data_9AVC
# 
_entry.id   9AVC 
# 
_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   9AVC         pdb_00009avc 10.2210/pdb9avc/pdb 
WWPDB D_1000280736 ?            ?                   
# 
_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       2025-05-21 
_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                        9AVC 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-01 
_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 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              soichi.wakatsuki@stanford.edu 
_pdbx_contact_author.name_first         Soichi 
_pdbx_contact_author.name_last          Wakatsuki 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5896-7968 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mathews, I.I.' 1 0000-0001-6254-3519 
'Pokhrel, S.'   2 0000-0003-2258-8768 
'Wakatsuki, S.' 3 0000-0001-5896-7968 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                4187 
_citation.page_last                 4187 
_citation.title                     
'A hidden cysteine in Fis1 targeted to prevent excessive mitochondrial fission and dysfunction under oxidative stress.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59434-6 
_citation.pdbx_database_id_PubMed   40328741 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pokhrel, S.'      1 0000-0003-2258-8768 
primary 'Heo, G.'          2 0000-0001-5324-4074 
primary 'Mathews, I.'      3 0000-0001-6254-3519 
primary 'Yokoi, S.'        4 0000-0003-2684-3420 
primary 'Matsui, T.'       5 0000-0001-7101-5259 
primary 'Mitsutake, A.'    6 0000-0002-4194-7255 
primary 'Wakatsuki, S.'    7 0000-0001-5896-7968 
primary 'Mochly-Rosen, D.' 8 0000-0002-6691-8733 
# 
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 'Mitochondrial fission 1 protein' 15045.287 2  ? Y38E ? ? 
2 water   nat water                             18.015    81 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'FIS1 homolog,hFis1,Tetratricopeptide repeat protein 11,TPR repeat protein 11' 
# 
_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       
;MEAVLNELVSVEDLLKFEKKFQSEKAAGSVSKSTQFEEAWCLVRSKYNDDIRKGIVLLEELLPKGSKEEQRDYVFYLAVG
NYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLLEVLFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEAVLNELVSVEDLLKFEKKFQSEKAAGSVSKSTQFEEAWCLVRSKYNDDIRKGIVLLEELLPKGSKEEQRDYVFYLAVG
NYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLLEVLFQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   ALA n 
1 4   VAL n 
1 5   LEU n 
1 6   ASN n 
1 7   GLU n 
1 8   LEU n 
1 9   VAL n 
1 10  SER n 
1 11  VAL n 
1 12  GLU n 
1 13  ASP n 
1 14  LEU n 
1 15  LEU n 
1 16  LYS n 
1 17  PHE n 
1 18  GLU n 
1 19  LYS n 
1 20  LYS n 
1 21  PHE n 
1 22  GLN n 
1 23  SER n 
1 24  GLU n 
1 25  LYS n 
1 26  ALA n 
1 27  ALA n 
1 28  GLY n 
1 29  SER n 
1 30  VAL n 
1 31  SER n 
1 32  LYS n 
1 33  SER n 
1 34  THR n 
1 35  GLN n 
1 36  PHE n 
1 37  GLU n 
1 38  GLU n 
1 39  ALA n 
1 40  TRP n 
1 41  CYS n 
1 42  LEU n 
1 43  VAL n 
1 44  ARG n 
1 45  SER n 
1 46  LYS n 
1 47  TYR n 
1 48  ASN n 
1 49  ASP n 
1 50  ASP n 
1 51  ILE n 
1 52  ARG n 
1 53  LYS n 
1 54  GLY n 
1 55  ILE n 
1 56  VAL n 
1 57  LEU n 
1 58  LEU n 
1 59  GLU n 
1 60  GLU n 
1 61  LEU n 
1 62  LEU n 
1 63  PRO n 
1 64  LYS n 
1 65  GLY n 
1 66  SER n 
1 67  LYS n 
1 68  GLU n 
1 69  GLU n 
1 70  GLN n 
1 71  ARG n 
1 72  ASP n 
1 73  TYR n 
1 74  VAL n 
1 75  PHE n 
1 76  TYR n 
1 77  LEU n 
1 78  ALA n 
1 79  VAL n 
1 80  GLY n 
1 81  ASN n 
1 82  TYR n 
1 83  ARG n 
1 84  LEU n 
1 85  LYS n 
1 86  GLU n 
1 87  TYR n 
1 88  GLU n 
1 89  LYS n 
1 90  ALA n 
1 91  LEU n 
1 92  LYS n 
1 93  TYR n 
1 94  VAL n 
1 95  ARG n 
1 96  GLY n 
1 97  LEU n 
1 98  LEU n 
1 99  GLN n 
1 100 THR n 
1 101 GLU n 
1 102 PRO n 
1 103 GLN n 
1 104 ASN n 
1 105 ASN n 
1 106 GLN n 
1 107 ALA n 
1 108 LYS n 
1 109 GLU n 
1 110 LEU n 
1 111 GLU n 
1 112 ARG n 
1 113 LEU n 
1 114 ILE n 
1 115 ASP n 
1 116 LYS n 
1 117 ALA n 
1 118 MET n 
1 119 LYS n 
1 120 LYS n 
1 121 ASP n 
1 122 GLY n 
1 123 LEU n 
1 124 LEU n 
1 125 GLU n 
1 126 VAL n 
1 127 LEU n 
1 128 PHE n 
1 129 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   129 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'FIS1, TTC11, CGI-135' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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                 'BL21 (DE3)' 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          pET-28a 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
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 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   VAL 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   ASN 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   VAL 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  VAL 11  11  ?   ?   ?   A . n 
A 1 12  GLU 12  12  ?   ?   ?   A . n 
A 1 13  ASP 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  LEU 15  15  ?   ?   ?   A . n 
A 1 16  LYS 16  16  ?   ?   ?   A . n 
A 1 17  PHE 17  17  ?   ?   ?   A . n 
A 1 18  GLU 18  18  ?   ?   ?   A . n 
A 1 19  LYS 19  19  ?   ?   ?   A . n 
A 1 20  LYS 20  20  ?   ?   ?   A . n 
A 1 21  PHE 21  21  ?   ?   ?   A . n 
A 1 22  GLN 22  22  ?   ?   ?   A . n 
A 1 23  SER 23  23  ?   ?   ?   A . n 
A 1 24  GLU 24  24  ?   ?   ?   A . n 
A 1 25  LYS 25  25  ?   ?   ?   A . n 
A 1 26  ALA 26  26  ?   ?   ?   A . n 
A 1 27  ALA 27  27  ?   ?   ?   A . n 
A 1 28  GLY 28  28  ?   ?   ?   A . n 
A 1 29  SER 29  29  ?   ?   ?   A . n 
A 1 30  VAL 30  30  ?   ?   ?   A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  LYS 32  32  32  LYS LYS A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  TRP 40  40  40  TRP TRP A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 GLN 106 106 106 GLN GLN A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 PHE 128 128 ?   ?   ?   A . n 
A 1 129 GLN 129 129 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLU 2   2   ?   ?   ?   B . n 
B 1 3   ALA 3   3   ?   ?   ?   B . n 
B 1 4   VAL 4   4   ?   ?   ?   B . n 
B 1 5   LEU 5   5   ?   ?   ?   B . n 
B 1 6   ASN 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   LEU 8   8   ?   ?   ?   B . n 
B 1 9   VAL 9   9   ?   ?   ?   B . n 
B 1 10  SER 10  10  ?   ?   ?   B . n 
B 1 11  VAL 11  11  ?   ?   ?   B . n 
B 1 12  GLU 12  12  ?   ?   ?   B . n 
B 1 13  ASP 13  13  ?   ?   ?   B . n 
B 1 14  LEU 14  14  ?   ?   ?   B . n 
B 1 15  LEU 15  15  ?   ?   ?   B . n 
B 1 16  LYS 16  16  ?   ?   ?   B . n 
B 1 17  PHE 17  17  ?   ?   ?   B . n 
B 1 18  GLU 18  18  ?   ?   ?   B . n 
B 1 19  LYS 19  19  ?   ?   ?   B . n 
B 1 20  LYS 20  20  ?   ?   ?   B . n 
B 1 21  PHE 21  21  ?   ?   ?   B . n 
B 1 22  GLN 22  22  ?   ?   ?   B . n 
B 1 23  SER 23  23  ?   ?   ?   B . n 
B 1 24  GLU 24  24  ?   ?   ?   B . n 
B 1 25  LYS 25  25  ?   ?   ?   B . n 
B 1 26  ALA 26  26  ?   ?   ?   B . n 
B 1 27  ALA 27  27  ?   ?   ?   B . n 
B 1 28  GLY 28  28  ?   ?   ?   B . n 
B 1 29  SER 29  29  ?   ?   ?   B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  LYS 32  32  32  LYS LYS B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  THR 34  34  34  THR THR B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  PHE 36  36  36  PHE PHE B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  GLU 38  38  38  GLU GLU B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  TRP 40  40  40  TRP TRP B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  VAL 43  43  43  VAL VAL B . n 
B 1 44  ARG 44  44  44  ARG ARG B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  TYR 47  47  47  TYR TYR B . n 
B 1 48  ASN 48  48  48  ASN ASN B . n 
B 1 49  ASP 49  49  49  ASP ASP B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  ILE 51  51  51  ILE ILE B . n 
B 1 52  ARG 52  52  52  ARG ARG B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  PRO 63  63  63  PRO PRO B . n 
B 1 64  LYS 64  64  64  LYS LYS B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  GLU 68  68  68  GLU GLU B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  GLN 70  70  70  GLN GLN B . n 
B 1 71  ARG 71  71  71  ARG ARG B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  TYR 73  73  73  TYR TYR B . n 
B 1 74  VAL 74  74  74  VAL VAL B . n 
B 1 75  PHE 75  75  75  PHE PHE B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  ALA 78  78  78  ALA ALA B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  ASN 81  81  81  ASN ASN B . n 
B 1 82  TYR 82  82  82  TYR TYR B . n 
B 1 83  ARG 83  83  83  ARG ARG B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  LYS 85  85  85  LYS LYS B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  TYR 87  87  87  TYR TYR B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  TYR 93  93  93  TYR TYR B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ARG 95  95  95  ARG ARG B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  GLN 99  99  99  GLN GLN B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 GLU 101 101 101 GLU GLU B . n 
B 1 102 PRO 102 102 102 PRO PRO B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 ASN 104 104 104 ASN ASN B . n 
B 1 105 ASN 105 105 105 ASN ASN B . n 
B 1 106 GLN 106 106 106 GLN GLN B . n 
B 1 107 ALA 107 107 107 ALA ALA B . n 
B 1 108 LYS 108 108 108 LYS LYS B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 ILE 114 114 114 ILE ILE B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 LYS 116 116 116 LYS LYS B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 MET 118 118 118 MET MET B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 VAL 126 126 126 VAL VAL B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 PHE 128 128 ?   ?   ?   B . n 
B 1 129 GLN 129 129 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1  201 53 HOH HOH A . 
C 2 HOH 2  202 67 HOH HOH A . 
C 2 HOH 3  203 8  HOH HOH A . 
C 2 HOH 4  204 58 HOH HOH A . 
C 2 HOH 5  205 7  HOH HOH A . 
C 2 HOH 6  206 23 HOH HOH A . 
C 2 HOH 7  207 22 HOH HOH A . 
C 2 HOH 8  208 12 HOH HOH A . 
C 2 HOH 9  209 17 HOH HOH A . 
C 2 HOH 10 210 9  HOH HOH A . 
C 2 HOH 11 211 47 HOH HOH A . 
C 2 HOH 12 212 10 HOH HOH A . 
C 2 HOH 13 213 76 HOH HOH A . 
C 2 HOH 14 214 1  HOH HOH A . 
C 2 HOH 15 215 64 HOH HOH A . 
C 2 HOH 16 216 5  HOH HOH A . 
C 2 HOH 17 217 42 HOH HOH A . 
C 2 HOH 18 218 26 HOH HOH A . 
C 2 HOH 19 219 73 HOH HOH A . 
C 2 HOH 20 220 11 HOH HOH A . 
C 2 HOH 21 221 49 HOH HOH A . 
C 2 HOH 22 222 45 HOH HOH A . 
C 2 HOH 23 223 39 HOH HOH A . 
C 2 HOH 24 224 36 HOH HOH A . 
C 2 HOH 25 225 60 HOH HOH A . 
C 2 HOH 26 226 37 HOH HOH A . 
C 2 HOH 27 227 62 HOH HOH A . 
C 2 HOH 28 228 4  HOH HOH A . 
C 2 HOH 29 229 6  HOH HOH A . 
C 2 HOH 30 230 3  HOH HOH A . 
C 2 HOH 31 231 13 HOH HOH A . 
C 2 HOH 32 232 50 HOH HOH A . 
C 2 HOH 33 233 74 HOH HOH A . 
C 2 HOH 34 234 41 HOH HOH A . 
C 2 HOH 35 235 34 HOH HOH A . 
C 2 HOH 36 236 43 HOH HOH A . 
C 2 HOH 37 237 2  HOH HOH A . 
C 2 HOH 38 238 63 HOH HOH A . 
C 2 HOH 39 239 66 HOH HOH A . 
C 2 HOH 40 240 65 HOH HOH A . 
C 2 HOH 41 241 79 HOH HOH A . 
C 2 HOH 42 242 56 HOH HOH A . 
C 2 HOH 43 243 15 HOH HOH A . 
C 2 HOH 44 244 57 HOH HOH A . 
C 2 HOH 45 245 40 HOH HOH A . 
C 2 HOH 46 246 30 HOH HOH A . 
C 2 HOH 47 247 61 HOH HOH A . 
C 2 HOH 48 248 35 HOH HOH A . 
C 2 HOH 49 249 25 HOH HOH A . 
D 2 HOH 1  201 54 HOH HOH B . 
D 2 HOH 2  202 38 HOH HOH B . 
D 2 HOH 3  203 27 HOH HOH B . 
D 2 HOH 4  204 28 HOH HOH B . 
D 2 HOH 5  205 33 HOH HOH B . 
D 2 HOH 6  206 48 HOH HOH B . 
D 2 HOH 7  207 80 HOH HOH B . 
D 2 HOH 8  208 14 HOH HOH B . 
D 2 HOH 9  209 44 HOH HOH B . 
D 2 HOH 10 210 51 HOH HOH B . 
D 2 HOH 11 211 52 HOH HOH B . 
D 2 HOH 12 212 46 HOH HOH B . 
D 2 HOH 13 213 81 HOH HOH B . 
D 2 HOH 14 214 16 HOH HOH B . 
D 2 HOH 15 215 19 HOH HOH B . 
D 2 HOH 16 216 18 HOH HOH B . 
D 2 HOH 17 217 71 HOH HOH B . 
D 2 HOH 18 218 72 HOH HOH B . 
D 2 HOH 19 219 32 HOH HOH B . 
D 2 HOH 20 220 31 HOH HOH B . 
D 2 HOH 21 221 78 HOH HOH B . 
D 2 HOH 22 222 77 HOH HOH B . 
D 2 HOH 23 223 69 HOH HOH B . 
D 2 HOH 24 224 59 HOH HOH B . 
D 2 HOH 25 225 75 HOH HOH B . 
D 2 HOH 26 226 55 HOH HOH B . 
D 2 HOH 27 227 20 HOH HOH B . 
D 2 HOH 28 228 29 HOH HOH B . 
D 2 HOH 29 229 68 HOH HOH B . 
D 2 HOH 30 230 24 HOH HOH B . 
D 2 HOH 31 231 21 HOH HOH B . 
D 2 HOH 32 232 70 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 ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.34 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AVC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.470 
_cell.length_a_esd                 ? 
_cell.length_b                     43.070 
_cell.length_b_esd                 ? 
_cell.length_c                     61.240 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9AVC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9AVC 
_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             1.88 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          34.57 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Sodium phosphate dibasic dihydrate, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'Rh coated collimating mirrors, K-B focusing mirrors' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-24 
_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                    'Si(111)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97946 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9AVC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.09 
_reflns.d_resolution_low                               38.1 
_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                                     13234 
_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                           98.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.77 
_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                                0.052000000000000005 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.048 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.09 2.14 ? ? ? ? ? ? 967 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.565                ? ? 1  1 0.605              ? ? ? ? 1.443 ? ? ? ? ? ? 
? ? ? 
2.14 2.2  ? ? ? ? ? ? 933 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.109                ? ? 2  1 0.7390000000000001 ? ? ? ? 1.018 ? ? ? ? ? ? 
? ? ? 
2.20 2.27 ? ? ? ? ? ? 932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.866                ? ? 3  1 0.84               ? ? ? ? 
0.8029999999999999   ? ? ? ? ? ? ? ? ? 
2.27 2.34 ? ? ? ? ? ? 882 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.6829999999999999   ? ? 4  1 0.892              ? ? ? ? 0.633 ? ? ? ? ? ? 
? ? ? 
2.34 2.41 ? ? ? ? ? ? 891 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.516                ? ? 5  1 0.9390000000000001 ? ? ? ? 0.478 ? ? ? ? ? ? 
? ? ? 
2.41 2.5  ? ? ? ? ? ? 827 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.36700000000000005  ? ? 6  1 0.973              ? ? ? ? 
0.33899999999999997  ? ? ? ? ? ? ? ? ? 
2.50 2.59 ? ? ? ? ? ? 809 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.28600000000000003  ? ? 7  1 0.9790000000000001 ? ? ? ? 0.265 ? ? ? ? ? ? 
? ? ? 
2.59 2.7  ? ? ? ? ? ? 810 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.24100000000000002  ? ? 8  1 0.983              ? ? ? ? 0.223 ? ? ? ? ? ? 
? ? ? 
2.70 2.82 ? ? ? ? ? ? 713 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.17600000000000002  ? ? 9  1 0.99               ? ? ? ? 0.162 ? ? ? ? ? ? 
? ? ? 
2.82 2.96 ? ? ? ? ? ? 714 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.11                 ? ? 10 1 0.996              ? ? ? ? 
0.10099999999999999  ? ? ? ? ? ? ? ? ? 
2.96 3.12 ? ? ? ? ? ? 712 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.08900000000000001  ? ? 11 1 0.997              ? ? ? ? 0.083 ? ? ? ? ? ? 
? ? ? 
3.12 3.3  ? ? ? ? ? ? 645 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.069                ? ? 12 1 0.998              ? ? ? ? 0.064 ? ? ? ? ? ? 
? ? ? 
3.30 3.53 ? ? ? ? ? ? 605 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.046                ? ? 13 1 0.9990000000000001 ? ? ? ? 0.042 ? ? ? ? ? ? 
? ? ? 
3.53 3.82 ? ? ? ? ? ? 578 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.038                ? ? 14 1 0.9990000000000001 ? ? ? ? 0.035 ? ? ? ? ? ? 
? ? ? 
3.82 4.18 ? ? ? ? ? ? 502 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.032                ? ? 15 1 0.9990000000000001 ? ? ? ? 
0.028999999999999998 ? ? ? ? ? ? ? ? ? 
4.18 4.67 ? ? ? ? ? ? 483 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.027999999999999997 ? ? 16 1 0.9990000000000001 ? ? ? ? 
0.026000000000000002 ? ? ? ? ? ? ? ? ? 
4.67 5.4  ? ? ? ? ? ? 435 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.027999999999999997 ? ? 17 1 0.9990000000000001 ? ? ? ? 0.025 ? ? ? ? ? ? 
? ? ? 
5.40 6.61 ? ? ? ? ? ? 345 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.027999999999999997 ? ? 18 1 0.9990000000000001 ? ? ? ? 
0.026000000000000002 ? ? ? ? ? ? ? ? ? 
6.61 9.35 ? ? ? ? ? ? 282 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.024                ? ? 19 1 0.9990000000000001 ? ? ? ? 
0.022000000000000002 ? ? ? ? ? ? ? ? ? 
9.35 38.1 ? ? ? ? ? ? 169 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.024                ? ? 20 1 0.9990000000000001 ? ? ? ? 
0.022000000000000002 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9AVC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.09 
_refine.ls_d_res_low                             38.01 
_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                     13227 
_refine.ls_number_reflns_R_free                  661 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.26 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1926 
_refine.ls_R_factor_R_free                       0.2440 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1899 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.57 
_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                            0.30 
_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.pdbx_number_atoms_protein        1615 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             81 
_refine_hist.number_atoms_total               1696 
_refine_hist.d_res_high                       2.09 
_refine_hist.d_res_low                        38.01 
# 
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' ? 0.007 ? 1658 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.896 ? 2223 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.889 ? 222  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.044 ? 240  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 285  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.09 2.25  . . 131 2484 98.00 . . . . 0.2708 . . . . . . . . . . . 0.3207 
'X-RAY DIFFRACTION' 2.25 2.48  . . 130 2490 99.00 . . . . 0.2306 . . . . . . . . . . . 0.3041 
'X-RAY DIFFRACTION' 2.48 2.84  . . 131 2493 98.00 . . . . 0.2214 . . . . . . . . . . . 0.3185 
'X-RAY DIFFRACTION' 2.84 3.57  . . 134 2546 99.00 . . . . 0.2071 . . . . . . . . . . . 0.2669 
'X-RAY DIFFRACTION' 3.57 38.01 . . 135 2553 98.00 . . . . 0.1642 . . . . . . . . . . . 0.2075 
# 
_struct.entry_id                     9AVC 
_struct.title                        'Fis1 Structure Y38E mutation' 
_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        9AVC 
_struct_keywords.text            'FIS1, mitochondrial fission, Drug design, UNKNOWN FUNCTION' 
_struct_keywords.pdbx_keywords   'UNKNOWN FUNCTION' 
# 
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 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FIS1_HUMAN 
_struct_ref.pdbx_db_accession          Q9Y3D6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEAVLNELVSVEDLLKFEKKFQSEKAAGSVSKSTQFEYAWCLVRSKYNDDIRKGIVLLEELLPKGSKEEQRDYVFYLAVG
NYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGL
;
_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 9AVC A 1 ? 123 ? Q9Y3D6 1 ? 123 ? 1 123 
2 1 9AVC B 1 ? 123 ? Q9Y3D6 1 ? 123 ? 1 123 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9AVC GLU A 38  ? UNP Q9Y3D6 TYR 38 'engineered mutation' 38  1  
1 9AVC LEU A 124 ? UNP Q9Y3D6 ?   ?  'expression tag'      124 2  
1 9AVC GLU A 125 ? UNP Q9Y3D6 ?   ?  'expression tag'      125 3  
1 9AVC VAL A 126 ? UNP Q9Y3D6 ?   ?  'expression tag'      126 4  
1 9AVC LEU A 127 ? UNP Q9Y3D6 ?   ?  'expression tag'      127 5  
1 9AVC PHE A 128 ? UNP Q9Y3D6 ?   ?  'expression tag'      128 6  
1 9AVC GLN A 129 ? UNP Q9Y3D6 ?   ?  'expression tag'      129 7  
2 9AVC GLU B 38  ? UNP Q9Y3D6 TYR 38 'engineered mutation' 38  8  
2 9AVC LEU B 124 ? UNP Q9Y3D6 ?   ?  'expression tag'      124 9  
2 9AVC GLU B 125 ? UNP Q9Y3D6 ?   ?  'expression tag'      125 10 
2 9AVC VAL B 126 ? UNP Q9Y3D6 ?   ?  'expression tag'      126 11 
2 9AVC LEU B 127 ? UNP Q9Y3D6 ?   ?  'expression tag'      127 12 
2 9AVC PHE B 128 ? UNP Q9Y3D6 ?   ?  'expression tag'      128 13 
2 9AVC GLN B 129 ? UNP Q9Y3D6 ?   ?  'expression tag'      129 14 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 31  ? ARG A 44  ? SER A 31  ARG A 44  1 ? 14 
HELX_P HELX_P2  AA2 TYR A 47  ? GLY A 65  ? TYR A 47  GLY A 65  1 ? 19 
HELX_P HELX_P3  AA3 SER A 66  ? LEU A 84  ? SER A 66  LEU A 84  1 ? 19 
HELX_P HELX_P4  AA4 GLU A 86  ? GLU A 101 ? GLU A 86  GLU A 101 1 ? 16 
HELX_P HELX_P5  AA5 ASN A 104 ? LYS A 120 ? ASN A 104 LYS A 120 1 ? 17 
HELX_P HELX_P6  AA6 SER B 31  ? ARG B 44  ? SER B 31  ARG B 44  1 ? 14 
HELX_P HELX_P7  AA7 TYR B 47  ? LEU B 62  ? TYR B 47  LEU B 62  1 ? 16 
HELX_P HELX_P8  AA8 PRO B 63  ? GLY B 65  ? PRO B 63  GLY B 65  5 ? 3  
HELX_P HELX_P9  AA9 SER B 66  ? LEU B 84  ? SER B 66  LEU B 84  1 ? 19 
HELX_P HELX_P10 AB1 GLU B 86  ? GLU B 101 ? GLU B 86  GLU B 101 1 ? 16 
HELX_P HELX_P11 AB2 ASN B 104 ? VAL B 126 ? ASN B 104 VAL B 126 1 ? 23 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            41 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            41 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             41 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             41 
_struct_conn.ptnr2_symmetry                1_455 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.049 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       41 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      41 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        41 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       41 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_455 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_pdbx_entry_details.entry_id                   9AVC 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    71 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG1 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   THR 
_pdbx_validate_close_contact.auth_seq_id_2    100 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -0.046 0.063  23.712 0.3592 0.3987 0.3990 0.0525  0.0129 0.0198 4.5332 3.3237 3.4632 1.0460  
0.6531  -0.3956 -0.0036 -0.0538 0.0044 0.3902  0.0623 -0.2708 -0.1571 0.1048 0.1892  
'X-RAY DIFFRACTION' 2 ? refined 17.634 -3.149 8.201  0.3979 0.3790 0.4034 -0.0390 0.0353 0.0366 3.7004 4.5935 4.9237 -1.7270 
-0.3399 2.1254  0.1432  -0.0554 0.0080 -0.0775 0.0581 -0.0445 -0.0590 0.2791 -0.2229 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 31 A 127 '( CHAIN A AND RESID 31:127 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 30 B 127 '( CHAIN B AND RESID 30:127 )' ? ? ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A GLU 2   ? A GLU 2   
3  1 Y 1 A ALA 3   ? A ALA 3   
4  1 Y 1 A VAL 4   ? A VAL 4   
5  1 Y 1 A LEU 5   ? A LEU 5   
6  1 Y 1 A ASN 6   ? A ASN 6   
7  1 Y 1 A GLU 7   ? A GLU 7   
8  1 Y 1 A LEU 8   ? A LEU 8   
9  1 Y 1 A VAL 9   ? A VAL 9   
10 1 Y 1 A SER 10  ? A SER 10  
11 1 Y 1 A VAL 11  ? A VAL 11  
12 1 Y 1 A GLU 12  ? A GLU 12  
13 1 Y 1 A ASP 13  ? A ASP 13  
14 1 Y 1 A LEU 14  ? A LEU 14  
15 1 Y 1 A LEU 15  ? A LEU 15  
16 1 Y 1 A LYS 16  ? A LYS 16  
17 1 Y 1 A PHE 17  ? A PHE 17  
18 1 Y 1 A GLU 18  ? A GLU 18  
19 1 Y 1 A LYS 19  ? A LYS 19  
20 1 Y 1 A LYS 20  ? A LYS 20  
21 1 Y 1 A PHE 21  ? A PHE 21  
22 1 Y 1 A GLN 22  ? A GLN 22  
23 1 Y 1 A SER 23  ? A SER 23  
24 1 Y 1 A GLU 24  ? A GLU 24  
25 1 Y 1 A LYS 25  ? A LYS 25  
26 1 Y 1 A ALA 26  ? A ALA 26  
27 1 Y 1 A ALA 27  ? A ALA 27  
28 1 Y 1 A GLY 28  ? A GLY 28  
29 1 Y 1 A SER 29  ? A SER 29  
30 1 Y 1 A VAL 30  ? A VAL 30  
31 1 Y 1 A PHE 128 ? A PHE 128 
32 1 Y 1 A GLN 129 ? A GLN 129 
33 1 Y 1 B MET 1   ? B MET 1   
34 1 Y 1 B GLU 2   ? B GLU 2   
35 1 Y 1 B ALA 3   ? B ALA 3   
36 1 Y 1 B VAL 4   ? B VAL 4   
37 1 Y 1 B LEU 5   ? B LEU 5   
38 1 Y 1 B ASN 6   ? B ASN 6   
39 1 Y 1 B GLU 7   ? B GLU 7   
40 1 Y 1 B LEU 8   ? B LEU 8   
41 1 Y 1 B VAL 9   ? B VAL 9   
42 1 Y 1 B SER 10  ? B SER 10  
43 1 Y 1 B VAL 11  ? B VAL 11  
44 1 Y 1 B GLU 12  ? B GLU 12  
45 1 Y 1 B ASP 13  ? B ASP 13  
46 1 Y 1 B LEU 14  ? B LEU 14  
47 1 Y 1 B LEU 15  ? B LEU 15  
48 1 Y 1 B LYS 16  ? B LYS 16  
49 1 Y 1 B PHE 17  ? B PHE 17  
50 1 Y 1 B GLU 18  ? B GLU 18  
51 1 Y 1 B LYS 19  ? B LYS 19  
52 1 Y 1 B LYS 20  ? B LYS 20  
53 1 Y 1 B PHE 21  ? B PHE 21  
54 1 Y 1 B GLN 22  ? B GLN 22  
55 1 Y 1 B SER 23  ? B SER 23  
56 1 Y 1 B GLU 24  ? B GLU 24  
57 1 Y 1 B LYS 25  ? B LYS 25  
58 1 Y 1 B ALA 26  ? B ALA 26  
59 1 Y 1 B ALA 27  ? B ALA 27  
60 1 Y 1 B GLY 28  ? B GLY 28  
61 1 Y 1 B SER 29  ? B SER 29  
62 1 Y 1 B PHE 128 ? B PHE 128 
63 1 Y 1 B GLN 129 ? B GLN 129 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HOH O    O N N 137 
HOH H1   H N N 138 
HOH H2   H N N 139 
ILE N    N N N 140 
ILE CA   C N S 141 
ILE C    C N N 142 
ILE O    O N N 143 
ILE CB   C N S 144 
ILE CG1  C N N 145 
ILE CG2  C N N 146 
ILE CD1  C N N 147 
ILE OXT  O N N 148 
ILE H    H N N 149 
ILE H2   H N N 150 
ILE HA   H N N 151 
ILE HB   H N N 152 
ILE HG12 H N N 153 
ILE HG13 H N N 154 
ILE HG21 H N N 155 
ILE HG22 H N N 156 
ILE HG23 H N N 157 
ILE HD11 H N N 158 
ILE HD12 H N N 159 
ILE HD13 H N N 160 
ILE HXT  H N N 161 
LEU N    N N N 162 
LEU CA   C N S 163 
LEU C    C N N 164 
LEU O    O N N 165 
LEU CB   C N N 166 
LEU CG   C N N 167 
LEU CD1  C N N 168 
LEU CD2  C N N 169 
LEU OXT  O N N 170 
LEU H    H N N 171 
LEU H2   H N N 172 
LEU HA   H N N 173 
LEU HB2  H N N 174 
LEU HB3  H N N 175 
LEU HG   H N N 176 
LEU HD11 H N N 177 
LEU HD12 H N N 178 
LEU HD13 H N N 179 
LEU HD21 H N N 180 
LEU HD22 H N N 181 
LEU HD23 H N N 182 
LEU HXT  H N N 183 
LYS N    N N N 184 
LYS CA   C N S 185 
LYS C    C N N 186 
LYS O    O N N 187 
LYS CB   C N N 188 
LYS CG   C N N 189 
LYS CD   C N N 190 
LYS CE   C N N 191 
LYS NZ   N N N 192 
LYS OXT  O N N 193 
LYS H    H N N 194 
LYS H2   H N N 195 
LYS HA   H N N 196 
LYS HB2  H N N 197 
LYS HB3  H N N 198 
LYS HG2  H N N 199 
LYS HG3  H N N 200 
LYS HD2  H N N 201 
LYS HD3  H N N 202 
LYS HE2  H N N 203 
LYS HE3  H N N 204 
LYS HZ1  H N N 205 
LYS HZ2  H N N 206 
LYS HZ3  H N N 207 
LYS HXT  H N N 208 
MET N    N N N 209 
MET CA   C N S 210 
MET C    C N N 211 
MET O    O N N 212 
MET CB   C N N 213 
MET CG   C N N 214 
MET SD   S N N 215 
MET CE   C N N 216 
MET OXT  O N N 217 
MET H    H N N 218 
MET H2   H N N 219 
MET HA   H N N 220 
MET HB2  H N N 221 
MET HB3  H N N 222 
MET HG2  H N N 223 
MET HG3  H N N 224 
MET HE1  H N N 225 
MET HE2  H N N 226 
MET HE3  H N N 227 
MET HXT  H N N 228 
PHE N    N N N 229 
PHE CA   C N S 230 
PHE C    C N N 231 
PHE O    O N N 232 
PHE CB   C N N 233 
PHE CG   C Y N 234 
PHE CD1  C Y N 235 
PHE CD2  C Y N 236 
PHE CE1  C Y N 237 
PHE CE2  C Y N 238 
PHE CZ   C Y N 239 
PHE OXT  O N N 240 
PHE H    H N N 241 
PHE H2   H N N 242 
PHE HA   H N N 243 
PHE HB2  H N N 244 
PHE HB3  H N N 245 
PHE HD1  H N N 246 
PHE HD2  H N N 247 
PHE HE1  H N N 248 
PHE HE2  H N N 249 
PHE HZ   H N N 250 
PHE HXT  H N N 251 
PRO N    N N N 252 
PRO CA   C N S 253 
PRO C    C N N 254 
PRO O    O N N 255 
PRO CB   C N N 256 
PRO CG   C N N 257 
PRO CD   C N N 258 
PRO OXT  O N N 259 
PRO H    H N N 260 
PRO HA   H N N 261 
PRO HB2  H N N 262 
PRO HB3  H N N 263 
PRO HG2  H N N 264 
PRO HG3  H N N 265 
PRO HD2  H N N 266 
PRO HD3  H N N 267 
PRO HXT  H N N 268 
SER N    N N N 269 
SER CA   C N S 270 
SER C    C N N 271 
SER O    O N N 272 
SER CB   C N N 273 
SER OG   O N N 274 
SER OXT  O N N 275 
SER H    H N N 276 
SER H2   H N N 277 
SER HA   H N N 278 
SER HB2  H N N 279 
SER HB3  H N N 280 
SER HG   H N N 281 
SER HXT  H N N 282 
THR N    N N N 283 
THR CA   C N S 284 
THR C    C N N 285 
THR O    O N N 286 
THR CB   C N R 287 
THR OG1  O N N 288 
THR CG2  C N N 289 
THR OXT  O N N 290 
THR H    H N N 291 
THR H2   H N N 292 
THR HA   H N N 293 
THR HB   H N N 294 
THR HG1  H N N 295 
THR HG21 H N N 296 
THR HG22 H N N 297 
THR HG23 H N N 298 
THR HXT  H N N 299 
TRP N    N N N 300 
TRP CA   C N S 301 
TRP C    C N N 302 
TRP O    O N N 303 
TRP CB   C N N 304 
TRP CG   C Y N 305 
TRP CD1  C Y N 306 
TRP CD2  C Y N 307 
TRP NE1  N Y N 308 
TRP CE2  C Y N 309 
TRP CE3  C Y N 310 
TRP CZ2  C Y N 311 
TRP CZ3  C Y N 312 
TRP CH2  C Y N 313 
TRP OXT  O N N 314 
TRP H    H N N 315 
TRP H2   H N N 316 
TRP HA   H N N 317 
TRP HB2  H N N 318 
TRP HB3  H N N 319 
TRP HD1  H N N 320 
TRP HE1  H N N 321 
TRP HE3  H N N 322 
TRP HZ2  H N N 323 
TRP HZ3  H N N 324 
TRP HH2  H N N 325 
TRP HXT  H N N 326 
TYR N    N N N 327 
TYR CA   C N S 328 
TYR C    C N N 329 
TYR O    O N N 330 
TYR CB   C N N 331 
TYR CG   C Y N 332 
TYR CD1  C Y N 333 
TYR CD2  C Y N 334 
TYR CE1  C Y N 335 
TYR CE2  C Y N 336 
TYR CZ   C Y N 337 
TYR OH   O N N 338 
TYR OXT  O N N 339 
TYR H    H N N 340 
TYR H2   H N N 341 
TYR HA   H N N 342 
TYR HB2  H N N 343 
TYR HB3  H N N 344 
TYR HD1  H N N 345 
TYR HD2  H N N 346 
TYR HE1  H N N 347 
TYR HE2  H N N 348 
TYR HH   H N N 349 
TYR HXT  H N N 350 
VAL N    N N N 351 
VAL CA   C N S 352 
VAL C    C N N 353 
VAL O    O N N 354 
VAL CB   C N N 355 
VAL CG1  C N N 356 
VAL CG2  C N N 357 
VAL OXT  O N N 358 
VAL H    H N N 359 
VAL H2   H N N 360 
VAL HA   H N N 361 
VAL HB   H N N 362 
VAL HG11 H N N 363 
VAL HG12 H N N 364 
VAL HG13 H N N 365 
VAL HG21 H N N 366 
VAL HG22 H N N 367 
VAL HG23 H N N 368 
VAL HXT  H N N 369 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HOH O   H1   sing N N 129 
HOH O   H2   sing N N 130 
ILE N   CA   sing N N 131 
ILE N   H    sing N N 132 
ILE N   H2   sing N N 133 
ILE CA  C    sing N N 134 
ILE CA  CB   sing N N 135 
ILE CA  HA   sing N N 136 
ILE C   O    doub N N 137 
ILE C   OXT  sing N N 138 
ILE CB  CG1  sing N N 139 
ILE CB  CG2  sing N N 140 
ILE CB  HB   sing N N 141 
ILE CG1 CD1  sing N N 142 
ILE CG1 HG12 sing N N 143 
ILE CG1 HG13 sing N N 144 
ILE CG2 HG21 sing N N 145 
ILE CG2 HG22 sing N N 146 
ILE CG2 HG23 sing N N 147 
ILE CD1 HD11 sing N N 148 
ILE CD1 HD12 sing N N 149 
ILE CD1 HD13 sing N N 150 
ILE OXT HXT  sing N N 151 
LEU N   CA   sing N N 152 
LEU N   H    sing N N 153 
LEU N   H2   sing N N 154 
LEU CA  C    sing N N 155 
LEU CA  CB   sing N N 156 
LEU CA  HA   sing N N 157 
LEU C   O    doub N N 158 
LEU C   OXT  sing N N 159 
LEU CB  CG   sing N N 160 
LEU CB  HB2  sing N N 161 
LEU CB  HB3  sing N N 162 
LEU CG  CD1  sing N N 163 
LEU CG  CD2  sing N N 164 
LEU CG  HG   sing N N 165 
LEU CD1 HD11 sing N N 166 
LEU CD1 HD12 sing N N 167 
LEU CD1 HD13 sing N N 168 
LEU CD2 HD21 sing N N 169 
LEU CD2 HD22 sing N N 170 
LEU CD2 HD23 sing N N 171 
LEU OXT HXT  sing N N 172 
LYS N   CA   sing N N 173 
LYS N   H    sing N N 174 
LYS N   H2   sing N N 175 
LYS CA  C    sing N N 176 
LYS CA  CB   sing N N 177 
LYS CA  HA   sing N N 178 
LYS C   O    doub N N 179 
LYS C   OXT  sing N N 180 
LYS CB  CG   sing N N 181 
LYS CB  HB2  sing N N 182 
LYS CB  HB3  sing N N 183 
LYS CG  CD   sing N N 184 
LYS CG  HG2  sing N N 185 
LYS CG  HG3  sing N N 186 
LYS CD  CE   sing N N 187 
LYS CD  HD2  sing N N 188 
LYS CD  HD3  sing N N 189 
LYS CE  NZ   sing N N 190 
LYS CE  HE2  sing N N 191 
LYS CE  HE3  sing N N 192 
LYS NZ  HZ1  sing N N 193 
LYS NZ  HZ2  sing N N 194 
LYS NZ  HZ3  sing N N 195 
LYS OXT HXT  sing N N 196 
MET N   CA   sing N N 197 
MET N   H    sing N N 198 
MET N   H2   sing N N 199 
MET CA  C    sing N N 200 
MET CA  CB   sing N N 201 
MET CA  HA   sing N N 202 
MET C   O    doub N N 203 
MET C   OXT  sing N N 204 
MET CB  CG   sing N N 205 
MET CB  HB2  sing N N 206 
MET CB  HB3  sing N N 207 
MET CG  SD   sing N N 208 
MET CG  HG2  sing N N 209 
MET CG  HG3  sing N N 210 
MET SD  CE   sing N N 211 
MET CE  HE1  sing N N 212 
MET CE  HE2  sing N N 213 
MET CE  HE3  sing N N 214 
MET OXT HXT  sing N N 215 
PHE N   CA   sing N N 216 
PHE N   H    sing N N 217 
PHE N   H2   sing N N 218 
PHE CA  C    sing N N 219 
PHE CA  CB   sing N N 220 
PHE CA  HA   sing N N 221 
PHE C   O    doub N N 222 
PHE C   OXT  sing N N 223 
PHE CB  CG   sing N N 224 
PHE CB  HB2  sing N N 225 
PHE CB  HB3  sing N N 226 
PHE CG  CD1  doub Y N 227 
PHE CG  CD2  sing Y N 228 
PHE CD1 CE1  sing Y N 229 
PHE CD1 HD1  sing N N 230 
PHE CD2 CE2  doub Y N 231 
PHE CD2 HD2  sing N N 232 
PHE CE1 CZ   doub Y N 233 
PHE CE1 HE1  sing N N 234 
PHE CE2 CZ   sing Y N 235 
PHE CE2 HE2  sing N N 236 
PHE CZ  HZ   sing N N 237 
PHE OXT HXT  sing N N 238 
PRO N   CA   sing N N 239 
PRO N   CD   sing N N 240 
PRO N   H    sing N N 241 
PRO CA  C    sing N N 242 
PRO CA  CB   sing N N 243 
PRO CA  HA   sing N N 244 
PRO C   O    doub N N 245 
PRO C   OXT  sing N N 246 
PRO CB  CG   sing N N 247 
PRO CB  HB2  sing N N 248 
PRO CB  HB3  sing N N 249 
PRO CG  CD   sing N N 250 
PRO CG  HG2  sing N N 251 
PRO CG  HG3  sing N N 252 
PRO CD  HD2  sing N N 253 
PRO CD  HD3  sing N N 254 
PRO OXT HXT  sing N N 255 
SER N   CA   sing N N 256 
SER N   H    sing N N 257 
SER N   H2   sing N N 258 
SER CA  C    sing N N 259 
SER CA  CB   sing N N 260 
SER CA  HA   sing N N 261 
SER C   O    doub N N 262 
SER C   OXT  sing N N 263 
SER CB  OG   sing N N 264 
SER CB  HB2  sing N N 265 
SER CB  HB3  sing N N 266 
SER OG  HG   sing N N 267 
SER OXT HXT  sing N N 268 
THR N   CA   sing N N 269 
THR N   H    sing N N 270 
THR N   H2   sing N N 271 
THR CA  C    sing N N 272 
THR CA  CB   sing N N 273 
THR CA  HA   sing N N 274 
THR C   O    doub N N 275 
THR C   OXT  sing N N 276 
THR CB  OG1  sing N N 277 
THR CB  CG2  sing N N 278 
THR CB  HB   sing N N 279 
THR OG1 HG1  sing N N 280 
THR CG2 HG21 sing N N 281 
THR CG2 HG22 sing N N 282 
THR CG2 HG23 sing N N 283 
THR OXT HXT  sing N N 284 
TRP N   CA   sing N N 285 
TRP N   H    sing N N 286 
TRP N   H2   sing N N 287 
TRP CA  C    sing N N 288 
TRP CA  CB   sing N N 289 
TRP CA  HA   sing N N 290 
TRP C   O    doub N N 291 
TRP C   OXT  sing N N 292 
TRP CB  CG   sing N N 293 
TRP CB  HB2  sing N N 294 
TRP CB  HB3  sing N N 295 
TRP CG  CD1  doub Y N 296 
TRP CG  CD2  sing Y N 297 
TRP CD1 NE1  sing Y N 298 
TRP CD1 HD1  sing N N 299 
TRP CD2 CE2  doub Y N 300 
TRP CD2 CE3  sing Y N 301 
TRP NE1 CE2  sing Y N 302 
TRP NE1 HE1  sing N N 303 
TRP CE2 CZ2  sing Y N 304 
TRP CE3 CZ3  doub Y N 305 
TRP CE3 HE3  sing N N 306 
TRP CZ2 CH2  doub Y N 307 
TRP CZ2 HZ2  sing N N 308 
TRP CZ3 CH2  sing Y N 309 
TRP CZ3 HZ3  sing N N 310 
TRP CH2 HH2  sing N N 311 
TRP OXT HXT  sing N N 312 
TYR N   CA   sing N N 313 
TYR N   H    sing N N 314 
TYR N   H2   sing N N 315 
TYR CA  C    sing N N 316 
TYR CA  CB   sing N N 317 
TYR CA  HA   sing N N 318 
TYR C   O    doub N N 319 
TYR C   OXT  sing N N 320 
TYR CB  CG   sing N N 321 
TYR CB  HB2  sing N N 322 
TYR CB  HB3  sing N N 323 
TYR CG  CD1  doub Y N 324 
TYR CG  CD2  sing Y N 325 
TYR CD1 CE1  sing Y N 326 
TYR CD1 HD1  sing N N 327 
TYR CD2 CE2  doub Y N 328 
TYR CD2 HD2  sing N N 329 
TYR CE1 CZ   doub Y N 330 
TYR CE1 HE1  sing N N 331 
TYR CE2 CZ   sing Y N 332 
TYR CE2 HE2  sing N N 333 
TYR CZ  OH   sing N N 334 
TYR OH  HH   sing N N 335 
TYR OXT HXT  sing N N 336 
VAL N   CA   sing N N 337 
VAL N   H    sing N N 338 
VAL N   H2   sing N N 339 
VAL CA  C    sing N N 340 
VAL CA  CB   sing N N 341 
VAL CA  HA   sing N N 342 
VAL C   O    doub N N 343 
VAL C   OXT  sing N N 344 
VAL CB  CG1  sing N N 345 
VAL CB  CG2  sing N N 346 
VAL CB  HB   sing N N 347 
VAL CG1 HG11 sing N N 348 
VAL CG1 HG12 sing N N 349 
VAL CG1 HG13 sing N N 350 
VAL CG2 HG21 sing N N 351 
VAL CG2 HG22 sing N N 352 
VAL CG2 HG23 sing N N 353 
VAL OXT HXT  sing N N 354 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Department of Energy (DOE, United States)'                                                'United States' DE-AC02-76SF00515 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' P30GM133894       2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Wild type structure' 
# 
_atom_sites.entry_id                    9AVC 
_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]   0.023004 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003784 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023218 
_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]   0.016549 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 31  ? -5.104  4.507   3.747   1.00 77.73  ? 31  SER A N   1 
ATOM   2    C CA  . SER A 1 31  ? -4.646  5.782   4.295   1.00 87.68  ? 31  SER A CA  1 
ATOM   3    C C   . SER A 1 31  ? -4.188  5.629   5.749   1.00 89.69  ? 31  SER A C   1 
ATOM   4    O O   . SER A 1 31  ? -4.431  4.600   6.382   1.00 75.34  ? 31  SER A O   1 
ATOM   5    C CB  . SER A 1 31  ? -5.750  6.838   4.207   1.00 89.42  ? 31  SER A CB  1 
ATOM   6    O OG  . SER A 1 31  ? -6.567  6.816   5.365   1.00 88.73  ? 31  SER A OG  1 
ATOM   7    N N   . LYS A 1 32  ? -3.523  6.665   6.274   1.00 94.46  ? 32  LYS A N   1 
ATOM   8    C CA  . LYS A 1 32  ? -3.021  6.610   7.646   1.00 89.29  ? 32  LYS A CA  1 
ATOM   9    C C   . LYS A 1 32  ? -4.157  6.637   8.658   1.00 79.13  ? 32  LYS A C   1 
ATOM   10   O O   . LYS A 1 32  ? -4.117  5.916   9.661   1.00 73.56  ? 32  LYS A O   1 
ATOM   11   C CB  . LYS A 1 32  ? -2.065  7.771   7.910   1.00 87.86  ? 32  LYS A CB  1 
ATOM   12   C CG  . LYS A 1 32  ? -0.595  7.462   7.687   1.00 90.47  ? 32  LYS A CG  1 
ATOM   13   C CD  . LYS A 1 32  ? 0.274   8.600   8.202   1.00 86.88  ? 32  LYS A CD  1 
ATOM   14   C CE  . LYS A 1 32  ? -0.408  9.953   7.976   1.00 89.69  ? 32  LYS A CE  1 
ATOM   15   N NZ  . LYS A 1 32  ? 0.013   10.994  8.956   1.00 88.97  ? 32  LYS A NZ  1 
ATOM   16   N N   . SER A 1 33  ? -5.170  7.476   8.425   1.00 81.71  ? 33  SER A N   1 
ATOM   17   C CA  . SER A 1 33  ? -6.242  7.611   9.404   1.00 83.21  ? 33  SER A CA  1 
ATOM   18   C C   . SER A 1 33  ? -7.038  6.317   9.539   1.00 77.59  ? 33  SER A C   1 
ATOM   19   O O   . SER A 1 33  ? -7.361  5.893   10.655  1.00 73.54  ? 33  SER A O   1 
ATOM   20   C CB  . SER A 1 33  ? -7.144  8.784   9.027   1.00 86.39  ? 33  SER A CB  1 
ATOM   21   O OG  . SER A 1 33  ? -7.581  8.679   7.684   1.00 92.49  ? 33  SER A OG  1 
ATOM   22   N N   . THR A 1 34  ? -7.328  5.653   8.419   1.00 65.18  ? 34  THR A N   1 
ATOM   23   C CA  . THR A 1 34  ? -8.147  4.450   8.481   1.00 77.95  ? 34  THR A CA  1 
ATOM   24   C C   . THR A 1 34  ? -7.362  3.236   8.971   1.00 85.43  ? 34  THR A C   1 
ATOM   25   O O   . THR A 1 34  ? -7.947  2.333   9.589   1.00 64.99  ? 34  THR A O   1 
ATOM   26   C CB  . THR A 1 34  ? -8.790  4.179   7.120   1.00 87.04  ? 34  THR A CB  1 
ATOM   27   O OG1 . THR A 1 34  ? -7.871  3.464   6.287   1.00 88.87  ? 34  THR A OG1 1 
ATOM   28   C CG2 . THR A 1 34  ? -9.212  5.489   6.445   1.00 67.56  ? 34  THR A CG2 1 
ATOM   29   N N   . GLN A 1 35  ? -6.045  3.195   8.739   1.00 77.35  ? 35  GLN A N   1 
ATOM   30   C CA  . GLN A 1 35  ? -5.252  2.142   9.367   1.00 60.82  ? 35  GLN A CA  1 
ATOM   31   C C   . GLN A 1 35  ? -5.210  2.313   10.879  1.00 61.24  ? 35  GLN A C   1 
ATOM   32   O O   . GLN A 1 35  ? -5.310  1.329   11.627  1.00 53.26  ? 35  GLN A O   1 
ATOM   33   C CB  . GLN A 1 35  ? -3.836  2.119   8.798   1.00 61.37  ? 35  GLN A CB  1 
ATOM   34   C CG  . GLN A 1 35  ? -3.712  1.319   7.516   1.00 76.01  ? 35  GLN A CG  1 
ATOM   35   C CD  . GLN A 1 35  ? -2.284  1.247   7.019   1.00 88.74  ? 35  GLN A CD  1 
ATOM   36   O OE1 . GLN A 1 35  ? -1.716  2.249   6.567   1.00 86.21  ? 35  GLN A OE1 1 
ATOM   37   N NE2 . GLN A 1 35  ? -1.683  0.059   7.120   1.00 85.70  ? 35  GLN A NE2 1 
ATOM   38   N N   . PHE A 1 36  ? -5.045  3.550   11.352  1.00 52.39  ? 36  PHE A N   1 
ATOM   39   C CA  . PHE A 1 36  ? -5.099  3.769   12.791  1.00 55.61  ? 36  PHE A CA  1 
ATOM   40   C C   . PHE A 1 36  ? -6.471  3.419   13.342  1.00 46.48  ? 36  PHE A C   1 
ATOM   41   O O   . PHE A 1 36  ? -6.578  2.817   14.413  1.00 48.21  ? 36  PHE A O   1 
ATOM   42   C CB  . PHE A 1 36  ? -4.757  5.212   13.143  1.00 53.91  ? 36  PHE A CB  1 
ATOM   43   C CG  . PHE A 1 36  ? -4.797  5.483   14.623  1.00 58.40  ? 36  PHE A CG  1 
ATOM   44   C CD1 . PHE A 1 36  ? -3.909  4.853   15.482  1.00 47.21  ? 36  PHE A CD1 1 
ATOM   45   C CD2 . PHE A 1 36  ? -5.769  6.322   15.159  1.00 58.85  ? 36  PHE A CD2 1 
ATOM   46   C CE1 . PHE A 1 36  ? -3.956  5.088   16.855  1.00 57.80  ? 36  PHE A CE1 1 
ATOM   47   C CE2 . PHE A 1 36  ? -5.826  6.562   16.519  1.00 49.60  ? 36  PHE A CE2 1 
