data_9MT0
# 
_entry.id   9MT0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9MT0         pdb_00009mt0 10.2210/pdb9mt0/pdb 
WWPDB D_1000291110 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        9MT0 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              berrye@upstate.edu 
_pdbx_contact_author.name_first         Edward 
_pdbx_contact_author.name_last          Berry 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8929-0259 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zafreen, L.'  1 ?                   
'Huang, L.-S.' 2 0000-0003-1427-2544 
'Luemmen, P.'  3 ?                   
'Berry, E.A.'  4 0000-0001-8929-0259 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal Structure of Insect Cytochrome c at different pH values.' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zafreen, L.'  1 ?                   
primary 'Huang, L.-S.' 2 0000-0003-1427-2544 
primary 'Luemmen, P.'  3 ?                   
primary 'Berry, E.A.'  4 0000-0001-8929-0259 
# 
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     nat 'Cytochrome c' 11658.432 2   ? ? ? ? 
2 non-polymer syn 'HEME C'       618.503   2   ? ? ? ? 
3 non-polymer syn ETHANOL        46.068    1   ? ? ? ? 
4 water       nat water          18.015    303 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GVPAGDVEKGKKIFVQRCAQCHTVEAGGKHKVGPNLHGLFGRKTGQAAGFAYTDANKAKGITWNEDTLFEYLENPKKYIP
GTKMIFAGLKKPNERGDLIAYLKSATK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GVPAGDVEKGKKIFVQRCAQCHTVEAGGKHKVGPNLHGLFGRKTGQAAGFAYTDANKAKGITWNEDTLFEYLENPKKYIP
GTKMIFAGLKKPNERGDLIAYLKSATK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'HEME C' HEC 
3 ETHANOL  EOH 
4 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   VAL n 
1 3   PRO n 
1 4   ALA n 
1 5   GLY n 
1 6   ASP n 
1 7   VAL n 
1 8   GLU n 
1 9   LYS n 
1 10  GLY n 
1 11  LYS n 
1 12  LYS n 
1 13  ILE n 
1 14  PHE n 
1 15  VAL n 
1 16  GLN n 
1 17  ARG n 
1 18  CYS n 
1 19  ALA n 
1 20  GLN n 
1 21  CYS n 
1 22  HIS n 
1 23  THR n 
1 24  VAL n 
1 25  GLU n 
1 26  ALA n 
1 27  GLY n 
1 28  GLY n 
1 29  LYS n 
1 30  HIS n 
1 31  LYS n 
1 32  VAL n 
1 33  GLY n 
1 34  PRO n 
1 35  ASN n 
1 36  LEU n 
1 37  HIS n 
1 38  GLY n 
1 39  LEU n 
1 40  PHE n 
1 41  GLY n 
1 42  ARG n 
1 43  LYS n 
1 44  THR n 
1 45  GLY n 
1 46  GLN n 
1 47  ALA n 
1 48  ALA n 
1 49  GLY n 
1 50  PHE n 
1 51  ALA n 
1 52  TYR n 
1 53  THR n 
1 54  ASP n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  ALA n 
1 59  LYS n 
1 60  GLY n 
1 61  ILE n 
1 62  THR n 
1 63  TRP n 
1 64  ASN n 
1 65  GLU n 
1 66  ASP n 
1 67  THR n 
1 68  LEU n 
1 69  PHE n 
1 70  GLU n 
1 71  TYR n 
1 72  LEU n 
1 73  GLU n 
1 74  ASN n 
1 75  PRO n 
1 76  LYS n 
1 77  LYS n 
1 78  TYR n 
1 79  ILE n 
1 80  PRO n 
1 81  GLY n 
1 82  THR n 
1 83  LYS n 
1 84  MET n 
1 85  ILE n 
1 86  PHE n 
1 87  ALA n 
1 88  GLY n 
1 89  LEU n 
1 90  LYS n 
1 91  LYS n 
1 92  PRO n 
1 93  ASN n 
1 94  GLU n 
1 95  ARG n 
1 96  GLY n 
1 97  ASP n 
1 98  LEU n 
1 99  ILE n 
1 100 ALA n 
1 101 TYR n 
1 102 LEU n 
1 103 LYS n 
1 104 SER n 
1 105 ALA n 
1 106 THR n 
1 107 LYS n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           107 
_entity_src_nat.common_name                'house fly' 
_entity_src_nat.pdbx_organism_scientific   'Musca domestica' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      7370 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     'flight muscle' 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 thorax 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.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 
EOH non-polymer         . ETHANOL         ? 'C2 H6 O'          46.068  
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  
HEC non-polymer         . 'HEME C'        ? 'C34 H34 Fe N4 O4' 618.503 
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER           ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -3  -3  GLY GLY A . n 
A 1 2   VAL 2   -2  -2  VAL VAL A . n 
A 1 3   PRO 3   -1  -1  PRO PRO A . n 
A 1 4   ALA 4   0   0   ALA ALA A . n 
A 1 5   GLY 5   1   1   GLY GLY A . n 
A 1 6   ASP 6   2   2   ASP ASP A . n 
A 1 7   VAL 7   3   3   VAL VAL A . n 
A 1 8   GLU 8   4   4   GLU GLU A . n 
A 1 9   LYS 9   5   5   LYS LYS A . n 
A 1 10  GLY 10  6   6   GLY GLY A . n 
A 1 11  LYS 11  7   7   LYS LYS A . n 
A 1 12  LYS 12  8   8   LYS LYS A . n 
A 1 13  ILE 13  9   9   ILE ILE A . n 
A 1 14  PHE 14  10  10  PHE PHE A . n 
A 1 15  VAL 15  11  11  VAL VAL A . n 
A 1 16  GLN 16  12  12  GLN GLN A . n 
A 1 17  ARG 17  13  13  ARG ARG A . n 
A 1 18  CYS 18  14  14  CYS CYS A . n 
A 1 19  ALA 19  15  15  ALA ALA A . n 
A 1 20  GLN 20  16  16  GLN GLN A . n 
A 1 21  CYS 21  17  17  CYS CYS A . n 
A 1 22  HIS 22  18  18  HIS HIS A . n 
A 1 23  THR 23  19  19  THR THR A . n 
A 1 24  VAL 24  20  20  VAL VAL A . n 
A 1 25  GLU 25  21  21  GLU GLU A . n 
A 1 26  ALA 26  22  22  ALA ALA A . n 
A 1 27  GLY 27  23  23  GLY GLY A . n 
A 1 28  GLY 28  24  24  GLY GLY A . n 
A 1 29  LYS 29  25  25  LYS LYS A . n 
A 1 30  HIS 30  26  26  HIS HIS A . n 
A 1 31  LYS 31  27  27  LYS LYS A . n 
A 1 32  VAL 32  28  28  VAL VAL A . n 
A 1 33  GLY 33  29  29  GLY GLY A . n 
A 1 34  PRO 34  30  30  PRO PRO A . n 
A 1 35  ASN 35  31  31  ASN ASN A . n 
A 1 36  LEU 36  32  32  LEU LEU A . n 
A 1 37  HIS 37  33  33  HIS HIS A . n 
A 1 38  GLY 38  34  34  GLY GLY A . n 
A 1 39  LEU 39  35  35  LEU LEU A . n 
A 1 40  PHE 40  36  36  PHE PHE A . n 
A 1 41  GLY 41  37  37  GLY GLY A . n 
A 1 42  ARG 42  38  38  ARG ARG A . n 
A 1 43  LYS 43  39  39  LYS LYS A . n 
A 1 44  THR 44  40  40  THR THR A . n 
A 1 45  GLY 45  41  41  GLY GLY A . n 
A 1 46  GLN 46  42  42  GLN GLN A . n 
A 1 47  ALA 47  43  43  ALA ALA A . n 
A 1 48  ALA 48  44  44  ALA ALA A . n 
A 1 49  GLY 49  45  45  GLY GLY A . n 
A 1 50  PHE 50  46  46  PHE PHE A . n 
A 1 51  ALA 51  47  47  ALA ALA A . n 
A 1 52  TYR 52  48  48  TYR TYR A . n 
A 1 53  THR 53  49  49  THR THR A . n 
A 1 54  ASP 54  50  50  ASP ASP A . n 
A 1 55  ALA 55  51  51  ALA ALA A . n 
A 1 56  ASN 56  52  52  ASN ASN A . n 
A 1 57  LYS 57  53  53  LYS LYS A . n 
A 1 58  ALA 58  54  54  ALA ALA A . n 
A 1 59  LYS 59  55  55  LYS LYS A . n 
A 1 60  GLY 60  56  56  GLY GLY A . n 
A 1 61  ILE 61  57  57  ILE ILE A . n 
A 1 62  THR 62  58  58  THR THR A . n 
A 1 63  TRP 63  59  59  TRP TRP A . n 
A 1 64  ASN 64  60  60  ASN ASN A . n 
A 1 65  GLU 65  61  61  GLU GLU A . n 
A 1 66  ASP 66  62  62  ASP ASP A . n 
A 1 67  THR 67  63  63  THR THR A . n 
A 1 68  LEU 68  64  64  LEU LEU A . n 
A 1 69  PHE 69  65  65  PHE PHE A . n 
A 1 70  GLU 70  66  66  GLU GLU A . n 
A 1 71  TYR 71  67  67  TYR TYR A . n 
A 1 72  LEU 72  68  68  LEU LEU A . n 
A 1 73  GLU 73  69  69  GLU GLU A . n 
A 1 74  ASN 74  70  70  ASN ASN A . n 
A 1 75  PRO 75  71  71  PRO PRO A . n 
A 1 76  LYS 76  72  72  LYS LYS A . n 
A 1 77  LYS 77  73  73  LYS LYS A . n 
A 1 78  TYR 78  74  74  TYR TYR A . n 
A 1 79  ILE 79  75  75  ILE ILE A . n 
A 1 80  PRO 80  76  76  PRO PRO A . n 
A 1 81  GLY 81  77  77  GLY GLY A . n 
A 1 82  THR 82  78  78  THR THR A . n 
A 1 83  LYS 83  79  79  LYS LYS A . n 
A 1 84  MET 84  80  80  MET MET A . n 
A 1 85  ILE 85  81  81  ILE ILE A . n 
A 1 86  PHE 86  82  82  PHE PHE A . n 
A 1 87  ALA 87  83  83  ALA ALA A . n 
A 1 88  GLY 88  84  84  GLY GLY A . n 
A 1 89  LEU 89  85  85  LEU LEU A . n 
A 1 90  LYS 90  86  86  LYS LYS A . n 
A 1 91  LYS 91  87  87  LYS LYS A . n 
A 1 92  PRO 92  88  88  PRO PRO A . n 
A 1 93  ASN 93  89  89  ASN ASN A . n 
A 1 94  GLU 94  90  90  GLU GLU A . n 
A 1 95  ARG 95  91  91  ARG ARG A . n 
A 1 96  GLY 96  92  92  GLY GLY A . n 
A 1 97  ASP 97  93  93  ASP ASP A . n 
A 1 98  LEU 98  94  94  LEU LEU A . n 
A 1 99  ILE 99  95  95  ILE ILE A . n 
A 1 100 ALA 100 96  96  ALA ALA A . n 
A 1 101 TYR 101 97  97  TYR TYR A . n 
A 1 102 LEU 102 98  98  LEU LEU A . n 
A 1 103 LYS 103 99  99  LYS LYS A . n 
A 1 104 SER 104 100 100 SER SER A . n 
A 1 105 ALA 105 101 101 ALA ALA A . n 
A 1 106 THR 106 102 102 THR THR A . n 
A 1 107 LYS 107 103 103 LYS LYS A . n 
B 1 1   GLY 1   -3  -3  GLY GLY B . n 
B 1 2   VAL 2   -2  -2  VAL VAL B . n 
B 1 3   PRO 3   -1  -1  PRO PRO B . n 
B 1 4   ALA 4   0   0   ALA ALA B . n 
B 1 5   GLY 5   1   1   GLY GLY B . n 
B 1 6   ASP 6   2   2   ASP ASP B . n 
B 1 7   VAL 7   3   3   VAL VAL B . n 
B 1 8   GLU 8   4   4   GLU GLU B . n 
B 1 9   LYS 9   5   5   LYS LYS B . n 
B 1 10  GLY 10  6   6   GLY GLY B . n 
B 1 11  LYS 11  7   7   LYS LYS B . n 
B 1 12  LYS 12  8   8   LYS LYS B . n 
B 1 13  ILE 13  9   9   ILE ILE B . n 
B 1 14  PHE 14  10  10  PHE PHE B . n 
B 1 15  VAL 15  11  11  VAL VAL B . n 
B 1 16  GLN 16  12  12  GLN GLN B . n 
B 1 17  ARG 17  13  13  ARG ARG B . n 
B 1 18  CYS 18  14  14  CYS CYS B . n 
B 1 19  ALA 19  15  15  ALA ALA B . n 
B 1 20  GLN 20  16  16  GLN GLN B . n 
B 1 21  CYS 21  17  17  CYS CYS B . n 
B 1 22  HIS 22  18  18  HIS HIS B . n 
B 1 23  THR 23  19  19  THR THR B . n 
B 1 24  VAL 24  20  20  VAL VAL B . n 
B 1 25  GLU 25  21  21  GLU GLU B . n 
B 1 26  ALA 26  22  22  ALA ALA B . n 
B 1 27  GLY 27  23  23  GLY GLY B . n 
B 1 28  GLY 28  24  24  GLY GLY B . n 
B 1 29  LYS 29  25  25  LYS LYS B . n 
B 1 30  HIS 30  26  26  HIS HIS B . n 
B 1 31  LYS 31  27  27  LYS LYS B . n 
B 1 32  VAL 32  28  28  VAL VAL B . n 
B 1 33  GLY 33  29  29  GLY GLY B . n 
B 1 34  PRO 34  30  30  PRO PRO B . n 
B 1 35  ASN 35  31  31  ASN ASN B . n 
B 1 36  LEU 36  32  32  LEU LEU B . n 
B 1 37  HIS 37  33  33  HIS HIS B . n 
B 1 38  GLY 38  34  34  GLY GLY B . n 
B 1 39  LEU 39  35  35  LEU LEU B . n 
B 1 40  PHE 40  36  36  PHE PHE B . n 
B 1 41  GLY 41  37  37  GLY GLY B . n 
B 1 42  ARG 42  38  38  ARG ARG B . n 
B 1 43  LYS 43  39  39  LYS LYS B . n 
B 1 44  THR 44  40  40  THR THR B . n 
B 1 45  GLY 45  41  41  GLY GLY B . n 
B 1 46  GLN 46  42  42  GLN GLN B . n 
B 1 47  ALA 47  43  43  ALA ALA B . n 
B 1 48  ALA 48  44  44  ALA ALA B . n 
B 1 49  GLY 49  45  45  GLY GLY B . n 
B 1 50  PHE 50  46  46  PHE PHE B . n 
B 1 51  ALA 51  47  47  ALA ALA B . n 
B 1 52  TYR 52  48  48  TYR TYR B . n 
B 1 53  THR 53  49  49  THR THR B . n 
B 1 54  ASP 54  50  50  ASP ASP B . n 
B 1 55  ALA 55  51  51  ALA ALA B . n 
B 1 56  ASN 56  52  52  ASN ASN B . n 
B 1 57  LYS 57  53  53  LYS LYS B . n 
B 1 58  ALA 58  54  54  ALA ALA B . n 
B 1 59  LYS 59  55  55  LYS LYS B . n 
B 1 60  GLY 60  56  56  GLY GLY B . n 
B 1 61  ILE 61  57  57  ILE ILE B . n 
B 1 62  THR 62  58  58  THR THR B . n 
B 1 63  TRP 63  59  59  TRP TRP B . n 
B 1 64  ASN 64  60  60  ASN ASN B . n 
B 1 65  GLU 65  61  61  GLU GLU B . n 
B 1 66  ASP 66  62  62  ASP ASP B . n 
B 1 67  THR 67  63  63  THR THR B . n 
B 1 68  LEU 68  64  64  LEU LEU B . n 
B 1 69  PHE 69  65  65  PHE PHE B . n 
B 1 70  GLU 70  66  66  GLU GLU B . n 
B 1 71  TYR 71  67  67  TYR TYR B . n 
B 1 72  LEU 72  68  68  LEU LEU B . n 
B 1 73  GLU 73  69  69  GLU GLU B . n 
B 1 74  ASN 74  70  70  ASN ASN B . n 
B 1 75  PRO 75  71  71  PRO PRO B . n 
B 1 76  LYS 76  72  72  LYS LYS B . n 
B 1 77  LYS 77  73  73  LYS LYS B . n 
B 1 78  TYR 78  74  74  TYR TYR B . n 
B 1 79  ILE 79  75  75  ILE ILE B . n 
B 1 80  PRO 80  76  76  PRO PRO B . n 
B 1 81  GLY 81  77  77  GLY GLY B . n 
B 1 82  THR 82  78  78  THR THR B . n 
B 1 83  LYS 83  79  79  LYS LYS B . n 
B 1 84  MET 84  80  80  MET MET B . n 
B 1 85  ILE 85  81  81  ILE ILE B . n 
B 1 86  PHE 86  82  82  PHE PHE B . n 
B 1 87  ALA 87  83  83  ALA ALA B . n 
B 1 88  GLY 88  84  84  GLY GLY B . n 
B 1 89  LEU 89  85  85  LEU LEU B . n 
B 1 90  LYS 90  86  86  LYS LYS B . n 
B 1 91  LYS 91  87  87  LYS LYS B . n 
B 1 92  PRO 92  88  88  PRO PRO B . n 
B 1 93  ASN 93  89  89  ASN ASN B . n 
B 1 94  GLU 94  90  90  GLU GLU B . n 
B 1 95  ARG 95  91  91  ARG ARG B . n 
B 1 96  GLY 96  92  92  GLY GLY B . n 
B 1 97  ASP 97  93  93  ASP ASP B . n 
B 1 98  LEU 98  94  94  LEU LEU B . n 
B 1 99  ILE 99  95  95  ILE ILE B . n 
B 1 100 ALA 100 96  96  ALA ALA B . n 
B 1 101 TYR 101 97  97  TYR TYR B . n 
B 1 102 LEU 102 98  98  LEU LEU B . n 
B 1 103 LYS 103 99  99  LYS LYS B . n 
B 1 104 SER 104 100 100 SER SER B . n 
B 1 105 ALA 105 101 101 ALA ALA B . n 
B 1 106 THR 106 102 102 THR THR B . n 
B 1 107 LYS 107 103 103 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEC 1   201 201 HEC HEC A . 
D 3 EOH 1   202 202 EOH EOH A . 
E 2 HEC 1   201 201 HEC HEC B . 
F 4 HOH 1   301 304 HOH HOH A . 
F 4 HOH 2   302 302 HOH HOH A . 
F 4 HOH 3   303 301 HOH HOH A . 
F 4 HOH 4   304 303 HOH HOH A . 
F 4 HOH 5   305 311 HOH HOH A . 
F 4 HOH 6   306 306 HOH HOH A . 
F 4 HOH 7   307 308 HOH HOH A . 
F 4 HOH 8   308 307 HOH HOH A . 
F 4 HOH 9   309 309 HOH HOH A . 
F 4 HOH 10  310 312 HOH HOH A . 
F 4 HOH 11  311 310 HOH HOH A . 
F 4 HOH 12  312 313 HOH HOH A . 
F 4 HOH 13  313 314 HOH HOH A . 
F 4 HOH 14  314 319 HOH HOH A . 
F 4 HOH 15  315 353 HOH HOH A . 
F 4 HOH 16  316 320 HOH HOH A . 
F 4 HOH 17  317 318 HOH HOH A . 
F 4 HOH 18  318 316 HOH HOH A . 
F 4 HOH 19  319 321 HOH HOH A . 
F 4 HOH 20  320 322 HOH HOH A . 
F 4 HOH 21  321 317 HOH HOH A . 
F 4 HOH 22  322 324 HOH HOH A . 
F 4 HOH 23  323 339 HOH HOH A . 
F 4 HOH 24  324 315 HOH HOH A . 
F 4 HOH 25  325 327 HOH HOH A . 
F 4 HOH 26  326 326 HOH HOH A . 
F 4 HOH 27  327 323 HOH HOH A . 
F 4 HOH 28  328 325 HOH HOH A . 
F 4 HOH 29  329 328 HOH HOH A . 
F 4 HOH 30  330 330 HOH HOH A . 
F 4 HOH 31  331 331 HOH HOH A . 
F 4 HOH 32  332 332 HOH HOH A . 
F 4 HOH 33  333 329 HOH HOH A . 
F 4 HOH 34  334 333 HOH HOH A . 
F 4 HOH 35  335 346 HOH HOH A . 
F 4 HOH 36  336 336 HOH HOH A . 
F 4 HOH 37  337 464 HOH HOH A . 
F 4 HOH 38  338 335 HOH HOH A . 
F 4 HOH 39  339 343 HOH HOH A . 
F 4 HOH 40  340 334 HOH HOH A . 
F 4 HOH 41  341 337 HOH HOH A . 
F 4 HOH 42  342 338 HOH HOH A . 
F 4 HOH 43  343 342 HOH HOH A . 
F 4 HOH 44  344 345 HOH HOH A . 
F 4 HOH 45  345 462 HOH HOH A . 
F 4 HOH 46  346 340 HOH HOH A . 
F 4 HOH 47  347 354 HOH HOH A . 
F 4 HOH 48  348 344 HOH HOH A . 
F 4 HOH 49  349 351 HOH HOH A . 
F 4 HOH 50  350 348 HOH HOH A . 
F 4 HOH 51  351 349 HOH HOH A . 
F 4 HOH 52  352 350 HOH HOH A . 
F 4 HOH 53  353 305 HOH HOH A . 
F 4 HOH 54  354 361 HOH HOH A . 
F 4 HOH 55  355 355 HOH HOH A . 
F 4 HOH 56  356 360 HOH HOH A . 
F 4 HOH 57  357 363 HOH HOH A . 
F 4 HOH 58  358 341 HOH HOH A . 
F 4 HOH 59  359 352 HOH HOH A . 
F 4 HOH 60  360 357 HOH HOH A . 
F 4 HOH 61  361 356 HOH HOH A . 
F 4 HOH 62  362 358 HOH HOH A . 
F 4 HOH 63  363 359 HOH HOH A . 
F 4 HOH 64  364 362 HOH HOH A . 
F 4 HOH 65  365 412 HOH HOH A . 
F 4 HOH 66  366 367 HOH HOH A . 
F 4 HOH 67  367 364 HOH HOH A . 
F 4 HOH 68  368 366 HOH HOH A . 
F 4 HOH 69  369 365 HOH HOH A . 
F 4 HOH 70  370 370 HOH HOH A . 
F 4 HOH 71  371 347 HOH HOH A . 
F 4 HOH 72  372 380 HOH HOH A . 
F 4 HOH 73  373 368 HOH HOH A . 
F 4 HOH 74  374 371 HOH HOH A . 
F 4 HOH 75  375 369 HOH HOH A . 
F 4 HOH 76  376 373 HOH HOH A . 
F 4 HOH 77  377 463 HOH HOH A . 
F 4 HOH 78  378 374 HOH HOH A . 
F 4 HOH 79  379 375 HOH HOH A . 
F 4 HOH 80  380 381 HOH HOH A . 
F 4 HOH 81  381 377 HOH HOH A . 
F 4 HOH 82  382 378 HOH HOH A . 
F 4 HOH 83  383 379 HOH HOH A . 
F 4 HOH 84  384 372 HOH HOH A . 
F 4 HOH 85  385 384 HOH HOH A . 
F 4 HOH 86  386 383 HOH HOH A . 
F 4 HOH 87  387 382 HOH HOH A . 
F 4 HOH 88  388 386 HOH HOH A . 
F 4 HOH 89  389 395 HOH HOH A . 
F 4 HOH 90  390 385 HOH HOH A . 
F 4 HOH 91  391 392 HOH HOH A . 
F 4 HOH 92  392 376 HOH HOH A . 
F 4 HOH 93  393 388 HOH HOH A . 
F 4 HOH 94  394 389 HOH HOH A . 
F 4 HOH 95  395 390 HOH HOH A . 
F 4 HOH 96  396 404 HOH HOH A . 
F 4 HOH 97  397 394 HOH HOH A . 
F 4 HOH 98  398 387 HOH HOH A . 
F 4 HOH 99  399 393 HOH HOH A . 
F 4 HOH 100 400 397 HOH HOH A . 
F 4 HOH 101 401 391 HOH HOH A . 
F 4 HOH 102 402 399 HOH HOH A . 
F 4 HOH 103 403 396 HOH HOH A . 
F 4 HOH 104 404 400 HOH HOH A . 
F 4 HOH 105 405 398 HOH HOH A . 
F 4 HOH 106 406 401 HOH HOH A . 
F 4 HOH 107 407 405 HOH HOH A . 
F 4 HOH 108 408 403 HOH HOH A . 
F 4 HOH 109 409 402 HOH HOH A . 
F 4 HOH 110 410 406 HOH HOH A . 
F 4 HOH 111 411 407 HOH HOH A . 
F 4 HOH 112 412 413 HOH HOH A . 
F 4 HOH 113 413 408 HOH HOH A . 
F 4 HOH 114 414 409 HOH HOH A . 
F 4 HOH 115 415 411 HOH HOH A . 
F 4 HOH 116 416 410 HOH HOH A . 
F 4 HOH 117 417 414 HOH HOH A . 
F 4 HOH 118 418 417 HOH HOH A . 
F 4 HOH 119 419 418 HOH HOH A . 
F 4 HOH 120 420 419 HOH HOH A . 
F 4 HOH 121 421 424 HOH HOH A . 
F 4 HOH 122 422 422 HOH HOH A . 
F 4 HOH 123 423 423 HOH HOH A . 
F 4 HOH 124 424 425 HOH HOH A . 
F 4 HOH 125 425 420 HOH HOH A . 
F 4 HOH 126 426 428 HOH HOH A . 
F 4 HOH 127 427 427 HOH HOH A . 
F 4 HOH 128 428 429 HOH HOH A . 
F 4 HOH 129 429 432 HOH HOH A . 
F 4 HOH 130 430 434 HOH HOH A . 
F 4 HOH 131 431 435 HOH HOH A . 
F 4 HOH 132 432 438 HOH HOH A . 
F 4 HOH 133 433 436 HOH HOH A . 
F 4 HOH 134 434 440 HOH HOH A . 
F 4 HOH 135 435 439 HOH HOH A . 
F 4 HOH 136 436 441 HOH HOH A . 
F 4 HOH 137 437 433 HOH HOH A . 
F 4 HOH 138 438 443 HOH HOH A . 
F 4 HOH 139 439 442 HOH HOH A . 
F 4 HOH 140 440 446 HOH HOH A . 
F 4 HOH 141 441 448 HOH HOH A . 
F 4 HOH 142 442 444 HOH HOH A . 
F 4 HOH 143 443 445 HOH HOH A . 
F 4 HOH 144 444 447 HOH HOH A . 
F 4 HOH 145 445 449 HOH HOH A . 
F 4 HOH 146 446 453 HOH HOH A . 
F 4 HOH 147 447 451 HOH HOH A . 
F 4 HOH 148 448 452 HOH HOH A . 
F 4 HOH 149 449 454 HOH HOH A . 
F 4 HOH 150 450 455 HOH HOH A . 
F 4 HOH 151 451 457 HOH HOH A . 
F 4 HOH 152 452 456 HOH HOH A . 
F 4 HOH 153 453 458 HOH HOH A . 
F 4 HOH 154 454 459 HOH HOH A . 
F 4 HOH 155 455 461 HOH HOH A . 
G 4 HOH 1   301 301 HOH HOH B . 
G 4 HOH 2   302 302 HOH HOH B . 
G 4 HOH 3   303 465 HOH HOH B . 
G 4 HOH 4   304 304 HOH HOH B . 
G 4 HOH 5   305 305 HOH HOH B . 
G 4 HOH 6   306 303 HOH HOH B . 
G 4 HOH 7   307 308 HOH HOH B . 
G 4 HOH 8   308 307 HOH HOH B . 
G 4 HOH 9   309 306 HOH HOH B . 
G 4 HOH 10  310 309 HOH HOH B . 
G 4 HOH 11  311 310 HOH HOH B . 
G 4 HOH 12  312 312 HOH HOH B . 
G 4 HOH 13  313 314 HOH HOH B . 
G 4 HOH 14  314 313 HOH HOH B . 
G 4 HOH 15  315 315 HOH HOH B . 
G 4 HOH 16  316 320 HOH HOH B . 
G 4 HOH 17  317 317 HOH HOH B . 
G 4 HOH 18  318 318 HOH HOH B . 
G 4 HOH 19  319 319 HOH HOH B . 
G 4 HOH 20  320 321 HOH HOH B . 
G 4 HOH 21  321 324 HOH HOH B . 
G 4 HOH 22  322 325 HOH HOH B . 
G 4 HOH 23  323 327 HOH HOH B . 
G 4 HOH 24  324 323 HOH HOH B . 
G 4 HOH 25  325 326 HOH HOH B . 
G 4 HOH 26  326 322 HOH HOH B . 
G 4 HOH 27  327 333 HOH HOH B . 
G 4 HOH 28  328 330 HOH HOH B . 
G 4 HOH 29  329 316 HOH HOH B . 
G 4 HOH 30  330 328 HOH HOH B . 
G 4 HOH 31  331 355 HOH HOH B . 
G 4 HOH 32  332 329 HOH HOH B . 
G 4 HOH 33  333 346 HOH HOH B . 
G 4 HOH 34  334 331 HOH HOH B . 
G 4 HOH 35  335 341 HOH HOH B . 
G 4 HOH 36  336 340 HOH HOH B . 
G 4 HOH 37  337 334 HOH HOH B . 
G 4 HOH 38  338 336 HOH HOH B . 
G 4 HOH 39  339 337 HOH HOH B . 
G 4 HOH 40  340 344 HOH HOH B . 
G 4 HOH 41  341 335 HOH HOH B . 
G 4 HOH 42  342 339 HOH HOH B . 
G 4 HOH 43  343 365 HOH HOH B . 
G 4 HOH 44  344 338 HOH HOH B . 
G 4 HOH 45  345 342 HOH HOH B . 
G 4 HOH 46  346 347 HOH HOH B . 
G 4 HOH 47  347 359 HOH HOH B . 
G 4 HOH 48  348 343 HOH HOH B . 
G 4 HOH 49  349 348 HOH HOH B . 
G 4 HOH 50  350 354 HOH HOH B . 
G 4 HOH 51  351 345 HOH HOH B . 
G 4 HOH 52  352 351 HOH HOH B . 
G 4 HOH 53  353 349 HOH HOH B . 
G 4 HOH 54  354 352 HOH HOH B . 
G 4 HOH 55  355 350 HOH HOH B . 
G 4 HOH 56  356 364 HOH HOH B . 
G 4 HOH 57  357 332 HOH HOH B . 
G 4 HOH 58  358 356 HOH HOH B . 
G 4 HOH 59  359 363 HOH HOH B . 
G 4 HOH 60  360 362 HOH HOH B . 
G 4 HOH 61  361 360 HOH HOH B . 
G 4 HOH 62  362 357 HOH HOH B . 
G 4 HOH 63  363 367 HOH HOH B . 
G 4 HOH 64  364 361 HOH HOH B . 
G 4 HOH 65  365 366 HOH HOH B . 
G 4 HOH 66  366 353 HOH HOH B . 
G 4 HOH 67  367 368 HOH HOH B . 
G 4 HOH 68  368 370 HOH HOH B . 
G 4 HOH 69  369 369 HOH HOH B . 
G 4 HOH 70  370 376 HOH HOH B . 
G 4 HOH 71  371 375 HOH HOH B . 
G 4 HOH 72  372 373 HOH HOH B . 
G 4 HOH 73  373 377 HOH HOH B . 
G 4 HOH 74  374 372 HOH HOH B . 
G 4 HOH 75  375 382 HOH HOH B . 
G 4 HOH 76  376 383 HOH HOH B . 
G 4 HOH 77  377 379 HOH HOH B . 
G 4 HOH 78  378 374 HOH HOH B . 
G 4 HOH 79  379 371 HOH HOH B . 
G 4 HOH 80  380 381 HOH HOH B . 
G 4 HOH 81  381 380 HOH HOH B . 
G 4 HOH 82  382 384 HOH HOH B . 
G 4 HOH 83  383 386 HOH HOH B . 
G 4 HOH 84  384 385 HOH HOH B . 
G 4 HOH 85  385 387 HOH HOH B . 
G 4 HOH 86  386 388 HOH HOH B . 
G 4 HOH 87  387 392 HOH HOH B . 
G 4 HOH 88  388 464 HOH HOH B . 
G 4 HOH 89  389 398 HOH HOH B . 
G 4 HOH 90  390 378 HOH HOH B . 
G 4 HOH 91  391 393 HOH HOH B . 
G 4 HOH 92  392 395 HOH HOH B . 
G 4 HOH 93  393 397 HOH HOH B . 
G 4 HOH 94  394 389 HOH HOH B . 
G 4 HOH 95  395 391 HOH HOH B . 
G 4 HOH 96  396 396 HOH HOH B . 
G 4 HOH 97  397 400 HOH HOH B . 
G 4 HOH 98  398 401 HOH HOH B . 
G 4 HOH 99  399 403 HOH HOH B . 
G 4 HOH 100 400 405 HOH HOH B . 
G 4 HOH 101 401 406 HOH HOH B . 
G 4 HOH 102 402 402 HOH HOH B . 
G 4 HOH 103 403 408 HOH HOH B . 
G 4 HOH 104 404 409 HOH HOH B . 
G 4 HOH 105 405 399 HOH HOH B . 
G 4 HOH 106 406 404 HOH HOH B . 
G 4 HOH 107 407 463 HOH HOH B . 
G 4 HOH 108 408 358 HOH HOH B . 
G 4 HOH 109 409 412 HOH HOH B . 
G 4 HOH 110 410 417 HOH HOH B . 
G 4 HOH 111 411 415 HOH HOH B . 
G 4 HOH 112 412 418 HOH HOH B . 
G 4 HOH 113 413 420 HOH HOH B . 
G 4 HOH 114 414 421 HOH HOH B . 
G 4 HOH 115 415 422 HOH HOH B . 
G 4 HOH 116 416 466 HOH HOH B . 
G 4 HOH 117 417 424 HOH HOH B . 
G 4 HOH 118 418 427 HOH HOH B . 
G 4 HOH 119 419 430 HOH HOH B . 
G 4 HOH 120 420 433 HOH HOH B . 
G 4 HOH 121 421 432 HOH HOH B . 
G 4 HOH 122 422 434 HOH HOH B . 
G 4 HOH 123 423 431 HOH HOH B . 
G 4 HOH 124 424 429 HOH HOH B . 
G 4 HOH 125 425 441 HOH HOH B . 
G 4 HOH 126 426 436 HOH HOH B . 
G 4 HOH 127 427 435 HOH HOH B . 
G 4 HOH 128 428 419 HOH HOH B . 
G 4 HOH 129 429 442 HOH HOH B . 
G 4 HOH 130 430 439 HOH HOH B . 
G 4 HOH 131 431 438 HOH HOH B . 
G 4 HOH 132 432 437 HOH HOH B . 
G 4 HOH 133 433 443 HOH HOH B . 
G 4 HOH 134 434 444 HOH HOH B . 
G 4 HOH 135 435 447 HOH HOH B . 
G 4 HOH 136 436 428 HOH HOH B . 
G 4 HOH 137 437 445 HOH HOH B . 
G 4 HOH 138 438 446 HOH HOH B . 
G 4 HOH 139 439 450 HOH HOH B . 
G 4 HOH 140 440 448 HOH HOH B . 
G 4 HOH 141 441 451 HOH HOH B . 
G 4 HOH 142 442 453 HOH HOH B . 
G 4 HOH 143 443 454 HOH HOH B . 
G 4 HOH 144 444 456 HOH HOH B . 
G 4 HOH 145 445 457 HOH HOH B . 
G 4 HOH 146 446 455 HOH HOH B . 
G 4 HOH 147 447 458 HOH HOH B . 
G 4 HOH 148 448 459 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? dev_3150 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? dev_3150 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DENZO     ? ? ? .        3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .        4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.772 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MT0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     33.876 
_cell.length_a_esd                 ? 
_cell.length_b                     58.634 
_cell.length_b_esd                 ? 
_cell.length_c                     51.674 
_cell.length_c_esd                 ? 
_cell.volume                       98273.099 
_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                         9MT0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MT0 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.63 
_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              9.7 
_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    
;Concentrated protein in 0.5 mM EDTA, 20 mM Tris-HCL pH 7.5 was mixed with an equal volume of precipitant containing  0.1 M Glycine pH 10.0 and 28% w/v Polyethylene Glycol Monomethyl Ether 2000 and allowed to vapor diffuse against a reservoir of the same precipitant. Before cryoprotection and freezing, the crystal was transferred to a well containing 0.1 M CAPS pH 11.0 and 28% w/v Polyethylene Glycol Monomethyl Ether 2000. The crystal fractured, and a fragment was ued for collection.
;
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 270' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-03-07 
_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   0.9804 
_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                        'CHESS BEAMLINE F1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9804 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   F1 
_diffrn_source.pdbx_synchrotron_site       CHESS 
# 
_reflns.B_iso_Wilson_estimate                          13.85 
_reflns.entry_id                                       9MT0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.20 
_reflns.d_resolution_low                               38.00 
_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                                     55990 
_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                     -3 
_reflns.percent_possible_obs                           91.83 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.36 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.097 
_reflns.pdbx_Rpim_I_all                                0.040 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.088 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.20 1.24 ? 1.6  ? ? ? ? 2478 ? ? ? ? ? ? ? ? ? ? ? 2.41 ? ? ? 0.534 0.264 ? 1  1 0.779 ? ? 45.23 ? 0.459 ? ? ? ? ? ? ? ? ? 
1.24 1.28 ? 2.2  ? ? ? ? 4514 ? ? ? ? ? ? ? ? ? ? ? 2.95 ? ? ? 0.461 0.225 ? 2  1 0.852 ? ? 81.20 ? 0.398 ? ? ? ? ? ? ? ? ? 
1.28 1.33 ? 3.1  ? ? ? ? 5302 ? ? ? ? ? ? ? ? ? ? ? 4.26 ? ? ? 0.429 0.194 ? 3  1 0.898 ? ? 96.33 ? 0.380 ? ? ? ? ? ? ? ? ? 
1.33 1.40 ? 4.5  ? ? ? ? 5406 ? ? ? ? ? ? ? ? ? ? ? 5.25 ? ? ? 0.352 0.148 ? 4  1 0.941 ? ? 97.78 ? 0.318 ? ? ? ? ? ? ? ? ? 
1.40 1.47 ? 6.6  ? ? ? ? 5456 ? ? ? ? ? ? ? ? ? ? ? 5.76 ? ? ? 0.253 0.104 ? 5  1 0.965 ? ? 98.02 ? 0.230 ? ? ? ? ? ? ? ? ? 
1.47 1.56 ? 8.9  ? ? ? ? 5424 ? ? ? ? ? ? ? ? ? ? ? 5.95 ? ? ? 0.182 0.074 ? 6  1 0.980 ? ? 98.62 ? 0.166 ? ? ? ? ? ? ? ? ? 
1.56 1.68 ? 11.6 ? ? ? ? 5469 ? ? ? ? ? ? ? ? ? ? ? 5.99 ? ? ? 0.130 0.052 ? 7  1 0.989 ? ? 99.06 ? 0.119 ? ? ? ? ? ? ? ? ? 
1.68 1.85 ? 14.2 ? ? ? ? 5514 ? ? ? ? ? ? ? ? ? ? ? 6.14 ? ? ? 0.102 0.040 ? 8  1 0.992 ? ? 99.26 ? 0.093 ? ? ? ? ? ? ? ? ? 
1.85 2.12 ? 16.9 ? ? ? ? 5536 ? ? ? ? ? ? ? ? ? ? ? 6.15 ? ? ? 0.085 0.034 ? 9  1 0.993 ? ? 99.60 ? 0.078 ? ? ? ? ? ? ? ? ? 
2.12 2.67 ? 19.0 ? ? ? ? 5545 ? ? ? ? ? ? ? ? ? ? ? 6.22 ? ? ? 0.083 0.033 ? 10 1 0.992 ? ? 99.73 ? 0.076 ? ? ? ? ? ? ? ? ? 
2.67 38.0 ? 18.9 ? ? ? ? 5346 ? ? ? ? ? ? ? ? ? ? ? 5.75 ? ? ? 0.089 0.037 ? 11 1 0.988 ? ? 94.75 ? 0.081 ? ? ? ? ? ? ? ? ? 
# 
_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                               21.76 
_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                                 9MT0 
_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                            1.20 
_refine.ls_d_res_low                             37.81 
_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                     55798 
_refine.ls_number_reflns_R_free                  1574 
_refine.ls_number_reflns_R_work                  54224 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.28 
_refine.ls_percent_reflns_R_free                 2.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1273 
_refine.ls_R_factor_R_free                       0.1650 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1262 
_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                          0.93 
_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       'CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.3377 
_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                            0.1264 
_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                       1.20 
_refine_hist.d_res_low                        37.81 
_refine_hist.number_atoms_solvent             303 
_refine_hist.number_atoms_total               2034 
_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        1642 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         89 
_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' ? 0.0086  ? 1907 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1051  ? 2604 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0738  ? 253  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0128  ? 333  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.7568 ? 710  ? 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' 1.20 1.24 . . 70  2581 48.48 . . . . 0.2793 . . . . . . . . . . . 0.3019 
'X-RAY DIFFRACTION' 1.24 1.28 . . 119 4450 83.67 . . . . 0.2286 . . . . . . . . . . . 0.2830 
'X-RAY DIFFRACTION' 1.28 1.33 . . 159 5120 96.26 . . . . 0.2062 . . . . . . . . . . . 0.2249 
'X-RAY DIFFRACTION' 1.33 1.40 . . 148 5220 97.69 . . . . 0.1771 . . . . . . . . . . . 0.2301 
'X-RAY DIFFRACTION' 1.40 1.47 . . 148 5230 97.87 . . . . 0.1283 . . . . . . . . . . . 0.2051 
'X-RAY DIFFRACTION' 1.47 1.56 . . 151 5198 98.54 . . . . 0.1132 . . . . . . . . . . . 0.1498 
'X-RAY DIFFRACTION' 1.56 1.68 . . 161 5304 99.00 . . . . 0.1049 . . . . . . . . . . . 0.1420 
'X-RAY DIFFRACTION' 1.68 1.85 . . 151 5287 99.23 . . . . 0.1030 . . . . . . . . . . . 0.1572 
'X-RAY DIFFRACTION' 1.85 2.12 . . 156 5354 99.58 . . . . 0.1110 . . . . . . . . . . . 0.1607 
'X-RAY DIFFRACTION' 2.12 2.67 . . 157 5331 99.76 . . . . 0.1191 . . . . . . . . . . . 0.1564 
'X-RAY DIFFRACTION' 2.67 37.8 . . 154 5149 94.68 . . . . 0.1275 . . . . . . . . . . . 0.1537 
# 
_struct.entry_id                     9MT0 
_struct.title                        '1.2 A Crystal Structure of Housefly cytochrome c at pH 11' 
_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        9MT0 
_struct_keywords.text            'Electron transport, metalloproteins, Insect, Protostome, cytochrome c, Alkaline pH' 
_struct_keywords.pdbx_keywords   'ELECTRON TRANSPORT' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1I8N8V4_MUSDO 
_struct_ref.pdbx_db_accession          A0A1I8N8V4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GVPAGDVEKGKKIFVQRCAQCHTVEAGGKHKVGPNLHGLFGRKTGQAAGFAYTDANKAKGITWNEDTLFEYLENPKKYIP
GTKMIFAGLKKPNERGDLIAYLKSATK
;
_struct_ref.pdbx_align_begin           2 
# 
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 9MT0 A 1 ? 107 ? A0A1I8N8V4 2 ? 108 ? -3 103 
2 1 9MT0 B 1 ? 107 ? A0A1I8N8V4 2 ? 108 ? -3 103 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,F 
2 1 B,E,G   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 ASP A 6  ? CYS A 18  ? ASP A 2  CYS A 14  1 ? 13 
HELX_P HELX_P2  AA2 THR A 53 ? GLY A 60  ? THR A 49 GLY A 56  1 ? 8  
HELX_P HELX_P3  AA3 ASN A 64 ? ASN A 74  ? ASN A 60 ASN A 70  1 ? 11 
HELX_P HELX_P4  AA4 ASN A 74 ? ILE A 79  ? ASN A 70 ILE A 75  1 ? 6  
HELX_P HELX_P5  AA5 LYS A 91 ? THR A 106 ? LYS A 87 THR A 102 1 ? 16 
HELX_P HELX_P6  AA6 ASP B 6  ? CYS B 18  ? ASP B 2  CYS B 14  1 ? 13 
HELX_P HELX_P7  AA7 THR B 53 ? GLY B 60  ? THR B 49 GLY B 56  1 ? 8  
HELX_P HELX_P8  AA8 ASN B 64 ? ASN B 74  ? ASN B 60 ASN B 70  1 ? 11 
HELX_P HELX_P9  AA9 ASN B 74 ? ILE B 79  ? ASN B 70 ILE B 75  1 ? 6  
HELX_P HELX_P10 AB1 LYS B 91 ? THR B 106 ? LYS B 87 THR B 102 1 ? 16 
# 
_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 
covale1 covale none ? A CYS 18 SG  ? ? ? 1_555 C HEC . CAB ? ? A CYS 14 A HEC 201 1_555 ? ? ? ? ? ? ? 1.759 ? ? 
covale2 covale none ? A CYS 21 SG  ? ? ? 1_555 C HEC . CAC ? ? A CYS 17 A HEC 201 1_555 ? ? ? ? ? ? ? 1.808 ? ? 
covale3 covale none ? B CYS 18 SG  ? ? ? 1_555 E HEC . CAB ? ? B CYS 14 B HEC 201 1_555 ? ? ? ? ? ? ? 1.755 ? ? 
covale4 covale none ? B CYS 21 SG  ? ? ? 1_555 E HEC . CAC ? ? B CYS 17 B HEC 201 1_555 ? ? ? ? ? ? ? 1.867 ? ? 
metalc1 metalc ?    ? A HIS 22 NE2 ? ? ? 1_555 C HEC . FE  ? ? A HIS 18 A HEC 201 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc2 metalc ?    ? A MET 84 SD  ? ? ? 1_555 C HEC . FE  ? ? A MET 80 A HEC 201 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc3 metalc ?    ? B HIS 22 NE2 ? ? ? 1_555 E HEC . FE  ? ? B HIS 18 B HEC 201 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc4 metalc ?    ? B MET 84 SD  ? ? ? 1_555 E HEC . FE  ? ? B MET 80 B HEC 201 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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  NE2 ? A HIS 22 ? A HIS 18  ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 NA ? C HEC .  ? A HEC 201 ? 1_555 90.1  ? 
2  NE2 ? A HIS 22 ? A HIS 18  ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 NB ? C HEC .  ? A HEC 201 ? 1_555 89.0  ? 
3  NA  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 NB ? C HEC .  ? A HEC 201 ? 1_555 92.0  ? 
4  NE2 ? A HIS 22 ? A HIS 18  ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 NC ? C HEC .  ? A HEC 201 ? 1_555 91.1  ? 
5  NA  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 NC ? C HEC .  ? A HEC 201 ? 1_555 178.8 ? 
6  NB  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 NC ? C HEC .  ? A HEC 201 ? 1_555 88.1  ? 
7  NE2 ? A HIS 22 ? A HIS 18  ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 ND ? C HEC .  ? A HEC 201 ? 1_555 91.2  ? 
8  NA  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 ND ? C HEC .  ? A HEC 201 ? 1_555 87.6  ? 
9  NB  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 ND ? C HEC .  ? A HEC 201 ? 1_555 179.6 ? 
10 NC  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 ND ? C HEC .  ? A HEC 201 ? 1_555 92.2  ? 
11 NE2 ? A HIS 22 ? A HIS 18  ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 SD ? A MET 84 ? A MET 80  ? 1_555 173.6 ? 
12 NA  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 SD ? A MET 84 ? A MET 80  ? 1_555 83.5  ? 
13 NB  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 SD ? A MET 84 ? A MET 80  ? 1_555 91.0  ? 
14 NC  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 SD ? A MET 84 ? A MET 80  ? 1_555 95.3  ? 
15 ND  ? C HEC .  ? A HEC 201 ? 1_555 FE ? C HEC . ? A HEC 201 ? 1_555 SD ? A MET 84 ? A MET 80  ? 1_555 88.7  ? 
16 NE2 ? B HIS 22 ? B HIS 18  ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 NA ? E HEC .  ? B HEC 201 ? 1_555 91.3  ? 
17 NE2 ? B HIS 22 ? B HIS 18  ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 NB ? E HEC .  ? B HEC 201 ? 1_555 86.3  ? 
18 NA  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 NB ? E HEC .  ? B HEC 201 ? 1_555 89.6  ? 
19 NE2 ? B HIS 22 ? B HIS 18  ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 NC ? E HEC .  ? B HEC 201 ? 1_555 91.6  ? 
20 NA  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 NC ? E HEC .  ? B HEC 201 ? 1_555 177.1 ? 
21 NB  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 NC ? E HEC .  ? B HEC 201 ? 1_555 90.3  ? 
22 NE2 ? B HIS 22 ? B HIS 18  ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 ND ? E HEC .  ? B HEC 201 ? 1_555 91.3  ? 
23 NA  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 ND ? E HEC .  ? B HEC 201 ? 1_555 89.7  ? 
24 NB  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 ND ? E HEC .  ? B HEC 201 ? 1_555 177.5 ? 
25 NC  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 ND ? E HEC .  ? B HEC 201 ? 1_555 90.5  ? 
26 NE2 ? B HIS 22 ? B HIS 18  ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 SD ? B MET 84 ? B MET 80  ? 1_555 176.6 ? 
27 NA  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 SD ? B MET 84 ? B MET 80  ? 1_555 85.4  ? 
28 NB  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 SD ? B MET 84 ? B MET 80  ? 1_555 94.5  ? 
29 NC  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 SD ? B MET 84 ? B MET 80  ? 1_555 91.7  ? 
30 ND  ? E HEC .  ? B HEC 201 ? 1_555 FE ? E HEC . ? B HEC 201 ? 1_555 SD ? B MET 84 ? B MET 80  ? 1_555 87.8  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 HEC C . ? CYS A 18 ? HEC A 201 ? 1_555 CYS A 14 ? 1_555 CAB SG CYS 2 HEC None Heme/heme-like 
2 HEC C . ? CYS A 21 ? HEC A 201 ? 1_555 CYS A 17 ? 1_555 CAC SG CYS 3 HEC None Heme/heme-like 
3 HEC E . ? CYS B 18 ? HEC B 201 ? 1_555 CYS B 14 ? 1_555 CAB SG CYS 2 HEC None Heme/heme-like 
4 HEC E . ? CYS B 21 ? HEC B 201 ? 1_555 CYS B 17 ? 1_555 CAC SG CYS 3 HEC None Heme/heme-like 
# 
_pdbx_entry_details.entry_id                   9MT0 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 356 ? ? O A HOH 424 ? ? 2.09 
2 1 O B LYS 103 ? ? O B HOH 301 ? ? 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 27 ? ? -125.43 -139.74 
2 1 ASN A 70 ? ? -165.37 86.90   
3 1 LYS B 27 ? ? -123.03 -135.12 
4 1 ASN B 70 ? ? -159.54 84.50   
5 1 ASN B 70 ? ? -166.24 84.50   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       448 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.84 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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  
EOH C1   C  N N 88  
EOH C2   C  N N 89  
EOH O    O  N N 90  
EOH H11  H  N N 91  
EOH H12  H  N N 92  
EOH H21  H  N N 93  
EOH H22  H  N N 94  
EOH H23  H  N N 95  
EOH HO   H  N N 96  
GLN N    N  N N 97  
GLN CA   C  N S 98  
GLN C    C  N N 99  
GLN O    O  N N 100 
GLN CB   C  N N 101 
GLN CG   C  N N 102 
GLN CD   C  N N 103 
GLN OE1  O  N N 104 
GLN NE2  N  N N 105 
GLN OXT  O  N N 106 
GLN H    H  N N 107 
GLN H2   H  N N 108 
GLN HA   H  N N 109 
GLN HB2  H  N N 110 
GLN HB3  H  N N 111 
GLN HG2  H  N N 112 
GLN HG3  H  N N 113 
GLN HE21 H  N N 114 
GLN HE22 H  N N 115 
GLN HXT  H  N N 116 
GLU N    N  N N 117 
GLU CA   C  N S 118 
GLU C    C  N N 119 
GLU O    O  N N 120 
GLU CB   C  N N 121 
GLU CG   C  N N 122 
GLU CD   C  N N 123 
GLU OE1  O  N N 124 
GLU OE2  O  N N 125 
GLU OXT  O  N N 126 
GLU H    H  N N 127 
GLU H2   H  N N 128 
GLU HA   H  N N 129 
GLU HB2  H  N N 130 
GLU HB3  H  N N 131 
GLU HG2  H  N N 132 
GLU HG3  H  N N 133 
GLU HE2  H  N N 134 
GLU HXT  H  N N 135 
GLY N    N  N N 136 
GLY CA   C  N N 137 
GLY C    C  N N 138 
GLY O    O  N N 139 
GLY OXT  O  N N 140 
GLY H    H  N N 141 
GLY H2   H  N N 142 
GLY HA2  H  N N 143 
GLY HA3  H  N N 144 
GLY HXT  H  N N 145 
HEC FE   FE N N 146 
HEC CHA  C  N N 147 
HEC CHB  C  N N 148 
HEC CHC  C  N N 149 
HEC CHD  C  N N 150 
HEC NA   N  Y N 151 
HEC C1A  C  Y N 152 
HEC C2A  C  Y N 153 
HEC C3A  C  Y N 154 
HEC C4A  C  Y N 155 
HEC CMA  C  N N 156 
HEC CAA  C  N N 157 
HEC CBA  C  N N 158 
HEC CGA  C  N N 159 
HEC O1A  O  N N 160 
HEC O2A  O  N N 161 
HEC NB   N  Y N 162 
HEC C1B  C  Y N 163 
HEC C2B  C  Y N 164 
HEC C3B  C  Y N 165 
HEC C4B  C  Y N 166 
HEC CMB  C  N N 167 
HEC CAB  C  N N 168 
HEC CBB  C  N N 169 
HEC NC   N  Y N 170 
HEC C1C  C  Y N 171 
HEC C2C  C  Y N 172 
HEC C3C  C  Y N 173 
HEC C4C  C  Y N 174 
HEC CMC  C  N N 175 
HEC CAC  C  N N 176 
HEC CBC  C  N N 177 
HEC ND   N  Y N 178 
HEC C1D  C  Y N 179 
HEC C2D  C  Y N 180 
HEC C3D  C  Y N 181 
HEC C4D  C  Y N 182 
HEC CMD  C  N N 183 
HEC CAD  C  N N 184 
HEC CBD  C  N N 185 
HEC CGD  C  N N 186 
HEC O1D  O  N N 187 
HEC O2D  O  N N 188 
HEC HHA  H  N N 189 
HEC HHB  H  N N 190 
HEC HHC  H  N N 191 
HEC HHD  H  N N 192 
HEC HMA1 H  N N 193 
HEC HMA2 H  N N 194 
HEC HMA3 H  N N 195 
HEC HAA1 H  N N 196 
HEC HAA2 H  N N 197 
HEC HBA1 H  N N 198 
HEC HBA2 H  N N 199 
HEC H2A  H  N N 200 
HEC HMB1 H  N N 201 
HEC HMB2 H  N N 202 
HEC HMB3 H  N N 203 
HEC HAB  H  N N 204 
HEC HBB1 H  N N 205 
HEC HBB2 H  N N 206 
HEC HBB3 H  N N 207 
HEC HMC1 H  N N 208 
HEC HMC2 H  N N 209 
HEC HMC3 H  N N 210 
HEC HAC  H  N N 211 
HEC HBC1 H  N N 212 
HEC HBC2 H  N N 213 
HEC HBC3 H  N N 214 
HEC HMD1 H  N N 215 
HEC HMD2 H  N N 216 
HEC HMD3 H  N N 217 
HEC HAD1 H  N N 218 
HEC HAD2 H  N N 219 
HEC HBD1 H  N N 220 
HEC HBD2 H  N N 221 
HEC H2D  H  N N 222 
HIS N    N  N N 223 
HIS CA   C  N S 224 
HIS C    C  N N 225 
HIS O    O  N N 226 
HIS CB   C  N N 227 
HIS CG   C  Y N 228 
HIS ND1  N  Y N 229 
HIS CD2  C  Y N 230 
HIS CE1  C  Y N 231 
HIS NE2  N  Y N 232 
HIS OXT  O  N N 233 
HIS H    H  N N 234 
HIS H2   H  N N 235 
HIS HA   H  N N 236 
HIS HB2  H  N N 237 
HIS HB3  H  N N 238 
HIS HD1  H  N N 239 
HIS HD2  H  N N 240 
HIS HE1  H  N N 241 
HIS HE2  H  N N 242 
HIS HXT  H  N N 243 
HOH O    O  N N 244 
HOH H1   H  N N 245 
HOH H2   H  N N 246 
ILE N    N  N N 247 
ILE CA   C  N S 248 
ILE C    C  N N 249 
ILE O    O  N N 250 
ILE CB   C  N S 251 
ILE CG1  C  N N 252 
ILE CG2  C  N N 253 
ILE CD1  C  N N 254 
ILE OXT  O  N N 255 
ILE H    H  N N 256 
ILE H2   H  N N 257 
ILE HA   H  N N 258 
ILE HB   H  N N 259 
ILE HG12 H  N N 260 
ILE HG13 H  N N 261 
ILE HG21 H  N N 262 
ILE HG22 H  N N 263 
ILE HG23 H  N N 264 
ILE HD11 H  N N 265 
ILE HD12 H  N N 266 
ILE HD13 H  N N 267 
ILE HXT  H  N N 268 
LEU N    N  N N 269 
LEU CA   C  N S 270 
LEU C    C  N N 271 
LEU O    O  N N 272 
LEU CB   C  N N 273 
LEU CG   C  N N 274 
LEU CD1  C  N N 275 
LEU CD2  C  N N 276 
LEU OXT  O  N N 277 
LEU H    H  N N 278 
LEU H2   H  N N 279 
LEU HA   H  N N 280 
LEU HB2  H  N N 281 
LEU HB3  H  N N 282 
LEU HG   H  N N 283 
LEU HD11 H  N N 284 
LEU HD12 H  N N 285 
LEU HD13 H  N N 286 
LEU HD21 H  N N 287 
LEU HD22 H  N N 288 
LEU HD23 H  N N 289 
LEU HXT  H  N N 290 
LYS N    N  N N 291 
LYS CA   C  N S 292 
LYS C    C  N N 293 
LYS O    O  N N 294 
LYS CB   C  N N 295 
LYS CG   C  N N 296 
LYS CD   C  N N 297 
LYS CE   C  N N 298 
LYS NZ   N  N N 299 
LYS OXT  O  N N 300 
LYS H    H  N N 301 
LYS H2   H  N N 302 
LYS HA   H  N N 303 
LYS HB2  H  N N 304 
LYS HB3  H  N N 305 
LYS HG2  H  N N 306 
LYS HG3  H  N N 307 
LYS HD2  H  N N 308 
LYS HD3  H  N N 309 
LYS HE2  H  N N 310 
LYS HE3  H  N N 311 
LYS HZ1  H  N N 312 
LYS HZ2  H  N N 313 
LYS HZ3  H  N N 314 
LYS HXT  H  N N 315 
MET N    N  N N 316 
MET CA   C  N S 317 
MET C    C  N N 318 
MET O    O  N N 319 
MET CB   C  N N 320 
MET CG   C  N N 321 
MET SD   S  N N 322 
MET CE   C  N N 323 
MET OXT  O  N N 324 
MET H    H  N N 325 
MET H2   H  N N 326 
MET HA   H  N N 327 
MET HB2  H  N N 328 
MET HB3  H  N N 329 
MET HG2  H  N N 330 
MET HG3  H  N N 331 
MET HE1  H  N N 332 
MET HE2  H  N N 333 
MET HE3  H  N N 334 
MET HXT  H  N N 335 
PHE N    N  N N 336 
PHE CA   C  N S 337 
PHE C    C  N N 338 
PHE O    O  N N 339 
PHE CB   C  N N 340 
PHE CG   C  Y N 341 
PHE CD1  C  Y N 342 
PHE CD2  C  Y N 343 
PHE CE1  C  Y N 344 
PHE CE2  C  Y N 345 
PHE CZ   C  Y N 346 
PHE OXT  O  N N 347 
PHE H    H  N N 348 
PHE H2   H  N N 349 
PHE HA   H  N N 350 
PHE HB2  H  N N 351 
PHE HB3  H  N N 352 
PHE HD1  H  N N 353 
PHE HD2  H  N N 354 
PHE HE1  H  N N 355 
PHE HE2  H  N N 356 
PHE HZ   H  N N 357 
PHE HXT  H  N N 358 
PRO N    N  N N 359 
PRO CA   C  N S 360 
PRO C    C  N N 361 
PRO O    O  N N 362 
PRO CB   C  N N 363 
PRO CG   C  N N 364 
PRO CD   C  N N 365 
PRO OXT  O  N N 366 
PRO H    H  N N 367 
PRO HA   H  N N 368 
PRO HB2  H  N N 369 
PRO HB3  H  N N 370 
PRO HG2  H  N N 371 
PRO HG3  H  N N 372 
PRO HD2  H  N N 373 
PRO HD3  H  N N 374 
PRO HXT  H  N N 375 
SER N    N  N N 376 
SER CA   C  N S 377 
SER C    C  N N 378 
SER O    O  N N 379 
SER CB   C  N N 380 
SER OG   O  N N 381 
SER OXT  O  N N 382 
SER H    H  N N 383 
SER H2   H  N N 384 
SER HA   H  N N 385 
SER HB2  H  N N 386 
SER HB3  H  N N 387 
SER HG   H  N N 388 
SER HXT  H  N N 389 
THR N    N  N N 390 
THR CA   C  N S 391 
THR C    C  N N 392 
THR O    O  N N 393 
THR CB   C  N R 394 
THR OG1  O  N N 395 
THR CG2  C  N N 396 
THR OXT  O  N N 397 
THR H    H  N N 398 
THR H2   H  N N 399 
THR HA   H  N N 400 
THR HB   H  N N 401 
THR HG1  H  N N 402 
THR HG21 H  N N 403 
THR HG22 H  N N 404 
THR HG23 H  N N 405 
THR HXT  H  N N 406 
TRP N    N  N N 407 
TRP CA   C  N S 408 
TRP C    C  N N 409 
TRP O    O  N N 410 
TRP CB   C  N N 411 
TRP CG   C  Y N 412 
TRP CD1  C  Y N 413 
TRP CD2  C  Y N 414 
TRP NE1  N  Y N 415 
TRP CE2  C  Y N 416 
TRP CE3  C  Y N 417 
TRP CZ2  C  Y N 418 
TRP CZ3  C  Y N 419 
TRP CH2  C  Y N 420 
TRP OXT  O  N N 421 
TRP H    H  N N 422 
TRP H2   H  N N 423 
TRP HA   H  N N 424 
TRP HB2  H  N N 425 
TRP HB3  H  N N 426 
TRP HD1  H  N N 427 
TRP HE1  H  N N 428 
TRP HE3  H  N N 429 
TRP HZ2  H  N N 430 
TRP HZ3  H  N N 431 
TRP HH2  H  N N 432 
TRP HXT  H  N N 433 
TYR N    N  N N 434 
TYR CA   C  N S 435 
TYR C    C  N N 436 
TYR O    O  N N 437 
TYR CB   C  N N 438 
TYR CG   C  Y N 439 
TYR CD1  C  Y N 440 
TYR CD2  C  Y N 441 
TYR CE1  C  Y N 442 
TYR CE2  C  Y N 443 
TYR CZ   C  Y N 444 
TYR OH   O  N N 445 
TYR OXT  O  N N 446 
TYR H    H  N N 447 
TYR H2   H  N N 448 
TYR HA   H  N N 449 
TYR HB2  H  N N 450 
TYR HB3  H  N N 451 
TYR HD1  H  N N 452 
TYR HD2  H  N N 453 
TYR HE1  H  N N 454 
TYR HE2  H  N N 455 
TYR HH   H  N N 456 
TYR HXT  H  N N 457 
VAL N    N  N N 458 
VAL CA   C  N S 459 
VAL C    C  N N 460 
VAL O    O  N N 461 
VAL CB   C  N N 462 
VAL CG1  C  N N 463 
VAL CG2  C  N N 464 
VAL OXT  O  N N 465 
VAL H    H  N N 466 
VAL H2   H  N N 467 
VAL HA   H  N N 468 
VAL HB   H  N N 469 
VAL HG11 H  N N 470 
VAL HG12 H  N N 471 
VAL HG13 H  N N 472 
VAL HG21 H  N N 473 
VAL HG22 H  N N 474 
VAL HG23 H  N N 475 
VAL HXT  H  N N 476 
# 
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  
EOH C1  C2   sing N N 83  
EOH C1  O    sing N N 84  
EOH C1  H11  sing N N 85  
EOH C1  H12  sing N N 86  
EOH C2  H21  sing N N 87  
EOH C2  H22  sing N N 88  
EOH C2  H23  sing N N 89  
EOH O   HO   sing N N 90  
GLN N   CA   sing N N 91  
GLN N   H    sing N N 92  
GLN N   H2   sing N N 93  
GLN CA  C    sing N N 94  
GLN CA  CB   sing N N 95  
GLN CA  HA   sing N N 96  
GLN C   O    doub N N 97  
GLN C   OXT  sing N N 98  
GLN CB  CG   sing N N 99  
GLN CB  HB2  sing N N 100 
GLN CB  HB3  sing N N 101 
GLN CG  CD   sing N N 102 
GLN CG  HG2  sing N N 103 
GLN CG  HG3  sing N N 104 
GLN CD  OE1  doub N N 105 
GLN CD  NE2  sing N N 106 
GLN NE2 HE21 sing N N 107 
GLN NE2 HE22 sing N N 108 
GLN OXT HXT  sing N N 109 
GLU N   CA   sing N N 110 
GLU N   H    sing N N 111 
GLU N   H2   sing N N 112 
GLU CA  C    sing N N 113 
GLU CA  CB   sing N N 114 
GLU CA  HA   sing N N 115 
GLU C   O    doub N N 116 
GLU C   OXT  sing N N 117 
GLU CB  CG   sing N N 118 
GLU CB  HB2  sing N N 119 
GLU CB  HB3  sing N N 120 
GLU CG  CD   sing N N 121 
GLU CG  HG2  sing N N 122 
GLU CG  HG3  sing N N 123 
GLU CD  OE1  doub N N 124 
GLU CD  OE2  sing N N 125 
GLU OE2 HE2  sing N N 126 
GLU OXT HXT  sing N N 127 
GLY N   CA   sing N N 128 
GLY N   H    sing N N 129 
GLY N   H2   sing N N 130 
GLY CA  C    sing N N 131 
GLY CA  HA2  sing N N 132 
GLY CA  HA3  sing N N 133 
GLY C   O    doub N N 134 
GLY C   OXT  sing N N 135 
GLY OXT HXT  sing N N 136 
HEC FE  NA   sing N N 137 
HEC FE  NB   sing N N 138 
HEC FE  NC   sing N N 139 
HEC FE  ND   sing N N 140 
HEC CHA C1A  doub N N 141 
HEC CHA C4D  sing N N 142 
HEC CHA HHA  sing N N 143 
HEC CHB C4A  doub N N 144 
HEC CHB C1B  sing N N 145 
HEC CHB HHB  sing N N 146 
HEC CHC C4B  doub N N 147 
HEC CHC C1C  sing N N 148 
HEC CHC HHC  sing N N 149 
HEC CHD C4C  doub N N 150 
HEC CHD C1D  sing N N 151 
HEC CHD HHD  sing N N 152 
HEC NA  C1A  sing Y N 153 
HEC NA  C4A  sing Y N 154 
HEC C1A C2A  sing Y N 155 
HEC C2A C3A  doub Y N 156 
HEC C2A CAA  sing N N 157 
HEC C3A C4A  sing Y N 158 
HEC C3A CMA  sing N N 159 
HEC CMA HMA1 sing N N 160 
HEC CMA HMA2 sing N N 161 
HEC CMA HMA3 sing N N 162 
HEC CAA CBA  sing N N 163 
HEC CAA HAA1 sing N N 164 
HEC CAA HAA2 sing N N 165 
HEC CBA CGA  sing N N 166 
HEC CBA HBA1 sing N N 167 
HEC CBA HBA2 sing N N 168 
HEC CGA O1A  doub N N 169 
HEC CGA O2A  sing N N 170 
HEC O2A H2A  sing N N 171 
HEC NB  C1B  sing Y N 172 
HEC NB  C4B  sing Y N 173 
HEC C1B C2B  doub Y N 174 
HEC C2B C3B  sing Y N 175 
HEC C2B CMB  sing N N 176 
HEC C3B C4B  sing Y N 177 
HEC C3B CAB  doub N E 178 
HEC CMB HMB1 sing N N 179 
HEC CMB HMB2 sing N N 180 
HEC CMB HMB3 sing N N 181 
HEC CAB CBB  sing N N 182 
HEC CAB HAB  sing N N 183 
HEC CBB HBB1 sing N N 184 
HEC CBB HBB2 sing N N 185 
HEC CBB HBB3 sing N N 186 
HEC NC  C1C  sing Y N 187 
HEC NC  C4C  sing Y N 188 
HEC C1C C2C  doub Y N 189 
HEC C2C C3C  sing Y N 190 
HEC C2C CMC  sing N N 191 
HEC C3C C4C  sing Y N 192 
HEC C3C CAC  doub N E 193 
HEC CMC HMC1 sing N N 194 
HEC CMC HMC2 sing N N 195 
HEC CMC HMC3 sing N N 196 
HEC CAC CBC  sing N N 197 
HEC CAC HAC  sing N N 198 
HEC CBC HBC1 sing N N 199 
HEC CBC HBC2 sing N N 200 
HEC CBC HBC3 sing N N 201 
HEC ND  C1D  sing Y N 202 
HEC ND  C4D  sing Y N 203 
HEC C1D C2D  doub Y N 204 
HEC C2D C3D  sing Y N 205 
HEC C2D CMD  sing N N 206 
HEC C3D C4D  doub Y N 207 
HEC C3D CAD  sing N N 208 
HEC CMD HMD1 sing N N 209 
HEC CMD HMD2 sing N N 210 
HEC CMD HMD3 sing N N 211 
HEC CAD CBD  sing N N 212 
HEC CAD HAD1 sing N N 213 
HEC CAD HAD2 sing N N 214 
HEC CBD CGD  sing N N 215 
HEC CBD HBD1 sing N N 216 
HEC CBD HBD2 sing N N 217 
HEC CGD O1D  doub N N 218 
HEC CGD O2D  sing N N 219 
HEC O2D H2D  sing N N 220 
HIS N   CA   sing N N 221 
HIS N   H    sing N N 222 
HIS N   H2   sing N N 223 
HIS CA  C    sing N N 224 
HIS CA  CB   sing N N 225 
HIS CA  HA   sing N N 226 
HIS C   O    doub N N 227 
HIS C   OXT  sing N N 228 
HIS CB  CG   sing N N 229 
HIS CB  HB2  sing N N 230 
HIS CB  HB3  sing N N 231 
HIS CG  ND1  sing Y N 232 
HIS CG  CD2  doub Y N 233 
HIS ND1 CE1  doub Y N 234 
HIS ND1 HD1  sing N N 235 
HIS CD2 NE2  sing Y N 236 
HIS CD2 HD2  sing N N 237 
HIS CE1 NE2  sing Y N 238 
HIS CE1 HE1  sing N N 239 
HIS NE2 HE2  sing N N 240 
HIS OXT HXT  sing N N 241 
HOH O   H1   sing N N 242 
HOH O   H2   sing N N 243 
ILE N   CA   sing N N 244 
ILE N   H    sing N N 245 
ILE N   H2   sing N N 246 
ILE CA  C    sing N N 247 
ILE CA  CB   sing N N 248 
ILE CA  HA   sing N N 249 
ILE C   O    doub N N 250 
ILE C   OXT  sing N N 251 
ILE CB  CG1  sing N N 252 
ILE CB  CG2  sing N N 253 
ILE CB  HB   sing N N 254 
ILE CG1 CD1  sing N N 255 
ILE CG1 HG12 sing N N 256 
ILE CG1 HG13 sing N N 257 
ILE CG2 HG21 sing N N 258 
ILE CG2 HG22 sing N N 259 
ILE CG2 HG23 sing N N 260 
ILE CD1 HD11 sing N N 261 
ILE CD1 HD12 sing N N 262 
ILE CD1 HD13 sing N N 263 
ILE OXT HXT  sing N N 264 
LEU N   CA   sing N N 265 
LEU N   H    sing N N 266 
LEU N   H2   sing N N 267 
LEU CA  C    sing N N 268 
LEU CA  CB   sing N N 269 
LEU CA  HA   sing N N 270 
LEU C   O    doub N N 271 
LEU C   OXT  sing N N 272 
LEU CB  CG   sing N N 273 
LEU CB  HB2  sing N N 274 
LEU CB  HB3  sing N N 275 
LEU CG  CD1  sing N N 276 
LEU CG  CD2  sing N N 277 
LEU CG  HG   sing N N 278 
LEU CD1 HD11 sing N N 279 
LEU CD1 HD12 sing N N 280 
LEU CD1 HD13 sing N N 281 
LEU CD2 HD21 sing N N 282 
LEU CD2 HD22 sing N N 283 
LEU CD2 HD23 sing N N 284 
LEU OXT HXT  sing N N 285 
LYS N   CA   sing N N 286 
LYS N   H    sing N N 287 
LYS N   H2   sing N N 288 
LYS CA  C    sing N N 289 
LYS CA  CB   sing N N 290 
LYS CA  HA   sing N N 291 
LYS C   O    doub N N 292 
LYS C   OXT  sing N N 293 
LYS CB  CG   sing N N 294 
LYS CB  HB2  sing N N 295 
LYS CB  HB3  sing N N 296 
LYS CG  CD   sing N N 297 
LYS CG  HG2  sing N N 298 
LYS CG  HG3  sing N N 299 
LYS CD  CE   sing N N 300 
LYS CD  HD2  sing N N 301 
LYS CD  HD3  sing N N 302 
LYS CE  NZ   sing N N 303 
LYS CE  HE2  sing N N 304 
LYS CE  HE3  sing N N 305 
LYS NZ  HZ1  sing N N 306 
LYS NZ  HZ2  sing N N 307 
LYS NZ  HZ3  sing N N 308 
LYS OXT HXT  sing N N 309 
MET N   CA   sing N N 310 
MET N   H    sing N N 311 
MET N   H2   sing N N 312 
MET CA  C    sing N N 313 
MET CA  CB   sing N N 314 
MET CA  HA   sing N N 315 
MET C   O    doub N N 316 
MET C   OXT  sing N N 317 
MET CB  CG   sing N N 318 
MET CB  HB2  sing N N 319 
MET CB  HB3  sing N N 320 
MET CG  SD   sing N N 321 
MET CG  HG2  sing N N 322 
MET CG  HG3  sing N N 323 
MET SD  CE   sing N N 324 
MET CE  HE1  sing N N 325 
MET CE  HE2  sing N N 326 
MET CE  HE3  sing N N 327 
MET OXT HXT  sing N N 328 
PHE N   CA   sing N N 329 
PHE N   H    sing N N 330 
PHE N   H2   sing N N 331 
PHE CA  C    sing N N 332 
PHE CA  CB   sing N N 333 
PHE CA  HA   sing N N 334 
PHE C   O    doub N N 335 
PHE C   OXT  sing N N 336 
PHE CB  CG   sing N N 337 
PHE CB  HB2  sing N N 338 
PHE CB  HB3  sing N N 339 
PHE CG  CD1  doub Y N 340 
PHE CG  CD2  sing Y N 341 
PHE CD1 CE1  sing Y N 342 
PHE CD1 HD1  sing N N 343 
PHE CD2 CE2  doub Y N 344 
PHE CD2 HD2  sing N N 345 
PHE CE1 CZ   doub Y N 346 
PHE CE1 HE1  sing N N 347 
PHE CE2 CZ   sing Y N 348 
PHE CE2 HE2  sing N N 349 
PHE CZ  HZ   sing N N 350 
PHE OXT HXT  sing N N 351 
PRO N   CA   sing N N 352 
PRO N   CD   sing N N 353 
PRO N   H    sing N N 354 
PRO CA  C    sing N N 355 
PRO CA  CB   sing N N 356 
PRO CA  HA   sing N N 357 
PRO C   O    doub N N 358 
PRO C   OXT  sing N N 359 
PRO CB  CG   sing N N 360 
PRO CB  HB2  sing N N 361 
PRO CB  HB3  sing N N 362 
PRO CG  CD   sing N N 363 
PRO CG  HG2  sing N N 364 
PRO CG  HG3  sing N N 365 
PRO CD  HD2  sing N N 366 
PRO CD  HD3  sing N N 367 
PRO OXT HXT  sing N N 368 
SER N   CA   sing N N 369 
SER N   H    sing N N 370 
SER N   H2   sing N N 371 
SER CA  C    sing N N 372 
SER CA  CB   sing N N 373 
SER CA  HA   sing N N 374 
SER C   O    doub N N 375 
SER C   OXT  sing N N 376 
SER CB  OG   sing N N 377 
SER CB  HB2  sing N N 378 
SER CB  HB3  sing N N 379 
SER OG  HG   sing N N 380 
SER OXT HXT  sing N N 381 
THR N   CA   sing N N 382 
THR N   H    sing N N 383 
THR N   H2   sing N N 384 
THR CA  C    sing N N 385 
THR CA  CB   sing N N 386 
THR CA  HA   sing N N 387 
THR C   O    doub N N 388 
THR C   OXT  sing N N 389 
THR CB  OG1  sing N N 390 
THR CB  CG2  sing N N 391 
THR CB  HB   sing N N 392 
THR OG1 HG1  sing N N 393 
THR CG2 HG21 sing N N 394 
THR CG2 HG22 sing N N 395 
THR CG2 HG23 sing N N 396 
THR OXT HXT  sing N N 397 
TRP N   CA   sing N N 398 
TRP N   H    sing N N 399 
TRP N   H2   sing N N 400 
TRP CA  C    sing N N 401 
TRP CA  CB   sing N N 402 
TRP CA  HA   sing N N 403 
TRP C   O    doub N N 404 
TRP C   OXT  sing N N 405 
TRP CB  CG   sing N N 406 
TRP CB  HB2  sing N N 407 
TRP CB  HB3  sing N N 408 
TRP CG  CD1  doub Y N 409 
TRP CG  CD2  sing Y N 410 
TRP CD1 NE1  sing Y N 411 
TRP CD1 HD1  sing N N 412 
TRP CD2 CE2  doub Y N 413 
TRP CD2 CE3  sing Y N 414 
TRP NE1 CE2  sing Y N 415 
TRP NE1 HE1  sing N N 416 
TRP CE2 CZ2  sing Y N 417 
TRP CE3 CZ3  doub Y N 418 
TRP CE3 HE3  sing N N 419 
TRP CZ2 CH2  doub Y N 420 
TRP CZ2 HZ2  sing N N 421 
TRP CZ3 CH2  sing Y N 422 
TRP CZ3 HZ3  sing N N 423 
TRP CH2 HH2  sing N N 424 
TRP OXT HXT  sing N N 425 
TYR N   CA   sing N N 426 
TYR N   H    sing N N 427 
TYR N   H2   sing N N 428 
TYR CA  C    sing N N 429 
TYR CA  CB   sing N N 430 
TYR CA  HA   sing N N 431 
TYR C   O    doub N N 432 
TYR C   OXT  sing N N 433 
TYR CB  CG   sing N N 434 
TYR CB  HB2  sing N N 435 
TYR CB  HB3  sing N N 436 
TYR CG  CD1  doub Y N 437 
TYR CG  CD2  sing Y N 438 
TYR CD1 CE1  sing Y N 439 
TYR CD1 HD1  sing N N 440 
TYR CD2 CE2  doub Y N 441 
TYR CD2 HD2  sing N N 442 
TYR CE1 CZ   doub Y N 443 
TYR CE1 HE1  sing N N 444 
TYR CE2 CZ   sing Y N 445 
TYR CE2 HE2  sing N N 446 
TYR CZ  OH   sing N N 447 
TYR OH  HH   sing N N 448 
TYR OXT HXT  sing N N 449 
VAL N   CA   sing N N 450 
VAL N   H    sing N N 451 
VAL N   H2   sing N N 452 
VAL CA  C    sing N N 453 
VAL CA  CB   sing N N 454 
VAL CA  HA   sing N N 455 
VAL C   O    doub N N 456 
VAL C   OXT  sing N N 457 
VAL CB  CG1  sing N N 458 
VAL CB  CG2  sing N N 459 
VAL CB  HB   sing N N 460 
VAL CG1 HG11 sing N N 461 
VAL CG1 HG12 sing N N 462 
VAL CG1 HG13 sing N N 463 
VAL CG2 HG21 sing N N 464 
VAL CG2 HG22 sing N N 465 
VAL CG2 HG23 sing N N 466 
VAL OXT HXT  sing N N 467 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2B4Z 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9MT0 
_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]   0.029519 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008897 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017055 
_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]   0.020212 
_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_b1 
_atom_type.scat_Cromer_Mann_b2 
_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.
;
? 
FE ? ? 20.90327 4.99816 2.55100  38.46870 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.
;
? 
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    . GLY A 1 1   ? 42.53508 33.46700 -30.07834 1.000 22.26745 ? -3  GLY A N    1 
ATOM   2    C  CA   . GLY A 1 1   ? 41.17391 32.96207 -29.93066 1.000 21.46477 ? -3  GLY A CA   1 
ATOM   3    C  C    . GLY A 1 1   ? 41.01759 32.14370 -28.65781 1.000 18.42958 ? -3  GLY A C    1 
ATOM   4    O  O    . GLY A 1 1   ? 41.76051 32.34564 -27.71687 1.000 21.32255 ? -3  GLY A O    1 
ATOM   5    H  HA2  . GLY A 1 1   ? 40.55350 33.70700 -29.89798 1.000 25.78245 ? -3  GLY A HA2  1 
ATOM   6    H  HA3  . GLY A 1 1   ? 40.95255 32.39978 -30.68944 1.000 25.78245 ? -3  GLY A HA3  1 
ATOM   7    N  N    . VAL A 1 2   ? 40.08246 31.19573 -28.64553 1.000 18.33901 ? -2  VAL A N    1 
ATOM   8    C  CA   . VAL A 1 2   ? 39.77576 30.40270 -27.45996 1.000 16.83722 ? -2  VAL A CA   1 
ATOM   9    C  C    . VAL A 1 2   ? 40.30984 28.98687 -27.68177 1.000 16.49019 ? -2  VAL A C    1 
ATOM   10   O  O    . VAL A 1 2   ? 39.82348 28.28505 -28.57999 1.000 19.14863 ? -2  VAL A O    1 
ATOM   11   C  CB   . VAL A 1 2   ? 38.27199 30.38717 -27.15939 1.000 18.53789 ? -2  VAL A CB   1 
ATOM   12   C  CG1  . VAL A 1 2   ? 37.96494 29.53137 -25.92968 1.000 19.92521 ? -2  VAL A CG1  1 
ATOM   13   C  CG2  . VAL A 1 2   ? 37.76274 31.80635 -26.97062 1.000 19.84172 ? -2  VAL A CG2  1 
ATOM   14   H  H    . VAL A 1 2   ? 39.60357 30.99225 -29.33027 1.000 22.03154 ? -2  VAL A H    1 
ATOM   15   H  HA   . VAL A 1 2   ? 40.23772 30.78588 -26.69795 1.000 20.22939 ? -2  VAL A HA   1 
ATOM   16   H  HB   . VAL A 1 2   ? 37.80685 29.99087 -27.91271 1.000 22.27019 ? -2  VAL A HB   1 
ATOM   17   H  HG11 . VAL A 1 2   ? 37.08642 29.76674 -25.59249 1.000 23.93498 ? -2  VAL A HG11 1 
ATOM   18   H  HG12 . VAL A 1 2   ? 37.98180 28.59547 -26.18405 1.000 23.93498 ? -2  VAL A HG12 1 
ATOM   19   H  HG13 . VAL A 1 2   ? 38.63641 29.70175 -25.25070 1.000 23.93498 ? -2  VAL A HG13 1 
ATOM   20   H  HG21 . VAL A 1 2   ? 36.83070 31.77454 -26.70379 1.000 23.83479 ? -2  VAL A HG21 1 
ATOM   21   H  HG22 . VAL A 1 2   ? 38.28924 32.24183 -26.28212 1.000 23.83479 ? -2  VAL A HG22 1 
ATOM   22   H  HG23 . VAL A 1 2   ? 37.85076 32.28749 -27.80827 1.000 23.83479 ? -2  VAL A HG23 1 
ATOM   23   N  N    . PRO A 1 3   ? 41.29811 28.51776 -26.91156 1.000 16.57017 ? -1  PRO A N    1 
ATOM   24   C  CA   . PRO A 1 3   ? 41.79257 27.15366 -27.12237 1.000 17.47170 ? -1  PRO A CA   1 
ATOM   25   C  C    . PRO A 1 3   ? 40.72733 26.10914 -26.84252 1.000 17.03844 ? -1  PRO A C    1 
ATOM   26   O  O    . PRO A 1 3   ? 39.79337 26.31867 -26.06762 1.000 17.94359 ? -1  PRO A O    1 
ATOM   27   C  CB   . PRO A 1 3   ? 42.94237 27.01773 -26.11824 1.000 19.79965 ? -1  PRO A CB   1 
ATOM   28   C  CG   . PRO A 1 3   ? 43.24001 28.36681 -25.64020 1.000 22.20793 ? -1  PRO A CG   1 
ATOM   29   C  CD   . PRO A 1 3   ? 42.00178 29.18192 -25.79952 1.000 18.67360 ? -1  PRO A CD   1 
ATOM   30   H  HA   . PRO A 1 3   ? 42.12199 27.06109 -28.03001 1.000 20.99077 ? -1  PRO A HA   1 
ATOM   31   H  HB2  . PRO A 1 3   ? 42.66485 26.44863 -25.38340 1.000 23.78431 ? -1  PRO A HB2  1 
ATOM   32   H  HB3  . PRO A 1 3   ? 43.71540 26.63421 -26.56124 1.000 23.78431 ? -1  PRO A HB3  1 
ATOM   33   H  HG2  . PRO A 1 3   ? 43.49937 28.32596 -24.70642 1.000 26.67425 ? -1  PRO A HG2  1 
ATOM   34   H  HG3  . PRO A 1 3   ? 43.96152 28.74219 -26.16881 1.000 26.67425 ? -1  PRO A HG3  1 
ATOM   35   H  HD2  . PRO A 1 3   ? 41.46728 29.15927 -24.99038 1.000 22.43305 ? -1  PRO A HD2  1 
ATOM   36   H  HD3  . PRO A 1 3   ? 42.21950 30.09921 -26.02774 1.000 22.43305 ? -1  PRO A HD3  1 
ATOM   37   N  N    . ALA A 1 4   ? 40.91404 24.95552 -27.47287 1.000 18.39964 ? 0   ALA A N    1 
ATOM   38   C  CA   . ALA A 1 4   ? 40.06246 23.80334 -27.24723 1.000 18.62795 ? 0   ALA A CA   1 
ATOM   39   C  C    . ALA A 1 4   ? 40.01507 23.45712 -25.76359 1.000 18.71365 ? 0   ALA A C    1 
ATOM   40   O  O    . ALA A 1 4   ? 40.95565 23.73202 -25.00172 1.000 21.48507 ? 0   ALA A O    1 
ATOM   41   C  CB   . ALA A 1 4   ? 40.63599 22.61277 -28.01396 1.000 23.91852 ? 0   ALA A CB   1 
ATOM   42   H  H    . ALA A 1 4   ? 41.53868 24.81269 -28.04648 1.000 22.10429 ? 0   ALA A H    1 
ATOM   43   H  HA   . ALA A 1 4   ? 39.16065 23.99241 -27.55035 1.000 22.37827 ? 0   ALA A HA   1 
ATOM   44   H  HB1  . ALA A 1 4   ? 40.08683 21.83198 -27.84162 1.000 28.72695 ? 0   ALA A HB1  1 
ATOM   45   H  HB2  . ALA A 1 4   ? 40.63275 22.81667 -28.96228 1.000 28.72695 ? 0   ALA A HB2  1 
ATOM   46   H  HB3  . ALA A 1 4   ? 41.54402 22.45138 -27.71341 1.000 28.72695 ? 0   ALA A HB3  1 
ATOM   47   N  N    . GLY A 1 5   ? 38.87506 22.89487 -25.34190 1.000 16.23525 ? 1   GLY A N    1 
ATOM   48   C  CA   . GLY A 1 5   ? 38.69138 22.45651 -23.97534 1.000 15.62962 ? 1   GLY A CA   1 
ATOM   49   C  C    . GLY A 1 5   ? 38.25451 21.00304 -23.89260 1.000 15.64232 ? 1   GLY A C    1 
ATOM   50   O  O    . GLY A 1 5   ? 37.97604 20.34448 -24.89617 1.000 18.31766 ? 1   GLY A O    1 
ATOM   51   H  H    . GLY A 1 5   ? 38.19005 22.75931 -25.84389 1.000 19.50702 ? 1   GLY A H    1 
ATOM   52   H  HA2  . GLY A 1 5   ? 39.52618 22.55330 -23.49094 1.000 18.78027 ? 1   GLY A HA2  1 
ATOM   53   H  HA3  . GLY A 1 5   ? 38.01377 23.00456 -23.54946 1.000 18.78027 ? 1   GLY A HA3  1 
ATOM   54   N  N    . ASP A 1 6   ? 38.18447 20.52997 -22.64898 1.000 14.71157 ? 2   ASP A N    1 
ATOM   55   C  CA   . ASP A 1 6   ? 37.81577 19.16169 -22.30114 1.000 15.58093 ? 2   ASP A CA   1 
ATOM   56   C  C    . ASP A 1 6   ? 36.34459 19.17001 -21.90130 1.000 14.93916 ? 2   ASP A C    1 
ATOM   57   O  O    . ASP A 1 6   ? 35.96826 19.78622 -20.90358 1.000 14.08650 ? 2   ASP A O    1 
ATOM   58   C  CB   . ASP A 1 6   ? 38.69719 18.72648 -21.12760 1.000 18.32367 ? 2   ASP A CB   1 
ATOM   59   C  CG   . ASP A 1 6   ? 38.43889 17.29993 -20.63427 1.000 24.23797 ? 2   ASP A CG   1 
ATOM   60   O  OD1  . ASP A 1 6   ? 37.28203 16.87474 -20.47155 1.000 23.30938 ? 2   ASP A OD1  1 
ATOM   61   O  OD2  . ASP A 1 6   ? 39.43472 16.61257 -20.33203 1.000 30.07886 ? 2   ASP A OD2  1 
ATOM   62   H  H    . ASP A 1 6   ? 38.35549 21.01002 -21.95622 1.000 17.67861 ? 2   ASP A H    1 
ATOM   63   H  HA   . ASP A 1 6   ? 37.92544 18.54733 -23.04373 1.000 18.72184 ? 2   ASP A HA   1 
ATOM   64   H  HB2  . ASP A 1 6   ? 39.62595 18.77714 -21.40281 1.000 22.01313 ? 2   ASP A HB2  1 
ATOM   65   H  HB3  . ASP A 1 6   ? 38.53877 19.32686 -20.38239 1.000 22.01313 ? 2   ASP A HB3  1 
ATOM   66   N  N    A VAL A 1 7   ? 35.49439 18.49683 -22.68492 0.618 15.80267 ? 3   VAL A N    1 
ATOM   67   N  N    B VAL A 1 7   ? 35.52912 18.44189 -22.65829 0.382 14.74550 ? 3   VAL A N    1 
ATOM   68   C  CA   A VAL A 1 7   ? 34.05855 18.59756 -22.42487 0.618 16.90802 ? 3   VAL A CA   1 
ATOM   69   C  CA   B VAL A 1 7   ? 34.08875 18.53176 -22.48684 0.382 14.20161 ? 3   VAL A CA   1 
ATOM   70   C  C    A VAL A 1 7   ? 33.66141 17.94940 -21.10961 0.618 17.25632 ? 3   VAL A C    1 
ATOM   71   C  C    B VAL A 1 7   ? 33.61926 17.87633 -21.19272 0.382 13.98040 ? 3   VAL A C    1 
ATOM   72   O  O    A VAL A 1 7   ? 32.69817 18.38952 -20.47866 0.618 18.34274 ? 3   VAL A O    1 
ATOM   73   O  O    B VAL A 1 7   ? 32.56986 18.24387 -20.65998 0.382 13.06346 ? 3   VAL A O    1 
ATOM   74   C  CB   A VAL A 1 7   ? 33.18471 18.08079 -23.58226 0.618 21.08601 ? 3   VAL A CB   1 
ATOM   75   C  CB   B VAL A 1 7   ? 33.40791 17.97681 -23.75060 0.382 16.87323 ? 3   VAL A CB   1 
ATOM   76   C  CG1  A VAL A 1 7   ? 33.46638 18.86904 -24.83774 0.618 23.72357 ? 3   VAL A CG1  1 
ATOM   77   C  CG1  B VAL A 1 7   ? 31.95025 17.68664 -23.51645 0.382 15.18498 ? 3   VAL A CG1  1 
ATOM   78   C  CG2  A VAL A 1 7   ? 33.37539 16.58887 -23.78938 0.618 22.59882 ? 3   VAL A CG2  1 
ATOM   79   C  CG2  B VAL A 1 7   ? 33.58439 18.97831 -24.89971 0.382 19.34495 ? 3   VAL A CG2  1 
ATOM   80   H  H    A VAL A 1 7   ? 35.71395 17.99457 -23.34759 0.618 18.98793 ? 3   VAL A H    1 
ATOM   81   H  H    B VAL A 1 7   ? 35.78127 17.89418 -23.27152 0.382 17.71933 ? 3   VAL A H    1 
ATOM   82   H  HA   A VAL A 1 7   ? 33.88963 19.55028 -22.35646 0.618 20.31435 ? 3   VAL A HA   1 
ATOM   83   H  HA   B VAL A 1 7   ? 33.83197 19.46237 -22.39237 0.382 17.06666 ? 3   VAL A HA   1 
ATOM   84   H  HB   A VAL A 1 7   ? 32.24979 18.21020 -23.35847 0.618 25.32794 ? 3   VAL A HB   1 
ATOM   85   H  HB   B VAL A 1 7   ? 33.82584 17.13471 -23.98957 0.382 20.27261 ? 3   VAL A HB   1 
ATOM   86   H  HG11 A VAL A 1 7   ? 32.75369 18.71091 -25.47647 0.618 28.49301 ? 3   VAL A HG11 1 
ATOM   87   H  HG11 B VAL A 1 7   ? 31.51811 17.53059 -24.37074 0.382 18.24670 ? 3   VAL A HG11 1 
ATOM   88   H  HG12 A VAL A 1 7   ? 33.50825 19.81234 -24.61566 0.618 28.49301 ? 3   VAL A HG12 1 
ATOM   89   H  HG12 B VAL A 1 7   ? 31.87110 16.89831 -22.95683 0.382 18.24670 ? 3   VAL A HG12 1 
ATOM   90   H  HG13 A VAL A 1 7   ? 34.31405 18.57877 -25.20937 0.618 28.49301 ? 3   VAL A HG13 1 
ATOM   91   H  HG13 B VAL A 1 7   ? 31.54368 18.44831 -23.07434 0.382 18.24670 ? 3   VAL A HG13 1 
ATOM   92   H  HG21 A VAL A 1 7   ? 33.00529 16.33977 -24.65071 0.618 27.14331 ? 3   VAL A HG21 1 
ATOM   93   H  HG21 B VAL A 1 7   ? 32.94845 18.76890 -25.60159 0.382 23.23867 ? 3   VAL A HG21 1 
ATOM   94   H  HG22 A VAL A 1 7   ? 34.32349 16.38534 -23.76539 0.618 27.14331 ? 3   VAL A HG22 1 
ATOM   95   H  HG22 B VAL A 1 7   ? 33.42430 19.87451 -24.56491 0.382 23.23867 ? 3   VAL A HG22 1 
ATOM   96   H  HG23 A VAL A 1 7   ? 32.91637 16.11053 -23.08130 0.618 27.14331 ? 3   VAL A HG23 1 
ATOM   97   H  HG23 B VAL A 1 7   ? 34.48936 18.90985 -25.24209 0.382 23.23867 ? 3   VAL A HG23 1 
ATOM   98   N  N    . GLU A 1 8   ? 34.35704 16.89734 -20.66915 1.000 15.79323 ? 4   GLU A N    1 
ATOM   99   C  CA   . GLU A 1 8   ? 33.97075 16.30103 -19.39402 1.000 18.11230 ? 4   GLU A CA   1 
ATOM   100  C  C    . GLU A 1 8   ? 34.27677 17.24363 -18.23669 1.000 16.07622 ? 4   GLU A C    1 
ATOM   101  O  O    . GLU A 1 8   ? 33.45802 17.38671 -17.31695 1.000 15.02713 ? 4   GLU A O    1 
ATOM   102  C  CB   . GLU A 1 8   ? 34.60900 14.92598 -19.23867 1.000 24.21984 ? 4   GLU A CB   1 
ATOM   103  C  CG   . GLU A 1 8   ? 34.07323 13.94930 -20.28734 1.000 35.06156 ? 4   GLU A CG   1 
ATOM   104  C  CD   . GLU A 1 8   ? 34.49643 12.51682 -20.06073 1.000 42.83746 ? 4   GLU A CD   1 
ATOM   105  O  OE1  . GLU A 1 8   ? 35.68857 12.20633 -20.28941 1.000 45.59395 ? 4   GLU A OE1  1 
ATOM   106  O  OE2  . GLU A 1 8   ? 33.63059 11.70044 -19.66313 1.000 44.34384 ? 4   GLU A OE2  1 
ATOM   107  H  H    . GLU A 1 8   ? 35.02300 16.52835 -21.06907 1.000 18.97660 ? 4   GLU A H    1 
ATOM   108  H  HA   . GLU A 1 8   ? 33.01278 16.14968 -19.37703 1.000 21.75949 ? 4   GLU A HA   1 
ATOM   109  H  HB2  . GLU A 1 8   ? 35.56941 15.00200 -19.35154 1.000 29.08854 ? 4   GLU A HB2  1 
ATOM   110  H  HB3  . GLU A 1 8   ? 34.40529 14.57390 -18.35807 1.000 29.08854 ? 4   GLU A HB3  1 
ATOM   111  H  HG2  . GLU A 1 8   ? 33.10373 13.97664 -20.27248 1.000 42.09859 ? 4   GLU A HG2  1 
ATOM   112  H  HG3  . GLU A 1 8   ? 34.39939 14.21899 -21.16014 1.000 42.09859 ? 4   GLU A HG3  1 
ATOM   113  N  N    . LYS A 1 9   ? 35.43998 17.90448 -18.26705 1.000 15.77629 ? 5   LYS A N    1 
ATOM   114  C  CA   . LYS A 1 9   ? 35.71647 18.93242 -17.26990 1.000 14.84523 ? 5   LYS A CA   1 
ATOM   115  C  C    . LYS A 1 9   ? 34.71660 20.07656 -17.38591 1.000 14.50201 ? 5   LYS A C    1 
ATOM   116  O  O    . LYS A 1 9   ? 34.27039 20.63697 -16.37634 1.000 14.47703 ? 5   LYS A O    1 
ATOM   117  C  CB   . LYS A 1 9   ? 37.14664 19.44528 -17.41381 1.000 17.62439 ? 5   LYS A CB   1 
ATOM   118  C  CG   . LYS A 1 9   ? 38.18556 18.40693 -17.04340 1.000 19.82725 ? 5   LYS A CG   1 
ATOM   119  C  CD   . LYS A 1 9   ? 39.60078 18.96919 -17.12295 1.000 24.07604 ? 5   LYS A CD   1 
ATOM   120  C  CE   . LYS A 1 9   ? 40.63921 17.98518 -16.58985 1.000 31.26526 ? 5   LYS A CE   1 
ATOM   121  N  NZ   . LYS A 1 9   ? 42.04068 18.48087 -16.77077 1.000 35.14575 ? 5   LYS A NZ   1 
ATOM   122  H  H    . LYS A 1 9   ? 36.06867 17.77887 -18.84026 1.000 18.95627 ? 5   LYS A H    1 
ATOM   123  H  HA   . LYS A 1 9   ? 35.63592 18.54357 -16.38492 1.000 17.83900 ? 5   LYS A HA   1 
ATOM   124  H  HB2  . LYS A 1 9   ? 37.29721 19.70407 -18.33645 1.000 21.17399 ? 5   LYS A HB2  1 
ATOM   125  H  HB3  . LYS A 1 9   ? 37.26695 20.21099 -16.83061 1.000 21.17399 ? 5   LYS A HB3  1 
ATOM   126  H  HG2  . LYS A 1 9   ? 38.02862 18.10698 -16.13439 1.000 23.81743 ? 5   LYS A HG2  1 
ATOM   127  H  HG3  . LYS A 1 9   ? 38.12172 17.65739 -17.65578 1.000 23.81743 ? 5   LYS A HG3  1 
ATOM   128  H  HD2  . LYS A 1 9   ? 39.81546 19.16358 -18.04870 1.000 28.91598 ? 5   LYS A HD2  1 
ATOM   129  H  HD3  . LYS A 1 9   ? 39.65236 19.78005 -16.59310 1.000 28.91598 ? 5   LYS A HD3  1 
ATOM   130  H  HE2  . LYS A 1 9   ? 40.48858 17.84704 -15.64163 1.000 37.54304 ? 5   LYS A HE2  1 
ATOM   131  H  HE3  . LYS A 1 9   ? 40.55341 17.14411 -17.06539 1.000 37.54304 ? 5   LYS A HE3  1 
ATOM   132  H  HZ1  . LYS A 1 9   ? 42.61946 17.86924 -16.48263 1.000 42.19963 ? 5   LYS A HZ1  1 
ATOM   133  H  HZ2  . LYS A 1 9   ? 42.19721 18.64373 -17.63162 1.000 42.19963 ? 5   LYS A HZ2  1 
ATOM   134  H  HZ3  . LYS A 1 9   ? 42.16000 19.23190 -16.30837 1.000 42.19963 ? 5   LYS A HZ3  1 
ATOM   135  N  N    . GLY A 1 10  ? 34.35298 20.43944 -18.61683 1.000 12.46295 ? 6   GLY A N    1 
ATOM   136  C  CA   . GLY A 1 10  ? 33.40013 21.51656 -18.79707 1.000 12.50129 ? 6   GLY A CA   1 
ATOM   137  C  C    . GLY A 1 10  ? 32.00148 21.17198 -18.31553 1.000 12.21589 ? 6   GLY A C    1 
ATOM   138  O  O    . GLY A 1 10  ? 31.30310 22.02682 -17.75767 1.000 12.83925 ? 6   GLY A O    1 
ATOM   139  H  H    . GLY A 1 10  ? 34.63852 20.08420 -19.34612 1.000 14.98027 ? 6   GLY A H    1 
ATOM   140  H  HA2  . GLY A 1 10  ? 33.70495 22.29502 -18.30515 1.000 15.02628 ? 6   GLY A HA2  1 
ATOM   141  H  HA3  . GLY A 1 10  ? 33.34798 21.73916 -19.73974 1.000 15.02628 ? 6   GLY A HA3  1 
ATOM   142  N  N    . LYS A 1 11  ? 31.59313 19.91107 -18.47911 1.000 12.17457 ? 7   LYS A N    1 
ATOM   143  C  CA   . LYS A 1 11  ? 30.30359 19.47111 -17.95161 1.000 12.80308 ? 7   LYS A CA   1 
ATOM   144  C  C    . LYS A 1 11  ? 30.26043 19.57983 -16.42945 1.000 12.29455 ? 7   LYS A C    1 
ATOM   145  O  O    . LYS A 1 11  ? 29.23314 19.96314 -15.85953 1.000 13.67841 ? 7   LYS A O    1 
ATOM   146  C  CB   . LYS A 1 11  ? 30.02736 18.03173 -18.39024 1.000 14.53824 ? 7   LYS A CB   1 
ATOM   147  C  CG   . LYS A 1 11  ? 28.67583 17.47869 -17.90437 1.000 15.82977 ? 7   LYS A CG   1 
ATOM   148  C  CD   . LYS A 1 11  ? 28.13073 16.32099 -18.74523 1.000 19.63509 ? 7   LYS A CD   1 
ATOM   149  C  CE   . LYS A 1 11  ? 29.05861 15.13044 -18.78168 1.000 21.07020 ? 7   LYS A CE   1 
ATOM   150  N  NZ   . LYS A 1 11  ? 29.18782 14.46806 -17.45734 1.000 23.34075 ? 7   LYS A NZ   1 
ATOM   151  H  H    . LYS A 1 11  ? 32.03730 19.29749 -18.88635 1.000 14.63421 ? 7   LYS A H    1 
ATOM   152  H  HA   . LYS A 1 11  ? 29.60667 20.04056 -18.31346 1.000 15.38842 ? 7   LYS A HA   1 
ATOM   153  H  HB2  . LYS A 1 11  ? 30.02968 17.99613 -19.35958 1.000 17.47062 ? 7   LYS A HB2  1 
ATOM   154  H  HB3  . LYS A 1 11  ? 30.72540 17.45915 -18.03556 1.000 17.47062 ? 7   LYS A HB3  1 
ATOM   155  H  HG2  . LYS A 1 11  ? 28.78056 17.15676 -16.99536 1.000 19.02045 ? 7   LYS A HG2  1 
ATOM   156  H  HG3  . LYS A 1 11  ? 28.02046 18.19335 -17.92978 1.000 19.02045 ? 7   LYS A HG3  1 
ATOM   157  H  HD2  . LYS A 1 11  ? 27.28523 16.02912 -18.36994 1.000 23.58683 ? 7   LYS A HD2  1 
ATOM   158  H  HD3  . LYS A 1 11  ? 28.00128 16.62658 -19.65669 1.000 23.58683 ? 7   LYS A HD3  1 
ATOM   159  H  HE2  . LYS A 1 11  ? 28.71343 14.47848 -19.41152 1.000 25.30897 ? 7   LYS A HE2  1 
ATOM   160  H  HE3  . LYS A 1 11  ? 29.94072 15.42419 -19.05825 1.000 25.30897 ? 7   LYS A HE3  1 
ATOM   161  H  HZ1  . LYS A 1 11  ? 29.70871 13.74967 -17.52583 1.000 28.03362 ? 7   LYS A HZ1  1 
ATOM   162  H  HZ2  . LYS A 1 11  ? 29.54783 15.03086 -16.86933 1.000 28.03362 ? 7   LYS A HZ2  1 
ATOM   163  H  HZ3  . LYS A 1 11  ? 28.38632 14.21670 -17.16322 1.000 28.03362 ? 7   LYS A HZ3  1 
ATOM   164  N  N    . LYS A 1 12  ? 31.35327 19.21947 -15.74786 1.000 12.74009 ? 8   LYS A N    1 
ATOM   165  C  CA   . LYS A 1 12  ? 31.40916 19.33220 -14.29649 1.000 13.62597 ? 8   LYS A CA   1 
ATOM   166  C  C    . LYS A 1 12  ? 31.26528 20.78205 -13.86052 1.000 12.47007 ? 8   LYS A C    1 
ATOM   167  O  O    . LYS A 1 12  ? 30.51871 21.08126 -12.92208 1.000 14.34321 ? 8   LYS A O    1 
ATOM   168  C  CB   . LYS A 1 12  ? 32.72560 18.75069 -13.78732 1.000 15.46178 ? 8   LYS A CB   1 
ATOM   169  C  CG   . LYS A 1 12  ? 32.89987 18.85535 -12.27878 1.000 19.35102 ? 8   LYS A CG   1 
ATOM   170  C  CD   . LYS A 1 12  ? 34.16500 18.16215 -11.81114 1.000 25.97414 ? 8   LYS A CD   1 
ATOM   171  C  CE   . LYS A 1 12  ? 34.40389 18.35830 -10.30684 1.000 33.34783 ? 8   LYS A CE   1 
ATOM   172  N  NZ   . LYS A 1 12  ? 35.02280 19.68383 -9.99571  1.000 38.66670 ? 8   LYS A NZ   1 
ATOM   173  H  H    . LYS A 1 12  ? 32.07226 18.90805 -16.10236 1.000 15.31284 ? 8   LYS A H    1 
ATOM   174  H  HA   . LYS A 1 12  ? 30.68050 18.82404 -13.90697 1.000 16.37589 ? 8   LYS A HA   1 
ATOM   175  H  HB2  . LYS A 1 12  ? 32.76413 17.81114 -14.02534 1.000 18.57886 ? 8   LYS A HB2  1 
ATOM   176  H  HB3  . LYS A 1 12  ? 33.45950 19.22886 -14.20403 1.000 18.57886 ? 8   LYS A HB3  1 
ATOM   177  H  HG2  . LYS A 1 12  ? 32.95452 19.79038 -12.02651 1.000 23.24595 ? 8   LYS A HG2  1 
ATOM   178  H  HG3  . LYS A 1 12  ? 32.14346 18.43672 -11.83890 1.000 23.24595 ? 8   LYS A HG3  1 
ATOM   179  H  HD2  . LYS A 1 12  ? 34.09099 17.21068 -11.98469 1.000 31.19370 ? 8   LYS A HD2  1 
ATOM   180  H  HD3  . LYS A 1 12  ? 34.92551 18.52839 -12.28904 1.000 31.19370 ? 8   LYS A HD3  1 
ATOM   181  H  HE2  . LYS A 1 12  ? 33.55478 18.30559 -9.84087  1.000 40.04212 ? 8   LYS A HE2  1 
ATOM   182  H  HE3  . LYS A 1 12  ? 35.00147 17.66440 -9.98701  1.000 40.04212 ? 8   LYS A HE3  1 
ATOM   183  H  HZ1  . LYS A 1 12  ? 35.15097 19.76152 -9.11842  1.000 46.42477 ? 8   LYS A HZ1  1 
ATOM   184  H  HZ2  . LYS A 1 12  ? 35.80702 19.75834 -10.40990 1.000 46.42477 ? 8   LYS A HZ2  1 
ATOM   185  H  HZ3  . LYS A 1 12  ? 34.48831 20.34096 -10.26884 1.000 46.42477 ? 8   LYS A HZ3  1 
ATOM   186  N  N    . ILE A 1 13  ? 31.95730 21.70024 -14.54063 1.000 12.50009 ? 9   ILE A N    1 
ATOM   187  C  CA   . ILE A 1 13  ? 31.79302 23.12768 -14.26564 1.000 12.66204 ? 9   ILE A CA   1 
ATOM   188  C  C    . ILE A 1 13  ? 30.34163 23.53999 -14.45549 1.000 12.55759 ? 9   ILE A C    1 
ATOM   189  O  O    . ILE A 1 13  ? 29.77140 24.26911 -13.63391 1.000 13.20001 ? 9   ILE A O    1 
ATOM   190  C  CB   . ILE A 1 13  ? 32.73854 23.96719 -15.14793 1.000 13.11643 ? 9   ILE A CB   1 
ATOM   191  C  CG1  . ILE A 1 13  ? 34.19417 23.72801 -14.75510 1.000 15.09825 ? 9   ILE A CG1  1 
ATOM   192  C  CG2  . ILE A 1 13  ? 32.42618 25.46224 -15.02041 1.000 14.09117 ? 9   ILE A CG2  1 
ATOM   193  C  CD1  . ILE A 1 13  ? 35.19183 24.17945 -15.83277 1.000 16.47708 ? 9   ILE A CD1  1 
ATOM   194  H  H    . ILE A 1 13  ? 32.52495 21.52532 -15.16254 1.000 15.02484 ? 9   ILE A H    1 
ATOM   195  H  HA   . ILE A 1 13  ? 32.03245 23.28759 -13.33936 1.000 15.21917 ? 9   ILE A HA   1 
ATOM   196  H  HB   . ILE A 1 13  ? 32.59973 23.68824 -16.06652 1.000 15.76445 ? 9   ILE A HB   1 
ATOM   197  H  HG12 . ILE A 1 13  ? 34.38629 24.22360 -13.94370 1.000 18.14263 ? 9   ILE A HG12 1 
ATOM   198  H  HG13 . ILE A 1 13  ? 34.32704 22.77916 -14.60363 1.000 18.14263 ? 9   ILE A HG13 1 
ATOM   199  H  HG21 . ILE A 1 13  ? 33.19250 25.97219 -15.32636 1.000 16.93413 ? 9   ILE A HG21 1 
ATOM   200  H  HG22 . ILE A 1 13  ? 31.65127 25.67057 -15.56540 1.000 16.93413 ? 9   ILE A HG22 1 
ATOM   201  H  HG23 . ILE A 1 13  ? 32.24168 25.66814 -14.09064 1.000 16.93413 ? 9   ILE A HG23 1 
ATOM   202  H  HD11 . ILE A 1 13  ? 36.06454 23.80717 -15.63103 1.000 19.79722 ? 9   ILE A HD11 1 
ATOM   203  H  HD12 . ILE A 1 13  ? 34.88828 23.86121 -16.69734 1.000 19.79722 ? 9   ILE A HD12 1 
ATOM   204  H  HD13 . ILE A 1 13  ? 35.23789 25.14836 -15.83448 1.000 19.79722 ? 9   ILE A HD13 1 
ATOM   205  N  N    . PHE A 1 14  ? 29.72632 23.11630 -15.56500 1.000 12.61211 ? 10  PHE A N    1 
ATOM   206  C  CA   . PHE A 1 14  ? 28.34699 23.49697 -15.83865 1.000 11.64097 ? 10  PHE A CA   1 
ATOM   207  C  C    . PHE A 1 14  ? 27.41748 23.03709 -14.72552 1.000 11.90023 ? 10  PHE A C    1 
ATOM   208  O  O    . PHE A 1 14  ? 26.57219 23.80443 -14.23896 1.000 12.66055 ? 10  PHE A O    1 
ATOM   209  C  CB   . PHE A 1 14  ? 27.87029 22.95666 -17.19318 1.000 11.98709 ? 10  PHE A CB   1 
ATOM   210  C  CG   . PHE A 1 14  ? 26.50135 23.44176 -17.55476 1.000 12.68443 ? 10  PHE A CG   1 
ATOM   211  C  CD1  . PHE A 1 14  ? 26.34807 24.63053 -18.24455 1.000 12.33796 ? 10  PHE A CD1  1 
ATOM   212  C  CD2  . PHE A 1 14  ? 25.36410 22.75125 -17.16215 1.000 13.01248 ? 10  PHE A CD2  1 
ATOM   213  C  CE1  . PHE A 1 14  ? 25.08601 25.11290 -18.56406 1.000 13.01849 ? 10  PHE A CE1  1 
ATOM   214  C  CE2  . PHE A 1 14  ? 24.11013 23.23853 -17.45910 1.000 14.26153 ? 10  PHE A CE2  1 
ATOM   215  C  CZ   . PHE A 1 14  ? 23.97076 24.43295 -18.15340 1.000 13.10578 ? 10  PHE A CZ   1 
ATOM   216  H  H    . PHE A 1 14  ? 30.08249 22.61445 -16.16574 1.000 15.15926 ? 10  PHE A H    1 
ATOM   217  H  HA   . PHE A 1 14  ? 28.31569 24.46512 -15.88965 1.000 13.99389 ? 10  PHE A HA   1 
ATOM   218  H  HB2  . PHE A 1 14  ? 28.48537 23.24786 -17.88438 1.000 14.40923 ? 10  PHE A HB2  1 
ATOM   219  H  HB3  . PHE A 1 14  ? 27.84664 21.98763 -17.15689 1.000 14.40923 ? 10  PHE A HB3  1 
ATOM   220  H  HD1  . PHE A 1 14  ? 27.10116 25.11376 -18.49804 1.000 14.83028 ? 10  PHE A HD1  1 
ATOM   221  H  HD2  . PHE A 1 14  ? 25.44892 21.95206 -16.69418 1.000 15.63971 ? 10  PHE A HD2  1 
ATOM   222  H  HE1  . PHE A 1 14  ? 24.99821 25.89695 -19.05646 1.000 15.64692 ? 10  PHE A HE1  1 
ATOM   223  H  HE2  . PHE A 1 14  ? 23.35445 22.76590 -17.19365 1.000 17.13856 ? 10  PHE A HE2  1 
ATOM   224  H  HZ   . PHE A 1 14  ? 23.12382 24.76953 -18.33862 1.000 15.75166 ? 10  PHE A HZ   1 
ATOM   225  N  N    A VAL A 1 15  ? 27.50935 21.76868 -14.32103 0.403 12.56752 ? 11  VAL A N    1 
ATOM   226  N  N    B VAL A 1 15  ? 27.54597 21.77081 -14.34006 0.597 12.58205 ? 11  VAL A N    1 
ATOM   227  C  CA   A VAL A 1 15  ? 26.58335 21.31102 -13.28050 0.403 12.79013 ? 11  VAL A CA   1 
ATOM   228  C  CA   B VAL A 1 15  ? 26.67620 21.22055 -13.30731 0.597 14.30416 ? 11  VAL A CA   1 
ATOM   229  C  C    A VAL A 1 15  ? 26.81732 22.05917 -11.97234 0.403 12.68804 ? 11  VAL A C    1 
ATOM   230  C  C    B VAL A 1 15  ? 26.83771 21.98914 -11.99446 0.597 13.72832 ? 11  VAL A C    1 
ATOM   231  O  O    A VAL A 1 15  ? 25.86190 22.41272 -11.26493 0.403 14.26078 ? 11  VAL A O    1 
ATOM   232  O  O    B VAL A 1 15  ? 25.84895 22.27772 -11.29921 0.597 15.85659 ? 11  VAL A O    1 
ATOM   233  C  CB   A VAL A 1 15  ? 26.60429 19.77935 -13.09621 0.403 14.53447 ? 11  VAL A CB   1 
ATOM   234  C  CB   B VAL A 1 15  ? 26.94531 19.70949 -13.15649 0.597 18.38843 ? 11  VAL A CB   1 
ATOM   235  C  CG1  A VAL A 1 15  ? 26.14678 19.07806 -14.36584 0.403 16.42078 ? 11  VAL A CG1  1 
ATOM   236  C  CG1  B VAL A 1 15  ? 26.22708 19.17128 -11.99221 0.597 21.23812 ? 11  VAL A CG1  1 
ATOM   237  C  CG2  A VAL A 1 15  ? 27.96956 19.28895 -12.67807 0.403 16.55643 ? 11  VAL A CG2  1 
ATOM   238  C  CG2  B VAL A 1 15  ? 26.54160 18.93311 -14.40710 0.597 19.11165 ? 11  VAL A CG2  1 
ATOM   239  H  H    A VAL A 1 15  ? 28.06654 21.18292 -14.61434 0.403 15.10575 ? 11  VAL A H    1 
ATOM   240  H  H    B VAL A 1 15  ? 28.12097 21.21448 -14.65544 0.597 15.12318 ? 11  VAL A H    1 
ATOM   241  H  HA   A VAL A 1 15  ? 25.68956 21.52733 -13.58913 0.403 15.37288 ? 11  VAL A HA   1 
ATOM   242  H  HA   B VAL A 1 15  ? 25.75083 21.32939 -13.57702 0.597 17.18972 ? 11  VAL A HA   1 
ATOM   243  H  HB   A VAL A 1 15  ? 25.98494 19.55507 -12.38417 0.403 17.46609 ? 11  VAL A HB   1 
ATOM   244  H  HB   B VAL A 1 15  ? 27.89978 19.59469 -13.02721 0.597 22.09085 ? 11  VAL A HB   1 
ATOM   245  H  HG11 A VAL A 1 15  ? 26.03859 18.13172 -14.18243 0.403 19.72967 ? 11  VAL A HG11 1 
ATOM   246  H  HG11 B VAL A 1 15  ? 26.11889 18.21370 -12.10287 0.597 25.51047 ? 11  VAL A HG11 1 
ATOM   247  H  HG12 A VAL A 1 15  ? 25.30097 19.45880 -14.64966 0.403 19.72967 ? 11  VAL A HG12 1 
ATOM   248  H  HG12 B VAL A 1 15  ? 26.74162 19.35561 -11.19085 0.597 25.51047 ? 11  VAL A HG12 1 
ATOM   249  H  HG13 A VAL A 1 15  ? 26.81578 19.20681 -15.05633 0.403 19.72967 ? 11  VAL A HG13 1 
ATOM   250  H  HG13 B VAL A 1 15  ? 25.35787 19.59766 -11.93256 0.597 25.51047 ? 11  VAL A HG13 1 
ATOM   251  H  HG21 A VAL A 1 15  ? 27.94972 18.32173 -12.60743 0.403 19.89244 ? 11  VAL A HG21 1 
ATOM   252  H  HG21 B VAL A 1 15  ? 26.88288 18.02757 -14.34054 0.597 22.95871 ? 11  VAL A HG21 1 
ATOM   253  H  HG22 A VAL A 1 15  ? 28.61998 19.55861 -13.34525 0.403 19.89244 ? 11  VAL A HG22 1 
ATOM   254  H  HG22 B VAL A 1 15  ? 25.57381 18.91802 -14.47075 0.597 22.95871 ? 11  VAL A HG22 1 
ATOM   255  H  HG23 A VAL A 1 15  ? 28.19572 19.67877 -11.81912 0.403 19.89244 ? 11  VAL A HG23 1 
ATOM   256  H  HG23 B VAL A 1 15  ? 26.91753 19.37185 -15.18626 0.597 22.95871 ? 11  VAL A HG23 1 
ATOM   257  N  N    . GLN A 1 16  ? 28.07803 22.34805 -11.64718 1.000 13.26046 ? 12  GLN A N    1 
ATOM   258  C  CA   . GLN A 1 16  ? 28.37136 22.98209 -10.36516 1.000 13.85376 ? 12  GLN A CA   1 
