data_9FYJ
# 
_entry.id   9FYJ 
# 
_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   9FYJ         pdb_00009fyj 10.2210/pdb9fyj/pdb 
WWPDB D_1292139898 ?            ?                   
# 
_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       2025-03-12 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FYJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              derek.logan@biochemistry.lu.se 
_pdbx_contact_author.name_first         Derek 
_pdbx_contact_author.name_last          Logan 
_pdbx_contact_author.name_mi            T. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0098-8560 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Adrover Forteza, J.' 1 ?                   
'Puric, E.'           2 ?                   
'Nilsson, U.J.'       3 0000-0001-5815-9522 
'Anderluh, M.'        4 ?                   
'Logan, D.T.'         5 0000-0002-0098-8560 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3669 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                59 
_citation.page_last                 59 
_citation.title                     
'Nanomolar inhibitor of the galectin-8 N-terminal domain binds via a non-canonical cation-pi interaction.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42004-025-01458-6 
_citation.pdbx_database_id_PubMed   39994474 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Puric, E.'     1  0000-0003-0836-0548 
primary 'Hassan, M.'    2  ?                   
primary 'Sjovall, F.'   3  0009-0000-1602-0549 
primary 'Tomasic, T.'   4  0000-0001-5534-209X 
primary 'Pevec, M.'     5  0000-0001-5968-3895 
primary 'Lah, J.'       6  0000-0003-1021-3803 
primary 'Forteza, J.A.' 7  ?                   
primary 'Sundin, A.'    8  ?                   
primary 'Leffler, H.'   9  0000-0003-4482-8945 
primary 'Nilsson, U.J.' 10 0000-0001-5815-9522 
primary 'Logan, D.T.'   11 0000-0002-0098-8560 
primary 'Anderluh, M.'  12 0000-0003-1768-8246 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Isoform 1 of Galectin-8' 17281.807 2   ? ? ? ? 
2 non-polymer syn 
;2-[[(2~{R},3~{R},4~{S},5~{S},6~{R})-2-(3,4-dichlorophenyl)sulfanyl-6-(hydroxymethyl)-5-oxidanyl-3-prop-2-ynoxy-oxan-4-yl]oxymethyl]-3-methyl-benzimidazole-5-carboxylic acid
;
567.438   2   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION' 35.453    1   ? ? ? ? 
4 water       nat water 18.015    378 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Gal-8,Po66 carbohydrate-binding protein,Po66-CBP,Prostate carcinoma tumor antigen 1,PCTA-1' 
# 
_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       
;SLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNTLIN
EKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFSFSSD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNTLIN
EKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFSFSSD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;2-[[(2~{R},3~{R},4~{S},5~{S},6~{R})-2-(3,4-dichlorophenyl)sulfanyl-6-(hydroxymethyl)-5-oxidanyl-3-prop-2-ynoxy-oxan-4-yl]oxymethyl]-3-methyl-benzimidazole-5-carboxylic acid
;
A1IHE 
3 'CHLORIDE ION' CL    
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   LEU n 
1 3   ASN n 
1 4   ASN n 
1 5   LEU n 
1 6   GLN n 
1 7   ASN n 
1 8   ILE n 
1 9   ILE n 
1 10  TYR n 
1 11  ASN n 
1 12  PRO n 
1 13  VAL n 
1 14  ILE n 
1 15  PRO n 
1 16  PHE n 
1 17  VAL n 
1 18  GLY n 
1 19  THR n 
1 20  ILE n 
1 21  PRO n 
1 22  ASP n 
1 23  GLN n 
1 24  LEU n 
1 25  ASP n 
1 26  PRO n 
1 27  GLY n 
1 28  THR n 
1 29  LEU n 
1 30  ILE n 
1 31  VAL n 
1 32  ILE n 
1 33  ARG n 
1 34  GLY n 
1 35  HIS n 
1 36  VAL n 
1 37  PRO n 
1 38  SER n 
1 39  ASP n 
1 40  ALA n 
1 41  ASP n 
1 42  ARG n 
1 43  PHE n 
1 44  GLN n 
1 45  VAL n 
1 46  ASP n 
1 47  LEU n 
1 48  GLN n 
1 49  ASN n 
1 50  GLY n 
1 51  SER n 
1 52  SER n 
1 53  MET n 
1 54  LYS n 
1 55  PRO n 
1 56  ARG n 
1 57  ALA n 
1 58  ASP n 
1 59  VAL n 
1 60  ALA n 
1 61  PHE n 
1 62  HIS n 
1 63  PHE n 
1 64  ASN n 
1 65  PRO n 
1 66  ARG n 
1 67  PHE n 
1 68  LYS n 
1 69  ARG n 
1 70  ALA n 
1 71  GLY n 
1 72  CYS n 
1 73  ILE n 
1 74  VAL n 
1 75  CYS n 
1 76  ASN n 
1 77  THR n 
1 78  LEU n 
1 79  ILE n 
1 80  ASN n 
1 81  GLU n 
1 82  LYS n 
1 83  TRP n 
1 84  GLY n 
1 85  ARG n 
1 86  GLU n 
1 87  GLU n 
1 88  ILE n 
1 89  THR n 
1 90  TYR n 
1 91  ASP n 
1 92  THR n 
1 93  PRO n 
1 94  PHE n 
1 95  LYS n 
1 96  ARG n 
1 97  GLU n 
1 98  LYS n 
1 99  SER n 
1 100 PHE n 
1 101 GLU n 
1 102 ILE n 
1 103 VAL n 
1 104 ILE n 
1 105 MET n 
1 106 VAL n 
1 107 LEU n 
1 108 LYS n 
1 109 ASP n 
1 110 LYS n 
1 111 PHE n 
1 112 GLN n 
1 113 VAL n 
1 114 ALA n 
1 115 VAL n 
1 116 ASN n 
1 117 GLY n 
1 118 LYS n 
1 119 HIS n 
1 120 THR n 
1 121 LEU n 
1 122 LEU n 
1 123 TYR n 
1 124 GLY n 
1 125 HIS n 
1 126 ARG n 
1 127 ILE n 
1 128 GLY n 
1 129 PRO n 
1 130 GLU n 
1 131 LYS n 
1 132 ILE n 
1 133 ASP n 
1 134 THR n 
1 135 LEU n 
1 136 GLY n 
1 137 ILE n 
1 138 TYR n 
1 139 GLY n 
1 140 LYS n 
1 141 VAL n 
1 142 ASN n 
1 143 ILE n 
1 144 HIS n 
1 145 SER n 
1 146 ILE n 
1 147 GLY n 
1 148 PHE n 
1 149 SER n 
1 150 PHE n 
1 151 SER n 
1 152 SER n 
1 153 ASP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   153 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 LGALS8 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1354003 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IHE non-polymer         . 
;2-[[(2~{R},3~{R},4~{S},5~{S},6~{R})-2-(3,4-dichlorophenyl)sulfanyl-6-(hydroxymethyl)-5-oxidanyl-3-prop-2-ynoxy-oxan-4-yl]oxymethyl]-3-methyl-benzimidazole-5-carboxylic acid
;
? 'C25 H24 Cl2 N2 O7 S' 567.438 
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 
CL    non-polymer         . 'CHLORIDE ION' ? 'Cl -1'               35.453  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
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   SER 1   4   ?   ?   ?   A . n 
A 1 2   LEU 2   5   ?   ?   ?   A . n 
A 1 3   ASN 3   6   ?   ?   ?   A . n 
A 1 4   ASN 4   7   ?   ?   ?   A . n 
A 1 5   LEU 5   8   8   LEU LEU A . n 
A 1 6   GLN 6   9   9   GLN GLN A . n 
A 1 7   ASN 7   10  10  ASN ASN A . n 
A 1 8   ILE 8   11  11  ILE ILE A . n 
A 1 9   ILE 9   12  12  ILE ILE A . n 
A 1 10  TYR 10  13  13  TYR TYR A . n 
A 1 11  ASN 11  14  14  ASN ASN A . n 
A 1 12  PRO 12  15  15  PRO PRO A . n 
A 1 13  VAL 13  16  16  VAL VAL A . n 
A 1 14  ILE 14  17  17  ILE ILE A . n 
A 1 15  PRO 15  18  18  PRO PRO A . n 
A 1 16  PHE 16  19  19  PHE PHE A . n 
A 1 17  VAL 17  20  20  VAL VAL A . n 
A 1 18  GLY 18  21  21  GLY GLY A . n 
A 1 19  THR 19  22  22  THR THR A . n 
A 1 20  ILE 20  23  23  ILE ILE A . n 
A 1 21  PRO 21  24  24  PRO PRO A . n 
A 1 22  ASP 22  25  25  ASP ASP A . n 
A 1 23  GLN 23  26  26  GLN GLN A . n 
A 1 24  LEU 24  27  27  LEU LEU A . n 
A 1 25  ASP 25  28  28  ASP ASP A . n 
A 1 26  PRO 26  29  29  PRO PRO A . n 
A 1 27  GLY 27  30  30  GLY GLY A . n 
A 1 28  THR 28  31  31  THR THR A . n 
A 1 29  LEU 29  32  32  LEU LEU A . n 
A 1 30  ILE 30  33  33  ILE ILE A . n 
A 1 31  VAL 31  34  34  VAL VAL A . n 
A 1 32  ILE 32  35  35  ILE ILE A . n 
A 1 33  ARG 33  36  36  ARG ARG A . n 
A 1 34  GLY 34  37  37  GLY GLY A . n 
A 1 35  HIS 35  38  38  HIS HIS A . n 
A 1 36  VAL 36  39  39  VAL VAL A . n 
A 1 37  PRO 37  40  40  PRO PRO A . n 
A 1 38  SER 38  41  41  SER SER A . n 
A 1 39  ASP 39  42  42  ASP ASP A . n 
A 1 40  ALA 40  43  43  ALA ALA A . n 
A 1 41  ASP 41  44  44  ASP ASP A . n 
A 1 42  ARG 42  45  45  ARG ARG A . n 
A 1 43  PHE 43  46  46  PHE PHE A . n 
A 1 44  GLN 44  47  47  GLN GLN A . n 
A 1 45  VAL 45  48  48  VAL VAL A . n 
A 1 46  ASP 46  49  49  ASP ASP A . n 
A 1 47  LEU 47  50  50  LEU LEU A . n 
A 1 48  GLN 48  51  51  GLN GLN A . n 
A 1 49  ASN 49  52  52  ASN ASN A . n 
A 1 50  GLY 50  53  53  GLY GLY A . n 
A 1 51  SER 51  54  54  SER SER A . n 
A 1 52  SER 52  55  55  SER SER A . n 
A 1 53  MET 53  56  56  MET MET A . n 
A 1 54  LYS 54  57  57  LYS LYS A . n 
A 1 55  PRO 55  58  58  PRO PRO A . n 
A 1 56  ARG 56  59  59  ARG ARG A . n 
A 1 57  ALA 57  60  60  ALA ALA A . n 
A 1 58  ASP 58  61  61  ASP ASP A . n 
A 1 59  VAL 59  62  62  VAL VAL A . n 
A 1 60  ALA 60  63  63  ALA ALA A . n 
A 1 61  PHE 61  64  64  PHE PHE A . n 
A 1 62  HIS 62  65  65  HIS HIS A . n 
A 1 63  PHE 63  66  66  PHE PHE A . n 
A 1 64  ASN 64  67  67  ASN ASN A . n 
A 1 65  PRO 65  68  68  PRO PRO A . n 
A 1 66  ARG 66  69  69  ARG ARG A . n 
A 1 67  PHE 67  70  70  PHE PHE A . n 
A 1 68  LYS 68  71  71  LYS LYS A . n 
A 1 69  ARG 69  72  72  ARG ARG A . n 
A 1 70  ALA 70  73  73  ALA ALA A . n 
A 1 71  GLY 71  74  74  GLY GLY A . n 
A 1 72  CYS 72  75  75  CYS CYS A . n 
A 1 73  ILE 73  76  76  ILE ILE A . n 
A 1 74  VAL 74  77  77  VAL VAL A . n 
A 1 75  CYS 75  78  78  CYS CYS A . n 
A 1 76  ASN 76  79  79  ASN ASN A . n 
A 1 77  THR 77  80  80  THR THR A . n 
A 1 78  LEU 78  81  81  LEU LEU A . n 
A 1 79  ILE 79  82  82  ILE ILE A . n 
A 1 80  ASN 80  83  83  ASN ASN A . n 
A 1 81  GLU 81  84  84  GLU GLU A . n 
A 1 82  LYS 82  85  85  LYS LYS A . n 
A 1 83  TRP 83  86  86  TRP TRP A . n 
A 1 84  GLY 84  87  87  GLY GLY A . n 
A 1 85  ARG 85  88  88  ARG ARG A . n 
A 1 86  GLU 86  89  89  GLU GLU A . n 
A 1 87  GLU 87  90  90  GLU GLU A . n 
A 1 88  ILE 88  91  91  ILE ILE A . n 
A 1 89  THR 89  92  92  THR THR A . n 
A 1 90  TYR 90  93  93  TYR TYR A . n 
A 1 91  ASP 91  94  94  ASP ASP A . n 
A 1 92  THR 92  95  95  THR THR A . n 
A 1 93  PRO 93  96  96  PRO PRO A . n 
A 1 94  PHE 94  97  97  PHE PHE A . n 
A 1 95  LYS 95  98  98  LYS LYS A . n 
A 1 96  ARG 96  99  99  ARG ARG A . n 
A 1 97  GLU 97  100 100 GLU GLU A . n 
A 1 98  LYS 98  101 101 LYS LYS A . n 
A 1 99  SER 99  102 102 SER SER A . n 
A 1 100 PHE 100 103 103 PHE PHE A . n 
A 1 101 GLU 101 104 104 GLU GLU A . n 
A 1 102 ILE 102 105 105 ILE ILE A . n 
A 1 103 VAL 103 106 106 VAL VAL A . n 
A 1 104 ILE 104 107 107 ILE ILE A . n 
A 1 105 MET 105 108 108 MET MET A . n 
A 1 106 VAL 106 109 109 VAL VAL A . n 
A 1 107 LEU 107 110 110 LEU LEU A . n 
A 1 108 LYS 108 111 111 LYS LYS A . n 
A 1 109 ASP 109 112 112 ASP ASP A . n 
A 1 110 LYS 110 113 113 LYS LYS A . n 
A 1 111 PHE 111 114 114 PHE PHE A . n 
A 1 112 GLN 112 115 115 GLN GLN A . n 
A 1 113 VAL 113 116 116 VAL VAL A . n 
A 1 114 ALA 114 117 117 ALA ALA A . n 
A 1 115 VAL 115 118 118 VAL VAL A . n 
A 1 116 ASN 116 119 119 ASN ASN A . n 
A 1 117 GLY 117 120 120 GLY GLY A . n 
A 1 118 LYS 118 121 121 LYS LYS A . n 
A 1 119 HIS 119 122 122 HIS HIS A . n 
A 1 120 THR 120 123 123 THR THR A . n 
A 1 121 LEU 121 124 124 LEU LEU A . n 
A 1 122 LEU 122 125 125 LEU LEU A . n 
A 1 123 TYR 123 126 126 TYR TYR A . n 
A 1 124 GLY 124 127 127 GLY GLY A . n 
A 1 125 HIS 125 128 128 HIS HIS A . n 
A 1 126 ARG 126 129 129 ARG ARG A . n 
A 1 127 ILE 127 130 130 ILE ILE A . n 
A 1 128 GLY 128 131 131 GLY GLY A . n 
A 1 129 PRO 129 132 132 PRO PRO A . n 
A 1 130 GLU 130 133 133 GLU GLU A . n 
A 1 131 LYS 131 134 134 LYS LYS A . n 
A 1 132 ILE 132 135 135 ILE ILE A . n 
A 1 133 ASP 133 136 136 ASP ASP A . n 
A 1 134 THR 134 137 137 THR THR A . n 
A 1 135 LEU 135 138 138 LEU LEU A . n 
A 1 136 GLY 136 139 139 GLY GLY A . n 
A 1 137 ILE 137 140 140 ILE ILE A . n 
A 1 138 TYR 138 141 141 TYR TYR A . n 
A 1 139 GLY 139 142 142 GLY GLY A . n 
A 1 140 LYS 140 143 143 LYS LYS A . n 
A 1 141 VAL 141 144 144 VAL VAL A . n 
A 1 142 ASN 142 145 145 ASN ASN A . n 
A 1 143 ILE 143 146 146 ILE ILE A . n 
A 1 144 HIS 144 147 147 HIS HIS A . n 
A 1 145 SER 145 148 148 SER SER A . n 
A 1 146 ILE 146 149 149 ILE ILE A . n 
A 1 147 GLY 147 150 150 GLY GLY A . n 
A 1 148 PHE 148 151 151 PHE PHE A . n 
A 1 149 SER 149 152 152 SER SER A . n 
A 1 150 PHE 150 153 153 PHE PHE A . n 
A 1 151 SER 151 154 154 SER SER A . n 
A 1 152 SER 152 155 155 SER SER A . n 
A 1 153 ASP 153 156 156 ASP ASP A . n 
B 1 1   SER 1   4   ?   ?   ?   B . n 
B 1 2   LEU 2   5   ?   ?   ?   B . n 
B 1 3   ASN 3   6   ?   ?   ?   B . n 
B 1 4   ASN 4   7   7   ASN ASN B . n 
B 1 5   LEU 5   8   8   LEU LEU B . n 
B 1 6   GLN 6   9   9   GLN GLN B . n 
B 1 7   ASN 7   10  10  ASN ASN B . n 
B 1 8   ILE 8   11  11  ILE ILE B . n 
B 1 9   ILE 9   12  12  ILE ILE B . n 
B 1 10  TYR 10  13  13  TYR TYR B . n 
B 1 11  ASN 11  14  14  ASN ASN B . n 
B 1 12  PRO 12  15  15  PRO PRO B . n 
B 1 13  VAL 13  16  16  VAL VAL B . n 
B 1 14  ILE 14  17  17  ILE ILE B . n 
B 1 15  PRO 15  18  18  PRO PRO B . n 
B 1 16  PHE 16  19  19  PHE PHE B . n 
B 1 17  VAL 17  20  20  VAL VAL B . n 
B 1 18  GLY 18  21  21  GLY GLY B . n 
B 1 19  THR 19  22  22  THR THR B . n 
B 1 20  ILE 20  23  23  ILE ILE B . n 
B 1 21  PRO 21  24  24  PRO PRO B . n 
B 1 22  ASP 22  25  25  ASP ASP B . n 
B 1 23  GLN 23  26  26  GLN GLN B . n 
B 1 24  LEU 24  27  27  LEU LEU B . n 
B 1 25  ASP 25  28  28  ASP ASP B . n 
B 1 26  PRO 26  29  29  PRO PRO B . n 
B 1 27  GLY 27  30  30  GLY GLY B . n 
B 1 28  THR 28  31  31  THR THR B . n 
B 1 29  LEU 29  32  32  LEU LEU B . n 
B 1 30  ILE 30  33  33  ILE ILE B . n 
B 1 31  VAL 31  34  34  VAL VAL B . n 
B 1 32  ILE 32  35  35  ILE ILE B . n 
B 1 33  ARG 33  36  36  ARG ARG B . n 
B 1 34  GLY 34  37  37  GLY GLY B . n 
B 1 35  HIS 35  38  38  HIS HIS B . n 
B 1 36  VAL 36  39  39  VAL VAL B . n 
B 1 37  PRO 37  40  40  PRO PRO B . n 
B 1 38  SER 38  41  41  SER SER B . n 
B 1 39  ASP 39  42  42  ASP ASP B . n 
B 1 40  ALA 40  43  43  ALA ALA B . n 
B 1 41  ASP 41  44  44  ASP ASP B . n 
B 1 42  ARG 42  45  45  ARG ARG B . n 
B 1 43  PHE 43  46  46  PHE PHE B . n 
B 1 44  GLN 44  47  47  GLN GLN B . n 
B 1 45  VAL 45  48  48  VAL VAL B . n 
B 1 46  ASP 46  49  49  ASP ASP B . n 
B 1 47  LEU 47  50  50  LEU LEU B . n 
B 1 48  GLN 48  51  51  GLN GLN B . n 
B 1 49  ASN 49  52  52  ASN ASN B . n 
B 1 50  GLY 50  53  53  GLY GLY B . n 
B 1 51  SER 51  54  54  SER SER B . n 
B 1 52  SER 52  55  55  SER SER B . n 
B 1 53  MET 53  56  56  MET MET B . n 
B 1 54  LYS 54  57  57  LYS LYS B . n 
B 1 55  PRO 55  58  58  PRO PRO B . n 
B 1 56  ARG 56  59  59  ARG ARG B . n 
B 1 57  ALA 57  60  60  ALA ALA B . n 
B 1 58  ASP 58  61  61  ASP ASP B . n 
B 1 59  VAL 59  62  62  VAL VAL B . n 
B 1 60  ALA 60  63  63  ALA ALA B . n 
B 1 61  PHE 61  64  64  PHE PHE B . n 
B 1 62  HIS 62  65  65  HIS HIS B . n 
B 1 63  PHE 63  66  66  PHE PHE B . n 
B 1 64  ASN 64  67  67  ASN ASN B . n 
B 1 65  PRO 65  68  68  PRO PRO B . n 
B 1 66  ARG 66  69  69  ARG ARG B . n 
B 1 67  PHE 67  70  70  PHE PHE B . n 
B 1 68  LYS 68  71  71  LYS LYS B . n 
B 1 69  ARG 69  72  72  ARG ARG B . n 
B 1 70  ALA 70  73  73  ALA ALA B . n 
B 1 71  GLY 71  74  74  GLY GLY B . n 
B 1 72  CYS 72  75  75  CYS CYS B . n 
B 1 73  ILE 73  76  76  ILE ILE B . n 
B 1 74  VAL 74  77  77  VAL VAL B . n 
B 1 75  CYS 75  78  78  CYS CYS B . n 
B 1 76  ASN 76  79  79  ASN ASN B . n 
B 1 77  THR 77  80  80  THR THR B . n 
B 1 78  LEU 78  81  81  LEU LEU B . n 
B 1 79  ILE 79  82  82  ILE ILE B . n 
B 1 80  ASN 80  83  83  ASN ASN B . n 
B 1 81  GLU 81  84  84  GLU GLU B . n 
B 1 82  LYS 82  85  85  LYS LYS B . n 
B 1 83  TRP 83  86  86  TRP TRP B . n 
B 1 84  GLY 84  87  87  GLY GLY B . n 
B 1 85  ARG 85  88  88  ARG ARG B . n 
B 1 86  GLU 86  89  89  GLU GLU B . n 
B 1 87  GLU 87  90  90  GLU GLU B . n 
B 1 88  ILE 88  91  91  ILE ILE B . n 
B 1 89  THR 89  92  92  THR THR B . n 
B 1 90  TYR 90  93  93  TYR TYR B . n 
B 1 91  ASP 91  94  94  ASP ASP B . n 
B 1 92  THR 92  95  95  THR THR B . n 
B 1 93  PRO 93  96  96  PRO PRO B . n 
B 1 94  PHE 94  97  97  PHE PHE B . n 
B 1 95  LYS 95  98  98  LYS LYS B . n 
B 1 96  ARG 96  99  99  ARG ARG B . n 
B 1 97  GLU 97  100 100 GLU GLU B . n 
B 1 98  LYS 98  101 101 LYS LYS B . n 
B 1 99  SER 99  102 102 SER SER B . n 
B 1 100 PHE 100 103 103 PHE PHE B . n 
B 1 101 GLU 101 104 104 GLU GLU B . n 
B 1 102 ILE 102 105 105 ILE ILE B . n 
B 1 103 VAL 103 106 106 VAL VAL B . n 
B 1 104 ILE 104 107 107 ILE ILE B . n 
B 1 105 MET 105 108 108 MET MET B . n 
B 1 106 VAL 106 109 109 VAL VAL B . n 
B 1 107 LEU 107 110 110 LEU LEU B . n 
B 1 108 LYS 108 111 111 LYS LYS B . n 
B 1 109 ASP 109 112 112 ASP ASP B . n 
B 1 110 LYS 110 113 113 LYS LYS B . n 
B 1 111 PHE 111 114 114 PHE PHE B . n 
B 1 112 GLN 112 115 115 GLN GLN B . n 
B 1 113 VAL 113 116 116 VAL VAL B . n 
B 1 114 ALA 114 117 117 ALA ALA B . n 
B 1 115 VAL 115 118 118 VAL VAL B . n 
B 1 116 ASN 116 119 119 ASN ASN B . n 
B 1 117 GLY 117 120 120 GLY GLY B . n 
B 1 118 LYS 118 121 121 LYS LYS B . n 
B 1 119 HIS 119 122 122 HIS HIS B . n 
B 1 120 THR 120 123 123 THR THR B . n 
B 1 121 LEU 121 124 124 LEU LEU B . n 
B 1 122 LEU 122 125 125 LEU LEU B . n 
B 1 123 TYR 123 126 126 TYR TYR B . n 
B 1 124 GLY 124 127 127 GLY GLY B . n 
B 1 125 HIS 125 128 128 HIS HIS B . n 
B 1 126 ARG 126 129 129 ARG ARG B . n 
B 1 127 ILE 127 130 130 ILE ILE B . n 
B 1 128 GLY 128 131 131 GLY GLY B . n 
B 1 129 PRO 129 132 132 PRO PRO B . n 
B 1 130 GLU 130 133 133 GLU GLU B . n 
B 1 131 LYS 131 134 134 LYS LYS B . n 
B 1 132 ILE 132 135 135 ILE ILE B . n 
B 1 133 ASP 133 136 136 ASP ASP B . n 
B 1 134 THR 134 137 137 THR THR B . n 
B 1 135 LEU 135 138 138 LEU LEU B . n 
B 1 136 GLY 136 139 139 GLY GLY B . n 
B 1 137 ILE 137 140 140 ILE ILE B . n 
B 1 138 TYR 138 141 141 TYR TYR B . n 
B 1 139 GLY 139 142 142 GLY GLY B . n 
B 1 140 LYS 140 143 143 LYS LYS B . n 
B 1 141 VAL 141 144 144 VAL VAL B . n 
B 1 142 ASN 142 145 145 ASN ASN B . n 
B 1 143 ILE 143 146 146 ILE ILE B . n 
B 1 144 HIS 144 147 147 HIS HIS B . n 
B 1 145 SER 145 148 148 SER SER B . n 
B 1 146 ILE 146 149 149 ILE ILE B . n 
B 1 147 GLY 147 150 150 GLY GLY B . n 
B 1 148 PHE 148 151 151 PHE PHE B . n 
B 1 149 SER 149 152 152 SER SER B . n 
B 1 150 PHE 150 153 153 PHE PHE B . n 
B 1 151 SER 151 154 154 SER SER B . n 
B 1 152 SER 152 155 155 SER SER B . n 
B 1 153 ASP 153 156 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IHE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IHE 
_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 A1IHE 1   201 194 A1IHE AEP A . 
