 37.10243  ?  54  VAL B N   1 
ATOM   1100 C CA  . VAL B 1 55 ? 12.55214 -31.06557 7.52787  1.000 37.97020  ?  54  VAL B CA  1 
ATOM   1101 C C   . VAL B 1 55 ? 13.92313 -31.48237 8.02875  1.000 27.03607  ?  54  VAL B C   1 
ATOM   1102 O O   . VAL B 1 55 ? 14.02097 -32.37096 8.88342  1.000 37.56116  ?  54  VAL B O   1 
ATOM   1103 C CB  . VAL B 1 55 ? 11.69864 -30.51154 8.68231  1.000 36.10522  ?  54  VAL B CB  1 
ATOM   1104 C CG1 . VAL B 1 55 ? 12.17280 -29.15193 9.09989  1.000 32.74415  ?  54  VAL B CG1 1 
ATOM   1105 C CG2 . VAL B 1 55 ? 10.22217 -30.46506 8.29900  1.000 42.79136  ?  54  VAL B CG2 1 
ATOM   1106 N N   . LYS B 1 56 ? 14.97397 -30.86690 7.49801  1.000 26.43886  ?  55  LYS B N   1 
ATOM   1107 C CA  . LYS B 1 56 ? 16.32044 -31.03608 8.03916  1.000 25.88126  ?  55  LYS B CA  1 
ATOM   1108 C C   . LYS B 1 56 ? 16.63536 -29.88834 8.99070  1.000 24.82472  ?  55  LYS B C   1 
ATOM   1109 O O   . LYS B 1 56 ? 16.46899 -28.72418 8.62712  1.000 24.50270  ?  55  LYS B O   1 
ATOM   1110 C CB  . LYS B 1 56 ? 17.35589 -31.09897 6.91474  1.000 27.10548  ?  55  LYS B CB  1 
ATOM   1111 C CG  . LYS B 1 56 ? 18.77629 -31.26190 7.40368  1.000 33.97054  ?  55  LYS B CG  1 
ATOM   1112 C CD  . LYS B 1 56 ? 19.63615 -31.92375 6.34161  1.000 52.86360  ?  55  LYS B CD  1 
ATOM   1113 C CE  . LYS B 1 56 ? 19.99951 -30.94242 5.25537  1.000 50.83255  ?  55  LYS B CE  1 
ATOM   1114 N NZ  . LYS B 1 56 ? 21.00485 -29.95900 5.74670  1.000 57.73882  ?  55  LYS B NZ  1 
ATOM   1115 N N   . TYR B 1 57 ? 17.06039 -30.20574 10.21202 1.000 24.47820  ?  56  TYR B N   1 
ATOM   1116 C CA  . TYR B 1 57 ? 17.42244 -29.17564 11.17599 1.000 23.64725  ?  56  TYR B CA  1 
ATOM   1117 C C   . TYR B 1 57 ? 18.89655 -29.28915 11.54477 1.000 24.33923  ?  56  TYR B C   1 
ATOM   1118 O O   . TYR B 1 57 ? 19.44331 -30.39510 11.66706 1.000 23.25609  ?  56  TYR B O   1 
ATOM   1119 C CB  . TYR B 1 57 ? 16.54921 -29.21662 12.44252 1.000 23.91821  ?  56  TYR B CB  1 
ATOM   1120 C CG  . TYR B 1 57 ? 16.68521 -30.46243 13.28488 1.000 24.40795  ?  56  TYR B CG  1 
ATOM   1121 C CD1 . TYR B 1 57 ? 15.93601 -31.59270 12.99414 1.000 33.31541  ?  56  TYR B CD1 1 
ATOM   1122 C CD2 . TYR B 1 57 ? 17.54096 -30.50376 14.38134 1.000 23.97841  ?  56  TYR B CD2 1 
ATOM   1123 C CE1 . TYR B 1 57 ? 16.04447 -32.75059 13.74897 1.000 33.04229  ?  56  TYR B CE1 1 
ATOM   1124 C CE2 . TYR B 1 57 ? 17.66042 -31.67246 15.15052 1.000 29.63878  ?  56  TYR B CE2 1 
ATOM   1125 C CZ  . TYR B 1 57 ? 16.90115 -32.78513 14.82398 1.000 31.34517  ?  56  TYR B CZ  1 
ATOM   1126 O OH  . TYR B 1 57 ? 16.97587 -33.96058 15.55295 1.000 36.19536  ?  56  TYR B OH  1 
ATOM   1127 N N   . ARG B 1 58 ? 19.53931 -28.13101 11.70819 1.000 17.01222  ?  57  ARG B N   1 
ATOM   1128 C CA  . ARG B 1 58 ? 20.96106 -28.07486 11.96162 1.000 16.40143  ?  57  ARG B CA  1 
ATOM   1129 C C   . ARG B 1 58 ? 21.25989 -28.39362 13.41643 1.000 15.77094  ?  57  ARG B C   1 
ATOM   1130 O O   . ARG B 1 58 ? 20.40107 -28.24030 14.28735 1.000 17.36771  ?  57  ARG B O   1 
ATOM   1131 C CB  . ARG B 1 58 ? 21.50046 -26.68206 11.64953 1.000 19.61983  ?  57  ARG B CB  1 
ATOM   1132 C CG  . ARG B 1 58 ? 21.21935 -26.19469 10.25245 1.000 23.19784  ?  57  ARG B CG  1 
ATOM   1133 C CD  . ARG B 1 58 ? 21.93448 -24.88254 10.04851 1.000 23.79565  ?  57  ARG B CD  1 
ATOM   1134 N NE  . ARG B 1 58 ? 21.90487 -24.47475 8.65821  1.000 31.06509  ?  57  ARG B NE  1 
ATOM   1135 C CZ  . ARG B 1 58 ? 22.70681 -23.55894 8.14667  1.000 40.99201  ?  57  ARG B CZ  1 
ATOM   1136 N NH1 . ARG B 1 58 ? 23.65300 -22.99425 8.87630  1.000 41.65009  ?  57  ARG B NH1 1 
ATOM   1137 N NH2 . ARG B 1 58 ? 22.55533 -23.20344 6.87210  1.000 37.32183  ?  57  ARG B NH2 1 
ATOM   1138 N N   . PRO B 1 59 ? 22.48768 -28.79485 13.71885 1.000 15.27188  ?  58  PRO B N   1 
ATOM   1139 C CA  . PRO B 1 59 ? 22.88449 -28.88690 15.12526 1.000 19.09426  ?  58  PRO B CA  1 
ATOM   1140 C C   . PRO B 1 59 ? 22.74539 -27.53624 15.80630 1.000 20.74958  ?  58  PRO B C   1 
ATOM   1141 O O   . PRO B 1 59 ? 22.76073 -26.47868 15.16480 1.000 15.45844  ?  58  PRO B O   1 
ATOM   1142 C CB  . PRO B 1 59 ? 24.34057 -29.33204 15.04938 1.000 18.23260  ?  58  PRO B CB  1 
ATOM   1143 C CG  . PRO B 1 59 ? 24.78977 -28.92270 13.70465 1.000 25.48911  ?  58  PRO B CG  1 
ATOM   1144 C CD  . PRO B 1 59 ? 23.61150 -29.08861 12.81742 1.000 15.27040  ?  58  PRO B CD  1 
ATOM   1145 N N   . TYR B 1 60 ? 22.59439 -27.56574 17.12770 1.000 14.56318  ?  59  TYR B N   1 
ATOM   1146 C CA  . TYR B 1 60 ? 22.47035 -26.30842 17.85469 1.000 14.59082  ?  59  TYR B CA  1 
ATOM   1147 C C   . TYR B 1 60 ? 23.04572 -26.48486 19.25298 1.000 15.35827  ?  59  TYR B C   1 
ATOM   1148 O O   . TYR B 1 60 ? 23.52615 -27.56176 19.61649 1.000 18.74007  ?  59  TYR B O   1 
ATOM   1149 C CB  . TYR B 1 60 ? 21.01377 -25.84054 17.88833 1.000 18.94164  ?  59  TYR B CB  1 
ATOM   1150 C CG  . TYR B 1 60 ? 20.08659 -26.79190 18.60325 1.000 16.45302  ?  59  TYR B CG  1 
ATOM   1151 C CD1 . TYR B 1 60 ? 19.53548 -27.87689 17.94033 1.000 19.39793  ?  59  TYR B CD1 1 
ATOM   1152 C CD2 . TYR B 1 60 ? 19.75335 -26.58624 19.93929 1.000 15.65337  ?  59  TYR B CD2 1 
ATOM   1153 C CE1 . TYR B 1 60 ? 18.66692 -28.75763 18.58300 1.000 17.62887  ?  59  TYR B CE1 1 
ATOM   1154 C CE2 . TYR B 1 60 ? 18.89104 -27.45477 20.58989 1.000 18.96317  ?  59  TYR B CE2 1 
ATOM   1155 C CZ  . TYR B 1 60 ? 18.35524 -28.53398 19.90386 1.000 30.40351  ?  59  TYR B CZ  1 
ATOM   1156 O OH  . TYR B 1 60 ? 17.50566 -29.38699 20.54763 1.000 23.92664  ?  59  TYR B OH  1 
ATOM   1157 N N   . LEU B 1 61 ? 23.03992 -25.40575 20.02167 1.000 14.31436  ?  60  LEU B N   1 
ATOM   1158 C CA  . LEU B 1 61 ? 23.54363 -25.42326 21.38337 1.000 14.15590  ?  60  LEU B CA  1 
ATOM   1159 C C   . LEU B 1 61 ? 22.39923 -25.16894 22.35748 1.000 19.26394  ?  60  LEU B C   1 
ATOM   1160 O O   . LEU B 1 61 ? 21.46691 -24.41158 22.06035 1.000 17.34098  ?  60  LEU B O   1 
ATOM   1161 C CB  . LEU B 1 61 ? 24.65317 -24.38076 21.55683 1.000 14.64451  ?  60  LEU B CB  1 
ATOM   1162 C CG  . LEU B 1 61 ? 25.87086 -24.55340 20.63458 1.000 13.54395  ?  60  LEU B CG  1 
ATOM   1163 C CD1 . LEU B 1 61 ? 26.88439 -23.43065 20.90695 1.000 13.43542  ?  60  LEU B CD1 1 
ATOM   1164 C CD2 . LEU B 1 61 ? 26.54025 -25.88364 20.83648 1.000 13.54452  ?  60  LEU B CD2 1 
ATOM   1165 N N   . ALA B 1 62 ? 22.47243 -25.80283 23.53360 1.000 15.88739  ?  61  ALA B N   1 
ATOM   1166 C CA  . ALA B 1 62 ? 21.43145 -25.68130 24.54855 1.000 17.17030  ?  61  ALA B CA  1 
ATOM   1167 C C   . ALA B 1 62 ? 22.04660 -25.27436 25.87709 1.000 15.79975  ?  61  ALA B C   1 
ATOM   1168 O O   . ALA B 1 62 ? 23.21613 -25.55003 26.14904 1.000 16.43413  ?  61  ALA B O   1 
ATOM   1169 C CB  . ALA B 1 62 ? 20.66792 -26.98254 24.72021 1.000 17.33306  ?  61  ALA B CB  1 
ATOM   1170 N N   . LEU B 1 63 ? 21.24954 -24.60358 26.70486 1.000 17.07627  ?  62  LEU B N   1 
ATOM   1171 C CA  . LEU B 1 63 ? 21.67335 -24.18298 28.03445 1.000 16.52296  ?  62  LEU B CA  1 
ATOM   1172 C C   . LEU B 1 63 ? 20.70310 -24.72502 29.07827 1.000 19.14632  ?  62  LEU B C   1 
ATOM   1173 O O   . LEU B 1 63 ? 19.48966 -24.51904 28.96796 1.000 18.23628  ?  62  LEU B O   1 
ATOM   1174 C CB  . LEU B 1 63 ? 21.74745 -22.64712 28.13945 1.000 16.55472  ?  62  LEU B CB  1 
ATOM   1175 C CG  . LEU B 1 63 ? 22.32001 -22.11582 29.45555 1.000 16.82522  ?  62  LEU B CG  1 
ATOM   1176 C CD1 . LEU B 1 63 ? 23.83620 -22.15869 29.44275 1.000 16.77329  ?  62  LEU B CD1 1 
ATOM   1177 C CD2 . LEU B 1 63 ? 21.82355 -20.69659 29.78092 1.000 18.97486  ?  62  LEU B CD2 1 
ATOM   1178 N N   . LYS B 1 64 ? 21.23076 -25.42260 30.08779 1.000 18.03124  ?  63  LYS B N   1 
ATOM   1179 C CA  . LYS B 1 64 ? 20.45015 -25.72380 31.28868 1.000 20.07905  ?  63  LYS B CA  1 
ATOM   1180 C C   . LYS B 1 64 ? 20.49942 -24.50159 32.20551 1.000 19.45008  ?  63  LYS B C   1 
ATOM   1181 O O   . LYS B 1 64 ? 21.55121 -24.18435 32.77326 1.000 26.34492  ?  63  LYS B O   1 
ATOM   1182 C CB  . LYS B 1 64 ? 20.98819 -26.96646 31.99509 1.000 22.25724  ?  63  LYS B CB  1 
ATOM   1183 C CG  . LYS B 1 64 ? 20.72157 -26.94272 33.51373 1.000 37.84971  ?  63  LYS B CG  1 
ATOM   1184 C CD  . LYS B 1 64 ? 19.97554 -28.14415 33.94959 1.000 35.86143  ?  63  LYS B CD  1 
ATOM   1185 C CE  . LYS B 1 64 ? 20.27509 -28.47884 35.41697 1.000 73.22792  ?  63  LYS B CE  1 
ATOM   1186 N NZ  . LYS B 1 64 ? 19.69748 -29.82045 35.83779 1.000 50.04215  ?  63  LYS B NZ  1 
ATOM   1187 N N   . THR B 1 65 ? 19.36864 -23.81545 32.35155 1.000 20.55620  ?  64  THR B N   1 
ATOM   1188 C CA  . THR B 1 65 ? 19.31287 -22.51243 33.00330 1.000 20.68815  ?  64  THR B CA  1 
ATOM   1189 C C   . THR B 1 65 ? 19.22602 -22.66117 34.52089 1.000 31.82758  ?  64  THR B C   1 
ATOM   1190 O O   . THR B 1 65 ? 19.15481 -23.77266 35.06105 1.000 24.11260  ?  64  THR B O   1 
ATOM   1191 C CB  . THR B 1 65 ? 18.11718 -21.72255 32.49260 1.000 24.02186  ?  64  THR B CB  1 
ATOM   1192 O OG1 . THR B 1 65 ? 16.91961 -22.34351 32.96689 1.000 28.10982  ?  64  THR B OG1 1 
ATOM   1193 C CG2 . THR B 1 65 ? 18.08227 -21.70619 30.97916 1.000 20.32264  ?  64  THR B CG2 1 
ATOM   1194 N N   . VAL B 1 66 ? 19.23807 -21.51611 35.22432 1.000 22.35709  ?  65  VAL B N   1 
ATOM   1195 C CA  . VAL B 1 66 ? 19.04135 -21.55398 36.67181 1.000 29.98889  ?  65  VAL B CA  1 
ATOM   1196 C C   . VAL B 1 66 ? 17.66566 -22.11186 37.01448 1.000 39.65273  ?  65  VAL B C   1 
ATOM   1197 O O   . VAL B 1 66 ? 17.50180 -22.78278 38.03852 1.000 46.39505  ?  65  VAL B O   1 
ATOM   1198 C CB  . VAL B 1 66 ? 19.25984 -20.15935 37.31799 1.000 27.78225  ?  65  VAL B CB  1 
ATOM   1199 C CG1 . VAL B 1 66 ? 20.64829 -19.66601 37.03525 1.000 32.64567  ?  65  VAL B CG1 1 
ATOM   1200 C CG2 . VAL B 1 66 ? 18.22010 -19.13815 36.85288 1.000 29.38047  ?  65  VAL B CG2 1 
ATOM   1201 N N   . ASP B 1 67 ? 16.66150 -21.86553 36.16668 1.000 29.29275  ?  66  ASP B N   1 
ATOM   1202 C CA  . ASP B 1 67 ? 15.33200 -22.43956 36.37425 1.000 35.28193  ?  66  ASP B CA  1 
ATOM   1203 C C   . ASP B 1 67 ? 15.27640 -23.93154 36.07694 1.000 48.67107  ?  66  ASP B C   1 
ATOM   1204 O O   . ASP B 1 67 ? 14.19251 -24.51554 36.16242 1.000 46.83887  ?  66  ASP B O   1 
ATOM   1205 C CB  . ASP B 1 67 ? 14.30672 -21.70191 35.50986 1.000 36.70134  ?  66  ASP B CB  1 
ATOM   1206 C CG  . ASP B 1 67 ? 14.35630 -20.19415 35.71242 1.000 60.58947  ?  66  ASP B CG  1 
ATOM   1207 O OD1 . ASP B 1 67 ? 14.52529 -19.75850 36.87669 1.000 47.32081  ?  66  ASP B OD1 1 
ATOM   1208 O OD2 . ASP B 1 67 ? 14.24437 -19.44233 34.71490 1.000 45.94931  -1 66  ASP B OD2 1 
ATOM   1209 N N   . ASN B 1 68 ? 16.40057 -24.55739 35.71993 1.000 37.39031  ?  67  ASN B N   1 
ATOM   1210 C CA  . ASN B 1 68 ? 16.50582 -25.98518 35.43481 1.000 35.29096  ?  67  ASN B CA  1 
ATOM   1211 C C   . ASN B 1 68 ? 15.71511 -26.41443 34.21024 1.000 33.18454  ?  67  ASN B C   1 
ATOM   1212 O O   . ASN B 1 68 ? 15.53757 -27.62240 33.99277 1.000 52.76843  ?  67  ASN B O   1 
ATOM   1213 C CB  . ASN B 1 68 ? 16.08833 -26.83631 36.63825 1.000 36.24729  ?  67  ASN B CB  1 
ATOM   1214 C CG  . ASN B 1 68 ? 17.08242 -26.73643 37.76510 1.000 67.39237  ?  67  ASN B CG  1 
ATOM   1215 O OD1 . ASN B 1 68 ? 18.18908 -27.27686 37.67743 1.000 57.48589  ?  67  ASN B OD1 1 
ATOM   1216 N ND2 . ASN B 1 68 ? 16.71565 -26.01160 38.82121 1.000 75.12822  ?  67  ASN B ND2 1 
ATOM   1217 N N   . ASP B 1 69 ? 15.23249 -25.47205 33.40668 1.000 31.64263  ?  68  ASP B N   1 
ATOM   1218 C CA  . ASP B 1 69 ? 14.69246 -25.77700 32.09298 1.000 24.95412  ?  68  ASP B CA  1 
ATOM   1219 C C   . ASP B 1 69 ? 15.77557 -25.54764 31.04030 1.000 27.07342  ?  68  ASP B C   1 
ATOM   1220 O O   . ASP B 1 69 ? 16.87108 -25.08223 31.34447 1.000 24.70982  ?  68  ASP B O   1 
ATOM   1221 C CB  . ASP B 1 69 ? 13.41573 -24.95933 31.80931 1.000 26.52157  ?  68  ASP B CB  1 
ATOM   1222 C CG  . ASP B 1 69 ? 13.60537 -23.45552 31.93638 1.000 40.81288  ?  68  ASP B CG  1 
ATOM   1223 O OD1 . ASP B 1 69 ? 14.75609 -22.96642 31.93169 1.000 40.32017  ?  68  ASP B OD1 1 
ATOM   1224 O OD2 . ASP B 1 69 ? 12.56967 -22.75091 32.03588 1.000 42.05098  -1 68  ASP B OD2 1 
ATOM   1225 N N   . ILE B 1 70 ? 15.46867 -25.90416 29.79320 1.000 21.76890  ?  69  ILE B N   1 
ATOM   1226 C CA  . ILE B 1 70 ? 16.44987 -25.89895 28.71366 1.000 21.44255  ?  69  ILE B CA  1 
ATOM   1227 C C   . ILE B 1 70 ? 16.09804 -24.79089 27.73622 1.000 24.47754  ?  69  ILE B C   1 
ATOM   1228 O O   . ILE B 1 70 ? 14.98463 -24.75139 27.19181 1.000 24.80194  ?  69  ILE B O   1 
ATOM   1229 C CB  . ILE B 1 70 ? 16.50876 -27.24821 27.99109 1.000 26.42249  ?  69  ILE B CB  1 
ATOM   1230 C CG1 . ILE B 1 70 ? 16.70712 -28.36969 29.00364 1.000 22.14752  ?  69  ILE B CG1 1 
ATOM   1231 C CG2 . ILE B 1 70 ? 17.62576 -27.23236 26.94712 1.000 23.18662  ?  69  ILE B CG2 1 
ATOM   1232 C CD1 . ILE B 1 70 ? 17.96822 -28.22089 29.82429 1.000 30.56159  ?  69  ILE B CD1 1 
ATOM   1233 N N   . ALA B 1 71 ? 17.05507 -23.91454 27.49235 1.000 19.23874  ?  70  ALA B N   1 
ATOM   1234 C CA  . ALA B 1 71 ? 16.92680 -22.85196 26.51048 1.000 19.80019  ?  70  ALA B CA  1 
ATOM   1235 C C   . ALA B 1 71 ? 17.84003 -23.14733 25.32821 1.000 17.92061  ?  70  ALA B C   1 
ATOM   1236 O O   . ALA B 1 71 ? 18.86583 -23.81815 25.47412 1.000 22.36959  ?  70  ALA B O   1 
ATOM   1237 C CB  . ALA B 1 71 ? 17.28361 -21.50244 27.13078 1.000 22.14165  ?  70  ALA B CB  1 
ATOM   1238 N N   . THR B 1 72 ? 17.44742 -22.69558 24.14128 1.000 17.91758  ?  71  THR B N   1 
ATOM   1239 C CA  . THR B 1 72 ? 18.42619 -22.65067 23.06740 1.000 17.62829  ?  71  THR B CA  1 
ATOM   1240 C C   . THR B 1 72 ? 19.41503 -21.55546 23.40342 1.000 18.78630  ?  71  THR B C   1 
ATOM   1241 O O   . THR B 1 72 ? 19.09342 -20.60861 24.12156 1.000 21.00518  ?  71  THR B O   1 
ATOM   1242 C CB  . THR B 1 72 ? 17.78021 -22.35949 21.72799 1.000 22.60789  ?  71  THR B CB  1 
ATOM   1243 O OG1 . THR B 1 72 ? 17.07314 -21.12461 21.84103 1.000 25.76731  ?  71  THR B OG1 1 
ATOM   1244 C CG2 . THR B 1 72 ? 16.81491 -23.46905 21.34511 1.000 17.77215  ?  71  THR B CG2 1 
ATOM   1245 N N   . TRP B 1 73 ? 20.63452 -21.69165 22.91585 1.000 16.03926  ?  72  TRP B N   1 
ATOM   1246 C CA  . TRP B 1 73 ? 21.68623 -20.85215 23.45227 1.000 15.61748  ?  72  TRP B CA  1 
ATOM   1247 C C   . TRP B 1 73 ? 22.63689 -20.44953 22.34831 1.000 17.58448  ?  72  TRP B C   1 
ATOM   1248 O O   . TRP B 1 73 ? 22.99998 -21.27095 21.50296 1.000 18.68974  ?  72  TRP B O   1 
ATOM   1249 C CB  . TRP B 1 73 ? 22.46456 -21.58276 24.55342 1.000 15.29235  ?  72  TRP B CB  1 
ATOM   1250 C CG  . TRP B 1 73 ? 23.58620 -20.75497 25.13937 1.000 15.57687  ?  72  TRP B CG  1 
ATOM   1251 C CD1 . TRP B 1 73 ? 23.45084 -19.61963 25.89617 1.000 15.42097  ?  72  TRP B CD1 1 
ATOM   1252 C CD2 . TRP B 1 73 ? 24.99435 -21.00196 25.03629 1.000 14.44981  ?  72  TRP B CD2 1 
ATOM   1253 N NE1 . TRP B 1 73 ? 24.68414 -19.14621 26.25760 1.000 15.37316  ?  72  TRP B NE1 1 
ATOM   1254 C CE2 . TRP B 1 73 ? 25.65111 -19.96432 25.73524 1.000 14.71692  ?  72  TRP B CE2 1 
ATOM   1255 C CE3 . TRP B 1 73 ? 25.75873 -21.98030 24.41052 1.000 17.92352  ?  72  TRP B CE3 1 
ATOM   1256 C CZ2 . TRP B 1 73 ? 27.04115 -19.89098 25.83735 1.000 14.13262  ?  72  TRP B CZ2 1 
ATOM   1257 C CZ3 . TRP B 1 73 ? 27.12363 -21.91495 24.51783 1.000 17.05904  ?  72  TRP B CZ3 1 
ATOM   1258 C CH2 . TRP B 1 73 ? 27.75684 -20.87698 25.22554 1.000 17.68075  ?  72  TRP B CH2 1 
ATOM   1259 N N   . THR B 1 74 ? 23.04370 -19.18452 22.37420 1.000 17.84279  ?  73  THR B N   1 
ATOM   1260 C CA  . THR B 1 74 ? 24.13803 -18.71128 21.53886 1.000 26.48518  ?  73  THR B CA  1 
ATOM   1261 C C   . THR B 1 74 ? 25.08070 -17.90340 22.42844 1.000 22.80277  ?  73  THR B C   1 
ATOM   1262 O O   . THR B 1 74 ? 24.60987 -17.07273 23.21720 1.000 21.01496  ?  73  THR B O   1 
ATOM   1263 C CB  . THR B 1 74 ? 23.57705 -17.86794 20.37539 1.000 34.76091  ?  73  THR B CB  1 
ATOM   1264 O OG1 . THR B 1 74 ? 24.64631 -17.33077 19.58249 1.000 43.18627  ?  73  THR B OG1 1 
ATOM   1265 C CG2 . THR B 1 74 ? 22.66309 -16.74502 20.89528 1.000 37.44443  ?  73  THR B CG2 1 
ATOM   1266 N N   . PRO B 1 75 ? 26.39182 -18.13878 22.37547 1.000 19.35520  ?  74  PRO B N   1 
ATOM   1267 C CA  . PRO B 1 75 ? 27.30808 -17.40011 23.25026 1.000 21.40924  ?  74  PRO B CA  1 
ATOM   1268 C C   . PRO B 1 75 ? 27.22601 -15.90801 22.99336 1.000 25.61974  ?  74  PRO B C   1 
ATOM   1269 O O   . PRO B 1 75 ? 27.03099 -15.47018 21.85742 1.000 23.62576  ?  74  PRO B O   1 
ATOM   1270 C CB  . PRO B 1 75 ? 28.69180 -17.94925 22.87424 1.000 22.75021  ?  74  PRO B CB  1 
ATOM   1271 C CG  . PRO B 1 75 ? 28.45227 -19.15985 22.11810 1.000 21.20217  ?  74  PRO B CG  1 
ATOM   1272 C CD  . PRO B 1 75 ? 27.09993 -19.10518 21.52292 1.000 19.33463  ?  74  PRO B CD  1 
ATOM   1273 N N   . SER B 1 76 ? 27.35704 -15.12488 24.06651 1.000 16.44484  ?  75  SER B N   1 
ATOM   1274 C CA  . SER B 1 76 ? 27.53360 -13.69635 23.88517 1.000 15.71534  ?  75  SER B CA  1 
ATOM   1275 C C   . SER B 1 76 ? 28.98118 -13.40499 23.48449 1.000 16.69090  ?  75  SER B C   1 
ATOM   1276 O O   . SER B 1 76 ? 29.85567 -14.28519 23.50907 1.000 18.79176  ?  75  SER B O   1 
ATOM   1277 C CB  . SER B 1 76 ? 27.17743 -12.94354 25.16085 1.000 18.15964  ?  75  SER B CB  1 
ATOM   1278 O OG  . SER B 1 76 ? 28.20502 -13.16198 26.11775 1.000 16.93201  ?  75  SER B OG  1 
ATOM   1279 N N   . VAL B 1 77 ? 29.23558 -12.15557 23.08517 1.000 18.95348  ?  76  VAL B N   1 
ATOM   1280 C CA  . VAL B 1 77 ? 30.60085 -11.78667 22.72765 1.000 16.27760  ?  76  VAL B CA  1 
ATOM   1281 C C   . VAL B 1 77 ? 31.50116 -11.92757 23.94078 1.000 15.95876  ?  76  VAL B C   1 
ATOM   1282 O O   . VAL B 1 77 ? 32.65058 -12.37820 23.83403 1.000 15.75583  ?  76  VAL B O   1 
ATOM   1283 C CB  . VAL B 1 77 ? 30.63850 -10.36701 22.13347 1.000 17.14670  ?  76  VAL B CB  1 
ATOM   1284 C CG1 . VAL B 1 77 ? 32.06201 -9.84606  22.03622 1.000 22.61259  ?  76  VAL B CG1 1 
ATOM   1285 C CG2 . VAL B 1 77 ? 30.00743 -10.39337 20.75769 1.000 33.65943  ?  76  VAL B CG2 1 
ATOM   1286 N N   . SER B 1 78 ? 30.98183 -11.57810 25.12138 1.000 16.02600  ?  77  SER B N   1 
ATOM   1287 C CA  . SER B 1 78 ? 31.77319 -11.73266 26.33618 1.000 16.84440  ?  77  SER B CA  1 
ATOM   1288 C C   . SER B 1 78 ? 32.04621 -13.20617 26.60971 1.000 16.35065  ?  77  SER B C   1 
ATOM   1289 O O   . SER B 1 78 ? 33.15483 -13.56965 27.03289 1.000 17.24264  ?  77  SER B O   1 
ATOM   1290 C CB  . SER B 1 78 ? 31.06688 -11.07418 27.51523 1.000 16.20914  ?  77  SER B CB  1 
ATOM   1291 O OG  . SER B 1 78 ? 31.08541 -9.63694  27.42375 1.000 24.88580  ?  77  SER B OG  1 
ATOM   1292 N N   . ASP B 1 79 ? 31.05221 -14.06609 26.36489 1.000 14.98693  ?  78  ASP B N   1 
ATOM   1293 C CA  . ASP B 1 79 ? 31.27107 -15.51040 26.42645 1.000 14.50421  ?  78  ASP B CA  1 
ATOM   1294 C C   . ASP B 1 79 ? 32.39986 -15.92799 25.48878 1.000 14.31122  ?  78  ASP B C   1 
ATOM   1295 O O   . ASP B 1 79 ? 33.30413 -16.68622 25.86383 1.000 19.49979  ?  78  ASP B O   1 
ATOM   1296 C CB  . ASP B 1 79 ? 30.00047 -16.26141 26.02649 1.000 14.39210  ?  78  ASP B CB  1 
ATOM   1297 C CG  . ASP B 1 79 ? 28.86967 -16.15031 27.03387 1.000 17.57960  ?  78  ASP B CG  1 
ATOM   1298 O OD1 . ASP B 1 79 ? 29.11736 -15.93758 28.23632 1.000 15.57383  ?  78  ASP B OD1 1 
ATOM   1299 O OD2 . ASP B 1 79 ? 27.71098 -16.31339 26.61013 1.000 17.95710  ?  78  ASP B OD2 1 
ATOM   1300 N N   . ILE B 1 80 ? 32.33060 -15.46987 24.23961 1.000 15.46335  ?  79  ILE B N   1 
ATOM   1301 C CA  . ILE B 1 80 ? 33.29677 -15.86444 23.22079 1.000 14.52095  ?  79  ILE B CA  1 
ATOM   1302 C C   . ILE B 1 80 ? 34.70993 -15.43695 23.59903 1.000 17.92415  ?  79  ILE B C   1 
ATOM   1303 O O   . ILE B 1 80 ? 35.66498 -16.19521 23.39791 1.000 18.76183  ?  79  ILE B O   1 
ATOM   1304 C CB  . ILE B 1 80 ? 32.84342 -15.29684 21.86352 1.000 14.93184  ?  79  ILE B CB  1 
ATOM   1305 C CG1 . ILE B 1 80 ? 31.69652 -16.15532 21.34104 1.000 20.25738  ?  79  ILE B CG1 1 
ATOM   1306 C CG2 . ILE B 1 80 ? 33.95186 -15.28236 20.83222 1.000 19.50403  ?  79  ILE B CG2 1 
ATOM   1307 C CD1 . ILE B 1 80 ? 30.77497 -15.36937 20.52591 1.000 20.40968  ?  79  ILE B CD1 1 
ATOM   1308 N N   . LEU B 1 81 ? 34.86555 -14.24818 24.19461 1.000 15.99857  ?  80  LEU B N   1 
ATOM   1309 C CA  . LEU B 1 81 ? 36.18155 -13.68583 24.49347 1.000 15.46973  ?  80  LEU B CA  1 
ATOM   1310 C C   . LEU B 1 81 ? 36.72559 -14.09318 25.86509 1.000 21.80682  ?  80  LEU B C   1 
ATOM   1311 O O   . LEU B 1 81 ? 37.89514 -13.81417 26.15798 1.000 20.25966  ?  80  LEU B O   1 
ATOM   1312 C CB  . LEU B 1 81 ? 36.12854 -12.14876 24.40310 1.000 16.09879  ?  80  LEU B CB  1 
ATOM   1313 C CG  . LEU B 1 81 ? 35.81351 -11.54216 23.02979 1.000 19.62052  ?  80  LEU B CG  1 
ATOM   1314 C CD1 . LEU B 1 81 ? 35.80489 -10.00292 23.14716 1.000 17.89623  ?  80  LEU B CD1 1 
ATOM   1315 C CD2 . LEU B 1 81 ? 36.83742 -12.01188 21.97345 1.000 16.90413  ?  80  LEU B CD2 1 
ATOM   1316 N N   . ALA B 1 82 ? 35.92630 -14.75165 26.70284 1.000 17.57555  ?  81  ALA B N   1 
ATOM   1317 C CA  . ALA B 1 82 ? 36.31262 -15.07767 28.06943 1.000 21.94879  ?  81  ALA B CA  1 
ATOM   1318 C C   . ALA B 1 82 ? 37.29901 -16.24122 28.12038 1.000 16.51755  ?  81  ALA B C   1 
ATOM   1319 O O   . ALA B 1 82 ? 37.37028 -17.08520 27.22042 1.000 17.39370  ?  81  ALA B O   1 
ATOM   1320 C CB  . ALA B 1 82 ? 35.08078 -15.42927 28.91173 1.000 19.73311  ?  81  ALA B CB  1 
ATOM   1321 N N   . GLU B 1 83 ? 38.03982 -16.30551 29.21814 1.000 16.33899  ?  82  GLU B N   1 
ATOM   1322 C CA  . GLU B 1 83 ? 39.03235 -17.35640 29.43622 1.000 20.55465  ?  82  GLU B CA  1 
ATOM   1323 C C   . GLU B 1 83 ? 38.84288 -18.00820 30.80272 1.000 23.08565  ?  82  GLU B C   1 
ATOM   1324 O O   . GLU B 1 83 ? 39.80563 -18.42044 31.47071 1.000 22.15090  ?  82  GLU B O   1 
ATOM   1325 C CB  . GLU B 1 83 ? 40.43481 -16.78619 29.25312 1.000 23.77288  ?  82  GLU B CB  1 