ATOM   48   C CZ  . PHE A 1 36  ? -4.920  5.953   17.370  1.00 52.23  ? 36  PHE A CZ  1 
ATOM   49   N N   . GLU A 1 37  ? -7.531  3.793   12.629  1.00 53.45  ? 37  GLU A N   1 
ATOM   50   C CA  . GLU A 1 37  ? -8.868  3.428   13.083  1.00 63.34  ? 37  GLU A CA  1 
ATOM   51   C C   . GLU A 1 37  ? -9.010  1.922   13.197  1.00 52.37  ? 37  GLU A C   1 
ATOM   52   O O   . GLU A 1 37  ? -9.616  1.429   14.153  1.00 50.84  ? 37  GLU A O   1 
ATOM   53   C CB  . GLU A 1 37  ? -9.938  3.999   12.156  1.00 62.18  ? 37  GLU A CB  1 
ATOM   54   C CG  . GLU A 1 37  ? -10.158 5.490   12.309  1.00 76.81  ? 37  GLU A CG  1 
ATOM   55   C CD  . GLU A 1 37  ? -11.022 6.076   11.197  1.00 79.55  ? 37  GLU A CD  1 
ATOM   56   O OE1 . GLU A 1 37  ? -11.251 5.400   10.167  1.00 75.37  ? 37  GLU A OE1 1 
ATOM   57   O OE2 . GLU A 1 37  ? -11.496 7.215   11.371  1.00 95.56  ? 37  GLU A OE2 1 
ATOM   58   N N   . GLU A 1 38  ? -8.419  1.164   12.264  1.00 54.87  ? 38  GLU A N   1 
ATOM   59   C CA  . GLU A 1 38  ? -8.461  -0.286  12.422  1.00 53.82  ? 38  GLU A CA  1 
ATOM   60   C C   . GLU A 1 38  ? -7.594  -0.745  13.588  1.00 53.93  ? 38  GLU A C   1 
ATOM   61   O O   . GLU A 1 38  ? -8.018  -1.595  14.381  1.00 54.38  ? 38  GLU A O   1 
ATOM   62   C CB  . GLU A 1 38  ? -8.044  -1.003  11.140  1.00 67.11  ? 38  GLU A CB  1 
ATOM   63   C CG  . GLU A 1 38  ? -8.166  -2.512  11.314  1.00 68.06  ? 38  GLU A CG  1 
ATOM   64   C CD  . GLU A 1 38  ? -7.711  -3.315  10.108  1.00 82.42  ? 38  GLU A CD  1 
ATOM   65   O OE1 . GLU A 1 38  ? -7.060  -2.742  9.203   1.00 66.05  ? 38  GLU A OE1 1 
ATOM   66   O OE2 . GLU A 1 38  ? -7.999  -4.536  10.081  1.00 77.29  ? 38  GLU A OE2 1 
ATOM   67   N N   . ALA A 1 39  ? -6.384  -0.192  13.724  1.00 47.03  ? 39  ALA A N   1 
ATOM   68   C CA  . ALA A 1 39  ? -5.523  -0.595  14.834  1.00 49.12  ? 39  ALA A CA  1 
ATOM   69   C C   . ALA A 1 39  ? -6.150  -0.234  16.174  1.00 46.91  ? 39  ALA A C   1 
ATOM   70   O O   . ALA A 1 39  ? -6.058  -0.999  17.139  1.00 48.17  ? 39  ALA A O   1 
ATOM   71   C CB  . ALA A 1 39  ? -4.142  0.051   14.698  1.00 44.44  ? 39  ALA A CB  1 
ATOM   72   N N   . TRP A 1 40  ? -6.784  0.934   16.258  1.00 43.02  ? 40  TRP A N   1 
ATOM   73   C CA  . TRP A 1 40  ? -7.482  1.303   17.488  1.00 46.12  ? 40  TRP A CA  1 
ATOM   74   C C   . TRP A 1 40  ? -8.467  0.213   17.904  1.00 46.77  ? 40  TRP A C   1 
ATOM   75   O O   . TRP A 1 40  ? -8.465  -0.239  19.053  1.00 46.19  ? 40  TRP A O   1 
ATOM   76   C CB  . TRP A 1 40  ? -8.196  2.635   17.285  1.00 45.64  ? 40  TRP A CB  1 
ATOM   77   C CG  . TRP A 1 40  ? -8.815  3.213   18.505  1.00 58.51  ? 40  TRP A CG  1 
ATOM   78   C CD1 . TRP A 1 40  ? -8.206  4.015   19.432  1.00 56.05  ? 40  TRP A CD1 1 
ATOM   79   C CD2 . TRP A 1 40  ? -10.177 3.083   18.918  1.00 49.09  ? 40  TRP A CD2 1 
ATOM   80   N NE1 . TRP A 1 40  ? -9.100  4.376   20.404  1.00 61.75  ? 40  TRP A NE1 1 
ATOM   81   C CE2 . TRP A 1 40  ? -10.322 3.823   20.111  1.00 63.30  ? 40  TRP A CE2 1 
ATOM   82   C CE3 . TRP A 1 40  ? -11.287 2.409   18.404  1.00 54.69  ? 40  TRP A CE3 1 
ATOM   83   C CZ2 . TRP A 1 40  ? -11.537 3.907   20.796  1.00 48.95  ? 40  TRP A CZ2 1 
ATOM   84   C CZ3 . TRP A 1 40  ? -12.499 2.499   19.089  1.00 64.19  ? 40  TRP A CZ3 1 
ATOM   85   C CH2 . TRP A 1 40  ? -12.610 3.238   20.271  1.00 57.67  ? 40  TRP A CH2 1 
ATOM   86   N N   . CYS A 1 41  ? -9.288  -0.252  16.961  1.00 42.56  ? 41  CYS A N   1 
ATOM   87   C CA  . CYS A 1 41  ? -10.224 -1.338  17.255  1.00 46.92  ? 41  CYS A CA  1 
ATOM   88   C C   . CYS A 1 41  ? -9.498  -2.617  17.663  1.00 52.34  ? 41  CYS A C   1 
ATOM   89   O O   . CYS A 1 41  ? -9.880  -3.275  18.637  1.00 42.22  ? 41  CYS A O   1 
ATOM   90   C CB  . CYS A 1 41  ? -11.108 -1.598  16.038  1.00 39.13  ? 41  CYS A CB  1 
ATOM   91   S SG  . CYS A 1 41  ? -12.147 -0.185  15.550  1.00 55.07  ? 41  CYS A SG  1 
ATOM   92   N N   . LEU A 1 42  ? -8.435  -2.973  16.944  1.00 43.92  ? 42  LEU A N   1 
ATOM   93   C CA  . LEU A 1 42  ? -7.788  -4.270  17.160  1.00 47.10  ? 42  LEU A CA  1 
ATOM   94   C C   . LEU A 1 42  ? -7.134  -4.367  18.539  1.00 40.23  ? 42  LEU A C   1 
ATOM   95   O O   . LEU A 1 42  ? -7.289  -5.376  19.237  1.00 47.07  ? 42  LEU A O   1 
ATOM   96   C CB  . LEU A 1 42  ? -6.759  -4.499  16.064  1.00 42.06  ? 42  LEU A CB  1 
ATOM   97   C CG  . LEU A 1 42  ? -7.363  -4.604  14.669  1.00 48.74  ? 42  LEU A CG  1 
ATOM   98   C CD1 . LEU A 1 42  ? -6.233  -4.746  13.696  1.00 51.92  ? 42  LEU A CD1 1 
ATOM   99   C CD2 . LEU A 1 42  ? -8.308  -5.799  14.565  1.00 50.39  ? 42  LEU A CD2 1 
ATOM   100  N N   . VAL A 1 43  ? -6.397  -3.330  18.947  1.00 43.05  ? 43  VAL A N   1 
ATOM   101  C CA  . VAL A 1 43  ? -5.675  -3.321  20.219  1.00 45.91  ? 43  VAL A CA  1 
ATOM   102  C C   . VAL A 1 43  ? -6.619  -3.321  21.429  1.00 52.82  ? 43  VAL A C   1 
ATOM   103  O O   . VAL A 1 43  ? -6.225  -3.732  22.537  1.00 44.46  ? 43  VAL A O   1 
ATOM   104  C CB  . VAL A 1 43  ? -4.710  -2.111  20.193  1.00 54.46  ? 43  VAL A CB  1 
ATOM   105  C CG1 . VAL A 1 43  ? -4.419  -1.572  21.570  1.00 67.47  ? 43  VAL A CG1 1 
ATOM   106  C CG2 . VAL A 1 43  ? -3.417  -2.496  19.515  1.00 53.38  ? 43  VAL A CG2 1 
ATOM   107  N N   . ARG A 1 44  ? -7.860  -2.877  21.249  1.00 44.12  ? 44  ARG A N   1 
ATOM   108  C CA  . ARG A 1 44  ? -8.878  -2.899  22.292  1.00 42.03  ? 44  ARG A CA  1 
ATOM   109  C C   . ARG A 1 44  ? -9.764  -4.146  22.228  1.00 49.84  ? 44  ARG A C   1 
ATOM   110  O O   . ARG A 1 44  ? -10.669 -4.294  23.056  1.00 45.09  ? 44  ARG A O   1 
ATOM   111  C CB  . ARG A 1 44  ? -9.750  -1.636  22.184  1.00 38.96  ? 44  ARG A CB  1 
ATOM   112  C CG  . ARG A 1 44  ? -9.082  -0.367  22.728  1.00 55.43  ? 44  ARG A CG  1 
ATOM   113  C CD  . ARG A 1 44  ? -9.613  0.881   22.025  1.00 67.12  ? 44  ARG A CD  1 
ATOM   114  N NE  . ARG A 1 44  ? -10.956 1.273   22.438  1.00 54.26  ? 44  ARG A NE  1 
ATOM   115  C CZ  . ARG A 1 44  ? -11.256 1.829   23.607  1.00 73.47  ? 44  ARG A CZ  1 
ATOM   116  N NH1 . ARG A 1 44  ? -10.318 2.136   24.489  1.00 75.81  ? 44  ARG A NH1 1 
ATOM   117  N NH2 . ARG A 1 44  ? -12.526 2.127   23.880  1.00 72.92  ? 44  ARG A NH2 1 
ATOM   118  N N   . SER A 1 45  ? -9.521  -5.041  21.274  1.00 41.92  ? 45  SER A N   1 
ATOM   119  C CA  . SER A 1 45  ? -10.392 -6.197  21.071  1.00 43.86  ? 45  SER A CA  1 
ATOM   120  C C   . SER A 1 45  ? -10.300 -7.174  22.230  1.00 40.64  ? 45  SER A C   1 
ATOM   121  O O   . SER A 1 45  ? -9.295  -7.236  22.953  1.00 46.67  ? 45  SER A O   1 
ATOM   122  C CB  . SER A 1 45  ? -10.009 -6.911  19.784  1.00 42.17  ? 45  SER A CB  1 
ATOM   123  O OG  . SER A 1 45  ? -10.741 -8.114  19.598  1.00 45.82  ? 45  SER A OG  1 
ATOM   124  N N   . LYS A 1 46  ? -11.343 -7.991  22.368  1.00 54.39  ? 46  LYS A N   1 
ATOM   125  C CA  . LYS A 1 46  ? -11.347 -9.072  23.349  1.00 47.62  ? 46  LYS A CA  1 
ATOM   126  C C   . LYS A 1 46  ? -10.582 -10.290 22.861  1.00 41.56  ? 46  LYS A C   1 
ATOM   127  O O   . LYS A 1 46  ? -10.377 -11.222 23.643  1.00 49.77  ? 46  LYS A O   1 
ATOM   128  C CB  . LYS A 1 46  ? -12.785 -9.493  23.693  1.00 43.76  ? 46  LYS A CB  1 
ATOM   129  C CG  . LYS A 1 46  ? -13.628 -9.807  22.496  1.00 46.54  ? 46  LYS A CG  1 
ATOM   130  C CD  . LYS A 1 46  ? -14.956 -10.462 22.846  1.00 56.84  ? 46  LYS A CD  1 
ATOM   131  C CE  . LYS A 1 46  ? -15.897 -9.433  23.420  1.00 54.50  ? 46  LYS A CE  1 
ATOM   132  N NZ  . LYS A 1 46  ? -16.207 -8.350  22.430  1.00 67.10  ? 46  LYS A NZ  1 
ATOM   133  N N   . TYR A 1 47  ? -10.166 -10.305 21.594  1.00 44.25  ? 47  TYR A N   1 
ATOM   134  C CA  . TYR A 1 47  ? -9.533  -11.459 20.965  1.00 44.00  ? 47  TYR A CA  1 
ATOM   135  C C   . TYR A 1 47  ? -8.026  -11.248 20.831  1.00 50.27  ? 47  TYR A C   1 
ATOM   136  O O   . TYR A 1 47  ? -7.584  -10.230 20.288  1.00 48.17  ? 47  TYR A O   1 
ATOM   137  C CB  . TYR A 1 47  ? -10.157 -11.715 19.588  1.00 42.34  ? 47  TYR A CB  1 
ATOM   138  C CG  . TYR A 1 47  ? -11.604 -12.189 19.659  1.00 46.73  ? 47  TYR A CG  1 
ATOM   139  C CD1 . TYR A 1 47  ? -11.909 -13.522 19.939  1.00 45.40  ? 47  TYR A CD1 1 
ATOM   140  C CD2 . TYR A 1 47  ? -12.659 -11.296 19.480  1.00 52.83  ? 47  TYR A CD2 1 
ATOM   141  C CE1 . TYR A 1 47  ? -13.240 -13.958 20.023  1.00 53.39  ? 47  TYR A CE1 1 
ATOM   142  C CE2 . TYR A 1 47  ? -13.988 -11.713 19.559  1.00 50.85  ? 47  TYR A CE2 1 
ATOM   143  C CZ  . TYR A 1 47  ? -14.274 -13.045 19.828  1.00 55.94  ? 47  TYR A CZ  1 
ATOM   144  O OH  . TYR A 1 47  ? -15.594 -13.458 19.907  1.00 63.86  ? 47  TYR A OH  1 
ATOM   145  N N   . ASN A 1 48  ? -7.242  -12.232 21.292  1.00 43.97  ? 48  ASN A N   1 
ATOM   146  C CA  . ASN A 1 48  ? -5.787  -12.098 21.248  1.00 53.15  ? 48  ASN A CA  1 
ATOM   147  C C   . ASN A 1 48  ? -5.275  -11.959 19.816  1.00 43.66  ? 48  ASN A C   1 
ATOM   148  O O   . ASN A 1 48  ? -4.384  -11.143 19.561  1.00 47.68  ? 48  ASN A O   1 
ATOM   149  C CB  . ASN A 1 48  ? -5.117  -13.282 21.954  1.00 52.51  ? 48  ASN A CB  1 
ATOM   150  C CG  . ASN A 1 48  ? -5.231  -13.203 23.482  1.00 45.39  ? 48  ASN A CG  1 
ATOM   151  O OD1 . ASN A 1 48  ? -5.595  -12.164 24.046  1.00 45.71  ? 48  ASN A OD1 1 
ATOM   152  N ND2 . ASN A 1 48  ? -4.925  -14.310 24.152  1.00 46.54  ? 48  ASN A ND2 1 
ATOM   153  N N   . ASP A 1 49  ? -5.813  -12.750 18.876  1.00 57.47  ? 49  ASP A N   1 
ATOM   154  C CA  . ASP A 1 49  ? -5.461  -12.598 17.458  1.00 53.34  ? 49  ASP A CA  1 
ATOM   155  C C   . ASP A 1 49  ? -5.569  -11.148 17.017  1.00 60.42  ? 49  ASP A C   1 
ATOM   156  O O   . ASP A 1 49  ? -4.647  -10.610 16.392  1.00 52.37  ? 49  ASP A O   1 
ATOM   157  C CB  . ASP A 1 49  ? -6.364  -13.450 16.564  1.00 57.36  ? 49  ASP A CB  1 
ATOM   158  C CG  . ASP A 1 49  ? -6.032  -14.918 16.606  1.00 81.59  ? 49  ASP A CG  1 
ATOM   159  O OD1 . ASP A 1 49  ? -6.851  -15.714 16.097  1.00 89.89  ? 49  ASP A OD1 1 
ATOM   160  O OD2 . ASP A 1 49  ? -4.948  -15.279 17.111  1.00 88.32  ? 49  ASP A OD2 1 
ATOM   161  N N   . ASP A 1 50  ? -6.708  -10.507 17.318  1.00 55.33  ? 50  ASP A N   1 
ATOM   162  C CA  . ASP A 1 50  ? -6.909  -9.108  16.948  1.00 46.98  ? 50  ASP A CA  1 
ATOM   163  C C   . ASP A 1 50  ? -5.796  -8.234  17.506  1.00 44.76  ? 50  ASP A C   1 
ATOM   164  O O   . ASP A 1 50  ? -5.202  -7.424  16.783  1.00 48.00  ? 50  ASP A O   1 
ATOM   165  C CB  . ASP A 1 50  ? -8.264  -8.597  17.470  1.00 45.35  ? 50  ASP A CB  1 
ATOM   166  C CG  . ASP A 1 50  ? -9.452  -9.078  16.657  1.00 52.33  ? 50  ASP A CG  1 
ATOM   167  O OD1 . ASP A 1 50  ? -9.266  -9.504  15.503  1.00 54.83  ? 50  ASP A OD1 1 
ATOM   168  O OD2 . ASP A 1 50  ? -10.594 -9.008  17.179  1.00 57.97  ? 50  ASP A OD2 1 
ATOM   169  N N   . ILE A 1 51  ? -5.516  -8.371  18.810  1.00 45.34  ? 51  ILE A N   1 
ATOM   170  C CA  . ILE A 1 51  ? -4.513  -7.525  19.459  1.00 45.56  ? 51  ILE A CA  1 
ATOM   171  C C   . ILE A 1 51  ? -3.155  -7.669  18.786  1.00 46.20  ? 51  ILE A C   1 
ATOM   172  O O   . ILE A 1 51  ? -2.440  -6.679  18.585  1.00 45.00  ? 51  ILE A O   1 
ATOM   173  C CB  . ILE A 1 51  ? -4.410  -7.852  20.958  1.00 49.37  ? 51  ILE A CB  1 
ATOM   174  C CG1 . ILE A 1 51  ? -5.766  -7.647  21.633  1.00 40.35  ? 51  ILE A CG1 1 
ATOM   175  C CG2 . ILE A 1 51  ? -3.282  -7.005  21.589  1.00 39.09  ? 51  ILE A CG2 1 
ATOM   176  C CD1 . ILE A 1 51  ? -5.806  -8.125  23.069  1.00 48.21  ? 51  ILE A CD1 1 
ATOM   177  N N   A ARG A 1 52  ? -2.768  -8.902  18.455  0.58 46.76  ? 52  ARG A N   1 
ATOM   178  N N   B ARG A 1 52  ? -2.772  -8.893  18.423  0.42 45.68  ? 52  ARG A N   1 
ATOM   179  C CA  A ARG A 1 52  ? -1.503  -9.109  17.756  0.58 46.96  ? 52  ARG A CA  1 
ATOM   180  C CA  B ARG A 1 52  ? -1.477  -9.068  17.768  0.42 46.25  ? 52  ARG A CA  1 
ATOM   181  C C   A ARG A 1 52  ? -1.475  -8.324  16.453  0.58 54.02  ? 52  ARG A C   1 
ATOM   182  C C   B ARG A 1 52  ? -1.439  -8.367  16.414  0.42 52.44  ? 52  ARG A C   1 
ATOM   183  O O   A ARG A 1 52  ? -0.560  -7.526  16.215  0.58 53.74  ? 52  ARG A O   1 
ATOM   184  O O   B ARG A 1 52  ? -0.461  -7.680  16.094  0.42 54.18  ? 52  ARG A O   1 
ATOM   185  C CB  A ARG A 1 52  ? -1.273  -10.597 17.492  0.58 49.05  ? 52  ARG A CB  1 
ATOM   186  C CB  B ARG A 1 52  ? -1.153  -10.552 17.623  0.42 49.28  ? 52  ARG A CB  1 
ATOM   187  C CG  A ARG A 1 52  ? -1.168  -11.450 18.740  0.58 49.16  ? 52  ARG A CG  1 
ATOM   188  C CG  B ARG A 1 52  ? -0.676  -11.196 18.914  0.42 46.36  ? 52  ARG A CG  1 
ATOM   189  C CD  A ARG A 1 52  ? -1.289  -12.928 18.380  0.58 58.64  ? 52  ARG A CD  1 
ATOM   190  C CD  B ARG A 1 52  ? -0.215  -12.622 18.669  0.42 51.23  ? 52  ARG A CD  1 
ATOM   191  N NE  A ARG A 1 52  ? -1.604  -13.730 19.556  0.58 55.11  ? 52  ARG A NE  1 
ATOM   192  N NE  B ARG A 1 52  ? -0.781  -13.520 19.666  0.42 59.48  ? 52  ARG A NE  1 
ATOM   193  C CZ  A ARG A 1 52  ? -2.538  -14.666 19.592  0.58 47.02  ? 52  ARG A CZ  1 
ATOM   194  C CZ  B ARG A 1 52  ? -0.395  -13.578 20.933  0.42 52.13  ? 52  ARG A CZ  1 
ATOM   195  N NH1 A ARG A 1 52  ? -3.236  -14.986 18.517  0.58 48.59  ? 52  ARG A NH1 1 
ATOM   196  N NH1 B ARG A 1 52  ? 0.636   -12.878 21.374  0.42 51.92  ? 52  ARG A NH1 1 
ATOM   197  N NH2 A ARG A 1 52  ? -2.781  -15.292 20.736  0.58 63.72  ? 52  ARG A NH2 1 
ATOM   198  N NH2 B ARG A 1 52  ? -1.056  -14.366 21.774  0.42 50.01  ? 52  ARG A NH2 1 
ATOM   199  N N   . LYS A 1 53  ? -2.499  -8.507  15.613  1.00 52.05  ? 53  LYS A N   1 
ATOM   200  C CA  . LYS A 1 53  ? -2.529  -7.835  14.310  1.00 50.19  ? 53  LYS A CA  1 
ATOM   201  C C   . LYS A 1 53  ? -2.556  -6.316  14.473  1.00 49.89  ? 53  LYS A C   1 
ATOM   202  O O   . LYS A 1 53  ? -1.980  -5.588  13.651  1.00 47.54  ? 53  LYS A O   1 
ATOM   203  C CB  . LYS A 1 53  ? -3.746  -8.302  13.496  1.00 53.07  ? 53  LYS A CB  1 
ATOM   204  C CG  . LYS A 1 53  ? -3.915  -9.843  13.336  1.00 66.78  ? 53  LYS A CG  1 
ATOM   205  C CD  . LYS A 1 53  ? -2.631  -10.663 13.594  1.00 82.92  ? 53  LYS A CD  1 
ATOM   206  C CE  . LYS A 1 53  ? -2.928  -12.151 13.803  1.00 83.26  ? 53  LYS A CE  1 
ATOM   207  N NZ  . LYS A 1 53  ? -3.766  -12.760 12.717  1.00 71.87  ? 53  LYS A NZ  1 
ATOM   208  N N   . GLY A 1 54  ? -3.203  -5.819  15.531  1.00 47.05  ? 54  GLY A N   1 
ATOM   209  C CA  . GLY A 1 54  ? -3.194  -4.385  15.784  1.00 45.10  ? 54  GLY A CA  1 
ATOM   210  C C   . GLY A 1 54  ? -1.801  -3.882  16.106  1.00 61.54  ? 54  GLY A C   1 
ATOM   211  O O   . GLY A 1 54  ? -1.426  -2.764  15.733  1.00 47.95  ? 54  GLY A O   1 
ATOM   212  N N   . ILE A 1 55  ? -1.015  -4.715  16.786  1.00 51.38  ? 55  ILE A N   1 
ATOM   213  C CA  . ILE A 1 55  ? 0.362   -4.369  17.107  1.00 49.21  ? 55  ILE A CA  1 
ATOM   214  C C   . ILE A 1 55  ? 1.177   -4.256  15.821  1.00 41.91  ? 55  ILE A C   1 
ATOM   215  O O   . ILE A 1 55  ? 1.881   -3.265  15.592  1.00 45.94  ? 55  ILE A O   1 
ATOM   216  C CB  . ILE A 1 55  ? 0.939   -5.419  18.070  1.00 57.94  ? 55  ILE A CB  1 
ATOM   217  C CG1 . ILE A 1 55  ? 0.602   -5.034  19.511  1.00 49.46  ? 55  ILE A CG1 1 
ATOM   218  C CG2 . ILE A 1 55  ? 2.475   -5.583  17.867  1.00 56.37  ? 55  ILE A CG2 1 
ATOM   219  C CD1 . ILE A 1 55  ? 0.898   -6.123  20.512  1.00 50.68  ? 55  ILE A CD1 1 
ATOM   220  N N   . VAL A 1 56  ? 1.044   -5.252  14.939  1.00 50.61  ? 56  VAL A N   1 
ATOM   221  C CA  . VAL A 1 56  ? 1.695   -5.208  13.627  1.00 54.81  ? 56  VAL A CA  1 
ATOM   222  C C   . VAL A 1 56  ? 1.394   -3.889  12.927  1.00 65.41  ? 56  VAL A C   1 
ATOM   223  O O   . VAL A 1 56  ? 2.303   -3.200  12.443  1.00 54.65  ? 56  VAL A O   1 
ATOM   224  C CB  . VAL A 1 56  ? 1.258   -6.410  12.773  1.00 52.20  ? 56  VAL A CB  1 
ATOM   225  C CG1 . VAL A 1 56  ? 1.597   -6.173  11.292  1.00 59.36  ? 56  VAL A CG1 1 
ATOM   226  C CG2 . VAL A 1 56  ? 1.932   -7.688  13.276  1.00 52.64  ? 56  VAL A CG2 1 
ATOM   227  N N   . LEU A 1 57  ? 0.115   -3.497  12.907  1.00 56.12  ? 57  LEU A N   1 
ATOM   228  C CA  . LEU A 1 57  ? -0.304  -2.314  12.158  1.00 61.04  ? 57  LEU A CA  1 
ATOM   229  C C   . LEU A 1 57  ? 0.232   -1.030  12.778  1.00 50.49  ? 57  LEU A C   1 
ATOM   230  O O   . LEU A 1 57  ? 0.664   -0.120  12.060  1.00 55.25  ? 57  LEU A O   1 
ATOM   231  C CB  . LEU A 1 57  ? -1.832  -2.251  12.074  1.00 51.55  ? 57  LEU A CB  1 
ATOM   232  C CG  . LEU A 1 57  ? -2.552  -3.043  10.990  1.00 59.69  ? 57  LEU A CG  1 
ATOM   233  C CD1 . LEU A 1 57  ? -4.072  -2.936  11.184  1.00 55.48  ? 57  LEU A CD1 1 
ATOM   234  C CD2 . LEU A 1 57  ? -2.138  -2.560  9.603   1.00 62.37  ? 57  LEU A CD2 1 
ATOM   235  N N   . LEU A 1 58  ? 0.192   -0.920  14.102  1.00 43.31  ? 58  LEU A N   1 
ATOM   236  C CA  . LEU A 1 58  ? 0.729   0.276   14.743  1.00 42.10  ? 58  LEU A CA  1 
ATOM   237  C C   . LEU A 1 58  ? 2.231   0.415   14.495  1.00 55.41  ? 58  LEU A C   1 
ATOM   238  O O   . LEU A 1 58  ? 2.742   1.533   14.379  1.00 51.13  ? 58  LEU A O   1 
ATOM   239  C CB  . LEU A 1 58  ? 0.444   0.221   16.237  1.00 42.08  ? 58  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 58  ? -1.030  0.481   16.549  1.00 46.88  ? 58  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 58  ? -1.268  0.220   18.025  1.00 45.86  ? 58  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 58  ? -1.383  1.922   16.166  1.00 37.36  ? 58  LEU A CD2 1 
ATOM   243  N N   . GLU A 1 59  ? 2.949   -0.699  14.406  1.00 46.75  ? 59  GLU A N   1 
ATOM   244  C CA  . GLU A 1 59  ? 4.391   -0.624  14.216  1.00 55.10  ? 59  GLU A CA  1 
ATOM   245  C C   . GLU A 1 59  ? 4.750   -0.112  12.824  1.00 58.87  ? 59  GLU A C   1 
ATOM   246  O O   . GLU A 1 59  ? 5.752   0.593   12.666  1.00 62.05  ? 59  GLU A O   1 
ATOM   247  C CB  . GLU A 1 59  ? 5.010   -1.994  14.464  1.00 57.53  ? 59  GLU A CB  1 
ATOM   248  C CG  . GLU A 1 59  ? 5.366   -2.229  15.929  1.00 54.33  ? 59  GLU A CG  1 
ATOM   249  C CD  . GLU A 1 59  ? 5.731   -3.678  16.224  1.00 81.50  ? 59  GLU A CD  1 
ATOM   250  O OE1 . GLU A 1 59  ? 5.533   -4.548  15.343  1.00 79.96  ? 59  GLU A OE1 1 
ATOM   251  O OE2 . GLU A 1 59  ? 6.226   -3.940  17.341  1.00 72.13  ? 59  GLU A OE2 1 
ATOM   252  N N   . GLU A 1 60  ? 3.944   -0.440  11.811  1.00 59.71  ? 60  GLU A N   1 
ATOM   253  C CA  . GLU A 1 60  ? 4.176   0.113   10.480  1.00 61.29  ? 60  GLU A CA  1 
ATOM   254  C C   . GLU A 1 60  ? 3.806   1.588   10.427  1.00 62.87  ? 60  GLU A C   1 
ATOM   255  O O   . GLU A 1 60  ? 4.511   2.388   9.805   1.00 65.17  ? 60  GLU A O   1 
ATOM   256  C CB  . GLU A 1 60  ? 3.388   -0.674  9.437   1.00 68.71  ? 60  GLU A CB  1 
ATOM   257  C CG  . GLU A 1 60  ? 3.217   -2.146  9.779   1.00 72.78  ? 60  GLU A CG  1 
ATOM   258  C CD  . GLU A 1 60  ? 2.595   -2.953  8.644   1.00 89.56  ? 60  GLU A CD  1 
ATOM   259  O OE1 . GLU A 1 60  ? 2.964   -4.143  8.488   1.00 94.41  ? 60  GLU A OE1 1 
ATOM   260  O OE2 . GLU A 1 60  ? 1.747   -2.397  7.908   1.00 86.71  ? 60  GLU A OE2 1 
ATOM   261  N N   . LEU A 1 61  ? 2.711   1.967   11.082  1.00 57.25  ? 61  LEU A N   1 
ATOM   262  C CA  . LEU A 1 61  ? 2.331   3.374   11.139  1.00 68.60  ? 61  LEU A CA  1 
ATOM   263  C C   . LEU A 1 61  ? 3.412   4.214   11.800  1.00 67.27  ? 61  LEU A C   1 
ATOM   264  O O   . LEU A 1 61  ? 3.626   5.372   11.416  1.00 59.11  ? 61  LEU A O   1 
ATOM   265  C CB  . LEU A 1 61  ? 1.013   3.515   11.902  1.00 68.89  ? 61  LEU A CB  1 
ATOM   266  C CG  . LEU A 1 61  ? -0.278  3.211   11.155  1.00 64.30  ? 61  LEU A CG  1 
ATOM   267  C CD1 . LEU A 1 61  ? -1.446  3.736   11.958  1.00 66.67  ? 61  LEU A CD1 1 
ATOM   268  C CD2 . LEU A 1 61  ? -0.259  3.850   9.769   1.00 61.89  ? 61  LEU A CD2 1 
ATOM   269  N N   . LEU A 1 62  ? 4.109   3.636   12.775  1.00 56.02  ? 62  LEU A N   1 
ATOM   270  C CA  . LEU A 1 62  ? 5.034   4.379   13.626  1.00 60.81  ? 62  LEU A CA  1 
ATOM   271  C C   . LEU A 1 62  ? 5.990   5.276   12.844  1.00 67.81  ? 62  LEU A C   1 
ATOM   272  O O   . LEU A 1 62  ? 6.067   6.473   13.161  1.00 74.28  ? 62  LEU A O   1 
ATOM   273  C CB  . LEU A 1 62  ? 5.759   3.360   14.519  1.00 70.20  ? 62  LEU A CB  1 
ATOM   274  C CG  . LEU A 1 62  ? 6.584   3.825   15.713  1.00 67.21  ? 62  LEU A CG  1 
ATOM   275  C CD1 . LEU A 1 62  ? 5.762   4.791   16.539  1.00 49.92  ? 62  LEU A CD1 1 
ATOM   276  C CD2 . LEU A 1 62  ? 7.030   2.613   16.551  1.00 56.51  ? 62  LEU A CD2 1 
ATOM   277  N N   . PRO A 1 63  ? 6.711   4.803   11.819  1.00 62.07  ? 63  PRO A N   1 
ATOM   278  C CA  . PRO A 1 63  ? 7.566   5.734   11.060  1.00 68.75  ? 63  PRO A CA  1 
ATOM   279  C C   . PRO A 1 63  ? 6.794   6.777   10.262  1.00 76.71  ? 63  PRO A C   1 
ATOM   280  O O   . PRO A 1 63  ? 7.366   7.823   9.923   1.00 73.92  ? 63  PRO A O   1 
ATOM   281  C CB  . PRO A 1 63  ? 8.363   4.809   10.126  1.00 57.68  ? 63  PRO A CB  1 
ATOM   282  C CG  . PRO A 1 63  ? 8.294   3.460   10.751  1.00 60.39  ? 63  PRO A CG  1 
ATOM   283  C CD  . PRO A 1 63  ? 6.966   3.400   11.443  1.00 65.36  ? 63  PRO A CD  1 
ATOM   284  N N   . LYS A 1 64  ? 5.527   6.518   9.932   1.00 64.64  ? 64  LYS A N   1 
ATOM   285  C CA  . LYS A 1 64  ? 4.775   7.348   8.998   1.00 69.14  ? 64  LYS A CA  1 
ATOM   286  C C   . LYS A 1 64  ? 4.079   8.529   9.661   1.00 70.76  ? 64  LYS A C   1 
ATOM   287  O O   . LYS A 1 64  ? 3.560   9.394   8.950   1.00 76.77  ? 64  LYS A O   1 
ATOM   288  C CB  . LYS A 1 64  ? 3.715   6.506   8.259   1.00 73.83  ? 64  LYS A CB  1 
ATOM   289  C CG  . LYS A 1 64  ? 4.218   5.647   7.084   1.00 78.94  ? 64  LYS A CG  1 
ATOM   290  C CD  . LYS A 1 64  ? 5.222   4.581   7.526   1.00 98.29  ? 64  LYS A CD  1 
ATOM   291  C CE  . LYS A 1 64  ? 4.978   3.206   6.882   1.00 100.29 ? 64  LYS A CE  1 
ATOM   292  N NZ  . LYS A 1 64  ? 5.951   2.176   7.413   1.00 78.14  ? 64  LYS A NZ  1 
ATOM   293  N N   . GLY A 1 65  ? 4.029   8.586   10.986  1.00 63.61  ? 65  GLY A N   1 
ATOM   294  C CA  . GLY A 1 65  ? 3.162   9.537   11.658  1.00 82.86  ? 65  GLY A CA  1 
ATOM   295  C C   . GLY A 1 65  ? 3.848   10.841  12.030  1.00 76.66  ? 65  GLY A C   1 
ATOM   296  O O   . GLY A 1 65  ? 5.041   10.881  12.296  1.00 67.53  ? 65  GLY A O   1 
ATOM   297  N N   . SER A 1 66  ? 3.062   11.918  12.072  1.00 73.32  ? 66  SER A N   1 
ATOM   298  C CA  . SER A 1 66  ? 3.528   13.156  12.693  1.00 71.65  ? 66  SER A CA  1 
ATOM   299  C C   . SER A 1 66  ? 3.835   12.906  14.168  1.00 70.85  ? 66  SER A C   1 
ATOM   300  O O   . SER A 1 66  ? 3.648   11.790  14.662  1.00 69.77  ? 66  SER A O   1 
ATOM   301  C CB  . SER A 1 66  ? 2.487   14.267  12.519  1.00 81.60  ? 66  SER A CB  1 
ATOM   302  O OG  . SER A 1 66  ? 1.374   14.060  13.370  1.00 85.45  ? 66  SER A OG  1 
ATOM   303  N N   . LYS A 1 67  ? 4.308   13.915  14.894  1.00 86.00  ? 67  LYS A N   1 
ATOM   304  C CA  . LYS A 1 67  ? 4.680   13.647  16.278  1.00 85.71  ? 67  LYS A CA  1 
ATOM   305  C C   . LYS A 1 67  ? 3.454   13.495  17.164  1.00 86.53  ? 67  LYS A C   1 
ATOM   306  O O   . LYS A 1 67  ? 3.410   12.597  18.014  1.00 83.93  ? 67  LYS A O   1 
ATOM   307  C CB  . LYS A 1 67  ? 5.603   14.735  16.809  1.00 100.63 ? 67  LYS A CB  1 
ATOM   308  C CG  . LYS A 1 67  ? 6.994   14.205  17.086  1.00 98.53  ? 67  LYS A CG  1 
ATOM   309  C CD  . LYS A 1 67  ? 7.644   13.751  15.791  1.00 98.10  ? 67  LYS A CD  1 
ATOM   310  C CE  . LYS A 1 67  ? 9.152   13.769  15.886  1.00 106.46 ? 67  LYS A CE  1 
ATOM   311  N NZ  . LYS A 1 67  ? 9.771   13.079  14.724  1.00 102.45 ? 67  LYS A NZ  1 
ATOM   312  N N   . GLU A 1 68  ? 2.446   14.354  16.985  1.00 84.13  ? 68  GLU A N   1 
ATOM   313  C CA  . GLU A 1 68  ? 1.227   14.172  17.757  1.00 81.01  ? 68  GLU A CA  1 
ATOM   314  C C   . GLU A 1 68  ? 0.448   12.948  17.306  1.00 79.09  ? 68  GLU A C   1 
ATOM   315  O O   . GLU A 1 68  ? -0.536  12.584  17.961  1.00 83.54  ? 68  GLU A O   1 
ATOM   316  C CB  . GLU A 1 68  ? 0.333   15.415  17.688  1.00 95.26  ? 68  GLU A CB  1 
ATOM   317  C CG  . GLU A 1 68  ? -0.347  15.668  16.344  1.00 103.83 ? 68  GLU A CG  1 
ATOM   318  C CD  . GLU A 1 68  ? 0.437   16.599  15.430  1.00 108.67 ? 68  GLU A CD  1 
ATOM   319  O OE1 . GLU A 1 68  ? 1.625   16.884  15.718  1.00 102.52 ? 68  GLU A OE1 1 
ATOM   320  O OE2 . GLU A 1 68  ? -0.147  17.052  14.420  1.00 107.12 ? 68  GLU A OE2 1 
ATOM   321  N N   . GLU A 1 69  ? 0.859   12.317  16.206  1.00 71.65  ? 69  GLU A N   1 
ATOM   322  C CA  . GLU A 1 69  ? 0.311   11.025  15.817  1.00 62.47  ? 69  GLU A CA  1 
ATOM   323  C C   . GLU A 1 69  ? 1.072   9.883   16.486  1.00 70.90  ? 69  GLU A C   1 
ATOM   324  O O   . GLU A 1 69  ? 0.452   8.951   17.012  1.00 59.51  ? 69  GLU A O   1 
ATOM   325  C CB  . GLU A 1 69  ? 0.332   10.879  14.286  1.00 60.17  ? 69  GLU A CB  1 
ATOM   326  C CG  . GLU A 1 69  ? -0.858  11.570  13.591  1.00 65.51  ? 69  GLU A CG  1 
ATOM   327  C CD  . GLU A 1 69  ? -0.731  11.687  12.064  1.00 86.66  ? 69  GLU A CD  1 
ATOM   328  O OE1 . GLU A 1 69  ? 0.269   11.209  11.480  1.00 66.21  ? 69  GLU A OE1 1 
ATOM   329  O OE2 . GLU A 1 69  ? -1.640  12.288  11.444  1.00 83.34  ? 69  GLU A OE2 1 
ATOM   330  N N   . GLN A 1 70  ? 2.408   9.961   16.514  1.00 55.87  ? 70  GLN A N   1 
ATOM   331  C CA  . GLN A 1 70  ? 3.212   8.893   17.106  1.00 45.52  ? 70  GLN A CA  1 
ATOM   332  C C   . GLN A 1 70  ? 2.943   8.752   18.601  1.00 40.36  ? 70  GLN A C   1 
ATOM   333  O O   . GLN A 1 70  ? 3.020   7.649   19.140  1.00 48.37  ? 70  GLN A O   1 
ATOM   334  C CB  . GLN A 1 70  ? 4.694   9.173   16.838  1.00 48.69  ? 70  GLN A CB  1 
ATOM   335  C CG  . GLN A 1 70  ? 5.066   9.060   15.372  1.00 59.08  ? 70  GLN A CG  1 
ATOM   336  C CD  . GLN A 1 70  ? 6.566   9.077   15.125  1.00 72.85  ? 70  GLN A CD  1 
ATOM   337  O OE1 . GLN A 1 70  ? 7.368   9.052   16.059  1.00 55.16  ? 70  GLN A OE1 1 
ATOM   338  N NE2 . GLN A 1 70  ? 6.950   9.182   13.854  1.00 69.49  ? 70  GLN A NE2 1 
ATOM   339  N N   . ARG A 1 71  ? 2.656   9.859   19.288  1.00 55.60  ? 71  ARG A N   1 
ATOM   340  C CA  . ARG A 1 71  ? 2.106   9.830   20.642  1.00 50.20  ? 71  ARG A CA  1 
ATOM   341  C C   . ARG A 1 71  ? 1.076   8.713   20.832  1.00 48.46  ? 71  ARG A C   1 
ATOM   342  O O   . ARG A 1 71  ? 1.239   7.816   21.674  1.00 39.30  ? 71  ARG A O   1 
ATOM   343  C CB  . ARG A 1 71  ? 1.455   11.190  20.902  1.00 71.29  ? 71  ARG A CB  1 
ATOM   344  C CG  . ARG A 1 71  ? 1.717   11.790  22.244  1.00 80.29  ? 71  ARG A CG  1 
ATOM   345  C CD  . ARG A 1 71  ? 1.284   13.243  22.217  1.00 59.29  ? 71  ARG A CD  1 
ATOM   346  N NE  . ARG A 1 71  ? -0.164  13.335  22.224  1.00 70.35  ? 71  ARG A NE  1 
ATOM   347  C CZ  . ARG A 1 71  ? -0.914  13.238  23.312  1.00 61.96  ? 71  ARG A CZ  1 
ATOM   348  N NH1 . ARG A 1 71  ? -0.378  13.059  24.509  1.00 48.81  ? 71  ARG A NH1 1 
ATOM   349  N NH2 . ARG A 1 71  ? -2.234  13.325  23.193  1.00 69.78  ? 71  ARG A NH2 1 
ATOM   350  N N   A ASP A 1 72  ? -0.001  8.771   20.041  0.53 51.92  ? 72  ASP A N   1 
ATOM   351  N N   B ASP A 1 72  ? 0.001   8.768   20.041  0.47 51.89  ? 72  ASP A N   1 
ATOM   352  C CA  A ASP A 1 72  ? -1.053  7.758   20.126  0.53 48.68  ? 72  ASP A CA  1 
ATOM   353  C CA  B ASP A 1 72  ? -1.057  7.761   20.118  0.47 48.70  ? 72  ASP A CA  1 
ATOM   354  C C   A ASP A 1 72  ? -0.532  6.383   19.729  0.53 50.81  ? 72  ASP A C   1 
ATOM   355  C C   B ASP A 1 72  ? -0.547  6.384   19.717  0.47 50.70  ? 72  ASP A C   1 
ATOM   356  O O   A ASP A 1 72  ? -0.852  5.381   20.380  0.53 46.49  ? 72  ASP A O   1 
ATOM   357  O O   B ASP A 1 72  ? -0.887  5.380   20.357  0.47 46.42  ? 72  ASP A O   1 
ATOM   358  C CB  A ASP A 1 72  ? -2.241  8.126   19.235  0.53 45.68  ? 72  ASP A CB  1 
ATOM   359  C CB  B ASP A 1 72  ? -2.223  8.170   19.221  0.47 45.81  ? 72  ASP A CB  1 
ATOM   360  C CG  A ASP A 1 72  ? -2.912  9.440   19.624  0.53 55.74  ? 72  ASP A CG  1 
ATOM   361  C CG  B ASP A 1 72  ? -3.060  9.297   19.813  0.47 55.82  ? 72  ASP A CG  1 
ATOM   362  O OD1 A ASP A 1 72  ? -2.829  9.851   20.800  0.53 50.19  ? 72  ASP A OD1 1 
ATOM   363  O OD1 B ASP A 1 72  ? -4.037  9.005   20.540  0.47 62.42  ? 72  ASP A OD1 1 
ATOM   364  O OD2 A ASP A 1 72  ? -3.588  10.034  18.751  0.53 48.50  ? 72  ASP A OD2 1 
ATOM   365  O OD2 B ASP A 1 72  ? -2.734  10.476  19.556  0.47 64.71  ? 72  ASP A OD2 1 
ATOM   366  N N   . TYR A 1 73  ? 0.252   6.308   18.647  1.00 44.89  ? 73  TYR A N   1 
ATOM   367  C CA  . TYR A 1 73  ? 0.805   5.022   18.236  1.00 46.37  ? 73  TYR A CA  1 
ATOM   368  C C   . TYR A 1 73  ? 1.575   4.375   19.377  1.00 47.32  ? 73  TYR A C   1 
ATOM   369  O O   . TYR A 1 73  ? 1.412   3.176   19.652  1.00 41.25  ? 73  TYR A O   1 
ATOM   370  C CB  . TYR A 1 73  ? 1.738   5.172   17.036  1.00 52.13  ? 73  TYR A CB  1 
ATOM   371  C CG  . TYR A 1 73  ? 1.150   5.745   15.781  1.00 62.00  ? 73  TYR A CG  1 
ATOM   372  C CD1 . TYR A 1 73  ? -0.217  5.743   15.554  1.00 49.22  ? 73  TYR A CD1 1 
ATOM   373  C CD2 . TYR A 1 73  ? 1.985   6.285   14.803  1.00 53.63  ? 73  TYR A CD2 1 
ATOM   374  C CE1 . TYR A 1 73  ? -0.742  6.275   14.392  1.00 52.93  ? 73  TYR A CE1 1 
ATOM   375  C CE2 . TYR A 1 73  ? 1.473   6.809   13.636  1.00 58.18  ? 73  TYR A CE2 1 
ATOM   376  C CZ  . TYR A 1 73  ? 0.109   6.805   13.433  1.00 66.27  ? 73  TYR A CZ  1 
ATOM   377  O OH  . TYR A 1 73  ? -0.400  7.338   12.267  1.00 76.31  ? 73  TYR A OH  1 
ATOM   378  N N   . VAL A 1 74  ? 2.443   5.153   20.036  1.00 43.63  ? 74  VAL A N   1 
ATOM   379  C CA  . VAL A 1 74  ? 3.303   4.592   21.079  1.00 38.60  ? 74  VAL A CA  1 
ATOM   380  C C   . VAL A 1 74  ? 2.456   4.158   22.267  1.00 42.87  ? 74  VAL A C   1 
ATOM   381  O O   . VAL A 1 74  ? 2.663   3.084   22.845  1.00 42.53  ? 74  VAL A O   1 
ATOM   382  C CB  . VAL A 1 74  ? 4.386   5.606   21.498  1.00 44.88  ? 74  VAL A CB  1 
ATOM   383  C CG1 . VAL A 1 74  ? 5.111   5.123   22.731  1.00 46.69  ? 74  VAL A CG1 1 
ATOM   384  C CG2 . VAL A 1 74  ? 5.403   5.866   20.362  1.00 44.97  ? 74  VAL A CG2 1 
ATOM   385  N N   . PHE A 1 75  ? 1.473   4.973   22.639  1.00 46.02  ? 75  PHE A N   1 
ATOM   386  C CA  . PHE A 1 75  ? 0.605   4.600   23.748  1.00 43.50  ? 75  PHE A CA  1 
ATOM   387  C C   . PHE A 1 75  ? -0.142  3.303   23.454  1.00 46.11  ? 75  PHE A C   1 
ATOM   388  O O   . PHE A 1 75  ? -0.186  2.400   24.294  1.00 44.44  ? 75  PHE A O   1 
ATOM   389  C CB  . PHE A 1 75  ? -0.372  5.727   24.073  1.00 39.41  ? 75  PHE A CB  1 
ATOM   390  C CG  . PHE A 1 75  ? -1.310  5.379   25.205  1.00 43.99  ? 75  PHE A CG  1 
ATOM   391  C CD1 . PHE A 1 75  ? -0.839  5.266   26.503  1.00 43.51  ? 75  PHE A CD1 1 
ATOM   392  C CD2 . PHE A 1 75  ? -2.645  5.140   24.961  1.00 44.56  ? 75  PHE A CD2 1 
ATOM   393  C CE1 . PHE A 1 75  ? -1.697  4.939   27.550  1.00 43.90  ? 75  PHE A CE1 1 
ATOM   394  C CE2 . PHE A 1 75  ? -3.515  4.805   26.006  1.00 53.86  ? 75  PHE A CE2 1 
ATOM   395  C CZ  . PHE A 1 75  ? -3.030  4.705   27.300  1.00 43.81  ? 75  PHE A CZ  1 
ATOM   396  N N   . TYR A 1 76  ? -0.705  3.164   22.251  1.00 45.06  ? 76  TYR A N   1 
ATOM   397  C CA  . TYR A 1 76  ? -1.455  1.941   21.995  1.00 41.24  ? 76  TYR A CA  1 
ATOM   398  C C   . TYR A 1 76  ? -0.576  0.723   21.760  1.00 49.03  ? 76  TYR A C   1 
ATOM   399  O O   . TYR A 1 76  ? -1.039  -0.400  21.981  1.00 45.29  ? 76  TYR A O   1 
ATOM   400  C CB  . TYR A 1 76  ? -2.400  2.129   20.820  1.00 43.79  ? 76  TYR A CB  1 
ATOM   401  C CG  . TYR A 1 76  ? -3.605  2.910   21.238  1.00 47.29  ? 76  TYR A CG  1 
ATOM   402  C CD1 . TYR A 1 76  ? -4.532  2.358   22.111  1.00 51.49  ? 76  TYR A CD1 1 
ATOM   403  C CD2 . TYR A 1 76  ? -3.805  4.201   20.801  1.00 53.69  ? 76  TYR A CD2 1 
ATOM   404  C CE1 . TYR A 1 76  ? -5.636  3.071   22.510  1.00 56.94  ? 76  TYR A CE1 1 
ATOM   405  C CE2 . TYR A 1 76  ? -4.935  4.927   21.194  1.00 58.51  ? 76  TYR A CE2 1 
ATOM   406  C CZ  . TYR A 1 76  ? -5.827  4.354   22.050  1.00 48.94  ? 76  TYR A CZ  1 
ATOM   407  O OH  . TYR A 1 76  ? -6.937  5.062   22.455  1.00 80.13  ? 76  TYR A OH  1 
ATOM   408  N N   . LEU A 1 77  ? 0.664   0.896   21.303  1.00 39.47  ? 77  LEU A N   1 
ATOM   409  C CA  . LEU A 1 77  ? 1.572   -0.238  21.299  1.00 42.13  ? 77  LEU A CA  1 
ATOM   410  C C   . LEU A 1 77  ? 1.838   -0.716  22.719  1.00 42.33  ? 77  LEU A C   1 
ATOM   411  O O   . LEU A 1 77  ? 1.858   -1.922  22.987  1.00 45.23  ? 77  LEU A O   1 
ATOM   412  C CB  . LEU A 1 77  ? 2.879   0.133   20.602  1.00 40.16  ? 77  LEU A CB  1 
ATOM   413  C CG  . LEU A 1 77  ? 2.816   0.047   19.080  1.00 44.59  ? 77  LEU A CG  1 
ATOM   414  C CD1 . LEU A 1 77  ? 3.993   0.829   18.447  1.00 52.57  ? 77  LEU A CD1 1 
ATOM   415  C CD2 . LEU A 1 77  ? 2.865   -1.411  18.688  1.00 41.49  ? 77  LEU A CD2 1 
ATOM   416  N N   . ALA A 1 78  ? 2.066   0.214   23.640  1.00 43.71  ? 78  ALA A N   1 
ATOM   417  C CA  . ALA A 1 78  ? 2.271   -0.191  25.024  1.00 48.93  ? 78  ALA A CA  1 
ATOM   418  C C   . ALA A 1 78  ? 1.048   -0.903  25.572  1.00 46.23  ? 78  ALA A C   1 
ATOM   419  O O   . ALA A 1 78  ? 1.179   -1.916  26.263  1.00 39.23  ? 78  ALA A O   1 
ATOM   420  C CB  . ALA A 1 78  ? 2.607   1.015   25.880  1.00 35.19  ? 78  ALA A CB  1 
ATOM   421  N N   . VAL A 1 79  ? -0.150  -0.398  25.262  1.00 41.20  ? 79  VAL A N   1 
ATOM   422  C CA  . VAL A 1 79  ? -1.376  -1.042  25.733  1.00 45.29  ? 79  VAL A CA  1 
ATOM   423  C C   . VAL A 1 79  ? -1.486  -2.445  25.173  1.00 47.61  ? 79  VAL A C   1 
ATOM   424  O O   . VAL A 1 79  ? -1.824  -3.396  25.889  1.00 39.48  ? 79  VAL A O   1 
ATOM   425  C CB  . VAL A 1 79  ? -2.615  -0.224  25.340  1.00 40.47  ? 79  VAL A CB  1 
ATOM   426  C CG1 . VAL A 1 79  ? -3.886  -1.090  25.521  1.00 40.07  ? 79  VAL A CG1 1 
ATOM   427  C CG2 . VAL A 1 79  ? -2.696  1.066   26.107  1.00 33.76  ? 79  VAL A CG2 1 
ATOM   428  N N   . GLY A 1 80  ? -1.270  -2.583  23.861  1.00 40.67  ? 80  GLY A N   1 
ATOM   429  C CA  . GLY A 1 80  ? -1.394  -3.888  23.236  1.00 41.62  ? 80  GLY A CA  1 
ATOM   430  C C   . GLY A 1 80  ? -0.413  -4.892  23.807  1.00 45.78  ? 80  GLY A C   1 
ATOM   431  O O   . GLY A 1 80  ? -0.782  -6.012  24.149  1.00 41.36  ? 80  GLY A O   1 
ATOM   432  N N   . ASN A 1 81  ? 0.854   -4.502  23.915  1.00 47.56  ? 81  ASN A N   1 
ATOM   433  C CA  . ASN A 1 81  ? 1.835   -5.418  24.486  1.00 44.20  ? 81  ASN A CA  1 
ATOM   434  C C   . ASN A 1 81  ? 1.477   -5.772  25.926  1.00 43.41  ? 81  ASN A C   1 
ATOM   435  O O   . ASN A 1 81  ? 1.586   -6.932  26.332  1.00 44.63  ? 81  ASN A O   1 
ATOM   436  C CB  . ASN A 1 81  ? 3.225   -4.792  24.398  1.00 45.16  ? 81  ASN A CB  1 
ATOM   437  C CG  . ASN A 1 81  ? 3.837   -4.946  23.015  1.00 55.24  ? 81  ASN A CG  1 
ATOM   438  O OD1 . ASN A 1 81  ? 4.144   -6.060  22.597  1.00 53.13  ? 81  ASN A OD1 1 
ATOM   439  N ND2 . ASN A 1 81  ? 3.977   -3.839  22.285  1.00 40.40  ? 81  ASN A ND2 1 
ATOM   440  N N   . TYR A 1 82  ? 1.036   -4.788  26.713  1.00 49.62  ? 82  TYR A N   1 
ATOM   441  C CA  . TYR A 1 82  ? 0.600   -5.065  28.082  1.00 42.67  ? 82  TYR A CA  1 
ATOM   442  C C   . TYR A 1 82  ? -0.446  -6.179  28.121  1.00 43.63  ? 82  TYR A C   1 
ATOM   443  O O   . TYR A 1 82  ? -0.317  -7.146  28.882  1.00 43.50  ? 82  TYR A O   1 
ATOM   444  C CB  . TYR A 1 82  ? 0.048   -3.790  28.719  1.00 42.54  ? 82  TYR A CB  1 
ATOM   445  C CG  . TYR A 1 82  ? -0.661  -4.020  30.041  1.00 47.64  ? 82  TYR A CG  1 
ATOM   446  C CD1 . TYR A 1 82  ? 0.039   -4.438  31.163  1.00 41.49  ? 82  TYR A CD1 1 
ATOM   447  C CD2 . TYR A 1 82  ? -2.033  -3.839  30.154  1.00 43.35  ? 82  TYR A CD2 1 
ATOM   448  C CE1 . TYR A 1 82  ? -0.613  -4.667  32.379  1.00 47.14  ? 82  TYR A CE1 1 
ATOM   449  C CE2 . TYR A 1 82  ? -2.688  -4.058  31.354  1.00 49.04  ? 82  TYR A CE2 1 
ATOM   450  C CZ  . TYR A 1 82  ? -1.971  -4.468  32.463  1.00 49.74  ? 82  TYR A CZ  1 
ATOM   451  O OH  . TYR A 1 82  ? -2.618  -4.695  33.655  1.00 47.35  ? 82  TYR A OH  1 
ATOM   452  N N   . ARG A 1 83  ? -1.477  -6.076  27.275  1.00 44.46  ? 83  ARG A N   1 
ATOM   453  C CA  . ARG A 1 83  ? -2.596  -7.023  27.327  1.00 40.28  ? 83  ARG A CA  1 
ATOM   454  C C   . ARG A 1 83  ? -2.193  -8.434  26.900  1.00 39.11  ? 83  ARG A C   1 
ATOM   455  O O   . ARG A 1 83  ? -2.824  -9.403  27.324  1.00 41.31  ? 83  ARG A O   1 
ATOM   456  C CB  . ARG A 1 83  ? -3.746  -6.521  26.461  1.00 40.00  ? 83  ARG A CB  1 
ATOM   457  C CG  . ARG A 1 83  ? -4.232  -5.142  26.892  1.00 43.06  ? 83  ARG A CG  1 
ATOM   458  C CD  . ARG A 1 83  ? -5.450  -4.704  26.114  1.00 44.87  ? 83  ARG A CD  1 
ATOM   459  N NE  . ARG A 1 83  ? -6.606  -5.550  26.383  1.00 43.19  ? 83  ARG A NE  1 
ATOM   460  C CZ  . ARG A 1 83  ? -7.508  -5.879  25.472  1.00 47.06  ? 83  ARG A CZ  1 
ATOM   461  N NH1 . ARG A 1 83  ? -7.375  -5.508  24.207  1.00 45.11  ? 83  ARG A NH1 1 
ATOM   462  N NH2 . ARG A 1 83  ? -8.558  -6.613  25.833  1.00 49.09  ? 83  ARG A NH2 1 
ATOM   463  N N   . LEU A 1 84  ? -1.160  -8.575  26.074  1.00 42.63  ? 84  LEU A N   1 
ATOM   464  C CA  . LEU A 1 84  ? -0.597  -9.874  25.729  1.00 46.89  ? 84  LEU A CA  1 
ATOM   465  C C   . LEU A 1 84  ? 0.529   -10.300 26.672  1.00 41.98  ? 84  LEU A C   1 
ATOM   466  O O   . LEU A 1 84  ? 1.244   -11.257 26.362  1.00 50.97  ? 84  LEU A O   1 
ATOM   467  C CB  . LEU A 1 84  ? -0.071  -9.842  24.287  1.00 50.15  ? 84  LEU A CB  1 
ATOM   468  C CG  . LEU A 1 84  ? -1.089  -9.465  23.207  1.00 47.53  ? 84  LEU A CG  1 
ATOM   469  C CD1 . LEU A 1 84  ? -0.374  -9.201  21.906  1.00 45.80  ? 84  LEU A CD1 1 
ATOM   470  C CD2 . LEU A 1 84  ? -2.091  -10.588 23.022  1.00 40.01  ? 84  LEU A CD2 1 
ATOM   471  N N   . LYS A 1 85  ? 0.738   -9.590  27.786  1.00 43.90  ? 85  LYS A N   1 
ATOM   472  C CA  . LYS A 1 85  ? 1.797   -9.925  28.751  1.00 54.75  ? 85  LYS A CA  1 
ATOM   473  C C   . LYS A 1 85  ? 3.198   -9.838  28.136  1.00 49.40  ? 85  LYS A C   1 
ATOM   474  O O   . LYS A 1 85  ? 4.118   -10.549 28.553  1.00 45.60  ? 85  LYS A O   1 
ATOM   475  C CB  . LYS A 1 85  ? 1.575   -11.312 29.366  1.00 54.95  ? 85  LYS A CB  1 
ATOM   476  C CG  . LYS A 1 85  ? 0.173   -11.536 29.931  1.00 53.46  ? 85  LYS A CG  1 
ATOM   477  C CD  . LYS A 1 85  ? 0.149   -12.735 30.881  1.00 57.40  ? 85  LYS A CD  1 
ATOM   478  C CE  . LYS A 1 85  ? -1.119  -12.739 31.751  1.00 72.21  ? 85  LYS A CE  1 
ATOM   479  N NZ  . LYS A 1 85  ? -1.062  -13.775 32.847  1.00 65.38  ? 85  LYS A NZ  1 
ATOM   480  N N   . GLU A 1 86  ? 3.367   -8.989  27.121  1.00 49.19  ? 86  GLU A N   1 
ATOM   481  C CA  . GLU A 1 86  ? 4.692   -8.617  26.624  1.00 53.28  ? 86  GLU A CA  1 
ATOM   482  C C   . GLU A 1 86  ? 5.165   -7.403  27.428  1.00 45.31  ? 86  GLU A C   1 
ATOM   483  O O   . GLU A 1 86  ? 5.139   -6.262  26.971  1.00 48.63  ? 86  GLU A O   1 
ATOM   484  C CB  . GLU A 1 86  ? 4.634   -8.310  25.132  1.00 48.32  ? 86  GLU A CB  1 
ATOM   485  C CG  . GLU A 1 86  ? 4.339   -9.487  24.226  1.00 43.62  ? 86  GLU A CG  1 
ATOM   486  C CD  . GLU A 1 86  ? 5.494   -10.463 24.113  1.00 55.24  ? 86  GLU A CD  1 
ATOM   487  O OE1 . GLU A 1 86  ? 6.631   -10.097 24.469  1.00 70.64  ? 86  GLU A OE1 1 
ATOM   488  O OE2 . GLU A 1 86  ? 5.262   -11.604 23.671  1.00 84.56  ? 86  GLU A OE2 1 
ATOM   489  N N   . TYR A 1 87  ? 5.572   -7.666  28.671  1.00 44.91  ? 87  TYR A N   1 
ATOM   490  C CA  . TYR A 1 87  ? 5.759   -6.567  29.610  1.00 47.80  ? 87  TYR A CA  1 
ATOM   491  C C   . TYR A 1 87  ? 7.005   -5.745  29.277  1.00 56.53  ? 87  TYR A C   1 
ATOM   492  O O   . TYR A 1 87  ? 7.003   -4.519  29.427  1.00 44.64  ? 87  TYR A O   1 
ATOM   493  C CB  . TYR A 1 87  ? 5.848   -7.097  31.039  1.00 49.58  ? 87  TYR A CB  1 
ATOM   494  C CG  . TYR A 1 87  ? 4.700   -7.966  31.528  1.00 49.48  ? 87  TYR A CG  1 
ATOM   495  C CD1 . TYR A 1 87  ? 3.386   -7.522  31.495  1.00 52.71  ? 87  TYR A CD1 1 
ATOM   496  C CD2 . TYR A 1 87  ? 4.955   -9.198  32.117  1.00 55.68  ? 87  TYR A CD2 1 
ATOM   497  C CE1 . TYR A 1 87  ? 2.350   -8.321  31.966  1.00 56.34  ? 87  TYR A CE1 1 
ATOM   498  C CE2 . TYR A 1 87  ? 3.941   -9.988  32.598  1.00 67.65  ? 87  TYR A CE2 1 
ATOM   499  C CZ  . TYR A 1 87  ? 2.646   -9.550  32.523  1.00 56.77  ? 87  TYR A CZ  1 
ATOM   500  O OH  . TYR A 1 87  ? 1.656   -10.356 33.020  1.00 69.88  ? 87  TYR A OH  1 
ATOM   501  N N   . GLU A 1 88  ? 8.090   -6.392  28.847  1.00 47.51  ? 88  GLU A N   1 
ATOM   502  C CA  . GLU A 1 88  ? 9.307   -5.630  28.559  1.00 56.61  ? 88  GLU A CA  1 
ATOM   503  C C   . GLU A 1 88  ? 9.106   -4.696  27.367  1.00 54.08  ? 88  GLU A C   1 
ATOM   504  O O   . GLU A 1 88  ? 9.595   -3.559  27.373  1.00 62.22  ? 88  GLU A O   1 
ATOM   505  C CB  . GLU A 1 88  ? 10.482  -6.585  28.311  1.00 51.45  ? 88  GLU A CB  1 
ATOM   506  C CG  . GLU A 1 88  ? 11.045  -7.322  29.562  1.00 64.70  ? 88  GLU A CG  1 
ATOM   507  C CD  . GLU A 1 88  ? 11.416  -6.446  30.786  1.00 84.68  ? 88  GLU A CD  1 
ATOM   508  O OE1 . GLU A 1 88  ? 12.139  -6.966  31.675  1.00 89.68  ? 88  GLU A OE1 1 