D 3 CL    1   202 1   CL    CL  A . 
E 2 A1IHE 1   201 194 A1IHE AEP B . 
F 4 HOH   1   301 333 HOH   HOH A . 
F 4 HOH   2   302 68  HOH   HOH A . 
F 4 HOH   3   303 354 HOH   HOH A . 
F 4 HOH   4   304 316 HOH   HOH A . 
F 4 HOH   5   305 226 HOH   HOH A . 
F 4 HOH   6   306 275 HOH   HOH A . 
F 4 HOH   7   307 272 HOH   HOH A . 
F 4 HOH   8   308 383 HOH   HOH A . 
F 4 HOH   9   309 276 HOH   HOH A . 
F 4 HOH   10  310 348 HOH   HOH A . 
F 4 HOH   11  311 116 HOH   HOH A . 
F 4 HOH   12  312 192 HOH   HOH A . 
F 4 HOH   13  313 215 HOH   HOH A . 
F 4 HOH   14  314 313 HOH   HOH A . 
F 4 HOH   15  315 60  HOH   HOH A . 
F 4 HOH   16  316 324 HOH   HOH A . 
F 4 HOH   17  317 220 HOH   HOH A . 
F 4 HOH   18  318 16  HOH   HOH A . 
F 4 HOH   19  319 234 HOH   HOH A . 
F 4 HOH   20  320 253 HOH   HOH A . 
F 4 HOH   21  321 344 HOH   HOH A . 
F 4 HOH   22  322 334 HOH   HOH A . 
F 4 HOH   23  323 188 HOH   HOH A . 
F 4 HOH   24  324 148 HOH   HOH A . 
F 4 HOH   25  325 138 HOH   HOH A . 
F 4 HOH   26  326 196 HOH   HOH A . 
F 4 HOH   27  327 233 HOH   HOH A . 
F 4 HOH   28  328 163 HOH   HOH A . 
F 4 HOH   29  329 63  HOH   HOH A . 
F 4 HOH   30  330 248 HOH   HOH A . 
F 4 HOH   31  331 57  HOH   HOH A . 
F 4 HOH   32  332 22  HOH   HOH A . 
F 4 HOH   33  333 225 HOH   HOH A . 
F 4 HOH   34  334 141 HOH   HOH A . 
F 4 HOH   35  335 29  HOH   HOH A . 
F 4 HOH   36  336 10  HOH   HOH A . 
F 4 HOH   37  337 246 HOH   HOH A . 
F 4 HOH   38  338 12  HOH   HOH A . 
F 4 HOH   39  339 80  HOH   HOH A . 
F 4 HOH   40  340 187 HOH   HOH A . 
F 4 HOH   41  341 94  HOH   HOH A . 
F 4 HOH   42  342 9   HOH   HOH A . 
F 4 HOH   43  343 24  HOH   HOH A . 
F 4 HOH   44  344 27  HOH   HOH A . 
F 4 HOH   45  345 96  HOH   HOH A . 
F 4 HOH   46  346 72  HOH   HOH A . 
F 4 HOH   47  347 20  HOH   HOH A . 
F 4 HOH   48  348 58  HOH   HOH A . 
F 4 HOH   49  349 4   HOH   HOH A . 
F 4 HOH   50  350 19  HOH   HOH A . 
F 4 HOH   51  351 8   HOH   HOH A . 
F 4 HOH   52  352 14  HOH   HOH A . 
F 4 HOH   53  353 105 HOH   HOH A . 
F 4 HOH   54  354 231 HOH   HOH A . 
F 4 HOH   55  355 262 HOH   HOH A . 
F 4 HOH   56  356 18  HOH   HOH A . 
F 4 HOH   57  357 279 HOH   HOH A . 
F 4 HOH   58  358 46  HOH   HOH A . 
F 4 HOH   59  359 26  HOH   HOH A . 
F 4 HOH   60  360 294 HOH   HOH A . 
F 4 HOH   61  361 166 HOH   HOH A . 
F 4 HOH   62  362 183 HOH   HOH A . 
F 4 HOH   63  363 309 HOH   HOH A . 
F 4 HOH   64  364 242 HOH   HOH A . 
F 4 HOH   65  365 379 HOH   HOH A . 
F 4 HOH   66  366 259 HOH   HOH A . 
F 4 HOH   67  367 107 HOH   HOH A . 
F 4 HOH   68  368 64  HOH   HOH A . 
F 4 HOH   69  369 51  HOH   HOH A . 
F 4 HOH   70  370 236 HOH   HOH A . 
F 4 HOH   71  371 53  HOH   HOH A . 
F 4 HOH   72  372 164 HOH   HOH A . 
F 4 HOH   73  373 237 HOH   HOH A . 
F 4 HOH   74  374 122 HOH   HOH A . 
F 4 HOH   75  375 73  HOH   HOH A . 
F 4 HOH   76  376 195 HOH   HOH A . 
F 4 HOH   77  377 83  HOH   HOH A . 
F 4 HOH   78  378 186 HOH   HOH A . 
F 4 HOH   79  379 306 HOH   HOH A . 
F 4 HOH   80  380 211 HOH   HOH A . 
F 4 HOH   81  381 93  HOH   HOH A . 
F 4 HOH   82  382 71  HOH   HOH A . 
F 4 HOH   83  383 264 HOH   HOH A . 
F 4 HOH   84  384 79  HOH   HOH A . 
F 4 HOH   85  385 128 HOH   HOH A . 
F 4 HOH   86  386 235 HOH   HOH A . 
F 4 HOH   87  387 230 HOH   HOH A . 
F 4 HOH   88  388 206 HOH   HOH A . 
F 4 HOH   89  389 157 HOH   HOH A . 
F 4 HOH   90  390 228 HOH   HOH A . 
F 4 HOH   91  391 54  HOH   HOH A . 
F 4 HOH   92  392 216 HOH   HOH A . 
F 4 HOH   93  393 104 HOH   HOH A . 
F 4 HOH   94  394 338 HOH   HOH A . 
F 4 HOH   95  395 201 HOH   HOH A . 
F 4 HOH   96  396 127 HOH   HOH A . 
F 4 HOH   97  397 98  HOH   HOH A . 
F 4 HOH   98  398 249 HOH   HOH A . 
F 4 HOH   99  399 384 HOH   HOH A . 
F 4 HOH   100 400 150 HOH   HOH A . 
F 4 HOH   101 401 173 HOH   HOH A . 
F 4 HOH   102 402 65  HOH   HOH A . 
F 4 HOH   103 403 346 HOH   HOH A . 
F 4 HOH   104 404 67  HOH   HOH A . 
F 4 HOH   105 405 317 HOH   HOH A . 
F 4 HOH   106 406 362 HOH   HOH A . 
F 4 HOH   107 407 52  HOH   HOH A . 
F 4 HOH   108 408 35  HOH   HOH A . 
F 4 HOH   109 409 250 HOH   HOH A . 
F 4 HOH   110 410 95  HOH   HOH A . 
F 4 HOH   111 411 84  HOH   HOH A . 
F 4 HOH   112 412 97  HOH   HOH A . 
F 4 HOH   113 413 296 HOH   HOH A . 
F 4 HOH   114 414 223 HOH   HOH A . 
F 4 HOH   115 415 256 HOH   HOH A . 
F 4 HOH   116 416 318 HOH   HOH A . 
F 4 HOH   117 417 36  HOH   HOH A . 
F 4 HOH   118 418 151 HOH   HOH A . 
F 4 HOH   119 419 43  HOH   HOH A . 
F 4 HOH   120 420 326 HOH   HOH A . 
F 4 HOH   121 421 147 HOH   HOH A . 
F 4 HOH   122 422 7   HOH   HOH A . 
F 4 HOH   123 423 155 HOH   HOH A . 
F 4 HOH   124 424 289 HOH   HOH A . 
F 4 HOH   125 425 319 HOH   HOH A . 
F 4 HOH   126 426 181 HOH   HOH A . 
F 4 HOH   127 427 213 HOH   HOH A . 
F 4 HOH   128 428 70  HOH   HOH A . 
F 4 HOH   129 429 76  HOH   HOH A . 
F 4 HOH   130 430 132 HOH   HOH A . 
F 4 HOH   131 431 307 HOH   HOH A . 
F 4 HOH   132 432 208 HOH   HOH A . 
F 4 HOH   133 433 197 HOH   HOH A . 
F 4 HOH   134 434 90  HOH   HOH A . 
F 4 HOH   135 435 227 HOH   HOH A . 
F 4 HOH   136 436 199 HOH   HOH A . 
F 4 HOH   137 437 371 HOH   HOH A . 
F 4 HOH   138 438 299 HOH   HOH A . 
F 4 HOH   139 439 277 HOH   HOH A . 
F 4 HOH   140 440 322 HOH   HOH A . 
F 4 HOH   141 441 356 HOH   HOH A . 
F 4 HOH   142 442 367 HOH   HOH A . 
F 4 HOH   143 443 267 HOH   HOH A . 
F 4 HOH   144 444 154 HOH   HOH A . 
F 4 HOH   145 445 149 HOH   HOH A . 
F 4 HOH   146 446 297 HOH   HOH A . 
F 4 HOH   147 447 291 HOH   HOH A . 
F 4 HOH   148 448 310 HOH   HOH A . 
F 4 HOH   149 449 372 HOH   HOH A . 
F 4 HOH   150 450 224 HOH   HOH A . 
F 4 HOH   151 451 290 HOH   HOH A . 
F 4 HOH   152 452 278 HOH   HOH A . 
F 4 HOH   153 453 184 HOH   HOH A . 
F 4 HOH   154 454 239 HOH   HOH A . 
F 4 HOH   155 455 286 HOH   HOH A . 
F 4 HOH   156 456 135 HOH   HOH A . 
F 4 HOH   157 457 146 HOH   HOH A . 
F 4 HOH   158 458 387 HOH   HOH A . 
F 4 HOH   159 459 301 HOH   HOH A . 
F 4 HOH   160 460 314 HOH   HOH A . 
F 4 HOH   161 461 349 HOH   HOH A . 
F 4 HOH   162 462 298 HOH   HOH A . 
F 4 HOH   163 463 261 HOH   HOH A . 
F 4 HOH   164 464 144 HOH   HOH A . 
F 4 HOH   165 465 390 HOH   HOH A . 
F 4 HOH   166 466 266 HOH   HOH A . 
F 4 HOH   167 467 254 HOH   HOH A . 
F 4 HOH   168 468 359 HOH   HOH A . 
F 4 HOH   169 469 143 HOH   HOH A . 
F 4 HOH   170 470 381 HOH   HOH A . 
F 4 HOH   171 471 374 HOH   HOH A . 
F 4 HOH   172 472 270 HOH   HOH A . 
F 4 HOH   173 473 190 HOH   HOH A . 
F 4 HOH   174 474 110 HOH   HOH A . 
F 4 HOH   175 475 302 HOH   HOH A . 
F 4 HOH   176 476 168 HOH   HOH A . 
F 4 HOH   177 477 160 HOH   HOH A . 
F 4 HOH   178 478 257 HOH   HOH A . 
F 4 HOH   179 479 198 HOH   HOH A . 
F 4 HOH   180 480 311 HOH   HOH A . 
F 4 HOH   181 481 134 HOH   HOH A . 
F 4 HOH   182 482 273 HOH   HOH A . 
F 4 HOH   183 483 304 HOH   HOH A . 
F 4 HOH   184 484 40  HOH   HOH A . 
F 4 HOH   185 485 368 HOH   HOH A . 
F 4 HOH   186 486 320 HOH   HOH A . 
F 4 HOH   187 487 274 HOH   HOH A . 
G 4 HOH   1   301 169 HOH   HOH B . 
G 4 HOH   2   302 178 HOH   HOH B . 
G 4 HOH   3   303 378 HOH   HOH B . 
G 4 HOH   4   304 280 HOH   HOH B . 
G 4 HOH   5   305 229 HOH   HOH B . 
G 4 HOH   6   306 380 HOH   HOH B . 
G 4 HOH   7   307 193 HOH   HOH B . 
G 4 HOH   8   308 345 HOH   HOH B . 
G 4 HOH   9   309 352 HOH   HOH B . 
G 4 HOH   10  310 77  HOH   HOH B . 
G 4 HOH   11  311 209 HOH   HOH B . 
G 4 HOH   12  312 325 HOH   HOH B . 
G 4 HOH   13  313 323 HOH   HOH B . 
G 4 HOH   14  314 321 HOH   HOH B . 
G 4 HOH   15  315 268 HOH   HOH B . 
G 4 HOH   16  316 308 HOH   HOH B . 
G 4 HOH   17  317 113 HOH   HOH B . 
G 4 HOH   18  318 282 HOH   HOH B . 
G 4 HOH   19  319 56  HOH   HOH B . 
G 4 HOH   20  320 21  HOH   HOH B . 
G 4 HOH   21  321 119 HOH   HOH B . 
G 4 HOH   22  322 180 HOH   HOH B . 
G 4 HOH   23  323 129 HOH   HOH B . 
G 4 HOH   24  324 158 HOH   HOH B . 
G 4 HOH   25  325 81  HOH   HOH B . 
G 4 HOH   26  326 245 HOH   HOH B . 
G 4 HOH   27  327 137 HOH   HOH B . 
G 4 HOH   28  328 3   HOH   HOH B . 
G 4 HOH   29  329 185 HOH   HOH B . 
G 4 HOH   30  330 252 HOH   HOH B . 
G 4 HOH   31  331 343 HOH   HOH B . 
G 4 HOH   32  332 258 HOH   HOH B . 
G 4 HOH   33  333 120 HOH   HOH B . 
G 4 HOH   34  334 92  HOH   HOH B . 
G 4 HOH   35  335 44  HOH   HOH B . 
G 4 HOH   36  336 182 HOH   HOH B . 
G 4 HOH   37  337 340 HOH   HOH B . 
G 4 HOH   38  338 103 HOH   HOH B . 
G 4 HOH   39  339 312 HOH   HOH B . 
G 4 HOH   40  340 315 HOH   HOH B . 
G 4 HOH   41  341 17  HOH   HOH B . 
G 4 HOH   42  342 23  HOH   HOH B . 
G 4 HOH   43  343 260 HOH   HOH B . 
G 4 HOH   44  344 89  HOH   HOH B . 
G 4 HOH   45  345 189 HOH   HOH B . 
G 4 HOH   46  346 142 HOH   HOH B . 
G 4 HOH   47  347 288 HOH   HOH B . 
G 4 HOH   48  348 204 HOH   HOH B . 
G 4 HOH   49  349 366 HOH   HOH B . 
G 4 HOH   50  350 373 HOH   HOH B . 
G 4 HOH   51  351 365 HOH   HOH B . 
G 4 HOH   52  352 131 HOH   HOH B . 
G 4 HOH   53  353 111 HOH   HOH B . 
G 4 HOH   54  354 100 HOH   HOH B . 
G 4 HOH   55  355 238 HOH   HOH B . 
G 4 HOH   56  356 159 HOH   HOH B . 
G 4 HOH   57  357 11  HOH   HOH B . 
G 4 HOH   58  358 386 HOH   HOH B . 
G 4 HOH   59  359 31  HOH   HOH B . 
G 4 HOH   60  360 265 HOH   HOH B . 
G 4 HOH   61  361 33  HOH   HOH B . 
G 4 HOH   62  362 212 HOH   HOH B . 
G 4 HOH   63  363 61  HOH   HOH B . 
G 4 HOH   64  364 331 HOH   HOH B . 
G 4 HOH   65  365 38  HOH   HOH B . 
G 4 HOH   66  366 243 HOH   HOH B . 
G 4 HOH   67  367 140 HOH   HOH B . 
G 4 HOH   68  368 217 HOH   HOH B . 
G 4 HOH   69  369 13  HOH   HOH B . 
G 4 HOH   70  370 1   HOH   HOH B . 
G 4 HOH   71  371 174 HOH   HOH B . 
G 4 HOH   72  372 6   HOH   HOH B . 
G 4 HOH   73  373 87  HOH   HOH B . 
G 4 HOH   74  374 255 HOH   HOH B . 
G 4 HOH   75  375 109 HOH   HOH B . 
G 4 HOH   76  376 99  HOH   HOH B . 
G 4 HOH   77  377 91  HOH   HOH B . 
G 4 HOH   78  378 124 HOH   HOH B . 
G 4 HOH   79  379 45  HOH   HOH B . 
G 4 HOH   80  380 300 HOH   HOH B . 
G 4 HOH   81  381 179 HOH   HOH B . 
G 4 HOH   82  382 32  HOH   HOH B . 
G 4 HOH   83  383 191 HOH   HOH B . 
G 4 HOH   84  384 241 HOH   HOH B . 
G 4 HOH   85  385 171 HOH   HOH B . 
G 4 HOH   86  386 281 HOH   HOH B . 
G 4 HOH   87  387 200 HOH   HOH B . 
G 4 HOH   88  388 271 HOH   HOH B . 
G 4 HOH   89  389 167 HOH   HOH B . 
G 4 HOH   90  390 303 HOH   HOH B . 
G 4 HOH   91  391 145 HOH   HOH B . 
G 4 HOH   92  392 86  HOH   HOH B . 
G 4 HOH   93  393 240 HOH   HOH B . 
G 4 HOH   94  394 125 HOH   HOH B . 
G 4 HOH   95  395 202 HOH   HOH B . 
G 4 HOH   96  396 74  HOH   HOH B . 
G 4 HOH   97  397 118 HOH   HOH B . 
G 4 HOH   98  398 232 HOH   HOH B . 
G 4 HOH   99  399 106 HOH   HOH B . 
G 4 HOH   100 400 50  HOH   HOH B . 
G 4 HOH   101 401 136 HOH   HOH B . 
G 4 HOH   102 402 376 HOH   HOH B . 
G 4 HOH   103 403 269 HOH   HOH B . 
G 4 HOH   104 404 5   HOH   HOH B . 
G 4 HOH   105 405 175 HOH   HOH B . 
G 4 HOH   106 406 121 HOH   HOH B . 
G 4 HOH   107 407 48  HOH   HOH B . 
G 4 HOH   108 408 244 HOH   HOH B . 
G 4 HOH   109 409 75  HOH   HOH B . 
G 4 HOH   110 410 351 HOH   HOH B . 
G 4 HOH   111 411 59  HOH   HOH B . 
G 4 HOH   112 412 34  HOH   HOH B . 
G 4 HOH   113 413 30  HOH   HOH B . 
G 4 HOH   114 414 263 HOH   HOH B . 
G 4 HOH   115 415 251 HOH   HOH B . 
G 4 HOH   116 416 332 HOH   HOH B . 
G 4 HOH   117 417 42  HOH   HOH B . 
G 4 HOH   118 418 218 HOH   HOH B . 
G 4 HOH   119 419 114 HOH   HOH B . 
G 4 HOH   120 420 172 HOH   HOH B . 
G 4 HOH   121 421 15  HOH   HOH B . 
G 4 HOH   122 422 112 HOH   HOH B . 
G 4 HOH   123 423 39  HOH   HOH B . 
G 4 HOH   124 424 342 HOH   HOH B . 
G 4 HOH   125 425 55  HOH   HOH B . 
G 4 HOH   126 426 153 HOH   HOH B . 
G 4 HOH   127 427 49  HOH   HOH B . 
G 4 HOH   128 428 292 HOH   HOH B . 
G 4 HOH   129 429 62  HOH   HOH B . 
G 4 HOH   130 430 102 HOH   HOH B . 
G 4 HOH   131 431 170 HOH   HOH B . 
G 4 HOH   132 432 247 HOH   HOH B . 
G 4 HOH   133 433 152 HOH   HOH B . 
G 4 HOH   134 434 130 HOH   HOH B . 
G 4 HOH   135 435 47  HOH   HOH B . 
G 4 HOH   136 436 207 HOH   HOH B . 
G 4 HOH   137 437 382 HOH   HOH B . 
G 4 HOH   138 438 353 HOH   HOH B . 
G 4 HOH   139 439 156 HOH   HOH B . 
G 4 HOH   140 440 25  HOH   HOH B . 
G 4 HOH   141 441 305 HOH   HOH B . 
G 4 HOH   142 442 133 HOH   HOH B . 
G 4 HOH   143 443 285 HOH   HOH B . 
G 4 HOH   144 444 287 HOH   HOH B . 
G 4 HOH   145 445 78  HOH   HOH B . 
G 4 HOH   146 446 361 HOH   HOH B . 
G 4 HOH   147 447 28  HOH   HOH B . 
G 4 HOH   148 448 85  HOH   HOH B . 
G 4 HOH   149 449 41  HOH   HOH B . 
G 4 HOH   150 450 360 HOH   HOH B . 
G 4 HOH   151 451 370 HOH   HOH B . 
G 4 HOH   152 452 176 HOH   HOH B . 
G 4 HOH   153 453 330 HOH   HOH B . 
G 4 HOH   154 454 389 HOH   HOH B . 
G 4 HOH   155 455 37  HOH   HOH B . 
G 4 HOH   156 456 358 HOH   HOH B . 
G 4 HOH   157 457 295 HOH   HOH B . 
G 4 HOH   158 458 126 HOH   HOH B . 
G 4 HOH   159 459 339 HOH   HOH B . 
G 4 HOH   160 460 388 HOH   HOH B . 
G 4 HOH   161 461 284 HOH   HOH B . 
G 4 HOH   162 462 335 HOH   HOH B . 
G 4 HOH   163 463 293 HOH   HOH B . 
G 4 HOH   164 464 341 HOH   HOH B . 
G 4 HOH   165 465 283 HOH   HOH B . 
G 4 HOH   166 466 336 HOH   HOH B . 
G 4 HOH   167 467 377 HOH   HOH B . 
G 4 HOH   168 468 139 HOH   HOH B . 
G 4 HOH   169 469 347 HOH   HOH B . 
G 4 HOH   170 470 327 HOH   HOH B . 
G 4 HOH   171 471 337 HOH   HOH B . 
G 4 HOH   172 472 2   HOH   HOH B . 
G 4 HOH   173 473 203 HOH   HOH B . 
G 4 HOH   174 474 329 HOH   HOH B . 
G 4 HOH   175 475 82  HOH   HOH B . 
G 4 HOH   176 476 101 HOH   HOH B . 
G 4 HOH   177 477 357 HOH   HOH B . 
G 4 HOH   178 478 165 HOH   HOH B . 
G 4 HOH   179 479 363 HOH   HOH B . 
G 4 HOH   180 480 108 HOH   HOH B . 
G 4 HOH   181 481 385 HOH   HOH B . 
G 4 HOH   182 482 364 HOH   HOH B . 
G 4 HOH   183 483 194 HOH   HOH B . 
G 4 HOH   184 484 222 HOH   HOH B . 
G 4 HOH   185 485 161 HOH   HOH B . 
G 4 HOH   186 486 219 HOH   HOH B . 
G 4 HOH   187 487 162 HOH   HOH B . 
G 4 HOH   188 488 88  HOH   HOH B . 
G 4 HOH   189 489 328 HOH   HOH B . 
G 4 HOH   190 490 117 HOH   HOH B . 
G 4 HOH   191 491 375 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21rc1_5084 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .            2 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? EDNA    ? ? ? .            3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .            4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FYJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.689 
_cell.length_a_esd                 ? 
_cell.length_b                     62.280 
_cell.length_b_esd                 ? 
_cell.length_c                     84.791 
_cell.length_c_esd                 ? 
_cell.volume                       283519.984 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9FYJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FYJ 
_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             2.05 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.94 
_exptl_crystal.description                  'flat plates' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'room temperature' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Drops consisted of 2 ul galectin-8N at 13.1 mg/ml in PBS buffer, 1 mM ligand, 5% DMSO mixed with 2 ul of reservoir solution consisting of 35% (w/v) Morpheus precipitant mix 4, 0.16 M Morpheus alcohol mix, 61 mM MES, 39 mM imidazole, pH 7.5. Morpheus precipitant mix 4 is made up of 25% (w/v) each of methane pentane diol (MPD), polyethylene glycol (PEG) 1000 and PEG 3350. Morpheus alcohol mix contains 0.2 M each of 1,6-hexanediol, 1-butanol, 1,2-propanediol, 2-propanol, 1,4-butanediol and 1,3-propanediol (1.2 M total).