ATOM   1326 C CG  . GLU B 1 83 ? 40.60218 -16.37099 27.80498 1.000 32.06847  ?  82  GLU B CG  1 
ATOM   1327 C CD  . GLU B 1 83 ? 41.97357 -15.88478 27.45487 1.000 35.31515  ?  82  GLU B CD  1 
ATOM   1328 O OE1 . GLU B 1 83 ? 42.71300 -15.47688 28.37822 1.000 53.94426  ?  82  GLU B OE1 1 
ATOM   1329 O OE2 . GLU B 1 83 ? 42.29616 -15.90378 26.24182 1.000 42.71393  -1 82  GLU B OE2 1 
ATOM   1330 N N   . ASP B 1 84 ? 37.58330 -18.13371 31.21526 1.000 17.63805  ?  83  ASP B N   1 
ATOM   1331 C CA  . ASP B 1 84 ? 37.20162 -18.72620 32.49033 1.000 17.41115  ?  83  ASP B CA  1 
ATOM   1332 C C   . ASP B 1 84 ? 36.23802 -19.89326 32.29182 1.000 19.30709  ?  83  ASP B C   1 
ATOM   1333 O O   . ASP B 1 84 ? 35.41104 -20.17514 33.15544 1.000 17.78415  ?  83  ASP B O   1 
ATOM   1334 C CB  . ASP B 1 84 ? 36.58249 -17.66583 33.40040 1.000 17.09082  ?  83  ASP B CB  1 
ATOM   1335 C CG  . ASP B 1 84 ? 35.29929 -17.05836 32.81273 1.000 21.15672  ?  83  ASP B CG  1 
ATOM   1336 O OD1 . ASP B 1 84 ? 34.98243 -17.31389 31.62392 1.000 19.15716  ?  83  ASP B OD1 1 
ATOM   1337 O OD2 . ASP B 1 84 ? 34.59001 -16.33171 33.54134 1.000 20.99982  -1 83  ASP B OD2 1 
ATOM   1338 N N   . TRP B 1 85 ? 36.32985 -20.56572 31.15440 1.000 15.50738  ?  84  TRP B N   1 
ATOM   1339 C CA  . TRP B 1 85 ? 35.47583 -21.70645 30.84678 1.000 16.12164  ?  84  TRP B CA  1 
ATOM   1340 C C   . TRP B 1 85 ? 35.96322 -22.96476 31.55323 1.000 19.32007  ?  84  TRP B C   1 
ATOM   1341 O O   . TRP B 1 85 ? 37.16598 -23.18710 31.70101 1.000 19.76749  ?  84  TRP B O   1 
ATOM   1342 C CB  . TRP B 1 85 ? 35.45498 -21.96379 29.33972 1.000 14.94123  ?  84  TRP B CB  1 
ATOM   1343 C CG  . TRP B 1 85 ? 34.67868 -20.96976 28.53030 1.000 14.65324  ?  84  TRP B CG  1 
ATOM   1344 C CD1 . TRP B 1 85 ? 35.16126 -19.86529 27.89622 1.000 14.67664  ?  84  TRP B CD1 1 
ATOM   1345 C CD2 . TRP B 1 85 ? 33.26734 -21.00700 28.26459 1.000 14.79872  ?  84  TRP B CD2 1 
ATOM   1346 N NE1 . TRP B 1 85 ? 34.13760 -19.20527 27.23800 1.000 14.89892  ?  84  TRP B NE1 1 
ATOM   1347 C CE2 . TRP B 1 85 ? 32.96620 -19.89626 27.44855 1.000 15.27870  ?  84  TRP B CE2 1 
ATOM   1348 C CE3 . TRP B 1 85 ? 32.23504 -21.88014 28.63406 1.000 16.59114  ?  84  TRP B CE3 1 
ATOM   1349 C CZ2 . TRP B 1 85 ? 31.67124 -19.62910 27.00422 1.000 15.58355  ?  84  TRP B CZ2 1 
ATOM   1350 C CZ3 . TRP B 1 85 ? 30.93783 -21.61418 28.19401 1.000 15.67751  ?  84  TRP B CZ3 1 
ATOM   1351 C CH2 . TRP B 1 85 ? 30.67305 -20.49872 27.38139 1.000 16.52734  ?  84  TRP B CH2 1 
ATOM   1352 N N   . ASN B 1 86 ? 35.01960 -23.83265 31.93127 1.000 18.35231  ?  85  ASN B N   1 
ATOM   1353 C CA  . ASN B 1 86 ? 35.39917 -25.12766 32.47060 1.000 19.93198  ?  85  ASN B CA  1 
ATOM   1354 C C   . ASN B 1 86 ? 34.48807 -26.22904 31.94160 1.000 27.76818  ?  85  ASN B C   1 
ATOM   1355 O O   . ASN B 1 86 ? 33.33839 -25.98381 31.56538 1.000 19.89618  ?  85  ASN B O   1 
ATOM   1356 C CB  . ASN B 1 86 ? 35.37434 -25.11965 34.00473 1.000 29.36710  ?  85  ASN B CB  1 
ATOM   1357 C CG  . ASN B 1 86 ? 34.22114 -24.30989 34.56302 1.000 47.80267  ?  85  ASN B CG  1 
ATOM   1358 O OD1 . ASN B 1 86 ? 33.06275 -24.69709 34.42351 1.000 60.81296  ?  85  ASN B OD1 1 
ATOM   1359 N ND2 . ASN B 1 86 ? 34.53154 -23.18126 35.20374 1.000 39.17271  ?  85  ASN B ND2 1 
ATOM   1360 N N   . ILE B 1 87 ? 35.02204 -27.44916 31.91381 1.000 19.32769  ?  86  ILE B N   1 
ATOM   1361 C CA  . ILE B 1 87 ? 34.21512 -28.63683 31.66258 1.000 20.27190  ?  86  ILE B CA  1 
ATOM   1362 C C   . ILE B 1 87 ? 33.48796 -29.03808 32.93915 1.000 25.47142  ?  86  ILE B C   1 
ATOM   1363 O O   . ILE B 1 87 ? 34.06386 -29.03392 34.03128 1.000 30.95792  ?  86  ILE B O   1 
ATOM   1364 C CB  . ILE B 1 87 ? 35.09963 -29.77304 31.12723 1.000 23.52488  ?  86  ILE B CB  1 
ATOM   1365 C CG1 . ILE B 1 87 ? 35.74372 -29.33866 29.81742 1.000 21.40435  ?  86  ILE B CG1 1 
ATOM   1366 C CG2 . ILE B 1 87 ? 34.28623 -31.03152 30.91823 1.000 33.36554  ?  86  ILE B CG2 1 
ATOM   1367 C CD1 . ILE B 1 87 ? 36.77813 -30.32440 29.28084 1.000 31.00504  ?  86  ILE B CD1 1 
ATOM   1368 N N   . VAL B 1 88 ? 32.20220 -29.35660 32.80372 1.000 22.07605  ?  87  VAL B N   1 
ATOM   1369 C CA  . VAL B 1 88 ? 31.33593 -29.75462 33.90749 1.000 29.59584  ?  87  VAL B CA  1 
ATOM   1370 C C   . VAL B 1 88 ? 31.12054 -31.25742 33.84021 1.000 25.81863  ?  87  VAL B C   1 
ATOM   1371 O O   . VAL B 1 88 ? 30.89843 -31.81067 32.76197 1.000 29.10352  ?  87  VAL B O   1 
ATOM   1372 C CB  . VAL B 1 88 ? 29.98777 -29.00475 33.83869 1.000 23.39935  ?  87  VAL B CB  1 
ATOM   1373 C CG1 . VAL B 1 88 ? 29.04806 -29.45475 34.95438 1.000 36.57425  ?  87  VAL B CG1 1 
ATOM   1374 C CG2 . VAL B 1 88 ? 30.21310 -27.51695 33.90350 1.000 29.19180  ?  87  VAL B CG2 1 
ATOM   1375 N N   . GLU B 1 89 ? 31.13563 -31.91608 34.99457 1.000 38.39150  ?  88  GLU B N   1 
ATOM   1376 C CA  . GLU B 1 89 ? 30.86755 -33.35302 35.06055 1.000 44.91737  ?  88  GLU B CA  1 
ATOM   1377 C C   . GLU B 1 89 ? 29.37841 -33.65213 34.96333 1.000 47.77372  ?  88  GLU B C   1 
ATOM   1378 O O   . GLU B 1 89 ? 28.98494 -34.72187 34.49106 1.000 61.32980  ?  88  GLU B O   1 
ATOM   1379 C CB  . GLU B 1 89 ? 31.43664 -33.94485 36.34950 1.000 50.18807  ?  88  GLU B CB  1 
ATOM   1380 C CG  . GLU B 1 89 ? 32.94084 -33.97783 36.35107 1.000 67.29698  ?  88  GLU B CG  1 
ATOM   1381 C CD  . GLU B 1 89 ? 33.48626 -34.54329 35.05320 1.000 80.67101  ?  88  GLU B CD  1 
ATOM   1382 O OE1 . GLU B 1 89 ? 33.43986 -35.78044 34.88210 1.000 98.91592  ?  88  GLU B OE1 1 
ATOM   1383 O OE2 . GLU B 1 89 ? 33.93558 -33.75035 34.19433 1.000 66.39514  -1 88  GLU B OE2 1 
HETATM 1384 C C01 A Y65 C 2 .  ? 23.48736 -11.08094 28.74362 0.490 16.36865  ?  101 Y65 B C01 1 
HETATM 1385 C C01 B Y65 C 2 .  ? 22.71841 -16.23344 28.35077 0.510 16.25678  ?  101 Y65 B C01 1 
HETATM 1386 C C02 A Y65 C 2 .  ? 22.52033 -11.95268 28.69358 0.490 19.60703  ?  101 Y65 B C02 1 
HETATM 1387 C C02 B Y65 C 2 .  ? 23.72550 -15.40039 28.46876 0.510 17.02032  ?  101 Y65 B C02 1 
HETATM 1388 C C03 A Y65 C 2 .  ? 21.31366 -11.14450 29.10458 0.490 17.08736  ?  101 Y65 B C03 1 
HETATM 1389 C C03 B Y65 C 2 .  ? 24.90107 -16.27748 28.86194 0.510 12.93819  ?  101 Y65 B C03 1 
HETATM 1390 C C04 A Y65 C 2 .  ? 21.88741 -10.16546 30.19890 0.490 19.43741  ?  101 Y65 B C04 1 
HETATM 1391 C C04 B Y65 C 2 .  ? 24.24775 -17.37145 29.77312 0.510 16.11085  ?  101 Y65 B C04 1 
HETATM 1392 C C16 A Y65 C 2 .  ? 25.24121 -16.19049 30.92152 0.490 17.01542  ?  101 Y65 B C16 1 
HETATM 1393 C C16 B Y65 C 2 .  ? 20.94466 -10.65568 30.79255 0.510 19.31831  ?  101 Y65 B C16 1 
HETATM 1394 C C18 A Y65 C 2 .  ? 24.58344 -15.71300 28.64024 0.490 15.62933  ?  101 Y65 B C18 1 
HETATM 1395 C C18 B Y65 C 2 .  ? 21.58611 -11.24413 28.52933 0.510 16.69405  ?  101 Y65 B C18 1 
HETATM 1396 O O05 A Y65 C 2 .  ? 23.15828 -10.25412 30.11140 0.490 17.00493  ?  101 Y65 B O05 1 
HETATM 1397 O O05 B Y65 C 2 .  ? 22.99469 -17.34700 29.49987 0.510 15.10578  ?  101 Y65 B O05 1 
HETATM 1398 O O21 A Y65 C 2 .  ? 23.77707 -17.73630 29.76518 0.490 20.32549  ?  101 Y65 B O21 1 
HETATM 1399 O O21 B Y65 C 2 .  ? 22.52759 -9.26839  29.61215 0.510 19.10615  ?  101 Y65 B O21 1 
HETATM 1400 C C06 A Y65 C 2 .  ? 21.44484 -10.74503 31.59057 0.490 18.42031  ?  101 Y65 B C06 1 
HETATM 1401 C C06 B Y65 C 2 .  ? 24.50044 -16.91904 31.26417 0.510 19.95010  ?  101 Y65 B C06 1 
HETATM 1402 C C17 A Y65 C 2 .  ? 24.98293 -16.82184 29.69689 0.490 13.61341  ?  101 Y65 B C17 1 
HETATM 1403 C C17 B Y65 C 2 .  ? 21.26050 -10.09012 29.55974 0.510 17.48877  ?  101 Y65 B C17 1 
HETATM 1404 C C19 A Y65 C 2 .  ? 23.35241 -15.64346 28.73304 0.490 18.60958  ?  101 Y65 B C19 1 
HETATM 1405 C C19 B Y65 C 2 .  ? 22.81021 -11.42078 28.66976 0.510 21.65202  ?  101 Y65 B C19 1 
HETATM 1406 C C20 A Y65 C 2 .  ? 22.90266 -17.22022 28.97555 0.490 12.35904  ?  101 Y65 B C20 1 
HETATM 1407 C C20 B Y65 C 2 .  ? 23.39554 -9.89478  28.91947 0.510 14.07411  ?  101 Y65 B C20 1 
HETATM 1408 C C23 A Y65 C 2 .  ? 21.27456 -17.41186 30.85123 0.490 14.66131  ?  101 Y65 B C23 1 
HETATM 1409 C C23 B Y65 C 2 .  ? 24.78779 -10.03656 30.99101 0.510 16.50416  ?  101 Y65 B C23 1 
HETATM 1410 C C25 A Y65 C 2 .  ? 19.42413 -17.82005 29.75643 0.490 18.62508  ?  101 Y65 B C25 1 
HETATM 1411 C C25 B Y65 C 2 .  ? 26.76730 -9.71002  30.16811 0.510 15.27665  ?  101 Y65 B C25 1 
HETATM 1412 C C26 A Y65 C 2 .  ? 18.12978 -18.08139 29.26355 0.490 24.53366  ?  101 Y65 B C26 1 
HETATM 1413 C C26 B Y65 C 2 .  ? 28.11156 -9.53426  29.83936 0.510 22.21103  ?  101 Y65 B C26 1 
HETATM 1414 C C28 A Y65 C 2 .  ? 18.98096 -18.03487 27.10134 0.490 27.19934  ?  101 Y65 B C28 1 
HETATM 1415 C C28 B Y65 C 2 .  ? 27.54518 -9.27975  27.60444 0.510 20.48439  ?  101 Y65 B C28 1 
HETATM 1416 C C30 A Y65 C 2 .  ? 20.45449 -17.66416 28.85325 0.490 24.33385  ?  101 Y65 B C30 1 
HETATM 1417 C C30 B Y65 C 2 .  ? 25.85293 -9.68043  29.13565 0.510 18.09162  ?  101 Y65 B C30 1 
HETATM 1418 C C37 A Y65 C 2 .  ? 25.79004 -11.55162 27.94198 0.490 17.67568  ?  101 Y65 B C37 1 
HETATM 1419 C C37 B Y65 C 2 .  ? 20.36277 -15.69327 27.81767 0.510 20.99763  ?  101 Y65 B C37 1 
HETATM 1420 C C39 A Y65 C 2 .  ? 26.58337 -12.80542 29.48469 0.490 15.46494  ?  101 Y65 B C39 1 
HETATM 1421 C C39 B Y65 C 2 .  ? 19.71084 -14.52892 29.48801 0.510 15.96532  ?  101 Y65 B C39 1 
HETATM 1422 C C40 A Y65 C 2 .  ? 25.26642 -12.45977 29.80261 0.490 17.89760  ?  101 Y65 B C40 1 
HETATM 1423 C C40 B Y65 C 2 .  ? 21.04429 -14.90278 29.66477 0.510 21.19958  ?  101 Y65 B C40 1 
HETATM 1424 C C41 A Y65 C 2 .  ? 27.53661 -13.69201 30.30157 0.490 13.28164  ?  101 Y65 B C41 1 
HETATM 1425 C C41 B Y65 C 2 .  ? 18.82599 -13.67532 30.43248 0.510 20.44593  ?  101 Y65 B C41 1 
HETATM 1426 C C42 A Y65 C 2 .  ? 28.08248 -12.96779 31.52864 0.490 15.27361  ?  101 Y65 B C42 1 
HETATM 1427 C C42 B Y65 C 2 .  ? 18.12818 -14.45662 31.53813 0.510 17.28393  ?  101 Y65 B C42 1 
HETATM 1428 C C44 A Y65 C 2 .  ? 29.08038 -11.91806 31.06795 0.490 17.39772  ?  101 Y65 B C44 1 
HETATM 1429 C C44 B Y65 C 2 .  ? 17.15823 -15.48321 30.94399 0.510 25.14338  ?  101 Y65 B C44 1 
HETATM 1430 N N22 A Y65 C 2 .  ? 21.58049 -17.40684 29.55562 0.490 23.51016  ?  101 Y65 B N22 1 
HETATM 1431 N N22 B Y65 C 2 .  ? 24.63981 -9.88535  29.67791 0.510 23.21753  ?  101 Y65 B N22 1 
HETATM 1432 N N24 A Y65 C 2 .  ? 19.98307 -17.64651 30.97250 0.490 13.33848  ?  101 Y65 B N24 1 
HETATM 1433 N N24 B Y65 C 2 .  ? 26.06544 -9.93515  31.30612 0.510 9.78270   ?  101 Y65 B N24 1 
HETATM 1434 N N27 A Y65 C 2 .  ? 17.97029 -18.17338 27.94895 0.490 26.41543  ?  101 Y65 B N27 1 
HETATM 1435 N N27 B Y65 C 2 .  ? 28.44502 -9.31597  28.57370 0.510 23.00733  ?  101 Y65 B N27 1 
HETATM 1436 N N29 A Y65 C 2 .  ? 20.19902 -17.78383 27.53734 0.490 25.83866  ?  101 Y65 B N29 1 
HETATM 1437 N N29 B Y65 C 2 .  ? 26.26700 -9.46318  27.87164 0.510 14.16672  ?  101 Y65 B N29 1 
HETATM 1438 N N31 A Y65 C 2 .  ? 16.97358 -18.25100 30.15085 0.490 28.19519  ?  101 Y65 B N31 1 
HETATM 1439 N N31 B Y65 C 2 .  ? 29.11874 -9.58553  30.88520 0.510 21.26196  ?  101 Y65 B N31 1 
HETATM 1440 N N36 A Y65 C 2 .  ? 24.80738 -11.68997 28.82341 0.490 20.55145  ?  101 Y65 B N36 1 
HETATM 1441 N N36 B Y65 C 2 .  ? 21.41538 -15.62002 28.60615 0.510 21.76796  ?  101 Y65 B N36 1 
HETATM 1442 N N38 A Y65 C 2 .  ? 26.86571 -12.23058 28.33368 0.490 18.57104  ?  101 Y65 B N38 1 
HETATM 1443 N N38 B Y65 C 2 .  ? 19.33641 -15.02873 28.33092 0.510 19.56606  ?  101 Y65 B N38 1 
HETATM 1444 N N43 A Y65 C 2 .  ? 26.98720 -12.30932 32.21634 0.490 17.72267  ?  101 Y65 B N43 1 
HETATM 1445 N N43 B Y65 C 2 .  ? 19.12033 -15.14631 32.33268 0.510 23.00067  ?  101 Y65 B N43 1 
HETATM 1446 O O07 A Y65 C 2 .  ? 22.40052 -11.79154 31.82977 0.490 13.76236  ?  101 Y65 B O07 1 
HETATM 1447 O O07 B Y65 C 2 .  ? 23.73167 -15.70327 31.39532 0.510 8.64826   ?  101 Y65 B O07 1 
HETATM 1448 O O09 A Y65 C 2 .  ? 22.86863 -12.49504 34.34445 0.490 18.27296  -1 101 Y65 B O09 1 
HETATM 1449 O O09 B Y65 C 2 .  ? 23.28270 -14.94495 33.78091 0.510 12.84849  -1 101 Y65 B O09 1 
HETATM 1450 O O10 A Y65 C 2 .  ? 20.74317 -13.23095 33.34683 0.490 20.55494  -1 101 Y65 B O10 1 
HETATM 1451 O O10 B Y65 C 2 .  ? 25.47399 -14.26555 32.77051 0.510 20.41741  -1 101 Y65 B O10 1 
HETATM 1452 O O11 A Y65 C 2 .  ? 22.88825 -14.33304 32.46539 0.490 11.72951  ?  101 Y65 B O11 1 
HETATM 1453 O O11 B Y65 C 2 .  ? 23.24835 -13.17309 31.88718 0.510 14.72094  ?  101 Y65 B O11 1 
HETATM 1454 O O13 A Y65 C 2 .  ? 25.36458 -14.58548 33.31187 0.490 18.49920  -1 101 Y65 B O13 1 
HETATM 1455 O O13 B Y65 C 2 .  ? 20.73137 -12.80911 32.61627 0.510 20.04597  -1 101 Y65 B O13 1 
HETATM 1456 O O14 A Y65 C 2 .  ? 23.63666 -15.93670 34.41647 0.490 12.32848  -1 101 Y65 B O14 1 
HETATM 1457 O O14 B Y65 C 2 .  ? 22.55847 -11.81595 33.95319 0.510 17.01773  -1 101 Y65 B O14 1 
HETATM 1458 O O15 A Y65 C 2 .  ? 24.31875 -16.52309 31.95595 0.490 22.22743  ?  101 Y65 B O15 1 
HETATM 1459 O O15 B Y65 C 2 .  ? 22.06506 -10.80029 31.63761 0.510 22.51497  ?  101 Y65 B O15 1 
HETATM 1460 O O32 A Y65 C 2 .  ? 22.75899 -15.16193 27.46359 0.490 16.65028  ?  101 Y65 B O32 1 
HETATM 1461 O O32 B Y65 C 2 .  ? 23.46115 -12.00377 27.47602 0.510 24.23576  ?  101 Y65 B O32 1 
HETATM 1462 O O33 A Y65 C 2 .  ? 24.98892 -16.20558 27.26866 0.490 18.34853  ?  101 Y65 B O33 1 
HETATM 1463 O O33 B Y65 C 2 .  ? 21.22757 -10.65693 27.18852 0.510 22.32409  ?  101 Y65 B O33 1 
HETATM 1464 O O34 A Y65 C 2 .  ? 20.79530 -10.43921 28.05720 0.490 14.74548  ?  101 Y65 B O34 1 
HETATM 1465 O O34 B Y65 C 2 .  ? 25.54243 -16.88148 27.82313 0.510 12.76243  ?  101 Y65 B O34 1 
HETATM 1466 O O35 A Y65 C 2 .  ? 22.29728 -12.48357 27.28681 0.490 21.24982  ?  101 Y65 B O35 1 
HETATM 1467 O O35 B Y65 C 2 .  ? 24.02947 -14.56945 27.22517 0.510 13.56794  ?  101 Y65 B O35 1 
HETATM 1468 O O45 A Y65 C 2 .  ? 28.78015 -10.69701 31.06825 0.490 20.51159  -1 101 Y65 B O45 1 
HETATM 1469 O O45 B Y65 C 2 .  ? 17.44191 -16.70711 30.99029 0.510 22.40416  -1 101 Y65 B O45 1 
HETATM 1470 O O46 A Y65 C 2 .  ? 30.21351 -12.27149 30.67456 0.490 18.69490  ?  101 Y65 B O46 1 
HETATM 1471 O O46 B Y65 C 2 .  ? 16.07603 -15.11258 30.41136 0.510 16.06216  ?  101 Y65 B O46 1 
HETATM 1472 P P08 A Y65 C 2 .  ? 22.19300 -12.93822 33.07425 0.490 14.86621  ?  101 Y65 B P08 1 
HETATM 1473 P P08 B Y65 C 2 .  ? 24.00461 -14.49671 32.54085 0.510 11.98935  ?  101 Y65 B P08 1 
HETATM 1474 P P12 A Y65 C 2 .  ? 24.07233 -15.33021 33.09952 0.490 13.91283  ?  101 Y65 B P12 1 
HETATM 1475 P P12 B Y65 C 2 .  ? 22.08869 -12.17212 32.57079 0.510 15.43695  ?  101 Y65 B P12 1 
HETATM 1476 O O   . HOH D 3 .  ? 18.23296 -11.44463 20.23233 1.000 40.09491  ?  101 HOH A O   1 
HETATM 1477 O O   . HOH D 3 .  ? 6.78965  6.92473   21.74099 1.000 46.66558  ?  102 HOH A O   1 
HETATM 1478 O O   . HOH D 3 .  ? 37.94758 1.70452   11.08632 1.000 52.56573  ?  103 HOH A O   1 
HETATM 1479 O O   . HOH D 3 .  ? 37.366   0.502     12.471   1.000 47.73011  ?  104 HOH A O   1 
HETATM 1480 O O   . HOH D 3 .  ? 15.472   5.614     31.003   1.000 26.25538  ?  105 HOH A O   1 
HETATM 1481 O O   . HOH D 3 .  ? 8.510    -9.882    24.591   1.000 21.69382  ?  106 HOH A O   1 
HETATM 1482 O O   . HOH D 3 .  ? 7.82089  -8.52907  35.78621 1.000 53.63208  ?  107 HOH A O   1 
HETATM 1483 O O   . HOH D 3 .  ? 18.46917 8.24383   33.24439 1.000 48.03038  ?  108 HOH A O   1 
HETATM 1484 O O   . HOH D 3 .  ? 31.32042 -10.45538 37.65330 1.000 46.32297  ?  109 HOH A O   1 
HETATM 1485 O O   . HOH D 3 .  ? 27.120   -4.262    39.847   1.000 35.69260  ?  110 HOH A O   1 
HETATM 1486 O O   . HOH D 3 .  ? 13.32447 -4.01368  35.24399 1.000 44.52310  ?  111 HOH A O   1 
HETATM 1487 O O   . HOH D 3 .  ? 20.694   3.875     35.927   1.000 29.84108  ?  112 HOH A O   1 
HETATM 1488 O O   . HOH D 3 .  ? 22.161   -0.019    38.273   1.000 32.63916  ?  113 HOH A O   1 
HETATM 1489 O O   . HOH D 3 .  ? 18.305   3.967     24.588   1.000 20.66365  ?  114 HOH A O   1 
HETATM 1490 O O   . HOH D 3 .  ? 27.96098 7.13431   18.06978 1.000 37.22619  ?  115 HOH A O   1 
HETATM 1491 O O   . HOH D 3 .  ? 20.398   5.880     24.375   1.000 24.43245  ?  116 HOH A O   1 
HETATM 1492 O O   . HOH D 3 .  ? 15.95292 -12.76643 38.79012 1.000 35.42243  ?  117 HOH A O   1 
HETATM 1493 O O   . HOH D 3 .  ? 16.87590 -15.94451 34.70819 1.000 43.75710  ?  118 HOH A O   1 
HETATM 1494 O O   . HOH D 3 .  ? 14.12647 3.15754   37.42010 1.000 40.19790  ?  119 HOH A O   1 
HETATM 1495 O O   . HOH D 3 .  ? 18.66875 -1.63524  36.17136 1.000 39.16619  ?  120 HOH A O   1 
HETATM 1496 O O   . HOH D 3 .  ? 28.385   -0.278    14.851   1.000 24.36385  ?  121 HOH A O   1 
HETATM 1497 O O   . HOH D 3 .  ? 24.126   -5.450    5.289    1.000 37.37752  ?  122 HOH A O   1 
HETATM 1498 O O   . HOH D 3 .  ? 10.436   0.039     17.163   1.000 28.87667  ?  123 HOH A O   1 
HETATM 1499 O O   . HOH D 3 .  ? 25.605   -2.418    14.978   1.000 20.22244  ?  124 HOH A O   1 
HETATM 1500 O O   . HOH D 3 .  ? 25.48516 5.17145   10.66323 1.000 38.31689  ?  125 HOH A O   1 
HETATM 1501 O O   . HOH D 3 .  ? 8.241    -12.991   30.775   1.000 36.91379  ?  126 HOH A O   1 
HETATM 1502 O O   . HOH D 3 .  ? 31.846   2.267     33.451   1.000 39.24569  ?  127 HOH A O   1 
HETATM 1503 O O   . HOH D 3 .  ? 18.296   7.624     29.120   1.000 47.11753  ?  128 HOH A O   1 
HETATM 1504 O O   . HOH D 3 .  ? 11.323   -15.217   28.146   1.000 26.78252  ?  129 HOH A O   1 
HETATM 1505 O O   . HOH D 3 .  ? 23.67668 6.80507   23.29313 1.000 36.10768  ?  130 HOH A O   1 
HETATM 1506 O O   . HOH D 3 .  ? 18.03927 -4.88552  39.13226 1.000 38.03793  ?  131 HOH A O   1 
HETATM 1507 O O   . HOH D 3 .  ? 17.293   -6.328    36.300   1.000 35.09010  ?  132 HOH A O   1 
HETATM 1508 O O   . HOH D 3 .  ? 25.029   -3.839    38.543   1.000 30.00918  ?  133 HOH A O   1 
HETATM 1509 O O   . HOH D 3 .  ? 24.97132 -4.19590  19.86775 1.000 21.56857  ?  134 HOH A O   1 
HETATM 1510 O O   . HOH D 3 .  ? 19.639   -6.219    35.792   1.000 22.01278  ?  135 HOH A O   1 
HETATM 1511 O O   . HOH D 3 .  ? 4.56604  -10.35461 32.53207 1.000 45.24763  ?  136 HOH A O   1 
HETATM 1512 O O   . HOH D 3 .  ? 9.11395  5.08627   24.99336 1.000 42.52629  ?  137 HOH A O   1 
HETATM 1513 O O   . HOH D 3 .  ? 18.61469 6.97890   16.51432 1.000 50.20681  ?  138 HOH A O   1 
HETATM 1514 O O   . HOH D 3 .  ? 18.216   2.455     14.527   1.000 30.18321  ?  139 HOH A O   1 
HETATM 1515 O O   . HOH D 3 .  ? 26.91302 -8.72680  33.93134 1.000 25.93531  ?  140 HOH A O   1 
HETATM 1516 O O   . HOH D 3 .  ? 30.98609 -4.21421  39.97685 1.000 38.99314  ?  141 HOH A O   1 
HETATM 1517 O O   . HOH D 3 .  ? 8.824    -1.928    18.589   1.000 26.00789  ?  142 HOH A O   1 
HETATM 1518 O O   . HOH D 3 .  ? 22.539   -1.902    13.486   1.000 22.19034  ?  143 HOH A O   1 
HETATM 1519 O O   . HOH D 3 .  ? 7.72072  2.13252   25.28573 1.000 28.51034  ?  144 HOH A O   1 
HETATM 1520 O O   . HOH D 3 .  ? 29.42393 -9.65714  33.96521 1.000 29.84463  ?  145 HOH A O   1 
HETATM 1521 O O   . HOH D 3 .  ? 19.54129 -16.78966 22.53103 1.000 23.82892  ?  146 HOH A O   1 
HETATM 1522 O O   . HOH D 3 .  ? 29.349   2.432     24.152   1.000 40.31083  ?  147 HOH A O   1 
HETATM 1523 O O   . HOH D 3 .  ? 10.47300 -12.63819 35.73036 1.000 42.42444  ?  148 HOH A O   1 
HETATM 1524 O O   . HOH D 3 .  ? 27.242   -8.145    20.875   1.000 28.69935  ?  149 HOH A O   1 
HETATM 1525 O O   . HOH D 3 .  ? 26.123   -6.999    18.590   1.000 29.50477  ?  150 HOH A O   1 
HETATM 1526 O O   . HOH D 3 .  ? 30.994   0.502     22.773   1.000 38.22478  ?  151 HOH A O   1 
HETATM 1527 O O   . HOH D 3 .  ? 16.46616 5.97813   16.85776 1.000 31.11722  ?  152 HOH A O   1 
HETATM 1528 O O   . HOH D 3 .  ? 33.39308 -11.36890 34.28795 1.000 38.22040  ?  153 HOH A O   1 
HETATM 1529 O O   . HOH D 3 .  ? 31.396   0.070     21.275   1.000 32.71790  ?  154 HOH A O   1 
HETATM 1530 O O   . HOH D 3 .  ? 25.01300 -10.02722 24.52176 1.000 26.66248  ?  155 HOH A O   1 
HETATM 1531 O O   . HOH D 3 .  ? 17.670   8.783     20.207   1.000 41.36409  ?  156 HOH A O   1 
HETATM 1532 O O   . HOH D 3 .  ? 17.55440 -13.91143 40.63818 1.000 45.24168  ?  157 HOH A O   1 
HETATM 1533 O O   . HOH D 3 .  ? 21.104   7.626     26.335   1.000 42.10448  ?  158 HOH A O   1 
HETATM 1534 O O   . HOH D 3 .  ? 23.191   -13.437   23.120   1.000 32.01281  ?  159 HOH A O   1 
HETATM 1535 O O   . HOH D 3 .  ? 10.923   7.184     30.969   1.000 52.04562  ?  160 HOH A O   1 
HETATM 1536 O O   . HOH D 3 .  ? 8.11055  -17.05815 26.02633 1.000 48.80557  ?  161 HOH A O   1 
HETATM 1537 O O   . HOH D 3 .  ? 24.208   1.636     37.507   1.000 34.41299  ?  162 HOH A O   1 
HETATM 1538 O O   . HOH D 3 .  ? 23.255   -13.237   21.389   1.000 42.22213  ?  163 HOH A O   1 
HETATM 1539 O O   . HOH D 3 .  ? 10.003   -14.815   30.807   1.000 34.18128  ?  164 HOH A O   1 
HETATM 1540 O O   . HOH D 3 .  ? 17.018   7.952     30.956   1.000 36.19051  ?  165 HOH A O   1 
HETATM 1541 O O   . HOH D 3 .  ? 12.883   7.141     31.340   1.000 44.87028  ?  166 HOH A O   1 
HETATM 1542 O O   . HOH D 3 .  ? 21.597   6.558     28.183   1.000 35.36091  ?  167 HOH A O   1 
HETATM 1543 O O   . HOH D 3 .  ? 19.422   8.433     21.437   1.000 37.97374  ?  168 HOH A O   1 
HETATM 1544 O O   . HOH D 3 .  ? 7.314    -12.662   33.698   1.000 43.35266  ?  169 HOH A O   1 
HETATM 1545 O O   . HOH D 3 .  ? 10.87916 -17.94198 27.17528 1.000 33.03292  ?  170 HOH A O   1 
HETATM 1546 O O   . HOH D 3 .  ? 20.384   8.926     23.354   1.000 56.03401  ?  171 HOH A O   1 
HETATM 1547 O O   . HOH D 3 .  ? 24.318   7.871     25.681   1.000 57.56684  ?  172 HOH A O   1 
HETATM 1548 O O   . HOH D 3 .  ? 23.664   6.944     27.454   1.000 49.06837  ?  173 HOH A O   1 
HETATM 1549 O O   . HOH E 3 .  ? 36.34939 -35.04042 24.39802 1.000 48.51244  ?  201 HOH B O   1 
HETATM 1550 O O   . HOH E 3 .  ? 5.50359  -35.62142 7.04880  1.000 55.57858  ?  202 HOH B O   1 
HETATM 1551 O O   . HOH E 3 .  ? 15.414   -38.035   4.317    1.000 49.74631  ?  203 HOH B O   1 