ATOM   509  O OE2 . GLU A 1 88  ? 11.033  -5.257  30.870  1.00 84.85  ? 88  GLU A OE2 1 
ATOM   510  N N   . LYS A 1 89  ? 8.387   -5.153  26.337  1.00 54.76  ? 89  LYS A N   1 
ATOM   511  C CA  . LYS A 1 89  ? 8.053   -4.282  25.212  1.00 49.64  ? 89  LYS A CA  1 
ATOM   512  C C   . LYS A 1 89  ? 7.139   -3.150  25.643  1.00 51.82  ? 89  LYS A C   1 
ATOM   513  O O   . LYS A 1 89  ? 7.377   -1.984  25.310  1.00 48.61  ? 89  LYS A O   1 
ATOM   514  C CB  . LYS A 1 89  ? 7.399   -5.094  24.098  1.00 50.81  ? 89  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 89  ? 8.281   -6.206  23.613  1.00 63.57  ? 89  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 89  ? 7.982   -6.611  22.185  1.00 77.40  ? 89  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 89  ? 7.504   -8.050  22.153  1.00 75.67  ? 89  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 89  ? 8.329   -8.853  21.213  1.00 70.31  ? 89  LYS A NZ  1 
ATOM   519  N N   . ALA A 1 90  ? 6.076   -3.474  26.381  1.00 41.75  ? 90  ALA A N   1 
ATOM   520  C CA  . ALA A 1 90  ? 5.159   -2.443  26.859  1.00 40.27  ? 90  ALA A CA  1 
ATOM   521  C C   . ALA A 1 90  ? 5.888   -1.393  27.678  1.00 47.83  ? 90  ALA A C   1 
ATOM   522  O O   . ALA A 1 90  ? 5.641   -0.188  27.526  1.00 39.69  ? 90  ALA A O   1 
ATOM   523  C CB  . ALA A 1 90  ? 4.052   -3.091  27.689  1.00 41.52  ? 90  ALA A CB  1 
ATOM   524  N N   . LEU A 1 91  ? 6.786   -1.838  28.563  1.00 48.95  ? 91  LEU A N   1 
ATOM   525  C CA  . LEU A 1 91  ? 7.547   -0.920  29.403  1.00 49.45  ? 91  LEU A CA  1 
ATOM   526  C C   . LEU A 1 91  ? 8.441   -0.015  28.569  1.00 48.71  ? 91  LEU A C   1 
ATOM   527  O O   . LEU A 1 91  ? 8.512   1.194   28.816  1.00 52.43  ? 91  LEU A O   1 
ATOM   528  C CB  . LEU A 1 91  ? 8.374   -1.709  30.417  1.00 55.02  ? 91  LEU A CB  1 
ATOM   529  C CG  . LEU A 1 91  ? 8.580   -1.040  31.773  1.00 53.98  ? 91  LEU A CG  1 
ATOM   530  C CD1 . LEU A 1 91  ? 7.254   -0.703  32.382  1.00 55.44  ? 91  LEU A CD1 1 
ATOM   531  C CD2 . LEU A 1 91  ? 9.347   -1.985  32.698  1.00 57.34  ? 91  LEU A CD2 1 
ATOM   532  N N   . LYS A 1 92  ? 9.104   -0.563  27.557  1.00 43.74  ? 92  LYS A N   1 
ATOM   533  C CA  . LYS A 1 92  ? 9.947   0.290   26.725  1.00 57.72  ? 92  LYS A CA  1 
ATOM   534  C C   . LYS A 1 92  ? 9.122   1.380   26.051  1.00 55.52  ? 92  LYS A C   1 
ATOM   535  O O   . LYS A 1 92  ? 9.533   2.546   26.018  1.00 44.34  ? 92  LYS A O   1 
ATOM   536  C CB  . LYS A 1 92  ? 10.710  -0.550  25.705  1.00 50.18  ? 92  LYS A CB  1 
ATOM   537  C CG  . LYS A 1 92  ? 11.874  -1.359  26.338  1.00 56.05  ? 92  LYS A CG  1 
ATOM   538  C CD  . LYS A 1 92  ? 12.435  -2.390  25.356  1.00 61.71  ? 92  LYS A CD  1 
ATOM   539  C CE  . LYS A 1 92  ? 13.825  -2.887  25.744  1.00 61.91  ? 92  LYS A CE  1 
ATOM   540  N NZ  . LYS A 1 92  ? 14.755  -2.890  24.578  1.00 81.39  ? 92  LYS A NZ  1 
ATOM   541  N N   . TYR A 1 93  ? 7.929   1.032   25.564  1.00 45.82  ? 93  TYR A N   1 
ATOM   542  C CA  . TYR A 1 93  ? 7.101   1.999   24.860  1.00 44.56  ? 93  TYR A CA  1 
ATOM   543  C C   . TYR A 1 93  ? 6.632   3.103   25.799  1.00 38.81  ? 93  TYR A C   1 
ATOM   544  O O   . TYR A 1 93  ? 6.779   4.291   25.495  1.00 41.37  ? 93  TYR A O   1 
ATOM   545  C CB  . TYR A 1 93  ? 5.908   1.290   24.207  1.00 51.28  ? 93  TYR A CB  1 
ATOM   546  C CG  . TYR A 1 93  ? 6.217   0.691   22.845  1.00 52.58  ? 93  TYR A CG  1 
ATOM   547  C CD1 . TYR A 1 93  ? 6.657   1.494   21.788  1.00 52.13  ? 93  TYR A CD1 1 
ATOM   548  C CD2 . TYR A 1 93  ? 6.077   -0.673  22.614  1.00 57.70  ? 93  TYR A CD2 1 
ATOM   549  C CE1 . TYR A 1 93  ? 6.940   0.946   20.545  1.00 54.91  ? 93  TYR A CE1 1 
ATOM   550  C CE2 . TYR A 1 93  ? 6.354   -1.223  21.379  1.00 42.63  ? 93  TYR A CE2 1 
ATOM   551  C CZ  . TYR A 1 93  ? 6.789   -0.413  20.352  1.00 58.81  ? 93  TYR A CZ  1 
ATOM   552  O OH  . TYR A 1 93  ? 7.070   -0.965  19.128  1.00 63.91  ? 93  TYR A OH  1 
ATOM   553  N N   . VAL A 1 94  ? 6.088   2.731   26.963  1.00 43.78  ? 94  VAL A N   1 
ATOM   554  C CA  . VAL A 1 94  ? 5.521   3.736   27.853  1.00 39.36  ? 94  VAL A CA  1 
ATOM   555  C C   . VAL A 1 94  ? 6.623   4.606   28.458  1.00 41.92  ? 94  VAL A C   1 
ATOM   556  O O   . VAL A 1 94  ? 6.433   5.816   28.646  1.00 42.46  ? 94  VAL A O   1 
ATOM   557  C CB  . VAL A 1 94  ? 4.652   3.070   28.935  1.00 46.87  ? 94  VAL A CB  1 
ATOM   558  C CG1 . VAL A 1 94  ? 5.498   2.564   30.093  1.00 44.70  ? 94  VAL A CG1 1 
ATOM   559  C CG2 . VAL A 1 94  ? 3.583   4.037   29.425  1.00 46.45  ? 94  VAL A CG2 1 
ATOM   560  N N   . ARG A 1 95  ? 7.791   4.016   28.759  1.00 43.01  ? 95  ARG A N   1 
ATOM   561  C CA  . ARG A 1 95  ? 8.885   4.797   29.333  1.00 51.71  ? 95  ARG A CA  1 
ATOM   562  C C   . ARG A 1 95  ? 9.366   5.857   28.361  1.00 44.43  ? 95  ARG A C   1 
ATOM   563  O O   . ARG A 1 95  ? 9.644   6.989   28.763  1.00 54.52  ? 95  ARG A O   1 
ATOM   564  C CB  . ARG A 1 95  ? 10.054  3.895   29.753  1.00 57.47  ? 95  ARG A CB  1 
ATOM   565  C CG  . ARG A 1 95  ? 9.703   2.897   30.846  1.00 70.79  ? 95  ARG A CG  1 
ATOM   566  C CD  . ARG A 1 95  ? 10.492  3.106   32.121  1.00 63.37  ? 95  ARG A CD  1 
ATOM   567  N NE  . ARG A 1 95  ? 9.918   2.326   33.212  1.00 70.32  ? 95  ARG A NE  1 
ATOM   568  C CZ  . ARG A 1 95  ? 10.462  1.243   33.751  1.00 76.40  ? 95  ARG A CZ  1 
ATOM   569  N NH1 . ARG A 1 95  ? 11.606  0.748   33.309  1.00 68.86  ? 95  ARG A NH1 1 
ATOM   570  N NH2 . ARG A 1 95  ? 9.834   0.636   34.758  1.00 77.66  ? 95  ARG A NH2 1 
ATOM   571  N N   . GLY A 1 96  ? 9.453   5.518   27.074  1.00 48.63  ? 96  GLY A N   1 
ATOM   572  C CA  . GLY A 1 96  ? 9.788   6.530   26.083  1.00 47.12  ? 96  GLY A CA  1 
ATOM   573  C C   . GLY A 1 96  ? 8.758   7.640   26.045  1.00 49.18  ? 96  GLY A C   1 
ATOM   574  O O   . GLY A 1 96  ? 9.096   8.820   25.917  1.00 44.42  ? 96  GLY A O   1 
ATOM   575  N N   . LEU A 1 97  ? 7.486   7.284   26.195  1.00 42.77  ? 97  LEU A N   1 
ATOM   576  C CA  . LEU A 1 97  ? 6.457   8.310   26.211  1.00 47.75  ? 97  LEU A CA  1 
ATOM   577  C C   . LEU A 1 97  ? 6.570   9.164   27.469  1.00 44.97  ? 97  LEU A C   1 
ATOM   578  O O   . LEU A 1 97  ? 6.388   10.387  27.421  1.00 44.21  ? 97  LEU A O   1 
ATOM   579  C CB  . LEU A 1 97  ? 5.087   7.641   26.100  1.00 41.45  ? 97  LEU A CB  1 
ATOM   580  C CG  . LEU A 1 97  ? 3.831   8.466   26.087  1.00 48.37  ? 97  LEU A CG  1 
ATOM   581  C CD1 . LEU A 1 97  ? 3.901   9.508   24.988  1.00 55.18  ? 97  LEU A CD1 1 
ATOM   582  C CD2 . LEU A 1 97  ? 2.636   7.516   25.871  1.00 53.64  ? 97  LEU A CD2 1 
ATOM   583  N N   . LEU A 1 98  ? 6.915   8.539   28.598  1.00 43.90  ? 98  LEU A N   1 
ATOM   584  C CA  . LEU A 1 98  ? 7.112   9.299   29.825  1.00 46.14  ? 98  LEU A CA  1 
ATOM   585  C C   . LEU A 1 98  ? 8.332   10.203  29.748  1.00 54.81  ? 98  LEU A C   1 
ATOM   586  O O   . LEU A 1 98  ? 8.364   11.238  30.419  1.00 55.05  ? 98  LEU A O   1 
ATOM   587  C CB  . LEU A 1 98  ? 7.219   8.348   31.011  1.00 43.20  ? 98  LEU A CB  1 
ATOM   588  C CG  . LEU A 1 98  ? 5.799   7.867   31.328  1.00 48.30  ? 98  LEU A CG  1 
ATOM   589  C CD1 . LEU A 1 98  ? 5.808   6.654   32.248  1.00 44.03  ? 98  LEU A CD1 1 
ATOM   590  C CD2 . LEU A 1 98  ? 4.980   9.005   31.922  1.00 53.50  ? 98  LEU A CD2 1 
ATOM   591  N N   . GLN A 1 99  ? 9.338   9.839   28.946  1.00 51.10  ? 99  GLN A N   1 
ATOM   592  C CA  . GLN A 1 99  ? 10.480  10.734  28.742  1.00 60.44  ? 99  GLN A CA  1 
ATOM   593  C C   . GLN A 1 99  ? 10.033  12.033  28.097  1.00 56.45  ? 99  GLN A C   1 
ATOM   594  O O   . GLN A 1 99  ? 10.476  13.123  28.489  1.00 54.82  ? 99  GLN A O   1 
ATOM   595  C CB  . GLN A 1 99  ? 11.533  10.074  27.846  1.00 55.70  ? 99  GLN A CB  1 
ATOM   596  C CG  . GLN A 1 99  ? 12.711  9.416   28.541  1.00 86.42  ? 99  GLN A CG  1 
ATOM   597  C CD  . GLN A 1 99  ? 13.375  8.343   27.663  1.00 91.75  ? 99  GLN A CD  1 
ATOM   598  O OE1 . GLN A 1 99  ? 13.696  7.245   28.131  1.00 96.76  ? 99  GLN A OE1 1 
ATOM   599  N NE2 . GLN A 1 99  ? 13.565  8.659   26.380  1.00 72.41  ? 99  GLN A NE2 1 
ATOM   600  N N   . THR A 1 100 ? 9.173   11.933  27.080  1.00 54.57  ? 100 THR A N   1 
ATOM   601  C CA  . THR A 1 100 ? 8.736   13.115  26.341  1.00 55.27  ? 100 THR A CA  1 
ATOM   602  C C   . THR A 1 100 ? 7.659   13.870  27.107  1.00 67.10  ? 100 THR A C   1 
ATOM   603  O O   . THR A 1 100 ? 7.593   15.105  27.042  1.00 58.51  ? 100 THR A O   1 
ATOM   604  C CB  . THR A 1 100 ? 8.201   12.696  24.969  1.00 55.66  ? 100 THR A CB  1 
ATOM   605  O OG1 . THR A 1 100 ? 9.250   12.086  24.212  1.00 83.13  ? 100 THR A OG1 1 
ATOM   606  C CG2 . THR A 1 100 ? 7.720   13.903  24.201  1.00 62.03  ? 100 THR A CG2 1 
ATOM   607  N N   . GLU A 1 101 ? 6.809   13.141  27.831  1.00 47.43  ? 101 GLU A N   1 
ATOM   608  C CA  . GLU A 1 101 ? 5.673   13.706  28.557  1.00 57.35  ? 101 GLU A CA  1 
ATOM   609  C C   . GLU A 1 101 ? 5.719   13.222  29.994  1.00 49.96  ? 101 GLU A C   1 
ATOM   610  O O   . GLU A 1 101 ? 4.968   12.314  30.379  1.00 49.74  ? 101 GLU A O   1 
ATOM   611  C CB  . GLU A 1 101 ? 4.356   13.300  27.907  1.00 53.27  ? 101 GLU A CB  1 
ATOM   612  C CG  . GLU A 1 101 ? 4.137   13.958  26.594  1.00 57.48  ? 101 GLU A CG  1 
ATOM   613  C CD  . GLU A 1 101 ? 2.867   13.498  25.941  1.00 69.27  ? 101 GLU A CD  1 
ATOM   614  O OE1 . GLU A 1 101 ? 1.855   13.316  26.656  1.00 61.83  ? 101 GLU A OE1 1 
ATOM   615  O OE2 . GLU A 1 101 ? 2.881   13.336  24.708  1.00 67.44  ? 101 GLU A OE2 1 
ATOM   616  N N   . PRO A 1 102 ? 6.581   13.817  30.817  1.00 57.28  ? 102 PRO A N   1 
ATOM   617  C CA  . PRO A 1 102 ? 6.745   13.326  32.195  1.00 55.22  ? 102 PRO A CA  1 
ATOM   618  C C   . PRO A 1 102 ? 5.475   13.396  33.023  1.00 57.69  ? 102 PRO A C   1 
ATOM   619  O O   . PRO A 1 102 ? 5.330   12.613  33.971  1.00 58.63  ? 102 PRO A O   1 
ATOM   620  C CB  . PRO A 1 102 ? 7.837   14.243  32.774  1.00 57.91  ? 102 PRO A CB  1 
ATOM   621  C CG  . PRO A 1 102 ? 8.366   15.056  31.620  1.00 55.98  ? 102 PRO A CG  1 
ATOM   622  C CD  . PRO A 1 102 ? 7.330   15.058  30.558  1.00 56.44  ? 102 PRO A CD  1 
ATOM   623  N N   . GLN A 1 103 ? 4.552   14.302  32.698  1.00 58.03  ? 103 GLN A N   1 
ATOM   624  C CA  . GLN A 1 103 ? 3.319   14.478  33.455  1.00 57.83  ? 103 GLN A CA  1 
ATOM   625  C C   . GLN A 1 103 ? 2.154   13.670  32.913  1.00 53.92  ? 103 GLN A C   1 
ATOM   626  O O   . GLN A 1 103 ? 1.045   13.797  33.436  1.00 66.64  ? 103 GLN A O   1 
ATOM   627  C CB  . GLN A 1 103 ? 2.919   15.957  33.494  1.00 61.24  ? 103 GLN A CB  1 
ATOM   628  C CG  . GLN A 1 103 ? 4.019   16.877  33.967  1.00 79.66  ? 103 GLN A CG  1 
ATOM   629  C CD  . GLN A 1 103 ? 4.552   16.444  35.316  1.00 84.36  ? 103 GLN A CD  1 
ATOM   630  O OE1 . GLN A 1 103 ? 5.755   16.240  35.490  1.00 73.43  ? 103 GLN A OE1 1 
ATOM   631  N NE2 . GLN A 1 103 ? 3.647   16.283  36.283  1.00 78.48  ? 103 GLN A NE2 1 
ATOM   632  N N   . ASN A 1 104 ? 2.366   12.851  31.887  1.00 51.67  ? 104 ASN A N   1 
ATOM   633  C CA  . ASN A 1 104 ? 1.266   12.125  31.257  1.00 53.29  ? 104 ASN A CA  1 
ATOM   634  C C   . ASN A 1 104 ? 0.724   11.064  32.210  1.00 49.17  ? 104 ASN A C   1 
ATOM   635  O O   . ASN A 1 104 ? 1.343   10.010  32.389  1.00 45.02  ? 104 ASN A O   1 
ATOM   636  C CB  . ASN A 1 104 ? 1.743   11.505  29.947  1.00 45.14  ? 104 ASN A CB  1 
ATOM   637  C CG  . ASN A 1 104 ? 0.604   10.910  29.141  1.00 52.32  ? 104 ASN A CG  1 
ATOM   638  O OD1 . ASN A 1 104 ? -0.255  10.224  29.684  1.00 49.61  ? 104 ASN A OD1 1 
ATOM   639  N ND2 . ASN A 1 104 ? 0.591   11.173  27.840  1.00 54.52  ? 104 ASN A ND2 1 
ATOM   640  N N   . ASN A 1 105 ? -0.451  11.319  32.798  1.00 47.94  ? 105 ASN A N   1 
ATOM   641  C CA  . ASN A 1 105 ? -0.982  10.429  33.832  1.00 45.85  ? 105 ASN A CA  1 
ATOM   642  C C   . ASN A 1 105 ? -1.577  9.141   33.271  1.00 46.38  ? 105 ASN A C   1 
ATOM   643  O O   . ASN A 1 105 ? -1.628  8.135   33.987  1.00 47.30  ? 105 ASN A O   1 
ATOM   644  C CB  . ASN A 1 105 ? -2.015  11.166  34.694  1.00 43.24  ? 105 ASN A CB  1 
ATOM   645  C CG  . ASN A 1 105 ? -3.182  11.717  33.878  1.00 62.79  ? 105 ASN A CG  1 
ATOM   646  O OD1 . ASN A 1 105 ? -2.982  12.535  32.987  1.00 48.67  ? 105 ASN A OD1 1 
ATOM   647  N ND2 . ASN A 1 105 ? -4.411  11.286  34.203  1.00 45.71  ? 105 ASN A ND2 1 
ATOM   648  N N   . GLN A 1 106 ? -2.015  9.120   32.011  1.00 46.58  ? 106 GLN A N   1 
ATOM   649  C CA  . GLN A 1 106 ? -2.437  7.843   31.447  1.00 47.64  ? 106 GLN A CA  1 
ATOM   650  C C   . GLN A 1 106 ? -1.244  6.936   31.221  1.00 52.47  ? 106 GLN A C   1 
ATOM   651  O O   . GLN A 1 106 ? -1.329  5.720   31.428  1.00 42.12  ? 106 GLN A O   1 
ATOM   652  C CB  . GLN A 1 106 ? -3.166  8.040   30.133  1.00 43.92  ? 106 GLN A CB  1 
ATOM   653  C CG  . GLN A 1 106 ? -4.573  8.488   30.290  1.00 53.25  ? 106 GLN A CG  1 
ATOM   654  C CD  . GLN A 1 106 ? -5.086  8.997   28.992  1.00 60.43  ? 106 GLN A CD  1 
ATOM   655  O OE1 . GLN A 1 106 ? -4.812  10.136  28.608  1.00 61.74  ? 106 GLN A OE1 1 
ATOM   656  N NE2 . GLN A 1 106 ? -5.781  8.133   28.260  1.00 49.35  ? 106 GLN A NE2 1 
ATOM   657  N N   . ALA A 1 107 ? -0.131  7.506   30.764  1.00 41.58  ? 107 ALA A N   1 
ATOM   658  C CA  . ALA A 1 107 ? 1.067   6.699   30.592  1.00 40.79  ? 107 ALA A CA  1 
ATOM   659  C C   . ALA A 1 107 ? 1.590   6.226   31.944  1.00 38.83  ? 107 ALA A C   1 
ATOM   660  O O   . ALA A 1 107 ? 1.913   5.044   32.118  1.00 42.57  ? 107 ALA A O   1 
ATOM   661  C CB  . ALA A 1 107 ? 2.129   7.497   29.830  1.00 46.76  ? 107 ALA A CB  1 
ATOM   662  N N   . LYS A 1 108 ? 1.668   7.129   32.924  1.00 39.24  ? 108 LYS A N   1 
ATOM   663  C CA  . LYS A 1 108 ? 2.145   6.713   34.237  1.00 40.91  ? 108 LYS A CA  1 
ATOM   664  C C   . LYS A 1 108 ? 1.279   5.595   34.811  1.00 40.34  ? 108 LYS A C   1 
ATOM   665  O O   . LYS A 1 108 ? 1.804   4.619   35.360  1.00 39.61  ? 108 LYS A O   1 
ATOM   666  C CB  . LYS A 1 108 ? 2.203   7.910   35.171  1.00 41.85  ? 108 LYS A CB  1 
ATOM   667  C CG  . LYS A 1 108 ? 3.026   7.687   36.433  1.00 48.35  ? 108 LYS A CG  1 
ATOM   668  C CD  . LYS A 1 108 ? 4.489   7.387   36.081  1.00 45.81  ? 108 LYS A CD  1 
ATOM   669  C CE  . LYS A 1 108 ? 5.349   7.295   37.335  1.00 57.86  ? 108 LYS A CE  1 
ATOM   670  N NZ  . LYS A 1 108 ? 6.755   6.855   37.069  1.00 50.44  ? 108 LYS A NZ  1 
ATOM   671  N N   . GLU A 1 109 ? -0.050  5.694   34.653  1.00 39.98  ? 109 GLU A N   1 
ATOM   672  C CA  . GLU A 1 109 ? -0.939  4.633   35.132  1.00 41.59  ? 109 GLU A CA  1 
ATOM   673  C C   . GLU A 1 109 ? -0.681  3.315   34.415  1.00 45.73  ? 109 GLU A C   1 
ATOM   674  O O   . GLU A 1 109 ? -0.676  2.245   35.040  1.00 44.44  ? 109 GLU A O   1 
ATOM   675  C CB  . GLU A 1 109 ? -2.403  5.053   34.957  1.00 41.14  ? 109 GLU A CB  1 
ATOM   676  C CG  . GLU A 1 109 ? -3.409  3.920   35.223  1.00 51.43  ? 109 GLU A CG  1 
ATOM   677  C CD  . GLU A 1 109 ? -3.464  3.506   36.677  1.00 53.17  ? 109 GLU A CD  1 
ATOM   678  O OE1 . GLU A 1 109 ? -2.792  4.158   37.518  1.00 60.04  ? 109 GLU A OE1 1 
ATOM   679  O OE2 . GLU A 1 109 ? -4.170  2.521   36.984  1.00 61.07  ? 109 GLU A OE2 1 
ATOM   680  N N   . LEU A 1 110 ? -0.498  3.358   33.092  1.00 45.53  ? 110 LEU A N   1 
ATOM   681  C CA  . LEU A 1 110 ? -0.184  2.128   32.374  1.00 38.22  ? 110 LEU A CA  1 
ATOM   682  C C   . LEU A 1 110 ? 1.147   1.547   32.833  1.00 45.74  ? 110 LEU A C   1 
ATOM   683  O O   . LEU A 1 110 ? 1.306   0.325   32.878  1.00 42.07  ? 110 LEU A O   1 
ATOM   684  C CB  . LEU A 1 110 ? -0.168  2.392   30.869  1.00 39.57  ? 110 LEU A CB  1 
ATOM   685  C CG  . LEU A 1 110 ? 0.163   1.223   29.942  1.00 46.96  ? 110 LEU A CG  1 
ATOM   686  C CD1 . LEU A 1 110 ? -0.750  0.031   30.214  1.00 42.83  ? 110 LEU A CD1 1 
ATOM   687  C CD2 . LEU A 1 110 ? 0.073   1.640   28.493  1.00 41.75  ? 110 LEU A CD2 1 
ATOM   688  N N   . GLU A 1 111 ? 2.111   2.403   33.207  1.00 43.81  ? 111 GLU A N   1 
ATOM   689  C CA  . GLU A 1 111 ? 3.380   1.896   33.727  1.00 42.87  ? 111 GLU A CA  1 
ATOM   690  C C   . GLU A 1 111 ? 3.188   1.212   35.074  1.00 48.50  ? 111 GLU A C   1 
ATOM   691  O O   . GLU A 1 111 ? 3.733   0.127   35.309  1.00 44.53  ? 111 GLU A O   1 
ATOM   692  C CB  . GLU A 1 111 ? 4.401   3.040   33.838  1.00 49.75  ? 111 GLU A CB  1 
ATOM   693  C CG  . GLU A 1 111 ? 5.816   2.599   34.224  1.00 60.08  ? 111 GLU A CG  1 
ATOM   694  C CD  . GLU A 1 111 ? 6.686   3.725   34.803  1.00 58.75  ? 111 GLU A CD  1 
ATOM   695  O OE1 . GLU A 1 111 ? 6.260   4.448   35.727  1.00 58.55  ? 111 GLU A OE1 1 
ATOM   696  O OE2 . GLU A 1 111 ? 7.827   3.874   34.334  1.00 61.33  ? 111 GLU A OE2 1 
ATOM   697  N N   . ARG A 1 112 ? 2.443   1.851   35.979  1.00 46.47  ? 112 ARG A N   1 
ATOM   698  C CA  . ARG A 1 112 ? 2.083   1.223   37.243  1.00 49.91  ? 112 ARG A CA  1 
ATOM   699  C C   . ARG A 1 112 ? 1.471   -0.156  37.010  1.00 45.55  ? 112 ARG A C   1 
ATOM   700  O O   . ARG A 1 112 ? 1.885   -1.132  37.643  1.00 46.11  ? 112 ARG A O   1 
ATOM   701  C CB  . ARG A 1 112 ? 1.129   2.144   38.015  1.00 50.05  ? 112 ARG A CB  1 
ATOM   702  C CG  . ARG A 1 112 ? 0.876   1.751   39.462  1.00 61.61  ? 112 ARG A CG  1 
ATOM   703  C CD  . ARG A 1 112 ? -0.372  2.437   40.063  1.00 56.08  ? 112 ARG A CD  1 
ATOM   704  N NE  . ARG A 1 112 ? -1.600  2.001   39.410  1.00 60.14  ? 112 ARG A NE  1 
ATOM   705  C CZ  . ARG A 1 112 ? -2.384  1.015   39.827  1.00 63.75  ? 112 ARG A CZ  1 
ATOM   706  N NH1 . ARG A 1 112 ? -2.063  0.262   40.871  1.00 60.81  ? 112 ARG A NH1 1 
ATOM   707  N NH2 . ARG A 1 112 ? -3.504  0.757   39.158  1.00 56.89  ? 112 ARG A NH2 1 
ATOM   708  N N   . LEU A 1 113 ? 0.556   -0.279  36.036  1.00 43.95  ? 113 LEU A N   1 
ATOM   709  C CA  . LEU A 1 113 ? -0.052  -1.580  35.750  1.00 37.49  ? 113 LEU A CA  1 
ATOM   710  C C   . LEU A 1 113 ? 0.978   -2.594  35.256  1.00 48.15  ? 113 LEU A C   1 
ATOM   711  O O   . LEU A 1 113 ? 0.981   -3.751  35.695  1.00 44.48  ? 113 LEU A O   1 
ATOM   712  C CB  . LEU A 1 113 ? -1.189  -1.444  34.736  1.00 40.41  ? 113 LEU A CB  1 
ATOM   713  C CG  . LEU A 1 113 ? -2.447  -0.673  35.141  1.00 42.72  ? 113 LEU A CG  1 
ATOM   714  C CD1 . LEU A 1 113 ? -3.513  -0.802  34.064  1.00 44.56  ? 113 LEU A CD1 1 
ATOM   715  C CD2 . LEU A 1 113 ? -2.975  -1.197  36.479  1.00 47.59  ? 113 LEU A CD2 1 
ATOM   716  N N   . ILE A 1 114 ? 1.861   -2.195  34.336  1.00 46.33  ? 114 ILE A N   1 
ATOM   717  C CA  . ILE A 1 114 ? 2.880   -3.139  33.868  1.00 50.00  ? 114 ILE A CA  1 
ATOM   718  C C   . ILE A 1 114 ? 3.761   -3.597  35.030  1.00 43.71  ? 114 ILE A C   1 
ATOM   719  O O   . ILE A 1 114 ? 3.977   -4.799  35.231  1.00 45.86  ? 114 ILE A O   1 
ATOM   720  C CB  . ILE A 1 114 ? 3.725   -2.532  32.735  1.00 43.40  ? 114 ILE A CB  1 
ATOM   721  C CG1 . ILE A 1 114 ? 2.879   -2.286  31.489  1.00 49.62  ? 114 ILE A CG1 1 
ATOM   722  C CG2 . ILE A 1 114 ? 4.880   -3.468  32.375  1.00 46.38  ? 114 ILE A CG2 1 
ATOM   723  C CD1 . ILE A 1 114 ? 3.222   -1.009  30.783  1.00 43.17  ? 114 ILE A CD1 1 
ATOM   724  N N   . ASP A 1 115 ? 4.279   -2.643  35.812  1.00 46.59  ? 115 ASP A N   1 
ATOM   725  C CA  . ASP A 1 115 ? 5.114   -2.984  36.967  1.00 48.99  ? 115 ASP A CA  1 
ATOM   726  C C   . ASP A 1 115 ? 4.444   -4.035  37.834  1.00 52.68  ? 115 ASP A C   1 
ATOM   727  O O   . ASP A 1 115 ? 5.085   -4.984  38.296  1.00 52.94  ? 115 ASP A O   1 
ATOM   728  C CB  . ASP A 1 115 ? 5.396   -1.744  37.819  1.00 52.23  ? 115 ASP A CB  1 
ATOM   729  C CG  . ASP A 1 115 ? 6.548   -0.908  37.287  1.00 78.12  ? 115 ASP A CG  1 
ATOM   730  O OD1 . ASP A 1 115 ? 7.303   -1.425  36.438  1.00 71.01  ? 115 ASP A OD1 1 
ATOM   731  O OD2 . ASP A 1 115 ? 6.715   0.252   37.745  1.00 70.78  ? 115 ASP A OD2 1 
ATOM   732  N N   . LYS A 1 116 ? 3.143   -3.894  38.048  1.00 47.73  ? 116 LYS A N   1 
ATOM   733  C CA  . LYS A 1 116 ? 2.459   -4.816  38.937  1.00 58.71  ? 116 LYS A CA  1 
ATOM   734  C C   . LYS A 1 116 ? 2.298   -6.193  38.304  1.00 45.61  ? 116 LYS A C   1 
ATOM   735  O O   . LYS A 1 116 ? 2.494   -7.215  38.970  1.00 48.03  ? 116 LYS A O   1 
ATOM   736  C CB  . LYS A 1 116 ? 1.112   -4.228  39.338  1.00 53.84  ? 116 LYS A CB  1 
ATOM   737  C CG  . LYS A 1 116 ? 0.298   -5.153  40.193  1.00 63.21  ? 116 LYS A CG  1 
ATOM   738  C CD  . LYS A 1 116 ? -0.552  -4.345  41.126  1.00 68.33  ? 116 LYS A CD  1 
ATOM   739  C CE  . LYS A 1 116 ? -1.763  -3.890  40.396  1.00 71.82  ? 116 LYS A CE  1 
ATOM   740  N NZ  . LYS A 1 116 ? -2.152  -4.918  39.396  1.00 82.42  ? 116 LYS A NZ  1 
ATOM   741  N N   . ALA A 1 117 ? 1.950   -6.247  37.019  1.00 50.04  ? 117 ALA A N   1 
ATOM   742  C CA  . ALA A 1 117 ? 1.786   -7.538  36.361  1.00 48.20  ? 117 ALA A CA  1 
ATOM   743  C C   . ALA A 1 117 ? 3.099   -8.295  36.280  1.00 56.02  ? 117 ALA A C   1 
ATOM   744  O O   . ALA A 1 117 ? 3.099   -9.530  36.224  1.00 47.40  ? 117 ALA A O   1 
ATOM   745  C CB  . ALA A 1 117 ? 1.218   -7.346  34.958  1.00 50.15  ? 117 ALA A CB  1 
ATOM   746  N N   . MET A 1 118 ? 4.222   -7.578  36.270  1.00 46.70  ? 118 MET A N   1 
ATOM   747  C CA  . MET A 1 118 ? 5.515   -8.230  36.175  1.00 49.97  ? 118 MET A CA  1 
ATOM   748  C C   . MET A 1 118 ? 5.877   -8.992  37.436  1.00 50.02  ? 118 MET A C   1 
ATOM   749  O O   . MET A 1 118 ? 6.717   -9.889  37.366  1.00 57.87  ? 118 MET A O   1 
ATOM   750  C CB  . MET A 1 118 ? 6.602   -7.196  35.863  1.00 48.26  ? 118 MET A CB  1 
ATOM   751  C CG  . MET A 1 118 ? 6.533   -6.652  34.451  1.00 61.35  ? 118 MET A CG  1 
ATOM   752  S SD  . MET A 1 118 ? 7.763   -5.361  34.148  1.00 69.10  ? 118 MET A SD  1 
ATOM   753  C CE  . MET A 1 118 ? 9.210   -6.346  33.776  1.00 62.73  ? 118 MET A CE  1 
ATOM   754  N N   . LYS A 1 119 ? 5.282   -8.664  38.588  1.00 51.97  ? 119 LYS A N   1 
ATOM   755  C CA  . LYS A 1 119 ? 5.715   -9.327  39.822  1.00 54.18  ? 119 LYS A CA  1 
ATOM   756  C C   . LYS A 1 119 ? 5.187   -10.755 39.925  1.00 55.83  ? 119 LYS A C   1 
ATOM   757  O O   . LYS A 1 119 ? 5.861   -11.622 40.495  1.00 55.90  ? 119 LYS A O   1 
ATOM   758  C CB  . LYS A 1 119 ? 5.289   -8.509  41.047  1.00 64.60  ? 119 LYS A CB  1 
ATOM   759  C CG  . LYS A 1 119 ? 5.873   -7.089  41.065  1.00 65.44  ? 119 LYS A CG  1 
ATOM   760  C CD  . LYS A 1 119 ? 5.301   -6.248  42.194  1.00 72.20  ? 119 LYS A CD  1 
ATOM   761  C CE  . LYS A 1 119 ? 5.728   -4.786  42.060  1.00 80.01  ? 119 LYS A CE  1 
ATOM   762  N NZ  . LYS A 1 119 ? 4.554   -3.898  41.754  1.00 86.11  ? 119 LYS A NZ  1 
ATOM   763  N N   . LYS A 1 120 ? 3.992   -11.024 39.400  1.00 52.56  ? 120 LYS A N   1 
ATOM   764  C CA  . LYS A 1 120 ? 3.421   -12.357 39.539  1.00 53.00  ? 120 LYS A CA  1 
ATOM   765  C C   . LYS A 1 120 ? 2.418   -12.588 38.424  1.00 47.77  ? 120 LYS A C   1 
ATOM   766  O O   . LYS A 1 120 ? 1.621   -11.696 38.113  1.00 55.51  ? 120 LYS A O   1 
ATOM   767  C CB  . LYS A 1 120 ? 2.757   -12.527 40.903  1.00 53.00  ? 120 LYS A CB  1 
ATOM   768  C CG  . LYS A 1 120 ? 2.310   -13.953 41.212  1.00 53.95  ? 120 LYS A CG  1 
ATOM   769  C CD  . LYS A 1 120 ? 2.080   -14.131 42.714  1.00 56.63  ? 120 LYS A CD  1 
ATOM   770  C CE  . LYS A 1 120 ? 1.719   -15.568 43.059  1.00 59.68  ? 120 LYS A CE  1 
ATOM   771  N NZ  . LYS A 1 120 ? 1.543   -15.767 44.520  1.00 62.74  ? 120 LYS A NZ  1 
ATOM   772  N N   . ASP A 1 121 ? 2.461   -13.778 37.824  1.00 57.09  ? 121 ASP A N   1 
ATOM   773  C CA  . ASP A 1 121 ? 1.533   -14.094 36.741  1.00 51.23  ? 121 ASP A CA  1 
ATOM   774  C C   . ASP A 1 121 ? 0.116   -14.136 37.292  1.00 52.75  ? 121 ASP A C   1 
ATOM   775  O O   . ASP A 1 121 ? -0.169  -14.872 38.245  1.00 56.48  ? 121 ASP A O   1 
ATOM   776  C CB  . ASP A 1 121 ? 1.894   -15.433 36.088  1.00 56.33  ? 121 ASP A CB  1 
ATOM   777  C CG  . ASP A 1 121 ? 1.039   -15.736 34.865  1.00 67.33  ? 121 ASP A CG  1 
ATOM   778  O OD1 . ASP A 1 121 ? 1.106   -14.968 33.884  1.00 62.04  ? 121 ASP A OD1 1 
ATOM   779  O OD2 . ASP A 1 121 ? 0.289   -16.740 34.885  1.00 66.66  ? 121 ASP A OD2 1 
ATOM   780  N N   . GLY A 1 122 ? -0.760  -13.337 36.715  1.00 56.23  ? 122 GLY A N   1 
ATOM   781  C CA  . GLY A 1 122 ? -2.138  -13.349 37.134  1.00 68.08  ? 122 GLY A CA  1 
ATOM   782  C C   . GLY A 1 122 ? -3.046  -12.736 36.102  1.00 63.56  ? 122 GLY A C   1 
ATOM   783  O O   . GLY A 1 122 ? -2.677  -12.579 34.933  1.00 52.43  ? 122 GLY A O   1 
ATOM   784  N N   . LEU A 1 123 ? -4.248  -12.396 36.564  1.00 64.97  ? 123 LEU A N   1 
ATOM   785  C CA  . LEU A 1 123 ? -5.272  -11.752 35.751  1.00 50.92  ? 123 LEU A CA  1 
ATOM   786  C C   . LEU A 1 123 ? -4.991  -10.257 35.664  1.00 61.44  ? 123 LEU A C   1 
ATOM   787  O O   . LEU A 1 123 ? -5.004  -9.566  36.690  1.00 57.96  ? 123 LEU A O   1 
ATOM   788  C CB  . LEU A 1 123 ? -6.640  -12.008 36.379  1.00 58.34  ? 123 LEU A CB  1 
ATOM   789  C CG  . LEU A 1 123 ? -7.924  -11.746 35.603  1.00 55.52  ? 123 LEU A CG  1 
ATOM   790  C CD1 . LEU A 1 123 ? -8.011  -12.701 34.419  1.00 51.22  ? 123 LEU A CD1 1 
ATOM   791  C CD2 . LEU A 1 123 ? -9.160  -11.893 36.543  1.00 49.62  ? 123 LEU A CD2 1 
ATOM   792  N N   . LEU A 1 124 ? -4.761  -9.756  34.445  1.00 53.50  ? 124 LEU A N   1 
ATOM   793  C CA  . LEU A 1 124 ? -4.478  -8.339  34.243  1.00 57.32  ? 124 LEU A CA  1 
ATOM   794  C C   . LEU A 1 124 ? -5.692  -7.495  34.620  1.00 64.72  ? 124 LEU A C   1 
ATOM   795  O O   . LEU A 1 124 ? -6.839  -7.912  34.448  1.00 65.86  ? 124 LEU A O   1 
ATOM   796  C CB  . LEU A 1 124 ? -4.085  -8.080  32.786  1.00 53.04  ? 124 LEU A CB  1 
ATOM   797  C CG  . LEU A 1 124 ? -2.867  -8.876  32.305  1.00 60.40  ? 124 LEU A CG  1 
ATOM   798  C CD1 . LEU A 1 124 ? -2.518  -8.491  30.873  1.00 58.81  ? 124 LEU A CD1 1 
ATOM   799  C CD2 . LEU A 1 124 ? -1.682  -8.645  33.227  1.00 46.98  ? 124 LEU A CD2 1 
ATOM   800  N N   . GLU A 1 125 ? -5.434  -6.297  35.146  1.00 70.18  ? 125 GLU A N   1 
ATOM   801  C CA  . GLU A 1 125 ? -6.521  -5.435  35.590  1.00 69.12  ? 125 GLU A CA  1 
ATOM   802  C C   . GLU A 1 125 ? -7.358  -4.903  34.433  1.00 73.06  ? 125 GLU A C   1 
ATOM   803  O O   . GLU A 1 125 ? -6.906  -4.781  33.293  1.00 74.67  ? 125 GLU A O   1 
ATOM   804  C CB  . GLU A 1 125 ? -6.003  -4.251  36.394  1.00 77.50  ? 125 GLU A CB  1 
ATOM   805  C CG  . GLU A 1 125 ? -6.097  -4.440  37.881  1.00 86.51  ? 125 GLU A CG  1 
ATOM   806  C CD  . GLU A 1 125 ? -5.456  -3.296  38.627  1.00 87.95  ? 125 GLU A CD  1 
ATOM   807  O OE1 . GLU A 1 125 ? -5.879  -2.136  38.421  1.00 84.54  ? 125 GLU A OE1 1 
ATOM   808  O OE2 . GLU A 1 125 ? -4.565  -3.556  39.455  1.00 84.47  ? 125 GLU A OE2 1 
ATOM   809  N N   . VAL A 1 126 ? -8.604  -4.557  34.773  1.00 87.34  ? 126 VAL A N   1 
ATOM   810  C CA  . VAL A 1 126 ? -9.574  -4.089  33.793  1.00 91.21  ? 126 VAL A CA  1 
ATOM   811  C C   . VAL A 1 126 ? -9.057  -2.835  33.084  1.00 89.80  ? 126 VAL A C   1 
ATOM   812  O O   . VAL A 1 126 ? -8.242  -2.075  33.625  1.00 92.48  ? 126 VAL A O   1 
ATOM   813  C CB  . VAL A 1 126 ? -10.922 -3.834  34.491  1.00 92.96  ? 126 VAL A CB  1 
ATOM   814  C CG1 . VAL A 1 126 ? -11.348 -5.068  35.283  1.00 86.07  ? 126 VAL A CG1 1 
ATOM   815  C CG2 . VAL A 1 126 ? -10.822 -2.645  35.437  1.00 100.96 ? 126 VAL A CG2 1 
ATOM   816  N N   . LEU A 1 127 ? -9.523  -2.629  31.852  1.00 87.48  ? 127 LEU A N   1 
ATOM   817  C CA  . LEU A 1 127 ? -9.101  -1.478  31.049  1.00 93.88  ? 127 LEU A CA  1 
ATOM   818  C C   . LEU A 1 127 ? -9.924  -1.346  29.770  1.00 97.39  ? 127 LEU A C   1 
ATOM   819  O O   . LEU A 1 127 ? -11.082 -0.927  29.804  1.00 88.13  ? 127 LEU A O   1 
ATOM   820  C CB  . LEU A 1 127 ? -7.617  -1.584  30.703  1.00 70.22  ? 127 LEU A CB  1 
ATOM   821  C CG  . LEU A 1 127 ? -6.770  -0.430  31.238  1.00 84.36  ? 127 LEU A CG  1 
ATOM   822  C CD1 . LEU A 1 127 ? -5.350  -0.540  30.739  1.00 58.68  ? 127 LEU A CD1 1 
ATOM   823  C CD2 . LEU A 1 127 ? -7.392  0.911   30.826  1.00 73.90  ? 127 LEU A CD2 1 
ATOM   824  N N   . VAL B 1 30  ? 22.351  5.029   29.049  1.00 95.34  ? 30  VAL B N   1 
ATOM   825  C CA  . VAL B 1 30  ? 21.094  5.762   29.030  1.00 93.07  ? 30  VAL B CA  1 
ATOM   826  C C   . VAL B 1 30  ? 20.918  6.475   27.683  1.00 91.68  ? 30  VAL B C   1 
ATOM   827  O O   . VAL B 1 30  ? 19.816  6.516   27.138  1.00 89.20  ? 30  VAL B O   1 
ATOM   828  C CB  . VAL B 1 30  ? 21.005  6.777   30.218  1.00 96.39  ? 30  VAL B CB  1 
ATOM   829  C CG1 . VAL B 1 30  ? 20.702  6.065   31.534  1.00 97.49  ? 30  VAL B CG1 1 
ATOM   830  C CG2 . VAL B 1 30  ? 22.281  7.603   30.348  1.00 91.67  ? 30  VAL B CG2 1 
ATOM   831  N N   . SER B 1 31  ? 22.017  6.996   27.137  1.00 89.60  ? 31  SER B N   1 
ATOM   832  C CA  . SER B 1 31  ? 21.959  8.024   26.102  1.00 82.78  ? 31  SER B CA  1 
ATOM   833  C C   . SER B 1 31  ? 21.447  7.482   24.768  1.00 80.47  ? 31  SER B C   1 
ATOM   834  O O   . SER B 1 31  ? 21.569  6.295   24.449  1.00 79.10  ? 31  SER B O   1 
ATOM   835  C CB  . SER B 1 31  ? 23.339  8.647   25.891  1.00 78.30  ? 31  SER B CB  1 
ATOM   836  O OG  . SER B 1 31  ? 23.395  9.311   24.638  1.00 74.13  ? 31  SER B OG  1 
ATOM   837  N N   . LYS B 1 32  ? 20.898  8.398   23.962  1.00 71.94  ? 32  LYS B N   1 
ATOM   838  C CA  . LYS B 1 32  ? 20.373  8.045   22.646  1.00 62.28  ? 32  LYS B CA  1 
ATOM   839  C C   . LYS B 1 32  ? 21.480  7.821   21.622  1.00 66.52  ? 32  LYS B C   1 
ATOM   840  O O   . LYS B 1 32  ? 21.379  6.914   20.788  1.00 52.31  ? 32  LYS B O   1 
ATOM   841  C CB  . LYS B 1 32  ? 19.431  9.132   22.148  1.00 53.28  ? 32  LYS B CB  1 
ATOM   842  C CG  . LYS B 1 32  ? 19.144  9.050   20.656  1.00 62.07  ? 32  LYS B CG  1 
ATOM   843  C CD  . LYS B 1 32  ? 18.708  10.414  20.124  1.00 72.34  ? 32  LYS B CD  1 
ATOM   844  C CE  . LYS B 1 32  ? 17.221  10.652  20.359  1.00 62.05  ? 32  LYS B CE  1 
ATOM   845  N NZ  . LYS B 1 32  ? 16.672  11.635  19.376  1.00 74.20  ? 32  LYS B NZ  1 
ATOM   846  N N   . SER B 1 33  ? 22.528  8.651   21.637  1.00 53.55  ? 33  SER B N   1 
ATOM   847  C CA  . SER B 1 33  ? 23.650  8.388   20.743  1.00 50.91  ? 33  SER B CA  1 
ATOM   848  C C   . SER B 1 33  ? 24.348  7.093   21.128  1.00 54.82  ? 33  SER B C   1 
ATOM   849  O O   . SER B 1 33  ? 24.771  6.325   20.258  1.00 58.97  ? 33  SER B O   1 
ATOM   850  C CB  . SER B 1 33  ? 24.628  9.562   20.752  1.00 51.04  ? 33  SER B CB  1 
ATOM   851  O OG  . SER B 1 33  ? 24.893  10.014  22.078  1.00 66.30  ? 33  SER B OG  1 
ATOM   852  N N   . THR B 1 34  ? 24.462  6.825   22.433  1.00 54.62  ? 34  THR B N   1 
ATOM   853  C CA  . THR B 1 34  ? 25.086  5.583   22.882  1.00 67.23  ? 34  THR B CA  1 
ATOM   854  C C   . THR B 1 34  ? 24.331  4.379   22.346  1.00 54.83  ? 34  THR B C   1 
ATOM   855  O O   . THR B 1 34  ? 24.935  3.453   21.795  1.00 53.99  ? 34  THR B O   1 
ATOM   856  C CB  . THR B 1 34  ? 25.155  5.537   24.413  1.00 73.07  ? 34  THR B CB  1 
ATOM   857  O OG1 . THR B 1 34  ? 26.121  6.489   24.879  1.00 74.66  ? 34  THR B OG1 1 
ATOM   858  C CG2 . THR B 1 34  ? 25.554  4.140   24.898  1.00 59.90  ? 34  THR B CG2 1 
ATOM   859  N N   . GLN B 1 35  ? 22.997  4.389   22.465  1.00 48.53  ? 35  GLN B N   1 
ATOM   860  C CA  . GLN B 1 35  ? 22.217  3.278   21.925  1.00 53.07  ? 35  GLN B CA  1 
ATOM   861  C C   . GLN B 1 35  ? 22.395  3.160   20.419  1.00 48.03  ? 35  GLN B C   1 
ATOM   862  O O   . GLN B 1 35  ? 22.579  2.055   19.895  1.00 49.58  ? 35  GLN B O   1 
ATOM   863  C CB  . GLN B 1 35  ? 20.737  3.440   22.270  1.00 50.30  ? 35  GLN B CB  1 
ATOM   864  C CG  . GLN B 1 35  ? 20.425  3.358   23.752  1.00 61.05  ? 35  GLN B CG  1 
ATOM   865  C CD  . GLN B 1 35  ? 18.967  3.048   23.993  1.00 71.80  ? 35  GLN B CD  1 
ATOM   866  O OE1 . GLN B 1 35  ? 18.563  1.882   24.059  1.00 80.05  ? 35  GLN B OE1 1 
ATOM   867  N NE2 . GLN B 1 35  ? 18.158  4.090   24.084  1.00 76.10  ? 35  GLN B NE2 1 
ATOM   868  N N   . PHE B 1 36  ? 22.344  4.282   19.696  1.00 49.64  ? 36  PHE B N   1 
ATOM   869  C CA  . PHE B 1 36  ? 22.458  4.161   18.248  1.00 53.59  ? 36  PHE B CA  1 
ATOM   870  C C   . PHE B 1 36  ? 23.851  3.684   17.842  1.00 50.03  ? 36  PHE B C   1 
ATOM   871  O O   . PHE B 1 36  ? 23.989  2.862   16.926  1.00 50.68  ? 36  PHE B O   1 
ATOM   872  C CB  . PHE B 1 36  ? 22.135  5.476   17.542  1.00 42.52  ? 36  PHE B CB  1 
ATOM   873  C CG  . PHE B 1 36  ? 22.422  5.416   16.072  1.00 57.17  ? 36  PHE B CG  1 
ATOM   874  C CD1 . PHE B 1 36  ? 21.543  4.775   15.219  1.00 50.91  ? 36  PHE B CD1 1 
ATOM   875  C CD2 . PHE B 1 36  ? 23.627  5.890   15.562  1.00 53.62  ? 36  PHE B CD2 1 
ATOM   876  C CE1 . PHE B 1 36  ? 21.824  4.663   13.865  1.00 55.76  ? 36  PHE B CE1 1 
ATOM   877  C CE2 . PHE B 1 36  ? 23.921  5.782   14.210  1.00 55.90  ? 36  PHE B CE2 1 
ATOM   878  C CZ  . PHE B 1 36  ? 23.010  5.165   13.361  1.00 55.46  ? 36  PHE B CZ  1 
ATOM   879  N N   . GLU B 1 37  ? 24.895  4.189   18.499  1.00 47.19  ? 37  GLU B N   1 
ATOM   880  C CA  . GLU B 1 37  ? 26.247  3.762   18.145  1.00 49.21  ? 37  GLU B CA  1 
ATOM   881  C C   . GLU B 1 37  ? 26.444  2.295   18.479  1.00 60.73  ? 37  GLU B C   1 
ATOM   882  O O   . GLU B 1 37  ? 27.003  1.537   17.679  1.00 54.49  ? 37  GLU B O   1 
ATOM   883  C CB  . GLU B 1 37  ? 27.288  4.606   18.873  1.00 57.00  ? 37  GLU B CB  1 
ATOM   884  C CG  . GLU B 1 37  ? 27.391  6.070   18.416  1.00 80.88  ? 37  GLU B CG  1 
ATOM   885  C CD  . GLU B 1 37  ? 27.773  6.240   16.949  1.00 64.61  ? 37  GLU B CD  1 
ATOM   886  O OE1 . GLU B 1 37  ? 28.443  5.352   16.389  1.00 66.83  ? 37  GLU B OE1 1 
ATOM   887  O OE2 . GLU B 1 37  ? 27.413  7.281   16.362  1.00 71.03  ? 37  GLU B OE2 1 
ATOM   888  N N   . GLU B 1 38  ? 25.971  1.875   19.652  1.00 53.67  ? 38  GLU B N   1 
ATOM   889  C CA  . GLU B 1 38  ? 25.992  0.459   19.987  1.00 53.05  ? 38  GLU B CA  1 
ATOM   890  C C   . GLU B 1 38  ? 25.241  -0.359  18.944  1.00 55.96  ? 38  GLU B C   1 
ATOM   891  O O   . GLU B 1 38  ? 25.729  -1.398  18.484  1.00 53.00  ? 38  GLU B O   1 
ATOM   892  C CB  . GLU B 1 38  ? 25.391  0.246   21.374  1.00 62.07  ? 38  GLU B CB  1 
ATOM   893  C CG  . GLU B 1 38  ? 25.413  -1.201  21.819  1.00 75.33  ? 38  GLU B CG  1 
ATOM   894  C CD  . GLU B 1 38  ? 25.004  -1.370  23.275  1.00 93.92  ? 38  GLU B CD  1 
ATOM   895  O OE1 . GLU B 1 38  ? 25.000  -0.359  24.021  1.00 93.36  ? 38  GLU B OE1 1 
ATOM   896  O OE2 . GLU B 1 38  ? 24.700  -2.516  23.672  1.00 81.43  ? 38  GLU B OE2 1 
ATOM   897  N N   . ALA B 1 39  ? 24.047  0.092   18.553  1.00 55.05  ? 39  ALA B N   1 
ATOM   898  C CA  . ALA B 1 39  ? 23.262  -0.686  17.596  1.00 54.04  ? 39  ALA B CA  1 
ATOM   899  C C   . ALA B 1 39  ? 23.926  -0.721  16.219  1.00 48.65  ? 39  ALA B C   1 
ATOM   900  O O   . ALA B 1 39  ? 23.873  -1.738  15.525  1.00 41.70  ? 39  ALA B O   1 
ATOM   901  C CB  . ALA B 1 39  ? 21.852  -0.125  17.498  1.00 47.21  ? 39  ALA B CB  1 
ATOM   902  N N   . TRP B 1 40  ? 24.544  0.381   15.805  1.00 43.18  ? 40  TRP B N   1 
ATOM   903  C CA  . TRP B 1 40  ? 25.289  0.401   14.545  1.00 45.92  ? 40  TRP B CA  1 
ATOM   904  C C   . TRP B 1 40  ? 26.356  -0.689  14.501  1.00 49.13  ? 40  TRP B C   1 
ATOM   905  O O   . TRP B 1 40  ? 26.577  -1.317  13.456  1.00 45.18  ? 40  TRP B O   1 
ATOM   906  C CB  . TRP B 1 40  ? 25.929  1.777   14.350  1.00 52.96  ? 40  TRP B CB  1 
ATOM   907  C CG  . TRP B 1 40  ? 26.506  1.974   12.978  1.00 70.21  ? 40  TRP B CG  1 
ATOM   908  C CD1 . TRP B 1 40  ? 25.834  2.342   11.850  1.00 66.59  ? 40  TRP B CD1 1 
ATOM   909  C CD2 . TRP B 1 40  ? 27.874  1.810   12.595  1.00 63.90  ? 40  TRP B CD2 1 
ATOM   910  N NE1 . TRP B 1 40  ? 26.698  2.413   10.787  1.00 68.26  ? 40  TRP B NE1 1 
ATOM   911  C CE2 . TRP B 1 40  ? 27.959  2.091   11.218  1.00 69.75  ? 40  TRP B CE2 1 
ATOM   912  C CE3 . TRP B 1 40  ? 29.031  1.455   13.283  1.00 60.55  ? 40  TRP B CE3 1 
ATOM   913  C CZ2 . TRP B 1 40  ? 29.159  2.024   10.514  1.00 77.29  ? 40  TRP B CZ2 1 
ATOM   914  C CZ3 . TRP B 1 40  ? 30.229  1.389   12.581  1.00 82.69  ? 40  TRP B CZ3 1 
ATOM   915  C CH2 . TRP B 1 40  ? 30.282  1.672   11.210  1.00 82.41  ? 40  TRP B CH2 1 
ATOM   916  N N   . CYS B 1 41  ? 27.037  -0.923  15.624  1.00 51.69  ? 41  CYS B N   1 
ATOM   917  C CA  . CYS B 1 41  ? 28.068  -1.960  15.656  1.00 51.06  ? 41  CYS B CA  1 
ATOM   918  C C   . CYS B 1 41  ? 27.443  -3.348  15.614  1.00 57.63  ? 41  CYS B C   1 
ATOM   919  O O   . CYS B 1 41  ? 27.918  -4.235  14.893  1.00 52.89  ? 41  CYS B O   1 
ATOM   920  C CB  . CYS B 1 41  ? 28.928  -1.804  16.905  1.00 61.19  ? 41  CYS B CB  1 
ATOM   921  S SG  . CYS B 1 41  ? 29.864  -0.254  16.987  1.00 58.83  ? 41  CYS B SG  1 
ATOM   922  N N   . LEU B 1 42  ? 26.360  -3.546  16.364  1.00 47.19  ? 42  LEU B N   1 
ATOM   923  C CA  . LEU B 1 42  ? 25.745  -4.865  16.459  1.00 52.27  ? 42  LEU B CA  1 
ATOM   924  C C   . LEU B 1 42  ? 25.123  -5.288  15.131  1.00 48.79  ? 42  LEU B C   1 
ATOM   925  O O   . LEU B 1 42  ? 25.154  -6.470  14.761  1.00 50.16  ? 42  LEU B O   1 
ATOM   926  C CB  . LEU B 1 42  ? 24.688  -4.848  17.560  1.00 48.85  ? 42  LEU B CB  1 
ATOM   927  C CG  . LEU B 1 42  ? 25.188  -4.686  18.989  1.00 49.89  ? 42  LEU B CG  1 
ATOM   928  C CD1 . LEU B 1 42  ? 23.983  -4.491  19.904  1.00 60.97  ? 42  LEU B CD1 1 
ATOM   929  C CD2 . LEU B 1 42  ? 25.976  -5.883  19.435  1.00 50.68  ? 42  LEU B CD2 1 
ATOM   930  N N   . VAL B 1 43  ? 24.539  -4.340  14.403  1.00 42.95  ? 43  VAL B N   1 
ATOM   931  C CA  . VAL B 1 43  ? 23.886  -4.687  13.145  1.00 59.67  ? 43  VAL B CA  1 
ATOM   932  C C   . VAL B 1 43  ? 24.910  -5.045  12.075  1.00 62.79  ? 43  VAL B C   1 
ATOM   933  O O   . VAL B 1 43  ? 24.597  -5.786  11.131  1.00 57.27  ? 43  VAL B O   1 
ATOM   934  C CB  . VAL B 1 43  ? 22.965  -3.525  12.733  1.00 60.53  ? 43  VAL B CB  1 
ATOM   935  C CG1 . VAL B 1 43  ? 23.050  -3.226  11.249  1.00 56.81  ? 43  VAL B CG1 1 
ATOM   936  C CG2 . VAL B 1 43  ? 21.542  -3.837  13.139  1.00 43.21  ? 43  VAL B CG2 1 
ATOM   937  N N   . ARG B 1 44  ? 26.137  -4.563  12.233  1.00 53.32  ? 44  ARG B N   1 
ATOM   938  C CA  . ARG B 1 44  ? 27.274  -4.825  11.361  1.00 50.90  ? 44  ARG B CA  1 
ATOM   939  C C   . ARG B 1 44  ? 28.009  -6.102  11.736  1.00 59.51  ? 44  ARG B C   1 
ATOM   940  O O   . ARG B 1 44  ? 29.040  -6.423  11.130  1.00 62.69  ? 44  ARG B O   1 
ATOM   941  C CB  . ARG B 1 44  ? 28.233  -3.626  11.435  1.00 60.09  ? 44  ARG B CB  1 
ATOM   942  C CG  . ARG B 1 44  ? 29.208  -3.458  10.294  1.00 82.73  ? 44  ARG B CG  1 
ATOM   943  C CD  . ARG B 1 44  ? 30.395  -2.642  10.778  1.00 94.12  ? 44  ARG B CD  1 
ATOM   944  N NE  . ARG B 1 44  ? 31.338  -2.265  9.730   1.00 86.92  ? 44  ARG B NE  1 
ATOM   945  C CZ  . ARG B 1 44  ? 31.071  -1.411  8.750   1.00 93.26  ? 44  ARG B CZ  1 
ATOM   946  N NH1 . ARG B 1 44  ? 29.872  -0.862  8.614   1.00 78.69  ? 44  ARG B NH1 1 
ATOM   947  N NH2 . ARG B 1 44  ? 32.032  -1.102  7.881   1.00 97.18  ? 44  ARG B NH2 1 
ATOM   948  N N   . SER B 1 45  ? 27.513  -6.840  12.714  1.00 55.33  ? 45  SER B N   1 
ATOM   949  C CA  . SER B 1 45  ? 28.301  -7.898  13.318  1.00 57.38  ? 45  SER B CA  1 
ATOM   950  C C   . SER B 1 45  ? 28.189  -9.201  12.541  1.00 65.71  ? 45  SER B C   1 
ATOM   951  O O   . SER B 1 45  ? 27.193  -9.464  11.863  1.00 65.62  ? 45  SER B O   1 
ATOM   952  C CB  . SER B 1 45  ? 27.868  -8.123  14.762  1.00 55.87  ? 45  SER B CB  1 
ATOM   953  O OG  . SER B 1 45  ? 28.229  -9.420  15.189  1.00 57.56  ? 45  SER B OG  1 
ATOM   954  N N   . LYS B 1 46  ? 29.239  -10.023 12.667  1.00 74.06  ? 46  LYS B N   1 
ATOM   955  C CA  . LYS B 1 46  ? 29.279  -11.351 12.058  1.00 62.93  ? 46  LYS B CA  1 
ATOM   956  C C   . LYS B 1 46  ? 28.299  -12.306 12.734  1.00 63.88  ? 46  LYS B C   1 
ATOM   957  O O   . LYS B 1 46  ? 27.785  -13.228 12.089  1.00 71.95  ? 46  LYS B O   1 
ATOM   958  C CB  . LYS B 1 46  ? 30.731  -11.865 12.108  1.00 65.99  ? 46  LYS B CB  1 
ATOM   959  C CG  . LYS B 1 46  ? 30.982  -13.347 12.444  1.00 80.22  ? 46  LYS B CG  1 
ATOM   960  C CD  . LYS B 1 46  ? 30.329  -14.351 11.502  1.00 92.87  ? 46  LYS B CD  1 
ATOM   961  C CE  . LYS B 1 46  ? 31.006  -15.707 11.531  1.00 97.12  ? 46  LYS B CE  1 
ATOM   962  N NZ  . LYS B 1 46  ? 30.698  -16.447 10.278  1.00 88.96  ? 46  LYS B NZ  1 
ATOM   963  N N   . TYR B 1 47  ? 27.995  -12.097 14.008  1.00 65.35  ? 47  TYR B N   1 
ATOM   964  C CA  . TYR B 1 47  ? 27.206  -13.061 14.765  1.00 64.39  ? 47  TYR B CA  1 
ATOM   965  C C   . TYR B 1 47  ? 25.729  -12.680 14.771  1.00 67.73  ? 47  TYR B C   1 
ATOM   966  O O   . TYR B 1 47  ? 25.375  -11.522 15.016  1.00 64.12  ? 47  TYR B O   1 
ATOM   967  C CB  . TYR B 1 47  ? 27.748  -13.169 16.187  1.00 72.84  ? 47  TYR B CB  1 
ATOM   968  C CG  . TYR B 1 47  ? 29.237  -13.435 16.213  1.00 69.29  ? 47  TYR B CG  1 
ATOM   969  C CD1 . TYR B 1 47  ? 30.152  -12.388 16.292  1.00 71.59  ? 47  TYR B CD1 1 
