data_9HGG
# 
_entry.id   9HGG 
# 
_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   9HGG         pdb_00009hgg 10.2210/pdb9hgg/pdb 
WWPDB D_1292141648 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_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                        9HGG 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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                 2 
_pdbx_contact_author.email              E.Zeqiraj@leeds.ac.uk 
_pdbx_contact_author.name_first         Elton 
_pdbx_contact_author.name_last          Zeqiraj 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0239-5926 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Makhlouf, L.' 1 0000-0001-7835-6005 
'Zeqiraj, E.'  2 0000-0003-0239-5926 
# 
_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            Biochem.J. 
_citation.journal_id_ASTM           BIJOAK 
_citation.journal_id_CSD            0043 
_citation.journal_id_ISSN           1470-8728 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Sequence rules for a long SPOP-binding degron required for protein ubiquitylation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1042/BCJ20253041 
_citation.pdbx_database_id_PubMed   40178506 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Makhlouf, L.' 1 0000-0001-7835-6005 
primary 'Mishra, M.'   2 0000-0001-8226-2861 
primary 'Makhlouf, H.' 3 0009-0003-5661-9283 
primary 'Manfield, I.' 4 0000-0003-3765-0325 
primary 'Busino, L.'   5 0000-0001-6758-9276 
primary 'Zeqiraj, E.'  6 0000-0003-0239-5926 
# 
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 'Speckle-type POZ protein'                 16283.759 1   ?                 ? ? ? 
2 polymer     syn 'Histone-lysine N-methyltransferase SETD2' 1776.898  1   2.1.1.359,2.1.1.- ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                            24.305    5   ?                 ? ? ? 
4 water       nat water                                      18.015    121 ?                 ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'HIB homolog 1,Roadkill homolog 1' 
2 
;HIF-1,Huntingtin yeast partner B,Huntingtin-interacting protein 1,HIP-1,Huntingtin-interacting protein B,Lysine N-methyltransferase 3A,Protein-lysine N-methyltransferase SETD2,SET domain-containing protein 2,hSET2,p231HBP
;
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;AAKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFS
ILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD
;
;AAKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFS
ILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD
;
A ? 
2 'polypeptide(L)' no no DKGSVQAPEISSNSIKD DKGSVQAPEISSNSIKD B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'MAGNESIUM ION' MG  
4 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ALA n 
1 3   LYS n 
1 4   VAL n 
1 5   VAL n 
1 6   LYS n 
1 7   PHE n 
1 8   SER n 
1 9   TYR n 
1 10  MET n 
1 11  TRP n 
1 12  THR n 
1 13  ILE n 
1 14  ASN n 
1 15  ASN n 
1 16  PHE n 
1 17  SER n 
1 18  PHE n 
1 19  CYS n 
1 20  ARG n 
1 21  GLU n 
1 22  GLU n 
1 23  MET n 
1 24  GLY n 
1 25  GLU n 
1 26  VAL n 
1 27  ILE n 
1 28  LYS n 
1 29  SER n 
1 30  SER n 
1 31  THR n 
1 32  PHE n 
1 33  SER n 
1 34  SER n 
1 35  GLY n 
1 36  ALA n 
1 37  ASN n 
1 38  ASP n 
1 39  LYS n 
1 40  LEU n 
1 41  LYS n 
1 42  TRP n 
1 43  CYS n 
1 44  LEU n 
1 45  ARG n 
1 46  VAL n 
1 47  ASN n 
1 48  PRO n 
1 49  LYS n 
1 50  GLY n 
1 51  LEU n 
1 52  ASP n 
1 53  GLU n 
1 54  GLU n 
1 55  SER n 
1 56  LYS n 
1 57  ASP n 
1 58  TYR n 
1 59  LEU n 
1 60  SER n 
1 61  LEU n 
1 62  TYR n 
1 63  LEU n 
1 64  LEU n 
1 65  LEU n 
1 66  VAL n 
1 67  SER n 
1 68  CYS n 
1 69  PRO n 
1 70  LYS n 
1 71  SER n 
1 72  GLU n 
1 73  VAL n 
1 74  ARG n 
1 75  ALA n 
1 76  LYS n 
1 77  PHE n 
1 78  LYS n 
1 79  PHE n 
1 80  SER n 
1 81  ILE n 
1 82  LEU n 
1 83  ASN n 
1 84  ALA n 
1 85  LYS n 
1 86  GLY n 
1 87  GLU n 
1 88  GLU n 
1 89  THR n 
1 90  LYS n 
1 91  ALA n 
1 92  MET n 
1 93  GLU n 
1 94  SER n 
1 95  GLN n 
1 96  ARG n 
1 97  ALA n 
1 98  TYR n 
1 99  ARG n 
1 100 PHE n 
1 101 VAL n 
1 102 GLN n 
1 103 GLY n 
1 104 LYS n 
1 105 ASP n 
1 106 TRP n 
1 107 GLY n 
1 108 PHE n 
1 109 LYS n 
1 110 LYS n 
1 111 PHE n 
1 112 ILE n 
1 113 ARG n 
1 114 ARG n 
1 115 ASP n 
1 116 PHE n 
1 117 LEU n 
1 118 LEU n 
1 119 ASP n 
1 120 GLU n 
1 121 ALA n 
1 122 ASN n 
1 123 GLY n 
1 124 LEU n 
1 125 LEU n 
1 126 PRO n 
1 127 ASP n 
1 128 ASP n 
1 129 LYS n 
1 130 LEU n 
1 131 THR n 
1 132 LEU n 
1 133 PHE n 
1 134 CYS n 
1 135 GLU n 
1 136 VAL n 
1 137 SER n 
1 138 VAL n 
1 139 VAL n 
1 140 GLN n 
1 141 ASP n 
2 1   ASP n 
2 2   LYS n 
2 3   GLY n 
2 4   SER n 
2 5   VAL n 
2 6   GLN n 
2 7   ALA n 
2 8   PRO n 
2 9   GLU n 
2 10  ILE n 
2 11  SER n 
2 12  SER n 
2 13  ASN n 
2 14  SER n 
2 15  ILE n 
2 16  LYS n 
2 17  ASP 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                   141 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SPOP 
_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                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       17 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
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 
MG  non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'           24.305  
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   ALA 1   26   26   ALA ALA A . n 
A 1 2   ALA 2   27   27   ALA ALA A . n 
A 1 3   LYS 3   28   28   LYS LYS A . n 
A 1 4   VAL 4   29   29   VAL VAL A . n 
A 1 5   VAL 5   30   30   VAL VAL A . n 
A 1 6   LYS 6   31   31   LYS LYS A . n 
A 1 7   PHE 7   32   32   PHE PHE A . n 
A 1 8   SER 8   33   33   SER SER A . n 
A 1 9   TYR 9   34   34   TYR TYR A . n 
A 1 10  MET 10  35   35   MET MET A . n 
A 1 11  TRP 11  36   36   TRP TRP A . n 
A 1 12  THR 12  37   37   THR THR A . n 
A 1 13  ILE 13  38   38   ILE ILE A . n 
A 1 14  ASN 14  39   39   ASN ASN A . n 
A 1 15  ASN 15  40   40   ASN ASN A . n 
A 1 16  PHE 16  41   41   PHE PHE A . n 
A 1 17  SER 17  42   42   SER SER A . n 
A 1 18  PHE 18  43   43   PHE PHE A . n 
A 1 19  CYS 19  44   44   CYS CYS A . n 
A 1 20  ARG 20  45   45   ARG ARG A . n 
A 1 21  GLU 21  46   46   GLU GLU A . n 
A 1 22  GLU 22  47   47   GLU GLU A . n 
A 1 23  MET 23  48   48   MET MET A . n 
A 1 24  GLY 24  49   49   GLY GLY A . n 
A 1 25  GLU 25  50   50   GLU GLU A . n 
A 1 26  VAL 26  51   51   VAL VAL A . n 
A 1 27  ILE 27  52   52   ILE ILE A . n 
A 1 28  LYS 28  53   53   LYS LYS A . n 
A 1 29  SER 29  54   54   SER SER A . n 
A 1 30  SER 30  55   55   SER SER A . n 
A 1 31  THR 31  56   56   THR THR A . n 
A 1 32  PHE 32  57   57   PHE PHE A . n 
A 1 33  SER 33  58   58   SER SER A . n 
A 1 34  SER 34  59   59   SER SER A . n 
A 1 35  GLY 35  60   ?    ?   ?   A . n 
A 1 36  ALA 36  61   ?    ?   ?   A . n 
A 1 37  ASN 37  62   ?    ?   ?   A . n 
A 1 38  ASP 38  63   63   ASP ASP A . n 
A 1 39  LYS 39  64   64   LYS LYS A . n 
A 1 40  LEU 40  65   65   LEU LEU A . n 
A 1 41  LYS 41  66   66   LYS LYS A . n 
A 1 42  TRP 42  67   67   TRP TRP A . n 
A 1 43  CYS 43  68   68   CYS CYS A . n 
A 1 44  LEU 44  69   69   LEU LEU A . n 
A 1 45  ARG 45  70   70   ARG ARG A . n 
A 1 46  VAL 46  71   71   VAL VAL A . n 
A 1 47  ASN 47  72   72   ASN ASN A . n 
A 1 48  PRO 48  73   73   PRO PRO A . n 
A 1 49  LYS 49  74   74   LYS LYS A . n 
A 1 50  GLY 50  75   75   GLY GLY A . n 
A 1 51  LEU 51  76   76   LEU LEU A . n 
A 1 52  ASP 52  77   77   ASP ASP A . n 
A 1 53  GLU 53  78   78   GLU GLU A . n 
A 1 54  GLU 54  79   79   GLU GLU A . n 
A 1 55  SER 55  80   80   SER SER A . n 
A 1 56  LYS 56  81   81   LYS LYS A . n 
A 1 57  ASP 57  82   82   ASP ASP A . n 
A 1 58  TYR 58  83   83   TYR TYR A . n 
A 1 59  LEU 59  84   84   LEU LEU A . n 
A 1 60  SER 60  85   85   SER SER A . n 
A 1 61  LEU 61  86   86   LEU LEU A . n 
A 1 62  TYR 62  87   87   TYR TYR A . n 
A 1 63  LEU 63  88   88   LEU LEU A . n 
A 1 64  LEU 64  89   89   LEU LEU A . n 
A 1 65  LEU 65  90   90   LEU LEU A . n 
A 1 66  VAL 66  91   91   VAL VAL A . n 
A 1 67  SER 67  92   92   SER SER A . n 
A 1 68  CYS 68  93   93   CYS CYS A . n 
A 1 69  PRO 69  94   94   PRO PRO A . n 
A 1 70  LYS 70  95   95   LYS LYS A . n 
A 1 71  SER 71  96   96   SER SER A . n 
A 1 72  GLU 72  97   97   GLU GLU A . n 
A 1 73  VAL 73  98   98   VAL VAL A . n 
A 1 74  ARG 74  99   99   ARG ARG A . n 
A 1 75  ALA 75  100  100  ALA ALA A . n 
A 1 76  LYS 76  101  101  LYS LYS A . n 
A 1 77  PHE 77  102  102  PHE PHE A . n 
A 1 78  LYS 78  103  103  LYS LYS A . n 
A 1 79  PHE 79  104  104  PHE PHE A . n 
A 1 80  SER 80  105  105  SER SER A . n 
A 1 81  ILE 81  106  106  ILE ILE A . n 
A 1 82  LEU 82  107  107  LEU LEU A . n 
A 1 83  ASN 83  108  108  ASN ASN A . n 
A 1 84  ALA 84  109  109  ALA ALA A . n 
A 1 85  LYS 85  110  110  LYS LYS A . n 
A 1 86  GLY 86  111  111  GLY GLY A . n 
A 1 87  GLU 87  112  112  GLU GLU A . n 
A 1 88  GLU 88  113  113  GLU GLU A . n 
A 1 89  THR 89  114  114  THR THR A . n 
A 1 90  LYS 90  115  115  LYS LYS A . n 
A 1 91  ALA 91  116  116  ALA ALA A . n 
A 1 92  MET 92  117  117  MET MET A . n 
A 1 93  GLU 93  118  118  GLU GLU A . n 
A 1 94  SER 94  119  119  SER SER A . n 
A 1 95  GLN 95  120  120  GLN GLN A . n 
A 1 96  ARG 96  121  121  ARG ARG A . n 
A 1 97  ALA 97  122  122  ALA ALA A . n 
A 1 98  TYR 98  123  123  TYR TYR A . n 
A 1 99  ARG 99  124  124  ARG ARG A . n 
A 1 100 PHE 100 125  125  PHE PHE A . n 
A 1 101 VAL 101 126  126  VAL VAL A . n 
A 1 102 GLN 102 127  127  GLN GLN A . n 
A 1 103 GLY 103 128  128  GLY GLY A . n 
A 1 104 LYS 104 129  129  LYS LYS A . n 
A 1 105 ASP 105 130  130  ASP ASP A . n 
A 1 106 TRP 106 131  131  TRP TRP A . n 
A 1 107 GLY 107 132  132  GLY GLY A . n 
A 1 108 PHE 108 133  133  PHE PHE A . n 
A 1 109 LYS 109 134  134  LYS LYS A . n 
A 1 110 LYS 110 135  135  LYS LYS A . n 
A 1 111 PHE 111 136  136  PHE PHE A . n 
A 1 112 ILE 112 137  137  ILE ILE A . n 
A 1 113 ARG 113 138  138  ARG ARG A . n 
A 1 114 ARG 114 139  139  ARG ARG A . n 
A 1 115 ASP 115 140  140  ASP ASP A . n 
A 1 116 PHE 116 141  141  PHE PHE A . n 
A 1 117 LEU 117 142  142  LEU LEU A . n 
A 1 118 LEU 118 143  143  LEU LEU A . n 
A 1 119 ASP 119 144  144  ASP ASP A . n 
A 1 120 GLU 120 145  145  GLU GLU A . n 
A 1 121 ALA 121 146  146  ALA ALA A . n 
A 1 122 ASN 122 147  147  ASN ASN A . n 
A 1 123 GLY 123 148  148  GLY GLY A . n 
A 1 124 LEU 124 149  149  LEU LEU A . n 
A 1 125 LEU 125 150  150  LEU LEU A . n 
A 1 126 PRO 126 151  151  PRO PRO A . n 
A 1 127 ASP 127 152  152  ASP ASP A . n 
A 1 128 ASP 128 153  153  ASP ASP A . n 
A 1 129 LYS 129 154  154  LYS LYS A . n 
A 1 130 LEU 130 155  155  LEU LEU A . n 
A 1 131 THR 131 156  156  THR THR A . n 
A 1 132 LEU 132 157  157  LEU LEU A . n 
A 1 133 PHE 133 158  158  PHE PHE A . n 
A 1 134 CYS 134 159  159  CYS CYS A . n 
A 1 135 GLU 135 160  160  GLU GLU A . n 
A 1 136 VAL 136 161  161  VAL VAL A . n 
A 1 137 SER 137 162  162  SER SER A . n 
A 1 138 VAL 138 163  163  VAL VAL A . n 
A 1 139 VAL 139 164  164  VAL VAL A . n 
A 1 140 GLN 140 165  165  GLN GLN A . n 
A 1 141 ASP 141 166  166  ASP ASP A . n 
B 2 1   ASP 1   1363 ?    ?   ?   B . n 
B 2 2   LYS 2   1364 1364 LYS LYS B . n 
B 2 3   GLY 3   1365 1365 GLY GLY B . n 
B 2 4   SER 4   1366 1366 SER SER B . n 
B 2 5   VAL 5   1367 1367 VAL VAL B . n 
B 2 6   GLN 6   1368 1368 GLN GLN B . n 
B 2 7   ALA 7   1369 1369 ALA ALA B . n 
B 2 8   PRO 8   1370 1370 PRO PRO B . n 
B 2 9   GLU 9   1371 1371 GLU GLU B . n 
B 2 10  ILE 10  1372 1372 ILE ILE B . n 
B 2 11  SER 11  1373 1373 SER SER B . n 
B 2 12  SER 12  1374 1374 SER SER B . n 
B 2 13  ASN 13  1375 1375 ASN ASN B . n 
B 2 14  SER 14  1376 1376 SER SER B . n 
B 2 15  ILE 15  1377 1377 ILE ILE B . n 
B 2 16  LYS 16  1378 ?    ?   ?   B . n 
B 2 17  ASP 17  1379 ?    ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 MG  1   201  1   MG  MG  A . 
D 3 MG  1   202  2   MG  MG  A . 
E 3 MG  1   203  3   MG  MG  A . 
F 3 MG  1   204  4   MG  MG  A . 
G 3 MG  1   205  5   MG  MG  A . 
H 4 HOH 1   301  111 HOH HOH A . 
H 4 HOH 2   302  104 HOH HOH A . 
H 4 HOH 3   303  131 HOH HOH A . 
H 4 HOH 4   304  71  HOH HOH A . 
H 4 HOH 5   305  10  HOH HOH A . 
H 4 HOH 6   306  68  HOH HOH A . 
H 4 HOH 7   307  8   HOH HOH A . 
H 4 HOH 8   308  120 HOH HOH A . 
H 4 HOH 9   309  57  HOH HOH A . 
H 4 HOH 10  310  1   HOH HOH A . 
H 4 HOH 11  311  12  HOH HOH A . 
H 4 HOH 12  312  44  HOH HOH A . 
H 4 HOH 13  313  7   HOH HOH A . 
H 4 HOH 14  314  86  HOH HOH A . 
H 4 HOH 15  315  33  HOH HOH A . 
H 4 HOH 16  316  84  HOH HOH A . 
H 4 HOH 17  317  45  HOH HOH A . 
H 4 HOH 18  318  42  HOH HOH A . 
H 4 HOH 19  319  11  HOH HOH A . 
H 4 HOH 20  320  76  HOH HOH A . 
H 4 HOH 21  321  75  HOH HOH A . 
H 4 HOH 22  322  43  HOH HOH A . 
H 4 HOH 23  323  53  HOH HOH A . 
H 4 HOH 24  324  88  HOH HOH A . 
H 4 HOH 25  325  4   HOH HOH A . 
H 4 HOH 26  326  20  HOH HOH A . 
H 4 HOH 27  327  17  HOH HOH A . 
H 4 HOH 28  328  13  HOH HOH A . 
H 4 HOH 29  329  54  HOH HOH A . 
H 4 HOH 30  330  21  HOH HOH A . 
H 4 HOH 31  331  59  HOH HOH A . 
H 4 HOH 32  332  102 HOH HOH A . 
H 4 HOH 33  333  34  HOH HOH A . 
H 4 HOH 34  334  58  HOH HOH A . 
H 4 HOH 35  335  46  HOH HOH A . 
H 4 HOH 36  336  16  HOH HOH A . 
H 4 HOH 37  337  32  HOH HOH A . 
H 4 HOH 38  338  98  HOH HOH A . 
H 4 HOH 39  339  41  HOH HOH A . 
H 4 HOH 40  340  37  HOH HOH A . 
H 4 HOH 41  341  126 HOH HOH A . 
H 4 HOH 42  342  26  HOH HOH A . 
H 4 HOH 43  343  5   HOH HOH A . 
H 4 HOH 44  344  30  HOH HOH A . 
H 4 HOH 45  345  72  HOH HOH A . 
H 4 HOH 46  346  106 HOH HOH A . 
H 4 HOH 47  347  140 HOH HOH A . 
H 4 HOH 48  348  52  HOH HOH A . 
H 4 HOH 49  349  121 HOH HOH A . 
H 4 HOH 50  350  61  HOH HOH A . 
H 4 HOH 51  351  70  HOH HOH A . 
H 4 HOH 52  352  38  HOH HOH A . 
H 4 HOH 53  353  14  HOH HOH A . 
H 4 HOH 54  354  47  HOH HOH A . 
H 4 HOH 55  355  107 HOH HOH A . 
H 4 HOH 56  356  63  HOH HOH A . 
H 4 HOH 57  357  27  HOH HOH A . 
H 4 HOH 58  358  24  HOH HOH A . 
H 4 HOH 59  359  103 HOH HOH A . 
H 4 HOH 60  360  105 HOH HOH A . 
H 4 HOH 61  361  85  HOH HOH A . 
H 4 HOH 62  362  89  HOH HOH A . 
H 4 HOH 63  363  112 HOH HOH A . 
H 4 HOH 64  364  109 HOH HOH A . 
H 4 HOH 65  365  23  HOH HOH A . 
H 4 HOH 66  366  130 HOH HOH A . 
H 4 HOH 67  367  116 HOH HOH A . 
H 4 HOH 68  368  96  HOH HOH A . 
H 4 HOH 69  369  25  HOH HOH A . 
H 4 HOH 70  370  22  HOH HOH A . 
H 4 HOH 71  371  123 HOH HOH A . 
H 4 HOH 72  372  100 HOH HOH A . 
H 4 HOH 73  373  77  HOH HOH A . 
H 4 HOH 74  374  39  HOH HOH A . 
H 4 HOH 75  375  49  HOH HOH A . 
H 4 HOH 76  376  64  HOH HOH A . 
H 4 HOH 77  377  35  HOH HOH A . 
H 4 HOH 78  378  67  HOH HOH A . 
H 4 HOH 79  379  81  HOH HOH A . 
H 4 HOH 80  380  93  HOH HOH A . 
H 4 HOH 81  381  91  HOH HOH A . 
H 4 HOH 82  382  114 HOH HOH A . 
H 4 HOH 83  383  80  HOH HOH A . 
H 4 HOH 84  384  127 HOH HOH A . 
H 4 HOH 85  385  82  HOH HOH A . 
H 4 HOH 86  386  73  HOH HOH A . 
H 4 HOH 87  387  97  HOH HOH A . 
H 4 HOH 88  388  36  HOH HOH A . 
H 4 HOH 89  389  55  HOH HOH A . 
H 4 HOH 90  390  83  HOH HOH A . 
H 4 HOH 91  391  119 HOH HOH A . 
H 4 HOH 92  392  51  HOH HOH A . 
H 4 HOH 93  393  125 HOH HOH A . 
H 4 HOH 94  394  132 HOH HOH A . 
H 4 HOH 95  395  99  HOH HOH A . 
H 4 HOH 96  396  87  HOH HOH A . 
H 4 HOH 97  397  101 HOH HOH A . 
H 4 HOH 98  398  56  HOH HOH A . 
H 4 HOH 99  399  117 HOH HOH A . 
H 4 HOH 100 400  9   HOH HOH A . 
H 4 HOH 101 401  141 HOH HOH A . 
H 4 HOH 102 402  95  HOH HOH A . 
H 4 HOH 103 403  79  HOH HOH A . 
H 4 HOH 104 404  48  HOH HOH A . 
H 4 HOH 105 405  74  HOH HOH A . 
H 4 HOH 106 406  110 HOH HOH A . 
I 4 HOH 1   1401 137 HOH HOH B . 
I 4 HOH 2   1402 6   HOH HOH B . 
I 4 HOH 3   1403 69  HOH HOH B . 
I 4 HOH 4   1404 15  HOH HOH B . 
I 4 HOH 5   1405 62  HOH HOH B . 
I 4 HOH 6   1406 2   HOH HOH B . 
I 4 HOH 7   1407 3   HOH HOH B . 
I 4 HOH 8   1408 40  HOH HOH B . 
I 4 HOH 9   1409 60  HOH HOH B . 
I 4 HOH 10  1410 18  HOH HOH B . 
I 4 HOH 11  1411 19  HOH HOH B . 
I 4 HOH 12  1412 115 HOH HOH B . 
I 4 HOH 13  1413 65  HOH HOH B . 
I 4 HOH 14  1414 50  HOH HOH B . 
I 4 HOH 15  1415 66  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A PHE 43   ? CG  ? A PHE 18 CG  
2  1 Y 1 A PHE 43   ? CD1 ? A PHE 18 CD1 
3  1 Y 1 A PHE 43   ? CD2 ? A PHE 18 CD2 
4  1 Y 1 A PHE 43   ? CE1 ? A PHE 18 CE1 
5  1 Y 1 A PHE 43   ? CE2 ? A PHE 18 CE2 
6  1 Y 1 A PHE 43   ? CZ  ? A PHE 18 CZ  
7  1 Y 1 A ARG 45   ? CG  ? A ARG 20 CG  
8  1 Y 1 A ARG 45   ? CD  ? A ARG 20 CD  
9  1 Y 1 A ARG 45   ? NE  ? A ARG 20 NE  
10 1 Y 1 A ARG 45   ? CZ  ? A ARG 20 CZ  
11 1 Y 1 A ARG 45   ? NH1 ? A ARG 20 NH1 
12 1 Y 1 A ARG 45   ? NH2 ? A ARG 20 NH2 
13 1 Y 1 A LYS 95   ? CG  ? A LYS 70 CG  
14 1 Y 1 A LYS 95   ? CD  ? A LYS 70 CD  
15 1 Y 1 A LYS 95   ? CE  ? A LYS 70 CE  
16 1 Y 1 A LYS 95   ? NZ  ? A LYS 70 NZ  
17 1 Y 1 A GLN 120  ? CG  ? A GLN 95 CG  
18 1 Y 1 A GLN 120  ? CD  ? A GLN 95 CD  
19 1 Y 1 A GLN 120  ? OE1 ? A GLN 95 OE1 
20 1 Y 1 A GLN 120  ? NE2 ? A GLN 95 NE2 
21 1 Y 1 B LYS 1364 ? CG  ? B LYS 2  CG  
22 1 Y 1 B LYS 1364 ? CD  ? B LYS 2  CD  
23 1 Y 1 B LYS 1364 ? CE  ? B LYS 2  CE  
24 1 Y 1 B LYS 1364 ? NZ  ? B LYS 2  NZ  
25 1 Y 1 B ASN 1375 ? CG  ? B ASN 13 CG  
26 1 Y 1 B ASN 1375 ? OD1 ? B ASN 13 OD1 
27 1 Y 1 B ASN 1375 ? ND2 ? B ASN 13 ND2 
28 1 Y 1 B ILE 1377 ? CG1 ? B ILE 15 CG1 
29 1 Y 1 B ILE 1377 ? CG2 ? B ILE 15 CG2 
30 1 Y 1 B ILE 1377 ? CD1 ? B ILE 15 CD1 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HGG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.565 
_cell.length_a_esd                 ? 
_cell.length_b                     51.043 
_cell.length_b_esd                 ? 
_cell.length_c                     54.901 
_cell.length_c_esd                 ? 
_cell.volume                       124885.023 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9HGG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (z,x,y)' 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_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                   9HGG 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          28.85 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'10% w/v PEG 20 000, 20% v/v PEG MME 550, 0.03 M sodium fluoride, 0.03 M sodium bromide, 0.1 M MES/imidazole pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9537 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          23.88 
_reflns.entry_id                                       9HGG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.90 
_reflns.d_resolution_low                               44.56 
_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                                     10343 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          45.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.90 
_reflns_shell.d_res_low                                     1.97 
_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                             1018 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.85 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.15 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9HGG 
_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                            1.90 
_refine.ls_d_res_low                             44.56 
_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                     10337 
_refine.ls_number_reflns_R_free                  484 
_refine.ls_number_reflns_R_work                  9853 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 4.68 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1973 
_refine.ls_R_factor_R_free                       0.2561 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1942 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.39 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.8991 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1756 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        44.56 
_refine_hist.number_atoms_solvent             121 
_refine_hist.number_atoms_total               1320 
_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        1194 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_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' ? 0.0124 ? 1226 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2122 ? 1649 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0635 ? 182  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0096 ? 208  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.7532 ? 163  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.90 2.17  . . 167 3189 99.85  . . . . 0.2386 . . . . . . . . . . . 0.2921 
'X-RAY DIFFRACTION' 2.17 2.74  . . 152 3264 100.00 . . . . 0.2325 . . . . . . . . . . . 0.2725 
'X-RAY DIFFRACTION' 2.74 44.56 . . 165 3400 99.92  . . . . 0.1681 . . . . . . . . . . . 0.2402 
# 
_struct.entry_id                     9HGG 
_struct.title                        'SETD2 peptide bound to SPOP MATH domain' 
_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        9HGG 
_struct_keywords.text            'Ubiquitination, Ligase, Complex, Degradation' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SPOP_HUMAN  O43791 ? 1 
;KVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSIL
NAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQD
;
28   
2 UNP SETD2_HUMAN Q9BYW2 ? 2 DKGSVQAPEISSNSIKD 1363 
# 
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 9HGG A 3 ? 141 ? O43791 28   ? 166  ? 28   166  
2 2 9HGG B 1 ? 17  ? Q9BYW2 1363 ? 1379 ? 1363 1379 
# 
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 9HGG ALA A 1 ? UNP O43791 ? ? 'expression tag' 26 1 
1 9HGG ALA A 2 ? UNP O43791 ? ? 'expression tag' 27 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1760 ? 
1 MORE         -34  ? 
1 'SSA (A^2)'  7960 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'assay for oligomerization' 
_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 ASN A 15  ? CYS A 19  ? ASN A 40  CYS A 44  5 ? 5 
HELX_P HELX_P2 AA2 ARG A 114 ? LEU A 118 ? ARG A 139 LEU A 143 1 ? 5 
HELX_P HELX_P3 AA3 ASP A 119 ? GLY A 123 ? ASP A 144 GLY A 148 5 ? 5 
HELX_P HELX_P4 AA4 LEU A 125 ? LYS A 129 ? LEU A 150 LYS A 154 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? E MG . MG ? ? ? 1_555 H HOH . O ? ? A MG 203 A HOH 329 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc2 metalc ? ? E MG . MG ? ? ? 1_555 H HOH . O ? ? A MG 203 A HOH 329 2_565 ? ? ? ? ? ? ? 2.349 ? ? 
metalc3 metalc ? ? E MG . MG ? ? ? 1_555 H HOH . O ? ? A MG 203 A HOH 372 1_555 ? ? ? ? ? ? ? 2.953 ? ? 
metalc4 metalc ? ? E MG . MG ? ? ? 1_555 H HOH . O ? ? A MG 203 A HOH 372 2_565 ? ? ? ? ? ? ? 2.953 ? ? 
metalc5 metalc ? ? F MG . MG ? ? ? 1_555 H HOH . O ? ? A MG 204 A HOH 358 3_645 ? ? ? ? ? ? ? 2.946 ? ? 
metalc6 metalc ? ? G MG . MG ? ? ? 1_555 H HOH . O ? ? A MG 205 A HOH 373 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc7 metalc ? ? G MG . MG ? ? ? 1_555 H HOH . O ? ? A MG 205 A HOH 391 2_565 ? ? ? ? ? ? ? 2.182 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 O ? H HOH . ? A HOH 329 ? 1_555 MG ? E MG . ? A MG 203 ? 1_555 O ? H HOH . ? A HOH 329 ? 2_565 134.1 ? 
2 O ? H HOH . ? A HOH 329 ? 1_555 MG ? E MG . ? A MG 203 ? 1_555 O ? H HOH . ? A HOH 372 ? 1_555 67.1  ? 
3 O ? H HOH . ? A HOH 329 ? 2_565 MG ? E MG . ? A MG 203 ? 1_555 O ? H HOH . ? A HOH 372 ? 1_555 67.1  ? 
4 O ? H HOH . ? A HOH 329 ? 1_555 MG ? E MG . ? A MG 203 ? 1_555 O ? H HOH . ? A HOH 372 ? 2_565 67.1  ? 
5 O ? H HOH . ? A HOH 329 ? 2_565 MG ? E MG . ? A MG 203 ? 1_555 O ? H HOH . ? A HOH 372 ? 2_565 67.1  ? 
6 O ? H HOH . ? A HOH 372 ? 1_555 MG ? E MG . ? A MG 203 ? 1_555 O ? H HOH . ? A HOH 372 ? 2_565 0.0   ? 
7 O ? H HOH . ? A HOH 373 ? 1_555 MG ? G MG . ? A MG 205 ? 1_555 O ? H HOH . ? A HOH 391 ? 2_565 146.2 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 4   ? ILE A 13  ? VAL A 29   ILE A 38   
AA1 2 LEU A 130 ? VAL A 139 ? LEU A 155  VAL A 164  
AA1 3 VAL A 73  ? LEU A 82  ? VAL A 98   LEU A 107  
AA1 4 GLU A 88  ? GLU A 93  ? GLU A 113  GLU A 118  
AA2 1 VAL A 4   ? ILE A 13  ? VAL A 29   ILE A 38   
AA2 2 LEU A 130 ? VAL A 139 ? LEU A 155  VAL A 164  
AA2 3 VAL A 73  ? LEU A 82  ? VAL A 98   LEU A 107  
AA2 4 TYR A 98  ? PHE A 100 ? TYR A 123  PHE A 125  
AA3 1 ILE A 27  ? LYS A 28  ? ILE A 52   LYS A 53   
AA3 2 LYS A 41  ? ASN A 47  ? LYS A 66   ASN A 72   
AA3 3 PHE A 32  ? SER A 33  ? PHE A 57   SER A 58   
AA4 1 ILE A 27  ? LYS A 28  ? ILE A 52   LYS A 53   
AA4 2 LYS A 41  ? ASN A 47  ? LYS A 66   ASN A 72   
AA4 3 TYR A 58  ? SER A 67  ? TYR A 83   SER A 92   
AA4 4 ASP A 105 ? ARG A 113 ? ASP A 130  ARG A 138  
AA4 5 SER B 11  ? SER B 12  ? SER B 1373 SER B 1374 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 11  ? N TRP A 36  O LEU A 132 ? O LEU A 157  
AA1 2 3 O SER A 137 ? O SER A 162 N LYS A 76  ? N LYS A 101  
AA1 3 4 N ILE A 81  ? N ILE A 106 O THR A 89  ? O THR A 114  
AA2 1 2 N TRP A 11  ? N TRP A 36  O LEU A 132 ? O LEU A 157  
AA2 2 3 O SER A 137 ? O SER A 162 N LYS A 76  ? N LYS A 101  
AA2 3 4 N VAL A 73  ? N VAL A 98  O PHE A 100 ? O PHE A 125  
AA3 1 2 N ILE A 27  ? N ILE A 52  O VAL A 46  ? O VAL A 71   
AA3 2 3 O TRP A 42  ? O TRP A 67  N PHE A 32  ? N PHE A 57   
AA4 1 2 N ILE A 27  ? N ILE A 52  O VAL A 46  ? O VAL A 71   
AA4 2 3 N ARG A 45  ? N ARG A 70  O TYR A 62  ? O TYR A 87   
AA4 3 4 N LEU A 63  ? N LEU A 88  O TRP A 106 ? O TRP A 131  
AA4 4 5 N GLY A 107 ? N GLY A 132 O SER B 11  ? O SER B 1373 
# 
_pdbx_entry_details.entry_id                   9HGG 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    130 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    1376 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.16 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 MET A 48  ? ? -37.36  123.79  
2 1 LYS A 95  ? ? -126.92 -132.02 
3 1 LYS A 135 ? ? -109.62 73.85   
# 
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 MG  201 ? C MG  . 
2 1 A MG  203 ? E MG  . 
3 1 A HOH 340 ? H HOH . 
4 1 A HOH 347 ? H HOH . 
5 1 A HOH 372 ? H HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x,-y,-z         
3 -x,y+1/2,-z+1/2 
4 -x,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 16.1831899359 19.6613718161 5.60882168066   0.168304949037 ? -0.0255472681238  ? 0.0410238301214 
? 0.266709587651 ? -0.00557725455653 ? 0.117093752177 ? 2.20655270746 ? -1.33706106042  ? 0.640703064444 ? 2.28407382865 ? 
-0.465899556911 ? 2.47937485868 ? -0.234437202824  ? -0.231033754681  ? 0.278626946024  ? -0.0466933956316 ? 0.0614680791527  ? 
-0.151535969752 ? 0.0299277258651 ? 0.114542399026  ? 0.129595089568   ? 
2  'X-RAY DIFFRACTION' ? refined 21.8579774    18.5741175857 -0.951788372334 0.208008149955 ? -0.0128053543347  ? 0.0423134263467 
? 0.291674617401 ? -0.00207099202888 ? 0.165351945658 ? 2.7935684426  ? -0.504723826178 ? -1.58153858502 ? 3.46644288308 ? 
-0.344161230925 ? 3.49603901585 ? 0.11769407244    ? -0.403261255674  ? 0.194349270543  ? -0.122299792199  ? -0.138135239647  ? 
-0.344226876433 ? -0.112494116389 ? 0.520319841693  ? 0.00532260178652 ? 
3  'X-RAY DIFFRACTION' ? refined 19.9215857235 15.6701917642 0.603611587239  0.266547939854 ? -0.0201132780953  ? -0.0483321130585 
? 0.267170735288 ? 0.0423064392878   ? 0.18238885322  ? 3.95261101861 ? 4.27908988519   ? 0.329679363566 ? 5.25132855998 ? 
1.43825742688   ? 2.19120600658 ? -0.51874705549   ? 1.2146028351     ? 0.322112295291  ? -0.511101516139  ? 0.59468047171    ? 
0.271599275578  ? -0.10612172442  ? 0.157261600221  ? -0.159765286596  ? 
4  'X-RAY DIFFRACTION' ? refined 5.15969445005 6.63215952834 5.34636416312   0.220170913467 ? -0.0925603799599  ? 0.0802354065529 
? 0.328531417095 ? -0.0358921689269  ? 0.379652327253 ? 6.02598386727 ? -1.02061014265  ? -0.14262315258 ? 4.53825514476 ? 
0.134690958684  ? 8.88486736069 ? -0.418603453025  ? -0.0271607162115 ? -1.01035928257  ? -0.0792043687974 ? 0.0526914272271  ? 
0.395238921647  ? 0.943154620319  ? -0.646927261062 ? 0.243315332479   ? 
5  'X-RAY DIFFRACTION' ? refined 26.3459205057 11.7926569744 0.123541427799  0.155123678742 ? 0.0513140757599   ? 0.00660327911145 
? 0.345784920055 ? -0.0266892402042  ? 0.190642486528 ? 4.51352278725 ? 1.37046970928   ? -2.33203442095 ? 2.50030560882 ? 
-0.674129790572 ? 3.10128225053 ? -0.0879383805998 ? 0.42732713481    ? -0.723906452675 ? -0.170225234228  ? -0.131138649396  ? 
-0.310153262806 ? 0.323662088663  ? 0.540688483578  ? 0.184717954846   ? 
6  'X-RAY DIFFRACTION' ? refined 24.3809079052 13.2607731749 10.6418829004   0.209490304989 ? 0.0489600693912   ? -0.0437153272279 
? 0.256443773116 ? 0.00338766112604  ? 0.18045205715  ? 4.85485391085 ? -2.6453086183   ? -3.53952446926 ? 5.16413087319 ? 
1.82510890458   ? 5.74030452264 ? -0.672612290736  ? -0.400047438002  ? 0.505238115563  ? 0.509261063409   ? 0.409290487289   ? 
-0.722208228031 ? 0.443674316737  ? 0.929149219509  ? 0.174551538026   ? 
7  'X-RAY DIFFRACTION' ? refined 12.5522386058 22.8825076194 18.8093950058   0.174690665719 ? -0.04952057842    ? -0.0233494259238 
? 0.239932154598 ? 0.0414734391467   ? 0.208454114053 ? 5.30843566202 ? -2.55153911198  ? 1.07122718412  ? 2.5155215139  ? 
0.321809144846  ? 8.4873571706  ? 0.0782135749426  ? -0.285968467716  ? 0.265959393689  ? 0.177776089252   ? -0.050590371042  ? 
-0.996985792556 ? -0.465040019532 ? 1.19630073473   ? -0.0336790779027 ? 
8  'X-RAY DIFFRACTION' ? refined 26.128719894  7.57846769292 6.75734213131   0.198179730845 ? 0.000233161912847 ? -0.0252464584756 
? 0.252826345656 ? 0.00939480857568  ? 0.184687809074 ? 3.55189442759 ? -1.26235603039  ? -2.4982036037  ? 1.93417231619 ? 
-0.286721180164 ? 5.23771467055 ? 0.0499488146155  ? -0.467177033529  ? 0.103951586742  ? 0.167942951383   ? 0.352022548415   ? 
0.100991811713  ? 0.26920324703   ? 0.478660547513  ? -0.386874942313  ? 
9  'X-RAY DIFFRACTION' ? refined 7.67812817137 12.9981180663 11.698315505    0.186750030222 ? -0.0175410757715  ? 0.0153818879106 
? 0.223781614464 ? 0.0552338856612   ? 0.214893364564 ? 5.10714376298 ? -1.98835256229  ? -1.46318272846 ? 2.7492262277  ? 
1.56155394728   ? 4.03140870286 ? -0.236247690327  ? -0.362705240618  ? -0.49207860846  ? 0.127563880336   ? 0.0838690412083  ? 
0.440469901525  ? 0.143037041179  ? -0.431622230429 ? 0.192059240485   ? 
10 'X-RAY DIFFRACTION' ? refined 18.3496351663 20.6018680183 9.88468642694   0.133200295115 ? -0.0101339900028  ? 
-6.55173954193e-05 ? 0.172787808884 ? 0.00227545408014  ? 0.113357178326 ? 2.80311861087 ? -1.47667645102  ? -1.45661088378 ? 
3.32695262625 ? 0.710444998883  ? 2.44786454016 ? 0.0363348845135  ? 0.0477506633332  ? 0.571486653469  ? 0.0580116789026  ? 
-0.0711851529871 ? -0.234848736894 ? -0.184325725752 ? 0.279305860149  ? -0.0176653405305 ? 
11 'X-RAY DIFFRACTION' ? refined 13.5531806363 5.22458297718 10.3768008321   0.267125504024 ? -0.0187729249423  ? 0.00366766280674 
? 0.123431082574 ? 0.0118511829337   ? 0.313297318678 ? 5.33095296627 ? -1.0217774801   ? -1.60097873769 ? 4.30988648591 ? 
2.4860987848    ? 6.75580827415 ? -0.224871508299  ? 0.0701384198389  ? -0.823413225711 ? 0.289989807595   ? 0.0667409475306  ? 
0.281350299535  ? 0.581279812586  ? 0.157296435071  ? 0.167163255683   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 26   ? A 23  A 48   ? ? 
;chain 'A' and (resid 26 through 48 )
;
2  'X-RAY DIFFRACTION' 2  A 24  A 49   ? A 37  A 65   ? ? 
;chain 'A' and (resid 49 through 65 )
;
3  'X-RAY DIFFRACTION' 3  A 38  A 66   ? A 44  A 72   ? ? 
;chain 'A' and (resid 66 through 72 )
;
4  'X-RAY DIFFRACTION' 4  A 45  A 73   ? A 56  A 84   ? ? 
;chain 'A' and (resid 73 through 84 )
;
5  'X-RAY DIFFRACTION' 5  A 57  A 85   ? A 69  A 97   ? ? 
;chain 'A' and (resid 85 through 97 )
;
6  'X-RAY DIFFRACTION' 6  A 70  A 98   ? A 78  A 106  ? ? 
;chain 'A' and (resid 98 through 106 )
;
7  'X-RAY DIFFRACTION' 7  A 79  A 107  ? A 88  A 116  ? ? 
;chain 'A' and (resid 107 through 116 )
;
8  'X-RAY DIFFRACTION' 8  A 89  A 117  ? A 101 A 129  ? ? 
;chain 'A' and (resid 117 through 129 )
;
9  'X-RAY DIFFRACTION' 9  A 102 A 130  ? A 119 A 147  ? ? 
;chain 'A' and (resid 130 through 147 )
;
10 'X-RAY DIFFRACTION' 10 A 120 A 148  ? A 138 A 166  ? ? 
;chain 'A' and (resid 148 through 166 )
;
11 'X-RAY DIFFRACTION' 11 B 1   B 1364 ? B 14  B 1377 ? ? 
;chain 'B' and (resid 1364 through 1377 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 60   ? A GLY 35 
2 1 Y 1 A ALA 61   ? A ALA 36 
3 1 Y 1 A ASN 62   ? A ASN 37 
4 1 Y 1 B ASP 1363 ? B ASP 1  
5 1 Y 1 B LYS 1378 ? B LYS 16 
6 1 Y 1 B ASP 1379 ? B ASP 17 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HOH O    O  N N 137 
HOH H1   H  N N 138 
HOH H2   H  N N 139 
ILE N    N  N N 140 
ILE CA   C  N S 141 
ILE C    C  N N 142 
ILE O    O  N N 143 
ILE CB   C  N S 144 
ILE CG1  C  N N 145 
ILE CG2  C  N N 146 
ILE CD1  C  N N 147 
ILE OXT  O  N N 148 
ILE H    H  N N 149 
ILE H2   H  N N 150 
ILE HA   H  N N 151 
ILE HB   H  N N 152 
ILE HG12 H  N N 153 
ILE HG13 H  N N 154 
ILE HG21 H  N N 155 
ILE HG22 H  N N 156 
ILE HG23 H  N N 157 
ILE HD11 H  N N 158 
ILE HD12 H  N N 159 
ILE HD13 H  N N 160 
ILE HXT  H  N N 161 
LEU N    N  N N 162 
LEU CA   C  N S 163 
LEU C    C  N N 164 
LEU O    O  N N 165 
LEU CB   C  N N 166 
LEU CG   C  N N 167 
LEU CD1  C  N N 168 
LEU CD2  C  N N 169 
LEU OXT  O  N N 170 
LEU H    H  N N 171 
LEU H2   H  N N 172 
LEU HA   H  N N 173 
LEU HB2  H  N N 174 
LEU HB3  H  N N 175 
LEU HG   H  N N 176 
LEU HD11 H  N N 177 
LEU HD12 H  N N 178 
LEU HD13 H  N N 179 
LEU HD21 H  N N 180 
LEU HD22 H  N N 181 
LEU HD23 H  N N 182 
LEU HXT  H  N N 183 
LYS N    N  N N 184 
LYS CA   C  N S 185 
LYS C    C  N N 186 
LYS O    O  N N 187 
LYS CB   C  N N 188 
LYS CG   C  N N 189 
LYS CD   C  N N 190 
LYS CE   C  N N 191 
LYS NZ   N  N N 192 
LYS OXT  O  N N 193 
LYS H    H  N N 194 
LYS H2   H  N N 195 
LYS HA   H  N N 196 
LYS HB2  H  N N 197 
LYS HB3  H  N N 198 
LYS HG2  H  N N 199 
LYS HG3  H  N N 200 
LYS HD2  H  N N 201 
LYS HD3  H  N N 202 
LYS HE2  H  N N 203 
LYS HE3  H  N N 204 
LYS HZ1  H  N N 205 
LYS HZ2  H  N N 206 
LYS HZ3  H  N N 207 
LYS HXT  H  N N 208 
MET N    N  N N 209 
MET CA   C  N S 210 
MET C    C  N N 211 
MET O    O  N N 212 
MET CB   C  N N 213 
MET CG   C  N N 214 
MET SD   S  N N 215 
MET CE   C  N N 216 
MET OXT  O  N N 217 
MET H    H  N N 218 
MET H2   H  N N 219 
MET HA   H  N N 220 
MET HB2  H  N N 221 
MET HB3  H  N N 222 
MET HG2  H  N N 223 
MET HG3  H  N N 224 
MET HE1  H  N N 225 
MET HE2  H  N N 226 
MET HE3  H  N N 227 
MET HXT  H  N N 228 
MG  MG   MG N N 229 
PHE N    N  N N 230 
PHE CA   C  N S 231 
PHE C    C  N N 232 
PHE O    O  N N 233 
PHE CB   C  N N 234 
PHE CG   C  Y N 235 
PHE CD1  C  Y N 236 
PHE CD2  C  Y N 237 
PHE CE1  C  Y N 238 
PHE CE2  C  Y N 239 
PHE CZ   C  Y N 240 
PHE OXT  O  N N 241 
PHE H    H  N N 242 
PHE H2   H  N N 243 
PHE HA   H  N N 244 
PHE HB2  H  N N 245 
PHE HB3  H  N N 246 
PHE HD1  H  N N 247 
PHE HD2  H  N N 248 
PHE HE1  H  N N 249 
PHE HE2  H  N N 250 
PHE HZ   H  N N 251 
PHE HXT  H  N N 252 
PRO N    N  N N 253 
PRO CA   C  N S 254 
PRO C    C  N N 255 
PRO O    O  N N 256 
PRO CB   C  N N 257 
PRO CG   C  N N 258 
PRO CD   C  N N 259 
PRO OXT  O  N N 260 
PRO H    H  N N 261 
PRO HA   H  N N 262 
PRO HB2  H  N N 263 
PRO HB3  H  N N 264 
PRO HG2  H  N N 265 
PRO HG3  H  N N 266 
PRO HD2  H  N N 267 
PRO HD3  H  N N 268 
PRO HXT  H  N N 269 
SER N    N  N N 270 
SER CA   C  N S 271 
SER C    C  N N 272 
SER O    O  N N 273 
SER CB   C  N N 274 
SER OG   O  N N 275 
SER OXT  O  N N 276 
SER H    H  N N 277 
SER H2   H  N N 278 
SER HA   H  N N 279 
SER HB2  H  N N 280 
SER HB3  H  N N 281 
SER HG   H  N N 282 
SER HXT  H  N N 283 
THR N    N  N N 284 
THR CA   C  N S 285 
THR C    C  N N 286 
THR O    O  N N 287 
THR CB   C  N R 288 
THR OG1  O  N N 289 
THR CG2  C  N N 290 
THR OXT  O  N N 291 
THR H    H  N N 292 
THR H2   H  N N 293 
THR HA   H  N N 294 
THR HB   H  N N 295 
THR HG1  H  N N 296 
THR HG21 H  N N 297 
THR HG22 H  N N 298 
THR HG23 H  N N 299 
THR HXT  H  N N 300 
TRP N    N  N N 301 
TRP CA   C  N S 302 
TRP C    C  N N 303 
TRP O    O  N N 304 
TRP CB   C  N N 305 
TRP CG   C  Y N 306 
TRP CD1  C  Y N 307 
TRP CD2  C  Y N 308 
TRP NE1  N  Y N 309 
TRP CE2  C  Y N 310 
TRP CE3  C  Y N 311 
TRP CZ2  C  Y N 312 
TRP CZ3  C  Y N 313 
TRP CH2  C  Y N 314 
TRP OXT  O  N N 315 
TRP H    H  N N 316 
TRP H2   H  N N 317 
TRP HA   H  N N 318 
TRP HB2  H  N N 319 
TRP HB3  H  N N 320 
TRP HD1  H  N N 321 
TRP HE1  H  N N 322 
TRP HE3  H  N N 323 
TRP HZ2  H  N N 324 
TRP HZ3  H  N N 325 
TRP HH2  H  N N 326 
TRP HXT  H  N N 327 
TYR N    N  N N 328 
TYR CA   C  N S 329 
TYR C    C  N N 330 
TYR O    O  N N 331 
TYR CB   C  N N 332 
TYR CG   C  Y N 333 
TYR CD1  C  Y N 334 
TYR CD2  C  Y N 335 
TYR CE1  C  Y N 336 
TYR CE2  C  Y N 337 
TYR CZ   C  Y N 338 
TYR OH   O  N N 339 
TYR OXT  O  N N 340 
TYR H    H  N N 341 
TYR H2   H  N N 342 
TYR HA   H  N N 343 
TYR HB2  H  N N 344 
TYR HB3  H  N N 345 
TYR HD1  H  N N 346 
TYR HD2  H  N N 347 
TYR HE1  H  N N 348 
TYR HE2  H  N N 349 
TYR HH   H  N N 350 
TYR HXT  H  N N 351 
VAL N    N  N N 352 
VAL CA   C  N S 353 
VAL C    C  N N 354 
VAL O    O  N N 355 
VAL CB   C  N N 356 
VAL CG1  C  N N 357 
VAL CG2  C  N N 358 
VAL OXT  O  N N 359 
VAL H    H  N N 360 
VAL H2   H  N N 361 
VAL HA   H  N N 362 
VAL HB   H  N N 363 
VAL HG11 H  N N 364 
VAL HG12 H  N N 365 
VAL HG13 H  N N 366 
VAL HG21 H  N N 367 
VAL HG22 H  N N 368 
VAL HG23 H  N N 369 
VAL HXT  H  N N 370 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HOH O   H1   sing N N 129 
HOH O   H2   sing N N 130 
ILE N   CA   sing N N 131 
ILE N   H    sing N N 132 
ILE N   H2   sing N N 133 
ILE CA  C    sing N N 134 
ILE CA  CB   sing N N 135 
ILE CA  HA   sing N N 136 
ILE C   O    doub N N 137 
ILE C   OXT  sing N N 138 
ILE CB  CG1  sing N N 139 
ILE CB  CG2  sing N N 140 
ILE CB  HB   sing N N 141 
ILE CG1 CD1  sing N N 142 
ILE CG1 HG12 sing N N 143 
ILE CG1 HG13 sing N N 144 
ILE CG2 HG21 sing N N 145 
ILE CG2 HG22 sing N N 146 
ILE CG2 HG23 sing N N 147 
ILE CD1 HD11 sing N N 148 
ILE CD1 HD12 sing N N 149 
ILE CD1 HD13 sing N N 150 
ILE OXT HXT  sing N N 151 
LEU N   CA   sing N N 152 
LEU N   H    sing N N 153 
LEU N   H2   sing N N 154 
LEU CA  C    sing N N 155 
LEU CA  CB   sing N N 156 
LEU CA  HA   sing N N 157 
LEU C   O    doub N N 158 
LEU C   OXT  sing N N 159 
LEU CB  CG   sing N N 160 
LEU CB  HB2  sing N N 161 
LEU CB  HB3  sing N N 162 
LEU CG  CD1  sing N N 163 
LEU CG  CD2  sing N N 164 
LEU CG  HG   sing N N 165 
LEU CD1 HD11 sing N N 166 
LEU CD1 HD12 sing N N 167 
LEU CD1 HD13 sing N N 168 
LEU CD2 HD21 sing N N 169 
LEU CD2 HD22 sing N N 170 
LEU CD2 HD23 sing N N 171 
LEU OXT HXT  sing N N 172 
LYS N   CA   sing N N 173 
LYS N   H    sing N N 174 
LYS N   H2   sing N N 175 
LYS CA  C    sing N N 176 
LYS CA  CB   sing N N 177 
LYS CA  HA   sing N N 178 
LYS C   O    doub N N 179 
LYS C   OXT  sing N N 180 
LYS CB  CG   sing N N 181 
LYS CB  HB2  sing N N 182 
LYS CB  HB3  sing N N 183 
LYS CG  CD   sing N N 184 
LYS CG  HG2  sing N N 185 
LYS CG  HG3  sing N N 186 
LYS CD  CE   sing N N 187 
LYS CD  HD2  sing N N 188 
LYS CD  HD3  sing N N 189 
LYS CE  NZ   sing N N 190 
LYS CE  HE2  sing N N 191 
LYS CE  HE3  sing N N 192 
LYS NZ  HZ1  sing N N 193 
LYS NZ  HZ2  sing N N 194 
LYS NZ  HZ3  sing N N 195 
LYS OXT HXT  sing N N 196 
MET N   CA   sing N N 197 
MET N   H    sing N N 198 
MET N   H2   sing N N 199 
MET CA  C    sing N N 200 
MET CA  CB   sing N N 201 
MET CA  HA   sing N N 202 
MET C   O    doub N N 203 
MET C   OXT  sing N N 204 
MET CB  CG   sing N N 205 
MET CB  HB2  sing N N 206 
MET CB  HB3  sing N N 207 
MET CG  SD   sing N N 208 
MET CG  HG2  sing N N 209 
MET CG  HG3  sing N N 210 
MET SD  CE   sing N N 211 
MET CE  HE1  sing N N 212 
MET CE  HE2  sing N N 213 
MET CE  HE3  sing N N 214 
MET OXT HXT  sing N N 215 
PHE N   CA   sing N N 216 
PHE N   H    sing N N 217 
PHE N   H2   sing N N 218 
PHE CA  C    sing N N 219 
PHE CA  CB   sing N N 220 
PHE CA  HA   sing N N 221 
PHE C   O    doub N N 222 
PHE C   OXT  sing N N 223 
PHE CB  CG   sing N N 224 
PHE CB  HB2  sing N N 225 
PHE CB  HB3  sing N N 226 
PHE CG  CD1  doub Y N 227 
PHE CG  CD2  sing Y N 228 
PHE CD1 CE1  sing Y N 229 
PHE CD1 HD1  sing N N 230 
PHE CD2 CE2  doub Y N 231 
PHE CD2 HD2  sing N N 232 
PHE CE1 CZ   doub Y N 233 
PHE CE1 HE1  sing N N 234 
PHE CE2 CZ   sing Y N 235 
PHE CE2 HE2  sing N N 236 
PHE CZ  HZ   sing N N 237 
PHE OXT HXT  sing N N 238 
PRO N   CA   sing N N 239 
PRO N   CD   sing N N 240 
PRO N   H    sing N N 241 
PRO CA  C    sing N N 242 
PRO CA  CB   sing N N 243 
PRO CA  HA   sing N N 244 
PRO C   O    doub N N 245 
PRO C   OXT  sing N N 246 
PRO CB  CG   sing N N 247 
PRO CB  HB2  sing N N 248 
PRO CB  HB3  sing N N 249 
PRO CG  CD   sing N N 250 
PRO CG  HG2  sing N N 251 
PRO CG  HG3  sing N N 252 
PRO CD  HD2  sing N N 253 
PRO CD  HD3  sing N N 254 
PRO OXT HXT  sing N N 255 
SER N   CA   sing N N 256 
SER N   H    sing N N 257 
SER N   H2   sing N N 258 
SER CA  C    sing N N 259 
SER CA  CB   sing N N 260 
SER CA  HA   sing N N 261 
SER C   O    doub N N 262 
SER C   OXT  sing N N 263 
SER CB  OG   sing N N 264 
SER CB  HB2  sing N N 265 
SER CB  HB3  sing N N 266 
SER OG  HG   sing N N 267 
SER OXT HXT  sing N N 268 
THR N   CA   sing N N 269 
THR N   H    sing N N 270 
THR N   H2   sing N N 271 
THR CA  C    sing N N 272 
THR CA  CB   sing N N 273 
THR CA  HA   sing N N 274 
THR C   O    doub N N 275 
THR C   OXT  sing N N 276 
THR CB  OG1  sing N N 277 
THR CB  CG2  sing N N 278 
THR CB  HB   sing N N 279 
THR OG1 HG1  sing N N 280 
THR CG2 HG21 sing N N 281 
THR CG2 HG22 sing N N 282 
THR CG2 HG23 sing N N 283 
THR OXT HXT  sing N N 284 
TRP N   CA   sing N N 285 
TRP N   H    sing N N 286 
TRP N   H2   sing N N 287 
TRP CA  C    sing N N 288 
TRP CA  CB   sing N N 289 
TRP CA  HA   sing N N 290 
TRP C   O    doub N N 291 
TRP C   OXT  sing N N 292 
TRP CB  CG   sing N N 293 
TRP CB  HB2  sing N N 294 
TRP CB  HB3  sing N N 295 
TRP CG  CD1  doub Y N 296 
TRP CG  CD2  sing Y N 297 
TRP CD1 NE1  sing Y N 298 
TRP CD1 HD1  sing N N 299 
TRP CD2 CE2  doub Y N 300 
TRP CD2 CE3  sing Y N 301 
TRP NE1 CE2  sing Y N 302 
TRP NE1 HE1  sing N N 303 
TRP CE2 CZ2  sing Y N 304 
TRP CE3 CZ3  doub Y N 305 
TRP CE3 HE3  sing N N 306 
TRP CZ2 CH2  doub Y N 307 
TRP CZ2 HZ2  sing N N 308 
TRP CZ3 CH2  sing Y N 309 
TRP CZ3 HZ3  sing N N 310 
TRP CH2 HH2  sing N N 311 
TRP OXT HXT  sing N N 312 
TYR N   CA   sing N N 313 
TYR N   H    sing N N 314 
TYR N   H2   sing N N 315 
TYR CA  C    sing N N 316 
TYR CA  CB   sing N N 317 
TYR CA  HA   sing N N 318 
TYR C   O    doub N N 319 
TYR C   OXT  sing N N 320 
TYR CB  CG   sing N N 321 
TYR CB  HB2  sing N N 322 
TYR CB  HB3  sing N N 323 
TYR CG  CD1  doub Y N 324 
TYR CG  CD2  sing Y N 325 
TYR CD1 CE1  sing Y N 326 
TYR CD1 HD1  sing N N 327 
TYR CD2 CE2  doub Y N 328 
TYR CD2 HD2  sing N N 329 
TYR CE1 CZ   doub Y N 330 
TYR CE1 HE1  sing N N 331 
TYR CE2 CZ   sing Y N 332 
TYR CE2 HE2  sing N N 333 
TYR CZ  OH   sing N N 334 
TYR OH  HH   sing N N 335 
TYR OXT HXT  sing N N 336 
VAL N   CA   sing N N 337 
VAL N   H    sing N N 338 
VAL N   H2   sing N N 339 
VAL CA  C    sing N N 340 
VAL CA  CB   sing N N 341 
VAL CA  HA   sing N N 342 
VAL C   O    doub N N 343 
VAL C   OXT  sing N N 344 
VAL CB  CG1  sing N N 345 
VAL CB  CG2  sing N N 346 
VAL CB  HB   sing N N 347 
VAL CG1 HG11 sing N N 348 
VAL CG1 HG12 sing N N 349 
VAL CG1 HG13 sing N N 350 
VAL CG2 HG21 sing N N 351 
VAL CG2 HG22 sing N N 352 
VAL CG2 HG23 sing N N 353 
VAL OXT HXT  sing N N 354 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Wellcome Trust'                                                                      'United Kingdom' 222372/Z/21/Z   1 
'Wellcome Trust'                                                                      'United Kingdom' 222531/Z/21/Z   2 
'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)' 'United States'  5R01HL159175-04 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7kpi 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 2 21 21' 
_space_group.name_Hall        'P 2 2ab (z,x,y)' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9HGG 
_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]   0.022439 
_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]   0.019591 
_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]   0.018215 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . ALA A 1 1   ? 41.33661 9.75677  18.81653 1.000 58.50970  ? 26   ALA A N    1 
ATOM   2    C  CA   . ALA A 1 1   ? 41.07490 11.17226 18.57288 1.000 47.13078  ? 26   ALA A CA   1 
ATOM   3    C  C    . ALA A 1 1   ? 40.92533 11.43789 17.08951 1.000 47.99621  ? 26   ALA A C    1 
ATOM   4    O  O    . ALA A 1 1   ? 41.71026 12.18439 16.50122 1.000 44.60770  ? 26   ALA A O    1 
ATOM   5    C  CB   . ALA A 1 1   ? 42.21349 12.02644 19.15136 1.000 47.45749  ? 26   ALA A CB   1 
ATOM   6    H  HA   . ALA A 1 1   ? 40.24934 11.42622 19.01429 1.000 56.88678  ? 26   ALA A HA   1 
ATOM   7    H  HB1  . ALA A 1 1   ? 43.06319 11.62838 18.90548 1.000 55.45987  ? 26   ALA A HB1  1 
ATOM   8    H  HB2  . ALA A 1 1   ? 42.15109 12.92368 18.78810 1.000 55.45987  ? 26   ALA A HB2  1 
ATOM   9    H  HB3  . ALA A 1 1   ? 42.12827 12.05396 20.11722 1.000 55.45987  ? 26   ALA A HB3  1 
ATOM   10   N  N    . ALA A 1 2   ? 39.93361 10.80668 16.47632 1.000 48.53312  ? 27   ALA A N    1 
ATOM   11   C  CA   . ALA A 1 2   ? 39.63955 11.07313 15.07590 1.000 53.56514  ? 27   ALA A CA   1 
ATOM   12   C  C    . ALA A 1 2   ? 39.39322 12.57116 14.87729 1.000 53.82866  ? 27   ALA A C    1 
ATOM   13   O  O    . ALA A 1 2   ? 38.93277 13.27512 15.78355 1.000 51.84112  ? 27   ALA A O    1 
ATOM   14   C  CB   . ALA A 1 2   ? 38.42365 10.24981 14.64536 1.000 52.63101  ? 27   ALA A CB   1 
ATOM   15   H  H    . ALA A 1 2   ? 39.41966 10.22402 16.84505 1.000 58.56958  ? 27   ALA A H    1 
ATOM   16   H  HA   . ALA A 1 2   ? 40.38426 10.81757 14.50933 1.000 64.60801  ? 27   ALA A HA   1 
ATOM   17   H  HB1  . ALA A 1 2   ? 37.65723 10.51696 15.17652 1.000 63.48706  ? 27   ALA A HB1  1 
ATOM   18   H  HB2  . ALA A 1 2   ? 38.24807 10.41361 13.70555 1.000 63.48706  ? 27   ALA A HB2  1 
ATOM   19   H  HB3  . ALA A 1 2   ? 38.61287 9.30911  14.78745 1.000 63.48706  ? 27   ALA A HB3  1 
ATOM   20   N  N    . LYS A 1 3   ? 39.73671 13.07465 13.69516 1.000 44.97463  ? 28   LYS A N    1 
ATOM   21   C  CA   . LYS A 1 3   ? 39.53571 14.48534 13.37996 1.000 39.62365  ? 28   LYS A CA   1 
ATOM   22   C  C    . LYS A 1 3   ? 38.17418 14.66407 12.70261 1.000 36.96120  ? 28   LYS A C    1 
ATOM   23   O  O    . LYS A 1 3   ? 37.99969 14.32107 11.52427 1.000 36.09393  ? 28   LYS A O    1 
ATOM   24   C  CB   . LYS A 1 3   ? 40.69065 15.00010 12.50979 1.000 47.67691  ? 28   LYS A CB   1 
ATOM   25   C  CG   . LYS A 1 3   ? 40.47242 16.40014 11.91380 1.000 42.43526  ? 28   LYS A CG   1 
ATOM   26   C  CD   . LYS A 1 3   ? 40.33334 17.45241 13.01439 1.000 47.02067  ? 28   LYS A CD   1 
ATOM   27   C  CE   . LYS A 1 3   ? 40.23705 18.85109 12.42630 1.000 43.03053  ? 28   LYS A CE   1 
ATOM   28   N  NZ   . LYS A 1 3   ? 40.12161 19.87035 13.51435 1.000 54.47055  ? 28   LYS A NZ   1 
ATOM   29   H  H    . LYS A 1 3   ? 40.08901 12.61763 13.05750 1.000 54.29939  ? 28   LYS A H    1 
ATOM   30   H  HA   . LYS A 1 3   ? 39.51726 15.00570 14.19836 1.000 46.71852  ? 28   LYS A HA   1 
ATOM   31   H  HB2  . LYS A 1 3   ? 41.49338 15.03597 13.05315 1.000 57.54214  ? 28   LYS A HB2  1 
ATOM   32   H  HB3  . LYS A 1 3   ? 40.81748 14.38472 11.77079 1.000 57.54214  ? 28   LYS A HB3  1 
ATOM   33   H  HG2  . LYS A 1 3   ? 41.23173 16.63631 11.35831 1.000 51.25216  ? 28   LYS A HG2  1 
ATOM   34   H  HG3  . LYS A 1 3   ? 39.66013 16.40212 11.38362 1.000 51.25216  ? 28   LYS A HG3  1 
ATOM   35   H  HD2  . LYS A 1 3   ? 39.52798 17.27923 13.52654 1.000 56.75465  ? 28   LYS A HD2  1 
ATOM   36   H  HD3  . LYS A 1 3   ? 41.10969 17.41685 13.59484 1.000 56.75465  ? 28   LYS A HD3  1 
ATOM   37   H  HE2  . LYS A 1 3   ? 41.03460 19.04118 11.90797 1.000 51.34694  ? 28   LYS A HE2  1 
ATOM   38   H  HE3  . LYS A 1 3   ? 39.45139 18.91231 11.86071 1.000 51.34694  ? 28   LYS A HE3  1 
ATOM   39   H  HZ1  . LYS A 1 3   ? 40.84780 19.85032 14.02850 1.000 65.69450  ? 28   LYS A HZ1  1 
ATOM   40   H  HZ2  . LYS A 1 3   ? 40.03939 20.68356 13.16218 1.000 65.69450  ? 28   LYS A HZ2  1 
ATOM   41   H  HZ3  . LYS A 1 3   ? 39.40714 19.69962 14.01683 1.000 65.69450  ? 28   LYS A HZ3  1 
ATOM   42   N  N    . VAL A 1 4   ? 37.22357 15.22025 13.43124 1.000 39.50627  ? 29   VAL A N    1 
ATOM   43   C  CA   . VAL A 1 4   ? 35.86324 15.44227 12.94125 1.000 35.52555  ? 29   VAL A CA   1 
ATOM   44   C  C    . VAL A 1 4   ? 35.67384 16.93428 12.70846 1.000 36.82721  ? 29   VAL A C    1 
ATOM   45   O  O    . VAL A 1 4   ? 36.18380 17.75897 13.47219 1.000 41.09103  ? 29   VAL A O    1 
ATOM   46   C  CB   . VAL A 1 4   ? 34.83446 14.90448 13.95016 1.000 41.62374  ? 29   VAL A CB   1 
ATOM   47   C  CG1  . VAL A 1 4   ? 33.45346 15.09760 13.43880 1.000 33.96007  ? 29   VAL A CG1  1 
ATOM   48   C  CG2  . VAL A 1 4   ? 35.10640 13.43988 14.27619 1.000 45.23335  ? 29   VAL A CG2  1 
ATOM   49   H  H    . VAL A 1 4   ? 37.34031 15.48828 14.24002 1.000 47.73737  ? 29   VAL A H    1 
ATOM   50   H  HA   . VAL A 1 4   ? 35.73569 14.98726 12.09414 1.000 42.96050  ? 29   VAL A HA   1 
ATOM   51   H  HB   . VAL A 1 4   ? 34.91604 15.40471 14.77721 1.000 50.27833  ? 29   VAL A HB   1 
ATOM   52   H  HG11 . VAL A 1 4   ? 33.49700 15.47944 12.54818 1.000 41.08193  ? 29   VAL A HG11 1 
ATOM   53   H  HG12 . VAL A 1 4   ? 33.00480 14.23812 13.40864 1.000 41.08193  ? 29   VAL A HG12 1 
ATOM   54   H  HG13 . VAL A 1 4   ? 32.97767 15.69841 14.03340 1.000 41.08193  ? 29   VAL A HG13 1 
ATOM   55   H  HG21 . VAL A 1 4   ? 35.46541 13.00237 13.48842 1.000 54.60986  ? 29   VAL A HG21 1 
ATOM   56   H  HG22 . VAL A 1 4   ? 35.74764 13.39181 15.00242 1.000 54.60986  ? 29   VAL A HG22 1 
ATOM   57   H  HG23 . VAL A 1 4   ? 34.27509 13.01553 14.54031 1.000 54.60986  ? 29   VAL A HG23 1 
ATOM   58   N  N    . VAL A 1 5   ? 34.95421 17.27600 11.65488 1.000 38.61175  ? 30   VAL A N    1 
ATOM   59   C  CA   . VAL A 1 5   ? 34.66434 18.65285 11.27541 1.000 35.30657  ? 30   VAL A CA   1 
ATOM   60   C  C    . VAL A 1 5   ? 33.16166 18.76462 11.11398 1.000 33.70453  ? 30   VAL A C    1 
ATOM   61   O  O    . VAL A 1 5   ? 32.58160 18.07046 10.27575 1.000 33.73227  ? 30   VAL A O    1 
ATOM   62   C  CB   . VAL A 1 5   ? 35.36655 19.05229 9.96705  1.000 36.51832  ? 30   VAL A CB   1 
ATOM   63   C  CG1  . VAL A 1 5   ? 34.82416 20.38928 9.46171  1.000 45.20136  ? 30   VAL A CG1  1 
