data_9AYD
# 
_entry.id   9AYD 
# 
_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   9AYD         pdb_00009ayd 10.2210/pdb9ayd/pdb 
WWPDB D_1000280737 ?            ?                   
# 
_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                        9AYD 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-07 
_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 non-polymer syn 'TRIETHYLENE GLYCOL'              150.173   2   ? ?    ? ? 
3 non-polymer nat 'ACETATE ION'                     59.044    1   ? ?    ? ? 
4 water       nat water                             18.015    192 ? ?    ? ? 
# 
_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         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'TRIETHYLENE GLYCOL' PGE 
3 'ACETATE ION'        ACT 
4 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
ACT non-polymer         . 'ACETATE ION'        ? 'C2 H3 O2 -1'    59.044  
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 
PGE non-polymer         . 'TRIETHYLENE GLYCOL' ? 'C6 H14 O4'      150.173 
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'     115.130 
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   1   MET MET A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   ALA 3   3   3   ALA ALA A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  PHE 17  17  17  PHE PHE A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  VAL 30  30  30  VAL VAL 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 128 128 128 PHE PHE A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   GLU 2   2   2   GLU GLU B . n 
B 1 3   ALA 3   3   3   ALA ALA B . n 
B 1 4   VAL 4   4   4   VAL VAL B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   ASN 6   6   6   ASN ASN B . n 
B 1 7   GLU 7   7   7   GLU GLU B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  VAL 11  11  11  VAL VAL B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASP 13  13  13  ASP ASP B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  LYS 16  16  16  LYS LYS B . n 
B 1 17  PHE 17  17  17  PHE PHE B . n 
B 1 18  GLU 18  18  18  GLU GLU B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  LYS 25  25  25  LYS LYS B . n 
B 1 26  ALA 26  26  26  ALA ALA B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  SER 29  29  29  SER SER 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 128 128 128 PHE PHE B . n 
B 1 129 GLN 129 129 129 GLN GLN B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PGE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PGE 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 PGE 1  201 150 PGE PJ3 A . 
D 3 ACT 1  202 1   ACT ACT A . 
E 2 PGE 1  201 150 PGE PJ3 B . 
F 4 HOH 1  301 60  HOH HOH A . 
F 4 HOH 2  302 159 HOH HOH A . 
F 4 HOH 3  303 126 HOH HOH A . 
F 4 HOH 4  304 85  HOH HOH A . 
F 4 HOH 5  305 53  HOH HOH A . 
F 4 HOH 6  306 83  HOH HOH A . 
F 4 HOH 7  307 140 HOH HOH A . 
F 4 HOH 8  308 127 HOH HOH A . 
F 4 HOH 9  309 48  HOH HOH A . 
F 4 HOH 10 310 13  HOH HOH A . 
F 4 HOH 11 311 2   HOH HOH A . 
F 4 HOH 12 312 101 HOH HOH A . 
F 4 HOH 13 313 35  HOH HOH A . 
F 4 HOH 14 314 121 HOH HOH A . 
F 4 HOH 15 315 186 HOH HOH A . 
F 4 HOH 16 316 203 HOH HOH A . 
F 4 HOH 17 317 137 HOH HOH A . 
F 4 HOH 18 318 7   HOH HOH A . 
F 4 HOH 19 319 155 HOH HOH A . 
F 4 HOH 20 320 30  HOH HOH A . 
F 4 HOH 21 321 150 HOH HOH A . 
F 4 HOH 22 322 151 HOH HOH A . 
F 4 HOH 23 323 182 HOH HOH A . 
F 4 HOH 24 324 193 HOH HOH A . 
F 4 HOH 25 325 197 HOH HOH A . 
F 4 HOH 26 326 46  HOH HOH A . 
F 4 HOH 27 327 29  HOH HOH A . 
F 4 HOH 28 328 97  HOH HOH A . 
F 4 HOH 29 329 65  HOH HOH A . 
F 4 HOH 30 330 57  HOH HOH A . 
F 4 HOH 31 331 107 HOH HOH A . 
F 4 HOH 32 332 51  HOH HOH A . 
F 4 HOH 33 333 181 HOH HOH A . 
F 4 HOH 34 334 47  HOH HOH A . 
F 4 HOH 35 335 87  HOH HOH A . 
F 4 HOH 36 336 80  HOH HOH A . 
F 4 HOH 37 337 178 HOH HOH A . 
F 4 HOH 38 338 78  HOH HOH A . 
F 4 HOH 39 339 20  HOH HOH A . 
F 4 HOH 40 340 64  HOH HOH A . 
F 4 HOH 41 341 82  HOH HOH A . 
F 4 HOH 42 342 54  HOH HOH A . 
F 4 HOH 43 343 9   HOH HOH A . 
F 4 HOH 44 344 6   HOH HOH A . 
F 4 HOH 45 345 90  HOH HOH A . 
F 4 HOH 46 346 134 HOH HOH A . 
F 4 HOH 47 347 112 HOH HOH A . 
F 4 HOH 48 348 25  HOH HOH A . 
F 4 HOH 49 349 124 HOH HOH A . 
F 4 HOH 50 350 62  HOH HOH A . 
F 4 HOH 51 351 89  HOH HOH A . 
F 4 HOH 52 352 15  HOH HOH A . 
F 4 HOH 53 353 61  HOH HOH A . 
F 4 HOH 54 354 50  HOH HOH A . 
F 4 HOH 55 355 16  HOH HOH A . 
F 4 HOH 56 356 169 HOH HOH A . 
F 4 HOH 57 357 39  HOH HOH A . 
F 4 HOH 58 358 73  HOH HOH A . 
F 4 HOH 59 359 113 HOH HOH A . 
F 4 HOH 60 360 37  HOH HOH A . 
F 4 HOH 61 361 27  HOH HOH A . 
F 4 HOH 62 362 154 HOH HOH A . 
F 4 HOH 63 363 3   HOH HOH A . 
F 4 HOH 64 364 5   HOH HOH A . 
F 4 HOH 65 365 196 HOH HOH A . 
F 4 HOH 66 366 189 HOH HOH A . 
F 4 HOH 67 367 19  HOH HOH A . 
F 4 HOH 68 368 170 HOH HOH A . 
F 4 HOH 69 369 93  HOH HOH A . 
F 4 HOH 70 370 179 HOH HOH A . 
F 4 HOH 71 371 36  HOH HOH A . 
F 4 HOH 72 372 71  HOH HOH A . 
F 4 HOH 73 373 1   HOH HOH A . 
F 4 HOH 74 374 133 HOH HOH A . 
F 4 HOH 75 375 148 HOH HOH A . 
F 4 HOH 76 376 118 HOH HOH A . 
F 4 HOH 77 377 111 HOH HOH A . 
F 4 HOH 78 378 158 HOH HOH A . 
F 4 HOH 79 379 129 HOH HOH A . 
F 4 HOH 80 380 132 HOH HOH A . 
F 4 HOH 81 381 95  HOH HOH A . 
F 4 HOH 82 382 174 HOH HOH A . 
F 4 HOH 83 383 94  HOH HOH A . 
F 4 HOH 84 384 191 HOH HOH A . 
F 4 HOH 85 385 86  HOH HOH A . 
F 4 HOH 86 386 69  HOH HOH A . 
F 4 HOH 87 387 194 HOH HOH A . 
F 4 HOH 88 388 201 HOH HOH A . 
F 4 HOH 89 389 192 HOH HOH A . 
F 4 HOH 90 390 67  HOH HOH A . 
F 4 HOH 91 391 56  HOH HOH A . 
F 4 HOH 92 392 175 HOH HOH A . 
F 4 HOH 93 393 74  HOH HOH A . 
F 4 HOH 94 394 202 HOH HOH A . 
F 4 HOH 95 395 195 HOH HOH A . 
G 4 HOH 1  301 183 HOH HOH B . 
G 4 HOH 2  302 204 HOH HOH B . 
G 4 HOH 3  303 141 HOH HOH B . 
G 4 HOH 4  304 70  HOH HOH B . 
G 4 HOH 5  305 84  HOH HOH B . 
G 4 HOH 6  306 157 HOH HOH B . 
G 4 HOH 7  307 22  HOH HOH B . 
G 4 HOH 8  308 131 HOH HOH B . 
G 4 HOH 9  309 146 HOH HOH B . 
G 4 HOH 10 310 147 HOH HOH B . 
G 4 HOH 11 311 8   HOH HOH B . 
G 4 HOH 12 312 18  HOH HOH B . 
G 4 HOH 13 313 156 HOH HOH B . 
G 4 HOH 14 314 114 HOH HOH B . 
G 4 HOH 15 315 58  HOH HOH B . 
G 4 HOH 16 316 115 HOH HOH B . 
G 4 HOH 17 317 63  HOH HOH B . 
G 4 HOH 18 318 180 HOH HOH B . 
G 4 HOH 19 319 45  HOH HOH B . 
G 4 HOH 20 320 109 HOH HOH B . 
G 4 HOH 21 321 68  HOH HOH B . 
G 4 HOH 22 322 38  HOH HOH B . 
G 4 HOH 23 323 81  HOH HOH B . 
G 4 HOH 24 324 79  HOH HOH B . 
G 4 HOH 25 325 59  HOH HOH B . 
G 4 HOH 26 326 108 HOH HOH B . 
G 4 HOH 27 327 143 HOH HOH B . 
G 4 HOH 28 328 125 HOH HOH B . 
G 4 HOH 29 329 66  HOH HOH B . 
G 4 HOH 30 330 34  HOH HOH B . 
G 4 HOH 31 331 144 HOH HOH B . 
G 4 HOH 32 332 200 HOH HOH B . 
G 4 HOH 33 333 190 HOH HOH B . 
G 4 HOH 34 334 42  HOH HOH B . 
G 4 HOH 35 335 123 HOH HOH B . 
G 4 HOH 36 336 77  HOH HOH B . 
G 4 HOH 37 337 32  HOH HOH B . 
G 4 HOH 38 338 52  HOH HOH B . 
G 4 HOH 39 339 24  HOH HOH B . 
G 4 HOH 40 340 98  HOH HOH B . 
G 4 HOH 41 341 96  HOH HOH B . 
G 4 HOH 42 342 160 HOH HOH B . 
G 4 HOH 43 343 91  HOH HOH B . 
G 4 HOH 44 344 88  HOH HOH B . 
G 4 HOH 45 345 17  HOH HOH B . 
G 4 HOH 46 346 100 HOH HOH B . 
G 4 HOH 47 347 41  HOH HOH B . 
G 4 HOH 48 348 49  HOH HOH B . 
G 4 HOH 49 349 10  HOH HOH B . 
G 4 HOH 50 350 102 HOH HOH B . 
G 4 HOH 51 351 177 HOH HOH B . 
G 4 HOH 52 352 119 HOH HOH B . 
G 4 HOH 53 353 11  HOH HOH B . 
G 4 HOH 54 354 12  HOH HOH B . 
G 4 HOH 55 355 55  HOH HOH B . 
G 4 HOH 56 356 72  HOH HOH B . 
G 4 HOH 57 357 105 HOH HOH B . 
G 4 HOH 58 358 120 HOH HOH B . 
G 4 HOH 59 359 128 HOH HOH B . 
G 4 HOH 60 360 106 HOH HOH B . 
G 4 HOH 61 361 153 HOH HOH B . 
G 4 HOH 62 362 40  HOH HOH B . 
G 4 HOH 63 363 21  HOH HOH B . 
G 4 HOH 64 364 164 HOH HOH B . 
G 4 HOH 65 365 161 HOH HOH B . 
G 4 HOH 66 366 167 HOH HOH B . 
G 4 HOH 67 367 26  HOH HOH B . 
G 4 HOH 68 368 43  HOH HOH B . 
G 4 HOH 69 369 99  HOH HOH B . 
G 4 HOH 70 370 4   HOH HOH B . 
G 4 HOH 71 371 173 HOH HOH B . 
G 4 HOH 72 372 162 HOH HOH B . 
G 4 HOH 73 373 187 HOH HOH B . 
G 4 HOH 74 374 198 HOH HOH B . 
G 4 HOH 75 375 185 HOH HOH B . 
G 4 HOH 76 376 122 HOH HOH B . 
G 4 HOH 77 377 165 HOH HOH B . 
G 4 HOH 78 378 145 HOH HOH B . 
G 4 HOH 79 379 44  HOH HOH B . 
G 4 HOH 80 380 116 HOH HOH B . 
G 4 HOH 81 381 33  HOH HOH B . 
G 4 HOH 82 382 139 HOH HOH B . 
G 4 HOH 83 383 152 HOH HOH B . 
G 4 HOH 84 384 171 HOH HOH B . 
G 4 HOH 85 385 23  HOH HOH B . 
G 4 HOH 86 386 172 HOH HOH B . 
G 4 HOH 87 387 110 HOH HOH B . 
G 4 HOH 88 388 103 HOH HOH B . 
G 4 HOH 89 389 136 HOH HOH B . 
G 4 HOH 90 390 92  HOH HOH B . 
G 4 HOH 91 391 130 HOH HOH B . 
G 4 HOH 92 392 176 HOH HOH B . 
G 4 HOH 93 393 166 HOH HOH B . 
G 4 HOH 94 394 135 HOH HOH B . 
G 4 HOH 95 395 184 HOH HOH B . 
G 4 HOH 96 396 163 HOH HOH B . 
G 4 HOH 97 397 14  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       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0405 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AYD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.500 
_cell.length_a_esd                 ? 
_cell.length_b                     81.440 
_cell.length_b_esd                 ? 
_cell.length_c                     47.190 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9AYD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9AYD 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.64 
_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              4.5 
_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 Acetate (pH 4.5), 30% PEG smear low' 
_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         2022-06-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    '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                                       9AYD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.53 
_reflns.d_resolution_low                               38.861 
_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                                     40271 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.25 
_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                                0.063 
_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                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.06 
_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 
1.53 1.57   ? ? ? ? ? ? 2961 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2.467                ? ? 1  1 0.75               ? ? ? ? 2.375 ? ? ? ? 
? ? ? ? ? 
1.57 1.61   ? ? ? ? ? ? 2841 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2.032                ? ? 2  1 0.8290000000000001 ? ? ? ? 1.956 ? ? ? ? 
? ? ? ? ? 
1.61 1.66   ? ? ? ? ? ? 2791 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.625                ? ? 3  1 0.855              ? ? ? ? 
1.5630000000000002   ? ? ? ? ? ? ? ? ? 
1.66 1.71   ? ? ? ? ? ? 2715 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.4469999999999998   ? ? 4  1 0.88               ? ? ? ? 1.39 ? ? ? ? ? 
? ? ? ? 
1.71 1.77   ? ? ? ? ? ? 2596 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.252                ? ? 5  1 0.889              ? ? ? ? 1.198 ? ? ? ? 
? ? ? ? ? 
1.77 1.83   ? ? ? ? ? ? 2529 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.8420000000000001   ? ? 6  1 0.963              ? ? ? ? 
0.8109999999999999   ? ? ? ? ? ? ? ? ? 
1.83 1.9    ? ? ? ? ? ? 2482 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.5720000000000001   ? ? 7  1 0.985              ? ? ? ? 0.55 ? ? ? ? ? 
? ? ? ? 
1.90 1.98   ? ? ? ? ? ? 2386 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.41200000000000003  ? ? 8  1 0.992              ? ? ? ? 0.397 ? ? ? ? 
? ? ? ? ? 
1.98 2.06   ? ? ? ? ? ? 2270 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.27899999999999997  ? ? 9  1 0.9940000000000001 ? ? ? ? 0.268 ? ? ? ? 
? ? ? ? ? 
2.06 2.16   ? ? ? ? ? ? 2168 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.16899999999999998  ? ? 10 1 0.997              ? ? ? ? 0.163 ? ? ? ? 
? ? ? ? ? 
2.16 2.28   ? ? ? ? ? ? 2071 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.11900000000000001  ? ? 11 1 0.998              ? ? ? ? 0.114 ? ? ? ? 
? ? ? ? ? 
2.28 2.42   ? ? ? ? ? ? 1983 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.083                ? ? 12 1 0.9990000000000001 ? ? ? ? 0.079 ? ? ? ? 
? ? ? ? ? 
2.42 2.59   ? ? ? ? ? ? 1866 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.064                ? ? 13 1 0.9990000000000001 ? ? ? ? 0.062 ? ? ? ? 
? ? ? ? ? 
2.59 2.79   ? ? ? ? ? ? 1755 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.053                ? ? 14 1 0.9990000000000001 ? ? ? ? 0.051 ? ? ? ? 
? ? ? ? ? 
2.79 3.06   ? ? ? ? ? ? 1594 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.046                ? ? 15 1 0.9990000000000001 ? ? ? ? 
0.044000000000000004 ? ? ? ? ? ? ? ? ? 
3.06 3.42   ? ? ? ? ? ? 1460 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.035                ? ? 16 1 0.9990000000000001 ? ? ? ? 0.033 ? ? ? ? 
? ? ? ? ? 
3.42 3.95   ? ? ? ? ? ? 1303 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.027999999999999997 ? ? 17 1 1.0                ? ? ? ? 
0.027000000000000003 ? ? ? ? ? ? ? ? ? 
3.95 4.84   ? ? ? ? ? ? 1113 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.025                ? ? 18 1 1.0                ? ? ? ? 0.024 ? ? ? ? 
? ? ? ? ? 
4.84 6.84   ? ? ? ? ? ? 870  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.024                ? ? 19 1 1.0                ? ? ? ? 0.023 ? ? ? ? 
? ? ? ? ? 
6.84 38.861 ? ? ? ? ? ? 517  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.021                ? ? 20 1 0.9990000000000001 ? ? ? ? 0.02 ? ? ? ? ? 
? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.96 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            1.63 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.67 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               28.962 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.952 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9AYD 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.53 
_refine.ls_d_res_low                             38.86 
_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                     38258 
_refine.ls_number_reflns_R_free                  2014 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.18 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18320 
_refine.ls_R_factor_R_free                       0.22590 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18093 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.104 
_refine.pdbx_overall_ESU_R_Free                  0.088 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.737 
_refine.overall_SU_ML                            0.065 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.53 
_refine_hist.d_res_low                        38.86 
_refine_hist.number_atoms_solvent             192 
_refine_hist.number_atoms_total               2330 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2114 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  0.012  2242 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  2237 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.137  1.647  3006 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.403  1.590  5175 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.166  5.000  274  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.756  5.000  14   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.290 10.000 461  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.062  0.200  325  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  2601 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  499  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.595  2.732  1076 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.578  2.730  1075 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.230  4.908  1356 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.229  4.910  1357 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.845  3.241  1166 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.844  3.242  1167 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.523  5.742  1651 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.278  580.36 2708 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 2.981  587.65 2668 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 2.653  3.000  4473 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.530 
_refine_ls_shell.d_res_low                        1.570 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             148 
_refine_ls_shell.number_reflns_R_work             2808 
_refine_ls_shell.percent_reflns_obs               99.36 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.232 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.307 
# 
_struct.entry_id                     9AYD 
_struct.title                        'Mitochondrial fission 1 (Fis1) protein structure Y38E mutation 1.53A' 
_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        9AYD 
_struct_keywords.text            'Fis1 structure, 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 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_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 9AYD A 1 ? 123 ? Q9Y3D6 1 ? 123 ? 1 123 
2 1 9AYD 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 9AYD GLU A 38  ? UNP Q9Y3D6 TYR 38 'engineered mutation' 38  1  
1 9AYD LEU A 124 ? UNP Q9Y3D6 ?   ?  'expression tag'      124 2  
1 9AYD GLU A 125 ? UNP Q9Y3D6 ?   ?  'expression tag'      125 3  
1 9AYD VAL A 126 ? UNP Q9Y3D6 ?   ?  'expression tag'      126 4  
1 9AYD LEU A 127 ? UNP Q9Y3D6 ?   ?  'expression tag'      127 5  
1 9AYD PHE A 128 ? UNP Q9Y3D6 ?   ?  'expression tag'      128 6  
1 9AYD GLN A 129 ? UNP Q9Y3D6 ?   ?  'expression tag'      129 7  
2 9AYD GLU B 38  ? UNP Q9Y3D6 TYR 38 'engineered mutation' 38  8  
2 9AYD LEU B 124 ? UNP Q9Y3D6 ?   ?  'expression tag'      124 9  
2 9AYD GLU B 125 ? UNP Q9Y3D6 ?   ?  'expression tag'      125 10 
2 9AYD VAL B 126 ? UNP Q9Y3D6 ?   ?  'expression tag'      126 11 
2 9AYD LEU B 127 ? UNP Q9Y3D6 ?   ?  'expression tag'      127 12 
2 9AYD PHE B 128 ? UNP Q9Y3D6 ?   ?  'expression tag'      128 13 
2 9AYD GLN B 129 ? UNP Q9Y3D6 ?   ?  'expression tag'      129 14 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,F 
2 1 B,E,G   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 2   ? ALA A 27  ? GLU A 2   ALA A 27  1 ? 26 
HELX_P HELX_P2  AA2 SER A 31  ? VAL A 43  ? SER A 31  VAL A 43  1 ? 13 
HELX_P HELX_P3  AA3 TYR A 47  ? LEU A 62  ? TYR A 47  LEU A 62  1 ? 16 
HELX_P HELX_P4  AA4 PRO A 63  ? GLY A 65  ? PRO A 63  GLY A 65  5 ? 3  
HELX_P HELX_P5  AA5 SER A 66  ? LEU A 84  ? SER A 66  LEU A 84  1 ? 19 
HELX_P HELX_P6  AA6 GLU A 86  ? GLU A 101 ? GLU A 86  GLU A 101 1 ? 16 
HELX_P HELX_P7  AA7 ASN A 104 ? LYS A 119 ? ASN A 104 LYS A 119 1 ? 16 
HELX_P HELX_P8  AA8 LEU A 124 ? GLN A 129 ? LEU A 124 GLN A 129 5 ? 6  
HELX_P HELX_P9  AA9 GLU B 2   ? GLY B 28  ? GLU B 2   GLY B 28  1 ? 27 
HELX_P HELX_P10 AB1 SER B 31  ? VAL B 43  ? SER B 31  VAL B 43  1 ? 13 
HELX_P HELX_P11 AB2 TYR B 47  ? LEU B 62  ? TYR B 47  LEU B 62  1 ? 16 
HELX_P HELX_P12 AB3 PRO B 63  ? GLY B 65  ? PRO B 63  GLY B 65  5 ? 3  
HELX_P HELX_P13 AB4 SER B 66  ? LEU B 84  ? SER B 66  LEU B 84  1 ? 19 
HELX_P HELX_P14 AB5 GLU B 86  ? GLU B 101 ? GLU B 86  GLU B 101 1 ? 16 
HELX_P HELX_P15 AB6 ASN B 104 ? LYS B 119 ? ASN B 104 LYS B 119 1 ? 16 
HELX_P HELX_P16 AB7 LEU B 124 ? GLN B 129 ? LEU B 124 GLN B 129 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9AYD 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     29 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -150.35 
_pdbx_validate_torsion.psi             77.62 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 372 ? F HOH . 
2 1 B HOH 373 ? G HOH . 
3 1 B HOH 397 ? G HOH . 
# 
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 
ACT C    C N N 1   
ACT O    O N N 2   
ACT OXT  O N N 3   
ACT CH3  C N N 4   
ACT H1   H N N 5   
ACT H2   H N N 6   
ACT H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
GLN N    N N N 95  
GLN CA   C N S 96  
GLN C    C N N 97  
GLN O    O N N 98  
GLN CB   C N N 99  
GLN CG   C N N 100 
GLN CD   C N N 101 
GLN OE1  O N N 102 
GLN NE2  N N N 103 
GLN OXT  O N N 104 
GLN H    H N N 105 
GLN H2   H N N 106 
GLN HA   H N N 107 
GLN HB2  H N N 108 
GLN HB3  H N N 109 
GLN HG2  H N N 110 
GLN HG3  H N N 111 
GLN HE21 H N N 112 
GLN HE22 H N N 113 
GLN HXT  H N N 114 
GLU N    N N N 115 
GLU CA   C N S 116 
GLU C    C N N 117 
GLU O    O N N 118 
GLU CB   C N N 119 
GLU CG   C N N 120 
GLU CD   C N N 121 
GLU OE1  O N N 122 
GLU OE2  O N N 123 
GLU OXT  O N N 124 
GLU H    H N N 125 
GLU H2   H N N 126 
GLU HA   H N N 127 
GLU HB2  H N N 128 
GLU HB3  H N N 129 
GLU HG2  H N N 130 
GLU HG3  H N N 131 
GLU HE2  H N N 132 
GLU HXT  H N N 133 
GLY N    N N N 134 
GLY CA   C N N 135 
GLY C    C N N 136 
GLY O    O N N 137 
GLY OXT  O N N 138 
GLY H    H N N 139 
GLY H2   H N N 140 
GLY HA2  H N N 141 
GLY HA3  H N N 142 
GLY HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PGE C1   C N N 236 
PGE O1   O N N 237 
PGE C2   C N N 238 
PGE O2   O N N 239 
PGE C3   C N N 240 
PGE C4   C N N 241 
PGE O4   O N N 242 
PGE C6   C N N 243 
PGE C5   C N N 244 
PGE O3   O N N 245 
PGE H1   H N N 246 
PGE H12  H N N 247 
PGE HO1  H N N 248 
PGE H2   H N N 249 
PGE H22  H N N 250 
PGE H3   H N N 251 
PGE H32  H N N 252 
PGE H4   H N N 253 
PGE H42  H N N 254 
PGE HO4  H N N 255 
PGE H6   H N N 256 
PGE H62  H N N 257 
PGE H5   H N N 258 
PGE H52  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
THR N    N N N 314 
THR CA   C N S 315 
THR C    C N N 316 
THR O    O N N 317 
THR CB   C N R 318 
THR OG1  O N N 319 
THR CG2  C N N 320 
THR OXT  O N N 321 
THR H    H N N 322 
THR H2   H N N 323 
THR HA   H N N 324 
THR HB   H N N 325 
THR HG1  H N N 326 
THR HG21 H N N 327 
THR HG22 H N N 328 
THR HG23 H N N 329 
THR HXT  H N N 330 
TRP N    N N N 331 
TRP CA   C N S 332 
TRP C    C N N 333 
TRP O    O N N 334 
TRP CB   C N N 335 
TRP CG   C Y N 336 
TRP CD1  C Y N 337 
TRP CD2  C Y N 338 
TRP NE1  N Y N 339 
TRP CE2  C Y N 340 
TRP CE3  C Y N 341 
TRP CZ2  C Y N 342 
TRP CZ3  C Y N 343 
TRP CH2  C Y N 344 
TRP OXT  O N N 345 
TRP H    H N N 346 
TRP H2   H N N 347 
TRP HA   H N N 348 
TRP HB2  H N N 349 
TRP HB3  H N N 350 
TRP HD1  H N N 351 
TRP HE1  H N N 352 
TRP HE3  H N N 353 
TRP HZ2  H N N 354 
TRP HZ3  H N N 355 
TRP HH2  H N N 356 
TRP HXT  H N N 357 
TYR N    N N N 358 
TYR CA   C N S 359 
TYR C    C N N 360 
TYR O    O N N 361 
TYR CB   C N N 362 
TYR CG   C Y N 363 
TYR CD1  C Y N 364 
TYR CD2  C Y N 365 
TYR CE1  C Y N 366 
TYR CE2  C Y N 367 
TYR CZ   C Y N 368 
TYR OH   O N N 369 
TYR OXT  O N N 370 
TYR H    H N N 371 
TYR H2   H N N 372 
TYR HA   H N N 373 
TYR HB2  H N N 374 
TYR HB3  H N N 375 
TYR HD1  H N N 376 
TYR HD2  H N N 377 
TYR HE1  H N N 378 
TYR HE2  H N N 379 
TYR HH   H N N 380 
TYR HXT  H N N 381 
VAL N    N N N 382 
VAL CA   C N S 383 
VAL C    C N N 384 
VAL O    O N N 385 
VAL CB   C N N 386 
VAL CG1  C N N 387 
VAL CG2  C N N 388 
VAL OXT  O N N 389 
VAL H    H N N 390 
VAL H2   H N N 391 
VAL HA   H N N 392 
VAL HB   H N N 393 
VAL HG11 H N N 394 
VAL HG12 H N N 395 
VAL HG13 H N N 396 
VAL HG21 H N N 397 
VAL HG22 H N N 398 
VAL HG23 H N N 399 
VAL HXT  H N N 400 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
HOH O   H1   sing N N 135 
HOH O   H2   sing N N 136 
ILE N   CA   sing N N 137 
ILE N   H    sing N N 138 
ILE N   H2   sing N N 139 
ILE CA  C    sing N N 140 
ILE CA  CB   sing N N 141 
ILE CA  HA   sing N N 142 
ILE C   O    doub N N 143 
ILE C   OXT  sing N N 144 
ILE CB  CG1  sing N N 145 
ILE CB  CG2  sing N N 146 
ILE CB  HB   sing N N 147 
ILE CG1 CD1  sing N N 148 
ILE CG1 HG12 sing N N 149 
ILE CG1 HG13 sing N N 150 
ILE CG2 HG21 sing N N 151 
ILE CG2 HG22 sing N N 152 
ILE CG2 HG23 sing N N 153 
ILE CD1 HD11 sing N N 154 
ILE CD1 HD12 sing N N 155 
ILE CD1 HD13 sing N N 156 
ILE OXT HXT  sing N N 157 
LEU N   CA   sing N N 158 
LEU N   H    sing N N 159 
LEU N   H2   sing N N 160 
LEU CA  C    sing N N 161 
LEU CA  CB   sing N N 162 
LEU CA  HA   sing N N 163 
LEU C   O    doub N N 164 
LEU C   OXT  sing N N 165 
LEU CB  CG   sing N N 166 
LEU CB  HB2  sing N N 167 
LEU CB  HB3  sing N N 168 
LEU CG  CD1  sing N N 169 
LEU CG  CD2  sing N N 170 
LEU CG  HG   sing N N 171 
LEU CD1 HD11 sing N N 172 
LEU CD1 HD12 sing N N 173 
LEU CD1 HD13 sing N N 174 
LEU CD2 HD21 sing N N 175 
LEU CD2 HD22 sing N N 176 
LEU CD2 HD23 sing N N 177 
LEU OXT HXT  sing N N 178 
LYS N   CA   sing N N 179 
LYS N   H    sing N N 180 
LYS N   H2   sing N N 181 
LYS CA  C    sing N N 182 
LYS CA  CB   sing N N 183 
LYS CA  HA   sing N N 184 
LYS C   O    doub N N 185 
LYS C   OXT  sing N N 186 
LYS CB  CG   sing N N 187 
LYS CB  HB2  sing N N 188 
LYS CB  HB3  sing N N 189 
LYS CG  CD   sing N N 190 
LYS CG  HG2  sing N N 191 
LYS CG  HG3  sing N N 192 
LYS CD  CE   sing N N 193 
LYS CD  HD2  sing N N 194 
LYS CD  HD3  sing N N 195 
LYS CE  NZ   sing N N 196 
LYS CE  HE2  sing N N 197 
LYS CE  HE3  sing N N 198 
LYS NZ  HZ1  sing N N 199 
LYS NZ  HZ2  sing N N 200 
LYS NZ  HZ3  sing N N 201 
LYS OXT HXT  sing N N 202 
MET N   CA   sing N N 203 
MET N   H    sing N N 204 
MET N   H2   sing N N 205 
MET CA  C    sing N N 206 
MET CA  CB   sing N N 207 
MET CA  HA   sing N N 208 
MET C   O    doub N N 209 
MET C   OXT  sing N N 210 
MET CB  CG   sing N N 211 
MET CB  HB2  sing N N 212 
MET CB  HB3  sing N N 213 
MET CG  SD   sing N N 214 
MET CG  HG2  sing N N 215 
MET CG  HG3  sing N N 216 
MET SD  CE   sing N N 217 
MET CE  HE1  sing N N 218 
MET CE  HE2  sing N N 219 
MET CE  HE3  sing N N 220 
MET OXT HXT  sing N N 221 
PGE C1  O1   sing N N 222 
PGE C1  C2   sing N N 223 
PGE C1  H1   sing N N 224 
PGE C1  H12  sing N N 225 
PGE O1  HO1  sing N N 226 
PGE C2  O2   sing N N 227 
PGE C2  H2   sing N N 228 
PGE C2  H22  sing N N 229 
PGE O2  C3   sing N N 230 
PGE C3  C4   sing N N 231 
PGE C3  H3   sing N N 232 
PGE C3  H32  sing N N 233 
PGE C4  O3   sing N N 234 
PGE C4  H4   sing N N 235 
PGE C4  H42  sing N N 236 
PGE O4  C6   sing N N 237 
PGE O4  HO4  sing N N 238 
PGE C6  C5   sing N N 239 
PGE C6  H6   sing N N 240 
PGE C6  H62  sing N N 241 
PGE C5  O3   sing N N 242 
PGE C5  H5   sing N N 243 
PGE C5  H52  sing N N 244 
PHE N   CA   sing N N 245 
PHE N   H    sing N N 246 
PHE N   H2   sing N N 247 
PHE CA  C    sing N N 248 
PHE CA  CB   sing N N 249 
PHE CA  HA   sing N N 250 
PHE C   O    doub N N 251 
PHE C   OXT  sing N N 252 
PHE CB  CG   sing N N 253 
PHE CB  HB2  sing N N 254 
PHE CB  HB3  sing N N 255 
PHE CG  CD1  doub Y N 256 
PHE CG  CD2  sing Y N 257 
PHE CD1 CE1  sing Y N 258 
PHE CD1 HD1  sing N N 259 
PHE CD2 CE2  doub Y N 260 
PHE CD2 HD2  sing N N 261 
PHE CE1 CZ   doub Y N 262 
PHE CE1 HE1  sing N N 263 
PHE CE2 CZ   sing Y N 264 
PHE CE2 HE2  sing N N 265 
PHE CZ  HZ   sing N N 266 
PHE OXT HXT  sing N N 267 
PRO N   CA   sing N N 268 
PRO N   CD   sing N N 269 
PRO N   H    sing N N 270 
PRO CA  C    sing N N 271 
PRO CA  CB   sing N N 272 
PRO CA  HA   sing N N 273 
PRO C   O    doub N N 274 
PRO C   OXT  sing N N 275 
PRO CB  CG   sing N N 276 
PRO CB  HB2  sing N N 277 
PRO CB  HB3  sing N N 278 
PRO CG  CD   sing N N 279 
PRO CG  HG2  sing N N 280 
PRO CG  HG3  sing N N 281 
PRO CD  HD2  sing N N 282 
PRO CD  HD3  sing N N 283 
PRO OXT HXT  sing N N 284 
SER N   CA   sing N N 285 
SER N   H    sing N N 286 
SER N   H2   sing N N 287 
SER CA  C    sing N N 288 
SER CA  CB   sing N N 289 
SER CA  HA   sing N N 290 
SER C   O    doub N N 291 
SER C   OXT  sing N N 292 
SER CB  OG   sing N N 293 
SER CB  HB2  sing N N 294 
SER CB  HB3  sing N N 295 
SER OG  HG   sing N N 296 
SER OXT HXT  sing N N 297 
THR N   CA   sing N N 298 
THR N   H    sing N N 299 
THR N   H2   sing N N 300 
THR CA  C    sing N N 301 
THR CA  CB   sing N N 302 
THR CA  HA   sing N N 303 
THR C   O    doub N N 304 
THR C   OXT  sing N N 305 
THR CB  OG1  sing N N 306 
THR CB  CG2  sing N N 307 
THR CB  HB   sing N N 308 
THR OG1 HG1  sing N N 309 
THR CG2 HG21 sing N N 310 
THR CG2 HG22 sing N N 311 
THR CG2 HG23 sing N N 312 
THR OXT HXT  sing N N 313 
TRP N   CA   sing N N 314 
TRP N   H    sing N N 315 
TRP N   H2   sing N N 316 
TRP CA  C    sing N N 317 
TRP CA  CB   sing N N 318 
TRP CA  HA   sing N N 319 
TRP C   O    doub N N 320 
TRP C   OXT  sing N N 321 
TRP CB  CG   sing N N 322 
TRP CB  HB2  sing N N 323 
TRP CB  HB3  sing N N 324 
TRP CG  CD1  doub Y N 325 
TRP CG  CD2  sing Y N 326 
TRP CD1 NE1  sing Y N 327 
TRP CD1 HD1  sing N N 328 
TRP CD2 CE2  doub Y N 329 
TRP CD2 CE3  sing Y N 330 
TRP NE1 CE2  sing Y N 331 
TRP NE1 HE1  sing N N 332 
TRP CE2 CZ2  sing Y N 333 
TRP CE3 CZ3  doub Y N 334 
TRP CE3 HE3  sing N N 335 
TRP CZ2 CH2  doub Y N 336 
TRP CZ2 HZ2  sing N N 337 
TRP CZ3 CH2  sing Y N 338 
TRP CZ3 HZ3  sing N N 339 
TRP CH2 HH2  sing N N 340 
TRP OXT HXT  sing N N 341 
TYR N   CA   sing N N 342 
TYR N   H    sing N N 343 
TYR N   H2   sing N N 344 
TYR CA  C    sing N N 345 
TYR CA  CB   sing N N 346 
TYR CA  HA   sing N N 347 
TYR C   O    doub N N 348 
TYR C   OXT  sing N N 349 
TYR CB  CG   sing N N 350 
TYR CB  HB2  sing N N 351 
TYR CB  HB3  sing N N 352 
TYR CG  CD1  doub Y N 353 
TYR CG  CD2  sing Y N 354 
TYR CD1 CE1  sing Y N 355 
TYR CD1 HD1  sing N N 356 
TYR CD2 CE2  doub Y N 357 
TYR CD2 HD2  sing N N 358 
TYR CE1 CZ   doub Y N 359 
TYR CE1 HE1  sing N N 360 
TYR CE2 CZ   sing Y N 361 
TYR CE2 HE2  sing N N 362 
TYR CZ  OH   sing N N 363 
TYR OH  HH   sing N N 364 
TYR OXT HXT  sing N N 365 
VAL N   CA   sing N N 366 
VAL N   H    sing N N 367 
VAL N   H2   sing N N 368 
VAL CA  C    sing N N 369 
VAL CA  CB   sing N N 370 
VAL CA  HA   sing N N 371 
VAL C   O    doub N N 372 
VAL C   OXT  sing N N 373 
VAL CB  CG1  sing N N 374 
VAL CB  CG2  sing N N 375 
VAL CB  HB   sing N N 376 
VAL CG1 HG11 sing N N 377 
VAL CG1 HG12 sing N N 378 
VAL CG1 HG13 sing N N 379 
VAL CG2 HG21 sing N N 380 
VAL CG2 HG22 sing N N 381 
VAL CG2 HG23 sing N N 382 
VAL OXT HXT  sing N N 383 
# 
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                    9AYD 
_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]   0.014599 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012279 
_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]   0.021191 
_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   . MET A 1 1   ? 30.255 0.903   40.925  1.00 57.86 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 29.746 -0.125  39.979  1.00 57.44 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 30.914 -0.979  39.489  1.00 48.81 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 31.555 -0.650  38.496  1.00 47.95 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 28.967 0.522   38.819  1.00 65.23 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 29.766 0.891   37.557  1.00 72.05 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 30.116 2.670   37.415  1.00 81.07 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 31.898 2.672   37.213  1.00 82.53 ? 1   MET A CE  1 
ATOM   9    N N   . GLU A 1 2   ? 31.217 -2.050  40.237  1.00 43.60 ? 2   GLU A N   1 
ATOM   10   C CA  . GLU A 1 2   ? 32.099 -3.097  39.746  1.00 42.59 ? 2   GLU A CA  1 
ATOM   11   C C   . GLU A 1 2   ? 31.606 -3.482  38.355  1.00 41.80 ? 2   GLU A C   1 
ATOM   12   O O   . GLU A 1 2   ? 30.406 -3.665  38.156  1.00 36.89 ? 2   GLU A O   1 
ATOM   13   C CB  . GLU A 1 2   ? 32.119 -4.279  40.724  1.00 44.69 ? 2   GLU A CB  1 
ATOM   14   C CG  . GLU A 1 2   ? 32.937 -5.480  40.265  1.00 45.53 ? 2   GLU A CG  1 
ATOM   15   C CD  . GLU A 1 2   ? 33.034 -6.606  41.289  1.00 44.16 ? 2   GLU A CD  1 
ATOM   16   O OE1 . GLU A 1 2   ? 32.014 -6.887  41.961  1.00 39.35 ? 2   GLU A OE1 1 
ATOM   17   O OE2 . GLU A 1 2   ? 34.124 -7.218  41.405  1.00 46.91 ? 2   GLU A OE2 1 
ATOM   18   N N   . ALA A 1 3   ? 32.537 -3.569  37.399  1.00 40.96 ? 3   ALA A N   1 
ATOM   19   C CA  . ALA A 1 3   ? 32.185 -3.668  35.992  1.00 39.73 ? 3   ALA A CA  1 
ATOM   20   C C   . ALA A 1 3   ? 31.467 -4.987  35.699  1.00 39.53 ? 3   ALA A C   1 
ATOM   21   O O   . ALA A 1 3   ? 30.475 -4.988  34.972  1.00 40.47 ? 3   ALA A O   1 
ATOM   22   C CB  . ALA A 1 3   ? 33.423 -3.500  35.151  1.00 39.35 ? 3   ALA A CB  1 
ATOM   23   N N   . VAL A 1 4   ? 31.956 -6.097  36.279  1.00 41.11 ? 4   VAL A N   1 
ATOM   24   C CA  . VAL A 1 4   ? 31.366 -7.415  36.078  1.00 42.31 ? 4   VAL A CA  1 
ATOM   25   C C   . VAL A 1 4   ? 29.989 -7.500  36.741  1.00 39.01 ? 4   VAL A C   1 
ATOM   26   O O   . VAL A 1 4   ? 29.105 -8.204  36.258  1.00 40.12 ? 4   VAL A O   1 
ATOM   27   C CB  . VAL A 1 4   ? 32.283 -8.538  36.599  1.00 44.63 ? 4   VAL A CB  1 
ATOM   28   C CG1 . VAL A 1 4   ? 31.564 -9.880  36.651  1.00 45.60 ? 4   VAL A CG1 1 
ATOM   29   C CG2 . VAL A 1 4   ? 33.559 -8.657  35.778  1.00 47.59 ? 4   VAL A CG2 1 
ATOM   30   N N   . LEU A 1 5   ? 29.812 -6.822  37.877  1.00 37.78 ? 5   LEU A N   1 
ATOM   31   C CA  . LEU A 1 5   ? 28.497 -6.748  38.490  1.00 34.34 ? 5   LEU A CA  1 
ATOM   32   C C   . LEU A 1 5   ? 27.543 -5.963  37.588  1.00 35.87 ? 5   LEU A C   1 
ATOM   33   O O   . LEU A 1 5   ? 26.380 -6.336  37.422  1.00 33.88 ? 5   LEU A O   1 
ATOM   34   C CB  . LEU A 1 5   ? 28.631 -6.074  39.856  1.00 32.64 ? 5   LEU A CB  1 
ATOM   35   C CG  . LEU A 1 5   ? 27.340 -5.950  40.656  1.00 29.49 ? 5   LEU A CG  1 
ATOM   36   C CD1 . LEU A 1 5   ? 26.706 -7.319  40.900  1.00 28.02 ? 5   LEU A CD1 1 
ATOM   37   C CD2 . LEU A 1 5   ? 27.622 -5.244  41.971  1.00 27.68 ? 5   LEU A CD2 1 
ATOM   38   N N   . ASN A 1 6   ? 28.043 -4.869  37.009  1.00 38.05 ? 6   ASN A N   1 
ATOM   39   C CA  . ASN A 1 6   ? 27.230 -4.020  36.153  1.00 40.15 ? 6   ASN A CA  1 
ATOM   40   C C   . ASN A 1 6   ? 26.692 -4.831  34.973  1.00 39.55 ? 6   ASN A C   1 
ATOM   41   O O   . ASN A 1 6   ? 25.536 -4.675  34.590  1.00 40.28 ? 6   ASN A O   1 
ATOM   42   C CB  . ASN A 1 6   ? 28.003 -2.785  35.680  1.00 42.58 ? 6   ASN A CB  1 
ATOM   43   C CG  . ASN A 1 6   ? 27.111 -1.678  35.156  1.00 47.06 ? 6   ASN A CG  1 
ATOM   44   O OD1 . ASN A 1 6   ? 25.886 -1.751  35.243  1.00 48.26 ? 6   ASN A OD1 1 
ATOM   45   N ND2 . ASN A 1 6   ? 27.719 -0.630  34.623  1.00 51.63 ? 6   ASN A ND2 1 
ATOM   46   N N   . GLU A 1 7   ? 27.529 -5.695  34.391  1.00 39.61 ? 7   GLU A N   1 
ATOM   47   C CA  . GLU A 1 7   ? 27.103 -6.498  33.253  1.00 42.05 ? 7   GLU A CA  1 
ATOM   48   C C   . GLU A 1 7   ? 26.005 -7.467  33.686  1.00 40.55 ? 7   GLU A C   1 
ATOM   49   O O   . GLU A 1 7   ? 25.048 -7.703  32.958  1.00 39.19 ? 7   GLU A O   1 
ATOM   50   C CB  . GLU A 1 7   ? 28.296 -7.246  32.660  1.00 44.97 ? 7   GLU A CB  1 
ATOM   51   C CG  . GLU A 1 7   ? 29.277 -6.340  31.946  1.00 48.64 ? 7   GLU A CG  1 
ATOM   52   C CD  . GLU A 1 7   ? 28.770 -5.802  30.621  1.00 55.02 ? 7   GLU A CD  1 
ATOM   53   O OE1 . GLU A 1 7   ? 28.570 -6.611  29.688  1.00 62.48 ? 7   GLU A OE1 1 
ATOM   54   O OE2 . GLU A 1 7   ? 28.570 -4.581  30.526  1.00 61.83 ? 7   GLU A OE2 1 
ATOM   55   N N   . LEU A 1 8   ? 26.152 -7.998  34.900  1.00 37.56 ? 8   LEU A N   1 
ATOM   56   C CA  . LEU A 1 8   ? 25.267 -9.010  35.448  1.00 37.66 ? 8   LEU A CA  1 
ATOM   57   C C   . LEU A 1 8   ? 23.859 -8.453  35.677  1.00 33.99 ? 8   LEU A C   1 
ATOM   58   O O   . LEU A 1 8   ? 22.857 -9.075  35.321  1.00 33.19 ? 8   LEU A O   1 
ATOM   59   C CB  . LEU A 1 8   ? 25.926 -9.464  36.753  1.00 38.46 ? 8   LEU A CB  1 
ATOM   60   C CG  . LEU A 1 8   ? 25.310 -10.657 37.468  1.00 39.28 ? 8   LEU A CG  1 
ATOM   61   C CD1 . LEU A 1 8   ? 26.271 -11.159 38.525  1.00 37.36 ? 8   LEU A CD1 1 
ATOM   62   C CD2 . LEU A 1 8   ? 23.979 -10.307 38.107  1.00 38.55 ? 8   LEU A CD2 1 
ATOM   63   N N   . VAL A 1 9   ? 23.783 -7.276  36.295  1.00 29.89 ? 9   VAL A N   1 
ATOM   64   C CA  . VAL A 1 9   ? 22.495 -6.676  36.594  1.00 28.76 ? 9   VAL A CA  1 
ATOM   65   C C   . VAL A 1 9   ? 21.854 -6.180  35.302  1.00 28.00 ? 9   VAL A C   1 
ATOM   66   O O   . VAL A 1 9   ? 20.632 -6.170  35.194  1.00 25.94 ? 9   VAL A O   1 
ATOM   67   C CB  . VAL A 1 9   ? 22.609 -5.557  37.648  1.00 29.45 ? 9   VAL A CB  1 
ATOM   68   C CG1 . VAL A 1 9   ? 23.215 -6.090  38.939  1.00 29.24 ? 9   VAL A CG1 1 
ATOM   69   C CG2 . VAL A 1 9   ? 23.383 -4.349  37.147  1.00 30.97 ? 9   VAL A CG2 1 
ATOM   70   N N   . SER A 1 10  ? 22.683 -5.738  34.347  1.00 30.60 ? 10  SER A N   1 
ATOM   71   C CA  . SER A 1 10  ? 22.186 -5.264  33.066  1.00 29.76 ? 10  SER A CA  1 
ATOM   72   C C   . SER A 1 10  ? 21.386 -6.367  32.375  1.00 29.28 ? 10  SER A C   1 
ATOM   73   O O   . SER A 1 10  ? 20.331 -6.111  31.805  1.00 29.62 ? 10  SER A O   1 
ATOM   74   C CB  . SER A 1 10  ? 23.306 -4.749  32.192  1.00 33.24 ? 10  SER A CB  1 
ATOM   75   O OG  . SER A 1 10  ? 23.807 -3.519  32.704  1.00 38.59 ? 10  SER A OG  1 
ATOM   76   N N   . VAL A 1 11  ? 21.883 -7.606  32.452  1.00 30.36 ? 11  VAL A N   1 
ATOM   77   C CA  . VAL A 1 11  ? 21.205 -8.731  31.826  1.00 30.79 ? 11  VAL A CA  1 
ATOM   78   C C   . VAL A 1 11  ? 19.880 -9.017  32.539  1.00 29.00 ? 11  VAL A C   1 
ATOM   79   O O   . VAL A 1 11  ? 18.860 -9.217  31.887  1.00 28.25 ? 11  VAL A O   1 
ATOM   80   C CB  . VAL A 1 11  ? 22.116 -9.968  31.761  1.00 33.54 ? 11  VAL A CB  1 
ATOM   81   C CG1 . VAL A 1 11  ? 21.371 -11.164 31.204  1.00 33.32 ? 11  VAL A CG1 1 
ATOM   82   C CG2 . VAL A 1 11  ? 23.361 -9.678  30.935  1.00 33.27 ? 11  VAL A CG2 1 
ATOM   83   N N   . GLU A 1 12  ? 19.878 -9.031  33.876  1.00 29.51 ? 12  GLU A N   1 
ATOM   84   C CA  . GLU A 1 12  ? 18.642 -9.202  34.625  1.00 27.50 ? 12  GLU A CA  1 
ATOM   85   C C   . GLU A 1 12  ? 17.607 -8.157  34.182  1.00 27.33 ? 12  GLU A C   1 
ATOM   86   O O   . GLU A 1 12  ? 16.441 -8.470  33.957  1.00 29.40 ? 12  GLU A O   1 
ATOM   87   C CB  . GLU A 1 12  ? 18.945 -9.111  36.124  1.00 31.61 ? 12  GLU A CB  1 
ATOM   88   C CG  . GLU A 1 12  ? 17.742 -9.362  37.016  1.00 36.89 ? 12  GLU A CG  1 
ATOM   89   C CD  . GLU A 1 12  ? 17.280 -10.804 37.167  1.00 41.65 ? 12  GLU A CD  1 
ATOM   90   O OE1 . GLU A 1 12  ? 17.925 -11.721 36.615  1.00 43.05 ? 12  GLU A OE1 1 
ATOM   91   O OE2 . GLU A 1 12  ? 16.264 -11.007 37.846  1.00 46.25 ? 12  GLU A OE2 1 
ATOM   92   N N   . ASP A 1 13  ? 18.026 -6.897  34.064  1.00 24.98 ? 13  ASP A N   1 
ATOM   93   C CA  . ASP A 1 13  ? 17.111 -5.842  33.657  1.00 26.34 ? 13  ASP A CA  1 
ATOM   94   C C   . ASP A 1 13  ? 16.614 -6.053  32.225  1.00 24.57 ? 13  ASP A C   1 
ATOM   95   O O   . ASP A 1 13  ? 15.456 -5.780  31.915  1.00 25.40 ? 13  ASP A O   1 
ATOM   96   C CB  . ASP A 1 13  ? 17.784 -4.475  33.777  1.00 27.87 ? 13  ASP A CB  1 
ATOM   97   C CG  . ASP A 1 13  ? 18.018 -3.985  35.194  1.00 29.22 ? 13  ASP A CG  1 
ATOM   98   O OD1 . ASP A 1 13  ? 17.483 -4.621  36.146  1.00 29.52 ? 13  ASP A OD1 1 
ATOM   99   O OD2 . ASP A 1 13  ? 18.736 -2.965  35.336  1.00 28.35 ? 13  ASP A OD2 1 
ATOM   100  N N   . LEU A 1 14  ? 17.513 -6.488  31.340  1.00 26.31 ? 14  LEU A N   1 
ATOM   101  C CA  . LEU A 1 14  ? 17.184 -6.743  29.949  1.00 28.23 ? 14  LEU A CA  1 
ATOM   102  C C   . LEU A 1 14  ? 16.095 -7.808  29.821  1.00 28.55 ? 14  LEU A C   1 
ATOM   103  O O   . LEU A 1 14  ? 15.147 -7.644  29.064  1.00 29.63 ? 14  LEU A O   1 
ATOM   104  C CB  . LEU A 1 14  ? 18.457 -7.186  29.226  1.00 30.46 ? 14  LEU A CB  1 
ATOM   105  C CG  . LEU A 1 14  ? 18.274 -7.601  27.770  1.00 33.72 ? 14  LEU A CG  1 
ATOM   106  C CD1 . LEU A 1 14  ? 17.813 -6.427  26.920  1.00 34.05 ? 14  LEU A CD1 1 
ATOM   107  C CD2 . LEU A 1 14  ? 19.566 -8.188  27.219  1.00 36.75 ? 14  LEU A CD2 1 
ATOM   108  N N   . LEU A 1 15  ? 16.237 -8.921  30.544  1.00 28.26 ? 15  LEU A N   1 
ATOM   109  C CA  . LEU A 1 15  ? 15.250 -9.989  30.467  1.00 30.47 ? 15  LEU A CA  1 
ATOM   110  C C   . LEU A 1 15  ? 13.884 -9.518  30.972  1.00 28.00 ? 15  LEU A C   1 
ATOM   111  O O   . LEU A 1 15  ? 12.854 -9.863  30.405  1.00 30.62 ? 15  LEU A O   1 
ATOM   112  C CB  . LEU A 1 15  ? 15.759 -11.197 31.258  1.00 33.59 ? 15  LEU A CB  1 
ATOM   113  C CG  . LEU A 1 15  ? 17.014 -11.869 30.702  1.00 37.88 ? 15  LEU A CG  1 
ATOM   114  C CD1 . LEU A 1 15  ? 17.380 -13.084 31.543  1.00 39.00 ? 15  LEU A CD1 1 
ATOM   115  C CD2 . LEU A 1 15  ? 16.847 -12.258 29.243  1.00 39.41 ? 15  LEU A CD2 1 
ATOM   116  N N   . LYS A 1 16  ? 13.868 -8.702  32.028  1.00 27.71 ? 16  LYS A N   1 
ATOM   117  C CA  . LYS A 1 16  ? 12.619 -8.175  32.553  1.00 30.92 ? 16  LYS A CA  1 
ATOM   118  C C   . LYS A 1 16  ? 11.967 -7.243  31.530  1.00 28.41 ? 16  LYS A C   1 
ATOM   119  O O   . LYS A 1 16  ? 10.753 -7.284  31.344  1.00 28.36 ? 16  LYS A O   1 
ATOM   120  C CB  . LYS A 1 16  ? 12.871 -7.461  33.884  1.00 34.18 ? 16  LYS A CB  1 
ATOM   121  C CG  . LYS A 1 16  ? 11.685 -6.699  34.468  1.00 37.28 ? 16  LYS A CG  1 
ATOM   122  C CD  . LYS A 1 16  ? 11.950 -6.147  35.856  1.00 42.97 ? 16  LYS A CD  1 
ATOM   123  C CE  . LYS A 1 16  ? 12.944 -5.006  35.876  1.00 47.68 ? 16  LYS A CE  1 
ATOM   124  N NZ  . LYS A 1 16  ? 13.410 -4.713  37.252  1.00 53.04 ? 16  LYS A NZ  1 
ATOM   125  N N   . PHE A 1 17  ? 12.776 -6.401  30.877  1.00 26.34 ? 17  PHE A N   1 
ATOM   126  C CA  . PHE A 1 17  ? 12.257 -5.480  29.880  1.00 24.85 ? 17  PHE A CA  1 
ATOM   127  C C   . PHE A 1 17  ? 11.759 -6.257  28.663  1.00 24.26 ? 17  PHE A C   1 
ATOM   128  O O   . PHE A 1 17  ? 10.709 -5.975  28.104  1.00 25.52 ? 17  PHE A O   1 
ATOM   129  C CB  . PHE A 1 17  ? 13.319 -4.464  29.455  1.00 24.82 ? 17  PHE A CB  1 
ATOM   130  C CG  . PHE A 1 17  ? 12.808 -3.554  28.376  1.00 24.06 ? 17  PHE A CG  1 
ATOM   131  C CD1 . PHE A 1 17  ? 11.782 -2.670  28.662  1.00 25.60 ? 17  PHE A CD1 1 
ATOM   132  C CD2 . PHE A 1 17  ? 13.295 -3.622  27.082  1.00 24.59 ? 17  PHE A CD2 1 
ATOM   133  C CE1 . PHE A 1 17  ? 11.274 -1.844  27.680  1.00 24.65 ? 17  PHE A CE1 1 
ATOM   134  C CE2 . PHE A 1 17  ? 12.761 -2.816  26.091  1.00 26.00 ? 17  PHE A CE2 1 
ATOM   135  C CZ  . PHE A 1 17  ? 11.756 -1.925  26.393  1.00 25.86 ? 17  PHE A CZ  1 
ATOM   136  N N   . GLU A 1 18  ? 12.524 -7.259  28.245  1.00 25.11 ? 18  GLU A N   1 
ATOM   137  C CA  . GLU A 1 18  ? 12.116 -8.069  27.116  1.00 25.39 ? 18  GLU A CA  1 
ATOM   138  C C   . GLU A 1 18  ? 10.727 -8.654  27.372  1.00 27.23 ? 18  GLU A C   1 
ATOM   139  O O   . GLU A 1 18  ? 9.876  -8.679  26.484  1.00 26.56 ? 18  GLU A O   1 
ATOM   140  C CB  . GLU A 1 18  ? 13.147 -9.175  26.903  1.00 27.61 ? 18  GLU A CB  1 
ATOM   141  C CG  . GLU A 1 18  ? 12.765 -10.123 25.796  1.00 27.81 ? 18  GLU A CG  1 
ATOM   142  C CD  . GLU A 1 18  ? 13.752 -11.243 25.555  1.00 31.38 ? 18  GLU A CD  1 
ATOM   143  O OE1 . GLU A 1 18  ? 14.739 -11.334 26.307  1.00 35.24 ? 18  GLU A OE1 1 
ATOM   144  O OE2 . GLU A 1 18  ? 13.533 -11.994 24.594  1.00 34.86 ? 18  GLU A OE2 1 
ATOM   145  N N   . LYS A 1 19  ? 10.523 -9.146  28.599  1.00 27.06 ? 19  LYS A N   1 
ATOM   146  C CA  . LYS A 1 19  ? 9.243  -9.698  29.004  1.00 30.40 ? 19  LYS A CA  1 
ATOM   147  C C   . LYS A 1 19  ? 8.158  -8.641  28.802  1.00 29.40 ? 19  LYS A C   1 
ATOM   148  O O   . LYS A 1 19  ? 7.125  -8.918  28.202  1.00 32.80 ? 19  LYS A O   1 
ATOM   149  C CB  . LYS A 1 19  ? 9.337  -10.204 30.448  1.00 33.98 ? 19  LYS A CB  1 
ATOM   150  C CG  . LYS A 1 19  ? 8.280  -11.205 30.888  1.00 39.80 ? 19  LYS A CG  1 
ATOM   151  C CD  . LYS A 1 19  ? 8.720  -11.969 32.128  1.00 43.07 ? 19  LYS A CD  1 
ATOM   152  C CE  . LYS A 1 19  ? 7.776  -13.077 32.537  1.00 48.62 ? 19  LYS A CE  1 
ATOM   153  N NZ  . LYS A 1 19  ? 6.488  -12.549 33.045  1.00 51.91 ? 19  LYS A NZ  1 
ATOM   154  N N   . LYS A 1 20  ? 8.404  -7.422  29.295  1.00 29.86 ? 20  LYS A N   1 
ATOM   155  C CA  . LYS A 1 20  ? 7.457  -6.324  29.175  1.00 29.74 ? 20  LYS A CA  1 
ATOM   156  C C   . LYS A 1 20  ? 7.211  -5.949  27.711  1.00 28.97 ? 20  LYS A C   1 
ATOM   157  O O   . LYS A 1 20  ? 6.082  -5.685  27.309  1.00 30.57 ? 20  LYS A O   1 
ATOM   158  C CB  . LYS A 1 20  ? 7.982  -5.113  29.956  1.00 32.29 ? 20  LYS A CB  1 
ATOM   159  C CG  . LYS A 1 20  ? 7.168  -3.834  29.788  1.00 34.65 ? 20  LYS A CG  1 
ATOM   160  C CD  . LYS A 1 20  ? 7.773  -2.642  30.469  1.00 37.71 ? 20  LYS A CD  1 
ATOM   161  C CE  . LYS A 1 20  ? 7.276  -1.335  29.900  1.00 40.52 ? 20  LYS A CE  1 
ATOM   162  N NZ  . LYS A 1 20  ? 8.007  -0.199  30.497  1.00 40.60 ? 20  LYS A NZ  1 
ATOM   163  N N   . PHE A 1 21  ? 8.283  -5.849  26.929  1.00 26.09 ? 21  PHE A N   1 
ATOM   164  C CA  . PHE A 1 21  ? 8.177  -5.484  25.526  1.00 26.13 ? 21  PHE A CA  1 
ATOM   165  C C   . PHE A 1 21  ? 7.372  -6.523  24.740  1.00 26.77 ? 21  PHE A C   1 
ATOM   166  O O   . PHE A 1 21  ? 6.511  -6.172  23.935  1.00 24.66 ? 21  PHE A O   1 
ATOM   167  C CB  . PHE A 1 21  ? 9.579  -5.328  24.935  1.00 25.77 ? 21  PHE A CB  1 
ATOM   168  C CG  . PHE A 1 21  ? 9.594  -4.961  23.478  1.00 28.43 ? 21  PHE A CG  1 
ATOM   169  C CD1 . PHE A 1 21  ? 9.452  -5.932  22.493  1.00 28.30 ? 21  PHE A CD1 1 
ATOM   170  C CD2 . PHE A 1 21  ? 9.706  -3.633  23.096  1.00 30.60 ? 21  PHE A CD2 1 
ATOM   171  C CE1 . PHE A 1 21  ? 9.460  -5.574  21.152  1.00 31.78 ? 21  PHE A CE1 1 
ATOM   172  C CE2 . PHE A 1 21  ? 9.715  -3.285  21.758  1.00 30.05 ? 21  PHE A CE2 1 
ATOM   173  C CZ  . PHE A 1 21  ? 9.580  -4.251  20.790  1.00 31.34 ? 21  PHE A CZ  1 
ATOM   174  N N   . GLN A 1 22  ? 7.671  -7.808  24.961  1.00 27.83 ? 22  GLN A N   1 
ATOM   175  C CA  . GLN A 1 22  ? 7.030  -8.864  24.193  1.00 30.61 ? 22  GLN A CA  1 
ATOM   176  C C   . GLN A 1 22  ? 5.552  -8.938  24.569  1.00 32.89 ? 22  GLN A C   1 
ATOM   177  O O   . GLN A 1 22  ? 4.709  -9.185  23.707  1.00 35.95 ? 22  GLN A O   1 
ATOM   178  C CB  . GLN A 1 22  ? 7.762  -10.195 24.388  1.00 31.07 ? 22  GLN A CB  1 
ATOM   179  C CG  . GLN A 1 22  ? 9.108  -10.241 23.679  1.00 30.28 ? 22  GLN A CG  1 
ATOM   180  C CD  . GLN A 1 22  ? 8.976  -10.215 22.173  1.00 31.27 ? 22  GLN A CD  1 
ATOM   181  O OE1 . GLN A 1 22  ? 7.932  -10.542 21.613  1.00 31.99 ? 22  GLN A OE1 1 
ATOM   182  N NE2 . GLN A 1 22  ? 10.044 -9.821  21.499  1.00 30.94 ? 22  GLN A NE2 1 
ATOM   183  N N   . SER A 1 23  ? 5.250  -8.699  25.851  1.00 30.66 ? 23  SER A N   1 
ATOM   184  C CA  . SER A 1 23  ? 3.877  -8.671  26.326  1.00 32.53 ? 23  SER A CA  1 
ATOM   185  C C   . SER A 1 23  ? 3.109  -7.539  25.652  1.00 30.98 ? 23  SER A C   1 
ATOM   186  O O   . SER A 1 23  ? 1.992  -7.745  25.198  1.00 31.93 ? 23  SER A O   1 
ATOM   187  C CB  . SER A 1 23  ? 3.811  -8.545  27.824  1.00 35.41 ? 23  SER A CB  1 
ATOM   188  O OG  . SER A 1 23  ? 2.460  -8.449  28.250  1.00 41.97 ? 23  SER A OG  1 
ATOM   189  N N   . GLU A 1 24  ? 3.725  -6.351  25.589  1.00 31.15 ? 24  GLU A N   1 
ATOM   190  C CA  . GLU A 1 24  ? 3.108  -5.201  24.950  1.00 32.06 ? 24  GLU A CA  1 
ATOM   191  C C   . GLU A 1 24  ? 2.908  -5.444  23.455  1.00 33.54 ? 24  GLU A C   1 
ATOM   192  O O   . GLU A 1 24  ? 1.875  -5.082  22.896  1.00 36.03 ? 24  GLU A O   1 
ATOM   193  C CB  . GLU A 1 24  ? 3.976  -3.962  25.176  1.00 34.80 ? 24  GLU A CB  1 
ATOM   194  C CG  . GLU A 1 24  ? 3.202  -2.724  25.523  1.00 39.61 ? 24  GLU A CG  1 
ATOM   195  C CD  . GLU A 1 24  ? 4.070  -1.495  25.734  1.00 40.16 ? 24  GLU A CD  1 
ATOM   196  O OE1 . GLU A 1 24  ? 4.761  -1.445  26.765  1.00 39.07 ? 24  GLU A OE1 1 
ATOM   197  O OE2 . GLU A 1 24  ? 4.048  -0.589  24.868  1.00 43.32 ? 24  GLU A OE2 1 
ATOM   198  N N   . LYS A 1 25  ? 3.893  -6.074  22.802  1.00 33.50 ? 25  LYS A N   1 
ATOM   199  C CA  . LYS A 1 25  ? 3.821  -6.287  21.370  1.00 36.55 ? 25  LYS A CA  1 
ATOM   200  C C   . LYS A 1 25  ? 2.707  -7.288  21.080  1.00 37.21 ? 25  LYS A C   1 
ATOM   201  O O   . LYS A 1 25  ? 1.953  -7.107  20.127  1.00 35.23 ? 25  LYS A O   1 
ATOM   202  C CB  . LYS A 1 25  ? 5.145  -6.832  20.823  1.00 39.13 ? 25  LYS A CB  1 
ATOM   203  C CG  . LYS A 1 25  ? 5.077  -7.354  19.394  1.00 43.27 ? 25  LYS A CG  1 
ATOM   204  C CD  . LYS A 1 25  ? 6.351  -8.008  18.890  1.00 47.77 ? 25  LYS A CD  1 
ATOM   205  C CE  . LYS A 1 25  ? 6.070  -9.232  18.039  1.00 52.24 ? 25  LYS A CE  1 
ATOM   206  N NZ  . LYS A 1 25  ? 6.973  -9.327  16.868  1.00 55.42 ? 25  LYS A NZ  1 
ATOM   207  N N   . ALA A 1 26  ? 2.634  -8.325  21.930  1.00 38.36 ? 26  ALA A N   1 
ATOM   208  C CA  . ALA A 1 26  ? 1.657  -9.402  21.812  1.00 38.74 ? 26  ALA A CA  1 
ATOM   209  C C   . ALA A 1 26  ? 0.243  -8.858  22.010  1.00 40.00 ? 26  ALA A C   1 
ATOM   210  O O   . ALA A 1 26  ? -0.711 -9.381  21.435  1.00 42.21 ? 26  ALA A O   1 
ATOM   211  C CB  . ALA A 1 26  ? 1.955  -10.481 22.827  1.00 40.89 ? 26  ALA A CB  1 
ATOM   212  N N   . ALA A 1 27  ? 0.122  -7.847  22.875  1.00 39.15 ? 27  ALA A N   1 
ATOM   213  C CA  . ALA A 1 27  ? -1.143 -7.163  23.110  1.00 40.15 ? 27  ALA A CA  1 
ATOM   214  C C   . ALA A 1 27  ? -1.471 -6.163  21.998  1.00 42.16 ? 27  ALA A C   1 
ATOM   215  O O   . ALA A 1 27  ? -2.571 -5.628  21.990  1.00 45.16 ? 27  ALA A O   1 
ATOM   216  C CB  . ALA A 1 27  ? -1.112 -6.480  24.453  1.00 42.52 ? 27  ALA A CB  1 
ATOM   217  N N   . GLY A 1 28  ? -0.525 -5.869  21.096  1.00 42.69 ? 28  GLY A N   1 
ATOM   218  C CA  . GLY A 1 28  ? -0.790 -4.996  19.956  1.00 45.75 ? 28  GLY A CA  1 
ATOM   219  C C   . GLY A 1 28  ? -0.552 -3.514  20.255  1.00 49.21 ? 28  GLY A C   1 
ATOM   220  O O   . GLY A 1 28  ? -1.181 -2.642  19.648  1.00 51.47 ? 28  GLY A O   1 
ATOM   221  N N   . SER A 1 29  ? 0.370  -3.209  21.172  1.00 54.17 ? 29  SER A N   1 
ATOM   222  C CA  . SER A 1 29  ? 0.493  -1.834  21.635  1.00 58.22 ? 29  SER A CA  1 
ATOM   223  C C   . SER A 1 29  ? 1.917  -1.489  22.059  1.00 57.36 ? 29  SER A C   1 
ATOM   224  O O   . SER A 1 29  ? 2.158  -1.385  23.255  1.00 63.63 ? 29  SER A O   1 
ATOM   225  C CB  . SER A 1 29  ? -0.473 -1.608  22.777  1.00 61.58 ? 29  SER A CB  1 
ATOM   226  O OG  . SER A 1 29  ? -0.197 -2.494  23.857  1.00 65.47 ? 29  SER A OG  1 
ATOM   227  N N   . VAL A 1 30  ? 2.836  -1.236  21.111  1.00 53.05 ? 30  VAL A N   1 
ATOM   228  C CA  . VAL A 1 30  ? 4.164  -0.765  21.499  1.00 50.95 ? 30  VAL A CA  1 
ATOM   229  C C   . VAL A 1 30  ? 4.184  0.767   21.539  1.00 43.83 ? 30  VAL A C   1 
ATOM   230  O O   . VAL A 1 30  ? 4.285  1.454   20.520  1.00 41.61 ? 30  VAL A O   1 
ATOM   231  C CB  . VAL A 1 30  ? 5.310  -1.318  20.633  1.00 53.95 ? 30  VAL A CB  1 
ATOM   232  C CG1 . VAL A 1 30  ? 6.658  -0.812  21.132  1.00 52.44 ? 30  VAL A CG1 1 
ATOM   233  C CG2 . VAL A 1 30  ? 5.310  -2.836  20.592  1.00 55.72 ? 30  VAL A CG2 1 
ATOM   234  N N   . SER A 1 31  ? 4.157  1.277   22.769  1.00 37.20 ? 31  SER A N   1 
ATOM   235  C CA  . SER A 1 31  ? 4.066  2.693   23.058  1.00 35.01 ? 31  SER A CA  1 
ATOM   236  C C   . SER A 1 31  ? 5.360  3.447   22.721  1.00 33.29 ? 31  SER A C   1 
ATOM   237  O O   . SER A 1 31  ? 6.430  2.855   22.562  1.00 32.71 ? 31  SER A O   1 
ATOM   238  C CB  . SER A 1 31  ? 3.714  2.847   24.510  1.00 34.50 ? 31  SER A CB  1 
ATOM   239  O OG  . SER A 1 31  ? 4.823  2.519   25.325  1.00 34.65 ? 31  SER A OG  1 
ATOM   240  N N   . LYS A 1 32  ? 5.258  4.784   22.671  1.00 32.21 ? 32  LYS A N   1 
ATOM   241  C CA  . LYS A 1 32  ? 6.415  5.650   22.483  1.00 33.33 ? 32  LYS A CA  1 
ATOM   242  C C   . LYS A 1 32  ? 7.410  5.447   23.625  1.00 30.02 ? 32  LYS A C   1 
ATOM   243  O O   . LYS A 1 32  ? 8.617  5.457   23.402  1.00 28.05 ? 32  LYS A O   1 
ATOM   244  C CB  . LYS A 1 32  ? 6.014  7.130   22.437  1.00 37.60 ? 32  LYS A CB  1 
ATOM   245  C CG  . LYS A 1 32  ? 5.124  7.544   21.272  1.00 42.51 ? 32  LYS A CG  1 
ATOM   246  C CD  . LYS A 1 32  ? 4.372  8.843   21.537  1.00 45.61 ? 32  LYS A CD  1 
ATOM   247  C CE  . LYS A 1 32  ? 4.858  10.026  20.732  1.00 47.85 ? 32  LYS A CE  1 
ATOM   248  N NZ  . LYS A 1 32  ? 4.930  11.261  21.551  1.00 46.65 ? 32  LYS A NZ  1 
ATOM   249  N N   . SER A 1 33  ? 6.889  5.298   24.847  1.00 27.46 ? 33  SER A N   1 
ATOM   250  C CA  . SER A 1 33  ? 7.715  5.098   26.026  1.00 29.42 ? 33  SER A CA  1 
ATOM   251  C C   . SER A 1 33  ? 8.518  3.803   25.924  1.00 26.75 ? 33  SER A C   1 
ATOM   252  O O   . SER A 1 33  ? 9.718  3.794   26.176  1.00 25.86 ? 33  SER A O   1 
ATOM   253  C CB  . SER A 1 33  ? 6.864  5.089   27.268  1.00 32.38 ? 33  SER A CB  1 
ATOM   254  O OG  . SER A 1 33  ? 7.642  4.755   28.412  1.00 39.19 ? 33  SER A OG  1 
ATOM   255  N N   . THR A 1 34  ? 7.836  2.706   25.566  1.00 27.05 ? 34  THR A N   1 
ATOM   256  C CA  . THR A 1 34  ? 8.486  1.408   25.493  1.00 25.64 ? 34  THR A CA  1 
ATOM   257  C C   . THR A 1 34  ? 9.466  1.396   24.317  1.00 23.61 ? 34  THR A C   1 
ATOM   258  O O   . THR A 1 34  ? 10.530 0.805   24.432  1.00 23.28 ? 34  THR A O   1 
ATOM   259  C CB  . THR A 1 34  ? 7.458  0.269   25.426  1.00 26.64 ? 34  THR A CB  1 
ATOM   260  O OG1 . THR A 1 34  ? 6.716  0.260   26.650  1.00 30.87 ? 34  THR A OG1 1 
ATOM   261  C CG2 . THR A 1 34  ? 8.093  -1.086  25.198  1.00 25.83 ? 34  THR A CG2 1 
ATOM   262  N N   . GLN A 1 35  ? 9.128  2.074   23.202  1.00 23.87 ? 35  GLN A N   1 
ATOM   263  C CA  . GLN A 1 35  ? 10.046 2.179   22.072  1.00 22.98 ? 35  GLN A CA  1 
ATOM   264  C C   . GLN A 1 35  ? 11.296 2.964   22.459  1.00 21.61 ? 35  GLN A C   1 