ATOM   259  C  C    . GLN A 1 16  ? 28.13608 24.48253 -10.35671 1.000 13.73496 ? 12  GLN A C    1 
ATOM   260  O  O    . GLN A 1 16  ? 27.90279 25.03503 -9.28090  1.000 15.34791 ? 12  GLN A O    1 
ATOM   261  C  CB   . GLN A 1 16  ? 29.80993 22.69164 -9.92889  1.000 15.32003 ? 12  GLN A CB   1 
ATOM   262  C  CG   . GLN A 1 16  ? 30.06596 21.23943 -9.61118  1.000 16.98124 ? 12  GLN A CG   1 
ATOM   263  C  CD   . GLN A 1 16  ? 31.45567 21.00122 -9.02473  1.000 20.01930 ? 12  GLN A CD   1 
ATOM   264  O  OE1  . GLN A 1 16  ? 32.31696 21.88710 -9.02772  1.000 22.12127 ? 12  GLN A OE1  1 
ATOM   265  N  NE2  . GLN A 1 16  ? 31.68027 19.79806 -8.53986  1.000 21.70432 ? 12  GLN A NE2  1 
ATOM   266  H  H    . GLN A 1 16  ? 28.77188 22.23337 -12.14217 1.000 15.93728 ? 12  GLN A H    1 
ATOM   267  H  HA   . GLN A 1 16  ? 27.77555 22.58996 -9.70778  1.000 16.64924 ? 12  GLN A HA   1 
ATOM   268  H  HB2  . GLN A 1 16  ? 30.41114 22.94870 -10.64539 1.000 18.40876 ? 12  GLN A HB2  1 
ATOM   269  H  HB3  . GLN A 1 16  ? 30.00437 23.20824 -9.13126  1.000 18.40876 ? 12  GLN A HB3  1 
ATOM   270  H  HG2  . GLN A 1 16  ? 29.41067 20.93703 -8.96306  1.000 20.40222 ? 12  GLN A HG2  1 
ATOM   271  H  HG3  . GLN A 1 16  ? 29.99085 20.71917 -10.42640 1.000 20.40222 ? 12  GLN A HG3  1 
ATOM   272  H  HE21 . GLN A 1 16  ? 31.06129 19.20158 -8.56574  1.000 26.06991 ? 12  GLN A HE21 1 
ATOM   273  H  HE22 . GLN A 1 16  ? 32.44597 19.60858 -8.19723  1.000 26.06991 ? 12  GLN A HE22 1 
ATOM   274  N  N    . ARG A 1 17  ? 28.14073 25.15361 -11.51870 1.000 13.14860 ? 13  ARG A N    1 
ATOM   275  C  CA   . ARG A 1 17  ? 28.10508 26.60319 -11.55867 1.000 13.78896 ? 13  ARG A CA   1 
ATOM   276  C  C    . ARG A 1 17  ? 26.95138 27.18176 -12.35146 1.000 13.41020 ? 13  ARG A C    1 
ATOM   277  O  O    . ARG A 1 17  ? 26.66709 28.37168 -12.17452 1.000 15.12002 ? 13  ARG A O    1 
ATOM   278  C  CB   . ARG A 1 17  ? 29.40771 27.15041 -12.15563 1.000 14.70758 ? 13  ARG A CB   1 
ATOM   279  C  CG   . ARG A 1 17  ? 30.65789 26.74402 -11.39622 1.000 19.89326 ? 13  ARG A CG   1 
ATOM   280  C  CD   . ARG A 1 17  ? 30.79614 27.49241 -10.09723 1.000 27.52644 ? 13  ARG A CD   1 
ATOM   281  N  NE   . ARG A 1 17  ? 31.29391 28.85589 -10.29313 1.000 33.74219 ? 13  ARG A NE   1 
ATOM   282  C  CZ   . ARG A 1 17  ? 32.57755 29.18229 -10.46673 1.000 37.11941 ? 13  ARG A CZ   1 
ATOM   283  N  NH1  . ARG A 1 17  ? 33.53796 28.25297 -10.48879 1.000 39.94083 ? 13  ARG A NH1  1 
ATOM   284  N  NH2  . ARG A 1 17  ? 32.90870 30.45567 -10.62596 1.000 36.42214 ? 13  ARG A NH2  1 
ATOM   285  H  H    . ARG A 1 17  ? 28.16444 24.78020 -12.29304 1.000 15.80305 ? 13  ARG A H    1 
ATOM   286  H  HA   . ARG A 1 17  ? 28.02453 26.92487 -10.64711 1.000 16.57148 ? 13  ARG A HA   1 
ATOM   287  H  HB2  . ARG A 1 17  ? 29.49496 26.82144 -13.06396 1.000 17.67382 ? 13  ARG A HB2  1 
ATOM   288  H  HB3  . ARG A 1 17  ? 29.36560 28.11949 -12.15635 1.000 17.67382 ? 13  ARG A HB3  1 
ATOM   289  H  HG2  . ARG A 1 17  ? 30.61627 25.79573 -11.19646 1.000 23.89664 ? 13  ARG A HG2  1 
ATOM   290  H  HG3  . ARG A 1 17  ? 31.43816 26.93457 -11.94006 1.000 23.89664 ? 13  ARG A HG3  1 
ATOM   291  H  HD2  . ARG A 1 17  ? 29.92832 27.54668 -9.66728  1.000 33.05645 ? 13  ARG A HD2  1 
ATOM   292  H  HD3  . ARG A 1 17  ? 31.42155 27.02213 -9.52400  1.000 33.05645 ? 13  ARG A HD3  1 
ATOM   293  H  HE   . ARG A 1 17  ? 30.71698 29.49365 -10.29665 1.000 40.51536 ? 13  ARG A HE   1 
ATOM   294  H  HH11 . ARG A 1 17  ? 33.33556 27.42300 -10.38988 1.000 47.95373 ? 13  ARG A HH11 1 
ATOM   295  H  HH12 . ARG A 1 17  ? 34.35831 28.48500 -10.60188 1.000 47.95373 ? 13  ARG A HH12 1 
ATOM   296  H  HH21 . ARG A 1 17  ? 32.29962 31.06275 -10.61691 1.000 43.73129 ? 13  ARG A HH21 1 
ATOM   297  H  HH22 . ARG A 1 17  ? 33.73267 30.67489 -10.73832 1.000 43.73129 ? 13  ARG A HH22 1 
ATOM   298  N  N    . CYS A 1 18  ? 26.31112 26.40432 -13.22886 1.000 12.50420 ? 14  CYS A N    1 
ATOM   299  C  CA   . CYS A 1 18  ? 25.30686 26.92633 -14.15014 1.000 12.15734 ? 14  CYS A CA   1 
ATOM   300  C  C    . CYS A 1 18  ? 23.96435 26.21110 -14.09296 1.000 11.28360 ? 14  CYS A C    1 
ATOM   301  O  O    . CYS A 1 18  ? 22.92918 26.84989 -14.30898 1.000 11.75768 ? 14  CYS A O    1 
ATOM   302  C  CB   . CYS A 1 18  ? 25.84237 26.80781 -15.58796 1.000 12.95106 ? 14  CYS A CB   1 
ATOM   303  S  SG   . CYS A 1 18  ? 27.56945 27.27208 -15.85536 1.000 12.50287 ? 14  CYS A SG   1 
ATOM   304  H  H    . CYS A 1 18  ? 26.44561 25.55861 -13.30816 1.000 15.02977 ? 14  CYS A H    1 
ATOM   305  H  HA   . CYS A 1 18  ? 25.14798 27.85436 -13.91688 1.000 14.61354 ? 14  CYS A HA   1 
ATOM   306  H  HB2  . CYS A 1 18  ? 25.75130 25.88317 -15.86659 1.000 15.56600 ? 14  CYS A HB2  1 
ATOM   307  H  HB3  . CYS A 1 18  ? 25.30396 27.38023 -16.15660 1.000 15.56600 ? 14  CYS A HB3  1 
ATOM   308  N  N    . ALA A 1 19  ? 23.95876 24.89586 -13.86121 1.000 12.27780 ? 15  ALA A N    1 
ATOM   309  C  CA   . ALA A 1 19  ? 22.74618 24.09443 -13.98498 1.000 12.33259 ? 15  ALA A CA   1 
ATOM   310  C  C    . ALA A 1 19  ? 21.65817 24.51590 -13.00397 1.000 13.59833 ? 15  ALA A C    1 
ATOM   311  O  O    . ALA A 1 19  ? 20.47538 24.29563 -13.29022 1.000 14.10502 ? 15  ALA A O    1 
ATOM   312  C  CB   . ALA A 1 19  ? 23.07504 22.62479 -13.78808 1.000 13.00193 ? 15  ALA A CB   1 
ATOM   313  H  H    . ALA A 1 19  ? 24.65018 24.44021 -13.62899 1.000 14.75809 ? 15  ALA A H    1 
ATOM   314  H  HA   . ALA A 1 19  ? 22.39328 24.21158 -14.88088 1.000 14.82383 ? 15  ALA A HA   1 
ATOM   315  H  HB1  . ALA A 1 19  ? 22.25018 22.11442 -13.78375 1.000 15.62704 ? 15  ALA A HB1  1 
ATOM   316  H  HB2  . ALA A 1 19  ? 23.64371 22.32819 -14.51578 1.000 15.62704 ? 15  ALA A HB2  1 
ATOM   317  H  HB3  . ALA A 1 19  ? 23.53639 22.51503 -12.94191 1.000 15.62704 ? 15  ALA A HB3  1 
ATOM   318  N  N    . GLN A 1 20  ? 22.01195 25.14857 -11.88050 1.000 13.37799 ? 16  GLN A N    1 
ATOM   319  C  CA   A GLN A 1 20  ? 20.99587 25.67632 -10.97027 0.250 13.56891 ? 16  GLN A CA   1 
ATOM   320  C  CA   B GLN A 1 20  ? 20.98356 25.64697 -10.97835 0.750 14.54644 ? 16  GLN A CA   1 
ATOM   321  C  C    . GLN A 1 20  ? 20.01707 26.57903 -11.69674 1.000 14.57543 ? 16  GLN A C    1 
ATOM   322  O  O    . GLN A 1 20  ? 18.83583 26.64505 -11.32955 1.000 16.68574 ? 16  GLN A O    1 
ATOM   323  C  CB   A GLN A 1 20  ? 21.67906 26.50597 -9.86341  0.250 14.33287 ? 16  GLN A CB   1 
ATOM   324  C  CB   B GLN A 1 20  ? 21.60655 26.30993 -9.75283  0.750 19.59392 ? 16  GLN A CB   1 
ATOM   325  C  CG   A GLN A 1 20  ? 20.76042 27.45571 -9.01931  0.250 14.74847 ? 16  GLN A CG   1 
ATOM   326  C  CG   B GLN A 1 20  ? 22.51466 27.47728 -10.04157 0.750 20.66958 ? 16  GLN A CG   1 
ATOM   327  C  CD   A GLN A 1 20  ? 21.52233 28.51190 -8.24871  0.250 16.68401 ? 16  GLN A CD   1 
ATOM   328  C  CD   B GLN A 1 20  ? 22.67760 28.39016 -8.84970  0.750 25.11757 ? 16  GLN A CD   1 
ATOM   329  O  OE1  A GLN A 1 20  ? 22.75508 28.54282 -8.24112  0.250 15.78589 ? 16  GLN A OE1  1 
ATOM   330  O  OE1  B GLN A 1 20  ? 23.78139 28.58100 -8.34522  0.750 27.81568 ? 16  GLN A OE1  1 
ATOM   331  N  NE2  A GLN A 1 20  ? 20.77953 29.41689 -7.61673  0.250 18.95757 ? 16  GLN A NE2  1 
ATOM   332  N  NE2  B GLN A 1 20  ? 21.57272 28.96567 -8.39454  0.750 25.75175 ? 16  GLN A NE2  1 
ATOM   333  H  H    . GLN A 1 20  ? 22.81987 25.29723 -11.62602 1.000 16.07831 ? 16  GLN A H    1 
ATOM   334  H  HA   . GLN A 1 20  ? 20.51659 24.93106 -10.57558 1.000 17.48045 ? 16  GLN A HA   1 
ATOM   335  H  HB2  A GLN A 1 20  ? 22.09584 25.88954 -9.24115  0.250 17.22418 ? 16  GLN A HB2  1 
ATOM   336  H  HB2  B GLN A 1 20  ? 20.89088 26.63408 -9.18393  0.750 23.53743 ? 16  GLN A HB2  1 
ATOM   337  H  HB3  A GLN A 1 20  ? 22.35437 27.06345 -10.28063 0.250 17.22418 ? 16  GLN A HB3  1 
ATOM   338  H  HB3  B GLN A 1 20  ? 22.13135 25.64540 -9.27967  0.750 23.53743 ? 16  GLN A HB3  1 
ATOM   339  H  HG2  A GLN A 1 20  ? 20.14744 27.91061 -9.61783  0.250 17.72290 ? 16  GLN A HG2  1 
ATOM   340  H  HG2  B GLN A 1 20  ? 23.39165 27.14370 -10.28757 0.750 24.82822 ? 16  GLN A HG2  1 
ATOM   341  H  HG3  A GLN A 1 20  ? 20.26422 26.92237 -8.37882  0.250 17.72290 ? 16  GLN A HG3  1 
ATOM   342  H  HG3  B GLN A 1 20  ? 22.14106 27.99717 -10.77030 0.750 24.82822 ? 16  GLN A HG3  1 
ATOM   343  H  HE21 A GLN A 1 20  ? 19.92169 29.37701 -7.66264  0.250 22.77381 ? 16  GLN A HE21 1 
ATOM   344  H  HE21 B GLN A 1 20  ? 20.81806 28.80979 -8.77636  0.750 30.92683 ? 16  GLN A HE21 1 
ATOM   345  H  HE22 A GLN A 1 20  ? 21.15725 30.04174 -7.16232  0.250 22.77381 ? 16  GLN A HE22 1 
ATOM   346  H  HE22 B GLN A 1 20  ? 21.61097 29.49471 -7.71760  0.750 30.92683 ? 16  GLN A HE22 1 
ATOM   347  N  N    . CYS A 1 21  ? 20.49897 27.30265 -12.70117 1.000 12.50796 ? 17  CYS A N    1 
ATOM   348  C  CA   . CYS A 1 21  ? 19.69318 28.29954 -13.39170 1.000 12.39263 ? 17  CYS A CA   1 
ATOM   349  C  C    . CYS A 1 21  ? 19.41969 28.01021 -14.85671 1.000 11.93102 ? 17  CYS A C    1 
ATOM   350  O  O    . CYS A 1 21  ? 18.60295 28.72405 -15.45296 1.000 13.67567 ? 17  CYS A O    1 
ATOM   351  C  CB   . CYS A 1 21  ? 20.33245 29.68345 -13.28633 1.000 13.33851 ? 17  CYS A CB   1 
ATOM   352  S  SG   . CYS A 1 21  ? 20.45948 30.22427 -11.57080 1.000 13.76321 ? 17  CYS A SG   1 
ATOM   353  H  H    . CYS A 1 21  ? 21.30085 27.23236 -13.00391 1.000 15.03428 ? 17  CYS A H    1 
ATOM   354  H  HA   . CYS A 1 21  ? 18.83366 28.32563 -12.94287 1.000 14.89589 ? 17  CYS A HA   1 
ATOM   355  H  HB2  . CYS A 1 21  ? 21.22525 29.65355 -13.66437 1.000 16.03094 ? 17  CYS A HB2  1 
ATOM   356  H  HB3  . CYS A 1 21  ? 19.78882 30.32510 -13.76971 1.000 16.03094 ? 17  CYS A HB3  1 
ATOM   357  N  N    . HIS A 1 22  ? 20.08096 27.01422 -15.46228 1.000 11.87665 ? 18  HIS A N    1 
ATOM   358  C  CA   . HIS A 1 22  ? 20.01285 26.81034 -16.90715 1.000 11.27381 ? 18  HIS A CA   1 
ATOM   359  C  C    . HIS A 1 22  ? 19.91944 25.33341 -17.26380 1.000 11.70181 ? 18  HIS A C    1 
ATOM   360  O  O    . HIS A 1 22  ? 20.65719 24.50657 -16.72203 1.000 13.03685 ? 18  HIS A O    1 
ATOM   361  C  CB   . HIS A 1 22  ? 21.30596 27.30296 -17.56617 1.000 11.01031 ? 18  HIS A CB   1 
ATOM   362  C  CG   . HIS A 1 22  ? 21.49446 28.79226 -17.58050 1.000 11.28602 ? 18  HIS A CG   1 
ATOM   363  N  ND1  . HIS A 1 22  ? 20.77213 29.62295 -18.40143 1.000 11.75258 ? 18  HIS A ND1  1 
ATOM   364  C  CD2  . HIS A 1 22  ? 22.37572 29.59850 -16.93016 1.000 10.02229 ? 18  HIS A CD2  1 
ATOM   365  C  CE1  . HIS A 1 22  ? 21.18472 30.87079 -18.25807 1.000 10.86603 ? 18  HIS A CE1  1 
ATOM   366  N  NE2  . HIS A 1 22  ? 22.17248 30.88395 -17.38046 1.000 10.52633 ? 18  HIS A NE2  1 
ATOM   367  H  H    . HIS A 1 22  ? 20.57624 26.44412 -15.05084 1.000 14.27671 ? 18  HIS A H    1 
ATOM   368  H  HA   . HIS A 1 22  ? 19.22199 27.27030 -17.22947 1.000 13.55330 ? 18  HIS A HA   1 
ATOM   369  H  HB2  . HIS A 1 22  ? 22.05783 26.92106 -17.08685 1.000 13.23710 ? 18  HIS A HB2  1 
ATOM   370  H  HB3  . HIS A 1 22  ? 21.31285 27.00187 -18.48824 1.000 13.23710 ? 18  HIS A HB3  1 
ATOM   371  H  HD1  . HIS A 1 22  ? 20.14385 29.36888 -18.93088 1.000 14.12782 ? 18  HIS A HD1  1 
ATOM   372  H  HD2  . HIS A 1 22  ? 23.00164 29.33052 -16.29667 1.000 12.05147 ? 18  HIS A HD2  1 
ATOM   373  H  HE1  . HIS A 1 22  ? 20.83881 31.61265 -18.69953 1.000 13.06397 ? 18  HIS A HE1  1 
ATOM   374  N  N    . THR A 1 23  ? 19.07371 25.03641 -18.25250 1.000 12.44471 ? 19  THR A N    1 
ATOM   375  C  CA   . THR A 1 23  ? 19.07827 23.77664 -18.97954 1.000 12.41597 ? 19  THR A CA   1 
ATOM   376  C  C    . THR A 1 23  ? 19.69610 23.99143 -20.36999 1.000 12.64401 ? 19  THR A C    1 
ATOM   377  O  O    . THR A 1 23  ? 19.83104 25.13206 -20.83112 1.000 12.38277 ? 19  THR A O    1 
ATOM   378  C  CB   . THR A 1 23  ? 17.65162 23.22493 -19.10454 1.000 12.92115 ? 19  THR A CB   1 
ATOM   379  O  OG1  . THR A 1 23  ? 16.83296 24.13641 -19.84884 1.000 12.55666 ? 19  THR A OG1  1 
ATOM   380  C  CG2  . THR A 1 23  ? 16.99609 22.96375 -17.74373 1.000 14.35806 ? 19  THR A CG2  1 
ATOM   381  H  H    . THR A 1 23  ? 18.46379 25.57678 -18.52743 1.000 14.95838 ? 19  THR A H    1 
ATOM   382  H  HA   . THR A 1 23  ? 19.60785 23.11640 -18.50571 1.000 14.92389 ? 19  THR A HA   1 
ATOM   383  H  HB   . THR A 1 23  ? 17.70789 22.37353 -19.56588 1.000 15.53011 ? 19  THR A HB   1 
ATOM   384  H  HG1  . THR A 1 23  ? 16.62141 24.79141 -19.36737 1.000 15.09272 ? 19  THR A HG1  1 
ATOM   385  H  HG21 . THR A 1 23  ? 16.14892 22.50732 -17.86572 1.000 17.25440 ? 19  THR A HG21 1 
ATOM   386  H  HG22 . THR A 1 23  ? 17.57576 22.41068 -17.19692 1.000 17.25440 ? 19  THR A HG22 1 
ATOM   387  H  HG23 . THR A 1 23  ? 16.83795 23.80366 -17.28499 1.000 17.25440 ? 19  THR A HG23 1 
ATOM   388  N  N    . VAL A 1 24  ? 20.09373 22.88898 -21.01755 1.000 12.96391 ? 20  VAL A N    1 
ATOM   389  C  CA   . VAL A 1 24  ? 20.77265 22.94889 -22.31119 1.000 13.14546 ? 20  VAL A CA   1 
ATOM   390  C  C    . VAL A 1 24  ? 20.03734 22.23452 -23.43303 1.000 14.49738 ? 20  VAL A C    1 
ATOM   391  O  O    . VAL A 1 24  ? 20.35427 22.50101 -24.59709 1.000 15.77869 ? 20  VAL A O    1 
ATOM   392  C  CB   . VAL A 1 24  ? 22.21721 22.41318 -22.23735 1.000 13.92981 ? 20  VAL A CB   1 
ATOM   393  C  CG1  . VAL A 1 24  ? 23.05782 23.23587 -21.29105 1.000 16.36281 ? 20  VAL A CG1  1 
ATOM   394  C  CG2  . VAL A 1 24  ? 22.25369 20.92906 -21.84963 1.000 16.77302 ? 20  VAL A CG2  1 
ATOM   395  H  H    . VAL A 1 24  ? 19.97944 22.08899 -20.72334 1.000 15.58142 ? 20  VAL A H    1 
ATOM   396  H  HA   . VAL A 1 24  ? 20.81627 23.88824 -22.54917 1.000 15.79928 ? 20  VAL A HA   1 
ATOM   397  H  HB   . VAL A 1 24  ? 22.60351 22.49058 -23.12374 1.000 16.74050 ? 20  VAL A HB   1 
ATOM   398  H  HG11 . VAL A 1 24  ? 23.95851 22.87615 -21.27462 1.000 19.66010 ? 20  VAL A HG11 1 
ATOM   399  H  HG12 . VAL A 1 24  ? 23.07429 24.15491 -21.60089 1.000 19.66010 ? 20  VAL A HG12 1 
ATOM   400  H  HG13 . VAL A 1 24  ? 22.66822 23.19286 -20.40378 1.000 19.66010 ? 20  VAL A HG13 1 
ATOM   401  H  HG21 . VAL A 1 24  ? 23.17223 20.67073 -21.67513 1.000 20.15235 ? 20  VAL A HG21 1 
ATOM   402  H  HG22 . VAL A 1 24  ? 21.71604 20.79745 -21.05307 1.000 20.15235 ? 20  VAL A HG22 1 
ATOM   403  H  HG23 . VAL A 1 24  ? 21.89533 20.40262 -22.58129 1.000 20.15235 ? 20  VAL A HG23 1 
ATOM   404  N  N    . GLU A 1 25  ? 19.16367 21.28200 -23.14435 1.000 15.07826 ? 21  GLU A N    1 
ATOM   405  C  CA   . GLU A 1 25  ? 18.57238 20.45651 -24.18356 1.000 15.97606 ? 21  GLU A CA   1 
ATOM   406  C  C    . GLU A 1 25  ? 17.47139 21.20161 -24.92617 1.000 14.55011 ? 21  GLU A C    1 
ATOM   407  O  O    . GLU A 1 25  ? 16.82150 22.09707 -24.37907 1.000 14.01119 ? 21  GLU A O    1 
ATOM   408  C  CB   . GLU A 1 25  ? 18.03238 19.14169 -23.60244 1.000 21.06276 ? 21  GLU A CB   1 
ATOM   409  C  CG   . GLU A 1 25  ? 16.79887 19.22196 -22.67423 1.000 26.18938 ? 21  GLU A CG   1 
ATOM   410  C  CD   . GLU A 1 25  ? 17.09719 19.63011 -21.22121 1.000 35.28695 ? 21  GLU A CD   1 
ATOM   411  O  OE1  . GLU A 1 25  ? 18.19339 20.17223 -20.94360 1.000 40.93506 ? 21  GLU A OE1  1 
ATOM   412  O  OE2  . GLU A 1 25  ? 16.21660 19.39948 -20.35309 1.000 40.08840 ? 21  GLU A OE2  1 
ATOM   413  H  H    . GLU A 1 25  ? 18.89496 21.09241 -22.34971 1.000 18.11864 ? 21  GLU A H    1 
ATOM   414  H  HA   . GLU A 1 25  ? 19.25882 20.23163 -24.83096 1.000 19.19601 ? 21  GLU A HA   1 
ATOM   415  H  HB2  . GLU A 1 25  ? 17.78665 18.56787 -24.34490 1.000 25.30003 ? 21  GLU A HB2  1 
ATOM   416  H  HB3  . GLU A 1 25  ? 18.74389 18.73075 -23.08689 1.000 25.30003 ? 21  GLU A HB3  1 
ATOM   417  H  HG2  . GLU A 1 25  ? 16.18336 19.87730 -23.03833 1.000 31.45198 ? 21  GLU A HG2  1 
ATOM   418  H  HG3  . GLU A 1 25  ? 16.37704 18.34885 -22.64877 1.000 31.45198 ? 21  GLU A HG3  1 
ATOM   419  N  N    . ALA A 1 26  ? 17.24617 20.80138 -26.17571 1.000 14.26182 ? 22  ALA A N    1 
ATOM   420  C  CA   . ALA A 1 26  ? 16.10277 21.31376 -26.92449 1.000 14.36251 ? 22  ALA A CA   1 
ATOM   421  C  C    . ALA A 1 26  ? 14.81554 20.98754 -26.17881 1.000 13.50866 ? 22  ALA A C    1 
ATOM   422  O  O    . ALA A 1 26  ? 14.56400 19.82598 -25.82398 1.000 16.36345 ? 22  ALA A O    1 
ATOM   423  C  CB   . ALA A 1 26  ? 16.04951 20.69979 -28.32844 1.000 15.78750 ? 22  ALA A CB   1 
ATOM   424  H  H    . ALA A 1 26  ? 17.73381 20.24074 -26.60870 1.000 17.13891 ? 22  ALA A H    1 
ATOM   425  H  HA   . ALA A 1 26  ? 16.19141 22.27494 -27.02026 1.000 17.25974 ? 22  ALA A HA   1 
ATOM   426  H  HB1  . ALA A 1 26  ? 15.31357 21.09762 -28.81938 1.000 18.96973 ? 22  ALA A HB1  1 
ATOM   427  H  HB2  . ALA A 1 26  ? 16.88675 20.88000 -28.78390 1.000 18.96973 ? 22  ALA A HB2  1 
ATOM   428  H  HB3  . ALA A 1 26  ? 15.91529 19.74237 -28.24953 1.000 18.96973 ? 22  ALA A HB3  1 
ATOM   429  N  N    . GLY A 1 27  ? 13.98989 22.01131 -25.96937 1.000 14.43458 ? 23  GLY A N    1 
ATOM   430  C  CA   . GLY A 1 27  ? 12.77433 21.86220 -25.19625 1.000 16.05379 ? 23  GLY A CA   1 
ATOM   431  C  C    . GLY A 1 27  ? 12.95850 21.85753 -23.69340 1.000 16.22682 ? 23  GLY A C    1 
ATOM   432  O  O    . GLY A 1 27  ? 11.97195 21.70682 -22.96718 1.000 18.94240 ? 23  GLY A O    1 
ATOM   433  H  H    . GLY A 1 27  ? 14.11882 22.80663 -26.27011 1.000 17.34623 ? 23  GLY A H    1 
ATOM   434  H  HA2  . GLY A 1 27  ? 12.17670 22.59373 -25.41671 1.000 19.28927 ? 23  GLY A HA2  1 
ATOM   435  H  HA3  . GLY A 1 27  ? 12.35242 21.02437 -25.44311 1.000 19.28927 ? 23  GLY A HA3  1 
ATOM   436  N  N    . GLY A 1 28  ? 14.18431 22.00446 -23.20099 1.000 14.28408 ? 24  GLY A N    1 
ATOM   437  C  CA   . GLY A 1 28  ? 14.39236 22.11169 -21.77271 1.000 14.79023 ? 24  GLY A CA   1 
ATOM   438  C  C    . GLY A 1 28  ? 13.76235 23.36733 -21.20064 1.000 14.29617 ? 24  GLY A C    1 
ATOM   439  O  O    . GLY A 1 28  ? 13.56524 24.37128 -21.88347 1.000 14.89146 ? 24  GLY A O    1 
ATOM   440  H  H    . GLY A 1 28  ? 14.90445 22.04441 -23.66939 1.000 17.16563 ? 24  GLY A H    1 
ATOM   441  H  HA2  . GLY A 1 28  ? 14.00047 21.34234 -21.33065 1.000 17.77300 ? 24  GLY A HA2  1 
ATOM   442  H  HA3  . GLY A 1 28  ? 15.34393 22.13261 -21.58568 1.000 17.77300 ? 24  GLY A HA3  1 
ATOM   443  N  N    . LYS A 1 29  ? 13.41814 23.30948 -19.92646 1.000 14.62187 ? 25  LYS A N    1 
ATOM   444  C  CA   . LYS A 1 29  ? 12.64127 24.40338 -19.36043 1.000 15.59561 ? 25  LYS A CA   1 
ATOM   445  C  C    . LYS A 1 29  ? 13.50632 25.62870 -19.06519 1.000 13.52825 ? 25  LYS A C    1 
ATOM   446  O  O    . LYS A 1 29  ? 14.70105 25.52705 -18.75764 1.000 13.80401 ? 25  LYS A O    1 
ATOM   447  C  CB   . LYS A 1 29  ? 11.91835 23.96826 -18.07921 1.000 17.05462 ? 25  LYS A CB   1 
ATOM   448  C  CG   . LYS A 1 29  ? 12.81973 23.54688 -16.95125 1.000 19.28873 ? 25  LYS A CG   1 
ATOM   449  C  CD   . LYS A 1 29  ? 12.00373 23.12890 -15.74583 1.000 26.70584 ? 25  LYS A CD   1 
ATOM   450  C  CE   . LYS A 1 29  ? 12.89297 22.65632 -14.61430 1.000 34.69243 ? 25  LYS A CE   1 
ATOM   451  N  NZ   . LYS A 1 29  ? 12.09063 22.42335 -13.38486 1.000 42.09638 ? 25  LYS A NZ   1 
ATOM   452  H  H    . LYS A 1 29  ? 13.61370 22.67118 -19.38430 1.000 17.57097 ? 25  LYS A H    1 
ATOM   453  H  HA   . LYS A 1 29  ? 11.97426 24.66244 -20.01532 1.000 18.73946 ? 25  LYS A HA   1 
ATOM   454  H  HB2  . LYS A 1 29  ? 11.38321 24.71216 -17.76119 1.000 20.49028 ? 25  LYS A HB2  1 
ATOM   455  H  HB3  . LYS A 1 29  ? 11.34589 23.21436 -18.29092 1.000 20.49028 ? 25  LYS A HB3  1 
ATOM   456  H  HG2  . LYS A 1 29  ? 13.36232 22.79381 -17.23301 1.000 23.17120 ? 25  LYS A HG2  1 
ATOM   457  H  HG3  . LYS A 1 29  ? 13.38950 24.28926 -16.69606 1.000 23.17120 ? 25  LYS A HG3  1 
ATOM   458  H  HD2  . LYS A 1 29  ? 11.48451 23.88523 -15.43074 1.000 32.07174 ? 25  LYS A HD2  1 
ATOM   459  H  HD3  . LYS A 1 29  ? 11.41258 22.40102 -15.99409 1.000 32.07174 ? 25  LYS A HD3  1 
ATOM   460  H  HE2  . LYS A 1 29  ? 13.32340 21.82402 -14.86510 1.000 41.65564 ? 25  LYS A HE2  1 
ATOM   461  H  HE3  . LYS A 1 29  ? 13.56252 23.33170 -14.42335 1.000 41.65564 ? 25  LYS A HE3  1 
ATOM   462  H  HZ1  . LYS A 1 29  ? 12.62404 22.18251 -12.71436 1.000 50.54038 ? 25  LYS A HZ1  1 
ATOM   463  H  HZ2  . LYS A 1 29  ? 11.65897 23.16771 -13.15747 1.000 50.54038 ? 25  LYS A HZ2  1 
ATOM   464  H  HZ3  . LYS A 1 29  ? 11.49597 21.77670 -13.52744 1.000 50.54038 ? 25  LYS A HZ3  1 
ATOM   465  N  N    . HIS A 1 30  ? 12.89388 26.80271 -19.18244 1.000 14.77002 ? 26  HIS A N    1 
ATOM   466  C  CA   . HIS A 1 30  ? 13.44246 27.99394 -18.56473 1.000 15.16114 ? 26  HIS A CA   1 
ATOM   467  C  C    . HIS A 1 30  ? 13.35532 27.82217 -17.05769 1.000 15.25371 ? 26  HIS A C    1 
ATOM   468  O  O    . HIS A 1 30  ? 12.41537 27.21637 -16.54469 1.000 16.26180 ? 26  HIS A O    1 
ATOM   469  C  CB   . HIS A 1 30  ? 12.64533 29.23389 -18.98589 1.000 15.91795 ? 26  HIS A CB   1 
ATOM   470  C  CG   . HIS A 1 30  ? 12.65216 29.48949 -20.46524 1.000 14.50417 ? 26  HIS A CG   1 
ATOM   471  N  ND1  . HIS A 1 30  ? 13.80525 29.43867 -21.21916 1.000 13.94756 ? 26  HIS A ND1  1 
ATOM   472  C  CD2  . HIS A 1 30  ? 11.65653 29.82740 -21.31989 1.000 15.87774 ? 26  HIS A CD2  1 
ATOM   473  C  CE1  . HIS A 1 30  ? 13.51386 29.70140 -22.48227 1.000 14.00477 ? 26  HIS A CE1  1 
ATOM   474  N  NE2  . HIS A 1 30  ? 12.21779 29.95097 -22.56724 1.000 15.28433 ? 26  HIS A NE2  1 
ATOM   475  H  H    . HIS A 1 30  ? 12.16141 26.93306 -19.61384 1.000 17.74876 ? 26  HIS A H    1 
ATOM   476  H  HA   . HIS A 1 30  ? 14.36298 28.13009 -18.83859 1.000 18.21810 ? 26  HIS A HA   1 
ATOM   477  H  HB2  . HIS A 1 30  ? 11.72241 29.11877 -18.71046 1.000 19.12626 ? 26  HIS A HB2  1 
ATOM   478  H  HB3  . HIS A 1 30  ? 13.02701 30.01192 -18.55012 1.000 19.12626 ? 26  HIS A HB3  1 
ATOM   479  H  HD2  . HIS A 1 30  ? 10.76094 29.95226 -21.10257 1.000 19.07801 ? 26  HIS A HD2  1 
ATOM   480  H  HE1  . HIS A 1 30  ? 14.11730 29.70931 -23.18987 1.000 16.83046 ? 26  HIS A HE1  1 
ATOM   481  H  HE2  . HIS A 1 30  ? 11.79491 30.15725 -23.28712 1.000 18.36592 ? 26  HIS A HE2  1 
ATOM   482  N  N    . LYS A 1 31  ? 14.36204 28.33231 -16.35429 1.000 14.72697 ? 27  LYS A N    1 
ATOM   483  C  CA   . LYS A 1 31  ? 14.39825 28.35062 -14.89806 1.000 16.08608 ? 27  LYS A CA   1 
ATOM   484  C  C    . LYS A 1 31  ? 14.62632 29.80561 -14.51064 1.000 15.78983 ? 27  LYS A C    1 
ATOM   485  O  O    . LYS A 1 31  ? 14.05583 30.69689 -15.14594 1.000 16.91622 ? 27  LYS A O    1 
ATOM   486  C  CB   . LYS A 1 31  ? 15.50681 27.40501 -14.41073 1.000 16.20184 ? 27  LYS A CB   1 
ATOM   487  C  CG   . LYS A 1 31  ? 15.32137 25.96187 -14.84070 1.000 18.87932 ? 27  LYS A CG   1 
ATOM   488  C  CD   . LYS A 1 31  ? 16.55696 25.09771 -14.55524 1.000 22.83564 ? 27  LYS A CD   1 
ATOM   489  C  CE   . LYS A 1 31  ? 16.72373 24.80461 -13.10219 1.000 24.81418 ? 27  LYS A CE   1 
ATOM   490  N  NZ   . LYS A 1 31  ? 17.72699 23.72670 -12.96690 1.000 23.76827 ? 27  LYS A NZ   1 
ATOM   491  H  H    . LYS A 1 31  ? 15.06037 28.68621 -16.71022 1.000 17.69710 ? 27  LYS A H    1 
ATOM   492  H  HA   . LYS A 1 31  ? 13.58599 28.03320 -14.47335 1.000 19.32803 ? 27  LYS A HA   1 
ATOM   493  H  HB2  . LYS A 1 31  ? 16.35553 27.71195 -14.76622 1.000 19.46694 ? 27  LYS A HB2  1 
ATOM   494  H  HB3  . LYS A 1 31  ? 15.52704 27.42360 -13.44112 1.000 19.46694 ? 27  LYS A HB3  1 
ATOM   495  H  HG2  . LYS A 1 31  ? 14.57091 25.58122 -14.35820 1.000 22.67991 ? 27  LYS A HG2  1 
ATOM   496  H  HG3  . LYS A 1 31  ? 15.15024 25.93489 -15.79511 1.000 22.67991 ? 27  LYS A HG3  1 
ATOM   497  H  HD2  . LYS A 1 31  ? 16.46927 24.25323 -15.02434 1.000 27.42749 ? 27  LYS A HD2  1 
ATOM   498  H  HD3  . LYS A 1 31  ? 17.34962 25.56608 -14.86056 1.000 27.42749 ? 27  LYS A HD3  1 
ATOM   499  H  HE2  . LYS A 1 31  ? 17.03825 25.59465 -12.63549 1.000 29.80174 ? 27  LYS A HE2  1 
ATOM   500  H  HE3  . LYS A 1 31  ? 15.88215 24.50775 -12.72204 1.000 29.80174 ? 27  LYS A HE3  1 
ATOM   501  H  HZ1  . LYS A 1 31  ? 17.85919 23.54010 -12.10678 1.000 28.54665 ? 27  LYS A HZ1  1 
ATOM   502  H  HZ2  . LYS A 1 31  ? 17.44248 22.99228 -13.38137 1.000 28.54665 ? 27  LYS A HZ2  1 
ATOM   503  H  HZ3  . LYS A 1 31  ? 18.49885 23.98206 -13.32900 1.000 28.54665 ? 27  LYS A HZ3  1 
ATOM   504  N  N    . VAL A 1 32  ? 15.45257 30.09115 -13.50371 1.000 16.16016 ? 28  VAL A N    1 
ATOM   505  C  CA   . VAL A 1 32  ? 15.81083 31.48675 -13.26328 1.000 14.69183 ? 28  VAL A CA   1 
ATOM   506  C  C    . VAL A 1 32  ? 16.46218 32.07673 -14.51112 1.000 14.40269 ? 28  VAL A C    1 
ATOM   507  O  O    . VAL A 1 32  ? 16.24225 33.24976 -14.84395 1.000 15.57151 ? 28  VAL A O    1 
ATOM   508  C  CB   . VAL A 1 32  ? 16.69405 31.62647 -12.00203 1.000 16.31105 ? 28  VAL A CB   1 
ATOM   509  C  CG1  . VAL A 1 32  ? 17.35214 32.99505 -11.92866 1.000 17.87999 ? 28  VAL A CG1  1 
ATOM   510  C  CG2  . VAL A 1 32  ? 15.87217 31.40510 -10.72536 1.000 19.04377 ? 28  VAL A CG2  1 
ATOM   511  H  H    . VAL A 1 32  ? 15.80571 29.52001 -12.96641 1.000 19.41692 ? 28  VAL A H    1 
ATOM   512  H  HA   . VAL A 1 32  ? 15.00147 31.99096 -13.08551 1.000 17.65493 ? 28  VAL A HA   1 
ATOM   513  H  HB   . VAL A 1 32  ? 17.38524 30.94857 -12.06212 1.000 19.59799 ? 28  VAL A HB   1 
ATOM   514  H  HG11 . VAL A 1 32  ? 17.64089 33.15817 -11.01712 1.000 21.48071 ? 28  VAL A HG11 1 
ATOM   515  H  HG12 . VAL A 1 32  ? 18.11661 33.01028 -12.52553 1.000 21.48071 ? 28  VAL A HG12 1 
ATOM   516  H  HG13 . VAL A 1 32  ? 16.70901 33.66955 -12.19762 1.000 21.48071 ? 28  VAL A HG13 1 
ATOM   517  H  HG21 . VAL A 1 32  ? 16.46614 31.43108 -9.95892  1.000 22.87726 ? 28  VAL A HG21 1 
ATOM   518  H  HG22 . VAL A 1 32  ? 15.20697 32.10729 -10.65228 1.000 22.87726 ? 28  VAL A HG22 1 
ATOM   519  H  HG23 . VAL A 1 32  ? 15.43593 30.54025 -10.77660 1.000 22.87726 ? 28  VAL A HG23 1 
ATOM   520  N  N    . GLY A 1 33  ? 17.28298 31.28166 -15.20283 1.000 12.88824 ? 29  GLY A N    1 
ATOM   521  C  CA   . GLY A 1 33  ? 17.84522 31.67662 -16.46668 1.000 13.17052 ? 29  GLY A CA   1 
ATOM   522  C  C    . GLY A 1 33  ? 17.21615 30.95304 -17.64903 1.000 12.47994 ? 29  GLY A C    1 
ATOM   523  O  O    . GLY A 1 33  ? 16.53103 29.93343 -17.49284 1.000 12.70696 ? 29  GLY A O    1 
ATOM   524  H  H    . GLY A 1 33  ? 17.52531 30.49773 -14.94527 1.000 15.49062 ? 29  GLY A H    1 
ATOM   525  H  HA2  . GLY A 1 33  ? 17.71411 32.62977 -16.59000 1.000 15.82935 ? 29  GLY A HA2  1 
ATOM   526  H  HA3  . GLY A 1 33  ? 18.79634 31.48616 -16.46594 1.000 15.82935 ? 29  GLY A HA3  1 
ATOM   527  N  N    . PRO A 1 34  ? 17.49902 31.42299 -18.86563 1.000 12.05947 ? 30  PRO A N    1 
ATOM   528  C  CA   . PRO A 1 34  ? 16.89566 30.81140 -20.05776 1.000 12.24607 ? 30  PRO A CA   1 
ATOM   529  C  C    . PRO A 1 34  ? 17.52341 29.46472 -20.40967 1.000 11.83839 ? 30  PRO A C    1 
ATOM   530  O  O    . PRO A 1 34  ? 18.72420 29.23694 -20.22261 1.000 12.11590 ? 30  PRO A O    1 
ATOM   531  C  CB   . PRO A 1 34  ? 17.19755 31.82212 -21.17438 1.000 11.95787 ? 30  PRO A CB   1 
ATOM   532  C  CG   . PRO A 1 34  ? 18.46435 32.54686 -20.68845 1.000 13.04156 ? 30  PRO A CG   1 
ATOM   533  C  CD   . PRO A 1 34  ? 18.23170 32.65750 -19.19883 1.000 13.11157 ? 30  PRO A CD   1 
ATOM   534  H  HA   . PRO A 1 34  ? 15.94051 30.71114 -19.92162 1.000 14.72001 ? 30  PRO A HA   1 
ATOM   535  H  HB2  . PRO A 1 34  ? 17.35814 31.35787 -22.01080 1.000 14.37417 ? 30  PRO A HB2  1 
ATOM   536  H  HB3  . PRO A 1 34  ? 16.45670 32.44013 -21.27490 1.000 14.37417 ? 30  PRO A HB3  1 
ATOM   537  H  HG2  . PRO A 1 34  ? 19.25450 32.02018 -20.88638 1.000 15.67460 ? 30  PRO A HG2  1 
ATOM   538  H  HG3  . PRO A 1 34  ? 18.53602 33.42105 -21.10264 1.000 15.67460 ? 30  PRO A HG3  1 
ATOM   539  H  HD2  . PRO A 1 34  ? 19.07521 32.69570 -18.72141 1.000 15.75861 ? 30  PRO A HD2  1 
ATOM   540  H  HD3  . PRO A 1 34  ? 17.69760 33.44031 -18.99187 1.000 15.75861 ? 30  PRO A HD3  1 
ATOM   541  N  N    . ASN A 1 35  ? 16.70241 28.58021 -20.97437 1.000 12.29571 ? 31  ASN A N    1 
ATOM   542  C  CA   . ASN A 1 35  ? 17.23237 27.42593 -21.67670 1.000 10.87292 ? 31  ASN A CA   1 
ATOM   543  C  C    . ASN A 1 35  ? 18.24322 27.88857 -22.72022 1.000 11.52918 ? 31  ASN A C    1 
ATOM   544  O  O    . ASN A 1 35  ? 18.05242 28.91563 -23.37805 1.000 12.34569 ? 31  ASN A O    1 
ATOM   545  C  CB   . ASN A 1 35  ? 16.08042 26.66181 -22.34358 1.000 11.91533 ? 31  ASN A CB   1 
ATOM   546  C  CG   . ASN A 1 35  ? 16.58137 25.58069 -23.26806 1.000 12.13085 ? 31  ASN A CG   1 
ATOM   547  O  OD1  . ASN A 1 35  ? 16.66513 25.78950 -24.47094 1.000 12.70739 ? 31  ASN A OD1  1 
ATOM   548  N  ND2  . ASN A 1 35  ? 16.94025 24.43079 -22.72218 1.000 13.46889 ? 31  ASN A ND2  1 
ATOM   549  H  H    . ASN A 1 35  ? 15.84383 28.62828 -20.96321 1.000 14.77958 ? 31  ASN A H    1 
ATOM   550  H  HA   . ASN A 1 35  ? 17.67673 26.82256 -21.06075 1.000 13.07223 ? 31  ASN A HA   1 
ATOM   551  H  HB2  . ASN A 1 35  ? 15.53435 26.24585 -21.65824 1.000 14.32313 ? 31  ASN A HB2  1 
ATOM   552  H  HB3  . ASN A 1 35  ? 15.54513 27.28150 -22.86353 1.000 14.32313 ? 31  ASN A HB3  1 
ATOM   553  H  HD21 . ASN A 1 35  ? 17.23080 23.79134 -23.21845 1.000 16.18739 ? 31  ASN A HD21 1 
ATOM   554  H  HD22 . ASN A 1 35  ? 16.88308 24.32249 -21.87095 1.000 16.18739 ? 31  ASN A HD22 1 
ATOM   555  N  N    . LEU A 1 36  ? 19.35527 27.15671 -22.82603 1.000 10.97580 ? 32  LEU A N    1 
ATOM   556  C  CA   . LEU A 1 36  ? 20.48561 27.55291 -23.65864 1.000 10.99144 ? 32  LEU A CA   1 
ATOM   557  C  C    . LEU A 1 36  ? 20.58281 26.77627 -24.96981 1.000 11.39410 ? 32  LEU A C    1 
ATOM   558  O  O    . LEU A 1 36  ? 21.56653 26.94546 -25.70727 1.000 11.78755 ? 32  LEU A O    1 
ATOM   559  C  CB   . LEU A 1 36  ? 21.79412 27.41246 -22.87700 1.000 11.00832 ? 32  LEU A CB   1 
ATOM   560  C  CG   . LEU A 1 36  ? 21.93926 28.28415 -21.62527 1.000 10.91054 ? 32  LEU A CG   1 
ATOM   561  C  CD1  . LEU A 1 36  ? 23.20276 27.91831 -20.86615 1.000 13.40651 ? 32  LEU A CD1  1 
ATOM   562  C  CD2  . LEU A 1 36  ? 21.92549 29.76018 -21.95546 1.000 13.56345 ? 32  LEU A CD2  1 
ATOM   563  H  H    . LEU A 1 36  ? 19.47652 26.41144 -22.41435 1.000 13.19568 ? 32  LEU A H    1 
ATOM   564  H  HA   . LEU A 1 36  ? 20.36583 28.48782 -23.88777 1.000 13.21446 ? 32  LEU A HA   1 
ATOM   565  H  HB2  . LEU A 1 36  ? 21.87643 26.48884 -22.59233 1.000 13.23472 ? 32  LEU A HB2  1 
ATOM   566  H  HB3  . LEU A 1 36  ? 22.52533 27.64290 -23.47124 1.000 13.23472 ? 32  LEU A HB3  1 
ATOM   567  H  HG   . LEU A 1 36  ? 21.17424 28.11555 -21.05324 1.000 13.11738 ? 32  LEU A HG   1 
ATOM   568  H  HD11 . LEU A 1 36  ? 23.28855 28.50172 -20.09597 1.000 16.11254 ? 32  LEU A HD11 1 
ATOM   569  H  HD12 . LEU A 1 36  ? 23.14075 26.99473 -20.57623 1.000 16.11254 ? 32  LEU A HD12 1 
ATOM   570  H  HD13 . LEU A 1 36  ? 23.96718 28.03027 -21.45270 1.000 16.11254 ? 32  LEU A HD13 1 
ATOM   571  H  HD21 . LEU A 1 36  ? 22.10359 30.26624 -21.14732 1.000 16.30086 ? 32  LEU A HD21 1 
ATOM   572  H  HD22 . LEU A 1 36  ? 22.61075 29.94211 -22.61744 1.000 16.30086 ? 32  LEU A HD22 1 
ATOM   573  H  HD23 . LEU A 1 36  ? 21.05350 29.99670 -22.30843 1.000 16.30086 ? 32  LEU A HD23 1 
ATOM   574  N  N    . HIS A 1 37  ? 19.59276 25.95243 -25.30013 1.000 12.27335 ? 33  HIS A N    1 
ATOM   575  C  CA   . HIS A 1 37  ? 19.69486 25.21787 -26.54153 1.000 12.35270 ? 33  HIS A CA   1 
ATOM   576  C  C    . HIS A 1 37  ? 19.72162 26.16833 -27.73612 1.000 12.74300 ? 33  HIS A C    1 
ATOM   577  O  O    . HIS A 1 37  ? 18.95370 27.13041 -27.79834 1.000 13.75073 ? 33  HIS A O    1 
ATOM   578  C  CB   . HIS A 1 37  ? 18.51918 24.26728 -26.71351 1.000 12.91319 ? 33  HIS A CB   1 
ATOM   579  C  CG   . HIS A 1 37  ? 18.63339 23.50623 -27.97953 1.000 14.05455 ? 33  HIS A CG   1 
ATOM   580  N  ND1  . HIS A 1 37  ? 17.94107 23.84535 -29.12220 1.000 15.20123 ? 33  HIS A ND1  1 
ATOM   581  C  CD2  . HIS A 1 37  ? 19.48879 22.51759 -28.32643 1.000 15.55143 ? 33  HIS A CD2  1 
ATOM   582  C  CE1  . HIS A 1 37  ? 18.33690 23.05972 -30.11091 1.000 16.12687 ? 33  HIS A CE1  1 
ATOM   583  N  NE2  . HIS A 1 37  ? 19.27802 22.24922 -29.65303 1.000 15.36741 ? 33  HIS A NE2  1 
ATOM   584  H  H    . HIS A 1 37  ? 18.88143 25.80971 -24.83835 1.000 14.75274 ? 33  HIS A H    1 
ATOM   585  H  HA   . HIS A 1 37  ? 20.51657 24.70302 -26.51643 1.000 14.84797 ? 33  HIS A HA   1 
ATOM   586  H  HB2  . HIS A 1 37  ? 18.50312 23.63735 -25.97606 1.000 15.52056 ? 33  HIS A HB2  1 
ATOM   587  H  HB3  . HIS A 1 37  ? 17.69341 24.77581 -26.73348 1.000 15.52056 ? 33  HIS A HB3  1 
ATOM   588  H  HD2  . HIS A 1 37  ? 20.10431 22.09879 -27.76907 1.000 18.68644 ? 33  HIS A HD2  1 
ATOM   589  H  HE1  . HIS A 1 37  ? 18.00900 23.07457 -30.98107 1.000 19.37697 ? 33  HIS A HE1  1 
ATOM   590  H  HE2  . HIS A 1 37  ? 19.69019 21.65126 -30.11364 1.000 18.46562 ? 33  HIS A HE2  1 
ATOM   591  N  N    . GLY A 1 38  ? 20.62465 25.90258 -28.68752 1.000 11.69767 ? 34  GLY A N    1 
ATOM   592  C  CA   . GLY A 1 38  ? 20.76533 26.74216 -29.86740 1.000 13.08665 ? 34  GLY A CA   1 
ATOM   593  C  C    . GLY A 1 38  ? 21.52024 28.03740 -29.65734 1.000 13.29935 ? 34  GLY A C    1 
ATOM   594  O  O    . GLY A 1 38  ? 21.44854 28.93784 -30.50224 1.000 14.54644 ? 34  GLY A O    1 
ATOM   595  H  H    . GLY A 1 38  ? 21.16868 25.23679 -28.66850 1.000 14.06193 ? 34  GLY A H    1 
ATOM   596  H  HA2  . GLY A 1 38  ? 21.23326 26.23748 -30.55095 1.000 15.72871 ? 34  GLY A HA2  1 
ATOM   597  H  HA3  . GLY A 1 38  ? 19.87977 26.96819 -30.19237 1.000 15.72871 ? 34  GLY A HA3  1 
ATOM   598  N  N    . LEU A 1 39  ? 22.27862 28.14201 -28.56835 1.000 12.04519 ? 35  LEU A N    1 
ATOM   599  C  CA   . LEU A 1 39  ? 22.93204 29.39054 -28.20402 1.000 11.42269 ? 35  LEU A CA   1 
ATOM   600  C  C    . LEU A 1 39  ? 23.91710 29.87654 -29.26742 1.000 11.88357 ? 35  LEU A C    1 
ATOM   601  O  O    . LEU A 1 39  ? 23.97041 31.08024 -29.55766 1.000 12.69900 ? 35  LEU A O    1 
ATOM   602  C  CB   . LEU A 1 39  ? 23.65816 29.16309 -26.88540 1.000 14.96986 ? 35  LEU A CB   1 
ATOM   603  C  CG   . LEU A 1 39  ? 24.35203 30.34534 -26.22145 1.000 16.66083 ? 35  LEU A CG   1 
ATOM   604  C  CD1  . LEU A 1 39  ? 23.31450 31.34900 -25.70550 1.000 19.41873 ? 35  LEU A CD1  1 
ATOM   605  C  CD2  . LEU A 1 39  ? 25.26077 29.87582 -25.10741 1.000 18.38849 ? 35  LEU A CD2  1 
ATOM   606  H  H    . LEU A 1 39  ? 22.43253 27.49910 -28.01828 1.000 14.47896 ? 35  LEU A H    1 
ATOM   607  H  HA   . LEU A 1 39  ? 22.26022 30.08420 -28.11234 1.000 13.73196 ? 35  LEU A HA   1 
ATOM   608  H  HB2  . LEU A 1 39  ? 23.00751 28.83113 -26.24716 1.000 17.98857 ? 35  LEU A HB2  1 
ATOM   609  H  HB3  . LEU A 1 39  ? 24.34236 28.49324 -27.04050 1.000 17.98857 ? 35  LEU A HB3  1 
ATOM   610  H  HG   . LEU A 1 39  ? 24.90598 30.79978 -26.87530 1.000 20.01773 ? 35  LEU A HG   1 
ATOM   611  H  HD11 . LEU A 1 39  ? 23.77451 32.07949 -25.26317 1.000 23.32721 ? 35  LEU A HD11 1 
ATOM   612  H  HD12 . LEU A 1 39  ? 22.80177 31.68724 -26.45624 1.000 23.32721 ? 35  LEU A HD12 1 
ATOM   613  H  HD13 . LEU A 1 39  ? 22.72601 30.90054 -25.07824 1.000 23.32721 ? 35  LEU A HD13 1 
ATOM   614  H  HD21 . LEU A 1 39  ? 25.71822 30.64273 -24.72862 1.000 22.09092 ? 35  LEU A HD21 1 
ATOM   615  H  HD22 . LEU A 1 39  ? 24.72560 29.44002 -24.42581 1.000 22.09092 ? 35  LEU A HD22 1 
ATOM   616  H  HD23 . LEU A 1 39  ? 25.90773 29.25059 -25.46994 1.000 22.09092 ? 35  LEU A HD23 1 
ATOM   617  N  N    . PHE A 1 40  ? 24.79841 28.99870 -29.75938 1.000 12.14326 ? 36  PHE A N    1 
ATOM   618  C  CA   . PHE A 1 40  ? 25.88796 29.46790 -30.61227 1.000 12.82736 ? 36  PHE A CA   1 
ATOM   619  C  C    . PHE A 1 40  ? 25.33377 29.92562 -31.95953 1.000 12.34004 ? 36  PHE A C    1 
ATOM   620  O  O    . PHE A 1 40  ? 24.50403 29.24934 -32.58109 1.000 14.53243 ? 36  PHE A O    1 
ATOM   621  C  CB   . PHE A 1 40  ? 26.94445 28.37389 -30.83195 1.000 13.38585 ? 36  PHE A CB   1 
ATOM   622  C  CG   . PHE A 1 40  ? 27.89812 28.17183 -29.67262 1.000 13.64918 ? 36  PHE A CG   1 
ATOM   623  C  CD1  . PHE A 1 40  ? 27.43254 27.77339 -28.42625 1.000 13.70544 ? 36  PHE A CD1  1 
ATOM   624  C  CD2  . PHE A 1 40  ? 29.25643 28.35052 -29.84631 1.000 14.87981 ? 36  PHE A CD2  1 
ATOM   625  C  CE1  . PHE A 1 40  ? 28.30456 27.57928 -27.37530 1.000 14.82078 ? 36  PHE A CE1  1 
ATOM   626  C  CE2  . PHE A 1 40  ? 30.13376 28.15806 -28.79150 1.000 15.44317 ? 36  PHE A CE2  1 
ATOM   627  C  CZ   . PHE A 1 40  ? 29.65537 27.76292 -27.54932 1.000 15.91481 ? 36  PHE A CZ   1 
ATOM   628  H  H    . PHE A 1 40  ? 24.78640 28.15061 -29.61730 1.000 14.59664 ? 36  PHE A H    1 
ATOM   629  H  HA   . PHE A 1 40  ? 26.32432 30.21385 -30.17175 1.000 15.41755 ? 36  PHE A HA   1 
ATOM   630  H  HB2  . PHE A 1 40  ? 26.48846 27.53155 -30.98500 1.000 16.08775 ? 36  PHE A HB2  1 
ATOM   631  H  HB3  . PHE A 1 40  ? 27.47525 28.60975 -31.60882 1.000 16.08775 ? 36  PHE A HB3  1 
ATOM   632  H  HD1  . PHE A 1 40  ? 26.52167 27.63578 -28.29869 1.000 16.47126 ? 36  PHE A HD1  1 
ATOM   633  H  HD2  . PHE A 1 40  ? 29.58525 28.60236 -30.67899 1.000 17.88050 ? 36  PHE A HD2  1 
ATOM   634  H  HE1  . PHE A 1 40  ? 27.97639 27.32255 -26.54386 1.000 17.80967 ? 36  PHE A HE1  1 
ATOM   635  H  HE2  . PHE A 1 40  ? 31.04537 28.29386 -28.91572 1.000 18.55653 ? 36  PHE A HE2  1 
ATOM   636  H  HZ   . PHE A 1 40  ? 30.24318 27.62392 -26.84217 1.000 19.12250 ? 36  PHE A HZ   1 
ATOM   637  N  N    . GLY A 1 41  ? 25.77973 31.09896 -32.40028 1.000 12.52300 ? 37  GLY A N    1 
ATOM   638  C  CA   . GLY A 1 41  ? 25.32823 31.65972 -33.66218 1.000 13.02848 ? 37  GLY A CA   1 
ATOM   639  C  C    . GLY A 1 41  ? 24.07941 32.49576 -33.57277 1.000 15.60207 ? 37  GLY A C    1 
ATOM   640  O  O    . GLY A 1 41  ? 23.60290 32.99421 -34.60311 1.000 17.49348 ? 37  GLY A O    1 
ATOM   641  H  H    . GLY A 1 41  ? 26.34796 31.58959 -31.98076 1.000 15.05233 ? 37  GLY A H    1 
ATOM   642  H  HA2  . GLY A 1 41  ? 26.03351 32.21917 -34.02341 1.000 15.65891 ? 37  GLY A HA2  1 
ATOM   643  H  HA3  . GLY A 1 41  ? 25.15393 30.93279 -34.28032 1.000 15.65891 ? 37  GLY A HA3  1 
ATOM   644  N  N    . ARG A 1 42  ? 23.51411 32.63536 -32.39005 1.000 14.44403 ? 38  ARG A N    1 
ATOM   645  C  CA   . ARG A 1 42  ? 22.29614 33.38525 -32.17685 1.000 14.42245 ? 38  ARG A CA   1 
ATOM   646  C  C    . ARG A 1 42  ? 22.61193 34.62963 -31.34676 1.000 12.89933 ? 38  ARG A C    1 
ATOM   647  O  O    . ARG A 1 42  ? 23.54615 34.64694 -30.53147 1.000 13.51626 ? 38  ARG A O    1 
ATOM   648  C  CB   . ARG A 1 42  ? 21.25721 32.47354 -31.51857 1.000 17.60495 ? 38  ARG A CB   1 
ATOM   649  C  CG   . ARG A 1 42  ? 19.84855 33.02949 -31.40558 1.000 16.46591 ? 38  ARG A CG   1 
ATOM   650  C  CD   . ARG A 1 42  ? 18.93745 32.02955 -30.70509 1.000 15.66712 ? 38  ARG A CD   1 
ATOM   651  N  NE   . ARG A 1 42  ? 19.31464 31.92345 -29.30606 1.000 16.61249 ? 38  ARG A NE   1 
ATOM   652  C  CZ   . ARG A 1 42  ? 18.98356 30.93638 -28.50223 1.000 16.21491 ? 38  ARG A CZ   1 
ATOM   653  N  NH1  . ARG A 1 42  ? 18.25818 29.91305 -28.92931 1.000 20.48517 ? 38  ARG A NH1  1 
ATOM   654  N  NH2  . ARG A 1 42  ? 19.40305 30.98513 -27.25127 1.000 17.45368 ? 38  ARG A NH2  1 
ATOM   655  H  H    . ARG A 1 42  ? 23.83187 32.29038 -31.66921 1.000 17.35756 ? 38  ARG A H    1 
ATOM   656  H  HA   . ARG A 1 42  ? 21.90745 33.70847 -33.00470 1.000 17.33167 ? 38  ARG A HA   1 
ATOM   657  H  HB2  . ARG A 1 42  ? 21.20039 31.65639 -32.03812 1.000 21.15067 ? 38  ARG A HB2  1 
ATOM   658  H  HB3  . ARG A 1 42  ? 21.55803 32.27401 -30.61825 1.000 21.15067 ? 38  ARG A HB3  1 
ATOM   659  H  HG2  . ARG A 1 42  ? 19.86300 33.85002 -30.88845 1.000 19.78382 ? 38  ARG A HG2  1 
ATOM   660  H  HG3  . ARG A 1 42  ? 19.49476 33.20224 -32.29209 1.000 19.78382 ? 38  ARG A HG3  1 
ATOM   661  H  HD2  . ARG A 1 42  ? 18.01685 32.33033 -30.75914 1.000 18.82527 ? 38  ARG A HD2  1 
ATOM   662  H  HD3  . ARG A 1 42  ? 19.02645 31.15743 -31.12028 1.000 18.82527 ? 38  ARG A HD3  1 
ATOM   663  H  HE   . ARG A 1 42  ? 19.79327 32.55754 -28.97674 1.000 19.95972 ? 38  ARG A HE   1 
ATOM   664  N  N    . LYS A 1 43  ? 21.84979 35.68991 -31.59607 1.000 12.72667 ? 39  LYS A N    1 
ATOM   665  C  CA   . LYS A 1 43  ? 22.02660 36.94063 -30.88495 1.000 12.31414 ? 39  LYS A CA   1 
ATOM   666  C  C    . LYS A 1 43  ? 21.59309 36.79872 -29.42715 1.000 12.90322 ? 39  LYS A C    1 
ATOM   667  O  O    . LYS A 1 43  ? 20.90810 35.84723 -29.05454 1.000 13.50772 ? 39  LYS A O    1 
ATOM   668  C  CB   . LYS A 1 43  ? 21.29019 38.08372 -31.59515 1.000 16.49491 ? 39  LYS A CB   1 
ATOM   669  C  CG   . LYS A 1 43  ? 21.96082 38.43614 -32.91858 1.000 22.58470 ? 39  LYS A CG   1 
ATOM   670  C  CD   . LYS A 1 43  ? 21.39644 39.66153 -33.57639 1.000 30.66217 ? 39  LYS A CD   1 
ATOM   671  C  CE   . LYS A 1 43  ? 22.28322 40.08929 -34.75236 1.000 33.07852 ? 39  LYS A CE   1 
ATOM   672  N  NZ   . LYS A 1 43  ? 22.57447 38.96328 -35.68869 1.000 36.01402 ? 39  LYS A NZ   1 
ATOM   673  H  H    . LYS A 1 43  ? 21.21758 35.70816 -32.17880 1.000 15.29673 ? 39  LYS A H    1 
ATOM   674  H  HA   . LYS A 1 43  ? 22.96574 37.18321 -30.87666 1.000 14.80169 ? 39  LYS A HA   1 
ATOM   675  H  HB2  . LYS A 1 43  ? 20.37648 37.81347 -31.77681 1.000 19.81862 ? 39  LYS A HB2  1 
ATOM   676  H  HB3  . LYS A 1 43  ? 21.29687 38.87116 -31.02877 1.000 19.81862 ? 39  LYS A HB3  1 
ATOM   677  H  HG2  . LYS A 1 43  ? 22.90414 38.59531 -32.75822 1.000 27.12637 ? 39  LYS A HG2  1 
ATOM   678  H  HG3  . LYS A 1 43  ? 21.84937 37.69370 -33.53280 1.000 27.12637 ? 39  LYS A HG3  1 
ATOM   679  H  HD2  . LYS A 1 43  ? 20.50672 39.47070 -33.91237 1.000 36.81933 ? 39  LYS A HD2  1 
ATOM   680  H  HD3  . LYS A 1 43  ? 21.36006 40.38836 -32.93507 1.000 36.81933 ? 39  LYS A HD3  1 
ATOM   681  H  HE2  . LYS A 1 43  ? 21.83185 40.78714 -35.25253 1.000 39.71895 ? 39  LYS A HE2  1 
ATOM   682  H  HE3  . LYS A 1 43  ? 23.12763 40.42062 -34.40871 1.000 39.71895 ? 39  LYS A HE3  1 
ATOM   683  H  HZ1  . LYS A 1 43  ? 22.96342 39.27379 -36.42653 1.000 43.24155 ? 39  LYS A HZ1  1 
ATOM   684  H  HZ2  . LYS A 1 43  ? 23.11956 38.37710 -35.29963 1.000 43.24155 ? 39  LYS A HZ2  1 
ATOM   685  H  HZ3  . LYS A 1 43  ? 21.81855 38.55029 -35.91258 1.000 43.24155 ? 39  LYS A HZ3  1 
ATOM   686  N  N    . THR A 1 44  ? 22.00984 37.76015 -28.60173 1.000 12.72511 ? 40  THR A N    1 
ATOM   687  C  CA   . THR A 1 44  ? 21.57776 37.77648 -27.21159 1.000 12.46058 ? 40  THR A CA   1 
ATOM   688  C  C    . THR A 1 44  ? 20.06870 37.97356 -27.11274 1.000 12.31969 ? 40  THR A C    1 
ATOM   689  O  O    . THR A 1 44  ? 19.44443 38.61992 -27.95479 1.000 13.08847 ? 40  THR A O    1 
ATOM   690  C  CB   . THR A 1 44  ? 22.25313 38.92131 -26.43340 1.000 13.48302 ? 40  THR A CB   1 
ATOM   691  O  OG1  . THR A 1 44  ? 21.82583 40.20285 -26.92348 1.000 15.35064 ? 40  THR A OG1  1 
ATOM   692  C  CG2  . THR A 1 44  ? 23.77518 38.83447 -26.47426 1.000 14.60272 ? 40  THR A CG2  1 
ATOM   693  H  H    . THR A 1 44  ? 22.53558 38.40462 -28.82050 1.000 15.29486 ? 40  THR A H    1 
ATOM   694  H  HA   . THR A 1 44  ? 21.82596 36.92762 -26.81318 1.000 14.97743 ? 40  THR A HA   1 
ATOM   695  H  HB   . THR A 1 44  ? 21.98492 38.83624 -25.50511 1.000 16.20435 ? 40  THR A HB   1 
ATOM   696  H  HG1  . THR A 1 44  ? 22.12926 40.81368 -26.43317 1.000 18.44550 ? 40  THR A HG1  1 
ATOM   697  H  HG21 . THR A 1 44  ? 24.16105 39.48598 -25.86800 1.000 17.54800 ? 40  THR A HG21 1 
ATOM   698  H  HG22 . THR A 1 44  ? 24.06413 37.94744 -26.20860 1.000 17.54800 ? 40  THR A HG22 1 
ATOM   699  H  HG23 . THR A 1 44  ? 24.09368 39.01334 -27.37285 1.000 17.54800 ? 40  THR A HG23 1 
ATOM   700  N  N    . GLY A 1 45  ? 19.47649 37.41320 -26.06051 1.000 13.09859 ? 41  GLY A N    1 
ATOM   701  C  CA   . GLY A 1 45  ? 18.09948 37.73876 -25.76022 1.000 13.81289 ? 41  GLY A CA   1 
ATOM   702  C  C    . GLY A 1 45  ? 17.03429 37.10074 -26.62231 1.000 14.71762 ? 41  GLY A C    1 
ATOM   703  O  O    . GLY A 1 45  ? 15.91833 37.63450 -26.69730 1.000 16.28108 ? 41  GLY A O    1 
ATOM   704  H  H    . GLY A 1 45  ? 19.84611 36.85505 -25.52065 1.000 15.74303 ? 41  GLY A H    1 
ATOM   705  H  HA2  . GLY A 1 45  ? 17.92056 37.47553 -24.84393 1.000 16.60020 ? 41  GLY A HA2  1 
ATOM   706  H  HA3  . GLY A 1 45  ? 17.99291 38.69965 -25.83929 1.000 16.60020 ? 41  GLY A HA3  1 
ATOM   707  N  N    . GLN A 1 46  ? 17.30591 35.92833 -27.19736 1.000 14.35598 ? 42  GLN A N    1 
ATOM   708  C  CA   . GLN A 1 46  ? 16.44743 35.34717 -28.22031 1.000 14.46057 ? 42  GLN A CA   1 
ATOM   709  C  C    . GLN A 1 46  ? 15.79592 34.01940 -27.85983 1.000 15.65150 ? 42  GLN A C    1 
ATOM   710  O  O    . GLN A 1 46  ? 15.02183 33.51379 -28.66848 1.000 18.39990 ? 42  GLN A O    1 
ATOM   711  C  CB   . GLN A 1 46  ? 17.24087 35.12604 -29.51580 1.000 18.10492 ? 42  GLN A CB   1 
ATOM   712  C  CG   . GLN A 1 46  ? 17.91761 36.34828 -30.07212 1.000 19.04556 ? 42  GLN A CG   1 
ATOM   713  C  CD   . GLN A 1 46  ? 16.94439 37.43878 -30.39443 1.000 20.06124 ? 42  GLN A CD   1 
ATOM   714  O  OE1  . GLN A 1 46  ? 16.05533 37.26551 -31.23533 1.000 23.01655 ? 42  GLN A OE1  1 
ATOM   715  N  NE2  . GLN A 1 46  ? 17.07673 38.56711 -29.72319 1.000 22.00145 ? 42  GLN A NE2  1 
ATOM   716  H  H    . GLN A 1 46  ? 17.99250 35.44705 -27.00613 1.000 17.25190 ? 42  GLN A H    1 
ATOM   717  H  HA   . GLN A 1 46  ? 15.73491 35.98900 -28.36615 1.000 17.37741 ? 42  GLN A HA   1 
ATOM   718  H  HB2  . GLN A 1 46  ? 17.93088 34.46658 -29.34289 1.000 21.75063 ? 42  GLN A HB2  1 
ATOM   719  H  HB3  . GLN A 1 46  ? 16.63136 34.79808 -30.19539 1.000 21.75063 ? 42  GLN A HB3  1 
ATOM   720  H  HG2  . GLN A 1 46  ? 18.54691 36.68902 -29.41731 1.000 22.87940 ? 42  GLN A HG2  1 
ATOM   721  H  HG3  . GLN A 1 46  ? 18.38459 36.10945 -30.88808 1.000 22.87940 ? 42  GLN A HG3  1 
ATOM   722  H  HE21 . GLN A 1 46  ? 17.69905 38.64710 -29.13505 1.000 26.42647 ? 42  GLN A HE21 1 
ATOM   723  H  HE22 . GLN A 1 46  ? 16.54065 39.22248 -29.87385 1.000 26.42647 ? 42  GLN A HE22 1 
ATOM   724  N  N    . ALA A 1 47  ? 16.07999 33.42659 -26.70521 1.000 14.20093 ? 43  ALA A N    1 
ATOM   725  C  CA   . ALA A 1 47  ? 15.39275 32.18785 -26.35862 1.000 14.08324 ? 43  ALA A CA   1 
ATOM   726  C  C    . ALA A 1 47  ? 13.90600 32.45652 -26.20171 1.000 14.48742 ? 43  ALA A C    1 
ATOM   727  O  O    . ALA A 1 47  ? 13.49954 33.32805 -25.43065 1.000 14.96586 ? 43  ALA A O    1 
ATOM   728  C  CB   . ALA A 1 47  ? 15.95677 31.60909 -25.06706 1.000 14.16431 ? 43  ALA A CB   1 
ATOM   729  H  H    . ALA A 1 47  ? 16.64689 33.71036 -26.12410 1.000 17.06585 ? 43  ALA A H    1 
ATOM   730  H  HA   . ALA A 1 47  ? 15.53003 31.53734 -27.06495 1.000 16.92461 ? 43  ALA A HA   1 
ATOM   731  H  HB1  . ALA A 1 47  ? 15.54795 30.74483 -24.90330 1.000 17.02190 ? 43  ALA A HB1  1 
ATOM   732  H  HB2  . ALA A 1 47  ? 16.91717 31.50863 -25.15895 1.000 17.02190 ? 43  ALA A HB2  1 
ATOM   733  H  HB3  . ALA A 1 47  ? 15.75591 32.21391 -24.33580 1.000 17.02190 ? 43  ALA A HB3  1 
ATOM   734  N  N    . ALA A 1 48  ? 13.10135 31.72112 -26.95223 1.000 15.89957 ? 44  ALA A N    1 
ATOM   735  C  CA   . ALA A 1 48  ? 11.67331 31.99036 -26.99323 1.000 15.93542 ? 44  ALA A CA   1 
ATOM   736  C  C    . ALA A 1 48  ? 11.04251 31.73028 -25.63894 1.000 15.10970 ? 44  ALA A C    1 
ATOM   737  O  O    . ALA A 1 48  ? 11.28575 30.69355 -25.01596 1.000 17.34601 ? 44  ALA A O    1 
ATOM   738  C  CB   . ALA A 1 48  ? 11.01616 31.10788 -28.04905 1.000 17.84706 ? 44  ALA A CB   1 
ATOM   739  H  H    . ALA A 1 48  ? 13.35395 31.06334 -27.44530 1.000 19.10421 ? 44  ALA A H    1 
ATOM   740  H  HA   . ALA A 1 48  ? 11.52703 32.92157 -27.22202 1.000 19.14723 ? 44  ALA A HA   1 
ATOM   741  H  HB1  . ALA A 1 48  ? 10.05270 31.16089 -27.94980 1.000 21.44120 ? 44  ALA A HB1  1 
ATOM   742  H  HB2  . ALA A 1 48  ? 11.27578 31.42200 -28.92929 1.000 21.44120 ? 44  ALA A HB2  1 
ATOM   743  H  HB3  . ALA A 1 48  ? 11.31170 30.19250 -27.92403 1.000 21.44120 ? 44  ALA A HB3  1 
ATOM   744  N  N    . GLY A 1 49  ? 10.22484 32.67920 -25.19046 1.000 16.01077 ? 45  GLY A N    1 
ATOM   745  C  CA   . GLY A 1 49  ? 9.46954  32.53297 -23.97131 1.000 16.00733 ? 45  GLY A CA   1 
ATOM   746  C  C    . GLY A 1 49  ? 10.11779 33.10031 -22.72007 1.000 15.69071 ? 45  GLY A C    1 
ATOM   747  O  O    . GLY A 1 49  ? 9.42636  33.24242 -21.69920 1.000 18.69265 ? 45  GLY A O    1 
ATOM   748  H  H    . GLY A 1 49  ? 10.09509 33.42911 -25.59097 1.000 19.23766 ? 45  GLY A H    1 
ATOM   749  H  HA2  . GLY A 1 49  ? 8.61500  32.97778 -24.08447 1.000 19.23352 ? 45  GLY A HA2  1 
ATOM   750  H  HA3  . GLY A 1 49  ? 9.31558  31.58775 -23.81717 1.000 19.23352 ? 45  GLY A HA3  1 
ATOM   751  N  N    . PHE A 1 50  ? 11.41742 33.40601 -22.73802 1.000 14.14765 ? 46  PHE A N    1 
ATOM   752  C  CA   . PHE A 1 50  ? 12.09668 33.87093 -21.53195 1.000 13.70449 ? 46  PHE A CA   1 
ATOM   753  C  C    . PHE A 1 50  ? 12.01786 35.39607 -21.43373 1.000 14.44969 ? 46  PHE A C    1 
ATOM   754  O  O    . PHE A 1 50  ? 12.17191 36.10304 -22.43855 1.000 16.41429 ? 46  PHE A O    1 
ATOM   755  C  CB   . PHE A 1 50  ? 13.56771 33.43461 -21.52470 1.000 13.50899 ? 46  PHE A CB   1 
ATOM   756  C  CG   . PHE A 1 50  ? 14.26564 33.79767 -20.24505 1.000 13.79808 ? 46  PHE A CG   1 
ATOM   757  C  CD1  . PHE A 1 50  ? 14.10160 33.01361 -19.11871 1.000 13.74810 ? 46  PHE A CD1  1 
ATOM   758  C  CD2  . PHE A 1 50  ? 15.03002 34.96348 -20.15244 1.000 13.77239 ? 46  PHE A CD2  1 
ATOM   759  C  CE1  . PHE A 1 50  ? 14.70794 33.35092 -17.93053 1.000 14.93765 ? 46  PHE A CE1  1 
ATOM   760  C  CE2  . PHE A 1 50  ? 15.61895 35.31875 -18.95361 1.000 13.70482 ? 46  PHE A CE2  1 
ATOM   761  C  CZ   . PHE A 1 50  ? 15.44619 34.52143 -17.83809 1.000 13.58115 ? 46  PHE A CZ   1 
ATOM   762  H  H    . PHE A 1 50  ? 11.92114 33.35178 -23.43295 1.000 17.00191 ? 46  PHE A H    1 
ATOM   763  H  HA   . PHE A 1 50  ? 11.66033 33.48402 -20.75684 1.000 16.47011 ? 46  PHE A HA   1 
ATOM   764  H  HB2  . PHE A 1 50  ? 13.61343 32.47151 -21.63078 1.000 16.23552 ? 46  PHE A HB2  1 
ATOM   765  H  HB3  . PHE A 1 50  ? 14.03171 33.87132 -22.25606 1.000 16.23552 ? 46  PHE A HB3  1 
ATOM   766  H  HD1  . PHE A 1 50  ? 13.57485 32.24854 -19.16449 1.000 16.52245 ? 46  PHE A HD1  1 
ATOM   767  H  HD2  . PHE A 1 50  ? 15.14312 35.50322 -20.90130 1.000 16.55160 ? 46  PHE A HD2  1 
ATOM   768  H  HE1  . PHE A 1 50  ? 14.62282 32.79460 -17.19015 1.000 17.94990 ? 46  PHE A HE1  1 
ATOM   769  H  HE2  . PHE A 1 50  ? 16.13076 36.09324 -18.89769 1.000 16.47051 ? 46  PHE A HE2  1 
ATOM   770  H  HZ   . PHE A 1 50  ? 15.82483 34.76965 -17.02573 1.000 16.32211 ? 46  PHE A HZ   1 
ATOM   771  N  N    . ALA A 1 51  ? 11.80232 35.90514 -20.20760 1.000 15.16350 ? 47  ALA A N    1 
ATOM   772  C  CA   . ALA A 1 51  ? 11.71792 37.34398 -19.94942 1.000 15.20347 ? 47  ALA A CA   1 
ATOM   773  C  C    . ALA A 1 51  ? 13.10869 37.89650 -19.63725 1.000 14.52234 ? 47  ALA A C    1 
ATOM   774  O  O    . ALA A 1 51  ? 13.56324 37.88637 -18.49341 1.000 17.10803 ? 47  ALA A O    1 
ATOM   775  C  CB   . ALA A 1 51  ? 10.73904 37.63460 -18.81117 1.000 18.66711 ? 47  ALA A CB   1 
ATOM   776  H  H    . ALA A 1 51  ? 11.70094 35.42414 -19.50193 1.000 18.22092 ? 47  ALA A H    1 
ATOM   777  H  HA   . ALA A 1 51  ? 11.40415 37.77445 -20.76007 1.000 18.26890 ? 47  ALA A HA   1 
ATOM   778  H  HB1  . ALA A 1 51  ? 10.70255 38.59250 -18.66288 1.000 22.42526 ? 47  ALA A HB1  1 
ATOM   779  H  HB2  . ALA A 1 51  ? 9.86095  37.30437 -19.05775 1.000 22.42526 ? 47  ALA A HB2  1 
ATOM   780  H  HB3  . ALA A 1 51  ? 11.04715 37.18699 -18.00767 1.000 22.42526 ? 47  ALA A HB3  1 
ATOM   781  N  N    . TYR A 1 52  ? 13.78597 38.41811 -20.66158 1.000 13.20837 ? 48  TYR A N    1 
ATOM   782  C  CA   . TYR A 1 52  ? 15.12252 38.98241 -20.51465 1.000 13.44633 ? 48  TYR A CA   1 
ATOM   783  C  C    . TYR A 1 52  ? 15.06698 40.43622 -20.06053 1.000 14.14480 ? 48  TYR A C    1 
ATOM   784  O  O    . TYR A 1 52  ? 14.09686 41.15685 -20.30790 1.000 16.85887 ? 48  TYR A O    1 
ATOM   785  C  CB   . TYR A 1 52  ? 15.83848 38.99051 -21.86064 1.000 14.64797 ? 48  TYR A CB   1 
ATOM   786  C  CG   . TYR A 1 52  ? 16.24118 37.64964 -22.40810 1.000 13.78276 ? 48  TYR A CG   1 
ATOM   787  C  CD1  . TYR A 1 52  ? 17.46727 37.09177 -22.08450 1.000 12.37331 ? 48  TYR A CD1  1 
ATOM   788  C  CD2  . TYR A 1 52  ? 15.42981 36.97251 -23.30817 1.000 14.32429 ? 48  TYR A CD2  1 
ATOM   789  C  CE1  . TYR A 1 52  ? 17.86567 35.88674 -22.61463 1.000 12.73172 ? 48  TYR A CE1  1 
ATOM   790  C  CE2  . TYR A 1 52  ? 15.82702 35.76167 -23.84247 1.000 13.50626 ? 48  TYR A CE2  1 
ATOM   791  C  CZ   . TYR A 1 52  ? 17.05683 35.23432 -23.49026 1.000 12.28493 ? 48  TYR A CZ   1 
ATOM   792  O  OH   . TYR A 1 52  ? 17.46448 34.06484 -24.08048 1.000 13.23519 ? 48  TYR A OH   1 
ATOM   793  H  H    . TYR A 1 52  ? 13.48608 38.45709 -21.46666 1.000 15.87478 ? 48  TYR A H    1 
ATOM   794  H  HA   . TYR A 1 52  ? 15.59959 38.44597 -19.86231 1.000 16.16032 ? 48  TYR A HA   1 
ATOM   795  H  HB2  . TYR A 1 52  ? 15.24955 39.40006 -22.51358 1.000 17.60230 ? 48  TYR A HB2  1 
ATOM   796  H  HB3  . TYR A 1 52  ? 16.64854 39.51611 -21.76874 1.000 17.60230 ? 48  TYR A HB3  1 
ATOM   797  H  HD1  . TYR A 1 52  ? 18.03188 37.54070 -21.49749 1.000 14.87270 ? 48  TYR A HD1  1 
ATOM   798  H  HD2  . TYR A 1 52  ? 14.61054 37.33751 -23.55408 1.000 17.21388 ? 48  TYR A HD2  1 
ATOM   799  H  HE1  . TYR A 1 52  ? 18.68579 35.51972 -22.37464 1.000 15.30280 ? 48  TYR A HE1  1 
ATOM   800  H  HE2  . TYR A 1 52  ? 15.27273 35.30526 -24.43352 1.000 16.23224 ? 48  TYR A HE2  1 
ATOM   801  H  HH   . TYR A 1 52  ? 18.29369 33.96929 -23.98624 1.000 15.90695 ? 48  TYR A HH   1 
ATOM   802  N  N    . THR A 1 53  ? 16.15392 40.88268 -19.43184 1.000 13.48173 ? 49  THR A N    1 
ATOM   803  C  CA   . THR A 1 53  ? 16.31643 42.31190 -19.22694 1.000 14.04322 ? 49  THR A CA   1 
ATOM   804  C  C    . THR A 1 53  ? 16.47728 43.02931 -20.56340 1.000 13.63418 ? 49  THR A C    1 
ATOM   805  O  O    . THR A 1 53  ? 16.96304 42.47204 -21.55665 1.000 13.91649 ? 49  THR A O    1 
ATOM   806  C  CB   . THR A 1 53  ? 17.55460 42.62686 -18.36555 1.000 14.70738 ? 49  THR A CB   1 
ATOM   807  O  OG1  . THR A 1 53  ? 18.75835 42.21576 -19.02943 1.000 13.62664 ? 49  THR A OG1  1 
ATOM   808  C  CG2  . THR A 1 53  ? 17.45440 42.01218 -16.96682 1.000 16.88418 ? 49  THR A CG2  1 
ATOM   809  H  H    . THR A 1 53  ? 16.78992 40.39169 -19.12519 1.000 16.20280 ? 49  THR A H    1 
ATOM   810  H  HA   . THR A 1 53  ? 15.52736 42.63892 -18.76725 1.000 16.87659 ? 49  THR A HA   1 
ATOM   811  H  HB   . THR A 1 53  ? 17.59947 43.58756 -18.23925 1.000 17.67358 ? 49  THR A HB   1 
ATOM   812  H  HG1  . THR A 1 53  ? 18.76067 41.38177 -19.12971 1.000 16.37670 ? 49  THR A HG1  1 
ATOM   813  H  HG21 . THR A 1 53  ? 18.28716 42.14241 -16.48677 1.000 20.28574 ? 49  THR A HG21 1 
ATOM   814  H  HG22 . THR A 1 53  ? 16.73552 42.43332 -16.47008 1.000 20.28574 ? 49  THR A HG22 1 
ATOM   815  H  HG23 . THR A 1 53  ? 17.27538 41.06124 -17.03438 1.000 20.28574 ? 49  THR A HG23 1 
ATOM   816  N  N    . ASP A 1 54  ? 16.14658 44.31879 -20.54785 1.000 14.50053 ? 50  ASP A N    1 
ATOM   817  C  CA   . ASP A 1 54  ? 16.49326 45.17568 -21.67401 1.000 14.79804 ? 50  ASP A CA   1 
ATOM   818  C  C    . ASP A 1 54  ? 17.99905 45.16902 -21.93401 1.000 14.35752 ? 50  ASP A C    1 
ATOM   819  O  O    . ASP A 1 54  ? 18.43060 45.22124 -23.08848 1.000 15.11488 ? 50  ASP A O    1 
ATOM   820  C  CB   . ASP A 1 54  ? 16.01107 46.59998 -21.40748 1.000 17.62521 ? 50  ASP A CB   1 
ATOM   821  C  CG   . ASP A 1 54  ? 14.55081 46.82699 -21.71523 1.000 20.59610 ? 50  ASP A CG   1 
ATOM   822  O  OD1  . ASP A 1 54  ? 13.84764 45.90145 -22.18532 1.000 20.34546 ? 50  ASP A OD1  1 
ATOM   823  O  OD2  . ASP A 1 54  ? 14.12558 47.98352 -21.48188 1.000 23.75972 ? 50  ASP A OD2  1 
ATOM   824  H  H    . ASP A 1 54  ? 15.72897 44.71619 -19.90967 1.000 17.42536 ? 50  ASP A H    1 
ATOM   825  H  HA   . ASP A 1 54  ? 16.04780 44.84273 -22.46875 1.000 17.78237 ? 50  ASP A HA   1 
ATOM   826  H  HB2  . ASP A 1 54  ? 16.14865 46.80388 -20.46919 1.000 21.17498 ? 50  ASP A HB2  1 
ATOM   827  H  HB3  . ASP A 1 54  ? 16.52570 47.21023 -21.95853 1.000 21.17498 ? 50  ASP A HB3  1 
ATOM   828  N  N    . ALA A 1 55  ? 18.81036 45.12518 -20.87802 1.000 14.33228 ? 51  ALA A N    1 
ATOM   829  C  CA   . ALA A 1 55  ? 20.26249 45.13057 -21.05008 1.000 15.10612 ? 51  ALA A CA   1 
ATOM   830  C  C    . ALA A 1 55  ? 20.71822 43.94615 -21.88120 1.000 13.62919 ? 51  ALA A C    1 
ATOM   831  O  O    . ALA A 1 55  ? 21.52555 44.09262 -22.81092 1.000 13.90219 ? 51  ALA A O    1 
ATOM   832  C  CB   . ALA A 1 55  ? 20.96041 45.13140 -19.68464 1.000 16.26748 ? 51  ALA A CB   1 
ATOM   833  H  H    . ALA A 1 55  ? 18.55107 45.09214 -20.05871 1.000 17.22346 ? 51  ALA A H    1 
ATOM   834  H  HA   . ALA A 1 55  ? 20.51514 45.94328 -21.51545 1.000 18.15207 ? 51  ALA A HA   1 
ATOM   835  H  HB1  . ALA A 1 55  ? 21.91959 45.18121 -19.82028 1.000 19.54570 ? 51  ALA A HB1  1 
ATOM   836  H  HB2  . ALA A 1 55  ? 20.65795 45.89987 -19.17585 1.000 19.54570 ? 51  ALA A HB2  1 
ATOM   837  H  HB3  . ALA A 1 55  ? 20.73489 44.31364 -19.21421 1.000 19.54570 ? 51  ALA A HB3  1 
ATOM   838  N  N    . ASN A 1 56  ? 20.22005 42.75310 -21.56827 1.000 13.05325 ? 52  ASN A N    1 
ATOM   839  C  CA   . ASN A 1 56  ? 20.62146 41.59299 -22.34805 1.000 13.11541 ? 52  ASN A CA   1 
ATOM   840  C  C    . ASN A 1 56  ? 20.17357 41.72372 -23.79617 1.000 14.57444 ? 52  ASN A C    1 
ATOM   841  O  O    . ASN A 1 56  ? 20.96172 41.47707 -24.72402 1.000 16.71169 ? 52  ASN A O    1 
ATOM   842  C  CB   . ASN A 1 56  ? 20.09668 40.31168 -21.72735 1.000 13.73390 ? 52  ASN A CB   1 
ATOM   843  C  CG   . ASN A 1 56  ? 20.32279 39.11841 -22.63167 1.000 16.19411 ? 52  ASN A CG   1 
ATOM   844  O  OD1  . ASN A 1 56  ? 19.67844 38.99113 -23.66261 1.000 15.99021 ? 52  ASN A OD1  1 
ATOM   845  N  ND2  . ASN A 1 56  ? 21.23522 38.26864 -22.26783 1.000 17.49653 ? 52  ASN A ND2  1 
ATOM   846  H  H    . ASN A 1 56  ? 19.66612 42.59356 -20.93007 1.000 15.68863 ? 52  ASN A H    1 
ATOM   847  H  HA   . ASN A 1 56  ? 21.58991 41.53957 -22.33575 1.000 15.76322 ? 52  ASN A HA   1 
ATOM   848  H  HB2  . ASN A 1 56  ? 20.55713 40.14998 -20.88905 1.000 16.50541 ? 52  ASN A HB2  1 
ATOM   849  H  HB3  . ASN A 1 56  ? 19.14336 40.39875 -21.57080 1.000 16.50541 ? 52  ASN A HB3  1 
ATOM   850  H  HD21 . ASN A 1 56  ? 21.39607 37.57662 -22.75243 1.000 21.02056 ? 52  ASN A HD21 1 
ATOM   851  H  HD22 . ASN A 1 56  ? 21.67852 38.39801 -21.54233 1.000 21.02056 ? 52  ASN A HD22 1 
ATOM   852  N  N    . LYS A 1 57  ? 18.90587 42.10028 -24.02014 1.000 13.67623 ? 53  LYS A N    1 
ATOM   853  C  CA   . LYS A 1 57  ? 18.41251 42.21430 -25.39135 1.000 15.50945 ? 53  LYS A CA   1 
ATOM   854  C  C    . LYS A 1 57  ? 19.18574 43.26973 -26.16740 1.000 16.74774 ? 53  LYS A C    1 
ATOM   855  O  O    . LYS A 1 57  ? 19.42852 43.10703 -27.37110 1.000 18.28714 ? 53  LYS A O    1 
ATOM   856  C  CB   . LYS A 1 57  ? 16.91244 42.50198 -25.39739 1.000 18.35506 ? 53  LYS A CB   1 
ATOM   857  C  CG   . LYS A 1 57  ? 16.09084 41.29635 -24.96286 1.000 21.39542 ? 53  LYS A CG   1 
ATOM   858  C  CD   . LYS A 1 57  ? 14.58639 41.54260 -25.02694 1.000 27.11103 ? 53  LYS A CD   1 
ATOM   859  C  CE   . LYS A 1 57  ? 14.10971 42.46699 -23.89742 1.000 33.60476 ? 53  LYS A CE   1 
ATOM   860  N  NZ   . LYS A 1 57  ? 12.63107 42.41867 -23.70379 1.000 38.43578 ? 53  LYS A NZ   1 
ATOM   861  H  H    . LYS A 1 57  ? 18.32841 42.28982 -23.41168 1.000 16.43621 ? 53  LYS A H    1 
ATOM   862  H  HA   . LYS A 1 57  ? 18.54130 41.36563 -25.84311 1.000 18.63606 ? 53  LYS A HA   1 
ATOM   863  H  HB2  . LYS A 1 57  ? 16.72664 43.23093 -24.78501 1.000 22.05080 ? 53  LYS A HB2  1 
ATOM   864  H  HB3  . LYS A 1 57  ? 16.63966 42.74570 -26.29577 1.000 22.05080 ? 53  LYS A HB3  1 
ATOM   865  H  HG2  . LYS A 1 57  ? 16.29559 40.54870 -25.54595 1.000 25.69923 ? 53  LYS A HG2  1 
ATOM   866  H  HG3  . LYS A 1 57  ? 16.31772 41.07410 -24.04633 1.000 25.69923 ? 53  LYS A HG3  1 
ATOM   867  H  HD2  . LYS A 1 57  ? 14.36643 41.96059 -25.87417 1.000 32.55797 ? 53  LYS A HD2  1 
ATOM   868  H  HD3  . LYS A 1 57  ? 14.11985 40.69627 -24.94352 1.000 32.55797 ? 53  LYS A HD3  1 
ATOM   869  H  HE2  . LYS A 1 57  ? 14.53064 42.19566 -23.06670 1.000 40.35044 ? 53  LYS A HE2  1 
ATOM   870  H  HE3  . LYS A 1 57  ? 14.35519 43.38086 -24.11071 1.000 40.35044 ? 53  LYS A HE3  1 
ATOM   871  H  HZ1  . LYS A 1 57  ? 12.39871 42.92142 -23.00712 1.000 46.14766 ? 53  LYS A HZ1  1 
ATOM   872  H  HZ2  . LYS A 1 57  ? 12.21871 42.72430 -24.43087 1.000 46.14766 ? 53  LYS A HZ2  1 
ATOM   873  H  HZ3  . LYS A 1 57  ? 12.37080 41.58070 -23.55487 1.000 46.14766 ? 53  LYS A HZ3  1 
ATOM   874  N  N    . ALA A 1 58  ? 19.58201 44.35425 -25.49544 1.000 14.35274 ? 54  ALA A N    1 
ATOM   875  C  CA   . ALA A 1 58  ? 20.26947 45.45719 -26.16082 1.000 15.74717 ? 54  ALA A CA   1 
ATOM   876  C  C    . ALA A 1 58  ? 21.67852 45.09700 -26.59935 1.000 15.66912 ? 54  ALA A C    1 
ATOM   877  O  O    . ALA A 1 58  ? 22.18135 45.68976 -27.56044 1.000 16.53945 ? 54  ALA A O    1 
ATOM   878  C  CB   . ALA A 1 58  ? 20.34198 46.67044 -25.23406 1.000 16.76108 ? 54  ALA A CB   1 
ATOM   879  H  H    . ALA A 1 58  ? 19.46501 44.47684 -24.65230 1.000 17.24802 ? 54  ALA A H    1 
ATOM   880  H  HA   . ALA A 1 58  ? 19.75266 45.68212 -26.95025 1.000 18.92134 ? 54  ALA A HA   1 
ATOM   881  H  HB1  . ALA A 1 58  ? 20.76192 47.40522 -25.70802 1.000 20.13803 ? 54  ALA A HB1  1 
ATOM   882  H  HB2  . ALA A 1 58  ? 19.44282 46.91905 -24.96835 1.000 20.13803 ? 54  ALA A HB2  1 
ATOM   883  H  HB3  . ALA A 1 58  ? 20.86614 46.43907 -24.45135 1.000 20.13803 ? 54  ALA A HB3  1 
ATOM   884  N  N    . LYS A 1 59  ? 22.34268 44.15743 -25.90852 1.000 14.22461 ? 55  LYS A N    1 
ATOM   885  C  CA   . LYS A 1 59  ? 23.75333 43.89149 -26.18242 1.000 15.01709 ? 55  LYS A CA   1 
ATOM   886  C  C    . LYS A 1 59  ? 23.99240 43.56355 -27.65702 1.000 14.64307 ? 55  LYS A C    1 
ATOM   887  O  O    . LYS A 1 59  ? 24.91040 44.11090 -28.28798 1.000 16.31198 ? 55  LYS A O    1 
ATOM   888  C  CB   . LYS A 1 59  ? 24.26762 42.78478 -25.26294 1.000 14.57123 ? 55  LYS A CB   1 
ATOM   889  C  CG   . LYS A 1 59  ? 25.77780 42.48545 -25.41491 1.000 14.34612 ? 55  LYS A CG   1 
ATOM   890  C  CD   . LYS A 1 59  ? 26.67060 43.63749 -24.94804 1.000 16.08260 ? 55  LYS A CD   1 
ATOM   891  C  CE   . LYS A 1 59  ? 28.14345 43.29655 -25.12844 1.000 16.80775 ? 55  LYS A CE   1 
ATOM   892  N  NZ   . LYS A 1 59  ? 29.06738 44.32567 -24.59379 1.000 17.71730 ? 55  LYS A NZ   1 
ATOM   893  H  H    . LYS A 1 59  ? 22.00309 43.66956 -25.28702 1.000 17.09426 ? 55  LYS A H    1 
ATOM   894  H  HA   . LYS A 1 59  ? 24.26450 44.69232 -25.98678 1.000 18.04524 ? 55  LYS A HA   1 
ATOM   895  H  HB2  . LYS A 1 59  ? 24.11093 43.04833 -24.34267 1.000 17.51020 ? 55  LYS A HB2  1 
ATOM   896  H  HB3  . LYS A 1 59  ? 23.78418 41.96746 -25.46087 1.000 17.51020 ? 55  LYS A HB3  1 
ATOM   897  H  HG2  . LYS A 1 59  ? 25.99876 41.70388 -24.88461 1.000 17.24007 ? 55  LYS A HG2  1 
ATOM   898  H  HG3  . LYS A 1 59  ? 25.97296 42.31780 -26.35016 1.000 17.24007 ? 55  LYS A HG3  1 
ATOM   899  H  HD2  . LYS A 1 59  ? 26.47335 44.43089 -25.47006 1.000 19.32385 ? 55  LYS A HD2  1 
ATOM   900  H  HD3  . LYS A 1 59  ? 26.50891 43.81058 -24.00740 1.000 19.32385 ? 55  LYS A HD3  1 
ATOM   901  H  HE2  . LYS A 1 59  ? 28.32991 42.46420 -24.66656 1.000 20.19403 ? 55  LYS A HE2  1 
ATOM   902  H  HE3  . LYS A 1 59  ? 28.32731 43.19865 -26.07581 1.000 20.19403 ? 55  LYS A HE3  1 
ATOM   903  H  HZ1  . LYS A 1 59  ? 29.90838 44.04084 -24.65466 1.000 21.28549 ? 55  LYS A HZ1  1 
ATOM   904  H  HZ2  . LYS A 1 59  ? 28.98376 45.08045 -25.05792 1.000 21.28549 ? 55  LYS A HZ2  1 
ATOM   905  H  HZ3  . LYS A 1 59  ? 28.87904 44.48953 -23.73952 1.000 21.28549 ? 55  LYS A HZ3  1 
ATOM   906  N  N    . GLY A 1 60  ? 23.16345 42.69173 -28.23335 1.000 15.03664 ? 56  GLY A N    1 
ATOM   907  C  CA   . GLY A 1 60  ? 23.11672 42.53450 -29.67852 1.000 16.32525 ? 56  GLY A CA   1 
ATOM   908  C  C    . GLY A 1 60  ? 24.24174 41.74868 -30.31989 1.000 16.28457 ? 56  GLY A C    1 
ATOM   909  O  O    . GLY A 1 60  ? 24.26501 41.64545 -31.55231 1.000 19.15874 ? 56  GLY A O    1 
ATOM   910  H  H    . GLY A 1 60  ? 22.61981 42.18171 -27.80448 1.000 18.06869 ? 56  GLY A H    1 
ATOM   911  H  HA2  . GLY A 1 60  ? 22.28727 42.08659 -29.90719 1.000 19.61503 ? 56  GLY A HA2  1 
ATOM   912  H  HA3  . GLY A 1 60  ? 23.11933 43.41799 -30.07895 1.000 19.61503 ? 56  GLY A HA3  1 
ATOM   913  N  N    . ILE A 1 61  ? 25.17435 41.21335 -29.53951 1.000 15.54007 ? 57  ILE A N    1 
ATOM   914  C  CA   . ILE A 1 61  ? 26.25012 40.38312 -30.07573 1.000 14.89175 ? 57  ILE A CA   1 
ATOM   915  C  C    . ILE A 1 61  ? 25.71045 38.99348 -30.42375 1.000 12.94496 ? 57  ILE A C    1 
ATOM   916  O  O    . ILE A 1 61  ? 24.61762 38.60896 -30.01562 1.000 13.55761 ? 57  ILE A O    1 
ATOM   917  C  CB   . ILE A 1 61  ? 27.46876 40.33110 -29.12255 1.000 15.62030 ? 57  ILE A CB   1 
ATOM   918  C  CG1  . ILE A 1 61  ? 27.12994 39.74557 -27.72717 1.000 14.29952 ? 57  ILE A CG1  1 
ATOM   919  C  CG2  . ILE A 1 61  ? 28.05658 41.73112 -28.96955 1.000 16.51921 ? 57  ILE A CG2  1 
ATOM   920  C  CD1  . ILE A 1 61  ? 27.04069 38.24047 -27.65607 1.000 14.05336 ? 57  ILE A CD1  1 
ATOM   921  H  H    . ILE A 1 61  ? 25.20975 41.31501 -28.68627 1.000 18.67281 ? 57  ILE A H    1 
ATOM   922  H  HA   . ILE A 1 61  ? 26.56737 40.78005 -30.90198 1.000 17.89483 ? 57  ILE A HA   1 
ATOM   923  H  HB   . ILE A 1 61  ? 28.11496 39.73064 -29.52600 1.000 18.76908 ? 57  ILE A HB   1 
ATOM   924  H  HG12 . ILE A 1 61  ? 27.81992 40.02312 -27.10445 1.000 17.18415 ? 57  ILE A HG12 1 
ATOM   925  H  HG13 . ILE A 1 61  ? 26.27041 40.09873 -27.44898 1.000 17.18415 ? 57  ILE A HG13 1 
ATOM   926  H  HG21 . ILE A 1 61  ? 28.86208 41.67838 -28.43170 1.000 19.84778 ? 57  ILE A HG21 1 
ATOM   927  H  HG22 . ILE A 1 61  ? 28.26816 42.08258 -29.84852 1.000 19.84778 ? 57  ILE A HG22 1 
ATOM   928  H  HG23 . ILE A 1 61  ? 27.40440 42.30152 -28.53342 1.000 19.84778 ? 57  ILE A HG23 1 
ATOM   929  H  HD11 . ILE A 1 61  ? 27.20470 37.95718 -26.74297 1.000 16.88876 ? 57  ILE A HD11 1 
ATOM   930  H  HD12 . ILE A 1 61  ? 26.15373 37.96322 -27.93416 1.000 16.88876 ? 57  ILE A HD12 1 
ATOM   931  H  HD13 . ILE A 1 61  ? 27.70761 37.85633 -28.24644 1.000 16.88876 ? 57  ILE A HD13 1 
ATOM   932  N  N    . THR A 1 62  ? 26.50049 38.25038 -31.20242 1.000 14.01466 ? 58  THR A N    1 
ATOM   933  C  CA   . THR A 1 62  ? 26.22476 36.85744 -31.51901 1.000 13.58196 ? 58  THR A CA   1 
ATOM   934  C  C    . THR A 1 62  ? 27.05035 35.98652 -30.57951 1.000 13.21517 ? 58  THR A C    1 
ATOM   935  O  O    . THR A 1 62  ? 28.27426 36.12986 -30.50697 1.000 15.03413 ? 58  THR A O    1 
ATOM   936  C  CB   . THR A 1 62  ? 26.60377 36.58778 -32.97622 1.000 14.61249 ? 58  THR A CB   1 
ATOM   937  O  OG1  . THR A 1 62  ? 25.82232 37.43821 -33.81570 1.000 17.23591 ? 58  THR A OG1  1 
ATOM   938  C  CG2  . THR A 1 62  ? 26.36475 35.14315 -33.32641 1.000 16.58498 ? 58  THR A CG2  1 
ATOM   939  H  H    . THR A 1 62  ? 27.22152 38.54570 -31.56642 1.000 16.84232 ? 58  THR A H    1 
ATOM   940  H  HA   . THR A 1 62  ? 25.28694 36.64175 -31.39708 1.000 16.32308 ? 58  THR A HA   1 
ATOM   941  H  HB   . THR A 1 62  ? 27.54581 36.76859 -33.12033 1.000 17.55972 ? 58  THR A HB   1 
ATOM   942  H  HG1  . THR A 1 62  ? 25.96633 37.25603 -34.62296 1.000 20.70781 ? 58  THR A HG1  1 
ATOM   943  H  HG21 . THR A 1 62  ? 26.29800 35.04173 -34.28878 1.000 19.92671 ? 58  THR A HG21 1 
ATOM   944  H  HG22 . THR A 1 62  ? 27.09840 34.59749 -33.00250 1.000 19.92671 ? 58  THR A HG22 1 
ATOM   945  H  HG23 . THR A 1 62  ? 25.53985 34.83523 -32.91945 1.000 19.92671 ? 58  THR A HG23 1 
ATOM   946  N  N    . TRP A 1 63  ? 26.38598 35.08031 -29.86657 1.000 12.86109 ? 59  TRP A N    1 
ATOM   947  C  CA   . TRP A 1 63  ? 27.12050 34.20731 -28.95822 1.000 12.52672 ? 59  TRP A CA   1 
ATOM   948  C  C    . TRP A 1 63  ? 27.99711 33.23769 -29.74058 1.000 12.23547 ? 59  TRP A C    1 
ATOM   949  O  O    . TRP A 1 63  ? 27.54990 32.62114 -30.71091 1.000 14.36073 ? 59  TRP A O    1 
ATOM   950  C  CB   . TRP A 1 63  ? 26.15824 33.45998 -28.04265 1.000 12.36562 ? 59  TRP A CB   1 
ATOM   951  C  CG   . TRP A 1 63  ? 25.51850 34.30890 -26.98646 1.000 12.61590 ? 59  TRP A CG   1 
ATOM   952  C  CD1  . TRP A 1 63  ? 24.17723 34.53410 -26.79755 1.000 13.26874 ? 59  TRP A CD1  1 
ATOM   953  C  CD2  . TRP A 1 63  ? 26.19308 35.02791 -25.94875 1.000 11.63422 ? 59  TRP A CD2  1 
ATOM   954  N  NE1  . TRP A 1 63  ? 23.98402 35.33500 -25.69914 1.000 13.11602 ? 59  TRP A NE1  1 
ATOM   955  C  CE2  . TRP A 1 63  ? 25.20544 35.66030 -25.16700 1.000 12.00292 ? 59  TRP A CE2  1 
ATOM   956  C  CE3  . TRP A 1 63  ? 27.53489 35.20970 -25.61281 1.000 13.18741 ? 59  TRP A CE3  1 
ATOM   957  C  CZ2  . TRP A 1 63  ? 25.52895 36.47466 -24.08443 1.000 12.96533 ? 59  TRP A CZ2  1 
ATOM   958  C  CZ3  . TRP A 1 63  ? 27.84738 36.01165 -24.53843 1.000 13.70635 ? 59  TRP A CZ3  1 
ATOM   959  C  CH2  . TRP A 1 63  ? 26.84933 36.62084 -23.77600 1.000 12.69213 ? 59  TRP A CH2  1 
ATOM   960  H  H    . TRP A 1 63  ? 25.53558 34.95422 -29.88952 1.000 15.45803 ? 59  TRP A H    1 
ATOM   961  H  HA   . TRP A 1 63  ? 27.70245 34.74415 -28.39783 1.000 15.05679 ? 59  TRP A HA   1 
ATOM   962  H  HB2  . TRP A 1 63  ? 25.44787 33.08147 -28.58394 1.000 14.86347 ? 59  TRP A HB2  1 
ATOM   963  H  HB3  . TRP A 1 63  ? 26.64612 32.75211 -27.59342 1.000 14.86347 ? 59  TRP A HB3  1 
ATOM   964  H  HD1  . TRP A 1 63  ? 23.49880 34.19387 -27.33503 1.000 15.94722 ? 59  TRP A HD1  1 
ATOM   965  H  HE1  . TRP A 1 63  ? 23.22155 35.59087 -25.39457 1.000 15.76395 ? 59  TRP A HE1  1 
ATOM   966  H  HE3  . TRP A 1 63  ? 28.20638 34.79642 -26.10597 1.000 15.84962 ? 59  TRP A HE3  1 
ATOM   967  H  HZ2  . TRP A 1 63  ? 24.86836 36.90333 -23.58970 1.000 15.58312 ? 59  TRP A HZ2  1 
ATOM   968  H  HZ3  . TRP A 1 63  ? 28.73984 36.15011 -24.31649 1.000 16.47235 ? 59  TRP A HZ3  1 
ATOM   969  H  HH2  . TRP A 1 63  ? 27.09014 37.13785 -23.04142 1.000 15.25529 ? 59  TRP A HH2  1 
ATOM   970  N  N    . ASN A 1 64  ? 29.23711 33.09509 -29.29956 1.000 12.43814 ? 60  ASN A N    1 
ATOM   971  C  CA   . ASN A 1 64  ? 30.22082 32.18530 -29.88101 1.000 12.48269 ? 60  ASN A CA   1 
ATOM   972  C  C    . ASN A 1 64  ? 31.31167 31.99987 -28.83165 1.000 12.44597 ? 60  ASN A C    1 
ATOM   973  O  O    . ASN A 1 64  ? 31.20807 32.51031 -27.71317 1.000 11.88368 ? 60  ASN A O    1 
ATOM   974  C  CB   . ASN A 1 64  ? 30.76074 32.69490 -31.22524 1.000 15.87598 ? 60  ASN A CB   1 
ATOM   975  C  CG   . ASN A 1 64  ? 31.82495 33.80524 -31.07734 1.000 18.21725 ? 60  ASN A CG   1 
ATOM   976  O  OD1  . ASN A 1 64  ? 31.83049 34.55673 -30.12677 1.000 16.84813 ? 60  ASN A OD1  1 
ATOM   977  N  ND2  . ASN A 1 64  ? 32.74895 33.87803 -32.03948 1.000 23.60932 ? 60  ASN A ND2  1 
ATOM   978  H  H    . ASN A 1 64  ? 29.55131 33.53532 -28.63093 1.000 14.95050 ? 60  ASN A H    1 
ATOM   979  H  HA   . ASN A 1 64  ? 29.79924 31.33087 -30.06299 1.000 15.00396 ? 60  ASN A HA   1 
ATOM   980  H  HB2  . ASN A 1 64  ? 31.16813 31.95411 -31.70081 1.000 19.07591 ? 60  ASN A HB2  1 
ATOM   981  H  HB3  . ASN A 1 64  ? 30.02402 33.05624 -31.74252 1.000 19.07591 ? 60  ASN A HB3  1 
ATOM   982  H  HD21 . ASN A 1 64  ? 33.36257 34.47940 -32.00175 1.000 28.35591 ? 60  ASN A HD21 1 
ATOM   983  H  HD22 . ASN A 1 64  ? 32.73013 33.32353 -32.69657 1.000 28.35591 ? 60  ASN A HD22 1 
ATOM   984  N  N    . GLU A 1 65  ? 32.37693 31.28779 -29.18968 1.000 12.93501 ? 61  GLU A N    1 
ATOM   985  C  CA   . GLU A 1 65  ? 33.44763 31.04125 -28.23183 1.000 13.08837 ? 61  GLU A CA   1 
ATOM   986  C  C    . GLU A 1 65  ? 34.01138 32.34138 -27.67546 1.000 12.79677 ? 61  GLU A C    1 
ATOM   987  O  O    . GLU A 1 65  ? 34.20730 32.46755 -26.46399 1.000 12.93124 ? 61  GLU A O    1 
ATOM   988  C  CB   . GLU A 1 65  ? 34.56984 30.24431 -28.90895 1.000 15.39922 ? 61  GLU A CB   1 
ATOM   989  C  CG   . GLU A 1 65  ? 34.20251 28.82350 -29.27664 1.000 16.64841 ? 61  GLU A CG   1 
ATOM   990  C  CD   . GLU A 1 65  ? 33.59234 28.65977 -30.66401 1.000 20.37191 ? 61  GLU A CD   1 
ATOM   991  O  OE1  . GLU A 1 65  ? 32.97541 29.59790 -31.22928 1.000 21.55157 ? 61  GLU A OE1  1 
ATOM   992  O  OE2  . GLU A 1 65  ? 33.73340 27.54679 -31.18963 1.000 24.07896 ? 61  GLU A OE2  1 
ATOM   993  H  H    . GLU A 1 65  ? 32.50338 30.94172 -29.96676 1.000 15.54674 ? 61  GLU A H    1 
ATOM   994  H  HA   . GLU A 1 65  ? 33.08548 30.52460 -27.49506 1.000 15.73078 ? 61  GLU A HA   1 
ATOM   995  H  HB2  . GLU A 1 65  ? 34.82272 30.70155 -29.72619 1.000 18.50379 ? 61  GLU A HB2  1 
ATOM   996  H  HB3  . GLU A 1 65  ? 35.32693 30.20313 -28.30395 1.000 18.50379 ? 61  GLU A HB3  1 
ATOM   997  H  HG2  . GLU A 1 65  ? 35.00511 28.27967 -29.24541 1.000 20.00282 ? 61  GLU A HG2  1 
ATOM   998  H  HG3  . GLU A 1 65  ? 33.55474 28.49619 -28.63308 1.000 20.00282 ? 61  GLU A HG3  1 
ATOM   999  N  N    . ASP A 1 66  ? 34.33653 33.30033 -28.55206 1.000 13.43493 ? 62  ASP A N    1 
ATOM   1000 C  CA   . ASP A 1 66  ? 35.02764 34.50724 -28.10219 1.000 14.67076 ? 62  ASP A CA   1 
ATOM   1001 C  C    . ASP A 1 66  ? 34.14569 35.37347 -27.21879 1.000 13.26354 ? 62  ASP A C    1 
ATOM   1002 O  O    . ASP A 1 66  ? 34.60965 35.88746 -26.19723 1.000 13.80374 ? 62  ASP A O    1 
ATOM   1003 C  CB   . ASP A 1 66  ? 35.53413 35.30459 -29.29570 1.000 18.68668 ? 62  ASP A CB   1 
ATOM   1004 C  CG   . ASP A 1 66  ? 36.57879 34.54925 -30.07743 1.000 21.77689 ? 62  ASP A CG   1 
ATOM   1005 O  OD1  . ASP A 1 66  ? 36.21011 33.56659 -30.72534 1.000 25.75155 ? 62  ASP A OD1  1 
ATOM   1006 O  OD2  . ASP A 1 66  ? 37.76988 34.91312 -30.02509 1.000 26.77534 ? 62  ASP A OD2  1 
ATOM   1007 H  H    . ASP A 1 66  ? 34.17142 33.27659 -29.39573 1.000 16.14665 ? 62  ASP A H    1 
ATOM   1008 H  HA   . ASP A 1 66  ? 35.79442 34.23413 -27.57458 1.000 17.62964 ? 62  ASP A HA   1 
ATOM   1009 H  HB2  . ASP A 1 66  ? 34.79142 35.49676 -29.88930 1.000 22.44875 ? 62  ASP A HB2  1 
ATOM   1010 H  HB3  . ASP A 1 66  ? 35.93036 36.13230 -28.98138 1.000 22.44875 ? 62  ASP A HB3  1 
ATOM   1011 N  N    . THR A 1 67  ? 32.88586 35.56904 -27.60495 1.000 12.91469 ? 63  THR A N    1 
ATOM   1012 C  CA   . THR A 1 67  ? 32.00836 36.39731 -26.78691 1.000 11.95721 ? 63  THR A CA   1 
ATOM   1013 C  C    . THR A 1 67  ? 31.69073 35.72223 -25.45336 1.000 11.16262 ? 63  THR A C    1 
ATOM   1014 O  O    . THR A 1 67  ? 31.62566 36.39572 -24.41637 1.000 12.00204 ? 63  THR A O    1 
ATOM   1015 C  CB   . THR A 1 67  ? 30.73679 36.81744 -27.55014 1.000 12.27430 ? 63  THR A CB   1 
ATOM   1016 O  OG1  . THR A 1 67  ? 30.04060 35.65181 -27.99982 1.000 12.48189 ? 63  THR A OG1  1 
ATOM   1017 C  CG2  . THR A 1 67  ? 31.09039 37.71414 -28.74686 1.000 12.79603 ? 63  THR A CG2  1 
ATOM   1018 H  H    . THR A 1 67  ? 32.52443 35.24400 -28.31440 1.000 15.52236 ? 63  THR A H    1 
ATOM   1019 H  HA   . THR A 1 67  ? 32.47367 37.22503 -26.58879 1.000 14.37338 ? 63  THR A HA   1 
ATOM   1020 H  HB   . THR A 1 67  ? 30.15737 37.32563 -26.96114 1.000 14.75389 ? 63  THR A HB   1 
ATOM   1021 H  HG1  . THR A 1 67  ? 30.43327 35.32130 -28.66478 1.000 15.00300 ? 63  THR A HG1  1 
ATOM   1022 H  HG21 . THR A 1 67  ? 30.28527 38.11440 -29.11083 1.000 15.37996 ? 63  THR A HG21 1 
ATOM   1023 H  HG22 . THR A 1 67  ? 31.69349 38.41995 -28.46579 1.000 15.37996 ? 63  THR A HG22 1 
ATOM   1024 H  HG23 . THR A 1 67  ? 31.52144 37.18885 -29.43908 1.000 15.37996 ? 63  THR A HG23 1 
ATOM   1025 N  N    . LEU A 1 68  ? 31.49528 34.39242 -25.44497 1.000 10.83711 ? 64  LEU A N    1 
ATOM   1026 C  CA   . LEU A 1 68  ? 31.29219 33.69039 -24.17928 1.000 10.63164 ? 64  LEU A CA   1 
ATOM   1027 C  C    . LEU A 1 68  ? 32.53533 33.77374 -23.29379 1.000 12.85706 ? 64  LEU A C    1 
ATOM   1028 O  O    . LEU A 1 68  ? 32.42053 33.87242 -22.07000 1.000 11.69787 ? 64  LEU A O    1 
ATOM   1029 C  CB   . LEU A 1 68  ? 30.91386 32.23634 -24.42383 1.000 11.85613 ? 64  LEU A CB   1 
ATOM   1030 C  CG   . LEU A 1 68  ? 29.47660 32.00830 -24.90709 1.000 12.34648 ? 64  LEU A CG   1 
ATOM   1031 C  CD1  . LEU A 1 68  ? 29.34460 30.59518 -25.42191 1.000 13.27622 ? 64  LEU A CD1  1 
ATOM   1032 C  CD2  . LEU A 1 68  ? 28.46625 32.26957 -23.81097 1.000 12.82474 ? 64  LEU A CD2  1 
ATOM   1033 H  H    . LEU A 1 68  ? 31.47676 33.88907 -26.14203 1.000 13.02926 ? 64  LEU A H    1 
ATOM   1034 H  HA   . LEU A 1 68  ? 30.55440 34.11337 -23.71274 1.000 12.78270 ? 64  LEU A HA   1 
ATOM   1035 H  HB2  . LEU A 1 68  ? 31.50854 31.87542 -25.09985 1.000 14.25209 ? 64  LEU A HB2  1 
ATOM   1036 H  HB3  . LEU A 1 68  ? 31.02181 31.74852 -23.59240 1.000 14.25209 ? 64  LEU A HB3  1 
ATOM   1037 H  HG   . LEU A 1 68  ? 29.28099 32.63347 -25.62249 1.000 14.84051 ? 64  LEU A HG   1 
ATOM   1038 H  HD11 . LEU A 1 68  ? 28.44982 30.46996 -25.77489 1.000 15.95619 ? 64  LEU A HD11 1 
ATOM   1039 H  HD12 . LEU A 1 68  ? 29.99971 30.45192 -26.12276 1.000 15.95619 ? 64  LEU A HD12 1 
ATOM   1040 H  HD13 . LEU A 1 68  ? 29.50142 29.97690 -24.69113 1.000 15.95619 ? 64  LEU A HD13 1 
ATOM   1041 H  HD21 . LEU A 1 68  ? 27.58821 31.99557 -24.11896 1.000 15.41442 ? 64  LEU A HD21 1 
ATOM   1042 H  HD22 . LEU A 1 68  ? 28.71486 31.75956 -23.02421 1.000 15.41442 ? 64  LEU A HD22 1 
ATOM   1043 H  HD23 . LEU A 1 68  ? 28.46323 33.21714 -23.60358 1.000 15.41442 ? 64  LEU A HD23 1 
ATOM   1044 N  N    . PHE A 1 69  ? 33.72993 33.69883 -23.89223 1.000 11.34108 ? 65  PHE A N    1 
ATOM   1045 C  CA   . PHE A 1 69  ? 34.96605 33.73638 -23.11652 1.000 11.71879 ? 65  PHE A CA   1 
ATOM   1046 C  C    . PHE A 1 69  ? 35.09273 35.05678 -22.35918 1.000 13.30336 ? 65  PHE A C    1 
ATOM   1047 O  O    . PHE A 1 69  ? 35.51306 35.07768 -21.20003 1.000 14.47792 ? 65  PHE A O    1 
ATOM   1048 C  CB   . PHE A 1 69  ? 36.14139 33.49272 -24.06493 1.000 12.42029 ? 65  PHE A CB   1 
ATOM   1049 C  CG   . PHE A 1 69  ? 37.45106 33.20373 -23.38234 1.000 14.99548 ? 65  PHE A CG   1 
ATOM   1050 C  CD1  . PHE A 1 69  ? 37.69767 31.96619 -22.79377 1.000 15.89862 ? 65  PHE A CD1  1 
ATOM   1051 C  CD2  . PHE A 1 69  ? 38.44530 34.14807 -23.37646 1.000 17.26956 ? 65  PHE A CD2  1 
ATOM   1052 C  CE1  . PHE A 1 69  ? 38.91794 31.69850 -22.21159 1.000 17.20710 ? 65  PHE A CE1  1 
ATOM   1053 C  CE2  . PHE A 1 69  ? 39.67887 33.87422 -22.78733 1.000 19.17415 ? 65  PHE A CE2  1 
ATOM   1054 C  CZ   . PHE A 1 69  ? 39.90332 32.65748 -22.21022 1.000 18.24531 ? 65  PHE A CZ   1 
ATOM   1055 H  H    . PHE A 1 69  ? 33.85063 33.62627 -24.74062 1.000 13.63402 ? 65  PHE A H    1 
ATOM   1056 H  HA   . PHE A 1 69  ? 34.97487 33.03351 -22.44809 1.000 14.08728 ? 65  PHE A HA   1 
ATOM   1057 H  HB2  . PHE A 1 69  ? 35.93086 32.73089 -24.62723 1.000 14.92907 ? 65  PHE A HB2  1 
ATOM   1058 H  HB3  . PHE A 1 69  ? 36.26550 34.28433 -24.61160 1.000 14.92907 ? 65  PHE A HB3  1 
ATOM   1059 H  HD1  . PHE A 1 69  ? 37.03368 31.31502 -22.79348 1.000 19.10307 ? 65  PHE A HD1  1 
ATOM   1060 H  HD2  . PHE A 1 69  ? 38.29554 34.97793 -23.76864 1.000 20.74820 ? 65  PHE A HD2  1 
ATOM   1061 H  HE1  . PHE A 1 69  ? 39.07476 30.86971 -21.81992 1.000 20.67325 ? 65  PHE A HE1  1 
ATOM   1062 H  HE2  . PHE A 1 69  ? 40.34826 34.51983 -22.78747 1.000 23.03371 ? 65  PHE A HE2  1 
ATOM   1063 H  HZ   . PHE A 1 69  ? 40.72544 32.47666 -21.81484 1.000 21.91910 ? 65  PHE A HZ   1 
ATOM   1064 N  N    . GLU A 1 70  ? 34.71613 36.16414 -22.99300 1.000 12.35708 ? 66  GLU A N    1 
ATOM   1065 C  CA   . GLU A 1 70  ? 34.68939 37.46684 -22.33081 1.000 13.29311 ? 66  GLU A CA   1 
ATOM   1066 C  C    . GLU A 1 70  ? 33.55722 37.56361 -21.30832 1.000 12.98803 ? 66  GLU A C    1 
ATOM   1067 O  O    . GLU A 1 70  ? 33.76439 37.98126 -20.16002 1.000 13.67649 ? 66  GLU A O    1 
ATOM   1068 C  CB   . GLU A 1 70  ? 34.57324 38.59403 -23.36229 1.000 16.22223 ? 66  GLU A CB   1 
ATOM   1069 C  CG   . GLU A 1 70  ? 34.65391 39.97116 -22.72257 1.000 16.27914 ? 66  GLU A CG   1 
ATOM   1070 C  CD   . GLU A 1 70  ? 34.77877 41.12687 -23.69821 1.000 19.12789 ? 66  GLU A CD   1 
ATOM   1071 O  OE1  . GLU A 1 70  ? 34.97069 40.89628 -24.91708 1.000 22.28837 ? 66  GLU A OE1  1 
ATOM   1072 O  OE2  . GLU A 1 70  ? 34.69200 42.28129 -23.21984 1.000 21.49452 ? 66  GLU A OE2  1 
ATOM   1073 H  H    . GLU A 1 70  ? 34.46792 36.19271 -23.81591 1.000 14.85322 ? 66  GLU A H    1 
ATOM   1074 H  HA   . GLU A 1 70  ? 35.52928 37.57493 -21.85774 1.000 15.97645 ? 66  GLU A HA   1 
ATOM   1075 H  HB2  . GLU A 1 70  ? 35.29797 38.51485 -24.00213 1.000 19.49141 ? 66  GLU A HB2  1 
ATOM   1076 H  HB3  . GLU A 1 70  ? 33.71962 38.52142 -23.81723 1.000 19.49141 ? 66  GLU A HB3  1 
ATOM   1077 H  HG2  . GLU A 1 70  ? 33.84785 40.11612 -22.20279 1.000 19.55969 ? 66  GLU A HG2  1 
ATOM   1078 H  HG3  . GLU A 1 70  ? 35.43130 39.99557 -22.14294 1.000 19.55969 ? 66  GLU A HG3  1 
ATOM   1079 N  N    . TYR A 1 71  ? 32.34192 37.21086 -21.72269 1.000 12.35882 ? 67  TYR A N    1 
ATOM   1080 C  CA   . TYR A 1 71  ? 31.18567 37.30058 -20.83408 1.000 12.01505 ? 67  TYR A CA   1 