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-06 
_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   0.8000 
_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                        'MAX IV BEAMLINE BioMAX' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BioMAX 
_diffrn_source.pdbx_synchrotron_site       'MAX IV' 
# 
_reflns.B_iso_Wilson_estimate                          14.56 
_reflns.entry_id                                       9FYJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.08 
_reflns.d_resolution_low                               45.4 
_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                                     119679 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.4 
_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                                0.056 
_reflns.pdbx_Rpim_I_all                                0.015 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.054 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.08 
_reflns_shell.d_res_low                                     1.12 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9860 
_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                               7.7 
_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                               1.573 
_reflns_shell.pdbx_Rpim_I_all                               0.554 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.559 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          83.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.465 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.64 
_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                                 9FYJ 
_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                            1.08 
_refine.ls_d_res_low                             42.40 
_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                     119551 
_refine.ls_number_reflns_R_free                  5966 
_refine.ls_number_reflns_R_work                  113585 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.80 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1333 
_refine.ls_R_factor_R_free                       0.1503 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1324 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 14.0188 
_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                            0.0972 
_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                       1.08 
_refine_hist.d_res_low                        42.40 
_refine_hist.number_atoms_solvent             378 
_refine_hist.number_atoms_total               2830 
_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        2377 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         75 
_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' ? 0.0081  ? 2592 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0343  ? 3531 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0935  ? 384  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0112  ? 474  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.1980 ? 1019 ? 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' 1.08 1.09  . . 160 3017 78.48  . . . . 0.2901 . . . . . . . . . . . 0.3009 
'X-RAY DIFFRACTION' 1.09 1.11  . . 162 3176 83.33  . . . . 0.2630 . . . . . . . . . . . 0.2696 
'X-RAY DIFFRACTION' 1.11 1.12  . . 184 3285 85.93  . . . . 0.2409 . . . . . . . . . . . 0.2535 
'X-RAY DIFFRACTION' 1.12 1.13  . . 159 3490 90.79  . . . . 0.2236 . . . . . . . . . . . 0.2373 
'X-RAY DIFFRACTION' 1.13 1.15  . . 180 3724 96.66  . . . . 0.2017 . . . . . . . . . . . 0.2289 
'X-RAY DIFFRACTION' 1.15 1.16  . . 181 3804 99.01  . . . . 0.1847 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 1.16 1.18  . . 194 3857 99.80  . . . . 0.1659 . . . . . . . . . . . 0.1969 
'X-RAY DIFFRACTION' 1.18 1.20  . . 222 3810 99.88  . . . . 0.1582 . . . . . . . . . . . 0.1966 
'X-RAY DIFFRACTION' 1.20 1.22  . . 210 3826 100.00 . . . . 0.1452 . . . . . . . . . . . 0.1889 
'X-RAY DIFFRACTION' 1.22 1.24  . . 217 3783 99.93  . . . . 0.1451 . . . . . . . . . . . 0.1729 
'X-RAY DIFFRACTION' 1.24 1.26  . . 217 3837 100.00 . . . . 0.1438 . . . . . . . . . . . 0.1656 
'X-RAY DIFFRACTION' 1.26 1.28  . . 203 3870 99.98  . . . . 0.1384 . . . . . . . . . . . 0.1724 
'X-RAY DIFFRACTION' 1.28 1.31  . . 196 3843 100.00 . . . . 0.1321 . . . . . . . . . . . 0.1623 
'X-RAY DIFFRACTION' 1.31 1.33  . . 223 3812 100.00 . . . . 0.1257 . . . . . . . . . . . 0.1622 
'X-RAY DIFFRACTION' 1.33 1.36  . . 215 3819 100.00 . . . . 0.1206 . . . . . . . . . . . 0.1592 
'X-RAY DIFFRACTION' 1.36 1.39  . . 215 3865 100.00 . . . . 0.1135 . . . . . . . . . . . 0.1396 
'X-RAY DIFFRACTION' 1.39 1.43  . . 205 3822 100.00 . . . . 0.1045 . . . . . . . . . . . 0.1367 
'X-RAY DIFFRACTION' 1.43 1.47  . . 184 3873 100.00 . . . . 0.1026 . . . . . . . . . . . 0.1353 
'X-RAY DIFFRACTION' 1.47 1.51  . . 201 3867 100.00 . . . . 0.1043 . . . . . . . . . . . 0.1401 
'X-RAY DIFFRACTION' 1.51 1.56  . . 210 3866 100.00 . . . . 0.1041 . . . . . . . . . . . 0.1312 
'X-RAY DIFFRACTION' 1.56 1.61  . . 210 3869 100.00 . . . . 0.1019 . . . . . . . . . . . 0.1213 
'X-RAY DIFFRACTION' 1.61 1.68  . . 214 3863 100.00 . . . . 0.1013 . . . . . . . . . . . 0.1345 
'X-RAY DIFFRACTION' 1.68 1.75  . . 199 3885 100.00 . . . . 0.1033 . . . . . . . . . . . 0.1355 
'X-RAY DIFFRACTION' 1.75 1.85  . . 219 3870 99.98  . . . . 0.1034 . . . . . . . . . . . 0.1173 
'X-RAY DIFFRACTION' 1.85 1.96  . . 199 3903 100.00 . . . . 0.1080 . . . . . . . . . . . 0.1342 
'X-RAY DIFFRACTION' 1.96 2.11  . . 179 3923 100.00 . . . . 0.1132 . . . . . . . . . . . 0.1341 
'X-RAY DIFFRACTION' 2.11 2.33  . . 198 3927 100.00 . . . . 0.1153 . . . . . . . . . . . 0.1351 
'X-RAY DIFFRACTION' 2.33 2.66  . . 197 3961 100.00 . . . . 0.1374 . . . . . . . . . . . 0.1452 
'X-RAY DIFFRACTION' 2.66 3.35  . . 204 3997 100.00 . . . . 0.1455 . . . . . . . . . . . 0.1552 
'X-RAY DIFFRACTION' 3.36 42.40 . . 209 4141 99.61  . . . . 0.1512 . . . . . . . . . . . 0.1594 
# 
_struct.entry_id                     9FYJ 
_struct.title                        'N-terminal domain of human galectin-8 in complex with an alpha-galactoside ligand' 
_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        9FYJ 
_struct_keywords.text            'inhibitor, complex, drug design, SUGAR BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'SUGAR BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LEG8_HUMAN 
_struct_ref.pdbx_db_accession          O00214 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNTLIN
EKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFSFSSD
;
_struct_ref.pdbx_align_begin           4 
# 
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 9FYJ A 1 ? 153 ? O00214 4 ? 156 ? 4 156 
2 1 9FYJ B 1 ? 153 ? O00214 4 ? 156 ? 4 156 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2560  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  14890 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 128 ? ILE A 132 ? GLY A 131 ILE A 135 5 ? 5 
HELX_P HELX_P2 AA2 GLY B 128 ? ILE B 132 ? GLY B 131 ILE B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ILE 14 A . ? ILE 17 A PRO 15 A ? PRO 18 A 1 9.31   
2 LYS 54 A . ? LYS 57 A PRO 55 A ? PRO 58 A 1 -3.58  
3 ILE 14 B . ? ILE 17 B PRO 15 B ? PRO 18 B 1 4.02   
4 LYS 54 B . ? LYS 57 B PRO 55 B ? PRO 58 B 1 -15.05 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
AA5 ? 6 ? 
AA6 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 8   ? TYR A 10  ? ILE A 11  TYR A 13  
AA1 2 ASN A 142 ? SER A 149 ? ASN A 145 SER A 152 
AA1 3 LEU A 29  ? HIS A 35  ? LEU A 32  HIS A 38  
AA1 4 SER A 99  ? VAL A 106 ? SER A 102 VAL A 109 
AA1 5 LYS A 110 ? VAL A 115 ? LYS A 113 VAL A 118 
AA1 6 LYS A 118 ? GLY A 124 ? LYS A 121 GLY A 127 
AA2 1 PHE A 16  ? THR A 19  ? PHE A 19  THR A 22  
AA2 2 THR A 134 ? GLY A 139 ? THR A 137 GLY A 142 
AA2 3 PHE A 43  ? ASN A 49  ? PHE A 46  ASN A 52  
AA2 4 ASP A 58  ? ARG A 66  ? ASP A 61  ARG A 69  
AA2 5 CYS A 72  ? ILE A 79  ? CYS A 75  ILE A 82  
AA2 6 LYS A 82  ? TRP A 83  ? LYS A 85  TRP A 86  
AA3 1 PHE A 16  ? THR A 19  ? PHE A 19  THR A 22  
AA3 2 THR A 134 ? GLY A 139 ? THR A 137 GLY A 142 
AA3 3 PHE A 43  ? ASN A 49  ? PHE A 46  ASN A 52  
AA3 4 ASP A 58  ? ARG A 66  ? ASP A 61  ARG A 69  
AA3 5 CYS A 72  ? ILE A 79  ? CYS A 75  ILE A 82  
AA3 6 GLU A 87  ? THR A 89  ? GLU A 90  THR A 92  
AA4 1 GLN B 6   ? TYR B 10  ? GLN B 9   TYR B 13  
AA4 2 ASN B 142 ? SER B 149 ? ASN B 145 SER B 152 
AA4 3 LEU B 29  ? HIS B 35  ? LEU B 32  HIS B 38  
AA4 4 SER B 99  ? VAL B 106 ? SER B 102 VAL B 109 
AA4 5 LYS B 110 ? VAL B 115 ? LYS B 113 VAL B 118 
AA4 6 LYS B 118 ? GLY B 124 ? LYS B 121 GLY B 127 
AA5 1 PHE B 16  ? THR B 19  ? PHE B 19  THR B 22  
AA5 2 THR B 134 ? GLY B 139 ? THR B 137 GLY B 142 
AA5 3 PHE B 43  ? ASN B 49  ? PHE B 46  ASN B 52  
AA5 4 ASP B 58  ? ARG B 66  ? ASP B 61  ARG B 69  
AA5 5 CYS B 72  ? ILE B 79  ? CYS B 75  ILE B 82  
AA5 6 LYS B 82  ? TRP B 83  ? LYS B 85  TRP B 86  
AA6 1 PHE B 16  ? THR B 19  ? PHE B 19  THR B 22  
AA6 2 THR B 134 ? GLY B 139 ? THR B 137 GLY B 142 
AA6 3 PHE B 43  ? ASN B 49  ? PHE B 46  ASN B 52  
AA6 4 ASP B 58  ? ARG B 66  ? ASP B 61  ARG B 69  
AA6 5 CYS B 72  ? ILE B 79  ? CYS B 75  ILE B 82  
AA6 6 GLU B 87  ? THR B 89  ? GLU B 90  THR B 92  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 9   ? N ILE A 12  O ILE A 146 ? O ILE A 149 
AA1 2 3 O GLY A 147 ? O GLY A 150 N VAL A 31  ? N VAL A 34  
AA1 3 4 N ILE A 32  ? N ILE A 35  O ILE A 102 ? O ILE A 105 
AA1 4 5 N VAL A 103 ? N VAL A 106 O ALA A 114 ? O ALA A 117 
AA1 5 6 N VAL A 113 ? N VAL A 116 O LEU A 121 ? O LEU A 124 
AA2 1 2 N GLY A 18  ? N GLY A 21  O LEU A 135 ? O LEU A 138 
AA2 2 3 O GLY A 136 ? O GLY A 139 N ASP A 46  ? N ASP A 49  
AA2 3 4 N LEU A 47  ? N LEU A 50  O PHE A 61  ? O PHE A 64  
AA2 4 5 N ARG A 66  ? N ARG A 69  O CYS A 72  ? O CYS A 75  
AA2 5 6 N ILE A 79  ? N ILE A 82  O LYS A 82  ? O LYS A 85  
AA3 1 2 N GLY A 18  ? N GLY A 21  O LEU A 135 ? O LEU A 138 
AA3 2 3 O GLY A 136 ? O GLY A 139 N ASP A 46  ? N ASP A 49  
AA3 3 4 N LEU A 47  ? N LEU A 50  O PHE A 61  ? O PHE A 64  
AA3 4 5 N ARG A 66  ? N ARG A 69  O CYS A 72  ? O CYS A 75  
AA3 5 6 N ILE A 73  ? N ILE A 76  O THR A 89  ? O THR A 92  
AA4 1 2 N GLN B 6   ? N GLN B 9   O PHE B 148 ? O PHE B 151 
AA4 2 3 O GLY B 147 ? O GLY B 150 N VAL B 31  ? N VAL B 34  
AA4 3 4 N ILE B 32  ? N ILE B 35  O ILE B 102 ? O ILE B 105 
AA4 4 5 N MET B 105 ? N MET B 108 O GLN B 112 ? O GLN B 115 
AA4 5 6 N VAL B 113 ? N VAL B 116 O THR B 120 ? O THR B 123 
AA5 1 2 N GLY B 18  ? N GLY B 21  O LEU B 135 ? O LEU B 138 
AA5 2 3 O THR B 134 ? O THR B 137 N GLN B 48  ? N GLN B 51  
AA5 3 4 N LEU B 47  ? N LEU B 50  O PHE B 61  ? O PHE B 64  
AA5 4 5 N ARG B 66  ? N ARG B 69  O CYS B 72  ? O CYS B 75  
AA5 5 6 N ILE B 79  ? N ILE B 82  O LYS B 82  ? O LYS B 85  
AA6 1 2 N GLY B 18  ? N GLY B 21  O LEU B 135 ? O LEU B 138 
AA6 2 3 O THR B 134 ? O THR B 137 N GLN B 48  ? N GLN B 51  
AA6 3 4 N LEU B 47  ? N LEU B 50  O PHE B 61  ? O PHE B 64  
AA6 4 5 N ARG B 66  ? N ARG B 69  O CYS B 72  ? O CYS B 75  
AA6 5 6 N ILE B 73  ? N ILE B 76  O THR B 89  ? O THR B 92  
# 
_pdbx_entry_details.entry_id                   9FYJ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HZ3 B LYS 143 ? ? O B HOH 301 ? ? 1.51 
2 1 O   B HOH 424 ? ? O B HOH 435 ? ? 1.97 
3 1 O   A HOH 437 ? ? O A HOH 470 ? ? 2.00 
4 1 O   A HOH 442 ? ? O A HOH 449 ? ? 2.11 
5 1 O   B HOH 337 ? ? O B HOH 459 ? ? 2.16 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1  1 HD1  B HIS 38  ? ? 1_555 O    A HOH 439 ? ? 2_655 1.22 
2  1 OD1  A ASP 94  ? B 1_555 HD22 B ASN 7   ? ? 4_445 1.41 
3  1 HE21 A GLN 9   ? ? 1_555 O    B HOH 457 ? ? 1_455 1.54 
4  1 HD21 B ASN 14  ? ? 1_555 O    A HOH 465 ? ? 1_655 1.55 
5  1 O    A HOH 465 ? ? 1_555 O    B HOH 457 ? ? 1_455 1.83 
6  1 ND1  B HIS 38  ? ? 1_555 O    A HOH 439 ? ? 2_655 1.84 
7  1 NE2  B HIS 147 ? ? 1_555 O    A HOH 439 ? ? 2_655 1.85 
8  1 O    A HOH 360 ? ? 1_555 O    A HOH 465 ? ? 2_554 1.88 
9  1 O    A HOH 424 ? ? 1_555 O    B HOH 356 ? ? 3_655 1.98 
10 1 O    A HOH 375 ? ? 1_555 O    B HOH 301 ? ? 2_654 1.99 
11 1 NE2  B GLN 26  ? B 1_555 O    B HOH 429 ? ? 2_654 2.19 
# 
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 ARG A 72  ? ? 57.13   -133.08 
2 1 LYS B 57  ? ? -160.08 113.40  
3 1 ARG B 72  ? ? 59.25   -132.89 
4 1 GLU B 100 ? ? 80.24   1.65    
5 1 SER B 154 ? ? -105.15 62.95   
6 1 SER B 154 ? ? -104.86 62.49   
# 
_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                       491 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.05 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 4   ? A SER 1   
2 1 Y 1 A LEU 5   ? A LEU 2   
3 1 Y 1 A ASN 6   ? A ASN 3   
4 1 Y 1 A ASN 7   ? A ASN 4   
5 1 Y 1 B SER 4   ? B SER 1   
6 1 Y 1 B LEU 5   ? B LEU 2   
7 1 Y 1 B ASN 6   ? B ASN 3   
8 1 Y 1 B ASP 156 ? B ASP 153 
# 
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 
A1IHE C2   C  N N 1   
A1IHE C3   C  N R 2   
A1IHE O1   O  N N 3   
A1IHE C5   C  N R 4   
A1IHE C7   C  Y N 5   
A1IHE O4   O  N N 6   
A1IHE C11  C  Y N 7   
A1IHE C13  C  Y N 8   
A1IHE C14  C  Y N 9   
A1IHE C15  C  N R 10  
A1IHE C17  C  N N 11  
A1IHE C18  C  N N 12  
A1IHE C19  C  N N 13  
A1IHE C20  C  N S 14  
A1IHE C22  C  N N 15  
A1IHE C23  C  Y N 16  
A1IHE C25  C  Y N 17  
A1IHE C26  C  Y N 18  
A1IHE C27  C  Y N 19  
A1IHE C28  C  Y N 20  
A1IHE C29  C  N N 21  
A1IHE C32  C  Y N 22  
A1IHE C33  C  Y N 23  
A1IHE C35  C  N N 24  
A1IHE C36  C  N S 25  
A1IHE C8   C  Y N 26  
A1IHE C9   C  Y N 27  
A1IHE N24  N  Y N 28  
A1IHE N34  N  Y N 29  
A1IHE O16  O  N N 30  
A1IHE O21  O  N N 31  
A1IHE O30  O  N N 32  
A1IHE O31  O  N N 33  
A1IHE O37  O  N N 34  
A1IHE S6   S  N N 35  
A1IHE CL10 CL N N 36  
A1IHE CL12 CL N N 37  
A1IHE H2A  H  N N 38  
A1IHE H2B  H  N N 39  
A1IHE H3   H  N N 40  
A1IHE H1   H  N N 41  
A1IHE H5   H  N N 42  
A1IHE H13  H  N N 43  
A1IHE H14  H  N N 44  
A1IHE H15  H  N N 45  
A1IHE H17A H  N N 46  
A1IHE H17B H  N N 47  
A1IHE H19  H  N N 48  
A1IHE H20  H  N N 49  
A1IHE H22A H  N N 50  
A1IHE H22B H  N N 51  
A1IHE H26  H  N N 52  
A1IHE H27  H  N N 53  
A1IHE H32  H  N N 54  
A1IHE H35B H  N N 55  
A1IHE H35A H  N N 56  
A1IHE H35C H  N N 57  
A1IHE H36  H  N N 58  
A1IHE H8   H  N N 59  
A1IHE H2   H  N N 60  
A1IHE H37  H  N N 61  
ALA   N    N  N N 62  
ALA   CA   C  N S 63  
ALA   C    C  N N 64  
ALA   O    O  N N 65  
ALA   CB   C  N N 66  
ALA   OXT  O  N N 67  
ALA   H    H  N N 68  
ALA   H2   H  N N 69  
ALA   HA   H  N N 70  
ALA   HB1  H  N N 71  
ALA   HB2  H  N N 72  
ALA   HB3  H  N N 73  
ALA   HXT  H  N N 74  
ARG   N    N  N N 75  
ARG   CA   C  N S 76  
ARG   C    C  N N 77  
ARG   O    O  N N 78  
ARG   CB   C  N N 79  
ARG   CG   C  N N 80  
ARG   CD   C  N N 81  
ARG   NE   N  N N 82  
ARG   CZ   C  N N 83  
ARG   NH1  N  N N 84  
ARG   NH2  N  N N 85  
ARG   OXT  O  N N 86  
ARG   H    H  N N 87  
ARG   H2   H  N N 88  
ARG   HA   H  N N 89  
ARG   HB2  H  N N 90  
ARG   HB3  H  N N 91  
ARG   HG2  H  N N 92  
ARG   HG3  H  N N 93  
ARG   HD2  H  N N 94  
ARG   HD3  H  N N 95  
ARG   HE   H  N N 96  
ARG   HH11 H  N N 97  
ARG   HH12 H  N N 98  
ARG   HH21 H  N N 99  
ARG   HH22 H  N N 100 
ARG   HXT  H  N N 101 
ASN   N    N  N N 102 
ASN   CA   C  N S 103 
ASN   C    C  N N 104 
ASN   O    O  N N 105 
ASN   CB   C  N N 106 
ASN   CG   C  N N 107 
ASN   OD1  O  N N 108 
ASN   ND2  N  N N 109 
ASN   OXT  O  N N 110 
ASN   H    H  N N 111 
ASN   H2   H  N N 112 
ASN   HA   H  N N 113 
ASN   HB2  H  N N 114 
ASN   HB3  H  N N 115 
ASN   HD21 H  N N 116 
ASN   HD22 H  N N 117 
ASN   HXT  H  N N 118 
ASP   N    N  N N 119 
ASP   CA   C  N S 120 
ASP   C    C  N N 121 
ASP   O    O  N N 122 
ASP   CB   C  N N 123 
ASP   CG   C  N N 124 
ASP   OD1  O  N N 125 
ASP   OD2  O  N N 126 
ASP   OXT  O  N N 127 
ASP   H    H  N N 128 
ASP   H2   H  N N 129 
ASP   HA   H  N N 130 
ASP   HB2  H  N N 131 
ASP   HB3  H  N N 132 
ASP   HD2  H  N N 133 
ASP   HXT  H  N N 134 
CL    CL   CL N N 135 
CYS   N    N  N N 136 
CYS   CA   C  N R 137 
CYS   C    C  N N 138 
CYS   O    O  N N 139 
CYS   CB   C  N N 140 
CYS   SG   S  N N 141 
CYS   OXT  O  N N 142 
CYS   H    H  N N 143 
CYS   H2   H  N N 144 
CYS   HA   H  N N 145 
CYS   HB2  H  N N 146 
CYS   HB3  H  N N 147 
CYS   HG   H  N N 148 
CYS   HXT  H  N N 149 
GLN   N    N  N N 150 
GLN   CA   C  N S 151 
GLN   C    C  N N 152 
GLN   O    O  N N 153 
GLN   CB   C  N N 154 
GLN   CG   C  N N 155 
GLN   CD   C  N N 156 
GLN   OE1  O  N N 157 
GLN   NE2  N  N N 158 
GLN   OXT  O  N N 159 
GLN   H    H  N N 160 
GLN   H2   H  N N 161 
GLN   HA   H  N N 162 
GLN   HB2  H  N N 163 
GLN   HB3  H  N N 164 
GLN   HG2  H  N N 165 
GLN   HG3  H  N N 166 
GLN   HE21 H  N N 167 
GLN   HE22 H  N N 168 
GLN   HXT  H  N N 169 
GLU   N    N  N N 170 
GLU   CA   C  N S 171 
GLU   C    C  N N 172 
GLU   O    O  N N 173 
GLU   CB   C  N N 174 
GLU   CG   C  N N 175 
GLU   CD   C  N N 176 
GLU   OE1  O  N N 177 
GLU   OE2  O  N N 178 
GLU   OXT  O  N N 179 
GLU   H    H  N N 180 
GLU   H2   H  N N 181 
GLU   HA   H  N N 182 
GLU   HB2  H  N N 183 
GLU   HB3  H  N N 184 
GLU   HG2  H  N N 185 
GLU   HG3  H  N N 186 
GLU   HE2  H  N N 187 
GLU   HXT  H  N N 188 
GLY   N    N  N N 189 
GLY   CA   C  N N 190 
GLY   C    C  N N 191 
GLY   O    O  N N 192 
GLY   OXT  O  N N 193 
GLY   H    H  N N 194 
GLY   H2   H  N N 195 
GLY   HA2  H  N N 196 
GLY   HA3  H  N N 197 
GLY   HXT  H  N N 198 
HIS   N    N  N N 199 
HIS   CA   C  N S 200 
HIS   C    C  N N 201 
HIS   O    O  N N 202 
HIS   CB   C  N N 203 
HIS   CG   C  Y N 204 
HIS   ND1  N  Y N 205 
HIS   CD2  C  Y N 206 
HIS   CE1  C  Y N 207 
HIS   NE2  N  Y N 208 
HIS   OXT  O  N N 209 
HIS   H    H  N N 210 
HIS   H2   H  N N 211 
HIS   HA   H  N N 212 
HIS   HB2  H  N N 213 