ATOM   265  O O   . GLN A 1 35  ? 12.392 2.646   22.021  1.00 21.96 ? 35  GLN A O   1 
ATOM   266  C CB  . GLN A 1 35  ? 9.398  2.839   20.855  1.00 27.42 ? 35  GLN A CB  1 
ATOM   267  C CG  . GLN A 1 35  ? 8.500  1.891   20.081  1.00 33.37 ? 35  GLN A CG  1 
ATOM   268  C CD  . GLN A 1 35  ? 8.101  2.544   18.786  1.00 40.49 ? 35  GLN A CD  1 
ATOM   269  O OE1 . GLN A 1 35  ? 7.243  3.425   18.765  1.00 44.70 ? 35  GLN A OE1 1 
ATOM   270  N NE2 . GLN A 1 35  ? 8.760  2.143   17.710  1.00 43.22 ? 35  GLN A NE2 1 
ATOM   271  N N   . PHE A 1 36  ? 11.124 4.020   23.265  1.00 21.33 ? 36  PHE A N   1 
ATOM   272  C CA  . PHE A 1 36  ? 12.283 4.765   23.738  1.00 18.84 ? 36  PHE A CA  1 
ATOM   273  C C   . PHE A 1 36  ? 13.160 3.861   24.607  1.00 18.76 ? 36  PHE A C   1 
ATOM   274  O O   . PHE A 1 36  ? 14.368 3.851   24.451  1.00 18.41 ? 36  PHE A O   1 
ATOM   275  C CB  . PHE A 1 36  ? 11.880 5.990   24.555  1.00 19.47 ? 36  PHE A CB  1 
ATOM   276  C CG  . PHE A 1 36  ? 13.070 6.688   25.160  1.00 20.64 ? 36  PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 36  ? 13.920 7.440   24.372  1.00 19.11 ? 36  PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 36  ? 13.399 6.501   26.492  1.00 23.13 ? 36  PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 36  ? 15.045 8.035   24.916  1.00 21.17 ? 36  PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 36  ? 14.541 7.071   27.027  1.00 23.54 ? 36  PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 36  ? 15.350 7.853   26.242  1.00 22.38 ? 36  PHE A CZ  1 
ATOM   282  N N   . GLU A 1 37  ? 12.542 3.124   25.538  1.00 20.05 ? 37  GLU A N   1 
ATOM   283  C CA  . GLU A 1 37  ? 13.295 2.231   26.409  1.00 20.54 ? 37  GLU A CA  1 
ATOM   284  C C   . GLU A 1 37  ? 14.020 1.157   25.578  1.00 19.81 ? 37  GLU A C   1 
ATOM   285  O O   . GLU A 1 37  ? 15.153 0.798   25.876  1.00 19.63 ? 37  GLU A O   1 
ATOM   286  C CB  . GLU A 1 37  ? 12.354 1.633   27.450  1.00 24.64 ? 37  GLU A CB  1 
ATOM   287  C CG  . GLU A 1 37  ? 11.815 2.653   28.437  1.00 28.62 ? 37  GLU A CG  1 
ATOM   288  C CD  . GLU A 1 37  ? 10.580 2.236   29.217  1.00 34.57 ? 37  GLU A CD  1 
ATOM   289  O OE1 . GLU A 1 37  ? 10.136 1.092   29.037  1.00 36.45 ? 37  GLU A OE1 1 
ATOM   290  O OE2 . GLU A 1 37  ? 10.044 3.082   29.978  1.00 39.69 ? 37  GLU A OE2 1 
ATOM   291  N N   . GLU A 1 38  ? 13.390 0.690   24.497  1.00 19.15 ? 38  GLU A N   1 
ATOM   292  C CA  . GLU A 1 38  ? 14.035 -0.232  23.573  1.00 19.50 ? 38  GLU A CA  1 
ATOM   293  C C   . GLU A 1 38  ? 15.279 0.414   22.968  1.00 19.13 ? 38  GLU A C   1 
ATOM   294  O O   . GLU A 1 38  ? 16.344 -0.190  22.918  1.00 19.45 ? 38  GLU A O   1 
ATOM   295  C CB  . GLU A 1 38  ? 13.037 -0.634  22.492  1.00 23.12 ? 38  GLU A CB  1 
ATOM   296  C CG  . GLU A 1 38  ? 13.550 -1.642  21.479  1.00 24.77 ? 38  GLU A CG  1 
ATOM   297  C CD  . GLU A 1 38  ? 12.654 -1.823  20.262  1.00 24.70 ? 38  GLU A CD  1 
ATOM   298  O OE1 . GLU A 1 38  ? 11.565 -1.197  20.220  1.00 30.17 ? 38  GLU A OE1 1 
ATOM   299  O OE2 . GLU A 1 38  ? 13.066 -2.548  19.328  1.00 29.29 ? 38  GLU A OE2 1 
ATOM   300  N N   . ALA A 1 39  ? 15.132 1.653   22.479  1.00 18.46 ? 39  ALA A N   1 
ATOM   301  C CA  . ALA A 1 39  ? 16.249 2.378   21.899  1.00 18.88 ? 39  ALA A CA  1 
ATOM   302  C C   . ALA A 1 39  ? 17.354 2.608   22.938  1.00 18.14 ? 39  ALA A C   1 
ATOM   303  O O   . ALA A 1 39  ? 18.539 2.529   22.628  1.00 18.83 ? 39  ALA A O   1 
ATOM   304  C CB  . ALA A 1 39  ? 15.770 3.694   21.332  1.00 20.10 ? 39  ALA A CB  1 
ATOM   305  N N   . TRP A 1 40  ? 16.958 2.932   24.167  1.00 18.85 ? 40  TRP A N   1 
ATOM   306  C CA  . TRP A 1 40  ? 17.871 3.176   25.273  1.00 19.64 ? 40  TRP A CA  1 
ATOM   307  C C   . TRP A 1 40  ? 18.749 1.949   25.526  1.00 20.50 ? 40  TRP A C   1 
ATOM   308  O O   . TRP A 1 40  ? 19.943 2.057   25.795  1.00 20.16 ? 40  TRP A O   1 
ATOM   309  C CB  . TRP A 1 40  ? 17.023 3.577   26.483  1.00 20.76 ? 40  TRP A CB  1 
ATOM   310  C CG  . TRP A 1 40  ? 17.756 3.855   27.757  1.00 21.73 ? 40  TRP A CG  1 
ATOM   311  C CD1 . TRP A 1 40  ? 18.056 5.079   28.275  1.00 22.46 ? 40  TRP A CD1 1 
ATOM   312  C CD2 . TRP A 1 40  ? 18.182 2.893   28.737  1.00 22.06 ? 40  TRP A CD2 1 
ATOM   313  N NE1 . TRP A 1 40  ? 18.677 4.944   29.483  1.00 23.14 ? 40  TRP A NE1 1 
ATOM   314  C CE2 . TRP A 1 40  ? 18.761 3.615   29.802  1.00 23.42 ? 40  TRP A CE2 1 
ATOM   315  C CE3 . TRP A 1 40  ? 18.156 1.497   28.806  1.00 23.33 ? 40  TRP A CE3 1 
ATOM   316  C CZ2 . TRP A 1 40  ? 19.318 2.993   30.914  1.00 23.83 ? 40  TRP A CZ2 1 
ATOM   317  C CZ3 . TRP A 1 40  ? 18.684 0.885   29.918  1.00 24.42 ? 40  TRP A CZ3 1 
ATOM   318  C CH2 . TRP A 1 40  ? 19.256 1.622   30.957  1.00 25.21 ? 40  TRP A CH2 1 
ATOM   319  N N   A CYS A 1 41  ? 18.135 0.762   25.454  0.50 18.76 ? 41  CYS A N   1 
ATOM   320  N N   B CYS A 1 41  ? 18.122 0.787   25.410  0.50 19.68 ? 41  CYS A N   1 
ATOM   321  C CA  A CYS A 1 41  ? 18.877 -0.488  25.550  0.50 19.03 ? 41  CYS A CA  1 
ATOM   322  C CA  B CYS A 1 41  ? 18.815 -0.475  25.547  0.50 20.88 ? 41  CYS A CA  1 
ATOM   323  C C   A CYS A 1 41  ? 19.814 -0.632  24.352  0.50 18.65 ? 41  CYS A C   1 
ATOM   324  C C   B CYS A 1 41  ? 19.763 -0.696  24.366  0.50 19.69 ? 41  CYS A C   1 
ATOM   325  O O   A CYS A 1 41  ? 20.997 -0.937  24.503  0.50 20.08 ? 41  CYS A O   1 
ATOM   326  O O   B CYS A 1 41  ? 20.913 -1.100  24.545  0.50 20.76 ? 41  CYS A O   1 
ATOM   327  C CB  A CYS A 1 41  ? 17.957 -1.711  25.588  0.50 20.16 ? 41  CYS A CB  1 
ATOM   328  C CB  B CYS A 1 41  ? 17.767 -1.575  25.663  0.50 23.53 ? 41  CYS A CB  1 
ATOM   329  S SG  A CYS A 1 41  ? 16.903 -1.826  27.057  0.50 20.25 ? 41  CYS A SG  1 
ATOM   330  S SG  B CYS A 1 41  ? 18.490 -3.213  25.858  0.50 28.62 ? 41  CYS A SG  1 
ATOM   331  N N   . LEU A 1 42  ? 19.266 -0.458  23.150  1.00 18.82 ? 42  LEU A N   1 
ATOM   332  C CA  . LEU A 1 42  ? 20.008 -0.755  21.927  1.00 18.98 ? 42  LEU A CA  1 
ATOM   333  C C   . LEU A 1 42  ? 21.249 0.130   21.784  1.00 19.16 ? 42  LEU A C   1 
ATOM   334  O O   . LEU A 1 42  ? 22.290 -0.352  21.356  1.00 19.57 ? 42  LEU A O   1 
ATOM   335  C CB  . LEU A 1 42  ? 19.078 -0.597  20.724  1.00 20.09 ? 42  LEU A CB  1 
ATOM   336  C CG  . LEU A 1 42  ? 18.047 -1.706  20.535  1.00 20.52 ? 42  LEU A CG  1 
ATOM   337  C CD1 . LEU A 1 42  ? 16.982 -1.294  19.540  1.00 22.20 ? 42  LEU A CD1 1 
ATOM   338  C CD2 . LEU A 1 42  ? 18.738 -2.982  20.088  1.00 22.02 ? 42  LEU A CD2 1 
ATOM   339  N N   . VAL A 1 43  ? 21.168 1.411   22.153  1.00 20.54 ? 43  VAL A N   1 
ATOM   340  C CA  . VAL A 1 43  ? 22.316 2.283   21.938  1.00 20.51 ? 43  VAL A CA  1 
ATOM   341  C C   . VAL A 1 43  ? 23.414 2.014   22.970  1.00 19.76 ? 43  VAL A C   1 
ATOM   342  O O   . VAL A 1 43  ? 24.495 2.587   22.845  1.00 21.24 ? 43  VAL A O   1 
ATOM   343  C CB  . VAL A 1 43  ? 21.940 3.780   21.915  1.00 22.28 ? 43  VAL A CB  1 
ATOM   344  C CG1 . VAL A 1 43  ? 20.998 4.102   20.769  1.00 22.01 ? 43  VAL A CG1 1 
ATOM   345  C CG2 . VAL A 1 43  ? 21.387 4.273   23.241  1.00 22.76 ? 43  VAL A CG2 1 
ATOM   346  N N   . ARG A 1 44  ? 23.143 1.157   23.969  1.00 22.23 ? 44  ARG A N   1 
ATOM   347  C CA  . ARG A 1 44  ? 24.141 0.700   24.930  1.00 22.97 ? 44  ARG A CA  1 
ATOM   348  C C   . ARG A 1 44  ? 24.782 -0.643  24.561  1.00 22.50 ? 44  ARG A C   1 
ATOM   349  O O   . ARG A 1 44  ? 25.608 -1.160  25.323  1.00 24.18 ? 44  ARG A O   1 
ATOM   350  C CB  . ARG A 1 44  ? 23.488 0.556   26.302  1.00 23.98 ? 44  ARG A CB  1 
ATOM   351  C CG  . ARG A 1 44  ? 23.135 1.876   26.959  1.00 25.40 ? 44  ARG A CG  1 
ATOM   352  C CD  . ARG A 1 44  ? 22.335 1.672   28.228  1.00 25.28 ? 44  ARG A CD  1 
ATOM   353  N NE  . ARG A 1 44  ? 22.379 2.842   29.086  1.00 25.48 ? 44  ARG A NE  1 
ATOM   354  C CZ  . ARG A 1 44  ? 21.807 4.009   28.817  1.00 25.64 ? 44  ARG A CZ  1 
ATOM   355  N NH1 . ARG A 1 44  ? 21.088 4.158   27.713  1.00 27.25 ? 44  ARG A NH1 1 
ATOM   356  N NH2 . ARG A 1 44  ? 21.956 5.016   29.667  1.00 26.38 ? 44  ARG A NH2 1 
ATOM   357  N N   . SER A 1 45  ? 24.368 -1.224  23.434  1.00 20.28 ? 45  SER A N   1 
ATOM   358  C CA  . SER A 1 45  ? 24.845 -2.526  23.011  1.00 20.65 ? 45  SER A CA  1 
ATOM   359  C C   . SER A 1 45  ? 26.332 -2.504  22.675  1.00 21.06 ? 45  SER A C   1 
ATOM   360  O O   . SER A 1 45  ? 26.866 -1.494  22.221  1.00 23.17 ? 45  SER A O   1 
ATOM   361  C CB  . SER A 1 45  ? 24.050 -3.015  21.848  1.00 20.58 ? 45  SER A CB  1 
ATOM   362  O OG  . SER A 1 45  ? 24.439 -4.332  21.482  1.00 21.16 ? 45  SER A OG  1 
ATOM   363  N N   . LYS A 1 46  ? 26.983 -3.659  22.843  1.00 23.18 ? 46  LYS A N   1 
ATOM   364  C CA  . LYS A 1 46  ? 28.324 -3.862  22.316  1.00 25.87 ? 46  LYS A CA  1 
ATOM   365  C C   . LYS A 1 46  ? 28.318 -4.046  20.791  1.00 23.29 ? 46  LYS A C   1 
ATOM   366  O O   . LYS A 1 46  ? 29.379 -3.942  20.179  1.00 27.08 ? 46  LYS A O   1 
ATOM   367  C CB  . LYS A 1 46  ? 28.965 -5.071  23.008  1.00 30.80 ? 46  LYS A CB  1 
ATOM   368  C CG  . LYS A 1 46  ? 28.202 -6.375  22.870  1.00 35.31 ? 46  LYS A CG  1 
ATOM   369  C CD  . LYS A 1 46  ? 28.732 -7.477  23.778  1.00 40.38 ? 46  LYS A CD  1 
ATOM   370  C CE  . LYS A 1 46  ? 27.793 -8.659  23.893  1.00 46.01 ? 46  LYS A CE  1 
ATOM   371  N NZ  . LYS A 1 46  ? 28.218 -9.603  24.953  1.00 50.11 ? 46  LYS A NZ  1 
ATOM   372  N N   . TYR A 1 47  ? 27.145 -4.275  20.174  1.00 20.64 ? 47  TYR A N   1 
ATOM   373  C CA  . TYR A 1 47  ? 27.048 -4.548  18.746  1.00 20.56 ? 47  TYR A CA  1 
ATOM   374  C C   . TYR A 1 47  ? 26.571 -3.323  17.968  1.00 19.74 ? 47  TYR A C   1 
ATOM   375  O O   . TYR A 1 47  ? 25.512 -2.768  18.250  1.00 19.93 ? 47  TYR A O   1 
ATOM   376  C CB  . TYR A 1 47  ? 26.073 -5.696  18.479  1.00 21.43 ? 47  TYR A CB  1 
ATOM   377  C CG  . TYR A 1 47  ? 26.541 -7.019  19.028  1.00 21.51 ? 47  TYR A CG  1 
ATOM   378  C CD1 . TYR A 1 47  ? 27.515 -7.752  18.383  1.00 24.36 ? 47  TYR A CD1 1 
ATOM   379  C CD2 . TYR A 1 47  ? 26.030 -7.515  20.214  1.00 23.04 ? 47  TYR A CD2 1 
ATOM   380  C CE1 . TYR A 1 47  ? 27.980 -8.947  18.900  1.00 25.13 ? 47  TYR A CE1 1 
ATOM   381  C CE2 . TYR A 1 47  ? 26.464 -8.722  20.736  1.00 24.72 ? 47  TYR A CE2 1 
ATOM   382  C CZ  . TYR A 1 47  ? 27.436 -9.447  20.072  1.00 25.02 ? 47  TYR A CZ  1 
ATOM   383  O OH  . TYR A 1 47  ? 27.879 -10.646 20.591  1.00 27.47 ? 47  TYR A OH  1 
ATOM   384  N N   . ASN A 1 48  ? 27.335 -2.964  16.938  1.00 22.29 ? 48  ASN A N   1 
ATOM   385  C CA  . ASN A 1 48  ? 27.021 -1.805  16.121  1.00 22.46 ? 48  ASN A CA  1 
ATOM   386  C C   . ASN A 1 48  ? 25.635 -1.906  15.488  1.00 22.09 ? 48  ASN A C   1 
ATOM   387  O O   . ASN A 1 48  ? 24.937 -0.901  15.388  1.00 21.18 ? 48  ASN A O   1 
ATOM   388  C CB  . ASN A 1 48  ? 28.076 -1.559  15.043  1.00 24.44 ? 48  ASN A CB  1 
ATOM   389  C CG  . ASN A 1 48  ? 29.401 -1.121  15.621  1.00 28.43 ? 48  ASN A CG  1 
ATOM   390  O OD1 . ASN A 1 48  ? 29.455 -0.603  16.731  1.00 30.13 ? 48  ASN A OD1 1 
ATOM   391  N ND2 . ASN A 1 48  ? 30.470 -1.303  14.867  1.00 33.59 ? 48  ASN A ND2 1 
ATOM   392  N N   . ASP A 1 49  ? 25.204 -3.103  15.080  1.00 22.55 ? 49  ASP A N   1 
ATOM   393  C CA  . ASP A 1 49  ? 23.905 -3.234  14.432  1.00 24.50 ? 49  ASP A CA  1 
ATOM   394  C C   . ASP A 1 49  ? 22.787 -2.866  15.407  1.00 22.07 ? 49  ASP A C   1 
ATOM   395  O O   . ASP A 1 49  ? 21.780 -2.291  15.013  1.00 22.98 ? 49  ASP A O   1 
ATOM   396  C CB  . ASP A 1 49  ? 23.713 -4.636  13.859  1.00 28.56 ? 49  ASP A CB  1 
ATOM   397  C CG  . ASP A 1 49  ? 24.517 -4.897  12.601  1.00 35.12 ? 49  ASP A CG  1 
ATOM   398  O OD1 . ASP A 1 49  ? 25.073 -3.923  12.040  1.00 41.08 ? 49  ASP A OD1 1 
ATOM   399  O OD2 . ASP A 1 49  ? 24.574 -6.067  12.196  1.00 42.13 ? 49  ASP A OD2 1 
ATOM   400  N N   . ASP A 1 50  ? 22.963 -3.204  16.683  1.00 20.65 ? 50  ASP A N   1 
ATOM   401  C CA  . ASP A 1 50  ? 22.030 -2.795  17.719  1.00 18.87 ? 50  ASP A CA  1 
ATOM   402  C C   . ASP A 1 50  ? 21.980 -1.268  17.828  1.00 18.81 ? 50  ASP A C   1 
ATOM   403  O O   . ASP A 1 50  ? 20.902 -0.687  17.891  1.00 18.92 ? 50  ASP A O   1 
ATOM   404  C CB  . ASP A 1 50  ? 22.398 -3.414  19.066  1.00 19.14 ? 50  ASP A CB  1 
ATOM   405  C CG  . ASP A 1 50  ? 22.008 -4.876  19.211  1.00 21.56 ? 50  ASP A CG  1 
ATOM   406  O OD1 . ASP A 1 50  ? 21.164 -5.358  18.414  1.00 23.43 ? 50  ASP A OD1 1 
ATOM   407  O OD2 . ASP A 1 50  ? 22.566 -5.520  20.106  1.00 23.11 ? 50  ASP A OD2 1 
ATOM   408  N N   . ILE A 1 51  ? 23.146 -0.625  17.911  1.00 18.05 ? 51  ILE A N   1 
ATOM   409  C CA  . ILE A 1 51  ? 23.170 0.822   18.069  1.00 18.17 ? 51  ILE A CA  1 
ATOM   410  C C   . ILE A 1 51  ? 22.446 1.482   16.897  1.00 18.08 ? 51  ILE A C   1 
ATOM   411  O O   . ILE A 1 51  ? 21.678 2.443   17.081  1.00 18.21 ? 51  ILE A O   1 
ATOM   412  C CB  . ILE A 1 51  ? 24.613 1.345   18.219  1.00 18.62 ? 51  ILE A CB  1 
ATOM   413  C CG1 . ILE A 1 51  ? 25.380 0.629   19.345  1.00 18.68 ? 51  ILE A CG1 1 
ATOM   414  C CG2 . ILE A 1 51  ? 24.596 2.863   18.379  1.00 19.05 ? 51  ILE A CG2 1 
ATOM   415  C CD1 . ILE A 1 51  ? 26.851 0.999   19.431  1.00 20.11 ? 51  ILE A CD1 1 
ATOM   416  N N   A ARG A 1 52  ? 22.688 0.981   15.683  0.50 17.99 ? 52  ARG A N   1 
ATOM   417  N N   B ARG A 1 52  ? 22.711 0.981   15.686  0.50 18.19 ? 52  ARG A N   1 
ATOM   418  C CA  A ARG A 1 52  ? 22.065 1.552   14.503  0.50 19.28 ? 52  ARG A CA  1 
ATOM   419  C CA  B ARG A 1 52  ? 22.086 1.499   14.482  0.50 19.62 ? 52  ARG A CA  1 
ATOM   420  C C   A ARG A 1 52  ? 20.549 1.371   14.552  0.50 19.22 ? 52  ARG A C   1 
ATOM   421  C C   B ARG A 1 52  ? 20.566 1.371   14.568  0.50 19.38 ? 52  ARG A C   1 
ATOM   422  O O   A ARG A 1 52  ? 19.815 2.241   14.095  0.50 19.77 ? 52  ARG A O   1 
ATOM   423  O O   B ARG A 1 52  ? 19.848 2.275   14.154  0.50 19.83 ? 52  ARG A O   1 
ATOM   424  C CB  A ARG A 1 52  ? 22.666 0.955   13.230  0.50 20.12 ? 52  ARG A CB  1 
ATOM   425  C CB  B ARG A 1 52  ? 22.627 0.779   13.245  0.50 20.84 ? 52  ARG A CB  1 
ATOM   426  C CG  A ARG A 1 52  ? 24.121 1.346   13.009  0.50 20.92 ? 52  ARG A CG  1 
ATOM   427  C CG  B ARG A 1 52  ? 24.075 1.113   12.912  0.50 22.50 ? 52  ARG A CG  1 
ATOM   428  C CD  A ARG A 1 52  ? 24.544 1.337   11.554  0.50 22.05 ? 52  ARG A CD  1 
ATOM   429  C CD  B ARG A 1 52  ? 24.612 0.287   11.758  0.50 24.82 ? 52  ARG A CD  1 
ATOM   430  N NE  A ARG A 1 52  ? 25.991 1.460   11.463  0.50 25.87 ? 52  ARG A NE  1 
ATOM   431  N NE  B ARG A 1 52  ? 26.039 0.496   11.577  0.50 27.08 ? 52  ARG A NE  1 
ATOM   432  C CZ  A ARG A 1 52  ? 26.651 2.591   11.267  0.50 26.21 ? 52  ARG A CZ  1 
ATOM   433  C CZ  B ARG A 1 52  ? 26.964 -0.447  11.681  0.50 29.70 ? 52  ARG A CZ  1 
ATOM   434  N NH1 A ARG A 1 52  ? 26.002 3.732   11.114  0.50 27.62 ? 52  ARG A NH1 1 
ATOM   435  N NH1 B ARG A 1 52  ? 26.614 -1.718  11.786  0.50 29.72 ? 52  ARG A NH1 1 
ATOM   436  N NH2 A ARG A 1 52  ? 27.971 2.572   11.235  0.50 27.71 ? 52  ARG A NH2 1 
ATOM   437  N NH2 B ARG A 1 52  ? 28.240 -0.107  11.650  0.50 33.42 ? 52  ARG A NH2 1 
ATOM   438  N N   . LYS A 1 53  ? 20.075 0.231   15.075  1.00 19.72 ? 53  LYS A N   1 
ATOM   439  C CA  . LYS A 1 53  ? 18.646 0.012   15.197  1.00 19.71 ? 53  LYS A CA  1 
ATOM   440  C C   . LYS A 1 53  ? 18.055 1.018   16.183  1.00 18.41 ? 53  LYS A C   1 
ATOM   441  O O   . LYS A 1 53  ? 16.976 1.548   15.936  1.00 18.77 ? 53  LYS A O   1 
ATOM   442  C CB  . LYS A 1 53  ? 18.346 -1.432  15.618  1.00 21.54 ? 53  LYS A CB  1 
ATOM   443  C CG  . LYS A 1 53  ? 16.874 -1.751  15.806  1.00 26.58 ? 53  LYS A CG  1 
ATOM   444  C CD  . LYS A 1 53  ? 16.012 -1.513  14.592  1.00 31.03 ? 53  LYS A CD  1 
ATOM   445  C CE  . LYS A 1 53  ? 14.564 -1.876  14.856  1.00 35.50 ? 53  LYS A CE  1 
ATOM   446  N NZ  . LYS A 1 53  ? 13.696 -1.483  13.727  1.00 40.72 ? 53  LYS A NZ  1 
ATOM   447  N N   . GLY A 1 54  ? 18.765 1.277   17.289  1.00 17.78 ? 54  GLY A N   1 
ATOM   448  C CA  . GLY A 1 54  ? 18.315 2.237   18.278  1.00 17.47 ? 54  GLY A CA  1 
ATOM   449  C C   . GLY A 1 54  ? 18.198 3.636   17.670  1.00 18.75 ? 54  GLY A C   1 
ATOM   450  O O   . GLY A 1 54  ? 17.247 4.361   17.945  1.00 18.54 ? 54  GLY A O   1 
ATOM   451  N N   . ILE A 1 55  ? 19.145 3.982   16.798  1.00 18.04 ? 55  ILE A N   1 
ATOM   452  C CA  . ILE A 1 55  ? 19.126 5.268   16.111  1.00 18.82 ? 55  ILE A CA  1 
ATOM   453  C C   . ILE A 1 55  ? 17.897 5.377   15.212  1.00 19.93 ? 55  ILE A C   1 
ATOM   454  O O   . ILE A 1 55  ? 17.224 6.406   15.220  1.00 19.88 ? 55  ILE A O   1 
ATOM   455  C CB  . ILE A 1 55  ? 20.445 5.511   15.359  1.00 19.74 ? 55  ILE A CB  1 
ATOM   456  C CG1 . ILE A 1 55  ? 21.566 5.823   16.353  1.00 20.53 ? 55  ILE A CG1 1 
ATOM   457  C CG2 . ILE A 1 55  ? 20.294 6.610   14.332  1.00 19.51 ? 55  ILE A CG2 1 
ATOM   458  C CD1 . ILE A 1 55  ? 22.932 5.773   15.768  1.00 20.67 ? 55  ILE A CD1 1 
ATOM   459  N N   . VAL A 1 56  ? 17.595 4.317   14.450  1.00 20.18 ? 56  VAL A N   1 
ATOM   460  C CA  . VAL A 1 56  ? 16.416 4.300   13.599  1.00 21.36 ? 56  VAL A CA  1 
ATOM   461  C C   . VAL A 1 56  ? 15.159 4.535   14.440  1.00 20.47 ? 56  VAL A C   1 
ATOM   462  O O   . VAL A 1 56  ? 14.329 5.364   14.073  1.00 20.64 ? 56  VAL A O   1 
ATOM   463  C CB  . VAL A 1 56  ? 16.326 3.005   12.763  1.00 24.26 ? 56  VAL A CB  1 
ATOM   464  C CG1 . VAL A 1 56  ? 14.981 2.854   12.069  1.00 25.50 ? 56  VAL A CG1 1 
ATOM   465  C CG2 . VAL A 1 56  ? 17.450 2.939   11.743  1.00 26.28 ? 56  VAL A CG2 1 
ATOM   466  N N   . LEU A 1 57  ? 15.033 3.842   15.581  1.00 19.89 ? 57  LEU A N   1 
ATOM   467  C CA  . LEU A 1 57  ? 13.864 3.989   16.439  1.00 20.21 ? 57  LEU A CA  1 
ATOM   468  C C   . LEU A 1 57  ? 13.748 5.434   16.930  1.00 19.68 ? 57  LEU A C   1 
ATOM   469  O O   . LEU A 1 57  ? 12.651 6.008   16.900  1.00 22.19 ? 57  LEU A O   1 
ATOM   470  C CB  . LEU A 1 57  ? 13.953 3.034   17.633  1.00 21.44 ? 57  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 57  ? 13.867 1.547   17.319  1.00 24.88 ? 57  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 57  ? 14.132 0.756   18.585  1.00 26.26 ? 57  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 57  ? 12.514 1.175   16.731  1.00 27.46 ? 57  LEU A CD2 1 
ATOM   474  N N   . LEU A 1 58  ? 14.877 6.043   17.339  1.00 19.16 ? 58  LEU A N   1 
ATOM   475  C CA  . LEU A 1 58  ? 14.829 7.407   17.866  1.00 19.74 ? 58  LEU A CA  1 
ATOM   476  C C   . LEU A 1 58  ? 14.490 8.410   16.766  1.00 20.66 ? 58  LEU A C   1 
ATOM   477  O O   . LEU A 1 58  ? 13.743 9.366   17.001  1.00 20.58 ? 58  LEU A O   1 
ATOM   478  C CB  . LEU A 1 58  ? 16.162 7.737   18.537  1.00 20.26 ? 58  LEU A CB  1 
ATOM   479  C CG  . LEU A 1 58  ? 16.458 6.981   19.835  1.00 19.60 ? 58  LEU A CG  1 
ATOM   480  C CD1 . LEU A 1 58  ? 17.910 7.127   20.241  1.00 20.35 ? 58  LEU A CD1 1 
ATOM   481  C CD2 . LEU A 1 58  ? 15.558 7.437   20.985  1.00 21.49 ? 58  LEU A CD2 1 
ATOM   482  N N   . GLU A 1 59  ? 15.002 8.200   15.554  1.00 20.67 ? 59  GLU A N   1 
ATOM   483  C CA  . GLU A 1 59  ? 14.677 9.112   14.462  1.00 22.55 ? 59  GLU A CA  1 
ATOM   484  C C   . GLU A 1 59  ? 13.184 9.031   14.120  1.00 23.43 ? 59  GLU A C   1 
ATOM   485  O O   . GLU A 1 59  ? 12.592 10.039  13.696  1.00 24.64 ? 59  GLU A O   1 
ATOM   486  C CB  . GLU A 1 59  ? 15.616 8.860   13.278  1.00 25.70 ? 59  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 59  ? 17.039 9.255   13.627  1.00 27.97 ? 59  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 59  ? 18.110 9.186   12.558  1.00 30.90 ? 59  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 59  ? 18.071 8.254   11.738  1.00 37.11 ? 59  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 59  ? 19.032 10.039  12.614  1.00 34.30 ? 59  GLU A OE2 1 
ATOM   491  N N   . GLU A 1 60  ? 12.571 7.848   14.300  1.00 23.71 ? 60  GLU A N   1 
ATOM   492  C CA  . GLU A 1 60  ? 11.147 7.688   14.053  1.00 26.88 ? 60  GLU A CA  1 
ATOM   493  C C   . GLU A 1 60  ? 10.329 8.422   15.109  1.00 26.06 ? 60  GLU A C   1 
ATOM   494  O O   . GLU A 1 60  ? 9.287  9.000   14.799  1.00 27.94 ? 60  GLU A O   1 
ATOM   495  C CB  . GLU A 1 60  ? 10.744 6.210   14.051  1.00 30.14 ? 60  GLU A CB  1 
ATOM   496  C CG  . GLU A 1 60  ? 11.385 5.406   12.944  1.00 34.51 ? 60  GLU A CG  1 
ATOM   497  C CD  . GLU A 1 60  ? 10.852 3.987   12.823  1.00 40.32 ? 60  GLU A CD  1 
ATOM   498  O OE1 . GLU A 1 60  ? 10.703 3.308   13.867  1.00 44.13 ? 60  GLU A OE1 1 
ATOM   499  O OE2 . GLU A 1 60  ? 10.610 3.558   11.689  1.00 47.03 ? 60  GLU A OE2 1 
ATOM   500  N N   . LEU A 1 61  ? 10.803 8.399   16.356  1.00 25.15 ? 61  LEU A N   1 
ATOM   501  C CA  . LEU A 1 61  ? 10.084 9.023   17.458  1.00 24.53 ? 61  LEU A CA  1 
ATOM   502  C C   . LEU A 1 61  ? 10.211 10.539  17.439  1.00 25.57 ? 61  LEU A C   1 
ATOM   503  O O   . LEU A 1 61  ? 9.312  11.229  17.902  1.00 26.06 ? 61  LEU A O   1 
ATOM   504  C CB  . LEU A 1 61  ? 10.653 8.509   18.778  1.00 24.94 ? 61  LEU A CB  1 
ATOM   505  C CG  . LEU A 1 61  ? 10.336 7.059   19.120  1.00 24.92 ? 61  LEU A CG  1 
ATOM   506  C CD1 . LEU A 1 61  ? 11.185 6.618   20.287  1.00 25.22 ? 61  LEU A CD1 1 
ATOM   507  C CD2 . LEU A 1 61  ? 8.854  6.880   19.434  1.00 26.71 ? 61  LEU A CD2 1 
ATOM   508  N N   A LEU A 1 62  ? 11.333 11.029  16.913  0.50 24.92 ? 62  LEU A N   1 
ATOM   509  N N   B LEU A 1 62  ? 11.333 11.029  16.908  0.50 26.12 ? 62  LEU A N   1 
ATOM   510  C CA  A LEU A 1 62  ? 11.716 12.422  17.081  0.50 26.17 ? 62  LEU A CA  1 
ATOM   511  C CA  B LEU A 1 62  ? 11.732 12.421  17.058  0.50 28.02 ? 62  LEU A CA  1 
ATOM   512  C C   A LEU A 1 62  ? 10.600 13.371  16.629  0.50 28.31 ? 62  LEU A C   1 
ATOM   513  C C   B LEU A 1 62  ? 10.603 13.365  16.629  0.50 29.41 ? 62  LEU A C   1 
ATOM   514  O O   A LEU A 1 62  ? 10.188 14.242  17.402  0.50 28.25 ? 62  LEU A O   1 
ATOM   515  O O   B LEU A 1 62  ? 10.189 14.225  17.414  0.50 28.93 ? 62  LEU A O   1 
ATOM   516  C CB  A LEU A 1 62  ? 13.037 12.655  16.342  0.50 27.08 ? 62  LEU A CB  1 
ATOM   517  C CB  B LEU A 1 62  ? 13.015 12.636  16.248  0.50 30.96 ? 62  LEU A CB  1 
ATOM   518  C CG  A LEU A 1 62  ? 13.608 14.070  16.459  0.50 27.22 ? 62  LEU A CG  1 
ATOM   519  C CG  B LEU A 1 62  ? 14.124 13.427  16.941  0.50 34.31 ? 62  LEU A CG  1 
ATOM   520  C CD1 A LEU A 1 62  ? 13.849 14.441  17.917  0.50 27.88 ? 62  LEU A CD1 1 
ATOM   521  C CD1 B LEU A 1 62  ? 15.039 14.073  15.913  0.50 35.76 ? 62  LEU A CD1 1 
ATOM   522  C CD2 A LEU A 1 62  ? 14.901 14.184  15.666  0.50 29.33 ? 62  LEU A CD2 1 
ATOM   523  C CD2 B LEU A 1 62  ? 13.558 14.475  17.891  0.50 35.07 ? 62  LEU A CD2 1 
ATOM   524  N N   . PRO A 1 63  ? 10.054 13.259  15.393  1.00 28.64 ? 63  PRO A N   1 
ATOM   525  C CA  . PRO A 1 63  ? 8.973  14.158  14.965  1.00 32.39 ? 63  PRO A CA  1 
ATOM   526  C C   . PRO A 1 63  ? 7.650  14.114  15.731  1.00 33.76 ? 63  PRO A C   1 
ATOM   527  O O   . PRO A 1 63  ? 6.851  15.040  15.595  1.00 37.13 ? 63  PRO A O   1 
ATOM   528  C CB  . PRO A 1 63  ? 8.684  13.757  13.509  1.00 35.62 ? 63  PRO A CB  1 
ATOM   529  C CG  . PRO A 1 63  ? 9.400  12.452  13.292  1.00 35.09 ? 63  PRO A CG  1 
ATOM   530  C CD  . PRO A 1 63  ? 10.519 12.391  14.306  1.00 32.14 ? 63  PRO A CD  1 
ATOM   531  N N   . LYS A 1 64  ? 7.424  13.064  16.528  1.00 34.43 ? 64  LYS A N   1 
ATOM   532  C CA  . LYS A 1 64  ? 6.175  12.896  17.256  1.00 35.02 ? 64  LYS A CA  1 
ATOM   533  C C   . LYS A 1 64  ? 6.304  13.331  18.716  1.00 32.49 ? 64  LYS A C   1 
ATOM   534  O O   . LYS A 1 64  ? 5.321  13.283  19.455  1.00 34.07 ? 64  LYS A O   1 
ATOM   535  C CB  . LYS A 1 64  ? 5.760  11.424  17.243  1.00 39.72 ? 64  LYS A CB  1 
ATOM   536  C CG  . LYS A 1 64  ? 5.941  10.693  15.921  1.00 44.07 ? 64  LYS A CG  1 
ATOM   537  C CD  . LYS A 1 64  ? 5.678  9.213   16.050  1.00 47.00 ? 64  LYS A CD  1 
ATOM   538  C CE  . LYS A 1 64  ? 5.249  8.570   14.752  1.00 49.68 ? 64  LYS A CE  1 
ATOM   539  N NZ  . LYS A 1 64  ? 5.012  7.120   14.925  1.00 53.39 ? 64  LYS A NZ  1 
ATOM   540  N N   . GLY A 1 65  ? 7.501  13.749  19.138  1.00 30.39 ? 65  GLY A N   1 
ATOM   541  C CA  . GLY A 1 65  ? 7.760  14.006  20.546  1.00 29.77 ? 65  GLY A CA  1 
ATOM   542  C C   . GLY A 1 65  ? 7.390  15.423  20.984  1.00 29.10 ? 65  GLY A C   1 
ATOM   543  O O   . GLY A 1 65  ? 7.438  16.358  20.191  1.00 31.30 ? 65  GLY A O   1 
ATOM   544  N N   . SER A 1 66  ? 7.051  15.562  22.269  1.00 28.61 ? 66  SER A N   1 
ATOM   545  C CA  . SER A 1 66  ? 6.976  16.852  22.937  1.00 27.86 ? 66  SER A CA  1 
ATOM   546  C C   . SER A 1 66  ? 8.382  17.445  23.022  1.00 25.54 ? 66  SER A C   1 
ATOM   547  O O   . SER A 1 66  ? 9.346  16.698  22.856  1.00 26.41 ? 66  SER A O   1 
ATOM   548  C CB  . SER A 1 66  ? 6.396  16.676  24.313  1.00 30.25 ? 66  SER A CB  1 
ATOM   549  O OG  . SER A 1 66  ? 7.279  15.894  25.107  1.00 29.90 ? 66  SER A OG  1 
ATOM   550  N N   . LYS A 1 67  ? 8.509  18.749  23.341  1.00 28.06 ? 67  LYS A N   1 
ATOM   551  C CA  . LYS A 1 67  ? 9.821  19.339  23.558  1.00 29.48 ? 67  LYS A CA  1 
ATOM   552  C C   . LYS A 1 67  ? 10.621 18.476  24.535  1.00 30.06 ? 67  LYS A C   1 
ATOM   553  O O   . LYS A 1 67  ? 11.801 18.209  24.320  1.00 29.94 ? 67  LYS A O   1 
ATOM   554  C CB  . LYS A 1 67  ? 9.707  20.785  24.084  1.00 35.06 ? 67  LYS A CB  1 
ATOM   555  C CG  . LYS A 1 67  ? 11.040 21.512  24.244  1.00 39.01 ? 67  LYS A CG  1 
ATOM   556  C CD  . LYS A 1 67  ? 10.921 22.997  24.470  1.00 42.78 ? 67  LYS A CD  1 
ATOM   557  C CE  . LYS A 1 67  ? 12.263 23.691  24.397  1.00 45.80 ? 67  LYS A CE  1 
ATOM   558  N NZ  . LYS A 1 67  ? 12.179 25.095  24.864  1.00 48.02 ? 67  LYS A NZ  1 
ATOM   559  N N   . GLU A 1 68  ? 9.965  18.082  25.626  1.00 28.52 ? 68  GLU A N   1 
ATOM   560  C CA  . GLU A 1 68  ? 10.626 17.378  26.706  1.00 30.69 ? 68  GLU A CA  1 
ATOM   561  C C   . GLU A 1 68  ? 11.111 16.017  26.205  1.00 28.72 ? 68  GLU A C   1 
ATOM   562  O O   . GLU A 1 68  ? 12.223 15.605  26.520  1.00 31.33 ? 68  GLU A O   1 
ATOM   563  C CB  . GLU A 1 68  ? 9.678  17.249  27.896  1.00 35.12 ? 68  GLU A CB  1 
ATOM   564  C CG  . GLU A 1 68  ? 10.254 16.447  29.048  1.00 40.14 ? 68  GLU A CG  1 
ATOM   565  C CD  . GLU A 1 68  ? 10.870 17.270  30.164  1.00 47.58 ? 68  GLU A CD  1 
ATOM   566  O OE1 . GLU A 1 68  ? 10.367 17.168  31.303  1.00 53.40 ? 68  GLU A OE1 1 
ATOM   567  O OE2 . GLU A 1 68  ? 11.847 18.011  29.897  1.00 55.99 ? 68  GLU A OE2 1 
ATOM   568  N N   . GLU A 1 69  ? 10.270 15.313  25.433  1.00 25.35 ? 69  GLU A N   1 
ATOM   569  C CA  . GLU A 1 69  ? 10.658 14.031  24.863  1.00 25.59 ? 69  GLU A CA  1 
ATOM   570  C C   . GLU A 1 69  ? 11.808 14.196  23.869  1.00 22.85 ? 69  GLU A C   1 
ATOM   571  O O   . GLU A 1 69  ? 12.747 13.404  23.873  1.00 24.27 ? 69  GLU A O   1 
ATOM   572  C CB  . GLU A 1 69  ? 9.459  13.352  24.201  1.00 25.66 ? 69  GLU A CB  1 
ATOM   573  C CG  . GLU A 1 69  ? 8.403  12.884  25.192  1.00 29.28 ? 69  GLU A CG  1 
ATOM   574  C CD  . GLU A 1 69  ? 7.070  12.475  24.580  1.00 31.86 ? 69  GLU A CD  1 
ATOM   575  O OE1 . GLU A 1 69  ? 6.721  12.990  23.512  1.00 32.58 ? 69  GLU A OE1 1 
ATOM   576  O OE2 . GLU A 1 69  ? 6.399  11.600  25.156  1.00 33.56 ? 69  GLU A OE2 1 
ATOM   577  N N   . GLN A 1 70  ? 11.734 15.205  22.996  1.00 24.15 ? 70  GLN A N   1 
ATOM   578  C CA  . GLN A 1 70  ? 12.745 15.416  21.970  1.00 25.57 ? 70  GLN A CA  1 
ATOM   579  C C   . GLN A 1 70  ? 14.131 15.646  22.577  1.00 24.71 ? 70  GLN A C   1 
ATOM   580  O O   . GLN A 1 70  ? 15.123 15.224  21.987  1.00 24.83 ? 70  GLN A O   1 
ATOM   581  C CB  . GLN A 1 70  ? 12.350 16.570  21.053  1.00 26.03 ? 70  GLN A CB  1 
ATOM   582  C CG  . GLN A 1 70  ? 11.159 16.245  20.172  1.00 28.39 ? 70  GLN A CG  1 
ATOM   583  C CD  . GLN A 1 70  ? 10.811 17.398  19.263  1.00 31.63 ? 70  GLN A CD  1 
ATOM   584  O OE1 . GLN A 1 70  ? 10.872 18.561  19.658  1.00 36.11 ? 70  GLN A OE1 1 
ATOM   585  N NE2 . GLN A 1 70  ? 10.471 17.091  18.024  1.00 36.05 ? 70  GLN A NE2 1 
ATOM   586  N N   . ARG A 1 71  ? 14.188 16.238  23.777  1.00 23.87 ? 71  ARG A N   1 
ATOM   587  C CA  . ARG A 1 71  ? 15.445 16.507  24.460  1.00 26.57 ? 71  ARG A CA  1 
ATOM   588  C C   . ARG A 1 71  ? 16.184 15.190  24.675  1.00 24.57 ? 71  ARG A C   1 
ATOM   589  O O   . ARG A 1 71  ? 17.389 15.094  24.447  1.00 23.86 ? 71  ARG A O   1 
ATOM   590  C CB  . ARG A 1 71  ? 15.176 17.194  25.804  1.00 31.62 ? 71  ARG A CB  1 
ATOM   591  C CG  . ARG A 1 71  ? 16.271 17.038  26.850  1.00 37.98 ? 71  ARG A CG  1 
ATOM   592  C CD  . ARG A 1 71  ? 15.875 17.630  28.194  1.00 43.50 ? 71  ARG A CD  1 
ATOM   593  N NE  . ARG A 1 71  ? 16.841 17.259  29.225  1.00 50.59 ? 71  ARG A NE  1 
ATOM   594  C CZ  . ARG A 1 71  ? 17.357 18.077  30.142  1.00 54.86 ? 71  ARG A CZ  1 
ATOM   595  N NH1 . ARG A 1 71  ? 16.951 19.332  30.233  1.00 55.99 ? 71  ARG A NH1 1 
ATOM   596  N NH2 . ARG A 1 71  ? 18.263 17.620  30.995  1.00 57.74 ? 71  ARG A NH2 1 
ATOM   597  N N   . ASP A 1 72  ? 15.420 14.179  25.101  1.00 25.15 ? 72  ASP A N   1 
ATOM   598  C CA  . ASP A 1 72  ? 15.984 12.875  25.407  1.00 25.02 ? 72  ASP A CA  1 
ATOM   599  C C   . ASP A 1 72  ? 16.326 12.133  24.115  1.00 20.05 ? 72  ASP A C   1 
ATOM   600  O O   . ASP A 1 72  ? 17.352 11.449  24.028  1.00 21.23 ? 72  ASP A O   1 
ATOM   601  C CB  . ASP A 1 72  ? 15.002 12.039  26.228  1.00 28.79 ? 72  ASP A CB  1 
ATOM   602  C CG  . ASP A 1 72  ? 14.695 12.618  27.596  1.00 34.53 ? 72  ASP A CG  1 
ATOM   603  O OD1 . ASP A 1 72  ? 15.546 13.360  28.129  1.00 41.33 ? 72  ASP A OD1 1 
ATOM   604  O OD2 . ASP A 1 72  ? 13.599 12.335  28.109  1.00 41.72 ? 72  ASP A OD2 1 
ATOM   605  N N   . TYR A 1 73  ? 15.448 12.235  23.114  1.00 20.14 ? 73  TYR A N   1 
ATOM   606  C CA  . TYR A 1 73  ? 15.694 11.586  21.836  1.00 19.55 ? 73  TYR A CA  1 
ATOM   607  C C   . TYR A 1 73  ? 16.993 12.090  21.213  1.00 19.37 ? 73  TYR A C   1 
ATOM   608  O O   . TYR A 1 73  ? 17.816 11.311  20.733  1.00 18.44 ? 73  TYR A O   1 
ATOM   609  C CB  . TYR A 1 73  ? 14.536 11.821  20.870  1.00 21.94 ? 73  TYR A CB  1 
ATOM   610  C CG  . TYR A 1 73  ? 13.178 11.308  21.296  1.00 21.53 ? 73  TYR A CG  1 
ATOM   611  C CD1 . TYR A 1 73  ? 13.010 10.343  22.277  1.00 21.46 ? 73  TYR A CD1 1 
ATOM   612  C CD2 . TYR A 1 73  ? 12.034 11.868  20.739  1.00 20.53 ? 73  TYR A CD2 1 
ATOM   613  C CE1 . TYR A 1 73  ? 11.745 9.898   22.635  1.00 23.02 ? 73  TYR A CE1 1 
ATOM   614  C CE2 . TYR A 1 73  ? 10.767 11.454  21.101  1.00 21.85 ? 73  TYR A CE2 1 
ATOM   615  C CZ  . TYR A 1 73  ? 10.622 10.462  22.056  1.00 22.15 ? 73  TYR A CZ  1 
ATOM   616  O OH  . TYR A 1 73  ? 9.355  10.078  22.388  1.00 23.96 ? 73  TYR A OH  1 
ATOM   617  N N   . VAL A 1 74  ? 17.156 13.417  21.182  1.00 19.39 ? 74  VAL A N   1 
ATOM   618  C CA  . VAL A 1 74  ? 18.327 14.038  20.575  1.00 19.90 ? 74  VAL A CA  1 
ATOM   619  C C   . VAL A 1 74  ? 19.601 13.701  21.354  1.00 19.21 ? 74  VAL A C   1 
ATOM   620  O O   . VAL A 1 74  ? 20.641 13.418  20.755  1.00 18.07 ? 74  VAL A O   1 
ATOM   621  C CB  . VAL A 1 74  ? 18.094 15.556  20.408  1.00 22.05 ? 74  VAL A CB  1 
ATOM   622  C CG1 . VAL A 1 74  ? 19.364 16.306  20.044  1.00 25.53 ? 74  VAL A CG1 1 
ATOM   623  C CG2 . VAL A 1 74  ? 17.006 15.807  19.378  1.00 22.60 ? 74  VAL A CG2 1 
ATOM   624  N N   . PHE A 1 75  ? 19.513 13.712  22.694  1.00 17.05 ? 75  PHE A N   1 
ATOM   625  C CA  . PHE A 1 75  ? 20.636 13.335  23.529  1.00 17.79 ? 75  PHE A CA  1 
ATOM   626  C C   . PHE A 1 75  ? 21.119 11.936  23.128  1.00 16.45 ? 75  PHE A C   1 
ATOM   627  O O   . PHE A 1 75  ? 22.300 11.721  22.901  1.00 16.65 ? 75  PHE A O   1 
ATOM   628  C CB  . PHE A 1 75  ? 20.258 13.413  25.005  1.00 18.94 ? 75  PHE A CB  1 
ATOM   629  C CG  . PHE A 1 75  ? 21.373 13.045  25.938  1.00 19.41 ? 75  PHE A CG  1 
ATOM   630  C CD1 . PHE A 1 75  ? 22.364 13.962  26.246  1.00 20.99 ? 75  PHE A CD1 1 
ATOM   631  C CD2 . PHE A 1 75  ? 21.461 11.764  26.470  1.00 20.98 ? 75  PHE A CD2 1 
ATOM   632  C CE1 . PHE A 1 75  ? 23.393 13.620  27.109  1.00 23.57 ? 75  PHE A CE1 1 
ATOM   633  C CE2 . PHE A 1 75  ? 22.493 11.432  27.328  1.00 22.84 ? 75  PHE A CE2 1 
ATOM   634  C CZ  . PHE A 1 75  ? 23.457 12.356  27.643  1.00 23.65 ? 75  PHE A CZ  1 
ATOM   635  N N   . TYR A 1 76  ? 20.199 10.963  23.088  1.00 16.53 ? 76  TYR A N   1 
ATOM   636  C CA  . TYR A 1 76  ? 20.597 9.599   22.779  1.00 17.19 ? 76  TYR A CA  1 
ATOM   637  C C   . TYR A 1 76  ? 20.962 9.387   21.314  1.00 15.96 ? 76  TYR A C   1 
ATOM   638  O O   . TYR A 1 76  ? 21.717 8.454   21.004  1.00 17.06 ? 76  TYR A O   1 
ATOM   639  C CB  . TYR A 1 76  ? 19.533 8.656   23.322  1.00 17.37 ? 76  TYR A CB  1 
ATOM   640  C CG  . TYR A 1 76  ? 19.783 8.357   24.775  1.00 17.72 ? 76  TYR A CG  1 
ATOM   641  C CD1 . TYR A 1 76  ? 20.872 7.585   25.150  1.00 17.66 ? 76  TYR A CD1 1 
ATOM   642  C CD2 . TYR A 1 76  ? 18.960 8.830   25.776  1.00 18.32 ? 76  TYR A CD2 1 
ATOM   643  C CE1 . TYR A 1 76  ? 21.153 7.331   26.483  1.00 20.94 ? 76  TYR A CE1 1 
ATOM   644  C CE2 . TYR A 1 76  ? 19.222 8.573   27.111  1.00 20.18 ? 76  TYR A CE2 1 
ATOM   645  C CZ  . TYR A 1 76  ? 20.324 7.830   27.470  1.00 21.96 ? 76  TYR A CZ  1 
ATOM   646  O OH  . TYR A 1 76  ? 20.557 7.578   28.804  1.00 25.48 ? 76  TYR A OH  1 
ATOM   647  N N   . LEU A 1 77  ? 20.440 10.218  20.408  1.00 16.74 ? 77  LEU A N   1 
ATOM   648  C CA  . LEU A 1 77  ? 20.911 10.201  19.027  1.00 16.41 ? 77  LEU A CA  1 
ATOM   649  C C   . LEU A 1 77  ? 22.370 10.648  18.955  1.00 17.43 ? 77  LEU A C   1 
ATOM   650  O O   . LEU A 1 77  ? 23.145 10.095  18.185  1.00 18.24 ? 77  LEU A O   1 
ATOM   651  C CB  . LEU A 1 77  ? 20.011 11.058  18.141  1.00 17.44 ? 77  LEU A CB  1 
ATOM   652  C CG  . LEU A 1 77  ? 18.713 10.369  17.736  1.00 17.88 ? 77  LEU A CG  1 
ATOM   653  C CD1 . LEU A 1 77  ? 17.683 11.379  17.248  1.00 19.37 ? 77  LEU A CD1 1 
ATOM   654  C CD2 . LEU A 1 77  ? 18.996 9.324   16.665  1.00 18.41 ? 77  LEU A CD2 1 
ATOM   655  N N   . ALA A 1 78  ? 22.744 11.622  19.785  1.00 16.91 ? 78  ALA A N   1 
ATOM   656  C CA  . ALA A 1 78  ? 24.130 12.062  19.856  1.00 18.10 ? 78  ALA A CA  1 
ATOM   657  C C   . ALA A 1 78  ? 24.994 10.954  20.452  1.00 17.11 ? 78  ALA A C   1 
ATOM   658  O O   . ALA A 1 78  ? 26.053 10.644  19.928  1.00 18.15 ? 78  ALA A O   1 
ATOM   659  C CB  . ALA A 1 78  ? 24.243 13.349  20.644  1.00 17.53 ? 78  ALA A CB  1 
ATOM   660  N N   . VAL A 1 79  ? 24.508 10.320  21.525  1.00 16.96 ? 79  VAL A N   1 
ATOM   661  C CA  . VAL A 1 79  ? 25.247 9.245   22.166  1.00 16.95 ? 79  VAL A CA  1 
ATOM   662  C C   . VAL A 1 79  ? 25.455 8.091   21.185  1.00 17.55 ? 79  VAL A C   1 
ATOM   663  O O   . VAL A 1 79  ? 26.565 7.563   21.097  1.00 17.36 ? 79  VAL A O   1 
ATOM   664  C CB  . VAL A 1 79  ? 24.514 8.753   23.425  1.00 17.99 ? 79  VAL A CB  1 
ATOM   665  C CG1 . VAL A 1 79  ? 25.076 7.453   23.970  1.00 19.17 ? 79  VAL A CG1 1 
ATOM   666  C CG2 . VAL A 1 79  ? 24.538 9.779   24.544  1.00 19.39 ? 79  VAL A CG2 1 
ATOM   667  N N   . GLY A 1 80  ? 24.369 7.650   20.535  1.00 16.72 ? 80  GLY A N   1 
ATOM   668  C CA  . GLY A 1 80  ? 24.443 6.522   19.616  1.00 17.64 ? 80  GLY A CA  1 
ATOM   669  C C   . GLY A 1 80  ? 25.432 6.759   18.480  1.00 17.51 ? 80  GLY A C   1 
ATOM   670  O O   . GLY A 1 80  ? 26.285 5.928   18.164  1.00 17.62 ? 80  GLY A O   1 
ATOM   671  N N   . ASN A 1 81  ? 25.327 7.928   17.849  1.00 17.09 ? 81  ASN A N   1 
ATOM   672  C CA  . ASN A 1 81  ? 26.230 8.294   16.774  1.00 18.02 ? 81  ASN A CA  1 
ATOM   673  C C   . ASN A 1 81  ? 27.670 8.371   17.278  1.00 17.71 ? 81  ASN A C   1 
ATOM   674  O O   . ASN A 1 81  ? 28.581 7.931   16.578  1.00 19.79 ? 81  ASN A O   1 
ATOM   675  C CB  . ASN A 1 81  ? 25.740 9.547   16.059  1.00 18.13 ? 81  ASN A CB  1 
ATOM   676  C CG  . ASN A 1 81  ? 24.671 9.201   15.052  1.00 18.13 ? 81  ASN A CG  1 
ATOM   677  O OD1 . ASN A 1 81  ? 24.961 8.531   14.055  1.00 21.29 ? 81  ASN A OD1 1 
ATOM   678  N ND2 . ASN A 1 81  ? 23.449 9.635   15.312  1.00 19.21 ? 81  ASN A ND2 1 
ATOM   679  N N   . TYR A 1 82  ? 27.870 8.916   18.486  1.00 16.46 ? 82  TYR A N   1 
ATOM   680  C CA  . TYR A 1 82  ? 29.193 8.967   19.079  1.00 16.96 ? 82  TYR A CA  1 
ATOM   681  C C   . TYR A 1 82  ? 29.789 7.558   19.169  1.00 17.51 ? 82  TYR A C   1 
ATOM   682  O O   . TYR A 1 82  ? 30.925 7.339   18.788  1.00 19.44 ? 82  TYR A O   1 
ATOM   683  C CB  . TYR A 1 82  ? 29.171 9.709   20.420  1.00 17.56 ? 82  TYR A CB  1 
ATOM   684  C CG  . TYR A 1 82  ? 30.456 9.610   21.197  1.00 18.84 ? 82  TYR A CG  1 
ATOM   685  C CD1 . TYR A 1 82  ? 31.607 10.238  20.750  1.00 19.29 ? 82  TYR A CD1 1 
ATOM   686  C CD2 . TYR A 1 82  ? 30.524 8.920   22.394  1.00 23.31 ? 82  TYR A CD2 1 
ATOM   687  C CE1 . TYR A 1 82  ? 32.797 10.130  21.446  1.00 20.68 ? 82  TYR A CE1 1 
ATOM   688  C CE2 . TYR A 1 82  ? 31.700 8.845   23.123  1.00 24.05 ? 82  TYR A CE2 1 
ATOM   689  C CZ  . TYR A 1 82  ? 32.839 9.464   22.653  1.00 22.68 ? 82  TYR A CZ  1 
ATOM   690  O OH  . TYR A 1 82  ? 34.027 9.370   23.334  1.00 26.32 ? 82  TYR A OH  1 
ATOM   691  N N   . ARG A 1 83  ? 29.016 6.601   19.685  1.00 17.52 ? 83  ARG A N   1 
ATOM   692  C CA  . ARG A 1 83  ? 29.543 5.251   19.879  1.00 18.75 ? 83  ARG A CA  1 
ATOM   693  C C   . ARG A 1 83  ? 29.852 4.559   18.549  1.00 19.71 ? 83  ARG A C   1 
ATOM   694  O O   . ARG A 1 83  ? 30.680 3.643   18.521  1.00 22.58 ? 83  ARG A O   1 
ATOM   695  C CB  . ARG A 1 83  ? 28.572 4.405   20.702  1.00 18.75 ? 83  ARG A CB  1 
ATOM   696  C CG  . ARG A 1 83  ? 28.361 4.908   22.122  1.00 18.34 ? 83  ARG A CG  1 
ATOM   697  C CD  . ARG A 1 83  ? 27.673 3.911   23.015  1.00 20.13 ? 83  ARG A CD  1 
ATOM   698  N NE  . ARG A 1 83  ? 28.564 2.782   23.209  1.00 21.43 ? 83  ARG A NE  1 
ATOM   699  C CZ  . ARG A 1 83  ? 28.198 1.517   23.071  1.00 23.08 ? 83  ARG A CZ  1 
ATOM   700  N NH1 . ARG A 1 83  ? 26.923 1.220   22.894  1.00 23.15 ? 83  ARG A NH1 1 
ATOM   701  N NH2 . ARG A 1 83  ? 29.105 0.556   23.151  1.00 25.76 ? 83  ARG A NH2 1 
ATOM   702  N N   . LEU A 1 84  ? 29.175 4.970   17.465  1.00 19.55 ? 84  LEU A N   1 
ATOM   703  C CA  . LEU A 1 84  ? 29.433 4.450   16.123  1.00 20.48 ? 84  LEU A CA  1 
ATOM   704  C C   . LEU A 1 84  ? 30.597 5.180   15.442  1.00 20.14 ? 84  LEU A C   1 
ATOM   705  O O   . LEU A 1 84  ? 30.954 4.845   14.314  1.00 21.77 ? 84  LEU A O   1 
ATOM   706  C CB  . LEU A 1 84  ? 28.161 4.573   15.272  1.00 20.77 ? 84  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 84  ? 27.023 3.623   15.642  1.00 22.60 ? 84  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 84  ? 25.757 4.013   14.902  1.00 25.02 ? 84  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 84  ? 27.397 2.188   15.318  1.00 24.86 ? 84  LEU A CD2 1 
ATOM   710  N N   . LYS A 1 85  ? 31.178 6.171   16.127  1.00 20.54 ? 85  LYS A N   1 
ATOM   711  C CA  . LYS A 1 85  ? 32.238 7.024   15.594  1.00 21.37 ? 85  LYS A CA  1 
ATOM   712  C C   . LYS A 1 85  ? 31.737 7.883   14.423  1.00 23.50 ? 85  LYS A C   1 
ATOM   713  O O   . LYS A 1 85  ? 32.523 8.345   13.604  1.00 24.67 ? 85  LYS A O   1 
ATOM   714  C CB  . LYS A 1 85  ? 33.488 6.214   15.232  1.00 23.88 ? 85  LYS A CB  1 
ATOM   715  C CG  . LYS A 1 85  ? 34.000 5.309   16.348  1.00 26.76 ? 85  LYS A CG  1 
ATOM   716  C CD  . LYS A 1 85  ? 35.284 4.601   16.009  1.00 31.84 ? 85  LYS A CD  1 
ATOM   717  C CE  . LYS A 1 85  ? 35.979 4.029   17.226  1.00 36.30 ? 85  LYS A CE  1 
ATOM   718  N NZ  . LYS A 1 85  ? 35.094 3.128   17.991  1.00 40.58 ? 85  LYS A NZ  1 
ATOM   719  N N   . GLU A 1 86  ? 30.425 8.142   14.392  1.00 22.45 ? 86  GLU A N   1 
ATOM   720  C CA  . GLU A 1 86  ? 29.813 9.040   13.431  1.00 24.36 ? 86  GLU A CA  1 
ATOM   721  C C   . GLU A 1 86  ? 29.824 10.434  14.049  1.00 22.10 ? 86  GLU A C   1 
ATOM   722  O O   . GLU A 1 86  ? 28.786 10.952  14.475  1.00 22.21 ? 86  GLU A O   1 
ATOM   723  C CB  . GLU A 1 86  ? 28.398 8.550   13.128  1.00 25.46 ? 86  GLU A CB  1 
ATOM   724  C CG  . GLU A 1 86  ? 28.357 7.232   12.391  1.00 29.76 ? 86  GLU A CG  1 
ATOM   725  C CD  . GLU A 1 86  ? 28.552 7.337   10.890  1.00 35.57 ? 86  GLU A CD  1 
ATOM   726  O OE1 . GLU A 1 86  ? 28.842 8.455   10.394  1.00 41.24 ? 86  GLU A OE1 1 
ATOM   727  O OE2 . GLU A 1 86  ? 28.392 6.311   10.224  1.00 44.56 ? 86  GLU A OE2 1 
ATOM   728  N N   . TYR A 1 87  ? 31.013 11.033  14.119  1.00 21.94 ? 87  TYR A N   1 
ATOM   729  C CA  . TYR A 1 87  ? 31.195 12.203  14.971  1.00 21.69 ? 87  TYR A CA  1 
ATOM   730  C C   . TYR A 1 87  ? 30.464 13.432  14.434  1.00 21.83 ? 87  TYR A C   1 
ATOM   731  O O   . TYR A 1 87  ? 29.934 14.220  15.231  1.00 21.17 ? 87  TYR A O   1 
ATOM   732  C CB  . TYR A 1 87  ? 32.679 12.492  15.185  1.00 21.88 ? 87  TYR A CB  1 
ATOM   733  C CG  . TYR A 1 87  ? 33.437 11.362  15.829  1.00 22.60 ? 87  TYR A CG  1 
ATOM   734  C CD1 . TYR A 1 87  ? 32.992 10.775  17.005  1.00 23.97 ? 87  TYR A CD1 1 
ATOM   735  C CD2 . TYR A 1 87  ? 34.584 10.860  15.251  1.00 23.70 ? 87  TYR A CD2 1 
ATOM   736  C CE1 . TYR A 1 87  ? 33.682 9.740   17.611  1.00 23.64 ? 87  TYR A CE1 1 
ATOM   737  C CE2 . TYR A 1 87  ? 35.278 9.814   15.832  1.00 24.60 ? 87  TYR A CE2 1 
ATOM   738  C CZ  . TYR A 1 87  ? 34.825 9.253   17.016  1.00 24.62 ? 87  TYR A CZ  1 
ATOM   739  O OH  . TYR A 1 87  ? 35.498 8.207   17.610  1.00 28.18 ? 87  TYR A OH  1 
ATOM   740  N N   . GLU A 1 88  ? 30.439 13.601  13.107  1.00 23.26 ? 88  GLU A N   1 
ATOM   741  C CA  . GLU A 1 88  ? 29.779 14.759  12.512  1.00 23.97 ? 88  GLU A CA  1 
ATOM   742  C C   . GLU A 1 88  ? 28.288 14.731  12.854  1.00 22.16 ? 88  GLU A C   1 
ATOM   743  O O   . GLU A 1 88  ? 27.701 15.761  13.224  1.00 22.55 ? 88  GLU A O   1 
ATOM   744  C CB  . GLU A 1 88  ? 30.036 14.825  11.003  1.00 28.61 ? 88  GLU A CB  1 
ATOM   745  C CG  . GLU A 1 88  ? 28.890 15.410  10.196  1.00 35.75 ? 88  GLU A CG  1 
ATOM   746  C CD  . GLU A 1 88  ? 29.186 15.632  8.721   1.00 42.49 ? 88  GLU A CD  1 
ATOM   747  O OE1 . GLU A 1 88  ? 29.384 14.631  7.994   1.00 47.32 ? 88  GLU A OE1 1 
ATOM   748  O OE2 . GLU A 1 88  ? 29.205 16.806  8.302   1.00 49.05 ? 88  GLU A OE2 1 
ATOM   749  N N   . LYS A 1 89  ? 27.681 13.534  12.764  1.00 21.04 ? 89  LYS A N   1 
ATOM   750  C CA  . LYS A 1 89  ? 26.268 13.388  13.069  1.00 23.00 ? 89  LYS A CA  1 
ATOM   751  C C   . LYS A 1 89  ? 26.025 13.653  14.550  1.00 20.87 ? 89  LYS A C   1 
ATOM   752  O O   . LYS A 1 89  ? 25.064 14.323  14.914  1.00 21.11 ? 89  LYS A O   1 
ATOM   753  C CB  . LYS A 1 89  ? 25.757 11.998  12.693  1.00 25.51 ? 89  LYS A CB  1 
ATOM   754  C CG  . LYS A 1 89  ? 25.679 11.715  11.202  1.00 28.16 ? 89  LYS A CG  1 
ATOM   755  C CD  . LYS A 1 89  ? 24.957 10.417  10.911  1.00 31.43 ? 89  LYS A CD  1 
ATOM   756  C CE  . LYS A 1 89  ? 25.146 9.934   9.491   1.00 34.70 ? 89  LYS A CE  1 
ATOM   757  N NZ  . LYS A 1 89  ? 26.578 9.717   9.177   1.00 39.11 ? 89  LYS A NZ  1 
ATOM   758  N N   . ALA A 1 90  ? 26.888 13.088  15.397  1.00 20.00 ? 90  ALA A N   1 
ATOM   759  C CA  . ALA A 1 90  ? 26.763 13.251  16.835  1.00 19.69 ? 90  ALA A CA  1 
ATOM   760  C C   . ALA A 1 90  ? 26.843 14.727  17.222  1.00 19.52 ? 90  ALA A C   1 
ATOM   761  O O   . ALA A 1 90  ? 26.070 15.190  18.051  1.00 18.84 ? 90  ALA A O   1 
ATOM   762  C CB  . ALA A 1 90  ? 27.829 12.440  17.529  1.00 19.27 ? 90  ALA A CB  1 
ATOM   763  N N   . LEU A 1 91  ? 27.786 15.453  16.619  1.00 20.97 ? 91  LEU A N   1 
ATOM   764  C CA  . LEU A 1 91  ? 27.992 16.859  16.940  1.00 21.08 ? 91  LEU A CA  1 
ATOM   765  C C   . LEU A 1 91  ? 26.776 17.675  16.511  1.00 19.82 ? 91  LEU A C   1 
ATOM   766  O O   . LEU A 1 91  ? 26.350 18.563  17.241  1.00 21.72 ? 91  LEU A O   1 
ATOM   767  C CB  . LEU A 1 91  ? 29.283 17.346  16.272  1.00 23.86 ? 91  LEU A CB  1 
ATOM   768  C CG  . LEU A 1 91  ? 29.828 18.691  16.742  1.00 27.64 ? 91  LEU A CG  1 
ATOM   769  C CD1 . LEU A 1 91  ? 30.281 18.605  18.197  1.00 29.95 ? 91  LEU A CD1 1 
ATOM   770  C CD2 . LEU A 1 91  ? 30.979 19.117  15.844  1.00 28.46 ? 91  LEU A CD2 1 
ATOM   771  N N   . LYS A 1 92  ? 26.192 17.361  15.348  1.00 19.53 ? 92  LYS A N   1 
ATOM   772  C CA  . LYS A 1 92  ? 25.003 18.077  14.904  1.00 21.19 ? 92  LYS A CA  1 
ATOM   773  C C   . LYS A 1 92  ? 23.848 17.891  15.889  1.00 20.17 ? 92  LYS A C   1 
ATOM   774  O O   . LYS A 1 92  ? 23.157 18.846  16.244  1.00 23.05 ? 92  LYS A O   1 
ATOM   775  C CB  . LYS A 1 92  ? 24.587 17.696  13.485  1.00 24.01 ? 92  LYS A CB  1 
ATOM   776  C CG  . LYS A 1 92  ? 25.518 18.196  12.394  1.00 29.53 ? 92  LYS A CG  1 
ATOM   777  C CD  . LYS A 1 92  ? 25.100 17.747  11.013  1.00 35.57 ? 92  LYS A CD  1 
ATOM   778  C CE  . LYS A 1 92  ? 26.029 18.237  9.925   1.00 39.25 ? 92  LYS A CE  1 
ATOM   779  N NZ  . LYS A 1 92  ? 25.640 17.691  8.602   1.00 43.12 ? 92  LYS A NZ  1 
ATOM   780  N N   . TYR A 1 93  ? 23.657 16.670  16.376  1.00 20.35 ? 93  TYR A N   1 
ATOM   781  C CA  . TYR A 1 93  ? 22.587 16.417  17.325  1.00 21.22 ? 93  TYR A CA  1 
ATOM   782  C C   . TYR A 1 93  ? 22.827 17.152  18.645  1.00 20.09 ? 93  TYR A C   1 
ATOM   783  O O   . TYR A 1 93  ? 21.927 17.823  19.147  1.00 22.10 ? 93  TYR A O   1 
ATOM   784  C CB  . TYR A 1 93  ? 22.419 14.913  17.561  1.00 20.87 ? 93  TYR A CB  1 
ATOM   785  C CG  . TYR A 1 93  ? 21.561 14.222  16.531  1.00 22.07 ? 93  TYR A CG  1 
ATOM   786  C CD1 . TYR A 1 93  ? 20.251 14.633  16.320  1.00 23.02 ? 93  TYR A CD1 1 
ATOM   787  C CD2 . TYR A 1 93  ? 22.042 13.165  15.769  1.00 22.55 ? 93  TYR A CD2 1 
ATOM   788  C CE1 . TYR A 1 93  ? 19.435 14.015  15.390  1.00 24.06 ? 93  TYR A CE1 1 
ATOM   789  C CE2 . TYR A 1 93  ? 21.245 12.560  14.813  1.00 23.79 ? 93  TYR A CE2 1 
ATOM   790  C CZ  . TYR A 1 93  ? 19.939 12.976  14.628  1.00 24.28 ? 93  TYR A CZ  1 
ATOM   791  O OH  . TYR A 1 93  ? 19.134 12.354  13.701  1.00 30.27 ? 93  TYR A OH  1 
ATOM   792  N N   . VAL A 1 94  ? 24.026 17.016  19.225  1.00 18.94 ? 94  VAL A N   1 
ATOM   793  C CA  . VAL A 1 94  ? 24.292 17.638  20.514  1.00 20.90 ? 94  VAL A CA  1 
ATOM   794  C C   . VAL A 1 94  ? 24.271 19.169  20.403  1.00 21.23 ? 94  VAL A C   1 
ATOM   795  O O   . VAL A 1 94  ? 23.826 19.833  21.336  1.00 22.74 ? 94  VAL A O   1 
ATOM   796  C CB  . VAL A 1 94  ? 25.595 17.107  21.148  1.00 22.07 ? 94  VAL A CB  1 
ATOM   797  C CG1 . VAL A 1 94  ? 26.846 17.706  20.511  1.00 21.67 ? 94  VAL A CG1 1 
ATOM   798  C CG2 . VAL A 1 94  ? 25.587 17.336  22.655  1.00 22.96 ? 94  VAL A CG2 1 
ATOM   799  N N   . ARG A 1 95  ? 24.708 19.743  19.272  1.00 21.34 ? 95  ARG A N   1 
ATOM   800  C CA  . ARG A 1 95  ? 24.698 21.200  19.127  1.00 23.87 ? 95  ARG A CA  1 
ATOM   801  C C   . ARG A 1 95  ? 23.265 21.705  19.026  1.00 23.93 ? 95  ARG A C   1 
ATOM   802  O O   . ARG A 1 95  ? 22.963 22.805  19.512  1.00 25.98 ? 95  ARG A O   1 
ATOM   803  C CB  . ARG A 1 95  ? 25.532 21.633  17.919  1.00 25.05 ? 95  ARG A CB  1 
ATOM   804  C CG  . ARG A 1 95  ? 27.022 21.536  18.196  1.00 29.38 ? 95  ARG A CG  1 
ATOM   805  C CD  . ARG A 1 95  ? 27.888 21.857  17.007  1.00 33.16 ? 95  ARG A CD  1 
ATOM   806  N NE  . ARG A 1 95  ? 29.275 21.961  17.424  1.00 41.74 ? 95  ARG A NE  1 
ATOM   807  C CZ  . ARG A 1 95  ? 30.277 22.323  16.632  1.00 46.21 ? 95  ARG A CZ  1 
ATOM   808  N NH1 . ARG A 1 95  ? 30.040 22.704  15.389  1.00 48.49 ? 95  ARG A NH1 1 
ATOM   809  N NH2 . ARG A 1 95  ? 31.516 22.307  17.093  1.00 48.85 ? 95  ARG A NH2 1 
ATOM   810  N N   . GLY A 1 96  ? 22.381 20.881  18.436  1.00 23.87 ? 96  GLY A N   1 
ATOM   811  C CA  . GLY A 1 96  ? 20.968 21.216  18.400  1.00 24.92 ? 96  GLY A CA  1 
ATOM   812  C C   . GLY A 1 96  ? 20.359 21.270  19.800  1.00 26.09 ? 96  GLY A C   1 
ATOM   813  O O   . GLY A 1 96  ? 19.596 22.182  20.121  1.00 28.56 ? 96  GLY A O   1 
ATOM   814  N N   . LEU A 1 97  ? 20.722 20.303  20.646  1.00 24.79 ? 97  LEU A N   1 
ATOM   815  C CA  . LEU A 1 97  ? 20.271 20.270  22.027  1.00 26.37 ? 97  LEU A CA  1 
ATOM   816  C C   . LEU A 1 97  ? 20.801 21.481  22.796  1.00 25.69 ? 97  LEU A C   1 
ATOM   817  O O   . LEU A 1 97  ? 20.070 22.087  23.587  1.00 27.88 ? 97  LEU A O   1 
ATOM   818  C CB  . LEU A 1 97  ? 20.739 18.953  22.655  1.00 26.55 ? 97  LEU A CB  1 
ATOM   819  C CG  . LEU A 1 97  ? 20.369 18.722  24.122  1.00 28.57 ? 97  LEU A CG  1 
ATOM   820  C CD1 . LEU A 1 97  ? 18.878 18.881  24.353  1.00 31.38 ? 97  LEU A CD1 1 
ATOM   821  C CD2 . LEU A 1 97  ? 20.821 17.338  24.572  1.00 27.80 ? 97  LEU A CD2 1 
ATOM   822  N N   . LEU A 1 98  ? 22.060 21.859  22.539  1.00 24.37 ? 98  LEU A N   1 
ATOM   823  C CA  . LEU A 1 98  ? 22.658 22.978  23.259  1.00 23.84 ? 98  LEU A CA  1 
ATOM   824  C C   . LEU A 1 98  ? 22.057 24.301  22.803  1.00 24.49 ? 98  LEU A C   1 
ATOM   825  O O   . LEU A 1 98  ? 22.135 25.274  23.543  1.00 27.45 ? 98  LEU A O   1 
ATOM   826  C CB  . LEU A 1 98  ? 24.181 22.959  23.080  1.00 24.33 ? 98  LEU A CB  1 
ATOM   827  C CG  . LEU A 1 98  ? 24.907 21.901  23.912  1.00 23.47 ? 98  LEU A CG  1 
ATOM   828  C CD1 . LEU A 1 98  ? 26.324 21.684  23.439  1.00 25.00 ? 98  LEU A CD1 1 
ATOM   829  C CD2 . LEU A 1 98  ? 24.915 22.283  25.380  1.00 23.98 ? 98  LEU A CD2 1 
ATOM   830  N N   . GLN A 1 99  ? 21.494 24.349  21.593  1.00 24.30 ? 99  GLN A N   1 
ATOM   831  C CA  . GLN A 1 99  ? 20.734 25.512  21.173  1.00 27.43 ? 99  GLN A CA  1 
ATOM   832  C C   . GLN A 1 99  ? 19.524 25.696  22.089  1.00 27.28 ? 99  GLN A C   1 
ATOM   833  O O   . GLN A 1 99  ? 19.231 26.811  22.481  1.00 34.44 ? 99  GLN A O   1 
ATOM   834  C CB  . GLN A 1 99  ? 20.342 25.391  19.701  1.00 31.52 ? 99  GLN A CB  1 
ATOM   835  C CG  . GLN A 1 99  ? 21.508 25.646  18.753  1.00 35.53 ? 99  GLN A CG  1 
ATOM   836  C CD  . GLN A 1 99  ? 21.136 25.457  17.300  1.00 41.67 ? 99  GLN A CD  1 
ATOM   837  O OE1 . GLN A 1 99  ? 20.393 24.546  16.935  1.00 47.64 ? 99  GLN A OE1 1 
ATOM   838  N NE2 . GLN A 1 99  ? 21.625 26.346  16.452  1.00 42.14 ? 99  GLN A NE2 1 
ATOM   839  N N   . THR A 1 100 ? 18.854 24.603  22.467  1.00 27.31 ? 100 THR A N   1 
ATOM   840  C CA  . THR A 1 100 ? 17.662 24.671  23.300  1.00 29.79 ? 100 THR A CA  1 
ATOM   841  C C   . THR A 1 100 ? 18.035 24.877  24.774  1.00 27.25 ? 100 THR A C   1 
ATOM   842  O O   . THR A 1 100 ? 17.293 25.542  25.494  1.00 31.89 ? 100 THR A O   1 
ATOM   843  C CB  . THR A 1 100 ? 16.787 23.423  23.106  1.00 35.41 ? 100 THR A CB  1 
ATOM   844  O OG1 . THR A 1 100 ? 17.448 22.316  23.705  1.00 42.64 ? 100 THR A OG1 1 
ATOM   845  C CG2 . THR A 1 100 ? 16.514 23.087  21.657  1.00 38.21 ? 100 THR A CG2 1 
ATOM   846  N N   . GLU A 1 101 ? 19.176 24.321  25.213  1.00 28.47 ? 101 GLU A N   1 
ATOM   847  C CA  . GLU A 1 101 ? 19.580 24.333  26.616  1.00 30.15 ? 101 GLU A CA  1 
ATOM   848  C C   . GLU A 1 101 ? 21.095 24.531  26.694  1.00 28.75 ? 101 GLU A C   1 
ATOM   849  O O   . GLU A 1 101 ? 21.839 23.574  26.930  1.00 26.84 ? 101 GLU A O   1 
ATOM   850  C CB  . GLU A 1 101 ? 19.212 23.032  27.344  1.00 35.30 ? 101 GLU A CB  1 
ATOM   851  C CG  . GLU A 1 101 ? 18.219 22.143  26.621  1.00 40.20 ? 101 GLU A CG  1 
ATOM   852  C CD  . GLU A 1 101 ? 17.639 21.027  27.473  1.00 42.81 ? 101 GLU A CD  1 
ATOM   853  O OE1 . GLU A 1 101 ? 18.405 20.405  28.234  1.00 42.97 ? 101 GLU A OE1 1 
ATOM   854  O OE2 . GLU A 1 101 ? 16.423 20.771  27.359  1.00 48.69 ? 101 GLU A OE2 1 
ATOM   855  N N   . PRO A 1 102 ? 21.609 25.760  26.457  1.00 28.15 ? 102 PRO A N   1 
ATOM   856  C CA  . PRO A 1 102 ? 23.052 26.014  26.467  1.00 30.49 ? 102 PRO A CA  1 
ATOM   857  C C   . PRO A 1 102 ? 23.796 25.619  27.745  1.00 32.74 ? 102 PRO A C   1 
ATOM   858  O O   . PRO A 1 102 ? 25.002 25.385  27.688  1.00 35.27 ? 102 PRO A O   1 
ATOM   859  C CB  . PRO A 1 102 ? 23.158 27.541  26.280  1.00 31.21 ? 102 PRO A CB  1 
ATOM   860  C CG  . PRO A 1 102 ? 21.872 27.936  25.606  1.00 31.18 ? 102 PRO A CG  1 
ATOM   861  C CD  . PRO A 1 102 ? 20.832 26.966  26.117  1.00 29.92 ? 102 PRO A CD  1 
ATOM   862  N N   . GLN A 1 103 ? 23.088 25.556  28.887  1.00 33.81 ? 103 GLN A N   1 
ATOM   863  C CA  . GLN A 1 103 ? 23.728 25.220  30.152  1.00 37.41 ? 103 GLN A CA  1 
ATOM   864  C C   . GLN A 1 103 ? 23.402 23.792  30.592  1.00 35.45 ? 103 GLN A C   1 
ATOM   865  O O   . GLN A 1 103 ? 23.588 23.459  31.761  1.00 37.42 ? 103 GLN A O   1 
ATOM   866  C CB  . GLN A 1 103 ? 23.353 26.235  31.235  1.00 43.16 ? 103 GLN A CB  1 
ATOM   867  C CG  . GLN A 1 103 ? 24.012 27.591  31.038  1.00 47.29 ? 103 GLN A CG  1 
ATOM   868  C CD  . GLN A 1 103 ? 25.489 27.505  30.735  1.00 53.73 ? 103 GLN A CD  1 
ATOM   869  O OE1 . GLN A 1 103 ? 25.959 27.959  29.692  1.00 58.80 ? 103 GLN A OE1 1 
ATOM   870  N NE2 . GLN A 1 103 ? 26.240 26.921  31.654  1.00 58.47 ? 103 GLN A NE2 1 
ATOM   871  N N   . ASN A 1 104 ? 22.960 22.936  29.657  1.00 29.58 ? 104 ASN A N   1 
ATOM   872  C CA  . ASN A 1 104 ? 22.825 21.514  29.950  1.00 28.83 ? 104 ASN A CA  1 
ATOM   873  C C   . ASN A 1 104 ? 24.236 20.949  30.082  1.00 27.50 ? 104 ASN A C   1 
ATOM   874  O O   . ASN A 1 104 ? 24.942 20.822  29.093  1.00 26.88 ? 104 ASN A O   1 
ATOM   875  C CB  . ASN A 1 104 ? 21.976 20.775  28.902  1.00 28.60 ? 104 ASN A CB  1 
ATOM   876  C CG  . ASN A 1 104 ? 21.858 19.272  29.111  1.00 28.66 ? 104 ASN A CG  1 