ATOM   1081 C  C    . TYR A 1 71  ? 31.40230 36.54112 -19.54324 1.000 11.95993 ? 67  TYR A C    1 
ATOM   1082 O  O    . TYR A 1 71  ? 31.14013 37.05352 -18.45848 1.000 12.76241 ? 67  TYR A O    1 
ATOM   1083 C  CB   . TYR A 1 71  ? 29.99146 36.71530 -21.55913 1.000 11.48908 ? 67  TYR A CB   1 
ATOM   1084 C  CG   . TYR A 1 71  ? 28.69195 36.65052 -20.77132 1.000 11.91816 ? 67  TYR A CG   1 
ATOM   1085 C  CD1  . TYR A 1 71  ? 28.09285 37.81032 -20.27148 1.000 11.86411 ? 67  TYR A CD1  1 
ATOM   1086 C  CD2  . TYR A 1 71  ? 28.05013 35.44366 -20.55780 1.000 13.75582 ? 67  TYR A CD2  1 
ATOM   1087 C  CE1  . TYR A 1 71  ? 26.87060 37.76679 -19.61234 1.000 12.70942 ? 67  TYR A CE1  1 
ATOM   1088 C  CE2  . TYR A 1 71  ? 26.81783 35.38288 -19.87271 1.000 14.05341 ? 67  TYR A CE2  1 
ATOM   1089 C  CZ   . TYR A 1 71  ? 26.23981 36.55862 -19.41962 1.000 13.50505 ? 67  TYR A CZ   1 
ATOM   1090 O  OH   . TYR A 1 71  ? 25.02480 36.57620 -18.76221 1.000 15.56291 ? 67  TYR A OH   1 
ATOM   1091 H  H    . TYR A 1 71  ? 32.15806 36.91730 -22.50984 1.000 14.85531 ? 67  TYR A H    1 
ATOM   1092 H  HA   . TYR A 1 71  ? 31.03028 38.23144 -20.60993 1.000 14.44279 ? 67  TYR A HA   1 
ATOM   1093 H  HB2  . TYR A 1 71  ? 29.82130 37.25576 -22.34644 1.000 13.81162 ? 67  TYR A HB2  1 
ATOM   1094 H  HB3  . TYR A 1 71  ? 30.21199 35.80774 -21.82105 1.000 13.81162 ? 67  TYR A HB3  1 
ATOM   1095 H  HD1  . TYR A 1 71  ? 28.52138 38.62822 -20.38248 1.000 14.26166 ? 67  TYR A HD1  1 
ATOM   1096 H  HD2  . TYR A 1 71  ? 28.43764 34.65851 -20.87130 1.000 16.53171 ? 67  TYR A HD2  1 
ATOM   1097 H  HE1  . TYR A 1 71  ? 26.47978 38.55164 -19.30223 1.000 15.27603 ? 67  TYR A HE1  1 
ATOM   1098 H  HE2  . TYR A 1 71  ? 26.39925 34.56525 -19.72719 1.000 16.88882 ? 67  TYR A HE2  1 
ATOM   1099 H  HH   . TYR A 1 71  ? 24.70929 35.79881 -18.72077 1.000 18.70022 ? 67  TYR A HH   1 
ATOM   1100 N  N    . LEU A 1 72  ? 31.82245 35.28467 -19.64627 1.000 11.81675 ? 68  LEU A N    1 
ATOM   1101 C  CA   . LEU A 1 72  ? 31.84431 34.41809 -18.47429 1.000 13.03266 ? 68  LEU A CA   1 
ATOM   1102 C  C    . LEU A 1 72  ? 32.93781 34.79285 -17.48300 1.000 14.05958 ? 68  LEU A C    1 
ATOM   1103 O  O    . LEU A 1 72  ? 32.83284 34.42945 -16.31123 1.000 15.39539 ? 68  LEU A O    1 
ATOM   1104 C  CB   . LEU A 1 72  ? 31.91854 32.94465 -18.88747 1.000 14.62149 ? 68  LEU A CB   1 
ATOM   1105 C  CG   . LEU A 1 72  ? 30.70036 32.44019 -19.67523 1.000 15.19812 ? 68  LEU A CG   1 
ATOM   1106 C  CD1  . LEU A 1 72  ? 30.98493 31.07811 -20.27489 1.000 18.17434 ? 68  LEU A CD1  1 
ATOM   1107 C  CD2  . LEU A 1 72  ? 29.44283 32.36589 -18.81538 1.000 16.92540 ? 68  LEU A CD2  1 
ATOM   1108 H  H    . LEU A 1 72  ? 32.09648 34.91333 -20.37195 1.000 14.20483 ? 68  LEU A H    1 
ATOM   1109 H  HA   . LEU A 1 72  ? 31.00459 34.51821 -17.99916 1.000 15.66392 ? 68  LEU A HA   1 
ATOM   1110 H  HB2  . LEU A 1 72  ? 32.70136 32.82064 -19.44669 1.000 17.57052 ? 68  LEU A HB2  1 
ATOM   1111 H  HB3  . LEU A 1 72  ? 31.99423 32.40347 -18.08605 1.000 17.57052 ? 68  LEU A HB3  1 
ATOM   1112 H  HG   . LEU A 1 72  ? 30.52996 33.07806 -20.38586 1.000 18.26248 ? 68  LEU A HG   1 
ATOM   1113 H  HD11 . LEU A 1 72  ? 30.25768 30.83672 -20.86965 1.000 21.83394 ? 68  LEU A HD11 1 
ATOM   1114 H  HD12 . LEU A 1 72  ? 31.81781 31.11897 -20.77040 1.000 21.83394 ? 68  LEU A HD12 1 
ATOM   1115 H  HD13 . LEU A 1 72  ? 31.05722 30.42699 -19.55955 1.000 21.83394 ? 68  LEU A HD13 1 
ATOM   1116 H  HD21 . LEU A 1 72  ? 28.75066 31.89774 -19.30796 1.000 20.33521 ? 68  LEU A HD21 1 
ATOM   1117 H  HD22 . LEU A 1 72  ? 29.64769 31.88724 -17.99696 1.000 20.33521 ? 68  LEU A HD22 1 
ATOM   1118 H  HD23 . LEU A 1 72  ? 29.14899 33.26655 -18.60712 1.000 20.33521 ? 68  LEU A HD23 1 
ATOM   1119 N  N    . GLU A 1 73  ? 33.94355 35.56125 -17.91297 1.000 13.95507 ? 69  GLU A N    1 
ATOM   1120 C  CA   . GLU A 1 73  ? 34.92768 36.10033 -16.98422 1.000 15.03730 ? 69  GLU A CA   1 
ATOM   1121 C  C    . GLU A 1 73  ? 34.29262 37.05919 -15.99103 1.000 15.07608 ? 69  GLU A C    1 
ATOM   1122 O  O    . GLU A 1 73  ? 34.70784 37.11682 -14.82607 1.000 15.97024 ? 69  GLU A O    1 
ATOM   1123 C  CB   . GLU A 1 73  ? 36.03188 36.80957 -17.76830 1.000 17.19394 ? 69  GLU A CB   1 
ATOM   1124 C  CG   . GLU A 1 73  ? 37.32658 37.00909 -16.96002 1.000 20.36005 ? 69  GLU A CG   1 
ATOM   1125 C  CD   . GLU A 1 73  ? 37.34240 38.21543 -16.04897 1.000 26.20859 ? 69  GLU A CD   1 
ATOM   1126 O  OE1  . GLU A 1 73  ? 36.67472 39.22067 -16.36624 1.000 29.40784 ? 69  GLU A OE1  1 
ATOM   1127 O  OE2  . GLU A 1 73  ? 38.05752 38.16759 -15.01831 1.000 30.91857 ? 69  GLU A OE2  1 
ATOM   1128 H  H    . GLU A 1 73  ? 34.07653 35.78323 -18.73311 1.000 16.77081 ? 69  GLU A H    1 
ATOM   1129 H  HA   . GLU A 1 73  ? 35.31884 35.36805 -16.48256 1.000 18.06948 ? 69  GLU A HA   1 
ATOM   1130 H  HB2  . GLU A 1 73  ? 36.24894 36.28015 -18.55156 1.000 20.65746 ? 69  GLU A HB2  1 
ATOM   1131 H  HB3  . GLU A 1 73  ? 35.71169 37.68468 -18.03768 1.000 20.65746 ? 69  GLU A HB3  1 
ATOM   1132 H  HG2  . GLU A 1 73  ? 37.46417 36.22593 -16.40448 1.000 24.45679 ? 69  GLU A HG2  1 
ATOM   1133 H  HG3  . GLU A 1 73  ? 38.06379 37.10785 -17.58265 1.000 24.45679 ? 69  GLU A HG3  1 
ATOM   1134 N  N    . ASN A 1 74  ? 33.31287 37.84081 -16.43501 1.000 14.18807 ? 70  ASN A N    1 
ATOM   1135 C  CA   . ASN A 1 74  ? 32.70573 38.88569 -15.62046 1.000 14.15125 ? 70  ASN A CA   1 
ATOM   1136 C  C    . ASN A 1 74  ? 31.40916 39.30671 -16.30907 1.000 13.02419 ? 70  ASN A C    1 
ATOM   1137 O  O    . ASN A 1 74  ? 31.39831 40.26204 -17.10369 1.000 13.92669 ? 70  ASN A O    1 
ATOM   1138 C  CB   . ASN A 1 74  ? 33.65605 40.06549 -15.44698 1.000 16.16754 ? 70  ASN A CB   1 
ATOM   1139 C  CG   . ASN A 1 74  ? 33.15297 41.07925 -14.44797 1.000 19.85182 ? 70  ASN A CG   1 
ATOM   1140 O  OD1  . ASN A 1 74  ? 31.96197 41.13410 -14.12554 1.000 21.93650 ? 70  ASN A OD1  1 
ATOM   1141 N  ND2  . ASN A 1 74  ? 34.06708 41.88155 -13.93348 1.000 23.87312 ? 70  ASN A ND2  1 
ATOM   1142 H  H    . ASN A 1 74  ? 32.97471 37.78373 -17.22368 1.000 17.05041 ? 70  ASN A H    1 
ATOM   1143 H  HA   . ASN A 1 74  ? 32.50701 38.56191 -14.72795 1.000 17.00623 ? 70  ASN A HA   1 
ATOM   1144 H  HB2  . ASN A 1 74  ? 34.51378 39.73713 -15.13492 1.000 19.42577 ? 70  ASN A HB2  1 
ATOM   1145 H  HB3  . ASN A 1 74  ? 33.76294 40.51337 -16.30073 1.000 19.42577 ? 70  ASN A HB3  1 
ATOM   1146 H  HD21 . ASN A 1 74  ? 33.83991 42.47962 -13.35876 1.000 28.67247 ? 70  ASN A HD21 1 
ATOM   1147 H  HD22 . ASN A 1 74  ? 34.88954 41.80595 -14.17316 1.000 28.67247 ? 70  ASN A HD22 1 
ATOM   1148 N  N    . PRO A 1 75  ? 30.30222 38.62016 -16.02816 1.000 12.50013 ? 71  PRO A N    1 
ATOM   1149 C  CA   . PRO A 1 75  ? 29.06871 38.89309 -16.78321 1.000 12.56371 ? 71  PRO A CA   1 
ATOM   1150 C  C    . PRO A 1 75  ? 28.59652 40.33021 -16.71246 1.000 13.24788 ? 71  PRO A C    1 
ATOM   1151 O  O    . PRO A 1 75  ? 28.21624 40.89948 -17.74669 1.000 13.68209 ? 71  PRO A O    1 
ATOM   1152 C  CB   . PRO A 1 75  ? 28.07437 37.89230 -16.18640 1.000 13.73186 ? 71  PRO A CB   1 
ATOM   1153 C  CG   . PRO A 1 75  ? 28.94793 36.71355 -15.80723 1.000 14.17239 ? 71  PRO A CG   1 
ATOM   1154 C  CD   . PRO A 1 75  ? 30.21686 37.34517 -15.28887 1.000 13.84246 ? 71  PRO A CD   1 
ATOM   1155 H  HA   . PRO A 1 75  ? 29.20322 38.67679 -17.71917 1.000 15.10118 ? 71  PRO A HA   1 
ATOM   1156 H  HB2  . PRO A 1 75  ? 27.63895 38.27377 -15.40807 1.000 16.50296 ? 71  PRO A HB2  1 
ATOM   1157 H  HB3  . PRO A 1 75  ? 27.41093 37.64156 -16.84812 1.000 16.50296 ? 71  PRO A HB3  1 
ATOM   1158 H  HG2  . PRO A 1 75  ? 28.51455 36.18435 -15.11945 1.000 17.03159 ? 71  PRO A HG2  1 
ATOM   1159 H  HG3  . PRO A 1 75  ? 29.12410 36.16405 -16.58691 1.000 17.03159 ? 71  PRO A HG3  1 
ATOM   1160 H  HD2  . PRO A 1 75  ? 30.15562 37.50524 -14.33413 1.000 16.63568 ? 71  PRO A HD2  1 
ATOM   1161 H  HD3  . PRO A 1 75  ? 30.98386 36.78385 -15.48263 1.000 16.63568 ? 71  PRO A HD3  1 
ATOM   1162 N  N    . LYS A 1 76  ? 28.64652 40.95294 -15.53479 1.000 14.95710 ? 72  LYS A N    1 
ATOM   1163 C  CA   . LYS A 1 76  ? 28.12012 42.30450 -15.41730 1.000 16.52149 ? 72  LYS A CA   1 
ATOM   1164 C  C    . LYS A 1 76  ? 28.99136 43.34605 -16.09599 1.000 16.29256 ? 72  LYS A C    1 
ATOM   1165 O  O    . LYS A 1 76  ? 28.51546 44.44091 -16.38326 1.000 17.81741 ? 72  LYS A O    1 
ATOM   1166 C  CB   . LYS A 1 76  ? 27.89107 42.67532 -13.95716 1.000 18.60123 ? 72  LYS A CB   1 
ATOM   1167 C  CG   . LYS A 1 76  ? 29.14176 42.81871 -13.10949 1.000 24.50116 ? 72  LYS A CG   1 
ATOM   1168 C  CD   . LYS A 1 76  ? 28.75831 43.32672 -11.72489 1.000 32.75753 ? 72  LYS A CD   1 
ATOM   1169 C  CE   . LYS A 1 76  ? 29.70096 42.83374 -10.64244 1.000 40.74788 ? 72  LYS A CE   1 
ATOM   1170 N  NZ   . LYS A 1 76  ? 29.45638 41.40234 -10.26606 1.000 44.30280 ? 72  LYS A NZ   1 
ATOM   1171 H  H    . LYS A 1 76  ? 28.97126 40.62282 -14.81011 1.000 17.97325 ? 72  LYS A H    1 
ATOM   1172 H  HA   . LYS A 1 76  ? 27.25608 42.32178 -15.85779 1.000 19.85051 ? 72  LYS A HA   1 
ATOM   1173 H  HB2  . LYS A 1 76  ? 27.42537 43.52574 -13.92886 1.000 22.34620 ? 72  LYS A HB2  1 
ATOM   1174 H  HB3  . LYS A 1 76  ? 27.34530 41.98449 -13.55000 1.000 22.34620 ? 72  LYS A HB3  1 
ATOM   1175 H  HG2  . LYS A 1 76  ? 29.57817 41.95728 -13.01792 1.000 29.42612 ? 72  LYS A HG2  1 
ATOM   1176 H  HG3  . LYS A 1 76  ? 29.74720 43.45528 -13.52073 1.000 29.42612 ? 72  LYS A HG3  1 
ATOM   1177 H  HD2  . LYS A 1 76  ? 28.78184 44.29644 -11.72494 1.000 39.33376 ? 72  LYS A HD2  1 
ATOM   1178 H  HD3  . LYS A 1 76  ? 27.86488 43.01656 -11.50930 1.000 39.33376 ? 72  LYS A HD3  1 
ATOM   1179 H  HE2  . LYS A 1 76  ? 30.61423 42.90787 -10.96077 1.000 48.92218 ? 72  LYS A HE2  1 
ATOM   1180 H  HE3  . LYS A 1 76  ? 29.58149 43.37699 -9.84776  1.000 48.92218 ? 72  LYS A HE3  1 
ATOM   1181 H  HZ1  . LYS A 1 76  ? 29.02662 40.98387 -10.92355 1.000 53.18809 ? 72  LYS A HZ1  1 
ATOM   1182 H  HZ2  . LYS A 1 76  ? 30.23106 40.98968 -10.11880 1.000 53.18809 ? 72  LYS A HZ2  1 
ATOM   1183 H  HZ3  . LYS A 1 76  ? 28.96258 41.36211 -9.52671  1.000 53.18809 ? 72  LYS A HZ3  1 
ATOM   1184 N  N    A LYS A 1 77  ? 30.26729 43.05040 -16.31394 0.576 14.29502 ? 73  LYS A N    1 
ATOM   1185 N  N    B LYS A 1 77  ? 30.26595 43.05064 -16.33333 0.424 15.18959 ? 73  LYS A N    1 
ATOM   1186 C  CA   A LYS A 1 77  ? 31.09389 43.95019 -17.10041 0.576 14.28220 ? 73  LYS A CA   1 
ATOM   1187 C  CA   B LYS A 1 77  ? 31.07570 43.98266 -17.10484 0.424 14.37647 ? 73  LYS A CA   1 
ATOM   1188 C  C    A LYS A 1 77  ? 30.70868 43.89880 -18.57001 0.576 13.62100 ? 73  LYS A C    1 
ATOM   1189 C  C    B LYS A 1 77  ? 30.74296 43.90024 -18.58858 0.424 14.32127 ? 73  LYS A C    1 
ATOM   1190 O  O    A LYS A 1 77  ? 30.67723 44.93310 -19.24569 0.576 14.62421 ? 73  LYS A O    1 
ATOM   1191 O  O    B LYS A 1 77  ? 30.76307 44.91817 -19.29122 0.424 15.74174 ? 73  LYS A O    1 
ATOM   1192 C  CB   A LYS A 1 77  ? 32.55242 43.55342 -16.91452 0.576 16.08973 ? 73  LYS A CB   1 
ATOM   1193 C  CB   B LYS A 1 77  ? 32.55926 43.70588 -16.86580 0.424 14.45809 ? 73  LYS A CB   1 
ATOM   1194 C  CG   A LYS A 1 77  ? 33.55967 44.33084 -17.73353 0.576 20.34409 ? 73  LYS A CG   1 
ATOM   1195 C  CG   B LYS A 1 77  ? 33.52309 44.67764 -17.54006 0.424 14.64479 ? 73  LYS A CG   1 
ATOM   1196 C  CD   A LYS A 1 77  ? 34.96435 43.95877 -17.29183 0.576 22.59564 ? 73  LYS A CD   1 
ATOM   1197 C  CD   B LYS A 1 77  ? 33.34614 46.12032 -17.07112 0.424 14.75548 ? 73  LYS A CD   1 
ATOM   1198 C  CE   A LYS A 1 77  ? 36.03939 44.47045 -18.22040 0.576 25.08028 ? 73  LYS A CE   1 
ATOM   1199 C  CE   B LYS A 1 77  ? 34.35930 47.04600 -17.71531 0.424 14.23804 ? 73  LYS A CE   1 
ATOM   1200 N  NZ   A LYS A 1 77  ? 37.36115 43.92914 -17.83271 0.576 23.70030 ? 73  LYS A NZ   1 
ATOM   1201 N  NZ   B LYS A 1 77  ? 34.17866 47.14907 -19.20152 0.424 12.34462 ? 73  LYS A NZ   1 
ATOM   1202 H  H    A LYS A 1 77  ? 30.67188 42.34914 -16.02386 0.576 17.17875 ? 73  LYS A H    1 
ATOM   1203 H  H    B LYS A 1 77  ? 30.67300 42.34103 -16.06804 0.424 18.25224 ? 73  LYS A H    1 
ATOM   1204 H  HA   A LYS A 1 77  ? 30.97342 44.86323 -16.79587 0.576 17.16337 ? 73  LYS A HA   1 
ATOM   1205 H  HA   B LYS A 1 77  ? 30.89348 44.88752 -16.80665 0.424 17.27649 ? 73  LYS A HA   1 
ATOM   1206 H  HB2  A LYS A 1 77  ? 32.78413 43.67860 -15.98096 0.576 19.33241 ? 73  LYS A HB2  1 
ATOM   1207 H  HB2  B LYS A 1 77  ? 32.72773 43.74702 -15.91143 0.424 17.37444 ? 73  LYS A HB2  1 
ATOM   1208 H  HB3  A LYS A 1 77  ? 32.64574 42.61888 -17.15708 0.576 19.33241 ? 73  LYS A HB3  1 
ATOM   1209 H  HB3  B LYS A 1 77  ? 32.76219 42.81838 -17.20056 0.424 17.37444 ? 73  LYS A HB3  1 
ATOM   1210 H  HG2  A LYS A 1 77  ? 33.45837 44.11286 -18.67327 0.576 24.43764 ? 73  LYS A HG2  1 
ATOM   1211 H  HG2  B LYS A 1 77  ? 34.43325 44.40869 -17.33961 0.424 17.59848 ? 73  LYS A HG2  1 
ATOM   1212 H  HG3  A LYS A 1 77  ? 33.43003 45.28252 -17.59786 0.576 24.43764 ? 73  LYS A HG3  1 
ATOM   1213 H  HG3  B LYS A 1 77  ? 33.37397 44.65539 -18.49827 0.424 17.59848 ? 73  LYS A HG3  1 
ATOM   1214 H  HD2  A LYS A 1 77  ? 35.12736 44.33526 -16.41286 0.576 27.13950 ? 73  LYS A HD2  1 
ATOM   1215 H  HD2  B LYS A 1 77  ? 32.45781 46.42841 -17.30955 0.424 17.73131 ? 73  LYS A HD2  1 
ATOM   1216 H  HD3  A LYS A 1 77  ? 35.03715 42.99212 -17.25741 0.576 27.13950 ? 73  LYS A HD3  1 
ATOM   1217 H  HD3  B LYS A 1 77  ? 33.46461 46.16176 -16.10927 0.424 17.73131 ? 73  LYS A HD3  1 
ATOM   1218 H  HE2  A LYS A 1 77  ? 35.84478 44.19001 -19.12836 0.576 30.12106 ? 73  LYS A HE2  1 
ATOM   1219 H  HE2  B LYS A 1 77  ? 34.26239 47.93438 -17.33809 0.424 17.11038 ? 73  LYS A HE2  1 
ATOM   1220 H  HE3  A LYS A 1 77  ? 36.07585 45.43859 -18.17282 0.576 30.12106 ? 73  LYS A HE3  1 
ATOM   1221 H  HE3  B LYS A 1 77  ? 35.25217 46.70817 -17.54342 0.424 17.11038 ? 73  LYS A HE3  1 
ATOM   1222 H  HZ1  A LYS A 1 77  ? 37.99796 44.28838 -18.34018 0.576 28.46509 ? 73  LYS A HZ1  1 
ATOM   1223 H  HZ1  B LYS A 1 77  ? 34.51442 47.91878 -19.49631 0.424 14.83827 ? 73  LYS A HZ1  1 
ATOM   1224 H  HZ2  A LYS A 1 77  ? 37.52978 44.11948 -16.97981 0.576 28.46509 ? 73  LYS A HZ2  1 
ATOM   1225 H  HZ2  B LYS A 1 77  ? 34.59845 46.47687 -19.60652 0.424 14.83827 ? 73  LYS A HZ2  1 
ATOM   1226 H  HZ3  A LYS A 1 77  ? 37.37129 43.04556 -17.93892 0.576 28.46509 ? 73  LYS A HZ3  1 
ATOM   1227 H  HZ3  B LYS A 1 77  ? 33.31319 47.11427 -19.40610 0.424 14.83827 ? 73  LYS A HZ3  1 
ATOM   1228 N  N    . TYR A 1 78  ? 30.45320 42.69805 -19.08375 1.000 13.41581 ? 74  TYR A N    1 
ATOM   1229 C  CA   . TYR A 1 78  ? 30.12695 42.55214 -20.49367 1.000 13.04682 ? 74  TYR A CA   1 
ATOM   1230 C  C    . TYR A 1 78  ? 28.72268 43.05289 -20.80958 1.000 12.72885 ? 74  TYR A C    1 
ATOM   1231 O  O    . TYR A 1 78  ? 28.50013 43.63178 -21.88373 1.000 14.02324 ? 74  TYR A O    1 
ATOM   1232 C  CB   . TYR A 1 78  ? 30.28829 41.09297 -20.88531 1.000 13.75356 ? 74  TYR A CB   1 
ATOM   1233 C  CG   . TYR A 1 78  ? 30.30694 40.83216 -22.38747 1.000 13.50701 ? 74  TYR A CG   1 
ATOM   1234 C  CD1  . TYR A 1 78  ? 31.29644 41.37019 -23.20506 1.000 14.18063 ? 74  TYR A CD1  1 
ATOM   1235 C  CD2  . TYR A 1 78  ? 29.34680 40.02737 -22.98297 1.000 13.38409 ? 74  TYR A CD2  1 
ATOM   1236 C  CE1  . TYR A 1 78  ? 31.32069 41.11425 -24.56196 1.000 14.47587 ? 74  TYR A CE1  1 
ATOM   1237 C  CE2  . TYR A 1 78  ? 29.36358 39.78020 -24.34277 1.000 13.85224 ? 74  TYR A CE2  1 
ATOM   1238 C  CZ   . TYR A 1 78  ? 30.36158 40.30505 -25.12624 1.000 13.65582 ? 74  TYR A CZ   1 
ATOM   1239 O  OH   . TYR A 1 78  ? 30.36685 40.04071 -26.47973 1.000 15.43618 ? 74  TYR A OH   1 
ATOM   1240 H  H    . TYR A 1 78  ? 30.46198 41.95986 -18.64263 1.000 16.12371 ? 74  TYR A H    1 
ATOM   1241 H  HA   . TYR A 1 78  ? 30.73926 43.08548 -21.02426 1.000 15.68091 ? 74  TYR A HA   1 
ATOM   1242 H  HB2  . TYR A 1 78  ? 31.12705 40.76783 -20.52246 1.000 16.52901 ? 74  TYR A HB2  1 
ATOM   1243 H  HB3  . TYR A 1 78  ? 29.54790 40.59020 -20.51122 1.000 16.52901 ? 74  TYR A HB3  1 
ATOM   1244 H  HD1  . TYR A 1 78  ? 31.95324 41.91191 -22.83084 1.000 17.04149 ? 74  TYR A HD1  1 
ATOM   1245 H  HD2  . TYR A 1 78  ? 28.67988 39.64733 -22.45791 1.000 16.08563 ? 74  TYR A HD2  1 
ATOM   1246 H  HE1  . TYR A 1 78  ? 31.98511 41.48875 -25.09413 1.000 17.39577 ? 74  TYR A HE1  1 
ATOM   1247 H  HE2  . TYR A 1 78  ? 28.69769 39.25744 -24.72775 1.000 16.64741 ? 74  TYR A HE2  1 
ATOM   1248 H  HH   . TYR A 1 78  ? 30.92425 40.53565 -26.86696 1.000 18.54815 ? 74  TYR A HH   1 
ATOM   1249 N  N    . ILE A 1 79  ? 27.77308 42.81793 -19.90246 1.000 12.92648 ? 75  ILE A N    1 
ATOM   1250 C  CA   . ILE A 1 79  ? 26.39157 43.25581 -20.07489 1.000 13.17561 ? 75  ILE A CA   1 
ATOM   1251 C  C    . ILE A 1 79  ? 25.99408 43.98496 -18.79856 1.000 12.77152 ? 75  ILE A C    1 
ATOM   1252 O  O    . ILE A 1 79  ? 25.30461 43.41403 -17.93244 1.000 12.94885 ? 75  ILE A O    1 
ATOM   1253 C  CB   . ILE A 1 79  ? 25.43374 42.10503 -20.42460 1.000 13.87684 ? 75  ILE A CB   1 
ATOM   1254 C  CG1  . ILE A 1 79  ? 25.99151 41.28641 -21.60923 1.000 13.88118 ? 75  ILE A CG1  1 
ATOM   1255 C  CG2  . ILE A 1 79  ? 24.04454 42.67010 -20.73120 1.000 15.21595 ? 75  ILE A CG2  1 
ATOM   1256 C  CD1  . ILE A 1 79  ? 25.05601 40.19431 -22.10741 1.000 14.29235 ? 75  ILE A CD1  1 
ATOM   1257 H  H    . ILE A 1 79  ? 27.90969 42.39794 -19.16453 1.000 15.53650 ? 75  ILE A H    1 
ATOM   1258 H  HA   . ILE A 1 79  ? 26.33573 43.87004 -20.82356 1.000 15.83546 ? 75  ILE A HA   1 
ATOM   1259 H  HB   . ILE A 1 79  ? 25.35796 41.50501 -19.66623 1.000 16.67694 ? 75  ILE A HB   1 
ATOM   1260 H  HG12 . ILE A 1 79  ? 26.16131 41.88900 -22.35014 1.000 16.68214 ? 75  ILE A HG12 1 
ATOM   1261 H  HG13 . ILE A 1 79  ? 26.81796 40.86160 -21.33099 1.000 16.68214 ? 75  ILE A HG13 1 
ATOM   1262 H  HG21 . ILE A 1 79  ? 23.41230 41.93715 -20.79404 1.000 18.28387 ? 75  ILE A HG21 1 
ATOM   1263 H  HG22 . ILE A 1 79  ? 23.78354 43.27171 -20.01647 1.000 18.28387 ? 75  ILE A HG22 1 
ATOM   1264 H  HG23 . ILE A 1 79  ? 24.07799 43.15117 -21.57283 1.000 18.28387 ? 75  ILE A HG23 1 
ATOM   1265 H  HD11 . ILE A 1 79  ? 25.53933 39.62083 -22.72257 1.000 17.17555 ? 75  ILE A HD11 1 
ATOM   1266 H  HD12 . ILE A 1 79  ? 24.74287 39.67662 -21.34923 1.000 17.17555 ? 75  ILE A HD12 1 
ATOM   1267 H  HD13 . ILE A 1 79  ? 24.30343 40.60563 -22.56057 1.000 17.17555 ? 75  ILE A HD13 1 
ATOM   1268 N  N    . PRO A 1 80  ? 26.37278 45.24916 -18.64509 1.000 13.37094 ? 76  PRO A N    1 
ATOM   1269 C  CA   . PRO A 1 80  ? 25.96589 45.98256 -17.43878 1.000 14.26907 ? 76  PRO A CA   1 
ATOM   1270 C  C    . PRO A 1 80  ? 24.44521 46.02777 -17.29653 1.000 13.77778 ? 76  PRO A C    1 
ATOM   1271 O  O    . PRO A 1 80  ? 23.71305 46.23760 -18.27153 1.000 15.91602 ? 76  PRO A O    1 
ATOM   1272 C  CB   . PRO A 1 80  ? 26.58019 47.36710 -17.65037 1.000 14.58464 ? 76  PRO A CB   1 
ATOM   1273 C  CG   . PRO A 1 80  ? 27.76988 47.11238 -18.54357 1.000 16.06092 ? 76  PRO A CG   1 
ATOM   1274 C  CD   . PRO A 1 80  ? 27.31255 46.03178 -19.47359 1.000 15.06488 ? 76  PRO A CD   1 
ATOM   1275 H  HA   . PRO A 1 80  ? 26.34442 45.58007 -16.64152 1.000 17.14761 ? 76  PRO A HA   1 
ATOM   1276 H  HB2  . PRO A 1 80  ? 25.93887 47.95405 -18.08060 1.000 17.52629 ? 76  PRO A HB2  1 
ATOM   1277 H  HB3  . PRO A 1 80  ? 26.85543 47.74314 -16.79965 1.000 17.52629 ? 76  PRO A HB3  1 
ATOM   1278 H  HG2  . PRO A 1 80  ? 27.99874 47.91887 -19.03153 1.000 19.29784 ? 76  PRO A HG2  1 
ATOM   1279 H  HG3  . PRO A 1 80  ? 28.52749 46.81901 -18.01362 1.000 19.29784 ? 76  PRO A HG3  1 
ATOM   1280 H  HD2  . PRO A 1 80  ? 26.86174 46.40816 -20.24561 1.000 18.10259 ? 76  PRO A HD2  1 
ATOM   1281 H  HD3  . PRO A 1 80  ? 28.05961 45.48351 -19.76029 1.000 18.10259 ? 76  PRO A HD3  1 
ATOM   1282 N  N    . GLY A 1 81  ? 23.95969 45.76099 -16.08255 1.000 16.23190 ? 77  GLY A N    1 
ATOM   1283 C  CA   . GLY A 1 81  ? 22.52759 45.67379 -15.84603 1.000 18.18920 ? 77  GLY A CA   1 
ATOM   1284 C  C    . GLY A 1 81  ? 21.90116 44.30178 -16.03921 1.000 17.12971 ? 77  GLY A C    1 
ATOM   1285 O  O    . GLY A 1 81  ? 20.69897 44.14545 -15.78049 1.000 19.70695 ? 77  GLY A O    1 
ATOM   1286 H  H    . GLY A 1 81  ? 24.44339 45.62760 -15.38409 1.000 19.50301 ? 77  GLY A H    1 
ATOM   1287 H  HA2  . GLY A 1 81  ? 22.35129 45.94780 -14.93239 1.000 21.85177 ? 77  GLY A HA2  1 
ATOM   1288 H  HA3  . GLY A 1 81  ? 22.07989 46.28556 -16.45118 1.000 21.85177 ? 77  GLY A HA3  1 
ATOM   1289 N  N    . THR A 1 82  ? 22.65497 43.29706 -16.47090 1.000 16.69799 ? 78  THR A N    1 
ATOM   1290 C  CA   . THR A 1 82  ? 22.08363 41.95770 -16.59304 1.000 15.98889 ? 78  THR A CA   1 
ATOM   1291 C  C    . THR A 1 82  ? 21.58881 41.44185 -15.23967 1.000 17.11900 ? 78  THR A C    1 
ATOM   1292 O  O    . THR A 1 82  ? 22.14006 41.77404 -14.18399 1.000 18.60673 ? 78  THR A O    1 
ATOM   1293 C  CB   . THR A 1 82  ? 23.11281 40.98321 -17.18362 1.000 14.61243 ? 78  THR A CB   1 
ATOM   1294 O  OG1  . THR A 1 82  ? 22.49632 39.68785 -17.37788 1.000 15.77525 ? 78  THR A OG1  1 
ATOM   1295 C  CG2  . THR A 1 82  ? 24.34941 40.81262 -16.32457 1.000 17.87826 ? 78  THR A CG2  1 
ATOM   1296 H  H    . THR A 1 82  ? 23.48275 43.35924 -16.69566 1.000 20.06232 ? 78  THR A H    1 
ATOM   1297 H  HA   . THR A 1 82  ? 21.32306 41.99590 -17.19385 1.000 19.21139 ? 78  THR A HA   1 
ATOM   1298 H  HB   . THR A 1 82  ? 23.41159 41.35610 -18.02777 1.000 17.55965 ? 78  THR A HB   1 
ATOM   1299 H  HG1  . THR A 1 82  ? 21.78803 39.77044 -17.82185 1.000 18.95503 ? 78  THR A HG1  1 
ATOM   1300 H  HG21 . THR A 1 82  ? 25.02516 40.31492 -16.81094 1.000 21.47864 ? 78  THR A HG21 1 
ATOM   1301 H  HG22 . THR A 1 82  ? 24.70941 41.68094 -16.08514 1.000 21.47864 ? 78  THR A HG22 1 
ATOM   1302 H  HG23 . THR A 1 82  ? 24.12587 40.32997 -15.51341 1.000 21.47864 ? 78  THR A HG23 1 
ATOM   1303 N  N    . LYS A 1 83  ? 20.54652 40.59477 -15.26279 1.000 17.37225 ? 79  LYS A N    1 
ATOM   1304 C  CA   A LYS A 1 83  ? 20.04998 39.98505 -14.03377 0.513 18.49521 ? 79  LYS A CA   1 
ATOM   1305 C  CA   B LYS A 1 83  ? 20.05230 39.98644 -14.03265 0.487 18.73582 ? 79  LYS A CA   1 
ATOM   1306 C  C    . LYS A 1 83  ? 20.65585 38.61313 -13.76743 1.000 17.20705 ? 79  LYS A C    1 
ATOM   1307 O  O    . LYS A 1 83  ? 20.22761 37.93565 -12.82594 1.000 19.73444 ? 79  LYS A O    1 
ATOM   1308 C  CB   A LYS A 1 83  ? 18.51074 39.94133 -13.99367 0.513 19.32193 ? 79  LYS A CB   1 
ATOM   1309 C  CB   B LYS A 1 83  ? 18.51484 39.95146 -13.98579 0.487 20.09877 ? 79  LYS A CB   1 
ATOM   1310 C  CG   A LYS A 1 83  ? 17.83298 39.04440 -15.00855 0.513 19.83532 ? 79  LYS A CG   1 
ATOM   1311 C  CG   B LYS A 1 83  ? 17.83388 38.97689 -14.91849 0.487 21.68322 ? 79  LYS A CG   1 
ATOM   1312 C  CD   A LYS A 1 83  ? 16.31851 39.19671 -14.94477 0.513 19.89814 ? 79  LYS A CD   1 
ATOM   1313 C  CD   B LYS A 1 83  ? 16.33970 38.96010 -14.67317 0.487 22.57364 ? 79  LYS A CD   1 
ATOM   1314 C  CE   A LYS A 1 83  ? 15.63231 38.51069 -16.12052 0.513 20.35925 ? 79  LYS A CE   1 
ATOM   1315 C  CE   B LYS A 1 83  ? 15.65805 37.88134 -15.49171 0.487 22.76017 ? 79  LYS A CE   1 
ATOM   1316 N  NZ   A LYS A 1 83  ? 14.15030 38.71261 -16.09698 0.513 21.31504 ? 79  LYS A NZ   1 
ATOM   1317 N  NZ   B LYS A 1 83  ? 15.88208 38.08080 -16.94118 0.487 20.23468 ? 79  LYS A NZ   1 
ATOM   1318 H  H    . LYS A 1 83  ? 20.12127 40.36590 -15.97439 1.000 20.87142 ? 79  LYS A H    1 
ATOM   1319 H  HA   . LYS A 1 83  ? 20.30688 40.55867 -13.29494 1.000 22.50771 ? 79  LYS A HA   1 
ATOM   1320 H  HB2  A LYS A 1 83  ? 18.24121 39.63089 -13.11510 0.513 23.21105 ? 79  LYS A HB2  1 
ATOM   1321 H  HB2  B LYS A 1 83  ? 18.24635 39.71667 -13.08374 0.487 24.14325 ? 79  LYS A HB2  1 
ATOM   1322 H  HB3  A LYS A 1 83  ? 18.18005 40.84081 -14.14357 0.513 23.21105 ? 79  LYS A HB3  1 
ATOM   1323 H  HB3  B LYS A 1 83  ? 18.18655 40.83627 -14.20994 0.487 24.14325 ? 79  LYS A HB3  1 
ATOM   1324 H  HG2  A LYS A 1 83  ? 18.12852 39.28448 -15.90069 0.513 23.82712 ? 79  LYS A HG2  1 
ATOM   1325 H  HG2  B LYS A 1 83  ? 17.99274 39.24225 -15.83786 0.487 26.04459 ? 79  LYS A HG2  1 
ATOM   1326 H  HG3  A LYS A 1 83  ? 18.05671 38.11903 -14.82273 0.513 23.82712 ? 79  LYS A HG3  1 
ATOM   1327 H  HG3  B LYS A 1 83  ? 18.18174 38.08435 -14.76597 0.487 26.04459 ? 79  LYS A HG3  1 
ATOM   1328 H  HD2  A LYS A 1 83  ? 15.99033 38.79526 -14.12499 0.513 23.90249 ? 79  LYS A HD2  1 
ATOM   1329 H  HD2  B LYS A 1 83  ? 16.16959 38.78462 -13.73446 0.487 27.11310 ? 79  LYS A HD2  1 
ATOM   1330 H  HD3  A LYS A 1 83  ? 16.09001 40.13914 -14.96728 0.513 23.90249 ? 79  LYS A HD3  1 
ATOM   1331 H  HD3  B LYS A 1 83  ? 15.96268 39.81792 -14.92395 0.487 27.11310 ? 79  LYS A HD3  1 
ATOM   1332 H  HE2  A LYS A 1 83  ? 15.97543 38.87867 -16.94983 0.513 24.45583 ? 79  LYS A HE2  1 
ATOM   1333 H  HE2  B LYS A 1 83  ? 16.01642 37.01479 -15.24361 0.487 27.33693 ? 79  LYS A HE2  1 
ATOM   1334 H  HE3  A LYS A 1 83  ? 15.80924 37.55774 -16.08211 0.513 24.45583 ? 79  LYS A HE3  1 
ATOM   1335 H  HE3  B LYS A 1 83  ? 14.70297 37.90574 -15.32401 0.487 27.33693 ? 79  LYS A HE3  1 
ATOM   1336 H  HZ1  A LYS A 1 83  ? 13.81536 38.41952 -15.32626 0.513 25.60277 ? 79  LYS A HZ1  1 
ATOM   1337 H  HZ1  B LYS A 1 83  ? 15.68430 38.91856 -17.16731 0.487 24.30635 ? 79  LYS A HZ1  1 
ATOM   1338 H  HZ2  A LYS A 1 83  ? 13.95950 39.57749 -16.18454 0.513 25.60277 ? 79  LYS A HZ2  1 
ATOM   1339 H  HZ2  B LYS A 1 83  ? 16.73416 37.92082 -17.14234 0.487 24.30635 ? 79  LYS A HZ2  1 
ATOM   1340 H  HZ3  A LYS A 1 83  ? 13.77132 38.26407 -16.76578 0.513 25.60277 ? 79  LYS A HZ3  1 
ATOM   1341 H  HZ3  B LYS A 1 83  ? 15.36601 37.52608 -17.40813 0.487 24.30635 ? 79  LYS A HZ3  1 
ATOM   1342 N  N    . MET A 1 84  ? 21.64047 38.19383 -14.56240 1.000 16.97496 ? 80  MET A N    1 
ATOM   1343 C  CA   . MET A 1 84  ? 22.37829 36.96850 -14.27825 1.000 16.75911 ? 80  MET A CA   1 
ATOM   1344 C  C    . MET A 1 84  ? 23.35442 37.27565 -13.15323 1.000 18.36620 ? 80  MET A C    1 
ATOM   1345 O  O    . MET A 1 84  ? 24.33370 38.01835 -13.34831 1.000 19.76225 ? 80  MET A O    1 
ATOM   1346 C  CB   . MET A 1 84  ? 23.13600 36.48762 -15.51146 1.000 16.58183 ? 80  MET A CB   1 
ATOM   1347 C  CG   . MET A 1 84  ? 24.09335 35.36150 -15.20401 1.000 15.51580 ? 80  MET A CG   1 
ATOM   1348 S  SD   . MET A 1 84  ? 24.58845 34.36059 -16.61292 1.000 14.56020 ? 80  MET A SD   1 
ATOM   1349 C  CE   . MET A 1 84  ? 26.27465 33.94662 -16.19865 1.000 15.10583 ? 80  MET A CE   1 
ATOM   1350 H  H    . MET A 1 84  ? 21.89837 38.60409 -15.27287 1.000 20.39468 ? 80  MET A H    1 
ATOM   1351 H  HA   . MET A 1 84  ? 21.75572 36.27064 -14.02074 1.000 20.13566 ? 80  MET A HA   1 
ATOM   1352 H  HB2  . MET A 1 84  ? 22.49862 36.16920 -16.16969 1.000 19.92292 ? 80  MET A HB2  1 
ATOM   1353 H  HB3  . MET A 1 84  ? 23.64799 37.22656 -15.87580 1.000 19.92292 ? 80  MET A HB3  1 
ATOM   1354 H  HG2  . MET A 1 84  ? 24.90016 35.74190 -14.82290 1.000 18.64369 ? 80  MET A HG2  1 
ATOM   1355 H  HG3  . MET A 1 84  ? 23.67140 34.76824 -14.56299 1.000 18.64369 ? 80  MET A HG3  1 
ATOM   1356 H  HE1  . MET A 1 84  ? 26.64293 33.38477 -16.89836 1.000 18.15172 ? 80  MET A HE1  1 
ATOM   1357 H  HE2  . MET A 1 84  ? 26.79145 34.76414 -16.12454 1.000 18.15172 ? 80  MET A HE2  1 
ATOM   1358 H  HE3  . MET A 1 84  ? 26.28454 33.47125 -15.35318 1.000 18.15172 ? 80  MET A HE3  1 
ATOM   1359 N  N    . ILE A 1 85  ? 23.07788 36.71674 -11.97556 1.000 19.20386 ? 81  ILE A N    1 
ATOM   1360 C  CA   . ILE A 1 85  ? 23.89462 36.93089 -10.78730 1.000 20.32716 ? 81  ILE A CA   1 
ATOM   1361 C  C    . ILE A 1 85  ? 24.92321 35.80413 -10.75482 1.000 22.20398 ? 81  ILE A C    1 
ATOM   1362 O  O    . ILE A 1 85  ? 24.64927 34.69920 -10.28643 1.000 23.47595 ? 81  ILE A O    1 
ATOM   1363 C  CB   . ILE A 1 85  ? 23.04176 36.98921 -9.51707  1.000 22.59315 ? 81  ILE A CB   1 
ATOM   1364 C  CG1  . ILE A 1 85  ? 21.83271 37.92245 -9.71014  1.000 25.71346 ? 81  ILE A CG1  1 
ATOM   1365 C  CG2  . ILE A 1 85  ? 23.88966 37.42808 -8.31617  1.000 24.35974 ? 81  ILE A CG2  1 
ATOM   1366 C  CD1  . ILE A 1 85  ? 22.16415 39.30701 -10.26647 1.000 30.58537 ? 81  ILE A CD1  1 
ATOM   1367 H  H    . ILE A 1 85  ? 22.40567 36.19772 -11.84008 1.000 23.06935 ? 81  ILE A H    1 
ATOM   1368 H  HA   . ILE A 1 85  ? 24.37083 37.77278 -10.86044 1.000 24.41732 ? 81  ILE A HA   1 
ATOM   1369 H  HB   . ILE A 1 85  ? 22.70396 36.09726 -9.34036  1.000 27.13651 ? 81  ILE A HB   1 
ATOM   1370 H  HG12 . ILE A 1 85  ? 21.21588 37.50108 -10.32889 1.000 30.88088 ? 81  ILE A HG12 1 
ATOM   1371 H  HG13 . ILE A 1 85  ? 21.40375 38.05050 -8.84962  1.000 30.88088 ? 81  ILE A HG13 1 
ATOM   1372 H  HG21 . ILE A 1 85  ? 23.30301 37.61337 -7.56623  1.000 29.25641 ? 81  ILE A HG21 1 
ATOM   1373 H  HG22 . ILE A 1 85  ? 24.50497 36.71431 -8.08632  1.000 29.25641 ? 81  ILE A HG22 1 
ATOM   1374 H  HG23 . ILE A 1 85  ? 24.38461 38.22757 -8.55436  1.000 29.25641 ? 81  ILE A HG23 1 
ATOM   1375 H  HD11 . ILE A 1 85  ? 21.41295 39.89958 -10.10690 1.000 36.72717 ? 81  ILE A HD11 1 
ATOM   1376 H  HD12 . ILE A 1 85  ? 22.95442 39.64663 -9.81811  1.000 36.72717 ? 81  ILE A HD12 1 
ATOM   1377 H  HD13 . ILE A 1 85  ? 22.33050 39.23299 -11.21923 1.000 36.72717 ? 81  ILE A HD13 1 
ATOM   1378 N  N    . PHE A 1 86  ? 26.11095 36.09044 -11.28315 1.000 21.60540 ? 82  PHE A N    1 
ATOM   1379 C  CA   . PHE A 1 86  ? 27.17315 35.10043 -11.39089 1.000 21.74802 ? 82  PHE A CA   1 
ATOM   1380 C  C    . PHE A 1 86  ? 28.47232 35.88006 -11.36788 1.000 24.01090 ? 82  PHE A C    1 
ATOM   1381 O  O    . PHE A 1 86  ? 28.68211 36.74446 -12.22587 1.000 24.15384 ? 82  PHE A O    1 
ATOM   1382 C  CB   . PHE A 1 86  ? 27.05634 34.27458 -12.67685 1.000 22.29918 ? 82  PHE A CB   1 
ATOM   1383 C  CG   . PHE A 1 86  ? 28.12408 33.22200 -12.81208 1.000 18.88232 ? 82  PHE A CG   1 
ATOM   1384 C  CD1  . PHE A 1 86  ? 28.07545 32.08241 -12.03755 1.000 22.38172 ? 82  PHE A CD1  1 
ATOM   1385 C  CD2  . PHE A 1 86  ? 29.18754 33.39156 -13.68867 1.000 19.65247 ? 82  PHE A CD2  1 
ATOM   1386 C  CE1  . PHE A 1 86  ? 29.06456 31.12559 -12.13096 1.000 24.52624 ? 82  PHE A CE1  1 
ATOM   1387 C  CE2  . PHE A 1 86  ? 30.18063 32.43905 -13.78987 1.000 21.04710 ? 82  PHE A CE2  1 
ATOM   1388 C  CZ   . PHE A 1 86  ? 30.11635 31.30356 -13.00724 1.000 22.81294 ? 82  PHE A CZ   1 
ATOM   1389 H  H    . PHE A 1 86  ? 26.32724 36.86397 -11.59053 1.000 25.95121 ? 82  PHE A H    1 
ATOM   1390 H  HA   . PHE A 1 86  ? 27.13785 34.47670 -10.64886 1.000 26.12235 ? 82  PHE A HA   1 
ATOM   1391 H  HB2  . PHE A 1 86  ? 26.19550 33.82760 -12.68473 1.000 26.78374 ? 82  PHE A HB2  1 
ATOM   1392 H  HB3  . PHE A 1 86  ? 27.12784 34.87028 -13.43904 1.000 26.78374 ? 82  PHE A HB3  1 
ATOM   1393 H  HD1  . PHE A 1 86  ? 27.36863 31.95759 -11.44617 1.000 26.88279 ? 82  PHE A HD1  1 
ATOM   1394 H  HD2  . PHE A 1 86  ? 29.23101 34.15736 -14.21457 1.000 23.60770 ? 82  PHE A HD2  1 
ATOM   1395 H  HE1  . PHE A 1 86  ? 29.02291 30.36064 -11.60367 1.000 29.45622 ? 82  PHE A HE1  1 
ATOM   1396 H  HE2  . PHE A 1 86  ? 30.88816 32.56104 -14.38098 1.000 25.28125 ? 82  PHE A HE2  1 
ATOM   1397 H  HZ   . PHE A 1 86  ? 30.78249 30.65769 -13.07043 1.000 27.40025 ? 82  PHE A HZ   1 
ATOM   1398 N  N    . ALA A 1 87  ? 29.31885 35.57944 -10.38085 1.000 26.35659 ? 83  ALA A N    1 
ATOM   1399 C  CA   . ALA A 1 87  ? 30.53105 36.35837 -10.15157 1.000 29.47856 ? 83  ALA A CA   1 
ATOM   1400 C  C    . ALA A 1 87  ? 31.46236 36.32642 -11.35774 1.000 27.45346 ? 83  ALA A C    1 
ATOM   1401 O  O    . ALA A 1 87  ? 32.00955 37.35939 -11.76191 1.000 32.76235 ? 83  ALA A O    1 
ATOM   1402 C  CB   . ALA A 1 87  ? 31.24894 35.82509 -8.91223  1.000 30.84416 ? 83  ALA A CB   1 
ATOM   1403 H  H    . ALA A 1 87  ? 29.21497 34.92850 -9.82851  1.000 31.65263 ? 83  ALA A H    1 
ATOM   1404 H  HA   . ALA A 1 87  ? 30.28329 37.28355 -9.99810  1.000 35.39901 ? 83  ALA A HA   1 
ATOM   1405 H  HB1  . ALA A 1 87  ? 32.07689 36.31576 -8.79126  1.000 37.03772 ? 83  ALA A HB1  1 
ATOM   1406 H  HB2  . ALA A 1 87  ? 30.67633 35.94670 -8.13878  1.000 37.03772 ? 83  ALA A HB2  1 
ATOM   1407 H  HB3  . ALA A 1 87  ? 31.43862 34.88222 -9.03839  1.000 37.03772 ? 83  ALA A HB3  1 
ATOM   1408 N  N    . GLY A 1 88  ? 31.65760 35.15842 -11.94001 1.000 23.62698 ? 84  GLY A N    1 
ATOM   1409 C  CA   . GLY A 1 88  ? 32.55779 35.01297 -13.06838 1.000 21.06967 ? 84  GLY A CA   1 
ATOM   1410 C  C    . GLY A 1 88  ? 33.48848 33.84216 -12.87511 1.000 21.45049 ? 84  GLY A C    1 
ATOM   1411 O  O    . GLY A 1 88  ? 33.86655 33.49179 -11.75472 1.000 25.03143 ? 84  GLY A O    1 
ATOM   1412 H  H    . GLY A 1 88  ? 31.27632 34.42663 -11.69773 1.000 28.37711 ? 84  GLY A H    1 
ATOM   1413 H  HA2  . GLY A 1 88  ? 32.04423 34.87105 -13.87895 1.000 25.30833 ? 84  GLY A HA2  1 
ATOM   1414 H  HA3  . GLY A 1 88  ? 33.08867 35.81868 -13.16788 1.000 25.30833 ? 84  GLY A HA3  1 
ATOM   1415 N  N    . LEU A 1 89  ? 33.86414 33.22581 -13.98634 1.000 18.26463 ? 85  LEU A N    1 
ATOM   1416 C  CA   . LEU A 1 89  ? 34.82084 32.12736 -14.00626 1.000 19.10098 ? 85  LEU A CA   1 
ATOM   1417 C  C    . LEU A 1 89  ? 36.14802 32.75510 -14.36911 1.000 18.87545 ? 85  LEU A C    1 
ATOM   1418 O  O    . LEU A 1 89  ? 36.39159 33.08273 -15.53414 1.000 18.84274 ? 85  LEU A O    1 
ATOM   1419 C  CB   . LEU A 1 89  ? 34.44754 31.10412 -15.06437 1.000 24.64940 ? 85  LEU A CB   1 
ATOM   1420 C  CG   . LEU A 1 89  ? 33.56953 29.92610 -14.70283 1.000 30.95425 ? 85  LEU A CG   1 
ATOM   1421 C  CD1  . LEU A 1 89  ? 33.38100 29.12023 -15.95058 1.000 32.54736 ? 85  LEU A CD1  1 
ATOM   1422 C  CD2  . LEU A 1 89  ? 34.20745 29.07302 -13.61675 1.000 30.65784 ? 85  LEU A CD2  1 
ATOM   1423 H  H    . LEU A 1 89  ? 33.56838 33.43351 -14.76672 1.000 21.94228 ? 85  LEU A H    1 
ATOM   1424 H  HA   . LEU A 1 89  ? 34.85125 31.69270 -13.13963 1.000 22.94590 ? 85  LEU A HA   1 
ATOM   1425 H  HB2  . LEU A 1 89  ? 33.98330 31.57938 -15.77113 1.000 29.60401 ? 85  LEU A HB2  1 
ATOM   1426 H  HB3  . LEU A 1 89  ? 35.27491 30.72919 -15.40463 1.000 29.60401 ? 85  LEU A HB3  1 
ATOM   1427 H  HG   . LEU A 1 89  ? 32.71696 30.22899 -14.35313 1.000 37.16983 ? 85  LEU A HG   1 
ATOM   1428 H  HD11 . LEU A 1 89  ? 32.80079 28.36768 -15.75583 1.000 39.08156 ? 85  LEU A HD11 1 
ATOM   1429 H  HD12 . LEU A 1 89  ? 32.97758 29.68152 -16.63110 1.000 39.08156 ? 85  LEU A HD12 1 
ATOM   1430 H  HD13 . LEU A 1 89  ? 34.24535 28.80157 -16.25432 1.000 39.08156 ? 85  LEU A HD13 1 
ATOM   1431 H  HD21 . LEU A 1 89  ? 33.71146 28.24348 -13.53466 1.000 36.81414 ? 85  LEU A HD21 1 
ATOM   1432 H  HD22 . LEU A 1 89  ? 35.12712 28.88569 -13.86173 1.000 36.81414 ? 85  LEU A HD22 1 
ATOM   1433 H  HD23 . LEU A 1 89  ? 34.18106 29.55864 -12.77747 1.000 36.81414 ? 85  LEU A HD23 1 
ATOM   1434 N  N    . LYS A 1 90  ? 37.01644 32.90486 -13.37678 1.000 19.44307 ? 86  LYS A N    1 
ATOM   1435 C  CA   . LYS A 1 90  ? 38.20653 33.70854 -13.58931 1.000 20.66833 ? 86  LYS A CA   1 
ATOM   1436 C  C    . LYS A 1 90  ? 39.29615 32.98299 -14.36597 1.000 19.67701 ? 86  LYS A C    1 
ATOM   1437 O  O    . LYS A 1 90  ? 40.03485 33.63196 -15.11378 1.000 24.73943 ? 86  LYS A O    1 
ATOM   1438 C  CB   . LYS A 1 90  ? 38.70016 34.23089 -12.24558 1.000 23.81240 ? 86  LYS A CB   1 
ATOM   1439 C  CG   . LYS A 1 90  ? 37.62611 35.00673 -11.46934 1.000 28.54641 ? 86  LYS A CG   1 
ATOM   1440 C  CD   . LYS A 1 90  ? 36.99737 36.13346 -12.30831 1.000 30.30965 ? 86  LYS A CD   1 
ATOM   1441 C  CE   . LYS A 1 90  ? 36.04402 36.95371 -11.52065 1.000 29.61018 ? 86  LYS A CE   1 
ATOM   1442 N  NZ   . LYS A 1 90  ? 35.64111 38.14919 -12.30361 1.000 30.21350 ? 86  LYS A NZ   1 
ATOM   1443 H  H    . LYS A 1 90  ? 36.94168 32.56082 -12.59215 1.000 23.35641 ? 86  LYS A H    1 
ATOM   1444 H  HA   . LYS A 1 90  ? 37.98184 34.47738 -14.13639 1.000 24.82672 ? 86  LYS A HA   1 
ATOM   1445 H  HB2  . LYS A 1 90  ? 38.97933 33.47936 -11.69953 1.000 28.59961 ? 86  LYS A HB2  1 
ATOM   1446 H  HB3  . LYS A 1 90  ? 39.44968 34.82784 -12.39651 1.000 28.59961 ? 86  LYS A HB3  1 
ATOM   1447 H  HG2  . LYS A 1 90  ? 36.91953 34.39600 -11.20729 1.000 34.28041 ? 86  LYS A HG2  1 
ATOM   1448 H  HG3  . LYS A 1 90  ? 38.02852 35.40585 -10.68216 1.000 34.28041 ? 86  LYS A HG3  1 
ATOM   1449 H  HD2  . LYS A 1 90  ? 37.69968 36.71732 -12.63506 1.000 36.39631 ? 86  LYS A HD2  1 
ATOM   1450 H  HD3  . LYS A 1 90  ? 36.51558 35.74408 -13.05474 1.000 36.39631 ? 86  LYS A HD3  1 
ATOM   1451 H  HE2  . LYS A 1 90  ? 35.25191 36.43151 -11.31876 1.000 35.55695 ? 86  LYS A HE2  1 
ATOM   1452 H  HE3  . LYS A 1 90  ? 36.46640 37.24722 -10.69825 1.000 35.55695 ? 86  LYS A HE3  1 
ATOM   1453 H  HZ1  . LYS A 1 90  ? 35.05845 38.63541 -11.83864 1.000 36.28093 ? 86  LYS A HZ1  1 
ATOM   1454 H  HZ2  . LYS A 1 90  ? 36.35481 38.64908 -12.48486 1.000 36.28093 ? 86  LYS A HZ2  1 
ATOM   1455 H  HZ3  . LYS A 1 90  ? 35.26227 37.89836 -13.06890 1.000 36.28093 ? 86  LYS A HZ3  1 
ATOM   1456 N  N    . LYS A 1 91  ? 39.39562 31.66348 -14.25355 1.000 17.24827 ? 87  LYS A N    1 
ATOM   1457 C  CA   . LYS A 1 91  ? 40.52843 30.95329 -14.85222 1.000 18.02784 ? 87  LYS A CA   1 
ATOM   1458 C  C    . LYS A 1 91  ? 40.25249 30.66564 -16.32877 1.000 16.74350 ? 87  LYS A C    1 
ATOM   1459 O  O    . LYS A 1 91  ? 39.21673 30.07882 -16.65211 1.000 17.15771 ? 87  LYS A O    1 
ATOM   1460 C  CB   . LYS A 1 91  ? 40.74727 29.63188 -14.13491 1.000 21.07093 ? 87  LYS A CB   1 
ATOM   1461 C  CG   . LYS A 1 91  ? 41.21987 29.80038 -12.71179 1.000 25.34976 ? 87  LYS A CG   1 
ATOM   1462 C  CD   . LYS A 1 91  ? 41.70000 28.48970 -12.13205 1.000 31.54215 ? 87  LYS A CD   1 
ATOM   1463 C  CE   . LYS A 1 91  ? 42.43929 28.69833 -10.80962 1.000 38.01572 ? 87  LYS A CE   1 
ATOM   1464 N  NZ   . LYS A 1 91  ? 43.15717 27.46571 -10.36951 1.000 41.57551 ? 87  LYS A NZ   1 
ATOM   1465 H  H    . LYS A 1 91  ? 38.83230 31.15950 -13.84335 1.000 20.72265 ? 87  LYS A H    1 
ATOM   1466 H  HA   . LYS A 1 91  ? 41.32520 31.50180 -14.78019 1.000 21.65813 ? 87  LYS A HA   1 
ATOM   1467 H  HB2  . LYS A 1 91  ? 39.90999 29.14250 -14.11564 1.000 25.30984 ? 87  LYS A HB2  1 
ATOM   1468 H  HB3  . LYS A 1 91  ? 41.41877 29.12173 -14.61422 1.000 25.30984 ? 87  LYS A HB3  1 
ATOM   1469 H  HG2  . LYS A 1 91  ? 41.95580 30.43190 -12.68974 1.000 30.44444 ? 87  LYS A HG2  1 
ATOM   1470 H  HG3  . LYS A 1 91  ? 40.48710 30.12566 -12.16575 1.000 30.44444 ? 87  LYS A HG3  1 
ATOM   1471 H  HD2  . LYS A 1 91  ? 40.93771 27.91291 -11.96732 1.000 37.87531 ? 87  LYS A HD2  1 
ATOM   1472 H  HD3  . LYS A 1 91  ? 42.30806 28.06540 -12.75746 1.000 37.87531 ? 87  LYS A HD3  1 
ATOM   1473 H  HE2  . LYS A 1 91  ? 43.09265 29.40711 -10.91758 1.000 45.64360 ? 87  LYS A HE2  1 
ATOM   1474 H  HE3  . LYS A 1 91  ? 41.79986 28.93864 -10.12094 1.000 45.64360 ? 87  LYS A HE3  1 
ATOM   1475 H  HZ1  . LYS A 1 91  ? 43.59579 27.62324 -9.61129  1.000 49.91534 ? 87  LYS A HZ1  1 
ATOM   1476 H  HZ2  . LYS A 1 91  ? 42.57501 26.80614 -10.23474 1.000 49.91534 ? 87  LYS A HZ2  1 
ATOM   1477 H  HZ3  . LYS A 1 91  ? 43.73986 27.21371 -10.99326 1.000 49.91534 ? 87  LYS A HZ3  1 
ATOM   1478 N  N    . PRO A 1 92  ? 41.15563 31.02219 -17.24919 1.000 16.55776 ? 88  PRO A N    1 
ATOM   1479 C  CA   . PRO A 1 92  ? 40.87560 30.77804 -18.66815 1.000 16.29858 ? 88  PRO A CA   1 
ATOM   1480 C  C    . PRO A 1 92  ? 40.73708 29.32028 -19.02798 1.000 15.87432 ? 88  PRO A C    1 
ATOM   1481 O  O    . PRO A 1 92  ? 39.96493 29.00496 -19.93614 1.000 15.59517 ? 88  PRO A O    1 
ATOM   1482 C  CB   . PRO A 1 92  ? 42.05906 31.43580 -19.39443 1.000 19.24744 ? 88  PRO A CB   1 
ATOM   1483 C  CG   . PRO A 1 92  ? 43.12177 31.55200 -18.39274 1.000 22.56958 ? 88  PRO A CG   1 
ATOM   1484 C  CD   . PRO A 1 92  ? 42.44237 31.72240 -17.06986 1.000 19.96173 ? 88  PRO A CD   1 
ATOM   1485 H  HA   . PRO A 1 92  ? 40.05897 31.24056 -18.91327 1.000 19.58302 ? 88  PRO A HA   1 
ATOM   1486 H  HB2  . PRO A 1 92  ? 42.34199 30.87540 -20.13389 1.000 23.12166 ? 88  PRO A HB2  1 
ATOM   1487 H  HB3  . PRO A 1 92  ? 41.79707 32.31033 -19.72224 1.000 23.12166 ? 88  PRO A HB3  1 
ATOM   1488 H  HG2  . PRO A 1 92  ? 43.66181 30.74625 -18.39761 1.000 27.10822 ? 88  PRO A HG2  1 
ATOM   1489 H  HG3  . PRO A 1 92  ? 43.67463 32.32316 -18.59415 1.000 27.10822 ? 88  PRO A HG3  1 
ATOM   1490 H  HD2  . PRO A 1 92  ? 42.96169 31.31204 -16.36077 1.000 23.97881 ? 88  PRO A HD2  1 
ATOM   1491 H  HD3  . PRO A 1 92  ? 42.29889 32.66173 -16.87501 1.000 23.97881 ? 88  PRO A HD3  1 
ATOM   1492 N  N    . ASN A 1 93  ? 41.45355 28.41992 -18.35631 1.000 17.82203 ? 89  ASN A N    1 
ATOM   1493 C  CA   . ASN A 1 93  ? 41.30630 27.00534 -18.67351 1.000 19.13534 ? 89  ASN A CA   1 
ATOM   1494 C  C    . ASN A 1 93  ? 39.91066 26.50126 -18.31147 1.000 17.72541 ? 89  ASN A C    1 
ATOM   1495 O  O    . ASN A 1 93  ? 39.32976 25.69068 -19.04521 1.000 18.01674 ? 89  ASN A O    1 
ATOM   1496 C  CB   . ASN A 1 93  ? 42.41292 26.19070 -17.99523 1.000 23.72921 ? 89  ASN A CB   1 
ATOM   1497 C  CG   . ASN A 1 93  ? 42.25433 26.10626 -16.49045 1.000 29.06580 ? 89  ASN A CG   1 
ATOM   1498 O  OD1  . ASN A 1 93  ? 42.40731 27.10416 -15.77242 1.000 31.04170 ? 89  ASN A OD1  1 
ATOM   1499 N  ND2  . ASN A 1 93  ? 41.97725 24.89604 -15.99546 1.000 30.55904 ? 89  ASN A ND2  1 
ATOM   1500 H  H    . ASN A 1 93  ? 42.01604 28.59608 -17.73008 1.000 21.41117 ? 89  ASN A H    1 
ATOM   1501 H  HA   . ASN A 1 93  ? 41.41430 26.87763 -19.62898 1.000 22.98714 ? 89  ASN A HA   1 
ATOM   1502 H  HB2  . ASN A 1 93  ? 42.39923 25.28709 -18.34765 1.000 28.49978 ? 89  ASN A HB2  1 
ATOM   1503 H  HB3  . ASN A 1 93  ? 43.26907 26.60668 -18.18193 1.000 28.49978 ? 89  ASN A HB3  1 
ATOM   1504 H  HD21 . ASN A 1 93  ? 41.87695 24.79079 -15.14784 1.000 36.69558 ? 89  ASN A HD21 1 
ATOM   1505 H  HD22 . ASN A 1 93  ? 41.89928 24.22259 -16.52459 1.000 36.69558 ? 89  ASN A HD22 1 
ATOM   1506 N  N    . GLU A 1 94  ? 39.33881 27.00420 -17.21529 1.000 16.23521 ? 90  GLU A N    1 
ATOM   1507 C  CA   . GLU A 1 94  ? 37.99330 26.60272 -16.82621 1.000 16.25682 ? 90  GLU A CA   1 
ATOM   1508 C  C    . GLU A 1 94  ? 36.95619 27.17455 -17.78542 1.000 14.84693 ? 90  GLU A C    1 
ATOM   1509 O  O    . GLU A 1 94  ? 36.02000 26.47441 -18.18812 1.000 15.28275 ? 90  GLU A O    1 
ATOM   1510 C  CB   . GLU A 1 94  ? 37.72179 27.00726 -15.37333 1.000 19.96211 ? 90  GLU A CB   1 
ATOM   1511 C  CG   . GLU A 1 94  ? 38.53501 26.15897 -14.37756 1.000 23.61685 ? 90  GLU A CG   1 
ATOM   1512 C  CD   . GLU A 1 94  ? 38.27861 26.47572 -12.90939 1.000 29.54633 ? 90  GLU A CD   1 
ATOM   1513 O  OE1  . GLU A 1 94  ? 37.51048 27.41137 -12.60179 1.000 31.88303 ? 90  GLU A OE1  1 
ATOM   1514 O  OE2  . GLU A 1 94  ? 38.86321 25.75894 -12.05877 1.000 34.59851 ? 90  GLU A OE2  1 
ATOM   1515 H  H    . GLU A 1 94  ? 39.70514 27.57376 -16.68520 1.000 19.50699 ? 90  GLU A H    1 
ATOM   1516 H  HA   . GLU A 1 94  ? 37.91855 25.63641 -16.86578 1.000 19.53291 ? 90  GLU A HA   1 
ATOM   1517 H  HB2  . GLU A 1 94  ? 37.96670 27.93776 -15.25050 1.000 23.97926 ? 90  GLU A HB2  1 
ATOM   1518 H  HB3  . GLU A 1 94  ? 36.77954 26.88375 -15.17887 1.000 23.97926 ? 90  GLU A HB3  1 
ATOM   1519 H  HG2  . GLU A 1 94  ? 38.31447 25.22468 -14.51668 1.000 28.36495 ? 90  GLU A HG2  1 
ATOM   1520 H  HG3  . GLU A 1 94  ? 39.47882 26.30580 -14.54658 1.000 28.36495 ? 90  GLU A HG3  1 
ATOM   1521 N  N    . ARG A 1 95  ? 37.11570 28.43923 -18.17828 1.000 14.00123 ? 91  ARG A N    1 
ATOM   1522 C  CA   . ARG A 1 95  ? 36.22848 28.99695 -19.19077 1.000 13.99579 ? 91  ARG A CA   1 
ATOM   1523 C  C    . ARG A 1 95  ? 36.30759 28.20937 -20.48587 1.000 12.63918 ? 91  ARG A C    1 
ATOM   1524 O  O    . ARG A 1 95  ? 35.28076 27.94758 -21.11975 1.000 13.64000 ? 91  ARG A O    1 
ATOM   1525 C  CB   . ARG A 1 95  ? 36.55322 30.47167 -19.42577 1.000 15.63424 ? 91  ARG A CB   1 
ATOM   1526 C  CG   . ARG A 1 95  ? 35.90837 31.38168 -18.41448 1.000 17.58995 ? 91  ARG A CG   1 
ATOM   1527 C  CD   . ARG A 1 95  ? 36.17623 32.82523 -18.72270 1.000 16.86864 ? 91  ARG A CD   1 
ATOM   1528 N  NE   . ARG A 1 95  ? 37.53175 33.11574 -18.27764 1.000 23.29985 ? 91  ARG A NE   1 
ATOM   1529 C  CZ   . ARG A 1 95  ? 38.35840 33.99335 -18.82188 1.000 21.27020 ? 91  ARG A CZ   1 
ATOM   1530 N  NH1  . ARG A 1 95  ? 38.01454 34.71630 -19.87615 1.000 23.04125 ? 91  ARG A NH1  1 
ATOM   1531 N  NH2  . ARG A 1 95  ? 39.55049 34.14425 -18.29156 1.000 27.02902 ? 91  ARG A NH2  1 
ATOM   1532 H  H    . ARG A 1 95  ? 37.71409 28.98129 -17.88214 1.000 16.82621 ? 91  ARG A H    1 
ATOM   1533 H  HA   . ARG A 1 95  ? 35.31517 28.94583 -18.86804 1.000 16.81967 ? 91  ARG A HA   1 
ATOM   1534 H  HB2  . ARG A 1 95  ? 37.51373 30.59545 -19.37105 1.000 18.78582 ? 91  ARG A HB2  1 
ATOM   1535 H  HB3  . ARG A 1 95  ? 36.23527 30.72806 -20.30559 1.000 18.78582 ? 91  ARG A HB3  1 
ATOM   1536 H  HG2  . ARG A 1 95  ? 34.94859 31.24147 -18.42222 1.000 21.13267 ? 91  ARG A HG2  1 
ATOM   1537 H  HG3  . ARG A 1 95  ? 36.26502 31.18692 -17.53370 1.000 21.13267 ? 91  ARG A HG3  1 
ATOM   1538 H  HD2  . ARG A 1 95  ? 36.10850 32.98465 -19.67711 1.000 20.26710 ? 91  ARG A HD2  1 
ATOM   1539 H  HD3  . ARG A 1 95  ? 35.55105 33.39359 -18.24623 1.000 20.26710 ? 91  ARG A HD3  1 
ATOM   1540 H  HE   . ARG A 1 95  ? 37.82186 32.67598 -17.59790 1.000 27.98454 ? 91  ARG A HE   1 
ATOM   1541 H  HH11 . ARG A 1 95  ? 37.23474 34.62208 -20.22634 1.000 27.67423 ? 91  ARG A HH11 1 
ATOM   1542 H  HH12 . ARG A 1 95  ? 38.57095 35.28017 -20.21089 1.000 27.67423 ? 91  ARG A HH12 1 
ATOM   1543 H  HH21 . ARG A 1 95  ? 39.77827 33.67780 -17.60588 1.000 32.45955 ? 91  ARG A HH21 1 
ATOM   1544 H  HH22 . ARG A 1 95  ? 40.10327 34.70949 -18.62999 1.000 32.45955 ? 91  ARG A HH22 1 
ATOM   1545 N  N    . GLY A 1 96  ? 37.52122 27.84984 -20.90184 1.000 13.00124 ? 92  GLY A N    1 
ATOM   1546 C  CA   . GLY A 1 96  ? 37.67906 27.09836 -22.13627 1.000 14.08024 ? 92  GLY A CA   1 
ATOM   1547 C  C    . GLY A 1 96  ? 37.02441 25.72876 -22.09239 1.000 13.44775 ? 92  GLY A C    1 
ATOM   1548 O  O    . GLY A 1 96  ? 36.39629 25.30493 -23.06513 1.000 13.12611 ? 92  GLY A O    1 
ATOM   1549 H  H    . GLY A 1 96  ? 38.25782 28.02570 -20.49429 1.000 15.62622 ? 92  GLY A H    1 
ATOM   1550 H  HA2  . GLY A 1 96  ? 37.28247 27.59942 -22.86604 1.000 16.92102 ? 92  GLY A HA2  1 
ATOM   1551 H  HA3  . GLY A 1 96  ? 38.62458 26.97558 -22.31465 1.000 16.92102 ? 92  GLY A HA3  1 
ATOM   1552 N  N    . ASP A 1 97  ? 37.16192 25.01945 -20.96845 1.000 13.45884 ? 93  ASP A N    1 
ATOM   1553 C  CA   . ASP A 1 97  ? 36.51569 23.71914 -20.82833 1.000 12.52073 ? 93  ASP A CA   1 
ATOM   1554 C  C    . ASP A 1 97  ? 34.99854 23.87455 -20.84000 1.000 13.00991 ? 93  ASP A C    1 
ATOM   1555 O  O    . ASP A 1 97  ? 34.28621 23.10875 -21.50410 1.000 12.45537 ? 93  ASP A O    1 
ATOM   1556 C  CB   . ASP A 1 97  ? 36.97639 23.01816 -19.53911 1.000 13.46755 ? 93  ASP A CB   1 
ATOM   1557 C  CG   . ASP A 1 97  ? 38.44431 22.58435 -19.57172 1.000 15.85042 ? 93  ASP A CG   1 
ATOM   1558 O  OD1  . ASP A 1 97  ? 39.01829 22.42776 -20.66938 1.000 16.24699 ? 93  ASP A OD1  1 
ATOM   1559 O  OD2  . ASP A 1 97  ? 39.01094 22.37289 -18.47778 1.000 18.36621 ? 93  ASP A OD2  1 
ATOM   1560 H  H    . ASP A 1 97  ? 37.61771 25.26539 -20.28189 1.000 16.17533 ? 93  ASP A H    1 
ATOM   1561 H  HA   . ASP A 1 97  ? 36.77914 23.15596 -21.57286 1.000 15.04960 ? 93  ASP A HA   1 
ATOM   1562 H  HB2  . ASP A 1 97  ? 36.86361 23.62812 -18.79337 1.000 16.18579 ? 93  ASP A HB2  1 
ATOM   1563 H  HB3  . ASP A 1 97  ? 36.43529 22.22463 -19.40342 1.000 16.18579 ? 93  ASP A HB3  1 
ATOM   1564 N  N    . LEU A 1 98  ? 34.48347 24.85972 -20.09872 1.000 12.14623 ? 94  LEU A N    1 
ATOM   1565 C  CA   . LEU A 1 98  ? 33.04921 25.09992 -20.07287 1.000 11.90573 ? 94  LEU A CA   1 
ATOM   1566 C  C    . LEU A 1 98  ? 32.51793 25.42074 -21.46896 1.000 11.78090 ? 94  LEU A C    1 
ATOM   1567 O  O    . LEU A 1 98  ? 31.45232 24.93432 -21.86943 1.000 12.53660 ? 94  LEU A O    1 
ATOM   1568 C  CB   . LEU A 1 98  ? 32.75134 26.22304 -19.08520 1.000 12.65121 ? 94  LEU A CB   1 
ATOM   1569 C  CG   . LEU A 1 98  ? 31.28897 26.67368 -19.00995 1.000 13.92949 ? 94  LEU A CG   1 
ATOM   1570 C  CD1  . LEU A 1 98  ? 30.35152 25.51762 -18.63782 1.000 13.94998 ? 94  LEU A CD1  1 
ATOM   1571 C  CD2  . LEU A 1 98  ? 31.14878 27.80580 -18.04975 1.000 15.88302 ? 94  LEU A CD2  1 
ATOM   1572 H  H    . LEU A 1 98  ? 34.94061 25.39713 -19.60698 1.000 14.60021 ? 94  LEU A H    1 
ATOM   1573 H  HA   . LEU A 1 98  ? 32.58570 24.30347 -19.77000 1.000 14.31160 ? 94  LEU A HA   1 
ATOM   1574 H  HB2  . LEU A 1 98  ? 33.00636 25.92292 -18.19875 1.000 15.20618 ? 94  LEU A HB2  1 
ATOM   1575 H  HB3  . LEU A 1 98  ? 33.27870 26.99694 -19.33793 1.000 15.20618 ? 94  LEU A HB3  1 
ATOM   1576 H  HG   . LEU A 1 98  ? 31.01669 26.97982 -19.88918 1.000 16.74012 ? 94  LEU A HG   1 
ATOM   1577 H  HD11 . LEU A 1 98  ? 29.49520 25.88128 -18.36328 1.000 16.76471 ? 94  LEU A HD11 1 
ATOM   1578 H  HD12 . LEU A 1 98  ? 30.23468 24.94425 -19.41145 1.000 16.76471 ? 94  LEU A HD12 1 
ATOM   1579 H  HD13 . LEU A 1 98  ? 30.74578 25.01343 -17.90895 1.000 16.76471 ? 94  LEU A HD13 1 
ATOM   1580 H  HD21 . LEU A 1 98  ? 30.30706 28.25837 -18.21584 1.000 19.08435 ? 94  LEU A HD21 1 
ATOM   1581 H  HD22 . LEU A 1 98  ? 31.16350 27.45624 -17.14504 1.000 19.08435 ? 94  LEU A HD22 1 
ATOM   1582 H  HD23 . LEU A 1 98  ? 31.88671 28.42212 -18.17827 1.000 19.08435 ? 94  LEU A HD23 1 
ATOM   1583 N  N    . ILE A 1 99  ? 33.23806 26.25751 -22.21301 1.000 11.93427 ? 95  ILE A N    1 
ATOM   1584 C  CA   . ILE A 1 99  ? 32.79197 26.64428 -23.54567 1.000 12.64646 ? 95  ILE A CA   1 
ATOM   1585 C  C    . ILE A 1 99  ? 32.78686 25.45245 -24.48981 1.000 12.06206 ? 95  ILE A C    1 
ATOM   1586 O  O    . ILE A 1 99  ? 31.87636 25.31617 -25.31250 1.000 13.00029 ? 95  ILE A O    1 
ATOM   1587 C  CB   . ILE A 1 99  ? 33.62827 27.83076 -24.05248 1.000 12.93694 ? 95  ILE A CB   1 
ATOM   1588 C  CG1  . ILE A 1 99  ? 33.22607 29.08731 -23.27341 1.000 14.35380 ? 95  ILE A CG1  1 
ATOM   1589 C  CG2  . ILE A 1 99  ? 33.45561 28.01941 -25.57259 1.000 14.59977 ? 95  ILE A CG2  1 
ATOM   1590 C  CD1  . ILE A 1 99  ? 34.16319 30.27283 -23.45944 1.000 16.20922 ? 95  ILE A CD1  1 
ATOM   1591 H  H    . ILE A 1 99  ? 33.98311 26.61341 -21.97253 1.000 14.34585 ? 95  ILE A H    1 
ATOM   1592 H  HA   . ILE A 1 99  ? 31.87139 26.94605 -23.49714 1.000 15.20047 ? 95  ILE A HA   1 
ATOM   1593 H  HB   . ILE A 1 99  ? 34.56942 27.65344 -23.89854 1.000 15.54905 ? 95  ILE A HB   1 
ATOM   1594 H  HG12 . ILE A 1 99  ? 32.34337 29.36304 -23.56620 1.000 17.24929 ? 95  ILE A HG12 1 
ATOM   1595 H  HG13 . ILE A 1 99  ? 33.20983 28.87247 -22.32765 1.000 17.24929 ? 95  ILE A HG13 1 
ATOM   1596 H  HG21 . ILE A 1 99  ? 33.78123 28.89879 -25.82068 1.000 17.54446 ? 95  ILE A HG21 1 
ATOM   1597 H  HG22 . ILE A 1 99  ? 33.96445 27.33553 -26.03549 1.000 17.54446 ? 95  ILE A HG22 1 
ATOM   1598 H  HG23 . ILE A 1 99  ? 32.51501 27.93985 -25.79586 1.000 17.54446 ? 95  ILE A HG23 1 
ATOM   1599 H  HD11 . ILE A 1 99  ? 33.94641 30.95285 -22.80257 1.000 19.47579 ? 95  ILE A HD11 1 
ATOM   1600 H  HD12 . ILE A 1 99  ? 35.07802 29.97446 -23.33711 1.000 19.47579 ? 95  ILE A HD12 1 
ATOM   1601 H  HD13 . ILE A 1 99  ? 34.04826 30.62884 -24.35440 1.000 19.47579 ? 95  ILE A HD13 1 
ATOM   1602 N  N    . ALA A 1 100 ? 33.77560 24.56880 -24.37627 1.000 12.75872 ? 96  ALA A N    1 
ATOM   1603 C  CA   . ALA A 1 100 ? 33.77013 23.34326 -25.17385 1.000 13.60193 ? 96  ALA A CA   1 
ATOM   1604 C  C    . ALA A 1 100 ? 32.53395 22.50204 -24.86229 1.000 13.48940 ? 96  ALA A C    1 
ATOM   1605 O  O    . ALA A 1 100 ? 31.86290 21.98820 -25.77048 1.000 13.87504 ? 96  ALA A O    1 
ATOM   1606 C  CB   . ALA A 1 100 ? 35.05785 22.54817 -24.92969 1.000 14.32350 ? 96  ALA A CB   1 
ATOM   1607 H  H    . ALA A 1 100 ? 34.45353 24.65003 -23.85337 1.000 15.33519 ? 96  ALA A H    1 
ATOM   1608 H  HA   . ALA A 1 100 ? 33.74663 23.57336 -26.11587 1.000 16.34704 ? 96  ALA A HA   1 
ATOM   1609 H  HB1  . ALA A 1 100 ? 35.01224 21.71403 -25.42267 1.000 17.21293 ? 96  ALA A HB1  1 
ATOM   1610 H  HB2  . ALA A 1 100 ? 35.81506 23.07189 -25.23505 1.000 17.21293 ? 96  ALA A HB2  1 
ATOM   1611 H  HB3  . ALA A 1 100 ? 35.14208 22.36720 -23.98045 1.000 17.21293 ? 96  ALA A HB3  1 
ATOM   1612 N  N    . TYR A 1 101 ? 32.18507 22.38738 -23.58132 1.000 12.43068 ? 97  TYR A N    1 
ATOM   1613 C  CA   . TYR A 1 101 ? 30.97100 21.68119 -23.21245 1.000 11.80619 ? 97  TYR A CA   1 
ATOM   1614 C  C    . TYR A 1 101 ? 29.73129 22.36166 -23.79795 1.000 12.14761 ? 97  TYR A C    1 
ATOM   1615 O  O    . TYR A 1 101 ? 28.87937 21.70026 -24.41051 1.000 12.84561 ? 97  TYR A O    1 
ATOM   1616 C  CB   . TYR A 1 101 ? 30.86589 21.54812 -21.68145 1.000 11.84689 ? 97  TYR A CB   1 
ATOM   1617 C  CG   . TYR A 1 101 ? 29.46293 21.15288 -21.25183 1.000 11.54862 ? 97  TYR A CG   1 
ATOM   1618 C  CD1  . TYR A 1 101 ? 29.03039 19.83953 -21.35486 1.000 12.45412 ? 97  TYR A CD1  1 
ATOM   1619 C  CD2  . TYR A 1 101 ? 28.55705 22.11563 -20.82194 1.000 12.02545 ? 97  TYR A CD2  1 
ATOM   1620 C  CE1  . TYR A 1 101 ? 27.71982 19.48314 -21.02412 1.000 12.20073 ? 97  TYR A CE1  1 
ATOM   1621 C  CE2  . TYR A 1 101 ? 27.24763 21.77197 -20.49621 1.000 12.61659 ? 97  TYR A CE2  1 
ATOM   1622 C  CZ   . TYR A 1 101 ? 26.84642 20.46404 -20.59789 1.000 13.96689 ? 97  TYR A CZ   1 
ATOM   1623 O  OH   . TYR A 1 101 ? 25.54404 20.15205 -20.28464 1.000 14.76099 ? 97  TYR A OH   1 
ATOM   1624 H  H    . TYR A 1 101 ? 32.62927 22.70579 -22.91731 1.000 14.94155 ? 97  TYR A H    1 
ATOM   1625 H  HA   . TYR A 1 101 ? 31.01444 20.78379 -23.57806 1.000 14.19216 ? 97  TYR A HA   1 
ATOM   1626 H  HB2  . TYR A 1 101 ? 31.48295 20.86488 -21.37597 1.000 14.24099 ? 97  TYR A HB2  1 
ATOM   1627 H  HB3  . TYR A 1 101 ? 31.08313 22.39926 -21.27004 1.000 14.24099 ? 97  TYR A HB3  1 
ATOM   1628 H  HD1  . TYR A 1 101 ? 29.62199 19.18494 -21.64886 1.000 14.96967 ? 97  TYR A HD1  1 
ATOM   1629 H  HD2  . TYR A 1 101 ? 28.82947 23.00199 -20.75088 1.000 14.45527 ? 97  TYR A HD2  1 
ATOM   1630 H  HE1  . TYR A 1 101 ? 27.44031 18.59860 -21.09016 1.000 14.66561 ? 97  TYR A HE1  1 
ATOM   1631 H  HE2  . TYR A 1 101 ? 26.64921 22.42454 -20.21170 1.000 15.16464 ? 97  TYR A HE2  1 
ATOM   1632 H  HH   . TYR A 1 101 ? 25.36621 19.37173 -20.53975 1.000 17.73791 ? 97  TYR A HH   1 
ATOM   1633 N  N    . LEU A 1 102 ? 29.63282 23.69412 -23.66801 1.000 11.22102 ? 98  LEU A N    1 
ATOM   1634 C  CA   . LEU A 1 102 ? 28.43825 24.39165 -24.16489 1.000 12.09771 ? 98  LEU A CA   1 
ATOM   1635 C  C    . LEU A 1 102 ? 28.29450 24.25649 -25.67653 1.000 11.22342 ? 98  LEU A C    1 
ATOM   1636 O  O    . LEU A 1 102 ? 27.17598 24.09074 -26.18636 1.000 12.13982 ? 98  LEU A O    1 
ATOM   1637 C  CB   . LEU A 1 102 ? 28.47814 25.87347 -23.79083 1.000 12.23229 ? 98  LEU A CB   1 
ATOM   1638 C  CG   . LEU A 1 102 ? 28.31994 26.23772 -22.31595 1.000 14.34214 ? 98  LEU A CG   1 
ATOM   1639 C  CD1  . LEU A 1 102 ? 28.57775 27.72146 -22.13908 1.000 16.98890 ? 98  LEU A CD1  1 
ATOM   1640 C  CD2  . LEU A 1 102 ? 26.90780 25.87457 -21.83944 1.000 17.46891 ? 98  LEU A CD2  1 
ATOM   1641 H  H    . LEU A 1 102 ? 30.22436 24.20363 -23.30735 1.000 13.48995 ? 98  LEU A H    1 
ATOM   1642 H  HA   . LEU A 1 102 ? 27.66621 23.98699 -23.73933 1.000 14.54198 ? 98  LEU A HA   1 
ATOM   1643 H  HB2  . LEU A 1 102 ? 29.33493 26.22755 -24.07622 1.000 14.70347 ? 98  LEU A HB2  1 
ATOM   1644 H  HB3  . LEU A 1 102 ? 27.75994 26.31825 -24.26755 1.000 14.70347 ? 98  LEU A HB3  1 
ATOM   1645 H  HG   . LEU A 1 102 ? 28.95658 25.74406 -21.77568 1.000 17.23530 ? 98  LEU A HG   1 
ATOM   1646 H  HD11 . LEU A 1 102 ? 28.54928 27.93644 -21.19363 1.000 20.41141 ? 98  LEU A HD11 1 
ATOM   1647 H  HD12 . LEU A 1 102 ? 29.45199 27.93541 -22.50077 1.000 20.41141 ? 98  LEU A HD12 1 
ATOM   1648 H  HD13 . LEU A 1 102 ? 27.89305 28.21958 -22.61232 1.000 20.41141 ? 98  LEU A HD13 1 
ATOM   1649 H  HD21 . LEU A 1 102 ? 26.76017 26.26411 -20.96345 1.000 20.98742 ? 98  LEU A HD21 1 
ATOM   1650 H  HD22 . LEU A 1 102 ? 26.26115 26.22631 -22.47112 1.000 20.98742 ? 98  LEU A HD22 1 
ATOM   1651 H  HD23 . LEU A 1 102 ? 26.82994 24.90899 -21.78946 1.000 20.98742 ? 98  LEU A HD23 1 
ATOM   1652 N  N    . LYS A 1 103 ? 29.41242 24.34218 -26.40976 1.000 11.37103 ? 99  LYS A N    1 
ATOM   1653 C  CA   . LYS A 1 103 ? 29.37541 24.24668 -27.86663 1.000 11.84233 ? 99  LYS A CA   1 
ATOM   1654 C  C    . LYS A 1 103 ? 28.76565 22.92681 -28.30053 1.000 12.81431 ? 99  LYS A C    1 
ATOM   1655 O  O    . LYS A 1 103 ? 27.97821 22.88430 -29.24945 1.000 13.97111 ? 99  LYS A O    1 
ATOM   1656 C  CB   . LYS A 1 103 ? 30.78223 24.40498 -28.45037 1.000 12.53437 ? 99  LYS A CB   1 
ATOM   1657 C  CG   . LYS A 1 103 ? 30.81061 24.49351 -29.96820 1.000 13.99086 ? 99  LYS A CG   1 
ATOM   1658 C  CD   . LYS A 1 103 ? 32.23567 24.73576 -30.49106 1.000 18.18815 ? 99  LYS A CD   1 
ATOM   1659 C  CE   . LYS A 1 103 ? 32.31034 24.81862 -32.00541 1.000 20.29153 ? 99  LYS A CE   1 
ATOM   1660 N  NZ   . LYS A 1 103 ? 31.68441 26.06702 -32.47862 1.000 22.30731 ? 99  LYS A NZ   1 
ATOM   1661 H  H    . LYS A 1 103 ? 30.20193 24.45522 -26.08804 1.000 13.66996 ? 99  LYS A H    1 
ATOM   1662 H  HA   . LYS A 1 103 ? 28.83054 24.96966 -28.21494 1.000 14.23553 ? 99  LYS A HA   1 
ATOM   1663 H  HB2  . LYS A 1 103 ? 31.17557 25.21908 -28.09904 1.000 15.06597 ? 99  LYS A HB2  1 
ATOM   1664 H  HB3  . LYS A 1 103 ? 31.31625 23.63870 -28.18859 1.000 15.06597 ? 99  LYS A HB3  1 
ATOM   1665 H  HG2  . LYS A 1 103 ? 30.48495 23.66106 -30.34487 1.000 16.81376 ? 99  LYS A HG2  1 
ATOM   1666 H  HG3  . LYS A 1 103 ? 30.25015 25.23036 -30.25774 1.000 16.81376 ? 99  LYS A HG3  1 
ATOM   1667 H  HD2  . LYS A 1 103 ? 32.56525 25.57372 -30.13037 1.000 21.85051 ? 99  LYS A HD2  1 
ATOM   1668 H  HD3  . LYS A 1 103 ? 32.80485 24.00448 -30.20442 1.000 21.85051 ? 99  LYS A HD3  1 
ATOM   1669 H  HE2  . LYS A 1 103 ? 33.23853 24.81056 -32.28701 1.000 24.37457 ? 99  LYS A HE2  1 
ATOM   1670 H  HE3  . LYS A 1 103 ? 31.83838 24.06695 -32.39674 1.000 24.37457 ? 99  LYS A HE3  1 
ATOM   1671 H  HZ1  . LYS A 1 103 ? 31.73729 26.11683 -33.36565 1.000 26.79349 ? 99  LYS A HZ1  1 
ATOM   1672 H  HZ2  . LYS A 1 103 ? 30.82761 26.08790 -32.23872 1.000 26.79349 ? 99  LYS A HZ2  1 
ATOM   1673 H  HZ3  . LYS A 1 103 ? 32.10069 26.76948 -32.12455 1.000 26.79349 ? 99  LYS A HZ3  1 
ATOM   1674 N  N    . SER A 1 104 ? 29.08412 21.84536 -27.60026 1.000 12.94565 ? 100 SER A N    1 
ATOM   1675 C  CA   A SER A 1 104 ? 28.56108 20.53772 -27.96713 0.683 15.88979 ? 100 SER A CA   1 
ATOM   1676 C  CA   B SER A 1 104 ? 28.56910 20.53284 -27.96171 0.317 13.74913 ? 100 SER A CA   1 
ATOM   1677 C  C    . SER A 1 104 ? 27.20195 20.25970 -27.34343 1.000 14.40241 ? 100 SER A C    1 
ATOM   1678 O  O    . SER A 1 104 ? 26.33809 19.65919 -27.98729 1.000 19.92692 ? 100 SER A O    1 
ATOM   1679 C  CB   A SER A 1 104 ? 29.55841 19.44461 -27.57488 0.683 23.76283 ? 100 SER A CB   1 
ATOM   1680 C  CB   B SER A 1 104 ? 29.58524 19.44918 -27.56275 0.317 15.23560 ? 100 SER A CB   1 
ATOM   1681 O  OG   A SER A 1 104 ? 30.80320 19.65787 -28.20109 0.683 29.36782 ? 100 SER A OG   1 
ATOM   1682 O  OG   B SER A 1 104 ? 29.92597 19.49563 -26.18186 0.317 14.82254 ? 100 SER A OG   1 
ATOM   1683 H  H    . SER A 1 104 ? 29.59907 21.84300 -26.91148 1.000 15.55951 ? 100 SER A H    1 
ATOM   1684 H  HA   . SER A 1 104 ? 28.45138 20.50453 -28.93034 1.000 16.52368 ? 100 SER A HA   1 
ATOM   1685 H  HB2  A SER A 1 104 ? 29.68163 19.45925 -26.61285 0.683 28.54012 ? 100 SER A HB2  1 
ATOM   1686 H  HB2  B SER A 1 104 ? 29.20050 18.57998 -27.75605 0.317 18.30745 ? 100 SER A HB2  1 
ATOM   1687 H  HB3  A SER A 1 104 ? 29.20860 18.58320 -27.85147 0.683 28.54012 ? 100 SER A HB3  1 
ATOM   1688 H  HB3  B SER A 1 104 ? 30.39320 19.57768 -28.08390 0.317 18.30745 ? 100 SER A HB3  1 
ATOM   1689 H  HG   A SER A 1 104 ? 30.71161 19.64025 -29.03590 0.683 35.26611 ? 100 SER A HG   1 
ATOM   1690 H  HG   B SER A 1 104 ? 30.35265 20.19963 -26.01475 0.317 17.81177 ? 100 SER A HG   1 
ATOM   1691 N  N    . ALA A 1 105 ? 26.97948 20.71562 -26.11707 1.000 12.93744 ? 101 ALA A N    1 
ATOM   1692 C  CA   . ALA A 1 105 ? 25.76132 20.35830 -25.39410 1.000 12.75668 ? 101 ALA A CA   1 
ATOM   1693 C  C    . ALA A 1 105 ? 24.52842 21.07012 -25.93393 1.000 13.33633 ? 101 ALA A C    1 
ATOM   1694 O  O    . ALA A 1 105 ? 23.40619 20.58293 -25.73890 1.000 15.15095 ? 101 ALA A O    1 
ATOM   1695 C  CB   . ALA A 1 105 ? 25.91925 20.68675 -23.91117 1.000 14.60314 ? 101 ALA A CB   1 
ATOM   1696 H  H    . ALA A 1 105 ? 27.51127 21.23046 -25.67921 1.000 15.54965 ? 101 ALA A H    1 
ATOM   1697 H  HA   . ALA A 1 105 ? 25.62668 19.40334 -25.49813 1.000 15.33275 ? 101 ALA A HA   1 
ATOM   1698 H  HB1  . ALA A 1 105 ? 25.15732 20.33267 -23.42640 1.000 17.54850 ? 101 ALA A HB1  1 
ATOM   1699 H  HB2  . ALA A 1 105 ? 26.73728 20.28146 -23.58333 1.000 17.54850 ? 101 ALA A HB2  1 
ATOM   1700 H  HB3  . ALA A 1 105 ? 25.96114 21.64987 -23.80374 1.000 17.54850 ? 101 ALA A HB3  1 
ATOM   1701 N  N    . THR A 1 106 ? 24.70790 22.27025 -26.48082 1.000 12.54498 ? 102 THR A N    1 
ATOM   1702 C  CA   . THR A 1 106 ? 23.60814 23.10226 -26.95711 1.000 11.42094 ? 102 THR A CA   1 
ATOM   1703 C  C    . THR A 1 106 ? 23.39689 23.02463 -28.46688 1.000 12.37228 ? 102 THR A C    1 
ATOM   1704 O  O    . THR A 1 106 ? 22.58748 23.79854 -29.00968 1.000 13.32124 ? 102 THR A O    1 
ATOM   1705 C  CB   . THR A 1 106 ? 23.79895 24.56682 -26.55196 1.000 12.98031 ? 102 THR A CB   1 
ATOM   1706 O  OG1  . THR A 1 106 ? 24.89953 25.13491 -27.26474 1.000 12.56085 ? 102 THR A OG1  1 
ATOM   1707 C  CG2  . THR A 1 106 ? 23.98269 24.71767 -25.03120 1.000 14.45541 ? 102 THR A CG2  1 
ATOM   1708 H  H    . THR A 1 106 ? 25.48042 22.63238 -26.58884 1.000 15.07871 ? 102 THR A H    1 
ATOM   1709 H  HA   . THR A 1 106 ? 22.80484 22.77572 -26.52238 1.000 13.72986 ? 102 THR A HA   1 
ATOM   1710 H  HB   . THR A 1 106 ? 22.99898 25.06481 -26.78206 1.000 15.60110 ? 102 THR A HB   1 
ATOM   1711 H  HG1  . THR A 1 106 ? 25.62250 24.81987 -26.97550 1.000 15.09775 ? 102 THR A HG1  1 
ATOM   1712 H  HG21 . THR A 1 106 ? 24.01085 25.65730 -24.79202 1.000 17.37123 ? 102 THR A HG21 1 
ATOM   1713 H  HG22 . THR A 1 106 ? 23.24434 24.29599 -24.56437 1.000 17.37123 ? 102 THR A HG22 1 
ATOM   1714 H  HG23 . THR A 1 106 ? 24.81170 24.29726 -24.75387 1.000 17.37123 ? 102 THR A HG23 1 
ATOM   1715 N  N    . LYS A 1 107 ? 24.07633 22.10797 -29.15726 1.000 13.21900 ? 103 LYS A N    1 
ATOM   1716 C  CA   A LYS A 1 107 ? 23.94736 21.98406 -30.59401 0.361 15.57375 ? 103 LYS A CA   1 
ATOM   1717 C  CA   B LYS A 1 107 ? 23.91892 21.94457 -30.60277 0.639 15.43683 ? 103 LYS A CA   1 
ATOM   1718 C  C    . LYS A 1 107 ? 22.50812 21.62904 -31.01718 1.000 17.98930 ? 103 LYS A C    1 
ATOM   1719 O  O    . LYS A 1 107 ? 21.77157 20.97011 -30.27172 1.000 16.87250 ? 103 LYS A O    1 
ATOM   1720 C  CB   A LYS A 1 107 ? 24.95824 20.93628 -31.07225 0.361 16.26686 ? 103 LYS A CB   1 
ATOM   1721 C  CB   B LYS A 1 107 ? 24.79903 20.80834 -31.12357 0.639 17.13708 ? 103 LYS A CB   1 
ATOM   1722 C  CG   A LYS A 1 107 ? 25.25814 20.97494 -32.54441 0.361 17.33008 ? 103 LYS A CG   1 
ATOM   1723 C  CG   B LYS A 1 107 ? 26.22334 21.20000 -31.29804 0.639 17.09133 ? 103 LYS A CG   1 
ATOM   1724 C  CD   A LYS A 1 107 ? 26.54788 20.24360 -32.89978 0.361 17.45871 ? 103 LYS A CD   1 
ATOM   1725 C  CD   B LYS A 1 107 ? 27.08876 20.15181 -31.96956 0.639 19.09691 ? 103 LYS A CD   1 
ATOM   1726 C  CE   A LYS A 1 107 ? 27.77164 21.13796 -32.71482 0.361 20.53821 ? 103 LYS A CE   1 
ATOM   1727 C  CE   B LYS A 1 107 ? 28.48364 20.74225 -32.17525 0.639 22.59166 ? 103 LYS A CE   1 
ATOM   1728 N  NZ   A LYS A 1 107 ? 29.02131 20.47597 -33.18086 0.361 23.70187 ? 103 LYS A NZ   1 
ATOM   1729 N  NZ   B LYS A 1 107 ? 29.47931 19.80879 -32.74932 0.639 27.39776 ? 103 LYS A NZ   1 
ATOM   1730 O  OXT  . LYS A 1 107 ? 22.08039 22.01205 -32.11205 1.000 20.58461 ? 103 LYS A OXT  1 
ATOM   1731 H  H    A LYS A 1 107 ? 24.62212 21.54374 -28.80604 0.361 15.88753 ? 103 LYS A H    1 
ATOM   1732 H  H    B LYS A 1 107 ? 24.64128 21.56200 -28.80748 0.639 15.88753 ? 103 LYS A H    1 
ATOM   1733 H  HA   A LYS A 1 107 ? 24.14004 22.82942 -31.02891 0.361 18.71323 ? 103 LYS A HA   1 
ATOM   1734 H  HA   B LYS A 1 107 ? 24.17921 22.79148 -30.99760 0.639 18.54893 ? 103 LYS A HA   1 
ATOM   1735 H  HB2  A LYS A 1 107 ? 25.79403 21.07737 -30.60059 0.361 19.54497 ? 103 LYS A HB2  1 
ATOM   1736 H  HB2  B LYS A 1 107 ? 24.76738 20.07259 -30.49224 0.639 20.58922 ? 103 LYS A HB2  1 
ATOM   1737 H  HB3  A LYS A 1 107 ? 24.60736 20.05507 -30.86918 0.361 19.54497 ? 103 LYS A HB3  1 
ATOM   1738 H  HB3  B LYS A 1 107 ? 24.46131 20.52020 -31.98602 0.639 20.58922 ? 103 LYS A HB3  1 
ATOM   1739 H  HG2  A LYS A 1 107 ? 24.53073 20.55234 -33.02730 0.361 20.82082 ? 103 LYS A HG2  1 
ATOM   1740 H  HG2  B LYS A 1 107 ? 26.25927 22.00106 -31.84385 0.639 20.53432 ? 103 LYS A HG2  1 
ATOM   1741 H  HG3  A LYS A 1 107 ? 25.35003 21.89891 -32.82503 0.361 20.82082 ? 103 LYS A HG3  1 
ATOM   1742 H  HG3  B LYS A 1 107 ? 26.60488 21.37674 -30.42392 0.639 20.53432 ? 103 LYS A HG3  1 
ATOM   1743 H  HD2  A LYS A 1 107 ? 26.64688 19.46952 -32.32367 0.361 20.97518 ? 103 LYS A HD2  1 
ATOM   1744 H  HD2  B LYS A 1 107 ? 27.15612 19.36454 -31.40690 0.639 22.94102 ? 103 LYS A HD2  1 
ATOM   1745 H  HD3  A LYS A 1 107 ? 26.51282 19.96404 -33.82796 0.361 20.97518 ? 103 LYS A HD3  1 
ATOM   1746 H  HD3  B LYS A 1 107 ? 26.71413 19.91238 -32.83166 0.639 22.94102 ? 103 LYS A HD3  1 
ATOM   1747 H  HE2  A LYS A 1 107 ? 27.65160 21.95318 -33.22660 0.361 24.67058 ? 103 LYS A HE2  1 
ATOM   1748 H  HE2  B LYS A 1 107 ? 28.41200 21.49771 -32.77944 0.639 27.13472 ? 103 LYS A HE2  1 
ATOM   1749 H  HE3  A LYS A 1 107 ? 27.87347 21.34910 -31.77358 0.361 24.67058 ? 103 LYS A HE3  1 
ATOM   1750 H  HE3  B LYS A 1 107 ? 28.82329 21.03609 -31.31549 0.639 27.13472 ? 103 LYS A HE3  1 
ATOM   1751 H  HZ1  A LYS A 1 107 ? 29.72665 20.97860 -32.97605 0.361 28.46697 ? 103 LYS A HZ1  1 
ATOM   1752 H  HZ1  B LYS A 1 107 ? 30.30148 20.12545 -32.62333 0.639 32.90204 ? 103 LYS A HZ1  1 
ATOM   1753 H  HZ2  A LYS A 1 107 ? 29.10924 19.68159 -32.78927 0.361 28.46697 ? 103 LYS A HZ2  1 
ATOM   1754 H  HZ2  B LYS A 1 107 ? 29.41281 19.01317 -32.35604 0.639 32.90204 ? 103 LYS A HZ2  1 
ATOM   1755 H  HZ3  A LYS A 1 107 ? 28.99447 20.36170 -34.06309 0.361 28.46697 ? 103 LYS A HZ3  1 
ATOM   1756 H  HZ3  B LYS A 1 107 ? 29.33773 19.71204 -33.62264 0.639 32.90204 ? 103 LYS A HZ3  1 
ATOM   1757 N  N    . GLY B 1 1   ? 11.28704 23.62364 13.25685  1.000 30.37823 ? -3  GLY B N    1 
ATOM   1758 C  CA   . GLY B 1 1   ? 11.48916 22.26421 12.78099  1.000 28.71510 ? -3  GLY B CA   1 
ATOM   1759 C  C    . GLY B 1 1   ? 12.07061 22.19231 11.38501  1.000 25.88969 ? -3  GLY B C    1 
ATOM   1760 O  O    . GLY B 1 1   ? 12.23187 23.22704 10.71884  1.000 24.37783 ? -3  GLY B O    1 
ATOM   1761 H  HA2  . GLY B 1 1   ? 12.09510 21.80503 13.38340  1.000 34.48284 ? -3  GLY B HA2  1 
ATOM   1762 H  HA3  . GLY B 1 1   ? 10.63706 21.80075 12.77632  1.000 34.48284 ? -3  GLY B HA3  1 
ATOM   1763 N  N    . VAL B 1 2   ? 12.36378 20.96723 10.94796  1.000 21.83501 ? -2  VAL B N    1 
ATOM   1764 C  CA   . VAL B 1 2   ? 13.02126 20.70891 9.66677   1.000 21.74228 ? -2  VAL B CA   1 
ATOM   1765 C  C    . VAL B 1 2   ? 12.23691 19.64095 8.89882   1.000 22.24865 ? -2  VAL B C    1 
ATOM   1766 O  O    . VAL B 1 2   ? 11.94850 18.57809 9.46825   1.000 23.96232 ? -2  VAL B O    1 
ATOM   1767 C  CB   . VAL B 1 2   ? 14.48050 20.26905 9.87789   1.000 22.87636 ? -2  VAL B CB   1 
ATOM   1768 C  CG1  . VAL B 1 2   ? 15.18812 20.10833 8.53634   1.000 24.16667 ? -2  VAL B CG1  1 
ATOM   1769 C  CG2  . VAL B 1 2   ? 15.23683 21.28056 10.74237  1.000 24.16010 ? -2  VAL B CG2  1 
ATOM   1770 H  H    . VAL B 1 2   ? 12.18679 20.24985 11.38801  1.000 26.22674 ? -2  VAL B H    1 
ATOM   1771 H  HA   . VAL B 1 2   ? 13.01185 21.52435 9.14154   1.000 26.11546 ? -2  VAL B HA   1 
ATOM   1772 H  HB   . VAL B 1 2   ? 14.47723 19.41448 10.33682  1.000 27.47636 ? -2  VAL B HB   1 
ATOM   1773 H  HG11 . VAL B 1 2   ? 16.14362 20.04117 8.68934   1.000 29.02474 ? -2  VAL B HG11 1 
ATOM   1774 H  HG12 . VAL B 1 2   ? 14.86502 19.30268 8.10340   1.000 29.02474 ? -2  VAL B HG12 1 
ATOM   1775 H  HG13 . VAL B 1 2   ? 14.99526 20.88131 7.98297   1.000 29.02474 ? -2  VAL B HG13 1 
ATOM   1776 H  HG21 . VAL B 1 2   ? 16.18056 21.05637 10.73814  1.000 29.01685 ? -2  VAL B HG21 1 
ATOM   1777 H  HG22 . VAL B 1 2   ? 15.10629 22.16915 10.37596  1.000 29.01685 ? -2  VAL B HG22 1 
ATOM   1778 H  HG23 . VAL B 1 2   ? 14.89181 21.24228 11.64813  1.000 29.01685 ? -2  VAL B HG23 1 
ATOM   1779 N  N    . PRO B 1 3   ? 11.90205 19.83356 7.61523   1.000 21.10891 ? -1  PRO B N    1 
ATOM   1780 C  CA   . PRO B 1 3   ? 11.19013 18.77191 6.89315   1.000 23.10843 ? -1  PRO B CA   1 
ATOM   1781 C  C    . PRO B 1 3   ? 12.07351 17.55621 6.68055   1.000 25.65711 ? -1  PRO B C    1 
ATOM   1782 O  O    . PRO B 1 3   ? 13.28893 17.67184 6.50154   1.000 24.92154 ? -1  PRO B O    1 
ATOM   1783 C  CB   . PRO B 1 3   ? 10.84043 19.41382 5.54302   1.000 25.71408 ? -1  PRO B CB   1 
ATOM   1784 C  CG   . PRO B 1 3   ? 11.19262 20.84393 5.64295   1.000 23.92737 ? -1  PRO B CG   1 
ATOM   1785 C  CD   . PRO B 1 3   ? 12.17474 20.99293 6.74519   1.000 22.49372 ? -1  PRO B CD   1 
ATOM   1786 H  HA   . PRO B 1 3   ? 10.38012 18.52680 7.36718   1.000 27.75484 ? -1  PRO B HA   1 
ATOM   1787 H  HB2  . PRO B 1 3   ? 11.35356 18.98555 4.84005   1.000 30.88162 ? -1  PRO B HB2  1 
ATOM   1788 H  HB3  . PRO B 1 3   ? 9.89141  19.30843 5.37228   1.000 30.88162 ? -1  PRO B HB3  1 
ATOM   1789 H  HG2  . PRO B 1 3   ? 11.58173 21.13624 4.80388   1.000 28.73757 ? -1  PRO B HG2  1 
ATOM   1790 H  HG3  . PRO B 1 3   ? 10.39205 21.35724 5.83403   1.000 28.73757 ? -1  PRO B HG3  1 
ATOM   1791 H  HD2  . PRO B 1 3   ? 13.08208 20.96051 6.40375   1.000 27.01719 ? -1  PRO B HD2  1 
ATOM   1792 H  HD3  . PRO B 1 3   ? 12.03009 21.82379 7.22441   1.000 27.01719 ? -1  PRO B HD3  1 
ATOM   1793 N  N    . ALA B 1 4   ? 11.44619 16.38459 6.65098   1.000 25.83786 ? 0   ALA B N    1 
ATOM   1794 C  CA   . ALA B 1 4   ? 12.15783 15.17287 6.26887   1.000 26.65107 ? 0   ALA B CA   1 
ATOM   1795 C  C    . ALA B 1 4   ? 12.67838 15.31664 4.84010   1.000 27.17173 ? 0   ALA B C    1 
ATOM   1796 O  O    . ALA B 1 4   ? 12.05635 15.97150 3.99663   1.000 27.25896 ? 0   ALA B O    1 
ATOM   1797 C  CB   . ALA B 1 4   ? 11.23337 13.96281 6.35388   1.000 29.26273 ? 0   ALA B CB   1 
ATOM   1798 H  H    . ALA B 1 4   ? 10.61713 16.26467 6.84560   1.000 31.03016 ? 0   ALA B H    1 
ATOM   1799 H  HA   . ALA B 1 4   ? 12.90402 15.02573 6.87092   1.000 32.00601 ? 0   ALA B HA   1 
ATOM   1800 H  HB1  . ALA B 1 4   ? 11.73863 13.16356 6.13750   1.000 35.14001 ? 0   ALA B HB1  1 
ATOM   1801 H  HB2  . ALA B 1 4   ? 10.88086 13.89740 7.25519   1.000 35.14001 ? 0   ALA B HB2  1 
ATOM   1802 H  HB3  . ALA B 1 4   ? 10.50635 14.07579 5.72175   1.000 35.14001 ? 0   ALA B HB3  1 
ATOM   1803 N  N    . GLY B 1 5   ? 13.83683 14.69880 4.57297   1.000 25.62745 ? 1   GLY B N    1 
ATOM   1804 C  CA   . GLY B 1 5   ? 14.54611 14.91039 3.32787   1.000 26.58636 ? 1   GLY B CA   1 
ATOM   1805 C  C    . GLY B 1 5   ? 14.89193 13.61397 2.61956   1.000 28.97670 ? 1   GLY B C    1 
ATOM   1806 O  O    . GLY B 1 5   ? 14.98039 12.54599 3.22303   1.000 31.60584 ? 1   GLY B O    1 
ATOM   1807 H  H    . GLY B 1 5   ? 14.22744 14.14985 5.10745   1.000 30.77766 ? 1   GLY B H    1 
ATOM   1808 H  HA2  . GLY B 1 5   ? 13.99581 15.44359 2.73308   1.000 31.92837 ? 1   GLY B HA2  1 
ATOM   1809 H  HA3  . GLY B 1 5   ? 15.37136 15.38759 3.50715   1.000 31.92837 ? 1   GLY B HA3  1 
ATOM   1810 N  N    . ASP B 1 6   ? 15.10070 13.73964 1.30818   1.000 28.92242 ? 2   ASP B N    1 
ATOM   1811 C  CA   . ASP B 1 6   ? 15.48097 12.63362 0.43243   1.000 30.07067 ? 2   ASP B CA   1 
ATOM   1812 C  C    . ASP B 1 6   ? 16.94799 12.78994 0.04158   1.000 28.62535 ? 2   ASP B C    1 
ATOM   1813 O  O    . ASP B 1 6   ? 17.33970 13.82114 -0.51864  1.000 27.41191 ? 2   ASP B O    1 
ATOM   1814 C  CB   . ASP B 1 6   ? 14.58833 12.61098 -0.81187  1.000 32.58970 ? 2   ASP B CB   1 
ATOM   1815 C  CG   . ASP B 1 6   ? 14.89793 11.43723 -1.74959  1.000 36.13030 ? 2   ASP B CG   1 
ATOM   1816 O  OD1  . ASP B 1 6   ? 15.83729 11.54409 -2.56227  1.000 35.52255 ? 2   ASP B OD1  1 
ATOM   1817 O  OD2  . ASP B 1 6   ? 14.20043 10.39968 -1.67728  1.000 40.64355 ? 2   ASP B OD2  1 
ATOM   1818 H  H    . ASP B 1 6   ? 15.02417 14.48701 0.88964   1.000 34.73164 ? 2   ASP B H    1 
ATOM   1819 H  HA   . ASP B 1 6   ? 15.38370 11.79136 0.90365   1.000 36.10954 ? 2   ASP B HA   1 
ATOM   1820 H  HB2  . ASP B 1 6   ? 13.66205 12.53544 -0.53403  1.000 39.13237 ? 2   ASP B HB2  1 
ATOM   1821 H  HB3  . ASP B 1 6   ? 14.71955 13.43350 -1.30900  1.000 39.13237 ? 2   ASP B HB3  1 
ATOM   1822 N  N    . VAL B 1 7   ? 17.75199 11.75569 0.32255   1.000 28.69307 ? 3   VAL B N    1 
ATOM   1823 C  CA   . VAL B 1 7   ? 19.20302 11.83748 0.12676   1.000 26.53626 ? 3   VAL B CA   1 
ATOM   1824 C  C    . VAL B 1 7   ? 19.55141 12.04194 -1.34527  1.000 25.25646 ? 3   VAL B C    1 
ATOM   1825 O  O    . VAL B 1 7   ? 20.45666 12.81652 -1.68559  1.000 24.15329 ? 3   VAL B O    1 
ATOM   1826 C  CB   . VAL B 1 7   ? 19.88957 10.58721 0.70980   1.000 30.86740 ? 3   VAL B CB   1 
ATOM   1827 C  CG1  . VAL B 1 7   ? 21.34457 10.48215 0.24218   1.000 30.33499 ? 3   VAL B CG1  1 
ATOM   1828 C  CG2  . VAL B 1 7   ? 19.82160 10.61988 2.23263   1.000 33.11517 ? 3   VAL B CG2  1 
ATOM   1829 H  H    . VAL B 1 7   ? 17.48441 10.99714 0.62687   1.000 34.45642 ? 3   VAL B H    1 
ATOM   1830 H  HA   . VAL B 1 7   ? 19.52893 12.61385 0.60835   1.000 31.86825 ? 3   VAL B HA   1 
ATOM   1831 H  HB   . VAL B 1 7   ? 19.42235 9.79960  0.38999   1.000 37.06561 ? 3   VAL B HB   1 
ATOM   1832 H  HG11 . VAL B 1 7   ? 21.83504 9.91814  0.86043   1.000 36.42672 ? 3   VAL B HG11 1 
ATOM   1833 H  HG12 . VAL B 1 7   ? 21.36344 10.09347 -0.64635  1.000 36.42672 ? 3   VAL B HG12 1 
ATOM   1834 H  HG13 . VAL B 1 7   ? 21.73508 11.36987 0.22325   1.000 36.42672 ? 3   VAL B HG13 1 
ATOM   1835 H  HG21 . VAL B 1 7   ? 20.23837 9.81782  2.58463   1.000 39.76294 ? 3   VAL B HG21 1 
ATOM   1836 H  HG22 . VAL B 1 7   ? 20.29237 11.40514 2.55299   1.000 39.76294 ? 3   VAL B HG22 1 
ATOM   1837 H  HG23 . VAL B 1 7   ? 18.89181 10.65696 2.50652   1.000 39.76294 ? 3   VAL B HG23 1 
ATOM   1838 N  N    . GLU B 1 8   ? 18.85077 11.34595 -2.23973  1.000 26.62957 ? 4   GLU B N    1 
ATOM   1839 C  CA   . GLU B 1 8   ? 19.17184 11.44921 -3.66024  1.000 28.76208 ? 4   GLU B CA   1 
ATOM   1840 C  C    . GLU B 1 8   ? 18.86869 12.84121 -4.20287  1.000 24.48597 ? 4   GLU B C    1 
ATOM   1841 O  O    . GLU B 1 8   ? 19.67447 13.41375 -4.94927  1.000 23.18742 ? 4   GLU B O    1 
ATOM   1842 C  CB   . GLU B 1 8   ? 18.41574 10.37831 -4.44214  1.000 36.09764 ? 4   GLU B CB   1 
ATOM   1843 C  CG   . GLU B 1 8   ? 19.09721 9.01722  -4.43652  1.000 46.20630 ? 4   GLU B CG   1 
ATOM   1844 C  CD   . GLU B 1 8   ? 20.08005 8.84816  -5.58656  1.000 53.97320 ? 4   GLU B CD   1 
ATOM   1845 O  OE1  . GLU B 1 8   ? 21.00629 9.68126  -5.71772  1.000 56.58322 ? 4   GLU B OE1  1 
ATOM   1846 O  OE2  . GLU B 1 8   ? 19.90988 7.88876  -6.37287  1.000 57.20247 ? 4   GLU B OE2  1 
ATOM   1847 H  H    . GLU B 1 8   ? 18.19782 10.81718 -2.05627  1.000 31.98021 ? 4   GLU B H    1 
ATOM   1848 H  HA   . GLU B 1 8   ? 20.12139 11.29143 -3.78004  1.000 34.53923 ? 4   GLU B HA   1 
ATOM   1849 H  HB2  . GLU B 1 8   ? 17.53504 10.26992 -4.05032  1.000 43.34189 ? 4   GLU B HB2  1 
ATOM   1850 H  HB3  . GLU B 1 8   ? 18.33514 10.66509 -5.36527  1.000 43.34189 ? 4   GLU B HB3  1 
ATOM   1851 H  HG2  . GLU B 1 8   ? 19.58636 8.91172  -3.60556  1.000 55.47229 ? 4   GLU B HG2  1 
ATOM   1852 H  HG3  . GLU B 1 8   ? 18.42212 8.32505  -4.51428  1.000 55.47229 ? 4   GLU B HG3  1 
ATOM   1853 N  N    . LYS B 1 9   ? 17.71162 13.40227 -3.84778  1.000 24.35588 ? 5   LYS B N    1 
ATOM   1854 C  CA   . LYS B 1 9   ? 17.41775 14.77117 -4.25395  1.000 23.63976 ? 5   LYS B CA   1 
ATOM   1855 C  C    . LYS B 1 9   ? 18.41069 15.74494 -3.63216  1.000 19.21136 ? 5   LYS B C    1 
ATOM   1856 O  O    . LYS B 1 9   ? 18.82934 16.71519 -4.27617  1.000 20.46899 ? 5   LYS B O    1 
ATOM   1857 C  CB   . LYS B 1 9   ? 15.98746 15.14586 -3.86495  1.000 27.09083 ? 5   LYS B CB   1 
ATOM   1858 C  CG   . LYS B 1 9   ? 14.90054 14.38690 -4.62964  1.000 30.68253 ? 5   LYS B CG   1 
ATOM   1859 C  CD   . LYS B 1 9   ? 13.50066 14.83443 -4.19278  1.000 34.39188 ? 5   LYS B CD   1 
ATOM   1860 C  CE   . LYS B 1 9   ? 12.42007 13.91171 -4.71482  1.000 41.26771 ? 5   LYS B CE   1 
ATOM   1861 N  NZ   . LYS B 1 9   ? 11.11079 14.20320 -4.05915  1.000 45.20528 ? 5   LYS B NZ   1 
ATOM   1862 H  H    . LYS B 1 9   ? 17.09542 13.02196 -3.38382  1.000 29.25178 ? 5   LYS B H    1 
ATOM   1863 H  HA   . LYS B 1 9   ? 17.48823 14.83360 -5.21937  1.000 28.39244 ? 5   LYS B HA   1 
ATOM   1864 H  HB2  . LYS B 1 9   ? 15.86549 14.95951 -2.92086  1.000 32.53372 ? 5   LYS B HB2  1 
ATOM   1865 H  HB3  . LYS B 1 9   ? 15.85898 16.09204 -4.03565  1.000 32.53372 ? 5   LYS B HB3  1 
ATOM   1866 H  HG2  . LYS B 1 9   ? 14.99450 14.55912 -5.57959  1.000 36.84377 ? 5   LYS B HG2  1 
ATOM   1867 H  HG3  . LYS B 1 9   ? 14.98676 13.43673 -4.45461  1.000 36.84377 ? 5   LYS B HG3  1 
ATOM   1868 H  HD2  . LYS B 1 9   ? 13.45424 14.83689 -3.22389  1.000 41.29498 ? 5   LYS B HD2  1 
ATOM   1869 H  HD3  . LYS B 1 9   ? 13.32904 15.72552 -4.53540  1.000 41.29498 ? 5   LYS B HD3  1 
ATOM   1870 H  HE2  . LYS B 1 9   ? 12.32039 14.03856 -5.67131  1.000 49.54598 ? 5   LYS B HE2  1 
ATOM   1871 H  HE3  . LYS B 1 9   ? 12.66103 12.99138 -4.52554  1.000 49.54598 ? 5   LYS B HE3  1 
ATOM   1872 H  HZ1  . LYS B 1 9   ? 10.46639 13.72023 -4.43808  1.000 54.27106 ? 5   LYS B HZ1  1 
ATOM   1873 H  HZ2  . LYS B 1 9   ? 11.15220 14.00098 -3.19342  1.000 54.27106 ? 5   LYS B HZ2  1 
ATOM   1874 H  HZ3  . LYS B 1 9   ? 10.91296 15.06669 -4.14493  1.000 54.27106 ? 5   LYS B HZ3  1 
ATOM   1875 N  N    . GLY B 1 10  ? 18.80932 15.49491 -2.38368  1.000 19.19267 ? 6   GLY B N    1 
ATOM   1876 C  CA   . GLY B 1 10  ? 19.77151 16.36515 -1.73201  1.000 18.20391 ? 6   GLY B CA   1 
ATOM   1877 C  C    . GLY B 1 10  ? 21.12897 16.33974 -2.39493  1.000 16.63048 ? 6   GLY B C    1 
ATOM   1878 O  O    . GLY B 1 10  ? 21.83431 17.35263 -2.40058  1.000 15.77728 ? 6   GLY B O    1 
ATOM   1879 H  H    . GLY B 1 10  ? 18.54007 14.83625 -1.90071  1.000 23.05594 ? 6   GLY B H    1 
ATOM   1880 H  HA2  . GLY B 1 10  ? 19.44103 17.27692 -1.75100  1.000 21.86942 ? 6   GLY B HA2  1 
ATOM   1881 H  HA3  . GLY B 1 10  ? 19.87886 16.08731 -0.80887  1.000 21.86942 ? 6   GLY B HA3  1 
ATOM   1882 N  N    . LYS B 1 11  ? 21.51214 15.18978 -2.95227  1.000 18.60029 ? 7   LYS B N    1 
ATOM   1883 C  CA   . LYS B 1 11  ? 22.78369 15.09361 -3.65783  1.000 18.81253 ? 7   LYS B CA   1 
ATOM   1884 C  C    . LYS B 1 11  ? 22.81368 16.03904 -4.84770  1.000 18.09132 ? 7   LYS B C    1 
ATOM   1885 O  O    . LYS B 1 11  ? 23.83133 16.69726 -5.09934  1.000 17.06634 ? 7   LYS B O    1 
ATOM   1886 C  CB   . LYS B 1 11  ? 23.02614 13.65305 -4.10406  1.000 21.29070 ? 7   LYS B CB   1 
ATOM   1887 C  CG   . LYS B 1 11  ? 24.38010 13.43673 -4.76229  1.000 25.60906 ? 7   LYS B CG   1 
ATOM   1888 C  CD   . LYS B 1 11  ? 24.62728 11.95639 -5.02184  1.000 33.15051 ? 7   LYS B CD   1 
ATOM   1889 C  CE   . LYS B 1 11  ? 26.08644 11.68185 -5.36880  1.000 41.00455 ? 7   LYS B CE   1 
ATOM   1890 N  NZ   . LYS B 1 11  ? 26.38668 10.22359 -5.35511  1.000 45.00735 ? 7   LYS B NZ   1 
ATOM   1891 H  H    . LYS B 1 11  ? 21.05943 14.45874 -2.93642  1.000 22.34508 ? 7   LYS B H    1 
ATOM   1892 H  HA   . LYS B 1 11  ? 23.50232 15.34229 -3.05564  1.000 22.59976 ? 7   LYS B HA   1 
ATOM   1893 H  HB2  . LYS B 1 11  ? 22.97806 13.07360 -3.32764  1.000 25.57356 ? 7   LYS B HB2  1 
ATOM   1894 H  HB3  . LYS B 1 11  ? 22.34183 13.40572 -4.74550  1.000 25.57356 ? 7   LYS B HB3  1 
ATOM   1895 H  HG2  . LYS B 1 11  ? 24.40621 13.90618 -5.61072  1.000 30.75560 ? 7   LYS B HG2  1 
ATOM   1896 H  HG3  . LYS B 1 11  ? 25.08041 13.76761 -4.17836  1.000 30.75560 ? 7   LYS B HG3  1 
ATOM   1897 H  HD2  . LYS B 1 11  ? 24.40334 11.44945 -4.22575  1.000 39.80534 ? 7   LYS B HD2  1 
ATOM   1898 H  HD3  . LYS B 1 11  ? 24.07765 11.66515 -5.76615  1.000 39.80534 ? 7   LYS B HD3  1 
ATOM   1899 H  HE2  . LYS B 1 11  ? 26.27496 12.02358 -6.25682  1.000 49.23019 ? 7   LYS B HE2  1 
ATOM   1900 H  HE3  . LYS B 1 11  ? 26.65856 12.11702 -4.71749  1.000 49.23019 ? 7   LYS B HE3  1 
ATOM   1901 H  HZ1  . LYS B 1 11  ? 27.24021 10.08654 -5.56676  1.000 54.03355 ? 7   LYS B HZ1  1 
ATOM   1902 H  HZ2  . LYS B 1 11  ? 26.23260 9.88868  -4.54505  1.000 54.03355 ? 7   LYS B HZ2  1 
ATOM   1903 H  HZ3  . LYS B 1 11  ? 25.87137 9.80116  -5.94512  1.000 54.03355 ? 7   LYS B HZ3  1 