HIS   HB3  H  N N 214 
HIS   HD1  H  N N 215 
HIS   HD2  H  N N 216 
HIS   HE1  H  N N 217 
HIS   HE2  H  N N 218 
HIS   HXT  H  N N 219 
HOH   O    O  N N 220 
HOH   H1   H  N N 221 
HOH   H2   H  N N 222 
ILE   N    N  N N 223 
ILE   CA   C  N S 224 
ILE   C    C  N N 225 
ILE   O    O  N N 226 
ILE   CB   C  N S 227 
ILE   CG1  C  N N 228 
ILE   CG2  C  N N 229 
ILE   CD1  C  N N 230 
ILE   OXT  O  N N 231 
ILE   H    H  N N 232 
ILE   H2   H  N N 233 
ILE   HA   H  N N 234 
ILE   HB   H  N N 235 
ILE   HG12 H  N N 236 
ILE   HG13 H  N N 237 
ILE   HG21 H  N N 238 
ILE   HG22 H  N N 239 
ILE   HG23 H  N N 240 
ILE   HD11 H  N N 241 
ILE   HD12 H  N N 242 
ILE   HD13 H  N N 243 
ILE   HXT  H  N N 244 
LEU   N    N  N N 245 
LEU   CA   C  N S 246 
LEU   C    C  N N 247 
LEU   O    O  N N 248 
LEU   CB   C  N N 249 
LEU   CG   C  N N 250 
LEU   CD1  C  N N 251 
LEU   CD2  C  N N 252 
LEU   OXT  O  N N 253 
LEU   H    H  N N 254 
LEU   H2   H  N N 255 
LEU   HA   H  N N 256 
LEU   HB2  H  N N 257 
LEU   HB3  H  N N 258 
LEU   HG   H  N N 259 
LEU   HD11 H  N N 260 
LEU   HD12 H  N N 261 
LEU   HD13 H  N N 262 
LEU   HD21 H  N N 263 
LEU   HD22 H  N N 264 
LEU   HD23 H  N N 265 
LEU   HXT  H  N N 266 
LYS   N    N  N N 267 
LYS   CA   C  N S 268 
LYS   C    C  N N 269 
LYS   O    O  N N 270 
LYS   CB   C  N N 271 
LYS   CG   C  N N 272 
LYS   CD   C  N N 273 
LYS   CE   C  N N 274 
LYS   NZ   N  N N 275 
LYS   OXT  O  N N 276 
LYS   H    H  N N 277 
LYS   H2   H  N N 278 
LYS   HA   H  N N 279 
LYS   HB2  H  N N 280 
LYS   HB3  H  N N 281 
LYS   HG2  H  N N 282 
LYS   HG3  H  N N 283 
LYS   HD2  H  N N 284 
LYS   HD3  H  N N 285 
LYS   HE2  H  N N 286 
LYS   HE3  H  N N 287 
LYS   HZ1  H  N N 288 
LYS   HZ2  H  N N 289 
LYS   HZ3  H  N N 290 
LYS   HXT  H  N N 291 
MET   N    N  N N 292 
MET   CA   C  N S 293 
MET   C    C  N N 294 
MET   O    O  N N 295 
MET   CB   C  N N 296 
MET   CG   C  N N 297 
MET   SD   S  N N 298 
MET   CE   C  N N 299 
MET   OXT  O  N N 300 
MET   H    H  N N 301 
MET   H2   H  N N 302 
MET   HA   H  N N 303 
MET   HB2  H  N N 304 
MET   HB3  H  N N 305 
MET   HG2  H  N N 306 
MET   HG3  H  N N 307 
MET   HE1  H  N N 308 
MET   HE2  H  N N 309 
MET   HE3  H  N N 310 
MET   HXT  H  N N 311 
PHE   N    N  N N 312 
PHE   CA   C  N S 313 
PHE   C    C  N N 314 
PHE   O    O  N N 315 
PHE   CB   C  N N 316 
PHE   CG   C  Y N 317 
PHE   CD1  C  Y N 318 
PHE   CD2  C  Y N 319 
PHE   CE1  C  Y N 320 
PHE   CE2  C  Y N 321 
PHE   CZ   C  Y N 322 
PHE   OXT  O  N N 323 
PHE   H    H  N N 324 
PHE   H2   H  N N 325 
PHE   HA   H  N N 326 
PHE   HB2  H  N N 327 
PHE   HB3  H  N N 328 
PHE   HD1  H  N N 329 
PHE   HD2  H  N N 330 
PHE   HE1  H  N N 331 
PHE   HE2  H  N N 332 
PHE   HZ   H  N N 333 
PHE   HXT  H  N N 334 
PRO   N    N  N N 335 
PRO   CA   C  N S 336 
PRO   C    C  N N 337 
PRO   O    O  N N 338 
PRO   CB   C  N N 339 
PRO   CG   C  N N 340 
PRO   CD   C  N N 341 
PRO   OXT  O  N N 342 
PRO   H    H  N N 343 
PRO   HA   H  N N 344 
PRO   HB2  H  N N 345 
PRO   HB3  H  N N 346 
PRO   HG2  H  N N 347 
PRO   HG3  H  N N 348 
PRO   HD2  H  N N 349 
PRO   HD3  H  N N 350 
PRO   HXT  H  N N 351 
SER   N    N  N N 352 
SER   CA   C  N S 353 
SER   C    C  N N 354 
SER   O    O  N N 355 
SER   CB   C  N N 356 
SER   OG   O  N N 357 
SER   OXT  O  N N 358 
SER   H    H  N N 359 
SER   H2   H  N N 360 
SER   HA   H  N N 361 
SER   HB2  H  N N 362 
SER   HB3  H  N N 363 
SER   HG   H  N N 364 
SER   HXT  H  N N 365 
THR   N    N  N N 366 
THR   CA   C  N S 367 
THR   C    C  N N 368 
THR   O    O  N N 369 
THR   CB   C  N R 370 
THR   OG1  O  N N 371 
THR   CG2  C  N N 372 
THR   OXT  O  N N 373 
THR   H    H  N N 374 
THR   H2   H  N N 375 
THR   HA   H  N N 376 
THR   HB   H  N N 377 
THR   HG1  H  N N 378 
THR   HG21 H  N N 379 
THR   HG22 H  N N 380 
THR   HG23 H  N N 381 
THR   HXT  H  N N 382 
TRP   N    N  N N 383 
TRP   CA   C  N S 384 
TRP   C    C  N N 385 
TRP   O    O  N N 386 
TRP   CB   C  N N 387 
TRP   CG   C  Y N 388 
TRP   CD1  C  Y N 389 
TRP   CD2  C  Y N 390 
TRP   NE1  N  Y N 391 
TRP   CE2  C  Y N 392 
TRP   CE3  C  Y N 393 
TRP   CZ2  C  Y N 394 
TRP   CZ3  C  Y N 395 
TRP   CH2  C  Y N 396 
TRP   OXT  O  N N 397 
TRP   H    H  N N 398 
TRP   H2   H  N N 399 
TRP   HA   H  N N 400 
TRP   HB2  H  N N 401 
TRP   HB3  H  N N 402 
TRP   HD1  H  N N 403 
TRP   HE1  H  N N 404 
TRP   HE3  H  N N 405 
TRP   HZ2  H  N N 406 
TRP   HZ3  H  N N 407 
TRP   HH2  H  N N 408 
TRP   HXT  H  N N 409 
TYR   N    N  N N 410 
TYR   CA   C  N S 411 
TYR   C    C  N N 412 
TYR   O    O  N N 413 
TYR   CB   C  N N 414 
TYR   CG   C  Y N 415 
TYR   CD1  C  Y N 416 
TYR   CD2  C  Y N 417 
TYR   CE1  C  Y N 418 
TYR   CE2  C  Y N 419 
TYR   CZ   C  Y N 420 
TYR   OH   O  N N 421 
TYR   OXT  O  N N 422 
TYR   H    H  N N 423 
TYR   H2   H  N N 424 
TYR   HA   H  N N 425 
TYR   HB2  H  N N 426 
TYR   HB3  H  N N 427 
TYR   HD1  H  N N 428 
TYR   HD2  H  N N 429 
TYR   HE1  H  N N 430 
TYR   HE2  H  N N 431 
TYR   HH   H  N N 432 
TYR   HXT  H  N N 433 
VAL   N    N  N N 434 
VAL   CA   C  N S 435 
VAL   C    C  N N 436 
VAL   O    O  N N 437 
VAL   CB   C  N N 438 
VAL   CG1  C  N N 439 
VAL   CG2  C  N N 440 
VAL   OXT  O  N N 441 
VAL   H    H  N N 442 
VAL   H2   H  N N 443 
VAL   HA   H  N N 444 
VAL   HB   H  N N 445 
VAL   HG11 H  N N 446 
VAL   HG12 H  N N 447 
VAL   HG13 H  N N 448 
VAL   HG21 H  N N 449 
VAL   HG22 H  N N 450 
VAL   HG23 H  N N 451 
VAL   HXT  H  N N 452 
# 
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 
A1IHE O1  C2   sing N N 1   
A1IHE C2  C3   sing N N 2   
A1IHE C3  O4   sing N N 3   
A1IHE O4  C5   sing N N 4   
A1IHE C5  S6   sing N N 5   
A1IHE S6  C7   sing N N 6   
A1IHE C7  C8   doub Y N 7   
A1IHE C8  C9   sing Y N 8   
A1IHE C9  CL10 sing N N 9   
A1IHE C9  C11  doub Y N 10  
A1IHE C11 CL12 sing N N 11  
A1IHE C11 C13  sing Y N 12  
A1IHE C13 C14  doub Y N 13  
A1IHE C5  C15  sing N N 14  
A1IHE C15 O16  sing N N 15  
A1IHE O16 C17  sing N N 16  
A1IHE C17 C18  sing N N 17  
A1IHE C18 C19  trip N N 18  
A1IHE C15 C20  sing N N 19  
A1IHE C20 O21  sing N N 20  
A1IHE O21 C22  sing N N 21  
A1IHE C22 C23  sing N N 22  
A1IHE C23 N24  doub Y N 23  
A1IHE N24 C25  sing Y N 24  
A1IHE C25 C26  doub Y N 25  
A1IHE C26 C27  sing Y N 26  
A1IHE C27 C28  doub Y N 27  
A1IHE C28 C29  sing N N 28  
A1IHE C29 O30  sing N N 29  
A1IHE C29 O31  doub N N 30  
A1IHE C28 C32  sing Y N 31  
A1IHE C25 C33  sing Y N 32  
A1IHE C33 N34  sing Y N 33  
A1IHE N34 C35  sing N N 34  
A1IHE C20 C36  sing N N 35  
A1IHE C36 O37  sing N N 36  
A1IHE C36 C3   sing N N 37  
A1IHE C14 C7   sing Y N 38  
A1IHE N34 C23  sing Y N 39  
A1IHE C33 C32  doub Y N 40  
A1IHE C2  H2A  sing N N 41  
A1IHE C2  H2B  sing N N 42  
A1IHE C3  H3   sing N N 43  
A1IHE O1  H1   sing N N 44  
A1IHE C5  H5   sing N N 45  
A1IHE C13 H13  sing N N 46  
A1IHE C14 H14  sing N N 47  
A1IHE C15 H15  sing N N 48  
A1IHE C17 H17A sing N N 49  
A1IHE C17 H17B sing N N 50  
A1IHE C19 H19  sing N N 51  
A1IHE C20 H20  sing N N 52  
A1IHE C22 H22A sing N N 53  
A1IHE C22 H22B sing N N 54  
A1IHE C26 H26  sing N N 55  
A1IHE C27 H27  sing N N 56  
A1IHE C32 H32  sing N N 57  
A1IHE C35 H35B sing N N 58  
A1IHE C35 H35A sing N N 59  
A1IHE C35 H35C sing N N 60  
A1IHE C36 H36  sing N N 61  
A1IHE C8  H8   sing N N 62  
A1IHE O30 H2   sing N N 63  
A1IHE O37 H37  sing N N 64  
ALA   N   CA   sing N N 65  
ALA   N   H    sing N N 66  
ALA   N   H2   sing N N 67  
ALA   CA  C    sing N N 68  
ALA   CA  CB   sing N N 69  
ALA   CA  HA   sing N N 70  
ALA   C   O    doub N N 71  
ALA   C   OXT  sing N N 72  
ALA   CB  HB1  sing N N 73  
ALA   CB  HB2  sing N N 74  
ALA   CB  HB3  sing N N 75  
ALA   OXT HXT  sing N N 76  
ARG   N   CA   sing N N 77  
ARG   N   H    sing N N 78  
ARG   N   H2   sing N N 79  
ARG   CA  C    sing N N 80  
ARG   CA  CB   sing N N 81  
ARG   CA  HA   sing N N 82  
ARG   C   O    doub N N 83  
ARG   C   OXT  sing N N 84  
ARG   CB  CG   sing N N 85  
ARG   CB  HB2  sing N N 86  
ARG   CB  HB3  sing N N 87  
ARG   CG  CD   sing N N 88  
ARG   CG  HG2  sing N N 89  
ARG   CG  HG3  sing N N 90  
ARG   CD  NE   sing N N 91  
ARG   CD  HD2  sing N N 92  
ARG   CD  HD3  sing N N 93  
ARG   NE  CZ   sing N N 94  
ARG   NE  HE   sing N N 95  
ARG   CZ  NH1  sing N N 96  
ARG   CZ  NH2  doub N N 97  
ARG   NH1 HH11 sing N N 98  
ARG   NH1 HH12 sing N N 99  
ARG   NH2 HH21 sing N N 100 
ARG   NH2 HH22 sing N N 101 
ARG   OXT HXT  sing N N 102 
ASN   N   CA   sing N N 103 
ASN   N   H    sing N N 104 
ASN   N   H2   sing N N 105 
ASN   CA  C    sing N N 106 
ASN   CA  CB   sing N N 107 
ASN   CA  HA   sing N N 108 
ASN   C   O    doub N N 109 
ASN   C   OXT  sing N N 110 
ASN   CB  CG   sing N N 111 
ASN   CB  HB2  sing N N 112 
ASN   CB  HB3  sing N N 113 
ASN   CG  OD1  doub N N 114 
ASN   CG  ND2  sing N N 115 
ASN   ND2 HD21 sing N N 116 
ASN   ND2 HD22 sing N N 117 
ASN   OXT HXT  sing N N 118 
ASP   N   CA   sing N N 119 
ASP   N   H    sing N N 120 
ASP   N   H2   sing N N 121 
ASP   CA  C    sing N N 122 
ASP   CA  CB   sing N N 123 
ASP   CA  HA   sing N N 124 
ASP   C   O    doub N N 125 
ASP   C   OXT  sing N N 126 
ASP   CB  CG   sing N N 127 
ASP   CB  HB2  sing N N 128 
ASP   CB  HB3  sing N N 129 
ASP   CG  OD1  doub N N 130 
ASP   CG  OD2  sing N N 131 
ASP   OD2 HD2  sing N N 132 
ASP   OXT HXT  sing N N 133 
CYS   N   CA   sing N N 134 
CYS   N   H    sing N N 135 
CYS   N   H2   sing N N 136 
CYS   CA  C    sing N N 137 
CYS   CA  CB   sing N N 138 
CYS   CA  HA   sing N N 139 
CYS   C   O    doub N N 140 
CYS   C   OXT  sing N N 141 
CYS   CB  SG   sing N N 142 
CYS   CB  HB2  sing N N 143 
CYS   CB  HB3  sing N N 144 
CYS   SG  HG   sing N N 145 
CYS   OXT HXT  sing N N 146 
GLN   N   CA   sing N N 147 
GLN   N   H    sing N N 148 
GLN   N   H2   sing N N 149 
GLN   CA  C    sing N N 150 
GLN   CA  CB   sing N N 151 
GLN   CA  HA   sing N N 152 
GLN   C   O    doub N N 153 
GLN   C   OXT  sing N N 154 
GLN   CB  CG   sing N N 155 
GLN   CB  HB2  sing N N 156 
GLN   CB  HB3  sing N N 157 
GLN   CG  CD   sing N N 158 
GLN   CG  HG2  sing N N 159 
GLN   CG  HG3  sing N N 160 
GLN   CD  OE1  doub N N 161 
GLN   CD  NE2  sing N N 162 
GLN   NE2 HE21 sing N N 163 
GLN   NE2 HE22 sing N N 164 
GLN   OXT HXT  sing N N 165 
GLU   N   CA   sing N N 166 
GLU   N   H    sing N N 167 
GLU   N   H2   sing N N 168 
GLU   CA  C    sing N N 169 
GLU   CA  CB   sing N N 170 
GLU   CA  HA   sing N N 171 
GLU   C   O    doub N N 172 
GLU   C   OXT  sing N N 173 
GLU   CB  CG   sing N N 174 
GLU   CB  HB2  sing N N 175 
GLU   CB  HB3  sing N N 176 
GLU   CG  CD   sing N N 177 
GLU   CG  HG2  sing N N 178 
GLU   CG  HG3  sing N N 179 
GLU   CD  OE1  doub N N 180 
GLU   CD  OE2  sing N N 181 
GLU   OE2 HE2  sing N N 182 
GLU   OXT HXT  sing N N 183 
GLY   N   CA   sing N N 184 
GLY   N   H    sing N N 185 
GLY   N   H2   sing N N 186 
GLY   CA  C    sing N N 187 
GLY   CA  HA2  sing N N 188 
GLY   CA  HA3  sing N N 189 
GLY   C   O    doub N N 190 
GLY   C   OXT  sing N N 191 
GLY   OXT HXT  sing N N 192 
HIS   N   CA   sing N N 193 
HIS   N   H    sing N N 194 
HIS   N   H2   sing N N 195 
HIS   CA  C    sing N N 196 
HIS   CA  CB   sing N N 197 
HIS   CA  HA   sing N N 198 
HIS   C   O    doub N N 199 
HIS   C   OXT  sing N N 200 
HIS   CB  CG   sing N N 201 
HIS   CB  HB2  sing N N 202 
HIS   CB  HB3  sing N N 203 
HIS   CG  ND1  sing Y N 204 
HIS   CG  CD2  doub Y N 205 
HIS   ND1 CE1  doub Y N 206 
HIS   ND1 HD1  sing N N 207 
HIS   CD2 NE2  sing Y N 208 
HIS   CD2 HD2  sing N N 209 
HIS   CE1 NE2  sing Y N 210 
HIS   CE1 HE1  sing N N 211 
HIS   NE2 HE2  sing N N 212 
HIS   OXT HXT  sing N N 213 
HOH   O   H1   sing N N 214 
HOH   O   H2   sing N N 215 
ILE   N   CA   sing N N 216 
ILE   N   H    sing N N 217 
ILE   N   H2   sing N N 218 
ILE   CA  C    sing N N 219 
ILE   CA  CB   sing N N 220 
ILE   CA  HA   sing N N 221 
ILE   C   O    doub N N 222 
ILE   C   OXT  sing N N 223 
ILE   CB  CG1  sing N N 224 
ILE   CB  CG2  sing N N 225 
ILE   CB  HB   sing N N 226 
ILE   CG1 CD1  sing N N 227 
ILE   CG1 HG12 sing N N 228 
ILE   CG1 HG13 sing N N 229 
ILE   CG2 HG21 sing N N 230 
ILE   CG2 HG22 sing N N 231 
ILE   CG2 HG23 sing N N 232 
ILE   CD1 HD11 sing N N 233 
ILE   CD1 HD12 sing N N 234 
ILE   CD1 HD13 sing N N 235 
ILE   OXT HXT  sing N N 236 
LEU   N   CA   sing N N 237 
LEU   N   H    sing N N 238 
LEU   N   H2   sing N N 239 
LEU   CA  C    sing N N 240 
LEU   CA  CB   sing N N 241 
LEU   CA  HA   sing N N 242 
LEU   C   O    doub N N 243 
LEU   C   OXT  sing N N 244 
LEU   CB  CG   sing N N 245 
LEU   CB  HB2  sing N N 246 
LEU   CB  HB3  sing N N 247 
LEU   CG  CD1  sing N N 248 
LEU   CG  CD2  sing N N 249 
LEU   CG  HG   sing N N 250 
LEU   CD1 HD11 sing N N 251 
LEU   CD1 HD12 sing N N 252 
LEU   CD1 HD13 sing N N 253 
LEU   CD2 HD21 sing N N 254 
LEU   CD2 HD22 sing N N 255 
LEU   CD2 HD23 sing N N 256 
LEU   OXT HXT  sing N N 257 
LYS   N   CA   sing N N 258 
LYS   N   H    sing N N 259 
LYS   N   H2   sing N N 260 
LYS   CA  C    sing N N 261 
LYS   CA  CB   sing N N 262 
LYS   CA  HA   sing N N 263 
LYS   C   O    doub N N 264 
LYS   C   OXT  sing N N 265 
LYS   CB  CG   sing N N 266 
LYS   CB  HB2  sing N N 267 
LYS   CB  HB3  sing N N 268 
LYS   CG  CD   sing N N 269 
LYS   CG  HG2  sing N N 270 
LYS   CG  HG3  sing N N 271 
LYS   CD  CE   sing N N 272 
LYS   CD  HD2  sing N N 273 
LYS   CD  HD3  sing N N 274 
LYS   CE  NZ   sing N N 275 
LYS   CE  HE2  sing N N 276 
LYS   CE  HE3  sing N N 277 
LYS   NZ  HZ1  sing N N 278 
LYS   NZ  HZ2  sing N N 279 
LYS   NZ  HZ3  sing N N 280 
LYS   OXT HXT  sing N N 281 
MET   N   CA   sing N N 282 
MET   N   H    sing N N 283 
MET   N   H2   sing N N 284 
MET   CA  C    sing N N 285 
MET   CA  CB   sing N N 286 
MET   CA  HA   sing N N 287 
MET   C   O    doub N N 288 
MET   C   OXT  sing N N 289 
MET   CB  CG   sing N N 290 
MET   CB  HB2  sing N N 291 
MET   CB  HB3  sing N N 292 
MET   CG  SD   sing N N 293 
MET   CG  HG2  sing N N 294 
MET   CG  HG3  sing N N 295 
MET   SD  CE   sing N N 296 
MET   CE  HE1  sing N N 297 
MET   CE  HE2  sing N N 298 
MET   CE  HE3  sing N N 299 
MET   OXT HXT  sing N N 300 
PHE   N   CA   sing N N 301 
PHE   N   H    sing N N 302 
PHE   N   H2   sing N N 303 
PHE   CA  C    sing N N 304 
PHE   CA  CB   sing N N 305 
PHE   CA  HA   sing N N 306 
PHE   C   O    doub N N 307 
PHE   C   OXT  sing N N 308 
PHE   CB  CG   sing N N 309 
PHE   CB  HB2  sing N N 310 
PHE   CB  HB3  sing N N 311 
PHE   CG  CD1  doub Y N 312 
PHE   CG  CD2  sing Y N 313 
PHE   CD1 CE1  sing Y N 314 
PHE   CD1 HD1  sing N N 315 
PHE   CD2 CE2  doub Y N 316 
PHE   CD2 HD2  sing N N 317 
PHE   CE1 CZ   doub Y N 318 
PHE   CE1 HE1  sing N N 319 
PHE   CE2 CZ   sing Y N 320 
PHE   CE2 HE2  sing N N 321 
PHE   CZ  HZ   sing N N 322 
PHE   OXT HXT  sing N N 323 
PRO   N   CA   sing N N 324 
PRO   N   CD   sing N N 325 
PRO   N   H    sing N N 326 
PRO   CA  C    sing N N 327 
PRO   CA  CB   sing N N 328 
PRO   CA  HA   sing N N 329 
PRO   C   O    doub N N 330 
PRO   C   OXT  sing N N 331 
PRO   CB  CG   sing N N 332 
PRO   CB  HB2  sing N N 333 
PRO   CB  HB3  sing N N 334 
PRO   CG  CD   sing N N 335 
PRO   CG  HG2  sing N N 336 
PRO   CG  HG3  sing N N 337 
PRO   CD  HD2  sing N N 338 
PRO   CD  HD3  sing N N 339 
PRO   OXT HXT  sing N N 340 
SER   N   CA   sing N N 341 
SER   N   H    sing N N 342 
SER   N   H2   sing N N 343 
SER   CA  C    sing N N 344 
SER   CA  CB   sing N N 345 
SER   CA  HA   sing N N 346 
SER   C   O    doub N N 347 
SER   C   OXT  sing N N 348 
SER   CB  OG   sing N N 349 
SER   CB  HB2  sing N N 350 
SER   CB  HB3  sing N N 351 
SER   OG  HG   sing N N 352 
SER   OXT HXT  sing N N 353 
THR   N   CA   sing N N 354 
THR   N   H    sing N N 355 
THR   N   H2   sing N N 356 
THR   CA  C    sing N N 357 
THR   CA  CB   sing N N 358 
THR   CA  HA   sing N N 359 
THR   C   O    doub N N 360 
THR   C   OXT  sing N N 361 
THR   CB  OG1  sing N N 362 
THR   CB  CG2  sing N N 363 
THR   CB  HB   sing N N 364 
THR   OG1 HG1  sing N N 365 
THR   CG2 HG21 sing N N 366 
THR   CG2 HG22 sing N N 367 
THR   CG2 HG23 sing N N 368 
THR   OXT HXT  sing N N 369 
TRP   N   CA   sing N N 370 
TRP   N   H    sing N N 371 
TRP   N   H2   sing N N 372 
TRP   CA  C    sing N N 373 
TRP   CA  CB   sing N N 374 
TRP   CA  HA   sing N N 375 
TRP   C   O    doub N N 376 
TRP   C   OXT  sing N N 377 
TRP   CB  CG   sing N N 378 
TRP   CB  HB2  sing N N 379 
TRP   CB  HB3  sing N N 380 
TRP   CG  CD1  doub Y N 381 
TRP   CG  CD2  sing Y N 382 
TRP   CD1 NE1  sing Y N 383 
TRP   CD1 HD1  sing N N 384 
TRP   CD2 CE2  doub Y N 385 
TRP   CD2 CE3  sing Y N 386 
TRP   NE1 CE2  sing Y N 387 
TRP   NE1 HE1  sing N N 388 
TRP   CE2 CZ2  sing Y N 389 
TRP   CE3 CZ3  doub Y N 390 
TRP   CE3 HE3  sing N N 391 
TRP   CZ2 CH2  doub Y N 392 
TRP   CZ2 HZ2  sing N N 393 
TRP   CZ3 CH2  sing Y N 394 
TRP   CZ3 HZ3  sing N N 395 
TRP   CH2 HH2  sing N N 396 
TRP   OXT HXT  sing N N 397 
TYR   N   CA   sing N N 398 
TYR   N   H    sing N N 399 
TYR   N   H2   sing N N 400 
TYR   CA  C    sing N N 401 
TYR   CA  CB   sing N N 402 
TYR   CA  HA   sing N N 403 
TYR   C   O    doub N N 404 
TYR   C   OXT  sing N N 405 
TYR   CB  CG   sing N N 406 
TYR   CB  HB2  sing N N 407 
TYR   CB  HB3  sing N N 408 
TYR   CG  CD1  doub Y N 409 
TYR   CG  CD2  sing Y N 410 
TYR   CD1 CE1  sing Y N 411 
TYR   CD1 HD1  sing N N 412 
TYR   CD2 CE2  doub Y N 413 
TYR   CD2 HD2  sing N N 414 
TYR   CE1 CZ   doub Y N 415 
TYR   CE1 HE1  sing N N 416 
TYR   CE2 CZ   sing Y N 417 
TYR   CE2 HE2  sing N N 418 
TYR   CZ  OH   sing N N 419 
TYR   OH  HH   sing N N 420 
TYR   OXT HXT  sing N N 421 
VAL   N   CA   sing N N 422 
VAL   N   H    sing N N 423 
VAL   N   H2   sing N N 424 
VAL   CA  C    sing N N 425 
VAL   CA  CB   sing N N 426 