HETATM 1552 O O   . HOH E 3 .  ? 22.83721 -11.45722 25.26622 1.000 22.83552  ?  204 HOH B O   1 
HETATM 1553 O O   . HOH E 3 .  ? 36.87793 -22.73988 35.35535 1.000 52.76530  ?  205 HOH B O   1 
HETATM 1554 O O   . HOH E 3 .  ? 28.85426 -11.71156 35.51080 1.000 36.90233  ?  206 HOH B O   1 
HETATM 1555 O O   . HOH E 3 .  ? 2.19733  -24.05243 5.71473  1.000 38.65100  ?  207 HOH B O   1 
HETATM 1556 O O   . HOH E 3 .  ? 32.25587 -11.59475 31.61419 1.000 33.38020  ?  208 HOH B O   1 
HETATM 1557 O O   . HOH E 3 .  ? 26.48391 -32.76938 14.21633 1.000 46.20748  ?  209 HOH B O   1 
HETATM 1558 O O   . HOH E 3 .  ? 2.607    -34.618   0.000    1.000 48.32973  ?  210 HOH B O   1 
HETATM 1559 O O   . HOH E 3 .  ? 23.54025 -15.82459 25.03938 1.000 23.39593  ?  211 HOH B O   1 
HETATM 1560 O O   . HOH E 3 .  ? 9.14516  -26.91044 11.85420 1.000 34.56191  ?  212 HOH B O   1 
HETATM 1561 O O   . HOH E 3 .  ? 30.84959 -33.02594 30.58005 1.000 20.04256  ?  213 HOH B O   1 
HETATM 1562 O O   . HOH E 3 .  ? 40.35256 -13.43613 25.75747 1.000 41.39387  ?  214 HOH B O   1 
HETATM 1563 O O   . HOH E 3 .  ? 35.39421 -15.23496 35.67113 1.000 32.53446  ?  215 HOH B O   1 
HETATM 1564 O O   . HOH E 3 .  ? 19.16736 -34.02718 17.48336 1.000 34.89451  ?  216 HOH B O   1 
HETATM 1565 O O   . HOH E 3 .  ? 21.38535 -23.77133 38.45315 1.000 32.63182  ?  217 HOH B O   1 
HETATM 1566 O O   . HOH E 3 .  ? 40.02963 -33.35330 21.94649 1.000 24.99507  ?  218 HOH B O   1 
HETATM 1567 O O   . HOH E 3 .  ? -1.49962 -24.66793 4.07121  1.000 43.61139  ?  219 HOH B O   1 
HETATM 1568 O O   . HOH E 3 .  ? 32.05631 -22.40715 35.59967 1.000 41.83205  ?  220 HOH B O   1 
HETATM 1569 O O   . HOH E 3 .  ? 6.27694  -36.37504 5.30543  1.000 56.50478  ?  221 HOH B O   1 
HETATM 1570 O O   . HOH E 3 .  ? 37.82272 -17.10257 24.62247 1.000 17.79560  ?  222 HOH B O   1 
HETATM 1571 O O   . HOH E 3 .  ? 43.48998 -17.90790 24.99503 1.000 28.95709  ?  223 HOH B O   1 
HETATM 1572 O O   . HOH E 3 .  ? 13.67423 -15.95581 31.15450 1.000 34.46386  ?  224 HOH B O   1 
HETATM 1573 O O   . HOH E 3 .  ? 38.52151 -28.91683 25.20124 1.000 22.32877  ?  225 HOH B O   1 
HETATM 1574 O O   . HOH E 3 .  ? 17.44926 -30.10581 34.38912 1.000 44.85222  ?  226 HOH B O   1 
HETATM 1575 O O   . HOH E 3 .  ? 37.95681 -14.34500 31.10096 1.000 32.38517  ?  227 HOH B O   1 
HETATM 1576 O O   . HOH E 3 .  ? 28.16915 -31.11798 24.25157 1.000 14.97059  ?  228 HOH B O   1 
HETATM 1577 O O   . HOH E 3 .  ? 8.06162  -22.50821 2.15540  1.000 39.43571  ?  229 HOH B O   1 
HETATM 1578 O O   . HOH E 3 .  ? 39.40764 -12.05958 27.61218 1.000 41.05384  ?  230 HOH B O   1 
HETATM 1579 O O   . HOH E 3 .  ? 10.41576 -26.65545 13.53709 1.000 36.41675  ?  231 HOH B O   1 
HETATM 1580 O O   . HOH E 3 .  ? 26.13746 -32.88863 24.09686 1.000 21.08435  ?  232 HOH B O   1 
HETATM 1581 O O   . HOH E 3 .  ? 33.164   -37.751   22.339   1.000 25.20438  ?  233 HOH B O   1 
HETATM 1582 O O   . HOH E 3 .  ? 15.46237 -36.31095 15.49196 1.000 48.37838  ?  234 HOH B O   1 
HETATM 1583 O O   . HOH E 3 .  ? 18.45733 -26.21715 14.45022 1.000 21.51996  ?  235 HOH B O   1 
HETATM 1584 O O   . HOH E 3 .  ? 24.55657 -33.22535 13.44832 1.000 41.08319  ?  236 HOH B O   1 
HETATM 1585 O O   . HOH E 3 .  ? 28.54154 -28.95344 14.40786 1.000 27.55028  ?  237 HOH B O   1 
HETATM 1586 O O   . HOH E 3 .  ? 21.10051 -24.22617 14.63175 1.000 21.25102  ?  238 HOH B O   1 
HETATM 1587 O O   . HOH E 3 .  ? 37.49761 -31.71969 25.25321 1.000 26.29111  ?  239 HOH B O   1 
HETATM 1588 O O   . HOH E 3 .  ? 22.73953 -33.72819 23.11092 1.000 25.17328  ?  240 HOH B O   1 
HETATM 1589 O O   . HOH E 3 .  ? 34.72979 -11.77993 28.61850 1.000 23.26363  ?  241 HOH B O   1 
HETATM 1590 O O   . HOH E 3 .  ? 29.63833 -14.03998 39.23197 1.000 41.61429  ?  242 HOH B O   1 
HETATM 1591 O O   . HOH E 3 .  ? 18.01141 -31.10655 24.71746 1.000 36.20240  ?  243 HOH B O   1 
HETATM 1592 O O   . HOH E 3 .  ? 21.56875 -22.91183 19.58421 1.000 18.87162  ?  244 HOH B O   1 
HETATM 1593 O O   . HOH E 3 .  ? 29.19807 -9.29463  25.15460 1.000 39.59523  ?  245 HOH B O   1 
HETATM 1594 O O   . HOH E 3 .  ? 28.30739 -22.89705 38.41404 1.000 39.28229  ?  246 HOH B O   1 
HETATM 1595 O O   . HOH E 3 .  ? 2.83766  -29.99326 0.54494  1.000 37.07349  ?  247 HOH B O   1 
HETATM 1596 O O   . HOH E 3 .  ? 28.88927 -21.02821 36.62942 1.000 37.20861  ?  248 HOH B O   1 
HETATM 1597 O O   . HOH E 3 .  ? 26.74106 -21.46438 35.91974 1.000 20.54249  ?  249 HOH B O   1 
HETATM 1598 O O   . HOH E 3 .  ? 21.71240 -31.30539 9.99655  1.000 32.56831  ?  250 HOH B O   1 
HETATM 1599 O O   . HOH E 3 .  ? 28.04239 -25.37756 36.51122 1.000 38.27750  ?  251 HOH B O   1 
HETATM 1600 O O   . HOH E 3 .  ? 19.33721 -18.65425 33.70210 1.000 23.70632  ?  252 HOH B O   1 
HETATM 1601 O O   . HOH E 3 .  ? 24.12887 -24.75679 13.12091 1.000 25.41952  ?  253 HOH B O   1 
HETATM 1602 O O   . HOH E 3 .  ? 37.70085 -24.76238 18.51561 1.000 16.72343  ?  254 HOH B O   1 
HETATM 1603 O O   . HOH E 3 .  ? 36.07085 -26.58995 17.33106 1.000 18.51091  ?  255 HOH B O   1 
HETATM 1604 O O   . HOH E 3 .  ? 16.76630 -28.99378 23.44431 1.000 40.24494  ?  256 HOH B O   1 
HETATM 1605 O O   . HOH E 3 .  ? 22.16077 -18.50670 40.50599 1.000 31.12660  ?  257 HOH B O   1 
HETATM 1606 O O   . HOH E 3 .  ? 42.70892 -22.27581 27.12709 1.000 27.34428  ?  258 HOH B O   1 
HETATM 1607 O O   . HOH E 3 .  ? 12.14350 -27.32125 4.40844  1.000 46.06409  ?  259 HOH B O   1 
HETATM 1608 O O   . HOH E 3 .  ? 26.66360 -10.52524 22.46278 1.000 26.32173  ?  260 HOH B O   1 
HETATM 1609 O O   . HOH E 3 .  ? -3.317   -26.719   0.602    1.000 45.54079  ?  261 HOH B O   1 
HETATM 1610 O O   . HOH E 3 .  ? -2.92033 -32.36336 8.79579  1.000 38.61693  ?  262 HOH B O   1 
HETATM 1611 O O   . HOH E 3 .  ? 28.97590 -34.65865 29.64724 1.000 41.22570  ?  263 HOH B O   1 
HETATM 1612 O O   . HOH E 3 .  ? 21.40842 -17.17838 24.58647 1.000 24.99506  ?  264 HOH B O   1 
HETATM 1613 O O   . HOH E 3 .  ? 40.502   -25.601   17.591   1.000 42.90903  ?  265 HOH B O   1 
HETATM 1614 O O   . HOH E 3 .  ? 15.09263 -27.15248 20.48130 1.000 28.38085  ?  266 HOH B O   1 
HETATM 1615 O O   . HOH E 3 .  ? -3.00297 -30.06084 8.58790  1.000 43.48189  ?  267 HOH B O   1 
HETATM 1616 O O   . HOH E 3 .  ? 27.66378 -34.40335 16.08535 1.000 43.86967  ?  268 HOH B O   1 
HETATM 1617 O O   . HOH E 3 .  ? 13.04839 -16.21113 33.91836 1.000 48.66123  ?  269 HOH B O   1 
HETATM 1618 O O   . HOH E 3 .  ? 24.04976 -35.74900 13.14116 1.000 38.68398  ?  270 HOH B O   1 
HETATM 1619 O O   . HOH E 3 .  ? 28.50337 -35.22743 20.13952 1.000 32.55984  ?  271 HOH B O   1 
HETATM 1620 O O   . HOH E 3 .  ? 14.89071 -27.45339 22.26183 1.000 39.63829  ?  272 HOH B O   1 
HETATM 1621 O O   . HOH E 3 .  ? 29.63611 -36.40533 19.51975 0.50  35.24838  ?  273 HOH B O   1 
HETATM 1622 O O   . HOH E 3 .  ? 28.709   -37.637   23.090   1.000 51.95878  ?  274 HOH B O   1 
HETATM 1623 O O   . HOH E 3 .  ? 7.32305  -26.32087 12.51060 1.000 47.16817  ?  275 HOH B O   1 
HETATM 1624 O O   . HOH E 3 .  ? 40.31082 -29.36547 30.38189 1.000 43.24333  ?  276 HOH B O   1 
HETATM 1625 O O   . HOH E 3 .  ? 38.234   -9.891    27.214   1.000 36.62254  ?  277 HOH B O   1 
HETATM 1626 O O   . HOH E 3 .  ? 31.07363 -30.79338 15.17702 1.000 37.24526  ?  278 HOH B O   1 
HETATM 1627 O O   . HOH E 3 .  ? 41.10826 -23.73387 19.51975 0.50  33.87123  ?  279 HOH B O   1 
HETATM 1628 O O   . HOH E 3 .  ? 24.95447 -27.44355 9.36529  1.000 33.52751  ?  280 HOH B O   1 
HETATM 1629 O O   . HOH E 3 .  ? 39.16886 -14.58134 33.60990 1.000 38.34622  ?  281 HOH B O   1 
HETATM 1630 O O   . HOH E 3 .  ? 26.91450 -35.24451 21.23729 1.000 33.38517  ?  282 HOH B O   1 
HETATM 1631 O O   . HOH E 3 .  ? 35.583   -9.542    27.136   1.000 28.35424  ?  283 HOH B O   1 
HETATM 1632 O O   . HOH E 3 .  ? 40.17111 -11.95594 30.32176 1.000 47.49108  ?  284 HOH B O   1 
HETATM 1633 O O   . HOH E 3 .  ? 40.16333 -29.26018 27.30918 1.000 42.46782  ?  285 HOH B O   1 
HETATM 1634 O O   . HOH E 3 .  ? 24.34410 -36.50246 21.43779 1.000 48.37026  ?  286 HOH B O   1 
HETATM 1635 O O   . HOH E 3 .  ? 18.83306 -35.37590 20.03662 1.000 46.83062  ?  287 HOH B O   1 
HETATM 1636 O O   . HOH E 3 .  ? 22.37935 -37.25501 21.46229 1.000 47.28322  ?  288 HOH B O   1 
HETATM 1637 O O   . HOH E 3 .  ? 42.53109 -28.32190 27.64585 1.000 37.94371  ?  289 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 4  ? 0.40435 0.51918 0.75173 0.03063  -0.02865 -0.22827 3  SER A N   
2    C CA  . SER A 4  ? 0.35718 0.47132 0.70067 0.03000  -0.02989 -0.22576 3  SER A CA  
3    C C   . SER A 4  ? 0.37033 0.48718 0.71845 0.03116  -0.03421 -0.22610 3  SER A C   
4    O O   . SER A 4  ? 0.42655 0.54765 0.78131 0.03066  -0.03427 -0.22873 3  SER A O   
5    C CB  . SER A 4  ? 0.48231 0.59702 0.82382 0.02747  -0.02563 -0.22582 3  SER A CB  
6    O OG  . SER A 4  ? 0.57203 0.69076 0.92049 0.02617  -0.02328 -0.22906 3  SER A OG  
7    N N   . LEU A 5  ? 0.28287 0.39708 0.62715 0.03262  -0.03773 -0.22356 4  LEU A N   
8    C CA  . LEU A 5  ? 0.26053 0.37583 0.60769 0.03437  -0.04234 -0.22348 4  LEU A CA  
9    C C   . LEU A 5  ? 0.24037 0.35711 0.58658 0.03327  -0.04330 -0.22192 4  LEU A C   
10   O O   . LEU A 5  ? 0.20835 0.32399 0.54979 0.03167  -0.04103 -0.22006 4  LEU A O   
11   C CB  . LEU A 5  ? 0.29054 0.40114 0.63345 0.03677  -0.04535 -0.22157 4  LEU A CB  
12   C CG  . LEU A 5  ? 0.29375 0.40163 0.63510 0.03749  -0.04357 -0.22222 4  LEU A CG  
13   C CD1 . LEU A 5  ? 0.32404 0.42636 0.65978 0.03930  -0.04566 -0.22002 4  LEU A CD1 
14   C CD2 . LEU A 5  ? 0.31416 0.42486 0.66212 0.03873  -0.04394 -0.22556 4  LEU A CD2 
15   N N   . ASN A 6  ? 0.19949 0.31847 0.54985 0.03436  -0.04690 -0.22275 5  ASN A N   
16   C CA  . ASN A 6  ? 0.22234 0.34203 0.57140 0.03393  -0.04882 -0.22088 5  ASN A CA  
17   C C   . ASN A 6  ? 0.18571 0.30087 0.52879 0.03563  -0.05170 -0.21763 5  ASN A C   
18   O O   . ASN A 6  ? 0.18832 0.29969 0.52843 0.03704  -0.05209 -0.21704 5  ASN A O   
19   C CB  . ASN A 6  ? 0.23546 0.35927 0.59111 0.03421  -0.05141 -0.22334 5  ASN A CB  
20   C CG  . ASN A 6  ? 0.27565 0.39839 0.63330 0.03723  -0.05564 -0.22462 5  ASN A CG  
21   O OD1 . ASN A 6  ? 0.24856 0.36687 0.60172 0.03941  -0.05796 -0.22245 5  ASN A OD1 
22   N ND2 . ASN A 6  ? 0.22844 0.35493 0.59239 0.03747  -0.05655 -0.22832 5  ASN A ND2 
23   N N   . PHE A 7  ? 0.24684 0.36223 0.58795 0.03539  -0.05342 -0.21553 6  PHE A N   
24   C CA  . PHE A 7  ? 0.20393 0.31500 0.53909 0.03661  -0.05551 -0.21248 6  PHE A CA  
25   C C   . PHE A 7  ? 0.19124 0.29950 0.52691 0.03938  -0.05943 -0.21266 6  PHE A C   
26   O O   . PHE A 7  ? 0.24341 0.34664 0.57381 0.04049  -0.06019 -0.21078 6  PHE A O   
27   C CB  . PHE A 7  ? 0.17689 0.28903 0.50987 0.03587  -0.05631 -0.21020 6  PHE A CB  
28   C CG  . PHE A 7  ? 0.17719 0.28494 0.50382 0.03682  -0.05796 -0.20717 6  PHE A CG  
29   C CD1 . PHE A 7  ? 0.17857 0.28311 0.49906 0.03600  -0.05565 -0.20582 6  PHE A CD1 
30   C CD2 . PHE A 7  ? 0.17671 0.28329 0.50330 0.03844  -0.06171 -0.20594 6  PHE A CD2 
31   C CE1 . PHE A 7  ? 0.17935 0.27980 0.49392 0.03646  -0.05678 -0.20341 6  PHE A CE1 
32   C CE2 . PHE A 7  ? 0.17764 0.27972 0.49811 0.03904  -0.06271 -0.20330 6  PHE A CE2 
33   C CZ  . PHE A 7  ? 0.18212 0.28118 0.49663 0.03788  -0.06011 -0.20211 6  PHE A CZ  
34   N N   . GLY A 8  ? 0.18573 0.29667 0.52700 0.04054  -0.06186 -0.21501 7  GLY A N   
35   C CA  . GLY A 8  ? 0.22669 0.33431 0.56743 0.04375  -0.06573 -0.21526 7  GLY A CA  
36   C C   . GLY A 8  ? 0.20247 0.30579 0.54059 0.04532  -0.06477 -0.21548 7  GLY A C   
37   O O   . GLY A 8  ? 0.19984 0.29735 0.53301 0.04747  -0.06659 -0.21380 7  GLY A O   
38   N N   . LYS A 9  ? 0.19849 0.30412 0.53946 0.04419  -0.06163 -0.21753 8  LYS A N   
39   C CA  . LYS A 9  ? 0.20144 0.30317 0.53993 0.04546  -0.06039 -0.21776 8  LYS A CA  
40   C C   . LYS A 9  ? 0.23008 0.32731 0.56167 0.04419  -0.05826 -0.21502 8  LYS A C   
41   O O   . LYS A 9  ? 0.21816 0.30982 0.54532 0.04571  -0.05859 -0.21412 8  LYS A O   
42   C CB  . LYS A 9  ? 0.20204 0.30770 0.54559 0.04446  -0.05750 -0.22077 8  LYS A CB  
43   C CG  . LYS A 9  ? 0.31475 0.42530 0.66555 0.04552  -0.05931 -0.22424 8  LYS A CG  
44   C CD  . LYS A 9  ? 0.48875 0.59646 0.83925 0.04971  -0.06316 -0.22510 8  LYS A CD  
45   C CE  . LYS A 9  ? 0.64327 0.74827 0.99268 0.05114  -0.06159 -0.22591 8  LYS A CE  
46   N NZ  . LYS A 9  ? 0.50790 0.61081 0.85755 0.05555  -0.06512 -0.22733 8  LYS A NZ  
47   N N   . ALA A 10 ? 0.20776 0.30705 0.53788 0.04145  -0.05597 -0.21382 9  ALA A N   
48   C CA  . ALA A 10 ? 0.19687 0.29228 0.52011 0.04031  -0.05431 -0.21145 9  ALA A CA  
49   C C   . ALA A 10 ? 0.19841 0.28904 0.51698 0.04160  -0.05706 -0.20919 9  ALA A C   
50   O O   . ALA A 10 ? 0.20224 0.28783 0.51520 0.04153  -0.05620 -0.20796 9  ALA A O   
51   C CB  . ALA A 10 ? 0.19210 0.29059 0.51404 0.03767  -0.05178 -0.21064 9  ALA A CB  
52   N N   . LEU A 11 ? 0.19673 0.28856 0.51734 0.04272  -0.06023 -0.20878 10 LEU A N   
53   C CA  . LEU A 11 ? 0.19897 0.28561 0.51477 0.04408  -0.06280 -0.20664 10 LEU A CA  
54   C C   . LEU A 11 ? 0.20662 0.28689 0.51968 0.04675  -0.06402 -0.20699 10 LEU A C   
55   O O   . LEU A 11 ? 0.21058 0.28438 0.51710 0.04679  -0.06354 -0.20534 10 LEU A O   
56   C CB  . LEU A 11 ? 0.19571 0.28518 0.51448 0.04486  -0.06601 -0.20630 10 LEU A CB  
57   C CG  . LEU A 11 ? 0.19813 0.28207 0.51168 0.04626  -0.06867 -0.20398 10 LEU A CG  
58   C CD1 . LEU A 11 ? 0.19720 0.27797 0.50421 0.04414  -0.06658 -0.20152 10 LEU A CD1 
59   C CD2 . LEU A 11 ? 0.27456 0.36197 0.59162 0.04707  -0.07194 -0.20386 10 LEU A CD2 
60   N N   . GLU A 12 ? 0.20938 0.29110 0.52693 0.04898  -0.06537 -0.20925 11 GLU A N   
61   C CA  . GLU A 12 ? 0.21738 0.29277 0.53176 0.05195  -0.06634 -0.20960 11 GLU A CA  
62   C C   . GLU A 12 ? 0.22035 0.29164 0.53029 0.05063  -0.06290 -0.20915 11 GLU A C   
63   O O   . GLU A 12 ? 0.27057 0.33413 0.57412 0.05176  -0.06292 -0.20794 11 GLU A O   
64   C CB  . GLU A 12 ? 0.21969 0.29836 0.53991 0.05451  -0.06797 -0.21247 11 GLU A CB  
65   C CG  . GLU A 12 ? 0.32382 0.40203 0.64488 0.05765  -0.07239 -0.21273 11 GLU A CG  
66   C CD  . GLU A 12 ? 0.77705 0.85838 1.10326 0.06055  -0.07420 -0.21588 11 GLU A CD  
67   O OE1 . GLU A 12 ? 0.57529 0.65798 0.90377 0.06033  -0.07192 -0.21763 11 GLU A OE1 
68   O OE2 . GLU A 12 ? 0.50699 0.58951 0.83484 0.06307  -0.07793 -0.21671 11 GLU A OE2 
69   N N   . ALA A 13 ? 0.21649 0.29242 0.52921 0.04814  -0.05976 -0.21015 12 ALA A N   
70   C CA  . ALA A 13 ? 0.21884 0.29153 0.52741 0.04667  -0.05649 -0.20985 12 ALA A CA  
71   C C   . ALA A 13 ? 0.25422 0.32213 0.55567 0.04504  -0.05574 -0.20748 12 ALA A C   
72   O O   . ALA A 13 ? 0.22493 0.28647 0.52097 0.04516  -0.05456 -0.20698 12 ALA A O   
73   C CB  . ALA A 13 ? 0.21435 0.29298 0.52659 0.04429  -0.05343 -0.21115 12 ALA A CB  
74   N N   . LEU A 14 ? 0.21386 0.28477 0.51512 0.04335  -0.05620 -0.20615 13 LEU A N   
75   C CA  . LEU A 14 ? 0.21418 0.28119 0.50897 0.04174  -0.05565 -0.20406 13 LEU A CA  
76   C C   . LEU A 14 ? 0.22125 0.27993 0.51082 0.04352  -0.05728 -0.20303 13 LEU A C   
77   O O   . LEU A 14 ? 0.22563 0.27846 0.50896 0.04235  -0.05551 -0.20228 13 LEU A O   
78   C CB  . LEU A 14 ? 0.20751 0.27915 0.50351 0.04048  -0.05666 -0.20282 13 LEU A CB  
79   C CG  . LEU A 14 ? 0.20171 0.27925 0.49904 0.03816  -0.05431 -0.20304 13 LEU A CG  
80   C CD1 . LEU A 14 ? 0.19579 0.27763 0.49492 0.03770  -0.05580 -0.20190 13 LEU A CD1 
81   C CD2 . LEU A 14 ? 0.20297 0.27802 0.49420 0.03614  -0.05180 -0.20232 13 LEU A CD2 
82   N N   . LYS A 15 ? 0.22300 0.28074 0.51457 0.04633  -0.06057 -0.20308 14 LYS A N   
83   C CA  . LYS A 15 ? 0.25677 0.30573 0.54231 0.04836  -0.06225 -0.20190 14 LYS A CA  
84   C C   . LYS A 15 ? 0.28264 0.32443 0.56418 0.04991  -0.06090 -0.20264 14 LYS A C   
85   O O   . LYS A 15 ? 0.27693 0.30956 0.55111 0.05067  -0.06084 -0.20150 14 LYS A O   
86   C CB  . LYS A 15 ? 0.23081 0.28069 0.51931 0.05153  -0.06635 -0.20199 14 LYS A CB  
87   C CG  . LYS A 15 ? 0.22376 0.27845 0.51441 0.05025  -0.06804 -0.20078 14 LYS A CG  
88   C CD  . LYS A 15 ? 0.22465 0.28035 0.51841 0.05357  -0.07220 -0.20126 14 LYS A CD  
89   C CE  . LYS A 15 ? 0.23479 0.29482 0.53049 0.05243  -0.07399 -0.20003 14 LYS A CE  
90   N NZ  . LYS A 15 ? 0.22851 0.29210 0.52927 0.05529  -0.07798 -0.20125 14 LYS A NZ  
91   N N   . GLU A 16 ? 0.23880 0.28413 0.52461 0.05031  -0.05958 -0.20454 15 GLU A N   
92   C CA  . GLU A 16 ? 0.24681 0.28606 0.52923 0.05161  -0.05796 -0.20534 15 GLU A CA  
93   C C   . GLU A 16 ? 0.42952 0.46737 0.70844 0.04824  -0.05403 -0.20523 15 GLU A C   
94   O O   . GLU A 16 ? 0.34988 0.38342 0.62640 0.04883  -0.05221 -0.20605 15 GLU A O   
95   C CB  . GLU A 16 ? 0.24640 0.29031 0.53534 0.05394  -0.05866 -0.20761 15 GLU A CB  
96   C CG  . GLU A 16 ? 0.24797 0.29282 0.53991 0.05773  -0.06268 -0.20819 15 GLU A CG  
97   C CD  . GLU A 16 ? 0.39474 0.44469 0.69326 0.05985  -0.06332 -0.21078 15 GLU A CD  
98   O OE1 . GLU A 16 ? 0.54658 0.59784 0.84644 0.05864  -0.06052 -0.21191 15 GLU A OE1 
99   O OE2 . GLU A 16 ? 0.37060 0.42332 0.67285 0.06269  -0.06663 -0.21182 15 GLU A OE2 
100  N N   . GLY A 17 ? 0.24159 0.28321 0.52015 0.04492  -0.05276 -0.20436 16 GLY A N   
101  C CA  . GLY A 17 ? 0.34468 0.38519 0.61944 0.04181  -0.04932 -0.20437 16 GLY A CA  
102  C C   . GLY A 17 ? 0.28671 0.33430 0.56582 0.04028  -0.04721 -0.20574 16 GLY A C   
103  O O   . GLY A 17 ? 0.33568 0.38236 0.61169 0.03813  -0.04445 -0.20608 16 GLY A O   
104  N N   . LYS A 18 ? 0.23054 0.28490 0.51637 0.04120  -0.04826 -0.20667 17 LYS A N   
105  C CA  . LYS A 18 ? 0.22652 0.28665 0.51553 0.03967  -0.04594 -0.20792 17 LYS A CA  
106  C C   . LYS A 18 ? 0.36179 0.42728 0.65082 0.03726  -0.04529 -0.20714 17 LYS A C   
107  O O   . LYS A 18 ? 0.21691 0.28292 0.50491 0.03690  -0.04693 -0.20571 17 LYS A O   
108  C CB  . LYS A 18 ? 0.23091 0.29515 0.52663 0.04152  -0.04671 -0.20960 17 LYS A CB  
109  C CG  . LYS A 18 ? 0.25331 0.31268 0.54901 0.04443  -0.04760 -0.21052 17 LYS A CG  
110  C CD  . LYS A 18 ? 0.36072 0.42471 0.66343 0.04661  -0.04943 -0.21218 17 LYS A CD  
111  C CE  . LYS A 18 ? 0.33920 0.39918 0.64199 0.04969  -0.05002 -0.21345 17 LYS A CE  
112  N NZ  . LYS A 18 ? 0.46655 0.53261 0.77689 0.05119  -0.05106 -0.21569 17 LYS A NZ  
113  N N   . LYS A 19 ? 0.21744 0.28656 0.50712 0.03581  -0.04284 -0.20809 18 LYS A N   
114  C CA  . LYS A 19 ? 0.21198 0.28592 0.50108 0.03398  -0.04192 -0.20764 18 LYS A CA  
115  C C   . LYS A 19 ? 0.23765 0.31687 0.53223 0.03434  -0.04194 -0.20852 18 LYS A C   
116  O O   . LYS A 19 ? 0.22231 0.30221 0.52063 0.03525  -0.04126 -0.21004 18 LYS A O   
117  C CB  . LYS A 19 ? 0.21309 0.28694 0.49834 0.03235  -0.03913 -0.20828 18 LYS A CB  
118  C CG  . LYS A 19 ? 0.25680 0.32559 0.53683 0.03153  -0.03846 -0.20794 18 LYS A CG  
119  C CD  . LYS A 19 ? 0.21805 0.28780 0.49476 0.02991  -0.03587 -0.20890 18 LYS A CD  
120  C CE  . LYS A 19 ? 0.29984 0.36939 0.57858 0.03057  -0.03415 -0.21049 18 LYS A CE  
121  N NZ  . LYS A 19 ? 0.35777 0.42731 0.63279 0.02915  -0.03176 -0.21153 18 LYS A NZ  
122  N N   . VAL A 20 ? 0.20341 0.28622 0.49828 0.03353  -0.04248 -0.20766 19 VAL A N   
123  C CA  . VAL A 20 ? 0.20030 0.28764 0.49987 0.03350  -0.04211 -0.20853 19 VAL A CA  
124  C C   . VAL A 20 ? 0.25328 0.34311 0.54959 0.03191  -0.04048 -0.20795 19 VAL A C   
125  O O   . VAL A 20 ? 0.21774 0.30685 0.50929 0.03122  -0.04087 -0.20658 19 VAL A O   
126  C CB  . VAL A 20 ? 0.19809 0.28710 0.50225 0.03467  -0.04497 -0.20825 19 VAL A CB  
127  C CG1 . VAL A 20 ? 0.20810 0.29452 0.51508 0.03675  -0.04678 -0.20910 19 VAL A CG1 
128  C CG2 . VAL A 20 ? 0.19544 0.28384 0.49636 0.03435  -0.04685 -0.20610 19 VAL A CG2 
129  N N   . SER A 21 ? 0.19639 0.28889 0.49493 0.03141  -0.03860 -0.20908 20 SER A N   
130  C CA  . SER A 21 ? 0.19424 0.28838 0.48923 0.03026  -0.03720 -0.20848 20 SER A CA  
131  C C   . SER A 21 ? 0.21885 0.31569 0.51819 0.02991  -0.03595 -0.20957 20 SER A C   
132  O O   . SER A 21 ? 0.21975 0.31778 0.52513 0.03045  -0.03605 -0.21106 20 SER A O   
133  C CB  . SER A 21 ? 0.20775 0.30041 0.49692 0.02956  -0.03474 -0.20883 20 SER A CB  
134  O OG  . SER A 21 ? 0.34851 0.44085 0.63976 0.02958  -0.03236 -0.21054 20 SER A OG  
135  N N   . ARG A 22 ? 0.19179 0.28942 0.48770 0.02900  -0.03467 -0.20897 21 ARG A N   
136  C CA  . ARG A 22 ? 0.19121 0.29081 0.49012 0.02828  -0.03288 -0.20993 21 ARG A CA  
137  C C   . ARG A 22 ? 0.21403 0.31182 0.50806 0.02743  -0.02900 -0.21065 21 ARG A C   
138  O O   . ARG A 22 ? 0.19614 0.29176 0.48279 0.02741  -0.02847 -0.20968 21 ARG A O   
139  C CB  . ARG A 22 ? 0.18755 0.28868 0.48584 0.02799  -0.03434 -0.20854 21 ARG A CB  
140  C CG  . ARG A 22 ? 0.20558 0.30916 0.51049 0.02876  -0.03747 -0.20847 21 ARG A CG  
141  C CD  . ARG A 22 ? 0.22082 0.32613 0.52527 0.02829  -0.03820 -0.20732 21 ARG A CD  
142  N NE  . ARG A 22 ? 0.18216 0.28828 0.48721 0.02698  -0.03484 -0.20863 21 ARG A NE  
143  C CZ  . ARG A 22 ? 0.22662 0.33204 0.52702 0.02613  -0.03340 -0.20771 21 ARG A CZ  
144  N NH1 . ARG A 22 ? 0.17954 0.28436 0.47517 0.02655  -0.03546 -0.20550 21 ARG A NH1 
145  N NH2 . ARG A 22 ? 0.20820 0.31311 0.50823 0.02486  -0.02960 -0.20907 21 ARG A NH2 
146  N N   . GLU A 23 ? 0.30636 0.34071 0.50657 -0.01189 0.05233  -0.19079 22 GLU A N   
147  C CA  . GLU A 23 ? 0.32406 0.34391 0.50885 -0.01396 0.06152  -0.18989 22 GLU A CA  
148  C C   . GLU A 23 ? 0.25677 0.26902 0.42832 -0.01641 0.06227  -0.18734 22 GLU A C   
149  O O   . GLU A 23 ? 0.34873 0.34458 0.49881 -0.01613 0.06488  -0.18423 22 GLU A O   
150  C CB  . GLU A 23 ? 0.41234 0.43585 0.61203 -0.01694 0.07207  -0.19548 22 GLU A CB  
151  C CG  . GLU A 23 ? 0.59008 0.61585 0.79774 -0.01394 0.07339  -0.19732 22 GLU A CG  
152  C CD  . GLU A 23 ? 0.78911 0.81797 1.01275 -0.01687 0.08498  -0.20278 22 GLU A CD  