ATOM   1904 N  N    . LYS B 1 12  ? 21.70323 16.12301 -5.59155  1.000 18.03363 ? 8   LYS B N    1 
ATOM   1905 C  CA   . LYS B 1 12  ? 21.63822 17.01243 -6.74415  1.000 18.02694 ? 8   LYS B CA   1 
ATOM   1906 C  C    . LYS B 1 12  ? 21.74199 18.46774 -6.31974  1.000 16.59292 ? 8   LYS B C    1 
ATOM   1907 O  O    . LYS B 1 12  ? 22.42359 19.26413 -6.97333  1.000 16.33050 ? 8   LYS B O    1 
ATOM   1908 C  CB   . LYS B 1 12  ? 20.32930 16.78598 -7.50517  1.000 20.24222 ? 8   LYS B CB   1 
ATOM   1909 C  CG   . LYS B 1 12  ? 20.15939 17.71244 -8.71574  1.000 25.16629 ? 8   LYS B CG   1 
ATOM   1910 C  CD   . LYS B 1 12  ? 18.97368 17.33592 -9.56284  1.000 30.82982 ? 8   LYS B CD   1 
ATOM   1911 C  CE   . LYS B 1 12  ? 18.93644 18.18067 -10.83843 1.000 35.28655 ? 8   LYS B CE   1 
ATOM   1912 N  NZ   . LYS B 1 12  ? 17.94992 17.71248 -11.85255 1.000 39.03187 ? 8   LYS B NZ   1 
ATOM   1913 H  H    . LYS B 1 12  ? 20.98104 15.67828 -5.44922  1.000 21.66508 ? 8   LYS B H    1 
ATOM   1914 H  HA   . LYS B 1 12  ? 22.37955 16.80897 -7.33570  1.000 21.65706 ? 8   LYS B HA   1 
ATOM   1915 H  HB2  . LYS B 1 12  ? 20.30784 15.87071 -7.82567  1.000 24.31540 ? 8   LYS B HB2  1 
ATOM   1916 H  HB3  . LYS B 1 12  ? 19.58560 16.94409 -6.90283  1.000 24.31540 ? 8   LYS B HB3  1 
ATOM   1917 H  HG2  . LYS B 1 12  ? 20.03053 18.62206 -8.40447  1.000 30.22428 ? 8   LYS B HG2  1 
ATOM   1918 H  HG3  . LYS B 1 12  ? 20.95394 17.66079 -9.26974  1.000 30.22428 ? 8   LYS B HG3  1 
ATOM   1919 H  HD2  . LYS B 1 12  ? 19.03672 16.40089 -9.81311  1.000 37.02052 ? 8   LYS B HD2  1 
ATOM   1920 H  HD3  . LYS B 1 12  ? 18.15588 17.49170 -9.06501  1.000 37.02052 ? 8   LYS B HD3  1 
ATOM   1921 H  HE2  . LYS B 1 12  ? 18.70344 19.09186 -10.60104 1.000 42.36858 ? 8   LYS B HE2  1 
ATOM   1922 H  HE3  . LYS B 1 12  ? 19.81409 18.15941 -11.25097 1.000 42.36858 ? 8   LYS B HE3  1 
ATOM   1923 H  HZ1  . LYS B 1 12  ? 17.94920 18.26182 -12.55278 1.000 46.86298 ? 8   LYS B HZ1  1 
ATOM   1924 H  HZ2  . LYS B 1 12  ? 18.16228 16.89335 -12.12828 1.000 46.86298 ? 8   LYS B HZ2  1 
ATOM   1925 H  HZ3  . LYS B 1 12  ? 17.13376 17.69537 -11.49802 1.000 46.86298 ? 8   LYS B HZ3  1 
ATOM   1926 N  N    . ILE B 1 13  ? 21.05238 18.83608 -5.24079  1.000 16.16938 ? 9   ILE B N    1 
ATOM   1927 C  CA   . ILE B 1 13  ? 21.16204 20.19132 -4.71439  1.000 15.17691 ? 9   ILE B CA   1 
ATOM   1928 C  C    . ILE B 1 13  ? 22.60406 20.48135 -4.32405  1.000 14.13380 ? 9   ILE B C    1 
ATOM   1929 O  O    . ILE B 1 13  ? 23.14917 21.54836 -4.64094  1.000 14.50743 ? 9   ILE B O    1 
ATOM   1930 C  CB   . ILE B 1 13  ? 20.19643 20.38718 -3.52759  1.000 15.88617 ? 9   ILE B CB   1 
ATOM   1931 C  CG1  . ILE B 1 13  ? 18.73223 20.26824 -3.99348  1.000 18.27888 ? 9   ILE B CG1  1 
ATOM   1932 C  CG2  . ILE B 1 13  ? 20.42455 21.75092 -2.89660  1.000 16.67755 ? 9   ILE B CG2  1 
ATOM   1933 C  CD1  . ILE B 1 13  ? 17.77294 19.99821 -2.90315  1.000 20.31679 ? 9   ILE B CD1  1 
ATOM   1934 H  H    . ILE B 1 13  ? 20.51925 18.32588 -4.79912  1.000 19.42799 ? 9   ILE B H    1 
ATOM   1935 H  HA   . ILE B 1 13  ? 20.90690 20.81961 -5.40798  1.000 18.23702 ? 9   ILE B HA   1 
ATOM   1936 H  HB   . ILE B 1 13  ? 20.37174 19.69271 -2.87345  1.000 19.08814 ? 9   ILE B HB   1 
ATOM   1937 H  HG12 . ILE B 1 13  ? 18.47179 21.10195 -4.41537  1.000 21.95939 ? 9   ILE B HG12 1 
ATOM   1938 H  HG13 . ILE B 1 13  ? 18.66713 19.53958 -4.63045  1.000 21.95939 ? 9   ILE B HG13 1 
ATOM   1939 H  HG21 . ILE B 1 13  ? 19.61470 22.02686 -2.43955  1.000 20.03779 ? 9   ILE B HG21 1 
ATOM   1940 H  HG22 . ILE B 1 13  ? 21.15652 21.68741 -2.26329  1.000 20.03779 ? 9   ILE B HG22 1 
ATOM   1941 H  HG23 . ILE B 1 13  ? 20.64462 22.38857 -3.59365  1.000 20.03779 ? 9   ILE B HG23 1 
ATOM   1942 H  HD11 . ILE B 1 13  ? 16.91102 19.77602 -3.28866  1.000 24.40488 ? 9   ILE B HD11 1 
ATOM   1943 H  HD12 . ILE B 1 13  ? 18.09934 19.25491 -2.37223  1.000 24.40488 ? 9   ILE B HD12 1 
ATOM   1944 H  HD13 . ILE B 1 13  ? 17.69321 20.79050 -2.34924  1.000 24.40488 ? 9   ILE B HD13 1 
ATOM   1945 N  N    . PHE B 1 14  ? 23.24519 19.53499 -3.62944  1.000 14.31150 ? 10  PHE B N    1 
ATOM   1946 C  CA   . PHE B 1 14  ? 24.62456 19.75914 -3.20859  1.000 13.81911 ? 10  PHE B CA   1 
ATOM   1947 C  C    . PHE B 1 14  ? 25.52661 20.01536 -4.41474  1.000 14.13951 ? 10  PHE B C    1 
ATOM   1948 O  O    . PHE B 1 14  ? 26.33339 20.95525 -4.42387  1.000 14.78863 ? 10  PHE B O    1 
ATOM   1949 C  CB   . PHE B 1 14  ? 25.17313 18.58867 -2.38662  1.000 14.45485 ? 10  PHE B CB   1 
ATOM   1950 C  CG   . PHE B 1 14  ? 26.58115 18.82492 -1.92333  1.000 14.92668 ? 10  PHE B CG   1 
ATOM   1951 C  CD1  . PHE B 1 14  ? 26.81386 19.50212 -0.73867  1.000 16.17688 ? 10  PHE B CD1  1 
ATOM   1952 C  CD2  . PHE B 1 14  ? 27.67547 18.44165 -2.68429  1.000 17.49317 ? 10  PHE B CD2  1 
ATOM   1953 C  CE1  . PHE B 1 14  ? 28.10307 19.77787 -0.31726  1.000 18.86589 ? 10  PHE B CE1  1 
ATOM   1954 C  CE2  . PHE B 1 14  ? 28.95441 18.71302 -2.25276  1.000 18.59214 ? 10  PHE B CE2  1 
ATOM   1955 C  CZ   . PHE B 1 14  ? 29.15851 19.38242 -1.07682  1.000 18.49801 ? 10  PHE B CZ   1 
ATOM   1956 H  H    . PHE B 1 14  ? 22.91276 18.77685 -3.39641  1.000 17.19853 ? 10  PHE B H    1 
ATOM   1957 H  HA   . PHE B 1 14  ? 24.62616 20.53866 -2.63130  1.000 16.60766 ? 10  PHE B HA   1 
ATOM   1958 H  HB2  . PHE B 1 14  ? 24.61499 18.46212 -1.60343  1.000 17.37055 ? 10  PHE B HB2  1 
ATOM   1959 H  HB3  . PHE B 1 14  ? 25.16558 17.78686 -2.93245  1.000 17.37055 ? 10  PHE B HB3  1 
ATOM   1960 H  HD1  . PHE B 1 14  ? 26.09334 19.77584 -0.21826  1.000 19.43699 ? 10  PHE B HD1  1 
ATOM   1961 H  HD2  . PHE B 1 14  ? 27.54452 17.99845 -3.49134  1.000 21.01653 ? 10  PHE B HD2  1 
ATOM   1962 H  HE1  . PHE B 1 14  ? 28.24645 20.23157 0.48180   1.000 22.66380 ? 10  PHE B HE1  1 
ATOM   1963 H  HE2  . PHE B 1 14  ? 29.68276 18.44021 -2.76265  1.000 22.33529 ? 10  PHE B HE2  1 
ATOM   1964 H  HZ   . PHE B 1 14  ? 30.02528 19.56802 -0.79546  1.000 22.22235 ? 10  PHE B HZ   1 
ATOM   1965 N  N    . VAL B 1 15  ? 25.42250 19.17054 -5.44599  1.000 14.89103 ? 11  VAL B N    1 
ATOM   1966 C  CA   . VAL B 1 15  ? 26.29784 19.31789 -6.59795  1.000 15.82142 ? 11  VAL B CA   1 
ATOM   1967 C  C    . VAL B 1 15  ? 26.06165 20.66553 -7.28204  1.000 15.36336 ? 11  VAL B C    1 
ATOM   1968 O  O    . VAL B 1 15  ? 27.01227 21.34705 -7.68225  1.000 16.15794 ? 11  VAL B O    1 
ATOM   1969 C  CB   . VAL B 1 15  ? 26.13173 18.10562 -7.53692  1.000 20.76756 ? 11  VAL B CB   1 
ATOM   1970 C  CG1  . VAL B 1 15  ? 26.75373 18.35717 -8.83082  1.000 25.39360 ? 11  VAL B CG1  1 
ATOM   1971 C  CG2  . VAL B 1 15  ? 26.72018 16.84103 -6.91055  1.000 23.39945 ? 11  VAL B CG2  1 
ATOM   1972 H  H    . VAL B 1 15  ? 24.86406 18.51866 -5.49888  1.000 17.89396 ? 11  VAL B H    1 
ATOM   1973 H  HA   . VAL B 1 15  ? 27.22301 19.32290 -6.30653  1.000 19.01043 ? 11  VAL B HA   1 
ATOM   1974 H  HB   . VAL B 1 15  ? 25.18222 17.96437 -7.67611  1.000 24.94580 ? 11  VAL B HB   1 
ATOM   1975 H  HG11 . VAL B 1 15  ? 26.92344 17.50903 -9.26986  1.000 30.49705 ? 11  VAL B HG11 1 
ATOM   1976 H  HG12 . VAL B 1 15  ? 26.15335 18.89478 -9.37065  1.000 30.49705 ? 11  VAL B HG12 1 
ATOM   1977 H  HG13 . VAL B 1 15  ? 27.58871 18.83121 -8.69301  1.000 30.49705 ? 11  VAL B HG13 1 
ATOM   1978 H  HG21 . VAL B 1 15  ? 26.51969 16.08304 -7.48165  1.000 28.10407 ? 11  VAL B HG21 1 
ATOM   1979 H  HG22 . VAL B 1 15  ? 27.68072 16.94746 -6.82719  1.000 28.10407 ? 11  VAL B HG22 1 
ATOM   1980 H  HG23 . VAL B 1 15  ? 26.32476 16.70902 -6.03470  1.000 28.10407 ? 11  VAL B HG23 1 
ATOM   1981 N  N    . GLN B 1 16  ? 24.78984 21.06881 -7.43075  1.000 15.23822 ? 12  GLN B N    1 
ATOM   1982 C  CA   . GLN B 1 16  ? 24.46760 22.29428 -8.15813  1.000 15.78187 ? 12  GLN B CA   1 
ATOM   1983 C  C    . GLN B 1 16  ? 24.65070 23.57467 -7.35201  1.000 15.28319 ? 12  GLN B C    1 
ATOM   1984 O  O    . GLN B 1 16  ? 24.82810 24.63766 -7.95734  1.000 15.69888 ? 12  GLN B O    1 
ATOM   1985 C  CB   . GLN B 1 16  ? 23.02489 22.25951 -8.65854  1.000 16.75764 ? 12  GLN B CB   1 
ATOM   1986 C  CG   . GLN B 1 16  ? 22.75689 21.21609 -9.71894  1.000 18.07425 ? 12  GLN B CG   1 
ATOM   1987 C  CD   . GLN B 1 16  ? 21.40971 21.37734 -10.38831 1.000 20.98932 ? 12  GLN B CD   1 
ATOM   1988 O  OE1  . GLN B 1 16  ? 20.54335 22.11881 -9.92726  1.000 23.44856 ? 12  GLN B OE1  1 
ATOM   1989 N  NE2  . GLN B 1 16  ? 21.23823 20.69199 -11.48649 1.000 21.02307 ? 12  GLN B NE2  1 
ATOM   1990 H  H    . GLN B 1 16  ? 24.10483 20.65115 -7.12104  1.000 18.31059 ? 12  GLN B H    1 
ATOM   1991 H  HA   . GLN B 1 16  ? 25.07226 22.32916 -8.91581  1.000 18.96297 ? 12  GLN B HA   1 
ATOM   1992 H  HB2  . GLN B 1 16  ? 22.44130 22.07080 -7.90707  1.000 20.13389 ? 12  GLN B HB2  1 
ATOM   1993 H  HB3  . GLN B 1 16  ? 22.80803 23.12561 -9.03768  1.000 20.13389 ? 12  GLN B HB3  1 
ATOM   1994 H  HG2  . GLN B 1 16  ? 23.43993 21.28214 -10.40449 1.000 21.71383 ? 12  GLN B HG2  1 
ATOM   1995 H  HG3  . GLN B 1 16  ? 22.78242 20.33745 -9.30875  1.000 21.71383 ? 12  GLN B HG3  1 
ATOM   1996 H  HE21 . GLN B 1 16  ? 21.87053 20.19042 -11.78350 1.000 25.25241 ? 12  GLN B HE21 1 
ATOM   1997 H  HE22 . GLN B 1 16  ? 20.49298 20.74220 -11.91274 1.000 25.25241 ? 12  GLN B HE22 1 
ATOM   1998 N  N    . ARG B 1 17  ? 24.60912 23.51357 -6.00937  1.000 14.83309 ? 13  ARG B N    1 
ATOM   1999 C  CA   . ARG B 1 17  ? 24.65334 24.71043 -5.18286  1.000 14.53458 ? 13  ARG B CA   1 
ATOM   2000 C  C    . ARG B 1 17  ? 25.85784 24.81513 -4.27088  1.000 15.64948 ? 13  ARG B C    1 
ATOM   2001 O  O    . ARG B 1 17  ? 26.19751 25.93837 -3.89025  1.000 17.18871 ? 13  ARG B O    1 
ATOM   2002 C  CB   . ARG B 1 17  ? 23.38900 24.82306 -4.31153  1.000 15.84201 ? 13  ARG B CB   1 
ATOM   2003 C  CG   . ARG B 1 17  ? 22.09372 24.82713 -5.09339  1.000 17.64277 ? 13  ARG B CG   1 
ATOM   2004 C  CD   . ARG B 1 17  ? 21.99529 26.00674 -6.05470  1.000 21.49288 ? 13  ARG B CD   1 
ATOM   2005 N  NE   . ARG B 1 17  ? 22.01263 27.30352 -5.36735  1.000 23.90452 ? 13  ARG B NE   1 
ATOM   2006 C  CZ   . ARG B 1 17  ? 20.93690 27.92653 -4.88290  1.000 28.51075 ? 13  ARG B CZ   1 
ATOM   2007 N  NH1  . ARG B 1 17  ? 19.72333 27.39664 -4.98469  1.000 29.56426 ? 13  ARG B NH1  1 
ATOM   2008 N  NH2  . ARG B 1 17  ? 21.07176 29.10497 -4.28830  1.000 31.41869 ? 13  ARG B NH2  1 
ATOM   2009 H  H    . ARG B 1 17  ? 24.55500 22.78139 -5.56151  1.000 17.82443 ? 13  ARG B H    1 
ATOM   2010 H  HA   . ARG B 1 17  ? 24.67709 25.47176 -5.78346  1.000 17.46622 ? 13  ARG B HA   1 
ATOM   2011 H  HB2  . ARG B 1 17  ? 23.36321 24.06750 -3.70377  1.000 19.03514 ? 13  ARG B HB2  1 
ATOM   2012 H  HB3  . ARG B 1 17  ? 23.43175 25.65168 -3.80908  1.000 19.03514 ? 13  ARG B HB3  1 
ATOM   2013 H  HG2  . ARG B 1 17  ? 22.03410 24.01023 -5.61303  1.000 21.19605 ? 13  ARG B HG2  1 
ATOM   2014 H  HG3  . ARG B 1 17  ? 21.34925 24.88136 -4.47393  1.000 21.19605 ? 13  ARG B HG3  1 
ATOM   2015 H  HD2  . ARG B 1 17  ? 22.74887 25.98101 -6.66489  1.000 25.81619 ? 13  ARG B HD2  1 
ATOM   2016 H  HD3  . ARG B 1 17  ? 21.16430 25.94175 -6.55083  1.000 25.81619 ? 13  ARG B HD3  1 
ATOM   2017 H  HE   . ARG B 1 17  ? 22.77404 27.69118 -5.26945  1.000 28.71015 ? 13  ARG B HE   1 
ATOM   2018 H  HH11 . ARG B 1 17  ? 19.61760 26.63500 -5.36983  1.000 35.50183 ? 13  ARG B HH11 1 
ATOM   2019 H  HH12 . ARG B 1 17  ? 19.04323 27.81515 -4.66546  1.000 35.50183 ? 13  ARG B HH12 1 
ATOM   2020 H  HH21 . ARG B 1 17  ? 21.85000 29.46384 -4.21653  1.000 37.72716 ? 13  ARG B HH21 1 
ATOM   2021 H  HH22 . ARG B 1 17  ? 20.38092 29.50991 -3.97466  1.000 37.72716 ? 13  ARG B HH22 1 
ATOM   2022 N  N    . CYS B 1 18  ? 26.51281 23.71632 -3.93228  1.000 14.78972 ? 14  CYS B N    1 
ATOM   2023 C  CA   . CYS B 1 18  ? 27.53898 23.73103 -2.88492  1.000 15.16491 ? 14  CYS B CA   1 
ATOM   2024 C  C    . CYS B 1 18  ? 28.88737 23.21713 -3.34922  1.000 14.96074 ? 14  CYS B C    1 
ATOM   2025 O  O    . CYS B 1 18  ? 29.92231 23.69789 -2.86673  1.000 16.39708 ? 14  CYS B O    1 
ATOM   2026 C  CB   . CYS B 1 18  ? 27.08260 22.85813 -1.69577  1.000 14.64959 ? 14  CYS B CB   1 
ATOM   2027 S  SG   . CYS B 1 18  ? 25.37685 23.07081 -1.14015  1.000 14.62673 ? 14  CYS B SG   1 
ATOM   2028 H  H    . CYS B 1 18  ? 26.38423 22.94596 -4.29231  1.000 17.77240 ? 14  CYS B H    1 
ATOM   2029 H  HA   . CYS B 1 18  ? 27.65046 24.64696 -2.58567  1.000 18.22262 ? 14  CYS B HA   1 
ATOM   2030 H  HB2  . CYS B 1 18  ? 27.18404 21.92758 -1.95010  1.000 17.60424 ? 14  CYS B HB2  1 
ATOM   2031 H  HB3  . CYS B 1 18  ? 27.65462 23.05939 -0.93868  1.000 17.60424 ? 14  CYS B HB3  1 
ATOM   2032 N  N    . ALA B 1 19  ? 28.90755 22.20846 -4.22417  1.000 16.11898 ? 15  ALA B N    1 
ATOM   2033 C  CA   . ALA B 1 19  ? 30.13758 21.52069 -4.59363  1.000 16.79808 ? 15  ALA B CA   1 
ATOM   2034 C  C    . ALA B 1 19  ? 31.17987 22.43062 -5.22198  1.000 15.48472 ? 15  ALA B C    1 
ATOM   2035 O  O    . ALA B 1 19  ? 32.37319 22.13261 -5.10470  1.000 17.42590 ? 15  ALA B O    1 
ATOM   2036 C  CB   . ALA B 1 19  ? 29.82880 20.36439 -5.53478  1.000 17.25424 ? 15  ALA B CB   1 
ATOM   2037 H  H    . ALA B 1 19  ? 28.21121 21.89957 -4.62330  1.000 19.36751 ? 15  ALA B H    1 
ATOM   2038 H  HA   . ALA B 1 19  ? 30.52751 21.16219 -3.78102  1.000 20.18242 ? 15  ALA B HA   1 
ATOM   2039 H  HB1  . ALA B 1 19  ? 30.66160 19.94994 -5.80970  1.000 20.72982 ? 15  ALA B HB1  1 
ATOM   2040 H  HB2  . ALA B 1 19  ? 29.27528 19.71776 -5.06961  1.000 20.72982 ? 15  ALA B HB2  1 
ATOM   2041 H  HB3  . ALA B 1 19  ? 29.35739 20.70597 -6.31067  1.000 20.72982 ? 15  ALA B HB3  1 
ATOM   2042 N  N    . GLN B 1 20  ? 30.78158 23.55573 -5.81723  1.000 16.85743 ? 16  GLN B N    1 
ATOM   2043 C  CA   . GLN B 1 20  ? 31.78891 24.44678 -6.37969  1.000 18.31820 ? 16  GLN B CA   1 
ATOM   2044 C  C    . GLN B 1 20  ? 32.75128 24.95437 -5.31443  1.000 18.62611 ? 16  GLN B C    1 
ATOM   2045 O  O    . GLN B 1 20  ? 33.92190 25.22753 -5.62071  1.000 21.12009 ? 16  GLN B O    1 
ATOM   2046 C  CB   . GLN B 1 20  ? 31.15228 25.61272 -7.12218  1.000 24.30414 ? 16  GLN B CB   1 
ATOM   2047 C  CG   . GLN B 1 20  ? 30.29820 26.55510 -6.30468  1.000 26.75490 ? 16  GLN B CG   1 
ATOM   2048 C  CD   . GLN B 1 20  ? 30.42421 27.99671 -6.76707  1.000 32.29582 ? 16  GLN B CD   1 
ATOM   2049 O  OE1  . GLN B 1 20  ? 31.50707 28.46881 -7.12733  1.000 36.26051 ? 16  GLN B OE1  1 
ATOM   2050 N  NE2  . GLN B 1 20  ? 29.31342 28.70317 -6.75378  1.000 30.85776 ? 16  GLN B NE2  1 
ATOM   2051 H  H    . GLN B 1 20  ? 29.96676 23.81632 -5.90537  1.000 20.25365 ? 16  GLN B H    1 
ATOM   2052 H  HA   . GLN B 1 20  ? 32.29736 23.94117 -7.03294  1.000 22.00657 ? 16  GLN B HA   1 
ATOM   2053 H  HB2  . GLN B 1 20  ? 31.86350 26.14305 -7.51437  1.000 29.18969 ? 16  GLN B HB2  1 
ATOM   2054 H  HB3  . GLN B 1 20  ? 30.58513 25.25006 -7.82055  1.000 29.18969 ? 16  GLN B HB3  1 
ATOM   2055 H  HG2  . GLN B 1 20  ? 29.36801 26.29236 -6.38604  1.000 32.13061 ? 16  GLN B HG2  1 
ATOM   2056 H  HG3  . GLN B 1 20  ? 30.57549 26.51070 -5.37622  1.000 32.13061 ? 16  GLN B HG3  1 
ATOM   2057 H  HE21 . GLN B 1 20  ? 28.57735 28.34225 -6.49389  1.000 37.05403 ? 16  GLN B HE21 1 
ATOM   2058 H  HE22 . GLN B 1 20  ? 29.32385 29.52560 -7.00500  1.000 37.05403 ? 16  GLN B HE22 1 
ATOM   2059 N  N    . CYS B 1 21  ? 32.29381 25.06120 -4.05305  1.000 17.65165 ? 17  CYS B N    1 
ATOM   2060 C  CA   . CYS B 1 21  ? 33.11140 25.58359 -2.96129  1.000 18.98788 ? 17  CYS B CA   1 
ATOM   2061 C  C    . CYS B 1 21  ? 33.42049 24.58024 -1.85874  1.000 18.14702 ? 17  CYS B C    1 
ATOM   2062 O  O    . CYS B 1 21  ? 34.26788 24.88049 -1.00616  1.000 19.26341 ? 17  CYS B O    1 
ATOM   2063 C  CB   . CYS B 1 21  ? 32.42593 26.80184 -2.34174  1.000 19.88282 ? 17  CYS B CB   1 
ATOM   2064 S  SG   . CYS B 1 21  ? 32.23650 28.18393 -3.49502  1.000 20.53237 ? 17  CYS B SG   1 
ATOM   2065 H  H    . CYS B 1 21  ? 31.50126 24.83222 -3.81008  1.000 21.20671 ? 17  CYS B H    1 
ATOM   2066 H  HA   . CYS B 1 21  ? 33.96457 25.86174 -3.32957  1.000 22.81018 ? 17  CYS B HA   1 
ATOM   2067 H  HB2  . CYS B 1 21  ? 31.54139 26.54318 -2.03911  1.000 23.88411 ? 17  CYS B HB2  1 
ATOM   2068 H  HB3  . CYS B 1 21  ? 32.95621 27.11123 -1.59075  1.000 23.88411 ? 17  CYS B HB3  1 
ATOM   2069 N  N    . HIS B 1 22  ? 32.78697 23.40600 -1.84835  1.000 17.51004 ? 18  HIS B N    1 
ATOM   2070 C  CA   . HIS B 1 22  ? 32.90290 22.47080 -0.74267  1.000 16.34310 ? 18  HIS B CA   1 
ATOM   2071 C  C    . HIS B 1 22  ? 33.03538 21.03093 -1.20777  1.000 17.79773 ? 18  HIS B C    1 
ATOM   2072 O  O    . HIS B 1 22  ? 32.35543 20.60400 -2.14779  1.000 18.85841 ? 18  HIS B O    1 
ATOM   2073 C  CB   . HIS B 1 22  ? 31.64951 22.48679 0.15472   1.000 15.75103 ? 18  HIS B CB   1 
ATOM   2074 C  CG   . HIS B 1 22  ? 31.43611 23.74288 0.94895   1.000 15.36137 ? 18  HIS B CG   1 
ATOM   2075 N  ND1  . HIS B 1 22  ? 32.15397 24.04841 2.09331   1.000 15.99996 ? 18  HIS B ND1  1 
ATOM   2076 C  CD2  . HIS B 1 22  ? 30.55328 24.75116 0.78420   1.000 15.51312 ? 18  HIS B CD2  1 
ATOM   2077 C  CE1  . HIS B 1 22  ? 31.69420 25.18348 2.59652   1.000 16.40013 ? 18  HIS B CE1  1 
ATOM   2078 N  NE2  . HIS B 1 22  ? 30.73344 25.63794 1.81415   1.000 15.36059 ? 18  HIS B NE2  1 
ATOM   2079 H  H    . HIS B 1 22  ? 32.27741 23.13002 -2.48380  1.000 21.03677 ? 18  HIS B H    1 
ATOM   2080 H  HA   . HIS B 1 22  ? 33.70449 22.73300 -0.26350  1.000 19.63645 ? 18  HIS B HA   1 
ATOM   2081 H  HB2  . HIS B 1 22  ? 30.86949 22.36644 -0.40917  1.000 18.92596 ? 18  HIS B HB2  1 
ATOM   2082 H  HB3  . HIS B 1 22  ? 31.71806 21.75431 0.78693   1.000 18.92596 ? 18  HIS B HB3  1 
ATOM   2083 H  HD1  . HIS B 1 22  ? 32.79376 23.57779 2.42312   1.000 19.22468 ? 18  HIS B HD1  1 
ATOM   2084 H  HD2  . HIS B 1 22  ? 29.93368 24.83000 0.09515   1.000 18.64047 ? 18  HIS B HD2  1 
ATOM   2085 H  HE1  . HIS B 1 22  ? 31.99843 25.59336 3.37391   1.000 19.70488 ? 18  HIS B HE1  1 
ATOM   2086 N  N    . THR B 1 23  ? 33.86559 20.26976 -0.49627  1.000 19.50154 ? 19  THR B N    1 
ATOM   2087 C  CA   . THR B 1 23  ? 33.88833 18.81885 -0.57052  1.000 20.21978 ? 19  THR B CA   1 
ATOM   2088 C  C    . THR B 1 23  ? 33.30576 18.23537 0.71497   1.000 21.22887 ? 19  THR B C    1 
ATOM   2089 O  O    . THR B 1 23  ? 33.22244 18.90767 1.75075   1.000 21.22007 ? 19  THR B O    1 
ATOM   2090 C  CB   . THR B 1 23  ? 35.31379 18.28809 -0.79514  1.000 21.45928 ? 19  THR B CB   1 
ATOM   2091 O  OG1  . THR B 1 23  ? 36.13695 18.65814 0.31548   1.000 23.03780 ? 19  THR B OG1  1 
ATOM   2092 C  CG2  . THR B 1 23  ? 35.92439 18.85080 -2.06818  1.000 24.42477 ? 19  THR B CG2  1 
ATOM   2093 H  H    . THR B 1 23  ? 34.44364 20.58883 0.05478   1.000 23.42658 ? 19  THR B H    1 
ATOM   2094 H  HA   . THR B 1 23  ? 33.34828 18.52390 -1.32035  1.000 24.28847 ? 19  THR B HA   1 
ATOM   2095 H  HB   . THR B 1 23  ? 35.27861 17.32262 -0.88181  1.000 25.77587 ? 19  THR B HB   1 
ATOM   2096 H  HG1  . THR B 1 23  ? 36.08359 19.48566 0.44951   1.000 27.67008 ? 19  THR B HG1  1 
ATOM   2097 H  HG21 . THR B 1 23  ? 36.79130 18.44584 -2.22746  1.000 29.33446 ? 19  THR B HG21 1 
ATOM   2098 H  HG22 . THR B 1 23  ? 35.34604 18.66412 -2.82419  1.000 29.33446 ? 19  THR B HG22 1 
ATOM   2099 H  HG23 . THR B 1 23  ? 36.03567 19.81093 -1.98650  1.000 29.33446 ? 19  THR B HG23 1 
ATOM   2100 N  N    . VAL B 1 24  ? 32.89973 16.96664 0.62628   1.000 23.09436 ? 20  VAL B N    1 
ATOM   2101 C  CA   . VAL B 1 24  ? 32.25010 16.26925 1.73319   1.000 24.44925 ? 20  VAL B CA   1 
ATOM   2102 C  C    . VAL B 1 24  ? 33.05722 15.09976 2.26695   1.000 25.99207 ? 20  VAL B C    1 
ATOM   2103 O  O    . VAL B 1 24  ? 32.80643 14.67545 3.40960   1.000 24.73771 ? 20  VAL B O    1 
ATOM   2104 C  CB   . VAL B 1 24  ? 30.82780 15.78843 1.36863   1.000 24.13989 ? 20  VAL B CB   1 
ATOM   2105 C  CG1  . VAL B 1 24  ? 29.89134 16.95733 1.17937   1.000 23.30347 ? 20  VAL B CG1  1 
ATOM   2106 C  CG2  . VAL B 1 24  ? 30.83938 14.90727 0.12165   1.000 27.15483 ? 20  VAL B CG2  1 
ATOM   2107 H  H    . VAL B 1 24  ? 32.99155 16.48110 -0.07758  1.000 27.73796 ? 20  VAL B H    1 
ATOM   2108 H  HA   . VAL B 1 24  ? 32.15902 16.91221 2.45374   1.000 29.36383 ? 20  VAL B HA   1 
ATOM   2109 H  HB   . VAL B 1 24  ? 30.49837 15.25305 2.10737   1.000 28.99259 ? 20  VAL B HB   1 
ATOM   2110 H  HG11 . VAL B 1 24  ? 29.22746 16.72517 0.51133   1.000 27.98890 ? 20  VAL B HG11 1 
ATOM   2111 H  HG12 . VAL B 1 24  ? 29.45629 17.15339 2.02387   1.000 27.98890 ? 20  VAL B HG12 1 
ATOM   2112 H  HG13 . VAL B 1 24  ? 30.40258 17.72698 0.88412   1.000 27.98890 ? 20  VAL B HG13 1 
ATOM   2113 H  HG21 . VAL B 1 24  ? 29.93850 14.59139 -0.05020  1.000 32.61052 ? 20  VAL B HG21 1 
ATOM   2114 H  HG22 . VAL B 1 24  ? 31.15590 15.43011 -0.63158  1.000 32.61052 ? 20  VAL B HG22 1 
ATOM   2115 H  HG23 . VAL B 1 24  ? 31.43093 14.15357 0.27303   1.000 32.61052 ? 20  VAL B HG23 1 
ATOM   2116 N  N    . GLU B 1 25  ? 33.97552 14.54029 1.48246   1.000 29.18217 ? 21  GLU B N    1 
ATOM   2117 C  CA   . GLU B 1 25  ? 34.62393 13.29034 1.83370   1.000 33.25702 ? 21  GLU B CA   1 
ATOM   2118 C  C    . GLU B 1 25  ? 35.73231 13.51615 2.85867   1.000 34.24793 ? 21  GLU B C    1 
ATOM   2119 O  O    . GLU B 1 25  ? 36.30165 14.60627 2.97588   1.000 33.36025 ? 21  GLU B O    1 
ATOM   2120 C  CB   . GLU B 1 25  ? 35.16585 12.58671 0.57472   1.000 36.60037 ? 21  GLU B CB   1 
ATOM   2121 C  CG   . GLU B 1 25  ? 36.42766 13.18631 -0.11228  1.000 39.32942 ? 21  GLU B CG   1 
ATOM   2122 C  CD   . GLU B 1 25  ? 36.14167 14.34822 -1.06127  1.000 43.26062 ? 21  GLU B CD   1 
ATOM   2123 O  OE1  . GLU B 1 25  ? 35.00129 14.86398 -1.08116  1.000 44.05359 ? 21  GLU B OE1  1 
ATOM   2124 O  OE2  . GLU B 1 25  ? 37.07480 14.73608 -1.80725  1.000 45.60856 ? 21  GLU B OE2  1 
ATOM   2125 H  H    . GLU B 1 25  ? 34.24085 14.87115 0.73431   1.000 35.04334 ? 21  GLU B H    1 
ATOM   2126 H  HA   . GLU B 1 25  ? 33.97538 12.69572 2.24200   1.000 39.93315 ? 21  GLU B HA   1 
ATOM   2127 H  HB2  . GLU B 1 25  ? 35.38957 11.67511 0.81933   1.000 43.94517 ? 21  GLU B HB2  1 
ATOM   2128 H  HB3  . GLU B 1 25  ? 34.46024 12.58795 -0.09087  1.000 43.94517 ? 21  GLU B HB3  1 
ATOM   2129 H  HG2  . GLU B 1 25  ? 37.02892 13.51202 0.57569   1.000 47.22004 ? 21  GLU B HG2  1 
ATOM   2130 H  HG3  . GLU B 1 25  ? 36.86050 12.48776 -0.62761  1.000 47.22004 ? 21  GLU B HG3  1 
ATOM   2131 N  N    . ALA B 1 26  ? 36.04508 12.45443 3.59523   1.000 36.11333 ? 22  ALA B N    1 
ATOM   2132 C  CA   . ALA B 1 26  ? 37.17095 12.49546 4.51646   1.000 37.61985 ? 22  ALA B CA   1 
ATOM   2133 C  C    . ALA B 1 26  ? 38.45675 12.75888 3.74500   1.000 39.13737 ? 22  ALA B C    1 
ATOM   2134 O  O    . ALA B 1 26  ? 38.73836 12.10411 2.73625   1.000 41.87578 ? 22  ALA B O    1 
ATOM   2135 C  CB   . ALA B 1 26  ? 37.27665 11.16722 5.26142   1.000 37.42158 ? 22  ALA B CB   1 
ATOM   2136 H  H    . ALA B 1 26  ? 35.62473 11.70431 3.58038   1.000 43.36072 ? 22  ALA B H    1 
ATOM   2137 H  HA   . ALA B 1 26  ? 37.04052 13.20447 5.16546   1.000 45.16855 ? 22  ALA B HA   1 
ATOM   2138 H  HB1  . ALA B 1 26  ? 38.02357 11.20998 5.87882   1.000 44.93063 ? 22  ALA B HB1  1 
ATOM   2139 H  HB2  . ALA B 1 26  ? 36.45269 11.01232 5.74927   1.000 44.93063 ? 22  ALA B HB2  1 
ATOM   2140 H  HB3  . ALA B 1 26  ? 37.41928 10.45503 4.61850   1.000 44.93063 ? 22  ALA B HB3  1 
ATOM   2141 N  N    . GLY B 1 27  ? 39.23507 13.73120 4.21177   1.000 39.28936 ? 23  GLY B N    1 
ATOM   2142 C  CA   . GLY B 1 27  ? 40.43418 14.12011 3.49838   1.000 37.20755 ? 23  GLY B CA   1 
ATOM   2143 C  C    . GLY B 1 27  ? 40.18952 14.92519 2.24258   1.000 35.81673 ? 23  GLY B C    1 
ATOM   2144 O  O    . GLY B 1 27  ? 41.15165 15.23194 1.52550   1.000 37.78748 ? 23  GLY B O    1 
ATOM   2145 H  H    . GLY B 1 27  ? 39.08665 14.17386 4.93400   1.000 47.17196 ? 23  GLY B H    1 
ATOM   2146 H  HA2  . GLY B 1 27  ? 40.98845 14.65353 4.08927   1.000 44.67379 ? 23  GLY B HA2  1 
ATOM   2147 H  HA3  . GLY B 1 27  ? 40.92021 13.31915 3.24711   1.000 44.67379 ? 23  GLY B HA3  1 
ATOM   2148 N  N    . GLY B 1 28  ? 38.93619 15.26819 1.94491   1.000 32.82389 ? 24  GLY B N    1 
ATOM   2149 C  CA   . GLY B 1 28  ? 38.66875 16.11372 0.80396   1.000 32.43945 ? 24  GLY B CA   1 
ATOM   2150 C  C    . GLY B 1 28  ? 39.28082 17.48471 0.98994   1.000 28.34585 ? 24  GLY B C    1 
ATOM   2151 O  O    . GLY B 1 28  ? 39.42655 17.97816 2.10522   1.000 29.43010 ? 24  GLY B O    1 
ATOM   2152 H  H    . GLY B 1 28  ? 38.23731 15.02599 2.38365   1.000 39.41339 ? 24  GLY B H    1 
ATOM   2153 H  HA2  . GLY B 1 28  ? 39.04289 15.71148 0.00451   1.000 38.95207 ? 24  GLY B HA2  1 
ATOM   2154 H  HA3  . GLY B 1 28  ? 37.71080 16.21337 0.68868   1.000 38.95207 ? 24  GLY B HA3  1 
ATOM   2155 N  N    . LYS B 1 29  ? 39.62094 18.11646 -0.12252  1.000 28.65699 ? 25  LYS B N    1 
ATOM   2156 C  CA   . LYS B 1 29  ? 40.35854 19.35857 -0.03933  1.000 29.11890 ? 25  LYS B CA   1 
ATOM   2157 C  C    . LYS B 1 29  ? 39.45385 20.53119 0.33166   1.000 24.56349 ? 25  LYS B C    1 
ATOM   2158 O  O    . LYS B 1 29  ? 38.23836 20.54324 0.06938   1.000 24.75784 ? 25  LYS B O    1 
ATOM   2159 C  CB   . LYS B 1 29  ? 41.10910 19.63096 -1.34072  1.000 33.56991 ? 25  LYS B CB   1 
ATOM   2160 C  CG   . LYS B 1 29  ? 40.24316 19.84179 -2.54651  1.000 39.07536 ? 25  LYS B CG   1 
ATOM   2161 C  CD   . LYS B 1 29  ? 41.11379 20.01111 -3.78277  1.000 42.77333 ? 25  LYS B CD   1 
ATOM   2162 C  CE   . LYS B 1 29  ? 40.27395 20.26818 -5.02098  1.000 45.86973 ? 25  LYS B CE   1 
ATOM   2163 N  NZ   . LYS B 1 29  ? 41.10750 20.59725 -6.20679  1.000 49.05167 ? 25  LYS B NZ   1 
ATOM   2164 H  H    . LYS B 1 29  ? 39.43919 17.85019 -0.91981  1.000 34.41311 ? 25  LYS B H    1 
ATOM   2165 H  HA   . LYS B 1 29  ? 41.01920 19.28540 0.66712   1.000 34.96741 ? 25  LYS B HA   1 
ATOM   2166 H  HB2  . LYS B 1 29  ? 41.64324 20.43219 -1.22393  1.000 40.30862 ? 25  LYS B HB2  1 
ATOM   2167 H  HB3  . LYS B 1 29  ? 41.68475 18.87264 -1.52642  1.000 40.30862 ? 25  LYS B HB3  1 
ATOM   2168 H  HG2  . LYS B 1 29  ? 39.66614 19.07262 -2.67422  1.000 46.91516 ? 25  LYS B HG2  1 
ATOM   2169 H  HG3  . LYS B 1 29  ? 39.70795 20.64231 -2.42979  1.000 46.91516 ? 25  LYS B HG3  1 
ATOM   2170 H  HD2  . LYS B 1 29  ? 41.70941 20.76610 -3.65578  1.000 51.35272 ? 25  LYS B HD2  1 
ATOM   2171 H  HD3  . LYS B 1 29  ? 41.62948 19.20218 -3.92626  1.000 51.35272 ? 25  LYS B HD3  1 
ATOM   2172 H  HE2  . LYS B 1 29  ? 39.75742 19.47318 -5.22609  1.000 55.06840 ? 25  LYS B HE2  1 
ATOM   2173 H  HE3  . LYS B 1 29  ? 39.67936 21.01591 -4.85284  1.000 55.06840 ? 25  LYS B HE3  1 
ATOM   2174 H  HZ1  . LYS B 1 29  ? 40.58687 20.74458 -6.91343  1.000 58.88674 ? 25  LYS B HZ1  1 
ATOM   2175 H  HZ2  . LYS B 1 29  ? 41.59019 21.32758 -6.04637  1.000 58.88674 ? 25  LYS B HZ2  1 
ATOM   2176 H  HZ3  . LYS B 1 29  ? 41.65758 19.92177 -6.38912  1.000 58.88674 ? 25  LYS B HZ3  1 
ATOM   2177 N  N    . HIS B 1 30  ? 40.05813 21.51823 0.96759   1.000 24.04794 ? 26  HIS B N    1 
ATOM   2178 C  CA   . HIS B 1 30  ? 39.43885 22.82139 1.07214   1.000 22.31031 ? 26  HIS B CA   1 
ATOM   2179 C  C    . HIS B 1 30  ? 39.50318 23.48240 -0.29174  1.000 22.81639 ? 26  HIS B C    1 
ATOM   2180 O  O    . HIS B 1 30  ? 40.46100 23.28873 -1.04452  1.000 24.64538 ? 26  HIS B O    1 
ATOM   2181 C  CB   . HIS B 1 30  ? 40.18209 23.68722 2.08830   1.000 22.05967 ? 26  HIS B CB   1 
ATOM   2182 C  CG   . HIS B 1 30  ? 40.28969 23.07638 3.45274   1.000 21.45036 ? 26  HIS B CG   1 
ATOM   2183 N  ND1  . HIS B 1 30  ? 39.20517 22.54446 4.11269   1.000 21.88735 ? 26  HIS B ND1  1 
ATOM   2184 C  CD2  . HIS B 1 30  ? 41.34319 22.94545 4.29579   1.000 22.96896 ? 26  HIS B CD2  1 
ATOM   2185 C  CE1  . HIS B 1 30  ? 39.58276 22.09077 5.29224   1.000 21.62711 ? 26  HIS B CE1  1 
ATOM   2186 N  NE2  . HIS B 1 30  ? 40.88016 22.31737 5.42632   1.000 21.42397 ? 26  HIS B NE2  1 
ATOM   2187 H  H    . HIS B 1 30  ? 40.82745 21.45955 1.34746   1.000 28.88226 ? 26  HIS B H    1 
ATOM   2188 H  HA   . HIS B 1 30  ? 38.51890 22.73981 1.36867   1.000 26.79710 ? 26  HIS B HA   1 
ATOM   2189 H  HB2  . HIS B 1 30  ? 41.08281 23.84269 1.76360   1.000 26.49634 ? 26  HIS B HB2  1 
ATOM   2190 H  HB3  . HIS B 1 30  ? 39.71216 24.53084 2.17976   1.000 26.49634 ? 26  HIS B HB3  1 
ATOM   2191 H  HD2  . HIS B 1 30  ? 42.21523 23.22772 4.13839   1.000 27.58748 ? 26  HIS B HD2  1 
ATOM   2192 H  HE1  . HIS B 1 30  ? 39.03265 21.68229 5.92106   1.000 25.97726 ? 26  HIS B HE1  1 
ATOM   2193 H  HE2  . HIS B 1 30  ? 41.35614 22.10559 6.11057   1.000 25.73349 ? 26  HIS B HE2  1 
ATOM   2194 N  N    . LYS B 1 31  ? 38.46152 24.22570 -0.62644  1.000 23.06596 ? 27  LYS B N    1 
ATOM   2195 C  CA   . LYS B 1 31  ? 38.40596 25.00973 -1.84591  1.000 23.81509 ? 27  LYS B CA   1 
ATOM   2196 C  C    . LYS B 1 31  ? 38.15121 26.44178 -1.39447  1.000 22.80696 ? 27  LYS B C    1 
ATOM   2197 O  O    . LYS B 1 31  ? 38.79694 26.89554 -0.43849  1.000 25.06410 ? 27  LYS B O    1 
ATOM   2198 C  CB   . LYS B 1 31  ? 37.34865 24.41412 -2.77787  1.000 26.51268 ? 27  LYS B CB   1 
ATOM   2199 C  CG   . LYS B 1 31  ? 37.53016 22.89846 -2.92132  1.000 28.13388 ? 27  LYS B CG   1 
ATOM   2200 C  CD   . LYS B 1 31  ? 37.05621 22.34834 -4.24870  1.000 34.43872 ? 27  LYS B CD   1 
ATOM   2201 C  CE   . LYS B 1 31  ? 35.57241 22.42054 -4.38353  1.000 33.93561 ? 27  LYS B CE   1 
ATOM   2202 N  NZ   . LYS B 1 31  ? 35.07719 21.56009 -5.52023  1.000 32.70891 ? 27  LYS B NZ   1 
ATOM   2203 H  H    . LYS B 1 31  ? 37.75030 24.29523 -0.14796  1.000 27.70388 ? 27  LYS B H    1 
ATOM   2204 H  HA   . LYS B 1 31  ? 39.21509 25.00404 -2.38085  1.000 28.60284 ? 27  LYS B HA   1 
ATOM   2205 H  HB2  . LYS B 1 31  ? 36.46580 24.58489 -2.41411  1.000 31.83994 ? 27  LYS B HB2  1 
ATOM   2206 H  HB3  . LYS B 1 31  ? 37.42938 24.81784 -3.65616  1.000 31.83994 ? 27  LYS B HB3  1 
ATOM   2207 H  HG2  . LYS B 1 31  ? 38.47288 22.68722 -2.83431  1.000 33.78539 ? 27  LYS B HG2  1 
ATOM   2208 H  HG3  . LYS B 1 31  ? 37.02502 22.45583 -2.22145  1.000 33.78539 ? 27  LYS B HG3  1 
ATOM   2209 H  HD2  . LYS B 1 31  ? 37.45143 22.86492 -4.96832  1.000 41.35119 ? 27  LYS B HD2  1 
ATOM   2210 H  HD3  . LYS B 1 31  ? 37.32239 21.41852 -4.32281  1.000 41.35119 ? 27  LYS B HD3  1 
ATOM   2211 H  HE2  . LYS B 1 31  ? 35.15993 22.10865 -3.56287  1.000 40.74746 ? 27  LYS B HE2  1 
ATOM   2212 H  HE3  . LYS B 1 31  ? 35.31024 23.33784 -4.55882  1.000 40.74746 ? 27  LYS B HE3  1 
ATOM   2213 H  HZ1  . LYS B 1 31  ? 34.19917 21.66492 -5.62121  1.000 39.27542 ? 27  LYS B HZ1  1 
ATOM   2214 H  HZ2  . LYS B 1 31  ? 35.48461 21.79136 -6.27695  1.000 39.27542 ? 27  LYS B HZ2  1 
ATOM   2215 H  HZ3  . LYS B 1 31  ? 35.24813 20.70335 -5.35032  1.000 39.27542 ? 27  LYS B HZ3  1 
ATOM   2216 N  N    . VAL B 1 32  ? 37.24184 27.17332 -2.02972  1.000 22.52616 ? 28  VAL B N    1 
ATOM   2217 C  CA   . VAL B 1 32  ? 36.88298 28.47424 -1.48265  1.000 22.11357 ? 28  VAL B CA   1 
ATOM   2218 C  C    . VAL B 1 32  ? 36.31366 28.30017 -0.07645  1.000 20.20784 ? 28  VAL B C    1 
ATOM   2219 O  O    . VAL B 1 32  ? 36.60455 29.09132 0.83217   1.000 21.05370 ? 28  VAL B O    1 
ATOM   2220 C  CB   . VAL B 1 32  ? 35.93250 29.22718 -2.43433  1.000 23.73521 ? 28  VAL B CB   1 
ATOM   2221 C  CG1  . VAL B 1 32  ? 35.35294 30.45621 -1.74791  1.000 24.94160 ? 28  VAL B CG1  1 
ATOM   2222 C  CG2  . VAL B 1 32  ? 36.66832 29.63616 -3.71550  1.000 27.34450 ? 28  VAL B CG2  1 
ATOM   2223 H  H    . VAL B 1 32  ? 36.83232 26.94928 -2.75201  1.000 27.05612 ? 28  VAL B H    1 
ATOM   2224 H  HA   . VAL B 1 32  ? 37.68032 29.02180 -1.40955  1.000 26.56101 ? 28  VAL B HA   1 
ATOM   2225 H  HB   . VAL B 1 32  ? 35.20175 28.63628 -2.67461  1.000 28.50698 ? 28  VAL B HB   1 
ATOM   2226 H  HG11 . VAL B 1 32  ? 35.04569 31.08015 -2.42408  1.000 29.95465 ? 28  VAL B HG11 1 
ATOM   2227 H  HG12 . VAL B 1 32  ? 34.60985 30.18377 -1.18713  1.000 29.95465 ? 28  VAL B HG12 1 
ATOM   2228 H  HG13 . VAL B 1 32  ? 36.04262 30.86958 -1.20535  1.000 29.95465 ? 28  VAL B HG13 1 
ATOM   2229 H  HG21 . VAL B 1 32  ? 36.02709 30.00129 -4.34510  1.000 32.83813 ? 28  VAL B HG21 1 
ATOM   2230 H  HG22 . VAL B 1 32  ? 37.33511 30.30579 -3.49665  1.000 32.83813 ? 28  VAL B HG22 1 
ATOM   2231 H  HG23 . VAL B 1 32  ? 37.09751 28.85416 -4.09651  1.000 32.83813 ? 28  VAL B HG23 1 
ATOM   2232 N  N    . GLY B 1 33  ? 35.55240 27.22091 0.14036   1.000 18.94059 ? 29  GLY B N    1 
ATOM   2233 C  CA   . GLY B 1 33  ? 35.03984 26.87960 1.44952   1.000 18.38865 ? 29  GLY B CA   1 
ATOM   2234 C  C    . GLY B 1 33  ? 35.69174 25.62829 2.02270   1.000 17.17052 ? 29  GLY B C    1 
ATOM   2235 O  O    . GLY B 1 33  ? 36.39791 24.87785 1.32970   1.000 19.10411 ? 29  GLY B O    1 
ATOM   2236 H  H    . GLY B 1 33  ? 35.32014 26.66608 -0.47432  1.000 22.75344 ? 29  GLY B H    1 
ATOM   2237 H  HA2  . GLY B 1 33  ? 35.20332 27.61565 2.05976   1.000 22.09111 ? 29  GLY B HA2  1 
ATOM   2238 H  HA3  . GLY B 1 33  ? 34.08404 26.72549 1.38947   1.000 22.09111 ? 29  GLY B HA3  1 
ATOM   2239 N  N    . PRO B 1 34  ? 35.45016 25.38203 3.31440   1.000 18.07269 ? 30  PRO B N    1 
ATOM   2240 C  CA   . PRO B 1 34  ? 36.06938 24.24028 3.99345   1.000 18.45800 ? 30  PRO B CA   1 
ATOM   2241 C  C    . PRO B 1 34  ? 35.43580 22.91566 3.62809   1.000 19.95731 ? 30  PRO B C    1 
ATOM   2242 O  O    . PRO B 1 34  ? 34.22929 22.81967 3.37936   1.000 20.36774 ? 30  PRO B O    1 
ATOM   2243 C  CB   . PRO B 1 34  ? 35.80352 24.52754 5.47869   1.000 18.25212 ? 30  PRO B CB   1 
ATOM   2244 C  CG   . PRO B 1 34  ? 34.53662 25.33421 5.47413   1.000 19.05473 ? 30  PRO B CG   1 
ATOM   2245 C  CD   . PRO B 1 34  ? 34.70279 26.22127 4.26554   1.000 18.66464 ? 30  PRO B CD   1 
ATOM   2246 H  HA   . PRO B 1 34  ? 37.01913 24.22263 3.79708   1.000 22.17433 ? 30  PRO B HA   1 
ATOM   2247 H  HB2  . PRO B 1 34  ? 35.68756 23.69572 5.96401   1.000 21.92727 ? 30  PRO B HB2  1 
ATOM   2248 H  HB3  . PRO B 1 34  ? 36.53945 25.03304 5.85786   1.000 21.92727 ? 30  PRO B HB3  1 
ATOM   2249 H  HG2  . PRO B 1 34  ? 33.76545 24.75292 5.38306   1.000 22.89040 ? 30  PRO B HG2  1 
ATOM   2250 H  HG3  . PRO B 1 34  ? 34.46449 25.85590 6.28871   1.000 22.89040 ? 30  PRO B HG3  1 
ATOM   2251 H  HD2  . PRO B 1 34  ? 33.83909 26.46878 3.89994   1.000 22.42229 ? 30  PRO B HD2  1 
ATOM   2252 H  HD3  . PRO B 1 34  ? 35.20815 27.01788 4.49120   1.000 22.42229 ? 30  PRO B HD3  1 
ATOM   2253 N  N    . ASN B 1 35  ? 36.25957 21.87709 3.62051   1.000 21.28705 ? 31  ASN B N    1 
ATOM   2254 C  CA   . ASN B 1 35  ? 35.77127 20.51252 3.61452   1.000 21.16075 ? 31  ASN B CA   1 
ATOM   2255 C  C    . ASN B 1 35  ? 34.78718 20.32564 4.75931   1.000 20.20607 ? 31  ASN B C    1 
ATOM   2256 O  O    . ASN B 1 35  ? 34.98758 20.83450 5.87311   1.000 21.56207 ? 31  ASN B O    1 
ATOM   2257 C  CB   . ASN B 1 35  ? 36.94506 19.53461 3.74217   1.000 24.02516 ? 31  ASN B CB   1 
ATOM   2258 C  CG   . ASN B 1 35  ? 36.49068 18.10594 3.97860   1.000 24.75808 ? 31  ASN B CG   1 
ATOM   2259 O  OD1  . ASN B 1 35  ? 36.45055 17.64356 5.11275   1.000 27.06737 ? 31  ASN B OD1  1 
ATOM   2260 N  ND2  . ASN B 1 35  ? 36.13403 17.40419 2.90710   1.000 25.56570 ? 31  ASN B ND2  1 
ATOM   2261 H  H    . ASN B 1 35  ? 37.11745 21.93745 3.61866   1.000 25.56919 ? 31  ASN B H    1 
ATOM   2262 H  HA   . ASN B 1 35  ? 35.31902 20.31723 2.77891   1.000 25.41763 ? 31  ASN B HA   1 
ATOM   2263 H  HB2  . ASN B 1 35  ? 37.46356 19.55344 2.92260   1.000 28.85492 ? 31  ASN B HB2  1 
ATOM   2264 H  HB3  . ASN B 1 35  ? 37.49968 19.80164 4.49183   1.000 28.85492 ? 31  ASN B HB3  1 
ATOM   2265 H  HD21 . ASN B 1 35  ? 35.86990 16.59043 2.99440   1.000 30.70356 ? 31  ASN B HD21 1 
ATOM   2266 H  HD22 . ASN B 1 35  ? 36.16748 17.76404 2.12672   1.000 30.70356 ? 31  ASN B HD22 1 
ATOM   2267 N  N    . LEU B 1 36  ? 33.70226 19.60961 4.46214   1.000 19.77736 ? 32  LEU B N    1 
ATOM   2268 C  CA   . LEU B 1 36  ? 32.57636 19.45983 5.37340   1.000 19.51513 ? 32  LEU B CA   1 
ATOM   2269 C  C    . LEU B 1 36  ? 32.53614 18.08978 6.02618   1.000 20.32990 ? 32  LEU B C    1 
ATOM   2270 O  O    . LEU B 1 36  ? 31.57716 17.79063 6.74211   1.000 20.95601 ? 32  LEU B O    1 
ATOM   2271 C  CB   . LEU B 1 36  ? 31.25586 19.73678 4.64696   1.000 17.72651 ? 32  LEU B CB   1 
ATOM   2272 C  CG   . LEU B 1 36  ? 31.09257 21.14051 4.05686   1.000 17.33242 ? 32  LEU B CG   1 
ATOM   2273 C  CD1  . LEU B 1 36  ? 29.76585 21.22008 3.32092   1.000 17.59797 ? 32  LEU B CD1  1 
ATOM   2274 C  CD2  . LEU B 1 36  ? 31.17168 22.20585 5.14393   1.000 19.22998 ? 32  LEU B CD2  1 
ATOM   2275 H  H    . LEU B 1 36  ? 33.59695 19.19203 3.71774   1.000 23.75755 ? 32  LEU B H    1 
ATOM   2276 H  HA   . LEU B 1 36  ? 32.66677 20.12060 6.07774   1.000 23.44288 ? 32  LEU B HA   1 
ATOM   2277 H  HB2  . LEU B 1 36  ? 31.17663 19.10659 3.91382   1.000 21.29654 ? 32  LEU B HB2  1 
ATOM   2278 H  HB3  . LEU B 1 36  ? 30.53083 19.60481 5.27768   1.000 21.29654 ? 32  LEU B HB3  1 
ATOM   2279 H  HG   . LEU B 1 36  ? 31.81358 21.31689 3.43241   1.000 20.82364 ? 32  LEU B HG   1 
ATOM   2280 H  HD11 . LEU B 1 36  ? 29.66007 22.11266 2.95620   1.000 21.14230 ? 32  LEU B HD11 1 
ATOM   2281 H  HD12 . LEU B 1 36  ? 29.76297 20.56715 2.60359   1.000 21.14230 ? 32  LEU B HD12 1 
ATOM   2282 H  HD13 . LEU B 1 36  ? 29.04717 21.03006 3.94406   1.000 21.14230 ? 32  LEU B HD13 1 
ATOM   2283 H  HD21 . LEU B 1 36  ? 30.85416 23.04870 4.78381   1.000 23.10070 ? 32  LEU B HD21 1 
ATOM   2284 H  HD22 . LEU B 1 36  ? 30.61641 21.93560 5.89195   1.000 23.10070 ? 32  LEU B HD22 1 
ATOM   2285 H  HD23 . LEU B 1 36  ? 32.09364 22.29548 5.43177   1.000 23.10070 ? 32  LEU B HD23 1 
ATOM   2286 N  N    . HIS B 1 37  ? 33.54769 17.25016 5.82386   1.000 23.19786 ? 33  HIS B N    1 
ATOM   2287 C  CA   . HIS B 1 37  ? 33.52099 15.96509 6.50178   1.000 23.93920 ? 33  HIS B CA   1 
ATOM   2288 C  C    . HIS B 1 37  ? 33.55051 16.16238 8.01086   1.000 24.45100 ? 33  HIS B C    1 
ATOM   2289 O  O    . HIS B 1 37  ? 34.30949 16.98198 8.53665   1.000 25.76605 ? 33  HIS B O    1 
ATOM   2290 C  CB   . HIS B 1 37  ? 34.67872 15.06545 6.08247   1.000 28.76536 ? 33  HIS B CB   1 
ATOM   2291 C  CG   . HIS B 1 37  ? 34.54382 13.67435 6.61468   1.000 35.98879 ? 33  HIS B CG   1 
ATOM   2292 N  ND1  . HIS B 1 37  ? 35.22163 13.23133 7.73143   1.000 39.98137 ? 33  HIS B ND1  1 
ATOM   2293 C  CD2  . HIS B 1 37  ? 33.76255 12.64318 6.21535   1.000 37.98899 ? 33  HIS B CD2  1 
ATOM   2294 C  CE1  . HIS B 1 37  ? 34.87927 11.98089 7.98291   1.000 40.65107 ? 33  HIS B CE1  1 
ATOM   2295 N  NE2  . HIS B 1 37  ? 33.99705 11.59989 7.07628   1.000 39.51293 ? 33  HIS B NE2  1 
ATOM   2296 H  H    . HIS B 1 37  ? 34.23026 17.39518 5.32121   1.000 27.86216 ? 33  HIS B H    1 
ATOM   2297 H  HA   . HIS B 1 37  ? 32.70146 15.51215 6.24857   1.000 28.75177 ? 33  HIS B HA   1 
ATOM   2298 H  HB2  . HIS B 1 37  ? 34.70711 15.01631 5.11413   1.000 34.54316 ? 33  HIS B HB2  1 
ATOM   2299 H  HB3  . HIS B 1 37  ? 35.50807 15.43832 6.42019   1.000 34.54316 ? 33  HIS B HB3  1 
ATOM   2300 H  HD2  . HIS B 1 37  ? 33.17673 12.64189 5.49305   1.000 45.61152 ? 33  HIS B HD2  1 
ATOM   2301 H  HE1  . HIS B 1 37  ? 35.20397 11.45752 8.67973   1.000 48.80601 ? 33  HIS B HE1  1 
ATOM   2302 H  HE2  . HIS B 1 37  ? 33.62916 10.82379 7.03251   1.000 47.44024 ? 33  HIS B HE2  1 
ATOM   2303 N  N    . GLY B 1 38  ? 32.69691 15.41531 8.69903   1.000 22.58445 ? 34  GLY B N    1 
ATOM   2304 C  CA   . GLY B 1 38  ? 32.54531 15.54418 10.13216  1.000 25.40662 ? 34  GLY B CA   1 
ATOM   2305 C  C    . GLY B 1 38  ? 31.64471 16.67367 10.58211  1.000 26.38650 ? 34  GLY B C    1 
ATOM   2306 O  O    . GLY B 1 38  ? 31.64076 17.00528 11.77108  1.000 29.15207 ? 34  GLY B O    1 
ATOM   2307 H  H    . GLY B 1 38  ? 32.18660 14.81711 8.35069   1.000 27.12607 ? 34  GLY B H    1 
ATOM   2308 H  HA2  . GLY B 1 38  ? 32.17743 14.71698 10.48045  1.000 30.51267 ? 34  GLY B HA2  1 
ATOM   2309 H  HA3  . GLY B 1 38  ? 33.42033 15.69049 10.52438  1.000 30.51267 ? 34  GLY B HA3  1 
ATOM   2310 N  N    . LEU B 1 39  ? 30.83656 17.23727 9.67848   1.000 24.51439 ? 35  LEU B N    1 
ATOM   2311 C  CA   . LEU B 1 39  ? 30.10728 18.47430 9.95548   1.000 24.40799 ? 35  LEU B CA   1 
ATOM   2312 C  C    . LEU B 1 39  ? 29.17718 18.34059 11.15366  1.000 25.36804 ? 35  LEU B C    1 
ATOM   2313 O  O    . LEU B 1 39  ? 29.11231 19.23378 12.01007  1.000 24.96036 ? 35  LEU B O    1 
ATOM   2314 C  CB   . LEU B 1 39  ? 29.28518 18.84751 8.72095   1.000 24.15348 ? 35  LEU B CB   1 
ATOM   2315 C  CG   . LEU B 1 39  ? 28.38288 20.07812 8.77849   1.000 22.10941 ? 35  LEU B CG   1 
ATOM   2316 C  CD1  . LEU B 1 39  ? 29.21892 21.31354 8.97453   1.000 24.37124 ? 35  LEU B CD1  1 
ATOM   2317 C  CD2  . LEU B 1 39  ? 27.56010 20.17503 7.51067   1.000 23.38235 ? 35  LEU B CD2  1 
ATOM   2318 H  H    . LEU B 1 39  ? 30.69156 16.92184 8.89166   1.000 29.44200 ? 35  LEU B H    1 
ATOM   2319 H  HA   . LEU B 1 39  ? 30.75256 19.17028 10.15576  1.000 29.31431 ? 35  LEU B HA   1 
ATOM   2320 H  HB2  . LEU B 1 39  ? 29.90713 18.99710 7.99176   1.000 29.00890 ? 35  LEU B HB2  1 
ATOM   2321 H  HB3  . LEU B 1 39  ? 28.70924 18.09426 8.51651   1.000 29.00890 ? 35  LEU B HB3  1 
ATOM   2322 H  HG   . LEU B 1 39  ? 27.77040 20.00672 9.52727   1.000 26.55602 ? 35  LEU B HG   1 
ATOM   2323 H  HD11 . LEU B 1 39  ? 28.64381 22.09364 8.93471   1.000 29.27022 ? 35  LEU B HD11 1 
ATOM   2324 H  HD12 . LEU B 1 39  ? 29.65337 21.26672 9.84053   1.000 29.27022 ? 35  LEU B HD12 1 
ATOM   2325 H  HD13 . LEU B 1 39  ? 29.88604 21.35819 8.27177   1.000 29.27022 ? 35  LEU B HD13 1 
ATOM   2326 H  HD21 . LEU B 1 39  ? 27.01903 20.97932 7.54603   1.000 28.08355 ? 35  LEU B HD21 1 
ATOM   2327 H  HD22 . LEU B 1 39  ? 28.15833 20.21209 6.74801   1.000 28.08355 ? 35  LEU B HD22 1 
ATOM   2328 H  HD23 . LEU B 1 39  ? 26.98824 19.39429 7.44486   1.000 28.08355 ? 35  LEU B HD23 1 
ATOM   2329 N  N    . PHE B 1 40  ? 28.40897 17.26363 11.20469  1.000 22.55828 ? 36  PHE B N    1 
ATOM   2330 C  CA   . PHE B 1 40  ? 27.35497 17.16513 12.20386  1.000 23.08258 ? 36  PHE B CA   1 
ATOM   2331 C  C    . PHE B 1 40  ? 27.96479 16.91597 13.57560  1.000 22.30944 ? 36  PHE B C    1 
ATOM   2332 O  O    . PHE B 1 40  ? 28.71768 15.95411 13.76910  1.000 25.53723 ? 36  PHE B O    1 
ATOM   2333 C  CB   . PHE B 1 40  ? 26.37416 16.05584 11.84000  1.000 22.96401 ? 36  PHE B CB   1 
ATOM   2334 C  CG   . PHE B 1 40  ? 25.40855 16.43634 10.74133  1.000 23.62271 ? 36  PHE B CG   1 
ATOM   2335 C  CD1  . PHE B 1 40  ? 25.83552 16.55075 9.42829   1.000 24.68080 ? 36  PHE B CD1  1 
ATOM   2336 C  CD2  . PHE B 1 40  ? 24.06939 16.67930 11.02368  1.000 24.60557 ? 36  PHE B CD2  1 
ATOM   2337 C  CE1  . PHE B 1 40  ? 24.94401 16.90022 8.42068   1.000 24.72534 ? 36  PHE B CE1  1 
ATOM   2338 C  CE2  . PHE B 1 40  ? 23.16966 17.02739 10.01336  1.000 25.73682 ? 36  PHE B CE2  1 
ATOM   2339 C  CZ   . PHE B 1 40  ? 23.60982 17.13740 8.71410   1.000 26.03204 ? 36  PHE B CZ   1 
ATOM   2340 H  H    . PHE B 1 40  ? 28.47466 16.58474 10.68087  1.000 27.09466 ? 36  PHE B H    1 
ATOM   2341 H  HA   . PHE B 1 40  ? 26.85953 17.99847 12.23518  1.000 27.72383 ? 36  PHE B HA   1 
ATOM   2342 H  HB2  . PHE B 1 40  ? 26.87561 15.28195 11.53910  1.000 27.58154 ? 36  PHE B HB2  1 
ATOM   2343 H  HB3  . PHE B 1 40  ? 25.85382 15.82871 12.62649  1.000 27.58154 ? 36  PHE B HB3  1 
ATOM   2344 H  HD1  . PHE B 1 40  ? 26.72765 16.39212 9.21891   1.000 29.64169 ? 36  PHE B HD1  1 
ATOM   2345 H  HD2  . PHE B 1 40  ? 23.76716 16.60890 11.90037  1.000 29.55141 ? 36  PHE B HD2  1 
ATOM   2346 H  HE1  . PHE B 1 40  ? 25.24449 16.97546 7.54378   1.000 29.69514 ? 36  PHE B HE1  1 
ATOM   2347 H  HE2  . PHE B 1 40  ? 22.27615 17.18428 10.21809  1.000 30.90891 ? 36  PHE B HE2  1 
ATOM   2348 H  HZ   . PHE B 1 40  ? 23.01599 17.36941 8.03703   1.000 31.26318 ? 36  PHE B HZ   1 
ATOM   2349 N  N    A GLY B 1 41  ? 27.68626 17.82167 14.51549  0.584 18.71188 ? 37  GLY B N    1 
ATOM   2350 N  N    B GLY B 1 41  ? 27.57439 17.74163 14.54127  0.416 22.59744 ? 37  GLY B N    1 
ATOM   2351 C  CA   A GLY B 1 41  ? 28.31281 17.79766 15.82536  0.584 16.03980 ? 37  GLY B CA   1 
ATOM   2352 C  CA   B GLY B 1 41  ? 28.00197 17.57896 15.91077  0.416 23.71361 ? 37  GLY B CA   1 
ATOM   2353 C  C    A GLY B 1 41  ? 29.55807 18.65416 15.97037  0.584 16.75399 ? 37  GLY B C    1 
ATOM   2354 C  C    B GLY B 1 41  ? 29.25039 18.34173 16.28723  0.416 25.53441 ? 37  GLY B C    1 
ATOM   2355 O  O    A GLY B 1 41  ? 30.10410 18.73801 17.07976  0.584 16.27873 ? 37  GLY B O    1 
ATOM   2356 O  O    B GLY B 1 41  ? 29.72468 18.18515 17.41978  0.416 27.05106 ? 37  GLY B O    1 
ATOM   2357 H  H    A GLY B 1 41  ? 27.12812 18.46749 14.41066  0.584 22.47898 ? 37  GLY B H    1 
ATOM   2358 H  H    B GLY B 1 41  ? 27.05220 18.41377 14.41822  0.416 27.14165 ? 37  GLY B H    1 
ATOM   2359 H  HA2  A GLY B 1 41  ? 27.66758 18.10529 16.48106  0.584 19.27248 ? 37  GLY B HA2  1 
ATOM   2360 H  HA2  B GLY B 1 41  ? 27.28737 17.87604 16.49557  0.416 28.48107 ? 37  GLY B HA2  1 
ATOM   2361 H  HA3  A GLY B 1 41  ? 28.56078 16.88280 16.03140  0.584 19.27248 ? 37  GLY B HA3  1 
ATOM   2362 H  HA3  B GLY B 1 41  ? 28.17160 16.63768 16.07241  0.416 28.48107 ? 37  GLY B HA3  1 
ATOM   2363 N  N    A ARG B 1 42  ? 30.01762 19.29533 14.89351  0.584 15.82589 ? 38  ARG B N    1 
ATOM   2364 N  N    B ARG B 1 42  ? 29.79515 19.16275 15.38518  0.416 26.34124 ? 38  ARG B N    1 
ATOM   2365 C  CA   A ARG B 1 42  ? 31.19712 20.14874 14.92647  0.584 18.41290 ? 38  ARG B CA   1 
ATOM   2366 C  CA   B ARG B 1 42  ? 30.97464 19.96708 15.66985  0.416 26.18449 ? 38  ARG B CA   1 
ATOM   2367 C  C    A ARG B 1 42  ? 30.77932 21.58447 15.22875  0.584 15.89054 ? 38  ARG B C    1 
ATOM   2368 C  C    B ARG B 1 42  ? 30.69687 21.45048 15.45259  0.416 22.31622 ? 38  ARG B C    1 
ATOM   2369 O  O    A ARG B 1 42  ? 29.78553 22.07933 14.67610  0.584 14.30708 ? 38  ARG B O    1 
ATOM   2370 O  O    B ARG B 1 42  ? 29.77471 21.84859 14.73209  0.416 22.72091 ? 38  ARG B O    1 
ATOM   2371 C  CB   A ARG B 1 42  ? 31.85960 20.08827 13.54468  0.584 23.92165 ? 38  ARG B CB   1 
ATOM   2372 C  CB   B ARG B 1 42  ? 32.19588 19.50681 14.86310  0.416 29.52656 ? 38  ARG B CB   1 
ATOM   2373 C  CG   A ARG B 1 42  ? 33.31482 20.55085 13.46551  0.584 26.18077 ? 38  ARG B CG   1 
ATOM   2374 C  CG   B ARG B 1 42  ? 32.10421 19.69884 13.36665  0.416 31.55003 ? 38  ARG B CG   1 
ATOM   2375 C  CD   A ARG B 1 42  ? 33.98492 20.14926 12.12140  0.584 26.61876 ? 38  ARG B CD   1 
ATOM   2376 C  CD   B ARG B 1 42  ? 33.39642 19.27461 12.71534  0.416 32.52185 ? 38  ARG B CD   1 
ATOM   2377 N  NE   A ARG B 1 42  ? 33.55593 20.94999 10.96575  0.584 27.36597 ? 38  ARG B NE   1 
ATOM   2378 N  NE   B ARG B 1 42  ? 33.51166 19.77561 11.35113  0.416 31.55618 ? 38  ARG B NE   1 
ATOM   2379 C  CZ   A ARG B 1 42  ? 33.73114 20.59551 9.68856   0.584 27.25798 ? 38  ARG B CZ   1 
ATOM   2380 C  CZ   B ARG B 1 42  ? 34.42359 19.37235 10.47331  0.416 28.43660 ? 38  ARG B CZ   1 
ATOM   2381 N  NH1  A ARG B 1 42  ? 34.29892 19.44004 9.37743   0.584 29.76672 ? 38  ARG B NH1  1 
ATOM   2382 N  NH1  B ARG B 1 42  ? 35.31042 18.43307 10.79037  0.416 25.76336 ? 38  ARG B NH1  1 
ATOM   2383 N  NH2  A ARG B 1 42  ? 33.32480 21.39335 8.71097   0.584 25.33563 ? 38  ARG B NH2  1 
ATOM   2384 N  NH2  B ARG B 1 42  ? 34.43793 19.90490 9.25638   0.416 29.22837 ? 38  ARG B NH2  1 
ATOM   2385 H  H    A ARG B 1 42  ? 29.65193 19.24793 14.11658  0.584 19.01580 ? 38  ARG B H    1 
ATOM   2386 H  H    B ARG B 1 42  ? 29.48862 19.26801 14.58859  0.416 31.63421 ? 38  ARG B H    1 
ATOM   2387 H  HA   A ARG B 1 42  ? 31.82303 19.86391 15.61057  0.584 22.12021 ? 38  ARG B HA   1 
ATOM   2388 H  HA   B ARG B 1 42  ? 31.19655 19.86212 16.60827  0.416 31.44612 ? 38  ARG B HA   1 
ATOM   2389 H  HB2  A ARG B 1 42  ? 31.83676 19.16774 13.23973  0.584 28.73071 ? 38  ARG B HB2  1 
ATOM   2390 H  HB2  B ARG B 1 42  ? 32.96893 20.00572 15.17032  0.416 35.45660 ? 38  ARG B HB2  1 
ATOM   2391 H  HB3  A ARG B 1 42  ? 31.34919 20.65047 12.94109  0.584 28.73071 ? 38  ARG B HB3  1 
ATOM   2392 H  HB3  B ARG B 1 42  ? 32.32714 18.55930 15.02403  0.416 35.45660 ? 38  ARG B HB3  1 
ATOM   2393 H  HG2  A ARG B 1 42  ? 33.34683 21.51728 13.54221  0.584 31.44165 ? 38  ARG B HG2  1 
ATOM   2394 H  HG2  B ARG B 1 42  ? 31.38299 19.15673 13.01048  0.416 37.88476 ? 38  ARG B HG2  1 
ATOM   2395 H  HG3  A ARG B 1 42  ? 33.81852 20.14387 14.18771  0.584 31.44165 ? 38  ARG B HG3  1 
ATOM   2396 H  HG3  B ARG B 1 42  ? 31.94635 20.63456 13.16561  0.416 37.88476 ? 38  ARG B HG3  1 
ATOM   2397 H  HD2  A ARG B 1 42  ? 34.94510 20.25448 12.21018  0.584 31.96724 ? 38  ARG B HD2  1 
ATOM   2398 H  HD2  B ARG B 1 42  ? 34.14194 19.62207 13.22950  0.416 39.05094 ? 38  ARG B HD2  1 
ATOM   2399 H  HD3  A ARG B 1 42  ? 33.76880 19.22280 11.93199  0.584 31.96724 ? 38  ARG B HD3  1 
ATOM   2400 H  HD3  B ARG B 1 42  ? 33.43615 18.30586 12.68651  0.416 39.05094 ? 38  ARG B HD3  1 
ATOM   2401 H  HE   A ARG B 1 42  ? 33.16452 21.69960 11.12225  0.584 32.86390 ? 38  ARG B HE   1 
ATOM   2402 H  HE   B ARG B 1 42  ? 32.94949 20.37461 11.09663  0.416 37.89215 ? 38  ARG B HE   1 
ATOM   2403 H  HH11 A ARG B 1 42  ? 34.40237 19.22010 8.55249   0.584 35.74479 ? 38  ARG B HH11 1 
ATOM   2404 H  HH11 B ARG B 1 42  ? 35.29884 18.07750 11.57334  0.416 30.94076 ? 38  ARG B HH11 1 
ATOM   2405 H  HH12 B ARG B 1 42  ? 35.89539 18.18135 10.21241  0.416 30.94076 ? 38  ARG B HH12 1 
ATOM   2406 H  HH21 B ARG B 1 42  ? 33.86022 20.50510 9.04282   0.416 35.09877 ? 38  ARG B HH21 1 
ATOM   2407 H  HH22 B ARG B 1 42  ? 35.02494 19.64945 8.68212   0.416 35.09877 ? 38  ARG B HH22 1 
ATOM   2408 N  N    . LYS B 1 43  ? 31.51826 22.24847 16.12634  1.000 18.40836 ? 39  LYS B N    1 
ATOM   2409 C  CA   . LYS B 1 43  ? 31.38559 23.69053 16.24414  1.000 17.04988 ? 39  LYS B CA   1 
ATOM   2410 C  C    A LYS B 1 43  ? 31.76349 24.37555 14.93487  0.821 16.49177 ? 39  LYS B C    1 
ATOM   2411 C  C    B LYS B 1 43  ? 31.72532 24.34779 14.91432  0.179 17.22403 ? 39  LYS B C    1 
ATOM   2412 O  O    A LYS B 1 43  ? 32.55810 23.85872 14.13562  0.821 17.63710 ? 39  LYS B O    1 
ATOM   2413 O  O    B LYS B 1 43  ? 32.34280 23.74603 14.02948  0.179 19.68148 ? 39  LYS B O    1 
ATOM   2414 C  CB   . LYS B 1 43  ? 32.34827 24.24698 17.31460  1.000 16.83221 ? 39  LYS B CB   1 
ATOM   2415 C  CG   . LYS B 1 43  ? 31.96576 24.04598 18.73763  1.000 18.20230 ? 39  LYS B CG   1 
ATOM   2416 C  CD   . LYS B 1 43  ? 33.18274 24.28054 19.63872  1.000 17.92411 ? 39  LYS B CD   1 
ATOM   2417 C  CE   . LYS B 1 43  ? 33.71689 25.71411 19.62779  1.000 19.34731 ? 39  LYS B CE   1 
ATOM   2418 N  NZ   . LYS B 1 43  ? 34.80678 25.87972 20.63125  1.000 17.39503 ? 39  LYS B NZ   1 
ATOM   2419 H  H    . LYS B 1 43  ? 32.08758 21.89078 16.66256  1.000 22.11476 ? 39  LYS B H    1 
ATOM   2420 H  HA   . LYS B 1 43  ? 30.46526 23.88424 16.48155  1.000 20.48458 ? 39  LYS B HA   1 
ATOM   2421 H  HB2  A LYS B 1 43  ? 33.21089 23.82078 17.19152  0.821 20.22337 ? 39  LYS B HB2  1 
ATOM   2422 H  HB2  B LYS B 1 43  ? 33.21089 23.82078 17.19152  0.179 20.22337 ? 39  LYS B HB2  1 
ATOM   2423 H  HB3  A LYS B 1 43  ? 32.42823 25.20376 17.17647  0.821 20.22337 ? 39  LYS B HB3  1 
ATOM   2424 H  HB3  B LYS B 1 43  ? 32.42823 25.20376 17.17647  0.179 20.22337 ? 39  LYS B HB3  1 
ATOM   2425 H  HG2  . LYS B 1 43  ? 31.26998 24.67598 18.98236  1.000 21.86749 ? 39  LYS B HG2  1 
ATOM   2426 H  HG3  . LYS B 1 43  ? 31.65146 23.13757 18.86761  1.000 21.86749 ? 39  LYS B HG3  1 
ATOM   2427 H  HD2  . LYS B 1 43  ? 32.93653 24.06809 20.55258  1.000 21.53366 ? 39  LYS B HD2  1 
ATOM   2428 H  HD3  . LYS B 1 43  ? 33.90165 23.69928 19.34514  1.000 21.53366 ? 39  LYS B HD3  1 
ATOM   2429 H  HE2  . LYS B 1 43  ? 34.07285 25.92046 18.74937  1.000 23.24150 ? 39  LYS B HE2  1 
ATOM   2430 H  HE3  . LYS B 1 43  ? 32.99948 26.32878 19.84781  1.000 23.24150 ? 39  LYS B HE3  1 
ATOM   2431 H  HZ1  . LYS B 1 43  ? 35.59289 25.94428 20.21899  1.000 20.89876 ? 39  LYS B HZ1  1 
ATOM   2432 H  HZ2  . LYS B 1 43  ? 34.67026 26.61747 21.10999  1.000 20.89876 ? 39  LYS B HZ2  1 
ATOM   2433 H  HZ3  . LYS B 1 43  ? 34.82486 25.17886 21.17950  1.000 20.89876 ? 39  LYS B HZ3  1 
ATOM   2434 N  N    A THR B 1 44  ? 31.28547 25.60877 14.78357  0.821 16.73114 ? 40  THR B N    1 
ATOM   2435 N  N    B THR B 1 44  ? 31.33127 25.61009 14.78494  0.179 16.44476 ? 40  THR B N    1 
ATOM   2436 C  CA   A THR B 1 44  ? 31.75196 26.43684 13.67564  0.821 16.40431 ? 40  THR B CA   1 
ATOM   2437 C  CA   B THR B 1 44  ? 31.81706 26.39878 13.66414  0.179 15.66914 ? 40  THR B CA   1 
ATOM   2438 C  C    A THR B 1 44  ? 33.27442 26.61024 13.73544  0.821 15.61579 ? 40  THR B C    1 
ATOM   2439 C  C    B THR B 1 44  ? 33.32644 26.54533 13.80813  0.179 15.57255 ? 40  THR B C    1 
ATOM   2440 O  O    A THR B 1 44  ? 33.90269 26.58380 14.81785  0.821 16.63551 ? 40  THR B O    1 
ATOM   2441 O  O    B THR B 1 44  ? 33.79815 27.16677 14.77057  0.179 16.11003 ? 40  THR B O    1 
ATOM   2442 C  CB   A THR B 1 44  ? 31.10973 27.83015 13.68851  0.821 17.38700 ? 40  THR B CB   1 
ATOM   2443 C  CB   B THR B 1 44  ? 31.15975 27.78186 13.62622  0.179 14.97937 ? 40  THR B CB   1 
ATOM   2444 O  OG1  A THR B 1 44  ? 31.58810 28.58089 14.81773  0.821 19.11603 ? 40  THR B OG1  1 
ATOM   2445 O  OG1  B THR B 1 44  ? 31.56143 28.54227 14.77337  0.179 15.44506 ? 40  THR B OG1  1 
ATOM   2446 C  CG2  A THR B 1 44  ? 29.59070 27.76374 13.71319  0.821 17.27179 ? 40  THR B CG2  1 
ATOM   2447 C  CG2  B THR B 1 44  ? 29.64233 27.66879 13.59922  0.179 14.31111 ? 40  THR B CG2  1 
ATOM   2448 H  H    A THR B 1 44  ? 30.70416 25.98208 15.29575  0.821 20.10210 ? 40  THR B H    1 
ATOM   2449 H  H    B THR B 1 44  ? 30.79717 26.02048 15.31966  0.179 19.75844 ? 40  THR B H    1 
ATOM   2450 H  HA   A THR B 1 44  ? 31.49935 25.99295 12.85099  0.821 19.70990 ? 40  THR B HA   1 
ATOM   2451 H  HA   B THR B 1 44  ? 31.59542 25.95923 12.82833  0.179 18.82770 ? 40  THR B HA   1 
ATOM   2452 H  HB   A THR B 1 44  ? 31.35765 28.28750 12.86981  0.821 20.88913 ? 40  THR B HB   1 
ATOM   2453 H  HB   B THR B 1 44  ? 31.43971 28.24156 12.81925  0.179 17.99997 ? 40  THR B HB   1 
ATOM   2454 H  HG1  A THR B 1 44  ? 31.40546 29.39492 14.71975  0.821 22.96396 ? 40  THR B HG1  1 
ATOM   2455 H  HG1  B THR B 1 44  ? 31.32349 29.34300 14.68496  0.179 18.55880 ? 40  THR B HG1  1 
ATOM   2456 H  HG21 A THR B 1 44  ? 29.21736 28.64198 13.53935  0.821 20.75088 ? 40  THR B HG21 1 
ATOM   2457 H  HG21 B THR B 1 44  ? 29.24888 28.53201 13.39685  0.179 17.19806 ? 40  THR B HG21 1 
ATOM   2458 H  HG22 A THR B 1 44  ? 29.27450 27.14726 13.03432  0.821 20.75088 ? 40  THR B HG22 1 
ATOM   2459 H  HG22 B THR B 1 44  ? 29.36915 27.03151 12.92088  0.179 17.19806 ? 40  THR B HG22 1 
ATOM   2460 H  HG23 A THR B 1 44  ? 29.28604 27.45853 14.58205  0.821 20.75088 ? 40  THR B HG23 1 
ATOM   2461 H  HG23 B THR B 1 44  ? 29.31659 27.36891 14.46228  0.179 17.19806 ? 40  THR B HG23 1 
ATOM   2462 N  N    A GLY B 1 45  ? 33.88094 26.76364 12.55367  0.821 16.24967 ? 41  GLY B N    1 
ATOM   2463 N  N    B GLY B 1 45  ? 34.08912 25.92482 12.90220  0.179 15.19757 ? 41  GLY B N    1 
ATOM   2464 C  CA   A GLY B 1 45  ? 35.24339 27.25873 12.48929  0.821 16.71745 ? 41  GLY B CA   1 
ATOM   2465 C  CA   B GLY B 1 45  ? 35.50388 26.22427 12.77266  0.179 13.58972 ? 41  GLY B CA   1 
ATOM   2466 C  C    A GLY B 1 45  ? 36.35190 26.27152 12.75220  0.821 16.58817 ? 41  GLY B C    1 
ATOM   2467 C  C    B GLY B 1 45  ? 36.48883 25.08940 12.97311  0.179 13.52226 ? 41  GLY B C    1 
ATOM   2468 O  O    A GLY B 1 45  ? 37.46938 26.70240 13.07041  0.821 17.94763 ? 41  GLY B O    1 
ATOM   2469 O  O    B GLY B 1 45  ? 37.65546 25.36446 13.26747  0.179 13.94394 ? 41  GLY B O    1 
ATOM   2470 H  H    A GLY B 1 45  ? 33.52521 26.58906 11.79040  0.821 19.52434 ? 41  GLY B H    1 
ATOM   2471 H  H    B GLY B 1 45  ? 33.80451 25.32697 12.35340  0.179 18.26182 ? 41  GLY B H    1 
ATOM   2472 H  HA2  A GLY B 1 45  ? 35.38977 27.62190 11.60184  0.821 20.08567 ? 41  GLY B HA2  1 
ATOM   2473 H  HA2  B GLY B 1 45  ? 35.65520 26.57507 11.88107  0.179 16.33240 ? 41  GLY B HA2  1 
ATOM   2474 H  HA3  A GLY B 1 45  ? 35.33564 27.97106 13.14119  0.821 20.08567 ? 41  GLY B HA3  1 
ATOM   2475 H  HA3  B GLY B 1 45  ? 35.72578 26.90871 13.42320  0.179 16.33240 ? 41  GLY B HA3  1 
ATOM   2476 N  N    A GLN B 1 46  ? 36.11295 24.96857 12.58362  0.821 15.43614 ? 42  GLN B N    1 
ATOM   2477 N  N    B GLN B 1 46  ? 36.07410 23.82910 12.79492  0.179 13.91081 ? 42  GLN B N    1 
ATOM   2478 C  CA   A GLN B 1 46  ? 37.04575 23.95144 13.06439  0.821 17.19731 ? 42  GLN B CA   1 
ATOM   2479 C  CA   B GLN B 1 46  ? 36.90101 22.68713 13.18568  0.179 15.45852 ? 42  GLN B CA   1 
ATOM   2480 C  C    A GLN B 1 46  ? 37.70313 23.08460 12.00087  0.821 16.86530 ? 42  GLN B C    1 
ATOM   2481 C  C    B GLN B 1 46  ? 37.33383 21.80694 12.01811  0.179 15.18692 ? 42  GLN B C    1 
ATOM   2482 O  O    A GLN B 1 46  ? 38.58887 22.29401 12.35810  0.821 20.40945 ? 42  GLN B O    1 
ATOM   2483 O  O    B GLN B 1 46  ? 37.74925 20.66323 12.23906  0.179 19.06302 ? 42  GLN B O    1 
ATOM   2484 C  CB   A GLN B 1 46  ? 36.33789 23.03080 14.06676  0.821 16.97926 ? 42  GLN B CB   1 
ATOM   2485 C  CB   B GLN B 1 46  ? 36.19624 21.84992 14.25043  0.179 18.17622 ? 42  GLN B CB   1 
ATOM   2486 C  CG   A GLN B 1 46  ? 35.69833 23.78167 15.23613  0.821 15.51967 ? 42  GLN B CG   1 
ATOM   2487 C  CG   B GLN B 1 46  ? 35.68062 22.65214 15.42422  0.179 19.72970 ? 42  GLN B CG   1 
ATOM   2488 C  CD   A GLN B 1 46  ? 36.69281 24.65066 15.99624  0.821 15.52291 ? 42  GLN B CD   1 
ATOM   2489 C  CD   B GLN B 1 46  ? 36.69224 23.63176 15.98410  0.179 21.68863 ? 42  GLN B CD   1 
ATOM   2490 O  OE1  A GLN B 1 46  ? 37.78859 24.20567 16.34890  0.821 17.17866 ? 42  GLN B OE1  1 
ATOM   2491 O  OE1  B GLN B 1 46  ? 37.89192 23.35511 16.01425  0.179 23.25509 ? 42  GLN B OE1  1 
ATOM   2492 N  NE2  A GLN B 1 46  ? 36.31748 25.90028 16.25074  0.821 18.26486 ? 42  GLN B NE2  1 
ATOM   2493 N  NE2  B GLN B 1 46  ? 36.21129 24.78226 16.43891  0.179 22.35313 ? 42  GLN B NE2  1 
ATOM   2494 H  H    A GLN B 1 46  ? 35.41574 24.65096 12.19295  0.821 18.54809 ? 42  GLN B H    1 
ATOM   2495 H  H    B GLN B 1 46  ? 35.31656 23.61420 12.44917  0.179 16.71770 ? 42  GLN B H    1 
ATOM   2496 H  HA   A GLN B 1 46  ? 37.76902 24.42030 13.50931  0.821 20.66150 ? 42  GLN B HA   1 
ATOM   2497 H  HA   B GLN B 1 46  ? 37.71636 23.04710 13.56846  0.179 18.57496 ? 42  GLN B HA   1 
ATOM   2498 H  HB2  A GLN B 1 46  ? 35.63599 22.54607 13.60494  0.821 20.39984 ? 42  GLN B HB2  1 
ATOM   2499 H  HB2  B GLN B 1 46  ? 35.43786 21.40328 13.84266  0.179 21.83619 ? 42  GLN B HB2  1 
ATOM   2500 H  HB3  A GLN B 1 46  ? 36.98607 22.40830 14.43181  0.821 20.39984 ? 42  GLN B HB3  1 
ATOM   2501 H  HB3  B GLN B 1 46  ? 36.82231 21.19357 14.59415  0.179 21.83619 ? 42  GLN B HB3  1 
ATOM   2502 H  HG2  A GLN B 1 46  ? 34.99640 24.35788 14.89527  0.821 18.64834 ? 42  GLN B HG2  1 
ATOM   2503 H  HG2  B GLN B 1 46  ? 34.90422 23.15901 15.13930  0.179 23.70036 ? 42  GLN B HG2  1 
ATOM   2504 H  HG3  A GLN B 1 46  ? 35.32593 23.13791 15.85886  0.821 18.64834 ? 42  GLN B HG3  1 
ATOM   2505 H  HG3  B GLN B 1 46  ? 35.43487 22.04115 16.13640  0.179 23.70036 ? 42  GLN B HG3  1 
ATOM   2506 H  HE21 A GLN B 1 46  ? 35.54743 26.17974 15.98898  0.821 21.94256 ? 42  GLN B HE21 1 
ATOM   2507 H  HE21 B GLN B 1 46  ? 35.36619 24.93816 16.40580  0.179 26.84848 ? 42  GLN B HE21 1 
ATOM   2508 H  HE22 A GLN B 1 46  ? 36.84472 26.42924 16.67715  0.821 21.94256 ? 42  GLN B HE22 1 
ATOM   2509 H  HE22 B GLN B 1 46  ? 36.74478 25.37179 16.76670  0.179 26.84848 ? 42  GLN B HE22 1 
ATOM   2510 N  N    A ALA B 1 47  ? 37.31377 23.18536 10.72871  0.821 18.49526 ? 43  ALA B N    1 
ATOM   2511 N  N    B ALA B 1 47  ? 37.27184 22.31076 10.79043  0.179 15.59451 ? 43  ALA B N    1 
ATOM   2512 C  CA   A ALA B 1 47  ? 37.96511 22.37323 9.70024   0.821 18.92270 ? 43  ALA B CA   1 
ATOM   2513 C  CA   B ALA B 1 47  ? 37.95728 21.66828 9.67696   0.179 14.20884 ? 43  ALA B CA   1 
ATOM   2514 C  C    A ALA B 1 47  ? 39.47360 22.60689 9.70797   0.821 19.80120 ? 43  ALA B C    1 
ATOM   2515 C  C    B ALA B 1 47  ? 39.41001 22.13578 9.68103   0.179 14.99158 ? 43  ALA B C    1 
ATOM   2516 O  O    A ALA B 1 47  ? 39.94016 23.75058 9.64226   0.821 20.86609 ? 43  ALA B O    1 
ATOM   2517 O  O    B ALA B 1 47  ? 39.68127 23.33696 9.58037   0.179 15.41182 ? 43  ALA B O    1 
ATOM   2518 C  CB   A ALA B 1 47  ? 37.39399 22.68528 8.31793   0.821 20.73066 ? 43  ALA B CB   1 
ATOM   2519 C  CB   B ALA B 1 47  ? 37.27029 22.02163 8.36136   0.179 12.67683 ? 43  ALA B CB   1 
ATOM   2520 H  H    A ALA B 1 47  ? 36.69048 23.70311 10.44055  0.821 22.21904 ? 43  ALA B H    1 
ATOM   2521 H  H    B ALA B 1 47  ? 36.83962 23.02302 10.57721  0.179 18.73814 ? 43  ALA B H    1 
ATOM   2522 H  HA   A ALA B 1 47  ? 37.79448 21.43740 9.88996   0.821 22.73197 ? 43  ALA B HA   1 
ATOM   2523 H  HA   B ALA B 1 47  ? 37.93329 20.70322 9.77177   0.179 17.07534 ? 43  ALA B HA   1 
ATOM   2524 H  HB1  A ALA B 1 47  ? 37.78346 22.07684 7.67062   0.821 24.90152 ? 43  ALA B HB1  1 
ATOM   2525 H  HB1  B ALA B 1 47  ? 37.74331 21.59067 7.63238   0.179 15.23693 ? 43  ALA B HB1  1 
ATOM   2526 H  HB2  A ALA B 1 47  ? 36.43096 22.57153 8.34109   0.821 24.90152 ? 43  ALA B HB2  1 
ATOM   2527 H  HB2  B ALA B 1 47  ? 36.35241 21.70930 8.39056   0.179 15.23693 ? 43  ALA B HB2  1 
ATOM   2528 H  HB3  A ALA B 1 47  ? 37.61340 23.60096 8.08493   0.821 24.90152 ? 43  ALA B HB3  1 
ATOM   2529 H  HB3  B ALA B 1 47  ? 37.28852 22.98436 8.24419   0.179 15.23693 ? 43  ALA B HB3  1 
ATOM   2530 N  N    A ALA B 1 48  ? 40.22392 21.51338 9.81773   0.821 21.72821 ? 44  ALA B N    1 
ATOM   2531 N  N    B ALA B 1 48  ? 40.33929 21.19209 9.80742   0.179 17.49900 ? 44  ALA B N    1 
ATOM   2532 C  CA   A ALA B 1 48  ? 41.66688 21.58519 10.02977  0.821 22.09385 ? 44  ALA B CA   1 
ATOM   2533 C  CA   B ALA B 1 48  ? 41.73475 21.53385 10.06296  0.179 18.93849 ? 44  ALA B CA   1 
ATOM   2534 C  C    A ALA B 1 48  ? 42.36087 22.28728 8.87360   0.821 22.14529 ? 44  ALA B C    1 
ATOM   2535 C  C    B ALA B 1 48  ? 42.35612 22.27692 8.88410   0.179 20.43721 ? 44  ALA B C    1 
ATOM   2536 O  O    A ALA B 1 48  ? 42.30338 21.82857 7.72819   0.821 22.37199 ? 44  ALA B O    1 
ATOM   2537 O  O    B ALA B 1 48  ? 42.24183 21.84620 7.73252   0.179 20.87787 ? 44  ALA B O    1 
ATOM   2538 C  CB   A ALA B 1 48  ? 42.22857 20.17549 10.18314  0.821 24.72644 ? 44  ALA B CB   1 
ATOM   2539 C  CB   B ALA B 1 48  ? 42.53166 20.26256 10.34761  0.179 19.26270 ? 44  ALA B CB   1 
ATOM   2540 H  H    A ALA B 1 48  ? 39.92040 20.70998 9.77278   0.821 26.09858 ? 44  ALA B H    1 
ATOM   2541 H  H    B ALA B 1 48  ? 40.18916 20.34727 9.74972   0.179 21.02352 ? 44  ALA B H    1 
ATOM   2542 H  HA   A ALA B 1 48  ? 41.83672 22.09337 10.83836  0.821 26.53735 ? 44  ALA B HA   1 
ATOM   2543 H  HA   B ALA B 1 48  ? 41.77395 22.12083 10.83421  0.179 22.75092 ? 44  ALA B HA   1 
ATOM   2544 H  HB1  A ALA B 1 48  ? 43.18437 20.23157 10.33871  0.821 29.69646 ? 44  ALA B HB1  1 
ATOM   2545 H  HB1  B ALA B 1 48  ? 43.45559 20.50130 10.52158  0.179 23.13997 ? 44  ALA B HB1  1 
ATOM   2546 H  HB2  A ALA B 1 48  ? 41.79572 19.74325 10.93594  0.821 29.69646 ? 44  ALA B HB2  1 
ATOM   2547 H  HB2  B ALA B 1 48  ? 42.15293 19.81937 11.12289  0.179 23.13997 ? 44  ALA B HB2  1 
ATOM   2548 H  HB3  A ALA B 1 48  ? 42.05452 19.67601 9.37005   0.821 29.69646 ? 44  ALA B HB3  1 
ATOM   2549 H  HB3  B ALA B 1 48  ? 42.48084 19.67833 9.57496   0.179 23.13997 ? 44  ALA B HB3  1 
ATOM   2550 N  N    . GLY B 1 49  ? 43.02204 23.39741 9.17874   1.000 21.60963 ? 45  GLY B N    1 
ATOM   2551 C  CA   . GLY B 1 49  ? 43.80031 24.11227 8.19728   1.000 22.54890 ? 45  GLY B CA   1 
ATOM   2552 C  C    . GLY B 1 49  ? 43.04904 25.12952 7.37677   1.000 21.24923 ? 45  GLY B C    1 
ATOM   2553 O  O    . GLY B 1 49  ? 43.67868 25.83293 6.57588   1.000 23.00683 ? 45  GLY B O    1 
ATOM   2554 H  H    . GLY B 1 49  ? 43.03037 23.75499 9.96084   1.000 25.95628 ? 45  GLY B H    1 
ATOM   2555 H  HA2  . GLY B 1 49  ? 44.51717 24.57875 8.65488   1.000 27.08341 ? 45  GLY B HA2  1 
ATOM   2556 H  HA3  . GLY B 1 49  ? 44.18472 23.46811 7.58231   1.000 27.08341 ? 45  GLY B HA3  1 
ATOM   2557 N  N    . PHE B 1 50  ? 41.72606 25.23110 7.52341   1.000 20.92662 ? 46  PHE B N    1 
ATOM   2558 C  CA   . PHE B 1 50  ? 40.97394 26.22614 6.77042   1.000 20.73681 ? 46  PHE B CA   1 
ATOM   2559 C  C    . PHE B 1 50  ? 41.02679 27.56777 7.48795   1.000 20.01891 ? 46  PHE B C    1 
ATOM   2560 O  O    . PHE B 1 50  ? 40.92053 27.63579 8.71571   1.000 23.05218 ? 46  PHE B O    1 
ATOM   2561 C  CB   . PHE B 1 50  ? 39.52198 25.79371 6.54558   1.000 19.90168 ? 46  PHE B CB   1 
ATOM   2562 C  CG   . PHE B 1 50  ? 38.75831 26.73913 5.66247   1.000 19.48817 ? 46  PHE B CG   1 
ATOM   2563 C  CD1  . PHE B 1 50  ? 38.88148 26.65817 4.28278   1.000 20.30320 ? 46  PHE B CD1  1 
ATOM   2564 C  CD2  . PHE B 1 50  ? 37.98384 27.75406 6.20675   1.000 18.54845 ? 46  PHE B CD2  1 
ATOM   2565 C  CE1  . PHE B 1 50  ? 38.20256 27.54174 3.45605   1.000 19.56315 ? 46  PHE B CE1  1 
ATOM   2566 C  CE2  . PHE B 1 50  ? 37.30919 28.64547 5.38374   1.000 18.32135 ? 46  PHE B CE2  1 
ATOM   2567 C  CZ   . PHE B 1 50  ? 37.44014 28.54831 4.00020   1.000 18.85193 ? 46  PHE B CZ   1 
ATOM   2568 H  H    . PHE B 1 50  ? 41.25043 24.74098 8.04606   1.000 25.13668 ? 46  PHE B H    1 
ATOM   2569 H  HA   . PHE B 1 50  ? 41.37250 26.32526 5.89165   1.000 24.90889 ? 46  PHE B HA   1 
ATOM   2570 H  HB2  . PHE B 1 50  ? 39.51530 24.91971 6.12489   1.000 23.90675 ? 46  PHE B HB2  1 
ATOM   2571 H  HB3  . PHE B 1 50  ? 39.06932 25.75290 7.40252   1.000 23.90675 ? 46  PHE B HB3  1 
ATOM   2572 H  HD1  . PHE B 1 50  ? 39.42561 26.00385 3.90769   1.000 24.38857 ? 46  PHE B HD1  1 
ATOM   2573 H  HD2  . PHE B 1 50  ? 37.91628 27.83769 7.13051   1.000 22.28286 ? 46  PHE B HD2  1 
ATOM   2574 H  HE1  . PHE B 1 50  ? 38.26327 27.45300 2.53228   1.000 23.50051 ? 46  PHE B HE1  1 
ATOM   2575 H  HE2  . PHE B 1 50  ? 36.77070 29.30640 5.75536   1.000 22.01035 ? 46  PHE B HE2  1 
ATOM   2576 H  HZ   . PHE B 1 50  ? 37.01349 29.16195 3.44674   1.000 22.64704 ? 46  PHE B HZ   1 
ATOM   2577 N  N    . ALA B 1 51  ? 41.17476 28.63834 6.70775   1.000 22.82902 ? 47  ALA B N    1 
ATOM   2578 C  CA   . ALA B 1 51  ? 41.23809 30.00521 7.22839   1.000 23.06392 ? 47  ALA B CA   1 
ATOM   2579 C  C    . ALA B 1 51  ? 39.82963 30.59296 7.28868   1.000 21.13680 ? 47  ALA B C    1 
ATOM   2580 O  O    . ALA B 1 51  ? 39.31709 31.11473 6.29880   1.000 23.43351 ? 47  ALA B O    1 
ATOM   2581 C  CB   . ALA B 1 51  ? 42.13959 30.85580 6.34422   1.000 24.63761 ? 47  ALA B CB   1 
ATOM   2582 H  H    . ALA B 1 51  ? 41.24247 28.59726 5.85141   1.000 27.41955 ? 47  ALA B H    1 
ATOM   2583 H  HA   . ALA B 1 51  ? 41.59053 29.97975 8.13173   1.000 27.70144 ? 47  ALA B HA   1 
ATOM   2584 H  HB1  . ALA B 1 51  ? 42.22111 31.74015 6.73432   1.000 29.58986 ? 47  ALA B HB1  1 
ATOM   2585 H  HB2  . ALA B 1 51  ? 43.01283 30.43724 6.28812   1.000 29.58986 ? 47  ALA B HB2  1 
ATOM   2586 H  HB3  . ALA B 1 51  ? 41.74580 30.91932 5.46003   1.000 29.58986 ? 47  ALA B HB3  1 
ATOM   2587 N  N    . TYR B 1 52  ? 39.21529 30.53400 8.45691   1.000 21.32136 ? 48  TYR B N    1 
ATOM   2588 C  CA   . TYR B 1 52  ? 37.87549 31.06214 8.67004   1.000 20.11958 ? 48  TYR B CA   1 
ATOM   2589 C  C    . TYR B 1 52  ? 37.88430 32.54368 9.03238   1.000 20.26764 ? 48  TYR B C    1 
ATOM   2590 O  O    . TYR B 1 52  ? 38.85500 33.07326 9.57606   1.000 22.94651 ? 48  TYR B O    1 
ATOM   2591 C  CB   . TYR B 1 52  ? 37.21992 30.33991 9.83091   1.000 20.97253 ? 48  TYR B CB   1 
ATOM   2592 C  CG   . TYR B 1 52  ? 36.84785 28.91348 9.58892   1.000 18.60007 ? 48  TYR B CG   1 
ATOM   2593 C  CD1  . TYR B 1 52  ? 35.60393 28.59675 9.06455   1.000 18.01888 ? 48  TYR B CD1  1 
ATOM   2594 C  CD2  . TYR B 1 52  ? 37.71189 27.87733 9.91450   1.000 18.86561 ? 48  TYR B CD2  1 
ATOM   2595 C  CE1  . TYR B 1 52  ? 35.23111 27.29080 8.87642   1.000 19.00544 ? 48  TYR B CE1  1 
ATOM   2596 C  CE2  . TYR B 1 52  ? 37.36387 26.57038 9.71939   1.000 18.91133 ? 48  TYR B CE2  1 
ATOM   2597 C  CZ   . TYR B 1 52  ? 36.10499 26.27480 9.20284   1.000 19.74541 ? 48  TYR B CZ   1 
ATOM   2598 O  OH   . TYR B 1 52  ? 35.74218 24.96500 9.05391   1.000 19.66041 ? 48  TYR B OH   1 
ATOM   2599 H  H    . TYR B 1 52  ? 39.56108 30.18384 9.16219   1.000 25.61036 ? 48  TYR B H    1 
ATOM   2600 H  HA   . TYR B 1 52  ? 37.38074 30.94054 7.84461   1.000 24.16822 ? 48  TYR B HA   1 
ATOM   2601 H  HB2  . TYR B 1 52  ? 37.83429 30.35230 10.58144  1.000 25.19176 ? 48  TYR B HB2  1 
ATOM   2602 H  HB3  . TYR B 1 52  ? 36.40522 30.81332 10.06123  1.000 25.19176 ? 48  TYR B HB3  1 
ATOM   2603 H  HD1  . TYR B 1 52  ? 35.01455 29.27934 8.83739   1.000 21.64738 ? 48  TYR B HD1  1 
ATOM   2604 H  HD2  . TYR B 1 52  ? 38.54629 28.07692 10.27344  1.000 22.66345 ? 48  TYR B HD2  1 
ATOM   2605 H  HE1  . TYR B 1 52  ? 34.39164 27.09065 8.52981   1.000 22.83126 ? 48  TYR B HE1  1 
ATOM   2606 H  HE2  . TYR B 1 52  ? 37.95965 25.88764 9.92873   1.000 22.71832 ? 48  TYR B HE2  1 
ATOM   2607 H  HH   . TYR B 1 52  ? 34.90525 24.90050 9.02249   1.000 23.61722 ? 48  TYR B HH   1 
ATOM   2608 N  N    . THR B 1 53  ? 36.73724 33.18930 8.83162   1.000 20.09286 ? 49  THR B N    1 
ATOM   2609 C  CA   . THR B 1 53  ? 36.56264 34.54559 9.33222   1.000 21.36887 ? 49  THR B CA   1 
ATOM   2610 C  C    . THR B 1 53  ? 36.43595 34.53675 10.85238  1.000 20.76584 ? 49  THR B C    1 
ATOM   2611 O  O    . THR B 1 53  ? 36.03535 33.54355 11.46595  1.000 19.29773 ? 49  THR B O    1 
ATOM   2612 C  CB   . THR B 1 53  ? 35.28705 35.19210 8.78041   1.000 21.43516 ? 49  THR B CB   1 
ATOM   2613 O  OG1  . THR B 1 53  ? 34.12156 34.45211 9.20635   1.000 21.13107 ? 49  THR B OG1  1 
ATOM   2614 C  CG2  . THR B 1 53  ? 35.33082 35.31659 7.26657   1.000 24.51501 ? 49  THR B CG2  1 
ATOM   2615 H  H    . THR B 1 53  ? 36.05643 32.86871 8.41530   1.000 24.13616 ? 49  THR B H    1 
ATOM   2616 H  HA   . THR B 1 53  ? 37.33239 35.06572 9.05323   1.000 25.66738 ? 49  THR B HA   1 
ATOM   2617 H  HB   . THR B 1 53  ? 35.21722 36.09346 9.13195   1.000 25.74692 ? 49  THR B HB   1 
ATOM   2618 H  HG1  . THR B 1 53  ? 34.21294 33.63868 9.01772   1.000 25.38201 ? 49  THR B HG1  1 
ATOM   2619 H  HG21 . THR B 1 53  ? 34.43066 35.39653 6.91410   1.000 29.44274 ? 49  THR B HG21 1 
ATOM   2620 H  HG22 . THR B 1 53  ? 35.83919 36.10279 7.01290   1.000 29.44274 ? 49  THR B HG22 1 
ATOM   2621 H  HG23 . THR B 1 53  ? 35.75126 34.53199 6.88119   1.000 29.44274 ? 49  THR B HG23 1 
ATOM   2622 N  N    . ASP B 1 54  ? 36.75941 35.68099 11.45814  1.000 20.48522 ? 50  ASP B N    1 
ATOM   2623 C  CA   . ASP B 1 54  ? 36.45235 35.87781 12.87145  1.000 20.05153 ? 50  ASP B CA   1 
ATOM   2624 C  C    . ASP B 1 54  ? 34.96633 35.66926 13.14869  1.000 18.63781 ? 50  ASP B C    1 
ATOM   2625 O  O    . ASP B 1 54  ? 34.58735 35.11014 14.18290  1.000 19.73784 ? 50  ASP B O    1 
ATOM   2626 C  CB   . ASP B 1 54  ? 36.86026 37.28573 13.30906  1.000 22.80003 ? 50  ASP B CB   1 
ATOM   2627 C  CG   . ASP B 1 54  ? 38.36847 37.52060 13.26273  1.000 27.26275 ? 50  ASP B CG   1 
ATOM   2628 O  OD1  . ASP B 1 54  ? 39.15390 36.55444 13.34695  1.000 27.26367 ? 50  ASP B OD1  1 
ATOM   2629 O  OD2  . ASP B 1 54  ? 38.76746 38.70109 13.17086  1.000 30.63435 ? 50  ASP B OD2  1 
ATOM   2630 H  H    . ASP B 1 54  ? 37.15020 36.34780 11.08098  1.000 24.60699 ? 50  ASP B H    1 
ATOM   2631 H  HA   . ASP B 1 54  ? 36.96042 35.23192 13.38681  1.000 24.08657 ? 50  ASP B HA   1 
ATOM   2632 H  HB2  . ASP B 1 54  ? 36.44041 37.93160 12.71959  1.000 27.38477 ? 50  ASP B HB2  1 
ATOM   2633 H  HB3  . ASP B 1 54  ? 36.56489 37.42858 14.22189  1.000 27.38477 ? 50  ASP B HB3  1 
ATOM   2634 N  N    . ALA B 1 55  ? 34.10735 36.09820 12.22922  1.000 20.74737 ? 51  ALA B N    1 
ATOM   2635 C  CA   . ALA B 1 55  ? 32.67028 35.98976 12.44695  1.000 19.90472 ? 51  ALA B CA   1 
ATOM   2636 C  C    . ALA B 1 55  ? 32.23573 34.53512 12.56814  1.000 18.16514 ? 51  ALA B C    1 
ATOM   2637 O  O    . ALA B 1 55  ? 31.45553 34.18048 13.45864  1.000 19.44823 ? 51  ALA B O    1 
ATOM   2638 C  CB   . ALA B 1 55  ? 31.92795 36.67460 11.29662  1.000 22.12013 ? 51  ALA B CB   1 
ATOM   2639 H  H    . ALA B 1 55  ? 34.32654 36.45294 11.47708  1.000 24.92157 ? 51  ALA B H    1 
ATOM   2640 H  HA   . ALA B 1 55  ? 32.44312 36.43839 13.27643  1.000 23.91040 ? 51  ALA B HA   1 
ATOM   2641 H  HB1  . ALA B 1 55  ? 30.97522 36.52676 11.40317  1.000 26.56888 ? 51  ALA B HB1  1 
ATOM   2642 H  HB2  . ALA B 1 55  ? 32.11967 37.62521 11.31858  1.000 26.56888 ? 51  ALA B HB2  1 
ATOM   2643 H  HB3  . ALA B 1 55  ? 32.22952 36.29566 10.45616  1.000 26.56888 ? 51  ALA B HB3  1 
ATOM   2644 N  N    . ASN B 1 56  ? 32.72267 33.67174 11.67330  1.000 18.32421 ? 52  ASN B N    1 
ATOM   2645 C  CA   . ASN B 1 56  ? 32.34860 32.26221 11.75764  1.000 17.58243 ? 52  ASN B CA   1 
ATOM   2646 C  C    . ASN B 1 56  ? 32.81170 31.66345 13.08167  1.000 17.52671 ? 52  ASN B C    1 
ATOM   2647 O  O    . ASN B 1 56  ? 32.03909 31.00024 13.78457  1.000 18.52823 ? 52  ASN B O    1 
ATOM   2648 C  CB   . ASN B 1 56  ? 32.89553 31.48852 10.55269  1.000 19.03816 ? 52  ASN B CB   1 
ATOM   2649 C  CG   . ASN B 1 56  ? 32.75981 29.98036 10.70460  1.000 17.47426 ? 52  ASN B CG   1 
ATOM   2650 O  OD1  . ASN B 1 56  ? 33.44392 29.36834 11.51450  1.000 19.51224 ? 52  ASN B OD1  1 
ATOM   2651 N  ND2  . ASN B 1 56  ? 31.88452 29.36907 9.90381   1.000 18.79553 ? 52  ASN B ND2  1 
ATOM   2652 H  H    . ASN B 1 56  ? 33.25488 33.86979 11.02745  1.000 22.01378 ? 52  ASN B H    1 
ATOM   2653 H  HA   . ASN B 1 56  ? 31.38250 32.18337 11.72127  1.000 21.12365 ? 52  ASN B HA   1 
ATOM   2654 H  HB2  . ASN B 1 56  ? 32.40602 31.75442 9.75859   1.000 22.87052 ? 52  ASN B HB2  1 
ATOM   2655 H  HB3  . ASN B 1 56  ? 33.83735 31.69490 10.44648  1.000 22.87052 ? 52  ASN B HB3  1 
ATOM   2656 H  HD21 . ASN B 1 56  ? 31.77589 28.51755 9.95593   1.000 22.57937 ? 52  ASN B HD21 1 
ATOM   2657 H  HD22 . ASN B 1 56  ? 31.42911 29.82666 9.33564   1.000 22.57937 ? 52  ASN B HD22 1 
ATOM   2658 N  N    . LYS B 1 57  ? 34.06374 31.93542 13.46615  1.000 17.54151 ? 53  LYS B N    1 
ATOM   2659 C  CA   . LYS B 1 57  ? 34.59647 31.39414 14.71905  1.000 17.65448 ? 53  LYS B CA   1 
ATOM   2660 C  C    . LYS B 1 57  ? 33.78754 31.87403 15.91854  1.000 19.22141 ? 53  LYS B C    1 
ATOM   2661 O  O    . LYS B 1 57  ? 33.49979 31.09643 16.83110  1.000 20.67913 ? 53  LYS B O    1 
ATOM   2662 C  CB   . LYS B 1 57  ? 36.08088 31.75600 14.85408  1.000 19.52326 ? 53  LYS B CB   1 
ATOM   2663 C  CG   . LYS B 1 57  ? 36.94577 31.03962 13.82668  1.000 21.62439 ? 53  LYS B CG   1 
ATOM   2664 C  CD   . LYS B 1 57  ? 38.44241 31.21585 14.04065  1.000 23.41381 ? 53  LYS B CD   1 
ATOM   2665 C  CE   . LYS B 1 57  ? 39.07634 32.23647 13.12803  1.000 29.31789 ? 53  LYS B CE   1 
ATOM   2666 N  NZ   . LYS B 1 57  ? 40.55863 32.08463 13.04674  1.000 28.03090 ? 53  LYS B NZ   1 
ATOM   2667 H  H    . LYS B 1 57  ? 34.61925 32.42369 13.02727  1.000 21.07454 ? 53  LYS B H    1 
ATOM   2668 H  HA   . LYS B 1 57  ? 34.53434 30.42628 14.70189  1.000 21.21010 ? 53  LYS B HA   1 
ATOM   2669 H  HB2  . LYS B 1 57  ? 36.18763 32.71151 14.72558  1.000 23.45264 ? 53  LYS B HB2  1 
ATOM   2670 H  HB3  . LYS B 1 57  ? 36.38998 31.50358 15.73819  1.000 23.45264 ? 53  LYS B HB3  1 
ATOM   2671 H  HG2  . LYS B 1 57  ? 36.75346 30.08970 13.86627  1.000 25.97399 ? 53  LYS B HG2  1 
ATOM   2672 H  HG3  . LYS B 1 57  ? 36.73257 31.38483 12.94562  1.000 25.97399 ? 53  LYS B HG3  1 
ATOM   2673 H  HD2  . LYS B 1 57  ? 38.59504 31.50311 14.95448  1.000 28.12130 ? 53  LYS B HD2  1 
ATOM   2674 H  HD3  . LYS B 1 57  ? 38.88224 30.36593 13.88221  1.000 28.12130 ? 53  LYS B HD3  1 
ATOM   2675 H  HE2  . LYS B 1 57  ? 38.71352 32.13233 12.23449  1.000 35.20620 ? 53  LYS B HE2  1 
ATOM   2676 H  HE3  . LYS B 1 57  ? 38.88268 33.12590 13.46316  1.000 35.20620 ? 53  LYS B HE3  1 
ATOM   2677 H  HZ1  . LYS B 1 57  ? 40.91012 32.76616 12.59499  1.000 33.66181 ? 53  LYS B HZ1  1 
ATOM   2678 H  HZ2  . LYS B 1 57  ? 40.90839 32.06944 13.86500  1.000 33.66181 ? 53  LYS B HZ2  1 
ATOM   2679 H  HZ3  . LYS B 1 57  ? 40.76447 31.32538 12.63050  1.000 33.66181 ? 53  LYS B HZ3  1 
ATOM   2680 N  N    . ALA B 1 58  ? 33.37619 33.14048 15.90904  1.000 18.01781 ? 54  ALA B N    1 
ATOM   2681 C  CA   . ALA B 1 58  ? 32.65982 33.71374 17.03900  1.000 17.53326 ? 54  ALA B CA   1 
ATOM   2682 C  C    . ALA B 1 58  ? 31.24784 33.16466 17.20353  1.000 17.48117 ? 54  ALA B C    1 
ATOM   2683 O  O    . ALA B 1 58  ? 30.68882 33.25762 18.29886  1.000 17.38314 ? 54  ALA B O    1 
ATOM   2684 C  CB   . ALA B 1 58  ? 32.59095 35.22904 16.87753  1.000 21.13530 ? 54  ALA B CB   1 
ATOM   2685 H  H    . ALA B 1 58  ? 33.49986 33.68957 15.25879  1.000 21.64610 ? 54  ALA B H    1 
ATOM   2686 H  HA   . ALA B 1 58  ? 33.15011 33.49723 17.84748  1.000 21.06464 ? 54  ALA B HA   1 
ATOM   2687 H  HB1  . ALA B 1 58  ? 32.09126 35.60335 17.61989  1.000 25.38709 ? 54  ALA B HB1  1 
ATOM   2688 H  HB2  . ALA B 1 58  ? 33.49236 35.58727 16.87144  1.000 25.38709 ? 54  ALA B HB2  1 
ATOM   2689 H  HB3  . ALA B 1 58  ? 32.14647 35.43760 16.04097  1.000 25.38709 ? 54  ALA B HB3  1 
ATOM   2690 N  N    . LYS B 1 59  ? 30.62893 32.65423 16.14091  1.000 17.02657 ? 55  LYS B N    1 
ATOM   2691 C  CA   . LYS B 1 59  ? 29.25745 32.16137 16.25762  1.000 17.00688 ? 55  LYS B CA   1 
ATOM   2692 C  C    . LYS B 1 59  ? 29.17850 31.02313 17.27554  1.000 16.55284 ? 55  LYS B C    1 
ATOM   2693 O  O    . LYS B 1 59  ? 28.34687 31.04642 18.18615  1.000 17.46676 ? 55  LYS B O    1 
ATOM   2694 C  CB   . LYS B 1 59  ? 28.73981 31.73277 14.88750  1.000 15.69486 ? 55  LYS B CB   1 
ATOM   2695 C  CG   . LYS B 1 59  ? 27.26521 31.33672 14.85108  1.000 16.05532 ? 55  LYS B CG   1 
ATOM   2696 C  CD   . LYS B 1 59  ? 26.29736 32.48707 15.07879  1.000 16.85823 ? 55  LYS B CD   1 
ATOM   2697 C  CE   . LYS B 1 59  ? 24.83170 32.02369 15.09594  1.000 18.30963 ? 55  LYS B CE   1 
ATOM   2698 N  NZ   . LYS B 1 59  ? 23.89099 33.18931 15.16016  1.000 19.12260 ? 55  LYS B NZ   1 
ATOM   2699 H  H    . LYS B 1 59  ? 30.97117 32.58186 15.35527  1.000 20.45661 ? 55  LYS B H    1 
ATOM   2700 H  HA   . LYS B 1 59  ? 28.68126 32.87587 16.57130  1.000 20.43299 ? 55  LYS B HA   1 
ATOM   2701 H  HB2  . LYS B 1 59  ? 28.85823 32.47111 14.26966  1.000 18.85857 ? 55  LYS B HB2  1 
ATOM   2702 H  HB3  . LYS B 1 59  ? 29.25453 30.96603 14.59075  1.000 18.85857 ? 55  LYS B HB3  1 
ATOM   2703 H  HG2  . LYS B 1 59  ? 27.06787 30.95701 13.98058  1.000 19.29111 ? 55  LYS B HG2  1 
ATOM   2704 H  HG3  . LYS B 1 59  ? 27.10419 30.67796 15.54462  1.000 19.29111 ? 55  LYS B HG3  1 
ATOM   2705 H  HD2  . LYS B 1 59  ? 26.49209 32.90200 15.93367  1.000 20.25461 ? 55  LYS B HD2  1 
ATOM   2706 H  HD3  . LYS B 1 59  ? 26.40001 33.13517 14.36441  1.000 20.25461 ? 55  LYS B HD3  1 
ATOM   2707 H  HE2  . LYS B 1 59  ? 24.64317 31.52307 14.28678  1.000 21.99628 ? 55  LYS B HE2  1 
ATOM   2708 H  HE3  . LYS B 1 59  ? 24.68000 31.46531 15.87446  1.000 21.99628 ? 55  LYS B HE3  1 
ATOM   2709 H  HZ1  . LYS B 1 59  ? 23.04879 32.90196 15.14513  1.000 22.97185 ? 55  LYS B HZ1  1 
ATOM   2710 H  HZ2  . LYS B 1 59  ? 24.02614 33.64856 15.91044  1.000 22.97185 ? 55  LYS B HZ2  1 
ATOM   2711 H  HZ3  . LYS B 1 59  ? 24.02506 33.72739 14.46403  1.000 22.97185 ? 55  LYS B HZ3  1 
ATOM   2712 N  N    . GLY B 1 60  ? 30.04573 30.02319 17.13694  1.000 16.66232 ? 56  GLY B N    1 
ATOM   2713 C  CA   . GLY B 1 60  ? 30.26842 29.04332 18.18537  1.000 17.65420 ? 56  GLY B CA   1 
ATOM   2714 C  C    . GLY B 1 60  ? 29.18952 28.00377 18.34779  1.000 17.38868 ? 56  GLY B C    1 
ATOM   2715 O  O    . GLY B 1 60  ? 29.23898 27.22461 19.31150  1.000 18.34859 ? 56  GLY B O    1 
ATOM   2716 H  H    . GLY B 1 60  ? 30.52275 29.89151 16.43357  1.000 20.01951 ? 56  GLY B H    1 
ATOM   2717 H  HA2  . GLY B 1 60  ? 31.09809 28.57674 17.99868  1.000 21.20977 ? 56  GLY B HA2  1 
ATOM   2718 H  HA3  . GLY B 1 60  ? 30.35273 29.51156 19.03067  1.000 21.20977 ? 56  GLY B HA3  1 
ATOM   2719 N  N    . ILE B 1 61  ? 28.21663 27.96154 17.44006  1.000 16.55717 ? 57  ILE B N    1 
ATOM   2720 C  CA   . ILE B 1 61  ? 27.15692 26.96562 17.49019  1.000 15.91085 ? 57  ILE B CA   1 
ATOM   2721 C  C    . ILE B 1 61  ? 27.68118 25.63715 16.98743  1.000 15.43050 ? 57  ILE B C    1 
ATOM   2722 O  O    . ILE B 1 61  ? 28.77280 25.57160 16.41199  1.000 15.26052 ? 57  ILE B O    1 
ATOM   2723 C  CB   . ILE B 1 61  ? 25.90201 27.42761 16.72486  1.000 15.97257 ? 57  ILE B CB   1 
ATOM   2724 C  CG1  . ILE B 1 61  ? 26.14967 27.67845 15.21431  1.000 15.47850 ? 57  ILE B CG1  1 
ATOM   2725 C  CG2  . ILE B 1 61  ? 25.37422 28.69835 17.37930  1.000 16.67904 ? 57  ILE B CG2  1 