VAL   CA  HA   sing N N 427 
VAL   C   O    doub N N 428 
VAL   C   OXT  sing N N 429 
VAL   CB  CG1  sing N N 430 
VAL   CB  CG2  sing N N 431 
VAL   CB  HB   sing N N 432 
VAL   CG1 HG11 sing N N 433 
VAL   CG1 HG12 sing N N 434 
VAL   CG1 HG13 sing N N 435 
VAL   CG2 HG21 sing N N 436 
VAL   CG2 HG22 sing N N 437 
VAL   CG2 HG23 sing N N 438 
VAL   OXT HXT  sing N N 439 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'H2020 Marie Curie Actions of the European Commission'         'European Union' 765581                         1 
'European Union (EU)'                                          'European Union' 'EUTOPIA PhD Co-tutelle grant' 2 
'Swedish Research Council'                                     Sweden           2020-03317                     3 
'Swedish Research Council'                                     Sweden           2016-04855                     4 
'Slovenian Research Agency'                                    Slovenia         P1-0208                        5 
'Slovenian Research Agency'                                    Slovenia         J1-50026                       6 
'European Cooperation in Science and Technology (COST) action' 'European Union' CA18103                        7 
'European Cooperation in Science and Technology (COST) action' 'European Union' CA18132                        8 
'European Regional Development Fund'                           'European Union' 'OP20.05187 RI-SI-EATRIS'      9 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'in-house galectin-8N structure' 
# 
_atom_sites.entry_id                    9FYJ 
_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]   0.018626 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016057 
_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]   0.011794 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
MG 
N  
O  
P  
S  
ZN 
# 
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    . LEU   A 1 5   ? 10.26365 -5.55981  21.70010  1.000 36.34780 ?  8   LEU   A N    1 
ATOM   2    C  CA   . LEU   A 1 5   ? 9.29006  -5.94134  20.67451  1.000 30.83663 ?  8   LEU   A CA   1 
ATOM   3    C  C    . LEU   A 1 5   ? 8.58966  -4.74455  20.06791  1.000 27.05598 ?  8   LEU   A C    1 
ATOM   4    O  O    . LEU   A 1 5   ? 7.93343  -4.88643  19.06053  1.000 26.56461 ?  8   LEU   A O    1 
ATOM   5    C  CB   . LEU   A 1 5   ? 8.23607  -6.92728  21.19067  1.000 34.73541 ?  8   LEU   A CB   1 
ATOM   6    C  CG   . LEU   A 1 5   ? 8.70310  -8.35744  21.40793  1.000 36.80402 ?  8   LEU   A CG   1 
ATOM   7    C  CD1  . LEU   A 1 5   ? 9.30000  -8.37576  22.76824  1.000 37.87138 ?  8   LEU   A CD1  1 
ATOM   8    C  CD2  . LEU   A 1 5   ? 7.56329  -9.34819  21.30196  1.000 38.00464 ?  8   LEU   A CD2  1 
ATOM   9    N  N    . GLN   A 1 6   ? 8.74496  -3.55901  20.65480  1.000 26.57001 ?  9   GLN   A N    1 
ATOM   10   C  CA   . GLN   A 1 6   ? 8.12410  -2.37270  20.07650  1.000 27.28302 ?  9   GLN   A CA   1 
ATOM   11   C  C    . GLN   A 1 6   ? 8.72760  -2.00558  18.73643  1.000 25.02640 ?  9   GLN   A C    1 
ATOM   12   O  O    . GLN   A 1 6   ? 8.16194  -1.16713  18.02193  1.000 27.31296 ?  9   GLN   A O    1 
ATOM   13   C  CB   . GLN   A 1 6   ? 8.26901  -1.18205  21.03130  1.000 32.19698 ?  9   GLN   A CB   1 
ATOM   14   C  CG   . GLN   A 1 6   ? 7.25375  -1.16375  22.14596  1.000 38.69806 ?  9   GLN   A CG   1 
ATOM   15   C  CD   . GLN   A 1 6   ? 7.38142  0.05669   23.03764  1.000 44.79653 ?  9   GLN   A CD   1 
ATOM   16   O  OE1  . GLN   A 1 6   ? 6.93497  1.14807   22.68279  1.000 47.45037 ?  9   GLN   A OE1  1 
ATOM   17   N  NE2  . GLN   A 1 6   ? 7.99108  -0.12263  24.20470  1.000 46.80532 ?  9   GLN   A NE2  1 
ATOM   18   H  HA   . GLN   A 1 6   ? 7.17805  -2.54812  19.95355  1.000 32.73962 ?  9   GLN   A HA   1 
ATOM   19   H  HB2  . GLN   A 1 6   ? 9.15039  -1.21279  21.43520  1.000 38.63637 ?  9   GLN   A HB2  1 
ATOM   20   H  HB3  . GLN   A 1 6   ? 8.16508  -0.36198  20.52377  1.000 38.63637 ?  9   GLN   A HB3  1 
ATOM   21   H  HG2  . GLN   A 1 6   ? 6.36300  -1.16251  21.76194  1.000 46.43767 ?  9   GLN   A HG2  1 
ATOM   22   H  HG3  . GLN   A 1 6   ? 7.37608  -1.95214  22.69766  1.000 46.43767 ?  9   GLN   A HG3  1 
ATOM   23   H  HE21 . GLN   A 1 6   ? 8.28872  -0.90042  24.41931  1.000 56.16639 ?  9   GLN   A HE21 1 
ATOM   24   H  HE22 . GLN   A 1 6   ? 8.08800  0.53910   24.74536  1.000 56.16639 ?  9   GLN   A HE22 1 
ATOM   25   N  N    . ASN   A 1 7   ? 9.85215  -2.62120  18.37740  1.000 22.29086 ?  10  ASN   A N    1 
ATOM   26   C  CA   . ASN   A 1 7   ? 10.60046 -2.23310  17.19430  1.000 21.52512 ?  10  ASN   A CA   1 
ATOM   27   C  C    . ASN   A 1 7   ? 10.49353 -3.23529  16.05143  1.000 19.74474 ?  10  ASN   A C    1 
ATOM   28   O  O    . ASN   A 1 7   ? 11.31333 -3.20073  15.12782  1.000 19.95298 ?  10  ASN   A O    1 
ATOM   29   C  CB   . ASN   A 1 7   ? 12.04854 -1.98693  17.57747  1.000 23.32125 ?  10  ASN   A CB   1 
ATOM   30   C  CG   . ASN   A 1 7   ? 12.17052 -0.87602  18.58839  1.000 27.08493 ?  10  ASN   A CG   1 
ATOM   31   O  OD1  . ASN   A 1 7   ? 11.36765 0.05883   18.58466  1.000 27.91544 ?  10  ASN   A OD1  1 
ATOM   32   N  ND2  . ASN   A 1 7   ? 13.13257 -0.98760  19.48530  1.000 30.15895 ?  10  ASN   A ND2  1 
ATOM   33   H  H    . ASN   A 1 7   ? 10.20296 -3.27511  18.81206  1.000 26.74903 ?  10  ASN   A H    1 
ATOM   34   H  HA   . ASN   A 1 7   ? 10.22861 -1.40554  16.85110  1.000 25.83014 ?  10  ASN   A HA   1 
ATOM   35   H  HB2  . ASN   A 1 7   ? 12.41978 -2.79481  17.96528  1.000 27.98550 ?  10  ASN   A HB2  1 
ATOM   36   H  HB3  . ASN   A 1 7   ? 12.55177 -1.73690  16.78681  1.000 27.98550 ?  10  ASN   A HB3  1 
ATOM   37   H  HD21 . ASN   A 1 7   ? 13.65378 -1.67157  19.47400  1.000 36.19074 ?  10  ASN   A HD21 1 
ATOM   38   H  HD22 . ASN   A 1 7   ? 13.23813 -0.37633  20.08096  1.000 36.19074 ?  10  ASN   A HD22 1 
ATOM   39   N  N    . ILE   A 1 8   ? 9.46918  -4.08950  16.06752  1.000 19.19228 ?  11  ILE   A N    1 
ATOM   40   C  CA   . ILE   A 1 8   ? 9.24224  -5.05902  15.00636  1.000 19.46579 ?  11  ILE   A CA   1 
ATOM   41   C  C    . ILE   A 1 8   ? 7.77800  -5.04734  14.59797  1.000 18.45631 ?  11  ILE   A C    1 
ATOM   42   O  O    . ILE   A 1 8   ? 6.87601  -4.80702  15.40098  1.000 20.99416 ?  11  ILE   A O    1 
ATOM   43   C  CB   . ILE   A 1 8   ? 9.68742  -6.49155  15.38453  1.000 23.47258 ?  11  ILE   A CB   1 
ATOM   44   C  CG1  . ILE   A 1 8   ? 9.61001  -7.43448  14.17100  1.000 28.57601 ?  11  ILE   A CG1  1 
ATOM   45   C  CG2  . ILE   A 1 8   ? 8.86878  -7.02088  16.54589  1.000 24.72924 ?  11  ILE   A CG2  1 
ATOM   46   C  CD1  . ILE   A 1 8   ? 10.81963 -8.34144  14.05564  1.000 30.03689 ?  11  ILE   A CD1  1 
ATOM   47   H  H    . ILE   A 1 8   ? 8.88353  -4.12379  16.69636  1.000 23.03074 ?  11  ILE   A H    1 
ATOM   48   H  HA   . ILE   A 1 8   ? 9.76789  -4.77846  14.24094  1.000 23.35895 ?  11  ILE   A HA   1 
ATOM   49   H  HB   . ILE   A 1 8   ? 10.61502 -6.45079  15.66522  1.000 28.16710 ?  11  ILE   A HB   1 
ATOM   50   H  HG12 . ILE   A 1 8   ? 8.82207  -7.99387  14.25543  1.000 34.29121 ?  11  ILE   A HG12 1 
ATOM   51   H  HG13 . ILE   A 1 8   ? 9.55453  -6.90326  13.36129  1.000 34.29121 ?  11  ILE   A HG13 1 
ATOM   52   H  HG21 . ILE   A 1 8   ? 9.06133  -6.49120  17.33536  1.000 29.67509 ?  11  ILE   A HG21 1 
ATOM   53   H  HG22 . ILE   A 1 8   ? 9.10677  -7.94794  16.70342  1.000 29.67509 ?  11  ILE   A HG22 1 
ATOM   54   H  HG23 . ILE   A 1 8   ? 7.92673  -6.95424  16.32453  1.000 29.67509 ?  11  ILE   A HG23 1 
ATOM   55   H  HD11 . ILE   A 1 8   ? 10.70974 -8.91772  13.28316  1.000 36.04426 ?  11  ILE   A HD11 1 
ATOM   56   H  HD12 . ILE   A 1 8   ? 11.61467 -7.79572  13.95078  1.000 36.04426 ?  11  ILE   A HD12 1 
ATOM   57   H  HD13 . ILE   A 1 8   ? 10.89029 -8.87759  14.86091  1.000 36.04426 ?  11  ILE   A HD13 1 
ATOM   58   N  N    . ILE   A 1 9   ? 7.53837  -5.36051  13.34268  1.000 16.02488 ?  12  ILE   A N    1 
ATOM   59   C  CA   . ILE   A 1 9   ? 6.18916  -5.59421  12.85144  1.000 15.22201 ?  12  ILE   A CA   1 
ATOM   60   C  C    . ILE   A 1 9   ? 6.21969  -6.81729  11.96006  1.000 14.65381 ?  12  ILE   A C    1 
ATOM   61   O  O    . ILE   A 1 9   ? 7.14563  -6.99095  11.15831  1.000 15.90483 ?  12  ILE   A O    1 
ATOM   62   C  CB   . ILE   A 1 9   ? 5.61521  -4.38139  12.09365  1.000 15.15696 ?  12  ILE   A CB   1 
ATOM   63   C  CG1  . ILE   A 1 9   ? 4.18310  -4.65359  11.65534  1.000 15.95710 ?  12  ILE   A CG1  1 
ATOM   64   C  CG2  . ILE   A 1 9   ? 6.50404  -3.98627  10.92675  1.000 17.95438 ?  12  ILE   A CG2  1 
ATOM   65   C  CD1  . ILE   A 1 9   ? 3.41905  -3.41469  11.18833  1.000 17.40522 ?  12  ILE   A CD1  1 
ATOM   66   H  H    . ILE   A 1 9   ? 8.14819  -5.44614  12.74235  1.000 19.22986 ?  12  ILE   A H    1 
ATOM   67   H  HA   . ILE   A 1 9   ? 5.60645  -5.76703  13.60741  1.000 18.26641 ?  12  ILE   A HA   1 
ATOM   68   H  HB   . ILE   A 1 9   ? 5.59744  -3.62595  12.70184  1.000 18.18835 ?  12  ILE   A HB   1 
ATOM   69   H  HG12 . ILE   A 1 9   ? 4.19974  -5.28325  10.91767  1.000 19.14852 ?  12  ILE   A HG12 1 
ATOM   70   H  HG13 . ILE   A 1 9   ? 3.69714  -5.03281  12.40431  1.000 19.14852 ?  12  ILE   A HG13 1 
ATOM   71   H  HG21 . ILE   A 1 9   ? 6.31318  -3.06743  10.68137  1.000 21.54526 ?  12  ILE   A HG21 1 
ATOM   72   H  HG22 . ILE   A 1 9   ? 7.43258  -4.07119  11.19415  1.000 21.54526 ?  12  ILE   A HG22 1 
ATOM   73   H  HG23 . ILE   A 1 9   ? 6.32066  -4.57378  10.17701  1.000 21.54526 ?  12  ILE   A HG23 1 
ATOM   74   H  HD11 . ILE   A 1 9   ? 2.47467  -3.53812  11.37224  1.000 20.88626 ?  12  ILE   A HD11 1 
ATOM   75   H  HD12 . ILE   A 1 9   ? 3.75089  -2.63959  11.66792  1.000 20.88626 ?  12  ILE   A HD12 1 
ATOM   76   H  HD13 . ILE   A 1 9   ? 3.55804  -3.29853  10.23539  1.000 20.88626 ?  12  ILE   A HD13 1 
ATOM   77   N  N    . TYR   A 1 10  ? 5.19987  -7.65776  12.09443  1.000 14.33438 ?  13  TYR   A N    1 
ATOM   78   C  CA   . TYR   A 1 10  ? 5.08152  -8.85157  11.28084  1.000 14.36344 ?  13  TYR   A CA   1 
ATOM   79   C  C    . TYR   A 1 10  ? 3.98686  -8.71461  10.22932  1.000 13.96721 ?  13  TYR   A C    1 
ATOM   80   O  O    . TYR   A 1 10  ? 2.92228  -8.12896  10.46938  1.000 14.74472 ?  13  TYR   A O    1 
ATOM   81   C  CB   . TYR   A 1 10  ? 4.80574  -10.09939 12.12251  1.000 16.18308 ?  13  TYR   A CB   1 
ATOM   82   C  CG   . TYR   A 1 10  ? 5.97451  -10.51329 12.96737  1.000 18.18855 ?  13  TYR   A CG   1 
ATOM   83   C  CD1  . TYR   A 1 10  ? 7.00032  -11.27298 12.43783  1.000 19.78190 ?  13  TYR   A CD1  1 
ATOM   84   C  CD2  . TYR   A 1 10  ? 6.05636  -10.14055 14.30081  1.000 22.32469 ?  13  TYR   A CD2  1 
ATOM   85   C  CE1  . TYR   A 1 10  ? 8.08005  -11.65474 13.20085  1.000 22.51931 ?  13  TYR   A CE1  1 
ATOM   86   C  CE2  . TYR   A 1 10  ? 7.13108  -10.51663 15.08228  1.000 25.05998 ?  13  TYR   A CE2  1 
ATOM   87   C  CZ   . TYR   A 1 10  ? 8.14500  -11.25947 14.51448  1.000 24.24378 ?  13  TYR   A CZ   1 
ATOM   88   O  OH   . TYR   A 1 10  ? 9.20874  -11.63613 15.29343  1.000 26.67368 ?  13  TYR   A OH   1 
ATOM   89   H  H    . TYR   A 1 10  ? 4.55889  -7.55251  12.65804  1.000 17.20126 ?  13  TYR   A H    1 
ATOM   90   H  HA   . TYR   A 1 10  ? 5.92750  -8.96548  10.82013  1.000 17.23613 ?  13  TYR   A HA   1 
ATOM   91   H  HB2  . TYR   A 1 10  ? 4.05845  -9.92000  12.71434  1.000 19.41970 ?  13  TYR   A HB2  1 
ATOM   92   H  HB3  . TYR   A 1 10  ? 4.59011  -10.83642 11.52989  1.000 19.41970 ?  13  TYR   A HB3  1 
ATOM   93   H  HD1  . TYR   A 1 10  ? 6.96004  -11.53211 11.54556  1.000 23.73828 ?  13  TYR   A HD1  1 
ATOM   94   H  HD2  . TYR   A 1 10  ? 5.37599  -9.62870  14.67499  1.000 26.78963 ?  13  TYR   A HD2  1 
ATOM   95   H  HE1  . TYR   A 1 10  ? 8.75742  -12.17400 12.83149  1.000 27.02318 ?  13  TYR   A HE1  1 
ATOM   96   H  HE2  . TYR   A 1 10  ? 7.17059  -10.27243 15.97877  1.000 30.07198 ?  13  TYR   A HE2  1 
ATOM   97   H  HH   . TYR   A 1 10  ? 9.62275  -10.95654 15.56240  1.000 32.00841 ?  13  TYR   A HH   1 
ATOM   98   N  N    . ASN   A 1 11  ? 4.27208  -9.26496  9.05371   1.000 13.72808 ?  14  ASN   A N    1 
ATOM   99   C  CA   . ASN   A 1 11  ? 3.30069  -9.42779  7.98263   1.000 13.29018 ?  14  ASN   A CA   1 
ATOM   100  C  C    . ASN   A 1 11  ? 2.53059  -8.14567  7.64948   1.000 13.13405 ?  14  ASN   A C    1 
ATOM   101  O  O    . ASN   A 1 11  ? 1.30545  -8.16090  7.57823   1.000 13.45781 ?  14  ASN   A O    1 
ATOM   102  C  CB   . ASN   A 1 11  ? 2.31812  -10.54838 8.28917   1.000 15.11667 ?  14  ASN   A CB   1 
ATOM   103  C  CG   . ASN   A 1 11  ? 2.97076  -11.85607 8.48002   1.000 18.60089 ?  14  ASN   A CG   1 
ATOM   104  O  OD1  . ASN   A 1 11  ? 3.91699  -12.18999 7.77450   1.000 19.70396 ?  14  ASN   A OD1  1 
ATOM   105  N  ND2  . ASN   A 1 11  ? 2.44622  -12.64622 9.40689   1.000 20.99489 ?  14  ASN   A ND2  1 
ATOM   106  H  H    . ASN   A 1 11  ? 5.05217  -9.56235  8.84725   1.000 16.47370 ?  14  ASN   A H    1 
ATOM   107  H  HA   . ASN   A 1 11  ? 3.80081  -9.66726  7.18674   1.000 15.94821 ?  14  ASN   A HA   1 
ATOM   108  H  HB2  . ASN   A 1 11  ? 1.83915  -10.33237 9.10454   1.000 18.14000 ?  14  ASN   A HB2  1 
ATOM   109  H  HB3  . ASN   A 1 11  ? 1.69502  -10.63112 7.55039   1.000 18.14000 ?  14  ASN   A HB3  1 
ATOM   110  H  HD21 . ASN   A 1 11  ? 1.76210  -12.38487 9.85775   1.000 25.19387 ?  14  ASN   A HD21 1 
ATOM   111  H  HD22 . ASN   A 1 11  ? 2.79017  -13.42000 9.55712   1.000 25.19387 ?  14  ASN   A HD22 1 
ATOM   112  N  N    . PRO   A 1 12  ? 3.22675  -7.02689  7.42835   1.000 13.39433 ?  15  PRO   A N    1 
ATOM   113  C  CA   . PRO   A 1 12  ? 2.49746  -5.80040  7.07948   1.000 13.92613 ?  15  PRO   A CA   1 
ATOM   114  C  C    . PRO   A 1 12  ? 1.88479  -5.86586  5.68691   1.000 13.62157 ?  15  PRO   A C    1 
ATOM   115  O  O    . PRO   A 1 12  ? 2.51614  -6.31947  4.73440   1.000 14.83456 ?  15  PRO   A O    1 
ATOM   116  C  CB   . PRO   A 1 12  ? 3.58304  -4.71835  7.14188   1.000 15.18261 ?  15  PRO   A CB   1 
ATOM   117  C  CG   . PRO   A 1 12  ? 4.83190  -5.46946  6.73759   1.000 14.35025 ?  15  PRO   A CG   1 
ATOM   118  C  CD   . PRO   A 1 12  ? 4.69100  -6.80132  7.43966   1.000 14.01073 ?  15  PRO   A CD   1 
ATOM   119  H  HA   . PRO   A 1 12  ? 1.80091  -5.62930  7.73250   1.000 16.71135 ?  15  PRO   A HA   1 
ATOM   120  H  HB2  . PRO   A 1 12  ? 3.38300  -4.00170  6.51955   1.000 18.21914 ?  15  PRO   A HB2  1 
ATOM   121  H  HB3  . PRO   A 1 12  ? 3.65747  -4.36488  8.04211   1.000 18.21914 ?  15  PRO   A HB3  1 
ATOM   122  H  HG2  . PRO   A 1 12  ? 4.85985  -5.58105  5.77444   1.000 17.22030 ?  15  PRO   A HG2  1 
ATOM   123  H  HG3  . PRO   A 1 12  ? 5.62204  -4.99476  7.03964   1.000 17.22030 ?  15  PRO   A HG3  1 
ATOM   124  H  HD2  . PRO   A 1 12  ? 5.15350  -7.50096  6.95232   1.000 16.81288 ?  15  PRO   A HD2  1 
ATOM   125  H  HD3  . PRO   A 1 12  ? 5.02732  -6.75183  8.34814   1.000 16.81288 ?  15  PRO   A HD3  1 
ATOM   126  N  N    . VAL   A 1 13  ? 0.66064  -5.34560  5.56352   1.000 13.84705 ?  16  VAL   A N    1 
ATOM   127  C  CA   . VAL   A 1 13  ? 0.06030  -5.11884  4.25169   1.000 14.02989 ?  16  VAL   A CA   1 
ATOM   128  C  C    . VAL   A 1 13  ? 0.95472  -4.17967  3.46794   1.000 14.09387 ?  16  VAL   A C    1 
ATOM   129  O  O    . VAL   A 1 13  ? 1.50487  -3.21475  4.01223   1.000 13.99246 ?  16  VAL   A O    1 
ATOM   130  C  CB   . VAL   A 1 13  ? -1.33528 -4.50111  4.44980   1.000 15.27492 ?  16  VAL   A CB   1 
ATOM   131  C  CG1  . VAL   A 1 13  ? -1.92610 -4.02222  3.13777   1.000 17.12362 ?  16  VAL   A CG1  1 
ATOM   132  C  CG2  . VAL   A 1 13  ? -2.27417 -5.50035  5.09884   1.000 17.25154 ?  16  VAL   A CG2  1 
ATOM   133  H  H    . VAL   A 1 13  ? 0.15911  -5.11634  6.22345   1.000 16.61646 ?  16  VAL   A H    1 
ATOM   134  H  HA   . VAL   A 1 13  ? -0.02394 -5.95320  3.76421   1.000 16.83587 ?  16  VAL   A HA   1 
ATOM   135  H  HB   . VAL   A 1 13  ? -1.23701 -3.73240  5.03317   1.000 18.32990 ?  16  VAL   A HB   1 
ATOM   136  H  HG11 . VAL   A 1 13  ? -2.84555 -3.75091  3.28581   1.000 20.54834 ?  16  VAL   A HG11 1 
ATOM   137  H  HG12 . VAL   A 1 13  ? -1.40717 -3.26944  2.81383   1.000 20.54834 ?  16  VAL   A HG12 1 
ATOM   138  H  HG13 . VAL   A 1 13  ? -1.89469 -4.74712  2.49401   1.000 20.54834 ?  16  VAL   A HG13 1 
ATOM   139  H  HG21 . VAL   A 1 13  ? -3.16107 -5.11127  5.15298   1.000 20.70185 ?  16  VAL   A HG21 1 
ATOM   140  H  HG22 . VAL   A 1 13  ? -2.29894 -6.30651  4.55997   1.000 20.70185 ?  16  VAL   A HG22 1 
ATOM   141  H  HG23 . VAL   A 1 13  ? -1.94886 -5.70730  5.98892   1.000 20.70185 ?  16  VAL   A HG23 1 
ATOM   142  N  N    . ILE   A 1 14  ? 1.10008  -4.45150  2.18429   1.000 13.69754 ?  17  ILE   A N    1 
ATOM   143  C  CA   . ILE   A 1 14  ? 1.82232  -3.58679  1.26027   1.000 13.96067 ?  17  ILE   A CA   1 
ATOM   144  C  C    . ILE   A 1 14  ? 0.78268  -2.87767  0.41281   1.000 15.03037 ?  17  ILE   A C    1 
ATOM   145  O  O    . ILE   A 1 14  ? -0.10696 -3.53131  -0.13860  1.000 17.13690 ?  17  ILE   A O    1 
ATOM   146  C  CB   . ILE   A 1 14  ? 2.80425  -4.39374  0.39247   1.000 14.92752 ?  17  ILE   A CB   1 
ATOM   147  C  CG1  . ILE   A 1 14  ? 3.76153  -5.19219  1.29733   1.000 15.58580 ?  17  ILE   A CG1  1 
ATOM   148  C  CG2  . ILE   A 1 14  ? 3.54674  -3.53284  -0.62316  1.000 15.52276 ?  17  ILE   A CG2  1 
ATOM   149  C  CD1  . ILE   A 1 14  ? 4.54541  -4.39444  2.31237   1.000 14.63768 ?  17  ILE   A CD1  1 
ATOM   150  H  H    . ILE   A 1 14  ? 0.77885  -5.15546  1.80899   1.000 16.43704 ?  17  ILE   A H    1 
ATOM   151  H  HA   . ILE   A 1 14  ? 2.33298  -2.91679  1.74112   1.000 16.75280 ?  17  ILE   A HA   1 
ATOM   152  H  HB   . ILE   A 1 14  ? 2.28572  -5.01927  -0.13738  1.000 17.91302 ?  17  ILE   A HB   1 