ATOM   877  O OD1 . ASN A 1 104 ? 22.758 18.635  29.635  1.00 28.11 ? 104 ASN A OD1 1 
ATOM   878  N ND2 . ASN A 1 104 ? 20.774 18.670  28.646  1.00 31.79 ? 104 ASN A ND2 1 
ATOM   879  N N   . ASN A 1 105 ? 24.636 20.621  31.313  1.00 26.55 ? 105 ASN A N   1 
ATOM   880  C CA  . ASN A 1 105 ? 25.999 20.207  31.589  1.00 26.47 ? 105 ASN A CA  1 
ATOM   881  C C   . ASN A 1 105 ? 26.275 18.854  30.949  1.00 23.38 ? 105 ASN A C   1 
ATOM   882  O O   . ASN A 1 105 ? 27.394 18.588  30.531  1.00 25.26 ? 105 ASN A O   1 
ATOM   883  C CB  . ASN A 1 105 ? 26.304 20.158  33.084  1.00 31.13 ? 105 ASN A CB  1 
ATOM   884  C CG  . ASN A 1 105 ? 26.350 21.536  33.706  1.00 36.51 ? 105 ASN A CG  1 
ATOM   885  O OD1 . ASN A 1 105 ? 26.959 22.454  33.154  1.00 43.05 ? 105 ASN A OD1 1 
ATOM   886  N ND2 . ASN A 1 105 ? 25.679 21.704  34.834  1.00 41.31 ? 105 ASN A ND2 1 
ATOM   887  N N   . GLN A 1 106 ? 25.251 18.005  30.857  1.00 25.70 ? 106 GLN A N   1 
ATOM   888  C CA  . GLN A 1 106 ? 25.479 16.692  30.270  1.00 25.41 ? 106 GLN A CA  1 
ATOM   889  C C   . GLN A 1 106 ? 25.717 16.820  28.767  1.00 23.90 ? 106 GLN A C   1 
ATOM   890  O O   . GLN A 1 106 ? 26.595 16.161  28.207  1.00 23.15 ? 106 GLN A O   1 
ATOM   891  C CB  . GLN A 1 106 ? 24.329 15.722  30.564  1.00 26.27 ? 106 GLN A CB  1 
ATOM   892  C CG  . GLN A 1 106 ? 24.167 15.386  32.039  1.00 27.55 ? 106 GLN A CG  1 
ATOM   893  C CD  . GLN A 1 106 ? 23.781 16.547  32.921  1.00 29.32 ? 106 GLN A CD  1 
ATOM   894  O OE1 . GLN A 1 106 ? 22.778 17.230  32.696  1.00 33.49 ? 106 GLN A OE1 1 
ATOM   895  N NE2 . GLN A 1 106 ? 24.597 16.791  33.931  1.00 31.52 ? 106 GLN A NE2 1 
ATOM   896  N N   . ALA A 1 107 ? 24.930 17.666  28.104  1.00 23.88 ? 107 ALA A N   1 
ATOM   897  C CA  . ALA A 1 107 ? 25.117 17.923  26.686  1.00 23.89 ? 107 ALA A CA  1 
ATOM   898  C C   . ALA A 1 107 ? 26.468 18.601  26.432  1.00 21.92 ? 107 ALA A C   1 
ATOM   899  O O   . ALA A 1 107 ? 27.142 18.276  25.457  1.00 21.65 ? 107 ALA A O   1 
ATOM   900  C CB  . ALA A 1 107 ? 23.957 18.729  26.166  1.00 25.16 ? 107 ALA A CB  1 
ATOM   901  N N   . LYS A 1 108 ? 26.866 19.563  27.280  1.00 22.53 ? 108 LYS A N   1 
ATOM   902  C CA  . LYS A 1 108 ? 28.175 20.180  27.130  1.00 23.19 ? 108 LYS A CA  1 
ATOM   903  C C   . LYS A 1 108 ? 29.288 19.134  27.217  1.00 22.95 ? 108 LYS A C   1 
ATOM   904  O O   . LYS A 1 108 ? 30.233 19.165  26.429  1.00 24.27 ? 108 LYS A O   1 
ATOM   905  C CB  . LYS A 1 108 ? 28.392 21.281  28.175  1.00 25.84 ? 108 LYS A CB  1 
ATOM   906  C CG  . LYS A 1 108 ? 27.585 22.556  27.934  1.00 29.89 ? 108 LYS A CG  1 
ATOM   907  C CD  . LYS A 1 108 ? 28.127 23.822  28.589  1.00 34.87 ? 108 LYS A CD  1 
ATOM   908  C CE  . LYS A 1 108 ? 27.991 23.852  30.094  1.00 37.54 ? 108 LYS A CE  1 
ATOM   909  N NZ  . LYS A 1 108 ? 28.495 25.138  30.638  1.00 39.91 ? 108 LYS A NZ  1 
ATOM   910  N N   . GLU A 1 109 ? 29.177 18.204  28.178  1.00 23.51 ? 109 GLU A N   1 
ATOM   911  C CA  . GLU A 1 109 ? 30.218 17.210  28.376  1.00 25.17 ? 109 GLU A CA  1 
ATOM   912  C C   . GLU A 1 109 ? 30.266 16.238  27.194  1.00 23.94 ? 109 GLU A C   1 
ATOM   913  O O   . GLU A 1 109 ? 31.335 15.779  26.812  1.00 23.89 ? 109 GLU A O   1 
ATOM   914  C CB  . GLU A 1 109 ? 29.987 16.448  29.682  1.00 27.97 ? 109 GLU A CB  1 
ATOM   915  C CG  . GLU A 1 109 ? 30.297 17.280  30.919  1.00 32.22 ? 109 GLU A CG  1 
ATOM   916  C CD  . GLU A 1 109 ? 30.007 16.591  32.247  1.00 38.56 ? 109 GLU A CD  1 
ATOM   917  O OE1 . GLU A 1 109 ? 29.629 15.397  32.231  1.00 43.60 ? 109 GLU A OE1 1 
ATOM   918  O OE2 . GLU A 1 109 ? 30.158 17.248  33.301  1.00 46.42 ? 109 GLU A OE2 1 
ATOM   919  N N   . LEU A 1 110 ? 29.104 15.903  26.633  1.00 21.94 ? 110 LEU A N   1 
ATOM   920  C CA  . LEU A 1 110 ? 29.055 15.014  25.480  1.00 20.99 ? 110 LEU A CA  1 
ATOM   921  C C   . LEU A 1 110 ? 29.684 15.694  24.256  1.00 20.41 ? 110 LEU A C   1 
ATOM   922  O O   . LEU A 1 110 ? 30.423 15.072  23.498  1.00 20.96 ? 110 LEU A O   1 
ATOM   923  C CB  . LEU A 1 110 ? 27.600 14.606  25.233  1.00 20.84 ? 110 LEU A CB  1 
ATOM   924  C CG  . LEU A 1 110 ? 27.344 13.700  24.033  1.00 21.30 ? 110 LEU A CG  1 
ATOM   925  C CD1 . LEU A 1 110 ? 28.183 12.438  24.109  1.00 22.56 ? 110 LEU A CD1 1 
ATOM   926  C CD2 . LEU A 1 110 ? 25.872 13.333  23.952  1.00 22.01 ? 110 LEU A CD2 1 
ATOM   927  N N   . GLU A 1 111 ? 29.392 16.986  24.049  1.00 20.43 ? 111 GLU A N   1 
ATOM   928  C CA  . GLU A 1 111 ? 29.975 17.716  22.935  1.00 20.74 ? 111 GLU A CA  1 
ATOM   929  C C   . GLU A 1 111 ? 31.498 17.705  23.072  1.00 22.48 ? 111 GLU A C   1 
ATOM   930  O O   . GLU A 1 111 ? 32.206 17.574  22.076  1.00 22.77 ? 111 GLU A O   1 
ATOM   931  C CB  . GLU A 1 111 ? 29.398 19.133  22.903  1.00 22.17 ? 111 GLU A CB  1 
ATOM   932  C CG  . GLU A 1 111 ? 29.923 20.011  21.776  1.00 25.66 ? 111 GLU A CG  1 
ATOM   933  C CD  . GLU A 1 111 ? 29.567 21.487  21.895  1.00 33.25 ? 111 GLU A CD  1 
ATOM   934  O OE1 . GLU A 1 111 ? 29.672 22.032  23.016  1.00 37.51 ? 111 GLU A OE1 1 
ATOM   935  O OE2 . GLU A 1 111 ? 29.248 22.117  20.860  1.00 38.40 ? 111 GLU A OE2 1 
ATOM   936  N N   . ARG A 1 112 ? 32.004 17.859  24.310  1.00 23.44 ? 112 ARG A N   1 
ATOM   937  C CA  . ARG A 1 112 ? 33.446 17.818  24.535  1.00 25.59 ? 112 ARG A CA  1 
ATOM   938  C C   . ARG A 1 112 ? 34.034 16.456  24.144  1.00 25.01 ? 112 ARG A C   1 
ATOM   939  O O   . ARG A 1 112 ? 35.078 16.408  23.505  1.00 25.30 ? 112 ARG A O   1 
ATOM   940  C CB  . ARG A 1 112 ? 33.773 18.169  25.991  1.00 30.65 ? 112 ARG A CB  1 
ATOM   941  C CG  . ARG A 1 112 ? 35.261 18.296  26.290  1.00 36.08 ? 112 ARG A CG  1 
ATOM   942  C CD  . ARG A 1 112 ? 35.517 18.600  27.754  1.00 41.74 ? 112 ARG A CD  1 
ATOM   943  N NE  . ARG A 1 112 ? 34.631 19.653  28.227  1.00 48.06 ? 112 ARG A NE  1 
ATOM   944  C CZ  . ARG A 1 112 ? 34.977 20.924  28.408  1.00 54.00 ? 112 ARG A CZ  1 
ATOM   945  N NH1 . ARG A 1 112 ? 36.233 21.313  28.255  1.00 58.50 ? 112 ARG A NH1 1 
ATOM   946  N NH2 . ARG A 1 112 ? 34.057 21.807  28.755  1.00 57.88 ? 112 ARG A NH2 1 
ATOM   947  N N   A LEU A 1 113 ? 33.357 15.364  24.531  0.50 23.90 ? 113 LEU A N   1 
ATOM   948  N N   B LEU A 1 113 ? 33.364 15.365  24.542  0.50 24.63 ? 113 LEU A N   1 
ATOM   949  C CA  A LEU A 1 113 ? 33.818 14.024  24.203  0.50 23.55 ? 113 LEU A CA  1 
ATOM   950  C CA  B LEU A 1 113 ? 33.808 14.020  24.206  0.50 24.73 ? 113 LEU A CA  1 
ATOM   951  C C   A LEU A 1 113 ? 33.864 13.834  22.689  0.50 22.38 ? 113 LEU A C   1 
ATOM   952  C C   B LEU A 1 113 ? 33.860 13.831  22.691  0.50 22.83 ? 113 LEU A C   1 
ATOM   953  O O   A LEU A 1 113 ? 34.812 13.258  22.166  0.50 21.62 ? 113 LEU A O   1 
ATOM   954  O O   B LEU A 1 113 ? 34.811 13.258  22.171  0.50 21.86 ? 113 LEU A O   1 
ATOM   955  C CB  A LEU A 1 113 ? 32.882 12.978  24.821  0.50 23.93 ? 113 LEU A CB  1 
ATOM   956  C CB  B LEU A 1 113 ? 32.853 12.996  24.830  0.50 26.69 ? 113 LEU A CB  1 
ATOM   957  C CG  A LEU A 1 113 ? 33.028 12.743  26.321  0.50 25.51 ? 113 LEU A CG  1 
ATOM   958  C CG  B LEU A 1 113 ? 33.426 12.130  25.949  0.50 29.87 ? 113 LEU A CG  1 
ATOM   959  C CD1 A LEU A 1 113 ? 32.012 11.712  26.794  0.50 26.17 ? 113 LEU A CD1 1 
ATOM   960  C CD1 B LEU A 1 113 ? 34.561 12.838  26.670  0.50 31.21 ? 113 LEU A CD1 1 
ATOM   961  C CD2 A LEU A 1 113 ? 34.440 12.286  26.659  0.50 25.82 ? 113 LEU A CD2 1 
ATOM   962  C CD2 B LEU A 1 113 ? 32.328 11.747  26.930  0.50 31.10 ? 113 LEU A CD2 1 
ATOM   963  N N   . ILE A 1 114 ? 32.814 14.284  21.993  1.00 20.61 ? 114 ILE A N   1 
ATOM   964  C CA  . ILE A 1 114 ? 32.730 14.117  20.553  1.00 19.89 ? 114 ILE A CA  1 
ATOM   965  C C   . ILE A 1 114 ? 33.855 14.907  19.886  1.00 20.77 ? 114 ILE A C   1 
ATOM   966  O O   . ILE A 1 114 ? 34.557 14.399  19.016  1.00 20.91 ? 114 ILE A O   1 
ATOM   967  C CB  . ILE A 1 114 ? 31.351 14.544  20.017  1.00 20.38 ? 114 ILE A CB  1 
ATOM   968  C CG1 . ILE A 1 114 ? 30.217 13.666  20.554  1.00 20.50 ? 114 ILE A CG1 1 
ATOM   969  C CG2 . ILE A 1 114 ? 31.360 14.563  18.500  1.00 22.96 ? 114 ILE A CG2 1 
ATOM   970  C CD1 . ILE A 1 114 ? 28.883 14.334  20.502  1.00 19.70 ? 114 ILE A CD1 1 
ATOM   971  N N   . ASP A 1 115 ? 34.022 16.163  20.326  1.00 21.86 ? 115 ASP A N   1 
ATOM   972  C CA  . ASP A 1 115 ? 35.028 17.046  19.768  1.00 23.93 ? 115 ASP A CA  1 
ATOM   973  C C   . ASP A 1 115 ? 36.420 16.433  19.911  1.00 24.24 ? 115 ASP A C   1 
ATOM   974  O O   . ASP A 1 115 ? 37.200 16.409  18.960  1.00 24.56 ? 115 ASP A O   1 
ATOM   975  C CB  . ASP A 1 115 ? 34.979 18.414  20.457  1.00 27.14 ? 115 ASP A CB  1 
ATOM   976  C CG  . ASP A 1 115 ? 36.135 19.318  20.056  1.00 32.96 ? 115 ASP A CG  1 
ATOM   977  O OD1 . ASP A 1 115 ? 36.108 19.825  18.921  1.00 36.95 ? 115 ASP A OD1 1 
ATOM   978  O OD2 . ASP A 1 115 ? 37.080 19.479  20.869  1.00 37.65 ? 115 ASP A OD2 1 
ATOM   979  N N   . LYS A 1 116 ? 36.733 15.969  21.119  1.00 24.15 ? 116 LYS A N   1 
ATOM   980  C CA  . LYS A 1 116 ? 38.037 15.388  21.400  1.00 25.35 ? 116 LYS A CA  1 
ATOM   981  C C   . LYS A 1 116 ? 38.305 14.168  20.527  1.00 24.57 ? 116 LYS A C   1 
ATOM   982  O O   . LYS A 1 116 ? 39.406 13.989  20.014  1.00 25.40 ? 116 LYS A O   1 
ATOM   983  C CB  . LYS A 1 116 ? 38.133 15.050  22.883  1.00 30.29 ? 116 LYS A CB  1 
ATOM   984  C CG  . LYS A 1 116 ? 38.345 16.240  23.810  1.00 36.16 ? 116 LYS A CG  1 
ATOM   985  C CD  . LYS A 1 116 ? 38.345 15.836  25.271  1.00 42.18 ? 116 LYS A CD  1 
ATOM   986  C CE  . LYS A 1 116 ? 39.022 14.500  25.518  1.00 45.67 ? 116 LYS A CE  1 
ATOM   987  N NZ  . LYS A 1 116 ? 39.126 14.186  26.961  1.00 49.59 ? 116 LYS A NZ  1 
ATOM   988  N N   . ALA A 1 117 ? 37.312 13.289  20.420  1.00 22.40 ? 117 ALA A N   1 
ATOM   989  C CA  . ALA A 1 117 ? 37.461 12.103  19.586  1.00 22.99 ? 117 ALA A CA  1 
ATOM   990  C C   . ALA A 1 117 ? 37.675 12.469  18.117  1.00 24.61 ? 117 ALA A C   1 
ATOM   991  O O   . ALA A 1 117 ? 38.501 11.859  17.437  1.00 24.70 ? 117 ALA A O   1 
ATOM   992  C CB  . ALA A 1 117 ? 36.245 11.237  19.731  1.00 24.35 ? 117 ALA A CB  1 
ATOM   993  N N   . MET A 1 118 ? 36.889 13.437  17.629  1.00 24.59 ? 118 MET A N   1 
ATOM   994  C CA  . MET A 1 118 ? 36.974 13.928  16.262  1.00 27.24 ? 118 MET A CA  1 
ATOM   995  C C   . MET A 1 118 ? 38.386 14.398  15.944  1.00 25.83 ? 118 MET A C   1 
ATOM   996  O O   . MET A 1 118 ? 38.901 14.154  14.856  1.00 30.31 ? 118 MET A O   1 
ATOM   997  C CB  . MET A 1 118 ? 36.049 15.126  16.054  1.00 32.11 ? 118 MET A CB  1 
ATOM   998  C CG  . MET A 1 118 ? 35.106 14.967  14.923  1.00 35.87 ? 118 MET A CG  1 
ATOM   999  S SD  . MET A 1 118 ? 33.802 16.194  15.103  1.00 45.26 ? 118 MET A SD  1 
ATOM   1000 C CE  . MET A 1 118 ? 34.527 17.593  14.252  1.00 47.87 ? 118 MET A CE  1 
ATOM   1001 N N   . LYS A 1 119 ? 38.997 15.070  16.917  1.00 24.63 ? 119 LYS A N   1 
ATOM   1002 C CA  . LYS A 1 119 ? 40.298 15.681  16.738  1.00 26.26 ? 119 LYS A CA  1 
ATOM   1003 C C   . LYS A 1 119 ? 41.413 14.706  17.110  1.00 25.41 ? 119 LYS A C   1 
ATOM   1004 O O   . LYS A 1 119 ? 42.584 15.069  17.046  1.00 27.86 ? 119 LYS A O   1 
ATOM   1005 C CB  . LYS A 1 119 ? 40.346 16.949  17.583  1.00 26.69 ? 119 LYS A CB  1 
ATOM   1006 C CG  . LYS A 1 119 ? 39.419 18.052  17.073  1.00 27.83 ? 119 LYS A CG  1 
ATOM   1007 C CD  . LYS A 1 119 ? 39.361 19.271  17.970  1.00 31.63 ? 119 LYS A CD  1 
ATOM   1008 C CE  . LYS A 1 119 ? 38.709 20.483  17.327  1.00 37.75 ? 119 LYS A CE  1 
ATOM   1009 N NZ  . LYS A 1 119 ? 37.393 20.155  16.732  1.00 42.65 ? 119 LYS A NZ  1 
ATOM   1010 N N   . LYS A 1 120 ? 41.035 13.486  17.507  1.00 25.74 ? 120 LYS A N   1 
ATOM   1011 C CA  . LYS A 1 120 ? 41.973 12.449  17.915  1.00 25.11 ? 120 LYS A CA  1 
ATOM   1012 C C   . LYS A 1 120 ? 42.862 12.940  19.057  1.00 24.86 ? 120 LYS A C   1 
ATOM   1013 O O   . LYS A 1 120 ? 44.035 12.605  19.144  1.00 24.71 ? 120 LYS A O   1 
ATOM   1014 C CB  . LYS A 1 120 ? 42.767 11.935  16.709  1.00 28.07 ? 120 LYS A CB  1 
ATOM   1015 C CG  . LYS A 1 120 ? 41.936 11.152  15.702  1.00 31.23 ? 120 LYS A CG  1 
ATOM   1016 C CD  . LYS A 1 120 ? 42.756 10.212  14.834  1.00 34.80 ? 120 LYS A CD  1 
ATOM   1017 C CE  . LYS A 1 120 ? 41.942 9.095   14.218  1.00 39.44 ? 120 LYS A CE  1 
ATOM   1018 N NZ  . LYS A 1 120 ? 40.897 9.614   13.310  1.00 41.06 ? 120 LYS A NZ  1 
ATOM   1019 N N   . ASP A 1 121 ? 42.280 13.698  19.983  1.00 23.57 ? 121 ASP A N   1 
ATOM   1020 C CA  . ASP A 1 121 ? 43.016 14.098  21.173  1.00 27.78 ? 121 ASP A CA  1 
ATOM   1021 C C   . ASP A 1 121 ? 43.317 12.819  21.964  1.00 30.78 ? 121 ASP A C   1 
ATOM   1022 O O   . ASP A 1 121 ? 42.478 11.927  22.075  1.00 32.57 ? 121 ASP A O   1 
ATOM   1023 C CB  . ASP A 1 121 ? 42.233 15.115  22.004  1.00 28.82 ? 121 ASP A CB  1 
ATOM   1024 C CG  . ASP A 1 121 ? 42.041 16.519  21.416  1.00 30.27 ? 121 ASP A CG  1 
ATOM   1025 O OD1 . ASP A 1 121 ? 42.688 16.866  20.397  1.00 33.30 ? 121 ASP A OD1 1 
ATOM   1026 O OD2 . ASP A 1 121 ? 41.228 17.266  21.981  1.00 32.89 ? 121 ASP A OD2 1 
ATOM   1027 N N   . GLY A 1 122 ? 44.548 12.664  22.441  1.00 34.18 ? 122 GLY A N   1 
ATOM   1028 C CA  . GLY A 1 122 ? 44.913 11.440  23.156  1.00 33.78 ? 122 GLY A CA  1 
ATOM   1029 C C   . GLY A 1 122 ? 45.055 10.187  22.282  1.00 31.23 ? 122 GLY A C   1 
ATOM   1030 O O   . GLY A 1 122 ? 45.086 9.065   22.807  1.00 32.33 ? 122 GLY A O   1 
ATOM   1031 N N   . LEU A 1 123 ? 45.184 10.367  20.962  1.00 26.70 ? 123 LEU A N   1 
ATOM   1032 C CA  . LEU A 1 123 ? 45.785 9.338   20.117  1.00 22.49 ? 123 LEU A CA  1 
ATOM   1033 C C   . LEU A 1 123 ? 47.200 9.032   20.621  1.00 22.46 ? 123 LEU A C   1 
ATOM   1034 O O   . LEU A 1 123 ? 48.005 9.941   20.825  1.00 26.30 ? 123 LEU A O   1 
ATOM   1035 C CB  . LEU A 1 123 ? 45.791 9.832   18.665  1.00 22.45 ? 123 LEU A CB  1 
ATOM   1036 C CG  . LEU A 1 123 ? 46.261 8.857   17.588  1.00 23.30 ? 123 LEU A CG  1 
ATOM   1037 C CD1 . LEU A 1 123 ? 45.223 7.786   17.311  1.00 23.51 ? 123 LEU A CD1 1 
ATOM   1038 C CD2 . LEU A 1 123 ? 46.604 9.589   16.299  1.00 25.52 ? 123 LEU A CD2 1 
ATOM   1039 N N   . LEU A 1 124 ? 47.500 7.742   20.809  1.00 22.49 ? 124 LEU A N   1 
ATOM   1040 C CA  . LEU A 1 124 ? 48.739 7.306   21.447  1.00 24.25 ? 124 LEU A CA  1 
ATOM   1041 C C   . LEU A 1 124 ? 49.903 7.177   20.459  1.00 24.51 ? 124 LEU A C   1 
ATOM   1042 O O   . LEU A 1 124 ? 51.053 7.399   20.838  1.00 26.52 ? 124 LEU A O   1 
ATOM   1043 C CB  . LEU A 1 124 ? 48.509 5.968   22.153  1.00 26.12 ? 124 LEU A CB  1 
ATOM   1044 C CG  . LEU A 1 124 ? 47.442 5.949   23.246  1.00 29.34 ? 124 LEU A CG  1 
ATOM   1045 C CD1 . LEU A 1 124 ? 47.436 4.599   23.946  1.00 32.30 ? 124 LEU A CD1 1 
ATOM   1046 C CD2 . LEU A 1 124 ? 47.644 7.065   24.252  1.00 31.86 ? 124 LEU A CD2 1 
ATOM   1047 N N   . GLU A 1 125 ? 49.634 6.819   19.202  1.00 24.94 ? 125 GLU A N   1 
ATOM   1048 C CA  . GLU A 1 125 ? 50.714 6.551   18.256  1.00 28.56 ? 125 GLU A CA  1 
ATOM   1049 C C   . GLU A 1 125 ? 51.623 7.780   18.120  1.00 32.32 ? 125 GLU A C   1 
ATOM   1050 O O   . GLU A 1 125 ? 52.827 7.623   17.928  1.00 33.54 ? 125 GLU A O   1 
ATOM   1051 C CB  . GLU A 1 125 ? 50.156 6.044   16.918  1.00 33.51 ? 125 GLU A CB  1 
ATOM   1052 C CG  . GLU A 1 125 ? 49.271 7.036   16.192  1.00 37.33 ? 125 GLU A CG  1 
ATOM   1053 C CD  . GLU A 1 125 ? 48.454 6.493   15.030  1.00 43.06 ? 125 GLU A CD  1 
ATOM   1054 O OE1 . GLU A 1 125 ? 48.701 6.928   13.887  1.00 52.23 ? 125 GLU A OE1 1 
ATOM   1055 O OE2 . GLU A 1 125 ? 47.540 5.675   15.273  1.00 41.16 ? 125 GLU A OE2 1 
ATOM   1056 N N   . VAL A 1 126 ? 51.050 8.989   18.259  1.00 31.35 ? 126 VAL A N   1 
ATOM   1057 C CA  . VAL A 1 126 ? 51.783 10.252  18.192  1.00 33.26 ? 126 VAL A CA  1 
ATOM   1058 C C   . VAL A 1 126 ? 52.873 10.333  19.261  1.00 33.51 ? 126 VAL A C   1 
ATOM   1059 O O   . VAL A 1 126 ? 53.891 11.004  19.071  1.00 35.80 ? 126 VAL A O   1 
ATOM   1060 C CB  . VAL A 1 126 ? 50.825 11.460  18.333  1.00 34.46 ? 126 VAL A CB  1 
ATOM   1061 C CG1 . VAL A 1 126 ? 51.554 12.780  18.563  1.00 40.83 ? 126 VAL A CG1 1 
ATOM   1062 C CG2 . VAL A 1 126 ? 49.903 11.568  17.134  1.00 40.54 ? 126 VAL A CG2 1 
ATOM   1063 N N   . LEU A 1 127 ? 52.617 9.729   20.421  1.00 32.17 ? 127 LEU A N   1 
ATOM   1064 C CA  . LEU A 1 127 ? 53.487 9.847   21.578  1.00 29.98 ? 127 LEU A CA  1 
ATOM   1065 C C   . LEU A 1 127 ? 54.755 9.015   21.400  1.00 31.23 ? 127 LEU A C   1 
ATOM   1066 O O   . LEU A 1 127 ? 55.731 9.240   22.123  1.00 31.46 ? 127 LEU A O   1 
ATOM   1067 C CB  . LEU A 1 127 ? 52.722 9.407   22.831  1.00 32.41 ? 127 LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 127 ? 51.411 10.148  23.120  1.00 33.38 ? 127 LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 127 ? 50.784 9.629   24.407  1.00 35.07 ? 127 LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 127 ? 51.603 11.655  23.204  1.00 37.10 ? 127 LEU A CD2 1 
ATOM   1071 N N   . PHE A 1 128 ? 54.749 8.110   20.411  1.00 31.41 ? 128 PHE A N   1 
ATOM   1072 C CA  . PHE A 1 128 ? 55.835 7.162   20.228  1.00 30.15 ? 128 PHE A CA  1 
ATOM   1073 C C   . PHE A 1 128 ? 56.588 7.422   18.923  1.00 34.08 ? 128 PHE A C   1 
ATOM   1074 O O   . PHE A 1 128 ? 57.375 6.584   18.487  1.00 36.28 ? 128 PHE A O   1 
ATOM   1075 C CB  . PHE A 1 128 ? 55.271 5.737   20.297  1.00 28.98 ? 128 PHE A CB  1 
ATOM   1076 C CG  . PHE A 1 128 ? 54.543 5.449   21.584  1.00 27.57 ? 128 PHE A CG  1 
ATOM   1077 C CD1 . PHE A 1 128 ? 55.153 5.652   22.814  1.00 29.35 ? 128 PHE A CD1 1 
ATOM   1078 C CD2 . PHE A 1 128 ? 53.242 4.991   21.571  1.00 28.09 ? 128 PHE A CD2 1 
ATOM   1079 C CE1 . PHE A 1 128 ? 54.480 5.378   23.996  1.00 30.21 ? 128 PHE A CE1 1 
ATOM   1080 C CE2 . PHE A 1 128 ? 52.580 4.696   22.752  1.00 30.64 ? 128 PHE A CE2 1 
ATOM   1081 C CZ  . PHE A 1 128 ? 53.188 4.917   23.964  1.00 30.06 ? 128 PHE A CZ  1 
ATOM   1082 N N   . GLN A 1 129 ? 56.378 8.590   18.319  1.00 38.62 ? 129 GLN A N   1 
ATOM   1083 C CA  . GLN A 1 129 ? 57.099 8.975   17.117  1.00 42.77 ? 129 GLN A CA  1 
ATOM   1084 C C   . GLN A 1 129 ? 58.202 9.986   17.469  1.00 44.18 ? 129 GLN A C   1 
ATOM   1085 O O   . GLN A 1 129 ? 58.535 10.099  18.669  1.00 41.36 ? 129 GLN A O   1 
ATOM   1086 C CB  . GLN A 1 129 ? 56.128 9.567   16.094  1.00 47.61 ? 129 GLN A CB  1 
ATOM   1087 C CG  . GLN A 1 129 ? 56.821 10.088  14.845  1.00 54.58 ? 129 GLN A CG  1 
ATOM   1088 C CD  . GLN A 1 129 ? 55.893 10.252  13.668  1.00 62.41 ? 129 GLN A CD  1 
ATOM   1089 O OE1 . GLN A 1 129 ? 54.707 9.932   13.734  1.00 67.40 ? 129 GLN A OE1 1 
ATOM   1090 N NE2 . GLN A 1 129 ? 56.437 10.754  12.569  1.00 66.47 ? 129 GLN A NE2 1 
ATOM   1091 N N   . MET B 1 1   ? 29.924 0.012   -19.735 1.00 47.16 ? 1   MET B N   1 
ATOM   1092 C CA  . MET B 1 1   ? 30.169 1.416   -20.168 1.00 48.49 ? 1   MET B CA  1 
ATOM   1093 C C   . MET B 1 1   ? 31.436 1.963   -19.518 1.00 46.16 ? 1   MET B C   1 
ATOM   1094 O O   . MET B 1 1   ? 31.874 1.470   -18.489 1.00 52.09 ? 1   MET B O   1 
ATOM   1095 C CB  . MET B 1 1   ? 29.017 2.333   -19.755 1.00 50.48 ? 1   MET B CB  1 
ATOM   1096 C CG  . MET B 1 1   ? 27.737 2.065   -20.499 1.00 53.65 ? 1   MET B CG  1 
ATOM   1097 S SD  . MET B 1 1   ? 26.680 3.519   -20.591 1.00 51.95 ? 1   MET B SD  1 
ATOM   1098 C CE  . MET B 1 1   ? 27.199 4.475   -19.164 1.00 49.56 ? 1   MET B CE  1 
ATOM   1099 N N   . GLU B 1 2   ? 31.982 3.032   -20.105 1.00 46.90 ? 2   GLU B N   1 
ATOM   1100 C CA  . GLU B 1 2   ? 33.090 3.759   -19.505 1.00 48.65 ? 2   GLU B CA  1 
ATOM   1101 C C   . GLU B 1 2   ? 32.647 4.383   -18.181 1.00 48.72 ? 2   GLU B C   1 
ATOM   1102 O O   . GLU B 1 2   ? 31.513 4.842   -18.047 1.00 46.82 ? 2   GLU B O   1 
ATOM   1103 C CB  . GLU B 1 2   ? 33.592 4.846   -20.455 1.00 53.22 ? 2   GLU B CB  1 
ATOM   1104 C CG  . GLU B 1 2   ? 34.881 5.514   -20.000 1.00 59.30 ? 2   GLU B CG  1 
ATOM   1105 C CD  . GLU B 1 2   ? 36.139 4.680   -20.176 1.00 64.86 ? 2   GLU B CD  1 
ATOM   1106 O OE1 . GLU B 1 2   ? 36.209 3.568   -19.601 1.00 69.78 ? 2   GLU B OE1 1 
ATOM   1107 O OE2 . GLU B 1 2   ? 37.055 5.145   -20.887 1.00 69.97 ? 2   GLU B OE2 1 
ATOM   1108 N N   . ALA B 1 3   ? 33.590 4.449   -17.234 1.00 51.91 ? 3   ALA B N   1 
ATOM   1109 C CA  . ALA B 1 3   ? 33.318 4.825   -15.854 1.00 55.12 ? 3   ALA B CA  1 
ATOM   1110 C C   . ALA B 1 3   ? 32.734 6.231   -15.744 1.00 54.75 ? 3   ALA B C   1 
ATOM   1111 O O   . ALA B 1 3   ? 31.660 6.387   -15.172 1.00 58.01 ? 3   ALA B O   1 
ATOM   1112 C CB  . ALA B 1 3   ? 34.584 4.703   -15.047 1.00 56.45 ? 3   ALA B CB  1 
ATOM   1113 N N   . VAL B 1 4   ? 33.444 7.241   -16.269 1.00 52.48 ? 4   VAL B N   1 
ATOM   1114 C CA  . VAL B 1 4   ? 33.073 8.638   -16.069 1.00 49.97 ? 4   VAL B CA  1 
ATOM   1115 C C   . VAL B 1 4   ? 31.718 8.918   -16.725 1.00 44.56 ? 4   VAL B C   1 
ATOM   1116 O O   . VAL B 1 4   ? 30.934 9.734   -16.240 1.00 43.63 ? 4   VAL B O   1 
ATOM   1117 C CB  . VAL B 1 4   ? 34.152 9.604   -16.601 1.00 53.01 ? 4   VAL B CB  1 
ATOM   1118 C CG1 . VAL B 1 4   ? 33.749 11.061  -16.413 1.00 54.27 ? 4   VAL B CG1 1 
ATOM   1119 C CG2 . VAL B 1 4   ? 35.514 9.341   -15.976 1.00 55.67 ? 4   VAL B CG2 1 
ATOM   1120 N N   . LEU B 1 5   ? 31.441 8.238   -17.840 1.00 39.08 ? 5   LEU B N   1 
ATOM   1121 C CA  . LEU B 1 5   ? 30.145 8.355   -18.486 1.00 32.51 ? 5   LEU B CA  1 
ATOM   1122 C C   . LEU B 1 5   ? 29.060 7.802   -17.563 1.00 32.45 ? 5   LEU B C   1 
ATOM   1123 O O   . LEU B 1 5   ? 27.977 8.373   -17.450 1.00 29.14 ? 5   LEU B O   1 
ATOM   1124 C CB  . LEU B 1 5   ? 30.192 7.591   -19.809 1.00 29.68 ? 5   LEU B CB  1 
ATOM   1125 C CG  . LEU B 1 5   ? 28.921 7.630   -20.653 1.00 26.27 ? 5   LEU B CG  1 
ATOM   1126 C CD1 . LEU B 1 5   ? 28.552 9.052   -21.058 1.00 26.21 ? 5   LEU B CD1 1 
ATOM   1127 C CD2 . LEU B 1 5   ? 29.097 6.772   -21.897 1.00 25.37 ? 5   LEU B CD2 1 
ATOM   1128 N N   . ASN B 1 6   ? 29.363 6.684   -16.894 1.00 34.62 ? 6   ASN B N   1 
ATOM   1129 C CA  . ASN B 1 6   ? 28.374 6.010   -16.070 1.00 36.32 ? 6   ASN B CA  1 
ATOM   1130 C C   . ASN B 1 6   ? 27.928 6.932   -14.931 1.00 36.90 ? 6   ASN B C   1 
ATOM   1131 O O   . ASN B 1 6   ? 26.764 6.920   -14.538 1.00 35.90 ? 6   ASN B O   1 
ATOM   1132 C CB  . ASN B 1 6   ? 28.888 4.661   -15.565 1.00 39.86 ? 6   ASN B CB  1 
ATOM   1133 C CG  . ASN B 1 6   ? 27.782 3.840   -14.943 1.00 43.63 ? 6   ASN B CG  1 
ATOM   1134 O OD1 . ASN B 1 6   ? 26.808 3.506   -15.617 1.00 49.03 ? 6   ASN B OD1 1 
ATOM   1135 N ND2 . ASN B 1 6   ? 27.894 3.560   -13.656 1.00 47.77 ? 6   ASN B ND2 1 
ATOM   1136 N N   . GLU B 1 7   ? 28.855 7.752   -14.422 1.00 38.13 ? 7   GLU B N   1 
ATOM   1137 C CA  . GLU B 1 7   ? 28.551 8.658   -13.324 1.00 39.84 ? 7   GLU B CA  1 
ATOM   1138 C C   . GLU B 1 7   ? 27.633 9.782   -13.825 1.00 36.75 ? 7   GLU B C   1 
ATOM   1139 O O   . GLU B 1 7   ? 26.656 10.119  -13.156 1.00 35.33 ? 7   GLU B O   1 
ATOM   1140 C CB  . GLU B 1 7   ? 29.820 9.240   -12.686 1.00 45.37 ? 7   GLU B CB  1 
ATOM   1141 C CG  . GLU B 1 7   ? 31.088 8.413   -12.872 1.00 51.70 ? 7   GLU B CG  1 
ATOM   1142 C CD  . GLU B 1 7   ? 31.344 7.286   -11.884 1.00 57.87 ? 7   GLU B CD  1 
ATOM   1143 O OE1 . GLU B 1 7   ? 31.653 7.590   -10.707 1.00 63.99 ? 7   GLU B OE1 1 
ATOM   1144 O OE2 . GLU B 1 7   ? 31.272 6.106   -12.296 1.00 61.33 ? 7   GLU B OE2 1 
ATOM   1145 N N   . LEU B 1 8   ? 27.914 10.364  -15.002 1.00 33.21 ? 8   LEU B N   1 
ATOM   1146 C CA  . LEU B 1 8   ? 27.098 11.488  -15.440 1.00 33.79 ? 8   LEU B CA  1 
ATOM   1147 C C   . LEU B 1 8   ? 25.695 11.004  -15.813 1.00 29.52 ? 8   LEU B C   1 
ATOM   1148 O O   . LEU B 1 8   ? 24.727 11.710  -15.542 1.00 29.56 ? 8   LEU B O   1 
ATOM   1149 C CB  . LEU B 1 8   ? 27.789 12.309  -16.543 1.00 37.79 ? 8   LEU B CB  1 
ATOM   1150 C CG  . LEU B 1 8   ? 27.825 11.752  -17.964 1.00 39.45 ? 8   LEU B CG  1 
ATOM   1151 C CD1 . LEU B 1 8   ? 26.568 12.125  -18.729 1.00 40.65 ? 8   LEU B CD1 1 
ATOM   1152 C CD2 . LEU B 1 8   ? 29.047 12.266  -18.708 1.00 41.47 ? 8   LEU B CD2 1 
ATOM   1153 N N   . VAL B 1 9   ? 25.560 9.814   -16.419 1.00 27.19 ? 9   VAL B N   1 
ATOM   1154 C CA  . VAL B 1 9   ? 24.229 9.321   -16.774 1.00 25.78 ? 9   VAL B CA  1 
ATOM   1155 C C   . VAL B 1 9   ? 23.451 8.977   -15.501 1.00 25.69 ? 9   VAL B C   1 
ATOM   1156 O O   . VAL B 1 9   ? 22.238 9.175   -15.438 1.00 24.75 ? 9   VAL B O   1 
ATOM   1157 C CB  . VAL B 1 9   ? 24.251 8.143   -17.775 1.00 26.97 ? 9   VAL B CB  1 
ATOM   1158 C CG1 . VAL B 1 9   ? 24.920 8.549   -19.075 1.00 25.88 ? 9   VAL B CG1 1 
ATOM   1159 C CG2 . VAL B 1 9   ? 24.877 6.872   -17.222 1.00 28.19 ? 9   VAL B CG2 1 
ATOM   1160 N N   . SER B 1 10  ? 24.165 8.493   -14.477 1.00 26.90 ? 10  SER B N   1 
ATOM   1161 C CA  . SER B 1 10  ? 23.559 8.192   -13.189 1.00 26.67 ? 10  SER B CA  1 
ATOM   1162 C C   . SER B 1 10  ? 22.946 9.435   -12.554 1.00 26.31 ? 10  SER B C   1 
ATOM   1163 O O   . SER B 1 10  ? 21.854 9.368   -12.003 1.00 27.33 ? 10  SER B O   1 
ATOM   1164 C CB  . SER B 1 10  ? 24.557 7.535   -12.261 1.00 29.70 ? 10  SER B CB  1 
ATOM   1165 O OG  . SER B 1 10  ? 24.861 6.223   -12.707 1.00 34.79 ? 10  SER B OG  1 
ATOM   1166 N N   . VAL B 1 11  ? 23.642 10.575  -12.649 1.00 25.82 ? 11  VAL B N   1 
ATOM   1167 C CA  . VAL B 1 11  ? 23.147 11.800  -12.047 1.00 27.42 ? 11  VAL B CA  1 
ATOM   1168 C C   . VAL B 1 11  ? 21.946 12.319  -12.839 1.00 26.76 ? 11  VAL B C   1 
ATOM   1169 O O   . VAL B 1 11  ? 20.983 12.820  -12.253 1.00 24.65 ? 11  VAL B O   1 
ATOM   1170 C CB  . VAL B 1 11  ? 24.272 12.849  -11.935 1.00 29.71 ? 11  VAL B CB  1 
ATOM   1171 C CG1 . VAL B 1 11  ? 23.761 14.182  -11.402 1.00 30.41 ? 11  VAL B CG1 1 
ATOM   1172 C CG2 . VAL B 1 11  ? 25.427 12.337  -11.079 1.00 31.43 ? 11  VAL B CG2 1 
ATOM   1173 N N   . GLU B 1 12  ? 22.012 12.247  -14.175 1.00 26.07 ? 12  GLU B N   1 
ATOM   1174 C CA  . GLU B 1 12  ? 20.885 12.662  -14.996 1.00 25.47 ? 12  GLU B CA  1 
ATOM   1175 C C   . GLU B 1 12  ? 19.645 11.854  -14.604 1.00 22.47 ? 12  GLU B C   1 
ATOM   1176 O O   . GLU B 1 12  ? 18.571 12.406  -14.449 1.00 23.80 ? 12  GLU B O   1 
ATOM   1177 C CB  . GLU B 1 12  ? 21.208 12.507  -16.483 1.00 27.98 ? 12  GLU B CB  1 
ATOM   1178 C CG  . GLU B 1 12  ? 20.250 13.240  -17.410 1.00 32.86 ? 12  GLU B CG  1 
ATOM   1179 C CD  . GLU B 1 12  ? 20.279 14.761  -17.385 1.00 35.15 ? 12  GLU B CD  1 
ATOM   1180 O OE1 . GLU B 1 12  ? 21.087 15.350  -16.632 1.00 40.00 ? 12  GLU B OE1 1 
ATOM   1181 O OE2 . GLU B 1 12  ? 19.503 15.365  -18.141 1.00 41.91 ? 12  GLU B OE2 1 
ATOM   1182 N N   . ASP B 1 13  ? 19.797 10.541  -14.418 1.00 22.52 ? 13  ASP B N   1 
ATOM   1183 C CA  . ASP B 1 13  ? 18.668 9.699   -14.062 1.00 22.92 ? 13  ASP B CA  1 
ATOM   1184 C C   . ASP B 1 13  ? 18.184 10.019  -12.645 1.00 22.68 ? 13  ASP B C   1 
ATOM   1185 O O   . ASP B 1 13  ? 16.987 9.966   -12.368 1.00 22.99 ? 13  ASP B O   1 
ATOM   1186 C CB  . ASP B 1 13  ? 19.036 8.215   -14.171 1.00 22.75 ? 13  ASP B CB  1 
ATOM   1187 C CG  . ASP B 1 13  ? 19.291 7.683   -15.575 1.00 24.44 ? 13  ASP B CG  1 
ATOM   1188 O OD1 . ASP B 1 13  ? 18.978 8.401   -16.557 1.00 24.98 ? 13  ASP B OD1 1 
ATOM   1189 O OD2 . ASP B 1 13  ? 19.858 6.557   -15.683 1.00 24.86 ? 13  ASP B OD2 1 
ATOM   1190 N N   . LEU B 1 14  ? 19.123 10.344  -11.747 1.00 22.21 ? 14  LEU B N   1 
ATOM   1191 C CA  . LEU B 1 14  ? 18.785 10.662  -10.368 1.00 22.32 ? 14  LEU B CA  1 
ATOM   1192 C C   . LEU B 1 14  ? 17.908 11.912  -10.313 1.00 22.64 ? 14  LEU B C   1 
ATOM   1193 O O   . LEU B 1 14  ? 16.903 11.945  -9.621  1.00 22.40 ? 14  LEU B O   1 
ATOM   1194 C CB  . LEU B 1 14  ? 20.070 10.837  -9.556  1.00 23.38 ? 14  LEU B CB  1 
ATOM   1195 C CG  . LEU B 1 14  ? 19.878 11.356  -8.131  1.00 26.19 ? 14  LEU B CG  1 
ATOM   1196 C CD1 . LEU B 1 14  ? 19.159 10.313  -7.278  1.00 26.68 ? 14  LEU B CD1 1 
ATOM   1197 C CD2 . LEU B 1 14  ? 21.216 11.741  -7.508  1.00 28.57 ? 14  LEU B CD2 1 
ATOM   1198 N N   . LEU B 1 15  ? 18.303 12.949  -11.042 1.00 23.32 ? 15  LEU B N   1 
ATOM   1199 C CA  . LEU B 1 15  ? 17.563 14.199  -10.984 1.00 24.76 ? 15  LEU B CA  1 
ATOM   1200 C C   . LEU B 1 15  ? 16.152 13.994  -11.525 1.00 25.28 ? 15  LEU B C   1 
ATOM   1201 O O   . LEU B 1 15  ? 15.194 14.586  -11.011 1.00 25.15 ? 15  LEU B O   1 
ATOM   1202 C CB  . LEU B 1 15  ? 18.330 15.268  -11.764 1.00 28.05 ? 15  LEU B CB  1 
ATOM   1203 C CG  . LEU B 1 15  ? 19.650 15.693  -11.125 1.00 30.14 ? 15  LEU B CG  1 
ATOM   1204 C CD1 . LEU B 1 15  ? 20.444 16.568  -12.072 1.00 31.74 ? 15  LEU B CD1 1 
ATOM   1205 C CD2 . LEU B 1 15  ? 19.416 16.413  -9.806  1.00 32.86 ? 15  LEU B CD2 1 
ATOM   1206 N N   . LYS B 1 16  ? 16.027 13.142  -12.547 1.00 24.28 ? 16  LYS B N   1 
ATOM   1207 C CA  . LYS B 1 16  ? 14.719 12.847  -13.113 1.00 24.76 ? 16  LYS B CA  1 
ATOM   1208 C C   . LYS B 1 16  ? 13.866 12.102  -12.089 1.00 23.56 ? 16  LYS B C   1 
ATOM   1209 O O   . LYS B 1 16  ? 12.685 12.411  -11.912 1.00 23.92 ? 16  LYS B O   1 
ATOM   1210 C CB  . LYS B 1 16  ? 14.890 12.084  -14.425 1.00 24.07 ? 16  LYS B CB  1 
ATOM   1211 C CG  . LYS B 1 16  ? 13.614 11.524  -15.030 1.00 29.09 ? 16  LYS B CG  1 
ATOM   1212 C CD  . LYS B 1 16  ? 13.929 10.794  -16.297 1.00 30.83 ? 16  LYS B CD  1 
ATOM   1213 C CE  . LYS B 1 16  ? 12.937 9.728   -16.685 1.00 34.22 ? 16  LYS B CE  1 
ATOM   1214 N NZ  . LYS B 1 16  ? 13.530 8.853   -17.718 1.00 38.43 ? 16  LYS B NZ  1 
ATOM   1215 N N   . PHE B 1 17  ? 14.471 11.119  -11.410 1.00 21.53 ? 17  PHE B N   1 
ATOM   1216 C CA  . PHE B 1 17  ? 13.753 10.349  -10.411 1.00 22.55 ? 17  PHE B CA  1 
ATOM   1217 C C   . PHE B 1 17  ? 13.348 11.225  -9.229  1.00 22.54 ? 17  PHE B C   1 
ATOM   1218 O O   . PHE B 1 17  ? 12.263 11.050  -8.691  1.00 23.21 ? 17  PHE B O   1 
ATOM   1219 C CB  . PHE B 1 17  ? 14.579 9.163   -9.912  1.00 21.96 ? 17  PHE B CB  1 
ATOM   1220 C CG  . PHE B 1 17  ? 13.867 8.385   -8.844  1.00 22.46 ? 17  PHE B CG  1 
ATOM   1221 C CD1 . PHE B 1 17  ? 12.708 7.693   -9.152  1.00 23.49 ? 17  PHE B CD1 1 
ATOM   1222 C CD2 . PHE B 1 17  ? 14.294 8.415   -7.528  1.00 24.46 ? 17  PHE B CD2 1 
ATOM   1223 C CE1 . PHE B 1 17  ? 11.999 7.037   -8.166  1.00 23.52 ? 17  PHE B CE1 1 
ATOM   1224 C CE2 . PHE B 1 17  ? 13.604 7.716   -6.550  1.00 26.29 ? 17  PHE B CE2 1 
ATOM   1225 C CZ  . PHE B 1 17  ? 12.461 7.031   -6.875  1.00 24.64 ? 17  PHE B CZ  1 
ATOM   1226 N N   . GLU B 1 18  ? 14.225 12.152  -8.819  1.00 22.72 ? 18  GLU B N   1 
ATOM   1227 C CA  . GLU B 1 18  ? 13.888 13.104  -7.772  1.00 25.13 ? 18  GLU B CA  1 
ATOM   1228 C C   . GLU B 1 18  ? 12.570 13.798  -8.104  1.00 24.17 ? 18  GLU B C   1 
ATOM   1229 O O   . GLU B 1 18  ? 11.704 13.956  -7.247  1.00 24.88 ? 18  GLU B O   1 
ATOM   1230 C CB  . GLU B 1 18  ? 14.951 14.194  -7.667  1.00 28.39 ? 18  GLU B CB  1 
ATOM   1231 C CG  . GLU B 1 18  ? 16.117 13.901  -6.762  1.00 35.09 ? 18  GLU B CG  1 
ATOM   1232 C CD  . GLU B 1 18  ? 17.003 15.129  -6.614  1.00 42.33 ? 18  GLU B CD  1 
ATOM   1233 O OE1 . GLU B 1 18  ? 16.468 16.203  -6.233  1.00 45.66 ? 18  GLU B OE1 1 
ATOM   1234 O OE2 . GLU B 1 18  ? 18.211 15.034  -6.924  1.00 48.32 ? 18  GLU B OE2 1 
ATOM   1235 N N   . LYS B 1 19  ? 12.450 14.263  -9.350  1.00 24.99 ? 19  LYS B N   1 
ATOM   1236 C CA  . LYS B 1 19  ? 11.276 15.019  -9.768  1.00 26.47 ? 19  LYS B CA  1 
ATOM   1237 C C   . LYS B 1 19  ? 10.021 14.150  -9.698  1.00 26.67 ? 19  LYS B C   1 
ATOM   1238 O O   . LYS B 1 19  ? 8.963  14.626  -9.296  1.00 27.13 ? 19  LYS B O   1 
ATOM   1239 C CB  . LYS B 1 19  ? 11.490 15.569  -11.179 1.00 30.36 ? 19  LYS B CB  1 
ATOM   1240 C CG  . LYS B 1 19  ? 12.488 16.720  -11.247 1.00 33.59 ? 19  LYS B CG  1 
ATOM   1241 C CD  . LYS B 1 19  ? 12.643 17.323  -12.629 1.00 39.70 ? 19  LYS B CD  1 
ATOM   1242 C CE  . LYS B 1 19  ? 11.355 17.912  -13.157 1.00 44.62 ? 19  LYS B CE  1 
ATOM   1243 N NZ  . LYS B 1 19  ? 11.605 18.835  -14.290 1.00 49.56 ? 19  LYS B NZ  1 
ATOM   1244 N N   . LYS B 1 20  ? 10.148 12.894  -10.132 1.00 25.04 ? 20  LYS B N   1 
ATOM   1245 C CA  . LYS B 1 20  ? 9.064  11.916  -10.049 1.00 24.58 ? 20  LYS B CA  1 
ATOM   1246 C C   . LYS B 1 20  ? 8.625  11.724  -8.598  1.00 25.47 ? 20  LYS B C   1 
ATOM   1247 O O   . LYS B 1 20  ? 7.434  11.757  -8.285  1.00 25.72 ? 20  LYS B O   1 
ATOM   1248 C CB  . LYS B 1 20  ? 9.511  10.580  -10.651 1.00 25.66 ? 20  LYS B CB  1 
ATOM   1249 C CG  . LYS B 1 20  ? 8.483  9.456   -10.569 1.00 26.87 ? 20  LYS B CG  1 
ATOM   1250 C CD  . LYS B 1 20  ? 8.986  8.181   -11.175 1.00 30.47 ? 20  LYS B CD  1 
ATOM   1251 C CE  . LYS B 1 20  ? 8.100  7.003   -10.839 1.00 33.67 ? 20  LYS B CE  1 
ATOM   1252 N NZ  . LYS B 1 20  ? 8.559  5.762   -11.502 1.00 35.99 ? 20  LYS B NZ  1 
ATOM   1253 N N   . PHE B 1 21  ? 9.599  11.448  -7.727  1.00 24.67 ? 21  PHE B N   1 
ATOM   1254 C CA  . PHE B 1 21  ? 9.336  11.210  -6.319  1.00 26.07 ? 21  PHE B CA  1 
ATOM   1255 C C   . PHE B 1 21  ? 8.598  12.402  -5.711  1.00 26.97 ? 21  PHE B C   1 
ATOM   1256 O O   . PHE B 1 21  ? 7.590  12.218  -5.037  1.00 26.42 ? 21  PHE B O   1 
ATOM   1257 C CB  . PHE B 1 21  ? 10.653 10.913  -5.598  1.00 26.84 ? 21  PHE B CB  1 
ATOM   1258 C CG  . PHE B 1 21  ? 10.521 10.544  -4.147  1.00 29.53 ? 21  PHE B CG  1 
ATOM   1259 C CD1 . PHE B 1 21  ? 10.433 11.525  -3.170  1.00 30.34 ? 21  PHE B CD1 1 
ATOM   1260 C CD2 . PHE B 1 21  ? 10.451 9.216   -3.758  1.00 31.95 ? 21  PHE B CD2 1 
ATOM   1261 C CE1 . PHE B 1 21  ? 10.307 11.185  -1.833  1.00 32.50 ? 21  PHE B CE1 1 
ATOM   1262 C CE2 . PHE B 1 21  ? 10.322 8.880   -2.420  1.00 32.55 ? 21  PHE B CE2 1 
ATOM   1263 C CZ  . PHE B 1 21  ? 10.244 9.862   -1.463  1.00 33.23 ? 21  PHE B CZ  1 
ATOM   1264 N N   . GLN B 1 22  ? 9.098  13.622  -5.955  1.00 27.67 ? 22  GLN B N   1 
ATOM   1265 C CA  . GLN B 1 22  ? 8.508  14.816  -5.362  1.00 29.34 ? 22  GLN B CA  1 
ATOM   1266 C C   . GLN B 1 22  ? 7.093  15.053  -5.894  1.00 28.10 ? 22  GLN B C   1 
ATOM   1267 O O   . GLN B 1 22  ? 6.218  15.477  -5.148  1.00 28.41 ? 22  GLN B O   1 
ATOM   1268 C CB  . GLN B 1 22  ? 9.394  16.043  -5.596  1.00 29.45 ? 22  GLN B CB  1 
ATOM   1269 C CG  . GLN B 1 22  ? 10.704 16.028  -4.803  1.00 33.03 ? 22  GLN B CG  1 
ATOM   1270 C CD  . GLN B 1 22  ? 10.527 15.815  -3.313  1.00 37.39 ? 22  GLN B CD  1 
ATOM   1271 O OE1 . GLN B 1 22  ? 9.687  16.439  -2.664  1.00 38.67 ? 22  GLN B OE1 1 
ATOM   1272 N NE2 . GLN B 1 22  ? 11.323 14.919  -2.746  1.00 38.67 ? 22  GLN B NE2 1 
ATOM   1273 N N   A SER B 1 23  ? 6.871  14.757  -7.181  0.50 28.27 ? 23  SER B N   1 
ATOM   1274 N N   B SER B 1 23  ? 6.871  14.754  -7.179  0.50 28.44 ? 23  SER B N   1 
ATOM   1275 C CA  A SER B 1 23  ? 5.551  14.888  -7.781  0.50 28.17 ? 23  SER B CA  1 
ATOM   1276 C CA  B SER B 1 23  ? 5.553  14.888  -7.781  0.50 28.26 ? 23  SER B CA  1 
ATOM   1277 C C   A SER B 1 23  ? 4.548  13.933  -7.130  0.50 27.12 ? 23  SER B C   1 
ATOM   1278 C C   B SER B 1 23  ? 4.547  13.932  -7.136  0.50 27.21 ? 23  SER B C   1 
ATOM   1279 O O   A SER B 1 23  ? 3.404  14.298  -6.872  0.50 28.69 ? 23  SER B O   1 
ATOM   1280 O O   B SER B 1 23  ? 3.402  14.297  -6.881  0.50 28.75 ? 23  SER B O   1 
ATOM   1281 C CB  A SER B 1 23  ? 5.619  14.671  -9.268  0.50 30.36 ? 23  SER B CB  1 
ATOM   1282 C CB  B SER B 1 23  ? 5.636  14.680  -9.268  0.50 30.80 ? 23  SER B CB  1 
ATOM   1283 O OG  A SER B 1 23  ? 4.318  14.710  -9.840  0.50 35.02 ? 23  SER B OG  1 
ATOM   1284 O OG  B SER B 1 23  ? 6.500  15.638  -9.860  0.50 34.79 ? 23  SER B OG  1 
ATOM   1285 N N   . GLU B 1 24  ? 4.974  12.697  -6.869  1.00 26.14 ? 24  GLU B N   1 
ATOM   1286 C CA  . GLU B 1 24  ? 4.096  11.717  -6.245  1.00 26.89 ? 24  GLU B CA  1 
ATOM   1287 C C   . GLU B 1 24  ? 3.783  12.130  -4.811  1.00 26.46 ? 24  GLU B C   1 
ATOM   1288 O O   . GLU B 1 24  ? 2.650  12.007  -4.356  1.00 27.84 ? 24  GLU B O   1 
ATOM   1289 C CB  . GLU B 1 24  ? 4.730  10.327  -6.259  1.00 27.40 ? 24  GLU B CB  1 
ATOM   1290 C CG  . GLU B 1 24  ? 4.693  9.665   -7.629  1.00 29.14 ? 24  GLU B CG  1 
ATOM   1291 C CD  . GLU B 1 24  ? 4.981  8.170   -7.662  1.00 31.19 ? 24  GLU B CD  1 
ATOM   1292 O OE1 . GLU B 1 24  ? 4.931  7.514   -6.603  1.00 34.42 ? 24  GLU B OE1 1 
ATOM   1293 O OE2 . GLU B 1 24  ? 5.243  7.659   -8.758  1.00 36.23 ? 24  GLU B OE2 1 
ATOM   1294 N N   . LYS B 1 25  ? 4.795  12.634  -4.101  1.00 27.33 ? 25  LYS B N   1 
ATOM   1295 C CA  . LYS B 1 25  ? 4.589  13.073  -2.734  1.00 30.85 ? 25  LYS B CA  1 
ATOM   1296 C C   . LYS B 1 25  ? 3.568  14.213  -2.722  1.00 32.05 ? 25  LYS B C   1 
ATOM   1297 O O   . LYS B 1 25  ? 2.674  14.239  -1.878  1.00 35.82 ? 25  LYS B O   1 
ATOM   1298 C CB  . LYS B 1 25  ? 5.924  13.490  -2.110  1.00 35.25 ? 25  LYS B CB  1 
ATOM   1299 C CG  . LYS B 1 25  ? 6.075  13.086  -0.651  1.00 41.37 ? 25  LYS B CG  1 
ATOM   1300 C CD  . LYS B 1 25  ? 7.512  12.966  -0.181  1.00 45.58 ? 25  LYS B CD  1 
ATOM   1301 C CE  . LYS B 1 25  ? 8.029  14.214  0.497   1.00 48.63 ? 25  LYS B CE  1 
ATOM   1302 N NZ  . LYS B 1 25  ? 7.128  14.656  1.586   1.00 51.44 ? 25  LYS B NZ  1 
ATOM   1303 N N   . ALA B 1 26  ? 3.684  15.137  -3.687  1.00 30.32 ? 26  ALA B N   1 
ATOM   1304 C CA  . ALA B 1 26  ? 2.763  16.264  -3.799  1.00 31.39 ? 26  ALA B CA  1 
ATOM   1305 C C   . ALA B 1 26  ? 1.342  15.806  -4.145  1.00 32.08 ? 26  ALA B C   1 
ATOM   1306 O O   . ALA B 1 26  ? 0.366  16.463  -3.756  1.00 36.12 ? 26  ALA B O   1 
ATOM   1307 C CB  . ALA B 1 26  ? 3.272  17.242  -4.832  1.00 33.18 ? 26  ALA B CB  1 
ATOM   1308 N N   . ALA B 1 27  ? 1.239  14.712  -4.906  1.00 33.21 ? 27  ALA B N   1 
ATOM   1309 C CA  . ALA B 1 27  ? -0.042 14.165  -5.317  1.00 33.75 ? 27  ALA B CA  1 
ATOM   1310 C C   . ALA B 1 27  ? -0.696 13.402  -4.168  1.00 33.51 ? 27  ALA B C   1 
ATOM   1311 O O   . ALA B 1 27  ? -1.854 12.998  -4.280  1.00 33.43 ? 27  ALA B O   1 
ATOM   1312 C CB  . ALA B 1 27  ? 0.148  13.294  -6.530  1.00 35.36 ? 27  ALA B CB  1 
ATOM   1313 N N   . GLY B 1 28  ? 0.057  13.197  -3.078  1.00 32.11 ? 28  GLY B N   1 
ATOM   1314 C CA  . GLY B 1 28  ? -0.502 12.716  -1.825  1.00 34.71 ? 28  GLY B CA  1 
ATOM   1315 C C   . GLY B 1 28  ? -0.144 11.263  -1.505  1.00 35.96 ? 28  GLY B C   1 
ATOM   1316 O O   . GLY B 1 28  ? -0.583 10.740  -0.481  1.00 36.97 ? 28  GLY B O   1 
ATOM   1317 N N   . SER B 1 29  ? 0.638  10.602  -2.366  1.00 34.92 ? 29  SER B N   1 
ATOM   1318 C CA  . SER B 1 29  ? 1.028  9.222   -2.109  1.00 32.54 ? 29  SER B CA  1 
ATOM   1319 C C   . SER B 1 29  ? 2.224  8.820   -2.965  1.00 31.53 ? 29  SER B C   1 
ATOM   1320 O O   . SER B 1 29  ? 2.178  8.892   -4.196  1.00 32.29 ? 29  SER B O   1 
ATOM   1321 C CB  . SER B 1 29  ? -0.122 8.273   -2.327  1.00 33.14 ? 29  SER B CB  1 
ATOM   1322 O OG  . SER B 1 29  ? 0.299  6.917   -2.163  1.00 32.38 ? 29  SER B OG  1 
ATOM   1323 N N   . VAL B 1 30  ? 3.286  8.363   -2.293  1.00 30.41 ? 30  VAL B N   1 
ATOM   1324 C CA  . VAL B 1 30  ? 4.407  7.744   -2.979  1.00 28.42 ? 30  VAL B CA  1 
ATOM   1325 C C   . VAL B 1 30  ? 4.099  6.247   -3.068  1.00 28.65 ? 30  VAL B C   1 
ATOM   1326 O O   . VAL B 1 30  ? 3.931  5.582   -2.048  1.00 29.64 ? 30  VAL B O   1 
ATOM   1327 C CB  . VAL B 1 30  ? 5.743  8.022   -2.261  1.00 29.16 ? 30  VAL B CB  1 
ATOM   1328 C CG1 . VAL B 1 30  ? 6.908  7.291   -2.919  1.00 28.17 ? 30  VAL B CG1 1 
ATOM   1329 C CG2 . VAL B 1 30  ? 6.039  9.511   -2.162  1.00 30.55 ? 30  VAL B CG2 1 
ATOM   1330 N N   . SER B 1 31  ? 4.013  5.736   -4.301  1.00 29.17 ? 31  SER B N   1 
ATOM   1331 C CA  . SER B 1 31  ? 3.563  4.379   -4.567  1.00 28.67 ? 31  SER B CA  1 
ATOM   1332 C C   . SER B 1 31  ? 4.619  3.378   -4.106  1.00 27.47 ? 31  SER B C   1 
ATOM   1333 O O   . SER B 1 31  ? 5.793  3.722   -3.966  1.00 27.90 ? 31  SER B O   1 
ATOM   1334 C CB  . SER B 1 31  ? 3.274  4.193   -6.028  1.00 30.70 ? 31  SER B CB  1 
ATOM   1335 O OG  . SER B 1 31  ? 4.480  4.214   -6.780  1.00 30.38 ? 31  SER B OG  1 
ATOM   1336 N N   . LYS B 1 32  ? 4.206  2.117   -3.934  1.00 28.85 ? 32  LYS B N   1 
ATOM   1337 C CA  . LYS B 1 32  ? 5.144  1.087   -3.515  1.00 30.47 ? 32  LYS B CA  1 
ATOM   1338 C C   . LYS B 1 32  ? 6.239  0.884   -4.569  1.00 27.84 ? 32  LYS B C   1 
ATOM   1339 O O   . LYS B 1 32  ? 7.377  0.571   -4.219  1.00 26.96 ? 32  LYS B O   1 
ATOM   1340 C CB  . LYS B 1 32  ? 4.406  -0.213  -3.173  1.00 32.01 ? 32  LYS B CB  1 
ATOM   1341 C CG  . LYS B 1 32  ? 3.717  -0.926  -4.333  1.00 34.64 ? 32  LYS B CG  1 
ATOM   1342 C CD  . LYS B 1 32  ? 2.822  -2.088  -3.906  1.00 37.45 ? 32  LYS B CD  1 
ATOM   1343 C CE  . LYS B 1 32  ? 3.494  -3.026  -2.930  1.00 38.45 ? 32  LYS B CE  1 
ATOM   1344 N NZ  . LYS B 1 32  ? 2.688  -4.246  -2.676  1.00 38.74 ? 32  LYS B NZ  1 
ATOM   1345 N N   A SER B 1 33  ? 5.896  1.065   -5.852  0.50 27.18 ? 33  SER B N   1 
ATOM   1346 N N   B SER B 1 33  ? 5.887  1.059   -5.852  0.50 26.68 ? 33  SER B N   1 
ATOM   1347 C CA  A SER B 1 33  ? 6.870  0.961   -6.928  0.50 26.75 ? 33  SER B CA  1 
ATOM   1348 C CA  B SER B 1 33  ? 6.851  0.979   -6.938  0.50 25.90 ? 33  SER B CA  1 
ATOM   1349 C C   A SER B 1 33  ? 7.928  2.058   -6.808  0.50 25.64 ? 33  SER B C   1 
ATOM   1350 C C   B SER B 1 33  ? 7.928  2.051   -6.779  0.50 25.32 ? 33  SER B C   1 
ATOM   1351 O O   A SER B 1 33  ? 9.115  1.803   -6.992  0.50 25.93 ? 33  SER B O   1 
ATOM   1352 O O   B SER B 1 33  ? 9.117  1.774   -6.913  0.50 25.85 ? 33  SER B O   1 
ATOM   1353 C CB  A SER B 1 33  ? 6.189  1.006   -8.270  0.50 29.27 ? 33  SER B CB  1 
ATOM   1354 C CB  B SER B 1 33  ? 6.171  1.116   -8.275  0.50 27.21 ? 33  SER B CB  1 
ATOM   1355 O OG  A SER B 1 33  ? 5.259  2.073   -8.331  0.50 32.52 ? 33  SER B OG  1 
ATOM   1356 O OG  B SER B 1 33  ? 7.120  1.039   -9.329  0.50 29.26 ? 33  SER B OG  1 
ATOM   1357 N N   . THR B 1 34  ? 7.497  3.279   -6.483  1.00 24.58 ? 34  THR B N   1 
ATOM   1358 C CA  . THR B 1 34  ? 8.413  4.404   -6.389  1.00 24.43 ? 34  THR B CA  1 
ATOM   1359 C C   . THR B 1 34  ? 9.311  4.247   -5.159  1.00 23.57 ? 34  THR B C   1 
ATOM   1360 O O   . THR B 1 34  ? 10.485 4.598   -5.216  1.00 24.57 ? 34  THR B O   1 
ATOM   1361 C CB  . THR B 1 34  ? 7.617  5.708   -6.485  1.00 24.36 ? 34  THR B CB  1 
ATOM   1362 O OG1 . THR B 1 34  ? 6.992  5.667   -7.765  1.00 27.19 ? 34  THR B OG1 1 
ATOM   1363 C CG2 . THR B 1 34  ? 8.455  6.960   -6.344  1.00 23.78 ? 34  THR B CG2 1 
ATOM   1364 N N   . GLN B 1 35  ? 8.778  3.685   -4.065  1.00 24.70 ? 35  GLN B N   1 
ATOM   1365 C CA  . GLN B 1 35  ? 9.580  3.419   -2.876  1.00 23.43 ? 35  GLN B CA  1 
ATOM   1366 C C   . GLN B 1 35  ? 10.659 2.375   -3.175  1.00 22.10 ? 35  GLN B C   1 
ATOM   1367 O O   . GLN B 1 35  ? 11.797 2.498   -2.737  1.00 22.80 ? 35  GLN B O   1 
ATOM   1368 C CB  . GLN B 1 35  ? 8.694  2.972   -1.712  1.00 26.02 ? 35  GLN B CB  1 
ATOM   1369 C CG  . GLN B 1 35  ? 7.857  4.075   -1.094  1.00 28.20 ? 35  GLN B CG  1 
ATOM   1370 C CD  . GLN B 1 35  ? 7.418  3.664   0.290   1.00 32.67 ? 35  GLN B CD  1 
ATOM   1371 O OE1 . GLN B 1 35  ? 6.566  2.804   0.454   1.00 36.99 ? 35  GLN B OE1 1 
ATOM   1372 N NE2 . GLN B 1 35  ? 8.014  4.267   1.308   1.00 38.63 ? 35  GLN B NE2 1 
ATOM   1373 N N   . PHE B 1 36  ? 10.318 1.331   -3.934  1.00 21.61 ? 36  PHE B N   1 
ATOM   1374 C CA  . PHE B 1 36  ? 11.343 0.373   -4.317  1.00 22.96 ? 36  PHE B CA  1 
ATOM   1375 C C   . PHE B 1 36  ? 12.440 1.069   -5.127  1.00 22.53 ? 36  PHE B C   1 
ATOM   1376 O O   . PHE B 1 36  ? 13.622 0.828   -4.918  1.00 22.01 ? 36  PHE B O   1 
ATOM   1377 C CB  . PHE B 1 36  ? 10.735 -0.805  -5.079  1.00 23.71 ? 36  PHE B CB  1 
ATOM   1378 C CG  . PHE B 1 36  ? 11.780 -1.722  -5.658  1.00 24.28 ? 36  PHE B CG  1 
ATOM   1379 C CD1 . PHE B 1 36  ? 12.508 -2.567  -4.837  1.00 24.82 ? 36  PHE B CD1 1 
ATOM   1380 C CD2 . PHE B 1 36  ? 12.112 -1.652  -7.001  1.00 26.13 ? 36  PHE B CD2 1 
ATOM   1381 C CE1 . PHE B 1 36  ? 13.501 -3.377  -5.363  1.00 24.51 ? 36  PHE B CE1 1 
ATOM   1382 C CE2 . PHE B 1 36  ? 13.105 -2.462  -7.528  1.00 26.78 ? 36  PHE B CE2 1 
ATOM   1383 C CZ  . PHE B 1 36  ? 13.785 -3.337  -6.709  1.00 26.87 ? 36  PHE B CZ  1 
ATOM   1384 N N   . GLU B 1 37  ? 12.033 1.951   -6.046  1.00 21.88 ? 37  GLU B N   1 
ATOM   1385 C CA  . GLU B 1 37  ? 12.967 2.641   -6.919  1.00 21.47 ? 37  GLU B CA  1 
ATOM   1386 C C   . GLU B 1 37  ? 13.909 3.521   -6.094  1.00 20.95 ? 37  GLU B C   1 
ATOM   1387 O O   . GLU B 1 37  ? 15.098 3.620   -6.384  1.00 22.16 ? 37  GLU B O   1 
ATOM   1388 C CB  . GLU B 1 37  ? 12.195 3.438   -7.974  1.00 23.58 ? 37  GLU B CB  1 
ATOM   1389 C CG  . GLU B 1 37  ? 11.514 2.537   -8.990  1.00 27.91 ? 37  GLU B CG  1 
ATOM   1390 C CD  . GLU B 1 37  ? 10.528 3.199   -9.937  1.00 34.45 ? 37  GLU B CD  1 
ATOM   1391 O OE1 . GLU B 1 37  ? 10.542 4.436   -10.017 1.00 38.30 ? 37  GLU B OE1 1 
ATOM   1392 O OE2 . GLU B 1 37  ? 9.742  2.465   -10.591 1.00 40.83 ? 37  GLU B OE2 1 
ATOM   1393 N N   . GLU B 1 38  ? 13.367 4.157   -5.056  1.00 21.39 ? 38  GLU B N   1 
ATOM   1394 C CA  . GLU B 1 38  ? 14.189 4.892   -4.109  1.00 20.88 ? 38  GLU B CA  1 
ATOM   1395 C C   . GLU B 1 38  ? 15.220 3.970   -3.449  1.00 20.71 ? 38  GLU B C   1 
ATOM   1396 O O   . GLU B 1 38  ? 16.395 4.309   -3.364  1.00 21.65 ? 38  GLU B O   1 
ATOM   1397 C CB  . GLU B 1 38  ? 13.293 5.532   -3.055  1.00 22.76 ? 38  GLU B CB  1 
ATOM   1398 C CG  . GLU B 1 38  ? 14.064 6.249   -1.988  1.00 25.17 ? 38  GLU B CG  1 
ATOM   1399 C CD  . GLU B 1 38  ? 13.220 6.766   -0.840  1.00 27.24 ? 38  GLU B CD  1 
ATOM   1400 O OE1 . GLU B 1 38  ? 11.980 6.570   -0.859  1.00 29.92 ? 38  GLU B OE1 1 
ATOM   1401 O OE2 . GLU B 1 38  ? 13.817 7.321   0.089   1.00 30.45 ? 38  GLU B OE2 1 
ATOM   1402 N N   . ALA B 1 39  ? 14.776 2.810   -2.954  1.00 20.67 ? 39  ALA B N   1 
ATOM   1403 C CA  . ALA B 1 39  ? 15.713 1.871   -2.353  1.00 21.17 ? 39  ALA B CA  1 
ATOM   1404 C C   . ALA B 1 39  ? 16.754 1.403   -3.370  1.00 20.64 ? 39  ALA B C   1 
ATOM   1405 O O   . ALA B 1 39  ? 17.926 1.270   -3.033  1.00 22.35 ? 39  ALA B O   1 
ATOM   1406 C CB  . ALA B 1 39  ? 14.978 0.690   -1.790  1.00 22.12 ? 39  ALA B CB  1 
ATOM   1407 N N   . TRP B 1 40  ? 16.313 1.143   -4.606  1.00 20.69 ? 40  TRP B N   1 
ATOM   1408 C CA  . TRP B 1 40  ? 17.187 0.702   -5.685  1.00 22.11 ? 40  TRP B CA  1 
ATOM   1409 C C   . TRP B 1 40  ? 18.325 1.709   -5.881  1.00 22.28 ? 40  TRP B C   1 
ATOM   1410 O O   . TRP B 1 40  ? 19.482 1.332   -6.065  1.00 25.07 ? 40  TRP B O   1 
ATOM   1411 C CB  . TRP B 1 40  ? 16.329 0.502   -6.943  1.00 24.76 ? 40  TRP B CB  1 
ATOM   1412 C CG  . TRP B 1 40  ? 17.042 0.061   -8.188  1.00 25.75 ? 40  TRP B CG  1 
ATOM   1413 C CD1 . TRP B 1 40  ? 17.149 -1.212  -8.672  1.00 28.25 ? 40  TRP B CD1 1 
ATOM   1414 C CD2 . TRP B 1 40  ? 17.678 0.912   -9.162  1.00 23.64 ? 40  TRP B CD2 1 
ATOM   1415 N NE1 . TRP B 1 40  ? 17.844 -1.217  -9.849  1.00 26.27 ? 40  TRP B NE1 1 
ATOM   1416 C CE2 . TRP B 1 40  ? 18.163 0.073   -10.188 1.00 25.79 ? 40  TRP B CE2 1 
ATOM   1417 C CE3 . TRP B 1 40  ? 17.901 2.287   -9.272  1.00 24.46 ? 40  TRP B CE3 1 
ATOM   1418 C CZ2 . TRP B 1 40  ? 18.863 0.566   -11.285 1.00 26.53 ? 40  TRP B CZ2 1 
ATOM   1419 C CZ3 . TRP B 1 40  ? 18.588 2.761   -10.362 1.00 26.00 ? 40  TRP B CZ3 1 
ATOM   1420 C CH2 . TRP B 1 40  ? 19.068 1.918   -11.352 1.00 26.87 ? 40  TRP B CH2 1 
ATOM   1421 N N   A CYS B 1 41  ? 17.989 3.006   -5.833  0.50 22.71 ? 41  CYS B N   1 
ATOM   1422 N N   B CYS B 1 41  ? 17.973 2.990   -5.779  0.50 23.18 ? 41  CYS B N   1 
ATOM   1423 C CA  A CYS B 1 41  ? 18.977 4.069   -5.909  0.50 22.49 ? 41  CYS B CA  1 
ATOM   1424 C CA  B CYS B 1 41  ? 18.914 4.082   -5.912  0.50 23.58 ? 41  CYS B CA  1 
ATOM   1425 C C   A CYS B 1 41  ? 19.922 4.036   -4.710  0.50 21.73 ? 41  CYS B C   1 
ATOM   1426 C C   B CYS B 1 41  ? 19.880 4.138   -4.723  0.50 22.54 ? 41  CYS B C   1 
ATOM   1427 O O   A CYS B 1 41  ? 21.141 4.082   -4.871  0.50 20.88 ? 41  CYS B O   1 
ATOM   1428 O O   B CYS B 1 41  ? 21.081 4.332   -4.906  0.50 23.03 ? 41  CYS B O   1 
ATOM   1429 C CB  A CYS B 1 41  ? 18.318 5.445   -5.927  0.50 23.65 ? 41  CYS B CB  1 
ATOM   1430 C CB  B CYS B 1 41  ? 18.118 5.374   -6.041  0.50 25.26 ? 41  CYS B CB  1 
ATOM   1431 S SG  A CYS B 1 41  ? 17.388 5.805   -7.437  0.50 25.70 ? 41  CYS B SG  1 
ATOM   1432 S SG  B CYS B 1 41  ? 19.154 6.837   -6.256  0.50 29.21 ? 41  CYS B SG  1 
ATOM   1433 N N   . LEU B 1 42  ? 19.346 3.976   -3.507  1.00 21.87 ? 42  LEU B N   1 
ATOM   1434 C CA  . LEU B 1 42  ? 20.122 4.107   -2.281  1.00 21.92 ? 42  LEU B CA  1 
ATOM   1435 C C   . LEU B 1 42  ? 21.154 2.990   -2.155  1.00 21.74 ? 42  LEU B C   1 
ATOM   1436 O O   . LEU B 1 42  ? 22.270 3.254   -1.729  1.00 23.39 ? 42  LEU B O   1 
ATOM   1437 C CB  . LEU B 1 42  ? 19.186 4.145   -1.067  1.00 22.73 ? 42  LEU B CB  1 
ATOM   1438 C CG  . LEU B 1 42  ? 18.332 5.410   -0.958  1.00 23.67 ? 42  LEU B CG  1 
ATOM   1439 C CD1 . LEU B 1 42  ? 17.187 5.227   0.024   1.00 25.08 ? 42  LEU B CD1 1 
ATOM   1440 C CD2 . LEU B 1 42  ? 19.204 6.578   -0.544  1.00 26.45 ? 42  LEU B CD2 1 
ATOM   1441 N N   . VAL B 1 43  ? 20.780 1.747   -2.505  1.00 21.46 ? 43  VAL B N   1 
ATOM   1442 C CA  . VAL B 1 43  ? 21.695 0.631   -2.301  1.00 22.48 ? 43  VAL B CA  1 
ATOM   1443 C C   . VAL B 1 43  ? 22.850 0.675   -3.307  1.00 22.80 ? 43  VAL B C   1 
ATOM   1444 O O   . VAL B 1 43  ? 23.826 -0.052  -3.135  1.00 24.03 ? 43  VAL B O   1 
ATOM   1445 C CB  . VAL B 1 43  ? 20.978 -0.736  -2.313  1.00 24.34 ? 43  VAL B CB  1 
ATOM   1446 C CG1 . VAL B 1 43  ? 19.958 -0.865  -1.193  1.00 25.66 ? 43  VAL B CG1 1 
ATOM   1447 C CG2 . VAL B 1 43  ? 20.346 -1.065  -3.655  1.00 26.72 ? 43  VAL B CG2 1 
ATOM   1448 N N   . ARG B 1 44  ? 22.762 1.528   -4.333  1.00 23.44 ? 44  ARG B N   1 
ATOM   1449 C CA  . ARG B 1 44  ? 23.852 1.750   -5.281  1.00 25.65 ? 44  ARG B CA  1 
ATOM   1450 C C   . ARG B 1 44  ? 24.731 2.948   -4.910  1.00 25.90 ? 44  ARG B C   1 
ATOM   1451 O O   . ARG B 1 44  ? 25.684 3.268   -5.624  1.00 28.22 ? 44  ARG B O   1 
ATOM   1452 C CB  . ARG B 1 44  ? 23.279 2.034   -6.670  1.00 26.54 ? 44  ARG B CB  1 
ATOM   1453 C CG  . ARG B 1 44  ? 22.629 0.822   -7.311  1.00 27.05 ? 44  ARG B CG  1 
ATOM   1454 C CD  . ARG B 1 44  ? 21.962 1.215   -8.611  1.00 30.01 ? 44  ARG B CD  1 
ATOM   1455 N NE  . ARG B 1 44  ? 21.790 0.062   -9.476  1.00 31.11 ? 44  ARG B NE  1 
ATOM   1456 C CZ  . ARG B 1 44  ? 20.998 -0.967  -9.207  1.00 30.30 ? 44  ARG B CZ  1 
ATOM   1457 N NH1 . ARG B 1 44  ? 20.227 -0.939  -8.134  1.00 29.15 ? 44  ARG B NH1 1 
ATOM   1458 N NH2 . ARG B 1 44  ? 20.960 -2.012  -10.019 1.00 32.99 ? 44  ARG B NH2 1 
ATOM   1459 N N   . SER B 1 45  ? 24.441 3.605   -3.787  1.00 24.70 ? 45  SER B N   1 
ATOM   1460 C CA  . SER B 1 45  ? 25.205 4.777   -3.394  1.00 25.86 ? 45  SER B CA  1 
ATOM   1461 C C   . SER B 1 45  ? 26.649 4.426   -3.042  1.00 25.11 ? 45  SER B C   1 
ATOM   1462 O O   . SER B 1 45  ? 26.960 3.317   -2.628  1.00 26.02 ? 45  SER B O   1 
ATOM   1463 C CB  . SER B 1 45  ? 24.552 5.482   -2.244  1.00 24.98 ? 45  SER B CB  1 
ATOM   1464 O OG  . SER B 1 45  ? 25.301 6.641   -1.892  1.00 25.62 ? 45  SER B OG  1 
ATOM   1465 N N   . LYS B 1 46  ? 27.536 5.409   -3.173  1.00 26.86 ? 46  LYS B N   1 
ATOM   1466 C CA  . LYS B 1 46  ? 28.903 5.290   -2.687  1.00 29.20 ? 46  LYS B CA  1 
ATOM   1467 C C   . LYS B 1 46  ? 28.970 5.430   -1.163  1.00 26.29 ? 46  LYS B C   1 
ATOM   1468 O O   . LYS B 1 46  ? 29.996 5.098   -0.571  1.00 29.69 ? 46  LYS B O   1 
ATOM   1469 C CB  . LYS B 1 46  ? 29.785 6.347   -3.361  1.00 32.21 ? 46  LYS B CB  1 
ATOM   1470 C CG  . LYS B 1 46  ? 29.465 7.795   -3.028  1.00 35.68 ? 46  LYS B CG  1 
ATOM   1471 C CD  . LYS B 1 46  ? 30.277 8.777   -3.845  1.00 40.92 ? 46  LYS B CD  1 
ATOM   1472 C CE  . LYS B 1 46  ? 29.894 8.811   -5.309  1.00 45.30 ? 46  LYS B CE  1 
ATOM   1473 N NZ  . LYS B 1 46  ? 30.635 9.869   -6.040  1.00 49.10 ? 46  LYS B NZ  1 
ATOM   1474 N N   . TYR B 1 47  ? 27.894 5.918   -0.526  1.00 22.57 ? 47  TYR B N   1 
ATOM   1475 C CA  . TYR B 1 47  ? 27.893 6.179   0.907   1.00 22.90 ? 47  TYR B CA  1 
ATOM   1476 C C   . TYR B 1 47  ? 27.138 5.095   1.674   1.00 21.79 ? 47  TYR B C   1 
ATOM   1477 O O   . TYR B 1 47  ? 25.995 4.755   1.363   1.00 22.15 ? 47  TYR B O   1 
ATOM   1478 C CB  . TYR B 1 47  ? 27.305 7.563   1.201   1.00 24.57 ? 47  TYR B CB  1 
ATOM   1479 C CG  . TYR B 1 47  ? 28.098 8.699   0.604   1.00 24.74 ? 47  TYR B CG  1 
ATOM   1480 C CD1 . TYR B 1 47  ? 29.369 9.007   1.071   1.00 25.60 ? 47  TYR B CD1 1 
ATOM   1481 C CD2 . TYR B 1 47  ? 27.604 9.437   -0.460  1.00 25.46 ? 47  TYR B CD2 1 
ATOM   1482 C CE1 . TYR B 1 47  ? 30.108 10.043  0.519   1.00 27.00 ? 47  TYR B CE1 1 
ATOM   1483 C CE2 . TYR B 1 47  ? 28.331 10.472  -1.030  1.00 26.22 ? 47  TYR B CE2 1 
ATOM   1484 C CZ  . TYR B 1 47  ? 29.589 10.779  -0.535  1.00 26.72 ? 47  TYR B CZ  1 
ATOM   1485 O OH  . TYR B 1 47  ? 30.338 11.778  -1.089  1.00 29.46 ? 47  TYR B OH  1 
ATOM   1486 N N   . ASN B 1 48  ? 27.798 4.569   2.710   1.00 25.67 ? 48  ASN B N   1 
ATOM   1487 C CA  . ASN B 1 48  ? 27.227 3.528   3.551   1.00 24.43 ? 48  ASN B CA  1 
ATOM   1488 C C   . ASN B 1 48  ? 25.896 3.953   4.170   1.00 25.93 ? 48  ASN B C   1 
ATOM   1489 O O   . ASN B 1 48  ? 24.979 3.137   4.241   1.00 24.94 ? 48  ASN B O   1 