ATOM   970  C CD2 . TYR B 1 47  ? 29.730  -14.728 16.137  1.00 69.94  ? 47  TYR B CD2 1 
ATOM   971  C CE1 . TYR B 1 47  ? 31.523  -12.624 16.309  1.00 69.71  ? 47  TYR B CE1 1 
ATOM   972  C CE2 . TYR B 1 47  ? 31.106  -14.976 16.154  1.00 79.14  ? 47  TYR B CE2 1 
ATOM   973  C CZ  . TYR B 1 47  ? 31.996  -13.916 16.241  1.00 73.76  ? 47  TYR B CZ  1 
ATOM   974  O OH  . TYR B 1 47  ? 33.360  -14.146 16.255  1.00 89.09  ? 47  TYR B OH  1 
ATOM   975  N N   . ASN B 1 48  ? 24.872  -13.670 14.511  1.00 62.76  ? 48  ASN B N   1 
ATOM   976  C CA  . ASN B 1 48  ? 23.439  -13.417 14.417  1.00 69.62  ? 48  ASN B CA  1 
ATOM   977  C C   . ASN B 1 48  ? 22.849  -12.930 15.732  1.00 76.85  ? 48  ASN B C   1 
ATOM   978  O O   . ASN B 1 48  ? 21.902  -12.138 15.717  1.00 64.02  ? 48  ASN B O   1 
ATOM   979  C CB  . ASN B 1 48  ? 22.715  -14.676 13.944  1.00 70.44  ? 48  ASN B CB  1 
ATOM   980  C CG  . ASN B 1 48  ? 22.736  -14.820 12.433  1.00 85.07  ? 48  ASN B CG  1 
ATOM   981  O OD1 . ASN B 1 48  ? 23.701  -14.423 11.770  1.00 73.30  ? 48  ASN B OD1 1 
ATOM   982  N ND2 . ASN B 1 48  ? 21.662  -15.377 11.877  1.00 82.17  ? 48  ASN B ND2 1 
ATOM   983  N N   . ASP B 1 49  ? 23.383  -13.391 16.870  1.00 72.24  ? 49  ASP B N   1 
ATOM   984  C CA  . ASP B 1 49  ? 22.905  -12.905 18.164  1.00 70.62  ? 49  ASP B CA  1 
ATOM   985  C C   . ASP B 1 49  ? 23.132  -11.412 18.304  1.00 64.52  ? 49  ASP B C   1 
ATOM   986  O O   . ASP B 1 49  ? 22.283  -10.694 18.844  1.00 62.91  ? 49  ASP B O   1 
ATOM   987  C CB  . ASP B 1 49  ? 23.606  -13.638 19.305  1.00 77.56  ? 49  ASP B CB  1 
ATOM   988  C CG  . ASP B 1 49  ? 22.926  -14.931 19.657  1.00 88.02  ? 49  ASP B CG  1 
ATOM   989  O OD1 . ASP B 1 49  ? 23.168  -15.927 18.943  1.00 94.29  ? 49  ASP B OD1 1 
ATOM   990  O OD2 . ASP B 1 49  ? 22.146  -14.951 20.633  1.00 91.72  ? 49  ASP B OD2 1 
ATOM   991  N N   . ASP B 1 50  ? 24.278  -10.928 17.830  1.00 58.29  ? 50  ASP B N   1 
ATOM   992  C CA  . ASP B 1 50  ? 24.541  -9.496  17.871  1.00 53.93  ? 50  ASP B CA  1 
ATOM   993  C C   . ASP B 1 50  ? 23.584  -8.738  16.966  1.00 55.94  ? 50  ASP B C   1 
ATOM   994  O O   . ASP B 1 50  ? 23.098  -7.666  17.335  1.00 55.62  ? 50  ASP B O   1 
ATOM   995  C CB  . ASP B 1 50  ? 25.980  -9.226  17.463  1.00 52.63  ? 50  ASP B CB  1 
ATOM   996  C CG  . ASP B 1 50  ? 26.931  -9.300  18.626  1.00 77.31  ? 50  ASP B CG  1 
ATOM   997  O OD1 . ASP B 1 50  ? 28.044  -8.719  18.522  1.00 62.69  ? 50  ASP B OD1 1 
ATOM   998  O OD2 . ASP B 1 50  ? 26.545  -9.910  19.656  1.00 79.31  ? 50  ASP B OD2 1 
ATOM   999  N N   . ILE B 1 51  ? 23.294  -9.273  15.777  1.00 53.25  ? 51  ILE B N   1 
ATOM   1000 C CA  . ILE B 1 51  ? 22.370  -8.582  14.878  1.00 56.09  ? 51  ILE B CA  1 
ATOM   1001 C C   . ILE B 1 51  ? 20.988  -8.477  15.509  1.00 58.43  ? 51  ILE B C   1 
ATOM   1002 O O   . ILE B 1 51  ? 20.353  -7.416  15.451  1.00 49.44  ? 51  ILE B O   1 
ATOM   1003 C CB  . ILE B 1 51  ? 22.310  -9.266  13.502  1.00 56.91  ? 51  ILE B CB  1 
ATOM   1004 C CG1 . ILE B 1 51  ? 23.718  -9.380  12.900  1.00 53.11  ? 51  ILE B CG1 1 
ATOM   1005 C CG2 . ILE B 1 51  ? 21.399  -8.467  12.563  1.00 45.40  ? 51  ILE B CG2 1 
ATOM   1006 C CD1 . ILE B 1 51  ? 23.790  -10.270 11.685  1.00 52.55  ? 51  ILE B CD1 1 
ATOM   1007 N N   . ARG B 1 52  ? 20.505  -9.568  16.127  1.00 47.18  ? 52  ARG B N   1 
ATOM   1008 C CA  . ARG B 1 52  ? 19.202  -9.527  16.787  1.00 53.04  ? 52  ARG B CA  1 
ATOM   1009 C C   . ARG B 1 52  ? 19.163  -8.437  17.847  1.00 53.06  ? 52  ARG B C   1 
ATOM   1010 O O   . ARG B 1 52  ? 18.182  -7.695  17.957  1.00 51.15  ? 52  ARG B O   1 
ATOM   1011 C CB  . ARG B 1 52  ? 18.863  -10.874 17.439  1.00 51.03  ? 52  ARG B CB  1 
ATOM   1012 C CG  . ARG B 1 52  ? 19.030  -12.079 16.549  1.00 70.81  ? 52  ARG B CG  1 
ATOM   1013 C CD  . ARG B 1 52  ? 17.994  -13.170 16.818  1.00 74.18  ? 52  ARG B CD  1 
ATOM   1014 N NE  . ARG B 1 52  ? 17.970  -14.100 15.695  1.00 87.13  ? 52  ARG B NE  1 
ATOM   1015 C CZ  . ARG B 1 52  ? 18.855  -15.069 15.512  1.00 86.99  ? 52  ARG B CZ  1 
ATOM   1016 N NH1 . ARG B 1 52  ? 19.803  -15.317 16.402  1.00 101.41 ? 52  ARG B NH1 1 
ATOM   1017 N NH2 . ARG B 1 52  ? 18.791  -15.806 14.405  1.00 92.79  ? 52  ARG B NH2 1 
ATOM   1018 N N   . LYS B 1 53  ? 20.210  -8.357  18.670  1.00 47.89  ? 53  LYS B N   1 
ATOM   1019 C CA  . LYS B 1 53  ? 20.233  -7.335  19.712  1.00 51.94  ? 53  LYS B CA  1 
ATOM   1020 C C   . LYS B 1 53  ? 20.288  -5.942  19.102  1.00 47.79  ? 53  LYS B C   1 
ATOM   1021 O O   . LYS B 1 53  ? 19.668  -5.007  19.620  1.00 47.96  ? 53  LYS B O   1 
ATOM   1022 C CB  . LYS B 1 53  ? 21.414  -7.556  20.657  1.00 45.97  ? 53  LYS B CB  1 
ATOM   1023 C CG  . LYS B 1 53  ? 21.284  -8.754  21.601  1.00 66.45  ? 53  LYS B CG  1 
ATOM   1024 C CD  . LYS B 1 53  ? 22.673  -9.196  22.088  1.00 69.18  ? 53  LYS B CD  1 
ATOM   1025 C CE  . LYS B 1 53  ? 22.607  -10.286 23.161  1.00 76.69  ? 53  LYS B CE  1 
ATOM   1026 N NZ  . LYS B 1 53  ? 21.992  -11.565 22.693  1.00 73.85  ? 53  LYS B NZ  1 
ATOM   1027 N N   . GLY B 1 54  ? 21.019  -5.784  17.991  1.00 41.69  ? 54  GLY B N   1 
ATOM   1028 C CA  . GLY B 1 54  ? 21.046  -4.499  17.316  1.00 43.07  ? 54  GLY B CA  1 
ATOM   1029 C C   . GLY B 1 54  ? 19.672  -4.071  16.837  1.00 51.66  ? 54  GLY B C   1 
ATOM   1030 O O   . GLY B 1 54  ? 19.296  -2.903  16.952  1.00 46.33  ? 54  GLY B O   1 
ATOM   1031 N N   . ILE B 1 55  ? 18.904  -5.012  16.298  1.00 46.39  ? 55  ILE B N   1 
ATOM   1032 C CA  . ILE B 1 55  ? 17.528  -4.714  15.900  1.00 41.77  ? 55  ILE B CA  1 
ATOM   1033 C C   . ILE B 1 55  ? 16.700  -4.306  17.110  1.00 42.58  ? 55  ILE B C   1 
ATOM   1034 O O   . ILE B 1 55  ? 15.863  -3.398  17.034  1.00 48.30  ? 55  ILE B O   1 
ATOM   1035 C CB  . ILE B 1 55  ? 16.920  -5.935  15.187  1.00 47.75  ? 55  ILE B CB  1 
ATOM   1036 C CG1 . ILE B 1 55  ? 17.510  -6.093  13.785  1.00 47.56  ? 55  ILE B CG1 1 
ATOM   1037 C CG2 . ILE B 1 55  ? 15.373  -5.865  15.175  1.00 51.94  ? 55  ILE B CG2 1 
ATOM   1038 C CD1 . ILE B 1 55  ? 17.439  -7.576  13.268  1.00 45.71  ? 55  ILE B CD1 1 
ATOM   1039 N N   . VAL B 1 56  ? 16.909  -4.975  18.243  1.00 44.79  ? 56  VAL B N   1 
ATOM   1040 C CA  . VAL B 1 56  ? 16.097  -4.674  19.422  1.00 48.83  ? 56  VAL B CA  1 
ATOM   1041 C C   . VAL B 1 56  ? 16.359  -3.245  19.878  1.00 56.88  ? 56  VAL B C   1 
ATOM   1042 O O   . VAL B 1 56  ? 15.427  -2.508  20.208  1.00 52.64  ? 56  VAL B O   1 
ATOM   1043 C CB  . VAL B 1 56  ? 16.366  -5.710  20.530  1.00 45.46  ? 56  VAL B CB  1 
ATOM   1044 C CG1 . VAL B 1 56  ? 15.974  -5.196  21.910  1.00 49.05  ? 56  VAL B CG1 1 
ATOM   1045 C CG2 . VAL B 1 56  ? 15.629  -7.022  20.221  1.00 60.41  ? 56  VAL B CG2 1 
ATOM   1046 N N   . LEU B 1 57  ? 17.622  -2.807  19.832  1.00 41.44  ? 57  LEU B N   1 
ATOM   1047 C CA  . LEU B 1 57  ? 17.939  -1.415  20.142  1.00 39.93  ? 57  LEU B CA  1 
ATOM   1048 C C   . LEU B 1 57  ? 17.285  -0.466  19.154  1.00 45.03  ? 57  LEU B C   1 
ATOM   1049 O O   . LEU B 1 57  ? 16.697  0.545   19.551  1.00 46.95  ? 57  LEU B O   1 
ATOM   1050 C CB  . LEU B 1 57  ? 19.452  -1.218  20.146  1.00 44.01  ? 57  LEU B CB  1 
ATOM   1051 C CG  . LEU B 1 57  ? 20.135  -1.740  21.400  1.00 54.12  ? 57  LEU B CG  1 
ATOM   1052 C CD1 . LEU B 1 57  ? 21.641  -1.639  21.252  1.00 55.99  ? 57  LEU B CD1 1 
ATOM   1053 C CD2 . LEU B 1 57  ? 19.645  -0.903  22.568  1.00 50.57  ? 57  LEU B CD2 1 
ATOM   1054 N N   . LEU B 1 58  ? 17.393  -0.764  17.853  1.00 40.42  ? 58  LEU B N   1 
ATOM   1055 C CA  . LEU B 1 58  ? 16.827  0.120   16.833  1.00 42.28  ? 58  LEU B CA  1 
ATOM   1056 C C   . LEU B 1 58  ? 15.311  0.232   16.965  1.00 43.05  ? 58  LEU B C   1 
ATOM   1057 O O   . LEU B 1 58  ? 14.737  1.306   16.735  1.00 41.88  ? 58  LEU B O   1 
ATOM   1058 C CB  . LEU B 1 58  ? 17.197  -0.392  15.438  1.00 37.50  ? 58  LEU B CB  1 
ATOM   1059 C CG  . LEU B 1 58  ? 18.663  -0.202  15.047  1.00 44.89  ? 58  LEU B CG  1 
ATOM   1060 C CD1 . LEU B 1 58  ? 18.974  -0.939  13.733  1.00 37.90  ? 58  LEU B CD1 1 
ATOM   1061 C CD2 . LEU B 1 58  ? 19.018  1.276   14.941  1.00 39.09  ? 58  LEU B CD2 1 
ATOM   1062 N N   . GLU B 1 59  ? 14.640  -0.875  17.306  1.00 43.94  ? 59  GLU B N   1 
ATOM   1063 C CA  . GLU B 1 59  ? 13.192  -0.830  17.470  1.00 44.84  ? 59  GLU B CA  1 
ATOM   1064 C C   . GLU B 1 59  ? 12.816  0.083   18.629  1.00 53.43  ? 59  GLU B C   1 
ATOM   1065 O O   . GLU B 1 59  ? 11.864  0.859   18.535  1.00 58.89  ? 59  GLU B O   1 
ATOM   1066 C CB  . GLU B 1 59  ? 12.641  -2.248  17.692  1.00 43.98  ? 59  GLU B CB  1 
ATOM   1067 C CG  . GLU B 1 59  ? 12.378  -3.005  16.396  1.00 50.65  ? 59  GLU B CG  1 
ATOM   1068 C CD  . GLU B 1 59  ? 12.033  -4.476  16.618  1.00 77.73  ? 59  GLU B CD  1 
ATOM   1069 O OE1 . GLU B 1 59  ? 11.664  -5.152  15.631  1.00 74.94  ? 59  GLU B OE1 1 
ATOM   1070 O OE2 . GLU B 1 59  ? 12.139  -4.963  17.772  1.00 80.40  ? 59  GLU B OE2 1 
ATOM   1071 N N   . GLU B 1 60  ? 13.572  0.022   19.726  1.00 48.15  ? 60  GLU B N   1 
ATOM   1072 C CA  . GLU B 1 60  ? 13.293  0.905   20.853  1.00 57.90  ? 60  GLU B CA  1 
ATOM   1073 C C   . GLU B 1 60  ? 13.636  2.359   20.530  1.00 50.84  ? 60  GLU B C   1 
ATOM   1074 O O   . GLU B 1 60  ? 12.921  3.273   20.957  1.00 46.32  ? 60  GLU B O   1 
ATOM   1075 C CB  . GLU B 1 60  ? 14.055  0.436   22.089  1.00 58.46  ? 60  GLU B CB  1 
ATOM   1076 C CG  . GLU B 1 60  ? 13.992  1.445   23.235  1.00 65.46  ? 60  GLU B CG  1 
ATOM   1077 C CD  . GLU B 1 60  ? 14.722  0.977   24.489  1.00 74.54  ? 60  GLU B CD  1 
ATOM   1078 O OE1 . GLU B 1 60  ? 14.308  1.406   25.595  1.00 85.53  ? 60  GLU B OE1 1 
ATOM   1079 O OE2 . GLU B 1 60  ? 15.699  0.201   24.369  1.00 68.36  ? 60  GLU B OE2 1 
ATOM   1080 N N   . LEU B 1 61  ? 14.720  2.601   19.772  1.00 43.61  ? 61  LEU B N   1 
ATOM   1081 C CA  . LEU B 1 61  ? 15.075  3.976   19.413  1.00 44.14  ? 61  LEU B CA  1 
ATOM   1082 C C   . LEU B 1 61  ? 14.042  4.618   18.498  1.00 43.78  ? 61  LEU B C   1 
ATOM   1083 O O   . LEU B 1 61  ? 13.842  5.835   18.555  1.00 47.29  ? 61  LEU B O   1 
ATOM   1084 C CB  . LEU B 1 61  ? 16.430  4.035   18.715  1.00 46.55  ? 61  LEU B CB  1 
ATOM   1085 C CG  . LEU B 1 61  ? 17.675  3.589   19.468  1.00 56.29  ? 61  LEU B CG  1 
ATOM   1086 C CD1 . LEU B 1 61  ? 18.823  3.498   18.493  1.00 54.72  ? 61  LEU B CD1 1 
ATOM   1087 C CD2 . LEU B 1 61  ? 17.979  4.595   20.541  1.00 57.23  ? 61  LEU B CD2 1 
ATOM   1088 N N   . LEU B 1 62  ? 13.405  3.822   17.643  1.00 44.95  ? 62  LEU B N   1 
ATOM   1089 C CA  . LEU B 1 62  ? 12.529  4.315   16.578  1.00 51.26  ? 62  LEU B CA  1 
ATOM   1090 C C   . LEU B 1 62  ? 11.445  5.269   17.051  1.00 45.79  ? 62  LEU B C   1 
ATOM   1091 O O   . LEU B 1 62  ? 11.295  6.340   16.443  1.00 51.21  ? 62  LEU B O   1 
ATOM   1092 C CB  . LEU B 1 62  ? 11.918  3.108   15.847  1.00 42.07  ? 62  LEU B CB  1 
ATOM   1093 C CG  . LEU B 1 62  ? 11.047  3.309   14.607  1.00 59.55  ? 62  LEU B CG  1 
ATOM   1094 C CD1 . LEU B 1 62  ? 11.796  4.074   13.542  1.00 46.17  ? 62  LEU B CD1 1 
ATOM   1095 C CD2 . LEU B 1 62  ? 10.581  1.961   14.064  1.00 59.62  ? 62  LEU B CD2 1 
ATOM   1096 N N   . PRO B 1 63  ? 10.660  4.966   18.087  1.00 48.31  ? 63  PRO B N   1 
ATOM   1097 C CA  . PRO B 1 63  ? 9.646   5.931   18.529  1.00 51.80  ? 63  PRO B CA  1 
ATOM   1098 C C   . PRO B 1 63  ? 10.238  7.165   19.173  1.00 56.00  ? 63  PRO B C   1 
ATOM   1099 O O   . PRO B 1 63  ? 9.506   8.125   19.433  1.00 59.46  ? 63  PRO B O   1 
ATOM   1100 C CB  . PRO B 1 63  ? 8.806   5.137   19.539  1.00 44.61  ? 63  PRO B CB  1 
ATOM   1101 C CG  . PRO B 1 63  ? 9.603   3.971   19.932  1.00 55.34  ? 63  PRO B CG  1 
ATOM   1102 C CD  . PRO B 1 63  ? 10.550  3.676   18.796  1.00 49.47  ? 63  PRO B CD  1 
ATOM   1103 N N   . LYS B 1 64  ? 11.536  7.179   19.445  1.00 61.62  ? 64  LYS B N   1 
ATOM   1104 C CA  . LYS B 1 64  ? 12.142  8.305   20.137  1.00 67.28  ? 64  LYS B CA  1 
ATOM   1105 C C   . LYS B 1 64  ? 12.880  9.244   19.193  1.00 61.35  ? 64  LYS B C   1 
ATOM   1106 O O   . LYS B 1 64  ? 13.410  10.265  19.640  1.00 61.25  ? 64  LYS B O   1 
ATOM   1107 C CB  . LYS B 1 64  ? 13.088  7.796   21.235  1.00 62.36  ? 64  LYS B CB  1 
ATOM   1108 C CG  . LYS B 1 64  ? 12.401  6.904   22.281  1.00 73.13  ? 64  LYS B CG  1 
ATOM   1109 C CD  . LYS B 1 64  ? 13.218  6.783   23.572  1.00 65.15  ? 64  LYS B CD  1 
ATOM   1110 C CE  . LYS B 1 64  ? 14.553  6.101   23.328  1.00 74.59  ? 64  LYS B CE  1 
ATOM   1111 N NZ  . LYS B 1 64  ? 14.889  5.100   24.384  1.00 83.37  ? 64  LYS B NZ  1 
ATOM   1112 N N   . GLY B 1 65  ? 12.908  8.944   17.901  1.00 59.80  ? 65  GLY B N   1 
ATOM   1113 C CA  . GLY B 1 65  ? 13.730  9.684   16.976  1.00 56.60  ? 65  GLY B CA  1 
ATOM   1114 C C   . GLY B 1 65  ? 12.992  10.796  16.262  1.00 59.10  ? 65  GLY B C   1 
ATOM   1115 O O   . GLY B 1 65  ? 11.771  10.797  16.157  1.00 58.02  ? 65  GLY B O   1 
ATOM   1116 N N   . SER B 1 66  ? 13.764  11.755  15.762  1.00 57.77  ? 66  SER B N   1 
ATOM   1117 C CA  . SER B 1 66  ? 13.221  12.751  14.855  1.00 69.10  ? 66  SER B CA  1 
ATOM   1118 C C   . SER B 1 66  ? 12.864  12.102  13.520  1.00 66.28  ? 66  SER B C   1 
ATOM   1119 O O   . SER B 1 66  ? 13.262  10.974  13.224  1.00 55.98  ? 66  SER B O   1 
ATOM   1120 C CB  . SER B 1 66  ? 14.231  13.860  14.632  1.00 64.91  ? 66  SER B CB  1 
ATOM   1121 O OG  . SER B 1 66  ? 15.283  13.338  13.845  1.00 72.44  ? 66  SER B OG  1 
ATOM   1122 N N   . LYS B 1 67  ? 12.110  12.833  12.696  1.00 64.28  ? 67  LYS B N   1 
ATOM   1123 C CA  . LYS B 1 67  ? 11.656  12.255  11.433  1.00 62.02  ? 67  LYS B CA  1 
ATOM   1124 C C   . LYS B 1 67  ? 12.826  11.807  10.565  1.00 70.19  ? 67  LYS B C   1 
ATOM   1125 O O   . LYS B 1 67  ? 12.714  10.806  9.846   1.00 59.17  ? 67  LYS B O   1 
ATOM   1126 C CB  . LYS B 1 67  ? 10.780  13.253  10.673  1.00 80.01  ? 67  LYS B CB  1 
ATOM   1127 C CG  . LYS B 1 67  ? 11.464  13.876  9.471   1.00 84.25  ? 67  LYS B CG  1 
ATOM   1128 C CD  . LYS B 1 67  ? 10.891  15.243  9.129   1.00 93.80  ? 67  LYS B CD  1 
ATOM   1129 C CE  . LYS B 1 67  ? 11.606  15.820  7.917   1.00 98.78  ? 67  LYS B CE  1 
ATOM   1130 N NZ  . LYS B 1 67  ? 11.066  15.264  6.643   1.00 98.21  ? 67  LYS B NZ  1 
ATOM   1131 N N   . GLU B 1 68  ? 13.954  12.516  10.634  1.00 54.65  ? 68  GLU B N   1 
ATOM   1132 C CA  . GLU B 1 68  ? 15.129  12.143  9.854   1.00 68.01  ? 68  GLU B CA  1 
ATOM   1133 C C   . GLU B 1 68  ? 15.856  10.962  10.487  1.00 69.22  ? 68  GLU B C   1 
ATOM   1134 O O   . GLU B 1 68  ? 16.317  10.049  9.788   1.00 61.34  ? 68  GLU B O   1 
ATOM   1135 C CB  . GLU B 1 68  ? 16.073  13.340  9.733   1.00 60.93  ? 68  GLU B CB  1 
ATOM   1136 C CG  . GLU B 1 68  ? 17.522  12.931  9.510   1.00 74.97  ? 68  GLU B CG  1 
ATOM   1137 C CD  . GLU B 1 68  ? 18.289  13.901  8.629   1.00 79.39  ? 68  GLU B CD  1 
ATOM   1138 O OE1 . GLU B 1 68  ? 17.659  14.701  7.901   1.00 100.06 ? 68  GLU B OE1 1 
ATOM   1139 O OE2 . GLU B 1 68  ? 19.533  13.863  8.674   1.00 77.97  ? 68  GLU B OE2 1 
ATOM   1140 N N   . GLU B 1 69  ? 15.980  10.970  11.815  1.00 61.88  ? 69  GLU B N   1 
ATOM   1141 C CA  . GLU B 1 69  ? 16.581  9.829   12.497  1.00 60.81  ? 69  GLU B CA  1 
ATOM   1142 C C   . GLU B 1 69  ? 15.786  8.556   12.229  1.00 60.64  ? 69  GLU B C   1 
ATOM   1143 O O   . GLU B 1 69  ? 16.362  7.477   12.037  1.00 53.68  ? 69  GLU B O   1 
ATOM   1144 C CB  . GLU B 1 69  ? 16.670  10.112  13.997  1.00 72.75  ? 69  GLU B CB  1 
ATOM   1145 C CG  . GLU B 1 69  ? 17.791  11.077  14.389  1.00 56.59  ? 69  GLU B CG  1 
ATOM   1146 C CD  . GLU B 1 69  ? 17.619  11.628  15.801  1.00 60.88  ? 69  GLU B CD  1 
ATOM   1147 O OE1 . GLU B 1 69  ? 16.480  11.628  16.322  1.00 64.22  ? 69  GLU B OE1 1 
ATOM   1148 O OE2 . GLU B 1 69  ? 18.631  12.034  16.405  1.00 74.09  ? 69  GLU B OE2 1 
ATOM   1149 N N   . GLN B 1 70  ? 14.459  8.670   12.180  1.00 48.36  ? 70  GLN B N   1 
ATOM   1150 C CA  . GLN B 1 70  ? 13.639  7.491   11.961  1.00 55.88  ? 70  GLN B CA  1 
ATOM   1151 C C   . GLN B 1 70  ? 13.898  6.894   10.589  1.00 55.00  ? 70  GLN B C   1 
ATOM   1152 O O   . GLN B 1 70  ? 13.829  5.674   10.421  1.00 49.07  ? 70  GLN B O   1 
ATOM   1153 C CB  . GLN B 1 70  ? 12.173  7.856   12.141  1.00 51.38  ? 70  GLN B CB  1 
ATOM   1154 C CG  . GLN B 1 70  ? 11.793  7.966   13.609  1.00 50.97  ? 70  GLN B CG  1 
ATOM   1155 C CD  . GLN B 1 70  ? 10.345  8.348   13.815  1.00 71.56  ? 70  GLN B CD  1 
ATOM   1156 O OE1 . GLN B 1 70  ? 9.679   8.850   12.902  1.00 56.08  ? 70  GLN B OE1 1 
ATOM   1157 N NE2 . GLN B 1 70  ? 9.842   8.113   15.026  1.00 64.20  ? 70  GLN B NE2 1 
ATOM   1158 N N   . ARG B 1 71  ? 14.224  7.736   9.609   1.00 55.93  ? 71  ARG B N   1 
ATOM   1159 C CA  . ARG B 1 71  ? 14.609  7.254   8.285   1.00 67.89  ? 71  ARG B CA  1 
ATOM   1160 C C   . ARG B 1 71  ? 15.881  6.430   8.343   1.00 56.58  ? 71  ARG B C   1 
ATOM   1161 O O   . ARG B 1 71  ? 15.989  5.388   7.689   1.00 51.43  ? 71  ARG B O   1 
ATOM   1162 C CB  . ARG B 1 71  ? 14.849  8.429   7.355   1.00 61.91  ? 71  ARG B CB  1 
ATOM   1163 C CG  . ARG B 1 71  ? 13.661  9.270   7.167   1.00 73.40  ? 71  ARG B CG  1 
ATOM   1164 C CD  . ARG B 1 71  ? 13.804  10.169  5.963   1.00 85.16  ? 71  ARG B CD  1 
ATOM   1165 N NE  . ARG B 1 71  ? 12.485  10.393  5.394   1.00 108.95 ? 71  ARG B NE  1 
ATOM   1166 C CZ  . ARG B 1 71  ? 11.744  9.466   4.800   1.00 105.78 ? 71  ARG B CZ  1 
ATOM   1167 N NH1 . ARG B 1 71  ? 12.225  8.258   4.517   1.00 91.44  ? 71  ARG B NH1 1 
ATOM   1168 N NH2 . ARG B 1 71  ? 10.489  9.761   4.476   1.00 101.35 ? 71  ARG B NH2 1 
ATOM   1169 N N   . ASP B 1 72  ? 16.879  6.926   9.070   1.00 52.34  ? 72  ASP B N   1 
ATOM   1170 C CA  . ASP B 1 72  ? 18.098  6.163   9.278   1.00 51.44  ? 72  ASP B CA  1 
ATOM   1171 C C   . ASP B 1 72  ? 17.795  4.882   10.021  1.00 61.09  ? 72  ASP B C   1 
ATOM   1172 O O   . ASP B 1 72  ? 18.168  3.795   9.571   1.00 57.06  ? 72  ASP B O   1 
ATOM   1173 C CB  . ASP B 1 72  ? 19.113  6.995   10.050  1.00 54.59  ? 72  ASP B CB  1 
ATOM   1174 C CG  . ASP B 1 72  ? 19.551  8.216   9.285   1.00 63.61  ? 72  ASP B CG  1 
ATOM   1175 O OD1 . ASP B 1 72  ? 19.344  8.251   8.050   1.00 63.10  ? 72  ASP B OD1 1 
ATOM   1176 O OD2 . ASP B 1 72  ? 20.081  9.147   9.924   1.00 71.89  ? 72  ASP B OD2 1 
ATOM   1177 N N   . TYR B 1 73  ? 17.094  4.993   11.159  1.00 50.40  ? 73  TYR B N   1 
ATOM   1178 C CA  . TYR B 1 73  ? 16.738  3.805   11.921  1.00 44.67  ? 73  TYR B CA  1 
ATOM   1179 C C   . TYR B 1 73  ? 16.089  2.761   11.023  1.00 50.76  ? 73  TYR B C   1 
ATOM   1180 O O   . TYR B 1 73  ? 16.454  1.577   11.062  1.00 50.07  ? 73  TYR B O   1 
ATOM   1181 C CB  . TYR B 1 73  ? 15.798  4.171   13.079  1.00 48.29  ? 73  TYR B CB  1 
ATOM   1182 C CG  . TYR B 1 73  ? 16.366  5.132   14.112  1.00 49.57  ? 73  TYR B CG  1 
ATOM   1183 C CD1 . TYR B 1 73  ? 17.737  5.309   14.265  1.00 48.78  ? 73  TYR B CD1 1 
ATOM   1184 C CD2 . TYR B 1 73  ? 15.523  5.849   14.946  1.00 49.89  ? 73  TYR B CD2 1 
ATOM   1185 C CE1 . TYR B 1 73  ? 18.247  6.187   15.226  1.00 44.17  ? 73  TYR B CE1 1 
ATOM   1186 C CE2 . TYR B 1 73  ? 16.017  6.709   15.905  1.00 45.48  ? 73  TYR B CE2 1 
ATOM   1187 C CZ  . TYR B 1 73  ? 17.375  6.888   16.038  1.00 58.94  ? 73  TYR B CZ  1 
ATOM   1188 O OH  . TYR B 1 73  ? 17.843  7.765   16.997  1.00 49.82  ? 73  TYR B OH  1 
ATOM   1189 N N   . VAL B 1 74  ? 15.168  3.193   10.158  1.00 46.90  ? 74  VAL B N   1 
ATOM   1190 C CA  . VAL B 1 74  ? 14.408  2.248   9.338   1.00 52.23  ? 74  VAL B CA  1 
ATOM   1191 C C   . VAL B 1 74  ? 15.316  1.536   8.342   1.00 48.52  ? 74  VAL B C   1 
ATOM   1192 O O   . VAL B 1 74  ? 15.174  0.331   8.103   1.00 47.01  ? 74  VAL B O   1 
ATOM   1193 C CB  . VAL B 1 74  ? 13.255  2.978   8.624   1.00 63.07  ? 74  VAL B CB  1 
ATOM   1194 C CG1 . VAL B 1 74  ? 12.817  2.195   7.399   1.00 51.93  ? 74  VAL B CG1 1 
ATOM   1195 C CG2 . VAL B 1 74  ? 12.088  3.187   9.584   1.00 48.60  ? 74  VAL B CG2 1 
ATOM   1196 N N   . PHE B 1 75  ? 16.248  2.270   7.729   1.00 44.91  ? 75  PHE B N   1 
ATOM   1197 C CA  . PHE B 1 75  ? 17.191  1.650   6.798   1.00 54.19  ? 75  PHE B CA  1 
ATOM   1198 C C   . PHE B 1 75  ? 18.059  0.616   7.503   1.00 45.73  ? 75  PHE B C   1 
ATOM   1199 O O   . PHE B 1 75  ? 18.316  -0.467  6.960   1.00 45.69  ? 75  PHE B O   1 
ATOM   1200 C CB  . PHE B 1 75  ? 18.066  2.721   6.144   1.00 40.38  ? 75  PHE B CB  1 
ATOM   1201 C CG  . PHE B 1 75  ? 19.239  2.164   5.380   1.00 57.93  ? 75  PHE B CG  1 
ATOM   1202 C CD1 . PHE B 1 75  ? 19.095  1.744   4.064   1.00 54.00  ? 75  PHE B CD1 1 
ATOM   1203 C CD2 . PHE B 1 75  ? 20.484  2.053   5.979   1.00 48.76  ? 75  PHE B CD2 1 
ATOM   1204 C CE1 . PHE B 1 75  ? 20.180  1.228   3.358   1.00 52.83  ? 75  PHE B CE1 1 
ATOM   1205 C CE2 . PHE B 1 75  ? 21.574  1.541   5.282   1.00 62.19  ? 75  PHE B CE2 1 
ATOM   1206 C CZ  . PHE B 1 75  ? 21.421  1.129   3.970   1.00 51.84  ? 75  PHE B CZ  1 
ATOM   1207 N N   . TYR B 1 76  ? 18.523  0.931   8.712   1.00 43.45  ? 76  TYR B N   1 
ATOM   1208 C CA  . TYR B 1 76  ? 19.370  -0.007  9.439   1.00 44.40  ? 76  TYR B CA  1 
ATOM   1209 C C   . TYR B 1 76  ? 18.581  -1.195  9.970   1.00 48.78  ? 76  TYR B C   1 
ATOM   1210 O O   . TYR B 1 76  ? 19.149  -2.283  10.117  1.00 41.10  ? 76  TYR B O   1 
ATOM   1211 C CB  . TYR B 1 76  ? 20.106  0.717   10.567  1.00 54.22  ? 76  TYR B CB  1 
ATOM   1212 C CG  . TYR B 1 76  ? 21.148  1.714   10.056  1.00 62.18  ? 76  TYR B CG  1 
ATOM   1213 C CD1 . TYR B 1 76  ? 22.315  1.283   9.450   1.00 73.19  ? 76  TYR B CD1 1 
ATOM   1214 C CD2 . TYR B 1 76  ? 20.956  3.076   10.192  1.00 63.01  ? 76  TYR B CD2 1 
ATOM   1215 C CE1 . TYR B 1 76  ? 23.264  2.196   8.987   1.00 84.06  ? 76  TYR B CE1 1 
ATOM   1216 C CE2 . TYR B 1 76  ? 21.886  3.993   9.729   1.00 69.60  ? 76  TYR B CE2 1 
ATOM   1217 C CZ  . TYR B 1 76  ? 23.037  3.548   9.127   1.00 74.88  ? 76  TYR B CZ  1 
ATOM   1218 O OH  . TYR B 1 76  ? 23.961  4.467   8.677   1.00 83.24  ? 76  TYR B OH  1 
ATOM   1219 N N   . LEU B 1 77  ? 17.275  -1.016  10.251  1.00 38.62  ? 77  LEU B N   1 
ATOM   1220 C CA  . LEU B 1 77  ? 16.416  -2.145  10.591  1.00 44.29  ? 77  LEU B CA  1 
ATOM   1221 C C   . LEU B 1 77  ? 16.232  -3.057  9.393   1.00 44.30  ? 77  LEU B C   1 
ATOM   1222 O O   . LEU B 1 77  ? 16.170  -4.286  9.536   1.00 43.32  ? 77  LEU B O   1 
ATOM   1223 C CB  . LEU B 1 77  ? 15.046  -1.643  11.087  1.00 40.88  ? 77  LEU B CB  1 
ATOM   1224 C CG  . LEU B 1 77  ? 14.999  -1.285  12.576  1.00 46.51  ? 77  LEU B CG  1 
ATOM   1225 C CD1 . LEU B 1 77  ? 13.906  -0.253  12.877  1.00 49.98  ? 77  LEU B CD1 1 
ATOM   1226 C CD2 . LEU B 1 77  ? 14.783  -2.548  13.404  1.00 48.85  ? 77  LEU B CD2 1 
ATOM   1227 N N   . ALA B 1 78  ? 16.103  -2.474  8.200   1.00 40.32  ? 78  ALA B N   1 
ATOM   1228 C CA  . ALA B 1 78  ? 16.035  -3.298  6.999   1.00 42.89  ? 78  ALA B CA  1 
ATOM   1229 C C   . ALA B 1 78  ? 17.310  -4.113  6.832   1.00 52.06  ? 78  ALA B C   1 
ATOM   1230 O O   . ALA B 1 78  ? 17.253  -5.336  6.638   1.00 44.29  ? 78  ALA B O   1 
ATOM   1231 C CB  . ALA B 1 78  ? 15.776  -2.414  5.777   1.00 45.32  ? 78  ALA B CB  1 
ATOM   1232 N N   . VAL B 1 79  ? 18.476  -3.449  6.926   1.00 43.32  ? 79  VAL B N   1 
ATOM   1233 C CA  . VAL B 1 79  ? 19.766  -4.133  6.797   1.00 46.23  ? 79  VAL B CA  1 
ATOM   1234 C C   . VAL B 1 79  ? 19.874  -5.283  7.791   1.00 43.19  ? 79  VAL B C   1 
ATOM   1235 O O   . VAL B 1 79  ? 20.253  -6.402  7.432   1.00 47.73  ? 79  VAL B O   1 
ATOM   1236 C CB  . VAL B 1 79  ? 20.930  -3.139  6.991   1.00 49.56  ? 79  VAL B CB  1 
ATOM   1237 C CG1 . VAL B 1 79  ? 22.262  -3.893  7.087   1.00 55.68  ? 79  VAL B CG1 1 
ATOM   1238 C CG2 . VAL B 1 79  ? 20.986  -2.118  5.865   1.00 50.10  ? 79  VAL B CG2 1 
ATOM   1239 N N   . GLY B 1 80  ? 19.575  -5.015  9.067   1.00 50.47  ? 80  GLY B N   1 
ATOM   1240 C CA  . GLY B 1 80  ? 19.711  -6.052  10.079  1.00 43.86  ? 80  GLY B CA  1 
ATOM   1241 C C   . GLY B 1 80  ? 18.828  -7.252  9.804   1.00 51.63  ? 80  GLY B C   1 
ATOM   1242 O O   . GLY B 1 80  ? 19.270  -8.402  9.893   1.00 51.12  ? 80  GLY B O   1 
ATOM   1243 N N   . ASN B 1 81  ? 17.567  -6.999  9.458   1.00 46.62  ? 81  ASN B N   1 
ATOM   1244 C CA  . ASN B 1 81  ? 16.641  -8.084  9.163   1.00 48.79  ? 81  ASN B CA  1 
ATOM   1245 C C   . ASN B 1 81  ? 17.069  -8.851  7.912   1.00 46.65  ? 81  ASN B C   1 
ATOM   1246 O O   . ASN B 1 81  ? 16.901  -10.074 7.836   1.00 50.10  ? 81  ASN B O   1 
ATOM   1247 C CB  . ASN B 1 81  ? 15.235  -7.511  8.997   1.00 45.82  ? 81  ASN B CB  1 
ATOM   1248 C CG  . ASN B 1 81  ? 14.469  -7.430  10.321  1.00 42.22  ? 81  ASN B CG  1 
ATOM   1249 O OD1 . ASN B 1 81  ? 14.018  -8.442  10.846  1.00 51.48  ? 81  ASN B OD1 1 
ATOM   1250 N ND2 . ASN B 1 81  ? 14.311  -6.216  10.848  1.00 46.02  ? 81  ASN B ND2 1 
ATOM   1251 N N   . TYR B 1 82  ? 17.589  -8.141  6.911   1.00 48.58  ? 82  TYR B N   1 
ATOM   1252 C CA  . TYR B 1 82  ? 18.125  -8.799  5.726   1.00 49.71  ? 82  TYR B CA  1 
ATOM   1253 C C   . TYR B 1 82  ? 19.225  -9.775  6.107   1.00 50.58  ? 82  TYR B C   1 
ATOM   1254 O O   . TYR B 1 82  ? 19.227  -10.929 5.665   1.00 55.04  ? 82  TYR B O   1 
ATOM   1255 C CB  . TYR B 1 82  ? 18.646  -7.740  4.753   1.00 48.92  ? 82  TYR B CB  1 
ATOM   1256 C CG  . TYR B 1 82  ? 19.553  -8.250  3.653   1.00 57.46  ? 82  TYR B CG  1 
ATOM   1257 C CD1 . TYR B 1 82  ? 19.037  -8.912  2.546   1.00 52.58  ? 82  TYR B CD1 1 
ATOM   1258 C CD2 . TYR B 1 82  ? 20.927  -8.052  3.715   1.00 59.92  ? 82  TYR B CD2 1 
ATOM   1259 C CE1 . TYR B 1 82  ? 19.870  -9.370  1.531   1.00 57.32  ? 82  TYR B CE1 1 
ATOM   1260 C CE2 . TYR B 1 82  ? 21.769  -8.515  2.710   1.00 66.02  ? 82  TYR B CE2 1 
ATOM   1261 C CZ  . TYR B 1 82  ? 21.235  -9.168  1.620   1.00 68.91  ? 82  TYR B CZ  1 
ATOM   1262 O OH  . TYR B 1 82  ? 22.071  -9.624  0.619   1.00 61.54  ? 82  TYR B OH  1 
ATOM   1263 N N   . ARG B 1 83  ? 20.174  -9.331  6.938   1.00 50.82  ? 83  ARG B N   1 
ATOM   1264 C CA  . ARG B 1 83  ? 21.258  -10.224 7.327   1.00 59.59  ? 83  ARG B CA  1 
ATOM   1265 C C   . ARG B 1 83  ? 20.743  -11.398 8.143   1.00 66.33  ? 83  ARG B C   1 
ATOM   1266 O O   . ARG B 1 83  ? 21.297  -12.499 8.046   1.00 53.17  ? 83  ARG B O   1 
ATOM   1267 C CB  . ARG B 1 83  ? 22.346  -9.464  8.095   1.00 48.45  ? 83  ARG B CB  1 
ATOM   1268 C CG  . ARG B 1 83  ? 23.000  -8.379  7.272   1.00 48.47  ? 83  ARG B CG  1 
ATOM   1269 C CD  . ARG B 1 83  ? 24.257  -7.841  7.887   1.00 47.74  ? 83  ARG B CD  1 
ATOM   1270 N NE  . ARG B 1 83  ? 25.342  -8.808  7.862   1.00 69.95  ? 83  ARG B NE  1 
ATOM   1271 C CZ  . ARG B 1 83  ? 26.230  -8.954  8.834   1.00 73.74  ? 83  ARG B CZ  1 
ATOM   1272 N NH1 . ARG B 1 83  ? 26.206  -8.184  9.913   1.00 53.59  ? 83  ARG B NH1 1 
ATOM   1273 N NH2 . ARG B 1 83  ? 27.164  -9.895  8.719   1.00 69.55  ? 83  ARG B NH2 1 
ATOM   1274 N N   . LEU B 1 84  ? 19.683  -11.197 8.931   1.00 60.09  ? 84  LEU B N   1 
ATOM   1275 C CA  . LEU B 1 84  ? 19.049  -12.298 9.653   1.00 51.38  ? 84  LEU B CA  1 
ATOM   1276 C C   . LEU B 1 84  ? 18.157  -13.145 8.770   1.00 58.68  ? 84  LEU B C   1 
ATOM   1277 O O   . LEU B 1 84  ? 17.484  -14.041 9.284   1.00 60.74  ? 84  LEU B O   1 
ATOM   1278 C CB  . LEU B 1 84  ? 18.196  -11.792 10.820  1.00 57.00  ? 84  LEU B CB  1 
ATOM   1279 C CG  . LEU B 1 84  ? 18.873  -11.339 12.110  1.00 64.67  ? 84  LEU B CG  1 
ATOM   1280 C CD1 . LEU B 1 84  ? 17.839  -11.363 13.216  1.00 72.24  ? 84  LEU B CD1 1 
ATOM   1281 C CD2 . LEU B 1 84  ? 20.055  -12.235 12.457  1.00 61.63  ? 84  LEU B CD2 1 
ATOM   1282 N N   . LYS B 1 85  ? 18.101  -12.865 7.473   1.00 63.98  ? 85  LYS B N   1 
ATOM   1283 C CA  . LYS B 1 85  ? 17.229  -13.568 6.548   1.00 58.08  ? 85  LYS B CA  1 
ATOM   1284 C C   . LYS B 1 85  ? 15.754  -13.369 6.877   1.00 67.69  ? 85  LYS B C   1 
ATOM   1285 O O   . LYS B 1 85  ? 14.914  -14.163 6.457   1.00 58.69  ? 85  LYS B O   1 
ATOM   1286 C CB  . LYS B 1 85  ? 17.582  -15.060 6.498   1.00 58.94  ? 85  LYS B CB  1 
ATOM   1287 C CG  . LYS B 1 85  ? 19.087  -15.310 6.474   1.00 61.27  ? 85  LYS B CG  1 
ATOM   1288 C CD  . LYS B 1 85  ? 19.457  -16.429 5.500   1.00 72.77  ? 85  LYS B CD  1 
ATOM   1289 C CE  . LYS B 1 85  ? 18.830  -17.738 5.909   1.00 72.05  ? 85  LYS B CE  1 
ATOM   1290 N NZ  . LYS B 1 85  ? 19.787  -18.590 6.649   1.00 83.77  ? 85  LYS B NZ  1 
ATOM   1291 N N   . GLU B 1 86  ? 15.412  -12.318 7.627   1.00 60.38  ? 86  GLU B N   1 
ATOM   1292 C CA  . GLU B 1 86  ? 14.015  -11.909 7.773   1.00 58.74  ? 86  GLU B CA  1 
ATOM   1293 C C   . GLU B 1 86  ? 13.601  -11.056 6.572   1.00 57.27  ? 86  GLU B C   1 
ATOM   1294 O O   . GLU B 1 86  ? 13.271  -9.876  6.688   1.00 63.19  ? 86  GLU B O   1 
ATOM   1295 C CB  . GLU B 1 86  ? 13.810  -11.163 9.083   1.00 58.85  ? 86  GLU B CB  1 
ATOM   1296 C CG  . GLU B 1 86  ? 13.917  -12.048 10.318  1.00 56.57  ? 86  GLU B CG  1 
ATOM   1297 C CD  . GLU B 1 86  ? 12.789  -13.048 10.419  1.00 66.18  ? 86  GLU B CD  1 
ATOM   1298 O OE1 . GLU B 1 86  ? 13.072  -14.239 10.662  1.00 79.27  ? 86  GLU B OE1 1 
ATOM   1299 O OE2 . GLU B 1 86  ? 11.620  -12.641 10.258  1.00 76.82  ? 86  GLU B OE2 1 
ATOM   1300 N N   . TYR B 1 87  ? 13.612  -11.700 5.398   1.00 64.45  ? 87  TYR B N   1 
ATOM   1301 C CA  . TYR B 1 87  ? 13.507  -10.968 4.134   1.00 67.20  ? 87  TYR B CA  1 
ATOM   1302 C C   . TYR B 1 87  ? 12.177  -10.239 4.009   1.00 62.15  ? 87  TYR B C   1 
ATOM   1303 O O   . TYR B 1 87  ? 12.124  -9.112  3.502   1.00 65.10  ? 87  TYR B O   1 
ATOM   1304 C CB  . TYR B 1 87  ? 13.709  -11.925 2.958   1.00 59.80  ? 87  TYR B CB  1 
ATOM   1305 C CG  . TYR B 1 87  ? 15.096  -12.520 2.915   1.00 67.49  ? 87  TYR B CG  1 
ATOM   1306 C CD1 . TYR B 1 87  ? 16.222  -11.710 3.025   1.00 62.93  ? 87  TYR B CD1 1 
ATOM   1307 C CD2 . TYR B 1 87  ? 15.285  -13.891 2.788   1.00 61.25  ? 87  TYR B CD2 1 
ATOM   1308 C CE1 . TYR B 1 87  ? 17.497  -12.249 3.003   1.00 64.41  ? 87  TYR B CE1 1 
ATOM   1309 C CE2 . TYR B 1 87  ? 16.554  -14.432 2.767   1.00 59.77  ? 87  TYR B CE2 1 
ATOM   1310 C CZ  . TYR B 1 87  ? 17.655  -13.612 2.873   1.00 63.82  ? 87  TYR B CZ  1 
ATOM   1311 O OH  . TYR B 1 87  ? 18.925  -14.147 2.855   1.00 76.95  ? 87  TYR B OH  1 
ATOM   1312 N N   . GLU B 1 88  ? 11.091  -10.857 4.471   1.00 57.46  ? 88  GLU B N   1 
ATOM   1313 C CA  . GLU B 1 88  ? 9.787   -10.207 4.383   1.00 59.65  ? 88  GLU B CA  1 
ATOM   1314 C C   . GLU B 1 88  ? 9.723   -8.968  5.277   1.00 65.60  ? 88  GLU B C   1 
ATOM   1315 O O   . GLU B 1 88  ? 9.171   -7.936  4.878   1.00 67.95  ? 88  GLU B O   1 
ATOM   1316 C CB  . GLU B 1 88  ? 8.679   -11.206 4.734   1.00 75.60  ? 88  GLU B CB  1 
ATOM   1317 C CG  . GLU B 1 88  ? 8.660   -11.661 6.199   1.00 81.86  ? 88  GLU B CG  1 
ATOM   1318 C CD  . GLU B 1 88  ? 9.942   -12.383 6.621   1.00 92.89  ? 88  GLU B CD  1 
ATOM   1319 O OE1 . GLU B 1 88  ? 10.659  -11.850 7.506   1.00 73.39  ? 88  GLU B OE1 1 
ATOM   1320 O OE2 . GLU B 1 88  ? 10.220  -13.486 6.077   1.00 83.23  ? 88  GLU B OE2 1 
ATOM   1321 N N   . LYS B 1 89  ? 10.294  -9.043  6.481   1.00 58.05  ? 89  LYS B N   1 
ATOM   1322 C CA  . LYS B 1 89  ? 10.361  -7.866  7.343   1.00 60.30  ? 89  LYS B CA  1 
ATOM   1323 C C   . LYS B 1 89  ? 11.261  -6.796  6.733   1.00 60.13  ? 89  LYS B C   1 
ATOM   1324 O O   . LYS B 1 89  ? 10.888  -5.621  6.674   1.00 55.17  ? 89  LYS B O   1 
ATOM   1325 C CB  . LYS B 1 89  ? 10.861  -8.266  8.732   1.00 64.74  ? 89  LYS B CB  1 
ATOM   1326 C CG  . LYS B 1 89  ? 9.800   -8.227  9.828   1.00 74.40  ? 89  LYS B CG  1 
ATOM   1327 C CD  . LYS B 1 89  ? 9.857   -6.913  10.620  1.00 64.53  ? 89  LYS B CD  1 
ATOM   1328 C CE  . LYS B 1 89  ? 8.765   -6.849  11.694  1.00 80.34  ? 89  LYS B CE  1 
ATOM   1329 N NZ  . LYS B 1 89  ? 9.110   -5.904  12.801  1.00 71.23  ? 89  LYS B NZ  1 
ATOM   1330 N N   . ALA B 1 90  ? 12.460  -7.186  6.279   1.00 45.29  ? 90  ALA B N   1 
ATOM   1331 C CA  . ALA B 1 90  ? 13.355  -6.221  5.645   1.00 47.78  ? 90  ALA B CA  1 
ATOM   1332 C C   . ALA B 1 90  ? 12.688  -5.555  4.453   1.00 51.16  ? 90  ALA B C   1 
ATOM   1333 O O   . ALA B 1 90  ? 12.806  -4.338  4.260   1.00 46.75  ? 90  ALA B O   1 
ATOM   1334 C CB  . ALA B 1 90  ? 14.650  -6.908  5.208   1.00 46.25  ? 90  ALA B CB  1 
ATOM   1335 N N   . LEU B 1 91  ? 11.977  -6.337  3.646   1.00 49.83  ? 91  LEU B N   1 
ATOM   1336 C CA  . LEU B 1 91  ? 11.294  -5.778  2.491   1.00 53.52  ? 91  LEU B CA  1 
ATOM   1337 C C   . LEU B 1 91  ? 10.202  -4.801  2.924   1.00 67.33  ? 91  LEU B C   1 
ATOM   1338 O O   . LEU B 1 91  ? 10.016  -3.751  2.300   1.00 60.14  ? 91  LEU B O   1 
ATOM   1339 C CB  . LEU B 1 91  ? 10.723  -6.917  1.655   1.00 57.20  ? 91  LEU B CB  1 
ATOM   1340 C CG  . LEU B 1 91  ? 10.710  -6.869  0.134   1.00 69.59  ? 91  LEU B CG  1 
ATOM   1341 C CD1 . LEU B 1 91  ? 11.981  -6.284  -0.450  1.00 60.42  ? 91  LEU B CD1 1 
ATOM   1342 C CD2 . LEU B 1 91  ? 10.533  -8.283  -0.341  1.00 66.74  ? 91  LEU B CD2 1 
ATOM   1343 N N   . LYS B 1 92  ? 9.493   -5.112  4.014   1.00 53.69  ? 92  LYS B N   1 
ATOM   1344 C CA  . LYS B 1 92  ? 8.471   -4.196  4.517   1.00 56.66  ? 92  LYS B CA  1 
ATOM   1345 C C   . LYS B 1 92  ? 9.078   -2.856  4.945   1.00 66.08  ? 92  LYS B C   1 
ATOM   1346 O O   . LYS B 1 92  ? 8.521   -1.789  4.651   1.00 60.01  ? 92  LYS B O   1 
ATOM   1347 C CB  . LYS B 1 92  ? 7.731   -4.843  5.683   1.00 69.51  ? 92  LYS B CB  1 
ATOM   1348 C CG  . LYS B 1 92  ? 6.448   -4.139  6.099   1.00 71.02  ? 92  LYS B CG  1 
ATOM   1349 C CD  . LYS B 1 92  ? 5.330   -4.331  5.083   1.00 84.71  ? 92  LYS B CD  1 
ATOM   1350 C CE  . LYS B 1 92  ? 4.064   -3.577  5.509   1.00 91.06  ? 92  LYS B CE  1 
ATOM   1351 N NZ  . LYS B 1 92  ? 2.837   -3.911  4.699   1.00 76.61  ? 92  LYS B NZ  1 
ATOM   1352 N N   . TYR B 1 93  ? 10.208  -2.891  5.657   1.00 54.01  ? 93  TYR B N   1 
ATOM   1353 C CA  . TYR B 1 93  ? 10.877  -1.649  6.059   1.00 58.18  ? 93  TYR B CA  1 
ATOM   1354 C C   . TYR B 1 93  ? 11.331  -0.844  4.852   1.00 50.16  ? 93  TYR B C   1 
ATOM   1355 O O   . TYR B 1 93  ? 11.175  0.381   4.816   1.00 56.95  ? 93  TYR B O   1 
ATOM   1356 C CB  . TYR B 1 93  ? 12.095  -1.949  6.943   1.00 50.85  ? 93  TYR B CB  1 
ATOM   1357 C CG  . TYR B 1 93  ? 11.775  -2.218  8.399   1.00 62.05  ? 93  TYR B CG  1 
ATOM   1358 C CD1 . TYR B 1 93  ? 11.195  -1.242  9.201   1.00 53.95  ? 93  TYR B CD1 1 
ATOM   1359 C CD2 . TYR B 1 93  ? 12.056  -3.451  8.968   1.00 53.28  ? 93  TYR B CD2 1 
ATOM   1360 C CE1 . TYR B 1 93  ? 10.905  -1.498  10.540  1.00 53.80  ? 93  TYR B CE1 1 
ATOM   1361 C CE2 . TYR B 1 93  ? 11.767  -3.718  10.296  1.00 53.05  ? 93  TYR B CE2 1 
ATOM   1362 C CZ  . TYR B 1 93  ? 11.197  -2.741  11.075  1.00 54.57  ? 93  TYR B CZ  1 
ATOM   1363 O OH  . TYR B 1 93  ? 10.910  -3.026  12.389  1.00 64.65  ? 93  TYR B OH  1 
ATOM   1364 N N   . VAL B 1 94  ? 11.950  -1.508  3.879   1.00 59.90  ? 94  VAL B N   1 
ATOM   1365 C CA  . VAL B 1 94  ? 12.546  -0.779  2.771   1.00 57.14  ? 94  VAL B CA  1 
ATOM   1366 C C   . VAL B 1 94  ? 11.476  -0.311  1.799   1.00 56.28  ? 94  VAL B C   1 
ATOM   1367 O O   . VAL B 1 94  ? 11.629  0.744   1.172   1.00 63.12  ? 94  VAL B O   1 
ATOM   1368 C CB  . VAL B 1 94  ? 13.637  -1.634  2.088   1.00 61.15  ? 94  VAL B CB  1 
ATOM   1369 C CG1 . VAL B 1 94  ? 13.043  -2.586  1.081   1.00 53.87  ? 94  VAL B CG1 1 
ATOM   1370 C CG2 . VAL B 1 94  ? 14.657  -0.728  1.393   1.00 56.04  ? 94  VAL B CG2 1 
ATOM   1371 N N   . ARG B 1 95  ? 10.364  -1.046  1.680   1.00 61.15  ? 95  ARG B N   1 
ATOM   1372 C CA  . ARG B 1 95  ? 9.242   -0.541  0.896   1.00 61.17  ? 95  ARG B CA  1 
ATOM   1373 C C   . ARG B 1 95  ? 8.686   0.736   1.505   1.00 62.92  ? 95  ARG B C   1 
ATOM   1374 O O   . ARG B 1 95  ? 8.325   1.670   0.779   1.00 58.90  ? 95  ARG B O   1 
ATOM   1375 C CB  . ARG B 1 95  ? 8.139   -1.594  0.785   1.00 62.78  ? 95  ARG B CB  1 
ATOM   1376 C CG  . ARG B 1 95  ? 8.070   -2.272  -0.573  1.00 79.38  ? 95  ARG B CG  1 
ATOM   1377 C CD  . ARG B 1 95  ? 8.801   -3.600  -0.538  1.00 79.49  ? 95  ARG B CD  1 
ATOM   1378 N NE  . ARG B 1 95  ? 8.843   -4.276  -1.829  1.00 79.07  ? 95  ARG B NE  1 
ATOM   1379 C CZ  . ARG B 1 95  ? 8.182   -5.387  -2.119  1.00 72.44  ? 95  ARG B CZ  1 
ATOM   1380 N NH1 . ARG B 1 95  ? 7.345   -5.941  -1.255  1.00 67.84  ? 95  ARG B NH1 1 
ATOM   1381 N NH2 . ARG B 1 95  ? 8.374   -5.964  -3.304  1.00 87.34  ? 95  ARG B NH2 1 
ATOM   1382 N N   . GLY B 1 96  ? 8.611   0.800   2.838   1.00 62.57  ? 96  GLY B N   1 
ATOM   1383 C CA  . GLY B 1 96  ? 8.089   2.001   3.476   1.00 59.93  ? 96  GLY B CA  1 
ATOM   1384 C C   . GLY B 1 96  ? 8.974   3.206   3.235   1.00 68.61  ? 96  GLY B C   1 
ATOM   1385 O O   . GLY B 1 96  ? 8.487   4.314   2.986   1.00 72.71  ? 96  GLY B O   1 
ATOM   1386 N N   . LEU B 1 97  ? 10.290  3.000   3.295   1.00 57.47  ? 97  LEU B N   1 
ATOM   1387 C CA  . LEU B 1 97  ? 11.229  4.068   2.994   1.00 51.50  ? 97  LEU B CA  1 
ATOM   1388 C C   . LEU B 1 97  ? 10.992  4.599   1.591   1.00 63.59  ? 97  LEU B C   1 
ATOM   1389 O O   . LEU B 1 97  ? 11.037  5.812   1.358   1.00 72.99  ? 97  LEU B O   1 
ATOM   1390 C CB  . LEU B 1 97  ? 12.655  3.540   3.137   1.00 60.43  ? 97  LEU B CB  1 
ATOM   1391 C CG  . LEU B 1 97  ? 13.727  4.450   3.722   1.00 71.50  ? 97  LEU B CG  1 
ATOM   1392 C CD1 . LEU B 1 97  ? 13.200  5.094   4.998   1.00 71.46  ? 97  LEU B CD1 1 
ATOM   1393 C CD2 . LEU B 1 97  ? 15.003  3.665   3.976   1.00 68.00  ? 97  LEU B CD2 1 
ATOM   1394 N N   . LEU B 1 98  ? 10.689  3.700   0.652   1.00 59.19  ? 98  LEU B N   1 
ATOM   1395 C CA  . LEU B 1 98  ? 10.525  4.072   -0.746  1.00 70.46  ? 98  LEU B CA  1 
ATOM   1396 C C   . LEU B 1 98  ? 9.171   4.685   -1.049  1.00 69.97  ? 98  LEU B C   1 
ATOM   1397 O O   . LEU B 1 98  ? 9.034   5.370   -2.068  1.00 79.28  ? 98  LEU B O   1 
ATOM   1398 C CB  . LEU B 1 98  ? 10.736  2.857   -1.644  1.00 56.80  ? 98  LEU B CB  1 
ATOM   1399 C CG  . LEU B 1 98  ? 12.215  2.557   -1.880  1.00 71.68  ? 98  LEU B CG  1 
ATOM   1400 C CD1 . LEU B 1 98  ? 12.403  1.183   -2.489  1.00 57.30  ? 98  LEU B CD1 1 
ATOM   1401 C CD2 . LEU B 1 98  ? 12.820  3.648   -2.760  1.00 70.15  ? 98  LEU B CD2 1 
ATOM   1402 N N   . GLN B 1 99  ? 8.162   4.428   -0.218  1.00 72.11  ? 99  GLN B N   1 
ATOM   1403 C CA  . GLN B 1 99  ? 6.903   5.151   -0.355  1.00 64.99  ? 99  GLN B CA  1 
ATOM   1404 C C   . GLN B 1 99  ? 7.140   6.652   -0.323  1.00 76.06  ? 99  GLN B C   1 
ATOM   1405 O O   . GLN B 1 99  ? 6.648   7.396   -1.183  1.00 73.11  ? 99  GLN B O   1 
ATOM   1406 C CB  . GLN B 1 99  ? 5.947   4.747   0.764   1.00 70.87  ? 99  GLN B CB  1 
ATOM   1407 C CG  . GLN B 1 99  ? 4.494   4.759   0.358   1.00 87.14  ? 99  GLN B CG  1 
ATOM   1408 C CD  . GLN B 1 99  ? 4.021   3.379   -0.011  1.00 98.35  ? 99  GLN B CD  1 
ATOM   1409 O OE1 . GLN B 1 99  ? 4.272   2.413   0.717   1.00 95.79  ? 99  GLN B OE1 1 
ATOM   1410 N NE2 . GLN B 1 99  ? 3.335   3.270   -1.149  1.00 87.56  ? 99  GLN B NE2 1 
ATOM   1411 N N   . THR B 1 100 ? 7.914   7.108   0.667   1.00 75.71  ? 100 THR B N   1 
ATOM   1412 C CA  . THR B 1 100 ? 8.132   8.527   0.932   1.00 85.14  ? 100 THR B CA  1 
ATOM   1413 C C   . THR B 1 100 ? 9.402   9.069   0.272   1.00 85.78  ? 100 THR B C   1 
ATOM   1414 O O   . THR B 1 100 ? 9.452   10.254  -0.078  1.00 80.04  ? 100 THR B O   1 
ATOM   1415 C CB  . THR B 1 100 ? 8.162   8.755   2.452   1.00 93.17  ? 100 THR B CB  1 
ATOM   1416 O OG1 . THR B 1 100 ? 9.112   9.777   2.786   1.00 95.33  ? 100 THR B OG1 1 
ATOM   1417 C CG2 . THR B 1 100 ? 8.476   7.454   3.207   1.00 74.50  ? 100 THR B CG2 1 
ATOM   1418 N N   . GLU B 1 101 ? 10.426  8.232   0.077   1.00 77.61  ? 101 GLU B N   1 
ATOM   1419 C CA  . GLU B 1 101 ? 11.652  8.617   -0.624  1.00 79.82  ? 101 GLU B CA  1 
ATOM   1420 C C   . GLU B 1 101 ? 11.861  7.712   -1.835  1.00 80.08  ? 101 GLU B C   1 
ATOM   1421 O O   . GLU B 1 101 ? 12.694  6.794   -1.801  1.00 76.73  ? 101 GLU B O   1 
ATOM   1422 C CB  . GLU B 1 101 ? 12.872  8.550   0.289   1.00 88.24  ? 101 GLU B CB  1 
ATOM   1423 C CG  . GLU B 1 101 ? 13.329  9.879   0.828   1.00 88.88  ? 101 GLU B CG  1 
ATOM   1424 C CD  . GLU B 1 101 ? 14.184  9.713   2.060   1.00 95.52  ? 101 GLU B CD  1 
ATOM   1425 O OE1 . GLU B 1 101 ? 14.175  10.622  2.914   1.00 99.53  ? 101 GLU B OE1 1 
ATOM   1426 O OE2 . GLU B 1 101 ? 14.852  8.658   2.184   1.00 91.69  ? 101 GLU B OE2 1 
ATOM   1427 N N   . PRO B 1 102 ? 11.140  7.957   -2.927  1.00 84.87  ? 102 PRO B N   1 
ATOM   1428 C CA  . PRO B 1 102 ? 11.298  7.099   -4.113  1.00 81.56  ? 102 PRO B CA  1 
ATOM   1429 C C   . PRO B 1 102 ? 12.643  7.251   -4.804  1.00 81.44  ? 102 PRO B C   1 
ATOM   1430 O O   . PRO B 1 102 ? 13.056  6.329   -5.514  1.00 77.90  ? 102 PRO B O   1 
ATOM   1431 C CB  . PRO B 1 102 ? 10.152  7.555   -5.024  1.00 93.68  ? 102 PRO B CB  1 