ATOM   153  H  HG12 . ILE   A 1 14  ? 3.23830  -5.84396  1.78959   1.000 18.70296 ?  17  ILE   A HG12 1 
ATOM   154  H  HG13 . ILE   A 1 14  ? 4.40614  -5.64400  0.73055   1.000 18.70296 ?  17  ILE   A HG13 1 
ATOM   155  H  HG21 . ILE   A 1 14  ? 4.23200  -4.06959  -1.05118  1.000 18.62731 ?  17  ILE   A HG21 1 
ATOM   156  H  HG22 . ILE   A 1 14  ? 2.91580  -3.21178  -1.28628  1.000 18.62731 ?  17  ILE   A HG22 1 
ATOM   157  H  HG23 . ILE   A 1 14  ? 3.95385  -2.78211  -0.16319  1.000 18.62731 ?  17  ILE   A HG23 1 
ATOM   158  H  HD11 . ILE   A 1 14  ? 5.31793  -4.91052  2.59128   1.000 17.56522 ?  17  ILE   A HD11 1 
ATOM   159  H  HD12 . ILE   A 1 14  ? 4.83295  -3.56195  1.90594   1.000 17.56522 ?  17  ILE   A HD12 1 
ATOM   160  H  HD13 . ILE   A 1 14  ? 3.97707  -4.21046  3.07659   1.000 17.56522 ?  17  ILE   A HD13 1 
ATOM   161  N  N    . PRO   A 1 15  ? 0.82971  -1.56003  0.29545   1.000 16.10501 ?  18  PRO   A N    1 
ATOM   162  C  CA   . PRO   A 1 15  ? 1.88619  -0.65851  0.73754   1.000 15.26951 ?  18  PRO   A CA   1 
ATOM   163  C  C    . PRO   A 1 15  ? 1.91887  -0.47800  2.24620   1.000 14.30808 ?  18  PRO   A C    1 
ATOM   164  O  O    . PRO   A 1 15  ? 0.88778  -0.33380  2.91175   1.000 15.54096 ?  18  PRO   A O    1 
ATOM   165  C  CB   . PRO   A 1 15  ? 1.52269  0.65162   0.03885   1.000 18.88759 ?  18  PRO   A CB   1 
ATOM   166  C  CG   . PRO   A 1 15  ? 0.03049  0.59295   -0.11438  1.000 20.91570 ?  18  PRO   A CG   1 
ATOM   167  C  CD   . PRO   A 1 15  ? -0.24961 -0.84040  -0.40393  1.000 20.27157 ?  18  PRO   A CD   1 
ATOM   168  H  HA   . PRO   A 1 15  ? 2.74532  -0.98482  0.42719   1.000 18.32342 ?  18  PRO   A HA   1 
ATOM   169  H  HB2  . PRO   A 1 15  ? 1.78802  1.40580   0.58814   1.000 22.66510 ?  18  PRO   A HB2  1 
ATOM   170  H  HB3  . PRO   A 1 15  ? 1.96090  0.70005   -0.82517  1.000 22.66510 ?  18  PRO   A HB3  1 
ATOM   171  H  HG2  . PRO   A 1 15  ? -0.40085 0.87473   0.70747   1.000 25.09885 ?  18  PRO   A HG2  1 
ATOM   172  H  HG3  . PRO   A 1 15  ? -0.25225 1.16007   -0.84878  1.000 25.09885 ?  18  PRO   A HG3  1 
ATOM   173  H  HD2  . PRO   A 1 15  ? -1.11667 -1.09798  -0.05358  1.000 24.32588 ?  18  PRO   A HD2  1 
ATOM   174  H  HD3  . PRO   A 1 15  ? -0.21334 -1.01098  -1.35812  1.000 24.32588 ?  18  PRO   A HD3  1 
ATOM   175  N  N    . PHE   A 1 16  ? 3.12698  -0.46870  2.79126   1.000 12.93065 ?  19  PHE   A N    1 
ATOM   176  C  CA   . PHE   A 1 16  ? 3.37071  -0.22507  4.20129   1.000 12.68334 ?  19  PHE   A CA   1 
ATOM   177  C  C    . PHE   A 1 16  ? 4.04201  1.13011   4.37395   1.000 12.23034 ?  19  PHE   A C    1 
ATOM   178  O  O    . PHE   A 1 16  ? 5.02733  1.42727   3.69233   1.000 12.45779 ?  19  PHE   A O    1 
ATOM   179  C  CB   . PHE   A 1 16  ? 4.29674  -1.29220  4.78927   1.000 12.59954 ?  19  PHE   A CB   1 
ATOM   180  C  CG   . PHE   A 1 16  ? 4.71170  -0.95848  6.20593   1.000 12.92277 ?  19  PHE   A CG   1 
ATOM   181  C  CD1  . PHE   A 1 16  ? 3.81270  -1.10149  7.23636   1.000 14.81285 ?  19  PHE   A CD1  1 
ATOM   182  C  CD2  . PHE   A 1 16  ? 5.95541  -0.42318  6.48266   1.000 15.06703 ?  19  PHE   A CD2  1 
ATOM   183  C  CE1  . PHE   A 1 16  ? 4.16544  -0.75589  8.54509   1.000 16.49070 ?  19  PHE   A CE1  1 
ATOM   184  C  CE2  . PHE   A 1 16  ? 6.30994  -0.05490  7.75522   1.000 16.73239 ?  19  PHE   A CE2  1 
ATOM   185  C  CZ   . PHE   A 1 16  ? 5.42333  -0.24414  8.79731   1.000 16.76188 ?  19  PHE   A CZ   1 
ATOM   186  H  H    . PHE   A 1 16  ? 3.84893  -0.60673  2.34479   1.000 15.51679 ?  19  PHE   A H    1 
ATOM   187  H  HA   . PHE   A 1 16  ? 2.52148  -0.23289  4.66996   1.000 15.22001 ?  19  PHE   A HA   1 
ATOM   188  N  N    . VAL   A 1 17  ? 3.52847  1.93588   5.29940   1.000 12.97832 ?  20  VAL   A N    1 
ATOM   189  C  CA   . VAL   A 1 17  ? 4.16812  3.18232   5.68333   1.000 13.64488 ?  20  VAL   A CA   1 
ATOM   190  C  C    . VAL   A 1 17  ? 4.12759  3.24888   7.20119   1.000 14.32011 ?  20  VAL   A C    1 
ATOM   191  O  O    . VAL   A 1 17  ? 3.04143  3.19137   7.79435   1.000 16.59519 ?  20  VAL   A O    1 
ATOM   192  C  CB   . VAL   A 1 17  ? 3.46798  4.40619   5.07910   1.000 16.44609 ?  20  VAL   A CB   1 
ATOM   193  C  CG1  . VAL   A 1 17  ? 4.22818  5.66464   5.44389   1.000 19.14252 ?  20  VAL   A CG1  1 
ATOM   194  C  CG2  . VAL   A 1 17  ? 3.33668  4.26474   3.57821   1.000 16.98182 ?  20  VAL   A CG2  1 
ATOM   195  H  H    . VAL   A 1 17  ? 2.79787  1.77603   5.72398   1.000 15.57398 ?  20  VAL   A H    1 
ATOM   196  H  HA   . VAL   A 1 17  ? 5.09161  3.18773   5.38663   1.000 16.37385 ?  20  VAL   A HA   1 
ATOM   197  H  HB   . VAL   A 1 17  ? 2.57119  4.47385   5.44253   1.000 19.73531 ?  20  VAL   A HB   1 
ATOM   198  H  HG11 . VAL   A 1 17  ? 3.88012  6.40578   4.92382   1.000 22.97102 ?  20  VAL   A HG11 1 
ATOM   199  H  HG12 . VAL   A 1 17  ? 4.11121  5.84104   6.39051   1.000 22.97102 ?  20  VAL   A HG12 1 
ATOM   200  H  HG13 . VAL   A 1 17  ? 5.16867  5.53416   5.24547   1.000 22.97102 ?  20  VAL   A HG13 1 
ATOM   201  H  HG21 . VAL   A 1 17  ? 2.99003  5.09338   3.21204   1.000 20.37819 ?  20  VAL   A HG21 1 
ATOM   202  H  HG22 . VAL   A 1 17  ? 4.21032  4.07638   3.20114   1.000 20.37819 ?  20  VAL   A HG22 1 
ATOM   203  H  HG23 . VAL   A 1 17  ? 2.72750  3.53590   3.38179   1.000 20.37819 ?  20  VAL   A HG23 1 
ATOM   204  N  N    . GLY   A 1 18  ? 5.27706  3.40495   7.83963   1.000 14.61926 ?  21  GLY   A N    1 
ATOM   205  C  CA   . GLY   A 1 18  ? 5.32981  3.42768   9.29337   1.000 15.41653 ?  21  GLY   A CA   1 
ATOM   206  C  C    . GLY   A 1 18  ? 6.33837  4.43937   9.80704   1.000 14.85831 ?  21  GLY   A C    1 
ATOM   207  O  O    . GLY   A 1 18  ? 7.38927  4.65677   9.21484   1.000 15.02696 ?  21  GLY   A O    1 
ATOM   208  H  H    . GLY   A 1 18  ? 6.04037  3.49975   7.45497   1.000 17.54311 ?  21  GLY   A H    1 
ATOM   209  H  HA2  . GLY   A 1 18  ? 4.45596  3.65895   9.64521   1.000 18.49983 ?  21  GLY   A HA2  1 
ATOM   210  H  HA3  . GLY   A 1 18  ? 5.58029  2.55000   9.62175   1.000 18.49983 ?  21  GLY   A HA3  1 
ATOM   211  N  N    . THR   A 1 19  ? 5.99353  5.04178   10.93364  1.000 15.60515 ?  22  THR   A N    1 
ATOM   212  C  CA   . THR   A 1 19  ? 6.90169  5.95762   11.60382  1.000 15.62597 ?  22  THR   A CA   1 
ATOM   213  C  C    . THR   A 1 19  ? 7.96806  5.15941   12.32485  1.000 16.26107 ?  22  THR   A C    1 
ATOM   214  O  O    . THR   A 1 19  ? 7.65910  4.20691   13.04915  1.000 19.21097 ?  22  THR   A O    1 
ATOM   215  C  CB   . THR   A 1 19  ? 6.12227  6.79582   12.61138  1.000 18.77571 ?  22  THR   A CB   1 
ATOM   216  O  OG1  . THR   A 1 19  ? 5.12225  7.55318   11.91719  1.000 20.66543 ?  22  THR   A OG1  1 
ATOM   217  C  CG2  . THR   A 1 19  ? 7.04803  7.73145   13.40430  1.000 20.94303 ?  22  THR   A CG2  1 
ATOM   218  H  H    . THR   A 1 19  ? 5.23822  4.93719   11.33134  1.000 18.72617 ?  22  THR   A H    1 
ATOM   219  H  HA   . THR   A 1 19  ? 7.32508  6.54698   10.96016  1.000 18.75117 ?  22  THR   A HA   1 
ATOM   220  H  HB   . THR   A 1 19  ? 5.69519  6.21145   13.25715  1.000 22.53085 ?  22  THR   A HB   1 
ATOM   221  H  HG1  . THR   A 1 19  ? 5.48533  8.15588   11.45836  1.000 24.79852 ?  22  THR   A HG1  1 
ATOM   222  H  HG21 . THR   A 1 19  ? 6.53692  8.46777   13.77511  1.000 25.13164 ?  22  THR   A HG21 1 
ATOM   223  H  HG22 . THR   A 1 19  ? 7.46988  7.24442   14.12938  1.000 25.13164 ?  22  THR   A HG22 1 
ATOM   224  H  HG23 . THR   A 1 19  ? 7.73692  8.08817   12.82199  1.000 25.13164 ?  22  THR   A HG23 1 
ATOM   225  N  N    . ILE   A 1 20  ? 9.21789  5.55633   12.12553  1.000 16.07851 ?  23  ILE   A N    1 
ATOM   226  C  CA   . ILE   A 1 20  ? 10.35964 4.96332   12.80746  1.000 16.51913 ?  23  ILE   A CA   1 
ATOM   227  C  C    . ILE   A 1 20  ? 10.45332 5.63786   14.17730  1.000 17.50550 ?  23  ILE   A C    1 
ATOM   228  O  O    . ILE   A 1 20  ? 10.55433 6.86871   14.28095  1.000 19.74794 ?  23  ILE   A O    1 
ATOM   229  C  CB   . ILE   A 1 20  ? 11.63971 5.12753   11.98000  1.000 15.69546 ?  23  ILE   A CB   1 
ATOM   230  C  CG1  . ILE   A 1 20  ? 11.45666 4.56133   10.56704  1.000 14.86737 ?  23  ILE   A CG1  1 
ATOM   231  C  CG2  . ILE   A 1 20  ? 12.80784 4.44106   12.67984  1.000 17.53283 ?  23  ILE   A CG2  1 
ATOM   232  C  CD1  . ILE   A 1 20  ? 12.62373 4.82503   9.65647   1.000 15.32179 ?  23  ILE   A CD1  1 
ATOM   233  H  H    . ILE   A 1 20  ? 9.43749  6.18686   11.58348  1.000 19.29421 ?  23  ILE   A H    1 
ATOM   234  H  HA   . ILE   A 1 20  ? 10.23265 4.01063   12.93849  1.000 19.82296 ?  23  ILE   A HA   1 
ATOM   235  H  HB   . ILE   A 1 20  ? 11.82938 6.07560   11.90194  1.000 18.83455 ?  23  ILE   A HB   1 
ATOM   236  H  HG12 . ILE   A 1 20  ? 11.33944 3.60039   10.62832  1.000 17.84084 ?  23  ILE   A HG12 1 
ATOM   237  H  HG13 . ILE   A 1 20  ? 10.67116 4.96655   10.16743  1.000 17.84084 ?  23  ILE   A HG13 1 
ATOM   238  H  HG21 . ILE   A 1 20  ? 13.63064 4.67167   12.22081  1.000 21.03939 ?  23  ILE   A HG21 1 
ATOM   239  H  HG22 . ILE   A 1 20  ? 12.84658 4.74403   13.60049  1.000 21.03939 ?  23  ILE   A HG22 1 
ATOM   240  H  HG23 . ILE   A 1 20  ? 12.67199 3.48099   12.65299  1.000 21.03939 ?  23  ILE   A HG23 1 
ATOM   241  H  HD11 . ILE   A 1 20  ? 12.33955 4.70694   8.73658   1.000 18.38614 ?  23  ILE   A HD11 1 
ATOM   242  H  HD12 . ILE   A 1 20  ? 12.93185 5.73455   9.79333   1.000 18.38614 ?  23  ILE   A HD12 1 
ATOM   243  H  HD13 . ILE   A 1 20  ? 13.33516 4.19975   9.86576   1.000 18.38614 ?  23  ILE   A HD13 1 
ATOM   244  N  N    . PRO   A 1 21  ? 10.43120 4.87451   15.26338  1.000 19.20858 ?  24  PRO   A N    1 
ATOM   245  C  CA   . PRO   A 1 21  ? 10.26125 5.47595   16.59289  1.000 19.77403 ?  24  PRO   A CA   1 
ATOM   246  C  C    . PRO   A 1 21  ? 11.52334 6.01847   17.22697  1.000 21.22417 ?  24  PRO   A C    1 
ATOM   247  O  O    . PRO   A 1 21  ? 11.43626 6.55998   18.33160  1.000 24.28689 ?  24  PRO   A O    1 
ATOM   248  C  CB   . PRO   A 1 21  ? 9.71760  4.30988   17.42498  1.000 21.82203 ?  24  PRO   A CB   1 
ATOM   249  C  CG   . PRO   A 1 21  ? 10.25054 3.09680   16.74613  1.000 21.74605 ?  24  PRO   A CG   1 
ATOM   250  C  CD   . PRO   A 1 21  ? 10.24417 3.41908   15.26967  1.000 17.58340 ?  24  PRO   A CD   1 
ATOM   251  H  HA   . PRO   A 1 21  ? 9.60353  6.18691   16.53963  1.000 23.72884 ?  24  PRO   A HA   1 
ATOM   252  H  HB2  . PRO   A 1 21  ? 10.04194 4.37151   18.33707  1.000 26.18644 ?  24  PRO   A HB2  1 
ATOM   253  H  HB3  . PRO   A 1 21  ? 8.74767  4.31805   17.41651  1.000 26.18644 ?  24  PRO   A HB3  1 
ATOM   254  H  HG2  . PRO   A 1 21  ? 11.15227 2.91751   17.05539  1.000 26.09526 ?  24  PRO   A HG2  1 
ATOM   255  H  HG3  . PRO   A 1 21  ? 9.67781  2.33707   16.93506  1.000 26.09526 ?  24  PRO   A HG3  1 
ATOM   256  H  HD2  . PRO   A 1 21  ? 10.97337 2.97200   14.81220  1.000 21.10008 ?  24  PRO   A HD2  1 
ATOM   257  H  HD3  . PRO   A 1 21  ? 9.39801  3.17466   14.86324  1.000 21.10008 ?  24  PRO   A HD3  1 
ATOM   258  N  N    . ASP   A 1 22  ? 12.67293 5.85855   16.58446  1.000 20.14786 ?  25  ASP   A N    1 
ATOM   259  C  CA   . ASP   A 1 22  ? 13.91553 6.39372   17.09900  1.000 20.24476 ?  25  ASP   A CA   1 
ATOM   260  C  C    . ASP   A 1 22  ? 14.77474 6.79343   15.91532  1.000 18.31879 ?  25  ASP   A C    1 
ATOM   261  O  O    . ASP   A 1 22  ? 14.47356 6.45995   14.76418  1.000 19.20481 ?  25  ASP   A O    1 
ATOM   262  C  CB   . ASP   A 1 22  ? 14.61656 5.38165   17.99513  1.000 25.64185 ?  25  ASP   A CB   1 
ATOM   263  C  CG   . ASP   A 1 22  ? 15.27969 6.03679   19.16084  1.000 33.59606 ?  25  ASP   A CG   1 
ATOM   264  O  OD1  . ASP   A 1 22  ? 15.94153 7.08517   18.95932  1.000 33.34558 ?  25  ASP   A OD1  1 
ATOM   265  O  OD2  . ASP   A 1 22  ? 15.11873 5.51405   20.27865  1.000 38.89023 ?  25  ASP   A OD2  1 
ATOM   266  H  H    . ASP   A 1 22  ? 12.75616 5.43771   15.83910  1.000 24.17743 ?  25  ASP   A H    1 
ATOM   267  H  HA   . ASP   A 1 22  ? 13.74815 7.18741   17.63094  1.000 24.29371 ?  25  ASP   A HA   1 
ATOM   268  H  HB2  . ASP   A 1 22  ? 13.96419 4.74841   18.33324  1.000 30.77022 ?  25  ASP   A HB2  1 
ATOM   269  H  HB3  . ASP   A 1 22  ? 15.29533 4.91638   17.48161  1.000 30.77022 ?  25  ASP   A HB3  1 
ATOM   270  N  N    . GLN   A 1 23  ? 15.83950 7.53449   16.20789  1.000 17.85660 ?  26  GLN   A N    1 
ATOM   271  C  CA   . GLN   A 1 23  ? 16.73127 8.02821   15.17332  1.000 17.30429 ?  26  GLN   A CA   1 
ATOM   272  C  C    . GLN   A 1 23  ? 17.56057 6.89386   14.60149  1.000 16.27753 ?  26  GLN   A C    1 
ATOM   273  O  O    . GLN   A 1 23  ? 17.99424 5.98002   15.31412  1.000 16.93083 ?  26  GLN   A O    1 
ATOM   274  C  CB   . GLN   A 1 23  ? 17.65565 9.11695   15.73755  1.000 17.80825 ?  26  GLN   A CB   1 
ATOM   275  C  CG   . GLN   A 1 23  ? 18.54425 9.79157   14.69515  1.000 18.99448 ?  26  GLN   A CG   1 
ATOM   276  C  CD   . GLN   A 1 23  ? 19.25144 11.04665  15.19087  1.000 19.92233 ?  26  GLN   A CD   1 
ATOM   277  O  OE1  . GLN   A 1 23  ? 18.76682 11.75033  16.07213  1.000 22.83879 ?  26  GLN   A OE1  1 
ATOM   278  N  NE2  . GLN   A 1 23  ? 20.39663 11.34754  14.58166  1.000 22.62120 ?  26  GLN   A NE2  1 
ATOM   279  H  H    . GLN   A 1 23  ? 16.06689 7.76558   17.00444  1.000 21.42791 ?  26  GLN   A H    1 
ATOM   280  H  HA   . GLN   A 1 23  ? 16.20568 8.41711   14.45678  1.000 20.76515 ?  26  GLN   A HA   1 
ATOM   281  H  HB2  . GLN   A 1 23  ? 17.10870 9.80558   16.14687  1.000 21.36991 ?  26  GLN   A HB2  1 
ATOM   282  H  HB3  . GLN   A 1 23  ? 18.23641 8.71552   16.40273  1.000 21.36991 ?  26  GLN   A HB3  1 
ATOM   283  H  HG2  . GLN   A 1 23  ? 19.22672 9.16168   14.41516  1.000 22.79338 ?  26  GLN   A HG2  1 
ATOM   284  H  HG3  . GLN   A 1 23  ? 17.99510 10.04463  13.93667  1.000 22.79338 ?  26  GLN   A HG3  1 
ATOM   285  H  HE21 . GLN   A 1 23  ? 20.69294 10.84440  13.95027  1.000 27.14544 ?  26  GLN   A HE21 1 
ATOM   286  H  HE22 . GLN   A 1 23  ? 20.83994 12.04502  14.81959  1.000 27.14544 ?  26  GLN   A HE22 1 
ATOM   287  N  N    . LEU   A 1 24  ? 17.80417 6.97755   13.29703  1.000 15.15386 ?  27  LEU   A N    1 
ATOM   288  C  CA   . LEU   A 1 24  ? 18.73150 6.07403   12.61930  1.000 14.70413 ?  27  LEU   A CA   1 
ATOM   289  C  C    . LEU   A 1 24  ? 20.16229 6.56096   12.86398  1.000 15.91749 ?  27  LEU   A C    1 
ATOM   290  O  O    . LEU   A 1 24  ? 20.86569 7.04981   11.97528  1.000 17.84811 ?  27  LEU   A O    1 
ATOM   291  C  CB   . LEU   A 1 24  ? 18.41114 5.97309   11.13248  1.000 15.15758 ?  27  LEU   A CB   1 
ATOM   292  C  CG   . LEU   A 1 24  ? 17.03178 5.40317   10.77899  1.000 15.08338 ?  27  LEU   A CG   1 
ATOM   293  C  CD1  . LEU   A 1 24  ? 16.91657 5.28491   9.26338   1.000 16.09414 ?  27  LEU   A CD1  1 
ATOM   294  C  CD2  . LEU   A 1 24  ? 16.74857 4.07001   11.42713  1.000 16.16081 ?  27  LEU   A CD2  1 
ATOM   295  H  H    . LEU   A 1 24  ? 17.44045 7.55641   12.77527  1.000 18.18463 ?  27  LEU   A H    1 
ATOM   296  H  HA   . LEU   A 1 24  ? 18.63830 5.18583   12.99786  1.000 17.64496 ?  27  LEU   A HA   1 
ATOM   297  H  HB2  . LEU   A 1 24  ? 18.46009 6.86378   10.75146  1.000 18.18909 ?  27  LEU   A HB2  1 
ATOM   298  H  HB3  . LEU   A 1 24  ? 19.07397 5.39835   10.71868  1.000 18.18909 ?  27  LEU   A HB3  1 
ATOM   299  H  HG   . LEU   A 1 24  ? 16.36050 6.01235   11.12420  1.000 18.10006 ?  27  LEU   A HG   1 
ATOM   300  H  HD11 . LEU   A 1 24  ? 16.02703 4.97068   9.03785   1.000 19.31297 ?  27  LEU   A HD11 1 
ATOM   301  H  HD12 . LEU   A 1 24  ? 17.07017 6.15636   8.86604   1.000 19.31297 ?  27  LEU   A HD12 1 
ATOM   302  H  HD13 . LEU   A 1 24  ? 17.58093 4.65420   8.94442   1.000 19.31297 ?  27  LEU   A HD13 1 
ATOM   303  H  HD21 . LEU   A 1 24  ? 15.88342 3.75029   11.12680  1.000 19.39298 ?  27  LEU   A HD21 1 
ATOM   304  H  HD22 . LEU   A 1 24  ? 17.44092 3.44083   11.17084  1.000 19.39298 ?  27  LEU   A HD22 1 
ATOM   305  H  HD23 . LEU   A 1 24  ? 16.74358 4.18199   12.39063  1.000 19.39298 ?  27  LEU   A HD23 1 
ATOM   306  N  N    . ASP   A 1 25  ? 20.60344 6.37478   14.10536  1.000 16.21841 ?  28  ASP   A N    1 
ATOM   307  C  CA   . ASP   A 1 25  ? 21.96804 6.70850   14.49084  1.000 17.03267 ?  28  ASP   A CA   1 
ATOM   308  C  C    . ASP   A 1 25  ? 22.94549 5.72927   13.83722  1.000 15.08834 ?  28  ASP   A C    1 
ATOM   309  O  O    . ASP   A 1 25  ? 22.61792 4.56256   13.64169  1.000 14.47068 ?  28  ASP   A O    1 
ATOM   310  C  CB   . ASP   A 1 25  ? 22.13204 6.56429   16.01205  1.000 18.41959 ?  28  ASP   A CB   1 
ATOM   311  C  CG   . ASP   A 1 25  ? 21.34048 7.58456   16.81326  1.000 22.45093 ?  28  ASP   A CG   1 
ATOM   312  O  OD1  . ASP   A 1 25  ? 21.20972 8.74007   16.37869  1.000 24.51712 ?  28  ASP   A OD1  1 
ATOM   313  O  OD2  . ASP   A 1 25  ? 20.85969 7.21446   17.90401  1.000 25.60601 ?  28  ASP   A OD2  1 
ATOM   314  H  H    . ASP   A 1 25  ? 20.12869 6.05442   14.74690  1.000 19.46209 ?  28  ASP   A H    1 
ATOM   315  H  HA   . ASP   A 1 25  ? 22.16715 7.61725   14.21617  1.000 20.43921 ?  28  ASP   A HA   1 
ATOM   316  H  HB2  . ASP   A 1 25  ? 21.82916 5.68151   16.27636  1.000 22.10350 ?  28  ASP   A HB2  1 
ATOM   317  H  HB3  . ASP   A 1 25  ? 23.06917 6.67460   16.23682  1.000 22.10350 ?  28  ASP   A HB3  1 
ATOM   318  N  N    . PRO   A 1 26  ? 24.17971 6.14607   13.58310  1.000 15.07124 ?  29  PRO   A N    1 
ATOM   319  C  CA   . PRO   A 1 26  ? 25.19090 5.18328   13.12530  1.000 14.51007 ?  29  PRO   A CA   1 
ATOM   320  C  C    . PRO   A 1 26  ? 25.24584 3.96886   14.03537  1.000 14.12279 ?  29  PRO   A C    1 
ATOM   321  O  O    . PRO   A 1 26  ? 25.25666 4.09400   15.26384  1.000 14.43003 ?  29  PRO   A O    1 
ATOM   322  C  CB   . PRO   A 1 26  ? 26.48172 6.00218   13.17519  1.000 16.32065 ?  29  PRO   A CB   1 
ATOM   323  C  CG   . PRO   A 1 26  ? 26.01546 7.41490   12.85015  1.000 18.00343 ?  29  PRO   A CG   1 