ATOM   1490 C CB  . ASN B 1 48  ? 28.197 3.085   4.647   1.00 27.06 ? 48  ASN B CB  1 
ATOM   1491 C CG  . ASN B 1 48  ? 29.286 2.179   4.119   1.00 30.54 ? 48  ASN B CG  1 
ATOM   1492 O OD1 . ASN B 1 48  ? 29.322 1.886   2.929   1.00 32.40 ? 48  ASN B OD1 1 
ATOM   1493 N ND2 . ASN B 1 48  ? 30.158 1.709   4.997   1.00 36.00 ? 48  ASN B ND2 1 
ATOM   1494 N N   . ASP B 1 49  ? 25.786 5.222   4.582   1.00 26.25 ? 49  ASP B N   1 
ATOM   1495 C CA  . ASP B 1 49  ? 24.566 5.746   5.179   1.00 26.75 ? 49  ASP B CA  1 
ATOM   1496 C C   . ASP B 1 49  ? 23.378 5.588   4.230   1.00 24.70 ? 49  ASP B C   1 
ATOM   1497 O O   . ASP B 1 49  ? 22.274 5.268   4.666   1.00 25.96 ? 49  ASP B O   1 
ATOM   1498 C CB  . ASP B 1 49  ? 24.704 7.229   5.535   1.00 29.31 ? 49  ASP B CB  1 
ATOM   1499 C CG  . ASP B 1 49  ? 25.504 7.559   6.782   1.00 34.48 ? 49  ASP B CG  1 
ATOM   1500 O OD1 . ASP B 1 49  ? 25.738 6.658   7.604   1.00 40.45 ? 49  ASP B OD1 1 
ATOM   1501 O OD2 . ASP B 1 49  ? 25.860 8.746   6.934   1.00 36.94 ? 49  ASP B OD2 1 
ATOM   1502 N N   . ASP B 1 50  ? 23.602 5.839   2.934   1.00 22.86 ? 50  ASP B N   1 
ATOM   1503 C CA  . ASP B 1 50  ? 22.565 5.673   1.929   1.00 23.88 ? 50  ASP B CA  1 
ATOM   1504 C C   . ASP B 1 50  ? 22.189 4.199   1.781   1.00 21.74 ? 50  ASP B C   1 
ATOM   1505 O O   . ASP B 1 50  ? 21.010 3.867   1.728   1.00 22.72 ? 50  ASP B O   1 
ATOM   1506 C CB  . ASP B 1 50  ? 23.001 6.194   0.563   1.00 24.45 ? 50  ASP B CB  1 
ATOM   1507 C CG  . ASP B 1 50  ? 23.004 7.705   0.415   1.00 25.81 ? 50  ASP B CG  1 
ATOM   1508 O OD1 . ASP B 1 50  ? 22.292 8.383   1.189   1.00 27.32 ? 50  ASP B OD1 1 
ATOM   1509 O OD2 . ASP B 1 50  ? 23.704 8.190   -0.500  1.00 26.63 ? 50  ASP B OD2 1 
ATOM   1510 N N   . ILE B 1 51  ? 23.186 3.310   1.694   1.00 22.29 ? 51  ILE B N   1 
ATOM   1511 C CA  . ILE B 1 51  ? 22.899 1.889   1.551   1.00 21.59 ? 51  ILE B CA  1 
ATOM   1512 C C   . ILE B 1 51  ? 22.040 1.400   2.721   1.00 21.25 ? 51  ILE B C   1 
ATOM   1513 O O   . ILE B 1 51  ? 21.074 0.648   2.519   1.00 21.69 ? 51  ILE B O   1 
ATOM   1514 C CB  . ILE B 1 51  ? 24.204 1.079   1.410   1.00 21.65 ? 51  ILE B CB  1 
ATOM   1515 C CG1 . ILE B 1 51  ? 25.066 1.544   0.228   1.00 22.90 ? 51  ILE B CG1 1 
ATOM   1516 C CG2 . ILE B 1 51  ? 23.876 -0.395  1.311   1.00 21.17 ? 51  ILE B CG2 1 
ATOM   1517 C CD1 . ILE B 1 51  ? 26.457 0.952   0.221   1.00 23.91 ? 51  ILE B CD1 1 
ATOM   1518 N N   A ARG B 1 52  ? 22.402 1.819   3.941   0.50 22.39 ? 52  ARG B N   1 
ATOM   1519 N N   B ARG B 1 52  ? 22.401 1.815   3.943   0.50 22.52 ? 52  ARG B N   1 
ATOM   1520 C CA  A ARG B 1 52  ? 21.691 1.403   5.141   0.50 23.52 ? 52  ARG B CA  1 
ATOM   1521 C CA  B ARG B 1 52  ? 21.686 1.393   5.140   0.50 23.69 ? 52  ARG B CA  1 
ATOM   1522 C C   A ARG B 1 52  ? 20.243 1.890   5.099   0.50 22.94 ? 52  ARG B C   1 
ATOM   1523 C C   B ARG B 1 52  ? 20.240 1.886   5.095   0.50 22.97 ? 52  ARG B C   1 
ATOM   1524 O O   A ARG B 1 52  ? 19.336 1.183   5.539   0.50 23.59 ? 52  ARG B O   1 
ATOM   1525 O O   B ARG B 1 52  ? 19.329 1.181   5.529   0.50 23.58 ? 52  ARG B O   1 
ATOM   1526 C CB  A ARG B 1 52  ? 22.413 1.907   6.394   0.50 24.73 ? 52  ARG B CB  1 
ATOM   1527 C CB  B ARG B 1 52  ? 22.398 1.883   6.404   0.50 25.38 ? 52  ARG B CB  1 
ATOM   1528 C CG  A ARG B 1 52  ? 23.662 1.107   6.736   0.50 26.70 ? 52  ARG B CG  1 
ATOM   1529 C CG  B ARG B 1 52  ? 23.718 1.178   6.679   0.50 27.68 ? 52  ARG B CG  1 
ATOM   1530 C CD  A ARG B 1 52  ? 24.360 1.598   7.990   0.50 29.75 ? 52  ARG B CD  1 
ATOM   1531 C CD  B ARG B 1 52  ? 24.377 1.649   7.962   0.50 31.55 ? 52  ARG B CD  1 
ATOM   1532 N NE  A ARG B 1 52  ? 25.421 0.692   8.411   0.50 31.58 ? 52  ARG B NE  1 
ATOM   1533 N NE  B ARG B 1 52  ? 25.811 1.391   7.977   0.50 34.71 ? 52  ARG B NE  1 
ATOM   1534 C CZ  A ARG B 1 52  ? 26.716 0.995   8.431   0.50 33.83 ? 52  ARG B CZ  1 
ATOM   1535 C CZ  B ARG B 1 52  ? 26.371 0.188   8.071   0.50 36.26 ? 52  ARG B CZ  1 
ATOM   1536 N NH1 A ARG B 1 52  ? 27.127 2.193   8.058   0.50 34.46 ? 52  ARG B NH1 1 
ATOM   1537 N NH1 B ARG B 1 52  ? 25.630 -0.889  8.270   0.50 36.39 ? 52  ARG B NH1 1 
ATOM   1538 N NH2 A ARG B 1 52  ? 27.595 0.093   8.831   0.50 35.79 ? 52  ARG B NH2 1 
ATOM   1539 N NH2 B ARG B 1 52  ? 27.684 0.070   7.988   0.50 37.71 ? 52  ARG B NH2 1 
ATOM   1540 N N   . LYS B 1 53  ? 20.030 3.106   4.582   1.00 23.20 ? 53  LYS B N   1 
ATOM   1541 C CA  . LYS B 1 53  ? 18.686 3.647   4.448   1.00 23.33 ? 53  LYS B CA  1 
ATOM   1542 C C   . LYS B 1 53  ? 17.889 2.827   3.437   1.00 22.76 ? 53  LYS B C   1 
ATOM   1543 O O   . LYS B 1 53  ? 16.713 2.556   3.646   1.00 23.34 ? 53  LYS B O   1 
ATOM   1544 C CB  . LYS B 1 53  ? 18.741 5.113   4.006   1.00 24.26 ? 53  LYS B CB  1 
ATOM   1545 C CG  . LYS B 1 53  ? 17.386 5.776   3.817   1.00 29.17 ? 53  LYS B CG  1 
ATOM   1546 C CD  . LYS B 1 53  ? 16.584 5.908   5.093   1.00 34.19 ? 53  LYS B CD  1 
ATOM   1547 C CE  . LYS B 1 53  ? 15.293 6.676   4.894   1.00 39.92 ? 53  LYS B CE  1 
ATOM   1548 N NZ  . LYS B 1 53  ? 14.553 6.838   6.167   1.00 45.76 ? 53  LYS B NZ  1 
ATOM   1549 N N   . GLY B 1 54  ? 18.541 2.430   2.339   1.00 22.06 ? 54  GLY B N   1 
ATOM   1550 C CA  . GLY B 1 54  ? 17.909 1.568   1.353   1.00 20.99 ? 54  GLY B CA  1 
ATOM   1551 C C   . GLY B 1 54  ? 17.483 0.227   1.960   1.00 21.69 ? 54  GLY B C   1 
ATOM   1552 O O   . GLY B 1 54  ? 16.395 -0.269  1.696   1.00 21.07 ? 54  GLY B O   1 
ATOM   1553 N N   . ILE B 1 55  ? 18.344 -0.334  2.805   1.00 21.68 ? 55  ILE B N   1 
ATOM   1554 C CA  . ILE B 1 55  ? 18.047 -1.592  3.475   1.00 22.08 ? 55  ILE B CA  1 
ATOM   1555 C C   . ILE B 1 55  ? 16.835 -1.426  4.389   1.00 22.84 ? 55  ILE B C   1 
ATOM   1556 O O   . ILE B 1 55  ? 15.932 -2.262  4.373   1.00 23.68 ? 55  ILE B O   1 
ATOM   1557 C CB  . ILE B 1 55  ? 19.285 -2.131  4.210   1.00 23.28 ? 55  ILE B CB  1 
ATOM   1558 C CG1 . ILE B 1 55  ? 20.316 -2.668  3.215   1.00 23.60 ? 55  ILE B CG1 1 
ATOM   1559 C CG2 . ILE B 1 55  ? 18.890 -3.204  5.211   1.00 23.83 ? 55  ILE B CG2 1 
ATOM   1560 C CD1 . ILE B 1 55  ? 21.657 -2.955  3.832   1.00 24.64 ? 55  ILE B CD1 1 
ATOM   1561 N N   . VAL B 1 56  ? 16.805 -0.338  5.173   1.00 23.96 ? 56  VAL B N   1 
ATOM   1562 C CA  . VAL B 1 56  ? 15.675 -0.078  6.053   1.00 26.60 ? 56  VAL B CA  1 
ATOM   1563 C C   . VAL B 1 56  ? 14.381 0.003   5.240   1.00 24.53 ? 56  VAL B C   1 
ATOM   1564 O O   . VAL B 1 56  ? 13.365 -0.552  5.642   1.00 26.66 ? 56  VAL B O   1 
ATOM   1565 C CB  . VAL B 1 56  ? 15.894 1.192   6.897   1.00 28.09 ? 56  VAL B CB  1 
ATOM   1566 C CG1 . VAL B 1 56  ? 14.619 1.631   7.601   1.00 29.11 ? 56  VAL B CG1 1 
ATOM   1567 C CG2 . VAL B 1 56  ? 17.028 1.011   7.898   1.00 30.75 ? 56  VAL B CG2 1 
ATOM   1568 N N   . LEU B 1 57  ? 14.416 0.698   4.101   1.00 24.55 ? 57  LEU B N   1 
ATOM   1569 C CA  . LEU B 1 57  ? 13.239 0.868   3.257   1.00 24.76 ? 57  LEU B CA  1 
ATOM   1570 C C   . LEU B 1 57  ? 12.746 -0.482  2.728   1.00 24.19 ? 57  LEU B C   1 
ATOM   1571 O O   . LEU B 1 57  ? 11.548 -0.765  2.751   1.00 25.88 ? 57  LEU B O   1 
ATOM   1572 C CB  . LEU B 1 57  ? 13.604 1.803   2.099   1.00 26.40 ? 57  LEU B CB  1 
ATOM   1573 C CG  . LEU B 1 57  ? 12.615 2.911   1.757   1.00 34.96 ? 57  LEU B CG  1 
ATOM   1574 C CD1 . LEU B 1 57  ? 12.977 3.527   0.413   1.00 33.51 ? 57  LEU B CD1 1 
ATOM   1575 C CD2 . LEU B 1 57  ? 11.177 2.423   1.765   1.00 37.90 ? 57  LEU B CD2 1 
ATOM   1576 N N   . LEU B 1 58  ? 13.672 -1.321  2.249   1.00 22.23 ? 58  LEU B N   1 
ATOM   1577 C CA  . LEU B 1 58  ? 13.317 -2.638  1.744   1.00 21.91 ? 58  LEU B CA  1 
ATOM   1578 C C   . LEU B 1 58  ? 12.717 -3.502  2.852   1.00 22.54 ? 58  LEU B C   1 
ATOM   1579 O O   . LEU B 1 58  ? 11.791 -4.268  2.590   1.00 24.39 ? 58  LEU B O   1 
ATOM   1580 C CB  . LEU B 1 58  ? 14.566 -3.280  1.139   1.00 21.81 ? 58  LEU B CB  1 
ATOM   1581 C CG  . LEU B 1 58  ? 15.041 -2.641  -0.169  1.00 22.42 ? 58  LEU B CG  1 
ATOM   1582 C CD1 . LEU B 1 58  ? 16.427 -3.131  -0.551  1.00 23.25 ? 58  LEU B CD1 1 
ATOM   1583 C CD2 . LEU B 1 58  ? 14.061 -2.922  -1.297  1.00 24.90 ? 58  LEU B CD2 1 
ATOM   1584 N N   . GLU B 1 59  ? 13.265 -3.410  4.069   1.00 23.53 ? 59  GLU B N   1 
ATOM   1585 C CA  . GLU B 1 59  ? 12.761 -4.181  5.194   1.00 25.20 ? 59  GLU B CA  1 
ATOM   1586 C C   . GLU B 1 59  ? 11.322 -3.772  5.525   1.00 25.77 ? 59  GLU B C   1 
ATOM   1587 O O   . GLU B 1 59  ? 10.504 -4.619  5.901   1.00 26.50 ? 59  GLU B O   1 
ATOM   1588 C CB  . GLU B 1 59  ? 13.734 -4.050  6.366   1.00 28.39 ? 59  GLU B CB  1 
ATOM   1589 C CG  . GLU B 1 59  ? 14.940 -4.975  6.211   1.00 31.26 ? 59  GLU B CG  1 
ATOM   1590 C CD  . GLU B 1 59  ? 16.054 -4.797  7.228   1.00 38.45 ? 59  GLU B CD  1 
ATOM   1591 O OE1 . GLU B 1 59  ? 16.043 -3.781  7.943   1.00 43.88 ? 59  GLU B OE1 1 
ATOM   1592 O OE2 . GLU B 1 59  ? 16.938 -5.687  7.296   1.00 44.70 ? 59  GLU B OE2 1 
ATOM   1593 N N   . GLU B 1 60  ? 11.003 -2.484  5.339   1.00 26.87 ? 60  GLU B N   1 
ATOM   1594 C CA  . GLU B 1 60  ? 9.648  -1.986  5.542   1.00 29.98 ? 60  GLU B CA  1 
ATOM   1595 C C   . GLU B 1 60  ? 8.697  -2.453  4.439   1.00 29.88 ? 60  GLU B C   1 
ATOM   1596 O O   . GLU B 1 60  ? 7.532  -2.753  4.709   1.00 30.61 ? 60  GLU B O   1 
ATOM   1597 C CB  . GLU B 1 60  ? 9.668  -0.461  5.618   1.00 33.50 ? 60  GLU B CB  1 
ATOM   1598 C CG  . GLU B 1 60  ? 10.243 0.035   6.921   1.00 39.34 ? 60  GLU B CG  1 
ATOM   1599 C CD  . GLU B 1 60  ? 10.535 1.522   6.999   1.00 42.27 ? 60  GLU B CD  1 
ATOM   1600 O OE1 . GLU B 1 60  ? 10.603 2.183   5.932   1.00 49.58 ? 60  GLU B OE1 1 
ATOM   1601 O OE2 . GLU B 1 60  ? 10.698 2.015   8.130   1.00 46.49 ? 60  GLU B OE2 1 
ATOM   1602 N N   . LEU B 1 61  ? 9.196  -2.501  3.200   1.00 27.53 ? 61  LEU B N   1 
ATOM   1603 C CA  . LEU B 1 61  ? 8.406  -2.922  2.056   1.00 28.28 ? 61  LEU B CA  1 
ATOM   1604 C C   . LEU B 1 61  ? 8.092  -4.414  2.117   1.00 29.43 ? 61  LEU B C   1 
ATOM   1605 O O   . LEU B 1 61  ? 7.021  -4.813  1.677   1.00 30.25 ? 61  LEU B O   1 
ATOM   1606 C CB  . LEU B 1 61  ? 9.177  -2.606  0.773   1.00 29.24 ? 61  LEU B CB  1 
ATOM   1607 C CG  . LEU B 1 61  ? 9.198  -1.132  0.375   1.00 29.73 ? 61  LEU B CG  1 
ATOM   1608 C CD1 . LEU B 1 61  ? 10.174 -0.894  -0.765  1.00 29.67 ? 61  LEU B CD1 1 
ATOM   1609 C CD2 . LEU B 1 61  ? 7.804  -0.649  -0.010  1.00 30.35 ? 61  LEU B CD2 1 
ATOM   1610 N N   . LEU B 1 62  ? 9.020  -5.213  2.663   1.00 30.69 ? 62  LEU B N   1 
ATOM   1611 C CA  . LEU B 1 62  ? 8.999  -6.664  2.510   1.00 30.99 ? 62  LEU B CA  1 
ATOM   1612 C C   . LEU B 1 62  ? 7.643  -7.250  2.914   1.00 33.35 ? 62  LEU B C   1 
ATOM   1613 O O   . LEU B 1 62  ? 7.033  -7.971  2.119   1.00 35.41 ? 62  LEU B O   1 
ATOM   1614 C CB  . LEU B 1 62  ? 10.171 -7.269  3.297   1.00 31.52 ? 62  LEU B CB  1 
ATOM   1615 C CG  . LEU B 1 62  ? 10.442 -8.758  3.101   1.00 35.84 ? 62  LEU B CG  1 
ATOM   1616 C CD1 . LEU B 1 62  ? 10.674 -9.104  1.639   1.00 34.36 ? 62  LEU B CD1 1 
ATOM   1617 C CD2 . LEU B 1 62  ? 11.639 -9.177  3.937   1.00 37.47 ? 62  LEU B CD2 1 
ATOM   1618 N N   . PRO B 1 63  ? 7.091  -6.969  4.120   1.00 35.49 ? 63  PRO B N   1 
ATOM   1619 C CA  . PRO B 1 63  ? 5.831  -7.597  4.534   1.00 37.20 ? 63  PRO B CA  1 
ATOM   1620 C C   . PRO B 1 63  ? 4.619  -7.271  3.660   1.00 34.98 ? 63  PRO B C   1 
ATOM   1621 O O   . PRO B 1 63  ? 3.641  -8.004  3.684   1.00 40.12 ? 63  PRO B O   1 
ATOM   1622 C CB  . PRO B 1 63  ? 5.587  -7.052  5.952   1.00 38.66 ? 63  PRO B CB  1 
ATOM   1623 C CG  . PRO B 1 63  ? 6.936  -6.559  6.416   1.00 39.40 ? 63  PRO B CG  1 
ATOM   1624 C CD  . PRO B 1 63  ? 7.638  -6.088  5.160   1.00 37.22 ? 63  PRO B CD  1 
ATOM   1625 N N   . LYS B 1 64  ? 4.675  -6.164  2.908   1.00 36.26 ? 64  LYS B N   1 
ATOM   1626 C CA  . LYS B 1 64  ? 3.531  -5.692  2.140   1.00 36.82 ? 64  LYS B CA  1 
ATOM   1627 C C   . LYS B 1 64  ? 3.608  -6.174  0.693   1.00 33.99 ? 64  LYS B C   1 
ATOM   1628 O O   . LYS B 1 64  ? 2.710  -5.898  -0.102  1.00 35.24 ? 64  LYS B O   1 
ATOM   1629 C CB  . LYS B 1 64  ? 3.470  -4.162  2.176   1.00 40.72 ? 64  LYS B CB  1 
ATOM   1630 C CG  . LYS B 1 64  ? 3.470  -3.552  3.572   1.00 46.70 ? 64  LYS B CG  1 
ATOM   1631 C CD  . LYS B 1 64  ? 3.563  -2.044  3.566   1.00 50.42 ? 64  LYS B CD  1 
ATOM   1632 C CE  . LYS B 1 64  ? 3.574  -1.444  4.957   1.00 55.03 ? 64  LYS B CE  1 
ATOM   1633 N NZ  . LYS B 1 64  ? 3.612  0.037   4.916   1.00 56.24 ? 64  LYS B NZ  1 
ATOM   1634 N N   . GLY B 1 65  ? 4.686  -6.882  0.346   1.00 30.36 ? 65  GLY B N   1 
ATOM   1635 C CA  . GLY B 1 65  ? 4.914  -7.275  -1.035  1.00 29.86 ? 65  GLY B CA  1 
ATOM   1636 C C   . GLY B 1 65  ? 4.138  -8.528  -1.433  1.00 30.61 ? 65  GLY B C   1 
ATOM   1637 O O   . GLY B 1 65  ? 3.873  -9.388  -0.598  1.00 32.18 ? 65  GLY B O   1 
ATOM   1638 N N   . SER B 1 66  ? 3.796  -8.615  -2.725  1.00 28.80 ? 66  SER B N   1 
ATOM   1639 C CA  . SER B 1 66  ? 3.465  -9.889  -3.345  1.00 28.20 ? 66  SER B CA  1 
ATOM   1640 C C   . SER B 1 66  ? 4.709  -10.765 -3.317  1.00 28.85 ? 66  SER B C   1 
ATOM   1641 O O   . SER B 1 66  ? 5.805  -10.269 -3.073  1.00 29.44 ? 66  SER B O   1 
ATOM   1642 C CB  . SER B 1 66  ? 3.000  -9.714  -4.754  1.00 29.32 ? 66  SER B CB  1 
ATOM   1643 O OG  . SER B 1 66  ? 4.085  -9.316  -5.586  1.00 28.11 ? 66  SER B OG  1 
ATOM   1644 N N   . LYS B 1 67  ? 4.538  -12.047 -3.637  1.00 31.10 ? 67  LYS B N   1 
ATOM   1645 C CA  . LYS B 1 67  ? 5.652  -12.987 -3.658  1.00 32.88 ? 67  LYS B CA  1 
ATOM   1646 C C   . LYS B 1 67  ? 6.675  -12.521 -4.690  1.00 32.57 ? 67  LYS B C   1 
ATOM   1647 O O   . LYS B 1 67  ? 7.879  -12.589 -4.455  1.00 30.90 ? 67  LYS B O   1 
ATOM   1648 C CB  . LYS B 1 67  ? 5.170  -14.410 -3.955  1.00 35.94 ? 67  LYS B CB  1 
ATOM   1649 C CG  . LYS B 1 67  ? 4.238  -14.983 -2.898  1.00 40.93 ? 67  LYS B CG  1 
ATOM   1650 C CD  . LYS B 1 67  ? 3.673  -16.323 -3.274  1.00 46.00 ? 67  LYS B CD  1 
ATOM   1651 C CE  . LYS B 1 67  ? 2.653  -16.817 -2.271  1.00 51.37 ? 67  LYS B CE  1 
ATOM   1652 N NZ  . LYS B 1 67  ? 2.064  -18.102 -2.701  1.00 54.30 ? 67  LYS B NZ  1 
ATOM   1653 N N   . GLU B 1 68  ? 6.171  -12.011 -5.814  1.00 31.22 ? 68  GLU B N   1 
ATOM   1654 C CA  . GLU B 1 68  ? 7.007  -11.551 -6.908  1.00 32.68 ? 68  GLU B CA  1 
ATOM   1655 C C   . GLU B 1 68  ? 7.848  -10.349 -6.464  1.00 29.67 ? 68  GLU B C   1 
ATOM   1656 O O   . GLU B 1 68  ? 9.048  -10.293 -6.736  1.00 31.74 ? 68  GLU B O   1 
ATOM   1657 C CB  . GLU B 1 68  ? 6.103  -11.245 -8.105  1.00 36.15 ? 68  GLU B CB  1 
ATOM   1658 C CG  . GLU B 1 68  ? 5.436  -12.481 -8.700  1.00 41.75 ? 68  GLU B CG  1 
ATOM   1659 C CD  . GLU B 1 68  ? 4.351  -13.211 -7.907  1.00 46.04 ? 68  GLU B CD  1 
ATOM   1660 O OE1 . GLU B 1 68  ? 3.742  -12.620 -6.968  1.00 41.50 ? 68  GLU B OE1 1 
ATOM   1661 O OE2 . GLU B 1 68  ? 4.121  -14.404 -8.222  1.00 52.88 ? 68  GLU B OE2 1 
ATOM   1662 N N   . GLU B 1 69  ? 7.211  -9.379  -5.789  1.00 28.67 ? 69  GLU B N   1 
ATOM   1663 C CA  . GLU B 1 69  ? 7.890  -8.206  -5.263  1.00 27.48 ? 69  GLU B CA  1 
ATOM   1664 C C   . GLU B 1 69  ? 8.921  -8.594  -4.195  1.00 28.40 ? 69  GLU B C   1 
ATOM   1665 O O   . GLU B 1 69  ? 10.020 -8.035  -4.127  1.00 26.16 ? 69  GLU B O   1 
ATOM   1666 C CB  . GLU B 1 69  ? 6.841  -7.234  -4.704  1.00 26.84 ? 69  GLU B CB  1 
ATOM   1667 C CG  . GLU B 1 69  ? 6.005  -6.538  -5.772  1.00 28.10 ? 69  GLU B CG  1 
ATOM   1668 C CD  . GLU B 1 69  ? 4.730  -5.880  -5.270  1.00 29.53 ? 69  GLU B CD  1 
ATOM   1669 O OE1 . GLU B 1 69  ? 4.257  -6.258  -4.169  1.00 31.02 ? 69  GLU B OE1 1 
ATOM   1670 O OE2 . GLU B 1 69  ? 4.214  -4.994  -5.982  1.00 33.69 ? 69  GLU B OE2 1 
ATOM   1671 N N   . GLN B 1 70  ? 8.556  -9.530  -3.319  1.00 27.29 ? 70  GLN B N   1 
ATOM   1672 C CA  . GLN B 1 70  ? 9.419  -9.920  -2.214  1.00 27.97 ? 70  GLN B CA  1 
ATOM   1673 C C   . GLN B 1 70  ? 10.737 -10.489 -2.743  1.00 28.08 ? 70  GLN B C   1 
ATOM   1674 O O   . GLN B 1 70  ? 11.793 -10.293 -2.134  1.00 28.14 ? 70  GLN B O   1 
ATOM   1675 C CB  . GLN B 1 70  ? 8.688  -10.913 -1.305  1.00 29.21 ? 70  GLN B CB  1 
ATOM   1676 C CG  . GLN B 1 70  ? 7.648  -10.255 -0.410  1.00 32.14 ? 70  GLN B CG  1 
ATOM   1677 C CD  . GLN B 1 70  ? 6.902  -11.233 0.465   1.00 35.95 ? 70  GLN B CD  1 
ATOM   1678 O OE1 . GLN B 1 70  ? 6.795  -12.410 0.140   1.00 39.99 ? 70  GLN B OE1 1 
ATOM   1679 N NE2 . GLN B 1 70  ? 6.345  -10.742 1.563   1.00 34.68 ? 70  GLN B NE2 1 
ATOM   1680 N N   . ARG B 1 71  ? 10.689 -11.170 -3.893  1.00 28.94 ? 71  ARG B N   1 
ATOM   1681 C CA  . ARG B 1 71  ? 11.898 -11.744 -4.472  1.00 29.67 ? 71  ARG B CA  1 
ATOM   1682 C C   . ARG B 1 71  ? 12.853 -10.625 -4.877  1.00 27.51 ? 71  ARG B C   1 
ATOM   1683 O O   . ARG B 1 71  ? 14.061 -10.751 -4.716  1.00 26.40 ? 71  ARG B O   1 
ATOM   1684 C CB  . ARG B 1 71  ? 11.568 -12.629 -5.679  1.00 35.11 ? 71  ARG B CB  1 
ATOM   1685 C CG  . ARG B 1 71  ? 10.850 -13.926 -5.330  1.00 42.05 ? 71  ARG B CG  1 
ATOM   1686 C CD  . ARG B 1 71  ? 10.550 -14.761 -6.560  1.00 49.04 ? 71  ARG B CD  1 
ATOM   1687 N NE  . ARG B 1 71  ? 9.380  -15.604 -6.346  1.00 55.77 ? 71  ARG B NE  1 
ATOM   1688 C CZ  . ARG B 1 71  ? 8.241  -15.533 -7.032  1.00 57.74 ? 71  ARG B CZ  1 
ATOM   1689 N NH1 . ARG B 1 71  ? 8.114  -14.701 -8.051  1.00 56.92 ? 71  ARG B NH1 1 
ATOM   1690 N NH2 . ARG B 1 71  ? 7.228  -16.317 -6.704  1.00 62.40 ? 71  ARG B NH2 1 
ATOM   1691 N N   . ASP B 1 72  ? 12.297 -9.518  -5.384  1.00 26.96 ? 72  ASP B N   1 
ATOM   1692 C CA  . ASP B 1 72  ? 13.100 -8.361  -5.751  1.00 27.36 ? 72  ASP B CA  1 
ATOM   1693 C C   . ASP B 1 72  ? 13.647 -7.695  -4.491  1.00 25.27 ? 72  ASP B C   1 
ATOM   1694 O O   . ASP B 1 72  ? 14.807 -7.298  -4.457  1.00 25.27 ? 72  ASP B O   1 
ATOM   1695 C CB  . ASP B 1 72  ? 12.284 -7.356  -6.572  1.00 30.54 ? 72  ASP B CB  1 
ATOM   1696 C CG  . ASP B 1 72  ? 11.899 -7.855  -7.951  1.00 35.01 ? 72  ASP B CG  1 
ATOM   1697 O OD1 . ASP B 1 72  ? 12.552 -8.794  -8.427  1.00 41.35 ? 72  ASP B OD1 1 
ATOM   1698 O OD2 . ASP B 1 72  ? 10.948 -7.293  -8.538  1.00 40.75 ? 72  ASP B OD2 1 
ATOM   1699 N N   . TYR B 1 73  ? 12.807 -7.558  -3.460  1.00 23.99 ? 73  TYR B N   1 
ATOM   1700 C CA  . TYR B 1 73  ? 13.231 -6.920  -2.228  1.00 23.49 ? 73  TYR B CA  1 
ATOM   1701 C C   . TYR B 1 73  ? 14.386 -7.693  -1.601  1.00 22.35 ? 73  TYR B C   1 
ATOM   1702 O O   . TYR B 1 73  ? 15.386 -7.114  -1.190  1.00 22.34 ? 73  TYR B O   1 
ATOM   1703 C CB  . TYR B 1 73  ? 12.075 -6.787  -1.233  1.00 24.34 ? 73  TYR B CB  1 
ATOM   1704 C CG  . TYR B 1 73  ? 10.854 -6.028  -1.693  1.00 25.12 ? 73  TYR B CG  1 
ATOM   1705 C CD1 . TYR B 1 73  ? 10.885 -5.070  -2.702  1.00 24.10 ? 73  TYR B CD1 1 
ATOM   1706 C CD2 . TYR B 1 73  ? 9.641  -6.256  -1.067  1.00 25.76 ? 73  TYR B CD2 1 
ATOM   1707 C CE1 . TYR B 1 73  ? 9.744  -4.375  -3.070  1.00 24.55 ? 73  TYR B CE1 1 
ATOM   1708 C CE2 . TYR B 1 73  ? 8.492  -5.578  -1.430  1.00 26.02 ? 73  TYR B CE2 1 
ATOM   1709 C CZ  . TYR B 1 73  ? 8.542  -4.628  -2.432  1.00 25.44 ? 73  TYR B CZ  1 
ATOM   1710 O OH  . TYR B 1 73  ? 7.392  -3.956  -2.765  1.00 26.64 ? 73  TYR B OH  1 
ATOM   1711 N N   . VAL B 1 74  ? 14.249 -9.021  -1.556  1.00 22.14 ? 74  VAL B N   1 
ATOM   1712 C CA  . VAL B 1 74  ? 15.228 -9.862  -0.890  1.00 23.31 ? 74  VAL B CA  1 
ATOM   1713 C C   . VAL B 1 74  ? 16.539 -9.843  -1.674  1.00 21.75 ? 74  VAL B C   1 
ATOM   1714 O O   . VAL B 1 74  ? 17.617 -9.874  -1.089  1.00 22.33 ? 74  VAL B O   1 
ATOM   1715 C CB  . VAL B 1 74  ? 14.664 -11.283 -0.699  1.00 25.27 ? 74  VAL B CB  1 
ATOM   1716 C CG1 . VAL B 1 74  ? 15.742 -12.276 -0.322  1.00 26.12 ? 74  VAL B CG1 1 
ATOM   1717 C CG2 . VAL B 1 74  ? 13.552 -11.278 0.331   1.00 24.75 ? 74  VAL B CG2 1 
ATOM   1718 N N   . PHE B 1 75  ? 16.451 -9.821  -3.003  1.00 21.52 ? 75  PHE B N   1 
ATOM   1719 C CA  . PHE B 1 75  ? 17.650 -9.748  -3.819  1.00 21.55 ? 75  PHE B CA  1 
ATOM   1720 C C   . PHE B 1 75  ? 18.452 -8.502  -3.445  1.00 19.67 ? 75  PHE B C   1 
ATOM   1721 O O   . PHE B 1 75  ? 19.657 -8.586  -3.216  1.00 19.31 ? 75  PHE B O   1 
ATOM   1722 C CB  . PHE B 1 75  ? 17.309 -9.756  -5.307  1.00 22.97 ? 75  PHE B CB  1 
ATOM   1723 C CG  . PHE B 1 75  ? 18.514 -9.672  -6.205  1.00 22.90 ? 75  PHE B CG  1 
ATOM   1724 C CD1 . PHE B 1 75  ? 19.270 -10.794 -6.517  1.00 24.86 ? 75  PHE B CD1 1 
ATOM   1725 C CD2 . PHE B 1 75  ? 18.895 -8.458  -6.751  1.00 23.58 ? 75  PHE B CD2 1 
ATOM   1726 C CE1 . PHE B 1 75  ? 20.376 -10.698 -7.344  1.00 25.19 ? 75  PHE B CE1 1 
ATOM   1727 C CE2 . PHE B 1 75  ? 19.999 -8.361  -7.582  1.00 25.66 ? 75  PHE B CE2 1 
ATOM   1728 C CZ  . PHE B 1 75  ? 20.738 -9.481  -7.879  1.00 26.25 ? 75  PHE B CZ  1 
ATOM   1729 N N   . TYR B 1 76  ? 17.776 -7.349  -3.357  1.00 20.13 ? 76  TYR B N   1 
ATOM   1730 C CA  . TYR B 1 76  ? 18.486 -6.110  -3.077  1.00 20.53 ? 76  TYR B CA  1 
ATOM   1731 C C   . TYR B 1 76  ? 18.858 -5.979  -1.601  1.00 21.38 ? 76  TYR B C   1 
ATOM   1732 O O   . TYR B 1 76  ? 19.834 -5.306  -1.294  1.00 21.25 ? 76  TYR B O   1 
ATOM   1733 C CB  . TYR B 1 76  ? 17.704 -4.921  -3.638  1.00 20.00 ? 76  TYR B CB  1 
ATOM   1734 C CG  . TYR B 1 76  ? 18.028 -4.681  -5.091  1.00 21.41 ? 76  TYR B CG  1 
ATOM   1735 C CD1 . TYR B 1 76  ? 19.286 -4.244  -5.453  1.00 23.41 ? 76  TYR B CD1 1 
ATOM   1736 C CD2 . TYR B 1 76  ? 17.158 -5.045  -6.107  1.00 21.11 ? 76  TYR B CD2 1 
ATOM   1737 C CE1 . TYR B 1 76  ? 19.628 -4.047  -6.781  1.00 24.71 ? 76  TYR B CE1 1 
ATOM   1738 C CE2 . TYR B 1 76  ? 17.488 -4.874  -7.442  1.00 24.19 ? 76  TYR B CE2 1 
ATOM   1739 C CZ  . TYR B 1 76  ? 18.730 -4.367  -7.784  1.00 24.68 ? 76  TYR B CZ  1 
ATOM   1740 O OH  . TYR B 1 76  ? 19.100 -4.171  -9.099  1.00 28.98 ? 76  TYR B OH  1 
ATOM   1741 N N   . LEU B 1 77  ? 18.157 -6.676  -0.691  1.00 21.67 ? 77  LEU B N   1 
ATOM   1742 C CA  . LEU B 1 77  ? 18.621 -6.774  0.685   1.00 22.37 ? 77  LEU B CA  1 
ATOM   1743 C C   . LEU B 1 77  ? 19.943 -7.542  0.752   1.00 21.08 ? 77  LEU B C   1 
ATOM   1744 O O   . LEU B 1 77  ? 20.841 -7.174  1.501   1.00 21.51 ? 77  LEU B O   1 
ATOM   1745 C CB  . LEU B 1 77  ? 17.543 -7.431  1.551   1.00 22.03 ? 77  LEU B CB  1 
ATOM   1746 C CG  . LEU B 1 77  ? 16.402 -6.495  1.935   1.00 22.47 ? 77  LEU B CG  1 
ATOM   1747 C CD1 . LEU B 1 77  ? 15.174 -7.244  2.439   1.00 23.81 ? 77  LEU B CD1 1 
ATOM   1748 C CD2 . LEU B 1 77  ? 16.882 -5.464  2.950   1.00 24.58 ? 77  LEU B CD2 1 
ATOM   1749 N N   . ALA B 1 78  ? 20.074 -8.608  -0.040  1.00 20.23 ? 78  ALA B N   1 
ATOM   1750 C CA  . ALA B 1 78  ? 21.338 -9.317  -0.115  1.00 21.07 ? 78  ALA B CA  1 
ATOM   1751 C C   . ALA B 1 78  ? 22.438 -8.443  -0.712  1.00 20.46 ? 78  ALA B C   1 
ATOM   1752 O O   . ALA B 1 78  ? 23.549 -8.416  -0.197  1.00 21.02 ? 78  ALA B O   1 
ATOM   1753 C CB  . ALA B 1 78  ? 21.153 -10.590 -0.896  1.00 22.95 ? 78  ALA B CB  1 
ATOM   1754 N N   . VAL B 1 79  ? 22.120 -7.704  -1.782  1.00 20.56 ? 79  VAL B N   1 
ATOM   1755 C CA  . VAL B 1 79  ? 23.099 -6.838  -2.420  1.00 20.78 ? 79  VAL B CA  1 
ATOM   1756 C C   . VAL B 1 79  ? 23.581 -5.770  -1.440  1.00 20.37 ? 79  VAL B C   1 
ATOM   1757 O O   . VAL B 1 79  ? 24.787 -5.533  -1.309  1.00 21.26 ? 79  VAL B O   1 
ATOM   1758 C CB  . VAL B 1 79  ? 22.548 -6.185  -3.702  1.00 20.91 ? 79  VAL B CB  1 
ATOM   1759 C CG1 . VAL B 1 79  ? 23.489 -5.104  -4.209  1.00 22.25 ? 79  VAL B CG1 1 
ATOM   1760 C CG2 . VAL B 1 79  ? 22.279 -7.213  -4.790  1.00 21.84 ? 79  VAL B CG2 1 
ATOM   1761 N N   . GLY B 1 80  ? 22.631 -5.080  -0.806  1.00 19.55 ? 80  GLY B N   1 
ATOM   1762 C CA  . GLY B 1 80  ? 22.981 -3.997  0.105   1.00 20.46 ? 80  GLY B CA  1 
ATOM   1763 C C   . GLY B 1 80  ? 23.856 -4.479  1.264   1.00 21.95 ? 80  GLY B C   1 
ATOM   1764 O O   . GLY B 1 80  ? 24.864 -3.862  1.599   1.00 22.39 ? 80  GLY B O   1 
ATOM   1765 N N   . ASN B 1 81  ? 23.490 -5.617  1.862   1.00 22.58 ? 81  ASN B N   1 
ATOM   1766 C CA  . ASN B 1 81  ? 24.266 -6.169  2.959   1.00 22.50 ? 81  ASN B CA  1 
ATOM   1767 C C   . ASN B 1 81  ? 25.659 -6.579  2.488   1.00 22.00 ? 81  ASN B C   1 
ATOM   1768 O O   . ASN B 1 81  ? 26.630 -6.365  3.205   1.00 23.97 ? 81  ASN B O   1 
ATOM   1769 C CB  . ASN B 1 81  ? 23.482 -7.267  3.676   1.00 22.70 ? 81  ASN B CB  1 
ATOM   1770 C CG  . ASN B 1 81  ? 22.522 -6.694  4.695   1.00 23.83 ? 81  ASN B CG  1 
ATOM   1771 O OD1 . ASN B 1 81  ? 22.954 -6.135  5.702   1.00 26.67 ? 81  ASN B OD1 1 
ATOM   1772 N ND2 . ASN B 1 81  ? 21.230 -6.831  4.456   1.00 24.54 ? 81  ASN B ND2 1 
ATOM   1773 N N   . TYR B 1 82  ? 25.758 -7.163  1.291   1.00 22.39 ? 82  TYR B N   1 
ATOM   1774 C CA  . TYR B 1 82  ? 27.046 -7.520  0.728   1.00 22.27 ? 82  TYR B CA  1 
ATOM   1775 C C   . TYR B 1 82  ? 27.938 -6.281  0.605   1.00 22.00 ? 82  TYR B C   1 
ATOM   1776 O O   . TYR B 1 82  ? 29.108 -6.309  0.984   1.00 23.68 ? 82  TYR B O   1 
ATOM   1777 C CB  . TYR B 1 82  ? 26.861 -8.230  -0.615  1.00 22.67 ? 82  TYR B CB  1 
ATOM   1778 C CG  . TYR B 1 82  ? 28.146 -8.439  -1.369  1.00 24.01 ? 82  TYR B CG  1 
ATOM   1779 C CD1 . TYR B 1 82  ? 29.122 -9.312  -0.911  1.00 24.65 ? 82  TYR B CD1 1 
ATOM   1780 C CD2 . TYR B 1 82  ? 28.410 -7.718  -2.517  1.00 26.76 ? 82  TYR B CD2 1 
ATOM   1781 C CE1 . TYR B 1 82  ? 30.306 -9.500  -1.609  1.00 25.71 ? 82  TYR B CE1 1 
ATOM   1782 C CE2 . TYR B 1 82  ? 29.590 -7.885  -3.220  1.00 26.94 ? 82  TYR B CE2 1 
ATOM   1783 C CZ  . TYR B 1 82  ? 30.540 -8.778  -2.768  1.00 26.51 ? 82  TYR B CZ  1 
ATOM   1784 O OH  . TYR B 1 82  ? 31.701 -8.871  -3.480  1.00 31.25 ? 82  TYR B OH  1 
ATOM   1785 N N   . ARG B 1 83  ? 27.377 -5.170  0.114   1.00 21.47 ? 83  ARG B N   1 
ATOM   1786 C CA  . ARG B 1 83  ? 28.171 -3.960  -0.057  1.00 22.08 ? 83  ARG B CA  1 
ATOM   1787 C C   . ARG B 1 83  ? 28.656 -3.405  1.291   1.00 23.09 ? 83  ARG B C   1 
ATOM   1788 O O   . ARG B 1 83  ? 29.700 -2.745  1.361   1.00 25.65 ? 83  ARG B O   1 
ATOM   1789 C CB  . ARG B 1 83  ? 27.361 -2.932  -0.843  1.00 21.66 ? 83  ARG B CB  1 
ATOM   1790 C CG  . ARG B 1 83  ? 27.053 -3.344  -2.275  1.00 22.16 ? 83  ARG B CG  1 
ATOM   1791 C CD  . ARG B 1 83  ? 26.598 -2.171  -3.124  1.00 24.13 ? 83  ARG B CD  1 
ATOM   1792 N NE  . ARG B 1 83  ? 27.710 -1.249  -3.324  1.00 24.96 ? 83  ARG B NE  1 
ATOM   1793 C CZ  . ARG B 1 83  ? 27.638 0.077   -3.254  1.00 25.19 ? 83  ARG B CZ  1 
ATOM   1794 N NH1 . ARG B 1 83  ? 26.466 0.679   -3.177  1.00 24.44 ? 83  ARG B NH1 1 
ATOM   1795 N NH2 . ARG B 1 83  ? 28.749 0.803   -3.271  1.00 27.36 ? 83  ARG B NH2 1 
ATOM   1796 N N   . LEU B 1 84  ? 27.879 -3.624  2.353   1.00 23.94 ? 84  LEU B N   1 
ATOM   1797 C CA  . LEU B 1 84  ? 28.252 -3.188  3.691   1.00 25.87 ? 84  LEU B CA  1 
ATOM   1798 C C   . LEU B 1 84  ? 29.205 -4.174  4.374   1.00 26.37 ? 84  LEU B C   1 
ATOM   1799 O O   . LEU B 1 84  ? 29.617 -3.929  5.501   1.00 29.12 ? 84  LEU B O   1 
ATOM   1800 C CB  . LEU B 1 84  ? 26.975 -3.004  4.516   1.00 26.62 ? 84  LEU B CB  1 
ATOM   1801 C CG  . LEU B 1 84  ? 26.062 -1.850  4.096   1.00 27.11 ? 84  LEU B CG  1 
ATOM   1802 C CD1 . LEU B 1 84  ? 24.782 -1.856  4.916   1.00 29.56 ? 84  LEU B CD1 1 
ATOM   1803 C CD2 . LEU B 1 84  ? 26.761 -0.510  4.237   1.00 26.68 ? 84  LEU B CD2 1 
ATOM   1804 N N   . LYS B 1 85  ? 29.560 -5.269  3.686   1.00 26.98 ? 85  LYS B N   1 
ATOM   1805 C CA  . LYS B 1 85  ? 30.375 -6.352  4.226   1.00 27.81 ? 85  LYS B CA  1 
ATOM   1806 C C   . LYS B 1 85  ? 29.680 -7.010  5.416   1.00 27.54 ? 85  LYS B C   1 
ATOM   1807 O O   . LYS B 1 85  ? 30.338 -7.621  6.256   1.00 32.44 ? 85  LYS B O   1 
ATOM   1808 C CB  . LYS B 1 85  ? 31.784 -5.855  4.573   1.00 28.85 ? 85  LYS B CB  1 
ATOM   1809 C CG  . LYS B 1 85  ? 32.503 -5.158  3.424   1.00 31.75 ? 85  LYS B CG  1 
ATOM   1810 C CD  . LYS B 1 85  ? 33.918 -4.745  3.753   1.00 35.00 ? 85  LYS B CD  1 
ATOM   1811 C CE  . LYS B 1 85  ? 34.474 -3.732  2.777   1.00 39.49 ? 85  LYS B CE  1 
ATOM   1812 N NZ  . LYS B 1 85  ? 35.839 -3.323  3.172   1.00 42.68 ? 85  LYS B NZ  1 
ATOM   1813 N N   . GLU B 1 86  ? 28.343 -6.949  5.424   1.00 27.80 ? 86  GLU B N   1 
ATOM   1814 C CA  . GLU B 1 86  ? 27.507 -7.710  6.337   1.00 29.39 ? 86  GLU B CA  1 
ATOM   1815 C C   . GLU B 1 86  ? 27.225 -9.078  5.717   1.00 27.78 ? 86  GLU B C   1 
ATOM   1816 O O   . GLU B 1 86  ? 26.102 -9.362  5.294   1.00 26.82 ? 86  GLU B O   1 
ATOM   1817 C CB  . GLU B 1 86  ? 26.215 -6.939  6.595   1.00 32.78 ? 86  GLU B CB  1 
ATOM   1818 C CG  . GLU B 1 86  ? 26.412 -5.733  7.486   1.00 36.02 ? 86  GLU B CG  1 
ATOM   1819 C CD  . GLU B 1 86  ? 25.994 -5.977  8.926   1.00 41.49 ? 86  GLU B CD  1 
ATOM   1820 O OE1 . GLU B 1 86  ? 26.102 -7.133  9.396   1.00 45.68 ? 86  GLU B OE1 1 
ATOM   1821 O OE2 . GLU B 1 86  ? 25.548 -5.015  9.569   1.00 47.26 ? 86  GLU B OE2 1 
ATOM   1822 N N   . TYR B 1 87  ? 28.256 -9.925  5.656   1.00 27.83 ? 87  TYR B N   1 
ATOM   1823 C CA  . TYR B 1 87  ? 28.202 -11.111 4.804   1.00 27.56 ? 87  TYR B CA  1 
ATOM   1824 C C   . TYR B 1 87  ? 27.198 -12.150 5.303   1.00 27.19 ? 87  TYR B C   1 
ATOM   1825 O O   . TYR B 1 87  ? 26.533 -12.793 4.489   1.00 24.86 ? 87  TYR B O   1 
ATOM   1826 C CB  . TYR B 1 87  ? 29.600 -11.707 4.641   1.00 28.49 ? 87  TYR B CB  1 
ATOM   1827 C CG  . TYR B 1 87  ? 30.622 -10.790 4.021   1.00 29.59 ? 87  TYR B CG  1 
ATOM   1828 C CD1 . TYR B 1 87  ? 30.363 -10.127 2.833   1.00 28.67 ? 87  TYR B CD1 1 
ATOM   1829 C CD2 . TYR B 1 87  ? 31.861 -10.603 4.609   1.00 30.06 ? 87  TYR B CD2 1 
ATOM   1830 C CE1 . TYR B 1 87  ? 31.304 -9.295  2.250   1.00 29.02 ? 87  TYR B CE1 1 
ATOM   1831 C CE2 . TYR B 1 87  ? 32.809 -9.767  4.043   1.00 30.96 ? 87  TYR B CE2 1 
ATOM   1832 C CZ  . TYR B 1 87  ? 32.531 -9.112  2.858   1.00 29.72 ? 87  TYR B CZ  1 
ATOM   1833 O OH  . TYR B 1 87  ? 33.460 -8.272  2.285   1.00 34.20 ? 87  TYR B OH  1 
ATOM   1834 N N   . GLU B 1 88  ? 27.098 -12.340 6.625   1.00 29.93 ? 88  GLU B N   1 
ATOM   1835 C CA  . GLU B 1 88  ? 26.177 -13.324 7.178   1.00 31.56 ? 88  GLU B CA  1 
ATOM   1836 C C   . GLU B 1 88  ? 24.722 -12.955 6.872   1.00 27.72 ? 88  GLU B C   1 
ATOM   1837 O O   . GLU B 1 88  ? 23.915 -13.818 6.539   1.00 29.45 ? 88  GLU B O   1 
ATOM   1838 C CB  . GLU B 1 88  ? 26.420 -13.498 8.679   1.00 35.94 ? 88  GLU B CB  1 
ATOM   1839 C CG  . GLU B 1 88  ? 27.692 -14.266 8.991   1.00 41.31 ? 88  GLU B CG  1 
ATOM   1840 C CD  . GLU B 1 88  ? 27.597 -15.782 8.881   1.00 47.34 ? 88  GLU B CD  1 
ATOM   1841 O OE1 . GLU B 1 88  ? 26.574 -16.284 8.368   1.00 54.05 ? 88  GLU B OE1 1 
ATOM   1842 O OE2 . GLU B 1 88  ? 28.540 -16.466 9.332   1.00 55.26 ? 88  GLU B OE2 1 
ATOM   1843 N N   . LYS B 1 89  ? 24.367 -11.678 7.020   1.00 26.60 ? 89  LYS B N   1 
ATOM   1844 C CA  . LYS B 1 89  ? 23.027 -11.229 6.681   1.00 27.34 ? 89  LYS B CA  1 
ATOM   1845 C C   . LYS B 1 89  ? 22.791 -11.376 5.180   1.00 25.59 ? 89  LYS B C   1 
ATOM   1846 O O   . LYS B 1 89  ? 21.729 -11.827 4.768   1.00 25.44 ? 89  LYS B O   1 
ATOM   1847 C CB  . LYS B 1 89  ? 22.812 -9.772  7.106   1.00 31.36 ? 89  LYS B CB  1 
ATOM   1848 C CG  . LYS B 1 89  ? 23.051 -9.503  8.586   1.00 37.34 ? 89  LYS B CG  1 
ATOM   1849 C CD  . LYS B 1 89  ? 22.843 -8.070  9.019   1.00 43.19 ? 89  LYS B CD  1 
ATOM   1850 C CE  . LYS B 1 89  ? 21.488 -7.829  9.647   1.00 47.47 ? 89  LYS B CE  1 
ATOM   1851 N NZ  . LYS B 1 89  ? 21.532 -6.684  10.587  1.00 50.87 ? 89  LYS B NZ  1 
ATOM   1852 N N   . ALA B 1 90  ? 23.774 -10.969 4.365   1.00 26.03 ? 90  ALA B N   1 
ATOM   1853 C CA  . ALA B 1 90  ? 23.657 -11.118 2.921   1.00 23.50 ? 90  ALA B CA  1 
ATOM   1854 C C   . ALA B 1 90  ? 23.396 -12.573 2.552   1.00 24.57 ? 90  ALA B C   1 
ATOM   1855 O O   . ALA B 1 90  ? 22.538 -12.846 1.721   1.00 24.00 ? 90  ALA B O   1 
ATOM   1856 C CB  . ALA B 1 90  ? 24.882 -10.608 2.212   1.00 23.00 ? 90  ALA B CB  1 
ATOM   1857 N N   . LEU B 1 91  ? 24.101 -13.494 3.221   1.00 24.63 ? 91  LEU B N   1 
ATOM   1858 C CA  . LEU B 1 91  ? 24.002 -14.895 2.869   1.00 25.92 ? 91  LEU B CA  1 
ATOM   1859 C C   . LEU B 1 91  ? 22.626 -15.434 3.264   1.00 25.47 ? 91  LEU B C   1 
ATOM   1860 O O   . LEU B 1 91  ? 22.039 -16.212 2.523   1.00 27.07 ? 91  LEU B O   1 
ATOM   1861 C CB  . LEU B 1 91  ? 25.152 -15.656 3.534   1.00 27.81 ? 91  LEU B CB  1 
ATOM   1862 C CG  . LEU B 1 91  ? 25.355 -17.102 3.089   1.00 30.14 ? 91  LEU B CG  1 
ATOM   1863 C CD1 . LEU B 1 91  ? 25.642 -17.187 1.592   1.00 30.98 ? 91  LEU B CD1 1 
ATOM   1864 C CD2 . LEU B 1 91  ? 26.490 -17.724 3.894   1.00 31.12 ? 91  LEU B CD2 1 
ATOM   1865 N N   . LYS B 1 92  ? 22.097 -15.017 4.415   1.00 26.91 ? 92  LYS B N   1 
ATOM   1866 C CA  . LYS B 1 92  ? 20.784 -15.479 4.843   1.00 28.31 ? 92  LYS B CA  1 
ATOM   1867 C C   . LYS B 1 92  ? 19.727 -15.020 3.839   1.00 27.17 ? 92  LYS B C   1 
ATOM   1868 O O   . LYS B 1 92  ? 18.844 -15.795 3.476   1.00 28.04 ? 92  LYS B O   1 
ATOM   1869 C CB  . LYS B 1 92  ? 20.444 -14.986 6.253   1.00 32.10 ? 92  LYS B CB  1 
ATOM   1870 C CG  . LYS B 1 92  ? 21.153 -15.707 7.390   1.00 38.40 ? 92  LYS B CG  1 
ATOM   1871 C CD  . LYS B 1 92  ? 20.807 -15.120 8.748   1.00 43.86 ? 92  LYS B CD  1 
ATOM   1872 C CE  . LYS B 1 92  ? 21.644 -15.678 9.877   1.00 47.30 ? 92  LYS B CE  1 
ATOM   1873 N NZ  . LYS B 1 92  ? 21.293 -15.042 11.170  1.00 51.65 ? 92  LYS B NZ  1 
ATOM   1874 N N   . TYR B 1 93  ? 19.824 -13.767 3.367   1.00 27.05 ? 93  TYR B N   1 
ATOM   1875 C CA  . TYR B 1 93  ? 18.843 -13.286 2.415   1.00 26.08 ? 93  TYR B CA  1 
ATOM   1876 C C   . TYR B 1 93  ? 18.940 -14.063 1.104   1.00 24.76 ? 93  TYR B C   1 
ATOM   1877 O O   . TYR B 1 93  ? 17.922 -14.471 0.565   1.00 25.06 ? 93  TYR B O   1 
ATOM   1878 C CB  . TYR B 1 93  ? 18.990 -11.784 2.160   1.00 25.34 ? 93  TYR B CB  1 
ATOM   1879 C CG  . TYR B 1 93  ? 18.346 -10.897 3.196   1.00 26.50 ? 93  TYR B CG  1 
ATOM   1880 C CD1 . TYR B 1 93  ? 16.976 -10.929 3.413   1.00 26.11 ? 93  TYR B CD1 1 
ATOM   1881 C CD2 . TYR B 1 93  ? 19.097 -9.992  3.931   1.00 27.55 ? 93  TYR B CD2 1 
ATOM   1882 C CE1 . TYR B 1 93  ? 16.370 -10.097 4.340   1.00 27.58 ? 93  TYR B CE1 1 
ATOM   1883 C CE2 . TYR B 1 93  ? 18.511 -9.170  4.876   1.00 28.32 ? 93  TYR B CE2 1 
ATOM   1884 C CZ  . TYR B 1 93  ? 17.144 -9.218  5.081   1.00 28.76 ? 93  TYR B CZ  1 
ATOM   1885 O OH  . TYR B 1 93  ? 16.582 -8.367  6.007   1.00 33.70 ? 93  TYR B OH  1 
ATOM   1886 N N   . VAL B 1 94  ? 20.155 -14.251 0.573   1.00 25.25 ? 94  VAL B N   1 
ATOM   1887 C CA  . VAL B 1 94  ? 20.280 -14.830 -0.756  1.00 26.10 ? 94  VAL B CA  1 
ATOM   1888 C C   . VAL B 1 94  ? 19.959 -16.324 -0.716  1.00 26.09 ? 94  VAL B C   1 
ATOM   1889 O O   . VAL B 1 94  ? 19.447 -16.852 -1.696  1.00 27.44 ? 94  VAL B O   1 
ATOM   1890 C CB  . VAL B 1 94  ? 21.650 -14.566 -1.403  1.00 25.99 ? 94  VAL B CB  1 
ATOM   1891 C CG1 . VAL B 1 94  ? 22.757 -15.407 -0.797  1.00 26.85 ? 94  VAL B CG1 1 
ATOM   1892 C CG2 . VAL B 1 94  ? 21.582 -14.754 -2.914  1.00 26.11 ? 94  VAL B CG2 1 
ATOM   1893 N N   . ARG B 1 95  ? 20.250 -16.997 0.408   1.00 26.21 ? 95  ARG B N   1 
ATOM   1894 C CA  . ARG B 1 95  ? 19.876 -18.395 0.567   1.00 27.59 ? 95  ARG B CA  1 
ATOM   1895 C C   . ARG B 1 95  ? 18.360 -18.561 0.594   1.00 28.69 ? 95  ARG B C   1 
ATOM   1896 O O   . ARG B 1 95  ? 17.843 -19.504 -0.015  1.00 31.03 ? 95  ARG B O   1 
ATOM   1897 C CB  . ARG B 1 95  ? 20.549 -18.967 1.813   1.00 30.42 ? 95  ARG B CB  1 
ATOM   1898 C CG  . ARG B 1 95  ? 22.015 -19.307 1.601   1.00 34.49 ? 95  ARG B CG  1 
ATOM   1899 C CD  . ARG B 1 95  ? 22.595 -19.948 2.839   1.00 38.76 ? 95  ARG B CD  1 
ATOM   1900 N NE  . ARG B 1 95  ? 23.986 -20.334 2.658   1.00 44.65 ? 95  ARG B NE  1 
ATOM   1901 C CZ  . ARG B 1 95  ? 24.758 -20.841 3.616   1.00 48.62 ? 95  ARG B CZ  1 
ATOM   1902 N NH1 . ARG B 1 95  ? 24.319 -20.896 4.862   1.00 49.57 ? 95  ARG B NH1 1 
ATOM   1903 N NH2 . ARG B 1 95  ? 25.977 -21.267 3.325   1.00 49.61 ? 95  ARG B NH2 1 
ATOM   1904 N N   . GLY B 1 96  ? 17.654 -17.656 1.286   1.00 28.99 ? 96  GLY B N   1 
ATOM   1905 C CA  . GLY B 1 96  ? 16.197 -17.653 1.296   1.00 29.00 ? 96  GLY B CA  1 
ATOM   1906 C C   . GLY B 1 96  ? 15.611 -17.483 -0.106  1.00 29.64 ? 96  GLY B C   1 
ATOM   1907 O O   . GLY B 1 96  ? 14.665 -18.174 -0.479  1.00 31.60 ? 96  GLY B O   1 
ATOM   1908 N N   . LEU B 1 97  ? 16.199 -16.582 -0.901  1.00 28.15 ? 97  LEU B N   1 
ATOM   1909 C CA  . LEU B 1 97  ? 15.761 -16.362 -2.268  1.00 29.64 ? 97  LEU B CA  1 
ATOM   1910 C C   . LEU B 1 97  ? 15.948 -17.638 -3.087  1.00 31.28 ? 97  LEU B C   1 
ATOM   1911 O O   . LEU B 1 97  ? 15.056 -18.025 -3.840  1.00 30.15 ? 97  LEU B O   1 
ATOM   1912 C CB  . LEU B 1 97  ? 16.546 -15.180 -2.858  1.00 29.37 ? 97  LEU B CB  1 
ATOM   1913 C CG  . LEU B 1 97  ? 16.239 -14.823 -4.310  1.00 31.13 ? 97  LEU B CG  1 
ATOM   1914 C CD1 . LEU B 1 97  ? 14.755 -14.572 -4.525  1.00 30.04 ? 97  LEU B CD1 1 
ATOM   1915 C CD2 . LEU B 1 97  ? 17.042 -13.603 -4.734  1.00 32.47 ? 97  LEU B CD2 1 
ATOM   1916 N N   . LEU B 1 98  ? 17.079 -18.328 -2.871  1.00 30.25 ? 98  LEU B N   1 
ATOM   1917 C CA  . LEU B 1 98  ? 17.419 -19.505 -3.655  1.00 31.34 ? 98  LEU B CA  1 
ATOM   1918 C C   . LEU B 1 98  ? 16.546 -20.694 -3.256  1.00 31.75 ? 98  LEU B C   1 
ATOM   1919 O O   . LEU B 1 98  ? 16.397 -21.611 -4.053  1.00 34.86 ? 98  LEU B O   1 
ATOM   1920 C CB  . LEU B 1 98  ? 18.907 -19.808 -3.474  1.00 29.87 ? 98  LEU B CB  1 
ATOM   1921 C CG  . LEU B 1 98  ? 19.832 -18.930 -4.315  1.00 30.70 ? 98  LEU B CG  1 
ATOM   1922 C CD1 . LEU B 1 98  ? 21.274 -19.063 -3.869  1.00 33.98 ? 98  LEU B CD1 1 
ATOM   1923 C CD2 . LEU B 1 98  ? 19.704 -19.284 -5.786  1.00 31.74 ? 98  LEU B CD2 1 
ATOM   1924 N N   . GLN B 1 99  ? 15.965 -20.665 -2.051  1.00 32.00 ? 99  GLN B N   1 
ATOM   1925 C CA  . GLN B 1 99  ? 14.996 -21.677 -1.644  1.00 34.25 ? 99  GLN B CA  1 
ATOM   1926 C C   . GLN B 1 99  ? 13.679 -21.501 -2.401  1.00 35.62 ? 99  GLN B C   1 
ATOM   1927 O O   . GLN B 1 99  ? 13.038 -22.487 -2.773  1.00 35.90 ? 99  GLN B O   1 
ATOM   1928 C CB  . GLN B 1 99  ? 14.791 -21.636 -0.126  1.00 35.80 ? 99  GLN B CB  1 
ATOM   1929 C CG  . GLN B 1 99  ? 15.970 -22.211 0.647   1.00 34.43 ? 99  GLN B CG  1 
ATOM   1930 C CD  . GLN B 1 99  ? 15.857 -22.034 2.138   1.00 39.37 ? 99  GLN B CD  1 
ATOM   1931 O OE1 . GLN B 1 99  ? 14.895 -21.462 2.648   1.00 40.58 ? 99  GLN B OE1 1 
ATOM   1932 N NE2 . GLN B 1 99  ? 16.862 -22.525 2.849   1.00 41.91 ? 99  GLN B NE2 1 
ATOM   1933 N N   . THR B 1 100 ? 13.283 -20.244 -2.623  1.00 38.05 ? 100 THR B N   1 
ATOM   1934 C CA  . THR B 1 100 ? 12.092 -19.920 -3.390  1.00 39.76 ? 100 THR B CA  1 
ATOM   1935 C C   . THR B 1 100 ? 12.354 -20.114 -4.883  1.00 37.49 ? 100 THR B C   1 
ATOM   1936 O O   . THR B 1 100 ? 11.482 -20.581 -5.609  1.00 42.24 ? 100 THR B O   1 
ATOM   1937 C CB  . THR B 1 100 ? 11.653 -18.470 -3.134  1.00 43.48 ? 100 THR B CB  1 
ATOM   1938 O OG1 . THR B 1 100 ? 11.509 -18.270 -1.728  1.00 48.55 ? 100 THR B OG1 1 
ATOM   1939 C CG2 . THR B 1 100 ? 10.352 -18.116 -3.818  1.00 46.81 ? 100 THR B CG2 1 
ATOM   1940 N N   . GLU B 1 101 ? 13.549 -19.716 -5.335  1.00 40.63 ? 101 GLU B N   1 
ATOM   1941 C CA  . GLU B 1 101 ? 13.855 -19.618 -6.754  1.00 43.08 ? 101 GLU B CA  1 
ATOM   1942 C C   . GLU B 1 101 ? 15.204 -20.291 -7.009  1.00 40.58 ? 101 GLU B C   1 
ATOM   1943 O O   . GLU B 1 101 ? 16.219 -19.633 -7.228  1.00 41.67 ? 101 GLU B O   1 
ATOM   1944 C CB  . GLU B 1 101 ? 13.814 -18.149 -7.195  1.00 46.19 ? 101 GLU B CB  1 
ATOM   1945 C CG  . GLU B 1 101 ? 13.653 -17.981 -8.694  1.00 50.25 ? 101 GLU B CG  1 
ATOM   1946 C CD  . GLU B 1 101 ? 13.573 -16.541 -9.167  1.00 52.35 ? 101 GLU B CD  1 
ATOM   1947 O OE1 . GLU B 1 101 ? 13.620 -15.641 -8.309  1.00 50.36 ? 101 GLU B OE1 1 
ATOM   1948 O OE2 . GLU B 1 101 ? 13.468 -16.325 -10.395 1.00 59.97 ? 101 GLU B OE2 1 
ATOM   1949 N N   . PRO B 1 102 ? 15.251 -21.644 -6.979  1.00 41.14 ? 102 PRO B N   1 
ATOM   1950 C CA  . PRO B 1 102 ? 16.494 -22.390 -7.196  1.00 45.26 ? 102 PRO B CA  1 
ATOM   1951 C C   . PRO B 1 102 ? 17.263 -22.108 -8.490  1.00 46.54 ? 102 PRO B C   1 
ATOM   1952 O O   . PRO B 1 102 ? 18.478 -22.291 -8.528  1.00 48.16 ? 102 PRO B O   1 
ATOM   1953 C CB  . PRO B 1 102 ? 16.029 -23.854 -7.243  1.00 44.91 ? 102 PRO B CB  1 
ATOM   1954 C CG  . PRO B 1 102 ? 14.713 -23.876 -6.490  1.00 41.96 ? 102 PRO B CG  1 
ATOM   1955 C CD  . PRO B 1 102 ? 14.096 -22.513 -6.718  1.00 42.13 ? 102 PRO B CD  1 
ATOM   1956 N N   . GLN B 1 103 ? 16.550 -21.687 -9.543  1.00 48.19 ? 103 GLN B N   1 
ATOM   1957 C CA  . GLN B 1 103 ? 17.119 -21.542 -10.876 1.00 54.53 ? 103 GLN B CA  1 
ATOM   1958 C C   . GLN B 1 103 ? 17.596 -20.107 -11.122 1.00 49.63 ? 103 GLN B C   1 
ATOM   1959 O O   . GLN B 1 103 ? 18.008 -19.779 -12.235 1.00 65.18 ? 103 GLN B O   1 
ATOM   1960 C CB  . GLN B 1 103 ? 16.083 -21.952 -11.929 1.00 59.24 ? 103 GLN B CB  1 
ATOM   1961 C CG  . GLN B 1 103 ? 15.599 -23.395 -11.795 1.00 64.44 ? 103 GLN B CG  1 
ATOM   1962 C CD  . GLN B 1 103 ? 14.481 -23.754 -12.750 1.00 69.07 ? 103 GLN B CD  1 
ATOM   1963 O OE1 . GLN B 1 103 ? 14.607 -23.629 -13.971 1.00 69.07 ? 103 GLN B OE1 1 
ATOM   1964 N NE2 . GLN B 1 103 ? 13.369 -24.221 -12.204 1.00 70.95 ? 103 GLN B NE2 1 
ATOM   1965 N N   . ASN B 1 104 ? 17.556 -19.252 -10.088 1.00 41.29 ? 104 ASN B N   1 
ATOM   1966 C CA  . ASN B 1 104 ? 17.944 -17.856 -10.242 1.00 36.31 ? 104 ASN B CA  1 
ATOM   1967 C C   . ASN B 1 104 ? 19.469 -17.776 -10.272 1.00 35.22 ? 104 ASN B C   1 
ATOM   1968 O O   . ASN B 1 104 ? 20.119 -17.829 -9.223  1.00 32.76 ? 104 ASN B O   1 
ATOM   1969 C CB  . ASN B 1 104 ? 17.350 -16.977 -9.135  1.00 35.20 ? 104 ASN B CB  1 
ATOM   1970 C CG  . ASN B 1 104 ? 17.605 -15.494 -9.316  1.00 35.13 ? 104 ASN B CG  1 
ATOM   1971 O OD1 . ASN B 1 104 ? 18.594 -15.074 -9.912  1.00 32.28 ? 104 ASN B OD1 1 
ATOM   1972 N ND2 . ASN B 1 104 ? 16.729 -14.684 -8.751  1.00 37.43 ? 104 ASN B ND2 1 
ATOM   1973 N N   A ASN B 1 105 ? 20.015 -17.629 -11.485 0.50 34.11 ? 105 ASN B N   1 
ATOM   1974 N N   B ASN B 1 105 ? 20.030 -17.625 -11.480 0.50 34.52 ? 105 ASN B N   1 
ATOM   1975 C CA  A ASN B 1 105 ? 21.452 -17.651 -11.708 0.50 33.53 ? 105 ASN B CA  1 
ATOM   1976 C CA  B ASN B 1 105 ? 21.471 -17.659 -11.682 0.50 34.23 ? 105 ASN B CA  1 
ATOM   1977 C C   A ASN B 1 105 ? 22.120 -16.419 -11.096 0.50 31.26 ? 105 ASN B C   1 
ATOM   1978 C C   B ASN B 1 105 ? 22.133 -16.411 -11.096 0.50 31.60 ? 105 ASN B C   1 
ATOM   1979 O O   A ASN B 1 105 ? 23.279 -16.499 -10.697 0.50 31.52 ? 105 ASN B O   1 
ATOM   1980 O O   B ASN B 1 105 ? 23.300 -16.471 -10.716 0.50 32.30 ? 105 ASN B O   1 
ATOM   1981 C CB  A ASN B 1 105 ? 21.783 -17.771 -13.199 0.50 34.58 ? 105 ASN B CB  1 
ATOM   1982 C CB  B ASN B 1 105 ? 21.828 -17.818 -13.163 0.50 35.90 ? 105 ASN B CB  1 
ATOM   1983 C CG  A ASN B 1 105 ? 21.410 -19.122 -13.774 0.50 36.13 ? 105 ASN B CG  1 
ATOM   1984 C CG  B ASN B 1 105 ? 23.277 -18.192 -13.392 0.50 38.62 ? 105 ASN B CG  1 
ATOM   1985 O OD1 A ASN B 1 105 ? 21.891 -20.145 -13.304 0.50 37.32 ? 105 ASN B OD1 1 
ATOM   1986 O OD1 B ASN B 1 105 ? 23.820 -19.048 -12.694 0.50 40.28 ? 105 ASN B OD1 1 
ATOM   1987 N ND2 A ASN B 1 105 ? 20.555 -19.140 -14.783 0.50 38.37 ? 105 ASN B ND2 1 
ATOM   1988 N ND2 B ASN B 1 105 ? 23.908 -17.566 -14.372 0.50 40.23 ? 105 ASN B ND2 1 
ATOM   1989 N N   . GLN B 1 106 ? 21.400 -15.287 -11.027 1.00 30.25 ? 106 GLN B N   1 
ATOM   1990 C CA  . GLN B 1 106 ? 21.946 -14.047 -10.480 1.00 29.92 ? 106 GLN B CA  1 
ATOM   1991 C C   . GLN B 1 106 ? 22.074 -14.154 -8.959  1.00 24.80 ? 106 GLN B C   1 
ATOM   1992 O O   . GLN B 1 106 ? 23.072 -13.725 -8.388  1.00 26.33 ? 106 GLN B O   1 
ATOM   1993 C CB  . GLN B 1 106 ? 21.094 -12.836 -10.864 1.00 29.33 ? 106 GLN B CB  1 
ATOM   1994 C CG  . GLN B 1 106 ? 21.140 -12.496 -12.346 1.00 33.28 ? 106 GLN B CG  1 
ATOM   1995 C CD  . GLN B 1 106 ? 20.526 -13.574 -13.206 1.00 36.51 ? 106 GLN B CD  1 
ATOM   1996 O OE1 . GLN B 1 106 ? 19.353 -13.917 -13.062 1.00 40.80 ? 106 GLN B OE1 1 
ATOM   1997 N NE2 . GLN B 1 106 ? 21.320 -14.138 -14.099 1.00 39.49 ? 106 GLN B NE2 1 
ATOM   1998 N N   . ALA B 1 107 ? 21.093 -14.807 -8.320  1.00 26.12 ? 107 ALA B N   1 
ATOM   1999 C CA  . ALA B 1 107 ? 21.180 -15.134 -6.906  1.00 26.82 ? 107 ALA B CA  1 
ATOM   2000 C C   . ALA B 1 107 ? 22.353 -16.088 -6.629  1.00 25.25 ? 107 ALA B C   1 
ATOM   2001 O O   . ALA B 1 107 ? 23.102 -15.889 -5.683  1.00 27.18 ? 107 ALA B O   1 
ATOM   2002 C CB  . ALA B 1 107 ? 19.854 -15.702 -6.455  1.00 29.62 ? 107 ALA B CB  1 
ATOM   2003 N N   . LYS B 1 108 ? 22.569 -17.069 -7.510  1.00 26.96 ? 108 LYS B N   1 
ATOM   2004 C CA  . LYS B 1 108 ? 23.662 -18.018 -7.349  1.00 29.51 ? 108 LYS B CA  1 
ATOM   2005 C C   . LYS B 1 108 ? 25.008 -17.301 -7.436  1.00 29.84 ? 108 LYS B C   1 
ATOM   2006 O O   . LYS B 1 108 ? 25.907 -17.564 -6.638  1.00 30.44 ? 108 LYS B O   1 
ATOM   2007 C CB  . LYS B 1 108 ? 23.593 -19.106 -8.423  1.00 32.48 ? 108 LYS B CB  1 
ATOM   2008 C CG  . LYS B 1 108 ? 22.479 -20.128 -8.245  1.00 36.89 ? 108 LYS B CG  1 
ATOM   2009 C CD  . LYS B 1 108 ? 22.719 -21.453 -8.962  1.00 42.30 ? 108 LYS B CD  1 
ATOM   2010 C CE  . LYS B 1 108 ? 22.630 -22.634 -8.016  1.00 47.28 ? 108 LYS B CE  1 
ATOM   2011 N NZ  . LYS B 1 108 ? 21.780 -23.718 -8.556  1.00 51.32 ? 108 LYS B NZ  1 
ATOM   2012 N N   . GLU B 1 109 ? 25.134 -16.395 -8.413  1.00 27.81 ? 109 GLU B N   1 
ATOM   2013 C CA  . GLU B 1 109 ? 26.361 -15.630 -8.594  1.00 28.82 ? 109 GLU B CA  1 
ATOM   2014 C C   . GLU B 1 109 ? 26.620 -14.753 -7.369  1.00 27.74 ? 109 GLU B C   1 
ATOM   2015 O O   . GLU B 1 109 ? 27.765 -14.612 -6.942  1.00 27.99 ? 109 GLU B O   1 
ATOM   2016 C CB  . GLU B 1 109 ? 26.292 -14.764 -9.854  1.00 32.27 ? 109 GLU B CB  1 
ATOM   2017 C CG  . GLU B 1 109 ? 26.419 -15.548 -11.149 1.00 38.80 ? 109 GLU B CG  1 
ATOM   2018 C CD  . GLU B 1 109 ? 26.317 -14.723 -12.420 1.00 43.23 ? 109 GLU B CD  1 
ATOM   2019 O OE1 . GLU B 1 109 ? 26.249 -13.481 -12.311 1.00 49.32 ? 109 GLU B OE1 1 
ATOM   2020 O OE2 . GLU B 1 109 ? 26.320 -15.324 -13.517 1.00 49.53 ? 109 GLU B OE2 1 
ATOM   2021 N N   . LEU B 1 110 ? 25.554 -14.149 -6.819  1.00 25.88 ? 110 LEU B N   1 
ATOM   2022 C CA  . LEU B 1 110 ? 25.699 -13.275 -5.663  1.00 26.72 ? 110 LEU B CA  1 
ATOM   2023 C C   . LEU B 1 110 ? 26.157 -14.085 -4.451  1.00 25.70 ? 110 LEU B C   1 
ATOM   2024 O O   . LEU B 1 110 ? 27.060 -13.667 -3.734  1.00 25.75 ? 110 LEU B O   1 
ATOM   2025 C CB  . LEU B 1 110 ? 24.377 -12.541 -5.404  1.00 25.31 ? 110 LEU B CB  1 
ATOM   2026 C CG  . LEU B 1 110 ? 24.346 -11.577 -4.216  1.00 25.92 ? 110 LEU B CG  1 
ATOM   2027 C CD1 . LEU B 1 110 ? 25.399 -10.479 -4.334  1.00 26.00 ? 110 LEU B CD1 1 
ATOM   2028 C CD2 . LEU B 1 110 ? 22.976 -10.935 -4.088  1.00 27.83 ? 110 LEU B CD2 1 
ATOM   2029 N N   . GLU B 1 111 ? 25.568 -15.274 -4.256  1.00 26.02 ? 111 GLU B N   1 
ATOM   2030 C CA  . GLU B 1 111 ? 25.982 -16.180 -3.196  1.00 26.24 ? 111 GLU B CA  1 
ATOM   2031 C C   . GLU B 1 111 ? 27.469 -16.499 -3.347  1.00 26.04 ? 111 GLU B C   1 
ATOM   2032 O O   . GLU B 1 111 ? 28.178 -16.501 -2.357  1.00 26.43 ? 111 GLU B O   1 
ATOM   2033 C CB  . GLU B 1 111 ? 25.134 -17.453 -3.223  1.00 26.81 ? 111 GLU B CB  1 
ATOM   2034 C CG  . GLU B 1 111 ? 25.448 -18.404 -2.091  1.00 28.95 ? 111 GLU B CG  1 
ATOM   2035 C CD  . GLU B 1 111 ? 24.665 -19.703 -2.125  1.00 33.34 ? 111 GLU B CD  1 
ATOM   2036 O OE1 . GLU B 1 111 ? 24.277 -20.169 -1.051  1.00 40.04 ? 111 GLU B OE1 1 
ATOM   2037 O OE2 . GLU B 1 111 ? 24.449 -20.241 -3.230  1.00 41.81 ? 111 GLU B OE2 1 
ATOM   2038 N N   . ARG B 1 112 ? 27.946 -16.708 -4.585  1.00 27.72 ? 112 ARG B N   1 
ATOM   2039 C CA  . ARG B 1 112 ? 29.355 -17.007 -4.826  1.00 29.05 ? 112 ARG B CA  1 
ATOM   2040 C C   . ARG B 1 112 ? 30.236 -15.832 -4.390  1.00 28.80 ? 112 ARG B C   1 
ATOM   2041 O O   . ARG B 1 112 ? 31.275 -16.051 -3.758  1.00 28.51 ? 112 ARG B O   1 
ATOM   2042 C CB  . ARG B 1 112 ? 29.588 -17.361 -6.302  1.00 34.50 ? 112 ARG B CB  1 
ATOM   2043 C CG  . ARG B 1 112 ? 30.907 -18.069 -6.573  1.00 40.25 ? 112 ARG B CG  1 
ATOM   2044 C CD  . ARG B 1 112 ? 31.146 -18.368 -8.045  1.00 45.78 ? 112 ARG B CD  1 
ATOM   2045 N NE  . ARG B 1 112 ? 31.508 -17.175 -8.797  1.00 52.12 ? 112 ARG B NE  1 
ATOM   2046 C CZ  . ARG B 1 112 ? 31.896 -17.158 -10.071 1.00 59.19 ? 112 ARG B CZ  1 
ATOM   2047 N NH1 . ARG B 1 112 ? 31.926 -18.274 -10.781 1.00 62.78 ? 112 ARG B NH1 1 
ATOM   2048 N NH2 . ARG B 1 112 ? 32.250 -16.016 -10.637 1.00 62.24 ? 112 ARG B NH2 1 
ATOM   2049 N N   . LEU B 1 113 ? 29.826 -14.599 -4.731  1.00 27.81 ? 113 LEU B N   1 
ATOM   2050 C CA  . LEU B 1 113 ? 30.577 -13.406 -4.354  1.00 28.07 ? 113 LEU B CA  1 
ATOM   2051 C C   . LEU B 1 113 ? 30.671 -13.282 -2.836  1.00 26.45 ? 113 LEU B C   1 
ATOM   2052 O O   . LEU B 1 113 ? 31.723 -12.956 -2.298  1.00 26.41 ? 113 LEU B O   1 
ATOM   2053 C CB  . LEU B 1 113 ? 29.895 -12.154 -4.923  1.00 30.01 ? 113 LEU B CB  1 
ATOM   2054 C CG  . LEU B 1 113 ? 30.048 -11.891 -6.420  1.00 33.34 ? 113 LEU B CG  1 
ATOM   2055 C CD1 . LEU B 1 113 ? 29.468 -10.524 -6.753  1.00 34.64 ? 113 LEU B CD1 1 
ATOM   2056 C CD2 . LEU B 1 113 ? 31.502 -11.948 -6.859  1.00 35.28 ? 113 LEU B CD2 1 
ATOM   2057 N N   . ILE B 1 114 ? 29.546 -13.505 -2.153  1.00 26.37 ? 114 ILE B N   1 
ATOM   2058 C CA  . ILE B 1 114 ? 29.499 -13.404 -0.704  1.00 26.05 ? 114 ILE B CA  1 
ATOM   2059 C C   . ILE B 1 114 ? 30.449 -14.438 -0.100  1.00 26.19 ? 114 ILE B C   1 
ATOM   2060 O O   . ILE B 1 114 ? 31.225 -14.110 0.796   1.00 28.11 ? 114 ILE B O   1 
ATOM   2061 C CB  . ILE B 1 114 ? 28.054 -13.554 -0.187  1.00 24.68 ? 114 ILE B CB  1 
ATOM   2062 C CG1 . ILE B 1 114 ? 27.151 -12.416 -0.683  1.00 24.71 ? 114 ILE B CG1 1 
ATOM   2063 C CG2 . ILE B 1 114 ? 28.035 -13.672 1.328   1.00 26.09 ? 114 ILE B CG2 1 
ATOM   2064 C CD1 . ILE B 1 114 ? 25.668 -12.715 -0.606  1.00 24.74 ? 114 ILE B CD1 1 
ATOM   2065 N N   . ASP B 1 115 ? 30.409 -15.674 -0.629  1.00 28.74 ? 115 ASP B N   1 
ATOM   2066 C CA  . ASP B 1 115 ? 31.243 -16.760 -0.145  1.00 31.89 ? 115 ASP B CA  1 
ATOM   2067 C C   . ASP B 1 115 ? 32.722 -16.410 -0.302  1.00 30.78 ? 115 ASP B C   1 
ATOM   2068 O O   . ASP B 1 115 ? 33.505 -16.596 0.624   1.00 33.20 ? 115 ASP B O   1 
ATOM   2069 C CB  . ASP B 1 115 ? 30.931 -18.060 -0.890  1.00 33.62 ? 115 ASP B CB  1 
ATOM   2070 C CG  . ASP B 1 115 ? 29.591 -18.682 -0.527  1.00 39.16 ? 115 ASP B CG  1 
ATOM   2071 O OD1 . ASP B 1 115 ? 28.994 -18.258 0.487   1.00 46.33 ? 115 ASP B OD1 1 
ATOM   2072 O OD2 . ASP B 1 115 ? 29.144 -19.579 -1.273  1.00 41.38 ? 115 ASP B OD2 1 
ATOM   2073 N N   . LYS B 1 116 ? 33.086 -15.925 -1.490  1.00 29.92 ? 116 LYS B N   1 
ATOM   2074 C CA  . LYS B 1 116 ? 34.451 -15.541 -1.799  1.00 31.31 ? 116 LYS B CA  1 
ATOM   2075 C C   . LYS B 1 116 ? 34.941 -14.501 -0.804  1.00 29.99 ? 116 LYS B C   1 
ATOM   2076 O O   . LYS B 1 116 ? 36.041 -14.630 -0.280  1.00 29.38 ? 116 LYS B O   1 
ATOM   2077 C CB  . LYS B 1 116 ? 34.560 -15.011 -3.233  1.00 34.17 ? 116 LYS B CB  1 
ATOM   2078 C CG  . LYS B 1 116 ? 34.608 -16.110 -4.289  1.00 38.16 ? 116 LYS B CG  1 
ATOM   2079 C CD  . LYS B 1 116 ? 34.650 -15.573 -5.713  1.00 43.26 ? 116 LYS B CD  1 
ATOM   2080 C CE  . LYS B 1 116 ? 34.785 -16.670 -6.748  1.00 44.97 ? 116 LYS B CE  1 
ATOM   2081 N NZ  . LYS B 1 116 ? 36.102 -17.344 -6.662  1.00 51.01 ? 116 LYS B NZ  1 
ATOM   2082 N N   . ALA B 1 117 ? 34.115 -13.476 -0.556  1.00 28.26 ? 117 ALA B N   1 
ATOM   2083 C CA  . ALA B 1 117 ? 34.482 -12.396 0.346   1.00 28.27 ? 117 ALA B CA  1 
ATOM   2084 C C   . ALA B 1 117 ? 34.661 -12.909 1.775   1.00 28.73 ? 117 ALA B C   1 
ATOM   2085 O O   . ALA B 1 117 ? 35.606 -12.505 2.451   1.00 29.95 ? 117 ALA B O   1 
ATOM   2086 C CB  . ALA B 1 117 ? 33.445 -11.298 0.291   1.00 28.41 ? 117 ALA B CB  1 
ATOM   2087 N N   . MET B 1 118 ? 33.739 -13.772 2.229   1.00 31.28 ? 118 MET B N   1 
ATOM   2088 C CA  . MET B 1 118 ? 33.790 -14.346 3.569   1.00 32.94 ? 118 MET B CA  1 
ATOM   2089 C C   . MET B 1 118 ? 35.100 -15.100 3.776   1.00 33.36 ? 118 MET B C   1 
ATOM   2090 O O   . MET B 1 118 ? 35.701 -15.020 4.847   1.00 37.57 ? 118 MET B O   1 
ATOM   2091 C CB  . MET B 1 118 ? 32.609 -15.287 3.819   1.00 35.59 ? 118 MET B CB  1 
ATOM   2092 C CG  . MET B 1 118 ? 31.359 -14.544 4.171   1.00 38.33 ? 118 MET B CG  1 
ATOM   2093 S SD  . MET B 1 118 ? 29.911 -15.597 4.345   1.00 41.38 ? 118 MET B SD  1 
ATOM   2094 C CE  . MET B 1 118 ? 29.931 -15.862 6.115   1.00 43.87 ? 118 MET B CE  1 
ATOM   2095 N N   . LYS B 1 119 ? 35.561 -15.792 2.733   1.00 32.76 ? 119 LYS B N   1 
ATOM   2096 C CA  . LYS B 1 119 ? 36.763 -16.603 2.829   1.00 35.09 ? 119 LYS B CA  1 
ATOM   2097 C C   . LYS B 1 119 ? 38.014 -15.798 2.472   1.00 32.40 ? 119 LYS B C   1 
ATOM   2098 O O   . LYS B 1 119 ? 39.110 -16.341 2.535   1.00 33.12 ? 119 LYS B O   1 
ATOM   2099 C CB  . LYS B 1 119 ? 36.596 -17.824 1.921   1.00 35.14 ? 119 LYS B CB  1 
ATOM   2100 C CG  . LYS B 1 119 ? 35.443 -18.731 2.330   1.00 39.28 ? 119 LYS B CG  1 
ATOM   2101 C CD  . LYS B 1 119 ? 35.044 -19.753 1.300   1.00 44.70 ? 119 LYS B CD  1 
ATOM   2102 C CE  . LYS B 1 119 ? 33.819 -20.533 1.733   1.00 49.54 ? 119 LYS B CE  1 
ATOM   2103 N NZ  . LYS B 1 119 ? 33.500 -21.626 0.788   1.00 51.60 ? 119 LYS B NZ  1 