ATOM   64   C  CG2  . VAL A 1 5   ? 36.89004 19.10572 10.14769 1.000 36.13136  ? 30   VAL A CG2  1 
ATOM   65   H  H    . VAL A 1 5   ? 34.60500 16.70315 11.11683 1.000 46.66394  ? 30   VAL A H    1 
ATOM   66   H  HA   . VAL A 1 5   ? 34.95840 19.25410 11.97750 1.000 42.69773  ? 30   VAL A HA   1 
ATOM   67   H  HB   . VAL A 1 5   ? 35.18113 18.37695 9.29591  1.000 44.15183  ? 30   VAL A HB   1 
ATOM   68   H  HG11 . VAL A 1 5   ? 35.44534 20.75760 8.81412  1.000 54.57147  ? 30   VAL A HG11 1 
ATOM   69   H  HG12 . VAL A 1 5   ? 33.96047 20.24259 9.04528  1.000 54.57147  ? 30   VAL A HG12 1 
ATOM   70   H  HG13 . VAL A 1 5   ? 34.73055 20.99619 10.21257 1.000 54.57147  ? 30   VAL A HG13 1 
ATOM   71   H  HG21 . VAL A 1 5   ? 37.09804 19.66656 10.91130 1.000 42.24177  ? 30   VAL A HG21 1 
ATOM   72   H  HG22 . VAL A 1 5   ? 37.22203 18.20668 10.29739 1.000 42.24177  ? 30   VAL A HG22 1 
ATOM   73   H  HG23 . VAL A 1 5   ? 37.29030 19.47690 9.34587  1.000 42.24177  ? 30   VAL A HG23 1 
ATOM   74   N  N    . LYS A 1 6   ? 32.53296 19.63033 11.90688 1.000 32.93258  ? 31   LYS A N    1 
ATOM   75   C  CA   . LYS A 1 6   ? 31.08237 19.70093 12.00950 1.000 30.59841  ? 31   LYS A CA   1 
ATOM   76   C  C    . LYS A 1 6   ? 30.56836 20.95666 11.32596 1.000 37.34816  ? 31   LYS A C    1 
ATOM   77   O  O    . LYS A 1 6   ? 31.14002 22.04120 11.50023 1.000 36.72442  ? 31   LYS A O    1 
ATOM   78   C  CB   . LYS A 1 6   ? 30.60934 19.73430 13.47157 1.000 32.12331  ? 31   LYS A CB   1 
ATOM   79   C  CG   . LYS A 1 6   ? 30.56764 18.38052 14.17865 1.000 41.53140  ? 31   LYS A CG   1 
ATOM   80   C  CD   . LYS A 1 6   ? 30.08859 18.46992 15.65105 1.000 40.35629  ? 31   LYS A CD   1 
ATOM   81   C  CE   . LYS A 1 6   ? 30.11658 17.06674 16.31650 1.000 50.62963  ? 31   LYS A CE   1 
ATOM   82   N  NZ   . LYS A 1 6   ? 30.25991 17.08965 17.80767 1.000 56.71624  ? 31   LYS A NZ   1 
ATOM   83   H  H    . LYS A 1 6   ? 32.93853 20.20052 12.40687 1.000 39.84894  ? 31   LYS A H    1 
ATOM   84   H  HA   . LYS A 1 6   ? 30.71442 18.91570 11.57486 1.000 37.04793  ? 31   LYS A HA   1 
ATOM   85   H  HB2  . LYS A 1 6   ? 31.21175 20.30453 13.97441 1.000 38.87782  ? 31   LYS A HB2  1 
ATOM   86   H  HB3  . LYS A 1 6   ? 29.71102 20.09960 13.49355 1.000 38.87782  ? 31   LYS A HB3  1 
ATOM   87   H  HG2  . LYS A 1 6   ? 29.95694 17.79620 13.70270 1.000 50.16753  ? 31   LYS A HG2  1 
ATOM   88   H  HG3  . LYS A 1 6   ? 31.45938 17.99880 14.17921 1.000 50.16753  ? 31   LYS A HG3  1 
ATOM   89   H  HD2  . LYS A 1 6   ? 30.67564 19.06017 16.14893 1.000 48.75739  ? 31   LYS A HD2  1 
ATOM   90   H  HD3  . LYS A 1 6   ? 29.17933 18.80675 15.67750 1.000 48.75739  ? 31   LYS A HD3  1 
ATOM   91   H  HE2  . LYS A 1 6   ? 29.28667 16.60924 16.10954 1.000 61.08541  ? 31   LYS A HE2  1 
ATOM   92   H  HE3  . LYS A 1 6   ? 30.86808 16.56900 15.95816 1.000 61.08541  ? 31   LYS A HE3  1 
ATOM   93   H  HZ1  . LYS A 1 6   ? 30.27269 16.25826 18.12505 1.000 68.38933  ? 31   LYS A HZ1  1 
ATOM   94   H  HZ2  . LYS A 1 6   ? 31.01801 17.49705 18.03439 1.000 68.38933  ? 31   LYS A HZ2  1 
ATOM   95   H  HZ3  . LYS A 1 6   ? 29.57637 17.52759 18.17248 1.000 68.38933  ? 31   LYS A HZ3  1 
ATOM   96   N  N    . PHE A 1 7   ? 29.46934 20.81837 10.58884 1.000 32.78661  ? 32   PHE A N    1 
ATOM   97   C  CA   . PHE A 1 7   ? 28.77283 22.00612 10.11442 1.000 32.89111  ? 32   PHE A CA   1 
ATOM   98   C  C    . PHE A 1 7   ? 27.27251 21.75654 10.05877 1.000 34.30232  ? 32   PHE A C    1 
ATOM   99   O  O    . PHE A 1 7   ? 26.79117 20.61861 10.01073 1.000 28.91098  ? 32   PHE A O    1 
ATOM   100  C  CB   . PHE A 1 7   ? 29.32003 22.46606 8.76583  1.000 41.27506  ? 32   PHE A CB   1 
ATOM   101  C  CG   . PHE A 1 7   ? 28.64086 21.85339 7.62435  1.000 37.00089  ? 32   PHE A CG   1 
ATOM   102  C  CD1  . PHE A 1 7   ? 29.05408 20.61716 7.17366  1.000 48.12571  ? 32   PHE A CD1  1 
ATOM   103  C  CD2  . PHE A 1 7   ? 27.58580 22.49908 6.99235  1.000 43.29547  ? 32   PHE A CD2  1 
ATOM   104  C  CE1  . PHE A 1 7   ? 28.42439 20.01377 6.11193  1.000 44.94021  ? 32   PHE A CE1  1 
ATOM   105  C  CE2  . PHE A 1 7   ? 26.95673 21.91128 5.93469  1.000 40.14911  ? 32   PHE A CE2  1 
ATOM   106  C  CZ   . PHE A 1 7   ? 27.38621 20.66066 5.48384  1.000 47.49354  ? 32   PHE A CZ   1 
ATOM   107  H  H    . PHE A 1 7   ? 29.11849 20.06803 10.35755 1.000 39.67378  ? 32   PHE A H    1 
ATOM   108  H  HA   . PHE A 1 7   ? 28.90246 22.72441 10.75329 1.000 39.79917  ? 32   PHE A HA   1 
ATOM   109  H  HB2  . PHE A 1 7   ? 29.21225 23.42747 8.69536  1.000 49.85992  ? 32   PHE A HB2  1 
ATOM   110  H  HB3  . PHE A 1 7   ? 30.26010 22.23285 8.71310  1.000 49.85992  ? 32   PHE A HB3  1 
ATOM   111  H  HD1  . PHE A 1 7   ? 29.76525 20.18816 7.59210  1.000 58.08069  ? 32   PHE A HD1  1 
ATOM   112  H  HD2  . PHE A 1 7   ? 27.30760 23.33462 7.29133  1.000 52.28441  ? 32   PHE A HD2  1 
ATOM   113  H  HE1  . PHE A 1 7   ? 28.69825 19.17421 5.82031  1.000 54.25809  ? 32   PHE A HE1  1 
ATOM   114  H  HE2  . PHE A 1 7   ? 26.24588 22.34052 5.51594  1.000 48.50878  ? 32   PHE A HE2  1 
ATOM   115  H  HZ   . PHE A 1 7   ? 26.96751 20.26334 4.75465  1.000 57.32209  ? 32   PHE A HZ   1 
ATOM   116  N  N    . SER A 1 8   ? 26.53769 22.86144 10.06910 1.000 28.90547  ? 33   SER A N    1 
ATOM   117  C  CA   . SER A 1 8   ? 25.10809 22.85485 10.29918 1.000 30.76654  ? 33   SER A CA   1 
ATOM   118  C  C    . SER A 1 8   ? 24.43278 23.48806 9.12296  1.000 26.28374  ? 33   SER A C    1 
ATOM   119  O  O    . SER A 1 8   ? 24.91264 24.49201 8.59538  1.000 29.61418  ? 33   SER A O    1 
ATOM   120  C  CB   . SER A 1 8   ? 24.76046 23.63408 11.54801 1.000 26.88701  ? 33   SER A CB   1 
ATOM   121  O  OG   . SER A 1 8   ? 25.54741 23.13274 12.59822 1.000 42.39845  ? 33   SER A OG   1 
ATOM   122  H  H    . SER A 1 8   ? 26.85886 23.64884 9.94086  1.000 35.01641  ? 33   SER A H    1 
ATOM   123  H  HA   . SER A 1 8   ? 24.79047 21.94426 10.40331 1.000 37.24969  ? 33   SER A HA   1 
ATOM   124  H  HB2  . SER A 1 8   ? 24.95485 24.57470 11.41253 1.000 32.59426  ? 33   SER A HB2  1 
ATOM   125  H  HB3  . SER A 1 8   ? 23.82063 23.51632 11.75720 1.000 32.59426  ? 33   SER A HB3  1 
ATOM   126  H  HG   . SER A 1 8   ? 25.28851 23.45402 13.32989 1.000 51.20799  ? 33   SER A HG   1 
ATOM   127  N  N    . TYR A 1 9   ? 23.32263 22.89788 8.72565  1.000 26.47196  ? 34   TYR A N    1 
ATOM   128  C  CA   . TYR A 1 9   ? 22.55710 23.36144 7.58599  1.000 22.52617  ? 34   TYR A CA   1 
ATOM   129  C  C    . TYR A 1 9   ? 21.11495 23.52832 8.03411  1.000 20.72937  ? 34   TYR A C    1 
ATOM   130  O  O    . TYR A 1 9   ? 20.58239 22.68149 8.74137  1.000 24.68949  ? 34   TYR A O    1 
ATOM   131  C  CB   . TYR A 1 9   ? 22.66318 22.38806 6.44242  1.000 23.43810  ? 34   TYR A CB   1 
ATOM   132  C  CG   . TYR A 1 9   ? 21.98544 22.87020 5.18743  1.000 27.47801  ? 34   TYR A CG   1 
ATOM   133  C  CD1  . TYR A 1 9   ? 22.46841 23.99005 4.49846  1.000 29.14162  ? 34   TYR A CD1  1 
ATOM   134  C  CD2  . TYR A 1 9   ? 20.89279 22.20217 4.66852  1.000 29.68132  ? 34   TYR A CD2  1 
ATOM   135  C  CE1  . TYR A 1 9   ? 21.85844 24.42306 3.36149  1.000 29.02583  ? 34   TYR A CE1  1 
ATOM   136  C  CE2  . TYR A 1 9   ? 20.30220 22.61249 3.49641  1.000 26.39731  ? 34   TYR A CE2  1 
ATOM   137  C  CZ   . TYR A 1 9   ? 20.77981 23.73093 2.86910  1.000 32.28308  ? 34   TYR A CZ   1 
ATOM   138  O  OH   . TYR A 1 9   ? 20.18304 24.15670 1.71365  1.000 29.28422  ? 34   TYR A OH   1 
ATOM   139  H  H    . TYR A 1 9   ? 22.98284 22.20794 9.11052  1.000 32.09619  ? 34   TYR A H    1 
ATOM   140  H  HA   . TYR A 1 9   ? 22.87914 24.21812 7.26460  1.000 27.36124  ? 34   TYR A HA   1 
ATOM   141  H  HB2  . TYR A 1 9   ? 23.60055 22.24400 6.23875  1.000 28.45556  ? 34   TYR A HB2  1 
ATOM   142  H  HB3  . TYR A 1 9   ? 22.24787 21.55110 6.70305  1.000 28.45556  ? 34   TYR A HB3  1 
ATOM   143  H  HD1  . TYR A 1 9   ? 23.21393 24.44257 4.82143  1.000 35.29979  ? 34   TYR A HD1  1 
ATOM   144  H  HD2  . TYR A 1 9   ? 20.55152 21.46358 5.11898  1.000 35.94743  ? 34   TYR A HD2  1 
ATOM   145  H  HE1  . TYR A 1 9   ? 22.16960 25.18123 2.92188  1.000 35.16084  ? 34   TYR A HE1  1 
ATOM   146  H  HE2  . TYR A 1 9   ? 19.58901 22.13707 3.13552  1.000 32.00662  ? 34   TYR A HE2  1 
ATOM   147  H  HH   . TYR A 1 9   ? 20.67331 24.71883 1.32733  1.000 35.47091  ? 34   TYR A HH   1 
ATOM   148  N  N    . MET A 1 10  ? 20.50869 24.63116 7.63616  1.000 24.18450  ? 35   MET A N    1 
ATOM   149  C  CA   . MET A 1 10  ? 19.09462 24.89314 7.84609  1.000 18.69622  ? 35   MET A CA   1 
ATOM   150  C  C    . MET A 1 10  ? 18.33240 24.92462 6.52393  1.000 22.02008  ? 35   MET A C    1 
ATOM   151  O  O    . MET A 1 10  ? 18.68904 25.66454 5.61066  1.000 22.87592  ? 35   MET A O    1 
ATOM   152  C  CB   . MET A 1 10  ? 18.89194 26.23656 8.56076  1.000 26.63646  ? 35   MET A CB   1 
ATOM   153  C  CG   . MET A 1 10  ? 17.54838 26.30826 9.27667  1.000 29.77383  ? 35   MET A CG   1 
ATOM   154  S  SD   . MET A 1 10  ? 17.21327 27.97016 9.87365  1.000 32.15702  ? 35   MET A SD   1 
ATOM   155  C  CE   . MET A 1 10  ? 17.20684 28.89055 8.34845  1.000 37.89065  ? 35   MET A CE   1 
ATOM   156  H  H    . MET A 1 10  ? 20.91088 25.27042 7.22484  1.000 29.35124  ? 35   MET A H    1 
ATOM   157  H  HA   . MET A 1 10  ? 18.74276 24.17185 8.39091  1.000 21.60050  ? 35   MET A HA   1 
ATOM   158  H  HB2  . MET A 1 10  ? 19.59346 26.35525 9.22005  1.000 32.29359  ? 35   MET A HB2  1 
ATOM   159  H  HB3  . MET A 1 10  ? 18.92596 26.95279 7.90750  1.000 32.29359  ? 35   MET A HB3  1 
ATOM   160  H  HG2  . MET A 1 10  ? 16.84230 26.05605 8.66125  1.000 36.05844  ? 35   MET A HG2  1 
ATOM   161  H  HG3  . MET A 1 10  ? 17.55664 25.70592 10.03694 1.000 36.05844  ? 35   MET A HG3  1 
ATOM   162  H  HE1  . MET A 1 10  ? 16.99893 29.81837 8.54036  1.000 45.79863  ? 35   MET A HE1  1 
ATOM   163  H  HE2  . MET A 1 10  ? 18.08291 28.82615 7.93704  1.000 45.79863  ? 35   MET A HE2  1 
ATOM   164  H  HE3  . MET A 1 10  ? 16.53527 28.51663 7.75678  1.000 45.79863  ? 35   MET A HE3  1 
ATOM   165  N  N    . TRP A 1 11  ? 17.24633 24.16557 6.46468  1.000 20.02060  ? 36   TRP A N    1 
ATOM   166  C  CA   . TRP A 1 11  ? 16.35842 24.12708 5.33462  1.000 18.36676  ? 36   TRP A CA   1 
ATOM   167  C  C    . TRP A 1 11  ? 14.94476 24.34807 5.83969  1.000 23.49433  ? 36   TRP A C    1 
ATOM   168  O  O    . TRP A 1 11  ? 14.47123 23.65426 6.75137  1.000 23.03500  ? 36   TRP A O    1 
ATOM   169  C  CB   . TRP A 1 11  ? 16.48789 22.79700 4.60506  1.000 28.04438  ? 36   TRP A CB   1 
ATOM   170  C  CG   . TRP A 1 11  ? 15.64776 22.66454 3.42626  1.000 26.05010  ? 36   TRP A CG   1 
ATOM   171  C  CD1  . TRP A 1 11  ? 15.24328 23.64962 2.58078  1.000 24.64601  ? 36   TRP A CD1  1 
ATOM   172  C  CD2  . TRP A 1 11  ? 15.11630 21.45366 2.91732  1.000 24.17816  ? 36   TRP A CD2  1 
ATOM   173  N  NE1  . TRP A 1 11  ? 14.50342 23.12005 1.58102  1.000 27.99384  ? 36   TRP A NE1  1 
ATOM   174  C  CE2  . TRP A 1 11  ? 14.39458 21.76955 1.77318  1.000 22.57386  ? 36   TRP A CE2  1 
ATOM   175  C  CE3  . TRP A 1 11  ? 15.18055 20.11878 3.33725  1.000 25.51456  ? 36   TRP A CE3  1 
ATOM   176  C  CZ2  . TRP A 1 11  ? 13.74445 20.80099 1.01123  1.000 28.57713  ? 36   TRP A CZ2  1 
ATOM   177  C  CZ3  . TRP A 1 11  ? 14.54271 19.16592 2.59381  1.000 22.43351  ? 36   TRP A CZ3  1 
ATOM   178  C  CH2  . TRP A 1 11  ? 13.83399 19.50202 1.44570  1.000 29.47914  ? 36   TRP A CH2  1 
ATOM   179  H  H    . TRP A 1 11  ? 16.99918 23.64295 7.10138  1.000 24.35457  ? 36   TRP A H    1 
ATOM   180  H  HA   . TRP A 1 11  ? 16.56399 24.83292 4.70183  1.000 22.36996  ? 36   TRP A HA   1 
ATOM   181  H  HB2  . TRP A 1 11  ? 17.40897 22.69034 4.32022  1.000 33.98310  ? 36   TRP A HB2  1 
ATOM   182  H  HB3  . TRP A 1 11  ? 16.24544 22.08492 5.21749  1.000 33.98310  ? 36   TRP A HB3  1 
ATOM   183  H  HD1  . TRP A 1 11  ? 15.44534 24.55239 2.67603  1.000 29.90506  ? 36   TRP A HD1  1 
ATOM   184  H  HE1  . TRP A 1 11  ? 14.15685 23.56098 0.92905  1.000 33.92245  ? 36   TRP A HE1  1 
ATOM   185  H  HE3  . TRP A 1 11  ? 15.64801 19.88566 4.10669  1.000 30.94732  ? 36   TRP A HE3  1 
ATOM   186  H  HZ2  . TRP A 1 11  ? 13.27100 21.02461 0.24264  1.000 34.62241  ? 36   TRP A HZ2  1 
ATOM   187  H  HZ3  . TRP A 1 11  ? 14.58341 18.27599 2.86077  1.000 27.25006  ? 36   TRP A HZ3  1 
ATOM   188  H  HH2  . TRP A 1 11  ? 13.41063 18.83086 0.96072  1.000 35.70481  ? 36   TRP A HH2  1 
ATOM   189  N  N    . THR A 1 12  ? 14.27860 25.33008 5.26162  1.000 20.51055  ? 37   THR A N    1 
ATOM   190  C  CA   . THR A 1 12  ? 12.87477 25.58106 5.55535  1.000 20.48571  ? 37   THR A CA   1 
ATOM   191  C  C    . THR A 1 12  ? 12.01209 25.27428 4.34153  1.000 20.17785  ? 37   THR A C    1 
ATOM   192  O  O    . THR A 1 12  ? 12.25286 25.79768 3.24326  1.000 27.87984  ? 37   THR A O    1 
ATOM   193  C  CB   . THR A 1 12  ? 12.66063 27.02348 5.99696  1.000 24.67125  ? 37   THR A CB   1 
ATOM   194  O  OG1  . THR A 1 12  ? 13.37446 27.25314 7.19096  1.000 27.83353  ? 37   THR A OG1  1 
ATOM   195  C  CG2  . THR A 1 12  ? 11.14927 27.27305 6.25592  1.000 25.05206  ? 37   THR A CG2  1 
ATOM   196  H  H    . THR A 1 12  ? 14.61981 25.87276 4.68832  1.000 24.94250  ? 37   THR A H    1 
ATOM   197  H  HA   . THR A 1 12  ? 12.59642 24.98903 6.27153  1.000 24.91270  ? 37   THR A HA   1 
ATOM   198  H  HB   . THR A 1 12  ? 12.96937 27.63335 5.30875  1.000 29.93534  ? 37   THR A HB   1 
ATOM   199  H  HG1  . THR A 1 12  ? 13.25291 28.04256 7.45104  1.000 33.73009  ? 37   THR A HG1  1 
ATOM   200  H  HG21 . THR A 1 12  ? 10.66939 27.30618 5.41359  1.000 30.39232  ? 37   THR A HG21 1 
ATOM   201  H  HG22 . THR A 1 12  ? 10.78312 26.55749 6.79888  1.000 30.39232  ? 37   THR A HG22 1 
ATOM   202  H  HG23 . THR A 1 12  ? 11.02706 28.11536 6.72119  1.000 30.39232  ? 37   THR A HG23 1 
ATOM   203  N  N    . ILE A 1 13  ? 11.00587 24.43340 4.55140  1.000 20.48939  ? 38   ILE A N    1 
ATOM   204  C  CA   . ILE A 1 13  ? 10.01854 24.10210 3.55046  1.000 21.65629  ? 38   ILE A CA   1 
ATOM   205  C  C    . ILE A 1 13  ? 8.77184  24.91705 3.79474  1.000 17.47311  ? 38   ILE A C    1 
ATOM   206  O  O    . ILE A 1 13  ? 8.18399  24.84436 4.88044  1.000 19.62071  ? 38   ILE A O    1 
ATOM   207  C  CB   . ILE A 1 13  ? 9.70449  22.61161 3.56332  1.000 18.71474  ? 38   ILE A CB   1 
ATOM   208  C  CG1  . ILE A 1 13  ? 10.95047 21.83029 3.15834  1.000 25.43652  ? 38   ILE A CG1  1 
ATOM   209  C  CG2  . ILE A 1 13  ? 8.56821  22.35049 2.58938  1.000 22.72678  ? 38   ILE A CG2  1 
ATOM   210  C  CD1  . ILE A 1 13  ? 10.85596 20.38089 3.48760  1.000 27.76962  ? 38   ILE A CD1  1 
ATOM   211  H  H    . ILE A 1 13  ? 10.87460 24.02902 5.29896  1.000 24.91712  ? 38   ILE A H    1 
ATOM   212  H  HA   . ILE A 1 13  ? 10.36449 24.34617 2.67774  1.000 26.31739  ? 38   ILE A HA   1 
ATOM   213  H  HB   . ILE A 1 13  ? 9.43891  22.32836 4.45221  1.000 22.78754  ? 38   ILE A HB   1 
ATOM   214  H  HG12 . ILE A 1 13  ? 11.07691 21.91265 2.20015  1.000 30.85367  ? 38   ILE A HG12 1 
ATOM   215  H  HG13 . ILE A 1 13  ? 11.71762 22.19494 3.62677  1.000 30.85367  ? 38   ILE A HG13 1 
ATOM   216  H  HG21 . ILE A 1 13  ? 7.73695  22.65679 2.98447  1.000 27.60198  ? 38   ILE A HG21 1 
ATOM   217  H  HG22 . ILE A 1 13  ? 8.74077  22.83336 1.76600  1.000 27.60198  ? 38   ILE A HG22 1 
ATOM   218  H  HG23 . ILE A 1 13  ? 8.51827  21.39847 2.41029  1.000 27.60198  ? 38   ILE A HG23 1 
ATOM   219  H  HD11 . ILE A 1 13  ? 10.54893 20.28427 4.40264  1.000 33.65339  ? 38   ILE A HD11 1 
ATOM   220  H  HD12 . ILE A 1 13  ? 10.22671 19.95970 2.88134  1.000 33.65339  ? 38   ILE A HD12 1 
ATOM   221  H  HD13 . ILE A 1 13  ? 11.73212 19.97669 3.38825  1.000 33.65339  ? 38   ILE A HD13 1 
ATOM   222  N  N    . ASN A 1 14  ? 8.35213  25.65285 2.78577  1.000 23.16604  ? 39   ASN A N    1 
ATOM   223  C  CA   . ASN A 1 14  ? 7.24065  26.57110 2.94089  1.000 26.98949  ? 39   ASN A CA   1 
ATOM   224  C  C    . ASN A 1 14  ? 5.92081  25.90246 2.60909  1.000 26.19802  ? 39   ASN A C    1 
ATOM   225  O  O    . ASN A 1 14  ? 5.86625  24.93914 1.84680  1.000 24.62590  ? 39   ASN A O    1 
ATOM   226  C  CB   . ASN A 1 14  ? 7.42465  27.80516 2.06134  1.000 26.50561  ? 39   ASN A CB   1 
ATOM   227  C  CG   . ASN A 1 14  ? 8.66417  28.56467 2.39683  1.000 25.91140  ? 39   ASN A CG   1 
ATOM   228  O  OD1  . ASN A 1 14  ? 8.66465  29.44284 3.24940  1.000 30.71286  ? 39   ASN A OD1  1 
ATOM   229  N  ND2  . ASN A 1 14  ? 9.73411  28.26255 1.70840  1.000 31.47046  ? 39   ASN A ND2  1 
ATOM   230  H  H    . ASN A 1 14  ? 8.69500  25.63955 1.99719  1.000 28.12909  ? 39   ASN A H    1 
ATOM   231  H  HA   . ASN A 1 14  ? 7.20577  26.85690 3.86717  1.000 32.71724  ? 39   ASN A HA   1 
ATOM   232  H  HB2  . ASN A 1 14  ? 7.48324  27.52769 1.13372  1.000 32.13658  ? 39   ASN A HB2  1 
ATOM   233  H  HB3  . ASN A 1 14  ? 6.66623  28.39748 2.18317  1.000 32.13658  ? 39   ASN A HB3  1 
ATOM   234  H  HD21 . ASN A 1 14  ? 10.47466 28.67153 1.86309  1.000 38.09439  ? 39   ASN A HD21 1 
ATOM   235  H  HD22 . ASN A 1 14  ? 9.69723  27.65490 1.10096  1.000 38.09439  ? 39   ASN A HD22 1 
ATOM   236  N  N    . ASN A 1 15  ? 4.86026  26.43843 3.20343  1.000 30.30568  ? 40   ASN A N    1 
ATOM   237  C  CA   . ASN A 1 15  ? 3.49601  25.95744 3.02171  1.000 29.94222  ? 40   ASN A CA   1 
ATOM   238  C  C    . ASN A 1 15  ? 3.44487  24.43612 3.13020  1.000 25.43663  ? 40   ASN A C    1 
ATOM   239  O  O    . ASN A 1 15  ? 3.04540  23.72804 2.22125  1.000 34.05238  ? 40   ASN A O    1 
ATOM   240  C  CB   . ASN A 1 15  ? 2.96173  26.45760 1.68403  1.000 28.38268  ? 40   ASN A CB   1 
ATOM   241  C  CG   . ASN A 1 15  ? 3.54281  27.79776 1.29106  1.000 31.70741  ? 40   ASN A CG   1 
ATOM   242  O  OD1  . ASN A 1 15  ? 4.33736  27.90245 0.34921  1.000 39.54092  ? 40   ASN A OD1  1 
ATOM   243  N  ND2  . ASN A 1 15  ? 3.19296  28.81958 2.03995  1.000 37.97766  ? 40   ASN A ND2  1 
ATOM   244  H  H    . ASN A 1 15  ? 4.90772  27.10970 3.73891  1.000 36.69666  ? 40   ASN A H    1 
ATOM   245  H  HA   . ASN A 1 15  ? 2.92607  26.30295 3.72647  1.000 36.26051  ? 40   ASN A HA   1 
ATOM   246  H  HB2  . ASN A 1 15  ? 3.18932  25.81671 0.99240  1.000 34.38906  ? 40   ASN A HB2  1 
ATOM   247  H  HB3  . ASN A 1 15  ? 1.99831  26.55338 1.74354  1.000 34.38906  ? 40   ASN A HB3  1 
ATOM   248  H  HD21 . ASN A 1 15  ? 2.66341  28.70222 2.70734  1.000 45.90303  ? 40   ASN A HD21 1 
ATOM   249  H  HD22 . ASN A 1 15  ? 3.49358  29.60556 1.86260  1.000 45.90303  ? 40   ASN A HD22 1 
ATOM   250  N  N    . PHE A 1 16  ? 3.90585  23.92552 4.26162  1.000 29.62632  ? 41   PHE A N    1 
ATOM   251  C  CA   . PHE A 1 16  ? 4.14628  22.49207 4.30697  1.000 27.40980  ? 41   PHE A CA   1 
ATOM   252  C  C    . PHE A 1 16  ? 2.84266  21.70008 4.29760  1.000 29.97629  ? 41   PHE A C    1 
ATOM   253  O  O    . PHE A 1 16  ? 2.74164  20.64961 3.64938  1.000 34.02204  ? 41   PHE A O    1 
ATOM   254  C  CB   . PHE A 1 16  ? 4.94727  22.13723 5.53113  1.000 31.15076  ? 41   PHE A CB   1 
ATOM   255  C  CG   . PHE A 1 16  ? 5.14230  20.66835 5.68556  1.000 28.40175  ? 41   PHE A CG   1 
ATOM   256  C  CD1  . PHE A 1 16  ? 6.15637  20.03384 4.99987  1.000 25.24200  ? 41   PHE A CD1  1 
ATOM   257  C  CD2  . PHE A 1 16  ? 4.28175  19.92048 6.46746  1.000 30.40153  ? 41   PHE A CD2  1 
ATOM   258  C  CE1  . PHE A 1 16  ? 6.33799  18.68387 5.14885  1.000 22.91593  ? 41   PHE A CE1  1 
ATOM   259  C  CE2  . PHE A 1 16  ? 4.44673  18.56812 6.59085  1.000 32.16604  ? 41   PHE A CE2  1 
ATOM   260  C  CZ   . PHE A 1 16  ? 5.49749  17.95278 5.91740  1.000 26.26950  ? 41   PHE A CZ   1 
ATOM   261  H  H    . PHE A 1 16  ? 4.07917  24.36361 4.98109  1.000 35.88142  ? 41   PHE A H    1 
ATOM   262  H  HA   . PHE A 1 16  ? 4.65746  22.24824 3.51948  1.000 33.22160  ? 41   PHE A HA   1 
ATOM   263  H  HB2  . PHE A 1 16  ? 5.82209  22.55136 5.46716  1.000 37.71075  ? 41   PHE A HB2  1 
ATOM   264  H  HB3  . PHE A 1 16  ? 4.48274  22.46298 6.31790  1.000 37.71075  ? 41   PHE A HB3  1 
ATOM   265  H  HD1  . PHE A 1 16  ? 6.71529  20.52054 4.43805  1.000 30.62024  ? 41   PHE A HD1  1 
ATOM   266  H  HD2  . PHE A 1 16  ? 3.58314  20.34131 6.91438  1.000 36.81169  ? 41   PHE A HD2  1 
ATOM   267  H  HE1  . PHE A 1 16  ? 7.04712  18.26513 4.71678  1.000 27.82896  ? 41   PHE A HE1  1 
ATOM   268  H  HE2  . PHE A 1 16  ? 3.86552  18.06765 7.11678  1.000 38.92909  ? 41   PHE A HE2  1 
ATOM   269  H  HZ   . PHE A 1 16  ? 5.62281  17.03460 5.99582  1.000 31.85324  ? 41   PHE A HZ   1 
ATOM   270  N  N    . SER A 1 17  ? 1.83420  22.16920 5.02167  1.000 34.14271  ? 42   SER A N    1 
ATOM   271  C  CA   . SER A 1 17  ? 0.54080  21.49071 4.97520  1.000 30.00950  ? 42   SER A CA   1 
ATOM   272  C  C    . SER A 1 17  ? 0.04397  21.28127 3.54223  1.000 35.88100  ? 42   SER A C    1 
ATOM   273  O  O    . SER A 1 17  ? -0.62970 20.28112 3.25897  1.000 46.44265  ? 42   SER A O    1 
ATOM   274  C  CB   . SER A 1 17  ? -0.48471 22.29284 5.77446  1.000 37.36575  ? 42   SER A CB   1 
ATOM   275  O  OG   . SER A 1 17  ? -0.77764 23.52042 5.10691  1.000 37.78918  ? 42   SER A OG   1 
ATOM   276  H  H    . SER A 1 17  ? 1.86841  22.85874 5.53447  1.000 41.30109  ? 42   SER A H    1 
ATOM   277  H  HA   . SER A 1 17  ? 0.63570  20.61454 5.38042  1.000 36.34124  ? 42   SER A HA   1 
ATOM   278  H  HB2  . SER A 1 17  ? -1.29974 21.77366 5.85856  1.000 45.16875  ? 42   SER A HB2  1 
ATOM   279  H  HB3  . SER A 1 17  ? -0.12267 22.48668 6.65324  1.000 45.16875  ? 42   SER A HB3  1 
ATOM   280  H  HG   . SER A 1 17  ? -0.06473 23.89366 4.86599  1.000 45.67686  ? 42   SER A HG   1 
ATOM   281  N  N    . PHE A 1 18  ? 0.34691  22.21074 2.63321  1.000 31.45131  ? 43   PHE A N    1 
ATOM   282  C  CA   . PHE A 1 18  ? -0.11716 22.17156 1.26048  1.000 28.31445  ? 43   PHE A CA   1 
ATOM   283  C  C    . PHE A 1 18  ? 0.66257  21.19791 0.37365  1.000 33.41659  ? 43   PHE A C    1 
ATOM   284  O  O    . PHE A 1 18  ? 0.35491  21.09717 -0.81267 1.000 30.25118  ? 43   PHE A O    1 
ATOM   285  C  CB   . PHE A 1 18  ? -0.03644 23.58352 0.65499  1.000 35.42954  ? 43   PHE A CB   1 
ATOM   286  H  H    . PHE A 1 18  ? 0.83834  22.89639 2.80046  1.000 38.07142  ? 43   PHE A H    1 
ATOM   287  H  HA   . PHE A 1 18  ? -1.04258 21.88087 1.26060  1.000 34.30718  ? 43   PHE A HA   1 
ATOM   288  N  N    . CYS A 1 19  ? 1.65238  20.47093 0.89961  1.000 35.70376  ? 44   CYS A N    1 
ATOM   289  C  CA   . CYS A 1 19  ? 2.43589  19.56284 0.06161  1.000 36.27081  ? 44   CYS A CA   1 
ATOM   290  C  C    . CYS A 1 19  ? 1.55569  18.44759 -0.48971 1.000 33.64791  ? 44   CYS A C    1 
ATOM   291  O  O    . CYS A 1 19  ? 0.81673  17.80727 0.25505  1.000 33.89576  ? 44   CYS A O    1 
ATOM   292  C  CB   . CYS A 1 19  ? 3.57618  18.95072 0.87905  1.000 35.73142  ? 44   CYS A CB   1 
ATOM   293  S  SG   . CYS A 1 19  ? 4.99499  20.00752 1.22048  1.000 35.25789  ? 44   CYS A SG   1 
ATOM   294  H  H    . CYS A 1 19  ? 1.88636  20.48552 1.72703  1.000 43.17436  ? 44   CYS A H    1 
ATOM   295  H  HA   . CYS A 1 19  ? 2.81014  20.06258 -0.68075 1.000 43.85482  ? 44   CYS A HA   1 
ATOM   296  H  HB2  . CYS A 1 19  ? 3.21565  18.67607 1.73665  1.000 43.20754  ? 44   CYS A HB2  1 
ATOM   297  H  HB3  . CYS A 1 19  ? 3.90914  18.17805 0.39633  1.000 43.20754  ? 44   CYS A HB3  1 
ATOM   298  H  HG   . CYS A 1 19  ? 5.80088  19.38619 1.85648  1.000 42.63931  ? 44   CYS A HG   1 
ATOM   299  N  N    . ARG A 1 20  ? 1.65303  18.18957 -1.79921 1.000 28.38219  ? 45   ARG A N    1 
ATOM   300  C  CA   . ARG A 1 20  ? 0.81807  17.17133 -2.43171 1.000 33.43453  ? 45   ARG A CA   1 
ATOM   301  C  C    . ARG A 1 20  ? 1.61756  15.92446 -2.77031 1.000 36.67247  ? 45   ARG A C    1 
ATOM   302  O  O    . ARG A 1 20  ? 1.09855  15.02781 -3.44003 1.000 35.21789  ? 45   ARG A O    1 
ATOM   303  C  CB   . ARG A 1 20  ? 0.13096  17.71799 -3.68250 1.000 29.41559  ? 45   ARG A CB   1 
ATOM   304  H  H    . ARG A 1 20  ? 2.19293  18.59061 -2.33520 1.000 34.38848  ? 45   ARG A H    1 
ATOM   305  H  HA   . ARG A 1 20  ? 0.11224  16.92570 -1.81335 1.000 40.45128  ? 45   ARG A HA   1 
ATOM   306  N  N    . GLU A 1 21  ? 2.86461  15.84596 -2.33014 1.000 25.69339  ? 46   GLU A N    1 
ATOM   307  C  CA   . GLU A 1 21  ? 3.65272  14.64571 -2.55671 1.000 27.20764  ? 46   GLU A CA   1 
ATOM   308  C  C    . GLU A 1 21  ? 3.01437  13.49630 -1.80005 1.000 28.99724  ? 46   GLU A C    1 
ATOM   309  O  O    . GLU A 1 21  ? 2.51788  13.66829 -0.68356 1.000 24.79680  ? 46   GLU A O    1 
ATOM   310  C  CB   . GLU A 1 21  ? 5.10061  14.83334 -2.09927 1.000 27.32683  ? 46   GLU A CB   1 
ATOM   311  C  CG   . GLU A 1 21  ? 6.00459  15.64990 -3.05304 1.000 27.98714  ? 46   GLU A CG   1 
ATOM   312  C  CD   . GLU A 1 21  ? 5.81307  17.15366 -2.94995 1.000 29.36519  ? 46   GLU A CD   1 
ATOM   313  O  OE1  . GLU A 1 21  ? 5.00332  17.57230 -2.10593 1.000 31.19087  ? 46   GLU A OE1  1 
ATOM   314  O  OE2  . GLU A 1 21  ? 6.43227  17.90807 -3.74413 1.000 27.96885  ? 46   GLU A OE2  1 
ATOM   315  H  H    . GLU A 1 21  ? 3.27478  16.46826 -1.90106 1.000 31.16191  ? 46   GLU A H    1 
ATOM   316  H  HA   . GLU A 1 21  ? 3.68101  14.44600 -3.50551 1.000 32.97902  ? 46   GLU A HA   1 
ATOM   317  H  HB2  . GLU A 1 21  ? 5.09278  15.29373 -1.24553 1.000 33.12204  ? 46   GLU A HB2  1 
ATOM   318  H  HB3  . GLU A 1 21  ? 5.50435  13.95697 -1.99991 1.000 33.12204  ? 46   GLU A HB3  1 
ATOM   319  H  HG2  . GLU A 1 21  ? 6.93196  15.45608 -2.84494 1.000 33.91441  ? 46   GLU A HG2  1 
ATOM   320  H  HG3  . GLU A 1 21  ? 5.80825  15.38986 -3.96668 1.000 33.91441  ? 46   GLU A HG3  1 
ATOM   321  N  N    . GLU A 1 22  ? 3.03148  12.32465 -2.40890 1.000 27.22440  ? 47   GLU A N    1 
ATOM   322  C  CA   . GLU A 1 22  ? 2.51103  11.12879 -1.76867 1.000 29.08176  ? 47   GLU A CA   1 
ATOM   323  C  C    . GLU A 1 22  ? 3.65026  10.17832 -1.42353 1.000 32.94961  ? 47   GLU A C    1 
ATOM   324  O  O    . GLU A 1 22  ? 4.83046  10.47716 -1.59499 1.000 30.81841  ? 47   GLU A O    1 
ATOM   325  C  CB   . GLU A 1 22  ? 1.47456  10.45351 -2.66266 1.000 32.47179  ? 47   GLU A CB   1 
ATOM   326  C  CG   . GLU A 1 22  ? 0.13291  11.19841 -2.73744 1.000 38.23130  ? 47   GLU A CG   1 
ATOM   327  C  CD   . GLU A 1 22  ? -0.64269 11.15520 -1.42147 1.000 45.18890  ? 47   GLU A CD   1 
ATOM   328  O  OE1  . GLU A 1 22  ? -0.50156 10.16432 -0.65748 1.000 39.76906  ? 47   GLU A OE1  1 
ATOM   329  O  OE2  . GLU A 1 22  ? -1.39144 12.12623 -1.15138 1.000 44.53850  ? 47   GLU A OE2  1 
ATOM   330  H  H    . GLU A 1 22  ? 3.34217  12.19543 -3.20033 1.000 32.99912  ? 47   GLU A H    1 
ATOM   331  H  HA   . GLU A 1 22  ? 2.07634  11.38296 -0.93961 1.000 35.22796  ? 47   GLU A HA   1 
ATOM   332  H  HB2  . GLU A 1 22  ? 1.83082  10.39628 -3.56306 1.000 39.29599  ? 47   GLU A HB2  1 
ATOM   333  H  HB3  . GLU A 1 22  ? 1.29928  9.56389  -2.31806 1.000 39.29599  ? 47   GLU A HB3  1 
ATOM   334  H  HG2  . GLU A 1 22  ? 0.29974  12.12848 -2.95663 1.000 46.20740  ? 47   GLU A HG2  1 
ATOM   335  H  HG3  . GLU A 1 22  ? -0.41766 10.78950 -3.42341 1.000 46.20740  ? 47   GLU A HG3  1 
ATOM   336  N  N    . MET A 1 23  ? 3.28257  9.04939  -0.83476 1.000 32.87883  ? 48   MET A N    1 
ATOM   337  C  CA   . MET A 1 23  ? 4.21213  7.95927  -0.59938 1.000 32.46549  ? 48   MET A CA   1 
ATOM   338  C  C    . MET A 1 23  ? 5.16431  7.85250  -1.77374 1.000 30.59182  ? 48   MET A C    1 
ATOM   339  O  O    . MET A 1 23  ? 4.75090  7.71166  -2.91776 1.000 32.99073  ? 48   MET A O    1 
ATOM   340  C  CB   . MET A 1 23  ? 3.39260  6.68251  -0.47914 1.000 36.62298  ? 48   MET A CB   1 
ATOM   341  C  CG   . MET A 1 23  ? 3.71160  5.77962  0.67468  1.000 43.22697  ? 48   MET A CG   1 
ATOM   342  S  SD   . MET A 1 23  ? 3.26251  4.07811  0.24675  1.000 61.96303  ? 48   MET A SD   1 
ATOM   343  C  CE   . MET A 1 23  ? 1.59315  4.27781  -0.40311 1.000 51.92087  ? 48   MET A CE   1 
ATOM   344  H  H    . MET A 1 23  ? 2.48449  8.88871  -0.55754 1.000 39.78444  ? 48   MET A H    1 
ATOM   345  H  HA   . MET A 1 23  ? 4.71678  8.09200  0.21831  1.000 39.28843  ? 48   MET A HA   1 
ATOM   346  H  HB2  . MET A 1 23  ? 2.45927  6.93233  -0.39325 1.000 44.27743  ? 48   MET A HB2  1 
ATOM   347  H  HB3  . MET A 1 23  ? 3.52424  6.16444  -1.28857 1.000 44.27743  ? 48   MET A HB3  1 
ATOM   348  H  HG2  . MET A 1 23  ? 4.66161  5.81496  0.86737  1.000 52.20221  ? 48   MET A HG2  1 
ATOM   349  H  HG3  . MET A 1 23  ? 3.20438  6.05166  1.45547  1.000 52.20221  ? 48   MET A HG3  1 
ATOM   350  H  HE1  . MET A 1 23  ? 1.24519  3.40744  -0.65267 1.000 62.63489  ? 48   MET A HE1  1 
ATOM   351  H  HE2  . MET A 1 23  ? 1.03271  4.67396  0.28236  1.000 62.63489  ? 48   MET A HE2  1 
ATOM   352  H  HE3  . MET A 1 23  ? 1.62411  4.85700  -1.18060 1.000 62.63489  ? 48   MET A HE3  1 
ATOM   353  N  N    . GLY A 1 24  ? 6.46703  7.92698  -1.49595 1.000 30.99505  ? 49   GLY A N    1 
ATOM   354  C  CA   . GLY A 1 24  ? 7.47452  7.65614  -2.48883 1.000 29.23838  ? 49   GLY A CA   1 
ATOM   355  C  C    . GLY A 1 24  ? 8.02706  8.90218  -3.14967 1.000 30.18331  ? 49   GLY A C    1 
ATOM   356  O  O    . GLY A 1 24  ? 9.16537  8.89497  -3.62346 1.000 27.74040  ? 49   GLY A O    1 
ATOM   357  H  H    . GLY A 1 24  ? 6.78343  8.13660  -0.72423 1.000 37.52390  ? 49   GLY A H    1 
ATOM   358  H  HA2  . GLY A 1 24  ? 8.21209  7.18567  -2.06985 1.000 35.41590  ? 49   GLY A HA2  1 
ATOM   359  H  HA3  . GLY A 1 24  ? 7.09283  7.09305  -3.18031 1.000 35.41590  ? 49   GLY A HA3  1 
ATOM   360  N  N    . GLU A 1 25  ? 7.24187  9.96473  -3.18457 1.000 32.24585  ? 50   GLU A N    1 
ATOM   361  C  CA   . GLU A 1 25  ? 7.66422  11.19307 -3.82618 1.000 24.85703  ? 50   GLU A CA   1 
ATOM   362  C  C    . GLU A 1 25  ? 8.57273  11.95568 -2.88170 1.000 29.13726  ? 50   GLU A C    1 
ATOM   363  O  O    . GLU A 1 25  ? 8.44781  11.88509 -1.65511 1.000 27.55442  ? 50   GLU A O    1 
ATOM   364  C  CB   . GLU A 1 25  ? 6.44018  12.02172 -4.17672 1.000 26.80454  ? 50   GLU A CB   1 
ATOM   365  C  CG   . GLU A 1 25  ? 5.40120  11.25491 -4.99306 1.000 33.49332  ? 50   GLU A CG   1 
ATOM   366  C  CD   . GLU A 1 25  ? 4.48274  12.16747 -5.74644 1.000 37.52372  ? 50   GLU A CD   1 
ATOM   367  O  OE1  . GLU A 1 25  ? 3.53663  12.65365 -5.10891 1.000 35.40530  ? 50   GLU A OE1  1 
ATOM   368  O  OE2  . GLU A 1 25  ? 4.67449  12.36264 -6.97230 1.000 51.67600  ? 50   GLU A OE2  1 
ATOM   369  H  H    . GLU A 1 25  ? 6.45416  9.99940  -2.84119 1.000 39.02486  ? 50   GLU A H    1 
ATOM   370  H  HA   . GLU A 1 25  ? 8.15174  11.01758 -4.64620 1.000 30.15828  ? 50   GLU A HA   1 
ATOM   371  H  HB2  . GLU A 1 25  ? 6.01557  12.31582 -3.35568 1.000 32.49529  ? 50   GLU A HB2  1 
ATOM   372  H  HB3  . GLU A 1 25  ? 6.72094  12.78969 -4.69855 1.000 32.49529  ? 50   GLU A HB3  1 
ATOM   373  H  HG2  . GLU A 1 25  ? 5.85673  10.68810 -5.63502 1.000 40.52182  ? 50   GLU A HG2  1 
ATOM   374  H  HG3  . GLU A 1 25  ? 4.86379  10.71285 -4.39451 1.000 40.52182  ? 50   GLU A HG3  1 
ATOM   375  N  N    . VAL A 1 26  ? 9.46645  12.72629 -3.45128 1.000 26.88302  ? 51   VAL A N    1 
ATOM   376  C  CA   . VAL A 1 26  ? 10.51789 13.33201 -2.66536 1.000 22.07328  ? 51   VAL A CA   1 
ATOM   377  C  C    . VAL A 1 26  ? 10.54164 14.82965 -2.91440 1.000 21.69129  ? 51   VAL A C    1 
ATOM   378  O  O    . VAL A 1 26  ? 10.25331 15.29674 -4.01556 1.000 25.03637  ? 51   VAL A O    1 
ATOM   379  C  CB   . VAL A 1 26  ? 11.87513 12.69148 -3.00592 1.000 25.38708  ? 51   VAL A CB   1 
ATOM   380  C  CG1  . VAL A 1 26  ? 12.28270 13.07600 -4.40770 1.000 25.01974  ? 51   VAL A CG1  1 
ATOM   381  C  CG2  . VAL A 1 26  ? 12.91949 13.16012 -2.01232 1.000 29.88442  ? 51   VAL A CG2  1 
ATOM   382  H  H    . VAL A 1 26  ? 9.48730  12.91486 -4.29009 1.000 32.58947  ? 51   VAL A H    1 
ATOM   383  H  HA   . VAL A 1 26  ? 10.33531 13.20916 -1.72066 1.000 26.81778  ? 51   VAL A HA   1 
ATOM   384  H  HB   . VAL A 1 26  ? 11.80531 11.72525 -2.95653 1.000 30.79434  ? 51   VAL A HB   1 
ATOM   385  H  HG11 . VAL A 1 26  ? 13.13367 12.65901 -4.61476 1.000 30.35354  ? 51   VAL A HG11 1 
ATOM   386  H  HG12 . VAL A 1 26  ? 11.60411 12.76924 -5.02924 1.000 30.35354  ? 51   VAL A HG12 1 
ATOM   387  H  HG13 . VAL A 1 26  ? 12.36610 14.04105 -4.45882 1.000 30.35354  ? 51   VAL A HG13 1 
ATOM   388  H  HG21 . VAL A 1 26  ? 13.76961 12.74626 -2.22891 1.000 36.19114  ? 51   VAL A HG21 1 
ATOM   389  H  HG22 . VAL A 1 26  ? 12.99776 14.12535 -2.06809 1.000 36.19114  ? 51   VAL A HG22 1 
ATOM   390  H  HG23 . VAL A 1 26  ? 12.64386 12.90167 -1.11894 1.000 36.19114  ? 51   VAL A HG23 1 
ATOM   391  N  N    . ILE A 1 27  ? 10.87299 15.57724 -1.87173 1.000 25.84293  ? 52   ILE A N    1 
ATOM   392  C  CA   . ILE A 1 27  ? 11.28108 16.97085 -1.98090 1.000 21.20826  ? 52   ILE A CA   1 
ATOM   393  C  C    . ILE A 1 27  ? 12.77240 17.03451 -1.67833 1.000 24.76396  ? 52   ILE A C    1 
ATOM   394  O  O    . ILE A 1 27  ? 13.19372 16.60690 -0.59908 1.000 22.24714  ? 52   ILE A O    1 
ATOM   395  C  CB   . ILE A 1 27  ? 10.51360 17.86192 -0.99148 1.000 21.71499  ? 52   ILE A CB   1 
ATOM   396  C  CG1  . ILE A 1 27  ? 9.02436  17.88286 -1.28643 1.000 36.04136  ? 52   ILE A CG1  1 
ATOM   397  C  CG2  . ILE A 1 27  ? 11.05462 19.28293 -1.05311 1.000 31.20229  ? 52   ILE A CG2  1 
ATOM   398  C  CD1  . ILE A 1 27  ? 8.24986  18.69239 -0.24549 1.000 35.37087  ? 52   ILE A CD1  1 
ATOM   399  H  H    . ILE A 1 27  ? 10.86906 15.28922 -1.06140 1.000 31.34136  ? 52   ILE A H    1 
ATOM   400  H  HA   . ILE A 1 27  ? 11.11312 17.28646 -2.88260 1.000 25.77976  ? 52   ILE A HA   1 
ATOM   401  H  HB   . ILE A 1 27  ? 10.64160 17.48790 -0.10569 1.000 26.38783  ? 52   ILE A HB   1 
ATOM   402  H  HG12 . ILE A 1 27  ? 8.87678  18.28564 -2.15643 1.000 43.57948  ? 52   ILE A HG12 1 
ATOM   403  H  HG13 . ILE A 1 27  ? 8.68468  16.97431 -1.27955 1.000 43.57948  ? 52   ILE A HG13 1 
ATOM   404  H  HG21 . ILE A 1 27  ? 10.98526 19.60801 -1.96438 1.000 37.77259  ? 52   ILE A HG21 1 
ATOM   405  H  HG22 . ILE A 1 27  ? 10.53219 19.84573 -0.46047 1.000 37.77259  ? 52   ILE A HG22 1 
ATOM   406  H  HG23 . ILE A 1 27  ? 11.98324 19.27972 -0.77283 1.000 37.77259  ? 52   ILE A HG23 1 
ATOM   407  H  HD11 . ILE A 1 27  ? 8.60238  18.49290 0.63589  1.000 42.77489  ? 52   ILE A HD11 1 
ATOM   408  H  HD12 . ILE A 1 27  ? 8.35534  19.63725 -0.43786 1.000 42.77489  ? 52   ILE A HD12 1 
ATOM   409  H  HD13 . ILE A 1 27  ? 7.31206  18.44852 -0.28964 1.000 42.77489  ? 52   ILE A HD13 1 
ATOM   410  N  N    . LYS A 1 28  ? 13.56221 17.60254 -2.58782 1.000 25.63992  ? 53   LYS A N    1 
ATOM   411  C  CA   . LYS A 1 28  ? 14.99919 17.76460 -2.36801 1.000 23.56448  ? 53   LYS A CA   1 
ATOM   412  C  C    . LYS A 1 28  ? 15.33077 19.21045 -1.98877 1.000 29.57182  ? 53   LYS A C    1 
ATOM   413  O  O    . LYS A 1 28  ? 14.78963 20.16475 -2.56107 1.000 24.67290  ? 53   LYS A O    1 
ATOM   414  C  CB   . LYS A 1 28  ? 15.79755 17.36255 -3.61813 1.000 34.94323  ? 53   LYS A CB   1 
ATOM   415  C  CG   . LYS A 1 28  ? 15.31422 16.06304 -4.29840 1.000 43.41371  ? 53   LYS A CG   1 
ATOM   416  C  CD   . LYS A 1 28  ? 15.54687 15.98851 -5.83045 1.000 54.44450  ? 53   LYS A CD   1 
ATOM   417  C  CE   . LYS A 1 28  ? 15.42168 14.53508 -6.38658 1.000 45.59620  ? 53   LYS A CE   1 
ATOM   418  N  NZ   . LYS A 1 28  ? 16.16516 13.49772 -5.59552 1.000 51.27139  ? 53   LYS A NZ   1 
ATOM   419  H  H    . LYS A 1 28  ? 13.28759 17.90402 -3.34498 1.000 31.09775  ? 53   LYS A H    1 
ATOM   420  H  HA   . LYS A 1 28  ? 15.26783 17.19187 -1.63268 1.000 28.60722  ? 53   LYS A HA   1 
ATOM   421  H  HB2  . LYS A 1 28  ? 15.72981 18.07710 -4.27060 1.000 42.26172  ? 53   LYS A HB2  1 
ATOM   422  H  HB3  . LYS A 1 28  ? 16.72450 17.23239 -3.36370 1.000 42.26172  ? 53   LYS A HB3  1 
ATOM   423  H  HG2  . LYS A 1 28  ? 15.78445 15.31473 -3.89864 1.000 52.42629  ? 53   LYS A HG2  1 
ATOM   424  H  HG3  . LYS A 1 28  ? 14.36021 15.97447 -4.14701 1.000 52.42629  ? 53   LYS A HG3  1 
ATOM   425  H  HD2  . LYS A 1 28  ? 14.88609 16.53933 -6.27864 1.000 65.66324  ? 53   LYS A HD2  1 
ATOM   426  H  HD3  . LYS A 1 28  ? 16.43926 16.31106 -6.03169 1.000 65.66324  ? 53   LYS A HD3  1 
ATOM   427  H  HE2  . LYS A 1 28  ? 14.48464 14.28439 -6.38885 1.000 55.04528  ? 53   LYS A HE2  1 
ATOM   428  H  HE3  . LYS A 1 28  ? 15.77166 14.51877 -7.29110 1.000 55.04528  ? 53   LYS A HE3  1 
ATOM   429  H  HZ1  . LYS A 1 28  ? 16.04883 12.69476 -5.96135 1.000 61.85551  ? 53   LYS A HZ1  1 
ATOM   430  H  HZ2  . LYS A 1 28  ? 17.03463 13.68754 -5.58597 1.000 61.85551  ? 53   LYS A HZ2  1 
ATOM   431  H  HZ3  . LYS A 1 28  ? 15.86418 13.47996 -4.75815 1.000 61.85551  ? 53   LYS A HZ3  1 
ATOM   432  N  N    . SER A 1 29  ? 16.24474 19.36482 -1.04244 1.000 26.90171  ? 54   SER A N    1 
ATOM   433  C  CA   . SER A 1 29  ? 16.78447 20.67101 -0.75391 1.000 20.84030  ? 54   SER A CA   1 
ATOM   434  C  C    . SER A 1 29  ? 17.77379 21.07891 -1.82545 1.000 18.96987  ? 54   SER A C    1 
ATOM   435  O  O    . SER A 1 29  ? 18.15655 20.30153 -2.69877 1.000 24.65134  ? 54   SER A O    1 
ATOM   436  C  CB   . SER A 1 29  ? 17.48149 20.66260 0.60331  1.000 27.81412  ? 54   SER A CB   1 
ATOM   437  O  OG   . SER A 1 29  ? 18.79882 20.11323 0.46377  1.000 23.83627  ? 54   SER A OG   1 
ATOM   438  H  H    . SER A 1 29  ? 16.56343 18.72895 -0.55901 1.000 32.61189  ? 54   SER A H    1 
ATOM   439  H  HA   . SER A 1 29  ? 16.06079 21.31656 -0.73277 1.000 25.33820  ? 54   SER A HA   1 
ATOM   440  H  HB2  . SER A 1 29  ? 17.54653 21.57139 0.93613  1.000 33.70679  ? 54   SER A HB2  1 
ATOM   441  H  HB3  . SER A 1 29  ? 16.97085 20.11817 1.22278  1.000 33.70679  ? 54   SER A HB3  1 
ATOM   442  H  HG   . SER A 1 29  ? 19.24064 20.24430 1.16606  1.000 28.93336  ? 54   SER A HG   1 
ATOM   443  N  N    . SER A 1 30  ? 18.17423 22.33578 -1.76101 1.000 22.19775  ? 55   SER A N    1 
ATOM   444  C  CA   . SER A 1 30  ? 19.31140 22.79838 -2.52285 1.000 22.08205  ? 55   SER A CA   1 
ATOM   445  C  C    . SER A 1 30  ? 20.61518 22.17199 -1.98368 1.000 23.88203  ? 55   SER A C    1 
ATOM   446  O  O    . SER A 1 30  ? 20.70589 21.73675 -0.82942 1.000 20.31289  ? 55   SER A O    1 
ATOM   447  C  CB   . SER A 1 30  ? 19.39361 24.33012 -2.44980 1.000 29.42429  ? 55   SER A CB   1 
ATOM   448  O  OG   . SER A 1 30  ? 18.25968 24.91533 -3.05702 1.000 23.64198  ? 55   SER A OG   1 
ATOM   449  H  H    . SER A 1 30  ? 17.80081 22.94304 -1.27997 1.000 26.96715  ? 55   SER A H    1 
ATOM   450  H  HA   . SER A 1 30  ? 19.21648 22.53679 -3.45208 1.000 26.82830  ? 55   SER A HA   1 
ATOM   451  H  HB2  . SER A 1 30  ? 19.43097 24.60181 -1.51937 1.000 35.63900  ? 55   SER A HB2  1 
ATOM   452  H  HB3  . SER A 1 30  ? 20.19137 24.62755 -2.91456 1.000 35.63900  ? 55   SER A HB3  1 
ATOM   453  H  HG   . SER A 1 30  ? 18.23509 24.71530 -3.87248 1.000 28.70022  ? 55   SER A HG   1 
ATOM   454  N  N    . THR A 1 31  ? 21.62581 22.14571 -2.84500 1.000 27.34761  ? 56   THR A N    1 
ATOM   455  C  CA   . THR A 1 31  ? 22.93890 21.59802 -2.51076 1.000 25.24886  ? 56   THR A CA   1 
ATOM   456  C  C    . THR A 1 31  ? 23.65692 22.51968 -1.53823 1.000 26.18037  ? 56   THR A C    1 
ATOM   457  O  O    . THR A 1 31  ? 23.52214 23.74851 -1.60479 1.000 33.19236  ? 56   THR A O    1 
ATOM   458  C  CB   . THR A 1 31  ? 23.73050 21.41762 -3.81259 1.000 30.08007  ? 56   THR A CB   1 
ATOM   459  O  OG1  . THR A 1 31  ? 23.05375 20.43979 -4.61812 1.000 31.62562  ? 56   THR A OG1  1 
ATOM   460  C  CG2  . THR A 1 31  ? 25.17748 21.01491 -3.60349 1.000 31.66691  ? 56   THR A CG2  1 
ATOM   461  H  H    . THR A 1 31  ? 21.57862 22.44548 -3.64968 1.000 33.14698  ? 56   THR A H    1 
ATOM   462  H  HA   . THR A 1 31  ? 22.86562 20.73404 -2.07594 1.000 30.62848  ? 56   THR A HA   1 
ATOM   463  H  HB   . THR A 1 31  ? 23.77381 22.27394 -4.26616 1.000 36.42593  ? 56   THR A HB   1 
ATOM   464  H  HG1  . THR A 1 31  ? 22.97530 19.72053 -4.19138 1.000 38.28059  ? 56   THR A HG1  1 
ATOM   465  H  HG21 . THR A 1 31  ? 25.59430 20.81996 -4.45740 1.000 38.33013  ? 56   THR A HG21 1 
ATOM   466  H  HG22 . THR A 1 31  ? 25.66357 21.73563 -3.17317 1.000 38.33013  ? 56   THR A HG22 1 
ATOM   467  H  HG23 . THR A 1 31  ? 25.22425 20.22485 -3.04268 1.000 38.33013  ? 56   THR A HG23 1 
ATOM   468  N  N    . PHE A 1 32  ? 24.41994 21.92659 -0.61131 1.000 25.67842  ? 57   PHE A N    1 
ATOM   469  C  CA   . PHE A 1 32  ? 25.17847 22.72461 0.35750  1.000 28.61865  ? 57   PHE A CA   1 
ATOM   470  C  C    . PHE A 1 32  ? 26.52735 22.09501 0.64361  1.000 31.45246  ? 57   PHE A C    1 
ATOM   471  O  O    . PHE A 1 32  ? 26.75300 20.90565 0.40506  1.000 24.38079  ? 57   PHE A O    1 
ATOM   472  C  CB   . PHE A 1 32  ? 24.38660 22.95396 1.63254  1.000 29.90666  ? 57   PHE A CB   1 
ATOM   473  C  CG   . PHE A 1 32  ? 24.09920 21.71167 2.43146  1.000 29.11478  ? 57   PHE A CG   1 
ATOM   474  C  CD1  . PHE A 1 32  ? 24.95539 21.25274 3.40106  1.000 31.79262  ? 57   PHE A CD1  1 
ATOM   475  C  CD2  . PHE A 1 32  ? 22.93693 21.00685 2.18522  1.000 33.13978  ? 57   PHE A CD2  1 
ATOM   476  C  CE1  . PHE A 1 32  ? 24.65643 20.11459 4.14111  1.000 31.35147  ? 57   PHE A CE1  1 
ATOM   477  C  CE2  . PHE A 1 32  ? 22.63543 19.86668 2.91524  1.000 35.41222  ? 57   PHE A CE2  1 
ATOM   478  C  CZ   . PHE A 1 32  ? 23.51584 19.41830 3.87999  1.000 32.21871  ? 57   PHE A CZ   1 
ATOM   479  H  H    . PHE A 1 32  ? 24.51235 21.07587 -0.52563 1.000 31.14395  ? 57   PHE A H    1 
ATOM   480  H  HA   . PHE A 1 32  ? 25.36990 23.59060 -0.03533 1.000 34.67223  ? 57   PHE A HA   1 
ATOM   481  H  HB2  . PHE A 1 32  ? 24.88920 23.55692 2.20241  1.000 36.21783  ? 57   PHE A HB2  1 
ATOM   482  H  HB3  . PHE A 1 32  ? 23.53419 23.35283 1.39760  1.000 36.21783  ? 57   PHE A HB3  1 
ATOM   483  H  HD1  . PHE A 1 32  ? 25.74807 21.71044 3.56555  1.000 38.48099  ? 57   PHE A HD1  1 
ATOM   484  H  HD2  . PHE A 1 32  ? 22.35163 21.29933 1.52433  1.000 40.09758  ? 57   PHE A HD2  1 
ATOM   485  H  HE1  . PHE A 1 32  ? 25.23359 19.82967 4.81237  1.000 37.95160  ? 57   PHE A HE1  1 
ATOM   486  H  HE2  . PHE A 1 32  ? 21.84348 19.40599 2.75563  1.000 42.82451  ? 57   PHE A HE2  1 
ATOM   487  H  HZ   . PHE A 1 32  ? 23.32935 18.63918 4.35232  1.000 38.99230  ? 57   PHE A HZ   1 
ATOM   488  N  N    . SER A 1 33  ? 27.43712 22.93526 1.10824  1.000 35.56189  ? 58   SER A N    1 
ATOM   489  C  CA   . SER A 1 33  ? 28.84572 22.60042 1.16595  1.000 32.02398  ? 58   SER A CA   1 
ATOM   490  C  C    . SER A 1 33  ? 29.33237 22.64755 2.60167  1.000 45.01184  ? 58   SER A C    1 
ATOM   491  O  O    . SER A 1 33  ? 28.82505 23.41487 3.42373  1.000 45.19893  ? 58   SER A O    1 
ATOM   492  C  CB   . SER A 1 33  ? 29.67697 23.57158 0.36276  1.000 46.43316  ? 58   SER A CB   1 
ATOM   493  O  OG   . SER A 1 33  ? 30.16574 24.57719 1.23963  1.000 59.05343  ? 58   SER A OG   1 
ATOM   494  H  H    . SER A 1 33  ? 27.25686 23.72310 1.40220  1.000 43.00412  ? 58   SER A H    1 
ATOM   495  H  HA   . SER A 1 33  ? 28.96575 21.70489 0.81306  1.000 38.75862  ? 58   SER A HA   1 
ATOM   496  H  HB2  . SER A 1 33  ? 30.42314 23.10305 -0.04295 1.000 56.04963  ? 58   SER A HB2  1 
ATOM   497  H  HB3  . SER A 1 33  ? 29.12742 23.97880 -0.32503 1.000 56.04963  ? 58   SER A HB3  1 
ATOM   498  H  HG   . SER A 1 33  ? 30.71778 25.06585 0.83707  1.000 71.19396  ? 58   SER A HG   1 
ATOM   499  N  N    . SER A 1 34  ? 30.36487 21.86543 2.86985  1.000 47.23985  ? 59   SER A N    1 
ATOM   500  C  CA   . SER A 1 34  ? 30.88052 21.71041 4.21150  1.000 56.92596  ? 59   SER A CA   1 
ATOM   501  C  C    . SER A 1 34  ? 31.82141 22.84625 4.59893  1.000 62.54938  ? 59   SER A C    1 
ATOM   502  O  O    . SER A 1 34  ? 31.37727 23.82452 5.21113  1.000 65.11948  ? 59   SER A O    1 
ATOM   503  C  CB   . SER A 1 34  ? 31.58804 20.35968 4.29225  1.000 60.57332  ? 59   SER A CB   1 
ATOM   504  O  OG   . SER A 1 34  ? 30.65964 19.31601 4.03450  1.000 47.18192  ? 59   SER A OG   1 
ATOM   505  H  H    . SER A 1 34  ? 30.78981 21.40681 2.27934  1.000 57.01767  ? 59   SER A H    1 
ATOM   506  H  HA   . SER A 1 34  ? 30.15595 21.73614 4.85589  1.000 68.64099  ? 59   SER A HA   1 
ATOM   507  H  HB2  . SER A 1 34  ? 32.29622 20.32906 3.63009  1.000 73.01783  ? 59   SER A HB2  1 
ATOM   508  H  HB3  . SER A 1 34  ? 31.95963 20.24546 5.18094  1.000 73.01783  ? 59   SER A HB3  1 
ATOM   509  H  HG   . SER A 1 34  ? 30.43140 19.32766 3.22618  1.000 56.94814  ? 59   SER A HG   1 
ATOM   510  N  N    . ASP A 1 38  ? 36.62095 22.34248 1.64671  1.000 62.32863  ? 63   ASP A N    1 
ATOM   511  C  CA   . ASP A 1 38  ? 36.73843 20.90548 1.90459  1.000 61.73758  ? 63   ASP A CA   1 
ATOM   512  C  C    . ASP A 1 38  ? 36.07351 20.04365 0.82421  1.000 57.59695  ? 63   ASP A C    1 
ATOM   513  O  O    . ASP A 1 38  ? 36.16062 18.81404 0.85327  1.000 54.62843  ? 63   ASP A O    1 
ATOM   514  C  CB   . ASP A 1 38  ? 36.14999 20.57243 3.28745  1.000 48.16159  ? 63   ASP A CB   1 
ATOM   515  C  CG   . ASP A 1 38  ? 34.66737 20.23856 3.24949  1.000 61.88844  ? 63   ASP A CG   1 
ATOM   516  O  OD1  . ASP A 1 38  ? 33.94166 20.58683 2.27964  1.000 59.37744  ? 63   ASP A OD1  1 
ATOM   517  O  OD2  . ASP A 1 38  ? 34.20046 19.60043 4.22150  1.000 52.96572  ? 63   ASP A OD2  1 
ATOM   518  H  HA   . ASP A 1 38  ? 37.68044 20.67435 1.89455  1.000 74.41494  ? 63   ASP A HA   1 
ATOM   519  H  HB2  . ASP A 1 38  ? 36.61817 19.80443 3.65061  1.000 58.12375  ? 63   ASP A HB2  1 
ATOM   520  H  HB3  . ASP A 1 38  ? 36.26706 21.33861 3.87069  1.000 58.12375  ? 63   ASP A HB3  1 
ATOM   521  N  N    . LYS A 1 39  ? 35.37494 20.71218 -0.09557 1.000 54.02002  ? 64   LYS A N    1 
ATOM   522  C  CA   . LYS A 1 39  ? 34.95302 20.16528 -1.38252 1.000 50.70896  ? 64   LYS A CA   1 
ATOM   523  C  C    . LYS A 1 39  ? 33.85691 19.10894 -1.29810 1.000 48.02258  ? 64   LYS A C    1 
ATOM   524  O  O    . LYS A 1 39  ? 33.64154 18.36780 -2.26598 1.000 45.07927  ? 64   LYS A O    1 
ATOM   525  C  CB   . LYS A 1 39  ? 36.13314 19.56761 -2.16500 1.000 52.60196  ? 64   LYS A CB   1 
ATOM   526  C  CG   . LYS A 1 39  ? 37.27878 20.52298 -2.51357 1.000 54.01251  ? 64   LYS A CG   1 
ATOM   527  C  CD   . LYS A 1 39  ? 37.50503 20.55885 -4.03392 1.000 59.35006  ? 64   LYS A CD   1 
ATOM   528  C  CE   . LYS A 1 39  ? 38.33723 21.75096 -4.50349 1.000 56.18916  ? 64   LYS A CE   1 
ATOM   529  N  NZ   . LYS A 1 39  ? 39.23842 21.35193 -5.62816 1.000 58.28318  ? 64   LYS A NZ   1 
ATOM   530  H  H    . LYS A 1 39  ? 35.12170 21.52704 0.01147  1.000 65.15386  ? 64   LYS A H    1 
ATOM   531  H  HA   . LYS A 1 39  ? 34.58590 20.91782 -1.87222 1.000 61.18060  ? 64   LYS A HA   1 
ATOM   532  H  HB2  . LYS A 1 39  ? 36.51324 18.85005 -1.63441 1.000 63.45220  ? 64   LYS A HB2  1 
ATOM   533  H  HB3  . LYS A 1 39  ? 35.79176 19.21620 -3.00219 1.000 63.45220  ? 64   LYS A HB3  1 
ATOM   534  H  HG2  . LYS A 1 39  ? 37.05857 21.41840 -2.21251 1.000 65.14486  ? 64   LYS A HG2  1 
ATOM   535  H  HG3  . LYS A 1 39  ? 38.09559 20.22086 -2.08644 1.000 65.14486  ? 64   LYS A HG3  1 
ATOM   536  H  HD2  . LYS A 1 39  ? 37.97047 19.75050 -4.30005 1.000 71.54992  ? 64   LYS A HD2  1 
ATOM   537  H  HD3  . LYS A 1 39  ? 36.64363 20.60694 -4.47730 1.000 71.54992  ? 64   LYS A HD3  1 
ATOM   538  H  HE2  . LYS A 1 39  ? 37.74801 22.45577 -4.81487 1.000 67.75683  ? 64   LYS A HE2  1 
ATOM   539  H  HE3  . LYS A 1 39  ? 38.88323 22.07483 -3.77008 1.000 67.75683  ? 64   LYS A HE3  1 
ATOM   540  H  HZ1  . LYS A 1 39  ? 39.73642 22.04529 -5.87986 1.000 70.26966  ? 64   LYS A HZ1  1 
ATOM   541  H  HZ2  . LYS A 1 39  ? 39.77434 20.69042 -5.36877 1.000 70.26966  ? 64   LYS A HZ2  1 
ATOM   542  H  HZ3  . LYS A 1 39  ? 38.75481 21.07642 -6.32265 1.000 70.26966  ? 64   LYS A HZ3  1 
ATOM   543  N  N    . LEU A 1 40  ? 33.13760 18.99742 -0.19273 1.000 34.98356  ? 65   LEU A N    1 
ATOM   544  C  CA   . LEU A 1 40  ? 32.02670 18.06882 -0.09751 1.000 32.77119  ? 65   LEU A CA   1 
ATOM   545  C  C    . LEU A 1 40  ? 30.73046 18.80485 -0.41225 1.000 34.86829  ? 65   LEU A C    1 
ATOM   546  O  O    . LEU A 1 40  ? 30.53490 19.94179 0.02617  1.000 33.22591  ? 65   LEU A O    1 
ATOM   547  C  CB   . LEU A 1 40  ? 31.95111 17.44848 1.28441  1.000 39.56629  ? 65   LEU A CB   1 
ATOM   548  C  CG   . LEU A 1 40  ? 32.41903 16.00687 1.33503  1.000 38.81577  ? 65   LEU A CG   1 
ATOM   549  C  CD1  . LEU A 1 40  ? 33.71656 15.81210 0.61148  1.000 38.68617  ? 65   LEU A CD1  1 
ATOM   550  C  CD2  . LEU A 1 40  ? 32.57689 15.59911 2.79038  1.000 43.61659  ? 65   LEU A CD2  1 
ATOM   551  H  H    . LEU A 1 40  ? 33.27608 19.45438 0.52254  1.000 42.31012  ? 65   LEU A H    1 
ATOM   552  H  HA   . LEU A 1 40  ? 32.14219 17.34931 -0.73773 1.000 39.65527  ? 65   LEU A HA   1 
ATOM   553  H  HB2  . LEU A 1 40  ? 32.51030 17.96308 1.88723  1.000 47.80940  ? 65   LEU A HB2  1 
ATOM   554  H  HB3  . LEU A 1 40  ? 31.02938 17.47181 1.58569  1.000 47.80940  ? 65   LEU A HB3  1 
ATOM   555  H  HG   . LEU A 1 40  ? 31.76180 15.44569 0.89457  1.000 46.90877  ? 65   LEU A HG   1 
ATOM   556  H  HD11 . LEU A 1 40  ? 33.99799 14.88913 0.71065  1.000 46.75325  ? 65   LEU A HD11 1 
ATOM   557  H  HD12 . LEU A 1 40  ? 33.58892 16.01995 -0.32735 1.000 46.75325  ? 65   LEU A HD12 1 
ATOM   558  H  HD13 . LEU A 1 40  ? 34.38321 16.40407 0.99366  1.000 46.75325  ? 65   LEU A HD13 1 
ATOM   559  H  HD21 . LEU A 1 40  ? 32.89401 14.68323 2.82911  1.000 52.66975  ? 65   LEU A HD21 1 
ATOM   560  H  HD22 . LEU A 1 40  ? 33.21818 16.18947 3.21597  1.000 52.66975  ? 65   LEU A HD22 1 
ATOM   561  H  HD23 . LEU A 1 40  ? 31.71691 15.67042 3.23338  1.000 52.66975  ? 65   LEU A HD23 1 
ATOM   562  N  N    . LYS A 1 41  ? 29.84920 18.17137 -1.19003 1.000 34.73606  ? 66   LYS A N    1 
ATOM   563  C  CA   . LYS A 1 41  ? 28.54946 18.75367 -1.49596 1.000 29.64074  ? 66   LYS A CA   1 
ATOM   564  C  C    . LYS A 1 41  ? 27.46265 17.79654 -1.04741 1.000 24.37287  ? 66   LYS A C    1 
ATOM   565  O  O    . LYS A 1 41  ? 27.57844 16.58452 -1.22387 1.000 24.92713  ? 66   LYS A O    1 
ATOM   566  C  CB   . LYS A 1 41  ? 28.40245 19.04667 -2.96376 1.000 29.71789  ? 66   LYS A CB   1 
ATOM   567  C  CG   . LYS A 1 41  ? 29.36809 20.10985 -3.55196 1.000 47.07489  ? 66   LYS A CG   1 
ATOM   568  C  CD   . LYS A 1 41  ? 28.82073 21.54413 -3.50300 1.000 57.18297  ? 66   LYS A CD   1 
ATOM   569  C  CE   . LYS A 1 41  ? 29.93301 22.58314 -3.78137 1.000 76.49547  ? 66   LYS A CE   1 
ATOM   570  N  NZ   . LYS A 1 41  ? 29.45119 24.00124 -3.78541 1.000 83.82871  ? 66   LYS A NZ   1 