ATOM   324  C  CD   . PRO   A 1 26  ? 24.70341 7.52890   13.60178  1.000 17.08769 ?  29  PRO   A CD   1 
ATOM   325  H  HA   . PRO   A 1 26  ? 25.01981 4.89556   12.21489  1.000 17.41209 ?  29  PRO   A HA   1 
ATOM   326  H  HB2  . PRO   A 1 26  ? 26.87612 5.95544   14.06015  1.000 19.58478 ?  29  PRO   A HB2  1 
ATOM   327  H  HB3  . PRO   A 1 26  ? 27.11223 5.67750   12.51341  1.000 19.58478 ?  29  PRO   A HB3  1 
ATOM   328  H  HG2  . PRO   A 1 26  ? 26.66165 8.06516   13.16717  1.000 21.60411 ?  29  PRO   A HG2  1 
ATOM   329  H  HG3  . PRO   A 1 26  ? 25.88475 7.51589   11.89432  1.000 21.60411 ?  29  PRO   A HG3  1 
ATOM   330  H  HD2  . PRO   A 1 26  ? 24.85193 7.82956   14.51197  1.000 20.50523 ?  29  PRO   A HD2  1 
ATOM   331  H  HD3  . PRO   A 1 26  ? 24.09663 8.13404   13.14734  1.000 20.50523 ?  29  PRO   A HD3  1 
ATOM   332  N  N    . GLY   A 1 27  ? 25.26223 2.78917   13.42007  1.000 13.85226 ?  30  GLY   A N    1 
ATOM   333  C  CA   . GLY   A 1 27  ? 25.17588 1.52721   14.10289  1.000 14.48372 ?  30  GLY   A CA   1 
ATOM   334  C  C    . GLY   A 1 27  ? 23.81547 0.86293   14.00093  1.000 15.39937 ?  30  GLY   A C    1 
ATOM   335  O  O    . GLY   A 1 27  ? 23.70254 -0.34502  14.23649  1.000 19.37579 ?  30  GLY   A O    1 
ATOM   336  H  H    . GLY   A 1 27  ? 25.32603 2.70241   12.56684  1.000 16.62271 ?  30  GLY   A H    1 
ATOM   337  H  HA2  . GLY   A 1 27  ? 25.83393 0.92128   13.72776  1.000 17.38047 ?  30  GLY   A HA2  1 
ATOM   338  H  HA3  . GLY   A 1 27  ? 25.37250 1.66440   15.04280  1.000 17.38047 ?  30  GLY   A HA3  1 
ATOM   339  N  N    . THR   A 1 28  ? 22.78513 1.62199   13.67032  1.000 13.53338 ?  31  THR   A N    1 
ATOM   340  C  CA   . THR   A 1 28  ? 21.43690 1.08008   13.62772  1.000 13.34144 ?  31  THR   A CA   1 
ATOM   341  C  C    . THR   A 1 28  ? 21.28073 0.09031   12.48166  1.000 13.01768 ?  31  THR   A C    1 
ATOM   342  O  O    . THR   A 1 28  ? 21.81858 0.29380   11.39083  1.000 13.65860 ?  31  THR   A O    1 
ATOM   343  C  CB   . THR   A 1 28  ? 20.44779 2.23847   13.49108  1.000 13.84573 ?  31  THR   A CB   1 
ATOM   344  O  OG1  . THR   A 1 28  ? 20.48251 3.01049   14.69841  1.000 15.15495 ?  31  THR   A OG1  1 
ATOM   345  C  CG2  . THR   A 1 28  ? 19.03819 1.75357   13.27709  1.000 14.95630 ?  31  THR   A CG2  1 
ATOM   346  H  H    . THR   A 1 28  ? 22.83796 2.45560   13.46561  1.000 16.24006 ?  31  THR   A H    1 
ATOM   347  H  HA   . THR   A 1 28  ? 21.24073 0.59449   14.44419  1.000 16.00973 ?  31  THR   A HA   1 
ATOM   348  H  HB   . THR   A 1 28  ? 20.69510 2.77498   12.72173  1.000 16.61488 ?  31  THR   A HB   1 
ATOM   349  H  HG1  . THR   A 1 28  ? 21.24198 3.35557   14.79703  1.000 18.18594 ?  31  THR   A HG1  1 
ATOM   350  H  HG21 . THR   A 1 28  ? 18.41235 2.48177   13.41479  1.000 17.94755 ?  31  THR   A HG21 1 
ATOM   351  H  HG22 . THR   A 1 28  ? 18.93652 1.41788   12.37273  1.000 17.94755 ?  31  THR   A HG22 1 
ATOM   352  H  HG23 . THR   A 1 28  ? 18.83409 1.04060   13.90233  1.000 17.94755 ?  31  THR   A HG23 1 
ATOM   353  N  N    . LEU   A 1 29  ? 20.52613 -0.98057  12.73744  1.000 12.94114 ?  32  LEU   A N    1 
ATOM   354  C  CA   . LEU   A 1 29  ? 20.19904 -1.97723  11.73290  1.000 13.24099 ?  32  LEU   A CA   1 
ATOM   355  C  C    . LEU   A 1 29  ? 18.70571 -1.96587  11.45717  1.000 12.96341 ?  32  LEU   A C    1 
ATOM   356  O  O    . LEU   A 1 29  ? 17.88562 -1.85856  12.37195  1.000 14.37841 ?  32  LEU   A O    1 
ATOM   357  C  CB   . LEU   A 1 29  ? 20.56617 -3.36599  12.23330  1.000 14.69050 ?  32  LEU   A CB   1 
ATOM   358  C  CG   . LEU   A 1 29  ? 22.03018 -3.58182  12.60420  1.000 16.18213 ?  32  LEU   A CG   1 
ATOM   359  C  CD1  . LEU   A 1 29  ? 22.19351 -4.97430  13.18468  1.000 19.75497 ?  32  LEU   A CD1  1 
ATOM   360  C  CD2  . LEU   A 1 29  ? 22.96163 -3.38190  11.42286  1.000 16.55437 ?  32  LEU   A CD2  1 
ATOM   361  H  H    . LEU   A 1 29  ? 20.18582 -1.15034  13.50879  1.000 15.52937 ?  32  LEU   A H    1 
ATOM   362  H  HA   . LEU   A 1 29  ? 20.67960 -1.77581  10.91474  1.000 15.88919 ?  32  LEU   A HA   1 
ATOM   363  H  HB2  . LEU   A 1 29  ? 20.03943 -3.54989  13.02679  1.000 17.62860 ?  32  LEU   A HB2  1 
ATOM   364  H  HB3  . LEU   A 1 29  ? 20.35000 -4.00489  11.53617  1.000 17.62860 ?  32  LEU   A HB3  1 
ATOM   365  H  HG   . LEU   A 1 29  ? 22.28570 -2.91937  13.26509  1.000 19.41855 ?  32  LEU   A HG   1 
ATOM   366  H  HD11 . LEU   A 1 29  ? 23.08269 -5.05621  13.56355  1.000 23.70597 ?  32  LEU   A HD11 1 
ATOM   367  H  HD12 . LEU   A 1 29  ? 21.52594 -5.10878  13.87546  1.000 23.70597 ?  32  LEU   A HD12 1 
ATOM   368  H  HD13 . LEU   A 1 29  ? 22.07385 -5.62730  12.47745  1.000 23.70597 ?  32  LEU   A HD13 1 
ATOM   369  H  HD21 . LEU   A 1 29  ? 23.85407 -3.66865  11.67229  1.000 19.86524 ?  32  LEU   A HD21 1 
ATOM   370  H  HD22 . LEU   A 1 29  ? 22.64129 -3.91034  10.67516  1.000 19.86524 ?  32  LEU   A HD22 1 
ATOM   371  H  HD23 . LEU   A 1 29  ? 22.97099 -2.44191  11.18363  1.000 19.86524 ?  32  LEU   A HD23 1 
ATOM   372  N  N    . ILE   A 1 30  ? 18.36472 -2.14145  10.19251  1.000 13.03618 ?  33  ILE   A N    1 
ATOM   373  C  CA   . ILE   A 1 30  ? 16.99716 -2.38706  9.73900   1.000 12.93910 ?  33  ILE   A CA   1 
ATOM   374  C  C    . ILE   A 1 30  ? 17.00427 -3.74616  9.05006   1.000 12.62370 ?  33  ILE   A C    1 
ATOM   375  O  O    . ILE   A 1 30  ? 17.78232 -3.94508  8.11493   1.000 14.06904 ?  33  ILE   A O    1 
ATOM   376  C  CB   . ILE   A 1 30  ? 16.51291 -1.31130  8.75375   1.000 13.96895 ?  33  ILE   A CB   1 
ATOM   377  C  CG1  . ILE   A 1 30  ? 16.80437 0.09453   9.26865   1.000 15.45703 ?  33  ILE   A CG1  1 
ATOM   378  C  CG2  . ILE   A 1 30  ? 15.03285 -1.50097  8.48997   1.000 15.30949 ?  33  ILE   A CG2  1 
ATOM   379  C  CD1  . ILE   A 1 30  ? 16.46397 1.18062   8.27482   1.000 17.80502 ?  33  ILE   A CD1  1 
ATOM   380  H  H    . ILE   A 1 30  ? 18.93057 -2.12272  9.54516   1.000 15.64342 ?  33  ILE   A H    1 
ATOM   381  H  HA   . ILE   A 1 30  ? 16.39880 -2.40009  10.50234  1.000 15.52692 ?  33  ILE   A HA   1 
ATOM   382  H  HB   . ILE   A 1 30  ? 17.00228 -1.41297  7.92243   1.000 16.76274 ?  33  ILE   A HB   1 
ATOM   383  H  HG12 . ILE   A 1 30  ? 16.28013 0.24954   10.06993  1.000 18.54843 ?  33  ILE   A HG12 1 
ATOM   384  H  HG13 . ILE   A 1 30  ? 17.75019 0.16359   9.47249   1.000 18.54843 ?  33  ILE   A HG13 1 
ATOM   385  H  HG21 . ILE   A 1 30  ? 14.75747 -0.89444  7.78485   1.000 18.37139 ?  33  ILE   A HG21 1 
ATOM   386  H  HG22 . ILE   A 1 30  ? 14.87573 -2.41846  8.21717   1.000 18.37139 ?  33  ILE   A HG22 1 
ATOM   387  H  HG23 . ILE   A 1 30  ? 14.53999 -1.30859  9.30297   1.000 18.37139 ?  33  ILE   A HG23 1 
ATOM   388  H  HD11 . ILE   A 1 30  ? 16.91242 1.99996   8.53648   1.000 21.36603 ?  33  ILE   A HD11 1 
ATOM   389  H  HD12 . ILE   A 1 30  ? 16.76260 0.90705   7.39342   1.000 21.36603 ?  33  ILE   A HD12 1 
ATOM   390  H  HD13 . ILE   A 1 30  ? 15.50344 1.31583   8.27144   1.000 21.36603 ?  33  ILE   A HD13 1 
ATOM   391  N  N    . VAL   A 1 31  ? 16.17765 -4.68336  9.51711   1.000 12.91881 ?  34  VAL   A N    1 
ATOM   392  C  CA   . VAL   A 1 31  ? 16.14870 -6.05262  9.00595   1.000 13.77792 ?  34  VAL   A CA   1 
ATOM   393  C  C    . VAL   A 1 31  ? 14.77241 -6.29458  8.41565   1.000 12.49015 ?  34  VAL   A C    1 
ATOM   394  O  O    . VAL   A 1 31  ? 13.76553 -6.17759  9.12013   1.000 13.90677 ?  34  VAL   A O    1 
ATOM   395  C  CB   . VAL   A 1 31  ? 16.46430 -7.07699  10.11140  1.000 15.07257 ?  34  VAL   A CB   1 
ATOM   396  C  CG1  . VAL   A 1 31  ? 16.46431 -8.46837  9.53789   1.000 16.26972 ?  34  VAL   A CG1  1 
ATOM   397  C  CG2  . VAL   A 1 31  ? 17.81053 -6.72895  10.77279  1.000 17.76884 ?  34  VAL   A CG2  1 
ATOM   398  H  H    . VAL   A 1 31  ? 15.60926 -4.54455  10.14740  1.000 15.50257 ?  34  VAL   A H    1 
ATOM   399  H  HA   . VAL   A 1 31  ? 16.80644 -6.15234  8.30002   1.000 16.53350 ?  34  VAL   A HA   1 
ATOM   400  H  HB   . VAL   A 1 31  ? 15.78202 -7.04768  10.80026  1.000 18.08708 ?  34  VAL   A HB   1 
ATOM   401  H  HG11 . VAL   A 1 31  ? 16.82623 -9.08150  10.19667  1.000 19.52366 ?  34  VAL   A HG11 1 
ATOM   402  H  HG12 . VAL   A 1 31  ? 15.55353 -8.71922  9.31776   1.000 19.52366 ?  34  VAL   A HG12 1 
ATOM   403  H  HG13 . VAL   A 1 31  ? 17.01316 -8.48032  8.73819   1.000 19.52366 ?  34  VAL   A HG13 1 
ATOM   404  H  HG21 . VAL   A 1 31  ? 18.08783 -7.47019  11.33366  1.000 21.32261 ?  34  VAL   A HG21 1 
ATOM   405  H  HG22 . VAL   A 1 31  ? 18.47157 -6.57277  10.08031  1.000 21.32261 ?  34  VAL   A HG22 1 
ATOM   406  H  HG23 . VAL   A 1 31  ? 17.70052 -5.92973  11.31136  1.000 21.32261 ?  34  VAL   A HG23 1 
ATOM   407  N  N    . ILE   A 1 32  ? 14.72928 -6.65012  7.13735   1.000 12.56684 ?  35  ILE   A N    1 
ATOM   408  C  CA   . ILE   A 1 32  ? 13.48168 -6.83809  6.41968   1.000 11.76165 ?  35  ILE   A CA   1 
ATOM   409  C  C    . ILE   A 1 32  ? 13.50048 -8.21670  5.79164   1.000 12.68096 ?  35  ILE   A C    1 
ATOM   410  O  O    . ILE   A 1 32  ? 14.35342 -8.49480  4.94368   1.000 13.59639 ?  35  ILE   A O    1 
ATOM   411  C  CB   . ILE   A 1 32  ? 13.29282 -5.75599  5.34676   1.000 13.01252 ?  35  ILE   A CB   1 
ATOM   412  C  CG1  . ILE   A 1 32  ? 13.32344 -4.36875  5.99113   1.000 13.35557 ?  35  ILE   A CG1  1 
ATOM   413  C  CG2  . ILE   A 1 32  ? 12.01675 -6.01105  4.56378   1.000 13.74937 ?  35  ILE   A CG2  1 
ATOM   414  C  CD1  . ILE   A 1 32  ? 13.41934 -3.23740  5.00475   1.000 15.07824 ?  35  ILE   A CD1  1 
ATOM   415  H  H    . ILE   A 1 32  ? 15.42788 -6.79083  6.65593   1.000 15.08021 ?  35  ILE   A H    1 
ATOM   416  H  HA   . ILE   A 1 32  ? 12.73616 -6.80323  7.03927   1.000 14.11398 ?  35  ILE   A HA   1 
ATOM   417  H  HB   . ILE   A 1 32  ? 14.02703 -5.79340  4.71395   1.000 15.61503 ?  35  ILE   A HB   1 
ATOM   418  H  HG12 . ILE   A 1 32  ? 12.50863 -4.24563  6.50280   1.000 16.02669 ?  35  ILE   A HG12 1 
ATOM   419  H  HG13 . ILE   A 1 32  ? 14.09451 -4.31519  6.57720   1.000 16.02669 ?  35  ILE   A HG13 1 
ATOM   420  H  HG21 . ILE   A 1 32  ? 11.85740 -5.26296  3.96725   1.000 16.49924 ?  35  ILE   A HG21 1 
ATOM   421  H  HG22 . ILE   A 1 32  ? 12.11919 -6.82759  4.05029   1.000 16.49924 ?  35  ILE   A HG22 1 
ATOM   422  H  HG23 . ILE   A 1 32  ? 11.27763 -6.10173  5.18538   1.000 16.49924 ?  35  ILE   A HG23 1 
ATOM   423  H  HD11 . ILE   A 1 32  ? 13.47671 -2.39942  5.48993   1.000 18.09389 ?  35  ILE   A HD11 1 
ATOM   424  H  HD12 . ILE   A 1 32  ? 14.21286 -3.35944  4.46039   1.000 18.09389 ?  35  ILE   A HD12 1 
ATOM   425  H  HD13 . ILE   A 1 32  ? 12.62885 -3.24069  4.44260   1.000 18.09389 ?  35  ILE   A HD13 1 
ATOM   426  N  N    . ARG   A 1 33  ? 12.56114 -9.07636  6.19554   1.000 12.99452 ?  36  ARG   A N    1 
ATOM   427  C  CA   . ARG   A 1 33  ? 12.44740 -10.42461 5.65600   1.000 12.85184 ?  36  ARG   A CA   1 
ATOM   428  C  C    . ARG   A 1 33  ? 11.21220 -10.49630 4.78132   1.000 12.73021 ?  36  ARG   A C    1 
ATOM   429  O  O    . ARG   A 1 33  ? 10.17282 -9.94970  5.15663   1.000 13.73696 ?  36  ARG   A O    1 
ATOM   430  C  CB   . ARG   A 1 33  ? 12.34027 -11.44352 6.79223   1.000 15.91913 ?  36  ARG   A CB   1 
ATOM   431  C  CG   . ARG   A 1 33  ? 13.66183 -11.58321 7.54582   1.000 19.56221 ?  36  ARG   A CG   1 
ATOM   432  C  CD   . ARG   A 1 33  ? 13.53017 -12.39721 8.83397   1.000 24.29868 ?  36  ARG   A CD   1 
ATOM   433  N  NE   . ARG   A 1 33  ? 13.23818 -13.80431 8.57344   1.000 30.00371 ?  36  ARG   A NE   1 
ATOM   434  C  CZ   . ARG   A 1 33  ? 14.15146 -14.76930 8.56732   1.000 36.53792 ?  36  ARG   A CZ   1 
ATOM   435  N  NH1  . ARG   A 1 33  ? 15.43364 -14.51235 8.78025   1.000 38.24886 ?  36  ARG   A NH1  1 
ATOM   436  N  NH2  . ARG   A 1 33  ? 13.76876 -16.02553 8.35018   1.000 38.69180 ?  36  ARG   A NH2  1 
ATOM   437  H  H    . ARG   A 1 33  ? 11.96965 -8.89343  6.79242   1.000 15.59342 ?  36  ARG   A H    1 
ATOM   438  H  HA   . ARG   A 1 33  ? 13.22450 -10.64569 5.11922   1.000 15.42220 ?  36  ARG   A HA   1 
ATOM   439  N  N    . GLY   A 1 34  ? 11.29731 -11.19400 3.65070   1.000 13.10991 ?  37  GLY   A N    1 
ATOM   440  C  CA   . GLY   A 1 34  ? 10.13950 -11.26794 2.77996   1.000 13.76692 ?  37  GLY   A CA   1 
ATOM   441  C  C    . GLY   A 1 34  ? 10.37895 -12.19671 1.61594   1.000 12.87338 ?  37  GLY   A C    1 
ATOM   442  O  O    . GLY   A 1 34  ? 11.30526 -13.01138 1.61707   1.000 14.30570 ?  37  GLY   A O    1 
ATOM   443  H  H    . GLY   A 1 34  ? 11.99349 -11.61856 3.37743   1.000 15.73189 ?  37  GLY   A H    1 
ATOM   444  H  HA2  . GLY   A 1 34  ? 9.37589  -11.59302 3.28209   1.000 16.52030 ?  37  GLY   A HA2  1 
ATOM   445  H  HA3  . GLY   A 1 34  ? 9.93691  -10.38486 2.43352   1.000 16.52030 ?  37  GLY   A HA3  1 
ATOM   446  N  N    . HIS   A 1 35  ? 9.49155  -12.08844 0.63953   1.000 13.75404 ?  38  HIS   A N    1 
ATOM   447  C  CA   A HIS   A 1 35  ? 9.49841  -12.98828 -0.50246  0.558 13.15430 ?  38  HIS   A CA   1 
ATOM   448  C  CA   B HIS   A 1 35  ? 9.49829  -12.98803 -0.50153  0.442 14.48961 ?  38  HIS   A CA   1 
ATOM   449  C  C    . HIS   A 1 35  ? 8.95619  -12.23173 -1.70386  1.000 13.06859 ?  38  HIS   A C    1 
ATOM   450  O  O    . HIS   A 1 35  ? 8.03457  -11.43754 -1.57823  1.000 14.20853 ?  38  HIS   A O    1 
ATOM   451  C  CB   A HIS   A 1 35  ? 8.63047  -14.19965 -0.13914  0.558 16.87578 ?  38  HIS   A CB   1 
ATOM   452  C  CB   B HIS   A 1 35  ? 8.64992  -14.20892 -0.12110  0.442 19.63090 ?  38  HIS   A CB   1 
ATOM   453  C  CG   A HIS   A 1 35  ? 8.66426  -15.30160 -1.14010  0.558 16.63662 ?  38  HIS   A CG   1 
ATOM   454  C  CG   B HIS   A 1 35  ? 8.24613  -15.06131 -1.27400  0.442 23.19113 ?  38  HIS   A CG   1 
ATOM   455  N  ND1  A HIS   A 1 35  ? 9.58293  -16.32748 -1.08938  0.558 17.23654 ?  38  HIS   A ND1  1 
ATOM   456  N  ND1  B HIS   A 1 35  ? 7.07151  -14.86439 -1.96632  0.442 24.14804 ?  38  HIS   A ND1  1 
ATOM   457  C  CD2  A HIS   A 1 35  ? 7.87144  -15.55491 -2.20639  0.558 16.28600 ?  38  HIS   A CD2  1 
ATOM   458  C  CD2  B HIS   A 1 35  ? 8.84320  -16.13744 -1.83727  0.442 25.60706 ?  38  HIS   A CD2  1 
ATOM   459  C  CE1  A HIS   A 1 35  ? 9.36651  -17.15428 -2.09522  0.558 17.35903 ?  38  HIS   A CE1  1 
ATOM   460  C  CE1  B HIS   A 1 35  ? 6.97445  -15.76842 -2.92369  0.442 26.01484 ?  38  HIS   A CE1  1 
ATOM   461  N  NE2  A HIS   A 1 35  ? 8.33217  -16.70973 -2.78456  0.558 17.85176 ?  38  HIS   A NE2  1 
ATOM   462  N  NE2  B HIS   A 1 35  ? 8.03585  -16.55280 -2.86703  0.442 26.48790 ?  38  HIS   A NE2  1 
ATOM   463  H  H    . HIS   A 1 35  ? 8.86890  -11.49573 0.61517   1.000 16.50485 ?  38  HIS   A H    1 
ATOM   464  H  HA   . HIS   A 1 35  ? 10.38611 -13.29114 -0.74976  1.000 17.38753 ?  38  HIS   A HA   1 
ATOM   465  H  HB2  A HIS   A 1 35  ? 8.94129  -14.56093 0.70571   0.558 20.25093 ?  38  HIS   A HB2  1 
ATOM   466  H  HB2  B HIS   A 1 35  ? 9.16162  -14.76337 0.48852   0.442 23.55708 ?  38  HIS   A HB2  1 
ATOM   467  H  HB3  A HIS   A 1 35  ? 7.70948  -13.90681 -0.05599  0.558 20.25093 ?  38  HIS   A HB3  1 
ATOM   468  H  HB3  B HIS   A 1 35  ? 7.83947  -13.89939 0.31280   0.442 23.55708 ?  38  HIS   A HB3  1 
ATOM   469  H  HD2  A HIS   A 1 35  ? 7.15017  -15.04263 -2.49317  0.558 19.54319 ?  38  HIS   A HD2  1 
ATOM   470  H  HD2  B HIS   A 1 35  ? 9.64832  -16.52273 -1.57607  0.442 30.72847 ?  38  HIS   A HD2  1 
ATOM   471  H  HE1  A HIS   A 1 35  ? 9.85895  -17.91982 -2.28586  0.558 20.83083 ?  38  HIS   A HE1  1 
ATOM   472  H  HE1  B HIS   A 1 35  ? 6.27691  -15.84073 -3.53453  0.442 31.21781 ?  38  HIS   A HE1  1 
ATOM   473  H  HE2  A HIS   A 1 35  ? 8.00051  -17.08433 -3.48404  0.558 21.42212 ?  38  HIS   A HE2  1 
ATOM   474  H  HE2  B HIS   A 1 35  ? 8.19529  -17.21626 -3.39049  0.442 31.78548 ?  38  HIS   A HE2  1 
ATOM   475  N  N    . VAL   A 1 36  ? 9.53465  -12.48153 -2.86842  1.000 13.66622 ?  39  VAL   A N    1 
ATOM   476  C  CA   . VAL   A 1 36  ? 9.10850  -11.83872 -4.10494  1.000 14.01314 ?  39  VAL   A CA   1 
ATOM   477  C  C    . VAL   A 1 36  ? 8.08326  -12.71499 -4.79782  1.000 14.70461 ?  39  VAL   A C    1 
ATOM   478  O  O    . VAL   A 1 36  ? 8.37096  -13.88405 -5.08809  1.000 16.97928 ?  39  VAL   A O    1 
ATOM   479  C  CB   . VAL   A 1 36  ? 10.31750 -11.58972 -5.02211  1.000 15.13230 ?  39  VAL   A CB   1 
ATOM   480  C  CG1  . VAL   A 1 36  ? 9.88184  -10.90598 -6.29652  1.000 15.59534 ?  39  VAL   A CG1  1 
ATOM   481  C  CG2  . VAL   A 1 36  ? 11.37191 -10.76821 -4.30252  1.000 16.53429 ?  39  VAL   A CG2  1 
ATOM   482  H  H    . VAL   A 1 36  ? 10.18896 -13.02984 -2.97248  1.000 16.39946 ?  39  VAL   A H    1 
ATOM   483  H  HA   . VAL   A 1 36  ? 8.68584  -10.99160 -3.89366  1.000 16.81577 ?  39  VAL   A HA   1 
ATOM   484  H  HB   . VAL   A 1 36  ? 10.71332 -12.44298 -5.25912  1.000 18.15876 ?  39  VAL   A HB   1 
ATOM   485  H  HG11 . VAL   A 1 36  ? 10.66795 -10.67614 -6.81623  1.000 18.71441 ?  39  VAL   A HG11 1 
ATOM   486  H  HG12 . VAL   A 1 36  ? 9.31635  -11.51070 -6.80193  1.000 18.71441 ?  39  VAL   A HG12 1 
ATOM   487  H  HG13 . VAL   A 1 36  ? 9.38795  -10.10224 -6.07075  1.000 18.71441 ?  39  VAL   A HG13 1 
ATOM   488  H  HG21 . VAL   A 1 36  ? 12.10188 -10.58542 -4.91460  1.000 19.84115 ?  39  VAL   A HG21 1 
ATOM   489  H  HG22 . VAL   A 1 36  ? 10.97405 -9.93541  -4.00410  1.000 19.84115 ?  39  VAL   A HG22 1 
ATOM   490  H  HG23 . VAL   A 1 36  ? 11.69783 -11.27110 -3.53978  1.000 19.84115 ?  39  VAL   A HG23 1 
ATOM   491  N  N    . PRO   A 1 37  ? 6.89874  -12.21122 -5.13142  1.000 15.14150 ?  40  PRO   A N    1 
ATOM   492  C  CA   . PRO   A 1 37  ? 5.93106  -13.03508 -5.86225  1.000 17.55336 ?  40  PRO   A CA   1 
ATOM   493  C  C    . PRO   A 1 37  ? 6.38059  -13.34036 -7.28559  1.000 16.83920 ?  40  PRO   A C    1 