ATOM   2726 C  CD1  . ILE B 1 61  ? 26.17831 26.45073 14.30980  1.000 16.03258 ? 57  ILE B CD1  1 
ATOM   2727 H  H    . ILE B 1 61  ? 28.15027 28.50699 16.77849  1.000 19.89333 ? 57  ILE B H    1 
ATOM   2728 H  HA   . ILE B 1 61  ? 26.89377 26.83786 18.41503  1.000 19.11775 ? 57  ILE B HA   1 
ATOM   2729 H  HB   . ILE B 1 61  ? 25.25539 26.70630 16.77480  1.000 19.19181 ? 57  ILE B HB   1 
ATOM   2730 H  HG12 . ILE B 1 61  ? 25.44252 28.25553 14.88598  1.000 18.59893 ? 57  ILE B HG12 1 
ATOM   2731 H  HG13 . ILE B 1 61  ? 27.00843 28.11955 15.12014  1.000 18.59893 ? 57  ILE B HG13 1 
ATOM   2732 H  HG21 . ILE B 1 61  ? 24.52938 28.93822 16.96745  1.000 20.03958 ? 57  ILE B HG21 1 
ATOM   2733 H  HG22 . ILE B 1 61  ? 25.24586 28.53568 18.32691  1.000 20.03958 ? 57  ILE B HG22 1 
ATOM   2734 H  HG23 . ILE B 1 61  ? 26.01923 29.41127 17.25046  1.000 20.03958 ? 57  ILE B HG23 1 
ATOM   2735 H  HD11 . ILE B 1 61  ? 25.99686 26.72622 13.39762  1.000 19.26382 ? 57  ILE B HD11 1 
ATOM   2736 H  HD12 . ILE B 1 61  ? 27.05532 26.03971 14.36295  1.000 19.26382 ? 57  ILE B HD12 1 
ATOM   2737 H  HD13 . ILE B 1 61  ? 25.50056 25.82365 14.60698  1.000 19.26382 ? 57  ILE B HD13 1 
ATOM   2738 N  N    . THR B 1 62  ? 26.90246 24.58546 17.19471  1.000 16.12906 ? 58  THR B N    1 
ATOM   2739 C  CA   . THR B 1 62  ? 27.16757 23.25993 16.65964  1.000 16.10131 ? 58  THR B CA   1 
ATOM   2740 C  C    . THR B 1 62  ? 26.25783 22.96772 15.46871  1.000 14.77869 ? 58  THR B C    1 
ATOM   2741 O  O    . THR B 1 62  ? 25.03832 23.18133 15.52513  1.000 15.05259 ? 58  THR B O    1 
ATOM   2742 C  CB   . THR B 1 62  ? 26.98958 22.21737 17.76112  1.000 18.00585 ? 58  THR B CB   1 
ATOM   2743 O  OG1  . THR B 1 62  ? 27.98488 22.45388 18.76301  1.000 18.97326 ? 58  THR B OG1  1 
ATOM   2744 C  CG2  . THR B 1 62  ? 27.13931 20.80521 17.22904  1.000 19.28916 ? 58  THR B CG2  1 
ATOM   2745 H  H    . THR B 1 62  ? 26.18234 24.61808 17.66372  1.000 19.37960 ? 58  THR B H    1 
ATOM   2746 H  HA   . THR B 1 62  ? 28.07798 23.21308 16.32820  1.000 19.34630 ? 58  THR B HA   1 
ATOM   2747 H  HB   . THR B 1 62  ? 26.09748 22.28781 18.13541  1.000 21.63175 ? 58  THR B HB   1 
ATOM   2748 H  HG1  . THR B 1 62  ? 27.88808 21.91215 19.39765  1.000 22.79264 ? 58  THR B HG1  1 
ATOM   2749 H  HG21 . THR B 1 62  ? 27.39276 20.20504 17.94769  1.000 23.17172 ? 58  THR B HG21 1 
ATOM   2750 H  HG22 . THR B 1 62  ? 26.29980 20.50343 16.84819  1.000 23.17172 ? 58  THR B HG22 1 
ATOM   2751 H  HG23 . THR B 1 62  ? 27.82364 20.78035 16.54204  1.000 23.17172 ? 58  THR B HG23 1 
ATOM   2752 N  N    . TRP B 1 63  ? 26.86208 22.47045 14.39228  1.000 14.62886 ? 59  TRP B N    1 
ATOM   2753 C  CA   . TRP B 1 63  ? 26.11142 22.15919 13.18742  1.000 14.98282 ? 59  TRP B CA   1 
ATOM   2754 C  C    . TRP B 1 63  ? 25.28215 20.89610 13.39460  1.000 15.95275 ? 59  TRP B C    1 
ATOM   2755 O  O    . TRP B 1 63  ? 25.79644 19.85800 13.82182  1.000 17.28215 ? 59  TRP B O    1 
ATOM   2756 C  CB   . TRP B 1 63  ? 27.05697 22.03568 11.98786  1.000 14.38515 ? 59  TRP B CB   1 
ATOM   2757 C  CG   . TRP B 1 63  ? 27.68133 23.35222 11.61327  1.000 15.13305 ? 59  TRP B CG   1 
ATOM   2758 C  CD1  . TRP B 1 63  ? 29.00562 23.65093 11.60492  1.000 15.18913 ? 59  TRP B CD1  1 
ATOM   2759 C  CD2  . TRP B 1 63  ? 27.00360 24.54168 11.19834  1.000 13.45845 ? 59  TRP B CD2  1 
ATOM   2760 N  NE1  . TRP B 1 63  ? 29.20435 24.95066 11.20322  1.000 14.85067 ? 59  TRP B NE1  1 
ATOM   2761 C  CE2  . TRP B 1 63  ? 27.98412 25.51425 10.93464  1.000 14.36523 ? 59  TRP B CE2  1 
ATOM   2762 C  CE3  . TRP B 1 63  ? 25.65243 24.86933 10.99183  1.000 14.22128 ? 59  TRP B CE3  1 
ATOM   2763 C  CZ2  . TRP B 1 63  ? 27.66412 26.79658 10.53264  1.000 14.31085 ? 59  TRP B CZ2  1 
ATOM   2764 C  CZ3  . TRP B 1 63  ? 25.34265 26.13769 10.59584  1.000 13.84901 ? 59  TRP B CZ3  1 
ATOM   2765 C  CH2  . TRP B 1 63  ? 26.33723 27.08471 10.33940  1.000 14.70389 ? 59  TRP B CH2  1 
ATOM   2766 H  H    . TRP B 1 63  ? 27.70415 22.30509 14.33598  1.000 17.57936 ? 59  TRP B H    1 
ATOM   2767 H  HA   . TRP B 1 63  ? 25.49276 22.87894 12.98712  1.000 18.00411 ? 59  TRP B HA   1 
ATOM   2768 H  HB2  . TRP B 1 63  ? 27.76949 21.41539 12.20800  1.000 17.28691 ? 59  TRP B HB2  1 
ATOM   2769 H  HB3  . TRP B 1 63  ? 26.55790 21.70963 11.22267  1.000 17.28691 ? 59  TRP B HB3  1 
ATOM   2770 H  HD1  . TRP B 1 63  ? 29.68380 23.05892 11.83837  1.000 18.25168 ? 59  TRP B HD1  1 
ATOM   2771 H  HE1  . TRP B 1 63  ? 29.96594 25.34382 11.13239  1.000 17.84553 ? 59  TRP B HE1  1 
ATOM   2772 H  HE3  . TRP B 1 63  ? 24.98439 24.23560 11.12222  1.000 17.09026 ? 59  TRP B HE3  1 
ATOM   2773 H  HZ2  . TRP B 1 63  ? 28.32269 27.43934 10.39831  1.000 17.19775 ? 59  TRP B HZ2  1 
ATOM   2774 H  HZ3  . TRP B 1 63  ? 24.44974 26.37712 10.49440  1.000 16.64354 ? 59  TRP B HZ3  1 
ATOM   2775 H  HH2  . TRP B 1 63  ? 26.09453 27.92795 10.03128  1.000 17.66940 ? 59  TRP B HH2  1 
ATOM   2776 N  N    . ASN B 1 64  ? 23.98585 21.00355 13.10540  1.000 15.55810 ? 60  ASN B N    1 
ATOM   2777 C  CA   . ASN B 1 64  ? 23.04146 19.89345 13.15020  1.000 16.74061 ? 60  ASN B CA   1 
ATOM   2778 C  C    . ASN B 1 64  ? 21.90966 20.25152 12.18836  1.000 16.89206 ? 60  ASN B C    1 
ATOM   2779 O  O    . ASN B 1 64  ? 21.96700 21.27457 11.50818  1.000 16.53345 ? 60  ASN B O    1 
ATOM   2780 C  CB   . ASN B 1 64  ? 22.56730 19.63213 14.58875  1.000 19.36182 ? 60  ASN B CB   1 
ATOM   2781 C  CG   . ASN B 1 64  ? 21.90924 20.84614 15.21848  1.000 18.87771 ? 60  ASN B CG   1 
ATOM   2782 O  OD1  . ASN B 1 64  ? 21.06679 21.49105 14.62303  1.000 18.28293 ? 60  ASN B OD1  1 
ATOM   2783 N  ND2  . ASN B 1 64  ? 22.30464 21.16750 16.44192  1.000 23.31258 ? 60  ASN B ND2  1 
ATOM   2784 H  H    . ASN B 1 64  ? 23.61534 21.74319 12.87033  1.000 18.69444 ? 60  ASN B H    1 
ATOM   2785 H  HA   . ASN B 1 64  ? 23.46728 19.07686 12.84563  1.000 20.11346 ? 60  ASN B HA   1 
ATOM   2786 H  HB2  . ASN B 1 64  ? 21.92016 18.90958 14.58212  1.000 23.25891 ? 60  ASN B HB2  1 
ATOM   2787 H  HB3  . ASN B 1 64  ? 23.33139 19.38816 15.13422  1.000 23.25891 ? 60  ASN B HB3  1 
ATOM   2788 H  HD21 . ASN B 1 64  ? 21.96057 21.84759 16.84028  1.000 27.99983 ? 60  ASN B HD21 1 
ATOM   2789 H  HD22 . ASN B 1 64  ? 22.90530 20.69594 16.83746  1.000 27.99983 ? 60  ASN B HD22 1 
ATOM   2790 N  N    A GLU B 1 65  ? 20.86338 19.42383 12.15004  0.463 17.37006 ? 61  GLU B N    1 
ATOM   2791 N  N    B GLU B 1 65  ? 20.86442 19.42341 12.14630  0.537 17.04906 ? 61  GLU B N    1 
ATOM   2792 C  CA   A GLU B 1 65  ? 19.78079 19.65498 11.19740  0.463 17.62946 ? 61  GLU B CA   1 
ATOM   2793 C  CA   B GLU B 1 65  ? 19.78266 19.65720 11.19321  0.537 17.16410 ? 61  GLU B CA   1 
ATOM   2794 C  C    A GLU B 1 65  ? 19.13439 21.01812 11.41398  0.463 17.54950 ? 61  GLU B C    1 
ATOM   2795 C  C    B GLU B 1 65  ? 19.12565 21.01413 11.41428  0.537 17.63344 ? 61  GLU B C    1 
ATOM   2796 O  O    A GLU B 1 65  ? 18.87903 21.75541 10.45300  0.463 17.89440 ? 61  GLU B O    1 
ATOM   2797 O  O    B GLU B 1 65  ? 18.84687 21.74079 10.45003  0.537 18.12764 ? 61  GLU B O    1 
ATOM   2798 C  CB   A GLU B 1 65  ? 18.73830 18.54343 11.29695  0.463 21.64753 ? 61  GLU B CB   1 
ATOM   2799 C  CB   B GLU B 1 65  ? 18.74448 18.54288 11.29224  0.537 21.31662 ? 61  GLU B CB   1 
ATOM   2800 C  CG   A GLU B 1 65  ? 19.23185 17.16421 10.87837  0.463 27.05840 ? 61  GLU B CG   1 
ATOM   2801 C  CG   B GLU B 1 65  ? 19.26590 17.16417 10.91862  0.537 27.18173 ? 61  GLU B CG   1 
ATOM   2802 C  CD   A GLU B 1 65  ? 18.20975 16.06977 11.13530  0.463 31.15942 ? 61  GLU B CD   1 
ATOM   2803 C  CD   B GLU B 1 65  ? 19.67483 16.32673 12.11969  0.537 30.65312 ? 61  GLU B CD   1 
ATOM   2804 O  OE1  A GLU B 1 65  ? 17.32005 16.27456 11.98812  0.463 34.96587 ? 61  GLU B OE1  1 
ATOM   2805 O  OE1  B GLU B 1 65  ? 20.26015 16.86718 13.09023  0.537 30.57255 ? 61  GLU B OE1  1 
ATOM   2806 O  OE2  A GLU B 1 65  ? 18.29541 15.00982 10.47900  0.463 31.89575 ? 61  GLU B OE2  1 
ATOM   2807 O  OE2  B GLU B 1 65  ? 19.40163 15.11191 12.08223  0.537 33.65700 ? 61  GLU B OE2  1 
ATOM   2808 H  H    A GLU B 1 65  ? 20.75753 18.73509 12.65406  0.463 20.86880 ? 61  GLU B H    1 
ATOM   2809 H  H    B GLU B 1 65  ? 20.75812 18.73280 12.64765  0.537 20.48360 ? 61  GLU B H    1 
ATOM   2810 H  HA   A GLU B 1 65  ? 20.15251 19.63672 10.30164  0.463 21.18008 ? 61  GLU B HA   1 
ATOM   2811 H  HA   B GLU B 1 65  ? 20.15527 19.64667 10.29769  0.537 20.62165 ? 61  GLU B HA   1 
ATOM   2812 H  HB2  A GLU B 1 65  ? 18.44317 18.48011 12.21879  0.463 26.00177 ? 61  GLU B HB2  1 
ATOM   2813 H  HB2  B GLU B 1 65  ? 18.42521 18.49790 12.20709  0.537 25.60467 ? 61  GLU B HB2  1 
ATOM   2814 H  HB3  A GLU B 1 65  ? 17.98968 18.77153 10.72386  0.463 26.00177 ? 61  GLU B HB3  1 
ATOM   2815 H  HB3  B GLU B 1 65  ? 18.00957 18.75069 10.69422  0.537 25.60467 ? 61  GLU B HB3  1 
ATOM   2816 H  HG2  A GLU B 1 65  ? 19.42827 17.17385 9.92852   0.463 32.49481 ? 61  GLU B HG2  1 
ATOM   2817 H  HG2  B GLU B 1 65  ? 18.56944 16.68345 10.44453  0.537 32.64281 ? 61  GLU B HG2  1 
ATOM   2818 H  HG3  A GLU B 1 65  ? 20.03340 16.94965 11.38075  0.463 32.49481 ? 61  GLU B HG3  1 
ATOM   2819 H  HG3  B GLU B 1 65  ? 20.04446 17.26711 10.34929  0.537 32.64281 ? 61  GLU B HG3  1 
ATOM   2820 N  N    . ASP B 1 66  ? 18.85861 21.36816 12.67620  1.000 17.14742 ? 62  ASP B N    1 
ATOM   2821 C  CA   . ASP B 1 66  ? 18.20045 22.63733 12.97744  1.000 17.62543 ? 62  ASP B CA   1 
ATOM   2822 C  C    . ASP B 1 66  ? 19.06479 23.82644 12.59324  1.000 16.40949 ? 62  ASP B C    1 
ATOM   2823 O  O    . ASP B 1 66  ? 18.58972 24.77304 11.95593  1.000 16.92301 ? 62  ASP B O    1 
ATOM   2824 C  CB   . ASP B 1 66  ? 17.86068 22.71919 14.46429  1.000 19.30346 ? 62  ASP B CB   1 
ATOM   2825 C  CG   . ASP B 1 66  ? 16.74050 21.78528 14.87850  1.000 24.58466 ? 62  ASP B CG   1 
ATOM   2826 O  OD1  . ASP B 1 66  ? 15.65860 21.79230 14.26575  1.000 26.37711 ? 62  ASP B OD1  1 
ATOM   2827 O  OD2  . ASP B 1 66  ? 16.94009 21.07340 15.88069  1.000 30.97502 ? 62  ASP B OD2  1 
ATOM   2828 H  H    . ASP B 1 66  ? 19.04664 20.89550 13.36962  1.000 20.60164 ? 62  ASP B H    1 
ATOM   2829 H  HA   . ASP B 1 66  ? 17.37928 22.67179 12.46228  1.000 21.17525 ? 62  ASP B HA   1 
ATOM   2830 H  HB2  . ASP B 1 66  ? 18.64857 22.48501 14.97936  1.000 23.18888 ? 62  ASP B HB2  1 
ATOM   2831 H  HB3  . ASP B 1 66  ? 17.58480 23.62529 14.67349  1.000 23.18888 ? 62  ASP B HB3  1 
ATOM   2832 N  N    . THR B 1 67  ? 20.33079 23.82435 13.01606  1.000 15.34418 ? 63  THR B N    1 
ATOM   2833 C  CA   . THR B 1 67  ? 21.17328 24.99213 12.76747  1.000 14.57896 ? 63  THR B CA   1 
ATOM   2834 C  C    . THR B 1 67  ? 21.49993 25.11913 11.28257  1.000 13.74420 ? 63  THR B C    1 
ATOM   2835 O  O    . THR B 1 67  ? 21.55369 26.23294 10.76001  1.000 15.07621 ? 63  THR B O    1 
ATOM   2836 C  CB   . THR B 1 67  ? 22.43829 24.98273 13.64351  1.000 14.58413 ? 63  THR B CB   1 
ATOM   2837 O  OG1  . THR B 1 67  ? 23.17251 23.78315 13.42388  1.000 15.17386 ? 63  THR B OG1  1 
ATOM   2838 C  CG2  . THR B 1 67  ? 22.08359 25.11776 15.11430  1.000 15.29839 ? 63  THR B CG2  1 
ATOM   2839 H  H    . THR B 1 67  ? 20.71570 23.18025 13.43627  1.000 18.43775 ? 63  THR B H    1 
ATOM   2840 H  HA   . THR B 1 67  ? 20.68353 25.78632 13.03262  1.000 17.51948 ? 63  THR B HA   1 
ATOM   2841 H  HB   . THR B 1 67  ? 22.99656 25.73947 13.40567  1.000 17.52568 ? 63  THR B HB   1 
ATOM   2842 H  HG1  . THR B 1 67  ? 23.72372 23.66557 14.04673  1.000 18.23336 ? 63  THR B HG1  1 
ATOM   2843 H  HG21 . THR B 1 67  ? 22.88601 25.05761 15.65597  1.000 18.38279 ? 63  THR B HG21 1 
ATOM   2844 H  HG22 . THR B 1 67  ? 21.65831 25.97450 15.27571  1.000 18.38279 ? 63  THR B HG22 1 
ATOM   2845 H  HG23 . THR B 1 67  ? 21.47402 24.40966 15.37493  1.000 18.38279 ? 63  THR B HG23 1 
ATOM   2846 N  N    . LEU B 1 68  ? 21.70041 23.99596 10.58579  1.000 13.47284 ? 64  LEU B N    1 
ATOM   2847 C  CA   . LEU B 1 68  ? 21.90838 24.06221 9.13615   1.000 13.69557 ? 64  LEU B CA   1 
ATOM   2848 C  C    . LEU B 1 68  ? 20.66540 24.58995 8.41779   1.000 14.24892 ? 64  LEU B C    1 
ATOM   2849 O  O    . LEU B 1 68  ? 20.77394 25.37218 7.46252   1.000 14.25894 ? 64  LEU B O    1 
ATOM   2850 C  CB   . LEU B 1 68  ? 22.26466 22.68254 8.58896   1.000 14.83172 ? 64  LEU B CB   1 
ATOM   2851 C  CG   . LEU B 1 68  ? 23.68643 22.20494 8.91923   1.000 15.19452 ? 64  LEU B CG   1 
ATOM   2852 C  CD1  . LEU B 1 68  ? 23.82726 20.70518 8.65917   1.000 17.28735 ? 64  LEU B CD1  1 
ATOM   2853 C  CD2  . LEU B 1 68  ? 24.75079 23.00582 8.14860   1.000 15.33567 ? 64  LEU B CD2  1 
ATOM   2854 H  H    . LEU B 1 68  ? 21.72063 23.20254 10.91698  1.000 16.19214 ? 64  LEU B H    1 
ATOM   2855 H  HA   . LEU B 1 68  ? 22.64797 24.66584 8.96432   1.000 16.45942 ? 64  LEU B HA   1 
ATOM   2856 H  HB2  . LEU B 1 68  ? 21.64524 22.03542 8.96106   1.000 17.82280 ? 64  LEU B HB2  1 
ATOM   2857 H  HB3  . LEU B 1 68  ? 22.18086 22.70450 7.62283   1.000 17.82280 ? 64  LEU B HB3  1 
ATOM   2858 H  HG   . LEU B 1 68  ? 23.84734 22.36064 9.86303   1.000 18.25815 ? 64  LEU B HG   1 
ATOM   2859 H  HD11 . LEU B 1 68  ? 24.75882 20.45360 8.75822   1.000 20.76955 ? 64  LEU B HD11 1 
ATOM   2860 H  HD12 . LEU B 1 68  ? 23.28390 20.22107 9.30049   1.000 20.76955 ? 64  LEU B HD12 1 
ATOM   2861 H  HD13 . LEU B 1 68  ? 23.52635 20.51137 7.75762   1.000 20.76955 ? 64  LEU B HD13 1 
ATOM   2862 H  HD21 . LEU B 1 68  ? 25.62551 22.63112 8.33668   1.000 18.42753 ? 64  LEU B HD21 1 
ATOM   2863 H  HD22 . LEU B 1 68  ? 24.56334 22.94769 7.19866   1.000 18.42753 ? 64  LEU B HD22 1 
ATOM   2864 H  HD23 . LEU B 1 68  ? 24.71880 23.93171 8.43602   1.000 18.42753 ? 64  LEU B HD23 1 
ATOM   2865 N  N    . PHE B 1 69  ? 19.47631 24.19377 8.87624   1.000 13.92936 ? 65  PHE B N    1 
ATOM   2866 C  CA   . PHE B 1 69  ? 18.25303 24.63647 8.21619   1.000 14.85400 ? 65  PHE B CA   1 
ATOM   2867 C  C    . PHE B 1 69  ? 18.09832 26.14620 8.31505   1.000 15.29432 ? 65  PHE B C    1 
ATOM   2868 O  O    . PHE B 1 69  ? 17.70940 26.80633 7.33798   1.000 16.29618 ? 65  PHE B O    1 
ATOM   2869 C  CB   . PHE B 1 69  ? 17.06196 23.89829 8.83062   1.000 16.20775 ? 65  PHE B CB   1 
ATOM   2870 C  CG   . PHE B 1 69  ? 15.74097 24.17851 8.15425   1.000 16.79499 ? 65  PHE B CG   1 
ATOM   2871 C  CD1  . PHE B 1 69  ? 15.42614 23.61580 6.92320   1.000 16.81018 ? 65  PHE B CD1  1 
ATOM   2872 C  CD2  . PHE B 1 69  ? 14.79221 24.97413 8.77454   1.000 17.35739 ? 65  PHE B CD2  1 
ATOM   2873 C  CE1  . PHE B 1 69  ? 14.19910 23.87154 6.29703   1.000 17.75011 ? 65  PHE B CE1  1 
ATOM   2874 C  CE2  . PHE B 1 69  ? 13.55831 25.23288 8.15062   1.000 18.80744 ? 65  PHE B CE2  1 
ATOM   2875 C  CZ   . PHE B 1 69  ? 13.25964 24.67423 6.91356   1.000 18.25292 ? 65  PHE B CZ   1 
ATOM   2876 H  H    . PHE B 1 69  ? 19.35232 23.67913 9.55401   1.000 16.73996 ? 65  PHE B H    1 
ATOM   2877 H  HA   . PHE B 1 69  ? 18.28241 24.41684 7.27184   1.000 17.84953 ? 65  PHE B HA   1 
ATOM   2878 H  HB2  . PHE B 1 69  ? 17.22531 22.94393 8.77210   1.000 19.47402 ? 65  PHE B HB2  1 
ATOM   2879 H  HB3  . PHE B 1 69  ? 16.97849 24.16423 9.75971   1.000 19.47402 ? 65  PHE B HB3  1 
ATOM   2880 H  HD1  . PHE B 1 69  ? 16.04261 23.05800 6.50641   1.000 20.19694 ? 65  PHE B HD1  1 
ATOM   2881 H  HD2  . PHE B 1 69  ? 14.97230 25.34027 9.61025   1.000 20.85360 ? 65  PHE B HD2  1 
ATOM   2882 H  HE1  . PHE B 1 69  ? 14.01689 23.49983 5.46424   1.000 21.32486 ? 65  PHE B HE1  1 
ATOM   2883 H  HE2  . PHE B 1 69  ? 12.93655 25.78294 8.56984   1.000 22.59365 ? 65  PHE B HE2  1 
ATOM   2884 H  HZ   . PHE B 1 69  ? 12.43945 24.83851 6.50711   1.000 21.92824 ? 65  PHE B HZ   1 
ATOM   2885 N  N    . GLU B 1 70  ? 18.43742 26.71699 9.47389   1.000 15.29418 ? 66  GLU B N    1 
ATOM   2886 C  CA   . GLU B 1 70  ? 18.36877 28.15731 9.66073   1.000 15.36683 ? 66  GLU B CA   1 
ATOM   2887 C  C    . GLU B 1 70  ? 19.47008 28.87525 8.88467   1.000 15.69092 ? 66  GLU B C    1 
ATOM   2888 O  O    . GLU B 1 70  ? 19.20737 29.85293 8.17505   1.000 17.03078 ? 66  GLU B O    1 
ATOM   2889 C  CB   . GLU B 1 70  ? 18.44127 28.46288 11.15540  1.000 17.52049 ? 66  GLU B CB   1 
ATOM   2890 C  CG   . GLU B 1 70  ? 18.33446 29.93525 11.48899  1.000 21.77023 ? 66  GLU B CG   1 
ATOM   2891 C  CD   . GLU B 1 70  ? 18.26524 30.22240 12.98680  1.000 26.28578 ? 66  GLU B CD   1 
ATOM   2892 O  OE1  . GLU B 1 70  ? 18.20232 29.27317 13.79627  1.000 27.50294 ? 66  GLU B OE1  1 
ATOM   2893 O  OE2  . GLU B 1 70  ? 18.29679 31.41029 13.34847  1.000 27.83171 ? 66  GLU B OE2  1 
ATOM   2894 H  H    . GLU B 1 70  ? 18.71092 26.28913 10.16796  1.000 18.37774 ? 66  GLU B H    1 
ATOM   2895 H  HA   . GLU B 1 70  ? 17.52459 28.49230 9.32011   1.000 18.46493 ? 66  GLU B HA   1 
ATOM   2896 H  HB2  . GLU B 1 70  ? 17.71161 28.00553 11.60187  1.000 21.04932 ? 66  GLU B HB2  1 
ATOM   2897 H  HB3  . GLU B 1 70  ? 19.29126 28.14388 11.49696  1.000 21.04932 ? 66  GLU B HB3  1 
ATOM   2898 H  HG2  . GLU B 1 70  ? 19.11340 30.39285 11.13578  1.000 26.14901 ? 66  GLU B HG2  1 
ATOM   2899 H  HG3  . GLU B 1 70  ? 17.52848 30.29001 11.08224  1.000 26.14901 ? 66  GLU B HG3  1 
ATOM   2900 N  N    . TYR B 1 71  ? 20.70025 28.39002 8.99570   1.000 14.54363 ? 67  TYR B N    1 
ATOM   2901 C  CA   . TYR B 1 71  ? 21.83032 29.02499 8.31959   1.000 14.89861 ? 67  TYR B CA   1 
ATOM   2902 C  C    . TYR B 1 71  ? 21.62128 29.09156 6.82101   1.000 15.59067 ? 67  TYR B C    1 
ATOM   2903 O  O    . TYR B 1 71  ? 21.83590 30.13924 6.20129   1.000 16.84798 ? 67  TYR B O    1 
ATOM   2904 C  CB   . TYR B 1 71  ? 23.08928 28.21937 8.61725   1.000 14.66746 ? 67  TYR B CB   1 
ATOM   2905 C  CG   . TYR B 1 71  ? 24.35088 28.65575 7.90411   1.000 14.11283 ? 67  TYR B CG   1 
ATOM   2906 C  CD1  . TYR B 1 71  ? 24.88855 29.91952 8.11288   1.000 15.11131 ? 67  TYR B CD1  1 
ATOM   2907 C  CD2  . TYR B 1 71  ? 25.04988 27.78047 7.08554   1.000 15.82998 ? 67  TYR B CD2  1 
ATOM   2908 C  CE1  . TYR B 1 71  ? 26.05862 30.31307 7.51759   1.000 16.48121 ? 67  TYR B CE1  1 
ATOM   2909 C  CE2  . TYR B 1 71  ? 26.26318 28.16373 6.46812   1.000 16.08455 ? 67  TYR B CE2  1 
ATOM   2910 C  CZ   . TYR B 1 71  ? 26.76288 29.44381 6.71215   1.000 15.75978 ? 67  TYR B CZ   1 
ATOM   2911 O  OH   . TYR B 1 71  ? 27.94945 29.87916 6.14571   1.000 17.48394 ? 67  TYR B OH   1 
ATOM   2912 H  H    . TYR B 1 71  ? 20.91323 27.69481 9.45497   1.000 17.47708 ? 67  TYR B H    1 
ATOM   2913 H  HA   . TYR B 1 71  ? 21.92547 29.93149 8.65142   1.000 17.90306 ? 67  TYR B HA   1 
ATOM   2914 H  HB2  . TYR B 1 71  ? 23.26595 28.27655 9.56931   1.000 17.62568 ? 67  TYR B HB2  1 
ATOM   2915 H  HB3  . TYR B 1 71  ? 22.92404 27.29736 8.36527   1.000 17.62568 ? 67  TYR B HB3  1 
ATOM   2916 H  HD1  . TYR B 1 71  ? 24.44260 30.51443 8.67154   1.000 18.15830 ? 67  TYR B HD1  1 
ATOM   2917 H  HD2  . TYR B 1 71  ? 24.71422 26.92545 6.94006   1.000 19.02070 ? 67  TYR B HD2  1 
ATOM   2918 H  HE1  . TYR B 1 71  ? 26.38034 31.17423 7.65826   1.000 19.80218 ? 67  TYR B HE1  1 
ATOM   2919 H  HE2  . TYR B 1 71  ? 26.71874 27.57479 5.91088   1.000 19.32618 ? 67  TYR B HE2  1 
ATOM   2920 H  HH   . TYR B 1 71  ? 28.31493 29.25032 5.72550   1.000 21.00546 ? 67  TYR B HH   1 
ATOM   2921 N  N    . LEU B 1 72  ? 21.25563 27.96318 6.21698   1.000 14.80351 ? 68  LEU B N    1 
ATOM   2922 C  CA   . LEU B 1 72  ? 21.25705 27.89185 4.75941   1.000 15.52997 ? 68  LEU B CA   1 
ATOM   2923 C  C    . LEU B 1 72  ? 20.17359 28.75401 4.13044   1.000 16.94862 ? 68  LEU B C    1 
ATOM   2924 O  O    . LEU B 1 72  ? 20.26984 29.06385 2.93778   1.000 19.54463 ? 68  LEU B O    1 
ATOM   2925 C  CB   . LEU B 1 72  ? 21.18433 26.43401 4.31825   1.000 16.11018 ? 68  LEU B CB   1 
ATOM   2926 C  CG   . LEU B 1 72  ? 22.41231 25.59078 4.68103   1.000 15.62160 ? 68  LEU B CG   1 
ATOM   2927 C  CD1  . LEU B 1 72  ? 22.12214 24.13616 4.38996   1.000 18.01577 ? 68  LEU B CD1  1 
ATOM   2928 C  CD2  . LEU B 1 72  ? 23.67947 26.05368 3.94314   1.000 18.23316 ? 68  LEU B CD2  1 
ATOM   2929 H  H    . LEU B 1 72  ? 21.00861 27.24279 6.61649   1.000 17.78894 ? 68  LEU B H    1 
ATOM   2930 H  HA   . LEU B 1 72  ? 22.09416 28.23851 4.41303   1.000 18.66070 ? 68  LEU B HA   1 
ATOM   2931 H  HB2  . LEU B 1 72  ? 20.41299 26.02369 4.73962   1.000 19.35694 ? 68  LEU B HB2  1 
ATOM   2932 H  HB3  . LEU B 1 72  ? 21.08747 26.40953 3.35341   1.000 19.35694 ? 68  LEU B HB3  1 
ATOM   2933 H  HG   . LEU B 1 72  ? 22.59603 25.70049 5.62714   1.000 18.77065 ? 68  LEU B HG   1 
ATOM   2934 H  HD11 . LEU B 1 72  ? 22.83832 23.59235 4.75364   1.000 21.64365 ? 68  LEU B HD11 1 
ATOM   2935 H  HD12 . LEU B 1 72  ? 21.27934 23.89323 4.80417   1.000 21.64365 ? 68  LEU B HD12 1 
ATOM   2936 H  HD13 . LEU B 1 72  ? 22.06689 24.01118 3.42963   1.000 21.64365 ? 68  LEU B HD13 1 
ATOM   2937 H  HD21 . LEU B 1 72  ? 24.37034 25.38116 4.04957   1.000 21.90452 ? 68  LEU B HD21 1 
ATOM   2938 H  HD22 . LEU B 1 72  ? 23.47267 26.16947 3.00255   1.000 21.90452 ? 68  LEU B HD22 1 
ATOM   2939 H  HD23 . LEU B 1 72  ? 23.97615 26.89560 4.32268   1.000 21.90452 ? 68  LEU B HD23 1 
ATOM   2940 N  N    A GLU B 1 73  ? 19.15376 29.14793 4.89394   0.363 17.92157 ? 69  GLU B N    1 
ATOM   2941 N  N    B GLU B 1 73  ? 19.17142 29.16788 4.90682   0.637 18.61203 ? 69  GLU B N    1 
ATOM   2942 C  CA   A GLU B 1 73  ? 18.14941 30.06758 4.37084   0.363 19.16517 ? 69  GLU B CA   1 
ATOM   2943 C  CA   B GLU B 1 73  ? 18.13172 30.05722 4.40045   0.637 20.79120 ? 69  GLU B CA   1 
ATOM   2944 C  C    A GLU B 1 73  ? 18.76021 31.42579 4.06305   0.363 20.48374 ? 69  GLU B C    1 
ATOM   2945 C  C    B GLU B 1 73  ? 18.66488 31.46169 4.14640   0.637 21.08091 ? 69  GLU B C    1 
ATOM   2946 O  O    A GLU B 1 73  ? 18.41970 32.05541 3.05413   0.363 22.43129 ? 69  GLU B O    1 
ATOM   2947 O  O    B GLU B 1 73  ? 18.16185 32.16206 3.25729   0.637 22.19186 ? 69  GLU B O    1 
ATOM   2948 C  CB   A GLU B 1 73  ? 17.02341 30.22957 5.39065   0.363 19.36733 ? 69  GLU B CB   1 
ATOM   2949 C  CB   B GLU B 1 73  ? 16.99592 30.11648 5.42205   0.637 22.85631 ? 69  GLU B CB   1 
ATOM   2950 C  CG   A GLU B 1 73  ? 15.87279 31.11949 4.92865   0.363 20.59823 ? 69  GLU B CG   1 
ATOM   2951 C  CG   B GLU B 1 73  ? 15.65777 30.63516 4.87892   0.637 25.87477 ? 69  GLU B CG   1 
ATOM   2952 C  CD   A GLU B 1 73  ? 14.70505 31.09909 5.89535   0.363 23.45858 ? 69  GLU B CD   1 
ATOM   2953 C  CD   B GLU B 1 73  ? 15.55768 32.15156 4.82970   0.637 28.78946 ? 69  GLU B CD   1 
ATOM   2954 O  OE1  A GLU B 1 73  ? 14.93131 30.87859 7.10482   0.363 26.15688 ? 69  GLU B OE1  1 
ATOM   2955 O  OE1  B GLU B 1 73  ? 16.30444 32.83109 5.55868   0.637 30.19600 ? 69  GLU B OE1  1 
ATOM   2956 O  OE2  A GLU B 1 73  ? 13.55679 31.29542 5.44311   0.363 24.98524 ? 69  GLU B OE2  1 
ATOM   2957 O  OE2  B GLU B 1 73  ? 14.71358 32.67080 4.06670   0.637 31.29784 ? 69  GLU B OE2  1 
ATOM   2958 H  H    A GLU B 1 73  ? 19.02114 28.90145 5.70712   0.363 21.53061 ? 69  GLU B H    1 
ATOM   2959 H  H    B GLU B 1 73  ? 19.06916 28.94854 5.73207   0.637 22.35917 ? 69  GLU B H    1 
ATOM   2960 H  HA   A GLU B 1 73  ? 17.78233 29.70021 3.55157   0.363 23.02293 ? 69  GLU B HA   1 
ATOM   2961 H  HA   B GLU B 1 73  ? 17.79334 29.70969 3.56044   0.637 24.97417 ? 69  GLU B HA   1 
ATOM   2962 H  HB2  A GLU B 1 73  ? 16.65568 29.35356 5.58630   0.363 23.26552 ? 69  GLU B HB2  1 
ATOM   2963 H  HB2  B GLU B 1 73  ? 16.84343 29.22132 5.76313   0.637 27.45230 ? 69  GLU B HB2  1 
ATOM   2964 H  HB3  A GLU B 1 73  ? 17.39172 30.62250 6.19741   0.363 23.26552 ? 69  GLU B HB3  1 
ATOM   2965 H  HB3  B GLU B 1 73  ? 17.26394 30.70560 6.14455   0.637 27.45230 ? 69  GLU B HB3  1 
ATOM   2966 H  HG2  A GLU B 1 73  ? 16.18797 32.03393 4.85538   0.363 24.74260 ? 69  GLU B HG2  1 
ATOM   2967 H  HG2  B GLU B 1 73  ? 15.53815 30.30231 3.97571   0.637 31.07446 ? 69  GLU B HG2  1 
ATOM   2968 H  HG3  A GLU B 1 73  ? 15.55627 30.80758 4.06643   0.363 24.74260 ? 69  GLU B HG3  1 
ATOM   2969 H  HG3  B GLU B 1 73  ? 14.94336 30.31089 5.44933   0.637 31.07446 ? 69  GLU B HG3  1 
ATOM   2970 N  N    . ASN B 1 74  ? 19.65351 31.89754 4.92601   1.000 19.95201 ? 70  ASN B N    1 
ATOM   2971 C  CA   . ASN B 1 74  ? 20.20714 33.24139 4.81771   1.000 19.46920 ? 70  ASN B CA   1 
ATOM   2972 C  C    . ASN B 1 74  ? 21.51613 33.24697 5.60973   1.000 18.71011 ? 70  ASN B C    1 
ATOM   2973 O  O    . ASN B 1 74  ? 21.53393 33.60065 6.80195   1.000 19.63546 ? 70  ASN B O    1 
ATOM   2974 C  CB   . ASN B 1 74  ? 19.21473 34.27243 5.37674   1.000 21.21347 ? 70  ASN B CB   1 
ATOM   2975 C  CG   . ASN B 1 74  ? 19.62843 35.70167 5.09304   1.000 22.44014 ? 70  ASN B CG   1 
ATOM   2976 O  OD1  . ASN B 1 74  ? 20.80674 35.98987 4.90469   1.000 25.28528 ? 70  ASN B OD1  1 
ATOM   2977 N  ND2  . ASN B 1 74  ? 18.65958 36.61119 5.07966   1.000 24.26791 ? 70  ASN B ND2  1 
ATOM   2978 H  H    A ASN B 1 74  ? 19.95990 31.45100 5.59408   0.363 23.96714 ? 70  ASN B H    1 
ATOM   2979 H  H    B ASN B 1 74  ? 20.02703 31.42218 5.53766   0.637 23.96714 ? 70  ASN B H    1 
ATOM   2980 H  HA   . ASN B 1 74  ? 20.38024 33.48718 3.89547   1.000 23.38777 ? 70  ASN B HA   1 
ATOM   2981 H  HB2  . ASN B 1 74  ? 18.34572 34.12614 4.97138   1.000 25.48089 ? 70  ASN B HB2  1 
ATOM   2982 H  HB3  . ASN B 1 74  ? 19.15467 34.16341 6.33872   1.000 25.48089 ? 70  ASN B HB3  1 
ATOM   2983 H  HD21 . ASN B 1 74  ? 18.84619 37.43596 4.92302   1.000 29.14622 ? 70  ASN B HD21 1 
ATOM   2984 H  HD22 . ASN B 1 74  ? 17.84600 36.37501 5.22765   1.000 29.14622 ? 70  ASN B HD22 1 
ATOM   2985 N  N    . PRO B 1 75  ? 22.62480 32.82158 4.99696   1.000 18.75681 ? 71  PRO B N    1 
ATOM   2986 C  CA   . PRO B 1 75  ? 23.87887 32.68626 5.76268   1.000 18.81380 ? 71  PRO B CA   1 
ATOM   2987 C  C    . PRO B 1 75  ? 24.33804 33.94807 6.47286   1.000 20.14620 ? 71  PRO B C    1 
ATOM   2988 O  O    . PRO B 1 75  ? 24.72134 33.87076 7.64760   1.000 18.88293 ? 71  PRO B O    1 
ATOM   2989 C  CB   . PRO B 1 75  ? 24.87730 32.20029 4.70482   1.000 19.30366 ? 71  PRO B CB   1 
ATOM   2990 C  CG   . PRO B 1 75  ? 24.01570 31.39704 3.78094   1.000 19.38647 ? 71  PRO B CG   1 
ATOM   2991 C  CD   . PRO B 1 75  ? 22.70966 32.14722 3.69073   1.000 19.13628 ? 71  PRO B CD   1 
ATOM   2992 H  HA   . PRO B 1 75  ? 23.76442 31.99782 6.43637   1.000 22.60129 ? 71  PRO B HA   1 
ATOM   2993 H  HB2  . PRO B 1 75  ? 25.28123 32.95458 4.24789   1.000 23.18912 ? 71  PRO B HB2  1 
ATOM   2994 H  HB3  . PRO B 1 75  ? 25.56564 31.65306 5.11423   1.000 23.18912 ? 71  PRO B HB3  1 
ATOM   2995 H  HG2  . PRO B 1 75  ? 24.43785 31.33415 2.90989   1.000 23.28850 ? 71  PRO B HG2  1 
ATOM   2996 H  HG3  . PRO B 1 75  ? 23.87877 30.50971 4.14808   1.000 23.28850 ? 71  PRO B HG3  1 
ATOM   2997 H  HD2  . PRO B 1 75  ? 22.73067 32.79366 2.96783   1.000 22.98827 ? 71  PRO B HD2  1 
ATOM   2998 H  HD3  . PRO B 1 75  ? 21.96674 31.53583 3.56758   1.000 22.98827 ? 71  PRO B HD3  1 
ATOM   2999 N  N    . LYS B 1 76  ? 24.29635 35.10778 5.81440   1.000 21.27770 ? 72  LYS B N    1 
ATOM   3000 C  CA   . LYS B 1 76  ? 24.78923 36.33153 6.44351   1.000 24.57128 ? 72  LYS B CA   1 
ATOM   3001 C  C    . LYS B 1 76  ? 23.88961 36.81186 7.57536   1.000 23.05860 ? 72  LYS B C    1 
ATOM   3002 O  O    . LYS B 1 76  ? 24.35297 37.55107 8.45023   1.000 23.11163 ? 72  LYS B O    1 
ATOM   3003 C  CB   . LYS B 1 76  ? 24.94828 37.43893 5.40297   1.000 28.06428 ? 72  LYS B CB   1 
ATOM   3004 C  CG   . LYS B 1 76  ? 23.61918 37.91456 4.83143   1.000 31.99426 ? 72  LYS B CG   1 
ATOM   3005 C  CD   . LYS B 1 76  ? 23.78487 38.71715 3.55064   1.000 36.90225 ? 72  LYS B CD   1 
ATOM   3006 C  CE   . LYS B 1 76  ? 22.43571 38.97684 2.87166   1.000 39.85349 ? 72  LYS B CE   1 
ATOM   3007 N  NZ   . LYS B 1 76  ? 21.70298 37.71529 2.50672   1.000 41.98094 ? 72  LYS B NZ   1 
ATOM   3008 H  H    . LYS B 1 76  ? 23.99302 35.21208 5.01645   1.000 25.55797 ? 72  LYS B H    1 
ATOM   3009 H  HA   . LYS B 1 76  ? 25.66470 36.14732 6.81839   1.000 29.51027 ? 72  LYS B HA   1 
ATOM   3010 H  HB2  . LYS B 1 76  ? 25.38523 38.19946 5.81717   1.000 33.70186 ? 72  LYS B HB2  1 
ATOM   3011 H  HB3  . LYS B 1 76  ? 25.48765 37.10574 4.66883   1.000 33.70186 ? 72  LYS B HB3  1 
ATOM   3012 H  HG2  . LYS B 1 76  ? 23.06581 37.14317 4.63235   1.000 38.41784 ? 72  LYS B HG2  1 
ATOM   3013 H  HG3  . LYS B 1 76  ? 23.17774 38.47988 5.48446   1.000 38.41784 ? 72  LYS B HG3  1 
ATOM   3014 H  HD2  . LYS B 1 76  ? 24.19140 39.57305 3.75818   1.000 44.30743 ? 72  LYS B HD2  1 
ATOM   3015 H  HD3  . LYS B 1 76  ? 24.34705 38.22393 2.93291   1.000 44.30743 ? 72  LYS B HD3  1 
ATOM   3016 H  HE2  . LYS B 1 76  ? 21.87190 39.48437 3.47616   1.000 47.84892 ? 72  LYS B HE2  1 
ATOM   3017 H  HE3  . LYS B 1 76  ? 22.58570 39.48050 2.05634   1.000 47.84892 ? 72  LYS B HE3  1 
ATOM   3018 H  HZ1  . LYS B 1 76  ? 21.00555 37.90747 1.98830   1.000 50.40186 ? 72  LYS B HZ1  1 
ATOM   3019 H  HZ2  . LYS B 1 76  ? 22.24624 37.16399 2.06736   1.000 50.40186 ? 72  LYS B HZ2  1 
ATOM   3020 H  HZ3  . LYS B 1 76  ? 21.41221 37.30835 3.24290   1.000 50.40186 ? 72  LYS B HZ3  1 
ATOM   3021 N  N    . LYS B 1 77  ? 22.61523 36.43213 7.58156   1.000 22.54943 ? 73  LYS B N    1 
ATOM   3022 C  CA   . LYS B 1 77  ? 21.77992 36.75960 8.73365   1.000 21.80751 ? 73  LYS B CA   1 
ATOM   3023 C  C    . LYS B 1 77  ? 22.20907 35.95825 9.95521   1.000 20.80541 ? 73  LYS B C    1 
ATOM   3024 O  O    . LYS B 1 77  ? 22.24964 36.48251 11.07576  1.000 23.10161 ? 73  LYS B O    1 
ATOM   3025 C  CB   . LYS B 1 77  ? 20.31668 36.48510 8.39835   1.000 23.81546 ? 73  LYS B CB   1 
ATOM   3026 C  CG   . LYS B 1 77  ? 19.32889 36.90094 9.48837   1.000 27.38120 ? 73  LYS B CG   1 
ATOM   3027 C  CD   . LYS B 1 77  ? 17.89584 36.61862 9.05657   1.000 29.68358 ? 73  LYS B CD   1 
ATOM   3028 C  CE   . LYS B 1 77  ? 16.93297 36.81780 10.20740  1.000 34.07909 ? 73  LYS B CE   1 
ATOM   3029 N  NZ   . LYS B 1 77  ? 15.58793 36.26750 9.89754   1.000 37.95755 ? 73  LYS B NZ   1 
ATOM   3030 H  H    . LYS B 1 77  ? 22.21936 35.99793 6.95359   1.000 27.08404 ? 73  LYS B H    1 
ATOM   3031 H  HA   . LYS B 1 77  ? 21.87104 37.70256 8.94203   1.000 26.19374 ? 73  LYS B HA   1 
ATOM   3032 H  HB2  . LYS B 1 77  ? 20.08720 36.97413 7.59269   1.000 28.60328 ? 73  LYS B HB2  1 
ATOM   3033 H  HB3  . LYS B 1 77  ? 20.20677 35.53268 8.25096   1.000 28.60328 ? 73  LYS B HB3  1 
ATOM   3034 H  HG2  . LYS B 1 77  ? 19.51060 36.39949 10.29857  1.000 32.88217 ? 73  LYS B HG2  1 
ATOM   3035 H  HG3  . LYS B 1 77  ? 19.41700 37.85159 9.65979   1.000 32.88217 ? 73  LYS B HG3  1 
ATOM   3036 H  HD2  . LYS B 1 77  ? 17.64852 37.22503 8.34103   1.000 35.64502 ? 73  LYS B HD2  1 
ATOM   3037 H  HD3  . LYS B 1 77  ? 17.82492 35.70024 8.75251   1.000 35.64502 ? 73  LYS B HD3  1 
ATOM   3038 H  HE2  . LYS B 1 77  ? 17.27429 36.36322 10.99338  1.000 40.91964 ? 73  LYS B HE2  1 
ATOM   3039 H  HE3  . LYS B 1 77  ? 16.83987 37.76646 10.38706  1.000 40.91964 ? 73  LYS B HE3  1 
ATOM   3040 H  HZ1  . LYS B 1 77  ? 15.07022 36.30383 10.62055  1.000 45.57379 ? 73  LYS B HZ1  1 
ATOM   3041 H  HZ2  . LYS B 1 77  ? 15.20815 36.74052 9.24629   1.000 45.57379 ? 73  LYS B HZ2  1 
ATOM   3042 H  HZ3  . LYS B 1 77  ? 15.65881 35.41996 9.63533   1.000 45.57379 ? 73  LYS B HZ3  1 
ATOM   3043 N  N    . TYR B 1 78  ? 22.53122 34.68150 9.75232   1.000 19.70397 ? 74  TYR B N    1 
ATOM   3044 C  CA   . TYR B 1 78  ? 22.91639 33.82097 10.86256  1.000 17.70095 ? 74  TYR B CA   1 
ATOM   3045 C  C    . TYR B 1 78  ? 24.32466 34.13136 11.35894  1.000 18.02192 ? 74  TYR B C    1 
ATOM   3046 O  O    . TYR B 1 78  ? 24.58473 34.07902 12.57113  1.000 19.64829 ? 74  TYR B O    1 
ATOM   3047 C  CB   . TYR B 1 78  ? 22.80412 32.36897 10.42496  1.000 17.54542 ? 74  TYR B CB   1 
ATOM   3048 C  CG   . TYR B 1 78  ? 22.81153 31.32896 11.52315  1.000 17.71840 ? 74  TYR B CG   1 
ATOM   3049 C  CD1  . TYR B 1 78  ? 21.80958 31.28731 12.48622  1.000 17.95849 ? 74  TYR B CD1  1 
ATOM   3050 C  CD2  . TYR B 1 78  ? 23.78945 30.34903 11.55805  1.000 17.59129 ? 74  TYR B CD2  1 
ATOM   3051 C  CE1  . TYR B 1 78  ? 21.79501 30.30220 13.47351  1.000 19.03257 ? 74  TYR B CE1  1 
ATOM   3052 C  CE2  . TYR B 1 78  ? 23.78246 29.36231 12.52237  1.000 17.07195 ? 74  TYR B CE2  1 
ATOM   3053 C  CZ   . TYR B 1 78  ? 22.78343 29.34780 13.48727  1.000 18.21868 ? 74  TYR B CZ   1 
ATOM   3054 O  OH   . TYR B 1 78  ? 22.79285 28.35442 14.43771  1.000 18.20862 ? 74  TYR B OH   1 
ATOM   3055 H  H    . TYR B 1 78  ? 22.53495 34.29070 8.98625   1.000 23.66949 ? 74  TYR B H    1 
ATOM   3056 H  HA   . TYR B 1 78  ? 22.31281 33.97074 11.60698  1.000 21.26586 ? 74  TYR B HA   1 
ATOM   3057 H  HB2  . TYR B 1 78  ? 21.97037 32.26436 9.94038   1.000 21.07923 ? 74  TYR B HB2  1 
ATOM   3058 H  HB3  . TYR B 1 78  ? 23.55375 32.17161 9.84187   1.000 21.07923 ? 74  TYR B HB3  1 
ATOM   3059 H  HD1  . TYR B 1 78  ? 21.13619 31.92859 12.47183  1.000 21.57492 ? 74  TYR B HD1  1 
ATOM   3060 H  HD2  . TYR B 1 78  ? 24.46459 30.35621 10.91849  1.000 21.13427 ? 74  TYR B HD2  1 
ATOM   3061 H  HE1  . TYR B 1 78  ? 21.12289 30.29143 14.11619  1.000 22.86381 ? 74  TYR B HE1  1 
ATOM   3062 H  HE2  . TYR B 1 78  ? 24.44443 28.70910 12.52632  1.000 20.51107 ? 74  TYR B HE2  1 
ATOM   3063 H  HH   . TYR B 1 78  ? 23.38082 27.78416 14.25145  1.000 21.87507 ? 74  TYR B HH   1 
ATOM   3064 N  N    . ILE B 1 79  ? 25.24747 34.42242 10.44181  1.000 18.37155 ? 75  ILE B N    1 
ATOM   3065 C  CA   . ILE B 1 79  ? 26.64145 34.71888 10.77268  1.000 18.24998 ? 75  ILE B CA   1 
ATOM   3066 C  C    . ILE B 1 79  ? 27.01398 36.01314 10.05742  1.000 19.49512 ? 75  ILE B C    1 
ATOM   3067 O  O    . ILE B 1 79  ? 27.62365 35.97264 8.97876   1.000 21.62891 ? 75  ILE B O    1 
ATOM   3068 C  CB   . ILE B 1 79  ? 27.56833 33.54551 10.40465  1.000 18.13128 ? 75  ILE B CB   1 
ATOM   3069 C  CG1  . ILE B 1 79  ? 27.06335 32.24783 11.06491  1.000 18.62042 ? 75  ILE B CG1  1 
ATOM   3070 C  CG2  . ILE B 1 79  ? 29.01961 33.84107 10.85231  1.000 18.88629 ? 75  ILE B CG2  1 
ATOM   3071 C  CD1  . ILE B 1 79  ? 27.93642 31.02184 10.88575  1.000 17.99003 ? 75  ILE B CD1  1 
ATOM   3072 H  H    . ILE B 1 79  ? 25.08587 34.45527 9.59777   1.000 22.07059 ? 75  ILE B H    1 
ATOM   3073 H  HA   . ILE B 1 79  ? 26.74128 34.85992 11.72716  1.000 21.92470 ? 75  ILE B HA   1 
ATOM   3074 H  HB   . ILE B 1 79  ? 27.55727 33.43538 9.44099   1.000 21.78227 ? 75  ILE B HB   1 
ATOM   3075 H  HG12 . ILE B 1 79  ? 26.98413 32.40497 12.01882  1.000 22.36924 ? 75  ILE B HG12 1 
ATOM   3076 H  HG13 . ILE B 1 79  ? 26.19398 32.03644 10.69018  1.000 22.36924 ? 75  ILE B HG13 1 
ATOM   3077 H  HG21 . ILE B 1 79  ? 29.60757 33.16207 10.48602  1.000 22.68828 ? 75  ILE B HG21 1 
ATOM   3078 H  HG22 . ILE B 1 79  ? 29.27949 34.71593 10.52369  1.000 22.68828 ? 75  ILE B HG22 1 
ATOM   3079 H  HG23 . ILE B 1 79  ? 29.06042 33.82620 11.82134  1.000 22.68828 ? 75  ILE B HG23 1 
ATOM   3080 H  HD11 . ILE B 1 79  ? 27.41355 30.22977 11.08607  1.000 21.61277 ? 75  ILE B HD11 1 
ATOM   3081 H  HD12 . ILE B 1 79  ? 28.24931 30.98832 9.96821   1.000 21.61277 ? 75  ILE B HD12 1 
ATOM   3082 H  HD13 . ILE B 1 79  ? 28.69213 31.08112 11.49097  1.000 21.61277 ? 75  ILE B HD13 1 
ATOM   3083 N  N    . PRO B 1 80  ? 26.68094 37.17598 10.61282  1.000 21.96822 ? 76  PRO B N    1 
ATOM   3084 C  CA   . PRO B 1 80  ? 27.03806 38.43307 9.94297   1.000 24.65868 ? 76  PRO B CA   1 
ATOM   3085 C  C    . PRO B 1 80  ? 28.54421 38.56465 9.77846   1.000 26.42816 ? 76  PRO B C    1 
ATOM   3086 O  O    . PRO B 1 80  ? 29.31520 38.32774 10.71170  1.000 27.40512 ? 76  PRO B O    1 
ATOM   3087 C  CB   . PRO B 1 80  ? 26.46565 39.50275 10.87460  1.000 26.91976 ? 76  PRO B CB   1 
ATOM   3088 C  CG   . PRO B 1 80  ? 25.36754 38.81594 11.58476  1.000 25.07275 ? 76  PRO B CG   1 
ATOM   3089 C  CD   . PRO B 1 80  ? 25.83805 37.41679 11.79483  1.000 22.98103 ? 76  PRO B CD   1 
ATOM   3090 H  HA   . PRO B 1 80  ? 26.61187 38.49465 9.07380   1.000 29.61514 ? 76  PRO B HA   1 
ATOM   3091 H  HB2  . PRO B 1 80  ? 27.14810 39.80485 11.49420  1.000 32.32844 ? 76  PRO B HB2  1 
ATOM   3092 H  HB3  . PRO B 1 80  ? 26.13262 40.25221 10.35662  1.000 32.32844 ? 76  PRO B HB3  1 
ATOM   3093 H  HG2  . PRO B 1 80  ? 25.20112 39.25442 12.43384  1.000 30.11203 ? 76  PRO B HG2  1 
ATOM   3094 H  HG3  . PRO B 1 80  ? 24.56475 38.83121 11.04052  1.000 30.11203 ? 76  PRO B HG3  1 
ATOM   3095 H  HD2  . PRO B 1 80  ? 26.35627 37.34369 12.61154  1.000 27.60196 ? 76  PRO B HD2  1 
ATOM   3096 H  HD3  . PRO B 1 80  ? 25.09051 36.79917 11.81986  1.000 27.60196 ? 76  PRO B HD3  1 
ATOM   3097 N  N    . GLY B 1 81  ? 28.95738 38.90884 8.56509   1.000 27.31220 ? 77  GLY B N    1 
ATOM   3098 C  CA   . GLY B 1 81  ? 30.35502 39.03205 8.23333   1.000 27.57780 ? 77  GLY B CA   1 
ATOM   3099 C  C    . GLY B 1 81  ? 31.00710 37.77986 7.68529   1.000 26.90497 ? 77  GLY B C    1 
ATOM   3100 O  O    . GLY B 1 81  ? 32.19102 37.83578 7.32879   1.000 27.76245 ? 77  GLY B O    1 
ATOM   3101 H  H    . GLY B 1 81  ? 28.42962 39.07832 7.90757   1.000 32.79937 ? 77  GLY B H    1 
ATOM   3102 H  HA2  . GLY B 1 81  ? 30.45308 39.72960 7.56646   1.000 33.11808 ? 77  GLY B HA2  1 
ATOM   3103 H  HA3  . GLY B 1 81  ? 30.84003 39.28925 9.03303   1.000 33.11808 ? 77  GLY B HA3  1 
ATOM   3104 N  N    . THR B 1 82  ? 30.29093 36.65219 7.62233   1.000 25.78255 ? 78  THR B N    1 
ATOM   3105 C  CA   . THR B 1 82  ? 30.85268 35.44905 7.01307   1.000 22.75677 ? 78  THR B CA   1 
ATOM   3106 C  C    . THR B 1 82  ? 31.27059 35.71932 5.56871   1.000 22.23107 ? 78  THR B C    1 
ATOM   3107 O  O    . THR B 1 82  ? 30.66272 36.53107 4.86104   1.000 24.48700 ? 78  THR B O    1 
ATOM   3108 C  CB   . THR B 1 82  ? 29.85496 34.27698 7.06373   1.000 22.45429 ? 78  THR B CB   1 
ATOM   3109 O  OG1  . THR B 1 82  ? 30.49067 33.10067 6.55292   1.000 21.15643 ? 78  THR B OG1  1 
ATOM   3110 C  CG2  . THR B 1 82  ? 28.57424 34.53746 6.26051   1.000 21.95569 ? 78  THR B CG2  1 
ATOM   3111 H  H    . THR B 1 82  ? 29.48969 36.56001 7.92085   1.000 30.96379 ? 78  THR B H    1 
ATOM   3112 H  HA   . THR B 1 82  ? 31.63863 35.18509 7.51657   1.000 27.33286 ? 78  THR B HA   1 
ATOM   3113 H  HB   . THR B 1 82  ? 29.58416 34.15560 7.98723   1.000 26.96987 ? 78  THR B HB   1 
ATOM   3114 H  HG1  . THR B 1 82  ? 31.21590 32.96819 6.95551   1.000 25.41244 ? 78  THR B HG1  1 
ATOM   3115 H  HG21 . THR B 1 82  ? 27.90884 33.86323 6.46923   1.000 26.37155 ? 78  THR B HG21 1 
ATOM   3116 H  HG22 . THR B 1 82  ? 28.21645 35.41170 6.48092   1.000 26.37155 ? 78  THR B HG22 1 
ATOM   3117 H  HG23 . THR B 1 82  ? 28.76652 34.50643 5.31027   1.000 26.37155 ? 78  THR B HG23 1 
ATOM   3118 N  N    . LYS B 1 83  ? 32.33187 35.03731 5.12844   1.000 22.81238 ? 79  LYS B N    1 
ATOM   3119 C  CA   A LYS B 1 83  ? 32.80344 35.15798 3.75242   0.509 22.91581 ? 79  LYS B CA   1 
ATOM   3120 C  CA   B LYS B 1 83  ? 32.80767 35.15432 3.75369   0.491 23.89601 ? 79  LYS B CA   1 
ATOM   3121 C  C    . LYS B 1 83  ? 32.23115 34.08665 2.82733   1.000 23.40899 ? 79  LYS B C    1 
ATOM   3122 O  O    . LYS B 1 83  ? 32.67656 33.97621 1.68431   1.000 25.42803 ? 79  LYS B O    1 
ATOM   3123 C  CB   A LYS B 1 83  ? 34.33640 35.18877 3.68933   0.509 23.85432 ? 79  LYS B CB   1 
ATOM   3124 C  CB   B LYS B 1 83  ? 34.34305 35.14941 3.69901   0.491 26.89862 ? 79  LYS B CB   1 
ATOM   3125 C  CG   A LYS B 1 83  ? 35.06663 33.92339 4.10735   0.509 23.61887 ? 79  LYS B CG   1 
ATOM   3126 C  CG   B LYS B 1 83  ? 35.03698 33.81867 3.99830   0.491 29.24152 ? 79  LYS B CG   1 
ATOM   3127 C  CD   A LYS B 1 83  ? 36.57541 34.17339 4.14568   0.509 26.04479 ? 79  LYS B CD   1 
ATOM   3128 C  CD   B LYS B 1 83  ? 36.53977 33.93382 3.77127   0.491 32.23207 ? 79  LYS B CD   1 
ATOM   3129 C  CE   A LYS B 1 83  ? 37.34938 32.96497 4.65586   0.509 24.73776 ? 79  LYS B CE   1 
ATOM   3130 C  CE   B LYS B 1 83  ? 37.24065 32.58706 3.89010   0.491 33.50991 ? 79  LYS B CE   1 
ATOM   3131 N  NZ   A LYS B 1 83  ? 38.82381 33.08574 4.42715   0.509 25.26957 ? 79  LYS B NZ   1 
ATOM   3132 N  NZ   B LYS B 1 83  ? 37.07915 31.98243 5.24029   0.491 33.50375 ? 79  LYS B NZ   1 
ATOM   3133 H  H    . LYS B 1 83  ? 32.79375 34.49767 5.61328   1.000 27.39958 ? 79  LYS B H    1 
ATOM   3134 H  HA   . LYS B 1 83  ? 32.50526 36.01464 3.40875   1.000 28.69993 ? 79  LYS B HA   1 
ATOM   3135 H  HB2  A LYS B 1 83  ? 34.59490 35.37479 2.77310   0.509 28.64991 ? 79  LYS B HB2  1 
ATOM   3136 H  HB2  B LYS B 1 83  ? 34.61269 35.41528 2.80598   0.491 32.30307 ? 79  LYS B HB2  1 
ATOM   3137 H  HB3  A LYS B 1 83  ? 34.64607 35.89956 4.27224   0.509 28.64991 ? 79  LYS B HB3  1 
ATOM   3138 H  HB3  B LYS B 1 83  ? 34.66884 35.79158 4.34891   0.491 32.30307 ? 79  LYS B HB3  1 
ATOM   3139 H  HG2  A LYS B 1 83  ? 34.77386 33.65483 4.99226   0.509 28.36738 ? 79  LYS B HG2  1 
ATOM   3140 H  HG2  B LYS B 1 83  ? 34.88271 33.57308 4.92393   0.491 35.11456 ? 79  LYS B HG2  1 
ATOM   3141 H  HG3  A LYS B 1 83  ? 34.88529 33.21592 3.46899   0.509 28.36738 ? 79  LYS B HG3  1 
ATOM   3142 H  HG3  B LYS B 1 83  ? 34.68787 33.13099 3.41000   0.491 35.11456 ? 79  LYS B HG3  1 
ATOM   3143 H  HD2  A LYS B 1 83  ? 36.88740 34.37468 3.24955   0.509 31.27847 ? 79  LYS B HD2  1 
ATOM   3144 H  HD2  B LYS B 1 83  ? 36.70231 34.28193 2.88059   0.491 38.70321 ? 79  LYS B HD2  1 
ATOM   3145 H  HD3  A LYS B 1 83  ? 36.75920 34.92037 4.73657   0.509 31.27847 ? 79  LYS B HD3  1 
ATOM   3146 H  HD3  B LYS B 1 83  ? 36.91805 34.53137 4.43515   0.491 38.70321 ? 79  LYS B HD3  1 
ATOM   3147 H  HE2  A LYS B 1 83  ? 37.20021 32.87310 5.60991   0.509 29.71004 ? 79  LYS B HE2  1 
ATOM   3148 H  HE2  B LYS B 1 83  ? 36.86486 31.97454 3.23857   0.491 40.23661 ? 79  LYS B HE2  1 
ATOM   3149 H  HE3  A LYS B 1 83  ? 37.03798 32.17118 4.19344   0.509 29.71004 ? 79  LYS B HE3  1 
ATOM   3150 H  HE3  B LYS B 1 83  ? 38.18896 32.70653 3.72474   0.491 40.23661 ? 79  LYS B HE3  1 
ATOM   3151 H  HZ1  A LYS B 1 83  ? 39.23482 32.34200 4.69176   0.509 30.34822 ? 79  LYS B HZ1  1 
ATOM   3152 H  HZ1  B LYS B 1 83  ? 37.63899 31.29720 5.33591   0.491 40.22923 ? 79  LYS B HZ1  1 
ATOM   3153 H  HZ2  A LYS B 1 83  ? 38.98811 33.21436 3.56196   0.509 30.34822 ? 79  LYS B HZ2  1 
ATOM   3154 H  HZ2  B LYS B 1 83  ? 37.25444 32.58840 5.86812   0.491 40.22923 ? 79  LYS B HZ2  1 
ATOM   3155 H  HZ3  A LYS B 1 83  ? 39.14795 33.77455 4.88822   0.509 30.34822 ? 79  LYS B HZ3  1 
ATOM   3156 H  HZ3  B LYS B 1 83  ? 36.24492 31.69067 5.34535   0.491 40.22923 ? 79  LYS B HZ3  1 
ATOM   3157 N  N    . MET B 1 84  ? 31.26008 33.30196 3.29143   1.000 23.17086 ? 80  MET B N    1 
ATOM   3158 C  CA   . MET B 1 84  ? 30.51401 32.42006 2.40006   1.000 21.56150 ? 80  MET B CA   1 
ATOM   3159 C  C    . MET B 1 84  ? 29.55724 33.28230 1.58959   1.000 23.62311 ? 80  MET B C    1 
ATOM   3160 O  O    . MET B 1 84  ? 28.59452 33.83501 2.13551   1.000 24.01683 ? 80  MET B O    1 
ATOM   3161 C  CB   . MET B 1 84  ? 29.74503 31.37885 3.20888   1.000 21.39211 ? 80  MET B CB   1 
ATOM   3162 C  CG   . MET B 1 84  ? 28.81418 30.54566 2.35676   1.000 19.01997 ? 80  MET B CG   1 
ATOM   3163 S  SD   . MET B 1 84  ? 28.33592 28.95450 3.08341   1.000 17.63964 ? 80  MET B SD   1 
ATOM   3164 C  CE   . MET B 1 84  ? 26.65009 28.85114 2.49938   1.000 17.23381 ? 80  MET B CE   1 
ATOM   3165 H  H    . MET B 1 84  ? 31.01614 33.26296 4.11518   1.000 27.82976 ? 80  MET B H    1 
ATOM   3166 H  HA   . MET B 1 84  ? 31.12558 31.94521 1.81576   1.000 25.89853 ? 80  MET B HA   1 
ATOM   3167 H  HB2  . MET B 1 84  ? 30.37796 30.78031 3.63553   1.000 25.69526 ? 80  MET B HB2  1 
ATOM   3168 H  HB3  . MET B 1 84  ? 29.21208 31.83194 3.88087   1.000 25.69526 ? 80  MET B HB3  1 
ATOM   3169 H  HG2  . MET B 1 84  ? 28.00103 31.05181 2.20346   1.000 22.84869 ? 80  MET B HG2  1 
ATOM   3170 H  HG3  . MET B 1 84  ? 29.25340 30.35967 1.51214   1.000 22.84869 ? 80  MET B HG3  1 
ATOM   3171 H  HE1  . MET B 1 84  ? 26.25812 28.02056 2.81147   1.000 20.70530 ? 80  MET B HE1  1 
ATOM   3172 H  HE2  . MET B 1 84  ? 26.14852 29.60492 2.84743   1.000 20.70530 ? 80  MET B HE2  1 
ATOM   3173 H  HE3  . MET B 1 84  ? 26.64992 28.87314 1.52963   1.000 20.70530 ? 80  MET B HE3  1 
ATOM   3174 N  N    . ILE B 1 85  ? 29.86017 33.44744 0.30414   1.000 23.38727 ? 81  ILE B N    1 
ATOM   3175 C  CA   . ILE B 1 85  ? 29.07110 34.29947 -0.58330  1.000 25.86477 ? 81  ILE B CA   1 
ATOM   3176 C  C    . ILE B 1 85  ? 28.00684 33.38731 -1.18316  1.000 27.47950 ? 81  ILE B C    1 
ATOM   3177 O  O    . ILE B 1 85  ? 28.22933 32.69224 -2.17442  1.000 28.53006 ? 81  ILE B O    1 
ATOM   3178 C  CB   . ILE B 1 85  ? 29.93652 34.98615 -1.63797  1.000 29.48144 ? 81  ILE B CB   1 
ATOM   3179 C  CG1  . ILE B 1 85  ? 31.16010 35.66265 -0.99174  1.000 34.20956 ? 81  ILE B CG1  1 
ATOM   3180 C  CG2  . ILE B 1 85  ? 29.11109 35.99258 -2.43290  1.000 30.98566 ? 81  ILE B CG2  1 
ATOM   3181 C  CD1  . ILE B 1 85  ? 30.84933 36.66523 0.09507   1.000 36.26769 ? 81  ILE B CD1  1 
ATOM   3182 H  H    . ILE B 1 85  ? 30.52886 33.07039 -0.08352  1.000 28.08946 ? 81  ILE B H    1 
ATOM   3183 H  HA   . ILE B 1 85  ? 28.62946 34.99424 -0.07032  1.000 31.06245 ? 81  ILE B HA   1 
ATOM   3184 H  HB   . ILE B 1 85  ? 30.26243 34.30724 -2.24932  1.000 35.40246 ? 81  ILE B HB   1 
ATOM   3185 H  HG12 . ILE B 1 85  ? 31.71750 34.97336 -0.59794  1.000 41.07620 ? 81  ILE B HG12 1 
ATOM   3186 H  HG13 . ILE B 1 85  ? 31.65144 36.13095 -1.68469  1.000 41.07620 ? 81  ILE B HG13 1 
ATOM   3187 H  HG21 . ILE B 1 85  ? 29.70654 36.52428 -2.98393  1.000 37.20752 ? 81  ILE B HG21 1 
ATOM   3188 H  HG22 . ILE B 1 85  ? 28.48210 35.51227 -2.99378  1.000 37.20752 ? 81  ILE B HG22 1 
ATOM   3189 H  HG23 . ILE B 1 85  ? 28.63189 36.56635 -1.81480  1.000 37.20752 ? 81  ILE B HG23 1 
ATOM   3190 H  HD11 . ILE B 1 85  ? 31.65939 37.14958 0.31892   1.000 43.54596 ? 81  ILE B HD11 1 
ATOM   3191 H  HD12 . ILE B 1 85  ? 30.17379 37.28185 -0.22789  1.000 43.54596 ? 81  ILE B HD12 1 
ATOM   3192 H  HD13 . ILE B 1 85  ? 30.51997 36.19289 0.87566   1.000 43.54596 ? 81  ILE B HD13 1 
ATOM   3193 N  N    . PHE B 1 86  ? 26.84105 33.37424 -0.54177  1.000 26.88929 ? 82  PHE B N    1 
ATOM   3194 C  CA   . PHE B 1 86  ? 25.74293 32.48802 -0.91702  1.000 27.55911 ? 82  PHE B CA   1 
ATOM   3195 C  C    . PHE B 1 86  ? 24.47601 33.11872 -0.37144  1.000 29.44718 ? 82  PHE B C    1 
ATOM   3196 O  O    . PHE B 1 86  ? 24.32392 33.23877 0.84897   1.000 30.37893 ? 82  PHE B O    1 
ATOM   3197 C  CB   . PHE B 1 86  ? 25.95763 31.09434 -0.31312  1.000 25.09987 ? 82  PHE B CB   1 
ATOM   3198 C  CG   . PHE B 1 86  ? 24.92265 30.09465 -0.71342  1.000 24.76747 ? 82  PHE B CG   1 
ATOM   3199 C  CD1  . PHE B 1 86  ? 25.02175 29.41796 -1.90919  1.000 25.71867 ? 82  PHE B CD1  1 
ATOM   3200 C  CD2  . PHE B 1 86  ? 23.86526 29.81074 0.12575   1.000 23.43098 ? 82  PHE B CD2  1 
ATOM   3201 C  CE1  . PHE B 1 86  ? 24.05880 28.48881 -2.27263  1.000 25.80885 ? 82  PHE B CE1  1 
ATOM   3202 C  CE2  . PHE B 1 86  ? 22.90850 28.88221 -0.22467  1.000 22.80477 ? 82  PHE B CE2  1 
ATOM   3203 C  CZ   . PHE B 1 86  ? 23.00158 28.22337 -1.41804  1.000 25.27931 ? 82  PHE B CZ   1 
ATOM   3204 H  H    . PHE B 1 86  ? 26.65668 33.88005 0.12888   1.000 32.29188 ? 82  PHE B H    1 
ATOM   3205 H  HA   . PHE B 1 86  ? 25.67686 32.39881 -1.88064  1.000 33.09566 ? 82  PHE B HA   1 
ATOM   3206 H  HB2  . PHE B 1 86  ? 26.82019 30.75884 -0.60353  1.000 30.14457 ? 82  PHE B HB2  1 
ATOM   3207 H  HB3  . PHE B 1 86  ? 25.93874 31.16791 0.65390   1.000 30.14457 ? 82  PHE B HB3  1 
ATOM   3208 H  HD1  . PHE B 1 86  ? 25.73936 29.58542 -2.47655  1.000 30.88713 ? 82  PHE B HD1  1 
ATOM   3209 H  HD2  . PHE B 1 86  ? 23.79675 30.25288 0.94106   1.000 28.14191 ? 82  PHE B HD2  1 
ATOM   3210 H  HE1  . PHE B 1 86  ? 24.12259 28.04529 -3.08757  1.000 30.99535 ? 82  PHE B HE1  1 
ATOM   3211 H  HE2  . PHE B 1 86  ? 22.20001 28.70433 0.35092   1.000 27.39045 ? 82  PHE B HE2  1 
ATOM   3212 H  HZ   . PHE B 1 86  ? 22.35607 27.59765 -1.65615  1.000 30.35990 ? 82  PHE B HZ   1 
ATOM   3213 N  N    . ALA B 1 87  ? 23.57536 33.51960 -1.26898  1.000 31.18730 ? 83  ALA B N    1 
ATOM   3214 C  CA   . ALA B 1 87  ? 22.40665 34.29404 -0.86332  1.000 32.37505 ? 83  ALA B CA   1 
ATOM   3215 C  C    . ALA B 1 87  ? 21.48236 33.48005 0.03044   1.000 31.64223 ? 83  ALA B C    1 
ATOM   3216 O  O    . ALA B 1 87  ? 20.93268 34.00891 1.00709   1.000 33.79491 ? 83  ALA B O    1 
ATOM   3217 C  CB   . ALA B 1 87  ? 21.65668 34.77828 -2.10052  1.000 33.62964 ? 83  ALA B CB   1 
ATOM   3218 H  H    . ALA B 1 87  ? 23.61581 33.35845 -2.11278  1.000 37.44948 ? 83  ALA B H    1 
ATOM   3219 H  HA   . ALA B 1 87  ? 22.70356 35.06811 -0.35977  1.000 38.87479 ? 83  ALA B HA   1 
ATOM   3220 H  HB1  . ALA B 1 87  ? 20.86571 35.26472 -1.82008  1.000 40.38030 ? 83  ALA B HB1  1 
ATOM   3221 H  HB2  . ALA B 1 87  ? 22.23801 35.36029 -2.61454  1.000 40.38030 ? 83  ALA B HB2  1 
ATOM   3222 H  HB3  . ALA B 1 87  ? 21.40060 34.01054 -2.63521  1.000 40.38030 ? 83  ALA B HB3  1 
ATOM   3223 N  N    . GLY B 1 88  ? 21.30189 32.20613 -0.28614  1.000 29.58382 ? 84  GLY B N    1 
ATOM   3224 C  CA   . GLY B 1 88  ? 20.51379 31.29602 0.52307   1.000 27.28535 ? 84  GLY B CA   1 
ATOM   3225 C  C    . GLY B 1 88  ? 19.70813 30.32024 -0.31095  1.000 26.64484 ? 84  GLY B C    1 
ATOM   3226 O  O    . GLY B 1 88  ? 19.42429 30.54340 -1.48824  1.000 29.64246 ? 84  GLY B O    1 
ATOM   3227 H  H    . GLY B 1 88  ? 21.63754 31.83762 -0.98695  1.000 35.52531 ? 84  GLY B H    1 
ATOM   3228 H  HA2  . GLY B 1 88  ? 21.10446 30.78712 1.10014   1.000 32.76714 ? 84  GLY B HA2  1 
ATOM   3229 H  HA3  . GLY B 1 88  ? 19.89852 31.80662 1.07229   1.000 32.76714 ? 84  GLY B HA3  1 
ATOM   3230 N  N    . LEU B 1 89  ? 19.33137 29.21182 0.32496   1.000 24.83145 ? 85  LEU B N    1 
ATOM   3231 C  CA   . LEU B 1 89  ? 18.41848 28.21866 -0.23476  1.000 24.80585 ? 85  LEU B CA   1 
ATOM   3232 C  C    . LEU B 1 89  ? 17.06863 28.50153 0.39494   1.000 26.08738 ? 85  LEU B C    1 
ATOM   3233 O  O    . LEU B 1 89  ? 16.79551 28.07385 1.51512   1.000 25.49281 ? 85  LEU B O    1 
ATOM   3234 C  CB   . LEU B 1 89  ? 18.84659 26.81116 0.15196   1.000 28.38844 ? 85  LEU B CB   1 
ATOM   3235 C  CG   . LEU B 1 89  ? 19.58365 25.85158 -0.74264  1.000 29.78756 ? 85  LEU B CG   1 
ATOM   3236 C  CD1  . LEU B 1 89  ? 19.62178 24.48568 -0.09889  1.000 26.36709 ? 85  LEU B CD1  1 
ATOM   3237 C  CD2  . LEU B 1 89  ? 18.92249 25.76624 -2.09827  1.000 28.21264 ? 85  LEU B CD2  1 
ATOM   3238 H  H    . LEU B 1 89  ? 19.60402 29.00698 1.11445   1.000 29.82247 ? 85  LEU B H    1 
ATOM   3239 H  HA   . LEU B 1 89  ? 18.39526 28.29872 -1.20117  1.000 29.79175 ? 85  LEU B HA   1 
ATOM   3240 H  HB2  . LEU B 1 89  ? 19.41805 26.91163 0.92930   1.000 34.09086 ? 85  LEU B HB2  1 
ATOM   3241 H  HB3  . LEU B 1 89  ? 18.03257 26.34390 0.39678   1.000 34.09086 ? 85  LEU B HB3  1 
ATOM   3242 H  HG   . LEU B 1 89  ? 20.49129 26.16832 -0.87208  1.000 35.76979 ? 85  LEU B HG   1 
ATOM   3243 H  HD11 . LEU B 1 89  ? 20.18153 23.90045 -0.63282  1.000 31.66524 ? 85  LEU B HD11 1 
ATOM   3244 H  HD12 . LEU B 1 89  ? 19.98801 24.56821 0.79551   1.000 31.66524 ? 85  LEU B HD12 1 
ATOM   3245 H  HD13 . LEU B 1 89  ? 18.71973 24.13167 -0.05561  1.000 31.66524 ? 85  LEU B HD13 1 
ATOM   3246 H  HD21 . LEU B 1 89  ? 19.31877 25.03500 -2.59743  1.000 33.87989 ? 85  LEU B HD21 1 
ATOM   3247 H  HD22 . LEU B 1 89  ? 17.97318 25.60794 -1.97724  1.000 33.87989 ? 85  LEU B HD22 1 
ATOM   3248 H  HD23 . LEU B 1 89  ? 19.06089 26.60225 -2.57032  1.000 33.87989 ? 85  LEU B HD23 1 
ATOM   3249 N  N    . LYS B 1 90  ? 16.21528 29.21464 -0.32615  1.000 28.52229 ? 86  LYS B N    1 
ATOM   3250 C  CA   . LYS B 1 90  ? 14.99277 29.70923 0.28726   1.000 31.45727 ? 86  LYS B CA   1 
ATOM   3251 C  C    . LYS B 1 90  ? 13.95231 28.60758 0.48614   1.000 30.57287 ? 86  LYS B C    1 
ATOM   3252 O  O    . LYS B 1 90  ? 13.23707 28.62084 1.49562   1.000 32.07992 ? 86  LYS B O    1 
ATOM   3253 C  CB   . LYS B 1 90  ? 14.45082 30.87896 -0.53632  1.000 35.80688 ? 86  LYS B CB   1 
ATOM   3254 C  CG   . LYS B 1 90  ? 15.47157 32.01830 -0.76662  1.000 38.30435 ? 86  LYS B CG   1 
ATOM   3255 C  CD   . LYS B 1 90  ? 15.95701 32.64580 0.54819   1.000 40.31036 ? 86  LYS B CD   1 
ATOM   3256 C  CE   . LYS B 1 90  ? 16.86433 33.84682 0.30893   1.000 40.77577 ? 86  LYS B CE   1 
ATOM   3257 N  NZ   . LYS B 1 90  ? 17.37800 34.42642 1.58153   1.000 41.55245 ? 86  LYS B NZ   1 
ATOM   3258 H  H    . LYS B 1 90  ? 16.31557 29.42309 -1.15445  1.000 34.25147 ? 86  LYS B H    1 
ATOM   3259 H  HA   . LYS B 1 90  ? 15.19040 30.04652 1.17499   1.000 37.77346 ? 86  LYS B HA   1 
ATOM   3260 H  HB2  . LYS B 1 90  ? 14.17959 30.54645 -1.40624  1.000 42.99298 ? 86  LYS B HB2  1 
ATOM   3261 H  HB3  . LYS B 1 90  ? 13.68720 31.25712 -0.07286  1.000 42.99298 ? 86  LYS B HB3  1 
ATOM   3262 H  HG2  . LYS B 1 90  ? 16.24403 31.66311 -1.23359  1.000 45.98994 ? 86  LYS B HG2  1 
ATOM   3263 H  HG3  . LYS B 1 90  ? 15.05502 32.71557 -1.29690  1.000 45.98994 ? 86  LYS B HG3  1 
ATOM   3264 H  HD2  . LYS B 1 90  ? 15.19003 32.94376 1.06187   1.000 48.39716 ? 86  LYS B HD2  1 
ATOM   3265 H  HD3  . LYS B 1 90  ? 16.45704 31.98460 1.05185   1.000 48.39716 ? 86  LYS B HD3  1 
ATOM   3266 H  HE2  . LYS B 1 90  ? 17.62491 33.56988 -0.22559  1.000 48.95565 ? 86  LYS B HE2  1 
ATOM   3267 H  HE3  . LYS B 1 90  ? 16.36473 34.53561 -0.15677  1.000 48.95565 ? 86  LYS B HE3  1 
ATOM   3268 H  HZ1  . LYS B 1 90  ? 17.94237 35.09208 1.40690   1.000 49.88767 ? 86  LYS B HZ1  1 
ATOM   3269 H  HZ2  . LYS B 1 90  ? 16.70197 34.74091 2.06752   1.000 49.88767 ? 86  LYS B HZ2  1 
ATOM   3270 H  HZ3  . LYS B 1 90  ? 17.80456 33.80158 2.05028   1.000 49.88767 ? 86  LYS B HZ3  1 
ATOM   3271 N  N    . LYS B 1 91  ? 13.87425 27.63350 -0.41866  1.000 26.99279 ? 87  LYS B N    1 
ATOM   3272 C  CA   . LYS B 1 91  ? 12.79796 26.64871 -0.35442  1.000 25.99926 ? 87  LYS B CA   1 
ATOM   3273 C  C    . LYS B 1 91  ? 13.02769 25.66827 0.79779   1.000 22.92664 ? 87  LYS B C    1 
ATOM   3274 O  O    . LYS B 1 91  ? 14.09630 25.05311 0.87146   1.000 23.69403 ? 87  LYS B O    1 
ATOM   3275 C  CB   . LYS B 1 91  ? 12.69511 25.89427 -1.67345  1.000 28.11192 ? 87  LYS B CB   1 
ATOM   3276 C  CG   . LYS B 1 91  ? 12.09886 26.72414 -2.78993  1.000 31.47211 ? 87  LYS B CG   1 
ATOM   3277 C  CD   . LYS B 1 91  ? 12.12824 25.96372 -4.10741  1.000 35.75637 ? 87  LYS B CD   1 
ATOM   3278 C  CE   . LYS B 1 91  ? 11.67434 26.82410 -5.27386  1.000 39.87656 ? 87  LYS B CE   1 
ATOM   3279 N  NZ   . LYS B 1 91  ? 11.66901 26.06409 -6.55698  1.000 42.71045 ? 87  LYS B NZ   1 
ATOM   3280 H  H    . LYS B 1 91  ? 14.42318 27.52080 -1.07102  1.000 32.41608 ? 87  LYS B H    1 
ATOM   3281 H  HA   . LYS B 1 91  ? 11.95932 27.10859 -0.19291  1.000 31.22384 ? 87  LYS B HA   1 
ATOM   3282 H  HB2  . LYS B 1 91  ? 13.58386 25.61913 -1.94790  1.000 33.75903 ? 87  LYS B HB2  1 
ATOM   3283 H  HB3  . LYS B 1 91  ? 12.13110 25.11538 -1.54650  1.000 33.75903 ? 87  LYS B HB3  1 
ATOM   3284 H  HG2  . LYS B 1 91  ? 11.17635 26.93631 -2.57811  1.000 37.79126 ? 87  LYS B HG2  1 
ATOM   3285 H  HG3  . LYS B 1 91  ? 12.61141 27.54093 -2.89508  1.000 37.79126 ? 87  LYS B HG3  1 
ATOM   3286 H  HD2  . LYS B 1 91  ? 13.03479 25.66776 -4.28481  1.000 42.93237 ? 87  LYS B HD2  1 
ATOM   3287 H  HD3  . LYS B 1 91  ? 11.53518 25.19849 -4.04740  1.000 42.93237 ? 87  LYS B HD3  1 
ATOM   3288 H  HE2  . LYS B 1 91  ? 10.77324 27.14120 -5.10542  1.000 47.87660 ? 87  LYS B HE2  1 
ATOM   3289 H  HE3  . LYS B 1 91  ? 12.27846 27.57692 -5.36976  1.000 47.87660 ? 87  LYS B HE3  1 
ATOM   3290 H  HZ1  . LYS B 1 91  ? 11.31636 26.56251 -7.20452  1.000 51.27727 ? 87  LYS B HZ1  1 
ATOM   3291 H  HZ2  . LYS B 1 91  ? 12.50087 25.84295 -6.78324  1.000 51.27727 ? 87  LYS B HZ2  1 
ATOM   3292 H  HZ3  . LYS B 1 91  ? 11.18652 25.32143 -6.46887  1.000 51.27727 ? 87  LYS B HZ3  1 
ATOM   3293 N  N    . PRO B 1 92  ? 12.05950 25.48348 1.70947   1.000 22.23258 ? 88  PRO B N    1 
ATOM   3294 C  CA   . PRO B 1 92  ? 12.30953 24.58172 2.85536   1.000 21.34208 ? 88  PRO B CA   1 
ATOM   3295 C  C    . PRO B 1 92  ? 12.60011 23.13069 2.49158   1.000 19.90737 ? 88  PRO B C    1 
ATOM   3296 O  O    . PRO B 1 92  ? 13.41052 22.47519 3.16622   1.000 19.76755 ? 88  PRO B O    1 
ATOM   3297 C  CB   . PRO B 1 92  ? 11.03726 24.72800 3.70839   1.000 23.29665 ? 88  PRO B CB   1 
ATOM   3298 C  CG   . PRO B 1 92  ? 10.04973 25.34601 2.84055   1.000 24.43306 ? 88  PRO B CG   1 
ATOM   3299 C  CD   . PRO B 1 92  ? 10.76346 26.17644 1.85893   1.000 23.67782 ? 88  PRO B CD   1 
ATOM   3300 H  HA   . PRO B 1 92  ? 13.07181 24.92151 3.34970   1.000 25.63523 ? 88  PRO B HA   1 
ATOM   3301 H  HB2  . PRO B 1 92  ? 10.73818 23.85334 4.00236   1.000 27.98071 ? 88  PRO B HB2  1 
ATOM   3302 H  HB3  . PRO B 1 92  ? 11.22135 25.29112 4.47644   1.000 27.98071 ? 88  PRO B HB3  1 
ATOM   3303 H  HG2  . PRO B 1 92  ? 9.54426  24.65221 2.38883   1.000 29.34440 ? 88  PRO B HG2  1 
ATOM   3304 H  HG3  . PRO B 1 92  ? 9.45507  25.89493 3.37530   1.000 29.34440 ? 88  PRO B HG3  1 
ATOM   3305 H  HD2  . PRO B 1 92  ? 10.28570 26.20157 1.01512   1.000 28.43812 ? 88  PRO B HD2  1 
ATOM   3306 H  HD3  . PRO B 1 92  ? 10.89007 27.07735 2.19544   1.000 28.43812 ? 88  PRO B HD3  1 
ATOM   3307 N  N    . ASN B 1 93  ? 11.96063 22.59631 1.44736   1.000 19.90114 ? 89  ASN B N    1 
ATOM   3308 C  CA   . ASN B 1 93  ? 12.22338 21.20946 1.09046   1.000 20.17729 ? 89  ASN B CA   1 
ATOM   3309 C  C    . ASN B 1 93  ? 13.55885 21.02419 0.37708   1.000 19.93397 ? 89  ASN B C    1 
ATOM   3310 O  O    . ASN B 1 93  ? 14.12994 19.93102 0.43651   1.000 21.50138 ? 89  ASN B O    1 
ATOM   3311 C  CB   . ASN B 1 93  ? 11.06439 20.66258 0.28093   1.000 21.64924 ? 89  ASN B CB   1 
ATOM   3312 C  CG   . ASN B 1 93  ? 9.81316  20.63605 1.08346   1.000 23.81172 ? 89  ASN B CG   1 
ATOM   3313 O  OD1  . ASN B 1 93  ? 8.94185  21.49055 0.92843   1.000 24.47790 ? 89  ASN B OD1  1 
ATOM   3314 N  ND2  . ASN B 1 93  ? 9.73587  19.68632 1.99902   1.000 24.00416 ? 89  ASN B ND2  1 
ATOM   3315 H  H    . ASN B 1 93  ? 11.39044 23.00336 0.94856   1.000 23.90610 ? 89  ASN B H    1 
ATOM   3316 H  HA   . ASN B 1 93  ? 12.28148 20.67760 1.89957   1.000 24.23747 ? 89  ASN B HA   1 
ATOM   3317 H  HB2  . ASN B 1 93  ? 10.91902 21.22641 -0.49487  1.000 26.00382 ? 89  ASN B HB2  1 
ATOM   3318 H  HB3  . ASN B 1 93  ? 11.26723 19.75677 -0.00058  1.000 26.00382 ? 89  ASN B HB3  1 
ATOM   3319 H  HD21 . ASN B 1 93  ? 9.03530  19.62187 2.49365   1.000 28.82972 ? 89  ASN B HD21 1 
ATOM   3320 H  HD22 . ASN B 1 93  ? 10.38613 19.13268 2.10024   1.000 28.82972 ? 89  ASN B HD22 1 
ATOM   3321 N  N    . GLU B 1 94  ? 14.06044 22.05047 -0.30729  1.000 19.71175 ? 90  GLU B N    1 
ATOM   3322 C  CA   . GLU B 1 94  ? 15.41515 21.94663 -0.83706  1.000 19.77299 ? 90  GLU B CA   1 
ATOM   3323 C  C    . GLU B 1 94  ? 16.41542 21.88714 0.30595   1.000 17.47834 ? 90  GLU B C    1 
ATOM   3324 O  O    . GLU B 1 94  ? 17.35462 21.08627 0.27477   1.000 17.74534 ? 90  GLU B O    1 
ATOM   3325 C  CB   . GLU B 1 94  ? 15.71880 23.10457 -1.79304  1.000 22.42111 ? 90  GLU B CB   1 
ATOM   3326 C  CG   . GLU B 1 94  ? 14.96468 22.98613 -3.14789  1.000 24.26013 ? 90  GLU B CG   1 
ATOM   3327 C  CD   . GLU B 1 94  ? 15.53345 23.88073 -4.25722  1.000 28.90625 ? 90  GLU B CD   1 
ATOM   3328 O  OE1  . GLU B 1 94  ? 16.41310 24.72027 -3.97622  1.000 32.14596 ? 90  GLU B OE1  1 
ATOM   3329 O  OE2  . GLU B 1 94  ? 15.09614 23.74469 -5.42209  1.000 32.44666 ? 90  GLU B OE2  1 
ATOM   3330 H  H    . GLU B 1 94  ? 13.65428 22.79011 -0.47333  1.000 23.67883 ? 90  GLU B H    1 
ATOM   3331 H  HA   . GLU B 1 94  ? 15.49645 21.13429 -1.36088  1.000 23.75232 ? 90  GLU B HA   1 
ATOM   3332 H  HB2  . GLU B 1 94  ? 15.45203 23.93748 -1.37353  1.000 26.93006 ? 90  GLU B HB2  1 
ATOM   3333 H  HB3  . GLU B 1 94  ? 16.67052 23.11722 -1.98005  1.000 26.93006 ? 90  GLU B HB3  1 
ATOM   3334 H  HG2  . GLU B 1 94  ? 15.01687 22.06725 -3.45421  1.000 29.13688 ? 90  GLU B HG2  1 
ATOM   3335 H  HG3  . GLU B 1 94  ? 14.03798 23.23832 -3.01173  1.000 29.13688 ? 90  GLU B HG3  1 
ATOM   3336 N  N    . ARG B 1 95  ? 16.20115 22.69321 1.34732   1.000 17.49246 ? 91  ARG B N    1 
ATOM   3337 C  CA   . ARG B 1 95  ? 17.05906 22.59425 2.52232   1.000 16.39641 ? 91  ARG B CA   1 
ATOM   3338 C  C    . ARG B 1 95  ? 16.92376 21.23962 3.19290   1.000 16.73948 ? 91  ARG B C    1 
ATOM   3339 O  O    . ARG B 1 95  ? 17.92442 20.64907 3.62026   1.000 16.48068 ? 91  ARG B O    1 
ATOM   3340 C  CB   . ARG B 1 95  ? 16.76340 23.72267 3.50265   1.000 17.88638 ? 91  ARG B CB   1 
ATOM   3341 C  CG   . ARG B 1 95  ? 17.33415 25.06335 3.04570   1.000 19.13965 ? 91  ARG B CG   1 
ATOM   3342 C  CD   . ARG B 1 95  ? 16.99668 26.18252 3.99713   1.000 18.48977 ? 91  ARG B CD   1 
ATOM   3343 N  NE   . ARG B 1 95  ? 15.62215 26.64058 3.78076   1.000 21.90439 ? 91  ARG B NE   1 
ATOM   3344 C  CZ   . ARG B 1 95  ? 14.80951 27.14469 4.71191   1.000 20.92947 ? 91  ARG B CZ   1 
ATOM   3345 N  NH1  . ARG B 1 95  ? 15.17689 27.24374 5.99102   1.000 21.93033 ? 91  ARG B NH1  1 
ATOM   3346 N  NH2  . ARG B 1 95  ? 13.58780 27.54419 4.35396   1.000 24.16651 ? 91  ARG B NH2  1 
ATOM   3347 H  H    . ARG B 1 95  ? 15.58331 23.28931 1.39772   1.000 21.01568 ? 91  ARG B H    1 
ATOM   3348 H  HA   . ARG B 1 95  ? 17.98108 22.69426 2.23809   1.000 19.70042 ? 91  ARG B HA   1 
ATOM   3349 H  HB2  . ARG B 1 95  ? 15.80245 23.81969 3.59241   1.000 21.48838 ? 91  ARG B HB2  1 
ATOM   3350 H  HB3  . ARG B 1 95  ? 17.15667 23.50560 4.36237   1.000 21.48838 ? 91  ARG B HB3  1 
ATOM   3351 H  HG2  . ARG B 1 95  ? 18.30020 24.99573 2.99028   1.000 22.99231 ? 91  ARG B HG2  1 
ATOM   3352 H  HG3  . ARG B 1 95  ? 16.96672 25.28588 2.17600   1.000 22.99231 ? 91  ARG B HG3  1 
ATOM   3353 H  HD2  . ARG B 1 95  ? 17.07790 25.86793 4.91110   1.000 22.21246 ? 91  ARG B HD2  1 
ATOM   3354 H  HD3  . ARG B 1 95  ? 17.59861 26.92846 3.84829   1.000 22.21246 ? 91  ARG B HD3  1 
ATOM   3355 H  HE   . ARG B 1 95  ? 15.31065 26.57912 2.98152   1.000 26.31000 ? 91  ARG B HE   1 
ATOM   3356 H  HH11 . ARG B 1 95  ? 15.95748 26.97864 6.23597   1.000 26.34113 ? 91  ARG B HH11 1 
ATOM   3357 H  HH12 . ARG B 1 95  ? 14.63306 27.57268 6.57037   1.000 26.34113 ? 91  ARG B HH12 1 
ATOM   3358 H  HH21 . ARG B 1 95  ? 13.33550 27.47475 3.53473   1.000 29.02454 ? 91  ARG B HH21 1 
ATOM   3359 H  HH22 . ARG B 1 95  ? 13.05265 27.87112 4.94246   1.000 29.02454 ? 91  ARG B HH22 1 
ATOM   3360 N  N    . GLY B 1 96  ? 15.69186 20.75606 3.35662   1.000 18.63126 ? 92  GLY B N    1 
ATOM   3361 C  CA   . GLY B 1 96  ? 15.51206 19.46910 3.99600   1.000 18.30202 ? 92  GLY B CA   1 
ATOM   3362 C  C    . GLY B 1 96  ? 16.18189 18.32951 3.25092   1.000 18.82980 ? 92  GLY B C    1 
ATOM   3363 O  O    . GLY B 1 96  ? 16.81454 17.46634 3.86255   1.000 18.83305 ? 92  GLY B O    1 
ATOM   3364 H  H    . GLY B 1 96  ? 14.96510 21.14532 3.11190   1.000 22.38225 ? 92  GLY B H    1 
ATOM   3365 H  HA2  . GLY B 1 96  ? 15.88440 19.50459 4.89099   1.000 21.98716 ? 92  GLY B HA2  1 
ATOM   3366 H  HA3  . GLY B 1 96  ? 14.56372 19.27427 4.05598   1.000 21.98716 ? 92  GLY B HA3  1 
ATOM   3367 N  N    . ASP B 1 97  ? 16.04824 18.30337 1.92285   1.000 19.07551 ? 93  ASP B N    1 
ATOM   3368 C  CA   . ASP B 1 97  ? 16.68908 17.25294 1.13902   1.000 19.90149 ? 93  ASP B CA   1 
ATOM   3369 C  C    . ASP B 1 97  ? 18.20795 17.36556 1.21709   1.000 17.70352 ? 93  ASP B C    1 
ATOM   3370 O  O    . ASP B 1 97  ? 18.91216 16.36342 1.40072   1.000 18.47040 ? 93  ASP B O    1 
ATOM   3371 C  CB   . ASP B 1 97  ? 16.22489 17.32569 -0.31877  1.000 20.51482 ? 93  ASP B CB   1 
ATOM   3372 C  CG   . ASP B 1 97  ? 14.76213 16.89639 -0.51714  1.000 23.86259 ? 93  ASP B CG   1 
ATOM   3373 O  OD1  . ASP B 1 97  ? 14.17989 16.24451 0.38246   1.000 26.58040 ? 93  ASP B OD1  1 
ATOM   3374 O  OD2  . ASP B 1 97  ? 14.18837 17.21522 -1.58134  1.000 25.42176 ? 93  ASP B OD2  1 
ATOM   3375 H  H    . ASP B 1 97  ? 15.59965 18.87229 1.45949   1.000 22.91534 ? 93  ASP B H    1 
ATOM   3376 H  HA   . ASP B 1 97  ? 16.42567 16.39123 1.49814   1.000 23.90652 ? 93  ASP B HA   1 
ATOM   3377 H  HB2  . ASP B 1 97  ? 16.31072 18.24046 -0.62977  1.000 24.64251 ? 93  ASP B HB2  1 
ATOM   3378 H  HB3  . ASP B 1 97  ? 16.78173 16.73946 -0.85465  1.000 24.64251 ? 93  ASP B HB3  1 
ATOM   3379 N  N    . LEU B 1 98  ? 18.73455 18.58188 1.06898   1.000 16.03470 ? 94  LEU B N    1 
ATOM   3380 C  CA   . LEU B 1 98  ? 20.17751 18.78437 1.16627   1.000 15.26691 ? 94  LEU B CA   1 
ATOM   3381 C  C    . LEU B 1 98  ? 20.71472 18.31554 2.51646   1.000 15.81170 ? 94  LEU B C    1 
ATOM   3382 O  O    . LEU B 1 98  ? 21.77113 17.67539 2.58561   1.000 15.64920 ? 94  LEU B O    1 
ATOM   3383 C  CB   . LEU B 1 98  ? 20.49525 20.26139 0.94627   1.000 15.52358 ? 94  LEU B CB   1 
ATOM   3384 C  CG   . LEU B 1 98  ? 21.95341 20.68351 1.12314   1.000 15.14950 ? 94  LEU B CG   1 
ATOM   3385 C  CD1  . LEU B 1 98  ? 22.88081 19.93512 0.17139   1.000 15.87676 ? 94  LEU B CD1  1 
ATOM   3386 C  CD2  . LEU B 1 98  ? 22.07133 22.15815 0.93291   1.000 17.87667 ? 94  LEU B CD2  1 
ATOM   3387 H  H    . LEU B 1 98  ? 18.28548 19.29862 0.91336   1.000 19.26636 ? 94  LEU B H    1 
ATOM   3388 H  HA   . LEU B 1 98  ? 20.62044 18.26577 0.47652   1.000 18.34502 ? 94  LEU B HA   1 
ATOM   3389 H  HB2  . LEU B 1 98  ? 20.24106 20.49067 0.03868   1.000 18.65303 ? 94  LEU B HB2  1 
ATOM   3390 H  HB3  . LEU B 1 98  ? 19.97114 20.77804 1.57816   1.000 18.65303 ? 94  LEU B HB3  1 
ATOM   3391 H  HG   . LEU B 1 98  ? 22.23971 20.45696 2.02181   1.000 18.20412 ? 94  LEU B HG   1 
ATOM   3392 H  HD11 . LEU B 1 98  ? 23.78269 20.27668 0.27556   1.000 19.07684 ? 94  LEU B HD11 1 
ATOM   3393 H  HD12 . LEU B 1 98  ? 22.85824 18.98962 0.38682   1.000 19.07684 ? 94  LEU B HD12 1 
ATOM   3394 H  HD13 . LEU B 1 98  ? 22.57759 20.07417 -0.73945  1.000 19.07684 ? 94  LEU B HD13 1 
ATOM   3395 H  HD21 . LEU B 1 98  ? 22.98100 22.43039 1.13112   1.000 21.47673 ? 94  LEU B HD21 1 
ATOM   3396 H  HD22 . LEU B 1 98  ? 21.85374 22.37632 0.01315   1.000 21.47673 ? 94  LEU B HD22 1 
ATOM   3397 H  HD23 . LEU B 1 98  ? 21.45417 22.60441 1.53362   1.000 21.47673 ? 94  LEU B HD23 1 
ATOM   3398 N  N    . ILE B 1 99  ? 20.00045 18.62943 3.59964   1.000 15.87287 ? 95  ILE B N    1 
ATOM   3399 C  CA   . ILE B 1 99  ? 20.47368 18.27189 4.93135   1.000 16.63808 ? 95  ILE B CA   1 
ATOM   3400 C  C    . ILE B 1 99  ? 20.52041 16.76058 5.10171   1.000 18.45458 ? 95  ILE B C    1 
ATOM   3401 O  O    . ILE B 1 99  ? 21.46430 16.22298 5.69290   1.000 19.18725 ? 95  ILE B O    1 
ATOM   3402 C  CB   . ILE B 1 99  ? 19.60520 18.97205 5.98845   1.000 17.15599 ? 95  ILE B CB   1 
ATOM   3403 C  CG1  . ILE B 1 99  ? 19.94412 20.46417 6.01734   1.000 16.83535 ? 95  ILE B CG1  1 
ATOM   3404 C  CG2  . ILE B 1 99  ? 19.77180 18.30105 7.36720   1.000 19.50693 ? 95  ILE B CG2  1 
ATOM   3405 C  CD1  . ILE B 1 99  ? 18.96117 21.31473 6.74294   1.000 18.22153 ? 95  ILE B CD1  1 
ATOM   3406 H  H    . ILE B 1 99  ? 19.24728 19.04446 3.59025   1.000 19.07217 ? 95  ILE B H    1 
ATOM   3407 H  HA   . ILE B 1 99  ? 21.38445 18.58595 5.04436   1.000 19.99043 ? 95  ILE B HA   1 
ATOM   3408 H  HB   . ILE B 1 99  ? 18.66921 18.88304 5.74989   1.000 20.61191 ? 95  ILE B HB   1 
ATOM   3409 H  HG12 . ILE B 1 99  ? 20.80369 20.57608 6.45268   1.000 20.22715 ? 95  ILE B HG12 1 
ATOM   3410 H  HG13 . ILE B 1 99  ? 19.99040 20.78693 5.10378   1.000 20.22715 ? 95  ILE B HG13 1 
ATOM   3411 H  HG21 . ILE B 1 99  ? 19.45799 18.90940 8.05447   1.000 23.43305 ? 95  ILE B HG21 1 
ATOM   3412 H  HG22 . ILE B 1 99  ? 19.24998 17.48357 7.38569   1.000 23.43305 ? 95  ILE B HG22 1 
ATOM   3413 H  HG23 . ILE B 1 99  ? 20.70975 18.09801 7.50833   1.000 23.43305 ? 95  ILE B HG23 1 
ATOM   3414 H  HD11 . ILE B 1 99  ? 19.18600 22.24770 6.60179   1.000 21.89056 ? 95  ILE B HD11 1 
ATOM   3415 H  HD12 . ILE B 1 99  ? 18.07231 21.13310 6.39966   1.000 21.89056 ? 95  ILE B HD12 1 
ATOM   3416 H  HD13 . ILE B 1 99  ? 18.99963 21.10471 7.68915   1.000 21.89056 ? 95  ILE B HD13 1 
ATOM   3417 N  N    . ALA B 1 100 ? 19.51873 16.05200 4.57347   1.000 18.30068 ? 96  ALA B N    1 
ATOM   3418 C  CA   . ALA B 1 100 ? 19.54875 14.59572 4.61161   1.000 20.04181 ? 96  ALA B CA   1 
ATOM   3419 C  C    . ALA B 1 100 ? 20.76373 14.05222 3.86560   1.000 19.66274 ? 96  ALA B C    1 
ATOM   3420 O  O    . ALA B 1 100 ? 21.43495 13.13291 4.34806   1.000 21.43784 ? 96  ALA B O    1 
ATOM   3421 C  CB   . ALA B 1 100 ? 18.25208 14.04021 4.01867   1.000 21.86817 ? 96  ALA B CB   1 
ATOM   3422 H  H    . ALA B 1 100 ? 18.82268 16.38529 4.19395   1.000 21.98554 ? 96  ALA B H    1 
ATOM   3423 H  HA   . ALA B 1 100 ? 19.61028 14.29987 5.53335   1.000 24.07490 ? 96  ALA B HA   1 
ATOM   3424 H  HB1  . ALA B 1 100 ? 18.27716 13.07127 4.05661   1.000 26.26653 ? 96  ALA B HB1  1 
ATOM   3425 H  HB2  . ALA B 1 100 ? 17.50106 14.37214 4.53508   1.000 26.26653 ? 96  ALA B HB2  1 
ATOM   3426 H  HB3  . ALA B 1 100 ? 18.17522 14.33328 3.09720   1.000 26.26653 ? 96  ALA B HB3  1 
ATOM   3427 N  N    . TYR B 1 101 ? 21.06612 14.60496 2.68353   1.000 18.37046 ? 97  TYR B N    1 
ATOM   3428 C  CA   . TYR B 1 101 ? 22.25747 14.17651 1.95305   1.000 19.21427 ? 97  TYR B CA   1 
ATOM   3429 C  C    . TYR B 1 101 ? 23.52782 14.44651 2.76157   1.000 20.91632 ? 97  TYR B C    1 
ATOM   3430 O  O    . TYR B 1 101 ? 24.40172 13.57954 2.87619   1.000 21.71272 ? 97  TYR B O    1 
ATOM   3431 C  CB   . TYR B 1 101 ? 22.32621 14.84880 0.57363   1.000 18.96416 ? 97  TYR B CB   1 
ATOM   3432 C  CG   . TYR B 1 101 ? 23.68322 14.66743 -0.07614  1.000 19.13520 ? 97  TYR B CG   1 
ATOM   3433 C  CD1  . TYR B 1 101 ? 24.04723 13.45684 -0.64398  1.000 19.97998 ? 97  TYR B CD1  1 
ATOM   3434 C  CD2  . TYR B 1 101 ? 24.61311 15.69702 -0.08651  1.000 19.07096 ? 97  TYR B CD2  1 
ATOM   3435 C  CE1  . TYR B 1 101 ? 25.29432 13.27783 -1.20153  1.000 20.56297 ? 97  TYR B CE1  1 
ATOM   3436 C  CE2  . TYR B 1 101 ? 25.87339 15.51864 -0.64335  1.000 17.95421 ? 97  TYR B CE2  1 
ATOM   3437 C  CZ   . TYR B 1 101 ? 26.19988 14.31664 -1.20239  1.000 20.47108 ? 97  TYR B CZ   1 
ATOM   3438 O  OH   . TYR B 1 101 ? 27.44406 14.15471 -1.76751  1.000 22.23286 ? 97  TYR B OH   1 
ATOM   3439 H  H    . TYR B 1 101 ? 20.60674 15.21728 2.29156   1.000 22.06928 ? 97  TYR B H    1 
ATOM   3440 H  HA   . TYR B 1 101 ? 22.19471 13.22030 1.80258   1.000 23.08185 ? 97  TYR B HA   1 
ATOM   3441 H  HB2  . TYR B 1 101 ? 21.65614 14.45523 -0.00689  1.000 22.78172 ? 97  TYR B HB2  1 
ATOM   3442 H  HB3  . TYR B 1 101 ? 22.16158 15.79950 0.67346   1.000 22.78172 ? 97  TYR B HB3  1 
ATOM   3443 H  HD1  . TYR B 1 101 ? 23.43922 12.75313 -0.64877  1.000 24.00070 ? 97  TYR B HD1  1 
ATOM   3444 H  HD2  . TYR B 1 101 ? 24.38927 16.51961 0.28517   1.000 22.90988 ? 97  TYR B HD2  1 
ATOM   3445 H  HE1  . TYR B 1 101 ? 25.52436 12.45833 -1.57623  1.000 24.70029 ? 97  TYR B HE1  1 
ATOM   3446 H  HE2  . TYR B 1 101 ? 26.49098 16.21393 -0.63534  1.000 21.56978 ? 97  TYR B HE2  1 
ATOM   3447 H  HH   . TYR B 1 101 ? 27.51872 13.37871 -2.08033  1.000 26.70416 ? 97  TYR B HH   1 
ATOM   3448 N  N    . LEU B 1 102 ? 23.64647 15.64218 3.33900   1.000 18.16571 ? 98  LEU B N    1 
ATOM   3449 C  CA   . LEU B 1 102 ? 24.85011 15.96336 4.10167   1.000 18.06314 ? 98  LEU B CA   1 
ATOM   3450 C  C    . LEU B 1 102 ? 25.02053 15.03791 5.29394   1.000 20.38905 ? 98  LEU B C    1 
ATOM   3451 O  O    . LEU B 1 102 ? 26.14627 14.66368 5.63554   1.000 21.37590 ? 98  LEU B O    1 
ATOM   3452 C  CB   . LEU B 1 102 ? 24.78595 17.40558 4.57597   1.000 17.05533 ? 98  LEU B CB   1 
ATOM   3453 C  CG   . LEU B 1 102 ? 24.93813 18.48898 3.51837   1.000 17.93445 ? 98  LEU B CG   1 
ATOM   3454 C  CD1  . LEU B 1 102 ? 24.63906 19.84664 4.13979   1.000 18.83089 ? 98  LEU B CD1  1 
ATOM   3455 C  CD2  . LEU B 1 102 ? 26.32197 18.45664 2.89139   1.000 19.50389 ? 98  LEU B CD2  1 
ATOM   3456 H  H    . LEU B 1 102 ? 23.06056 16.27087 3.30646   1.000 21.82358 ? 98  LEU B H    1 
ATOM   3457 H  HA   . LEU B 1 102 ? 25.62009 15.85531 3.52170   1.000 21.70050 ? 98  LEU B HA   1 
ATOM   3458 H  HB2  . LEU B 1 102 ? 23.92379 17.54245 4.99887   1.000 20.49112 ? 98  LEU B HB2  1 
ATOM   3459 H  HB3  . LEU B 1 102 ? 25.49721 17.53911 5.22185   1.000 20.49112 ? 98  LEU B HB3  1 
ATOM   3460 H  HG   . LEU B 1 102 ? 24.30600 18.33327 2.79929   1.000 21.54607 ? 98  LEU B HG   1 
ATOM   3461 H  HD11 . LEU B 1 102 ? 24.67055 20.52487 3.44703   1.000 22.62180 ? 98  LEU B HD11 1 
ATOM   3462 H  HD12 . LEU B 1 102 ? 23.75569 19.82317 4.53981   1.000 22.62180 ? 98  LEU B HD12 1 
ATOM   3463 H  HD13 . LEU B 1 102 ? 25.30487 20.03656 4.81915   1.000 22.62180 ? 98  LEU B HD13 1 
ATOM   3464 H  HD21 . LEU B 1 102 ? 26.43727 19.24614 2.33976   1.000 23.42939 ? 98  LEU B HD21 1 
ATOM   3465 H  HD22 . LEU B 1 102 ? 26.98797 18.44566 3.59653   1.000 23.42939 ? 98  LEU B HD22 1 
ATOM   3466 H  HD23 . LEU B 1 102 ? 26.40344 17.65797 2.34698   1.000 23.42939 ? 98  LEU B HD23 1 
ATOM   3467 N  N    . LYS B 1 103 ? 23.91645 14.67428 5.94855   1.000 20.98618 ? 99  LYS B N    1 
ATOM   3468 C  CA   . LYS B 1 103 ? 24.00878 13.76926 7.09142   1.000 23.70555 ? 99  LYS B CA   1 
ATOM   3469 C  C    . LYS B 1 103 ? 24.60993 12.42725 6.67706   1.000 24.76585 ? 99  LYS B C    1 
ATOM   3470 O  O    . LYS B 1 103 ? 25.40122 11.83308 7.41713   1.000 28.84327 ? 99  LYS B O    1 
ATOM   3471 C  CB   . LYS B 1 103 ? 22.62965 13.59010 7.73148   1.000 27.54490 ? 99  LYS B CB   1 
ATOM   3472 C  CG   . LYS B 1 103 ? 22.66493 13.06195 9.15452   1.000 30.05844 ? 99  LYS B CG   1 
ATOM   3473 C  CD   . LYS B 1 103 ? 21.25323 12.73921 9.64304   1.000 30.82939 ? 99  LYS B CD   1 
ATOM   3474 C  CE   B LYS B 1 103 ? 21.24139 12.21390 11.06847  0.368 30.40905 ? 99  LYS B CE   1 
ATOM   3475 N  NZ   B LYS B 1 103 ? 21.34871 13.30587 12.07415  0.368 31.03132 ? 99  LYS B NZ   1 
ATOM   3476 H  H    . LYS B 1 103 ? 23.11835 14.93086 5.75671   1.000 25.20814 ? 99  LYS B H    1 
ATOM   3477 H  HA   . LYS B 1 103 ? 24.59107 14.15798 7.76279   1.000 28.47139 ? 99  LYS B HA   1 
ATOM   3478 H  HB2  . LYS B 1 103 ? 22.18200 14.45046 7.74843   1.000 33.07860 ? 99  LYS B HB2  1 
ATOM   3479 H  HB3  . LYS B 1 103 ? 22.11967 12.96125 7.19728   1.000 33.07860 ? 99  LYS B HB3  1 
ATOM   3480 H  HG2  . LYS B 1 103 ? 23.19577 12.25074 9.18681   1.000 36.09485 ? 99  LYS B HG2  1 
ATOM   3481 H  HG3  . LYS B 1 103 ? 23.04852 13.73299 9.74058   1.000 36.09485 ? 99  LYS B HG3  1 
ATOM   3482 H  HD2  . LYS B 1 103 ? 20.71470 13.54548 9.61460   1.000 37.02000 ? 99  LYS B HD2  1 
ATOM   3483 H  HD3  . LYS B 1 103 ? 20.86524 12.06066 9.06865   1.000 37.02000 ? 99  LYS B HD3  1 
ATOM   3484 H  HE2  . LYS B 1 103 ? 20.40993 11.73972 11.22573  1.000 36.51559 ? 99  LYS B HE2  1 
ATOM   3485 H  HE3  . LYS B 1 103 ? 21.99379 11.61444 11.19272  1.000 36.51559 ? 99  LYS B HE3  1 
ATOM   3486 H  HZ1  . LYS B 1 103 ? 21.44016 12.96090 12.88946  1.000 37.26231 ? 99  LYS B HZ1  1 
ATOM   3487 H  HZ2  . LYS B 1 103 ? 22.05580 13.81593 11.89537  1.000 37.26231 ? 99  LYS B HZ2  1 
ATOM   3488 H  HZ3  . LYS B 1 103 ? 20.61603 13.81074 12.05465  1.000 37.26231 ? 99  LYS B HZ3  1 
ATOM   3489 N  N    . SER B 1 104 ? 24.27223 11.95127 5.48084   1.000 23.58046 ? 100 SER B N    1 
ATOM   3490 C  CA   . SER B 1 104 ? 24.84675 10.70598 4.98197   1.000 26.31646 ? 100 SER B CA   1 
ATOM   3491 C  C    . SER B 1 104 ? 26.27600 10.90740 4.48625   1.000 26.51608 ? 100 SER B C    1 
ATOM   3492 O  O    . SER B 1 104 ? 27.18552 10.15206 4.84830   1.000 27.83994 ? 100 SER B O    1 
ATOM   3493 C  CB   . SER B 1 104 ? 23.97402 10.15672 3.85369   1.000 29.45094 ? 100 SER B CB   1 
ATOM   3494 O  OG   . SER B 1 104 ? 24.57330 9.02143  3.24709   1.000 34.14512 ? 100 SER B OG   1 
ATOM   3495 H  H    . SER B 1 104 ? 23.71710 12.32623 4.94154   1.000 28.32128 ? 100 SER B H    1 
ATOM   3496 H  HA   . SER B 1 104 ? 24.86761 10.05958 5.70491   1.000 31.60448 ? 100 SER B HA   1 
ATOM   3497 H  HB2  . SER B 1 104 ? 23.11285 9.90007  4.21894   1.000 35.36586 ? 100 SER B HB2  1 
ATOM   3498 H  HB3  . SER B 1 104 ? 23.85722 10.84693 3.18223   1.000 35.36586 ? 100 SER B HB3  1 
ATOM   3499 H  HG   . SER B 1 104 ? 24.10699 8.76277  2.59805   1.000 40.99887 ? 100 SER B HG   1 
ATOM   3500 N  N    . ALA B 1 105 ? 26.49700 11.93091 3.66620   1.000 26.26564 ? 101 ALA B N    1 
ATOM   3501 C  CA   . ALA B 1 105 ? 27.76174 12.04446 2.95229   1.000 23.51736 ? 101 ALA B CA   1 
ATOM   3502 C  C    . ALA B 1 105 ? 28.91665 12.51933 3.82765   1.000 25.26224 ? 101 ALA B C    1 
ATOM   3503 O  O    . ALA B 1 105 ? 30.06960 12.21490 3.51836   1.000 28.22556 ? 101 ALA B O    1 
ATOM   3504 C  CB   . ALA B 1 105 ? 27.60388 12.99269 1.77183   1.000 23.33491 ? 101 ALA B CB   1 
ATOM   3505 H  H    . ALA B 1 105 ? 25.93860 12.56534 3.50716   1.000 31.54350 ? 101 ALA B H    1 
ATOM   3506 H  HA   . ALA B 1 105 ? 27.99303 11.16106 2.62515   1.000 28.24556 ? 101 ALA B HA   1 
ATOM   3507 H  HB1  . ALA B 1 105 ? 28.42954 13.00352 1.26285   1.000 28.02662 ? 101 ALA B HB1  1 
ATOM   3508 H  HB2  . ALA B 1 105 ? 26.87464 12.68215 1.21264   1.000 28.02662 ? 101 ALA B HB2  1 
ATOM   3509 H  HB3  . ALA B 1 105 ? 27.40920 13.88250 2.10536   1.000 28.02662 ? 101 ALA B HB3  1 
ATOM   3510 N  N    . THR B 1 106 ? 28.65842 13.28759 4.88370   1.000 24.74994 ? 102 THR B N    1 
ATOM   3511 C  CA   . THR B 1 106 ? 29.74276 13.80435 5.71827   1.000 24.92291 ? 102 THR B CA   1 
ATOM   3512 C  C    . THR B 1 106 ? 30.04950 12.92877 6.92311   1.000 27.28614 ? 102 THR B C    1 
ATOM   3513 O  O    . THR B 1 106 ? 30.94298 13.27354 7.70712   1.000 27.74011 ? 102 THR B O    1 
ATOM   3514 C  CB   . THR B 1 106 ? 29.42393 15.21513 6.21900   1.000 24.86100 ? 102 THR B CB   1 
ATOM   3515 O  OG1  . THR B 1 106 ? 28.34472 15.16504 7.16349   1.000 22.74758 ? 102 THR B OG1  1 
ATOM   3516 C  CG2  . THR B 1 106 ? 29.06109 16.13932 5.07983   1.000 24.18401 ? 102 THR B CG2  1 
ATOM   3517 H  H    . THR B 1 106 ? 27.86982 13.52130 5.13487   1.000 29.72466 ? 102 THR B H    1 
ATOM   3518 H  HA   . THR B 1 106 ? 30.53491 13.84995 5.16031   1.000 29.93222 ? 102 THR B HA   1 
ATOM   3519 H  HB   . THR B 1 106 ? 30.21307 15.57855 6.65037   1.000 29.85793 ? 102 THR B HB   1 
ATOM   3520 H  HG1  . THR B 1 106 ? 27.70058 14.73294 6.84105   1.000 27.32182 ? 102 THR B HG1  1 
ATOM   3521 H  HG21 . THR B 1 106 ? 29.04604 17.05825 5.39006   1.000 29.04554 ? 102 THR B HG21 1 
ATOM   3522 H  HG22 . THR B 1 106 ? 29.71336 16.05855 4.36645   1.000 29.04554 ? 102 THR B HG22 1 
ATOM   3523 H  HG23 . THR B 1 106 ? 28.18488 15.90988 4.73268   1.000 29.04554 ? 102 THR B HG23 1 
ATOM   3524 N  N    . LYS B 1 107 ? 29.34508 11.81669 7.09021   1.000 32.26205 ? 103 LYS B N    1 
ATOM   3525 C  CA   . LYS B 1 107 ? 29.47899 11.01616 8.29305   1.000 37.38532 ? 103 LYS B CA   1 
ATOM   3526 C  C    . LYS B 1 107 ? 30.78954 10.24337 8.28974   1.000 39.41174 ? 103 LYS B C    1 
ATOM   3527 O  O    . LYS B 1 107 ? 31.29674 9.84495  7.24057   1.000 42.15785 ? 103 LYS B O    1 
ATOM   3528 C  CB   . LYS B 1 107 ? 28.30516 10.04941 8.44308   1.000 39.53105 ? 103 LYS B CB   1 
ATOM   3529 C  CG   . LYS B 1 107 ? 28.13920 9.57101  9.87483   1.000 43.62509 ? 103 LYS B CG   1 
ATOM   3530 C  CD   . LYS B 1 107 ? 27.05482 8.53186  10.03309  1.000 46.53758 ? 103 LYS B CD   1 
ATOM   3531 C  CE   . LYS B 1 107 ? 26.89909 8.16600  11.50663  1.000 48.54738 ? 103 LYS B CE   1 
ATOM   3532 N  NZ   . LYS B 1 107 ? 25.83663 7.16226  11.73090  1.000 50.79039 ? 103 LYS B NZ   1 
ATOM   3533 O  OXT  . LYS B 1 107 ? 31.36953 10.00983 9.34829   1.000 42.12212 ? 103 LYS B OXT  1 
ATOM   3534 H  H    . LYS B 1 107 ? 28.78234 11.50598 6.51890   1.000 38.73919 ? 103 LYS B H    1 
ATOM   3535 H  HA   . LYS B 1 107 ? 29.47467 11.60889 9.06087   1.000 44.88711 ? 103 LYS B HA   1 
ATOM   3536 H  HB2  . LYS B 1 107 ? 27.48741 10.49785 8.17645   1.000 47.46199 ? 103 LYS B HB2  1 
ATOM   3537 H  HB3  . LYS B 1 107 ? 28.45722 9.27431  7.88004   1.000 47.46199 ? 103 LYS B HB3  1 
ATOM   3538 H  HG2  . LYS B 1 107 ? 28.97398 9.17802  10.17417  1.000 52.37484 ? 103 LYS B HG2  1 
ATOM   3539 H  HG3  . LYS B 1 107 ? 27.90943 10.32867 10.43524  1.000 52.37484 ? 103 LYS B HG3  1 
ATOM   3540 H  HD2  . LYS B 1 107 ? 26.21193 8.88595  9.70895   1.000 55.86983 ? 103 LYS B HD2  1 
ATOM   3541 H  HD3  . LYS B 1 107 ? 27.29181 7.73285  9.53678   1.000 55.86983 ? 103 LYS B HD3  1 
ATOM   3542 H  HE2  . LYS B 1 107 ? 27.73507 7.79708  11.83209  1.000 58.28159 ? 103 LYS B HE2  1 
ATOM   3543 H  HE3  . LYS B 1 107 ? 26.67045 8.96354  12.00919  1.000 58.28159 ? 103 LYS B HE3  1 
ATOM   3544 H  HZ1  . LYS B 1 107 ? 25.71426 7.03836  12.60370  1.000 60.97319 ? 103 LYS B HZ1  1 
ATOM   3545 H  HZ2  . LYS B 1 107 ? 25.07295 7.44129  11.36891  1.000 60.97319 ? 103 LYS B HZ2  1 
ATOM   3546 H  HZ3  . LYS B 1 107 ? 26.06656 6.38726  11.35859  1.000 60.97319 ? 103 LYS B HZ3  1 
HETATM 3547 FE FE   . HEC C 2 .   ? 23.30019 32.50193 -16.90092 1.000 11.46743 ? 201 HEC A FE   1 