ATOM   571  H  H    . LYS A 1 41  ? 29.98599 17.40254 -1.55027 1.000 42.01311  ? 66   LYS A H    1 
ATOM   572  H  HA   . LYS A 1 41  ? 28.44726 19.59177 -1.01844 1.000 35.89873  ? 66   LYS A HA   1 
ATOM   573  H  HB2  . LYS A 1 41  ? 28.55317 18.22264 -3.45280 1.000 35.99131  ? 66   LYS A HB2  1 
ATOM   574  H  HB3  . LYS A 1 41  ? 27.49925 19.36434 -3.11935 1.000 35.99131  ? 66   LYS A HB3  1 
ATOM   575  H  HG2  . LYS A 1 41  ? 30.19577 20.09315 -3.04643 1.000 56.81971  ? 66   LYS A HG2  1 
ATOM   576  H  HG3  . LYS A 1 41  ? 29.54243 19.89279 -4.48115 1.000 56.81971  ? 66   LYS A HG3  1 
ATOM   577  H  HD2  . LYS A 1 41  ? 28.13046 21.64812 -4.17651 1.000 68.94941  ? 66   LYS A HD2  1 
ATOM   578  H  HD3  . LYS A 1 41  ? 28.45376 21.71844 -2.62218 1.000 68.94941  ? 66   LYS A HD3  1 
ATOM   579  H  HE2  . LYS A 1 41  ? 30.61250 22.50454 -3.09361 1.000 92.12440  ? 66   LYS A HE2  1 
ATOM   580  H  HE3  . LYS A 1 41  ? 30.31959 22.40057 -4.65207 1.000 92.12440  ? 66   LYS A HE3  1 
ATOM   581  H  HZ1  . LYS A 1 41  ? 30.13426 24.55442 -3.92506 1.000 100.92430 ? 66   LYS A HZ1  1 
ATOM   582  H  HZ2  . LYS A 1 41  ? 28.84955 24.11648 -4.43105 1.000 100.92430 ? 66   LYS A HZ2  1 
ATOM   583  H  HZ3  . LYS A 1 41  ? 29.07598 24.19748 -3.00259 1.000 100.92430 ? 66   LYS A HZ3  1 
ATOM   584  N  N    . TRP A 1 42  ? 26.39586 18.34093 -0.47696 1.000 24.26336  ? 67   TRP A N    1 
ATOM   585  C  CA   . TRP A 1 42  ? 25.35441 17.53344 0.14149  1.000 22.36439  ? 67   TRP A CA   1 
ATOM   586  C  C    . TRP A 1 42  ? 24.00230 18.08966 -0.26798 1.000 24.34152  ? 67   TRP A C    1 
ATOM   587  O  O    . TRP A 1 42  ? 23.89532 19.22770 -0.73044 1.000 24.54219  ? 67   TRP A O    1 
ATOM   588  C  CB   . TRP A 1 42  ? 25.46276 17.53481 1.68531  1.000 20.75994  ? 67   TRP A CB   1 
ATOM   589  C  CG   . TRP A 1 42  ? 26.76338 17.05034 2.28921  1.000 23.23564  ? 67   TRP A CG   1 
ATOM   590  C  CD1  . TRP A 1 42  ? 27.87546 17.82050 2.60425  1.000 22.04482  ? 67   TRP A CD1  1 
ATOM   591  C  CD2  . TRP A 1 42  ? 27.09370 15.69996 2.68557  1.000 18.73783  ? 67   TRP A CD2  1 
ATOM   592  N  NE1  . TRP A 1 42  ? 28.86389 17.02270 3.13644  1.000 21.31796  ? 67   TRP A NE1  1 
ATOM   593  C  CE2  . TRP A 1 42  ? 28.40937 15.72564 3.20313  1.000 24.74625  ? 67   TRP A CE2  1 
ATOM   594  C  CE3  . TRP A 1 42  ? 26.41617 14.47050 2.61551  1.000 22.62608  ? 67   TRP A CE3  1 
ATOM   595  C  CZ2  . TRP A 1 42  ? 29.04737 14.58818 3.67474  1.000 23.02374  ? 67   TRP A CZ2  1 
ATOM   596  C  CZ3  . TRP A 1 42  ? 27.06436 13.32464 3.08136  1.000 24.37716  ? 67   TRP A CZ3  1 
ATOM   597  C  CH2  . TRP A 1 42  ? 28.36632 13.39811 3.61143  1.000 21.45902  ? 67   TRP A CH2  1 
ATOM   598  H  H    . TRP A 1 42  ? 26.25062 19.18753 -0.43480 1.000 29.44587  ? 67   TRP A H    1 
ATOM   599  H  HA   . TRP A 1 42  ? 25.43231 16.61820 -0.17024 1.000 27.16711  ? 67   TRP A HA   1 
ATOM   600  H  HB2  . TRP A 1 42  ? 25.33234 18.44552 1.99271  1.000 25.24178  ? 67   TRP A HB2  1 
ATOM   601  H  HB3  . TRP A 1 42  ? 24.76096 16.96322 2.03412  1.000 25.24178  ? 67   TRP A HB3  1 
ATOM   602  H  HD1  . TRP A 1 42  ? 27.94268 18.73902 2.47495  1.000 26.78363  ? 67   TRP A HD1  1 
ATOM   603  H  HE1  . TRP A 1 42  ? 29.64116 17.29218 3.38709  1.000 25.91140  ? 67   TRP A HE1  1 
ATOM   604  H  HE3  . TRP A 1 42  ? 25.55547 14.42120 2.26671  1.000 27.48114  ? 67   TRP A HE3  1 
ATOM   605  H  HZ2  . TRP A 1 42  ? 29.90881 14.63035 4.02265  1.000 27.95834  ? 67   TRP A HZ2  1 
ATOM   606  H  HZ3  . TRP A 1 42  ? 26.63057 12.50300 3.04090  1.000 29.58244  ? 67   TRP A HZ3  1 
ATOM   607  H  HH2  . TRP A 1 42  ? 28.77394 12.62347 3.92558  1.000 26.08067  ? 67   TRP A HH2  1 
ATOM   608  N  N    . CYS A 1 43  ? 22.96205 17.28072 -0.10059 1.000 24.36229  ? 68   CYS A N    1 
ATOM   609  C  CA   . CYS A 1 43  ? 21.60204 17.81311 -0.12552 1.000 23.92815  ? 68   CYS A CA   1 
ATOM   610  C  C    . CYS A 1 43  ? 20.72872 16.96808 0.79401  1.000 21.94603  ? 68   CYS A C    1 
ATOM   611  O  O    . CYS A 1 43  ? 21.10867 15.88199 1.22251  1.000 18.86803  ? 68   CYS A O    1 
ATOM   612  C  CB   . CYS A 1 43  ? 21.06642 17.90774 -1.54460 1.000 28.81987  ? 68   CYS A CB   1 
ATOM   613  S  SG   . CYS A 1 43  ? 20.28176 16.47226 -2.17042 1.000 39.95028  ? 68   CYS A SG   1 
ATOM   614  H  H    . CYS A 1 43  ? 23.01533 16.43195 0.02733  1.000 29.56459  ? 68   CYS A H    1 
ATOM   615  H  HA   . CYS A 1 43  ? 21.58200 18.71456 0.23207  1.000 29.04362  ? 68   CYS A HA   1 
ATOM   616  H  HB2  . CYS A 1 43  ? 20.41510 18.62592 -1.57476 1.000 34.91369  ? 68   CYS A HB2  1 
ATOM   617  H  HB3  . CYS A 1 43  ? 21.80909 18.10838 -2.13543 1.000 34.91369  ? 68   CYS A HB3  1 
ATOM   618  H  HG   . CYS A 1 43  ? 20.13377 16.59295 -3.35513 1.000 48.27019  ? 68   CYS A HG   1 
ATOM   619  N  N    . LEU A 1 44  ? 19.58977 17.52939 1.18556  1.000 25.76938  ? 69   LEU A N    1 
ATOM   620  C  CA   . LEU A 1 44  ? 18.62002 16.80813 2.00736  1.000 26.71246  ? 69   LEU A CA   1 
ATOM   621  C  C    . LEU A 1 44  ? 17.49242 16.32101 1.11516  1.000 21.19608  ? 69   LEU A C    1 
ATOM   622  O  O    . LEU A 1 44  ? 17.08086 17.00963 0.16463  1.000 22.81886  ? 69   LEU A O    1 
ATOM   623  C  CB   . LEU A 1 44  ? 18.04619 17.68213 3.12096  1.000 21.17403  ? 69   LEU A CB   1 
ATOM   624  C  CG   . LEU A 1 44  ? 19.09798 18.33981 4.02443  1.000 21.25907  ? 69   LEU A CG   1 
ATOM   625  C  CD1  . LEU A 1 44  ? 18.41594 19.13099 5.13542  1.000 23.23149  ? 69   LEU A CD1  1 
ATOM   626  C  CD2  . LEU A 1 44  ? 20.01585 17.29545 4.63238  1.000 26.52419  ? 69   LEU A CD2  1 
ATOM   627  H  H    . LEU A 1 44  ? 19.35347 18.33216 0.98727  1.000 31.25311  ? 69   LEU A H    1 
ATOM   628  H  HA   . LEU A 1 44  ? 19.05761 16.05320 2.43102  1.000 32.38479  ? 69   LEU A HA   1 
ATOM   629  H  HB2  . LEU A 1 44  ? 17.52254 18.39144 2.71652  1.000 25.73867  ? 69   LEU A HB2  1 
ATOM   630  H  HB3  . LEU A 1 44  ? 17.47985 17.13117 3.68363  1.000 25.73867  ? 69   LEU A HB3  1 
ATOM   631  H  HG   . LEU A 1 44  ? 19.63459 18.94423 3.48812  1.000 25.84073  ? 69   LEU A HG   1 
ATOM   632  H  HD11 . LEU A 1 44  ? 19.09497 19.53896 5.69522  1.000 28.20764  ? 69   LEU A HD11 1 
ATOM   633  H  HD12 . LEU A 1 44  ? 17.85868 19.81804 4.73751  1.000 28.20764  ? 69   LEU A HD12 1 
ATOM   634  H  HD13 . LEU A 1 44  ? 17.87042 18.52752 5.66375  1.000 28.20764  ? 69   LEU A HD13 1 
ATOM   635  H  HD21 . LEU A 1 44  ? 19.47656 16.60411 5.04724  1.000 32.15888  ? 69   LEU A HD21 1 
ATOM   636  H  HD22 . LEU A 1 44  ? 20.56462 16.91069 3.93116  1.000 32.15888  ? 69   LEU A HD22 1 
ATOM   637  H  HD23 . LEU A 1 44  ? 20.57942 17.71954 5.29829  1.000 32.15888  ? 69   LEU A HD23 1 
ATOM   638  N  N    . ARG A 1 45  ? 17.03239 15.10426 1.38646  1.000 22.91818  ? 70   ARG A N    1 
ATOM   639  C  CA   . ARG A 1 45  ? 15.84783 14.55868 0.75125  1.000 23.15808  ? 70   ARG A CA   1 
ATOM   640  C  C    . ARG A 1 45  ? 14.79204 14.33861 1.82637  1.000 23.07433  ? 70   ARG A C    1 
ATOM   641  O  O    . ARG A 1 45  ? 15.08540 13.72177 2.85213  1.000 20.02868  ? 70   ARG A O    1 
ATOM   642  C  CB   . ARG A 1 45  ? 16.11651 13.24358 0.01493  1.000 35.02019  ? 70   ARG A CB   1 
ATOM   643  C  CG   . ARG A 1 45  ? 17.16434 13.28553 -1.11963 1.000 31.95903  ? 70   ARG A CG   1 
ATOM   644  C  CD   . ARG A 1 45  ? 17.16192 11.94804 -1.82928 1.000 33.78544  ? 70   ARG A CD   1 
ATOM   645  N  NE   . ARG A 1 45  ? 17.62462 12.03510 -3.20636 1.000 45.91074  ? 70   ARG A NE   1 
ATOM   646  C  CZ   . ARG A 1 45  ? 18.32553 11.09235 -3.83132 1.000 54.03180  ? 70   ARG A CZ   1 
ATOM   647  N  NH1  . ARG A 1 45  ? 18.57311 9.91645  -3.26527 1.000 46.89304  ? 70   ARG A NH1  1 
ATOM   648  N  NH2  . ARG A 1 45  ? 18.79937 11.33999 -5.05075 1.000 53.13046  ? 70   ARG A NH2  1 
ATOM   649  H  H    . ARG A 1 45  ? 17.40071 14.56727 1.94822  1.000 27.83166  ? 70   ARG A H    1 
ATOM   650  H  HA   . ARG A 1 45  ? 15.52657 15.19303 0.09148  1.000 28.11954  ? 70   ARG A HA   1 
ATOM   651  H  HB2  . ARG A 1 45  ? 16.42763 12.59376 0.66442  1.000 42.35407  ? 70   ARG A HB2  1 
ATOM   652  H  HB3  . ARG A 1 45  ? 15.28256 12.94466 -0.38013 1.000 42.35407  ? 70   ARG A HB3  1 
ATOM   653  H  HG2  . ARG A 1 45  ? 16.93779 13.98210 -1.75552 1.000 38.68068  ? 70   ARG A HG2  1 
ATOM   654  H  HG3  . ARG A 1 45  ? 18.04689 13.44711 -0.75099 1.000 38.68068  ? 70   ARG A HG3  1 
ATOM   655  H  HD2  . ARG A 1 45  ? 17.74837 11.33815 -1.35493 1.000 40.87237  ? 70   ARG A HD2  1 
ATOM   656  H  HD3  . ARG A 1 45  ? 16.25736 11.59795 -1.83949 1.000 40.87237  ? 70   ARG A HD3  1 
ATOM   657  H  HE   . ARG A 1 45  ? 17.43110 12.74718 -3.64804 1.000 55.42274  ? 70   ARG A HE   1 
ATOM   658  H  HH11 . ARG A 1 45  ? 18.27793 9.74895  -2.47507 1.000 56.60149  ? 70   ARG A HH11 1 
ATOM   659  H  HH12 . ARG A 1 45  ? 19.02859 9.32264  -3.68898 1.000 56.60149  ? 70   ARG A HH12 1 
ATOM   660  H  HH21 . ARG A 1 45  ? 18.65088 12.10066 -5.42348 1.000 64.08640  ? 70   ARG A HH21 1 
ATOM   661  H  HH22 . ARG A 1 45  ? 19.25390 10.73927 -5.46563 1.000 64.08640  ? 70   ARG A HH22 1 
ATOM   662  N  N    . VAL A 1 46  ? 13.56766 14.82041 1.56617  1.000 22.29973  ? 71   VAL A N    1 
ATOM   663  C  CA   . VAL A 1 46  ? 12.41681 14.64395 2.44467  1.000 21.08235  ? 71   VAL A CA   1 
ATOM   664  C  C    . VAL A 1 46  ? 11.28475 13.95294 1.69054  1.000 21.11410  ? 71   VAL A C    1 
ATOM   665  O  O    . VAL A 1 46  ? 10.87801 14.38870 0.60126  1.000 23.46239  ? 71   VAL A O    1 
ATOM   666  C  CB   . VAL A 1 46  ? 11.93154 16.00090 2.99039  1.000 26.10256  ? 71   VAL A CB   1 
ATOM   667  C  CG1  . VAL A 1 46  ? 10.47428 15.95956 3.29584  1.000 21.85370  ? 71   VAL A CG1  1 
ATOM   668  C  CG2  . VAL A 1 46  ? 12.77882 16.38926 4.21713  1.000 24.78691  ? 71   VAL A CG2  1 
ATOM   669  H  H    . VAL A 1 46  ? 13.37881 15.26939 0.85740  1.000 27.08952  ? 71   VAL A H    1 
ATOM   670  H  HA   . VAL A 1 46  ? 12.67685 14.06360 3.17711  1.000 25.62867  ? 71   VAL A HA   1 
ATOM   671  H  HB   . VAL A 1 46  ? 12.04755 16.69092 2.31860  1.000 31.65292  ? 71   VAL A HB   1 
ATOM   672  H  HG11 . VAL A 1 46  ? 10.25838 15.09969 3.68941  1.000 24.97851  ? 71   VAL A HG11 1 
ATOM   673  H  HG12 . VAL A 1 46  ? 10.26204 16.67147 3.91957  1.000 24.97851  ? 71   VAL A HG12 1 
ATOM   674  H  HG13 . VAL A 1 46  ? 9.97554  16.08124 2.47283  1.000 24.97851  ? 71   VAL A HG13 1 
ATOM   675  H  HG21 . VAL A 1 46  ? 12.48649 17.25545 4.54142  1.000 30.07414  ? 71   VAL A HG21 1 
ATOM   676  H  HG22 . VAL A 1 46  ? 12.65900 15.71955 4.90852  1.000 30.07414  ? 71   VAL A HG22 1 
ATOM   677  H  HG23 . VAL A 1 46  ? 13.71199 16.43162 3.95581  1.000 30.07414  ? 71   VAL A HG23 1 
ATOM   678  N  N    . ASN A 1 47  ? 10.75954 12.88026 2.28687  1.000 22.86160  ? 72   ASN A N    1 
ATOM   679  C  CA   . ASN A 1 47  ? 9.55001  12.21412 1.81029  1.000 21.48116  ? 72   ASN A CA   1 
ATOM   680  C  C    . ASN A 1 47  ? 8.41688  12.56899 2.76549  1.000 23.74455  ? 72   ASN A C    1 
ATOM   681  O  O    . ASN A 1 47  ? 8.37483  12.06418 3.89254  1.000 20.43869  ? 72   ASN A O    1 
ATOM   682  C  CB   . ASN A 1 47  ? 9.76595  10.69973 1.73971  1.000 27.73222  ? 72   ASN A CB   1 
ATOM   683  C  CG   . ASN A 1 47  ? 11.02501 10.33815 0.95256  1.000 29.75608  ? 72   ASN A CG   1 
ATOM   684  O  OD1  . ASN A 1 47  ? 12.06595 9.97773  1.50969  1.000 29.05705  ? 72   ASN A OD1  1 
ATOM   685  N  ND2  . ASN A 1 47  ? 10.94581 10.49443 -0.34288 1.000 34.33791  ? 72   ASN A ND2  1 
ATOM   686  H  H    . ASN A 1 47  ? 11.09585 12.51159 2.98729  1.000 27.76376  ? 72   ASN A H    1 
ATOM   687  H  HA   . ASN A 1 47  ? 9.31924  12.51742 0.91829  1.000 25.56092  ? 72   ASN A HA   1 
ATOM   688  H  HB2  . ASN A 1 47  ? 9.85910  10.34835 2.63902  1.000 33.60851  ? 72   ASN A HB2  1 
ATOM   689  H  HB3  . ASN A 1 47  ? 9.00503  10.28897 1.30020  1.000 33.60851  ? 72   ASN A HB3  1 
ATOM   690  H  HD21 . ASN A 1 47  ? 10.21770 10.78391 -0.69736 1.000 41.53534  ? 72   ASN A HD21 1 
ATOM   691  H  HD22 . ASN A 1 47  ? 11.62181 10.30775 -0.84065 1.000 41.53534  ? 72   ASN A HD22 1 
ATOM   692  N  N    . PRO A 1 48  ? 7.53852  13.49837 2.40391  1.000 22.96522  ? 73   PRO A N    1 
ATOM   693  C  CA   . PRO A 1 48  ? 6.52956  13.96137 3.37194  1.000 24.96817  ? 73   PRO A CA   1 
ATOM   694  C  C    . PRO A 1 48  ? 5.64807  12.85834 3.89837  1.000 22.94626  ? 73   PRO A C    1 
ATOM   695  O  O    . PRO A 1 48  ? 5.20162  12.90999 5.05059  1.000 28.74807  ? 73   PRO A O    1 
ATOM   696  C  CB   . PRO A 1 48  ? 5.69506  14.97053 2.56138  1.000 24.09268  ? 73   PRO A CB   1 
ATOM   697  C  CG   . PRO A 1 48  ? 6.63401  15.45562 1.47834  1.000 29.86275  ? 73   PRO A CG   1 
ATOM   698  C  CD   . PRO A 1 48  ? 7.50074  14.26055 1.13920  1.000 26.19050  ? 73   PRO A CD   1 
ATOM   699  H  HA   . PRO A 1 48  ? 6.97531  14.40969 4.10761  1.000 30.29165  ? 73   PRO A HA   1 
ATOM   700  H  HB2  . PRO A 1 48  ? 4.91998  14.52973 2.17950  1.000 29.24107  ? 73   PRO A HB2  1 
ATOM   701  H  HB3  . PRO A 1 48  ? 5.41287  15.70239 3.13204  1.000 29.24107  ? 73   PRO A HB3  1 
ATOM   702  H  HG2  . PRO A 1 48  ? 6.12445  15.74394 0.70495  1.000 36.16514  ? 73   PRO A HG2  1 
ATOM   703  H  HG3  . PRO A 1 48  ? 7.17257  16.18959 1.81322  1.000 36.16514  ? 73   PRO A HG3  1 
ATOM   704  H  HD2  . PRO A 1 48  ? 7.09996  13.73349 0.43035  1.000 31.75844  ? 73   PRO A HD2  1 
ATOM   705  H  HD3  . PRO A 1 48  ? 8.39169  14.54285 0.87954  1.000 31.75844  ? 73   PRO A HD3  1 
ATOM   706  N  N    . LYS A 1 49  ? 5.38034  11.86345 3.08166  1.000 19.93171  ? 74   LYS A N    1 
ATOM   707  C  CA   . LYS A 1 49  ? 4.50391  10.76621 3.40652  1.000 22.94986  ? 74   LYS A CA   1 
ATOM   708  C  C    . LYS A 1 49  ? 5.22188  9.48322  3.19350  1.000 23.01083  ? 74   LYS A C    1 
ATOM   709  O  O    . LYS A 1 49  ? 4.66405  8.50567  2.67875  1.000 25.76018  ? 74   LYS A O    1 
ATOM   710  C  CB   . LYS A 1 49  ? 3.24056  10.84116 2.57816  1.000 23.87193  ? 74   LYS A CB   1 
ATOM   711  C  CG   . LYS A 1 49  ? 2.33486  11.93364 3.05408  1.000 27.46785  ? 74   LYS A CG   1 
ATOM   712  C  CD   . LYS A 1 49  ? 1.04561  11.87049 2.33881  1.000 30.48796  ? 74   LYS A CD   1 
ATOM   713  C  CE   . LYS A 1 49  ? 0.01111  12.80283 2.91516  1.000 36.50196  ? 74   LYS A CE   1 
ATOM   714  N  NZ   . LYS A 1 49  ? -1.23789 12.74544 2.11200  1.000 40.31627  ? 74   LYS A NZ   1 
ATOM   715  H  H    . LYS A 1 49  ? 5.71331  11.79995 2.29129  1.000 24.24790  ? 74   LYS A H    1 
ATOM   716  H  HA   . LYS A 1 49  ? 4.24461  10.81094 4.34015  1.000 27.86968  ? 74   LYS A HA   1 
ATOM   717  H  HB2  . LYS A 1 49  ? 3.47391  11.01890 1.65358  1.000 28.97616  ? 74   LYS A HB2  1 
ATOM   718  H  HB3  . LYS A 1 49  ? 2.76397  9.99888  2.64402  1.000 28.97616  ? 74   LYS A HB3  1 
ATOM   719  H  HG2  . LYS A 1 49  ? 2.16868  11.82964 4.00406  1.000 33.29126  ? 74   LYS A HG2  1 
ATOM   720  H  HG3  . LYS A 1 49  ? 2.74424  12.79589 2.88133  1.000 33.29126  ? 74   LYS A HG3  1 
ATOM   721  H  HD2  . LYS A 1 49  ? 1.18628  12.11629 1.41107  1.000 36.91540  ? 74   LYS A HD2  1 
ATOM   722  H  HD3  . LYS A 1 49  ? 0.69756  10.96674 2.39346  1.000 36.91540  ? 74   LYS A HD3  1 
ATOM   723  H  HE2  . LYS A 1 49  ? -0.19343 12.53951 3.82605  1.000 44.13219  ? 74   LYS A HE2  1 
ATOM   724  H  HE3  . LYS A 1 49  ? 0.34790  13.71237 2.90042  1.000 44.13219  ? 74   LYS A HE3  1 
ATOM   725  H  HZ1  . LYS A 1 49  ? -1.58500 11.92667 2.14709  1.000 48.70937  ? 74   LYS A HZ1  1 
ATOM   726  H  HZ2  . LYS A 1 49  ? -1.83250 13.32519 2.43203  1.000 48.70937  ? 74   LYS A HZ2  1 
ATOM   727  H  HZ3  . LYS A 1 49  ? -1.06369 12.94918 1.26333  1.000 48.70937  ? 74   LYS A HZ3  1 
ATOM   728  N  N    . GLY A 1 50  ? 6.49841  9.48118  3.53078  1.000 27.93147  ? 75   GLY A N    1 
ATOM   729  C  CA   . GLY A 1 50  ? 7.28426  8.29621  3.50608  1.000 26.62681  ? 75   GLY A CA   1 
ATOM   730  C  C    . GLY A 1 50  ? 7.64802  7.79045  2.12425  1.000 27.68125  ? 75   GLY A C    1 
ATOM   731  O  O    . GLY A 1 50  ? 7.65744  8.50967  1.11912  1.000 26.39511  ? 75   GLY A O    1 
ATOM   732  H  H    . GLY A 1 50  ? 6.93408  10.17848 3.78290  1.000 33.84761  ? 75   GLY A H    1 
ATOM   733  H  HA2  . GLY A 1 50  ? 8.11146  8.46285  3.98449  1.000 32.28201  ? 75   GLY A HA2  1 
ATOM   734  H  HA3  . GLY A 1 50  ? 6.79515  7.59046  3.95729  1.000 32.28201  ? 75   GLY A HA3  1 
ATOM   735  N  N    . LEU A 1 51  ? 7.92921  6.49171  2.10908  1.000 31.07284  ? 76   LEU A N    1 
ATOM   736  C  CA   . LEU A 1 51  ? 8.36759  5.77250  0.92243  1.000 30.61785  ? 76   LEU A CA   1 
ATOM   737  C  C    . LEU A 1 51  ? 7.53969  4.53983  0.60884  1.000 33.60738  ? 76   LEU A C    1 
ATOM   738  O  O    . LEU A 1 51  ? 7.64632  4.02195  -0.51113 1.000 37.90865  ? 76   LEU A O    1 
ATOM   739  C  CB   . LEU A 1 51  ? 9.81648  5.31464  1.08779  1.000 32.32486  ? 76   LEU A CB   1 
ATOM   740  C  CG   . LEU A 1 51  ? 10.79345 6.17652  1.84491  1.000 31.92115  ? 76   LEU A CG   1 
ATOM   741  C  CD1  . LEU A 1 51  ? 11.92583 5.31583  2.29326  1.000 45.71149  ? 76   LEU A CD1  1 
ATOM   742  C  CD2  . LEU A 1 51  ? 11.31007 7.24434  0.90223  1.000 36.95117  ? 76   LEU A CD2  1 
ATOM   743  H  H    . LEU A 1 51  ? 7.87097  5.98605  2.80227  1.000 37.61725  ? 76   LEU A H    1 
ATOM   744  H  HA   . LEU A 1 51  ? 8.31624  6.37769  0.16612  1.000 37.07127  ? 76   LEU A HA   1 
ATOM   745  H  HB2  . LEU A 1 51  ? 9.79708  4.46044  1.54699  1.000 39.11967  ? 76   LEU A HB2  1 
ATOM   746  H  HB3  . LEU A 1 51  ? 10.18620 5.20455  0.19780  1.000 39.11967  ? 76   LEU A HB3  1 
ATOM   747  H  HG   . LEU A 1 51  ? 10.37940 6.59510  2.61579  1.000 38.63522  ? 76   LEU A HG   1 
ATOM   748  H  HD11 . LEU A 1 51  ? 12.50997 5.83601  2.86692  1.000 55.18364  ? 76   LEU A HD11 1 
ATOM   749  H  HD12 . LEU A 1 51  ? 11.57129 4.55721  2.78285  1.000 55.18364  ? 76   LEU A HD12 1 
ATOM   750  H  HD13 . LEU A 1 51  ? 12.41559 5.00749  1.51482  1.000 55.18364  ? 76   LEU A HD13 1 
ATOM   751  H  HD21 . LEU A 1 51  ? 11.97905 7.77501  1.36239  1.000 44.67125  ? 76   LEU A HD21 1 
ATOM   752  H  HD22 . LEU A 1 51  ? 11.70387 6.81651  0.12583  1.000 44.67125  ? 76   LEU A HD22 1 
ATOM   753  H  HD23 . LEU A 1 51  ? 10.57032 7.80917  0.62903  1.000 44.67125  ? 76   LEU A HD23 1 
ATOM   754  N  N    . ASP A 1 52  ? 6.76949  4.01525  1.55460  1.000 37.34887  ? 77   ASP A N    1 
ATOM   755  C  CA   . ASP A 1 52  ? 6.06205  2.74806  1.40567  1.000 45.60333  ? 77   ASP A CA   1 
ATOM   756  C  C    . ASP A 1 52  ? 4.88592  2.75791  2.37533  1.000 50.49304  ? 77   ASP A C    1 
ATOM   757  O  O    . ASP A 1 52  ? 4.81682  3.58299  3.29260  1.000 45.72635  ? 77   ASP A O    1 
ATOM   758  C  CB   . ASP A 1 52  ? 6.98325  1.54785  1.66212  1.000 38.14737  ? 77   ASP A CB   1 
ATOM   759  C  CG   . ASP A 1 52  ? 7.79700  1.68636  2.94425  1.000 47.09881  ? 77   ASP A CG   1 
ATOM   760  O  OD1  . ASP A 1 52  ? 7.42363  2.52076  3.79037  1.000 43.31634  ? 77   ASP A OD1  1 
ATOM   761  O  OD2  . ASP A 1 52  ? 8.83816  0.98107  3.09123  1.000 51.72195  ? 77   ASP A OD2  1 
ATOM   762  H  H    . ASP A 1 52  ? 6.63492  4.38591  2.31886  1.000 45.14849  ? 77   ASP A H    1 
ATOM   763  H  HA   . ASP A 1 52  ? 5.72002  2.66236  0.50203  1.000 55.05384  ? 77   ASP A HA   1 
ATOM   764  H  HB2  . ASP A 1 52  ? 6.44292  0.74567  1.73594  1.000 46.10669  ? 77   ASP A HB2  1 
ATOM   765  H  HB3  . ASP A 1 52  ? 7.60394  1.46279  0.92158  1.000 46.10669  ? 77   ASP A HB3  1 
ATOM   766  N  N    . GLU A 1 53  ? 3.93021  1.86500  2.11839  1.000 56.15849  ? 78   GLU A N    1 
ATOM   767  C  CA   . GLU A 1 53  ? 2.80464  1.72113  3.02994  1.000 54.23955  ? 78   GLU A CA   1 
ATOM   768  C  C    . GLU A 1 53  ? 3.29043  1.69102  4.47542  1.000 55.34762  ? 78   GLU A C    1 
ATOM   769  O  O    . GLU A 1 53  ? 2.69960  2.33865  5.34755  1.000 56.26476  ? 78   GLU A O    1 
ATOM   770  C  CB   . GLU A 1 53  ? 2.01262  0.46443  2.67849  1.000 64.94161  ? 78   GLU A CB   1 
ATOM   771  C  CG   . GLU A 1 53  ? 0.65369  0.36960  3.37348  1.000 72.14820  ? 78   GLU A CG   1 
ATOM   772  C  CD   . GLU A 1 53  ? -0.31411 1.48014  2.97035  1.000 74.75830  ? 78   GLU A CD   1 
ATOM   773  O  OE1  . GLU A 1 53  ? -0.27325 1.91730  1.79497  1.000 77.95030  ? 78   GLU A OE1  1 
ATOM   774  O  OE2  . GLU A 1 53  ? -1.11773 1.90017  3.83482  1.000 71.24158  ? 78   GLU A OE2  1 
ATOM   775  H  H    . GLU A 1 53  ? 3.91253  1.34187  1.43602  1.000 67.72004  ? 78   GLU A H    1 
ATOM   776  H  HA   . GLU A 1 53  ? 2.20255  2.47561  2.93432  1.000 65.41730  ? 78   GLU A HA   1 
ATOM   777  H  HB2  . GLU A 1 53  ? 1.85574  0.45363  1.72133  1.000 78.25978  ? 78   GLU A HB2  1 
ATOM   778  H  HB3  . GLU A 1 53  ? 2.53165  -0.31272 2.93840  1.000 78.25978  ? 78   GLU A HB3  1 
ATOM   779  H  HG2  . GLU A 1 53  ? 0.24345  -0.47919 3.14512  1.000 86.90769  ? 78   GLU A HG2  1 
ATOM   780  H  HG3  . GLU A 1 53  ? 0.78755  0.42602  4.33254  1.000 86.90769  ? 78   GLU A HG3  1 
ATOM   781  N  N    . GLU A 1 54  ? 4.39442  0.98389  4.73474  1.000 49.55773  ? 79   GLU A N    1 
ATOM   782  C  CA   . GLU A 1 54  ? 4.99167  0.94532  6.06705  1.000 51.88883  ? 79   GLU A CA   1 
ATOM   783  C  C    . GLU A 1 54  ? 5.09491  2.33873  6.68847  1.000 50.25887  ? 79   GLU A C    1 
ATOM   784  O  O    . GLU A 1 54  ? 4.57137  2.59622  7.78308  1.000 48.21127  ? 79   GLU A O    1 
ATOM   785  C  CB   . GLU A 1 54  ? 6.38644  0.29783  5.98274  1.000 53.08055  ? 79   GLU A CB   1 
ATOM   786  C  CG   . GLU A 1 54  ? 7.29353  0.50001  7.21034  1.000 47.90918  ? 79   GLU A CG   1 
ATOM   787  C  CD   . GLU A 1 54  ? 7.16702  -0.61537 8.22814  1.000 63.61254  ? 79   GLU A CD   1 
ATOM   788  O  OE1  . GLU A 1 54  ? 6.65578  -1.69896 7.87176  1.000 70.01831  ? 79   GLU A OE1  1 
ATOM   789  O  OE2  . GLU A 1 54  ? 7.57418  -0.41302 9.39070  1.000 67.60721  ? 79   GLU A OE2  1 
ATOM   790  H  H    . GLU A 1 54  ? 4.81818  0.51535  4.15122  1.000 59.79913  ? 79   GLU A H    1 
ATOM   791  H  HA   . GLU A 1 54  ? 4.42385  0.40727  6.64062  1.000 62.59644  ? 79   GLU A HA   1 
ATOM   792  H  HB2  . GLU A 1 54  ? 6.27120  -0.65804 5.86469  1.000 64.02651  ? 79   GLU A HB2  1 
ATOM   793  H  HB3  . GLU A 1 54  ? 6.85003  0.67307  5.21777  1.000 64.02651  ? 79   GLU A HB3  1 
ATOM   794  H  HG2  . GLU A 1 54  ? 8.21762  0.53437  6.91746  1.000 57.82086  ? 79   GLU A HG2  1 
ATOM   795  H  HG3  . GLU A 1 54  ? 7.05270  1.33208  7.64686  1.000 57.82086  ? 79   GLU A HG3  1 
ATOM   796  N  N    . SER A 1 55  ? 5.83078  3.23159  6.03314  1.000 44.38504  ? 80   SER A N    1 
ATOM   797  C  CA   . SER A 1 55  ? 6.20193  4.50787  6.62649  1.000 36.48517  ? 80   SER A CA   1 
ATOM   798  C  C    . SER A 1 55  ? 5.28860  5.63757  6.20123  1.000 30.42397  ? 80   SER A C    1 
ATOM   799  O  O    . SER A 1 55  ? 5.65967  6.80222  6.35432  1.000 24.16621  ? 80   SER A O    1 
ATOM   800  C  CB   . SER A 1 55  ? 7.66545  4.82834  6.28271  1.000 33.82605  ? 80   SER A CB   1 
ATOM   801  O  OG   . SER A 1 55  ? 7.89232  4.82204  4.88175  1.000 35.08651  ? 80   SER A OG   1 
ATOM   802  H  H    . SER A 1 55  ? 6.12926  3.11759  5.23470  1.000 53.59189  ? 80   SER A H    1 
ATOM   803  H  HA   . SER A 1 55  ? 6.12889  4.43686  7.59112  1.000 44.11205  ? 80   SER A HA   1 
ATOM   804  H  HB2  . SER A 1 55  ? 7.88174  5.70799  6.62960  1.000 40.92111  ? 80   SER A HB2  1 
ATOM   805  H  HB3  . SER A 1 55  ? 8.23579  4.16012  6.69390  1.000 40.92111  ? 80   SER A HB3  1 
ATOM   806  H  HG   . SER A 1 55  ? 8.69170  5.02250  4.71926  1.000 42.43366  ? 80   SER A HG   1 
ATOM   807  N  N    . LYS A 1 56  ? 4.08415  5.32583  5.68852  1.000 28.15280  ? 81   LYS A N    1 
ATOM   808  C  CA   . LYS A 1 56  ? 3.24173  6.37421  5.11323  1.000 28.72659  ? 81   LYS A CA   1 
ATOM   809  C  C    . LYS A 1 56  ? 2.76167  7.37409  6.15762  1.000 31.55370  ? 81   LYS A C    1 
ATOM   810  O  O    . LYS A 1 56  ? 2.47058  8.52235  5.79782  1.000 28.76408  ? 81   LYS A O    1 
ATOM   811  C  CB   . LYS A 1 56  ? 2.08141  5.72812  4.36202  1.000 36.23064  ? 81   LYS A CB   1 
ATOM   812  C  CG   . LYS A 1 56  ? 0.77889  5.63706  5.12110  1.000 39.63915  ? 81   LYS A CG   1 
ATOM   813  C  CD   . LYS A 1 56  ? -0.34195 5.17474  4.20401  1.000 51.24698  ? 81   LYS A CD   1 
ATOM   814  C  CE   . LYS A 1 56  ? -1.53082 4.67602  4.99351  1.000 52.16389  ? 81   LYS A CE   1 
ATOM   815  N  NZ   . LYS A 1 56  ? -2.48137 3.93165  4.11175  1.000 76.41868  ? 81   LYS A NZ   1 
ATOM   816  H  H    . LYS A 1 56  ? 3.74636  4.53530  5.66502  1.000 32.99818  ? 81   LYS A H    1 
ATOM   817  H  HA   . LYS A 1 56  ? 3.74901  6.88915  4.46639  1.000 34.80175  ? 81   LYS A HA   1 
ATOM   818  H  HB2  . LYS A 1 56  ? 1.91154  6.24704  3.56030  1.000 43.80661  ? 81   LYS A HB2  1 
ATOM   819  H  HB3  . LYS A 1 56  ? 2.33929  4.82395  4.12355  1.000 43.80661  ? 81   LYS A HB3  1 
ATOM   820  H  HG2  . LYS A 1 56  ? 0.86885  4.99802  5.84528  1.000 47.89683  ? 81   LYS A HG2  1 
ATOM   821  H  HG3  . LYS A 1 56  ? 0.54772  6.50985  5.47563  1.000 47.89683  ? 81   LYS A HG3  1 
ATOM   822  H  HD2  . LYS A 1 56  ? -0.63227 5.91719  3.65139  1.000 61.82622  ? 81   LYS A HD2  1 
ATOM   823  H  HD3  . LYS A 1 56  ? -0.02146 4.45012  3.64445  1.000 61.82622  ? 81   LYS A HD3  1 
ATOM   824  H  HE2  . LYS A 1 56  ? -1.22640 4.07678  5.69289  1.000 62.92651  ? 81   LYS A HE2  1 
ATOM   825  H  HE3  . LYS A 1 56  ? -1.99953 5.43032  5.38369  1.000 62.92651  ? 81   LYS A HE3  1 
ATOM   826  H  HZ1  . LYS A 1 56  ? -3.18194 3.65398  4.58526  1.000 92.03226  ? 81   LYS A HZ1  1 
ATOM   827  H  HZ2  . LYS A 1 56  ? -2.76739 4.46170  3.45651  1.000 92.03226  ? 81   LYS A HZ2  1 
ATOM   828  H  HZ3  . LYS A 1 56  ? -2.07540 3.22459  3.75489  1.000 92.03226  ? 81   LYS A HZ3  1 
ATOM   829  N  N    . ASP A 1 57  ? 2.71844  6.97869  7.43240  1.000 30.48908  ? 82   ASP A N    1 
ATOM   830  C  CA   . ASP A 1 57  ? 2.35285  7.86225  8.53596  1.000 33.00105  ? 82   ASP A CA   1 
ATOM   831  C  C    . ASP A 1 57  ? 3.51153  8.70594  9.02131  1.000 31.76274  ? 82   ASP A C    1 
ATOM   832  O  O    . ASP A 1 57  ? 3.35794  9.42607  10.01676 1.000 25.12796  ? 82   ASP A O    1 
ATOM   833  C  CB   . ASP A 1 57  ? 1.85945  7.04866  9.73008  1.000 34.32071  ? 82   ASP A CB   1 
ATOM   834  C  CG   . ASP A 1 57  ? 0.56229  6.35741  9.47644  1.000 42.63149  ? 82   ASP A CG   1 
ATOM   835  O  OD1  . ASP A 1 57  ? -0.44910 7.03202  9.13040  1.000 50.54048  ? 82   ASP A OD1  1 
ATOM   836  O  OD2  . ASP A 1 57  ? 0.54640  5.12377  9.63007  1.000 47.83179  ? 82   ASP A OD2  1 
ATOM   837  H  H    . ASP A 1 57  ? 2.90253  6.17885  7.68923  1.000 36.91674  ? 82   ASP A H    1 
ATOM   838  H  HA   . ASP A 1 57  ? 1.63837  8.43846  8.22229  1.000 39.93110  ? 82   ASP A HA   1 
ATOM   839  H  HB2  . ASP A 1 57  ? 2.52068  6.37192  9.94389  1.000 41.51469  ? 82   ASP A HB2  1 
ATOM   840  H  HB3  . ASP A 1 57  ? 1.73698  7.64349  10.48643 1.000 41.51469  ? 82   ASP A HB3  1 
ATOM   841  N  N    . TYR A 1 58  ? 4.66459  8.59406  8.38240  1.000 26.02776  ? 83   TYR A N    1 
ATOM   842  C  CA   . TYR A 1 58  ? 5.85268  9.29626  8.81760  1.000 26.54620  ? 83   TYR A CA   1 
ATOM   843  C  C    . TYR A 1 58  ? 6.40747  10.15440 7.69842  1.000 29.22700  ? 83   TYR A C    1 
ATOM   844  O  O    . TYR A 1 58  ? 6.19899  9.89431  6.49734  1.000 24.01303  ? 83   TYR A O    1 
ATOM   845  C  CB   . TYR A 1 58  ? 6.97445  8.34574  9.27714  1.000 24.71807  ? 83   TYR A CB   1 
ATOM   846  C  CG   . TYR A 1 58  ? 6.62493  7.55003  10.50925 1.000 25.66978  ? 83   TYR A CG   1 
ATOM   847  C  CD1  . TYR A 1 58  ? 5.71961  6.49735  10.43043 1.000 29.28863  ? 83   TYR A CD1  1 
ATOM   848  C  CD2  . TYR A 1 58  ? 7.21131  7.82830  11.74001 1.000 24.37016  ? 83   TYR A CD2  1 
ATOM   849  C  CE1  . TYR A 1 58  ? 5.40997  5.74690  11.51726 1.000 28.82483  ? 83   TYR A CE1  1 
ATOM   850  C  CE2  . TYR A 1 58  ? 6.90392  7.09431  12.84277 1.000 26.72367  ? 83   TYR A CE2  1 
ATOM   851  C  CZ   . TYR A 1 58  ? 5.99304  6.05178  12.74268 1.000 30.56107  ? 83   TYR A CZ   1 
ATOM   852  O  OH   . TYR A 1 58  ? 5.66617  5.31647  13.85126 1.000 40.75534  ? 83   TYR A OH   1 
ATOM   853  H  H    . TYR A 1 58  ? 4.78263  8.10835  7.68259  1.000 31.56316  ? 83   TYR A H    1 
ATOM   854  H  HA   . TYR A 1 58  ? 5.59190  9.85854  9.56376  1.000 32.18529  ? 83   TYR A HA   1 
ATOM   855  H  HB2  . TYR A 1 58  ? 7.16424  7.71794  8.56248  1.000 29.99153  ? 83   TYR A HB2  1 
ATOM   856  H  HB3  . TYR A 1 58  ? 7.76573  8.86995  9.47708  1.000 29.99153  ? 83   TYR A HB3  1 
ATOM   857  H  HD1  . TYR A 1 58  ? 5.31755  6.30355  9.61453  1.000 35.47620  ? 83   TYR A HD1  1 
ATOM   858  H  HD2  . TYR A 1 58  ? 7.82211  8.52616  11.80946 1.000 29.57403  ? 83   TYR A HD2  1 
ATOM   859  H  HE1  . TYR A 1 58  ? 4.81440  5.03641  11.44380 1.000 32.94057  ? 83   TYR A HE1  1 
ATOM   860  H  HE2  . TYR A 1 58  ? 7.30212  7.28994  13.66011 1.000 30.41918  ? 83   TYR A HE2  1 
ATOM   861  H  HH   . TYR A 1 58  ? 6.08119  5.60696  14.52131 1.000 49.23625  ? 83   TYR A HH   1 
ATOM   862  N  N    . LEU A 1 59  ? 7.16663  11.14688 8.10739  1.000 24.70342  ? 84   LEU A N    1 
ATOM   863  C  CA   . LEU A 1 59  ? 8.03591  11.86612 7.20684  1.000 18.27676  ? 84   LEU A CA   1 
ATOM   864  C  C    . LEU A 1 59  ? 9.40677  11.24822 7.31284  1.000 20.96174  ? 84   LEU A C    1 
ATOM   865  O  O    . LEU A 1 59  ? 9.89923  11.05724 8.43237  1.000 22.84527  ? 84   LEU A O    1 
ATOM   866  C  CB   . LEU A 1 59  ? 8.09467  13.33312 7.55611  1.000 16.50457  ? 84   LEU A CB   1 
ATOM   867  C  CG   . LEU A 1 59  ? 9.07659  14.12322 6.72902  1.000 21.61795  ? 84   LEU A CG   1 
ATOM   868  C  CD1  . LEU A 1 59  ? 8.45909  15.50168 6.54622  1.000 26.23390  ? 84   LEU A CD1  1 
ATOM   869  C  CD2  . LEU A 1 59  ? 10.40824 14.18704 7.41506  1.000 27.56868  ? 84   LEU A CD2  1 
ATOM   870  H  H    . LEU A 1 59  ? 7.19606  11.42805 8.91959  1.000 29.97395  ? 84   LEU A H    1 
ATOM   871  H  HA   . LEU A 1 59  ? 7.71223  11.80018 6.29482  1.000 22.26195  ? 84   LEU A HA   1 
ATOM   872  H  HB2  . LEU A 1 59  ? 7.21545  13.71959 7.41999  1.000 18.15626  ? 84   LEU A HB2  1 
ATOM   873  H  HB3  . LEU A 1 59  ? 8.35484  13.42003 8.48652  1.000 18.15626  ? 84   LEU A HB3  1 
ATOM   874  H  HG   . LEU A 1 59  ? 9.24689  13.71700 5.86480  1.000 26.27139  ? 84   LEU A HG   1 
ATOM   875  H  HD11 . LEU A 1 59  ? 8.18032  15.84012 7.41146  1.000 31.81052  ? 84   LEU A HD11 1 
ATOM   876  H  HD12 . LEU A 1 59  ? 9.12032  16.09477 6.15645  1.000 31.81052  ? 84   LEU A HD12 1 
ATOM   877  H  HD13 . LEU A 1 59  ? 7.69210  15.42851 5.95691  1.000 31.81052  ? 84   LEU A HD13 1 
ATOM   878  H  HD21 . LEU A 1 59  ? 10.92866 14.90831 7.02798  1.000 33.41226  ? 84   LEU A HD21 1 
ATOM   879  H  HD22 . LEU A 1 59  ? 10.26868 14.35053 8.36094  1.000 33.41226  ? 84   LEU A HD22 1 
ATOM   880  H  HD23 . LEU A 1 59  ? 10.86883 13.34262 7.28976  1.000 33.41226  ? 84   LEU A HD23 1 
ATOM   881  N  N    . SER A 1 60  ? 9.99573  10.91043 6.16056  1.000 22.70395  ? 85   SER A N    1 
ATOM   882  C  CA   . SER A 1 60  ? 11.36197 10.41147 6.09595  1.000 19.87612  ? 85   SER A CA   1 
ATOM   883  C  C    . SER A 1 60  ? 12.31987 11.55791 5.83356  1.000 19.93677  ? 85   SER A C    1 
ATOM   884  O  O    . SER A 1 60  ? 11.97563 12.53506 5.17344  1.000 17.31170  ? 85   SER A O    1 
ATOM   885  C  CB   . SER A 1 60  ? 11.51361 9.39292  4.97880  1.000 20.10518  ? 85   SER A CB   1 
ATOM   886  O  OG   . SER A 1 60  ? 10.41154 8.50019  4.96697  1.000 21.21039  ? 85   SER A OG   1 
ATOM   887  H  H    . SER A 1 60  ? 9.61327  10.96429 5.39217  1.000 27.57458  ? 85   SER A H    1 
ATOM   888  H  HA   . SER A 1 60  ? 11.58471 9.98670  6.93907  1.000 24.18118  ? 85   SER A HA   1 
ATOM   889  H  HB2  . SER A 1 60  ? 11.55376 9.85835  4.12870  1.000 24.45606  ? 85   SER A HB2  1 
ATOM   890  H  HB3  . SER A 1 60  ? 12.32955 8.88750  5.11917  1.000 24.45606  ? 85   SER A HB3  1 
ATOM   891  H  HG   . SER A 1 60  ? 10.27334 8.20409  5.74081  1.000 25.78231  ? 85   SER A HG   1 
ATOM   892  N  N    . LEU A 1 61  ? 13.56181 11.38292 6.26794  1.000 17.48853  ? 86   LEU A N    1 
ATOM   893  C  CA   . LEU A 1 61  ? 14.56780 12.40570 6.08299  1.000 18.79480  ? 86   LEU A CA   1 
ATOM   894  C  C    . LEU A 1 61  ? 15.92270 11.76211 5.82684  1.000 22.13336  ? 86   LEU A C    1 
ATOM   895  O  O    . LEU A 1 61  ? 16.34588 10.87036 6.57567  1.000 19.08561  ? 86   LEU A O    1 
ATOM   896  C  CB   . LEU A 1 61  ? 14.63329 13.28529 7.29407  1.000 23.56553  ? 86   LEU A CB   1 
ATOM   897  C  CG   . LEU A 1 61  ? 15.63249 14.45264 7.25556  1.000 18.51850  ? 86   LEU A CG   1 
ATOM   898  C  CD1  . LEU A 1 61  ? 15.50339 15.33136 6.05016  1.000 21.67128  ? 86   LEU A CD1  1 
ATOM   899  C  CD2  . LEU A 1 61  ? 15.39978 15.17624 8.57168  1.000 24.46861  ? 86   LEU A CD2  1 
ATOM   900  H  H    . LEU A 1 61  ? 13.84136 10.67751 6.67272  1.000 21.31608  ? 86   LEU A H    1 
ATOM   901  H  HA   . LEU A 1 61  ? 14.35099 12.94220 5.30449  1.000 22.88360  ? 86   LEU A HA   1 
ATOM   902  H  HB2  . LEU A 1 61  ? 13.75361 13.67034 7.43118  1.000 28.60848  ? 86   LEU A HB2  1 
ATOM   903  H  HB3  . LEU A 1 61  ? 14.87480 12.73115 8.05268  1.000 28.60848  ? 86   LEU A HB3  1 
ATOM   904  H  HG   . LEU A 1 61  ? 16.54978 14.14983 7.16732  1.000 22.55205  ? 86   LEU A HG   1 
ATOM   905  H  HD11 . LEU A 1 61  ? 15.67542 14.80356 5.25471  1.000 26.33538  ? 86   LEU A HD11 1 
ATOM   906  H  HD12 . LEU A 1 61  ? 14.60425 15.69392 6.01849  1.000 26.33538  ? 86   LEU A HD12 1 
ATOM   907  H  HD13 . LEU A 1 61  ? 16.14880 16.05260 6.11454  1.000 26.33538  ? 86   LEU A HD13 1 
ATOM   908  H  HD21 . LEU A 1 61  ? 14.51120 15.56520 8.56540  1.000 29.69217  ? 86   LEU A HD21 1 
ATOM   909  H  HD22 . LEU A 1 61  ? 15.47725 14.54008 9.29982  1.000 29.69217  ? 86   LEU A HD22 1 
ATOM   910  H  HD23 . LEU A 1 61  ? 16.06582 15.87450 8.67023  1.000 29.69217  ? 86   LEU A HD23 1 
ATOM   911  N  N    . TYR A 1 62  ? 16.57833 12.18896 4.74944  1.000 19.79931  ? 87   TYR A N    1 
ATOM   912  C  CA   . TYR A 1 62  ? 17.79678 11.53278 4.30548  1.000 21.02799  ? 87   TYR A CA   1 
ATOM   913  C  C    . TYR A 1 62  ? 18.84137 12.55683 3.92626  1.000 21.56011  ? 87   TYR A C    1 
ATOM   914  O  O    . TYR A 1 62  ? 18.50516 13.63055 3.43359  1.000 16.86869  ? 87   TYR A O    1 
ATOM   915  C  CB   . TYR A 1 62  ? 17.57474 10.66035 3.09323  1.000 20.70967  ? 87   TYR A CB   1 
ATOM   916  C  CG   . TYR A 1 62  ? 16.74818 9.44316  3.38005  1.000 21.91110  ? 87   TYR A CG   1 
ATOM   917  C  CD1  . TYR A 1 62  ? 15.37353 9.49545  3.33820  1.000 22.75119  ? 87   TYR A CD1  1 
ATOM   918  C  CD2  . TYR A 1 62  ? 17.34499 8.24973  3.67497  1.000 26.75236  ? 87   TYR A CD2  1 
ATOM   919  C  CE1  . TYR A 1 62  ? 14.61069 8.36782  3.57846  1.000 26.70930  ? 87   TYR A CE1  1 
ATOM   920  C  CE2  . TYR A 1 62  ? 16.59171 7.12640  3.96164  1.000 27.34184  ? 87   TYR A CE2  1 
ATOM   921  C  CZ   . TYR A 1 62  ? 15.23293 7.19357  3.88585  1.000 28.23298  ? 87   TYR A CZ   1 
ATOM   922  O  OH   . TYR A 1 62  ? 14.48593 6.04353  4.10836  1.000 31.33538  ? 87   TYR A OH   1 
ATOM   923  H  H    . TYR A 1 62  ? 16.33483 12.85506 4.26301  1.000 24.08901  ? 87   TYR A H    1 
ATOM   924  H  HA   . TYR A 1 62  ? 18.11779 10.99567 5.04668  1.000 25.56343  ? 87   TYR A HA   1 
ATOM   925  H  HB2  . TYR A 1 62  ? 17.11564 11.17872 2.41395  1.000 25.18145  ? 87   TYR A HB2  1 
ATOM   926  H  HB3  . TYR A 1 62  ? 18.43556 10.36365 2.75877  1.000 25.18145  ? 87   TYR A HB3  1 
ATOM   927  H  HD1  . TYR A 1 62  ? 14.95147 10.30143 3.14540  1.000 27.63127  ? 87   TYR A HD1  1 
ATOM   928  H  HD2  . TYR A 1 62  ? 18.27318 8.19222  3.68298  1.000 32.43268  ? 87   TYR A HD2  1 
ATOM   929  H  HE1  . TYR A 1 62  ? 13.68284 8.40943  3.53100  1.000 32.38101  ? 87   TYR A HE1  1 
ATOM   930  H  HE2  . TYR A 1 62  ? 17.00900 6.33146  4.20422  1.000 33.14005  ? 87   TYR A HE2  1 
ATOM   931  H  HH   . TYR A 1 62  ? 14.99296 5.40797  4.31950  1.000 37.93230  ? 87   TYR A HH   1 
ATOM   932  N  N    . LEU A 1 63  ? 20.11372 12.20331 4.15612  1.000 21.38876  ? 88   LEU A N    1 
ATOM   933  C  CA   . LEU A 1 63  ? 21.27266 13.00821 3.77909  1.000 22.01348  ? 88   LEU A CA   1 
ATOM   934  C  C    . LEU A 1 63  ? 21.91381 12.31276 2.58728  1.000 15.90631  ? 88   LEU A C    1 
ATOM   935  O  O    . LEU A 1 63  ? 22.25020 11.12115 2.68368  1.000 18.28755  ? 88   LEU A O    1 
ATOM   936  C  CB   . LEU A 1 63  ? 22.27147 13.14580 4.92571  1.000 15.45990  ? 88   LEU A CB   1 
ATOM   937  C  CG   . LEU A 1 63  ? 23.56338 13.92541 4.71764  1.000 17.69177  ? 88   LEU A CG   1 
ATOM   938  C  CD1  . LEU A 1 63  ? 23.21371 15.32416 4.33188  1.000 27.24207  ? 88   LEU A CD1  1 
ATOM   939  C  CD2  . LEU A 1 63  ? 24.44165 13.93545 5.88831  1.000 20.37487  ? 88   LEU A CD2  1 
ATOM   940  H  H    . LEU A 1 63  ? 20.33454 11.46929 4.54604  1.000 25.99636  ? 88   LEU A H    1 
ATOM   941  H  HA   . LEU A 1 63  ? 20.99603 13.90593 3.53730  1.000 26.74602  ? 88   LEU A HA   1 
ATOM   942  H  HB2  . LEU A 1 63  ? 21.80857 13.58061 5.65890  1.000 18.88172  ? 88   LEU A HB2  1 
ATOM   943  H  HB3  . LEU A 1 63  ? 22.53569 12.24929 5.18527  1.000 18.88172  ? 88   LEU A HB3  1 
ATOM   944  H  HG   . LEU A 1 63  ? 24.06961 13.48513 4.01709  1.000 21.55997  ? 88   LEU A HG   1 
ATOM   945  H  HD11 . LEU A 1 63  ? 22.67363 15.71971 5.03385  1.000 33.02032  ? 88   LEU A HD11 1 
ATOM   946  H  HD12 . LEU A 1 63  ? 24.03104 15.83364 4.21656  1.000 33.02032  ? 88   LEU A HD12 1 
ATOM   947  H  HD13 . LEU A 1 63  ? 22.71450 15.30702 3.50038  1.000 33.02032  ? 88   LEU A HD13 1 
ATOM   948  H  HD21 . LEU A 1 63  ? 25.23066 14.46242 5.68666  1.000 24.77968  ? 88   LEU A HD21 1 
ATOM   949  H  HD22 . LEU A 1 63  ? 23.96517 14.32658 6.63723  1.000 24.77968  ? 88   LEU A HD22 1 
ATOM   950  H  HD23 . LEU A 1 63  ? 24.69766 13.02385 6.09887  1.000 24.77968  ? 88   LEU A HD23 1 
ATOM   951  N  N    . LEU A 1 64  ? 22.05457 13.05555 1.47309  1.000 19.55778  ? 89   LEU A N    1 
ATOM   952  C  CA   . LEU A 1 64  ? 22.66731 12.61433 0.20503  1.000 21.80376  ? 89   LEU A CA   1 
ATOM   953  C  C    . LEU A 1 64  ? 24.03238 13.28807 -0.02645 1.000 20.86280  ? 89   LEU A C    1 
ATOM   954  O  O    . LEU A 1 64  ? 24.16107 14.51341 0.08455  1.000 22.18348  ? 89   LEU A O    1 
ATOM   955  C  CB   . LEU A 1 64  ? 21.71654 12.94484 -0.96298 1.000 25.45905  ? 89   LEU A CB   1 
ATOM   956  C  CG   . LEU A 1 64  ? 21.90029 12.31560 -2.34588 1.000 28.02786  ? 89   LEU A CG   1 
ATOM   957  C  CD1  . LEU A 1 64  ? 20.81584 12.66911 -3.32257 1.000 38.61862  ? 89   LEU A CD1  1 
ATOM   958  C  CD2  . LEU A 1 64  ? 23.17158 12.73758 -2.93054 1.000 32.53810  ? 89   LEU A CD2  1 
ATOM   959  H  H    . LEU A 1 64  ? 21.78514 13.87084 1.42508  1.000 23.79918  ? 89   LEU A H    1 
ATOM   960  H  HA   . LEU A 1 64  ? 22.83252 11.65946 0.24791  1.000 26.49436  ? 89   LEU A HA   1 
ATOM   961  H  HB2  . LEU A 1 64  ? 20.82372 12.69577 -0.67709 1.000 30.88071  ? 89   LEU A HB2  1 
ATOM   962  H  HB3  . LEU A 1 64  ? 21.76512 13.90365 -1.10160 1.000 30.88071  ? 89   LEU A HB3  1 
ATOM   963  H  HG   . LEU A 1 64  ? 21.87336 11.35622 -2.20534 1.000 33.96327  ? 89   LEU A HG   1 
ATOM   964  H  HD11 . LEU A 1 64  ? 19.99127 12.82509 -2.83610 1.000 46.67219  ? 89   LEU A HD11 1 
ATOM   965  H  HD12 . LEU A 1 64  ? 21.07307 13.47134 -3.80336 1.000 46.67219  ? 89   LEU A HD12 1 
ATOM   966  H  HD13 . LEU A 1 64  ? 20.69899 11.93392 -3.94446 1.000 46.67219  ? 89   LEU A HD13 1 
ATOM   967  H  HD21 . LEU A 1 64  ? 23.89039 12.22821 -2.52463 1.000 39.37557  ? 89   LEU A HD21 1 
ATOM   968  H  HD22 . LEU A 1 64  ? 23.14925 12.57423 -3.88643 1.000 39.37557  ? 89   LEU A HD22 1 
ATOM   969  H  HD23 . LEU A 1 64  ? 23.29919 13.68382 -2.75956 1.000 39.37557  ? 89   LEU A HD23 1 
ATOM   970  N  N    . LEU A 1 65  ? 25.05956 12.49020 -0.33493 1.000 19.71475  ? 90   LEU A N    1 
ATOM   971  C  CA   . LEU A 1 65  ? 26.32322 13.03758 -0.80232 1.000 19.02560  ? 90   LEU A CA   1 
ATOM   972  C  C    . LEU A 1 65  ? 26.23629 13.33103 -2.29709 1.000 27.36506  ? 90   LEU A C    1 
ATOM   973  O  O    . LEU A 1 65  ? 26.11429 12.41251 -3.12400 1.000 26.64057  ? 90   LEU A O    1 
ATOM   974  C  CB   . LEU A 1 65  ? 27.47284 12.06010 -0.51426 1.000 23.23620  ? 90   LEU A CB   1 
ATOM   975  C  CG   . LEU A 1 65  ? 28.87935 12.48182 -0.94455 1.000 25.26824  ? 90   LEU A CG   1 
ATOM   976  C  CD1  . LEU A 1 65  ? 29.27987 13.75756 -0.23406 1.000 22.34851  ? 90   LEU A CD1  1 
ATOM   977  C  CD2  . LEU A 1 65  ? 29.84282 11.36500 -0.64095 1.000 23.25085  ? 90   LEU A CD2  1 
ATOM   978  H  H    . LEU A 1 65  ? 25.04368 11.63209 -0.28011 1.000 23.98754  ? 90   LEU A H    1 
ATOM   979  H  HA   . LEU A 1 65  ? 26.50162 13.86795 -0.33374 1.000 23.16056  ? 90   LEU A HA   1 
ATOM   980  H  HB2  . LEU A 1 65  ? 27.50422 11.91265 0.44396  1.000 28.21328  ? 90   LEU A HB2  1 
ATOM   981  H  HB3  . LEU A 1 65  ? 27.27651 11.22762 -0.97177 1.000 28.21328  ? 90   LEU A HB3  1 
ATOM   982  H  HG   . LEU A 1 65  ? 28.90358 12.65905 -1.89791 1.000 30.65173  ? 90   LEU A HG   1 
ATOM   983  H  HD11 . LEU A 1 65  ? 28.71818 14.48347 -0.54783 1.000 27.14805  ? 90   LEU A HD11 1 
ATOM   984  H  HD12 . LEU A 1 65  ? 29.16209 13.63734 0.72123  1.000 27.14805  ? 90   LEU A HD12 1 
ATOM   985  H  HD13 . LEU A 1 65  ? 30.20994 13.95009 -0.43103 1.000 27.14805  ? 90   LEU A HD13 1 
ATOM   986  H  HD21 . LEU A 1 65  ? 30.01840 11.34995 0.31291  1.000 28.23087  ? 90   LEU A HD21 1 
ATOM   987  H  HD22 . LEU A 1 65  ? 29.44809 10.52336 -0.91795 1.000 28.23087  ? 90   LEU A HD22 1 
ATOM   988  H  HD23 . LEU A 1 65  ? 30.66811 11.51908 -1.12681 1.000 28.23087  ? 90   LEU A HD23 1 
ATOM   989  N  N    . VAL A 1 66  ? 26.35801 14.60990 -2.66295 1.000 24.53297  ? 91   VAL A N    1 
ATOM   990  C  CA   . VAL A 1 66  ? 26.31467 15.00234 -4.05891 1.000 25.41990  ? 91   VAL A CA   1 
ATOM   991  C  C    . VAL A 1 66  ? 27.68033 15.04883 -4.72504 1.000 25.41168  ? 91   VAL A C    1 
ATOM   992  O  O    . VAL A 1 66  ? 27.78476 14.82534 -5.93913 1.000 29.85692  ? 91   VAL A O    1 
ATOM   993  C  CB   . VAL A 1 66  ? 25.60638 16.36842 -4.17197 1.000 22.40568  ? 91   VAL A CB   1 
ATOM   994  C  CG1  . VAL A 1 66  ? 25.71245 16.87993 -5.58099 1.000 23.97834  ? 91   VAL A CG1  1 
ATOM   995  C  CG2  . VAL A 1 66  ? 24.16095 16.21948 -3.74066 1.000 22.61553  ? 91   VAL A CG2  1 
ATOM   996  H  H    . VAL A 1 66  ? 26.46650 15.26517 -2.11664 1.000 29.76941  ? 91   VAL A H    1 
ATOM   997  H  HA   . VAL A 1 66  ? 25.80978 14.33054 -4.54334 1.000 30.83373  ? 91   VAL A HA   1 
ATOM   998  H  HB   . VAL A 1 66  ? 26.02869 17.02002 -3.59062 1.000 27.21666  ? 91   VAL A HB   1 
ATOM   999  H  HG11 . VAL A 1 66  ? 25.76958 16.12510 -6.18752 1.000 29.10385  ? 91   VAL A HG11 1 
ATOM   1000 H  HG12 . VAL A 1 66  ? 24.92560 17.40926 -5.78487 1.000 29.10385  ? 91   VAL A HG12 1 
ATOM   1001 H  HG13 . VAL A 1 66  ? 26.50904 17.42789 -5.65891 1.000 29.10385  ? 91   VAL A HG13 1 
ATOM   1002 H  HG21 . VAL A 1 66  ? 24.12582 15.68121 -2.93447 1.000 27.46848  ? 91   VAL A HG21 1 
ATOM   1003 H  HG22 . VAL A 1 66  ? 23.79084 17.09920 -3.56742 1.000 27.46848  ? 91   VAL A HG22 1 
ATOM   1004 H  HG23 . VAL A 1 66  ? 23.66275 15.78494 -4.45050 1.000 27.46848  ? 91   VAL A HG23 1 
ATOM   1005 N  N    . SER A 1 67  ? 28.74143 15.33123 -3.97434 1.000 27.97177  ? 92   SER A N    1 
ATOM   1006 C  CA   . SER A 1 67  ? 30.06377 15.42567 -4.56716 1.000 26.04543  ? 92   SER A CA   1 
ATOM   1007 C  C    . SER A 1 67  ? 31.10705 15.19248 -3.49821 1.000 24.60467  ? 92   SER A C    1 
ATOM   1008 O  O    . SER A 1 67  ? 30.98155 15.69219 -2.38166 1.000 28.48947  ? 92   SER A O    1 
ATOM   1009 C  CB   . SER A 1 67  ? 30.31035 16.78815 -5.21832 1.000 30.89451  ? 92   SER A CB   1 
ATOM   1010 O  OG   . SER A 1 67  ? 31.59974 16.84717 -5.79968 1.000 36.27685  ? 92   SER A OG   1 
ATOM   1011 H  H    . SER A 1 67  ? 28.71813 15.47073 -3.12605 1.000 33.89597  ? 92   SER A H    1 
ATOM   1012 H  HA   . SER A 1 67  ? 30.14160 14.73747 -5.24630 1.000 31.58436  ? 92   SER A HA   1 
ATOM   1013 H  HB2  . SER A 1 67  ? 29.64589 16.93150 -5.91031 1.000 37.40326  ? 92   SER A HB2  1 
ATOM   1014 H  HB3  . SER A 1 67  ? 30.23824 17.47874 -4.54098 1.000 37.40326  ? 92   SER A HB3  1 
ATOM   1015 H  HG   . SER A 1 67  ? 31.67235 16.26171 -6.39765 1.000 43.86207  ? 92   SER A HG   1 
ATOM   1016 N  N    . CYS A 1 68  ? 32.13372 14.45285 -3.84577 1.000 24.54006  ? 93   CYS A N    1 
ATOM   1017 C  CA   . CYS A 1 68  ? 33.32121 14.35338 -3.01571 1.000 31.12557  ? 93   CYS A CA   1 
ATOM   1018 C  C    . CYS A 1 68  ? 34.52341 14.24926 -3.93782 1.000 30.55088  ? 93   CYS A C    1 
ATOM   1019 O  O    . CYS A 1 68  ? 34.39046 13.89765 -5.11602 1.000 30.15388  ? 93   CYS A O    1 
ATOM   1020 C  CB   . CYS A 1 68  ? 33.24718 13.15838 -2.05733 1.000 27.12782  ? 93   CYS A CB   1 
ATOM   1021 S  SG   . CYS A 1 68  ? 32.98546 11.51988 -2.83993 1.000 33.62533  ? 93   CYS A SG   1 
ATOM   1022 H  H    . CYS A 1 68  ? 32.17144 13.98953 -4.56931 1.000 29.77792  ? 93   CYS A H    1 
ATOM   1023 H  HA   . CYS A 1 68  ? 33.42581 15.14729 -2.46828 1.000 37.68053  ? 93   CYS A HA   1 
ATOM   1024 H  HB2  . CYS A 1 68  ? 34.08190 13.11167 -1.56544 1.000 32.88322  ? 93   CYS A HB2  1 
ATOM   1025 H  HB3  . CYS A 1 68  ? 32.50920 13.30548 -1.44525 1.000 32.88322  ? 93   CYS A HB3  1 
ATOM   1026 H  HG   . CYS A 1 68  ? 33.92398 11.26900 -3.54438 1.000 40.68024  ? 93   CYS A HG   1 
ATOM   1027 N  N    . PRO A 1 69  ? 35.71760 14.58514 -3.43732 1.000 30.48272  ? 94   PRO A N    1 
ATOM   1028 C  CA   . PRO A 1 69  ? 36.88639 14.67962 -4.31635 1.000 33.92652  ? 94   PRO A CA   1 
ATOM   1029 C  C    . PRO A 1 69  ? 37.71086 13.41395 -4.40089 1.000 33.08626  ? 94   PRO A C    1 
ATOM   1030 O  O    . PRO A 1 69  ? 38.70166 13.40725 -5.13340 1.000 45.17983  ? 94   PRO A O    1 
ATOM   1031 C  CB   . PRO A 1 69  ? 37.70519 15.79782 -3.66191 1.000 37.85376  ? 94   PRO A CB   1 
ATOM   1032 C  CG   . PRO A 1 69  ? 37.45030 15.54544 -2.14905 1.000 37.61722  ? 94   PRO A CG   1 
ATOM   1033 C  CD   . PRO A 1 69  ? 36.00273 15.04953 -2.06013 1.000 34.55208  ? 94   PRO A CD   1 
ATOM   1034 H  HA   . PRO A 1 69  ? 36.61792 14.95231 -5.20767 1.000 41.04167  ? 94   PRO A HA   1 
ATOM   1035 H  HB2  . PRO A 1 69  ? 38.64482 15.70941 -3.88590 1.000 45.75436  ? 94   PRO A HB2  1 
ATOM   1036 H  HB3  . PRO A 1 69  ? 37.37845 16.66798 -3.93935 1.000 45.75436  ? 94   PRO A HB3  1 
ATOM   1037 H  HG2  . PRO A 1 69  ? 38.06676 14.87329 -1.81876 1.000 45.47050  ? 94   PRO A HG2  1 
ATOM   1038 H  HG3  . PRO A 1 69  ? 37.56361 16.37161 -1.65357 1.000 45.47050  ? 94   PRO A HG3  1 
ATOM   1039 H  HD2  . PRO A 1 69  ? 35.92621 14.31904 -1.42654 1.000 41.79234  ? 94   PRO A HD2  1 
ATOM   1040 H  HD3  . PRO A 1 69  ? 35.40533 15.77106 -1.80831 1.000 41.79234  ? 94   PRO A HD3  1 
ATOM   1041 N  N    . LYS A 1 70  ? 37.39220 12.38960 -3.60994 1.000 32.88490  ? 95   LYS A N    1 
ATOM   1042 C  CA   . LYS A 1 70  ? 38.06846 11.08814 -3.70663 1.000 41.49816  ? 95   LYS A CA   1 
ATOM   1043 C  C    . LYS A 1 70  ? 36.95359 10.05658 -3.86304 1.000 46.81005  ? 95   LYS A C    1 
ATOM   1044 O  O    . LYS A 1 70  ? 36.03898 10.27588 -4.66091 1.000 49.86159  ? 95   LYS A O    1 
ATOM   1045 C  CB   . LYS A 1 70  ? 38.98057 10.82313 -2.51347 1.000 44.87354  ? 95   LYS A CB   1 
ATOM   1046 H  H    . LYS A 1 70  ? 36.78348 12.41921 -3.00316 1.000 39.29733  ? 95   LYS A H    1 
ATOM   1047 H  HA   . LYS A 1 70  ? 38.67677 11.04030 -4.46067 1.000 50.12764  ? 95   LYS A HA   1 
ATOM   1048 N  N    . SER A 1 71  ? 36.96551 8.96078  -3.10209 1.000 46.88042  ? 96   SER A N    1 
ATOM   1049 C  CA   . SER A 1 71  ? 36.04487 7.86036  -3.37725 1.000 44.97798  ? 96   SER A CA   1 
ATOM   1050 C  C    . SER A 1 71  ? 34.89438 7.77373  -2.38005 1.000 58.67119  ? 96   SER A C    1 
ATOM   1051 O  O    . SER A 1 71  ? 33.72278 7.79590  -2.78493 1.000 51.97991  ? 96   SER A O    1 
ATOM   1052 C  CB   . SER A 1 71  ? 36.78817 6.51827  -3.39559 1.000 60.21418  ? 96   SER A CB   1 
ATOM   1053 O  OG   . SER A 1 71  ? 37.30262 6.22577  -2.10254 1.000 71.89725  ? 96   SER A OG   1 
ATOM   1054 H  H    . SER A 1 71  ? 37.48979 8.83510  -2.43207 1.000 56.58635  ? 96   SER A H    1 
ATOM   1055 H  HA   . SER A 1 71  ? 35.67026 8.02573  -4.25658 1.000 54.30342  ? 96   SER A HA   1 
ATOM   1056 H  HB2  . SER A 1 71  ? 36.17254 5.81674  -3.65970 1.000 72.58686  ? 96   SER A HB2  1 
ATOM   1057 H  HB3  . SER A 1 71  ? 37.52302 6.56970  -4.02667 1.000 72.58686  ? 96   SER A HB3  1 
ATOM   1058 H  HG   . SER A 1 71  ? 37.68663 5.47871  -2.10835 1.000 86.60654  ? 96   SER A HG   1 
ATOM   1059 N  N    . GLU A 1 72  ? 35.18890 7.62591  -1.08573 1.000 52.11777  ? 97   GLU A N    1 
ATOM   1060 C  CA   . GLU A 1 72  ? 34.14247 7.47722  -0.08143 1.000 49.16548  ? 97   GLU A CA   1 
ATOM   1061 C  C    . GLU A 1 72  ? 34.38492 8.48055  1.02861  1.000 47.87313  ? 97   GLU A C    1 
ATOM   1062 O  O    . GLU A 1 72  ? 35.53348 8.85088  1.31269  1.000 42.15706  ? 97   GLU A O    1 
ATOM   1063 C  CB   . GLU A 1 72  ? 34.07706 6.05694  0.50231  1.000 43.82536  ? 97   GLU A CB   1 
ATOM   1064 C  CG   . GLU A 1 72  ? 35.35732 5.53793  1.13624  1.000 47.01688  ? 97   GLU A CG   1 
ATOM   1065 C  CD   . GLU A 1 72  ? 35.18253 4.11303  1.66729  1.000 52.34737  ? 97   GLU A CD   1 
ATOM   1066 O  OE1  . GLU A 1 72  ? 35.43329 3.12848  0.93778  1.000 51.61157  ? 97   GLU A OE1  1 
ATOM   1067 O  OE2  . GLU A 1 72  ? 34.71205 3.98685  2.81922  1.000 57.92574  ? 97   GLU A OE2  1 
ATOM   1068 H  H    . GLU A 1 72  ? 35.98827 7.60912  -0.76900 1.000 62.87117  ? 97   GLU A H    1 
ATOM   1069 H  HA   . GLU A 1 72  ? 33.28057 7.65592  -0.48898 1.000 59.32842  ? 97   GLU A HA   1 
ATOM   1070 H  HB2  . GLU A 1 72  ? 33.39130 6.04239  1.18819  1.000 52.92028  ? 97   GLU A HB2  1 
ATOM   1071 H  HB3  . GLU A 1 72  ? 33.84336 5.44547  -0.21350 1.000 52.92028  ? 97   GLU A HB3  1 
ATOM   1072 H  HG2  . GLU A 1 72  ? 36.06454 5.53169  0.47238  1.000 56.75010  ? 97   GLU A HG2  1 
ATOM   1073 H  HG3  . GLU A 1 72  ? 35.60378 6.11214  1.87815  1.000 56.75010  ? 97   GLU A HG3  1 
ATOM   1074 N  N    . VAL A 1 73  ? 33.28201 8.89925  1.64363  1.000 36.34532  ? 98   VAL A N    1 
ATOM   1075 C  CA   . VAL A 1 73  ? 33.25800 9.83779  2.75077  1.000 30.52533  ? 98   VAL A CA   1 
ATOM   1076 C  C    . VAL A 1 73  ? 32.66179 9.12879  3.95980  1.000 32.89928  ? 98   VAL A C    1 
ATOM   1077 O  O    . VAL A 1 73  ? 31.73666 8.32430  3.84294  1.000 30.11054  ? 98   VAL A O    1 