153  O OE1 . GLU A 23 ? 0.93861 0.96391 1.16211 -0.02166 0.09363  -0.20452 22 GLU A OE1 
154  O OE2 . GLU A 23 ? 0.71560 0.75008 0.95234 -0.01443 0.08581  -0.20533 22 GLU A OE2 
155  N N   . GLY A 24 ? 0.25913 0.28143 0.44168 -0.01846 0.05952  -0.18870 23 GLY A N   
156  C CA  . GLY A 24 ? 0.25264 0.26742 0.42279 -0.02064 0.06052  -0.18634 23 GLY A CA  
157  C C   . GLY A 24 ? 0.25067 0.25877 0.40520 -0.01757 0.05261  -0.18071 23 GLY A C   
158  O O   . GLY A 24 ? 0.30938 0.31115 0.45414 -0.01886 0.05296  -0.17880 23 GLY A O   
159  N N   . TRP A 25 ? 0.24437 0.25361 0.39722 -0.01367 0.04583  -0.17833 24 TRP A N   
160  C CA  . TRP A 25 ? 0.24334 0.24650 0.38399 -0.01108 0.03919  -0.17373 24 TRP A CA  
161  C C   . TRP A 25 ? 0.26463 0.24969 0.38402 -0.01050 0.04127  -0.17148 24 TRP A C   
162  O O   . TRP A 25 ? 0.32634 0.30179 0.43715 -0.01038 0.04566  -0.17235 24 TRP A O   
163  C CB  . TRP A 25 ? 0.23561 0.24370 0.38045 -0.00769 0.03251  -0.17239 24 TRP A CB  
164  C CG  . TRP A 25 ? 0.22213 0.24403 0.38222 -0.00727 0.02794  -0.17329 24 TRP A CG  
165  C CD1 . TRP A 25 ? 0.21678 0.24580 0.38524 -0.00928 0.02801  -0.17477 24 TRP A CD1 
166  C CD2 . TRP A 25 ? 0.21495 0.24268 0.38123 -0.00455 0.02239  -0.17280 24 TRP A CD2 
167  N NE1 . TRP A 25 ? 0.20783 0.24558 0.38599 -0.00764 0.02245  -0.17518 24 TRP A NE1 
168  C CE2 . TRP A 25 ? 0.20652 0.24367 0.38356 -0.00477 0.01919  -0.17394 24 TRP A CE2 
169  C CE3 . TRP A 25 ? 0.21661 0.24090 0.37887 -0.00200 0.01979  -0.17159 24 TRP A CE3 
170  C CZ2 . TRP A 25 ? 0.20060 0.24281 0.38330 -0.00234 0.01369  -0.17371 24 TRP A CZ2 
171  C CZ3 . TRP A 25 ? 0.20932 0.24014 0.37890 0.00008  0.01466  -0.17146 24 TRP A CZ3 
172  C CH2 . TRP A 25 ? 0.20178 0.24100 0.38090 -0.00003 0.01174  -0.17241 24 TRP A CH2 
173  N N   . ASN A 26 ? 0.27169 0.25066 0.38166 -0.00973 0.03776  -0.16876 25 ASN A N   
174  C CA  . ASN A 26 ? 0.27772 0.23790 0.36660 -0.00862 0.03805  -0.16703 25 ASN A CA  
175  C C   . ASN A 26 ? 0.39391 0.34605 0.47399 -0.00530 0.03259  -0.16567 25 ASN A C   
176  O O   . ASN A 26 ? 0.35492 0.29099 0.41850 -0.00467 0.03466  -0.16586 25 ASN A O   
177  C CB  . ASN A 26 ? 0.27812 0.23474 0.36165 -0.00832 0.03531  -0.16512 25 ASN A CB  
178  C CG  . ASN A 26 ? 0.27851 0.23767 0.36506 -0.01200 0.04141  -0.16647 25 ASN A CG  
179  O OD1 . ASN A 26 ? 0.34613 0.30175 0.43080 -0.01490 0.04881  -0.16869 25 ASN A OD1 
180  N ND2 . ASN A 26 ? 0.29342 0.25832 0.38501 -0.01216 0.03886  -0.16541 25 ASN A ND2 
181  N N   . GLY A 27 ? 0.31791 0.27975 0.40791 -0.00334 0.02570  -0.16447 26 GLY A N   
182  C CA  . GLY A 27 ? 0.27737 0.23387 0.36237 -0.00088 0.02059  -0.16378 26 GLY A CA  
183  C C   . GLY A 27 ? 0.36852 0.32780 0.45734 -0.00103 0.02389  -0.16542 26 GLY A C   
184  O O   . GLY A 27 ? 0.30617 0.27815 0.40930 -0.00242 0.02759  -0.16719 26 GLY A O   
185  N N   . LYS A 28 ? 0.28674 0.23293 0.36233 0.00053  0.02219  -0.16521 27 LYS A N   
186  C CA  . LYS A 28 ? 0.35451 0.29950 0.43022 0.00083  0.02603  -0.16679 27 LYS A CA  
187  C C   . LYS A 28 ? 0.29131 0.24091 0.37217 0.00282  0.01949  -0.16605 27 LYS A C   
188  O O   . LYS A 28 ? 0.28370 0.23046 0.36142 0.00391  0.01217  -0.16445 27 LYS A O   
189  C CB  . LYS A 28 ? 0.37976 0.30263 0.43285 0.00100  0.03058  -0.16735 27 LYS A CB  
190  C CG  . LYS A 28 ? 0.44861 0.36381 0.49381 -0.00111 0.03815  -0.16821 27 LYS A CG  
191  C CD  . LYS A 28 ? 0.40276 0.33622 0.46923 -0.00384 0.04513  -0.17047 27 LYS A CD  
192  C CE  . LYS A 28 ? 0.45911 0.38690 0.52023 -0.00675 0.05228  -0.17134 27 LYS A CE  
193  N NZ  . LYS A 28 ? 0.53950 0.48618 0.62402 -0.01003 0.05802  -0.17425 27 LYS A NZ  
194  N N   . GLY A 29 ? 0.28016 0.23639 0.36946 0.00326  0.02232  -0.16758 28 GLY A N   
195  C CA  . GLY A 29 ? 0.27587 0.23477 0.36839 0.00511  0.01685  -0.16700 28 GLY A CA  
196  C C   . GLY A 29 ? 0.32944 0.30473 0.43873 0.00548  0.01140  -0.16610 28 GLY A C   
197  O O   . GLY A 29 ? 0.28458 0.26083 0.39537 0.00676  0.00634  -0.16531 28 GLY A O   
198  N N   . MET A 30 ? 0.24648 0.23312 0.36710 0.00424  0.01260  -0.16632 29 MET A N   
199  C CA  . MET A 30 ? 0.24270 0.24201 0.37633 0.00458  0.00819  -0.16548 29 MET A CA  
200  C C   . MET A 30 ? 0.26631 0.27607 0.41245 0.00512  0.00921  -0.16749 29 MET A C   
201  O O   . MET A 30 ? 0.27138 0.28234 0.42090 0.00470  0.01407  -0.17007 29 MET A O   
202  C CB  . MET A 30 ? 0.22689 0.23016 0.36353 0.00315  0.00854  -0.16469 29 MET A CB  
203  C CG  . MET A 30 ? 0.23465 0.22764 0.36018 0.00321  0.00666  -0.16310 29 MET A CG  
204  S SD  . MET A 30 ? 0.27331 0.27022 0.40229 0.00200  0.00735  -0.16222 29 MET A SD  
205  C CE  . MET A 30 ? 0.23247 0.23016 0.36121 -0.00050 0.01490  -0.16424 29 MET A CE  
206  N N   . PHE A 31 ? 0.21736 0.23394 0.37069 0.00614  0.00462  -0.16668 30 PHE A N   
207  C CA  . PHE A 31 ? 0.23812 0.26342 0.40254 0.00702  0.00420  -0.16882 30 PHE A CA  
208  C C   . PHE A 31 ? 0.28811 0.31844 0.45708 0.00734  -0.00009 -0.16745 30 PHE A C   
209  O O   . PHE A 31 ? 0.23237 0.25960 0.39710 0.00722  -0.00241 -0.16497 30 PHE A O   
210  C CB  . PHE A 31 ? 0.21496 0.23767 0.37880 0.00917  0.00388  -0.17005 30 PHE A CB  
211  C CG  . PHE A 31 ? 0.21727 0.23393 0.37375 0.01031  -0.00025 -0.16769 30 PHE A CG  
212  C CD1 . PHE A 31 ? 0.21222 0.23234 0.37266 0.01132  -0.00451 -0.16685 30 PHE A CD1 
213  C CD2 . PHE A 31 ? 0.22639 0.23233 0.37101 0.01013  0.00003  -0.16658 30 PHE A CD2 
214  C CE1 . PHE A 31 ? 0.23237 0.24691 0.38715 0.01172  -0.00777 -0.16504 30 PHE A CE1 
215  C CE2 . PHE A 31 ? 0.22893 0.22955 0.36828 0.01067  -0.00440 -0.16498 30 PHE A CE2 
216  C CZ  . PHE A 31 ? 0.22247 0.22820 0.36800 0.01129  -0.00797 -0.16428 30 PHE A CZ  
217  N N   . ALA A 32 ? 0.19909 0.23621 0.37683 0.00779  -0.00109 -0.16953 31 ALA A N   
218  C CA  . ALA A 32 ? 0.19571 0.23448 0.37489 0.00836  -0.00486 -0.16852 31 ALA A CA  
219  C C   . ALA A 32 ? 0.19733 0.23607 0.37872 0.01099  -0.00845 -0.16973 31 ALA A C   
220  O O   . ALA A 32 ? 0.19935 0.23990 0.38536 0.01251  -0.00807 -0.17235 31 ALA A O   
221  C CB  . ALA A 32 ? 0.19328 0.23644 0.37735 0.00703  -0.00450 -0.16994 31 ALA A CB  
222  N N   . TYR A 33 ? 0.21300 0.24846 0.39055 0.01157  -0.01149 -0.16797 32 TYR A N   
223  C CA  . TYR A 33 ? 0.20178 0.23456 0.37858 0.01416  -0.01516 -0.16881 32 TYR A CA  
224  C C   . TYR A 33 ? 0.28664 0.31451 0.45817 0.01406  -0.01762 -0.16748 32 TYR A C   
225  O O   . TYR A 33 ? 0.21910 0.24515 0.38723 0.01186  -0.01571 -0.16547 32 TYR A O   
226  C CB  . TYR A 33 ? 0.20479 0.23268 0.37648 0.01492  -0.01503 -0.16749 32 TYR A CB  
227  C CG  . TYR A 33 ? 0.20468 0.22802 0.37046 0.01300  -0.01433 -0.16443 32 TYR A CG  
228  C CD1 . TYR A 33 ? 0.22350 0.24728 0.38866 0.01124  -0.01213 -0.16340 32 TYR A CD1 
229  C CD2 . TYR A 33 ? 0.21124 0.22903 0.37253 0.01297  -0.01595 -0.16309 32 TYR A CD2 
230  C CE1 . TYR A 33 ? 0.20281 0.22343 0.36583 0.00987  -0.01247 -0.16158 32 TYR A CE1 
231  C CE2 . TYR A 33 ? 0.27275 0.28756 0.43225 0.01100  -0.01503 -0.16130 32 TYR A CE2 
232  C CZ  . TYR A 33 ? 0.30271 0.31987 0.46451 0.00963  -0.01373 -0.16077 32 TYR A CZ  
233  O OH  . TYR A 33 ? 0.31326 0.32844 0.47645 0.00801  -0.01374 -0.15988 32 TYR A OH  
234  N N   . TYR A 34 ? 0.22143 0.24564 0.39136 0.01662  -0.02170 -0.16884 33 TYR A N   
235  C CA  . TYR A 34 ? 0.21752 0.23355 0.37937 0.01685  -0.02446 -0.16810 33 TYR A CA  
236  C C   . TYR A 34 ? 0.25234 0.25910 0.40451 0.01628  -0.02346 -0.16548 33 TYR A C   
237  O O   . TYR A 34 ? 0.25898 0.26500 0.41109 0.01740  -0.02366 -0.16538 33 TYR A O   
238  C CB  . TYR A 34 ? 0.24274 0.25824 0.40761 0.02039  -0.03056 -0.17161 33 TYR A CB  
239  C CG  . TYR A 34 ? 0.23588 0.23921 0.38905 0.02134  -0.03500 -0.17126 33 TYR A CG  
240  C CD1 . TYR A 34 ? 0.37926 0.37157 0.52184 0.02292  -0.03678 -0.17014 33 TYR A CD1 
241  C CD2 . TYR A 34 ? 0.23957 0.24023 0.39012 0.02042  -0.03731 -0.17207 33 TYR A CD2 
242  C CE1 . TYR A 34 ? 0.27218 0.25014 0.40080 0.02353  -0.04040 -0.16979 33 TYR A CE1 
243  C CE2 . TYR A 34 ? 0.26910 0.25522 0.40535 0.02104  -0.04150 -0.17168 33 TYR A CE2 
244  C CZ  . TYR A 34 ? 0.33661 0.31117 0.46173 0.02270  -0.04299 -0.17060 33 TYR A CZ  
245  O OH  . TYR A 34 ? 0.32293 0.28029 0.43101 0.02303  -0.04664 -0.17018 33 TYR A OH  
246  N N   . VAL A 35 ? 0.22804 0.22677 0.37184 0.01432  -0.02188 -0.16369 34 VAL A N   
247  C CA  . VAL A 35 ? 0.30977 0.29863 0.44504 0.01321  -0.02003 -0.16191 34 VAL A CA  
248  C C   . VAL A 35 ? 0.25526 0.23028 0.37738 0.01366  -0.02179 -0.16197 34 VAL A C   
249  O O   . VAL A 35 ? 0.25551 0.22695 0.37339 0.01245  -0.02101 -0.16185 34 VAL A O   
250  C CB  . VAL A 35 ? 0.31999 0.31040 0.45803 0.00987  -0.01475 -0.16014 34 VAL A CB  
251  C CG1 . VAL A 35 ? 0.30503 0.28618 0.43731 0.00852  -0.01268 -0.15929 34 VAL A CG1 
252  C CG2 . VAL A 35 ? 0.32323 0.32466 0.47156 0.00958  -0.01407 -0.16018 34 VAL A CG2 
253  N N   . PRO A 36 ? 0.51977 0.25464 0.49290 0.07126  -0.25216 -0.06896 35 PRO A N   
254  C CA  . PRO A 36 ? 0.52768 0.22737 0.49425 0.06682  -0.25057 -0.06684 35 PRO A CA  
255  C C   . PRO A 36 ? 0.52913 0.23592 0.49678 0.06451  -0.24554 -0.06047 35 PRO A C   
256  O O   . PRO A 36 ? 0.52620 0.26106 0.50030 0.06274  -0.24388 -0.06028 35 PRO A O   
257  C CB  . PRO A 36 ? 0.57492 0.26040 0.54513 0.05540  -0.25407 -0.07805 35 PRO A CB  
258  C CG  . PRO A 36 ? 0.59167 0.30242 0.57006 0.05408  -0.25827 -0.09045 35 PRO A CG  
259  C CD  . PRO A 36 ? 0.52375 0.27312 0.50334 0.06217  -0.25665 -0.08469 35 PRO A CD  
260  N N   . GLY A 37 ? 0.53400 0.21835 0.49514 0.06478  -0.24316 -0.05576 36 GLY A N   
261  C CA  . GLY A 37 ? 0.53692 0.22761 0.49823 0.06198  -0.23861 -0.05065 36 GLY A CA  
262  C C   . GLY A 37 ? 0.54674 0.23589 0.51181 0.04995  -0.23863 -0.05258 36 GLY A C   
263  O O   . GLY A 37 ? 0.55167 0.23356 0.52292 0.04321  -0.24165 -0.05929 36 GLY A O   
264  N N   . GLY A 38 ? 0.54976 0.24692 0.51533 0.04722  -0.23442 -0.04687 37 GLY A N   
265  C CA  . GLY A 38 ? 0.55926 0.25609 0.53346 0.03630  -0.23296 -0.04623 37 GLY A CA  
266  C C   . GLY A 38 ? 0.59661 0.30191 0.56895 0.03520  -0.22792 -0.03719 37 GLY A C   
267  O O   . GLY A 38 ? 0.58000 0.28852 0.54313 0.04272  -0.22579 -0.03295 37 GLY A O   
268  N N   . VAL A 39 ? 0.56999 0.28032 0.55484 0.02551  -0.22560 -0.03571 38 VAL A N   
269  C CA  . VAL A 39 ? 0.57749 0.29915 0.56349 0.02297  -0.22058 -0.02660 38 VAL A CA  
270  C C   . VAL A 39 ? 0.65286 0.39234 0.65411 0.01467  -0.21938 -0.03250 38 VAL A C   
271  O O   . VAL A 39 ? 0.85100 0.58965 0.86850 0.00740  -0.22116 -0.04238 38 VAL A O   
272  C CB  . VAL A 39 ? 0.64945 0.35951 0.63919 0.01996  -0.21727 -0.01385 38 VAL A CB  
273  C CG1 . VAL A 39 ? 0.86640 0.59282 0.85748 0.01815  -0.21183 -0.00296 38 VAL A CG1 
274  C CG2 . VAL A 39 ? 0.67532 0.37357 0.64973 0.02852  -0.21883 -0.00969 38 VAL A CG2 
275  N N   . TYR A 40 ? 0.71243 0.47041 0.71065 0.01571  -0.21625 -0.02858 39 TYR A N   
276  C CA  . TYR A 40 ? 0.78930 0.56609 0.80201 0.00761  -0.21436 -0.03288 39 TYR A CA  
277  C C   . TYR A 40 ? 0.96832 0.75321 0.97964 0.00631  -0.20900 -0.02128 39 TYR A C   
278  O O   . TYR A 40 ? 0.86288 0.64738 0.85986 0.01356  -0.20730 -0.01318 39 TYR A O   
279  C CB  . TYR A 40 ? 0.80014 0.60138 0.81201 0.01094  -0.21679 -0.04220 39 TYR A CB  
280  C CG  . TYR A 40 ? 0.97452 0.78685 0.97391 0.02127  -0.21493 -0.03505 39 TYR A CG  
281  C CD1 . TYR A 40 ? 0.99014 0.79453 0.98095 0.03153  -0.21648 -0.03369 39 TYR A CD1 
282  C CD2 . TYR A 40 ? 0.85334 0.68425 0.85421 0.02072  -0.21086 -0.03019 39 TYR A CD2 
283  C CE1 . TYR A 40 ? 0.94650 0.76090 0.93535 0.04092  -0.21321 -0.02812 39 TYR A CE1 
284  C CE2 . TYR A 40 ? 0.79860 0.63968 0.79473 0.03009  -0.20804 -0.02451 39 TYR A CE2 
285  C CZ  . TYR A 40 ? 0.91381 0.74650 0.90638 0.04014  -0.20884 -0.02376 39 TYR A CZ  
286  O OH  . TYR A 40 ? 0.77858 0.62094 0.77552 0.04941  -0.20457 -0.01905 39 TYR A OH  
287  N N   . LYS A 41 ? 0.85980 0.65498 0.88867 -0.00307 -0.20613 -0.02243 40 LYS A N   
288  C CA  . LYS A 41 ? 0.97035 0.77361 1.00136 -0.00551 -0.20059 -0.01019 40 LYS A CA  
289  C C   . LYS A 41 ? 0.81871 0.64429 0.83978 -0.00153 -0.19961 -0.01108 40 LYS A C   
290  O O   . LYS A 41 ? 0.88000 0.72128 0.90435 -0.00195 -0.20170 -0.02115 40 LYS A O   
291  C CB  . LYS A 41 ? 1.00534 0.80926 1.06519 -0.01740 -0.19680 -0.01039 40 LYS A CB  
292  C CG  . LYS A 41 ? 1.04525 0.82765 1.12498 -0.02219 -0.19591 -0.00863 40 LYS A CG  
293  C CD  . LYS A 41 ? 1.14522 0.92997 1.26378 -0.03441 -0.19087 -0.01210 40 LYS A CD  
294  C CE  . LYS A 41 ? 1.04968 0.84361 1.17522 -0.03639 -0.18373 0.00616  40 LYS A CE  
295  N NZ  . LYS A 41 ? 0.95603 0.74157 1.07066 -0.02961 -0.18030 0.03042  40 LYS A NZ  
296  N N   . SER A 42 ? 0.83706 0.66805 0.84768 0.00286  -0.19606 -0.00032 41 SER A N   
297  C CA  . SER A 42 ? 1.00504 0.85718 1.01155 0.00537  -0.19371 -0.00018 41 SER A CA  
298  C C   . SER A 42 ? 0.98456 0.84978 1.00671 -0.00448 -0.19109 -0.00037 41 SER A C   
299  O O   . SER A 42 ? 0.84761 0.70820 0.88142 -0.01113 -0.18770 0.00758  41 SER A O   
300  C CB  . SER A 42 ? 0.91599 0.77407 0.91085 0.01182  -0.19032 0.00821  41 SER A CB  
301  O OG  . SER A 42 ? 0.84813 0.70248 0.83296 0.02185  -0.19198 0.00306  41 SER A OG  
302  N N   . GLN A 43 ? 0.87768 0.76186 0.90310 -0.00495 -0.19199 -0.00837 42 GLN A N   
303  C CA  . GLN A 43 ? 0.94724 0.84642 0.98998 -0.01479 -0.19027 -0.01308 42 GLN A CA  
304  C C   . GLN A 43 ? 0.83692 0.75386 0.87801 -0.01525 -0.18582 -0.00589 42 GLN A C   
305  O O   . GLN A 43 ? 0.85648 0.78124 0.91323 -0.02412 -0.18294 -0.00606 42 GLN A O   
306  C CB  . GLN A 43 ? 0.84723 0.76430 0.89736 -0.01602 -0.19431 -0.02838 42 GLN A CB  
307  C CG  . GLN A 43 ? 0.97559 0.87945 1.03636 -0.02001 -0.19815 -0.03963 42 GLN A CG  
308  C CD  . GLN A 43 ? 0.99633 0.88389 1.08038 -0.03091 -0.19495 -0.03970 42 GLN A CD  
309  O OE1 . GLN A 43 ? 1.15652 1.05388 1.25766 -0.03859 -0.19077 -0.03932 42 GLN A OE1 
310  N NE2 . GLN A 43 ? 0.95841 0.82134 1.04666 -0.03126 -0.19611 -0.03879 42 GLN A NE2 
311  N N   . THR A 44 ? 0.71848 0.64206 0.74496 -0.00622 -0.18461 -0.00058 43 THR A N   
312  C CA  . THR A 44 ? 0.78238 0.72232 0.80756 -0.00615 -0.18012 0.00592  43 THR A CA  
313  C C   . THR A 44 ? 0.75738 0.69171 0.77116 -0.00020 -0.17749 0.01445  43 THR A C   
314  O O   . THR A 44 ? 0.80311 0.72509 0.80846 0.00647  -0.17937 0.01324  43 THR A O   
315  C CB  . THR A 44 ? 0.79305 0.75477 0.81786 -0.00061 -0.17965 0.00282  43 THR A CB  
316  O OG1 . THR A 44 ? 0.72757 0.68386 0.74573 0.01032  -0.18021 0.00298  43 THR A OG1 
317  C CG2 . THR A 44 ? 0.69940 0.67731 0.73436 -0.00498 -0.18256 -0.00633 43 THR A CG2 
318  N N   . ASP A 45 ? 0.73657 0.68402 0.75096 -0.00246 -0.17311 0.02189  44 ASP A N   
319  C CA  . ASP A 45 ? 0.82032 0.77344 0.82454 0.00385  -0.17045 0.02765  44 ASP A CA  
320  C C   . ASP A 45 ? 0.78899 0.74805 0.78829 0.01386  -0.17041 0.01913  44 ASP A C   
321  O O   . ASP A 45 ? 0.70637 0.66777 0.69921 0.02051  -0.16967 0.01714  44 ASP A O   
322  C CB  . ASP A 45 ? 0.65300 0.62471 0.65998 -0.00005 -0.16556 0.03693  44 ASP A CB  
323  C CG  . ASP A 45 ? 0.85119 0.81772 0.87165 -0.00994 -0.16371 0.04677  44 ASP A CG  
324  O OD1 . ASP A 45 ? 0.88788 0.83617 0.91495 -0.01277 -0.16557 0.04802  44 ASP A OD1 
325  O OD2 . ASP A 45 ? 0.92833 0.90900 0.95646 -0.01492 -0.15976 0.05305  44 ASP A OD2 
326  N N   . VAL A 46 ? 0.64992 0.61515 0.65618 0.01553  -0.17041 0.01410  45 VAL A N   
327  C CA  . VAL A 46 ? 0.74800 0.71690 0.75878 0.02555  -0.16886 0.00801  45 VAL A CA  
328  C C   . VAL A 46 ? 0.90749 0.85745 0.91525 0.03082  -0.17232 0.00330  45 VAL A C   
329  O O   . VAL A 46 ? 0.80636 0.75507 0.81567 0.03833  -0.17085 -0.00263 45 VAL A O   
330  C CB  . VAL A 46 ? 0.59973 0.58252 0.62241 0.02722  -0.16712 0.00877  45 VAL A CB  
331  C CG1 . VAL A 46 ? 0.53356 0.51957 0.56963 0.03832  -0.16353 0.00559  45 VAL A CG1 
332  C CG2 . VAL A 46 ? 0.53868 0.54069 0.56415 0.02187  -0.16374 0.01296  45 VAL A CG2 
333  N N   . ILE A 47 ? 0.80774 0.74464 0.81338 0.02679  -0.17685 0.00382  46 ILE A N   
334  C CA  . ILE A 47 ? 0.81204 0.72968 0.81357 0.03083  -0.18057 0.00004  46 ILE A CA  
335  C C   . ILE A 47 ? 0.77344 0.68090 0.76476 0.02999  -0.18129 0.00170  46 ILE A C   
336  O O   . ILE A 47 ? 0.83454 0.73386 0.82219 0.03663  -0.18223 -0.00299 46 ILE A O   
337  C CB  . ILE A 47 ? 0.73795 0.64879 0.74138 0.02621  -0.18513 -0.00142 46 ILE A CB  
338  C CG1 . ILE A 47 ? 0.69456 0.62536 0.70782 0.02941  -0.18418 -0.00146 46 ILE A CG1 
339  C CG2 . ILE A 47 ? 0.69836 0.58806 0.69675 0.02974  -0.18915 -0.00497 46 ILE A CG2 
340  C CD1 . ILE A 47 ? 0.60409 0.54270 0.62066 0.02357  -0.18833 -0.00555 46 ILE A CD1 
341  N N   . LYS A 48 ? 0.74446 0.65547 0.73362 0.02244  -0.18020 0.00955  47 LYS A N   
342  C CA  . LYS A 48 ? 0.70523 0.61380 0.68708 0.02268  -0.17970 0.01632  47 LYS A CA  
343  C C   . LYS A 48 ? 0.73988 0.66565 0.71558 0.03124  -0.17724 0.01192  47 LYS A C   
344  O O   . LYS A 48 ? 0.92800 0.85322 0.89647 0.03601  -0.17829 0.01128  47 LYS A O   
345  C CB  . LYS A 48 ? 0.78846 0.70311 0.77606 0.01400  -0.17684 0.02904  47 LYS A CB  
346  C CG  . LYS A 48 ? 0.80801 0.72764 0.79188 0.01520  -0.17464 0.04231  47 LYS A CG  
347  C CD  . LYS A 48 ? 0.90373 0.82837 0.90147 0.00665  -0.17029 0.05790  47 LYS A CD  
348  C CE  . LYS A 48 ? 0.77805 0.71817 0.77425 0.01001  -0.16622 0.07667  47 LYS A CE  
349  N NZ  . LYS A 48 ? 0.77765 0.70377 0.77089 0.01378  -0.16848 0.08032  47 LYS A NZ  
350  N N   . ASN A 49 ? 0.75534 0.69959 0.73607 0.03345  -0.17376 0.00714  48 ASN A N   
351  C CA  . ASN A 49 ? 0.88418 0.84881 0.86490 0.04132  -0.17094 -0.00221 48 ASN A CA  
352  C C   . ASN A 49 ? 0.87608 0.83080 0.86367 0.04940  -0.17202 -0.01643 48 ASN A C   
353  O O   . ASN A 49 ? 0.88174 0.84574 0.86705 0.05541  -0.17196 -0.02549 48 ASN A O   
354  C CB  . ASN A 49 ? 0.94897 0.93558 0.93811 0.04111  -0.16624 -0.00473 48 ASN A CB  
355  C CG  . ASN A 49 ? 0.95108 0.95518 0.93369 0.03519  -0.16410 0.00810  48 ASN A CG  
356  O OD1 . ASN A 49 ? 1.02864 1.03987 1.00223 0.03480  -0.16438 0.01729  48 ASN A OD1 
357  N ND2 . ASN A 49 ? 0.88124 0.89443 0.87043 0.03117  -0.16131 0.01067  48 ASN A ND2 
358  N N   . THR A 50 ? 0.84135 0.78099 0.83947 0.05017  -0.17262 -0.01817 49 THR A N   
359  C CA  . THR A 50 ? 0.76840 0.69974 0.77960 0.05850  -0.17203 -0.02926 49 THR A CA  
360  C C   . THR A 50 ? 0.81862 0.73154 0.81906 0.06016  -0.17686 -0.03110 49 THR A C   
361  O O   . THR A 50 ? 0.85382 0.76880 0.85978 0.06702  -0.17614 -0.04320 49 THR A O   
362  C CB  . THR A 50 ? 0.67397 0.59948 0.70080 0.06008  -0.17061 -0.02538 49 THR A CB  
363  O OG1 . THR A 50 ? 0.58571 0.52951 0.62198 0.05830  -0.16611 -0.02169 49 THR A OG1 
364  C CG2 . THR A 50 ? 0.69471 0.61552 0.74360 0.06986  -0.16745 -0.03425 49 THR A CG2 
365  N N   . PHE A 51 ? 0.73094 0.62718 0.71894 0.05380  -0.18146 -0.02088 50 PHE A N   
366  C CA  . PHE A 51 ? 0.74270 0.61855 0.72306 0.05516  -0.18603 -0.02175 50 PHE A CA  
367  C C   . PHE A 51 ? 0.77321 0.64677 0.73937 0.05056  -0.18815 -0.01276 50 PHE A C   
368  O O   . PHE A 51 ? 0.84718 0.70309 0.80775 0.05090  -0.19179 -0.01167 50 PHE A O   
369  C CB  . PHE A 51 ? 0.63883 0.49685 0.62263 0.05293  -0.18937 -0.01892 50 PHE A CB  
370  C CG  . PHE A 51 ? 0.81876 0.68266 0.81915 0.05861  -0.18656 -0.02178 50 PHE A CG  
371  C CD1 . PHE A 51 ? 0.94009 0.81883 0.94774 0.05562  -0.18414 -0.01631 50 PHE A CD1 
372  C CD2 . PHE A 51 ? 0.55019 0.40667 0.56208 0.06740  -0.18564 -0.02813 50 PHE A CD2 
373  C CE1 . PHE A 51 ? 0.72554 0.61418 0.75152 0.06209  -0.18049 -0.01465 50 PHE A CE1 
374  C CE2 . PHE A 51 ? 0.63121 0.49534 0.66471 0.07375  -0.18137 -0.02622 50 PHE A CE2 
375  C CZ  . PHE A 51 ? 0.65653 0.53798 0.69692 0.07142  -0.17865 -0.01814 50 PHE A CZ  
376  N N   . GLY A 52 ? 0.73302 0.69756 0.77423 -0.08669 -0.12971 0.17850  51 GLY A N   
377  C CA  . GLY A 52 ? 0.70286 0.64368 0.72013 -0.08921 -0.13561 0.19764  51 GLY A CA  
378  C C   . GLY A 52 ? 0.80756 0.73063 0.85816 -0.09978 -0.14217 0.20433  51 GLY A C   
379  O O   . GLY A 52 ? 0.85408 0.79428 0.94066 -0.10671 -0.14710 0.19157  51 GLY A O   
380  N N   . GLU A 53 ? 0.81036 0.70320 0.85103 -0.10006 -0.13967 0.22407  52 GLU A N   
381  C CA  . GLU A 53 ? 0.98627 0.85771 1.06851 -0.11558 -0.13465 0.22553  52 GLU A CA  
382  C C   . GLU A 53 ? 0.89884 0.76140 0.99849 -0.11596 -0.15519 0.20343  52 GLU A C   
383  O O   . GLU A 53 ? 0.87231 0.74261 1.01206 -0.13353 -0.15629 0.18417  52 GLU A O   
384  C CB  . GLU A 53 ? 0.92971 0.76442 1.00535 -0.11344 -0.11318 0.25869  52 GLU A CB  
385  C CG  . GLU A 53 ? 1.15563 0.96556 1.28950 -0.13555 -0.09342 0.25615  52 GLU A CG  
386  C CD  . GLU A 53 ? 1.33399 1.11644 1.47458 -0.13737 -0.05538 0.29179  52 GLU A CD  
387  O OE1 . GLU A 53 ? 1.38865 1.17356 1.47749 -0.11796 -0.04764 0.32271  52 GLU A OE1 
388  O OE2 . GLU A 53 ? 1.27537 1.03676 1.47462 -0.15883 -0.03030 0.28665  52 GLU A OE2 
389  N N   . GLU A 54 ? 0.91314 0.76477 0.98514 -0.09805 -0.17070 0.20255  53 GLU A N   
390  C CA  . GLU A 54 ? 0.82446 0.66665 0.90965 -0.09630 -0.18730 0.18095  53 GLU A CA  
391  C C   . GLU A 54 ? 0.82128 0.67996 0.88292 -0.07858 -0.20197 0.16860  53 GLU A C   
392  O O   . GLU A 54 ? 0.67138 0.53935 0.70485 -0.06645 -0.20216 0.17648  53 GLU A O   
393  C CB  . GLU A 54 ? 0.68506 0.48376 0.78014 -0.09374 -0.18352 0.19235  53 GLU A CB  
394  C CG  . GLU A 54 ? 0.92182 0.69962 1.06243 -0.11755 -0.16455 0.18641  53 GLU A CG  
395  C CD  . GLU A 54 ? 1.07456 0.80343 1.23791 -0.11566 -0.15300 0.19315  53 GLU A CD  
396  O OE1 . GLU A 54 ? 1.06429 0.78049 1.20614 -0.09309 -0.16454 0.20535  53 GLU A OE1 
397  O OE2 . GLU A 54 ? 1.07901 0.78387 1.28913 -0.13745 -0.12923 0.18418  53 GLU A OE2 
398  N N   . VAL A 55 ? 0.71543 0.58131 0.79082 -0.07784 -0.21149 0.14649  54 VAL A N   