ATOM   1432 C CG  . PRO B 1 102 ? 9.923   8.983   -4.626  1.00 80.81  ? 102 PRO B CG  1 
ATOM   1433 C CD  . PRO B 1 102 ? 10.170  9.042   -3.146  1.00 77.77  ? 102 PRO B CD  1 
ATOM   1434 N N   . GLN B 1 103 ? 13.328  8.380   -4.631  1.00 89.08  ? 103 GLN B N   1 
ATOM   1435 C CA  . GLN B 1 103 ? 14.635  8.621   -5.235  1.00 89.36  ? 103 GLN B CA  1 
ATOM   1436 C C   . GLN B 1 103 ? 15.782  8.108   -4.375  1.00 80.83  ? 103 GLN B C   1 
ATOM   1437 O O   . GLN B 1 103 ? 16.946  8.263   -4.760  1.00 72.33  ? 103 GLN B O   1 
ATOM   1438 C CB  . GLN B 1 103 ? 14.835  10.122  -5.495  1.00 86.12  ? 103 GLN B CB  1 
ATOM   1439 C CG  . GLN B 1 103 ? 13.563  10.877  -5.890  1.00 100.65 ? 103 GLN B CG  1 
ATOM   1440 C CD  . GLN B 1 103 ? 12.719  11.276  -4.680  1.00 108.45 ? 103 GLN B CD  1 
ATOM   1441 O OE1 . GLN B 1 103 ? 12.970  10.820  -3.557  1.00 101.48 ? 103 GLN B OE1 1 
ATOM   1442 N NE2 . GLN B 1 103 ? 11.710  12.123  -4.906  1.00 92.98  ? 103 GLN B NE2 1 
ATOM   1443 N N   . ASN B 1 104 ? 15.490  7.520   -3.219  1.00 68.24  ? 104 ASN B N   1 
ATOM   1444 C CA  . ASN B 1 104 ? 16.541  7.072   -2.320  1.00 60.64  ? 104 ASN B CA  1 
ATOM   1445 C C   . ASN B 1 104 ? 17.257  5.875   -2.938  1.00 65.08  ? 104 ASN B C   1 
ATOM   1446 O O   . ASN B 1 104 ? 16.649  4.824   -3.172  1.00 60.92  ? 104 ASN B O   1 
ATOM   1447 C CB  . ASN B 1 104 ? 15.945  6.738   -0.955  1.00 62.65  ? 104 ASN B CB  1 
ATOM   1448 C CG  . ASN B 1 104 ? 16.973  6.234   0.045   1.00 65.80  ? 104 ASN B CG  1 
ATOM   1449 O OD1 . ASN B 1 104 ? 18.064  5.791   -0.315  1.00 65.85  ? 104 ASN B OD1 1 
ATOM   1450 N ND2 . ASN B 1 104 ? 16.633  6.334   1.328   1.00 62.58  ? 104 ASN B ND2 1 
ATOM   1451 N N   . ASN B 1 105 ? 18.552  6.042   -3.206  1.00 56.60  ? 105 ASN B N   1 
ATOM   1452 C CA  . ASN B 1 105 ? 19.312  5.027   -3.932  1.00 60.74  ? 105 ASN B CA  1 
ATOM   1453 C C   . ASN B 1 105 ? 19.818  3.918   -3.021  1.00 63.94  ? 105 ASN B C   1 
ATOM   1454 O O   . ASN B 1 105 ? 19.973  2.773   -3.474  1.00 55.23  ? 105 ASN B O   1 
ATOM   1455 C CB  . ASN B 1 105 ? 20.491  5.667   -4.659  1.00 73.61  ? 105 ASN B CB  1 
ATOM   1456 C CG  . ASN B 1 105 ? 20.068  6.431   -5.891  1.00 67.73  ? 105 ASN B CG  1 
ATOM   1457 O OD1 . ASN B 1 105 ? 19.192  5.986   -6.637  1.00 75.94  ? 105 ASN B OD1 1 
ATOM   1458 N ND2 . ASN B 1 105 ? 20.718  7.565   -6.139  1.00 68.67  ? 105 ASN B ND2 1 
ATOM   1459 N N   . GLN B 1 106 ? 20.082  4.232   -1.747  1.00 57.26  ? 106 GLN B N   1 
ATOM   1460 C CA  . GLN B 1 106 ? 20.438  3.185   -0.794  1.00 59.59  ? 106 GLN B CA  1 
ATOM   1461 C C   . GLN B 1 106 ? 19.282  2.205   -0.618  1.00 61.50  ? 106 GLN B C   1 
ATOM   1462 O O   . GLN B 1 106 ? 19.482  0.984   -0.585  1.00 54.06  ? 106 GLN B O   1 
ATOM   1463 C CB  . GLN B 1 106 ? 20.819  3.782   0.567   1.00 70.45  ? 106 GLN B CB  1 
ATOM   1464 C CG  . GLN B 1 106 ? 21.121  5.278   0.618   1.00 76.52  ? 106 GLN B CG  1 
ATOM   1465 C CD  . GLN B 1 106 ? 22.234  5.681   -0.287  1.00 66.99  ? 106 GLN B CD  1 
ATOM   1466 O OE1 . GLN B 1 106 ? 23.307  5.080   -0.271  1.00 91.78  ? 106 GLN B OE1 1 
ATOM   1467 N NE2 . GLN B 1 106 ? 21.991  6.695   -1.105  1.00 80.96  ? 106 GLN B NE2 1 
ATOM   1468 N N   . ALA B 1 107 ? 18.060  2.735   -0.487  1.00 55.37  ? 107 ALA B N   1 
ATOM   1469 C CA  . ALA B 1 107 ? 16.889  1.887   -0.297  1.00 51.81  ? 107 ALA B CA  1 
ATOM   1470 C C   . ALA B 1 107 ? 16.593  1.067   -1.542  1.00 59.49  ? 107 ALA B C   1 
ATOM   1471 O O   . ALA B 1 107 ? 16.211  -0.102  -1.439  1.00 49.31  ? 107 ALA B O   1 
ATOM   1472 C CB  . ALA B 1 107 ? 15.677  2.737   0.073   1.00 52.09  ? 107 ALA B CB  1 
ATOM   1473 N N   . LYS B 1 108 ? 16.741  1.666   -2.727  1.00 53.29  ? 108 LYS B N   1 
ATOM   1474 C CA  . LYS B 1 108 ? 16.555  0.898   -3.949  1.00 49.87  ? 108 LYS B CA  1 
ATOM   1475 C C   . LYS B 1 108 ? 17.567  -0.241  -4.023  1.00 54.96  ? 108 LYS B C   1 
ATOM   1476 O O   . LYS B 1 108 ? 17.215  -1.384  -4.339  1.00 64.37  ? 108 LYS B O   1 
ATOM   1477 C CB  . LYS B 1 108 ? 16.677  1.810   -5.167  1.00 54.80  ? 108 LYS B CB  1 
ATOM   1478 C CG  . LYS B 1 108 ? 15.378  1.989   -5.924  1.00 63.00  ? 108 LYS B CG  1 
ATOM   1479 C CD  . LYS B 1 108 ? 15.347  3.340   -6.606  1.00 63.82  ? 108 LYS B CD  1 
ATOM   1480 C CE  . LYS B 1 108 ? 13.933  3.764   -6.968  1.00 83.54  ? 108 LYS B CE  1 
ATOM   1481 N NZ  . LYS B 1 108 ? 13.893  5.175   -7.497  1.00 89.06  ? 108 LYS B NZ  1 
ATOM   1482 N N   . GLU B 1 109 ? 18.831  0.055   -3.707  1.00 53.24  ? 109 GLU B N   1 
ATOM   1483 C CA  . GLU B 1 109 ? 19.887  -0.957  -3.746  1.00 51.79  ? 109 GLU B CA  1 
ATOM   1484 C C   . GLU B 1 109 ? 19.640  -2.064  -2.732  1.00 59.54  ? 109 GLU B C   1 
ATOM   1485 O O   . GLU B 1 109 ? 19.856  -3.247  -3.024  1.00 53.32  ? 109 GLU B O   1 
ATOM   1486 C CB  . GLU B 1 109 ? 21.238  -0.287  -3.495  1.00 68.30  ? 109 GLU B CB  1 
ATOM   1487 C CG  . GLU B 1 109 ? 22.495  -1.160  -3.625  1.00 77.96  ? 109 GLU B CG  1 
ATOM   1488 C CD  . GLU B 1 109 ? 22.457  -2.201  -4.730  1.00 73.16  ? 109 GLU B CD  1 
ATOM   1489 O OE1 . GLU B 1 109 ? 23.007  -3.299  -4.505  1.00 89.29  ? 109 GLU B OE1 1 
ATOM   1490 O OE2 . GLU B 1 109 ? 21.950  -1.918  -5.836  1.00 76.37  ? 109 GLU B OE2 1 
ATOM   1491 N N   . LEU B 1 110 ? 19.209  -1.705  -1.524  1.00 52.22  ? 110 LEU B N   1 
ATOM   1492 C CA  . LEU B 1 110 ? 18.943  -2.731  -0.527  1.00 54.52  ? 110 LEU B CA  1 
ATOM   1493 C C   . LEU B 1 110 ? 17.759  -3.592  -0.945  1.00 52.06  ? 110 LEU B C   1 
ATOM   1494 O O   . LEU B 1 110 ? 17.781  -4.814  -0.768  1.00 52.29  ? 110 LEU B O   1 
ATOM   1495 C CB  . LEU B 1 110 ? 18.714  -2.081  0.835   1.00 48.25  ? 110 LEU B CB  1 
ATOM   1496 C CG  . LEU B 1 110 ? 18.302  -3.005  1.968   1.00 58.84  ? 110 LEU B CG  1 
ATOM   1497 C CD1 . LEU B 1 110 ? 19.342  -4.090  2.182   1.00 57.15  ? 110 LEU B CD1 1 
ATOM   1498 C CD2 . LEU B 1 110 ? 18.141  -2.168  3.212   1.00 63.52  ? 110 LEU B CD2 1 
ATOM   1499 N N   . GLU B 1 111 ? 16.732  -2.981  -1.542  1.00 53.73  ? 111 GLU B N   1 
ATOM   1500 C CA  . GLU B 1 111 ? 15.608  -3.774  -2.031  1.00 54.70  ? 111 GLU B CA  1 
ATOM   1501 C C   . GLU B 1 111 ? 16.052  -4.753  -3.110  1.00 59.97  ? 111 GLU B C   1 
ATOM   1502 O O   . GLU B 1 111 ? 15.627  -5.915  -3.113  1.00 61.40  ? 111 GLU B O   1 
ATOM   1503 C CB  . GLU B 1 111 ? 14.501  -2.880  -2.579  1.00 59.59  ? 111 GLU B CB  1 
ATOM   1504 C CG  . GLU B 1 111 ? 13.205  -3.668  -2.804  1.00 72.00  ? 111 GLU B CG  1 
ATOM   1505 C CD  . GLU B 1 111 ? 12.142  -2.880  -3.532  1.00 68.31  ? 111 GLU B CD  1 
ATOM   1506 O OE1 . GLU B 1 111 ? 12.501  -1.915  -4.241  1.00 74.14  ? 111 GLU B OE1 1 
ATOM   1507 O OE2 . GLU B 1 111 ? 10.949  -3.234  -3.404  1.00 80.63  ? 111 GLU B OE2 1 
ATOM   1508 N N   . ARG B 1 112 ? 16.886  -4.292  -4.049  1.00 57.69  ? 112 ARG B N   1 
ATOM   1509 C CA  . ARG B 1 112 ? 17.456  -5.180  -5.062  1.00 56.62  ? 112 ARG B CA  1 
ATOM   1510 C C   . ARG B 1 112 ? 18.162  -6.366  -4.415  1.00 54.72  ? 112 ARG B C   1 
ATOM   1511 O O   . ARG B 1 112 ? 17.935  -7.521  -4.791  1.00 60.00  ? 112 ARG B O   1 
ATOM   1512 C CB  . ARG B 1 112 ? 18.423  -4.400  -5.964  1.00 61.51  ? 112 ARG B CB  1 
ATOM   1513 C CG  . ARG B 1 112 ? 18.645  -5.004  -7.353  1.00 70.42  ? 112 ARG B CG  1 
ATOM   1514 C CD  . ARG B 1 112 ? 19.714  -4.239  -8.126  1.00 59.88  ? 112 ARG B CD  1 
ATOM   1515 N NE  . ARG B 1 112 ? 21.017  -4.363  -7.485  1.00 74.53  ? 112 ARG B NE  1 
ATOM   1516 C CZ  . ARG B 1 112 ? 21.844  -5.390  -7.647  1.00 84.81  ? 112 ARG B CZ  1 
ATOM   1517 N NH1 . ARG B 1 112 ? 21.586  -6.359  -8.512  1.00 82.89  ? 112 ARG B NH1 1 
ATOM   1518 N NH2 . ARG B 1 112 ? 22.958  -5.445  -6.924  1.00 67.46  ? 112 ARG B NH2 1 
ATOM   1519 N N   . LEU B 1 113 ? 19.001  -6.096  -3.407  1.00 53.37  ? 113 LEU B N   1 
ATOM   1520 C CA  . LEU B 1 113 ? 19.714  -7.177  -2.732  1.00 58.16  ? 113 LEU B CA  1 
ATOM   1521 C C   . LEU B 1 113 ? 18.753  -8.130  -2.029  1.00 60.59  ? 113 LEU B C   1 
ATOM   1522 O O   . LEU B 1 113 ? 18.964  -9.350  -2.031  1.00 52.11  ? 113 LEU B O   1 
ATOM   1523 C CB  . LEU B 1 113 ? 20.731  -6.601  -1.741  1.00 59.04  ? 113 LEU B CB  1 
ATOM   1524 C CG  . LEU B 1 113 ? 21.972  -5.911  -2.327  1.00 66.25  ? 113 LEU B CG  1 
ATOM   1525 C CD1 . LEU B 1 113 ? 22.852  -5.326  -1.227  1.00 55.24  ? 113 LEU B CD1 1 
ATOM   1526 C CD2 . LEU B 1 113 ? 22.789  -6.878  -3.210  1.00 54.54  ? 113 LEU B CD2 1 
ATOM   1527 N N   . ILE B 1 114 ? 17.695  -7.600  -1.419  1.00 46.90  ? 114 ILE B N   1 
ATOM   1528 C CA  . ILE B 1 114 ? 16.717  -8.465  -0.771  1.00 61.08  ? 114 ILE B CA  1 
ATOM   1529 C C   . ILE B 1 114 ? 16.077  -9.391  -1.789  1.00 59.35  ? 114 ILE B C   1 
ATOM   1530 O O   . ILE B 1 114 ? 16.044  -10.611 -1.601  1.00 62.45  ? 114 ILE B O   1 
ATOM   1531 C CB  . ILE B 1 114 ? 15.657  -7.634  -0.035  1.00 57.98  ? 114 ILE B CB  1 
ATOM   1532 C CG1 . ILE B 1 114 ? 16.278  -6.983  1.195   1.00 52.16  ? 114 ILE B CG1 1 
ATOM   1533 C CG2 . ILE B 1 114 ? 14.496  -8.529  0.351   1.00 58.63  ? 114 ILE B CG2 1 
ATOM   1534 C CD1 . ILE B 1 114 ? 15.522  -5.762  1.659   1.00 48.88  ? 114 ILE B CD1 1 
ATOM   1535 N N   . ASP B 1 115 ? 15.562  -8.819  -2.883  1.00 58.94  ? 115 ASP B N   1 
ATOM   1536 C CA  . ASP B 1 115 ? 14.978  -9.611  -3.964  1.00 58.26  ? 115 ASP B CA  1 
ATOM   1537 C C   . ASP B 1 115 ? 15.883  -10.768 -4.348  1.00 56.99  ? 115 ASP B C   1 
ATOM   1538 O O   . ASP B 1 115 ? 15.432  -11.907 -4.488  1.00 61.59  ? 115 ASP B O   1 
ATOM   1539 C CB  . ASP B 1 115 ? 14.741  -8.733  -5.196  1.00 59.58  ? 115 ASP B CB  1 
ATOM   1540 C CG  . ASP B 1 115 ? 13.596  -7.754  -5.022  1.00 85.20  ? 115 ASP B CG  1 
ATOM   1541 O OD1 . ASP B 1 115 ? 12.783  -7.928  -4.082  1.00 77.02  ? 115 ASP B OD1 1 
ATOM   1542 O OD2 . ASP B 1 115 ? 13.510  -6.806  -5.843  1.00 83.07  ? 115 ASP B OD2 1 
ATOM   1543 N N   . LYS B 1 116 ? 17.172  -10.478 -4.536  1.00 61.06  ? 116 LYS B N   1 
ATOM   1544 C CA  . LYS B 1 116 ? 18.115  -11.475 -5.023  1.00 54.72  ? 116 LYS B CA  1 
ATOM   1545 C C   . LYS B 1 116 ? 18.366  -12.570 -3.998  1.00 54.33  ? 116 LYS B C   1 
ATOM   1546 O O   . LYS B 1 116 ? 18.417  -13.750 -4.356  1.00 62.88  ? 116 LYS B O   1 
ATOM   1547 C CB  . LYS B 1 116 ? 19.424  -10.802 -5.411  1.00 62.26  ? 116 LYS B CB  1 
ATOM   1548 C CG  . LYS B 1 116 ? 20.244  -11.604 -6.386  1.00 76.48  ? 116 LYS B CG  1 
ATOM   1549 C CD  . LYS B 1 116 ? 20.843  -10.701 -7.445  1.00 81.00  ? 116 LYS B CD  1 
ATOM   1550 C CE  . LYS B 1 116 ? 22.324  -10.528 -7.227  1.00 87.33  ? 116 LYS B CE  1 
ATOM   1551 N NZ  . LYS B 1 116 ? 22.900  -9.642  -8.269  1.00 84.61  ? 116 LYS B NZ  1 
ATOM   1552 N N   . ALA B 1 117 ? 18.548  -12.209 -2.724  1.00 58.38  ? 117 ALA B N   1 
ATOM   1553 C CA  . ALA B 1 117 ? 18.700  -13.236 -1.694  1.00 57.83  ? 117 ALA B CA  1 
ATOM   1554 C C   . ALA B 1 117 ? 17.446  -14.096 -1.583  1.00 57.42  ? 117 ALA B C   1 
ATOM   1555 O O   . ALA B 1 117 ? 17.528  -15.315 -1.374  1.00 60.90  ? 117 ALA B O   1 
ATOM   1556 C CB  . ALA B 1 117 ? 19.022  -12.591 -0.347  1.00 59.44  ? 117 ALA B CB  1 
ATOM   1557 N N   . MET B 1 118 ? 16.273  -13.479 -1.734  1.00 57.15  ? 118 MET B N   1 
ATOM   1558 C CA  . MET B 1 118 ? 15.020  -14.223 -1.637  1.00 57.00  ? 118 MET B CA  1 
ATOM   1559 C C   . MET B 1 118 ? 14.931  -15.279 -2.728  1.00 58.78  ? 118 MET B C   1 
ATOM   1560 O O   . MET B 1 118 ? 14.644  -16.451 -2.456  1.00 71.12  ? 118 MET B O   1 
ATOM   1561 C CB  . MET B 1 118 ? 13.844  -13.257 -1.736  1.00 63.70  ? 118 MET B CB  1 
ATOM   1562 C CG  . MET B 1 118 ? 13.421  -12.692 -0.399  1.00 76.30  ? 118 MET B CG  1 
ATOM   1563 S SD  . MET B 1 118 ? 11.847  -11.802 -0.443  1.00 76.68  ? 118 MET B SD  1 
ATOM   1564 C CE  . MET B 1 118 ? 11.899  -11.112 -2.098  1.00 80.48  ? 118 MET B CE  1 
ATOM   1565 N N   . LYS B 1 119 ? 15.192  -14.872 -3.975  1.00 58.08  ? 119 LYS B N   1 
ATOM   1566 C CA  . LYS B 1 119 ? 15.121  -15.785 -5.112  1.00 58.85  ? 119 LYS B CA  1 
ATOM   1567 C C   . LYS B 1 119 ? 16.065  -16.972 -4.933  1.00 73.46  ? 119 LYS B C   1 
ATOM   1568 O O   . LYS B 1 119 ? 15.706  -18.110 -5.255  1.00 71.91  ? 119 LYS B O   1 
ATOM   1569 C CB  . LYS B 1 119 ? 15.431  -15.027 -6.408  1.00 55.87  ? 119 LYS B CB  1 
ATOM   1570 C CG  . LYS B 1 119 ? 15.251  -15.858 -7.654  1.00 69.49  ? 119 LYS B CG  1 
ATOM   1571 C CD  . LYS B 1 119 ? 15.009  -15.037 -8.921  1.00 77.65  ? 119 LYS B CD  1 
ATOM   1572 C CE  . LYS B 1 119 ? 15.554  -15.784 -10.149 1.00 86.13  ? 119 LYS B CE  1 
ATOM   1573 N NZ  . LYS B 1 119 ? 15.280  -15.093 -11.445 1.00 83.44  ? 119 LYS B NZ  1 
ATOM   1574 N N   . LYS B 1 120 ? 17.274  -16.733 -4.410  1.00 61.44  ? 120 LYS B N   1 
ATOM   1575 C CA  . LYS B 1 120 ? 18.210  -17.838 -4.194  1.00 59.18  ? 120 LYS B CA  1 
ATOM   1576 C C   . LYS B 1 120 ? 17.761  -18.722 -3.034  1.00 68.82  ? 120 LYS B C   1 
ATOM   1577 O O   . LYS B 1 120 ? 17.925  -19.950 -3.080  1.00 69.10  ? 120 LYS B O   1 
ATOM   1578 C CB  . LYS B 1 120 ? 19.619  -17.291 -3.946  1.00 61.61  ? 120 LYS B CB  1 
ATOM   1579 C CG  . LYS B 1 120 ? 20.291  -16.764 -5.203  1.00 66.11  ? 120 LYS B CG  1 
ATOM   1580 C CD  . LYS B 1 120 ? 21.648  -16.137 -4.930  1.00 72.77  ? 120 LYS B CD  1 
ATOM   1581 C CE  . LYS B 1 120 ? 22.152  -15.430 -6.190  1.00 62.82  ? 120 LYS B CE  1 
ATOM   1582 N NZ  . LYS B 1 120 ? 23.183  -14.403 -5.895  1.00 76.64  ? 120 LYS B NZ  1 
ATOM   1583 N N   . ASP B 1 121 ? 17.198  -18.110 -1.986  1.00 62.00  ? 121 ASP B N   1 
ATOM   1584 C CA  . ASP B 1 121 ? 16.738  -18.855 -0.817  1.00 60.99  ? 121 ASP B CA  1 
ATOM   1585 C C   . ASP B 1 121 ? 15.542  -19.732 -1.150  1.00 79.30  ? 121 ASP B C   1 
ATOM   1586 O O   . ASP B 1 121 ? 15.443  -20.865 -0.663  1.00 83.93  ? 121 ASP B O   1 
ATOM   1587 C CB  . ASP B 1 121 ? 16.390  -17.890 0.313   1.00 54.90  ? 121 ASP B CB  1 
ATOM   1588 C CG  . ASP B 1 121 ? 17.413  -17.909 1.420   1.00 79.50  ? 121 ASP B CG  1 
ATOM   1589 O OD1 . ASP B 1 121 ? 18.483  -18.521 1.226   1.00 80.29  ? 121 ASP B OD1 1 
ATOM   1590 O OD2 . ASP B 1 121 ? 17.155  -17.309 2.483   1.00 80.31  ? 121 ASP B OD2 1 
ATOM   1591 N N   . GLY B 1 122 ? 14.614  -19.225 -1.964  1.00 79.19  ? 122 GLY B N   1 
ATOM   1592 C CA  . GLY B 1 122 ? 13.528  -20.069 -2.435  1.00 76.74  ? 122 GLY B CA  1 
ATOM   1593 C C   . GLY B 1 122 ? 14.035  -21.295 -3.170  1.00 79.56  ? 122 GLY B C   1 
ATOM   1594 O O   . GLY B 1 122 ? 13.572  -22.413 -2.933  1.00 91.88  ? 122 GLY B O   1 
ATOM   1595 N N   . LEU B 1 123 ? 15.003  -21.096 -4.069  1.00 77.47  ? 123 LEU B N   1 
ATOM   1596 C CA  . LEU B 1 123 ? 15.620  -22.208 -4.787  1.00 81.15  ? 123 LEU B CA  1 
ATOM   1597 C C   . LEU B 1 123 ? 16.170  -23.250 -3.817  1.00 93.15  ? 123 LEU B C   1 
ATOM   1598 O O   . LEU B 1 123 ? 15.911  -24.451 -3.964  1.00 86.92  ? 123 LEU B O   1 
ATOM   1599 C CB  . LEU B 1 123 ? 16.733  -21.676 -5.699  1.00 83.16  ? 123 LEU B CB  1 
ATOM   1600 C CG  . LEU B 1 123 ? 17.841  -22.613 -6.213  1.00 88.14  ? 123 LEU B CG  1 
ATOM   1601 C CD1 . LEU B 1 123 ? 17.312  -23.926 -6.786  1.00 87.91  ? 123 LEU B CD1 1 
ATOM   1602 C CD2 . LEU B 1 123 ? 18.730  -21.903 -7.223  1.00 87.00  ? 123 LEU B CD2 1 
ATOM   1603 N N   . LEU B 1 124 ? 16.944  -22.803 -2.823  1.00 79.23  ? 124 LEU B N   1 
ATOM   1604 C CA  . LEU B 1 124 ? 17.506  -23.729 -1.844  1.00 84.65  ? 124 LEU B CA  1 
ATOM   1605 C C   . LEU B 1 124 ? 16.413  -24.546 -1.170  1.00 88.58  ? 124 LEU B C   1 
ATOM   1606 O O   . LEU B 1 124 ? 16.591  -25.740 -0.912  1.00 94.89  ? 124 LEU B O   1 
ATOM   1607 C CB  . LEU B 1 124 ? 18.314  -22.961 -0.797  1.00 70.42  ? 124 LEU B CB  1 
ATOM   1608 C CG  . LEU B 1 124 ? 19.702  -22.446 -1.199  1.00 65.00  ? 124 LEU B CG  1 
ATOM   1609 C CD1 . LEU B 1 124 ? 20.383  -21.724 -0.038  1.00 64.43  ? 124 LEU B CD1 1 
ATOM   1610 C CD2 . LEU B 1 124 ? 20.572  -23.578 -1.715  1.00 61.89  ? 124 LEU B CD2 1 
ATOM   1611 N N   . GLU B 1 125 ? 15.265  -23.916 -0.900  1.00 98.11  ? 125 GLU B N   1 
ATOM   1612 C CA  . GLU B 1 125 ? 14.200  -24.561 -0.139  1.00 101.31 ? 125 GLU B CA  1 
ATOM   1613 C C   . GLU B 1 125 ? 13.683  -25.810 -0.838  1.00 104.59 ? 125 GLU B C   1 
ATOM   1614 O O   . GLU B 1 125 ? 13.348  -26.803 -0.182  1.00 115.23 ? 125 GLU B O   1 
ATOM   1615 C CB  . GLU B 1 125 ? 13.054  -23.572 0.082   1.00 98.01  ? 125 GLU B CB  1 
ATOM   1616 C CG  . GLU B 1 125 ? 12.517  -23.525 1.498   1.00 103.82 ? 125 GLU B CG  1 
ATOM   1617 C CD  . GLU B 1 125 ? 13.439  -22.787 2.448   1.00 111.07 ? 125 GLU B CD  1 
ATOM   1618 O OE1 . GLU B 1 125 ? 13.367  -21.538 2.502   1.00 112.69 ? 125 GLU B OE1 1 
ATOM   1619 O OE2 . GLU B 1 125 ? 14.235  -23.454 3.142   1.00 112.74 ? 125 GLU B OE2 1 
ATOM   1620 N N   . VAL B 1 126 ? 13.618  -25.785 -2.164  1.00 97.37  ? 126 VAL B N   1 
ATOM   1621 C CA  . VAL B 1 126 ? 12.871  -26.777 -2.922  1.00 96.77  ? 126 VAL B CA  1 
ATOM   1622 C C   . VAL B 1 126 ? 13.789  -27.666 -3.761  1.00 105.15 ? 126 VAL B C   1 
ATOM   1623 O O   . VAL B 1 126 ? 13.326  -28.324 -4.691  1.00 109.10 ? 126 VAL B O   1 
ATOM   1624 C CB  . VAL B 1 126 ? 11.800  -26.104 -3.795  1.00 101.08 ? 126 VAL B CB  1 
ATOM   1625 C CG1 . VAL B 1 126 ? 10.909  -25.214 -2.946  1.00 107.29 ? 126 VAL B CG1 1 
ATOM   1626 C CG2 . VAL B 1 126 ? 12.454  -25.282 -4.897  1.00 102.60 ? 126 VAL B CG2 1 
ATOM   1627 N N   . LEU B 1 127 ? 15.076  -27.718 -3.446  1.00 101.07 ? 127 LEU B N   1 
ATOM   1628 C CA  . LEU B 1 127 ? 15.994  -28.491 -4.278  1.00 103.29 ? 127 LEU B CA  1 
ATOM   1629 C C   . LEU B 1 127 ? 16.024  -29.972 -3.895  1.00 116.16 ? 127 LEU B C   1 
ATOM   1630 O O   . LEU B 1 127 ? 15.130  -30.472 -3.208  1.00 116.63 ? 127 LEU B O   1 
ATOM   1631 C CB  . LEU B 1 127 ? 17.400  -27.884 -4.216  1.00 98.08  ? 127 LEU B CB  1 
ATOM   1632 C CG  . LEU B 1 127 ? 18.458  -28.344 -3.216  1.00 96.88  ? 127 LEU B CG  1 
ATOM   1633 C CD1 . LEU B 1 127 ? 19.600  -27.350 -3.262  1.00 93.74  ? 127 LEU B CD1 1 
ATOM   1634 C CD2 . LEU B 1 127 ? 17.923  -28.445 -1.797  1.00 105.21 ? 127 LEU B CD2 1 
HETATM 1635 O O   . HOH C 2 .   ? -4.105  -16.399 22.162  1.00 59.29  ? 201 HOH A O   1 
HETATM 1636 O O   . HOH C 2 .   ? -10.079 1.237   8.916   1.00 61.71  ? 202 HOH A O   1 
HETATM 1637 O O   . HOH C 2 .   ? 7.517   -4.842  38.881  1.00 58.52  ? 203 HOH A O   1 
HETATM 1638 O O   . HOH C 2 .   ? 6.147   17.155  26.902  1.00 67.54  ? 204 HOH A O   1 
HETATM 1639 O O   . HOH C 2 .   ? -1.923  13.002  20.030  1.00 65.32  ? 205 HOH A O   1 
HETATM 1640 O O   . HOH C 2 .   ? 5.672   -4.251  19.864  1.00 58.70  ? 206 HOH A O   1 
HETATM 1641 O O   A HOH C 2 .   ? -14.859 1.768   22.735  0.37 64.86  ? 207 HOH A O   1 
HETATM 1642 O O   B HOH C 2 .   ? -15.541 3.546   22.408  0.63 64.86  ? 207 HOH A O   1 
HETATM 1643 O O   . HOH C 2 .   ? 5.211   2.149   38.808  1.00 69.30  ? 208 HOH A O   1 
HETATM 1644 O O   . HOH C 2 .   ? 1.788   -18.250 45.397  1.00 50.85  ? 209 HOH A O   1 
HETATM 1645 O O   . HOH C 2 .   ? -1.629  -4.801  36.111  1.00 46.16  ? 210 HOH A O   1 
HETATM 1646 O O   . HOH C 2 .   ? -3.807  4.759   31.588  1.00 50.42  ? 211 HOH A O   1 
HETATM 1647 O O   . HOH C 2 .   ? 5.091   -7.310  20.437  1.00 63.44  ? 212 HOH A O   1 
HETATM 1648 O O   . HOH C 2 .   ? 12.151  3.141   26.144  1.00 64.12  ? 213 HOH A O   1 
HETATM 1649 O O   . HOH C 2 .   ? -8.666  -13.311 23.573  1.00 50.81  ? 214 HOH A O   1 
HETATM 1650 O O   . HOH C 2 .   ? 8.014   8.725   35.546  1.00 54.68  ? 215 HOH A O   1 
HETATM 1651 O O   . HOH C 2 .   ? -1.077  6.113   38.374  1.00 51.58  ? 216 HOH A O   1 
HETATM 1652 O O   . HOH C 2 .   ? -1.075  -15.170 24.393  1.00 75.31  ? 217 HOH A O   1 
HETATM 1653 O O   . HOH C 2 .   ? 4.750   -15.198 38.371  1.00 54.11  ? 218 HOH A O   1 
HETATM 1654 O O   . HOH C 2 .   ? -17.625 -6.054  22.986  1.00 67.87  ? 219 HOH A O   1 
HETATM 1655 O O   . HOH C 2 .   ? 8.445   5.014   23.418  1.00 45.95  ? 220 HOH A O   1 
HETATM 1656 O O   . HOH C 2 .   ? 3.082   -0.988  40.141  1.00 57.01  ? 221 HOH A O   1 
HETATM 1657 O O   . HOH C 2 .   ? -12.452 -3.304  19.741  1.00 55.68  ? 222 HOH A O   1 
HETATM 1658 O O   . HOH C 2 .   ? 4.499   -11.945 35.993  1.00 53.40  ? 223 HOH A O   1 
HETATM 1659 O O   . HOH C 2 .   ? 2.994   -12.909 33.675  1.00 58.69  ? 224 HOH A O   1 
HETATM 1660 O O   . HOH C 2 .   ? -3.073  8.254   12.290  1.00 65.28  ? 225 HOH A O   1 
HETATM 1661 O O   . HOH C 2 .   ? 7.346   10.736  34.615  1.00 51.95  ? 226 HOH A O   1 
HETATM 1662 O O   . HOH C 2 .   ? 0.564   -10.910 35.583  1.00 49.10  ? 227 HOH A O   1 
HETATM 1663 O O   . HOH C 2 .   ? -2.496  11.704  28.061  1.00 49.24  ? 228 HOH A O   1 
HETATM 1664 O O   . HOH C 2 .   ? -7.650  -14.779 19.692  1.00 55.32  ? 229 HOH A O   1 
HETATM 1665 O O   . HOH C 2 .   ? 8.134   -8.293  26.152  1.00 53.73  ? 230 HOH A O   1 
HETATM 1666 O O   . HOH C 2 .   ? 11.707  -2.868  29.223  1.00 54.70  ? 231 HOH A O   1 
HETATM 1667 O O   . HOH C 2 .   ? 5.355   12.284  20.158  1.00 65.27  ? 232 HOH A O   1 
HETATM 1668 O O   . HOH C 2 .   ? 11.282  9.555   24.121  1.00 67.13  ? 233 HOH A O   1 
HETATM 1669 O O   . HOH C 2 .   ? -13.752 -7.141  20.893  1.00 53.76  ? 234 HOH A O   1 
HETATM 1670 O O   . HOH C 2 .   ? -6.359  5.354   29.213  1.00 70.24  ? 235 HOH A O   1 
HETATM 1671 O O   . HOH C 2 .   ? -4.409  -14.714 27.074  1.00 57.20  ? 236 HOH A O   1 
HETATM 1672 O O   . HOH C 2 .   ? 4.244   16.256  30.409  1.00 54.70  ? 237 HOH A O   1 
HETATM 1673 O O   . HOH C 2 .   ? -2.649  -16.256 34.244  1.00 61.05  ? 238 HOH A O   1 
HETATM 1674 O O   . HOH C 2 .   ? 8.425   -9.409  29.168  1.00 60.50  ? 239 HOH A O   1 
HETATM 1675 O O   . HOH C 2 .   ? -4.317  4.939   40.124  1.00 71.44  ? 240 HOH A O   1 
HETATM 1676 O O   . HOH C 2 .   ? 5.138   -4.252  11.615  1.00 62.16  ? 241 HOH A O   1 
HETATM 1677 O O   . HOH C 2 .   ? 0.708   -0.458  42.183  1.00 64.51  ? 242 HOH A O   1 
HETATM 1678 O O   . HOH C 2 .   ? -1.444  14.427  30.890  1.00 73.23  ? 243 HOH A O   1 
HETATM 1679 O O   . HOH C 2 .   ? 12.627  -0.470  30.357  1.00 62.90  ? 244 HOH A O   1 
HETATM 1680 O O   . HOH C 2 .   ? -1.287  -9.939  37.013  1.00 54.70  ? 245 HOH A O   1 
HETATM 1681 O O   . HOH C 2 .   ? -13.577 -0.904  21.733  1.00 84.97  ? 246 HOH A O   1 
HETATM 1682 O O   . HOH C 2 .   ? 9.284   -7.294  38.743  1.00 63.45  ? 247 HOH A O   1 
HETATM 1683 O O   . HOH C 2 .   ? 6.351   9.743   22.756  1.00 69.31  ? 248 HOH A O   1 
HETATM 1684 O O   . HOH C 2 .   ? -0.058  -2.771  43.990  1.00 71.85  ? 249 HOH A O   1 
HETATM 1685 O O   . HOH D 2 .   ? 14.747  -6.229  -7.785  1.00 79.78  ? 201 HOH B O   1 
HETATM 1686 O O   . HOH D 2 .   ? 16.863  6.041   -7.384  1.00 68.68  ? 202 HOH B O   1 
HETATM 1687 O O   . HOH D 2 .   ? 13.165  -3.164  21.080  1.00 56.86  ? 203 HOH B O   1 
HETATM 1688 O O   . HOH D 2 .   ? 15.063  -16.565 -13.469 1.00 76.27  ? 204 HOH B O   1 
HETATM 1689 O O   . HOH D 2 .   ? 25.215  -16.066 17.440  1.00 73.37  ? 205 HOH B O   1 
HETATM 1690 O O   . HOH D 2 .   ? 12.278  -5.376  13.133  1.00 62.74  ? 206 HOH B O   1 
HETATM 1691 O O   . HOH D 2 .   ? 10.187  13.126  -3.052  1.00 81.85  ? 207 HOH B O   1 
HETATM 1692 O O   . HOH D 2 .   ? 9.479   1.673   6.347   1.00 58.39  ? 208 HOH B O   1 
HETATM 1693 O O   . HOH D 2 .   ? 13.147  -9.055  13.254  1.00 56.90  ? 209 HOH B O   1 
HETATM 1694 O O   . HOH D 2 .   ? 22.343  1.689   15.101  1.00 81.01  ? 210 HOH B O   1 
HETATM 1695 O O   . HOH D 2 .   ? 30.136  -8.099  17.002  1.00 71.40  ? 211 HOH B O   1 
HETATM 1696 O O   . HOH D 2 .   ? 26.810  2.381   8.127   1.00 83.37  ? 212 HOH B O   1 
HETATM 1697 O O   . HOH D 2 .   ? 15.834  -8.844  17.451  1.00 59.42  ? 213 HOH B O   1 
HETATM 1698 O O   . HOH D 2 .   ? 29.186  2.824   16.002  1.00 51.80  ? 214 HOH B O   1 
HETATM 1699 O O   . HOH D 2 .   ? 26.656  -0.829  10.831  1.00 85.82  ? 215 HOH B O   1 
HETATM 1700 O O   . HOH D 2 .   ? 27.045  8.223   23.004  1.00 53.30  ? 216 HOH B O   1 
HETATM 1701 O O   . HOH D 2 .   ? 20.545  8.579   -2.487  1.00 60.81  ? 217 HOH B O   1 
HETATM 1702 O O   . HOH D 2 .   ? 10.748  -6.097  -4.707  1.00 86.17  ? 218 HOH B O   1 
HETATM 1703 O O   . HOH D 2 .   ? 21.575  -10.437 -2.324  1.00 64.82  ? 219 HOH B O   1 
HETATM 1704 O O   . HOH D 2 .   ? 13.315  7.916   -8.110  1.00 83.13  ? 220 HOH B O   1 
HETATM 1705 O O   . HOH D 2 .   ? 19.904  -13.157 20.871  1.00 87.89  ? 221 HOH B O   1 
HETATM 1706 O O   . HOH D 2 .   ? 28.603  5.622   26.134  1.00 62.35  ? 222 HOH B O   1 
HETATM 1707 O O   . HOH D 2 .   ? 11.515  15.556  13.577  1.00 82.57  ? 223 HOH B O   1 
HETATM 1708 O O   . HOH D 2 .   ? 9.420   -6.633  16.803  1.00 72.47  ? 224 HOH B O   1 
HETATM 1709 O O   . HOH D 2 .   ? 16.165  -32.335 -1.191  1.00 81.64  ? 225 HOH B O   1 
HETATM 1710 O O   . HOH D 2 .   ? 30.850  -4.628  14.421  1.00 70.08  ? 226 HOH B O   1 
HETATM 1711 O O   . HOH D 2 .   ? 15.751  8.018   19.318  1.00 75.65  ? 227 HOH B O   1 
HETATM 1712 O O   . HOH D 2 .   ? 25.595  -3.001  -2.946  1.00 64.15  ? 228 HOH B O   1 
HETATM 1713 O O   . HOH D 2 .   ? 14.934  -2.146  -6.292  1.00 61.82  ? 229 HOH B O   1 
HETATM 1714 O O   . HOH D 2 .   ? 8.734   7.706   22.601  1.00 61.64  ? 230 HOH B O   1 
HETATM 1715 O O   . HOH D 2 .   ? 31.886  -1.143  12.852  1.00 87.39  ? 231 HOH B O   1 
HETATM 1716 O O   . HOH D 2 .   ? 14.058  17.723  13.723  1.00 82.52  ? 232 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 31  ? 1.0204 1.3395 0.5934 -0.0870 -0.0431 0.2153  31  SER A N   
2    C CA  . SER A 31  ? 1.1361 1.4421 0.7532 -0.0830 -0.0432 0.2501  31  SER A CA  
3    C C   . SER A 31  ? 1.1520 1.4295 0.8262 -0.0651 -0.0301 0.2285  31  SER A C   
4    O O   . SER A 31  ? 0.9710 1.2371 0.6545 -0.0548 -0.0258 0.1922  31  SER A O   
5    C CB  . SER A 31  ? 1.1536 1.4526 0.7913 -0.0834 -0.0770 0.2903  31  SER A CB  
6    O OG  . SER A 31  ? 1.1353 1.4088 0.8274 -0.0655 -0.0899 0.2787  31  SER A OG  
7    N N   . LYS A 32  ? 1.2044 1.4695 0.9152 -0.0633 -0.0252 0.2522  32  LYS A N   
8    C CA  . LYS A 32  ? 1.1304 1.3705 0.8916 -0.0489 -0.0144 0.2338  32  LYS A CA  
9    C C   . LYS A 32  ? 0.9977 1.2116 0.7973 -0.0344 -0.0338 0.2261  32  LYS A C   
10   O O   . LYS A 32  ? 0.9247 1.1242 0.7462 -0.0230 -0.0262 0.1961  32  LYS A O   
11   C CB  . LYS A 32  ? 1.1054 1.3386 0.8944 -0.0540 -0.0072 0.2614  32  LYS A CB  
12   C CG  . LYS A 32  ? 1.1341 1.3898 0.9134 -0.0611 0.0221  0.2524  32  LYS A CG  
13   C CD  . LYS A 32  ? 1.0794 1.3242 0.8975 -0.0668 0.0260  0.2773  32  LYS A CD  
14   C CE  . LYS A 32  ? 1.1181 1.3429 0.9470 -0.0738 0.0013  0.3196  32  LYS A CE  
15   N NZ  . LYS A 32  ? 1.1023 1.2957 0.9825 -0.0726 -0.0032 0.3330  32  LYS A NZ  
16   N N   . SER A 33  ? 1.0283 1.2375 0.8386 -0.0343 -0.0586 0.2541  33  SER A N   
17   C CA  . SER A 33  ? 1.0399 1.2291 0.8927 -0.0193 -0.0744 0.2475  33  SER A CA  
18   C C   . SER A 33  ? 0.9699 1.1677 0.8105 -0.0160 -0.0770 0.2155  33  SER A C   
19   O O   . SER A 33  ? 0.9135 1.0960 0.7848 -0.0047 -0.0743 0.1931  33  SER A O   
20   C CB  . SER A 33  ? 1.0752 1.2610 0.9461 -0.0179 -0.1005 0.2853  33  SER A CB  
21   O OG  . SER A 33  ? 1.1580 1.3711 0.9852 -0.0311 -0.1144 0.3044  33  SER A OG  
22   N N   . THR A 34  ? 0.8204 1.0422 0.6138 -0.0279 -0.0821 0.2123  34  THR A N   
23   C CA  . THR A 34  ? 0.9841 1.2115 0.7660 -0.0280 -0.0878 0.1830  34  THR A CA  
24   C C   . THR A 34  ? 1.0857 1.3027 0.8575 -0.0255 -0.0642 0.1441  34  THR A C   
25   O O   . THR A 34  ? 0.8262 1.0340 0.6092 -0.0215 -0.0665 0.1191  34  THR A O   
26   C CB  . THR A 34  ? 1.1062 1.3610 0.8400 -0.0434 -0.1047 0.1915  34  THR A CB  
27   O OG1 . THR A 34  ? 1.1435 1.4098 0.8232 -0.0547 -0.0859 0.1741  34  THR A OG1 
28   C CG2 . THR A 34  ? 0.8544 1.1208 0.5917 -0.0473 -0.1264 0.2378  34  THR A CG2 
29   N N   . GLN A 35  ? 0.9883 1.2073 0.7435 -0.0275 -0.0417 0.1398  35  GLN A N   
30   C CA  . GLN A 35  ? 0.7818 0.9887 0.5405 -0.0204 -0.0205 0.1056  35  GLN A CA  
31   C C   . GLN A 35  ? 0.7782 0.9604 0.5883 -0.0071 -0.0189 0.1010  35  GLN A C   
32   O O   . GLN A 35  ? 0.6788 0.8462 0.4986 -0.0009 -0.0146 0.0748  35  GLN A O   
33   C CB  . GLN A 35  ? 0.7912 1.0122 0.5285 -0.0237 0.0039  0.1032  35  GLN A CB  
34   C CG  . GLN A 35  ? 0.9886 1.2308 0.6687 -0.0341 0.0117  0.0866  35  GLN A CG  
35   C CD  . GLN A 35  ? 1.1488 1.4101 0.8127 -0.0353 0.0403  0.0810  35  GLN A CD  
36   O OE1 . GLN A 35  ? 1.1115 1.3914 0.7725 -0.0435 0.0456  0.1107  35  GLN A OE1 
37   N NE2 . GLN A 35  ? 1.1139 1.3710 0.7712 -0.0269 0.0593  0.0436  35  GLN A NE2 
38   N N   . PHE A 36  ? 0.6580 0.8335 0.4992 -0.0036 -0.0227 0.1261  36  PHE A N   
39   C CA  . PHE A 36  ? 0.6917 0.8445 0.5768 0.0076  -0.0226 0.1200  36  PHE A CA  
40   C C   . PHE A 36  ? 0.5728 0.7198 0.4733 0.0123  -0.0375 0.1115  36  PHE A C   
41   O O   . PHE A 36  ? 0.5933 0.7263 0.5122 0.0186  -0.0330 0.0923  36  PHE A O   
42   C CB  . PHE A 36  ? 0.6637 0.8069 0.5777 0.0093  -0.0257 0.1461  36  PHE A CB  
43   C CG  . PHE A 36  ? 0.7151 0.8350 0.6689 0.0197  -0.0251 0.1368  36  PHE A CG  
44   C CD1 . PHE A 36  ? 0.5734 0.6853 0.5349 0.0231  -0.0110 0.1166  36  PHE A CD1 
45   C CD2 . PHE A 36  ? 0.7150 0.8229 0.6980 0.0268  -0.0391 0.1470  36  PHE A CD2 
46   C CE1 . PHE A 36  ? 0.7042 0.7965 0.6957 0.0304  -0.0116 0.1080  36  PHE A CE1 
47   C CE2 . PHE A 36  ? 0.5942 0.6823 0.6082 0.0356  -0.0368 0.1351  36  PHE A CE2 
48   C CZ  . PHE A 36  ? 0.6295 0.7100 0.6448 0.0360  -0.0234 0.1160  36  PHE A CZ  
49   N N   . GLU A 37  ? 0.6585 0.8190 0.5532 0.0083  -0.0558 0.1275  37  GLU A N   
50   C CA  . GLU A 37  ? 0.7766 0.9398 0.6900 0.0115  -0.0697 0.1199  37  GLU A CA  
51   C C   . GLU A 37  ? 0.6446 0.8064 0.5388 0.0063  -0.0643 0.0899  37  GLU A C   
52   O O   . GLU A 37  ? 0.6201 0.7743 0.5374 0.0099  -0.0652 0.0766  37  GLU A O   
53   C CB  . GLU A 37  ? 0.7558 0.9401 0.6665 0.0072  -0.0924 0.1433  37  GLU A CB  
54   C CG  . GLU A 37  ? 0.9316 1.1107 0.8763 0.0163  -0.1024 0.1732  37  GLU A CG  
55   C CD  . GLU A 37  ? 0.9613 1.1623 0.8992 0.0117  -0.1268 0.2022  37  GLU A CD  
56   O OE1 . GLU A 37  ? 0.9148 1.1371 0.8118 -0.0018 -0.1347 0.2006  37  GLU A OE1 
57   O OE2 . GLU A 37  ? 1.1535 1.3495 1.1278 0.0220  -0.1393 0.2262  37  GLU A OE2 
58   N N   . GLU A 38  ? 0.6885 0.8558 0.5404 -0.0025 -0.0573 0.0781  38  GLU A N   
59   C CA  . GLU A 38  ? 0.6838 0.8412 0.5200 -0.0062 -0.0518 0.0474  38  GLU A CA  
60   C C   . GLU A 38  ? 0.6862 0.8202 0.5428 0.0036  -0.0347 0.0319  38  GLU A C   
61   O O   . GLU A 38  ? 0.6926 0.8123 0.5612 0.0040  -0.0356 0.0159  38  GLU A O   
62   C CB  . GLU A 38  ? 0.8660 1.0324 0.6516 -0.0164 -0.0473 0.0337  38  GLU A CB  
63   C CG  . GLU A 38  ? 0.8882 1.0370 0.6605 -0.0198 -0.0436 0.0001  38  GLU A CG  
64   C CD  . GLU A 38  ? 1.0858 1.2386 0.8071 -0.0282 -0.0366 -0.0212 38  GLU A CD  
65   O OE1 . GLU A 38  ? 0.8811 1.0530 0.5756 -0.0304 -0.0288 -0.0110 38  GLU A OE1 
66   O OE2 . GLU A 38  ? 1.0311 1.1669 0.7386 -0.0333 -0.0380 -0.0492 38  GLU A OE2 
67   N N   . ALA A 39  ? 0.5980 0.7293 0.4597 0.0099  -0.0205 0.0385  39  ALA A N   
68   C CA  . ALA A 39  ? 0.6237 0.7364 0.5063 0.0188  -0.0074 0.0262  39  ALA A CA  
69   C C   . ALA A 39  ? 0.5880 0.6888 0.5056 0.0238  -0.0140 0.0306  39  ALA A C   
70   O O   . ALA A 39  ? 0.6056 0.6906 0.5339 0.0269  -0.0102 0.0167  39  ALA A O   
71   C CB  . ALA A 39  ? 0.5611 0.6799 0.4474 0.0226  0.0069  0.0353  39  ALA A CB  
72   N N   . TRP A 40  ? 0.5303 0.6384 0.4659 0.0250  -0.0237 0.0501  40  TRP A N   
73   C CA  . TRP A 40  ? 0.5616 0.6617 0.5292 0.0305  -0.0279 0.0509  40  TRP A CA  
74   C C   . TRP A 40  ? 0.5698 0.6695 0.5377 0.0262  -0.0326 0.0359  40  TRP A C   
75   O O   . TRP A 40  ? 0.5622 0.6497 0.5430 0.0281  -0.0275 0.0261  40  TRP A O   
76   C CB  . TRP A 40  ? 0.5459 0.6548 0.5334 0.0341  -0.0389 0.0719  40  TRP A CB  
77   C CG  . TRP A 40  ? 0.6997 0.8017 0.7216 0.0423  -0.0400 0.0709  40  TRP A CG  
78   C CD1 . TRP A 40  ? 0.6677 0.7534 0.7086 0.0489  -0.0334 0.0717  40  TRP A CD1 
79   C CD2 . TRP A 40  ? 0.5697 0.6837 0.6117 0.0444  -0.0474 0.0677  40  TRP A CD2 
80   N NE1 . TRP A 40  ? 0.7312 0.8161 0.7988 0.0559  -0.0348 0.0666  40  TRP A NE1 
81   C CE2 . TRP A 40  ? 0.7432 0.8477 0.8143 0.0539  -0.0422 0.0649  40  TRP A CE2 
82   C CE3 . TRP A 40  ? 0.6349 0.7691 0.6740 0.0380  -0.0576 0.0660  40  TRP A CE3 
83   C CZ2 . TRP A 40  ? 0.5480 0.6656 0.6463 0.0590  -0.0441 0.0602  40  TRP A CZ2 
84   C CZ3 . TRP A 40  ? 0.7399 0.8888 0.8102 0.0417  -0.0614 0.0638  40  TRP A CZ3 
85   C CH2 . TRP A 40  ? 0.6498 0.7917 0.7497 0.0530  -0.0531 0.0608  40  TRP A CH2 
86   N N   . CYS A 41  ? 0.5172 0.6310 0.4688 0.0179  -0.0431 0.0349  41  CYS A N   
87   C CA  . CYS A 41  ? 0.5722 0.6863 0.5243 0.0097  -0.0488 0.0214  41  CYS A CA  
88   C C   . CYS A 41  ? 0.6538 0.7439 0.5912 0.0073  -0.0388 0.0015  41  CYS A C   
89   O O   . CYS A 41  ? 0.5248 0.6044 0.4749 0.0045  -0.0379 -0.0058 41  CYS A O   
90   C CB  . CYS A 41  ? 0.4729 0.6068 0.4068 -0.0014 -0.0641 0.0233  41  CYS A CB  
91   S SG  . CYS A 41  ? 0.6568 0.8212 0.6145 0.0024  -0.0812 0.0505  41  CYS A SG  
92   N N   . LEU A 42  ? 0.5581 0.6401 0.4705 0.0089  -0.0307 -0.0065 42  LEU A N   
93   C CA  . LEU A 42  ? 0.6103 0.6684 0.5109 0.0088  -0.0229 -0.0267 42  LEU A CA  
94   C C   . LEU A 42  ? 0.5215 0.5622 0.4448 0.0172  -0.0149 -0.0261 42  LEU A C   
95   O O   . LEU A 42  ? 0.6136 0.6346 0.5402 0.0141  -0.0157 -0.0355 42  LEU A O   
96   C CB  . LEU A 42  ? 0.5554 0.6145 0.4285 0.0118  -0.0132 -0.0362 42  LEU A CB  
97   C CG  . LEU A 42  ? 0.6455 0.7204 0.4860 0.0008  -0.0215 -0.0402 42  LEU A CG  
98   C CD1 . LEU A 42  ? 0.6937 0.7730 0.5062 0.0046  -0.0072 -0.0502 42  LEU A CD1 
99   C CD2 . LEU A 42  ? 0.6746 0.7362 0.5038 -0.0114 -0.0324 -0.0582 42  LEU A CD2 
100  N N   . VAL A 43  ? 0.5503 0.5971 0.4882 0.0259  -0.0088 -0.0139 43  VAL A N   
101  C CA  . VAL A 43  ? 0.5848 0.6184 0.5410 0.0324  -0.0032 -0.0128 43  VAL A CA  
102  C C   . VAL A 43  ? 0.6684 0.6984 0.6400 0.0282  -0.0085 -0.0097 43  VAL A C   
103  O O   . VAL A 43  ? 0.5648 0.5809 0.5436 0.0296  -0.0061 -0.0113 43  VAL A O   
104  C CB  . VAL A 43  ? 0.6864 0.7300 0.6529 0.0391  0.0027  -0.0009 43  VAL A CB  
105  C CG1 . VAL A 43  ? 0.8466 0.8832 0.8340 0.0423  0.0030  0.0044  43  VAL A CG1 
106  C CG2 . VAL A 43  ? 0.6751 0.7205 0.6328 0.0442  0.0129  -0.0068 43  VAL A CG2 
107  N N   . ARG A 44  ? 0.5511 0.5965 0.5286 0.0230  -0.0154 -0.0046 44  ARG A N   
108  C CA  . ARG A 44  ? 0.5180 0.5677 0.5114 0.0184  -0.0177 -0.0031 44  ARG A CA  
109  C C   . ARG A 44  ? 0.6201 0.6667 0.6069 0.0056  -0.0233 -0.0106 44  ARG A C   
110  O O   . ARG A 44  ? 0.5529 0.6074 0.5531 -0.0012 -0.0240 -0.0087 44  ARG A O   
111  C CB  . ARG A 44  ? 0.4652 0.5375 0.4778 0.0223  -0.0214 0.0069  44  ARG A CB  
112  C CG  . ARG A 44  ? 0.6705 0.7395 0.6962 0.0328  -0.0162 0.0133  44  ARG A CG  
113  C CD  . ARG A 44  ? 0.8087 0.8926 0.8490 0.0389  -0.0222 0.0252  44  ARG A CD  
114  N NE  . ARG A 44  ? 0.6317 0.7334 0.6966 0.0411  -0.0256 0.0266  44  ARG A NE  
115  C CZ  . ARG A 44  ? 0.8685 0.9702 0.9530 0.0469  -0.0187 0.0221  44  ARG A CZ  
116  N NH1 . ARG A 44  ? 0.9059 0.9887 0.9858 0.0497  -0.0109 0.0169  44  ARG A NH1 
117  N NH2 . ARG A 44  ? 0.8455 0.9694 0.9557 0.0502  -0.0198 0.0220  44  ARG A NH2 
118  N N   . SER A 45  ? 0.5303 0.5657 0.4970 0.0009  -0.0266 -0.0200 45  SER A N   
119  C CA  . SER A 45  ? 0.5591 0.5883 0.5190 -0.0140 -0.0343 -0.0283 45  SER A CA  
120  C C   . SER A 45  ? 0.5250 0.5303 0.4890 -0.0198 -0.0319 -0.0303 45  SER A C   
121  O O   . SER A 45  ? 0.6069 0.5950 0.5716 -0.0108 -0.0252 -0.0287 45  SER A O   
122  C CB  . SER A 45  ? 0.5506 0.5677 0.4839 -0.0167 -0.0374 -0.0423 45  SER A CB  
123  O OG  . SER A 45  ? 0.6042 0.6075 0.5293 -0.0327 -0.0460 -0.0534 45  SER A OG  
124  N N   . LYS A 46  ? 0.6984 0.7031 0.6651 -0.0366 -0.0390 -0.0321 46  LYS A N   
125  C CA  . LYS A 46  ? 0.6210 0.5998 0.5886 -0.0465 -0.0388 -0.0312 46  LYS A CA  
126  C C   . LYS A 46  ? 0.5638 0.5015 0.5139 -0.0465 -0.0417 -0.0444 46  LYS A C   
127  O O   . LYS A 46  ? 0.6772 0.5857 0.6283 -0.0520 -0.0430 -0.0418 46  LYS A O   
128  C CB  . LYS A 46  ? 0.5624 0.5577 0.5424 -0.0677 -0.0448 -0.0263 46  LYS A CB  
129  C CG  . LYS A 46  ? 0.5953 0.6019 0.5712 -0.0802 -0.0565 -0.0348 46  LYS A CG  
130  C CD  . LYS A 46  ? 0.7161 0.7364 0.7071 -0.1048 -0.0638 -0.0303 46  LYS A CD  
131  C CE  . LYS A 46  ? 0.6603 0.7302 0.6804 -0.1037 -0.0590 -0.0174 46  LYS A CE  
132  N NZ  . LYS A 46  ? 0.8063 0.9095 0.8339 -0.0925 -0.0644 -0.0172 46  LYS A NZ  
133  N N   . TYR A 47  ? 0.6042 0.5387 0.5383 -0.0403 -0.0426 -0.0584 47  TYR A N   
134  C CA  . TYR A 47  ? 0.6192 0.5160 0.5365 -0.0390 -0.0438 -0.0768 47  TYR A CA  
135  C C   . TYR A 47  ? 0.7026 0.5898 0.6176 -0.0164 -0.0326 -0.0816 47  TYR A C   
136  O O   . TYR A 47  ? 0.6682 0.5819 0.5802 -0.0060 -0.0260 -0.0793 47  TYR A O   
137  C CB  . TYR A 47  ? 0.6030 0.5058 0.4999 -0.0499 -0.0515 -0.0933 47  TYR A CB  
138  C CG  . TYR A 47  ? 0.6546 0.5640 0.5568 -0.0750 -0.0652 -0.0910 47  TYR A CG  
139  C CD1 . TYR A 47  ? 0.6510 0.5221 0.5519 -0.0908 -0.0725 -0.0991 47  TYR A CD1 
140  C CD2 . TYR A 47  ? 0.7131 0.6678 0.6264 -0.0831 -0.0713 -0.0791 47  TYR A CD2 
141  C CE1 . TYR A 47  ? 0.7462 0.6269 0.6555 -0.1172 -0.0852 -0.0954 47  TYR A CE1 
142  C CE2 . TYR A 47  ? 0.6796 0.6481 0.6043 -0.1064 -0.0836 -0.0759 47  TYR A CE2 
143  C CZ  . TYR A 47  ? 0.7568 0.6897 0.6790 -0.1249 -0.0902 -0.0840 47  TYR A CZ  
144  O OH  . TYR A 47  ? 0.8467 0.7967 0.7832 -0.1512 -0.1026 -0.0795 47  TYR A OH  
145  N N   . ASN A 48  ? 0.6339 0.4839 0.5530 -0.0093 -0.0312 -0.0869 48  ASN A N   
146  C CA  . ASN A 48  ? 0.7497 0.5951 0.6745 0.0130  -0.0209 -0.0904 48  ASN A CA  
147  C C   . ASN A 48  ? 0.6322 0.4876 0.5392 0.0217  -0.0123 -0.1103 48  ASN A C   
148  O O   . ASN A 48  ? 0.6738 0.5529 0.5849 0.0355  -0.0017 -0.1069 48  ASN A O   
149  C CB  . ASN A 48  ? 0.7519 0.5547 0.6885 0.0200  -0.0237 -0.0920 48  ASN A CB  
150  C CG  . ASN A 48  ? 0.6574 0.4577 0.6096 0.0149  -0.0297 -0.0672 48  ASN A CG  
151  O OD1 . ASN A 48  ? 0.6498 0.4819 0.6052 0.0102  -0.0283 -0.0523 48  ASN A OD1 
152  N ND2 . ASN A 48  ? 0.6824 0.4432 0.6427 0.0156  -0.0367 -0.0631 48  ASN A ND2 
153  N N   . ASP A 49  ? 0.8199 0.6584 0.7055 0.0121  -0.0165 -0.1313 49  ASP A N   
154  C CA  . ASP A 49  ? 0.7715 0.6235 0.6315 0.0168  -0.0082 -0.1514 49  ASP A CA  
155  C C   . ASP A 49  ? 0.8471 0.7470 0.7016 0.0162  -0.0047 -0.1358 49  ASP A C   
156  O O   . ASP A 49  ? 0.7408 0.6601 0.5889 0.0283  0.0084  -0.1386 49  ASP A O   
157  C CB  . ASP A 49  ? 0.8377 0.6713 0.6703 -0.0008 -0.0179 -0.1739 49  ASP A CB  
158  C CG  . ASP A 49  ? 1.1625 0.9427 0.9949 0.0026  -0.0186 -0.1973 49  ASP A CG  
159  O OD1 . ASP A 49  ? 1.2816 1.0386 1.0953 -0.0153 -0.0297 -0.2149 49  ASP A OD1 
160  O OD2 . ASP A 49  ? 1.2475 1.0082 1.1000 0.0230  -0.0094 -0.1986 49  ASP A OD2 
161  N N   . ASP A 50  ? 0.7746 0.6943 0.6335 0.0018  -0.0162 -0.1185 50  ASP A N   
162  C CA  . ASP A 50  ? 0.6556 0.6157 0.5137 0.0019  -0.0158 -0.1012 50  ASP A CA  
163  C C   . ASP A 50  ? 0.6173 0.5889 0.4944 0.0182  -0.0039 -0.0873 50  ASP A C   
164  O O   . ASP A 50  ? 0.6535 0.6479 0.5224 0.0238  0.0040  -0.0830 50  ASP A O   
165  C CB  . ASP A 50  ? 0.6244 0.6019 0.4968 -0.0114 -0.0291 -0.0843 50  ASP A CB  
166  C CG  . ASP A 50  ? 0.7167 0.6997 0.5717 -0.0301 -0.0435 -0.0931 50  ASP A CG  
167  O OD1 . ASP A 50  ? 0.7599 0.7393 0.5843 -0.0336 -0.0439 -0.1108 50  ASP A OD1 
168  O OD2 . ASP A 50  ? 0.7786 0.7731 0.6509 -0.0422 -0.0543 -0.0827 50  ASP A OD2 
169  N N   . ILE A 51  ? 0.6212 0.5785 0.5231 0.0233  -0.0037 -0.0786 51  ILE A N   
170  C CA  . ILE A 51  ? 0.6137 0.5822 0.5350 0.0357  0.0043  -0.0652 51  ILE A CA  
171  C C   . ILE A 51  ? 0.6217 0.5934 0.5403 0.0493  0.0177  -0.0752 51  ILE A C   
172  O O   . ILE A 51  ? 0.5964 0.5918 0.5216 0.0549  0.0253  -0.0650 51  ILE A O   
173  C CB  . ILE A 51  ? 0.6610 0.6120 0.6030 0.0371  0.0005  -0.0566 51  ILE A CB  
174  C CG1 . ILE A 51  ? 0.5440 0.4994 0.4896 0.0232  -0.0089 -0.0471 51  ILE A CG1 
175  C CG2 . ILE A 51  ? 0.5204 0.4837 0.4809 0.0484  0.0067  -0.0450 51  ILE A CG2 
176  C CD1 . ILE A 51  ? 0.6451 0.5836 0.6029 0.0203  -0.0123 -0.0391 51  ILE A CD1 
177  N N   A ARG A 52  ? 0.6390 0.5868 0.5508 0.0548  0.0214  -0.0955 52  ARG A N   
178  N N   B ARG A 52  ? 0.6254 0.5736 0.5366 0.0547  0.0215  -0.0957 52  ARG A N   
179  C CA  A ARG A 52  ? 0.6391 0.5940 0.5510 0.0697  0.0371  -0.1087 52  ARG A CA  
180  C CA  B ARG A 52  ? 0.6296 0.5855 0.5421 0.0700  0.0373  -0.1080 52  ARG A CA  
181  C C   A ARG A 52  ? 0.7262 0.7133 0.6131 0.0654  0.0456  -0.1103 52  ARG A C   
182  C C   B ARG A 52  ? 0.7065 0.6933 0.5929 0.0658  0.0463  -0.1115 52  ARG A C   
183  O O   A ARG A 52  ? 0.7106 0.7250 0.6062 0.0720  0.0573  -0.1012 52  ARG A O   
184  O O   B ARG A 52  ? 0.7171 0.7305 0.6108 0.0734  0.0592  -0.1052 52  ARG A O   
185  C CB  A ARG A 52  ? 0.6789 0.5989 0.5859 0.0770  0.0395  -0.1347 52  ARG A CB  