ATOM   1078 C  CB   . VAL A 1 73  ? 32.43573 11.09680 2.41070  1.000 33.46157  ? 98   VAL A CB   1 
ATOM   1079 C  CG1  . VAL A 1 73  ? 32.35379 12.03519 3.63220  1.000 34.56097  ? 98   VAL A CG1  1 
ATOM   1080 C  CG2  . VAL A 1 73  ? 33.03897 11.78786 1.23332  1.000 35.84826  ? 98   VAL A CG2  1 
ATOM   1081 H  H    . VAL A 1 73  ? 32.49387 8.63630  1.42159  1.000 43.94422  ? 98   VAL A H    1 
ATOM   1082 H  HA   . VAL A 1 73  ? 34.16467 10.11166 2.96014  1.000 34.98117  ? 98   VAL A HA   1 
ATOM   1083 H  HB   . VAL A 1 73  ? 31.52843 10.84225 2.18068  1.000 40.48373  ? 98   VAL A HB   1 
ATOM   1084 H  HG11 . VAL A 1 73  ? 31.81867 12.81012 3.39978  1.000 41.80301  ? 98   VAL A HG11 1 
ATOM   1085 H  HG12 . VAL A 1 73  ? 31.94230 11.55822 4.36982  1.000 41.80301  ? 98   VAL A HG12 1 
ATOM   1086 H  HG13 . VAL A 1 73  ? 33.25009 12.31358 3.87725  1.000 41.80301  ? 98   VAL A HG13 1 
ATOM   1087 H  HG21 . VAL A 1 73  ? 33.82331 11.29500 0.94557  1.000 43.34775  ? 98   VAL A HG21 1 
ATOM   1088 H  HG22 . VAL A 1 73  ? 32.38618 11.81850 0.51651  1.000 43.34775  ? 98   VAL A HG22 1 
ATOM   1089 H  HG23 . VAL A 1 73  ? 33.29033 12.68873 1.49053  1.000 43.34775  ? 98   VAL A HG23 1 
ATOM   1090 N  N    . ARG A 1 74  ? 33.18241 9.42891  5.12788  1.000 35.31988  ? 99   ARG A N    1 
ATOM   1091 C  CA   . ARG A 1 74  ? 32.70298 8.82710  6.36545  1.000 32.42655  ? 99   ARG A CA   1 
ATOM   1092 C  C    . ARG A 1 74  ? 32.13571 9.97269  7.18729  1.000 32.19825  ? 99   ARG A C    1 
ATOM   1093 O  O    . ARG A 1 74  ? 32.82823 10.97679 7.40336  1.000 31.92959  ? 99   ARG A O    1 
ATOM   1094 C  CB   . ARG A 1 74  ? 33.85796 8.07447  7.02638  1.000 41.12072  ? 99   ARG A CB   1 
ATOM   1095 C  CG   . ARG A 1 74  ? 33.66154 7.55501  8.45079  1.000 48.55267  ? 99   ARG A CG   1 
ATOM   1096 C  CD   . ARG A 1 74  ? 34.93731 6.86518  9.00680  1.000 53.34674  ? 99   ARG A CD   1 
ATOM   1097 N  NE   . ARG A 1 74  ? 36.14397 7.27897  8.29345  1.000 63.62721  ? 99   ARG A NE   1 
ATOM   1098 C  CZ   . ARG A 1 74  ? 37.34834 7.39094  8.83921  1.000 65.18900  ? 99   ARG A CZ   1 
ATOM   1099 N  NH1  . ARG A 1 74  ? 37.55952 7.09476  10.11413 1.000 63.99889  ? 99   ARG A NH1  1 
ATOM   1100 N  NH2  . ARG A 1 74  ? 38.36738 7.80502  8.08368  1.000 65.85143  ? 99   ARG A NH2  1 
ATOM   1101 H  H    . ARG A 1 74  ? 33.82649 9.98796  5.23842  1.000 42.71370  ? 99   ARG A H    1 
ATOM   1102 H  HA   . ARG A 1 74  ? 31.98902 8.18081  6.24939  1.000 39.24171  ? 99   ARG A HA   1 
ATOM   1103 H  HB2  . ARG A 1 74  ? 34.05946 7.30201  6.47537  1.000 49.67470  ? 99   ARG A HB2  1 
ATOM   1104 H  HB3  . ARG A 1 74  ? 34.62181 8.67175  7.05243  1.000 49.67470  ? 99   ARG A HB3  1 
ATOM   1105 H  HG2  . ARG A 1 74  ? 33.44254 8.29885  9.03358  1.000 58.59305  ? 99   ARG A HG2  1 
ATOM   1106 H  HG3  . ARG A 1 74  ? 32.94085 6.90581  8.45639  1.000 58.59305  ? 99   ARG A HG3  1 
ATOM   1107 H  HD2  . ARG A 1 74  ? 35.04397 7.09923  9.94207  1.000 64.34593  ? 99   ARG A HD2  1 
ATOM   1108 H  HD3  . ARG A 1 74  ? 34.84588 5.90400  8.91368  1.000 64.34593  ? 99   ARG A HD3  1 
ATOM   1109 H  HE   . ARG A 1 74  ? 36.06771 7.46380  7.45702  1.000 76.68250  ? 99   ARG A HE   1 
ATOM   1110 H  HH11 . ARG A 1 74  ? 36.90841 6.82344  10.60611 1.000 77.12851  ? 99   ARG A HH11 1 
ATOM   1111 H  HH12 . ARG A 1 74  ? 38.34762 7.17394  10.44914 1.000 77.12851  ? 99   ARG A HH12 1 
ATOM   1112 H  HH21 . ARG A 1 74  ? 38.23872 7.99519  7.25489  1.000 79.35156  ? 99   ARG A HH21 1 
ATOM   1113 H  HH22 . ARG A 1 74  ? 39.15277 7.88172  8.42555  1.000 79.35156  ? 99   ARG A HH22 1 
ATOM   1114 N  N    . ALA A 1 75  ? 30.86486 9.85135  7.59716  1.000 27.15835  ? 100  ALA A N    1 
ATOM   1115 C  CA   . ALA A 1 75  ? 30.23244 10.92448 8.32785  1.000 26.20505  ? 100  ALA A CA   1 
ATOM   1116 C  C    . ALA A 1 75  ? 29.08436 10.46542 9.22617  1.000 28.09653  ? 100  ALA A C    1 
ATOM   1117 O  O    . ALA A 1 75  ? 28.36739 9.50674  8.92771  1.000 27.18473  ? 100  ALA A O    1 
ATOM   1118 C  CB   . ALA A 1 75  ? 29.67818 11.99841 7.37020  1.000 24.30453  ? 100  ALA A CB   1 
ATOM   1119 H  H    . ALA A 1 75  ? 30.36727 9.16345  7.46007  1.000 30.94079  ? 100  ALA A H    1 
ATOM   1120 H  HA   . ALA A 1 75  ? 30.91709 11.28057 8.91551  1.000 29.79684  ? 100  ALA A HA   1 
ATOM   1121 H  HB1  . ALA A 1 75  ? 30.40658 12.35071 6.83521  1.000 28.09072  ? 100  ALA A HB1  1 
ATOM   1122 H  HB2  . ALA A 1 75  ? 29.01051 11.59386 6.79448  1.000 28.09072  ? 100  ALA A HB2  1 
ATOM   1123 H  HB3  . ALA A 1 75  ? 29.27690 12.71049 7.89251  1.000 28.09072  ? 100  ALA A HB3  1 
ATOM   1124 N  N    . LYS A 1 76  ? 28.90979 11.18633 10.33086 1.000 28.98014  ? 101  LYS A N    1 
ATOM   1125 C  CA   . LYS A 1 76  ? 27.72869 11.11504 11.17771 1.000 28.10416  ? 101  LYS A CA   1 
ATOM   1126 C  C    . LYS A 1 76  ? 26.85204 12.31276 10.83311 1.000 27.24256  ? 101  LYS A C    1 
ATOM   1127 O  O    . LYS A 1 76  ? 27.32624 13.32418 10.29864 1.000 22.30848  ? 101  LYS A O    1 
ATOM   1128 C  CB   . LYS A 1 76  ? 28.07147 11.12208 12.68563 1.000 32.26186  ? 101  LYS A CB   1 
ATOM   1129 C  CG   . LYS A 1 76  ? 29.25980 10.24287 13.17744 1.000 34.56006  ? 101  LYS A CG   1 
ATOM   1130 C  CD   . LYS A 1 76  ? 29.73509 10.45663 14.66983 1.000 35.65863  ? 101  LYS A CD   1 
ATOM   1131 C  CE   . LYS A 1 76  ? 28.88648 9.81919  15.81694 1.000 44.87279  ? 101  LYS A CE   1 
ATOM   1132 N  NZ   . LYS A 1 76  ? 29.59000 9.81257  17.18531 1.000 51.91601  ? 101  LYS A NZ   1 
ATOM   1133 H  H    . LYS A 1 76  ? 29.49071 11.74974 10.62190 1.000 35.10602  ? 101  LYS A H    1 
ATOM   1134 H  HA   . LYS A 1 76  ? 27.25749 10.28152 11.02239 1.000 34.05484  ? 101  LYS A HA   1 
ATOM   1135 H  HB2  . LYS A 1 76  ? 28.28176 12.03559 12.93501 1.000 39.04407  ? 101  LYS A HB2  1 
ATOM   1136 H  HB3  . LYS A 1 76  ? 27.28575 10.81924 13.16711 1.000 39.04407  ? 101  LYS A HB3  1 
ATOM   1137 H  HG2  . LYS A 1 76  ? 28.99965 9.31206  13.09487 1.000 41.80192  ? 101  LYS A HG2  1 
ATOM   1138 H  HG3  . LYS A 1 76  ? 30.02437 10.42532 12.60907 1.000 41.80192  ? 101  LYS A HG3  1 
ATOM   1139 H  HD2  . LYS A 1 76  ? 30.62849 10.08755 14.75050 1.000 43.12021  ? 101  LYS A HD2  1 
ATOM   1140 H  HD3  . LYS A 1 76  ? 29.75406 11.41152 14.83934 1.000 43.12021  ? 101  LYS A HD3  1 
ATOM   1141 H  HE2  . LYS A 1 76  ? 28.06267 10.32243 15.91173 1.000 54.17720  ? 101  LYS A HE2  1 
ATOM   1142 H  HE3  . LYS A 1 76  ? 28.68806 8.89889  15.58331 1.000 54.17720  ? 101  LYS A HE3  1 
ATOM   1143 H  HZ1  . LYS A 1 76  ? 29.06648 9.42990  17.79489 1.000 62.62906  ? 101  LYS A HZ1  1 
ATOM   1144 H  HZ2  . LYS A 1 76  ? 30.35299 9.35735  17.13311 1.000 62.62906  ? 101  LYS A HZ2  1 
ATOM   1145 H  HZ3  . LYS A 1 76  ? 29.76808 10.64653 17.44006 1.000 62.62906  ? 101  LYS A HZ3  1 
ATOM   1146 N  N    . PHE A 1 77  ? 25.56538 12.19091 11.14659 1.000 25.75147  ? 102  PHE A N    1 
ATOM   1147 C  CA   . PHE A 1 77  ? 24.58474 13.21851 10.82485 1.000 22.91252  ? 102  PHE A CA   1 
ATOM   1148 C  C    . PHE A 1 77  ? 23.55056 13.24545 11.94545 1.000 26.10009  ? 102  PHE A C    1 
ATOM   1149 O  O    . PHE A 1 77  ? 23.28628 12.22399 12.59331 1.000 21.86188  ? 102  PHE A O    1 
ATOM   1150 C  CB   . PHE A 1 77  ? 23.93531 12.99552 9.44610  1.000 19.34979  ? 102  PHE A CB   1 
ATOM   1151 C  CG   . PHE A 1 77  ? 23.31168 11.63010 9.24627  1.000 23.56761  ? 102  PHE A CG   1 
ATOM   1152 C  CD1  . PHE A 1 77  ? 21.98770 11.40602 9.58379  1.000 19.98386  ? 102  PHE A CD1  1 
ATOM   1153 C  CD2  . PHE A 1 77  ? 24.04066 10.58536 8.70834  1.000 20.19674  ? 102  PHE A CD2  1 
ATOM   1154 C  CE1  . PHE A 1 77  ? 21.42369 10.14880 9.39389  1.000 21.94413  ? 102  PHE A CE1  1 
ATOM   1155 C  CE2  . PHE A 1 77  ? 23.46812 9.32820  8.52445  1.000 25.07902  ? 102  PHE A CE2  1 
ATOM   1156 C  CZ   . PHE A 1 77  ? 22.15784 9.12101  8.86099  1.000 25.91170  ? 102  PHE A CZ   1 
ATOM   1157 H  H    . PHE A 1 77  ? 25.23120 11.51044 11.55266 1.000 31.23161  ? 102  PHE A H    1 
ATOM   1158 H  HA   . PHE A 1 77  ? 25.00873 14.09004 10.78525 1.000 27.82486  ? 102  PHE A HA   1 
ATOM   1159 H  HB2  . PHE A 1 77  ? 23.23471 13.65559 9.32623  1.000 23.54959  ? 102  PHE A HB2  1 
ATOM   1160 H  HB3  . PHE A 1 77  ? 24.61619 13.10687 8.76426  1.000 23.54959  ? 102  PHE A HB3  1 
ATOM   1161 H  HD1  . PHE A 1 77  ? 21.47512 12.09660 9.93772  1.000 24.31048  ? 102  PHE A HD1  1 
ATOM   1162 H  HD2  . PHE A 1 77  ? 24.92757 10.72398 8.46530  1.000 24.56593  ? 102  PHE A HD2  1 
ATOM   1163 H  HE1  . PHE A 1 77  ? 20.53643 10.00348 9.63169  1.000 26.66280  ? 102  PHE A HE1  1 
ATOM   1164 H  HE2  . PHE A 1 77  ? 23.97513 8.63181  8.17392  1.000 30.42467  ? 102  PHE A HE2  1 
ATOM   1165 H  HZ   . PHE A 1 77  ? 21.76753 8.28728  8.72884  1.000 31.42389  ? 102  PHE A HZ   1 
ATOM   1166 N  N    . LYS A 1 78  ? 23.02935 14.44472 12.21402 1.000 21.10183  ? 103  LYS A N    1 
ATOM   1167 C  CA   . LYS A 1 78  ? 21.99129 14.68116 13.21180 1.000 18.65892  ? 103  LYS A CA   1 
ATOM   1168 C  C    . LYS A 1 78  ? 20.92921 15.54139 12.53945 1.000 21.93267  ? 103  LYS A C    1 
ATOM   1169 O  O    . LYS A 1 78  ? 21.25214 16.57734 11.95487 1.000 24.09233  ? 103  LYS A O    1 
ATOM   1170 C  CB   . LYS A 1 78  ? 22.60166 15.34332 14.45357 1.000 23.41734  ? 103  LYS A CB   1 
ATOM   1171 C  CG   . LYS A 1 78  ? 21.63901 16.01233 15.42221 1.000 31.11461  ? 103  LYS A CG   1 
ATOM   1172 C  CD   . LYS A 1 78  ? 22.36480 16.59789 16.63353 1.000 37.65318  ? 103  LYS A CD   1 
ATOM   1173 C  CE   . LYS A 1 78  ? 21.45579 17.49916 17.48588 1.000 48.24640  ? 103  LYS A CE   1 
ATOM   1174 N  NZ   . LYS A 1 78  ? 22.04062 17.83075 18.84179 1.000 44.69790  ? 103  LYS A NZ   1 
ATOM   1175 H  H    . LYS A 1 78  ? 23.27314 15.16526 11.81278 1.000 25.65204  ? 103  LYS A H    1 
ATOM   1176 H  HA   . LYS A 1 78  ? 21.56349 13.86522 13.51532 1.000 22.72055  ? 103  LYS A HA   1 
ATOM   1177 H  HB2  . LYS A 1 78  ? 23.07653 14.66111 14.95356 1.000 28.43065  ? 103  LYS A HB2  1 
ATOM   1178 H  HB3  . LYS A 1 78  ? 23.22130 16.02689 14.15412 1.000 28.43065  ? 103  LYS A HB3  1 
ATOM   1179 H  HG2  . LYS A 1 78  ? 21.17745 16.73402 14.96720 1.000 37.66738  ? 103  LYS A HG2  1 
ATOM   1180 H  HG3  . LYS A 1 78  ? 20.99830 15.35711 15.74015 1.000 37.66738  ? 103  LYS A HG3  1 
ATOM   1181 H  HD2  . LYS A 1 78  ? 22.68101 15.87293 17.19508 1.000 45.51366  ? 103  LYS A HD2  1 
ATOM   1182 H  HD3  . LYS A 1 78  ? 23.11467 17.13135 16.32691 1.000 45.51366  ? 103  LYS A HD3  1 
ATOM   1183 H  HE2  . LYS A 1 78  ? 21.30895 18.33355 17.01351 1.000 58.22553  ? 103  LYS A HE2  1 
ATOM   1184 H  HE3  . LYS A 1 78  ? 20.61025 17.04610 17.62972 1.000 58.22553  ? 103  LYS A HE3  1 
ATOM   1185 H  HZ1  . LYS A 1 78  ? 22.17388 17.08367 19.30677 1.000 53.96733  ? 103  LYS A HZ1  1 
ATOM   1186 H  HZ2  . LYS A 1 78  ? 22.81831 18.25212 18.74307 1.000 53.96733  ? 103  LYS A HZ2  1 
ATOM   1187 H  HZ3  . LYS A 1 78  ? 21.48254 18.35654 19.29367 1.000 53.96733  ? 103  LYS A HZ3  1 
ATOM   1188 N  N    . PHE A 1 79  ? 19.66784 15.09557 12.59776 1.000 20.17102  ? 104  PHE A N    1 
ATOM   1189 C  CA   . PHE A 1 79  ? 18.50702 15.82947 12.09869 1.000 21.71118  ? 104  PHE A CA   1 
ATOM   1190 C  C    . PHE A 1 79  ? 17.65597 16.27320 13.29820 1.000 20.78736  ? 104  PHE A C    1 
ATOM   1191 O  O    . PHE A 1 79  ? 17.47060 15.51710 14.25264 1.000 18.87995  ? 104  PHE A O    1 
ATOM   1192 C  CB   . PHE A 1 79  ? 17.62855 14.98718 11.11913 1.000 25.34617  ? 104  PHE A CB   1 
ATOM   1193 C  CG   . PHE A 1 79  ? 18.32661 14.55566 9.81192  1.000 22.59569  ? 104  PHE A CG   1 
ATOM   1194 C  CD1  . PHE A 1 79  ? 18.82039 15.48837 8.92083  1.000 29.92103  ? 104  PHE A CD1  1 
ATOM   1195 C  CD2  . PHE A 1 79  ? 18.41777 13.20625 9.46250  1.000 25.62554  ? 104  PHE A CD2  1 
ATOM   1196 C  CE1  . PHE A 1 79  ? 19.44849 15.08705 7.72396  1.000 35.88550  ? 104  PHE A CE1  1 
ATOM   1197 C  CE2  . PHE A 1 79  ? 19.04058 12.79068 8.28770  1.000 28.84984  ? 104  PHE A CE2  1 
ATOM   1198 C  CZ   . PHE A 1 79  ? 19.55945 13.72089 7.40950  1.000 26.69934  ? 104  PHE A CZ   1 
ATOM   1199 H  H    . PHE A 1 79  ? 19.45398 14.33540 12.93836 1.000 24.53507  ? 104  PHE A H    1 
ATOM   1200 H  HA   . PHE A 1 79  ? 18.81429 16.60406 11.60220 1.000 26.38326  ? 104  PHE A HA   1 
ATOM   1201 H  HB2  . PHE A 1 79  ? 17.34775 14.17971 11.57745 1.000 30.74524  ? 104  PHE A HB2  1 
ATOM   1202 H  HB3  . PHE A 1 79  ? 16.85323 15.51533 10.87248 1.000 30.74524  ? 104  PHE A HB3  1 
ATOM   1203 H  HD1  . PHE A 1 79  ? 18.73735 16.39448 9.11312  1.000 36.23508  ? 104  PHE A HD1  1 
ATOM   1204 H  HD2  . PHE A 1 79  ? 18.05221 12.56695 10.03043 1.000 31.08049  ? 104  PHE A HD2  1 
ATOM   1205 H  HE1  . PHE A 1 79  ? 19.78989 15.72677 7.14163  1.000 43.39245  ? 104  PHE A HE1  1 
ATOM   1206 H  HE2  . PHE A 1 79  ? 19.10703 11.88343 8.09438  1.000 34.94966  ? 104  PHE A HE2  1 
ATOM   1207 H  HZ   . PHE A 1 79  ? 19.97524 13.44874 6.62340  1.000 32.36905  ? 104  PHE A HZ   1 
ATOM   1208 N  N    . SER A 1 80  ? 17.14003 17.49515 13.25231 1.000 19.78938  ? 105  SER A N    1 
ATOM   1209 C  CA   . SER A 1 80  ? 16.26568 18.04447 14.27902 1.000 17.15204  ? 105  SER A CA   1 
ATOM   1210 C  C    . SER A 1 80  ? 15.34164 19.06676 13.61219 1.000 19.63334  ? 105  SER A C    1 
ATOM   1211 O  O    . SER A 1 80  ? 15.51479 19.42620 12.44968 1.000 19.49429  ? 105  SER A O    1 
ATOM   1212 C  CB   . SER A 1 80  ? 17.07576 18.66291 15.39222 1.000 27.33236  ? 105  SER A CB   1 
ATOM   1213 O  OG   . SER A 1 80  ? 17.86651 19.73135 14.89234 1.000 27.48781  ? 105  SER A OG   1 
ATOM   1214 H  H    . SER A 1 80  ? 17.28745 18.04826 12.61049 1.000 24.07711  ? 105  SER A H    1 
ATOM   1215 H  HA   . SER A 1 80  ? 15.71249 17.34759 14.66533 1.000 20.91229  ? 105  SER A HA   1 
ATOM   1216 H  HB2  . SER A 1 80  ? 16.47352 19.00416 16.07174 1.000 33.12867  ? 105  SER A HB2  1 
ATOM   1217 H  HB3  . SER A 1 80  ? 17.65844 17.98793 15.77404 1.000 33.12867  ? 105  SER A HB3  1 
ATOM   1218 H  HG   . SER A 1 80  ? 18.42643 19.43960 14.33830 1.000 33.31521  ? 105  SER A HG   1 
ATOM   1219 N  N    . ILE A 1 81  ? 14.34595 19.54353 14.35811 1.000 20.24035  ? 106  ILE A N    1 
ATOM   1220 C  CA   . ILE A 1 81  ? 13.28300 20.38783 13.81138 1.000 14.49291  ? 106  ILE A CA   1 
ATOM   1221 C  C    . ILE A 1 81  ? 13.18590 21.62201 14.68319 1.000 19.63634  ? 106  ILE A C    1 
ATOM   1222 O  O    . ILE A 1 81  ? 13.32842 21.52092 15.90405 1.000 26.09122  ? 106  ILE A O    1 
ATOM   1223 C  CB   . ILE A 1 81  ? 11.93836 19.63653 13.81262 1.000 15.57437  ? 106  ILE A CB   1 
ATOM   1224 C  CG1  . ILE A 1 81  ? 11.99443 18.37224 12.99454 1.000 21.46833  ? 106  ILE A CG1  1 
ATOM   1225 C  CG2  . ILE A 1 81  ? 10.84183 20.58505 13.35373 1.000 19.84470  ? 106  ILE A CG2  1 
ATOM   1226 C  CD1  . ILE A 1 81  ? 10.85806 17.41214 13.29450 1.000 27.40598  ? 106  ILE A CD1  1 
ATOM   1227 H  H    . ILE A 1 81  ? 14.26272 19.38876 15.19996 1.000 24.61827  ? 106  ILE A H    1 
ATOM   1228 H  HA   . ILE A 1 81  ? 13.49657 20.65435 12.90349 1.000 17.72133  ? 106  ILE A HA   1 
ATOM   1229 H  HB   . ILE A 1 81  ? 11.73945 19.34580 14.71640 1.000 19.01909  ? 106  ILE A HB   1 
ATOM   1230 H  HG12 . ILE A 1 81  ? 11.94753 18.60491 12.05403 1.000 26.09184  ? 106  ILE A HG12 1 
ATOM   1231 H  HG13 . ILE A 1 81  ? 12.82875 17.91425 13.18180 1.000 26.09184  ? 106  ILE A HG13 1 
ATOM   1232 H  HG21 . ILE A 1 81  ? 10.63204 21.19807 14.07560 1.000 24.14349  ? 106  ILE A HG21 1 
ATOM   1233 H  HG22 . ILE A 1 81  ? 11.15529 21.07959 12.58038 1.000 24.14349  ? 106  ILE A HG22 1 
ATOM   1234 H  HG23 . ILE A 1 81  ? 10.05504 20.06841 13.11933 1.000 24.14349  ? 106  ILE A HG23 1 
ATOM   1235 H  HD11 . ILE A 1 81  ? 10.86340 17.20253 14.24157 1.000 33.21702  ? 106  ILE A HD11 1 
ATOM   1236 H  HD12 . ILE A 1 81  ? 10.01768 17.83232 13.05345 1.000 33.21702  ? 106  ILE A HD12 1 
ATOM   1237 H  HD13 . ILE A 1 81  ? 10.98369 16.60219 12.77575 1.000 33.21702  ? 106  ILE A HD13 1 
ATOM   1238 N  N    . LEU A 1 82  ? 12.98409 22.77638 14.08196 1.000 16.63376  ? 107  LEU A N    1 
ATOM   1239 C  CA   . LEU A 1 82  ? 12.80826 24.00138 14.84814 1.000 21.06064  ? 107  LEU A CA   1 
ATOM   1240 C  C    . LEU A 1 82  ? 11.36177 24.12814 15.27990 1.000 23.95971  ? 107  LEU A C    1 
ATOM   1241 O  O    . LEU A 1 82  ? 10.46458 24.08957 14.43334 1.000 26.80058  ? 107  LEU A O    1 
ATOM   1242 C  CB   . LEU A 1 82  ? 13.19461 25.20461 14.00983 1.000 21.27768  ? 107  LEU A CB   1 
ATOM   1243 C  CG   . LEU A 1 82  ? 13.10150 26.56064 14.70732 1.000 30.47542  ? 107  LEU A CG   1 
ATOM   1244 C  CD1  . LEU A 1 82  ? 14.15378 26.66237 15.83322 1.000 24.28621  ? 107  LEU A CD1  1 
ATOM   1245 C  CD2  . LEU A 1 82  ? 13.22923 27.67839 13.71365 1.000 28.79270  ? 107  LEU A CD2  1 
ATOM   1246 H  H    . LEU A 1 82  ? 12.94383 22.88218 13.22944 1.000 19.82306  ? 107  LEU A H    1 
ATOM   1247 H  HA   . LEU A 1 82  ? 13.37438 23.97575 15.63538 1.000 25.60261  ? 107  LEU A HA   1 
ATOM   1248 H  HB2  . LEU A 1 82  ? 14.11422 25.09116 13.72287 1.000 25.86306  ? 107  LEU A HB2  1 
ATOM   1249 H  HB3  . LEU A 1 82  ? 12.60786 25.23709 13.23809 1.000 25.86306  ? 107  LEU A HB3  1 
ATOM   1250 H  HG   . LEU A 1 82  ? 12.22953 26.65134 15.12246 1.000 36.90035  ? 107  LEU A HG   1 
ATOM   1251 H  HD11 . LEU A 1 82  ? 15.03418 26.50455 15.45785 1.000 29.47330  ? 107  LEU A HD11 1 
ATOM   1252 H  HD12 . LEU A 1 82  ? 14.11457 27.54979 16.22290 1.000 29.47330  ? 107  LEU A HD12 1 
ATOM   1253 H  HD13 . LEU A 1 82  ? 13.95811 25.99517 16.50958 1.000 29.47330  ? 107  LEU A HD13 1 
ATOM   1254 H  HD21 . LEU A 1 82  ? 12.52019 27.59926 13.05646 1.000 34.88108  ? 107  LEU A HD21 1 
ATOM   1255 H  HD22 . LEU A 1 82  ? 13.15488 28.52563 14.18008 1.000 34.88108  ? 107  LEU A HD22 1 
ATOM   1256 H  HD23 . LEU A 1 82  ? 14.09324 27.61576 13.27723 1.000 34.88108  ? 107  LEU A HD23 1 
ATOM   1257 N  N    . ASN A 1 83  ? 11.12008 24.29148 16.59493 1.000 27.29126  ? 108  ASN A N    1 
ATOM   1258 C  CA   . ASN A 1 83  ? 9.75423  24.43603 17.07045 1.000 22.52304  ? 108  ASN A CA   1 
ATOM   1259 C  C    . ASN A 1 83  ? 9.36536  25.90462 17.18531 1.000 25.21086  ? 108  ASN A C    1 
ATOM   1260 O  O    . ASN A 1 83  ? 10.15341 26.82121 16.95274 1.000 22.25039  ? 108  ASN A O    1 
ATOM   1261 C  CB   . ASN A 1 83  ? 9.52918  23.66875 18.37706 1.000 25.69417  ? 108  ASN A CB   1 
ATOM   1262 C  CG   . ASN A 1 83  ? 10.01369 24.39143 19.61910 1.000 25.24369  ? 108  ASN A CG   1 
ATOM   1263 O  OD1  . ASN A 1 83  ? 10.49119 25.52811 19.56747 1.000 21.75597  ? 108  ASN A OD1  1 
ATOM   1264 N  ND2  . ASN A 1 83  ? 9.82653  23.75421 20.76479 1.000 22.80508  ? 108  ASN A ND2  1 
ATOM   1265 H  H    . ASN A 1 83  ? 11.72365 24.31962 17.20689 1.000 33.07936  ? 108  ASN A H    1 
ATOM   1266 H  HA   . ASN A 1 83  ? 9.16951  24.03715 16.40720 1.000 27.35749  ? 108  ASN A HA   1 
ATOM   1267 H  HB2  . ASN A 1 83  ? 8.57822  23.50954 18.48296 1.000 31.16285  ? 108  ASN A HB2  1 
ATOM   1268 H  HB3  . ASN A 1 83  ? 10.00331 22.82407 18.32589 1.000 31.16285  ? 108  ASN A HB3  1 
ATOM   1269 H  HD21 . ASN A 1 83  ? 9.45090  22.98060 20.77018 1.000 27.69594  ? 108  ASN A HD21 1 
ATOM   1270 H  HD22 . ASN A 1 83  ? 10.08063 24.11399 21.50343 1.000 27.69594  ? 108  ASN A HD22 1 
ATOM   1271 N  N    . ALA A 1 84  ? 8.11185  26.14815 17.52323 1.000 27.04648  ? 109  ALA A N    1 
ATOM   1272 C  CA   . ALA A 1 84  ? 7.64037  27.52457 17.54767 1.000 26.24527  ? 109  ALA A CA   1 
ATOM   1273 C  C    . ALA A 1 84  ? 8.19937  28.33828 18.70493 1.000 33.23296  ? 109  ALA A C    1 
ATOM   1274 O  O    . ALA A 1 84  ? 8.08999  29.56996 18.68564 1.000 29.86359  ? 109  ALA A O    1 
ATOM   1275 C  CB   . ALA A 1 84  ? 6.10594  27.53289 17.57745 1.000 33.40954  ? 109  ALA A CB   1 
ATOM   1276 H  H    . ALA A 1 84  ? 7.52896  25.55303 17.73695 1.000 32.78562  ? 109  ALA A H    1 
ATOM   1277 H  HA   . ALA A 1 84  ? 7.93035  27.96901 16.73571 1.000 31.82417  ? 109  ALA A HA   1 
ATOM   1278 H  HB1  . ALA A 1 84  ? 5.80339  27.09194 18.38673 1.000 40.42129  ? 109  ALA A HB1  1 
ATOM   1279 H  HB2  . ALA A 1 84  ? 5.79481  28.45155 17.56521 1.000 40.42129  ? 109  ALA A HB2  1 
ATOM   1280 H  HB3  . ALA A 1 84  ? 5.77241  27.06029 16.79879 1.000 40.42129  ? 109  ALA A HB3  1 
ATOM   1281 N  N    . LYS A 1 85  ? 8.80220  27.70714 19.70205 1.000 26.78878  ? 110  LYS A N    1 
ATOM   1282 C  CA   . LYS A 1 85  ? 9.44852  28.41965 20.81117 1.000 32.80306  ? 110  LYS A CA   1 
ATOM   1283 C  C    . LYS A 1 85  ? 10.90668 28.75594 20.50467 1.000 32.88605  ? 110  LYS A C    1 
ATOM   1284 O  O    . LYS A 1 85  ? 11.53166 29.53155 21.24374 1.000 26.38560  ? 110  LYS A O    1 
ATOM   1285 C  CB   . LYS A 1 85  ? 9.33305  27.59290 22.10443 1.000 41.63046  ? 110  LYS A CB   1 
ATOM   1286 C  CG   . LYS A 1 85  ? 7.92533  27.62817 22.74888 1.000 40.39892  ? 110  LYS A CG   1 
ATOM   1287 C  CD   . LYS A 1 85  ? 7.54260  26.26912 23.34372 1.000 45.76306  ? 110  LYS A CD   1 
ATOM   1288 C  CE   . LYS A 1 85  ? 6.29682  26.32659 24.24441 1.000 58.93327  ? 110  LYS A CE   1 
ATOM   1289 N  NZ   . LYS A 1 85  ? 5.64908  27.67397 24.35564 1.000 67.42433  ? 110  LYS A NZ   1 
ATOM   1290 H  H    . LYS A 1 85  ? 8.85506  26.85118 19.76642 1.000 32.47638  ? 110  LYS A H    1 
ATOM   1291 H  HA   . LYS A 1 85  ? 8.98965  29.25757 20.97920 1.000 39.69351  ? 110  LYS A HA   1 
ATOM   1292 H  HB2  . LYS A 1 85  ? 9.54214  26.66761 21.90190 1.000 50.28640  ? 110  LYS A HB2  1 
ATOM   1293 H  HB3  . LYS A 1 85  ? 9.96399  27.94115 22.75370 1.000 50.28640  ? 110  LYS A HB3  1 
ATOM   1294 H  HG2  . LYS A 1 85  ? 7.91511  28.28609 23.46158 1.000 48.80855  ? 110  LYS A HG2  1 
ATOM   1295 H  HG3  . LYS A 1 85  ? 7.26899  27.86049 22.07348 1.000 48.80855  ? 110  LYS A HG3  1 
ATOM   1296 H  HD2  . LYS A 1 85  ? 7.35755  25.65029 22.62005 1.000 55.24551  ? 110  LYS A HD2  1 
ATOM   1297 H  HD3  . LYS A 1 85  ? 8.28168  25.94138 23.87968 1.000 55.24551  ? 110  LYS A HD3  1 
ATOM   1298 H  HE2  . LYS A 1 85  ? 5.63291  25.71530 23.88879 1.000 71.04977  ? 110  LYS A HE2  1 
ATOM   1299 H  HE3  . LYS A 1 85  ? 6.55280  26.05427 25.13952 1.000 71.04977  ? 110  LYS A HE3  1 
ATOM   1300 H  HZ1  . LYS A 1 85  ? 4.93920  27.62724 24.89042 1.000 81.23904  ? 110  LYS A HZ1  1 
ATOM   1301 H  HZ2  . LYS A 1 85  ? 6.22599  28.26221 24.69217 1.000 81.23904  ? 110  LYS A HZ2  1 
ATOM   1302 H  HZ3  . LYS A 1 85  ? 5.38749  27.95323 23.55210 1.000 81.23904  ? 110  LYS A HZ3  1 
ATOM   1303 N  N    . GLY A 1 86  ? 11.44456 28.28960 19.39000 1.000 23.50956  ? 111  GLY A N    1 
ATOM   1304 C  CA   . GLY A 1 86  ? 12.82287 28.60146 19.05620 1.000 27.44315  ? 111  GLY A CA   1 
ATOM   1305 C  C    . GLY A 1 86  ? 13.80947 27.53991 19.47244 1.000 25.11783  ? 111  GLY A C    1 
ATOM   1306 O  O    . GLY A 1 86  ? 14.97423 27.84539 19.61319 1.000 29.56432  ? 111  GLY A O    1 
ATOM   1307 H  H    . GLY A 1 86  ? 11.03611 27.79560 18.81666 1.000 28.54132  ? 111  GLY A H    1 
ATOM   1308 H  HA2  . GLY A 1 86  ? 12.89474 28.71746 18.09585 1.000 33.26163  ? 111  GLY A HA2  1 
ATOM   1309 H  HA3  . GLY A 1 86  ? 13.07202 29.43043 19.49395 1.000 33.26163  ? 111  GLY A HA3  1 
ATOM   1310 N  N    . GLU A 1 87  ? 13.37558 26.30387 19.64150 1.000 22.19674  ? 112  GLU A N    1 
ATOM   1311 C  CA   . GLU A 1 87  ? 14.21448 25.23865 20.17024 1.000 26.59871  ? 112  GLU A CA   1 
ATOM   1312 C  C    . GLU A 1 87  ? 14.34971 24.10040 19.16868 1.000 26.44428  ? 112  GLU A C    1 
ATOM   1313 O  O    . GLU A 1 87  ? 13.38902 23.74633 18.49030 1.000 25.67862  ? 112  GLU A O    1 
ATOM   1314 C  CB   . GLU A 1 87  ? 13.63049 24.67926 21.46667 1.000 26.71172  ? 112  GLU A CB   1 
ATOM   1315 C  CG   . GLU A 1 87  ? 14.23306 25.25928 22.73432 1.000 37.12568  ? 112  GLU A CG   1 
ATOM   1316 C  CD   . GLU A 1 87  ? 14.18963 24.27559 23.91391 1.000 40.87490  ? 112  GLU A CD   1 
ATOM   1317 O  OE1  . GLU A 1 87  ? 13.32630 23.36601 23.94032 1.000 34.84393  ? 112  GLU A OE1  1 
ATOM   1318 O  OE2  . GLU A 1 87  ? 15.04334 24.42291 24.80051 1.000 35.84871  ? 112  GLU A OE2  1 
ATOM   1319 H  H    . GLU A 1 87  ? 12.57650 26.04827 19.45242 1.000 26.81325  ? 112  GLU A H    1 
ATOM   1320 H  HA   . GLU A 1 87  ? 15.09876 25.60087 20.33685 1.000 32.24830  ? 112  GLU A HA   1 
ATOM   1321 H  HB2  . GLU A 1 87  ? 12.67900 24.86719 21.48263 1.000 32.38391  ? 112  GLU A HB2  1 
ATOM   1322 H  HB3  . GLU A 1 87  ? 13.77971 23.72096 21.48388 1.000 32.38391  ? 112  GLU A HB3  1 
ATOM   1323 H  HG2  . GLU A 1 87  ? 15.16091 25.48792 22.56785 1.000 44.88066  ? 112  GLU A HG2  1 
ATOM   1324 H  HG3  . GLU A 1 87  ? 13.73590 26.05304 22.98666 1.000 44.88066  ? 112  GLU A HG3  1 
ATOM   1325 N  N    . GLU A 1 88  ? 15.55144 23.52928 19.08046 1.000 26.73731  ? 113  GLU A N    1 
ATOM   1326 C  CA   . GLU A 1 88  ? 15.73905 22.29321 18.33230 1.000 23.11755  ? 113  GLU A CA   1 
ATOM   1327 C  C    . GLU A 1 88  ? 15.03309 21.16373 19.05137 1.000 25.94582  ? 113  GLU A C    1 
ATOM   1328 O  O    . GLU A 1 88  ? 15.21653 20.97680 20.26122 1.000 26.91296  ? 113  GLU A O    1 
ATOM   1329 C  CB   . GLU A 1 88  ? 17.21545 21.97284 18.19093 1.000 33.40472  ? 113  GLU A CB   1 
ATOM   1330 C  CG   . GLU A 1 88  ? 17.91690 22.85438 17.24833 1.000 33.07369  ? 113  GLU A CG   1 
ATOM   1331 C  CD   . GLU A 1 88  ? 19.29168 22.34205 16.93221 1.000 40.16685  ? 113  GLU A CD   1 
ATOM   1332 O  OE1  . GLU A 1 88  ? 19.58618 21.18195 17.32264 1.000 48.44414  ? 113  GLU A OE1  1 
ATOM   1333 O  OE2  . GLU A 1 88  ? 20.08621 23.10170 16.33351 1.000 41.46340  ? 113  GLU A OE2  1 
ATOM   1334 H  H    . GLU A 1 88  ? 16.26775 23.83743 19.44315 1.000 32.41461  ? 113  GLU A H    1 
ATOM   1335 H  HA   . GLU A 1 88  ? 15.36831 22.39109 17.44131 1.000 27.88754  ? 113  GLU A HA   1 
ATOM   1336 H  HB2  . GLU A 1 88  ? 17.64040 22.06600 19.05790 1.000 40.41551  ? 113  GLU A HB2  1 
ATOM   1337 H  HB3  . GLU A 1 88  ? 17.30888 21.06159 17.87187 1.000 40.41551  ? 113  GLU A HB3  1 
ATOM   1338 H  HG2  . GLU A 1 88  ? 17.41280 22.90530 16.42117 1.000 40.01827  ? 113  GLU A HG2  1 
ATOM   1339 H  HG3  . GLU A 1 88  ? 18.00316 23.73793 17.63920 1.000 40.01827  ? 113  GLU A HG3  1 
ATOM   1340 N  N    . THR A 1 89  ? 14.21705 20.42898 18.31022 1.000 18.65976  ? 114  THR A N    1 
ATOM   1341 C  CA   . THR A 1 89  ? 13.29571 19.45820 18.85900 1.000 21.21639  ? 114  THR A CA   1 
ATOM   1342 C  C    . THR A 1 89  ? 13.37655 18.17634 18.06143 1.000 24.58833  ? 114  THR A C    1 
ATOM   1343 O  O    . THR A 1 89  ? 13.58188 18.21443 16.84237 1.000 22.55434  ? 114  THR A O    1 
ATOM   1344 C  CB   . THR A 1 89  ? 11.84592 20.00065 18.81755 1.000 25.41765  ? 114  THR A CB   1 
ATOM   1345 O  OG1  . THR A 1 89  ? 11.82516 21.29862 19.41491 1.000 30.09209  ? 114  THR A OG1  1 
ATOM   1346 C  CG2  . THR A 1 89  ? 10.92002 19.09298 19.59056 1.000 32.43455  ? 114  THR A CG2  1 
ATOM   1347 H  H    . THR A 1 89  ? 14.18022 20.47982 17.45252 1.000 21.71704  ? 114  THR A H    1 
ATOM   1348 H  HA   . THR A 1 89  ? 13.53433 19.26060 19.77819 1.000 25.78952  ? 114  THR A HA   1 
ATOM   1349 H  HB   . THR A 1 89  ? 11.53598 20.04636 17.89954 1.000 30.83103  ? 114  THR A HB   1 
ATOM   1350 H  HG1  . THR A 1 89  ? 12.30924 21.82530 18.97461 1.000 36.44036  ? 114  THR A HG1  1 
ATOM   1351 H  HG21 . THR A 1 89  ? 10.48849 18.46777 18.98741 1.000 39.25131  ? 114  THR A HG21 1 
ATOM   1352 H  HG22 . THR A 1 89  ? 11.42190 18.59460 20.25436 1.000 39.25131  ? 114  THR A HG22 1 
ATOM   1353 H  HG23 . THR A 1 89  ? 10.23921 19.61813 20.03957 1.000 39.25131  ? 114  THR A HG23 1 
ATOM   1354 N  N    . LYS A 1 90  ? 13.24889 17.05599 18.77456 1.000 21.34192  ? 115  LYS A N    1 
ATOM   1355 C  CA   . LYS A 1 90  ? 13.14698 15.71038 18.19767 1.000 20.70864  ? 115  LYS A CA   1 
ATOM   1356 C  C    . LYS A 1 90  ? 14.42843 15.28440 17.48072 1.000 27.48484  ? 115  LYS A C    1 
ATOM   1357 O  O    . LYS A 1 90  ? 14.39994 14.52437 16.51135 1.000 21.23075  ? 115  LYS A O    1 
ATOM   1358 C  CB   . LYS A 1 90  ? 11.93086 15.62257 17.26956 1.000 22.30094  ? 115  LYS A CB   1 
ATOM   1359 C  CG   . LYS A 1 90  ? 10.60939 15.66267 18.03971 1.000 25.34329  ? 115  LYS A CG   1 
ATOM   1360 C  CD   . LYS A 1 90  ? 10.27417 14.32182 18.66342 1.000 23.27467  ? 115  LYS A CD   1 
ATOM   1361 C  CE   . LYS A 1 90  ? 9.32719  14.42298 19.87464 1.000 27.83705  ? 115  LYS A CE   1 
ATOM   1362 N  NZ   . LYS A 1 90  ? 10.17928 14.43836 21.12391 1.000 34.66598  ? 115  LYS A NZ   1 
ATOM   1363 H  H    . LYS A 1 90  ? 13.21723 17.04681 19.63393 1.000 25.94014  ? 115  LYS A H    1 
ATOM   1364 H  HA   . LYS A 1 90  ? 13.02971 15.07346 18.91980 1.000 25.18021  ? 115  LYS A HA   1 
ATOM   1365 H  HB2  . LYS A 1 90  ? 11.94563 16.37291 16.65502 1.000 27.09097  ? 115  LYS A HB2  1 
ATOM   1366 H  HB3  . LYS A 1 90  ? 11.96790 14.78851 16.77573 1.000 27.09097  ? 115  LYS A HB3  1 
ATOM   1367 H  HG2  . LYS A 1 90  ? 10.67385 16.31951 18.75056 1.000 30.74180  ? 115  LYS A HG2  1 
ATOM   1368 H  HG3  . LYS A 1 90  ? 9.89243  15.90131 17.43151 1.000 30.74180  ? 115  LYS A HG3  1 
ATOM   1369 H  HD2  . LYS A 1 90  ? 9.84262  13.76536 17.99632 1.000 28.25945  ? 115  LYS A HD2  1 
ATOM   1370 H  HD3  . LYS A 1 90  ? 11.09542 13.90244 18.96435 1.000 28.25945  ? 115  LYS A HD3  1 
ATOM   1371 H  HE2  . LYS A 1 90  ? 8.81011  15.24239 19.82878 1.000 33.73431  ? 115  LYS A HE2  1 
ATOM   1372 H  HE3  . LYS A 1 90  ? 8.73297  13.65675 19.90091 1.000 33.73431  ? 115  LYS A HE3  1 
ATOM   1373 H  HZ1  . LYS A 1 90  ? 9.65988  14.44148 21.84663 1.000 41.92902  ? 115  LYS A HZ1  1 
ATOM   1374 H  HZ2  . LYS A 1 90  ? 10.70038 13.71720 21.14584 1.000 41.92902  ? 115  LYS A HZ2  1 
ATOM   1375 H  HZ3  . LYS A 1 90  ? 10.69212 15.16568 21.13365 1.000 41.92902  ? 115  LYS A HZ3  1 
ATOM   1376 N  N    . ALA A 1 91  ? 15.57357 15.67393 18.03938 1.000 24.11558  ? 116  ALA A N    1 
ATOM   1377 C  CA   . ALA A 1 91  ? 16.83086 15.36805 17.40358 1.000 26.09243  ? 116  ALA A CA   1 
ATOM   1378 C  C    . ALA A 1 91  ? 17.05778 13.87431 17.41123 1.000 28.10333  ? 116  ALA A C    1 
ATOM   1379 O  O    . ALA A 1 91  ? 16.83554 13.19194 18.42714 1.000 28.68368  ? 116  ALA A O    1 
ATOM   1380 C  CB   . ALA A 1 91  ? 17.98070 16.07224 18.12189 1.000 28.75688  ? 116  ALA A CB   1 
ATOM   1381 H  H    . ALA A 1 91  ? 15.63879 16.11077 18.77729 1.000 29.26854  ? 116  ALA A H    1 
ATOM   1382 H  HA   . ALA A 1 91  ? 16.81669 15.68093 16.48553 1.000 29.66170  ? 116  ALA A HA   1 
ATOM   1383 H  HB1  . ALA A 1 91  ? 18.82009 15.79184 17.72478 1.000 32.85903  ? 116  ALA A HB1  1 
ATOM   1384 H  HB2  . ALA A 1 91  ? 17.87318 17.03141 18.02533 1.000 32.85903  ? 116  ALA A HB2  1 
ATOM   1385 H  HB3  . ALA A 1 91  ? 17.96187 15.83015 19.06101 1.000 32.85903  ? 116  ALA A HB3  1 
ATOM   1386 N  N    . MET A 1 92  ? 17.55372 13.37900 16.27760 1.000 24.99224  ? 117  MET A N    1 
ATOM   1387 C  CA   . MET A 1 92  ? 18.08314 12.02670 16.18218 1.000 30.02545  ? 117  MET A CA   1 
ATOM   1388 C  C    . MET A 1 92  ? 19.38854 12.05203 15.40020 1.000 23.29791  ? 117  MET A C    1 
ATOM   1389 O  O    . MET A 1 92  ? 19.51742 12.71850 14.36272 1.000 26.31394  ? 117  MET A O    1 
ATOM   1390 C  CB   . MET A 1 92  ? 17.10034 11.05474 15.53016 1.000 23.44503  ? 117  MET A CB   1 
ATOM   1391 C  CG   . MET A 1 92  ? 15.72113 11.10943 16.03651 1.000 24.43008  ? 117  MET A CG   1 
ATOM   1392 S  SD   . MET A 1 92  ? 15.07473 9.40656  15.81373 1.000 27.11154  ? 117  MET A SD   1 
ATOM   1393 C  CE   . MET A 1 92  ? 14.85233 9.49349  14.03949 1.000 23.50550  ? 117  MET A CE   1 
ATOM   1394 H  H    . MET A 1 92  ? 17.59358 13.81759 15.53893 1.000 28.34146  ? 117  MET A H    1 
ATOM   1395 H  HA   . MET A 1 92  ? 18.25261 11.69902 17.07929 1.000 36.36039  ? 117  MET A HA   1 
ATOM   1396 H  HB2  . MET A 1 92  ? 17.06631 11.24768 14.58015 1.000 28.02084  ? 117  MET A HB2  1 
ATOM   1397 H  HB3  . MET A 1 92  ? 17.42441 10.15185 15.67392 1.000 28.02084  ? 117  MET A HB3  1 
ATOM   1398 H  HG2  . MET A 1 92  ? 15.70636 11.35113 16.97579 1.000 28.10051  ? 117  MET A HG2  1 
ATOM   1399 H  HG3  . MET A 1 92  ? 15.18865 11.73759 15.52388 1.000 28.10051  ? 117  MET A HG3  1 
ATOM   1400 H  HE1  . MET A 1 92  ? 14.45477 8.66457  13.73006 1.000 28.53645  ? 117  MET A HE1  1 
ATOM   1401 H  HE2  . MET A 1 92  ? 14.26780 10.23888 13.83063 1.000 28.53645  ? 117  MET A HE2  1 
ATOM   1402 H  HE3  . MET A 1 92  ? 15.71672 9.62302  13.61883 1.000 28.53645  ? 117  MET A HE3  1 
ATOM   1403 N  N    . GLU A 1 93  ? 20.37958 11.32343 15.90313 1.000 29.35198  ? 118  GLU A N    1 
ATOM   1404 C  CA   . GLU A 1 93  ? 21.69724 11.25941 15.28219 1.000 25.87003  ? 118  GLU A CA   1 
ATOM   1405 C  C    . GLU A 1 93  ? 22.05313 9.80718  15.01093 1.000 27.18864  ? 118  GLU A C    1 
ATOM   1406 O  O    . GLU A 1 93  ? 21.58882 8.89922  15.71124 1.000 30.77922  ? 118  GLU A O    1 
ATOM   1407 C  CB   . GLU A 1 93  ? 22.77542 11.91948 16.15299 1.000 28.34885  ? 118  GLU A CB   1 
ATOM   1408 C  CG   . GLU A 1 93  ? 22.98134 11.34192 17.52564 1.000 42.03287  ? 118  GLU A CG   1 
ATOM   1409 C  CD   . GLU A 1 93  ? 23.92253 12.19392 18.35922 1.000 46.36480  ? 118  GLU A CD   1 
ATOM   1410 O  OE1  . GLU A 1 93  ? 24.74282 12.93815 17.75003 1.000 38.17087  ? 118  GLU A OE1  1 
ATOM   1411 O  OE2  . GLU A 1 93  ? 23.79449 12.15585 19.60722 1.000 47.47865  ? 118  GLU A OE2  1 
ATOM   1412 H  H    . GLU A 1 93  ? 20.31112 10.84865 16.61692 1.000 35.55223  ? 118  GLU A H    1 
ATOM   1413 H  HA   . GLU A 1 93  ? 21.68259 11.73570 14.43730 1.000 31.37389  ? 118  GLU A HA   1 
ATOM   1414 H  HB2  . GLU A 1 93  ? 23.62279 11.85002 15.68605 1.000 34.34847  ? 118  GLU A HB2  1 
ATOM   1415 H  HB3  . GLU A 1 93  ? 22.53697 12.85232 16.27068 1.000 34.34847  ? 118  GLU A HB3  1 
ATOM   1416 H  HG2  . GLU A 1 93  ? 22.12781 11.29406 17.98400 1.000 50.76929  ? 118  GLU A HG2  1 
ATOM   1417 H  HG3  . GLU A 1 93  ? 23.36492 10.45462 17.44519 1.000 50.76929  ? 118  GLU A HG3  1 
ATOM   1418 N  N    . SER A 1 94  ? 22.83776 9.60705  13.96172 1.000 29.60425  ? 119  SER A N    1 
ATOM   1419 C  CA   . SER A 1 94  ? 23.54750 8.35456  13.77410 1.000 28.85094  ? 119  SER A CA   1 
ATOM   1420 C  C    . SER A 1 94  ? 24.46037 8.12345  14.97032 1.000 28.96231  ? 119  SER A C    1 
ATOM   1421 O  O    . SER A 1 94  ? 25.14843 9.03894  15.45402 1.000 33.29996  ? 119  SER A O    1 
ATOM   1422 C  CB   . SER A 1 94  ? 24.32001 8.39949  12.45652 1.000 33.61337  ? 119  SER A CB   1 
ATOM   1423 O  OG   . SER A 1 94  ? 25.27899 9.47872  12.40399 1.000 21.12393  ? 119  SER A OG   1 
ATOM   1424 H  H    . SER A 1 94  ? 22.97656 10.18503 13.34021 1.000 35.85495  ? 119  SER A H    1 
ATOM   1425 H  HA   . SER A 1 94  ? 22.93613 7.60375  13.71563 1.000 34.95097  ? 119  SER A HA   1 
ATOM   1426 H  HB2  . SER A 1 94  ? 24.79503 7.56053  12.34977 1.000 40.66589  ? 119  SER A HB2  1 
ATOM   1427 H  HB3  . SER A 1 94  ? 23.68574 8.51615  11.73196 1.000 40.66589  ? 119  SER A HB3  1 
ATOM   1428 H  HG   . SER A 1 94  ? 25.94860 9.29124  12.87524 1.000 25.67856  ? 119  SER A HG   1 
ATOM   1429 N  N    . GLN A 1 95  ? 24.39592 6.91666  15.52493 1.000 35.86042  ? 120  GLN A N    1 
ATOM   1430 C  CA   . GLN A 1 95  ? 25.25400 6.63697  16.66705 1.000 26.40474  ? 120  GLN A CA   1 
ATOM   1431 C  C    . GLN A 1 95  ? 26.71237 6.56832  16.25395 1.000 36.52253  ? 120  GLN A C    1 
ATOM   1432 O  O    . GLN A 1 95  ? 27.60459 6.55836  17.12040 1.000 35.29849  ? 120  GLN A O    1 
ATOM   1433 C  CB   . GLN A 1 95  ? 24.83670 5.32936  17.33231 1.000 38.64082  ? 120  GLN A CB   1 
ATOM   1434 H  H    . GLN A 1 95  ? 23.88635 6.27284  15.26912 1.000 43.36235  ? 120  GLN A H    1 
ATOM   1435 H  HA   . GLN A 1 95  ? 25.15153 7.33743  17.33019 1.000 31.56061  ? 120  GLN A HA   1 
ATOM   1436 N  N    . ARG A 1 96  ? 26.96103 6.49495  14.95852 1.000 33.24728  ? 121  ARG A N    1 
ATOM   1437 C  CA   . ARG A 1 96  ? 28.29496 6.26366  14.41934 1.000 32.45511  ? 121  ARG A CA   1 
ATOM   1438 C  C    . ARG A 1 96  ? 28.29205 6.77206  12.99736 1.000 31.03203  ? 121  ARG A C    1 
ATOM   1439 O  O    . ARG A 1 96  ? 27.25215 7.15993  12.46968 1.000 32.24581  ? 121  ARG A O    1 
ATOM   1440 C  CB   . ARG A 1 96  ? 28.66324 4.78364  14.48126 1.000 34.91532  ? 121  ARG A CB   1 
ATOM   1441 C  CG   . ARG A 1 96  ? 27.54090 3.82246  13.97987 1.000 35.32641  ? 121  ARG A CG   1 
ATOM   1442 C  CD   . ARG A 1 96  ? 27.47295 3.69585  12.50717 1.000 32.00480  ? 121  ARG A CD   1 
ATOM   1443 N  NE   . ARG A 1 96  ? 26.66597 2.55803  12.06615 1.000 35.22380  ? 121  ARG A NE   1 
ATOM   1444 C  CZ   . ARG A 1 96  ? 26.78947 1.98019  10.87529 1.000 34.91575  ? 121  ARG A CZ   1 
ATOM   1445 N  NH1  . ARG A 1 96  ? 27.62653 2.44993  9.95884  1.000 34.36398  ? 121  ARG A NH1  1 
ATOM   1446 N  NH2  . ARG A 1 96  ? 26.06747 0.89618  10.60233 1.000 33.01681  ? 121  ARG A NH2  1 
ATOM   1447 H  H    . ARG A 1 96  ? 26.35834 6.57790  14.35067 1.000 40.22658  ? 121  ARG A H    1 
ATOM   1448 H  HA   . ARG A 1 96  ? 28.94987 6.75897  14.93573 1.000 39.27598  ? 121  ARG A HA   1 
ATOM   1449 H  HB2  . ARG A 1 96  ? 29.44602 4.63567  13.92784 1.000 42.22823  ? 121  ARG A HB2  1 
ATOM   1450 H  HB3  . ARG A 1 96  ? 28.85946 4.55140  15.40238 1.000 42.22823  ? 121  ARG A HB3  1 
ATOM   1451 H  HG2  . ARG A 1 96  ? 27.70165 2.93806  14.34443 1.000 42.72154  ? 121  ARG A HG2  1 
ATOM   1452 H  HG3  . ARG A 1 96  ? 26.68362 4.15695  14.28661 1.000 42.72154  ? 121  ARG A HG3  1 
ATOM   1453 H  HD2  . ARG A 1 96  ? 27.07820 4.50201  12.13951 1.000 38.73560  ? 121  ARG A HD2  1 
ATOM   1454 H  HD3  . ARG A 1 96  ? 28.37070 3.57763  12.15935 1.000 38.73560  ? 121  ARG A HD3  1 
ATOM   1455 H  HE   . ARG A 1 96  ? 26.07723 2.24464  12.60907 1.000 42.59840  ? 121  ARG A HE   1 
ATOM   1456 H  HH11 . ARG A 1 96  ? 28.10507 3.14394  10.12897 1.000 41.56662  ? 121  ARG A HH11 1 
ATOM   1457 H  HH12 . ARG A 1 96  ? 27.69043 2.06031  9.19483  1.000 41.56662  ? 121  ARG A HH12 1 
ATOM   1458 H  HH21 . ARG A 1 96  ? 25.52937 0.57799  11.19293 1.000 39.95001  ? 121  ARG A HH21 1 
ATOM   1459 H  HH22 . ARG A 1 96  ? 26.13897 0.51381  9.83534  1.000 39.95001  ? 121  ARG A HH22 1 
ATOM   1460 N  N    . ALA A 1 97  ? 29.46837 6.73154  12.36892 1.000 34.23969  ? 122  ALA A N    1 
ATOM   1461 C  CA   . ALA A 1 97  ? 29.65642 7.25896  11.03836 1.000 30.94866  ? 122  ALA A CA   1 
ATOM   1462 C  C    . ALA A 1 97  ? 29.16096 6.25917  10.00711 1.000 25.58297  ? 122  ALA A C    1 
ATOM   1463 O  O    . ALA A 1 97  ? 29.26117 5.04377  10.19909 1.000 28.72497  ? 122  ALA A O    1 
ATOM   1464 C  CB   . ALA A 1 97  ? 31.12802 7.57645  10.80497 1.000 35.84973  ? 122  ALA A CB   1 
ATOM   1465 H  H    . ALA A 1 97  ? 30.18321 6.39414  12.70768 1.000 41.41747  ? 122  ALA A H    1 
ATOM   1466 H  HA   . ALA A 1 97  ? 29.15137 8.08019  10.93157 1.000 37.46824  ? 122  ALA A HA   1 
ATOM   1467 H  HB1  . ALA A 1 97  ? 31.22885 7.98039  9.92885  1.000 43.34952  ? 122  ALA A HB1  1 
ATOM   1468 H  HB2  . ALA A 1 97  ? 31.43065 8.19275  11.49016 1.000 43.34952  ? 122  ALA A HB2  1 
ATOM   1469 H  HB3  . ALA A 1 97  ? 31.63972 6.75367  10.85074 1.000 43.34952  ? 122  ALA A HB3  1 
ATOM   1470 N  N    . TYR A 1 98  ? 28.57166 6.77696  8.94507  1.000 25.60479  ? 123  TYR A N    1 
ATOM   1471 C  CA   . TYR A 1 98  ? 28.12812 5.98415  7.79986  1.000 26.13730  ? 123  TYR A CA   1 
ATOM   1472 C  C    . TYR A 1 98  ? 29.00740 6.30550  6.59167  1.000 24.31527  ? 123  TYR A C    1 
ATOM   1473 O  O    . TYR A 1 98  ? 29.61918 7.36697  6.50391  1.000 26.52866  ? 123  TYR A O    1 
ATOM   1474 C  CB   . TYR A 1 98  ? 26.62604 6.22977  7.49865  1.000 25.56023  ? 123  TYR A CB   1 
ATOM   1475 C  CG   . TYR A 1 98  ? 25.71907 5.46471  8.45536  1.000 22.46259  ? 123  TYR A CG   1 
ATOM   1476 C  CD1  . TYR A 1 98  ? 25.55040 5.89110  9.74331  1.000 21.82352  ? 123  TYR A CD1  1 
ATOM   1477 C  CD2  . TYR A 1 98  ? 25.07071 4.31225  8.06962  1.000 25.83497  ? 123  TYR A CD2  1 
ATOM   1478 C  CE1  . TYR A 1 98  ? 24.75818 5.18458  10.62560 1.000 29.67317  ? 123  TYR A CE1  1 
ATOM   1479 C  CE2  . TYR A 1 98  ? 24.26713 3.60025  8.93302  1.000 22.60040  ? 123  TYR A CE2  1 
ATOM   1480 C  CZ   . TYR A 1 98  ? 24.11557 4.03439  10.21640 1.000 28.62101  ? 123  TYR A CZ   1 
ATOM   1481 O  OH   . TYR A 1 98  ? 23.31831 3.32396  11.10614 1.000 27.61320  ? 123  TYR A OH   1 
ATOM   1482 H  H    . TYR A 1 98  ? 28.40895 7.61668  8.85564  1.000 31.05559  ? 123  TYR A H    1 
ATOM   1483 H  HA   . TYR A 1 98  ? 28.22045 5.03684  7.98691  1.000 31.69460  ? 123  TYR A HA   1 
ATOM   1484 H  HB2  . TYR A 1 98  ? 26.43351 7.17613  7.58940  1.000 31.00213  ? 123  TYR A HB2  1 
ATOM   1485 H  HB3  . TYR A 1 98  ? 26.43021 5.93655  6.59500  1.000 31.00213  ? 123  TYR A HB3  1 
ATOM   1486 H  HD1  . TYR A 1 98  ? 25.97514 6.66761  10.02882 1.000 26.51806  ? 123  TYR A HD1  1 
ATOM   1487 H  HD2  . TYR A 1 98  ? 25.17884 4.00495  7.19855  1.000 31.33181  ? 123  TYR A HD2  1 
ATOM   1488 H  HE1  . TYR A 1 98  ? 24.65714 5.48525  11.49983 1.000 35.93765  ? 123  TYR A HE1  1 
ATOM   1489 H  HE2  . TYR A 1 98  ? 23.83231 2.83096  8.64315  1.000 27.45032  ? 123  TYR A HE2  1 
ATOM   1490 H  HH   . TYR A 1 98  ? 22.92623 2.69896  10.70458 1.000 33.46569  ? 123  TYR A HH   1 
ATOM   1491 N  N    . ARG A 1 99  ? 29.07606 5.34665  5.66256  1.000 23.24017  ? 124  ARG A N    1 
ATOM   1492 C  CA   . ARG A 1 99  ? 29.92120 5.44180  4.47652  1.000 24.97502  ? 124  ARG A CA   1 
ATOM   1493 C  C    . ARG A 1 99  ? 29.10258 5.97401  3.31237  1.000 26.25046  ? 124  ARG A C    1 
ATOM   1494 O  O    . ARG A 1 99  ? 28.16382 5.31123  2.84976  1.000 27.35533  ? 124  ARG A O    1 
ATOM   1495 C  CB   . ARG A 1 99  ? 30.50565 4.06768  4.14300  1.000 29.92048  ? 124  ARG A CB   1 
ATOM   1496 C  CG   . ARG A 1 99  ? 31.30167 3.97259  2.83338  1.000 33.96002  ? 124  ARG A CG   1 
ATOM   1497 C  CD   . ARG A 1 99  ? 31.63431 2.50560  2.51805  1.000 34.23215  ? 124  ARG A CD   1 
ATOM   1498 N  NE   . ARG A 1 99  ? 32.40617 2.34195  1.28947  1.000 36.39809  ? 124  ARG A NE   1 
ATOM   1499 C  CZ   . ARG A 1 99  ? 31.91663 1.86526  0.15150  1.000 40.45784  ? 124  ARG A CZ   1 
ATOM   1500 N  NH1  . ARG A 1 99  ? 30.63937 1.54798  0.02110  1.000 34.60857  ? 124  ARG A NH1  1 
ATOM   1501 N  NH2  . ARG A 1 99  ? 32.72426 1.71562  -0.88719 1.000 40.99589  ? 124  ARG A NH2  1 
ATOM   1502 H  H    . ARG A 1 99  ? 28.62905 4.61296  5.70114  1.000 28.21805  ? 124  ARG A H    1 
ATOM   1503 H  HA   . ARG A 1 99  ? 30.64929 6.06155  4.63989  1.000 30.29986  ? 124  ARG A HA   1 
ATOM   1504 H  HB2  . ARG A 1 99  ? 31.10481 3.81105  4.86137  1.000 36.23442  ? 124  ARG A HB2  1 
ATOM   1505 H  HB3  . ARG A 1 99  ? 29.77351 3.43457  4.07951  1.000 36.23442  ? 124  ARG A HB3  1 
ATOM   1506 H  HG2  . ARG A 1 99  ? 30.77419 4.33455  2.10424  1.000 41.08187  ? 124  ARG A HG2  1 
ATOM   1507 H  HG3  . ARG A 1 99  ? 32.13170 4.46706  2.91974  1.000 41.08187  ? 124  ARG A HG3  1 
ATOM   1508 H  HD2  . ARG A 1 99  ? 32.15546 2.13720  3.24851  1.000 41.40843  ? 124  ARG A HD2  1 
ATOM   1509 H  HD3  . ARG A 1 99  ? 30.80658 2.00986  2.41803  1.000 41.40843  ? 124  ARG A HD3  1 
ATOM   1510 H  HE   . ARG A 1 99  ? 33.23521 2.57017  1.30416  1.000 44.00756  ? 124  ARG A HE   1 
ATOM   1511 H  HH11 . ARG A 1 99  ? 30.10138 1.64876  0.68443  1.000 41.86013  ? 124  ARG A HH11 1 
ATOM   1512 H  HH12 . ARG A 1 99  ? 30.34680 1.24089  -0.72703 1.000 41.86013  ? 124  ARG A HH12 1 
ATOM   1513 H  HH21 . ARG A 1 99  ? 33.55528 1.92643  -0.81961 1.000 49.52491  ? 124  ARG A HH21 1 
ATOM   1514 H  HH22 . ARG A 1 99  ? 32.41775 1.40764  -1.62935 1.000 49.52491  ? 124  ARG A HH22 1 
ATOM   1515 N  N    . PHE A 1 100 ? 29.48282 7.15121  2.81438  1.000 30.55396  ? 125  PHE A N    1 
ATOM   1516 C  CA   . PHE A 1 100 ? 28.84756 7.80570  1.67934  1.000 24.63304  ? 125  PHE A CA   1 
ATOM   1517 C  C    . PHE A 1 100 ? 29.72216 7.72718  0.42362  1.000 24.50973  ? 125  PHE A C    1 
ATOM   1518 O  O    . PHE A 1 100 ? 30.94452 7.84512  0.49145  1.000 28.86629  ? 125  PHE A O    1 
ATOM   1519 C  CB   . PHE A 1 100 ? 28.58055 9.29116  1.99051  1.000 23.83897  ? 125  PHE A CB   1 
ATOM   1520 C  CG   . PHE A 1 100 ? 27.50515 9.53211  3.02818  1.000 24.62381  ? 125  PHE A CG   1 
ATOM   1521 C  CD1  . PHE A 1 100 ? 27.77948 9.39643  4.35961  1.000 25.55199  ? 125  PHE A CD1  1 
ATOM   1522 C  CD2  . PHE A 1 100 ? 26.24608 9.92258  2.65032  1.000 24.11751  ? 125  PHE A CD2  1 
ATOM   1523 C  CE1  . PHE A 1 100 ? 26.80818 9.62710  5.31926  1.000 29.19737  ? 125  PHE A CE1  1 
ATOM   1524 C  CE2  . PHE A 1 100 ? 25.26122 10.14151 3.58601  1.000 27.46514  ? 125  PHE A CE2  1 
ATOM   1525 C  CZ   . PHE A 1 100 ? 25.53890 9.99867  4.92187  1.000 25.20388  ? 125  PHE A CZ   1 
ATOM   1526 H  H    . PHE A 1 100 ? 30.13718 7.60812  3.13476  1.000 36.99460  ? 125  PHE A H    1 
ATOM   1527 H  HA   . PHE A 1 100 ? 28.01312 7.34694  1.49455  1.000 29.88949  ? 125  PHE A HA   1 
ATOM   1528 H  HB2  . PHE A 1 100 ? 29.40079 9.68987  2.32086  1.000 28.93661  ? 125  PHE A HB2  1 
ATOM   1529 H  HB3  . PHE A 1 100 ? 28.30275 9.73298  1.17288  1.000 28.93661  ? 125  PHE A HB3  1 
ATOM   1530 H  HD1  . PHE A 1 100 ? 28.63408 9.14457  4.62631  1.000 30.99223  ? 125  PHE A HD1  1 
ATOM   1531 H  HD2  . PHE A 1 100 ? 26.05493 10.04122 1.74794  1.000 29.27086  ? 125  PHE A HD2  1 
ATOM   1532 H  HE1  . PHE A 1 100 ? 27.00867 9.53271  6.22248  1.000 35.36668  ? 125  PHE A HE1  1 
ATOM   1533 H  HE2  . PHE A 1 100 ? 24.40674 10.38649 3.31263  1.000 33.28801  ? 125  PHE A HE2  1 
ATOM   1534 H  HZ   . PHE A 1 100 ? 24.87614 10.15120 5.55621  1.000 30.57450  ? 125  PHE A HZ   1 
ATOM   1535 N  N    . VAL A 1 101 ? 29.09394 7.54221  -0.73128 1.000 31.22216  ? 126  VAL A N    1 
ATOM   1536 C  CA   . VAL A 1 101 ? 29.70375 7.86850  -2.01907 1.000 31.75172  ? 126  VAL A CA   1 
ATOM   1537 C  C    . VAL A 1 101 ? 28.73601 8.79093  -2.74764 1.000 30.77169  ? 126  VAL A C    1 
ATOM   1538 O  O    . VAL A 1 101 ? 27.60323 9.00459  -2.30089 1.000 26.16352  ? 126  VAL A O    1 
ATOM   1539 C  CB   . VAL A 1 101 ? 30.03061 6.62592  -2.86325 1.000 37.18080  ? 126  VAL A CB   1 
ATOM   1540 C  CG1  . VAL A 1 101 ? 31.18938 5.86905  -2.24107 1.000 35.18626  ? 126  VAL A CG1  1 
ATOM   1541 C  CG2  . VAL A 1 101 ? 28.82986 5.73100  -2.97350 1.000 33.80646  ? 126  VAL A CG2  1 
ATOM   1542 H  H    . VAL A 1 101 ? 28.29821 7.22285  -0.79785 1.000 37.79643  ? 126  VAL A H    1 
ATOM   1543 H  HA   . VAL A 1 101 ? 30.54193 8.33564  -1.87717 1.000 38.43191  ? 126  VAL A HA   1 
ATOM   1544 H  HB   . VAL A 1 101 ? 30.28180 6.90814  -3.75664 1.000 44.94680  ? 126  VAL A HB   1 
ATOM   1545 H  HG11 . VAL A 1 101 ? 31.54750 5.24746  -2.89397 1.000 42.55335  ? 126  VAL A HG11 1 
ATOM   1546 H  HG12 . VAL A 1 101 ? 31.87478 6.50251  -1.97677 1.000 42.55335  ? 126  VAL A HG12 1 
ATOM   1547 H  HG13 . VAL A 1 101 ? 30.86932 5.38464  -1.46402 1.000 42.55335  ? 126  VAL A HG13 1 
ATOM   1548 H  HG21 . VAL A 1 101 ? 29.04775 4.97937  -3.54663 1.000 40.89759  ? 126  VAL A HG21 1 
ATOM   1549 H  HG22 . VAL A 1 101 ? 28.59015 5.41375  -2.08874 1.000 40.89759  ? 126  VAL A HG22 1 
ATOM   1550 H  HG23 . VAL A 1 101 ? 28.09411 6.23525  -3.35468 1.000 40.89759  ? 126  VAL A HG23 1 
ATOM   1551 N  N    . GLN A 1 102 ? 29.19404 9.36323  -3.86210 1.000 24.15758  ? 127  GLN A N    1 
ATOM   1552 C  CA   . GLN A 1 102 ? 28.31867 10.27011 -4.58843 1.000 27.71610  ? 127  GLN A CA   1 
ATOM   1553 C  C    . GLN A 1 102 ? 27.08770 9.48699  -5.01292 1.000 20.18825  ? 127  GLN A C    1 
ATOM   1554 O  O    . GLN A 1 102 ? 27.18931 8.34839  -5.45068 1.000 25.71020  ? 127  GLN A O    1 
ATOM   1555 C  CB   . GLN A 1 102 ? 29.02075 10.86346 -5.79681 1.000 26.69329  ? 127  GLN A CB   1 
ATOM   1556 C  CG   . GLN A 1 102 ? 30.00894 11.90874 -5.38796 1.000 33.31810  ? 127  GLN A CG   1 
ATOM   1557 C  CD   . GLN A 1 102 ? 30.75808 12.49976 -6.53962 1.000 27.41584  ? 127  GLN A CD   1 
ATOM   1558 O  OE1  . GLN A 1 102 ? 31.91648 12.89211 -6.37465 1.000 24.71355  ? 127  GLN A OE1  1 
ATOM   1559 N  NE2  . GLN A 1 102 ? 30.09503 12.64503 -7.70619 1.000 20.88426  ? 127  GLN A NE2  1 
ATOM   1560 H  H    . GLN A 1 102 ? 29.97545 9.24551  -4.20142 1.000 29.31894  ? 127  GLN A H    1 
ATOM   1561 H  HA   . GLN A 1 102 ? 28.06190 11.01991 -4.02916 1.000 33.58917  ? 127  GLN A HA   1 
ATOM   1562 H  HB2  . GLN A 1 102 ? 29.49424 10.16181 -6.27051 1.000 32.36179  ? 127  GLN A HB2  1 
ATOM   1563 H  HB3  . GLN A 1 102 ? 28.36410 11.27353 -6.38124 1.000 32.36179  ? 127  GLN A HB3  1 
ATOM   1564 H  HG2  . GLN A 1 102 ? 29.53733 12.62802 -4.93949 1.000 40.31156  ? 127  GLN A HG2  1 
ATOM   1565 H  HG3  . GLN A 1 102 ? 30.65617 11.51004 -4.78544 1.000 40.31156  ? 127  GLN A HG3  1 
ATOM   1566 H  HE21 . GLN A 1 102 ? 29.27252 12.40121 -7.76655 1.000 25.39096  ? 127  GLN A HE21 1 
ATOM   1567 H  HE22 . GLN A 1 102 ? 30.49504 12.98140 -8.38915 1.000 25.39096  ? 127  GLN A HE22 1 
ATOM   1568 N  N    . GLY A 1 103 ? 25.91557 10.06220 -4.82603 1.000 24.97394  ? 128  GLY A N    1 
ATOM   1569 C  CA   . GLY A 1 103 ? 24.67923 9.39846  -5.15087 1.000 24.58487  ? 128  GLY A CA   1 
ATOM   1570 C  C    . GLY A 1 103 ? 23.98668 8.69119  -3.99743 1.000 28.97028  ? 128  GLY A C    1 
ATOM   1571 O  O    . GLY A 1 103 ? 22.80802 8.38356  -4.10572 1.000 29.50743  ? 128  GLY A O    1 
ATOM   1572 H  H    . GLY A 1 103 ? 25.81304 10.85352 -4.50524 1.000 30.29857  ? 128  GLY A H    1 
ATOM   1573 H  HA2  . GLY A 1 103 ? 24.06033 10.05706 -5.50318 1.000 29.83168  ? 128  GLY A HA2  1 
ATOM   1574 H  HA3  . GLY A 1 103 ? 24.85752 8.73471  -5.83538 1.000 29.83168  ? 128  GLY A HA3  1 
ATOM   1575 N  N    . LYS A 1 104 ? 24.68777 8.47029  -2.88993 1.000 28.78758  ? 129  LYS A N    1 
ATOM   1576 C  CA   . LYS A 1 104 ? 24.22536 7.62840  -1.78966 1.000 35.42335  ? 129  LYS A CA   1 
ATOM   1577 C  C    . LYS A 1 104 ? 23.54778 8.47395  -0.71985 1.000 28.13843  ? 129  LYS A C    1 
ATOM   1578 O  O    . LYS A 1 104 ? 24.11370 9.47617  -0.27928 1.000 27.19171  ? 129  LYS A O    1 
ATOM   1579 C  CB   . LYS A 1 104 ? 25.42956 6.87670  -1.20490 1.000 32.06557  ? 129  LYS A CB   1 
ATOM   1580 C  CG   . LYS A 1 104 ? 25.16026 6.08042  0.03492  1.000 34.80251  ? 129  LYS A CG   1 
ATOM   1581 C  CD   . LYS A 1 104 ? 24.67377 4.70468  -0.32881 1.000 31.65799  ? 129  LYS A CD   1 
ATOM   1582 C  CE   . LYS A 1 104 ? 24.48594 3.87274  0.90601  1.000 36.32638  ? 129  LYS A CE   1 
ATOM   1583 N  NZ   . LYS A 1 104 ? 23.93549 2.55591  0.51071  1.000 39.07260  ? 129  LYS A NZ   1 
ATOM   1584 H  H    . LYS A 1 104 ? 25.46467 8.80967  -2.74554 1.000 34.87494  ? 129  LYS A H    1 