399  C CA  . VAL A 55 ? 0.82505 0.70733 0.89196 -0.06273 -0.21547 0.13328  54 VAL A CA  
400  C C   . VAL A 55 ? 0.48008 0.33863 0.54808 -0.05310 -0.22646 0.12120  54 VAL A C   
401  O O   . VAL A 55 ? 0.60734 0.45366 0.68868 -0.05962 -0.23049 0.11126  54 VAL A O   
402  C CB  . VAL A 55 ? 0.66595 0.58266 0.74925 -0.06299 -0.20969 0.12619  54 VAL A CB  
403  C CG1 . VAL A 55 ? 0.65119 0.58280 0.73254 -0.04785 -0.19669 0.12285  54 VAL A CG1 
404  C CG2 . VAL A 55 ? 0.73963 0.67872 0.83839 -0.07888 -0.20269 0.13576  54 VAL A CG2 
405  N N   . LYS A 56 ? 0.45713 0.31434 0.51447 -0.03929 -0.22981 0.11733  55 LYS A N   
406  C CA  . LYS A 56 ? 0.47655 0.31572 0.54213 -0.02834 -0.23744 0.10396  55 LYS A CA  
407  C C   . LYS A 56 ? 0.46581 0.31631 0.54268 -0.02004 -0.22780 0.08598  55 LYS A C   
408  O O   . LYS A 56 ? 0.40979 0.28247 0.48920 -0.01655 -0.21439 0.08193  55 LYS A O   
409  C CB  . LYS A 56 ? 0.46410 0.30822 0.52088 -0.01716 -0.24628 0.10657  55 LYS A CB  
410  C CG  . LYS A 56 ? 0.72367 0.54507 0.79559 -0.00680 -0.25600 0.10261  55 LYS A CG  
411  C CD  . LYS A 56 ? 0.75796 0.60061 0.82168 0.00609  -0.26792 0.11260  55 LYS A CD  
412  C CE  . LYS A 56 ? 0.69595 0.58115 0.75821 0.00986  -0.27070 0.08647  55 LYS A CE  
413  N NZ  . LYS A 56 ? 0.87915 0.80435 0.93351 0.02296  -0.28914 0.09020  55 LYS A NZ  
414  N N   . TYR A 57 ? 0.41806 0.25183 0.50387 -0.01572 -0.22881 0.07637  56 TYR A N   
415  C CA  . TYR A 57 ? 0.39997 0.24079 0.49592 -0.00193 -0.21413 0.06615  56 TYR A CA  
416  C C   . TYR A 57 ? 0.39990 0.21385 0.50842 0.00856  -0.21370 0.05141  56 TYR A C   
417  O O   . TYR A 57 ? 0.41408 0.20321 0.52268 0.00470  -0.22530 0.04953  56 TYR A O   
418  C CB  . TYR A 57 ? 0.44103 0.30098 0.53237 -0.00182 -0.21083 0.07081  56 TYR A CB  
419  C CG  . TYR A 57 ? 0.45720 0.30379 0.54219 -0.01198 -0.22297 0.06131  56 TYR A CG  
420  C CD1 . TYR A 57 ? 0.43020 0.25748 0.51462 -0.00212 -0.21858 0.04875  56 TYR A CD1 
421  C CD2 . TYR A 57 ? 0.43348 0.28606 0.51817 -0.03347 -0.23320 0.06102  56 TYR A CD2 
422  C CE1 . TYR A 57 ? 0.65066 0.46563 0.73039 -0.01465 -0.22525 0.03326  56 TYR A CE1 
423  C CE2 . TYR A 57 ? 0.58326 0.42302 0.67089 -0.04770 -0.23786 0.04319  56 TYR A CE2 
424  C CZ  . TYR A 57 ? 0.62624 0.44806 0.70933 -0.03867 -0.23434 0.02801  56 TYR A CZ  
425  O OH  . TYR A 57 ? 0.62663 0.43560 0.71361 -0.05530 -0.23443 0.00412  56 TYR A OH  
426  N N   A ARG A 58 ? 0.27584 0.22422 0.33739 0.00847  -0.07537 -0.13572 57 ARG A N   
427  N N   B ARG A 58 ? 0.27566 0.22411 0.33731 0.00850  -0.07533 -0.13571 57 ARG A N   
428  C CA  A ARG A 58 ? 0.25841 0.21704 0.32719 0.00974  -0.07884 -0.13932 57 ARG A CA  
429  C CA  B ARG A 58 ? 0.25834 0.21698 0.32725 0.00982  -0.07890 -0.13930 57 ARG A CA  
430  C C   A ARG A 58 ? 0.24719 0.21767 0.32894 0.01330  -0.07738 -0.14114 57 ARG A C   
431  C C   B ARG A 58 ? 0.24716 0.21764 0.32901 0.01336  -0.07746 -0.14113 57 ARG A C   
432  O O   A ARG A 58 ? 0.26840 0.23976 0.35163 0.01356  -0.07223 -0.13959 57 ARG A O   
433  O O   B ARG A 58 ? 0.26880 0.24019 0.35220 0.01367  -0.07236 -0.13958 57 ARG A O   
434  C CB  A ARG A 58 ? 0.26460 0.22411 0.32772 0.00530  -0.07437 -0.14076 57 ARG A CB  
435  C CB  B ARG A 58 ? 0.26452 0.22409 0.32784 0.00542  -0.07453 -0.14076 57 ARG A CB  
436  C CG  A ARG A 58 ? 0.33116 0.27980 0.38099 0.00135  -0.07634 -0.14000 57 ARG A CG  
437  C CG  B ARG A 58 ? 0.33066 0.27935 0.38085 0.00158  -0.07648 -0.13993 57 ARG A CG  
438  C CD  A ARG A 58 ? 0.38477 0.33528 0.43018 -0.00302 -0.07141 -0.14175 57 ARG A CD  
439  C CD  B ARG A 58 ? 0.41834 0.37097 0.46644 -0.00183 -0.07433 -0.14243 57 ARG A CD  
440  N NE  A ARG A 58 ? 0.37926 0.31866 0.41050 -0.00741 -0.07250 -0.14124 57 ARG A NE  
441  N NE  B ARG A 58 ? 0.37988 0.32135 0.41333 -0.00672 -0.07351 -0.14164 57 ARG A NE  
442  C CZ  A ARG A 58 ? 0.39059 0.32854 0.41512 -0.01193 -0.06843 -0.14251 57 ARG A CZ  
443  C CZ  B ARG A 58 ? 0.41389 0.35634 0.44300 -0.01038 -0.07247 -0.14368 57 ARG A CZ  
444  N NH1 A ARG A 58 ? 0.35125 0.29804 0.38223 -0.01264 -0.06301 -0.14420 57 ARG A NH1 
445  N NH1 B ARG A 58 ? 0.42995 0.38399 0.46884 -0.00964 -0.07213 -0.14655 57 ARG A NH1 
446  N NH2 A ARG A 58 ? 0.47116 0.39791 0.48161 -0.01600 -0.06978 -0.14219 57 ARG A NH2 
447  N NH2 B ARG A 58 ? 0.49711 0.42828 0.51164 -0.01506 -0.07151 -0.14307 57 ARG A NH2 
448  N N   . PRO A 59 ? 0.25455 0.23397 0.34586 0.01594  -0.08185 -0.14464 58 PRO A N   
449  C CA  . PRO A 59 ? 0.23593 0.22650 0.33851 0.01846  -0.07920 -0.14721 58 PRO A CA  
450  C C   . PRO A 59 ? 0.24526 0.23962 0.34563 0.01504  -0.07091 -0.14779 58 PRO A C   
451  O O   . PRO A 59 ? 0.25514 0.24539 0.34757 0.01111  -0.06801 -0.14714 58 PRO A O   
452  C CB  . PRO A 59 ? 0.24178 0.23976 0.35447 0.02131  -0.08544 -0.15135 58 PRO A CB  
453  C CG  . PRO A 59 ? 0.29422 0.28696 0.39988 0.01874  -0.08925 -0.15126 58 PRO A CG  
454  C CD  . PRO A 59 ? 0.29863 0.27836 0.39090 0.01638  -0.08916 -0.14678 58 PRO A CD  
455  N N   . TYR A 60 ? 0.25082 0.25237 0.35772 0.01638  -0.06706 -0.14900 59 TYR A N   
456  C CA  . TYR A 60 ? 0.23977 0.24428 0.34457 0.01333  -0.05939 -0.14933 59 TYR A CA  
457  C C   . TYR A 60 ? 0.21606 0.23091 0.33051 0.01529  -0.05767 -0.15286 59 TYR A C   
458  O O   . TYR A 60 ? 0.22592 0.24546 0.34871 0.01889  -0.06211 -0.15513 59 TYR A O   
459  C CB  . TYR A 60 ? 0.22044 0.21718 0.31717 0.01139  -0.05461 -0.14501 59 TYR A CB  
460  C CG  . TYR A 60 ? 0.25259 0.24863 0.35229 0.01430  -0.05572 -0.14320 59 TYR A CG  
461  C CD1 . TYR A 60 ? 0.31918 0.30938 0.41827 0.01644  -0.06081 -0.14114 59 TYR A CD1 
462  C CD2 . TYR A 60 ? 0.23018 0.23094 0.33295 0.01474  -0.05192 -0.14363 59 TYR A CD2 
463  C CE1 . TYR A 60 ? 0.29096 0.28070 0.39341 0.01901  -0.06187 -0.13960 59 TYR A CE1 
464  C CE2 . TYR A 60 ? 0.29996 0.29998 0.40518 0.01719  -0.05333 -0.14214 59 TYR A CE2 
465  C CZ  . TYR A 60 ? 0.32966 0.32455 0.43523 0.01935  -0.05822 -0.14017 59 TYR A CZ  
466  O OH  . TYR A 60 ? 0.32390 0.31839 0.43255 0.02164  -0.05958 -0.13888 59 TYR A OH  
467  N N   . LEU A 61 ? 0.23326 0.25127 0.34648 0.01271  -0.05107 -0.15362 60 LEU A N   
468  C CA  . LEU A 61 ? 0.20746 0.23387 0.32752 0.01363  -0.04819 -0.15687 60 LEU A CA  
469  C C   . LEU A 61 ? 0.20888 0.23238 0.32400 0.01275  -0.04357 -0.15416 60 LEU A C   
470  O O   . LEU A 61 ? 0.20593 0.22272 0.31338 0.01037  -0.04045 -0.15069 60 LEU A O   
471  C CB  . LEU A 61 ? 0.20751 0.24035 0.33084 0.01116  -0.04444 -0.16075 60 LEU A CB  
472  C CG  . LEU A 61 ? 0.21023 0.24688 0.33978 0.01187  -0.04908 -0.16413 60 LEU A CG  
473  C CD1 . LEU A 61 ? 0.21015 0.25324 0.34345 0.00899  -0.04459 -0.16807 60 LEU A CD1 
474  C CD2 . LEU A 61 ? 0.20926 0.25119 0.34926 0.01633  -0.05470 -0.16711 60 LEU A CD2 
475  N N   . ALA A 62 ? 0.22231 0.25067 0.34203 0.01462  -0.04324 -0.15606 61 ALA A N   
476  C CA  . ALA A 62 ? 0.24701 0.27276 0.36231 0.01411  -0.03997 -0.15399 61 ALA A CA  
477  C C   . ALA A 62 ? 0.26543 0.29770 0.38307 0.01316  -0.03579 -0.15779 61 ALA A C   
478  O O   . ALA A 62 ? 0.20121 0.24078 0.32616 0.01397  -0.03632 -0.16228 61 ALA A O   
479  C CB  . ALA A 62 ? 0.20073 0.22373 0.31728 0.01732  -0.04442 -0.15202 61 ALA A CB  
480  N N   . LEU A 63 ? 0.21267 0.24179 0.32416 0.01134  -0.03158 -0.15620 62 LEU A N   
481  C CA  . LEU A 63 ? 0.20360 0.23671 0.31451 0.00992  -0.02710 -0.15935 62 LEU A CA  
482  C C   . LEU A 63 ? 0.20490 0.23471 0.31179 0.01105  -0.02774 -0.15800 62 LEU A C   
483  O O   . LEU A 63 ? 0.20480 0.22790 0.30668 0.01089  -0.02823 -0.15403 62 LEU A O   
484  C CB  . LEU A 63 ? 0.20515 0.23680 0.31119 0.00602  -0.02094 -0.15918 62 LEU A CB  
485  C CG  . LEU A 63 ? 0.20817 0.24379 0.31332 0.00400  -0.01565 -0.16291 62 LEU A CG  
486  C CD1 . LEU A 63 ? 0.20788 0.25194 0.32124 0.00350  -0.01454 -0.16791 62 LEU A CD1 
487  C CD2 . LEU A 63 ? 0.23958 0.27037 0.33732 0.00066  -0.01006 -0.16116 62 LEU A CD2 
488  N N   . LYS A 64 ? 0.21395 0.24837 0.32351 0.01215  -0.02784 -0.16162 63 LYS A N   
489  C CA  . LYS A 64 ? 0.20991 0.24154 0.31427 0.01246  -0.02756 -0.16151 63 LYS A CA  
490  C C   . LYS A 64 ? 0.22480 0.25471 0.32183 0.00903  -0.02147 -0.16243 63 LYS A C   
491  O O   . LYS A 64 ? 0.27387 0.30862 0.37212 0.00730  -0.01733 -0.16642 63 LYS A O   
492  C CB  . LYS A 64 ? 0.24609 0.28300 0.35569 0.01461  -0.02954 -0.16552 63 LYS A CB  
493  C CG  . LYS A 64 ? 0.31798 0.35136 0.42376 0.01614  -0.03212 -0.16475 63 LYS A CG  
494  C CD  . LYS A 64 ? 0.32846 0.35876 0.42469 0.01365  -0.02800 -0.16590 63 LYS A CD  
495  C CE  . LYS A 64 ? 0.37903 0.41469 0.47562 0.01180  -0.02300 -0.17125 63 LYS A CE  
496  N NZ  . LYS A 64 ? 0.35973 0.39113 0.44527 0.00870  -0.01813 -0.17193 63 LYS A NZ  
497  N N   . THR A 65 ? 0.21560 0.23848 0.30567 0.00799  -0.02076 -0.15897 64 THR A N   
498  C CA  . THR A 65 ? 0.21994 0.23990 0.30300 0.00473  -0.01518 -0.15932 64 THR A CA  
499  C C   . THR A 65 ? 0.23576 0.25447 0.31222 0.00418  -0.01382 -0.16190 64 THR A C   
500  O O   . THR A 65 ? 0.28306 0.30289 0.36029 0.00628  -0.01730 -0.16318 64 THR A O   
501  C CB  . THR A 65 ? 0.22109 0.23374 0.30066 0.00394  -0.01512 -0.15488 64 THR A CB  
502  O OG1 . THR A 65 ? 0.27916 0.28683 0.35614 0.00573  -0.01918 -0.15296 64 THR A OG1 
503  C CG2 . THR A 65 ? 0.22887 0.24130 0.31338 0.00457  -0.01693 -0.15215 64 THR A CG2 
504  N N   . VAL A 66 ? 0.23279 0.24857 0.30198 0.00114  -0.00857 -0.16279 65 VAL A N   
505  C CA  . VAL A 66 ? 0.32381 0.33670 0.38411 0.00016  -0.00717 -0.16522 65 VAL A CA  
506  C C   . VAL A 66 ? 0.36146 0.36791 0.41746 0.00190  -0.01261 -0.16277 65 VAL A C   
507  O O   . VAL A 66 ? 0.35926 0.36354 0.40834 0.00183  -0.01366 -0.16491 65 VAL A O   
508  C CB  . VAL A 66 ? 0.24869 0.25899 0.30131 -0.00371 -0.00011 -0.16670 65 VAL A CB  
509  C CG1 . VAL A 66 ? 0.34804 0.36503 0.40612 -0.00563 0.00529  -0.16927 65 VAL A CG1 
510  C CG2 . VAL A 66 ? 0.36368 0.36711 0.41332 -0.00477 0.00030  -0.16303 65 VAL A CG2 
511  N N   . ASP A 67 ? 0.23787 0.24101 0.29787 0.00330  -0.01614 -0.15854 66 ASP A N   
512  C CA  . ASP A 67 ? 0.32697 0.32459 0.38566 0.00518  -0.02190 -0.15618 66 ASP A CA  
513  C C   . ASP A 67 ? 0.35060 0.35117 0.41511 0.00843  -0.02750 -0.15583 66 ASP A C   
514  O O   . ASP A 67 ? 0.34608 0.34275 0.41102 0.01016  -0.03266 -0.15387 66 ASP A O   
515  C CB  . ASP A 67 ? 0.27705 0.26942 0.33864 0.00506  -0.02247 -0.15194 66 ASP A CB  
516  C CG  . ASP A 67 ? 0.44752 0.43618 0.50411 0.00190  -0.01689 -0.15225 66 ASP A CG  
517  O OD1 . ASP A 67 ? 0.47179 0.45807 0.52012 0.00022  -0.01517 -0.15490 66 ASP A OD1 
518  O OD2 . ASP A 67 ? 0.39019 0.37799 0.45057 0.00087  -0.01392 -0.14999 66 ASP A OD2 
519  N N   . ASN A 68 ? 0.28594 0.29323 0.35585 0.00928  -0.02673 -0.15783 67 ASN A N   
520  C CA  . ASN A 68 ? 0.28790 0.29838 0.36427 0.01234  -0.03153 -0.15800 67 ASN A CA  
521  C C   . ASN A 68 ? 0.28287 0.29134 0.36566 0.01443  -0.03567 -0.15363 67 ASN A C   
522  O O   . ASN A 68 ? 0.42968 0.43839 0.51666 0.01701  -0.04037 -0.15290 67 ASN A O   
523  C CB  . ASN A 68 ? 0.34573 0.35432 0.41752 0.01326  -0.03460 -0.15987 67 ASN A CB  
524  C CG  . ASN A 68 ? 0.35199 0.36532 0.43043 0.01586  -0.03764 -0.16173 67 ASN A CG  
525  O OD1 . ASN A 68 ? 0.61319 0.63247 0.69771 0.01626  -0.03585 -0.16385 67 ASN A OD1 
526  N ND2 . ASN A 68 ? 0.53698 0.54775 0.61517 0.01771  -0.04255 -0.16116 67 ASN A ND2 
527  N N   . ASP A 69 ? 0.25227 0.25839 0.33577 0.01320  -0.03366 -0.15082 68 ASP A N   
528  C CA  . ASP A 69 ? 0.31715 0.32146 0.40621 0.01471  -0.03652 -0.14714 68 ASP A CA  
529  C C   . ASP A 69 ? 0.28773 0.29596 0.38014 0.01403  -0.03437 -0.14765 68 ASP A C   
530  O O   . ASP A 69 ? 0.29346 0.30583 0.38485 0.01231  -0.03056 -0.15062 68 ASP A O   
531  C CB  . ASP A 69 ? 0.26349 0.26053 0.35100 0.01391  -0.03649 -0.14330 68 ASP A CB  
532  C CG  . ASP A 69 ? 0.42382 0.41849 0.50639 0.01086  -0.03117 -0.14357 68 ASP A CG  
533  O OD1 . ASP A 69 ? 0.32332 0.32193 0.40438 0.00909  -0.02703 -0.14586 68 ASP A OD1 
534  O OD2 . ASP A 69 ? 0.34091 0.32958 0.42202 0.01021  -0.03113 -0.14153 68 ASP A OD2 
535  N N   . ILE A 70 ? 0.22141 0.22815 0.31785 0.01531  -0.03705 -0.14502 69 ILE A N   
536  C CA  . ILE A 70 ? 0.20358 0.21354 0.30319 0.01511  -0.03671 -0.14572 69 ILE A CA  
537  C C   . ILE A 70 ? 0.24064 0.24588 0.33732 0.01273  -0.03372 -0.14295 69 ILE A C   
538  O O   . ILE A 70 ? 0.25836 0.25748 0.35427 0.01289  -0.03468 -0.13939 69 ILE A O   
539  C CB  . ILE A 70 ? 0.22937 0.24028 0.33458 0.01812  -0.04210 -0.14522 69 ILE A CB  
540  C CG1 . ILE A 70 ? 0.25959 0.27473 0.36852 0.02064  -0.04510 -0.14798 69 ILE A CG1 
541  C CG2 . ILE A 70 ? 0.24459 0.25814 0.35250 0.01783  -0.04238 -0.14629 69 ILE A CG2 
542  C CD1 . ILE A 70 ? 0.29296 0.31445 0.40237 0.01984  -0.04225 -0.15267 69 ILE A CD1 
543  N N   . ALA A 71 ? 0.20290 0.21100 0.29866 0.01049  -0.03001 -0.14479 70 ALA A N   
544  C CA  . ALA A 71 ? 0.20305 0.20716 0.29602 0.00797  -0.02686 -0.14278 70 ALA A CA  
545  C C   . ALA A 71 ? 0.20261 0.20901 0.29807 0.00814  -0.02885 -0.14370 70 ALA A C   
546  O O   . ALA A 71 ? 0.22195 0.23487 0.32191 0.00937  -0.03076 -0.14701 70 ALA A O   
547  C CB  . ALA A 71 ? 0.25503 0.25999 0.34470 0.00487  -0.02089 -0.14427 70 ALA A CB  
548  N N   . THR A 72 ? 0.22140 0.22212 0.31399 0.00679  -0.02836 -0.14110 71 THR A N   
549  C CA  . THR A 72 ? 0.20568 0.20794 0.29882 0.00605  -0.02964 -0.14249 71 THR A CA  
550  C C   . THR A 72 ? 0.23527 0.24217 0.32839 0.00335  -0.02510 -0.14535 71 THR A C   
551  O O   . THR A 72 ? 0.25648 0.26167 0.34651 0.00106  -0.01993 -0.14474 71 THR A O   
552  C CB  . THR A 72 ? 0.22151 0.21548 0.30979 0.00467  -0.02973 -0.13932 71 THR A CB  
553  O OG1 . THR A 72 ? 0.36813 0.35740 0.45201 0.00166  -0.02387 -0.13753 71 THR A OG1 
554  C CG2 . THR A 72 ? 0.23533 0.22435 0.32403 0.00707  -0.03365 -0.13657 71 THR A CG2 
555  N N   . TRP A 73 ? 0.22243 0.23518 0.31977 0.00363  -0.02709 -0.14866 72 TRP A N   
556  C CA  . TRP A 73 ? 0.25910 0.27795 0.35872 0.00148  -0.02294 -0.15220 72 TRP A CA  
557  C C   . TRP A 73 ? 0.25419 0.27483 0.35530 0.00002  -0.02399 -0.15412 72 TRP A C   
558  O O   . TRP A 73 ? 0.20903 0.23027 0.31294 0.00198  -0.02965 -0.15479 72 TRP A O   
559  C CB  . TRP A 73 ? 0.20445 0.23119 0.31049 0.00342  -0.02363 -0.15599 72 TRP A CB  
560  C CG  . TRP A 73 ? 0.20509 0.23857 0.31463 0.00112  -0.01908 -0.16028 72 TRP A CG  
561  C CD1 . TRP A 73 ? 0.20634 0.23940 0.31226 -0.00182 -0.01267 -0.16063 72 TRP A CD1 
562  C CD2 . TRP A 73 ? 0.20494 0.24651 0.32314 0.00163  -0.02059 -0.16509 72 TRP A CD2 
563  N NE1 . TRP A 73 ? 0.20705 0.24733 0.31840 -0.00347 -0.00963 -0.16527 72 TRP A NE1 
564  C CE2 . TRP A 73 ? 0.20593 0.25188 0.32551 -0.00138 -0.01441 -0.16824 72 TRP A CE2 
565  C CE3 . TRP A 73 ? 0.20456 0.24983 0.33003 0.00435  -0.02664 -0.16721 72 TRP A CE3 
566  C CZ2 . TRP A 73 ? 0.20604 0.26047 0.33484 -0.00186 -0.01385 -0.17364 72 TRP A CZ2 
567  C CZ3 . TRP A 73 ? 0.20470 0.25831 0.33952 0.00421  -0.02661 -0.17256 72 TRP A CZ3 
568  C CH2 . TRP A 73 ? 0.21214 0.27058 0.34901 0.00106  -0.02010 -0.17588 72 TRP A CH2 
569  N N   . THR A 74 ? 0.27891 0.30010 0.37816 -0.00346 -0.01870 -0.15509 73 THR A N   
570  C CA  . THR A 74 ? 0.41751 0.44157 0.51873 -0.00555 -0.01857 -0.15775 73 THR A CA  
571  C C   . THR A 74 ? 0.21490 0.24662 0.32139 -0.00731 -0.01361 -0.16183 73 THR A C   
572  O O   . THR A 74 ? 0.30955 0.33959 0.41260 -0.00930 -0.00775 -0.16084 73 THR A O   
573  C CB  . THR A 74 ? 0.38859 0.40466 0.48167 -0.00882 -0.01574 -0.15482 73 THR A CB  
574  O OG1 . THR A 74 ? 0.56057 0.56830 0.64786 -0.00763 -0.01827 -0.15066 73 THR A OG1 
575  C CG2 . THR A 74 ? 0.34498 0.36248 0.43880 -0.01064 -0.01761 -0.15721 73 THR A CG2 
576  N N   . PRO A 75 ? 0.33456 0.37434 0.44963 -0.00678 -0.01553 -0.16656 74 PRO A N   
577  C CA  . PRO A 75 ? 0.29342 0.34027 0.41388 -0.00904 -0.00994 -0.17081 74 PRO A CA  
578  C C   . PRO A 75 ? 0.30106 0.34453 0.41638 -0.01341 -0.00393 -0.16979 74 PRO A C   
579  O O   . PRO A 75 ? 0.32870 0.36674 0.43904 -0.01476 -0.00512 -0.16754 74 PRO A O   
580  C CB  . PRO A 75 ? 0.33740 0.39268 0.46897 -0.00772 -0.01399 -0.17608 74 PRO A CB  
581  C CG  . PRO A 75 ? 0.43151 0.48435 0.56357 -0.00393 -0.02206 -0.17446 74 PRO A CG  
582  C CD  . PRO A 75 ? 0.25945 0.30188 0.38009 -0.00431 -0.02277 -0.16848 74 PRO A CD  
583  N N   . SER A 76 ? 0.22444 0.27030 0.34022 -0.01581 0.00285  -0.17135 75 SER A N   
584  C CA  . SER A 76 ? 0.24296 0.28704 0.35611 -0.02009 0.00899  -0.17135 75 SER A CA  
585  C C   . SER A 76 ? 0.21546 0.26730 0.33746 -0.02175 0.00908  -0.17661 75 SER A C   
586  O O   . SER A 76 ? 0.22903 0.28794 0.35983 -0.01950 0.00490  -0.18047 75 SER A O   
587  C CB  . SER A 76 ? 0.22787 0.27083 0.33789 -0.02216 0.01622  -0.17104 75 SER A CB  
588  O OG  . SER A 76 ? 0.21569 0.26689 0.33306 -0.02233 0.01825  -0.17604 75 SER A OG  
589  N N   . VAL A 77 ? 0.23757 0.28829 0.35823 -0.02571 0.01394  -0.17707 76 VAL A N   
590  C CA  . VAL A 77 ? 0.21892 0.27724 0.34876 -0.02754 0.01419  -0.18244 76 VAL A CA  
591  C C   . VAL A 77 ? 0.21777 0.28506 0.35715 -0.02791 0.01800  -0.18762 76 VAL A C   
592  O O   . VAL A 77 ? 0.21731 0.29299 0.36787 -0.02717 0.01555  -0.19293 76 VAL A O   
593  C CB  . VAL A 77 ? 0.22208 0.27709 0.34845 -0.03198 0.01900  -0.18195 76 VAL A CB  
594  C CG1 . VAL A 77 ? 0.23315 0.29584 0.36933 -0.03355 0.01800  -0.18759 76 VAL A CG1 
595  C CG2 . VAL A 77 ? 0.40529 0.45074 0.52155 -0.03185 0.01596  -0.17699 76 VAL A CG2 
596  N N   . SER A 78 ? 0.21816 0.28342 0.35326 -0.02914 0.02406  -0.18636 77 SER A N   
597  C CA  . SER A 78 ? 0.21852 0.29101 0.36080 -0.02967 0.02794  -0.19108 77 SER A CA  
598  C C   . SER A 78 ? 0.22173 0.29923 0.37036 -0.02528 0.02180  -0.19325 77 SER A C   
599  O O   . SER A 78 ? 0.21678 0.30318 0.37692 -0.02521 0.02237  -0.19915 77 SER A O   
600  C CB  . SER A 78 ? 0.30910 0.37633 0.44274 -0.03170 0.03492  -0.18866 77 SER A CB  
601  O OG  . SER A 78 ? 0.39904 0.46248 0.52890 -0.03598 0.04125  -0.18746 77 SER A OG  
602  N N   . ASP A 79 ? 0.21436 0.28640 0.35667 -0.02166 0.01612  -0.18884 78 ASP A N   
603  C CA  . ASP A 79 ? 0.25961 0.33589 0.40831 -0.01729 0.00971  -0.19065 78 ASP A CA  
604  C C   . ASP A 79 ? 0.21124 0.29403 0.37121 -0.01586 0.00421  -0.19473 78 ASP A C   
605  O O   . ASP A 79 ? 0.21029 0.30116 0.38192 -0.01391 0.00226  -0.19987 78 ASP A O   
606  C CB  . ASP A 79 ? 0.21079 0.27937 0.35086 -0.01399 0.00436  -0.18493 78 ASP A CB  
607  C CG  . ASP A 79 ? 0.25796 0.32029 0.38806 -0.01451 0.00824  -0.18125 78 ASP A CG  
608  O OD1 . ASP A 79 ? 0.21416 0.27887 0.34436 -0.01610 0.01362  -0.18365 78 ASP A OD1 
609  O OD2 . ASP A 79 ? 0.25834 0.31293 0.38039 -0.01325 0.00562  -0.17605 78 ASP A OD2 
610  N N   . ILE A 80 ? 0.21356 0.29231 0.36997 -0.01667 0.00130  -0.19252 79 ILE A N   
611  C CA  . ILE A 80 ? 0.21319 0.29647 0.37840 -0.01536 -0.00483 -0.19592 79 ILE A CA  
612  C C   . ILE A 80 ? 0.31179 0.40555 0.49097 -0.01719 -0.00135 -0.20328 79 ILE A C   
613  O O   . ILE A 80 ? 0.24646 0.34730 0.43808 -0.01466 -0.00624 -0.20806 79 ILE A O   
614  C CB  . ILE A 80 ? 0.21632 0.29206 0.37259 -0.01717 -0.00717 -0.19217 79 ILE A CB  
615  C CG1 . ILE A 80 ? 0.24914 0.31477 0.39314 -0.01531 -0.01075 -0.18553 79 ILE A CG1 
616  C CG2 . ILE A 80 ? 0.21915 0.29875 0.38314 -0.01646 -0.01355 -0.19573 79 ILE A CG2 
617  C CD1 . ILE A 80 ? 0.22910 0.29491 0.37611 -0.01083 -0.01905 -0.18527 79 ILE A CD1 
618  N N   . LEU A 81 ? 0.21446 0.30919 0.39258 -0.02165 0.00714  -0.20447 80 LEU A N   
619  C CA  . LEU A 81 ? 0.21530 0.31939 0.40661 -0.02419 0.01116  -0.21145 80 LEU A CA  
620  C C   . LEU A 81 ? 0.23899 0.35065 0.43959 -0.02418 0.01583  -0.21640 80 LEU A C   
621  O O   . LEU A 81 ? 0.27538 0.39602 0.48968 -0.02588 0.01888  -0.22316 80 LEU A O   
622  C CB  . LEU A 81 ? 0.21773 0.31891 0.40384 -0.02948 0.01844  -0.21058 80 LEU A CB  
623  C CG  . LEU A 81 ? 0.22002 0.31524 0.39946 -0.03036 0.01446  -0.20745 80 LEU A CG  
624  C CD1 . LEU A 81 ? 0.22251 0.31545 0.39821 -0.03577 0.02255  -0.20720 80 LEU A CD1 
625  C CD2 . LEU A 81 ? 0.22131 0.32257 0.41190 -0.02843 0.00705  -0.21201 80 LEU A CD2 
626  N N   . ALA A 82 ? 0.27291 0.38096 0.46649 -0.02250 0.01652  -0.21342 81 ALA A N   
627  C CA  . ALA A 82 ? 0.21459 0.32766 0.41327 -0.02334 0.02197  -0.21736 81 ALA A CA  
628  C C   . ALA A 82 ? 0.29407 0.41680 0.50920 -0.02002 0.01756  -0.22372 81 ALA A C   
629  O O   . ALA A 82 ? 0.29314 0.41690 0.51325 -0.01580 0.00897  -0.22367 81 ALA A O   
630  C CB  . ALA A 82 ? 0.26177 0.36699 0.44663 -0.02233 0.02317  -0.21203 81 ALA A CB  
631  N N   . GLU A 83 ? 0.21471 0.34396 0.43820 -0.02211 0.02377  -0.22928 82 GLU A N   
632  C CA  . GLU A 83 ? 0.21344 0.35217 0.45383 -0.01932 0.02076  -0.23596 82 GLU A CA  
633  C C   . GLU A 83 ? 0.39428 0.53256 0.63156 -0.01948 0.02484  -0.23673 82 GLU A C   
634  O O   . GLU A 83 ? 0.27289 0.41923 0.52359 -0.02016 0.02769  -0.24353 82 GLU A O   
635  C CB  . GLU A 83 ? 0.23610 0.38527 0.49471 -0.02180 0.02388  -0.24404 82 GLU A CB  
636  C CG  . GLU A 83 ? 0.28366 0.43189 0.54264 -0.02246 0.02099  -0.24303 82 GLU A CG  
637  C CD  . GLU A 83 ? 0.35246 0.51096 0.63226 -0.02082 0.01721  -0.25072 82 GLU A CD  
638  O OE1 . GLU A 83 ? 0.52342 0.69049 0.81902 -0.01918 0.01720  -0.25716 82 GLU A OE1 
639  O OE2 . GLU A 83 ? 0.32125 0.47870 0.60143 -0.02111 0.01401  -0.25028 82 GLU A OE2 
640  N N   . ASP A 84 ? 0.22501 0.35353 0.44461 -0.01894 0.02514  -0.22995 83 ASP A N   
641  C CA  . ASP A 84 ? 0.22138 0.34739 0.43461 -0.01881 0.02836  -0.22976 83 ASP A CA  
642  C C   . ASP A 84 ? 0.22217 0.34343 0.42937 -0.01368 0.02054  -0.22537 83 ASP A C   
643  O O   . ASP A 84 ? 0.24083 0.35579 0.43591 -0.01348 0.02229  -0.22217 83 ASP A O   
644  C CB  . ASP A 84 ? 0.31004 0.42819 0.50715 -0.02317 0.03684  -0.22626 83 ASP A CB  