186  C CB  B ARG A 52  ? 0.6800 0.6008 0.5914 0.0787  0.0398  -0.1326 52  ARG A CB  
187  C CG  A ARG A 52  ? 0.6835 0.5686 0.6157 0.0820  0.0302  -0.1299 52  ARG A CG  
188  C CG  B ARG A 52  ? 0.6415 0.5357 0.5843 0.0883  0.0339  -0.1250 52  ARG A CG  
189  C CD  A ARG A 52  ? 0.8207 0.6627 0.7446 0.0847  0.0283  -0.1554 52  ARG A CD  
190  C CD  B ARG A 52  ? 0.7143 0.5713 0.6608 0.1007  0.0370  -0.1490 52  ARG A CD  
191  N NE  A ARG A 52  ? 0.7827 0.5873 0.7241 0.0813  0.0142  -0.1451 52  ARG A NE  
192  N NE  B ARG A 52  ? 0.8295 0.6451 0.7855 0.0944  0.0210  -0.1426 52  ARG A NE  
193  C CZ  A ARG A 52  ? 0.6964 0.4644 0.6259 0.0669  0.0025  -0.1533 52  ARG A CZ  
194  C CZ  B ARG A 52  ? 0.7304 0.5375 0.7129 0.0993  0.0131  -0.1218 52  ARG A CZ  
195  N NH1 A ARG A 52  ? 0.7278 0.4898 0.6285 0.0552  0.0020  -0.1751 52  ARG A NH1 
196  N NH1 B ARG A 52  ? 0.7106 0.5455 0.7164 0.1123  0.0186  -0.1084 52  ARG A NH1 
197  N NH2 A ARG A 52  ? 0.9126 0.6503 0.8584 0.0618  -0.0099 -0.1380 52  ARG A NH2 
198  N NH2 B ARG A 52  ? 0.7148 0.4861 0.6994 0.0887  -0.0016 -0.1132 52  ARG A NH2 
199  N N   . LYS A 53  ? 0.7118 0.6982 0.5676 0.0517  0.0384  -0.1191 53  LYS A N   
200  C CA  . LYS A 53  ? 0.6882 0.7051 0.5137 0.0454  0.0442  -0.1190 53  LYS A CA  
201  C C   . LYS A 53  ? 0.6706 0.7172 0.5077 0.0419  0.0417  -0.0884 53  LYS A C   
202  O O   . LYS A 53  ? 0.6359 0.7100 0.4604 0.0416  0.0519  -0.0811 53  LYS A O   
203  C CB  . LYS A 53  ? 0.7382 0.7493 0.5289 0.0288  0.0312  -0.1313 53  LYS A CB  
204  C CG  . LYS A 53  ? 0.9287 0.9022 0.7063 0.0281  0.0298  -0.1635 53  LYS A CG  
205  C CD  . LYS A 53  ? 1.1347 1.0871 0.9288 0.0486  0.0469  -0.1824 53  LYS A CD  
206  C CE  . LYS A 53  ? 1.1557 1.0592 0.9487 0.0484  0.0405  -0.2081 53  LYS A CE  
207  N NZ  . LYS A 53  ? 1.0291 0.9221 0.7795 0.0319  0.0333  -0.2332 53  LYS A NZ  
208  N N   . GLY A 54  ? 0.6287 0.6692 0.4896 0.0388  0.0292  -0.0708 54  GLY A N   
209  C CA  . GLY A 54  ? 0.5921 0.6534 0.4682 0.0376  0.0268  -0.0447 54  GLY A CA  
210  C C   . GLY A 54  ? 0.7902 0.8612 0.6867 0.0476  0.0403  -0.0376 54  GLY A C   
211  O O   . GLY A 54  ? 0.6103 0.7026 0.5090 0.0450  0.0438  -0.0200 54  GLY A O   
212  N N   . ILE A 55  ? 0.6608 0.7168 0.5745 0.0582  0.0467  -0.0496 55  ILE A N   
213  C CA  . ILE A 55  ? 0.6207 0.6901 0.5589 0.0678  0.0583  -0.0440 55  ILE A CA  
214  C C   . ILE A 55  ? 0.5244 0.6209 0.4470 0.0696  0.0757  -0.0496 55  ILE A C   
215  O O   . ILE A 55  ? 0.5635 0.6860 0.4959 0.0671  0.0831  -0.0334 55  ILE A O   
216  C CB  . ILE A 55  ? 0.7310 0.7787 0.6917 0.0797  0.0582  -0.0549 55  ILE A CB  
217  C CG1 . ILE A 55  ? 0.6211 0.6560 0.6023 0.0766  0.0447  -0.0401 55  ILE A CG1 
218  C CG2 . ILE A 55  ? 0.6976 0.7644 0.6797 0.0933  0.0742  -0.0597 55  ILE A CG2 
219  C CD1 . ILE A 55  ? 0.6395 0.6495 0.6366 0.0846  0.0396  -0.0463 55  ILE A CD1 
220  N N   . VAL A 56  ? 0.6453 0.7364 0.5412 0.0717  0.0826  -0.0731 56  VAL A N   
221  C CA  . VAL A 56  ? 0.6969 0.8162 0.5693 0.0719  0.1012  -0.0822 56  VAL A CA  
222  C C   . VAL A 56  ? 0.8281 0.9749 0.6821 0.0569  0.0989  -0.0572 56  VAL A C   
223  O O   . VAL A 56  ? 0.6803 0.8582 0.5380 0.0556  0.1134  -0.0456 56  VAL A O   
224  C CB  . VAL A 56  ? 0.6808 0.7847 0.5178 0.0724  0.1047  -0.1136 56  VAL A CB  
225  C CG1 . VAL A 56  ? 0.7735 0.9103 0.5715 0.0665  0.1215  -0.1211 56  VAL A CG1 
226  C CG2 . VAL A 56  ? 0.6873 0.7661 0.5469 0.0909  0.1124  -0.1386 56  VAL A CG2 
227  N N   . LEU A 57  ? 0.7190 0.8557 0.5574 0.0453  0.0797  -0.0461 57  LEU A N   
228  C CA  . LEU A 57  ? 0.7803 0.9389 0.6002 0.0319  0.0738  -0.0211 57  LEU A CA  
229  C C   . LEU A 57  ? 0.6327 0.8002 0.4855 0.0312  0.0732  0.0073  57  LEU A C   
230  O O   . LEU A 57  ? 0.6878 0.8795 0.5320 0.0229  0.0792  0.0271  57  LEU A O   
231  C CB  . LEU A 57  ? 0.6692 0.8160 0.4735 0.0224  0.0514  -0.0161 57  LEU A CB  
232  C CG  . LEU A 57  ? 0.7865 0.9355 0.5459 0.0135  0.0469  -0.0344 57  LEU A CG  
233  C CD1 . LEU A 57  ? 0.7361 0.8764 0.4954 0.0047  0.0219  -0.0262 57  LEU A CD1 
234  C CD2 . LEU A 57  ? 0.8228 1.0038 0.5429 0.0043  0.0565  -0.0268 57  LEU A CD2 
235  N N   . LEU A 58  ? 0.5366 0.6840 0.4250 0.0376  0.0651  0.0103  58  LEU A N   
236  C CA  . LEU A 58  ? 0.5097 0.6616 0.4284 0.0357  0.0636  0.0331  58  LEU A CA  
237  C C   . LEU A 58  ? 0.6654 0.8420 0.5978 0.0375  0.0824  0.0353  58  LEU A C   
238  O O   . LEU A 58  ? 0.6024 0.7933 0.5470 0.0292  0.0841  0.0578  58  LEU A O   
239  C CB  . LEU A 58  ? 0.5079 0.6347 0.4562 0.0417  0.0527  0.0305  58  LEU A CB  
240  C CG  . LEU A 58  ? 0.5756 0.6861 0.5194 0.0382  0.0355  0.0350  58  LEU A CG  
241  C CD1 . LEU A 58  ? 0.5621 0.6513 0.5292 0.0436  0.0289  0.0283  58  LEU A CD1 
242  C CD2 . LEU A 58  ? 0.4517 0.5692 0.3986 0.0310  0.0278  0.0604  58  LEU A CD2 
243  N N   . GLU A 59  ? 0.5533 0.7358 0.4873 0.0482  0.0965  0.0125  59  GLU A N   
244  C CA  . GLU A 59  ? 0.6421 0.8544 0.5970 0.0520  0.1157  0.0134  59  GLU A CA  
245  C C   . GLU A 59  ? 0.6872 0.9346 0.6150 0.0412  0.1312  0.0231  59  GLU A C   
246  O O   . GLU A 59  ? 0.7112 0.9879 0.6584 0.0354  0.1430  0.0391  59  GLU A O   
247  C CB  . GLU A 59  ? 0.6699 0.8786 0.6375 0.0698  0.1264  -0.0144 59  GLU A CB  
248  C CG  . GLU A 59  ? 0.6217 0.8121 0.6303 0.0792  0.1157  -0.0138 59  GLU A CG  
249  C CD  . GLU A 59  ? 0.9666 1.1432 0.9868 0.0977  0.1206  -0.0390 59  GLU A CD  
250  O OE1 . GLU A 59  ? 0.9569 1.1300 0.9513 0.1034  0.1311  -0.0612 59  GLU A OE1 
251  O OE2 . GLU A 59  ? 0.8395 1.0070 0.8942 0.1062  0.1128  -0.0365 59  GLU A OE2 
252  N N   . GLU A 60  ? 0.7133 0.9603 0.5953 0.0358  0.1308  0.0152  60  GLU A N   
253  C CA  . GLU A 60  ? 0.7332 1.0142 0.5815 0.0222  0.1433  0.0281  60  GLU A CA  
254  C C   . GLU A 60  ? 0.7520 1.0342 0.6025 0.0058  0.1288  0.0668  60  GLU A C   
255  O O   . GLU A 60  ? 0.7721 1.0839 0.6203 -0.0063 0.1401  0.0887  60  GLU A O   
256  C CB  . GLU A 60  ? 0.8454 1.1250 0.6401 0.0194  0.1437  0.0078  60  GLU A CB  
257  C CG  . GLU A 60  ? 0.9054 1.1601 0.6998 0.0353  0.1457  -0.0308 60  GLU A CG  
258  C CD  . GLU A 60  ? 1.1364 1.3913 0.8753 0.0304  0.1484  -0.0553 60  GLU A CD  
259  O OE1 . GLU A 60  ? 1.2023 1.4494 0.9355 0.0430  0.1624  -0.0908 60  GLU A OE1 
260  O OE2 . GLU A 60  ? 1.1104 1.3723 0.8119 0.0140  0.1355  -0.0394 60  GLU A OE2 
261  N N   . LEU A 61  ? 0.6892 0.9393 0.5467 0.0053  0.1043  0.0760  61  LEU A N   
262  C CA  . LEU A 61  ? 0.8318 1.0760 0.6987 -0.0064 0.0891  0.1109  61  LEU A CA  
263  C C   . LEU A 61  ? 0.7994 1.0489 0.7076 -0.0097 0.0950  0.1272  61  LEU A C   
264  O O   . LEU A 61  ? 0.6925 0.9496 0.6036 -0.0238 0.0924  0.1578  61  LEU A O   
265  C CB  . LEU A 61  ? 0.8436 1.0537 0.7202 -0.0015 0.0648  0.1114  61  LEU A CB  
266  C CG  . LEU A 61  ? 0.7982 1.0060 0.6390 -0.0050 0.0508  0.1099  61  LEU A CG  
267  C CD1 . LEU A 61  ? 0.8292 1.0112 0.6929 -0.0011 0.0282  0.1190  61  LEU A CD1 
268  C CD2 . LEU A 61  ? 0.7712 1.0047 0.5758 -0.0201 0.0516  0.1341  61  LEU A CD2 
269  N N   . LEU A 62  ? 0.6476 0.8930 0.5881 0.0018  0.1014  0.1087  62  LEU A N   
270  C CA  . LEU A 62  ? 0.6934 0.9403 0.6768 -0.0017 0.1015  0.1213  62  LEU A CA  
271  C C   . LEU A 62  ? 0.7696 1.0496 0.7571 -0.0184 0.1144  0.1469  62  LEU A C   
272  O O   . LEU A 62  ? 0.8490 1.1173 0.8560 -0.0308 0.1035  0.1720  62  LEU A O   
273  C CB  . LEU A 62  ? 0.8026 1.0512 0.8134 0.0135  0.1086  0.0963  62  LEU A CB  
274  C CG  . LEU A 62  ? 0.7507 0.9962 0.8070 0.0129  0.1031  0.1019  62  LEU A CG  
275  C CD1 . LEU A 62  ? 0.5415 0.7507 0.6044 0.0067  0.0813  0.1142  62  LEU A CD1 
276  C CD2 . LEU A 62  ? 0.6092 0.8525 0.6853 0.0304  0.1054  0.0774  62  LEU A CD2 
277  N N   . PRO A 63  ? 0.6895 1.0099 0.6591 -0.0208 0.1376  0.1423  63  PRO A N   
278  C CA  . PRO A 63  ? 0.7616 1.1169 0.7339 -0.0405 0.1505  0.1710  63  PRO A CA  
279  C C   . PRO A 63  ? 0.8759 1.2215 0.8173 -0.0584 0.1379  0.2036  63  PRO A C   
280  O O   . PRO A 63  ? 0.8324 1.1924 0.7838 -0.0777 0.1406  0.2353  63  PRO A O   
281  C CB  . PRO A 63  ? 0.6114 1.0143 0.5661 -0.0359 0.1809  0.1524  63  PRO A CB  
282  C CG  . PRO A 63  ? 0.6471 1.0363 0.6112 -0.0113 0.1831  0.1136  63  PRO A CG  
283  C CD  . PRO A 63  ? 0.7305 1.0681 0.6848 -0.0054 0.1556  0.1092  63  PRO A CD  
284  N N   . LYS A 64  ? 0.7424 1.0653 0.6484 -0.0535 0.1232  0.1989  64  LYS A N   
285  C CA  . LYS A 64  ? 0.8116 1.1317 0.6839 -0.0687 0.1108  0.2300  64  LYS A CA  
286  C C   . LYS A 64  ? 0.8372 1.1161 0.7354 -0.0720 0.0839  0.2556  64  LYS A C   
287  O O   . LYS A 64  ? 0.9209 1.1950 0.8010 -0.0847 0.0712  0.2880  64  LYS A O   
288  C CB  . LYS A 64  ? 0.8875 1.2074 0.7104 -0.0628 0.1053  0.2133  64  LYS A CB  
289  C CG  . LYS A 64  ? 0.9533 1.3155 0.7307 -0.0667 0.1303  0.1968  64  LYS A CG  
290  C CD  . LYS A 64  ? 1.1857 1.5641 0.9849 -0.0515 0.1551  0.1604  64  LYS A CD  
291  C CE  . LYS A 64  ? 1.2215 1.6096 0.9795 -0.0412 0.1677  0.1216  64  LYS A CE  
292  N NZ  . LYS A 64  ? 0.9275 1.3253 0.7161 -0.0223 0.1897  0.0869  64  LYS A NZ  
293  N N   . GLY A 65  ? 0.7432 0.9917 0.6820 -0.0606 0.0744  0.2418  65  GLY A N   
294  C CA  . GLY A 65  ? 0.9941 1.2001 0.9541 -0.0588 0.0498  0.2564  65  GLY A CA  
295  C C   . GLY A 65  ? 0.9089 1.1008 0.9030 -0.0731 0.0451  0.2830  65  GLY A C   
296  O O   . GLY A 65  ? 0.7800 0.9904 0.7956 -0.0811 0.0588  0.2819  65  GLY A O   
297  N N   . SER A 66  ? 0.8751 1.0327 0.8778 -0.0759 0.0240  0.3068  66  SER A N   
298  C CA  . SER A 66  ? 0.8511 0.9796 0.8915 -0.0866 0.0150  0.3255  66  SER A CA  
299  C C   . SER A 66  ? 0.8363 0.9458 0.9100 -0.0760 0.0146  0.2944  66  SER A C   
300  O O   . SER A 66  ? 0.8216 0.9404 0.8888 -0.0604 0.0207  0.2629  66  SER A O   
301  C CB  . SER A 66  ? 0.9885 1.0774 1.0345 -0.0861 -0.0088 0.3521  66  SER A CB  
302  O OG  . SER A 66  ? 1.0429 1.1028 1.1009 -0.0642 -0.0219 0.3286  66  SER A OG  
303  N N   . LYS A 67  ? 1.0262 1.1078 1.1336 -0.0856 0.0063  0.3029  67  LYS A N   
304  C CA  . LYS A 67  ? 1.0183 1.0868 1.1515 -0.0784 0.0055  0.2733  67  LYS A CA  
305  C C   . LYS A 67  ? 1.0399 1.0737 1.1743 -0.0577 -0.0073 0.2502  67  LYS A C   
306  O O   . LYS A 67  ? 1.0053 1.0438 1.1397 -0.0455 -0.0034 0.2205  67  LYS A O   
307  C CB  . LYS A 67  ? 1.2020 1.2527 1.3688 -0.0977 -0.0002 0.2860  67  LYS A CB  
308  C CG  . LYS A 67  ? 1.1569 1.2472 1.3395 -0.1076 0.0140  0.2773  67  LYS A CG  
309  C CD  . LYS A 67  ? 1.1396 1.2827 1.3050 -0.1170 0.0340  0.2950  67  LYS A CD  
310  C CE  . LYS A 67  ? 1.2229 1.4051 1.4171 -0.1343 0.0466  0.3000  67  LYS A CE  
311  N NZ  . LYS A 67  ? 1.1581 1.3992 1.3352 -0.1379 0.0714  0.3078  67  LYS A NZ  
312  N N   . GLU A 68  ? 1.0195 1.0201 1.1569 -0.0534 -0.0223 0.2646  68  GLU A N   
313  C CA  . GLU A 68  ? 0.9870 0.9631 1.1280 -0.0326 -0.0314 0.2422  68  GLU A CA  
314  C C   . GLU A 68  ? 0.9629 0.9663 1.0761 -0.0194 -0.0261 0.2298  68  GLU A C   
315  O O   . GLU A 68  ? 1.0220 1.0142 1.1378 -0.0035 -0.0309 0.2096  68  GLU A O   
316  C CB  . GLU A 68  ? 1.1751 1.1104 1.3339 -0.0281 -0.0487 0.2598  68  GLU A CB  
317  C CG  . GLU A 68  ? 1.2858 1.2304 1.4287 -0.0286 -0.0565 0.2921  68  GLU A CG  
318  C CD  . GLU A 68  ? 1.3478 1.2901 1.4911 -0.0510 -0.0592 0.3319  68  GLU A CD  
319  O OE1 . GLU A 68  ? 1.2659 1.2088 1.4206 -0.0682 -0.0517 0.3337  68  GLU A OE1 
320  O OE2 . GLU A 68  ? 1.3319 1.2736 1.4647 -0.0529 -0.0700 0.3634  68  GLU A OE2 
321  N N   . GLU A 69  ? 0.8655 0.9050 0.9520 -0.0269 -0.0159 0.2404  69  GLU A N   
322  C CA  . GLU A 69  ? 0.7502 0.8148 0.8086 -0.0170 -0.0096 0.2232  69  GLU A CA  
323  C C   . GLU A 69  ? 0.8517 0.9325 0.9097 -0.0129 0.0047  0.1945  69  GLU A C   
324  O O   . GLU A 69  ? 0.7101 0.7891 0.7618 -0.0005 0.0046  0.1707  69  GLU A O   
325  C CB  . GLU A 69  ? 0.7225 0.8162 0.7476 -0.0268 -0.0057 0.2450  69  GLU A CB  
326  C CG  . GLU A 69  ? 0.7963 0.8785 0.8142 -0.0251 -0.0244 0.2693  69  GLU A CG  
327  C CD  . GLU A 69  ? 1.0670 1.1767 1.0491 -0.0397 -0.0235 0.2983  69  GLU A CD  
328  O OE1 . GLU A 69  ? 0.8050 0.9454 0.7654 -0.0511 -0.0050 0.2974  69  GLU A OE1 
329  O OE2 . GLU A 69  ? 1.0292 1.1316 1.0055 -0.0396 -0.0415 0.3231  69  GLU A OE2 
330  N N   . GLN A 70  ? 0.6524 0.7492 0.7210 -0.0236 0.0159  0.1981  70  GLN A N   
331  C CA  . GLN A 70  ? 0.5138 0.6285 0.5874 -0.0182 0.0279  0.1742  70  GLN A CA  
332  C C   . GLN A 70  ? 0.4508 0.5397 0.5429 -0.0090 0.0191  0.1531  70  GLN A C   
333  O O   . GLN A 70  ? 0.5512 0.6468 0.6399 0.0006  0.0237  0.1316  70  GLN A O   
334  C CB  . GLN A 70  ? 0.5396 0.6813 0.6292 -0.0321 0.0400  0.1859  70  GLN A CB  
335  C CG  . GLN A 70  ? 0.6673 0.8442 0.7334 -0.0410 0.0543  0.2024  70  GLN A CG  
336  C CD  . GLN A 70  ? 0.8228 1.0377 0.9074 -0.0526 0.0715  0.2093  70  GLN A CD  
337  O OE1 . GLN A 70  ? 0.5871 0.8042 0.7043 -0.0528 0.0712  0.2006  70  GLN A OE1 
338  N NE2 . GLN A 70  ? 0.7759 1.0240 0.8402 -0.0640 0.0859  0.2270  70  GLN A NE2 
339  N N   . ARG A 71  ? 0.6479 0.7060 0.7585 -0.0124 0.0068  0.1588  71  ARG A N   
340  C CA  . ARG A 71  ? 0.5850 0.6170 0.7053 -0.0035 -0.0015 0.1379  71  ARG A CA  
341  C C   . ARG A 71  ? 0.5681 0.6029 0.6702 0.0110  -0.0004 0.1195  71  ARG A C   
342  O O   . ARG A 71  ? 0.4517 0.4894 0.5522 0.0164  0.0022  0.1005  71  ARG A O   
343  C CB  . ARG A 71  ? 0.8590 0.8559 0.9940 -0.0049 -0.0139 0.1470  71  ARG A CB  
344  C CG  . ARG A 71  ? 0.9756 0.9458 1.1292 -0.0073 -0.0206 0.1322  71  ARG A CG  
345  C CD  . ARG A 71  ? 0.7161 0.6498 0.8869 -0.0102 -0.0314 0.1441  71  ARG A CD  
346  N NE  . ARG A 71  ? 0.8616 0.7807 1.0305 0.0067  -0.0359 0.1386  71  ARG A NE  
347  C CZ  . ARG A 71  ? 0.7594 0.6635 0.9314 0.0187  -0.0368 0.1135  71  ARG A CZ  
348  N NH1 . ARG A 71  ? 0.5950 0.4931 0.7666 0.0147  -0.0351 0.0916  71  ARG A NH1 
349  N NH2 . ARG A 71  ? 0.8590 0.7577 1.0347 0.0342  -0.0396 0.1111  71  ARG A NH2 
350  N N   A ASP A 72  ? 0.6164 0.6507 0.7058 0.0160  -0.0041 0.1274  72  ASP A N   
351  N N   B ASP A 72  ? 0.6159 0.6503 0.7053 0.0160  -0.0040 0.1274  72  ASP A N   
352  C CA  A ASP A 72  ? 0.5788 0.6175 0.6532 0.0265  -0.0044 0.1120  72  ASP A CA  
353  C CA  B ASP A 72  ? 0.5791 0.6179 0.6535 0.0265  -0.0045 0.1122  72  ASP A CA  
354  C C   A ASP A 72  ? 0.6047 0.6658 0.6601 0.0272  0.0061  0.1011  72  ASP A C   
355  C C   B ASP A 72  ? 0.6033 0.6645 0.6586 0.0272  0.0060  0.1012  72  ASP A C   
356  O O   A ASP A 72  ? 0.5522 0.6112 0.6028 0.0335  0.0073  0.0827  72  ASP A O   
357  O O   B ASP A 72  ? 0.5516 0.6105 0.6017 0.0336  0.0071  0.0828  72  ASP A O   
358  C CB  A ASP A 72  ? 0.5429 0.5826 0.6102 0.0297  -0.0128 0.1254  72  ASP A CB  
359  C CB  B ASP A 72  ? 0.5445 0.5839 0.6123 0.0294  -0.0129 0.1262  72  ASP A CB  
360  C CG  A ASP A 72  ? 0.6706 0.6854 0.7620 0.0338  -0.0240 0.1349  72  ASP A CG  
361  C CG  B ASP A 72  ? 0.6715 0.6859 0.7634 0.0358  -0.0238 0.1301  72  ASP A CG  
362  O OD1 A ASP A 72  ? 0.6010 0.5955 0.7103 0.0370  -0.0245 0.1217  72  ASP A OD1 
363  O OD1 B ASP A 72  ? 0.7546 0.7642 0.8530 0.0457  -0.0261 0.1145  72  ASP A OD1 
364  O OD2 A ASP A 72  ? 0.5785 0.5938 0.6704 0.0349  -0.0331 0.1547  72  ASP A OD2 
365  O OD2 B ASP A 72  ? 0.7845 0.7838 0.8903 0.0309  -0.0292 0.1487  72  ASP A OD2 
366  N N   . TYR A 73  ? 0.5262 0.6084 0.5708 0.0206  0.0144  0.1120  73  TYR A N   
367  C CA  . TYR A 73  ? 0.5435 0.6456 0.5725 0.0236  0.0265  0.0982  73  TYR A CA  
368  C C   . TYR A 73  ? 0.5510 0.6497 0.5973 0.0288  0.0298  0.0824  73  TYR A C   
369  O O   . TYR A 73  ? 0.4774 0.5745 0.5156 0.0366  0.0322  0.0650  73  TYR A O   
370  C CB  . TYR A 73  ? 0.6107 0.7403 0.6296 0.0156  0.0388  0.1109  73  TYR A CB  
371  C CG  . TYR A 73  ? 0.7407 0.8787 0.7363 0.0078  0.0356  0.1302  73  TYR A CG  
372  C CD1 . TYR A 73  ? 0.5873 0.7140 0.5688 0.0110  0.0224  0.1313  73  TYR A CD1 
373  C CD2 . TYR A 73  ? 0.6293 0.7908 0.6175 -0.0040 0.0454  0.1496  73  TYR A CD2 
374  C CE1 . TYR A 73  ? 0.6380 0.7747 0.5982 0.0034  0.0162  0.1521  73  TYR A CE1 
375  C CE2 . TYR A 73  ? 0.6926 0.8631 0.6551 -0.0130 0.0410  0.1710  73  TYR A CE2 
376  C CZ  . TYR A 73  ? 0.8042 0.9614 0.7523 -0.0089 0.0251  0.1726  73  TYR A CZ  
377  O OH  . TYR A 73  ? 0.9363 1.1043 0.8590 -0.0182 0.0174  0.1969  73  TYR A OH  
378  N N   . VAL A 74  ? 0.4968 0.5937 0.5672 0.0231  0.0283  0.0895  74  VAL A N   
379  C CA  . VAL A 74  ? 0.4267 0.5256 0.5144 0.0264  0.0289  0.0781  74  VAL A CA  
380  C C   . VAL A 74  ? 0.4899 0.5652 0.5739 0.0326  0.0194  0.0640  74  VAL A C   
381  O O   . VAL A 74  ? 0.4857 0.5612 0.5691 0.0391  0.0199  0.0520  74  VAL A O   
382  C CB  . VAL A 74  ? 0.4956 0.5997 0.6098 0.0155  0.0265  0.0897  74  VAL A CB  
383  C CG1 . VAL A 74  ? 0.5126 0.6173 0.6442 0.0178  0.0216  0.0790  74  VAL A CG1 
384  C CG2 . VAL A 74  ? 0.4839 0.6198 0.6049 0.0076  0.0392  0.1045  74  VAL A CG2 
385  N N   . PHE A 75  ? 0.5368 0.5925 0.6193 0.0309  0.0112  0.0659  75  PHE A N   
386  C CA  . PHE A 75  ? 0.5120 0.5509 0.5899 0.0356  0.0052  0.0524  75  PHE A CA  
387  C C   . PHE A 75  ? 0.5500 0.5920 0.6101 0.0420  0.0080  0.0431  75  PHE A C   
388  O O   . PHE A 75  ? 0.5318 0.5683 0.5884 0.0445  0.0067  0.0329  75  PHE A O   
389  C CB  . PHE A 75  ? 0.4645 0.4856 0.5474 0.0352  -0.0011 0.0542  75  PHE A CB  
390  C CG  . PHE A 75  ? 0.5277 0.5378 0.6058 0.0395  -0.0037 0.0393  75  PHE A CG  
391  C CD1 . PHE A 75  ? 0.5238 0.5268 0.6025 0.0364  -0.0061 0.0292  75  PHE A CD1 
392  C CD2 . PHE A 75  ? 0.5366 0.5476 0.6088 0.0449  -0.0038 0.0364  75  PHE A CD2 
393  C CE1 . PHE A 75  ? 0.5339 0.5304 0.6038 0.0383  -0.0064 0.0165  75  PHE A CE1 
394  C CE2 . PHE A 75  ? 0.6567 0.6635 0.7260 0.0473  -0.0035 0.0235  75  PHE A CE2 
395  C CZ  . PHE A 75  ? 0.5330 0.5323 0.5992 0.0437  -0.0037 0.0137  75  PHE A CZ  
396  N N   . TYR A 76  ? 0.5382 0.5884 0.5856 0.0428  0.0106  0.0475  76  TYR A N   
397  C CA  . TYR A 76  ? 0.4953 0.5457 0.5260 0.0461  0.0113  0.0367  76  TYR A CA  
398  C C   . TYR A 76  ? 0.5942 0.6497 0.6192 0.0498  0.0184  0.0275  76  TYR A C   
399  O O   . TYR A 76  ? 0.5529 0.5993 0.5687 0.0522  0.0172  0.0163  76  TYR A O   
400  C CB  . TYR A 76  ? 0.5296 0.5879 0.5465 0.0443  0.0088  0.0426  76  TYR A CB  
401  C CG  . TYR A 76  ? 0.5727 0.6246 0.5994 0.0450  0.0002  0.0471  76  TYR A CG  
402  C CD1 . TYR A 76  ? 0.6272 0.6732 0.6561 0.0466  -0.0026 0.0362  76  TYR A CD1 
403  C CD2 . TYR A 76  ? 0.6504 0.7025 0.6870 0.0445  -0.0045 0.0626  76  TYR A CD2 
404  C CE1 . TYR A 76  ? 0.6917 0.7373 0.7344 0.0491  -0.0077 0.0383  76  TYR A CE1 
405  C CE2 . TYR A 76  ? 0.7084 0.7546 0.7602 0.0488  -0.0120 0.0652  76  TYR A CE2 
406  C CZ  . TYR A 76  ? 0.5862 0.6315 0.6418 0.0519  -0.0124 0.0517  76  TYR A CZ  
407  O OH  . TYR A 76  ? 0.9748 1.0197 1.0498 0.0580  -0.0170 0.0522  76  TYR A OH  
408  N N   . LEU A 77  ? 0.4655 0.5355 0.4986 0.0505  0.0262  0.0319  77  LEU A N   
409  C CA  . LEU A 77  ? 0.4963 0.5713 0.5334 0.0578  0.0333  0.0215  77  LEU A CA  
410  C C   . LEU A 77  ? 0.4987 0.5599 0.5498 0.0610  0.0258  0.0178  77  LEU A C   
411  O O   . LEU A 77  ? 0.5396 0.5905 0.5884 0.0674  0.0252  0.0081  77  LEU A O   
412  C CB  . LEU A 77  ? 0.4585 0.5592 0.5081 0.0581  0.0446  0.0278  77  LEU A CB  
413  C CG  . LEU A 77  ? 0.5162 0.6341 0.5441 0.0566  0.0561  0.0270  77  LEU A CG  
414  C CD1 . LEU A 77  ? 0.6027 0.7508 0.6440 0.0516  0.0678  0.0400  77  LEU A CD1 
415  C CD2 . LEU A 77  ? 0.4821 0.5964 0.4980 0.0668  0.0634  0.0062  77  LEU A CD2 
416  N N   . ALA A 78  ? 0.5123 0.5717 0.5769 0.0556  0.0189  0.0256  78  ALA A N   
417  C CA  . ALA A 78  ? 0.5797 0.6281 0.6513 0.0560  0.0102  0.0231  78  ALA A CA  
418  C C   . ALA A 78  ? 0.5578 0.5871 0.6116 0.0554  0.0054  0.0164  78  ALA A C   
419  O O   . ALA A 78  ? 0.4727 0.4922 0.5255 0.0581  0.0010  0.0136  78  ALA A O   
420  C CB  . ALA A 78  ? 0.4019 0.4503 0.4849 0.0478  0.0032  0.0294  78  ALA A CB  
421  N N   . VAL A 79  ? 0.4992 0.5247 0.5417 0.0515  0.0056  0.0158  79  VAL A N   
422  C CA  . VAL A 79  ? 0.5591 0.5731 0.5886 0.0489  0.0024  0.0103  79  VAL A CA  
423  C C   . VAL A 79  ? 0.5939 0.6010 0.6141 0.0519  0.0040  0.0037  79  VAL A C   
424  O O   . VAL A 79  ? 0.4972 0.4905 0.5122 0.0497  -0.0002 0.0012  79  VAL A O   
425  C CB  . VAL A 79  ? 0.4977 0.5156 0.5242 0.0461  0.0024  0.0114  79  VAL A CB  
426  C CG1 . VAL A 79  ? 0.4974 0.5113 0.5138 0.0424  0.0006  0.0059  79  VAL A CG1 
427  C CG2 . VAL A 79  ? 0.4099 0.4266 0.4464 0.0444  0.0005  0.0139  79  VAL A CG2 
428  N N   . GLY A 80  ? 0.5050 0.5200 0.5205 0.0554  0.0099  0.0006  80  GLY A N   
429  C CA  . GLY A 80  ? 0.5240 0.5289 0.5283 0.0581  0.0118  -0.0103 80  GLY A CA  
430  C C   . GLY A 80  ? 0.5773 0.5699 0.5923 0.0661  0.0115  -0.0137 80  GLY A C   
431  O O   . GLY A 80  ? 0.5300 0.5014 0.5400 0.0655  0.0068  -0.0189 80  GLY A O   
432  N N   . ASN A 81  ? 0.5891 0.5954 0.6224 0.0731  0.0151  -0.0091 81  ASN A N   
433  C CA  . ASN A 81  ? 0.5436 0.5420 0.5939 0.0830  0.0126  -0.0100 81  ASN A CA  
434  C C   . ASN A 81  ? 0.5398 0.5202 0.5894 0.0774  -0.0005 -0.0019 81  ASN A C   
435  O O   . ASN A 81  ? 0.5612 0.5211 0.6134 0.0820  -0.0061 -0.0027 81  ASN A O   
436  C CB  . ASN A 81  ? 0.5388 0.5632 0.6140 0.0896  0.0176  -0.0042 81  ASN A CB  
437  C CG  . ASN A 81  ? 0.6595 0.7019 0.7375 0.0981  0.0333  -0.0137 81  ASN A CG  
438  O OD1 . ASN A 81  ? 0.6346 0.6682 0.7157 0.1099  0.0387  -0.0264 81  ASN A OD1 
439  N ND2 . ASN A 81  ? 0.4646 0.5308 0.5398 0.0917  0.0412  -0.0081 81  ASN A ND2 
440  N N   . TYR A 82  ? 0.6180 0.6046 0.6629 0.0672  -0.0052 0.0059  82  TYR A N   
441  C CA  . TYR A 82  ? 0.5369 0.5105 0.5741 0.0594  -0.0154 0.0127  82  TYR A CA  
442  C C   . TYR A 82  ? 0.5612 0.5130 0.5833 0.0544  -0.0175 0.0097  82  TYR A C   
443  O O   . TYR A 82  ? 0.5658 0.4999 0.5871 0.0534  -0.0257 0.0160  82  TYR A O   
444  C CB  . TYR A 82  ? 0.5343 0.5177 0.5643 0.0495  -0.0160 0.0151  82  TYR A CB  
445  C CG  . TYR A 82  ? 0.6069 0.5813 0.6217 0.0392  -0.0223 0.0189  82  TYR A CG  
446  C CD1 . TYR A 82  ? 0.5308 0.5008 0.5448 0.0369  -0.0326 0.0277  82  TYR A CD1 
447  C CD2 . TYR A 82  ? 0.5571 0.5314 0.5587 0.0312  -0.0179 0.0151  82  TYR A CD2 
448  C CE1 . TYR A 82  ? 0.6109 0.5752 0.6050 0.0251  -0.0375 0.0327  82  TYR A CE1 
449  C CE2 . TYR A 82  ? 0.6350 0.6065 0.6219 0.0206  -0.0204 0.0184  82  TYR A CE2 
450  C CZ  . TYR A 82  ? 0.6479 0.6138 0.6280 0.0168  -0.0297 0.0273  82  TYR A CZ  
451  O OH  . TYR A 82  ? 0.6246 0.5900 0.5845 0.0040  -0.0313 0.0320  82  TYR A OH  
452  N N   . ARG A 83  ? 0.5750 0.5280 0.5862 0.0500  -0.0117 0.0020  83  ARG A N   
453  C CA  . ARG A 83  ? 0.5320 0.4680 0.5306 0.0408  -0.0147 -0.0005 83  ARG A CA  
454  C C   . ARG A 83  ? 0.5252 0.4353 0.5254 0.0468  -0.0173 -0.0062 83  ARG A C   
455  O O   . ARG A 83  ? 0.5627 0.4506 0.5561 0.0380  -0.0235 -0.0038 83  ARG A O   
456  C CB  . ARG A 83  ? 0.5268 0.4754 0.5175 0.0346  -0.0103 -0.0069 83  ARG A CB  
457  C CG  . ARG A 83  ? 0.5575 0.5274 0.5512 0.0313  -0.0079 -0.0021 83  ARG A CG  
458  C CD  . ARG A 83  ? 0.5765 0.5603 0.5681 0.0265  -0.0064 -0.0054 83  ARG A CD  
459  N NE  . ARG A 83  ? 0.5584 0.5378 0.5449 0.0147  -0.0095 -0.0064 83  ARG A NE  
460  C CZ  . ARG A 83  ? 0.6068 0.5914 0.5901 0.0087  -0.0120 -0.0112 83  ARG A CZ  
461  N NH1 . ARG A 83  ? 0.5805 0.5734 0.5602 0.0138  -0.0119 -0.0156 83  ARG A NH1 
462  N NH2 . ARG A 83  ? 0.6331 0.6165 0.6157 -0.0049 -0.0153 -0.0106 83  ARG A NH2 
463  N N   . LEU A 84  ? 0.5657 0.4777 0.5763 0.0612  -0.0120 -0.0143 84  LEU A N   
464  C CA  . LEU A 84  ? 0.6260 0.5121 0.6434 0.0716  -0.0132 -0.0226 84  LEU A CA  
465  C C   . LEU A 84  ? 0.5593 0.4377 0.5980 0.0823  -0.0207 -0.0111 84  LEU A C   
466  O O   . LEU A 84  ? 0.6744 0.5345 0.7278 0.0967  -0.0208 -0.0178 84  LEU A O   
467  C CB  . LEU A 84  ? 0.6637 0.5602 0.6815 0.0831  -0.0007 -0.0404 84  LEU A CB  
468  C CG  . LEU A 84  ? 0.6352 0.5412 0.6297 0.0728  0.0043  -0.0509 84  LEU A CG  
469  C CD1 . LEU A 84  ? 0.6079 0.5326 0.5995 0.0831  0.0176  -0.0642 84  LEU A CD1 
470  C CD2 . LEU A 84  ? 0.5550 0.4303 0.5347 0.0627  -0.0024 -0.0608 84  LEU A CD2 
471  N N   . LYS A 85  ? 0.5777 0.4707 0.6195 0.0767  -0.0274 0.0051  85  LYS A N   
472  C CA  . LYS A 85  ? 0.7097 0.6001 0.7705 0.0846  -0.0383 0.0191  85  LYS A CA  
473  C C   . LYS A 85  ? 0.6258 0.5344 0.7167 0.1044  -0.0327 0.0138  85  LYS A C   
474  O O   . LYS A 85  ? 0.5721 0.4735 0.6870 0.1174  -0.0412 0.0211  85  LYS A O   
475  C CB  . LYS A 85  ? 0.7252 0.5778 0.7847 0.0834  -0.0506 0.0278  85  LYS A CB  
476  C CG  . LYS A 85  ? 0.7206 0.5578 0.7527 0.0616  -0.0544 0.0341  85  LYS A CG  
477  C CD  . LYS A 85  ? 0.7820 0.5855 0.8134 0.0566  -0.0698 0.0519  85  LYS A CD  
478  C CE  . LYS A 85  ? 0.9795 0.7802 0.9838 0.0312  -0.0728 0.0641  85  LYS A CE  
479  N NZ  . LYS A 85  ? 0.9040 0.6760 0.9041 0.0229  -0.0890 0.0882  85  LYS A NZ  
480  N N   . GLU A 86  ? 0.6143 0.5485 0.7061 0.1070  -0.0184 0.0027  86  GLU A N   
481  C CA  . GLU A 86  ? 0.6467 0.6101 0.7677 0.1212  -0.0107 0.0006  86  GLU A CA  
482  C C   . GLU A 86  ? 0.5340 0.5244 0.6631 0.1122  -0.0173 0.0151  86  GLU A C   
483  O O   . GLU A 86  ? 0.5700 0.5825 0.6952 0.1051  -0.0093 0.0138  86  GLU A O   
484  C CB  . GLU A 86  ? 0.5813 0.5597 0.6951 0.1250  0.0081  -0.0163 86  GLU A CB  
485  C CG  . GLU A 86  ? 0.5327 0.4866 0.6379 0.1344  0.0157  -0.0357 86  GLU A CG  
486  C CD  . GLU A 86  ? 0.6701 0.6202 0.8083 0.1574  0.0187  -0.0429 86  GLU A CD  
487  O OE1 . GLU A 86  ? 0.8447 0.8233 1.0159 0.1668  0.0185  -0.0331 86  GLU A OE1 
488  O OE2 . GLU A 86  ? 1.0535 0.9719 1.1874 0.1662  0.0208  -0.0589 86  GLU A OE2 
489  N N   . TYR A 87  ? 0.5275 0.5130 0.6659 0.1109  -0.0340 0.0297  87  TYR A N   
490  C CA  . TYR A 87  ? 0.5590 0.5625 0.6946 0.0974  -0.0433 0.0409  87  TYR A CA  
491  C C   . TYR A 87  ? 0.6469 0.6870 0.8139 0.1018  -0.0397 0.0429  87  TYR A C   
492  O O   . TYR A 87  ? 0.4929 0.5483 0.6549 0.0891  -0.0394 0.0447  87  TYR A O   
493  C CB  . TYR A 87  ? 0.5874 0.5779 0.7184 0.0922  -0.0635 0.0566  87  TYR A CB  
494  C CG  . TYR A 87  ? 0.6071 0.5637 0.7092 0.0846  -0.0683 0.0595  87  TYR A CG  
495  C CD1 . TYR A 87  ? 0.6610 0.6098 0.7318 0.0702  -0.0606 0.0527  87  TYR A CD1 
496  C CD2 . TYR A 87  ? 0.6906 0.6250 0.7998 0.0906  -0.0821 0.0720  87  TYR A CD2 
497  C CE1 . TYR A 87  ? 0.7231 0.6465 0.7712 0.0606  -0.0643 0.0570  87  TYR A CE1 
498  C CE2 . TYR A 87  ? 0.8610 0.7646 0.9447 0.0802  -0.0871 0.0780  87  TYR A CE2 
499  C CZ  . TYR A 87  ? 0.7345 0.6348 0.7878 0.0643  -0.0774 0.0703  87  TYR A CZ  
500  O OH  . TYR A 87  ? 0.9164 0.7909 0.9479 0.0517  -0.0818 0.0779  87  TYR A OH  
501  N N   . GLU A 88  ? 0.5159 0.5708 0.7185 0.1195  -0.0371 0.0427  88  GLU A N   
502  C CA  . GLU A 88  ? 0.6057 0.7021 0.8432 0.1219  -0.0331 0.0465  88  GLU A CA  
503  C C   . GLU A 88  ? 0.5708 0.6840 0.8001 0.1159  -0.0129 0.0373  88  GLU A C   
504  O O   . GLU A 88  ? 0.6618 0.8003 0.9020 0.1045  -0.0125 0.0437  88  GLU A O   
505  C CB  . GLU A 88  ? 0.5194 0.6330 0.8024 0.1448  -0.0321 0.0471  88  GLU A CB  
506  C CG  . GLU A 88  ? 0.6822 0.7899 0.9861 0.1511  -0.0570 0.0636  88  GLU A CG  
507  C CD  . GLU A 88  ? 0.9295 1.0546 1.2333 0.1325  -0.0784 0.0805  88  GLU A CD  
508  O OE1 . GLU A 88  ? 0.9823 1.1147 1.3103 0.1383  -0.0995 0.0960  88  GLU A OE1 
509  O OE2 . GLU A 88  ? 0.9372 1.0683 1.2183 0.1127  -0.0759 0.0782  88  GLU A OE2 
510  N N   . LYS A 89  ? 0.5912 0.6894 0.7999 0.1216  0.0022  0.0236  89  LYS A N   
511  C CA  . LYS A 89  ? 0.5269 0.6388 0.7205 0.1140  0.0187  0.0181  89  LYS A CA  
512  C C   . LYS A 89  ? 0.5670 0.6674 0.7346 0.0948  0.0116  0.0244  89  LYS A C   
513  O O   . LYS A 89  ? 0.5187 0.6376 0.6906 0.0845  0.0158  0.0305  89  LYS A O   
514  C CB  . LYS A 89  ? 0.5541 0.6506 0.7259 0.1225  0.0327  0.0015  89  LYS A CB  
515  C CG  . LYS A 89  ? 0.7045 0.8089 0.9021 0.1438  0.0423  -0.0097 89  LYS A CG  
516  C CD  . LYS A 89  ? 0.8861 0.9911 1.0637 0.1498  0.0625  -0.0292 89  LYS A CD  
517  C CE  . LYS A 89  ? 0.8805 0.9461 1.0485 0.1622  0.0598  -0.0456 89  LYS A CE  
518  N NZ  . LYS A 89  ? 0.8025 0.8805 0.9886 0.1832  0.0786  -0.0657 89  LYS A NZ  
519  N N   . ALA A 90  ? 0.4579 0.5280 0.6005 0.0897  0.0014  0.0232  90  ALA A N   
520  C CA  . ALA A 90  ? 0.4495 0.5097 0.5708 0.0746  -0.0038 0.0262  90  ALA A CA  
521  C C   . ALA A 90  ? 0.5357 0.6096 0.6722 0.0648  -0.0131 0.0351  90  ALA A C   
522  O O   . ALA A 90  ? 0.4332 0.5094 0.5654 0.0544  -0.0114 0.0369  90  ALA A O   
523  C CB  . ALA A 90  ? 0.4825 0.5149 0.5800 0.0710  -0.0123 0.0240  90  ALA A CB  
524  N N   . LEU A 91  ? 0.5412 0.6226 0.6962 0.0674  -0.0250 0.0412  91  LEU A N   
525  C CA  . LEU A 91  ? 0.5380 0.6337 0.7071 0.0558  -0.0370 0.0486  91  LEU A CA  
526  C C   . LEU A 91  ? 0.5102 0.6344 0.7060 0.0521  -0.0285 0.0527  91  LEU A C   
527  O O   . LEU A 91  ? 0.5569 0.6823 0.7528 0.0373  -0.0328 0.0553  91  LEU A O   
528  C CB  . LEU A 91  ? 0.6008 0.7034 0.7863 0.0601  -0.0536 0.0568  91  LEU A CB  
529  C CG  . LEU A 91  ? 0.5904 0.6930 0.7677 0.0440  -0.0727 0.0618  91  LEU A CG  
530  C CD1 . LEU A 91  ? 0.6324 0.7065 0.7675 0.0338  -0.0729 0.0540  91  LEU A CD1 
531  C CD2 . LEU A 91  ? 0.6257 0.7359 0.8172 0.0493  -0.0915 0.0735  91  LEU A CD2 
532  N N   . LYS A 92  ? 0.4326 0.5790 0.6505 0.0645  -0.0153 0.0526  92  LYS A N   
533  C CA  . LYS A 92  ? 0.5907 0.7691 0.8332 0.0586  -0.0048 0.0586  92  LYS A CA  
534  C C   . LYS A 92  ? 0.5751 0.7406 0.7938 0.0464  0.0030  0.0592  92  LYS A C   
535  O O   . LYS A 92  ? 0.4264 0.6016 0.6569 0.0315  0.0010  0.0677  92  LYS A O   
536  C CB  . LYS A 92  ? 0.4777 0.6848 0.7443 0.0753  0.0122  0.0555  92  LYS A CB  
537  C CG  . LYS A 92  ? 0.5305 0.7609 0.8383 0.0878  0.0034  0.0593  92  LYS A CG  
538  C CD  . LYS A 92  ? 0.5878 0.8392 0.9177 0.1101  0.0224  0.0504  92  LYS A CD  
539  C CE  . LYS A 92  ? 0.5591 0.8484 0.9449 0.1230  0.0172  0.0568  92  LYS A CE  
540  N NZ  . LYS A 92  ? 0.7786 1.1158 1.1982 0.1323  0.0422  0.0528  92  LYS A NZ  
541  N N   . TYR A 93  ? 0.4707 0.6125 0.6576 0.0516  0.0095  0.0513  93  TYR A N   
542  C CA  . TYR A 93  ? 0.4649 0.5960 0.6321 0.0426  0.0150  0.0541  93  TYR A CA  
543  C C   . TYR A 93  ? 0.4011 0.5108 0.5626 0.0296  0.0017  0.0563  93  TYR A C   
544  O O   . TYR A 93  ? 0.4310 0.5414 0.5994 0.0180  0.0017  0.0648  93  TYR A O   
545  C CB  . TYR A 93  ? 0.5658 0.6797 0.7031 0.0509  0.0216  0.0450  93  TYR A CB  
546  C CG  . TYR A 93  ? 0.5764 0.7102 0.7110 0.0588  0.0382  0.0417  93  TYR A CG  
547  C CD1 . TYR A 93  ? 0.5619 0.7190 0.6998 0.0514  0.0494  0.0517  93  TYR A CD1 
548  C CD2 . TYR A 93  ? 0.6458 0.7739 0.7728 0.0724  0.0431  0.0283  93  TYR A CD2 
549  C CE1 . TYR A 93  ? 0.5926 0.7711 0.7225 0.0575  0.0667  0.0468  93  TYR A CE1 
550  C CE2 . TYR A 93  ? 0.4512 0.5960 0.5723 0.0798  0.0595  0.0204  93  TYR A CE2 
551  C CZ  . TYR A 93  ? 0.6471 0.8194 0.7680 0.0724  0.0721  0.0290  93  TYR A CZ  
552  O OH  . TYR A 93  ? 0.7088 0.9009 0.8187 0.0788  0.0903  0.0194  93  TYR A OH  
553  N N   . VAL A 94  ? 0.4752 0.5647 0.6236 0.0307  -0.0093 0.0485  94  VAL A N   
554  C CA  . VAL A 94  ? 0.4297 0.4977 0.5680 0.0201  -0.0190 0.0453  94  VAL A CA  
555  C C   . VAL A 94  ? 0.4519 0.5292 0.6117 0.0068  -0.0290 0.0503  94  VAL A C   
556  O O   . VAL A 94  ? 0.4639 0.5259 0.6236 -0.0043 -0.0332 0.0497  94  VAL A O   
557  C CB  . VAL A 94  ? 0.5388 0.5881 0.6540 0.0231  -0.0255 0.0354  94  VAL A CB  
558  C CG1 . VAL A 94  ? 0.5070 0.5633 0.6280 0.0201  -0.0384 0.0364  94  VAL A CG1 
559  C CG2 . VAL A 94  ? 0.5461 0.5732 0.6455 0.0174  -0.0270 0.0274  94  VAL A CG2 
560  N N   . ARG A 95  ? 0.4503 0.5522 0.6319 0.0077  -0.0342 0.0551  95  ARG A N   
561  C CA  . ARG A 95  ? 0.5479 0.6637 0.7532 -0.0072 -0.0462 0.0606  95  ARG A CA  
562  C C   . ARG A 95  ? 0.4451 0.5723 0.6707 -0.0179 -0.0384 0.0708  95  ARG A C   
563  O O   . ARG A 95  ? 0.5735 0.6913 0.8067 -0.0350 -0.0478 0.0723  95  ARG A O   
564  C CB  . ARG A 95  ? 0.6017 0.7485 0.8333 -0.0022 -0.0541 0.0664  95  ARG A CB  
565  C CG  . ARG A 95  ? 0.7810 0.9153 0.9935 0.0050  -0.0660 0.0615  95  ARG A CG  
566  C CD  . ARG A 95  ? 0.6812 0.8251 0.9017 -0.0076 -0.0885 0.0645  95  ARG A CD  
567  N NE  . ARG A 95  ? 0.7850 0.9111 0.9756 -0.0048 -0.0998 0.0612  95  ARG A NE  
568  C CZ  . ARG A 95  ? 0.8545 0.9934 1.0550 0.0034  -0.1118 0.0704  95  ARG A CZ  
569  N NH1 . ARG A 95  ? 0.7335 0.9051 0.9778 0.0132  -0.1135 0.0812  95  ARG A NH1 
570  N NH2 . ARG A 95  ? 0.8879 1.0076 1.0553 0.0022  -0.1221 0.0698  95  ARG A NH2 
571  N N   . GLY A 96  ? 0.4900 0.6358 0.7221 -0.0096 -0.0214 0.0778  96  GLY A N   
572  C CA  . GLY A 96  ? 0.4631 0.6190 0.7082 -0.0216 -0.0130 0.0909  96  GLY A CA  
573  C C   . GLY A 96  ? 0.5088 0.6260 0.7338 -0.0296 -0.0167 0.0907  96  GLY A C   
574  O O   . GLY A 96  ? 0.4463 0.5567 0.6848 -0.0463 -0.0210 0.1006  96  GLY A O   
575  N N   . LEU A 97  ? 0.4461 0.5369 0.6420 -0.0178 -0.0161 0.0798  97  LEU A N   
576  C CA  . LEU A 97  ? 0.5252 0.5813 0.7078 -0.0215 -0.0198 0.0784  97  LEU A CA  
577  C C   . LEU A 97  ? 0.4968 0.5286 0.6833 -0.0330 -0.0344 0.0685  97  LEU A C   
578  O O   . LEU A 97  ? 0.4934 0.5006 0.6858 -0.0428 -0.0392 0.0715  97  LEU A O   
579  C CB  . LEU A 97  ? 0.4590 0.5008 0.6151 -0.0060 -0.0152 0.0686  97  LEU A CB  
580  C CG  . LEU A 97  ? 0.5603 0.5719 0.7058 -0.0036 -0.0176 0.0657  97  LEU A CG  
581  C CD1 . LEU A 97  ? 0.6443 0.6521 0.8000 -0.0107 -0.0159 0.0847  97  LEU A CD1 
582  C CD2 . LEU A 97  ? 0.6340 0.6455 0.7586 0.0108  -0.0121 0.0579  97  LEU A CD2 
583  N N   . LEU A 98  ? 0.4827 0.5201 0.6653 -0.0328 -0.0428 0.0570  98  LEU A N   
584  C CA  . LEU A 98  ? 0.5181 0.5358 0.6991 -0.0460 -0.0575 0.0453  98  LEU A CA  
585  C C   . LEU A 98  ? 0.6152 0.6422 0.8253 -0.0661 -0.0659 0.0555  98  LEU A C   
586  O O   . LEU A 98  ? 0.6270 0.6273 0.8371 -0.0803 -0.0771 0.0466  98  LEU A O   
587  C CB  . LEU A 98  ? 0.4833 0.5090 0.6491 -0.0428 -0.0659 0.0341  98  LEU A CB  
588  C CG  . LEU A 98  ? 0.5649 0.5708 0.6996 -0.0294 -0.0592 0.0213  98  LEU A CG  
589  C CD1 . LEU A 98  ? 0.5130 0.5296 0.6303 -0.0248 -0.0644 0.0168  98  LEU A CD1 
590  C CD2 . LEU A 98  ? 0.6465 0.6181 0.7680 -0.0343 -0.0614 0.0053  98  LEU A CD2 
591  N N   . GLN A 99  ? 0.5468 0.6118 0.7828 -0.0685 -0.0600 0.0728  99  GLN A N   
592  C CA  . GLN A 99  ? 0.6496 0.7289 0.9179 -0.0902 -0.0661 0.0859  99  GLN A CA  
593  C C   . GLN A 99  ? 0.6094 0.6565 0.8789 -0.1008 -0.0640 0.0940  99  GLN A C   
594  O O   . GLN A 99  ? 0.5903 0.6185 0.8739 -0.1215 -0.0763 0.0945  99  GLN A O   
595  C CB  . GLN A 99  ? 0.5622 0.6942 0.8598 -0.0883 -0.0548 0.1033  99  GLN A CB  
596  C CG  . GLN A 99  ? 0.9294 1.1007 1.2536 -0.0911 -0.0647 0.1036  99  GLN A CG  
597  C CD  . GLN A 99  ? 0.9729 1.1937 1.3197 -0.0759 -0.0481 0.1135  99  GLN A CD  
598  O OE1 . GLN A 99  ? 1.0273 1.2681 1.3808 -0.0613 -0.0515 0.1085  99  GLN A OE1 
599  N NE2 . GLN A 99  ? 0.7181 0.9574 1.0757 -0.0789 -0.0298 0.1274  99  GLN A NE2 
600  N N   . THR A 100 ? 0.5926 0.6323 0.8484 -0.0877 -0.0503 0.1016  100 THR A N   
601  C CA  . THR A 100 ? 0.6102 0.6209 0.8689 -0.0960 -0.0495 0.1150  100 THR A CA  
602  C C   . THR A 100 ? 0.7830 0.7403 1.0262 -0.0917 -0.0590 0.0970  100 THR A C   
603  O O   . THR A 100 ? 0.6820 0.6047 0.9363 -0.1040 -0.0666 0.1023  100 THR A O   
604  C CB  . THR A 100 ? 0.6138 0.6398 0.8612 -0.0838 -0.0336 0.1308  100 THR A CB  
605  O OG1 . THR A 100 ? 0.9400 1.0163 1.2023 -0.0880 -0.0218 0.1450  100 THR A OG1 
606  C CG2 . THR A 100 ? 0.7037 0.6997 0.9535 -0.0920 -0.0356 0.1491  100 THR A CG2 
607  N N   . GLU A 101 ? 0.5441 0.4945 0.7637 -0.0745 -0.0580 0.0758  101 GLU A N   
608  C CA  . GLU A 101 ? 0.6889 0.5966 0.8933 -0.0663 -0.0623 0.0556  101 GLU A CA  
609  C C   . GLU A 101 ? 0.6011 0.5084 0.7885 -0.0665 -0.0689 0.0303  101 GLU A C   
610  O O   . GLU A 101 ? 0.6032 0.5180 0.7689 -0.0514 -0.0630 0.0188  101 GLU A O   
611  C CB  . GLU A 101 ? 0.6433 0.5476 0.8333 -0.0451 -0.0519 0.0571  101 GLU A CB  
612  C CG  . GLU A 101 ? 0.6948 0.5927 0.8965 -0.0457 -0.0489 0.0817  101 GLU A CG  
613  C CD  . GLU A 101 ? 0.8478 0.7481 1.0359 -0.0262 -0.0416 0.0841  101 GLU A CD  
614  O OE1 . GLU A 101 ? 0.7615 0.6483 0.9394 -0.0126 -0.0411 0.0639  101 GLU A OE1 
615  O OE2 . GLU A 101 ? 0.8188 0.7373 1.0063 -0.0259 -0.0364 0.1062  101 GLU A OE2 
616  N N   . PRO A 102 ? 0.6941 0.5930 0.8891 -0.0855 -0.0823 0.0221  102 PRO A N   
617  C CA  . PRO A 102 ? 0.6734 0.5769 0.8479 -0.0889 -0.0910 0.0006  102 PRO A CA  
618  C C   . PRO A 102 ? 0.7239 0.5991 0.8689 -0.0764 -0.0869 -0.0255 102 PRO A C   
619  O O   . PRO A 102 ? 0.7400 0.6276 0.8601 -0.0739 -0.0885 -0.0387 102 PRO A O   
620  C CB  . PRO A 102 ? 0.7054 0.5995 0.8953 -0.1150 -0.1083 -0.0031 102 PRO A CB  
621  C CG  . PRO A 102 ? 0.6710 0.5621 0.8938 -0.1260 -0.1069 0.0207  102 PRO A CG  
622  C CD  . PRO A 102 ? 0.6814 0.5614 0.9017 -0.1068 -0.0917 0.0317  102 PRO A CD  
623  N N   . GLN A 103 ? 0.7387 0.5785 0.8875 -0.0683 -0.0814 -0.0320 103 GLN A N   
624  C CA  . GLN A 103 ? 0.7513 0.5673 0.8787 -0.0549 -0.0749 -0.0586 103 GLN A CA  
625  C C   . GLN A 103 ? 0.6987 0.5305 0.8195 -0.0326 -0.0601 -0.0531 103 GLN A C   
626  O O   . GLN A 103 ? 0.8682 0.6868 0.9770 -0.0201 -0.0522 -0.0730 103 GLN A O   
627  C CB  . GLN A 103 ? 0.8063 0.5730 0.9474 -0.0559 -0.0779 -0.0718 103 GLN A CB  
628  C CG  . GLN A 103 ? 1.0442 0.7884 1.1940 -0.0809 -0.0941 -0.0782 103 GLN A CG  
629  C CD  . GLN A 103 ? 1.1090 0.8662 1.2302 -0.0944 -0.1027 -0.1003 103 GLN A CD  
630  O OE1 . GLN A 103 ? 0.9616 0.7402 1.0884 -0.1142 -0.1159 -0.0902 103 GLN A OE1 
631  N NE2 . GLN A 103 ? 1.0477 0.7961 1.1382 -0.0839 -0.0953 -0.1294 103 GLN A NE2 
632  N N   . ASN A 104 ? 0.6578 0.5188 0.7866 -0.0279 -0.0557 -0.0285 104 ASN A N   
633  C CA  . ASN A 104 ? 0.6757 0.5501 0.7992 -0.0095 -0.0439 -0.0228 104 ASN A CA  
634  C C   . ASN A 104 ? 0.6270 0.5172 0.7239 -0.0040 -0.0388 -0.0383 104 ASN A C   
635  O O   . ASN A 104 ? 0.5698 0.4841 0.6567 -0.0083 -0.0410 -0.0315 104 ASN A O   
636  C CB  . ASN A 104 ? 0.5602 0.4606 0.6942 -0.0086 -0.0409 0.0039  104 ASN A CB  
637  C CG  . ASN A 104 ? 0.6492 0.5601 0.7784 0.0075  -0.0316 0.0103  104 ASN A CG  
638  O OD1 . ASN A 104 ? 0.6179 0.5348 0.7321 0.0164  -0.0264 -0.0025 104 ASN A OD1 
639  N ND2 . ASN A 104 ? 0.6718 0.5870 0.8129 0.0092  -0.0302 0.0312  104 ASN A ND2 
640  N N   . ASN A 105 ? 0.6186 0.4965 0.7063 0.0059  -0.0315 -0.0575 105 ASN A N   
641  C CA  . ASN A 105 ? 0.5965 0.4892 0.6565 0.0073  -0.0257 -0.0721 105 ASN A CA  
642  C C   . ASN A 105 ? 0.5960 0.5150 0.6514 0.0159  -0.0184 -0.0587 105 ASN A C   
643  O O   . ASN A 105 ? 0.6099 0.5442 0.6432 0.0122  -0.0172 -0.0614 105 ASN A O   
644  C CB  . ASN A 105 ? 0.5716 0.4470 0.6243 0.0141  -0.0174 -0.0995 105 ASN A CB  
645  C CG  . ASN A 105 ? 0.8132 0.6813 0.8914 0.0324  -0.0088 -0.0978 105 ASN A CG  
646  O OD1 . ASN A 105 ? 0.6319 0.4819 0.7354 0.0353  -0.0144 -0.0857 105 ASN A OD1 
647  N ND2 . ASN A 105 ? 0.5931 0.4772 0.6664 0.0438  0.0041  -0.1083 105 ASN A ND2 
648  N N   . GLN A 106 ? 0.5909 0.5144 0.6646 0.0255  -0.0151 -0.0434 106 GLN A N   
649  C CA  . GLN A 106 ? 0.5989 0.5452 0.6662 0.0304  -0.0104 -0.0322 106 GLN A CA  
650  C C   . GLN A 106 ? 0.6573 0.6166 0.7197 0.0231  -0.0161 -0.0195 106 GLN A C   
651  O O   . GLN A 106 ? 0.5263 0.4986 0.5752 0.0232  -0.0147 -0.0172 106 GLN A O   
652  C CB  . GLN A 106 ? 0.5448 0.4947 0.6293 0.0405  -0.0076 -0.0198 106 GLN A CB  
653  C CG  . GLN A 106 ? 0.6606 0.6088 0.7539 0.0517  -0.0013 -0.0299 106 GLN A CG  
654  C CD  . GLN A 106 ? 0.7447 0.6928 0.8588 0.0603  -0.0039 -0.0144 106 GLN A CD  
655  O OE1 . GLN A 106 ? 0.7623 0.6905 0.8932 0.0618  -0.0091 -0.0085 106 GLN A OE1 
656  N NE2 . GLN A 106 ? 0.5980 0.5674 0.7099 0.0640  -0.0022 -0.0055 106 GLN A NE2 
657  N N   . ALA A 107 ? 0.5156 0.4720 0.5922 0.0169  -0.0222 -0.0101 107 ALA A N   
658  C CA  . ALA A 107 ? 0.4992 0.4726 0.5779 0.0119  -0.0265 0.0007  107 ALA A CA  
659  C C   . ALA A 107 ? 0.4784 0.4545 0.5426 0.0041  -0.0344 -0.0074 107 ALA A C   
660  O O   . ALA A 107 ? 0.5235 0.5131 0.5811 0.0058  -0.0362 -0.0018 107 ALA A O   
661  C CB  . ALA A 107 ? 0.5668 0.5423 0.6677 0.0050  -0.0299 0.0132  107 ALA A CB  
662  N N   . LYS A 108 ? 0.4906 0.4521 0.5483 -0.0046 -0.0401 -0.0208 108 LYS A N   
663  C CA  . LYS A 108 ? 0.5169 0.4828 0.5549 -0.0142 -0.0495 -0.0279 108 LYS A CA  
664  C C   . LYS A 108 ? 0.5157 0.4882 0.5287 -0.0096 -0.0441 -0.0304 108 LYS A C   
665  O O   . LYS A 108 ? 0.5061 0.4901 0.5086 -0.0136 -0.0520 -0.0226 108 LYS A O   
666  C CB  . LYS A 108 ? 0.5382 0.4849 0.5672 -0.0250 -0.0553 -0.0467 108 LYS A CB  
667  C CG  . LYS A 108 ? 0.6247 0.5783 0.6341 -0.0399 -0.0700 -0.0518 108 LYS A CG  
668  C CD  . LYS A 108 ? 0.5779 0.5509 0.6116 -0.0468 -0.0836 -0.0331 108 LYS A CD  