ATOM   1585 H  HA   . LYS A 1 104 ? 23.56687 6.99027  -2.10603 1.000 42.83786  ? 129  LYS A HA   1 
ATOM   1586 H  HB2  . LYS A 1 104 ? 25.75846 6.25966  -1.87720 1.000 38.80853  ? 129  LYS A HB2  1 
ATOM   1587 H  HB3  . LYS A 1 104 ? 26.11625 7.52596  -0.98619 1.000 38.80853  ? 129  LYS A HB3  1 
ATOM   1588 H  HG2  . LYS A 1 104 ? 25.97672 5.99460  0.55158  1.000 42.09286  ? 129  LYS A HG2  1 
ATOM   1589 H  HG3  . LYS A 1 104 ? 24.47748 6.52141  0.56428  1.000 42.09286  ? 129  LYS A HG3  1 
ATOM   1590 H  HD2  . LYS A 1 104 ? 23.82266 4.77161  -0.78928 1.000 38.31944  ? 129  LYS A HD2  1 
ATOM   1591 H  HD3  . LYS A 1 104 ? 25.32621 4.26898  -0.89922 1.000 38.31944  ? 129  LYS A HD3  1 
ATOM   1592 H  HE2  . LYS A 1 104 ? 25.33833 3.73973  1.34945  1.000 43.92150  ? 129  LYS A HE2  1 
ATOM   1593 H  HE3  . LYS A 1 104 ? 23.86306 4.30870  1.50839  1.000 43.92150  ? 129  LYS A HE3  1 
ATOM   1594 H  HZ1  . LYS A 1 104 ? 23.87756 2.02423  1.22210  1.000 47.21697  ? 129  LYS A HZ1  1 
ATOM   1595 H  HZ2  . LYS A 1 104 ? 23.12405 2.65813  0.15968  1.000 47.21697  ? 129  LYS A HZ2  1 
ATOM   1596 H  HZ3  . LYS A 1 104 ? 24.46543 2.17338  -0.09338 1.000 47.21697  ? 129  LYS A HZ3  1 
ATOM   1597 N  N    . ASP A 1 105 ? 22.35380 8.05169  -0.27459 1.000 22.10264  ? 130  ASP A N    1 
ATOM   1598 C  CA   . ASP A 1 105 ? 21.69792 8.70833  0.85285  1.000 26.55631  ? 130  ASP A CA   1 
ATOM   1599 C  C    . ASP A 1 105 ? 21.74939 7.82157  2.10093  1.000 27.47850  ? 130  ASP A C    1 
ATOM   1600 O  O    . ASP A 1 105 ? 21.81801 6.59047  2.00831  1.000 20.00659  ? 130  ASP A O    1 
ATOM   1601 C  CB   . ASP A 1 105 ? 20.23639 9.06070  0.53790  1.000 30.72430  ? 130  ASP A CB   1 
ATOM   1602 C  CG   . ASP A 1 105 ? 19.43534 7.87461  0.09759  1.000 36.64227  ? 130  ASP A CG   1 
ATOM   1603 O  OD1  . ASP A 1 105 ? 19.93866 6.73186  0.13502  1.000 38.29893  ? 130  ASP A OD1  1 
ATOM   1604 O  OD2  . ASP A 1 105 ? 18.27288 8.08197  -0.27942 1.000 48.93739  ? 130  ASP A OD2  1 
ATOM   1605 H  H    . ASP A 1 105 ? 21.91407 7.39324  -0.61026 1.000 26.85302  ? 130  ASP A H    1 
ATOM   1606 H  HA   . ASP A 1 105 ? 22.17218 9.53259  1.04407  1.000 32.19742  ? 130  ASP A HA   1 
ATOM   1607 H  HB2  . ASP A 1 105 ? 19.82023 9.42423  1.33511  1.000 37.19901  ? 130  ASP A HB2  1 
ATOM   1608 H  HB3  . ASP A 1 105 ? 20.21648 9.71746  -0.17565 1.000 37.19901  ? 130  ASP A HB3  1 
ATOM   1609 N  N    . TRP A 1 106 ? 21.74219 8.46043  3.27049  1.000 22.49409  ? 131  TRP A N    1 
ATOM   1610 C  CA   . TRP A 1 106 ? 21.53237 7.76164  4.52813  1.000 23.64066  ? 131  TRP A CA   1 
ATOM   1611 C  C    . TRP A 1 106 ? 20.51859 8.54530  5.34162  1.000 24.26621  ? 131  TRP A C    1 
ATOM   1612 O  O    . TRP A 1 106 ? 20.55552 9.77989  5.35802  1.000 17.46266  ? 131  TRP A O    1 
ATOM   1613 C  CB   . TRP A 1 106 ? 22.82630 7.63842  5.33457  1.000 20.78380  ? 131  TRP A CB   1 
ATOM   1614 C  CG   . TRP A 1 106 ? 23.73107 6.57041  4.87751  1.000 21.98396  ? 131  TRP A CG   1 
ATOM   1615 C  CD1  . TRP A 1 106 ? 24.89812 6.72354  4.22056  1.000 19.69221  ? 131  TRP A CD1  1 
ATOM   1616 C  CD2  . TRP A 1 106 ? 23.53457 5.16844  5.04234  1.000 18.58450  ? 131  TRP A CD2  1 
ATOM   1617 N  NE1  . TRP A 1 106 ? 25.46955 5.48558  3.96565  1.000 23.19399  ? 131  TRP A NE1  1 
ATOM   1618 C  CE2  . TRP A 1 106 ? 24.64101 4.51704  4.46015  1.000 25.81560  ? 131  TRP A CE2  1 
ATOM   1619 C  CE3  . TRP A 1 106 ? 22.52440 4.39659  5.62993  1.000 21.79922  ? 131  TRP A CE3  1 
ATOM   1620 C  CZ2  . TRP A 1 106 ? 24.76469 3.12954  4.45149  1.000 27.34812  ? 131  TRP A CZ2  1 
ATOM   1621 C  CZ3  . TRP A 1 106 ? 22.64312 3.02658  5.63205  1.000 22.61225  ? 131  TRP A CZ3  1 
ATOM   1622 C  CH2  . TRP A 1 106 ? 23.75114 2.40118  5.04614  1.000 25.27293  ? 131  TRP A CH2  1 
ATOM   1623 H  H    . TRP A 1 106 ? 21.85834 9.30811  3.35735  1.000 27.32276  ? 131  TRP A H    1 
ATOM   1624 H  HA   . TRP A 1 106 ? 21.19982 6.86728  4.35368  1.000 28.69863  ? 131  TRP A HA   1 
ATOM   1625 H  HB2  . TRP A 1 106 ? 23.30939 8.47738  5.27393  1.000 25.27040  ? 131  TRP A HB2  1 
ATOM   1626 H  HB3  . TRP A 1 106 ? 22.59795 7.45314  6.25893  1.000 25.27040  ? 131  TRP A HB3  1 
ATOM   1627 H  HD1  . TRP A 1 106 ? 25.26682 7.54093  3.97390  1.000 23.96050  ? 131  TRP A HD1  1 
ATOM   1628 H  HE1  . TRP A 1 106 ? 26.21814 5.35025  3.56454  1.000 28.16263  ? 131  TRP A HE1  1 
ATOM   1629 H  HE3  . TRP A 1 106 ? 21.78259 4.80548  6.01389  1.000 26.48890  ? 131  TRP A HE3  1 
ATOM   1630 H  HZ2  . TRP A 1 106 ? 25.49814 2.71082  4.06210  1.000 33.14758  ? 131  TRP A HZ2  1 
ATOM   1631 H  HZ3  . TRP A 1 106 ? 21.97945 2.50879  6.02745  1.000 27.46455  ? 131  TRP A HZ3  1 
ATOM   1632 H  HH2  . TRP A 1 106 ? 23.80636 1.47289  5.05743  1.000 30.65736  ? 131  TRP A HH2  1 
ATOM   1633 N  N    . GLY A 1 107 ? 19.62810 7.85867  6.04269  1.000 23.76953  ? 132  GLY A N    1 
ATOM   1634 C  CA   . GLY A 1 107 ? 18.65496 8.64323  6.79046  1.000 22.41306  ? 132  GLY A CA   1 
ATOM   1635 C  C    . GLY A 1 107 ? 17.66416 7.80054  7.54194  1.000 25.00180  ? 132  GLY A C    1 
ATOM   1636 O  O    . GLY A 1 107 ? 17.84323 6.59980  7.72986  1.000 18.17928  ? 132  GLY A O    1 
ATOM   1637 H  H    . GLY A 1 107 ? 19.56900 7.00254  6.09890  1.000 28.85328  ? 132  GLY A H    1 
ATOM   1638 H  HA2  . GLY A 1 107 ? 19.12188 9.20246  7.43089  1.000 27.22551  ? 132  GLY A HA2  1 
ATOM   1639 H  HA3  . GLY A 1 107 ? 18.16339 9.21000  6.17562  1.000 27.22551  ? 132  GLY A HA3  1 
ATOM   1640 N  N    . PHE A 1 108 ? 16.62351 8.48791  8.00356  1.000 21.00094  ? 133  PHE A N    1 
ATOM   1641 C  CA   . PHE A 1 108 ? 15.58460 7.90978  8.83763  1.000 24.85009  ? 133  PHE A CA   1 
ATOM   1642 C  C    . PHE A 1 108 ? 14.32987 7.82589  7.97785  1.000 19.01089  ? 133  PHE A C    1 
ATOM   1643 O  O    . PHE A 1 108 ? 13.76667 8.85014  7.57129  1.000 16.83842  ? 133  PHE A O    1 
ATOM   1644 C  CB   . PHE A 1 108 ? 15.35653 8.71950  10.11221 1.000 20.11923  ? 133  PHE A CB   1 
ATOM   1645 C  CG   . PHE A 1 108 ? 16.55232 8.83704  10.99989 1.000 19.55390  ? 133  PHE A CG   1 
ATOM   1646 C  CD1  . PHE A 1 108 ? 16.85876 7.83699  11.92238 1.000 29.24645  ? 133  PHE A CD1  1 
ATOM   1647 C  CD2  . PHE A 1 108 ? 17.33169 9.97079  10.96067 1.000 19.39154  ? 133  PHE A CD2  1 
ATOM   1648 C  CE1  . PHE A 1 108 ? 17.94326 7.94337  12.77549 1.000 24.62944  ? 133  PHE A CE1  1 
ATOM   1649 C  CE2  . PHE A 1 108 ? 18.40508 10.09991 11.82096 1.000 20.00439  ? 133  PHE A CE2  1 
ATOM   1650 C  CZ   . PHE A 1 108 ? 18.71437 9.09365  12.72741 1.000 24.45074  ? 133  PHE A CZ   1 
ATOM   1651 H  H    . PHE A 1 108 ? 16.49636 9.32228  7.83845  1.000 25.53097  ? 133  PHE A H    1 
ATOM   1652 H  HA   . PHE A 1 108 ? 15.84055 7.01805  9.12083  1.000 30.14995  ? 133  PHE A HA   1 
ATOM   1653 H  HB2  . PHE A 1 108 ? 15.08863 9.61780  9.86282  1.000 24.47292  ? 133  PHE A HB2  1 
ATOM   1654 H  HB3  . PHE A 1 108 ? 14.65234 8.29384  10.62585 1.000 24.47292  ? 133  PHE A HB3  1 
ATOM   1655 H  HD1  . PHE A 1 108 ? 16.32080 7.07959  11.96533 1.000 35.42558  ? 133  PHE A HD1  1 
ATOM   1656 H  HD2  . PHE A 1 108 ? 17.13596 10.64938 10.35561 1.000 23.59970  ? 133  PHE A HD2  1 
ATOM   1657 H  HE1  . PHE A 1 108 ? 18.15011 7.25743  13.36844 1.000 29.88518  ? 133  PHE A HE1  1 
ATOM   1658 H  HE2  . PHE A 1 108 ? 18.92660 10.86940 11.79288 1.000 24.33511  ? 133  PHE A HE2  1 
ATOM   1659 H  HZ   . PHE A 1 108 ? 19.43899 9.19204  13.30199 1.000 29.67073  ? 133  PHE A HZ   1 
ATOM   1660 N  N    . LYS A 1 109 ? 13.94144 6.60508  7.64532  1.000 17.62984  ? 134  LYS A N    1 
ATOM   1661 C  CA   . LYS A 1 109 ? 12.66855 6.40455  6.96494  1.000 25.93023  ? 134  LYS A CA   1 
ATOM   1662 C  C    . LYS A 1 109 ? 11.48961 6.86669  7.81541  1.000 29.30547  ? 134  LYS A C    1 
ATOM   1663 O  O    . LYS A 1 109 ? 10.51800 7.42255  7.28360  1.000 28.30984  ? 134  LYS A O    1 
ATOM   1664 C  CB   . LYS A 1 109 ? 12.51014 4.93185  6.58295  1.000 23.96468  ? 134  LYS A CB   1 
ATOM   1665 C  CG   . LYS A 1 109 ? 11.15845 4.61563  5.90129  1.000 32.68088  ? 134  LYS A CG   1 
ATOM   1666 C  CD   . LYS A 1 109 ? 11.16743 3.33695  5.04351  1.000 32.04965  ? 134  LYS A CD   1 
ATOM   1667 C  CE   . LYS A 1 109 ? 11.57307 2.09552  5.78606  1.000 43.40898  ? 134  LYS A CE   1 
ATOM   1668 N  NZ   . LYS A 1 109 ? 10.37115 1.37841  6.31151  1.000 55.90935  ? 134  LYS A NZ   1 
ATOM   1669 H  H    . LYS A 1 109 ? 14.38684 5.88549  7.79833  1.000 21.48565  ? 134  LYS A H    1 
ATOM   1670 H  HA   . LYS A 1 109 ? 12.66763 6.93438  6.15243  1.000 31.44612  ? 134  LYS A HA   1 
ATOM   1671 H  HB2  . LYS A 1 109 ? 13.21838 4.69057  5.96563  1.000 29.08746  ? 134  LYS A HB2  1 
ATOM   1672 H  HB3  . LYS A 1 109 ? 12.57190 4.39164  7.38623  1.000 29.08746  ? 134  LYS A HB3  1 
ATOM   1673 H  HG2  . LYS A 1 109 ? 10.48271 4.50333  6.58806  1.000 39.54690  ? 134  LYS A HG2  1 
ATOM   1674 H  HG3  . LYS A 1 109 ? 10.92205 5.35626  5.32121  1.000 39.54690  ? 134  LYS A HG3  1 
ATOM   1675 H  HD2  . LYS A 1 109 ? 10.27408 3.19077  4.69498  1.000 38.78942  ? 134  LYS A HD2  1 
ATOM   1676 H  HD3  . LYS A 1 109 ? 11.79310 3.45818  4.31225  1.000 38.78942  ? 134  LYS A HD3  1 
ATOM   1677 H  HE2  . LYS A 1 109 ? 12.04986 1.50033  5.18663  1.000 52.42062  ? 134  LYS A HE2  1 
ATOM   1678 H  HE3  . LYS A 1 109 ? 12.14047 2.33646  6.53500  1.000 52.42062  ? 134  LYS A HE3  1 
ATOM   1679 H  HZ1  . LYS A 1 109 ? 10.62254 0.65683  6.76783  1.000 67.42107  ? 134  LYS A HZ1  1 
ATOM   1680 H  HZ2  . LYS A 1 109 ? 9.90844  1.91442  6.85068  1.000 67.42107  ? 134  LYS A HZ2  1 
ATOM   1681 H  HZ3  . LYS A 1 109 ? 9.84828  1.12595  5.63700  1.000 67.42107  ? 134  LYS A HZ3  1 
ATOM   1682 N  N    . LYS A 1 110 ? 11.53981 6.62442  9.12517  1.000 23.88138  ? 135  LYS A N    1 
ATOM   1683 C  CA   . LYS A 1 110 ? 10.50014 7.06016  10.05797 1.000 19.22446  ? 135  LYS A CA   1 
ATOM   1684 C  C    . LYS A 1 110 ? 11.06825 8.17592  10.92253 1.000 23.06547  ? 135  LYS A C    1 
ATOM   1685 O  O    . LYS A 1 110 ? 11.33869 7.99797  12.09331 1.000 21.56489  ? 135  LYS A O    1 
ATOM   1686 C  CB   . LYS A 1 110 ? 10.01862 5.90205  10.89060 1.000 30.26276  ? 135  LYS A CB   1 
ATOM   1687 C  CG   . LYS A 1 110 ? 9.15811  4.94293  10.09838 1.000 26.88587  ? 135  LYS A CG   1 
ATOM   1688 C  CD   . LYS A 1 110 ? 8.71295  3.74868  10.94506 1.000 34.94625  ? 135  LYS A CD   1 
ATOM   1689 C  CE   . LYS A 1 110 ? 7.70277  2.92173  10.18154 1.000 38.12279  ? 135  LYS A CE   1 
ATOM   1690 N  NZ   . LYS A 1 110 ? 7.32128  1.66892  10.88876 1.000 47.79757  ? 135  LYS A NZ   1 
ATOM   1691 H  H    . LYS A 1 110 ? 12.18229 6.19872  9.50675  1.000 28.98750  ? 135  LYS A H    1 
ATOM   1692 H  HA   . LYS A 1 110 ? 9.74174  7.40244  9.55940  1.000 22.15343  ? 135  LYS A HA   1 
ATOM   1693 H  HB2  . LYS A 1 110 ? 10.78555 5.41262  11.22702 1.000 36.64515  ? 135  LYS A HB2  1 
ATOM   1694 H  HB3  . LYS A 1 110 ? 9.49079  6.24102  11.63046 1.000 36.64515  ? 135  LYS A HB3  1 
ATOM   1695 H  HG2  . LYS A 1 110 ? 8.36523  5.40664  9.78657  1.000 32.59288  ? 135  LYS A HG2  1 
ATOM   1696 H  HG3  . LYS A 1 110 ? 9.66497  4.60733  9.34250  1.000 32.59288  ? 135  LYS A HG3  1 
ATOM   1697 H  HD2  . LYS A 1 110 ? 9.47903  3.19086  11.15210 1.000 42.26535  ? 135  LYS A HD2  1 
ATOM   1698 H  HD3  . LYS A 1 110 ? 8.30112  4.06420  11.76465 1.000 42.26535  ? 135  LYS A HD3  1 
ATOM   1699 H  HE2  . LYS A 1 110 ? 6.89832  3.44794  10.05164 1.000 46.07719  ? 135  LYS A HE2  1 
ATOM   1700 H  HE3  . LYS A 1 110 ? 8.08095  2.67631  9.32268  1.000 46.07719  ? 135  LYS A HE3  1 
ATOM   1701 H  HZ1  . LYS A 1 110 ? 8.03872  1.15579  11.00740 1.000 57.68693  ? 135  LYS A HZ1  1 
ATOM   1702 H  HZ2  . LYS A 1 110 ? 6.97019  1.86272  11.68330 1.000 57.68693  ? 135  LYS A HZ2  1 
ATOM   1703 H  HZ3  . LYS A 1 110 ? 6.72085  1.21958  10.40951 1.000 57.68693  ? 135  LYS A HZ3  1 
ATOM   1704 N  N    . PHE A 1 111 ? 11.21951 9.35856  10.34039 1.000 19.54963  ? 136  PHE A N    1 
ATOM   1705 C  CA   . PHE A 1 111 ? 11.85637 10.41102 11.12720 1.000 17.56885  ? 136  PHE A CA   1 
ATOM   1706 C  C    . PHE A 1 111 ? 10.91101 11.07076 12.13632 1.000 26.82160  ? 136  PHE A C    1 
ATOM   1707 O  O    . PHE A 1 111 ? 11.32493 11.39050 13.25966 1.000 22.59123  ? 136  PHE A O    1 
ATOM   1708 C  CB   . PHE A 1 111 ? 12.44004 11.48478 10.24161 1.000 16.72979  ? 136  PHE A CB   1 
ATOM   1709 C  CG   . PHE A 1 111 ? 13.10317 12.56351 11.02338 1.000 21.89786  ? 136  PHE A CG   1 
ATOM   1710 C  CD1  . PHE A 1 111 ? 14.19815 12.28639 11.82396 1.000 27.64211  ? 136  PHE A CD1  1 
ATOM   1711 C  CD2  . PHE A 1 111 ? 12.59285 13.86041 11.01992 1.000 25.91812  ? 136  PHE A CD2  1 
ATOM   1712 C  CE1  . PHE A 1 111 ? 14.78947 13.30076 12.59099 1.000 24.90547  ? 136  PHE A CE1  1 
ATOM   1713 C  CE2  . PHE A 1 111 ? 13.16342 14.87304 11.79372 1.000 23.65709  ? 136  PHE A CE2  1 
ATOM   1714 C  CZ   . PHE A 1 111 ? 14.26369 14.59514 12.57402 1.000 21.17611  ? 136  PHE A CZ   1 
ATOM   1715 H  H    . PHE A 1 111 ? 10.97816 9.56680  9.54164  1.000 23.78940  ? 136  PHE A H    1 
ATOM   1716 H  HA   . PHE A 1 111 ? 12.57510 9.97979  11.61544 1.000 21.41246  ? 136  PHE A HA   1 
ATOM   1717 H  HB2  . PHE A 1 111 ? 13.10159 11.08694 9.65427  1.000 20.40559  ? 136  PHE A HB2  1 
ATOM   1718 H  HB3  . PHE A 1 111 ? 11.72887 11.88511 9.71731  1.000 20.40559  ? 136  PHE A HB3  1 
ATOM   1719 H  HD1  . PHE A 1 111 ? 14.54331 11.42331 11.85326 1.000 33.50038  ? 136  PHE A HD1  1 
ATOM   1720 H  HD2  . PHE A 1 111 ? 11.85448 14.05609 10.48944 1.000 31.43159  ? 136  PHE A HD2  1 
ATOM   1721 H  HE1  . PHE A 1 111 ? 15.53509 13.11093 13.11339 1.000 30.21641  ? 136  PHE A HE1  1 
ATOM   1722 H  HE2  . PHE A 1 111 ? 12.80257 15.73010 11.78223 1.000 28.71835  ? 136  PHE A HE2  1 
ATOM   1723 H  HZ   . PHE A 1 111 ? 14.65455 15.26534 13.08682 1.000 25.74118  ? 136  PHE A HZ   1 
ATOM   1724 N  N    . ILE A 1 112 ? 9.66354  11.32254 11.74997 1.000 18.28121  ? 137  ILE A N    1 
ATOM   1725 C  CA   . ILE A 1 112 ? 8.70091  11.92747 12.66535 1.000 23.95309  ? 137  ILE A CA   1 
ATOM   1726 C  C    . ILE A 1 112 ? 7.29983  11.56743 12.19361 1.000 26.20449  ? 137  ILE A C    1 
ATOM   1727 O  O    . ILE A 1 112 ? 7.02646  11.61144 10.98124 1.000 21.45658  ? 137  ILE A O    1 
ATOM   1728 C  CB   . ILE A 1 112 ? 8.89806  13.44060 12.75167 1.000 22.83441  ? 137  ILE A CB   1 
ATOM   1729 C  CG1  . ILE A 1 112 ? 7.96824  14.07061 13.80269 1.000 30.92379  ? 137  ILE A CG1  1 
ATOM   1730 C  CG2  . ILE A 1 112 ? 8.51253  14.09654 11.47690 1.000 25.26916  ? 137  ILE A CG2  1 
ATOM   1731 C  CD1  . ILE A 1 112 ? 8.38976  13.88433 15.19939 1.000 25.19135  ? 137  ILE A CD1  1 
ATOM   1732 H  H    . ILE A 1 112 ? 9.35192  11.15299 10.96655 1.000 22.26730  ? 137  ILE A H    1 
ATOM   1733 H  HA   . ILE A 1 112 ? 8.82428  11.56756 13.55762 1.000 29.07356  ? 137  ILE A HA   1 
ATOM   1734 H  HB   . ILE A 1 112 ? 9.83422  13.56851 12.97109 1.000 27.73114  ? 137  ILE A HB   1 
ATOM   1735 H  HG12 . ILE A 1 112 ? 7.92180  15.02544 13.63823 1.000 37.43839  ? 137  ILE A HG12 1 
ATOM   1736 H  HG13 . ILE A 1 112 ? 7.08758  13.67475 13.70985 1.000 37.43839  ? 137  ILE A HG13 1 
ATOM   1737 H  HG21 . ILE A 1 112 ? 7.54620  14.08192 11.39385 1.000 30.65284  ? 137  ILE A HG21 1 
ATOM   1738 H  HG22 . ILE A 1 112 ? 8.83003  15.01307 11.48470 1.000 30.65284  ? 137  ILE A HG22 1 
ATOM   1739 H  HG23 . ILE A 1 112 ? 8.91532  13.61322 10.73861 1.000 30.65284  ? 137  ILE A HG23 1 
ATOM   1740 H  HD11 . ILE A 1 112 ? 9.23529  14.33922 15.33742 1.000 30.55946  ? 137  ILE A HD11 1 
ATOM   1741 H  HD12 . ILE A 1 112 ? 7.71351  14.25801 15.78586 1.000 30.55946  ? 137  ILE A HD12 1 
ATOM   1742 H  HD13 . ILE A 1 112 ? 8.49200  12.93578 15.37457 1.000 30.55946  ? 137  ILE A HD13 1 
ATOM   1743 N  N    . ARG A 1 113 ? 6.44063  11.15659 13.13409 1.000 31.23232  ? 138  ARG A N    1 
ATOM   1744 C  CA   . ARG A 1 113 ? 5.05898  10.82781 12.83190 1.000 28.79813  ? 138  ARG A CA   1 
ATOM   1745 C  C    . ARG A 1 113 ? 4.34782  12.04795 12.27956 1.000 24.98272  ? 138  ARG A C    1 
ATOM   1746 O  O    . ARG A 1 113 ? 4.47040  13.15550 12.81483 1.000 25.39586  ? 138  ARG A O    1 
ATOM   1747 C  CB   . ARG A 1 113 ? 4.31976  10.32698 14.06323 1.000 32.98006  ? 138  ARG A CB   1 
ATOM   1748 C  CG   . ARG A 1 113 ? 4.11153  8.83505  14.07106 1.000 36.43630  ? 138  ARG A CG   1 
ATOM   1749 C  CD   . ARG A 1 113 ? 3.02163  8.39253  14.99989 1.000 36.61290  ? 138  ARG A CD   1 
ATOM   1750 N  NE   . ARG A 1 113 ? 1.74532  8.20348  14.32579 1.000 46.60606  ? 138  ARG A NE   1 
ATOM   1751 C  CZ   . ARG A 1 113 ? 1.44158  7.12991  13.60806 1.000 41.46284  ? 138  ARG A CZ   1 
ATOM   1752 N  NH1  . ARG A 1 113 ? 2.33647  6.18394  13.37342 1.000 41.35401  ? 138  ARG A NH1  1 
ATOM   1753 N  NH2  . ARG A 1 113 ? 0.21420  7.00225  13.11677 1.000 38.45770  ? 138  ARG A NH2  1 
ATOM   1754 H  H    . ARG A 1 113 ? 6.64293  11.06095 13.96447 1.000 37.80863  ? 138  ARG A H    1 
ATOM   1755 H  HA   . ARG A 1 113 ? 5.05105  10.11508 12.17399 1.000 34.88760  ? 138  ARG A HA   1 
ATOM   1756 H  HB2  . ARG A 1 113 ? 4.83283  10.55997 14.85276 1.000 39.90592  ? 138  ARG A HB2  1 
ATOM   1757 H  HB3  . ARG A 1 113 ? 3.44725  10.74938 14.09798 1.000 39.90592  ? 138  ARG A HB3  1 
ATOM   1758 H  HG2  . ARG A 1 113 ? 3.87452  8.54611  13.17594 1.000 44.05340  ? 138  ARG A HG2  1 
ATOM   1759 H  HG3  . ARG A 1 113 ? 4.93412  8.40440  14.35178 1.000 44.05340  ? 138  ARG A HG3  1 
ATOM   1760 H  HD2  . ARG A 1 113 ? 3.27465  7.54773  15.40387 1.000 44.26532  ? 138  ARG A HD2  1 
ATOM   1761 H  HD3  . ARG A 1 113 ? 2.89999  9.06582  15.68749 1.000 44.26532  ? 138  ARG A HD3  1 
ATOM   1762 H  HE   . ARG A 1 113 ? 1.15387  8.82375  14.39696 1.000 56.25711  ? 138  ARG A HE   1 
ATOM   1763 H  HH11 . ARG A 1 113 ? 3.13325  6.25810  13.68845 1.000 49.95466  ? 138  ARG A HH11 1 
ATOM   1764 H  HH12 . ARG A 1 113 ? 2.12133  5.49494  12.90588 1.000 49.95466  ? 138  ARG A HH12 1 
ATOM   1765 H  HH21 . ARG A 1 113 ? -0.37393 7.61190  13.26515 1.000 46.47909  ? 138  ARG A HH21 1 
ATOM   1766 H  HH22 . ARG A 1 113 ? 0.00761  6.30993  12.65027 1.000 46.47909  ? 138  ARG A HH22 1 
ATOM   1767 N  N    . ARG A 1 114 ? 3.60099  11.83573 11.19385 1.000 25.70521  ? 139  ARG A N    1 
ATOM   1768 C  CA   . ARG A 1 114 ? 2.87722  12.92843 10.56755 1.000 26.66929  ? 139  ARG A CA   1 
ATOM   1769 C  C    . ARG A 1 114 ? 1.86926  13.52881 11.53741 1.000 22.51490  ? 139  ARG A C    1 
ATOM   1770 O  O    . ARG A 1 114 ? 1.74158  14.75525 11.62617 1.000 24.41963  ? 139  ARG A O    1 
ATOM   1771 C  CB   . ARG A 1 114 ? 2.17914  12.43405 9.28538  1.000 27.13379  ? 139  ARG A CB   1 
ATOM   1772 C  CG   . ARG A 1 114 ? 3.18440  12.09151 8.12853  1.000 24.81592  ? 139  ARG A CG   1 
ATOM   1773 C  CD   . ARG A 1 114 ? 2.49351  11.82741 6.78942  1.000 29.32092  ? 139  ARG A CD   1 
ATOM   1774 N  NE   . ARG A 1 114 ? 1.47953  12.83474 6.50245  1.000 27.13808  ? 139  ARG A NE   1 
ATOM   1775 C  CZ   . ARG A 1 114 ? 1.73240  14.03303 5.99057  1.000 31.23806  ? 139  ARG A CZ   1 
ATOM   1776 N  NH1  . ARG A 1 114 ? 2.94591  14.37159 5.59243  1.000 32.76123  ? 139  ARG A NH1  1 
ATOM   1777 N  NH2  . ARG A 1 114 ? 0.74178  14.91933 5.87882  1.000 32.08036  ? 139  ARG A NH2  1 
ATOM   1778 H  H    . ARG A 1 114 ? 3.50064  11.07400 10.80745 1.000 31.17610  ? 139  ARG A H    1 
ATOM   1779 H  HA   . ARG A 1 114 ? 3.50344  13.62347 10.31131 1.000 32.33299  ? 139  ARG A HA   1 
ATOM   1780 H  HB2  . ARG A 1 114 ? 1.67577  11.63088 9.49141  1.000 32.89039  ? 139  ARG A HB2  1 
ATOM   1781 H  HB3  . ARG A 1 114 ? 1.58100  13.12763 8.96588  1.000 32.89039  ? 139  ARG A HB3  1 
ATOM   1782 H  HG2  . ARG A 1 114 ? 3.79202  12.83795 8.00801  1.000 30.10895  ? 139  ARG A HG2  1 
ATOM   1783 H  HG3  . ARG A 1 114 ? 3.68183  11.29434 8.36930  1.000 30.10895  ? 139  ARG A HG3  1 
ATOM   1784 H  HD2  . ARG A 1 114 ? 3.15311  11.84757 6.07849  1.000 35.51495  ? 139  ARG A HD2  1 
ATOM   1785 H  HD3  . ARG A 1 114 ? 2.06167  10.95927 6.81680  1.000 35.51495  ? 139  ARG A HD3  1 
ATOM   1786 H  HE   . ARG A 1 114 ? 0.66049  12.63897 6.67695  1.000 32.89554  ? 139  ARG A HE   1 
ATOM   1787 H  HH11 . ARG A 1 114 ? 3.59362  13.81015 5.66219  1.000 39.64332  ? 139  ARG A HH11 1 
ATOM   1788 H  HH12 . ARG A 1 114 ? 3.08807  15.15339 5.26353  1.000 39.64332  ? 139  ARG A HH12 1 
ATOM   1789 H  HH21 . ARG A 1 114 ? -0.05184 14.71206 6.13728  1.000 38.82628  ? 139  ARG A HH21 1 
ATOM   1790 H  HH22 . ARG A 1 114 ? 0.89674  15.69802 5.54830  1.000 38.82628  ? 139  ARG A HH22 1 
ATOM   1791 N  N    . ASP A 1 115 ? 1.13554  12.69942 12.26263 1.000 27.97736  ? 140  ASP A N    1 
ATOM   1792 C  CA   . ASP A 1 115 ? 0.09845  13.29548 13.11063 1.000 27.17336  ? 140  ASP A CA   1 
ATOM   1793 C  C    . ASP A 1 115 ? 0.68817  13.93667 14.36293 1.000 27.94501  ? 140  ASP A C    1 
ATOM   1794 O  O    . ASP A 1 115 ? -0.03275 14.60602 15.08812 1.000 32.07932  ? 140  ASP A O    1 
ATOM   1795 C  CB   . ASP A 1 115 ? -0.99052 12.27026 13.45005 1.000 33.34102  ? 140  ASP A CB   1 
ATOM   1796 C  CG   . ASP A 1 115 ? -0.47999 11.11978 14.24790 1.000 33.66878  ? 140  ASP A CG   1 
ATOM   1797 O  OD1  . ASP A 1 115 ? 0.63586  11.25040 14.76551 1.000 28.03631  ? 140  ASP A OD1  1 
ATOM   1798 O  OD2  . ASP A 1 115 ? -1.16788 10.07763 14.34065 1.000 36.01785  ? 140  ASP A OD2  1 
ATOM   1799 H  H    . ASP A 1 115 ? 1.20891  11.84282 12.28419 1.000 33.90268  ? 140  ASP A H    1 
ATOM   1800 H  HA   . ASP A 1 115 ? -0.36047 13.99505 12.61983 1.000 32.93788  ? 140  ASP A HA   1 
ATOM   1801 H  HB2  . ASP A 1 115 ? -1.68487 12.70773 13.96716 1.000 40.33907  ? 140  ASP A HB2  1 
ATOM   1802 H  HB3  . ASP A 1 115 ? -1.36189 11.92035 12.62510 1.000 40.33907  ? 140  ASP A HB3  1 
ATOM   1803 N  N    . PHE A 1 116 ? 1.98571  13.75165 14.63119 1.000 28.84525  ? 141  PHE A N    1 
ATOM   1804 C  CA   . PHE A 1 116 ? 2.65650  14.53735 15.65533 1.000 26.25273  ? 141  PHE A CA   1 
ATOM   1805 C  C    . PHE A 1 116 ? 3.10030  15.85223 15.05071 1.000 21.40072  ? 141  PHE A C    1 
ATOM   1806 O  O    . PHE A 1 116 ? 2.94097  16.91876 15.65057 1.000 24.75965  ? 141  PHE A O    1 
ATOM   1807 C  CB   . PHE A 1 116 ? 3.84031  13.73992 16.21034 1.000 24.19583  ? 141  PHE A CB   1 
ATOM   1808 C  CG   . PHE A 1 116 ? 4.51429  14.37696 17.39335 1.000 24.52433  ? 141  PHE A CG   1 
ATOM   1809 C  CD1  . PHE A 1 116 ? 5.44852  15.38367 17.19379 1.000 26.67585  ? 141  PHE A CD1  1 
ATOM   1810 C  CD2  . PHE A 1 116 ? 4.22210  13.96486 18.68724 1.000 30.47401  ? 141  PHE A CD2  1 
ATOM   1811 C  CE1  . PHE A 1 116 ? 6.05272  15.98062 18.25220 1.000 30.29503  ? 141  PHE A CE1  1 
ATOM   1812 C  CE2  . PHE A 1 116 ? 4.83327  14.55364 19.75752 1.000 31.40663  ? 141  PHE A CE2  1 
ATOM   1813 C  CZ   . PHE A 1 116 ? 5.76504  15.55787 19.54063 1.000 33.43604  ? 141  PHE A CZ   1 
ATOM   1814 H  H    . PHE A 1 116 ? 2.49147  13.18042 14.23431 1.000 34.94415  ? 141  PHE A H    1 
ATOM   1815 H  HA   . PHE A 1 116 ? 2.06871  14.72221 16.40448 1.000 31.83312  ? 141  PHE A HA   1 
ATOM   1816 H  HB2  . PHE A 1 116 ? 3.52258  12.86659 16.48827 1.000 29.36484  ? 141  PHE A HB2  1 
ATOM   1817 H  HB3  . PHE A 1 116 ? 4.50473  13.64386 15.51018 1.000 29.36484  ? 141  PHE A HB3  1 
ATOM   1818 H  HD1  . PHE A 1 116 ? 5.66192  15.65096 16.32897 1.000 32.34087  ? 141  PHE A HD1  1 
ATOM   1819 H  HD2  . PHE A 1 116 ? 3.60545  13.28265 18.82592 1.000 36.89866  ? 141  PHE A HD2  1 
ATOM   1820 H  HE1  . PHE A 1 116 ? 6.65879  16.67221 18.11335 1.000 36.68388  ? 141  PHE A HE1  1 
ATOM   1821 H  HE2  . PHE A 1 116 ? 4.62664  14.28380 20.62320 1.000 38.01780  ? 141  PHE A HE2  1 
ATOM   1822 H  HZ   . PHE A 1 116 ? 6.19924  15.94979 20.26366 1.000 40.45309  ? 141  PHE A HZ   1 
ATOM   1823 N  N    . LEU A 1 117 ? 3.60902  15.78649 13.83122 1.000 23.94811  ? 142  LEU A N    1 
ATOM   1824 C  CA   . LEU A 1 117 ? 4.03655  16.97964 13.12700 1.000 21.92046  ? 142  LEU A CA   1 
ATOM   1825 C  C    . LEU A 1 117 ? 2.89703  17.94057 12.93020 1.000 26.27554  ? 142  LEU A C    1 
ATOM   1826 O  O    . LEU A 1 117 ? 3.07300  19.15893 13.06034 1.000 25.02092  ? 142  LEU A O    1 
ATOM   1827 C  CB   . LEU A 1 117 ? 4.60051  16.59207 11.77187 1.000 25.36748  ? 142  LEU A CB   1 
ATOM   1828 C  CG   . LEU A 1 117 ? 5.30838  17.68100 10.99916 1.000 32.35956  ? 142  LEU A CG   1 
ATOM   1829 C  CD1  . LEU A 1 117 ? 6.51895  18.19989 11.68853 1.000 23.07402  ? 142  LEU A CD1  1 
ATOM   1830 C  CD2  . LEU A 1 117 ? 5.71760  17.08191 9.69408  1.000 35.63087  ? 142  LEU A CD2  1 
ATOM   1831 H  H    . LEU A 1 117 ? 3.71813  15.05864 13.38632 1.000 29.06758  ? 142  LEU A H    1 
ATOM   1832 H  HA   . LEU A 1 117 ? 4.72468  17.41790 13.65169 1.000 26.63440  ? 142  LEU A HA   1 
ATOM   1833 H  HB2  . LEU A 1 117 ? 5.24081  15.87600 11.90666 1.000 30.77082  ? 142  LEU A HB2  1 
ATOM   1834 H  HB3  . LEU A 1 117 ? 3.86669  16.28121 11.21890 1.000 30.77082  ? 142  LEU A HB3  1 
ATOM   1835 H  HG   . LEU A 1 117 ? 4.71109  18.43831 10.89604 1.000 39.16132  ? 142  LEU A HG   1 
ATOM   1836 H  HD11 . LEU A 1 117 ? 6.24577  18.69446 12.47700 1.000 28.01867  ? 142  LEU A HD11 1 
ATOM   1837 H  HD12 . LEU A 1 117 ? 7.08101  17.45220 11.94533 1.000 28.01867  ? 142  LEU A HD12 1 
ATOM   1838 H  HD13 . LEU A 1 117 ? 7.00157  18.78371 11.08261 1.000 28.01867  ? 142  LEU A HD13 1 
ATOM   1839 H  HD21 . LEU A 1 117 ? 6.30015  16.32492 9.86292  1.000 43.08689  ? 142  LEU A HD21 1 
ATOM   1840 H  HD22 . LEU A 1 117 ? 4.92450  16.78932 9.21838  1.000 43.08689  ? 142  LEU A HD22 1 
ATOM   1841 H  HD23 . LEU A 1 117 ? 6.18780  17.75137 9.17288  1.000 43.08689  ? 142  LEU A HD23 1 
ATOM   1842 N  N    . LEU A 1 118 ? 1.72612  17.41547 12.56477 1.000 25.06742  ? 143  LEU A N    1 
ATOM   1843 C  CA   . LEU A 1 118 ? 0.58861  18.25397 12.25236 1.000 27.53727  ? 143  LEU A CA   1 
ATOM   1844 C  C    . LEU A 1 118 ? -0.15857 18.72470 13.47892 1.000 30.48848  ? 143  LEU A C    1 
ATOM   1845 O  O    . LEU A 1 118 ? -1.06617 19.53764 13.32535 1.000 34.44535  ? 143  LEU A O    1 
ATOM   1846 C  CB   . LEU A 1 118 ? -0.39130 17.49821 11.35938 1.000 29.95078  ? 143  LEU A CB   1 
ATOM   1847 C  CG   . LEU A 1 118 ? 0.09173  17.09586 9.97080  1.000 31.20596  ? 143  LEU A CG   1 
ATOM   1848 C  CD1  . LEU A 1 118 ? -1.03223 16.30849 9.24855  1.000 31.54299  ? 143  LEU A CD1  1 
ATOM   1849 C  CD2  . LEU A 1 118 ? 0.50130  18.31187 9.17806  1.000 32.32015  ? 143  LEU A CD2  1 
ATOM   1850 H  H    . LEU A 1 118 ? 1.57262  16.57238 12.49242 1.000 30.41075  ? 143  LEU A H    1 
ATOM   1851 H  HA   . LEU A 1 118 ? 0.91497  19.03158 11.77308 1.000 33.37457  ? 143  LEU A HA   1 
ATOM   1852 H  HB2  . LEU A 1 118 ? -0.64100 16.68073 11.81795 1.000 36.27078  ? 143  LEU A HB2  1 
ATOM   1853 H  HB3  . LEU A 1 118 ? -1.17212 18.05982 11.23360 1.000 36.27078  ? 143  LEU A HB3  1 
ATOM   1854 H  HG   . LEU A 1 118 ? 0.87274  16.52510 10.04256 1.000 37.77699  ? 143  LEU A HG   1 
ATOM   1855 H  HD11 . LEU A 1 118 ? -1.81312 16.87782 9.16505  1.000 38.18144  ? 143  LEU A HD11 1 
ATOM   1856 H  HD12 . LEU A 1 118 ? -0.71876 16.04587 8.36897  1.000 38.18144  ? 143  LEU A HD12 1 
ATOM   1857 H  HD13 . LEU A 1 118 ? -1.25146 15.52077 9.77040  1.000 38.18144  ? 143  LEU A HD13 1 
ATOM   1858 H  HD21 . LEU A 1 118 ? -0.20579 18.97404 9.22761  1.000 39.11402  ? 143  LEU A HD21 1 
ATOM   1859 H  HD22 . LEU A 1 118 ? 1.31949  18.67290 9.55373  1.000 39.11402  ? 143  LEU A HD22 1 
ATOM   1860 H  HD23 . LEU A 1 118 ? 0.64748  18.05250 8.25488  1.000 39.11402  ? 143  LEU A HD23 1 
ATOM   1861 N  N    . ASP A 1 119 ? 0.18401  18.22379 14.67508 1.000 33.20184  ? 144  ASP A N    1 
ATOM   1862 C  CA   . ASP A 1 119 ? -0.46954 18.60486 15.93197 1.000 30.41701  ? 144  ASP A CA   1 
ATOM   1863 C  C    . ASP A 1 119 ? 0.04648  19.97863 16.34932 1.000 29.18865  ? 144  ASP A C    1 
ATOM   1864 O  O    . ASP A 1 119 ? 1.21303  20.12091 16.72830 1.000 30.30651  ? 144  ASP A O    1 
ATOM   1865 C  CB   . ASP A 1 119 ? -0.19809 17.54025 16.99950 1.000 28.72172  ? 144  ASP A CB   1 
ATOM   1866 C  CG   . ASP A 1 119 ? -0.98762 17.75051 18.26565 1.000 34.42217  ? 144  ASP A CG   1 
ATOM   1867 O  OD1  . ASP A 1 119 ? -1.67732 18.78736 18.38880 1.000 34.40482  ? 144  ASP A OD1  1 
ATOM   1868 O  OD2  . ASP A 1 119 ? -0.89933 16.86719 19.17889 1.000 29.89322  ? 144  ASP A OD2  1 
ATOM   1869 H  H    . ASP A 1 119 ? 0.81036  17.64501 14.78597 1.000 40.17205  ? 144  ASP A H    1 
ATOM   1870 H  HA   . ASP A 1 119 ? -1.42958 18.67007 15.80963 1.000 36.83026  ? 144  ASP A HA   1 
ATOM   1871 H  HB2  . ASP A 1 119 ? -0.43468 16.67000 16.64232 1.000 34.79591  ? 144  ASP A HB2  1 
ATOM   1872 H  HB3  . ASP A 1 119 ? 0.74402  17.55946 17.22962 1.000 34.79591  ? 144  ASP A HB3  1 
ATOM   1873 N  N    . GLU A 1 120 ? -0.81585 20.99331 16.26092 1.000 32.62147  ? 145  GLU A N    1 
ATOM   1874 C  CA   A GLU A 1 120 ? -0.38123 22.35255 16.54510 0.447 33.29424  ? 145  GLU A CA   1 
ATOM   1875 C  CA   B GLU A 1 120 ? -0.38916 22.35827 16.55106 0.553 32.82746  ? 145  GLU A CA   1 
ATOM   1876 C  C    . GLU A 1 120 ? 0.14878  22.48755 17.96016 1.000 31.39104  ? 145  GLU A C    1 
ATOM   1877 O  O    . GLU A 1 120 ? 0.88896  23.43096 18.23369 1.000 31.88704  ? 145  GLU A O    1 
ATOM   1878 C  CB   A GLU A 1 120 ? -1.53496 23.33315 16.30470 0.447 35.23453  ? 145  GLU A CB   1 
ATOM   1879 C  CB   B GLU A 1 120 ? -1.54383 23.35845 16.38264 0.553 35.22783  ? 145  GLU A CB   1 
ATOM   1880 C  CG   A GLU A 1 120 ? -1.60134 23.87369 14.87626 0.447 41.62051  ? 145  GLU A CG   1 
ATOM   1881 C  CG   B GLU A 1 120 ? -2.00906 23.66213 14.96084 0.553 41.08425  ? 145  GLU A CG   1 
ATOM   1882 C  CD   A GLU A 1 120 ? -1.77276 22.77599 13.82050 0.447 41.04005  ? 145  GLU A CD   1 
ATOM   1883 C  CD   B GLU A 1 120 ? -1.13378 24.68487 14.22665 0.553 45.50628  ? 145  GLU A CD   1 
ATOM   1884 O  OE1  A GLU A 1 120 ? -2.61912 21.87398 14.02697 0.447 43.72393  ? 145  GLU A OE1  1 
ATOM   1885 O  OE1  B GLU A 1 120 ? 0.04977  24.87397 14.61868 0.553 46.29856  ? 145  GLU A OE1  1 
ATOM   1886 O  OE2  A GLU A 1 120 ? -1.05063 22.81111 12.79467 0.447 37.35020  ? 145  GLU A OE2  1 
ATOM   1887 O  OE2  B GLU A 1 120 ? -1.63708 25.29638 13.25347 0.553 47.00389  ? 145  GLU A OE2  1 
ATOM   1888 H  H    . GLU A 1 120 ? -1.64322 20.92013 16.03797 1.000 39.47561  ? 145  GLU A H    1 
ATOM   1889 H  HA   . GLU A 1 120 ? 0.33489  22.59376 15.93692 1.000 39.72279  ? 145  GLU A HA   1 
ATOM   1890 H  HB2  A GLU A 1 120 ? -2.37241 22.87934 16.48811 0.447 42.61128  ? 145  GLU A HB2  1 
ATOM   1891 H  HB2  B GLU A 1 120 ? -2.31224 23.00890 16.86040 0.553 42.60324  ? 145  GLU A HB2  1 
ATOM   1892 H  HB3  A GLU A 1 120 ? -1.42985 24.08987 16.90239 0.447 42.61128  ? 145  GLU A HB3  1 
ATOM   1893 H  HB3  B GLU A 1 120 ? -1.26608 24.20192 16.77291 0.553 42.60324  ? 145  GLU A HB3  1 
ATOM   1894 H  HG2  A GLU A 1 120 ? -2.35723 24.47723 14.80364 0.447 50.27445  ? 145  GLU A HG2  1 
ATOM   1895 H  HG2  B GLU A 1 120 ? -1.99684 22.83985 14.44645 0.553 49.63095  ? 145  GLU A HG2  1 
ATOM   1896 H  HG3  A GLU A 1 120 ? -0.77805 24.34817 14.68142 0.447 50.27445  ? 145  GLU A HG3  1 
ATOM   1897 H  HG3  B GLU A 1 120 ? -2.91092 24.01742 14.99708 0.553 49.63095  ? 145  GLU A HG3  1 
ATOM   1898 N  N    . ALA A 1 121 ? -0.22173 21.56348 18.85591 1.000 34.10519  ? 146  ALA A N    1 
ATOM   1899 C  CA   . ALA A 1 121 ? 0.27621  21.60347 20.22334 1.000 29.54534  ? 146  ALA A CA   1 
ATOM   1900 C  C    . ALA A 1 121 ? 1.78121  21.37947 20.29930 1.000 30.26614  ? 146  ALA A C    1 
ATOM   1901 O  O    . ALA A 1 121 ? 2.40816  21.79015 21.27568 1.000 32.64416  ? 146  ALA A O    1 
ATOM   1902 C  CB   . ALA A 1 121 ? -0.44612 20.55610 21.08482 1.000 32.70280  ? 146  ALA A CB   1 
ATOM   1903 H  H    . ALA A 1 121 ? -0.75660 20.91000 18.69316 1.000 41.25608  ? 146  ALA A H    1 
ATOM   1904 H  HA   . ALA A 1 121 ? 0.08597  22.48423 20.58246 1.000 35.78425  ? 146  ALA A HA   1 
ATOM   1905 H  HB1  . ALA A 1 121 ? -0.31040 19.67840 20.69479 1.000 39.57321  ? 146  ALA A HB1  1 
ATOM   1906 H  HB2  . ALA A 1 121 ? -0.08025 20.57916 21.98288 1.000 39.57321  ? 146  ALA A HB2  1 
ATOM   1907 H  HB3  . ALA A 1 121 ? -1.39309 20.76495 21.10798 1.000 39.57321  ? 146  ALA A HB3  1 
ATOM   1908 N  N    . ASN A 1 122 ? 2.37154  20.69117 19.33290 1.000 30.29014  ? 147  ASN A N    1 
ATOM   1909 C  CA   . ASN A 1 122 ? 3.80487  20.42423 19.37020 1.000 29.41793  ? 147  ASN A CA   1 
ATOM   1910 C  C    . ASN A 1 122 ? 4.61725  21.52907 18.72547 1.000 29.43322  ? 147  ASN A C    1 
ATOM   1911 O  O    . ASN A 1 122 ? 5.85606  21.47151 18.76355 1.000 22.77654  ? 147  ASN A O    1 
ATOM   1912 C  CB   . ASN A 1 122 ? 4.10744  19.09259 18.69231 1.000 29.00542  ? 147  ASN A CB   1 
ATOM   1913 C  CG   . ASN A 1 122 ? 3.33164  17.95415 19.31845 1.000 32.50299  ? 147  ASN A CG   1 
ATOM   1914 O  OD1  . ASN A 1 122 ? 3.34491  17.79289 20.52881 1.000 30.52459  ? 147  ASN A OD1  1 
ATOM   1915 N  ND2  . ASN A 1 122 ? 2.63254  17.18601 18.50651 1.000 26.52019  ? 147  ASN A ND2  1 
ATOM   1916 H  H    . ASN A 1 122 ? 1.96606  20.36856 18.64652 1.000 36.67801  ? 147  ASN A H    1 
ATOM   1917 H  HA   . ASN A 1 122 ? 4.08748  20.35025 20.29516 1.000 35.63136  ? 147  ASN A HA   1 
ATOM   1918 H  HB2  . ASN A 1 122 ? 3.86289  19.14794 17.75527 1.000 35.13634  ? 147  ASN A HB2  1 
ATOM   1919 H  HB3  . ASN A 1 122 ? 5.05399  18.89834 18.77723 1.000 35.13634  ? 147  ASN A HB3  1 
ATOM   1920 H  HD21 . ASN A 1 122 ? 2.63139  17.34286 17.66093 1.000 32.15408  ? 147  ASN A HD21 1 
ATOM   1921 H  HD22 . ASN A 1 122 ? 2.17766  16.52808 18.82243 1.000 32.15408  ? 147  ASN A HD22 1 
ATOM   1922 N  N    . GLY A 1 123 ? 3.95324  22.53076 18.16344 1.000 24.40212  ? 148  GLY A N    1 
ATOM   1923 C  CA   . GLY A 1 123 ? 4.59468  23.70788 17.64512 1.000 22.01415  ? 148  GLY A CA   1 
ATOM   1924 C  C    . GLY A 1 123 ? 5.59862  23.47370 16.53502 1.000 27.69761  ? 148  GLY A C    1 
ATOM   1925 O  O    . GLY A 1 123 ? 6.55790  24.23717 16.42682 1.000 20.90097  ? 148  GLY A O    1 
ATOM   1926 H  H    . GLY A 1 123 ? 3.09840  22.54574 18.07055 1.000 29.61239  ? 148  GLY A H    1 
ATOM   1927 H  HA2  . GLY A 1 123 ? 3.91153  24.30376 17.29997 1.000 26.74683  ? 148  GLY A HA2  1 
ATOM   1928 H  HA3  . GLY A 1 123 ? 5.06099  24.14947 18.37206 1.000 26.74683  ? 148  GLY A HA3  1 
ATOM   1929 N  N    . LEU A 1 124 ? 5.40733  22.45147 15.67889 1.000 18.81454  ? 149  LEU A N    1 
ATOM   1930 C  CA   . LEU A 1 124 ? 6.44784  22.12295 14.71462 1.000 22.84692  ? 149  LEU A CA   1 
ATOM   1931 C  C    . LEU A 1 124 ? 6.25059  22.73635 13.33187 1.000 21.85078  ? 149  LEU A C    1 
ATOM   1932 O  O    . LEU A 1 124 ? 7.13093  22.60682 12.48143 1.000 22.43404  ? 149  LEU A O    1 
ATOM   1933 C  CB   . LEU A 1 124 ? 6.56218  20.60276 14.56789 1.000 23.93677  ? 149  LEU A CB   1 
ATOM   1934 C  CG   . LEU A 1 124 ? 6.97029  19.98814 15.90582 1.000 27.02607  ? 149  LEU A CG   1 
ATOM   1935 C  CD1  . LEU A 1 124 ? 7.10002  18.50424 15.73486 1.000 23.81632  ? 149  LEU A CD1  1 
ATOM   1936 C  CD2  . LEU A 1 124 ? 8.30172  20.56466 16.37739 1.000 20.64547  ? 149  LEU A CD2  1 
ATOM   1937 H  H    . LEU A 1 124 ? 4.70428  21.95722 15.64675 1.000 22.90730  ? 149  LEU A H    1 
ATOM   1938 H  HA   . LEU A 1 124 ? 7.28548  22.46985 15.05947 1.000 27.74615  ? 149  LEU A HA   1 
ATOM   1939 H  HB2  . LEU A 1 124 ? 5.70538  20.23443 14.30120 1.000 29.05397  ? 149  LEU A HB2  1 
ATOM   1940 H  HB3  . LEU A 1 124 ? 7.23659  20.38787 13.90463 1.000 29.05397  ? 149  LEU A HB3  1 
ATOM   1941 H  HG   . LEU A 1 124 ? 6.29917  20.18811 16.57702 1.000 32.76113  ? 149  LEU A HG   1 
ATOM   1942 H  HD11 . LEU A 1 124 ? 6.26915  18.15368 15.37757 1.000 28.90943  ? 149  LEU A HD11 1 
ATOM   1943 H  HD12 . LEU A 1 124 ? 7.82807  18.31952 15.12109 1.000 28.90943  ? 149  LEU A HD12 1 
ATOM   1944 H  HD13 . LEU A 1 124 ? 7.28482  18.10188 16.59792 1.000 28.90943  ? 149  LEU A HD13 1 
ATOM   1945 H  HD21 . LEU A 1 124 ? 8.14180  21.42152 16.80298 1.000 25.10440  ? 149  LEU A HD21 1 
ATOM   1946 H  HD22 . LEU A 1 124 ? 8.70498  19.95078 17.01097 1.000 25.10440  ? 149  LEU A HD22 1 
ATOM   1947 H  HD23 . LEU A 1 124 ? 8.88518  20.67971 15.61108 1.000 25.10440  ? 149  LEU A HD23 1 
ATOM   1948 N  N    . LEU A 1 125 ? 5.14474  23.39916 13.06867 1.000 18.47286  ? 150  LEU A N    1 
ATOM   1949 C  CA   . LEU A 1 125 ? 4.89286  23.97946 11.75117 1.000 21.79000  ? 150  LEU A CA   1 
ATOM   1950 C  C    . LEU A 1 125 ? 4.47497  25.43202 11.89304 1.000 26.83336  ? 150  LEU A C    1 
ATOM   1951 O  O    . LEU A 1 125 ? 3.40332  25.82997 11.42283 1.000 24.70381  ? 150  LEU A O    1 
ATOM   1952 C  CB   . LEU A 1 125 ? 3.82192  23.19014 11.01725 1.000 23.08314  ? 150  LEU A CB   1 
ATOM   1953 C  CG   . LEU A 1 125 ? 4.14401  21.76572 10.60423 1.000 25.86491  ? 150  LEU A CG   1 
ATOM   1954 C  CD1  . LEU A 1 125 ? 2.87956  21.15795 9.98443  1.000 22.79271  ? 150  LEU A CD1  1 
ATOM   1955 C  CD2  . LEU A 1 125 ? 5.29857  21.77778 9.63333  1.000 31.18474  ? 150  LEU A CD2  1 
ATOM   1956 H  H    . LEU A 1 125 ? 4.51330  23.53223 13.63715 1.000 22.49727  ? 150  LEU A H    1 
ATOM   1957 H  HA   . LEU A 1 125 ? 5.70877  23.94138 11.22797 1.000 26.47784  ? 150  LEU A HA   1 
ATOM   1958 H  HB2  . LEU A 1 125 ? 3.04324  23.14366 11.59378 1.000 28.02961  ? 150  LEU A HB2  1 
ATOM   1959 H  HB3  . LEU A 1 125 ? 3.60475  23.67339 10.20472 1.000 28.02961  ? 150  LEU A HB3  1 
ATOM   1960 H  HG   . LEU A 1 125 ? 4.41123  21.21866 11.35935 1.000 31.36774  ? 150  LEU A HG   1 
ATOM   1961 H  HD11 . LEU A 1 125 ? 3.08011  20.26151 9.67285  1.000 27.68110  ? 150  LEU A HD11 1 
ATOM   1962 H  HD12 . LEU A 1 125 ? 2.18195  21.12582 10.65764 1.000 27.68110  ? 150  LEU A HD12 1 
ATOM   1963 H  HD13 . LEU A 1 125 ? 2.59556  21.71110 9.23993  1.000 27.68110  ? 150  LEU A HD13 1 
ATOM   1964 H  HD21 . LEU A 1 125 ? 5.07220  22.34602 8.88049  1.000 37.75154  ? 150  LEU A HD21 1 
ATOM   1965 H  HD22 . LEU A 1 125 ? 6.08580  22.12260 10.08307 1.000 37.75154  ? 150  LEU A HD22 1 
ATOM   1966 H  HD23 . LEU A 1 125 ? 5.46280  20.87230 9.32668  1.000 37.75154  ? 150  LEU A HD23 1 
ATOM   1967 N  N    . PRO A 1 126 ? 5.25735  26.22442 12.61233 1.000 19.01234  ? 151  PRO A N    1 
ATOM   1968 C  CA   . PRO A 1 126 ? 4.94085  27.64899 12.77051 1.000 26.91550  ? 151  PRO A CA   1 
ATOM   1969 C  C    . PRO A 1 126 ? 4.79365  28.32333 11.41080 1.000 31.91182  ? 151  PRO A C    1 
ATOM   1970 O  O    . PRO A 1 126 ? 5.69622  28.28401 10.56987 1.000 29.90168  ? 151  PRO A O    1 
ATOM   1971 C  CB   . PRO A 1 126 ? 6.13896  28.18713 13.55026 1.000 19.33458  ? 151  PRO A CB   1 
ATOM   1972 C  CG   . PRO A 1 126 ? 7.23261  27.20423 13.29861 1.000 24.50335  ? 151  PRO A CG   1 
ATOM   1973 C  CD   . PRO A 1 126 ? 6.56699  25.85400 13.17504 1.000 20.08898  ? 151  PRO A CD   1 
ATOM   1974 H  HA   . PRO A 1 126 ? 4.13114  27.77367 13.28986 1.000 32.62845  ? 151  PRO A HA   1 
ATOM   1975 H  HB2  . PRO A 1 126 ? 6.37979  29.06703 13.22060 1.000 23.53134  ? 151  PRO A HB2  1 
ATOM   1976 H  HB3  . PRO A 1 126 ? 5.92446  28.23409 14.49508 1.000 23.53134  ? 151  PRO A HB3  1 
ATOM   1977 H  HG2  . PRO A 1 126 ? 7.69454  27.43437 12.47730 1.000 29.73387  ? 151  PRO A HG2  1 
ATOM   1978 H  HG3  . PRO A 1 126 ? 7.85492  27.21206 14.04263 1.000 29.73387  ? 151  PRO A HG3  1 
ATOM   1979 H  HD2  . PRO A 1 126 ? 7.05765  25.27319 12.57270 1.000 24.43662  ? 151  PRO A HD2  1 
ATOM   1980 H  HD3  . PRO A 1 126 ? 6.47051  25.42824 14.04125 1.000 24.43662  ? 151  PRO A HD3  1 
ATOM   1981 N  N    . ASP A 1 127 ? 3.64281  28.94220 11.18958 1.000 31.35756  ? 152  ASP A N    1 
ATOM   1982 C  CA   . ASP A 1 127 ? 3.35344  29.62544 9.92986  1.000 38.22273  ? 152  ASP A CA   1 
ATOM   1983 C  C    . ASP A 1 127 ? 3.29189  28.65689 8.74822  1.000 36.74221  ? 152  ASP A C    1 
ATOM   1984 O  O    . ASP A 1 127 ? 3.45735  29.06439 7.59715  1.000 40.16175  ? 152  ASP A O    1 
ATOM   1985 C  CB   . ASP A 1 127 ? 4.38560  30.71436 9.62613  1.000 37.10876  ? 152  ASP A CB   1 
ATOM   1986 C  CG   . ASP A 1 127 ? 3.80654  31.85008 8.79168  1.000 50.71352  ? 152  ASP A CG   1 
ATOM   1987 O  OD1  . ASP A 1 127 ? 2.56406  31.88936 8.61369  1.000 56.43711  ? 152  ASP A OD1  1 
ATOM   1988 O  OD2  . ASP A 1 127 ? 4.60434  32.63786 8.23286  1.000 51.25667  ? 152  ASP A OD2  1 
ATOM   1989 H  H    . ASP A 1 127 ? 3.00169  28.98240 11.76137 1.000 37.95891  ? 152  ASP A H    1 
ATOM   1990 H  HA   . ASP A 1 127 ? 2.48454  30.04617 10.02424 1.000 46.19712  ? 152  ASP A HA   1 
ATOM   1991 H  HB2  . ASP A 1 127 ? 4.70728  31.08820 10.46139 1.000 44.86036  ? 152  ASP A HB2  1 
ATOM   1992 H  HB3  . ASP A 1 127 ? 5.12298  30.32333 9.13188  1.000 44.86036  ? 152  ASP A HB3  1 
ATOM   1993 N  N    . ASP A 1 128 ? 3.06722  27.37600 9.02638  1.000 26.91504  ? 153  ASP A N    1 
ATOM   1994 C  CA   . ASP A 1 128 ? 3.04139  26.32596 8.01963  1.000 25.19761  ? 153  ASP A CA   1 
ATOM   1995 C  C    . ASP A 1 128 ? 4.40606  26.10196 7.39099  1.000 24.03263  ? 153  ASP A C    1 
ATOM   1996 O  O    . ASP A 1 128 ? 4.51182  25.68616 6.22854  1.000 32.47507  ? 153  ASP A O    1 
ATOM   1997 C  CB   . ASP A 1 128 ? 2.02291  26.59444 6.92574  1.000 27.90479  ? 153  ASP A CB   1 
ATOM   1998 C  CG   . ASP A 1 128 ? 1.55030  25.32438 6.29592  1.000 27.69046  ? 153  ASP A CG   1 
ATOM   1999 O  OD1  . ASP A 1 128 ? 1.82391  24.26698 6.91834  1.000 26.99195  ? 153  ASP A OD1  1 
ATOM   2000 O  OD2  . ASP A 1 128 ? 0.85313  25.37482 5.24772  1.000 30.78473  ? 153  ASP A OD2  1 
ATOM   2001 H  H    . ASP A 1 128 ? 2.92190  27.08207 9.82142  1.000 32.62789  ? 153  ASP A H    1 
ATOM   2002 H  HA   . ASP A 1 128 ? 2.77874  25.50999 8.47362  1.000 30.56697  ? 153  ASP A HA   1 
ATOM   2003 H  HB2  . ASP A 1 128 ? 1.25600  27.05076 7.30592  1.000 33.81559  ? 153  ASP A HB2  1 
ATOM   2004 H  HB3  . ASP A 1 128 ? 2.42846  27.14440 6.23728  1.000 33.81559  ? 153  ASP A HB3  1 
ATOM   2005 N  N    . LYS A 1 129 ? 5.46409  26.37263 8.13925  1.000 22.85993  ? 154  LYS A N    1 
ATOM   2006 C  CA   . LYS A 1 129 ? 6.82947  26.19479 7.66782  1.000 21.15163  ? 154  LYS A CA   1 
ATOM   2007 C  C    . LYS A 1 129 ? 7.46737  25.08179 8.47521  1.000 19.48227  ? 154  LYS A C    1 
ATOM   2008 O  O    . LYS A 1 129 ? 7.38647  25.05980 9.70661  1.000 24.91866  ? 154  LYS A O    1 
ATOM   2009 C  CB   . LYS A 1 129 ? 7.61278  27.51416 7.73310  1.000 25.31492  ? 154  LYS A CB   1 
ATOM   2010 C  CG   . LYS A 1 129 ? 7.02521  28.59302 6.76472  1.000 21.02660  ? 154  LYS A CG   1 
ATOM   2011 C  CD   . LYS A 1 129 ? 7.68325  29.95289 6.91533  1.000 30.46158  ? 154  LYS A CD   1 
ATOM   2012 C  CE   . LYS A 1 129 ? 6.84852  31.04536 6.25933  1.000 39.39183  ? 154  LYS A CE   1 
ATOM   2013 N  NZ   . LYS A 1 129 ? 6.61153  30.77591 4.80516  1.000 36.78200  ? 154  LYS A NZ   1 
ATOM   2014 H  H    . LYS A 1 129 ? 5.41583  26.66848 8.94532  1.000 27.76176  ? 154  LYS A H    1 
ATOM   2015 H  HA   . LYS A 1 129 ? 6.84918  25.92195 6.73719  1.000 25.71180  ? 154  LYS A HA   1 
ATOM   2016 H  HB2  . LYS A 1 129 ? 7.57315  27.86378 8.63704  1.000 30.70775  ? 154  LYS A HB2  1 
ATOM   2017 H  HB3  . LYS A 1 129 ? 8.53495  27.34996 7.48104  1.000 30.70775  ? 154  LYS A HB3  1 
ATOM   2018 H  HG2  . LYS A 1 129 ? 7.15533  28.29901 5.84955  1.000 25.56176  ? 154  LYS A HG2  1 
ATOM   2019 H  HG3  . LYS A 1 129 ? 6.07852  28.69842 6.94789  1.000 25.56176  ? 154  LYS A HG3  1 
ATOM   2020 H  HD2  . LYS A 1 129 ? 7.77646  30.16328 7.85764  1.000 36.88374  ? 154  LYS A HD2  1 
ATOM   2021 H  HD3  . LYS A 1 129 ? 8.55536  29.93775 6.49094  1.000 36.88374  ? 154  LYS A HD3  1 
ATOM   2022 H  HE2  . LYS A 1 129 ? 5.98689  31.09743 6.70180  1.000 47.60004  ? 154  LYS A HE2  1 
ATOM   2023 H  HE3  . LYS A 1 129 ? 7.31371  31.89287 6.33817  1.000 47.60004  ? 154  LYS A HE3  1 
ATOM   2024 H  HZ1  . LYS A 1 129 ? 7.38911  30.70520 4.37801  1.000 44.46825  ? 154  LYS A HZ1  1 
ATOM   2025 H  HZ2  . LYS A 1 129 ? 6.15759  30.01679 4.70628  1.000 44.46825  ? 154  LYS A HZ2  1 
ATOM   2026 H  HZ3  . LYS A 1 129 ? 6.14339  31.44145 4.44461  1.000 44.46825  ? 154  LYS A HZ3  1 
ATOM   2027 N  N    . LEU A 1 130 ? 8.10085  24.15627 7.78976  1.000 21.64392  ? 155  LEU A N    1 
ATOM   2028 C  CA   . LEU A 1 130 ? 8.86080  23.09606 8.44640  1.000 16.34740  ? 155  LEU A CA   1 
ATOM   2029 C  C    . LEU A 1 130 ? 10.33077 23.42295 8.30440  1.000 19.32222  ? 155  LEU A C    1 
ATOM   2030 O  O    . LEU A 1 130 ? 10.84834 23.44000 7.17909  1.000 19.01745  ? 155  LEU A O    1 
ATOM   2031 C  CB   . LEU A 1 130 ? 8.54143  21.74048 7.81836  1.000 17.97026  ? 155  LEU A CB   1 
ATOM   2032 C  CG   . LEU A 1 130 ? 9.43263  20.62925 8.36227  1.000 17.44142  ? 155  LEU A CG   1 
ATOM   2033 C  CD1  . LEU A 1 130 ? 9.13179  20.47935 9.86048  1.000 25.41980  ? 155  LEU A CD1  1 
ATOM   2034 C  CD2  . LEU A 1 130 ? 9.24334  19.34616 7.68369  1.000 22.38553  ? 155  LEU A CD2  1 
ATOM   2035 H  H    . LEU A 1 130 ? 8.11010  24.11400 6.93085  1.000 26.30255  ? 155  LEU A H    1 
ATOM   2036 H  HA   . LEU A 1 130 ? 8.63574  23.06317 9.38936  1.000 19.94673  ? 155  LEU A HA   1 
ATOM   2037 H  HB2  . LEU A 1 130 ? 7.61884  21.51111 8.01098  1.000 21.89416  ? 155  LEU A HB2  1 
ATOM   2038 H  HB3  . LEU A 1 130 ? 8.67633  21.79552 6.85936  1.000 21.89416  ? 155  LEU A HB3  1 
ATOM   2039 H  HG   . LEU A 1 130 ? 10.35958 20.87016 8.20860  1.000 21.25955  ? 155  LEU A HG   1 
ATOM   2040 H  HD11 . LEU A 1 130 ? 9.52240  19.65083 10.17967 1.000 30.83360  ? 155  LEU A HD11 1 
ATOM   2041 H  HD12 . LEU A 1 130 ? 9.51680  21.23160 10.33671 1.000 30.83360  ? 155  LEU A HD12 1 
ATOM   2042 H  HD13 . LEU A 1 130 ? 8.17055  20.46313 9.98949  1.000 30.83360  ? 155  LEU A HD13 1 
ATOM   2043 H  HD21 . LEU A 1 130 ? 9.90013  18.71383 8.01489  1.000 27.19248  ? 155  LEU A HD21 1 
ATOM   2044 H  HD22 . LEU A 1 130 ? 8.34840  19.02050 7.86789  1.000 27.19248  ? 155  LEU A HD22 1 
ATOM   2045 H  HD23 . LEU A 1 130 ? 9.35898  19.47369 6.72909  1.000 27.19248  ? 155  LEU A HD23 1 
ATOM   2046 N  N    . THR A 1 131 ? 10.99608 23.70596 9.42389  1.000 23.58867  ? 156  THR A N    1 
ATOM   2047 C  CA   . THR A 1 131 ? 12.40715 24.04027 9.40150  1.000 18.61233  ? 156  THR A CA   1 
ATOM   2048 C  C    . THR A 1 131 ? 13.21676 22.90003 9.97837  1.000 19.58205  ? 156  THR A C    1 
ATOM   2049 O  O    . THR A 1 131 ? 13.01976 22.49975 11.12477 1.000 19.74590  ? 156  THR A O    1 
ATOM   2050 C  CB   . THR A 1 131 ? 12.70219 25.31913 10.17507 1.000 17.04661  ? 156  THR A CB   1 
ATOM   2051 O  OG1  . THR A 1 131 ? 11.96642 26.38639 9.55521  1.000 16.39309  ? 156  THR A OG1  1 
ATOM   2052 C  CG2  . THR A 1 131 ? 14.17425 25.62820 10.07767 1.000 26.25807  ? 156  THR A CG2  1 
ATOM   2053 H  H    . THR A 1 131 ? 10.64416 23.70903 10.20858 1.000 28.63625  ? 156  THR A H    1 
ATOM   2054 H  HA   . THR A 1 131 ? 12.66524 24.16899 8.47536  1.000 22.66464  ? 156  THR A HA   1 
ATOM   2055 H  HB   . THR A 1 131 ? 12.45581 25.23070 11.10909 1.000 20.78577  ? 156  THR A HB   1 
ATOM   2056 H  HG1  . THR A 1 131 ? 12.29193 26.55918 8.80037  1.000 20.00155  ? 156  THR A HG1  1 
ATOM   2057 H  HG21 . THR A 1 131 ? 14.34242 26.53750 10.37057 1.000 31.83952  ? 156  THR A HG21 1 
ATOM   2058 H  HG22 . THR A 1 131 ? 14.67907 25.01845 10.63827 1.000 31.83952  ? 156  THR A HG22 1 
ATOM   2059 H  HG23 . THR A 1 131 ? 14.47327 25.53272 9.15986  1.000 31.83952  ? 156  THR A HG23 1 
ATOM   2060 N  N    . LEU A 1 132 ? 14.11679 22.37767 9.16963  1.000 20.15289  ? 157  LEU A N    1 
ATOM   2061 C  CA   . LEU A 1 132 ? 14.93756 21.24935 9.54709  1.000 22.67393  ? 157  LEU A CA   1 
ATOM   2062 C  C    . LEU A 1 132 ? 16.36440 21.73133 9.65100  1.000 17.39928  ? 157  LEU A C    1 
ATOM   2063 O  O    . LEU A 1 132 ? 16.81268 22.58708 8.87055  1.000 23.94289  ? 157  LEU A O    1 
ATOM   2064 C  CB   . LEU A 1 132 ? 14.82040 20.12632 8.55244  1.000 19.64568  ? 157  LEU A CB   1 
ATOM   2065 C  CG   . LEU A 1 132 ? 13.36616 19.74945 8.29943  1.000 19.04636  ? 157  LEU A CG   1 
ATOM   2066 C  CD1  . LEU A 1 132 ? 13.27967 18.91120 7.08398  1.000 19.02803  ? 157  LEU A CD1  1 
ATOM   2067 C  CD2  . LEU A 1 132 ? 12.76162 19.05421 9.50512  1.000 19.64702  ? 157  LEU A CD2  1 
ATOM   2068 H  H    . LEU A 1 132 ? 14.27378 22.66838 8.37562  1.000 24.51331  ? 157  LEU A H    1 
ATOM   2069 H  HA   . LEU A 1 132 ? 14.65954 20.88953 10.40390 1.000 27.53856  ? 157  LEU A HA   1 
ATOM   2070 H  HB2  . LEU A 1 132 ? 15.21550 20.40265 7.71075  1.000 23.90467  ? 157  LEU A HB2  1 
ATOM   2071 H  HB3  . LEU A 1 132 ? 15.28314 19.34602 8.89581  1.000 23.90467  ? 157  LEU A HB3  1 
ATOM   2072 H  HG   . LEU A 1 132 ? 12.84085 20.55181 8.15392  1.000 23.18548  ? 157  LEU A HG   1 
ATOM   2073 H  HD11 . LEU A 1 132 ? 13.57359 19.43154 6.31994  1.000 23.16348  ? 157  LEU A HD11 1 
ATOM   2074 H  HD12 . LEU A 1 132 ? 13.85035 18.13468 7.19463  1.000 23.16348  ? 157  LEU A HD12 1 
ATOM   2075 H  HD13 . LEU A 1 132 ? 12.35967 18.63044 6.95880  1.000 23.16348  ? 157  LEU A HD13 1 
ATOM   2076 H  HD21 . LEU A 1 132 ? 11.84272 18.81668 9.30486  1.000 23.90626  ? 157  LEU A HD21 1 
ATOM   2077 H  HD22 . LEU A 1 132 ? 13.27526 18.25453 9.69899  1.000 23.90626  ? 157  LEU A HD22 1 
ATOM   2078 H  HD23 . LEU A 1 132 ? 12.78943 19.65735 10.26430 1.000 23.90626  ? 157  LEU A HD23 1 
ATOM   2079 N  N    . PHE A 1 133 ? 17.05786 21.19683 10.62938 1.000 15.84714  ? 158  PHE A N    1 
ATOM   2080 C  CA   . PHE A 1 133 ? 18.49992 21.35624 10.76148 1.000 20.62472  ? 158  PHE A CA   1 
ATOM   2081 C  C    . PHE A 1 133 ? 19.18848 20.02800 10.48434 1.000 25.12109  ? 158  PHE A C    1 
ATOM   2082 O  O    . PHE A 1 133 ? 18.69624 18.96940 10.89226 1.000 22.33676  ? 158  PHE A O    1 
ATOM   2083 C  CB   . PHE A 1 133 ? 18.87225 21.82225 12.14977 1.000 22.81493  ? 158  PHE A CB   1 
ATOM   2084 C  CG   . PHE A 1 133 ? 18.18041 23.03467 12.56938 1.000 25.46726  ? 158  PHE A CG   1 
ATOM   2085 C  CD1  . PHE A 1 133 ? 18.58049 24.27073 12.11775 1.000 29.62821  ? 158  PHE A CD1  1 
ATOM   2086 C  CD2  . PHE A 1 133 ? 17.10821 22.94902 13.41999 1.000 28.62029  ? 158  PHE A CD2  1 
ATOM   2087 C  CE1  . PHE A 1 133 ? 17.92105 25.39860 12.52461 1.000 31.97392  ? 158  PHE A CE1  1 
ATOM   2088 C  CE2  . PHE A 1 133 ? 16.45155 24.07156 13.83770 1.000 30.88687  ? 158  PHE A CE2  1 
ATOM   2089 C  CZ   . PHE A 1 133 ? 16.83981 25.29134 13.38421 1.000 27.89495  ? 158  PHE A CZ   1 
ATOM   2090 H  H    . PHE A 1 133 ? 16.70981 20.71953 11.25440 1.000 19.34642  ? 158  PHE A H    1 
ATOM   2091 H  HA   . PHE A 1 133 ? 18.80868 22.01452 10.11942 1.000 25.07951  ? 158  PHE A HA   1 
ATOM   2092 H  HB2  . PHE A 1 133 ? 18.65165 21.12159 12.78326 1.000 27.70777  ? 158  PHE A HB2  1 