ATOM   2104 N N   . LYS B 1 120 ? 37.847 -14.516 2.100   1.00 32.08 ? 120 LYS B N   1 
ATOM   2105 C CA  . LYS B 1 120 ? 38.926 -13.638 1.660   1.00 32.62 ? 120 LYS B CA  1 
ATOM   2106 C C   . LYS B 1 120 ? 39.692 -14.280 0.506   1.00 30.31 ? 120 LYS B C   1 
ATOM   2107 O O   . LYS B 1 120 ? 40.916 -14.208 0.433   1.00 30.33 ? 120 LYS B O   1 
ATOM   2108 C CB  . LYS B 1 120 ? 39.835 -13.238 2.829   1.00 35.61 ? 120 LYS B CB  1 
ATOM   2109 C CG  . LYS B 1 120 ? 39.215 -12.253 3.811   1.00 38.83 ? 120 LYS B CG  1 
ATOM   2110 C CD  . LYS B 1 120 ? 40.195 -11.730 4.840   1.00 40.08 ? 120 LYS B CD  1 
ATOM   2111 C CE  . LYS B 1 120 ? 39.723 -10.471 5.540   1.00 41.62 ? 120 LYS B CE  1 
ATOM   2112 N NZ  . LYS B 1 120 ? 38.426 -10.678 6.228   1.00 44.64 ? 120 LYS B NZ  1 
ATOM   2113 N N   . ASP B 1 121 ? 38.946 -14.916 -0.402  1.00 31.59 ? 121 ASP B N   1 
ATOM   2114 C CA  . ASP B 1 121 ? 39.518 -15.477 -1.609  1.00 31.28 ? 121 ASP B CA  1 
ATOM   2115 C C   . ASP B 1 121 ? 40.219 -14.370 -2.386  1.00 30.81 ? 121 ASP B C   1 
ATOM   2116 O O   . ASP B 1 121 ? 39.615 -13.346 -2.661  1.00 29.18 ? 121 ASP B O   1 
ATOM   2117 C CB  . ASP B 1 121 ? 38.429 -16.120 -2.469  1.00 33.97 ? 121 ASP B CB  1 
ATOM   2118 C CG  . ASP B 1 121 ? 38.975 -16.811 -3.704  1.00 41.66 ? 121 ASP B CG  1 
ATOM   2119 O OD1 . ASP B 1 121 ? 39.653 -17.841 -3.544  1.00 47.90 ? 121 ASP B OD1 1 
ATOM   2120 O OD2 . ASP B 1 121 ? 38.727 -16.302 -4.813  1.00 49.41 ? 121 ASP B OD2 1 
ATOM   2121 N N   . GLY B 1 122 ? 41.488 -14.591 -2.739  1.00 32.52 ? 122 GLY B N   1 
ATOM   2122 C CA  . GLY B 1 122 ? 42.246 -13.639 -3.539  1.00 31.37 ? 122 GLY B CA  1 
ATOM   2123 C C   . GLY B 1 122 ? 42.963 -12.582 -2.698  1.00 28.83 ? 122 GLY B C   1 
ATOM   2124 O O   . GLY B 1 122 ? 43.429 -11.572 -3.225  1.00 31.57 ? 122 GLY B O   1 
ATOM   2125 N N   . LEU B 1 123 ? 43.076 -12.824 -1.389  1.00 27.03 ? 123 LEU B N   1 
ATOM   2126 C CA  . LEU B 1 123 ? 43.875 -11.965 -0.531  1.00 26.31 ? 123 LEU B CA  1 
ATOM   2127 C C   . LEU B 1 123 ? 45.314 -11.956 -1.046  1.00 25.77 ? 123 LEU B C   1 
ATOM   2128 O O   . LEU B 1 123 ? 45.881 -13.008 -1.329  1.00 28.09 ? 123 LEU B O   1 
ATOM   2129 C CB  . LEU B 1 123 ? 43.790 -12.478 0.907   1.00 28.22 ? 123 LEU B CB  1 
ATOM   2130 C CG  . LEU B 1 123 ? 44.465 -11.627 1.977   1.00 28.92 ? 123 LEU B CG  1 
ATOM   2131 C CD1 . LEU B 1 123 ? 43.661 -10.359 2.223   1.00 29.75 ? 123 LEU B CD1 1 
ATOM   2132 C CD2 . LEU B 1 123 ? 44.630 -12.430 3.264   1.00 30.06 ? 123 LEU B CD2 1 
ATOM   2133 N N   . LEU B 1 124 ? 45.896 -10.755 -1.159  1.00 25.78 ? 124 LEU B N   1 
ATOM   2134 C CA  . LEU B 1 124 ? 47.168 -10.581 -1.852  1.00 28.58 ? 124 LEU B CA  1 
ATOM   2135 C C   . LEU B 1 124 ? 48.367 -10.737 -0.917  1.00 28.64 ? 124 LEU B C   1 
ATOM   2136 O O   . LEU B 1 124 ? 49.433 -11.184 -1.343  1.00 28.78 ? 124 LEU B O   1 
ATOM   2137 C CB  . LEU B 1 124 ? 47.199 -9.200  -2.508  1.00 29.57 ? 124 LEU B CB  1 
ATOM   2138 C CG  . LEU B 1 124 ? 46.130 -8.948  -3.567  1.00 31.33 ? 124 LEU B CG  1 
ATOM   2139 C CD1 . LEU B 1 124 ? 46.295 -7.554  -4.155  1.00 33.08 ? 124 LEU B CD1 1 
ATOM   2140 C CD2 . LEU B 1 124 ? 46.203 -9.998  -4.665  1.00 32.55 ? 124 LEU B CD2 1 
ATOM   2141 N N   . GLU B 1 125 ? 48.224 -10.326 0.341   1.00 27.34 ? 125 GLU B N   1 
ATOM   2142 C CA  . GLU B 1 125 ? 49.392 -10.178 1.197   1.00 31.08 ? 125 GLU B CA  1 
ATOM   2143 C C   . GLU B 1 125 ? 50.109 -11.525 1.345   1.00 32.79 ? 125 GLU B C   1 
ATOM   2144 O O   . GLU B 1 125 ? 51.335 -11.556 1.381   1.00 32.77 ? 125 GLU B O   1 
ATOM   2145 C CB  . GLU B 1 125 ? 49.020 -9.520  2.531   1.00 33.94 ? 125 GLU B CB  1 
ATOM   2146 C CG  . GLU B 1 125 ? 47.949 -10.246 3.336   1.00 38.45 ? 125 GLU B CG  1 
ATOM   2147 C CD  . GLU B 1 125 ? 47.619 -9.575  4.662   1.00 45.50 ? 125 GLU B CD  1 
ATOM   2148 O OE1 . GLU B 1 125 ? 48.351 -8.638  5.055   1.00 49.41 ? 125 GLU B OE1 1 
ATOM   2149 O OE2 . GLU B 1 125 ? 46.631 -9.982  5.301   1.00 53.05 ? 125 GLU B OE2 1 
ATOM   2150 N N   . VAL B 1 126 ? 49.346 -12.625 1.338   1.00 33.58 ? 126 VAL B N   1 
ATOM   2151 C CA  . VAL B 1 126 ? 49.901 -13.955 1.585   1.00 35.31 ? 126 VAL B CA  1 
ATOM   2152 C C   . VAL B 1 126 ? 50.837 -14.407 0.456   1.00 33.96 ? 126 VAL B C   1 
ATOM   2153 O O   . VAL B 1 126 ? 51.573 -15.388 0.610   1.00 34.56 ? 126 VAL B O   1 
ATOM   2154 C CB  . VAL B 1 126 ? 48.783 -14.992 1.841   1.00 36.00 ? 126 VAL B CB  1 
ATOM   2155 C CG1 . VAL B 1 126 ? 47.928 -14.610 3.039   1.00 37.60 ? 126 VAL B CG1 1 
ATOM   2156 C CG2 . VAL B 1 126 ? 47.901 -15.235 0.627   1.00 35.87 ? 126 VAL B CG2 1 
ATOM   2157 N N   . LEU B 1 127 ? 50.809 -13.716 -0.686  1.00 33.69 ? 127 LEU B N   1 
ATOM   2158 C CA  . LEU B 1 127 ? 51.615 -14.078 -1.843  1.00 34.09 ? 127 LEU B CA  1 
ATOM   2159 C C   . LEU B 1 127 ? 53.042 -13.527 -1.734  1.00 35.39 ? 127 LEU B C   1 
ATOM   2160 O O   . LEU B 1 127 ? 53.907 -13.926 -2.517  1.00 37.00 ? 127 LEU B O   1 
ATOM   2161 C CB  . LEU B 1 127 ? 50.924 -13.540 -3.103  1.00 36.58 ? 127 LEU B CB  1 
ATOM   2162 C CG  . LEU B 1 127 ? 49.454 -13.931 -3.268  1.00 38.79 ? 127 LEU B CG  1 
ATOM   2163 C CD1 . LEU B 1 127 ? 48.821 -13.164 -4.415  1.00 40.59 ? 127 LEU B CD1 1 
ATOM   2164 C CD2 . LEU B 1 127 ? 49.295 -15.433 -3.473  1.00 39.47 ? 127 LEU B CD2 1 
ATOM   2165 N N   . PHE B 1 128 ? 53.299 -12.629 -0.771  1.00 32.11 ? 128 PHE B N   1 
ATOM   2166 C CA  . PHE B 1 128 ? 54.571 -11.922 -0.704  1.00 32.53 ? 128 PHE B CA  1 
ATOM   2167 C C   . PHE B 1 128 ? 55.294 -12.215 0.611   1.00 36.31 ? 128 PHE B C   1 
ATOM   2168 O O   . PHE B 1 128 ? 56.087 -11.403 1.099   1.00 39.86 ? 128 PHE B O   1 
ATOM   2169 C CB  . PHE B 1 128 ? 54.320 -10.424 -0.893  1.00 30.75 ? 128 PHE B CB  1 
ATOM   2170 C CG  . PHE B 1 128 ? 53.550 -10.097 -2.145  1.00 29.45 ? 128 PHE B CG  1 
ATOM   2171 C CD1 . PHE B 1 128 ? 54.049 -10.447 -3.389  1.00 31.61 ? 128 PHE B CD1 1 
ATOM   2172 C CD2 . PHE B 1 128 ? 52.318 -9.464  -2.085  1.00 31.24 ? 128 PHE B CD2 1 
ATOM   2173 C CE1 . PHE B 1 128 ? 53.329 -10.179 -4.542  1.00 31.47 ? 128 PHE B CE1 1 
ATOM   2174 C CE2 . PHE B 1 128 ? 51.615 -9.169  -3.243  1.00 32.24 ? 128 PHE B CE2 1 
ATOM   2175 C CZ  . PHE B 1 128 ? 52.113 -9.541  -4.468  1.00 30.05 ? 128 PHE B CZ  1 
ATOM   2176 N N   . GLN B 1 129 ? 55.046 -13.392 1.173   1.00 41.36 ? 129 GLN B N   1 
ATOM   2177 C CA  . GLN B 1 129 ? 55.574 -13.722 2.487   1.00 44.65 ? 129 GLN B CA  1 
ATOM   2178 C C   . GLN B 1 129 ? 56.824 -14.595 2.327   1.00 49.43 ? 129 GLN B C   1 
ATOM   2179 O O   . GLN B 1 129 ? 57.267 -14.745 1.167   1.00 55.31 ? 129 GLN B O   1 
ATOM   2180 C CB  . GLN B 1 129 ? 54.485 -14.401 3.318   1.00 48.18 ? 129 GLN B CB  1 
ATOM   2181 C CG  . GLN B 1 129 ? 53.953 -15.678 2.690   1.00 51.29 ? 129 GLN B CG  1 
ATOM   2182 C CD  . GLN B 1 129 ? 52.794 -16.301 3.433   1.00 53.74 ? 129 GLN B CD  1 
ATOM   2183 O OE1 . GLN B 1 129 ? 52.415 -17.430 3.152   1.00 55.07 ? 129 GLN B OE1 1 
ATOM   2184 N NE2 . GLN B 1 129 ? 52.203 -15.578 4.374   1.00 58.01 ? 129 GLN B NE2 1 
HETATM 2185 C C1  . PGE C 2 .   ? 9.480  -4.814  40.209  1.00 39.79 ? 201 PGE A C1  1 
HETATM 2186 O O1  . PGE C 2 .   ? 9.250  -5.908  39.323  1.00 42.40 ? 201 PGE A O1  1 
HETATM 2187 C C2  . PGE C 2 .   ? 8.823  -3.584  39.611  1.00 40.02 ? 201 PGE A C2  1 
HETATM 2188 O O2  . PGE C 2 .   ? 9.516  -3.165  38.433  1.00 41.63 ? 201 PGE A O2  1 
HETATM 2189 C C3  . PGE C 2 .   ? 8.776  -2.150  37.735  1.00 40.73 ? 201 PGE A C3  1 
HETATM 2190 C C4  . PGE C 2 .   ? 9.646  -1.023  37.192  1.00 44.11 ? 201 PGE A C4  1 
HETATM 2191 O O4  . PGE C 2 .   ? 13.682 -1.591  35.769  1.00 50.35 ? 201 PGE A O4  1 
HETATM 2192 C C6  . PGE C 2 .   ? 12.981 -0.383  36.063  1.00 49.63 ? 201 PGE A C6  1 
HETATM 2193 C C5  . PGE C 2 .   ? 11.505 -0.559  35.736  1.00 47.41 ? 201 PGE A C5  1 
HETATM 2194 O O3  . PGE C 2 .   ? 10.916 -1.430  36.709  1.00 45.12 ? 201 PGE A O3  1 
HETATM 2195 C C   . ACT D 3 .   ? 26.354 -2.046  39.748  1.00 42.54 ? 202 ACT A C   1 
HETATM 2196 O O   . ACT D 3 .   ? 27.525 -2.392  39.512  1.00 50.03 ? 202 ACT A O   1 
HETATM 2197 O OXT . ACT D 3 .   ? 26.046 -1.089  40.479  1.00 35.78 ? 202 ACT A OXT 1 
HETATM 2198 C CH3 . ACT D 3 .   ? 25.233 -2.817  39.100  1.00 43.97 ? 202 ACT A CH3 1 
HETATM 2199 C C1  . PGE E 2 .   ? 11.789 10.369  -20.621 1.00 37.74 ? 201 PGE B C1  1 
HETATM 2200 O O1  . PGE E 2 .   ? 11.414 11.476  -19.805 1.00 39.83 ? 201 PGE B O1  1 
HETATM 2201 C C2  . PGE E 2 .   ? 10.871 9.217   -20.290 1.00 35.53 ? 201 PGE B C2  1 
HETATM 2202 O O2  . PGE E 2 .   ? 11.187 8.626   -19.029 1.00 34.50 ? 201 PGE B O2  1 
HETATM 2203 C C3  . PGE E 2 .   ? 10.275 7.543   -18.767 1.00 34.14 ? 201 PGE B C3  1 
HETATM 2204 C C4  . PGE E 2 .   ? 10.766 6.488   -17.793 1.00 39.23 ? 201 PGE B C4  1 
HETATM 2205 O O4  . PGE E 2 .   ? 14.836 6.253   -16.165 1.00 46.71 ? 201 PGE B O4  1 
HETATM 2206 C C6  . PGE E 2 .   ? 13.936 5.217   -16.570 1.00 43.81 ? 201 PGE B C6  1 
HETATM 2207 C C5  . PGE E 2 .   ? 12.489 5.679   -16.406 1.00 41.71 ? 201 PGE B C5  1 
HETATM 2208 O O3  . PGE E 2 .   ? 12.140 6.579   -17.464 1.00 39.95 ? 201 PGE B O3  1 
HETATM 2209 O O   . HOH F 4 .   ? 40.137 19.465  21.698  1.00 41.16 ? 301 HOH A O   1 
HETATM 2210 O O   . HOH F 4 .   ? 29.352 24.092  24.376  1.00 55.80 ? 302 HOH A O   1 
HETATM 2211 O O   . HOH F 4 .   ? 11.805 -3.111  17.200  1.00 47.97 ? 303 HOH A O   1 
HETATM 2212 O O   . HOH F 4 .   ? 5.879  15.273  27.146  1.00 36.72 ? 304 HOH A O   1 
HETATM 2213 O O   . HOH F 4 .   ? 8.186  9.361   12.518  1.00 39.24 ? 305 HOH A O   1 
HETATM 2214 O O   . HOH F 4 .   ? 30.856 21.683  25.262  1.00 38.60 ? 306 HOH A O   1 
HETATM 2215 O O   . HOH F 4 .   ? 6.849  1.769   28.722  1.00 41.67 ? 307 HOH A O   1 
HETATM 2216 O O   . HOH F 4 .   ? 9.686  -1.038  18.426  1.00 43.13 ? 308 HOH A O   1 
HETATM 2217 O O   . HOH F 4 .   ? 35.531 7.602   20.143  1.00 39.13 ? 309 HOH A O   1 
HETATM 2218 O O   . HOH F 4 .   ? 20.701 -2.547  12.654  1.00 30.23 ? 310 HOH A O   1 
HETATM 2219 O O   . HOH F 4 .   ? 21.587 9.629   13.000  1.00 23.43 ? 311 HOH A O   1 
HETATM 2220 O O   . HOH F 4 .   ? 47.631 12.512  21.218  1.00 35.48 ? 312 HOH A O   1 
HETATM 2221 O O   . HOH F 4 .   ? 23.790 7.312   12.026  1.00 32.50 ? 313 HOH A O   1 
HETATM 2222 O O   . HOH F 4 .   ? 30.719 2.840   42.660  1.00 46.93 ? 314 HOH A O   1 
HETATM 2223 O O   . HOH F 4 .   ? 13.291 14.658  29.383  1.00 40.81 ? 315 HOH A O   1 
HETATM 2224 O O   . HOH F 4 .   ? 15.027 -10.542 34.880  1.00 45.13 ? 316 HOH A O   1 
HETATM 2225 O O   . HOH F 4 .   ? 0.315  -9.624  26.109  1.00 41.01 ? 317 HOH A O   1 
HETATM 2226 O O   . HOH F 4 .   ? 9.084  8.199   24.289  1.00 27.28 ? 318 HOH A O   1 
HETATM 2227 O O   . HOH F 4 .   ? 28.131 12.324  8.578   1.00 43.01 ? 319 HOH A O   1 
HETATM 2228 O O   . HOH F 4 .   ? 19.468 -1.680  33.074  1.00 32.11 ? 320 HOH A O   1 
HETATM 2229 O O   . HOH F 4 .   ? 23.355 -0.863  35.606  1.00 57.79 ? 321 HOH A O   1 
HETATM 2230 O O   . HOH F 4 .   ? 8.615  -7.353  33.012  1.00 40.36 ? 322 HOH A O   1 
HETATM 2231 O O   . HOH F 4 .   ? 27.422 24.132  20.986  1.00 43.44 ? 323 HOH A O   1 
HETATM 2232 O O   . HOH F 4 .   ? 32.080 20.287  29.858  1.00 48.26 ? 324 HOH A O   1 
HETATM 2233 O O   . HOH F 4 .   ? 26.864 25.717  25.718  1.00 43.67 ? 325 HOH A O   1 
HETATM 2234 O O   . HOH F 4 .   ? 38.774 9.883   15.567  1.00 39.12 ? 326 HOH A O   1 
HETATM 2235 O O   . HOH F 4 .   ? 33.860 7.322   25.154  1.00 34.17 ? 327 HOH A O   1 
HETATM 2236 O O   . HOH F 4 .   ? 31.459 1.545   16.930  1.00 41.24 ? 328 HOH A O   1 
HETATM 2237 O O   . HOH F 4 .   ? 28.787 18.210  12.588  1.00 36.48 ? 329 HOH A O   1 
HETATM 2238 O O   . HOH F 4 .   ? 14.674 26.276  24.877  1.00 37.34 ? 330 HOH A O   1 
HETATM 2239 O O   . HOH F 4 .   ? 13.593 19.556  22.697  1.00 39.01 ? 331 HOH A O   1 
HETATM 2240 O O   . HOH F 4 .   ? 31.274 -4.977  43.823  1.00 41.73 ? 332 HOH A O   1 
HETATM 2241 O O   . HOH F 4 .   ? 31.779 2.222   13.991  1.00 42.31 ? 333 HOH A O   1 
HETATM 2242 O O   . HOH F 4 .   ? 37.875 7.476   16.385  1.00 37.60 ? 334 HOH A O   1 
HETATM 2243 O O   . HOH F 4 .   ? 43.126 19.430  19.408  1.00 30.87 ? 335 HOH A O   1 
HETATM 2244 O O   . HOH F 4 .   ? 46.316 13.493  17.805  1.00 36.89 ? 336 HOH A O   1 
HETATM 2245 O O   . HOH F 4 .   ? 20.976 27.350  29.230  1.00 44.57 ? 337 HOH A O   1 
HETATM 2246 O O   . HOH F 4 .   ? 23.402 4.609   11.650  1.00 35.72 ? 338 HOH A O   1 
HETATM 2247 O O   . HOH F 4 .   ? 36.328 11.201  23.309  1.00 35.92 ? 339 HOH A O   1 
HETATM 2248 O O   . HOH F 4 .   ? 22.459 19.879  33.540  1.00 44.45 ? 340 HOH A O   1 
HETATM 2249 O O   . HOH F 4 .   ? 9.616  18.613  15.833  1.00 52.62 ? 341 HOH A O   1 
HETATM 2250 O O   . HOH F 4 .   ? 35.113 8.130   12.554  1.00 39.21 ? 342 HOH A O   1 
HETATM 2251 O O   A HOH F 4 .   ? 31.243 3.324   23.865  0.50 23.92 ? 343 HOH A O   1 
HETATM 2252 O O   B HOH F 4 .   ? 31.252 3.650   24.809  0.50 27.36 ? 343 HOH A O   1 
HETATM 2253 O O   . HOH F 4 .   ? 7.615  10.572  20.048  1.00 29.63 ? 344 HOH A O   1 
HETATM 2254 O O   . HOH F 4 .   ? 13.963 6.177   11.403  1.00 39.46 ? 345 HOH A O   1 
HETATM 2255 O O   . HOH F 4 .   ? 23.112 21.253  14.781  1.00 38.55 ? 346 HOH A O   1 
HETATM 2256 O O   . HOH F 4 .   ? 23.595 3.722   31.564  1.00 47.19 ? 347 HOH A O   1 
HETATM 2257 O O   . HOH F 4 .   ? 13.885 -3.736  33.068  1.00 32.96 ? 348 HOH A O   1 
HETATM 2258 O O   . HOH F 4 .   ? 33.614 15.685  28.494  1.00 40.18 ? 349 HOH A O   1 
HETATM 2259 O O   . HOH F 4 .   ? 33.226 3.767   20.027  1.00 38.40 ? 350 HOH A O   1 
HETATM 2260 O O   . HOH F 4 .   ? 29.395 -2.666  12.113  1.00 50.03 ? 351 HOH A O   1 
HETATM 2261 O O   . HOH F 4 .   ? 33.094 6.414   20.386  1.00 32.56 ? 352 HOH A O   1 
HETATM 2262 O O   . HOH F 4 .   ? 31.874 12.080  11.171  1.00 41.90 ? 353 HOH A O   1 
HETATM 2263 O O   . HOH F 4 .   ? 25.002 24.778  19.811  1.00 35.42 ? 354 HOH A O   1 
HETATM 2264 O O   . HOH F 4 .   ? 20.871 3.878   11.990  1.00 29.24 ? 355 HOH A O   1 
HETATM 2265 O O   . HOH F 4 .   ? 22.594 -7.751  13.429  1.00 43.71 ? 356 HOH A O   1 
HETATM 2266 O O   . HOH F 4 .   ? 7.231  8.947   25.920  1.00 40.56 ? 357 HOH A O   1 
HETATM 2267 O O   . HOH F 4 .   ? 19.779 6.086   10.828  1.00 36.78 ? 358 HOH A O   1 
HETATM 2268 O O   . HOH F 4 .   ? 3.855  -4.990  29.042  1.00 57.04 ? 359 HOH A O   1 
HETATM 2269 O O   A HOH F 4 .   ? 24.643 -6.299  23.616  0.50 27.50 ? 360 HOH A O   1 
HETATM 2270 O O   B HOH F 4 .   ? 25.520 -5.545  24.738  0.50 28.98 ? 360 HOH A O   1 
HETATM 2271 O O   . HOH F 4 .   ? 6.061  20.289  22.779  1.00 32.80 ? 361 HOH A O   1 
HETATM 2272 O O   . HOH F 4 .   ? 29.181 11.303  11.071  1.00 27.92 ? 362 HOH A O   1 
HETATM 2273 O O   . HOH F 4 .   ? 30.414 -2.389  43.086  1.00 26.73 ? 363 HOH A O   1 
HETATM 2274 O O   . HOH F 4 .   ? 26.950 -5.504  14.775  1.00 27.56 ? 364 HOH A O   1 
HETATM 2275 O O   . HOH F 4 .   ? 7.046  5.202   15.977  1.00 54.01 ? 365 HOH A O   1 
HETATM 2276 O O   . HOH F 4 .   ? 34.644 -10.161 41.344  1.00 41.66 ? 366 HOH A O   1 
HETATM 2277 O O   . HOH F 4 .   ? 19.404 18.266  17.591  1.00 32.81 ? 367 HOH A O   1 
HETATM 2278 O O   . HOH F 4 .   ? 4.143  6.021   25.832  1.00 34.25 ? 368 HOH A O   1 
HETATM 2279 O O   . HOH F 4 .   ? 28.521 -1.951  25.273  1.00 38.29 ? 369 HOH A O   1 
HETATM 2280 O O   . HOH F 4 .   ? 2.050  -1.490  18.197  1.00 48.76 ? 370 HOH A O   1 
HETATM 2281 O O   . HOH F 4 .   ? 7.339  19.369  26.509  1.00 30.24 ? 371 HOH A O   1 
HETATM 2282 O O   . HOH F 4 .   ? -0.000 -0.000  18.663  0.50 42.90 ? 372 HOH A O   1 
HETATM 2283 O O   . HOH F 4 .   ? 29.613 -4.852  16.070  1.00 26.27 ? 373 HOH A O   1 
HETATM 2284 O O   . HOH F 4 .   ? 20.049 25.309  29.668  1.00 47.87 ? 374 HOH A O   1 
HETATM 2285 O O   . HOH F 4 .   ? 30.772 -4.233  13.696  1.00 50.69 ? 375 HOH A O   1 
HETATM 2286 O O   . HOH F 4 .   ? 28.085 20.615  13.929  1.00 42.61 ? 376 HOH A O   1 
HETATM 2287 O O   . HOH F 4 .   ? 33.644 6.348   11.291  1.00 73.47 ? 377 HOH A O   1 
HETATM 2288 O O   . HOH F 4 .   ? 6.767  -12.017 27.253  1.00 48.95 ? 378 HOH A O   1 
HETATM 2289 O O   . HOH F 4 .   ? 22.607 -2.029  10.950  1.00 47.21 ? 379 HOH A O   1 
HETATM 2290 O O   . HOH F 4 .   ? -0.259 -3.866  26.889  1.00 47.61 ? 380 HOH A O   1 
HETATM 2291 O O   . HOH F 4 .   ? 11.794 20.598  27.674  1.00 43.14 ? 381 HOH A O   1 
HETATM 2292 O O   . HOH F 4 .   ? 19.950 -3.000  30.425  1.00 50.58 ? 382 HOH A O   1 
HETATM 2293 O O   . HOH F 4 .   ? 18.980 -0.306  11.624  1.00 37.38 ? 383 HOH A O   1 
HETATM 2294 O O   . HOH F 4 .   ? 36.058 15.587  28.601  1.00 50.81 ? 384 HOH A O   1 
HETATM 2295 O O   . HOH F 4 .   ? 6.210  17.782  28.266  1.00 38.03 ? 385 HOH A O   1 
HETATM 2296 O O   . HOH F 4 .   ? 11.244 -3.203  32.391  1.00 38.20 ? 386 HOH A O   1 
HETATM 2297 O O   . HOH F 4 .   ? 4.263  1.016   29.742  1.00 48.53 ? 387 HOH A O   1 
HETATM 2298 O O   . HOH F 4 .   ? 24.264 -4.648  26.550  1.00 50.96 ? 388 HOH A O   1 
HETATM 2299 O O   . HOH F 4 .   ? 21.924 7.910   10.919  1.00 40.94 ? 389 HOH A O   1 
HETATM 2300 O O   . HOH F 4 .   ? 16.097 -1.238  32.605  1.00 47.20 ? 390 HOH A O   1 
HETATM 2301 O O   . HOH F 4 .   ? 32.419 5.611   23.138  1.00 38.71 ? 391 HOH A O   1 
HETATM 2302 O O   A HOH F 4 .   ? 21.639 -2.095  28.581  0.50 39.43 ? 392 HOH A O   1 
HETATM 2303 O O   B HOH F 4 .   ? 22.054 -2.791  26.862  0.50 35.09 ? 392 HOH A O   1 
HETATM 2304 O O   . HOH F 4 .   ? 20.444 1.661   9.862   1.00 35.38 ? 393 HOH A O   1 
HETATM 2305 O O   . HOH F 4 .   ? 25.110 27.517  21.003  1.00 47.72 ? 394 HOH A O   1 
HETATM 2306 O O   . HOH F 4 .   ? 25.736 22.016  13.858  1.00 43.11 ? 395 HOH A O   1 
HETATM 2307 O O   . HOH G 4 .   ? 26.463 4.449   7.835   1.00 43.91 ? 301 HOH B O   1 
HETATM 2308 O O   . HOH G 4 .   ? 4.561  1.457   0.157   1.00 47.67 ? 302 HOH B O   1 
HETATM 2309 O O   . HOH G 4 .   ? 33.230 -7.586  -0.088  1.00 41.88 ? 303 HOH B O   1 
HETATM 2310 O O   . HOH G 4 .   ? 12.697 8.615   1.913   1.00 41.98 ? 304 HOH B O   1 
HETATM 2311 O O   . HOH G 4 .   ? 24.382 -16.444 7.128   1.00 41.59 ? 305 HOH B O   1 
HETATM 2312 O O   . HOH G 4 .   ? 9.554  11.694  -18.103 1.00 54.22 ? 306 HOH B O   1 
HETATM 2313 O O   . HOH G 4 .   ? 19.319 -6.366  6.680   1.00 28.99 ? 307 HOH B O   1 
HETATM 2314 O O   . HOH G 4 .   ? 45.207 -15.421 -1.827  1.00 44.25 ? 308 HOH B O   1 
HETATM 2315 O O   . HOH G 4 .   ? 6.309  -2.511  6.961   1.00 47.26 ? 309 HOH B O   1 
HETATM 2316 O O   . HOH G 4 .   ? 8.977  17.262  -0.309  1.00 58.55 ? 310 HOH B O   1 
HETATM 2317 O O   . HOH G 4 .   ? 7.402  -2.194  -4.672  1.00 29.33 ? 311 HOH B O   1 
HETATM 2318 O O   . HOH G 4 .   ? 3.104  0.997   -7.328  1.00 31.67 ? 312 HOH B O   1 
HETATM 2319 O O   . HOH G 4 .   ? 0.469  9.852   -5.922  1.00 45.90 ? 313 HOH B O   1 
HETATM 2320 O O   . HOH G 4 .   ? 3.896  5.341   -9.064  1.00 47.74 ? 314 HOH B O   1 
HETATM 2321 O O   . HOH G 4 .   ? 2.122  16.263  -8.040  1.00 41.38 ? 315 HOH B O   1 
HETATM 2322 O O   . HOH G 4 .   ? 0.062  6.625   0.435   1.00 46.90 ? 316 HOH B O   1 
HETATM 2323 O O   . HOH G 4 .   ? 22.246 -4.499  7.641   1.00 43.25 ? 317 HOH B O   1 
HETATM 2324 O O   . HOH G 4 .   ? 13.014 4.756   -10.918 1.00 44.51 ? 318 HOH B O   1 
HETATM 2325 O O   . HOH G 4 .   ? 21.459 5.606   7.175   1.00 35.15 ? 319 HOH B O   1 
HETATM 2326 O O   . HOH G 4 .   ? 1.539  -4.966  -6.108  1.00 46.73 ? 320 HOH B O   1 
HETATM 2327 O O   . HOH G 4 .   ? 33.666 5.918   -10.108 1.00 46.00 ? 321 HOH B O   1 
HETATM 2328 O O   . HOH G 4 .   ? 22.121 -21.688 -1.627  1.00 44.75 ? 322 HOH B O   1 
HETATM 2329 O O   . HOH G 4 .   ? 35.791 -8.174  3.650   1.00 46.43 ? 323 HOH B O   1 
HETATM 2330 O O   . HOH G 4 .   ? 15.620 17.009  -9.878  1.00 40.96 ? 324 HOH B O   1 
HETATM 2331 O O   . HOH G 4 .   ? 33.727 8.181   -19.298 1.00 51.86 ? 325 HOH B O   1 
HETATM 2332 O O   . HOH G 4 .   ? 26.964 -20.326 0.980   1.00 50.49 ? 326 HOH B O   1 
HETATM 2333 O O   . HOH G 4 .   ? 9.781  6.773   0.719   1.00 44.16 ? 327 HOH B O   1 
HETATM 2334 O O   . HOH G 4 .   ? 4.554  8.992   -11.033 1.00 40.40 ? 328 HOH B O   1 
HETATM 2335 O O   . HOH G 4 .   ? 42.920 -16.885 -2.344  1.00 46.52 ? 329 HOH B O   1 
HETATM 2336 O O   . HOH G 4 .   ? 6.775  17.042  -2.976  1.00 41.10 ? 330 HOH B O   1 
HETATM 2337 O O   . HOH G 4 .   ? 18.801 17.703  -6.690  1.00 49.05 ? 331 HOH B O   1 
HETATM 2338 O O   . HOH G 4 .   ? 36.047 -10.750 4.516   1.00 47.17 ? 332 HOH B O   1 
HETATM 2339 O O   . HOH G 4 .   ? 20.053 -23.297 -6.453  1.00 48.71 ? 333 HOH B O   1 
HETATM 2340 O O   . HOH G 4 .   ? 26.258 -9.796  8.702   1.00 33.44 ? 334 HOH B O   1 
HETATM 2341 O O   . HOH G 4 .   ? 7.031  3.967   -9.935  1.00 38.64 ? 335 HOH B O   1 
HETATM 2342 O O   . HOH G 4 .   ? 17.507 14.752  -15.469 1.00 35.49 ? 336 HOH B O   1 
HETATM 2343 O O   . HOH G 4 .   ? 5.636  -2.751  -6.780  1.00 34.05 ? 337 HOH B O   1 
HETATM 2344 O O   . HOH G 4 .   ? 31.416 -5.870  -0.491  1.00 35.27 ? 338 HOH B O   1 
HETATM 2345 O O   . HOH G 4 .   ? 20.276 5.123   -13.332 1.00 31.59 ? 339 HOH B O   1 
HETATM 2346 O O   . HOH G 4 .   ? 0.114  4.550   -3.621  1.00 38.41 ? 340 HOH B O   1 
HETATM 2347 O O   . HOH G 4 .   ? 32.830 -7.642  7.513   1.00 52.77 ? 341 HOH B O   1 
HETATM 2348 O O   . HOH G 4 .   ? 33.544 -11.233 -3.536  1.00 38.85 ? 342 HOH B O   1 
HETATM 2349 O O   . HOH G 4 .   ? 20.107 -0.715  7.484   1.00 33.15 ? 343 HOH B O   1 
HETATM 2350 O O   . HOH G 4 .   ? 28.511 3.357   -5.716  1.00 41.24 ? 344 HOH B O   1 
HETATM 2351 O O   . HOH G 4 .   ? 10.491 12.876  -13.644 1.00 34.41 ? 345 HOH B O   1 
HETATM 2352 O O   . HOH G 4 .   ? 31.304 -1.143  3.067   1.00 43.03 ? 346 HOH B O   1 
HETATM 2353 O O   . HOH G 4 .   ? 16.605 9.500   -17.671 1.00 39.82 ? 347 HOH B O   1 
HETATM 2354 O O   . HOH G 4 .   ? 2.585  12.708  0.526   1.00 45.93 ? 348 HOH B O   1 
HETATM 2355 O O   . HOH G 4 .   ? 15.109 8.214   -13.607 1.00 28.00 ? 349 HOH B O   1 
HETATM 2356 O O   . HOH G 4 .   ? 15.521 -14.362 2.115   1.00 41.91 ? 350 HOH B O   1 
HETATM 2357 O O   . HOH G 4 .   ? 13.747 -21.151 -9.799  1.00 46.25 ? 351 HOH B O   1 
HETATM 2358 O O   . HOH G 4 .   ? 18.381 -16.518 -13.808 1.00 42.97 ? 352 HOH B O   1 
HETATM 2359 O O   . HOH G 4 .   ? 5.524  -3.741  -0.552  1.00 32.86 ? 353 HOH B O   1 
HETATM 2360 O O   . HOH G 4 .   ? 28.002 7.089   4.804   1.00 29.86 ? 354 HOH B O   1 
HETATM 2361 O O   . HOH G 4 .   ? 12.538 -1.421  8.291   1.00 48.03 ? 355 HOH B O   1 
HETATM 2362 O O   . HOH G 4 .   ? 22.958 -18.549 5.913   1.00 41.26 ? 356 HOH B O   1 
HETATM 2363 O O   . HOH G 4 .   ? 18.535 -2.456  8.768   1.00 39.61 ? 357 HOH B O   1 
HETATM 2364 O O   . HOH G 4 .   ? 42.675 -15.776 2.200   1.00 46.86 ? 358 HOH B O   1 
HETATM 2365 O O   . HOH G 4 .   ? 3.540  -12.323 -0.367  1.00 41.35 ? 359 HOH B O   1 
HETATM 2366 O O   . HOH G 4 .   ? 19.528 -21.873 -0.663  1.00 36.77 ? 360 HOH B O   1 
HETATM 2367 O O   . HOH G 4 .   ? 32.621 10.350  -2.390  1.00 49.85 ? 361 HOH B O   1 
HETATM 2368 O O   . HOH G 4 .   ? 26.634 7.675   -4.950  1.00 42.18 ? 362 HOH B O   1 
HETATM 2369 O O   . HOH G 4 .   ? 1.215  1.945   -3.434  1.00 31.63 ? 363 HOH B O   1 
HETATM 2370 O O   . HOH G 4 .   ? 19.603 -15.879 -15.933 1.00 55.10 ? 364 HOH B O   1 
HETATM 2371 O O   . HOH G 4 .   ? 12.675 -18.626 1.828   1.00 60.45 ? 365 HOH B O   1 
HETATM 2372 O O   . HOH G 4 .   ? 6.986  1.464   3.216   1.00 50.59 ? 366 HOH B O   1 
HETATM 2373 O O   . HOH G 4 .   ? 23.387 4.899   8.612   1.00 35.46 ? 367 HOH B O   1 
HETATM 2374 O O   . HOH G 4 .   ? 28.952 -11.149 8.847   1.00 39.38 ? 368 HOH B O   1 
HETATM 2375 O O   . HOH G 4 .   ? 31.094 -6.653  9.168   1.00 60.58 ? 369 HOH B O   1 
HETATM 2376 O O   . HOH G 4 .   ? 30.598 5.854   3.492   1.00 26.58 ? 370 HOH B O   1 
HETATM 2377 O O   . HOH G 4 .   ? 23.223 -22.359 7.494   1.00 43.78 ? 371 HOH B O   1 
HETATM 2378 O O   . HOH G 4 .   ? 16.385 5.001   8.274   1.00 61.59 ? 372 HOH B O   1 
HETATM 2379 O O   . HOH G 4 .   ? 34.250 0.000   -20.430 0.50 63.94 ? 373 HOH B O   1 
HETATM 2380 O O   . HOH G 4 .   ? 7.603  5.045   4.617   1.00 51.13 ? 374 HOH B O   1 
HETATM 2381 O O   . HOH G 4 .   ? 15.420 16.297  -14.246 1.00 46.82 ? 375 HOH B O   1 
HETATM 2382 O O   . HOH G 4 .   ? 13.067 -15.089 0.709   1.00 45.25 ? 376 HOH B O   1 
HETATM 2383 O O   . HOH G 4 .   ? 16.172 -16.034 -12.886 1.00 56.97 ? 377 HOH B O   1 
HETATM 2384 O O   . HOH G 4 .   ? 34.927 -11.780 6.631   1.00 48.86 ? 378 HOH B O   1 
HETATM 2385 O O   . HOH G 4 .   ? 19.139 3.904   8.125   1.00 41.84 ? 379 HOH B O   1 
HETATM 2386 O O   . HOH G 4 .   ? 1.596  -1.550  -0.239  1.00 39.39 ? 380 HOH B O   1 
HETATM 2387 O O   . HOH G 4 .   ? 12.288 8.298   -12.794 1.00 33.96 ? 381 HOH B O   1 
HETATM 2388 O O   . HOH G 4 .   ? 22.085 3.579   -13.283 1.00 48.87 ? 382 HOH B O   1 
HETATM 2389 O O   . HOH G 4 .   ? 42.021 -15.531 4.972   1.00 61.89 ? 383 HOH B O   1 
HETATM 2390 O O   A HOH G 4 .   ? 16.599 5.058   -12.863 0.50 40.77 ? 384 HOH B O   1 
HETATM 2391 O O   B HOH G 4 .   ? 16.126 5.858   -13.947 0.50 32.37 ? 384 HOH B O   1 
HETATM 2392 O O   . HOH G 4 .   ? 3.323  -1.648  -7.856  1.00 36.25 ? 385 HOH B O   1 
HETATM 2393 O O   A HOH G 4 .   ? 18.591 6.720   -10.035 0.50 38.11 ? 386 HOH B O   1 
HETATM 2394 O O   B HOH G 4 .   ? 17.511 6.200   -11.196 0.50 32.88 ? 386 HOH B O   1 
HETATM 2395 O O   . HOH G 4 .   ? 0.939  -2.855  -7.546  1.00 36.28 ? 387 HOH B O   1 
HETATM 2396 O O   . HOH G 4 .   ? 4.228  -1.359  0.208   1.00 39.28 ? 388 HOH B O   1 
HETATM 2397 O O   . HOH G 4 .   ? 22.292 -12.710 14.737  1.00 51.19 ? 389 HOH B O   1 
HETATM 2398 O O   . HOH G 4 .   ? 0.554  1.231   -6.183  1.00 36.24 ? 390 HOH B O   1 
HETATM 2399 O O   . HOH G 4 .   ? 10.466 9.297   -14.420 1.00 54.49 ? 391 HOH B O   1 
HETATM 2400 O O   A HOH G 4 .   ? 21.590 6.272   -8.692  0.50 48.15 ? 392 HOH B O   1 
HETATM 2401 O O   B HOH G 4 .   ? 22.949 5.979   -7.637  0.50 44.36 ? 392 HOH B O   1 
HETATM 2402 O O   . HOH G 4 .   ? 45.747 -15.922 -4.693  1.00 61.59 ? 393 HOH B O   1 
HETATM 2403 O O   . HOH G 4 .   ? 22.424 -10.599 12.662  1.00 45.79 ? 394 HOH B O   1 
HETATM 2404 O O   . HOH G 4 .   ? 0.813  10.810  -8.523  1.00 43.85 ? 395 HOH B O   1 
HETATM 2405 O O   . HOH G 4 .   ? 16.712 19.023  -10.821 1.00 51.00 ? 396 HOH B O   1 
HETATM 2406 O O   . HOH G 4 .   ? 0.000  0.000   -2.031  0.50 31.59 ? 397 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   . MET A 1   ? 0.7061 0.6164 0.8759 0.0842  0.1627  -0.0587 1   MET A N   
2    C CA  . MET A 1   ? 0.7216 0.5993 0.8614 0.0874  0.1334  -0.0294 1   MET A CA  
3    C C   . MET A 1   ? 0.6596 0.4300 0.7648 0.0422  0.0864  -0.0181 1   MET A C   
4    O O   . MET A 1   ? 0.6892 0.3377 0.7949 0.0057  0.0708  0.0260  1   MET A O   
5    C CB  . MET A 1   ? 0.8168 0.7191 0.9423 0.0914  0.1104  0.0231  1   MET A CB  
6    C CG  . MET A 1   ? 0.9097 0.8307 0.9970 0.0832  0.1117  0.0682  1   MET A CG  
7    S SD  . MET A 1   ? 1.0614 0.9010 1.1176 0.0709  0.0536  0.1695  1   MET A SD  
8    C CE  . MET A 1   ? 1.0654 0.9240 1.1460 0.0832  0.0894  0.1597  1   MET A CE  
9    N N   . GLU A 2   ? 0.5746 0.4250 0.6568 0.0380  0.0639  -0.0335 2   GLU A N   
10   C CA  . GLU A 2   ? 0.5555 0.4335 0.6289 0.0144  0.0524  -0.0175 2   GLU A CA  
11   C C   . GLU A 2   ? 0.5577 0.4429 0.5876 0.0153  0.0702  -0.0298 2   GLU A C   
12   O O   . GLU A 2   ? 0.5595 0.3499 0.4919 -0.0314 0.0794  -0.0381 2   GLU A O   
13   C CB  . GLU A 2   ? 0.5659 0.4691 0.6628 0.0512  0.0429  0.0081  2   GLU A CB  
14   C CG  . GLU A 2   ? 0.5424 0.5169 0.6706 0.0696  0.0411  0.0176  2   GLU A CG  
15   C CD  . GLU A 2   ? 0.4887 0.5282 0.6608 0.0627  0.0499  0.0282  2   GLU A CD  
16   O OE1 . GLU A 2   ? 0.4406 0.5289 0.5255 0.0412  0.0030  0.0679  2   GLU A OE1 
17   O OE2 . GLU A 2   ? 0.5059 0.5622 0.7141 0.0852  0.0299  0.0119  2   GLU A OE2 
18   N N   . ALA A 3   ? 0.5397 0.4404 0.5761 0.0151  0.0492  -0.0543 3   ALA A N   
19   C CA  . ALA A 3   ? 0.5490 0.3902 0.5704 0.0366  0.0557  -0.0494 3   ALA A CA  
20   C C   . ALA A 3   ? 0.5485 0.4004 0.5529 0.0500  0.0283  -0.0894 3   ALA A C   
21   O O   . ALA A 3   ? 0.5713 0.4323 0.5339 0.0931  0.0356  -0.0572 3   ALA A O   
22   C CB  . ALA A 3   ? 0.5573 0.3525 0.5853 0.0417  0.0544  -0.0414 3   ALA A CB  
23   N N   . VAL A 4   ? 0.5292 0.4787 0.5539 0.1010  0.0183  -0.0892 4   VAL A N   
24   C CA  . VAL A 4   ? 0.4994 0.5207 0.5872 0.0779  0.0296  -0.1123 4   VAL A CA  
25   C C   . VAL A 4   ? 0.4827 0.4692 0.5302 0.1512  0.0311  -0.1342 4   VAL A C   
26   O O   . VAL A 4   ? 0.4580 0.5256 0.5408 0.1168  0.0174  -0.1193 4   VAL A O   
27   C CB  . VAL A 4   ? 0.5081 0.5404 0.6471 0.0879  0.0428  -0.1226 4   VAL A CB  
28   C CG1 . VAL A 4   ? 0.5099 0.5528 0.6698 0.0619  0.0317  -0.1326 4   VAL A CG1 
29   C CG2 . VAL A 4   ? 0.5203 0.5995 0.6880 0.0556  0.0454  -0.1333 4   VAL A CG2 
30   N N   . LEU A 5   ? 0.4705 0.4914 0.4736 0.0954  0.0088  -0.0756 5   LEU A N   
31   C CA  . LEU A 5   ? 0.4414 0.4369 0.4261 0.0930  0.0134  -0.0798 5   LEU A CA  
32   C C   . LEU A 5   ? 0.4543 0.4977 0.4108 0.0765  0.0156  -0.0295 5   LEU A C   
33   O O   . LEU A 5   ? 0.4239 0.4807 0.3825 0.0644  0.0252  -0.0116 5   LEU A O   
34   C CB  . LEU A 5   ? 0.4355 0.3735 0.4309 0.0626  0.0086  -0.0647 5   LEU A CB  
35   C CG  . LEU A 5   ? 0.4154 0.2749 0.4301 0.0298  0.0094  -0.0524 5   LEU A CG  
36   C CD1 . LEU A 5   ? 0.4070 0.2249 0.4325 0.0533  0.0220  -0.0752 5   LEU A CD1 
37   C CD2 . LEU A 5   ? 0.4039 0.2173 0.4305 -0.0015 0.0043  -0.0423 5   LEU A CD2 
38   N N   . ASN A 6   ? 0.4779 0.5393 0.4284 0.0679  0.0348  -0.0175 6   ASN A N   
39   C CA  . ASN A 6   ? 0.5062 0.5677 0.4514 0.0704  0.0462  0.0146  6   ASN A CA  
40   C C   . ASN A 6   ? 0.5056 0.5633 0.4338 0.0970  0.0543  0.0103  6   ASN A C   
41   O O   . ASN A 6   ? 0.4667 0.5984 0.4651 0.0986  0.0659  0.0624  6   ASN A O   
42   C CB  . ASN A 6   ? 0.5400 0.5547 0.5231 0.0483  0.0432  0.0428  6   ASN A CB  
43   C CG  . ASN A 6   ? 0.5845 0.5782 0.6252 0.0331  0.0492  0.1075  6   ASN A CG  
44   O OD1 . ASN A 6   ? 0.6078 0.5316 0.6940 0.0205  0.0773  0.1831  6   ASN A OD1 
45   N ND2 . ASN A 6   ? 0.6482 0.6135 0.6997 0.0246  0.0681  0.1269  6   ASN A ND2 
46   N N   . GLU A 7   ? 0.5249 0.5393 0.4405 0.1494  0.0329  0.0414  7   GLU A N   
47   C CA  . GLU A 7   ? 0.5849 0.5625 0.4502 0.1484  0.0128  0.0247  7   GLU A CA  
48   C C   . GLU A 7   ? 0.5956 0.5348 0.4101 0.1621  0.0036  0.0284  7   GLU A C   
49   O O   . GLU A 7   ? 0.5784 0.5155 0.3949 0.2112  -0.0039 -0.0200 7   GLU A O   
50   C CB  . GLU A 7   ? 0.6352 0.6043 0.4690 0.1625  0.0128  -0.0183 7   GLU A CB  
51   C CG  . GLU A 7   ? 0.7100 0.6173 0.5206 0.1539  0.0174  -0.0109 7   GLU A CG  
52   C CD  . GLU A 7   ? 0.7932 0.7029 0.5942 0.1558  -0.0133 0.0122  7   GLU A CD  
53   O OE1 . GLU A 7   ? 0.9116 0.8133 0.6488 0.1196  -0.0291 -0.0171 7   GLU A OE1 
54   O OE2 . GLU A 7   ? 0.8953 0.7264 0.7275 0.1550  -0.0067 -0.0013 7   GLU A OE2 
55   N N   . LEU A 8   ? 0.5733 0.4545 0.3991 0.1836  0.0050  0.0075  8   LEU A N   
56   C CA  . LEU A 8   ? 0.5734 0.4076 0.4497 0.1616  -0.0069 0.0219  8   LEU A CA  
57   C C   . LEU A 8   ? 0.5442 0.3501 0.3972 0.1076  -0.0019 -0.0151 8   LEU A C   
58   O O   . LEU A 8   ? 0.5445 0.3662 0.3503 0.1090  -0.0200 -0.0222 8   LEU A O   
59   C CB  . LEU A 8   ? 0.5745 0.3921 0.4947 0.1784  -0.0148 0.0449  8   LEU A CB  
60   C CG  . LEU A 8   ? 0.5814 0.3618 0.5492 0.1625  0.0026  0.0573  8   LEU A CG  
61   C CD1 . LEU A 8   ? 0.5713 0.3311 0.5171 0.1942  0.0107  0.0689  8   LEU A CD1 
62   C CD2 . LEU A 8   ? 0.5885 0.2971 0.5788 0.1780  0.0055  0.0592  8   LEU A CD2 
63   N N   . VAL A 9   ? 0.4894 0.3180 0.3284 0.0665  0.0014  0.0095  9   VAL A N   
64   C CA  . VAL A 9   ? 0.4769 0.2970 0.3186 0.0364  0.0362  0.0113  9   VAL A CA  
65   C C   . VAL A 9   ? 0.4617 0.2796 0.3225 0.0481  0.0345  0.0037  9   VAL A C   
66   O O   . VAL A 9   ? 0.4393 0.2275 0.3186 0.0127  0.0530  0.0222  9   VAL A O   
67   C CB  . VAL A 9   ? 0.4821 0.2963 0.3402 0.0004  0.0228  -0.0012 9   VAL A CB  
68   C CG1 . VAL A 9   ? 0.4939 0.2682 0.3489 -0.0152 0.0195  -0.0115 9   VAL A CG1 
69   C CG2 . VAL A 9   ? 0.4856 0.3189 0.3719 0.0058  0.0292  0.0023  9   VAL A CG2 
70   N N   . SER A 10  ? 0.4873 0.3330 0.3423 0.0771  0.0473  0.0048  10  SER A N   
71   C CA  . SER A 10  ? 0.4895 0.2865 0.3545 0.1161  0.0579  0.0376  10  SER A CA  
72   C C   . SER A 10  ? 0.4921 0.2974 0.3228 0.1502  0.0292  0.0117  10  SER A C   
73   O O   . SER A 10  ? 0.4898 0.3173 0.3184 0.1605  0.0358  0.0158  10  SER A O   
74   C CB  . SER A 10  ? 0.5353 0.3373 0.3901 0.0779  0.0688  0.0487  10  SER A CB  
75   O OG  . SER A 10  ? 0.5793 0.3995 0.4873 0.0490  0.0645  0.0664  10  SER A OG  
76   N N   . VAL A 11  ? 0.5223 0.2889 0.3423 0.1538  0.0239  -0.0119 11  VAL A N   
77   C CA  . VAL A 11  ? 0.5188 0.2971 0.3539 0.1438  -0.0035 -0.0209 11  VAL A CA  
78   C C   . VAL A 11  ? 0.5348 0.2443 0.3224 0.1310  -0.0166 -0.0235 11  VAL A C   
79   O O   . VAL A 11  ? 0.5737 0.1920 0.3076 0.1048  -0.0529 -0.0229 11  VAL A O   
80   C CB  . VAL A 11  ? 0.5295 0.3320 0.4127 0.1603  -0.0024 -0.0538 11  VAL A CB  
81   C CG1 . VAL A 11  ? 0.5501 0.2509 0.4647 0.1895  -0.0004 -0.0367 11  VAL A CG1 
82   C CG2 . VAL A 11  ? 0.5292 0.3312 0.4036 0.1787  0.0067  -0.0829 11  VAL A CG2 
83   N N   . GLU A 12  ? 0.5521 0.2347 0.3342 0.1041  -0.0133 -0.0114 12  GLU A N   
84   C CA  . GLU A 12  ? 0.5396 0.1884 0.3166 0.0892  -0.0060 0.0052  12  GLU A CA  
85   C C   . GLU A 12  ? 0.5275 0.1631 0.3478 0.0684  -0.0060 0.0026  12  GLU A C   
86   O O   . GLU A 12  ? 0.5439 0.1964 0.3765 0.0699  -0.0053 -0.0259 12  GLU A O   
87   C CB  . GLU A 12  ? 0.5566 0.3063 0.3380 0.0809  0.0017  0.0342  12  GLU A CB  
88   C CG  . GLU A 12  ? 0.5612 0.4187 0.4218 0.0551  0.0178  0.0511  12  GLU A CG  
89   C CD  . GLU A 12  ? 0.6011 0.4623 0.5188 0.0514  0.0532  0.0960  12  GLU A CD  
90   O OE1 . GLU A 12  ? 0.6239 0.4313 0.5802 0.0691  0.0621  0.1642  12  GLU A OE1 
91   O OE2 . GLU A 12  ? 0.6221 0.5619 0.5733 0.0199  0.0865  0.1273  12  GLU A OE2 
92   N N   . ASP A 13  ? 0.4925 0.1469 0.3097 0.0588  -0.0066 -0.0153 13  ASP A N   
93   C CA  . ASP A 13  ? 0.4921 0.1799 0.3287 0.0771  0.0102  -0.0183 13  ASP A CA  
94   C C   . ASP A 13  ? 0.4804 0.1320 0.3211 0.0767  0.0202  -0.0021 13  ASP A C   
95   O O   . ASP A 13  ? 0.4604 0.1849 0.3194 0.0352  0.0076  0.0020  13  ASP A O   
96   C CB  . ASP A 13  ? 0.5299 0.1957 0.3333 0.0426  0.0276  -0.0223 13  ASP A CB  
97   C CG  . ASP A 13  ? 0.5392 0.2083 0.3626 0.0162  0.0554  -0.0450 13  ASP A CG  
98   O OD1 . ASP A 13  ? 0.5799 0.1721 0.3697 0.0233  0.0690  -0.0430 13  ASP A OD1 
99   O OD2 . ASP A 13  ? 0.5255 0.1664 0.3850 0.0239  0.0562  -0.0474 13  ASP A OD2 
100  N N   . LEU A 14  ? 0.5021 0.1697 0.3278 0.1055  0.0180  -0.0029 14  LEU A N   
101  C CA  . LEU A 14  ? 0.5356 0.2070 0.3297 0.1102  0.0189  -0.0073 14  LEU A CA  
102  C C   . LEU A 14  ? 0.5575 0.1972 0.3298 0.0987  0.0113  0.0222  14  LEU A C   
103  O O   . LEU A 14  ? 0.5669 0.2252 0.3335 0.1278  0.0229  0.0525  14  LEU A O   
104  C CB  . LEU A 14  ? 0.5414 0.2622 0.3538 0.1321  0.0205  -0.0186 14  LEU A CB  
105  C CG  . LEU A 14  ? 0.5892 0.3309 0.3610 0.1386  0.0116  -0.0183 14  LEU A CG  
106  C CD1 . LEU A 14  ? 0.6033 0.3374 0.3529 0.1323  0.0078  -0.0104 14  LEU A CD1 
107  C CD2 . LEU A 14  ? 0.6078 0.3975 0.3907 0.1414  0.0336  -0.0424 14  LEU A CD2 
108  N N   . LEU A 15  ? 0.5685 0.1861 0.3189 0.0923  -0.0090 0.0101  15  LEU A N   
109  C CA  . LEU A 15  ? 0.5987 0.1793 0.3796 0.0657  -0.0178 0.0017  15  LEU A CA  
110  C C   . LEU A 15  ? 0.5810 0.1678 0.3150 0.0045  0.0011  0.0234  15  LEU A C   
111  O O   . LEU A 15  ? 0.6102 0.1858 0.3674 -0.0182 -0.0260 0.0207  15  LEU A O   
112  C CB  . LEU A 15  ? 0.6271 0.2164 0.4325 0.0806  -0.0669 0.0142  15  LEU A CB  
113  C CG  . LEU A 15  ? 0.6687 0.2882 0.4821 0.0852  -0.0673 -0.0039 15  LEU A CG  
114  C CD1 . LEU A 15  ? 0.7035 0.2563 0.5218 0.0968  -0.0851 -0.0156 15  LEU A CD1 
115  C CD2 . LEU A 15  ? 0.6820 0.3020 0.5132 0.1054  -0.0675 -0.0270 15  LEU A CD2 
116  N N   . LYS A 16  ? 0.5798 0.1638 0.3092 -0.0024 0.0427  0.0252  16  LYS A N   
117  C CA  . LYS A 16  ? 0.5642 0.2452 0.3654 -0.0221 0.0624  0.0277  16  LYS A CA  
118  C C   . LYS A 16  ? 0.5033 0.2093 0.3667 -0.0252 0.0822  0.0140  16  LYS A C   
119  O O   . LYS A 16  ? 0.5113 0.1681 0.3979 -0.0675 0.0767  -0.0301 16  LYS A O   
120  C CB  . LYS A 16  ? 0.6228 0.2963 0.3795 -0.0499 0.0775  0.0057  16  LYS A CB  
121  C CG  . LYS A 16  ? 0.6685 0.3219 0.4259 -0.0599 0.1077  0.0438  16  LYS A CG  
122  C CD  . LYS A 16  ? 0.7490 0.4245 0.4590 -0.0551 0.0944  0.0298  16  LYS A CD  
123  C CE  . LYS A 16  ? 0.8237 0.4931 0.4948 -0.0853 0.0981  0.0013  16  LYS A CE  
124  N NZ  . LYS A 16  ? 0.9075 0.5879 0.5199 -0.0954 0.0652  -0.0045 16  LYS A NZ  
125  N N   . PHE A 17  ? 0.4186 0.2266 0.3555 -0.0069 0.0812  0.0171  17  PHE A N   
126  C CA  . PHE A 17  ? 0.3867 0.1745 0.3828 0.0130  0.0788  0.0022  17  PHE A CA  
127  C C   . PHE A 17  ? 0.3718 0.1764 0.3735 0.0080  0.0804  0.0163  17  PHE A C   
128  O O   . PHE A 17  ? 0.3982 0.1400 0.4313 0.0052  0.0380  0.0116  17  PHE A O   
129  C CB  . PHE A 17  ? 0.3609 0.1845 0.3975 0.0407  0.0717  0.0332  17  PHE A CB  
130  C CG  . PHE A 17  ? 0.3368 0.1604 0.4168 0.0253  0.0557  0.0352  17  PHE A CG  
131  C CD1 . PHE A 17  ? 0.3212 0.2169 0.4345 0.0389  0.0470  0.0293  17  PHE A CD1 
132  C CD2 . PHE A 17  ? 0.3507 0.1520 0.4316 0.0552  0.0479  0.0508  17  PHE A CD2 
133  C CE1 . PHE A 17  ? 0.3146 0.1475 0.4746 0.0284  0.0514  0.0497  17  PHE A CE1 
134  C CE2 . PHE A 17  ? 0.3473 0.1972 0.4434 0.0081  0.0640  0.0923  17  PHE A CE2 
135  C CZ  . PHE A 17  ? 0.3436 0.1701 0.4687 0.0081  0.0578  0.0652  17  PHE A CZ  
136  N N   . GLU A 18  ? 0.4056 0.1819 0.3663 0.0383  0.0416  0.0079  18  GLU A N   
137  C CA  . GLU A 18  ? 0.4579 0.1332 0.3734 0.0132  0.0307  0.0284  18  GLU A CA  
138  C C   . GLU A 18  ? 0.4605 0.2024 0.3716 0.0153  0.0307  0.0330  18  GLU A C   
139  O O   . GLU A 18  ? 0.4803 0.1429 0.3857 -0.0057 0.0278  0.0388  18  GLU A O   
140  C CB  . GLU A 18  ? 0.4784 0.1933 0.3774 0.0553  0.0211  0.0286  18  GLU A CB  
141  C CG  . GLU A 18  ? 0.4910 0.1705 0.3952 0.0352  0.0268  0.0340  18  GLU A CG  
142  C CD  . GLU A 18  ? 0.5369 0.2070 0.4481 0.0625  0.0165  0.0301  18  GLU A CD  
143  O OE1 . GLU A 18  ? 0.5628 0.2786 0.4973 0.1061  -0.0279 -0.0062 18  GLU A OE1 
144  O OE2 . GLU A 18  ? 0.5695 0.2669 0.4879 0.0170  0.0657  -0.0093 18  GLU A OE2 
145  N N   . LYS A 19  ? 0.4635 0.1733 0.3914 0.0124  0.0194  0.0586  19  LYS A N   
146  C CA  . LYS A 19  ? 0.4538 0.2518 0.4493 -0.0091 0.0378  0.0246  19  LYS A CA  
147  C C   . LYS A 19  ? 0.4715 0.1939 0.4515 -0.0270 0.0447  0.0366  19  LYS A C   
148  O O   . LYS A 19  ? 0.4944 0.2703 0.4814 -0.0794 0.0489  0.0234  19  LYS A O   
149  C CB  . LYS A 19  ? 0.5044 0.2937 0.4928 -0.0136 0.0497  0.0375  19  LYS A CB  
150  C CG  . LYS A 19  ? 0.5716 0.3578 0.5827 -0.0439 0.0487  0.0547  19  LYS A CG  
151  C CD  . LYS A 19  ? 0.6329 0.3857 0.6177 -0.0270 0.0385  0.0777  19  LYS A CD  
152  C CE  . LYS A 19  ? 0.6412 0.4804 0.7255 -0.0493 0.0607  0.0568  19  LYS A CE  
153  N NZ  . LYS A 19  ? 0.6713 0.5061 0.7948 -0.0112 0.0445  0.0282  19  LYS A NZ  
154  N N   . LYS A 20  ? 0.4363 0.2402 0.4580 -0.0427 0.0518  0.0064  20  LYS A N   
155  C CA  . LYS A 20  ? 0.4103 0.2418 0.4778 -0.0353 0.0731  -0.0298 20  LYS A CA  
156  C C   . LYS A 20  ? 0.3822 0.2260 0.4924 -0.0387 0.0778  -0.0511 20  LYS A C   
157  O O   . LYS A 20  ? 0.3705 0.2454 0.5455 -0.0770 0.0762  -0.0415 20  LYS A O   
158  C CB  . LYS A 20  ? 0.4645 0.2646 0.4975 -0.0234 0.0794  -0.0726 20  LYS A CB  
159  C CG  . LYS A 20  ? 0.5096 0.2547 0.5521 -0.0478 0.0601  -0.0708 20  LYS A CG  
160  C CD  . LYS A 20  ? 0.5600 0.2996 0.5730 -0.0449 0.0717  -0.1072 20  LYS A CD  
161  C CE  . LYS A 20  ? 0.6286 0.3175 0.5934 -0.0413 0.0790  -0.1050 20  LYS A CE  
162  N NZ  . LYS A 20  ? 0.6641 0.2593 0.6190 -0.0345 0.0876  -0.1054 20  LYS A NZ  
163  N N   . PHE A 21  ? 0.3680 0.1531 0.4700 -0.0068 0.0697  -0.0219 21  PHE A N   
164  C CA  . PHE A 21  ? 0.3623 0.1528 0.4776 0.0033  0.0497  -0.0072 21  PHE A CA  
165  C C   . PHE A 21  ? 0.3677 0.1885 0.4608 0.0027  0.0402  -0.0045 21  PHE A C   
166  O O   . PHE A 21  ? 0.3397 0.1223 0.4748 -0.0248 0.0280  0.0157  21  PHE A O   
167  C CB  . PHE A 21  ? 0.3307 0.1757 0.4728 0.0345  0.0407  0.0137  21  PHE A CB  
168  C CG  . PHE A 21  ? 0.3381 0.2584 0.4836 0.0506  0.0336  0.0364  21  PHE A CG  
169  C CD1 . PHE A 21  ? 0.3295 0.2841 0.4616 0.0473  0.0213  0.0671  21  PHE A CD1 
170  C CD2 . PHE A 21  ? 0.3730 0.2915 0.4980 0.0677  0.0383  0.0718  21  PHE A CD2 
171  C CE1 . PHE A 21  ? 0.3698 0.3472 0.4903 0.0427  0.0221  0.0756  21  PHE A CE1 
172  C CE2 . PHE A 21  ? 0.3635 0.2830 0.4954 0.0532  0.0279  0.0927  21  PHE A CE2 
173  C CZ  . PHE A 21  ? 0.3739 0.3221 0.4946 0.0591  0.0227  0.0668  21  PHE A CZ  
174  N N   . GLN A 22  ? 0.3882 0.1871 0.4819 0.0044  0.0164  0.0204  22  GLN A N   
175  C CA  . GLN A 22  ? 0.4061 0.2297 0.5272 0.0036  -0.0014 0.0067  22  GLN A CA  
176  C C   . GLN A 22  ? 0.4135 0.2714 0.5646 -0.0210 0.0096  -0.0044 22  GLN A C   
177  O O   . GLN A 22  ? 0.4441 0.3495 0.5721 -0.0758 0.0193  -0.0519 22  GLN A O   
178  C CB  . GLN A 22  ? 0.4368 0.2106 0.5329 0.0059  -0.0059 0.0039  22  GLN A CB  
179  C CG  . GLN A 22  ? 0.4388 0.2057 0.5058 0.0448  -0.0173 0.0080  22  GLN A CG  
180  C CD  . GLN A 22  ? 0.4491 0.2323 0.5066 0.0560  -0.0311 -0.0162 22  GLN A CD  
181  O OE1 . GLN A 22  ? 0.4689 0.2521 0.4943 0.0472  -0.0326 -0.0368 22  GLN A OE1 
182  N NE2 . GLN A 22  ? 0.4770 0.2116 0.4867 0.0243  -0.0461 -0.0128 22  GLN A NE2 
183  N N   . SER A 23  ? 0.3717 0.2305 0.5626 -0.0334 0.0286  0.0115  23  SER A N   
184  C CA  . SER A 23  ? 0.3540 0.2747 0.6070 -0.0147 0.0068  -0.0144 23  SER A CA  
185  C C   . SER A 23  ? 0.3556 0.2226 0.5986 -0.0499 -0.0013 -0.0162 23  SER A C   
186  O O   . SER A 23  ? 0.3336 0.2951 0.5843 -0.0022 0.0247  -0.0308 23  SER A O   
187  C CB  . SER A 23  ? 0.3757 0.3470 0.6225 0.0151  0.0313  0.0195  23  SER A CB  
188  O OG  . SER A 23  ? 0.4441 0.4315 0.7190 0.0487  0.0770  0.0315  23  SER A OG  
189  N N   . GLU A 24  ? 0.3131 0.2410 0.6294 -0.0563 0.0206  -0.0524 24  GLU A N   
190  C CA  . GLU A 24  ? 0.3153 0.2152 0.6874 -0.0414 -0.0113 -0.0899 24  GLU A CA  
191  C C   . GLU A 24  ? 0.3127 0.2412 0.7203 -0.0126 0.0010  -0.1041 24  GLU A C   
192  O O   . GLU A 24  ? 0.3190 0.3062 0.7435 0.0437  -0.0054 -0.1649 24  GLU A O   
193  C CB  . GLU A 24  ? 0.3444 0.2526 0.7249 -0.0714 -0.0348 -0.0871 24  GLU A CB  
194  C CG  . GLU A 24  ? 0.3995 0.3315 0.7739 -0.0398 -0.0218 -0.0941 24  GLU A CG  
195  C CD  . GLU A 24  ? 0.4046 0.3412 0.7799 -0.0529 -0.0357 -0.0990 24  GLU A CD  
196  O OE1 . GLU A 24  ? 0.3696 0.3140 0.8007 0.0015  -0.0586 -0.1631 24  GLU A OE1 
197  O OE2 . GLU A 24  ? 0.4666 0.3450 0.8343 -0.0506 -0.0168 -0.0953 24  GLU A OE2 
198  N N   . LYS A 25  ? 0.3117 0.2178 0.7431 -0.0191 -0.0074 -0.1043 25  LYS A N   
199  C CA  . LYS A 25  ? 0.3599 0.2701 0.7586 -0.0073 -0.0198 -0.0979 25  LYS A CA  
200  C C   . LYS A 25  ? 0.3794 0.2808 0.7533 -0.0219 -0.0514 -0.1285 25  LYS A C   
201  O O   . LYS A 25  ? 0.3211 0.2917 0.7257 0.0338  -0.0559 -0.1830 25  LYS A O   
202  C CB  . LYS A 25  ? 0.3693 0.3202 0.7972 0.0566  -0.0198 -0.0497 25  LYS A CB  
203  C CG  . LYS A 25  ? 0.4244 0.4003 0.8193 0.0696  -0.0239 -0.0409 25  LYS A CG  
204  C CD  . LYS A 25  ? 0.4927 0.4631 0.8591 0.0793  0.0234  -0.0341 25  LYS A CD  
205  C CE  . LYS A 25  ? 0.5488 0.5534 0.8826 0.0552  0.0367  -0.0523 25  LYS A CE  
206  N NZ  . LYS A 25  ? 0.6032 0.6122 0.8903 0.0371  0.0369  -0.0474 25  LYS A NZ  
207  N N   . ALA A 26  ? 0.3983 0.2508 0.8085 -0.0034 -0.0309 -0.1270 26  ALA A N   
208  C CA  . ALA A 26  ? 0.4502 0.1917 0.8299 -0.0014 -0.0514 -0.0967 26  ALA A CA  
209  C C   . ALA A 26  ? 0.3803 0.2736 0.8657 -0.0367 -0.0732 -0.0706 26  ALA A C   
210  O O   . ALA A 26  ? 0.4120 0.2779 0.9137 -0.0734 -0.0648 -0.0476 26  ALA A O   
211  C CB  . ALA A 26  ? 0.4915 0.2249 0.8371 0.0300  -0.0472 -0.0975 26  ALA A CB  
212  N N   . ALA A 27  ? 0.3422 0.2548 0.8905 -0.0015 -0.0708 -0.0439 27  ALA A N   
213  C CA  . ALA A 27  ? 0.2989 0.3181 0.9082 -0.0483 -0.0534 -0.1064 27  ALA A CA  
214  C C   . ALA A 27  ? 0.3787 0.3121 0.9108 -0.0360 -0.0849 -0.1352 27  ALA A C   
215  O O   . ALA A 27  ? 0.3394 0.3979 0.9783 -0.0135 -0.1044 -0.1405 27  ALA A O   
216  C CB  . ALA A 27  ? 0.3149 0.4019 0.8988 -0.0123 -0.0227 -0.0816 27  ALA A CB  
217  N N   . GLY A 28  ? 0.4275 0.2904 0.9038 -0.0973 -0.0675 -0.1015 28  GLY A N   
218  C CA  . GLY A 28  ? 0.4948 0.2962 0.9472 -0.0531 -0.1060 -0.0925 28  GLY A CA  
219  C C   . GLY A 28  ? 0.5651 0.3085 0.9960 -0.0472 -0.1115 -0.0720 28  GLY A C   
220  O O   . GLY A 28  ? 0.6976 0.2773 0.9807 -0.0077 -0.1477 -0.0627 28  GLY A O   
221  N N   . SER A 29  ? 0.5922 0.4191 1.0469 -0.0466 -0.1368 -0.0457 29  SER A N   
222  C CA  . SER A 29  ? 0.6681 0.4702 1.0736 -0.0306 -0.1156 -0.0633 29  SER A CA  
223  C C   . SER A 29  ? 0.6676 0.4306 1.0811 -0.0539 -0.1053 -0.0663 29  SER A C   
224  O O   . SER A 29  ? 0.7836 0.5419 1.0919 -0.0341 -0.1401 -0.0166 29  SER A O   
225  C CB  . SER A 29  ? 0.6879 0.5468 1.1051 -0.0021 -0.0877 -0.0463 29  SER A CB  
226  O OG  . SER A 29  ? 0.6486 0.7158 1.1230 -0.0249 -0.0860 -0.0064 29  SER A OG  
227  N N   . VAL A 30  ? 0.6734 0.2982 1.0439 -0.0172 -0.0704 -0.1014 30  VAL A N   
228  C CA  . VAL A 30  ? 0.6041 0.3520 0.9797 -0.0095 -0.0741 -0.1070 30  VAL A CA  
229  C C   . VAL A 30  ? 0.4750 0.3624 0.8278 0.0023  -0.0680 -0.0588 30  VAL A C   
230  O O   . VAL A 30  ? 0.4491 0.3210 0.8106 0.0251  -0.0759 -0.0768 30  VAL A O   
231  C CB  . VAL A 30  ? 0.6446 0.3687 1.0364 0.0055  -0.0705 -0.0902 30  VAL A CB  
232  C CG1 . VAL A 30  ? 0.6524 0.2661 1.0737 0.0218  -0.0763 -0.1072 30  VAL A CG1 
233  C CG2 . VAL A 30  ? 0.6641 0.3425 1.1103 0.0096  -0.0479 -0.0839 30  VAL A CG2 
234  N N   . SER A 31  ? 0.3607 0.2790 0.7735 -0.0047 -0.0415 -0.0623 31  SER A N   
235  C CA  . SER A 31  ? 0.3406 0.2515 0.7380 0.0334  -0.0183 -0.0143 31  SER A CA  
236  C C   . SER A 31  ? 0.3480 0.1913 0.7256 0.0200  -0.0171 -0.0245 31  SER A C   
237  O O   . SER A 31  ? 0.3277 0.2261 0.6887 0.0013  -0.0474 -0.0323 31  SER A O   
238  C CB  . SER A 31  ? 0.3612 0.2222 0.7273 0.0214  0.0279  -0.0269 31  SER A CB  
239  O OG  . SER A 31  ? 0.4104 0.1686 0.7372 0.0401  0.0429  -0.0401 31  SER A OG  
240  N N   . LYS A 32  ? 0.3485 0.1911 0.6842 0.0352  -0.0426 0.0256  32  LYS A N   
241  C CA  . LYS A 32  ? 0.3387 0.2489 0.6787 0.0259  -0.0254 0.0269  32  LYS A CA  
242  C C   . LYS A 32  ? 0.3428 0.1946 0.6032 0.0136  0.0070  0.0228  32  LYS A C   
243  O O   . LYS A 32  ? 0.3123 0.1829 0.5703 -0.0139 0.0069  0.0450  32  LYS A O   
244  C CB  . LYS A 32  ? 0.4409 0.2690 0.7188 0.0413  -0.0338 0.0699  32  LYS A CB  
245  C CG  . LYS A 32  ? 0.4754 0.3682 0.7716 0.0501  -0.0291 0.0601  32  LYS A CG  
246  C CD  . LYS A 32  ? 0.5455 0.3748 0.8127 0.0741  -0.0060 0.0826  32  LYS A CD  
247  C CE  . LYS A 32  ? 0.5704 0.3977 0.8499 0.0567  0.0199  0.0721  32  LYS A CE  
248  N NZ  . LYS A 32  ? 0.5772 0.3132 0.8817 0.0894  0.0244  0.1069  32  LYS A NZ  
249  N N   . SER A 33  ? 0.3438 0.1094 0.5899 -0.0179 0.0286  -0.0097 33  SER A N   
250  C CA  . SER A 33  ? 0.3641 0.1625 0.5912 0.0000  0.0042  -0.0372 33  SER A CA  
251  C C   . SER A 33  ? 0.2869 0.1709 0.5584 -0.0082 0.0042  -0.0256 33  SER A C   
252  O O   . SER A 33  ? 0.3032 0.1800 0.4992 0.0028  -0.0010 -0.0030 33  SER A O   
253  C CB  . SER A 33  ? 0.3864 0.2515 0.5922 0.0517  0.0113  -0.0573 33  SER A CB  
254  O OG  . SER A 33  ? 0.4302 0.4058 0.6528 0.0341  -0.0230 -0.0569 33  SER A OG  
255  N N   . THR A 34  ? 0.2753 0.1544 0.5979 0.0016  -0.0026 -0.0199 34  THR A N   
256  C CA  . THR A 34  ? 0.2861 0.1282 0.5599 -0.0126 -0.0106 -0.0159 34  THR A CA  
257  C C   . THR A 34  ? 0.2707 0.1163 0.5098 -0.0313 -0.0291 0.0083  34  THR A C   
258  O O   . THR A 34  ? 0.2792 0.1279 0.4773 0.0046  0.0115  0.0199  34  THR A O   
259  C CB  . THR A 34  ? 0.2906 0.1332 0.5884 -0.0107 0.0152  0.0057  34  THR A CB  
260  O OG1 . THR A 34  ? 0.3476 0.1843 0.6407 0.0145  0.0659  0.0046  34  THR A OG1 
261  C CG2 . THR A 34  ? 0.2705 0.1177 0.5929 -0.0189 0.0241  0.0559  34  THR A CG2 
262  N N   . GLN A 35  ? 0.3000 0.1211 0.4858 -0.0109 -0.0532 0.0071  35  GLN A N   
263  C CA  . GLN A 35  ? 0.3140 0.0883 0.4706 -0.0054 -0.0474 0.0128  35  GLN A CA  
264  C C   . GLN A 35  ? 0.3011 0.1126 0.4073 -0.0064 -0.0391 0.0008  35  GLN A C   
265  O O   . GLN A 35  ? 0.3068 0.1119 0.4156 0.0175  -0.0510 0.0130  35  GLN A O   
266  C CB  . GLN A 35  ? 0.3598 0.1675 0.5142 -0.0200 -0.0675 0.0154  35  GLN A CB  
267  C CG  . GLN A 35  ? 0.4394 0.2775 0.5510 -0.0294 -0.0886 0.0289  35  GLN A CG  
268  C CD  . GLN A 35  ? 0.5438 0.4202 0.5743 0.0206  -0.0881 0.0592  35  GLN A CD  
269  O OE1 . GLN A 35  ? 0.6292 0.4122 0.6570 0.0549  -0.1128 0.1244  35  GLN A OE1 
270  N NE2 . GLN A 35  ? 0.5828 0.4778 0.5812 0.0066  -0.0390 0.0657  35  GLN A NE2 
271  N N   . PHE A 36  ? 0.2878 0.1098 0.4125 -0.0073 -0.0269 0.0031  36  PHE A N   
272  C CA  . PHE A 36  ? 0.2807 0.0656 0.3694 -0.0100 -0.0104 0.0119  36  PHE A CA  
273  C C   . PHE A 36  ? 0.2749 0.0939 0.3439 0.0005  -0.0029 0.0138  36  PHE A C   
274  O O   . PHE A 36  ? 0.2720 0.0684 0.3590 0.0007  -0.0025 0.0034  36  PHE A O   
275  C CB  . PHE A 36  ? 0.2688 0.1009 0.3698 -0.0120 0.0038  -0.0064 36  PHE A CB  
276  C CG  . PHE A 36  ? 0.2742 0.1256 0.3844 -0.0121 -0.0019 -0.0137 36  PHE A CG  
277  C CD1 . PHE A 36  ? 0.2736 0.0855 0.3669 -0.0071 -0.0029 -0.0215 36  PHE A CD1 
278  C CD2 . PHE A 36  ? 0.3070 0.1857 0.3860 -0.0393 0.0033  -0.0143 36  PHE A CD2 
279  C CE1 . PHE A 36  ? 0.2728 0.1448 0.3864 -0.0166 -0.0102 -0.0323 36  PHE A CE1 
280  C CE2 . PHE A 36  ? 0.3205 0.1834 0.3905 -0.0308 0.0009  -0.0317 36  PHE A CE2 
281  C CZ  . PHE A 36  ? 0.2690 0.1751 0.4061 -0.0459 -0.0044 -0.0186 36  PHE A CZ  
282  N N   . GLU A 37  ? 0.2679 0.1315 0.3622 -0.0119 0.0076  0.0058  37  GLU A N   
283  C CA  . GLU A 37  ? 0.3036 0.1151 0.3617 -0.0104 0.0177  0.0006  37  GLU A CA  
284  C C   . GLU A 37  ? 0.2673 0.1413 0.3438 -0.0014 0.0319  0.0094  37  GLU A C   
285  O O   . GLU A 37  ? 0.2821 0.1265 0.3369 0.0028  0.0188  0.0259  37  GLU A O   
286  C CB  . GLU A 37  ? 0.3271 0.2094 0.3995 -0.0046 0.0438  0.0029  37  GLU A CB  
287  C CG  . GLU A 37  ? 0.4015 0.2271 0.4587 -0.0057 0.0796  -0.0018 37  GLU A CG  
288  C CD  . GLU A 37  ? 0.4756 0.2951 0.5426 -0.0233 0.1214  -0.0096 37  GLU A CD  
289  O OE1 . GLU A 37  ? 0.5052 0.2664 0.6130 -0.0531 0.1682  -0.0088 37  GLU A OE1 
290  O OE2 . GLU A 37  ? 0.5829 0.3147 0.6103 0.0309  0.1670  -0.0062 37  GLU A OE2 
291  N N   . GLU A 38  ? 0.2711 0.1240 0.3324 -0.0028 0.0424  0.0103  38  GLU A N   
292  C CA  . GLU A 38  ? 0.3020 0.1048 0.3341 0.0074  0.0219  0.0225  38  GLU A CA  
293  C C   . GLU A 38  ? 0.3055 0.1108 0.3104 0.0066  0.0170  0.0335  38  GLU A C   
294  O O   . GLU A 38  ? 0.3096 0.0903 0.3389 -0.0191 0.0144  0.0087  38  GLU A O   
295  C CB  . GLU A 38  ? 0.3592 0.1623 0.3567 -0.0167 0.0039  0.0113  38  GLU A CB  
296  C CG  . GLU A 38  ? 0.4070 0.1483 0.3856 -0.0166 0.0125  0.0169  38  GLU A CG  
297  C CD  . GLU A 38  ? 0.4359 0.1214 0.3811 -0.0549 0.0087  0.0191  38  GLU A CD  
298  O OE1 . GLU A 38  ? 0.4304 0.2754 0.4405 -0.0768 -0.0117 -0.0254 38  GLU A OE1 
299  O OE2 . GLU A 38  ? 0.5378 0.1693 0.4057 -0.0974 0.0095  -0.0214 38  GLU A OE2 
300  N N   . ALA A 39  ? 0.2793 0.1005 0.3214 0.0067  0.0146  0.0283  39  ALA A N   
301  C CA  . ALA A 39  ? 0.2746 0.1178 0.3248 0.0044  0.0259  0.0174  39  ALA A CA  
302  C C   . ALA A 39  ? 0.2692 0.1068 0.3131 0.0172  0.0225  0.0185  39  ALA A C   
303  O O   . ALA A 39  ? 0.2651 0.1057 0.3445 0.0029  0.0374  -0.0056 39  ALA A O   
304  C CB  . ALA A 39  ? 0.2976 0.1346 0.3313 0.0238  0.0052  0.0094  39  ALA A CB  
305  N N   . TRP A 40  ? 0.2829 0.1054 0.3278 -0.0017 0.0231  0.0059  40  TRP A N   
306  C CA  . TRP A 40  ? 0.3009 0.1043 0.3408 0.0022  0.0158  0.0018  40  TRP A CA  
307  C C   . TRP A 40  ? 0.3013 0.1344 0.3429 0.0126  0.0169  0.0004  40  TRP A C   
308  O O   . TRP A 40  ? 0.2865 0.1233 0.3560 0.0175  0.0230  -0.0101 40  TRP A O   
309  C CB  . TRP A 40  ? 0.3228 0.1143 0.3515 -0.0028 0.0109  -0.0078 40  TRP A CB  
310  C CG  . TRP A 40  ? 0.3352 0.1463 0.3439 0.0011  0.0025  -0.0098 40  TRP A CG  
311  C CD1 . TRP A 40  ? 0.3492 0.1491 0.3550 -0.0051 -0.0058 -0.0021 40  TRP A CD1 
312  C CD2 . TRP A 40  ? 0.3372 0.1386 0.3622 0.0143  -0.0115 -0.0214 40  TRP A CD2 
313  N NE1 . TRP A 40  ? 0.3584 0.1574 0.3631 -0.0082 -0.0228 -0.0097 40  TRP A NE1 
314  C CE2 . TRP A 40  ? 0.3740 0.1647 0.3510 0.0057  -0.0077 -0.0143 40  TRP A CE2 
315  C CE3 . TRP A 40  ? 0.3803 0.1421 0.3641 0.0215  -0.0015 -0.0111 40  TRP A CE3 
316  C CZ2 . TRP A 40  ? 0.3910 0.1765 0.3378 0.0144  0.0027  -0.0188 40  TRP A CZ2 
317  C CZ3 . TRP A 40  ? 0.4164 0.1463 0.3649 0.0378  0.0031  -0.0008 40  TRP A CZ3 
318  C CH2 . TRP A 40  ? 0.4262 0.1749 0.3568 0.0109  -0.0082 0.0234  40  TRP A CH2 