669  C CE  . LYS A 108 ? 0.7330 0.7148 0.7507 -0.0630 -0.1025 -0.0366 108 LYS A CE  
670  N NZ  . LYS A 108 ? 0.6203 0.6289 0.6673 -0.0677 -0.1167 -0.0168 108 LYS A NZ  
671  N N   . GLU A 109 ? 0.5151 0.4820 0.5220 -0.0016 -0.0315 -0.0388 109 GLU A N   
672  C CA  . GLU A 109 ? 0.5394 0.5152 0.5257 0.0001  -0.0251 -0.0392 109 GLU A CA  
673  C C   . GLU A 109 ? 0.5864 0.5724 0.5787 0.0046  -0.0268 -0.0215 109 GLU A C   
674  O O   . GLU A 109 ? 0.5740 0.5648 0.5496 0.0005  -0.0304 -0.0155 109 GLU A O   
675  C CB  . GLU A 109 ? 0.5337 0.5077 0.5217 0.0083  -0.0109 -0.0506 109 GLU A CB  
676  C CG  . GLU A 109 ? 0.6645 0.6520 0.6378 0.0085  -0.0029 -0.0478 109 GLU A CG  
677  C CD  . GLU A 109 ? 0.6955 0.6882 0.6364 -0.0034 -0.0033 -0.0542 109 GLU A CD  
678  O OE1 . GLU A 109 ? 0.7894 0.7754 0.7165 -0.0112 -0.0099 -0.0641 109 GLU A OE1 
679  O OE2 . GLU A 109 ? 0.7964 0.8002 0.7238 -0.0072 0.0020  -0.0483 109 GLU A OE2 
680  N N   . LEU A 110 ? 0.5760 0.5637 0.5904 0.0127  -0.0240 -0.0131 110 LEU A N   
681  C CA  . LEU A 110 ? 0.4792 0.4743 0.4986 0.0179  -0.0245 -0.0009 110 LEU A CA  
682  C C   . LEU A 110 ? 0.5712 0.5722 0.5946 0.0148  -0.0359 0.0076  110 LEU A C   
683  O O   . LEU A 110 ? 0.5253 0.5275 0.5457 0.0179  -0.0389 0.0152  110 LEU A O   
684  C CB  . LEU A 110 ? 0.4891 0.4876 0.5266 0.0257  -0.0186 0.0043  110 LEU A CB  
685  C CG  . LEU A 110 ? 0.5790 0.5842 0.6210 0.0322  -0.0166 0.0119  110 LEU A CG  
686  C CD1 . LEU A 110 ? 0.5337 0.5336 0.5601 0.0326  -0.0152 0.0101  110 LEU A CD1 
687  C CD2 . LEU A 110 ? 0.5077 0.5187 0.5598 0.0372  -0.0098 0.0154  110 LEU A CD2 
688  N N   . GLU A 111 ? 0.5427 0.5467 0.5753 0.0083  -0.0439 0.0070  111 GLU A N   
689  C CA  . GLU A 111 ? 0.5243 0.5395 0.5652 0.0048  -0.0573 0.0163  111 GLU A CA  
690  C C   . GLU A 111 ? 0.6055 0.6176 0.6197 -0.0023 -0.0669 0.0173  111 GLU A C   
691  O O   . GLU A 111 ? 0.5523 0.5697 0.5698 0.0008  -0.0758 0.0297  111 GLU A O   
692  C CB  . GLU A 111 ? 0.6035 0.6251 0.6617 -0.0042 -0.0653 0.0155  111 GLU A CB  
693  C CG  . GLU A 111 ? 0.7216 0.7629 0.7984 -0.0074 -0.0804 0.0270  111 GLU A CG  
694  C CD  . GLU A 111 ? 0.6999 0.7466 0.7858 -0.0232 -0.0933 0.0238  111 GLU A CD  
695  O OE1 . GLU A 111 ? 0.7107 0.7422 0.7716 -0.0348 -0.0984 0.0105  111 GLU A OE1 
696  O OE2 . GLU A 111 ? 0.7145 0.7822 0.8336 -0.0247 -0.0981 0.0337  111 GLU A OE2 
697  N N   . ARG A 112 ? 0.5913 0.5952 0.5792 -0.0116 -0.0653 0.0046  112 ARG A N   
698  C CA  . ARG A 112 ? 0.6460 0.6493 0.6012 -0.0206 -0.0712 0.0057  112 ARG A CA  
699  C C   . ARG A 112 ? 0.5933 0.5941 0.5433 -0.0147 -0.0669 0.0175  112 ARG A C   
700  O O   . ARG A 112 ? 0.6031 0.6050 0.5438 -0.0182 -0.0790 0.0318  112 ARG A O   
701  C CB  . ARG A 112 ? 0.6587 0.6557 0.5872 -0.0287 -0.0624 -0.0144 112 ARG A CB  
702  C CG  . ARG A 112 ? 0.8173 0.8181 0.7053 -0.0424 -0.0678 -0.0157 112 ARG A CG  
703  C CD  . ARG A 112 ? 0.7565 0.7550 0.6191 -0.0463 -0.0511 -0.0379 112 ARG A CD  
704  N NE  . ARG A 112 ? 0.8044 0.8048 0.6757 -0.0369 -0.0336 -0.0372 112 ARG A NE  
705  C CZ  . ARG A 112 ? 0.8539 0.8622 0.7062 -0.0419 -0.0276 -0.0287 112 ARG A CZ  
706  N NH1 . ARG A 112 ? 0.8254 0.8384 0.6468 -0.0555 -0.0378 -0.0167 112 ARG A NH1 
707  N NH2 . ARG A 112 ? 0.7613 0.7736 0.6268 -0.0346 -0.0127 -0.0298 112 ARG A NH2 
708  N N   . LEU A 113 ? 0.5716 0.5679 0.5305 -0.0060 -0.0522 0.0135  113 LEU A N   
709  C CA  . LEU A 113 ? 0.4928 0.4837 0.4479 -0.0028 -0.0491 0.0228  113 LEU A CA  
710  C C   . LEU A 113 ? 0.6222 0.6103 0.5970 0.0059  -0.0589 0.0369  113 LEU A C   
711  O O   . LEU A 113 ? 0.5812 0.5609 0.5481 0.0042  -0.0663 0.0492  113 LEU A O   
712  C CB  . LEU A 113 ? 0.5278 0.5174 0.4904 0.0034  -0.0340 0.0148  113 LEU A CB  
713  C CG  . LEU A 113 ? 0.5595 0.5541 0.5097 -0.0014 -0.0222 0.0016  113 LEU A CG  
714  C CD1 . LEU A 113 ? 0.5776 0.5748 0.5406 0.0052  -0.0117 -0.0011 113 LEU A CD1 
715  C CD2 . LEU A 113 ? 0.6300 0.6279 0.5505 -0.0144 -0.0222 0.0038  113 LEU A CD2 
716  N N   . ILE A 114 ? 0.5876 0.5828 0.5901 0.0155  -0.0584 0.0358  114 ILE A N   
717  C CA  . ILE A 114 ? 0.6257 0.6224 0.6515 0.0265  -0.0651 0.0462  114 ILE A CA  
718  C C   . ILE A 114 ? 0.5452 0.5457 0.5700 0.0220  -0.0841 0.0599  114 ILE A C   
719  O O   . ILE A 114 ? 0.5744 0.5651 0.6028 0.0274  -0.0925 0.0722  114 ILE A O   
720  C CB  . ILE A 114 ? 0.5272 0.5387 0.5830 0.0356  -0.0588 0.0426  114 ILE A CB  
721  C CG1 . ILE A 114 ? 0.6077 0.6155 0.6621 0.0404  -0.0425 0.0332  114 ILE A CG1 
722  C CG2 . ILE A 114 ? 0.5528 0.5720 0.6372 0.0488  -0.0641 0.0512  114 ILE A CG2 
723  C CD1 . ILE A 114 ? 0.5172 0.5381 0.5851 0.0393  -0.0361 0.0296  114 ILE A CD1 
724  N N   . ASP A 115 ? 0.5792 0.5920 0.5989 0.0116  -0.0931 0.0585  115 ASP A N   
725  C CA  . ASP A 115 ? 0.6086 0.6288 0.6240 0.0047  -0.1145 0.0723  115 ASP A CA  
726  C C   . ASP A 115 ? 0.6703 0.6754 0.6558 -0.0015 -0.1210 0.0842  115 ASP A C   
727  O O   . ASP A 115 ? 0.6718 0.6754 0.6645 0.0016  -0.1378 0.1031  115 ASP A O   
728  C CB  . ASP A 115 ? 0.6512 0.6821 0.6513 -0.0113 -0.1223 0.0640  115 ASP A CB  
729  C CG  . ASP A 115 ? 0.9610 1.0105 0.9969 -0.0095 -0.1264 0.0619  115 ASP A CG  
730  O OD1 . ASP A 115 ? 0.8546 0.9154 0.9280 0.0046  -0.1254 0.0704  115 ASP A OD1 
731  O OD2 . ASP A 115 ? 0.8696 0.9227 0.8968 -0.0231 -0.1305 0.0513  115 ASP A OD2 
732  N N   . LYS A 116 ? 0.6213 0.6163 0.5759 -0.0102 -0.1079 0.0751  116 LYS A N   
733  C CA  . LYS A 116 ? 0.7743 0.7584 0.6980 -0.0205 -0.1126 0.0880  116 LYS A CA  
734  C C   . LYS A 116 ? 0.6096 0.5744 0.5492 -0.0100 -0.1127 0.1006  116 LYS A C   
735  O O   . LYS A 116 ? 0.6466 0.6002 0.5782 -0.0137 -0.1275 0.1214  116 LYS A O   
736  C CB  . LYS A 116 ? 0.7232 0.7085 0.6141 -0.0330 -0.0960 0.0734  116 LYS A CB  
737  C CG  . LYS A 116 ? 0.8547 0.8334 0.7136 -0.0466 -0.0969 0.0872  116 LYS A CG  
738  C CD  . LYS A 116 ? 0.9276 0.9195 0.7490 -0.0624 -0.0858 0.0736  116 LYS A CD  
739  C CE  . LYS A 116 ? 0.9682 0.9627 0.7980 -0.0578 -0.0624 0.0551  116 LYS A CE  
740  N NZ  . LYS A 116 ? 1.0994 1.0803 0.9519 -0.0497 -0.0594 0.0647  116 LYS A NZ  
741  N N   . ALA A 117 ? 0.6606 0.6192 0.6215 0.0022  -0.0979 0.0886  117 ALA A N   
742  C CA  . ALA A 117 ? 0.6401 0.5766 0.6146 0.0116  -0.0977 0.0957  117 ALA A CA  
743  C C   . ALA A 117 ? 0.7306 0.6627 0.7353 0.0265  -0.1132 0.1090  117 ALA A C   
744  O O   . ALA A 117 ? 0.6272 0.5349 0.6390 0.0323  -0.1202 0.1205  117 ALA A O   
745  C CB  . ALA A 117 ? 0.6612 0.5953 0.6489 0.0207  -0.0797 0.0775  117 ALA A CB  
746  N N   . MET A 118 ? 0.5976 0.5528 0.6238 0.0331  -0.1192 0.1077  118 MET A N   
747  C CA  . MET A 118 ? 0.6254 0.5846 0.6885 0.0493  -0.1332 0.1200  118 MET A CA  
748  C C   . MET A 118 ? 0.6318 0.5832 0.6857 0.0432  -0.1579 0.1458  118 MET A C   
749  O O   . MET A 118 ? 0.7225 0.6677 0.8085 0.0592  -0.1709 0.1595  118 MET A O   
750  C CB  . MET A 118 ? 0.5832 0.5758 0.6746 0.0545  -0.1332 0.1134  118 MET A CB  
751  C CG  . MET A 118 ? 0.7403 0.7413 0.8493 0.0643  -0.1109 0.0937  118 MET A CG  
752  S SD  . MET A 118 ? 0.8145 0.8555 0.9554 0.0644  -0.1106 0.0898  118 MET A SD  
753  C CE  . MET A 118 ? 0.7097 0.7680 0.9058 0.0880  -0.1184 0.1005  118 MET A CE  
754  N N   . LYS A 119 ? 0.6702 0.6230 0.6815 0.0212  -0.1647 0.1533  119 LYS A N   
755  C CA  . LYS A 119 ? 0.7036 0.6529 0.7019 0.0130  -0.1907 0.1813  119 LYS A CA  
756  C C   . LYS A 119 ? 0.7382 0.6516 0.7314 0.0144  -0.1961 0.2000  119 LYS A C   
757  O O   . LYS A 119 ? 0.7382 0.6419 0.7437 0.0192  -0.2195 0.2263  119 LYS A O   
758  C CB  . LYS A 119 ? 0.8470 0.8117 0.7958 -0.0129 -0.1954 0.1820  119 LYS A CB  
759  C CG  . LYS A 119 ? 0.8462 0.8405 0.7996 -0.0167 -0.1939 0.1636  119 LYS A CG  
760  C CD  . LYS A 119 ? 0.9461 0.9503 0.8467 -0.0415 -0.1942 0.1564  119 LYS A CD  
761  C CE  . LYS A 119 ? 1.0363 1.0607 0.9429 -0.0452 -0.1898 0.1331  119 LYS A CE  
762  N NZ  . LYS A 119 ? 1.1228 1.1414 1.0077 -0.0506 -0.1633 0.1062  119 LYS A NZ  
763  N N   . LYS A 120 ? 0.7089 0.6019 0.6861 0.0093  -0.1770 0.1885  120 LYS A N   
764  C CA  . LYS A 120 ? 0.7290 0.5851 0.6996 0.0058  -0.1829 0.2066  120 LYS A CA  
765  C C   . LYS A 120 ? 0.6679 0.5055 0.6418 0.0084  -0.1605 0.1856  120 LYS A C   
766  O O   . LYS A 120 ? 0.7656 0.6208 0.7227 -0.0003 -0.1415 0.1653  120 LYS A O   
767  C CB  . LYS A 120 ? 0.7454 0.6005 0.6676 -0.0217 -0.1923 0.2290  120 LYS A CB  
768  C CG  . LYS A 120 ? 0.7727 0.5883 0.6887 -0.0288 -0.2035 0.2559  120 LYS A CG  
769  C CD  . LYS A 120 ? 0.8200 0.6413 0.6902 -0.0552 -0.2193 0.2865  120 LYS A CD  
770  C CE  . LYS A 120 ? 0.8741 0.6535 0.7398 -0.0641 -0.2333 0.3191  120 LYS A CE  
771  N NZ  . LYS A 120 ? 0.9263 0.7133 0.7442 -0.0915 -0.2495 0.3532  120 LYS A NZ  
772  N N   . ASP A 121 ? 0.7903 0.5919 0.7868 0.0204  -0.1642 0.1899  121 ASP A N   
773  C CA  . ASP A 121 ? 0.7220 0.5042 0.7203 0.0210  -0.1461 0.1694  121 ASP A CA  
774  C C   . ASP A 121 ? 0.7551 0.5342 0.7150 -0.0072 -0.1393 0.1752  121 ASP A C   
775  O O   . ASP A 121 ? 0.8145 0.5759 0.7557 -0.0234 -0.1522 0.2016  121 ASP A O   
776  C CB  . ASP A 121 ? 0.7911 0.5299 0.8191 0.0382  -0.1534 0.1716  121 ASP A CB  
777  C CG  . ASP A 121 ? 0.9365 0.6562 0.9656 0.0388  -0.1361 0.1461  121 ASP A CG  
778  O OD1 . ASP A 121 ? 0.8591 0.6020 0.8961 0.0488  -0.1195 0.1202  121 ASP A OD1 
779  O OD2 . ASP A 121 ? 0.9435 0.6250 0.9643 0.0271  -0.1403 0.1533  121 ASP A OD2 
780  N N   . GLY A 122 ? 0.7958 0.5950 0.7458 -0.0135 -0.1193 0.1527  122 GLY A N   
781  C CA  . GLY A 122 ? 0.9540 0.7573 0.8756 -0.0383 -0.1101 0.1556  122 GLY A CA  
782  C C   . GLY A 122 ? 0.8903 0.7087 0.8159 -0.0381 -0.0904 0.1292  122 GLY A C   
783  O O   . GLY A 122 ? 0.7431 0.5588 0.6904 -0.0203 -0.0850 0.1104  122 GLY A O   
784  N N   . LEU A 123 ? 0.9089 0.7464 0.8132 -0.0585 -0.0797 0.1293  123 LEU A N   
785  C CA  . LEU A 123 ? 0.7226 0.5808 0.6314 -0.0606 -0.0626 0.1081  123 LEU A CA  
786  C C   . LEU A 123 ? 0.8443 0.7355 0.7547 -0.0497 -0.0530 0.0916  123 LEU A C   
787  O O   . LEU A 123 ? 0.7994 0.7113 0.6916 -0.0573 -0.0507 0.0950  123 LEU A O   
788  C CB  . LEU A 123 ? 0.8182 0.6884 0.7099 -0.0863 -0.0550 0.1167  123 LEU A CB  
789  C CG  . LEU A 123 ? 0.7729 0.6622 0.6743 -0.0932 -0.0412 0.1012  123 LEU A CG  
790  C CD1 . LEU A 123 ? 0.7236 0.5809 0.6418 -0.0900 -0.0479 0.0952  123 LEU A CD1 
791  C CD2 . LEU A 123 ? 0.6957 0.6080 0.5816 -0.1198 -0.0321 0.1130  123 LEU A CD2 
792  N N   . LEU A 124 ? 0.7359 0.6309 0.6659 -0.0335 -0.0474 0.0734  124 LEU A N   
793  C CA  . LEU A 124 ? 0.7741 0.6950 0.7089 -0.0237 -0.0396 0.0596  124 LEU A CA  
794  C C   . LEU A 124 ? 0.8621 0.8096 0.7874 -0.0344 -0.0265 0.0521  124 LEU A C   
795  O O   . LEU A 124 ? 0.8752 0.8271 0.8000 -0.0451 -0.0206 0.0520  124 LEU A O   
796  C CB  . LEU A 124 ? 0.7135 0.6327 0.6690 -0.0072 -0.0360 0.0455  124 LEU A CB  
797  C CG  . LEU A 124 ? 0.8091 0.7069 0.7790 0.0068  -0.0448 0.0485  124 LEU A CG  
798  C CD1 . LEU A 124 ? 0.7819 0.6856 0.7672 0.0212  -0.0374 0.0329  124 LEU A CD1 
799  C CD2 . LEU A 124 ? 0.6369 0.5387 0.6093 0.0114  -0.0548 0.0596  124 LEU A CD2 
800  N N   . GLU A 125 ? 0.9268 0.8927 0.8472 -0.0312 -0.0222 0.0447  125 GLU A N   
801  C CA  . GLU A 125 ? 0.9072 0.8979 0.8213 -0.0379 -0.0084 0.0347  125 GLU A CA  
802  C C   . GLU A 125 ? 0.9457 0.9484 0.8817 -0.0300 0.0006  0.0224  125 GLU A C   
803  O O   . GLU A 125 ? 0.9636 0.9583 0.9152 -0.0181 -0.0030 0.0185  125 GLU A O   
804  C CB  . GLU A 125 ? 1.0130 1.0146 0.9169 -0.0354 -0.0066 0.0260  125 GLU A CB  
805  C CG  . GLU A 125 ? 1.1353 1.1439 1.0078 -0.0512 -0.0067 0.0326  125 GLU A CG  
806  C CD  . GLU A 125 ? 1.1556 1.1710 1.0151 -0.0497 -0.0076 0.0208  125 GLU A CD  
807  O OE1 . GLU A 125 ? 1.1057 1.1315 0.9748 -0.0424 0.0038  0.0015  125 GLU A OE1 
808  O OE2 . GLU A 125 ? 1.1201 1.1296 0.9598 -0.0566 -0.0208 0.0310  125 GLU A OE2 
809  N N   . VAL A 126 ? 1.1185 1.1445 1.0555 -0.0371 0.0126  0.0168  126 VAL A N   
810  C CA  . VAL A 126 ? 1.1542 1.1969 1.1145 -0.0309 0.0192  0.0081  126 VAL A CA  
811  C C   . VAL A 126 ? 1.1314 1.1739 1.1065 -0.0134 0.0190  -0.0020 126 VAL A C   
812  O O   . VAL A 126 ? 1.1696 1.2063 1.1378 -0.0084 0.0183  -0.0065 126 VAL A O   
813  C CB  . VAL A 126 ? 1.1648 1.2389 1.1284 -0.0400 0.0334  0.0038  126 VAL A CB  
814  C CG1 . VAL A 126 ? 1.0832 1.1579 1.0294 -0.0613 0.0339  0.0176  126 VAL A CG1 
815  C CG2 . VAL A 126 ? 1.2644 1.3509 1.2207 -0.0342 0.0436  -0.0089 126 VAL A CG2 
816  N N   . LEU A 127 ? 1.0936 1.1420 1.0880 -0.0062 0.0179  -0.0042 127 LEU A N   
817  C CA  . LEU A 127 ? 1.1703 1.2178 1.1789 0.0085  0.0165  -0.0091 127 LEU A CA  
818  C C   . LEU A 127 ? 1.2045 1.2646 1.2314 0.0129  0.0144  -0.0083 127 LEU A C   
819  O O   . LEU A 127 ? 1.0740 1.1569 1.1177 0.0138  0.0195  -0.0112 127 LEU A O   
820  C CB  . LEU A 127 ? 0.8802 0.9063 0.8815 0.0133  0.0087  -0.0053 127 LEU A CB  
821  C CG  . LEU A 127 ? 1.0606 1.0821 1.0625 0.0190  0.0090  -0.0097 127 LEU A CG  
822  C CD1 . LEU A 127 ? 0.7396 0.7481 0.7419 0.0231  0.0017  -0.0042 127 LEU A CD1 
823  C CD2 . LEU A 127 ? 0.9189 0.9494 0.9394 0.0280  0.0136  -0.0161 127 LEU A CD2 
824  N N   . VAL B 30  ? 1.2104 1.3899 1.0220 0.1603  -0.1385 -0.2606 30  VAL B N   
825  C CA  . VAL B 30  ? 1.1827 1.3592 0.9943 0.1498  -0.1117 -0.2566 30  VAL B CA  
826  C C   . VAL B 30  ? 1.1405 1.3128 1.0301 0.1212  -0.0958 -0.2533 30  VAL B C   
827  O O   . VAL B 30  ? 1.1115 1.2752 1.0025 0.1084  -0.0690 -0.2303 30  VAL B O   
828  C CB  . VAL B 30  ? 1.2261 1.4184 1.0181 0.1700  -0.1253 -0.2973 30  VAL B CB  
829  C CG1 . VAL B 30  ? 1.2731 1.4633 0.9679 0.1990  -0.1287 -0.2903 30  VAL B CG1 
830  C CG2 . VAL B 30  ? 1.1420 1.3525 0.9887 0.1738  -0.1588 -0.3448 30  VAL B CG2 
831  N N   . SER B 31  ? 1.0907 1.2697 1.0438 0.1120  -0.1118 -0.2761 31  SER B N   
832  C CA  . SER B 31  ? 0.9843 1.1547 1.0061 0.0890  -0.0985 -0.2824 31  SER B CA  
833  C C   . SER B 31  ? 0.9563 1.1092 0.9920 0.0698  -0.0739 -0.2421 31  SER B C   
834  O O   . SER B 31  ? 0.9475 1.0971 0.9607 0.0692  -0.0721 -0.2154 31  SER B O   
835  C CB  . SER B 31  ? 0.9022 1.0843 0.9887 0.0808  -0.1181 -0.3169 31  SER B CB  
836  O OG  . SER B 31  ? 0.8354 0.9997 0.9817 0.0551  -0.0990 -0.3098 31  SER B OG  
837  N N   . LYS B 32  ? 0.8411 0.9792 0.9131 0.0558  -0.0566 -0.2399 32  LYS B N   
838  C CA  . LYS B 32  ? 0.7199 0.8418 0.8047 0.0405  -0.0356 -0.2059 32  LYS B CA  
839  C C   . LYS B 32  ? 0.7614 0.8775 0.8886 0.0255  -0.0369 -0.2011 32  LYS B C   
840  O O   . LYS B 32  ? 0.5860 0.6959 0.7056 0.0190  -0.0278 -0.1725 32  LYS B O   
841  C CB  . LYS B 32  ? 0.6052 0.7113 0.7080 0.0369  -0.0195 -0.2058 32  LYS B CB  
842  C CG  . LYS B 32  ? 0.7161 0.8024 0.8400 0.0231  -0.0026 -0.1780 32  LYS B CG  
843  C CD  . LYS B 32  ? 0.8458 0.9068 0.9961 0.0222  0.0073  -0.1858 32  LYS B CD  
844  C CE  . LYS B 32  ? 0.7214 0.7888 0.8475 0.0362  0.0158  -0.1802 32  LYS B CE  
845  N NZ  . LYS B 32  ? 0.8789 0.9162 1.0241 0.0380  0.0267  -0.1739 32  LYS B NZ  
846  N N   . SER B 33  ? 0.5803 0.6993 0.7551 0.0187  -0.0462 -0.2306 33  SER B N   
847  C CA  . SER B 33  ? 0.5317 0.6530 0.7495 0.0042  -0.0448 -0.2286 33  SER B CA  
848  C C   . SER B 33  ? 0.5805 0.7250 0.7776 0.0160  -0.0623 -0.2254 33  SER B C   
849  O O   . SER B 33  ? 0.6302 0.7736 0.8367 0.0098  -0.0560 -0.2065 33  SER B O   
850  C CB  . SER B 33  ? 0.5121 0.6354 0.7919 -0.0091 -0.0485 -0.2642 33  SER B CB  
851  O OG  . SER B 33  ? 0.6996 0.8428 0.9767 0.0038  -0.0722 -0.3023 33  SER B OG  
852  N N   . THR B 34  ? 0.5832 0.7458 0.7464 0.0364  -0.0848 -0.2436 34  THR B N   
853  C CA  . THR B 34  ? 0.7483 0.9255 0.8806 0.0537  -0.1038 -0.2391 34  THR B CA  
854  C C   . THR B 34  ? 0.6139 0.7690 0.7002 0.0538  -0.0885 -0.1959 34  THR B C   
855  O O   . THR B 34  ? 0.6026 0.7571 0.6918 0.0550  -0.0915 -0.1831 34  THR B O   
856  C CB  . THR B 34  ? 0.8322 1.0245 0.9194 0.0799  -0.1291 -0.2621 34  THR B CB  
857  O OG1 . THR B 34  ? 0.8266 1.0456 0.9643 0.0807  -0.1501 -0.3090 34  THR B OG1 
858  C CG2 . THR B 34  ? 0.6826 0.8763 0.7169 0.1032  -0.1464 -0.2481 34  THR B CG2 
859  N N   . GLN B 35  ? 0.5524 0.6909 0.6005 0.0518  -0.0715 -0.1754 35  GLN B N   
860  C CA  . GLN B 35  ? 0.6283 0.7474 0.6406 0.0473  -0.0558 -0.1378 35  GLN B CA  
861  C C   . GLN B 35  ? 0.5546 0.6640 0.6064 0.0295  -0.0423 -0.1223 35  GLN B C   
862  O O   . GLN B 35  ? 0.5827 0.6814 0.6199 0.0293  -0.0412 -0.1026 35  GLN B O   
863  C CB  . GLN B 35  ? 0.6065 0.7193 0.5853 0.0451  -0.0380 -0.1242 35  GLN B CB  
864  C CG  . GLN B 35  ? 0.7583 0.8777 0.6837 0.0636  -0.0455 -0.1334 35  GLN B CG  
865  C CD  . GLN B 35  ? 0.9086 1.0233 0.7963 0.0592  -0.0223 -0.1120 35  GLN B CD  
866  O OE1 . GLN B 35  ? 1.0316 1.1314 0.8786 0.0567  -0.0128 -0.0856 35  GLN B OE1 
867  N NE2 . GLN B 35  ? 0.9532 1.0803 0.8582 0.0572  -0.0116 -0.1242 35  GLN B NE2 
868  N N   . PHE B 36  ? 0.5604 0.6684 0.6574 0.0162  -0.0312 -0.1306 36  PHE B N   
869  C CA  . PHE B 36  ? 0.6058 0.7010 0.7292 0.0021  -0.0162 -0.1132 36  PHE B CA  
870  C C   . PHE B 36  ? 0.5477 0.6534 0.6999 0.0016  -0.0245 -0.1212 36  PHE B C   
871  O O   . PHE B 36  ? 0.5599 0.6568 0.7087 -0.0017 -0.0174 -0.1024 36  PHE B O   
872  C CB  . PHE B 36  ? 0.4586 0.5414 0.6156 -0.0093 -0.0010 -0.1172 36  PHE B CB  
873  C CG  . PHE B 36  ? 0.6420 0.7095 0.8205 -0.0211 0.0146  -0.1006 36  PHE B CG  
874  C CD1 . PHE B 36  ? 0.5756 0.6300 0.7286 -0.0220 0.0247  -0.0737 36  PHE B CD1 
875  C CD2 . PHE B 36  ? 0.5814 0.6509 0.8049 -0.0312 0.0190  -0.1136 36  PHE B CD2 
876  C CE1 . PHE B 36  ? 0.6381 0.6781 0.8025 -0.0293 0.0377  -0.0592 36  PHE B CE1 
877  C CE2 . PHE B 36  ? 0.6108 0.6659 0.8473 -0.0408 0.0366  -0.0969 36  PHE B CE2 
878  C CZ  . PHE B 36  ? 0.6221 0.6607 0.8245 -0.0379 0.0450  -0.0693 36  PHE B CZ  
879  N N   . GLU B 37  ? 0.4938 0.6218 0.6775 0.0057  -0.0400 -0.1521 37  GLU B N   
880  C CA  . GLU B 37  ? 0.5005 0.6488 0.7205 0.0065  -0.0482 -0.1645 37  GLU B CA  
881  C C   . GLU B 37  ? 0.6604 0.8095 0.8376 0.0259  -0.0637 -0.1521 37  GLU B C   
882  O O   . GLU B 37  ? 0.5778 0.7271 0.7653 0.0263  -0.0605 -0.1428 37  GLU B O   
883  C CB  . GLU B 37  ? 0.5726 0.7521 0.8410 0.0070  -0.0648 -0.2058 37  GLU B CB  
884  C CG  . GLU B 37  ? 0.8592 1.0324 1.1816 -0.0163 -0.0474 -0.2213 37  GLU B CG  
885  C CD  . GLU B 37  ? 0.6445 0.8058 1.0047 -0.0370 -0.0198 -0.2064 37  GLU B CD  
886  O OE1 . GLU B 37  ? 0.6648 0.8408 1.0336 -0.0341 -0.0192 -0.1995 37  GLU B OE1 
887  O OE2 . GLU B 37  ? 0.7288 0.8633 1.1067 -0.0542 0.0019  -0.2018 37  GLU B OE2 
888  N N   . GLU B 38  ? 0.5901 0.7349 0.7142 0.0435  -0.0789 -0.1510 38  GLU B N   
889  C CA  . GLU B 38  ? 0.6049 0.7353 0.6755 0.0621  -0.0901 -0.1331 38  GLU B CA  
890  C C   . GLU B 38  ? 0.6588 0.7586 0.7088 0.0504  -0.0696 -0.0989 38  GLU B C   
891  O O   . GLU B 38  ? 0.6278 0.7175 0.6686 0.0580  -0.0738 -0.0888 38  GLU B O   
892  C CB  . GLU B 38  ? 0.7432 0.8647 0.7506 0.0797  -0.1016 -0.1316 38  GLU B CB  
893  C CG  . GLU B 38  ? 0.9413 1.0367 0.8840 0.1000  -0.1114 -0.1107 38  GLU B CG  
894  C CD  . GLU B 38  ? 1.2028 1.2884 1.0772 0.1206  -0.1224 -0.1105 38  GLU B CD  
895  O OE1 . GLU B 38  ? 1.1847 1.2940 1.0687 0.1246  -0.1304 -0.1357 38  GLU B OE1 
896  O OE2 . GLU B 38  ? 1.0784 1.1290 0.8864 0.1332  -0.1221 -0.0853 38  GLU B OE2 
897  N N   . ALA B 39  ? 0.6539 0.7400 0.6979 0.0337  -0.0491 -0.0835 39  ALA B N   
898  C CA  . ALA B 39  ? 0.6553 0.7168 0.6810 0.0229  -0.0329 -0.0553 39  ALA B CA  
899  C C   . ALA B 39  ? 0.5736 0.6364 0.6386 0.0149  -0.0250 -0.0541 39  ALA B C   
900  O O   . ALA B 39  ? 0.4971 0.5421 0.5454 0.0150  -0.0218 -0.0381 39  ALA B O   
901  C CB  . ALA B 39  ? 0.5735 0.6296 0.5907 0.0099  -0.0159 -0.0445 39  ALA B CB  
902  N N   . TRP B 40  ? 0.4815 0.5624 0.5967 0.0071  -0.0199 -0.0712 40  TRP B N   
903  C CA  . TRP B 40  ? 0.5034 0.5871 0.6544 -0.0004 -0.0084 -0.0707 40  TRP B CA  
904  C C   . TRP B 40  ? 0.5404 0.6334 0.6928 0.0139  -0.0212 -0.0759 40  TRP B C   
905  O O   . TRP B 40  ? 0.4930 0.5770 0.6465 0.0129  -0.0121 -0.0653 40  TRP B O   
906  C CB  . TRP B 40  ? 0.5688 0.6690 0.7744 -0.0122 0.0005  -0.0908 40  TRP B CB  
907  C CG  . TRP B 40  ? 0.7774 0.8752 1.0149 -0.0237 0.0213  -0.0858 40  TRP B CG  
908  C CD1 . TRP B 40  ? 0.7432 0.8156 0.9712 -0.0336 0.0429  -0.0657 40  TRP B CD1 
909  C CD2 . TRP B 40  ? 0.6745 0.7979 0.9556 -0.0242 0.0234  -0.1018 40  TRP B CD2 
910  N NE1 . TRP B 40  ? 0.7539 0.8296 1.0101 -0.0406 0.0605  -0.0657 40  TRP B NE1 
911  C CE2 . TRP B 40  ? 0.7493 0.8587 1.0424 -0.0366 0.0506  -0.0883 40  TRP B CE2 
912  C CE3 . TRP B 40  ? 0.6099 0.7698 0.9211 -0.0132 0.0044  -0.1276 40  TRP B CE3 
913  C CZ2 . TRP B 40  ? 0.8232 0.9547 1.1589 -0.0413 0.0640  -0.0990 40  TRP B CZ2 
914  C CZ3 . TRP B 40  ? 0.8646 1.0518 1.2255 -0.0171 0.0146  -0.1412 40  TRP B CZ3 
915  C CH2 . TRP B 40  ? 0.8614 1.0347 1.2350 -0.0326 0.0464  -0.1264 40  TRP B CH2 
916  N N   . CYS B 41  ? 0.5677 0.6788 0.7175 0.0308  -0.0441 -0.0941 41  CYS B N   
917  C CA  . CYS B 41  ? 0.5566 0.6773 0.7062 0.0507  -0.0603 -0.1012 41  CYS B CA  
918  C C   . CYS B 41  ? 0.6738 0.7545 0.7613 0.0614  -0.0634 -0.0749 41  CYS B C   
919  O O   . CYS B 41  ? 0.6171 0.6890 0.7033 0.0693  -0.0633 -0.0699 41  CYS B O   
920  C CB  . CYS B 41  ? 0.6713 0.8226 0.8311 0.0706  -0.0881 -0.1295 41  CYS B CB  
921  S SG  . CYS B 41  ? 0.5960 0.7981 0.8411 0.0558  -0.0872 -0.1689 41  CYS B SG  
922  N N   . LEU B 42  ? 0.5673 0.6220 0.6039 0.0604  -0.0639 -0.0589 42  LEU B N   
923  C CA  . LEU B 42  ? 0.6655 0.6774 0.6430 0.0668  -0.0647 -0.0345 42  LEU B CA  
924  C C   . LEU B 42  ? 0.6277 0.6185 0.6075 0.0496  -0.0458 -0.0170 42  LEU B C   
925  O O   . LEU B 42  ? 0.6646 0.6247 0.6166 0.0563  -0.0481 -0.0053 42  LEU B O   
926  C CB  . LEU B 42  ? 0.6446 0.6385 0.5732 0.0648  -0.0631 -0.0224 42  LEU B CB  
927  C CG  . LEU B 42  ? 0.6623 0.6669 0.5662 0.0876  -0.0841 -0.0365 42  LEU B CG  
928  C CD1 . LEU B 42  ? 0.8227 0.8127 0.6812 0.0807  -0.0737 -0.0237 42  LEU B CD1 
929  C CD2 . LEU B 42  ? 0.6934 0.6750 0.5571 0.1165  -0.1049 -0.0332 42  LEU B CD2 
930  N N   . VAL B 43  ? 0.5397 0.5433 0.5488 0.0296  -0.0285 -0.0162 43  VAL B N   
931  C CA  . VAL B 43  ? 0.7581 0.7441 0.7651 0.0164  -0.0136 -0.0019 43  VAL B CA  
932  C C   . VAL B 43  ? 0.7883 0.7791 0.8185 0.0232  -0.0120 -0.0083 43  VAL B C   
933  O O   . VAL B 43  ? 0.7305 0.6999 0.7458 0.0206  -0.0061 0.0017  43  VAL B O   
934  C CB  . VAL B 43  ? 0.7591 0.7563 0.7845 -0.0006 0.0015  0.0005  43  VAL B CB  
935  C CG1 . VAL B 43  ? 0.7048 0.7022 0.7515 -0.0072 0.0149  0.0031  43  VAL B CG1 
936  C CG2 . VAL B 43  ? 0.5551 0.5379 0.5487 -0.0100 0.0058  0.0143  43  VAL B CG2 
937  N N   . ARG B 44  ? 0.6455 0.6667 0.7136 0.0323  -0.0174 -0.0276 44  ARG B N   
938  C CA  . ARG B 44  ? 0.5995 0.6363 0.6980 0.0402  -0.0140 -0.0384 44  ARG B CA  
939  C C   . ARG B 44  ? 0.7184 0.7460 0.7968 0.0652  -0.0335 -0.0429 44  ARG B C   
940  O O   . ARG B 44  ? 0.7437 0.7894 0.8489 0.0768  -0.0332 -0.0556 44  ARG B O   
941  C CB  . ARG B 44  ? 0.6817 0.7616 0.8400 0.0350  -0.0087 -0.0606 44  ARG B CB  
942  C CG  . ARG B 44  ? 0.9469 1.0487 1.1478 0.0323  0.0084  -0.0701 44  ARG B CG  
943  C CD  . ARG B 44  ? 1.0543 1.2039 1.3179 0.0312  0.0060  -0.0988 44  ARG B CD  
944  N NE  . ARG B 44  ? 0.9373 1.1137 1.2514 0.0224  0.0296  -0.1093 44  ARG B NE  
945  C CZ  . ARG B 44  ? 1.0179 1.1830 1.3428 0.0011  0.0603  -0.0982 44  ARG B CZ  
946  N NH1 . ARG B 44  ? 0.8567 0.9859 1.1471 -0.0106 0.0679  -0.0775 44  ARG B NH1 
947  N NH2 . ARG B 44  ? 1.0440 1.2344 1.4139 -0.0069 0.0849  -0.1081 44  ARG B NH2 
948  N N   . SER B 45  ? 0.6915 0.6894 0.7213 0.0751  -0.0488 -0.0327 45  SER B N   
949  C CA  . SER B 45  ? 0.7294 0.7153 0.7356 0.1044  -0.0709 -0.0380 45  SER B CA  
950  C C   . SER B 45  ? 0.8597 0.8030 0.8340 0.1119  -0.0695 -0.0256 45  SER B C   
951  O O   . SER B 45  ? 0.8751 0.7887 0.8295 0.0930  -0.0550 -0.0093 45  SER B O   
952  C CB  . SER B 45  ? 0.7337 0.6979 0.6913 0.1146  -0.0865 -0.0302 45  SER B CB  
953  O OG  . SER B 45  ? 0.7838 0.7094 0.6939 0.1418  -0.1040 -0.0234 45  SER B OG  
954  N N   . LYS B 46  ? 0.9669 0.9088 0.9380 0.1422  -0.0871 -0.0368 46  LYS B N   
955  C CA  . LYS B 46  ? 0.8526 0.7484 0.7901 0.1559  -0.0899 -0.0287 46  LYS B CA  
956  C C   . LYS B 46  ? 0.9116 0.7377 0.7780 0.1545  -0.0945 -0.0038 46  LYS B C   
957  O O   . LYS B 46  ? 1.0394 0.8174 0.8769 0.1488  -0.0883 0.0078  46  LYS B O   
958  C CB  . LYS B 46  ? 0.8770 0.7957 0.8345 0.1933  -0.1091 -0.0508 46  LYS B CB  
959  C CG  . LYS B 46  ? 1.0956 0.9558 0.9967 0.2264  -0.1292 -0.0438 46  LYS B CG  
960  C CD  . LYS B 46  ? 1.2873 1.0876 1.1535 0.2178  -0.1177 -0.0288 46  LYS B CD  
961  C CE  . LYS B 46  ? 1.3685 1.1228 1.1989 0.2566  -0.1369 -0.0321 46  LYS B CE  
962  N NZ  . LYS B 46  ? 1.2796 0.9988 1.1015 0.2490  -0.1241 -0.0306 46  LYS B NZ  
963  N N   . TYR B 47  ? 0.9428 0.7607 0.7794 0.1577  -0.1032 0.0039  47  TYR B N   
964  C CA  . TYR B 47  ? 0.9778 0.7263 0.7423 0.1587  -0.1049 0.0287  47  TYR B CA  
965  C C   . TYR B 47  ? 1.0273 0.7641 0.7820 0.1200  -0.0820 0.0464  47  TYR B C   
966  O O   . TYR B 47  ? 0.9572 0.7382 0.7409 0.1042  -0.0743 0.0411  47  TYR B O   
967  C CB  . TYR B 47  ? 1.1000 0.8415 0.8260 0.1898  -0.1271 0.0283  47  TYR B CB  
968  C CG  . TYR B 47  ? 1.0399 0.8071 0.7858 0.2312  -0.1535 0.0050  47  TYR B CG  
969  C CD1 . TYR B 47  ? 1.0214 0.8671 0.8317 0.2392  -0.1638 -0.0247 47  TYR B CD1 
970  C CD2 . TYR B 47  ? 1.0795 0.7937 0.7842 0.2623  -0.1679 0.0102  47  TYR B CD2 
971  C CE1 . TYR B 47  ? 0.9766 0.8567 0.8155 0.2765  -0.1880 -0.0506 47  TYR B CE1 
972  C CE2 . TYR B 47  ? 1.1782 0.9229 0.9058 0.3044  -0.1938 -0.0145 47  TYR B CE2 
973  C CZ  . TYR B 47  ? 1.0573 0.8899 0.8552 0.3109  -0.2037 -0.0458 47  TYR B CZ  
974  O OH  . TYR B 47  ? 1.2270 1.1005 1.0577 0.3516  -0.2292 -0.0746 47  TYR B OH  
975  N N   . ASN B 48  ? 0.9969 0.6745 0.7131 0.1051  -0.0714 0.0651  48  ASN B N   
976  C CA  . ASN B 48  ? 1.0860 0.7583 0.8010 0.0675  -0.0496 0.0782  48  ASN B CA  
977  C C   . ASN B 48  ? 1.1854 0.8611 0.8734 0.0617  -0.0440 0.0893  48  ASN B C   
978  O O   . ASN B 48  ? 1.0053 0.7115 0.7157 0.0358  -0.0282 0.0902  48  ASN B O   
979  C CB  . ASN B 48  ? 1.1287 0.7361 0.8114 0.0520  -0.0406 0.0921  48  ASN B CB  
980  C CG  . ASN B 48  ? 1.2984 0.9167 1.0172 0.0436  -0.0385 0.0788  48  ASN B CG  
981  O OD1 . ASN B 48  ? 1.1262 0.7808 0.8781 0.0618  -0.0470 0.0620  48  ASN B OD1 
982  N ND2 . ASN B 48  ? 1.2731 0.8625 0.9866 0.0155  -0.0262 0.0846  48  ASN B ND2 
983  N N   . ASP B 49  ? 1.1543 0.7994 0.7912 0.0884  -0.0571 0.0970  49  ASP B N   
984  C CA  . ASP B 49  ? 1.1432 0.7927 0.7472 0.0876  -0.0522 0.1060  49  ASP B CA  
985  C C   . ASP B 49  ? 1.0237 0.7483 0.6795 0.0871  -0.0564 0.0844  49  ASP B C   
986  O O   . ASP B 49  ? 0.9966 0.7413 0.6522 0.0700  -0.0424 0.0875  49  ASP B O   
987  C CB  . ASP B 49  ? 1.2699 0.8732 0.8038 0.1246  -0.0702 0.1159  49  ASP B CB  
988  C CG  . ASP B 49  ? 1.4555 0.9712 0.9177 0.1170  -0.0555 0.1465  49  ASP B CG  
989  O OD1 . ASP B 49  ? 1.5530 1.0221 1.0073 0.1205  -0.0588 0.1508  49  ASP B OD1 
990  O OD2 . ASP B 49  ? 1.5266 1.0181 0.9401 0.1067  -0.0387 0.1656  49  ASP B OD2 
991  N N   . ASP B 50  ? 0.9155 0.6815 0.6177 0.1052  -0.0740 0.0611  50  ASP B N   
992  C CA  . ASP B 50  ? 0.8201 0.6519 0.5769 0.1010  -0.0761 0.0391  50  ASP B CA  
993  C C   . ASP B 50  ? 0.8238 0.6787 0.6228 0.0670  -0.0534 0.0402  50  ASP B C   
994  O O   . ASP B 50  ? 0.8030 0.6895 0.6207 0.0559  -0.0464 0.0338  50  ASP B O   
995  C CB  . ASP B 50  ? 0.7754 0.6454 0.5789 0.1230  -0.0954 0.0136  50  ASP B CB  
996  C CG  . ASP B 50  ? 1.0926 0.9715 0.8732 0.1586  -0.1231 0.0003  50  ASP B CG  
997  O OD1 . ASP B 50  ? 0.8730 0.8029 0.7060 0.1728  -0.1389 -0.0281 50  ASP B OD1 
998  O OD2 . ASP B 50  ? 1.1556 0.9919 0.8658 0.1719  -0.1281 0.0175  50  ASP B OD2 
999  N N   . ILE B 51  ? 0.7910 0.6295 0.6029 0.0532  -0.0436 0.0466  51  ILE B N   
1000 C CA  . ILE B 51  ? 0.8082 0.6682 0.6549 0.0261  -0.0257 0.0469  51  ILE B CA  
1001 C C   . ILE B 51  ? 0.8478 0.7002 0.6721 0.0061  -0.0109 0.0600  51  ILE B C   
1002 O O   . ILE B 51  ? 0.7132 0.5997 0.5655 -0.0065 -0.0017 0.0544  51  ILE B O   
1003 C CB  . ILE B 51  ? 0.8209 0.6635 0.6779 0.0187  -0.0210 0.0491  51  ILE B CB  
1004 C CG1 . ILE B 51  ? 0.7611 0.6159 0.6411 0.0401  -0.0324 0.0347  51  ILE B CG1 
1005 C CG2 . ILE B 51  ? 0.6559 0.5238 0.5453 -0.0034 -0.0065 0.0476  51  ILE B CG2 
1006 C CD1 . ILE B 51  ? 0.7630 0.5933 0.6404 0.0398  -0.0299 0.0359  51  ILE B CD1 
1007 N N   . ARG B 52  ? 0.7375 0.5439 0.5113 0.0032  -0.0066 0.0775  52  ARG B N   
1008 C CA  . ARG B 52  ? 0.8195 0.6218 0.5738 -0.0178 0.0122  0.0897  52  ARG B CA  
1009 C C   . ARG B 52  ? 0.8085 0.6454 0.5622 -0.0097 0.0119  0.0821  52  ARG B C   
1010 O O   . ARG B 52  ? 0.7683 0.6346 0.5408 -0.0260 0.0263  0.0798  52  ARG B O   
1011 C CB  . ARG B 52  ? 0.8351 0.5750 0.5288 -0.0212 0.0199  0.1114  52  ARG B CB  
1012 C CG  . ARG B 52  ? 1.1038 0.7971 0.7895 -0.0252 0.0173  0.1173  52  ARG B CG  
1013 C CD  . ARG B 52  ? 1.1764 0.8164 0.8256 -0.0507 0.0377  0.1372  52  ARG B CD  
1014 N NE  . ARG B 52  ? 1.3482 0.9550 1.0075 -0.0607 0.0353  0.1351  52  ARG B NE  
1015 C CZ  . ARG B 52  ? 1.3743 0.9282 1.0027 -0.0400 0.0214  0.1387  52  ARG B CZ  
1016 N NH1 . ARG B 52  ? 1.5814 1.1074 1.1644 -0.0074 0.0079  0.1463  52  ARG B NH1 
1017 N NH2 . ARG B 52  ? 1.4513 0.9807 1.0936 -0.0491 0.0190  0.1321  52  ARG B NH2 
1018 N N   . LYS B 53  ? 0.7512 0.5860 0.4822 0.0179  -0.0061 0.0759  53  LYS B N   
1019 C CA  . LYS B 53  ? 0.7930 0.6596 0.5207 0.0279  -0.0096 0.0644  53  LYS B CA  
1020 C C   . LYS B 53  ? 0.7016 0.6200 0.4943 0.0208  -0.0102 0.0431  53  LYS B C   
1021 O O   . LYS B 53  ? 0.6923 0.6368 0.4933 0.0156  -0.0024 0.0358  53  LYS B O   
1022 C CB  . LYS B 53  ? 0.7325 0.5894 0.4247 0.0619  -0.0341 0.0574  53  LYS B CB  
1023 C CG  . LYS B 53  ? 1.0387 0.8376 0.6484 0.0751  -0.0329 0.0809  53  LYS B CG  
1024 C CD  . LYS B 53  ? 1.0868 0.8726 0.6689 0.1151  -0.0644 0.0724  53  LYS B CD  
1025 C CE  . LYS B 53  ? 1.2353 0.9565 0.7222 0.1358  -0.0657 0.0971  53  LYS B CE  
1026 N NZ  . LYS B 53  ? 1.2328 0.8874 0.6857 0.1183  -0.0461 0.1266  53  LYS B NZ  
1027 N N   . GLY B 54  ? 0.6059 0.5359 0.4424 0.0212  -0.0173 0.0334  54  GLY B N   
1028 C CA  . GLY B 54  ? 0.5922 0.5597 0.4845 0.0128  -0.0136 0.0177  54  GLY B CA  
1029 C C   . GLY B 54  ? 0.6943 0.6698 0.5988 -0.0083 0.0054  0.0251  54  GLY B C   
1030 O O   . GLY B 54  ? 0.6100 0.6113 0.5389 -0.0114 0.0099  0.0145  54  GLY B O   
1031 N N   . ILE B 55  ? 0.6398 0.5935 0.5293 -0.0219 0.0151  0.0410  55  ILE B N   
1032 C CA  . ILE B 55  ? 0.5719 0.5398 0.4755 -0.0406 0.0307  0.0449  55  ILE B CA  
1033 C C   . ILE B 55  ? 0.5831 0.5653 0.4694 -0.0431 0.0406  0.0449  55  ILE B C   
1034 O O   . ILE B 55  ? 0.6375 0.6494 0.5484 -0.0487 0.0489  0.0376  55  ILE B O   
1035 C CB  . ILE B 55  ? 0.6598 0.6022 0.5522 -0.0561 0.0372  0.0577  55  ILE B CB  
1036 C CG1 . ILE B 55  ? 0.6518 0.5890 0.5663 -0.0533 0.0297  0.0538  55  ILE B CG1 
1037 C CG2 . ILE B 55  ? 0.7032 0.6643 0.6059 -0.0766 0.0533  0.0602  55  ILE B CG2 
1038 C CD1 . ILE B 55  ? 0.6488 0.5469 0.5410 -0.0608 0.0290  0.0632  55  ILE B CD1 
1039 N N   . VAL B 56  ? 0.6341 0.5940 0.4737 -0.0362 0.0404  0.0533  56  VAL B N   
1040 C CA  . VAL B 56  ? 0.6895 0.6613 0.5044 -0.0380 0.0537  0.0547  56  VAL B CA  
1041 C C   . VAL B 56  ? 0.7726 0.7792 0.6093 -0.0240 0.0460  0.0336  56  VAL B C   
1042 O O   . VAL B 56  ? 0.7062 0.7400 0.5540 -0.0289 0.0584  0.0270  56  VAL B O   
1043 C CB  . VAL B 56  ? 0.6823 0.6142 0.4308 -0.0296 0.0553  0.0707  56  VAL B CB  
1044 C CG1 . VAL B 56  ? 0.7350 0.6801 0.4487 -0.0206 0.0639  0.0678  56  VAL B CG1 
1045 C CG2 . VAL B 56  ? 0.8909 0.7862 0.6183 -0.0519 0.0730  0.0925  56  VAL B CG2 
1046 N N   . LEU B 57  ? 0.5724 0.5805 0.4217 -0.0074 0.0257  0.0199  57  LEU B N   
1047 C CA  . LEU B 57  ? 0.5341 0.5710 0.4120 0.0023  0.0179  -0.0034 57  LEU B CA  
1048 C C   . LEU B 57  ? 0.5762 0.6325 0.5021 -0.0092 0.0272  -0.0091 57  LEU B C   
1049 O O   . LEU B 57  ? 0.5900 0.6665 0.5275 -0.0068 0.0324  -0.0213 57  LEU B O   
1050 C CB  . LEU B 57  ? 0.5805 0.6182 0.4734 0.0174  -0.0042 -0.0191 57  LEU B CB  
1051 C CG  . LEU B 57  ? 0.7276 0.7559 0.5729 0.0387  -0.0202 -0.0229 57  LEU B CG  
1052 C CD1 . LEU B 57  ? 0.7393 0.7769 0.6110 0.0535  -0.0441 -0.0417 57  LEU B CD1 
1053 C CD2 . LEU B 57  ? 0.6830 0.7290 0.5092 0.0469  -0.0187 -0.0368 57  LEU B CD2 
1054 N N   . LEU B 58  ? 0.5127 0.5605 0.4627 -0.0184 0.0285  -0.0010 58  LEU B N   
1055 C CA  . LEU B 58  ? 0.5198 0.5800 0.5068 -0.0244 0.0352  -0.0044 58  LEU B CA  
1056 C C   . LEU B 58  ? 0.5240 0.6021 0.5097 -0.0316 0.0487  -0.0009 58  LEU B C   
1057 O O   . LEU B 58  ? 0.4958 0.5906 0.5049 -0.0276 0.0519  -0.0104 58  LEU B O   
1058 C CB  . LEU B 58  ? 0.4594 0.5051 0.4603 -0.0302 0.0342  0.0049  58  LEU B CB  
1059 C CG  . LEU B 58  ? 0.5499 0.5878 0.5679 -0.0237 0.0253  -0.0024 58  LEU B CG  
1060 C CD1 . LEU B 58  ? 0.4650 0.4880 0.4869 -0.0279 0.0269  0.0081  58  LEU B CD1 
1061 C CD2 . LEU B 58  ? 0.4624 0.5097 0.5130 -0.0207 0.0265  -0.0174 58  LEU B CD2 
1062 N N   . GLU B 59  ? 0.5449 0.6192 0.5056 -0.0423 0.0577  0.0119  59  GLU B N   
1063 C CA  . GLU B 59  ? 0.5455 0.6454 0.5129 -0.0520 0.0730  0.0123  59  GLU B CA  
1064 C C   . GLU B 59  ? 0.6487 0.7713 0.6100 -0.0415 0.0788  -0.0006 59  GLU B C   
1065 O O   . GLU B 59  ? 0.6998 0.8522 0.6853 -0.0394 0.0858  -0.0106 59  GLU B O   
1066 C CB  . GLU B 59  ? 0.5471 0.6341 0.4900 -0.0701 0.0854  0.0282  59  GLU B CB  
1067 C CG  . GLU B 59  ? 0.6283 0.7065 0.5897 -0.0840 0.0832  0.0346  59  GLU B CG  
1068 C CD  . GLU B 59  ? 0.9882 1.0410 0.9242 -0.1039 0.0944  0.0493  59  GLU B CD  
1069 O OE1 . GLU B 59  ? 0.9492 0.9967 0.9016 -0.1177 0.0933  0.0509  59  GLU B OE1 
1070 O OE2 . GLU B 59  ? 1.0416 1.0755 0.9379 -0.1050 0.1044  0.0591  59  GLU B OE2 
1071 N N   . GLU B 60  ? 0.5974 0.7072 0.5250 -0.0313 0.0739  -0.0030 60  GLU B N   
1072 C CA  . GLU B 60  ? 0.7178 0.8477 0.6346 -0.0185 0.0775  -0.0186 60  GLU B CA  
1073 C C   . GLU B 60  ? 0.6131 0.7527 0.5658 -0.0057 0.0659  -0.0398 60  GLU B C   
1074 O O   . GLU B 60  ? 0.5452 0.7072 0.5076 0.0024  0.0721  -0.0543 60  GLU B O   
1075 C CB  . GLU B 60  ? 0.7482 0.8600 0.6132 -0.0073 0.0716  -0.0173 60  GLU B CB  
1076 C CG  . GLU B 60  ? 0.8351 0.9659 0.6863 0.0104  0.0700  -0.0387 60  GLU B CG  
1077 C CD  . GLU B 60  ? 0.9754 1.0893 0.7673 0.0263  0.0612  -0.0389 60  GLU B CD  
1078 O OE1 . GLU B 60  ? 1.1202 1.2483 0.8811 0.0385  0.0683  -0.0498 60  GLU B OE1 
1079 O OE2 . GLU B 60  ? 0.9121 0.9993 0.6860 0.0300  0.0464  -0.0296 60  GLU B OE2 
1080 N N   . LEU B 61  ? 0.5210 0.6418 0.4942 -0.0041 0.0512  -0.0423 61  LEU B N   
1081 C CA  . LEU B 61  ? 0.5164 0.6373 0.5236 0.0040  0.0442  -0.0603 61  LEU B CA  
1082 C C   . LEU B 61  ? 0.4999 0.6297 0.5339 0.0034  0.0527  -0.0585 61  LEU B C   
1083 O O   . LEU B 61  ? 0.5380 0.6692 0.5894 0.0140  0.0518  -0.0739 61  LEU B O   
1084 C CB  . LEU B 61  ? 0.5471 0.6476 0.5738 0.0017  0.0325  -0.0617 61  LEU B CB  
1085 C CG  . LEU B 61  ? 0.6769 0.7728 0.6891 0.0072  0.0180  -0.0698 61  LEU B CG  
1086 C CD1 . LEU B 61  ? 0.6514 0.7353 0.6925 0.0017  0.0119  -0.0688 61  LEU B CD1 
1087 C CD2 . LEU B 61  ? 0.6848 0.7910 0.6988 0.0190  0.0090  -0.0969 61  LEU B CD2 
1088 N N   . LEU B 62  ? 0.5125 0.6461 0.5494 -0.0068 0.0589  -0.0418 62  LEU B N   
1089 C CA  . LEU B 62  ? 0.5815 0.7236 0.6426 -0.0040 0.0616  -0.0400 62  LEU B CA  
1090 C C   . LEU B 62  ? 0.4996 0.6680 0.5721 0.0091  0.0670  -0.0549 62  LEU B C   
1091 O O   . LEU B 62  ? 0.5655 0.7249 0.6554 0.0225  0.0629  -0.0615 62  LEU B O   
1092 C CB  . LEU B 62  ? 0.4628 0.6131 0.5225 -0.0179 0.0655  -0.0248 62  LEU B CB  
1093 C CG  . LEU B 62  ? 0.6732 0.8352 0.7543 -0.0144 0.0636  -0.0231 62  LEU B CG  
1094 C CD1 . LEU B 62  ? 0.5123 0.6433 0.5987 -0.0038 0.0557  -0.0201 62  LEU B CD1 
1095 C CD2 . LEU B 62  ? 0.6719 0.8420 0.7514 -0.0315 0.0655  -0.0128 62  LEU B CD2 
1096 N N   . PRO B 63  ? 0.5251 0.7239 0.5868 0.0077  0.0776  -0.0603 63  PRO B N   
1097 C CA  . PRO B 63  ? 0.5547 0.7831 0.6304 0.0234  0.0833  -0.0778 63  PRO B CA  
1098 C C   . PRO B 63  ? 0.6147 0.8256 0.6875 0.0405  0.0763  -0.0967 63  PRO B C   
1099 O O   . PRO B 63  ? 0.6491 0.8761 0.7340 0.0579  0.0786  -0.1135 63  PRO B O   
1100 C CB  . PRO B 63  ? 0.4565 0.7209 0.5175 0.0137  0.1011  -0.0773 63  PRO B CB  
1101 C CG  . PRO B 63  ? 0.6114 0.8522 0.6392 -0.0026 0.1027  -0.0608 63  PRO B CG  
1102 C CD  . PRO B 63  ? 0.5460 0.7522 0.5813 -0.0082 0.0877  -0.0489 63  PRO B CD  
1103 N N   . LYS B 64  ? 0.7002 0.8806 0.7605 0.0370  0.0670  -0.0977 64  LYS B N   
1104 C CA  . LYS B 64  ? 0.7765 0.9421 0.8378 0.0501  0.0592  -0.1206 64  LYS B CA  
1105 C C   . LYS B 64  ? 0.7056 0.8332 0.7921 0.0519  0.0510  -0.1233 64  LYS B C   
1106 O O   . LYS B 64  ? 0.7078 0.8170 0.8022 0.0596  0.0449  -0.1440 64  LYS B O   
1107 C CB  . LYS B 64  ? 0.7245 0.8873 0.7576 0.0471  0.0526  -0.1267 64  LYS B CB  
1108 C CG  . LYS B 64  ? 0.8640 1.0545 0.8600 0.0466  0.0645  -0.1214 64  LYS B CG  
1109 C CD  . LYS B 64  ? 0.7768 0.9630 0.7356 0.0552  0.0553  -0.1344 64  LYS B CD  
1110 C CE  . LYS B 64  ? 0.9061 1.0686 0.8593 0.0480  0.0396  -0.1259 64  LYS B CE  
1111 N NZ  . LYS B 64  ? 1.0355 1.1972 0.9350 0.0528  0.0374  -0.1191 64  LYS B NZ  
1112 N N   . GLY B 65  ? 0.6872 0.8001 0.7846 0.0448  0.0522  -0.1036 65  GLY B N   
1113 C CA  . GLY B 65  ? 0.6549 0.7269 0.7688 0.0433  0.0495  -0.1011 65  GLY B CA  
1114 C C   . GLY B 65  ? 0.6900 0.7423 0.8133 0.0601  0.0519  -0.1021 65  GLY B C   
1115 O O   . GLY B 65  ? 0.6685 0.7457 0.7902 0.0733  0.0534  -0.1014 65  GLY B O   
1116 N N   . SER B 66  ? 0.6850 0.6911 0.8189 0.0599  0.0528  -0.1044 66  SER B N   
1117 C CA  . SER B 66  ? 0.8402 0.8112 0.9740 0.0769  0.0558  -0.0984 66  SER B CA  
1118 C C   . SER B 66  ? 0.8087 0.7783 0.9314 0.0778  0.0575  -0.0721 66  SER B C   
1119 O O   . SER B 66  ? 0.6737 0.6603 0.7930 0.0615  0.0579  -0.0596 66  SER B O   
1120 C CB  . SER B 66  ? 0.8027 0.7160 0.9477 0.0714  0.0609  -0.1043 66  SER B CB  
1121 O OG  . SER B 66  ? 0.9022 0.7989 1.0514 0.0508  0.0676  -0.0876 66  SER B OG  
1122 N N   . LYS B 67  ? 0.7941 0.7404 0.9078 0.1002  0.0568  -0.0650 67  LYS B N   
1123 C CA  . LYS B 67  ? 0.7698 0.7183 0.8686 0.1065  0.0545  -0.0437 67  LYS B CA  
1124 C C   . LYS B 67  ? 0.8867 0.8033 0.9770 0.0873  0.0627  -0.0248 67  LYS B C   
1125 O O   . LYS B 67  ? 0.7442 0.6790 0.8248 0.0824  0.0601  -0.0114 67  LYS B O   
1126 C CB  . LYS B 67  ? 1.0119 0.9322 1.0961 0.1395  0.0499  -0.0398 67  LYS B CB  
1127 C CG  . LYS B 67  ? 1.0975 0.9468 1.1569 0.1439  0.0582  -0.0183 67  LYS B CG  
1128 C CD  . LYS B 67  ? 1.2413 1.0399 1.2827 0.1771  0.0563  -0.0180 67  LYS B CD  
1129 C CE  . LYS B 67  ? 1.3418 1.0615 1.3500 0.1796  0.0694  0.0081  67  LYS B CE  
1130 N NZ  . LYS B 67  ? 1.3439 1.0686 1.3190 0.1983  0.0615  0.0285  67  LYS B NZ  
1131 N N   . GLU B 68  ? 0.7024 0.5745 0.7995 0.0754  0.0733  -0.0261 68  GLU B N   
1132 C CA  . GLU B 68  ? 0.8805 0.7278 0.9758 0.0561  0.0850  -0.0108 68  GLU B CA  
1133 C C   . GLU B 68  ? 0.8765 0.7654 0.9883 0.0337  0.0816  -0.0175 68  GLU B C   
1134 O O   . GLU B 68  ? 0.7769 0.6718 0.8819 0.0243  0.0846  -0.0040 68  GLU B O   
1135 C CB  . GLU B 68  ? 0.8072 0.5959 0.9120 0.0479  0.1005  -0.0125 68  GLU B CB  
1136 C CG  . GLU B 68  ? 0.9802 0.7640 1.1041 0.0198  0.1137  -0.0099 68  GLU B CG  
1137 C CD  . GLU B 68  ? 1.0589 0.7772 1.1803 0.0118  0.1374  0.0029  68  GLU B CD  
1138 O OE1 . GLU B 68  ? 1.3479 1.0165 1.4376 0.0315  0.1436  0.0187  68  GLU B OE1 
1139 O OE2 . GLU B 68  ? 1.0317 0.7480 1.1828 -0.0138 0.1508  -0.0032 68  GLU B OE2 
1140 N N   . GLU B 69  ? 0.7689 0.6841 0.8983 0.0281  0.0747  -0.0390 69  GLU B N   
1141 C CA  . GLU B 69  ? 0.7409 0.6925 0.8772 0.0130  0.0688  -0.0445 69  GLU B CA  
1142 C C   . GLU B 69  ? 0.7342 0.7177 0.8522 0.0148  0.0632  -0.0315 69  GLU B C   
1143 O O   . GLU B 69  ? 0.6437 0.6374 0.7584 0.0035  0.0621  -0.0240 69  GLU B O   
1144 C CB  . GLU B 69  ? 0.8817 0.8540 1.0286 0.0131  0.0605  -0.0697 69  GLU B CB  
1145 C CG  . GLU B 69  ? 0.6762 0.6245 0.8495 0.0040  0.0627  -0.0890 69  GLU B CG  
1146 C CD  . GLU B 69  ? 0.7238 0.6875 0.9020 0.0111  0.0525  -0.1176 69  GLU B CD  
1147 O OE1 . GLU B 69  ? 0.7658 0.7486 0.9259 0.0265  0.0489  -0.1205 69  GLU B OE1 
1148 O OE2 . GLU B 69  ? 0.8843 0.8452 1.0856 0.0016  0.0478  -0.1398 69  GLU B OE2 
1149 N N   . GLN B 70  ? 0.5762 0.5757 0.6854 0.0293  0.0597  -0.0307 70  GLN B N   
1150 C CA  . GLN B 70  ? 0.6635 0.6963 0.7633 0.0272  0.0553  -0.0225 70  GLN B CA  
1151 C C   . GLN B 70  ? 0.6615 0.6782 0.7499 0.0246  0.0561  -0.0048 70  GLN B C   