ATOM   2093 H  HB3  . PHE A 1 133 ? 19.82509 22.00243 12.17287 1.000 27.70777  ? 158  PHE A HB3  1 
ATOM   2094 H  HD1  . PHE A 1 133 ? 19.30126 24.34015 11.53417 1.000 35.88370  ? 158  PHE A HD1  1 
ATOM   2095 H  HD2  . PHE A 1 133 ? 16.82407 22.11468 13.71672 1.000 34.67419  ? 158  PHE A HD2  1 
ATOM   2096 H  HE1  . PHE A 1 133 ? 18.19777 26.23443 12.22509 1.000 38.69855  ? 158  PHE A HE1  1 
ATOM   2097 H  HE2  . PHE A 1 133 ? 15.73958 24.00062 14.43181 1.000 37.39409  ? 158  PHE A HE2  1 
ATOM   2098 H  HZ   . PHE A 1 133 ? 16.37998 26.05454 13.65063 1.000 33.80378  ? 158  PHE A HZ   1 
ATOM   2099 N  N    . CYS A 1 134 ? 20.31600 20.07382 9.80280  1.000 18.49743  ? 159  CYS A N    1 
ATOM   2100 C  CA   A CYS A 1 134 ? 21.16150 18.89995 9.62336  0.726 24.97827  ? 159  CYS A CA   1 
ATOM   2101 C  CA   B CYS A 1 134 ? 21.15755 18.89664 9.64002  0.274 24.79995  ? 159  CYS A CA   1 
ATOM   2102 C  C    . CYS A 1 134 ? 22.57216 19.29680 10.02406 1.000 27.43652  ? 159  CYS A C    1 
ATOM   2103 O  O    . CYS A 1 134 ? 23.14220 20.23812 9.45147  1.000 24.44022  ? 159  CYS A O    1 
ATOM   2104 C  CB   A CYS A 1 134 ? 21.13650 18.38941 8.18739  0.726 24.32401  ? 159  CYS A CB   1 
ATOM   2105 C  CB   B CYS A 1 134 ? 21.11090 18.32805 8.22991  0.274 24.09872  ? 159  CYS A CB   1 
ATOM   2106 S  SG   A CYS A 1 134 ? 22.21750 16.94198 7.90964  0.726 20.58395  ? 159  CYS A SG   1 
ATOM   2107 S  SG   B CYS A 1 134 ? 22.27406 19.04512 7.11981  0.274 30.12846  ? 159  CYS A SG   1 
ATOM   2108 H  H    . CYS A 1 134 ? 20.62009 20.78515 9.42713  1.000 22.52676  ? 159  CYS A H    1 
ATOM   2109 H  HA   . CYS A 1 134 ? 20.84894 18.17862 10.19160 1.000 30.08979  ? 159  CYS A HA   1 
ATOM   2110 H  HB2  A CYS A 1 134 ? 20.22902 18.13011 7.96345  0.726 29.51866  ? 159  CYS A HB2  1 
ATOM   2111 H  HB2  B CYS A 1 134 ? 21.29454 17.37659 8.27364  0.274 29.24831  ? 159  CYS A HB2  1 
ATOM   2112 H  HB3  A CYS A 1 134 ? 21.43362 19.09994 7.59767  0.726 29.51866  ? 159  CYS A HB3  1 
ATOM   2113 H  HB3  B CYS A 1 134 ? 20.22496 18.47850 7.86471  0.274 29.24831  ? 159  CYS A HB3  1 
ATOM   2114 H  HG   A CYS A 1 134 ? 21.92120 16.07800 8.68794  0.726 25.03058  ? 159  CYS A HG   1 
ATOM   2115 H  HG   B CYS A 1 134 ? 23.38389 18.80014 7.50486  0.274 36.48400  ? 159  CYS A HG   1 
ATOM   2116 N  N    . GLU A 1 135 ? 23.12209 18.60891 11.00361 1.000 23.87242  ? 160  GLU A N    1 
ATOM   2117 C  CA   . GLU A 1 135 ? 24.50509 18.80599 11.39745 1.000 25.70234  ? 160  GLU A CA   1 
ATOM   2118 C  C    . GLU A 1 135 ? 25.25715 17.58285 10.88557 1.000 27.31420  ? 160  GLU A C    1 
ATOM   2119 O  O    . GLU A 1 135 ? 24.97293 16.46120 11.31032 1.000 24.45402  ? 160  GLU A O    1 
ATOM   2120 C  CB   . GLU A 1 135 ? 24.63665 18.99361 12.90835 1.000 25.95555  ? 160  GLU A CB   1 
ATOM   2121 C  CG   . GLU A 1 135 ? 25.91261 18.39433 13.48997 1.000 37.26003  ? 160  GLU A CG   1 
ATOM   2122 C  CD   . GLU A 1 135 ? 26.00013 18.49218 15.02817 1.000 43.54938  ? 160  GLU A CD   1 
ATOM   2123 O  OE1  . GLU A 1 135 ? 25.57030 19.52933 15.60357 1.000 41.48122  ? 160  GLU A OE1  1 
ATOM   2124 O  OE2  . GLU A 1 135 ? 26.45639 17.49480 15.65128 1.000 38.72818  ? 160  GLU A OE2  1 
ATOM   2125 H  H    . GLU A 1 135 ? 22.70881 18.01164 11.46411 1.000 28.97675  ? 160  GLU A H    1 
ATOM   2126 H  HA   . GLU A 1 135 ? 24.88562 19.60615 11.00268 1.000 31.17265  ? 160  GLU A HA   1 
ATOM   2127 H  HB2  . GLU A 1 135 ? 24.63792 19.94322 13.10616 1.000 31.47650  ? 160  GLU A HB2  1 
ATOM   2128 H  HB3  . GLU A 1 135 ? 23.88273 18.56518 13.34304 1.000 31.47650  ? 160  GLU A HB3  1 
ATOM   2129 H  HG2  . GLU A 1 135 ? 25.95397 17.45526 13.25052 1.000 45.04188  ? 160  GLU A HG2  1 
ATOM   2130 H  HG3  . GLU A 1 135 ? 26.67570 18.86502 13.11978 1.000 45.04188  ? 160  GLU A HG3  1 
ATOM   2131 N  N    . VAL A 1 136 ? 26.22299 17.81469 9.99898  1.000 29.42584  ? 161  VAL A N    1 
ATOM   2132 C  CA   . VAL A 1 136 ? 27.05262 16.77637 9.41805  1.000 27.44922  ? 161  VAL A CA   1 
ATOM   2133 C  C    . VAL A 1 136 ? 28.40771 16.81432 10.08765 1.000 26.18852  ? 161  VAL A C    1 
ATOM   2134 O  O    . VAL A 1 136 ? 29.05020 17.86746 10.13231 1.000 28.85179  ? 161  VAL A O    1 
ATOM   2135 C  CB   . VAL A 1 136 ? 27.19305 16.99187 7.90150  1.000 24.49417  ? 161  VAL A CB   1 
ATOM   2136 C  CG1  . VAL A 1 136 ? 28.08052 15.90388 7.24365  1.000 24.89641  ? 161  VAL A CG1  1 
ATOM   2137 C  CG2  . VAL A 1 136 ? 25.84427 17.06474 7.26617  1.000 28.98788  ? 161  VAL A CG2  1 
ATOM   2138 H  H    . VAL A 1 136 ? 26.42045 18.60024 9.70999  1.000 35.64085  ? 161  VAL A H    1 
ATOM   2139 H  HA   . VAL A 1 136 ? 26.65422 15.90727 9.58187  1.000 33.26891  ? 161  VAL A HA   1 
ATOM   2140 H  HB   . VAL A 1 136 ? 27.64364 17.83731 7.74949  1.000 29.72285  ? 161  VAL A HB   1 
ATOM   2141 H  HG11 . VAL A 1 136 ? 28.46522 15.34734 7.93874  1.000 30.20553  ? 161  VAL A HG11 1 
ATOM   2142 H  HG12 . VAL A 1 136 ? 27.53240 15.36386 6.65302  1.000 30.20553  ? 161  VAL A HG12 1 
ATOM   2143 H  HG13 . VAL A 1 136 ? 28.78620 16.33567 6.73721  1.000 30.20553  ? 161  VAL A HG13 1 
ATOM   2144 H  HG21 . VAL A 1 136 ? 25.22356 16.52475 7.78001  1.000 35.11530  ? 161  VAL A HG21 1 
ATOM   2145 H  HG22 . VAL A 1 136 ? 25.54929 17.98875 7.25644  1.000 35.11530  ? 161  VAL A HG22 1 
ATOM   2146 H  HG23 . VAL A 1 136 ? 25.90392 16.72698 6.35883  1.000 35.11530  ? 161  VAL A HG23 1 
ATOM   2147 N  N    . SER A 1 137 ? 28.87466 15.65615 10.54985 1.000 28.24868  ? 162  SER A N    1 
ATOM   2148 C  CA   . SER A 1 137 ? 30.17593 15.52558 11.18972 1.000 30.70210  ? 162  SER A CA   1 
ATOM   2149 C  C    . SER A 1 137 ? 31.05261 14.62476 10.32401 1.000 28.81998  ? 162  SER A C    1 
ATOM   2150 O  O    . SER A 1 137 ? 30.95198 13.39239 10.39435 1.000 25.04097  ? 162  SER A O    1 
ATOM   2151 C  CB   . SER A 1 137 ? 30.03381 14.95282 12.60991 1.000 29.88543  ? 162  SER A CB   1 
ATOM   2152 O  OG   . SER A 1 137 ? 29.26944 15.81129 13.42911 1.000 29.00665  ? 162  SER A OG   1 
ATOM   2153 H  H    . SER A 1 137 ? 28.44204 14.91446 10.50143 1.000 34.22826  ? 162  SER A H    1 
ATOM   2154 H  HA   . SER A 1 137 ? 30.59077 16.40089 11.24101 1.000 37.17237  ? 162  SER A HA   1 
ATOM   2155 H  HB2  . SER A 1 137 ? 29.59230 14.09063 12.55896 1.000 36.19236  ? 162  SER A HB2  1 
ATOM   2156 H  HB3  . SER A 1 137 ? 30.91687 14.85092 12.99814 1.000 36.19236  ? 162  SER A HB3  1 
ATOM   2157 H  HG   . SER A 1 137 ? 28.51219 15.93550 13.08741 1.000 35.13783  ? 162  SER A HG   1 
ATOM   2158 N  N    . VAL A 1 138 ? 31.93302 15.23868 9.54886  1.000 26.87530  ? 163  VAL A N    1 
ATOM   2159 C  CA   . VAL A 1 138 ? 32.78446 14.52509 8.61306  1.000 26.75460  ? 163  VAL A CA   1 
ATOM   2160 C  C    . VAL A 1 138 ? 34.10363 14.16580 9.27310  1.000 32.70683  ? 163  VAL A C    1 
ATOM   2161 O  O    . VAL A 1 138 ? 34.83163 15.03463 9.76383  1.000 26.61113  ? 163  VAL A O    1 
ATOM   2162 C  CB   . VAL A 1 138 ? 33.01928 15.34182 7.33328  1.000 32.72161  ? 163  VAL A CB   1 
ATOM   2163 C  CG1  . VAL A 1 138 ? 33.94417 14.57202 6.38995  1.000 38.83229  ? 163  VAL A CG1  1 
ATOM   2164 C  CG2  . VAL A 1 138 ? 31.70232 15.68046 6.65486  1.000 32.19562  ? 163  VAL A CG2  1 
ATOM   2165 H  H    . VAL A 1 138 ? 32.05867 16.08945 9.54690  1.000 32.58021  ? 163  VAL A H    1 
ATOM   2166 H  HA   . VAL A 1 138 ? 32.34025 13.69440 8.38169  1.000 32.43537  ? 163  VAL A HA   1 
ATOM   2167 H  HB   . VAL A 1 138 ? 33.44690 16.18125 7.56439  1.000 39.59578  ? 163  VAL A HB   1 
ATOM   2168 H  HG11 . VAL A 1 138 ? 33.97385 15.02855 5.53462  1.000 46.92859  ? 163  VAL A HG11 1 
ATOM   2169 H  HG12 . VAL A 1 138 ? 34.83273 14.53748 6.77746  1.000 46.92859  ? 163  VAL A HG12 1 
ATOM   2170 H  HG13 . VAL A 1 138 ? 33.59901 13.67305 6.27328  1.000 46.92859  ? 163  VAL A HG13 1 
ATOM   2171 H  HG21 . VAL A 1 138 ? 30.97441 15.29868 7.16992  1.000 38.96459  ? 163  VAL A HG21 1 
ATOM   2172 H  HG22 . VAL A 1 138 ? 31.60754 16.64491 6.61286  1.000 38.96459  ? 163  VAL A HG22 1 
ATOM   2173 H  HG23 . VAL A 1 138 ? 31.70396 15.30893 5.75883  1.000 38.96459  ? 163  VAL A HG23 1 
ATOM   2174 N  N    . VAL A 1 139 ? 34.41020 12.87634 9.25890  1.000 29.31667  ? 164  VAL A N    1 
ATOM   2175 C  CA   . VAL A 1 139 ? 35.66134 12.34556 9.76827  1.000 34.50604  ? 164  VAL A CA   1 
ATOM   2176 C  C    . VAL A 1 139 ? 36.73695 12.54625 8.71108  1.000 36.00911  ? 164  VAL A C    1 
ATOM   2177 O  O    . VAL A 1 139 ? 36.58847 12.10739 7.56711  1.000 44.18371  ? 164  VAL A O    1 
ATOM   2178 C  CB   . VAL A 1 139 ? 35.50003 10.86360 10.12755 1.000 40.22505  ? 164  VAL A CB   1 
ATOM   2179 C  CG1  . VAL A 1 139 ? 36.67597 10.37647 10.92262 1.000 45.81814  ? 164  VAL A CG1  1 
ATOM   2180 C  CG2  . VAL A 1 139 ? 34.19903 10.65319 10.89841 1.000 43.43993  ? 164  VAL A CG2  1 
ATOM   2181 H  H    . VAL A 1 139 ? 33.88959 12.26680 8.94740  1.000 35.50984  ? 164  VAL A H    1 
ATOM   2182 H  HA   . VAL A 1 139 ? 35.92925 12.83146 10.56390 1.000 41.73709  ? 164  VAL A HA   1 
ATOM   2183 H  HB   . VAL A 1 139 ? 35.46183 10.34153 9.31093  1.000 48.59990  ? 164  VAL A HB   1 
ATOM   2184 H  HG11 . VAL A 1 139 ? 36.54824 9.43815  11.13272 1.000 55.31161  ? 164  VAL A HG11 1 
ATOM   2185 H  HG12 . VAL A 1 139 ? 37.48245 10.49069 10.39588 1.000 55.31161  ? 164  VAL A HG12 1 
ATOM   2186 H  HG13 . VAL A 1 139 ? 36.73957 10.89304 11.74116 1.000 55.31161  ? 164  VAL A HG13 1 
ATOM   2187 H  HG21 . VAL A 1 139 ? 34.11479 9.71388  11.12533 1.000 52.45776  ? 164  VAL A HG21 1 
ATOM   2188 H  HG22 . VAL A 1 139 ? 34.22112 11.18819 11.70723 1.000 52.45776  ? 164  VAL A HG22 1 
ATOM   2189 H  HG23 . VAL A 1 139 ? 33.45387 10.92694 10.34099 1.000 52.45776  ? 164  VAL A HG23 1 
ATOM   2190 N  N    . GLN A 1 140 ? 37.81716 13.20449 9.08468  1.000 31.12873  ? 165  GLN A N    1 
ATOM   2191 C  CA   . GLN A 1 140 ? 38.86244 13.51925 8.12753  1.000 42.02984  ? 165  GLN A CA   1 
ATOM   2192 C  C    . GLN A 1 140 ? 39.90013 12.41016 8.06072  1.000 39.54092  ? 165  GLN A C    1 
ATOM   2193 O  O    . GLN A 1 140 ? 40.26739 11.82744 9.07327  1.000 38.08430  ? 165  GLN A O    1 
ATOM   2194 C  CB   . GLN A 1 140 ? 39.53567 14.83462 8.49077  1.000 41.72557  ? 165  GLN A CB   1 
ATOM   2195 C  CG   . GLN A 1 140 ? 38.51025 15.91916 8.77381  1.000 46.17234  ? 165  GLN A CG   1 
ATOM   2196 C  CD   . GLN A 1 140 ? 38.91185 17.22942 8.14620  1.000 54.31304  ? 165  GLN A CD   1 
ATOM   2197 O  OE1  . GLN A 1 140 ? 39.88855 17.87133 8.58741  1.000 62.51883  ? 165  GLN A OE1  1 
ATOM   2198 N  NE2  . GLN A 1 140 ? 38.15188 17.66019 7.13338  1.000 59.13770  ? 165  GLN A NE2  1 
ATOM   2199 H  H    . GLN A 1 140 ? 37.96942 13.47995 9.88502  1.000 35.70526  ? 165  GLN A H    1 
ATOM   2200 H  HA   . GLN A 1 140 ? 38.46508 13.60383 7.24670  1.000 50.76566  ? 165  GLN A HA   1 
ATOM   2201 H  HB2  . GLN A 1 140 ? 40.07715 14.70964 9.28580  1.000 50.40053  ? 165  GLN A HB2  1 
ATOM   2202 H  HB3  . GLN A 1 140 ? 40.09312 15.12504 7.75198  1.000 50.40053  ? 165  GLN A HB3  1 
ATOM   2203 H  HG2  . GLN A 1 140 ? 37.65225 15.65428 8.40698  1.000 55.73665  ? 165  GLN A HG2  1 
ATOM   2204 H  HG3  . GLN A 1 140 ? 38.43550 16.04898 9.73218  1.000 55.73665  ? 165  GLN A HG3  1 
ATOM   2205 H  HE21 . GLN A 1 140 ? 37.47647 17.19501 6.87447  1.000 71.29508  ? 165  GLN A HE21 1 
ATOM   2206 H  HE22 . GLN A 1 140 ? 38.33862 18.40236 6.74106  1.000 71.29508  ? 165  GLN A HE22 1 
ATOM   2207 N  N    . ASP A 1 141 ? 40.35609 12.12223 6.85282  1.000 46.60377  ? 166  ASP A N    1 
ATOM   2208 C  CA   . ASP A 1 141 ? 41.32878 11.06828 6.62421  1.000 48.70472  ? 166  ASP A CA   1 
ATOM   2209 C  C    . ASP A 1 141 ? 42.72425 11.56869 6.98361  1.000 50.13205  ? 166  ASP A C    1 
ATOM   2210 O  O    . ASP A 1 141 ? 43.00087 12.75249 6.82098  1.000 42.07387  ? 166  ASP A O    1 
ATOM   2211 C  CB   . ASP A 1 141 ? 41.27964 10.60716 5.16006  1.000 50.23362  ? 166  ASP A CB   1 
ATOM   2212 C  CG   . ASP A 1 141 ? 39.92511 9.99975  4.77205  1.000 62.28774  ? 166  ASP A CG   1 
ATOM   2213 O  OD1  . ASP A 1 141 ? 39.53762 8.96512  5.36601  1.000 65.10847  ? 166  ASP A OD1  1 
ATOM   2214 O  OD2  . ASP A 1 141 ? 39.25764 10.55287 3.86168  1.000 51.79458  ? 166  ASP A OD2  1 
ATOM   2215 H  H    . ASP A 1 141 ? 40.11332 12.53023 6.13574  1.000 56.25437  ? 166  ASP A H    1 
ATOM   2216 H  HA   . ASP A 1 141 ? 41.12529 10.29854 7.17829  1.000 58.77551  ? 166  ASP A HA   1 
ATOM   2217 H  HB2  . ASP A 1 141 ? 41.44223 11.36983 4.58318  1.000 60.61019  ? 166  ASP A HB2  1 
ATOM   2218 H  HB3  . ASP A 1 141 ? 41.96208 9.93256  5.01838  1.000 60.61019  ? 166  ASP A HB3  1 
ATOM   2219 N  N    . LYS B 2 2   ? 6.10177  1.74907  15.81134 1.000 57.91867  ? 1364 LYS B N    1 
ATOM   2220 C  CA   . LYS B 2 2   ? 5.07415  0.88130  16.38276 1.000 65.57250  ? 1364 LYS B CA   1 
ATOM   2221 C  C    . LYS B 2 2   ? 3.95912  1.75783  16.97678 1.000 69.92080  ? 1364 LYS B C    1 
ATOM   2222 O  O    . LYS B 2 2   ? 3.25726  1.37002  17.92312 1.000 74.30593  ? 1364 LYS B O    1 
ATOM   2223 C  CB   . LYS B 2 2   ? 5.69859  -0.03675 17.42625 1.000 64.83621  ? 1364 LYS B CB   1 
ATOM   2224 H  HA   . LYS B 2 2   ? 4.67661  0.30529  15.71114 1.000 79.01684  ? 1364 LYS B HA   1 
ATOM   2225 N  N    . GLY B 2 3   ? 3.78095  2.93156  16.36818 1.000 60.69397  ? 1365 GLY B N    1 
ATOM   2226 C  CA   . GLY B 2 3   ? 3.05628  4.02854  16.97077 1.000 58.80567  ? 1365 GLY B CA   1 
ATOM   2227 C  C    . GLY B 2 3   ? 3.96760  5.09443  17.52675 1.000 56.86803  ? 1365 GLY B C    1 
ATOM   2228 O  O    . GLY B 2 3   ? 3.48294  6.13313  18.00653 1.000 54.55843  ? 1365 GLY B O    1 
ATOM   2229 H  H    . GLY B 2 3   ? 4.08232  3.11340  15.58351 1.000 73.16261  ? 1365 GLY B H    1 
ATOM   2230 H  HA2  . GLY B 2 3   ? 2.48202  4.43602  16.30362 1.000 70.89665  ? 1365 GLY B HA2  1 
ATOM   2231 H  HA3  . GLY B 2 3   ? 2.50744  3.68865  17.69475 1.000 70.89665  ? 1365 GLY B HA3  1 
ATOM   2232 N  N    . SER B 2 4   ? 5.27558  4.86719  17.46023 1.000 50.67921  ? 1366 SER B N    1 
ATOM   2233 C  CA   . SER B 2 4   ? 6.24002  5.75039  18.08203 1.000 34.76882  ? 1366 SER B CA   1 
ATOM   2234 C  C    . SER B 2 4   ? 6.32263  7.04823  17.31250 1.000 34.94911  ? 1366 SER B C    1 
ATOM   2235 O  O    . SER B 2 4   ? 6.12226  7.09113  16.09770 1.000 35.05287  ? 1366 SER B O    1 
ATOM   2236 C  CB   . SER B 2 4   ? 7.60915  5.07323  18.13328 1.000 47.28740  ? 1366 SER B CB   1 
ATOM   2237 O  OG   . SER B 2 4   ? 7.52859  3.84672  18.85660 1.000 56.21776  ? 1366 SER B OG   1 
ATOM   2238 H  H    . SER B 2 4   ? 5.63071  4.19752  17.05402 1.000 61.14490  ? 1366 SER B H    1 
ATOM   2239 H  HA   . SER B 2 4   ? 5.97303  5.95366  18.99214 1.000 42.05243  ? 1366 SER B HA   1 
ATOM   2240 H  HB2  . SER B 2 4   ? 7.90697  4.88967  17.22857 1.000 57.07473  ? 1366 SER B HB2  1 
ATOM   2241 H  HB3  . SER B 2 4   ? 8.23893  5.66289  18.57666 1.000 57.07473  ? 1366 SER B HB3  1 
ATOM   2242 H  HG   . SER B 2 4   ? 8.29475  3.51339  18.94318 1.000 67.79116  ? 1366 SER B HG   1 
ATOM   2243 N  N    . VAL B 2 5   ? 6.62076  8.12441  18.03296 1.000 24.15119  ? 1367 VAL B N    1 
ATOM   2244 C  CA   . VAL B 2 5   ? 6.81600  9.40421  17.35451 1.000 21.96029  ? 1367 VAL B CA   1 
ATOM   2245 C  C    . VAL B 2 5   ? 7.92983  9.30640  16.34253 1.000 26.19864  ? 1367 VAL B C    1 
ATOM   2246 O  O    . VAL B 2 5   ? 7.90628  9.99617  15.30808 1.000 22.02308  ? 1367 VAL B O    1 
ATOM   2247 C  CB   . VAL B 2 5   ? 7.08463  10.51568 18.38359 1.000 22.32004  ? 1367 VAL B CB   1 
ATOM   2248 C  CG1  . VAL B 2 5   ? 7.17562  11.82683 17.67110 1.000 27.95565  ? 1367 VAL B CG1  1 
ATOM   2249 C  CG2  . VAL B 2 5   ? 5.98448  10.49369 19.48563 1.000 30.26888  ? 1367 VAL B CG2  1 
ATOM   2250 H  H    . VAL B 2 5   ? 6.71315  8.14222  18.88779 1.000 28.13352  ? 1367 VAL B H    1 
ATOM   2251 H  HA   . VAL B 2 5   ? 6.00093  9.62825  16.87872 1.000 24.70312  ? 1367 VAL B HA   1 
ATOM   2252 H  HB   . VAL B 2 5   ? 7.92974  10.37631 18.83885 1.000 27.11390  ? 1367 VAL B HB   1 
ATOM   2253 H  HG11 . VAL B 2 5   ? 6.86884  11.71205 16.75808 1.000 33.87662  ? 1367 VAL B HG11 1 
ATOM   2254 H  HG12 . VAL B 2 5   ? 6.61702  12.47441 18.12881 1.000 33.87662  ? 1367 VAL B HG12 1 
ATOM   2255 H  HG13 . VAL B 2 5   ? 8.09868  12.12491 17.67489 1.000 33.87662  ? 1367 VAL B HG13 1 
ATOM   2256 H  HG21 . VAL B 2 5   ? 6.02215  11.32377 19.98607 1.000 36.65250  ? 1367 VAL B HG21 1 
ATOM   2257 H  HG22 . VAL B 2 5   ? 5.11618  10.40121 19.06324 1.000 36.65250  ? 1367 VAL B HG22 1 
ATOM   2258 H  HG23 . VAL B 2 5   ? 6.14583  9.74271  20.07799 1.000 36.65250  ? 1367 VAL B HG23 1 
ATOM   2259 N  N    . GLN B 2 6   ? 8.93938  8.47169  16.62402 1.000 22.25048  ? 1368 GLN B N    1 
ATOM   2260 C  CA   . GLN B 2 6   ? 10.13630 8.39737  15.80533 1.000 18.86477  ? 1368 GLN B CA   1 
ATOM   2261 C  C    . GLN B 2 6   ? 10.61713 6.95545  15.80997 1.000 29.04280  ? 1368 GLN B C    1 
ATOM   2262 O  O    . GLN B 2 6   ? 10.30201 6.16402  16.71041 1.000 22.27021  ? 1368 GLN B O    1 
ATOM   2263 C  CB   . GLN B 2 6   ? 11.25863 9.29600  16.28997 1.000 22.37797  ? 1368 GLN B CB   1 
ATOM   2264 C  CG   . GLN B 2 6   ? 10.98893 10.79828 16.32629 1.000 18.67473  ? 1368 GLN B CG   1 
ATOM   2265 C  CD   . GLN B 2 6   ? 12.17763 11.59948 16.80108 1.000 19.91710  ? 1368 GLN B CD   1 
ATOM   2266 O  OE1  . GLN B 2 6   ? 12.56301 11.50096 17.95005 1.000 18.67271  ? 1368 GLN B OE1  1 
ATOM   2267 N  NE2  . GLN B 2 6   ? 12.76994 12.39901 15.90457 1.000 18.51668  ? 1368 GLN B NE2  1 
ATOM   2268 H  H    . GLN B 2 6   ? 8.94684  7.93407  17.29522 1.000 27.03043  ? 1368 GLN B H    1 
ATOM   2269 H  HA   . GLN B 2 6   ? 9.90603  8.67822  14.90588 1.000 20.98850  ? 1368 GLN B HA   1 
ATOM   2270 H  HB2  . GLN B 2 6   ? 11.48370 9.02939  17.19505 1.000 27.18340  ? 1368 GLN B HB2  1 
ATOM   2271 H  HB3  . GLN B 2 6   ? 12.02093 9.16185  15.70534 1.000 27.18340  ? 1368 GLN B HB3  1 
ATOM   2272 H  HG2  . GLN B 2 6   ? 10.76302 11.09969 15.43241 1.000 22.73952  ? 1368 GLN B HG2  1 
ATOM   2273 H  HG3  . GLN B 2 6   ? 10.25076 10.97149 16.93127 1.000 22.73952  ? 1368 GLN B HG3  1 
ATOM   2274 H  HE21 . GLN B 2 6   ? 12.46998 12.43889 15.09956 1.000 22.54986  ? 1368 GLN B HE21 1 
ATOM   2275 H  HE22 . GLN B 2 6   ? 13.45024 12.87251 16.13391 1.000 22.54986  ? 1368 GLN B HE22 1 
ATOM   2276 N  N    . ALA B 2 7   ? 11.35987 6.61362  14.78312 1.000 21.34305  ? 1369 ALA B N    1 
ATOM   2277 C  CA   . ALA B 2 7   ? 12.09038 5.35522  14.82884 1.000 24.66379  ? 1369 ALA B CA   1 
ATOM   2278 C  C    . ALA B 2 7   ? 13.53984 5.67702  14.50895 1.000 22.30624  ? 1369 ALA B C    1 
ATOM   2279 O  O    . ALA B 2 7   ? 13.79811 6.46837  13.61391 1.000 22.42011  ? 1369 ALA B O    1 
ATOM   2280 C  CB   . ALA B 2 7   ? 11.51336 4.34577  13.83678 1.000 29.96687  ? 1369 ALA B CB   1 
ATOM   2281 H  H    . ALA B 2 7   ? 11.45861 7.07630  14.06494 1.000 25.94151  ? 1369 ALA B H    1 
ATOM   2282 H  HA   . ALA B 2 7   ? 12.03568 4.93581  15.70177 1.000 29.92639  ? 1369 ALA B HA   1 
ATOM   2283 H  HB1  . ALA B 2 7   ? 10.55081 4.30645  13.95009 1.000 36.29008  ? 1369 ALA B HB1  1 
ATOM   2284 H  HB2  . ALA B 2 7   ? 11.72890 4.63069  12.93497 1.000 36.29008  ? 1369 ALA B HB2  1 
ATOM   2285 H  HB3  . ALA B 2 7   ? 11.90272 3.47447  14.01035 1.000 36.29008  ? 1369 ALA B HB3  1 
ATOM   2286 N  N    . PRO B 2 8   ? 14.49750 5.10425  15.24508 1.000 21.60759  ? 1370 PRO B N    1 
ATOM   2287 C  CA   . PRO B 2 8   ? 15.90583 5.47525  15.04246 1.000 27.54697  ? 1370 PRO B CA   1 
ATOM   2288 C  C    . PRO B 2 8   ? 16.65540 4.70740  13.96372 1.000 34.50964  ? 1370 PRO B C    1 
ATOM   2289 O  O    . PRO B 2 8   ? 17.81155 5.06584  13.67192 1.000 29.12431  ? 1370 PRO B O    1 
ATOM   2290 C  CB   . PRO B 2 8   ? 16.52453 5.19957  16.42959 1.000 25.39088  ? 1370 PRO B CB   1 
ATOM   2291 C  CG   . PRO B 2 8   ? 15.72420 4.01656  16.95981 1.000 37.39323  ? 1370 PRO B CG   1 
ATOM   2292 C  CD   . PRO B 2 8   ? 14.30178 4.21495  16.41041 1.000 27.52669  ? 1370 PRO B CD   1 
ATOM   2293 H  HA   . PRO B 2 8   ? 15.96327 6.42123  14.83577 1.000 33.38621  ? 1370 PRO B HA   1 
ATOM   2294 H  HB2  . PRO B 2 8   ? 17.46380 4.97522  16.33825 1.000 30.79890  ? 1370 PRO B HB2  1 
ATOM   2295 H  HB3  . PRO B 2 8   ? 16.42311 5.97650  17.00142 1.000 30.79890  ? 1370 PRO B HB3  1 
ATOM   2296 H  HG2  . PRO B 2 8   ? 16.10783 3.18673  16.63559 1.000 45.20172  ? 1370 PRO B HG2  1 
ATOM   2297 H  HG3  . PRO B 2 8   ? 15.72500 4.02576  17.92976 1.000 45.20172  ? 1370 PRO B HG3  1 
ATOM   2298 H  HD2  . PRO B 2 8   ? 13.91820 3.36750  16.13547 1.000 33.36188  ? 1370 PRO B HD2  1 
ATOM   2299 H  HD3  . PRO B 2 8   ? 13.73308 4.63705  17.07322 1.000 33.36188  ? 1370 PRO B HD3  1 
ATOM   2300 N  N    . GLU B 2 9   ? 16.04551 3.67476  13.36555 1.000 25.48575  ? 1371 GLU B N    1 
ATOM   2301 C  CA   . GLU B 2 9   ? 16.71650 2.91254  12.32019 1.000 29.68669  ? 1371 GLU B CA   1 
ATOM   2302 C  C    . GLU B 2 9   ? 17.22401 3.82325  11.21056 1.000 33.67215  ? 1371 GLU B C    1 
ATOM   2303 O  O    . GLU B 2 9   ? 16.50181 4.69232  10.72862 1.000 29.87813  ? 1371 GLU B O    1 
ATOM   2304 C  CB   . GLU B 2 9   ? 15.77545 1.88398  11.68687 1.000 40.25485  ? 1371 GLU B CB   1 
ATOM   2305 C  CG   . GLU B 2 9   ? 15.48383 0.66266  12.51279 1.000 45.04060  ? 1371 GLU B CG   1 
ATOM   2306 C  CD   . GLU B 2 9   ? 14.45139 0.94222  13.60505 1.000 47.68824  ? 1371 GLU B CD   1 
ATOM   2307 O  OE1  . GLU B 2 9   ? 14.30688 0.08729  14.50462 1.000 48.18808  ? 1371 GLU B OE1  1 
ATOM   2308 O  OE2  . GLU B 2 9   ? 13.79508 2.00676  13.55516 1.000 40.12765  ? 1371 GLU B OE2  1 
ATOM   2309 H  H    . GLU B 2 9   ? 15.25071 3.40242  13.54921 1.000 30.91274  ? 1371 GLU B H    1 
ATOM   2310 H  HA   . GLU B 2 9   ? 17.46176 2.45093  12.73542 1.000 35.95388  ? 1371 GLU B HA   1 
ATOM   2311 H  HB2  . GLU B 2 9   ? 14.92689 2.31877  11.50855 1.000 48.63567  ? 1371 GLU B HB2  1 
ATOM   2312 H  HB3  . GLU B 2 9   ? 16.17347 1.57995  10.85618 1.000 48.63567  ? 1371 GLU B HB3  1 
ATOM   2313 H  HG2  . GLU B 2 9   ? 15.13451 -0.03560 11.93720 1.000 54.37856  ? 1371 GLU B HG2  1 
ATOM   2314 H  HG3  . GLU B 2 9   ? 16.30210 0.36297  12.93884 1.000 54.37856  ? 1371 GLU B HG3  1 
ATOM   2315 N  N    . ILE B 2 10  ? 18.44963 3.56592  10.75630 1.000 33.43131  ? 1372 ILE B N    1 
ATOM   2316 C  CA   . ILE B 2 10  ? 19.04870 4.28193  9.63973  1.000 29.68986  ? 1372 ILE B CA   1 
ATOM   2317 C  C    . ILE B 2 10  ? 19.15302 3.34702  8.44846  1.000 32.23224  ? 1372 ILE B C    1 
ATOM   2318 O  O    . ILE B 2 10  ? 19.54691 2.17589  8.58322  1.000 27.13087  ? 1372 ILE B O    1 
ATOM   2319 C  CB   . ILE B 2 10  ? 20.43076 4.84155  10.04910 1.000 32.58254  ? 1372 ILE B CB   1 
ATOM   2320 C  CG1  . ILE B 2 10  ? 20.18170 6.07659  10.91212 1.000 25.69463  ? 1372 ILE B CG1  1 
ATOM   2321 C  CG2  . ILE B 2 10  ? 21.28956 5.13290  8.82558  1.000 27.14462  ? 1372 ILE B CG2  1 
ATOM   2322 C  CD1  . ILE B 2 10  ? 21.45191 6.69313  11.47053 1.000 33.79719  ? 1372 ILE B CD1  1 
ATOM   2323 H  H    . ILE B 2 10  ? 18.96465 2.96368  11.09047 1.000 40.44742  ? 1372 ILE B H    1 
ATOM   2324 H  HA   . ILE B 2 10  ? 18.47869 5.01986  9.37244  1.000 35.95767  ? 1372 ILE B HA   1 
ATOM   2325 H  HB   . ILE B 2 10  ? 20.93133 4.18877  10.56312 1.000 39.42890  ? 1372 ILE B HB   1 
ATOM   2326 H  HG12 . ILE B 2 10  ? 19.73684 6.74970  10.37367 1.000 31.16340  ? 1372 ILE B HG12 1 
ATOM   2327 H  HG13 . ILE B 2 10  ? 19.61902 5.82606  11.66147 1.000 31.16340  ? 1372 ILE B HG13 1 
ATOM   2328 H  HG21 . ILE B 2 10  ? 22.11434 5.55549  9.11204  1.000 32.90339  ? 1372 ILE B HG21 1 
ATOM   2329 H  HG22 . ILE B 2 10  ? 21.48576 4.29850  8.37151  1.000 32.90339  ? 1372 ILE B HG22 1 
ATOM   2330 H  HG23 . ILE B 2 10  ? 20.80282 5.72596  8.23207  1.000 32.90339  ? 1372 ILE B HG23 1 
ATOM   2331 H  HD11 . ILE B 2 10  ? 21.21469 7.42880  12.05655 1.000 40.88647  ? 1372 ILE B HD11 1 
ATOM   2332 H  HD12 . ILE B 2 10  ? 21.93857 6.01753  11.96814 1.000 40.88647  ? 1372 ILE B HD12 1 
ATOM   2333 H  HD13 . ILE B 2 10  ? 21.99503 7.01778  10.73533 1.000 40.88647  ? 1372 ILE B HD13 1 
ATOM   2334 N  N    . SER B 2 11  ? 18.81451 3.87962  7.26972  1.000 29.35508  ? 1373 SER B N    1 
ATOM   2335 C  CA   . SER B 2 11  ? 18.81257 3.09729  6.04341  1.000 26.81502  ? 1373 SER B CA   1 
ATOM   2336 C  C    . SER B 2 11  ? 19.18714 3.99166  4.86781  1.000 25.02902  ? 1373 SER B C    1 
ATOM   2337 O  O    . SER B 2 11  ? 19.29975 5.21221  5.00576  1.000 21.19431  ? 1373 SER B O    1 
ATOM   2338 C  CB   . SER B 2 11  ? 17.45104 2.49877  5.80152  1.000 24.09822  ? 1373 SER B CB   1 
ATOM   2339 O  OG   . SER B 2 11  ? 16.57364 3.60769  5.62839  1.000 29.88847  ? 1373 SER B OG   1 
ATOM   2340 H  H    . SER B 2 11  ? 18.58093 4.69991  7.15943  1.000 35.55594  ? 1373 SER B H    1 
ATOM   2341 H  HA   . SER B 2 11  ? 19.47712 2.39491  6.12044  1.000 32.50786  ? 1373 SER B HA   1 
ATOM   2342 H  HB2  . SER B 2 11  ? 17.46169 1.94961  5.00201  1.000 29.24771  ? 1373 SER B HB2  1 
ATOM   2343 H  HB3  . SER B 2 11  ? 17.17604 1.96765  6.56518  1.000 29.24771  ? 1373 SER B HB3  1 
ATOM   2344 H  HG   . SER B 2 11  ? 15.80914 3.33762  5.40885  1.000 36.19601  ? 1373 SER B HG   1 
ATOM   2345 N  N    . SER B 2 12  ? 19.33883 3.36031  3.69059  1.000 28.89625  ? 1374 SER B N    1 
ATOM   2346 C  CA   . SER B 2 12  ? 19.83753 4.04111  2.49666  1.000 31.88011  ? 1374 SER B CA   1 
ATOM   2347 C  C    . SER B 2 12  ? 18.99544 3.76800  1.25810  1.000 37.21165  ? 1374 SER B C    1 
ATOM   2348 O  O    . SER B 2 12  ? 17.89463 3.22339  1.35371  1.000 40.60268  ? 1374 SER B O    1 
ATOM   2349 C  CB   . SER B 2 12  ? 21.28616 3.61997  2.20853  1.000 30.10239  ? 1374 SER B CB   1 
ATOM   2350 O  OG   . SER B 2 12  ? 21.37656 2.20601  2.09108  1.000 39.28175  ? 1374 SER B OG   1 
ATOM   2351 H  H    . SER B 2 12  ? 19.15648 2.52970  3.56239  1.000 35.00534  ? 1374 SER B H    1 
ATOM   2352 H  HA   . SER B 2 12  ? 19.79487 4.99338  2.67628  1.000 38.58598  ? 1374 SER B HA   1 
ATOM   2353 H  HB2  . SER B 2 12  ? 21.57584 4.02692  1.37704  1.000 36.45271  ? 1374 SER B HB2  1 
ATOM   2354 H  HB3  . SER B 2 12  ? 21.85373 3.91505  2.93771  1.000 36.45271  ? 1374 SER B HB3  1 
ATOM   2355 H  HG   . SER B 2 12  ? 22.18194 1.97289  2.03989  1.000 47.46795  ? 1374 SER B HG   1 
ATOM   2356 N  N    . ASN B 2 13  ? 19.52376 4.15246  0.09093  1.000 56.62802  ? 1375 ASN B N    1 
ATOM   2357 C  CA   . ASN B 2 13  ? 18.86670 3.94894  -1.20317 1.000 56.39213  ? 1375 ASN B CA   1 
ATOM   2358 C  C    . ASN B 2 13  ? 17.40612 4.37081  -1.14001 1.000 48.97720  ? 1375 ASN B C    1 
ATOM   2359 O  O    . ASN B 2 13  ? 16.52697 3.70899  -1.68895 1.000 53.84968  ? 1375 ASN B O    1 
ATOM   2360 C  CB   . ASN B 2 13  ? 18.98541 2.49528  -1.67803 1.000 55.31068  ? 1375 ASN B CB   1 
ATOM   2361 H  H    . ASN B 2 13  ? 20.28551 4.54546  0.02103  1.000 68.28347  ? 1375 ASN B H    1 
ATOM   2362 H  HA   . ASN B 2 13  ? 19.31671 4.50811  -1.85564 1.000 68.00041  ? 1375 ASN B HA   1 
ATOM   2363 N  N    . SER B 2 14  ? 17.14951 5.49623  -0.46303 1.000 40.59535  ? 1376 SER B N    1 
ATOM   2364 C  CA   . SER B 2 14  ? 15.78782 6.01004  -0.38595 1.000 36.35974  ? 1376 SER B CA   1 
ATOM   2365 C  C    . SER B 2 14  ? 15.16747 6.21523  -1.76260 1.000 47.12352  ? 1376 SER B C    1 
ATOM   2366 O  O    . SER B 2 14  ? 13.94171 6.34237  -1.85256 1.000 48.09623  ? 1376 SER B O    1 
ATOM   2367 C  CB   . SER B 2 14  ? 15.75218 7.32216  0.37048  1.000 32.42117  ? 1376 SER B CB   1 
ATOM   2368 O  OG   . SER B 2 14  ? 16.14866 8.39184  -0.48481 1.000 46.97385  ? 1376 SER B OG   1 
ATOM   2369 H  H    . SER B 2 14  ? 17.73742 5.96830  -0.04938 1.000 49.04426  ? 1376 SER B H    1 
ATOM   2370 H  HA   . SER B 2 14  ? 15.25409 5.36427  0.10293  1.000 43.96153  ? 1376 SER B HA   1 
ATOM   2371 H  HB2  . SER B 2 14  ? 14.84915 7.48397  0.68555  1.000 39.23525  ? 1376 SER B HB2  1 
ATOM   2372 H  HB3  . SER B 2 14  ? 16.36226 7.27289  1.12299  1.000 39.23525  ? 1376 SER B HB3  1 
ATOM   2373 H  HG   . SER B 2 14  ? 16.05141 9.12673  -0.08973 1.000 56.69846  ? 1376 SER B HG   1 
ATOM   2374 N  N    . ILE B 2 15  ? 15.97584 6.28170  -2.82947 1.000 47.54842  ? 1377 ILE B N    1 
ATOM   2375 C  CA   . ILE B 2 15  ? 15.46426 6.29029  -4.20114 1.000 52.93034  ? 1377 ILE B CA   1 
ATOM   2376 C  C    . ILE B 2 15  ? 15.39978 4.84177  -4.70705 1.000 52.00015  ? 1377 ILE B C    1 
ATOM   2377 O  O    . ILE B 2 15  ? 16.35853 4.07372  -4.54744 1.000 54.94266  ? 1377 ILE B O    1 
ATOM   2378 C  CB   . ILE B 2 15  ? 16.33156 7.16136  -5.14067 1.000 46.12863  ? 1377 ILE B CB   1 
ATOM   2379 H  H    . ILE B 2 15  ? 16.83351 6.32303  -2.78170 1.000 57.38795  ? 1377 ILE B H    1 
ATOM   2380 H  HA   . ILE B 2 15  ? 14.57567 6.67925  -4.20604 1.000 63.84625  ? 1377 ILE B HA   1 
HETATM 2381 MG MG   . MG  C 3 .   ? 9.96040  25.52150 0.00000  0.50  17.13090  ? 201  MG  A MG   1 
HETATM 2382 MG MG   . MG  D 3 .   ? 12.50561 16.44087 21.77386 1.000 26.33401  ? 202  MG  A MG   1 
HETATM 2383 MG MG   . MG  E 3 .   ? 12.73202 25.52150 0.00000  0.50  38.21261  ? 203  MG  A MG   1 
HETATM 2384 MG MG   . MG  F 3 .   ? 26.29206 0.12662  7.23434  1.000 29.09139  ? 204  MG  A MG   1 
HETATM 2385 MG MG   . MG  G 3 .   ? 7.27589  16.01954 -7.78515 1.000 54.75550  ? 205  MG  A MG   1 
HETATM 2386 O  O    . HOH H 4 .   ? -2.500   8.103    14.211   1.000 44.04965  ? 301  HOH A O    1 
HETATM 2387 O  O    . HOH H 4 .   ? 39.07185 13.73372 18.12407 1.000 45.59576  ? 302  HOH A O    1 
HETATM 2388 O  O    . HOH H 4 .   ? 26.87204 15.49623 13.23818 1.000 30.27674  ? 303  HOH A O    1 
HETATM 2389 O  O    . HOH H 4 .   ? 40.95271 10.53555 11.03977 1.000 39.17002  ? 304  HOH A O    1 
HETATM 2390 O  O    . HOH H 4 .   ? 3.25977  20.47319 15.37463 1.000 23.27988  ? 305  HOH A O    1 
HETATM 2391 O  O    . HOH H 4 .   ? 33.734   17.209   -4.556   1.000 33.54418  ? 306  HOH A O    1 
HETATM 2392 O  O    . HOH H 4 .   ? 0.97822  15.19474 19.05104 1.000 28.96172  ? 307  HOH A O    1 
HETATM 2393 O  O    . HOH H 4 .   ? 41.189   13.345   -5.624   1.000 33.40943  ? 308  HOH A O    1 
HETATM 2394 O  O    . HOH H 4 .   ? 7.67996  20.75908 20.37931 1.000 35.65164  ? 309  HOH A O    1 
HETATM 2395 O  O    . HOH H 4 .   ? 6.33604  10.87096 0.45893  1.000 27.75866  ? 310  HOH A O    1 
HETATM 2396 O  O    . HOH H 4 .   ? 18.54059 12.31358 20.15291 1.000 19.67658  ? 311  HOH A O    1 
HETATM 2397 O  O    . HOH H 4 .   ? -2.52912 14.91285 15.67579 1.000 36.63296  ? 312  HOH A O    1 
HETATM 2398 O  O    . HOH H 4 .   ? 8.55884  16.86841 -5.19586 1.000 31.33103  ? 313  HOH A O    1 
HETATM 2399 O  O    . HOH H 4 .   ? 36.99675 12.08678 17.04797 1.000 40.30435  ? 314  HOH A O    1 
HETATM 2400 O  O    . HOH H 4 .   ? 9.65521  23.63413 12.00233 1.000 16.76798  ? 315  HOH A O    1 
HETATM 2401 O  O    . HOH H 4 .   ? 10.324   30.884   4.665    1.000 37.14087  ? 316  HOH A O    1 
HETATM 2402 O  O    . HOH H 4 .   ? 2.67411  7.25965  -4.44210 1.000 29.84225  ? 317  HOH A O    1 
HETATM 2403 O  O    . HOH H 4 .   ? 0.91426  13.89236 -5.79939 1.000 30.55966  ? 318  HOH A O    1 
HETATM 2404 O  O    . HOH H 4 .   ? 2.53748  24.03633 14.44383 1.000 24.16602  ? 319  HOH A O    1 
HETATM 2405 O  O    . HOH H 4 .   ? 1.40520  22.15664 13.50071 1.000 37.00785  ? 320  HOH A O    1 
HETATM 2406 O  O    . HOH H 4 .   ? 5.24372  18.65506 22.15264 1.000 36.66215  ? 321  HOH A O    1 
HETATM 2407 O  O    . HOH H 4 .   ? 24.40823 2.73772  13.44233 1.000 36.09622  ? 322  HOH A O    1 
HETATM 2408 O  O    . HOH H 4 .   ? 2.93236  19.75944 -3.52311 1.000 36.94200  ? 323  HOH A O    1 
HETATM 2409 O  O    . HOH H 4 .   ? 40.393   10.211   21.263   1.000 43.46483  ? 324  HOH A O    1 
HETATM 2410 O  O    . HOH H 4 .   ? 1.18698  10.08731 11.41911 1.000 26.70706  ? 325  HOH A O    1 
HETATM 2411 O  O    . HOH H 4 .   ? 17.23334 21.78161 21.82919 1.000 34.79125  ? 326  HOH A O    1 
HETATM 2412 O  O    . HOH H 4 .   ? 35.51774 10.75325 5.29885  1.000 28.47169  ? 327  HOH A O    1 
HETATM 2413 O  O    . HOH H 4 .   ? 9.55456  26.38730 10.76345 1.000 21.15945  ? 328  HOH A O    1 
HETATM 2414 O  O    . HOH H 4 .   ? 13.64720 27.19442 1.37114  1.000 33.44327  ? 329  HOH A O    1 
HETATM 2415 O  O    . HOH H 4 .   ? 33.939   15.022   -7.552   1.000 27.59456  ? 330  HOH A O    1 
HETATM 2416 O  O    . HOH H 4 .   ? 6.35540  2.76452  13.20353 1.000 39.13381  ? 331  HOH A O    1 
HETATM 2417 O  O    . HOH H 4 .   ? 19.56262 7.40010  -3.58798 1.000 50.00307  ? 332  HOH A O    1 
HETATM 2418 O  O    . HOH H 4 .   ? 20.35999 19.01188 14.01368 1.000 23.73538  ? 333  HOH A O    1 
HETATM 2419 O  O    . HOH H 4 .   ? 10.63921 24.11230 23.36562 1.000 39.59501  ? 334  HOH A O    1 
HETATM 2420 O  O    . HOH H 4 .   ? 28.74030 7.30192  -7.46792 1.000 29.18757  ? 335  HOH A O    1 
HETATM 2421 O  O    . HOH H 4 .   ? 15.845   23.650   -3.449   1.000 27.27748  ? 336  HOH A O    1 
HETATM 2422 O  O    . HOH H 4 .   ? 33.68192 6.00926  -4.88170 1.000 37.96262  ? 337  HOH A O    1 
HETATM 2423 O  O    . HOH H 4 .   ? 10.17589 26.36599 12.89259 1.000 33.46783  ? 338  HOH A O    1 
HETATM 2424 O  O    . HOH H 4 .   ? 12.56185 21.80186 -2.61987 1.000 22.06432  ? 339  HOH A O    1 
HETATM 2425 O  O    . HOH H 4 .   ? 21.88970 25.52150 0.00000  0.50  22.84712  ? 340  HOH A O    1 
HETATM 2426 O  O    . HOH H 4 .   ? 5.63616  -0.99000 3.20810  1.000 49.72416  ? 341  HOH A O    1 
HETATM 2427 O  O    . HOH H 4 .   ? 28.20603 2.77620  1.67017  1.000 33.10613  ? 342  HOH A O    1 
HETATM 2428 O  O    . HOH H 4 .   ? 4.40125  28.87908 4.96974  1.000 25.36443  ? 343  HOH A O    1 
HETATM 2429 O  O    . HOH H 4 .   ? 16.818   26.389   23.884   1.000 32.58649  ? 344  HOH A O    1 
HETATM 2430 O  O    . HOH H 4 .   ? 0.76725  24.93644 11.85156 1.000 32.05778  ? 345  HOH A O    1 
HETATM 2431 O  O    . HOH H 4 .   ? 34.10127 21.56819 13.21474 1.000 44.77847  ? 346  HOH A O    1 
HETATM 2432 O  O    . HOH H 4 .   ? 3.99409  0.00000  0.00000  0.50  49.30448  ? 347  HOH A O    1 
HETATM 2433 O  O    . HOH H 4 .   ? 9.64015  4.13226  -2.51442 1.000 35.47184  ? 348  HOH A O    1 
HETATM 2434 O  O    . HOH H 4 .   ? 34.64613 0.44501  1.40756  1.000 45.41051  ? 349  HOH A O    1 
HETATM 2435 O  O    . HOH H 4 .   ? -3.45991 18.33478 20.55405 1.000 46.73232  ? 350  HOH A O    1 
HETATM 2436 O  O    . HOH H 4 .   ? 31.71396 6.33701  14.07012 1.000 39.47291  ? 351  HOH A O    1 
HETATM 2437 O  O    . HOH H 4 .   ? 17.55856 24.13656 0.36677  1.000 28.97522  ? 352  HOH A O    1 
HETATM 2438 O  O    . HOH H 4 .   ? 19.76093 10.15133 18.43321 1.000 24.25127  ? 353  HOH A O    1 
HETATM 2439 O  O    . HOH H 4 .   ? -0.71766 9.88055  9.23982  1.000 29.58435  ? 354  HOH A O    1 
HETATM 2440 O  O    . HOH H 4 .   ? 24.08803 0.08040  12.50574 1.000 39.57793  ? 355  HOH A O    1 
HETATM 2441 O  O    . HOH H 4 .   ? 19.59306 6.82942  15.58359 1.000 31.97511  ? 356  HOH A O    1 
HETATM 2442 O  O    . HOH H 4 .   ? 1.32619  16.61597 22.21493 1.000 35.15856  ? 357  HOH A O    1 
HETATM 2443 O  O    . HOH H 4 .   ? 17.176   28.062   21.500   1.000 29.99371  ? 358  HOH A O    1 
HETATM 2444 O  O    . HOH H 4 .   ? 40.81511 19.38788 16.31142 1.000 40.46167  ? 359  HOH A O    1 
HETATM 2445 O  O    . HOH H 4 .   ? -1.72467 14.28562 -3.14586 1.000 35.40552  ? 360  HOH A O    1 
HETATM 2446 O  O    . HOH H 4 .   ? 12.54614 18.09207 -5.29812 1.000 33.65268  ? 361  HOH A O    1 
HETATM 2447 O  O    . HOH H 4 .   ? 38.096   16.483   15.952   1.000 32.29483  ? 362  HOH A O    1 
HETATM 2448 O  O    . HOH H 4 .   ? 25.02115 25.45009 -3.54229 1.000 35.60276  ? 363  HOH A O    1 
HETATM 2449 O  O    . HOH H 4 .   ? 36.12629 11.63131 -0.99239 1.000 35.21042  ? 364  HOH A O    1 
HETATM 2450 O  O    . HOH H 4 .   ? 21.92716 0.86477  10.06782 1.000 35.14888  ? 365  HOH A O    1 
HETATM 2451 O  O    . HOH H 4 .   ? 9.38169  12.55803 -6.46248 1.000 34.89148  ? 366  HOH A O    1 
HETATM 2452 O  O    . HOH H 4 .   ? 37.100   5.783    12.829   1.000 43.76661  ? 367  HOH A O    1 
HETATM 2453 O  O    . HOH H 4 .   ? 27.626   7.570    19.999   1.000 37.86960  ? 368  HOH A O    1 
HETATM 2454 O  O    . HOH H 4 .   ? 21.05103 23.41229 -5.56148 1.000 28.37907  ? 369  HOH A O    1 
HETATM 2455 O  O    . HOH H 4 .   ? 28.466   16.881   -8.133   1.000 25.73142  ? 370  HOH A O    1 
HETATM 2456 O  O    . HOH H 4 .   ? 2.29582  20.51309 24.08637 1.000 45.35800  ? 371  HOH A O    1 
HETATM 2457 O  O    . HOH H 4 .   ? 15.68473 25.52150 0.00000  0.50  34.65893  ? 372  HOH A O    1 
HETATM 2458 O  O    . HOH H 4 .   ? 7.31658  14.00521 -7.26078 1.000 43.10839  ? 373  HOH A O    1 
HETATM 2459 O  O    . HOH H 4 .   ? 15.855   21.754   -5.035   1.000 32.08680  ? 374  HOH A O    1 
HETATM 2460 O  O    . HOH H 4 .   ? 22.80784 4.72287  13.90554 1.000 35.14799  ? 375  HOH A O    1 
HETATM 2461 O  O    . HOH H 4 .   ? 32.13436 7.92698  17.15238 1.000 37.95758  ? 376  HOH A O    1 
HETATM 2462 O  O    . HOH H 4 .   ? 21.11124 12.95829 21.08713 1.000 32.71658  ? 377  HOH A O    1 
HETATM 2463 O  O    . HOH H 4 .   ? -3.29816 5.69333  9.53861  1.000 42.98661  ? 378  HOH A O    1 
HETATM 2464 O  O    . HOH H 4 .   ? 44.186   9.595    20.390   1.000 39.45732  ? 379  HOH A O    1 
HETATM 2465 O  O    . HOH H 4 .   ? -2.841   8.509    11.943   1.000 40.78260  ? 380  HOH A O    1 
HETATM 2466 O  O    . HOH H 4 .   ? 39.476   4.772    -4.206   1.000 45.01956  ? 381  HOH A O    1 
HETATM 2467 O  O    . HOH H 4 .   ? 24.737   20.505   -7.569   1.000 37.33469  ? 382  HOH A O    1 
HETATM 2468 O  O    . HOH H 4 .   ? 0.21609  31.18522 6.25724  1.000 40.09968  ? 383  HOH A O    1 
HETATM 2469 O  O    . HOH H 4 .   ? 2.798    26.666   15.755   1.000 41.58534  ? 384  HOH A O    1 
HETATM 2470 O  O    . HOH H 4 .   ? 4.23316  25.06093 20.57342 1.000 37.57314  ? 385  HOH A O    1 
HETATM 2471 O  O    . HOH H 4 .   ? 20.99543 17.67724 -5.42808 1.000 32.74603  ? 386  HOH A O    1 
HETATM 2472 O  O    . HOH H 4 .   ? 9.05709  29.39961 10.69368 1.000 42.51276  ? 387  HOH A O    1 
HETATM 2473 O  O    . HOH H 4 .   ? 12.13337 3.21291  9.97825  1.000 28.53575  ? 388  HOH A O    1 
HETATM 2474 O  O    . HOH H 4 .   ? 14.50709 30.61841 6.65966  1.000 36.05006  ? 389  HOH A O    1 
HETATM 2475 O  O    . HOH H 4 .   ? 2.83446  26.35003 19.13202 1.000 41.87819  ? 390  HOH A O    1 
HETATM 2476 O  O    . HOH H 4 .   ? 8.005    33.491   9.156    1.000 49.89689  ? 391  HOH A O    1 
HETATM 2477 O  O    . HOH H 4 .   ? -3.97312 16.60282 16.60154 1.000 27.57332  ? 392  HOH A O    1 
HETATM 2478 O  O    . HOH H 4 .   ? 20.65443 21.41891 -7.22935 1.000 39.33997  ? 393  HOH A O    1 
HETATM 2479 O  O    . HOH H 4 .   ? 35.992   7.608    -7.273   1.000 32.90139  ? 394  HOH A O    1 
HETATM 2480 O  O    . HOH H 4 .   ? 7.83827  31.63127 11.33757 1.000 39.14879  ? 395  HOH A O    1 
HETATM 2481 O  O    . HOH H 4 .   ? 18.81183 7.61358  18.43246 1.000 31.18635  ? 396  HOH A O    1 
HETATM 2482 O  O    . HOH H 4 .   ? 11.97932 30.39728 11.00262 1.000 46.14167  ? 397  HOH A O    1 
HETATM 2483 O  O    . HOH H 4 .   ? 37.49837 13.64233 1.32083  1.000 39.89531  ? 398  HOH A O    1 
HETATM 2484 O  O    . HOH H 4 .   ? 11.62813 13.62020 -7.84728 1.000 47.35604  ? 399  HOH A O    1 
HETATM 2485 O  O    . HOH H 4 .   ? 1.24625  13.88455 21.70112 1.000 32.28041  ? 400  HOH A O    1 
HETATM 2486 O  O    . HOH H 4 .   ? 32.99465 9.82734  14.10822 1.000 46.73468  ? 401  HOH A O    1 
HETATM 2487 O  O    . HOH H 4 .   ? 10.542   29.477   13.181   1.000 35.56342  ? 402  HOH A O    1 
HETATM 2488 O  O    . HOH H 4 .   ? 40.803   3.992    11.309   1.000 33.71256  ? 403  HOH A O    1 
HETATM 2489 O  O    . HOH H 4 .   ? 36.38360 14.26047 3.35667  1.000 37.12182  ? 404  HOH A O    1 
HETATM 2490 O  O    . HOH H 4 .   ? 34.352   11.626   16.919   1.000 46.76204  ? 405  HOH A O    1 
HETATM 2491 O  O    . HOH H 4 .   ? 31.644   23.203   -8.232   1.000 42.72611  ? 406  HOH A O    1 
HETATM 2492 O  O    . HOH I 4 .   ? 15.64667 -1.95089 14.32664 1.000 43.81051  ? 1401 HOH B O    1 
HETATM 2493 O  O    . HOH I 4 .   ? 14.41173 10.07101 -0.08258 1.000 37.45334  ? 1402 HOH B O    1 
HETATM 2494 O  O    . HOH I 4 .   ? 20.31283 4.61030  14.61358 1.000 34.55854  ? 1403 HOH B O    1 
HETATM 2495 O  O    . HOH I 4 .   ? 13.69693 9.14334  18.85962 1.000 26.06686  ? 1404 HOH B O    1 
HETATM 2496 O  O    . HOH I 4 .   ? 19.89048 1.57107  12.03208 1.000 32.13375  ? 1405 HOH B O    1 
HETATM 2497 O  O    . HOH I 4 .   ? 15.28902 4.07034  8.10132  1.000 24.62710  ? 1406 HOH B O    1 
HETATM 2498 O  O    . HOH I 4 .   ? 13.60963 5.62547  10.91038 1.000 18.41781  ? 1407 HOH B O    1 
HETATM 2499 O  O    . HOH I 4 .   ? 6.60751  7.43210  20.79551 1.000 35.62349  ? 1408 HOH B O    1 
HETATM 2500 O  O    . HOH I 4 .   ? 11.52225 4.35957  18.69746 1.000 38.38651  ? 1409 HOH B O    1 
HETATM 2501 O  O    . HOH I 4 .   ? 12.14636 7.15471  18.82878 1.000 31.62034  ? 1410 HOH B O    1 
HETATM 2502 O  O    . HOH I 4 .   ? 10.10155 7.94915  19.52553 1.000 32.05065  ? 1411 HOH B O    1 
HETATM 2503 O  O    . HOH I 4 .   ? 10.85188 -0.59767 15.31622 1.000 41.94286  ? 1412 HOH B O    1 
HETATM 2504 O  O    . HOH I 4 .   ? 18.79096 -0.41414 3.86359  1.000 42.14500  ? 1413 HOH B O    1 
HETATM 2505 O  O    . HOH I 4 .   ? 14.01050 1.88207  8.36875  1.000 32.71381  ? 1414 HOH B O    1 
HETATM 2506 O  O    . HOH I 4 .   ? 8.69107  7.21575  21.58708 1.000 34.13174  ? 1415 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   . ALA A 1   ? 0.51755 1.07533 0.63022 0.23449  -0.05430 0.00997  26   ALA A N   
2    C CA  . ALA A 1   ? 0.35817 0.92455 0.50803 0.20898  -0.06617 0.00169  26   ALA A CA  
3    C C   . ALA A 1   ? 0.36066 0.92878 0.53419 0.19273  -0.04772 0.01298  26   ALA A C   
4    O O   . ALA A 1   ? 0.29232 0.88633 0.51624 0.17650  -0.05109 0.01594  26   ALA A O   
5    C CB  . ALA A 1   ? 0.33576 0.93414 0.53327 0.20042  -0.09078 -0.00707 26   ALA A CB  
10   N N   . ALA A 2   ? 0.38928 0.92845 0.52630 0.19721  -0.02767 0.02027  27   ALA A N   
11   C CA  . ALA A 2   ? 0.44975 0.98395 0.60152 0.18209  -0.00965 0.02991  27   ALA A CA  
12   C C   . ALA A 2   ? 0.43661 0.98124 0.62739 0.15577  -0.02177 0.02276  27   ALA A C   
13   O O   . ALA A 2   ? 0.41317 0.95406 0.60249 0.15072  -0.04129 0.00887  27   ALA A O   
14   C CB  . ALA A 2   ? 0.46731 0.96217 0.57025 0.18984  0.00926  0.03532  27   ALA A CB  
20   N N   . LYS A 3   ? 0.30998 0.86495 0.53390 0.13936  -0.01065 0.03237  28   LYS A N   
21   C CA  . LYS A 3   ? 0.22737 0.78886 0.48930 0.11316  -0.02042 0.02836  28   LYS A CA  
22   C C   . LYS A 3   ? 0.21199 0.74384 0.44852 0.10456  -0.00744 0.02971  28   LYS A C   
23   O O   . LYS A 3   ? 0.20787 0.72769 0.43585 0.10223  0.01480  0.04220  28   LYS A O   
24   C CB  . LYS A 3   ? 0.30301 0.89182 0.61667 0.09938  -0.01552 0.03962  28   LYS A CB  
25   C CG  . LYS A 3   ? 0.22368 0.81315 0.57551 0.07095  -0.02041 0.04018  28   LYS A CG  
26   C CD  . LYS A 3   ? 0.27445 0.86576 0.64636 0.05948  -0.05145 0.02276  28   LYS A CD  
27   C CE  . LYS A 3   ? 0.21099 0.80028 0.62370 0.03101  -0.05791 0.02381  28   LYS A CE  
28   N NZ  . LYS A 3   ? 0.35213 0.93647 0.78103 0.02098  -0.09060 0.00535  28   LYS A NZ  
42   N N   . VAL A 4   ? 0.25372 0.77107 0.47627 0.10008  -0.02189 0.01614  29   VAL A N   
43   C CA  . VAL A 4   ? 0.22822 0.70224 0.41935 0.08913  -0.01182 0.01486  29   VAL A CA  
44   C C   . VAL A 4   ? 0.23349 0.70739 0.45839 0.06401  -0.02478 0.00902  29   VAL A C   
45   O O   . VAL A 4   ? 0.27090 0.76430 0.52607 0.05799  -0.04859 -0.00188 29   VAL A O   
46   C CB  . VAL A 4   ? 0.33252 0.77593 0.47306 0.10231  -0.01592 0.00470  29   VAL A CB  
47   C CG1 . VAL A 4   ? 0.25782 0.66186 0.37064 0.09137  -0.00557 0.00425  29   VAL A CG1 
48   C CG2 . VAL A 4   ? 0.38909 0.83141 0.49816 0.12725  -0.00524 0.01147  29   VAL A CG2 
58   N N   . VAL A 5   ? 0.26588 0.71621 0.48499 0.05004  -0.01055 0.01591  30   VAL A N   
59   C CA  . VAL A 5   ? 0.21719 0.66054 0.46376 0.02656  -0.01982 0.01292  30   VAL A CA  
60   C C   . VAL A 5   ? 0.22475 0.62479 0.43108 0.02316  -0.01434 0.00750  30   VAL A C   
61   O O   . VAL A 5   ? 0.24088 0.62133 0.41947 0.02657  0.00634  0.01695  30   VAL A O   
62   C CB  . VAL A 5   ? 0.21355 0.67560 0.49839 0.01238  -0.00604 0.03070  30   VAL A CB  
63   C CG1 . VAL A 5   ? 0.32346 0.76737 0.62662 -0.01121 -0.01229 0.02985  30   VAL A CG1 
64   C CG2 . VAL A 5   ? 0.17534 0.68710 0.51038 0.01307  -0.01295 0.03691  30   VAL A CG2 
74   N N   . LYS A 6   ? 0.22081 0.60643 0.42405 0.01747  -0.03358 -0.00823 31   LYS A N   
75   C CA  . LYS A 6   ? 0.21611 0.56557 0.38092 0.01797  -0.03058 -0.01526 31   LYS A CA  
76   C C   . LYS A 6   ? 0.30133 0.63407 0.48365 -0.00208 -0.03479 -0.01608 31   LYS A C   
77   O O   . LYS A 6   ? 0.27763 0.62092 0.49681 -0.01458 -0.05247 -0.02133 31   LYS A O   
78   C CB  . LYS A 6   ? 0.24523 0.58890 0.38641 0.03085  -0.04784 -0.03288 31   LYS A CB  
79   C CG  . LYS A 6   ? 0.37539 0.72134 0.48127 0.05298  -0.03982 -0.03115 31   LYS A CG  
80   C CD  . LYS A 6   ? 0.37058 0.71217 0.45061 0.06739  -0.05594 -0.04717 31   LYS A CD  
81   C CE  . LYS A 6   ? 0.51161 0.85530 0.55679 0.08962  -0.04616 -0.04167 31   LYS A CE  
82   N NZ  . LYS A 6   ? 0.59101 0.94430 0.61964 0.10741  -0.06433 -0.05493 31   LYS A NZ  
96   N N   . PHE A 7   ? 0.26149 0.56677 0.41748 -0.00498 -0.02037 -0.01137 32   PHE A N   
97   C CA  . PHE A 7   ? 0.26673 0.55153 0.43145 -0.02040 -0.02634 -0.01439 32   PHE A CA  
98   C C   . PHE A 7   ? 0.30770 0.56296 0.43267 -0.01563 -0.01889 -0.01846 32   PHE A C   
99   O O   . PHE A 7   ? 0.25179 0.50070 0.34599 -0.00477 -0.00461 -0.01410 32   PHE A O   
100  C CB  . PHE A 7   ? 0.36157 0.65150 0.55519 -0.03591 -0.01579 0.00217  32   PHE A CB  
101  C CG  . PHE A 7   ? 0.32202 0.59450 0.48934 -0.03468 0.00618  0.01418  32   PHE A CG  
102  C CD1 . PHE A 7   ? 0.46455 0.74667 0.61734 -0.02351 0.02403  0.02471  32   PHE A CD1 
103  C CD2 . PHE A 7   ? 0.41474 0.65992 0.57037 -0.04325 0.00774  0.01415  32   PHE A CD2 
104  C CE1 . PHE A 7   ? 0.43954 0.70275 0.56523 -0.02125 0.04217  0.03386  32   PHE A CE1 
105  C CE2 . PHE A 7   ? 0.38863 0.61788 0.51897 -0.04135 0.02577  0.02401  32   PHE A CE2 
106  C CZ  . PHE A 7   ? 0.48397 0.72161 0.59896 -0.03061 0.04262  0.03345  32   PHE A CZ  
116  N N   . SER A 8   ? 0.24435 0.48143 0.37249 -0.02419 -0.02974 -0.02674 33   SER A N   
117  C CA  . SER A 8   ? 0.28616 0.50040 0.38243 -0.01863 -0.02808 -0.03415 33   SER A CA  
118  C C   . SER A 8   ? 0.23516 0.42953 0.33397 -0.03104 -0.02174 -0.02707 33   SER A C   
119  O O   . SER A 8   ? 0.26849 0.46124 0.39548 -0.04432 -0.02866 -0.02386 33   SER A O   
120  C CB  . SER A 8   ? 0.23930 0.44996 0.33232 -0.01233 -0.04891 -0.05330 33   SER A CB  
121  O OG  . SER A 8   ? 0.42915 0.65992 0.52187 -0.00071 -0.05690 -0.05952 33   SER A OG  
127  N N   . TYR A 9   ? 0.25206 0.43141 0.32234 -0.02688 -0.00933 -0.02399 34   TYR A N   
128  C CA  . TYR A 9   ? 0.20953 0.36971 0.27665 -0.03598 -0.00309 -0.01739 34   TYR A CA  
129  C C   . TYR A 9   ? 0.19913 0.34442 0.24407 -0.03005 -0.00663 -0.02737 34   TYR A C   
130  O O   . TYR A 9   ? 0.25514 0.40409 0.27885 -0.01926 -0.00226 -0.03106 34   TYR A O   
131  C CB  . TYR A 9   ? 0.22544 0.38401 0.28109 -0.03669 0.01607  -0.00234 34   TYR A CB  
132  C CG  . TYR A 9   ? 0.28428 0.42413 0.33563 -0.04501 0.02165  0.00514  34   TYR A CG  
133  C CD1 . TYR A 9   ? 0.29826 0.43529 0.37370 -0.05665 0.01760  0.01159  34   TYR A CD1 
134  C CD2 . TYR A 9   ? 0.32616 0.45120 0.35040 -0.04154 0.03038  0.00681  34   TYR A CD2 
135  C CE1 . TYR A 9   ? 0.30499 0.42437 0.37349 -0.06234 0.02271  0.01943  34   TYR A CE1 
136  C CE2 . TYR A 9   ? 0.29188 0.40065 0.31045 -0.04755 0.03415  0.01333  34   TYR A CE2 
137  C CZ  . TYR A 9   ? 0.36060 0.46643 0.39958 -0.05689 0.03050  0.01955  34   TYR A CZ  
138  O OH  . TYR A 9   ? 0.33110 0.41994 0.36163 -0.06117 0.03410  0.02692  34   TYR A OH  
148  N N   . MET A 10  ? 0.24600 0.37564 0.29726 -0.03659 -0.01423 -0.03055 35   MET A N   
149  C CA  . MET A 10  ? 0.18667 0.30362 0.22008 -0.03104 -0.01652 -0.03823 35   MET A CA  
150  C C   . MET A 10  ? 0.23612 0.33790 0.26264 -0.03776 -0.00741 -0.02824 35   MET A C   
151  O O   . MET A 10  ? 0.24554 0.33777 0.28587 -0.04759 -0.00880 -0.02110 35   MET A O   
152  C CB  . MET A 10  ? 0.28670 0.39547 0.32989 -0.02928 -0.03576 -0.05296 35   MET A CB  
153  C CG  . MET A 10  ? 0.33458 0.43979 0.35690 -0.01651 -0.03815 -0.06395 35   MET A CG  
154  S SD  . MET A 10  ? 0.36762 0.45663 0.39756 -0.01236 -0.06067 -0.08160 35   MET A SD  
155  C CE  . MET A 10  ? 0.44198 0.50869 0.48900 -0.02886 -0.06123 -0.07027 35   MET A CE  
165  N N   . TRP A 11  ? 0.21842 0.31814 0.22413 -0.03227 0.00076  -0.02770 36   TRP A N   
166  C CA  . TRP A 11  ? 0.20492 0.29136 0.20158 -0.03659 0.00667  -0.02091 36   TRP A CA  
167  C C   . TRP A 11  ? 0.27349 0.35844 0.26075 -0.02971 0.00237  -0.02953 36   TRP A C   
168  O O   . TRP A 11  ? 0.26709 0.36351 0.24463 -0.02166 0.00558  -0.03375 36   TRP A O   
169  C CB  . TRP A 11  ? 0.33200 0.41880 0.31476 -0.03772 0.02107  -0.01031 36   TRP A CB  
170  C CG  . TRP A 11  ? 0.31514 0.38808 0.28657 -0.04139 0.02533  -0.00446 36   TRP A CG  
171  C CD1 . TRP A 11  ? 0.30037 0.36058 0.27549 -0.04584 0.02027  -0.00241 36   TRP A CD1 
172  C CD2 . TRP A 11  ? 0.29896 0.36739 0.25232 -0.04054 0.03414  0.00007  36   TRP A CD2 
173  N NE1 . TRP A 11  ? 0.35129 0.40157 0.31078 -0.04682 0.02517  0.00267  36   TRP A NE1 
174  C CE2 . TRP A 11  ? 0.28549 0.34009 0.23212 -0.04422 0.03291  0.00345  36   TRP A CE2 
175  C CE3 . TRP A 11  ? 0.31833 0.39106 0.26005 -0.03680 0.04182  0.00150  36   TRP A CE3 
176  C CZ2 . TRP A 11  ? 0.37040 0.41579 0.29961 -0.04475 0.03757  0.00670  36   TRP A CZ2 
177  C CZ3 . TRP A 11  ? 0.28846 0.34983 0.21408 -0.03831 0.04697  0.00541  36   TRP A CZ3 
178  C CH2 . TRP A 11  ? 0.38403 0.43225 0.30379 -0.04244 0.04412  0.00717  36   TRP A CH2 
189  N N   . THR A 12  ? 0.23882 0.31093 0.22956 -0.03194 -0.00432 -0.03099 37   THR A N   
190  C CA  . THR A 12  ? 0.24063 0.31330 0.22443 -0.02468 -0.00768 -0.03775 37   THR A CA  
191  C C   . THR A 12  ? 0.24189 0.30646 0.21832 -0.02929 -0.00254 -0.02964 37   THR A C   
192  O O   . THR A 12  ? 0.34371 0.39346 0.32214 -0.03574 -0.00404 -0.02301 37   THR A O   
193  C CB  . THR A 12  ? 0.29376 0.35769 0.28594 -0.01970 -0.02233 -0.04867 37   THR A CB  
194  O OG1 . THR A 12  ? 0.32998 0.40112 0.32644 -0.01392 -0.02945 -0.05865 37   THR A OG1 
195  C CG2 . THR A 12  ? 0.29967 0.36741 0.28478 -0.00952 -0.02452 -0.05508 37   THR A CG2 