319  N N   A CYS A 41  ? 0.2933 0.1024 0.3168 0.0276  0.0211  0.0065  41  CYS A N   
320  N N   B CYS A 41  ? 0.3019 0.1175 0.3283 0.0208  0.0255  0.0046  41  CYS A N   
321  C CA  A CYS A 41  ? 0.3021 0.0976 0.3233 0.0269  0.0149  0.0026  41  CYS A CA  
322  C CA  B CYS A 41  ? 0.3194 0.1320 0.3417 0.0345  0.0202  0.0007  41  CYS A CA  
323  C C   A CYS A 41  ? 0.2923 0.0934 0.3228 0.0068  0.0134  -0.0016 41  CYS A C   
324  C C   B CYS A 41  ? 0.3001 0.1168 0.3310 0.0083  0.0139  -0.0003 41  CYS A C   
325  O O   A CYS A 41  ? 0.2946 0.1470 0.3210 0.0045  0.0135  -0.0183 41  CYS A O   
326  O O   B CYS A 41  ? 0.3022 0.1521 0.3344 0.0044  0.0049  -0.0083 41  CYS A O   
327  C CB  A CYS A 41  ? 0.3152 0.1164 0.3344 0.0210  0.0122  0.0171  41  CYS A CB  
328  C CB  B CYS A 41  ? 0.3379 0.1910 0.3651 0.0235  0.0291  0.0121  41  CYS A CB  
329  S SG  A CYS A 41  ? 0.3269 0.0970 0.3453 -0.0036 0.0108  0.0386  41  CYS A SG  
330  S SG  B CYS A 41  ? 0.4090 0.2260 0.4524 0.0503  0.0222  0.0399  41  CYS A SG  
331  N N   . LEU A 42  ? 0.2828 0.1119 0.3204 0.0024  0.0168  -0.0033 42  LEU A N   
332  C CA  . LEU A 42  ? 0.2626 0.1199 0.3385 0.0002  0.0276  0.0025  42  LEU A CA  
333  C C   . LEU A 42  ? 0.2649 0.1298 0.3334 -0.0018 0.0259  0.0079  42  LEU A C   
334  O O   . LEU A 42  ? 0.2704 0.1352 0.3377 0.0130  0.0194  0.0114  42  LEU A O   
335  C CB  . LEU A 42  ? 0.2853 0.1328 0.3451 -0.0385 0.0250  0.0155  42  LEU A CB  
336  C CG  . LEU A 42  ? 0.2853 0.1175 0.3766 -0.0344 0.0160  0.0051  42  LEU A CG  
337  C CD1 . LEU A 42  ? 0.3023 0.1586 0.3824 -0.0590 0.0026  -0.0038 42  LEU A CD1 
338  C CD2 . LEU A 42  ? 0.3239 0.1052 0.4072 -0.0301 0.0088  0.0153  42  LEU A CD2 
339  N N   . VAL A 43  ? 0.2692 0.1500 0.3611 -0.0036 0.0200  -0.0273 43  VAL A N   
340  C CA  . VAL A 43  ? 0.2649 0.1376 0.3767 0.0029  0.0352  -0.0253 43  VAL A CA  
341  C C   . VAL A 43  ? 0.2606 0.1311 0.3589 0.0054  0.0385  -0.0382 43  VAL A C   
342  O O   . VAL A 43  ? 0.2534 0.1702 0.3835 -0.0171 0.0134  -0.0271 43  VAL A O   
343  C CB  . VAL A 43  ? 0.2943 0.1355 0.4168 -0.0079 0.0367  -0.0556 43  VAL A CB  
344  C CG1 . VAL A 43  ? 0.2938 0.1230 0.4192 -0.0021 0.0490  -0.0426 43  VAL A CG1 
345  C CG2 . VAL A 43  ? 0.2869 0.1658 0.4119 -0.0319 0.0457  -0.0343 43  VAL A CG2 
346  N N   . ARG A 44  ? 0.2834 0.2024 0.3587 -0.0232 0.0289  -0.0060 44  ARG A N   
347  C CA  . ARG A 44  ? 0.3163 0.2044 0.3518 -0.0140 0.0042  -0.0182 44  ARG A CA  
348  C C   . ARG A 44  ? 0.3111 0.2310 0.3126 0.0216  0.0000  -0.0094 44  ARG A C   
349  O O   . ARG A 44  ? 0.3487 0.2456 0.3242 0.0182  -0.0285 -0.0150 44  ARG A O   
350  C CB  . ARG A 44  ? 0.3320 0.2347 0.3443 -0.0129 -0.0025 -0.0123 44  ARG A CB  
351  C CG  . ARG A 44  ? 0.3511 0.2570 0.3570 -0.0108 0.0000  -0.0285 44  ARG A CG  
352  C CD  . ARG A 44  ? 0.3516 0.2335 0.3753 -0.0162 0.0062  -0.0224 44  ARG A CD  
353  N NE  . ARG A 44  ? 0.3603 0.2074 0.4002 0.0236  -0.0044 -0.0135 44  ARG A NE  
354  C CZ  . ARG A 44  ? 0.3652 0.1972 0.4115 0.0138  -0.0139 -0.0384 44  ARG A CZ  
355  N NH1 . ARG A 44  ? 0.3755 0.2246 0.4350 -0.0091 -0.0206 -0.0393 44  ARG A NH1 
356  N NH2 . ARG A 44  ? 0.3718 0.2040 0.4264 -0.0146 -0.0143 -0.0549 44  ARG A NH2 
357  N N   . SER A 45  ? 0.3143 0.1426 0.3137 0.0206  0.0091  -0.0016 45  SER A N   
358  C CA  . SER A 45  ? 0.3263 0.1274 0.3307 0.0103  0.0065  0.0165  45  SER A CA  
359  C C   . SER A 45  ? 0.3354 0.1370 0.3274 0.0202  0.0077  0.0130  45  SER A C   
360  O O   . SER A 45  ? 0.3920 0.1471 0.3412 -0.0237 -0.0024 0.0289  45  SER A O   
361  C CB  . SER A 45  ? 0.3192 0.1214 0.3412 0.0140  0.0003  0.0138  45  SER A CB  
362  O OG  . SER A 45  ? 0.3299 0.0937 0.3800 -0.0064 -0.0117 0.0196  45  SER A OG  
363  N N   . LYS A 46  ? 0.3809 0.1420 0.3578 0.0259  -0.0108 0.0135  46  LYS A N   
364  C CA  . LYS A 46  ? 0.3964 0.1867 0.3998 0.0299  0.0015  0.0139  46  LYS A CA  
365  C C   . LYS A 46  ? 0.3339 0.1531 0.3978 0.0114  0.0054  0.0055  46  LYS A C   
366  O O   . LYS A 46  ? 0.3434 0.2641 0.4211 0.0237  0.0144  -0.0257 46  LYS A O   
367  C CB  . LYS A 46  ? 0.4491 0.2552 0.4658 0.0994  0.0016  0.0103  46  LYS A CB  
368  C CG  . LYS A 46  ? 0.5516 0.2586 0.5314 0.0989  0.0072  0.0222  46  LYS A CG  
369  C CD  . LYS A 46  ? 0.6364 0.2800 0.6178 0.1311  0.0116  0.0686  46  LYS A CD  
370  C CE  . LYS A 46  ? 0.6968 0.3555 0.6957 0.1076  0.0149  0.0390  46  LYS A CE  
371  N NZ  . LYS A 46  ? 0.7539 0.4256 0.7244 0.1163  -0.0018 0.0639  46  LYS A NZ  
372  N N   . TYR A 47  ? 0.3014 0.1068 0.3758 0.0078  0.0089  0.0147  47  TYR A N   
373  C CA  . TYR A 47  ? 0.2965 0.1130 0.3713 0.0120  0.0064  0.0242  47  TYR A CA  
374  C C   . TYR A 47  ? 0.2949 0.1105 0.3443 0.0083  0.0032  0.0101  47  TYR A C   
375  O O   . TYR A 47  ? 0.2798 0.1270 0.3501 0.0068  0.0087  -0.0010 47  TYR A O   
376  C CB  . TYR A 47  ? 0.3057 0.1312 0.3773 0.0174  -0.0106 0.0042  47  TYR A CB  
377  C CG  . TYR A 47  ? 0.3236 0.1270 0.3664 0.0243  -0.0023 0.0001  47  TYR A CG  
378  C CD1 . TYR A 47  ? 0.3562 0.1718 0.3975 0.0622  0.0059  0.0169  47  TYR A CD1 
379  C CD2 . TYR A 47  ? 0.3579 0.1464 0.3710 0.0475  -0.0058 0.0192  47  TYR A CD2 
380  C CE1 . TYR A 47  ? 0.3608 0.1766 0.4173 0.0726  -0.0131 0.0250  47  TYR A CE1 
381  C CE2 . TYR A 47  ? 0.3789 0.1565 0.4037 0.0472  -0.0032 0.0359  47  TYR A CE2 
382  C CZ  . TYR A 47  ? 0.3539 0.1709 0.4258 0.0583  0.0008  0.0305  47  TYR A CZ  
383  O OH  . TYR A 47  ? 0.3806 0.1729 0.4900 0.0487  -0.0576 0.0274  47  TYR A OH  
384  N N   . ASN A 48  ? 0.3100 0.1683 0.3684 0.0040  0.0218  -0.0018 48  ASN A N   
385  C CA  . ASN A 48  ? 0.3362 0.1564 0.3605 -0.0074 0.0313  -0.0084 48  ASN A CA  
386  C C   . ASN A 48  ? 0.3356 0.1373 0.3663 -0.0094 0.0217  -0.0165 48  ASN A C   
387  O O   . ASN A 48  ? 0.3247 0.1353 0.3445 0.0055  0.0423  0.0109  48  ASN A O   
388  C CB  . ASN A 48  ? 0.3428 0.1855 0.4002 -0.0110 0.0492  -0.0120 48  ASN A CB  
389  C CG  . ASN A 48  ? 0.3735 0.2645 0.4420 -0.0315 0.0461  -0.0136 48  ASN A CG  
390  O OD1 . ASN A 48  ? 0.4111 0.2721 0.4613 -0.0438 0.0259  -0.0004 48  ASN A OD1 
391  N ND2 . ASN A 48  ? 0.4038 0.3830 0.4894 -0.0363 0.0703  -0.0391 48  ASN A ND2 
392  N N   . ASP A 49  ? 0.3403 0.1495 0.3668 -0.0088 0.0230  -0.0381 49  ASP A N   
393  C CA  . ASP A 49  ? 0.3611 0.1897 0.3799 0.0129  0.0060  -0.0489 49  ASP A CA  
394  C C   . ASP A 49  ? 0.3324 0.1586 0.3473 -0.0096 0.0017  -0.0248 49  ASP A C   
395  O O   . ASP A 49  ? 0.3284 0.1800 0.3645 0.0022  0.0146  -0.0338 49  ASP A O   
396  C CB  . ASP A 49  ? 0.4044 0.2419 0.4385 -0.0054 0.0139  -0.1000 49  ASP A CB  
397  C CG  . ASP A 49  ? 0.4870 0.3486 0.4988 0.0015  0.0400  -0.1143 49  ASP A CG  
398  O OD1 . ASP A 49  ? 0.5494 0.4970 0.5144 0.0011  0.1010  -0.0857 49  ASP A OD1 
399  O OD2 . ASP A 49  ? 0.6101 0.3990 0.5915 0.0767  0.0154  -0.1872 49  ASP A OD2 
400  N N   . ASP A 50  ? 0.3190 0.1187 0.3467 0.0090  0.0000  -0.0022 50  ASP A N   
401  C CA  . ASP A 50  ? 0.2889 0.1069 0.3209 -0.0111 -0.0024 0.0078  50  ASP A CA  
402  C C   . ASP A 50  ? 0.2945 0.1106 0.3094 -0.0134 0.0034  -0.0050 50  ASP A C   
403  O O   . ASP A 50  ? 0.2917 0.1093 0.3180 -0.0207 0.0061  -0.0018 50  ASP A O   
404  C CB  . ASP A 50  ? 0.2840 0.1070 0.3361 -0.0155 -0.0096 0.0114  50  ASP A CB  
405  C CG  . ASP A 50  ? 0.3336 0.1112 0.3742 -0.0204 -0.0098 0.0025  50  ASP A CG  
406  O OD1 . ASP A 50  ? 0.3497 0.1232 0.4173 -0.0053 -0.0224 -0.0022 50  ASP A OD1 
407  O OD2 . ASP A 50  ? 0.3579 0.1218 0.3982 -0.0118 -0.0049 0.0097  50  ASP A OD2 
408  N N   . ILE A 51  ? 0.2832 0.0919 0.3105 0.0030  0.0071  -0.0004 51  ILE A N   
409  C CA  . ILE A 51  ? 0.2880 0.0965 0.3056 -0.0037 0.0055  -0.0167 51  ILE A CA  
410  C C   . ILE A 51  ? 0.2816 0.0980 0.3071 -0.0150 0.0054  -0.0114 51  ILE A C   
411  O O   . ILE A 51  ? 0.2906 0.0880 0.3131 -0.0019 0.0145  0.0032  51  ILE A O   
412  C CB  . ILE A 51  ? 0.2842 0.1148 0.3083 -0.0017 0.0055  -0.0083 51  ILE A CB  
413  C CG1 . ILE A 51  ? 0.2937 0.0970 0.3189 0.0167  -0.0084 -0.0135 51  ILE A CG1 
414  C CG2 . ILE A 51  ? 0.2899 0.1225 0.3114 -0.0155 0.0015  -0.0242 51  ILE A CG2 
415  C CD1 . ILE A 51  ? 0.3087 0.1073 0.3479 0.0405  -0.0223 0.0206  51  ILE A CD1 
416  N N   A ARG A 52  ? 0.2948 0.0790 0.3096 -0.0260 0.0009  -0.0020 52  ARG A N   
417  N N   B ARG A 52  ? 0.3002 0.0809 0.3098 -0.0204 0.0044  0.0039  52  ARG A N   
418  C CA  A ARG A 52  ? 0.3162 0.1153 0.3010 -0.0289 0.0013  0.0096  52  ARG A CA  
419  C CA  B ARG A 52  ? 0.3241 0.1171 0.3042 -0.0201 0.0072  0.0216  52  ARG A CA  
420  C C   A ARG A 52  ? 0.3199 0.1108 0.2996 -0.0219 0.0033  0.0116  52  ARG A C   
421  C C   B ARG A 52  ? 0.3259 0.1133 0.2972 -0.0177 0.0058  0.0181  52  ARG A C   
422  O O   A ARG A 52  ? 0.3373 0.1065 0.3072 -0.0157 -0.0002 0.0010  52  ARG A O   
423  O O   B ARG A 52  ? 0.3430 0.1174 0.2931 -0.0123 -0.0017 0.0076  52  ARG A O   
424  C CB  A ARG A 52  ? 0.3248 0.1369 0.3025 -0.0229 0.0060  0.0140  52  ARG A CB  
425  C CB  B ARG A 52  ? 0.3421 0.1386 0.3109 -0.0037 0.0177  0.0330  52  ARG A CB  
426  C CG  A ARG A 52  ? 0.3217 0.1837 0.2893 -0.0205 0.0012  0.0095  52  ARG A CG  
427  C CG  B ARG A 52  ? 0.3418 0.2000 0.3128 0.0083  0.0181  0.0295  52  ARG A CG  
428  C CD  A ARG A 52  ? 0.3384 0.2120 0.2871 -0.0258 0.0024  0.0113  52  ARG A CD  
429  C CD  B ARG A 52  ? 0.3766 0.2573 0.3090 0.0113  0.0254  0.0284  52  ARG A CD  
430  N NE  A ARG A 52  ? 0.3721 0.3006 0.3100 -0.0389 0.0194  0.0103  52  ARG A NE  
431  N NE  B ARG A 52  ? 0.3998 0.3015 0.3276 0.0210  0.0357  0.0357  52  ARG A NE  
432  C CZ  A ARG A 52  ? 0.3665 0.3289 0.3001 -0.0658 0.0210  0.0064  52  ARG A CZ  
433  C CZ  B ARG A 52  ? 0.4023 0.3731 0.3530 0.0456  0.0454  0.0258  52  ARG A CZ  
434  N NH1 A ARG A 52  ? 0.3954 0.3344 0.3194 -0.0780 0.0279  0.0027  52  ARG A NH1 
435  N NH1 B ARG A 52  ? 0.4040 0.3779 0.3470 0.0665  0.0449  0.0355  52  ARG A NH1 
436  N NH2 A ARG A 52  ? 0.3687 0.3761 0.3078 -0.0832 0.0229  0.0146  52  ARG A NH2 
437  N NH2 B ARG A 52  ? 0.4394 0.4399 0.3903 0.0100  0.0315  0.0189  52  ARG A NH2 
438  N N   . LYS A 53  ? 0.3275 0.1097 0.3118 -0.0177 0.0185  0.0047  53  LYS A N   
439  C CA  . LYS A 53  ? 0.3210 0.1067 0.3211 -0.0117 0.0087  0.0084  53  LYS A CA  
440  C C   . LYS A 53  ? 0.2865 0.0980 0.3149 0.0075  0.0012  0.0174  53  LYS A C   
441  O O   . LYS A 53  ? 0.2862 0.1081 0.3188 0.0093  -0.0093 0.0123  53  LYS A O   
442  C CB  . LYS A 53  ? 0.3557 0.1093 0.3532 0.0030  -0.0036 0.0215  53  LYS A CB  
443  C CG  . LYS A 53  ? 0.3782 0.2341 0.3975 -0.0006 -0.0066 0.0105  53  LYS A CG  
444  C CD  . LYS A 53  ? 0.4099 0.3219 0.4471 -0.0044 -0.0092 0.0276  53  LYS A CD  
445  C CE  . LYS A 53  ? 0.4164 0.4205 0.5117 -0.0198 -0.0249 0.0094  53  LYS A CE  
446  N NZ  . LYS A 53  ? 0.4747 0.5085 0.5639 -0.0043 -0.0364 0.0167  53  LYS A NZ  
447  N N   . GLY A 54  ? 0.2874 0.0884 0.2995 0.0148  0.0225  -0.0013 54  GLY A N   
448  C CA  . GLY A 54  ? 0.2710 0.0874 0.3053 -0.0005 0.0152  0.0038  54  GLY A CA  
449  C C   . GLY A 54  ? 0.2964 0.1012 0.3148 0.0020  0.0077  0.0220  54  GLY A C   
450  O O   . GLY A 54  ? 0.2851 0.1135 0.3056 0.0011  0.0106  0.0279  54  GLY A O   
451  N N   . ILE A 55  ? 0.3049 0.0881 0.2923 -0.0005 -0.0017 0.0130  55  ILE A N   
452  C CA  . ILE A 55  ? 0.3207 0.0849 0.3095 -0.0095 -0.0158 0.0133  55  ILE A CA  
453  C C   . ILE A 55  ? 0.3416 0.1006 0.3150 -0.0037 -0.0268 0.0050  55  ILE A C   
454  O O   . ILE A 55  ? 0.3185 0.1152 0.3216 0.0113  -0.0228 0.0164  55  ILE A O   
455  C CB  . ILE A 55  ? 0.3274 0.0916 0.3309 -0.0009 -0.0227 0.0232  55  ILE A CB  
456  C CG1 . ILE A 55  ? 0.3274 0.1116 0.3408 -0.0050 -0.0227 0.0319  55  ILE A CG1 
457  C CG2 . ILE A 55  ? 0.3168 0.0986 0.3260 -0.0278 -0.0401 0.0278  55  ILE A CG2 
458  C CD1 . ILE A 55  ? 0.3232 0.1077 0.3542 -0.0169 -0.0102 0.0163  55  ILE A CD1 
459  N N   . VAL A 56  ? 0.3449 0.1162 0.3056 -0.0101 -0.0174 -0.0110 56  VAL A N   
460  C CA  . VAL A 56  ? 0.3595 0.1458 0.3060 -0.0067 -0.0240 -0.0062 56  VAL A CA  
461  C C   . VAL A 56  ? 0.3311 0.1382 0.3083 -0.0064 -0.0340 -0.0023 56  VAL A C   
462  O O   . VAL A 56  ? 0.3320 0.1372 0.3149 -0.0095 -0.0509 0.0211  56  VAL A O   
463  C CB  . VAL A 56  ? 0.3949 0.2074 0.3191 -0.0089 -0.0277 -0.0354 56  VAL A CB  
464  C CG1 . VAL A 56  ? 0.3991 0.2336 0.3359 -0.0180 -0.0104 -0.0360 56  VAL A CG1 
465  C CG2 . VAL A 56  ? 0.3916 0.2573 0.3493 0.0047  -0.0360 -0.0274 56  VAL A CG2 
466  N N   . LEU A 57  ? 0.3204 0.1187 0.3163 0.0103  -0.0175 -0.0024 57  LEU A N   
467  C CA  . LEU A 57  ? 0.3344 0.1201 0.3131 -0.0009 -0.0126 -0.0109 57  LEU A CA  
468  C C   . LEU A 57  ? 0.2994 0.1094 0.3390 0.0011  -0.0173 -0.0096 57  LEU A C   
469  O O   . LEU A 57  ? 0.3297 0.1393 0.3738 0.0132  -0.0306 -0.0223 57  LEU A O   
470  C CB  . LEU A 57  ? 0.3286 0.1443 0.3414 -0.0033 -0.0211 0.0046  57  LEU A CB  
471  C CG  . LEU A 57  ? 0.3724 0.1626 0.4102 0.0023  -0.0120 0.0022  57  LEU A CG  
472  C CD1 . LEU A 57  ? 0.3650 0.2090 0.4236 -0.0460 -0.0043 0.0389  57  LEU A CD1 
473  C CD2 . LEU A 57  ? 0.4041 0.2031 0.4359 -0.0051 -0.0118 -0.0107 57  LEU A CD2 
474  N N   . LEU A 58  ? 0.2920 0.1008 0.3350 0.0192  -0.0274 0.0105  58  LEU A N   
475  C CA  . LEU A 58  ? 0.2964 0.1153 0.3380 0.0196  -0.0173 0.0062  58  LEU A CA  
476  C C   . LEU A 58  ? 0.2877 0.1367 0.3604 0.0152  -0.0230 0.0234  58  LEU A C   
477  O O   . LEU A 58  ? 0.3023 0.1198 0.3598 0.0376  -0.0187 0.0197  58  LEU A O   
478  C CB  . LEU A 58  ? 0.3180 0.1082 0.3433 -0.0167 -0.0260 0.0197  58  LEU A CB  
479  C CG  . LEU A 58  ? 0.3194 0.0990 0.3260 -0.0076 -0.0158 0.0216  58  LEU A CG  
480  C CD1 . LEU A 58  ? 0.3308 0.1321 0.3101 -0.0231 -0.0154 0.0184  58  LEU A CD1 
481  C CD2 . LEU A 58  ? 0.3357 0.1421 0.3387 -0.0039 -0.0198 0.0198  58  LEU A CD2 
482  N N   . GLU A 59  ? 0.3096 0.1271 0.3484 -0.0150 -0.0314 0.0681  59  GLU A N   
483  C CA  . GLU A 59  ? 0.3486 0.1418 0.3661 0.0103  -0.0443 0.0808  59  GLU A CA  
484  C C   . GLU A 59  ? 0.3454 0.1710 0.3738 0.0152  -0.0402 0.0815  59  GLU A C   
485  O O   . GLU A 59  ? 0.3707 0.1531 0.4123 0.0268  -0.0426 0.0656  59  GLU A O   
486  C CB  . GLU A 59  ? 0.3945 0.2051 0.3765 -0.0084 -0.0414 0.0860  59  GLU A CB  
487  C CG  . GLU A 59  ? 0.4096 0.2576 0.3953 -0.0189 -0.0407 0.0839  59  GLU A CG  
488  C CD  . GLU A 59  ? 0.4700 0.2796 0.4242 -0.0333 -0.0417 0.0761  59  GLU A CD  
489  O OE1 . GLU A 59  ? 0.5734 0.4032 0.4334 -0.0070 -0.0395 -0.0139 59  GLU A OE1 
490  O OE2 . GLU A 59  ? 0.5413 0.2720 0.4897 -0.0722 -0.0359 0.0518  59  GLU A OE2 
491  N N   . GLU A 60  ? 0.3527 0.1829 0.3651 0.0085  -0.0528 0.0509  60  GLU A N   
492  C CA  . GLU A 60  ? 0.3799 0.2132 0.4281 -0.0011 -0.0643 0.0384  60  GLU A CA  
493  C C   . GLU A 60  ? 0.3417 0.2081 0.4402 -0.0001 -0.0653 0.0412  60  GLU A C   
494  O O   . GLU A 60  ? 0.3554 0.2477 0.4584 0.0311  -0.0755 0.0554  60  GLU A O   
495  C CB  . GLU A 60  ? 0.4364 0.2228 0.4858 -0.0189 -0.0881 -0.0126 60  GLU A CB  
496  C CG  . GLU A 60  ? 0.4896 0.2929 0.5286 0.0122  -0.1032 0.0036  60  GLU A CG  
497  C CD  . GLU A 60  ? 0.5914 0.3469 0.5936 -0.0378 -0.1332 -0.0011 60  GLU A CD  
498  O OE1 . GLU A 60  ? 0.6794 0.3717 0.6255 0.0251  -0.1552 0.0427  60  GLU A OE1 
499  O OE2 . GLU A 60  ? 0.7198 0.4545 0.6124 -0.0041 -0.1590 -0.0214 60  GLU A OE2 
500  N N   . LEU A 61  ? 0.3346 0.1823 0.4385 0.0229  -0.0545 0.0489  61  LEU A N   
501  C CA  . LEU A 61  ? 0.3368 0.1606 0.4344 -0.0058 -0.0251 0.0431  61  LEU A CA  
502  C C   . LEU A 61  ? 0.3517 0.1528 0.4668 0.0061  -0.0163 0.0340  61  LEU A C   
503  O O   . LEU A 61  ? 0.3414 0.1661 0.4826 0.0139  -0.0061 0.0063  61  LEU A O   
504  C CB  . LEU A 61  ? 0.3479 0.1829 0.4166 -0.0077 -0.0082 0.0554  61  LEU A CB  
505  C CG  . LEU A 61  ? 0.3382 0.1884 0.4202 -0.0276 -0.0066 0.0683  61  LEU A CG  
506  C CD1 . LEU A 61  ? 0.3498 0.1996 0.4088 -0.0669 0.0016  0.0762  61  LEU A CD1 
507  C CD2 . LEU A 61  ? 0.3521 0.2127 0.4498 -0.0145 -0.0028 0.0709  61  LEU A CD2 
508  N N   A LEU A 62  ? 0.3682 0.1122 0.4662 -0.0007 -0.0081 0.0384  62  LEU A N   
509  N N   B LEU A 62  ? 0.3736 0.1471 0.4716 0.0007  -0.0031 0.0445  62  LEU A N   
510  C CA  A LEU A 62  ? 0.3937 0.1046 0.4958 0.0092  -0.0110 0.0403  62  LEU A CA  
511  C CA  B LEU A 62  ? 0.4090 0.1464 0.5090 0.0052  -0.0055 0.0496  62  LEU A CA  
512  C C   A LEU A 62  ? 0.4136 0.1463 0.5156 0.0350  -0.0031 0.0499  62  LEU A C   
513  C C   B LEU A 62  ? 0.4254 0.1718 0.5201 0.0295  0.0008  0.0527  62  LEU A C   
514  O O   A LEU A 62  ? 0.4142 0.1271 0.5317 0.0008  0.0094  0.0285  62  LEU A O   
515  O O   B LEU A 62  ? 0.4207 0.1431 0.5354 -0.0031 0.0112  0.0336  62  LEU A O   
516  C CB  A LEU A 62  ? 0.4126 0.1272 0.4891 0.0038  -0.0106 0.0481  62  LEU A CB  
517  C CB  B LEU A 62  ? 0.4498 0.2086 0.5178 -0.0046 0.0064  0.0677  62  LEU A CB  
518  C CG  A LEU A 62  ? 0.4072 0.1330 0.4940 0.0060  -0.0168 0.0334  62  LEU A CG  
519  C CG  B LEU A 62  ? 0.4730 0.2849 0.5454 -0.0152 -0.0020 0.0668  62  LEU A CG  
520  C CD1 A LEU A 62  ? 0.4152 0.1532 0.4908 0.0198  -0.0167 0.0423  62  LEU A CD1 
521  C CD1 B LEU A 62  ? 0.4674 0.3329 0.5582 -0.0189 0.0091  0.0620  62  LEU A CD1 
522  C CD2 A LEU A 62  ? 0.4117 0.1961 0.5066 -0.0028 -0.0124 0.0341  62  LEU A CD2 
523  C CD2 B LEU A 62  ? 0.4863 0.2922 0.5540 0.0022  0.0010  0.0718  62  LEU A CD2 
524  N N   . PRO A 63  ? 0.4039 0.1618 0.5224 0.0606  -0.0081 0.0643  63  PRO A N   
525  C CA  . PRO A 63  ? 0.4404 0.2146 0.5755 0.1017  -0.0236 0.0382  63  PRO A CA  
526  C C   . PRO A 63  ? 0.4409 0.2382 0.6035 0.1212  -0.0278 0.0304  63  PRO A C   
527  O O   . PRO A 63  ? 0.5003 0.2832 0.6273 0.1777  -0.0500 0.0089  63  PRO A O   
528  C CB  . PRO A 63  ? 0.4846 0.3025 0.5661 0.0881  -0.0382 0.0644  63  PRO A CB  
529  C CG  . PRO A 63  ? 0.4918 0.2546 0.5867 0.0550  -0.0253 0.0500  63  PRO A CG  
530  C CD  . PRO A 63  ? 0.4690 0.2152 0.5370 0.0438  -0.0116 0.0563  63  PRO A CD  
531  N N   . LYS A 64  ? 0.4257 0.2816 0.6007 0.0741  -0.0237 0.0267  64  LYS A N   
532  C CA  . LYS A 64  ? 0.4434 0.2831 0.6039 0.0659  -0.0080 -0.0011 64  LYS A CA  
533  C C   . LYS A 64  ? 0.3738 0.2667 0.5937 0.0511  0.0000  -0.0025 64  LYS A C   
534  O O   . LYS A 64  ? 0.4144 0.2918 0.5880 0.0057  0.0149  -0.0362 64  LYS A O   
535  C CB  . LYS A 64  ? 0.5132 0.3291 0.6666 0.0207  -0.0013 -0.0119 64  LYS A CB  
536  C CG  . LYS A 64  ? 0.5928 0.3994 0.6820 0.0217  0.0108  -0.0143 64  LYS A CG  
537  C CD  . LYS A 64  ? 0.6529 0.4201 0.7129 -0.0268 0.0115  0.0113  64  LYS A CD  
538  C CE  . LYS A 64  ? 0.7223 0.4330 0.7322 -0.0378 0.0036  0.0074  64  LYS A CE  
539  N NZ  . LYS A 64  ? 0.7994 0.4621 0.7671 -0.0692 0.0132  0.0000  64  LYS A NZ  
540  N N   . GLY A 65  ? 0.3617 0.2358 0.5572 0.0568  0.0014  -0.0099 65  GLY A N   
541  C CA  . GLY A 65  ? 0.3456 0.2215 0.5639 0.0523  -0.0010 -0.0072 65  GLY A CA  
542  C C   . GLY A 65  ? 0.3391 0.2173 0.5491 0.0721  -0.0051 0.0085  65  GLY A C   
543  O O   . GLY A 65  ? 0.3774 0.2221 0.5899 0.0816  -0.0415 0.0184  65  GLY A O   
544  N N   . SER A 66  ? 0.3520 0.1831 0.5518 0.0292  0.0212  0.0227  66  SER A N   
545  C CA  . SER A 66  ? 0.3261 0.2032 0.5290 0.0506  0.0235  0.0116  66  SER A CA  
546  C C   . SER A 66  ? 0.3335 0.1143 0.5226 0.0236  0.0328  -0.0010 66  SER A C   
547  O O   . SER A 66  ? 0.3123 0.1661 0.5248 0.0449  0.0162  0.0379  66  SER A O   
548  C CB  . SER A 66  ? 0.3461 0.2318 0.5712 0.0191  0.0383  0.0072  66  SER A CB  
549  O OG  . SER A 66  ? 0.3534 0.1660 0.6166 0.0394  0.0352  -0.0073 66  SER A OG  
550  N N   . LYS A 67  ? 0.4184 0.1258 0.5218 0.0256  0.0238  0.0102  67  LYS A N   
551  C CA  . LYS A 67  ? 0.4389 0.0896 0.5916 0.0343  0.0157  0.0095  67  LYS A CA  
552  C C   . LYS A 67  ? 0.4221 0.1805 0.5393 0.0507  0.0320  0.0077  67  LYS A C   
553  O O   . LYS A 67  ? 0.4257 0.1574 0.5542 0.0320  0.0647  0.0332  67  LYS A O   
554  C CB  . LYS A 67  ? 0.4878 0.1478 0.6964 0.0167  0.0306  -0.0620 67  LYS A CB  
555  C CG  . LYS A 67  ? 0.5141 0.2222 0.7456 -0.0145 0.0424  -0.0146 67  LYS A CG  
556  C CD  . LYS A 67  ? 0.5504 0.2726 0.8023 -0.0149 0.0509  -0.0462 67  LYS A CD  
557  C CE  . LYS A 67  ? 0.5234 0.3650 0.8515 -0.0147 0.0642  -0.0345 67  LYS A CE  
558  N NZ  . LYS A 67  ? 0.5279 0.4268 0.8698 0.0124  0.0721  -0.0527 67  LYS A NZ  
559  N N   . GLU A 68  ? 0.3685 0.1814 0.5338 0.0868  0.0408  0.0107  68  GLU A N   
560  C CA  . GLU A 68  ? 0.4026 0.2476 0.5159 0.0649  0.0271  0.0338  68  GLU A CA  
561  C C   . GLU A 68  ? 0.3533 0.2364 0.5012 0.0718  0.0206  0.0222  68  GLU A C   
562  O O   . GLU A 68  ? 0.3809 0.2762 0.5331 0.0844  -0.0352 -0.0070 68  GLU A O   
563  C CB  . GLU A 68  ? 0.4480 0.3278 0.5584 0.0702  0.0418  0.0292  68  GLU A CB  
564  C CG  . GLU A 68  ? 0.5474 0.3661 0.6115 0.0714  0.0375  0.0616  68  GLU A CG  
565  C CD  . GLU A 68  ? 0.6630 0.4596 0.6850 0.0423  0.0521  0.0302  68  GLU A CD  
566  O OE1 . GLU A 68  ? 0.7756 0.5428 0.7105 0.0770  0.0890  0.0515  68  GLU A OE1 
567  O OE2 . GLU A 68  ? 0.7169 0.6037 0.8067 -0.0077 0.0779  0.0429  68  GLU A OE2 
568  N N   . GLU A 69  ? 0.3224 0.1664 0.4740 0.0717  0.0582  0.0327  69  GLU A N   
569  C CA  . GLU A 69  ? 0.3139 0.1618 0.4965 0.0763  0.0558  0.0264  69  GLU A CA  
570  C C   . GLU A 69  ? 0.2966 0.1176 0.4539 0.0383  0.0464  0.0323  69  GLU A C   
571  O O   . GLU A 69  ? 0.3207 0.1195 0.4819 0.0529  0.0531  0.0314  69  GLU A O   
572  C CB  . GLU A 69  ? 0.3273 0.1054 0.5423 0.0517  0.0567  0.0247  69  GLU A CB  
573  C CG  . GLU A 69  ? 0.3569 0.1678 0.5876 0.0251  0.0624  0.0323  69  GLU A CG  
574  C CD  . GLU A 69  ? 0.3773 0.2183 0.6147 -0.0277 0.0626  0.0439  69  GLU A CD  
575  O OE1 . GLU A 69  ? 0.3849 0.2078 0.6450 -0.0152 0.0167  0.0158  69  GLU A OE1 
576  O OE2 . GLU A 69  ? 0.3953 0.2354 0.6441 -0.0676 0.0597  0.0456  69  GLU A OE2 
577  N N   . GLN A 70  ? 0.3305 0.1496 0.4375 0.0736  0.0333  0.0282  70  GLN A N   
578  C CA  . GLN A 70  ? 0.3571 0.1568 0.4574 0.0621  0.0295  0.0316  70  GLN A CA  
579  C C   . GLN A 70  ? 0.3620 0.1309 0.4457 0.0493  0.0427  0.0470  70  GLN A C   
580  O O   . GLN A 70  ? 0.3476 0.1416 0.4541 0.0643  0.0601  0.0732  70  GLN A O   
581  C CB  . GLN A 70  ? 0.3864 0.1484 0.4540 0.0562  -0.0038 0.0190  70  GLN A CB  
582  C CG  . GLN A 70  ? 0.4081 0.2020 0.4683 0.0703  -0.0392 0.0354  70  GLN A CG  
583  C CD  . GLN A 70  ? 0.5087 0.1950 0.4978 0.0617  -0.0590 0.0363  70  GLN A CD  
584  O OE1 . GLN A 70  ? 0.5985 0.2075 0.5660 0.0626  -0.0693 0.0020  70  GLN A OE1 
585  N NE2 . GLN A 70  ? 0.5824 0.2605 0.5268 0.0391  -0.0489 0.0271  70  GLN A NE2 
586  N N   . ARG A 71  ? 0.3643 0.0875 0.4549 0.0362  0.0407  0.0471  71  ARG A N   
587  C CA  . ARG A 71  ? 0.3569 0.1840 0.4683 0.0429  0.0448  0.0360  71  ARG A CA  
588  C C   . ARG A 71  ? 0.3285 0.1698 0.4350 0.0292  0.0605  0.0175  71  ARG A C   
589  O O   . ARG A 71  ? 0.3308 0.1770 0.3987 0.0428  0.0315  0.0229  71  ARG A O   
590  C CB  . ARG A 71  ? 0.3970 0.2895 0.5147 0.0563  0.0322  -0.0315 71  ARG A CB  
591  C CG  . ARG A 71  ? 0.5057 0.3758 0.5616 0.0508  0.0094  0.0016  71  ARG A CG  
592  C CD  . ARG A 71  ? 0.5969 0.4612 0.5945 0.0168  -0.0026 -0.0063 71  ARG A CD  
593  N NE  . ARG A 71  ? 0.7048 0.5439 0.6735 0.0233  -0.0498 -0.0017 71  ARG A NE  
594  C CZ  . ARG A 71  ? 0.7847 0.5094 0.7901 -0.0238 -0.0501 -0.0239 71  ARG A CZ  
595  N NH1 . ARG A 71  ? 0.8016 0.5101 0.8153 -0.0218 -0.0377 0.0023  71  ARG A NH1 
596  N NH2 . ARG A 71  ? 0.8105 0.5095 0.8738 -0.0085 -0.0523 -0.0406 71  ARG A NH2 
597  N N   . ASP A 72  ? 0.3323 0.1782 0.4451 0.0144  0.0621  0.0286  72  ASP A N   
598  C CA  . ASP A 72  ? 0.3522 0.1754 0.4228 0.0091  0.0440  0.0511  72  ASP A CA  
599  C C   . ASP A 72  ? 0.2704 0.1142 0.3770 0.0123  0.0368  0.0559  72  ASP A C   
600  O O   . ASP A 72  ? 0.2829 0.1487 0.3751 0.0367  0.0205  0.0321  72  ASP A O   
601  C CB  . ASP A 72  ? 0.3897 0.2211 0.4830 -0.0173 0.0783  0.0285  72  ASP A CB  
602  C CG  . ASP A 72  ? 0.4728 0.3072 0.5316 -0.0155 0.0903  0.0054  72  ASP A CG  
603  O OD1 . ASP A 72  ? 0.5902 0.3719 0.6081 -0.0349 0.0645  -0.0424 72  ASP A OD1 
604  O OD2 . ASP A 72  ? 0.5102 0.4311 0.6436 -0.0071 0.1285  -0.0229 72  ASP A OD2 
605  N N   . TYR A 73  ? 0.2813 0.0943 0.3895 0.0039  0.0384  0.0345  73  TYR A N   
606  C CA  . TYR A 73  ? 0.2774 0.0916 0.3735 0.0151  0.0093  0.0157  73  TYR A CA  
607  C C   . TYR A 73  ? 0.2825 0.1000 0.3533 0.0239  0.0147  0.0160  73  TYR A C   
608  O O   . TYR A 73  ? 0.2764 0.0818 0.3424 0.0094  0.0230  0.0115  73  TYR A O   
609  C CB  . TYR A 73  ? 0.2568 0.1532 0.4235 0.0269  0.0071  0.0135  73  TYR A CB  
610  C CG  . TYR A 73  ? 0.2504 0.1357 0.4318 0.0099  -0.0046 0.0318  73  TYR A CG  
611  C CD1 . TYR A 73  ? 0.2425 0.1136 0.4590 0.0092  0.0039  0.0162  73  TYR A CD1 
612  C CD2 . TYR A 73  ? 0.2315 0.1229 0.4257 0.0099  -0.0061 0.0200  73  TYR A CD2 
613  C CE1 . TYR A 73  ? 0.2503 0.1351 0.4891 0.0000  -0.0084 0.0430  73  TYR A CE1 
614  C CE2 . TYR A 73  ? 0.2402 0.1294 0.4606 0.0133  -0.0049 0.0152  73  TYR A CE2 
615  C CZ  . TYR A 73  ? 0.2427 0.1188 0.4802 0.0070  -0.0041 0.0084  73  TYR A CZ  
616  O OH  . TYR A 73  ? 0.2505 0.1307 0.5291 0.0028  -0.0072 -0.0138 73  TYR A OH  
617  N N   . VAL A 74  ? 0.2842 0.0947 0.3576 0.0196  0.0152  0.0165  74  VAL A N   
618  C CA  . VAL A 74  ? 0.2973 0.1064 0.3525 0.0120  0.0122  0.0395  74  VAL A CA  
619  C C   . VAL A 74  ? 0.2868 0.1217 0.3212 -0.0035 0.0295  0.0204  74  VAL A C   
620  O O   . VAL A 74  ? 0.2977 0.1026 0.2861 0.0086  0.0143  0.0026  74  VAL A O   
621  C CB  . VAL A 74  ? 0.3152 0.1162 0.4064 0.0140  0.0054  0.0642  74  VAL A CB  
622  C CG1 . VAL A 74  ? 0.3628 0.1323 0.4747 -0.0056 0.0133  0.0384  74  VAL A CG1 
623  C CG2 . VAL A 74  ? 0.3199 0.1354 0.4034 -0.0148 -0.0039 0.0457  74  VAL A CG2 
624  N N   . PHE A 75  ? 0.2597 0.0861 0.3017 -0.0058 0.0193  0.0020  75  PHE A N   
625  C CA  . PHE A 75  ? 0.2779 0.0968 0.3010 0.0048  0.0189  -0.0042 75  PHE A CA  
626  C C   . PHE A 75  ? 0.2417 0.0855 0.2978 -0.0089 0.0132  0.0009  75  PHE A C   
627  O O   . PHE A 75  ? 0.2440 0.0992 0.2894 -0.0161 0.0070  0.0009  75  PHE A O   
628  C CB  . PHE A 75  ? 0.2878 0.1043 0.3275 0.0028  0.0251  0.0021  75  PHE A CB  
629  C CG  . PHE A 75  ? 0.3011 0.1263 0.3100 0.0163  0.0198  0.0000  75  PHE A CG  
630  C CD1 . PHE A 75  ? 0.3158 0.1429 0.3387 0.0160  0.0044  0.0008  75  PHE A CD1 
631  C CD2 . PHE A 75  ? 0.3196 0.1216 0.3557 -0.0006 0.0032  0.0049  75  PHE A CD2 
632  C CE1 . PHE A 75  ? 0.3271 0.2013 0.3670 -0.0020 -0.0178 -0.0091 75  PHE A CE1 
633  C CE2 . PHE A 75  ? 0.3462 0.1594 0.3622 0.0181  -0.0068 0.0006  75  PHE A CE2 
634  C CZ  . PHE A 75  ? 0.3348 0.2097 0.3540 0.0184  -0.0271 0.0089  75  PHE A CZ  
635  N N   . TYR A 76  ? 0.2518 0.0656 0.3105 -0.0084 0.0323  -0.0048 76  TYR A N   
636  C CA  . TYR A 76  ? 0.2704 0.0774 0.3054 0.0052  0.0098  -0.0114 76  TYR A CA  
637  C C   . TYR A 76  ? 0.2442 0.0611 0.3010 -0.0037 0.0025  -0.0009 76  TYR A C   
638  O O   . TYR A 76  ? 0.2663 0.0627 0.3191 0.0100  0.0222  -0.0011 76  TYR A O   
639  C CB  . TYR A 76  ? 0.2670 0.0929 0.2999 0.0032  0.0230  -0.0036 76  TYR A CB  
640  C CG  . TYR A 76  ? 0.2588 0.1252 0.2890 -0.0110 0.0169  -0.0029 76  TYR A CG  
641  C CD1 . TYR A 76  ? 0.2791 0.1106 0.2812 0.0234  0.0407  0.0224  76  TYR A CD1 
642  C CD2 . TYR A 76  ? 0.3014 0.0875 0.3069 -0.0266 0.0309  -0.0108 76  TYR A CD2 
643  C CE1 . TYR A 76  ? 0.3201 0.1837 0.2916 0.0130  0.0315  0.0215  76  TYR A CE1 
644  C CE2 . TYR A 76  ? 0.3132 0.1395 0.3138 -0.0146 0.0288  -0.0165 76  TYR A CE2 
645  C CZ  . TYR A 76  ? 0.3155 0.2142 0.3046 -0.0023 0.0336  0.0118  76  TYR A CZ  
646  O OH  . TYR A 76  ? 0.3680 0.2872 0.3128 0.0123  0.0319  0.0188  76  TYR A OH  
647  N N   . LEU A 77  ? 0.2602 0.0988 0.2769 0.0212  -0.0161 -0.0006 77  LEU A N   
648  C CA  . LEU A 77  ? 0.2597 0.0912 0.2726 0.0225  -0.0109 -0.0130 77  LEU A CA  
649  C C   . LEU A 77  ? 0.2817 0.1318 0.2485 -0.0006 0.0065  0.0056  77  LEU A C   
650  O O   . LEU A 77  ? 0.3129 0.1051 0.2750 -0.0141 0.0187  -0.0296 77  LEU A O   
651  C CB  . LEU A 77  ? 0.2633 0.1171 0.2823 0.0184  -0.0188 0.0010  77  LEU A CB  
652  C CG  . LEU A 77  ? 0.2726 0.1256 0.2810 0.0165  -0.0347 -0.0072 77  LEU A CG  
653  C CD1 . LEU A 77  ? 0.2766 0.1421 0.3172 0.0155  -0.0459 -0.0033 77  LEU A CD1 
654  C CD2 . LEU A 77  ? 0.2817 0.1336 0.2839 0.0037  -0.0092 -0.0036 77  LEU A CD2 
655  N N   . ALA A 78  ? 0.2783 0.0942 0.2699 -0.0122 0.0149  0.0126  78  ALA A N   
656  C CA  . ALA A 78  ? 0.2767 0.1226 0.2881 -0.0278 0.0106  0.0144  78  ALA A CA  
657  C C   . ALA A 78  ? 0.2535 0.1193 0.2772 -0.0373 0.0123  0.0144  78  ALA A C   
658  O O   . ALA A 78  ? 0.2697 0.1389 0.2807 -0.0298 0.0218  0.0110  78  ALA A O   
659  C CB  . ALA A 78  ? 0.2764 0.1093 0.2802 -0.0343 0.0275  0.0268  78  ALA A CB  
660  N N   . VAL A 79  ? 0.2465 0.1135 0.2842 -0.0035 0.0215  0.0234  79  VAL A N   
661  C CA  . VAL A 79  ? 0.2574 0.1010 0.2856 0.0201  0.0155  0.0025  79  VAL A CA  
662  C C   . VAL A 79  ? 0.2572 0.1129 0.2965 0.0068  0.0239  -0.0070 79  VAL A C   
663  O O   . VAL A 79  ? 0.2390 0.1001 0.3206 0.0081  0.0149  -0.0103 79  VAL A O   
664  C CB  . VAL A 79  ? 0.2825 0.1109 0.2898 0.0228  0.0199  0.0241  79  VAL A CB  
665  C CG1 . VAL A 79  ? 0.3009 0.1151 0.3120 0.0361  0.0225  0.0297  79  VAL A CG1 
666  C CG2 . VAL A 79  ? 0.3110 0.1524 0.2732 0.0296  0.0214  0.0125  79  VAL A CG2 
667  N N   . GLY A 80  ? 0.2639 0.0916 0.2798 -0.0013 0.0296  0.0056  80  GLY A N   
668  C CA  . GLY A 80  ? 0.2890 0.0799 0.3013 0.0123  0.0175  0.0009  80  GLY A CA  
669  C C   . GLY A 80  ? 0.2941 0.0877 0.2834 0.0006  0.0118  -0.0160 80  GLY A C   
670  O O   . GLY A 80  ? 0.3006 0.0715 0.2971 0.0028  0.0238  -0.0189 80  GLY A O   
671  N N   . ASN A 81  ? 0.2866 0.0854 0.2772 0.0013  0.0126  -0.0138 81  ASN A N   
672  C CA  . ASN A 81  ? 0.3026 0.1051 0.2769 -0.0035 0.0119  -0.0124 81  ASN A CA  
673  C C   . ASN A 81  ? 0.2885 0.1039 0.2804 -0.0191 0.0226  -0.0118 81  ASN A C   
674  O O   . ASN A 81  ? 0.2847 0.1197 0.3472 -0.0016 0.0216  -0.0115 81  ASN A O   
675  C CB  . ASN A 81  ? 0.3053 0.1058 0.2775 -0.0045 0.0109  -0.0130 81  ASN A CB  
676  C CG  . ASN A 81  ? 0.3064 0.1122 0.2703 -0.0167 0.0172  0.0071  81  ASN A CG  
677  O OD1 . ASN A 81  ? 0.3524 0.1617 0.2946 -0.0083 0.0274  -0.0236 81  ASN A OD1 
678  N ND2 . ASN A 81  ? 0.3173 0.1174 0.2951 0.0044  0.0128  -0.0072 81  ASN A ND2 
679  N N   . TYR A 82  ? 0.2700 0.0800 0.2754 0.0064  0.0316  -0.0122 82  TYR A N   
680  C CA  . TYR A 82  ? 0.2715 0.0751 0.2978 0.0017  0.0206  -0.0247 82  TYR A CA  
681  C C   . TYR A 82  ? 0.2658 0.0807 0.3186 0.0027  0.0154  -0.0135 82  TYR A C   
682  O O   . TYR A 82  ? 0.2832 0.1235 0.3317 -0.0054 0.0258  -0.0314 82  TYR A O   
683  C CB  . TYR A 82  ? 0.2700 0.0960 0.3012 -0.0092 0.0174  -0.0249 82  TYR A CB  
684  C CG  . TYR A 82  ? 0.2758 0.1213 0.3185 -0.0193 0.0164  -0.0333 82  TYR A CG  
685  C CD1 . TYR A 82  ? 0.2795 0.1237 0.3294 -0.0156 0.0211  -0.0048 82  TYR A CD1 
686  C CD2 . TYR A 82  ? 0.3088 0.2265 0.3502 0.0037  0.0192  -0.0033 82  TYR A CD2 
687  C CE1 . TYR A 82  ? 0.2869 0.1444 0.3543 -0.0257 0.0091  -0.0161 82  TYR A CE1 
688  C CE2 . TYR A 82  ? 0.3180 0.2464 0.3492 -0.0203 0.0141  0.0012  82  TYR A CE2 
689  C CZ  . TYR A 82  ? 0.3093 0.1825 0.3696 -0.0290 -0.0022 -0.0183 82  TYR A CZ  
690  O OH  . TYR A 82  ? 0.3185 0.2459 0.4355 -0.0254 -0.0239 -0.0189 82  TYR A OH  
691  N N   . ARG A 83  ? 0.2624 0.0704 0.3329 0.0095  0.0180  -0.0056 83  ARG A N   
692  C CA  . ARG A 83  ? 0.2912 0.0782 0.3428 0.0212  0.0129  0.0034  83  ARG A CA  
693  C C   . ARG A 83  ? 0.3206 0.1006 0.3274 0.0050  0.0149  0.0036  83  ARG A C   
694  O O   . ARG A 83  ? 0.3506 0.1285 0.3787 0.0363  -0.0055 -0.0189 83  ARG A O   
695  C CB  . ARG A 83  ? 0.2700 0.0872 0.3550 0.0202  0.0140  0.0051  83  ARG A CB  
696  C CG  . ARG A 83  ? 0.2750 0.0672 0.3545 0.0035  0.0133  0.0079  83  ARG A CG  
697  C CD  . ARG A 83  ? 0.2664 0.1429 0.3556 0.0148  0.0120  0.0262  83  ARG A CD  
698  N NE  . ARG A 83  ? 0.2849 0.1509 0.3784 0.0221  -0.0033 0.0423  83  ARG A NE  
699  C CZ  . ARG A 83  ? 0.3150 0.1530 0.4089 0.0238  0.0211  0.0189  83  ARG A CZ  
700  N NH1 . ARG A 83  ? 0.3284 0.1794 0.3716 0.0211  0.0302  -0.0431 83  ARG A NH1 
701  N NH2 . ARG A 83  ? 0.3241 0.1992 0.4555 0.0423  0.0349  0.0384  83  ARG A NH2 
702  N N   . LEU A 84  ? 0.3197 0.0981 0.3250 0.0033  0.0132  0.0008  84  LEU A N   
703  C CA  . LEU A 84  ? 0.3069 0.1427 0.3284 -0.0070 0.0343  -0.0201 84  LEU A CA  
704  C C   . LEU A 84  ? 0.2992 0.1457 0.3205 -0.0157 0.0384  -0.0295 84  LEU A C   
705  O O   . LEU A 84  ? 0.3320 0.1499 0.3453 -0.0436 0.0853  -0.0285 84  LEU A O   
706  C CB  . LEU A 84  ? 0.3080 0.1407 0.3403 -0.0074 0.0376  -0.0265 84  LEU A CB  
707  C CG  . LEU A 84  ? 0.3204 0.2034 0.3346 -0.0220 0.0357  -0.0415 84  LEU A CG  
708  C CD1 . LEU A 84  ? 0.3360 0.2355 0.3792 -0.0003 0.0383  -0.0372 84  LEU A CD1 
709  C CD2 . LEU A 84  ? 0.3685 0.2038 0.3721 -0.0232 0.0248  -0.0317 84  LEU A CD2 
710  N N   . LYS A 85  ? 0.2878 0.1654 0.3268 -0.0106 0.0360  -0.0598 85  LYS A N   
711  C CA  . LYS A 85  ? 0.3123 0.1461 0.3533 -0.0229 0.0360  -0.0457 85  LYS A CA  
712  C C   . LYS A 85  ? 0.3492 0.1894 0.3542 -0.0301 0.0426  -0.0330 85  LYS A C   
713  O O   . LYS A 85  ? 0.3445 0.2126 0.3800 -0.0069 0.0515  -0.0236 85  LYS A O   
714  C CB  . LYS A 85  ? 0.3150 0.2069 0.3852 -0.0232 0.0569  -0.0330 85  LYS A CB  
715  C CG  . LYS A 85  ? 0.3468 0.2277 0.4420 -0.0055 0.0567  -0.0154 85  LYS A CG  
716  C CD  . LYS A 85  ? 0.3764 0.3247 0.5085 0.0000  0.0522  -0.0286 85  LYS A CD  
717  C CE  . LYS A 85  ? 0.4396 0.3920 0.5474 -0.0081 0.0381  -0.0061 85  LYS A CE  
718  N NZ  . LYS A 85  ? 0.5070 0.4311 0.6035 -0.0256 0.0282  0.0063  85  LYS A NZ  
719  N N   . GLU A 86  ? 0.3618 0.1620 0.3289 -0.0235 0.0415  -0.0110 86  GLU A N   
720  C CA  . GLU A 86  ? 0.3982 0.1961 0.3311 -0.0266 0.0320  -0.0285 86  GLU A CA  
721  C C   . GLU A 86  ? 0.3468 0.1697 0.3229 -0.0172 0.0362  -0.0184 86  GLU A C   
722  O O   . GLU A 86  ? 0.3410 0.1740 0.3288 -0.0489 0.0308  -0.0072 86  GLU A O   
723  C CB  . GLU A 86  ? 0.4299 0.1901 0.3473 -0.0349 0.0293  -0.0065 86  GLU A CB  
724  C CG  . GLU A 86  ? 0.5130 0.2334 0.3843 -0.0604 0.0173  -0.0337 86  GLU A CG  
725  C CD  . GLU A 86  ? 0.6051 0.3192 0.4268 -0.0599 0.0311  -0.0270 86  GLU A CD  
726  O OE1 . GLU A 86  ? 0.6679 0.4046 0.4943 -0.0998 0.0879  0.0021  86  GLU A OE1 
727  O OE2 . GLU A 86  ? 0.7368 0.4643 0.4920 -0.0460 0.0084  -0.1389 86  GLU A OE2 
728  N N   . TYR A 87  ? 0.3341 0.1529 0.3465 0.0066  0.0520  -0.0195 87  TYR A N   
729  C CA  . TYR A 87  ? 0.3294 0.1693 0.3252 -0.0158 0.0377  -0.0211 87  TYR A CA  
730  C C   . TYR A 87  ? 0.3295 0.1715 0.3282 -0.0212 0.0584  0.0141  87  TYR A C   
731  O O   . TYR A 87  ? 0.3438 0.1295 0.3311 -0.0261 0.0637  0.0154  87  TYR A O   
732  C CB  . TYR A 87  ? 0.3119 0.1886 0.3306 0.0071  0.0437  -0.0267 87  TYR A CB  
733  C CG  . TYR A 87  ? 0.3178 0.2037 0.3369 0.0059  0.0146  -0.0369 87  TYR A CG  
734  C CD1 . TYR A 87  ? 0.3441 0.2140 0.3525 0.0368  0.0065  -0.0242 87  TYR A CD1 
735  C CD2 . TYR A 87  ? 0.3305 0.2060 0.3638 0.0008  0.0141  -0.0439 87  TYR A CD2 
736  C CE1 . TYR A 87  ? 0.3425 0.1951 0.3605 0.0021  -0.0100 -0.0372 87  TYR A CE1 
737  C CE2 . TYR A 87  ? 0.3337 0.2061 0.3948 0.0110  -0.0074 -0.0283 87  TYR A CE2 
738  C CZ  . TYR A 87  ? 0.3359 0.2165 0.3828 0.0264  -0.0145 -0.0395 87  TYR A CZ  
739  O OH  . TYR A 87  ? 0.3767 0.2148 0.4790 0.0699  -0.0332 -0.0691 87  TYR A OH  
740  N N   . GLU A 88  ? 0.3573 0.1807 0.3456 -0.0185 0.0472  0.0089  88  GLU A N   
741  C CA  . GLU A 88  ? 0.4124 0.1252 0.3730 -0.0082 0.0549  0.0078  88  GLU A CA  
742  C C   . GLU A 88  ? 0.3871 0.1108 0.3439 0.0074  0.0494  0.0228  88  GLU A C   
743  O O   . GLU A 88  ? 0.3679 0.1417 0.3471 0.0291  0.0343  0.0072  88  GLU A O   
744  C CB  . GLU A 88  ? 0.4907 0.2019 0.3944 0.0147  0.0521  0.0379  88  GLU A CB  
745  C CG  . GLU A 88  ? 0.5761 0.3375 0.4445 0.0426  0.0576  0.0469  88  GLU A CG  
746  C CD  . GLU A 88  ? 0.7082 0.4374 0.4686 0.0386  0.0684  0.0538  88  GLU A CD  
747  O OE1 . GLU A 88  ? 0.7976 0.4509 0.5494 0.0809  0.0810  0.0504  88  GLU A OE1 
748  O OE2 . GLU A 88  ? 0.8346 0.4771 0.5518 0.0468  0.0589  0.0696  88  GLU A OE2 
749  N N   . LYS A 89  ? 0.3711 0.1164 0.3117 0.0113  0.0330  -0.0091 89  LYS A N   
750  C CA  . LYS A 89  ? 0.3741 0.1584 0.3413 -0.0013 0.0211  0.0034  89  LYS A CA  
751  C C   . LYS A 89  ? 0.3263 0.1348 0.3318 -0.0145 0.0080  -0.0066 89  LYS A C   
752  O O   . LYS A 89  ? 0.3135 0.1527 0.3356 0.0115  -0.0005 0.0000  89  LYS A O   
753  C CB  . LYS A 89  ? 0.4096 0.1881 0.3714 -0.0211 0.0201  -0.0129 89  LYS A CB  
754  C CG  . LYS A 89  ? 0.4686 0.1989 0.4025 -0.0218 0.0197  -0.0134 89  LYS A CG  
755  C CD  . LYS A 89  ? 0.5207 0.2420 0.4313 -0.0525 0.0132  -0.0241 89  LYS A CD  
756  C CE  . LYS A 89  ? 0.5672 0.3095 0.4415 -0.0350 0.0193  -0.0183 89  LYS A CE  
757  N NZ  . LYS A 89  ? 0.6010 0.4019 0.4827 -0.0504 0.0208  -0.0337 89  LYS A NZ  
758  N N   . ALA A 90  ? 0.3289 0.1107 0.3202 -0.0274 0.0155  0.0030  90  ALA A N   
759  C CA  . ALA A 90  ? 0.3059 0.1266 0.3154 -0.0288 0.0260  0.0120  90  ALA A CA  
760  C C   . ALA A 90  ? 0.3077 0.1288 0.3050 -0.0166 0.0268  0.0079  90  ALA A C   
761  O O   . ALA A 90  ? 0.2965 0.1109 0.3081 -0.0099 0.0306  0.0066  90  ALA A O   
762  C CB  . ALA A 90  ? 0.3069 0.1046 0.3204 -0.0325 0.0222  0.0165  90  ALA A CB  
763  N N   . LEU A 91  ? 0.3430 0.1202 0.3335 -0.0130 0.0590  -0.0027 91  LEU A N   
764  C CA  . LEU A 91  ? 0.3483 0.1106 0.3420 -0.0120 0.0484  0.0030  91  LEU A CA  
765  C C   . LEU A 91  ? 0.3374 0.0908 0.3249 -0.0367 0.0365  0.0047  91  LEU A C   
766  O O   . LEU A 91  ? 0.3933 0.0963 0.3356 -0.0197 0.0409  -0.0043 91  LEU A O   
767  C CB  . LEU A 91  ? 0.3891 0.1361 0.3811 -0.0275 0.0708  0.0210  91  LEU A CB  
768  C CG  . LEU A 91  ? 0.4170 0.2078 0.4253 -0.0398 0.0681  -0.0140 91  LEU A CG  
769  C CD1 . LEU A 91  ? 0.4312 0.2708 0.4357 -0.0661 0.0629  -0.0298 91  LEU A CD1 
770  C CD2 . LEU A 91  ? 0.4300 0.2030 0.4480 -0.0405 0.0739  -0.0122 91  LEU A CD2 
771  N N   . LYS A 92  ? 0.3734 0.0552 0.3133 0.0048  0.0203  0.0064  92  LYS A N   
772  C CA  . LYS A 92  ? 0.3845 0.0658 0.3547 0.0278  0.0249  0.0357  92  LYS A CA  
773  C C   . LYS A 92  ? 0.3566 0.0687 0.3410 0.0024  0.0119  0.0496  92  LYS A C   
774  O O   . LYS A 92  ? 0.4036 0.0960 0.3759 0.0235  0.0179  0.0039  92  LYS A O   
775  C CB  . LYS A 92  ? 0.4292 0.1017 0.3814 0.0431  0.0266  0.0293  92  LYS A CB  
776  C CG  . LYS A 92  ? 0.4876 0.2056 0.4285 0.0346  0.0356  0.0270  92  LYS A CG  
777  C CD  . LYS A 92  ? 0.5587 0.3328 0.4597 0.0132  0.0210  0.0182  92  LYS A CD  
778  C CE  . LYS A 92  ? 0.6167 0.4056 0.4690 0.0063  0.0429  0.0378  92  LYS A CE  
779  N NZ  . LYS A 92  ? 0.6557 0.4443 0.5383 -0.0277 0.0178  0.0060  92  LYS A NZ  
780  N N   . TYR A 93  ? 0.3752 0.0738 0.3242 0.0202  0.0038  0.0575  93  TYR A N   
781  C CA  . TYR A 93  ? 0.3476 0.1106 0.3480 -0.0122 0.0113  0.0267  93  TYR A CA  
782  C C   . TYR A 93  ? 0.3161 0.0860 0.3612 -0.0090 0.0162  0.0107  93  TYR A C   
783  O O   . TYR A 93  ? 0.3214 0.1289 0.3892 0.0403  0.0122  -0.0095 93  TYR A O   
784  C CB  . TYR A 93  ? 0.3368 0.1144 0.3416 -0.0217 0.0034  0.0390  93  TYR A CB  
785  C CG  . TYR A 93  ? 0.3715 0.1199 0.3469 -0.0070 -0.0085 0.0213  93  TYR A CG  
786  C CD1 . TYR A 93  ? 0.3764 0.1493 0.3488 -0.0093 -0.0266 0.0200  93  TYR A CD1 
787  C CD2 . TYR A 93  ? 0.3792 0.1267 0.3507 -0.0118 -0.0050 0.0263  93  TYR A CD2 
788  C CE1 . TYR A 93  ? 0.3937 0.1381 0.3821 -0.0155 -0.0368 0.0184  93  TYR A CE1 
789  C CE2 . TYR A 93  ? 0.4246 0.1339 0.3451 -0.0178 -0.0175 0.0396  93  TYR A CE2 
790  C CZ  . TYR A 93  ? 0.4208 0.1511 0.3503 -0.0363 -0.0356 0.0082  93  TYR A CZ  
791  O OH  . TYR A 93  ? 0.4923 0.2646 0.3933 -0.0974 -0.0758 0.0177  93  TYR A OH  
792  N N   . VAL A 94  ? 0.3133 0.0692 0.3369 0.0000  0.0139  0.0100  94  VAL A N   
793  C CA  . VAL A 94  ? 0.3494 0.0955 0.3489 -0.0105 0.0077  0.0111  94  VAL A CA  
794  C C   . VAL A 94  ? 0.3595 0.0943 0.3526 0.0038  0.0039  -0.0028 94  VAL A C   
795  O O   . VAL A 94  ? 0.3749 0.1067 0.3823 0.0226  0.0158  -0.0153 94  VAL A O   
796  C CB  . VAL A 94  ? 0.3635 0.0983 0.3766 -0.0335 -0.0101 0.0220  94  VAL A CB  
797  C CG1 . VAL A 94  ? 0.3628 0.1014 0.3590 -0.0259 -0.0030 0.0106  94  VAL A CG1 
798  C CG2 . VAL A 94  ? 0.3932 0.0840 0.3950 -0.0148 -0.0110 0.0294  94  VAL A CG2 
799  N N   . ARG A 95  ? 0.3686 0.0768 0.3654 0.0421  0.0202  -0.0077 95  ARG A N   
800  C CA  . ARG A 95  ? 0.4042 0.0804 0.4221 0.0110  0.0226  0.0005  95  ARG A CA  
801  C C   . ARG A 95  ? 0.3984 0.0892 0.4216 0.0165  0.0090  -0.0108 95  ARG A C   
802  O O   . ARG A 95  ? 0.4345 0.1180 0.4342 0.0499  0.0030  -0.0333 95  ARG A O   
803  C CB  . ARG A 95  ? 0.4359 0.0792 0.4364 0.0419  0.0313  0.0201  95  ARG A CB  
804  C CG  . ARG A 95  ? 0.4575 0.1583 0.5003 0.0241  0.0381  -0.0072 95  ARG A CG  
805  C CD  . ARG A 95  ? 0.4957 0.2151 0.5489 0.0282  0.0630  0.0098  95  ARG A CD  
806  N NE  . ARG A 95  ? 0.5326 0.4022 0.6509 -0.0094 0.0520  -0.0107 95  ARG A NE  
807  C CZ  . ARG A 95  ? 0.5604 0.5120 0.6833 -0.0369 0.0803  -0.0033 95  ARG A CZ  
808  N NH1 . ARG A 95  ? 0.5999 0.5187 0.7237 0.0170  0.0709  0.0202  95  ARG A NH1 
809  N NH2 . ARG A 95  ? 0.5575 0.5512 0.7471 -0.0832 0.0676  -0.0516 95  ARG A NH2 
810  N N   . GLY A 96  ? 0.3764 0.1085 0.4220 0.0291  0.0052  -0.0127 96  GLY A N   
811  C CA  . GLY A 96  ? 0.3802 0.1165 0.4499 0.0377  0.0050  0.0138  96  GLY A CA  
812  C C   . GLY A 96  ? 0.3790 0.1538 0.4583 0.0539  0.0064  -0.0119 96  GLY A C   
813  O O   . GLY A 96  ? 0.4076 0.1754 0.5020 0.0796  0.0308  -0.0047 96  GLY A O   
814  N N   . LEU A 97  ? 0.3697 0.1163 0.4556 0.0337  0.0256  -0.0217 97  LEU A N   
815  C CA  . LEU A 97  ? 0.3692 0.1649 0.4677 0.0260  0.0290  -0.0302 97  LEU A CA  
816  C C   . LEU A 97  ? 0.3678 0.1716 0.4366 0.0025  0.0386  -0.0252 97  LEU A C   
817  O O   . LEU A 97  ? 0.4005 0.2002 0.4586 -0.0329 0.0622  -0.0490 97  LEU A O   
818  C CB  . LEU A 97  ? 0.3706 0.1629 0.4750 0.0231  0.0368  -0.0289 97  LEU A CB  
819  C CG  . LEU A 97  ? 0.4011 0.1908 0.4935 0.0231  0.0398  -0.0460 97  LEU A CG  
820  C CD1 . LEU A 97  ? 0.4116 0.2523 0.5281 -0.0408 0.0423  -0.0412 97  LEU A CD1 
821  C CD2 . LEU A 97  ? 0.4028 0.1445 0.5087 0.0029  0.0444  -0.0693 97  LEU A CD2 
822  N N   . LEU A 98  ? 0.3671 0.1490 0.4097 0.0026  0.0225  -0.0435 98  LEU A N   
823  C CA  . LEU A 98  ? 0.3635 0.1165 0.4255 0.0104  0.0232  -0.0388 98  LEU A CA  
824  C C   . LEU A 98  ? 0.3746 0.1309 0.4248 0.0222  0.0244  -0.0423 98  LEU A C   
825  O O   . LEU A 98  ? 0.4574 0.1106 0.4748 0.0339  0.0176  -0.0682 98  LEU A O   
826  C CB  . LEU A 98  ? 0.3536 0.1446 0.4260 0.0000  0.0185  -0.0257 98  LEU A CB  
827  C CG  . LEU A 98  ? 0.3418 0.1327 0.4170 -0.0007 0.0182  -0.0231 98  LEU A CG  
828  C CD1 . LEU A 98  ? 0.3669 0.1553 0.4277 0.0030  0.0234  -0.0269 98  LEU A CD1 
829  C CD2 . LEU A 98  ? 0.3337 0.1459 0.4314 -0.0028 0.0162  -0.0402 98  LEU A CD2 
830  N N   . GLN A 99  ? 0.3879 0.0930 0.4422 0.0262  0.0211  -0.0264 99  GLN A N   
831  C CA  . GLN A 99  ? 0.4427 0.1268 0.4725 0.0515  0.0262  -0.0049 99  GLN A CA  
832  C C   . GLN A 99  ? 0.4122 0.1283 0.4958 0.0515  0.0301  0.0015  99  GLN A C   
833  O O   . GLN A 99  ? 0.4977 0.1943 0.6162 0.1265  0.0510  -0.0677 99  GLN A O   
834  C CB  . GLN A 99  ? 0.5048 0.2135 0.4790 0.0679  0.0151  0.0131  99  GLN A CB  
835  C CG  . GLN A 99  ? 0.5748 0.2674 0.5078 0.0806  0.0236  0.0357  99  GLN A CG  
836  C CD  . GLN A 99  ? 0.7211 0.3270 0.5352 0.0581  0.0245  0.0137  99  GLN A CD  
837  O OE1 . GLN A 99  ? 0.8104 0.3512 0.6482 0.0506  0.0014  0.0477  99  GLN A OE1 
838  N NE2 . GLN A 99  ? 0.8007 0.2755 0.5249 0.0458  0.0287  -0.0008 99  GLN A NE2 
839  N N   . THR A 100 ? 0.3935 0.1592 0.4849 0.0473  0.0270  0.0192  100 THR A N   
840  C CA  . THR A 100 ? 0.4272 0.1836 0.5210 0.0723  0.0258  -0.0108 100 THR A CA  
841  C C   . THR A 100 ? 0.4050 0.1147 0.5155 0.0644  0.0345  -0.0211 100 THR A C   
842  O O   . THR A 100 ? 0.4044 0.2330 0.5742 0.1426  0.0676  0.0057  100 THR A O   
843  C CB  . THR A 100 ? 0.4646 0.3064 0.5743 0.0074  0.0074  -0.0431 100 THR A CB  
844  O OG1 . THR A 100 ? 0.5518 0.4102 0.6580 0.0040  0.0040  -0.0008 100 THR A OG1 
845  C CG2 . THR A 100 ? 0.5068 0.3546 0.5901 0.0130  0.0131  -0.0230 100 THR A CG2 
846  N N   . GLU A 101 ? 0.3646 0.2097 0.5074 0.0670  0.0283  -0.0396 101 GLU A N   
847  C CA  . GLU A 101 ? 0.4060 0.2165 0.5230 0.0502  0.0239  -0.0381 101 GLU A CA  
848  C C   . GLU A 101 ? 0.4015 0.2151 0.4756 0.0706  0.0098  -0.0448 101 GLU A C   
849  O O   . GLU A 101 ? 0.3884 0.1752 0.4562 0.0603  0.0431  -0.0371 101 GLU A O   
850  C CB  . GLU A 101 ? 0.4622 0.3114 0.5675 0.0225  0.0401  -0.0033 101 GLU A CB  
851  C CG  . GLU A 101 ? 0.5287 0.3647 0.6339 -0.0026 0.0144  0.0235  101 GLU A CG  
852  C CD  . GLU A 101 ? 0.5437 0.3801 0.7027 -0.0600 0.0118  0.0157  101 GLU A CD  
853  O OE1 . GLU A 101 ? 0.5407 0.3574 0.7344 -0.0935 -0.0139 0.0140  101 GLU A OE1 
854  O OE2 . GLU A 101 ? 0.5639 0.5128 0.7732 -0.0088 0.0171  0.0544  101 GLU A OE2 
855  N N   . PRO A 102 ? 0.4083 0.1787 0.4824 0.0826  -0.0215 -0.0337 102 PRO A N   
856  C CA  . PRO A 102 ? 0.4385 0.1746 0.5450 0.0437  -0.0287 -0.0253 102 PRO A CA  
857  C C   . PRO A 102 ? 0.4684 0.2158 0.5597 0.0322  -0.0592 -0.0284 102 PRO A C   
858  O O   . PRO A 102 ? 0.4726 0.2246 0.6428 0.0533  -0.1488 -0.0127 102 PRO A O   
859  C CB  . PRO A 102 ? 0.4534 0.1775 0.5547 0.0193  -0.0273 -0.0143 102 PRO A CB  
860  C CG  . PRO A 102 ? 0.4410 0.1911 0.5524 0.0627  -0.0115 -0.0285 102 PRO A CG  
861  C CD  . PRO A 102 ? 0.4143 0.1912 0.5313 0.0843  -0.0098 -0.0080 102 PRO A CD  
862  N N   . GLN A 103 ? 0.5403 0.2058 0.5381 0.0578  -0.0650 -0.0817 103 GLN A N   
863  C CA  . GLN A 103 ? 0.5697 0.3205 0.5311 0.0624  -0.0751 -0.0752 103 GLN A CA  
864  C C   . GLN A 103 ? 0.5730 0.3136 0.4602 0.0785  -0.0480 -0.0802 103 GLN A C   
865  O O   . GLN A 103 ? 0.6502 0.3089 0.4625 0.1496  -0.0628 -0.1015 103 GLN A O   
866  C CB  . GLN A 103 ? 0.6504 0.4223 0.5671 0.0454  -0.0905 -0.1001 103 GLN A CB  
867  C CG  . GLN A 103 ? 0.7293 0.4584 0.6090 0.0338  -0.1020 -0.1044 103 GLN A CG  
868  C CD  . GLN A 103 ? 0.7883 0.5876 0.6654 0.0194  -0.0971 -0.1129 103 GLN A CD  
869  O OE1 . GLN A 103 ? 0.9007 0.6523 0.6809 -0.0350 -0.0755 -0.1340 103 GLN A OE1 
870  N NE2 . GLN A 103 ? 0.8262 0.6813 0.7138 0.0178  -0.1262 -0.0873 103 GLN A NE2 
871  N N   . ASN A 104 ? 0.4625 0.2111 0.4501 0.0779  0.0042  -0.0608 104 ASN A N   
872  C CA  . ASN A 104 ? 0.4535 0.2364 0.4054 0.0341  0.0306  -0.0247 104 ASN A CA  
873  C C   . ASN A 104 ? 0.4316 0.2283 0.3847 0.0145  0.0328  -0.0162 104 ASN A C   
874  O O   . ASN A 104 ? 0.4033 0.2039 0.4138 0.0333  0.0480  0.0117  104 ASN A O   
875  C CB  . ASN A 104 ? 0.4283 0.2360 0.4224 0.0198  0.0290  -0.0203 104 ASN A CB  
876  C CG  . ASN A 104 ? 0.4045 0.2596 0.4248 -0.0113 0.0321  0.0287  104 ASN A CG  
877  O OD1 . ASN A 104 ? 0.4017 0.2427 0.4236 -0.0076 0.0401  0.0225  104 ASN A OD1 
878  N ND2 . ASN A 104 ? 0.4680 0.2687 0.4711 0.0060  0.0062  -0.0268 104 ASN A ND2 
879  N N   . ASN A 105 ? 0.4359 0.2102 0.3625 -0.0061 0.0384  -0.0240 105 ASN A N   
880  C CA  . ASN A 105 ? 0.4466 0.1680 0.3912 0.0224  0.0341  -0.0450 105 ASN A CA  
881  C C   . ASN A 105 ? 0.3927 0.1714 0.3241 0.0194  0.0405  -0.0419 105 ASN A C   
882  O O   . ASN A 105 ? 0.3760 0.2109 0.3727 0.0200  0.0449  -0.0327 105 ASN A O   
883  C CB  . ASN A 105 ? 0.5228 0.2401 0.4199 0.0322  0.0314  -0.0308 105 ASN A CB  
884  C CG  . ASN A 105 ? 0.6254 0.2616 0.5000 0.0029  0.0227  -0.0498 105 ASN A CG  
885  O OD1 . ASN A 105 ? 0.6756 0.3345 0.6255 -0.0052 0.0067  -0.0122 105 ASN A OD1 
886  N ND2 . ASN A 105 ? 0.6908 0.3198 0.5587 -0.0003 0.0424  -0.0343 105 ASN A ND2 
887  N N   . GLN A 106 ? 0.4114 0.2050 0.3601 -0.0025 0.0543  -0.0390 106 GLN A N   
888  C CA  . GLN A 106 ? 0.4090 0.1846 0.3717 -0.0147 0.0705  -0.0301 106 GLN A CA  
889  C C   . GLN A 106 ? 0.3669 0.1831 0.3579 -0.0258 0.0558  -0.0184 106 GLN A C   
890  O O   . GLN A 106 ? 0.3904 0.1462 0.3428 -0.0189 0.0507  -0.0389 106 GLN A O   
891  C CB  . GLN A 106 ? 0.4368 0.1925 0.3687 -0.0210 0.0980  0.0078  106 GLN A CB  
892  C CG  . GLN A 106 ? 0.4825 0.1952 0.3689 -0.0171 0.0925  0.0055  106 GLN A CG  
893  C CD  . GLN A 106 ? 0.5302 0.2123 0.3714 -0.0099 0.1082  0.0108  106 GLN A CD  
894  O OE1 . GLN A 106 ? 0.5473 0.2800 0.4450 0.0032  0.1171  0.0048  106 GLN A OE1 
895  N NE2 . GLN A 106 ? 0.5569 0.2230 0.4178 -0.0229 0.0789  0.0103  106 GLN A NE2 
896  N N   . ALA A 107 ? 0.3509 0.2195 0.3367 -0.0379 0.0514  -0.0097 107 ALA A N   
897  C CA  . ALA A 107 ? 0.3549 0.2158 0.3367 -0.0424 0.0329  -0.0150 107 ALA A CA  
898  C C   . ALA A 107 ? 0.3421 0.1802 0.3103 -0.0350 0.0296  -0.0207 107 ALA A C   
899  O O   . ALA A 107 ? 0.3243 0.1677 0.3304 -0.0256 0.0372  -0.0143 107 ALA A O   
900  C CB  . ALA A 107 ? 0.3431 0.2635 0.3491 -0.0528 0.0214  0.0030  107 ALA A CB  
901  N N   . LYS A 108 ? 0.3403 0.1635 0.3520 -0.0265 0.0283  -0.0402 108 LYS A N   
902  C CA  . LYS A 108 ? 0.3417 0.1772 0.3621 -0.0213 0.0278  -0.0484 108 LYS A CA  
903  C C   . LYS A 108 ? 0.3362 0.1880 0.3477 -0.0224 0.0221  -0.0308 108 LYS A C   
904  O O   . LYS A 108 ? 0.3419 0.2046 0.3755 -0.0526 0.0198  -0.0610 108 LYS A O   
905  C CB  . LYS A 108 ? 0.3789 0.2146 0.3882 -0.0243 0.0261  -0.0837 108 LYS A CB  
906  C CG  . LYS A 108 ? 0.4398 0.2509 0.4447 0.0058  0.0296  -0.0754 108 LYS A CG  
907  C CD  . LYS A 108 ? 0.5005 0.3040 0.5202 0.0125  -0.0023 -0.1137 108 LYS A CD  
908  C CE  . LYS A 108 ? 0.5575 0.3131 0.5557 -0.0019 -0.0050 -0.1380 108 LYS A CE  
909  N NZ  . LYS A 108 ? 0.5831 0.3478 0.5853 -0.0309 -0.0290 -0.1463 108 LYS A NZ  
910  N N   . GLU A 109 ? 0.3513 0.1942 0.3474 -0.0511 0.0267  -0.0318 109 GLU A N   
911  C CA  . GLU A 109 ? 0.3852 0.2295 0.3414 -0.0128 -0.0038 -0.0319 109 GLU A CA  
912  C C   . GLU A 109 ? 0.3594 0.2161 0.3338 -0.0083 -0.0053 -0.0296 109 GLU A C   
913  O O   . GLU A 109 ? 0.3494 0.1837 0.3743 -0.0417 0.0033  -0.0618 109 GLU A O   
914  C CB  . GLU A 109 ? 0.4470 0.2534 0.3623 0.0002  0.0015  -0.0148 109 GLU A CB  
915  C CG  . GLU A 109 ? 0.5242 0.2876 0.4122 -0.0019 -0.0153 -0.0350 109 GLU A CG  
916  C CD  . GLU A 109 ? 0.6460 0.3696 0.4492 -0.0352 -0.0017 -0.0355 109 GLU A CD  
917  O OE1 . GLU A 109 ? 0.7368 0.3778 0.5418 -0.0805 -0.0116 -0.0060 109 GLU A OE1 
918  O OE2 . GLU A 109 ? 0.7482 0.5092 0.5063 -0.0163 0.0120  -0.1273 109 GLU A OE2 
919  N N   . LEU A 110 ? 0.3393 0.1753 0.3188 -0.0050 0.0065  -0.0158 110 LEU A N   
920  C CA  . LEU A 110 ? 0.3256 0.1519 0.3198 -0.0087 0.0030  -0.0093 110 LEU A CA  
921  C C   . LEU A 110 ? 0.3282 0.1109 0.3361 -0.0105 0.0141  0.0137  110 LEU A C   
922  O O   . LEU A 110 ? 0.3058 0.1468 0.3435 -0.0444 0.0162  -0.0029 110 LEU A O   
923  C CB  . LEU A 110 ? 0.3355 0.1172 0.3391 -0.0040 -0.0046 0.0227  110 LEU A CB  
924  C CG  . LEU A 110 ? 0.3403 0.1232 0.3455 -0.0084 -0.0227 0.0176  110 LEU A CG  
925  C CD1 . LEU A 110 ? 0.3448 0.1478 0.3644 0.0058  -0.0322 0.0155  110 LEU A CD1 
926  C CD2 . LEU A 110 ? 0.3597 0.1153 0.3613 -0.0166 -0.0262 0.0106  110 LEU A CD2 
927  N N   . GLU A 111 ? 0.3015 0.1245 0.3502 0.0062  0.0250  0.0081  111 GLU A N   
928  C CA  . GLU A 111 ? 0.3089 0.1039 0.3749 -0.0204 0.0340  -0.0189 111 GLU A CA  
929  C C   . GLU A 111 ? 0.3153 0.1563 0.3822 -0.0020 0.0149  -0.0212 111 GLU A C   
930  O O   . GLU A 111 ? 0.3204 0.1534 0.3913 -0.0600 0.0360  -0.0224 111 GLU A O   
931  C CB  . GLU A 111 ? 0.3329 0.1273 0.3821 0.0080  0.0550  -0.0376 111 GLU A CB  
932  C CG  . GLU A 111 ? 0.3647 0.2053 0.4050 -0.0108 0.0516  -0.0126 111 GLU A CG  
933  C CD  . GLU A 111 ? 0.4731 0.2693 0.5207 0.0412  0.0323  -0.0122 111 GLU A CD  
934  O OE1 . GLU A 111 ? 0.5077 0.2987 0.6188 -0.0459 0.0214  -0.0581 111 GLU A OE1 
935  O OE2 . GLU A 111 ? 0.5552 0.3321 0.5715 0.0426  0.0006  0.0368  111 GLU A OE2 
936  N N   . ARG A 112 ? 0.3213 0.1692 0.4000 0.0054  0.0075  -0.0247 112 ARG A N   
937  C CA  . ARG A 112 ? 0.3435 0.1983 0.4305 -0.0115 -0.0068 -0.0235 112 ARG A CA  
938  C C   . ARG A 112 ? 0.3365 0.2076 0.4059 -0.0068 0.0030  -0.0133 112 ARG A C   
939  O O   . ARG A 112 ? 0.3289 0.2248 0.4074 -0.0359 -0.0077 -0.0204 112 ARG A O   
940  C CB  . ARG A 112 ? 0.4084 0.2845 0.4715 -0.0083 -0.0061 -0.0351 112 ARG A CB  
941  C CG  . ARG A 112 ? 0.4586 0.3727 0.5396 -0.0152 -0.0174 -0.0593 112 ARG A CG  
942  C CD  . ARG A 112 ? 0.5501 0.4468 0.5889 -0.0121 -0.0164 -0.0724 112 ARG A CD  
943  N NE  . ARG A 112 ? 0.6262 0.5085 0.6911 -0.0002 0.0004  -0.0864 112 ARG A NE  
944  C CZ  . ARG A 112 ? 0.6965 0.5580 0.7971 -0.0011 0.0093  -0.0740 112 ARG A CZ  
945  N NH1 . ARG A 112 ? 0.6985 0.6629 0.8613 -0.0048 0.0090  -0.0648 112 ARG A NH1 
946  N NH2 . ARG A 112 ? 0.7217 0.6369 0.8403 0.0503  0.0200  -0.0764 112 ARG A NH2 
947  N N   A LEU A 113 ? 0.3124 0.1981 0.3973 0.0051  -0.0017 -0.0062 113 LEU A N   