1152 O O   . GLN B 70  ? 0.5825 0.6171 0.6650 0.0145  0.0530  0.0010  70  GLN B O   
1153 C CB  . GLN B 70  ? 0.5965 0.6567 0.6990 0.0434  0.0519  -0.0299 70  GLN B CB  
1154 C CG  . GLN B 70  ? 0.5794 0.6692 0.6881 0.0431  0.0532  -0.0472 70  GLN B CG  
1155 C CD  . GLN B 70  ? 0.8256 0.9502 0.9431 0.0598  0.0525  -0.0575 70  GLN B CD  
1156 O OE1 . GLN B 70  ? 0.6299 0.7505 0.7506 0.0774  0.0475  -0.0549 70  GLN B OE1 
1157 N NE2 . GLN B 70  ? 0.7197 0.8804 0.8394 0.0569  0.0576  -0.0701 70  GLN B NE2 
1158 N N   . ARG B 71  ? 0.6884 0.6669 0.7698 0.0339  0.0614  0.0039  71  ARG B N   
1159 C CA  . ARG B 71  ? 0.8522 0.8111 0.9161 0.0334  0.0647  0.0206  71  ARG B CA  
1160 C C   . ARG B 71  ? 0.7074 0.6649 0.7774 0.0141  0.0702  0.0228  71  ARG B C   
1161 O O   . ARG B 71  ? 0.6439 0.6078 0.7022 0.0102  0.0680  0.0306  71  ARG B O   
1162 C CB  . ARG B 71  ? 0.7978 0.7076 0.8469 0.0467  0.0746  0.0314  71  ARG B CB  
1163 C CG  . ARG B 71  ? 0.9488 0.8532 0.9868 0.0721  0.0671  0.0303  71  ARG B CG  
1164 C CD  . ARG B 71  ? 1.1269 0.9748 1.1339 0.0897  0.0758  0.0478  71  ARG B CD  
1165 N NE  . ARG B 71  ? 1.4324 1.2886 1.4188 0.1203  0.0604  0.0493  71  ARG B NE  
1166 C CZ  . ARG B 71  ? 1.3831 1.2756 1.3604 0.1281  0.0456  0.0493  71  ARG B CZ  
1167 N NH1 . ARG B 71  ? 1.1949 1.1065 1.1729 0.1087  0.0463  0.0523  71  ARG B NH1 
1168 N NH2 . ARG B 71  ? 1.3236 1.2344 1.2929 0.1572  0.0284  0.0436  71  ARG B NH2 
1169 N N   . ASP B 72  ? 0.6499 0.5988 0.7399 0.0040  0.0763  0.0134  72  ASP B N   
1170 C CA  . ASP B 72  ? 0.6320 0.5885 0.7340 -0.0108 0.0782  0.0105  72  ASP B CA  
1171 C C   . ASP B 72  ? 0.7458 0.7340 0.8415 -0.0148 0.0658  0.0070  72  ASP B C   
1172 O O   . ASP B 72  ? 0.6965 0.6878 0.7835 -0.0192 0.0641  0.0138  72  ASP B O   
1173 C CB  . ASP B 72  ? 0.6644 0.6145 0.7954 -0.0196 0.0829  -0.0054 72  ASP B CB  
1174 C CG  . ASP B 72  ? 0.7894 0.6994 0.9282 -0.0212 0.1003  -0.0006 72  ASP B CG  
1175 O OD1 . ASP B 72  ? 0.7987 0.6841 0.9147 -0.0150 0.1105  0.0185  72  ASP B OD1 
1176 O OD2 . ASP B 72  ? 0.8891 0.7889 1.0537 -0.0282 0.1041  -0.0163 72  ASP B OD2 
1177 N N   . TYR B 73  ? 0.6033 0.6116 0.7000 -0.0125 0.0588  -0.0032 73  TYR B N   
1178 C CA  . TYR B 73  ? 0.5271 0.5585 0.6115 -0.0174 0.0515  -0.0034 73  TYR B CA  
1179 C C   . TYR B 73  ? 0.6083 0.6422 0.6780 -0.0200 0.0503  0.0095  73  TYR B C   
1180 O O   . TYR B 73  ? 0.6033 0.6365 0.6624 -0.0272 0.0472  0.0141  73  TYR B O   
1181 C CB  . TYR B 73  ? 0.5666 0.6192 0.6491 -0.0132 0.0497  -0.0136 73  TYR B CB  
1182 C CG  . TYR B 73  ? 0.5794 0.6312 0.6728 -0.0092 0.0478  -0.0311 73  TYR B CG  
1183 C CD1 . TYR B 73  ? 0.5686 0.6095 0.6755 -0.0135 0.0449  -0.0393 73  TYR B CD1 
1184 C CD2 . TYR B 73  ? 0.5788 0.6448 0.6719 -0.0007 0.0482  -0.0431 73  TYR B CD2 
1185 C CE1 . TYR B 73  ? 0.5048 0.5479 0.6257 -0.0107 0.0403  -0.0606 73  TYR B CE1 
1186 C CE2 . TYR B 73  ? 0.5209 0.5852 0.6219 0.0040  0.0446  -0.0628 73  TYR B CE2 
1187 C CZ  . TYR B 73  ? 0.6907 0.7428 0.8059 -0.0016 0.0396  -0.0722 73  TYR B CZ  
1188 O OH  . TYR B 73  ? 0.5712 0.6240 0.6977 0.0025  0.0334  -0.0967 73  TYR B OH  
1189 N N   . VAL B 74  ? 0.5599 0.5942 0.6281 -0.0121 0.0510  0.0136  74  VAL B N   
1190 C CA  . VAL B 74  ? 0.6278 0.6708 0.6858 -0.0139 0.0465  0.0200  74  VAL B CA  
1191 C C   . VAL B 74  ? 0.5921 0.6135 0.6382 -0.0165 0.0470  0.0285  74  VAL B C   
1192 O O   . VAL B 74  ? 0.5749 0.5992 0.6119 -0.0241 0.0424  0.0306  74  VAL B O   
1193 C CB  . VAL B 74  ? 0.7616 0.8139 0.8210 0.0009  0.0429  0.0187  74  VAL B CB  
1194 C CG1 . VAL B 74  ? 0.6239 0.6778 0.6715 0.0030  0.0356  0.0233  74  VAL B CG1 
1195 C CG2 . VAL B 74  ? 0.5616 0.6493 0.6357 0.0017  0.0415  0.0076  74  VAL B CG2 
1196 N N   . PHE B 75  ? 0.5539 0.5520 0.6004 -0.0110 0.0547  0.0326  75  PHE B N   
1197 C CA  . PHE B 75  ? 0.6804 0.6617 0.7169 -0.0123 0.0589  0.0391  75  PHE B CA  
1198 C C   . PHE B 75  ? 0.5698 0.5564 0.6115 -0.0219 0.0557  0.0348  75  PHE B C   
1199 O O   . PHE B 75  ? 0.5753 0.5563 0.6043 -0.0231 0.0526  0.0375  75  PHE B O   
1200 C CB  . PHE B 75  ? 0.5126 0.4694 0.5522 -0.0078 0.0738  0.0442  75  PHE B CB  
1201 C CG  . PHE B 75  ? 0.7396 0.6856 0.7758 -0.0107 0.0832  0.0481  75  PHE B CG  
1202 C CD1 . PHE B 75  ? 0.7035 0.6364 0.7119 -0.0020 0.0859  0.0572  75  PHE B CD1 
1203 C CD2 . PHE B 75  ? 0.6127 0.5657 0.6743 -0.0197 0.0882  0.0397  75  PHE B CD2 
1204 C CE1 . PHE B 75  ? 0.6925 0.6180 0.6970 -0.0029 0.0969  0.0591  75  PHE B CE1 
1205 C CE2 . PHE B 75  ? 0.7828 0.7329 0.8470 -0.0207 0.0980  0.0405  75  PHE B CE2 
1206 C CZ  . PHE B 75  ? 0.6665 0.6021 0.7013 -0.0126 0.1040  0.0508  75  PHE B CZ  
1207 N N   . TYR B 76  ? 0.5328 0.5282 0.5899 -0.0258 0.0546  0.0265  76  TYR B N   
1208 C CA  . TYR B 76  ? 0.5437 0.5426 0.6007 -0.0290 0.0483  0.0220  76  TYR B CA  
1209 C C   . TYR B 76  ? 0.6057 0.6065 0.6412 -0.0333 0.0402  0.0260  76  TYR B C   
1210 O O   . TYR B 76  ? 0.5157 0.5067 0.5391 -0.0332 0.0348  0.0276  76  TYR B O   
1211 C CB  . TYR B 76  ? 0.6581 0.6672 0.7349 -0.0287 0.0463  0.0092  76  TYR B CB  
1212 C CG  . TYR B 76  ? 0.7507 0.7559 0.8561 -0.0299 0.0567  0.0027  76  TYR B CG  
1213 C CD1 . TYR B 76  ? 0.8860 0.8912 1.0037 -0.0304 0.0614  0.0010  76  TYR B CD1 
1214 C CD2 . TYR B 76  ? 0.7575 0.7577 0.8788 -0.0314 0.0639  -0.0025 76  TYR B CD2 
1215 C CE1 . TYR B 76  ? 1.0137 1.0178 1.1625 -0.0359 0.0760  -0.0054 76  TYR B CE1 
1216 C CE2 . TYR B 76  ? 0.8353 0.8257 0.9837 -0.0370 0.0774  -0.0076 76  TYR B CE2 
1217 C CZ  . TYR B 76  ? 0.8958 0.8899 1.0595 -0.0411 0.0849  -0.0088 76  TYR B CZ  
1218 O OH  . TYR B 76  ? 0.9935 0.9802 1.1890 -0.0508 0.1032  -0.0144 76  TYR B OH  
1219 N N   . LEU B 77  ? 0.4744 0.4866 0.5062 -0.0371 0.0406  0.0273  77  LEU B N   
1220 C CA  . LEU B 77  ? 0.5511 0.5646 0.5670 -0.0466 0.0383  0.0315  77  LEU B CA  
1221 C C   . LEU B 77  ? 0.5581 0.5591 0.5658 -0.0498 0.0355  0.0355  77  LEU B C   
1222 O O   . LEU B 77  ? 0.5558 0.5420 0.5483 -0.0578 0.0329  0.0388  77  LEU B O   
1223 C CB  . LEU B 77  ? 0.4971 0.5353 0.5207 -0.0508 0.0423  0.0282  77  LEU B CB  
1224 C CG  . LEU B 77  ? 0.5663 0.6151 0.5857 -0.0506 0.0457  0.0240  77  LEU B CG  
1225 C CD1 . LEU B 77  ? 0.5956 0.6725 0.6310 -0.0471 0.0506  0.0160  77  LEU B CD1 
1226 C CD2 . LEU B 77  ? 0.6074 0.6467 0.6020 -0.0617 0.0487  0.0313  77  LEU B CD2 
1227 N N   . ALA B 78  ? 0.5054 0.5079 0.5186 -0.0423 0.0358  0.0351  78  ALA B N   
1228 C CA  . ALA B 78  ? 0.5461 0.5365 0.5469 -0.0416 0.0313  0.0360  78  ALA B CA  
1229 C C   . ALA B 78  ? 0.6733 0.6411 0.6634 -0.0389 0.0311  0.0376  78  ALA B C   
1230 O O   . ALA B 78  ? 0.5848 0.5370 0.5611 -0.0439 0.0257  0.0370  78  ALA B O   
1231 C CB  . ALA B 78  ? 0.5768 0.5694 0.5758 -0.0285 0.0320  0.0366  78  ALA B CB  
1232 N N   . VAL B 79  ? 0.5600 0.5264 0.5596 -0.0311 0.0371  0.0375  79  VAL B N   
1233 C CA  . VAL B 79  ? 0.6017 0.5560 0.5989 -0.0255 0.0368  0.0354  79  VAL B CA  
1234 C C   . VAL B 79  ? 0.5714 0.5140 0.5557 -0.0284 0.0275  0.0353  79  VAL B C   
1235 O O   . VAL B 79  ? 0.6407 0.5632 0.6096 -0.0247 0.0225  0.0349  79  VAL B O   
1236 C CB  . VAL B 79  ? 0.6322 0.5971 0.6537 -0.0206 0.0452  0.0310  79  VAL B CB  
1237 C CG1 . VAL B 79  ? 0.7082 0.6718 0.7354 -0.0131 0.0425  0.0243  79  VAL B CG1 
1238 C CG2 . VAL B 79  ? 0.6381 0.6011 0.6644 -0.0177 0.0592  0.0348  79  VAL B CG2 
1239 N N   . GLY B 80  ? 0.6605 0.6110 0.6459 -0.0327 0.0256  0.0360  80  GLY B N   
1240 C CA  . GLY B 80  ? 0.5904 0.5227 0.5534 -0.0327 0.0186  0.0393  80  GLY B CA  
1241 C C   . GLY B 80  ? 0.7044 0.6120 0.6453 -0.0441 0.0181  0.0458  80  GLY B C   
1242 O O   . GLY B 80  ? 0.7159 0.5921 0.6345 -0.0402 0.0125  0.0488  80  GLY B O   
1243 N N   . ASN B 81  ? 0.6337 0.5549 0.5827 -0.0578 0.0231  0.0460  81  ASN B N   
1244 C CA  . ASN B 81  ? 0.6707 0.5744 0.6086 -0.0733 0.0231  0.0475  81  ASN B CA  
1245 C C   . ASN B 81  ? 0.6531 0.5355 0.5838 -0.0678 0.0163  0.0424  81  ASN B C   
1246 O O   . ASN B 81  ? 0.7134 0.5632 0.6269 -0.0759 0.0134  0.0429  81  ASN B O   
1247 C CB  . ASN B 81  ? 0.6154 0.5516 0.5741 -0.0866 0.0278  0.0431  81  ASN B CB  
1248 C CG  . ASN B 81  ? 0.5663 0.5136 0.5243 -0.0998 0.0379  0.0479  81  ASN B CG  
1249 O OD1 . ASN B 81  ? 0.6957 0.6216 0.6389 -0.1161 0.0442  0.0535  81  ASN B OD1 
1250 N ND2 . ASN B 81  ? 0.5995 0.5774 0.5716 -0.0927 0.0416  0.0455  81  ASN B ND2 
1251 N N   . TYR B 82  ? 0.6692 0.5664 0.6102 -0.0543 0.0153  0.0373  82  TYR B N   
1252 C CA  . TYR B 82  ? 0.6933 0.5724 0.6231 -0.0449 0.0108  0.0314  82  TYR B CA  
1253 C C   . TYR B 82  ? 0.7200 0.5682 0.6336 -0.0352 0.0069  0.0323  82  TYR B C   
1254 O O   . TYR B 82  ? 0.7929 0.6097 0.6886 -0.0354 0.0010  0.0283  82  TYR B O   
1255 C CB  . TYR B 82  ? 0.6739 0.5725 0.6125 -0.0306 0.0162  0.0295  82  TYR B CB  
1256 C CG  . TYR B 82  ? 0.7913 0.6752 0.7167 -0.0162 0.0166  0.0241  82  TYR B CG  
1257 C CD1 . TYR B 82  ? 0.7394 0.6115 0.6470 -0.0145 0.0100  0.0163  82  TYR B CD1 
1258 C CD2 . TYR B 82  ? 0.8190 0.7055 0.7523 -0.0035 0.0235  0.0235  82  TYR B CD2 
1259 C CE1 . TYR B 82  ? 0.8090 0.6684 0.7005 0.0011  0.0117  0.0098  82  TYR B CE1 
1260 C CE2 . TYR B 82  ? 0.9023 0.7806 0.8257 0.0107  0.0270  0.0170  82  TYR B CE2 
1261 C CZ  . TYR B 82  ? 0.9520 0.8149 0.8513 0.0138  0.0218  0.0110  82  TYR B CZ  
1262 O OH  . TYR B 82  ? 0.8659 0.7210 0.7514 0.0302  0.0266  0.0031  82  TYR B OH  
1263 N N   . ARG B 83  ? 0.7181 0.5746 0.6383 -0.0248 0.0081  0.0351  83  ARG B N   
1264 C CA  . ARG B 83  ? 0.8423 0.6739 0.7481 -0.0097 0.0009  0.0338  83  ARG B CA  
1265 C C   . ARG B 83  ? 0.9519 0.7413 0.8269 -0.0174 -0.0043 0.0420  83  ARG B C   
1266 O O   . ARG B 83  ? 0.8053 0.5569 0.6582 -0.0061 -0.0116 0.0408  83  ARG B O   
1267 C CB  . ARG B 83  ? 0.6867 0.5434 0.6108 0.0040  -0.0001 0.0308  83  ARG B CB  
1268 C CG  . ARG B 83  ? 0.6649 0.5560 0.6209 0.0088  0.0095  0.0230  83  ARG B CG  
1269 C CD  . ARG B 83  ? 0.6384 0.5550 0.6206 0.0213  0.0077  0.0137  83  ARG B CD  
1270 N NE  . ARG B 83  ? 0.9242 0.8316 0.9020 0.0413  -0.0016 0.0055  83  ARG B NE  
1271 C CZ  . ARG B 83  ? 0.9665 0.8838 0.9514 0.0571  -0.0143 -0.0025 83  ARG B CZ  
1272 N NH1 . ARG B 83  ? 0.7012 0.6380 0.6970 0.0539  -0.0189 -0.0043 83  ARG B NH1 
1273 N NH2 . ARG B 83  ? 0.9183 0.8264 0.8979 0.0795  -0.0245 -0.0110 83  ARG B NH2 
1274 N N   . LEU B 84  ? 0.8732 0.6652 0.7448 -0.0363 0.0014  0.0504  84  LEU B N   
1275 C CA  . LEU B 84  ? 0.7877 0.5357 0.6286 -0.0495 0.0031  0.0606  84  LEU B CA  
1276 C C   . LEU B 84  ? 0.8881 0.6136 0.7278 -0.0685 0.0046  0.0558  84  LEU B C   
1277 O O   . LEU B 84  ? 0.9333 0.6212 0.7533 -0.0866 0.0101  0.0635  84  LEU B O   
1278 C CB  . LEU B 84  ? 0.8548 0.6174 0.6935 -0.0648 0.0134  0.0703  84  LEU B CB  
1279 C CG  . LEU B 84  ? 0.9557 0.7231 0.7784 -0.0486 0.0109  0.0766  84  LEU B CG  
1280 C CD1 . LEU B 84  ? 1.0594 0.8218 0.8636 -0.0666 0.0246  0.0885  84  LEU B CD1 
1281 C CD2 . LEU B 84  ? 0.9418 0.6680 0.7318 -0.0241 -0.0020 0.0798  84  LEU B CD2 
1282 N N   . LYS B 85  ? 0.9416 0.6886 0.8008 -0.0659 0.0007  0.0427  85  LYS B N   
1283 C CA  . LYS B 85  ? 0.8703 0.6043 0.7319 -0.0820 -0.0019 0.0323  85  LYS B CA  
1284 C C   . LYS B 85  ? 0.9783 0.7344 0.8592 -0.1110 0.0058  0.0320  85  LYS B C   
1285 O O   . LYS B 85  ? 0.8679 0.6087 0.7533 -0.1313 0.0046  0.0227  85  LYS B O   
1286 C CB  . LYS B 85  ? 0.9126 0.5827 0.7444 -0.0811 -0.0072 0.0315  85  LYS B CB  
1287 C CG  . LYS B 85  ? 0.9547 0.6051 0.7681 -0.0490 -0.0146 0.0321  85  LYS B CG  
1288 C CD  . LYS B 85  ? 1.1201 0.7287 0.9163 -0.0392 -0.0237 0.0188  85  LYS B CD  
1289 C CE  . LYS B 85  ? 1.1412 0.6841 0.9124 -0.0583 -0.0236 0.0226  85  LYS B CE  
1290 N NZ  . LYS B 85  ? 1.3209 0.8065 1.0552 -0.0367 -0.0283 0.0330  85  LYS B NZ  
1291 N N   . GLU B 86  ? 0.8677 0.6624 0.7641 -0.1136 0.0138  0.0389  86  GLU B N   
1292 C CA  . GLU B 86  ? 0.8256 0.6572 0.7492 -0.1361 0.0209  0.0341  86  GLU B CA  
1293 C C   . GLU B 86  ? 0.7838 0.6595 0.7327 -0.1273 0.0116  0.0194  86  GLU B C   
1294 O O   . GLU B 86  ? 0.8389 0.7559 0.8060 -0.1208 0.0139  0.0194  86  GLU B O   
1295 C CB  . GLU B 86  ? 0.8192 0.6718 0.7449 -0.1389 0.0333  0.0458  86  GLU B CB  
1296 C CG  . GLU B 86  ? 0.8160 0.6241 0.7094 -0.1495 0.0444  0.0616  86  GLU B CG  
1297 C CD  . GLU B 86  ? 0.9426 0.7318 0.8402 -0.1828 0.0564  0.0607  86  GLU B CD  
1298 O OE1 . GLU B 86  ? 1.1394 0.8672 1.0052 -0.1900 0.0595  0.0696  86  GLU B OE1 
1299 O OE2 . GLU B 86  ? 1.0496 0.8850 0.9842 -0.2017 0.0631  0.0499  86  GLU B OE2 
1300 N N   . TYR B 87  ? 0.8809 0.7425 0.8254 -0.1248 0.0003  0.0063  87  TYR B N   
1301 C CA  . TYR B 87  ? 0.9033 0.7949 0.8550 -0.1075 -0.0104 -0.0054 87  TYR B CA  
1302 C C   . TYR B 87  ? 0.8122 0.7544 0.7947 -0.1157 -0.0131 -0.0153 87  TYR B C   
1303 O O   . TYR B 87  ? 0.8386 0.8100 0.8249 -0.0965 -0.0168 -0.0158 87  TYR B O   
1304 C CB  . TYR B 87  ? 0.8238 0.6890 0.7594 -0.1027 -0.0228 -0.0203 87  TYR B CB  
1305 C CG  . TYR B 87  ? 0.9453 0.7669 0.8520 -0.0869 -0.0214 -0.0135 87  TYR B CG  
1306 C CD1 . TYR B 87  ? 0.8874 0.7161 0.7874 -0.0651 -0.0148 -0.0021 87  TYR B CD1 
1307 C CD2 . TYR B 87  ? 0.8877 0.6619 0.7776 -0.0937 -0.0264 -0.0205 87  TYR B CD2 
1308 C CE1 . TYR B 87  ? 0.9223 0.7210 0.8038 -0.0491 -0.0140 0.0004  87  TYR B CE1 
1309 C CE2 . TYR B 87  ? 0.8897 0.6268 0.7546 -0.0746 -0.0265 -0.0163 87  TYR B CE2 
1310 C CZ  . TYR B 87  ? 0.9361 0.6900 0.7990 -0.0517 -0.0207 -0.0066 87  TYR B CZ  
1311 O OH  . TYR B 87  ? 1.1172 0.8437 0.9627 -0.0312 -0.0215 -0.0061 87  TYR B OH  
1312 N N   . GLU B 88  ? 0.7416 0.6943 0.7472 -0.1434 -0.0101 -0.0237 88  GLU B N   
1313 C CA  . GLU B 88  ? 0.7379 0.7479 0.7807 -0.1502 -0.0134 -0.0373 88  GLU B CA  
1314 C C   . GLU B 88  ? 0.8002 0.8399 0.8524 -0.1414 -0.0021 -0.0248 88  GLU B C   
1315 O O   . GLU B 88  ? 0.8107 0.8916 0.8793 -0.1257 -0.0093 -0.0321 88  GLU B O   
1316 C CB  . GLU B 88  ? 0.9272 0.9452 1.0001 -0.1866 -0.0085 -0.0512 88  GLU B CB  
1317 C CG  . GLU B 88  ? 1.0151 1.0103 1.0849 -0.2115 0.0161  -0.0335 88  GLU B CG  
1318 C CD  . GLU B 88  ? 1.1938 1.1189 1.2166 -0.2058 0.0215  -0.0135 88  GLU B CD  
1319 O OE1 . GLU B 88  ? 0.9571 0.8725 0.9588 -0.1927 0.0307  0.0058  88  GLU B OE1 
1320 O OE2 . GLU B 88  ? 1.0913 0.9719 1.0991 -0.2126 0.0147  -0.0197 88  GLU B OE2 
1321 N N   . LYS B 89  ? 0.7171 0.7334 0.7553 -0.1479 0.0139  -0.0070 89  LYS B N   
1322 C CA  . LYS B 89  ? 0.7360 0.7760 0.7790 -0.1372 0.0231  0.0023  89  LYS B CA  
1323 C C   . LYS B 89  ? 0.7391 0.7765 0.7690 -0.1074 0.0156  0.0069  89  LYS B C   
1324 O O   . LYS B 89  ? 0.6617 0.7294 0.7051 -0.0937 0.0146  0.0044  89  LYS B O   
1325 C CB  . LYS B 89  ? 0.8085 0.8202 0.8313 -0.1476 0.0388  0.0184  89  LYS B CB  
1326 C CG  . LYS B 89  ? 0.9155 0.9552 0.9562 -0.1682 0.0561  0.0184  89  LYS B CG  
1327 C CD  . LYS B 89  ? 0.7796 0.8483 0.8240 -0.1520 0.0617  0.0216  89  LYS B CD  
1328 C CE  . LYS B 89  ? 0.9632 1.0649 1.0243 -0.1702 0.0813  0.0196  89  LYS B CE  
1329 N NZ  . LYS B 89  ? 0.8499 0.9598 0.8968 -0.1554 0.0893  0.0259  89  LYS B NZ  
1330 N N   . ALA B 90  ? 0.5723 0.5720 0.5766 -0.0970 0.0124  0.0134  90  ALA B N   
1331 C CA  . ALA B 90  ? 0.6082 0.6045 0.6026 -0.0729 0.0105  0.0179  90  ALA B CA  
1332 C C   . ALA B 90  ? 0.6424 0.6604 0.6409 -0.0588 0.0010  0.0094  90  ALA B C   
1333 O O   . ALA B 90  ? 0.5836 0.6106 0.5820 -0.0421 0.0033  0.0139  90  ALA B O   
1334 C CB  . ALA B 90  ? 0.6087 0.5683 0.5802 -0.0653 0.0097  0.0221  90  ALA B CB  
1335 N N   . LEU B 91  ? 0.6234 0.6470 0.6230 -0.0641 -0.0109 -0.0038 91  LEU B N   
1336 C CA  . LEU B 91  ? 0.6632 0.7089 0.6613 -0.0463 -0.0245 -0.0142 91  LEU B CA  
1337 C C   . LEU B 91  ? 0.8149 0.9031 0.8401 -0.0426 -0.0262 -0.0191 91  LEU B C   
1338 O O   . LEU B 91  ? 0.7238 0.8211 0.7400 -0.0178 -0.0322 -0.0180 91  LEU B O   
1339 C CB  . LEU B 91  ? 0.7095 0.7565 0.7074 -0.0544 -0.0399 -0.0330 91  LEU B CB  
1340 C CG  . LEU B 91  ? 0.8762 0.9204 0.8475 -0.0306 -0.0564 -0.0432 91  LEU B CG  
1341 C CD1 . LEU B 91  ? 0.7840 0.7954 0.7162 -0.0071 -0.0467 -0.0261 91  LEU B CD1 
1342 C CD2 . LEU B 91  ? 0.8448 0.8760 0.8151 -0.0455 -0.0677 -0.0616 91  LEU B CD2 
1343 N N   . LYS B 92  ? 0.6242 0.7361 0.6796 -0.0653 -0.0191 -0.0237 92  LYS B N   
1344 C CA  . LYS B 92  ? 0.6370 0.7942 0.7215 -0.0607 -0.0185 -0.0306 92  LYS B CA  
1345 C C   . LYS B 92  ? 0.7638 0.9102 0.8365 -0.0408 -0.0099 -0.0164 92  LYS B C   
1346 O O   . LYS B 92  ? 0.6781 0.8453 0.7568 -0.0191 -0.0164 -0.0206 92  LYS B O   
1347 C CB  . LYS B 92  ? 0.7814 0.9628 0.8969 -0.0912 -0.0058 -0.0361 92  LYS B CB  
1348 C CG  . LYS B 92  ? 0.7674 1.0084 0.9224 -0.0893 -0.0054 -0.0505 92  LYS B CG  
1349 C CD  . LYS B 92  ? 0.9165 1.2020 1.1003 -0.0850 -0.0258 -0.0756 92  LYS B CD  
1350 C CE  . LYS B 92  ? 0.9595 1.3122 1.1884 -0.0788 -0.0263 -0.0928 92  LYS B CE  
1351 N NZ  . LYS B 92  ? 0.7432 1.1537 1.0139 -0.0791 -0.0469 -0.1237 92  LYS B NZ  
1352 N N   . TYR B 93  ? 0.6273 0.7405 0.6844 -0.0468 0.0033  -0.0017 93  TYR B N   
1353 C CA  . TYR B 93  ? 0.6866 0.7874 0.7367 -0.0313 0.0111  0.0080  93  TYR B CA  
1354 C C   . TYR B 93  ? 0.5991 0.6788 0.6278 -0.0070 0.0063  0.0138  93  TYR B C   
1355 O O   . TYR B 93  ? 0.6854 0.7649 0.7137 0.0106  0.0077  0.0162  93  TYR B O   
1356 C CB  . TYR B 93  ? 0.6065 0.6793 0.6462 -0.0415 0.0223  0.0182  93  TYR B CB  
1357 C CG  . TYR B 93  ? 0.7403 0.8272 0.7902 -0.0572 0.0309  0.0172  93  TYR B CG  
1358 C CD1 . TYR B 93  ? 0.6243 0.7364 0.6891 -0.0518 0.0360  0.0123  93  TYR B CD1 
1359 C CD2 . TYR B 93  ? 0.6383 0.7087 0.6773 -0.0750 0.0349  0.0215  93  TYR B CD2 
1360 C CE1 . TYR B 93  ? 0.6173 0.7421 0.6846 -0.0645 0.0462  0.0115  93  TYR B CE1 
1361 C CE2 . TYR B 93  ? 0.6335 0.7106 0.6714 -0.0876 0.0453  0.0237  93  TYR B CE2 
1362 C CZ  . TYR B 93  ? 0.6385 0.7448 0.6899 -0.0825 0.0516  0.0186  93  TYR B CZ  
1363 O OH  . TYR B 93  ? 0.7668 0.8792 0.8105 -0.0936 0.0642  0.0210  93  TYR B OH  
1364 N N   . VAL B 94  ? 0.7379 0.7939 0.7441 -0.0049 0.0030  0.0171  94  VAL B N   
1365 C CA  . VAL B 94  ? 0.7212 0.7506 0.6991 0.0171  0.0047  0.0262  94  VAL B CA  
1366 C C   . VAL B 94  ? 0.7090 0.7534 0.6760 0.0394  -0.0108 0.0197  94  VAL B C   
1367 O O   . VAL B 94  ? 0.8105 0.8340 0.7537 0.0625  -0.0080 0.0295  94  VAL B O   
1368 C CB  . VAL B 94  ? 0.7889 0.7902 0.7443 0.0141  0.0090  0.0308  94  VAL B CB  
1369 C CG1 . VAL B 94  ? 0.6995 0.7069 0.6404 0.0176  -0.0069 0.0196  94  VAL B CG1 
1370 C CG2 . VAL B 94  ? 0.7424 0.7126 0.6742 0.0295  0.0235  0.0448  94  VAL B CG2 
1371 N N   . ARG B 95  ? 0.7529 0.8331 0.7375 0.0338  -0.0272 0.0023  95  ARG B N   
1372 C CA  . ARG B 95  ? 0.7455 0.8515 0.7273 0.0581  -0.0464 -0.0089 95  ARG B CA  
1373 C C   . ARG B 95  ? 0.7577 0.8784 0.7547 0.0729  -0.0442 -0.0073 95  ARG B C   
1374 O O   . ARG B 95  ? 0.7167 0.8300 0.6913 0.1048  -0.0536 -0.0047 95  ARG B O   
1375 C CB  . ARG B 95  ? 0.7409 0.8920 0.7526 0.0444  -0.0643 -0.0335 95  ARG B CB  
1376 C CG  . ARG B 95  ? 0.9624 1.1072 0.9466 0.0564  -0.0830 -0.0441 95  ARG B CG  
1377 C CD  . ARG B 95  ? 0.9731 1.0940 0.9532 0.0303  -0.0764 -0.0450 95  ARG B CD  
1378 N NE  . ARG B 95  ? 0.9813 1.0916 0.9312 0.0425  -0.0933 -0.0570 95  ARG B NE  
1379 C CZ  . ARG B 95  ? 0.8839 1.0152 0.8534 0.0271  -0.1099 -0.0820 95  ARG B CZ  
1380 N NH1 . ARG B 95  ? 0.7966 0.9626 0.8184 -0.0030 -0.1099 -0.0967 95  ARG B NH1 
1381 N NH2 . ARG B 95  ? 1.0891 1.2048 1.0246 0.0410  -0.1251 -0.0935 95  ARG B NH2 
1382 N N   . GLY B 96  ? 0.7366 0.8743 0.7665 0.0531  -0.0320 -0.0088 96  GLY B N   
1383 C CA  . GLY B 96  ? 0.6935 0.8452 0.7383 0.0681  -0.0295 -0.0104 96  GLY B CA  
1384 C C   . GLY B 96  ? 0.8312 0.9312 0.8445 0.0874  -0.0192 0.0080  96  GLY B C   
1385 O O   . GLY B 96  ? 0.8880 0.9822 0.8925 0.1151  -0.0247 0.0086  96  GLY B O   
1386 N N   . LEU B 97  ? 0.7084 0.7692 0.7059 0.0730  -0.0036 0.0222  97  LEU B N   
1387 C CA  . LEU B 97  ? 0.6578 0.6685 0.6304 0.0850  0.0104  0.0387  97  LEU B CA  
1388 C C   . LEU B 97  ? 0.8339 0.8177 0.7645 0.1156  0.0032  0.0479  97  LEU B C   
1389 O O   . LEU B 97  ? 0.9711 0.9203 0.8817 0.1363  0.0090  0.0584  97  LEU B O   
1390 C CB  . LEU B 97  ? 0.7804 0.7658 0.7498 0.0636  0.0266  0.0478  97  LEU B CB  
1391 C CG  . LEU B 97  ? 0.9286 0.8832 0.9047 0.0570  0.0455  0.0554  97  LEU B CG  
1392 C CD1 . LEU B 97  ? 0.9123 0.8865 0.9165 0.0547  0.0438  0.0445  97  LEU B CD1 
1393 C CD2 . LEU B 97  ? 0.8835 0.8323 0.8677 0.0358  0.0561  0.0571  97  LEU B CD2 
1394 N N   . LEU B 98  ? 0.7798 0.7762 0.6930 0.1206  -0.0105 0.0433  98  LEU B N   
1395 C CA  . LEU B 98  ? 0.9484 0.9178 0.8110 0.1524  -0.0188 0.0518  98  LEU B CA  
1396 C C   . LEU B 98  ? 0.9350 0.9287 0.7946 0.1849  -0.0427 0.0411  98  LEU B C   
1397 O O   . LEU B 98  ? 1.0806 1.0411 0.8905 0.2194  -0.0487 0.0522  98  LEU B O   
1398 C CB  . LEU B 98  ? 0.7802 0.7550 0.6228 0.1481  -0.0270 0.0467  98  LEU B CB  
1399 C CG  . LEU B 98  ? 0.9883 0.9235 0.8116 0.1329  -0.0023 0.0624  98  LEU B CG  
1400 C CD1 . LEU B 98  ? 0.8056 0.7521 0.6196 0.1245  -0.0110 0.0519  98  LEU B CD1 
1401 C CD2 . LEU B 98  ? 1.0046 0.8844 0.7763 0.1561  0.0152  0.0858  98  LEU B CD2 
1402 N N   . GLN B 99  ? 0.9263 0.9779 0.8358 0.1767  -0.0560 0.0195  99  GLN B N   
1403 C CA  . GLN B 99  ? 0.8239 0.9051 0.7402 0.2096  -0.0773 0.0065  99  GLN B CA  
1404 C C   . GLN B 99  ? 0.9911 1.0204 0.8784 0.2366  -0.0673 0.0243  99  GLN B C   
1405 O O   . GLN B 99  ? 0.9741 0.9822 0.8216 0.2781  -0.0819 0.0292  99  GLN B O   
1406 C CB  . GLN B 99  ? 0.8528 1.0046 0.8352 0.1904  -0.0832 -0.0184 99  GLN B CB  
1407 C CG  . GLN B 99  ? 1.0312 1.2437 1.0358 0.2163  -0.1127 -0.0441 99  GLN B CG  
1408 C CD  . GLN B 99  ? 1.1485 1.4094 1.1789 0.1952  -0.1274 -0.0654 99  GLN B CD  
1409 O OE1 . GLN B 99  ? 1.1001 1.3766 1.1627 0.1535  -0.1132 -0.0694 99  GLN B OE1 
1410 N NE2 . GLN B 99  ? 1.0105 1.2919 1.0243 0.2251  -0.1570 -0.0801 99  GLN B NE2 
1411 N N   . THR B 100 ? 0.9894 0.9938 0.8937 0.2145  -0.0430 0.0335  100 THR B N   
1412 C CA  . THR B 100 ? 1.1305 1.0857 1.0187 0.2330  -0.0315 0.0459  100 THR B CA  
1413 C C   . THR B 100 ? 1.1813 1.0564 1.0215 0.2321  -0.0078 0.0741  100 THR B C   
1414 O O   . THR B 100 ? 1.1391 0.9577 0.9444 0.2579  -0.0015 0.0889  100 THR B O   
1415 C CB  . THR B 100 ? 1.2075 1.1866 1.1459 0.2099  -0.0206 0.0337  100 THR B CB  
1416 O OG1 . THR B 100 ? 1.2601 1.1769 1.1852 0.2063  0.0010  0.0484  100 THR B OG1 
1417 C CG2 . THR B 100 ? 0.9439 0.9671 0.9196 0.1688  -0.0149 0.0238  100 THR B CG2 
1418 N N   . GLU B 101 ? 1.0812 0.9487 0.9188 0.2036  0.0070  0.0817  101 GLU B N   
1419 C CA  . GLU B 101 ? 1.1445 0.9461 0.9421 0.1997  0.0329  0.1064  101 GLU B CA  
1420 C C   . GLU B 101 ? 1.1612 0.9618 0.9196 0.2057  0.0288  0.1126  101 GLU B C   
1421 O O   . GLU B 101 ? 1.1110 0.9223 0.8822 0.1789  0.0396  0.1114  101 GLU B O   
1422 C CB  . GLU B 101 ? 1.2415 1.0356 1.0757 0.1612  0.0577  0.1070  101 GLU B CB  
1423 C CG  . GLU B 101 ? 1.2632 1.0103 1.1035 0.1595  0.0765  0.1142  101 GLU B CG  
1424 C CD  . GLU B 101 ? 1.3238 1.0894 1.2160 0.1238  0.0886  0.1021  101 GLU B CD  
1425 O OE1 . GLU B 101 ? 1.3718 1.1242 1.2857 0.1216  0.0928  0.0949  101 GLU B OE1 
1426 O OE2 . GLU B 101 ? 1.2604 1.0537 1.1699 0.1007  0.0918  0.0979  101 GLU B OE2 
1427 N N   . PRO B 102 ? 1.2437 1.0300 0.9508 0.2440  0.0120  0.1179  102 PRO B N   
1428 C CA  . PRO B 102 ? 1.2164 1.0021 0.8805 0.2534  0.0057  0.1207  102 PRO B CA  
1429 C C   . PRO B 102 ? 1.2486 0.9754 0.8702 0.2451  0.0401  0.1460  102 PRO B C   
1430 O O   . PRO B 102 ? 1.2085 0.9424 0.8089 0.2413  0.0411  0.1446  102 PRO B O   
1431 C CB  . PRO B 102 ? 1.3871 1.1694 1.0031 0.3029  -0.0230 0.1193  102 PRO B CB  
1432 C CG  . PRO B 102 ? 1.2405 0.9813 0.8486 0.3221  -0.0157 0.1321  102 PRO B CG  
1433 C CD  . PRO B 102 ? 1.1685 0.9364 0.8501 0.2847  -0.0037 0.1205  102 PRO B CD  
1434 N N   . GLN B 103 ? 1.3684 1.0377 0.9787 0.2415  0.0694  0.1672  103 GLN B N   
1435 C CA  . GLN B 103 ? 1.4006 1.0159 0.9788 0.2291  0.1084  0.1908  103 GLN B CA  
1436 C C   . GLN B 103 ? 1.2640 0.9028 0.9043 0.1836  0.1300  0.1824  103 GLN B C   
1437 O O   . GLN B 103 ? 1.1709 0.7768 0.8003 0.1682  0.1644  0.1972  103 GLN B O   
1438 C CB  . GLN B 103 ? 1.3995 0.9356 0.9371 0.2445  0.1327  0.2176  103 GLN B CB  
1439 C CG  . GLN B 103 ? 1.6063 1.1204 1.0977 0.2923  0.1057  0.2220  103 GLN B CG  
1440 C CD  . GLN B 103 ? 1.6735 1.2235 1.2235 0.2917  0.0832  0.2007  103 GLN B CD  
1441 O OE1 . GLN B 103 ? 1.5452 1.1437 1.1668 0.2563  0.0836  0.1812  103 GLN B OE1 
1442 N NE2 . GLN B 103 ? 1.4965 1.0231 1.0131 0.3340  0.0632  0.2040  103 GLN B NE2 
1443 N N   . ASN B 104 ? 1.0645 0.7598 0.7684 0.1630  0.1117  0.1588  104 ASN B N   
1444 C CA  . ASN B 104 ? 0.9425 0.6597 0.7018 0.1255  0.1276  0.1496  104 ASN B CA  
1445 C C   . ASN B 104 ? 0.9960 0.7299 0.7467 0.1164  0.1331  0.1472  104 ASN B C   
1446 O O   . ASN B 104 ? 0.9337 0.7018 0.6792 0.1231  0.1088  0.1344  104 ASN B O   
1447 C CB  . ASN B 104 ? 0.9323 0.7001 0.7482 0.1115  0.1058  0.1272  104 ASN B CB  
1448 C CG  . ASN B 104 ? 0.9472 0.7386 0.8145 0.0783  0.1166  0.1163  104 ASN B CG  
1449 O OD1 . ASN B 104 ? 0.9493 0.7349 0.8176 0.0653  0.1343  0.1201  104 ASN B OD1 
1450 N ND2 . ASN B 104 ? 0.8832 0.7026 0.7921 0.0671  0.1056  0.1014  104 ASN B ND2 
1451 N N   . ASN B 105 ? 0.8959 0.6064 0.6484 0.1006  0.1661  0.1574  105 ASN B N   
1452 C CA  . ASN B 105 ? 0.9494 0.6706 0.6879 0.0970  0.1758  0.1561  105 ASN B CA  
1453 C C   . ASN B 105 ? 0.9550 0.7248 0.7494 0.0735  0.1659  0.1347  105 ASN B C   
1454 O O   . ASN B 105 ? 0.8422 0.6305 0.6259 0.0763  0.1578  0.1264  105 ASN B O   
1455 C CB  . ASN B 105 ? 1.1330 0.8128 0.8510 0.0910  0.2192  0.1753  105 ASN B CB  
1456 C CG  . ASN B 105 ? 1.1036 0.7272 0.7425 0.1202  0.2310  0.2005  105 ASN B CG  
1457 O OD1 . ASN B 105 ? 1.2237 0.8492 0.8123 0.1491  0.2067  0.2003  105 ASN B OD1 
1458 N ND2 . ASN B 105 ? 1.1374 0.7086 0.7629 0.1133  0.2688  0.2217  105 ASN B ND2 
1459 N N   . GLN B 106 ? 0.8466 0.6334 0.6958 0.0529  0.1653  0.1251  106 GLN B N   
1460 C CA  . GLN B 106 ? 0.8473 0.6761 0.7410 0.0360  0.1516  0.1061  106 GLN B CA  
1461 C C   . GLN B 106 ? 0.8657 0.7199 0.7511 0.0436  0.1193  0.0955  106 GLN B C   
1462 O O   . GLN B 106 ? 0.7635 0.6368 0.6539 0.0389  0.1092  0.0853  106 GLN B O   
1463 C CB  . GLN B 106 ? 0.9633 0.8045 0.9091 0.0172  0.1535  0.0967  106 GLN B CB  
1464 C CG  . GLN B 106 ? 1.0490 0.8568 1.0017 0.0127  0.1757  0.1059  106 GLN B CG  
1465 C CD  . GLN B 106 ? 0.9400 0.7210 0.8845 0.0067  0.2106  0.1177  106 GLN B CD  
1466 O OE1 . GLN B 106 ? 1.2372 1.0409 1.2092 -0.0061 0.2220  0.1090  106 GLN B OE1 
1467 N NE2 . GLN B 106 ? 1.1467 0.8780 1.0515 0.0172  0.2294  0.1381  106 GLN B NE2 
1468 N N   . ALA B 107 ? 0.7912 0.6458 0.6669 0.0549  0.1034  0.0964  107 ALA B N   
1469 C CA  . ALA B 107 ? 0.7356 0.6201 0.6127 0.0586  0.0752  0.0837  107 ALA B CA  
1470 C C   . ALA B 107 ? 0.8469 0.7288 0.6846 0.0734  0.0652  0.0820  107 ALA B C   
1471 O O   . ALA B 107 ? 0.7076 0.6122 0.5537 0.0667  0.0480  0.0680  107 ALA B O   
1472 C CB  . ALA B 107 ? 0.7354 0.6275 0.6164 0.0698  0.0623  0.0822  107 ALA B CB  
1473 N N   . LYS B 108 ? 0.7943 0.6450 0.5853 0.0943  0.0759  0.0957  108 LYS B N   
1474 C CA  . LYS B 108 ? 0.7668 0.6139 0.5140 0.1114  0.0663  0.0922  108 LYS B CA  
1475 C C   . LYS B 108 ? 0.8266 0.6791 0.5826 0.0975  0.0747  0.0847  108 LYS B C   
1476 O O   . LYS B 108 ? 0.9430 0.8101 0.6925 0.0988  0.0558  0.0693  108 LYS B O   
1477 C CB  . LYS B 108 ? 0.8634 0.6693 0.5495 0.1383  0.0811  0.1118  108 LYS B CB  
1478 C CG  . LYS B 108 ? 0.9801 0.7879 0.6255 0.1694  0.0535  0.1082  108 LYS B CG  
1479 C CD  . LYS B 108 ? 1.0243 0.7835 0.6170 0.1959  0.0685  0.1327  108 LYS B CD  
1480 C CE  . LYS B 108 ? 1.2802 1.0472 0.8468 0.2291  0.0361  0.1271  108 LYS B CE  
1481 N NZ  . LYS B 108 ? 1.3873 1.0968 0.8996 0.2575  0.0507  0.1539  108 LYS B NZ  
1482 N N   . GLU B 109 ? 0.8020 0.6441 0.5770 0.0841  0.1022  0.0928  109 GLU B N   
1483 C CA  . GLU B 109 ? 0.7768 0.6269 0.5639 0.0749  0.1108  0.0843  109 GLU B CA  
1484 C C   . GLU B 109 ? 0.8542 0.7301 0.6780 0.0595  0.0886  0.0671  109 GLU B C   
1485 O O   . GLU B 109 ? 0.7769 0.6557 0.5935 0.0607  0.0801  0.0555  109 GLU B O   
1486 C CB  . GLU B 109 ? 0.9800 0.8232 0.7920 0.0629  0.1437  0.0929  109 GLU B CB  
1487 C CG  . GLU B 109 ? 1.0930 0.9485 0.9208 0.0577  0.1570  0.0836  109 GLU B CG  
1488 C CD  . GLU B 109 ? 1.0482 0.8987 0.8330 0.0750  0.1509  0.0768  109 GLU B CD  
1489 O OE1 . GLU B 109 ? 1.2419 1.1068 1.0439 0.0724  0.1441  0.0618  109 GLU B OE1 
1490 O OE2 . GLU B 109 ? 1.1138 0.9435 0.8446 0.0937  0.1530  0.0854  109 GLU B OE2 
1491 N N   . LEU B 110 ? 0.7448 0.6349 0.6043 0.0459  0.0808  0.0656  110 LEU B N   
1492 C CA  . LEU B 110 ? 0.7591 0.6671 0.6453 0.0315  0.0634  0.0531  110 LEU B CA  
1493 C C   . LEU B 110 ? 0.7314 0.6456 0.6012 0.0345  0.0402  0.0424  110 LEU B C   
1494 O O   . LEU B 110 ? 0.7331 0.6472 0.6063 0.0266  0.0298  0.0317  110 LEU B O   
1495 C CB  . LEU B 110 ? 0.6636 0.5851 0.5845 0.0184  0.0625  0.0541  110 LEU B CB  
1496 C CG  . LEU B 110 ? 0.7865 0.7222 0.7271 0.0041  0.0477  0.0452  110 LEU B CG  
1497 C CD1 . LEU B 110 ? 0.7665 0.6949 0.7099 0.0008  0.0484  0.0403  110 LEU B CD1 
1498 C CD2 . LEU B 110 ? 0.8328 0.7811 0.7997 -0.0042 0.0501  0.0466  110 LEU B CD2 
1499 N N   . GLU B 111 ? 0.7570 0.6754 0.6091 0.0471  0.0310  0.0434  111 GLU B N   
1500 C CA  . GLU B 111 ? 0.7680 0.6997 0.6107 0.0501  0.0071  0.0280  111 GLU B CA  
1501 C C   . GLU B 111 ? 0.8506 0.7668 0.6612 0.0595  0.0033  0.0193  111 GLU B C   
1502 O O   . GLU B 111 ? 0.8652 0.7861 0.6818 0.0502  -0.0130 0.0025  111 GLU B O   
1503 C CB  . GLU B 111 ? 0.8311 0.7741 0.6592 0.0687  -0.0048 0.0281  111 GLU B CB  
1504 C CG  . GLU B 111 ? 0.9755 0.9472 0.8131 0.0668  -0.0325 0.0059  111 GLU B CG  
1505 C CD  . GLU B 111 ? 0.9293 0.9168 0.7493 0.0926  -0.0497 0.0015  111 GLU B CD  
1506 O OE1 . GLU B 111 ? 1.0251 0.9873 0.8047 0.1178  -0.0406 0.0177  111 GLU B OE1 
1507 O OE2 . GLU B 111 ? 1.0643 1.0890 0.9105 0.0884  -0.0717 -0.0187 111 GLU B OE2 
1508 N N   . ARG B 112 ? 0.8405 0.7360 0.6155 0.0775  0.0199  0.0299  112 ARG B N   
1509 C CA  . ARG B 112 ? 0.8429 0.7238 0.5846 0.0890  0.0204  0.0212  112 ARG B CA  
1510 C C   . ARG B 112 ? 0.8112 0.6895 0.5783 0.0726  0.0206  0.0112  112 ARG B C   
1511 O O   . ARG B 112 ? 0.8834 0.7560 0.6402 0.0729  0.0047  -0.0064 112 ARG B O   
1512 C CB  . ARG B 112 ? 0.9242 0.7842 0.6285 0.1071  0.0479  0.0378  112 ARG B CB  
1513 C CG  . ARG B 112 ? 1.0598 0.9055 0.7101 0.1295  0.0469  0.0296  112 ARG B CG  
1514 C CD  . ARG B 112 ? 0.9450 0.7697 0.5606 0.1433  0.0825  0.0486  112 ARG B CD  
1515 N NE  . ARG B 112 ? 1.1154 0.9453 0.7711 0.1264  0.1078  0.0517  112 ARG B NE  
1516 C CZ  . ARG B 112 ? 1.2426 1.0765 0.9033 0.1271  0.1120  0.0378  112 ARG B CZ  
1517 N NH1 . ARG B 112 ? 1.2332 1.0604 0.8559 0.1434  0.0964  0.0211  112 ARG B NH1 
1518 N NH2 . ARG B 112 ? 1.0040 0.8499 0.7094 0.1134  0.1303  0.0381  112 ARG B NH2 
1519 N N   . LEU B 113 ? 0.7825 0.6631 0.5824 0.0596  0.0363  0.0205  113 LEU B N   
1520 C CA  . LEU B 113 ? 0.8381 0.7137 0.6579 0.0495  0.0346  0.0123  113 LEU B CA  
1521 C C   . LEU B 113 ? 0.8644 0.7394 0.6982 0.0333  0.0124  0.0014  113 LEU B C   
1522 O O   . LEU B 113 ? 0.7646 0.6220 0.5933 0.0309  0.0039  -0.0101 113 LEU B O   
1523 C CB  . LEU B 113 ? 0.8355 0.7192 0.6886 0.0417  0.0516  0.0220  113 LEU B CB  
1524 C CG  . LEU B 113 ? 0.9268 0.8119 0.7783 0.0516  0.0784  0.0288  113 LEU B CG  
1525 C CD1 . LEU B 113 ? 0.7678 0.6681 0.6630 0.0405  0.0904  0.0324  113 LEU B CD1 
1526 C CD2 . LEU B 113 ? 0.7882 0.6650 0.6191 0.0660  0.0833  0.0180  113 LEU B CD2 
1527 N N   . ILE B 114 ? 0.6795 0.5713 0.5312 0.0216  0.0050  0.0044  114 ILE B N   
1528 C CA  . ILE B 114 ? 0.8529 0.7470 0.7208 0.0024  -0.0107 -0.0058 114 ILE B CA  
1529 C C   . ILE B 114 ? 0.8397 0.7265 0.6889 0.0053  -0.0280 -0.0250 114 ILE B C   
1530 O O   . ILE B 114 ? 0.8854 0.7515 0.7360 -0.0065 -0.0357 -0.0360 114 ILE B O   
1531 C CB  . ILE B 114 ? 0.7960 0.7180 0.6889 -0.0084 -0.0129 -0.0016 114 ILE B CB  
1532 C CG1 . ILE B 114 ? 0.7148 0.6398 0.6273 -0.0148 0.0013  0.0126  114 ILE B CG1 
1533 C CG2 . ILE B 114 ? 0.7957 0.7258 0.7061 -0.0293 -0.0263 -0.0151 114 ILE B CG2 
1534 C CD1 . ILE B 114 ? 0.6589 0.6097 0.5887 -0.0154 0.0036  0.0179  114 ILE B CD1 
1535 N N   . ASP B 115 ? 0.8369 0.7370 0.6656 0.0227  -0.0354 -0.0303 115 ASP B N   
1536 C CA  . ASP B 115 ? 0.8364 0.7334 0.6438 0.0300  -0.0552 -0.0528 115 ASP B CA  
1537 C C   . ASP B 115 ? 0.8380 0.7018 0.6255 0.0335  -0.0539 -0.0621 115 ASP B C   
1538 O O   . ASP B 115 ? 0.8999 0.7505 0.6899 0.0226  -0.0696 -0.0826 115 ASP B O   
1539 C CB  . ASP B 115 ? 0.8621 0.7693 0.6326 0.0592  -0.0597 -0.0525 115 ASP B CB  
1540 C CG  . ASP B 115 ? 1.1704 1.1100 0.9569 0.0616  -0.0697 -0.0507 115 ASP B CG  
1541 O OD1 . ASP B 115 ? 1.0447 1.0068 0.8749 0.0385  -0.0763 -0.0569 115 ASP B OD1 
1542 O OD2 . ASP B 115 ? 1.1543 1.0952 0.9067 0.0887  -0.0697 -0.0429 115 ASP B OD2 
1543 N N   . LYS B 116 ? 0.8999 0.7502 0.6700 0.0488  -0.0345 -0.0491 116 LYS B N   
1544 C CA  . LYS B 116 ? 0.8355 0.6588 0.5847 0.0593  -0.0320 -0.0595 116 LYS B CA  
1545 C C   . LYS B 116 ? 0.8310 0.6306 0.6026 0.0412  -0.0357 -0.0632 116 LYS B C   
1546 O O   . LYS B 116 ? 0.9531 0.7248 0.7112 0.0424  -0.0469 -0.0812 116 LYS B O   
1547 C CB  . LYS B 116 ? 0.9358 0.7599 0.6698 0.0786  -0.0067 -0.0456 116 LYS B CB  
1548 C CG  . LYS B 116 ? 1.1327 0.9386 0.8344 0.0990  -0.0033 -0.0598 116 LYS B CG  
1549 C CD  . LYS B 116 ? 1.1987 1.0126 0.8662 0.1219  0.0186  -0.0501 116 LYS B CD  
1550 C CE  . LYS B 116 ? 1.2724 1.0906 0.9550 0.1271  0.0469  -0.0414 116 LYS B CE  
1551 N NZ  . LYS B 116 ? 1.2473 1.0707 0.8967 0.1453  0.0746  -0.0303 116 LYS B NZ  
1552 N N   . ALA B 117 ? 0.8707 0.6761 0.6715 0.0266  -0.0268 -0.0466 117 ALA B N   
1553 C CA  . ALA B 117 ? 0.8692 0.6461 0.6819 0.0117  -0.0308 -0.0469 117 ALA B CA  
1554 C C   . ALA B 117 ? 0.8668 0.6295 0.6854 -0.0112 -0.0467 -0.0605 117 ALA B C   
1555 O O   . ALA B 117 ? 0.9269 0.6488 0.7381 -0.0187 -0.0530 -0.0692 117 ALA B O   
1556 C CB  . ALA B 117 ? 0.8775 0.6664 0.7144 0.0027  -0.0199 -0.0274 117 ALA B CB  
1557 N N   . MET B 118 ? 0.8475 0.6428 0.6813 -0.0224 -0.0528 -0.0641 118 MET B N   
1558 C CA  . MET B 118 ? 0.8406 0.6336 0.6914 -0.0478 -0.0663 -0.0808 118 MET B CA  
1559 C C   . MET B 118 ? 0.8785 0.6459 0.7089 -0.0424 -0.0826 -0.1075 118 MET B C   
1560 O O   . MET B 118 ? 1.0451 0.7764 0.8806 -0.0623 -0.0883 -0.1194 118 MET B O   
1561 C CB  . MET B 118 ? 0.9005 0.7446 0.7750 -0.0539 -0.0718 -0.0838 118 MET B CB  
1562 C CG  . MET B 118 ? 1.0435 0.9071 0.9484 -0.0732 -0.0593 -0.0666 118 MET B CG  
1563 S SD  . MET B 118 ? 1.0157 0.9412 0.9566 -0.0820 -0.0681 -0.0772 118 MET B SD  
1564 C CE  . MET B 118 ? 1.0684 1.0112 0.9783 -0.0451 -0.0844 -0.0885 118 MET B CE  
1565 N N   . LYS B 119 ? 0.8740 0.6554 0.6773 -0.0148 -0.0890 -0.1172 119 LYS B N   
1566 C CA  . LYS B 119 ? 0.8992 0.6598 0.6772 -0.0044 -0.1062 -0.1460 119 LYS B CA  
1567 C C   . LYS B 119 ? 1.1078 0.8134 0.8699 -0.0021 -0.1024 -0.1499 119 LYS B C   
1568 O O   . LYS B 119 ? 1.1003 0.7732 0.8585 -0.0120 -0.1170 -0.1744 119 LYS B O   
1569 C CB  . LYS B 119 ? 0.8670 0.6489 0.6070 0.0306  -0.1083 -0.1497 119 LYS B CB  
1570 C CG  . LYS B 119 ? 1.0550 0.8219 0.7634 0.0453  -0.1287 -0.1826 119 LYS B CG  
1571 C CD  . LYS B 119 ? 1.1618 0.9574 0.8312 0.0768  -0.1372 -0.1893 119 LYS B CD  
1572 C CE  . LYS B 119 ? 1.2944 1.0647 0.9134 0.1038  -0.1454 -0.2135 119 LYS B CE  
1573 N NZ  . LYS B 119 ? 1.2698 1.0620 0.8386 0.1377  -0.1552 -0.2214 119 LYS B NZ  
1574 N N   . LYS B 120 ? 0.9617 0.6561 0.7166 0.0117  -0.0843 -0.1281 120 LYS B N   
1575 C CA  . LYS B 120 ? 0.9549 0.5988 0.6949 0.0197  -0.0827 -0.1321 120 LYS B CA  
1576 C C   . LYS B 120 ? 1.0850 0.6881 0.8418 -0.0097 -0.0849 -0.1273 120 LYS B C   
1577 O O   . LYS B 120 ? 1.1116 0.6599 0.8538 -0.0113 -0.0925 -0.1409 120 LYS B O   
1578 C CB  . LYS B 120 ? 0.9844 0.6376 0.7190 0.0441  -0.0644 -0.1137 120 LYS B CB  
1579 C CG  . LYS B 120 ? 1.0420 0.7185 0.7514 0.0743  -0.0569 -0.1207 120 LYS B CG  
1580 C CD  . LYS B 120 ? 1.1180 0.8129 0.8342 0.0927  -0.0350 -0.1044 120 LYS B CD  
1581 C CE  . LYS B 120 ? 0.9914 0.7126 0.6828 0.1169  -0.0207 -0.1073 120 LYS B CE  
1582 N NZ  . LYS B 120 ? 1.1497 0.9022 0.8600 0.1242  0.0052  -0.0882 120 LYS B NZ  
1583 N N   . ASP B 121 ? 0.9824 0.6073 0.7661 -0.0321 -0.0766 -0.1075 121 ASP B N   
1584 C CA  . ASP B 121 ? 0.9789 0.5652 0.7733 -0.0609 -0.0732 -0.0984 121 ASP B CA  
1585 C C   . ASP B 121 ? 1.2134 0.7799 1.0199 -0.0907 -0.0845 -0.1218 121 ASP B C   
1586 O O   . ASP B 121 ? 1.2946 0.8004 1.0940 -0.1084 -0.0837 -0.1236 121 ASP B O   
1587 C CB  . ASP B 121 ? 0.8821 0.5038 0.7000 -0.0755 -0.0599 -0.0739 121 ASP B CB  
1588 C CG  . ASP B 121 ? 1.2060 0.8034 1.0111 -0.0641 -0.0493 -0.0504 121 ASP B CG  
1589 O OD1 . ASP B 121 ? 1.2355 0.7981 1.0171 -0.0402 -0.0525 -0.0529 121 ASP B OD1 
1590 O OD2 . ASP B 121 ? 1.2058 0.8216 1.0240 -0.0762 -0.0392 -0.0318 121 ASP B OD2 
1591 N N   . GLY B 122 ? 1.1894 0.8049 1.0146 -0.0965 -0.0955 -0.1410 122 GLY B N   
1592 C CA  . GLY B 122 ? 1.1560 0.7607 0.9989 -0.1230 -0.1101 -0.1714 122 GLY B CA  
1593 C C   . GLY B 122 ? 1.2219 0.7660 1.0352 -0.1125 -0.1222 -0.1946 122 GLY B C   
1594 O O   . GLY B 122 ? 1.3922 0.8857 1.2131 -0.1402 -0.1250 -0.2081 122 GLY B O   
1595 N N   . LEU B 123 ? 1.2061 0.7525 0.9849 -0.0726 -0.1274 -0.1998 123 LEU B N   
1596 C CA  . LEU B 123 ? 1.2821 0.7726 1.0286 -0.0554 -0.1379 -0.2227 123 LEU B CA  
1597 C C   . LEU B 123 ? 1.4632 0.8769 1.1992 -0.0644 -0.1288 -0.2092 123 LEU B C   
1598 O O   . LEU B 123 ? 1.4070 0.7595 1.1362 -0.0785 -0.1379 -0.2302 123 LEU B O   
1599 C CB  . LEU B 123 ? 1.3124 0.8237 1.0238 -0.0092 -0.1362 -0.2229 123 LEU B CB  
1600 C CG  . LEU B 123 ? 1.4051 0.8643 1.0794 0.0206  -0.1386 -0.2369 123 LEU B CG  
1601 C CD1 . LEU B 123 ? 1.4233 0.8289 1.0882 0.0096  -0.1587 -0.2742 123 LEU B CD1 
1602 C CD2 . LEU B 123 ? 1.3878 0.8847 1.0332 0.0619  -0.1327 -0.2389 123 LEU B CD2 
1603 N N   . LEU B 124 ? 1.2885 0.7014 1.0205 -0.0545 -0.1120 -0.1752 124 LEU B N   
1604 C CA  . LEU B 124 ? 1.3878 0.7268 1.1017 -0.0563 -0.1050 -0.1593 124 LEU B CA  
1605 C C   . LEU B 124 ? 1.4488 0.7400 1.1770 -0.1020 -0.1022 -0.1600 124 LEU B C   
1606 O O   . LEU B 124 ? 1.5639 0.7717 1.2696 -0.1072 -0.1033 -0.1632 124 LEU B O   
1607 C CB  . LEU B 124 ? 1.2011 0.5606 0.9138 -0.0412 -0.0902 -0.1245 124 LEU B CB  
1608 C CG  . LEU B 124 ? 1.1280 0.5150 0.8267 0.0036  -0.0886 -0.1218 124 LEU B CG  
1609 C CD1 . LEU B 124 ? 1.1113 0.5197 0.8170 0.0125  -0.0766 -0.0917 124 LEU B CD1 
1610 C CD2 . LEU B 124 ? 1.1186 0.4471 0.7859 0.0322  -0.0978 -0.1398 124 LEU B CD2 
1611 N N   . GLU B 125 ? 1.5398 0.8819 1.3062 -0.1356 -0.0969 -0.1579 125 GLU B N   
1612 C CA  . GLU B 125 ? 1.5846 0.8923 1.3725 -0.1837 -0.0871 -0.1557 125 GLU B CA  
1613 C C   . GLU B 125 ? 1.6443 0.8959 1.4340 -0.2045 -0.0997 -0.1904 125 GLU B C   
1614 O O   . GLU B 125 ? 1.8050 0.9825 1.5905 -0.2352 -0.0890 -0.1853 125 GLU B O   
1615 C CB  . GLU B 125 ? 1.4995 0.8889 1.3356 -0.2113 -0.0810 -0.1547 125 GLU B CB  
1616 C CG  . GLU B 125 ? 1.5721 0.9508 1.4216 -0.2446 -0.0563 -0.1259 125 GLU B CG  
1617 C CD  . GLU B 125 ? 1.6704 1.0557 1.4940 -0.2181 -0.0437 -0.0886 125 GLU B CD  
1618 O OE1 . GLU B 125 ? 1.6596 1.1196 1.5026 -0.2073 -0.0422 -0.0812 125 GLU B OE1 
1619 O OE2 . GLU B 125 ? 1.7288 1.0430 1.5120 -0.2066 -0.0369 -0.0684 125 GLU B OE2 
1620 N N   . VAL B 126 ? 1.5420 0.8233 1.3343 -0.1878 -0.1219 -0.2263 126 VAL B N   
1621 C CA  . VAL B 126 ? 1.5404 0.7897 1.3468 -0.2122 -0.1380 -0.2679 126 VAL B CA  
1622 C C   . VAL B 126 ? 1.6824 0.8686 1.4442 -0.1783 -0.1536 -0.2901 126 VAL B C   
1623 O O   . VAL B 126 ? 1.7354 0.9071 1.5029 -0.1861 -0.1733 -0.3322 126 VAL B O   
1624 C CB  . VAL B 126 ? 1.5511 0.8894 1.4000 -0.2235 -0.1555 -0.3000 126 VAL B CB  
1625 C CG1 . VAL B 126 ? 1.5928 0.9959 1.4878 -0.2531 -0.1398 -0.2798 126 VAL B CG1 
1626 C CG2 . VAL B 126 ? 1.5620 0.9536 1.3829 -0.1727 -0.1716 -0.3090 126 VAL B CG2 
1627 N N   . LEU B 127 ? 1.6567 0.8071 1.3762 -0.1399 -0.1464 -0.2659 127 LEU B N   
1628 C CA  . LEU B 127 ? 1.7154 0.8150 1.3941 -0.1022 -0.1605 -0.2888 127 LEU B CA  
1629 C C   . LEU B 127 ? 1.9188 0.9124 1.5824 -0.1173 -0.1584 -0.2942 127 LEU B C   
1630 O O   . LEU B 127 ? 1.9223 0.8927 1.6163 -0.1626 -0.1453 -0.2865 127 LEU B O   
1631 C CB  . LEU B 127 ? 1.6521 0.7737 1.3008 -0.0508 -0.1536 -0.2656 127 LEU B CB  
1632 C CG  . LEU B 127 ? 1.6676 0.7264 1.2870 -0.0296 -0.1425 -0.2358 127 LEU B CG  
1633 C CD1 . LEU B 127 ? 1.6092 0.7308 1.2218 0.0134  -0.1360 -0.2186 127 LEU B CD1 
1634 C CD2 . LEU B 127 ? 1.7811 0.8060 1.4104 -0.0658 -0.1262 -0.2021 127 LEU B CD2 
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