203  N N   . ILE A 13  ? 0.24513 0.31988 0.21349 -0.02590 0.00298  -0.02961 38   ILE A N   
204  C CA  . ILE A 13  ? 0.26342 0.33321 0.22622 -0.02946 0.00480  -0.02444 38   ILE A CA  
205  C C   . ILE A 13  ? 0.20712 0.28180 0.17497 -0.02230 -0.00292 -0.03125 38   ILE A C   
206  O O   . ILE A 13  ? 0.22786 0.31945 0.19819 -0.01388 -0.00230 -0.03735 38   ILE A O   
207  C CB  . ILE A 13  ? 0.22636 0.30368 0.18103 -0.03231 0.01443  -0.01925 38   ILE A CB  
208  C CG1 . ILE A 13  ? 0.31659 0.38607 0.26381 -0.03711 0.02175  -0.01257 38   ILE A CG1 
209  C CG2 . ILE A 13  ? 0.27966 0.35261 0.23124 -0.03616 0.01249  -0.01623 38   ILE A CG2 
210  C CD1 . ILE A 13  ? 0.34736 0.42161 0.28615 -0.03790 0.03038  -0.00883 38   ILE A CD1 
222  N N   . ASN A 14  ? 0.28367 0.34484 0.25169 -0.02395 -0.00933 -0.02934 39   ASN A N   
223  C CA  . ASN A 14  ? 0.32940 0.39350 0.30258 -0.01523 -0.01798 -0.03590 39   ASN A CA  
224  C C   . ASN A 14  ? 0.31454 0.39256 0.28830 -0.01486 -0.01609 -0.03363 39   ASN A C   
225  O O   . ASN A 14  ? 0.29729 0.37299 0.26539 -0.02341 -0.01159 -0.02663 39   ASN A O   
226  C CB  . ASN A 14  ? 0.33079 0.37192 0.30439 -0.01578 -0.02731 -0.03448 39   ASN A CB  
227  C CG  . ASN A 14  ? 0.32597 0.35375 0.30480 -0.01811 -0.03104 -0.03615 39   ASN A CG  
228  O OD1 . ASN A 14  ? 0.38555 0.41117 0.37023 -0.01043 -0.03959 -0.04622 39   ASN A OD1 
229  N ND2 . ASN A 14  ? 0.39985 0.41853 0.37735 -0.02828 -0.02548 -0.02646 39   ASN A ND2 
236  N N   . ASN A 15  ? 0.35905 0.45194 0.34049 -0.00417 -0.02041 -0.04016 40   ASN A N   
237  C CA  . ASN A 15  ? 0.34545 0.45790 0.33432 -0.00290 -0.01985 -0.03824 40   ASN A CA  
238  C C   . ASN A 15  ? 0.28416 0.40882 0.27350 -0.01290 -0.00972 -0.03131 40   ASN A C   
239  O O   . ASN A 15  ? 0.39457 0.51599 0.38327 -0.02201 -0.01064 -0.02587 40   ASN A O   
240  C CB  . ASN A 15  ? 0.33088 0.42956 0.31798 -0.00474 -0.02920 -0.03556 40   ASN A CB  
241  C CG  . ASN A 15  ? 0.38330 0.45671 0.36472 -0.00005 -0.03770 -0.03800 40   ASN A CG  
242  O OD1 . ASN A 15  ? 0.49329 0.54396 0.46513 -0.00768 -0.03841 -0.03166 40   ASN A OD1 
243  N ND2 . ASN A 15  ? 0.45991 0.53632 0.44675 0.01301  -0.04367 -0.04661 40   ASN A ND2 
250  N N   . PHE A 16  ? 0.33368 0.46963 0.32235 -0.01063 -0.00103 -0.03181 41   PHE A N   
251  C CA  . PHE A 16  ? 0.30561 0.44449 0.29135 -0.02074 0.00840  -0.02408 41   PHE A CA  
252  C C   . PHE A 16  ? 0.32679 0.48644 0.32573 -0.02513 0.01109  -0.01876 41   PHE A C   
253  O O   . PHE A 16  ? 0.38075 0.53335 0.37858 -0.03718 0.01238  -0.01257 41   PHE A O   
254  C CB  . PHE A 16  ? 0.35241 0.49816 0.33302 -0.01592 0.01669  -0.02479 41   PHE A CB  
255  C CG  . PHE A 16  ? 0.31816 0.46582 0.29516 -0.02440 0.02660  -0.01607 41   PHE A CG  
256  C CD1 . PHE A 16  ? 0.28910 0.41540 0.25458 -0.03261 0.02816  -0.01243 41   PHE A CD1 
257  C CD2 . PHE A 16  ? 0.33313 0.50338 0.31861 -0.02372 0.03466  -0.01045 41   PHE A CD2 
258  C CE1 . PHE A 16  ? 0.26207 0.38621 0.22242 -0.03885 0.03628  -0.00507 41   PHE A CE1 
259  C CE2 . PHE A 16  ? 0.35735 0.52511 0.33970 -0.03229 0.04304  -0.00132 41   PHE A CE2 
260  C CZ  . PHE A 16  ? 0.29575 0.43810 0.26427 -0.03950 0.04300  0.00048  41   PHE A CZ  
270  N N   . SER A 17  ? 0.36630 0.55213 0.37884 -0.01525 0.01167  -0.02100 42   SER A N   
271  C CA  . SER A 17  ? 0.29948 0.50984 0.33091 -0.02050 0.01393  -0.01443 42   SER A CA  
272  C C   . SER A 17  ? 0.37667 0.57478 0.41186 -0.03179 0.00317  -0.01294 42   SER A C   
273  O O   . SER A 17  ? 0.50336 0.71047 0.55078 -0.04348 0.00364  -0.00640 42   SER A O   
274  C CB  . SER A 17  ? 0.37733 0.61899 0.42341 -0.00504 0.01491  -0.01773 42   SER A CB  
275  O OG  . SER A 17  ? 0.38568 0.61867 0.43147 0.00324  0.00234  -0.02582 42   SER A OG  
281  N N   . PHE A 18  ? 0.33112 0.50808 0.35581 -0.02835 -0.00738 -0.01859 43   PHE A N   
282  C CA  . PHE A 18  ? 0.29592 0.46052 0.31939 -0.03512 -0.01890 -0.01808 43   PHE A CA  
283  C C   . PHE A 18  ? 0.37550 0.51277 0.38140 -0.04769 -0.01904 -0.01467 43   PHE A C   
284  O O   . PHE A 18  ? 0.34193 0.46593 0.34155 -0.05211 -0.02924 -0.01502 43   PHE A O   
285  C CB  . PHE A 18  ? 0.39345 0.54372 0.40899 -0.02460 -0.02895 -0.02361 43   PHE A CB  
288  N N   . CYS A 19  ? 0.41079 0.53911 0.40668 -0.05162 -0.00864 -0.01186 44   CYS A N   
289  C CA  . CYS A 19  ? 0.43316 0.53480 0.41016 -0.06039 -0.00828 -0.00930 44   CYS A CA  
290  C C   . CYS A 19  ? 0.39754 0.49975 0.38117 -0.07173 -0.01403 -0.00697 44   CYS A C   
291  O O   . CYS A 19  ? 0.38712 0.51038 0.39038 -0.07710 -0.01015 -0.00308 44   CYS A O   
292  C CB  . CYS A 19  ? 0.43109 0.52739 0.39915 -0.06060 0.00409  -0.00649 44   CYS A CB  
293  S SG  . CYS A 19  ? 0.43191 0.51867 0.38906 -0.05124 0.00804  -0.00937 44   CYS A SG  
299  N N   . ARG A 20  ? 0.34439 0.42276 0.31125 -0.07540 -0.02355 -0.00893 45   ARG A N   
300  C CA  . ARG A 20  ? 0.40797 0.48258 0.37981 -0.08631 -0.03328 -0.00914 45   ARG A CA  
301  C C   . ARG A 20  ? 0.46532 0.51185 0.41621 -0.09268 -0.03023 -0.00813 45   ARG A C   
302  O O   . ARG A 20  ? 0.45171 0.48576 0.40065 -0.10152 -0.04055 -0.01009 45   ARG A O   
303  C CB  . ARG A 20  ? 0.36072 0.42922 0.32772 -0.08407 -0.04996 -0.01402 45   ARG A CB  
306  N N   . GLU A 21  ? 0.33498 0.37081 0.27044 -0.08768 -0.01766 -0.00584 46   GLU A N   
307  C CA  . GLU A 21  ? 0.36930 0.37965 0.28481 -0.09107 -0.01363 -0.00468 46   GLU A CA  
308  C C   . GLU A 21  ? 0.38374 0.40115 0.31687 -0.10226 -0.01170 -0.00030 46   GLU A C   
309  O O   . GLU A 21  ? 0.31328 0.35850 0.27039 -0.10377 -0.00468 0.00471  46   GLU A O   
310  C CB  . GLU A 21  ? 0.37777 0.38194 0.27858 -0.08257 -0.00003 -0.00213 46   GLU A CB  
311  C CG  . GLU A 21  ? 0.39808 0.38767 0.27764 -0.07359 -0.00027 -0.00368 46   GLU A CG  
312  C CD  . GLU A 21  ? 0.40633 0.41168 0.29773 -0.06837 -0.00237 -0.00426 46   GLU A CD  
313  O OE1 . GLU A 21  ? 0.41423 0.44242 0.32845 -0.06955 -0.00357 -0.00506 46   GLU A OE1 
314  O OE2 . GLU A 21  ? 0.39707 0.39116 0.27446 -0.06246 -0.00288 -0.00334 46   GLU A OE2 
321  N N   . GLU A 22  ? 0.37440 0.36543 0.29458 -0.10934 -0.01785 -0.00170 47   GLU A N   
322  C CA  . GLU A 22  ? 0.39272 0.38369 0.32856 -0.12170 -0.01652 0.00400  47   GLU A CA  
323  C C   . GLU A 22  ? 0.45711 0.42353 0.37129 -0.11857 -0.00606 0.00724  47   GLU A C   
324  O O   . GLU A 22  ? 0.44163 0.39692 0.33242 -0.10663 0.00102  0.00526  47   GLU A O   
325  C CB  . GLU A 22  ? 0.43748 0.41591 0.38039 -0.13437 -0.03505 -0.00046 47   GLU A CB  
326  C CG  . GLU A 22  ? 0.48903 0.50000 0.46358 -0.13956 -0.04504 -0.00107 47   GLU A CG  
327  C CD  . GLU A 22  ? 0.55171 0.60066 0.56461 -0.14672 -0.03470 0.00990  47   GLU A CD  
328  O OE1 . GLU A 22  ? 0.48248 0.52700 0.50156 -0.15454 -0.02554 0.01857  47   GLU A OE1 
329  O OE2 . GLU A 22  ? 0.52453 0.60774 0.55998 -0.14290 -0.03513 0.01053  47   GLU A OE2 
336  N N   . MET A 23  ? 0.45425 0.41533 0.37966 -0.12929 -0.00409 0.01396  48   MET A N   
337  C CA  . MET A 23  ? 0.46561 0.39801 0.36992 -0.12694 0.00299  0.01708  48   MET A CA  
338  C C   . MET A 23  ? 0.46527 0.36431 0.33277 -0.11643 -0.00225 0.00739  48   MET A C   
339  O O   . MET A 23  ? 0.50574 0.38546 0.36230 -0.11918 -0.01735 -0.00115 48   MET A O   
340  C CB  . MET A 23  ? 0.51864 0.43596 0.43690 -0.14364 -0.00381 0.02226  48   MET A CB  
341  C CG  . MET A 23  ? 0.60207 0.51617 0.52419 -0.14600 0.00972  0.03488  48   MET A CG  
342  S SD  . MET A 23  ? 0.85482 0.72454 0.77495 -0.16272 -0.00272 0.03680  48   MET A SD  
343  C CE  . MET A 23  ? 0.71012 0.59653 0.66611 -0.18266 -0.02232 0.03342  48   MET A CE  
353  N N   . GLY A 24  ? 0.39633 0.37062 0.41073 -0.06160 0.02236  -0.02822 49   GLY A N   
354  C CA  . GLY A 24  ? 0.39372 0.34150 0.37570 -0.05583 0.01735  -0.03147 49   GLY A CA  
355  C C   . GLY A 24  ? 0.40703 0.36509 0.37472 -0.04315 0.00525  -0.03198 49   GLY A C   
356  O O   . GLY A 24  ? 0.39121 0.33093 0.33187 -0.03381 0.00731  -0.02953 49   GLY A O   
360  N N   . GLU A 25  ? 0.41749 0.40350 0.40420 -0.04188 -0.00498 -0.03396 50   GLU A N   
361  C CA  . GLU A 25  ? 0.32636 0.31818 0.29991 -0.02987 -0.01432 -0.03333 50   GLU A CA  
362  C C   . GLU A 25  ? 0.38119 0.37672 0.34917 -0.01991 -0.00284 -0.02438 50   GLU A C   
363  O O   . GLU A 25  ? 0.35371 0.35904 0.33420 -0.02130 0.00803  -0.01954 50   GLU A O   
364  C CB  . GLU A 25  ? 0.33414 0.35311 0.33120 -0.03001 -0.02800 -0.03706 50   GLU A CB  
365  C CG  . GLU A 25  ? 0.41260 0.43786 0.42213 -0.04297 -0.04255 -0.04743 50   GLU A CG  
366  C CD  . GLU A 25  ? 0.45007 0.50227 0.47338 -0.03765 -0.06143 -0.04973 50   GLU A CD  
367  O OE1 . GLU A 25  ? 0.40103 0.48375 0.46046 -0.03721 -0.06056 -0.04673 50   GLU A OE1 
368  O OE2 . GLU A 25  ? 0.64084 0.68412 0.63850 -0.03273 -0.07633 -0.05368 50   GLU A OE2 
375  N N   . VAL A 26  ? 0.36153 0.34985 0.31005 -0.01071 -0.00512 -0.02274 51   VAL A N   
376  C CA  . VAL A 26  ? 0.30197 0.29274 0.24397 -0.00450 0.00461  -0.01654 51   VAL A CA  
377  C C   . VAL A 26  ? 0.29496 0.29231 0.23690 0.00178  0.00132  -0.01704 51   VAL A C   
378  O O   . VAL A 26  ? 0.34149 0.33325 0.27653 0.00580  -0.00751 -0.01895 51   VAL A O   
379  C CB  . VAL A 26  ? 0.35683 0.33023 0.27754 -0.00047 0.01036  -0.01261 51   VAL A CB  
380  C CG1 . VAL A 26  ? 0.36334 0.32219 0.26511 0.00450  0.00449  -0.01516 51   VAL A CG1 
381  C CG2 . VAL A 26  ? 0.41008 0.39478 0.33061 0.00352  0.01857  -0.00639 51   VAL A CG2 
391  N N   . ILE A 27  ? 0.34264 0.34962 0.28965 0.00277  0.00909  -0.01537 52   ILE A N   
392  C CA  . ILE A 27  ? 0.28597 0.29127 0.22858 0.00728  0.01091  -0.01609 52   ILE A CA  
393  C C   . ILE A 27  ? 0.33577 0.33854 0.26661 0.00621  0.01720  -0.01397 52   ILE A C   
394  O O   . ILE A 27  ? 0.29966 0.31316 0.23248 0.00302  0.02177  -0.01268 52   ILE A O   
395  C CB  . ILE A 27  ? 0.28378 0.30042 0.24087 0.00745  0.01605  -0.01881 52   ILE A CB  
396  C CG1 . ILE A 27  ? 0.45573 0.48184 0.43184 0.01017  0.01049  -0.01945 52   ILE A CG1 
397  C CG2 . ILE A 27  ? 0.40933 0.41697 0.35924 0.01050  0.02097  -0.02080 52   ILE A CG2 
398  C CD1 . ILE A 27  ? 0.43848 0.47529 0.43016 0.01244  0.01954  -0.02137 52   ILE A CD1 
410  N N   . LYS A 28  ? 0.35441 0.34569 0.27410 0.00925  0.01782  -0.01275 53   LYS A N   
411  C CA  . LYS A 28  ? 0.32850 0.32290 0.24395 0.00716  0.02411  -0.01076 53   LYS A CA  
412  C C   . LYS A 28  ? 0.40323 0.39820 0.32216 0.00306  0.02928  -0.01511 53   LYS A C   
413  O O   . LYS A 28  ? 0.34661 0.32760 0.26325 0.00623  0.03037  -0.01629 53   LYS A O   
414  C CB  . LYS A 28  ? 0.48168 0.46210 0.38390 0.01202  0.02572  -0.00619 53   LYS A CB  
415  C CG  . LYS A 28  ? 0.59591 0.56512 0.48849 0.01567  0.02109  -0.00510 53   LYS A CG  
416  C CD  . LYS A 28  ? 0.75012 0.69725 0.62128 0.02183  0.02082  -0.00395 53   LYS A CD  
417  C CE  . LYS A 28  ? 0.64734 0.58005 0.50506 0.02339  0.01919  -0.00526 53   LYS A CE  
418  N NZ  . LYS A 28  ? 0.71513 0.65332 0.57962 0.02362  0.02729  -0.00100 53   LYS A NZ  
432  N N   . SER A 29  ? 0.36275 0.37309 0.28630 -0.00385 0.03246  -0.01744 54   SER A N   
433  C CA  . SER A 29  ? 0.28573 0.29431 0.21179 -0.01153 0.03808  -0.02392 54   SER A CA  
434  C C   . SER A 29  ? 0.26595 0.26440 0.19042 -0.01194 0.04376  -0.02005 54   SER A C   
435  O O   . SER A 29  ? 0.34059 0.33584 0.26021 -0.00537 0.04358  -0.01246 54   SER A O   
436  C CB  . SER A 29  ? 0.36456 0.39708 0.29517 -0.02087 0.03692  -0.02946 54   SER A CB  
437  O OG  . SER A 29  ? 0.30629 0.35672 0.24267 -0.02237 0.03576  -0.02411 54   SER A OG  
443  N N   . SER A 30  ? 0.30872 0.29862 0.23608 -0.02011 0.05129  -0.02577 55   SER A N   
444  C CA  . SER A 30  ? 0.30792 0.29257 0.23853 -0.02454 0.06001  -0.02263 55   SER A CA  
445  C C   . SER A 30  ? 0.31476 0.33245 0.26019 -0.03185 0.05789  -0.02205 55   SER A C   
446  O O   . SER A 30  ? 0.25920 0.30230 0.21030 -0.03610 0.04978  -0.02635 55   SER A O   
447  C CB  . SER A 30  ? 0.40696 0.37188 0.33915 -0.03433 0.07070  -0.03008 55   SER A CB  
448  O OG  . SER A 30  ? 0.34798 0.28292 0.26739 -0.02331 0.07386  -0.02697 55   SER A OG  
454  N N   . THR A 31  ? 0.35648 0.37475 0.30786 -0.03169 0.06606  -0.01534 56   THR A N   
455  C CA  . THR A 31  ? 0.31171 0.36491 0.28273 -0.03609 0.06569  -0.01226 56   THR A CA  
456  C C   . THR A 31  ? 0.30942 0.38577 0.29954 -0.05583 0.06460  -0.02382 56   THR A C   
457  O O   . THR A 31  ? 0.40537 0.46098 0.39481 -0.06751 0.07223  -0.03248 56   THR A O   
458  C CB  . THR A 31  ? 0.37549 0.41950 0.34792 -0.02946 0.07857  -0.00165 56   THR A CB  
459  O OG1 . THR A 31  ? 0.40949 0.43256 0.35958 -0.01228 0.07718  0.00611  56   THR A OG1 
460  C CG2 . THR A 31  ? 0.37366 0.45621 0.37333 -0.03315 0.08178  0.00305  56   THR A CG2 
468  N N   . PHE A 32  ? 0.28361 0.40248 0.28957 -0.05957 0.05484  -0.02429 57   PHE A N   
469  C CA  . PHE A 32  ? 0.30522 0.45301 0.32915 -0.08035 0.05001  -0.03731 57   PHE A CA  
470  C C   . PHE A 32  ? 0.31459 0.51400 0.36647 -0.08168 0.04419  -0.03090 57   PHE A C   
471  O O   . PHE A 32  ? 0.21977 0.43317 0.27342 -0.06374 0.04249  -0.01624 57   PHE A O   
472  C CB  . PHE A 32  ? 0.32656 0.47530 0.33446 -0.08599 0.03906  -0.04997 57   PHE A CB  
473  C CG  . PHE A 32  ? 0.31193 0.48365 0.31066 -0.07244 0.02646  -0.04249 57   PHE A CG  
474  C CD1 . PHE A 32  ? 0.32666 0.54516 0.33615 -0.07560 0.01388  -0.04210 57   PHE A CD1 
475  C CD2 . PHE A 32  ? 0.37796 0.52380 0.35739 -0.05634 0.02773  -0.03500 57   PHE A CD2 
476  C CE1 . PHE A 32  ? 0.31986 0.55432 0.31703 -0.06091 0.00474  -0.03257 57   PHE A CE1 
477  C CE2 . PHE A 32  ? 0.40452 0.56582 0.37516 -0.04483 0.01969  -0.02727 57   PHE A CE2 
478  C CZ  . PHE A 32  ? 0.34761 0.55096 0.32559 -0.04601 0.00937  -0.02490 57   PHE A CZ  
488  N N   . SER A 33  ? 0.34959 0.57647 0.42514 -0.10335 0.04234  -0.04218 58   SER A N   
489  C CA  . SER A 33  ? 0.27493 0.55484 0.38700 -0.10748 0.03926  -0.03622 58   SER A CA  
490  C C   . SER A 33  ? 0.41915 0.74955 0.54154 -0.12058 0.01836  -0.04732 58   SER A C   
491  O O   . SER A 33  ? 0.43087 0.75009 0.53640 -0.13635 0.01142  -0.06557 58   SER A O   
492  C CB  . SER A 33  ? 0.44939 0.72625 0.58861 -0.12500 0.05566  -0.03965 58   SER A CB  
493  O OG  . SER A 33  ? 0.59577 0.89588 0.75212 -0.15404 0.04796  -0.05955 58   SER A OG  
499  N N   . SER A 34  ? 0.41946 0.80605 0.56939 -0.11350 0.00912  -0.03626 59   SER A N   
500  C CA  . SER A 34  ? 0.52099 0.96318 0.67876 -0.12078 -0.01403 -0.04273 59   SER A CA  
501  C C   . SER A 34  ? 0.56972 1.04769 0.75919 -0.15376 -0.02023 -0.06217 59   SER A C   
502  O O   . SER A 34  ? 0.61494 1.07305 0.78625 -0.17582 -0.02436 -0.08472 59   SER A O   
503  C CB  . SER A 34  ? 0.54585 1.03443 0.72123 -0.09567 -0.02100 -0.01975 59   SER A CB  
504  O OG  . SER A 34  ? 0.39970 0.85012 0.54287 -0.06860 -0.01493 -0.00477 59   SER A OG  
510  N N   . ASP A 38  ? 0.46691 1.06260 0.83869 -0.14494 0.02227  -0.01346 63   ASP A N   
511  C CA  . ASP A 38  ? 0.45124 1.07539 0.81911 -0.11196 0.01322  0.00683  63   ASP A CA  
512  C C   . ASP A 38  ? 0.41861 1.00492 0.76489 -0.08500 0.03537  0.02503  63   ASP A C   
513  O O   . ASP A 38  ? 0.37918 0.97645 0.72000 -0.05534 0.03376  0.04350  63   ASP A O   
514  C CB  . ASP A 38  ? 0.28571 0.92349 0.62072 -0.10892 -0.01469 0.00015  63   ASP A CB  
515  C CG  . ASP A 38  ? 0.48999 1.08408 0.77741 -0.09895 -0.01134 0.00012  63   ASP A CG  
516  O OD1 . ASP A 38  ? 0.48192 1.02174 0.75241 -0.10076 0.00928  -0.00170 63   ASP A OD1 
517  O OD2 . ASP A 38  ? 0.38251 0.98677 0.64317 -0.08658 -0.02917 0.00282  63   ASP A OD2 
521  N N   . LYS A 39  ? 0.39586 0.93194 0.72472 -0.09522 0.05626  0.01925  64   LYS A N   
522  C CA  . LYS A 39  ? 0.38016 0.86211 0.68444 -0.07228 0.08065  0.03382  64   LYS A CA  
523  C C   . LYS A 39  ? 0.37568 0.81786 0.63110 -0.04597 0.07480  0.04135  64   LYS A C   
524  O O   . LYS A 39  ? 0.35640 0.76328 0.59312 -0.02385 0.09160  0.05433  64   LYS A O   
525  C CB  . LYS A 39  ? 0.38204 0.89264 0.72395 -0.05640 0.09851  0.05199  64   LYS A CB  
526  C CG  . LYS A 39  ? 0.37756 0.90876 0.76591 -0.07852 0.10972  0.04592  64   LYS A CG  
527  C CD  . LYS A 39  ? 0.45963 0.95094 0.84446 -0.06939 0.14439  0.05603  64   LYS A CD  
528  C CE  . LYS A 39  ? 0.40548 0.90129 0.82817 -0.09617 0.16203  0.04788  64   LYS A CE  
529  N NZ  . LYS A 39  ? 0.42898 0.92401 0.86150 -0.08246 0.18704  0.05813  64   LYS A NZ  
543  N N   . LEU A 40  ? 0.21754 0.66171 0.44997 -0.04823 0.05304  0.03304  65   LEU A N   
544  C CA  . LEU A 40  ? 0.21746 0.62163 0.40606 -0.02711 0.04958  0.03908  65   LEU A CA  
545  C C   . LEU A 40  ? 0.27747 0.61958 0.42779 -0.03743 0.05314  0.02546  65   LEU A C   
546  O O   . LEU A 40  ? 0.25719 0.59691 0.40834 -0.06065 0.04777  0.00873  65   LEU A O   
547  C CB  . LEU A 40  ? 0.29284 0.73366 0.47684 -0.02067 0.02687  0.04103  65   LEU A CB  
548  C CG  . LEU A 40  ? 0.27390 0.73661 0.46431 0.00954  0.02818  0.06351  65   LEU A CG  
549  C CD1 . LEU A 40  ? 0.24590 0.74437 0.47963 0.01741  0.04174  0.07623  65   LEU A CD1 
550  C CD2 . LEU A 40  ? 0.31891 0.82864 0.50969 0.01373  0.00462  0.06656  65   LEU A CD2 
562  N N   . LYS A 41  ? 0.42472 0.57460 0.32050 -0.10924 0.04528  -0.06928 66   LYS A N   
563  C CA  . LYS A 41  ? 0.37887 0.50655 0.24080 -0.11745 0.02609  -0.02727 66   LYS A CA  
564  C C   . LYS A 41  ? 0.31434 0.42231 0.18941 -0.09206 0.01659  -0.02691 66   LYS A C   
565  O O   . LYS A 41  ? 0.31255 0.43530 0.19927 -0.08764 0.02743  -0.05887 66   LYS A O   
566  C CB  . LYS A 41  ? 0.38771 0.54087 0.20057 -0.16458 0.02841  -0.01889 66   LYS A CB  
567  C CG  . LYS A 41  ? 0.61115 0.78052 0.39696 -0.20011 0.03707  -0.01462 66   LYS A CG  
568  C CD  . LYS A 41  ? 0.75716 0.89508 0.52046 -0.20783 0.01264  0.03772  66   LYS A CD  
569  C CE  . LYS A 41  ? 1.00321 1.14784 0.75543 -0.23188 0.02094  0.03656  66   LYS A CE  
570  N NZ  . LYS A 41  ? 1.11005 1.21864 0.85642 -0.23364 -0.00513 0.08095  66   LYS A NZ  
584  N N   . TRP A 42  ? 0.32358 0.39802 0.20030 -0.07685 -0.00205 0.00695  67   TRP A N   
585  C CA  . TRP A 42  ? 0.30202 0.35397 0.19375 -0.05249 -0.00948 0.00666  67   TRP A CA  
586  C C   . TRP A 42  ? 0.33427 0.37551 0.21509 -0.06060 -0.02808 0.04233  67   TRP A C   
587  O O   . TRP A 42  ? 0.34093 0.38125 0.21031 -0.07772 -0.03949 0.07202  67   TRP A O   
588  C CB  . TRP A 42  ? 0.28411 0.29996 0.20472 -0.02007 -0.01097 0.00387  67   TRP A CB  
589  C CG  . TRP A 42  ? 0.30746 0.32770 0.24769 -0.00854 -0.00145 -0.02532 67   TRP A CG  
590  C CD1 . TRP A 42  ? 0.28783 0.31315 0.23663 -0.01110 0.00267  -0.02689 67   TRP A CD1 
591  C CD2 . TRP A 42  ? 0.24449 0.26292 0.20455 0.00774  0.00157  -0.05584 67   TRP A CD2 
592  N NE1 . TRP A 42  ? 0.26762 0.29819 0.24417 0.00266  0.00634  -0.05635 67   TRP A NE1 
593  C CE2 . TRP A 42  ? 0.31015 0.33444 0.29566 0.01509  0.00438  -0.07341 67   TRP A CE2 
594  C CE3 . TRP A 42  ? 0.29548 0.30764 0.25656 0.01565  0.00081  -0.06978 67   TRP A CE3 
595  C CZ2 . TRP A 42  ? 0.27847 0.30031 0.29602 0.03188  0.00239  -0.10165 67   TRP A CZ2 
596  C CZ3 . TRP A 42  ? 0.31042 0.31740 0.29839 0.03160  0.00148  -0.09892 67   TRP A CZ3 
597  C CH2 . TRP A 42  ? 0.26187 0.27289 0.28059 0.04039  0.00035  -0.11344 67   TRP A CH2 
608  N N   . CYS A 43  ? 0.33504 0.36736 0.22326 -0.04882 -0.03316 0.03984  68   CYS A N   
609  C CA  . CYS A 43  ? 0.33114 0.34844 0.22957 -0.04707 -0.05232 0.07157  68   CYS A CA  
610  C C   . CYS A 43  ? 0.30602 0.30107 0.22676 -0.02212 -0.04989 0.05903  68   CYS A C   
611  O O   . CYS A 43  ? 0.26889 0.26077 0.18724 -0.01120 -0.03734 0.02963  68   CYS A O   
612  C CB  . CYS A 43  ? 0.39387 0.43723 0.26392 -0.07941 -0.06731 0.09068  68   CYS A CB  
613  S SG  . CYS A 43  ? 0.53360 0.59621 0.38812 -0.08777 -0.06571 0.07204  68   CYS A SG  
619  N N   . LEU A 44  ? 0.35181 0.32806 0.29925 -0.01330 -0.06180 0.08067  69   LEU A N   
620  C CA  . LEU A 44  ? 0.36386 0.31991 0.33118 0.00423  -0.05786 0.06858  69   LEU A CA  
621  C C   . LEU A 44  ? 0.28746 0.26387 0.25403 -0.00726 -0.07092 0.07689  69   LEU A C   
622  O O   . LEU A 44  ? 0.30160 0.29580 0.26961 -0.02428 -0.09071 0.10483  69   LEU A O   
623  C CB  . LEU A 44  ? 0.29177 0.21535 0.29740 0.01946  -0.05658 0.07858  69   LEU A CB  
624  C CG  . LEU A 44  ? 0.30039 0.20223 0.30512 0.02646  -0.04536 0.07412  69   LEU A CG  
625  C CD1 . LEU A 44  ? 0.32355 0.20751 0.35163 0.03346  -0.03122 0.06646  69   LEU A CD1 
626  C CD2 . LEU A 44  ? 0.37808 0.27175 0.35797 0.03311  -0.03323 0.04563  69   LEU A CD2 
638  N N   . ARG A 45  ? 0.31238 0.28520 0.27321 -0.00092 -0.06230 0.05382  70   ARG A N   
639  C CA  . ARG A 45  ? 0.30900 0.29797 0.27294 -0.00998 -0.07277 0.05819  70   ARG A CA  
640  C C   . ARG A 45  ? 0.30535 0.26835 0.30302 0.00738  -0.06728 0.05019  70   ARG A C   
641  O O   . ARG A 45  ? 0.27847 0.21397 0.26855 0.01980  -0.05032 0.02677  70   ARG A O   
642  C CB  . ARG A 45  ? 0.46499 0.47457 0.39105 -0.02334 -0.06458 0.03449  70   ARG A CB  
643  C CG  . ARG A 45  ? 0.42824 0.46763 0.31842 -0.04771 -0.06260 0.03229  70   ARG A CG  
644  C CD  . ARG A 45  ? 0.45426 0.51334 0.31610 -0.06278 -0.05154 0.00492  70   ARG A CD  
645  N NE  . ARG A 45  ? 0.60837 0.70275 0.43328 -0.09919 -0.05240 0.00681  70   ARG A NE  
646  C CZ  . ARG A 45  ? 0.71300 0.82703 0.51293 -0.11615 -0.03197 -0.02673 70   ARG A CZ  
647  N NH1 . ARG A 45  ? 0.62277 0.72396 0.43499 -0.09718 -0.01349 -0.06215 70   ARG A NH1 
648  N NH2 . ARG A 45  ? 0.70097 0.84134 0.47640 -0.15049 -0.02757 -0.02420 70   ARG A NH2 
662  N N   . VAL A 46  ? 0.27996 0.25183 0.31550 0.00512  -0.08287 0.06912  71   VAL A N   
663  C CA  . VAL A 46  ? 0.25691 0.21160 0.33252 0.01658  -0.07571 0.05840  71   VAL A CA  
664  C C   . VAL A 46  ? 0.24629 0.22678 0.32917 0.00598  -0.08817 0.05970  71   VAL A C   
665  O O   . VAL A 46  ? 0.26294 0.27221 0.35631 -0.00762 -0.11423 0.08636  71   VAL A O   
666  C CB  . VAL A 46  ? 0.30424 0.24598 0.44156 0.02622  -0.08048 0.07537  71   VAL A CB  
667  C CG1 . VAL A 46  ? 0.23056 0.17458 0.42521 0.03022  -0.08159 0.07041  71   VAL A CG1 
668  C CG2 . VAL A 46  ? 0.30199 0.20933 0.43047 0.03619  -0.05735 0.06037  71   VAL A CG2 
678  N N   . ASN A 47  ? 0.27525 0.24327 0.35012 0.00924  -0.07155 0.03228  72   ASN A N   
679  C CA  . ASN A 47  ? 0.24617 0.23514 0.33487 0.00031  -0.07933 0.02883  72   ASN A CA  
680  C C   . ASN A 47  ? 0.25883 0.23390 0.40946 0.01024  -0.07103 0.02031  72   ASN A C   
681  O O   . ASN A 47  ? 0.23089 0.17399 0.37170 0.01536  -0.04565 -0.00693 72   ASN A O   
682  C CB  . ASN A 47  ? 0.34485 0.32945 0.37940 -0.00658 -0.06439 0.00106  72   ASN A CB  
683  C CG  . ASN A 47  ? 0.38408 0.37985 0.36667 -0.01559 -0.06436 -0.00028 72   ASN A CG  
684  O OD1 . ASN A 47  ? 0.39143 0.36392 0.34869 -0.00689 -0.04912 -0.01713 72   ASN A OD1 
685  N ND2 . ASN A 47  ? 0.43426 0.46615 0.40428 -0.03564 -0.08243 0.01751  72   ASN A ND2 
692  N N   . PRO A 48  ? 0.21590 0.37505 0.28162 -0.04100 -0.01211 -0.03971 73   PRO A N   
693  C CA  . PRO A 48  ? 0.23461 0.40604 0.30802 -0.02894 -0.02086 -0.03980 73   PRO A CA  
694  C C   . PRO A 48  ? 0.19336 0.38617 0.29232 -0.03335 -0.00874 -0.04508 73   PRO A C   
695  O O   . PRO A 48  ? 0.25905 0.46527 0.36798 -0.02403 -0.00539 -0.04045 73   PRO A O   
696  C CB  . PRO A 48  ? 0.22869 0.40321 0.28351 -0.02123 -0.03992 -0.04314 73   PRO A CB  
697  C CG  . PRO A 48  ? 0.31908 0.46893 0.34664 -0.02979 -0.04281 -0.03646 73   PRO A CG  
698  C CD  . PRO A 48  ? 0.26789 0.42078 0.30645 -0.04434 -0.02315 -0.03993 73   PRO A CD  
706  N N   . LYS A 49  ? 0.15198 0.34655 0.25878 -0.04953 -0.00110 -0.05525 74   LYS A N   
707  C CA  . LYS A 49  ? 0.17741 0.38554 0.30904 -0.06373 0.01071  -0.06122 74   LYS A CA  
708  C C   . LYS A 49  ? 0.18993 0.36235 0.32203 -0.07583 0.02889  -0.06357 74   LYS A C   
709  O O   . LYS A 49  ? 0.22411 0.38954 0.36512 -0.09651 0.03534  -0.07774 74   LYS A O   
710  C CB  . LYS A 49  ? 0.17350 0.41849 0.31503 -0.07443 -0.00243 -0.07726 74   LYS A CB  
711  C CG  . LYS A 49  ? 0.20311 0.48877 0.35177 -0.05510 -0.01664 -0.07365 74   LYS A CG  
712  C CD  . LYS A 49  ? 0.22492 0.54865 0.38484 -0.06073 -0.02819 -0.08522 74   LYS A CD  
713  C CE  . LYS A 49  ? 0.28572 0.64715 0.45404 -0.03560 -0.03681 -0.08031 74   LYS A CE  
714  N NZ  . LYS A 49  ? 0.31712 0.71815 0.49657 -0.03875 -0.04873 -0.08983 74   LYS A NZ  
728  N N   . GLY A 50  ? 0.26341 0.41234 0.38552 -0.06246 0.03603  -0.05193 75   GLY A N   
729  C CA  . GLY A 50  ? 0.25847 0.37248 0.38075 -0.06248 0.05432  -0.05102 75   GLY A CA  
730  C C   . GLY A 50  ? 0.28285 0.37802 0.39090 -0.06977 0.05801  -0.07069 75   GLY A C   
731  O O   . GLY A 50  ? 0.26630 0.37825 0.35835 -0.07224 0.04623  -0.08028 75   GLY A O   
735  N N   . LEU A 51  ? 0.33940 0.39329 0.44794 -0.07126 0.07589  -0.07612 76   LEU A N   
736  C CA  . LEU A 51  ? 0.34940 0.37440 0.43954 -0.07305 0.08428  -0.09883 76   LEU A CA  
737  C C   . LEU A 51  ? 0.40205 0.38367 0.49121 -0.09641 0.09199  -0.12014 76   LEU A C   
738  O O   . LEU A 51  ? 0.47150 0.42986 0.53900 -0.10231 0.09442  -0.14786 76   LEU A O   
739  C CB  . LEU A 51  ? 0.37888 0.38384 0.46547 -0.04462 0.10083  -0.08966 76   LEU A CB  
740  C CG  . LEU A 51  ? 0.35733 0.39978 0.45575 -0.02389 0.09679  -0.06461 76   LEU A CG  
741  C CD1 . LEU A 51  ? 0.53650 0.55937 0.64096 0.00482  0.11357  -0.05456 76   LEU A CD1 
742  C CD2 . LEU A 51  ? 0.41182 0.49266 0.49950 -0.02602 0.08850  -0.06915 76   LEU A CD2 
754  N N   . ASP A 52  ? 0.44772 0.41478 0.55659 -0.11161 0.09761  -0.10896 77   ASP A N   
755  C CA  . ASP A 52  ? 0.56901 0.48385 0.67986 -0.14047 0.10815  -0.12548 77   ASP A CA  
756  C C   . ASP A 52  ? 0.61246 0.55302 0.75303 -0.16584 0.10840  -0.10937 77   ASP A C   
757  O O   . ASP A 52  ? 0.53286 0.51859 0.68594 -0.15129 0.10487  -0.08430 77   ASP A O   
758  C CB  . ASP A 52  ? 0.50734 0.33959 0.60249 -0.12203 0.13116  -0.12051 77   ASP A CB  
759  C CG  . ASP A 52  ? 0.61852 0.45124 0.71978 -0.08843 0.14062  -0.08105 77   ASP A CG  
760  O OD1 . ASP A 52  ? 0.54765 0.43319 0.66499 -0.08899 0.13216  -0.05946 77   ASP A OD1 
761  O OD2 . ASP A 52  ? 0.69792 0.48162 0.78566 -0.05742 0.15518  -0.07334 77   ASP A OD2 
766  N N   . GLU A 53  ? 0.68872 0.60483 0.84022 -0.20631 0.11250  -0.12707 78   GLU A N   
767  C CA  . GLU A 53  ? 0.64497 0.59122 0.82466 -0.22968 0.11580  -0.10790 78   GLU A CA  
768  C C   . GLU A 53  ? 0.66367 0.59255 0.84674 -0.21117 0.13715  -0.06808 78   GLU A C   
769  O O   . GLU A 53  ? 0.64902 0.63814 0.85065 -0.20932 0.13632  -0.04776 78   GLU A O   
770  C CB  . GLU A 53  ? 0.79499 0.69904 0.97346 -0.26343 0.11709  -0.12047 78   GLU A CB  
771  C CG  . GLU A 53  ? 0.85853 0.81364 1.06913 -0.28961 0.11477  -0.10346 78   GLU A CG  
772  C CD  . GLU A 53  ? 0.84953 0.90745 1.08349 -0.28823 0.08995  -0.11293 78   GLU A CD  
773  O OE1 . GLU A 53  ? 0.88757 0.96530 1.10888 -0.28260 0.06964  -0.14005 78   GLU A OE1 
774  O OE2 . GLU A 53  ? 0.77621 0.89276 1.03788 -0.28915 0.09199  -0.09167 78   GLU A OE2 
781  N N   . GLU A 54  ? 0.62425 0.47740 0.78133 -0.18568 0.15214  -0.05488 79   GLU A N   
782  C CA  . GLU A 54  ? 0.66098 0.50103 0.80953 -0.15586 0.16573  -0.01389 79   GLU A CA  
783  C C   . GLU A 54  ? 0.61012 0.53404 0.76544 -0.13101 0.15092  0.00005  79   GLU A C   
784  O O   . GLU A 54  ? 0.57094 0.52737 0.73350 -0.13198 0.15734  0.02415  79   GLU A O   
785  C CB  . GLU A 54  ? 0.70878 0.47866 0.82937 -0.11729 0.17465  -0.00753 79   GLU A CB  
786  C CG  . GLU A 54  ? 0.64478 0.42152 0.75403 -0.07419 0.17916  0.03168  79   GLU A CG  
787  C CD  . GLU A 54  ? 0.87207 0.57849 0.96642 -0.07454 0.20231  0.06634  79   GLU A CD  
788  O OE1 . GLU A 54  ? 0.98043 0.60980 1.07015 -0.10444 0.21762  0.05866  79   GLU A OE1 
789  O OE2 . GLU A 54  ? 0.92043 0.64471 1.00362 -0.04633 0.20475  0.10173  79   GLU A OE2 
796  N N   . SER A 55  ? 0.52809 0.48187 0.67647 -0.10782 0.13296  -0.01428 80   SER A N   
797  C CA  . SER A 55  ? 0.40931 0.42031 0.55664 -0.08219 0.11870  -0.00199 80   SER A CA  
798  C C   . SER A 55  ? 0.30735 0.38087 0.46775 -0.09402 0.10008  -0.01811 80   SER A C   
799  O O   . SER A 55  ? 0.21891 0.32644 0.37286 -0.07402 0.08481  -0.01595 80   SER A O   
800  C CB  . SER A 55  ? 0.38243 0.38695 0.51585 -0.05130 0.11209  -0.00252 80   SER A CB  
801  O OG  . SER A 55  ? 0.40250 0.39923 0.53140 -0.05847 0.10703  -0.02953 80   SER A OG  
807  N N   . LYS A 56  ? 0.26705 0.35646 0.44617 -0.12596 0.09978  -0.03429 81   LYS A N   
808  C CA  . LYS A 56  ? 0.24938 0.40154 0.44055 -0.13027 0.07889  -0.05079 81   LYS A CA  
809  C C   . LYS A 56  ? 0.26537 0.46958 0.46395 -0.11207 0.07481  -0.03571 81   LYS A C   
810  O O   . LYS A 56  ? 0.21768 0.46063 0.41459 -0.09804 0.05511  -0.04479 81   LYS A O   
811  C CB  . LYS A 56  ? 0.33228 0.49956 0.54475 -0.16727 0.07657  -0.07206 81   LYS A CB  
812  C CG  . LYS A 56  ? 0.35373 0.56307 0.58930 -0.17747 0.07907  -0.05948 81   LYS A CG  
813  C CD  . LYS A 56  ? 0.48944 0.71839 0.73932 -0.20408 0.06627  -0.07952 81   LYS A CD  
814  C CE  . LYS A 56  ? 0.48002 0.74096 0.76101 -0.22422 0.07690  -0.06531 81   LYS A CE  
815  N NZ  . LYS A 56  ? 0.77862 1.04829 1.07665 -0.25826 0.06708  -0.08542 81   LYS A NZ  
829  N N   . ASP A 57  ? 0.25288 0.45292 0.45265 -0.10827 0.09329  -0.01257 82   ASP A N   
830  C CA  . ASP A 57  ? 0.27020 0.51567 0.46802 -0.08667 0.09260  -0.00017 82   ASP A CA  
831  C C   . ASP A 57  ? 0.27002 0.49945 0.43737 -0.05318 0.08096  0.00685  82   ASP A C   
832  O O   . ASP A 57  ? 0.18077 0.43703 0.33695 -0.03276 0.07942  0.01404  82   ASP A O   
833  C CB  . ASP A 57  ? 0.28358 0.53307 0.48738 -0.09710 0.11959  0.02393  82   ASP A CB  
834  C CG  . ASP A 57  ? 0.37066 0.64266 0.60648 -0.13044 0.12828  0.02090  82   ASP A CG  
835  O OD1 . ASP A 57  ? 0.44807 0.77023 0.70200 -0.12649 0.11303  0.00656  82   ASP A OD1 
836  O OD2 . ASP A 57  ? 0.45030 0.67957 0.68752 -0.15658 0.14672  0.03434  82   ASP A OD2 
841  N N   . TYR A 58  ? 0.21484 0.40502 0.36907 -0.04841 0.07398  0.00357  83   TYR A N   
842  C CA  . TYR A 58  ? 0.23127 0.41310 0.36427 -0.02407 0.06284  0.01002  83   TYR A CA  
843  C C   . TYR A 58  ? 0.26797 0.44693 0.39559 -0.02332 0.04404  -0.00564 83   TYR A C   
844  O O   . TYR A 58  ? 0.20240 0.37410 0.33589 -0.03803 0.04273  -0.01892 83   TYR A O   
845  C CB  . TYR A 58  ? 0.22241 0.36994 0.34682 -0.01462 0.07470  0.02768  83   TYR A CB  
846  C CG  . TYR A 58  ? 0.23867 0.37999 0.35667 -0.01086 0.09347  0.05153  83   TYR A CG  
847  C CD1 . TYR A 58  ? 0.28642 0.40928 0.41713 -0.03466 0.11420  0.05725  83   TYR A CD1 
848  C CD2 . TYR A 58  ? 0.22558 0.37854 0.32184 0.01358  0.09045  0.06911  83   TYR A CD2 
849  C CE1 . TYR A 58  ? 0.28747 0.39894 0.40881 -0.03494 0.13486  0.08427  83   TYR A CE1 
850  C CE2 . TYR A 58  ? 0.26221 0.40878 0.34439 0.01871  0.10892  0.09503  83   TYR A CE2 
851  C CZ  . TYR A 58  ? 0.31439 0.43823 0.40857 -0.00580 0.13316  0.10532  83   TYR A CZ  
852  O OH  . TYR A 58  ? 0.45282 0.56626 0.52944 -0.00417 0.15519  0.13670  83   TYR A OH  
862  N N   . LEU A 59  ? 0.21441 0.39703 0.32718 -0.00830 0.02996  -0.00354 84   LEU A N   
863  C CA  . LEU A 59  ? 0.13837 0.31208 0.24399 -0.01069 0.01676  -0.01037 84   LEU A CA  
864  C C   . LEU A 59  ? 0.17363 0.33973 0.28309 -0.00626 0.02383  -0.00104 84   LEU A C   
865  O O   . LEU A 59  ? 0.19593 0.36891 0.30317 0.00701  0.02473  0.01089  84   LEU A O   
866  C CB  . LEU A 59  ? 0.12052 0.29719 0.20939 -0.00250 -0.00303 -0.01446 84   LEU A CB  
867  C CG  . LEU A 59  ? 0.19247 0.35597 0.27295 -0.01118 -0.01445 -0.01625 84   LEU A CG  
868  C CD1 . LEU A 59  ? 0.26265 0.41138 0.32274 -0.00729 -0.03253 -0.02339 84   LEU A CD1 
869  C CD2 . LEU A 59  ? 0.26451 0.43500 0.34798 -0.01007 -0.01745 -0.00922 84   LEU A CD2 
881  N N   . SER A 60  ? 0.27853 0.23256 0.35156 -0.04206 0.00062  -0.04617 85   SER A N   
882  C CA  . SER A 60  ? 0.24976 0.19684 0.30860 -0.03500 -0.00102 -0.04773 85   SER A CA  
883  C C   . SER A 60  ? 0.24973 0.21433 0.29344 -0.02933 -0.00492 -0.03556 85   SER A C   
884  O O   . SER A 60  ? 0.20822 0.19629 0.25326 -0.02901 -0.00799 -0.03065 85   SER A O   
885  C CB  . SER A 60  ? 0.24670 0.20605 0.31116 -0.03389 -0.00412 -0.06806 85   SER A CB  
886  O OG  . SER A 60  ? 0.25834 0.20851 0.33905 -0.04346 -0.00026 -0.08287 85   SER A OG  
892  N N   . LEU A 61  ? 0.22542 0.18185 0.25722 -0.02446 -0.00462 -0.02975 86   LEU A N   
893  C CA  . LEU A 61  ? 0.24097 0.21403 0.25912 -0.02169 -0.00720 -0.01952 86   LEU A CA  
894  C C   . LEU A 61  ? 0.28187 0.26247 0.29663 -0.01313 -0.00993 -0.02106 86   LEU A C   
895  O O   . LEU A 61  ? 0.24785 0.21142 0.26589 -0.00995 -0.00772 -0.01794 86   LEU A O   
896  C CB  . LEU A 61  ? 0.31034 0.26776 0.31729 -0.02965 -0.00140 -0.00574 86   LEU A CB  
897  C CG  . LEU A 61  ? 0.24668 0.21778 0.23915 -0.03178 -0.00109 0.00361  86   LEU A CG  
898  C CD1 . LEU A 61  ? 0.27808 0.27175 0.27358 -0.02792 -0.00218 0.00405  86   LEU A CD1 
899  C CD2 . LEU A 61  ? 0.33308 0.28258 0.31403 -0.04494 0.00832  0.01139  86   LEU A CD2 
911  N N   . TYR A 62  ? 0.24474 0.25217 0.25537 -0.00839 -0.01350 -0.02403 87   TYR A N   
912  C CA  . TYR A 62  ? 0.25612 0.27432 0.26853 0.00103  -0.01367 -0.02805 87   TYR A CA  
913  C C   . TYR A 62  ? 0.25799 0.30130 0.25990 0.00202  -0.01583 -0.01909 87   TYR A C   
914  O O   . TYR A 62  ? 0.19696 0.25293 0.19105 -0.00277 -0.01679 -0.01542 87   TYR A O   
915  C CB  . TYR A 62  ? 0.24680 0.27373 0.26635 0.00489  -0.01216 -0.04873 87   TYR A CB  
916  C CG  . TYR A 62  ? 0.26639 0.26719 0.29895 0.00294  -0.00705 -0.06136 87   TYR A CG  
917  C CD1 . TYR A 62  ? 0.27722 0.27400 0.31323 -0.00705 -0.00873 -0.06803 87   TYR A CD1 
918  C CD2 . TYR A 62  ? 0.33024 0.31128 0.37495 0.01134  0.00108  -0.06532 87   TYR A CD2 
919  C CE1 . TYR A 62  ? 0.33092 0.30399 0.37992 -0.01148 -0.00259 -0.08124 87   TYR A CE1 
920  C CE2 . TYR A 62  ? 0.34302 0.29494 0.40090 0.00862  0.00901  -0.07642 87   TYR A CE2 
921  C CZ  . TYR A 62  ? 0.35528 0.30354 0.41390 -0.00421 0.00702  -0.08599 87   TYR A CZ  
922  O OH  . TYR A 62  ? 0.39933 0.31909 0.47218 -0.00950 0.01651  -0.09950 87   TYR A OH  
932  N N   . LEU A 63  ? 0.25202 0.30363 0.25702 0.00881  -0.01546 -0.01375 88   LEU A N   
933  C CA  . LEU A 63  ? 0.25297 0.33175 0.25169 0.00933  -0.01647 -0.00663 88   LEU A CA  
934  C C   . LEU A 63  ? 0.16695 0.26371 0.17371 0.02049  -0.01317 -0.01942 88   LEU A C   
935  O O   . LEU A 63  ? 0.19488 0.28293 0.21704 0.03062  -0.00880 -0.02491 88   LEU A O   
936  C CB  . LEU A 63  ? 0.16833 0.25191 0.16717 0.00689  -0.01870 0.00939  88   LEU A CB  
937  C CG  . LEU A 63  ? 0.18727 0.30206 0.18288 0.00447  -0.01968 0.01725  88   LEU A CG  
938  C CD1 . LEU A 63  ? 0.31271 0.42990 0.29246 -0.00767 -0.01703 0.01761  88   LEU A CD1 
939  C CD2 . LEU A 63  ? 0.21706 0.34305 0.21404 -0.00055 -0.02412 0.03256  88   LEU A CD2 
951  N N   . LEU A 64  ? 0.20887 0.32878 0.20546 0.01848  -0.01285 -0.02358 89   LEU A N   
952  C CA  . LEU A 64  ? 0.22973 0.37121 0.22751 0.02559  -0.00781 -0.03731 89   LEU A CA  
953  C C   . LEU A 64  ? 0.20907 0.37785 0.20576 0.02759  -0.00553 -0.02756 89   LEU A C   
954  O O   . LEU A 64  ? 0.22641 0.40461 0.21186 0.01900  -0.00789 -0.01486 89   LEU A O   
955  C CB  . LEU A 64  ? 0.27670 0.43013 0.26050 0.01951  -0.00976 -0.04811 89   LEU A CB  
956  C CG  . LEU A 64  ? 0.30447 0.47758 0.28288 0.02144  -0.00427 -0.06909 89   LEU A CG  
957  C CD1 . LEU A 64  ? 0.43789 0.62877 0.40068 0.01226  -0.01010 -0.07566 89   LEU A CD1 
958  C CD2 . LEU A 64  ? 0.35455 0.55274 0.32900 0.02577  0.00130  -0.06542 89   LEU A CD2 
970  N N   . LEU A 65  ? 0.18573 0.36631 0.19704 0.03868  0.00147  -0.03348 90   LEU A N   
971  C CA  . LEU A 65  ? 0.16594 0.37811 0.17883 0.04062  0.00549  -0.02763 90   LEU A CA  
972  C C   . LEU A 65  ? 0.27070 0.50167 0.26739 0.03831  0.01110  -0.04112 90   LEU A C   
973  O O   . LEU A 65  ? 0.26119 0.49167 0.25936 0.04361  0.01906  -0.06132 90   LEU A O   
974  C CB  . LEU A 65  ? 0.20702 0.42813 0.24772 0.05545  0.01244  -0.02588 90   LEU A CB  
975  C CG  . LEU A 65  ? 0.21714 0.47576 0.26718 0.05888  0.01795  -0.01960 90   LEU A CG  
976  C CD1 . LEU A 65  ? 0.17768 0.45248 0.21898 0.04483  0.00879  -0.00042 90   LEU A CD1 
977  C CD2 . LEU A 65  ? 0.17735 0.44385 0.26222 0.07717  0.02603  -0.01616 90   LEU A CD2 
989  N N   . VAL A 66  ? 0.23452 0.48268 0.21494 0.02921  0.00901  -0.03005 91   VAL A N   
990  C CA  . VAL A 66  ? 0.24436 0.51493 0.20655 0.02630  0.01359  -0.03720 91   VAL A CA  
991  C C   . VAL A 66  ? 0.23373 0.53017 0.20163 0.03000  0.02329  -0.03863 91   VAL A C   
992  O O   . VAL A 66  ? 0.28990 0.59426 0.25027 0.02908  0.02763  -0.04987 91   VAL A O   
993  C CB  . VAL A 66  ? 0.21198 0.47487 0.16447 0.01542  0.00679  -0.01938 91   VAL A CB  
994  C CG1 . VAL A 66  ? 0.22917 0.50725 0.17465 0.01223  0.00897  -0.01844 91   VAL A CG1 
995  C CG2 . VAL A 66  ? 0.22270 0.46469 0.17190 0.01309  -0.00039 -0.02008 91   VAL A CG2 
1005 N N   . SER A 67  ? 0.25692 0.56545 0.24043 0.03184  0.02552  -0.02643 92   SER A N   
1006 C CA  . SER A 67  ? 0.22204 0.55264 0.21493 0.03415  0.03303  -0.02574 92   SER A CA  
1007 C C   . SER A 67  ? 0.18936 0.53522 0.21029 0.03981  0.03368  -0.01483 92   SER A C   
1008 O O   . SER A 67  ? 0.23903 0.58102 0.26242 0.03222  0.02490  -0.00077 92   SER A O   
1009 C CB  . SER A 67  ? 0.28708 0.62128 0.26549 0.02143  0.03022  -0.01406 92   SER A CB  
1010 O OG  . SER A 67  ? 0.34561 0.70086 0.33188 0.02303  0.03842  -0.01461 92   SER A OG  
1016 N N   . CYS A 68  ? 0.17673 0.53667 0.21902 0.05122  0.04291  -0.01995 93   CYS A N   
1017 C CA  . CYS A 68  ? 0.24420 0.62352 0.31491 0.05550  0.04123  -0.00491 93   CYS A CA  
1018 C C   . CYS A 68  ? 0.22680 0.62543 0.30856 0.06013  0.05339  -0.00917 93   CYS A C   
1019 O O   . CYS A 68  ? 0.22704 0.61985 0.29882 0.06342  0.06502  -0.02629 93   CYS A O   
1020 C CB  . CYS A 68  ? 0.18640 0.55753 0.28681 0.07132  0.03950  -0.00081 93   CYS A CB  
1021 S SG  . CYS A 68  ? 0.26965 0.61974 0.38822 0.09299  0.05807  -0.02399 93   CYS A SG  
1027 N N   . PRO A 69  ? 0.21154 0.63437 0.31229 0.05800  0.05105  0.00571  94   PRO A N   
1028 C CA  . PRO A 69  ? 0.24453 0.68854 0.35598 0.05993  0.06302  0.00286  94   PRO A CA  
1029 C C   . PRO A 69  ? 0.21756 0.67018 0.36938 0.08046  0.07620  0.00023  94   PRO A C   
1030 O O   . PRO A 69  ? 0.36034 0.83083 0.52546 0.08319  0.08889  -0.00295 94   PRO A O   
1031 C CB  . PRO A 69  ? 0.28703 0.75314 0.39809 0.04412  0.05326  0.01995  94   PRO A CB  
1032 C CG  . PRO A 69  ? 0.28140 0.74526 0.40262 0.04363  0.03880  0.03398  94   PRO A CG  
1033 C CD  . PRO A 69  ? 0.25767 0.69009 0.36507 0.04898  0.03657  0.02513  94   PRO A CD  
1041 N N   . LYS A 70  ? 0.21146 0.65144 0.38658 0.09487  0.07432  0.00395  95   LYS A N   
1042 C CA  . LYS A 70  ? 0.30615 0.74607 0.52452 0.11678  0.09016  0.00172  95   LYS A CA  
1043 C C   . LYS A 70  ? 0.38669 0.78899 0.60289 0.12750  0.09909  -0.01535 95   LYS A C   
1044 O O   . LYS A 70  ? 0.44301 0.82761 0.62389 0.11844  0.10258  -0.03511 95   LYS A O   
1045 C CB  . LYS A 70  ? 0.32942 0.79156 0.58401 0.12422  0.07958  0.02746  95   LYS A CB  
1048 N N   . SER A 71  ? 0.38064 0.76920 0.63140 0.14486  0.10164  -0.00775 96   SER A N   
1049 C CA  . SER A 71  ? 0.36890 0.71753 0.62253 0.15533  0.11629  -0.02784 96   SER A CA  
1050 C C   . SER A 71  ? 0.55413 0.88038 0.79473 0.15375  0.10006  -0.01998 96   SER A C   
1051 O O   . SER A 71  ? 0.48747 0.78993 0.69761 0.14627  0.10110  -0.03979 96   SER A O   
1052 C CB  . SER A 71  ? 0.54833 0.88770 0.85183 0.17703  0.13617  -0.03122 96   SER A CB  
1053 O OG  . SER A 71  ? 0.68317 1.03399 1.01461 0.18785  0.12043  -0.00008 96   SER A OG  
1059 N N   . GLU A 72  ? 0.46205 0.79499 0.72319 0.15940  0.08494  0.00809  97   GLU A N   
1060 C CA  . GLU A 72  ? 0.43609 0.74563 0.68635 0.15779  0.07148  0.01771  97   GLU A CA  
1061 C C   . GLU A 72  ? 0.41540 0.75134 0.65222 0.14258  0.04643  0.04437  97   GLU A C   
1062 O O   . GLU A 72  ? 0.32821 0.69659 0.57698 0.13958  0.04044  0.06060  97   GLU A O   
1063 C CB  . GLU A 72  ? 0.36815 0.64629 0.65072 0.17727  0.08036  0.02453  97   GLU A CB  
1064 C CG  . GLU A 72  ? 0.38955 0.68858 0.70829 0.19042  0.07859  0.05050  97   GLU A CG  
1065 C CD  . GLU A 72  ? 0.46081 0.72341 0.80474 0.20907  0.08862  0.05842  97   GLU A CD  
1066 O OE1 . GLU A 72  ? 0.45171 0.69317 0.81613 0.22345  0.11158  0.04172  97   GLU A OE1 
1067 O OE2 . GLU A 72  ? 0.53690 0.78869 0.87533 0.20703  0.07455  0.08054  97   GLU A OE2 
1074 N N   . VAL A 73  ? 0.31352 0.57578 0.49166 0.06281  0.15014  0.09161  98   VAL A N   
1075 C CA  . VAL A 73  ? 0.21064 0.51299 0.43620 0.05945  0.11693  0.07971  98   VAL A CA  
1076 C C   . VAL A 73  ? 0.26852 0.54276 0.43875 0.08919  0.09859  0.07259  98   VAL A C   
1077 O O   . VAL A 73  ? 0.27786 0.48997 0.37623 0.09434  0.11496  0.07880  98   VAL A O   
1078 C CB  . VAL A 73  ? 0.25167 0.53345 0.48627 0.02001  0.10910  0.08037  98   VAL A CB  
1079 C CG1 . VAL A 73  ? 0.24496 0.55117 0.51703 0.01456  0.07098  0.06097  98   VAL A CG1 
1080 C CG2 . VAL A 73  ? 0.26969 0.55558 0.53680 -0.00494 0.12802  0.08585  98   VAL A CG2 
1090 N N   . ARG A 74  ? 0.27300 0.59285 0.47615 0.10885  0.06655  0.05750  99   ARG A N   
1091 C CA  . ARG A 74  ? 0.26393 0.55778 0.41035 0.14358  0.05003  0.05277  99   ARG A CA  
1092 C C   . ARG A 74  ? 0.25309 0.55380 0.41650 0.12416  0.01508  0.03590  99   ARG A C   
1093 O O   . ARG A 74  ? 0.20469 0.56649 0.44200 0.10926  -0.00869 0.01861  99   ARG A O   
1094 C CB  . ARG A 74  ? 0.35380 0.69734 0.51126 0.19539  0.04281  0.05028  99   ARG A CB  
1095 C CG  . ARG A 74  ? 0.47654 0.79553 0.57271 0.23465  0.02157  0.04463  99   ARG A CG  
1096 C CD  . ARG A 74  ? 0.52609 0.87875 0.62209 0.27104  0.01221  0.04079  99   ARG A CD  
1097 N NE  . ARG A 74  ? 0.60275 1.02741 0.78738 0.25644  0.00962  0.03243  99   ARG A NE  
1098 C CZ  . ARG A 74  ? 0.58596 1.07477 0.81616 0.27202  -0.01449 0.01606  99   ARG A CZ  
1099 N NH1 . ARG A 74  ? 0.58289 1.07702 0.77175 0.30626  -0.03931 0.00696  99   ARG A NH1 
1100 N NH2 . ARG A 74  ? 0.54527 1.09374 0.86305 0.25275  -0.01027 0.00848  99   ARG A NH2 
1114 N N   . ALA A 75  ? 0.23154 0.46888 0.33148 0.12092  0.01566  0.03854  100  ALA A N   
1115 C CA  . ALA A 75  ? 0.21649 0.45251 0.32667 0.10333  -0.01316 0.02382  100  ALA A CA  
1116 C C   . ALA A 75  ? 0.28540 0.46188 0.32026 0.12062  -0.01361 0.02480  100  ALA A C   
1117 O O   . ALA A 75  ? 0.31192 0.43185 0.28912 0.12614  0.01622  0.03785  100  ALA A O   
1118 C CB  . ALA A 75  ? 0.18591 0.41009 0.32746 0.05490  -0.00700 0.02702  100  ALA A CB  
1124 N N   . LYS A 76  ? 0.29124 0.48015 0.32972 0.12682  -0.04505 0.00798  101  LYS A N   
1125 C CA  . LYS A 76  ? 0.31854 0.45291 0.29638 0.13483  -0.04610 0.00688  101  LYS A CA  
1126 C C   . LYS A 76  ? 0.30323 0.42484 0.30702 0.09166  -0.05353 0.00104  101  LYS A C   
1127 O O   . LYS A 76  ? 0.20758 0.36530 0.27474 0.06349  -0.06489 -0.00571 101  LYS A O   
1128 C CB  . LYS A 76  ? 0.37346 0.52602 0.32633 0.17689  -0.07514 -0.00778 101  LYS A CB  
1129 C CG  . LYS A 76  ? 0.39787 0.57700 0.33826 0.21524  -0.07388 -0.00827 101  LYS A CG  
1130 C CD  . LYS A 76  ? 0.41245 0.60862 0.33379 0.23872  -0.09784 -0.02996 101  LYS A CD  
1131 C CE  . LYS A 76  ? 0.57946 0.71224 0.41325 0.26904  -0.08136 -0.02615 101  LYS A CE  
1132 N NZ  . LYS A 76  ? 0.66732 0.82664 0.47861 0.30489  -0.10058 -0.04523 101  LYS A NZ  
1146 N N   . PHE A 77  ? 0.31839 0.38639 0.27366 0.08835  -0.04310 0.00429  102  PHE A N   
1147 C CA  . PHE A 77  ? 0.28226 0.33461 0.25370 0.05475  -0.04720 0.00152  102  PHE A CA  
1148 C C   . PHE A 77  ? 0.35114 0.36465 0.27590 0.06816  -0.05079 -0.00538 102  PHE A C   
1149 O O   . PHE A 77  ? 0.32673 0.30768 0.19624 0.09622  -0.03487 -0.00097 102  PHE A O   
1150 C CB  . PHE A 77  ? 0.24329 0.27783 0.21408 0.02813  -0.02130 0.01578  102  PHE A CB  
1151 C CG  . PHE A 77  ? 0.32735 0.32260 0.24551 0.03767  0.00967  0.02272  102  PHE A CG  
1152 C CD1 . PHE A 77  ? 0.30649 0.26266 0.19015 0.03296  0.02180  0.01885  102  PHE A CD1 
1153 C CD2 . PHE A 77  ? 0.28777 0.28413 0.19549 0.04941  0.03040  0.03076  102  PHE A CD2 
1154 C CE1 . PHE A 77  ? 0.35744 0.27553 0.20080 0.03599  0.05576  0.02015  102  PHE A CE1 
1155 C CE2 . PHE A 77  ? 0.38016 0.33210 0.24063 0.05511  0.06425  0.03364  102  PHE A CE2 
1156 C CZ  . PHE A 77  ? 0.40806 0.32530 0.25116 0.04344  0.07193  0.02507  102  PHE A CZ  
1166 N N   . LYS A 78  ? 0.28069 0.29414 0.22694 0.05058  -0.06839 -0.01563 103  LYS A N   
1167 C CA  . LYS A 78  ? 0.27398 0.25228 0.18270 0.05986  -0.07106 -0.02307 103  LYS A CA  
1168 C C   . LYS A 78  ? 0.31287 0.27805 0.24242 0.02944  -0.06616 -0.01973 103  LYS A C   
1169 O O   . LYS A 78  ? 0.31781 0.30335 0.29425 0.00830  -0.07759 -0.02076 103  LYS A O   
1170 C CB  . LYS A 78  ? 0.32695 0.32471 0.23809 0.07924  -0.10308 -0.04427 103  LYS A CB  
1171 C CG  . LYS A 78  ? 0.44374 0.41027 0.32821 0.08344  -0.11040 -0.05587 103  LYS A CG  
1172 C CD  . LYS A 78  ? 0.51574 0.50402 0.41088 0.09818  -0.12991 -0.07631 103  LYS A CD  
1173 C CE  . LYS A 78  ? 0.66324 0.62334 0.54656 0.09633  -0.13294 -0.08652 103  LYS A CE  
1174 N NZ  . LYS A 78  ? 0.61641 0.59105 0.49086 0.11927  -0.14951 -0.10629 103  LYS A NZ  
1188 N N   . PHE A 79  ? 0.31281 0.24457 0.20903 0.02885  -0.04602 -0.01557 104  PHE A N   
1189 C CA  . PHE A 79  ? 0.32963 0.25460 0.24070 0.00863  -0.04266 -0.01398 104  PHE A CA  
1190 C C   . PHE A 79  ? 0.33457 0.23286 0.22240 0.02074  -0.04646 -0.02468 104  PHE A C   
1191 O O   . PHE A 79  ? 0.33342 0.20605 0.17789 0.04215  -0.03516 -0.02828 104  PHE A O   
1192 C CB  . PHE A 79  ? 0.37986 0.30119 0.28199 -0.00442 -0.01678 -0.00707 104  PHE A CB  
1193 C CG  . PHE A 79  ? 0.33190 0.27645 0.25018 -0.01638 -0.01018 0.00270  104  PHE A CG  
1194 C CD1 . PHE A 79  ? 0.40471 0.37386 0.35829 -0.02922 -0.02249 0.01130  104  PHE A CD1 
1195 C CD2 . PHE A 79  ? 0.38168 0.31616 0.27582 -0.01421 0.01411  0.00348  104  PHE A CD2 
1196 C CE1 . PHE A 79  ? 0.47119 0.45859 0.43370 -0.03759 -0.01269 0.02140  104  PHE A CE1 
1197 C CE2 . PHE A 79  ? 0.41315 0.36589 0.31712 -0.02335 0.02207  0.01070  104  PHE A CE2 
1198 C CZ  . PHE A 79  ? 0.36541 0.34668 0.30237 -0.03431 0.00804  0.02007  104  PHE A CZ  
1208 N N   . SER A 80  ? 0.31363 0.21258 0.22570 0.01019  -0.05832 -0.02796 105  SER A N   
1209 C CA  . SER A 80  ? 0.29485 0.16842 0.18843 0.02059  -0.06007 -0.03811 105  SER A CA  
1210 C C   . SER A 80  ? 0.31549 0.19224 0.23824 0.00626  -0.06015 -0.03302 105  SER A C   
1211 O O   . SER A 80  ? 0.29737 0.19386 0.24946 -0.00825 -0.06158 -0.02135 105  SER A O   
1212 C CB  . SER A 80  ? 0.42742 0.29686 0.31423 0.03471  -0.08347 -0.05472 105  SER A CB  
1213 O OG  . SER A 80  ? 0.40646 0.29630 0.34165 0.01706  -0.10198 -0.05918 105  SER A OG  
1219 N N   . ILE A 81  ? 0.33423 0.19016 0.24465 0.01501  -0.05664 -0.04017 106  ILE A N   
1220 C CA  . ILE A 81  ? 0.25256 0.11273 0.18537 0.00978  -0.05352 -0.03431 106  ILE A CA  
1221 C C   . ILE A 81  ? 0.32653 0.15986 0.25970 0.01824  -0.06445 -0.04438 106  ILE A C   
1222 O O   . ILE A 81  ? 0.41829 0.24419 0.32887 0.02958  -0.06321 -0.05418 106  ILE A O   
1223 C CB  . ILE A 81  ? 0.26737 0.13351 0.19087 0.01218  -0.03174 -0.03603 106  ILE A CB  
1224 C CG1 . ILE A 81  ? 0.33486 0.22287 0.25797 0.00058  -0.01765 -0.03283 106  ILE A CG1 
1225 C CG2 . ILE A 81  ? 0.30850 0.18837 0.25713 0.01405  -0.03274 -0.03195 106  ILE A CG2 
1226 C CD1 . ILE A 81  ? 0.41359 0.29999 0.32772 -0.00097 0.01016  -0.04306 106  ILE A CD1 
1238 N N   . LEU A 82  ? 0.16069 0.24873 0.22259 -0.02273 0.05854  0.06486  107  LEU A N   
1239 C CA  . LEU A 82  ? 0.23382 0.28670 0.27969 -0.05615 0.05069  0.06242  107  LEU A CA  
1240 C C   . LEU A 82  ? 0.30976 0.29839 0.30221 -0.04544 0.04361  0.05438  107  LEU A C   
1241 O O   . LEU A 82  ? 0.36579 0.32453 0.32797 -0.02737 0.05789  0.05512  107  LEU A O   
1242 C CB  . LEU A 82  ? 0.23944 0.28224 0.28678 -0.08232 0.07187  0.07328  107  LEU A CB  
1243 C CG  . LEU A 82  ? 0.37959 0.37122 0.40712 -0.11777 0.06209  0.06877  107  LEU A CG  
1244 C CD1 . LEU A 82  ? 0.27162 0.30928 0.34187 -0.14765 0.03878  0.06068  107  LEU A CD1 
1245 C CD2 . LEU A 82  ? 0.36831 0.33394 0.39173 -0.12242 0.07806  0.08055  107  LEU A CD2 
1257 N N   . ASN A 83  ? 0.36036 0.33622 0.34037 -0.05402 0.02138  0.04587  108  ASN A N   
1258 C CA  . ASN A 83  ? 0.33195 0.26143 0.26239 -0.04215 0.01562  0.03907  108  ASN A CA  
1259 C C   . ASN A 83  ? 0.39582 0.27334 0.28874 -0.05725 0.01631  0.03243  108  ASN A C   
1260 O O   . ASN A 83  ? 0.35763 0.22511 0.26268 -0.08296 0.01996  0.03419  108  ASN A O   
1261 C CB  . ASN A 83  ? 0.36737 0.31325 0.29565 -0.03412 -0.00617 0.03621  108  ASN A CB  
1262 C CG  . ASN A 83  ? 0.36067 0.31138 0.28709 -0.05163 -0.02727 0.02691  108  ASN A CG  
1263 O OD1 . ASN A 83  ? 0.32195 0.25583 0.24885 -0.07469 -0.02844 0.01970  108  ASN A OD1 
1264 N ND2 . ASN A 83  ? 0.32605 0.29501 0.24543 -0.04085 -0.04503 0.02684  108  ASN A ND2 
1271 N N   . ALA A 84  ? 0.44317 0.29126 0.29321 -0.03924 0.01213  0.02314  109  ALA A N   
1272 C CA  . ALA A 84  ? 0.46178 0.26257 0.27285 -0.04100 0.01146  0.01254  109  ALA A CA  
1273 C C   . ALA A 84  ? 0.56672 0.33468 0.36130 -0.06609 -0.00985 0.00390  109  ALA A C   
1274 O O   . ALA A 84  ? 0.54312 0.27619 0.31536 -0.06852 -0.01130 -0.00264 109  ALA A O   
1275 C CB  . ALA A 84  ? 0.55895 0.35521 0.35525 -0.01139 0.01159  -0.00066 109  ALA A CB  
1281 N N   . LYS A 85  ? 0.45991 0.27349 0.28445 -0.07335 -0.02849 0.00010  110  LYS A N   
1282 C CA  . LYS A 85  ? 0.53762 0.34620 0.36255 -0.09389 -0.05387 -0.01635 110  LYS A CA  
1283 C C   . LYS A 85  ? 0.51312 0.34473 0.39167 -0.13241 -0.05470 -0.01372 110  LYS A C   
1284 O O   . LYS A 85  ? 0.42835 0.25811 0.31608 -0.15147 -0.07273 -0.02851 110  LYS A O   
1285 C CB  . LYS A 85  ? 0.63340 0.48882 0.45955 -0.07748 -0.07466 -0.02144 110  LYS A CB  
1286 C CG  . LYS A 85  ? 0.62918 0.48140 0.42439 -0.04134 -0.06911 -0.02274 110  LYS A CG  
1287 C CD  . LYS A 85  ? 0.66916 0.57982 0.48980 -0.02180 -0.06458 -0.01098 110  LYS A CD  
1288 C CE  . LYS A 85  ? 0.82546 0.76546 0.64827 -0.00148 -0.05567 -0.01255 110  LYS A CE  
1289 N NZ  . LYS A 85  ? 0.95262 0.85906 0.75014 0.00446  -0.05619 -0.02504 110  LYS A NZ  
1303 N N   . GLY A 86  ? 0.37108 0.23339 0.28879 -0.13802 -0.03210 0.00470  111  GLY A N   
1304 C CA  . GLY A 86  ? 0.38940 0.29068 0.36263 -0.17390 -0.02936 0.00997  111  GLY A CA  