HETATM 3548 C  CHA  . HEC C 2 .   ? 21.70372 34.60081 -19.14501 1.000 10.94708 ? 201 HEC A CHA  1 
HETATM 3549 C  CHB  . HEC C 2 .   ? 25.32831 31.38367 -19.38394 1.000 11.42329 ? 201 HEC A CHB  1 
HETATM 3550 C  CHC  . HEC C 2 .   ? 25.18643 30.81371 -14.56777 1.000 12.63675 ? 201 HEC A CHC  1 
HETATM 3551 C  CHD  . HEC C 2 .   ? 20.96504 33.24626 -14.54671 1.000 13.14846 ? 201 HEC A CHD  1 
HETATM 3552 N  NA   . HEC C 2 .   ? 23.49179 32.95375 -18.85960 1.000 11.67576 ? 201 HEC A NA   1 
HETATM 3553 C  C1A  . HEC C 2 .   ? 22.78396 33.85180 -19.60164 1.000 11.17252 ? 201 HEC A C1A  1 
HETATM 3554 C  C2A  . HEC C 2 .   ? 23.32940 33.91974 -20.91007 1.000 11.39812 ? 201 HEC A C2A  1 
HETATM 3555 C  C3A  . HEC C 2 .   ? 24.30540 32.93318 -21.00835 1.000 11.44052 ? 201 HEC A C3A  1 
HETATM 3556 C  C4A  . HEC C 2 .   ? 24.41508 32.39095 -19.69455 1.000 10.77544 ? 201 HEC A C4A  1 
HETATM 3557 C  CMA  . HEC C 2 .   ? 25.17107 32.62179 -22.20239 1.000 12.12233 ? 201 HEC A CMA  1 
HETATM 3558 C  CAA  . HEC C 2 .   ? 22.73761 34.74433 -22.06205 1.000 12.31890 ? 201 HEC A CAA  1 
HETATM 3559 C  CBA  . HEC C 2 .   ? 21.65345 33.96558 -22.79671 1.000 11.73090 ? 201 HEC A CBA  1 
HETATM 3560 C  CGA  . HEC C 2 .   ? 21.06122 34.65812 -24.00443 1.000 11.32861 ? 201 HEC A CGA  1 
HETATM 3561 O  O1A  . HEC C 2 .   ? 21.38544 35.83161 -24.29469 1.000 11.79015 ? 201 HEC A O1A  1 
HETATM 3562 O  O2A  . HEC C 2 .   ? 20.10642 34.05458 -24.56984 1.000 12.54936 ? 201 HEC A O2A  1 
HETATM 3563 N  NB   . HEC C 2 .   ? 24.97166 31.30317 -16.93853 1.000 10.81703 ? 201 HEC A NB   1 
HETATM 3564 C  C1B  . HEC C 2 .   ? 25.57913 30.91781 -18.09794 1.000 11.25289 ? 201 HEC A C1B  1 
HETATM 3565 C  C2B  . HEC C 2 .   ? 26.55553 29.93425 -17.78923 1.000 12.21155 ? 201 HEC A C2B  1 
HETATM 3566 C  C3B  . HEC C 2 .   ? 26.59017 29.81582 -16.40415 1.000 12.39713 ? 201 HEC A C3B  1 
HETATM 3567 C  C4B  . HEC C 2 .   ? 25.59275 30.69329 -15.89253 1.000 11.37030 ? 201 HEC A C4B  1 
HETATM 3568 C  CMB  . HEC C 2 .   ? 27.38003 29.18693 -18.79917 1.000 11.84374 ? 201 HEC A CMB  1 
HETATM 3569 C  CAB  . HEC C 2 .   ? 27.58369 29.00578 -15.56098 1.000 13.04329 ? 201 HEC A CAB  1 
HETATM 3570 C  CBB  . HEC C 2 .   ? 29.02119 29.54108 -15.69840 1.000 13.55201 ? 201 HEC A CBB  1 
HETATM 3571 N  NC   . HEC C 2 .   ? 23.12986 32.08930 -14.94052 1.000 12.35450 ? 201 HEC A NC   1 
HETATM 3572 C  C1C  . HEC C 2 .   ? 24.02841 31.43732 -14.13620 1.000 12.47411 ? 201 HEC A C1C  1 
HETATM 3573 C  C2C  . HEC C 2 .   ? 23.47466 31.27613 -12.83493 1.000 13.85290 ? 201 HEC A C2C  1 
HETATM 3574 C  C3C  . HEC C 2 .   ? 22.26756 31.97740 -12.82889 1.000 14.02590 ? 201 HEC A C3C  1 
HETATM 3575 C  C4C  . HEC C 2 .   ? 22.06193 32.46013 -14.15962 1.000 12.02584 ? 201 HEC A C4C  1 
HETATM 3576 C  CMC  . HEC C 2 .   ? 24.17743 30.64542 -11.65278 1.000 14.84446 ? 201 HEC A CMC  1 
HETATM 3577 C  CAC  . HEC C 2 .   ? 21.16772 31.87801 -11.74633 1.000 14.52566 ? 201 HEC A CAC  1 
HETATM 3578 C  CBC  . HEC C 2 .   ? 21.62409 32.36883 -10.35994 1.000 14.54858 ? 201 HEC A CBC  1 
HETATM 3579 N  ND   . HEC C 2 .   ? 21.62080 33.71841 -16.87253 1.000 11.32302 ? 201 HEC A ND   1 
HETATM 3580 C  C1D  . HEC C 2 .   ? 20.77821 33.84449 -15.80262 1.000 11.36134 ? 201 HEC A C1D  1 
HETATM 3581 C  C2D  . HEC C 2 .   ? 19.79067 34.81624 -16.08692 1.000 12.62487 ? 201 HEC A C2D  1 
HETATM 3582 C  C3D  . HEC C 2 .   ? 19.96828 35.18914 -17.40452 1.000 11.61876 ? 201 HEC A C3D  1 
HETATM 3583 C  C4D  . HEC C 2 .   ? 21.12734 34.51496 -17.87868 1.000 11.89129 ? 201 HEC A C4D  1 
HETATM 3584 C  CMD  . HEC C 2 .   ? 18.73621 35.31257 -15.13139 1.000 13.00392 ? 201 HEC A CMD  1 
HETATM 3585 C  CAD  . HEC C 2 .   ? 19.22920 36.32597 -18.14775 1.000 13.17792 ? 201 HEC A CAD  1 
HETATM 3586 C  CBD  . HEC C 2 .   ? 19.93503 37.64370 -17.88318 1.000 13.67905 ? 201 HEC A CBD  1 
HETATM 3587 C  CGD  . HEC C 2 .   ? 19.22233 38.87653 -18.37240 1.000 12.89119 ? 201 HEC A CGD  1 
HETATM 3588 O  O1D  . HEC C 2 .   ? 18.08409 38.78753 -18.88771 1.000 13.35231 ? 201 HEC A O1D  1 
HETATM 3589 O  O2D  . HEC C 2 .   ? 19.78650 39.96943 -18.14566 1.000 14.02472 ? 201 HEC A O2D  1 
HETATM 3590 H  HHA  . HEC C 2 .   ? 21.31303 35.24677 -19.76991 1.000 13.16123 ? 201 HEC A HHA  1 
HETATM 3591 H  HHB  . HEC C 2 .   ? 25.82737 30.97634 -20.12247 1.000 13.73267 ? 201 HEC A HHB  1 
HETATM 3592 H  HHC  . HEC C 2 .   ? 25.76881 30.42441 -13.88244 1.000 15.18883 ? 201 HEC A HHC  1 
HETATM 3593 H  HHD  . HEC C 2 .   ? 20.26409 33.39089 -13.87727 1.000 15.80288 ? 201 HEC A HHD  1 
HETATM 3594 H  HMA1 . HEC C 2 .   ? 26.11516 32.67971 -21.94600 1.000 14.57152 ? 201 HEC A HMA1 1 
HETATM 3595 H  HMA2 . HEC C 2 .   ? 24.98698 33.26666 -22.91700 1.000 14.57152 ? 201 HEC A HMA2 1 
HETATM 3596 H  HMA3 . HEC C 2 .   ? 24.97470 31.71628 -22.52159 1.000 14.57152 ? 201 HEC A HMA3 1 
HETATM 3597 H  HAA1 . HEC C 2 .   ? 23.44499 34.96793 -22.68696 1.000 14.80741 ? 201 HEC A HAA1 1 
HETATM 3598 H  HAA2 . HEC C 2 .   ? 22.35333 35.55931 -21.70283 1.000 14.80741 ? 201 HEC A HAA2 1 
HETATM 3599 H  HBA1 . HEC C 2 .   ? 20.93421 33.79049 -22.16986 1.000 14.10181 ? 201 HEC A HBA1 1 
HETATM 3600 H  HBA2 . HEC C 2 .   ? 22.03716 33.12515 -23.09224 1.000 14.10181 ? 201 HEC A HBA2 1 
HETATM 3601 H  HMB1 . HEC C 2 .   ? 27.55468 28.28972 -18.47448 1.000 14.23722 ? 201 HEC A HMB1 1 
HETATM 3602 H  HMB2 . HEC C 2 .   ? 28.22121 29.64992 -18.93684 1.000 14.23722 ? 201 HEC A HMB2 1 
HETATM 3603 H  HMB3 . HEC C 2 .   ? 26.89716 29.13807 -19.63902 1.000 14.23722 ? 201 HEC A HMB3 1 
HETATM 3604 H  HAB  . HEC C 2 .   ? 27.32003 29.04806 -14.63886 1.000 15.67668 ? 201 HEC A HAB  1 
HETATM 3605 H  HBB1 . HEC C 2 .   ? 29.59553 29.06685 -15.07700 1.000 16.28715 ? 201 HEC A HBB1 1 
HETATM 3606 H  HBB2 . HEC C 2 .   ? 29.02577 30.48954 -15.49513 1.000 16.28715 ? 201 HEC A HBB2 1 
HETATM 3607 H  HBB3 . HEC C 2 .   ? 29.32658 29.39617 -16.60759 1.000 16.28715 ? 201 HEC A HBB3 1 
HETATM 3608 H  HMC1 . HEC C 2 .   ? 23.52367 30.21736 -11.07810 1.000 17.83808 ? 201 HEC A HMC1 1 
HETATM 3609 H  HMC2 . HEC C 2 .   ? 24.64774 31.33052 -11.15244 1.000 17.83808 ? 201 HEC A HMC2 1 
HETATM 3610 H  HMC3 . HEC C 2 .   ? 24.81208 29.98344 -11.96885 1.000 17.83808 ? 201 HEC A HMC3 1 
HETATM 3611 H  HAC  . HEC C 2 .   ? 20.39406 32.37305 -12.02559 1.000 17.45552 ? 201 HEC A HAC  1 
HETATM 3612 H  HBC1 . HEC C 2 .   ? 20.84328 32.50874 -9.80168  1.000 17.48303 ? 201 HEC A HBC1 1 
HETATM 3613 H  HBC2 . HEC C 2 .   ? 22.10988 33.20194 -10.46403 1.000 17.48303 ? 201 HEC A HBC2 1 
HETATM 3614 H  HBC3 . HEC C 2 .   ? 22.19990 31.69778 -9.96115  1.000 17.48303 ? 201 HEC A HBC3 1 
HETATM 3615 H  HMD1 . HEC C 2 .   ? 18.00570 35.72664 -15.63666 1.000 15.62943 ? 201 HEC A HMD1 1 
HETATM 3616 H  HMD2 . HEC C 2 .   ? 19.12961 35.97442 -14.52509 1.000 15.62943 ? 201 HEC A HMD2 1 
HETATM 3617 H  HMD3 . HEC C 2 .   ? 18.38667 34.55986 -14.61019 1.000 15.62943 ? 201 HEC A HMD3 1 
HETATM 3618 H  HAD1 . HEC C 2 .   ? 18.31445 36.37935 -17.82949 1.000 15.83824 ? 201 HEC A HAD1 1 
HETATM 3619 H  HAD2 . HEC C 2 .   ? 19.23044 36.14390 -19.10051 1.000 15.83824 ? 201 HEC A HAD2 1 
HETATM 3620 H  HBD1 . HEC C 2 .   ? 20.80218 37.60932 -18.31651 1.000 16.43959 ? 201 HEC A HBD1 1 
HETATM 3621 H  HBD2 . HEC C 2 .   ? 20.05530 37.72991 -16.92454 1.000 16.43959 ? 201 HEC A HBD2 1 
HETATM 3622 C  C1   . EOH D 3 .   ? 25.78437 40.66716 -8.82706  1.000 37.12340 ? 202 EOH A C1   1 
HETATM 3623 C  C2   . EOH D 3 .   ? 26.40112 42.05643 -8.80921  1.000 37.30506 ? 202 EOH A C2   1 
HETATM 3624 O  O    . EOH D 3 .   ? 26.51408 39.75653 -9.62789  1.000 37.49282 ? 202 EOH A O    1 
HETATM 3625 H  H11  . EOH D 3 .   ? 24.76460 40.73569 -9.20582  1.000 44.57281 ? 202 EOH A H11  1 
HETATM 3626 H  H12  . EOH D 3 .   ? 25.73798 40.28560 -7.80708  1.000 44.57281 ? 202 EOH A H12  1 
HETATM 3627 H  H21  . EOH D 3 .   ? 25.70670 42.75627 -8.34434  1.000 44.79080 ? 202 EOH A H21  1 
HETATM 3628 H  H22  . EOH D 3 .   ? 26.60862 42.37496 -9.83077  1.000 44.79080 ? 202 EOH A H22  1 
HETATM 3629 H  H23  . EOH D 3 .   ? 27.33026 42.03416 -8.23973  1.000 44.79080 ? 202 EOH A H23  1 
HETATM 3630 H  HO   . EOH D 3 .   ? 27.45256 39.75271 -9.34569  1.000 45.01611 ? 202 EOH A HO   1 
HETATM 3631 FE FE   . HEC E 2 .   ? 29.60262 27.20267 2.34608   1.000 15.65741 ? 201 HEC B FE   1 
HETATM 3632 C  CHA  . HEC E 2 .   ? 31.21648 27.87093 5.26576   1.000 16.18881 ? 201 HEC B CHA  1 
HETATM 3633 C  CHB  . HEC E 2 .   ? 27.66473 24.87768 3.92798   1.000 13.60595 ? 201 HEC B CHB  1 
HETATM 3634 C  CHC  . HEC E 2 .   ? 27.71022 26.85971 -0.45833  1.000 16.12925 ? 201 HEC B CHC  1 
HETATM 3635 C  CHD  . HEC E 2 .   ? 31.82167 29.14144 0.64705   1.000 16.51531 ? 201 HEC B CHD  1 
HETATM 3636 N  NA   . HEC E 2 .   ? 29.46255 26.52328 4.21363   1.000 14.96898 ? 201 HEC B NA   1 
HETATM 3637 C  C1A  . HEC E 2 .   ? 30.17623 26.94092 5.31527   1.000 15.38241 ? 201 HEC B C1A  1 
HETATM 3638 C  C2A  . HEC E 2 .   ? 29.69492 26.33851 6.51519   1.000 14.51385 ? 201 HEC B C2A  1 
HETATM 3639 C  C3A  . HEC E 2 .   ? 28.72818 25.42401 6.11166   1.000 14.94437 ? 201 HEC B C3A  1 
HETATM 3640 C  C4A  . HEC E 2 .   ? 28.60526 25.57932 4.70420   1.000 14.12460 ? 201 HEC B C4A  1 
HETATM 3641 C  CMA  . HEC E 2 .   ? 27.91586 24.49157 6.97518   1.000 14.93678 ? 201 HEC B CMA  1 
HETATM 3642 C  CAA  . HEC E 2 .   ? 30.35605 26.43467 7.90869   1.000 16.19543 ? 201 HEC B CAA  1 
HETATM 3643 C  CBA  . HEC E 2 .   ? 31.42783 25.35746 8.07030   1.000 16.35588 ? 201 HEC B CBA  1 
HETATM 3644 C  CGA  . HEC E 2 .   ? 32.17960 25.41336 9.37816   1.000 15.90287 ? 201 HEC B CGA  1 
HETATM 3645 O  O1A  . HEC E 2 .   ? 31.82578 26.22666 10.28654  1.000 17.08064 ? 201 HEC B O1A  1 
HETATM 3646 O  O2A  . HEC E 2 .   ? 33.11287 24.56938 9.49245   1.000 18.02159 ? 201 HEC B O2A  1 
HETATM 3647 N  NB   . HEC E 2 .   ? 28.00892 26.06078 1.82629   1.000 14.61603 ? 201 HEC B NB   1 
HETATM 3648 C  C1B  . HEC E 2 .   ? 27.42488 25.07414 2.56108   1.000 14.82242 ? 201 HEC B C1B  1 
HETATM 3649 C  C2B  . HEC E 2 .   ? 26.38952 24.39055 1.83326   1.000 14.34121 ? 201 HEC B C2B  1 
HETATM 3650 C  C3B  . HEC E 2 .   ? 26.32444 25.03285 0.59675   1.000 13.98402 ? 201 HEC B C3B  1 
HETATM 3651 C  C4B  . HEC E 2 .   ? 27.34047 26.05749 0.62670   1.000 14.03270 ? 201 HEC B C4B  1 
HETATM 3652 C  CMB  . HEC E 2 .   ? 25.61914 23.18246 2.32447   1.000 14.38256 ? 201 HEC B CMB  1 
HETATM 3653 C  CAB  . HEC E 2 .   ? 25.34753 24.72711 -0.55916  1.000 14.69743 ? 201 HEC B CAB  1 
HETATM 3654 C  CBB  . HEC E 2 .   ? 23.93150 25.11073 -0.11637  1.000 14.23772 ? 201 HEC B CBB  1 
HETATM 3655 N  NC   . HEC E 2 .   ? 29.67891 27.95147 0.51205   1.000 15.68720 ? 201 HEC B NC   1 
HETATM 3656 C  C1C  . HEC E 2 .   ? 28.80918 27.72062 -0.53144  1.000 15.50172 ? 201 HEC B C1C  1 
HETATM 3657 C  C2C  . HEC E 2 .   ? 29.27316 28.33240 -1.75368  1.000 16.27730 ? 201 HEC B C2C  1 
HETATM 3658 C  C3C  . HEC E 2 .   ? 30.46916 28.95827 -1.43735  1.000 17.67710 ? 201 HEC B C3C  1 
HETATM 3659 C  C4C  . HEC E 2 .   ? 30.72351 28.63940 -0.05847  1.000 16.24778 ? 201 HEC B C4C  1 
HETATM 3660 C  CMC  . HEC E 2 .   ? 28.62758 28.24629 -3.12368  1.000 17.83286 ? 201 HEC B CMC  1 
HETATM 3661 C  CAC  . HEC E 2 .   ? 31.49474 29.53470 -2.44122  1.000 18.53273 ? 201 HEC B CAC  1 
HETATM 3662 C  CBC  . HEC E 2 .   ? 30.97623 30.62521 -3.39571  1.000 20.74697 ? 201 HEC B CBC  1 
HETATM 3663 N  ND   . HEC E 2 .   ? 31.24289 28.26857 2.86972   1.000 16.54883 ? 201 HEC B ND   1 
HETATM 3664 C  C1D  . HEC E 2 .   ? 32.02199 29.01389 2.03170   1.000 17.23218 ? 201 HEC B C1D  1 
HETATM 3665 C  C2D  . HEC E 2 .   ? 33.08045 29.64938 2.74357   1.000 19.59123 ? 201 HEC B C2D  1 
HETATM 3666 C  C3D  . HEC E 2 .   ? 32.94125 29.26761 4.08477   1.000 17.64396 ? 201 HEC B C3D  1 
HETATM 3667 C  C4D  . HEC E 2 .   ? 31.78639 28.41782 4.11977   1.000 16.27936 ? 201 HEC B C4D  1 
HETATM 3668 C  CMD  . HEC E 2 .   ? 34.09343 30.62042 2.18783   1.000 20.46923 ? 201 HEC B CMD  1 
HETATM 3669 C  CAD  . HEC E 2 .   ? 33.67222 29.87721 5.30707   1.000 19.03215 ? 201 HEC B CAD  1 
HETATM 3670 C  CBD  . HEC E 2 .   ? 32.92178 31.09368 5.82770   1.000 18.72257 ? 201 HEC B CBD  1 
HETATM 3671 C  CGD  . HEC E 2 .   ? 33.69327 31.90308 6.83698   1.000 18.81700 ? 201 HEC B CGD  1 
HETATM 3672 O  O1D  . HEC E 2 .   ? 34.84342 31.55414 7.24802   1.000 20.67436 ? 201 HEC B O1D  1 
HETATM 3673 O  O2D  . HEC E 2 .   ? 33.10907 32.94344 7.22624   1.000 20.44885 ? 201 HEC B O2D  1 
HETATM 3674 H  HHA  . HEC E 2 .   ? 31.58232 28.16872 6.12475   1.000 19.45130 ? 201 HEC B HHA  1 
HETATM 3675 H  HHB  . HEC E 2 .   ? 27.13128 24.19247 4.38220   1.000 16.35187 ? 201 HEC B HHB  1 
HETATM 3676 H  HHC  . HEC E 2 .   ? 27.13741 26.81309 -1.25213  1.000 19.37983 ? 201 HEC B HHC  1 
HETATM 3677 H  HHD  . HEC E 2 .   ? 32.50608 29.62046 0.13468   1.000 19.84310 ? 201 HEC B HHD  1 
HETATM 3678 H  HMA1 . HEC E 2 .   ? 27.01977 24.86561 7.10752   1.000 17.94886 ? 201 HEC B HMA1 1 
HETATM 3679 H  HMA2 . HEC E 2 .   ? 28.35594 24.38376 7.84415   1.000 17.94886 ? 201 HEC B HMA2 1 
HETATM 3680 H  HMA3 . HEC E 2 .   ? 27.84332 23.61863 6.53573   1.000 17.94886 ? 201 HEC B HMA3 1 
HETATM 3681 H  HAA1 . HEC E 2 .   ? 29.67816 26.31493 8.59209   1.000 19.45925 ? 201 HEC B HAA1 1 
HETATM 3682 H  HAA2 . HEC E 2 .   ? 30.76499 27.30864 8.00789   1.000 19.45925 ? 201 HEC B HAA2 1 
HETATM 3683 H  HBA1 . HEC E 2 .   ? 32.06815 25.45666 7.34847   1.000 19.65179 ? 201 HEC B HBA1 1 
HETATM 3684 H  HBA2 . HEC E 2 .   ? 30.99797 24.49036 8.00493   1.000 19.65179 ? 201 HEC B HBA2 1 
HETATM 3685 H  HMB1 . HEC E 2 .   ? 25.54876 22.53068 1.60953   1.000 17.28380 ? 201 HEC B HMB1 1 
HETATM 3686 H  HMB2 . HEC E 2 .   ? 24.73043 23.45563 2.60098   1.000 17.28380 ? 201 HEC B HMB2 1 
HETATM 3687 H  HMB3 . HEC E 2 .   ? 26.08420 22.78629 3.07791   1.000 17.28380 ? 201 HEC B HMB3 1 
HETATM 3688 H  HAB  . HEC E 2 .   ? 25.59659 25.21590 -1.34698  1.000 17.66164 ? 201 HEC B HAB  1 
HETATM 3689 H  HBB1 . HEC E 2 .   ? 23.33095 25.02974 -0.87378  1.000 17.11000 ? 201 HEC B HBB1 1 
HETATM 3690 H  HBB2 . HEC E 2 .   ? 23.93800 26.02621 0.20420   1.000 17.11000 ? 201 HEC B HBB2 1 
HETATM 3691 H  HBB3 . HEC E 2 .   ? 23.65013 24.51342 0.59423   1.000 17.11000 ? 201 HEC B HBB3 1 
HETATM 3692 H  HMC1 . HEC E 2 .   ? 29.31191 28.10057 -3.79552  1.000 21.42416 ? 201 HEC B HMC1 1 
HETATM 3693 H  HMC2 . HEC E 2 .   ? 28.15966 29.07443 -3.31376  1.000 21.42416 ? 201 HEC B HMC2 1 
HETATM 3694 H  HMC3 . HEC E 2 .   ? 27.99778 27.50872 -3.13907  1.000 21.42416 ? 201 HEC B HMC3 1 
HETATM 3695 H  HAC  . HEC E 2 .   ? 32.23581 29.89192 -1.94643  1.000 22.26400 ? 201 HEC B HAC  1 
HETATM 3696 H  HBC1 . HEC E 2 .   ? 31.71554 31.19882 -3.65123  1.000 24.92109 ? 201 HEC B HBC1 1 
HETATM 3697 H  HBC2 . HEC E 2 .   ? 30.29573 31.14560 -2.94073  1.000 24.92109 ? 201 HEC B HBC2 1 
HETATM 3698 H  HBC3 . HEC E 2 .   ? 30.59827 30.20243 -4.18267  1.000 24.92109 ? 201 HEC B HBC3 1 
HETATM 3699 H  HMD1 . HEC E 2 .   ? 34.86394 30.67049 2.79133   1.000 24.58781 ? 201 HEC B HMD1 1 
HETATM 3700 H  HMD2 . HEC E 2 .   ? 33.68530 31.50759 2.10561   1.000 24.58781 ? 201 HEC B HMD2 1 
HETATM 3701 H  HMD3 . HEC E 2 .   ? 34.38975 30.31461 1.30518   1.000 24.58781 ? 201 HEC B HMD3 1 
HETATM 3702 H  HAD1 . HEC E 2 .   ? 34.56682 30.14355 5.04314   1.000 22.86331 ? 201 HEC B HAD1 1 
HETATM 3703 H  HAD2 . HEC E 2 .   ? 33.72684 29.21141 6.01036   1.000 22.86331 ? 201 HEC B HAD2 1 
HETATM 3704 H  HBD1 . HEC E 2 .   ? 32.10009 30.78993 6.24418   1.000 22.49181 ? 201 HEC B HBD1 1 
HETATM 3705 H  HBD2 . HEC E 2 .   ? 32.71026 31.66700 5.07440   1.000 22.49181 ? 201 HEC B HBD2 1 
HETATM 3706 O  O    . HOH F 4 .   ? 43.63349 28.92771 -16.42112 1.000 30.96809 ? 301 HOH A O    1 
HETATM 3707 O  O    . HOH F 4 .   ? 31.07147 40.17579 -11.42548 1.000 40.50656 ? 302 HOH A O    1 
HETATM 3708 O  O    . HOH F 4 .   ? 36.22485 40.75936 -18.16539 1.000 33.21641 ? 303 HOH A O    1 
HETATM 3709 O  O    . HOH F 4 .   ? 34.39857 45.26775 -20.77710 1.000 50.57349 ? 304 HOH A O    1 
HETATM 3710 O  O    . HOH F 4 .   ? 31.49983 20.61470 -30.43639 1.000 38.21074 ? 305 HOH A O    1 
HETATM 3711 O  O    . HOH F 4 .   ? 37.55461 29.93084 -12.86667 1.000 32.28206 ? 306 HOH A O    1 
HETATM 3712 O  O    . HOH F 4 .   ? 32.96769 20.99594 -28.16243 1.000 21.90379 ? 307 HOH A O    1 
HETATM 3713 O  O    . HOH F 4 .   ? 34.35878 39.27878 -26.83249 1.000 45.60301 ? 308 HOH A O    1 
HETATM 3714 O  O    . HOH F 4 .   ? 38.40369 36.96465 -21.08657 1.000 36.07771 ? 309 HOH A O    1 
HETATM 3715 O  O    . HOH F 4 .   ? 40.83712 34.04117 -25.99317 1.000 42.71311 ? 310 HOH A O    1 
HETATM 3716 O  O    . HOH F 4 .   ? 17.88295 22.85797 -10.51230 1.000 44.33381 ? 311 HOH A O    1 
HETATM 3717 O  O    . HOH F 4 .   ? 24.26160 33.54133 -7.98052  1.000 39.78637 ? 312 HOH A O    1 
HETATM 3718 O  O    . HOH F 4 .   ? 38.82829 35.64504 -27.73982 1.000 33.29274 ? 313 HOH A O    1 
HETATM 3719 O  O    . HOH F 4 .   ? 34.29606 44.40177 -24.72929 1.000 51.50434 ? 314 HOH A O    1 
HETATM 3720 O  O    . HOH F 4 .   ? 25.81221 40.04624 -12.15432 1.000 24.32766 ? 315 HOH A O    1 
HETATM 3721 O  O    . HOH F 4 .   ? 14.47210 35.05569 -14.08188 1.000 31.95792 ? 316 HOH A O    1 
HETATM 3722 O  O    . HOH F 4 .   ? 32.02099 41.44587 -27.99034 1.000 25.41166 ? 317 HOH A O    1 
HETATM 3723 O  O    . HOH F 4 .   ? 18.99987 46.16695 -15.92900 1.000 37.28940 ? 318 HOH A O    1 
HETATM 3724 O  O    . HOH F 4 .   ? 19.66884 34.17946 -27.17872 1.000 14.81053 ? 319 HOH A O    1 
HETATM 3725 O  O    . HOH F 4 .   ? 29.01186 46.51695 -14.80170 1.000 40.06381 ? 320 HOH A O    1 
HETATM 3726 O  O    . HOH F 4 .   ? 35.65837 25.92327 -30.32480 1.000 33.37309 ? 321 HOH A O    1 
HETATM 3727 O  O    . HOH F 4 .   ? 23.50215 22.41448 -34.32844 1.000 32.83609 ? 322 HOH A O    1 
HETATM 3728 O  O    . HOH F 4 .   ? 34.40424 34.32180 -9.27701  1.000 47.70948 ? 323 HOH A O    1 
HETATM 3729 O  O    . HOH F 4 .   ? 36.78241 41.36555 -14.77976 1.000 37.61155 ? 324 HOH A O    1 
HETATM 3730 O  O    . HOH F 4 .   ? 21.72757 19.68109 -27.92154 1.000 23.44793 ? 325 HOH A O    1 
HETATM 3731 O  O    . HOH F 4 .   ? 33.76884 42.79369 -20.75367 1.000 21.27121 ? 326 HOH A O    1 
HETATM 3732 O  O    A HOH F 4 .   ? 43.63851 23.69490 -25.00375 0.496 22.70292 ? 327 HOH A O    1 
HETATM 3733 O  O    B HOH F 4 .   ? 43.26284 22.94797 -23.25205 0.504 25.11726 ? 327 HOH A O    1 
HETATM 3734 O  O    . HOH F 4 .   ? 40.13814 36.50385 -14.68332 1.000 28.99753 ? 328 HOH A O    1 
HETATM 3735 O  O    . HOH F 4 .   ? 31.31725 47.54626 -19.39853 1.000 18.23054 ? 329 HOH A O    1 
HETATM 3736 O  O    . HOH F 4 .   ? 24.33176 47.27783 -27.89274 1.000 19.26086 ? 330 HOH A O    1 
HETATM 3737 O  O    . HOH F 4 .   ? 19.68291 31.11352 -24.56648 1.000 20.01762 ? 331 HOH A O    1 
HETATM 3738 O  O    . HOH F 4 .   ? 17.76460 28.84397 -26.06539 0.994 16.75469 ? 332 HOH A O    1 
HETATM 3739 O  O    . HOH F 4 .   ? 11.07212 26.68495 -14.25540 1.000 40.31905 ? 333 HOH A O    1 
HETATM 3740 O  O    . HOH F 4 .   ? 27.18467 29.41828 -9.73089  1.000 27.15238 ? 334 HOH A O    1 
HETATM 3741 O  O    . HOH F 4 .   ? 20.13822 20.48171 -19.08078 1.000 35.65210 ? 335 HOH A O    1 
HETATM 3742 O  O    . HOH F 4 .   ? 36.92088 19.69502 -27.31219 1.000 35.84255 ? 336 HOH A O    1 
HETATM 3743 O  O    . HOH F 4 .   ? 38.58749 22.84015 -15.82794 1.000 28.11949 ? 337 HOH A O    1 
HETATM 3744 O  O    . HOH F 4 .   ? 37.89080 26.99461 -30.00192 1.000 25.84431 ? 338 HOH A O    1 
HETATM 3745 O  O    . HOH F 4 .   ? 36.05256 32.92397 -33.37334 1.000 22.66065 ? 339 HOH A O    1 
HETATM 3746 O  O    . HOH F 4 .   ? 31.27440 28.89302 -33.25402 1.000 28.63165 ? 340 HOH A O    1 
HETATM 3747 O  O    . HOH F 4 .   ? 28.10222 23.81252 -6.83655  1.000 17.72131 ? 341 HOH A O    1 
HETATM 3748 O  O    . HOH F 4 .   ? 41.72061 22.55523 -18.08470 1.000 30.68788 ? 342 HOH A O    1 
HETATM 3749 O  O    . HOH F 4 .   ? 11.83792 31.68720 -16.43645 1.000 22.27258 ? 343 HOH A O    1 
HETATM 3750 O  O    . HOH F 4 .   ? 16.66767 28.33740 -11.29303 1.000 18.64211 ? 344 HOH A O    1 
HETATM 3751 O  O    . HOH F 4 .   ? 36.86457 43.87210 -22.65777 1.000 52.18050 ? 345 HOH A O    1 
HETATM 3752 O  O    . HOH F 4 .   ? 24.77302 26.03361 -29.86348 1.000 14.61074 ? 346 HOH A O    1 
HETATM 3753 O  O    . HOH F 4 .   ? 32.52465 26.50053 -35.06592 1.000 34.19494 ? 347 HOH A O    1 
HETATM 3754 O  O    . HOH F 4 .   ? 24.25082 47.02048 -20.85815 1.000 17.74901 ? 348 HOH A O    1 
HETATM 3755 O  O    . HOH F 4 .   ? 12.38519 35.84131 -25.24248 1.000 30.61307 ? 349 HOH A O    1 
HETATM 3756 O  O    . HOH F 4 .   ? 20.41847 21.82878 -16.09888 1.000 23.70272 ? 350 HOH A O    1 
HETATM 3757 O  O    . HOH F 4 .   ? 33.45010 40.50324 -19.07953 1.000 17.40449 ? 351 HOH A O    1 
HETATM 3758 O  O    . HOH F 4 .   ? 19.91565 41.03821 -29.20837 1.000 18.95899 ? 352 HOH A O    1 
HETATM 3759 O  O    . HOH F 4 .   ? 27.74414 37.89943 -7.98880  1.000 44.50987 ? 353 HOH A O    1 
HETATM 3760 O  O    . HOH F 4 .   ? 38.69442 14.60583 -18.56379 1.000 40.45746 ? 354 HOH A O    1 
HETATM 3761 O  O    . HOH F 4 .   ? 12.93667 36.21624 -16.08687 1.000 23.77991 ? 355 HOH A O    1 
HETATM 3762 O  O    . HOH F 4 .   ? 8.12018  35.29595 -20.35739 1.000 35.03188 ? 356 HOH A O    1 
HETATM 3763 O  O    . HOH F 4 .   ? 11.32546 40.94778 -20.34678 1.000 37.38699 ? 357 HOH A O    1 
HETATM 3764 O  O    . HOH F 4 .   ? 31.63510 44.69550 -25.59214 1.000 40.01695 ? 358 HOH A O    1 
HETATM 3765 O  O    . HOH F 4 .   ? 13.97222 17.61211 -27.39978 0.785 31.19034 ? 359 HOH A O    1 
HETATM 3766 O  O    . HOH F 4 .   ? 31.80526 15.47320 -16.15765 1.000 34.35885 ? 360 HOH A O    1 
HETATM 3767 O  O    . HOH F 4 .   ? 33.98822 42.53546 -26.93887 1.000 47.13883 ? 361 HOH A O    1 
HETATM 3768 O  O    . HOH F 4 .   ? 27.02202 24.76905 -31.05996 1.000 15.99830 ? 362 HOH A O    1 
HETATM 3769 O  O    . HOH F 4 .   ? 22.99604 38.40813 -19.80085 1.000 17.28174 ? 363 HOH A O    1 
HETATM 3770 O  O    . HOH F 4 .   ? 14.84411 24.78641 -26.33004 1.000 14.76412 ? 364 HOH A O    1 
HETATM 3771 O  O    . HOH F 4 .   ? 17.95832 37.51108 -11.25988 1.000 40.63060 ? 365 HOH A O    1 
HETATM 3772 O  O    . HOH F 4 .   ? 33.64850 19.11876 -6.66748  1.000 33.33403 ? 366 HOH A O    1 
HETATM 3773 O  O    . HOH F 4 .   ? 36.98735 25.91200 -25.73610 1.000 18.94057 ? 367 HOH A O    1 
HETATM 3774 O  O    . HOH F 4 .   ? 37.22862 36.87110 -26.03142 1.000 22.03783 ? 368 HOH A O    1 
HETATM 3775 O  O    . HOH F 4 .   ? 36.60413 14.79017 -22.22768 1.000 35.36660 ? 369 HOH A O    1 
HETATM 3776 O  O    . HOH F 4 .   ? 41.37441 20.96722 -21.14230 1.000 34.64685 ? 370 HOH A O    1 
HETATM 3777 O  O    . HOH F 4 .   ? 41.89471 17.93030 -19.90812 1.000 46.28372 ? 371 HOH A O    1 
HETATM 3778 O  O    . HOH F 4 .   ? 22.44728 43.21271 -33.03846 1.000 33.90827 ? 372 HOH A O    1 
HETATM 3779 O  O    . HOH F 4 .   ? 36.19370 20.81847 -14.29829 1.000 26.60126 ? 373 HOH A O    1 
HETATM 3780 O  O    . HOH F 4 .   ? 28.66285 39.46995 -13.01643 1.000 19.80962 ? 374 HOH A O    1 
HETATM 3781 O  O    . HOH F 4 .   ? 42.61836 35.36948 -32.18287 1.000 43.10771 ? 375 HOH A O    1 
HETATM 3782 O  O    . HOH F 4 .   ? 11.63499 25.81980 -23.39476 1.000 29.24167 ? 376 HOH A O    1 
HETATM 3783 O  O    . HOH F 4 .   ? 24.39178 42.24491 -12.50401 1.000 33.90091 ? 377 HOH A O    1 
HETATM 3784 O  O    . HOH F 4 .   ? 25.81157 40.28724 -33.74890 1.000 36.76058 ? 378 HOH A O    1 
HETATM 3785 O  O    . HOH F 4 .   ? 17.00879 27.05407 -18.07580 1.000 13.82267 ? 379 HOH A O    1 
HETATM 3786 O  O    . HOH F 4 .   ? 28.86674 25.83020 -32.84051 1.000 22.17834 ? 380 HOH A O    1 
HETATM 3787 O  O    . HOH F 4 .   ? 40.67195 24.56966 -21.57634 1.000 31.51408 ? 381 HOH A O    1 
HETATM 3788 O  O    . HOH F 4 .   ? 20.50010 35.32302 -11.70866 1.000 19.26886 ? 382 HOH A O    1 
HETATM 3789 O  O    . HOH F 4 .   ? 15.71609 17.25613 -26.29604 0.451 17.39969 ? 383 HOH A O    1 
HETATM 3790 O  O    . HOH F 4 .   ? 38.25807 31.56887 -30.92456 1.000 21.29711 ? 384 HOH A O    1 
HETATM 3791 O  O    . HOH F 4 .   ? 12.17167 46.50133 -24.43731 1.000 22.87765 ? 385 HOH A O    1 
HETATM 3792 O  O    . HOH F 4 .   ? 23.97771 19.39179 -18.00215 1.000 38.68201 ? 386 HOH A O    1 
HETATM 3793 O  O    . HOH F 4 .   ? 18.86551 18.89663 -27.59817 1.000 19.34978 ? 387 HOH A O    1 
HETATM 3794 O  O    A HOH F 4 .   ? 30.60020 12.05567 -18.14993 0.594 22.52632 ? 388 HOH A O    1 
HETATM 3795 O  O    B HOH F 4 .   ? 32.21226 13.33415 -18.04295 0.406 30.02890 ? 388 HOH A O    1 
HETATM 3796 O  O    . HOH F 4 .   ? 26.58732 27.28587 -8.05599  1.000 42.64896 ? 389 HOH A O    1 
HETATM 3797 O  O    . HOH F 4 .   ? 23.46013 18.02447 -24.40513 1.000 17.87112 ? 390 HOH A O    1 
HETATM 3798 O  O    . HOH F 4 .   ? 17.65099 25.36302 -9.01794  1.000 41.07513 ? 391 HOH A O    1 
HETATM 3799 O  O    . HOH F 4 .   ? 33.34065 23.74780 -11.00241 1.000 34.25093 ? 392 HOH A O    1 
HETATM 3800 O  O    . HOH F 4 .   ? 30.35429 36.96415 -32.35248 1.000 25.74788 ? 393 HOH A O    1 
HETATM 3801 O  O    . HOH F 4 .   ? 40.67391 26.38746 -23.29978 1.000 25.01595 ? 394 HOH A O    1 
HETATM 3802 O  O    . HOH F 4 .   ? 22.41306 29.89540 -34.50278 1.000 24.52875 ? 395 HOH A O    1 
HETATM 3803 O  O    . HOH F 4 .   ? 18.12331 29.07602 -8.76168  1.000 41.25429 ? 396 HOH A O    1 
HETATM 3804 O  O    . HOH F 4 .   ? 37.16197 22.29484 -27.62890 1.000 26.60742 ? 397 HOH A O    1 
HETATM 3805 O  O    . HOH F 4 .   ? 21.91374 32.99577 -28.51672 1.000 24.66809 ? 398 HOH A O    1 
HETATM 3806 O  O    . HOH F 4 .   ? 28.51914 33.52731 -8.45215  1.000 29.06068 ? 399 HOH A O    1 
HETATM 3807 O  O    . HOH F 4 .   ? 16.62029 21.32733 -14.23436 1.000 42.96741 ? 400 HOH A O    1 
HETATM 3808 O  O    . HOH F 4 .   ? 23.87871 45.78668 -23.25932 1.000 18.51309 ? 401 HOH A O    1 
HETATM 3809 O  O    . HOH F 4 .   ? 14.00432 20.68337 -18.70026 1.000 26.84919 ? 402 HOH A O    1 
HETATM 3810 O  O    . HOH F 4 .   ? 13.21014 28.47485 -25.38138 1.000 39.47407 ? 403 HOH A O    1 
HETATM 3811 O  O    . HOH F 4 .   ? 9.89599  34.96353 -27.06359 1.000 35.72389 ? 404 HOH A O    1 
HETATM 3812 O  O    . HOH F 4 .   ? 14.90792 45.51855 -18.12416 1.000 29.08870 ? 405 HOH A O    1 
HETATM 3813 O  O    . HOH F 4 .   ? 12.24020 39.22922 -23.10478 1.000 27.69848 ? 406 HOH A O    1 
HETATM 3814 O  O    . HOH F 4 .   ? 42.09878 28.62596 -22.05249 1.000 25.77234 ? 407 HOH A O    1 
HETATM 3815 O  O    . HOH F 4 .   ? 36.39656 31.49823 -10.76389 1.000 36.44229 ? 408 HOH A O    1 
HETATM 3816 O  O    . HOH F 4 .   ? 23.45466 26.43062 -32.13392 1.000 26.87149 ? 409 HOH A O    1 
HETATM 3817 O  O    . HOH F 4 .   ? 29.13930 39.46199 -32.12920 1.000 32.18843 ? 410 HOH A O    1 
HETATM 3818 O  O    . HOH F 4 .   ? 30.69993 45.70169 -22.40243 1.000 21.01970 ? 411 HOH A O    1 
HETATM 3819 O  O    . HOH F 4 .   ? 23.45880 36.04027 -35.47109 1.000 43.38725 ? 412 HOH A O    1 
HETATM 3820 O  O    . HOH F 4 .   ? 11.47147 34.32715 -17.59659 1.000 20.26854 ? 413 HOH A O    1 
HETATM 3821 O  O    . HOH F 4 .   ? 17.67056 46.19408 -18.22234 1.000 26.66952 ? 414 HOH A O    1 
HETATM 3822 O  O    . HOH F 4 .   ? 34.39307 36.48012 -32.35047 1.000 49.71392 ? 415 HOH A O    1 
HETATM 3823 O  O    . HOH F 4 .   ? 10.21409 26.76272 -20.78494 1.000 28.48474 ? 416 HOH A O    1 
HETATM 3824 O  O    . HOH F 4 .   ? 35.42382 22.22827 -11.78358 1.000 35.12842 ? 417 HOH A O    1 
HETATM 3825 O  O    . HOH F 4 .   ? 32.59994 44.02517 -12.07918 1.000 51.10226 ? 418 HOH A O    1 
HETATM 3826 O  O    . HOH F 4 .   ? 28.96354 30.52865 -33.45155 1.000 31.64649 ? 419 HOH A O    1 
HETATM 3827 O  O    . HOH F 4 .   ? 31.18555 32.75302 -34.84837 0.830 40.52751 ? 420 HOH A O    1 
HETATM 3828 O  O    . HOH F 4 .   ? 18.76838 48.02336 -18.86115 1.000 44.73223 ? 421 HOH A O    1 
HETATM 3829 O  O    . HOH F 4 .   ? 29.80672 16.33375 -14.37976 1.000 41.36996 ? 422 HOH A O    1 
HETATM 3830 O  O    . HOH F 4 .   ? 36.82690 29.31434 -31.36079 1.000 30.14537 ? 423 HOH A O    1 
HETATM 3831 O  O    . HOH F 4 .   ? 8.38275  36.72793 -21.86098 1.000 39.28889 ? 424 HOH A O    1 
HETATM 3832 O  O    . HOH F 4 .   ? 15.35096 28.19597 -26.88414 1.000 43.12259 ? 425 HOH A O    1 
HETATM 3833 O  O    . HOH F 4 .   ? 11.85134 19.97665 -19.08537 1.000 38.79330 ? 426 HOH A O    1 
HETATM 3834 O  O    . HOH F 4 .   ? 10.85184 37.44456 -14.73822 1.000 47.23967 ? 427 HOH A O    1 
HETATM 3835 O  O    . HOH F 4 .   ? 35.44342 25.10576 -27.78258 1.000 27.38321 ? 428 HOH A O    1 
HETATM 3836 O  O    . HOH F 4 .   ? 9.65874  39.09881 -22.40281 1.000 44.59299 ? 429 HOH A O    1 
HETATM 3837 O  O    . HOH F 4 .   ? 30.43367 35.63441 -34.71019 1.000 42.51193 ? 430 HOH A O    1 
HETATM 3838 O  O    . HOH F 4 .   ? 32.49491 37.99038 -31.98756 1.000 49.48473 ? 431 HOH A O    1 
HETATM 3839 O  O    . HOH F 4 .   ? 28.92115 32.74482 -34.48583 1.000 41.64353 ? 432 HOH A O    1 
HETATM 3840 O  O    . HOH F 4 .   ? 26.47176 31.57447 -8.44708  1.000 40.49713 ? 433 HOH A O    1 
HETATM 3841 O  O    . HOH F 4 .   ? 18.32179 32.62134 -8.03269  1.000 42.26004 ? 434 HOH A O    1 
HETATM 3842 O  O    . HOH F 4 .   ? 14.21232 27.38506 -10.69350 1.000 40.40375 ? 435 HOH A O    1 
HETATM 3843 O  O    . HOH F 4 .   ? 36.82658 39.06704 -28.18608 1.000 52.35580 ? 436 HOH A O    1 
HETATM 3844 O  O    . HOH F 4 .   ? 26.80800 47.41662 -30.09256 1.000 50.46324 ? 437 HOH A O    1 
HETATM 3845 O  O    . HOH F 4 .   ? 38.48993 37.87433 -23.80048 1.000 43.55618 ? 438 HOH A O    1 
HETATM 3846 O  O    . HOH F 4 .   ? 20.77059 17.56165 -24.37687 1.000 27.33133 ? 439 HOH A O    1 
HETATM 3847 O  O    . HOH F 4 .   ? 8.55903  35.14313 -17.43619 1.000 50.28230 ? 440 HOH A O    1 
HETATM 3848 O  O    . HOH F 4 .   ? 37.37393 18.51525 -13.45861 1.000 42.14688 ? 441 HOH A O    1 
HETATM 3849 O  O    . HOH F 4 .   ? 38.61677 40.82252 -27.30669 1.000 49.89211 ? 442 HOH A O    1 
HETATM 3850 O  O    . HOH F 4 .   ? 43.18434 24.33785 -20.58498 1.000 48.31181 ? 443 HOH A O    1 
HETATM 3851 O  O    . HOH F 4 .   ? 31.49891 40.90418 -30.69957 1.000 34.89227 ? 444 HOH A O    1 
HETATM 3852 O  O    . HOH F 4 .   ? 25.56486 24.46626 -33.46357 1.000 31.40318 ? 445 HOH A O    1 
HETATM 3853 O  O    . HOH F 4 .   ? 31.74330 46.34833 -13.63547 1.000 47.00044 ? 446 HOH A O    1 
HETATM 3854 O  O    . HOH F 4 .   ? 15.06170 20.41307 -16.10696 1.000 54.35951 ? 447 HOH A O    1 
HETATM 3855 O  O    . HOH F 4 .   ? 24.15738 19.63580 -35.34048 1.000 34.78146 ? 448 HOH A O    1 
HETATM 3856 O  O    . HOH F 4 .   ? 35.26310 22.93129 -28.66900 1.000 30.72303 ? 449 HOH A O    1 
HETATM 3857 O  O    . HOH F 4 .   ? 30.11098 16.92937 -5.24115  1.000 36.37198 ? 450 HOH A O    1 
HETATM 3858 O  O    . HOH F 4 .   ? 33.74361 21.31081 -31.57257 1.000 34.91119 ? 451 HOH A O    1 
HETATM 3859 O  O    . HOH F 4 .   ? 24.37447 16.69655 -17.32415 1.000 54.13173 ? 452 HOH A O    1 
HETATM 3860 O  O    . HOH F 4 .   ? 19.45303 34.98225 -9.04659  1.000 28.83527 ? 453 HOH A O    1 
HETATM 3861 O  O    . HOH F 4 .   ? 20.71383 35.26197 -7.22803  1.000 52.63998 ? 454 HOH A O    1 
HETATM 3862 O  O    . HOH F 4 .   ? 35.21669 19.05721 -30.74058 1.000 34.30103 ? 455 HOH A O    1 
HETATM 3863 O  O    . HOH G 4 .   ? 31.42943 10.27345 5.10397   1.000 50.46473 ? 301 HOH B O    1 
HETATM 3864 O  O    . HOH G 4 .   ? 28.82888 17.67378 19.40088  1.000 37.46676 ? 302 HOH B O    1 
HETATM 3865 O  O    . HOH G 4 .   ? 27.09851 35.67512 2.38599   1.000 41.33959 ? 303 HOH B O    1 
HETATM 3866 O  O    . HOH G 4 .   ? 39.12913 20.11893 14.14826  1.000 42.72522 ? 304 HOH B O    1 
HETATM 3867 O  O    . HOH G 4 .   ? 30.47916 15.00682 15.24008  1.000 39.81167 ? 305 HOH B O    1 
HETATM 3868 O  O    . HOH G 4 .   ? 23.26864 22.48831 18.31695  1.000 49.08622 ? 306 HOH B O    1 
HETATM 3869 O  O    . HOH G 4 .   ? 41.72206 27.73966 11.07926  1.000 41.92034 ? 307 HOH B O    1 
HETATM 3870 O  O    . HOH G 4 .   ? 33.97736 39.39831 8.10975   1.000 44.77372 ? 308 HOH B O    1 
HETATM 3871 O  O    . HOH G 4 .   ? 15.91677 35.28206 5.93948   1.000 49.60733 ? 309 HOH B O    1 
HETATM 3872 O  O    . HOH G 4 .   ? 33.67426 23.35881 11.73835  1.000 18.95595 ? 310 HOH B O    1 
HETATM 3873 O  O    . HOH G 4 .   ? 38.39596 30.90074 1.14062   1.000 35.68286 ? 311 HOH B O    1 
HETATM 3874 O  O    . HOH G 4 .   ? 14.13428 28.67232 8.22918   1.000 27.43960 ? 312 HOH B O    1 
HETATM 3875 O  O    . HOH G 4 .   ? 33.63843 28.32244 17.10238  1.000 19.63413 ? 313 HOH B O    1 
HETATM 3876 O  O    . HOH G 4 .   ? 28.95054 15.18562 -3.67651  1.000 39.92870 ? 314 HOH B O    1 
HETATM 3877 O  O    . HOH G 4 .   ? 16.70153 32.83558 8.17540   1.000 42.42067 ? 315 HOH B O    1 
HETATM 3878 O  O    A HOH G 4 .   ? 34.84128 34.41729 0.22646   0.578 30.51369 ? 316 HOH B O    1 
HETATM 3879 O  O    B HOH G 4 .   ? 34.24338 35.90180 0.16812   0.422 31.74725 ? 316 HOH B O    1 
HETATM 3880 O  O    . HOH G 4 .   ? 11.27389 12.73377 -1.85860  1.000 43.11021 ? 317 HOH B O    1 
HETATM 3881 O  O    . HOH G 4 .   ? 15.66744 26.92327 -2.70007  1.000 37.60326 ? 318 HOH B O    1 
HETATM 3882 O  O    . HOH G 4 .   ? 41.60890 23.27750 -3.44080  1.000 38.72205 ? 319 HOH B O    1 
HETATM 3883 O  O    . HOH G 4 .   ? 9.86731  23.62636 -0.38693  1.000 25.65575 ? 320 HOH B O    1 
HETATM 3884 O  O    . HOH G 4 .   ? 36.03288 26.64620 -4.77555  1.000 26.19339 ? 321 HOH B O    1 
HETATM 3885 O  O    . HOH G 4 .   ? 24.42781 34.89371 17.18015  1.000 23.15291 ? 322 HOH B O    1 
HETATM 3886 O  O    . HOH G 4 .   ? 31.37578 34.77815 20.41887  1.000 19.62624 ? 323 HOH B O    1 
HETATM 3887 O  O    . HOH G 4 .   ? 12.78056 30.94419 2.79527   1.000 46.20538 ? 324 HOH B O    1 
HETATM 3888 O  O    . HOH G 4 .   ? 38.85224 35.34910 15.75324  1.000 19.72608 ? 325 HOH B O    1 
HETATM 3889 O  O    . HOH G 4 .   ? 40.27745 25.81507 11.37161  1.000 40.79498 ? 326 HOH B O    1 
HETATM 3890 O  O    . HOH G 4 .   ? 39.24939 27.96102 14.68724  1.000 33.30649 ? 327 HOH B O    1 
HETATM 3891 O  O    . HOH G 4 .   ? 28.32347 24.81252 20.16717  1.000 18.78525 ? 328 HOH B O    1 
HETATM 3892 O  O    . HOH G 4 .   ? 18.03190 13.67057 13.94146  1.000 51.53067 ? 329 HOH B O    1 
HETATM 3893 O  O    . HOH G 4 .   ? 29.08125 37.88946 13.38834  1.000 36.53591 ? 330 HOH B O    1 
HETATM 3894 O  O    . HOH G 4 .   ? 36.38888 18.83153 7.68587   1.000 44.97208 ? 331 HOH B O    1 
HETATM 3895 O  O    . HOH G 4 .   ? 28.04964 11.56710 -2.37315  1.000 33.70380 ? 332 HOH B O    1 
HETATM 3896 O  O    . HOH G 4 .   ? 40.86317 30.32087 10.99023  1.000 34.46812 ? 333 HOH B O    1 
HETATM 3897 O  O    . HOH G 4 .   ? 12.34963 18.16141 2.38576   1.000 24.85752 ? 334 HOH B O    1 
HETATM 3898 O  O    B HOH G 4 .   ? 33.48986 22.26651 8.06393   0.468 17.56716 ? 335 HOH B O    1 
HETATM 3899 O  O    . HOH G 4 .   ? 25.36793 28.06929 -5.39274  1.000 29.96096 ? 336 HOH B O    1 
HETATM 3900 O  O    . HOH G 4 .   ? 31.21907 27.55301 21.17645  1.000 24.29906 ? 337 HOH B O    1 
HETATM 3901 O  O    . HOH G 4 .   ? 36.19355 35.18684 16.40239  1.000 23.25636 ? 338 HOH B O    1 
HETATM 3902 O  O    . HOH G 4 .   ? 19.25555 20.79385 -13.37937 1.000 47.06700 ? 339 HOH B O    1 
HETATM 3903 O  O    . HOH G 4 .   ? 14.28751 19.50397 -3.09031  1.000 36.46807 ? 340 HOH B O    1 
HETATM 3904 O  O    . HOH G 4 .   ? 17.02915 17.74697 -6.07081  1.000 32.88457 ? 341 HOH B O    1 
HETATM 3905 O  O    . HOH G 4 .   ? 20.40537 28.33469 15.79568  1.000 29.36246 ? 342 HOH B O    1 
HETATM 3906 O  O    . HOH G 4 .   ? 24.00881 33.04608 -3.94326  1.000 42.28648 ? 343 HOH B O    1 
HETATM 3907 O  O    . HOH G 4 .   ? 38.72865 15.99562 5.70711   1.000 41.84250 ? 344 HOH B O    1 
HETATM 3908 O  O    . HOH G 4 .   ? 32.58286 18.62132 -4.05683  1.000 27.35364 ? 345 HOH B O    1 
HETATM 3909 O  O    . HOH G 4 .   ? 28.76209 14.59961 9.83669   1.000 29.53534 ? 346 HOH B O    1 
HETATM 3910 O  O    . HOH G 4 .   ? 27.73930 39.73577 6.22350   1.000 41.81879 ? 347 HOH B O    1 
HETATM 3911 O  O    . HOH G 4 .   ? 19.61291 32.55803 8.58723   1.000 23.63303 ? 348 HOH B O    1 
HETATM 3912 O  O    . HOH G 4 .   ? 33.94450 31.13832 19.56108  1.000 31.63986 ? 349 HOH B O    1 
HETATM 3913 O  O    . HOH G 4 .   ? 18.93229 31.31909 16.04315  1.000 27.94940 ? 350 HOH B O    1 
HETATM 3914 O  O    . HOH G 4 .   ? 24.67342 24.89998 -10.71080 1.000 15.32515 ? 351 HOH B O    1 
HETATM 3915 O  O    A HOH G 4 .   ? 38.58209 21.55665 16.59050  0.896 19.73062 ? 352 HOH B O    1 
HETATM 3916 O  O    . HOH G 4 .   ? 20.89827 12.88950 -7.39464  1.000 37.56381 ? 353 HOH B O    1 
HETATM 3917 O  O    . HOH G 4 .   ? 15.98730 16.95511 6.47463   1.000 25.39555 ? 354 HOH B O    1 
HETATM 3918 O  O    . HOH G 4 .   ? 11.83972 14.73049 0.33446   1.000 37.93395 ? 355 HOH B O    1 
HETATM 3919 O  O    . HOH G 4 .   ? 33.11503 15.68636 13.74598  1.000 39.77496 ? 356 HOH B O    1 
HETATM 3920 O  O    . HOH G 4 .   ? 12.32400 11.67203 3.27384   1.000 50.80989 ? 357 HOH B O    1 
HETATM 3921 O  O    . HOH G 4 .   ? 14.32790 24.24846 14.09946  1.000 28.63137 ? 358 HOH B O    1 
HETATM 3922 O  O    . HOH G 4 .   ? 15.02732 13.38098 6.74121   1.000 39.31276 ? 359 HOH B O    1 
HETATM 3923 O  O    . HOH G 4 .   ? 29.20320 35.62903 14.30687  1.000 36.37119 ? 360 HOH B O    1 
HETATM 3924 O  O    . HOH G 4 .   ? 20.35266 11.08955 5.94603   1.000 34.94234 ? 361 HOH B O    1 
HETATM 3925 O  O    . HOH G 4 .   ? 31.04674 10.91465 1.22010   1.000 42.16172 ? 362 HOH B O    1 
HETATM 3926 O  O    . HOH G 4 .   ? 11.41863 17.67449 -1.80780  1.000 36.68600 ? 363 HOH B O    1 
HETATM 3927 O  O    . HOH G 4 .   ? 18.68500 25.02365 -6.09857  1.000 34.79309 ? 364 HOH B O    1 
HETATM 3928 O  O    . HOH G 4 .   ? 30.03718 30.70727 7.98182   1.000 20.84089 ? 365 HOH B O    1 
HETATM 3929 O  O    . HOH G 4 .   ? 40.30076 34.56307 11.70104  1.000 41.86278 ? 366 HOH B O    1 
HETATM 3930 O  O    . HOH G 4 .   ? 9.33958  16.64060 3.54992   1.000 43.70035 ? 367 HOH B O    1 
HETATM 3931 O  O    . HOH G 4 .   ? 39.25813 33.98436 1.77265   1.000 57.15660 ? 368 HOH B O    1 
HETATM 3932 O  O    . HOH G 4 .   ? 15.94206 25.71842 12.34755  1.000 23.85389 ? 369 HOH B O    1 
HETATM 3933 O  O    . HOH G 4 .   ? 38.96060 16.65773 -2.72095  1.000 38.75422 ? 370 HOH B O    1 
HETATM 3934 O  O    . HOH G 4 .   ? 35.89109 22.11870 0.46567   1.000 22.56174 ? 371 HOH B O    1 
HETATM 3935 O  O    . HOH G 4 .   ? 24.40943 24.75450 18.57630  1.000 25.23712 ? 372 HOH B O    1 
HETATM 3936 O  O    . HOH G 4 .   ? 43.01894 24.51680 11.80721  1.000 28.63506 ? 373 HOH B O    1 
HETATM 3937 O  O    . HOH G 4 .   ? 32.39392 32.45168 -0.71795  1.000 26.52407 ? 374 HOH B O    1 
HETATM 3938 O  O    . HOH G 4 .   ? 41.33207 19.22883 3.83525   1.000 29.49094 ? 375 HOH B O    1 
HETATM 3939 O  O    . HOH G 4 .   ? 41.10500 26.97151 1.25864   1.000 31.81591 ? 376 HOH B O    1 
HETATM 3940 O  O    A HOH G 4 .   ? 12.12142 19.21308 13.20216  0.683 29.88978 ? 377 HOH B O    1 
HETATM 3941 O  O    B HOH G 4 .   ? 13.85951 19.07450 14.13519  0.317 22.35422 ? 377 HOH B O    1 
HETATM 3942 O  O    . HOH G 4 .   ? 40.12372 30.79609 3.29294   1.000 30.17203 ? 378 HOH B O    1 
HETATM 3943 O  O    . HOH G 4 .   ? 21.38388 39.12229 11.80213  1.000 37.31527 ? 379 HOH B O    1 
HETATM 3944 O  O    . HOH G 4 .   ? 33.78325 21.28386 17.61102  1.000 26.00559 ? 380 HOH B O    1 
HETATM 3945 O  O    . HOH G 4 .   ? 31.87441 19.97666 18.98294  1.000 23.44262 ? 381 HOH B O    1 
HETATM 3946 O  O    . HOH G 4 .   ? 22.56397 36.15442 13.93398  1.000 34.23144 ? 382 HOH B O    1 
HETATM 3947 O  O    . HOH G 4 .   ? 26.42974 12.85458 9.93419   1.000 34.73278 ? 383 HOH B O    1 
HETATM 3948 O  O    . HOH G 4 .   ? 24.01211 35.28550 2.91298   1.000 29.78125 ? 384 HOH B O    1 
HETATM 3949 O  O    . HOH G 4 .   ? 11.27117 28.09828 6.07444   1.000 36.94712 ? 385 HOH B O    1 
HETATM 3950 O  O    . HOH G 4 .   ? 16.65293 9.34616  1.63064   1.000 49.44017 ? 386 HOH B O    1 
HETATM 3951 O  O    . HOH G 4 .   ? 19.16214 39.52159 4.94539   1.000 34.95153 ? 387 HOH B O    1 
HETATM 3952 O  O    . HOH G 4 .   ? 12.28011 26.12843 11.32760  1.000 41.67883 ? 388 HOH B O    1 
HETATM 3953 O  O    . HOH G 4 .   ? 40.23642 25.79442 15.69109  1.000 32.37685 ? 389 HOH B O    1 
HETATM 3954 O  O    . HOH G 4 .   ? 33.29333 7.88172  8.47144   1.000 52.22421 ? 390 HOH B O    1 
HETATM 3955 O  O    . HOH G 4 .   ? 17.48353 8.72376  -1.71505  1.000 45.84362 ? 391 HOH B O    1 
HETATM 3956 O  O    . HOH G 4 .   ? 19.56500 22.73731 -7.15488  1.000 34.94112 ? 392 HOH B O    1 
HETATM 3957 O  O    . HOH G 4 .   ? 40.95898 23.71236 13.54374  1.000 33.98934 ? 393 HOH B O    1 
HETATM 3958 O  O    . HOH G 4 .   ? 32.69755 16.32769 -2.39573  1.000 38.55968 ? 394 HOH B O    1 
HETATM 3959 O  O    . HOH G 4 .   ? 9.75561  16.70297 10.40959  1.000 48.15937 ? 395 HOH B O    1 
HETATM 3960 O  O    . HOH G 4 .   ? 37.85765 37.90737 9.69420   1.000 33.90147 ? 396 HOH B O    1 
HETATM 3961 O  O    . HOH G 4 .   ? 19.05462 33.56483 11.31596  1.000 32.60822 ? 397 HOH B O    1 
HETATM 3962 O  O    . HOH G 4 .   ? 24.29426 12.42407 11.90102  1.000 47.88987 ? 398 HOH B O    1 
HETATM 3963 O  O    . HOH G 4 .   ? 8.41721  16.69203 7.11538   1.000 35.37166 ? 399 HOH B O    1 
HETATM 3964 O  O    . HOH G 4 .   ? 34.97019 38.56539 10.59610  1.000 30.56611 ? 400 HOH B O    1 
HETATM 3965 O  O    . HOH G 4 .   ? 41.65121 28.47563 3.64978   1.000 30.23354 ? 401 HOH B O    1 
HETATM 3966 O  O    . HOH G 4 .   ? 19.14268 19.04226 15.03275  1.000 49.19086 ? 402 HOH B O    1 
HETATM 3967 O  O    . HOH G 4 .   ? 20.68751 23.27415 18.11030  1.000 21.54565 ? 403 HOH B O    1 
HETATM 3968 O  O    . HOH G 4 .   ? 36.08362 28.16203 18.45184  1.000 33.33492 ? 404 HOH B O    1 
HETATM 3969 O  O    . HOH G 4 .   ? 13.99808 16.17841 9.85432   1.000 50.08348 ? 405 HOH B O    1 
HETATM 3970 O  O    . HOH G 4 .   ? 15.54613 38.73471 7.89001   1.000 44.77731 ? 406 HOH B O    1 
HETATM 3971 O  O    . HOH G 4 .   ? 38.69218 19.20495 7.89447   1.000 46.50016 ? 407 HOH B O    1 
HETATM 3972 O  O    . HOH G 4 .   ? 17.30710 29.19361 -3.55903  1.000 44.13485 ? 408 HOH B O    1 
HETATM 3973 O  O    . HOH G 4 .   ? 34.82347 28.76687 -6.37527  1.000 39.42625 ? 409 HOH B O    1 
HETATM 3974 O  O    . HOH G 4 .   ? 26.60468 30.46282 -5.63098  1.000 37.86207 ? 410 HOH B O    1 
HETATM 3975 O  O    . HOH G 4 .   ? 38.37095 28.62047 17.03722  1.000 33.17255 ? 411 HOH B O    1 
HETATM 3976 O  O    . HOH G 4 .   ? 30.50977 21.20271 20.87530  1.000 38.66960 ? 412 HOH B O    1 
HETATM 3977 O  O    . HOH G 4 .   ? 43.84655 33.48408 12.62405  1.000 34.05514 ? 413 HOH B O    1 
HETATM 3978 O  O    . HOH G 4 .   ? 42.63408 32.39445 10.06701  1.000 50.86875 ? 414 HOH B O    1 
HETATM 3979 O  O    . HOH G 4 .   ? 42.03687 32.30068 2.81676   1.000 46.52756 ? 415 HOH B O    1 
HETATM 3980 O  O    . HOH G 4 .   ? 30.49884 13.33844 11.63255  1.000 46.68885 ? 416 HOH B O    1 
HETATM 3981 O  O    . HOH G 4 .   ? 33.17167 29.48108 20.91163  1.000 33.45989 ? 417 HOH B O    1 
HETATM 3982 O  O    . HOH G 4 .   ? 36.33595 19.91024 17.22223  1.000 25.25264 ? 418 HOH B O    1 
HETATM 3983 O  O    . HOH G 4 .   ? 30.07603 23.75363 21.99273  1.000 22.63995 ? 419 HOH B O    1 
HETATM 3984 O  O    . HOH G 4 .   ? 14.40110 13.39678 11.94817  1.000 49.23572 ? 420 HOH B O    1 
HETATM 3985 O  O    . HOH G 4 .   ? 10.82078 22.51969 -2.84700  1.000 38.79933 ? 421 HOH B O    1 
HETATM 3986 O  O    . HOH G 4 .   ? 11.56973 20.40523 -3.24318  1.000 39.71122 ? 422 HOH B O    1 
HETATM 3987 O  O    . HOH G 4 .   ? 18.92578 13.23341 -9.07341  0.932 47.01782 ? 423 HOH B O    1 
HETATM 3988 O  O    . HOH G 4 .   ? 20.33739 35.44357 15.27427  1.000 45.01683 ? 424 HOH B O    1 
HETATM 3989 O  O    . HOH G 4 .   ? 18.23733 35.61220 13.69084  1.000 38.67942 ? 425 HOH B O    1 
HETATM 3990 O  O    . HOH G 4 .   ? 14.61969 27.79592 10.91514  1.000 34.04499 ? 426 HOH B O    1 
HETATM 3991 O  O    . HOH G 4 .   ? 42.62359 35.14163 10.97759  1.000 43.77660 ? 427 HOH B O    1 
HETATM 3992 O  O    . HOH G 4 .   ? 33.55359 9.55757  1.75105   1.000 50.33243 ? 428 HOH B O    1 
HETATM 3993 O  O    . HOH G 4 .   ? 30.82159 11.50489 -1.43329  1.000 37.06506 ? 429 HOH B O    1 
HETATM 3994 O  O    . HOH G 4 .   ? 38.47382 26.24225 -6.05251  1.000 46.62805 ? 430 HOH B O    1 
HETATM 3995 O  O    . HOH G 4 .   ? 13.52067 13.91356 9.55672   1.000 41.28849 ? 431 HOH B O    1 
HETATM 3996 O  O    . HOH G 4 .   ? 44.37012 29.10677 3.80076   1.000 38.22456 ? 432 HOH B O    1 
HETATM 3997 O  O    . HOH G 4 .   ? 35.32772 7.70291  5.68377   1.000 47.78838 ? 433 HOH B O    1 
HETATM 3998 O  O    . HOH G 4 .   ? 8.63865  26.08967 -0.91814  1.000 40.62046 ? 434 HOH B O    1 
HETATM 3999 O  O    . HOH G 4 .   ? 17.51353 40.30881 7.09737   1.000 49.28537 ? 435 HOH B O    1 
HETATM 4000 O  O    . HOH G 4 .   ? 11.39485 28.75327 8.55249   0.932 47.49787 ? 436 HOH B O    1 
HETATM 4001 O  O    . HOH G 4 .   ? 31.54083 26.14235 23.55803  1.000 31.74358 ? 437 HOH B O    1 
HETATM 4002 O  O    . HOH G 4 .   ? 15.07835 18.89010 -5.57591  1.000 40.25127 ? 438 HOH B O    1 
HETATM 4003 O  O    . HOH G 4 .   ? 9.98813  13.81731 10.04642  1.000 30.63993 ? 439 HOH B O    1 
HETATM 4004 O  O    . HOH G 4 .   ? 40.83006 17.68360 13.65947  1.000 51.68981 ? 440 HOH B O    1 
HETATM 4005 O  O    . HOH G 4 .   ? 25.40882 19.17352 20.53357  1.000 47.41067 ? 441 HOH B O    1 
HETATM 4006 O  O    . HOH G 4 .   ? 28.57917 20.02890 22.79897  1.000 44.07402 ? 442 HOH B O    1 
HETATM 4007 O  O    . HOH G 4 .   ? 22.67489 19.99947 -15.99657 1.000 33.86540 ? 443 HOH B O    1 
HETATM 4008 O  O    . HOH G 4 .   ? 33.29030 33.39295 -3.22773  1.000 33.53170 ? 444 HOH B O    1 
HETATM 4009 O  O    . HOH G 4 .   ? 7.09228  19.08401 6.65078   1.000 40.70259 ? 445 HOH B O    1 
HETATM 4010 O  O    . HOH G 4 .   ? 7.66449  25.96236 -3.38991  1.000 54.47915 ? 446 HOH B O    1 
HETATM 4011 O  O    . HOH G 4 .   ? 9.06855  15.81101 12.65620  1.000 43.60399 ? 447 HOH B O    1 
HETATM 4012 O  O    . HOH G 4 .   ? 46.12388 33.82898 12.69117  1.000 47.51702 ? 448 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   . GLY A 1   ? 0.17517 0.43162 0.23927 0.00132  0.07429  0.00323  -3  GLY A N   
2    C  CA  . GLY A 1   ? 0.16281 0.41836 0.23439 0.02992  0.06564  0.01287  -3  GLY A CA  
3    C  C   . GLY A 1   ? 0.12391 0.40616 0.17017 0.01530  0.01773  -0.00678 -3  GLY A C   
4    O  O   . GLY A 1   ? 0.17250 0.42334 0.21432 -0.00668 0.00315  0.00096  -3  GLY A O   
7    N  N   . VAL A 2   ? 0.12461 0.40017 0.17201 0.00670  0.04191  0.00271  -2  VAL A N   
8    C  CA  . VAL A 2   ? 0.09890 0.38968 0.15116 -0.00314 0.00687  -0.02359 -2  VAL A CA  
9    C  C   . VAL A 2   ? 0.10820 0.40134 0.11701 0.01164  0.00998  -0.01482 -2  VAL A C   
10   O  O   . VAL A 2   ? 0.14512 0.45065 0.13179 -0.00148 0.00174  -0.00806 -2  VAL A O   
11   C  CB  . VAL A 2   ? 0.12893 0.39255 0.18288 0.01422  0.04637  -0.03266 -2  VAL A CB  
12   C  CG1 . VAL A 2   ? 0.17126 0.40424 0.18157 -0.01638 0.07406  -0.02070 -2  VAL A CG1 
13   C  CG2 . VAL A 2   ? 0.14124 0.40294 0.20972 0.00742  0.03617  -0.04839 -2  VAL A CG2 
23   N  N   . PRO A 3   ? 0.09821 0.36872 0.16266 0.00530  0.02032  -0.00288 -1  PRO A N   
24   C  CA  . PRO A 3   ? 0.11535 0.38076 0.16774 -0.00178 -0.00846 -0.00753 -1  PRO A CA  
25   C  C   . PRO A 3   ? 0.13698 0.36709 0.14331 0.00020  -0.01649 0.00567  -1  PRO A C   
26   O  O   . PRO A 3   ? 0.13107 0.38993 0.16078 -0.02965 0.02628  -0.00316 -1  PRO A O   
27   C  CB  . PRO A 3   ? 0.12096 0.40781 0.22353 0.03140  -0.03769 -0.01262 -1  PRO A CB  
28   C  CG  . PRO A 3   ? 0.21577 0.38359 0.24444 0.01471  -0.04811 0.00912  -1  PRO A CG  
29   C  CD  . PRO A 3   ? 0.14210 0.36377 0.20365 -0.03676 -0.06917 -0.00905 -1  PRO A CD  
37   N  N   . ALA A 4   ? 0.20741 0.35949 0.13220 -0.01483 0.01876  0.01357  0   ALA A N   
38   C  CA  . ALA A 4   ? 0.21568 0.35932 0.13278 0.02825  0.04060  0.00890  0   ALA A CA  
39   C  C   . ALA A 4   ? 0.17630 0.37923 0.15550 0.02283  0.00049  0.01968  0   ALA A C   
40   O  O   . ALA A 4   ? 0.18992 0.43200 0.19441 -0.01742 0.02263  0.06435  0   ALA A O   
41   C  CB  . ALA A 4   ? 0.35658 0.36132 0.19089 0.05273  0.12005  0.02042  0   ALA A CB  
47   N  N   . GLY A 5   ? 0.14204 0.32659 0.14823 -0.00124 0.01459  -0.00371 1   GLY A N   
48   C  CA  . GLY A 5   ? 0.18591 0.29552 0.11243 0.02159  0.02690  -0.00824 1   GLY A CA  
49   C  C   . GLY A 5   ? 0.16258 0.29742 0.13433 0.00048  0.04352  -0.02412 1   GLY A C   
50   O  O   . GLY A 5   ? 0.23657 0.31658 0.14284 -0.00181 0.02323  -0.00961 1   GLY A O   
54   N  N   . ASP A 6   ? 0.12849 0.29350 0.13698 0.01378  0.03018  -0.02000 2   ASP A N   
55   C  CA  . ASP A 6   ? 0.15159 0.27811 0.16231 0.00204  0.02993  -0.02741 2   ASP A CA  
56   C  C   . ASP A 6   ? 0.16291 0.27352 0.13119 0.01475  0.02961  0.00817  2   ASP A C   
57   O  O   . ASP A 6   ? 0.14256 0.25606 0.13660 0.01200  0.01733  -0.01466 2   ASP A O   
58   C  CB  . ASP A 6   ? 0.14510 0.31429 0.23683 0.03589  0.01228  0.02537  2   ASP A CB  
59   C  CG  . ASP A 6   ? 0.25055 0.33942 0.33096 0.09796  0.07290  0.05889  2   ASP A CG  
60   O  OD1 . ASP A 6   ? 0.24916 0.32849 0.30801 0.06982  0.08810  0.04744  2   ASP A OD1 
61   O  OD2 . ASP A 6   ? 0.31866 0.40455 0.41965 0.10361  0.07319  0.08211  2   ASP A OD2 
66   N  N   A VAL A 7   ? 0.19480 0.28361 0.12201 -0.00323 0.01851  -0.00630 3   VAL A N   
67   N  N   B VAL A 7   ? 0.16119 0.27743 0.12164 0.01344  0.01035  -0.01542 3   VAL A N   
68   C  CA  A VAL A 7   ? 0.21380 0.29203 0.13660 -0.02562 0.01263  0.00105  3   VAL A CA  
69   C  CA  B VAL A 7   ? 0.14872 0.27300 0.11788 0.01992  -0.02021 -0.02040 3   VAL A CA  
70   C  C   A VAL A 7   ? 0.23443 0.27710 0.14414 -0.00387 0.01386  0.00748  3   VAL A C   
71   C  C   B VAL A 7   ? 0.16562 0.25762 0.10795 0.00613  -0.03502 -0.02348 3   VAL A C   
72   O  O   A VAL A 7   ? 0.26758 0.29826 0.13110 0.00267  0.05256  0.01268  3   VAL A O   
73   O  O   B VAL A 7   ? 0.15989 0.25026 0.08620 -0.00272 -0.00582 -0.03599 3   VAL A O   
74   C  CB  A VAL A 7   ? 0.32434 0.33450 0.14233 -0.08481 0.04213  0.00330  3   VAL A CB  
75   C  CB  B VAL A 7   ? 0.21907 0.30360 0.11844 0.00982  -0.00997 -0.02232 3   VAL A CB  
76   C  CG1 A VAL A 7   ? 0.35359 0.36009 0.18770 -0.09057 0.06808  0.01904  3   VAL A CG1 
77   C  CG1 B VAL A 7   ? 0.15985 0.30196 0.11515 0.04784  0.00160  -0.02083 3   VAL A CG1 
78   C  CG2 A VAL A 7   ? 0.37972 0.34626 0.13267 -0.10184 0.05728  -0.00272 3   VAL A CG2 
79   C  CG2 B VAL A 7   ? 0.27435 0.32071 0.13996 0.00662  -0.01798 -0.00416 3   VAL A CG2 
98   N  N   . GLU A 8   ? 0.18567 0.27001 0.14439 0.00771  0.02783  0.00038  4   GLU A N   
99   C  CA  . GLU A 8   ? 0.24782 0.29387 0.14650 0.00333  0.01360  0.01427  4   GLU A CA  
100  C  C   . GLU A 8   ? 0.18565 0.28498 0.14020 0.02744  0.03528  0.01938  4   GLU A C   
101  O  O   . GLU A 8   ? 0.17261 0.27176 0.12659 0.02485  0.00408  0.01336  4   GLU A O   
102  C  CB  . GLU A 8   ? 0.35534 0.31101 0.25389 0.01050  0.03817  0.01782  4   GLU A CB  
103  C  CG  . GLU A 8   ? 0.55121 0.37949 0.40148 0.03748  0.07335  0.02500  4   GLU A CG  
104  C  CD  . GLU A 8   ? 0.65197 0.44548 0.53018 0.03947  0.09013  0.03141  4   GLU A CD  
105  O  OE1 . GLU A 8   ? 0.66211 0.47765 0.59260 0.08282  0.11420  0.03028  4   GLU A OE1 
106  O  OE2 . GLU A 8   ? 0.66970 0.46144 0.55372 0.00841  0.07632  0.02449  4   GLU A OE2 
113  N  N   . LYS A 9   ? 0.14253 0.30758 0.14931 0.05184  0.02295  0.01687  5   LYS A N   
114  C  CA  . LYS A 9   ? 0.12827 0.28162 0.15417 0.05928  0.01162  0.00555  5   LYS A CA  
115  C  C   . LYS A 9   ? 0.13107 0.29600 0.12394 0.01155  0.00718  0.00351  5   LYS A C   
116  O  O   . LYS A 9   ? 0.14745 0.29599 0.10663 0.03942  -0.00075 0.00309  5   LYS A O   
117  C  CB  . LYS A 9   ? 0.14792 0.32767 0.19407 0.04794  0.00132  0.00703  5   LYS A CB  
118  C  CG  . LYS A 9   ? 0.13234 0.37726 0.24374 0.06438  -0.03734 0.02289  5   LYS A CG  
119  C  CD  . LYS A 9   ? 0.15922 0.41197 0.34359 0.09308  -0.05133 0.04134  5   LYS A CD  
120  C  CE  . LYS A 9   ? 0.22840 0.49364 0.46591 0.05396  -0.01193 0.04462  5   LYS A CE  
121  N  NZ  . LYS A 9   ? 0.27623 0.53689 0.52226 0.01296  0.02412  0.04037  5   LYS A NZ  
135  N  N   . GLY A 10  ? 0.10156 0.27251 0.09947 0.01897  0.00072  -0.00054 6   GLY A N   
136  C  CA  . GLY A 10  ? 0.10800 0.25696 0.11003 0.01291  0.01623  0.01360  6   GLY A CA  
137  C  C   . GLY A 10  ? 0.12541 0.26258 0.07616 0.00608  -0.02432 -0.01051 6   GLY A C   
138  O  O   . GLY A 10  ? 0.12559 0.27139 0.09086 0.00573  -0.01057 0.00828  6   GLY A O   
142  N  N   . LYS A 11  ? 0.11166 0.24766 0.10325 0.00119  0.00028  0.01150  7   LYS A N   
143  C  CA  . LYS A 11  ? 0.12853 0.24846 0.10948 -0.00659 -0.02945 0.01770  7   LYS A CA  
144  C  C   . LYS A 11  ? 0.12485 0.23517 0.10712 0.01115  -0.00699 0.01722  7   LYS A C   
145  O  O   . LYS A 11  ? 0.13106 0.25873 0.12993 0.00967  0.01319  0.00845  7   LYS A O   
146  C  CB  . LYS A 11  ? 0.16784 0.26668 0.11787 -0.00295 -0.00825 0.02409  7   LYS A CB  
147  C  CG  . LYS A 11  ? 0.12971 0.27860 0.19315 -0.03466 -0.00493 0.00574  7   LYS A CG  
148  C  CD  . LYS A 11  ? 0.22813 0.28847 0.22944 -0.03587 0.01870  -0.00292 7   LYS A CD  
149  C  CE  . LYS A 11  ? 0.27152 0.30041 0.22864 -0.01635 -0.03568 0.01102  7   LYS A CE  
150  N  NZ  . LYS A 11  ? 0.31834 0.33175 0.23675 0.00038  -0.09258 0.00252  7   LYS A NZ  
164  N  N   . LYS A 12  ? 0.14482 0.25938 0.07986 0.00644  0.00797  0.01616  8   LYS A N   
165  C  CA  . LYS A 12  ? 0.14577 0.26893 0.10303 -0.00261 -0.01242 0.03463  8   LYS A CA  
166  C  C   . LYS A 12  ? 0.10479 0.26645 0.10256 -0.01267 -0.01708 0.02482  8   LYS A C   
167  O  O   . LYS A 12  ? 0.12797 0.32669 0.09031 0.01529  0.01122  0.02034  8   LYS A O   
168  C  CB  . LYS A 12  ? 0.18369 0.29197 0.11182 0.02206  -0.00790 0.01583  8   LYS A CB  
169  C  CG  . LYS A 12  ? 0.22355 0.36675 0.14495 0.07042  -0.05170 0.04459  8   LYS A CG  
170  C  CD  . LYS A 12  ? 0.35294 0.45161 0.18235 0.05751  -0.03134 0.06877  8   LYS A CD  
171  C  CE  . LYS A 12  ? 0.49070 0.50845 0.26792 0.03512  -0.00656 0.03048  8   LYS A CE  
172  N  NZ  . LYS A 12  ? 0.58993 0.54438 0.33484 0.01854  0.02317  0.02452  8   LYS A NZ  
186  N  N   . ILE A 13  ? 0.11470 0.25750 0.10275 -0.00703 -0.01527 0.02819  9   ILE A N   
187  C  CA  . ILE A 13  ? 0.13007 0.25184 0.09918 -0.01603 -0.00496 0.01758  9   ILE A CA  
188  C  C   . ILE A 13  ? 0.10739 0.27740 0.09234 -0.00344 -0.02864 0.01570  9   ILE A C   
189  O  O   . ILE A 13  ? 0.10214 0.29611 0.10329 0.00651  0.00465  -0.00531 9   ILE A O   
190  C  CB  . ILE A 13  ? 0.11218 0.27397 0.11222 -0.01001 -0.01079 0.00828  9   ILE A CB  
191  C  CG1 . ILE A 13  ? 0.12569 0.31421 0.13376 -0.00738 0.00794  -0.00312 9   ILE A CG1 
192  C  CG2 . ILE A 13  ? 0.13346 0.28104 0.12090 -0.02366 0.00141  0.02849  9   ILE A CG2 
193  C  CD1 . ILE A 13  ? 0.12703 0.34206 0.15697 -0.00963 -0.00131 0.01887  9   ILE A CD1 
205  N  N   . PHE A 14  ? 0.10892 0.26810 0.10219 0.00066  -0.01675 0.01464  10  PHE A N   
206  C  CA  . PHE A 14  ? 0.10019 0.25893 0.08319 -0.00075 -0.01050 0.01221  10  PHE A CA  
207  C  C   . PHE A 14  ? 0.12446 0.25274 0.07495 -0.00623 -0.00741 -0.02265 10  PHE A C   
208  O  O   . PHE A 14  ? 0.11300 0.27750 0.09054 0.00881  -0.00024 -0.00974 10  PHE A O   
209  C  CB  . PHE A 14  ? 0.08461 0.27708 0.09377 -0.00029 -0.01812 0.01963  10  PHE A CB  
210  C  CG  . PHE A 14  ? 0.11851 0.28662 0.07682 -0.00550 -0.00411 0.00824  10  PHE A CG  
211  C  CD1 . PHE A 14  ? 0.11619 0.25891 0.09369 -0.01254 -0.01251 -0.00409 10  PHE A CD1 
212  C  CD2 . PHE A 14  ? 0.09094 0.31034 0.09313 0.01949  0.01039  0.00984  10  PHE A CD2 
213  C  CE1 . PHE A 14  ? 0.13040 0.27495 0.08930 0.01512  -0.00563 -0.00024 10  PHE A CE1 
214  C  CE2 . PHE A 14  ? 0.13188 0.31541 0.09458 -0.01667 -0.00407 -0.01714 10  PHE A CE2 
215  C  CZ  . PHE A 14  ? 0.11721 0.28592 0.09482 0.00833  -0.00942 -0.01684 10  PHE A CZ  
225  N  N   A VAL A 15  ? 0.12141 0.26932 0.08677 -0.00427 -0.02115 -0.00570 11  VAL A N   
226  N  N   B VAL A 15  ? 0.11601 0.26634 0.09571 0.01978  -0.00831 0.00143  11  VAL A N   
227  C  CA  A VAL A 15  ? 0.10938 0.29801 0.07858 -0.03561 0.00861  -0.00336 11  VAL A CA  
228  C  CA  B VAL A 15  ? 0.12919 0.30807 0.10623 -0.01420 0.03710  0.01236  11  VAL A CA  
229  C  C   A VAL A 15  ? 0.08345 0.31492 0.08371 -0.02940 -0.00056 0.00808  11  VAL A C   
230  C  C   B VAL A 15  ? 0.08938 0.31987 0.11237 -0.02073 0.01257  0.01931  11  VAL A C   
231  O  O   A VAL A 15  ? 0.11495 0.33849 0.08841 -0.00475 -0.01040 0.00734  11  VAL A O   
232  O  O   B VAL A 15  ? 0.11047 0.37064 0.12136 0.02291  0.02104  0.03044  11  VAL A O   
233  C  CB  A VAL A 15  ? 0.13124 0.32053 0.10047 -0.06456 0.01024  0.02618  11  VAL A CB  
234  C  CB  B VAL A 15  ? 0.19768 0.31519 0.18581 -0.03783 0.03986  0.04547  11  VAL A CB  
235  C  CG1 A VAL A 15  ? 0.16594 0.33150 0.12648 -0.08980 0.00581  0.00820  11  VAL A CG1 
236  C  CG1 B VAL A 15  ? 0.25442 0.32467 0.22786 -0.07209 0.05186  0.04566  11  VAL A CG1 
237  C  CG2 A VAL A 15  ? 0.17087 0.32274 0.13546 -0.04812 -0.02084 0.01296  11  VAL A CG2 
238  C  CG2 B VAL A 15  ? 0.22240 0.28584 0.21792 0.00948  0.01096  0.04211  11  VAL A CG2 
257  N  N   . GLN A 16  ? 0.10866 0.31332 0.08186 -0.01103 0.00599  0.01832  12  GLN A N   
258  C  CA  . GLN A 16  ? 0.12239 0.32310 0.08089 0.00709  0.00107  0.00243  12  GLN A CA  
259  C  C   . GLN A 16  ? 0.12308 0.31816 0.08062 -0.00096 -0.00623 0.00609  12  GLN A C   
260  O  O   . GLN A 16  ? 0.16123 0.33733 0.08459 -0.00332 -0.00427 -0.00084 12  GLN A O   
261  C  CB  . GLN A 16  ? 0.10148 0.37586 0.10475 0.00459  -0.00871 -0.01352 12  GLN A CB  
262  C  CG  . GLN A 16  ? 0.12627 0.41056 0.10839 0.02829  -0.00912 0.00810  12  GLN A CG  
263  C  CD  . GLN A 16  ? 0.17368 0.44373 0.14323 0.02571  0.03662  0.01205  12  GLN A CD  
264  O  OE1 . GLN A 16  ? 0.18572 0.49318 0.16161 0.06765  -0.00993 -0.00026 12  GLN A OE1 
265  N  NE2 . GLN A 16  ? 0.20300 0.43578 0.18589 0.10124  0.03212  0.03540  12  GLN A NE2 
274  N  N   . ARG A 17  ? 0.11904 0.29514 0.08541 0.00996  -0.00487 -0.00549 13  ARG A N   
275  C  CA  . ARG A 17  ? 0.13669 0.30312 0.08411 -0.01046 -0.01883 -0.01786 13  ARG A CA  
276  C  C   . ARG A 17  ? 0.17236 0.26657 0.07059 -0.01874 -0.01772 0.00047  13  ARG A C   
277  O  O   . ARG A 17  ? 0.19046 0.26221 0.12183 -0.00383 -0.02359 -0.03143 13  ARG A O   
278  C  CB  . ARG A 17  ? 0.12831 0.32509 0.10543 -0.02018 -0.01822 -0.01413 13  ARG A CB  
279  C  CG  . ARG A 17  ? 0.18066 0.41243 0.16276 -0.04676 -0.05874 -0.01988 13  ARG A CG  
280  C  CD  . ARG A 17  ? 0.31814 0.51058 0.21715 -0.06265 -0.07847 0.02333  13  ARG A CD  
281  N  NE  . ARG A 17  ? 0.43764 0.57108 0.27333 -0.06003 -0.08633 0.02659  13  ARG A NE  
282  C  CZ  . ARG A 17  ? 0.47791 0.63035 0.30211 -0.06677 -0.05886 0.04336  13  ARG A CZ  
283  N  NH1 . ARG A 17  ? 0.50089 0.68124 0.33544 -0.04099 -0.04285 0.05651  13  ARG A NH1 
284  N  NH2 . ARG A 17  ? 0.47575 0.63737 0.27076 -0.07766 -0.10266 0.03824  13  ARG A NH2 
298  N  N   . CYS A 18  ? 0.11981 0.27316 0.08213 -0.00104 -0.00134 -0.00213 14  CYS A N   
299  C  CA  . CYS A 18  ? 0.09859 0.28599 0.07735 -0.00064 -0.01080 0.01615  14  CYS A CA  
300  C  C   . CYS A 18  ? 0.08732 0.26310 0.07831 0.00539  -0.00616 0.01000  14  CYS A C   
301  O  O   . CYS A 18  ? 0.08834 0.26899 0.08941 0.01230  0.00249  0.00043  14  CYS A O   
302  C  CB  . CYS A 18  ? 0.11525 0.26090 0.11593 -0.00891 0.01348  0.00980  14  CYS A CB  
303  S  SG  . CYS A 18  ? 0.10622 0.25724 0.11160 0.00454  0.00381  0.01398  14  CYS A SG  
308  N  N   . ALA A 19  ? 0.12055 0.23843 0.10752 0.01385  -0.00535 0.00816  15  ALA A N   
309  C  CA  . ALA A 19  ? 0.12739 0.24277 0.09843 -0.01430 -0.00599 -0.00996 15  ALA A CA  
310  C  C   . ALA A 19  ? 0.14010 0.27594 0.10063 0.00723  -0.01744 0.01129  15  ALA A C   
311  O  O   . ALA A 19  ? 0.12660 0.28100 0.12832 -0.01102 0.00288  0.01024  15  ALA A O   
312  C  CB  . ALA A 19  ? 0.13010 0.24908 0.11484 -0.01483 -0.01182 0.00650  15  ALA A CB  
318  N  N   . GLN A 20  ? 0.12857 0.30024 0.07949 -0.00168 0.01497  0.00613  16  GLN A N   
319  C  CA  A GLN A 20  ? 0.12034 0.31344 0.08177 0.01197  0.00985  0.01495  16  GLN A CA  
320  C  CA  B GLN A 20  ? 0.14957 0.32145 0.08168 0.01121  -0.00484 0.01177  16  GLN A CA  
321  C  C   . GLN A 20  ? 0.12821 0.31492 0.11067 0.00568  0.02797  0.02206  16  GLN A C   
322  O  O   . GLN A 20  ? 0.14506 0.34966 0.13926 0.01546  0.03906  0.03430  16  GLN A O   
323  C  CB  A GLN A 20  ? 0.13434 0.32525 0.08500 0.03281  -0.00416 0.01687  16  GLN A CB  
324  C  CB  B GLN A 20  ? 0.27397 0.36473 0.10578 0.03343  0.00149  0.01422  16  GLN A CB  
325  C  CG  A GLN A 20  ? 0.14631 0.32721 0.08685 0.01424  0.01601  0.01457  16  GLN A CG  
326  C  CG  B GLN A 20  ? 0.31394 0.35855 0.11286 0.00758  0.00659  0.01772  16  GLN A CG  
327  C  CD  A GLN A 20  ? 0.21140 0.31619 0.10633 0.03220  0.03874  0.00349  16  GLN A CD  
328  C  CD  B GLN A 20  ? 0.41646 0.41140 0.12649 -0.03580 0.00184  0.02447  16  GLN A CD  
329  O  OE1 A GLN A 20  ? 0.19165 0.31849 0.08964 0.04650  0.00417  0.01162  16  GLN A OE1 
330  O  OE1 B GLN A 20  ? 0.45182 0.45219 0.15286 -0.13644 -0.00125 -0.03570 16  GLN A OE1 
331  N  NE2 A GLN A 20  ? 0.25270 0.33311 0.13449 0.01459  0.08798  0.01151  16  GLN A NE2 
332  N  NE2 B GLN A 20  ? 0.44600 0.40743 0.12502 0.02491  -0.03044 0.04479  16  GLN A NE2 
347  N  N   . CYS A 21  ? 0.12351 0.27184 0.07990 -0.00495 0.00987  0.01327  17  CYS A N   
348  C  CA  . CYS A 21  ? 0.12113 0.24588 0.10386 0.00331  0.00851  0.01306  17  CYS A CA  
349  C  C   . CYS A 21  ? 0.08184 0.26534 0.10614 0.01167  -0.00170 0.01810  17  CYS A C   
350  O  O   . CYS A 21  ? 0.11782 0.29269 0.10911 0.04638  -0.00308 -0.01332 17  CYS A O   
351  C  CB  . CYS A 21  ? 0.14600 0.27191 0.08890 0.03231  0.02401  0.00801  17  CYS A CB  
352  S  SG  . CYS A 21  ? 0.16266 0.26425 0.09602 0.00640  0.01423  -0.00713 17  CYS A SG  
357  N  N   . HIS A 22  ? 0.11147 0.24663 0.09316 0.01522  -0.01175 0.01655  18  HIS A N   
358  C  CA  . HIS A 22  ? 0.11155 0.21733 0.09947 0.01264  -0.00434 0.03026  18  HIS A CA  
359  C  C   . HIS A 22  ? 0.10741 0.23205 0.10516 0.02357  -0.00441 0.04480  18  HIS A C   
360  O  O   . HIS A 22  ? 0.14242 0.22343 0.12949 -0.00746 -0.00095 0.01192  18  HIS A O   
361  C  CB  . HIS A 22  ? 0.09199 0.24220 0.08414 -0.00235 0.01017  -0.00811 18  HIS A CB  
362  C  CG  . HIS A 22  ? 0.08373 0.24177 0.10332 -0.00112 0.00971  0.01465  18  HIS A CG  
363  N  ND1 . HIS A 22  ? 0.10787 0.23437 0.10430 0.00873  0.01201  -0.01660 18  HIS A ND1 
364  C  CD2 . HIS A 22  ? 0.06643 0.22288 0.09149 -0.00153 0.01580  0.00341  18  HIS A CD2 
365  C  CE1 . HIS A 22  ? 0.10112 0.23039 0.08135 0.02365  -0.01581 -0.00226 18  HIS A CE1 
366  N  NE2 . HIS A 22  ? 0.09317 0.20784 0.09894 0.00195  0.01806  -0.00926 18  HIS A NE2 
374  N  N   . THR A 23  ? 0.11280 0.24989 0.11015 0.03151  -0.00361 0.00332  19  THR A N   
375  C  CA  . THR A 23  ? 0.10626 0.24926 0.11623 0.02106  0.00705  0.01008  19  THR A CA  
376  C  C   . THR A 23  ? 0.09141 0.26138 0.12763 0.00523  -0.02160 -0.00754 19  THR A C   
377  O  O   . THR A 23  ? 0.10318 0.25065 0.11666 0.00337  -0.00629 -0.00670 19  THR A O   
378  C  CB  . THR A 23  ? 0.11610 0.26515 0.10969 0.00074  -0.00480 -0.01005 19  THR A CB  
379  O  OG1 . THR A 23  ? 0.10414 0.26631 0.10664 0.00635  -0.01831 -0.00094 19  THR A OG1 
380  C  CG2 . THR A 23  ? 0.12170 0.26873 0.15511 -0.00042 0.01678  0.00436  19  THR A CG2 
388  N  N   . VAL A 24  ? 0.13388 0.24016 0.11853 0.01399  0.00716  -0.00069 20  VAL A N   
389  C  CA  . VAL A 24  ? 0.10548 0.28321 0.11077 -0.01275 0.00800  -0.01441 20  VAL A CA  
390  C  C   . VAL A 24  ? 0.11905 0.29342 0.13836 0.03816  -0.03321 -0.03152 20  VAL A C   
391  O  O   . VAL A 24  ? 0.15423 0.33012 0.11517 0.04547  -0.02696 -0.01888 20  VAL A O   
392  C  CB  . VAL A 24  ? 0.10354 0.30231 0.12342 0.02292  -0.01978 -0.00399 20  VAL A CB  
393  C  CG1 . VAL A 24  ? 0.11141 0.34795 0.16235 0.01131  -0.03361 -0.00547 20  VAL A CG1 
394  C  CG2 . VAL A 24  ? 0.14523 0.32061 0.17146 0.03132  -0.02418 -0.02226 20  VAL A CG2 
404  N  N   . GLU A 25  ? 0.14359 0.27878 0.15054 0.01715  -0.04918 -0.03075 21  GLU A N   
405  C  CA  . GLU A 25  ? 0.14768 0.29477 0.16457 -0.00583 -0.03857 -0.01802 21  GLU A CA  
406  C  C   . GLU A 25  ? 0.12380 0.27833 0.15071 -0.02658 -0.04556 -0.02143 21  GLU A C   
407  O  O   . GLU A 25  ? 0.13051 0.24640 0.15545 0.00545  0.00506  -0.01644 21  GLU A O   
408  C  CB  . GLU A 25  ? 0.25167 0.30357 0.24505 -0.01225 -0.10218 -0.00760 21  GLU A CB  
409  C  CG  . GLU A 25  ? 0.26929 0.34683 0.37895 -0.04674 -0.00828 0.05151  21  GLU A CG  
410  C  CD  . GLU A 25  ? 0.40741 0.41826 0.51508 -0.02140 0.17449  0.08891  21  GLU A CD  
411  O  OE1 . GLU A 25  ? 0.57755 0.41685 0.56095 -0.01161 0.26249  0.06570  21  GLU A OE1 
412  O  OE2 . GLU A 25  ? 0.47776 0.44978 0.59564 0.01560  0.18447  0.12717  21  GLU A OE2 
419  N  N   . ALA A 26  ? 0.13415 0.25836 0.14937 0.00578  -0.01236 -0.01973 22  ALA A N   
420  C  CA  . ALA A 26  ? 0.12812 0.26414 0.15345 -0.00589 -0.00066 0.00102  22  ALA A CA  
421  C  C   . ALA A 26  ? 0.11489 0.24419 0.15419 -0.00203 -0.02798 -0.00350 22  ALA A C   
422  O  O   . ALA A 26  ? 0.16483 0.25811 0.19880 -0.03335 -0.02525 -0.02405 22  ALA A O   
423  C  CB  . ALA A 26  ? 0.15846 0.28185 0.15955 -0.03093 -0.02600 -0.02610 22  ALA A CB  
429  N  N   . GLY A 27  ? 0.11889 0.27912 0.15044 0.00016  -0.02472 -0.00532 23  GLY A N   
430  C  CA  . GLY A 27  ? 0.12010 0.29967 0.19019 0.00363  -0.00865 0.00761  23  GLY A CA  
431  C  C   . GLY A 27  ? 0.12853 0.29646 0.19156 -0.03866 -0.00582 -0.00515 23  GLY A C   
432  O  O   . GLY A 27  ? 0.13723 0.34460 0.23790 -0.02466 0.01289  0.00923  23  GLY A O   
436  N  N   . GLY A 28  ? 0.10251 0.27559 0.16462 -0.01680 -0.02802 0.00508  24  GLY A N   
437  C  CA  . GLY A 28  ? 0.13705 0.26248 0.16243 0.00392  -0.01928 0.02118  24  GLY A CA  
438  C  C   . GLY A 28  ? 0.12174 0.24599 0.17545 0.01605  -0.00918 -0.00849 24  GLY A C   
439  O  O   . GLY A 28  ? 0.11708 0.26658 0.18215 0.00377  -0.01031 -0.01017 24  GLY A O   
443  N  N   . LYS A 29  ? 0.13088 0.25217 0.17252 0.00348  0.02774  0.00276  25  LYS A N   
444  C  CA  . LYS A 29  ? 0.15633 0.25502 0.18121 -0.00309 0.02457  -0.02858 25  LYS A CA  
445  C  C   . LYS A 29  ? 0.10765 0.26117 0.14519 -0.01276 0.01004  -0.02719 25  LYS A C   
446  O  O   . LYS A 29  ? 0.10212 0.26623 0.15614 0.01558  -0.00199 -0.00734 25  LYS A O   
447  C  CB  . LYS A 29  ? 0.15380 0.28691 0.20729 -0.01833 0.03963  -0.02299 25  LYS A CB  
448  C  CG  . LYS A 29  ? 0.18755 0.32771 0.21762 -0.03148 -0.02100 0.00752  25  LYS A CG  
449  C  CD  . LYS A 29  ? 0.39461 0.39574 0.22435 -0.05091 0.04136  0.06565  25  LYS A CD  
450  C  CE  . LYS A 29  ? 0.55016 0.44847 0.31952 -0.08143 0.12988  0.06880  25  LYS A CE  
451  N  NZ  . LYS A 29  ? 0.71618 0.49897 0.38432 -0.06655 0.19530  0.06676  25  LYS A NZ  
465  N  N   . HIS A 30  ? 0.12152 0.26586 0.17382 0.00987  0.01184  -0.01356 26  HIS A N   
466  C  CA  . HIS A 30  ? 0.12928 0.24601 0.20077 0.01310  0.04306  -0.00310 26  HIS A CA  
467  C  C   . HIS A 30  ? 0.12188 0.27792 0.17977 -0.01104 0.03580  0.00431  26  HIS A C   
468  O  O   . HIS A 30  ? 0.14253 0.30055 0.17479 -0.02412 0.01944  -0.00362 26  HIS A O   
469  C  CB  . HIS A 30  ? 0.11960 0.27558 0.20963 0.01215  0.04711  -0.00579 26  HIS A CB  
470  C  CG  . HIS A 30  ? 0.09022 0.26664 0.19424 0.01314  0.03216  -0.01761 26  HIS A CG  
471  N  ND1 . HIS A 30  ? 0.08385 0.25492 0.19117 0.00631  0.00356  -0.02105 26  HIS A ND1 
472  C  CD2 . HIS A 30  ? 0.10505 0.29631 0.20193 0.00894  -0.00945 -0.01705 26  HIS A CD2 
473  C  CE1 . HIS A 30  ? 0.10244 0.27016 0.15951 0.01312  -0.00757 -0.01583 26  HIS A CE1 
474  N  NE2 . HIS A 30  ? 0.10876 0.28029 0.19168 0.00507  -0.00610 -0.02287 26  HIS A NE2 
482  N  N   . LYS A 31  ? 0.12917 0.28834 0.14205 -0.00757 0.01550  -0.02884 27  LYS A N   
483  C  CA  . LYS A 31  ? 0.14629 0.29002 0.17489 0.01032  0.01930  -0.02513 27  LYS A CA  
484  C  C   . LYS A 31  ? 0.10707 0.31556 0.17732 0.01712  0.02844  -0.02395 27  LYS A C   
485  O  O   . LYS A 31  ? 0.14136 0.33551 0.16587 0.04254  0.01344  -0.01929 27  LYS A O   
486  C  CB  . LYS A 31  ? 0.19288 0.27938 0.14333 -0.00858 0.02701  -0.00931 27  LYS A CB  
487  C  CG  . LYS A 31  ? 0.22558 0.29969 0.19205 0.01806  0.06904  -0.00106 27  LYS A CG  
488  C  CD  . LYS A 31  ? 0.28418 0.32778 0.25569 -0.00392 0.09210  -0.03125 27  LYS A CD  
489  C  CE  . LYS A 31  ? 0.24572 0.35684 0.34026 -0.02243 -0.00557 -0.01747 27  LYS A CE  
490  N  NZ  . LYS A 31  ? 0.15356 0.36966 0.37986 -0.00100 -0.01783 0.04455  27  LYS A NZ  
504  N  N   . VAL A 32  ? 0.14418 0.30955 0.16028 -0.00107 0.03108  -0.03301 28  VAL A N   
505  C  CA  . VAL A 32  ? 0.12374 0.30205 0.13244 0.01850  0.02420  -0.03167 28  VAL A CA  
506  C  C   . VAL A 32  ? 0.10924 0.30078 0.13721 0.04629  0.00527  -0.02900 28  VAL A C   
507  O  O   . VAL A 32  ? 0.15134 0.27882 0.16149 0.01904  0.00877  -0.04211 28  VAL A O   
508  C  CB  . VAL A 32  ? 0.18638 0.31154 0.12183 0.01934  0.01367  -0.02094 28  VAL A CB  
509  C  CG1 . VAL A 32  ? 0.19643 0.32736 0.15557 -0.00053 0.02738  -0.03920 28  VAL A CG1 
510  C  CG2 . VAL A 32  ? 0.23080 0.34634 0.14644 0.02766  0.04496  -0.00926 28  VAL A CG2 
520  N  N   . GLY A 33  ? 0.10599 0.25898 0.12473 0.03216  0.02025  -0.02086 29  GLY A N   
521  C  CA  . GLY A 33  ? 0.10639 0.27019 0.12384 0.03365  0.02822  -0.01380 29  GLY A CA  
522  C  C   . GLY A 33  ? 0.09583 0.25701 0.12134 0.01951  -0.00730 -0.01419 29  GLY A C   
523  O  O   . GLY A 33  ? 0.11285 0.25059 0.11936 0.01546  0.01475  -0.00712 29  GLY A O   
527  N  N   . PRO A 34  ? 0.10967 0.24629 0.10224 0.01532  -0.00085 -0.02393 30  PRO A N   
528  C  CA  . PRO A 34  ? 0.09971 0.25340 0.11219 0.01615  -0.00157 -0.00584 30  PRO A CA  
529  C  C   . PRO A 34  ? 0.09227 0.23791 0.11962 0.00233  -0.00246 -0.02740 30  PRO A C   
530  O  O   . PRO A 34  ? 0.07934 0.25513 0.12588 0.00672  -0.00738 -0.02305 30  PRO A O   
531  C  CB  . PRO A 34  ? 0.09572 0.24346 0.11517 -0.00936 -0.01216 -0.00914 30  PRO A CB  
532  C  CG  . PRO A 34  ? 0.12896 0.25453 0.11203 0.01518  0.01400  -0.00458 30  PRO A CG  
533  C  CD  . PRO A 34  ? 0.11897 0.22995 0.14926 -0.00467 0.00081  -0.00778 30  PRO A CD  
541  N  N   . ASN A 35  ? 0.09373 0.24205 0.13141 0.00705  -0.01720 -0.02268 31  ASN A N   
542  C  CA  . ASN A 35  ? 0.09263 0.21922 0.10127 0.03321  -0.00697 -0.01312 31  ASN A CA  
543  C  C   . ASN A 35  ? 0.08977 0.22660 0.12169 0.00653  0.00664  -0.01185 31  ASN A C   
544  O  O   . ASN A 35  ? 0.11705 0.21900 0.13302 0.02241  -0.01660 0.00209  31  ASN A O   
545  C  CB  . ASN A 35  ? 0.07774 0.23876 0.13622 0.00715  -0.03640 -0.00305 31  ASN A CB  
546  C  CG  . ASN A 35  ? 0.09147 0.23377 0.13568 0.01952  -0.00801 -0.03305 31  ASN A CG  
547  O  OD1 . ASN A 35  ? 0.12618 0.25020 0.10645 0.00293  -0.00843 -0.01963 31  ASN A OD1 
548  N  ND2 . ASN A 35  ? 0.09758 0.28251 0.13166 0.01768  -0.00684 -0.03311 31  ASN A ND2 
555  N  N   . LEU A 36  ? 0.08452 0.22778 0.10474 0.00498  -0.00791 -0.01576 32  LEU A N   
556  C  CA  . LEU A 36  ? 0.09935 0.23713 0.08115 0.00340  0.00258  -0.01981 32  LEU A CA  
557  C  C   . LEU A 36  ? 0.08023 0.24747 0.10522 0.00713  0.01758  -0.00252 32  LEU A C   
558  O  O   . LEU A 36  ? 0.09555 0.26460 0.08773 0.00639  -0.00677 -0.01151 32  LEU A O   
559  C  CB  . LEU A 36  ? 0.08056 0.24700 0.09071 -0.01101 -0.01267 -0.00400 32  LEU A CB  
560  C  CG  . LEU A 36  ? 0.07722 0.24593 0.09140 -0.02123 -0.01803 -0.00856 32  LEU A CG  
561  C  CD1 . LEU A 36  ? 0.11010 0.29571 0.10358 -0.02945 -0.01448 -0.02553 32  LEU A CD1 
562  C  CD2 . LEU A 36  ? 0.13342 0.27073 0.11120 -0.01770 -0.01241 -0.02100 32  LEU A CD2 
574  N  N   . HIS A 37  ? 0.09550 0.25963 0.11120 -0.02502 -0.00238 -0.01159 33  HIS A N   
575  C  CA  . HIS A 37  ? 0.08226 0.28210 0.10499 0.00106  -0.01583 -0.00768 33  HIS A CA  
576  C  C   . HIS A 37  ? 0.13434 0.26337 0.08647 -0.00718 -0.01790 -0.02171 33  HIS A C   
577  O  O   . HIS A 37  ? 0.14616 0.24971 0.12659 0.02130  -0.02644 -0.02265 33  HIS A O   
578  C  CB  . HIS A 37  ? 0.10282 0.29284 0.09498 -0.01156 -0.01045 -0.01268 33  HIS A CB  
579  C  CG  . HIS A 37  ? 0.13383 0.28936 0.11083 -0.02165 -0.00560 -0.02926 33  HIS A CG  
580  N  ND1 . HIS A 37  ? 0.15998 0.29814 0.11945 -0.01969 -0.02302 -0.01685 33  HIS A ND1 
581  C  CD2 . HIS A 37  ? 0.12187 0.30176 0.16726 -0.00466 0.01199  -0.01657 33  HIS A CD2 
582  C  CE1 . HIS A 37  ? 0.17381 0.31176 0.12718 0.00187  -0.02044 -0.02873 33  HIS A CE1 
583  N  NE2 . HIS A 37  ? 0.16438 0.28776 0.13175 -0.02707 0.02067  -0.03827 33  HIS A NE2 
591  N  N   . GLY A 38  ? 0.13116 0.24183 0.07147 -0.01179 -0.02179 0.00089  34  GLY A N   
592  C  CA  . GLY A 38  ? 0.13615 0.25148 0.10960 -0.00010 -0.01201 -0.00175 34  GLY A CA  
593  C  C   . GLY A 38  ? 0.15169 0.24444 0.10918 0.01904  -0.00030 0.01393  34  GLY A C   
594  O  O   . GLY A 38  ? 0.16626 0.25588 0.13056 0.00788  -0.01383 -0.00382 34  GLY A O   
598  N  N   . LEU A 39  ? 0.12049 0.23466 0.10252 0.00657  -0.00632 0.00103  35  LEU A N   
599  C  CA  . LEU A 39  ? 0.11012 0.23043 0.09347 -0.00372 0.02916  -0.01949 35  LEU A CA  
600  C  C   . LEU A 39  ? 0.14681 0.21201 0.09270 -0.01866 -0.01001 -0.03255 35  LEU A C   
601  O  O   . LEU A 39  ? 0.15280 0.21636 0.11335 -0.00988 -0.00021 -0.01457 35  LEU A O   
602  C  CB  . LEU A 39  ? 0.15938 0.29315 0.11625 -0.06560 0.01221  -0.01086 35  LEU A CB  
603  C  CG  . LEU A 39  ? 0.20222 0.31772 0.11309 -0.09759 0.01590  -0.01296 35  LEU A CG  
604  C  CD1 . LEU A 39  ? 0.29723 0.31259 0.12800 -0.04907 -0.01948 -0.01781 35  LEU A CD1 
605  C  CD2 . LEU A 39  ? 0.14678 0.36979 0.18211 -0.07489 -0.01966 -0.03268 35  LEU A CD2 
617  N  N   . PHE A 40  ? 0.13660 0.22606 0.09873 -0.00622 0.00062  -0.00556 36  PHE A N   
618  C  CA  . PHE A 40  ? 0.13888 0.24159 0.10692 -0.00950 -0.01820 -0.01041 36  PHE A CA  
619  C  C   . PHE A 40  ? 0.13898 0.24455 0.08534 0.01579  -0.02628 -0.03350 36  PHE A C   
620  O  O   . PHE A 40  ? 0.16714 0.28105 0.10398 -0.00633 -0.02966 -0.01901 36  PHE A O   
621  C  CB  . PHE A 40  ? 0.16771 0.24925 0.09164 -0.00560 -0.00807 0.00012  36  PHE A CB  
622  C  CG  . PHE A 40  ? 0.15411 0.23928 0.12522 0.01979  0.00520  -0.01644 36  PHE A CG  
623  C  CD1 . PHE A 40  ? 0.12566 0.27264 0.12245 0.00386  -0.03914 0.00539  36  PHE A CD1 
624  C  CD2 . PHE A 40  ? 0.15037 0.25935 0.15565 0.01475  0.00933  -0.01434 36  PHE A CD2 
625  C  CE1 . PHE A 40  ? 0.18355 0.25729 0.12228 0.02023  -0.02024 0.00640  36  PHE A CE1 
626  C  CE2 . PHE A 40  ? 0.13478 0.26329 0.18870 0.00751  -0.01835 -0.01756 36  PHE A CE2 
627  C  CZ  . PHE A 40  ? 0.18252 0.25927 0.16290 0.04031  -0.05184 -0.04331 36  PHE A CZ  
637  N  N   . GLY A 41  ? 0.14771 0.22764 0.10046 -0.00218 -0.01836 0.00428  37  GLY A N   
638  C  CA  . GLY A 41  ? 0.12360 0.25602 0.11541 -0.00466 -0.00368 -0.01013 37  GLY A CA  
639  C  C   . GLY A 41  ? 0.16494 0.26404 0.16383 -0.01098 0.00005  -0.00063 37  GLY A C   
640  O  O   . GLY A 41  ? 0.17109 0.31940 0.17418 0.02428  -0.04098 0.02542  37  GLY A O   
644  N  N   . ARG A 42  ? 0.13111 0.26167 0.15602 0.00542  -0.00892 -0.01377 38  ARG A N   
645  C  CA  . ARG A 42  ? 0.13115 0.24572 0.17112 0.03022  0.01206  -0.00522 38  ARG A CA  
646  C  C   . ARG A 42  ? 0.13033 0.24620 0.11359 0.01614  0.00094  -0.01828 38  ARG A C   
647  O  O   . ARG A 42  ? 0.12743 0.26435 0.12177 0.03034  -0.01911 0.00285  38  ARG A O   
648  C  CB  . ARG A 42  ? 0.13282 0.29796 0.23813 0.01196  0.00442  0.02761  38  ARG A CB  
649  C  CG  . ARG A 42  ? 0.12745 0.30213 0.19605 -0.00249 0.00118  0.02228  38  ARG A CG  
650  C  CD  . ARG A 42  ? 0.14860 0.30183 0.14484 0.00424  0.01905  0.01181  38  ARG A CD  
651  N  NE  . ARG A 42  ? 0.19188 0.29060 0.14871 0.00307  -0.04550 0.01589  38  ARG A NE  
652  C  CZ  . ARG A 42  ? 0.13975 0.30020 0.17614 0.00156  -0.04319 -0.00824 38  ARG A CZ  
653  N  NH1 . ARG A 42  ? 0.23550 0.34352 0.19932 -0.05168 -0.06587 0.02101  38  ARG A NH1 
654  N  NH2 . ARG A 42  ? 0.18866 0.32306 0.15144 0.06246  -0.03508 -0.00863 38  ARG A NH2 
664  N  N   . LYS A 43  ? 0.12245 0.23099 0.13012 0.03035  -0.02260 -0.01632 39  LYS A N   
665  C  CA  . LYS A 43  ? 0.10521 0.23294 0.12973 0.01679  -0.02111 -0.01562 39  LYS A CA  
666  C  C   . LYS A 43  ? 0.09396 0.26309 0.13321 -0.00321 -0.02596 -0.00525 39  LYS A C   
667  O  O   . LYS A 43  ? 0.13244 0.27626 0.10453 -0.02597 -0.02292 -0.00850 39  LYS A O   
668  C  CB  . LYS A 43  ? 0.25284 0.27391 0.09998 0.05069  -0.01932 -0.03140 39  LYS A CB  
669  C  CG  . LYS A 43  ? 0.41853 0.31707 0.12252 0.11018  -0.00440 -0.00628 39  LYS A CG  
670  C  CD  . LYS A 43  ? 0.51817 0.38375 0.26310 0.00372  0.08720  -0.02915 39  LYS A CD  
671  C  CE  . LYS A 43  ? 0.52280 0.43237 0.30166 -0.07695 0.15710  -0.06344 39  LYS A CE  
672  N  NZ  . LYS A 43  ? 0.53888 0.48035 0.34914 -0.12227 0.18873  -0.04890 39  LYS A NZ  
686  N  N   . THR A 44  ? 0.10804 0.25395 0.12150 -0.00311 -0.00308 -0.00336 40  THR A N   
687  C  CA  . THR A 44  ? 0.12803 0.22780 0.11762 0.00473  0.01727  0.01043  40  THR A CA  
688  C  C   . THR A 44  ? 0.12578 0.25267 0.08965 -0.00072 -0.00067 -0.00531 40  THR A C   
689  O  O   . THR A 44  ? 0.11980 0.26999 0.10751 0.01481  -0.00316 0.01464  40  THR A O   
690  C  CB  . THR A 44  ? 0.18055 0.20068 0.13106 0.00356  0.00905  -0.01704 40  THR A CB  
691  O  OG1 . THR A 44  ? 0.20210 0.22130 0.15985 0.00377  -0.01297 -0.03326 40  THR A OG1 
692  C  CG2 . THR A 44  ? 0.18006 0.23399 0.14079 -0.04763 -0.02074 -0.01060 40  THR A CG2 
700  N  N   . GLY A 45  ? 0.15181 0.24351 0.10236 0.00446  0.00678  -0.00480 41  GLY A N   
701  C  CA  . GLY A 45  ? 0.14812 0.25507 0.12163 0.01010  0.03927  -0.00670 41  GLY A CA  
702  C  C   . GLY A 45  ? 0.12183 0.29032 0.14705 0.01550  -0.00488 -0.03252 41  GLY A C   
703  O  O   . GLY A 45  ? 0.13364 0.31027 0.17470 0.01968  0.02852  -0.02097 41  GLY A O   
707  N  N   . GLN A 46  ? 0.13845 0.27540 0.13162 0.02968  -0.01894 -0.00671 42  GLN A N   
708  C  CA  . GLN A 46  ? 0.14739 0.28846 0.11359 0.02170  -0.05404 -0.01689 42  GLN A CA  
709  C  C   . GLN A 46  ? 0.14499 0.29176 0.15793 0.01801  -0.01688 -0.02420 42  GLN A C   
710  O  O   . GLN A 46  ? 0.17813 0.33804 0.18294 -0.02988 -0.07572 -0.02577 42  GLN A O   
711  C  CB  . GLN A 46  ? 0.18407 0.36090 0.14294 -0.00489 -0.04485 -0.00860 42  GLN A CB  
712  C  CG  . GLN A 46  ? 0.20693 0.38252 0.13420 -0.01182 -0.05176 -0.00376 42  GLN A CG  
713  C  CD  . GLN A 46  ? 0.16325 0.39216 0.20683 -0.00803 -0.07692 -0.01344 42  GLN A CD  
714  O  OE1 . GLN A 46  ? 0.20620 0.41650 0.25182 -0.00241 -0.10591 -0.01137 42  GLN A OE1 
715  N  NE2 . GLN A 46  ? 0.22547 0.42710 0.18338 0.00818  -0.01699 0.02197  42  GLN A NE2 
724  N  N   . ALA A 47  ? 0.10486 0.27043 0.16428 -0.01431 -0.01636 -0.03673 43  ALA A N   
725  C  CA  . ALA A 47  ? 0.10743 0.24893 0.17874 -0.01435 0.00937  -0.05483 43  ALA A CA  
726  C  C   . ALA A 47  ? 0.07809 0.29395 0.17842 -0.00131 -0.01589 -0.03115 43  ALA A C   
727  O  O   . ALA A 47  ? 0.09764 0.29607 0.17492 0.01728  0.00623  -0.04179 43  ALA A O   
728  C  CB  . ALA A 47  ? 0.11513 0.25424 0.16880 0.00706  -0.01863 -0.01816 43  ALA A CB  
734  N  N   . ALA A 48  ? 0.10524 0.32254 0.17633 0.00569  -0.00298 -0.05390 44  ALA A N   
735  C  CA  . ALA A 48  ? 0.10512 0.32849 0.17186 -0.00239 -0.00023 -0.03286 44  ALA A CA  
736  C  C   . ALA A 48  ? 0.08921 0.32162 0.16326 -0.01636 -0.02193 -0.02104 44  ALA A C   
737  O  O   . ALA A 48  ? 0.16346 0.31419 0.18142 -0.01381 -0.05327 -0.01145 44  ALA A O   
738  C  CB  . ALA A 48  ? 0.15206 0.35722 0.16882 0.00752  -0.00609 -0.03870 44  ALA A CB  
744  N  N   . GLY A 49  ? 0.09740 0.34249 0.16845 0.01388  -0.02292 -0.02168 45  GLY A N   
745  C  CA  . GLY A 49  ? 0.09741 0.35600 0.15480 0.01444  -0.02123 -0.02922 45  GLY A CA  
746  C  C   . GLY A 49  ? 0.09528 0.35889 0.14200 0.02000  -0.01426 -0.01485 45  GLY A C   
747  O  O   . GLY A 49  ? 0.11153 0.43978 0.15893 -0.01614 0.00173  -0.02582 45  GLY A O   
751  N  N   . PHE A 50  ? 0.09381 0.30322 0.14051 -0.00181 -0.00494 -0.01983 46  PHE A N   
752  C  CA  . PHE A 50  ? 0.10356 0.27228 0.14487 0.00974  0.00061  -0.01683 46  PHE A CA  
753  C  C   . PHE A 50  ? 0.08667 0.26319 0.19916 -0.02206 0.02730  -0.02841 46  PHE A C   
754  O  O   . PHE A 50  ? 0.12943 0.25965 0.23459 0.01978  0.01629  0.02007  46  PHE A O   
755  C  CB  . PHE A 50  ? 0.09260 0.27374 0.14694 -0.01167 0.00462  -0.02118 46  PHE A CB  
756  C  CG  . PHE A 50  ? 0.10419 0.26975 0.15032 0.01955  -0.00613 -0.02322 46  PHE A CG  
757  C  CD1 . PHE A 50  ? 0.11286 0.26842 0.14108 0.02320  -0.00631 -0.03187 46  PHE A CD1 
758  C  CD2 . PHE A 50  ? 0.09724 0.27394 0.15211 0.01426  -0.01076 -0.00391 46  PHE A CD2 
759  C  CE1 . PHE A 50  ? 0.14280 0.28527 0.13950 0.02871  0.03189  0.00564  46  PHE A CE1 
760  C  CE2 . PHE A 50  ? 0.08790 0.27549 0.15733 0.01440  -0.02060 -0.01856 46  PHE A CE2 
761  C  CZ  . PHE A 50  ? 0.09705 0.27822 0.14075 0.03841  0.01008  -0.01249 46  PHE A CZ  