645  C CG  . ASP A 84 ? 0.28424 0.39286 0.46672 -0.02305 0.03488  -0.21856 83 ASP A CG  
646  O OD1 . ASP A 84 ? 0.22054 0.32860 0.40500 -0.02013 0.02757  -0.21604 83 ASP A OD1 
647  O OD2 . ASP A 84 ? 0.28207 0.38325 0.45093 -0.02588 0.04063  -0.21505 83 ASP A OD2 
648  N N   . TRP A 85 ? 0.21372 0.33749 0.42906 -0.00952 0.01184  -0.22524 84 TRP A N   
649  C CA  . TRP A 85 ? 0.21152 0.33106 0.42277 -0.00469 0.00434  -0.22142 84 TRP A CA  
650  C C   . TRP A 85 ? 0.29226 0.41755 0.51357 -0.00245 0.00349  -0.22644 84 TRP A C   
651  O O   . TRP A 85 ? 0.29850 0.43312 0.53584 -0.00303 0.00513  -0.23368 84 TRP A O   
652  C CB  . TRP A 85 ? 0.20752 0.32657 0.42305 -0.00116 -0.00448 -0.21945 84 TRP A CB  
653  C CG  . TRP A 85 ? 0.23056 0.34181 0.43362 -0.00294 -0.00461 -0.21338 84 TRP A CG  
654  C CD1 . TRP A 85 ? 0.20875 0.32131 0.41356 -0.00588 -0.00247 -0.21437 84 TRP A CD1 
655  C CD2 . TRP A 85 ? 0.20686 0.30768 0.39436 -0.00212 -0.00677 -0.20567 84 TRP A CD2 
656  N NE1 . TRP A 85 ? 0.20774 0.31113 0.39866 -0.00699 -0.00307 -0.20772 84 TRP A NE1 
657  C CE2 . TRP A 85 ? 0.20715 0.30338 0.38777 -0.00472 -0.00562 -0.20239 84 TRP A CE2 
658  C CE3 . TRP A 85 ? 0.20654 0.30162 0.38607 0.00046  -0.00950 -0.20153 84 TRP A CE3 
659  C CZ2 . TRP A 85 ? 0.23045 0.31667 0.39706 -0.00488 -0.00674 -0.19532 84 TRP A CZ2 
660  C CZ3 . TRP A 85 ? 0.20621 0.29162 0.37229 0.00042  -0.01090 -0.19452 84 TRP A CZ3 
661  C CH2 . TRP A 85 ? 0.20649 0.28760 0.36645 -0.00229 -0.00931 -0.19156 84 TRP A CH2 
662  N N   . ASN A 86 ? 0.22886 0.34857 0.44149 0.00002  0.00091  -0.22284 85 ASN A N   
663  C CA  . ASN A 86 ? 0.37620 0.50017 0.59730 0.00254  -0.00077 -0.22696 85 ASN A CA  
664  C C   . ASN A 86 ? 0.38258 0.50165 0.60010 0.00742  -0.00913 -0.22239 85 ASN A C   
665  O O   . ASN A 86 ? 0.29381 0.40414 0.49705 0.00771  -0.01077 -0.21550 85 ASN A O   
666  C CB  . ASN A 86 ? 0.46544 0.58727 0.67828 -0.00055 0.00719  -0.22844 85 ASN A CB  
667  C CG  . ASN A 86 ? 0.48870 0.61343 0.70230 -0.00595 0.01651  -0.23212 85 ASN A CG  
668  O OD1 . ASN A 86 ? 0.71201 0.83001 0.91067 -0.00921 0.02255  -0.22901 85 ASN A OD1 
669  N ND2 . ASN A 86 ? 0.62859 0.76315 0.86006 -0.00688 0.01759  -0.23888 85 ASN A ND2 
670  N N   . ILE A 87 ? 0.23643 0.36119 0.46796 0.01116  -0.01436 -0.22644 86 ILE A N   
671  C CA  . ILE A 87 ? 0.24113 0.36158 0.47035 0.01563  -0.02147 -0.22296 86 ILE A CA  
672  C C   . ILE A 87 ? 0.31027 0.42621 0.52888 0.01474  -0.01776 -0.22172 86 ILE A C   
673  O O   . ILE A 87 ? 0.32467 0.44400 0.54515 0.01218  -0.01138 -0.22647 86 ILE A O   
674  C CB  . ILE A 87 ? 0.30923 0.43717 0.55775 0.01989  -0.02802 -0.22822 86 ILE A CB  
675  C CG1 . ILE A 87 ? 0.30214 0.43213 0.55830 0.02145  -0.03312 -0.22837 86 ILE A CG1 
676  C CG2 . ILE A 87 ? 0.30433 0.42824 0.55161 0.02422  -0.03442 -0.22551 86 ILE A CG2 
677  C CD1 . ILE A 87 ? 0.54584 0.68433 0.82358 0.02537  -0.03895 -0.23500 86 ILE A CD1 
678  N N   . VAL A 88 ? 0.23029 0.33802 0.43729 0.01668  -0.02158 -0.21540 87 VAL A N   
679  C CA  . VAL A 88 ? 0.39132 0.49336 0.58660 0.01615  -0.01919 -0.21341 87 VAL A CA  
680  C C   . VAL A 88 ? 0.32890 0.43157 0.53083 0.02044  -0.02536 -0.21416 87 VAL A C   
681  O O   . VAL A 88 ? 0.32770 0.42854 0.53279 0.02391  -0.03255 -0.21096 87 VAL A O   
682  C CB  . VAL A 88 ? 0.37834 0.47047 0.55621 0.01496  -0.01890 -0.20588 87 VAL A CB  
683  C CG1 . VAL A 88 ? 0.41129 0.49745 0.57881 0.01549  -0.01875 -0.20390 87 VAL A CG1 
684  C CG2 . VAL A 88 ? 0.37281 0.46354 0.54314 0.01048  -0.01207 -0.20530 87 VAL A CG2 
685  N N   . GLU A 89 ? 0.43236 0.53694 0.63583 0.02005  -0.02234 -0.21839 88 GLU A N   
686  C CA  . GLU A 89 ? 0.42874 0.53262 0.63609 0.02360  -0.02726 -0.21886 88 GLU A CA  
687  C C   . GLU A 89 ? 0.54642 0.64065 0.73837 0.02430  -0.02946 -0.21218 88 GLU A C   
688  O O   . GLU A 89 ? 0.54729 0.63837 0.74012 0.02754  -0.03613 -0.20810 88 GLU A O   
689  C CB  . GLU A 89 ? 0.47764 0.58587 0.69026 0.02242  -0.02253 -0.22569 88 GLU A CB  
690  C CG  . GLU A 89 ? 0.60180 0.72048 0.83436 0.02276  -0.02202 -0.23327 88 GLU A CG  
691  C CD  . GLU A 89 ? 0.75396 0.87585 0.99138 0.02164  -0.01731 -0.23987 88 GLU A CD  
692  O OE1 . GLU A 89 ? 0.76312 0.87865 0.98632 0.02019  -0.01374 -0.23847 88 GLU A OE1 
693  O OE2 . GLU A 89 ? 0.61688 0.74726 0.87225 0.02215  -0.01726 -0.24659 88 GLU A OE2 
694  N N   . ASP B 3  ? 0.75165 0.75123 0.47518 -0.01521 -0.01542 -0.01169 2  ASP B N   
695  C CA  . ASP B 3  ? 0.72284 0.72859 0.44579 -0.00040 -0.03869 -0.00584 2  ASP B CA  
696  C C   . ASP B 3  ? 0.69469 0.72096 0.44416 0.00276  -0.03869 -0.01994 2  ASP B C   
697  O O   . ASP B 3  ? 0.68437 0.74482 0.45932 0.01124  -0.05425 -0.01977 2  ASP B O   
698  C CB  . ASP B 3  ? 0.53847 0.55171 0.28543 0.01808  -0.03920 0.00455  2  ASP B CB  
699  C CG  . ASP B 3  ? 0.90170 0.89634 0.63145 0.01401  -0.03097 0.01622  2  ASP B CG  
700  O OD1 . ASP B 3  ? 1.11013 1.10885 0.81466 0.00400  -0.03398 0.02231  2  ASP B OD1 
701  O OD2 . ASP B 3  ? 0.55536 0.54011 0.30005 0.02307  -0.02068 0.01863  2  ASP B OD2 
702  N N   . SER B 4  ? 0.61798 0.62730 0.36533 -0.00269 -0.02155 -0.03182 3  SER B N   
703  C CA  . SER B 4  ? 0.50220 0.52849 0.27327 -0.00691 -0.01876 -0.04382 3  SER B CA  
704  C C   . SER B 4  ? 0.46993 0.52272 0.27793 -0.00023 -0.01698 -0.04289 3  SER B C   
705  O O   . SER B 4  ? 0.42326 0.51057 0.25174 -0.00186 -0.02707 -0.04809 3  SER B O   
706  C CB  . SER B 4  ? 0.59940 0.64378 0.36288 -0.01722 -0.03600 -0.05059 3  SER B CB  
707  O OG  . SER B 4  ? 0.78013 0.85569 0.55477 -0.01270 -0.05791 -0.04273 3  SER B OG  
708  N N   . LEU B 5  ? 0.27114 0.30956 0.08866 0.00687  -0.00349 -0.03765 4  LEU B N   
709  C CA  . LEU B 5  ? 0.26304 0.31724 0.11024 0.01389  0.00180  -0.03785 4  LEU B CA  
710  C C   . LEU B 5  ? 0.26774 0.30661 0.12275 0.00624  0.01407  -0.04303 4  LEU B C   
711  O O   . LEU B 5  ? 0.25617 0.26826 0.09722 0.00378  0.02122  -0.04470 4  LEU B O   
712  C CB  . LEU B 5  ? 0.23445 0.27879 0.08662 0.02470  0.00665  -0.02860 4  LEU B CB  
713  C CG  . LEU B 5  ? 0.33239 0.37756 0.16740 0.03495  -0.00597 -0.01941 4  LEU B CG  
714  C CD1 . LEU B 5  ? 0.30061 0.32762 0.13601 0.04220  0.00136  -0.01113 4  LEU B CD1 
715  C CD2 . LEU B 5  ? 0.33346 0.41237 0.18019 0.04837  -0.02446 -0.02033 4  LEU B CD2 
716  N N   . ASN B 6  ? 0.25450 0.31181 0.13032 0.00494  0.01586  -0.04569 5  ASN B N   
717  C CA  . ASN B 6  ? 0.23312 0.27261 0.11253 -0.00030 0.02502  -0.04623 5  ASN B CA  
718  C C   . ASN B 6  ? 0.24167 0.26235 0.12656 0.00787  0.03193  -0.03721 5  ASN B C   
719  O O   . ASN B 6  ? 0.19747 0.21939 0.08586 0.01295  0.03112  -0.03255 5  ASN B O   
720  C CB  . ASN B 6  ? 0.20921 0.27262 0.10164 -0.01220 0.02532  -0.05234 5  ASN B CB  
721  C CG  . ASN B 6  ? 0.21739 0.30818 0.13007 -0.00660 0.02633  -0.05099 5  ASN B CG  
722  O OD1 . ASN B 6  ? 0.24280 0.32141 0.15986 0.00404  0.02935  -0.04360 5  ASN B OD1 
723  N ND2 . ASN B 6  ? 0.21113 0.34099 0.13736 -0.01551 0.02489  -0.06058 5  ASN B ND2 
724  N N   . PHE B 7  ? 0.27558 0.28394 0.16168 0.00775  0.03671  -0.03584 6  PHE B N   
725  C CA  . PHE B 7  ? 0.20241 0.19739 0.09666 0.01025  0.04077  -0.02900 6  PHE B CA  
726  C C   . PHE B 7  ? 0.20665 0.21191 0.11138 0.00899  0.04063  -0.02605 6  PHE B C   
727  O O   . PHE B 7  ? 0.17949 0.18832 0.09458 0.00829  0.04033  -0.02437 6  PHE B O   
728  C CB  . PHE B 7  ? 0.19421 0.19868 0.09322 0.01174  0.04095  -0.03338 6  PHE B CB  
729  C CG  . PHE B 7  ? 0.18550 0.18524 0.09390 0.01374  0.04330  -0.02862 6  PHE B CG  
730  C CD1 . PHE B 7  ? 0.18347 0.18239 0.09918 0.01820  0.04574  -0.02947 6  PHE B CD1 
731  C CD2 . PHE B 7  ? 0.18949 0.18512 0.09475 0.01203  0.04311  -0.02238 6  PHE B CD2 
732  C CE1 . PHE B 7  ? 0.21566 0.21199 0.13872 0.02321  0.04782  -0.02464 6  PHE B CE1 
733  C CE2 . PHE B 7  ? 0.19110 0.18162 0.09932 0.01708  0.04399  -0.01703 6  PHE B CE2 
734  C CZ  . PHE B 7  ? 0.22265 0.21477 0.14174 0.02402  0.04649  -0.01833 6  PHE B CZ  
735  N N   . GLY B 8  ? 0.20168 0.22387 0.10975 0.00832  0.03922  -0.02808 7  GLY B N   
736  C CA  . GLY B 8  ? 0.18516 0.21742 0.10393 0.00967  0.04047  -0.02737 7  GLY B CA  
737  C C   . GLY B 8  ? 0.17557 0.21445 0.10069 0.01795  0.03773  -0.02806 7  GLY B C   
738  O O   . GLY B 8  ? 0.19803 0.23115 0.12675 0.02031  0.03928  -0.02647 7  GLY B O   
739  N N   . LYS B 9  ? 0.21469 0.26611 0.13685 0.02344  0.03231  -0.03046 8  LYS B N   
740  C CA  . LYS B 9  ? 0.25483 0.31142 0.17430 0.03699  0.02737  -0.02871 8  LYS B CA  
741  C C   . LYS B 9  ? 0.28760 0.31947 0.19616 0.03522  0.02881  -0.02159 8  LYS B C   
742  O O   . LYS B 9  ? 0.22199 0.24723 0.12629 0.04408  0.02821  -0.01768 8  LYS B O   
743  C CB  . LYS B 9  ? 0.21687 0.29689 0.12893 0.04465  0.01789  -0.03288 8  LYS B CB  
744  C CG  . LYS B 9  ? 0.22978 0.34988 0.16408 0.04702  0.01505  -0.04326 8  LYS B CG  
745  C CD  . LYS B 9  ? 0.49857 0.62924 0.45550 0.05847  0.02006  -0.04701 8  LYS B CD  
746  C CE  . LYS B 9  ? 0.66183 0.83452 0.65114 0.05510  0.02201  -0.05886 8  LYS B CE  
747  N NZ  . LYS B 9  ? 0.65654 0.83562 0.66721 0.06381  0.03019  -0.06525 8  LYS B NZ  
748  N N   . ALA B 10 ? 0.16614 0.18626 0.06996 0.02467  0.03186  -0.02157 9  ALA B N   
749  C CA  . ALA B 10 ? 0.16100 0.17095 0.06326 0.02178  0.03500  -0.01836 9  ALA B CA  
750  C C   . ALA B 10 ? 0.17653 0.18522 0.09125 0.02101  0.03694  -0.01659 9  ALA B C   
751  O O   . ALA B 10 ? 0.19332 0.19713 0.10567 0.02299  0.03823  -0.01300 9  ALA B O   
752  C CB  . ALA B 10 ? 0.16468 0.17248 0.06492 0.01397  0.03914  -0.02301 9  ALA B CB  
753  N N   . LEU B 11 ? 0.15676 0.16845 0.07944 0.01700  0.03757  -0.01888 10 LEU B N   
754  C CA  . LEU B 11 ? 0.18374 0.19508 0.11191 0.01512  0.03823  -0.01763 10 LEU B CA  
755  C C   . LEU B 11 ? 0.15063 0.16088 0.07771 0.01991  0.03838  -0.01778 10 LEU B C   
756  O O   . LEU B 11 ? 0.17916 0.18518 0.10475 0.02013  0.03929  -0.01624 10 LEU B O   
757  C CB  . LEU B 11 ? 0.17804 0.19109 0.10565 0.00889  0.03925  -0.01918 10 LEU B CB  
758  C CG  . LEU B 11 ? 0.16602 0.17979 0.09224 0.00616  0.03879  -0.01735 10 LEU B CG  
759  C CD1 . LEU B 11 ? 0.17913 0.18997 0.10529 0.01099  0.03883  -0.01303 10 LEU B CD1 
760  C CD2 . LEU B 11 ? 0.20613 0.22257 0.12611 0.00011  0.03778  -0.01602 10 LEU B CD2 
761  N N   . GLU B 12 ? 0.14149 0.15652 0.06843 0.02600  0.03840  -0.02074 11 GLU B N   
762  C CA  . GLU B 12 ? 0.15736 0.17049 0.08284 0.03667  0.03943  -0.02293 11 GLU B CA  
763  C C   . GLU B 12 ? 0.19764 0.19455 0.10832 0.04555  0.03829  -0.01636 11 GLU B C   
764  O O   . GLU B 12 ? 0.23347 0.21545 0.13682 0.04883  0.04130  -0.01622 11 GLU B O   
765  C CB  . GLU B 12 ? 0.19278 0.22189 0.12511 0.04799  0.03856  -0.02871 11 GLU B CB  
766  C CG  . GLU B 12 ? 0.48661 0.52197 0.43051 0.04958  0.04448  -0.03786 11 GLU B CG  
767  C CD  . GLU B 12 ? 0.81701 0.88014 0.77772 0.05374  0.04533  -0.04544 11 GLU B CD  
768  O OE1 . GLU B 12 ? 0.51885 0.60018 0.48406 0.06470  0.03779  -0.04576 11 GLU B OE1 
769  O OE2 . GLU B 12 ? 0.78487 0.85437 0.75254 0.04603  0.05354  -0.05134 11 GLU B OE2 
770  N N   . ALA B 13 ? 0.17576 0.17078 0.07639 0.04726  0.03559  -0.01125 12 ALA B N   
771  C CA  . ALA B 13 ? 0.23054 0.20566 0.10928 0.05080  0.03668  -0.00340 12 ALA B CA  
772  C C   . ALA B 13 ? 0.25182 0.22134 0.13491 0.03889  0.04229  -0.00192 12 ALA B C   
773  O O   . ALA B 13 ? 0.23174 0.18038 0.09810 0.04019  0.04639  0.00268  12 ALA B O   
774  C CB  . ALA B 13 ? 0.21295 0.19058 0.07976 0.04800  0.03314  -0.00001 12 ALA B CB  
775  N N   . LEU B 14 ? 0.16605 0.15138 0.06728 0.02867  0.04259  -0.00566 13 LEU B N   
776  C CA  . LEU B 14 ? 0.16274 0.14969 0.06874 0.02192  0.04688  -0.00503 13 LEU B CA  
777  C C   . LEU B 14 ? 0.18078 0.15856 0.08259 0.02219  0.04859  -0.00551 13 LEU B C   
778  O O   . LEU B 14 ? 0.21962 0.18462 0.11057 0.01842  0.05438  -0.00241 13 LEU B O   
779  C CB  . LEU B 14 ? 0.19134 0.19249 0.11240 0.01798  0.04616  -0.00871 13 LEU B CB  
780  C CG  . LEU B 14 ? 0.20468 0.21111 0.12736 0.01680  0.04888  -0.01089 13 LEU B CG  
781  C CD1 . LEU B 14 ? 0.13979 0.15065 0.07204 0.01801  0.04845  -0.01460 13 LEU B CD1 
782  C CD2 . LEU B 14 ? 0.18814 0.19850 0.10974 0.01414  0.05685  -0.00980 13 LEU B CD2 
783  N N   . LYS B 15 ? 0.17106 0.15389 0.07877 0.02370  0.04540  -0.01059 14 LYS B N   
784  C CA  . LYS B 15 ? 0.20365 0.17813 0.10502 0.02226  0.04773  -0.01472 14 LYS B CA  
785  C C   . LYS B 15 ? 0.22143 0.16678 0.10362 0.02982  0.05254  -0.01506 14 LYS B C   
786  O O   . LYS B 15 ? 0.24861 0.17541 0.11866 0.02528  0.05692  -0.01931 14 LYS B O   
787  C CB  . LYS B 15 ? 0.22878 0.21773 0.13893 0.02027  0.04531  -0.02193 14 LYS B CB  
788  C CG  . LYS B 15 ? 0.15575 0.16073 0.07239 0.01215  0.04199  -0.02025 14 LYS B CG  
789  C CD  . LYS B 15 ? 0.22180 0.23860 0.14025 0.00872  0.04084  -0.02549 14 LYS B CD  
790  C CE  . LYS B 15 ? 0.19343 0.21491 0.10703 0.00867  0.03667  -0.01797 14 LYS B CE  
791  N NZ  . LYS B 15 ? 0.18281 0.19514 0.08526 0.01087  0.04012  -0.01757 14 LYS B NZ  
792  N N   . GLU B 16 ? 0.20443 0.18643 0.11219 0.02233  0.05652  -0.04426 15 GLU B N   
793  C CA  . GLU B 16 ? 0.22913 0.20158 0.12295 0.02898  0.05539  -0.04167 15 GLU B CA  
794  C C   . GLU B 16 ? 0.29570 0.25449 0.17812 0.02660  0.05603  -0.03833 15 GLU B C   
795  O O   . GLU B 16 ? 0.28356 0.22748 0.14943 0.03183  0.05613  -0.03481 15 GLU B O   
796  C CB  . GLU B 16 ? 0.21633 0.19952 0.10797 0.03867  0.05240  -0.04645 15 GLU B CB  
797  C CG  . GLU B 16 ? 0.21864 0.21514 0.12328 0.04083  0.05417  -0.05059 15 GLU B CG  
798  C CD  . GLU B 16 ? 0.43553 0.45468 0.34964 0.04995  0.04960  -0.05939 15 GLU B CD  
799  O OE1 . GLU B 16 ? 0.34597 0.37071 0.25442 0.05658  0.04287  -0.06269 15 GLU B OE1 
800  O OE2 . GLU B 16 ? 0.37747 0.41060 0.30678 0.04968  0.05255  -0.06429 15 GLU B OE2 
801  N N   . GLY B 17 ? 0.24227 0.20349 0.13210 0.01922  0.05732  -0.03940 16 GLY B N   
802  C CA  . GLY B 17 ? 0.22262 0.17201 0.10477 0.01505  0.06048  -0.03774 16 GLY B CA  
803  C C   . GLY B 17 ? 0.33563 0.28400 0.20856 0.01684  0.06017  -0.03857 16 GLY B C   
804  O O   . GLY B 17 ? 0.34780 0.28162 0.20916 0.01426  0.06437  -0.03645 16 GLY B O   
805  N N   . LYS B 18 ? 0.28417 0.24614 0.16082 0.02056  0.05626  -0.04253 17 LYS B N   
806  C CA  . LYS B 18 ? 0.24341 0.20492 0.11019 0.02286  0.05478  -0.04464 17 LYS B CA  
807  C C   . LYS B 18 ? 0.27748 0.24660 0.15587 0.01583  0.05630  -0.04728 17 LYS B C   
808  O O   . LYS B 18 ? 0.27539 0.25130 0.16962 0.01111  0.05686  -0.04795 17 LYS B O   
809  C CB  . LYS B 18 ? 0.23951 0.21195 0.10376 0.03164  0.04881  -0.04983 17 LYS B CB  
810  C CG  . LYS B 18 ? 0.25322 0.21960 0.10623 0.04329  0.04480  -0.04737 17 LYS B CG  
811  C CD  . LYS B 18 ? 0.30355 0.28970 0.16114 0.05459  0.03594  -0.05538 17 LYS B CD  
812  C CE  . LYS B 18 ? 0.39933 0.38103 0.24477 0.07006  0.02984  -0.05407 17 LYS B CE  
813  N NZ  . LYS B 18 ? 0.61601 0.62759 0.47603 0.08101  0.02008  -0.06588 17 LYS B NZ  
814  N N   . LYS B 19 ? 0.26966 0.23428 0.13735 0.01640  0.05652  -0.04825 18 LYS B N   
815  C CA  . LYS B 19 ? 0.25825 0.22861 0.13423 0.01161  0.05752  -0.05100 18 LYS B CA  
816  C C   . LYS B 19 ? 0.22650 0.20954 0.10503 0.01517  0.05245  -0.05719 18 LYS B C   
817  O O   . LYS B 19 ? 0.24499 0.23230 0.11390 0.02071  0.04849  -0.06174 18 LYS B O   
818  C CB  . LYS B 19 ? 0.24827 0.20496 0.10986 0.00990  0.06186  -0.04919 18 LYS B CB  
819  C CG  . LYS B 19 ? 0.31292 0.25330 0.16962 0.00489  0.06936  -0.04474 18 LYS B CG  
820  C CD  . LYS B 19 ? 0.34980 0.27446 0.19256 0.00120  0.07650  -0.04382 18 LYS B CD  
821  C CE  . LYS B 19 ? 0.54531 0.44945 0.35802 0.00901  0.07589  -0.03980 18 LYS B CE  
822  N NZ  . LYS B 19 ? 0.92953 0.81200 0.72839 0.00927  0.08075  -0.03452 18 LYS B NZ  
823  N N   . VAL B 20 ? 0.21922 0.20772 0.11199 0.00932  0.05315  -0.05910 19 VAL B N   
824  C CA  . VAL B 20 ? 0.22139 0.22025 0.12032 0.00808  0.05000  -0.06577 19 VAL B CA  
825  C C   . VAL B 20 ? 0.22738 0.22544 0.13003 0.00314  0.05121  -0.06759 19 VAL B C   
826  O O   . VAL B 20 ? 0.22546 0.21811 0.13218 -0.00010 0.05468  -0.06428 19 VAL B O   
827  C CB  . VAL B 20 ? 0.19883 0.20845 0.11565 0.00374  0.05026  -0.06823 19 VAL B CB  
828  C CG1 . VAL B 20 ? 0.20323 0.21616 0.11829 0.00908  0.04921  -0.06763 19 VAL B CG1 
829  C CG2 . VAL B 20 ? 0.21077 0.21424 0.13684 -0.00176 0.05372  -0.06423 19 VAL B CG2 
830  N N   . SER B 21 ? 0.22887 0.23441 0.13160 0.00256  0.04786  -0.07462 20 SER B N   
831  C CA  . SER B 21 ? 0.28110 0.28571 0.18736 -0.00218 0.04905  -0.07729 20 SER B CA  
832  C C   . SER B 21 ? 0.27020 0.28802 0.18502 -0.00574 0.04548  -0.08702 20 SER B C   
833  O O   . SER B 21 ? 0.25612 0.28760 0.17644 -0.00404 0.04143  -0.09295 20 SER B O   
834  C CB  . SER B 21 ? 0.34494 0.33904 0.23418 0.00166  0.04993  -0.07546 20 SER B CB  
835  O OG  . SER B 21 ? 0.46667 0.45836 0.33690 0.00914  0.04496  -0.07859 20 SER B OG  
836  N N   . ARG B 22 ? 0.23576 0.25143 0.15391 -0.01081 0.04712  -0.09000 21 ARG B N   
837  C CA  . ARG B 22 ? 0.22315 0.24954 0.15115 -0.01690 0.04561  -0.10017 21 ARG B CA  
838  C C   . ARG B 22 ? 0.25442 0.27942 0.17161 -0.01475 0.04175  -0.10484 21 ARG B C   
839  O O   . ARG B 22 ? 0.26546 0.27725 0.17268 -0.01311 0.04461  -0.09964 21 ARG B O   
840  C CB  . ARG B 22 ? 0.23811 0.25726 0.17592 -0.02529 0.05225  -0.09969 21 ARG B CB  
841  C CG  . ARG B 22 ? 0.27872 0.29995 0.22676 -0.02974 0.05627  -0.09966 21 ARG B CG  
842  C CD  . ARG B 22 ? 0.24015 0.24798 0.19020 -0.03731 0.06327  -0.10030 21 ARG B CD  
843  N NE  . ARG B 22 ? 0.24875 0.26183 0.20354 -0.04508 0.06458  -0.11065 21 ARG B NE  
844  C CZ  . ARG B 22 ? 0.27304 0.27153 0.22334 -0.04962 0.06917  -0.11153 21 ARG B CZ  
845  N NH1 . ARG B 22 ? 0.24152 0.22034 0.18235 -0.04557 0.07190  -0.10344 21 ARG B NH1 
846  N NH2 . ARG B 22 ? 0.24801 0.25245 0.20295 -0.05703 0.07006  -0.12167 21 ARG B NH2 
847  N N   . GLU B 23 ? 0.28172 0.32217 0.20273 -0.01467 0.03501  -0.11599 22 GLU B N   
848  C CA  . GLU B 23 ? 0.27869 0.31713 0.18922 -0.01299 0.03056  -0.12155 22 GLU B CA  
849  C C   . GLU B 23 ? 0.34054 0.36931 0.25543 -0.02135 0.03726  -0.12154 22 GLU B C   
850  O O   . GLU B 23 ? 0.31982 0.33751 0.22118 -0.01879 0.03730  -0.12033 22 GLU B O   
851  C CB  . GLU B 23 ? 0.35368 0.41517 0.27370 -0.01195 0.02067  -0.13597 22 GLU B CB  
852  C CG  . GLU B 23 ? 0.40970 0.48720 0.33201 -0.00240 0.01231  -0.13892 22 GLU B CG  
853  C CD  . GLU B 23 ? 0.73081 0.83472 0.66368 0.00247  -0.00061 -0.15488 22 GLU B CD  
854  O OE1 . GLU B 23 ? 0.88026 0.98790 0.81592 -0.00208 -0.00292 -0.16308 22 GLU B OE1 
855  O OE2 . GLU B 23 ? 0.76305 0.88490 0.70235 0.01189  -0.00902 -0.15982 22 GLU B OE2 
856  N N   . GLY B 24 ? 0.27993 0.30999 0.21089 -0.03069 0.04360  -0.12291 23 GLY B N   
857  C CA  . GLY B 24 ? 0.28726 0.30564 0.22006 -0.03787 0.04981  -0.12384 23 GLY B CA  
858  C C   . GLY B 24 ? 0.25253 0.25295 0.17762 -0.03423 0.05461  -0.11350 23 GLY B C   
859  O O   . GLY B 24 ? 0.32141 0.31039 0.24549 -0.03751 0.05894  -0.11410 23 GLY B O   
860  N N   . TRP B 25 ? 0.24727 0.24566 0.16772 -0.02725 0.05394  -0.10516 24 TRP B N   
861  C CA  . TRP B 25 ? 0.24250 0.23015 0.15983 -0.02342 0.05741  -0.09836 24 TRP B CA  
862  C C   . TRP B 25 ? 0.25419 0.23728 0.16232 -0.02124 0.05751  -0.10053 24 TRP B C   
863  O O   . TRP B 25 ? 0.32326 0.30917 0.22179 -0.01931 0.05397  -0.10380 24 TRP B O   
864  C CB  . TRP B 25 ? 0.23347 0.22254 0.14995 -0.01833 0.05730  -0.09113 24 TRP B CB  
865  C CG  . TRP B 25 ? 0.22250 0.21229 0.14720 -0.01916 0.05816  -0.08762 24 TRP B CG  
866  C CD1 . TRP B 25 ? 0.22234 0.20772 0.15236 -0.02313 0.06038  -0.08907 24 TRP B CD1 
867  C CD2 . TRP B 25 ? 0.23521 0.22685 0.16067 -0.01571 0.05778  -0.08193 24 TRP B CD2 
868  N NE1 . TRP B 25 ? 0.21439 0.19911 0.14763 -0.02152 0.06080  -0.08450 24 TRP B NE1 
869  C CE2 . TRP B 25 ? 0.20789 0.19783 0.13978 -0.01711 0.05871  -0.08036 24 TRP B CE2 
870  C CE3 . TRP B 25 ? 0.21527 0.20708 0.13420 -0.01187 0.05768  -0.07816 24 TRP B CE3 
871  C CZ2 . TRP B 25 ? 0.22129 0.21205 0.15499 -0.01438 0.05831  -0.07549 24 TRP B CZ2 
872  C CZ3 . TRP B 25 ? 0.20800 0.20013 0.12931 -0.01018 0.05802  -0.07349 24 TRP B CZ3 
873  C CH2 . TRP B 25 ? 0.21753 0.21034 0.14706 -0.01125 0.05772  -0.07236 24 TRP B CH2 
874  N N   . ASN B 26 ? 0.27643 0.25158 0.18566 -0.02017 0.06116  -0.09948 25 ASN B N   
875  C CA  . ASN B 26 ? 0.29327 0.26398 0.19472 -0.01812 0.06253  -0.10198 25 ASN B CA  
876  C C   . ASN B 26 ? 0.33587 0.30772 0.23173 -0.01381 0.06457  -0.09809 25 ASN B C   
877  O O   . ASN B 26 ? 0.44964 0.41893 0.33281 -0.01201 0.06437  -0.09976 25 ASN B O   
878  C CB  . ASN B 26 ? 0.32803 0.29029 0.23236 -0.01711 0.06568  -0.10351 25 ASN B CB  
879  C CG  . ASN B 26 ? 0.30040 0.25520 0.20471 -0.02236 0.06596  -0.10778 25 ASN B CG  
880  O OD1 . ASN B 26 ? 0.33570 0.29321 0.23801 -0.02798 0.06439  -0.11302 25 ASN B OD1 
881  N ND2 . ASN B 26 ? 0.28327 0.22753 0.18847 -0.02027 0.06816  -0.10658 25 ASN B ND2 
882  N N   . GLY B 27 ? 0.39422 0.36854 0.29802 -0.01239 0.06709  -0.09365 26 GLY B N   
883  C CA  . GLY B 27 ? 0.38390 0.35862 0.28320 -0.01105 0.07075  -0.09049 26 GLY B CA  
884  C C   . GLY B 27 ? 0.39039 0.36446 0.27816 -0.00959 0.06765  -0.08772 26 GLY B C   
885  O O   . GLY B 27 ? 0.43315 0.41108 0.32350 -0.00978 0.06283  -0.08754 26 GLY B O   
886  N N   . LYS B 28 ? 0.37946 0.34754 0.25260 -0.00749 0.07085  -0.08625 27 LYS B N   
887  C CA  . LYS B 28 ? 0.39136 0.35571 0.24735 -0.00284 0.06723  -0.08430 27 LYS B CA  
888  C C   . LYS B 28 ? 0.43034 0.38963 0.28366 -0.00382 0.07324  -0.07866 27 LYS B C   
889  O O   . LYS B 28 ? 0.41101 0.36871 0.27305 -0.00884 0.08131  -0.07781 27 LYS B O   
890  C CB  . LYS B 28 ? 0.37173 0.32942 0.20571 0.00205  0.06490  -0.08804 27 LYS B CB  
891  C CG  . LYS B 28 ? 0.47228 0.43296 0.30761 0.00186  0.05922  -0.09503 27 LYS B CG  