1305 C C   . GLY A 86  ? 0.31022 0.30331 0.34084 -0.17217 -0.03973 0.01177  111  GLY A C   
1306 O O   . GLY A 86  ? 0.33522 0.37512 0.41296 -0.20098 -0.04645 0.00904  111  GLY A O   
1310 N N   . GLU A 87  ? 0.26563 0.28505 0.29270 -0.13526 -0.04034 0.01658  112  GLU A N   
1311 C CA  . GLU A 87  ? 0.28224 0.37731 0.35108 -0.12268 -0.05349 0.01813  112  GLU A CA  
1312 C C   . GLU A 87  ? 0.26284 0.38902 0.35290 -0.09570 -0.03403 0.03364  112  GLU A C   
1313 O O   . GLU A 87  ? 0.27699 0.36203 0.33665 -0.07554 -0.01855 0.03980  112  GLU A O   
1314 C CB  . GLU A 87  ? 0.29515 0.38602 0.33376 -0.09944 -0.07638 0.01117  112  GLU A CB  
1315 C CG  . GLU A 87  ? 0.41710 0.53210 0.46141 -0.11628 -0.10623 -0.00712 112  GLU A CG  
1316 C CD  . GLU A 87  ? 0.45607 0.60638 0.49061 -0.08588 -0.12702 -0.00603 112  GLU A CD  
1317 O OE1 . GLU A 87  ? 0.39565 0.52598 0.40228 -0.05674 -0.11915 0.00852  112  GLU A OE1 
1318 O OE2 . GLU A 87  ? 0.37117 0.56494 0.42598 -0.08947 -0.14790 -0.01954 112  GLU A OE2 
1325 N N   . GLU A 88  ? 0.22390 0.42665 0.36534 -0.09280 -0.03688 0.03703  113  GLU A N   
1326 C CA  . GLU A 88  ? 0.16318 0.39587 0.31931 -0.05703 -0.02538 0.04703  113  GLU A CA  
1327 C C   . GLU A 88  ? 0.21823 0.42373 0.34387 -0.02332 -0.03995 0.04813  113  GLU A C   
1328 O O   . GLU A 88  ? 0.22646 0.44706 0.34905 -0.02038 -0.06290 0.04443  113  GLU A O   
1329 C CB  . GLU A 88  ? 0.24171 0.57051 0.45700 -0.05582 -0.02765 0.04857  113  GLU A CB  
1330 C CG  . GLU A 88  ? 0.21352 0.57930 0.46383 -0.08749 -0.00652 0.05458  113  GLU A CG  
1331 C CD  . GLU A 88  ? 0.26232 0.70856 0.55527 -0.07257 -0.00371 0.05363  113  GLU A CD  
1332 O OE1 . GLU A 88  ? 0.35829 0.83034 0.65203 -0.03262 -0.01719 0.05007  113  GLU A OE1 
1333 O OE2 . GLU A 88  ? 0.26124 0.73424 0.57993 -0.09920 0.01111  0.05644  113  GLU A OE2 
1340 N N   . THR A 89  ? 0.14728 0.31258 0.24912 0.00039  -0.02704 0.05376  114  THR A N   
1341 C CA  . THR A 89  ? 0.20494 0.32805 0.27314 0.02236  -0.03682 0.05799  114  THR A CA  
1342 C C   . THR A 89  ? 0.24728 0.36658 0.32038 0.05529  -0.03146 0.06222  114  THR A C   
1343 O O   . THR A 89  ? 0.21408 0.34348 0.29940 0.06224  -0.01411 0.05937  114  THR A O   
1344 C CB  . THR A 89  ? 0.29291 0.35528 0.31757 0.01109  -0.02911 0.05619  114  THR A CB  
1345 O OG1 . THR A 89  ? 0.35673 0.41490 0.37174 -0.01496 -0.03418 0.04849  114  THR A OG1 
1346 C CG2 . THR A 89  ? 0.40171 0.43379 0.39686 0.02449  -0.03968 0.06364  114  THR A CG2 
1354 N N   . LYS A 90  ? 0.21621 0.31853 0.27615 0.07712  -0.04728 0.06931  115  LYS A N   
1355 C CA  . LYS A 90  ? 0.22458 0.28836 0.27389 0.09792  -0.04585 0.06419  115  LYS A CA  
1356 C C   . LYS A 90  ? 0.28595 0.39422 0.36413 0.11943  -0.04272 0.05764  115  LYS A C   
1357 O O   . LYS A 90  ? 0.21572 0.30224 0.28871 0.13321  -0.03599 0.04985  115  LYS A O   
1358 C CB  . LYS A 90  ? 0.26818 0.28308 0.29608 0.09031  -0.03284 0.05819  115  LYS A CB  
1359 C CG  . LYS A 90  ? 0.32971 0.30388 0.32934 0.06848  -0.03733 0.06161  115  LYS A CG  
1360 C CD  . LYS A 90  ? 0.31260 0.26079 0.31094 0.06713  -0.04829 0.06965  115  LYS A CD  
1361 C CE  . LYS A 90  ? 0.37659 0.32077 0.36031 0.04537  -0.04929 0.07773  115  LYS A CE  
1362 N NZ  . LYS A 90  ? 0.46929 0.41438 0.43348 0.05592  -0.06618 0.07843  115  LYS A NZ  
1376 N N   . ALA A 91  ? 0.21200 0.38525 0.31902 0.12039  -0.05000 0.05873  116  ALA A N   
1377 C CA  . ALA A 91  ? 0.21024 0.43657 0.34458 0.13764  -0.04517 0.05237  116  ALA A CA  
1378 C C   . ALA A 91  ? 0.25450 0.44353 0.36978 0.16648  -0.05377 0.05025  116  ALA A C   
1379 O O   . ALA A 91  ? 0.27948 0.43379 0.37658 0.17093  -0.06875 0.05726  116  ALA A O   
1380 C CB  . ALA A 91  ? 0.20508 0.51158 0.37597 0.12577  -0.05321 0.05183  116  ALA A CB  
1386 N N   . MET A 92  ? 0.31621 0.35594 0.27744 0.04100  0.11923  0.07359  117  MET A N   
1387 C CA  . MET A 92  ? 0.37642 0.42963 0.33478 0.04094  0.09677  0.07859  117  MET A CA  
1388 C C   . MET A 92  ? 0.28951 0.34580 0.24991 0.02926  0.08235  0.05342  117  MET A C   
1389 O O   . MET A 92  ? 0.32594 0.37060 0.30327 0.01743  0.08575  0.04740  117  MET A O   
1390 C CB  . MET A 92  ? 0.28690 0.33781 0.26609 0.03840  0.09098  0.11241  117  MET A CB  
1391 C CG  . MET A 92  ? 0.29574 0.34925 0.28324 0.04600  0.10646  0.13984  117  MET A CG  
1392 S SD  . MET A 92  ? 0.32460 0.38100 0.32452 0.04063  0.09404  0.16940  117  MET A SD  
1393 C CE  . MET A 92  ? 0.26878 0.32387 0.30045 0.02104  0.08010  0.16630  117  MET A CE  
1403 N N   . GLU A 93  ? 0.36599 0.44087 0.30838 0.03520  0.06763  0.04036  118  GLU A N   
1404 C CA  . GLU A 93  ? 0.31743 0.40421 0.26130 0.02700  0.05373  0.01694  118  GLU A CA  
1405 C C   . GLU A 93  ? 0.33439 0.42583 0.27282 0.03561  0.03615  0.03128  118  GLU A C   
1406 O O   . GLU A 93  ? 0.38484 0.47524 0.30940 0.05002  0.03551  0.05132  118  GLU A O   
1407 C CB  . GLU A 93  ? 0.34562 0.45947 0.27203 0.02663  0.05387  -0.01887 118  GLU A CB  
1408 C CG  . GLU A 93  ? 0.51931 0.66089 0.41686 0.04639  0.04884  -0.02035 118  GLU A CG  
1409 C CD  . GLU A 93  ? 0.56856 0.74270 0.45039 0.04197  0.04966  -0.06018 118  GLU A CD  
1410 O OE1 . GLU A 93  ? 0.45813 0.63811 0.35408 0.02171  0.04930  -0.08808 118  GLU A OE1 
1411 O OE2 . GLU A 93  ? 0.58489 0.77848 0.44060 0.05717  0.05228  -0.06402 118  GLU A OE2 
1418 N N   . SER A 94  ? 0.36163 0.45326 0.30993 0.02737  0.02516  0.02242  119  SER A N   
1419 C CA  . SER A 94  ? 0.35400 0.45151 0.29069 0.03818  0.01002  0.02748  119  SER A CA  
1420 C C   . SER A 94  ? 0.35186 0.48511 0.26347 0.05632  0.00508  0.01337  119  SER A C   
1421 O O   . SER A 94  ? 0.39754 0.56058 0.30713 0.05172  0.00636  -0.01468 119  SER A O   
1422 C CB  . SER A 94  ? 0.41040 0.50571 0.36105 0.02712  0.00149  0.01648  119  SER A CB  
1423 O OG  . SER A 94  ? 0.24186 0.36107 0.19968 0.01723  0.00378  -0.01363 119  SER A OG  
1429 N N   . GLN A 95  ? 0.44696 0.57787 0.33770 0.07732  0.00148  0.03320  120  GLN A N   
1430 C CA  . GLN A 95  ? 0.32277 0.49409 0.18640 0.10054  -0.00334 0.02347  120  GLN A CA  
1431 C C   . GLN A 95  ? 0.43891 0.64648 0.30230 0.10392  -0.01693 0.00145  120  GLN A C   
1432 O O   . GLN A 95  ? 0.41264 0.67047 0.25807 0.12073  -0.02338 -0.01362 120  GLN A O   
1433 C CB  . GLN A 95  ? 0.49136 0.64680 0.33002 0.12636  0.00023  0.05447  120  GLN A CB  
1436 N N   . ARG A 96  ? 0.39749 0.58584 0.27991 0.08990  -0.02141 0.00013  121  ARG A N   
1437 C CA  . ARG A 96  ? 0.37675 0.59595 0.26044 0.09513  -0.03280 -0.01520 121  ARG A CA  
1438 C C   . ARG A 96  ? 0.35761 0.55304 0.26842 0.07044  -0.03232 -0.02183 121  ARG A C   
1439 O O   . ARG A 96  ? 0.38098 0.53813 0.30608 0.05368  -0.02446 -0.01175 121  ARG A O   
1440 C CB  . ARG A 96  ? 0.41854 0.63070 0.27738 0.12517  -0.03778 0.00660  121  ARG A CB  
1441 C CG  . ARG A 96  ? 0.44770 0.59273 0.30182 0.12460  -0.03066 0.03797  121  ARG A CG  
1442 C CD  . ARG A 96  ? 0.41112 0.52258 0.28234 0.10665  -0.03372 0.03824  121  ARG A CD  
1443 N NE  . ARG A 96  ? 0.47400 0.52903 0.33531 0.10786  -0.02908 0.06345  121  ARG A NE  
1444 C CZ  . ARG A 96  ? 0.48029 0.50360 0.34276 0.10155  -0.03265 0.06563  121  ARG A CZ  
1445 N NH1 . ARG A 96  ? 0.46318 0.50493 0.33757 0.09527  -0.04027 0.04766  121  ARG A NH1 
1446 N NH2 . ARG A 96  ? 0.47767 0.44884 0.32798 0.10065  -0.02703 0.08529  121  ARG A NH2 
1460 N N   . ALA A 97  ? 0.38707 0.60970 0.30418 0.07119  -0.04025 -0.03677 122  ALA A N   
1461 C CA  . ALA A 97  ? 0.34266 0.54991 0.28333 0.05062  -0.03876 -0.04457 122  ALA A CA  
1462 C C   . ALA A 97  ? 0.29226 0.45196 0.22782 0.05548  -0.04130 -0.02095 122  ALA A C   
1463 O O   . ALA A 97  ? 0.34331 0.49160 0.25650 0.07719  -0.04577 -0.00521 122  ALA A O   
1464 C CB  . ALA A 97  ? 0.38425 0.64343 0.33444 0.04963  -0.04470 -0.06930 122  ALA A CB  
1470 N N   . TYR A 98  ? 0.29633 0.42641 0.25013 0.03577  -0.03669 -0.01833 123  TYR A N   
1471 C CA  . TYR A 98  ? 0.31733 0.40761 0.26816 0.03503  -0.04022 -0.00204 123  TYR A CA  
1472 C C   . TYR A 98  ? 0.28767 0.38661 0.24960 0.02926  -0.04226 -0.01434 123  TYR A C   
1473 O O   . TYR A 98  ? 0.30071 0.42708 0.28018 0.01830  -0.03699 -0.03245 123  TYR A O   
1474 C CB  . TYR A 98  ? 0.31775 0.37428 0.27914 0.01976  -0.03443 0.01397  123  TYR A CB  
1475 C CG  . TYR A 98  ? 0.28860 0.32841 0.23647 0.02744  -0.03261 0.03245  123  TYR A CG  
1476 C CD1 . TYR A 98  ? 0.27536 0.33431 0.21953 0.03321  -0.02656 0.03075  123  TYR A CD1 
1477 C CD2 . TYR A 98  ? 0.34660 0.35083 0.28418 0.02800  -0.03531 0.05021  123  TYR A CD2 
1478 C CE1 . TYR A 98  ? 0.38401 0.42845 0.31498 0.04222  -0.02253 0.04966  123  TYR A CE1 
1479 C CE2 . TYR A 98  ? 0.31501 0.30186 0.24184 0.03314  -0.03022 0.06797  123  TYR A CE2 
1480 C CZ  . TYR A 98  ? 0.38536 0.39306 0.30904 0.04177  -0.02345 0.06938  123  TYR A CZ  
1481 O OH  . TYR A 98  ? 0.38207 0.37288 0.29422 0.04884  -0.01585 0.08949  123  TYR A OH  
1491 N N   . ARG A 99  ? 0.28685 0.35950 0.23668 0.03633  -0.04809 -0.00485 124  ARG A N   
1492 C CA  . ARG A 99  ? 0.30532 0.38364 0.25998 0.03585  -0.04983 -0.01348 124  ARG A CA  
1493 C C   . ARG A 99  ? 0.32575 0.37832 0.29333 0.01831  -0.04640 -0.00805 124  ARG A C   
1494 O O   . ARG A 99  ? 0.35405 0.37286 0.31247 0.01532  -0.05039 0.00553  124  ARG A O   
1495 C CB  . ARG A 99  ? 0.38198 0.44471 0.31016 0.05750  -0.05644 -0.00700 124  ARG A CB  
1496 C CG  . ARG A 99  ? 0.43348 0.49586 0.36099 0.06066  -0.05772 -0.01313 124  ARG A CG  
1497 C CD  . ARG A 99  ? 0.45814 0.48970 0.35283 0.08328  -0.06136 -0.00439 124  ARG A CD  
1498 N NE  . ARG A 99  ? 0.48789 0.51772 0.37735 0.08980  -0.06164 -0.00992 124  ARG A NE  
1499 C CZ  . ARG A 99  ? 0.55827 0.54502 0.43392 0.08449  -0.06318 -0.00624 124  ARG A CZ  
1500 N NH1 . ARG A 99  ? 0.49947 0.44591 0.36958 0.06888  -0.06557 0.00164  124  ARG A NH1 
1501 N NH2 . ARG A 99  ? 0.56709 0.55579 0.43478 0.09436  -0.06229 -0.01160 124  ARG A NH2 
1515 N N   . PHE A 100 ? 0.36744 0.43782 0.35565 0.00691  -0.03799 -0.01877 125  PHE A N   
1516 C CA  . PHE A 100 ? 0.29457 0.34734 0.29403 -0.00465 -0.03181 -0.01229 125  PHE A CA  
1517 C C   . PHE A 100 ? 0.29268 0.34846 0.29012 -0.00024 -0.03203 -0.01712 125  PHE A C   
1518 O O   . PHE A 100 ? 0.33750 0.42027 0.33901 0.00455  -0.02994 -0.03033 125  PHE A O   
1519 C CB  . PHE A 100 ? 0.27423 0.33589 0.29565 -0.01842 -0.01544 -0.01753 125  PHE A CB  
1520 C CG  . PHE A 100 ? 0.28601 0.34031 0.30928 -0.02223 -0.01195 -0.00991 125  PHE A CG  
1521 C CD1 . PHE A 100 ? 0.29398 0.36489 0.31199 -0.01875 -0.01371 -0.01861 125  PHE A CD1 
1522 C CD2 . PHE A 100 ? 0.28342 0.31967 0.31327 -0.02704 -0.00620 0.00658  125  PHE A CD2 
1523 C CE1 . PHE A 100 ? 0.34245 0.40676 0.36016 -0.02037 -0.00883 -0.01110 125  PHE A CE1 
1524 C CE2 . PHE A 100 ? 0.32625 0.35865 0.35865 -0.02861 -0.00138 0.01516  125  PHE A CE2 
1525 C CZ  . PHE A 100 ? 0.29607 0.33973 0.32183 -0.02557 -0.00201 0.00626  125  PHE A CZ  
1535 N N   . VAL A 101 ? 0.38712 0.42057 0.37861 -0.00154 -0.03443 -0.00665 126  VAL A N   
1536 C CA  . VAL A 101 ? 0.39253 0.42887 0.38501 0.00098  -0.02947 -0.00895 126  VAL A CA  
1537 C C   . VAL A 101 ? 0.37942 0.40705 0.38271 -0.00713 -0.02020 0.00263  126  VAL A C   
1538 O O   . VAL A 101 ? 0.32156 0.34222 0.33032 -0.01332 -0.02009 0.01250  126  VAL A O   
1539 C CB  . VAL A 101 ? 0.47544 0.49556 0.44170 0.01363  -0.04155 -0.00805 126  VAL A CB  
1540 C CG1 . VAL A 101 ? 0.44932 0.48258 0.40502 0.02806  -0.04553 -0.01725 126  VAL A CG1 
1541 C CG2 . VAL A 101 ? 0.44809 0.43857 0.39783 0.01004  -0.05328 0.00166  126  VAL A CG2 
1551 N N   . GLN A 102 ? 0.29358 0.32454 0.29976 -0.00436 -0.01046 0.00345  127  GLN A N   
1552 C CA  . GLN A 102 ? 0.33818 0.36324 0.35167 -0.00628 0.00095  0.01774  127  GLN A CA  
1553 C C   . GLN A 102 ? 0.25045 0.26679 0.24982 -0.00483 -0.01585 0.02990  127  GLN A C   
1554 O O   . GLN A 102 ? 0.32979 0.33810 0.30897 -0.00129 -0.03218 0.02593  127  GLN A O   
1555 C CB  . GLN A 102 ? 0.32401 0.35246 0.33775 0.00019  0.01469  0.01941  127  GLN A CB  
1556 C CG  . GLN A 102 ? 0.39783 0.43540 0.43271 -0.00769 0.03692  0.00861  127  GLN A CG  
1557 C CD  . GLN A 102 ? 0.32156 0.36134 0.35877 -0.00242 0.05444  0.01148  127  GLN A CD  
1558 O OE1 . GLN A 102 ? 0.27774 0.33175 0.32952 -0.00921 0.06697  -0.00202 127  GLN A OE1 
1559 N NE2 . GLN A 102 ? 0.24631 0.27648 0.27071 0.00944  0.05735  0.02956  127  GLN A NE2 
1568 N N   . GLY A 103 ? 0.30680 0.32536 0.31674 -0.00847 -0.01110 0.04355  128  GLY A N   
1569 C CA  . GLY A 103 ? 0.30336 0.32451 0.30624 -0.01084 -0.02672 0.05424  128  GLY A CA  
1570 C C   . GLY A 103 ? 0.35950 0.37597 0.36527 -0.02045 -0.03697 0.05433  128  GLY A C   
1571 O O   . GLY A 103 ? 0.36275 0.38715 0.37124 -0.02622 -0.04547 0.06483  128  GLY A O   
1575 N N   . LYS A 104 ? 0.35960 0.36835 0.36585 -0.02168 -0.03516 0.04371  129  LYS A N   
1576 C CA  . LYS A 104 ? 0.44740 0.44805 0.45047 -0.02704 -0.04375 0.04414  129  LYS A CA  
1577 C C   . LYS A 104 ? 0.34626 0.35554 0.36733 -0.03020 -0.03178 0.05179  129  LYS A C   
1578 O O   . LYS A 104 ? 0.32949 0.34384 0.35983 -0.02812 -0.01692 0.04547  129  LYS A O   
1579 C CB  . LYS A 104 ? 0.41261 0.40454 0.40120 -0.02031 -0.04786 0.03025  129  LYS A CB  
1580 C CG  . LYS A 104 ? 0.45263 0.43513 0.43458 -0.02041 -0.05220 0.03213  129  LYS A CG  
1581 C CD  . LYS A 104 ? 0.42788 0.38427 0.39071 -0.02371 -0.06412 0.03584  129  LYS A CD  
1582 C CE  . LYS A 104 ? 0.49509 0.43646 0.44868 -0.02126 -0.06406 0.04029  129  LYS A CE  
1583 N NZ  . LYS A 104 ? 0.54723 0.45481 0.48255 -0.02869 -0.07135 0.04337  129  LYS A NZ  
1597 N N   . ASP A 105 ? 0.31897 0.24904 0.27179 -0.01907 0.01187  -0.05454 130  ASP A N   
1598 C CA  . ASP A 105 ? 0.37500 0.30234 0.33168 -0.02342 0.00864  -0.04097 130  ASP A CA  
1599 C C   . ASP A 105 ? 0.38209 0.30578 0.35618 -0.01617 0.00568  -0.03481 130  ASP A C   
1600 O O   . ASP A 105 ? 0.28823 0.20017 0.27176 -0.00936 0.00521  -0.03885 130  ASP A O   
1601 C CB  . ASP A 105 ? 0.43413 0.35165 0.38160 -0.02830 0.00248  -0.03713 130  ASP A CB  
1602 C CG  . ASP A 105 ? 0.50911 0.41734 0.46580 -0.02748 -0.00396 -0.04667 130  ASP A CG  
1603 O OD1 . ASP A 105 ? 0.52800 0.42908 0.49811 -0.02314 -0.00251 -0.05387 130  ASP A OD1 
1604 O OD2 . ASP A 105 ? 0.66585 0.57451 0.61903 -0.03080 -0.01034 -0.04877 130  ASP A OD2 
1609 N N   . TRP A 106 ? 0.31510 0.24776 0.29181 -0.01574 0.00498  -0.02495 131  TRP A N   
1610 C CA  . TRP A 106 ? 0.32781 0.25724 0.31318 -0.00622 0.00310  -0.01384 131  TRP A CA  
1611 C C   . TRP A 106 ? 0.33662 0.26710 0.31829 -0.01130 0.00098  -0.00336 131  TRP A C   
1612 O O   . TRP A 106 ? 0.24892 0.19025 0.22433 -0.01775 0.00072  -0.00615 131  TRP A O   
1613 C CB  . TRP A 106 ? 0.28237 0.23430 0.27301 0.00752  0.00334  -0.01502 131  TRP A CB  
1614 C CG  . TRP A 106 ? 0.29595 0.24628 0.29306 0.01927  0.00528  -0.02194 131  TRP A CG  
1615 C CD1 . TRP A 106 ? 0.25875 0.22944 0.26003 0.02079  0.00769  -0.03657 131  TRP A CD1 
1616 C CD2 . TRP A 106 ? 0.25960 0.18481 0.26172 0.03174  0.00711  -0.01482 131  TRP A CD2 
1617 N NE1 . TRP A 106 ? 0.30362 0.26660 0.31104 0.03610  0.00889  -0.04039 131  TRP A NE1 
1618 C CE2 . TRP A 106 ? 0.34729 0.27860 0.35498 0.04311  0.00877  -0.02684 131  TRP A CE2 
1619 C CE3 . TRP A 106 ? 0.30914 0.20534 0.31379 0.03383  0.01009  0.00076  131  TRP A CE3 
1620 C CZ2 . TRP A 106 ? 0.37327 0.27842 0.38741 0.05839  0.01215  -0.02408 131  TRP A CZ2 
1621 C CZ3 . TRP A 106 ? 0.32619 0.19414 0.33884 0.04621  0.01579  0.00501  131  TRP A CZ3 
1622 C CH2 . TRP A 106 ? 0.35781 0.22806 0.37439 0.05928  0.01621  -0.00747 131  TRP A CH2 
1633 N N   . GLY A 107 ? 0.33266 0.25088 0.31959 -0.00833 0.00171  0.00865  132  GLY A N   
1634 C CA  . GLY A 107 ? 0.31467 0.23859 0.29833 -0.01222 0.00064  0.01715  132  GLY A CA  
1635 C C   . GLY A 107 ? 0.34873 0.26049 0.34074 -0.01016 0.00548  0.03161  132  GLY A C   
1636 O O   . GLY A 107 ? 0.26521 0.16070 0.26482 -0.00363 0.01135  0.03858  132  GLY A O   
1640 N N   . PHE A 108 ? 0.29594 0.21483 0.28717 -0.01516 0.00511  0.03676  133  PHE A N   
1641 C CA  . PHE A 108 ? 0.34341 0.25697 0.34382 -0.01500 0.01283  0.05158  133  PHE A CA  
1642 C C   . PHE A 108 ? 0.26596 0.17409 0.28228 -0.03040 0.01168  0.04332  133  PHE A C   
1643 O O   . PHE A 108 ? 0.23567 0.15689 0.24722 -0.03490 0.00456  0.03554  133  PHE A O   
1644 C CB  . PHE A 108 ? 0.28031 0.21461 0.26952 -0.00642 0.01374  0.06130  133  PHE A CB  
1645 C CG  . PHE A 108 ? 0.27278 0.22264 0.24754 0.01076  0.01206  0.06442  133  PHE A CG  
1646 C CD1 . PHE A 108 ? 0.39841 0.34476 0.36806 0.02746  0.01998  0.08239  133  PHE A CD1 
1647 C CD2 . PHE A 108 ? 0.26661 0.23638 0.23381 0.01147  0.00355  0.04914  133  PHE A CD2 
1648 C CE1 . PHE A 108 ? 0.33719 0.30670 0.29191 0.04813  0.01584  0.08353  133  PHE A CE1 
1649 C CE2 . PHE A 108 ? 0.26907 0.26286 0.22815 0.02706  0.00017  0.04634  133  PHE A CE2 
1650 C CZ  . PHE A 108 ? 0.32662 0.32424 0.27816 0.04710  0.00443  0.06263  133  PHE A CZ  
1660 N N   . LYS A 109 ? 0.24805 0.13733 0.28447 -0.03721 0.01838  0.04264  134  LYS A N   
1661 C CA  . LYS A 109 ? 0.34475 0.23674 0.40374 -0.05237 0.01721  0.03086  134  LYS A CA  
1662 C C   . LYS A 109 ? 0.37889 0.28797 0.44662 -0.05573 0.02225  0.04069  134  LYS A C   
1663 O O   . LYS A 109 ? 0.35686 0.28500 0.43379 -0.06280 0.01485  0.02853  134  LYS A O   
1664 C CB  . LYS A 109 ? 0.31930 0.18605 0.40520 -0.06126 0.02618  0.02519  134  LYS A CB  
1665 C CG  . LYS A 109 ? 0.41570 0.29183 0.53419 -0.07946 0.02483  0.00654  134  LYS A CG  
1666 C CD  . LYS A 109 ? 0.40646 0.26370 0.54757 -0.08839 0.02700  -0.01281 134  LYS A CD  
1667 C CE  . LYS A 109 ? 0.55951 0.38623 0.70360 -0.08334 0.04331  0.00366  134  LYS A CE  
1668 N NZ  . LYS A 109 ? 0.70875 0.53553 0.88002 -0.09544 0.05652  0.00735  134  LYS A NZ  
1682 N N   . LYS A 110 ? 0.31254 0.21837 0.37647 -0.04809 0.03502  0.06248  135  LYS A N   
1683 C CA  . LYS A 110 ? 0.24538 0.17034 0.31472 -0.04873 0.04249  0.07344  135  LYS A CA  
1684 C C   . LYS A 110 ? 0.29832 0.24103 0.33704 -0.03222 0.03710  0.08074  135  LYS A C   
1685 O O   . LYS A 110 ? 0.28256 0.22799 0.30882 -0.01972 0.04661  0.09864  135  LYS A O   
1686 C CB  . LYS A 110 ? 0.38431 0.29314 0.47240 -0.05233 0.06475  0.09304  135  LYS A CB  
1687 C CG  . LYS A 110 ? 0.33224 0.22994 0.45936 -0.07329 0.07070  0.07877  135  LYS A CG  
1688 C CD  . LYS A 110 ? 0.43641 0.31864 0.57275 -0.07425 0.09054  0.09307  135  LYS A CD  
1689 C CE  . LYS A 110 ? 0.46402 0.34456 0.63991 -0.09587 0.09403  0.07294  135  LYS A CE  
1690 N NZ  . LYS A 110 ? 0.58952 0.44808 0.77849 -0.09901 0.11543  0.08642  135  LYS A NZ  
1704 N N   . PHE A 111 ? 0.25370 0.20893 0.28017 -0.03125 0.02255  0.06585  136  PHE A N   
1705 C CA  . PHE A 111 ? 0.23184 0.20104 0.23465 -0.01811 0.01818  0.06736  136  PHE A CA  
1706 C C   . PHE A 111 ? 0.34217 0.33333 0.34360 -0.01272 0.02264  0.07332  136  PHE A C   
1707 O O   . PHE A 111 ? 0.28958 0.29405 0.27474 0.00068  0.02528  0.07992  136  PHE A O   
1708 C CB  . PHE A 111 ? 0.22541 0.19365 0.21659 -0.01934 0.00591  0.05119  136  PHE A CB  
1709 C CG  . PHE A 111 ? 0.29213 0.27297 0.26692 -0.00974 0.00291  0.04749  136  PHE A CG  
1710 C CD1 . PHE A 111 ? 0.36523 0.35375 0.33129 0.00021  0.00405  0.05010  136  PHE A CD1 
1711 C CD2 . PHE A 111 ? 0.34258 0.32985 0.31234 -0.00882 -0.00113 0.03938  136  PHE A CD2 
1712 C CE1 . PHE A 111 ? 0.32779 0.33500 0.28351 0.00822  -0.00006 0.04021  136  PHE A CE1 
1713 C CE2 . PHE A 111 ? 0.31385 0.31166 0.27336 -0.00165 -0.00290 0.03125  136  PHE A CE2 
1714 C CZ  . PHE A 111 ? 0.28012 0.29024 0.23424 0.00549  -0.00292 0.02953  136  PHE A CZ  
1724 N N   . ILE A 112 ? 0.22537 0.22595 0.24328 -0.02074 0.02236  0.06834  137  ILE A N   
1725 C CA  . ILE A 112 ? 0.28871 0.31337 0.30803 -0.01481 0.02759  0.07254  137  ILE A CA  
1726 C C   . ILE A 112 ? 0.30308 0.33973 0.35284 -0.02679 0.03149  0.06900  137  ILE A C   
1727 O O   . ILE A 112 ? 0.24016 0.27409 0.30100 -0.03464 0.02102  0.05464  137  ILE A O   
1728 C CB  . ILE A 112 ? 0.27778 0.31126 0.27856 -0.00486 0.01675  0.06049  137  ILE A CB  
1729 C CG1 . ILE A 112 ? 0.37153 0.43139 0.37204 0.00460  0.02242  0.06280  137  ILE A CG1 
1730 C CG2 . ILE A 112 ? 0.30941 0.33655 0.31415 -0.00950 0.00565  0.04713  137  ILE A CG2 
1731 C CD1 . ILE A 112 ? 0.29970 0.37281 0.28465 0.01692  0.03139  0.07369  137  ILE A CD1 
1743 N N   . ARG A 113 ? 0.35640 0.40976 0.42052 -0.02770 0.04735  0.08119  138  ARG A N   
1744 C CA  . ARG A 113 ? 0.30670 0.38024 0.40726 -0.04061 0.05343  0.07541  138  ARG A CA  
1745 C C   . ARG A 113 ? 0.25018 0.34792 0.35113 -0.03412 0.03757  0.05760  138  ARG A C   
1746 O O   . ARG A 113 ? 0.26048 0.36626 0.33819 -0.01853 0.03270  0.05722  138  ARG A O   
1747 C CB  . ARG A 113 ? 0.34987 0.43959 0.46362 -0.04143 0.07708  0.09371  138  ARG A CB  
1748 C CG  . ARG A 113 ? 0.39006 0.46096 0.53340 -0.05900 0.09766  0.10553  138  ARG A CG  
1749 C CD  . ARG A 113 ? 0.37698 0.46851 0.54563 -0.06568 0.12411  0.12027  138  ARG A CD  
1750 N NE  . ARG A 113 ? 0.47764 0.59576 0.69742 -0.08634 0.12577  0.10068  138  ARG A NE  
1751 C CZ  . ARG A 113 ? 0.40601 0.50849 0.66090 -0.10833 0.13021  0.08900  138  ARG A CZ  
1752 N NH1 . ARG A 113 ? 0.42509 0.48123 0.66495 -0.11020 0.13078  0.09412  138  ARG A NH1 
1753 N NH2 . ARG A 113 ? 0.34198 0.47788 0.64136 -0.12499 0.12952  0.06709  138  ARG A NH2 
1767 N N   . ARG A 114 ? 0.24638 0.35623 0.37407 -0.04424 0.02924  0.04121  139  ARG A N   
1768 C CA  . ARG A 114 ? 0.25096 0.38483 0.37752 -0.03346 0.01342  0.02570  139  ARG A CA  
1769 C C   . ARG A 114 ? 0.18383 0.35158 0.32005 -0.02466 0.02141  0.02844  139  ARG A C   
1770 O O   . ARG A 114 ? 0.21244 0.38685 0.32854 -0.00645 0.01226  0.02422  139  ARG A O   
1771 C CB  . ARG A 114 ? 0.24125 0.39255 0.39716 -0.04358 0.00258  0.00559  139  ARG A CB  
1772 C CG  . ARG A 114 ? 0.22765 0.34888 0.36635 -0.04663 -0.00900 -0.00123 139  ARG A CG  
1773 C CD  . ARG A 114 ? 0.26956 0.41536 0.42914 -0.05004 -0.02417 -0.02556 139  ARG A CD  
1774 N NE  . ARG A 114 ? 0.22931 0.41233 0.38949 -0.03323 -0.03665 -0.03532 139  ARG A NE  
1775 C CZ  . ARG A 114 ? 0.29663 0.47169 0.41859 -0.01041 -0.04957 -0.03289 139  ARG A CZ  
1776 N NH1 . ARG A 114 ? 0.34210 0.47691 0.42576 -0.00508 -0.05171 -0.02377 139  ARG A NH1 
1777 N NH2 . ARG A 114 ? 0.29589 0.50347 0.41955 0.00816  -0.05867 -0.03920 139  ARG A NH2 
1791 N N   . ASP A 115 ? 0.23578 0.42376 0.40347 -0.03686 0.04048  0.03541  140  ASP A N   
1792 C CA  . ASP A 115 ? 0.20884 0.43588 0.38775 -0.02764 0.04878  0.03592  140  ASP A CA  
1793 C C   . ASP A 115 ? 0.23369 0.45239 0.37570 -0.01065 0.05642  0.05089  140  ASP A C   
1794 O O   . ASP A 115 ? 0.27554 0.52458 0.41874 0.00158  0.06155  0.04954  140  ASP A O   
1795 C CB  . ASP A 115 ? 0.25996 0.51743 0.48942 -0.04742 0.06981  0.03714  140  ASP A CB  
1796 C CG  . ASP A 115 ? 0.27274 0.50321 0.50331 -0.06045 0.09507  0.06083  140  ASP A CG  
1797 O OD1 . ASP A 115 ? 0.22586 0.42500 0.41439 -0.04845 0.09505  0.07657  140  ASP A OD1 
1798 O OD2 . ASP A 115 ? 0.28474 0.52462 0.55915 -0.08204 0.11554  0.06326  140  ASP A OD2 
1803 N N   . PHE A 116 ? 0.26747 0.45060 0.37792 -0.00814 0.05635  0.06202  141  PHE A N   
1804 C CA  . PHE A 116 ? 0.24768 0.42792 0.32188 0.01044  0.05687  0.06748  141  PHE A CA  
1805 C C   . PHE A 116 ? 0.19774 0.36474 0.25065 0.02255  0.03646  0.05075  141  PHE A C   
1806 O O   . PHE A 116 ? 0.24126 0.41963 0.27986 0.03871  0.03403  0.04353  141  PHE A O   
1807 C CB  . PHE A 116 ? 0.23691 0.39229 0.29013 0.00977  0.06495  0.08424  141  PHE A CB  
1808 C CG  . PHE A 116 ? 0.25005 0.41304 0.26871 0.02970  0.06596  0.08751  141  PHE A CG  
1809 C CD1 . PHE A 116 ? 0.28930 0.43930 0.28496 0.03872  0.04874  0.07170  141  PHE A CD1 
1810 C CD2 . PHE A 116 ? 0.32097 0.50577 0.33114 0.03935  0.08521  0.10493  141  PHE A CD2 
1811 C CE1 . PHE A 116 ? 0.33970 0.50218 0.30919 0.05568  0.04790  0.06764  141  PHE A CE1 
1812 C CE2 . PHE A 116 ? 0.33920 0.53812 0.31599 0.06038  0.08370  0.10371  141  PHE A CE2 
1813 C CZ  . PHE A 116 ? 0.37425 0.56360 0.33257 0.06796  0.06356  0.08239  141  PHE A CZ  
1823 N N   . LEU A 117 ? 0.23881 0.38055 0.29056 0.01513  0.02366  0.04422  142  LEU A N   
1824 C CA  . LEU A 117 ? 0.22621 0.34877 0.25791 0.02538  0.00855  0.03240  142  LEU A CA  
1825 C C   . LEU A 117 ? 0.27193 0.41549 0.31093 0.03906  0.00287  0.02256  142  LEU A C   
1826 O O   . LEU A 117 ? 0.26636 0.39787 0.28644 0.05422  -0.00209 0.01573  142  LEU A O   
1827 C CB  . LEU A 117 ? 0.27857 0.37634 0.30893 0.01562  -0.00105 0.02958  142  LEU A CB  
1828 C CG  . LEU A 117 ? 0.38497 0.45402 0.39053 0.02409  -0.01139 0.02312  142  LEU A CG  
1829 C CD1 . LEU A 117 ? 0.28089 0.32966 0.26616 0.02613  -0.00818 0.02296  142  LEU A CD1 
1830 C CD2 . LEU A 117 ? 0.43172 0.48507 0.43701 0.01491  -0.01807 0.02192  142  LEU A CD2 
1842 N N   . LEU A 118 ? 0.23608 0.41108 0.30529 0.03430  0.00352  0.01963  143  LEU A N   
1843 C CA  . LEU A 118 ? 0.25507 0.45699 0.33423 0.05023  -0.00411 0.00879  143  LEU A CA  
1844 C C   . LEU A 118 ? 0.27988 0.51287 0.36567 0.06183  0.00646  0.00828  143  LEU A C   
1845 O O   . LEU A 118 ? 0.32030 0.57581 0.41265 0.07930  0.00033  -0.00147 143  LEU A O   
1846 C CB  . LEU A 118 ? 0.26300 0.49746 0.37753 0.04096  -0.00940 0.00011  143  LEU A CB  
1847 C CG  . LEU A 118 ? 0.28719 0.50195 0.39655 0.03411  -0.02279 -0.00506 143  LEU A CG  
1848 C CD1 . LEU A 118 ? 0.26212 0.52214 0.41423 0.02477  -0.02830 -0.02072 143  LEU A CD1 
1849 C CD2 . LEU A 118 ? 0.32246 0.50999 0.39556 0.05574  -0.03665 -0.00625 143  LEU A CD2 
1861 N N   . ASP A 119 ? 0.31399 0.55117 0.39636 0.05566  0.02231  0.01881  144  ASP A N   
1862 C CA  . ASP A 119 ? 0.26706 0.53721 0.35144 0.06798  0.03483  0.01911  144  ASP A CA  
1863 C C   . ASP A 119 ? 0.26827 0.51978 0.32098 0.08915  0.02722  0.00889  144  ASP A C   
1864 O O   . ASP A 119 ? 0.30027 0.52386 0.32738 0.08852  0.02637  0.01021  144  ASP A O   
1865 C CB  . ASP A 119 ? 0.24255 0.52115 0.32759 0.05699  0.05542  0.03686  144  ASP A CB  
1866 C CG  . ASP A 119 ? 0.30001 0.61966 0.38822 0.06903  0.07216  0.03974  144  ASP A CG  
1867 O OD1 . ASP A 119 ? 0.29207 0.63340 0.38176 0.08668  0.06651  0.02502  144  ASP A OD1 
1868 O OD2 . ASP A 119 ? 0.23992 0.56940 0.32649 0.06321  0.09283  0.05836  144  ASP A OD2 
1873 N N   . GLU A 120 ? 0.30483 0.57242 0.36222 0.10829  0.02169  -0.00368 145  GLU A N   
1874 C CA  A GLU A 120 ? 0.33029 0.57273 0.36200 0.12791  0.01553  -0.01616 145  GLU A CA  
1875 C CA  B GLU A 120 ? 0.32428 0.56698 0.35604 0.12807  0.01557  -0.01624 145  GLU A CA  
1876 C C   . GLU A 120 ? 0.30908 0.56003 0.32361 0.13271  0.02556  -0.01907 145  GLU A C   
1877 O O   . GLU A 120 ? 0.33123 0.55522 0.32511 0.14197  0.02066  -0.03235 145  GLU A O   
1878 C CB  A GLU A 120 ? 0.34537 0.60639 0.38700 0.15143  0.01023  -0.02794 145  GLU A CB  
1879 C CB  B GLU A 120 ? 0.34500 0.60720 0.38630 0.15210  0.01083  -0.02835 145  GLU A CB  
1880 C CG  A GLU A 120 ? 0.43754 0.66911 0.47474 0.15959  -0.00482 -0.02930 145  GLU A CG  
1881 C CG  B GLU A 120 ? 0.42077 0.67194 0.46830 0.15961  -0.00336 -0.02941 145  GLU A CG  
1882 C CD  A GLU A 120 ? 0.42042 0.66346 0.47545 0.14180  -0.01070 -0.02117 145  GLU A CD  
1883 C CD  B GLU A 120 ? 0.50730 0.69667 0.52507 0.16920  -0.01218 -0.03108 145  GLU A CD  
1884 O OE1 A GLU A 120 ? 0.42769 0.71895 0.51467 0.13153  -0.00479 -0.02060 145  GLU A OE1 
1885 O OE1 B GLU A 120 ? 0.53586 0.68862 0.53466 0.15956  -0.00832 -0.03175 145  GLU A OE1 
1886 O OE2 A GLU A 120 ? 0.39199 0.59641 0.43073 0.13729  -0.01964 -0.01691 145  GLU A OE2 
1887 O OE2 B GLU A 120 ? 0.53077 0.71016 0.54500 0.18727  -0.02187 -0.03160 145  GLU A OE2 
1898 N N   . ALA A 121 ? 0.32796 0.61679 0.35109 0.12716  0.04063  -0.00762 146  ALA A N   
1899 C CA  . ALA A 121 ? 0.27265 0.57623 0.27371 0.13596  0.05015  -0.00846 146  ALA A CA  
1900 C C   . ALA A 121 ? 0.30047 0.57174 0.27777 0.12818  0.04440  -0.00695 146  ALA A C   
1901 O O   . ALA A 121 ? 0.33535 0.61447 0.29051 0.13996  0.04479  -0.01746 146  ALA A O   
1902 C CB  . ALA A 121 ? 0.29405 0.64197 0.30654 0.13243  0.07151  0.01008  146  ALA A CB  
1908 N N   . ASN A 122 ? 0.30890 0.55049 0.29150 0.10981  0.03902  0.00372  147  ASN A N   
1909 C CA  . ASN A 122 ? 0.31262 0.52875 0.27638 0.10304  0.03389  0.00453  147  ASN A CA  
1910 C C   . ASN A 122 ? 0.32791 0.50679 0.28363 0.10337  0.02008  -0.01513 147  ASN A C   
1911 O O   . ASN A 122 ? 0.25306 0.41508 0.19727 0.09760  0.01546  -0.01994 147  ASN A O   
1912 C CB  . ASN A 122 ? 0.30874 0.51087 0.28246 0.08401  0.03706  0.02490  147  ASN A CB  
1913 C CG  . ASN A 122 ? 0.33943 0.57038 0.32516 0.08055  0.05559  0.04603  147  ASN A CG  
1914 O OD1 . ASN A 122 ? 0.31132 0.56706 0.28141 0.09277  0.06716  0.05317  147  ASN A OD1 
1915 N ND2 . ASN A 122 ? 0.25471 0.48407 0.26887 0.06442  0.05981  0.05492  147  ASN A ND2 
1922 N N   . GLY A 123 ? 0.33703 0.26042 0.32972 0.02568  0.06498  -0.07437 148  GLY A N   
1923 C CA  . GLY A 123 ? 0.30872 0.22437 0.30335 0.02683  0.05785  -0.07555 148  GLY A CA  
1924 C C   . GLY A 123 ? 0.37824 0.30070 0.37344 0.02366  0.05054  -0.07308 148  GLY A C   
1925 O O   . GLY A 123 ? 0.29788 0.20903 0.28723 0.02142  0.04523  -0.07373 148  GLY A O   
1929 N N   . LEU A 124 ? 0.25669 0.19738 0.26080 0.02256  0.05064  -0.07147 149  LEU A N   
1930 C CA  . LEU A 124 ? 0.30646 0.25474 0.30688 0.01997  0.04429  -0.06970 149  LEU A CA  
1931 C C   . LEU A 124 ? 0.28181 0.24701 0.30141 0.02423  0.03350  -0.06046 149  LEU A C   
1932 O O   . LEU A 124 ? 0.28843 0.26233 0.30163 0.02250  0.02480  -0.05132 149  LEU A O   
1933 C CB  . LEU A 124 ? 0.31897 0.27957 0.31095 0.01666  0.04522  -0.06701 149  LEU A CB  
1934 C CG  . LEU A 124 ? 0.36932 0.31880 0.33875 0.01593  0.04706  -0.06329 149  LEU A CG  
1935 C CD1 . LEU A 124 ? 0.32725 0.28510 0.29256 0.01430  0.04872  -0.05896 149  LEU A CD1 
1936 C CD2 . LEU A 124 ? 0.29780 0.23778 0.24885 0.01539  0.04012  -0.06349 149  LEU A CD2 
1948 N N   . LEU A 125 ? 0.23017 0.20037 0.27134 0.03179  0.03441  -0.06163 150  LEU A N   
1949 C CA  . LEU A 125 ? 0.26233 0.24850 0.31710 0.04042  0.02384  -0.05154 150  LEU A CA  
1950 C C   . LEU A 125 ? 0.32789 0.29869 0.39296 0.04864  0.02560  -0.04708 150  LEU A C   
1951 O O   . LEU A 125 ? 0.28996 0.27340 0.37527 0.06036  0.02380  -0.04657 150  LEU A O   
1952 C CB  . LEU A 125 ? 0.26220 0.27815 0.33670 0.04561  0.02026  -0.05784 150  LEU A CB  
1953 C CG  . LEU A 125 ? 0.29451 0.32613 0.36211 0.03852  0.01840  -0.06267 150  LEU A CG  
1954 C CD1 . LEU A 125 ? 0.23628 0.29797 0.33178 0.04280  0.01502  -0.07422 150  LEU A CD1 
1955 C CD2 . LEU A 125 ? 0.36736 0.40182 0.41570 0.03890  0.00831  -0.04967 150  LEU A CD2 
1967 N N   . PRO A 126 ? 0.24180 0.18549 0.29509 0.04316  0.02954  -0.04594 151  PRO A N   
1968 C CA  . PRO A 126 ? 0.34569 0.26872 0.40826 0.05004  0.03352  -0.04239 151  PRO A CA  
1969 C C   . PRO A 126 ? 0.40330 0.33435 0.47485 0.06236  0.02707  -0.02568 151  PRO A C   
1970 O O   . PRO A 126 ? 0.38004 0.31419 0.44190 0.06032  0.02170  -0.01369 151  PRO A O   
1971 C CB  . PRO A 126 ? 0.26347 0.16012 0.31104 0.03838  0.03581  -0.04534 151  PRO A CB  
1972 C CG  . PRO A 126 ? 0.32927 0.23926 0.36249 0.02880  0.02915  -0.04320 151  PRO A CG  
1973 C CD  . PRO A 126 ? 0.26594 0.19901 0.29834 0.03095  0.02888  -0.04788 151  PRO A CD  
1981 N N   . ASP A 127 ? 0.38929 0.32383 0.47832 0.07732  0.02857  -0.02405 152  ASP A N   
1982 C CA  . ASP A 127 ? 0.47212 0.41382 0.56635 0.09461  0.02251  -0.00708 152  ASP A CA  
1983 C C   . ASP A 127 ? 0.44296 0.41982 0.53326 0.09996  0.00936  -0.00267 152  ASP A C   
1984 O O   . ASP A 127 ? 0.48735 0.46873 0.56988 0.11310  0.00329  0.01371  152  ASP A O   
1985 C CB  . ASP A 127 ? 0.47204 0.38258 0.55535 0.09325  0.02773  0.00851  152  ASP A CB  
1986 C CG  . ASP A 127 ? 0.64532 0.54674 0.73482 0.11528  0.02959  0.02580  152  ASP A CG  
1987 O OD1 . ASP A 127 ? 0.70680 0.62670 0.81085 0.13231  0.02551  0.02350  152  ASP A OD1 
1988 O OD2 . ASP A 127 ? 0.66296 0.54117 0.74339 0.11684  0.03534  0.04263  152  ASP A OD2 
1993 N N   . ASP A 128 ? 0.31004 0.30915 0.40346 0.09056  0.00638  -0.01735 153  ASP A N   
1994 C CA  . ASP A 128 ? 0.27889 0.30975 0.36875 0.09253  -0.00533 -0.01824 153  ASP A CA  
1995 C C   . ASP A 128 ? 0.27501 0.29881 0.33931 0.08618  -0.00783 -0.00605 153  ASP A C   
1996 O O   . ASP A 128 ? 0.37847 0.42216 0.43328 0.09413  -0.01760 0.00026  153  ASP A O   
1997 C CB  . ASP A 128 ? 0.29965 0.35821 0.40240 0.11395  -0.01747 -0.01430 153  ASP A CB  
1998 C CG  . ASP A 128 ? 0.28178 0.37836 0.39197 0.11314  -0.02897 -0.02761 153  ASP A CG  
1999 O OD1 . ASP A 128 ? 0.27279 0.36965 0.38313 0.09529  -0.02302 -0.04066 153  ASP A OD1 
2000 O OD2 . ASP A 128 ? 0.30906 0.43474 0.42589 0.13091  -0.04345 -0.02667 153  ASP A OD2 
2005 N N   . LYS A 129 ? 0.27254 0.26991 0.32612 0.07262  0.00071  -0.00381 154  LYS A N   
2006 C CA  . LYS A 129 ? 0.25890 0.25051 0.29426 0.06511  0.00046  0.00670  154  LYS A CA  
2007 C C   . LYS A 129 ? 0.23951 0.23328 0.26744 0.04905  0.00250  -0.00558 154  LYS A C   
2008 O O   . LYS A 129 ? 0.31181 0.29267 0.34231 0.04097  0.00850  -0.01705 154  LYS A O   
2009 C CB  . LYS A 129 ? 0.32193 0.28397 0.35595 0.06377  0.00822  0.01992  154  LYS A CB  
2010 C CG  . LYS A 129 ? 0.26872 0.22502 0.30517 0.08376  0.00855  0.03689  154  LYS A CG  
2011 C CD  . LYS A 129 ? 0.39917 0.31988 0.43835 0.08168  0.02075  0.04904  154  LYS A CD  
2012 C CE  . LYS A 129 ? 0.51493 0.42440 0.55738 0.10406  0.02388  0.06410  154  LYS A CE  
2013 N NZ  . LYS A 129 ? 0.48018 0.41060 0.50677 0.12405  0.01581  0.08018  154  LYS A NZ  
2027 N N   . LEU A 130 ? 0.26601 0.27457 0.28180 0.04653  -0.00170 -0.00270 155  LEU A N   
2028 C CA  . LEU A 130 ? 0.20203 0.21109 0.20800 0.03406  0.00092  -0.01092 155  LEU A CA  
2029 C C   . LEU A 130 ? 0.24572 0.24575 0.24269 0.02759  0.00240  -0.00022 155  LEU A C   
2030 O O   . LEU A 130 ? 0.24148 0.24913 0.23198 0.03221  0.00055  0.01244  155  LEU A O   
2031 C CB  . LEU A 130 ? 0.21664 0.24795 0.21820 0.03542  -0.00296 -0.01729 155  LEU A CB  
2032 C CG  . LEU A 130 ? 0.21505 0.24409 0.20355 0.02546  0.00141  -0.02219 155  LEU A CG  
2033 C CD1 . LEU A 130 ? 0.32053 0.33467 0.31064 0.01937  0.00939  -0.03364 155  LEU A CD1 
2034 C CD2 . LEU A 130 ? 0.27363 0.31951 0.25741 0.02618  -0.00024 -0.02807 155  LEU A CD2 
2046 N N   . THR A 131 ? 0.30464 0.28975 0.30187 0.01774  0.00589  -0.00603 156  THR A N   
2047 C CA  . THR A 131 ? 0.24332 0.22393 0.23993 0.00983  0.00668  0.00051  156  THR A CA  
2048 C C   . THR A 131 ? 0.25618 0.24597 0.24188 0.00360  0.00499  -0.00668 156  THR A C   
2049 O O   . THR A 131 ? 0.26229 0.24653 0.24143 0.00119  0.00535  -0.01907 156  THR A O   
2050 C CB  . THR A 131 ? 0.22666 0.18608 0.23496 0.00343  0.00974  -0.00265 156  THR A CB  
2051 O OG1 . THR A 131 ? 0.21921 0.16702 0.23664 0.01170  0.01348  0.00682  156  THR A OG1 
2052 C CG2 . THR A 131 ? 0.34088 0.30056 0.35625 -0.00650 0.01055  0.00189  156  THR A CG2 
2060 N N   . LEU A 132 ? 0.26052 0.26311 0.24209 0.00322  0.00447  0.00223  157  LEU A N   
2061 C CA  . LEU A 132 ? 0.29252 0.30520 0.26379 0.00037  0.00343  -0.00200 157  LEU A CA  
2062 C C   . LEU A 132 ? 0.22114 0.23725 0.20271 -0.00690 0.00266  0.00203  157  LEU A C   
2063 O O   . LEU A 132 ? 0.30013 0.31487 0.29473 -0.00900 0.00611  0.01306  157  LEU A O   
2064 C CB  . LEU A 132 ? 0.25329 0.27973 0.21342 0.00632  0.00437  0.00254  157  LEU A CB  
2065 C CG  . LEU A 132 ? 0.24602 0.27353 0.20412 0.01210  0.00408  -0.00381 157  LEU A CG  
2066 C CD1 . LEU A 132 ? 0.24386 0.28567 0.19345 0.01778  0.00311  -0.00038 157  LEU A CD1 
2067 C CD2 . LEU A 132 ? 0.25748 0.27755 0.21147 0.00991  0.00763  -0.01762 157  LEU A CD2 
2079 N N   . PHE A 133 ? 0.20157 0.22221 0.17834 -0.00986 -0.00103 -0.00701 158  PHE A N   
2080 C CA  . PHE A 133 ? 0.25377 0.28660 0.24327 -0.01594 -0.00395 -0.00624 158  PHE A CA  
2081 C C   . PHE A 133 ? 0.30895 0.35872 0.28682 -0.01038 -0.00370 -0.00250 158  PHE A C   
2082 O O   . PHE A 133 ? 0.28145 0.32874 0.23851 -0.00350 -0.00314 -0.00702 158  PHE A O   
2083 C CB  . PHE A 133 ? 0.28151 0.31050 0.27486 -0.02115 -0.01149 -0.02157 158  PHE A CB  
2084 C CG  . PHE A 133 ? 0.31878 0.32804 0.32082 -0.02593 -0.01078 -0.02798 158  PHE A CG  
2085 C CD1 . PHE A 133 ? 0.36489 0.36809 0.39276 -0.03486 -0.00741 -0.02413 158  PHE A CD1 
2086 C CD2 . PHE A 133 ? 0.36945 0.36353 0.35446 -0.02105 -0.01071 -0.03748 158  PHE A CD2 
2087 C CE1 . PHE A 133 ? 0.39945 0.38060 0.43482 -0.03829 -0.00511 -0.03028 158  PHE A CE1 
2088 C CE2 . PHE A 133 ? 0.40210 0.37675 0.39471 -0.02413 -0.00891 -0.04397 158  PHE A CE2 
2089 C CZ  . PHE A 133 ? 0.35842 0.32596 0.37550 -0.03234 -0.00656 -0.04050 158  PHE A CZ  
2099 N N   . CYS A 134 ? 0.21516 0.28017 0.20749 -0.01301 -0.00169 0.00595  159  CYS A N   
2100 C CA  A CYS A 134 ? 0.29400 0.37618 0.27888 -0.00715 -0.00109 0.00903  159  CYS A CA  
2101 C CA  B CYS A 134 ? 0.29181 0.37392 0.27655 -0.00713 -0.00119 0.00886  159  CYS A CA  
2102 C C   . CYS A 134 ? 0.31044 0.41154 0.32049 -0.01329 -0.00590 0.00609  159  CYS A C   
2103 O O   . CYS A 134 ? 0.26204 0.36752 0.29905 -0.02210 -0.00144 0.01176  159  CYS A O   
2104 C CB  A CYS A 134 ? 0.28658 0.37295 0.26468 -0.00193 0.00795  0.02249  159  CYS A CB  
2105 C CB  B CYS A 134 ? 0.28417 0.37039 0.26108 -0.00157 0.00774  0.02197  159  CYS A CB  
2106 S SG  A CYS A 134 ? 0.23587 0.34090 0.20532 0.00642  0.01139  0.02639  159  CYS A SG  
2107 S SG  B CYS A 134 ? 0.34820 0.44696 0.34958 -0.00625 0.01607  0.03640  159  CYS A SG  
2116 N N   . GLU A 135 ? 0.26395 0.37635 0.26675 -0.00807 -0.01424 -0.00292 160  GLU A N   
2117 C CA  . GLU A 135 ? 0.26995 0.40809 0.29854 -0.01153 -0.02172 -0.00808 160  GLU A CA  
2118 C C   . GLU A 135 ? 0.28650 0.44261 0.30871 -0.00068 -0.01736 0.00096  160  GLU A C   
2119 O O   . GLU A 135 ? 0.26185 0.41281 0.25448 0.01209  -0.01796 0.00033  160  GLU A O   
2120 C CB  . GLU A 135 ? 0.27385 0.41477 0.29756 -0.01027 -0.03698 -0.02606 160  GLU A CB  
2121 C CG  . GLU A 135 ? 0.40397 0.57589 0.43585 -0.00274 -0.04806 -0.03197 160  GLU A CG  
2122 C CD  . GLU A 135 ? 0.48729 0.66238 0.50501 0.00315  -0.06547 -0.05057 160  GLU A CD  
2123 O OE1 . GLU A 135 ? 0.46335 0.62592 0.48682 -0.00672 -0.07110 -0.06348 160  GLU A OE1 
2124 O OE2 . GLU A 135 ? 0.42915 0.61671 0.42563 0.01992  -0.07248 -0.05160 160  GLU A OE2 
2131 N N   . VAL A 136 ? 0.29751 0.47246 0.34808 -0.00539 -0.01065 0.00957  161  VAL A N   
2132 C CA  . VAL A 136 ? 0.26659 0.46007 0.31628 0.00464  -0.00446 0.01853  161  VAL A CA  
2133 C C   . VAL A 136 ? 0.22904 0.45652 0.30948 0.00480  -0.01478 0.01046  161  VAL A C   
2134 O O   . VAL A 136 ? 0.24440 0.48685 0.36499 -0.00897 -0.01738 0.00492  161  VAL A O   
2135 C CB  . VAL A 136 ? 0.22662 0.41848 0.28556 0.00134  0.01244  0.03443  161  VAL A CB  
2136 C CG1 . VAL A 136 ? 0.22620 0.43624 0.28351 0.01258  0.02115  0.04347  161  VAL A CG1 
2137 C CG2 . VAL A 136 ? 0.30256 0.46570 0.33315 0.00241  0.01852  0.03984  161  VAL A CG2 
2147 N N   . SER A 137 ? 0.25607 0.49672 0.32053 0.02086  -0.01960 0.00978  162  SER A N   
2148 C CA  . SER A 137 ? 0.26546 0.54383 0.35725 0.02593  -0.03174 0.00200  162  SER A CA  
2149 C C   . SER A 137 ? 0.23230 0.53004 0.33269 0.03639  -0.01994 0.01492  162  SER A C   
2150 O O   . SER A 137 ? 0.19758 0.48828 0.26558 0.05440  -0.01656 0.02070  162  SER A O   
2151 C CB  . SER A 137 ? 0.26500 0.54320 0.32731 0.04098  -0.04868 -0.00943 162  SER A CB  
2152 O OG  . SER A 137 ? 0.26253 0.52312 0.31647 0.03201  -0.05850 -0.02237 162  SER A OG  
2158 N N   . VAL A 138 ? 0.18520 0.50581 0.33013 0.02553  -0.01177 0.01920  163  VAL A N   
2159 C CA  . VAL A 138 ? 0.17544 0.51063 0.33048 0.03381  0.00288  0.03179  163  VAL A CA  
2160 C C   . VAL A 138 ? 0.23344 0.59673 0.41255 0.04128  -0.00872 0.02312  163  VAL A C   
2161 O O   . VAL A 138 ? 0.13470 0.51968 0.35671 0.02964  -0.01952 0.01066  163  VAL A O   
2162 C CB  . VAL A 138 ? 0.24361 0.57427 0.42539 0.01913  0.02243  0.04267  163  VAL A CB  
2163 C CG1 . VAL A 138 ? 0.31927 0.65323 0.50295 0.02823  0.03732  0.05308  163  VAL A CG1 
2164 C CG2 . VAL A 138 ? 0.25931 0.55451 0.40947 0.01427  0.03261  0.05150  163  VAL A CG2 
2174 N N   . VAL A 139 ? 0.20006 0.56134 0.35249 0.06071  -0.00568 0.02944  164  VAL A N   
2175 C CA  . VAL A 139 ? 0.25130 0.63801 0.42176 0.07171  -0.01436 0.02450  164  VAL A CA  
2176 C C   . VAL A 139 ? 0.24960 0.65532 0.46326 0.06512  0.00022  0.03099  164  VAL A C   
2177 O O   . VAL A 139 ? 0.36379 0.75294 0.56205 0.06736  0.02027  0.04493  164  VAL A O   
2178 C CB  . VAL A 139 ? 0.34502 0.71648 0.46686 0.09565  -0.01295 0.03059  164  VAL A CB  
2179 C CG1 . VAL A 139 ? 0.40305 0.79965 0.53818 0.10899  -0.02558 0.02422  164  VAL A CG1 
2180 C CG2 . VAL A 139 ? 0.41122 0.75294 0.48636 0.10070  -0.01833 0.02737  164  VAL A CG2 
2190 N N   . GLN A 140 ? 0.15939 0.59706 0.42630 0.05703  -0.00932 0.01991  165  GLN A N   
2191 C CA  . GLN A 140 ? 0.27508 0.73127 0.59059 0.04897  0.00663  0.02395  165  GLN A CA  
2192 C C   . GLN A 140 ? 0.23636 0.71083 0.55518 0.06737  0.00815  0.02767  165  GLN A C   
2193 O O   . GLN A 140 ? 0.21590 0.70451 0.52662 0.08167  -0.01027 0.02081  165  GLN A O   
2194 C CB  . GLN A 140 ? 0.24089 0.72233 0.62216 0.02885  -0.00135 0.00968  165  GLN A CB  
2195 C CG  . GLN A 140 ? 0.30536 0.76755 0.68144 0.01177  -0.00583 0.00441  165  GLN A CG  
2196 C CD  . GLN A 140 ? 0.38768 0.85437 0.82160 -0.01190 0.00902  0.00249  165  GLN A CD  
2197 O OE1 . GLN A 140 ? 0.46351 0.95854 0.95338 -0.02244 0.00019  -0.00148 165  GLN A OE1 
2198 N NE2 . GLN A 140 ? 0.46490 0.90391 0.87815 -0.02065 0.03156  0.01167  165  GLN A NE2 
2207 N N   . ASP A 141 ? 0.32441 0.79562 0.65070 0.06783  0.03100  0.03891  166  ASP A N   
2208 C CA  . ASP A 141 ? 0.34500 0.83097 0.67459 0.08490  0.03611  0.04371  166  ASP A CA  
2209 C C   . ASP A 141 ? 0.32390 0.85526 0.72562 0.07985  0.02832  0.03098  166  ASP A C   
2210 O O   . ASP A 141 ? 0.20056 0.74513 0.65292 0.05939  0.03153  0.02231  166  ASP A O   
2211 C CB  . ASP A 141 ? 0.37969 0.84171 0.68725 0.08670  0.06339  0.05943  166  ASP A CB  
2212 C CG  . ASP A 141 ? 0.57046 0.98687 0.80932 0.09269  0.06909  0.07058  166  ASP A CG  
2213 O OD1 . ASP A 141 ? 0.62326 1.02811 0.82245 0.10916  0.06091  0.07210  166  ASP A OD1 
2214 O OD2 . ASP A 141 ? 0.45074 0.84156 0.67566 0.08130  0.08208  0.07709  166  ASP A OD2 
2219 N N   . LYS B 2   ? 0.78411 0.54191 0.87462 -0.10197 0.14431  0.05206  1364 LYS B N   
2220 C CA  . LYS B 2   ? 0.88232 0.62521 0.98393 -0.12177 0.17285  0.05199  1364 LYS B CA  
2221 C C   . LYS B 2   ? 0.91815 0.70052 1.03801 -0.13333 0.18663  0.04676  1364 LYS B C   
2222 O O   . LYS B 2   ? 0.97978 0.75058 1.09292 -0.14462 0.21321  0.05562  1364 LYS B O   
2223 C CB  . LYS B 2   ? 0.90816 0.59343 0.96189 -0.10997 0.18653  0.08149  1364 LYS B CB  
2225 N N   . GLY B 3   ? 0.77725 0.60663 0.92222 -0.13045 0.16962  0.03094  1365 GLY B N   
2226 C CA  . GLY B 3   ? 0.73750 0.60384 0.89301 -0.13161 0.17826  0.02882  1365 GLY B CA  
2227 C C   . GLY B 3   ? 0.72964 0.58785 0.84324 -0.10913 0.16724  0.04808  1365 GLY B C   
2228 O O   . GLY B 3   ? 0.68921 0.57566 0.80811 -0.10693 0.17471  0.04585  1365 GLY B O   
2232 N N   . SER B 4   ? 0.67550 0.50000 0.75008 -0.09183 0.15021  0.06382  1366 SER B N   
2233 C CA  . SER B 4   ? 0.49140 0.30813 0.52153 -0.07067 0.13901  0.08067  1366 SER B CA  
2234 C C   . SER B 4   ? 0.47633 0.32870 0.52288 -0.06387 0.11567  0.06413  1366 SER B C   
2235 O O   . SER B 4   ? 0.45934 0.33215 0.54036 -0.06884 0.10058  0.04534  1366 SER B O   
2236 C CB  . SER B 4   ? 0.67275 0.45747 0.66649 -0.05307 0.12388  0.09561  1366 SER B CB  
2237 O OG  . SER B 4   ? 0.80326 0.55491 0.77784 -0.05368 0.14043  0.11009  1366 SER B OG  
2243 N N   . VAL B 5   ? 0.34642 0.20894 0.36227 -0.04951 0.10861  0.06825  1367 VAL B N   
2244 C CA  . VAL B 5   ? 0.30865 0.19598 0.32976 -0.03980 0.08393  0.05313  1367 VAL B CA  
2245 C C   . VAL B 5   ? 0.36650 0.24577 0.38316 -0.03563 0.06134  0.05176  1367 VAL B C   
2246 O O   . VAL B 5   ? 0.30384 0.19878 0.33415 -0.03361 0.04450  0.03900  1367 VAL B O   
2247 C CB  . VAL B 5   ? 0.32436 0.21394 0.30976 -0.02767 0.08290  0.05541  1367 VAL B CB  
2248 C CG1 . VAL B 5   ? 0.39000 0.29167 0.38052 -0.01998 0.06309  0.04060  1367 VAL B CG1 
2249 C CG2 . VAL B 5   ? 0.42168 0.32085 0.40755 -0.03139 0.11039  0.05672  1367 VAL B CG2 
2259 N N   . GLN B 6   ? 0.33197 0.18715 0.32630 -0.03144 0.06131  0.06546  1368 GLN B N   
2260 C CA  . GLN B 6   ? 0.29102 0.14517 0.28059 -0.02548 0.04210  0.06255  1368 GLN B CA  
2261 C C   . GLN B 6   ? 0.42978 0.25622 0.41750 -0.02268 0.04927  0.07301  1368 GLN B C   
2262 O O   . GLN B 6   ? 0.35765 0.15688 0.33164 -0.02183 0.06824  0.08907  1368 GLN B O   
2263 C CB  . GLN B 6   ? 0.34285 0.20566 0.30175 -0.01504 0.02843  0.06385  1368 GLN B CB  
2264 C CG  . GLN B 6   ? 0.29301 0.16950 0.24704 -0.01710 0.02264  0.05298  1368 GLN B CG  
2265 C CD  . GLN B 6   ? 0.31497 0.19882 0.24297 -0.01331 0.01160  0.04887  1368 GLN B CD  
2266 O OE1 . GLN B 6   ? 0.30660 0.19308 0.20980 -0.00572 0.01347  0.05423  1368 GLN B OE1 
2267 N NE2 . GLN B 6   ? 0.29420 0.18297 0.22638 -0.01983 0.00100  0.03805  1368 GLN B NE2 
2276 N N   . ALA B 7   ? 0.32778 0.15665 0.32651 -0.02040 0.03654  0.06429  1369 ALA B N   
2277 C CA  . ALA B 7   ? 0.38173 0.18175 0.37364 -0.00997 0.04029  0.07321  1369 ALA B CA  
2278 C C   . ALA B 7   ? 0.34848 0.16961 0.32945 0.00525  0.02059  0.06875  1369 ALA B C   
2279 O O   . ALA B 7   ? 0.33672 0.18599 0.32915 -0.00196 0.00870  0.05331  1369 ALA B O   
2280 C CB  . ALA B 7   ? 0.44370 0.22668 0.46823 -0.02327 0.04880  0.06036  1369 ALA B CB  
2286 N N   . PRO B 8   ? 0.35088 0.16150 0.30861 0.02729  0.01767  0.08207  1370 PRO B N   
2287 C CA  . PRO B 8   ? 0.41532 0.26149 0.36984 0.04146  -0.00130 0.07317  1370 PRO B CA  
2288 C C   . PRO B 8   ? 0.49552 0.34458 0.47111 0.04901  -0.00608 0.06076  1370 PRO B C   
2289 O O   . PRO B 8   ? 0.41245 0.30103 0.39311 0.05729  -0.01940 0.04888  1370 PRO B O   
2290 C CB  . PRO B 8   ? 0.40090 0.24380 0.32005 0.06750  -0.00510 0.09154  1370 PRO B CB  
2291 C CG  . PRO B 8   ? 0.57811 0.36114 0.48152 0.07366  0.01552  0.11462  1370 PRO B CG  
2292 C CD  . PRO B 8   ? 0.44906 0.21870 0.37814 0.04158  0.03215  0.10695  1370 PRO B CD  
2300 N N   . GLU B 9   ? 0.38867 0.20051 0.37917 0.04461  0.00600  0.05926  1371 GLU B N   
2301 C CA  . GLU B 9   ? 0.43540 0.24769 0.44487 0.05263  0.00305  0.04337  1371 GLU B CA  
2302 C C   . GLU B 9   ? 0.46408 0.32675 0.48856 0.04025  -0.00804 0.02122  1371 GLU B C   
2303 O O   . GLU B 9   ? 0.41062 0.28597 0.43864 0.01854  -0.00832 0.01512  1371 GLU B O   
2304 C CB  . GLU B 9   ? 0.57795 0.34615 0.60541 0.03976  0.01854  0.03621  1371 GLU B CB  
2305 C CG  . GLU B 9   ? 0.66485 0.36786 0.67862 0.05163  0.03598  0.05606  1371 GLU B CG  
2306 C CD  . GLU B 9   ? 0.70740 0.40043 0.70411 0.03696  0.04662  0.07451  1371 GLU B CD  
2307 O OE1 . GLU B 9   ? 0.73136 0.39257 0.70699 0.04412  0.05580  0.09147  1371 GLU B OE1 
2308 O OE2 . GLU B 9   ? 0.59949 0.32068 0.60450 0.01883  0.04563  0.07024  1371 GLU B OE2 
2315 N N   . ILE B 10  ? 0.44952 0.33886 0.48186 0.05586  -0.01522 0.00933  1372 ILE B N   
2316 C CA  . ILE B 10  ? 0.38329 0.31750 0.42729 0.04324  -0.01985 -0.01134 1372 ILE B CA  
2317 C C   . ILE B 10  ? 0.41261 0.33919 0.47287 0.04623  -0.01479 -0.03037 1372 ILE B C   
2318 O O   . ILE B 10  ? 0.35343 0.25694 0.42048 0.06907  -0.01199 -0.03192 1372 ILE B O   
2319 C CB  . ILE B 10  ? 0.40229 0.38777 0.44792 0.05407  -0.02919 -0.01640 1372 ILE B CB  
2320 C CG1 . ILE B 10  ? 0.31673 0.31316 0.34639 0.03979  -0.03312 -0.00671 1372 ILE B CG1 
2321 C CG2 . ILE B 10  ? 0.31356 0.34239 0.37542 0.04512  -0.02731 -0.03969 1372 ILE B CG2 
2322 C CD1 . ILE B 10  ? 0.39969 0.45060 0.43386 0.04516  -0.04276 -0.01624 1372 ILE B CD1 
2334 N N   . SER B 11  ? 0.36988 0.31347 0.43201 0.02563  -0.01354 -0.04527 1373 SER B N   
2335 C CA  . SER B 11  ? 0.33470 0.27638 0.40776 0.02548  -0.00922 -0.06801 1373 SER B CA  
2336 C C   . SER B 11  ? 0.30124 0.28436 0.36539 0.01065  -0.00954 -0.08186 1373 SER B C   
2337 O O   . SER B 11  ? 0.25116 0.25322 0.30091 -0.00206 -0.01126 -0.07166 1373 SER B O   
2338 C CB  . SER B 11  ? 0.31099 0.21489 0.38975 0.01376  -0.00520 -0.07205 1373 SER B CB  
2339 O OG  . SER B 11  ? 0.38324 0.30107 0.45131 -0.00540 -0.01011 -0.06608 1373 SER B OG  
2345 N N   . SER B 12  ? 0.34605 0.33713 0.41475 0.01175  -0.00555 -0.10558 1374 SER B N   
2346 C CA  . SER B 12  ? 0.37616 0.40555 0.42959 0.00071  -0.00176 -0.11883 1374 SER B CA  
2347 C C   . SER B 12  ? 0.44904 0.47447 0.49036 -0.00784 -0.00287 -0.13699 1374 SER B C   
2348 O O   . SER B 12  ? 0.49830 0.49628 0.54814 -0.01041 -0.00805 -0.14051 1374 SER B O   
2349 C CB  . SER B 12  ? 0.33657 0.40222 0.40497 0.01459  0.00585  -0.13603 1374 SER B CB  
2350 O OG  . SER B 12  ? 0.45299 0.49838 0.54116 0.03539  0.00744  -0.15372 1374 SER B OG  
2356 N N   . ASN B 13  ? 0.69114 0.74848 0.71198 -0.01339 0.00301  -0.15043 1375 ASN B N   
2357 C CA  . ASN B 13  ? 0.69273 0.75672 0.69319 -0.01842 0.00028  -0.17057 1375 ASN B CA  
2358 C C   . ASN B 13  ? 0.60802 0.65485 0.59803 -0.02630 -0.01362 -0.16035 1375 ASN B C   
2359 O O   . ASN B 13  ? 0.66825 0.71326 0.66454 -0.02736 -0.02138 -0.18169 1375 ASN B O   
2360 C CB  . ASN B 13  ? 0.67315 0.73200 0.69640 -0.00742 0.00336  -0.20423 1375 ASN B CB  
2363 N N   . SER B 14  ? 0.50899 0.54735 0.48610 -0.03173 -0.01671 -0.13122 1376 SER B N   
2364 C CA  . SER B 14  ? 0.46130 0.48988 0.43033 -0.03469 -0.02991 -0.12172 1376 SER B CA  
2365 C C   . SER B 14  ? 0.60121 0.65093 0.53834 -0.03330 -0.03957 -0.13595 1376 SER B C   
2366 O O   . SER B 14  ? 0.61136 0.66514 0.55094 -0.03142 -0.05439 -0.13856 1376 SER B O   
2367 C CB  . SER B 14  ? 0.42138 0.43689 0.37358 -0.03791 -0.02956 -0.09086 1376 SER B CB  
2368 O OG  . SER B 14  ? 0.61888 0.64055 0.52536 -0.04119 -0.02514 -0.08070 1376 SER B OG  
2374 N N   . ILE B 15  ? 0.61068 0.67943 0.51651 -0.03272 -0.03168 -0.14585 1377 ILE B N   
2375 C CA  . ILE B 15  ? 0.68329 0.77554 0.55228 -0.02807 -0.04121 -0.16316 1377 ILE B CA  
2376 C C   . ILE B 15  ? 0.65681 0.76417 0.55479 -0.02740 -0.04288 -0.20539 1377 ILE B C   
2377 O O   . ILE B 15  ? 0.68764 0.79153 0.60840 -0.02722 -0.02830 -0.21881 1377 ILE B O   
2378 C CB  . ILE B 15  ? 0.61382 0.71524 0.42362 -0.02900 -0.02768 -0.15060 1377 ILE B CB  
# 