948  N N   B LEU A 113 ? 0.3225 0.2062 0.4071 -0.0026 -0.0003 -0.0026 113 LEU A N   
949  C CA  A LEU A 113 ? 0.3099 0.1861 0.3988 0.0023  -0.0025 0.0018  113 LEU A CA  
950  C CA  B LEU A 113 ? 0.3289 0.1939 0.4166 -0.0082 0.0000  0.0071  113 LEU A CA  
951  C C   A LEU A 113 ? 0.2909 0.1729 0.3863 0.0103  -0.0021 0.0084  113 LEU A C   
952  C C   B LEU A 113 ? 0.2958 0.1760 0.3957 0.0065  -0.0022 0.0117  113 LEU A C   
953  O O   A LEU A 113 ? 0.2992 0.1328 0.3891 0.0042  0.0114  0.0033  113 LEU A O   
954  O O   B LEU A 113 ? 0.3031 0.1338 0.3935 0.0006  0.0109  0.0058  113 LEU A O   
955  C CB  A LEU A 113 ? 0.2864 0.2178 0.4050 0.0165  -0.0037 0.0179  113 LEU A CB  
956  C CB  B LEU A 113 ? 0.3247 0.2420 0.4474 -0.0086 0.0039  0.0276  113 LEU A CB  
957  C CG  A LEU A 113 ? 0.3198 0.2427 0.4067 0.0251  -0.0024 0.0006  113 LEU A CG  
958  C CG  B LEU A 113 ? 0.3854 0.2700 0.4793 -0.0092 -0.0012 0.0341  113 LEU A CG  
959  C CD1 A LEU A 113 ? 0.3280 0.2482 0.4180 0.0322  -0.0066 -0.0007 113 LEU A CD1 
960  C CD1 B LEU A 113 ? 0.4089 0.2996 0.4770 -0.0099 -0.0196 0.0367  113 LEU A CD1 
961  C CD2 A LEU A 113 ? 0.3393 0.2335 0.4081 0.0328  -0.0287 0.0098  113 LEU A CD2 
962  C CD2 B LEU A 113 ? 0.4081 0.2867 0.4866 0.0119  0.0063  0.0280  113 LEU A CD2 
963  N N   . ILE A 114 ? 0.2637 0.1449 0.3746 0.0081  0.0022  -0.0033 114 ILE A N   
964  C CA  . ILE A 114 ? 0.2709 0.1250 0.3598 0.0030  0.0026  -0.0257 114 ILE A CA  
965  C C   . ILE A 114 ? 0.3112 0.1287 0.3490 -0.0199 0.0100  -0.0257 114 ILE A C   
966  O O   . ILE A 114 ? 0.3008 0.1349 0.3584 -0.0069 0.0034  -0.0198 114 ILE A O   
967  C CB  . ILE A 114 ? 0.2690 0.1452 0.3599 0.0095  0.0110  -0.0345 114 ILE A CB  
968  C CG1 . ILE A 114 ? 0.2722 0.1453 0.3611 -0.0022 0.0023  -0.0435 114 ILE A CG1 
969  C CG2 . ILE A 114 ? 0.3122 0.1960 0.3642 0.0092  0.0086  -0.0355 114 ILE A CG2 
970  C CD1 . ILE A 114 ? 0.2699 0.1228 0.3557 -0.0206 -0.0047 -0.0542 114 ILE A CD1 
971  N N   . ASP A 115 ? 0.3186 0.1401 0.3719 -0.0243 0.0197  -0.0478 115 ASP A N   
972  C CA  . ASP A 115 ? 0.3471 0.1493 0.4125 -0.0121 0.0481  -0.0290 115 ASP A CA  
973  C C   . ASP A 115 ? 0.3485 0.1537 0.4187 -0.0164 0.0249  -0.0441 115 ASP A C   
974  O O   . ASP A 115 ? 0.3527 0.1566 0.4238 -0.0041 0.0264  -0.0763 115 ASP A O   
975  C CB  . ASP A 115 ? 0.4143 0.1665 0.4504 0.0062  0.0674  -0.0399 115 ASP A CB  
976  C CG  . ASP A 115 ? 0.4668 0.2755 0.5099 -0.0130 0.0714  0.0033  115 ASP A CG  
977  O OD1 . ASP A 115 ? 0.5699 0.2783 0.5557 0.0255  0.0756  0.0861  115 ASP A OD1 
978  O OD2 . ASP A 115 ? 0.4792 0.3957 0.5556 -0.0373 0.0753  0.0293  115 ASP A OD2 
979  N N   . LYS A 116 ? 0.3197 0.1778 0.4200 -0.0241 0.0372  -0.0314 116 LYS A N   
980  C CA  . LYS A 116 ? 0.3178 0.2073 0.4379 -0.0072 0.0231  -0.0242 116 LYS A CA  
981  C C   . LYS A 116 ? 0.3252 0.1974 0.4109 -0.0239 0.0371  -0.0042 116 LYS A C   
982  O O   . LYS A 116 ? 0.3162 0.2202 0.4287 -0.0020 0.0338  -0.0248 116 LYS A O   
983  C CB  . LYS A 116 ? 0.3698 0.2954 0.4855 0.0452  0.0368  -0.0091 116 LYS A CB  
984  C CG  . LYS A 116 ? 0.4348 0.4209 0.5180 0.0327  0.0125  -0.0268 116 LYS A CG  
985  C CD  . LYS A 116 ? 0.5359 0.5137 0.5529 0.0390  0.0177  0.0004  116 LYS A CD  
986  C CE  . LYS A 116 ? 0.6010 0.5411 0.5931 0.0553  0.0122  0.0174  116 LYS A CE  
987  N NZ  . LYS A 116 ? 0.6609 0.6045 0.6187 0.0257  0.0238  0.0282  116 LYS A NZ  
988  N N   . ALA A 117 ? 0.3062 0.1708 0.3740 -0.0182 0.0518  -0.0264 117 ALA A N   
989  C CA  . ALA A 117 ? 0.3172 0.1410 0.4152 -0.0146 0.0570  -0.0387 117 ALA A CA  
990  C C   . ALA A 117 ? 0.3150 0.1999 0.4202 -0.0154 0.0365  -0.0557 117 ALA A C   
991  O O   . ALA A 117 ? 0.2834 0.1909 0.4638 0.0167  0.0192  -0.0383 117 ALA A O   
992  C CB  . ALA A 117 ? 0.3369 0.1491 0.4389 -0.0258 0.0773  -0.0316 117 ALA A CB  
993  N N   . MET A 118 ? 0.3126 0.2041 0.4174 -0.0335 0.0111  -0.0476 118 MET A N   
994  C CA  . MET A 118 ? 0.3582 0.2421 0.4345 0.0120  0.0329  -0.0340 118 MET A CA  
995  C C   . MET A 118 ? 0.3437 0.2259 0.4117 0.0257  0.0263  -0.0025 118 MET A C   
996  O O   . MET A 118 ? 0.3819 0.3664 0.4032 0.0499  0.0318  0.0064  118 MET A O   
997  C CB  . MET A 118 ? 0.3559 0.3213 0.5426 0.0449  0.0199  -0.0061 118 MET A CB  
998  C CG  . MET A 118 ? 0.4095 0.3140 0.6393 -0.0083 -0.0071 -0.0278 118 MET A CG  
999  S SD  . MET A 118 ? 0.4935 0.3410 0.8851 0.0932  -0.0750 0.0767  118 MET A SD  
1000 C CE  . MET A 118 ? 0.5362 0.4258 0.8565 0.0152  -0.0143 0.0501  118 MET A CE  
1001 N N   . LYS A 119 ? 0.3163 0.1942 0.4252 0.0282  0.0283  0.0231  119 LYS A N   
1002 C CA  . LYS A 119 ? 0.3080 0.2199 0.4697 0.0204  0.0232  0.0293  119 LYS A CA  
1003 C C   . LYS A 119 ? 0.2784 0.2081 0.4787 0.0323  0.0262  0.0059  119 LYS A C   
1004 O O   . LYS A 119 ? 0.2827 0.2352 0.5405 0.0119  0.0211  0.0257  119 LYS A O   
1005 C CB  . LYS A 119 ? 0.3224 0.1716 0.5201 -0.0278 0.0379  0.0309  119 LYS A CB  
1006 C CG  . LYS A 119 ? 0.3359 0.1614 0.5598 -0.0407 0.0180  0.0343  119 LYS A CG  
1007 C CD  . LYS A 119 ? 0.4029 0.1971 0.6016 -0.1020 0.0035  -0.0015 119 LYS A CD  
1008 C CE  . LYS A 119 ? 0.4666 0.3307 0.6368 -0.0867 0.0020  0.0571  119 LYS A CE  
1009 N NZ  . LYS A 119 ? 0.5238 0.4402 0.6562 -0.0662 -0.0062 0.0322  119 LYS A NZ  
1010 N N   . LYS A 120 ? 0.2932 0.2258 0.4590 0.0246  0.0176  -0.0101 120 LYS A N   
1011 C CA  . LYS A 120 ? 0.2884 0.2030 0.4624 0.0264  0.0115  -0.0404 120 LYS A CA  
1012 C C   . LYS A 120 ? 0.2908 0.1911 0.4626 0.0282  0.0204  -0.0558 120 LYS A C   
1013 O O   . LYS A 120 ? 0.2909 0.1446 0.5033 0.0233  0.0280  -0.0423 120 LYS A O   
1014 C CB  . LYS A 120 ? 0.3336 0.2398 0.4931 0.0493  0.0047  -0.0568 120 LYS A CB  
1015 C CG  . LYS A 120 ? 0.3611 0.3009 0.5243 0.0506  -0.0226 -0.0677 120 LYS A CG  
1016 C CD  . LYS A 120 ? 0.4259 0.3764 0.5198 0.0570  -0.0142 -0.0827 120 LYS A CD  
1017 C CE  . LYS A 120 ? 0.4729 0.4495 0.5762 0.0287  -0.0270 -0.0649 120 LYS A CE  
1018 N NZ  . LYS A 120 ? 0.4687 0.4884 0.6029 0.0580  -0.0281 -0.0673 120 LYS A NZ  
1019 N N   . ASP A 121 ? 0.2911 0.1732 0.4310 0.0559  -0.0040 -0.0608 121 ASP A N   
1020 C CA  . ASP A 121 ? 0.3509 0.2513 0.4533 0.0369  -0.0112 -0.0718 121 ASP A CA  
1021 C C   . ASP A 121 ? 0.4126 0.3005 0.4563 0.0943  -0.0059 -0.0468 121 ASP A C   
1022 O O   . ASP A 121 ? 0.5154 0.2698 0.4522 0.0323  0.0197  -0.0709 121 ASP A O   
1023 C CB  . ASP A 121 ? 0.3518 0.2508 0.4922 0.0462  -0.0065 -0.0704 121 ASP A CB  
1024 C CG  . ASP A 121 ? 0.4052 0.2449 0.5000 0.0093  -0.0047 -0.0895 121 ASP A CG  
1025 O OD1 . ASP A 121 ? 0.4911 0.2810 0.4930 0.0321  0.0097  -0.0477 121 ASP A OD1 
1026 O OD2 . ASP A 121 ? 0.3822 0.3448 0.5226 0.0201  0.0157  -0.0760 121 ASP A OD2 
1027 N N   . GLY A 122 ? 0.4789 0.3543 0.4653 0.1144  -0.0071 -0.0357 122 GLY A N   
1028 C CA  . GLY A 122 ? 0.5355 0.2921 0.4558 0.1355  0.0156  -0.0444 122 GLY A CA  
1029 C C   . GLY A 122 ? 0.5151 0.2531 0.4184 0.0980  0.0403  -0.0141 122 GLY A C   
1030 O O   . GLY A 122 ? 0.5681 0.2738 0.3862 0.1369  0.0396  0.0076  122 GLY A O   
1031 N N   . LEU A 123 ? 0.4659 0.1442 0.4041 0.0756  0.0368  -0.0171 123 LEU A N   
1032 C CA  . LEU A 123 ? 0.3715 0.1206 0.3622 0.0237  0.0227  -0.0071 123 LEU A CA  
1033 C C   . LEU A 123 ? 0.3709 0.1002 0.3821 -0.0160 -0.0039 0.0182  123 LEU A C   
1034 O O   . LEU A 123 ? 0.4145 0.1105 0.4740 -0.0428 -0.0548 -0.0073 123 LEU A O   
1035 C CB  . LEU A 123 ? 0.3672 0.1136 0.3720 0.0163  0.0369  0.0159  123 LEU A CB  
1036 C CG  . LEU A 123 ? 0.3577 0.1463 0.3811 0.0015  0.0512  0.0044  123 LEU A CG  
1037 C CD1 . LEU A 123 ? 0.3505 0.1687 0.3741 -0.0051 0.0391  -0.0020 123 LEU A CD1 
1038 C CD2 . LEU A 123 ? 0.3909 0.1865 0.3920 0.0153  0.0545  -0.0006 123 LEU A CD2 
1039 N N   . LEU A 124 ? 0.3808 0.0840 0.3895 -0.0350 -0.0311 0.0015  124 LEU A N   
1040 C CA  . LEU A 124 ? 0.3853 0.1244 0.4114 -0.0390 -0.0456 -0.0112 124 LEU A CA  
1041 C C   . LEU A 124 ? 0.3646 0.1161 0.4504 -0.0050 -0.0372 0.0161  124 LEU A C   
1042 O O   . LEU A 124 ? 0.3691 0.1383 0.5003 -0.0302 -0.0540 0.0312  124 LEU A O   
1043 C CB  . LEU A 124 ? 0.4368 0.1424 0.4132 -0.0646 -0.0657 -0.0097 124 LEU A CB  
1044 C CG  . LEU A 124 ? 0.4942 0.2065 0.4138 -0.0617 -0.0527 0.0064  124 LEU A CG  
1045 C CD1 . LEU A 124 ? 0.5363 0.2601 0.4307 -0.0278 -0.0616 0.0313  124 LEU A CD1 
1046 C CD2 . LEU A 124 ? 0.5457 0.2604 0.4043 -0.0390 -0.0429 0.0041  124 LEU A CD2 
1047 N N   . GLU A 125 ? 0.3538 0.1306 0.4633 0.0160  -0.0079 0.0023  125 GLU A N   
1048 C CA  . GLU A 125 ? 0.3919 0.1912 0.5019 -0.0006 0.0220  0.0008  125 GLU A CA  
1049 C C   . GLU A 125 ? 0.3912 0.2519 0.5849 -0.0260 0.0477  0.0490  125 GLU A C   
1050 O O   . GLU A 125 ? 0.3823 0.2687 0.6234 -0.0143 0.0397  0.0757  125 GLU A O   
1051 C CB  . GLU A 125 ? 0.4723 0.2923 0.5086 -0.0244 0.0476  0.0056  125 GLU A CB  
1052 C CG  . GLU A 125 ? 0.5331 0.3521 0.5331 0.0101  0.0351  -0.0033 125 GLU A CG  
1053 C CD  . GLU A 125 ? 0.6088 0.4448 0.5822 -0.0092 0.0335  -0.0030 125 GLU A CD  
1054 O OE1 . GLU A 125 ? 0.7332 0.6517 0.5993 0.0051  0.0323  0.0404  125 GLU A OE1 
1055 O OE2 . GLU A 125 ? 0.6510 0.3075 0.6055 0.0125  -0.0072 -0.0055 125 GLU A OE2 
1056 N N   . VAL A 126 ? 0.3629 0.2012 0.6270 -0.0596 0.0428  0.0667  126 VAL A N   
1057 C CA  . VAL A 126 ? 0.3953 0.1700 0.6983 -0.0456 0.0666  0.0410  126 VAL A CA  
1058 C C   . VAL A 126 ? 0.3687 0.1835 0.7208 -0.0389 0.0881  0.0016  126 VAL A C   
1059 O O   . VAL A 126 ? 0.3959 0.1772 0.7869 -0.0495 0.1424  -0.0414 126 VAL A O   
1060 C CB  . VAL A 126 ? 0.4645 0.1299 0.7149 -0.0095 0.0344  0.1365  126 VAL A CB  
1061 C CG1 . VAL A 126 ? 0.4777 0.2853 0.7880 -0.0595 0.0219  0.0761  126 VAL A CG1 
1062 C CG2 . VAL A 126 ? 0.5052 0.2909 0.7442 -0.0453 0.0232  0.0936  126 VAL A CG2 
1063 N N   . LEU A 127 ? 0.3604 0.1379 0.7239 -0.0820 0.0619  -0.0280 127 LEU A N   
1064 C CA  . LEU A 127 ? 0.3001 0.1422 0.6968 -0.0950 0.0442  -0.0740 127 LEU A CA  
1065 C C   . LEU A 127 ? 0.3284 0.1621 0.6959 -0.0644 0.0066  -0.0409 127 LEU A C   
1066 O O   . LEU A 127 ? 0.3234 0.1781 0.6936 -0.0360 -0.0201 -0.1049 127 LEU A O   
1067 C CB  . LEU A 127 ? 0.3245 0.2094 0.6973 -0.1089 0.0353  -0.0958 127 LEU A CB  
1068 C CG  . LEU A 127 ? 0.3248 0.2500 0.6935 -0.0914 0.0425  -0.1077 127 LEU A CG  
1069 C CD1 . LEU A 127 ? 0.3531 0.2754 0.7037 -0.0531 0.0357  -0.0891 127 LEU A CD1 
1070 C CD2 . LEU A 127 ? 0.4020 0.2718 0.7358 -0.0760 0.0414  -0.1217 127 LEU A CD2 
1071 N N   . PHE A 128 ? 0.3658 0.1782 0.6494 -0.0040 0.0149  0.0012  128 PHE A N   
1072 C CA  . PHE A 128 ? 0.3690 0.1527 0.6237 -0.0012 0.0149  0.0068  128 PHE A CA  
1073 C C   . PHE A 128 ? 0.4298 0.2077 0.6571 0.0034  0.0328  0.0458  128 PHE A C   
1074 O O   . PHE A 128 ? 0.4556 0.2194 0.7033 0.0497  0.0866  0.0889  128 PHE A O   
1075 C CB  . PHE A 128 ? 0.3874 0.1441 0.5694 0.0061  0.0008  0.0115  128 PHE A CB  
1076 C CG  . PHE A 128 ? 0.3948 0.1433 0.5093 -0.0024 -0.0322 0.0075  128 PHE A CG  
1077 C CD1 . PHE A 128 ? 0.3825 0.2443 0.4881 -0.0075 -0.0309 0.0099  128 PHE A CD1 
1078 C CD2 . PHE A 128 ? 0.3659 0.2313 0.4699 0.0138  -0.0336 -0.0120 128 PHE A CD2 
1079 C CE1 . PHE A 128 ? 0.3981 0.2836 0.4661 -0.0244 -0.0437 -0.0124 128 PHE A CE1 
1080 C CE2 . PHE A 128 ? 0.3858 0.3255 0.4525 0.0070  -0.0512 -0.0100 128 PHE A CE2 
1081 C CZ  . PHE A 128 ? 0.3835 0.3151 0.4434 -0.0184 -0.0541 -0.0042 128 PHE A CZ  
1082 N N   . GLN A 129 ? 0.4924 0.2908 0.6841 -0.0070 0.0022  0.1035  129 GLN A N   
1083 C CA  . GLN A 129 ? 0.5234 0.3996 0.7019 -0.0302 -0.0079 0.1502  129 GLN A CA  
1084 C C   . GLN A 129 ? 0.5471 0.4176 0.7139 -0.0344 -0.0622 0.1546  129 GLN A C   
1085 O O   . GLN A 129 ? 0.4678 0.3980 0.7055 -0.0252 -0.0763 0.1945  129 GLN A O   
1086 C CB  . GLN A 129 ? 0.5754 0.4912 0.7423 -0.0216 -0.0199 0.2065  129 GLN A CB  
1087 C CG  . GLN A 129 ? 0.6558 0.6123 0.8055 -0.0259 -0.0042 0.2275  129 GLN A CG  
1088 C CD  . GLN A 129 ? 0.7180 0.7710 0.8823 -0.0425 -0.0323 0.2470  129 GLN A CD  
1089 O OE1 . GLN A 129 ? 0.7015 0.8501 1.0092 -0.0133 -0.0109 0.2497  129 GLN A OE1 
1090 N NE2 . GLN A 129 ? 0.7847 0.8122 0.9285 -0.0554 -0.0213 0.3051  129 GLN A NE2 
1091 N N   . MET B 1   ? 0.4857 0.6189 0.6872 0.0518  0.0130  0.2594  1   MET B N   
1092 C CA  . MET B 1   ? 0.5121 0.6209 0.7092 0.0605  0.0302  0.2393  1   MET B CA  
1093 C C   . MET B 1   ? 0.4853 0.5727 0.6957 0.0946  0.0378  0.2417  1   MET B C   
1094 O O   . MET B 1   ? 0.5645 0.7045 0.7099 0.0801  -0.0128 0.2390  1   MET B O   
1095 C CB  . MET B 1   ? 0.5129 0.6661 0.7391 0.0471  0.0332  0.2046  1   MET B CB  
1096 C CG  . MET B 1   ? 0.5939 0.7169 0.7275 -0.0120 0.0294  0.1938  1   MET B CG  
1097 S SD  . MET B 1   ? 0.6161 0.6604 0.6972 -0.0736 0.0360  0.1976  1   MET B SD  
1098 C CE  . MET B 1   ? 0.6301 0.6188 0.6339 -0.0294 0.0460  0.1817  1   MET B CE  
1099 N N   . GLU B 2   ? 0.4807 0.6145 0.6865 0.1081  0.0777  0.2395  2   GLU B N   
1100 C CA  . GLU B 2   ? 0.4602 0.6830 0.7053 0.1779  0.0455  0.2275  2   GLU B CA  
1101 C C   . GLU B 2   ? 0.4375 0.7454 0.6680 0.2186  0.0411  0.2427  2   GLU B C   
1102 O O   . GLU B 2   ? 0.4431 0.6927 0.6429 0.2659  0.0727  0.3012  2   GLU B O   
1103 C CB  . GLU B 2   ? 0.5207 0.7357 0.7655 0.1492  0.0798  0.2242  2   GLU B CB  
1104 C CG  . GLU B 2   ? 0.6185 0.8004 0.8340 0.0909  0.0730  0.2188  2   GLU B CG  
1105 C CD  . GLU B 2   ? 0.6853 0.8820 0.8970 0.0976  0.1055  0.2117  2   GLU B CD  
1106 O OE1 . GLU B 2   ? 0.8063 0.9120 0.9330 0.0993  0.1026  0.2303  2   GLU B OE1 
1107 O OE2 . GLU B 2   ? 0.8052 0.9159 0.9373 0.0215  0.1236  0.2511  2   GLU B OE2 
1108 N N   . ALA B 3   ? 0.4814 0.8036 0.6873 0.2683  0.0104  0.2434  3   ALA B N   
1109 C CA  . ALA B 3   ? 0.5291 0.8981 0.6668 0.1997  -0.0236 0.2110  3   ALA B CA  
1110 C C   . ALA B 3   ? 0.4977 0.9035 0.6789 0.1433  -0.0214 0.1483  3   ALA B C   
1111 O O   . ALA B 3   ? 0.5075 1.0052 0.6910 0.1501  -0.0021 0.1681  3   ALA B O   
1112 C CB  . ALA B 3   ? 0.5637 0.9187 0.6623 0.2277  -0.0313 0.2204  3   ALA B CB  
1113 N N   . VAL B 4   ? 0.4396 0.9300 0.6241 0.0630  -0.0500 0.1028  4   VAL B N   
1114 C CA  . VAL B 4   ? 0.4360 0.8940 0.5684 0.0097  -0.0625 0.0703  4   VAL B CA  
1115 C C   . VAL B 4   ? 0.4348 0.7732 0.4850 -0.0135 -0.0578 0.0460  4   VAL B C   
1116 O O   . VAL B 4   ? 0.3974 0.7709 0.4894 -0.0727 -0.1001 -0.0082 4   VAL B O   
1117 C CB  . VAL B 4   ? 0.4837 0.9334 0.5971 -0.0080 -0.0803 0.0424  4   VAL B CB  
1118 C CG1 . VAL B 4   ? 0.5148 0.9395 0.6076 0.0041  -0.0687 0.0320  4   VAL B CG1 
1119 C CG2 . VAL B 4   ? 0.5011 0.9779 0.6363 -0.0010 -0.0993 0.0490  4   VAL B CG2 
1120 N N   . LEU B 5   ? 0.3905 0.6690 0.4251 0.0183  -0.0039 0.0864  5   LEU B N   
1121 C CA  . LEU B 5   ? 0.3684 0.4844 0.3823 0.0217  0.0046  0.0909  5   LEU B CA  
1122 C C   . LEU B 5   ? 0.3471 0.4894 0.3963 0.0550  0.0098  0.1144  5   LEU B C   
1123 O O   . LEU B 5   ? 0.3487 0.3832 0.3753 0.0609  0.0045  0.0687  5   LEU B O   
1124 C CB  . LEU B 5   ? 0.3690 0.3920 0.3666 0.0183  0.0279  0.0980  5   LEU B CB  
1125 C CG  . LEU B 5   ? 0.3676 0.2890 0.3413 0.0129  0.0153  0.0761  5   LEU B CG  
1126 C CD1 . LEU B 5   ? 0.3582 0.2650 0.3724 0.0166  0.0125  0.0578  5   LEU B CD1 
1127 C CD2 . LEU B 5   ? 0.3477 0.2569 0.3591 0.0451  0.0287  0.0732  5   LEU B CD2 
1128 N N   . ASN B 6   ? 0.3599 0.5067 0.4486 0.0908  0.0238  0.1329  6   ASN B N   
1129 C CA  . ASN B 6   ? 0.4039 0.5111 0.4647 0.0841  0.0213  0.1607  6   ASN B CA  
1130 C C   . ASN B 6   ? 0.4094 0.5654 0.4270 0.0322  0.0174  0.1334  6   ASN B C   
1131 O O   . ASN B 6   ? 0.3887 0.5734 0.4016 0.0560  0.0124  0.0851  6   ASN B O   
1132 C CB  . ASN B 6   ? 0.4535 0.5185 0.5425 0.1015  0.0250  0.1720  6   ASN B CB  
1133 C CG  . ASN B 6   ? 0.5487 0.5075 0.6015 0.0490  0.0182  0.1777  6   ASN B CG  
1134 O OD1 . ASN B 6   ? 0.6493 0.5416 0.6719 0.0251  -0.0161 0.1617  6   ASN B OD1 
1135 N ND2 . ASN B 6   ? 0.6134 0.5785 0.6231 0.0363  0.0047  0.1774  6   ASN B ND2 
1136 N N   . GLU B 7   ? 0.3842 0.6279 0.4366 0.0028  0.0115  0.1237  7   GLU B N   
1137 C CA  . GLU B 7   ? 0.4301 0.6685 0.4149 -0.0402 0.0229  0.1077  7   GLU B CA  
1138 C C   . GLU B 7   ? 0.3772 0.6324 0.3867 -0.0470 0.0281  0.0506  7   GLU B C   
1139 O O   . GLU B 7   ? 0.4093 0.5887 0.3443 -0.0482 0.0405  0.0164  7   GLU B O   
1140 C CB  . GLU B 7   ? 0.4828 0.7767 0.4643 -0.0474 -0.0024 0.0957  7   GLU B CB  
1141 C CG  . GLU B 7   ? 0.5760 0.8280 0.5601 -0.0268 -0.0275 0.0898  7   GLU B CG  
1142 C CD  . GLU B 7   ? 0.7106 0.8899 0.5979 -0.0339 -0.0400 0.1082  7   GLU B CD  
1143 O OE1 . GLU B 7   ? 0.7601 1.0005 0.6708 -0.0334 -0.0988 0.0503  7   GLU B OE1 
1144 O OE2 . GLU B 7   ? 0.7631 0.9011 0.6659 -0.0885 -0.0534 0.0938  7   GLU B OE2 
1145 N N   . LEU B 8   ? 0.3588 0.5271 0.3757 -0.0551 0.0030  0.0309  8   LEU B N   
1146 C CA  . LEU B 8   ? 0.4053 0.4831 0.3952 -0.0783 0.0110  0.0282  8   LEU B CA  
1147 C C   . LEU B 8   ? 0.3864 0.4100 0.3251 -0.0360 0.0069  -0.0104 8   LEU B C   
1148 O O   . LEU B 8   ? 0.4156 0.3760 0.3315 -0.0439 0.0372  -0.0524 8   LEU B O   
1149 C CB  . LEU B 8   ? 0.4428 0.5502 0.4428 -0.0802 0.0180  0.0529  8   LEU B CB  
1150 C CG  . LEU B 8   ? 0.4783 0.5416 0.4788 -0.0832 0.0018  0.0389  8   LEU B CG  
1151 C CD1 . LEU B 8   ? 0.5112 0.5140 0.5190 -0.0629 0.0002  0.0595  8   LEU B CD1 
1152 C CD2 . LEU B 8   ? 0.5091 0.5773 0.4889 -0.0564 0.0088  0.0608  8   LEU B CD2 
1153 N N   . VAL B 9   ? 0.3540 0.3389 0.3400 0.0052  0.0243  0.0067  9   VAL B N   
1154 C CA  . VAL B 9   ? 0.3583 0.3018 0.3192 0.0139  0.0164  0.0021  9   VAL B CA  
1155 C C   . VAL B 9   ? 0.3670 0.2940 0.3151 0.0273  0.0183  0.0165  9   VAL B C   
1156 O O   . VAL B 9   ? 0.3716 0.2233 0.3452 0.0274  0.0180  0.0261  9   VAL B O   
1157 C CB  . VAL B 9   ? 0.3579 0.3110 0.3557 0.0724  0.0222  -0.0156 9   VAL B CB  
1158 C CG1 . VAL B 9   ? 0.3528 0.2873 0.3429 0.0670  0.0163  -0.0220 9   VAL B CG1 
1159 C CG2 . VAL B 9   ? 0.3627 0.3292 0.3789 0.0750  0.0059  -0.0193 9   VAL B CG2 
1160 N N   . SER B 10  ? 0.3789 0.3024 0.3407 0.0360  0.0177  0.0397  10  SER B N   
1161 C CA  . SER B 10  ? 0.3971 0.2784 0.3375 0.0195  0.0158  0.0568  10  SER B CA  
1162 C C   . SER B 10  ? 0.3834 0.3021 0.3140 -0.0233 0.0311  0.0252  10  SER B C   
1163 O O   . SER B 10  ? 0.3832 0.3028 0.3525 -0.0401 0.0439  0.0082  10  SER B O   
1164 C CB  . SER B 10  ? 0.4185 0.3220 0.3876 0.0483  0.0077  0.0677  10  SER B CB  
1165 O OG  . SER B 10  ? 0.4687 0.3868 0.4664 0.0391  0.0159  0.0206  10  SER B OG  
1166 N N   . VAL B 11  ? 0.3652 0.2985 0.3172 -0.0285 0.0339  0.0081  11  VAL B N   
1167 C CA  . VAL B 11  ? 0.4008 0.3084 0.3324 -0.0424 0.0320  -0.0097 11  VAL B CA  
1168 C C   . VAL B 11  ? 0.3840 0.2958 0.3367 -0.0258 0.0555  -0.0194 11  VAL B C   
1169 O O   . VAL B 11  ? 0.3831 0.2428 0.3105 -0.0230 0.0695  -0.0105 11  VAL B O   
1170 C CB  . VAL B 11  ? 0.4247 0.3430 0.3610 -0.0606 0.0097  -0.0251 11  VAL B CB  
1171 C CG1 . VAL B 11  ? 0.4337 0.3458 0.3758 -0.0804 0.0206  -0.0415 11  VAL B CG1 
1172 C CG2 . VAL B 11  ? 0.4586 0.3611 0.3745 -0.0498 -0.0012 -0.0284 11  VAL B CG2 
1173 N N   . GLU B 12  ? 0.3857 0.2493 0.3556 -0.0222 0.0534  -0.0167 12  GLU B N   
1174 C CA  . GLU B 12  ? 0.3698 0.2509 0.3467 -0.0090 0.0674  0.0117  12  GLU B CA  
1175 C C   . GLU B 12  ? 0.3507 0.2034 0.2995 0.0070  0.0667  0.0240  12  GLU B C   
1176 O O   . GLU B 12  ? 0.3642 0.2013 0.3387 0.0132  0.0657  0.0332  12  GLU B O   
1177 C CB  . GLU B 12  ? 0.3886 0.3182 0.3564 0.0078  0.0678  0.0253  12  GLU B CB  
1178 C CG  . GLU B 12  ? 0.4057 0.4343 0.4082 0.0236  0.0428  0.0240  12  GLU B CG  
1179 C CD  . GLU B 12  ? 0.4189 0.4650 0.4516 0.0721  0.0337  0.0358  12  GLU B CD  
1180 O OE1 . GLU B 12  ? 0.4869 0.5395 0.4931 0.0480  0.0048  0.0778  12  GLU B OE1 
1181 O OE2 . GLU B 12  ? 0.4691 0.6087 0.5143 0.0549  -0.0362 0.0597  12  GLU B OE2 
1182 N N   . ASP B 13  ? 0.3448 0.1981 0.3128 0.0211  0.0538  0.0184  13  ASP B N   
1183 C CA  . ASP B 13  ? 0.3522 0.2036 0.3149 0.0180  0.0459  0.0053  13  ASP B CA  
1184 C C   . ASP B 13  ? 0.3364 0.2203 0.3048 0.0056  0.0420  0.0304  13  ASP B C   
1185 O O   . ASP B 13  ? 0.3481 0.1889 0.3362 0.0461  0.0723  0.0088  13  ASP B O   
1186 C CB  . ASP B 13  ? 0.3502 0.1980 0.3163 0.0383  0.0419  0.0348  13  ASP B CB  
1187 C CG  . ASP B 13  ? 0.3780 0.2172 0.3332 0.0353  0.0303  0.0217  13  ASP B CG  
1188 O OD1 . ASP B 13  ? 0.3827 0.2140 0.3524 -0.0006 0.0036  0.0138  13  ASP B OD1 
1189 O OD2 . ASP B 13  ? 0.3784 0.1992 0.3668 0.0227  0.0027  0.0056  13  ASP B OD2 
1190 N N   . LEU B 14  ? 0.3238 0.2188 0.3013 -0.0265 0.0409  0.0124  14  LEU B N   
1191 C CA  . LEU B 14  ? 0.3389 0.2131 0.2957 -0.0320 0.0291  0.0193  14  LEU B CA  
1192 C C   . LEU B 14  ? 0.3314 0.2327 0.2961 -0.0258 0.0348  0.0192  14  LEU B C   
1193 O O   . LEU B 14  ? 0.3342 0.1932 0.3234 -0.0211 0.0493  0.0270  14  LEU B O   
1194 C CB  . LEU B 14  ? 0.3447 0.2435 0.3000 -0.0227 0.0323  0.0127  14  LEU B CB  
1195 C CG  . LEU B 14  ? 0.4018 0.2719 0.3213 -0.0128 0.0280  -0.0070 14  LEU B CG  
1196 C CD1 . LEU B 14  ? 0.4506 0.2711 0.2920 -0.0128 0.0284  -0.0155 14  LEU B CD1 
1197 C CD2 . LEU B 14  ? 0.4417 0.2762 0.3675 -0.0090 0.0120  0.0006  14  LEU B CD2 
1198 N N   . LEU B 15  ? 0.3454 0.2213 0.3192 -0.0342 0.0498  0.0161  15  LEU B N   
1199 C CA  . LEU B 15  ? 0.3718 0.2162 0.3528 -0.0225 0.0455  0.0159  15  LEU B CA  
1200 C C   . LEU B 15  ? 0.3940 0.2087 0.3575 -0.0221 0.0343  0.0250  15  LEU B C   
1201 O O   . LEU B 15  ? 0.3956 0.1879 0.3719 -0.0050 0.0256  0.0554  15  LEU B O   
1202 C CB  . LEU B 15  ? 0.4093 0.2555 0.4007 -0.0559 0.0546  0.0189  15  LEU B CB  
1203 C CG  . LEU B 15  ? 0.4284 0.2766 0.4401 -0.0634 0.0431  0.0080  15  LEU B CG  
1204 C CD1 . LEU B 15  ? 0.4642 0.2501 0.4916 -0.0934 0.0350  0.0174  15  LEU B CD1 
1205 C CD2 . LEU B 15  ? 0.4563 0.3241 0.4681 -0.0733 0.0135  -0.0024 15  LEU B CD2 
1206 N N   . LYS B 16  ? 0.3852 0.1854 0.3518 -0.0054 0.0331  0.0403  16  LYS B N   
1207 C CA  . LYS B 16  ? 0.4040 0.1852 0.3514 0.0040  0.0340  0.0136  16  LYS B CA  
1208 C C   . LYS B 16  ? 0.3560 0.1757 0.3632 0.0236  0.0295  0.0218  16  LYS B C   
1209 O O   . LYS B 16  ? 0.3493 0.1830 0.3764 0.0242  0.0241  0.0322  16  LYS B O   
1210 C CB  . LYS B 16  ? 0.4249 0.1088 0.3807 -0.0201 0.0379  0.0069  16  LYS B CB  
1211 C CG  . LYS B 16  ? 0.4468 0.2545 0.4037 -0.0316 0.0539  0.0169  16  LYS B CG  
1212 C CD  . LYS B 16  ? 0.4936 0.2521 0.4256 -0.0191 0.0669  -0.0058 16  LYS B CD  
1213 C CE  . LYS B 16  ? 0.5129 0.3266 0.4604 -0.0409 0.0799  0.0015  16  LYS B CE  
1214 N NZ  . LYS B 16  ? 0.5697 0.3815 0.5088 -0.0163 0.0881  -0.0166 16  LYS B NZ  
1215 N N   . PHE B 17  ? 0.3495 0.1173 0.3509 0.0187  0.0435  0.0080  17  PHE B N   
1216 C CA  . PHE B 17  ? 0.3441 0.1575 0.3549 0.0399  0.0430  0.0223  17  PHE B CA  
1217 C C   . PHE B 17  ? 0.3448 0.1713 0.3401 0.0131  0.0485  0.0230  17  PHE B C   
1218 O O   . PHE B 17  ? 0.3516 0.1552 0.3748 0.0179  0.0659  0.0462  17  PHE B O   
1219 C CB  . PHE B 17  ? 0.3325 0.1455 0.3561 0.0382  0.0485  0.0128  17  PHE B CB  
1220 C CG  . PHE B 17  ? 0.3487 0.1486 0.3557 0.0470  0.0622  0.0148  17  PHE B CG  
1221 C CD1 . PHE B 17  ? 0.3654 0.1748 0.3520 0.0298  0.0574  0.0357  17  PHE B CD1 
1222 C CD2 . PHE B 17  ? 0.3768 0.1829 0.3694 0.0206  0.0586  0.0289  17  PHE B CD2 
1223 C CE1 . PHE B 17  ? 0.4066 0.1016 0.3854 -0.0002 0.0627  0.0351  17  PHE B CE1 
1224 C CE2 . PHE B 17  ? 0.4112 0.2022 0.3854 0.0165  0.0591  0.0471  17  PHE B CE2 
1225 C CZ  . PHE B 17  ? 0.4107 0.1572 0.3681 0.0195  0.0655  0.0380  17  PHE B CZ  
1226 N N   . GLU B 18  ? 0.3475 0.1775 0.3381 0.0027  0.0445  0.0093  18  GLU B N   
1227 C CA  . GLU B 18  ? 0.3987 0.1825 0.3735 -0.0012 0.0515  0.0163  18  GLU B CA  
1228 C C   . GLU B 18  ? 0.3898 0.1538 0.3746 -0.0047 0.0589  -0.0049 18  GLU B C   
1229 O O   . GLU B 18  ? 0.4185 0.1574 0.3693 -0.0007 0.0667  -0.0133 18  GLU B O   
1230 C CB  . GLU B 18  ? 0.4108 0.2295 0.4383 -0.0310 0.0607  0.0060  18  GLU B CB  
1231 C CG  . GLU B 18  ? 0.4970 0.3384 0.4975 -0.0278 0.0566  0.0351  18  GLU B CG  
1232 C CD  . GLU B 18  ? 0.5526 0.4323 0.6233 -0.0776 0.0380  0.0119  18  GLU B CD  
1233 O OE1 . GLU B 18  ? 0.6162 0.4035 0.7150 -0.1174 -0.0088 -0.0137 18  GLU B OE1 
1234 O OE2 . GLU B 18  ? 0.5930 0.5697 0.6732 -0.0586 0.0625  0.0758  18  GLU B OE2 
1235 N N   . LYS B 19  ? 0.4038 0.1755 0.3698 0.0207  0.0627  0.0034  19  LYS B N   
1236 C CA  . LYS B 19  ? 0.3913 0.1872 0.4270 -0.0012 0.0497  0.0306  19  LYS B CA  
1237 C C   . LYS B 19  ? 0.3827 0.2157 0.4149 0.0000  0.0466  0.0253  19  LYS B C   
1238 O O   . LYS B 19  ? 0.3820 0.2087 0.4400 -0.0192 0.0927  0.0534  19  LYS B O   
1239 C CB  . LYS B 19  ? 0.4416 0.2548 0.4570 -0.0047 0.0354  0.0382  19  LYS B CB  
1240 C CG  . LYS B 19  ? 0.4783 0.2875 0.5104 -0.0287 0.0313  0.0440  19  LYS B CG  
1241 C CD  . LYS B 19  ? 0.5830 0.4046 0.5209 -0.0108 0.0156  0.0466  19  LYS B CD  
1242 C CE  . LYS B 19  ? 0.6300 0.4934 0.5717 0.0010  0.0099  0.0579  19  LYS B CE  
1243 N NZ  . LYS B 19  ? 0.7125 0.5592 0.6113 -0.0012 -0.0026 0.0845  19  LYS B NZ  
1244 N N   . LYS B 20  ? 0.3467 0.1980 0.4065 0.0012  0.0279  0.0188  20  LYS B N   
1245 C CA  . LYS B 20  ? 0.3312 0.1721 0.4304 0.0246  0.0333  0.0217  20  LYS B CA  
1246 C C   . LYS B 20  ? 0.3327 0.1834 0.4513 0.0244  0.0319  0.0342  20  LYS B C   
1247 O O   . LYS B 20  ? 0.3339 0.1877 0.4556 0.0212  0.0223  0.0210  20  LYS B O   
1248 C CB  . LYS B 20  ? 0.3582 0.1909 0.4257 0.0133  0.0302  -0.0085 20  LYS B CB  
1249 C CG  . LYS B 20  ? 0.4024 0.1977 0.4206 -0.0039 0.0349  -0.0364 20  LYS B CG  
1250 C CD  . LYS B 20  ? 0.4668 0.2152 0.4755 -0.0156 0.0347  -0.0566 20  LYS B CD  
1251 C CE  . LYS B 20  ? 0.5267 0.2342 0.5184 -0.0390 0.0218  -0.0230 20  LYS B CE  
1252 N NZ  . LYS B 20  ? 0.5577 0.2724 0.5371 -0.0128 -0.0003 -0.0417 20  LYS B NZ  
1253 N N   . PHE B 21  ? 0.3045 0.1962 0.4366 0.0234  0.0407  0.0360  21  PHE B N   
1254 C CA  . PHE B 21  ? 0.3254 0.2211 0.4438 0.0280  0.0412  0.0126  21  PHE B CA  
1255 C C   . PHE B 21  ? 0.3329 0.2321 0.4596 0.0286  0.0608  0.0074  21  PHE B C   
1256 O O   . PHE B 21  ? 0.3312 0.2212 0.4513 0.0130  0.0615  -0.0149 21  PHE B O   
1257 C CB  . PHE B 21  ? 0.3217 0.2781 0.4198 0.0406  0.0463  0.0242  21  PHE B CB  
1258 C CG  . PHE B 21  ? 0.3719 0.3370 0.4130 0.0319  0.0408  0.0219  21  PHE B CG  
1259 C CD1 . PHE B 21  ? 0.3904 0.3855 0.3766 0.0651  0.0417  0.0274  21  PHE B CD1 
1260 C CD2 . PHE B 21  ? 0.4265 0.3760 0.4114 0.0162  0.0202  0.0202  21  PHE B CD2 
1261 C CE1 . PHE B 21  ? 0.4039 0.4396 0.3911 0.0600  0.0542  0.0356  21  PHE B CE1 
1262 C CE2 . PHE B 21  ? 0.4250 0.3796 0.4319 0.0163  0.0344  0.0608  21  PHE B CE2 
1263 C CZ  . PHE B 21  ? 0.4185 0.4383 0.4057 0.0316  0.0470  0.0388  21  PHE B CZ  
1264 N N   . GLN B 22  ? 0.3417 0.2248 0.4847 0.0040  0.0551  -0.0070 22  GLN B N   
1265 C CA  . GLN B 22  ? 0.3579 0.2403 0.5162 0.0059  0.0707  -0.0189 22  GLN B CA  
1266 C C   . GLN B 22  ? 0.3604 0.1940 0.5131 -0.0149 0.0535  0.0053  22  GLN B C   
1267 O O   . GLN B 22  ? 0.3493 0.2139 0.5160 -0.0141 0.0589  -0.0056 22  GLN B O   
1268 C CB  . GLN B 22  ? 0.3923 0.1966 0.5298 0.0365  0.0724  -0.0205 22  GLN B CB  
1269 C CG  . GLN B 22  ? 0.4113 0.2858 0.5578 0.0166  0.0665  -0.0302 22  GLN B CG  
1270 C CD  . GLN B 22  ? 0.4930 0.3496 0.5779 0.0463  0.0502  -0.0319 22  GLN B CD  
1271 O OE1 . GLN B 22  ? 0.5292 0.3611 0.5788 0.0271  0.0135  -0.0863 22  GLN B OE1 
1272 N NE2 . GLN B 22  ? 0.5317 0.3687 0.5688 0.0791  0.0876  -0.0544 22  GLN B NE2 
1273 N N   A SER B 23  ? 0.3507 0.2059 0.5175 -0.0185 0.0501  0.0250  23  SER B N   
1274 N N   B SER B 23  ? 0.3562 0.2056 0.5187 -0.0175 0.0528  0.0162  23  SER B N   
1275 C CA  A SER B 23  ? 0.3398 0.1964 0.5341 -0.0065 0.0418  0.0286  23  SER B CA  
1276 C CA  B SER B 23  ? 0.3465 0.1928 0.5344 -0.0058 0.0460  0.0128  23  SER B CA  
1277 C C   A SER B 23  ? 0.3220 0.1818 0.5265 0.0154  0.0453  0.0220  23  SER B C   
1278 C C   B SER B 23  ? 0.3261 0.1802 0.5272 0.0175  0.0464  0.0143  23  SER B C   
1279 O O   A SER B 23  ? 0.3233 0.2060 0.5609 0.0186  0.0460  -0.0098 23  SER B O   
1280 O O   B SER B 23  ? 0.3263 0.2045 0.5613 0.0198  0.0472  -0.0157 23  SER B O   
1281 C CB  A SER B 23  ? 0.3508 0.2644 0.5381 -0.0135 0.0425  0.0464  23  SER B CB  
1282 C CB  B SER B 23  ? 0.3654 0.2634 0.5413 -0.0061 0.0455  0.0151  23  SER B CB  
1283 O OG  A SER B 23  ? 0.3887 0.3774 0.5645 -0.0145 0.0182  0.0759  23  SER B OG  
1284 O OG  B SER B 23  ? 0.4150 0.3457 0.5612 -0.0307 0.0560  0.0267  23  SER B OG  
1285 N N   . GLU B 24  ? 0.3020 0.1785 0.5123 0.0396  0.0576  -0.0053 24  GLU B N   
1286 C CA  . GLU B 24  ? 0.3203 0.1833 0.5182 0.0199  0.0569  -0.0088 24  GLU B CA  
1287 C C   . GLU B 24  ? 0.3233 0.1415 0.5406 0.0002  0.0472  -0.0090 24  GLU B C   
1288 O O   . GLU B 24  ? 0.3413 0.1614 0.5551 -0.0102 0.0703  -0.0280 24  GLU B O   
1289 C CB  . GLU B 24  ? 0.3440 0.2043 0.4928 0.0475  0.0611  0.0012  24  GLU B CB  
1290 C CG  . GLU B 24  ? 0.3795 0.2456 0.4820 0.0612  0.0401  -0.0101 24  GLU B CG  
1291 C CD  . GLU B 24  ? 0.4403 0.2564 0.4882 0.0777  0.0180  -0.0257 24  GLU B CD  
1292 O OE1 . GLU B 24  ? 0.5392 0.2670 0.5013 0.1418  0.0299  -0.0258 24  GLU B OE1 
1293 O OE2 . GLU B 24  ? 0.4899 0.3677 0.5188 0.0787  0.0322  -0.0311 24  GLU B OE2 
1294 N N   . LYS B 25  ? 0.3205 0.1541 0.5636 -0.0534 0.0502  -0.0167 25  LYS B N   
1295 C CA  . LYS B 25  ? 0.3739 0.2041 0.5940 -0.0379 0.0598  -0.0567 25  LYS B CA  
1296 C C   . LYS B 25  ? 0.3728 0.2179 0.6269 -0.0271 0.0823  -0.0504 25  LYS B C   
1297 O O   . LYS B 25  ? 0.4177 0.3189 0.6243 -0.0577 0.0995  -0.0637 25  LYS B O   
1298 C CB  . LYS B 25  ? 0.3853 0.3147 0.6393 -0.0593 0.0586  -0.0178 25  LYS B CB  
1299 C CG  . LYS B 25  ? 0.4594 0.4275 0.6849 -0.0574 0.0554  -0.0249 25  LYS B CG  
1300 C CD  . LYS B 25  ? 0.4917 0.4933 0.7468 -0.0365 0.0550  -0.0276 25  LYS B CD  
1301 C CE  . LYS B 25  ? 0.5527 0.5109 0.7840 -0.0213 0.0704  -0.0475 25  LYS B CE  
1302 N NZ  . LYS B 25  ? 0.5756 0.5684 0.8103 -0.0045 0.0757  -0.0432 25  LYS B NZ  
1303 N N   . ALA B 26  ? 0.3257 0.1962 0.6302 -0.0193 0.1121  -0.0674 26  ALA B N   
1304 C CA  . ALA B 26  ? 0.3231 0.1689 0.7003 -0.0168 0.1146  -0.0523 26  ALA B CA  
1305 C C   . ALA B 26  ? 0.3199 0.1687 0.7302 0.0132  0.1006  -0.0587 26  ALA B C   
1306 O O   . ALA B 26  ? 0.3639 0.2285 0.7796 0.0317  0.1369  -0.0947 26  ALA B O   
1307 C CB  . ALA B 26  ? 0.3653 0.1741 0.7210 -0.0267 0.0977  -0.0545 26  ALA B CB  
1308 N N   . ALA B 27  ? 0.3440 0.1917 0.7257 -0.0095 0.0740  -0.0422 27  ALA B N   
1309 C CA  . ALA B 27  ? 0.3637 0.1967 0.7219 -0.0031 0.0504  -0.0371 27  ALA B CA  
1310 C C   . ALA B 27  ? 0.3542 0.1944 0.7243 0.0086  0.0478  -0.0423 27  ALA B C   
1311 O O   . ALA B 27  ? 0.3619 0.1838 0.7243 -0.0132 0.0157  -0.0573 27  ALA B O   
1312 C CB  . ALA B 27  ? 0.3902 0.2322 0.7211 0.0004  0.0477  -0.0431 27  ALA B CB  
1313 N N   . GLY B 28  ? 0.3313 0.1928 0.6957 -0.0168 0.0492  -0.0392 28  GLY B N   
1314 C CA  . GLY B 28  ? 0.3793 0.2545 0.6847 -0.0055 0.0583  -0.0496 28  GLY B CA  
1315 C C   . GLY B 28  ? 0.4144 0.2723 0.6797 0.0128  0.0782  -0.0318 28  GLY B C   
1316 O O   . GLY B 28  ? 0.4306 0.2904 0.6836 -0.0175 0.1066  -0.0491 28  GLY B O   
1317 N N   . SER B 29  ? 0.4039 0.2822 0.6407 0.0239  0.0510  -0.0195 29  SER B N   
1318 C CA  . SER B 29  ? 0.3774 0.2580 0.6007 0.0176  0.0483  -0.0190 29  SER B CA  
1319 C C   . SER B 29  ? 0.3727 0.2479 0.5773 0.0181  0.0342  -0.0189 29  SER B C   
1320 O O   . SER B 29  ? 0.3720 0.2657 0.5891 0.0133  0.0198  -0.0137 29  SER B O   
1321 C CB  . SER B 29  ? 0.3979 0.2548 0.6062 0.0144  0.0393  -0.0160 29  SER B CB  
1322 O OG  . SER B 29  ? 0.4100 0.2403 0.5799 0.0156  0.0480  -0.0098 29  SER B OG  
1323 N N   . VAL B 30  ? 0.3814 0.2269 0.5471 0.0038  0.0275  -0.0246 30  VAL B N   
1324 C CA  . VAL B 30  ? 0.3799 0.1790 0.5208 -0.0003 0.0399  -0.0287 30  VAL B CA  
1325 C C   . VAL B 30  ? 0.4009 0.1702 0.5172 0.0152  0.0494  -0.0004 30  VAL B C   
1326 O O   . VAL B 30  ? 0.3892 0.1903 0.5465 0.0065  0.0615  0.0172  30  VAL B O   
1327 C CB  . VAL B 30  ? 0.3966 0.1834 0.5276 0.0119  0.0238  -0.0466 30  VAL B CB  
1328 C CG1 . VAL B 30  ? 0.3835 0.1600 0.5268 0.0094  0.0156  -0.0562 30  VAL B CG1 
1329 C CG2 . VAL B 30  ? 0.4089 0.1916 0.5600 0.0089  0.0038  -0.0127 30  VAL B CG2 
1330 N N   . SER B 31  ? 0.3817 0.2057 0.5207 -0.0260 0.0323  0.0070  31  SER B N   
1331 C CA  . SER B 31  ? 0.3920 0.1916 0.5054 -0.0113 0.0356  0.0293  31  SER B CA  
1332 C C   . SER B 31  ? 0.3918 0.1548 0.4970 -0.0120 0.0455  0.0224  31  SER B C   
1333 O O   . SER B 31  ? 0.3745 0.1807 0.5047 -0.0155 0.0480  0.0081  31  SER B O   
1334 C CB  . SER B 31  ? 0.3972 0.2446 0.5246 -0.0215 0.0284  0.0224  31  SER B CB  
1335 O OG  . SER B 31  ? 0.3981 0.2749 0.4812 -0.0206 0.0237  0.0222  31  SER B OG  
1336 N N   . LYS B 32  ? 0.4122 0.1869 0.4968 -0.0541 0.0671  0.0252  32  LYS B N   
1337 C CA  . LYS B 32  ? 0.4518 0.2101 0.4958 -0.0232 0.0581  0.0311  32  LYS B CA  
1338 C C   . LYS B 32  ? 0.4241 0.1746 0.4588 -0.0244 0.0388  0.0334  32  LYS B C   
1339 O O   . LYS B 32  ? 0.4050 0.1873 0.4320 -0.0135 0.0383  0.0498  32  LYS B O   
1340 C CB  . LYS B 32  ? 0.4537 0.2191 0.5435 -0.0308 0.0750  0.0321  32  LYS B CB  
1341 C CG  . LYS B 32  ? 0.4838 0.2532 0.5791 -0.0401 0.0691  0.0458  32  LYS B CG  
1342 C CD  . LYS B 32  ? 0.5088 0.2740 0.6399 -0.0359 0.0857  0.0567  32  LYS B CD  
1343 C CE  . LYS B 32  ? 0.5481 0.2464 0.6664 -0.0324 0.0804  0.0678  32  LYS B CE  
1344 N NZ  . LYS B 32  ? 0.5665 0.2317 0.6737 -0.0179 0.0862  0.1123  32  LYS B NZ  
1345 N N   A SER B 33  ? 0.4340 0.1336 0.4650 -0.0151 0.0359  0.0347  33  SER B N   
1346 N N   B SER B 33  ? 0.4233 0.1348 0.4555 -0.0128 0.0402  0.0275  33  SER B N   
1347 C CA  A SER B 33  ? 0.4293 0.1372 0.4497 -0.0210 0.0365  0.0207  33  SER B CA  
1348 C CA  B SER B 33  ? 0.4131 0.1382 0.4327 -0.0167 0.0395  0.0099  33  SER B CA  
1349 C C   A SER B 33  ? 0.3894 0.1500 0.4346 -0.0076 0.0480  -0.0083 33  SER B C   
1350 C C   B SER B 33  ? 0.3817 0.1534 0.4267 -0.0061 0.0490  -0.0125 33  SER B C   
1351 O O   A SER B 33  ? 0.3768 0.1654 0.4429 -0.0138 0.0511  -0.0283 33  SER B O   
1352 O O   B SER B 33  ? 0.3711 0.1746 0.4363 -0.0081 0.0510  -0.0295 33  SER B O   
1353 C CB  A SER B 33  ? 0.4548 0.1831 0.4739 -0.0259 0.0286  0.0172  33  SER B CB  
1354 C CB  B SER B 33  ? 0.4224 0.1659 0.4455 -0.0151 0.0365  0.0010  33  SER B CB  
1355 O OG  A SER B 33  ? 0.4883 0.2399 0.5074 -0.0014 0.0090  0.0325  33  SER B OG  
1356 O OG  B SER B 33  ? 0.4362 0.2307 0.4446 -0.0234 0.0328  0.0066  33  SER B OG  
1357 N N   . THR B 34  ? 0.3615 0.1545 0.4180 -0.0031 0.0479  -0.0028 34  THR B N   
1358 C CA  . THR B 34  ? 0.3678 0.1335 0.4269 0.0139  0.0539  0.0126  34  THR B CA  
1359 C C   . THR B 34  ? 0.3770 0.1217 0.3967 0.0220  0.0671  -0.0015 34  THR B C   
1360 O O   . THR B 34  ? 0.3717 0.1442 0.4177 0.0139  0.0560  0.0103  34  THR B O   
1361 C CB  . THR B 34  ? 0.3825 0.1122 0.4307 0.0103  0.0494  0.0192  34  THR B CB  
1362 O OG1 . THR B 34  ? 0.4222 0.1600 0.4506 0.0077  0.0311  0.0594  34  THR B OG1 
1363 C CG2 . THR B 34  ? 0.3747 0.0828 0.4460 0.0256  0.0702  0.0357  34  THR B CG2 
1364 N N   . GLN B 35  ? 0.3807 0.1574 0.4003 -0.0023 0.0806  -0.0178 35  GLN B N   
1365 C CA  . GLN B 35  ? 0.3968 0.1176 0.3757 0.0140  0.0842  -0.0226 35  GLN B CA  
1366 C C   . GLN B 35  ? 0.3798 0.1213 0.3383 0.0072  0.0606  -0.0266 35  GLN B C   
1367 O O   . GLN B 35  ? 0.3824 0.1222 0.3617 0.0071  0.0347  0.0049  35  GLN B O   
1368 C CB  . GLN B 35  ? 0.4321 0.1545 0.4020 0.0261  0.1005  -0.0250 35  GLN B CB  
1369 C CG  . GLN B 35  ? 0.4390 0.2204 0.4119 0.0318  0.1167  -0.0475 35  GLN B CG  
1370 C CD  . GLN B 35  ? 0.5083 0.2948 0.4380 0.0262  0.1281  -0.0669 35  GLN B CD  
1371 O OE1 . GLN B 35  ? 0.5463 0.3591 0.4998 -0.0115 0.1354  -0.0556 35  GLN B OE1 
1372 N NE2 . GLN B 35  ? 0.5954 0.3933 0.4791 0.0029  0.0901  -0.0764 35  GLN B NE2 
1373 N N   . PHE B 36  ? 0.3707 0.1057 0.3444 0.0019  0.0287  0.0021  36  PHE B N   
1374 C CA  . PHE B 36  ? 0.3607 0.1481 0.3634 0.0109  0.0325  -0.0071 36  PHE B CA  
1375 C C   . PHE B 36  ? 0.3737 0.1261 0.3563 0.0119  0.0208  0.0063  36  PHE B C   
1376 O O   . PHE B 36  ? 0.3751 0.1095 0.3516 0.0241  0.0311  0.0156  36  PHE B O   
1377 C CB  . PHE B 36  ? 0.3755 0.1528 0.3723 0.0075  0.0338  -0.0066 36  PHE B CB  
1378 C CG  . PHE B 36  ? 0.3926 0.1728 0.3571 0.0064  0.0426  -0.0310 36  PHE B CG  
1379 C CD1 . PHE B 36  ? 0.4064 0.1584 0.3781 0.0046  0.0520  -0.0133 36  PHE B CD1 
1380 C CD2 . PHE B 36  ? 0.4143 0.2150 0.3636 0.0241  0.0479  -0.0203 36  PHE B CD2 
1381 C CE1 . PHE B 36  ? 0.4072 0.1359 0.3882 0.0178  0.0473  -0.0192 36  PHE B CE1 
1382 C CE2 . PHE B 36  ? 0.4273 0.2078 0.3823 0.0285  0.0515  -0.0252 36  PHE B CE2 
1383 C CZ  . PHE B 36  ? 0.4395 0.1750 0.4064 0.0394  0.0525  -0.0042 36  PHE B CZ  
1384 N N   . GLU B 37  ? 0.3719 0.1292 0.3300 0.0098  0.0213  -0.0021 37  GLU B N   
1385 C CA  . GLU B 37  ? 0.3684 0.1156 0.3315 0.0114  0.0322  -0.0024 37  GLU B CA  
1386 C C   . GLU B 37  ? 0.3634 0.1087 0.3237 0.0306  0.0260  -0.0102 37  GLU B C   
1387 O O   . GLU B 37  ? 0.3749 0.1207 0.3463 0.0414  0.0474  -0.0002 37  GLU B O   
1388 C CB  . GLU B 37  ? 0.3994 0.1486 0.3477 0.0074  0.0092  0.0031  37  GLU B CB  
1389 C CG  . GLU B 37  ? 0.4749 0.1876 0.3978 -0.0077 -0.0026 -0.0075 37  GLU B CG  
1390 C CD  . GLU B 37  ? 0.5709 0.2846 0.4532 -0.0063 -0.0629 -0.0032 37  GLU B CD  
1391 O OE1 . GLU B 37  ? 0.6863 0.2872 0.4815 0.0616  -0.0753 0.0058  37  GLU B OE1 
1392 O OE2 . GLU B 37  ? 0.6729 0.2990 0.5794 -0.0357 -0.0855 -0.0321 37  GLU B OE2 
1393 N N   . GLU B 38  ? 0.3639 0.1285 0.3201 0.0282  0.0356  0.0182  38  GLU B N   
1394 C CA  . GLU B 38  ? 0.3816 0.0893 0.3221 0.0130  0.0395  0.0096  38  GLU B CA  
1395 C C   . GLU B 38  ? 0.3846 0.1002 0.3019 0.0076  0.0367  0.0179  38  GLU B C   
1396 O O   . GLU B 38  ? 0.3889 0.1147 0.3187 0.0161  0.0266  -0.0054 38  GLU B O   
1397 C CB  . GLU B 38  ? 0.4076 0.1253 0.3319 0.0021  0.0524  0.0198  38  GLU B CB  
1398 C CG  . GLU B 38  ? 0.4247 0.1641 0.3673 -0.0119 0.0377  0.0048  38  GLU B CG  
1399 C CD  . GLU B 38  ? 0.4663 0.1810 0.3878 0.0064  0.0473  -0.0113 38  GLU B CD  
1400 O OE1 . GLU B 38  ? 0.4817 0.2310 0.4239 0.0505  0.0581  -0.0049 38  GLU B OE1 
1401 O OE2 . GLU B 38  ? 0.5702 0.1632 0.4234 0.0207  0.0210  -0.0601 38  GLU B OE2 
1402 N N   . ALA B 39  ? 0.3956 0.0858 0.3037 0.0048  0.0289  0.0087  39  ALA B N   
1403 C CA  . ALA B 39  ? 0.3920 0.1039 0.3084 0.0039  0.0241  0.0143  39  ALA B CA  
1404 C C   . ALA B 39  ? 0.3736 0.0839 0.3268 0.0173  0.0190  0.0045  39  ALA B C   
1405 O O   . ALA B 39  ? 0.3594 0.1501 0.3394 0.0107  0.0015  0.0005  39  ALA B O   
1406 C CB  . ALA B 39  ? 0.4205 0.0821 0.3377 0.0047  0.0296  0.0174  39  ALA B CB  
1407 N N   . TRP B 40  ? 0.3734 0.0866 0.3260 0.0140  0.0301  0.0000  40  TRP B N   
1408 C CA  . TRP B 40  ? 0.3901 0.1188 0.3310 0.0095  0.0446  -0.0068 40  TRP B CA  
1409 C C   . TRP B 40  ? 0.3760 0.1343 0.3361 0.0090  0.0472  -0.0129 40  TRP B C   
1410 O O   . TRP B 40  ? 0.4082 0.1322 0.4120 0.0251  0.0575  -0.0032 40  TRP B O   
1411 C CB  . TRP B 40  ? 0.4187 0.1705 0.3516 0.0123  0.0438  -0.0170 40  TRP B CB  
1412 C CG  . TRP B 40  ? 0.4384 0.1939 0.3459 0.0423  0.0418  -0.0161 40  TRP B CG  
1413 C CD1 . TRP B 40  ? 0.4664 0.2283 0.3785 0.0497  0.0453  -0.0404 40  TRP B CD1 
1414 C CD2 . TRP B 40  ? 0.4354 0.1247 0.3381 0.0550  0.0334  -0.0143 40  TRP B CD2 
1415 N NE1 . TRP B 40  ? 0.4840 0.1730 0.3411 0.0472  0.0273  -0.0552 40  TRP B NE1 
1416 C CE2 . TRP B 40  ? 0.4572 0.1841 0.3385 0.0536  0.0531  -0.0311 40  TRP B CE2 
1417 C CE3 . TRP B 40  ? 0.4618 0.1211 0.3465 0.0674  0.0445  0.0097  40  TRP B CE3 
1418 C CZ2 . TRP B 40  ? 0.4692 0.1860 0.3525 0.0589  0.0556  -0.0321 40  TRP B CZ2 
1419 C CZ3 . TRP B 40  ? 0.4665 0.1548 0.3664 0.0642  0.0420  0.0109  40  TRP B CZ3 
1420 C CH2 . TRP B 40  ? 0.4720 0.2020 0.3469 0.0380  0.0577  0.0096  40  TRP B CH2 
1421 N N   A CYS B 41  ? 0.3819 0.1329 0.3481 0.0065  0.0492  0.0074  41  CYS B N   
1422 N N   B CYS B 41  ? 0.3896 0.1373 0.3538 0.0073  0.0399  -0.0045 41  CYS B N   
1423 C CA  A CYS B 41  ? 0.3819 0.1290 0.3436 0.0064  0.0442  0.0115  41  CYS B CA  
1424 C CA  B CYS B 41  ? 0.3953 0.1509 0.3496 -0.0028 0.0290  -0.0062 41  CYS B CA  
1425 C C   A CYS B 41  ? 0.3726 0.1034 0.3495 0.0131  0.0331  0.0211  41  CYS B C   
1426 C C   B CYS B 41  ? 0.3777 0.1325 0.3458 0.0096  0.0294  -0.0075 41  CYS B C   
1427 O O   A CYS B 41  ? 0.3694 0.0803 0.3434 0.0112  0.0200  0.0516  41  CYS B O   
1428 O O   B CYS B 41  ? 0.3744 0.1667 0.3339 0.0157  0.0332  -0.0407 41  CYS B O   
1429 C CB  A CYS B 41  ? 0.3996 0.1412 0.3575 0.0194  0.0533  0.0122  41  CYS B CB  
1430 C CB  B CYS B 41  ? 0.4238 0.1693 0.3665 0.0093  0.0158  0.0028  41  CYS B CB  
1431 S SG  A CYS B 41  ? 0.4308 0.1837 0.3618 0.0252  0.0570  0.0291  41  CYS B SG  
1432 S SG  B CYS B 41  ? 0.5020 0.2042 0.4034 -0.0164 -0.0069 0.0420  41  CYS B SG  
1433 N N   . LEU B 42  ? 0.3704 0.1234 0.3368 0.0093  0.0115  0.0055  42  LEU B N   
1434 C CA  . LEU B 42  ? 0.3630 0.1208 0.3491 0.0071  0.0063  -0.0058 42  LEU B CA  
1435 C C   . LEU B 42  ? 0.3657 0.1108 0.3495 0.0041  0.0022  0.0007  42  LEU B C   
1436 O O   . LEU B 42  ? 0.4010 0.1577 0.3298 -0.0029 0.0046  0.0040  42  LEU B O   
1437 C CB  . LEU B 42  ? 0.3953 0.1390 0.3290 0.0369  0.0030  -0.0125 42  LEU B CB  
1438 C CG  . LEU B 42  ? 0.4006 0.1506 0.3480 0.0429  0.0202  -0.0299 42  LEU B CG  
1439 C CD1 . LEU B 42  ? 0.4197 0.1876 0.3457 0.0637  0.0281  -0.0578 42  LEU B CD1 
1440 C CD2 . LEU B 42  ? 0.4255 0.2007 0.3786 0.0334  0.0230  -0.0478 42  LEU B CD2 
1441 N N   . VAL B 43  ? 0.3832 0.1053 0.3269 0.0229  -0.0170 -0.0130 43  VAL B N   
1442 C CA  . VAL B 43  ? 0.3733 0.1222 0.3586 0.0267  -0.0200 -0.0399 43  VAL B CA  
1443 C C   . VAL B 43  ? 0.3853 0.1445 0.3362 0.0227  -0.0151 -0.0462 43  VAL B C   
1444 O O   . VAL B 43  ? 0.3793 0.1567 0.3768 0.0351  -0.0194 -0.0395 43  VAL B O   
1445 C CB  . VAL B 43  ? 0.4273 0.1251 0.3722 0.0163  -0.0102 -0.0307 43  VAL B CB  
1446 C CG1 . VAL B 43  ? 0.4449 0.1423 0.3877 0.0363  -0.0104 -0.0435 43  VAL B CG1 
1447 C CG2 . VAL B 43  ? 0.4540 0.1741 0.3871 0.0232  -0.0190 -0.0350 43  VAL B CG2 
1448 N N   . ARG B 44  ? 0.3862 0.1721 0.3323 0.0397  0.0038  -0.0314 44  ARG B N   
1449 C CA  . ARG B 44  ? 0.4263 0.2256 0.3225 0.0328  0.0193  -0.0440 44  ARG B CA  
1450 C C   . ARG B 44  ? 0.4346 0.2244 0.3250 0.0189  0.0309  -0.0010 44  ARG B C   
1451 O O   . ARG B 44  ? 0.4622 0.2680 0.3418 0.0614  0.0705  0.0000  44  ARG B O   
1452 C CB  . ARG B 44  ? 0.4316 0.2394 0.3371 0.0335  0.0041  -0.0454 44  ARG B CB  
1453 C CG  . ARG B 44  ? 0.4362 0.2391 0.3522 0.0264  0.0097  -0.0475 44  ARG B CG  
1454 C CD  . ARG B 44  ? 0.4562 0.3158 0.3681 0.0254  -0.0055 -0.0395 44  ARG B CD  
1455 N NE  . ARG B 44  ? 0.4788 0.3161 0.3872 0.0099  0.0032  -0.0405 44  ARG B NE  
1456 C CZ  . ARG B 44  ? 0.4979 0.2527 0.4003 0.0299  0.0027  -0.0447 44  ARG B CZ  
1457 N NH1 . ARG B 44  ? 0.4865 0.1991 0.4218 0.0200  0.0255  -0.0535 44  ARG B NH1 
1458 N NH2 . ARG B 44  ? 0.5212 0.2944 0.4377 0.0668  0.0039  -0.0745 44  ARG B NH2 
1459 N N   . SER B 45  ? 0.3932 0.2044 0.3406 0.0200  0.0310  0.0000  45  SER B N   
1460 C CA  . SER B 45  ? 0.4117 0.2045 0.3663 -0.0004 0.0394  -0.0112 45  SER B CA  
1461 C C   . SER B 45  ? 0.4088 0.1995 0.3457 0.0002  0.0432  0.0031  45  SER B C   
1462 O O   . SER B 45  ? 0.4060 0.1779 0.4045 0.0382  0.0125  -0.0241 45  SER B O   
1463 C CB  . SER B 45  ? 0.3769 0.1918 0.3803 -0.0197 0.0455  -0.0183 45  SER B CB  
1464 O OG  . SER B 45  ? 0.4069 0.1401 0.4264 -0.0069 0.0026  -0.0083 45  SER B OG  
1465 N N   . LYS B 46  ? 0.4334 0.2106 0.3763 -0.0090 0.0459  0.0188  46  LYS B N   
1466 C CA  . LYS B 46  ? 0.4406 0.2648 0.4037 -0.0260 0.0554  0.0336  46  LYS B CA  
1467 C C   . LYS B 46  ? 0.3978 0.2191 0.3818 -0.0174 0.0500  0.0277  46  LYS B C   
1468 O O   . LYS B 46  ? 0.4271 0.2751 0.4256 -0.0161 0.0351  0.0017  46  LYS B O   
1469 C CB  . LYS B 46  ? 0.4898 0.2948 0.4391 -0.0405 0.0671  0.0581  46  LYS B CB  
1470 C CG  . LYS B 46  ? 0.5378 0.3150 0.5025 -0.0385 0.0653  0.0574  46  LYS B CG  
1471 C CD  . LYS B 46  ? 0.5974 0.3840 0.5732 -0.0595 0.0755  0.0898  46  LYS B CD  
1472 C CE  . LYS B 46  ? 0.6444 0.4619 0.6148 -0.0441 0.0610  0.0763  46  LYS B CE  
1473 N NZ  . LYS B 46  ? 0.6771 0.5161 0.6722 -0.0323 0.0780  0.0956  46  LYS B NZ  
1474 N N   . TYR B 47  ? 0.3770 0.1352 0.3450 -0.0193 0.0315  0.0147  47  TYR B N   
1475 C CA  . TYR B 47  ? 0.3753 0.1538 0.3407 -0.0183 0.0430  0.0088  47  TYR B CA  
1476 C C   . TYR B 47  ? 0.3646 0.1422 0.3211 -0.0217 0.0210  -0.0078 47  TYR B C   
1477 O O   . TYR B 47  ? 0.3422 0.1393 0.3599 -0.0071 0.0096  -0.0020 47  TYR B O   
1478 C CB  . TYR B 47  ? 0.3777 0.1691 0.3867 -0.0015 0.0414  0.0366  47  TYR B CB  
1479 C CG  . TYR B 47  ? 0.3861 0.1673 0.3862 -0.0215 0.0486  0.0150  47  TYR B CG  
1480 C CD1 . TYR B 47  ? 0.3991 0.1600 0.4136 -0.0380 0.0507  0.0045  47  TYR B CD1 
1481 C CD2 . TYR B 47  ? 0.4218 0.1630 0.3824 -0.0208 0.0610  0.0267  47  TYR B CD2 
1482 C CE1 . TYR B 47  ? 0.4314 0.1593 0.4349 -0.0328 0.0553  0.0280  47  TYR B CE1 
1483 C CE2 . TYR B 47  ? 0.4277 0.1479 0.4206 -0.0046 0.0626  0.0418  47  TYR B CE2 
1484 C CZ  . TYR B 47  ? 0.4326 0.1428 0.4399 -0.0231 0.0642  0.0213  47  TYR B CZ  
1485 O OH  . TYR B 47  ? 0.4634 0.1528 0.5029 -0.0109 0.1010  0.0432  47  TYR B OH  
1486 N N   . ASN B 48  ? 0.4254 0.1930 0.3568 -0.0310 0.0050  0.0063  48  ASN B N   
1487 C CA  . ASN B 48  ? 0.4267 0.1357 0.3657 -0.0462 -0.0085 -0.0001 48  ASN B CA  
1488 C C   . ASN B 48  ? 0.4415 0.1813 0.3624 -0.0553 0.0025  0.0006  48  ASN B C   
1489 O O   . ASN B 48  ? 0.4421 0.2000 0.3052 -0.0783 -0.0139 -0.0065 48  ASN B O   
1490 C CB  . ASN B 48  ? 0.4411 0.1729 0.4141 -0.0468 -0.0309 0.0108  48  ASN B CB  
1491 C CG  . ASN B 48  ? 0.4886 0.2584 0.4130 0.0042  -0.0235 0.0228  48  ASN B CG  
1492 O OD1 . ASN B 48  ? 0.5263 0.2881 0.4163 0.0227  0.0015  0.0242  48  ASN B OD1 
1493 N ND2 . ASN B 48  ? 0.5021 0.4001 0.4653 0.0359  -0.0261 0.0400  48  ASN B ND2 
1494 N N   . ASP B 49  ? 0.4631 0.2082 0.3260 -0.0448 0.0114  -0.0187 49  ASP B N   
1495 C CA  . ASP B 49  ? 0.4762 0.1932 0.3470 -0.0322 0.0333  -0.0320 49  ASP B CA  
1496 C C   . ASP B 49  ? 0.4320 0.1859 0.3205 -0.0196 0.0498  -0.0364 49  ASP B C   
1497 O O   . ASP B 49  ? 0.4199 0.2004 0.3659 -0.0395 0.0351  -0.0074 49  ASP B O   
1498 C CB  . ASP B 49  ? 0.5269 0.1983 0.3883 -0.0272 0.0274  -0.0431 49  ASP B CB  
1499 C CG  . ASP B 49  ? 0.6176 0.2585 0.4340 -0.0160 0.0142  -0.0454 49  ASP B CG  
1500 O OD1 . ASP B 49  ? 0.6796 0.4023 0.4548 0.0381  0.0049  0.0143  49  ASP B OD1 
1501 O OD2 . ASP B 49  ? 0.6564 0.2373 0.5095 -0.0035 0.0185  -0.0269 49  ASP B OD2 
1502 N N   . ASP B 50  ? 0.4060 0.1344 0.3279 -0.0373 0.0272  -0.0036 50  ASP B N   
1503 C CA  . ASP B 50  ? 0.4213 0.1494 0.3364 -0.0261 0.0241  -0.0328 50  ASP B CA  
1504 C C   . ASP B 50  ? 0.3869 0.1218 0.3173 0.0049  0.0065  -0.0134 50  ASP B C   
1505 O O   . ASP B 50  ? 0.3881 0.1504 0.3246 -0.0089 0.0080  -0.0316 50  ASP B O   
1506 C CB  . ASP B 50  ? 0.4458 0.1477 0.3355 -0.0277 0.0199  -0.0201 50  ASP B CB  
1507 C CG  . ASP B 50  ? 0.4679 0.1535 0.3592 -0.0036 0.0391  -0.0246 50  ASP B CG  
1508 O OD1 . ASP B 50  ? 0.4875 0.1812 0.3693 0.0116  0.0456  -0.0567 50  ASP B OD1 
1509 O OD2 . ASP B 50  ? 0.4642 0.1749 0.3724 0.0323  0.0365  0.0098  50  ASP B OD2 
1510 N N   . ILE B 51  ? 0.3946 0.1262 0.3258 -0.0117 0.0109  -0.0100 51  ILE B N   
1511 C CA  . ILE B 51  ? 0.3848 0.1209 0.3143 -0.0077 0.0173  -0.0158 51  ILE B CA  
1512 C C   . ILE B 51  ? 0.3821 0.1194 0.3057 -0.0096 0.0217  -0.0284 51  ILE B C   
1513 O O   . ILE B 51  ? 0.4093 0.0955 0.3192 -0.0036 0.0151  -0.0386 51  ILE B O   
1514 C CB  . ILE B 51  ? 0.3766 0.1188 0.3271 -0.0247 0.0280  -0.0280 51  ILE B CB  
1515 C CG1 . ILE B 51  ? 0.3878 0.1543 0.3279 -0.0092 0.0342  -0.0233 51  ILE B CG1 
1516 C CG2 . ILE B 51  ? 0.3752 0.1014 0.3275 -0.0024 0.0268  -0.0145 51  ILE B CG2 
1517 C CD1 . ILE B 51  ? 0.3863 0.1835 0.3384 -0.0211 0.0478  -0.0346 51  ILE B CD1 
1518 N N   A ARG B 52  ? 0.3984 0.1402 0.3120 -0.0157 0.0241  -0.0163 52  ARG B N   
1519 N N   B ARG B 52  ? 0.4012 0.1486 0.3057 -0.0179 0.0246  -0.0162 52  ARG B N   
1520 C CA  A ARG B 52  ? 0.4142 0.1592 0.3200 -0.0160 0.0230  -0.0112 52  ARG B CA  
1521 C CA  B ARG B 52  ? 0.4190 0.1752 0.3057 -0.0198 0.0214  -0.0131 52  ARG B CA  
1522 C C   A ARG B 52  ? 0.4085 0.1422 0.3209 -0.0130 0.0307  -0.0116 52  ARG B C   
1523 C C   B ARG B 52  ? 0.4121 0.1471 0.3133 -0.0149 0.0300  -0.0108 52  ARG B C   
1524 O O   A ARG B 52  ? 0.4109 0.1481 0.3372 -0.0178 0.0413  -0.0023 52  ARG B O   
1525 O O   B ARG B 52  ? 0.4126 0.1527 0.3306 -0.0196 0.0404  -0.0026 52  ARG B O   
1526 C CB  A ARG B 52  ? 0.4143 0.1841 0.3410 -0.0241 0.0147  -0.0158 52  ARG B CB  
1527 C CB  B ARG B 52  ? 0.4277 0.2203 0.3162 -0.0323 0.0141  -0.0198 52  ARG B CB  
1528 C CG  A ARG B 52  ? 0.4307 0.2189 0.3648 -0.0058 0.0139  -0.0273 52  ARG B CG  
1529 C CG  B ARG B 52  ? 0.4468 0.2792 0.3256 -0.0175 0.0110  -0.0366 52  ARG B CG  
1530 C CD  A ARG B 52  ? 0.4582 0.2809 0.3912 0.0073  0.0033  -0.0415 52  ARG B CD  
1531 C CD  B ARG B 52  ? 0.4878 0.3680 0.3428 -0.0113 0.0018  -0.0574 52  ARG B CD  
1532 N NE  A ARG B 52  ? 0.4768 0.3000 0.4231 0.0193  -0.0022 -0.0386 52  ARG B NE  
1533 N NE  B ARG B 52  ? 0.5033 0.4525 0.3628 -0.0201 -0.0054 -0.0678 52  ARG B NE  
1534 C CZ  A ARG B 52  ? 0.4789 0.3667 0.4398 0.0152  -0.0177 -0.0526 52  ARG B CZ  
1535 C CZ  B ARG B 52  ? 0.5324 0.4856 0.3593 -0.0107 -0.0094 -0.1124 52  ARG B CZ  
1536 N NH1 A ARG B 52  ? 0.4814 0.3891 0.4386 -0.0089 -0.0210 -0.0553 52  ARG B NH1 
1537 N NH1 B ARG B 52  ? 0.5532 0.4857 0.3437 -0.0278 -0.0127 -0.1291 52  ARG B NH1 
1538 N NH2 A ARG B 52  ? 0.4852 0.4214 0.4529 0.0356  -0.0102 -0.0590 52  ARG B NH2 
1539 N NH2 B ARG B 52  ? 0.5351 0.5321 0.3654 -0.0068 -0.0187 -0.1301 52  ARG B NH2 
1540 N N   . LYS B 53  ? 0.4146 0.1458 0.3210 -0.0173 0.0321  -0.0058 53  LYS B N   
1541 C CA  . LYS B 53  ? 0.4215 0.1339 0.3310 -0.0066 0.0186  -0.0165 53  LYS B CA  
1542 C C   . LYS B 53  ? 0.3792 0.1665 0.3190 -0.0005 0.0289  -0.0201 53  LYS B C   
1543 O O   . LYS B 53  ? 0.3576 0.1684 0.3605 -0.0027 0.0228  -0.0362 53  LYS B O   
1544 C CB  . LYS B 53  ? 0.4417 0.1224 0.3573 -0.0091 0.0088  -0.0267 53  LYS B CB  
1545 C CG  . LYS B 53  ? 0.4861 0.2087 0.4135 0.0173  -0.0126 -0.0313 53  LYS B CG  
1546 C CD  . LYS B 53  ? 0.5519 0.2761 0.4710 0.0337  0.0145  -0.0188 53  LYS B CD  
1547 C CE  . LYS B 53  ? 0.5827 0.3997 0.5342 0.0680  0.0237  -0.0454 53  LYS B CE  
1548 N NZ  . LYS B 53  ? 0.6375 0.5258 0.5753 0.0416  0.0326  -0.0172 53  LYS B NZ  
1549 N N   . GLY B 54  ? 0.3787 0.1486 0.3106 0.0106  0.0291  -0.0170 54  GLY B N   
1550 C CA  . GLY B 54  ? 0.3726 0.1390 0.2857 0.0093  0.0276  -0.0042 54  GLY B CA  
1551 C C   . GLY B 54  ? 0.3703 0.1455 0.3083 -0.0053 0.0374  -0.0029 54  GLY B C   
1552 O O   . GLY B 54  ? 0.3587 0.1169 0.3248 -0.0023 0.0172  0.0004  54  GLY B O   
1553 N N   . ILE B 55  ? 0.4029 0.1125 0.3081 -0.0020 0.0450  0.0071  55  ILE B N   
1554 C CA  . ILE B 55  ? 0.4112 0.1159 0.3115 -0.0116 0.0340  0.0114  55  ILE B CA  
1555 C C   . ILE B 55  ? 0.4054 0.1441 0.3183 -0.0164 0.0236  -0.0001 55  ILE B C   
1556 O O   . ILE B 55  ? 0.4092 0.1316 0.3588 -0.0362 0.0306  -0.0012 55  ILE B O   
1557 C CB  . ILE B 55  ? 0.4033 0.1569 0.3240 -0.0217 0.0352  0.0325  55  ILE B CB  
1558 C CG1 . ILE B 55  ? 0.4044 0.1463 0.3460 0.0003  0.0300  0.0485  55  ILE B CG1 
1559 C CG2 . ILE B 55  ? 0.4231 0.1485 0.3336 -0.0213 0.0238  0.0356  55  ILE B CG2 
1560 C CD1 . ILE B 55  ? 0.3967 0.1539 0.3856 0.0169  0.0228  0.0268  55  ILE B CD1 
1561 N N   . VAL B 56  ? 0.4441 0.1307 0.3354 -0.0303 0.0383  -0.0112 56  VAL B N   
1562 C CA  . VAL B 56  ? 0.4782 0.1853 0.3469 -0.0077 0.0454  -0.0228 56  VAL B CA  
1563 C C   . VAL B 56  ? 0.4404 0.1727 0.3188 -0.0032 0.0657  -0.0393 56  VAL B C   
1564 O O   . VAL B 56  ? 0.4621 0.1816 0.3691 -0.0078 0.0585  0.0162  56  VAL B O   
1565 C CB  . VAL B 56  ? 0.4998 0.2300 0.3374 -0.0184 0.0667  -0.0554 56  VAL B CB  
1566 C CG1 . VAL B 56  ? 0.5334 0.2130 0.3594 -0.0209 0.0677  -0.1073 56  VAL B CG1 
1567 C CG2 . VAL B 56  ? 0.5215 0.2850 0.3618 -0.0015 0.0700  -0.0733 56  VAL B CG2 
1568 N N   . LEU B 57  ? 0.4385 0.1831 0.3111 0.0004  0.0571  -0.0424 57  LEU B N   
1569 C CA  . LEU B 57  ? 0.4322 0.1744 0.3341 -0.0036 0.0642  -0.0411 57  LEU B CA  
1570 C C   . LEU B 57  ? 0.4183 0.1755 0.3251 0.0017  0.0388  -0.0295 57  LEU B C   
1571 O O   . LEU B 57  ? 0.4339 0.1782 0.3711 0.0044  0.0414  -0.0022 57  LEU B O   
1572 C CB  . LEU B 57  ? 0.4960 0.1236 0.3835 -0.0106 0.0880  -0.0320 57  LEU B CB  
1573 C CG  . LEU B 57  ? 0.5545 0.2983 0.4753 -0.0003 0.0710  0.0600  57  LEU B CG  
1574 C CD1 . LEU B 57  ? 0.5716 0.2386 0.4630 0.0201  0.0843  0.0767  57  LEU B CD1 
1575 C CD2 . LEU B 57  ? 0.5905 0.3276 0.5218 -0.0568 0.0494  0.0741  57  LEU B CD2 