892  C CD  . LYS B 28 ? 0.40538 0.37470 0.25212 -0.00044 0.05237  -0.09806 27 LYS B CD  
893  C CE  . LYS B 28 ? 0.54913 0.52147 0.40233 -0.00526 0.04972  -0.10570 27 LYS B CE  
894  N NZ  . LYS B 28 ? 0.56433 0.54842 0.43248 -0.01067 0.04518  -0.11064 27 LYS B NZ  
895  N N   . GLY B 29 ? 0.35974 0.31655 0.20127 0.00067  0.06939  -0.07610 28 GLY B N   
896  C CA  . GLY B 29 ? 0.31925 0.26760 0.15639 -0.00123 0.07546  -0.07053 28 GLY B CA  
897  C C   . GLY B 29 ? 0.42599 0.38137 0.28458 -0.00604 0.07747  -0.06845 28 GLY B C   
898  O O   . GLY B 29 ? 0.38511 0.33321 0.24325 -0.00992 0.08419  -0.06541 28 GLY B O   
899  N N   . MET B 30 ? 0.33971 0.30694 0.21557 -0.00646 0.07227  -0.07057 29 MET B N   
900  C CA  . MET B 30 ? 0.26259 0.23614 0.15648 -0.00950 0.07268  -0.06924 29 MET B CA  
901  C C   . MET B 30 ? 0.30858 0.28373 0.20012 -0.00617 0.06769  -0.06633 29 MET B C   
902  O O   . MET B 30 ? 0.35659 0.33227 0.23731 -0.00133 0.06249  -0.06732 29 MET B O   
903  C CB  . MET B 30 ? 0.27947 0.26096 0.18964 -0.01100 0.07053  -0.07291 29 MET B CB  
904  C CG  . MET B 30 ? 0.26160 0.24283 0.17464 -0.01273 0.07485  -0.07698 29 MET B CG  
905  S SD  . MET B 30 ? 0.34686 0.33385 0.27540 -0.01162 0.07222  -0.08135 29 MET B SD  
906  C CE  . MET B 30 ? 0.25748 0.24209 0.17972 -0.01125 0.06634  -0.08145 29 MET B CE  
907  N N   . PHE B 31 ? 0.30273 0.27987 0.20489 -0.00826 0.06896  -0.06423 30 PHE B N   
908  C CA  . PHE B 31 ? 0.24594 0.22540 0.14821 -0.00530 0.06467  -0.06185 30 PHE B CA  
909  C C   . PHE B 31 ? 0.25140 0.23472 0.16894 -0.00785 0.06512  -0.06137 30 PHE B C   
910  O O   . PHE B 31 ? 0.26328 0.24678 0.18845 -0.01123 0.06913  -0.06306 30 PHE B O   
911  C CB  . PHE B 31 ? 0.29494 0.26574 0.17981 -0.00140 0.06536  -0.05837 30 PHE B CB  
912  C CG  . PHE B 31 ? 0.31190 0.27207 0.19382 -0.00605 0.07304  -0.05574 30 PHE B CG  
913  C CD1 . PHE B 31 ? 0.23474 0.19538 0.12651 -0.00913 0.07485  -0.05455 30 PHE B CD1 
914  C CD2 . PHE B 31 ? 0.32942 0.27754 0.19784 -0.00825 0.07941  -0.05542 30 PHE B CD2 
915  C CE1 . PHE B 31 ? 0.27766 0.22861 0.16813 -0.01540 0.08308  -0.05446 30 PHE B CE1 
916  C CE2 . PHE B 31 ? 0.34180 0.27752 0.20759 -0.01508 0.08906  -0.05435 30 PHE B CE2 
917  C CZ  . PHE B 31 ? 0.31119 0.24909 0.18893 -0.01919 0.09101  -0.05455 30 PHE B CZ  
918  N N   . ALA B 32 ? 0.24291 0.22969 0.16429 -0.00597 0.06122  -0.06040 31 ALA B N   
919  C CA  . ALA B 32 ? 0.18805 0.17596 0.11878 -0.00634 0.06071  -0.05974 31 ALA B CA  
920  C C   . ALA B 32 ? 0.23379 0.21860 0.15945 -0.00462 0.06074  -0.05608 31 ALA B C   
921  O O   . ALA B 32 ? 0.21922 0.20237 0.13458 -0.00150 0.05977  -0.05429 31 ALA B O   
922  C CB  . ALA B 32 ? 0.19307 0.18268 0.12903 -0.00584 0.05807  -0.06121 31 ALA B CB  
923  N N   . TYR B 33 ? 0.18487 0.16882 0.11660 -0.00552 0.06145  -0.05620 32 TYR B N   
924  C CA  . TYR B 33 ? 0.18686 0.16631 0.11390 -0.00440 0.06192  -0.05318 32 TYR B CA  
925  C C   . TYR B 33 ? 0.22119 0.20173 0.15596 -0.00381 0.06020  -0.05490 32 TYR B C   
926  O O   . TYR B 33 ? 0.24656 0.23066 0.18920 -0.00355 0.05893  -0.05933 32 TYR B O   
927  C CB  . TYR B 33 ? 0.25739 0.22842 0.17641 -0.00753 0.06739  -0.05224 32 TYR B CB  
928  C CG  . TYR B 33 ? 0.25319 0.22558 0.18175 -0.01404 0.07256  -0.05745 32 TYR B CG  
929  C CD1 . TYR B 33 ? 0.26526 0.24073 0.19726 -0.01689 0.07535  -0.06070 32 TYR B CD1 
930  C CD2 . TYR B 33 ? 0.25040 0.22253 0.18567 -0.01764 0.07508  -0.06086 32 TYR B CD2 
931  C CE1 . TYR B 33 ? 0.25480 0.23489 0.19865 -0.02326 0.08093  -0.06764 32 TYR B CE1 
932  C CE2 . TYR B 33 ? 0.28709 0.26524 0.23530 -0.02448 0.08030  -0.06904 32 TYR B CE2 
933  C CZ  . TYR B 33 ? 0.29627 0.27908 0.24947 -0.02734 0.08345  -0.07251 32 TYR B CZ  
934  O OH  . TYR B 33 ? 0.34990 0.34203 0.31923 -0.03451 0.08924  -0.08257 32 TYR B OH  
935  N N   . TYR B 34 ? 0.18150 0.15800 0.11175 -0.00194 0.05965  -0.05202 33 TYR B N   
936  C CA  . TYR B 34 ? 0.17910 0.15410 0.11208 0.00007  0.05751  -0.05326 33 TYR B CA  
937  C C   . TYR B 34 ? 0.25518 0.22845 0.19117 -0.00318 0.05997  -0.05718 33 TYR B C   
938  O O   . TYR B 34 ? 0.26487 0.23254 0.19570 -0.00710 0.06475  -0.05568 33 TYR B O   
939  C CB  . TYR B 34 ? 0.17942 0.15115 0.10600 0.00332  0.05647  -0.04863 33 TYR B CB  
940  C CG  . TYR B 34 ? 0.19080 0.15781 0.11586 0.00600  0.05472  -0.04863 33 TYR B CG  
941  C CD1 . TYR B 34 ? 0.29938 0.26123 0.22144 0.00566  0.05552  -0.04888 33 TYR B CD1 
942  C CD2 . TYR B 34 ? 0.23356 0.19817 0.15743 0.00857  0.05312  -0.04842 33 TYR B CD2 
943  C CE1 . TYR B 34 ? 0.28552 0.24218 0.20436 0.00883  0.05328  -0.04932 33 TYR B CE1 
944  C CE2 . TYR B 34 ? 0.24940 0.20645 0.16790 0.01180  0.05167  -0.04796 33 TYR B CE2 
945  C CZ  . TYR B 34 ? 0.24822 0.20254 0.16478 0.01239  0.05100  -0.04864 33 TYR B CZ  
946  O OH  . TYR B 34 ? 0.34847 0.29463 0.25842 0.01603  0.04893  -0.04852 33 TYR B OH  
947  N N   . VAL B 35 ? 0.19277 0.16914 0.13539 -0.00118 0.05685  -0.06322 34 VAL B N   
948  C CA  . VAL B 35 ? 0.21688 0.19532 0.16615 -0.00468 0.05835  -0.07030 34 VAL B CA  
949  C C   . VAL B 35 ? 0.26060 0.23433 0.20511 0.00131  0.05290  -0.07129 34 VAL B C   
950  O O   . VAL B 35 ? 0.24889 0.22115 0.19034 0.00887  0.04693  -0.07233 34 VAL B O   
951  C CB  . VAL B 35 ? 0.23604 0.22749 0.20154 -0.00698 0.05811  -0.08094 34 VAL B CB  
952  C CG1 . VAL B 35 ? 0.27029 0.26794 0.24727 -0.01343 0.06104  -0.09078 34 VAL B CG1 
953  C CG2 . VAL B 35 ? 0.24911 0.24312 0.21679 -0.01213 0.06371  -0.07939 34 VAL B CG2 
954  N N   . PRO B 36 ? 0.35684 0.18583 0.30777 0.01833  -0.10535 -0.07239 35 PRO B N   
955  C CA  . PRO B 36 ? 0.35995 0.18008 0.31013 0.02056  -0.11052 -0.08294 35 PRO B CA  
956  C C   . PRO B 36 ? 0.37423 0.21634 0.33112 0.01758  -0.11242 -0.08885 35 PRO B C   
957  O O   . PRO B 36 ? 0.35437 0.21465 0.31834 0.01059  -0.11071 -0.08532 35 PRO B O   
958  C CB  . PRO B 36 ? 0.37951 0.17662 0.33489 0.01175  -0.11622 -0.08429 35 PRO B CB  
959  C CG  . PRO B 36 ? 0.48618 0.27316 0.44168 0.00682  -0.11353 -0.07096 35 PRO B CG  
960  C CD  . PRO B 36 ? 0.37208 0.18824 0.32742 0.00655  -0.10635 -0.06291 35 PRO B CD  
961  N N   . GLY B 37 ? 0.35317 0.19791 0.30790 0.02296  -0.11618 -0.09768 36 GLY B N   
962  C CA  . GLY B 37 ? 0.35031 0.21504 0.31133 0.01994  -0.11885 -0.10383 36 GLY B CA  
963  C C   . GLY B 37 ? 0.36629 0.22492 0.33539 0.00933  -0.12330 -0.11028 36 GLY B C   
964  O O   . GLY B 37 ? 0.39122 0.22892 0.36358 0.00402  -0.12643 -0.10934 36 GLY B O   
965  N N   . GLY B 38 ? 0.36486 0.24121 0.33997 0.00595  -0.12575 -0.11652 37 GLY B N   
966  C CA  . GLY B 38 ? 0.39014 0.26163 0.37618 -0.00417 -0.13214 -0.12308 37 GLY B CA  
967  C C   . GLY B 38 ? 0.37606 0.27034 0.36713 -0.00616 -0.13389 -0.13030 37 GLY B C   
968  O O   . GLY B 38 ? 0.36209 0.27544 0.34809 0.00110  -0.13163 -0.13138 37 GLY B O   
969  N N   . VAL B 39 ? 0.38932 0.28122 0.39283 -0.01699 -0.13979 -0.13378 38 VAL B N   
970  C CA  . VAL B 39 ? 0.38870 0.29928 0.39836 -0.01948 -0.14307 -0.14302 38 VAL B CA  
971  C C   . VAL B 39 ? 0.59496 0.50755 0.61854 -0.03474 -0.14552 -0.13576 38 VAL B C   
972  O O   . VAL B 39 ? 0.68675 0.58014 0.72265 -0.04391 -0.15416 -0.13394 38 VAL B O   
973  C CB  . VAL B 39 ? 0.42845 0.33820 0.44080 -0.01330 -0.14891 -0.15830 38 VAL B CB  
974  C CG1 . VAL B 39 ? 0.44566 0.37620 0.46487 -0.01639 -0.15082 -0.16575 38 VAL B CG1 
975  C CG2 . VAL B 39 ? 0.45097 0.37005 0.45031 0.00123  -0.14420 -0.16104 38 VAL B CG2 
976  N N   . TYR B 40 ? 0.58375 0.52089 0.60825 -0.03809 -0.14013 -0.13094 39 TYR B N   
977  C CA  . TYR B 40 ? 0.65942 0.60648 0.69731 -0.05291 -0.14250 -0.12379 39 TYR B CA  
978  C C   . TYR B 40 ? 0.68243 0.64706 0.72533 -0.05422 -0.14506 -0.13408 39 TYR B C   
979  O O   . TYR B 40 ? 0.56687 0.54671 0.60191 -0.04445 -0.14142 -0.14093 39 TYR B O   
980  C CB  . TYR B 40 ? 0.54752 0.51557 0.58403 -0.05688 -0.13406 -0.10857 39 TYR B CB  
981  C CG  . TYR B 40 ? 0.79950 0.79281 0.82875 -0.04612 -0.12714 -0.11237 39 TYR B CG  
982  C CD1 . TYR B 40 ? 0.72983 0.74883 0.76528 -0.04927 -0.12696 -0.11574 39 TYR B CD1 
983  C CD2 . TYR B 40 ? 0.81272 0.80353 0.83205 -0.03289 -0.12310 -0.11242 39 TYR B CD2 
984  C CE1 . TYR B 40 ? 0.47996 0.52051 0.51345 -0.03896 -0.12432 -0.12024 39 TYR B CE1 
985  C CE2 . TYR B 40 ? 0.68342 0.69487 0.70232 -0.02288 -0.12165 -0.11614 39 TYR B CE2 
986  C CZ  . TYR B 40 ? 0.75297 0.78880 0.77973 -0.02574 -0.12293 -0.12052 39 TYR B CZ  
987  O OH  . TYR B 40 ? 0.82651 0.88111 0.85713 -0.01521 -0.12497 -0.12538 39 TYR B OH  
988  N N   . LYS B 41 ? 0.66483 0.62758 0.72314 -0.06729 -0.15300 -0.13337 40 LYS B N   
989  C CA  . LYS B 41 ? 0.40633 0.38639 0.47097 -0.07039 -0.15560 -0.14186 40 LYS B CA  
990  C C   . LYS B 41 ? 0.51189 0.52298 0.57296 -0.07139 -0.14612 -0.13437 40 LYS B C   
991  O O   . LYS B 41 ? 0.53764 0.56038 0.59812 -0.07523 -0.14040 -0.12109 40 LYS B O   
992  C CB  . LYS B 41 ? 0.64598 0.61539 0.73138 -0.08539 -0.16838 -0.14044 40 LYS B CB  
993  C CG  . LYS B 41 ? 0.63087 0.56932 0.72626 -0.08277 -0.18310 -0.15319 40 LYS B CG  
994  C CD  . LYS B 41 ? 0.79072 0.73733 0.87849 -0.06825 -0.17987 -0.17112 40 LYS B CD  
995  C CE  . LYS B 41 ? 0.71598 0.64321 0.80512 -0.05686 -0.18461 -0.18071 40 LYS B CE  
996  N NZ  . LYS B 41 ? 0.88546 0.80174 0.96205 -0.04975 -0.17928 -0.17606 40 LYS B NZ  
997  N N   . SER B 42 ? 0.59575 0.62391 0.65577 -0.06707 -0.14564 -0.14422 41 SER B N   
998  C CA  . SER B 42 ? 0.77567 0.83300 0.83528 -0.06609 -0.13956 -0.14077 41 SER B CA  
999  C C   . SER B 42 ? 0.61021 0.68475 0.68162 -0.08100 -0.13994 -0.13183 41 SER B C   
1000 O O   . SER B 42 ? 0.57748 0.64587 0.65991 -0.09191 -0.14708 -0.13294 41 SER B O   
1001 C CB  . SER B 42 ? 0.57871 0.64918 0.63671 -0.05889 -0.14113 -0.15189 41 SER B CB  
1002 O OG  . SER B 42 ? 0.44852 0.51365 0.49701 -0.04617 -0.14079 -0.15454 41 SER B OG  
1003 N N   . GLN B 43 ? 0.64069 0.74100 0.71141 -0.08078 -0.13358 -0.12360 42 GLN B N   
1004 C CA  . GLN B 43 ? 0.58518 0.71092 0.66625 -0.09544 -0.13304 -0.11082 42 GLN B CA  
1005 C C   . GLN B 43 ? 0.59280 0.74189 0.68193 -0.10105 -0.13460 -0.11574 42 GLN B C   
1006 O O   . GLN B 43 ? 0.59899 0.75431 0.70040 -0.11710 -0.13934 -0.10684 42 GLN B O   
1007 C CB  . GLN B 43 ? 0.62613 0.78202 0.70322 -0.09060 -0.12575 -0.10346 42 GLN B CB  
1008 C CG  . GLN B 43 ? 0.84246 0.98110 0.91323 -0.08826 -0.12378 -0.09474 42 GLN B CG  
1009 C CD  . GLN B 43 ? 1.08905 1.19458 1.14847 -0.07270 -0.12386 -0.10592 42 GLN B CD  
1010 O OE1 . GLN B 43 ? 0.80983 0.92369 0.86384 -0.05781 -0.12175 -0.11531 42 GLN B OE1 
1011 N NE2 . GLN B 43 ? 1.07817 1.14772 1.13664 -0.07613 -0.12846 -0.10485 42 GLN B NE2 
1012 N N   . THR B 44 ? 0.58177 0.74415 0.66658 -0.08882 -0.13237 -0.12832 43 THR B N   
1013 C CA  . THR B 44 ? 0.53114 0.71765 0.62328 -0.09261 -0.13359 -0.13382 43 THR B CA  
1014 C C   . THR B 44 ? 0.44963 0.62162 0.53952 -0.08543 -0.13751 -0.14719 43 THR B C   
1015 O O   . THR B 44 ? 0.44747 0.59932 0.52962 -0.07542 -0.13857 -0.15196 43 THR B O   
1016 C CB  . THR B 44 ? 0.52742 0.75419 0.62108 -0.08481 -0.12954 -0.13660 43 THR B CB  
1017 O OG1 . THR B 44 ? 0.42685 0.64660 0.51545 -0.06690 -0.13067 -0.14689 43 THR B OG1 
1018 C CG2 . THR B 44 ? 0.50935 0.76196 0.60410 -0.09014 -0.12504 -0.12384 43 THR B CG2 
1019 N N   . ASP B 45 ? 0.37986 0.56759 0.47707 -0.09109 -0.13979 -0.15195 44 ASP B N   
1020 C CA  . ASP B 45 ? 0.47774 0.65817 0.57196 -0.08396 -0.14181 -0.16061 44 ASP B CA  
1021 C C   . ASP B 45 ? 0.40995 0.59557 0.49879 -0.06851 -0.13870 -0.15974 44 ASP B C   
1022 O O   . ASP B 45 ? 0.38111 0.55491 0.46450 -0.06097 -0.13918 -0.15929 44 ASP B O   
1023 C CB  . ASP B 45 ? 0.51284 0.70545 0.61441 -0.09251 -0.14295 -0.16172 44 ASP B CB  
1024 C CG  . ASP B 45 ? 0.40623 0.58794 0.51755 -0.10770 -0.14974 -0.16164 44 ASP B CG  
1025 O OD1 . ASP B 45 ? 0.61397 0.77186 0.72515 -0.10885 -0.15400 -0.16211 44 ASP B OD1 
1026 O OD2 . ASP B 45 ? 0.61496 0.80965 0.73598 -0.11807 -0.15217 -0.16023 44 ASP B OD2 
1027 N N   . VAL B 46 ? 0.49179 0.69780 0.58451 -0.06357 -0.13706 -0.15902 45 VAL B N   
1028 C CA  . VAL B 46 ? 0.50854 0.71393 0.60122 -0.04824 -0.13770 -0.15838 45 VAL B CA  
1029 C C   . VAL B 46 ? 0.38677 0.56997 0.47242 -0.04134 -0.13897 -0.15556 45 VAL B C   
1030 O O   . VAL B 46 ? 0.45942 0.63306 0.54477 -0.03319 -0.14174 -0.15164 45 VAL B O   
1031 C CB  . VAL B 46 ? 0.34917 0.58143 0.44904 -0.04146 -0.13679 -0.16158 45 VAL B CB  
1032 C CG1 . VAL B 46 ? 0.37940 0.60487 0.48350 -0.02495 -0.14050 -0.16190 45 VAL B CG1 
1033 C CG2 . VAL B 46 ? 0.43043 0.68654 0.53708 -0.04701 -0.13548 -0.16415 45 VAL B CG2 
1034 N N   . ILE B 47 ? 0.35563 0.53203 0.43698 -0.04593 -0.13804 -0.15595 46 ILE B N   
1035 C CA  . ILE B 47 ? 0.34338 0.49671 0.41694 -0.03968 -0.13903 -0.15358 46 ILE B CA  
1036 C C   . ILE B 47 ? 0.39186 0.52819 0.45938 -0.04099 -0.13992 -0.15293 46 ILE B C   
1037 O O   . ILE B 47 ? 0.42009 0.54874 0.48372 -0.03283 -0.14143 -0.14888 46 ILE B O   
1038 C CB  . ILE B 47 ? 0.46988 0.61502 0.53879 -0.04469 -0.13525 -0.14948 46 ILE B CB  
1039 C CG1 . ILE B 47 ? 0.51913 0.69019 0.59224 -0.04057 -0.13265 -0.14858 46 ILE B CG1 
1040 C CG2 . ILE B 47 ? 0.35230 0.47005 0.41178 -0.03827 -0.13522 -0.14645 46 ILE B CG2 
1041 C CD1 . ILE B 47 ? 0.68103 0.84989 0.74936 -0.04682 -0.12692 -0.13857 46 ILE B CD1 
1042 N N   . LYS B 48 ? 0.32505 0.45951 0.39340 -0.05099 -0.14005 -0.15690 47 LYS B N   
1043 C CA  . LYS B 48 ? 0.33120 0.45673 0.39446 -0.04996 -0.14106 -0.15949 47 LYS B CA  
1044 C C   . LYS B 48 ? 0.32412 0.46395 0.38761 -0.04350 -0.14157 -0.15547 47 LYS B C   
1045 O O   . LYS B 48 ? 0.32258 0.46333 0.38090 -0.03899 -0.14280 -0.15464 47 LYS B O   
1046 C CB  . LYS B 48 ? 0.34518 0.46837 0.41341 -0.06036 -0.14308 -0.16562 47 LYS B CB  
1047 C CG  . LYS B 48 ? 0.39819 0.50221 0.47031 -0.06833 -0.14711 -0.16779 47 LYS B CG  
1048 C CD  . LYS B 48 ? 0.46988 0.57047 0.55230 -0.07891 -0.15270 -0.17240 47 LYS B CD  
1049 C CE  . LYS B 48 ? 0.61717 0.69522 0.70996 -0.08849 -0.16101 -0.17139 47 LYS B CE  
1050 N NZ  . LYS B 48 ? 0.49081 0.56612 0.59977 -0.10140 -0.16954 -0.17194 47 LYS B NZ  
1051 N N   . ASN B 49 ? 0.31572 0.47004 0.38673 -0.04333 -0.14183 -0.15243 48 ASN B N   
1052 C CA  . ASN B 49 ? 0.30941 0.47601 0.38424 -0.03929 -0.14493 -0.14624 48 ASN B CA  
1053 C C   . ASN B 49 ? 0.35498 0.51871 0.43056 -0.03122 -0.14910 -0.13693 48 ASN B C   
1054 O O   . ASN B 49 ? 0.30975 0.48413 0.38801 -0.03021 -0.15362 -0.12842 48 ASN B O   
1055 C CB  . ASN B 49 ? 0.30628 0.48585 0.39104 -0.04022 -0.14575 -0.14553 48 ASN B CB  
1056 C CG  . ASN B 49 ? 0.39063 0.57732 0.47614 -0.04889 -0.14313 -0.15186 48 ASN B CG  
1057 O OD1 . ASN B 49 ? 0.40928 0.59155 0.48969 -0.05344 -0.14228 -0.15643 48 ASN B OD1 
1058 N ND2 . ASN B 49 ? 0.38712 0.58575 0.48025 -0.05025 -0.14272 -0.15306 48 ASN B ND2 
1059 N N   . THR B 50 ? 0.32613 0.47798 0.40075 -0.02632 -0.14871 -0.13679 49 THR B N   
1060 C CA  . THR B 50 ? 0.34781 0.49401 0.42453 -0.01853 -0.15357 -0.12753 49 THR B CA  
1061 C C   . THR B 50 ? 0.32749 0.46290 0.39280 -0.01723 -0.15221 -0.12740 49 THR B C   
1062 O O   . THR B 50 ? 0.39124 0.53068 0.45668 -0.01399 -0.15671 -0.11749 49 THR B O   
1063 C CB  . THR B 50 ? 0.28924 0.43017 0.37349 -0.01106 -0.15497 -0.12840 49 THR B CB  
1064 O OG1 . THR B 50 ? 0.32510 0.47752 0.42220 -0.00898 -0.15845 -0.12809 49 THR B OG1 
1065 C CG2 . THR B 50 ? 0.28519 0.41493 0.37166 -0.00293 -0.16016 -0.11949 49 THR B CG2 
1066 N N   . PHE B 51 ? 0.30221 0.42536 0.35888 -0.02045 -0.14709 -0.13681 50 PHE B N   
1067 C CA  . PHE B 51 ? 0.44461 0.55353 0.49122 -0.01753 -0.14628 -0.13781 50 PHE B CA  
1068 C C   . PHE B 51 ? 0.34958 0.45813 0.38899 -0.02081 -0.14445 -0.14624 50 PHE B C   
1069 O O   . PHE B 51 ? 0.49997 0.59968 0.53155 -0.01674 -0.14432 -0.14831 50 PHE B O   
1070 C CB  . PHE B 51 ? 0.40184 0.49283 0.44589 -0.01713 -0.14398 -0.14073 50 PHE B CB  
1071 C CG  . PHE B 51 ? 0.43204 0.52528 0.48321 -0.01018 -0.14616 -0.13557 50 PHE B CG  
1072 C CD1 . PHE B 51 ? 0.48442 0.59115 0.54442 -0.01125 -0.14553 -0.13880 50 PHE B CD1 
1073 C CD2 . PHE B 51 ? 0.39061 0.47455 0.44094 -0.00152 -0.14952 -0.12849 50 PHE B CD2 
1074 C CE1 . PHE B 51 ? 0.41560 0.52727 0.48388 -0.00189 -0.14815 -0.13755 50 PHE B CE1 
1075 C CE2 . PHE B 51 ? 0.29972 0.38434 0.35937 0.00673  -0.15272 -0.12568 50 PHE B CE2 
1076 C CZ  . PHE B 51 ? 0.43265 0.53154 0.50146 0.00747  -0.15202 -0.13152 50 PHE B CZ  
1077 N N   . GLY B 52 ? 0.39606 0.51444 0.43892 -0.02654 -0.14373 -0.15198 51 GLY B N   
1078 C CA  . GLY B 52 ? 0.39104 0.50680 0.43043 -0.02791 -0.14354 -0.16271 51 GLY B CA  
1079 C C   . GLY B 52 ? 0.44638 0.53759 0.48787 -0.03395 -0.14381 -0.16927 51 GLY B C   
1080 O O   . GLY B 52 ? 0.42750 0.51120 0.47312 -0.03950 -0.14328 -0.16535 51 GLY B O   
1081 N N   . GLU B 53 ? 0.36426 0.44597 0.40531 -0.03266 -0.14634 -0.17904 52 GLU B N   
1082 C CA  . GLU B 53 ? 0.42104 0.47819 0.46960 -0.04036 -0.15052 -0.18305 52 GLU B CA  
1083 C C   . GLU B 53 ? 0.56488 0.60068 0.61028 -0.04011 -0.15043 -0.17743 52 GLU B C   
1084 O O   . GLU B 53 ? 0.44168 0.46479 0.49505 -0.05021 -0.15349 -0.17283 52 GLU B O   
1085 C CB  . GLU B 53 ? 0.44041 0.49224 0.49386 -0.03702 -0.15606 -0.19599 52 GLU B CB  
1086 C CG  . GLU B 53 ? 0.79185 0.86121 0.85164 -0.03942 -0.15789 -0.20259 52 GLU B CG  
1087 C CD  . GLU B 53 ? 0.71525 0.77619 0.78759 -0.05400 -0.16187 -0.19898 52 GLU B CD  
1088 O OE1 . GLU B 53 ? 0.89039 0.92943 0.97162 -0.06267 -0.16731 -0.19480 52 GLU B OE1 
1089 O OE2 . GLU B 53 ? 0.56687 0.64549 0.64163 -0.05770 -0.16037 -0.19885 52 GLU B OE2 
1090 N N   . GLU B 54 ? 0.52645 0.56120 0.56150 -0.02961 -0.14783 -0.17646 53 GLU B N   
1091 C CA  . GLU B 54 ? 0.46274 0.47638 0.49360 -0.02821 -0.14744 -0.17119 53 GLU B CA  
1092 C C   . GLU B 54 ? 0.44087 0.46445 0.46328 -0.02108 -0.14337 -0.16255 53 GLU B C   
1093 O O   . GLU B 54 ? 0.41251 0.45800 0.43254 -0.01579 -0.14251 -0.16020 53 GLU B O   
1094 C CB  . GLU B 54 ? 0.48948 0.48678 0.51769 -0.02133 -0.14991 -0.17804 53 GLU B CB  
1095 C CG  . GLU B 54 ? 0.70919 0.68974 0.75042 -0.02660 -0.15760 -0.18600 53 GLU B CG  
1096 C CD  . GLU B 54 ? 0.70197 0.67304 0.74246 -0.01573 -0.16075 -0.19527 53 GLU B CD  
1097 O OE1 . GLU B 54 ? 0.68187 0.65922 0.71011 -0.00611 -0.15579 -0.19371 53 GLU B OE1 
1098 O OE2 . GLU B 54 ? 1.13809 1.09735 1.19213 -0.01617 -0.16942 -0.20418 53 GLU B OE2 
1099 N N   . VAL B 55 ? 0.46092 0.46799 0.48082 -0.02136 -0.14161 -0.15540 54 VAL B N   
1100 C CA  . VAL B 55 ? 0.47274 0.48299 0.48697 -0.01380 -0.13776 -0.14520 54 VAL B CA  
1101 C C   . VAL B 55 ? 0.34434 0.33270 0.35021 -0.00861 -0.13656 -0.14310 54 VAL B C   
1102 O O   . VAL B 55 ? 0.48378 0.45254 0.49083 -0.01403 -0.13555 -0.14126 54 VAL B O   
1103 C CB  . VAL B 55 ? 0.44528 0.46167 0.46488 -0.01735 -0.13397 -0.13761 54 VAL B CB  
1104 C CG1 . VAL B 55 ? 0.40077 0.42351 0.41984 -0.00729 -0.13435 -0.13154 54 VAL B CG1 
1105 C CG2 . VAL B 55 ? 0.52032 0.55639 0.54917 -0.02469 -0.13516 -0.14129 54 VAL B CG2 
1106 N N   . LYS B 56 ? 0.33728 0.33101 0.33626 0.00077  -0.13771 -0.14151 55 LYS B N   
1107 C CA  . LYS B 56 ? 0.33918 0.31450 0.32969 0.00690  -0.13607 -0.13800 55 LYS B CA  
1108 C C   . LYS B 56 ? 0.32675 0.29980 0.31667 0.01152  -0.13356 -0.12539 55 LYS B C   
1109 O O   . LYS B 56 ? 0.31525 0.30556 0.31018 0.01519  -0.13719 -0.11976 55 LYS B O   
1110 C CB  . LYS B 56 ? 0.35275 0.34044 0.33670 0.01475  -0.13962 -0.14354 55 LYS B CB  
1111 C CG  . LYS B 56 ? 0.44819 0.41933 0.42321 0.02166  -0.13817 -0.14048 55 LYS B CG  
1112 C CD  . LYS B 56 ? 0.68439 0.66907 0.65512 0.02833  -0.13960 -0.15029 55 LYS B CD  
1113 C CE  . LYS B 56 ? 0.64663 0.67001 0.61476 0.03322  -0.14246 -0.14449 55 LYS B CE  
1114 N NZ  . LYS B 56 ? 0.73623 0.75819 0.69940 0.03777  -0.14351 -0.12878 55 LYS B NZ  
1115 N N   . TYR B 57 ? 0.33012 0.28320 0.31674 0.01141  -0.12947 -0.12111 56 TYR B N   
1116 C CA  . TYR B 57 ? 0.31987 0.27171 0.30690 0.01790  -0.12834 -0.11253 56 TYR B CA  
1117 C C   . TYR B 57 ? 0.33803 0.27103 0.31572 0.02441  -0.12704 -0.10817 56 TYR B C   
1118 O O   . TYR B 57 ? 0.33218 0.24772 0.30373 0.02182  -0.12487 -0.11135 56 TYR B O   
1119 C CB  . TYR B 57 ? 0.32043 0.27594 0.31242 0.01368  -0.12436 -0.11089 56 TYR B CB  
1120 C CG  . TYR B 57 ? 0.33296 0.27300 0.32143 0.00570  -0.11975 -0.10811 56 TYR B CG  
1121 C CD1 . TYR B 57 ? 0.44466 0.38305 0.43812 -0.00622 -0.12086 -0.11043 56 TYR B CD1 
1122 C CD2 . TYR B 57 ? 0.33345 0.26111 0.31652 0.00924  -0.11634 -0.10171 56 TYR B CD2 
1123 C CE1 . TYR B 57 ? 0.44531 0.36913 0.44102 -0.01565 -0.12065 -0.10436 56 TYR B CE1 
1124 C CE2 . TYR B 57 ? 0.40951 0.32444 0.39219 -0.00001 -0.11405 -0.09585 56 TYR B CE2 
1125 C CZ  . TYR B 57 ? 0.42922 0.34216 0.41960 -0.01303 -0.11719 -0.09615 56 TYR B CZ  
1126 O OH  . TYR B 57 ? 0.49316 0.39328 0.48882 -0.02440 -0.11901 -0.08706 56 TYR B OH  
1127 N N   . ARG B 58 ? 0.22334 0.21387 0.20917 0.01162  -0.05093 -0.08743 57 ARG B N   
1128 C CA  . ARG B 58 ? 0.22109 0.21507 0.18702 0.00671  -0.04162 -0.08568 57 ARG B CA  
1129 C C   . ARG B 58 ? 0.20599 0.20987 0.18336 0.00397  -0.03009 -0.08468 57 ARG B C   
1130 O O   . ARG B 58 ? 0.21925 0.22578 0.21486 0.00451  -0.02678 -0.08417 57 ARG B O   
1131 C CB  . ARG B 58 ? 0.27265 0.25656 0.21625 0.00376  -0.04019 -0.08233 57 ARG B CB  
1132 C CG  . ARG B 58 ? 0.32853 0.29814 0.25474 0.00523  -0.05191 -0.08165 57 ARG B CG  
1133 C CD  . ARG B 58 ? 0.34782 0.30665 0.24966 0.00008  -0.04887 -0.07708 57 ARG B CD  
1134 N NE  . ARG B 58 ? 0.45347 0.39636 0.33050 -0.00065 -0.05902 -0.07521 57 ARG B NE  
1135 C CZ  . ARG B 58 ? 0.59221 0.52425 0.44105 -0.00723 -0.05656 -0.07083 57 ARG B CZ  
1136 N NH1 . ARG B 58 ? 0.60027 0.53745 0.44480 -0.01316 -0.04446 -0.06885 57 ARG B NH1 
1137 N NH2 . ARG B 58 ? 0.55996 0.47458 0.38352 -0.00833 -0.06677 -0.06831 57 ARG B NH2 