771  N  N   . ALA A 51  ? 0.11604 0.26150 0.19860 0.00598  0.01899  -0.03198 47  ALA A N   
772  C  CA  . ALA A 51  ? 0.08169 0.25343 0.24254 0.01485  0.03334  -0.03977 47  ALA A CA  
773  C  C   . ALA A 51  ? 0.10153 0.27865 0.17160 0.01322  0.01329  -0.03661 47  ALA A C   
774  O  O   . ALA A 51  ? 0.14297 0.31470 0.19236 -0.01189 0.03402  -0.03021 47  ALA A O   
775  C  CB  . ALA A 51  ? 0.13276 0.27249 0.30402 0.01535  0.03485  -0.05566 47  ALA A CB  
781  N  N   . TYR A 52  ? 0.10318 0.25206 0.14662 0.00357  0.00376  -0.02889 48  TYR A N   
782  C  CA  . TYR A 52  ? 0.09967 0.24544 0.16579 -0.01005 0.00893  -0.00769 48  TYR A CA  
783  C  C   . TYR A 52  ? 0.09213 0.27310 0.17221 0.03358  -0.01797 -0.01305 48  TYR A C   
784  O  O   . TYR A 52  ? 0.15095 0.29477 0.19484 0.02024  -0.01178 -0.03321 48  TYR A O   
785  C  CB  . TYR A 52  ? 0.12499 0.27006 0.16151 0.02117  -0.00938 0.00295  48  TYR A CB  
786  C  CG  . TYR A 52  ? 0.10337 0.28225 0.13805 -0.00581 -0.01194 -0.02460 48  TYR A CG  
787  C  CD1 . TYR A 52  ? 0.09348 0.27016 0.10649 -0.02622 0.00108  -0.01414 48  TYR A CD1 
788  C  CD2 . TYR A 52  ? 0.11730 0.28546 0.14151 0.01726  0.00614  -0.00495 48  TYR A CD2 
789  C  CE1 . TYR A 52  ? 0.11199 0.24702 0.12475 -0.00197 0.01815  -0.02520 48  TYR A CE1 
790  C  CE2 . TYR A 52  ? 0.08059 0.27533 0.15726 -0.01451 -0.00118 -0.04231 48  TYR A CE2 
791  C  CZ  . TYR A 52  ? 0.09139 0.25147 0.12391 -0.01886 -0.00050 -0.02697 48  TYR A CZ  
792  O  OH  . TYR A 52  ? 0.10619 0.25189 0.14480 0.00215  0.00184  -0.03740 48  TYR A OH  
802  N  N   . THR A 53  ? 0.12181 0.25470 0.13574 0.02960  0.01383  -0.00407 49  THR A N   
803  C  CA  . THR A 53  ? 0.15066 0.24365 0.13927 0.03825  0.00416  -0.01196 49  THR A CA  
804  C  C   . THR A 53  ? 0.12777 0.24408 0.14618 0.00398  -0.01901 -0.02682 49  THR A C   
805  O  O   . THR A 53  ? 0.12613 0.25087 0.15176 0.01491  -0.00679 -0.02932 49  THR A O   
806  C  CB  . THR A 53  ? 0.14672 0.27168 0.14042 0.01774  0.00312  -0.03077 49  THR A CB  
807  O  OG1 . THR A 53  ? 0.13011 0.24589 0.14175 -0.00331 -0.00441 -0.03110 49  THR A OG1 
808  C  CG2 . THR A 53  ? 0.19812 0.30318 0.14022 0.03527  0.00651  -0.04687 49  THR A CG2 
816  N  N   . ASP A 54  ? 0.14191 0.23647 0.17258 0.02590  -0.01707 -0.00947 50  ASP A N   
817  C  CA  . ASP A 54  ? 0.13234 0.22726 0.20266 0.01023  -0.02291 -0.01399 50  ASP A CA  
818  C  C   . ASP A 54  ? 0.15793 0.21757 0.17001 0.01170  -0.03996 -0.02179 50  ASP A C   
819  O  O   . ASP A 54  ? 0.16052 0.27144 0.14233 0.01741  -0.04683 -0.00238 50  ASP A O   
820  C  CB  . ASP A 54  ? 0.15156 0.25769 0.26042 0.01986  -0.03639 0.00989  50  ASP A CB  
821  C  CG  . ASP A 54  ? 0.18779 0.27969 0.31508 0.06035  -0.01970 0.00235  50  ASP A CG  
822  O  OD1 . ASP A 54  ? 0.14407 0.32978 0.29918 0.00848  0.01216  0.04229  50  ASP A OD1 
823  O  OD2 . ASP A 54  ? 0.22767 0.32412 0.35097 0.06208  -0.00875 0.00282  50  ASP A OD2 
828  N  N   . ALA A 55  ? 0.13850 0.23233 0.17373 -0.00165 -0.03622 -0.02144 51  ALA A N   
829  C  CA  . ALA A 55  ? 0.15083 0.23265 0.19048 0.00230  -0.04323 -0.01985 51  ALA A CA  
830  C  C   . ALA A 55  ? 0.14501 0.21298 0.15986 0.00659  -0.06549 -0.00755 51  ALA A C   
831  O  O   . ALA A 55  ? 0.13032 0.24259 0.15532 0.00415  -0.01776 0.00101  51  ALA A O   
832  C  CB  . ALA A 55  ? 0.14854 0.27123 0.19832 0.01062  -0.05801 -0.04596 51  ALA A CB  
838  N  N   . ASN A 56  ? 0.14142 0.20325 0.15129 0.01113  -0.02996 -0.01452 52  ASN A N   
839  C  CA  . ASN A 56  ? 0.12726 0.21731 0.15376 0.01660  -0.04586 -0.02279 52  ASN A CA  
840  C  C   . ASN A 56  ? 0.12205 0.25159 0.18012 0.03540  -0.02600 -0.02858 52  ASN A C   
841  O  O   . ASN A 56  ? 0.16704 0.31522 0.15271 0.04250  -0.01974 -0.04196 52  ASN A O   
842  C  CB  . ASN A 56  ? 0.12033 0.22585 0.17565 0.00195  -0.02147 -0.03391 52  ASN A CB  
843  C  CG  . ASN A 56  ? 0.16245 0.25750 0.19535 -0.03350 -0.01928 -0.01869 52  ASN A CG  
844  O  OD1 . ASN A 56  ? 0.15116 0.28577 0.17062 -0.00458 -0.01465 -0.01121 52  ASN A OD1 
845  N  ND2 . ASN A 56  ? 0.14691 0.26804 0.24984 -0.01280 -0.00790 0.00195  52  ASN A ND2 
852  N  N   . LYS A 57  ? 0.12768 0.23985 0.15210 0.01846  -0.02615 -0.01498 53  LYS A N   
853  C  CA  . LYS A 57  ? 0.15676 0.26784 0.16469 0.01153  -0.07007 -0.00901 53  LYS A CA  
854  C  C   . LYS A 57  ? 0.21515 0.27778 0.14340 0.00330  -0.05825 -0.00091 53  LYS A C   
855  O  O   . LYS A 57  ? 0.28116 0.28643 0.12724 -0.00498 -0.03667 -0.00422 53  LYS A O   
856  C  CB  . LYS A 57  ? 0.17026 0.30807 0.21908 -0.00791 -0.08117 0.01128  53  LYS A CB  
857  C  CG  . LYS A 57  ? 0.16022 0.34840 0.30432 -0.03713 -0.04491 -0.01052 53  LYS A CG  
858  C  CD  . LYS A 57  ? 0.19622 0.40355 0.43032 0.00887  -0.04768 -0.00577 53  LYS A CD  
859  C  CE  . LYS A 57  ? 0.28607 0.46881 0.52195 0.03678  0.03906  0.03044  53  LYS A CE  
860  N  NZ  . LYS A 57  ? 0.37580 0.49777 0.58681 0.04680  0.16579  0.03903  53  LYS A NZ  
874  N  N   . ALA A 58  ? 0.16793 0.24701 0.13040 0.00360  -0.03422 -0.02007 54  ALA A N   
875  C  CA  . ALA A 58  ? 0.18339 0.26267 0.15226 0.01031  -0.05723 0.02155  54  ALA A CA  
876  C  C   . ALA A 58  ? 0.20905 0.24237 0.14393 0.01006  -0.01299 0.02808  54  ALA A C   
877  O  O   . ALA A 58  ? 0.22032 0.26293 0.14517 0.01705  -0.02174 0.02615  54  ALA A O   
878  C  CB  . ALA A 58  ? 0.24279 0.26088 0.13317 -0.02894 -0.00893 0.01593  54  ALA A CB  
884  N  N   . LYS A 59  ? 0.18160 0.22461 0.13426 -0.00387 -0.00638 0.02123  55  LYS A N   
885  C  CA  . LYS A 59  ? 0.18589 0.23618 0.14851 -0.01607 0.02462  -0.00560 55  LYS A CA  
886  C  C   . LYS A 59  ? 0.16950 0.24397 0.14290 -0.00997 0.00225  0.00611  55  LYS A C   
887  O  O   . LYS A 59  ? 0.22111 0.25274 0.14593 0.00214  -0.00641 0.01217  55  LYS A O   
888  C  CB  . LYS A 59  ? 0.16666 0.23593 0.15106 -0.00382 -0.01465 0.01342  55  LYS A CB  
889  C  CG  . LYS A 59  ? 0.14452 0.26458 0.13599 -0.02288 -0.01560 -0.01405 55  LYS A CG  
890  C  CD  . LYS A 59  ? 0.16952 0.27090 0.17064 -0.01189 0.00723  -0.01780 55  LYS A CD  
891  C  CE  . LYS A 59  ? 0.18367 0.28576 0.16918 -0.01205 -0.01579 -0.02080 55  LYS A CE  
892  N  NZ  . LYS A 59  ? 0.16951 0.30852 0.19515 0.00636  0.01413  -0.01130 55  LYS A NZ  
906  N  N   . GLY A 60  ? 0.17081 0.24949 0.15103 -0.01361 -0.03396 0.00773  56  GLY A N   
907  C  CA  . GLY A 60  ? 0.20431 0.28213 0.13384 0.01287  -0.03899 0.01562  56  GLY A CA  
908  C  C   . GLY A 60  ? 0.21910 0.30047 0.09917 0.00747  -0.01883 0.00514  56  GLY A C   
909  O  O   . GLY A 60  ? 0.27374 0.32071 0.13350 0.04744  -0.04213 0.00116  56  GLY A O   
913  N  N   . ILE A 61  ? 0.19029 0.28692 0.11324 0.01426  -0.02121 -0.00010 57  ILE A N   
914  C  CA  . ILE A 61  ? 0.19855 0.25086 0.11641 -0.01252 -0.01536 0.03667  57  ILE A CA  
915  C  C   . ILE A 61  ? 0.11099 0.25730 0.12356 0.01192  -0.00128 0.00618  57  ILE A C   
916  O  O   . ILE A 61  ? 0.11554 0.26721 0.13239 0.01491  -0.02161 0.00039  57  ILE A O   
917  C  CB  . ILE A 61  ? 0.20420 0.24146 0.14783 -0.02098 -0.02133 0.02481  57  ILE A CB  
918  C  CG1 . ILE A 61  ? 0.14901 0.24935 0.14495 0.00405  -0.02282 0.01886  57  ILE A CG1 
919  C  CG2 . ILE A 61  ? 0.17593 0.27633 0.17540 -0.03912 0.00438  0.02213  57  ILE A CG2 
920  C  CD1 . ILE A 61  ? 0.11367 0.28363 0.13667 0.00246  -0.00791 0.01673  57  ILE A CD1 
932  N  N   . THR A 62  ? 0.15595 0.24265 0.13389 0.01497  0.01731  0.00877  58  THR A N   
933  C  CA  . THR A 62  ? 0.13768 0.23060 0.14777 0.00294  0.00108  0.01644  58  THR A CA  
934  C  C   . THR A 62  ? 0.09594 0.24469 0.16148 0.01073  -0.01203 0.01439  58  THR A C   
935  O  O   . THR A 62  ? 0.11205 0.25388 0.20531 0.00222  0.01231  0.03116  58  THR A O   
936  C  CB  . THR A 62  ? 0.15555 0.25850 0.14116 0.03527  0.00826  0.00953  58  THR A CB  
937  O  OG1 . THR A 62  ? 0.21772 0.30895 0.12822 0.03191  -0.01052 0.00431  58  THR A OG1 
938  C  CG2 . THR A 62  ? 0.20193 0.25361 0.17461 0.01375  -0.00898 0.00815  58  THR A CG2 
946  N  N   . TRP A 63  ? 0.08263 0.27800 0.12803 0.01870  -0.01604 0.00348  59  TRP A N   
947  C  CA  . TRP A 63  ? 0.08663 0.27971 0.10962 0.02130  -0.01714 -0.00617 59  TRP A CA  
948  C  C   . TRP A 63  ? 0.10107 0.26443 0.09939 -0.00952 -0.02631 -0.00978 59  TRP A C   
949  O  O   . TRP A 63  ? 0.12429 0.26952 0.15184 0.00353  -0.03894 -0.00846 59  TRP A O   
950  C  CB  . TRP A 63  ? 0.09280 0.26978 0.10726 -0.00801 0.00187  -0.01318 59  TRP A CB  
951  C  CG  . TRP A 63  ? 0.10057 0.25440 0.12437 0.00474  -0.02795 0.02324  59  TRP A CG  
952  C  CD1 . TRP A 63  ? 0.12944 0.24034 0.13437 -0.01997 -0.01523 0.01440  59  TRP A CD1 
953  C  CD2 . TRP A 63  ? 0.08405 0.24383 0.11416 0.01328  -0.01961 0.02796  59  TRP A CD2 
954  N  NE1 . TRP A 63  ? 0.08627 0.27659 0.13549 0.01235  -0.00559 -0.00124 59  TRP A NE1 
955  C  CE2 . TRP A 63  ? 0.09459 0.23018 0.13128 0.00934  -0.00886 -0.00010 59  TRP A CE2 
956  C  CE3 . TRP A 63  ? 0.12819 0.26066 0.11222 0.02507  -0.01152 0.01614  59  TRP A CE3 
957  C  CZ2 . TRP A 63  ? 0.12819 0.23967 0.12476 0.01846  0.00338  0.00706  59  TRP A CZ2 
958  C  CZ3 . TRP A 63  ? 0.13123 0.27975 0.10980 -0.00066 0.00041  0.01888  59  TRP A CZ3 
959  C  CH2 . TRP A 63  ? 0.11713 0.25799 0.10713 0.00306  -0.00383 0.00032  59  TRP A CH2 
970  N  N   . ASN A 64  ? 0.11004 0.25964 0.10291 0.00921  -0.02444 -0.01654 60  ASN A N   
971  C  CA  . ASN A 64  ? 0.10314 0.26202 0.10913 0.01808  -0.00142 -0.03350 60  ASN A CA  
972  C  C   . ASN A 64  ? 0.11821 0.23931 0.11536 0.01893  0.00138  -0.00008 60  ASN A C   
973  O  O   . ASN A 64  ? 0.10878 0.25008 0.09267 0.00698  0.00089  -0.01152 60  ASN A O   
974  C  CB  . ASN A 64  ? 0.17779 0.31197 0.11345 0.04240  0.01345  -0.01133 60  ASN A CB  
975  C  CG  . ASN A 64  ? 0.23232 0.32452 0.13533 0.02024  0.04419  0.03699  60  ASN A CG  
976  O  OD1 . ASN A 64  ? 0.13634 0.34459 0.15922 -0.01146 -0.00839 0.03043  60  ASN A OD1 
977  N  ND2 . ASN A 64  ? 0.34229 0.36916 0.18559 0.01122  0.10615  0.01256  60  ASN A ND2 
984  N  N   . GLU A 65  ? 0.10970 0.25781 0.12396 0.02743  0.01693  -0.00295 61  GLU A N   
985  C  CA  . GLU A 65  ? 0.12140 0.26499 0.11091 0.01958  -0.00732 0.00347  61  GLU A CA  
986  C  C   . GLU A 65  ? 0.08359 0.27055 0.13208 0.01325  0.03062  0.01945  61  GLU A C   
987  O  O   . GLU A 65  ? 0.09611 0.28523 0.10999 0.00463  0.00455  0.00601  61  GLU A O   
988  C  CB  . GLU A 65  ? 0.14383 0.28088 0.16039 0.05172  -0.02018 -0.00862 61  GLU A CB  
989  C  CG  . GLU A 65  ? 0.13488 0.30257 0.19511 0.05301  0.00068  -0.01022 61  GLU A CG  
990  C  CD  . GLU A 65  ? 0.24798 0.33547 0.19058 0.06971  -0.03583 -0.00710 61  GLU A CD  
991  O  OE1 . GLU A 65  ? 0.32767 0.35010 0.14109 0.11187  0.05242  -0.01075 61  GLU A OE1 
992  O  OE2 . GLU A 65  ? 0.31477 0.36465 0.23547 0.08845  -0.08012 -0.02503 61  GLU A OE2 
999  N  N   . ASP A 66  ? 0.09830 0.30175 0.11042 0.03069  0.01477  0.01222  62  ASP A N   
1000 C  CA  . ASP A 66  ? 0.13467 0.29240 0.13035 -0.01304 0.04697  0.01051  62  ASP A CA  
1001 C  C   . ASP A 66  ? 0.09643 0.27850 0.12902 0.00837  0.03806  0.01100  62  ASP A C   
1002 O  O   . ASP A 66  ? 0.09717 0.26654 0.16077 0.00523  0.01841  0.00664  62  ASP A O   
1003 C  CB  . ASP A 66  ? 0.19451 0.34191 0.17358 -0.00912 0.09082  0.01121  62  ASP A CB  
1004 C  CG  . ASP A 66  ? 0.19550 0.40734 0.22459 -0.05229 0.09530  0.01767  62  ASP A CG  
1005 O  OD1 . ASP A 66  ? 0.28713 0.42876 0.26255 -0.01918 0.10134  -0.01809 62  ASP A OD1 
1006 O  OD2 . ASP A 66  ? 0.22907 0.49401 0.29426 0.02696  0.11039  0.01419  62  ASP A OD2 
1011 N  N   . THR A 67  ? 0.10308 0.27551 0.11211 -0.00003 0.00730  0.01082  63  THR A N   
1012 C  CA  . THR A 67  ? 0.08577 0.24776 0.12078 0.00170  0.01992  0.01679  63  THR A CA  
1013 C  C   . THR A 67  ? 0.08494 0.23162 0.10756 0.00762  0.01375  -0.00534 63  THR A C   
1014 O  O   . THR A 67  ? 0.08700 0.24243 0.12659 -0.00252 -0.00281 -0.00421 63  THR A O   
1015 C  CB  . THR A 67  ? 0.10651 0.23437 0.12549 -0.00839 0.00977  0.01076  63  THR A CB  
1016 O  OG1 . THR A 67  ? 0.11037 0.23747 0.12642 -0.00020 0.01639  -0.00713 63  THR A OG1 
1017 C  CG2 . THR A 67  ? 0.14461 0.22679 0.11478 -0.01172 0.00454  -0.00269 63  THR A CG2 
1025 N  N   . LEU A 68  ? 0.07069 0.24217 0.09890 0.01834  0.00535  -0.00933 64  LEU A N   
1026 C  CA  . LEU A 68  ? 0.09343 0.22710 0.08342 0.01230  0.00582  0.00619  64  LEU A CA  
1027 C  C   . LEU A 68  ? 0.10898 0.25907 0.12046 0.00456  0.00570  0.00476  64  LEU A C   
1028 O  O   . LEU A 68  ? 0.09263 0.24110 0.11074 -0.00804 -0.00035 0.00542  64  LEU A O   
1029 C  CB  . LEU A 68  ? 0.12147 0.23606 0.09295 0.01905  0.01190  0.00084  64  LEU A CB  
1030 C  CG  . LEU A 68  ? 0.09746 0.23722 0.13443 0.01572  -0.00033 0.00007  64  LEU A CG  
1031 C  CD1 . LEU A 68  ? 0.11406 0.24689 0.14348 -0.00633 0.01419  0.00254  64  LEU A CD1 
1032 C  CD2 . LEU A 68  ? 0.10778 0.22618 0.15332 -0.00567 0.03915  0.00457  64  LEU A CD2 
1044 N  N   . PHE A 69  ? 0.06858 0.24582 0.11651 0.00035  -0.00493 0.01113  65  PHE A N   
1045 C  CA  . PHE A 69  ? 0.07395 0.24719 0.12412 0.00831  0.00315  0.01252  65  PHE A CA  
1046 C  C   . PHE A 69  ? 0.09823 0.23761 0.16963 -0.00390 0.00867  -0.01386 65  PHE A C   
1047 O  O   . PHE A 69  ? 0.14294 0.26317 0.14398 -0.01054 -0.03584 -0.01409 65  PHE A O   
1048 C  CB  . PHE A 69  ? 0.07412 0.27057 0.12722 -0.01005 -0.01854 0.01353  65  PHE A CB  
1049 C  CG  . PHE A 69  ? 0.10561 0.30550 0.15865 0.01582  -0.00228 0.00930  65  PHE A CG  
1050 C  CD1 . PHE A 69  ? 0.09400 0.34541 0.16467 0.03562  -0.00567 0.02051  65  PHE A CD1 
1051 C  CD2 . PHE A 69  ? 0.09634 0.35677 0.20306 -0.01213 -0.02714 0.00645  65  PHE A CD2 
1052 C  CE1 . PHE A 69  ? 0.10379 0.38571 0.16429 0.00973  0.01457  0.04641  65  PHE A CE1 
1053 C  CE2 . PHE A 69  ? 0.13822 0.39283 0.19748 -0.00623 0.00763  0.01053  65  PHE A CE2 
1054 C  CZ  . PHE A 69  ? 0.11957 0.40858 0.16509 0.03545  0.01616  0.02951  65  PHE A CZ  
1064 N  N   . GLU A 70  ? 0.09211 0.22521 0.15219 -0.01222 0.00032  0.02145  66  GLU A N   
1065 C  CA  . GLU A 70  ? 0.08406 0.22259 0.19843 -0.02210 -0.00909 0.00540  66  GLU A CA  
1066 C  C   . GLU A 70  ? 0.08975 0.24669 0.15704 -0.02123 -0.01981 -0.00361 66  GLU A C   
1067 O  O   . GLU A 70  ? 0.11399 0.25873 0.14693 -0.01769 -0.02624 -0.01116 66  GLU A O   
1068 C  CB  . GLU A 70  ? 0.15988 0.25083 0.20566 -0.02142 -0.00535 0.02290  66  GLU A CB  
1069 C  CG  . GLU A 70  ? 0.18235 0.22004 0.21615 0.01233  0.02124  0.04716  66  GLU A CG  
1070 C  CD  . GLU A 70  ? 0.19709 0.27840 0.25129 -0.00838 0.04132  0.02240  66  GLU A CD  
1071 O  OE1 . GLU A 70  ? 0.26882 0.31617 0.26186 0.00178  0.03411  0.05161  66  GLU A OE1 
1072 O  OE2 . GLU A 70  ? 0.26251 0.29080 0.26338 -0.02120 0.06778  0.00231  66  GLU A OE2 
1079 N  N   . TYR A 71  ? 0.10278 0.25408 0.11272 -0.02342 -0.01892 0.00046  67  TYR A N   
1080 C  CA  . TYR A 71  ? 0.09495 0.25602 0.10555 -0.01287 -0.00710 0.02172  67  TYR A CA  
1081 C  C   . TYR A 71  ? 0.10766 0.25434 0.09242 -0.00749 0.00205  0.02131  67  TYR A C   
1082 O  O   . TYR A 71  ? 0.11076 0.25481 0.11934 0.00015  -0.00659 -0.00135 67  TYR A O   
1083 C  CB  . TYR A 71  ? 0.08119 0.24606 0.10928 -0.02100 -0.01357 0.00212  67  TYR A CB  
1084 C  CG  . TYR A 71  ? 0.10088 0.23642 0.11554 -0.01536 -0.02269 -0.00998 67  TYR A CG  
1085 C  CD1 . TYR A 71  ? 0.09986 0.25063 0.10029 -0.01142 -0.02499 0.00509  67  TYR A CD1 
1086 C  CD2 . TYR A 71  ? 0.16862 0.24764 0.10640 -0.00799 -0.01568 -0.01650 67  TYR A CD2 
1087 C  CE1 . TYR A 71  ? 0.11194 0.27345 0.09751 -0.00315 -0.01030 0.00197  67  TYR A CE1 
1088 C  CE2 . TYR A 71  ? 0.14360 0.26559 0.12478 -0.04520 -0.01477 -0.00699 67  TYR A CE2 
1089 C  CZ  . TYR A 71  ? 0.09918 0.30578 0.10817 -0.01330 -0.01538 -0.01267 67  TYR A CZ  
1090 O  OH  . TYR A 71  ? 0.11698 0.34665 0.12769 -0.02817 0.00493  0.00025  67  TYR A OH  
1100 N  N   . LEU A 72  ? 0.11649 0.22206 0.11043 0.00889  -0.00601 0.01460  68  LEU A N   
1101 C  CA  . LEU A 72  ? 0.12013 0.25128 0.12377 0.01741  -0.00869 0.02618  68  LEU A CA  
1102 C  C   . LEU A 72  ? 0.13998 0.26699 0.12723 0.01360  -0.00523 0.02243  68  LEU A C   
1103 O  O   . LEU A 72  ? 0.17306 0.28493 0.12696 0.00861  -0.01884 0.02237  68  LEU A O   
1104 C  CB  . LEU A 72  ? 0.17446 0.24165 0.13944 0.01484  0.02080  0.04580  68  LEU A CB  
1105 C  CG  . LEU A 72  ? 0.15709 0.26775 0.15262 -0.01731 0.01917  0.00084  68  LEU A CG  
1106 C  CD1 . LEU A 72  ? 0.27242 0.25612 0.16201 -0.01918 -0.00248 0.01162  68  LEU A CD1 
1107 C  CD2 . LEU A 72  ? 0.19296 0.28092 0.16922 -0.04795 0.02884  0.01437  68  LEU A CD2 
1119 N  N   . GLU A 73  ? 0.11700 0.28095 0.13228 0.01311  -0.00545 0.00847  69  GLU A N   
1120 C  CA  . GLU A 73  ? 0.10667 0.27696 0.18772 0.01312  -0.04404 0.00714  69  GLU A CA  
1121 C  C   . GLU A 73  ? 0.11589 0.27147 0.18546 0.00549  -0.05490 0.00509  69  GLU A C   
1122 O  O   . GLU A 73  ? 0.15596 0.27260 0.17823 0.01661  -0.06080 0.00064  69  GLU A O   
1123 C  CB  . GLU A 73  ? 0.11135 0.33647 0.20548 -0.00311 -0.04494 -0.01683 69  GLU A CB  
1124 C  CG  . GLU A 73  ? 0.12465 0.36233 0.28662 0.03204  -0.01860 -0.00032 69  GLU A CG  
1125 C  CD  . GLU A 73  ? 0.15215 0.44187 0.40179 0.00202  -0.05633 0.01356  69  GLU A CD  
1126 O  OE1 . GLU A 73  ? 0.22660 0.44399 0.44677 -0.01984 -0.02447 0.03871  69  GLU A OE1 
1127 O  OE2 . GLU A 73  ? 0.23090 0.48763 0.45624 -0.02341 -0.08301 -0.02148 69  GLU A OE2 
1134 N  N   . ASN A 74  ? 0.13515 0.25611 0.14782 0.00927  -0.04151 0.01029  70  ASN A N   
1135 C  CA  . ASN A 74  ? 0.14108 0.25934 0.13726 -0.01541 -0.04487 -0.01836 70  ASN A CA  
1136 C  C   . ASN A 74  ? 0.12329 0.23753 0.13404 -0.03004 -0.01397 0.00729  70  ASN A C   
1137 O  O   . ASN A 74  ? 0.10829 0.24522 0.17564 -0.01505 0.00625  0.01542  70  ASN A O   
1138 C  CB  . ASN A 74  ? 0.15270 0.28325 0.17834 -0.02506 -0.06341 -0.04488 70  ASN A CB  
1139 C  CG  . ASN A 74  ? 0.18212 0.30801 0.26414 -0.01898 -0.10968 -0.04244 70  ASN A CG  
1140 O  OD1 . ASN A 74  ? 0.23029 0.32576 0.27744 -0.00782 -0.03763 -0.06527 70  ASN A OD1 
1141 N  ND2 . ASN A 74  ? 0.27942 0.32018 0.30747 0.00445  -0.15485 -0.06367 70  ASN A ND2 
1148 N  N   . PRO A 75  ? 0.13202 0.24619 0.09674 -0.00867 -0.03685 0.00457  71  PRO A N   
1149 C  CA  . PRO A 75  ? 0.14732 0.23804 0.09200 0.00359  -0.02159 0.00607  71  PRO A CA  
1150 C  C   . PRO A 75  ? 0.10384 0.25177 0.14775 -0.01756 -0.05649 -0.00630 71  PRO A C   
1151 O  O   . PRO A 75  ? 0.11514 0.26510 0.13961 0.00750  -0.03901 -0.01194 71  PRO A O   
1152 C  CB  . PRO A 75  ? 0.14930 0.24613 0.12633 -0.01914 0.01519  0.00841  71  PRO A CB  
1153 C  CG  . PRO A 75  ? 0.16418 0.23084 0.14346 -0.03820 -0.01089 -0.00850 71  PRO A CG  
1154 C  CD  . PRO A 75  ? 0.18214 0.22446 0.11935 0.00051  -0.03189 0.00163  71  PRO A CD  
1162 N  N   . LYS A 76  ? 0.14444 0.29076 0.13310 -0.00719 -0.03546 0.00772  72  LYS A N   
1163 C  CA  . LYS A 76  ? 0.17299 0.27170 0.18305 0.00398  0.01097  -0.02287 72  LYS A CA  
1164 C  C   . LYS A 76  ? 0.17492 0.25411 0.19001 0.00360  -0.01772 -0.01930 72  LYS A C   
1165 O  O   . LYS A 76  ? 0.17402 0.26514 0.23782 0.03556  0.00616  0.00600  72  LYS A O   
1166 C  CB  . LYS A 76  ? 0.21626 0.30858 0.18192 -0.02328 0.02483  -0.02608 72  LYS A CB  
1167 C  CG  . LYS A 76  ? 0.34582 0.38665 0.19846 -0.00739 0.01200  -0.05199 72  LYS A CG  
1168 C  CD  . LYS A 76  ? 0.49782 0.46167 0.28515 -0.04413 0.02048  -0.05567 72  LYS A CD  
1169 C  CE  . LYS A 76  ? 0.64937 0.51598 0.38288 -0.05216 0.03851  -0.04499 72  LYS A CE  
1170 N  NZ  . LYS A 76  ? 0.70413 0.53731 0.44187 -0.08858 0.01817  -0.06655 72  LYS A NZ  
1184 N  N   A LYS A 77  ? 0.13105 0.23893 0.17316 -0.01088 -0.06837 -0.02607 73  LYS A N   
1185 N  N   B LYS A 77  ? 0.18325 0.21916 0.17473 0.01514  -0.00103 -0.01379 73  LYS A N   
1186 C  CA  A LYS A 77  ? 0.11518 0.24972 0.17776 0.00276  -0.07388 -0.02310 73  LYS A CA  
1187 C  CA  B LYS A 77  ? 0.17130 0.21165 0.16328 0.01196  -0.00418 -0.01376 73  LYS A CA  
1188 C  C   A LYS A 77  ? 0.10631 0.23951 0.17172 -0.01303 -0.06983 -0.01088 73  LYS A C   
1189 C  C   B LYS A 77  ? 0.17336 0.19675 0.17404 -0.00705 0.00574  -0.00375 73  LYS A C   
1190 O  O   A LYS A 77  ? 0.12416 0.25095 0.18054 -0.00626 -0.08466 -0.00157 73  LYS A O   
1191 O  O   B LYS A 77  ? 0.23467 0.16598 0.19747 -0.02681 0.04990  -0.00074 73  LYS A O   
1192 C  CB  A LYS A 77  ? 0.10787 0.29277 0.21070 -0.00624 -0.06303 -0.03161 73  LYS A CB  
1193 C  CB  B LYS A 77  ? 0.16119 0.23956 0.14858 0.00010  -0.00740 -0.02700 73  LYS A CB  
1194 C  CG  A LYS A 77  ? 0.17368 0.33146 0.26785 -0.02887 -0.02712 -0.00769 73  LYS A CG  
1195 C  CG  B LYS A 77  ? 0.17964 0.25716 0.11964 -0.02236 0.00145  -0.02260 73  LYS A CG  
1196 C  CD  A LYS A 77  ? 0.18144 0.37696 0.30013 -0.04182 -0.03262 0.01885  73  LYS A CD  
1197 C  CD  B LYS A 77  ? 0.15413 0.26701 0.13950 -0.03197 -0.01043 -0.03650 73  LYS A CD  
1198 C  CE  A LYS A 77  ? 0.22454 0.41738 0.31102 -0.02638 -0.01989 0.02403  73  LYS A CE  
1199 C  CE  B LYS A 77  ? 0.12737 0.25545 0.15816 -0.01640 -0.01671 -0.01477 73  LYS A CE  
1200 N  NZ  A LYS A 77  ? 0.19465 0.42289 0.28297 -0.02337 -0.01936 0.02536  73  LYS A NZ  
1201 N  NZ  B LYS A 77  ? 0.07258 0.23974 0.15672 -0.00184 -0.03316 -0.01683 73  LYS A NZ  
1228 N  N   . TYR A 78  ? 0.13640 0.21274 0.16060 -0.00834 -0.02822 0.00139  74  TYR A N   
1229 C  CA  . TYR A 78  ? 0.12648 0.23814 0.13110 -0.01911 -0.01961 0.00025  74  TYR A CA  
1230 C  C   . TYR A 78  ? 0.10881 0.24348 0.13135 -0.00937 -0.00675 0.00059  74  TYR A C   
1231 O  O   . TYR A 78  ? 0.15290 0.25357 0.12635 -0.00394 0.00153  0.01772  74  TYR A O   
1232 C  CB  . TYR A 78  ? 0.13701 0.24929 0.13627 -0.03010 -0.02451 0.01091  74  TYR A CB  
1233 C  CG  . TYR A 78  ? 0.10772 0.27082 0.13466 -0.00803 -0.02346 0.00731  74  TYR A CG  
1234 C  CD1 . TYR A 78  ? 0.11630 0.27578 0.14672 -0.01658 -0.01692 -0.00599 74  TYR A CD1 
1235 C  CD2 . TYR A 78  ? 0.12203 0.26249 0.12401 -0.01364 -0.02924 0.02025  74  TYR A CD2 
1236 C  CE1 . TYR A 78  ? 0.13153 0.26363 0.15486 -0.01827 0.00450  -0.00323 74  TYR A CE1 
1237 C  CE2 . TYR A 78  ? 0.13598 0.25875 0.13159 -0.00110 -0.00300 0.02586  74  TYR A CE2 
1238 C  CZ  . TYR A 78  ? 0.13124 0.27637 0.11124 -0.00050 0.00716  0.00649  74  TYR A CZ  
1239 O  OH  . TYR A 78  ? 0.15674 0.29162 0.13815 -0.01200 0.02113  -0.00501 74  TYR A OH  
1249 N  N   . ILE A 79  ? 0.12080 0.24691 0.12344 -0.02279 -0.02596 0.00022  75  ILE A N   
1250 C  CA  . ILE A 79  ? 0.10105 0.27424 0.12532 -0.02136 -0.02221 0.01414  75  ILE A CA  
1251 C  C   . ILE A 79  ? 0.10975 0.26162 0.11389 -0.01274 -0.03102 0.01303  75  ILE A C   
1252 O  O   . ILE A 79  ? 0.12062 0.24416 0.12723 -0.00533 -0.00385 -0.00910 75  ILE A O   
1253 C  CB  . ILE A 79  ? 0.09495 0.29155 0.14076 0.01036  -0.02773 0.00635  75  ILE A CB  
1254 C  CG1 . ILE A 79  ? 0.13977 0.26862 0.11903 -0.00769 0.00455  -0.01773 75  ILE A CG1 
1255 C  CG2 . ILE A 79  ? 0.14012 0.29897 0.13905 -0.00045 -0.04914 -0.00930 75  ILE A CG2 
1256 C  CD1 . ILE A 79  ? 0.14878 0.26251 0.13175 0.00914  -0.00056 -0.01624 75  ILE A CD1 
1268 N  N   . PRO A 80  ? 0.15172 0.22732 0.12899 0.00196  -0.01331 0.00357  76  PRO A N   
1269 C  CA  . PRO A 80  ? 0.16727 0.23128 0.14361 0.00005  -0.02362 -0.02194 76  PRO A CA  
1270 C  C   . PRO A 80  ? 0.13805 0.21420 0.17125 -0.02361 -0.00803 -0.03406 76  PRO A C   
1271 O  O   . PRO A 80  ? 0.15019 0.25850 0.19605 0.00943  -0.02809 -0.01940 76  PRO A O   
1272 C  CB  . PRO A 80  ? 0.16431 0.23101 0.15883 -0.01527 -0.01925 -0.00196 76  PRO A CB  
1273 C  CG  . PRO A 80  ? 0.18074 0.22779 0.20172 -0.02738 -0.01912 0.00499  76  PRO A CG  
1274 C  CD  . PRO A 80  ? 0.17890 0.23104 0.16246 -0.01575 0.01123  0.00779  76  PRO A CD  
1282 N  N   . GLY A 81  ? 0.21152 0.22586 0.17935 0.01356  0.03865  -0.00304 77  GLY A N   
1283 C  CA  . GLY A 81  ? 0.21512 0.24779 0.22819 0.01356  0.04756  -0.03672 77  GLY A CA  
1284 C  C   . GLY A 81  ? 0.19056 0.24717 0.21313 0.01876  0.02500  -0.01482 77  GLY A C   
1285 O  O   . GLY A 81  ? 0.17541 0.30115 0.27221 -0.00476 0.07502  -0.02570 77  GLY A O   
1289 N  N   . THR A 82  ? 0.22100 0.24428 0.16917 0.02106  0.02241  -0.03437 78  THR A N   
1290 C  CA  . THR A 82  ? 0.21209 0.26474 0.13067 -0.00791 0.00357  -0.03830 78  THR A CA  
1291 C  C   . THR A 82  ? 0.19502 0.29456 0.16087 0.01143  -0.02964 -0.01982 78  THR A C   
1292 O  O   . THR A 82  ? 0.20447 0.29542 0.20708 0.03586  -0.01331 -0.02869 78  THR A O   
1293 C  CB  . THR A 82  ? 0.20767 0.24011 0.10743 0.02428  -0.01201 -0.02058 78  THR A CB  
1294 O  OG1 . THR A 82  ? 0.19533 0.26244 0.14162 -0.00120 0.01058  -0.03243 78  THR A OG1 
1295 C  CG2 . THR A 82  ? 0.20659 0.26532 0.20739 0.02518  0.01421  -0.01049 78  THR A CG2 
1303 N  N   . LYS A 83  ? 0.18053 0.31553 0.16401 0.01807  -0.00825 -0.02685 79  LYS A N   
1304 C  CA  A LYS A 83  ? 0.18342 0.33917 0.18014 0.01246  0.00831  -0.01328 79  LYS A CA  
1305 C  CA  B LYS A 83  ? 0.19434 0.33431 0.18323 0.02480  0.02755  -0.02671 79  LYS A CA  
1306 C  C   . LYS A 83  ? 0.16530 0.33194 0.15655 0.01455  0.03479  -0.00978 79  LYS A C   
1307 O  O   . LYS A 83  ? 0.22261 0.35332 0.17389 0.01790  0.03503  0.00933  79  LYS A O   
1308 C  CB  A LYS A 83  ? 0.17675 0.35638 0.20102 -0.01514 -0.00338 -0.00009 79  LYS A CB  
1309 C  CB  B LYS A 83  ? 0.21435 0.34494 0.20437 0.01633  0.04616  -0.04592 79  LYS A CB  
1310 C  CG  A LYS A 83  ? 0.15383 0.36366 0.23617 -0.02646 -0.02018 0.02935  79  LYS A CG  
1311 C  CG  B LYS A 83  ? 0.24117 0.34340 0.23930 0.01405  0.04897  -0.05932 79  LYS A CG  
1312 C  CD  A LYS A 83  ? 0.13085 0.37918 0.24601 -0.06312 -0.00037 0.04623  79  LYS A CD  
1313 C  CD  B LYS A 83  ? 0.25836 0.35820 0.24113 -0.01385 0.04941  -0.06127 79  LYS A CD  
1314 C  CE  A LYS A 83  ? 0.12426 0.38800 0.26131 -0.07335 0.00443  0.03898  79  LYS A CE  
1315 C  CE  B LYS A 83  ? 0.27266 0.35778 0.23434 0.00260  0.05923  -0.05292 79  LYS A CE  
1316 N  NZ  A LYS A 83  ? 0.12058 0.41805 0.27125 -0.05805 0.00774  0.03097  79  LYS A NZ  
1317 N  NZ  B LYS A 83  ? 0.22835 0.34169 0.19879 0.01163  0.04414  -0.06031 79  LYS A NZ  
1342 N  N   . MET A 84  ? 0.17632 0.32247 0.14618 0.02716  0.01036  -0.02590 80  MET A N   
1343 C  CA  . MET A 84  ? 0.15614 0.32264 0.15799 0.01116  0.02270  -0.02670 80  MET A CA  
1344 C  C   . MET A 84  ? 0.15844 0.36531 0.17408 0.01298  -0.01973 -0.02088 80  MET A C   
1345 O  O   . MET A 84  ? 0.18569 0.37468 0.19051 0.00523  -0.06668 -0.00679 80  MET A O   
1346 C  CB  . MET A 84  ? 0.12812 0.31506 0.18685 -0.00633 -0.00472 -0.01570 80  MET A CB  
1347 C  CG  . MET A 84  ? 0.13867 0.27367 0.17718 0.05154  0.06114  -0.03390 80  MET A CG  
1348 S  SD  . MET A 84  ? 0.13360 0.27358 0.14604 -0.00486 -0.01493 -0.01506 80  MET A SD  
1349 C  CE  . MET A 84  ? 0.13645 0.26962 0.16789 -0.01478 -0.02929 -0.00267 80  MET A CE  
1359 N  N   . ILE A 85  ? 0.17547 0.40409 0.15010 0.01800  0.02033  -0.02440 81  ILE A N   
1360 C  CA  . ILE A 85  ? 0.20147 0.42459 0.14627 0.03411  -0.00052 0.01128  81  ILE A CA  
1361 C  C   . ILE A 85  ? 0.24350 0.43292 0.16724 0.04749  0.00639  0.03546  81  ILE A C   
1362 O  O   . ILE A 85  ? 0.22466 0.43903 0.22828 -0.00016 -0.01450 0.00468  81  ILE A O   
1363 C  CB  . ILE A 85  ? 0.23864 0.45569 0.16411 0.05782  0.02088  -0.01914 81  ILE A CB  
1364 C  CG1 . ILE A 85  ? 0.29600 0.46858 0.21241 0.03604  0.10590  -0.01615 81  ILE A CG1 
1365 C  CG2 . ILE A 85  ? 0.25050 0.48497 0.19009 0.02536  -0.01782 -0.02561 81  ILE A CG2 
1366 C  CD1 . ILE A 85  ? 0.39532 0.48785 0.27894 0.02278  0.09593  -0.03201 81  ILE A CD1 
1378 N  N   . PHE A 86  ? 0.22039 0.42806 0.17246 0.04554  -0.01152 0.04130  82  PHE A N   
1379 C  CA  . PHE A 86  ? 0.18783 0.43085 0.20765 0.02384  0.01798  0.02246  82  PHE A CA  
1380 C  C   . PHE A 86  ? 0.21756 0.46587 0.22887 -0.00234 0.02020  -0.00678 82  PHE A C   
1381 O  O   . PHE A 86  ? 0.25431 0.42850 0.23492 0.00107  0.00345  -0.02319 82  PHE A O   
1382 C  CB  . PHE A 86  ? 0.20716 0.41582 0.22429 0.04709  -0.01492 0.02548  82  PHE A CB  
1383 C  CG  . PHE A 86  ? 0.15911 0.36743 0.19090 0.00923  -0.02578 -0.02974 82  PHE A CG  
1384 C  CD1 . PHE A 86  ? 0.27920 0.33180 0.23940 -0.01527 0.01413  -0.02764 82  PHE A CD1 
1385 C  CD2 . PHE A 86  ? 0.14139 0.36146 0.24386 0.02910  -0.03115 -0.00992 82  PHE A CD2 
1386 C  CE1 . PHE A 86  ? 0.33583 0.35221 0.24384 0.02020  0.03658  0.00785  82  PHE A CE1 
1387 C  CE2 . PHE A 86  ? 0.17734 0.35388 0.26847 0.01492  -0.00325 -0.01869 82  PHE A CE2 
1388 C  CZ  . PHE A 86  ? 0.25811 0.34500 0.26368 0.02381  0.01442  0.01647  82  PHE A CZ  
1398 N  N   . ALA A 87  ? 0.21757 0.52749 0.25637 -0.03937 -0.03059 0.00443  83  ALA A N   
1399 C  CA  . ALA A 87  ? 0.27474 0.56735 0.27796 -0.10241 -0.01432 -0.03725 83  ALA A CA  
1400 C  C   . ALA A 87  ? 0.24815 0.53787 0.25708 -0.08893 -0.05345 -0.05077 83  ALA A C   
1401 O  O   . ALA A 87  ? 0.31375 0.58666 0.34440 -0.13074 0.03311  -0.08184 83  ALA A O   
1402 C  CB  . ALA A 87  ? 0.26113 0.61466 0.29615 -0.12443 -0.04655 -0.03839 83  ALA A CB  
1408 N  N   . GLY A 88  ? 0.17466 0.48928 0.23378 0.03903  0.00179  -0.00658 84  GLY A N   
1409 C  CA  . GLY A 88  ? 0.15409 0.43993 0.20653 0.04795  -0.00869 0.03553  84  GLY A CA  
1410 C  C   . GLY A 88  ? 0.19651 0.43430 0.18421 0.06121  -0.03565 0.04768  84  GLY A C   
1411 O  O   . GLY A 88  ? 0.31952 0.47000 0.16156 0.14054  -0.02619 0.03284  84  GLY A O   
1415 N  N   . LEU A 89  ? 0.15218 0.38761 0.15418 0.02659  -0.01770 0.03097  85  LEU A N   
1416 C  CA  . LEU A 89  ? 0.17997 0.37870 0.16708 0.04866  -0.00982 0.04576  85  LEU A CA  
1417 C  C   . LEU A 89  ? 0.18238 0.36169 0.17311 0.05488  -0.03152 0.02335  85  LEU A C   
1418 O  O   . LEU A 89  ? 0.18383 0.36980 0.16231 0.03025  -0.02674 0.00949  85  LEU A O   
1419 C  CB  . LEU A 89  ? 0.30460 0.41361 0.21836 0.02009  -0.03370 0.03630  85  LEU A CB  
1420 C  CG  . LEU A 89  ? 0.42343 0.46713 0.28555 -0.03269 0.03015  0.03446  85  LEU A CG  
1421 C  CD1 . LEU A 89  ? 0.45014 0.48922 0.29729 -0.07303 0.04292  0.01305  85  LEU A CD1 
1422 C  CD2 . LEU A 89  ? 0.43537 0.44927 0.28021 -0.06157 0.07328  0.06395  85  LEU A CD2 
1434 N  N   . LYS A 90  ? 0.18707 0.38486 0.16682 0.06827  0.01189  0.01017  86  LYS A N   
1435 C  CA  . LYS A 90  ? 0.19223 0.41036 0.18271 0.04822  -0.00532 -0.03784 86  LYS A CA  
1436 C  C   . LYS A 90  ? 0.15996 0.38383 0.20384 0.03712  -0.00659 -0.04551 86  LYS A C   
1437 O  O   . LYS A 90  ? 0.24674 0.39412 0.29912 0.01773  0.07656  -0.00513 86  LYS A O   
1438 C  CB  . LYS A 90  ? 0.24900 0.44429 0.21147 0.06425  -0.02995 -0.05739 86  LYS A CB  
1439 C  CG  . LYS A 90  ? 0.33383 0.48968 0.26112 0.10442  -0.01136 -0.05320 86  LYS A CG  
1440 C  CD  . LYS A 90  ? 0.35131 0.51188 0.28844 0.10337  -0.06570 -0.07019 86  LYS A CD  
1441 C  CE  . LYS A 90  ? 0.33617 0.51730 0.27158 0.11038  -0.14472 -0.07238 86  LYS A CE  
1442 N  NZ  . LYS A 90  ? 0.38466 0.50948 0.25383 0.07176  -0.13072 -0.12163 86  LYS A NZ  
1456 N  N   . LYS A 91  ? 0.10468 0.36361 0.18707 0.01739  -0.03009 -0.03152 87  LYS A N   
1457 C  CA  . LYS A 91  ? 0.10080 0.37714 0.20704 0.00792  -0.02364 -0.03083 87  LYS A CA  
1458 C  C   . LYS A 91  ? 0.10144 0.35462 0.18013 -0.00716 -0.02826 -0.04031 87  LYS A C   
1459 O  O   . LYS A 91  ? 0.10366 0.37232 0.17594 -0.00636 -0.02121 -0.03639 87  LYS A O   
1460 C  CB  . LYS A 91  ? 0.18786 0.42467 0.18807 0.06276  -0.05638 -0.03243 87  LYS A CB  
1461 C  CG  . LYS A 91  ? 0.29936 0.46763 0.19619 0.08077  -0.10109 -0.02313 87  LYS A CG  
1462 C  CD  . LYS A 91  ? 0.43374 0.51644 0.24828 0.10145  -0.13345 0.03390  87  LYS A CD  
1463 C  CE  . LYS A 91  ? 0.57943 0.56110 0.30390 0.08831  -0.12864 0.05845  87  LYS A CE  
1464 N  NZ  . LYS A 91  ? 0.66134 0.58936 0.32898 0.07997  -0.11878 0.06311  87  LYS A NZ  
1478 N  N   . PRO A 92  ? 0.10736 0.35435 0.16741 -0.00981 -0.03503 -0.02784 88  PRO A N   
1479 C  CA  . PRO A 92  ? 0.09886 0.34824 0.17218 0.00180  -0.03133 -0.00564 88  PRO A CA  
1480 C  C   . PRO A 92  ? 0.08788 0.33468 0.18059 0.01548  -0.00053 -0.00815 88  PRO A C   
1481 O  O   . PRO A 92  ? 0.09212 0.32419 0.17623 0.00012  -0.00356 -0.02978 88  PRO A O   
1482 C  CB  . PRO A 92  ? 0.15754 0.38007 0.19370 -0.01973 0.00297  -0.02175 88  PRO A CB  
1483 C  CG  . PRO A 92  ? 0.18303 0.43410 0.24041 -0.04315 0.01955  -0.02835 88  PRO A CG  
1484 C  CD  . PRO A 92  ? 0.11745 0.41053 0.23047 -0.03369 -0.02462 -0.04709 88  PRO A CD  
1492 N  N   . ASN A 93  ? 0.11546 0.35553 0.20616 0.04189  0.02307  -0.03284 89  ASN A N   
1493 C  CA  . ASN A 93  ? 0.17383 0.35430 0.19892 0.06394  0.01481  -0.00276 89  ASN A CA  
1494 C  C   . ASN A 93  ? 0.17458 0.34150 0.15741 0.04664  -0.00150 0.00930  89  ASN A C   
1495 O  O   . ASN A 93  ? 0.20781 0.32513 0.15162 0.03987  -0.01237 0.00057  89  ASN A O   
1496 C  CB  . ASN A 93  ? 0.22081 0.41663 0.26416 0.08239  0.02407  -0.01926 89  ASN A CB  
1497 C  CG  . ASN A 93  ? 0.30969 0.46129 0.33339 0.08288  -0.01915 -0.04387 89  ASN A CG  
1498 O  OD1 . ASN A 93  ? 0.35106 0.47314 0.35525 0.07985  -0.06474 -0.08693 89  ASN A OD1 
1499 N  ND2 . ASN A 93  ? 0.32883 0.49331 0.33897 0.10886  -0.08056 0.00627  89  ASN A ND2 
1506 N  N   . GLU A 94  ? 0.14049 0.32823 0.14815 0.00675  -0.02752 -0.01262 90  GLU A N   
1507 C  CA  . GLU A 94  ? 0.16880 0.34026 0.10863 -0.01872 0.00408  -0.01295 90  GLU A CA  
1508 C  C   . GLU A 94  ? 0.13798 0.31825 0.10789 -0.01015 0.00387  -0.03220 90  GLU A C   
1509 O  O   . GLU A 94  ? 0.15647 0.32018 0.10402 -0.00527 -0.00330 -0.01249 90  GLU A O   
1510 C  CB  . GLU A 94  ? 0.23183 0.38169 0.14495 0.00439  -0.02220 -0.01662 90  GLU A CB  
1511 C  CG  . GLU A 94  ? 0.33418 0.41531 0.14784 0.01757  -0.05266 0.02597  90  GLU A CG  
1512 C  CD  . GLU A 94  ? 0.48881 0.45393 0.17988 0.07075  -0.06398 0.03606  90  GLU A CD  
1513 O  OE1 . GLU A 94  ? 0.56152 0.45794 0.19195 0.07726  0.02803  -0.00958 90  GLU A OE1 
1514 O  OE2 . GLU A 94  ? 0.60453 0.50589 0.20416 0.07727  -0.08273 0.03315  90  GLU A OE2 
1521 N  N   . ARG A 95  ? 0.10380 0.28699 0.14119 -0.00569 0.00866  -0.02243 91  ARG A N   
1522 C  CA  . ARG A 95  ? 0.11763 0.25786 0.15629 0.01611  0.00541  -0.00535 91  ARG A CA  
1523 C  C   . ARG A 95  ? 0.07843 0.25711 0.14469 0.00183  0.01813  0.00111  91  ARG A C   
1524 O  O   . ARG A 95  ? 0.09528 0.26730 0.15568 -0.00114 -0.01488 0.00483  91  ARG A O   
1525 C  CB  . ARG A 95  ? 0.14359 0.25615 0.19429 0.01617  -0.01735 -0.01421 91  ARG A CB  
1526 C  CG  . ARG A 95  ? 0.19974 0.25778 0.21082 0.04803  0.00190  -0.01652 91  ARG A CG  
1527 C  CD  . ARG A 95  ? 0.14347 0.27507 0.22239 0.03998  -0.02641 -0.01480 91  ARG A CD  
1528 N  NE  . ARG A 95  ? 0.26903 0.29418 0.32207 0.02565  0.00339  -0.03245 91  ARG A NE  
1529 C  CZ  . ARG A 95  ? 0.20354 0.30904 0.29559 0.03301  -0.09595 -0.02463 91  ARG A CZ  
1530 N  NH1 . ARG A 95  ? 0.25113 0.37678 0.24755 0.04407  -0.05175 0.01539  91  ARG A NH1 
1531 N  NH2 . ARG A 95  ? 0.29255 0.34573 0.38869 0.06927  -0.13936 -0.01953 91  ARG A NH2 
1545 N  N   . GLY A 96  ? 0.09955 0.26313 0.13131 -0.00635 0.00806  0.00314  92  GLY A N   
1546 C  CA  . GLY A 96  ? 0.13118 0.26716 0.13665 -0.00277 0.02088  0.01950  92  GLY A CA  
1547 C  C   . GLY A 96  ? 0.09984 0.27378 0.13733 0.03523  -0.01674 0.02502  92  GLY A C   
1548 O  O   . GLY A 96  ? 0.10218 0.27939 0.11715 0.00877  0.00821  0.01092  92  GLY A O   
1552 N  N   . ASP A 97  ? 0.11718 0.26297 0.13122 0.02854  0.01041  -0.00371 93  ASP A N   
1553 C  CA  . ASP A 97  ? 0.11164 0.23865 0.12544 0.00638  0.00695  -0.01277 93  ASP A CA  
1554 C  C   . ASP A 97  ? 0.13807 0.25359 0.10266 0.01376  -0.00129 -0.00778 93  ASP A C   
1555 O  O   . ASP A 97  ? 0.11533 0.26137 0.09655 0.00469  -0.00125 0.00661  93  ASP A O   
1556 C  CB  . ASP A 97  ? 0.10816 0.25408 0.14947 0.00466  -0.01636 -0.00091 93  ASP A CB  
1557 C  CG  . ASP A 97  ? 0.16577 0.29772 0.13875 -0.00033 -0.01478 -0.00236 93  ASP A CG  
1558 O  OD1 . ASP A 97  ? 0.16559 0.29833 0.15339 0.02186  -0.01598 -0.01982 93  ASP A OD1 
1559 O  OD2 . ASP A 97  ? 0.17279 0.35744 0.16760 0.01086  -0.00135 0.01207  93  ASP A OD2 
1564 N  N   . LEU A 98  ? 0.11074 0.23640 0.11436 -0.00660 0.01365  -0.01403 94  LEU A N   
1565 C  CA  . LEU A 98  ? 0.09335 0.23147 0.12754 0.00125  0.00649  -0.00873 94  LEU A CA  
1566 C  C   . LEU A 98  ? 0.06977 0.26224 0.11561 0.00071  0.01410  -0.00984 94  LEU A C   
1567 O  O   . LEU A 98  ? 0.10083 0.24936 0.12614 0.00366  0.00473  0.00669  94  LEU A O   
1568 C  CB  . LEU A 98  ? 0.11033 0.24183 0.12852 -0.00083 0.00270  -0.00632 94  LEU A CB  
1569 C  CG  . LEU A 98  ? 0.09728 0.26918 0.16280 -0.00812 0.00718  -0.02099 94  LEU A CG  
1570 C  CD1 . LEU A 98  ? 0.12484 0.28136 0.12383 -0.01636 0.00589  -0.00563 94  LEU A CD1 
1571 C  CD2 . LEU A 98  ? 0.13615 0.27934 0.18799 0.01873  0.00554  0.01004  94  LEU A CD2 
1583 N  N   . ILE A 99  ? 0.10112 0.24865 0.10368 -0.00820 -0.00139 -0.01822 95  ILE A N   
1584 C  CA  . ILE A 99  ? 0.11383 0.24852 0.11816 0.00672  -0.02296 -0.00261 95  ILE A CA  
1585 C  C   . ILE A 99  ? 0.10343 0.24540 0.10948 -0.02432 0.00993  -0.00661 95  ILE A C   
1586 O  O   . ILE A 99  ? 0.12166 0.26369 0.10860 -0.01306 -0.00028 0.01012  95  ILE A O   
1587 C  CB  . ILE A 99  ? 0.11532 0.25041 0.12581 -0.01678 -0.02114 0.01684  95  ILE A CB  
1588 C  CG1 . ILE A 99  ? 0.11925 0.25141 0.17472 -0.01078 -0.05252 0.02838  95  ILE A CG1 
1589 C  CG2 . ILE A 99  ? 0.13149 0.25755 0.16569 -0.01495 -0.03229 0.01987  95  ILE A CG2 
1590 C  CD1 . ILE A 99  ? 0.18914 0.25225 0.17448 0.00578  -0.07229 0.02632  95  ILE A CD1 
1602 N  N   . ALA A 100 ? 0.10112 0.26447 0.11919 0.00417  0.01724  -0.02096 96  ALA A N   
1603 C  CA  . ALA A 100 ? 0.11620 0.28129 0.11932 0.01510  0.01823  -0.00071 96  ALA A CA  
1604 C  C   . ALA A 100 ? 0.12397 0.27708 0.11148 0.00304  0.00186  -0.00467 96  ALA A C   
1605 O  O   . ALA A 100 ? 0.15959 0.26888 0.09872 -0.01013 0.01322  -0.01439 96  ALA A O   
1606 C  CB  . ALA A 100 ? 0.14533 0.26926 0.12963 0.00387  0.03457  -0.03194 96  ALA A CB  
1612 N  N   . TYR A 101 ? 0.11940 0.25713 0.09578 0.01025  -0.00284 -0.00783 97  TYR A N   
1613 C  CA  . TYR A 101 ? 0.09184 0.24476 0.11198 -0.00082 -0.00226 0.00380  97  TYR A CA  
1614 C  C   . TYR A 101 ? 0.13277 0.23471 0.09408 0.00103  0.00532  0.01643  97  TYR A C   
1615 O  O   . TYR A 101 ? 0.12556 0.25380 0.10871 -0.00946 -0.02859 0.00018  97  TYR A O   
1616 C  CB  . TYR A 101 ? 0.10327 0.24190 0.10496 -0.00468 0.01072  0.00339  97  TYR A CB  
1617 C  CG  . TYR A 101 ? 0.11694 0.22829 0.09356 0.01714  -0.00037 0.02542  97  TYR A CG  
1618 C  CD1 . TYR A 101 ? 0.14561 0.22770 0.09989 0.02809  0.00281  0.03266  97  TYR A CD1 
1619 C  CD2 . TYR A 101 ? 0.11888 0.23354 0.10449 0.01053  -0.02321 -0.00766 97  TYR A CD2 
1620 C  CE1 . TYR A 101 ? 0.12236 0.23317 0.10805 0.01034  0.01169  -0.00402 97  TYR A CE1 
1621 C  CE2 . TYR A 101 ? 0.14286 0.24316 0.09336 0.01950  -0.01345 -0.02347 97  TYR A CE2 
1622 C  CZ  . TYR A 101 ? 0.14051 0.26829 0.12188 0.00229  0.01986  -0.01052 97  TYR A CZ  
1623 O  OH  . TYR A 101 ? 0.11305 0.29723 0.15058 -0.00058 0.01967  -0.02092 97  TYR A OH  
1633 N  N   . LEU A 102 ? 0.09063 0.24165 0.09406 -0.01055 0.00980  0.01905  98  LEU A N   
1634 C  CA  . LEU A 102 ? 0.11392 0.23447 0.11126 -0.00251 0.01231  0.01996  98  LEU A CA  
1635 C  C   . LEU A 102 ? 0.11600 0.22025 0.09019 0.01880  0.00797  0.00451  98  LEU A C   
1636 O  O   . LEU A 102 ? 0.10304 0.23794 0.12027 -0.00261 -0.01285 0.00710  98  LEU A O   
1637 C  CB  . LEU A 102 ? 0.11263 0.24738 0.10477 0.01112  -0.00955 0.02088  98  LEU A CB  
1638 C  CG  . LEU A 102 ? 0.15191 0.26274 0.13028 0.02623  0.01687  0.02423  98  LEU A CG  
1639 C  CD1 . LEU A 102 ? 0.20260 0.27862 0.16428 0.02680  0.03404  -0.01108 98  LEU A CD1 
1640 C  CD2 . LEU A 102 ? 0.19916 0.30331 0.16127 0.04238  0.09134  0.03851  98  LEU A CD2 
1652 N  N   . LYS A 103 ? 0.11488 0.23533 0.08183 0.01120  0.00619  0.00503  99  LYS A N   
1653 C  CA  . LYS A 103 ? 0.10814 0.24271 0.09911 0.00531  0.02545  0.02405  99  LYS A CA  
1654 C  C   . LYS A 103 ? 0.11759 0.22340 0.14590 -0.01856 -0.01988 -0.00845 99  LYS A C   
1655 O  O   . LYS A 103 ? 0.14385 0.23658 0.15042 0.01018  -0.02906 -0.01420 99  LYS A O   
1656 C  CB  . LYS A 103 ? 0.11753 0.26306 0.09565 0.00977  0.01593  0.00323  99  LYS A CB  
1657 C  CG  . LYS A 103 ? 0.14518 0.27407 0.11234 0.00452  0.04738  -0.01114 99  LYS A CG  
1658 C  CD  . LYS A 103 ? 0.19628 0.35700 0.13779 0.02944  0.04411  -0.00769 99  LYS A CD  
1659 C  CE  . LYS A 103 ? 0.23012 0.38238 0.15849 0.03349  0.07622  -0.00499 99  LYS A CE  
1660 N  NZ  . LYS A 103 ? 0.25961 0.39882 0.18914 0.03615  0.04243  0.01173  99  LYS A NZ  
1674 N  N   . SER A 104 ? 0.14293 0.21476 0.13418 0.02097  0.01903  0.00722  100 SER A N   
1675 C  CA  A SER A 104 ? 0.20211 0.22674 0.17488 0.01284  0.03346  0.00979  100 SER A CA  
1676 C  CA  B SER A 104 ? 0.17200 0.21252 0.13788 -0.01100 0.00843  0.00252  100 SER A CA  
1677 C  C   . SER A 104 ? 0.18521 0.24152 0.12050 -0.03019 -0.00761 0.00130  100 SER A C   
1678 O  O   . SER A 104 ? 0.28323 0.33453 0.13937 -0.11016 0.00117  -0.03558 100 SER A O   
1679 C  CB  A SER A 104 ? 0.29965 0.29778 0.30545 0.02727  0.10072  -0.00410 100 SER A CB  
1680 C  CB  B SER A 104 ? 0.19240 0.21858 0.16790 -0.03133 0.00759  -0.01399 100 SER A CB  
1681 O  OG  A SER A 104 ? 0.34504 0.34445 0.42636 0.08148  0.15680  -0.01168 100 SER A OG  
1682 O  OG  B SER A 104 ? 0.16543 0.20252 0.19524 -0.01813 0.01652  -0.01486 100 SER A OG  
1691 N  N   . ALA A 105 ? 0.14633 0.22764 0.11759 0.00075  -0.01189 -0.00338 101 ALA A N   
1692 C  CA  . ALA A 105 ? 0.12315 0.24568 0.11587 -0.00719 -0.00351 0.01451  101 ALA A CA  
1693 C  C   . ALA A 105 ? 0.13721 0.24176 0.12776 -0.02813 0.00154  -0.00549 101 ALA A C   
1694 O  O   . ALA A 105 ? 0.17245 0.23723 0.16599 -0.02813 -0.00594 0.04379  101 ALA A O   
1695 C  CB  . ALA A 105 ? 0.14851 0.27163 0.13472 -0.02287 -0.01118 0.01569  101 ALA A CB  
1701 N  N   . THR A 106 ? 0.13255 0.21179 0.13231 -0.00623 -0.01924 0.03259  102 THR A N   
1702 C  CA  . THR A 106 ? 0.07856 0.22096 0.13442 -0.01366 -0.00823 0.02602  102 THR A CA  
1703 C  C   . THR A 106 ? 0.09341 0.26332 0.11336 -0.00925 -0.02864 0.03191  102 THR A C   
1704 O  O   . THR A 106 ? 0.10698 0.28563 0.11353 0.00804  -0.02229 0.00192  102 THR A O   
1705 C  CB  . THR A 106 ? 0.11719 0.24474 0.13126 0.01117  -0.00009 0.02458  102 THR A CB  
1706 O  OG1 . THR A 106 ? 0.10514 0.24859 0.12352 -0.01514 -0.00638 0.02718  102 THR A OG1 
1707 C  CG2 . THR A 106 ? 0.16163 0.26562 0.12199 0.01786  0.00321  -0.00398 102 THR A CG2 
1715 N  N   . LYS A 107 ? 0.11145 0.26538 0.12543 0.02355  -0.00885 0.00772  103 LYS A N   
1716 C  CA  A LYS A 107 ? 0.16110 0.28933 0.14131 0.04072  -0.02601 0.00143  103 LYS A CA  
1717 C  CA  B LYS A 107 ? 0.13531 0.28805 0.16317 0.02703  -0.01462 0.00064  103 LYS A CA  
1718 C  C   . LYS A 107 ? 0.19799 0.34331 0.14221 0.06484  0.00198  0.00352  103 LYS A C   
1719 O  O   . LYS A 107 ? 0.17206 0.30674 0.16228 0.02707  -0.01773 -0.02787 103 LYS A O   
1720 C  CB  A LYS A 107 ? 0.19589 0.28430 0.13788 0.04822  -0.02933 0.01175  103 LYS A CB  
1721 C  CB  B LYS A 107 ? 0.15995 0.29831 0.19287 0.03448  0.03619  0.02380  103 LYS A CB  
1722 C  CG  A LYS A 107 ? 0.21901 0.28366 0.15579 0.02702  -0.00583 -0.00409 103 LYS A CG  
1723 C  CG  B LYS A 107 ? 0.12703 0.32272 0.19964 0.01810  0.03131  0.01302  103 LYS A CG  
1724 C  CD  A LYS A 107 ? 0.19463 0.27942 0.18930 0.01257  -0.01814 0.00142  103 LYS A CD  
1725 C  CD  B LYS A 107 ? 0.14293 0.34259 0.24008 0.01215  0.06318  0.00647  103 LYS A CD  
1726 C  CE  A LYS A 107 ? 0.24013 0.28056 0.25968 0.02511  0.03008  0.02879  103 LYS A CE  
1727 C  CE  B LYS A 107 ? 0.18173 0.37730 0.29935 0.01708  0.11920  -0.00066 103 LYS A CE  
1728 N  NZ  A LYS A 107 ? 0.30637 0.28263 0.31157 0.04766  0.07693  0.05210  103 LYS A NZ  
1729 N  NZ  B LYS A 107 ? 0.30192 0.39004 0.34903 0.03077  0.17006  0.01040  103 LYS A NZ  
1730 O  OXT . LYS A 107 ? 0.21988 0.41161 0.15063 0.06799  -0.01747 0.02750  103 LYS A OXT 
1757 N  N   . GLY B 1   ? 0.27400 0.60950 0.27074 0.02274  0.03105  0.01153  -3  GLY B N   
1758 C  CA  . GLY B 1   ? 0.26173 0.58825 0.24106 -0.01261 0.00514  -0.00362 -3  GLY B CA  
1759 C  C   . GLY B 1   ? 0.20595 0.56455 0.21318 -0.02902 -0.00042 0.01382  -3  GLY B C   
1760 O  O   . GLY B 1   ? 0.14495 0.57785 0.20344 0.00291  -0.00301 -0.02185 -3  GLY B O   
1763 N  N   . VAL B 2   ? 0.15603 0.51171 0.16189 -0.04320 0.02081  0.03460  -2  VAL B N   
1764 C  CA  . VAL B 2   ? 0.13427 0.48535 0.20649 -0.03834 0.01959  0.03575  -2  VAL B CA  
1765 C  C   . VAL B 2   ? 0.14284 0.49896 0.20354 -0.04069 0.02081  0.05300  -2  VAL B C   
1766 O  O   . VAL B 2   ? 0.20427 0.49828 0.20791 -0.04929 0.03050  0.05028  -2  VAL B O   
1767 C  CB  . VAL B 2   ? 0.12772 0.48500 0.25648 -0.02513 -0.01152 0.06073  -2  VAL B CB  
1768 C  CG1 . VAL B 2   ? 0.14076 0.48453 0.29294 0.02387  0.04698  0.06708  -2  VAL B CG1 
1769 C  CG2 . VAL B 2   ? 0.17814 0.48942 0.25042 -0.04628 -0.00408 0.06592  -2  VAL B CG2 
1779 N  N   . PRO B 3   ? 0.13384 0.48586 0.18234 -0.04438 0.01249  0.03208  -1  PRO B N   
1780 C  CA  . PRO B 3   ? 0.16850 0.49631 0.21320 -0.08625 0.03786  0.00770  -1  PRO B CA  
1781 C  C   . PRO B 3   ? 0.24264 0.51757 0.21464 -0.09280 0.05115  0.01521  -1  PRO B C   
1782 O  O   . PRO B 3   ? 0.20611 0.52354 0.21726 -0.07850 0.00895  0.01541  -1  PRO B O   
1783 C  CB  . PRO B 3   ? 0.22696 0.52910 0.22096 -0.04838 0.02790  0.00998  -1  PRO B CB  
1784 C  CG  . PRO B 3   ? 0.17995 0.52206 0.20713 -0.02322 0.01589  0.02589  -1  PRO B CG  
1785 C  CD  . PRO B 3   ? 0.13072 0.50235 0.22159 -0.03066 0.01095  0.02010  -1  PRO B CD  
1793 N  N   . ALA B 4   ? 0.23171 0.52899 0.22101 -0.10424 0.07026  0.00315  0   ALA B N   
1794 C  CA  . ALA B 4   ? 0.24389 0.52051 0.24822 -0.11639 0.08662  -0.00936 0   ALA B CA  
1795 C  C   . ALA B 4   ? 0.26428 0.53937 0.22875 -0.10037 0.06650  0.02058  0   ALA B C   
1796 O  O   . ALA B 4   ? 0.22147 0.57649 0.23776 -0.08581 0.03128  0.03500  0   ALA B O   
1797 C  CB  . ALA B 4   ? 0.33845 0.50978 0.26362 -0.10929 0.14175  -0.01943 0   ALA B CB  
1803 N  N   . GLY B 5   ? 0.22533 0.52346 0.22493 -0.12893 0.05813  -0.01272 1   GLY B N   
1804 C  CA  . GLY B 5   ? 0.28487 0.51549 0.20980 -0.13163 0.06078  -0.02344 1   GLY B CA  
1805 C  C   . GLY B 5   ? 0.35123 0.50060 0.24915 -0.18667 0.08870  -0.03112 1   GLY B C   
1806 O  O   . GLY B 5   ? 0.44466 0.49037 0.26585 -0.21614 0.11632  -0.05762 1   GLY B O   
1810 N  N   . ASP B 6   ? 0.35497 0.50015 0.24380 -0.20387 0.08595  -0.04954 2   ASP B N   
1811 C  CA  . ASP B 6   ? 0.37279 0.50517 0.26460 -0.22803 0.07621  -0.06466 2   ASP B CA  
1812 C  C   . ASP B 6   ? 0.36229 0.47587 0.24946 -0.20919 0.07863  -0.03932 2   ASP B C   
1813 O  O   . ASP B 6   ? 0.32791 0.49439 0.21922 -0.21036 0.04849  -0.03560 2   ASP B O   
1814 C  CB  . ASP B 6   ? 0.37835 0.55441 0.30550 -0.24599 0.03728  -0.06899 2   ASP B CB  
1815 C  CG  . ASP B 6   ? 0.42822 0.58253 0.36204 -0.26839 0.05015  -0.07414 2   ASP B CG  
1816 O  OD1 . ASP B 6   ? 0.41901 0.58324 0.34745 -0.25837 0.04382  -0.05143 2   ASP B OD1 
1817 O  OD2 . ASP B 6   ? 0.49777 0.61030 0.43619 -0.28870 0.11227  -0.08089 2   ASP B OD2 
1822 N  N   . VAL B 7   ? 0.42194 0.42496 0.24330 -0.19418 0.07280  -0.02572 3   VAL B N   
1823 C  CA  . VAL B 7   ? 0.40394 0.39991 0.20440 -0.12550 0.07911  -0.00812 3   VAL B CA  
1824 C  C   . VAL B 7   ? 0.35843 0.39546 0.20574 -0.11466 0.06060  -0.01357 3   VAL B C   
1825 O  O   . VAL B 7   ? 0.32124 0.38179 0.21469 -0.10223 0.03728  -0.02511 3   VAL B O   
1826 C  CB  . VAL B 7   ? 0.54670 0.39399 0.23213 -0.07904 0.10406  0.01019  3   VAL B CB  
1827 C  CG1 . VAL B 7   ? 0.57384 0.35954 0.21920 -0.06217 0.07356  0.01861  3   VAL B CG1 
1828 C  CG2 . VAL B 7   ? 0.61591 0.39589 0.24642 -0.06653 0.10800  0.03300  3   VAL B CG2 
1838 N  N   . GLU B 8   ? 0.37822 0.41436 0.21922 -0.11246 0.05162  -0.06599 4   GLU B N   
1839 C  CA  . GLU B 8   ? 0.38204 0.44349 0.26730 -0.13399 0.04822  -0.09928 4   GLU B CA  
1840 C  C   . GLU B 8   ? 0.25712 0.44021 0.23302 -0.12168 0.04382  -0.06715 4   GLU B C   
1841 O  O   . GLU B 8   ? 0.23486 0.44494 0.20122 -0.11357 0.00930  -0.03840 4   GLU B O   
1842 C  CB  . GLU B 8   ? 0.52496 0.49157 0.35502 -0.18830 0.06334  -0.17800 4   GLU B CB  
1843 C  CG  . GLU B 8   ? 0.69138 0.56830 0.49595 -0.16220 0.14942  -0.18873 4   GLU B CG  
1844 C  CD  . GLU B 8   ? 0.81245 0.62528 0.61300 -0.16112 0.20701  -0.19818 4   GLU B CD  
1845 O  OE1 . GLU B 8   ? 0.85491 0.64773 0.64726 -0.15358 0.21688  -0.20964 4   GLU B OE1 
1846 O  OE2 . GLU B 8   ? 0.86738 0.64485 0.66120 -0.16568 0.22595  -0.18956 4   GLU B OE2 
1853 N  N   . LYS B 9   ? 0.21553 0.47619 0.23370 -0.09247 0.01454  -0.07351 5   LYS B N   
1854 C  CA  . LYS B 9   ? 0.19055 0.48835 0.21931 -0.07841 0.00220  -0.04032 5   LYS B CA  
1855 C  C   . LYS B 9   ? 0.13695 0.43815 0.15484 -0.05532 -0.01648 -0.01316 5   LYS B C   
1856 O  O   . LYS B 9   ? 0.19012 0.44215 0.14546 -0.07516 0.00874  -0.00693 5   LYS B O   
1857 C  CB  . LYS B 9   ? 0.20220 0.55126 0.27586 -0.12415 -0.01473 -0.06152 5   LYS B CB  
1858 C  CG  . LYS B 9   ? 0.23144 0.60159 0.33277 -0.13773 -0.04984 -0.04853 5   LYS B CG  
1859 C  CD  . LYS B 9   ? 0.27864 0.64229 0.38580 -0.15173 -0.09081 -0.04823 5   LYS B CD  
1860 C  CE  . LYS B 9   ? 0.37675 0.69214 0.49909 -0.10177 -0.00233 -0.00989 5   LYS B CE  
1861 N  NZ  . LYS B 9   ? 0.43531 0.72100 0.56129 -0.06179 0.03506  0.01840  5   LYS B NZ  
1875 N  N   . GLY B 10  ? 0.15673 0.40295 0.16955 -0.05412 0.02455  -0.03215 6   GLY B N   
1876 C  CA  . GLY B 10  ? 0.19530 0.36697 0.12939 -0.03317 0.03750  -0.02551 6   GLY B CA  
1877 C  C   . GLY B 10  ? 0.16781 0.33605 0.12802 -0.02523 0.02321  -0.01798 6   GLY B C   
1878 O  O   . GLY B 10  ? 0.14950 0.33569 0.11427 -0.02983 0.01178  -0.01174 6   GLY B O   
1882 N  N   . LYS B 11  ? 0.21205 0.33550 0.15918 -0.04487 0.03772  -0.03577 7   LYS B N   
1883 C  CA  . LYS B 11  ? 0.19576 0.35424 0.16479 -0.03154 0.02924  -0.03323 7   LYS B CA  
1884 C  C   . LYS B 11  ? 0.20448 0.34910 0.13381 -0.04906 0.02512  -0.03948 7   LYS B C   
1885 O  O   . LYS B 11  ? 0.16655 0.35081 0.13108 -0.03191 0.00514  -0.03156 7   LYS B O   
1886 C  CB  . LYS B 11  ? 0.24519 0.37787 0.18588 0.03125  0.01224  -0.02132 7   LYS B CB  
1887 C  CG  . LYS B 11  ? 0.31533 0.40992 0.24777 0.08467  0.01233  -0.04000 7   LYS B CG  
1888 C  CD  . LYS B 11  ? 0.43589 0.47244 0.35124 0.13368  0.07313  -0.05142 7   LYS B CD  
1889 C  CE  . LYS B 11  ? 0.58903 0.52707 0.44189 0.14589  0.13332  -0.04649 7   LYS B CE  
1890 N  NZ  . LYS B 11  ? 0.66819 0.55235 0.48953 0.16913  0.16078  -0.03188 7   LYS B NZ  
1904 N  N   . LYS B 12  ? 0.19403 0.37047 0.12070 -0.04378 0.01353  -0.04092 8   LYS B N   
1905 C  CA  . LYS B 12  ? 0.16713 0.40007 0.11774 -0.05608 -0.00225 -0.02145 8   LYS B CA  
1906 C  C   . LYS B 12  ? 0.14152 0.37773 0.11120 -0.04946 -0.00500 -0.01074 8   LYS B C   
1907 O  O   . LYS B 12  ? 0.13605 0.37675 0.10768 -0.03355 -0.00428 -0.00701 8   LYS B O   
1908 C  CB  . LYS B 12  ? 0.18507 0.44600 0.13803 -0.06518 -0.01670 -0.00031 8   LYS B CB  
1909 C  CG  . LYS B 12  ? 0.26153 0.48639 0.20829 -0.09119 -0.09200 0.00246  8   LYS B CG  
1910 C  CD  . LYS B 12  ? 0.36461 0.55848 0.24830 -0.13172 -0.10625 0.03421  8   LYS B CD  
1911 C  CE  . LYS B 12  ? 0.44987 0.60103 0.28982 -0.15781 -0.15926 0.04436  8   LYS B CE  
1912 N  NZ  . LYS B 12  ? 0.51118 0.62965 0.34220 -0.16142 -0.14561 0.02514  8   LYS B NZ  
1926 N  N   . ILE B 13  ? 0.10883 0.38053 0.12499 -0.03223 -0.01491 0.00211  9   ILE B N   
1927 C  CA  . ILE B 13  ? 0.09472 0.35528 0.12665 -0.00672 0.00557  0.00631  9   ILE B CA  
1928 C  C   . ILE B 13  ? 0.11455 0.33630 0.08617 0.00091  -0.00436 0.01705  9   ILE B C   
1929 O  O   . ILE B 13  ? 0.12654 0.32924 0.09544 -0.01925 -0.00850 0.00688  9   ILE B O   
1930 C  CB  . ILE B 13  ? 0.10271 0.36421 0.13668 -0.02045 0.02116  -0.00300 9   ILE B CB  
1931 C  CG1 . ILE B 13  ? 0.11058 0.39844 0.18549 -0.03028 0.02529  -0.01296 9   ILE B CG1 
1932 C  CG2 . ILE B 13  ? 0.11371 0.34919 0.17077 -0.00861 -0.00927 0.01283  9   ILE B CG2 
1933 C  CD1 . ILE B 13  ? 0.14192 0.44500 0.18503 0.00710  0.03713  -0.00699 9   ILE B CD1 
1945 N  N   . PHE B 14  ? 0.12329 0.32018 0.10030 -0.01181 -0.00352 0.00213  10  PHE B N   
1946 C  CA  . PHE B 14  ? 0.10953 0.32229 0.09325 -0.01692 0.01151  -0.00614 10  PHE B CA  
1947 C  C   . PHE B 14  ? 0.11656 0.33390 0.08678 -0.02016 0.00517  -0.01163 10  PHE B C   
1948 O  O   . PHE B 14  ? 0.10351 0.36489 0.09350 -0.01843 -0.00322 0.00451  10  PHE B O   
1949 C  CB  . PHE B 14  ? 0.12651 0.30707 0.11564 -0.00188 0.02216  0.00214  10  PHE B CB  
1950 C  CG  . PHE B 14  ? 0.10177 0.35991 0.10547 0.00703  0.00536  0.01604  10  PHE B CG  
1951 C  CD1 . PHE B 14  ? 0.10680 0.37771 0.13014 0.04022  -0.01453 -0.01086 10  PHE B CD1 
1952 C  CD2 . PHE B 14  ? 0.14146 0.39211 0.13110 0.03425  0.00609  0.03099  10  PHE B CD2 
1953 C  CE1 . PHE B 14  ? 0.13153 0.41131 0.17398 0.03471  -0.00285 0.01890  10  PHE B CE1 
1954 C  CE2 . PHE B 14  ? 0.13605 0.40193 0.16844 0.03621  0.02399  0.00861  10  PHE B CE2 
1955 C  CZ  . PHE B 14  ? 0.10242 0.40778 0.19265 0.00976  0.00068  0.00842  10  PHE B CZ  
1965 N  N   . VAL B 15  ? 0.11507 0.35497 0.09575 -0.01839 0.01305  -0.00757 11  VAL B N   
1966 C  CA  . VAL B 15  ? 0.12839 0.35926 0.11349 -0.01984 -0.00887 -0.03388 11  VAL B CA  
1967 C  C   . VAL B 15  ? 0.10426 0.36920 0.11028 -0.05079 0.00158  -0.01306 11  VAL B C   
1968 O  O   . VAL B 15  ? 0.10786 0.40250 0.10357 -0.03270 -0.00079 -0.01018 11  VAL B O   
1969 C  CB  . VAL B 15  ? 0.21485 0.39053 0.18369 0.02607  0.06172  -0.05615 11  VAL B CB  
1970 C  CG1 . VAL B 15  ? 0.31464 0.41307 0.23713 -0.00931 0.08301  -0.05919 11  VAL B CG1 
1971 C  CG2 . VAL B 15  ? 0.23657 0.41546 0.23704 0.04699  0.09443  -0.07312 11  VAL B CG2 
1981 N  N   . GLN B 16  ? 0.10975 0.35984 0.10939 -0.05698 0.00958  -0.01339 12  GLN B N   
1982 C  CA  . GLN B 16  ? 0.13293 0.35930 0.10741 -0.02352 0.00180  -0.00673 12  GLN B CA  
1983 C  C   . GLN B 16  ? 0.12253 0.35511 0.10306 -0.03660 0.01304  0.00564  12  GLN B C   
1984 O  O   . GLN B 16  ? 0.13381 0.36873 0.09394 -0.02760 -0.00609 0.00066  12  GLN B O   
1985 C  CB  . GLN B 16  ? 0.15563 0.35853 0.12256 -0.02714 -0.01023 -0.01186 12  GLN B CB  
1986 C  CG  . GLN B 16  ? 0.18375 0.38030 0.12269 -0.04663 -0.04402 -0.00088 12  GLN B CG  
1987 C  CD  . GLN B 16  ? 0.18568 0.43423 0.17759 -0.08780 -0.05604 0.02192  12  GLN B CD  
1988 O  OE1 . GLN B 16  ? 0.17495 0.47693 0.23905 -0.07002 -0.06363 0.05008  12  GLN B OE1 
1989 N  NE2 . GLN B 16  ? 0.20237 0.42466 0.17175 -0.09973 -0.06138 0.03065  12  GLN B NE2 
1998 N  N   . ARG B 17  ? 0.14394 0.33368 0.08597 -0.01650 -0.01120 0.00664  13  ARG B N   
1999 C  CA  . ARG B 17  ? 0.11392 0.33963 0.09870 -0.01762 -0.01896 -0.00326 13  ARG B CA  
2000 C  C   . ARG B 17  ? 0.16009 0.34158 0.09294 -0.03382 0.02073  -0.00685 13  ARG B C   
2001 O  O   . ARG B 17  ? 0.16054 0.35900 0.13355 -0.03689 -0.01029 -0.01862 13  ARG B O   
2002 C  CB  . ARG B 17  ? 0.11995 0.36888 0.11310 -0.00694 -0.01231 -0.02488 13  ARG B CB  
2003 C  CG  . ARG B 17  ? 0.17663 0.38447 0.10924 0.01979  -0.03147 -0.01185 13  ARG B CG  
2004 C  CD  . ARG B 17  ? 0.23822 0.42714 0.15127 0.00424  -0.01066 -0.00901 13  ARG B CD  
2005 N  NE  . ARG B 17  ? 0.25137 0.45427 0.20262 0.05658  -0.03336 0.02214  13  ARG B NE  
2006 C  CZ  . ARG B 17  ? 0.35685 0.46905 0.25739 0.09201  -0.02707 0.02519  13  ARG B CZ  
2007 N  NH1 . ARG B 17  ? 0.35946 0.47386 0.28998 0.06985  0.01582  0.03282  13  ARG B NH1 
2008 N  NH2 . ARG B 17  ? 0.40856 0.49834 0.28687 0.09221  -0.04214 0.02251  13  ARG B NH2 
2022 N  N   . CYS B 18  ? 0.13103 0.34296 0.08795 -0.02121 -0.00316 -0.01590 14  CYS B N   
2023 C  CA  . CYS B 18  ? 0.13285 0.35365 0.08970 -0.02933 0.00230  -0.00756 14  CYS B CA  
2024 C  C   . CYS B 18  ? 0.10385 0.36898 0.09561 -0.03580 0.00416  -0.01900 14  CYS B C   
2025 O  O   . CYS B 18  ? 0.11103 0.40709 0.10490 -0.04692 0.00228  -0.01410 14  CYS B O   
2026 C  CB  . CYS B 18  ? 0.10895 0.35691 0.09075 -0.01384 0.00275  -0.01550 14  CYS B CB  
2027 S  SG  . CYS B 18  ? 0.10287 0.36052 0.09237 -0.03011 0.00054  -0.01598 14  CYS B SG  
2032 N  N   . ALA B 19  ? 0.11758 0.39342 0.10145 -0.00992 -0.00720 -0.00515 15  ALA B N   
2033 C  CA  . ALA B 19  ? 0.11358 0.41213 0.11255 -0.04405 0.00648  -0.01750 15  ALA B CA  
2034 C  C   . ALA B 19  ? 0.09873 0.39120 0.09842 0.01399  -0.00050 -0.01089 15  ALA B C   
2035 O  O   . ALA B 19  ? 0.11074 0.42593 0.12544 -0.00643 0.00659  -0.04103 15  ALA B O   
2036 C  CB  . ALA B 19  ? 0.10898 0.41393 0.13268 0.00070  -0.00715 -0.04518 15  ALA B CB  
2042 N  N   . GLN B 20  ? 0.13941 0.39812 0.10298 -0.04297 0.00483  -0.01929 16  GLN B N   
2043 C  CA  . GLN B 20  ? 0.15112 0.43240 0.11249 -0.06258 0.00113  -0.01556 16  GLN B CA  
2044 C  C   . GLN B 20  ? 0.14633 0.43531 0.12606 -0.06019 0.02078  -0.02205 16  GLN B C   
2045 O  O   . GLN B 20  ? 0.18281 0.46788 0.15178 -0.07282 0.04099  -0.04379 16  GLN B O   
2046 C  CB  . GLN B 20  ? 0.26434 0.48305 0.17606 -0.11322 0.00636  -0.03013 16  GLN B CB  
2047 C  CG  . GLN B 20  ? 0.30699 0.51509 0.19449 -0.10792 -0.01181 -0.00129 16  GLN B CG  
2048 C  CD  . GLN B 20  ? 0.40924 0.56680 0.25105 -0.03674 0.00697  0.02777  16  GLN B CD  
2049 O  OE1 . GLN B 20  ? 0.49938 0.60225 0.27611 -0.02910 0.02452  0.02712  16  GLN B OE1 
2050 N  NE2 . GLN B 20  ? 0.34934 0.56928 0.25384 0.03583  -0.02613 0.06764  16  GLN B NE2 
2059 N  N   . CYS B 21  ? 0.12546 0.42985 0.11537 -0.06589 0.00742  -0.03522 17  CYS B N   
2060 C  CA  . CYS B 21  ? 0.15404 0.43952 0.12789 -0.06325 0.02191  -0.04605 17  CYS B CA  
2061 C  C   . CYS B 21  ? 0.11553 0.44019 0.13378 -0.03701 0.00310  -0.01469 17  CYS B C   
2062 O  O   . CYS B 21  ? 0.11999 0.46247 0.14946 -0.03281 -0.00198 -0.01399 17  CYS B O   
2063 C  CB  . CYS B 21  ? 0.14977 0.46179 0.14390 -0.06900 -0.00456 -0.05168 17  CYS B CB  
2064 S  SG  . CYS B 21  ? 0.18694 0.46697 0.12623 -0.09055 0.01247  -0.01108 17  CYS B SG  
2069 N  N   . HIS B 22  ? 0.13018 0.42068 0.11444 -0.02348 0.01199  -0.03425 18  HIS B N   
2070 C  CA  . HIS B 22  ? 0.10541 0.40710 0.10845 -0.02498 0.00342  -0.02752 18  HIS B CA  
2071 C  C   . HIS B 22  ? 0.11096 0.43095 0.13432 -0.01421 0.00145  -0.05405 18  HIS B C   
2072 O  O   . HIS B 22  ? 0.12000 0.47174 0.12479 -0.01542 0.00168  -0.04113 18  HIS B O   
2073 C  CB  . HIS B 22  ? 0.10604 0.39104 0.10139 0.00650  -0.00118 -0.02883 18  HIS B CB  
2074 C  CG  . HIS B 22  ? 0.10194 0.38387 0.09786 -0.01356 -0.00045 -0.01787 18  HIS B CG  
2075 N  ND1 . HIS B 22  ? 0.10555 0.39389 0.10848 0.01093  -0.00806 -0.01614 18  HIS B ND1 
2076 C  CD2 . HIS B 22  ? 0.10680 0.38362 0.09901 -0.05110 0.00234  -0.01493 18  HIS B CD2 
2077 C  CE1 . HIS B 22  ? 0.13587 0.38815 0.09911 0.00602  0.00550  -0.01639 18  HIS B CE1 
2078 N  NE2 . HIS B 22  ? 0.09764 0.38537 0.10062 -0.00851 0.00068  -0.03026 18  HIS B NE2 
2086 N  N   . THR B 23  ? 0.12223 0.45552 0.16322 0.00644  -0.01413 -0.06326 19  THR B N   
2087 C  CA  . THR B 23  ? 0.12311 0.46686 0.17829 0.01697  -0.00876 -0.07590 19  THR B CA  
2088 C  C   . THR B 23  ? 0.14548 0.46783 0.19329 0.03806  -0.03867 -0.07910 19  THR B C   
2089 O  O   . THR B 23  ? 0.14813 0.45924 0.19890 0.04314  -0.04499 -0.07431 19  THR B O   
2090 C  CB  . THR B 23  ? 0.13065 0.49390 0.19080 0.02758  0.00225  -0.06741 19  THR B CB  
2091 O  OG1 . THR B 23  ? 0.14464 0.52104 0.20965 0.05134  -0.01405 -0.08686 19  THR B OG1 
2092 C  CG2 . THR B 23  ? 0.18344 0.50891 0.23568 0.03793  0.03941  -0.06601 19  THR B CG2 
2100 N  N   . VAL B 24  ? 0.20871 0.44894 0.21983 0.04370  -0.00797 -0.11149 20  VAL B N   
2101 C  CA  . VAL B 24  ? 0.24932 0.45038 0.22926 0.03272  -0.03164 -0.08298 20  VAL B CA  
2102 C  C   . VAL B 24  ? 0.26991 0.45263 0.26505 0.06091  -0.00996 -0.10031 20  VAL B C   
2103 O  O   . VAL B 24  ? 0.21166 0.43848 0.28978 0.09499  -0.04521 -0.05263 20  VAL B O   
2104 C  CB  . VAL B 24  ? 0.23445 0.46711 0.21565 0.03329  -0.04979 -0.06732 20  VAL B CB  
2105 C  CG1 . VAL B 24  ? 0.21884 0.45098 0.21561 0.06267  -0.05122 0.02325  20  VAL B CG1 
2106 C  CG2 . VAL B 24  ? 0.30915 0.48469 0.23792 -0.01378 -0.00828 -0.09090 20  VAL B CG2 
2116 N  N   . GLU B 25  ? 0.28607 0.48337 0.33935 0.07890  0.02228  -0.08463 21  GLU B N   
2117 C  CA  . GLU B 25  ? 0.38190 0.50614 0.37558 0.11615  0.06871  -0.06036 21  GLU B CA  
2118 C  C   . GLU B 25  ? 0.36537 0.53553 0.40037 0.15726  0.07450  -0.04747 21  GLU B C   
2119 O  O   . GLU B 25  ? 0.35350 0.53542 0.37861 0.17720  0.07329  -0.06025 21  GLU B O   
2120 C  CB  . GLU B 25  ? 0.47948 0.51707 0.39410 0.11748  0.11282  -0.08322 21  GLU B CB  
2121 C  CG  . GLU B 25  ? 0.55020 0.54165 0.40249 0.08269  0.11676  -0.09750 21  GLU B CG  
2122 C  CD  . GLU B 25  ? 0.63112 0.57466 0.43793 0.03835  0.20650  -0.12407 21  GLU B CD  
2123 O  OE1 . GLU B 25  ? 0.67590 0.56329 0.43465 0.06291  0.25845  -0.13176 21  GLU B OE1 
2124 O  OE2 . GLU B 25  ? 0.66689 0.59162 0.47440 0.00388  0.19964  -0.15182 21  GLU B OE2 
2131 N  N   . ALA B 26  ? 0.38693 0.57294 0.41227 0.16138  0.04242  -0.00547 22  ALA B N   
2132 C  CA  . ALA B 26  ? 0.39461 0.59804 0.43673 0.19827  -0.03060 0.02003  22  ALA B CA  
2133 C  C   . ALA B 26  ? 0.36480 0.64695 0.47529 0.19119  -0.02724 0.01183  22  ALA B C   
2134 O  O   . ALA B 26  ? 0.41382 0.66854 0.50873 0.18834  -0.00531 -0.00163 22  ALA B O   
2135 C  CB  . ALA B 26  ? 0.42375 0.58535 0.41275 0.22491  -0.10649 0.03540  22  ALA B CB  
2141 N  N   . GLY B 27  ? 0.34480 0.67623 0.47178 0.18418  -0.01968 0.04599  23  GLY B N   
2142 C  CA  . GLY B 27  ? 0.28477 0.68121 0.44774 0.19791  -0.02647 0.06695  23  GLY B CA  
2143 C  C   . GLY B 27  ? 0.24599 0.67477 0.44011 0.17088  0.02800  0.04143  23  GLY B C   
2144 O  O   . GLY B 27  ? 0.28615 0.68919 0.46041 0.15510  0.04644  0.04336  23  GLY B O   
2148 N  N   . GLY B 28  ? 0.22911 0.63131 0.38674 0.15745  0.02852  0.00081  24  GLY B N   
2149 C  CA  . GLY B 28  ? 0.25568 0.60812 0.36875 0.15576  0.06594  -0.04394 24  GLY B CA  
2150 C  C   . GLY B 28  ? 0.17261 0.59483 0.30958 0.08227  -0.01294 -0.07517 24  GLY B C   
2151 O  O   . GLY B 28  ? 0.16465 0.60001 0.35355 0.04558  -0.01798 -0.09635 24  GLY B O   
2155 N  N   . LYS B 29  ? 0.18720 0.61177 0.28986 0.09010  -0.00363 -0.10886 25  LYS B N   
2156 C  CA  . LYS B 29  ? 0.22308 0.61213 0.27118 0.05618  0.05052  -0.11505 25  LYS B CA  
2157 C  C   . LYS B 29  ? 0.15127 0.56810 0.21393 0.00886  -0.00761 -0.11250 25  LYS B C   
2158 O  O   . LYS B 29  ? 0.15305 0.56343 0.22421 0.00681  -0.01343 -0.11528 25  LYS B O   
2159 C  CB  . LYS B 29  ? 0.32677 0.65245 0.29628 0.04722  0.09729  -0.13560 25  LYS B CB  
2160 C  CG  . LYS B 29  ? 0.41444 0.70375 0.36650 0.03459  0.10168  -0.07778 25  LYS B CG  
2161 C  CD  . LYS B 29  ? 0.47273 0.74566 0.40680 0.01571  0.13941  -0.05808 25  LYS B CD  
2162 C  CE  . LYS B 29  ? 0.53854 0.77562 0.42868 -0.01308 0.16993  -0.05344 25  LYS B CE  
2163 N  NZ  . LYS B 29  ? 0.60695 0.79634 0.46045 -0.04134 0.18147  -0.03389 25  LYS B NZ  
2177 N  N   . HIS B 30  ? 0.15279 0.57020 0.19073 -0.02104 0.01010  -0.10829 26  HIS B N   
2178 C  CA  . HIS B 30  ? 0.14401 0.54315 0.16053 -0.01742 -0.00108 -0.07794 26  HIS B CA  
2179 C  C   . HIS B 30  ? 0.16047 0.54291 0.16354 0.01906  0.01436  -0.06501 26  HIS B C   
2180 O  O   . HIS B 30  ? 0.15930 0.59103 0.18608 0.01473  0.01062  -0.07425 26  HIS B O   
2181 C  CB  . HIS B 30  ? 0.15283 0.53408 0.15126 -0.02618 0.01011  -0.06916 26  HIS B CB  
2182 C  CG  . HIS B 30  ? 0.14177 0.51133 0.16192 0.02091  0.01680  -0.03462 26  HIS B CG  
2183 N  ND1 . HIS B 30  ? 0.13400 0.52574 0.17188 0.02280  -0.00347 -0.03478 26  HIS B ND1 
2184 C  CD2 . HIS B 30  ? 0.16679 0.53591 0.17002 0.03406  -0.01358 -0.02824 26  HIS B CD2 
2185 C  CE1 . HIS B 30  ? 0.13760 0.49603 0.18810 0.06243  -0.00568 -0.01849 26  HIS B CE1 
2186 N  NE2 . HIS B 30  ? 0.12805 0.49411 0.19186 0.03319  -0.00537 -0.02831 26  HIS B NE2 
2194 N  N   . LYS B 31  ? 0.14748 0.55149 0.17743 0.03454  0.01107  -0.03239 27  LYS B N   
2195 C  CA  . LYS B 31  ? 0.15706 0.58255 0.16525 -0.01988 0.00372  -0.04568 27  LYS B CA  
2196 C  C   . LYS B 31  ? 0.17112 0.55307 0.14236 -0.01241 -0.01135 -0.00062 27  LYS B C   
2197 O  O   . LYS B 31  ? 0.18941 0.57637 0.18654 -0.05885 -0.03182 -0.03110 27  LYS B O   
2198 C  CB  . LYS B 31  ? 0.19803 0.61292 0.19641 -0.03621 0.04017  -0.05940 27  LYS B CB  
2199 C  CG  . LYS B 31  ? 0.20655 0.64373 0.21868 -0.05817 -0.00735 -0.09717 27  LYS B CG  
2200 C  CD  . LYS B 31  ? 0.30522 0.68368 0.31962 -0.01470 0.02892  -0.10395 27  LYS B CD  
2201 C  CE  . LYS B 31  ? 0.25768 0.70708 0.32464 -0.01954 -0.00041 -0.13915 27  LYS B CE  
2202 N  NZ  . LYS B 31  ? 0.21409 0.71992 0.30878 -0.00280 -0.03012 -0.17539 27  LYS B NZ  
2216 N  N   . VAL B 32  ? 0.15986 0.55272 0.14331 -0.08445 0.00391  -0.01788 28  VAL B N   
2217 C  CA  . VAL B 32  ? 0.18825 0.51677 0.13520 -0.09012 0.00330  -0.00337 28  VAL B CA  
2218 C  C   . VAL B 32  ? 0.15183 0.46902 0.14695 -0.07189 -0.02075 0.00279  28  VAL B C   
2219 O  O   . VAL B 32  ? 0.16807 0.47783 0.15404 -0.09784 -0.02147 0.00651  28  VAL B O   
2220 C  CB  . VAL B 32  ? 0.23718 0.52143 0.14322 -0.07495 0.02810  -0.01075 28  VAL B CB  
2221 C  CG1 . VAL B 32  ? 0.25807 0.53201 0.15759 -0.11566 0.01392  0.01146  28  VAL B CG1 
2222 C  CG2 . VAL B 32  ? 0.32111 0.54418 0.17367 -0.01824 0.08223  0.00807  28  VAL B CG2 
2232 N  N   . GLY B 33  ? 0.13435 0.46308 0.12223 -0.06914 0.00582  -0.02851 29  GLY B N   
2233 C  CA  . GLY B 33  ? 0.12146 0.44966 0.12756 -0.04558 0.00256  -0.03363 29  GLY B CA  
2234 C  C   . GLY B 33  ? 0.10830 0.42025 0.12385 -0.01349 0.00502  -0.04401 29  GLY B C   
2235 O  O   . GLY B 33  ? 0.11892 0.46746 0.13950 -0.00889 -0.00027 -0.04663 29  GLY B O   
2239 N  N   . PRO B 34  ? 0.11450 0.44981 0.12237 -0.02095 -0.00098 -0.01162 30  PRO B N   
2240 C  CA  . PRO B 34  ? 0.12914 0.43790 0.13427 -0.00099 0.02189  -0.01005 30  PRO B CA  
2241 C  C   . PRO B 34  ? 0.12682 0.45034 0.18113 0.01092  0.02555  -0.04490 30  PRO B C   
2242 O  O   . PRO B 34  ? 0.11862 0.46819 0.18708 0.00981  -0.00631 -0.02958 30  PRO B O   
2243 C  CB  . PRO B 34  ? 0.11153 0.43661 0.14536 -0.01651 -0.00615 -0.01033 30  PRO B CB  
2244 C  CG  . PRO B 34  ? 0.13051 0.45573 0.13775 -0.00207 0.01813  -0.03054 30  PRO B CG  
2245 C  CD  . PRO B 34  ? 0.14696 0.43663 0.12559 -0.02818 0.01942  -0.04677 30  PRO B CD  
2253 N  N   . ASN B 35  ? 0.13140 0.48446 0.19295 0.03930  -0.01969 -0.03411 31  ASN B N   
2254 C  CA  . ASN B 35  ? 0.14659 0.46486 0.19256 0.08743  -0.00038 -0.03757 31  ASN B CA  
2255 C  C   . ASN B 35  ? 0.14785 0.46922 0.15067 0.07558  -0.02276 -0.04121 31  ASN B C   
2256 O  O   . ASN B 35  ? 0.14887 0.49766 0.17273 0.05853  -0.02780 -0.04941 31  ASN B O   
2257 C  CB  . ASN B 35  ? 0.17966 0.51134 0.22184 0.07712  0.01093  -0.03800 31  ASN B CB  
2258 C  CG  . ASN B 35  ? 0.19120 0.49613 0.25337 0.13483  -0.02854 -0.03777 31  ASN B CG  
2259 O  OD1 . ASN B 35  ? 0.21441 0.54378 0.27024 0.15211  -0.03194 -0.03279 31  ASN B OD1 
2260 N  ND2 . ASN B 35  ? 0.19354 0.51024 0.26760 0.13355  -0.03391 -0.06232 31  ASN B ND2 
2267 N  N   . LEU B 36  ? 0.12614 0.46025 0.16506 0.04915  -0.00892 -0.05113 32  LEU B N   
2268 C  CA  . LEU B 36  ? 0.12972 0.43934 0.17242 0.06507  -0.01292 -0.05905 32  LEU B CA  
2269 C  C   . LEU B 36  ? 0.17288 0.43201 0.16756 0.07881  -0.02447 -0.04127 32  LEU B C   
2270 O  O   . LEU B 36  ? 0.19626 0.46547 0.13450 0.05655  -0.01041 -0.01727 32  LEU B O   
2271 C  CB  . LEU B 36  ? 0.11637 0.39873 0.15843 0.04752  -0.00513 -0.07601 32  LEU B CB  
2272 C  CG  . LEU B 36  ? 0.11160 0.40478 0.14217 0.04785  -0.00745 -0.01533 32  LEU B CG  
2273 C  CD1 . LEU B 36  ? 0.13557 0.39245 0.14062 0.01594  0.00328  -0.00492 32  LEU B CD1 
2274 C  CD2 . LEU B 36  ? 0.13543 0.43748 0.15775 0.01551  0.03440  -0.00669 32  LEU B CD2 
2286 N  N   . HIS B 37  ? 0.20597 0.45145 0.22399 0.07133  -0.00498 -0.02325 33  HIS B N   
2287 C  CA  . HIS B 37  ? 0.25201 0.43316 0.22441 0.12374  -0.03032 0.01750  33  HIS B CA  
2288 C  C   . HIS B 37  ? 0.26805 0.43169 0.22928 0.11947  -0.03439 -0.00166 33  HIS B C   
2289 O  O   . HIS B 37  ? 0.28508 0.43882 0.25509 0.08884  -0.07302 0.02952  33  HIS B O   
2290 C  CB  . HIS B 37  ? 0.28084 0.47169 0.34042 0.14990  0.03174  0.00587  33  HIS B CB  
2291 C  CG  . HIS B 37  ? 0.41912 0.50597 0.44232 0.15656  0.08360  0.03557  33  HIS B CG  
2292 N  ND1 . HIS B 37  ? 0.50901 0.51494 0.49516 0.18064  0.10703  0.06025  33  HIS B ND1 
2293 C  CD2 . HIS B 37  ? 0.42902 0.51996 0.49442 0.14918  0.11588  0.02480  33  HIS B CD2 
2294 C  CE1 . HIS B 37  ? 0.52354 0.51431 0.50671 0.14609  0.10059  0.06222  33  HIS B CE1 
2295 N  NE2 . HIS B 37  ? 0.48485 0.51907 0.49740 0.13844  0.09978  0.05501  33  HIS B NE2 
2303 N  N   . GLY B 38  ? 0.23920 0.40560 0.21331 0.13095  -0.04525 0.01203  34  GLY B N   
2304 C  CA  . GLY B 38  ? 0.37535 0.40123 0.18876 0.17776  -0.05295 -0.02052 34  GLY B CA  
2305 C  C   . GLY B 38  ? 0.44572 0.39547 0.16138 0.16507  -0.01704 0.00554  34  GLY B C   
2306 O  O   . GLY B 38  ? 0.51380 0.43405 0.15979 0.15221  -0.00091 0.01965  34  GLY B O   
2310 N  N   . LEU B 39  ? 0.39269 0.39047 0.14828 0.14407  -0.02957 0.02754  35  LEU B N   
2311 C  CA  . LEU B 39  ? 0.37865 0.40120 0.14754 0.14303  0.00440  0.05144  35  LEU B CA  
2312 C  C   . LEU B 39  ? 0.42756 0.39369 0.14262 0.11219  0.02034  0.03519  35  LEU B C   
2313 O  O   . LEU B 39  ? 0.44880 0.36429 0.13529 0.09034  0.03873  0.03316  35  LEU B O   
2314 C  CB  . LEU B 39  ? 0.34336 0.41301 0.16135 0.15689  0.04682  0.05827  35  LEU B CB  
2315 C  CG  . LEU B 39  ? 0.28861 0.40629 0.14515 0.14286  0.05146  0.04693  35  LEU B CG  
2316 C  CD1 . LEU B 39  ? 0.37686 0.39316 0.15598 0.12108  0.06070  -0.02495 35  LEU B CD1 
2317 C  CD2 . LEU B 39  ? 0.31642 0.40851 0.16349 0.13090  0.07544  0.06578  35  LEU B CD2 
2329 N  N   . PHE B 40  ? 0.35477 0.37894 0.12340 0.09474  0.00894  0.04165  36  PHE B N   
2330 C  CA  . PHE B 40  ? 0.36875 0.37799 0.13028 0.13096  -0.00986 0.02069  36  PHE B CA  
2331 C  C   . PHE B 40  ? 0.34230 0.37209 0.13326 0.13612  -0.01899 0.02451  36  PHE B C   
2332 O  O   . PHE B 40  ? 0.40374 0.40603 0.16053 0.18286  0.00806  0.04249  36  PHE B O   
2333 C  CB  . PHE B 40  ? 0.36807 0.37970 0.12476 0.09969  -0.01986 0.01259  36  PHE B CB  
2334 C  CG  . PHE B 40  ? 0.34866 0.40329 0.14560 0.06763  -0.03083 -0.00416 36  PHE B CG  
2335 C  CD1 . PHE B 40  ? 0.38262 0.40974 0.14540 0.08645  -0.03344 0.00850  36  PHE B CD1 
2336 C  CD2 . PHE B 40  ? 0.32971 0.41501 0.19018 0.06550  -0.02538 0.01057  36  PHE B CD2 
2337 C  CE1 . PHE B 40  ? 0.38227 0.40968 0.14750 0.08465  -0.02949 -0.02235 36  PHE B CE1 
2338 C  CE2 . PHE B 40  ? 0.33232 0.42644 0.21912 0.06451  0.00183  -0.03568 36  PHE B CE2 
2339 C  CZ  . PHE B 40  ? 0.38314 0.40951 0.19645 0.09083  0.00675  -0.01863 36  PHE B CZ  
2349 N  N   A GLY B 41  ? 0.23060 0.36282 0.11754 0.06901  -0.02574 -0.02758 37  GLY B N   
2350 N  N   B GLY B 41  ? 0.31386 0.39549 0.14926 0.13028  0.01865  0.02017  37  GLY B N   
2351 C  CA  A GLY B 41  ? 0.17759 0.32565 0.10620 0.07062  -0.03746 -0.01726 37  GLY B CA  
2352 C  CA  B GLY B 41  ? 0.32457 0.40316 0.17329 0.12867  0.04187  0.04700  37  GLY B CA  
2353 C  C   A GLY B 41  ? 0.17579 0.34202 0.11876 0.09007  0.00455  0.00518  37  GLY B C   
2354 C  C   B GLY B 41  ? 0.32700 0.40726 0.23593 0.11353  0.06445  0.06900  37  GLY B C   
2355 O  O   A GLY B 41  ? 0.15503 0.32453 0.13895 0.05889  -0.01527 0.04072  37  GLY B O   
2356 O  O   B GLY B 41  ? 0.34807 0.40368 0.27607 0.13254  0.07693  0.10168  37  GLY B O   
2363 N  N   A ARG B 42  ? 0.14442 0.33902 0.11787 0.09287  0.00293  0.04377  38  ARG B N   
2364 N  N   B ARG B 42  ? 0.32364 0.40986 0.26735 0.09072  0.05282  0.05497  38  ARG B N   
2365 C  CA  A ARG B 42  ? 0.15468 0.34854 0.19639 0.04721  0.07260  0.05678  38  ARG B CA  
2366 C  CA  B ARG B 42  ? 0.31773 0.42400 0.25316 0.06513  0.04814  0.03418  38  ARG B CA  
2367 C  C   A ARG B 42  ? 0.10767 0.35247 0.14363 0.04431  0.00681  0.01784  38  ARG B C   
2368 C  C   B ARG B 42  ? 0.24431 0.40885 0.19475 0.06675  0.02422  0.02037  38  ARG B C   
2369 O  O   A ARG B 42  ? 0.10276 0.33057 0.11028 0.04708  -0.01142 0.01546  38  ARG B O   
2370 O  O   B ARG B 42  ? 0.27227 0.41163 0.17939 0.08643  0.05130  0.02348  38  ARG B O   
2371 C  CB  A ARG B 42  ? 0.24611 0.36363 0.29917 0.04419  0.13464  0.05728  38  ARG B CB  
2372 C  CB  B ARG B 42  ? 0.39720 0.43460 0.29008 0.03474  0.09443  0.01660  38  ARG B CB  
2373 C  CG  A ARG B 42  ? 0.27704 0.37277 0.34494 0.04294  0.12809  0.03808  38  ARG B CG  
2374 C  CG  B ARG B 42  ? 0.45328 0.43741 0.30807 0.03040  0.14900  0.01734  38  ARG B CG  
2375 C  CD  A ARG B 42  ? 0.31198 0.36522 0.33419 0.03091  0.14094  0.01515  38  ARG B CD  
2376 C  CD  B ARG B 42  ? 0.49170 0.43935 0.30463 0.03755  0.17596  0.01238  38  ARG B CD  
2377 N  NE  A ARG B 42  ? 0.33292 0.38461 0.32226 0.04462  0.16580  -0.00591 38  ARG B NE  
2378 N  NE  B ARG B 42  ? 0.48350 0.44439 0.27110 0.04139  0.17817  0.00180  38  ARG B NE  
2379 C  CZ  A ARG B 42  ? 0.29393 0.40305 0.33871 0.03211  0.12085  0.02704  38  ARG B CZ  
2380 C  CZ  B ARG B 42  ? 0.40854 0.43886 0.23306 0.02233  0.15545  0.00906  38  ARG B CZ  
2381 N  NH1 A ARG B 42  ? 0.33100 0.42479 0.37521 0.04239  0.14799  0.04477  38  ARG B NH1 
2382 N  NH1 B ARG B 42  ? 0.35451 0.43040 0.19398 0.03630  0.10983  -0.00500 38  ARG B NH1 
2383 N  NH2 A ARG B 42  ? 0.24806 0.40497 0.30960 -0.04235 0.12728  0.02016  38  ARG B NH2 
2384 N  NH2 B ARG B 42  ? 0.42488 0.45021 0.23546 0.01872  0.17141  0.02457  38  ARG B NH2 
2408 N  N   . LYS B 43  ? 0.16965 0.39563 0.13415 0.07257  -0.01725 0.03113  39  LYS B N   
2409 C  CA  . LYS B 43  ? 0.14365 0.38653 0.11764 0.04332  -0.02449 0.01406  39  LYS B CA  
2410 C  C   A LYS B 43  ? 0.11246 0.39316 0.12099 0.00585  -0.01662 -0.02750 39  LYS B C   
2411 C  C   B LYS B 43  ? 0.14627 0.39160 0.11657 0.03682  -0.00666 -0.00629 39  LYS B C   
2412 O  O   A LYS B 43  ? 0.12302 0.42116 0.12594 0.02633  -0.01577 -0.04838 39  LYS B O   
2413 O  O   B LYS B 43  ? 0.19347 0.41239 0.14195 0.04535  0.03485  -0.01693 39  LYS B O   
2414 C  CB  . LYS B 43  ? 0.12566 0.38583 0.12806 0.03076  0.00845  0.00399  39  LYS B CB  
2415 C  CG  . LYS B 43  ? 0.15240 0.37116 0.16804 -0.00375 -0.00234 -0.01496 39  LYS B CG  
2416 C  CD  . LYS B 43  ? 0.18883 0.33303 0.15918 0.01433  -0.04083 0.01127  39  LYS B CD  
2417 C  CE  . LYS B 43  ? 0.23402 0.32779 0.17330 0.01141  -0.02127 0.00653  39  LYS B CE  
2418 N  NZ  . LYS B 43  ? 0.19147 0.32410 0.14536 -0.00266 -0.06492 -0.00166 39  LYS B NZ  
2434 N  N   A THR B 44  ? 0.11464 0.39675 0.12432 0.00892  -0.01906 -0.02116 40  THR B N   
2435 N  N   B THR B 44  ? 0.13807 0.37734 0.10941 0.03188  -0.00450 -0.01635 40  THR B N   
2436 C  CA  A THR B 44  ? 0.12150 0.39254 0.10925 0.02106  -0.01545 -0.01454 40  THR B CA  
2437 C  CA  B THR B 44  ? 0.13883 0.35610 0.10043 0.03405  0.00470  -0.01654 40  THR B CA  
2438 C  C   A THR B 44  ? 0.10540 0.38440 0.10353 0.01566  -0.00796 -0.00981 40  THR B C   
2439 C  C   B THR B 44  ? 0.15614 0.33128 0.10427 0.05523  0.00395  -0.00935 40  THR B C   
2440 O  O   A THR B 44  ? 0.10661 0.41932 0.10614 0.00583  -0.00148 -0.00311 40  THR B O   
2441 O  O   B THR B 44  ? 0.17693 0.31430 0.12087 0.05606  -0.00407 0.01894  40  THR B O   
2442 C  CB  A THR B 44  ? 0.13707 0.38761 0.13594 0.01325  -0.03870 -0.02205 40  THR B CB  
2443 C  CB  B THR B 44  ? 0.12725 0.34346 0.09844 0.01678  0.00713  -0.02105 40  THR B CB  
2444 O  OG1 A THR B 44  ? 0.14605 0.44244 0.13783 -0.00579 -0.02453 -0.04608 40  THR B OG1 
2445 O  OG1 B THR B 44  ? 0.14909 0.33033 0.10742 -0.00424 0.03877  -0.02131 40  THR B OG1 
2446 C  CG2 A THR B 44  ? 0.12127 0.37803 0.15695 0.01482  -0.03993 -0.02173 40  THR B CG2 
2447 C  CG2 B THR B 44  ? 0.10796 0.33761 0.09819 0.01474  0.01574  -0.01521 40  THR B CG2 
2462 N  N   A GLY B 45  ? 0.14911 0.37367 0.09464 -0.00549 -0.00803 -0.00186 41  GLY B N   
2463 N  N   B GLY B 45  ? 0.16239 0.30638 0.10867 0.07523  0.00673  -0.01604 41  GLY B N   
2464 C  CA  A GLY B 45  ? 0.10776 0.39053 0.13689 0.01857  0.00346  0.00850  41  GLY B CA  
2465 C  CA  B GLY B 45  ? 0.14345 0.28678 0.08612 0.06667  0.01095  -0.01329 41  GLY B CA  
2466 C  C   A GLY B 45  ? 0.11872 0.38272 0.12884 0.02589  -0.02146 -0.01082 41  GLY B C   
2467 C  C   B GLY B 45  ? 0.15645 0.26742 0.08992 0.05236  0.03336  -0.00673 41  GLY B C   
2468 O  O   A GLY B 45  ? 0.12158 0.39949 0.16086 0.01776  -0.02934 -0.00587 41  GLY B O   
2469 O  O   B GLY B 45  ? 0.17967 0.26202 0.08812 0.04899  0.04003  0.00164  41  GLY B O   
2476 N  N   A GLN B 46  ? 0.10953 0.35686 0.12012 0.00742  -0.02485 -0.01089 42  GLN B N   
2477 N  N   B GLN B 46  ? 0.14968 0.28122 0.09765 0.05670  0.00763  0.00651  42  GLN B N   
2478 C  CA  A GLN B 46  ? 0.13833 0.38560 0.12948 0.03789  -0.03346 0.00047  42  GLN B CA  
2479 C  CA  B GLN B 46  ? 0.18751 0.28514 0.11471 0.07097  0.00906  0.01205  42  GLN B CA  
2480 C  C   A GLN B 46  ? 0.11232 0.40321 0.12528 0.03149  -0.01389 -0.00802 42  GLN B C   
2481 C  C   B GLN B 46  ? 0.15060 0.28931 0.13713 0.10442  -0.00967 0.01009  42  GLN B C   
2482 O  O   A GLN B 46  ? 0.15475 0.47479 0.14593 0.06620  -0.02454 -0.01702 42  GLN B O   
2483 O  O   B GLN B 46  ? 0.24614 0.30657 0.17160 0.09500  0.01652  0.00007  42  GLN B O   
2484 C  CB  A GLN B 46  ? 0.15124 0.35700 0.13689 0.04908  0.00970  0.02058  42  GLN B CB  
2485 C  CB  B GLN B 46  ? 0.24430 0.30012 0.14619 0.07221  0.04832  0.01521  42  GLN B CB  
2486 C  CG  A GLN B 46  ? 0.12622 0.33650 0.12695 0.03525  -0.02369 0.01772  42  GLN B CG  
2487 C  CG  B GLN B 46  ? 0.28386 0.31009 0.15569 0.08683  0.03512  0.02393  42  GLN B CG  
2488 C  CD  A GLN B 46  ? 0.14665 0.32361 0.11954 0.06477  -0.03321 0.01472  42  GLN B CD  
2489 C  CD  B GLN B 46  ? 0.32923 0.32971 0.16513 0.08871  0.00204  0.01591  42  GLN B CD  
2490 O  OE1 A GLN B 46  ? 0.15441 0.34741 0.15088 0.08257  -0.04363 -0.00274 42  GLN B OE1 
2491 O  OE1 B GLN B 46  ? 0.35421 0.33373 0.19565 0.10424  0.01630  0.00770  42  GLN B OE1 
2492 N  NE2 A GLN B 46  ? 0.18964 0.33081 0.17353 0.05879  -0.05308 0.03739  42  GLN B NE2 
2493 N  NE2 B GLN B 46  ? 0.34323 0.33433 0.17176 0.08338  -0.02372 0.01792  42  GLN B NE2 
2510 N  N   A ALA B 47  ? 0.12093 0.41322 0.16858 0.04336  -0.01649 0.00052  43  ALA B N   
2511 N  N   B ALA B 47  ? 0.14585 0.31496 0.13171 0.06462  0.00959  -0.01947 43  ALA B N   
2512 C  CA  A ALA B 47  ? 0.11425 0.41927 0.18545 0.04755  -0.00562 -0.01443 43  ALA B CA  
2513 C  CA  B ALA B 47  ? 0.10129 0.33744 0.10114 0.03923  0.00552  -0.02767 43  ALA B CA  
2514 C  C   A ALA B 47  ? 0.11896 0.43381 0.19958 -0.00910 0.03051  -0.00775 43  ALA B C   
2515 C  C   B ALA B 47  ? 0.09912 0.37203 0.09846 0.03361  -0.00400 -0.03385 43  ALA B C   
2516 O  O   A ALA B 47  ? 0.11791 0.47011 0.20480 0.00613  0.00340  0.01177  43  ALA B O   
2517 O  O   B ALA B 47  ? 0.10547 0.37410 0.10600 0.02132  -0.00885 -0.04277 43  ALA B O   
2518 C  CB  A ALA B 47  ? 0.16090 0.43753 0.18924 0.03090  -0.06178 -0.00629 43  ALA B CB  
2519 C  CB  B ALA B 47  ? 0.08608 0.30876 0.08682 0.01010  -0.00750 -0.02776 43  ALA B CB  
2530 N  N   A ALA B 48  ? 0.12166 0.48372 0.22019 0.01429  0.00045  -0.00500 44  ALA B N   
2531 N  N   B ALA B 48  ? 0.11641 0.42548 0.12299 0.02972  0.00094  -0.03607 44  ALA B N   
2532 C  CA  A ALA B 48  ? 0.12773 0.50404 0.20770 0.02062  -0.00505 -0.00666 44  ALA B CA  
2533 C  CA  B ALA B 48  ? 0.12149 0.46172 0.13637 0.02375  0.00597  -0.02738 44  ALA B CA  
2534 C  C   A ALA B 48  ? 0.13433 0.49966 0.20743 0.02097  0.02257  -0.02810 44  ALA B C   
2535 C  C   B ALA B 48  ? 0.12669 0.49272 0.15710 0.01862  0.00646  -0.02494 44  ALA B C   
2536 O  O   A ALA B 48  ? 0.13828 0.52088 0.19087 0.04387  -0.00035 -0.04460 44  ALA B O   
2537 O  O   B ALA B 48  ? 0.13298 0.50263 0.15766 0.02915  0.00787  -0.02944 44  ALA B O   
2538 C  CB  A ALA B 48  ? 0.18411 0.51980 0.23559 0.00502  0.01739  -0.00705 44  ALA B CB  
2539 C  CB  B ALA B 48  ? 0.12567 0.46669 0.13953 0.01824  0.01103  -0.02431 44  ALA B CB  
2550 N  N   . GLY B 49  ? 0.13996 0.51994 0.16117 0.00164  -0.01737 -0.01428 45  GLY B N   
2551 C  CA  . GLY B 49  ? 0.14595 0.51842 0.19238 -0.00188 0.03105  -0.02617 45  GLY B CA  
2552 C  C   . GLY B 49  ? 0.13874 0.50988 0.15875 -0.03842 0.01449  -0.00621 45  GLY B C   
2553 O  O   . GLY B 49  ? 0.14354 0.52880 0.20182 -0.01427 0.02731  -0.00173 45  GLY B O   
2557 N  N   . PHE B 50  ? 0.12989 0.49194 0.17329 0.01339  0.01566  -0.02627 46  PHE B N   
2558 C  CA  . PHE B 50  ? 0.12079 0.47836 0.18875 -0.00540 -0.00175 -0.03464 46  PHE B CA  
2559 C  C   . PHE B 50  ? 0.11392 0.45313 0.19358 0.00033  0.00339  -0.02260 46  PHE B C   