1576 N N   . LEU B 58  ? 0.3852 0.1315 0.3278 -0.0187 0.0240  0.0019  58  LEU B N   
1577 C CA  . LEU B 58  ? 0.3822 0.1363 0.3136 -0.0388 0.0290  0.0117  58  LEU B CA  
1578 C C   . LEU B 58  ? 0.3862 0.1492 0.3209 -0.0355 0.0393  0.0149  58  LEU B C   
1579 O O   . LEU B 58  ? 0.4274 0.1300 0.3692 -0.0727 0.0493  0.0002  58  LEU B O   
1580 C CB  . LEU B 58  ? 0.4010 0.1001 0.3273 -0.0269 0.0398  0.0232  58  LEU B CB  
1581 C CG  . LEU B 58  ? 0.4079 0.1170 0.3267 -0.0306 0.0392  0.0232  58  LEU B CG  
1582 C CD1 . LEU B 58  ? 0.4167 0.1365 0.3300 -0.0265 0.0419  0.0347  58  LEU B CD1 
1583 C CD2 . LEU B 58  ? 0.4429 0.1592 0.3437 -0.0107 0.0247  0.0315  58  LEU B CD2 
1584 N N   . GLU B 59  ? 0.4061 0.1446 0.3432 -0.0359 0.0474  0.0298  59  GLU B N   
1585 C CA  . GLU B 59  ? 0.4225 0.1624 0.3723 -0.0303 0.0562  0.0548  59  GLU B CA  
1586 C C   . GLU B 59  ? 0.4222 0.1827 0.3739 -0.0234 0.0802  0.0555  59  GLU B C   
1587 O O   . GLU B 59  ? 0.4253 0.1924 0.3891 -0.0229 0.0746  0.0517  59  GLU B O   
1588 C CB  . GLU B 59  ? 0.4622 0.2084 0.4081 -0.0384 0.0478  0.0848  59  GLU B CB  
1589 C CG  . GLU B 59  ? 0.4735 0.2654 0.4486 -0.0378 0.0728  0.0931  59  GLU B CG  
1590 C CD  . GLU B 59  ? 0.5675 0.3764 0.5169 -0.0205 0.0449  0.1215  59  GLU B CD  
1591 O OE1 . GLU B 59  ? 0.6738 0.4319 0.5615 -0.0699 0.0423  0.0910  59  GLU B OE1 
1592 O OE2 . GLU B 59  ? 0.6547 0.4368 0.6068 -0.0042 0.0536  0.2311  59  GLU B OE2 
1593 N N   . GLU B 60  ? 0.4462 0.1897 0.3849 -0.0270 0.0783  0.0458  60  GLU B N   
1594 C CA  . GLU B 60  ? 0.4569 0.2617 0.4204 -0.0236 0.1044  0.0145  60  GLU B CA  
1595 C C   . GLU B 60  ? 0.4221 0.2730 0.4402 -0.0155 0.0862  0.0330  60  GLU B C   
1596 O O   . GLU B 60  ? 0.4251 0.2880 0.4497 -0.0203 0.1002  0.0240  60  GLU B O   
1597 C CB  . GLU B 60  ? 0.5235 0.2873 0.4619 -0.0103 0.1085  0.0121  60  GLU B CB  
1598 C CG  . GLU B 60  ? 0.5921 0.4024 0.5001 -0.0335 0.1105  -0.0095 60  GLU B CG  
1599 C CD  . GLU B 60  ? 0.6587 0.4206 0.5267 -0.0693 0.1339  -0.0016 60  GLU B CD  
1600 O OE1 . GLU B 60  ? 0.7769 0.5399 0.5669 -0.0515 0.1021  0.0376  60  GLU B OE1 
1601 O OE2 . GLU B 60  ? 0.7413 0.5012 0.5237 -0.0755 0.1375  -0.0480 60  GLU B OE2 
1602 N N   . LEU B 61  ? 0.4078 0.2058 0.4321 -0.0293 0.0617  0.0625  61  LEU B N   
1603 C CA  . LEU B 61  ? 0.4211 0.1953 0.4580 -0.0203 0.0399  0.0672  61  LEU B CA  
1604 C C   . LEU B 61  ? 0.4573 0.1989 0.4619 -0.0427 0.0301  0.0597  61  LEU B C   
1605 O O   . LEU B 61  ? 0.4318 0.2176 0.5000 -0.0105 0.0231  0.0333  61  LEU B O   
1606 C CB  . LEU B 61  ? 0.4301 0.2208 0.4599 0.0034  0.0342  0.0674  61  LEU B CB  
1607 C CG  . LEU B 61  ? 0.4399 0.2259 0.4636 0.0139  0.0246  0.0794  61  LEU B CG  
1608 C CD1 . LEU B 61  ? 0.4473 0.2381 0.4415 0.0264  0.0262  0.0834  61  LEU B CD1 
1609 C CD2 . LEU B 61  ? 0.4430 0.2538 0.4564 0.0271  0.0294  0.0797  61  LEU B CD2 
1610 N N   . LEU B 62  ? 0.4675 0.2176 0.4808 -0.0536 0.0194  0.0474  62  LEU B N   
1611 C CA  . LEU B 62  ? 0.4864 0.2162 0.4747 -0.0722 0.0098  0.0536  62  LEU B CA  
1612 C C   . LEU B 62  ? 0.4978 0.2580 0.5113 -0.0750 0.0143  0.0609  62  LEU B C   
1613 O O   . LEU B 62  ? 0.5090 0.2950 0.5412 -0.0926 -0.0034 0.0676  62  LEU B O   
1614 C CB  . LEU B 62  ? 0.5248 0.2041 0.4684 -0.0886 0.0026  0.0861  62  LEU B CB  
1615 C CG  . LEU B 62  ? 0.5740 0.2613 0.5262 -0.0280 0.0011  0.0783  62  LEU B CG  
1616 C CD1 . LEU B 62  ? 0.5854 0.2093 0.5107 -0.0126 0.0030  0.1081  62  LEU B CD1 
1617 C CD2 . LEU B 62  ? 0.5869 0.2917 0.5451 -0.0205 -0.0159 0.0930  62  LEU B CD2 
1618 N N   . PRO B 63  ? 0.4837 0.3221 0.5427 -0.1159 0.0418  0.0696  63  PRO B N   
1619 C CA  . PRO B 63  ? 0.4656 0.3790 0.5685 -0.0924 0.0460  0.0339  63  PRO B CA  
1620 C C   . PRO B 63  ? 0.4653 0.3119 0.5516 -0.1243 0.0359  -0.0001 63  PRO B C   
1621 O O   . PRO B 63  ? 0.4838 0.4036 0.6369 -0.1826 0.0406  0.0125  63  PRO B O   
1622 C CB  . PRO B 63  ? 0.4989 0.4085 0.5611 -0.0828 0.0496  0.0347  63  PRO B CB  
1623 C CG  . PRO B 63  ? 0.5046 0.4159 0.5766 -0.0751 0.0443  0.0291  63  PRO B CG  
1624 C CD  . PRO B 63  ? 0.4930 0.3602 0.5609 -0.0772 0.0449  0.0416  63  PRO B CD  
1625 N N   . LYS B 64  ? 0.4905 0.3474 0.5397 -0.0859 0.0420  0.0480  64  LYS B N   
1626 C CA  . LYS B 64  ? 0.4899 0.3514 0.5575 -0.0678 0.0289  0.0130  64  LYS B CA  
1627 C C   . LYS B 64  ? 0.4560 0.2861 0.5491 -0.0444 0.0305  0.0190  64  LYS B C   
1628 O O   . LYS B 64  ? 0.4720 0.2824 0.5845 -0.0128 0.0078  -0.0418 64  LYS B O   
1629 C CB  . LYS B 64  ? 0.5675 0.3713 0.6080 -0.0196 0.0239  0.0107  64  LYS B CB  
1630 C CG  . LYS B 64  ? 0.6745 0.4285 0.6712 0.0085  0.0195  -0.0170 64  LYS B CG  
1631 C CD  . LYS B 64  ? 0.7519 0.4404 0.7233 0.0346  0.0110  -0.0401 64  LYS B CD  
1632 C CE  . LYS B 64  ? 0.8346 0.4992 0.7568 0.0220  -0.0007 -0.0552 64  LYS B CE  
1633 N NZ  . LYS B 64  ? 0.8679 0.4872 0.7814 0.0120  -0.0124 -0.0679 64  LYS B NZ  
1634 N N   . GLY B 65  ? 0.4078 0.2376 0.5079 -0.0679 0.0300  0.0547  65  GLY B N   
1635 C CA  . GLY B 65  ? 0.3896 0.2385 0.5063 -0.0393 0.0299  0.0466  65  GLY B CA  
1636 C C   . GLY B 65  ? 0.3745 0.2730 0.5153 -0.0353 0.0203  0.0250  65  GLY B C   
1637 O O   . GLY B 65  ? 0.4356 0.2692 0.5176 -0.0429 0.0184  0.0172  65  GLY B O   
1638 N N   . SER B 66  ? 0.3709 0.2120 0.5114 0.0117  -0.0030 0.0185  66  SER B N   
1639 C CA  . SER B 66  ? 0.3702 0.2033 0.4978 0.0027  0.0067  0.0385  66  SER B CA  
1640 C C   . SER B 66  ? 0.3640 0.2276 0.5044 0.0046  0.0128  0.0248  66  SER B C   
1641 O O   . SER B 66  ? 0.3701 0.2299 0.5183 0.0067  0.0003  0.0497  66  SER B O   
1642 C CB  . SER B 66  ? 0.3962 0.2270 0.4909 0.0124  0.0063  0.0229  66  SER B CB  
1643 O OG  . SER B 66  ? 0.3971 0.2032 0.4675 0.0016  0.0059  0.0240  66  SER B OG  
1644 N N   . LYS B 67  ? 0.3876 0.2230 0.5707 -0.0429 0.0130  0.0335  67  LYS B N   
1645 C CA  . LYS B 67  ? 0.3889 0.2259 0.6343 -0.0448 0.0152  0.0094  67  LYS B CA  
1646 C C   . LYS B 67  ? 0.4081 0.2308 0.5986 -0.0327 0.0201  -0.0012 67  LYS B C   
1647 O O   . LYS B 67  ? 0.4005 0.1978 0.5756 -0.0331 0.0042  -0.0080 67  LYS B O   
1648 C CB  . LYS B 67  ? 0.4522 0.2155 0.6979 -0.0408 -0.0041 0.0290  67  LYS B CB  
1649 C CG  . LYS B 67  ? 0.5356 0.2607 0.7587 -0.0484 0.0087  0.0263  67  LYS B CG  
1650 C CD  . LYS B 67  ? 0.6302 0.2799 0.8375 -0.0697 -0.0009 0.0132  67  LYS B CD  
1651 C CE  . LYS B 67  ? 0.6770 0.3857 0.8889 -0.0762 0.0226  0.0224  67  LYS B CE  
1652 N NZ  . LYS B 67  ? 0.7447 0.3863 0.9321 -0.0730 0.0219  0.0224  67  LYS B NZ  
1653 N N   . GLU B 68  ? 0.3870 0.2367 0.5624 -0.0487 0.0333  -0.0090 68  GLU B N   
1654 C CA  . GLU B 68  ? 0.4353 0.2530 0.5534 -0.0379 0.0341  -0.0170 68  GLU B CA  
1655 C C   . GLU B 68  ? 0.4075 0.2157 0.5040 -0.0068 0.0334  -0.0022 68  GLU B C   
1656 O O   . GLU B 68  ? 0.4159 0.2414 0.5484 -0.0048 0.0326  -0.0306 68  GLU B O   
1657 C CB  . GLU B 68  ? 0.5020 0.3038 0.5675 -0.0480 0.0187  -0.0274 68  GLU B CB  
1658 C CG  . GLU B 68  ? 0.5933 0.3544 0.6383 -0.0655 0.0016  -0.0575 68  GLU B CG  
1659 C CD  . GLU B 68  ? 0.6587 0.4198 0.6708 -0.0646 0.0120  -0.0508 68  GLU B CD  
1660 O OE1 . GLU B 68  ? 0.6330 0.3279 0.6157 -0.0614 -0.0431 -0.0669 68  GLU B OE1 
1661 O OE2 . GLU B 68  ? 0.7438 0.5028 0.7626 -0.1093 0.0030  -0.0984 68  GLU B OE2 
1662 N N   . GLU B 69  ? 0.3950 0.2007 0.4936 -0.0064 0.0089  0.0135  69  GLU B N   
1663 C CA  . GLU B 69  ? 0.3935 0.1748 0.4755 -0.0193 0.0021  0.0429  69  GLU B CA  
1664 C C   . GLU B 69  ? 0.3902 0.1772 0.5117 -0.0212 0.0020  0.0354  69  GLU B C   
1665 O O   . GLU B 69  ? 0.3415 0.1383 0.5140 -0.0043 -0.0160 0.0286  69  GLU B O   
1666 C CB  . GLU B 69  ? 0.3996 0.1303 0.4899 -0.0214 -0.0215 0.0521  69  GLU B CB  
1667 C CG  . GLU B 69  ? 0.3868 0.1727 0.5082 -0.0194 -0.0240 0.0424  69  GLU B CG  
1668 C CD  . GLU B 69  ? 0.4109 0.1849 0.5262 -0.0085 -0.0214 0.0747  69  GLU B CD  
1669 O OE1 . GLU B 69  ? 0.3918 0.2253 0.5614 -0.0168 0.0175  0.0664  69  GLU B OE1 
1670 O OE2 . GLU B 69  ? 0.4265 0.2714 0.5820 0.0491  -0.0313 0.0975  69  GLU B OE2 
1671 N N   . GLN B 70  ? 0.3926 0.1621 0.4822 -0.0125 -0.0033 0.0356  70  GLN B N   
1672 C CA  . GLN B 70  ? 0.4014 0.1608 0.5005 -0.0184 -0.0140 0.0378  70  GLN B CA  
1673 C C   . GLN B 70  ? 0.3797 0.1749 0.5123 -0.0270 -0.0220 0.0284  70  GLN B C   
1674 O O   . GLN B 70  ? 0.3876 0.1582 0.5232 -0.0276 -0.0486 0.0543  70  GLN B O   
1675 C CB  . GLN B 70  ? 0.4376 0.1528 0.5194 -0.0401 -0.0158 0.0402  70  GLN B CB  
1676 C CG  . GLN B 70  ? 0.4510 0.2347 0.5352 -0.0464 -0.0033 0.0480  70  GLN B CG  
1677 C CD  . GLN B 70  ? 0.5443 0.2499 0.5715 -0.0348 0.0172  0.0732  70  GLN B CD  
1678 O OE1 . GLN B 70  ? 0.5954 0.2191 0.7049 -0.0524 0.0699  0.0534  70  GLN B OE1 
1679 N NE2 . GLN B 70  ? 0.5457 0.2000 0.5719 -0.0362 0.0375  0.1342  70  GLN B NE2 
1680 N N   . ARG B 71  ? 0.4020 0.1516 0.5456 -0.0059 -0.0009 -0.0052 71  ARG B N   
1681 C CA  . ARG B 71  ? 0.3971 0.1974 0.5328 0.0090  -0.0093 0.0140  71  ARG B CA  
1682 C C   . ARG B 71  ? 0.3866 0.1931 0.4654 0.0185  -0.0216 0.0275  71  ARG B C   
1683 O O   . ARG B 71  ? 0.3850 0.1855 0.4326 0.0038  -0.0117 0.0495  71  ARG B O   
1684 C CB  . ARG B 71  ? 0.4681 0.2671 0.5987 -0.0079 -0.0160 -0.0280 71  ARG B CB  
1685 C CG  . ARG B 71  ? 0.5613 0.3399 0.6964 -0.0278 -0.0189 -0.0103 71  ARG B CG  
1686 C CD  . ARG B 71  ? 0.6818 0.4370 0.7442 -0.0379 -0.0218 -0.0249 71  ARG B CD  
1687 N NE  . ARG B 71  ? 0.7660 0.5378 0.8153 -0.0732 -0.0034 0.0182  71  ARG B NE  
1688 C CZ  . ARG B 71  ? 0.8205 0.5443 0.8290 -0.0609 -0.0205 0.0549  71  ARG B CZ  
1689 N NH1 . ARG B 71  ? 0.8546 0.4673 0.8407 -0.0489 -0.0056 0.0571  71  ARG B NH1 
1690 N NH2 . ARG B 71  ? 0.8745 0.6132 0.8830 -0.0883 0.0107  0.0443  71  ARG B NH2 
1691 N N   . ASP B 72  ? 0.3845 0.1858 0.4541 0.0196  -0.0306 0.0222  72  ASP B N   
1692 C CA  . ASP B 72  ? 0.4102 0.1833 0.4460 0.0173  -0.0313 0.0475  72  ASP B CA  
1693 C C   . ASP B 72  ? 0.3738 0.1817 0.4044 0.0209  -0.0070 0.0507  72  ASP B C   
1694 O O   . ASP B 72  ? 0.3861 0.1883 0.3856 0.0114  0.0089  0.0623  72  ASP B O   
1695 C CB  . ASP B 72  ? 0.4497 0.2505 0.4602 0.0218  -0.0635 0.0636  72  ASP B CB  
1696 C CG  . ASP B 72  ? 0.5309 0.3146 0.4846 0.0186  -0.0698 0.0556  72  ASP B CG  
1697 O OD1 . ASP B 72  ? 0.6240 0.3962 0.5509 0.0365  -0.0761 -0.0074 72  ASP B OD1 
1698 O OD2 . ASP B 72  ? 0.5635 0.4236 0.5611 0.0569  -0.0870 0.0392  72  ASP B OD2 
1699 N N   . TYR B 73  ? 0.3713 0.1399 0.3999 -0.0014 -0.0009 0.0414  73  TYR B N   
1700 C CA  . TYR B 73  ? 0.3675 0.1354 0.3896 -0.0180 0.0068  0.0336  73  TYR B CA  
1701 C C   . TYR B 73  ? 0.3667 0.1112 0.3713 -0.0127 0.0075  0.0008  73  TYR B C   
1702 O O   . TYR B 73  ? 0.3618 0.1274 0.3597 -0.0027 0.0133  0.0199  73  TYR B O   
1703 C CB  . TYR B 73  ? 0.3947 0.1285 0.4017 -0.0155 0.0206  0.0332  73  TYR B CB  
1704 C CG  . TYR B 73  ? 0.3955 0.1395 0.4194 -0.0082 0.0146  0.0399  73  TYR B CG  
1705 C CD1 . TYR B 73  ? 0.3802 0.1166 0.4188 0.0045  0.0068  0.0262  73  TYR B CD1 
1706 C CD2 . TYR B 73  ? 0.3885 0.1389 0.4511 0.0152  0.0145  0.0532  73  TYR B CD2 
1707 C CE1 . TYR B 73  ? 0.3766 0.1352 0.4209 -0.0057 0.0156  0.0482  73  TYR B CE1 
1708 C CE2 . TYR B 73  ? 0.3873 0.1603 0.4408 0.0262  0.0088  0.0340  73  TYR B CE2 
1709 C CZ  . TYR B 73  ? 0.3682 0.1630 0.4352 0.0009  0.0086  0.0360  73  TYR B CZ  
1710 O OH  . TYR B 73  ? 0.3347 0.1804 0.4970 -0.0003 0.0247  0.0202  73  TYR B OH  
1711 N N   . VAL B 74  ? 0.3721 0.1137 0.3553 -0.0212 -0.0093 0.0172  74  VAL B N   
1712 C CA  . VAL B 74  ? 0.3823 0.1308 0.3725 -0.0193 -0.0160 0.0074  74  VAL B CA  
1713 C C   . VAL B 74  ? 0.3817 0.1013 0.3434 -0.0150 -0.0186 0.0003  74  VAL B C   
1714 O O   . VAL B 74  ? 0.3792 0.1350 0.3339 0.0158  -0.0148 -0.0021 74  VAL B O   
1715 C CB  . VAL B 74  ? 0.4112 0.1581 0.3908 -0.0445 -0.0091 0.0372  74  VAL B CB  
1716 C CG1 . VAL B 74  ? 0.4207 0.1624 0.4091 -0.0482 0.0016  0.0368  74  VAL B CG1 
1717 C CG2 . VAL B 74  ? 0.4135 0.1203 0.4066 -0.0396 -0.0156 0.0739  74  VAL B CG2 
1718 N N   . PHE B 75  ? 0.3533 0.1190 0.3450 0.0059  -0.0070 -0.0018 75  PHE B N   
1719 C CA  . PHE B 75  ? 0.3667 0.1333 0.3187 0.0122  -0.0048 0.0045  75  PHE B CA  
1720 C C   . PHE B 75  ? 0.3229 0.1139 0.3104 0.0244  0.0029  0.0004  75  PHE B C   
1721 O O   . PHE B 75  ? 0.3270 0.0937 0.3129 -0.0041 -0.0022 0.0050  75  PHE B O   
1722 C CB  . PHE B 75  ? 0.3887 0.1515 0.3324 0.0395  -0.0286 0.0068  75  PHE B CB  
1723 C CG  . PHE B 75  ? 0.4118 0.1419 0.3161 0.0441  -0.0128 0.0065  75  PHE B CG  
1724 C CD1 . PHE B 75  ? 0.4444 0.1456 0.3543 0.0501  0.0052  0.0157  75  PHE B CD1 
1725 C CD2 . PHE B 75  ? 0.4337 0.1134 0.3487 0.0619  -0.0071 -0.0054 75  PHE B CD2 
1726 C CE1 . PHE B 75  ? 0.4639 0.1379 0.3550 0.0808  0.0096  -0.0274 75  PHE B CE1 
1727 C CE2 . PHE B 75  ? 0.4427 0.1555 0.3766 0.0611  -0.0025 -0.0160 75  PHE B CE2 
1728 C CZ  . PHE B 75  ? 0.4593 0.1667 0.3713 0.0737  0.0084  -0.0030 75  PHE B CZ  
1729 N N   . TYR B 76  ? 0.3178 0.1276 0.3195 0.0272  0.0034  0.0153  76  TYR B N   
1730 C CA  . TYR B 76  ? 0.3482 0.1198 0.3119 0.0284  -0.0013 0.0092  76  TYR B CA  
1731 C C   . TYR B 76  ? 0.3539 0.1393 0.3190 0.0253  0.0116  0.0240  76  TYR B C   
1732 O O   . TYR B 76  ? 0.3727 0.1227 0.3119 0.0073  -0.0010 0.0216  76  TYR B O   
1733 C CB  . TYR B 76  ? 0.3433 0.1242 0.2923 0.0244  -0.0085 0.0053  76  TYR B CB  
1734 C CG  . TYR B 76  ? 0.3797 0.1357 0.2980 0.0176  0.0036  0.0267  76  TYR B CG  
1735 C CD1 . TYR B 76  ? 0.4003 0.1681 0.3210 0.0069  0.0097  0.0247  76  TYR B CD1 
1736 C CD2 . TYR B 76  ? 0.3931 0.0993 0.3096 0.0249  0.0064  0.0120  76  TYR B CD2 
1737 C CE1 . TYR B 76  ? 0.4126 0.2111 0.3151 0.0241  0.0160  0.0307  76  TYR B CE1 
1738 C CE2 . TYR B 76  ? 0.4205 0.1770 0.3215 0.0382  0.0109  0.0069  76  TYR B CE2 
1739 C CZ  . TYR B 76  ? 0.4147 0.1949 0.3280 0.0435  0.0122  0.0115  76  TYR B CZ  
1740 O OH  . TYR B 76  ? 0.4918 0.2479 0.3614 0.0892  0.0321  0.0084  76  TYR B OH  
1741 N N   . LEU B 77  ? 0.3908 0.1083 0.3241 0.0174  0.0180  0.0435  77  LEU B N   
1742 C CA  . LEU B 77  ? 0.3756 0.1441 0.3303 0.0026  0.0193  0.0157  77  LEU B CA  
1743 C C   . LEU B 77  ? 0.3719 0.1310 0.2981 0.0108  0.0011  0.0032  77  LEU B C   
1744 O O   . LEU B 77  ? 0.3792 0.1274 0.3106 -0.0074 -0.0014 0.0093  77  LEU B O   
1745 C CB  . LEU B 77  ? 0.3690 0.1248 0.3432 -0.0087 0.0224  0.0152  77  LEU B CB  
1746 C CG  . LEU B 77  ? 0.3773 0.1198 0.3566 0.0076  0.0236  0.0257  77  LEU B CG  
1747 C CD1 . LEU B 77  ? 0.3787 0.1582 0.3675 0.0170  0.0343  0.0152  77  LEU B CD1 
1748 C CD2 . LEU B 77  ? 0.4055 0.1630 0.3651 0.0211  0.0041  0.0169  77  LEU B CD2 
1749 N N   . ALA B 78  ? 0.3584 0.1042 0.3058 0.0058  -0.0051 0.0149  78  ALA B N   
1750 C CA  . ALA B 78  ? 0.3821 0.1095 0.3086 0.0364  0.0000  0.0019  78  ALA B CA  
1751 C C   . ALA B 78  ? 0.3603 0.1184 0.2986 0.0414  -0.0055 -0.0106 78  ALA B C   
1752 O O   . ALA B 78  ? 0.3591 0.1310 0.3083 0.0294  -0.0034 0.0134  78  ALA B O   
1753 C CB  . ALA B 78  ? 0.4185 0.1161 0.3374 0.0323  -0.0195 -0.0096 78  ALA B CB  
1754 N N   . VAL B 79  ? 0.3366 0.1571 0.2872 0.0177  0.0041  0.0117  79  VAL B N   
1755 C CA  . VAL B 79  ? 0.3483 0.1567 0.2843 0.0091  0.0111  -0.0021 79  VAL B CA  
1756 C C   . VAL B 79  ? 0.3518 0.1329 0.2892 0.0148  0.0101  0.0008  79  VAL B C   
1757 O O   . VAL B 79  ? 0.3881 0.1016 0.3179 0.0133  -0.0071 0.0152  79  VAL B O   
1758 C CB  . VAL B 79  ? 0.3591 0.1489 0.2865 0.0007  0.0219  0.0007  79  VAL B CB  
1759 C CG1 . VAL B 79  ? 0.3825 0.1547 0.3079 -0.0052 0.0281  0.0125  79  VAL B CG1 
1760 C CG2 . VAL B 79  ? 0.3750 0.1714 0.2833 0.0008  0.0086  -0.0079 79  VAL B CG2 
1761 N N   . GLY B 80  ? 0.3402 0.1031 0.2992 -0.0008 0.0011  -0.0007 80  GLY B N   
1762 C CA  . GLY B 80  ? 0.3598 0.1171 0.3003 0.0124  -0.0007 -0.0189 80  GLY B CA  
1763 C C   . GLY B 80  ? 0.3816 0.1492 0.3030 -0.0026 -0.0249 -0.0167 80  GLY B C   
1764 O O   . GLY B 80  ? 0.3950 0.1269 0.3287 -0.0068 -0.0357 -0.0223 80  GLY B O   
1765 N N   . ASN B 81  ? 0.3913 0.1699 0.2966 -0.0008 -0.0303 -0.0063 81  ASN B N   
1766 C CA  . ASN B 81  ? 0.3875 0.1577 0.3095 0.0065  -0.0218 0.0082  81  ASN B CA  
1767 C C   . ASN B 81  ? 0.3858 0.1395 0.3107 0.0100  -0.0284 0.0092  81  ASN B C   
1768 O O   . ASN B 81  ? 0.4011 0.1858 0.3236 0.0191  -0.0353 -0.0039 81  ASN B O   
1769 C CB  . ASN B 81  ? 0.4123 0.1526 0.2974 0.0230  -0.0231 0.0339  81  ASN B CB  
1770 C CG  . ASN B 81  ? 0.4173 0.1764 0.3116 0.0210  -0.0128 0.0364  81  ASN B CG  
1771 O OD1 . ASN B 81  ? 0.4591 0.2031 0.3509 0.0114  -0.0178 0.0064  81  ASN B OD1 
1772 N ND2 . ASN B 81  ? 0.4165 0.2153 0.3005 0.0293  -0.0065 0.0261  81  ASN B ND2 
1773 N N   . TYR B 82  ? 0.3775 0.1433 0.3298 0.0093  -0.0234 0.0153  82  TYR B N   
1774 C CA  . TYR B 82  ? 0.3852 0.1248 0.3359 0.0179  -0.0272 0.0051  82  TYR B CA  
1775 C C   . TYR B 82  ? 0.3546 0.1336 0.3475 0.0206  -0.0305 -0.0191 82  TYR B C   
1776 O O   . TYR B 82  ? 0.3461 0.1789 0.3745 0.0162  -0.0307 -0.0420 82  TYR B O   
1777 C CB  . TYR B 82  ? 0.4036 0.1193 0.3385 0.0217  -0.0373 0.0026  82  TYR B CB  
1778 C CG  . TYR B 82  ? 0.4207 0.1367 0.3548 0.0183  -0.0243 0.0101  82  TYR B CG  
1779 C CD1 . TYR B 82  ? 0.4280 0.1317 0.3769 0.0084  -0.0263 0.0159  82  TYR B CD1 
1780 C CD2 . TYR B 82  ? 0.4436 0.2054 0.3674 0.0232  -0.0096 0.0273  82  TYR B CD2 
1781 C CE1 . TYR B 82  ? 0.4168 0.1646 0.3953 0.0041  -0.0238 0.0152  82  TYR B CE1 
1782 C CE2 . TYR B 82  ? 0.4403 0.2180 0.3651 0.0470  -0.0104 0.0253  82  TYR B CE2 
1783 C CZ  . TYR B 82  ? 0.4321 0.1989 0.3761 0.0438  -0.0120 0.0132  82  TYR B CZ  
1784 O OH  . TYR B 82  ? 0.4649 0.3110 0.4111 0.0586  0.0083  0.0076  82  TYR B OH  
1785 N N   . ARG B 83  ? 0.3152 0.1398 0.3607 0.0088  -0.0235 -0.0137 83  ARG B N   
1786 C CA  . ARG B 83  ? 0.3485 0.1341 0.3562 -0.0063 -0.0146 -0.0071 83  ARG B CA  
1787 C C   . ARG B 83  ? 0.3785 0.1255 0.3733 -0.0188 -0.0413 0.0064  83  ARG B C   
1788 O O   . ARG B 83  ? 0.3794 0.1888 0.4063 -0.0305 -0.0348 -0.0063 83  ARG B O   
1789 C CB  . ARG B 83  ? 0.3405 0.1200 0.3624 -0.0127 -0.0093 -0.0041 83  ARG B CB  
1790 C CG  . ARG B 83  ? 0.3484 0.1250 0.3683 0.0071  -0.0038 -0.0068 83  ARG B CG  
1791 C CD  . ARG B 83  ? 0.3784 0.1560 0.3822 0.0185  -0.0084 0.0028  83  ARG B CD  
1792 N NE  . ARG B 83  ? 0.3797 0.1596 0.4089 0.0193  0.0066  0.0068  83  ARG B NE  
1793 C CZ  . ARG B 83  ? 0.4003 0.1651 0.3917 0.0220  -0.0226 0.0248  83  ARG B CZ  
1794 N NH1 . ARG B 83  ? 0.4158 0.1628 0.3497 0.0428  -0.0275 0.0109  83  ARG B NH1 
1795 N NH2 . ARG B 83  ? 0.4298 0.1656 0.4439 0.0147  -0.0172 0.0414  83  ARG B NH2 
1796 N N   . LEU B 84  ? 0.3977 0.1406 0.3713 -0.0134 -0.0458 -0.0084 84  LEU B N   
1797 C CA  . LEU B 84  ? 0.4451 0.1617 0.3760 -0.0042 -0.0467 -0.0170 84  LEU B CA  
1798 C C   . LEU B 84  ? 0.4488 0.1818 0.3711 -0.0131 -0.0514 -0.0154 84  LEU B C   
1799 O O   . LEU B 84  ? 0.4870 0.2375 0.3816 0.0350  -0.0717 -0.0268 84  LEU B O   
1800 C CB  . LEU B 84  ? 0.4533 0.1653 0.3926 0.0083  -0.0391 -0.0007 84  LEU B CB  
1801 C CG  . LEU B 84  ? 0.4724 0.1771 0.3802 0.0177  -0.0320 -0.0043 84  LEU B CG  
1802 C CD1 . LEU B 84  ? 0.4664 0.2210 0.4355 0.0044  -0.0350 -0.0204 84  LEU B CD1 
1803 C CD2 . LEU B 84  ? 0.5022 0.1750 0.3363 0.0048  -0.0403 -0.0020 84  LEU B CD2 
1804 N N   . LYS B 85  ? 0.4520 0.1825 0.3905 0.0212  -0.0607 -0.0155 85  LYS B N   
1805 C CA  . LYS B 85  ? 0.4743 0.1799 0.4022 -0.0004 -0.0967 -0.0078 85  LYS B CA  
1806 C C   . LYS B 85  ? 0.4768 0.1899 0.3794 0.0082  -0.1135 -0.0014 85  LYS B C   
1807 O O   . LYS B 85  ? 0.5398 0.2543 0.4382 0.0098  -0.1337 0.0625  85  LYS B O   
1808 C CB  . LYS B 85  ? 0.4771 0.1983 0.4207 -0.0082 -0.1044 -0.0043 85  LYS B CB  
1809 C CG  . LYS B 85  ? 0.5019 0.2166 0.4879 -0.0132 -0.0941 0.0125  85  LYS B CG  
1810 C CD  . LYS B 85  ? 0.5148 0.2610 0.5538 -0.0278 -0.0856 0.0436  85  LYS B CD  
1811 C CE  . LYS B 85  ? 0.5590 0.3277 0.6136 -0.0409 -0.0625 0.0625  85  LYS B CE  
1812 N NZ  . LYS B 85  ? 0.5762 0.3903 0.6550 -0.0503 -0.0545 0.0463  85  LYS B NZ  
1813 N N   . GLU B 86  ? 0.4840 0.1835 0.3888 0.0286  -0.0937 0.0010  86  GLU B N   
1814 C CA  . GLU B 86  ? 0.5187 0.2033 0.3946 0.0121  -0.0770 0.0015  86  GLU B CA  
1815 C C   . GLU B 86  ? 0.4726 0.1954 0.3873 0.0026  -0.0647 -0.0121 86  GLU B C   
1816 O O   . GLU B 86  ? 0.4524 0.1826 0.3839 0.0053  -0.0475 -0.0165 86  GLU B O   
1817 C CB  . GLU B 86  ? 0.5751 0.2397 0.4306 0.0167  -0.0405 0.0081  86  GLU B CB  
1818 C CG  . GLU B 86  ? 0.6418 0.2356 0.4912 0.0137  -0.0321 -0.0062 86  GLU B CG  
1819 C CD  . GLU B 86  ? 0.7472 0.3057 0.5233 0.0159  -0.0185 -0.0245 86  GLU B CD  
1820 O OE1 . GLU B 86  ? 0.8131 0.3265 0.5961 -0.0050 -0.0875 -0.0306 86  GLU B OE1 
1821 O OE2 . GLU B 86  ? 0.8237 0.3079 0.6640 0.0283  0.0195  -0.0640 86  GLU B OE2 
1822 N N   . TYR B 87  ? 0.4647 0.1953 0.3974 -0.0087 -0.0897 -0.0139 87  TYR B N   
1823 C CA  . TYR B 87  ? 0.4703 0.1713 0.4055 -0.0009 -0.0772 0.0011  87  TYR B CA  
1824 C C   . TYR B 87  ? 0.4388 0.2193 0.3750 0.0063  -0.0845 0.0101  87  TYR B C   
1825 O O   . TYR B 87  ? 0.4140 0.1568 0.3738 -0.0003 -0.0602 0.0000  87  TYR B O   
1826 C CB  . TYR B 87  ? 0.4887 0.1628 0.4308 0.0205  -0.0565 0.0017  87  TYR B CB  
1827 C CG  . TYR B 87  ? 0.4499 0.2319 0.4422 0.0131  -0.0510 -0.0241 87  TYR B CG  
1828 C CD1 . TYR B 87  ? 0.4582 0.1949 0.4361 -0.0063 -0.0346 -0.0209 87  TYR B CD1 
1829 C CD2 . TYR B 87  ? 0.4510 0.2400 0.4510 0.0111  -0.0550 -0.0375 87  TYR B CD2 
1830 C CE1 . TYR B 87  ? 0.4781 0.2098 0.4145 -0.0059 -0.0198 -0.0200 87  TYR B CE1 
1831 C CE2 . TYR B 87  ? 0.4597 0.2577 0.4589 0.0057  -0.0458 -0.0274 87  TYR B CE2 
1832 C CZ  . TYR B 87  ? 0.4710 0.2195 0.4385 0.0017  -0.0281 -0.0288 87  TYR B CZ  
1833 O OH  . TYR B 87  ? 0.5137 0.2719 0.5138 -0.0199 -0.0166 -0.0490 87  TYR B OH  
1834 N N   . GLU B 88  ? 0.4944 0.2389 0.4038 0.0048  -0.0777 -0.0053 88  GLU B N   
1835 C CA  . GLU B 88  ? 0.5203 0.2565 0.4222 -0.0035 -0.0711 0.0265  88  GLU B CA  
1836 C C   . GLU B 88  ? 0.5008 0.1627 0.3897 -0.0034 -0.0585 0.0117  88  GLU B C   
1837 O O   . GLU B 88  ? 0.5081 0.2334 0.3775 -0.0349 -0.0567 0.0414  88  GLU B O   
1838 C CB  . GLU B 88  ? 0.5775 0.3360 0.4519 -0.0222 -0.0962 0.0332  88  GLU B CB  
1839 C CG  . GLU B 88  ? 0.6362 0.4010 0.5322 -0.0065 -0.1099 0.0289  88  GLU B CG  
1840 C CD  . GLU B 88  ? 0.7202 0.4483 0.6301 -0.0045 -0.1249 0.0351  88  GLU B CD  
1841 O OE1 . GLU B 88  ? 0.7559 0.6106 0.6870 -0.0385 -0.1300 0.0589  88  GLU B OE1 
1842 O OE2 . GLU B 88  ? 0.7548 0.5952 0.7494 0.0400  -0.1536 0.0482  88  GLU B OE2 
1843 N N   . LYS B 89  ? 0.4965 0.1484 0.3656 -0.0384 -0.0490 0.0052  89  LYS B N   
1844 C CA  . LYS B 89  ? 0.4947 0.1621 0.3818 -0.0383 -0.0298 0.0022  89  LYS B CA  
1845 C C   . LYS B 89  ? 0.4473 0.1610 0.3638 -0.0172 -0.0187 0.0162  89  LYS B C   
1846 O O   . LYS B 89  ? 0.4369 0.1351 0.3944 -0.0308 -0.0106 0.0409  89  LYS B O   
1847 C CB  . LYS B 89  ? 0.5762 0.1765 0.4386 -0.0394 -0.0322 -0.0344 89  LYS B CB  
1848 C CG  . LYS B 89  ? 0.6535 0.2858 0.4794 -0.0464 -0.0313 -0.0253 89  LYS B CG  
1849 C CD  . LYS B 89  ? 0.7189 0.3537 0.5681 -0.0275 -0.0291 -0.0650 89  LYS B CD  
1850 C CE  . LYS B 89  ? 0.7710 0.4159 0.6165 -0.0356 -0.0062 -0.0794 89  LYS B CE  
1851 N NZ  . LYS B 89  ? 0.8405 0.4613 0.6308 -0.0398 -0.0119 -0.0931 89  LYS B NZ  
1852 N N   . ALA B 90  ? 0.4416 0.1817 0.3657 -0.0129 -0.0110 0.0288  90  ALA B N   
1853 C CA  . ALA B 90  ? 0.4169 0.1377 0.3381 -0.0021 -0.0248 0.0112  90  ALA B CA  
1854 C C   . ALA B 90  ? 0.4500 0.1468 0.3364 -0.0100 -0.0466 0.0244  90  ALA B C   
1855 O O   . ALA B 90  ? 0.4294 0.1565 0.3259 -0.0279 -0.0297 0.0115  90  ALA B O   
1856 C CB  . ALA B 90  ? 0.4256 0.0991 0.3492 -0.0275 -0.0399 0.0175  90  ALA B CB  
1857 N N   . LEU B 91  ? 0.4521 0.1297 0.3540 -0.0112 -0.0491 0.0210  91  LEU B N   
1858 C CA  . LEU B 91  ? 0.4826 0.1328 0.3691 0.0153  -0.0677 0.0237  91  LEU B CA  
1859 C C   . LEU B 91  ? 0.4724 0.1342 0.3608 0.0123  -0.0880 0.0283  91  LEU B C   
1860 O O   . LEU B 91  ? 0.5133 0.1250 0.3901 0.0030  -0.1200 0.0040  91  LEU B O   
1861 C CB  . LEU B 91  ? 0.5071 0.1546 0.3949 0.0263  -0.0655 0.0644  91  LEU B CB  
1862 C CG  . LEU B 91  ? 0.5300 0.1913 0.4239 0.0327  -0.0533 0.0560  91  LEU B CG  
1863 C CD1 . LEU B 91  ? 0.5572 0.1990 0.4209 0.0763  -0.0586 0.0390  91  LEU B CD1 
1864 C CD2 . LEU B 91  ? 0.5159 0.2181 0.4484 0.0315  -0.0517 0.0672  91  LEU B CD2 
1865 N N   . LYS B 92  ? 0.4890 0.1603 0.3730 -0.0065 -0.0712 0.0321  92  LYS B N   
1866 C CA  . LYS B 92  ? 0.5233 0.1527 0.3995 -0.0057 -0.0446 0.0721  92  LYS B CA  
1867 C C   . LYS B 92  ? 0.5077 0.1264 0.3982 -0.0194 -0.0378 0.0762  92  LYS B C   
1868 O O   . LYS B 92  ? 0.4850 0.1671 0.4130 -0.0130 -0.0342 0.0613  92  LYS B O   
1869 C CB  . LYS B 92  ? 0.6008 0.2268 0.3919 -0.0179 -0.0446 0.0813  92  LYS B CB  
1870 C CG  . LYS B 92  ? 0.6607 0.3604 0.4379 0.0023  -0.0560 0.0713  92  LYS B CG  
1871 C CD  . LYS B 92  ? 0.7444 0.4586 0.4636 -0.0177 -0.0294 0.0457  92  LYS B CD  
1872 C CE  . LYS B 92  ? 0.7757 0.5325 0.4889 -0.0323 -0.0398 0.0447  92  LYS B CE  
1873 N NZ  . LYS B 92  ? 0.8117 0.6050 0.5454 -0.0579 -0.0209 0.0025  92  LYS B NZ  
1874 N N   . TYR B 93  ? 0.4994 0.1165 0.4117 -0.0439 -0.0341 0.0572  93  TYR B N   
1875 C CA  . TYR B 93  ? 0.4794 0.1054 0.4061 -0.0068 -0.0200 0.0499  93  TYR B CA  
1876 C C   . TYR B 93  ? 0.4252 0.1155 0.4000 0.0011  -0.0476 0.0460  93  TYR B C   
1877 O O   . TYR B 93  ? 0.3938 0.1376 0.4208 -0.0180 -0.0450 0.0464  93  TYR B O   
1878 C CB  . TYR B 93  ? 0.4767 0.1024 0.3834 -0.0107 -0.0013 0.0414  93  TYR B CB  
1879 C CG  . TYR B 93  ? 0.4858 0.1483 0.3725 -0.0115 0.0141  0.0305  93  TYR B CG  
1880 C CD1 . TYR B 93  ? 0.4955 0.1421 0.3543 -0.0189 0.0175  0.0112  93  TYR B CD1 
1881 C CD2 . TYR B 93  ? 0.5125 0.1573 0.3769 -0.0073 0.0073  0.0513  93  TYR B CD2 
1882 C CE1 . TYR B 93  ? 0.4962 0.1599 0.3918 0.0245  0.0359  0.0280  93  TYR B CE1 
1883 C CE2 . TYR B 93  ? 0.5227 0.1661 0.3870 0.0065  0.0148  0.0412  93  TYR B CE2 
1884 C CZ  . TYR B 93  ? 0.5321 0.1739 0.3865 0.0021  0.0448  0.0078  93  TYR B CZ  
1885 O OH  . TYR B 93  ? 0.6134 0.2260 0.4408 0.0035  0.0864  -0.0295 93  TYR B OH  
1886 N N   . VAL B 94  ? 0.4287 0.1145 0.4162 0.0061  -0.0446 0.0524  94  VAL B N   
1887 C CA  . VAL B 94  ? 0.4426 0.1398 0.4093 -0.0015 -0.0560 0.0316  94  VAL B CA  
1888 C C   . VAL B 94  ? 0.4468 0.1472 0.3973 -0.0198 -0.0808 0.0220  94  VAL B C   
1889 O O   . VAL B 94  ? 0.4527 0.1493 0.4404 -0.0026 -0.0793 -0.0126 94  VAL B O   
1890 C CB  . VAL B 94  ? 0.4499 0.1297 0.4078 0.0283  -0.0313 0.0051  94  VAL B CB  
1891 C CG1 . VAL B 94  ? 0.4643 0.1264 0.4293 0.0317  -0.0258 -0.0016 94  VAL B CG1 
1892 C CG2 . VAL B 94  ? 0.4606 0.1218 0.4095 0.0229  -0.0318 -0.0058 94  VAL B CG2 
1893 N N   . ARG B 95  ? 0.4456 0.1255 0.4245 -0.0808 -0.0891 0.0257  95  ARG B N   
1894 C CA  . ARG B 95  ? 0.4787 0.1278 0.4418 -0.0724 -0.0788 0.0250  95  ARG B CA  
1895 C C   . ARG B 95  ? 0.4588 0.1836 0.4475 -0.0544 -0.0548 0.0373  95  ARG B C   
1896 O O   . ARG B 95  ? 0.5040 0.1428 0.5321 -0.0450 -0.0683 0.0431  95  ARG B O   
1897 C CB  . ARG B 95  ? 0.5321 0.1399 0.4837 -0.0685 -0.0918 0.0636  95  ARG B CB  
1898 C CG  . ARG B 95  ? 0.5845 0.1972 0.5286 -0.0465 -0.0819 0.0559  95  ARG B CG  
1899 C CD  . ARG B 95  ? 0.6477 0.2476 0.5771 -0.0038 -0.1059 0.0714  95  ARG B CD  
1900 N NE  . ARG B 95  ? 0.7046 0.3555 0.6364 0.0280  -0.0850 0.0986  95  ARG B NE  
1901 C CZ  . ARG B 95  ? 0.7617 0.4298 0.6556 0.0316  -0.0968 0.1607  95  ARG B CZ  
1902 N NH1 . ARG B 95  ? 0.7810 0.4313 0.6711 -0.0177 -0.0650 0.1767  95  ARG B NH1 
1903 N NH2 . ARG B 95  ? 0.7829 0.4158 0.6863 0.0716  -0.0932 0.2032  95  ARG B NH2 
1904 N N   . GLY B 96  ? 0.4358 0.1785 0.4869 -0.0727 -0.0379 0.0245  96  GLY B N   
1905 C CA  . GLY B 96  ? 0.4409 0.1828 0.4782 -0.0537 -0.0290 0.0057  96  GLY B CA  
1906 C C   . GLY B 96  ? 0.4312 0.2087 0.4860 -0.0221 -0.0249 0.0339  96  GLY B C   
1907 O O   . GLY B 96  ? 0.4839 0.2208 0.4960 -0.0441 -0.0392 0.0397  96  GLY B O   
1908 N N   . LEU B 97  ? 0.4055 0.2030 0.4609 -0.0167 -0.0189 0.0245  97  LEU B N   
1909 C CA  . LEU B 97  ? 0.4232 0.2324 0.4703 -0.0419 -0.0307 0.0519  97  LEU B CA  
1910 C C   . LEU B 97  ? 0.4488 0.2765 0.4629 -0.0011 -0.0541 0.0391  97  LEU B C   
1911 O O   . LEU B 97  ? 0.4713 0.1795 0.4945 0.0149  -0.0862 0.0348  97  LEU B O   
1912 C CB  . LEU B 97  ? 0.4248 0.2190 0.4717 -0.0358 -0.0345 0.0533  97  LEU B CB  
1913 C CG  . LEU B 97  ? 0.4668 0.2188 0.4971 -0.0142 -0.0418 0.0467  97  LEU B CG  
1914 C CD1 . LEU B 97  ? 0.4893 0.1492 0.5028 0.0269  -0.0567 0.0624  97  LEU B CD1 
1915 C CD2 . LEU B 97  ? 0.5019 0.2472 0.4845 -0.0102 -0.0366 0.0669  97  LEU B CD2 
1916 N N   . LEU B 98  ? 0.4737 0.2235 0.4520 0.0199  -0.0502 -0.0140 98  LEU B N   
1917 C CA  . LEU B 98  ? 0.4883 0.2076 0.4947 -0.0199 -0.0402 -0.0188 98  LEU B CA  
1918 C C   . LEU B 98  ? 0.4760 0.2120 0.5181 -0.0321 -0.0593 -0.0280 98  LEU B C   
1919 O O   . LEU B 98  ? 0.5434 0.2273 0.5538 -0.0539 -0.0910 -0.0721 98  LEU B O   
1920 C CB  . LEU B 98  ? 0.4895 0.1444 0.5008 -0.0058 -0.0263 -0.0269 98  LEU B CB  
1921 C CG  . LEU B 98  ? 0.4973 0.1731 0.4960 0.0130  -0.0327 0.0148  98  LEU B CG  
1922 C CD1 . LEU B 98  ? 0.5075 0.2625 0.5209 -0.0049 -0.0528 -0.0106 98  LEU B CD1 
1923 C CD2 . LEU B 98  ? 0.5028 0.2017 0.5014 0.0120  -0.0405 0.0364  98  LEU B CD2 
1924 N N   . GLN B 99  ? 0.4810 0.2071 0.5275 -0.0526 -0.0607 0.0125  99  GLN B N   
1925 C CA  . GLN B 99  ? 0.4863 0.2394 0.5756 -0.0768 -0.0725 0.0046  99  GLN B CA  
1926 C C   . GLN B 99  ? 0.5073 0.2362 0.6098 -0.0833 -0.0888 0.0222  99  GLN B C   
1927 O O   . GLN B 99  ? 0.5605 0.1948 0.6085 -0.1078 -0.1308 0.0671  99  GLN B O   
1928 C CB  . GLN B 99  ? 0.5234 0.2422 0.5944 -0.0846 -0.0425 -0.0282 99  GLN B CB  
1929 C CG  . GLN B 99  ? 0.5441 0.1954 0.5684 -0.1113 -0.0475 -0.0284 99  GLN B CG  
1930 C CD  . GLN B 99  ? 0.6095 0.2907 0.5954 -0.0371 -0.0298 -0.0245 99  GLN B CD  
1931 O OE1 . GLN B 99  ? 0.6256 0.3431 0.5732 -0.0142 0.0119  -0.0150 99  GLN B OE1 
1932 N NE2 . GLN B 99  ? 0.6530 0.3408 0.5982 -0.0158 -0.0498 -0.0505 99  GLN B NE2 
1933 N N   . THR B 100 ? 0.5668 0.2688 0.6101 -0.0324 -0.0847 0.0445  100 THR B N   
1934 C CA  . THR B 100 ? 0.5724 0.2931 0.6452 -0.0392 -0.1002 0.0155  100 THR B CA  
1935 C C   . THR B 100 ? 0.6110 0.1841 0.6293 -0.0125 -0.1199 0.0266  100 THR B C   
1936 O O   . THR B 100 ? 0.6529 0.3056 0.6461 -0.0074 -0.1488 0.0277  100 THR B O   
1937 C CB  . THR B 100 ? 0.5981 0.3708 0.6828 0.0239  -0.0831 -0.0123 100 THR B CB  
1938 O OG1 . THR B 100 ? 0.6110 0.5118 0.7215 0.0082  -0.0658 -0.0238 100 THR B OG1 
1939 C CG2 . THR B 100 ? 0.6065 0.4621 0.7098 0.0005  -0.0991 -0.0178 100 THR B CG2 
1940 N N   . GLU B 101 ? 0.6511 0.2705 0.6220 0.0020  -0.1129 0.0220  101 GLU B N   
1941 C CA  . GLU B 101 ? 0.7208 0.2912 0.6246 -0.0182 -0.1197 -0.0001 101 GLU B CA  
1942 C C   . GLU B 101 ? 0.7319 0.1885 0.6213 -0.0509 -0.1155 -0.0452 101 GLU B C   
1943 O O   . GLU B 101 ? 0.7127 0.2878 0.5826 -0.0575 -0.1174 -0.0597 101 GLU B O   
1944 C CB  . GLU B 101 ? 0.7773 0.3387 0.6388 -0.0416 -0.1190 0.0443  101 GLU B CB  
1945 C CG  . GLU B 101 ? 0.8270 0.4178 0.6642 -0.0235 -0.1331 0.0644  101 GLU B CG  
1946 C CD  . GLU B 101 ? 0.8535 0.4590 0.6764 -0.0031 -0.1540 0.0905  101 GLU B CD  
1947 O OE1 . GLU B 101 ? 0.8348 0.3999 0.6786 0.0293  -0.1911 0.0787  101 GLU B OE1 
1948 O OE2 . GLU B 101 ? 0.9318 0.6470 0.6997 -0.0157 -0.1864 0.1011  101 GLU B OE2 
1949 N N   . PRO B 102 ? 0.7456 0.1810 0.6365 -0.0810 -0.0936 -0.0540 102 PRO B N   
1950 C CA  . PRO B 102 ? 0.7355 0.3037 0.6803 -0.0741 -0.0930 -0.0507 102 PRO B CA  
1951 C C   . PRO B 102 ? 0.7299 0.3347 0.7033 -0.1152 -0.0713 -0.0739 102 PRO B C   
1952 O O   . PRO B 102 ? 0.7346 0.3619 0.7331 -0.0985 -0.0274 -0.0854 102 PRO B O   
1953 C CB  . PRO B 102 ? 0.7438 0.2822 0.6803 -0.0482 -0.0748 -0.0288 102 PRO B CB  
1954 C CG  . PRO B 102 ? 0.7511 0.2208 0.6224 -0.0627 -0.0642 -0.0291 102 PRO B CG  
1955 C CD  . PRO B 102 ? 0.7273 0.2260 0.6472 -0.0897 -0.0961 -0.0307 102 PRO B CD  
1956 N N   . GLN B 103 ? 0.7903 0.3452 0.6952 -0.1132 -0.1095 -0.1203 103 GLN B N   
1957 C CA  . GLN B 103 ? 0.8294 0.5103 0.7321 -0.1124 -0.0873 -0.1371 103 GLN B CA  
1958 C C   . GLN B 103 ? 0.7474 0.4751 0.6632 -0.1057 -0.1789 -0.1925 103 GLN B C   
1959 O O   . GLN B 103 ? 1.2169 0.3480 0.9113 -0.0160 -0.0702 -0.1016 103 GLN B O   
1960 C CB  . GLN B 103 ? 0.8936 0.5708 0.7864 -0.1396 -0.1027 -0.1793 103 GLN B CB  
1961 C CG  . GLN B 103 ? 0.9638 0.6088 0.8758 -0.1545 -0.0595 -0.2014 103 GLN B CG  
1962 C CD  . GLN B 103 ? 0.9796 0.7130 0.9316 -0.1495 -0.0593 -0.2419 103 GLN B CD  
1963 O OE1 . GLN B 103 ? 1.0860 0.6068 0.9316 -0.1756 -0.0366 -0.3352 103 GLN B OE1 
1964 N NE2 . GLN B 103 ? 1.0003 0.7248 0.9704 -0.1226 -0.0085 -0.2322 103 GLN B NE2 
1965 N N   . ASN B 104 ? 0.6379 0.3853 0.5455 -0.0223 -0.0926 -0.0864 104 ASN B N   
1966 C CA  . ASN B 104 ? 0.6051 0.3107 0.4636 0.0163  -0.0725 -0.0729 104 ASN B CA  
1967 C C   . ASN B 104 ? 0.6296 0.2666 0.4420 0.0445  -0.0802 -0.0530 104 ASN B C   
1968 O O   . ASN B 104 ? 0.6135 0.2072 0.4237 0.0251  -0.0831 -0.0517 104 ASN B O   
1969 C CB  . ASN B 104 ? 0.5701 0.2946 0.4726 0.0021  -0.0536 -0.0583 104 ASN B CB  
1970 C CG  . ASN B 104 ? 0.5755 0.2981 0.4609 0.0105  -0.0215 -0.0731 104 ASN B CG  
1971 O OD1 . ASN B 104 ? 0.5781 0.2065 0.4418 -0.0106 -0.0237 -0.0550 104 ASN B OD1 
1972 N ND2 . ASN B 104 ? 0.6077 0.3140 0.5005 0.0191  -0.0297 -0.0986 104 ASN B ND2 
1973 N N   A ASN B 105 ? 0.6360 0.2375 0.4222 0.0585  -0.0822 -0.0536 105 ASN B N   
1974 N N   B ASN B 105 ? 0.6266 0.2580 0.4269 0.0542  -0.0804 -0.0499 105 ASN B N   
1975 C CA  A ASN B 105 ? 0.6318 0.2284 0.4135 0.0694  -0.1017 -0.0513 105 ASN B CA  
1976 C CA  B ASN B 105 ? 0.6182 0.2602 0.4220 0.0627  -0.0992 -0.0445 105 ASN B CA  
1977 C C   A ASN B 105 ? 0.5992 0.2147 0.3738 0.0737  -0.0968 -0.0563 105 ASN B C   
1978 C C   B ASN B 105 ? 0.5891 0.2325 0.3789 0.0768  -0.0960 -0.0517 105 ASN B C   
1979 O O   A ASN B 105 ? 0.6084 0.1890 0.3999 0.0724  -0.0887 -0.0629 105 ASN B O   
1980 O O   B ASN B 105 ? 0.5996 0.2220 0.4054 0.0752  -0.0909 -0.0577 105 ASN B O   
1981 C CB  A ASN B 105 ? 0.6687 0.2291 0.4158 0.0885  -0.1018 -0.0569 105 ASN B CB  
1982 C CB  B ASN B 105 ? 0.6468 0.2894 0.4278 0.0723  -0.0966 -0.0442 105 ASN B CB  
1983 C CG  A ASN B 105 ? 0.6975 0.2429 0.4321 0.0899  -0.1060 -0.0609 105 ASN B CG  
1984 C CG  B ASN B 105 ? 0.6599 0.3535 0.4539 0.0713  -0.0917 -0.0277 105 ASN B CG  
1985 O OD1 A ASN B 105 ? 0.7138 0.2482 0.4560 0.0810  -0.0998 -0.0249 105 ASN B OD1 
1986 O OD1 B ASN B 105 ? 0.6671 0.3767 0.4864 0.1188  -0.0714 -0.0329 105 ASN B OD1 
1987 N ND2 A ASN B 105 ? 0.7234 0.2987 0.4357 0.1128  -0.1068 -0.0551 105 ASN B ND2 
1988 N ND2 B ASN B 105 ? 0.6837 0.3495 0.4952 0.0517  -0.0824 -0.0113 105 ASN B ND2 
1989 N N   . GLN B 106 ? 0.5651 0.2222 0.3619 0.0550  -0.1084 -0.0540 106 GLN B N   
1990 C CA  . GLN B 106 ? 0.5399 0.2031 0.3937 0.0610  -0.0986 -0.0305 106 GLN B CA  
1991 C C   . GLN B 106 ? 0.4777 0.0902 0.3744 0.0422  -0.0909 -0.0283 106 GLN B C   
1992 O O   . GLN B 106 ? 0.4834 0.1294 0.3875 0.0344  -0.1065 -0.0174 106 GLN B O   
1993 C CB  . GLN B 106 ? 0.5413 0.1715 0.4014 0.0546  -0.0994 -0.0439 106 GLN B CB  
1994 C CG  . GLN B 106 ? 0.5909 0.2536 0.4199 0.0784  -0.0970 -0.0321 106 GLN B CG  
1995 C CD  . GLN B 106 ? 0.6368 0.3029 0.4473 0.0755  -0.1056 -0.0399 106 GLN B CD  
1996 O OE1 . GLN B 106 ? 0.6752 0.3308 0.5440 0.0942  -0.1204 0.0390  106 GLN B OE1 
1997 N NE2 . GLN B 106 ? 0.6893 0.3423 0.4687 0.0892  -0.0520 -0.0280 106 GLN B NE2 
1998 N N   . ALA B 107 ? 0.4808 0.1367 0.3748 0.0360  -0.0733 -0.0067 107 ALA B N   
1999 C CA  . ALA B 107 ? 0.4928 0.1340 0.3919 0.0275  -0.0752 -0.0237 107 ALA B CA  
2000 C C   . ALA B 107 ? 0.4681 0.1272 0.3638 0.0134  -0.0907 -0.0368 107 ALA B C   
2001 O O   . ALA B 107 ? 0.4806 0.1742 0.3778 -0.0108 -0.0945 -0.0230 107 ALA B O   
2002 C CB  . ALA B 107 ? 0.4955 0.2218 0.4078 0.0308  -0.0709 -0.0125 107 ALA B CB  
2003 N N   . LYS B 108 ? 0.4997 0.1378 0.3866 0.0323  -0.1063 -0.0515 108 LYS B N   
2004 C CA  . LYS B 108 ? 0.5288 0.1511 0.4412 0.0468  -0.0951 -0.0576 108 LYS B CA  
2005 C C   . LYS B 108 ? 0.5240 0.1810 0.4285 0.0655  -0.0863 -0.0630 108 LYS B C   
2006 O O   . LYS B 108 ? 0.5265 0.1803 0.4495 0.0952  -0.0925 -0.0787 108 LYS B O   
2007 C CB  . LYS B 108 ? 0.5607 0.1981 0.4752 0.0539  -0.1025 -0.0891 108 LYS B CB  
2008 C CG  . LYS B 108 ? 0.6267 0.2368 0.5381 0.0221  -0.0946 -0.0963 108 LYS B CG  
2009 C CD  . LYS B 108 ? 0.7113 0.2770 0.6188 0.0160  -0.0727 -0.1316 108 LYS B CD  
2010 C CE  . LYS B 108 ? 0.7821 0.3092 0.7049 -0.0139 -0.0670 -0.1148 108 LYS B CE  
2011 N NZ  . LYS B 108 ? 0.8137 0.3598 0.7764 -0.0650 -0.0692 -0.0827 108 LYS B NZ  
2012 N N   . GLU B 109 ? 0.5157 0.1517 0.3890 0.0658  -0.0803 -0.0716 109 GLU B N   
2013 C CA  . GLU B 109 ? 0.5174 0.1493 0.4284 0.0606  -0.0704 -0.0564 109 GLU B CA  
2014 C C   . GLU B 109 ? 0.4602 0.2114 0.3821 0.0557  -0.0682 -0.0401 109 GLU B C   
2015 O O   . GLU B 109 ? 0.4487 0.2255 0.3892 0.0093  -0.0615 -0.0228 109 GLU B O   
2016 C CB  . GLU B 109 ? 0.5817 0.2336 0.4108 0.0476  -0.0682 -0.0578 109 GLU B CB  
2017 C CG  . GLU B 109 ? 0.6985 0.3168 0.4588 0.0387  -0.0533 -0.0721 109 GLU B CG  
2018 C CD  . GLU B 109 ? 0.7892 0.3431 0.5101 0.0121  -0.0428 -0.0333 109 GLU B CD  
2019 O OE1 . GLU B 109 ? 0.8838 0.3795 0.6106 0.0656  -0.0370 0.0285  109 GLU B OE1 
2020 O OE2 . GLU B 109 ? 0.8809 0.4756 0.5252 -0.0348 -0.0371 -0.0248 109 GLU B OE2 
2021 N N   . LEU B 110 ? 0.4561 0.1703 0.3568 0.0507  -0.0511 -0.0196 110 LEU B N   
2022 C CA  . LEU B 110 ? 0.4564 0.1906 0.3679 0.0364  -0.0388 -0.0265 110 LEU B CA  
2023 C C   . LEU B 110 ? 0.4179 0.1757 0.3828 0.0136  -0.0655 -0.0315 110 LEU B C   
2024 O O   . LEU B 110 ? 0.3961 0.1566 0.4256 -0.0024 -0.0761 -0.0289 110 LEU B O   
2025 C CB  . LEU B 110 ? 0.4607 0.1638 0.3371 0.0532  -0.0384 0.0245  110 LEU B CB  
2026 C CG  . LEU B 110 ? 0.4762 0.1313 0.3772 0.0379  -0.0092 0.0206  110 LEU B CG  
2027 C CD1 . LEU B 110 ? 0.4725 0.1124 0.4030 0.0486  -0.0067 0.0068  110 LEU B CD1 
2028 C CD2 . LEU B 110 ? 0.4763 0.1816 0.3993 0.0281  0.0025  0.0166  110 LEU B CD2 
2029 N N   . GLU B 111 ? 0.4228 0.1702 0.3957 0.0234  -0.0557 -0.0105 111 GLU B N   
2030 C CA  . GLU B 111 ? 0.4312 0.1866 0.3791 -0.0021 -0.0578 -0.0163 111 GLU B CA  
2031 C C   . GLU B 111 ? 0.4349 0.1547 0.3997 0.0260  -0.0595 -0.0230 111 GLU B C   
2032 O O   . GLU B 111 ? 0.4414 0.1826 0.3803 0.0472  -0.0475 -0.0046 111 GLU B O   
2033 C CB  . GLU B 111 ? 0.4608 0.2029 0.3546 -0.0143 -0.0631 -0.0206 111 GLU B CB  
2034 C CG  . GLU B 111 ? 0.5083 0.2246 0.3669 -0.0173 -0.0536 -0.0066 111 GLU B CG  
2035 C CD  . GLU B 111 ? 0.6178 0.2577 0.3910 -0.0596 -0.0381 0.0493  111 GLU B CD  
2036 O OE1 . GLU B 111 ? 0.7072 0.4362 0.3779 -0.0651 0.0115  0.0317  111 GLU B OE1 
2037 O OE2 . GLU B 111 ? 0.7298 0.3348 0.5238 -0.0301 -0.0589 -0.0100 111 GLU B OE2 
2038 N N   . ARG B 112 ? 0.4389 0.1908 0.4236 0.0278  -0.0576 -0.0309 112 ARG B N   
2039 C CA  . ARG B 112 ? 0.4595 0.1987 0.4453 0.0124  -0.0523 -0.0406 112 ARG B CA  
2040 C C   . ARG B 112 ? 0.4213 0.2333 0.4395 0.0163  -0.0669 -0.0266 112 ARG B C   
2041 O O   . ARG B 112 ? 0.4237 0.2052 0.4542 0.0382  -0.0680 -0.0520 112 ARG B O   
2042 C CB  . ARG B 112 ? 0.5399 0.2946 0.4764 -0.0004 -0.0446 -0.0740 112 ARG B CB  
2043 C CG  . ARG B 112 ? 0.6251 0.3809 0.5232 0.0058  -0.0229 -0.0871 112 ARG B CG  
2044 C CD  . ARG B 112 ? 0.7384 0.4454 0.5557 0.0053  0.0023  -0.1128 112 ARG B CD  
2045 N NE  . ARG B 112 ? 0.8574 0.4929 0.6299 -0.0049 0.0314  -0.0916 112 ARG B NE  
2046 C CZ  . ARG B 112 ? 0.9744 0.5886 0.6858 -0.0093 0.0349  -0.0807 112 ARG B CZ  
2047 N NH1 . ARG B 112 ? 1.0233 0.6018 0.7600 -0.0092 0.0165  -0.0951 112 ARG B NH1 
2048 N NH2 . ARG B 112 ? 0.9976 0.6422 0.7250 -0.0220 0.0503  -0.0307 112 ARG B NH2 
2049 N N   . LEU B 113 ? 0.3883 0.2394 0.4288 0.0468  -0.0256 -0.0365 113 LEU B N   
2050 C CA  . LEU B 113 ? 0.3982 0.2260 0.4419 0.0417  -0.0121 0.0020  113 LEU B CA  
2051 C C   . LEU B 113 ? 0.3717 0.2051 0.4278 0.0340  -0.0298 -0.0004 113 LEU B C   
2052 O O   . LEU B 113 ? 0.3932 0.1921 0.4178 0.0020  -0.0079 -0.0246 113 LEU B O   
2053 C CB  . LEU B 113 ? 0.4154 0.2473 0.4774 0.0408  -0.0147 0.0242  113 LEU B CB  
2054 C CG  . LEU B 113 ? 0.4590 0.3020 0.5057 0.0529  0.0110  0.0146  113 LEU B CG  
2055 C CD1 . LEU B 113 ? 0.4944 0.2959 0.5257 0.0678  0.0222  -0.0066 113 LEU B CD1 
2056 C CD2 . LEU B 113 ? 0.4648 0.3608 0.5149 0.0408  0.0195  0.0310  113 LEU B CD2 
2057 N N   . ILE B 114 ? 0.3848 0.2183 0.3987 0.0112  -0.0375 -0.0288 114 ILE B N   
2058 C CA  . ILE B 114 ? 0.3785 0.2131 0.3980 0.0094  -0.0453 -0.0374 114 ILE B CA  
2059 C C   . ILE B 114 ? 0.3950 0.1892 0.4109 0.0049  -0.0586 -0.0331 114 ILE B C   
2060 O O   . ILE B 114 ? 0.4277 0.2338 0.4064 -0.0134 -0.0612 -0.0059 114 ILE B O   
2061 C CB  . ILE B 114 ? 0.3582 0.1932 0.3861 0.0060  -0.0462 -0.0282 114 ILE B CB  
2062 C CG1 . ILE B 114 ? 0.3771 0.1742 0.3873 0.0129  -0.0339 -0.0291 114 ILE B CG1 
2063 C CG2 . ILE B 114 ? 0.3631 0.2329 0.3952 -0.0212 -0.0378 -0.0467 114 ILE B CG2 
2064 C CD1 . ILE B 114 ? 0.3917 0.1571 0.3910 0.0127  -0.0297 -0.0343 114 ILE B CD1 
2065 N N   . ASP B 115 ? 0.4252 0.2197 0.4471 0.0325  -0.0699 -0.0685 115 ASP B N   
2066 C CA  . ASP B 115 ? 0.4655 0.2666 0.4794 0.0507  -0.0836 -0.0299 115 ASP B CA  
2067 C C   . ASP B 115 ? 0.4565 0.2422 0.4704 0.0691  -0.0787 -0.0458 115 ASP B C   
2068 O O   . ASP B 115 ? 0.4862 0.2827 0.4925 0.0493  -0.0918 0.0000  115 ASP B O   
2069 C CB  . ASP B 115 ? 0.5068 0.2580 0.5123 0.0771  -0.0885 -0.0188 115 ASP B CB  
2070 C CG  . ASP B 115 ? 0.5509 0.3396 0.5973 0.0973  -0.0611 0.0166  115 ASP B CG  
2071 O OD1 . ASP B 115 ? 0.6627 0.4619 0.6357 0.0759  0.0011  0.0214  115 ASP B OD1 
2072 O OD2 . ASP B 115 ? 0.5970 0.3447 0.6303 0.1150  -0.0746 0.0561  115 ASP B OD2 
2073 N N   . LYS B 116 ? 0.4457 0.2125 0.4784 0.0796  -0.0895 -0.0281 116 LYS B N   
2074 C CA  . LYS B 116 ? 0.4492 0.2407 0.4998 0.0850  -0.0829 -0.0467 116 LYS B CA  
2075 C C   . LYS B 116 ? 0.4294 0.2349 0.4751 0.0610  -0.0725 -0.0454 116 LYS B C   
2076 O O   . LYS B 116 ? 0.4091 0.1997 0.5073 0.0156  -0.0652 -0.0230 116 LYS B O   
2077 C CB  . LYS B 116 ? 0.5053 0.2673 0.5256 0.0929  -0.0524 -0.0708 116 LYS B CB  
2078 C CG  . LYS B 116 ? 0.5737 0.2944 0.5817 0.1060  -0.0404 -0.0868 116 LYS B CG  
2079 C CD  . LYS B 116 ? 0.6346 0.3790 0.6297 0.1122  -0.0314 -0.0450 116 LYS B CD  
2080 C CE  . LYS B 116 ? 0.7033 0.3011 0.7040 0.1318  -0.0164 -0.0235 116 LYS B CE  
2081 N NZ  . LYS B 116 ? 0.7154 0.4666 0.7558 0.1186  -0.0329 0.0179  116 LYS B NZ  
2082 N N   . ALA B 117 ? 0.3863 0.2408 0.4463 0.0416  -0.0843 -0.0615 117 ALA B N   
2083 C CA  . ALA B 117 ? 0.3924 0.2467 0.4349 0.0210  -0.0799 -0.0699 117 ALA B CA  
2084 C C   . ALA B 117 ? 0.4146 0.2426 0.4344 0.0214  -0.0796 -0.0759 117 ALA B C   
2085 O O   . ALA B 117 ? 0.3863 0.3094 0.4422 0.0159  -0.0764 -0.0590 117 ALA B O   
2086 C CB  . ALA B 117 ? 0.4017 0.2554 0.4221 0.0273  -0.0623 -0.0859 117 ALA B CB  
2087 N N   . MET B 118 ? 0.4025 0.3560 0.4299 0.0166  -0.0581 -0.0404 118 MET B N   
2088 C CA  . MET B 118 ? 0.4558 0.3331 0.4627 -0.0227 -0.0609 -0.0156 118 MET B CA  
2089 C C   . MET B 118 ? 0.4610 0.3371 0.4691 -0.0242 -0.0551 0.0356  118 MET B C   
2090 O O   . MET B 118 ? 0.4846 0.4663 0.4763 0.0128  -0.0538 0.0200  118 MET B O   
2091 C CB  . MET B 118 ? 0.4891 0.3710 0.4919 -0.0363 -0.0520 -0.0035 118 MET B CB  
2092 C CG  . MET B 118 ? 0.5398 0.3714 0.5450 -0.0310 -0.0440 -0.0014 118 MET B CG  
2093 S SD  . MET B 118 ? 0.6179 0.3413 0.6129 -0.0666 -0.0424 -0.0080 118 MET B SD  
2094 C CE  . MET B 118 ? 0.6310 0.4235 0.6122 -0.0356 -0.0509 0.0181  118 MET B CE  
2095 N N   . LYS B 119 ? 0.4463 0.3298 0.4684 -0.0163 -0.0583 0.0651  119 LYS B N   
2096 C CA  . LYS B 119 ? 0.4640 0.3236 0.5456 -0.0040 -0.0693 0.0536  119 LYS B CA  
2097 C C   . LYS B 119 ? 0.4440 0.2668 0.5203 0.0029  -0.0703 0.0303  119 LYS B C   
2098 O O   . LYS B 119 ? 0.4475 0.2372 0.5736 0.0378  -0.0711 0.0235  119 LYS B O   
2099 C CB  . LYS B 119 ? 0.4607 0.2653 0.6089 -0.0018 -0.0871 0.0698  119 LYS B CB  
2100 C CG  . LYS B 119 ? 0.5035 0.3171 0.6718 -0.0261 -0.1045 0.0712  119 LYS B CG  
2101 C CD  . LYS B 119 ? 0.5852 0.3821 0.7308 -0.0494 -0.1133 0.0456  119 LYS B CD  
2102 C CE  . LYS B 119 ? 0.6197 0.4671 0.7955 -0.0694 -0.1062 0.0472  119 LYS B CE  
2103 N NZ  . LYS B 119 ? 0.6457 0.4736 0.8412 -0.0749 -0.1090 0.0425  119 LYS B NZ  
2104 N N   . LYS B 120 ? 0.4374 0.2552 0.5262 0.0034  -0.0610 0.0117  120 LYS B N   
2105 C CA  . LYS B 120 ? 0.4452 0.2745 0.5196 -0.0024 -0.0609 0.0034  120 LYS B CA  
2106 C C   . LYS B 120 ? 0.4114 0.2025 0.5375 -0.0070 -0.0793 0.0022  120 LYS B C   
2107 O O   . LYS B 120 ? 0.4212 0.1852 0.5459 -0.0388 -0.0324 -0.0006 120 LYS B O   
2108 C CB  . LYS B 120 ? 0.4814 0.3153 0.5563 -0.0295 -0.0529 -0.0173 120 LYS B CB  
2109 C CG  . LYS B 120 ? 0.5067 0.4056 0.5631 -0.0187 -0.0267 -0.0405 120 LYS B CG  
2110 C CD  . LYS B 120 ? 0.5440 0.4222 0.5565 -0.0254 -0.0157 -0.0763 120 LYS B CD  
2111 C CE  . LYS B 120 ? 0.5585 0.4622 0.5603 -0.0128 0.0007  -0.0903 120 LYS B CE  
2112 N NZ  . LYS B 120 ? 0.5821 0.5255 0.5884 -0.0279 -0.0038 -0.0870 120 LYS B NZ  
2113 N N   . ASP B 121 ? 0.4565 0.2133 0.5304 -0.0149 -0.0794 -0.0299 121 ASP B N   
2114 C CA  . ASP B 121 ? 0.4607 0.2036 0.5239 0.0004  -0.0901 -0.0441 121 ASP B CA  
2115 C C   . ASP B 121 ? 0.4698 0.2370 0.4635 0.0113  -0.0779 -0.0404 121 ASP B C   
2116 O O   . ASP B 121 ? 0.5262 0.1520 0.4305 -0.0092 -0.0551 -0.0350 121 ASP B O   
2117 C CB  . ASP B 121 ? 0.5042 0.2116 0.5749 -0.0209 -0.1193 -0.0553 121 ASP B CB  
2118 C CG  . ASP B 121 ? 0.6135 0.3602 0.6090 0.0175  -0.1260 -0.0814 121 ASP B CG  
2119 O OD1 . ASP B 121 ? 0.6672 0.4397 0.7130 0.0603  -0.1475 -0.0403 121 ASP B OD1 
2120 O OD2 . ASP B 121 ? 0.7330 0.4724 0.6716 0.0561  -0.1336 -0.0478 121 ASP B OD2 
2121 N N   . GLY B 122 ? 0.4845 0.2808 0.4700 -0.0100 -0.0389 -0.0456 122 GLY B N   
2122 C CA  . GLY B 122 ? 0.5170 0.2380 0.4370 -0.0353 -0.0414 -0.0640 122 GLY B CA  
2123 C C   . GLY B 122 ? 0.4756 0.2087 0.4110 -0.0432 -0.0246 -0.0363 122 GLY B C   
2124 O O   . GLY B 122 ? 0.4914 0.3100 0.3979 -0.0422 -0.0339 0.0402  122 GLY B O   
2125 N N   . LEU B 123 ? 0.4545 0.1744 0.3978 -0.0244 -0.0200 -0.0260 123 LEU B N   
2126 C CA  . LEU B 123 ? 0.4562 0.1440 0.3993 -0.0288 -0.0344 0.0027  123 LEU B CA  
2127 C C   . LEU B 123 ? 0.4397 0.1349 0.4043 -0.0208 -0.0402 -0.0027 123 LEU B C   
2128 O O   . LEU B 123 ? 0.4530 0.1529 0.4611 0.0058  -0.0051 0.0301  123 LEU B O   
2129 C CB  . LEU B 123 ? 0.4726 0.1861 0.4133 -0.0321 -0.0388 0.0068  123 LEU B CB  
2130 C CG  . LEU B 123 ? 0.4872 0.2188 0.3928 -0.0330 -0.0715 0.0307  123 LEU B CG  
2131 C CD1 . LEU B 123 ? 0.4767 0.2469 0.4066 -0.0425 -0.0701 -0.0025 123 LEU B CD1 
2132 C CD2 . LEU B 123 ? 0.5016 0.2204 0.4198 -0.0210 -0.0779 0.0579  123 LEU B CD2 
2133 N N   . LEU B 124 ? 0.4569 0.1179 0.4047 -0.0099 -0.0375 -0.0076 124 LEU B N   
2134 C CA  . LEU B 124 ? 0.4712 0.1694 0.4449 -0.0109 -0.0456 0.0141  124 LEU B CA  
2135 C C   . LEU B 124 ? 0.4700 0.1783 0.4396 -0.0206 -0.0574 0.0446  124 LEU B C   
2136 O O   . LEU B 124 ? 0.4539 0.1672 0.4725 0.0131  -0.0677 0.0830  124 LEU B O   
2137 C CB  . LEU B 124 ? 0.5124 0.1700 0.4411 0.0067  -0.0465 0.0172  124 LEU B CB  
2138 C CG  . LEU B 124 ? 0.5481 0.1868 0.4553 0.0186  -0.0518 0.0074  124 LEU B CG  
2139 C CD1 . LEU B 124 ? 0.5742 0.2032 0.4795 -0.0200 -0.0595 0.0246  124 LEU B CD1 
2140 C CD2 . LEU B 124 ? 0.5924 0.1928 0.4516 0.0339  -0.0425 0.0063  124 LEU B CD2 
2141 N N   . GLU B 125 ? 0.4472 0.1664 0.4251 -0.0325 -0.0787 0.0619  125 GLU B N   
2142 C CA  . GLU B 125 ? 0.4805 0.2116 0.4888 -0.0022 -0.1063 0.1113  125 GLU B CA  
2143 C C   . GLU B 125 ? 0.4809 0.2363 0.5283 0.0227  -0.1235 0.1104  125 GLU B C   
2144 O O   . GLU B 125 ? 0.4878 0.2132 0.5441 -0.0069 -0.1020 0.1527  125 GLU B O   
2145 C CB  . GLU B 125 ? 0.5234 0.2597 0.5063 -0.0020 -0.1090 0.0837  125 GLU B CB  
2146 C CG  . GLU B 125 ? 0.5580 0.3599 0.5429 -0.0217 -0.0929 0.0616  125 GLU B CG  
2147 C CD  . GLU B 125 ? 0.6260 0.4752 0.6274 -0.0331 -0.0633 0.0172  125 GLU B CD  
2148 O OE1 . GLU B 125 ? 0.6798 0.5717 0.6257 -0.0388 -0.0942 -0.0419 125 GLU B OE1 
2149 O OE2 . GLU B 125 ? 0.6740 0.6320 0.7095 -0.0248 -0.0289 0.0379  125 GLU B OE2 
2150 N N   . VAL B 126 ? 0.5002 0.1923 0.5832 0.0183  -0.1154 0.0719  126 VAL B N   
2151 C CA  . VAL B 126 ? 0.5037 0.2042 0.6335 0.0298  -0.0968 0.1047  126 VAL B CA  
2152 C C   . VAL B 126 ? 0.4934 0.1520 0.6449 0.0403  -0.0984 0.0965  126 VAL B C   
2153 O O   . VAL B 126 ? 0.5405 0.1036 0.6687 0.0756  -0.0835 0.0886  126 VAL B O   
2154 C CB  . VAL B 126 ? 0.5137 0.2021 0.6517 0.0140  -0.0658 0.1254  126 VAL B CB  
2155 C CG1 . VAL B 126 ? 0.5422 0.2138 0.6725 0.0071  -0.0642 0.1283  126 VAL B CG1 
2156 C CG2 . VAL B 126 ? 0.4796 0.2197 0.6636 0.0120  -0.0767 0.1368  126 VAL B CG2 
2157 N N   . LEU B 127 ? 0.4961 0.1565 0.6274 0.0251  -0.0939 0.0741  127 LEU B N   
2158 C CA  . LEU B 127 ? 0.4861 0.1528 0.6561 0.0338  -0.1072 0.0829  127 LEU B CA  
2159 C C   . LEU B 127 ? 0.4662 0.2333 0.6451 0.0294  -0.0872 0.0720  127 LEU B C   
2160 O O   . LEU B 127 ? 0.4576 0.2686 0.6796 0.0183  -0.0676 0.0690  127 LEU B O   
2161 C CB  . LEU B 127 ? 0.5051 0.2257 0.6589 0.0355  -0.1145 0.0730  127 LEU B CB  
2162 C CG  . LEU B 127 ? 0.5439 0.2474 0.6822 0.0087  -0.1141 0.0765  127 LEU B CG  
2163 C CD1 . LEU B 127 ? 0.5957 0.2623 0.6841 0.0113  -0.1067 0.0953  127 LEU B CD1 
2164 C CD2 . LEU B 127 ? 0.5635 0.2573 0.6787 -0.0076 -0.0977 0.0528  127 LEU B CD2 
2165 N N   . PHE B 128 ? 0.4217 0.1850 0.6130 0.0009  -0.0968 0.1036  128 PHE B N   
2166 C CA  . PHE B 128 ? 0.4221 0.2259 0.5877 -0.0125 -0.0934 0.0971  128 PHE B CA  
2167 C C   . PHE B 128 ? 0.5253 0.2399 0.6142 -0.0349 -0.1160 0.1296  128 PHE B C   
2168 O O   . PHE B 128 ? 0.5558 0.3477 0.6108 -0.0799 -0.1392 0.1548  128 PHE B O   
2169 C CB  . PHE B 128 ? 0.3992 0.2170 0.5521 -0.0225 -0.0525 0.0724  128 PHE B CB  
2170 C CG  . PHE B 128 ? 0.3981 0.2137 0.5071 0.0180  -0.0207 0.0860  128 PHE B CG  
2171 C CD1 . PHE B 128 ? 0.4213 0.2449 0.5347 0.0469  0.0022  0.0758  128 PHE B CD1 
2172 C CD2 . PHE B 128 ? 0.3744 0.2969 0.5157 0.0180  0.0079  0.0785  128 PHE B CD2 
2173 C CE1 . PHE B 128 ? 0.4292 0.2723 0.4939 0.0309  0.0089  0.0826  128 PHE B CE1 
2174 C CE2 . PHE B 128 ? 0.3944 0.3181 0.5123 0.0223  0.0161  0.0870  128 PHE B CE2 
2175 C CZ  . PHE B 128 ? 0.3955 0.2446 0.5017 0.0150  0.0151  0.0839  128 PHE B CZ  
2176 N N   . GLN B 129 ? 0.6053 0.2970 0.6691 -0.0374 -0.1084 0.1823  129 GLN B N   
2177 C CA  . GLN B 129 ? 0.6700 0.3614 0.6649 -0.0595 -0.0959 0.2090  129 GLN B CA  
2178 C C   . GLN B 129 ? 0.7194 0.4146 0.7439 -0.0327 -0.0823 0.2201  129 GLN B C   
2179 O O   . GLN B 129 ? 0.7905 0.5218 0.7890 0.0345  -0.1224 0.2435  129 GLN B O   
2180 C CB  . GLN B 129 ? 0.7332 0.4211 0.6762 -0.0677 -0.0572 0.2366  129 GLN B CB  
2181 C CG  . GLN B 129 ? 0.7644 0.4820 0.7020 -0.0867 -0.0467 0.2042  129 GLN B CG  
2182 C CD  . GLN B 129 ? 0.8012 0.5291 0.7115 -0.0744 -0.0277 0.2171  129 GLN B CD  
2183 O OE1 . GLN B 129 ? 0.8182 0.5175 0.7564 -0.0504 -0.0567 0.1590  129 GLN B OE1 
2184 N NE2 . GLN B 129 ? 0.8683 0.6022 0.7334 -0.0749 -0.0115 0.2051  129 GLN B NE2 
2185 C C1  . PGE C .   ? 0.6586 0.2579 0.5954 0.0139  0.0263  -0.0398 201 PGE A C1  
2186 O O1  . PGE C .   ? 0.6764 0.2828 0.6517 0.0529  -0.0241 -0.0686 201 PGE A O1  
2187 C C2  . PGE C .   ? 0.6886 0.2566 0.5754 0.0072  0.0290  -0.0104 201 PGE A C2  
2188 O O2  . PGE C .   ? 0.7392 0.3203 0.5220 0.0320  0.0411  -0.0013 201 PGE A O2  
2189 C C3  . PGE C .   ? 0.8109 0.1614 0.5753 0.0814  0.0361  -0.0597 201 PGE A C3  
2190 C C4  . PGE C .   ? 0.8720 0.2223 0.5816 0.0815  0.0421  -0.0081 201 PGE A C4  
2191 O O4  . PGE C .   ? 0.9509 0.3861 0.5761 -0.0238 0.0512  0.0393  201 PGE A O4  
2192 C C6  . PGE C .   ? 0.9402 0.3847 0.5606 -0.0043 0.0621  0.0436  201 PGE A C6  
2193 C C5  . PGE C .   ? 0.9308 0.3142 0.5560 0.0340  0.0587  0.0381  201 PGE A C5  
2194 O O3  . PGE C .   ? 0.9150 0.2264 0.5727 0.0536  0.0611  0.0037  201 PGE A O3  
2199 C C1  . PGE E .   ? 0.6153 0.2254 0.5932 0.0371  0.0601  0.0270  201 PGE B C1  
2200 O O1  . PGE E .   ? 0.6630 0.2409 0.6095 0.0373  0.0723  0.0089  201 PGE B O1  
2201 C C2  . PGE E .   ? 0.5916 0.1864 0.5717 0.0363  0.0533  0.0051  201 PGE B C2  
2202 O O2  . PGE E .   ? 0.5313 0.2417 0.5379 0.0249  0.0673  0.0158  201 PGE B O2  
2203 C C3  . PGE E .   ? 0.5515 0.1489 0.5967 -0.0124 0.0606  -0.0724 201 PGE B C3  
2204 C C4  . PGE E .   ? 0.6199 0.3199 0.5505 -0.0452 0.0575  -0.0100 201 PGE B C4  
2205 O O4  . PGE E .   ? 0.7379 0.3468 0.6899 -0.1725 0.0494  0.0579  201 PGE B O4  
2206 C C6  . PGE E .   ? 0.6796 0.3516 0.6333 -0.1103 0.0539  0.0423  201 PGE B C6  
2207 C C5  . PGE E .   ? 0.6866 0.2999 0.5980 -0.1011 0.0612  0.0402  201 PGE B C5  
2208 O O3  . PGE E .   ? 0.6251 0.3485 0.5439 -0.0495 0.0532  -0.0042 201 PGE B O3  
# 