1138 N N   . PRO B 59 ? 0.20165 0.21075 0.16786 0.00082  -0.02386 -0.08508 58 PRO B N   
1139 C CA  . PRO B 59 ? 0.24654 0.26121 0.21774 -0.00186 -0.01404 -0.08355 58 PRO B CA  
1140 C C   . PRO B 59 ? 0.26960 0.28080 0.23799 -0.00324 -0.00800 -0.08099 58 PRO B C   
1141 O O   . PRO B 59 ? 0.20855 0.21239 0.16641 -0.00323 -0.01086 -0.08004 58 PRO B O   
1142 C CB  . PRO B 59 ? 0.23882 0.25759 0.19634 -0.00408 -0.01144 -0.08605 58 PRO B CB  
1143 C CG  . PRO B 59 ? 0.33721 0.35267 0.27859 -0.00441 -0.01562 -0.08805 58 PRO B CG  
1144 C CD  . PRO B 59 ? 0.20740 0.21748 0.15533 -0.00056 -0.02532 -0.08795 58 PRO B CD  
1145 N N   . TYR B 60 ? 0.18710 0.20236 0.16387 -0.00463 -0.00012 -0.07990 59 TYR B N   
1146 C CA  . TYR B 60 ? 0.18866 0.20174 0.16399 -0.00531 0.00560  -0.07897 59 TYR B CA  
1147 C C   . TYR B 60 ? 0.19785 0.21504 0.17066 -0.00793 0.01504  -0.07827 59 TYR B C   
1148 O O   . TYR B 60 ? 0.24021 0.26013 0.21170 -0.00927 0.01597  -0.07794 59 TYR B O   
1149 C CB  . TYR B 60 ? 0.23783 0.25030 0.23156 -0.00248 0.00315  -0.08032 59 TYR B CB  
1150 C CG  . TYR B 60 ? 0.19706 0.21707 0.21101 -0.00295 0.00694  -0.08132 59 TYR B CG  
1151 C CD1 . TYR B 60 ? 0.23002 0.25162 0.25539 -0.00173 0.00035  -0.08208 59 TYR B CD1 
1152 C CD2 . TYR B 60 ? 0.18283 0.20805 0.20387 -0.00524 0.01744  -0.08173 59 TYR B CD2 
1153 C CE1 . TYR B 60 ? 0.19896 0.22689 0.24396 -0.00359 0.00422  -0.08257 59 TYR B CE1 
1154 C CE2 . TYR B 60 ? 0.21693 0.24865 0.25494 -0.00760 0.02252  -0.08216 59 TYR B CE2 
1155 C CZ  . TYR B 60 ? 0.35726 0.39013 0.40781 -0.00716 0.01595  -0.08223 59 TYR B CZ  
1156 O OH  . TYR B 60 ? 0.26743 0.30616 0.33551 -0.01086 0.02146  -0.08222 59 TYR B OH  
1157 N N   . LEU B 61 ? 0.18567 0.20172 0.15649 -0.00831 0.02062  -0.07841 60 LEU B N   
1158 C CA  . LEU B 61 ? 0.18459 0.20282 0.15045 -0.01033 0.02897  -0.07818 60 LEU B CA  
1159 C C   . LEU B 61 ? 0.24370 0.26552 0.22272 -0.01027 0.03553  -0.07925 60 LEU B C   
1160 O O   . LEU B 61 ? 0.21512 0.23747 0.20628 -0.00792 0.03386  -0.08169 60 LEU B O   
1161 C CB  . LEU B 61 ? 0.19666 0.21152 0.14825 -0.01105 0.03072  -0.07893 60 LEU B CB  
1162 C CG  . LEU B 61 ? 0.18719 0.20076 0.12666 -0.01250 0.02666  -0.07938 60 LEU B CG  
1163 C CD1 . LEU B 61 ? 0.19030 0.20113 0.11906 -0.01426 0.02957  -0.08051 60 LEU B CD1 
1164 C CD2 . LEU B 61 ? 0.18658 0.20381 0.12425 -0.01311 0.02583  -0.08041 60 LEU B CD2 
1165 N N   . ALA B 62 ? 0.20119 0.22505 0.17741 -0.01308 0.04276  -0.07807 61 ALA B N   
1166 C CA  . ALA B 62 ? 0.21233 0.24104 0.19902 -0.01470 0.05165  -0.07959 61 ALA B CA  
1167 C C   . ALA B 62 ? 0.20052 0.22755 0.17225 -0.01639 0.05960  -0.07984 61 ALA B C   
1168 O O   . ALA B 62 ? 0.21597 0.23761 0.17084 -0.01700 0.05766  -0.07780 61 ALA B O   
1169 C CB  . ALA B 62 ? 0.20995 0.24159 0.20704 -0.01828 0.05381  -0.07725 61 ALA B CB  
1170 N N   . LEU B 63 ? 0.21264 0.24467 0.19151 -0.01669 0.06800  -0.08367 62 LEU B N   
1171 C CA  . LEU B 63 ? 0.21094 0.24161 0.17525 -0.01805 0.07610  -0.08498 62 LEU B CA  
1172 C C   . LEU B 63 ? 0.24110 0.27708 0.20929 -0.02316 0.08793  -0.08542 62 LEU B C   
1173 O O   . LEU B 63 ? 0.21938 0.26473 0.20879 -0.02345 0.09260  -0.08997 62 LEU B O   
1174 C CB  . LEU B 63 ? 0.21020 0.24200 0.17680 -0.01363 0.07596  -0.09098 62 LEU B CB  
1175 C CG  . LEU B 63 ? 0.21955 0.24794 0.17179 -0.01311 0.07919  -0.08962 62 LEU B CG  
1176 C CD1 . LEU B 63 ? 0.22771 0.24669 0.16291 -0.01164 0.07102  -0.08420 62 LEU B CD1 
1177 C CD2 . LEU B 63 ? 0.24210 0.27435 0.20451 -0.00905 0.08025  -0.09581 62 LEU B CD2 
1178 N N   . LYS B 64 ? 0.23598 0.26547 0.18366 -0.02762 0.09257  -0.08111 63 LYS B N   
1179 C CA  . LYS B 64 ? 0.26210 0.29474 0.20608 -0.03386 0.10608  -0.08147 63 LYS B CA  
1180 C C   . LYS B 64 ? 0.25491 0.28910 0.19501 -0.02988 0.10783  -0.08429 63 LYS B C   
1181 O O   . LYS B 64 ? 0.35143 0.37665 0.27290 -0.02685 0.10219  -0.08115 63 LYS B O   
1182 C CB  . LYS B 64 ? 0.30142 0.32194 0.22232 -0.04011 0.10650  -0.07308 63 LYS B CB  
1183 C CG  . LYS B 64 ? 0.50563 0.52323 0.40926 -0.04536 0.11754  -0.07163 63 LYS B CG  
1184 C CD  . LYS B 64 ? 0.48259 0.49798 0.38200 -0.05627 0.12759  -0.06665 63 LYS B CD  
1185 C CE  . LYS B 64 ? 0.97020 0.97286 0.83927 -0.06170 0.13202  -0.06059 63 LYS B CE  
1186 N NZ  . LYS B 64 ? 0.68273 0.67767 0.54097 -0.07480 0.14094  -0.05288 63 LYS B NZ  
1187 N N   . THR B 65 ? 0.25841 0.30428 0.21835 -0.02925 0.11437  -0.09093 64 THR B N   
1188 C CA  . THR B 65 ? 0.25861 0.30739 0.22006 -0.02415 0.11423  -0.09572 64 THR B CA  
1189 C C   . THR B 65 ? 0.40593 0.45301 0.35037 -0.02787 0.12268  -0.09360 64 THR B C   
1190 O O   . THR B 65 ? 0.31419 0.35687 0.24512 -0.03520 0.12889  -0.08790 64 THR B O   
1191 C CB  . THR B 65 ? 0.28643 0.34841 0.27789 -0.02141 0.11633  -0.10571 64 THR B CB  
1192 O OG1 . THR B 65 ? 0.33054 0.40274 0.33476 -0.02780 0.12802  -0.10832 64 THR B OG1 
1193 C CG2 . THR B 65 ? 0.23403 0.29667 0.24147 -0.01804 0.10809  -0.10826 64 THR B CG2 
1194 N N   . VAL B 66 ? 0.28543 0.33493 0.22911 -0.02299 0.12277  -0.09848 65 VAL B N   
1195 C CA  . VAL B 66 ? 0.38730 0.43663 0.31550 -0.02595 0.13142  -0.09821 65 VAL B CA  
1196 C C   . VAL B 66 ? 0.50167 0.56233 0.44263 -0.03378 0.14492  -0.10125 65 VAL B C   
1197 O O   . VAL B 66 ? 0.59388 0.65152 0.51740 -0.04056 0.15374  -0.09728 65 VAL B O   
1198 C CB  . VAL B 66 ? 0.35916 0.41008 0.28635 -0.01859 0.12898  -0.10457 65 VAL B CB  
1199 C CG1 . VAL B 66 ? 0.42866 0.46798 0.34375 -0.01203 0.11637  -0.10125 65 VAL B CG1 
1200 C CG2 . VAL B 66 ? 0.36497 0.42952 0.32183 -0.01526 0.13044  -0.11556 65 VAL B CG2 
1201 N N   . ASP B 67 ? 0.35601 0.42931 0.32766 -0.03334 0.14644  -0.10854 66 ASP B N   
1202 C CA  . ASP B 67 ? 0.42204 0.50748 0.41104 -0.04098 0.15871  -0.11239 66 ASP B CA  
1203 C C   . ASP B 67 ? 0.59516 0.67555 0.57857 -0.04983 0.16260  -0.10391 66 ASP B C   
1204 O O   . ASP B 67 ? 0.56349 0.65332 0.56285 -0.05715 0.17261  -0.10626 66 ASP B O   
1205 C CB  . ASP B 67 ? 0.42256 0.52267 0.44925 -0.03660 0.15672  -0.12420 66 ASP B CB  
1206 C CG  . ASP B 67 ? 0.72152 0.82531 0.75529 -0.02791 0.15139  -0.13316 66 ASP B CG  
1207 O OD1 . ASP B 67 ? 0.55895 0.66211 0.57692 -0.02786 0.15643  -0.13410 66 ASP B OD1 
1208 O OD2 . ASP B 67 ? 0.52843 0.63470 0.58273 -0.02104 0.14163  -0.13937 66 ASP B OD2 
1209 N N   . ASN B 68 ? 0.46394 0.52991 0.42681 -0.04956 0.15469  -0.09486 67 ASN B N   
1210 C CA  . ASN B 68 ? 0.44256 0.50109 0.39725 -0.05778 0.15676  -0.08657 67 ASN B CA  
1211 C C   . ASN B 68 ? 0.40210 0.47085 0.38791 -0.05899 0.15683  -0.09030 67 ASN B C   
1212 O O   . ASN B 68 ? 0.65141 0.71691 0.63664 -0.06706 0.16056  -0.08450 67 ASN B O   
1213 C CB  . ASN B 68 ? 0.46203 0.51627 0.39892 -0.06886 0.16890  -0.08082 67 ASN B CB  
1214 C CG  . ASN B 68 ? 0.87343 0.91291 0.77426 -0.06808 0.16645  -0.07511 67 ASN B CG  
1215 O OD1 . ASN B 68 ? 0.76084 0.78429 0.63907 -0.06752 0.15771  -0.06784 67 ASN B OD1 
1216 N ND2 . ASN B 68 ? 0.97115 1.01613 0.86724 -0.06734 0.17329  -0.07956 67 ASN B ND2 
1217 N N   . ASP B 69 ? 0.36962 0.44965 0.38301 -0.05124 0.15197  -0.09986 68 ASP B N   
1218 C CA  . ASP B 69 ? 0.27266 0.36044 0.31504 -0.04953 0.14787  -0.10403 68 ASP B CA  
1219 C C   . ASP B 69 ? 0.30538 0.38361 0.33968 -0.04164 0.13306  -0.10145 68 ASP B C   
1220 O O   . ASP B 69 ? 0.28682 0.35523 0.29681 -0.03825 0.12856  -0.09858 68 ASP B O   
1221 C CB  . ASP B 69 ? 0.27498 0.37904 0.35368 -0.04567 0.14912  -0.11648 68 ASP B CB  
1222 C CG  . ASP B 69 ? 0.45534 0.56040 0.53496 -0.03656 0.14285  -0.12360 68 ASP B CG  
1223 O OD1 . ASP B 69 ? 0.46043 0.55424 0.51731 -0.03182 0.13538  -0.11921 68 ASP B OD1 
1224 O OD2 . ASP B 69 ? 0.45838 0.57571 0.56365 -0.03434 0.14489  -0.13430 68 ASP B OD2 
1225 N N   . ILE B 70 ? 0.23152 0.31015 0.28545 -0.03839 0.12170  -0.10047 69 ILE B N   
1226 C CA  . ILE B 70 ? 0.23433 0.30175 0.27863 -0.03211 0.10522  -0.09519 69 ILE B CA  
1227 C C   . ILE B 70 ? 0.26525 0.33615 0.32864 -0.02351 0.09540  -0.10257 69 ILE B C   
1228 O O   . ILE B 70 ? 0.25707 0.33642 0.34887 -0.02191 0.09349  -0.10868 69 ILE B O   
1229 C CB  . ILE B 70 ? 0.29853 0.36057 0.34483 -0.03503 0.09802  -0.08769 69 ILE B CB  
1230 C CG1 . ILE B 70 ? 0.25208 0.30853 0.28090 -0.04439 0.10679  -0.08016 69 ILE B CG1 
1231 C CG2 . ILE B 70 ? 0.26515 0.31701 0.29883 -0.02905 0.08284  -0.08363 69 ILE B CG2 
1232 C CD1 . ILE B 70 ? 0.37363 0.41865 0.36892 -0.04462 0.10724  -0.07561 69 ILE B CD1 
1233 N N   . ALA B 71 ? 0.20668 0.26970 0.25460 -0.01827 0.08809  -0.10195 70 ALA B N   
1234 C CA  . ALA B 71 ? 0.21079 0.27167 0.26986 -0.01090 0.07653  -0.10652 70 ALA B CA  
1235 C C   . ALA B 71 ? 0.19524 0.24480 0.24086 -0.00891 0.06351  -0.09933 70 ALA B C   
1236 O O   . ALA B 71 ? 0.26031 0.30415 0.28548 -0.01177 0.06385  -0.09272 70 ALA B O   
1237 C CB  . ALA B 71 ? 0.24291 0.30299 0.29539 -0.00738 0.07851  -0.11189 70 ALA B CB  
1238 N N   . THR B 72 ? 0.19253 0.23862 0.24963 -0.00411 0.05161  -0.10130 71 THR B N   
1239 C CA  . THR B 72 ? 0.19838 0.23324 0.23817 -0.00258 0.04068  -0.09559 71 THR B CA  
1240 C C   . THR B 72 ? 0.22094 0.24956 0.24329 -0.00176 0.04106  -0.09517 71 THR B C   
1241 O O   . THR B 72 ? 0.24611 0.27739 0.27460 0.00006  0.04499  -0.10059 71 THR B O   
1242 C CB  . THR B 72 ? 0.25932 0.28896 0.31071 0.00188  0.02725  -0.09727 71 THR B CB  
1243 O OG1 . THR B 72 ? 0.29481 0.32417 0.36006 0.00617  0.02417  -0.10413 71 THR B OG1 
1244 C CG2 . THR B 72 ? 0.18955 0.22535 0.26036 0.00154  0.02550  -0.09851 71 THR B CG2 
1245 N N   . TRP B 73 ? 0.19532 0.21664 0.19746 -0.00325 0.03730  -0.08981 72 TRP B N   
1246 C CA  . TRP B 73 ? 0.19661 0.21369 0.18309 -0.00385 0.03981  -0.08955 72 TRP B CA  
1247 C C   . TRP B 73 ? 0.22938 0.23712 0.20163 -0.00457 0.03173  -0.08589 72 TRP B C   
1248 O O   . TRP B 73 ? 0.24573 0.25235 0.21204 -0.00610 0.02797  -0.08267 72 TRP B O   
1249 C CB  . TRP B 73 ? 0.19553 0.21581 0.16971 -0.00703 0.04842  -0.08793 72 TRP B CB  
1250 C CG  . TRP B 73 ? 0.20540 0.22147 0.16498 -0.00712 0.05001  -0.08877 72 TRP B CG  
1251 C CD1 . TRP B 73 ? 0.20282 0.21880 0.16431 -0.00503 0.05293  -0.09336 72 TRP B CD1 
1252 C CD2 . TRP B 73 ? 0.19772 0.20995 0.14136 -0.00908 0.04830  -0.08643 72 TRP B CD2 
1253 N NE1 . TRP B 73 ? 0.20847 0.21963 0.15601 -0.00556 0.05224  -0.09238 72 TRP B NE1 
1254 C CE2 . TRP B 73 ? 0.20402 0.21287 0.14229 -0.00783 0.04866  -0.08673 72 TRP B CE2 
1255 C CE3 . TRP B 73 ? 0.24416 0.25588 0.18097 -0.01101 0.04486  -0.08349 72 TRP B CE3 
1256 C CZ2 . TRP B 73 ? 0.20104 0.20595 0.12998 -0.00825 0.04508  -0.08248 72 TRP B CZ2 
1257 C CZ3 . TRP B 73 ? 0.23704 0.24554 0.16559 -0.01110 0.04146  -0.07944 72 TRP B CZ3 
1258 C CH2 . TRP B 73 ? 0.24706 0.25236 0.17237 -0.00984 0.04179  -0.07911 72 TRP B CH2 
1259 N N   . THR B 74 ? 0.23667 0.23784 0.20343 -0.00398 0.02948  -0.08685 73 THR B N   
1260 C CA  . THR B 74 ? 0.35448 0.34687 0.30497 -0.00693 0.02485  -0.08318 73 THR B CA  
1261 C C   . THR B 74 ? 0.31076 0.30202 0.25362 -0.00816 0.02943  -0.08485 73 THR B C   
1262 O O   . THR B 74 ? 0.28548 0.27682 0.23618 -0.00526 0.03074  -0.08885 73 THR B O   
1263 C CB  . THR B 74 ? 0.46296 0.44375 0.41404 -0.00583 0.01410  -0.08153 73 THR B CB  
1264 O OG1 . THR B 74 ? 0.57905 0.55016 0.51167 -0.01062 0.01114  -0.07728 73 THR B OG1 
1265 C CG2 . THR B 74 ? 0.49316 0.47101 0.45855 -0.00135 0.01089  -0.08623 73 THR B CG2 
1266 N N   . PRO B 75 ? 0.27140 0.26272 0.20129 -0.01195 0.03175  -0.08342 74 PRO B N   
1267 C CA  . PRO B 75 ? 0.29946 0.28984 0.22415 -0.01274 0.03518  -0.08600 74 PRO B CA  
1268 C C   . PRO B 75 ? 0.35583 0.33643 0.28118 -0.01285 0.03033  -0.08605 74 PRO B C   
1269 O O   . PRO B 75 ? 0.33465 0.30639 0.25664 -0.01496 0.02383  -0.08226 74 PRO B O   
1270 C CB  . PRO B 75 ? 0.31886 0.31107 0.23447 -0.01653 0.03563  -0.08333 74 PRO B CB  
1271 C CG  . PRO B 75 ? 0.29791 0.29407 0.21360 -0.01702 0.03435  -0.08127 74 PRO B CG  
1272 C CD  . PRO B 75 ? 0.27321 0.26658 0.19483 -0.01525 0.03097  -0.08105 74 PRO B CD  
1273 N N   . SER B 76 ? 0.23854 0.21920 0.16709 -0.01049 0.03252  -0.09044 75 SER B N   
1274 C CA  . SER B 76 ? 0.23273 0.20294 0.16143 -0.01112 0.02704  -0.09078 75 SER B CA  
1275 C C   . SER B 76 ? 0.25037 0.21633 0.16747 -0.01765 0.02758  -0.08838 75 SER B C   
1276 O O   . SER B 76 ? 0.27655 0.24962 0.18783 -0.02039 0.03239  -0.08855 75 SER B O   
1277 C CB  . SER B 76 ? 0.26004 0.23244 0.19751 -0.00587 0.02866  -0.09777 75 SER B CB  
1278 O OG  . SER B 76 ? 0.24515 0.22232 0.17587 -0.00649 0.03440  -0.10066 75 SER B OG  
1279 N N   . VAL B 77 ? 0.28369 0.23771 0.19874 -0.02056 0.02214  -0.08669 76 VAL B N   
1280 C CA  . VAL B 77 ? 0.25392 0.20451 0.16004 -0.02819 0.02390  -0.08500 76 VAL B CA  
1281 C C   . VAL B 77 ? 0.24582 0.20530 0.15524 -0.02638 0.02931  -0.09159 76 VAL B C   
1282 O O   . VAL B 77 ? 0.24276 0.20772 0.14816 -0.03098 0.03344  -0.09286 76 VAL B O   
1283 C CB  . VAL B 77 ? 0.27163 0.20526 0.17460 -0.03255 0.01651  -0.08112 76 VAL B CB  
1284 C CG1 . VAL B 77 ? 0.34347 0.27480 0.24090 -0.04096 0.01983  -0.08088 76 VAL B CG1 
1285 C CG2 . VAL B 77 ? 0.48756 0.41007 0.38127 -0.03597 0.01043  -0.07360 76 VAL B CG2 
1286 N N   . SER B 78 ? 0.24350 0.20489 0.16052 -0.01932 0.02903  -0.09700 77 SER B N   
1287 C CA  . SER B 78 ? 0.25122 0.21919 0.16961 -0.01618 0.03204  -0.10155 77 SER B CA  
1288 C C   . SER B 78 ? 0.24180 0.21982 0.15963 -0.01360 0.03425  -0.09556 77 SER B C   
1289 O O   . SER B 78 ? 0.25191 0.23322 0.17000 -0.01340 0.03375  -0.09439 77 SER B O   
1290 C CB  . SER B 78 ? 0.24112 0.20868 0.16608 -0.00873 0.03076  -0.10652 77 SER B CB  
1291 O OG  . SER B 78 ? 0.35290 0.31028 0.28237 -0.00959 0.02548  -0.11097 77 SER B OG  
1292 N N   . ASP B 79 ? 0.22325 0.20477 0.14141 -0.01179 0.03571  -0.09289 78 ASP B N   
1293 C CA  . ASP B 79 ? 0.21526 0.20322 0.13262 -0.01068 0.03652  -0.08766 78 ASP B CA  
1294 C C   . ASP B 79 ? 0.21263 0.20267 0.12846 -0.01553 0.03555  -0.08559 78 ASP B C   
1295 O O   . ASP B 79 ? 0.27668 0.27037 0.19385 -0.01432 0.03439  -0.08437 78 ASP B O   
1296 C CB  . ASP B 79 ? 0.21238 0.20297 0.13148 -0.00983 0.03817  -0.08635 78 ASP B CB  
1297 C CG  . ASP B 79 ? 0.25072 0.24308 0.17414 -0.00545 0.04109  -0.08893 78 ASP B CG  
1298 O OD1 . ASP B 79 ? 0.22596 0.21809 0.14768 -0.00232 0.04201  -0.08952 78 ASP B OD1 
1299 O OD2 . ASP B 79 ? 0.25302 0.24741 0.18186 -0.00524 0.04268  -0.09113 78 ASP B OD2 
1300 N N   . ILE B 80 ? 0.22956 0.21639 0.14159 -0.02145 0.03593  -0.08596 79 ILE B N   
1301 C CA  . ILE B 80 ? 0.21725 0.20738 0.12710 -0.02717 0.03668  -0.08440 79 ILE B CA  
1302 C C   . ILE B 80 ? 0.25821 0.25089 0.17194 -0.02968 0.03748  -0.08734 79 ILE B C   
1303 O O   . ILE B 80 ? 0.26482 0.26492 0.18312 -0.03065 0.03778  -0.08760 79 ILE B O   
1304 C CB  . ILE B 80 ? 0.22869 0.21087 0.12777 -0.03440 0.03711  -0.08388 79 ILE B CB  
1305 C CG1 . ILE B 80 ? 0.29644 0.27926 0.19399 -0.03150 0.03536  -0.08165 79 ILE B CG1 
1306 C CG2 . ILE B 80 ? 0.28772 0.27180 0.18154 -0.04285 0.03985  -0.08312 79 ILE B CG2 
1307 C CD1 . ILE B 80 ? 0.30475 0.27519 0.19554 -0.03375 0.03116  -0.07917 79 ILE B CD1 
1308 N N   . LEU B 81 ? 0.23577 0.22255 0.14956 -0.03036 0.03729  -0.09105 80 LEU B N   
1309 C CA  . LEU B 81 ? 0.22694 0.21541 0.14543 -0.03379 0.03803  -0.09537 80 LEU B CA  
1310 C C   . LEU B 81 ? 0.30370 0.29592 0.22894 -0.02595 0.03473  -0.09701 80 LEU B C   
1311 O O   . LEU B 81 ? 0.28122 0.27612 0.21244 -0.02776 0.03431  -0.10147 80 LEU B O   
1312 C CB  . LEU B 81 ? 0.23999 0.21718 0.15451 -0.03944 0.03829  -0.09938 80 LEU B CB  
1313 C CG  . LEU B 81 ? 0.29224 0.25863 0.19462 -0.04995 0.03993  -0.09670 80 LEU B CG  
1314 C CD1 . LEU B 81 ? 0.27432 0.22693 0.17873 -0.05269 0.03530  -0.09473 80 LEU B CD1 
1315 C CD2 . LEU B 81 ? 0.25708 0.23005 0.15514 -0.05990 0.04594  -0.09682 80 LEU B CD2 
1316 N N   . ALA B 82 ? 0.30079 0.22497 0.14203 -0.00883 0.00131  -0.08034 81 ALA B N   
1317 C CA  . ALA B 82 ? 0.34893 0.28655 0.19847 -0.00649 0.00476  -0.09050 81 ALA B CA  
1318 C C   . ALA B 82 ? 0.27187 0.22934 0.12638 -0.00772 0.00806  -0.08850 81 ALA B C   
1319 O O   . ALA B 82 ? 0.28142 0.24455 0.13492 -0.00795 0.01094  -0.08398 81 ALA B O   
1320 C CB  . ALA B 82 ? 0.31713 0.25979 0.17285 0.00360  0.00492  -0.09533 81 ALA B CB  
1321 N N   . GLU B 83 ? 0.26489 0.23062 0.12529 -0.00751 0.00639  -0.09193 82 GLU B N   
1322 C CA  . GLU B 83 ? 0.31022 0.29320 0.17756 -0.00655 0.00649  -0.09234 82 GLU B CA  
1323 C C   . GLU B 83 ? 0.34357 0.32769 0.20589 -0.00081 0.00167  -0.09094 82 GLU B C   
1324 O O   . GLU B 83 ? 0.32569 0.32514 0.19080 0.00043  -0.00478 -0.09568 82 GLU B O   
1325 C CB  . GLU B 83 ? 0.34232 0.34128 0.21966 -0.01712 0.00742  -0.10195 82 GLU B CB  
1326 C CG  . GLU B 83 ? 0.45021 0.44343 0.32482 -0.02741 0.01640  -0.09956 82 GLU B CG  
1327 C CD  . GLU B 83 ? 0.48091 0.49039 0.37051 -0.04122 0.02192  -0.10517 82 GLU B CD  
1328 O OE1 . GLU B 83 ? 0.70776 0.73070 0.61118 -0.04461 0.01601  -0.11251 82 GLU B OE1 
1329 O OE2 . GLU B 83 ? 0.57544 0.58586 0.46164 -0.05094 0.03283  -0.10338 82 GLU B OE2 
1330 N N   . ASP B 84 ? 0.28189 0.25274 0.13553 0.00191  0.00419  -0.08613 83 ASP B N   
1331 C CA  . ASP B 84 ? 0.28433 0.25220 0.12501 0.00254  0.00348  -0.08455 83 ASP B CA  
1332 C C   . ASP B 84 ? 0.31207 0.27387 0.14763 0.00435  0.00920  -0.07909 83 ASP B C   
1333 O O   . ASP B 84 ? 0.29704 0.25551 0.12318 0.00646  0.01107  -0.07783 83 ASP B O   
1334 C CB  . ASP B 84 ? 0.28464 0.24532 0.11941 0.00163  0.00440  -0.08938 83 ASP B CB  
1335 C CG  . ASP B 84 ? 0.33462 0.29021 0.17902 0.00484  0.01043  -0.09163 83 ASP B CG  
1336 O OD1 . ASP B 84 ? 0.30642 0.26276 0.15871 0.00601  0.01144  -0.08838 83 ASP B OD1 
1337 O OD2 . ASP B 84 ? 0.33364 0.28652 0.17774 0.00589  0.01389  -0.09890 83 ASP B OD2 
1338 N N   . TRP B 85 ? 0.26078 0.22421 0.10422 0.00565  0.01134  -0.07732 84 TRP B N   
1339 C CA  . TRP B 85 ? 0.27102 0.22921 0.11232 0.00709  0.01542  -0.07395 84 TRP B CA  
1340 C C   . TRP B 85 ? 0.31379 0.27564 0.14464 0.00859  0.01384  -0.07597 84 TRP B C   
1341 O O   . TRP B 85 ? 0.32286 0.28074 0.14747 0.01750  0.00587  -0.07623 84 TRP B O   
1342 C CB  . TRP B 85 ? 0.25253 0.21221 0.10296 0.00928  0.01625  -0.07414 84 TRP B CB  
1343 C CG  . TRP B 85 ? 0.24630 0.20849 0.10196 0.00801  0.01496  -0.07462 84 TRP B CG  
1344 C CD1 . TRP B 85 ? 0.24610 0.20899 0.10256 0.00616  0.01254  -0.07578 84 TRP B CD1 
1345 C CD2 . TRP B 85 ? 0.24593 0.21152 0.10483 0.00665  0.01571  -0.07686 84 TRP B CD2 
1346 N NE1 . TRP B 85 ? 0.24957 0.21165 0.10488 0.00478  0.01006  -0.07786 84 TRP B NE1 
1347 C CE2 . TRP B 85 ? 0.25114 0.21813 0.11125 0.00512  0.01177  -0.07952 84 TRP B CE2 
1348 C CE3 . TRP B 85 ? 0.26621 0.23664 0.12753 0.00437  0.01972  -0.07936 84 TRP B CE3 
1349 C CZ2 . TRP B 85 ? 0.24933 0.22657 0.11620 0.00533  0.00835  -0.08625 84 TRP B CZ2 
1350 C CZ3 . TRP B 85 ? 0.24764 0.22951 0.11852 0.00076  0.02004  -0.08609 84 TRP B CZ3 
1351 C CH2 . TRP B 85 ? 0.25487 0.24267 0.13043 0.00329  0.01271  -0.09040 84 TRP B CH2 
1352 N N   . ASN B 86 ? 0.30940 0.26024 0.12766 0.00653  0.01842  -0.07272 85 ASN B N   
1353 C CA  . ASN B 86 ? 0.34869 0.26999 0.13863 0.00905  0.01663  -0.06561 85 ASN B CA  
1354 C C   . ASN B 86 ? 0.45424 0.35922 0.24160 0.00222  0.02620  -0.06490 85 ASN B C   
1355 O O   . ASN B 86 ? 0.34628 0.26451 0.14517 -0.00652 0.03398  -0.07009 85 ASN B O   
1356 C CB  . ASN B 86 ? 0.48089 0.39332 0.24160 0.00500  0.01268  -0.05802 85 ASN B CB  
1357 C CG  . ASN B 86 ? 0.70547 0.63742 0.47339 -0.00515 0.02237  -0.06311 85 ASN B CG  
1358 O OD1 . ASN B 86 ? 0.86933 0.80053 0.64075 -0.01294 0.03351  -0.06435 85 ASN B OD1 
1359 N ND2 . ASN B 86 ? 0.58805 0.53804 0.36229 -0.00332 0.01768  -0.06762 85 ASN B ND2 
1360 N N   . ILE B 87 ? 0.35707 0.23754 0.13976 0.00755  0.02288  -0.05768 86 ILE B N   
1361 C CA  . ILE B 87 ? 0.38020 0.23553 0.15450 -0.00172 0.03182  -0.05606 86 ILE B CA  
1362 C C   . ILE B 87 ? 0.46306 0.29886 0.20588 -0.01456 0.03647  -0.04504 86 ILE B C   
1363 O O   . ILE B 87 ? 0.54396 0.36813 0.26417 -0.01051 0.02735  -0.03286 86 ILE B O   
1364 C CB  . ILE B 87 ? 0.42702 0.25726 0.20955 0.01011  0.02735  -0.05430 86 ILE B CB  
1365 C CG1 . ILE B 87 ? 0.38295 0.23678 0.19354 0.01810  0.02832  -0.06862 86 ILE B CG1 
1366 C CG2 . ILE B 87 ? 0.56663 0.36309 0.33802 -0.00155 0.03681  -0.05342 86 ILE B CG2 
1367 C CD1 . ILE B 87 ? 0.50485 0.34171 0.33149 0.03269  0.02632  -0.07258 86 ILE B CD1 
1368 N N   . VAL B 88 ? 0.42121 0.25623 0.16134 -0.03235 0.05081  -0.05011 87 VAL B N   
1369 C CA  . VAL B 88 ? 0.53126 0.35119 0.24206 -0.05094 0.06183  -0.04267 87 VAL B CA  
1370 C C   . VAL B 88 ? 0.50358 0.27909 0.19832 -0.06103 0.06666  -0.03356 87 VAL B C   
1371 O O   . VAL B 88 ? 0.53978 0.31115 0.25487 -0.06260 0.06982  -0.04292 87 VAL B O   
1372 C CB  . VAL B 88 ? 0.43511 0.29167 0.16228 -0.06570 0.07693  -0.05808 87 VAL B CB  
1373 C CG1 . VAL B 88 ? 0.61491 0.46080 0.31395 -0.08911 0.09409  -0.05392 87 VAL B CG1 
1374 C CG2 . VAL B 88 ? 0.48885 0.38251 0.23780 -0.05283 0.06994  -0.06550 87 VAL B CG2 
1375 N N   . GLU B 89 ? 0.68858 0.42749 0.34263 -0.07033 0.06760  -0.01549 88 GLU B N   
1376 C CA  . GLU B 89 ? 0.79595 0.48221 0.42850 -0.08300 0.07304  -0.00391 88 GLU B CA  
1377 C C   . GLU B 89 ? 0.82916 0.52302 0.46300 -0.11409 0.09666  -0.01418 88 GLU B C   
1378 O O   . GLU B 89 ? 1.01159 0.67333 0.64533 -0.12699 0.10383  -0.01471 88 GLU B O   
1379 C CB  . GLU B 89 ? 0.89560 0.53385 0.47746 -0.08283 0.06298  0.02332  88 GLU B CB  
1380 C CG  . GLU B 89 ? 1.11413 0.74051 0.70234 -0.05099 0.03625  0.03369  88 GLU B CG  
1381 C CD  . GLU B 89 ? 1.27222 0.89119 0.90172 -0.03296 0.03180  0.02239  88 GLU B CD  
1382 O OE1 . GLU B 89 ? 1.52376 1.09055 1.14405 -0.03535 0.03311  0.03015  88 GLU B OE1 
1383 O OE2 . GLU B 89 ? 1.06377 0.72650 0.73244 -0.01849 0.02885  0.00473  88 GLU B OE2 
# 