2560 O  O   . PHE B 50  ? 0.13953 0.52173 0.21462 -0.00322 0.02237  -0.05641 46  PHE B O   
2561 C  CB  . PHE B 50  ? 0.12791 0.48068 0.14759 -0.00770 0.01262  -0.03964 46  PHE B CB  
2562 C  CG  . PHE B 50  ? 0.12523 0.46437 0.15086 -0.03592 -0.00055 -0.05746 46  PHE B CG  
2563 C  CD1 . PHE B 50  ? 0.16656 0.47354 0.13133 -0.03161 0.00751  -0.05286 46  PHE B CD1 
2564 C  CD2 . PHE B 50  ? 0.12903 0.44682 0.12891 -0.03206 -0.00577 -0.04549 46  PHE B CD2 
2565 C  CE1 . PHE B 50  ? 0.13760 0.46954 0.13617 -0.04556 0.00768  -0.06555 46  PHE B CE1 
2566 C  CE2 . PHE B 50  ? 0.12592 0.43718 0.13302 -0.05339 -0.00032 -0.04417 46  PHE B CE2 
2567 C  CZ  . PHE B 50  ? 0.12996 0.44147 0.14486 -0.06444 0.00893  -0.06134 46  PHE B CZ  
2577 N  N   . ALA B 51  ? 0.15519 0.50913 0.20308 -0.02610 -0.00501 -0.02934 47  ALA B N   
2578 C  CA  . ALA B 51  ? 0.14307 0.51179 0.22146 -0.06309 0.01385  -0.03971 47  ALA B CA  
2579 C  C   . ALA B 51  ? 0.13573 0.50350 0.16388 -0.04600 0.01154  -0.04714 47  ALA B C   
2580 O  O   . ALA B 51  ? 0.18741 0.52638 0.17658 -0.07044 0.00953  -0.03763 47  ALA B O   
2581 C  CB  . ALA B 51  ? 0.16136 0.51886 0.25590 -0.09388 0.02106  -0.04066 47  ALA B CB  
2587 N  N   . TYR B 52  ? 0.13391 0.51298 0.16323 -0.03078 0.00272  -0.05872 48  TYR B N   
2588 C  CA  . TYR B 52  ? 0.13152 0.48729 0.14565 -0.03810 0.01004  -0.06976 48  TYR B CA  
2589 C  C   . TYR B 52  ? 0.14087 0.48709 0.14211 -0.04010 -0.00532 -0.05107 48  TYR B C   
2590 O  O   . TYR B 52  ? 0.16773 0.50928 0.19485 -0.05709 -0.02574 -0.06878 48  TYR B O   
2591 C  CB  . TYR B 52  ? 0.18611 0.46817 0.14259 -0.03533 -0.02387 -0.05473 48  TYR B CB  
2592 C  CG  . TYR B 52  ? 0.13150 0.44596 0.12925 -0.02241 -0.00904 -0.04702 48  TYR B CG  
2593 C  CD1 . TYR B 52  ? 0.14268 0.43105 0.11091 0.01755  -0.00213 -0.02719 48  TYR B CD1 
2594 C  CD2 . TYR B 52  ? 0.15326 0.44227 0.12128 -0.02493 -0.01835 -0.01451 48  TYR B CD2 
2595 C  CE1 . TYR B 52  ? 0.15012 0.43288 0.13912 -0.02878 0.03239  -0.04518 48  TYR B CE1 
2596 C  CE2 . TYR B 52  ? 0.12782 0.47002 0.12070 -0.01300 0.00548  -0.01006 48  TYR B CE2 
2597 C  CZ  . TYR B 52  ? 0.14870 0.47057 0.13097 -0.00424 -0.00900 -0.05322 48  TYR B CZ  
2598 O  OH  . TYR B 52  ? 0.12235 0.47977 0.14489 0.01987  -0.00519 -0.02066 48  TYR B OH  
2608 N  N   . THR B 53  ? 0.13440 0.47449 0.15455 -0.06023 0.00897  -0.06047 49  THR B N   
2609 C  CA  . THR B 53  ? 0.19429 0.48004 0.13759 -0.06084 -0.02322 -0.02490 49  THR B CA  
2610 C  C   . THR B 53  ? 0.18323 0.45814 0.14764 -0.06581 -0.03407 -0.02104 49  THR B C   
2611 O  O   . THR B 53  ? 0.17812 0.43454 0.12057 -0.04100 -0.01125 -0.01839 49  THR B O   
2612 C  CB  . THR B 53  ? 0.15958 0.49900 0.15585 -0.09216 -0.00336 -0.02215 49  THR B CB  
2613 O  OG1 . THR B 53  ? 0.16982 0.49271 0.14036 -0.06548 0.00475  -0.06093 49  THR B OG1 
2614 C  CG2 . THR B 53  ? 0.24332 0.51932 0.16881 -0.11025 0.01700  -0.00992 49  THR B CG2 
2622 N  N   . ASP B 54  ? 0.16125 0.45685 0.16024 -0.07141 -0.00990 -0.05924 50  ASP B N   
2623 C  CA  . ASP B 54  ? 0.16542 0.44118 0.15527 -0.02321 0.01251  -0.06543 50  ASP B CA  
2624 C  C   . ASP B 54  ? 0.16659 0.41391 0.12765 -0.01484 -0.03039 -0.04095 50  ASP B C   
2625 O  O   . ASP B 54  ? 0.18695 0.42564 0.13736 -0.05403 -0.03681 -0.02754 50  ASP B O   
2626 C  CB  . ASP B 54  ? 0.20662 0.47162 0.18806 -0.06983 -0.00920 -0.08710 50  ASP B CB  
2627 C  CG  . ASP B 54  ? 0.29561 0.51154 0.22872 -0.11265 0.01611  -0.06562 50  ASP B CG  
2628 O  OD1 . ASP B 54  ? 0.27623 0.55384 0.20582 -0.10738 -0.02869 -0.09618 50  ASP B OD1 
2629 O  OD2 . ASP B 54  ? 0.34845 0.54430 0.27121 -0.13605 0.01476  -0.03032 50  ASP B OD2 
2634 N  N   . ALA B 55  ? 0.19970 0.43676 0.15185 -0.02638 -0.02282 -0.04359 51  ALA B N   
2635 C  CA  . ALA B 55  ? 0.17530 0.41982 0.16117 0.00420  -0.03958 -0.03574 51  ALA B CA  
2636 C  C   . ALA B 55  ? 0.16679 0.40565 0.11775 -0.00028 0.00423  -0.05080 51  ALA B C   
2637 O  O   . ALA B 55  ? 0.17255 0.42738 0.13902 -0.00884 -0.01137 -0.04960 51  ALA B O   
2638 C  CB  . ALA B 55  ? 0.23889 0.42585 0.17572 -0.03186 0.00847  -0.02422 51  ALA B CB  
2644 N  N   . ASN B 56  ? 0.13682 0.42042 0.13900 -0.03735 -0.01554 -0.05494 52  ASN B N   
2645 C  CA  . ASN B 56  ? 0.12704 0.40804 0.13298 -0.00020 -0.01974 -0.05658 52  ASN B CA  
2646 C  C   . ASN B 56  ? 0.14001 0.39875 0.12718 0.00157  -0.02645 -0.04726 52  ASN B C   
2647 O  O   . ASN B 56  ? 0.14985 0.41316 0.14098 0.00765  -0.00319 -0.06288 52  ASN B O   
2648 C  CB  . ASN B 56  ? 0.16080 0.42583 0.13674 -0.00591 0.00577  -0.05426 52  ASN B CB  
2649 C  CG  . ASN B 56  ? 0.11229 0.43175 0.11991 -0.01183 0.00051  -0.05235 52  ASN B CG  
2650 O  OD1 . ASN B 56  ? 0.12800 0.46914 0.14424 -0.01697 0.00877  -0.07806 52  ASN B OD1 
2651 N  ND2 . ASN B 56  ? 0.15923 0.41937 0.13555 -0.02477 -0.02353 -0.05900 52  ASN B ND2 
2658 N  N   . LYS B 57  ? 0.14834 0.39037 0.12778 0.00881  -0.02991 -0.05497 53  LYS B N   
2659 C  CA  . LYS B 57  ? 0.13440 0.40640 0.12999 0.02701  -0.02862 -0.03266 53  LYS B CA  
2660 C  C   . LYS B 57  ? 0.18122 0.41598 0.13313 0.01114  -0.01703 -0.04321 53  LYS B C   
2661 O  O   . LYS B 57  ? 0.21138 0.43259 0.14175 0.02802  -0.02301 -0.04058 53  LYS B O   
2662 C  CB  . LYS B 57  ? 0.17045 0.43899 0.13236 0.03695  -0.03097 -0.04775 53  LYS B CB  
2663 C  CG  . LYS B 57  ? 0.16340 0.49090 0.16733 0.05152  -0.00040 -0.07074 53  LYS B CG  
2664 C  CD  . LYS B 57  ? 0.14097 0.54211 0.20653 0.02126  -0.01660 -0.03046 53  LYS B CD  
2665 C  CE  . LYS B 57  ? 0.28181 0.58920 0.24294 -0.05249 -0.06843 -0.01829 53  LYS B CE  
2666 N  NZ  . LYS B 57  ? 0.25654 0.58830 0.22021 -0.11983 -0.01667 -0.06729 53  LYS B NZ  
2680 N  N   . ALA B 58  ? 0.16205 0.39806 0.12448 -0.01086 -0.00715 -0.04345 54  ALA B N   
2681 C  CA  . ALA B 58  ? 0.15535 0.38858 0.12225 0.01180  0.02528  -0.02921 54  ALA B CA  
2682 C  C   . ALA B 58  ? 0.16230 0.37465 0.12726 0.03215  0.00245  -0.02934 54  ALA B C   
2683 O  O   . ALA B 58  ? 0.16198 0.38452 0.11398 0.02017  -0.00725 -0.04091 54  ALA B O   
2684 C  CB  . ALA B 58  ? 0.22233 0.40162 0.17910 -0.02462 0.01434  -0.05528 54  ALA B CB  
2690 N  N   . LYS B 59  ? 0.14319 0.38932 0.11442 0.02687  -0.00831 -0.04348 55  LYS B N   
2691 C  CA  . LYS B 59  ? 0.14003 0.38336 0.12280 0.04512  -0.02388 -0.01249 55  LYS B CA  
2692 C  C   . LYS B 59  ? 0.14053 0.37539 0.11302 0.02043  -0.02918 -0.00449 55  LYS B C   
2693 O  O   . LYS B 59  ? 0.17351 0.38112 0.10903 0.00562  0.01244  -0.01681 55  LYS B O   
2694 C  CB  . LYS B 59  ? 0.14879 0.35640 0.09114 0.02204  -0.00661 0.00510  55  LYS B CB  
2695 C  CG  . LYS B 59  ? 0.10706 0.36258 0.14039 0.00341  -0.00154 -0.03754 55  LYS B CG  
2696 C  CD  . LYS B 59  ? 0.13257 0.38158 0.12638 0.00454  0.01770  -0.01379 55  LYS B CD  
2697 C  CE  . LYS B 59  ? 0.16255 0.39419 0.13895 0.03320  0.01646  0.00136  55  LYS B CE  
2698 N  NZ  . LYS B 59  ? 0.13658 0.41432 0.17568 0.02587  0.00583  -0.01535 55  LYS B NZ  
2712 N  N   . GLY B 60  ? 0.13788 0.37628 0.11894 0.02658  -0.00992 -0.02426 56  GLY B N   
2713 C  CA  . GLY B 60  ? 0.14678 0.40080 0.12320 0.01825  -0.01090 -0.01825 56  GLY B CA  
2714 C  C   . GLY B 60  ? 0.14218 0.41334 0.10517 0.02194  0.00725  0.00138  56  GLY B C   
2715 O  O   . GLY B 60  ? 0.14386 0.44008 0.11322 0.02514  -0.00733 0.01176  56  GLY B O   
2719 N  N   . ILE B 61  ? 0.11941 0.40608 0.10361 0.02626  0.00390  -0.00646 57  ILE B N   
2720 C  CA  . ILE B 61  ? 0.12892 0.36878 0.10684 0.04173  -0.01852 0.00419  57  ILE B CA  
2721 C  C   . ILE B 61  ? 0.11888 0.37028 0.09713 0.04188  -0.00382 0.01419  57  ILE B C   
2722 O  O   . ILE B 61  ? 0.10212 0.36667 0.11104 0.03084  -0.00159 -0.00982 57  ILE B O   
2723 C  CB  . ILE B 61  ? 0.13218 0.37524 0.09947 0.05234  0.00990  0.01185  57  ILE B CB  
2724 C  CG1 . ILE B 61  ? 0.12935 0.35972 0.09904 0.01072  -0.01820 0.00682  57  ILE B CG1 
2725 C  CG2 . ILE B 61  ? 0.12550 0.40271 0.10552 0.07455  -0.00115 -0.00541 57  ILE B CG2 
2726 C  CD1 . ILE B 61  ? 0.15619 0.36081 0.09216 0.00288  0.00859  0.01367  57  ILE B CD1 
2738 N  N   . THR B 62  ? 0.14274 0.37128 0.09881 0.05962  0.00414  0.00525  58  THR B N   
2739 C  CA  . THR B 62  ? 0.13927 0.37125 0.10125 0.08600  -0.00233 0.00487  58  THR B CA  
2740 C  C   . THR B 62  ? 0.10722 0.35268 0.10162 0.05990  -0.00165 0.01054  58  THR B C   
2741 O  O   . THR B 62  ? 0.11456 0.34520 0.11217 0.04132  0.01298  0.02566  58  THR B O   
2742 C  CB  . THR B 62  ? 0.20850 0.36638 0.10926 0.07538  -0.02611 0.01090  58  THR B CB  
2743 O  OG1 . THR B 62  ? 0.21204 0.38478 0.12408 0.08739  0.01201  0.02818  58  THR B OG1 
2744 C  CG2 . THR B 62  ? 0.23543 0.37160 0.12587 0.07489  0.00247  0.04511  58  THR B CG2 
2752 N  N   . TRP B 63  ? 0.11536 0.34263 0.09784 0.05121  -0.00080 -0.00661 59  TRP B N   
2753 C  CA  . TRP B 63  ? 0.12910 0.33257 0.10762 0.03845  0.00729  0.01486  59  TRP B CA  
2754 C  C   . TRP B 63  ? 0.18107 0.32443 0.10063 0.02817  0.02899  0.00531  59  TRP B C   
2755 O  O   . TRP B 63  ? 0.18282 0.33736 0.13647 0.04247  0.01030  0.02346  59  TRP B O   
2756 C  CB  . TRP B 63  ? 0.11996 0.33651 0.09011 0.03924  0.00378  0.01483  59  TRP B CB  
2757 C  CG  . TRP B 63  ? 0.12231 0.34817 0.10451 0.04609  -0.00693 0.01066  59  TRP B CG  
2758 C  CD1 . TRP B 63  ? 0.12731 0.35178 0.09803 0.06102  -0.01163 -0.00080 59  TRP B CD1 
2759 C  CD2 . TRP B 63  ? 0.08985 0.33506 0.08645 0.02344  -0.00119 0.01101  59  TRP B CD2 
2760 N  NE1 . TRP B 63  ? 0.10071 0.36915 0.09439 0.03817  0.00051  0.00945  59  TRP B NE1 
2761 C  CE2 . TRP B 63  ? 0.10081 0.35443 0.09057 0.02355  0.00324  0.01463  59  TRP B CE2 
2762 C  CE3 . TRP B 63  ? 0.13265 0.32176 0.08594 0.00657  -0.01643 0.00547  59  TRP B CE3 
2763 C  CZ2 . TRP B 63  ? 0.11511 0.33983 0.08881 -0.00801 -0.01024 0.00957  59  TRP B CZ2 
2764 C  CZ3 . TRP B 63  ? 0.11486 0.31002 0.10133 0.01254  -0.02840 0.01050  59  TRP B CZ3 
2765 C  CH2 . TRP B 63  ? 0.12280 0.33019 0.10569 -0.00664 -0.02785 0.01145  59  TRP B CH2 
2776 N  N   . ASN B 64  ? 0.14941 0.32234 0.11939 0.01784  0.00035  0.00780  60  ASN B N   
2777 C  CA  . ASN B 64  ? 0.16695 0.32363 0.14549 0.01601  -0.01606 0.02615  60  ASN B CA  
2778 C  C   . ASN B 64  ? 0.14588 0.35367 0.14227 0.00094  0.01977  0.01381  60  ASN B C   
2779 O  O   . ASN B 64  ? 0.16441 0.33053 0.13326 0.01383  0.01791  0.03839  60  ASN B O   
2780 C  CB  . ASN B 64  ? 0.24025 0.35076 0.14465 0.00067  -0.01020 0.01977  60  ASN B CB  
2781 C  CG  . ASN B 64  ? 0.20916 0.39326 0.11485 0.02396  0.01817  0.00758  60  ASN B CG  
2782 O  OD1 . ASN B 64  ? 0.17009 0.39194 0.13264 0.00932  -0.00915 0.03000  60  ASN B OD1 
2783 N  ND2 . ASN B 64  ? 0.28815 0.44832 0.14930 0.06941  0.00613  -0.01128 60  ASN B ND2 
2790 N  N   A GLU B 65  ? 0.18357 0.35374 0.12267 -0.02905 0.04169  0.02981  61  GLU B N   
2791 N  N   B GLU B 65  ? 0.17227 0.34772 0.12780 -0.02328 -0.00325 0.03687  61  GLU B N   
2792 C  CA  A GLU B 65  ? 0.17006 0.36824 0.13154 -0.04383 0.03481  0.01034  61  GLU B CA  
2793 C  CA  B GLU B 65  ? 0.15968 0.35667 0.13581 -0.03777 -0.05398 0.02748  61  GLU B CA  
2794 C  C   A GLU B 65  ? 0.16839 0.34224 0.15617 -0.03870 0.06543  0.02816  61  GLU B C   
2795 C  C   B GLU B 65  ? 0.16865 0.36819 0.13315 -0.01498 -0.00004 0.04733  61  GLU B C   
2796 O  O   A GLU B 65  ? 0.14362 0.34708 0.18920 -0.05777 0.06167  0.00392  61  GLU B O   
2797 O  O   B GLU B 65  ? 0.17838 0.37207 0.13832 0.02215  -0.05356 0.03636  61  GLU B O   
2798 C  CB  A GLU B 65  ? 0.22887 0.40805 0.18559 -0.05791 0.06459  0.00187  61  GLU B CB  
2799 C  CB  B GLU B 65  ? 0.22037 0.38002 0.20955 -0.04229 -0.07020 0.04391  61  GLU B CB  
2800 C  CG  A GLU B 65  ? 0.32768 0.44651 0.25390 -0.08041 0.10411  -0.00292 61  GLU B CG  
2801 C  CG  B GLU B 65  ? 0.34751 0.40088 0.28438 -0.05831 -0.02047 0.05383  61  GLU B CG  
2802 C  CD  A GLU B 65  ? 0.40591 0.46352 0.31449 -0.10415 0.15186  0.00080  61  GLU B CD  
2803 C  CD  B GLU B 65  ? 0.41778 0.39942 0.34748 -0.08118 0.01498  0.07514  61  GLU B CD  
2804 O  OE1 A GLU B 65  ? 0.48275 0.48193 0.36386 -0.09867 0.18370  -0.01001 61  GLU B OE1 
2805 O  OE1 B GLU B 65  ? 0.43150 0.36526 0.36486 -0.11324 0.07251  0.05857  61  GLU B OE1 
2806 O  OE2 A GLU B 65  ? 0.41368 0.46667 0.33155 -0.11764 0.14342  0.00411  61  GLU B OE2 
2807 O  OE2 B GLU B 65  ? 0.46149 0.43171 0.38561 -0.07911 0.00333  0.07985  61  GLU B OE2 
2820 N  N   . ASP B 66  ? 0.12831 0.39320 0.13001 -0.02457 0.01989  0.02676  62  ASP B N   
2821 C  CA  . ASP B 66  ? 0.13638 0.40833 0.12497 -0.03556 0.02216  0.00354  62  ASP B CA  
2822 C  C   . ASP B 66  ? 0.10517 0.40509 0.11322 0.00499  0.00676  0.00661  62  ASP B C   
2823 O  O   . ASP B 66  ? 0.10922 0.40937 0.12441 0.02255  0.01041  0.03485  62  ASP B O   
2824 C  CB  . ASP B 66  ? 0.14256 0.43143 0.15945 -0.03344 0.03881  0.00323  62  ASP B CB  
2825 C  CG  . ASP B 66  ? 0.18688 0.50057 0.24665 -0.06344 0.00824  0.03873  62  ASP B CG  
2826 O  OD1 . ASP B 66  ? 0.18492 0.51835 0.29895 -0.05607 -0.00459 0.03632  62  ASP B OD1 
2827 O  OD2 . ASP B 66  ? 0.25835 0.53677 0.38179 -0.06575 -0.01930 0.07063  62  ASP B OD2 
2832 N  N   . THR B 67  ? 0.09402 0.37459 0.11439 0.00580  0.00134  0.01330  63  THR B N   
2833 C  CA  . THR B 67  ? 0.11025 0.33509 0.10859 0.01777  -0.00219 0.00065  63  THR B CA  
2834 C  C   . THR B 67  ? 0.08873 0.32071 0.11277 0.02961  -0.01019 0.00734  63  THR B C   
2835 O  O   . THR B 67  ? 0.10689 0.34525 0.12069 0.01895  -0.00507 0.01860  63  THR B O   
2836 C  CB  . THR B 67  ? 0.12569 0.32889 0.09956 0.00136  -0.01645 0.00769  63  THR B CB  
2837 O  OG1 . THR B 67  ? 0.12245 0.31763 0.13646 0.01669  -0.00367 0.01059  63  THR B OG1 
2838 C  CG2 . THR B 67  ? 0.11903 0.33663 0.12560 0.03540  -0.00742 0.00156  63  THR B CG2 
2846 N  N   . LEU B 68  ? 0.09890 0.30797 0.10504 0.01731  0.00707  0.03721  64  LEU B N   
2847 C  CA  . LEU B 68  ? 0.10275 0.32251 0.09511 0.00855  0.00061  0.01972  64  LEU B CA  
2848 C  C   . LEU B 68  ? 0.10880 0.33186 0.10074 0.01657  0.02068  0.00050  64  LEU B C   
2849 O  O   . LEU B 68  ? 0.10491 0.34123 0.09564 0.02284  0.00266  0.00492  64  LEU B O   
2850 C  CB  . LEU B 68  ? 0.09863 0.34308 0.12183 0.00482  -0.00538 0.02090  64  LEU B CB  
2851 C  CG  . LEU B 68  ? 0.10218 0.35151 0.12363 0.04335  0.01193  0.02352  64  LEU B CG  
2852 C  CD1 . LEU B 68  ? 0.14767 0.36508 0.14409 0.04778  0.01484  0.02539  64  LEU B CD1 
2853 C  CD2 . LEU B 68  ? 0.09708 0.35479 0.13082 0.02026  0.01689  0.01941  64  LEU B CD2 
2865 N  N   . PHE B 69  ? 0.08789 0.34077 0.10059 0.01297  -0.00436 0.01243  65  PHE B N   
2866 C  CA  . PHE B 69  ? 0.09256 0.36245 0.10938 0.01777  0.00327  0.00554  65  PHE B CA  
2867 C  C   . PHE B 69  ? 0.11421 0.37214 0.09477 0.03846  0.00172  0.00501  65  PHE B C   
2868 O  O   . PHE B 69  ? 0.12131 0.38495 0.11292 0.04358  -0.01607 -0.00202 65  PHE B O   
2869 C  CB  . PHE B 69  ? 0.10653 0.40492 0.10438 0.00705  -0.00358 -0.01003 65  PHE B CB  
2870 C  CG  . PHE B 69  ? 0.10429 0.41471 0.11913 0.00546  0.00037  -0.02306 65  PHE B CG  
2871 C  CD1 . PHE B 69  ? 0.11319 0.40776 0.11776 0.00922  -0.01319 -0.00784 65  PHE B CD1 
2872 C  CD2 . PHE B 69  ? 0.10864 0.41740 0.13346 -0.00215 -0.01067 -0.01413 65  PHE B CD2 
2873 C  CE1 . PHE B 69  ? 0.11151 0.42654 0.13638 0.02484  -0.00027 -0.01539 65  PHE B CE1 
2874 C  CE2 . PHE B 69  ? 0.11949 0.44213 0.15298 0.02009  -0.01808 -0.00995 65  PHE B CE2 
2875 C  CZ  . PHE B 69  ? 0.10794 0.42700 0.15858 -0.01680 0.00217  -0.00120 65  PHE B CZ  
2885 N  N   . GLU B 70  ? 0.10671 0.36926 0.10514 0.04580  -0.01000 -0.02609 66  GLU B N   
2886 C  CA  . GLU B 70  ? 0.10159 0.35929 0.12299 0.04740  -0.00831 -0.02577 66  GLU B CA  
2887 C  C   . GLU B 70  ? 0.11710 0.34336 0.13573 0.05962  0.00609  -0.02466 66  GLU B C   
2888 O  O   . GLU B 70  ? 0.17181 0.30973 0.16556 0.04316  -0.02231 0.00952  66  GLU B O   
2889 C  CB  . GLU B 70  ? 0.12263 0.41609 0.12697 0.02662  0.00757  -0.05310 66  GLU B CB  
2890 C  CG  . GLU B 70  ? 0.18652 0.45402 0.18663 0.04618  -0.02985 -0.08382 66  GLU B CG  
2891 C  CD  . GLU B 70  ? 0.23463 0.51896 0.24515 0.02625  0.00363  -0.08604 66  GLU B CD  
2892 O  OE1 . GLU B 70  ? 0.26663 0.56848 0.20987 -0.00711 0.05057  -0.12435 66  GLU B OE1 
2893 O  OE2 . GLU B 70  ? 0.24646 0.52846 0.28256 0.10049  -0.02969 -0.10101 66  GLU B OE2 
2900 N  N   . TYR B 71  ? 0.10311 0.34009 0.10939 0.04440  -0.00517 0.00238  67  TYR B N   
2901 C  CA  . TYR B 71  ? 0.10718 0.33389 0.12500 0.05328  -0.01589 0.01267  67  TYR B CA  
2902 C  C   . TYR B 71  ? 0.14484 0.31801 0.12953 0.05046  -0.01151 0.01892  67  TYR B C   
2903 O  O   . TYR B 71  ? 0.19021 0.32401 0.12593 0.03596  -0.04696 0.00258  67  TYR B O   
2904 C  CB  . TYR B 71  ? 0.09759 0.33917 0.12054 0.05071  0.00004  0.00389  67  TYR B CB  
2905 C  CG  . TYR B 71  ? 0.09775 0.34819 0.09029 0.04261  0.00151  0.01459  67  TYR B CG  
2906 C  CD1 . TYR B 71  ? 0.11353 0.35521 0.10542 0.01539  -0.01381 0.01429  67  TYR B CD1 
2907 C  CD2 . TYR B 71  ? 0.13679 0.36565 0.09903 0.05127  0.01387  0.01051  67  TYR B CD2 
2908 C  CE1 . TYR B 71  ? 0.15303 0.36638 0.10680 0.02997  -0.01573 0.00589  67  TYR B CE1 
2909 C  CE2 . TYR B 71  ? 0.11765 0.38083 0.11266 0.02183  0.01839  -0.00245 67  TYR B CE2 
2910 C  CZ  . TYR B 71  ? 0.12682 0.37082 0.10116 0.01174  0.01481  0.02348  67  TYR B CZ  
2911 O  OH  . TYR B 71  ? 0.15992 0.40059 0.10380 -0.01602 0.01389  0.00273  67  TYR B OH  
2921 N  N   . LEU B 72  ? 0.12475 0.32599 0.11173 0.02263  -0.00071 0.00659  68  LEU B N   
2922 C  CA  . LEU B 72  ? 0.15348 0.32055 0.11603 0.04173  -0.01534 0.00838  68  LEU B CA  
2923 C  C   . LEU B 72  ? 0.17897 0.33957 0.12543 0.05638  -0.05406 -0.01229 68  LEU B C   
2924 O  O   . LEU B 72  ? 0.24729 0.37214 0.12317 0.04065  -0.04478 0.00923  68  LEU B O   
2925 C  CB  . LEU B 72  ? 0.16637 0.33436 0.11138 0.03684  -0.02422 -0.00662 68  LEU B CB  
2926 C  CG  . LEU B 72  ? 0.15952 0.33886 0.09517 0.00738  0.02545  -0.01654 68  LEU B CG  
2927 C  CD1 . LEU B 72  ? 0.19646 0.35841 0.12964 0.01521  0.03537  0.00093  68  LEU B CD1 
2928 C  CD2 . LEU B 72  ? 0.21352 0.35066 0.12860 0.01936  0.03158  0.00585  68  LEU B CD2 
2940 N  N   A GLU B 73  ? 0.18282 0.34464 0.15348 0.06444  -0.04850 -0.00630 69  GLU B N   
2941 N  N   B GLU B 73  ? 0.18555 0.35872 0.16290 0.06663  -0.05164 -0.00301 69  GLU B N   
2942 C  CA  A GLU B 73  ? 0.19424 0.35134 0.18260 0.07122  -0.05751 -0.00485 69  GLU B CA  
2943 C  CA  B GLU B 73  ? 0.20992 0.37724 0.20280 0.07916  -0.06558 -0.00539 69  GLU B CA  
2944 C  C   A GLU B 73  ? 0.22926 0.36736 0.18167 0.07812  -0.06258 -0.00452 69  GLU B C   
2945 C  C   B GLU B 73  ? 0.22763 0.38208 0.19126 0.08559  -0.07888 0.00052  69  GLU B C   
2946 O  O   A GLU B 73  ? 0.28415 0.38606 0.18209 0.06948  -0.05363 0.00747  69  GLU B O   
2947 O  O   B GLU B 73  ? 0.25237 0.38990 0.20092 0.08267  -0.09969 0.01783  69  GLU B O   
2948 C  CB  A GLU B 73  ? 0.17190 0.34591 0.21807 0.07099  -0.08305 0.00712  69  GLU B CB  
2949 C  CB  B GLU B 73  ? 0.20828 0.39677 0.26339 0.08572  -0.09847 0.00075  69  GLU B CB  
2950 C  CG  A GLU B 73  ? 0.18460 0.35028 0.24776 0.06568  -0.10376 0.00095  69  GLU B CG  
2951 C  CG  B GLU B 73  ? 0.24816 0.41852 0.31643 0.09599  -0.11514 -0.00510 69  GLU B CG  
2952 C  CD  A GLU B 73  ? 0.20474 0.39218 0.29441 0.08911  -0.08969 0.02261  69  GLU B CD  
2953 C  CD  B GLU B 73  ? 0.29937 0.42454 0.36996 0.10817  -0.11503 0.00863  69  GLU B CD  
2954 O  OE1 A GLU B 73  ? 0.23719 0.41454 0.34210 0.08690  -0.04706 0.00582  69  GLU B OE1 
2955 O  OE1 B GLU B 73  ? 0.32537 0.40059 0.42135 0.11145  -0.07026 -0.00774 69  GLU B OE1 
2956 O  OE2 A GLU B 73  ? 0.21410 0.42385 0.31138 0.06865  -0.09833 0.02202  69  GLU B OE2 
2957 O  OE2 B GLU B 73  ? 0.35418 0.44231 0.39268 0.11098  -0.10813 0.02298  69  GLU B OE2 
2970 N  N   . ASN B 74  ? 0.21943 0.35489 0.18376 0.08000  -0.09194 -0.01757 70  ASN B N   
2971 C  CA  . ASN B 74  ? 0.21024 0.32623 0.20328 0.05679  -0.08212 0.00543  70  ASN B CA  
2972 C  C   . ASN B 74  ? 0.21877 0.31932 0.17281 0.06952  -0.03626 0.00275  70  ASN B C   
2973 O  O   . ASN B 74  ? 0.22495 0.34560 0.17550 0.06511  -0.02557 -0.01198 70  ASN B O   
2974 C  CB  . ASN B 74  ? 0.22427 0.33779 0.24395 0.09550  -0.06041 0.02392  70  ASN B CB  
2975 C  CG  . ASN B 74  ? 0.26695 0.34325 0.24242 0.09263  -0.05096 0.03885  70  ASN B CG  
2976 O  OD1 . ASN B 74  ? 0.30835 0.36598 0.28640 0.07810  0.00641  0.02310  70  ASN B OD1 
2977 N  ND2 . ASN B 74  ? 0.27869 0.35328 0.29011 0.07824  -0.07243 0.04675  70  ASN B ND2 
2985 N  N   . PRO B 75  ? 0.22050 0.33982 0.15236 0.08397  -0.02822 0.02292  71  PRO B N   
2986 C  CA  . PRO B 75  ? 0.22653 0.35766 0.13065 0.05138  -0.04570 0.00473  71  PRO B CA  
2987 C  C   . PRO B 75  ? 0.24179 0.35305 0.17062 0.03423  -0.04601 -0.00019 71  PRO B C   
2988 O  O   . PRO B 75  ? 0.22738 0.33391 0.15617 0.02859  -0.04193 0.02016  71  PRO B O   
2989 C  CB  . PRO B 75  ? 0.24133 0.37022 0.12190 0.06014  -0.01167 0.01528  71  PRO B CB  
2990 C  CG  . PRO B 75  ? 0.24533 0.37436 0.11691 0.04102  -0.01248 0.00268  71  PRO B CG  
2991 C  CD  . PRO B 75  ? 0.23961 0.36011 0.12737 0.03886  -0.01833 0.00290  71  PRO B CD  
2999 N  N   . LYS B 76  ? 0.26124 0.35726 0.18996 0.03020  -0.02382 0.02603  72  LYS B N   
3000 C  CA  . LYS B 76  ? 0.32189 0.38450 0.22720 0.02796  -0.00276 0.01572  72  LYS B CA  
3001 C  C   . LYS B 76  ? 0.29180 0.36964 0.21468 0.03688  -0.03935 0.00523  72  LYS B C   
3002 O  O   . LYS B 76  ? 0.29606 0.36919 0.21289 0.02191  -0.03946 -0.02902 72  LYS B O   
3003 C  CB  . LYS B 76  ? 0.39161 0.41658 0.25813 0.00666  -0.03698 0.01520  72  LYS B CB  
3004 C  CG  . LYS B 76  ? 0.44777 0.46443 0.30344 -0.02187 -0.06828 0.00888  72  LYS B CG  
3005 C  CD  . LYS B 76  ? 0.53477 0.52447 0.34288 -0.03004 -0.05204 0.01017  72  LYS B CD  
3006 C  CE  . LYS B 76  ? 0.58299 0.56336 0.36790 -0.06750 -0.05387 0.00802  72  LYS B CE  
3007 N  NZ  . LYS B 76  ? 0.62386 0.59166 0.37956 -0.08164 -0.03878 0.01157  72  LYS B NZ  
3021 N  N   . LYS B 77  ? 0.29341 0.37234 0.19103 0.05091  -0.07190 0.00575  73  LYS B N   
3022 C  CA  . LYS B 77  ? 0.26127 0.38551 0.18180 0.06168  -0.05349 0.00492  73  LYS B CA  
3023 C  C   . LYS B 77  ? 0.24929 0.37358 0.16764 0.04143  -0.09237 -0.03822 73  LYS B C   
3024 O  O   . LYS B 77  ? 0.31662 0.36951 0.19162 0.05956  -0.09416 -0.02626 73  LYS B O   
3025 C  CB  . LYS B 77  ? 0.25119 0.43561 0.21808 0.09928  -0.02778 0.04078  73  LYS B CB  
3026 C  CG  . LYS B 77  ? 0.24418 0.51262 0.28356 0.09040  -0.01339 0.01248  73  LYS B CG  
3027 C  CD  . LYS B 77  ? 0.19596 0.59018 0.34170 0.07852  -0.01387 -0.00335 73  LYS B CD  
3028 C  CE  . LYS B 77  ? 0.22975 0.65227 0.41283 0.08036  0.01311  -0.00353 73  LYS B CE  
3029 N  NZ  . LYS B 77  ? 0.28646 0.68773 0.46803 0.04829  0.02100  0.01034  73  LYS B NZ  
3043 N  N   . TYR B 78  ? 0.22011 0.35673 0.17181 0.04619  -0.05281 -0.02905 74  TYR B N   
3044 C  CA  . TYR B 78  ? 0.17013 0.35583 0.14660 0.04491  -0.03595 0.00209  74  TYR B CA  
3045 C  C   . TYR B 78  ? 0.19366 0.36659 0.12450 0.05175  -0.01323 0.00743  74  TYR B C   
3046 O  O   . TYR B 78  ? 0.20503 0.39706 0.14446 0.02429  -0.03140 -0.00328 74  TYR B O   
3047 C  CB  . TYR B 78  ? 0.14016 0.36584 0.16064 0.06113  -0.03226 -0.01429 74  TYR B CB  
3048 C  CG  . TYR B 78  ? 0.14574 0.36399 0.16348 0.05136  -0.02989 -0.02233 74  TYR B CG  
3049 C  CD1 . TYR B 78  ? 0.14475 0.35636 0.18122 0.02477  -0.01605 -0.00643 74  TYR B CD1 
3050 C  CD2 . TYR B 78  ? 0.14800 0.36510 0.15529 0.02779  -0.00361 -0.00123 74  TYR B CD2 
3051 C  CE1 . TYR B 78  ? 0.13888 0.36952 0.21475 0.00387  -0.01573 -0.00143 74  TYR B CE1 
3052 C  CE2 . TYR B 78  ? 0.15704 0.37225 0.11937 0.01587  -0.01582 -0.00660 74  TYR B CE2 
3053 C  CZ  . TYR B 78  ? 0.16157 0.36051 0.17014 0.03221  -0.03464 0.00608  74  TYR B CZ  
3054 O  OH  . TYR B 78  ? 0.16482 0.35282 0.17420 0.01805  -0.00036 -0.00358 74  TYR B OH  
3064 N  N   . ILE B 79  ? 0.19404 0.36305 0.14095 0.01778  -0.00012 -0.00436 75  ILE B N   
3065 C  CA  . ILE B 79  ? 0.18460 0.34855 0.16026 0.01264  -0.02663 0.00246  75  ILE B CA  
3066 C  C   . ILE B 79  ? 0.22183 0.34064 0.17826 0.02030  -0.01493 -0.00124 75  ILE B C   
3067 O  O   . ILE B 79  ? 0.27150 0.36566 0.18464 -0.00081 -0.00060 -0.00790 75  ILE B O   
3068 C  CB  . ILE B 79  ? 0.15624 0.36860 0.16407 -0.00618 -0.04405 0.00631  75  ILE B CB  
3069 C  CG1 . ILE B 79  ? 0.16987 0.38709 0.15053 -0.00836 -0.02053 -0.01020 75  ILE B CG1 
3070 C  CG2 . ILE B 79  ? 0.18662 0.36236 0.16862 -0.04244 -0.02263 0.02122  75  ILE B CG2 
3071 C  CD1 . ILE B 79  ? 0.14788 0.39359 0.14208 0.00380  -0.02818 -0.00660 75  ILE B CD1 
3083 N  N   . PRO B 80  ? 0.28545 0.33419 0.21506 0.01495  0.00012  -0.01946 76  PRO B N   
3084 C  CA  . PRO B 80  ? 0.33339 0.34768 0.25585 -0.03345 -0.00323 -0.03190 76  PRO B CA  
3085 C  C   . PRO B 80  ? 0.36907 0.36573 0.26935 -0.05900 0.00414  -0.06454 76  PRO B C   
3086 O  O   . PRO B 80  ? 0.35344 0.39682 0.29101 -0.06030 -0.01281 -0.04634 76  PRO B O   
3087 C  CB  . PRO B 80  ? 0.35685 0.36805 0.29793 -0.01917 0.00279  -0.01989 76  PRO B CB  
3088 C  CG  . PRO B 80  ? 0.34220 0.35302 0.25743 -0.01405 -0.01251 -0.04611 76  PRO B CG  
3089 C  CD  . PRO B 80  ? 0.28955 0.34799 0.23563 0.00855  -0.02877 -0.02542 76  PRO B CD  
3097 N  N   . GLY B 81  ? 0.37372 0.37328 0.29074 -0.05380 0.01153  -0.06374 77  GLY B N   
3098 C  CA  . GLY B 81  ? 0.36419 0.39928 0.28436 -0.07138 0.00986  -0.06447 77  GLY B CA  
3099 C  C   . GLY B 81  ? 0.36430 0.41487 0.24310 -0.07960 -0.00905 -0.05350 77  GLY B C   
3100 O  O   . GLY B 81  ? 0.37874 0.42208 0.25403 -0.08676 0.03766  -0.05202 77  GLY B O   
3104 N  N   . THR B 82  ? 0.34124 0.41338 0.22500 -0.07253 0.00527  -0.02318 78  THR B N   
3105 C  CA  . THR B 82  ? 0.23930 0.41339 0.21197 -0.05955 -0.02025 -0.02525 78  THR B CA  
3106 C  C   . THR B 82  ? 0.20954 0.43618 0.19897 -0.05110 -0.04622 0.02577  78  THR B C   
3107 O  O   . THR B 82  ? 0.25691 0.45058 0.22291 -0.04007 0.00930  0.00297  78  THR B O   
3108 C  CB  . THR B 82  ? 0.22527 0.43232 0.19557 -0.04602 -0.03999 -0.00476 78  THR B CB  
3109 O  OG1 . THR B 82  ? 0.19369 0.44485 0.16530 -0.05655 -0.01947 -0.01610 78  THR B OG1 
3110 C  CG2 . THR B 82  ? 0.21166 0.43044 0.19212 -0.05383 -0.04242 0.00364  78  THR B CG2 
3118 N  N   . LYS B 83  ? 0.22471 0.45335 0.18871 -0.11535 0.01518  -0.03556 79  LYS B N   
3119 C  CA  A LYS B 83  ? 0.25395 0.46007 0.15667 -0.11366 0.01636  -0.03168 79  LYS B CA  
3120 C  CA  B LYS B 83  ? 0.27592 0.46172 0.17029 -0.11626 0.02372  -0.02244 79  LYS B CA  
3121 C  C   . LYS B 83  ? 0.25631 0.47477 0.15836 -0.11038 -0.01566 -0.02160 79  LYS B C   
3122 O  O   . LYS B 83  ? 0.33697 0.47602 0.15316 -0.12021 -0.00524 -0.01223 79  LYS B O   
3123 C  CB  A LYS B 83  ? 0.25615 0.47840 0.17181 -0.08842 0.01473  -0.03171 79  LYS B CB  
3124 C  CB  B LYS B 83  ? 0.33077 0.48272 0.20853 -0.09541 0.05055  -0.00517 79  LYS B CB  
3125 C  CG  A LYS B 83  ? 0.21675 0.49200 0.18866 -0.09464 -0.04166 -0.02773 79  LYS B CG  
3126 C  CG  B LYS B 83  ? 0.36674 0.50044 0.24386 -0.09299 0.05557  0.01377  79  LYS B CG  
3127 C  CD  A LYS B 83  ? 0.22808 0.50424 0.25726 -0.07406 0.00049  -0.00866 79  LYS B CD  
3128 C  CD  B LYS B 83  ? 0.42940 0.51194 0.28333 -0.07660 0.09098  0.03285  79  LYS B CD  
3129 C  CE  A LYS B 83  ? 0.15655 0.49576 0.28761 -0.03514 -0.03987 0.01304  79  LYS B CE  
3130 C  CE  B LYS B 83  ? 0.45837 0.51562 0.29923 -0.04853 0.10559  0.04575  79  LYS B CE  
3131 N  NZ  A LYS B 83  ? 0.12977 0.49979 0.33057 -0.01312 -0.01501 0.03070  79  LYS B NZ  
3132 N  NZ  B LYS B 83  ? 0.46715 0.51385 0.29199 -0.03836 0.14688  0.04117  79  LYS B NZ  
3157 N  N   . MET B 84  ? 0.23295 0.47349 0.17395 -0.10934 -0.04331 -0.01562 80  MET B N   
3158 C  CA  . MET B 84  ? 0.19264 0.47435 0.15225 -0.08322 -0.03309 0.00195  80  MET B CA  
3159 C  C   . MET B 84  ? 0.25552 0.49084 0.15121 -0.08275 -0.02472 -0.01227 80  MET B C   
3160 O  O   . MET B 84  ? 0.27743 0.45994 0.17515 -0.06033 -0.01554 0.00597  80  MET B O   
3161 C  CB  . MET B 84  ? 0.21173 0.44897 0.15209 -0.06617 -0.01266 -0.02278 80  MET B CB  
3162 C  CG  . MET B 84  ? 0.14855 0.42378 0.15035 -0.07768 -0.02062 -0.02164 80  MET B CG  
3163 S  SD  . MET B 84  ? 0.14288 0.41456 0.11279 -0.04046 -0.00144 -0.01918 80  MET B SD  
3164 C  CE  . MET B 84  ? 0.12626 0.41439 0.11415 -0.01330 -0.01519 0.01005  80  MET B CE  
3174 N  N   . ILE B 85  ? 0.26686 0.48350 0.13825 -0.08055 0.00670  0.00724  81  ILE B N   
3175 C  CA  . ILE B 85  ? 0.31422 0.50330 0.16522 -0.07161 0.00166  0.02273  81  ILE B CA  
3176 C  C   . ILE B 85  ? 0.34541 0.52620 0.17249 -0.06278 -0.00245 0.02059  81  ILE B C   
3177 O  O   . ILE B 85  ? 0.35088 0.52533 0.20780 -0.04997 -0.01544 -0.01397 81  ILE B O   
3178 C  CB  . ILE B 85  ? 0.37264 0.51294 0.23459 -0.05268 0.00104  0.03091  81  ILE B CB  
3179 C  CG1 . ILE B 85  ? 0.50166 0.51718 0.28097 -0.01682 0.04382  0.04217  81  ILE B CG1 
3180 C  CG2 . ILE B 85  ? 0.40645 0.52380 0.24706 -0.05124 0.01896  0.03252  81  ILE B CG2 
3181 C  CD1 . ILE B 85  ? 0.54845 0.52060 0.30895 -0.00713 0.07191  0.07597  81  ILE B CD1 
3193 N  N   . PHE B 86  ? 0.33283 0.51164 0.17720 -0.11117 -0.03034 0.02298  82  PHE B N   
3194 C  CA  . PHE B 86  ? 0.36346 0.50088 0.18278 -0.07781 -0.03203 0.04077  82  PHE B CA  
3195 C  C   . PHE B 86  ? 0.38546 0.50078 0.23262 -0.05475 -0.03868 0.08875  82  PHE B C   
3196 O  O   . PHE B 86  ? 0.41804 0.49313 0.24309 -0.04684 -0.02016 0.04620  82  PHE B O   
3197 C  CB  . PHE B 86  ? 0.29837 0.48178 0.17353 -0.07641 -0.05032 -0.00447 82  PHE B CB  
3198 C  CG  . PHE B 86  ? 0.30393 0.47632 0.16080 -0.03417 -0.02338 -0.02925 82  PHE B CG  
3199 C  CD1 . PHE B 86  ? 0.34282 0.47152 0.16285 -0.03297 0.01906  -0.05166 82  PHE B CD1 
3200 C  CD2 . PHE B 86  ? 0.26273 0.46260 0.16494 0.00773  -0.05080 -0.01852 82  PHE B CD2 
3201 C  CE1 . PHE B 86  ? 0.36784 0.46081 0.15197 -0.02658 0.02274  -0.06134 82  PHE B CE1 
3202 C  CE2 . PHE B 86  ? 0.27249 0.44455 0.14943 0.00666  -0.03724 -0.01216 82  PHE B CE2 
3203 C  CZ  . PHE B 86  ? 0.34228 0.45770 0.16053 -0.01148 -0.02130 -0.02106 82  PHE B CZ  
3213 N  N   . ALA B 87  ? 0.36740 0.51048 0.30709 -0.05237 -0.06926 0.12509  83  ALA B N   
3214 C  CA  . ALA B 87  ? 0.37879 0.51460 0.33672 -0.03063 -0.04120 0.13107  83  ALA B CA  
3215 C  C   . ALA B 87  ? 0.37172 0.51128 0.31926 0.00811  -0.05370 0.10660  83  ALA B C   
3216 O  O   . ALA B 87  ? 0.40987 0.49949 0.37470 0.06954  -0.05172 0.13067  83  ALA B O   
3217 C  CB  . ALA B 87  ? 0.38238 0.53602 0.35937 -0.03638 -0.05777 0.15412  83  ALA B CB  
3223 N  N   . GLY B 88  ? 0.36048 0.50162 0.26194 0.00778  -0.07709 0.06867  84  GLY B N   
3224 C  CA  . GLY B 88  ? 0.31861 0.49070 0.22740 -0.00352 -0.10829 0.05262  84  GLY B CA  
3225 C  C   . GLY B 88  ? 0.33245 0.49100 0.18893 0.02398  -0.09391 0.05785  84  GLY B C   
3226 O  O   . GLY B 88  ? 0.40502 0.51342 0.20783 0.00253  -0.09752 0.05646  84  GLY B O   
3230 N  N   . LEU B 89  ? 0.32098 0.46737 0.15514 0.03068  -0.07605 0.03963  85  LEU B N   
3231 C  CA  . LEU B 89  ? 0.30990 0.47515 0.15746 0.03548  -0.07754 0.02703  85  LEU B CA  
3232 C  C   . LEU B 89  ? 0.29248 0.50423 0.19450 0.01897  -0.08911 0.02125  85  LEU B C   
3233 O  O   . LEU B 89  ? 0.26459 0.51902 0.18500 0.01886  -0.07124 0.04598  85  LEU B O   
3234 C  CB  . LEU B 89  ? 0.42428 0.48460 0.16975 0.03159  -0.01536 0.04769  85  LEU B CB  
3235 C  CG  . LEU B 89  ? 0.45702 0.49922 0.17555 0.03469  0.03417  0.03169  85  LEU B CG  
3236 C  CD1 . LEU B 89  ? 0.35583 0.48274 0.16326 0.00574  0.09880  -0.01510 85  LEU B CD1 
3237 C  CD2 . LEU B 89  ? 0.45282 0.48657 0.13256 0.03050  0.04000  0.01855  85  LEU B CD2 
3249 N  N   . LYS B 90  ? 0.34045 0.51888 0.22438 0.05038  -0.10637 0.04638  86  LYS B N   
3250 C  CA  . LYS B 90  ? 0.39269 0.53930 0.26324 0.06673  -0.12158 0.04099  86  LYS B CA  
3251 C  C   . LYS B 90  ? 0.34322 0.56273 0.25568 0.07213  -0.07719 0.01439  86  LYS B C   
3252 O  O   . LYS B 90  ? 0.33915 0.60634 0.27340 0.09383  -0.08484 0.01196  86  LYS B O   
3253 C  CB  . LYS B 90  ? 0.47740 0.52887 0.35423 0.07481  -0.17303 0.04830  86  LYS B CB  
3254 C  CG  . LYS B 90  ? 0.52027 0.51771 0.41741 0.07160  -0.20067 0.05555  86  LYS B CG  
3255 C  CD  . LYS B 90  ? 0.55771 0.50099 0.47291 0.06458  -0.19817 0.03195  86  LYS B CD  
3256 C  CE  . LYS B 90  ? 0.56803 0.49128 0.48998 0.07993  -0.21292 0.02257  86  LYS B CE  
3257 N  NZ  . LYS B 90  ? 0.58236 0.47188 0.52456 0.09977  -0.17427 0.01215  86  LYS B NZ  
3271 N  N   . LYS B 91  ? 0.23523 0.54796 0.24242 0.08256  -0.08669 0.00254  87  LYS B N   
3272 C  CA  . LYS B 91  ? 0.23427 0.53008 0.22350 0.06765  -0.07636 -0.01449 87  LYS B CA  
3273 C  C   . LYS B 91  ? 0.17483 0.50486 0.19142 0.06731  -0.04816 -0.02325 87  LYS B C   
3274 O  O   . LYS B 91  ? 0.16306 0.53243 0.20477 0.06880  -0.03076 0.00681  87  LYS B O   
3275 C  CB  . LYS B 91  ? 0.29629 0.53410 0.23773 0.05136  -0.12430 -0.00123 87  LYS B CB  
3276 C  CG  . LYS B 91  ? 0.35839 0.56686 0.27054 0.06295  -0.15630 0.00736  87  LYS B CG  
3277 C  CD  . LYS B 91  ? 0.45090 0.61393 0.29374 0.06418  -0.18424 -0.00118 87  LYS B CD  
3278 C  CE  . LYS B 91  ? 0.53163 0.64635 0.33715 0.06442  -0.14021 -0.01744 87  LYS B CE  
3279 N  NZ  . LYS B 91  ? 0.57333 0.66437 0.38511 0.05415  -0.12430 -0.03031 87  LYS B NZ  
3293 N  N   . PRO B 92  ? 0.15073 0.48871 0.20530 0.05140  -0.04126 -0.01631 88  PRO B N   
3294 C  CA  . PRO B 92  ? 0.13179 0.48231 0.19681 0.02450  -0.02681 -0.01614 88  PRO B CA  
3295 C  C   . PRO B 92  ? 0.13444 0.45815 0.16380 0.00897  -0.03076 -0.02080 88  PRO B C   
3296 O  O   . PRO B 92  ? 0.12090 0.47975 0.15043 0.00722  -0.00373 -0.02310 88  PRO B O   
3297 C  CB  . PRO B 92  ? 0.14903 0.52838 0.20776 0.04334  -0.02824 -0.03155 88  PRO B CB  
3298 C  CG  . PRO B 92  ? 0.15973 0.51922 0.24939 0.03851  -0.05132 -0.03474 88  PRO B CG  
3299 C  CD  . PRO B 92  ? 0.15916 0.48214 0.25835 0.03714  -0.06814 -0.03529 88  PRO B CD  
3307 N  N   . ASN B 93  ? 0.12120 0.48034 0.15461 0.01482  -0.00207 -0.02007 89  ASN B N   
3308 C  CA  . ASN B 93  ? 0.12353 0.48456 0.15855 -0.02001 -0.00371 -0.02128 89  ASN B CA  
3309 C  C   . ASN B 93  ? 0.12551 0.48090 0.15099 -0.00590 -0.00968 -0.03760 89  ASN B C   
3310 O  O   . ASN B 93  ? 0.13287 0.51813 0.16596 -0.01076 -0.00235 -0.05822 89  ASN B O   
3311 C  CB  . ASN B 93  ? 0.13583 0.53244 0.15431 -0.01784 0.00617  -0.02265 89  ASN B CB  
3312 C  CG  . ASN B 93  ? 0.14917 0.57290 0.18266 0.02050  -0.01056 -0.00506 89  ASN B CG  
3313 O  OD1 . ASN B 93  ? 0.14409 0.56102 0.22494 0.02884  -0.01066 -0.02000 89  ASN B OD1 
3314 N  ND2 . ASN B 93  ? 0.15215 0.59661 0.16328 -0.01884 0.00548  -0.00584 89  ASN B ND2 
3321 N  N   . GLU B 94  ? 0.12817 0.47711 0.14368 0.04436  -0.00858 -0.02247 90  GLU B N   
3322 C  CA  . GLU B 94  ? 0.12871 0.47389 0.14869 0.03616  0.01055  -0.01758 90  GLU B CA  
3323 C  C   . GLU B 94  ? 0.10909 0.42230 0.13270 0.01484  0.00613  -0.02435 90  GLU B C   
3324 O  O   . GLU B 94  ? 0.11486 0.42543 0.13395 0.01812  0.01436  0.00835  90  GLU B O   
3325 C  CB  . GLU B 94  ? 0.18271 0.49663 0.17256 0.01154  -0.04314 0.00453  90  GLU B CB  
3326 C  CG  . GLU B 94  ? 0.21379 0.52466 0.18332 -0.00536 -0.06370 0.03068  90  GLU B CG  
3327 C  CD  . GLU B 94  ? 0.35506 0.56207 0.18117 -0.03824 -0.08878 0.02845  90  GLU B CD  
3328 O  OE1 . GLU B 94  ? 0.39777 0.55140 0.27223 -0.10171 -0.04688 0.04042  90  GLU B OE1 
3329 O  OE2 . GLU B 94  ? 0.42632 0.58963 0.21687 0.00128  -0.07669 0.03341  90  GLU B OE2 
3336 N  N   . ARG B 95  ? 0.10762 0.40176 0.15525 0.00463  0.01894  -0.01575 91  ARG B N   
3337 C  CA  . ARG B 95  ? 0.10865 0.39209 0.12225 -0.00433 -0.01601 0.00319  91  ARG B CA  
3338 C  C   . ARG B 95  ? 0.10743 0.41426 0.11433 -0.01749 0.00553  -0.00588 91  ARG B C   
3339 O  O   . ARG B 95  ? 0.11565 0.39112 0.11942 -0.00656 0.01635  -0.00434 91  ARG B O   
3340 C  CB  . ARG B 95  ? 0.11576 0.41226 0.15158 0.02239  -0.02241 0.00295  91  ARG B CB  
3341 C  CG  . ARG B 95  ? 0.15471 0.42013 0.15237 0.03609  -0.01826 0.00289  91  ARG B CG  
3342 C  CD  . ARG B 95  ? 0.12532 0.42820 0.14900 0.05178  -0.01711 0.00253  91  ARG B CD  
3343 N  NE  . ARG B 95  ? 0.16142 0.47198 0.19887 0.06490  -0.03068 -0.03438 91  ARG B NE  
3344 C  CZ  . ARG B 95  ? 0.15701 0.46945 0.16877 0.06990  -0.03519 -0.01907 91  ARG B CZ  
3345 N  NH1 . ARG B 95  ? 0.16803 0.50945 0.15577 0.04507  -0.03140 -0.01536 91  ARG B NH1 
3346 N  NH2 . ARG B 95  ? 0.17746 0.50046 0.24029 0.06435  -0.06390 -0.04109 91  ARG B NH2 
3360 N  N   . GLY B 96  ? 0.12627 0.42898 0.15265 -0.04005 0.02471  -0.01056 92  GLY B N   
3361 C  CA  . GLY B 96  ? 0.12095 0.42014 0.15430 -0.04755 0.01761  0.00275  92  GLY B CA  
3362 C  C   . GLY B 96  ? 0.15292 0.42886 0.13367 -0.04948 0.02836  0.00515  92  GLY B C   
3363 O  O   . GLY B 96  ? 0.17316 0.41184 0.13057 -0.04084 0.03495  0.01179  92  GLY B O   
3367 N  N   . ASP B 97  ? 0.13645 0.42908 0.15925 -0.05590 0.01075  -0.02579 93  ASP B N   
3368 C  CA  . ASP B 97  ? 0.15065 0.43437 0.17114 -0.04911 -0.01194 -0.02730 93  ASP B CA  
3369 C  C   . ASP B 97  ? 0.13944 0.37909 0.15412 -0.04127 0.01273  -0.00377 93  ASP B C   
3370 O  O   . ASP B 97  ? 0.18425 0.37437 0.14318 -0.07370 0.02484  -0.00441 93  ASP B O   
3371 C  CB  . ASP B 97  ? 0.14515 0.46360 0.17072 -0.07233 -0.01679 -0.02412 93  ASP B CB  
3372 C  CG  . ASP B 97  ? 0.19031 0.54332 0.17304 -0.10906 -0.00906 -0.02173 93  ASP B CG  
3373 O  OD1 . ASP B 97  ? 0.23173 0.58490 0.19331 -0.14947 0.02216  0.00675  93  ASP B OD1 
3374 O  OD2 . ASP B 97  ? 0.20497 0.54713 0.21381 -0.11716 -0.01723 -0.01578 93  ASP B OD2 
3379 N  N   . LEU B 98  ? 0.13049 0.36174 0.11702 -0.02632 0.00889  -0.01530 94  LEU B N   
3380 C  CA  . LEU B 98  ? 0.11013 0.34928 0.12066 -0.00596 0.00565  -0.00819 94  LEU B CA  
3381 C  C   . LEU B 98  ? 0.14970 0.34402 0.10705 0.00980  -0.00511 0.01249  94  LEU B C   
3382 O  O   . LEU B 98  ? 0.13954 0.33400 0.12106 -0.00658 0.00893  0.00713  94  LEU B O   
3383 C  CB  . LEU B 98  ? 0.12568 0.35150 0.11265 0.00250  0.00392  -0.01582 94  LEU B CB  
3384 C  CG  . LEU B 98  ? 0.09916 0.36253 0.11392 -0.01112 -0.00839 0.00060  94  LEU B CG  
3385 C  CD1 . LEU B 98  ? 0.10522 0.37674 0.12129 0.00393  0.01723  0.00641  94  LEU B CD1 
3386 C  CD2 . LEU B 98  ? 0.14483 0.36892 0.16548 -0.00130 -0.02737 0.00604  94  LEU B CD2 
3398 N  N   . ILE B 99  ? 0.14589 0.36188 0.09533 -0.00288 -0.00615 -0.01781 95  ILE B N   
3399 C  CA  . ILE B 99  ? 0.15090 0.37177 0.10950 -0.00434 -0.01622 0.00023  95  ILE B CA  
3400 C  C   . ILE B 99  ? 0.19654 0.39412 0.11053 -0.04883 0.00998  -0.00093 95  ILE B C   
3401 O  O   . ILE B 99  ? 0.21659 0.38970 0.12273 0.00180  0.00117  0.01369  95  ILE B O   
3402 C  CB  . ILE B 99  ? 0.13452 0.39590 0.12143 0.00915  0.00742  -0.01084 95  ILE B CB  
3403 C  CG1 . ILE B 99  ? 0.11984 0.41022 0.10960 0.00876  -0.01089 -0.00021 95  ILE B CG1 
3404 C  CG2 . ILE B 99  ? 0.21871 0.41183 0.11064 0.01568  0.01976  -0.00534 95  ILE B CG2 
3405 C  CD1 . ILE B 99  ? 0.15160 0.42160 0.11914 0.03216  0.00715  -0.00873 95  ILE B CD1 
3417 N  N   . ALA B 100 ? 0.20075 0.35948 0.13512 -0.02076 0.02865  0.01992  96  ALA B N   
3418 C  CA  . ALA B 100 ? 0.26061 0.35126 0.14963 -0.06185 0.02316  0.01447  96  ALA B CA  
3419 C  C   . ALA B 100 ? 0.26064 0.32542 0.16104 -0.00693 0.04169  0.01819  96  ALA B C   
3420 O  O   . ALA B 100 ? 0.31458 0.31622 0.18374 -0.01185 0.00029  0.01154  96  ALA B O   
3421 C  CB  . ALA B 100 ? 0.28552 0.35726 0.18812 -0.07039 0.01862  0.02850  96  ALA B CB  
3427 N  N   . TYR B 101 ? 0.23334 0.31958 0.14508 -0.00337 0.01163  -0.00303 97  TYR B N   
3428 C  CA  . TYR B 101 ? 0.24837 0.32261 0.15908 0.00397  0.00232  -0.00634 97  TYR B CA  
3429 C  C   . TYR B 101 ? 0.27880 0.33367 0.18225 0.00323  0.00087  -0.00591 97  TYR B C   
3430 O  O   . TYR B 101 ? 0.30834 0.34185 0.17479 0.05961  -0.01108 0.00512  97  TYR B O   
3431 C  CB  . TYR B 101 ? 0.24510 0.30508 0.17037 0.00978  0.00360  -0.00542 97  TYR B CB  
3432 C  CG  . TYR B 101 ? 0.23733 0.32888 0.16084 0.00902  -0.01294 -0.01271 97  TYR B CG  
3433 C  CD1 . TYR B 101 ? 0.25756 0.32790 0.17369 0.01216  0.01280  -0.01125 97  TYR B CD1 
3434 C  CD2 . TYR B 101 ? 0.23727 0.34170 0.14564 0.02096  -0.00087 0.01209  97  TYR B CD2 
3435 C  CE1 . TYR B 101 ? 0.25400 0.34241 0.18488 0.01729  0.00838  -0.02788 97  TYR B CE1 
3436 C  CE2 . TYR B 101 ? 0.18677 0.33837 0.15704 0.01084  -0.02217 -0.00937 97  TYR B CE2 
3437 C  CZ  . TYR B 101 ? 0.26021 0.34631 0.17130 0.03246  0.01139  -0.01520 97  TYR B CZ  
3438 O  OH  . TYR B 101 ? 0.27100 0.33952 0.23422 0.06339  -0.00439 -0.00610 97  TYR B OH  
3448 N  N   . LEU B 102 ? 0.21987 0.31736 0.15299 0.01034  -0.01242 0.00818  98  LEU B N   
3449 C  CA  . LEU B 102 ? 0.19885 0.34321 0.14425 0.05655  -0.00801 0.01534  98  LEU B CA  
3450 C  C   . LEU B 102 ? 0.25761 0.35632 0.16076 0.08311  -0.02301 0.02097  98  LEU B C   
3451 O  O   . LEU B 102 ? 0.29225 0.35064 0.16930 0.08124  -0.04330 -0.00748 98  LEU B O   
3452 C  CB  . LEU B 102 ? 0.14047 0.36863 0.13892 0.02173  -0.01249 0.00087  98  LEU B CB  
3453 C  CG  . LEU B 102 ? 0.16278 0.38909 0.12955 0.00812  -0.01002 0.02436  98  LEU B CG  
3454 C  CD1 . LEU B 102 ? 0.18013 0.38499 0.15037 -0.02912 -0.01988 0.03395  98  LEU B CD1 
3455 C  CD2 . LEU B 102 ? 0.15340 0.40336 0.18430 0.02061  0.00434  0.03409  98  LEU B CD2 
3467 N  N   . LYS B 103 ? 0.26331 0.37476 0.15931 0.06094  -0.01519 0.03319  99  LYS B N   
3468 C  CA  . LYS B 103 ? 0.34671 0.38278 0.17122 0.07338  -0.01601 0.04868  99  LYS B CA  
3469 C  C   . LYS B 103 ? 0.37325 0.36883 0.19891 0.11418  -0.00834 0.06791  99  LYS B C   
3470 O  O   . LYS B 103 ? 0.45600 0.41822 0.22169 0.11268  -0.04460 0.03761  99  LYS B O   
3471 C  CB  . LYS B 103 ? 0.39744 0.43044 0.21870 0.05394  -0.00961 0.07283  99  LYS B CB  
3472 C  CG  . LYS B 103 ? 0.39706 0.46732 0.27770 0.01983  0.05790  0.05042  99  LYS B CG  
3473 C  CD  . LYS B 103 ? 0.36752 0.49567 0.30818 -0.01243 0.05225  0.04466  99  LYS B CD  
3474 C  CE  B LYS B 103 ? 0.35668 0.50616 0.29257 -0.04256 0.04062  0.04041  99  LYS B CE  
3475 N  NZ  B LYS B 103 ? 0.37472 0.51690 0.28742 -0.05570 0.05874  0.03978  99  LYS B NZ  
3489 N  N   . SER B 104 ? 0.34379 0.36004 0.19212 0.07673  0.01409  0.01658  100 SER B N   
3490 C  CA  . SER B 104 ? 0.43000 0.36363 0.20627 0.08040  0.02476  0.01706  100 SER B CA  
3491 C  C   . SER B 104 ? 0.40088 0.36375 0.24286 0.11608  0.02039  0.02779  100 SER B C   
3492 O  O   . SER B 104 ? 0.39906 0.40151 0.25722 0.13047  0.01701  0.04725  100 SER B O   
3493 C  CB  . SER B 104 ? 0.51701 0.36148 0.24051 0.06738  0.03337  -0.00868 100 SER B CB  
3494 O  OG  . SER B 104 ? 0.60845 0.38603 0.30288 0.05800  0.06137  -0.00468 100 SER B OG  
3500 N  N   . ALA B 105 ? 0.39524 0.35874 0.24399 0.09464  0.01591  -0.01526 101 ALA B N   
3501 C  CA  . ALA B 105 ? 0.32964 0.36868 0.19523 0.12546  -0.04605 -0.04025 101 ALA B CA  
3502 C  C   . ALA B 105 ? 0.34107 0.41065 0.20814 0.14854  -0.06218 -0.04264 101 ALA B C   
3503 O  O   . ALA B 105 ? 0.36267 0.44097 0.26880 0.18561  -0.03430 -0.07422 101 ALA B O   
3504 C  CB  . ALA B 105 ? 0.31319 0.38442 0.18900 0.08693  -0.07524 -0.00932 101 ALA B CB  
3510 N  N   . THR B 106 ? 0.34392 0.40588 0.19058 0.13915  -0.03555 -0.02771 102 THR B N   
3511 C  CA  . THR B 106 ? 0.31726 0.44415 0.18555 0.13739  -0.06049 -0.00253 102 THR B CA  
3512 C  C   . THR B 106 ? 0.35531 0.47709 0.20434 0.13978  -0.07215 0.00760  102 THR B C   
3513 O  O   . THR B 106 ? 0.36416 0.47199 0.21785 0.14831  -0.04554 0.02322  102 THR B O   
3514 C  CB  . THR B 106 ? 0.28990 0.44082 0.21389 0.10882  -0.03142 -0.01585 102 THR B CB  
3515 O  OG1 . THR B 106 ? 0.23098 0.46035 0.17298 0.10746  -0.03998 -0.01677 102 THR B OG1 
3516 C  CG2 . THR B 106 ? 0.25736 0.44774 0.21378 0.08877  -0.08801 0.00262  102 THR B CG2 
3524 N  N   . LYS B 107 ? 0.43751 0.50646 0.28184 0.12847  -0.03657 0.03547  103 LYS B N   
3525 C  CA  . LYS B 107 ? 0.50114 0.56362 0.35571 0.12165  -0.09312 0.08313  103 LYS B CA  
3526 C  C   . LYS B 107 ? 0.52740 0.58868 0.38139 0.14397  -0.16003 0.08493  103 LYS B C   
3527 O  O   . LYS B 107 ? 0.56536 0.58882 0.44762 0.14202  -0.10113 0.04658  103 LYS B O   
3528 C  CB  . LYS B 107 ? 0.52111 0.58639 0.39450 0.09206  -0.07974 0.14148  103 LYS B CB  
3529 C  CG  . LYS B 107 ? 0.58685 0.61578 0.45493 0.05821  -0.04572 0.16615  103 LYS B CG  
3530 C  CD  . LYS B 107 ? 0.63567 0.63169 0.50085 0.04818  -0.00725 0.19290  103 LYS B CD  
3531 C  CE  . LYS B 107 ? 0.66626 0.64413 0.53419 0.05660  0.01021  0.21085  103 LYS B CE  
3532 N  NZ  . LYS B 107 ? 0.69982 0.66130 0.56869 0.08038  0.02579  0.21172  103 LYS B NZ  
3533 O  OXT . LYS B 107 ? 0.57272 0.61179 0.41593 0.13250  -0.15858 0.10729  103 LYS B OXT 
3547 FE FE  . HEC C .   ? 0.10480 0.23585 0.09506 -0.00362 -0.00621 -0.00669 201 HEC A FE  
3548 C  CHA . HEC C .   ? 0.10818 0.21123 0.09653 0.01664  0.00109  -0.00196 201 HEC A CHA 
3549 C  CHB . HEC C .   ? 0.08694 0.23808 0.10901 -0.01089 0.00798  -0.00284 201 HEC A CHB 
3550 C  CHC . HEC C .   ? 0.12251 0.25806 0.09957 0.01170  -0.01631 0.01913  201 HEC A CHC 
3551 C  CHD . HEC C .   ? 0.11569 0.27050 0.11339 0.00626  0.01403  -0.03692 201 HEC A CHD 
3552 N  NA  . HEC C .   ? 0.08484 0.25176 0.10703 0.00762  0.00595  0.00109  201 HEC A NA  
3553 C  C1A . HEC C .   ? 0.09841 0.23466 0.09143 -0.00389 0.00255  -0.01891 201 HEC A C1A 
3554 C  C2A . HEC C .   ? 0.07832 0.25082 0.10394 -0.00213 -0.02478 -0.01124 201 HEC A C2A 
3555 C  C3A . HEC C .   ? 0.09943 0.23857 0.09668 -0.01527 0.00065  -0.02066 201 HEC A C3A 
3556 C  C4A . HEC C .   ? 0.08756 0.23123 0.09063 0.00084  -0.01261 -0.01269 201 HEC A C4A 
3557 C  CMA . HEC C .   ? 0.08717 0.25390 0.11953 -0.01027 0.00895  0.01184  201 HEC A CMA 
3558 C  CAA . HEC C .   ? 0.10231 0.25731 0.10844 -0.00046 0.00118  -0.00400 201 HEC A CAA 
3559 C  CBA . HEC C .   ? 0.07237 0.27499 0.09836 0.00023  -0.01023 0.00628  201 HEC A CBA 
3560 C  CGA . HEC C .   ? 0.07637 0.24586 0.10821 -0.00165 -0.01083 -0.03289 201 HEC A CGA 
3561 O  O1A . HEC C .   ? 0.12618 0.22163 0.10016 0.00794  -0.01659 -0.01219 201 HEC A O1A 
3562 O  O2A . HEC C .   ? 0.08726 0.27611 0.11345 -0.00046 -0.00951 -0.00754 201 HEC A O2A 
3563 N  NB  . HEC C .   ? 0.08964 0.20939 0.11197 0.00914  0.02238  0.00183  201 HEC A NB  
3564 C  C1B . HEC C .   ? 0.09450 0.23810 0.09495 0.00642  -0.01394 0.02824  201 HEC A C1B 
3565 C  C2B . HEC C .   ? 0.13096 0.22093 0.11209 0.00704  -0.00178 0.00573  201 HEC A C2B 
3566 C  C3B . HEC C .   ? 0.11742 0.24353 0.11008 -0.00704 -0.02523 0.01222  201 HEC A C3B 
3567 C  C4B . HEC C .   ? 0.09350 0.24613 0.09239 0.00324  -0.02754 0.01695  201 HEC A C4B 
3568 C  CMB . HEC C .   ? 0.08700 0.24565 0.11736 0.01850  0.00075  -0.00222 201 HEC A CMB 
3569 C  CAB . HEC C .   ? 0.09850 0.28029 0.11680 0.00327  -0.01219 0.03364  201 HEC A CAB 
3570 C  CBB . HEC C .   ? 0.08474 0.27572 0.15446 0.00414  0.00099  0.03168  201 HEC A CBB 
3571 N  NC  . HEC C .   ? 0.09935 0.25972 0.11035 -0.00896 0.02480  -0.01739 201 HEC A NC  
3572 C  C1C . HEC C .   ? 0.10947 0.26411 0.10038 -0.00585 -0.00547 -0.00258 201 HEC A C1C 
3573 C  C2C . HEC C .   ? 0.17721 0.25403 0.09511 0.01023  0.00601  -0.01120 201 HEC A C2C 
3574 C  C3C . HEC C .   ? 0.19326 0.25506 0.08460 0.02814  0.01549  -0.03558 201 HEC A C3C 
3575 C  C4C . HEC C .   ? 0.11143 0.25714 0.08836 0.00003  -0.00549 -0.01911 201 HEC A C4C 
3576 C  CMC . HEC C .   ? 0.19499 0.27307 0.09597 0.01890  0.00692  0.00756  201 HEC A CMC 
3577 C  CAC . HEC C .   ? 0.19249 0.27264 0.08679 0.04185  0.03791  -0.00624 201 HEC A CAC 
3578 C  CBC . HEC C .   ? 0.18459 0.27884 0.08936 0.01318  0.03228  -0.00807 201 HEC A CBC 
3579 N  ND  . HEC C .   ? 0.06843 0.24359 0.11820 0.00013  -0.00597 0.00151  201 HEC A ND  
3580 C  C1D . HEC C .   ? 0.08048 0.24630 0.10490 0.00058  0.02027  -0.02494 201 HEC A C1D 
3581 C  C2D . HEC C .   ? 0.13148 0.24283 0.10538 -0.00362 0.00327  -0.03318 201 HEC A C2D 
3582 C  C3D . HEC C .   ? 0.10013 0.23487 0.10646 -0.00543 0.01964  -0.02431 201 HEC A C3D 
3583 C  C4D . HEC C .   ? 0.12639 0.23292 0.09250 -0.00816 -0.01296 -0.02100 201 HEC A C4D 
3584 C  CMD . HEC C .   ? 0.13916 0.23169 0.12324 0.00630  0.01816  -0.01488 201 HEC A CMD 
3585 C  CAD . HEC C .   ? 0.15038 0.23966 0.11066 0.00527  -0.00603 -0.01933 201 HEC A CAD 
3586 C  CBD . HEC C .   ? 0.13280 0.24925 0.13769 -0.00968 0.01313  -0.01162 201 HEC A CBD 
3587 C  CGD . HEC C .   ? 0.13309 0.23662 0.12009 0.01583  0.01555  -0.01800 201 HEC A CGD 
3588 O  O1D . HEC C .   ? 0.13084 0.23019 0.14630 0.01046  -0.02100 -0.00832 201 HEC A O1D 
3589 O  O2D . HEC C .   ? 0.14337 0.23150 0.15801 0.00079  -0.00669 -0.01195 201 HEC A O2D 
3622 C  C1  . EOH D .   ? 0.41541 0.48406 0.51105 0.00601  -0.06876 -0.00905 202 EOH A C1  
3623 C  C2  . EOH D .   ? 0.44238 0.46909 0.50594 0.03846  -0.07212 -0.00291 202 EOH A C2  
3624 O  O   . EOH D .   ? 0.41561 0.49139 0.51755 -0.00487 -0.05065 0.00051  202 EOH A O   
3631 FE FE  . HEC E .   ? 0.10767 0.38761 0.09962 -0.03410 0.00002  -0.01586 201 HEC B FE  
3632 C  CHA . HEC E .   ? 0.11701 0.38484 0.11325 -0.03283 0.01719  -0.02107 201 HEC B CHA 
3633 C  CHB . HEC E .   ? 0.09329 0.33597 0.08771 0.01044  -0.00488 0.00915  201 HEC B CHB 
3634 C  CHC . HEC E .   ? 0.15766 0.35660 0.09858 -0.01165 0.02512  -0.00272 201 HEC B CHC 
3635 C  CHD . HEC E .   ? 0.14113 0.38209 0.10429 -0.05746 0.01469  -0.01571 201 HEC B CHD 
3636 N  NA  . HEC E .   ? 0.09501 0.37925 0.09450 -0.00662 -0.00013 0.00339  201 HEC B NA  
3637 C  C1A . HEC E .   ? 0.10011 0.38294 0.10142 -0.02444 0.00370  -0.02894 201 HEC B C1A 
3638 C  C2A . HEC E .   ? 0.09296 0.36502 0.09348 -0.01743 0.00083  -0.01648 201 HEC B C2A 
3639 C  C3A . HEC E .   ? 0.11014 0.36581 0.09187 -0.01361 -0.00101 -0.00558 201 HEC B C3A 
3640 C  C4A . HEC E .   ? 0.08967 0.35731 0.08969 -0.00841 0.00008  -0.00088 201 HEC B C4A 
3641 C  CMA . HEC E .   ? 0.12505 0.35337 0.08911 -0.01718 0.00340  -0.00629 201 HEC B CMA 
3642 C  CAA . HEC E .   ? 0.11990 0.39021 0.10524 -0.01351 0.01008  -0.02994 201 HEC B CAA 
3643 C  CBA . HEC E .   ? 0.10702 0.40662 0.10781 0.03024  -0.00393 -0.01347 201 HEC B CBA 
3644 C  CGA . HEC E .   ? 0.10083 0.40172 0.10169 0.00701  0.00017  -0.00812 201 HEC B CGA 
3645 O  O1A . HEC E .   ? 0.11652 0.42260 0.10986 0.00191  -0.00635 -0.01170 201 HEC B O1A 
3646 O  O2A . HEC E .   ? 0.12383 0.43451 0.12639 0.02766  -0.01529 -0.02086 201 HEC B O2A 
3647 N  NB  . HEC E .   ? 0.11318 0.34021 0.10196 -0.03940 -0.01549 -0.01124 201 HEC B NB  
3648 C  C1B . HEC E .   ? 0.14517 0.33105 0.08696 0.01106  -0.01577 -0.00443 201 HEC B C1B 
3649 C  C2B . HEC E .   ? 0.12201 0.33124 0.09165 -0.01828 -0.01721 -0.00560 201 HEC B C2B 
3650 C  C3B . HEC E .   ? 0.09215 0.33732 0.10186 -0.01421 -0.01034 -0.00730 201 HEC B C3B 
3651 C  C4B . HEC E .   ? 0.09439 0.34871 0.09007 -0.00941 -0.00424 -0.00273 201 HEC B C4B 
3652 C  CMB . HEC E .   ? 0.10078 0.35263 0.09306 -0.01865 0.00603  0.00953  201 HEC B CMB 
3653 C  CAB . HEC E .   ? 0.11207 0.34176 0.10460 -0.01829 -0.02192 0.00518  201 HEC B CAB 
3654 C  CBB . HEC E .   ? 0.09369 0.34290 0.10438 -0.01800 -0.01089 0.00118  201 HEC B CBB 
3655 N  NC  . HEC E .   ? 0.12657 0.37313 0.09635 -0.02067 0.00200  0.02225  201 HEC B NC  
3656 C  C1C . HEC E .   ? 0.13055 0.36379 0.09466 -0.04674 0.00675  -0.00149 201 HEC B C1C 
3657 C  C2C . HEC E .   ? 0.12624 0.38344 0.10879 -0.07586 0.00966  -0.02414 201 HEC B C2C 
3658 C  C3C . HEC E .   ? 0.15482 0.38632 0.13051 -0.07742 0.03273  -0.01483 201 HEC B C3C 
3659 C  C4C . HEC E .   ? 0.14281 0.37609 0.09844 -0.02939 0.01100  -0.01921 201 HEC B C4C 
3660 C  CMC . HEC E .   ? 0.16220 0.40806 0.10731 -0.07146 0.00193  -0.01070 201 HEC B CMC 
3661 C  CAC . HEC E .   ? 0.15646 0.43112 0.11659 -0.10174 0.00337  -0.00617 201 HEC B CAC 
3662 C  CBC . HEC E .   ? 0.22793 0.44237 0.11799 -0.08177 0.00480  0.00497  201 HEC B CBC 
3663 N  ND  . HEC E .   ? 0.12052 0.40084 0.10742 -0.05391 -0.00441 -0.00849 201 HEC B ND  
3664 C  C1D . HEC E .   ? 0.15162 0.39824 0.10489 -0.04597 -0.00284 -0.02343 201 HEC B C1D 
3665 C  C2D . HEC E .   ? 0.20480 0.42294 0.11664 -0.07402 -0.01279 -0.01876 201 HEC B C2D 
3666 C  C3D . HEC E .   ? 0.13697 0.40994 0.12347 -0.04357 -0.01908 -0.01870 201 HEC B C3D 
3667 C  C4D . HEC E .   ? 0.11522 0.39454 0.10878 -0.01961 -0.00836 -0.02562 201 HEC B C4D 
3668 C  CMD . HEC E .   ? 0.21255 0.43598 0.12920 -0.12485 0.02144  -0.03272 201 HEC B CMD 
3669 C  CAD . HEC E .   ? 0.16464 0.42081 0.13768 -0.03653 -0.03505 -0.02990 201 HEC B CAD 
3670 C  CBD . HEC E .   ? 0.15793 0.43085 0.12259 -0.05105 -0.01912 -0.01535 201 HEC B CBD 
3671 C  CGD . HEC E .   ? 0.14314 0.43392 0.13790 -0.03951 -0.02353 -0.02644 201 HEC B CGD 
3672 O  O1D . HEC E .   ? 0.16651 0.46650 0.15252 -0.04303 -0.03135 -0.03512 201 HEC B O1D 
3673 O  O2D . HEC E .   ? 0.17444 0.44359 0.15893 -0.08164 -0.01002 -0.04506 201 HEC B O2D 
3706 O  O   . HOH F .   ? 0.20789 0.65957 0.30918 0.11506  -0.04020 -0.08381 301 HOH A O   
3707 O  O   . HOH F .   ? 0.48353 0.66487 0.39066 0.20705  -0.18972 -0.11846 302 HOH A O   
3708 O  O   . HOH F .   ? 0.28313 0.43792 0.54102 -0.04783 -0.07803 0.05345  303 HOH A O   
3709 O  O   . HOH F .   ? 0.87838 0.45939 0.58379 -0.23993 0.36278  -0.15580 304 HOH A O   
3710 O  O   . HOH F .   ? 0.34000 0.87153 0.24030 0.12229  -0.03431 0.01695  305 HOH A O   
3711 O  O   . HOH F .   ? 0.34469 0.49043 0.39145 0.03989  0.11222  0.02628  306 HOH A O   
3712 O  O   . HOH F .   ? 0.31207 0.33327 0.18690 -0.00305 0.06707  -0.01848 307 HOH A O   
3713 O  O   . HOH F .   ? 0.73558 0.63688 0.36024 -0.22583 0.06126  0.09284  308 HOH A O   
3714 O  O   . HOH F .   ? 0.58296 0.45747 0.33037 0.10137  -0.00555 -0.02690 309 HOH A O   
3715 O  O   . HOH F .   ? 0.37095 0.80279 0.44917 0.15106  -0.03427 -0.19634 310 HOH A O   
3716 O  O   . HOH F .   ? 0.37393 0.83026 0.48030 -0.02290 -0.18992 0.13496  311 HOH A O   
3717 O  O   . HOH F .   ? 0.77830 0.41214 0.32126 -0.10387 -0.16377 0.09839  312 HOH A O   
3718 O  O   . HOH F .   ? 0.17729 0.63102 0.45667 0.03882  0.04614  0.01966  313 HOH A O   
3719 O  O   . HOH F .   ? 0.86011 0.51437 0.58245 -0.13268 -0.17818 0.21859  314 HOH A O   
3720 O  O   . HOH F .   ? 0.35586 0.34560 0.22288 -0.08886 0.04293  -0.04033 315 HOH A O   
3721 O  O   . HOH F .   ? 0.44676 0.49833 0.26916 0.23242  0.10096  0.01084  316 HOH A O   
3722 O  O   . HOH F .   ? 0.29942 0.45244 0.21368 -0.09423 0.08225  -0.01835 317 HOH A O   
3723 O  O   . HOH F .   ? 0.47669 0.60280 0.33733 0.19792  -0.15035 -0.17519 318 HOH A O   
3724 O  O   . HOH F .   ? 0.14070 0.27341 0.14862 -0.00714 -0.01811 -0.01969 319 HOH A O   
3725 O  O   . HOH F .   ? 0.76075 0.34984 0.41165 0.11908  -0.21119 -0.14471 320 HOH A O   
3726 O  O   . HOH F .   ? 0.28274 0.45126 0.53403 0.07662  -0.14343 -0.09864 321 HOH A O   
3727 O  O   . HOH F .   ? 0.30514 0.70344 0.23904 0.05478  0.03278  0.05869  322 HOH A O   
3728 O  O   . HOH F .   ? 0.36223 1.11916 0.33135 0.21467  -0.04171 -0.11607 323 HOH A O   
3729 O  O   . HOH F .   ? 0.23486 0.37224 0.82196 -0.03344 -0.09478 -0.04387 324 HOH A O   
3730 O  O   . HOH F .   ? 0.34478 0.29469 0.25145 -0.03217 -0.08199 -0.02606 325 HOH A O   
3731 O  O   . HOH F .   ? 0.25515 0.28003 0.27303 -0.04618 -0.00493 -0.02446 326 HOH A O   
3732 O  O   A HOH F .   ? 0.20934 0.47290 0.18036 0.09921  0.00443  0.05268  327 HOH A O   
3733 O  O   B HOH F .   ? 0.14285 0.52534 0.28615 0.00163  0.01896  -0.09595 327 HOH A O   
3734 O  O   . HOH F .   ? 0.24858 0.43849 0.41471 -0.03477 -0.09368 -0.01843 328 HOH A O   
3735 O  O   . HOH F .   ? 0.21753 0.26118 0.21397 -0.04901 -0.01405 0.01260  329 HOH A O   
3736 O  O   . HOH F .   ? 0.19038 0.32368 0.21776 0.02008  -0.01252 -0.00411 330 HOH A O   
3737 O  O   . HOH F .   ? 0.17939 0.31052 0.27067 -0.00875 -0.01020 -0.02782 331 HOH A O   
3738 O  O   . HOH F .   ? 0.17525 0.30919 0.15216 0.03142  0.01994  0.01244  332 HOH A O   
3739 O  O   . HOH F .   ? 0.41401 0.79935 0.31857 -0.25821 0.09691  -0.06707 333 HOH A O   
3740 O  O   . HOH F .   ? 0.50737 0.36014 0.16415 0.06827  -0.08446 -0.04888 334 HOH A O   
3741 O  O   . HOH F .   ? 0.48265 0.38851 0.48346 0.16888  0.26607  0.14707  335 HOH A O   
3742 O  O   . HOH F .   ? 0.44702 0.62479 0.29005 -0.18712 0.07188  -0.11982 336 HOH A O   
3743 O  O   . HOH F .   ? 0.31752 0.52142 0.22947 0.13966  -0.09713 -0.05742 337 HOH A O   
3744 O  O   . HOH F .   ? 0.15677 0.50387 0.32132 0.00868  -0.01252 -0.13986 338 HOH A O   
3745 O  O   . HOH F .   ? 0.18855 0.47363 0.19882 0.01635  0.02973  -0.01440 339 HOH A O   
3746 O  O   . HOH F .   ? 0.37576 0.53996 0.17216 0.14925  -0.04121 -0.06273 340 HOH A O   
3747 O  O   . HOH F .   ? 0.13143 0.42775 0.11415 -0.02612 -0.01242 0.00802  341 HOH A O   
3748 O  O   . HOH F .   ? 0.18477 0.62359 0.35764 0.07518  -0.00229 0.09288  342 HOH A O   
3749 O  O   . HOH F .   ? 0.14984 0.41493 0.28149 0.01694  -0.01024 0.01871  343 HOH A O   
3750 O  O   . HOH F .   ? 0.20154 0.35677 0.15001 0.03102  0.04853  0.01462  344 HOH A O   
3751 O  O   . HOH F .   ? 0.57717 0.72803 0.67741 -0.33096 0.11803  -0.16655 345 HOH A O   
3752 O  O   . HOH F .   ? 0.15385 0.24142 0.15988 0.00586  -0.01897 0.00161  346 HOH A O   
3753 O  O   . HOH F .   ? 0.51971 0.57740 0.20214 -0.00303 0.14685  0.00541  347 HOH A O   
3754 O  O   . HOH F .   ? 0.19751 0.29863 0.17824 0.00158  -0.03621 -0.02473 348 HOH A O   
3755 O  O   . HOH F .   ? 0.38127 0.33974 0.44215 0.08809  -0.16941 -0.06858 349 HOH A O   
3756 O  O   . HOH F .   ? 0.29590 0.31289 0.29180 -0.06641 -0.15667 0.05978  350 HOH A O   
3757 O  O   . HOH F .   ? 0.15552 0.31608 0.18969 -0.00619 0.00045  -0.00447 351 HOH A O   
3758 O  O   . HOH F .   ? 0.25259 0.26772 0.20005 0.00524  -0.06711 0.00521  352 HOH A O   
3759 O  O   . HOH F .   ? 0.34637 0.50722 0.83759 -0.07311 0.04529  -0.06451 353 HOH A O   
3760 O  O   . HOH F .   ? 0.51154 0.46973 0.55593 0.05319  0.04069  0.20641  354 HOH A O   
3761 O  O   . HOH F .   ? 0.18542 0.40703 0.31108 0.02116  0.00801  -0.05670 355 HOH A O   
3762 O  O   . HOH F .   ? 0.33993 0.56757 0.42356 -0.01026 -0.03490 -0.07379 356 HOH A O   
3763 O  O   . HOH F .   ? 0.23156 0.46043 0.72854 0.10679  0.02106  0.08282  357 HOH A O   
3764 O  O   . HOH F .   ? 0.31564 0.60293 0.60189 0.13340  0.18129  0.21047  358 HOH A O   
3765 O  O   . HOH F .   ? 0.34698 0.46126 0.37685 -0.05153 0.06946  -0.04899 359 HOH A O   
3766 O  O   . HOH F .   ? 0.43337 0.45248 0.41963 -0.11667 -0.01012 0.20283  360 HOH A O   
3767 O  O   . HOH F .   ? 0.53776 0.64616 0.60714 -0.10892 -0.01843 0.21707  361 HOH A O   
3768 O  O   . HOH F .   ? 0.14065 0.29672 0.17050 0.00941  -0.00174 0.00795  362 HOH A O   
3769 O  O   . HOH F .   ? 0.17381 0.29735 0.18547 0.00394  0.00788  -0.00566 363 HOH A O   
3770 O  O   . HOH F .   ? 0.14696 0.28738 0.12662 -0.02036 -0.02694 -0.01207 364 HOH A O   
3771 O  O   . HOH F .   ? 0.41686 0.69831 0.42861 0.12885  0.21382  0.09490  365 HOH A O   
3772 O  O   . HOH F .   ? 0.36126 0.60577 0.29951 0.14593  -0.10200 -0.06198 366 HOH A O   
3773 O  O   . HOH F .   ? 0.15225 0.43923 0.12817 -0.05254 0.00943  0.02806  367 HOH A O   
3774 O  O   . HOH F .   ? 0.16052 0.41153 0.26529 -0.03671 0.05200  0.01360  368 HOH A O   
3775 O  O   . HOH F .   ? 0.43860 0.47748 0.42769 -0.04130 0.14113  0.03196  369 HOH A O   
3776 O  O   . HOH F .   ? 0.19877 0.49170 0.62596 0.00457  0.04385  -0.14427 370 HOH A O   
3777 O  O   . HOH F .   ? 0.33833 0.89205 0.52820 0.07965  -0.08651 0.15198  371 HOH A O   
3778 O  O   . HOH F .   ? 0.41061 0.58004 0.29770 0.07081  -0.11019 0.08256  372 HOH A O   
3779 O  O   . HOH F .   ? 0.28461 0.51524 0.21087 0.15611  -0.08081 -0.06013 373 HOH A O   
3780 O  O   . HOH F .   ? 0.20446 0.41518 0.13304 0.02947  0.02757  -0.01026 374 HOH A O   
3781 O  O   . HOH F .   ? 0.73958 0.36909 0.52923 -0.01834 -0.22392 0.02391  375 HOH A O   
3782 O  O   . HOH F .   ? 0.33667 0.52971 0.24467 0.18181  -0.06666 -0.02227 376 HOH A O   
3783 O  O   . HOH F .   ? 0.21258 0.56282 0.51268 -0.02690 0.01208  -0.29481 377 HOH A O   
3784 O  O   . HOH F .   ? 0.77362 0.35493 0.26819 0.04684  -0.14551 0.05152  378 HOH A O   
3785 O  O   . HOH F .   ? 0.10159 0.27452 0.14909 0.00158  -0.00279 -0.00827 379 HOH A O   
3786 O  O   . HOH F .   ? 0.20985 0.38717 0.24566 0.00966  0.05734  0.00544  380 HOH A O   
3787 O  O   . HOH F .   ? 0.20616 0.57034 0.42089 -0.11704 -0.01134 -0.11508 381 HOH A O   
3788 O  O   . HOH F .   ? 0.21173 0.33962 0.18078 -0.00478 0.01945  -0.01173 382 HOH A O   
3789 O  O   . HOH F .   ? 0.17684 0.22441 0.25987 0.01843  0.03205  -0.01469 383 HOH A O   
3790 O  O   . HOH F .   ? 0.18505 0.44254 0.18160 0.04447  -0.00570 -0.01977 384 HOH A O   
3791 O  O   . HOH F .   ? 0.23331 0.41282 0.22312 -0.01506 0.02701  0.09314  385 HOH A O   
3792 O  O   . HOH F .   ? 0.65362 0.51171 0.30441 -0.19389 0.19571  -0.06733 386 HOH A O   
3793 O  O   . HOH F .   ? 0.26089 0.27931 0.19500 0.03353  -0.00187 -0.03873 387 HOH A O   
3794 O  O   A HOH F .   ? 0.31907 0.31909 0.21774 0.03801  -0.10667 -0.03949 388 HOH A O   
3795 O  O   B HOH F .   ? 0.39800 0.24380 0.49916 0.00444  -0.19756 -0.10605 388 HOH A O   
3796 O  O   . HOH F .   ? 0.84576 0.37090 0.40381 -0.03816 0.19469  -0.13363 389 HOH A O   
3797 O  O   . HOH F .   ? 0.17615 0.27768 0.22518 -0.02302 0.01093  0.04287  390 HOH A O   
3798 O  O   . HOH F .   ? 0.34054 0.71515 0.50497 0.04197  -0.09296 0.27566  391 HOH A O   
3799 O  O   . HOH F .   ? 0.31667 0.72818 0.25653 -0.04518 -0.09062 0.01255  392 HOH A O   
3800 O  O   . HOH F .   ? 0.23990 0.53010 0.20831 -0.02625 0.03567  0.04811  393 HOH A O   
3801 O  O   . HOH F .   ? 0.17870 0.54263 0.22916 -0.02367 0.05469  -0.08421 394 HOH A O   
3802 O  O   . HOH F .   ? 0.24987 0.39510 0.28701 -0.02654 -0.08295 0.00083  395 HOH A O   
3803 O  O   . HOH F .   ? 0.61190 0.71076 0.24482 0.10069  0.10165  -0.03774 396 HOH A O   
3804 O  O   . HOH F .   ? 0.25006 0.56760 0.19330 -0.09236 0.02870  -0.01702 397 HOH A O   
3805 O  O   . HOH F .   ? 0.22394 0.45944 0.25389 0.01825  -0.05207 -0.02668 398 HOH A O   
3806 O  O   . HOH F .   ? 0.33553 0.53208 0.23656 -0.00973 -0.03565 0.05474  399 HOH A O   
3807 O  O   . HOH F .   ? 0.81429 0.42811 0.39017 -0.13973 0.00470  -0.01061 400 HOH A O   
3808 O  O   . HOH F .   ? 0.24412 0.27832 0.18097 -0.01936 0.00366  -0.01085 401 HOH A O   
3809 O  O   . HOH F .   ? 0.40928 0.31136 0.29950 0.01246  0.01847  0.05603  402 HOH A O   
3810 O  O   . HOH F .   ? 0.47108 0.51606 0.51270 0.16211  -0.11687 -0.16682 403 HOH A O   
3811 O  O   . HOH F .   ? 0.44491 0.48253 0.42990 0.09263  -0.11138 0.08996  404 HOH A O   
3812 O  O   . HOH F .   ? 0.46369 0.40224 0.23931 0.18799  0.05631  -0.03287 405 HOH A O   
3813 O  O   . HOH F .   ? 0.19179 0.51737 0.34326 -0.01362 -0.08209 0.12471  406 HOH A O   
3814 O  O   . HOH F .   ? 0.26272 0.52422 0.19229 -0.00219 0.01649  -0.01061 407 HOH A O   
3815 O  O   . HOH F .   ? 0.47028 0.68268 0.23168 0.17185  -0.02019 0.09869  408 HOH A O   
3816 O  O   . HOH F .   ? 0.22328 0.60352 0.19419 0.07722  -0.04690 -0.00112 409 HOH A O   
3817 O  O   . HOH F .   ? 0.41502 0.38928 0.41872 -0.07277 0.22993  -0.02480 410 HOH A O   
3818 O  O   . HOH F .   ? 0.23620 0.28465 0.27781 -0.01292 0.03345  0.05057  411 HOH A O   
3819 O  O   . HOH F .   ? 0.51366 0.70667 0.42819 0.30928  -0.14066 -0.04357 412 HOH A O   
3820 O  O   . HOH F .   ? 0.20784 0.32459 0.23769 0.00020  0.03363  -0.01589 413 HOH A O   
3821 O  O   . HOH F .   ? 0.42473 0.30659 0.28201 0.03926  -0.13394 -0.08886 414 HOH A O   
3822 O  O   . HOH F .   ? 0.93545 0.59906 0.35439 -0.04448 0.06563  0.18515  415 HOH A O   
3823 O  O   . HOH F .   ? 0.16321 0.38862 0.53046 0.07066  -0.05839 -0.01083 416 HOH A O   
3824 O  O   . HOH F .   ? 0.47949 0.63421 0.22102 0.18882  -0.08185 -0.00919 417 HOH A O   
3825 O  O   . HOH F .   ? 0.43912 0.95755 0.54498 0.19766  -0.01157 -0.26932 418 HOH A O   
3826 O  O   . HOH F .   ? 0.20207 0.63107 0.36928 0.03536  0.07733  0.00309  419 HOH A O   
3827 O  O   . HOH F .   ? 0.54531 0.69212 0.30243 0.16343  0.09514  -0.13050 420 HOH A O   
3828 O  O   . HOH F .   ? 0.61254 0.80476 0.28232 0.29003  0.08442  0.02042  421 HOH A O   
3829 O  O   . HOH F .   ? 0.62128 0.49755 0.45304 0.04612  -0.05474 0.04575  422 HOH A O   
3830 O  O   . HOH F .   ? 0.17064 0.49942 0.47533 0.07632  0.00633  0.01484  423 HOH A O   
3831 O  O   . HOH F .   ? 0.34343 0.68633 0.46304 -0.19943 0.03584  -0.07656 424 HOH A O   
3832 O  O   . HOH F .   ? 0.32344 0.35028 0.96474 0.03348  -0.18743 -0.18415 425 HOH A O   
3833 O  O   . HOH F .   ? 0.52743 0.51259 0.43395 -0.04337 0.12821  -0.01906 426 HOH A O   
3834 O  O   . HOH F .   ? 0.53537 0.81635 0.44318 0.30387  0.12102  0.03011  427 HOH A O   
3835 O  O   . HOH F .   ? 0.25226 0.60543 0.18275 0.00884  -0.01006 -0.07175 428 HOH A O   
3836 O  O   . HOH F .   ? 0.36884 0.75964 0.56585 0.08946  -0.03739 0.15131  429 HOH A O   
3837 O  O   . HOH F .   ? 0.48370 0.85951 0.27205 0.01839  -0.01355 -0.16766 430 HOH A O   
3838 O  O   . HOH F .   ? 0.66959 0.74024 0.47036 -0.12753 0.04725  0.19184  431 HOH A O   
3839 O  O   . HOH F .   ? 0.35875 0.53483 0.68868 0.16622  -0.20816 -0.13432 432 HOH A O   
3840 O  O   . HOH F .   ? 0.72804 0.49958 0.31108 0.17231  -0.13497 -0.15442 433 HOH A O   
3841 O  O   . HOH F .   ? 0.41730 0.83884 0.34955 -0.07807 0.02695  -0.04946 434 HOH A O   
3842 O  O   . HOH F .   ? 0.28402 0.70882 0.54232 -0.10337 0.16527  0.01933  435 HOH A O   
3843 O  O   . HOH F .   ? 0.71552 0.65733 0.61643 -0.15144 -0.04712 0.22672  436 HOH A O   
3844 O  O   . HOH F .   ? 0.53231 0.71769 0.66738 0.10801  0.00005  -0.34575 437 HOH A O   
3845 O  O   . HOH F .   ? 0.44165 0.40223 0.81106 0.03843  0.09691  0.13874  438 HOH A O   
3846 O  O   . HOH F .   ? 0.19362 0.29320 0.55165 -0.00841 0.00246  -0.04427 439 HOH A O   
3847 O  O   . HOH F .   ? 0.89382 0.40348 0.61320 -0.19208 0.06509  0.03952  440 HOH A O   
3848 O  O   . HOH F .   ? 0.53056 0.71749 0.35334 0.34012  0.07491  0.15101  441 HOH A O   
3849 O  O   . HOH F .   ? 0.59415 0.61353 0.68799 -0.11982 0.21127  0.04869  442 HOH A O   
3850 O  O   . HOH F .   ? 0.30698 0.79231 0.73634 -0.09536 -0.19402 0.06146  443 HOH A O   
3851 O  O   . HOH F .   ? 0.57223 0.46410 0.28942 -0.11244 0.09304  0.00711  444 HOH A O   
3852 O  O   . HOH F .   ? 0.37636 0.53816 0.27866 -0.11489 -0.01455 0.09026  445 HOH A O   
3853 O  O   . HOH F .   ? 0.53387 0.65931 0.59261 -0.18912 0.13959  -0.30755 446 HOH A O   
3854 O  O   . HOH F .   ? 0.56533 0.65187 0.84822 -0.27187 -0.08026 0.22642  447 HOH A O   
3855 O  O   . HOH F .   ? 0.50043 0.49905 0.32207 -0.02363 0.15539  0.05870  448 HOH A O   
3856 O  O   . HOH F .   ? 0.36494 0.59264 0.20976 -0.07095 0.06299  -0.01751 449 HOH A O   
3857 O  O   . HOH F .   ? 0.52484 0.55301 0.30413 0.00299  0.04904  -0.06396 450 HOH A O   
3858 O  O   . HOH F .   ? 0.32801 0.50443 0.49402 -0.03528 -0.07124 0.10578  451 HOH A O   
3859 O  O   . HOH F .   ? 0.77044 0.79118 0.49514 0.14463  0.23730  0.06293  452 HOH A O   
3860 O  O   . HOH F .   ? 0.38576 0.45514 0.25471 -0.00161 0.10933  -0.04789 453 HOH A O   
3861 O  O   . HOH F .   ? 0.60345 0.83954 0.55709 -0.15585 0.19829  -0.06477 454 HOH A O   
3862 O  O   . HOH F .   ? 0.35160 0.44793 0.50375 0.04913  0.13274  0.15535  455 HOH A O   
3863 O  O   . HOH G .   ? 0.59647 0.86593 0.45503 0.40543  -0.12508 -0.16544 301 HOH B O   
3864 O  O   . HOH G .   ? 0.42782 0.71465 0.28110 0.02295  -0.04523 0.14419  302 HOH B O   
3865 O  O   . HOH G .   ? 0.59703 0.40096 0.57272 0.04471  0.26343  0.02640  303 HOH B O   
3866 O  O   . HOH G .   ? 0.54767 0.67916 0.39653 -0.01546 -0.02686 -0.15468 304 HOH B O   
3867 O  O   . HOH G .   ? 0.60965 0.59979 0.30322 0.28779  -0.03431 0.08557  305 HOH B O   
3868 O  O   . HOH G .   ? 0.33817 0.35999 1.16689 0.01913  0.03496  -0.10109 306 HOH B O   
3869 O  O   . HOH G .   ? 0.63845 0.56495 0.38938 -0.26519 -0.21637 0.06964  307 HOH B O   
3870 O  O   . HOH G .   ? 0.67544 0.69622 0.32954 -0.30325 0.06188  0.00311  308 HOH B O   
3871 O  O   . HOH G .   ? 0.39491 0.39539 1.09456 0.03956  -0.21772 -0.20128 309 HOH B O   
3872 O  O   . HOH G .   ? 0.13317 0.45866 0.12841 0.05556  -0.00950 -0.00290 310 HOH B O   
3873 O  O   . HOH G .   ? 0.42056 0.66807 0.26715 -0.23872 -0.06073 0.02178  311 HOH B O   
3874 O  O   . HOH G .   ? 0.29881 0.52959 0.21419 0.00962  0.04124  -0.05983 312 HOH B O   
3875 O  O   . HOH G .   ? 0.20368 0.41201 0.13031 0.02068  -0.02656 -0.02491 313 HOH B O   
3876 O  O   . HOH G .   ? 0.62214 0.41694 0.47803 0.04609  0.03700  0.01417  314 HOH B O   
3877 O  O   . HOH G .   ? 0.32754 0.81587 0.46838 0.14418  -0.14653 -0.13290 315 HOH B O   
3878 O  O   A HOH G .   ? 0.32955 0.50018 0.32965 -0.02774 -0.00599 -0.07631 316 HOH B O   
3879 O  O   B HOH G .   ? 0.48123 0.54148 0.18354 -0.08976 -0.06600 0.04534  316 HOH B O   
3880 O  O   . HOH G .   ? 0.51945 0.59731 0.52123 -0.04148 -0.15010 0.06880  317 HOH B O   
3881 O  O   . HOH G .   ? 0.31631 0.68644 0.42600 0.12863  0.09469  0.12626  318 HOH B O   
3882 O  O   . HOH G .   ? 0.47637 0.65736 0.33753 0.00932  0.23110  -0.01831 319 HOH B O   
3883 O  O   . HOH G .   ? 0.21179 0.53524 0.22777 0.03497  -0.08182 -0.04891 320 HOH B O   
3884 O  O   . HOH G .   ? 0.18529 0.63641 0.17353 -0.08885 0.01236  -0.03679 321 HOH B O   
3885 O  O   . HOH G .   ? 0.25038 0.42725 0.20208 0.01304  0.02856  -0.00872 322 HOH B O   
3886 O  O   . HOH G .   ? 0.23230 0.34972 0.16369 -0.00021 -0.01329 -0.02769 323 HOH B O   
3887 O  O   . HOH G .   ? 0.41326 0.82093 0.52140 0.22915  -0.18330 -0.14827 324 HOH B O   
3888 O  O   . HOH G .   ? 0.14769 0.43046 0.17135 0.00295  -0.04529 0.00257  325 HOH B O   
3889 O  O   . HOH G .   ? 0.32808 0.68815 0.53379 -0.03818 -0.23225 -0.02124 326 HOH B O   
3890 O  O   . HOH G .   ? 0.30092 0.49324 0.47134 0.00807  -0.11984 -0.12465 327 HOH B O   
3891 O  O   . HOH G .   ? 0.14849 0.44955 0.11572 0.06208  0.00261  0.00662  328 HOH B O   
3892 O  O   . HOH G .   ? 0.70580 0.65358 0.59856 -0.22742 0.22813  0.15288  329 HOH B O   
3893 O  O   . HOH G .   ? 0.52068 0.54490 0.32262 0.10604  -0.11073 -0.08486 330 HOH B O   
3894 O  O   . HOH G .   ? 0.61199 0.82641 0.27033 -0.18758 0.09409  -0.10197 331 HOH B O   
3895 O  O   . HOH G .   ? 0.42392 0.39136 0.46532 0.09878  0.16036  -0.00159 332 HOH B O   
3896 O  O   . HOH G .   ? 0.26302 0.79209 0.25452 0.04444  -0.05779 -0.05565 333 HOH B O   
3897 O  O   . HOH G .   ? 0.16720 0.55856 0.21871 -0.02700 0.04373  0.01171  334 HOH B O   
3898 O  O   B HOH G .   ? 0.11754 0.33826 0.21167 -0.00859 0.05627  0.04503  335 HOH B O   
3899 O  O   . HOH G .   ? 0.55247 0.41974 0.16617 -0.06852 -0.08007 -0.00922 336 HOH B O   
3900 O  O   . HOH G .   ? 0.24419 0.40630 0.27276 0.00601  -0.11983 0.00746  337 HOH B O   
3901 O  O   . HOH G .   ? 0.18527 0.51927 0.17910 -0.00209 -0.02195 -0.06267 338 HOH B O   
3902 O  O   . HOH G .   ? 0.48291 0.70463 0.60080 0.08232  -0.30942 -0.04703 339 HOH B O   
3903 O  O   . HOH G .   ? 0.42711 0.71543 0.24308 -0.20350 -0.06695 -0.00872 340 HOH B O   
3904 O  O   . HOH G .   ? 0.27889 0.57360 0.39697 -0.03486 -0.16879 0.06585  341 HOH B O   
3905 O  O   . HOH G .   ? 0.36760 0.43866 0.30938 0.11903  0.17821  0.06040  342 HOH B O   
3906 O  O   . HOH G .   ? 0.55293 0.75039 0.30337 -0.16739 -0.11437 0.11211  343 HOH B O   
3907 O  O   . HOH G .   ? 0.31974 0.74193 0.52816 0.11366  -0.14822 -0.12915 344 HOH B O   
3908 O  O   . HOH G .   ? 0.27620 0.53861 0.22450 0.08732  -0.05912 -0.11602 345 HOH B O   
3909 O  O   . HOH G .   ? 0.50728 0.45344 0.16149 0.16157  0.01088  0.00714  346 HOH B O   
3910 O  O   . HOH G .   ? 0.48102 0.66972 0.43819 -0.12626 -0.10910 0.10378  347 HOH B O   
3911 O  O   . HOH G .   ? 0.20817 0.42815 0.26163 0.07173  -0.07182 0.00840  348 HOH B O   
3912 O  O   . HOH G .   ? 0.55710 0.38724 0.25783 0.08702  -0.14448 -0.11720 349 HOH B O   
3913 O  O   . HOH G .   ? 0.17858 0.69317 0.19020 -0.02957 0.00321  -0.07519 350 HOH B O   
3914 O  O   . HOH G .   ? 0.12230 0.35513 0.10486 -0.01635 -0.02104 0.02843  351 HOH B O   
3915 O  O   A HOH G .   ? 0.21200 0.36740 0.17028 -0.00173 -0.01000 0.01072  352 HOH B O   
3916 O  O   . HOH G .   ? 0.45529 0.65575 0.31622 -0.04210 0.05393  -0.17313 353 HOH B O   
3917 O  O   . HOH G .   ? 0.22000 0.53761 0.20730 -0.01679 0.04161  0.06419  354 HOH B O   
3918 O  O   . HOH G .   ? 0.23787 0.56609 0.63736 -0.13358 -0.08043 0.09288  355 HOH B O   
3919 O  O   . HOH G .   ? 0.71524 0.51198 0.28405 -0.00601 -0.16088 0.10768  356 HOH B O   
3920 O  O   . HOH G .   ? 0.47188 0.66657 0.79209 -0.25317 0.18475  -0.16580 357 HOH B O   
3921 O  O   . HOH G .   ? 0.23892 0.46121 0.38773 0.01499  -0.00438 -0.07082 358 HOH B O   
3922 O  O   . HOH G .   ? 0.63538 0.52939 0.32894 0.05076  -0.05648 0.10615  359 HOH B O   
3923 O  O   . HOH G .   ? 0.28128 0.59625 0.50441 0.15127  0.02588  -0.12678 360 HOH B O   
3924 O  O   . HOH G .   ? 0.62188 0.41263 0.29314 -0.09780 -0.07418 0.06501  361 HOH B O   
3925 O  O   . HOH G .   ? 0.63112 0.54553 0.42530 0.26813  0.06357  -0.04364 362 HOH B O   
3926 O  O   . HOH G .   ? 0.32143 0.72732 0.34515 -0.08183 -0.06262 0.03513  363 HOH B O   
3927 O  O   . HOH G .   ? 0.33302 0.50081 0.48815 0.01774  -0.13097 0.09489  364 HOH B O   
3928 O  O   . HOH G .   ? 0.18632 0.47038 0.13516 -0.05199 -0.01111 -0.03983 365 HOH B O   
3929 O  O   . HOH G .   ? 0.31506 0.78539 0.49015 0.17640  -0.04869 -0.01684 366 HOH B O   
3930 O  O   . HOH G .   ? 0.25391 0.74407 0.66243 -0.08976 -0.11891 0.10304  367 HOH B O   
3931 O  O   . HOH G .   ? 0.72027 0.79769 0.65373 0.30397  0.20366  0.15439  368 HOH B O   
3932 O  O   . HOH G .   ? 0.14723 0.56234 0.19677 0.03578  0.00613  -0.03994 369 HOH B O   
3933 O  O   . HOH G .   ? 0.44525 0.54516 0.48207 0.06038  0.03384  -0.18203 370 HOH B O   
3934 O  O   . HOH G .   ? 0.13603 0.52737 0.19385 0.01037  -0.00482 -0.07120 371 HOH B O   
3935 O  O   . HOH G .   ? 0.24397 0.42645 0.28848 0.07072  0.13604  0.06492  372 HOH B O   
3936 O  O   . HOH G .   ? 0.24420 0.64174 0.20206 -0.03231 -0.01884 -0.06811 373 HOH B O   
3937 O  O   . HOH G .   ? 0.31293 0.50681 0.18805 -0.12069 0.01401  -0.05355 374 HOH B O   
3938 O  O   . HOH G .   ? 0.19929 0.64935 0.27188 -0.04617 0.05955  -0.02255 375 HOH B O   
3939 O  O   . HOH G .   ? 0.20547 0.71343 0.28997 0.03462  -0.04685 -0.09037 376 HOH B O   
3940 O  O   A HOH G .   ? 0.48089 0.46734 0.18744 -0.01122 0.12245  0.06115  377 HOH B O   
3941 O  O   B HOH G .   ? 0.38478 0.31874 0.14584 -0.02504 -0.00599 0.00410  377 HOH B O   
3942 O  O   . HOH G .   ? 0.22637 0.62322 0.29681 -0.08268 -0.03651 -0.02944 378 HOH B O   
3943 O  O   . HOH G .   ? 0.44846 0.46530 0.50405 0.08597  0.01025  -0.12873 379 HOH B O   
3944 O  O   . HOH G .   ? 0.24172 0.39819 0.34819 0.00560  -0.13510 -0.00849 380 HOH B O   
3945 O  O   . HOH G .   ? 0.21582 0.37714 0.29776 0.03752  -0.06263 0.05462  381 HOH B O   
3946 O  O   . HOH G .   ? 0.53284 0.52378 0.24403 0.17854  0.08329  0.01553  382 HOH B O   
3947 O  O   . HOH G .   ? 0.58702 0.47731 0.25536 0.16731  -0.06157 0.02149  383 HOH B O   
3948 O  O   . HOH G .   ? 0.47865 0.43792 0.21498 0.00628  -0.05868 0.06748  384 HOH B O   
3949 O  O   . HOH G .   ? 0.32298 0.68132 0.39952 0.02139  0.15548  -0.08717 385 HOH B O   
3950 O  O   . HOH G .   ? 0.59545 0.59016 0.69290 -0.33198 0.04464  0.11228  386 HOH B O   
3951 O  O   . HOH G .   ? 0.59895 0.39562 0.33343 0.02348  0.12269  0.02760  387 HOH B O   
3952 O  O   . HOH G .   ? 0.42815 0.77286 0.38259 -0.12310 0.14596  -0.15945 388 HOH B O   
3953 O  O   . HOH G .   ? 0.35356 0.53788 0.33873 0.06696  -0.18104 -0.10080 389 HOH B O   
3954 O  O   . HOH G .   ? 0.49268 0.90355 0.58805 0.24142  0.04934  0.31626  390 HOH B O   
3955 O  O   . HOH G .   ? 0.64939 0.43522 0.65723 -0.08013 0.04928  0.04458  391 HOH B O   
3956 O  O   . HOH G .   ? 0.25680 0.72603 0.34477 -0.01210 -0.03303 -0.04825 392 HOH B O   
3957 O  O   . HOH G .   ? 0.27687 0.77886 0.23572 -0.00947 0.04294  0.08588  393 HOH B O   
3958 O  O   . HOH G .   ? 0.49639 0.62759 0.34111 -0.09174 0.10883  -0.22179 394 HOH B O   
3959 O  O   . HOH G .   ? 0.58063 0.46314 0.78606 -0.01384 0.09941  0.24606  395 HOH B O   
3960 O  O   . HOH G .   ? 0.44480 0.53736 0.30594 -0.14616 -0.02895 0.00148  396 HOH B O   
3961 O  O   . HOH G .   ? 0.32683 0.50067 0.41147 0.11326  -0.13728 -0.10088 397 HOH B O   
3962 O  O   . HOH G .   ? 0.94721 0.51148 0.36091 0.02966  0.11313  0.06299  398 HOH B O   
3963 O  O   . HOH G .   ? 0.21501 0.59849 0.53046 -0.06372 0.01171  0.18248  399 HOH B O   
3964 O  O   . HOH G .   ? 0.32254 0.58481 0.25403 -0.07078 0.03147  -0.02842 400 HOH B O   
3965 O  O   . HOH G .   ? 0.23276 0.65223 0.26375 -0.05585 0.06222  -0.12140 401 HOH B O   
3966 O  O   . HOH G .   ? 0.55520 0.67135 0.64248 0.08441  0.29217  0.21849  402 HOH B O   
3967 O  O   . HOH G .   ? 0.27427 0.40633 0.13803 0.00350  0.07272  0.00307  403 HOH B O   
3968 O  O   . HOH G .   ? 0.34838 0.51779 0.40041 0.02843  -0.21811 -0.04120 404 HOH B O   
3969 O  O   . HOH G .   ? 0.83776 0.66363 0.40156 -0.36517 0.03861  -0.00361 405 HOH B O   
3970 O  O   . HOH G .   ? 0.59633 0.62602 0.47898 0.03056  -0.08538 0.18242  406 HOH B O   
3971 O  O   . HOH G .   ? 0.38810 0.47775 0.90095 0.01574  0.15516  0.04891  407 HOH B O   
3972 O  O   . HOH G .   ? 0.52930 0.64172 0.50590 0.00769  -0.12926 -0.04278 408 HOH B O   
3973 O  O   . HOH G .   ? 0.42505 0.62749 0.44547 -0.02012 -0.09693 -0.04515 409 HOH B O   
3974 O  O   . HOH G .   ? 0.74507 0.40136 0.29216 -0.03488 -0.18492 0.03915  410 HOH B O   
3975 O  O   . HOH G .   ? 0.48275 0.47477 0.30288 0.04311  -0.21456 -0.00094 411 HOH B O   
3976 O  O   . HOH G .   ? 0.50251 0.47985 0.48691 -0.18449 0.19984  -0.13104 412 HOH B O   
3977 O  O   . HOH G .   ? 0.43208 0.64635 0.21550 -0.11654 -0.04427 0.02627  413 HOH B O   
3978 O  O   . HOH G .   ? 0.84434 0.75137 0.33707 0.32998  0.07180  0.00704  414 HOH B O   
3979 O  O   . HOH G .   ? 0.47739 0.76635 0.52410 -0.06941 -0.11512 -0.02782 415 HOH B O   
3980 O  O   . HOH G .   ? 0.61838 0.77050 0.38508 -0.32789 -0.15162 0.16946  416 HOH B O   
3981 O  O   . HOH G .   ? 0.33456 0.42989 0.50687 -0.13059 0.16583  -0.21883 417 HOH B O   
3982 O  O   . HOH G .   ? 0.23784 0.44653 0.27511 -0.04833 -0.05937 0.06115  418 HOH B O   
3983 O  O   . HOH G .   ? 0.22089 0.43751 0.20181 0.04918  -0.04777 0.03439  419 HOH B O   
3984 O  O   . HOH G .   ? 0.36654 0.75039 0.75380 -0.02415 0.03388  0.12870  420 HOH B O   
3985 O  O   . HOH G .   ? 0.57902 0.65723 0.23795 0.01799  0.12521  -0.03141 421 HOH B O   
3986 O  O   . HOH G .   ? 0.45771 0.73642 0.31471 0.04999  -0.02742 -0.06404 422 HOH B O   
3987 O  O   . HOH G .   ? 0.61739 0.48416 0.68491 -0.06416 -0.04582 0.00142  423 HOH B O   
3988 O  O   . HOH G .   ? 0.83231 0.55141 0.32671 -0.02658 -0.12329 0.01408  424 HOH B O   
3989 O  O   . HOH G .   ? 0.35298 0.55789 0.55877 0.07253  -0.01757 0.10369  425 HOH B O   
3990 O  O   . HOH G .   ? 0.61788 0.50134 0.17433 0.00179  0.06651  -0.04046 426 HOH B O   
3991 O  O   . HOH G .   ? 0.35421 0.73986 0.56924 -0.03574 0.05146  -0.06487 427 HOH B O   
3992 O  O   . HOH G .   ? 0.56392 0.63371 0.71478 0.12286  0.02930  0.27541  428 HOH B O   
3993 O  O   . HOH G .   ? 0.43827 0.59791 0.37213 0.13666  -0.05664 -0.13312 429 HOH B O   
3994 O  O   . HOH G .   ? 0.46896 0.73919 0.56350 -0.07995 0.29463  0.01533  430 HOH B O   
3995 O  O   . HOH G .   ? 0.56102 0.52994 0.47782 0.10758  0.05048  0.08353  431 HOH B O   
3996 O  O   . HOH G .   ? 0.29430 0.72651 0.43154 0.00925  -0.04568 -0.13091 432 HOH B O   
3997 O  O   . HOH G .   ? 0.75206 0.70352 0.36016 0.17111  -0.13458 0.05228  433 HOH B O   
3998 O  O   . HOH G .   ? 0.45162 0.66638 0.42540 0.06190  -0.25221 0.03772  434 HOH B O   
3999 O  O   . HOH G .   ? 0.47022 1.03119 0.37121 0.13826  0.08055  -0.00612 435 HOH B O   
4000 O  O   . HOH G .   ? 0.44884 0.89549 0.46037 0.19135  -0.17929 -0.22678 436 HOH B O   
4001 O  O   . HOH G .   ? 0.24098 0.60777 0.35736 0.13921  0.04738  0.19942  437 HOH B O   
4002 O  O   . HOH G .   ? 0.41493 0.75721 0.35723 -0.00958 -0.09095 -0.07865 438 HOH B O   
4003 O  O   . HOH G .   ? 0.41648 0.49977 0.24792 -0.06974 -0.07627 0.04532  439 HOH B O   
4004 O  O   . HOH G .   ? 0.59634 1.03950 0.32814 0.05519  0.05430  -0.04643 440 HOH B O   
4005 O  O   . HOH G .   ? 0.92955 0.58392 0.28792 0.07062  0.03027  -0.06271 441 HOH B O   
4006 O  O   . HOH G .   ? 0.47107 0.63290 0.57063 -0.12752 -0.13467 0.02837  442 HOH B O   
4007 O  O   . HOH G .   ? 0.48813 0.38112 0.41748 -0.00898 0.09851  0.02656  443 HOH B O   
4008 O  O   . HOH G .   ? 0.38814 0.58175 0.30416 -0.06768 0.08199  0.05418  444 HOH B O   
4009 O  O   . HOH G .   ? 0.31296 0.90648 0.32708 0.17067  0.05501  0.18706  445 HOH B O   
4010 O  O   . HOH G .   ? 0.51216 0.91683 0.64097 0.08699  0.25432  -0.00595 446 HOH B O   
4011 O  O   . HOH G .   ? 0.36465 0.38572 0.90637 -0.08417 -0.24815 0.19284  447 HOH B O   
4012 O  O   . HOH G .   ? 0.63865 0.82956 0.33722 -0.14511 0.05464  -0.22568 448 HOH B O   
# 