ATOM   494  O  O    . PRO   A 1 37  ? 7.24054  -12.67468 -7.86491  1.000 18.13442 ?  40  PRO   A O    1 
ATOM   495  C  CB   . PRO   A 1 37  ? 4.65315  -12.19238 -5.85012  1.000 20.18958 ?  40  PRO   A CB   1 
ATOM   496  C  CG   . PRO   A 1 37  ? 5.06081  -10.84782 -5.57054  1.000 20.54587 ?  40  PRO   A CG   1 
ATOM   497  C  CD   . PRO   A 1 37  ? 6.34647  -10.89179 -4.78762  1.000 16.15218 ?  40  PRO   A CD   1 
ATOM   498  H  HA   . PRO   A 1 37  ? 5.77937  -13.86923 -5.39097  1.000 21.06403 ?  40  PRO   A HA   1 
ATOM   499  H  HB2  . PRO   A 1 37  ? 4.22058  -12.24582 -6.71668  1.000 24.22749 ?  40  PRO   A HB2  1 
ATOM   500  H  HB3  . PRO   A 1 37  ? 4.05501  -12.51931 -5.16001  1.000 24.22749 ?  40  PRO   A HB3  1 
ATOM   501  H  HG2  . PRO   A 1 37  ? 5.19595  -10.37761 -6.40811  1.000 24.65504 ?  40  PRO   A HG2  1 
ATOM   502  H  HG3  . PRO   A 1 37  ? 4.36879  -10.40889 -5.05156  1.000 24.65504 ?  40  PRO   A HG3  1 
ATOM   503  H  HD2  . PRO   A 1 37  ? 6.94609  -10.18209 -5.06633  1.000 19.38262 ?  40  PRO   A HD2  1 
ATOM   504  H  HD3  . PRO   A 1 37  ? 6.17440  -10.82586 -3.83528  1.000 19.38262 ?  40  PRO   A HD3  1 
ATOM   505  N  N    . SER   A 1 38  ? 5.76964  -14.37766 -7.85519  1.000 19.55037 ?  41  SER   A N    1 
ATOM   506  C  CA   . SER   A 1 38  ? 6.21939  -14.89309 -9.14622  1.000 21.43862 ?  41  SER   A CA   1 
ATOM   507  C  C    . SER   A 1 38  ? 6.04440  -13.89741 -10.28409 1.000 21.82893 ?  41  SER   A C    1 
ATOM   508  O  O    . SER   A 1 38  ? 6.73534  -14.01962 -11.30175 1.000 24.37556 ?  41  SER   A O    1 
ATOM   509  C  CB   . SER   A 1 38  ? 5.48880  -16.19205 -9.50680  1.000 23.59326 ?  41  SER   A CB   1 
ATOM   510  O  OG   . SER   A 1 38  ? 4.10101  -15.96829 -9.64588  1.000 25.41562 ?  41  SER   A OG   1 
ATOM   511  H  H    . SER   A 1 38  ? 5.09868  -14.79728 -7.51853  1.000 23.46045 ?  41  SER   A H    1 
ATOM   512  H  HA   . SER   A 1 38  ? 7.16514  -15.08919 -9.05673  1.000 25.72634 ?  41  SER   A HA   1 
ATOM   513  H  HB2  . SER   A 1 38  ? 5.83969  -16.52880 -10.34607 1.000 28.31191 ?  41  SER   A HB2  1 
ATOM   514  H  HB3  . SER   A 1 38  ? 5.63441  -16.84205 -8.80168  1.000 28.31191 ?  41  SER   A HB3  1 
ATOM   515  H  HG   . SER   A 1 38  ? 3.73995  -15.92340 -8.88877  1.000 30.49875 ?  41  SER   A HG   1 
ATOM   516  N  N    . ASP   A 1 39  ? 5.12286  -12.94169 -10.15364 1.000 22.30292 ?  42  ASP   A N    1 
ATOM   517  C  CA   . ASP   A 1 39  ? 4.82953  -11.98550 -11.21379 1.000 24.33134 ?  42  ASP   A CA   1 
ATOM   518  C  C    . ASP   A 1 39  ? 5.39461  -10.60012 -10.92689 1.000 22.37654 ?  42  ASP   A C    1 
ATOM   519  O  O    . ASP   A 1 39  ? 5.02355  -9.63764  -11.60693 1.000 23.38956 ?  42  ASP   A O    1 
ATOM   520  C  CB   . ASP   A 1 39  ? 3.31753  -11.91019 -11.46003 1.000 28.81752 ?  42  ASP   A CB   1 
ATOM   521  C  CG   . ASP   A 1 39  ? 2.55988  -11.23372 -10.31706 1.000 32.62570 ?  42  ASP   A CG   1 
ATOM   522  O  OD1  . ASP   A 1 39  ? 3.00739  -11.29647 -9.15225  1.000 33.17557 ?  42  ASP   A OD1  1 
ATOM   523  O  OD2  . ASP   A 1 39  ? 1.49814  -10.62933 -10.58812 1.000 36.67754 ?  42  ASP   A OD2  1 
ATOM   524  H  H    . ASP   A 1 39  ? 4.64748  -12.82758 -9.44611  1.000 26.76351 ?  42  ASP   A H    1 
ATOM   525  H  HA   . ASP   A 1 39  ? 5.24227  -12.30065 -12.03308 1.000 29.19761 ?  42  ASP   A HA   1 
ATOM   526  H  HB2  . ASP   A 1 39  ? 3.15488  -11.40086 -12.26937 1.000 34.58103 ?  42  ASP   A HB2  1 
ATOM   527  H  HB3  . ASP   A 1 39  ? 2.96893  -12.81000 -11.55862 1.000 34.58103 ?  42  ASP   A HB3  1 
ATOM   528  N  N    . ALA   A 1 40  ? 6.28902  -10.46878 -9.95005  1.000 18.48825 ?  43  ALA   A N    1 
ATOM   529  C  CA   . ALA   A 1 40  ? 6.75801  -9.14711  -9.56838  1.000 17.01662 ?  43  ALA   A CA   1 
ATOM   530  C  C    . ALA   A 1 40  ? 7.49590  -8.45828  -10.70698 1.000 17.41568 ?  43  ALA   A C    1 
ATOM   531  O  O    . ALA   A 1 40  ? 8.33623  -9.04914  -11.39523 1.000 18.72955 ?  43  ALA   A O    1 
ATOM   532  C  CB   . ALA   A 1 40  ? 7.68601  -9.26465  -8.36836  1.000 18.25465 ?  43  ALA   A CB   1 
ATOM   533  H  H    . ALA   A 1 40  ? 6.63173  -11.11849 -9.50280  1.000 22.18591 ?  43  ALA   A H    1 
ATOM   534  H  HA   . ALA   A 1 40  ? 5.99082  -8.60001  -9.33816  1.000 20.41994 ?  43  ALA   A HA   1 
ATOM   535  H  HB1  . ALA   A 1 40  ? 8.00554  -8.38077  -8.12846  1.000 21.90558 ?  43  ALA   A HB1  1 
ATOM   536  H  HB2  . ALA   A 1 40  ? 7.19540  -9.65166  -7.62646  1.000 21.90558 ?  43  ALA   A HB2  1 
ATOM   537  H  HB3  . ALA   A 1 40  ? 8.43494  -9.83472  -8.60295  1.000 21.90558 ?  43  ALA   A HB3  1 
ATOM   538  N  N    . ASP   A 1 41  ? 7.21129  -7.16515  -10.84096 1.000 16.29880 ?  44  ASP   A N    1 
ATOM   539  C  CA   . ASP   A 1 41  ? 7.93583  -6.24382  -11.69830 1.000 17.82186 ?  44  ASP   A CA   1 
ATOM   540  C  C    . ASP   A 1 41  ? 9.03109  -5.50813  -10.91765 1.000 16.86675 ?  44  ASP   A C    1 
ATOM   541  O  O    . ASP   A 1 41  ? 10.17548 -5.41047  -11.37067 1.000 16.75877 ?  44  ASP   A O    1 
ATOM   542  C  CB   . ASP   A 1 41  ? 6.94808  -5.29306  -12.43865 1.000 20.31708 ?  44  ASP   A CB   1 
ATOM   543  C  CG   . ASP   A 1 41  ? 5.80829  -4.66686  -11.52601 1.000 20.32190 ?  44  ASP   A CG   1 
ATOM   544  O  OD1  . ASP   A 1 41  ? 5.80316  -4.85681  -10.25279 1.000 17.93569 ?  44  ASP   A OD1  1 
ATOM   545  O  OD2  . ASP   A 1 41  ? 4.91970  -3.95766  -12.13138 1.000 22.56555 ?  44  ASP   A OD2  1 
ATOM   546  H  H    . ASP   A 1 41  ? 6.56715  -6.77960  -10.42140 1.000 19.55856 ?  44  ASP   A H    1 
ATOM   547  H  HA   . ASP   A 1 41  ? 8.38694  -6.72186  -12.41166 1.000 21.38624 ?  44  ASP   A HA   1 
ATOM   548  H  HB2  . ASP   A 1 41  ? 7.45460  -4.55717  -12.81654 1.000 24.38050 ?  44  ASP   A HB2  1 
ATOM   549  H  HB3  . ASP   A 1 41  ? 6.51173  -5.79324  -13.14598 1.000 24.38050 ?  44  ASP   A HB3  1 
ATOM   550  N  N    . ARG   A 1 42  ? 8.72649  -5.03648  -9.71930  1.000 15.15508 ?  45  ARG   A N    1 
ATOM   551  C  CA   . ARG   A 1 42  ? 9.66377  -4.27477  -8.90224  1.000 13.83842 ?  45  ARG   A CA   1 
ATOM   552  C  C    . ARG   A 1 42  ? 9.04168  -4.15110  -7.52302  1.000 12.94900 ?  45  ARG   A C    1 
ATOM   553  O  O    . ARG   A 1 42  ? 7.81987  -4.27372  -7.36921  1.000 14.02320 ?  45  ARG   A O    1 
ATOM   554  C  CB   . ARG   A 1 42  ? 9.92509  -2.88091  -9.46731  1.000 13.90582 ?  45  ARG   A CB   1 
ATOM   555  C  CG   . ARG   A 1 42  ? 8.69932  -2.06945  -9.78030  1.000 14.53713 ?  45  ARG   A CG   1 
ATOM   556  C  CD   . ARG   A 1 42  ? 9.07514  -0.69135  -10.27803 1.000 15.63205 ?  45  ARG   A CD   1 
ATOM   557  N  NE   . ARG   A 1 42  ? 9.44353  0.16193   -9.15768  1.000 13.80996 ?  45  ARG   A NE   1 
ATOM   558  C  CZ   . ARG   A 1 42  ? 10.08234 1.32084   -9.27444  1.000 13.80426 ?  45  ARG   A CZ   1 
ATOM   559  N  NH1  . ARG   A 1 42  ? 10.61798 1.70881   -10.42120 1.000 16.31507 ?  45  ARG   A NH1  1 
ATOM   560  N  NH2  . ARG   A 1 42  ? 10.16145 2.12881   -8.21685  1.000 14.34483 ?  45  ARG   A NH2  1 
ATOM   561  H  H    . ARG   A 1 42  ? 7.96085  -5.14606  -9.34328  1.000 18.18610 ?  45  ARG   A H    1 
ATOM   562  H  HA   . ARG   A 1 42  ? 10.51118 -4.74426  -8.85347  1.000 16.60610 ?  45  ARG   A HA   1 
ATOM   563  H  HB2  . ARG   A 1 42  ? 10.44425 -2.38099  -8.81811  1.000 16.68699 ?  45  ARG   A HB2  1 
ATOM   564  H  HB3  . ARG   A 1 42  ? 10.42716 -2.97525  -10.29188 1.000 16.68699 ?  45  ARG   A HB3  1 
ATOM   565  H  HG2  . ARG   A 1 42  ? 8.18395  -2.51531  -10.47059 1.000 17.44455 ?  45  ARG   A HG2  1 
ATOM   566  H  HG3  . ARG   A 1 42  ? 8.16340  -1.97057  -8.97785  1.000 17.44455 ?  45  ARG   A HG3  1 
ATOM   567  H  HD2  . ARG   A 1 42  ? 9.83225  -0.75724  -10.88080 1.000 18.75846 ?  45  ARG   A HD2  1 
ATOM   568  H  HD3  . ARG   A 1 42  ? 8.31931  -0.29274  -10.73709 1.000 18.75846 ?  45  ARG   A HD3  1 
ATOM   569  H  HE   . ARG   A 1 42  ? 9.23339  -0.10208  -8.36664  1.000 16.57195 ?  45  ARG   A HE   1 
ATOM   570  H  HH11 . ARG   A 1 42  ? 10.55731 1.20579   -11.11610 1.000 19.57809 ?  45  ARG   A HH11 1 
ATOM   571  H  HH12 . ARG   A 1 42  ? 11.02662 2.46386   -10.47127 1.000 19.57809 ?  45  ARG   A HH12 1 
ATOM   572  H  HH21 . ARG   A 1 42  ? 9.80146  1.89725   -7.47093  1.000 17.21380 ?  45  ARG   A HH21 1 
ATOM   573  H  HH22 . ARG   A 1 42  ? 10.57247 2.88154   -8.28058  1.000 17.21380 ?  45  ARG   A HH22 1 
ATOM   574  N  N    . PHE   A 1 43  ? 9.88765  -3.84476  -6.53247  1.000 12.35537 ?  46  PHE   A N    1 
ATOM   575  C  CA   . PHE   A 1 43  ? 9.40629  -3.30557  -5.25843  1.000 11.79415 ?  46  PHE   A CA   1 
ATOM   576  C  C    . PHE   A 1 43  ? 10.44050 -2.31894  -4.76060  1.000 11.15991 ?  46  PHE   A C    1 
ATOM   577  O  O    . PHE   A 1 43  ? 11.53576 -2.22861  -5.30938  1.000 11.54734 ?  46  PHE   A O    1 
ATOM   578  C  CB   . PHE   A 1 43  ? 9.08962  -4.39748  -4.22156  1.000 12.07158 ?  46  PHE   A CB   1 
ATOM   579  C  CG   . PHE   A 1 43  ? 10.28891 -5.06276  -3.59777  1.000 12.32403 ?  46  PHE   A CG   1 
ATOM   580  C  CD1  . PHE   A 1 43  ? 10.84320 -6.19578  -4.16614  1.000 13.12021 ?  46  PHE   A CD1  1 
ATOM   581  C  CD2  . PHE   A 1 43  ? 10.82917 -4.59026  -2.40127  1.000 12.98301 ?  46  PHE   A CD2  1 
ATOM   582  C  CE1  . PHE   A 1 43  ? 11.92341 -6.82610  -3.56802  1.000 13.65022 ?  46  PHE   A CE1  1 
ATOM   583  C  CE2  . PHE   A 1 43  ? 11.91855 -5.21899  -1.80177  1.000 14.25292 ?  46  PHE   A CE2  1 
ATOM   584  C  CZ   . PHE   A 1 43  ? 12.46209 -6.35171  -2.38692  1.000 14.15000 ?  46  PHE   A CZ   1 
ATOM   585  H  H    . PHE   A 1 43  ? 10.74126 -3.94032  -6.57524  1.000 14.82645 ?  46  PHE   A H    1 
ATOM   586  H  HA   . PHE   A 1 43  ? 8.57113  -2.83386  -5.40299  1.000 14.15299 ?  46  PHE   A HA   1 
ATOM   587  H  HB2  . PHE   A 1 43  ? 8.57506  -3.99696  -3.50342  1.000 14.48589 ?  46  PHE   A HB2  1 
ATOM   588  H  HB3  . PHE   A 1 43  ? 8.56846  -5.09024  -4.65674  1.000 14.48589 ?  46  PHE   A HB3  1 
ATOM   589  H  HD1  . PHE   A 1 43  ? 10.48856 -6.53708  -4.95522  1.000 15.74425 ?  46  PHE   A HD1  1 
ATOM   590  H  HD2  . PHE   A 1 43  ? 10.45503 -3.84139  -1.99616  1.000 15.57961 ?  46  PHE   A HD2  1 
ATOM   591  H  HE1  . PHE   A 1 43  ? 12.29165 -7.58057  -3.96811  1.000 16.38027 ?  46  PHE   A HE1  1 
ATOM   592  H  HE2  . PHE   A 1 43  ? 12.27869 -4.88068  -1.01389  1.000 17.10351 ?  46  PHE   A HE2  1 
ATOM   593  H  HZ   . PHE   A 1 43  ? 13.18104 -6.78757  -1.98938  1.000 16.98000 ?  46  PHE   A HZ   1 
ATOM   594  N  N    . GLN   A 1 44  ? 10.09430 -1.58053  -3.71050  1.000 11.07427 ?  47  GLN   A N    1 
ATOM   595  C  CA   . GLN   A 1 44  ? 11.06543 -0.64957  -3.16612  1.000 11.12262 ?  47  GLN   A CA   1 
ATOM   596  C  C    . GLN   A 1 44  ? 10.90661 -0.53657  -1.66093  1.000 10.55641 ?  47  GLN   A C    1 
ATOM   597  O  O    . GLN   A 1 44  ? 9.81068  -0.66060  -1.10965  1.000 11.42595 ?  47  GLN   A O    1 
ATOM   598  C  CB   . GLN   A 1 44  ? 10.95224 0.72233   -3.82493  1.000 11.82347 ?  47  GLN   A CB   1 
ATOM   599  C  CG   . GLN   A 1 44  ? 9.68594  1.46671   -3.46165  1.000 12.44421 ?  47  GLN   A CG   1 
ATOM   600  C  CD   . GLN   A 1 44  ? 9.22678  2.43935   -4.54428  1.000 12.47602 ?  47  GLN   A CD   1 
ATOM   601  O  OE1  . GLN   A 1 44  ? 8.90530  2.01773   -5.65731  1.000 13.97103 ?  47  GLN   A OE1  1 
ATOM   602  N  NE2  . GLN   A 1 44  ? 9.23057  3.73511   -4.24929  1.000 12.56469 ?  47  GLN   A NE2  1 
ATOM   603  H  H    . GLN   A 1 44  ? 9.33165  -1.60245  -3.31365  1.000 13.28912 ?  47  GLN   A H    1 
ATOM   604  H  HA   . GLN   A 1 44  ? 11.95631 -0.99711  -3.32875  1.000 13.34714 ?  47  GLN   A HA   1 
ATOM   605  H  HB2  . GLN   A 1 44  ? 11.70605 1.26564   -3.54654  1.000 14.18817 ?  47  GLN   A HB2  1 
ATOM   606  H  HB3  . GLN   A 1 44  ? 10.96336 0.60813   -4.78812  1.000 14.18817 ?  47  GLN   A HB3  1 
ATOM   607  H  HG2  . GLN   A 1 44  ? 8.97401  0.82384   -3.31753  1.000 14.93305 ?  47  GLN   A HG2  1 
ATOM   608  H  HG3  . GLN   A 1 44  ? 9.84240  1.97578   -2.65093  1.000 14.93305 ?  47  GLN   A HG3  1 
ATOM   609  H  HE21 . GLN   A 1 44  ? 8.97786  4.31051   -4.83636  1.000 15.07763 ?  47  GLN   A HE21 1 
ATOM   610  H  HE22 . GLN   A 1 44  ? 9.48574  3.99826   -3.47132  1.000 15.07763 ?  47  GLN   A HE22 1 
ATOM   611  N  N    . VAL   A 1 45  ? 12.04100 -0.27470  -1.01574  1.000 10.75256 ?  48  VAL   A N    1 
ATOM   612  C  CA   . VAL   A 1 45  ? 12.14108 0.10825   0.39097   1.000 11.03614 ?  48  VAL   A CA   1 
ATOM   613  C  C    . VAL   A 1 45  ? 12.64970 1.54092   0.40740   1.000 10.98700 ?  48  VAL   A C    1 
ATOM   614  O  O    . VAL   A 1 45  ? 13.73828 1.81814   -0.11260  1.000 11.85901 ?  48  VAL   A O    1 
ATOM   615  C  CB   . VAL   A 1 45  ? 13.11044 -0.81647  1.14174   1.000 11.65813 ?  48  VAL   A CB   1 
ATOM   616  C  CG1  . VAL   A 1 45  ? 13.25630 -0.35539  2.59396   1.000 13.14205 ?  48  VAL   A CG1  1 
ATOM   617  C  CG2  . VAL   A 1 45  ? 12.64104 -2.25756  1.06289   1.000 12.91087 ?  48  VAL   A CG2  1 
ATOM   618  H  H    . VAL   A 1 45  ? 12.81200 -0.31463  -1.39463  1.000 12.90307 ?  48  VAL   A H    1 
ATOM   619  H  HA   . VAL   A 1 45  ? 11.27308 0.06502   0.82180   1.000 13.24337 ?  48  VAL   A HA   1 
ATOM   620  H  HB   . VAL   A 1 45  ? 13.98531 -0.77315  0.72505   1.000 13.98975 ?  48  VAL   A HB   1 
ATOM   621  H  HG11 . VAL   A 1 45  ? 13.71054 -1.04664  3.10065   1.000 15.77046 ?  48  VAL   A HG11 1 
ATOM   622  H  HG12 . VAL   A 1 45  ? 13.77448 0.46434   2.61450   1.000 15.77046 ?  48  VAL   A HG12 1 
ATOM   623  H  HG13 . VAL   A 1 45  ? 12.37416 -0.19849  2.96560   1.000 15.77046 ?  48  VAL   A HG13 1 
ATOM   624  H  HG21 . VAL   A 1 45  ? 13.15989 -2.79309  1.68330   1.000 15.49304 ?  48  VAL   A HG21 1 
ATOM   625  H  HG22 . VAL   A 1 45  ? 11.70083 -2.29676  1.29818   1.000 15.49304 ?  48  VAL   A HG22 1 
ATOM   626  H  HG23 . VAL   A 1 45  ? 12.76938 -2.58243  0.15797   1.000 15.49304 ?  48  VAL   A HG23 1 
ATOM   627  N  N    . ASP   A 1 46  ? 11.86297 2.44309   0.99058   1.000 10.58040 ?  49  ASP   A N    1 
ATOM   628  C  CA   . ASP   A 1 46  ? 12.15278 3.86886   1.01515   1.000 10.49295 ?  49  ASP   A CA   1 
ATOM   629  C  C    . ASP   A 1 46  ? 12.30659 4.35189   2.45323   1.000 10.89938 ?  49  ASP   A C    1 
ATOM   630  O  O    . ASP   A 1 46  ? 11.40629 4.18074   3.28276   1.000 11.82988 ?  49  ASP   A O    1 
ATOM   631  C  CB   . ASP   A 1 46  ? 11.00573 4.63713   0.34794   1.000 11.65411 ?  49  ASP   A CB   1 
ATOM   632  C  CG   . ASP   A 1 46  ? 10.95547 4.43088   -1.17497  1.000 12.56270 ?  49  ASP   A CG   1 
ATOM   633  O  OD1  . ASP   A 1 46  ? 11.93549 3.93387   -1.77571  1.000 13.14495 ?  49  ASP   A OD1  1 
ATOM   634  O  OD2  . ASP   A 1 46  ? 9.90187  4.79566   -1.75690  1.000 13.98727 ?  49  ASP   A OD2  1 
ATOM   635  H  H    . ASP   A 1 46  ? 11.12953 2.24264   1.39243   1.000 12.69649 ?  49  ASP   A H    1 
ATOM   636  H  HA   . ASP   A 1 46  ? 12.98837 4.03722   0.55218   1.000 12.59154 ?  49  ASP   A HA   1 
ATOM   637  H  HB2  . ASP   A 1 46  ? 10.16322 4.33215   0.71952   1.000 13.98493 ?  49  ASP   A HB2  1 
ATOM   638  H  HB3  . ASP   A 1 46  ? 11.11960 5.58525   0.51825   1.000 13.98493 ?  49  ASP   A HB3  1 
ATOM   639  N  N    . LEU   A 1 47  ? 13.42799 4.98354   2.74398   1.000 10.17921 ?  50  LEU   A N    1 
ATOM   640  C  CA   . LEU   A 1 47  ? 13.65288 5.65456   4.02611   1.000 10.48292 ?  50  LEU   A CA   1 
ATOM   641  C  C    . LEU   A 1 47  ? 13.36477 7.12979   3.76427   1.000 10.98237 ?  50  LEU   A C    1 
ATOM   642  O  O    . LEU   A 1 47  ? 14.08141 7.78259   2.99960   1.000 12.18707 ?  50  LEU   A O    1 
ATOM   643  C  CB   . LEU   A 1 47  ? 15.08337 5.43374   4.51221   1.000 11.73786 ?  50  LEU   A CB   1 
ATOM   644  C  CG   . LEU   A 1 47  ? 15.49073 3.97024   4.66551   1.000 13.41801 ?  50  LEU   A CG   1 
ATOM   645  C  CD1  . LEU   A 1 47  ? 16.88295 3.88566   5.26516   1.000 13.20552 ?  50  LEU   A CD1  1 
ATOM   646  C  CD2  . LEU   A 1 47  ? 14.49588 3.15969   5.44641   1.000 15.19407 ?  50  LEU   A CD2  1 
ATOM   647  H  H    . LEU   A 1 47  ? 14.09579 5.04311   2.20537   1.000 12.21505 ?  50  LEU   A H    1 
ATOM   648  H  HA   . LEU   A 1 47  ? 13.06410 5.31462   4.71797   1.000 12.57950 ?  50  LEU   A HA   1 
ATOM   649  H  HB2  . LEU   A 1 47  ? 15.69042 5.84060   3.87437   1.000 14.08543 ?  50  LEU   A HB2  1 
ATOM   650  H  HB3  . LEU   A 1 47  ? 15.18135 5.85657   5.37969   1.000 14.08543 ?  50  LEU   A HB3  1 
ATOM   651  H  HG   . LEU   A 1 47  ? 15.50677 3.56600   3.78390   1.000 16.10162 ?  50  LEU   A HG   1 
ATOM   652  H  HD11 . LEU   A 1 47  ? 17.15348 2.95501   5.30534   1.000 15.84662 ?  50  LEU   A HD11 1 
ATOM   653  H  HD12 . LEU   A 1 47  ? 17.49846 4.38522   4.70616   1.000 15.84662 ?  50  LEU   A HD12 1 
ATOM   654  H  HD13 . LEU   A 1 47  ? 16.86567 4.26395   6.15819   1.000 15.84662 ?  50  LEU   A HD13 1 
ATOM   655  H  HD21 . LEU   A 1 47  ? 14.84458 2.26261   5.56700   1.000 18.23289 ?  50  LEU   A HD21 1 
ATOM   656  H  HD22 . LEU   A 1 47  ? 14.35532 3.57878   6.30984   1.000 18.23289 ?  50  LEU   A HD22 1 
ATOM   657  H  HD23 . LEU   A 1 47  ? 13.66028 3.12648   4.95490   1.000 18.23289 ?  50  LEU   A HD23 1 
ATOM   658  N  N    . GLN   A 1 48  ? 12.30595 7.64063   4.39175   1.000 11.32796 ?  51  GLN   A N    1 
ATOM   659  C  CA   . GLN   A 1 48  ? 11.66729 8.89199   4.01750   1.000 12.08451 ?  51  GLN   A CA   1 
ATOM   660  C  C    . GLN   A 1 48  ? 11.74062 9.92581   5.13049   1.000 12.44628 ?  51  GLN   A C    1 
ATOM   661  O  O    . GLN   A 1 48  ? 11.80791 9.59384   6.32671   1.000 12.78187 ?  51  GLN   A O    1 
ATOM   662  C  CB   . GLN   A 1 48  ? 10.16522 8.67321   3.71918   1.000 12.55998 ?  51  GLN   A CB   1 
ATOM   663  C  CG   . GLN   A 1 48  ? 9.91417  7.66093   2.64474   1.000 13.33355 ?  51  GLN   A CG   1 
ATOM   664  C  CD   . GLN   A 1 48  ? 8.45185  7.30952   2.39725   1.000 13.40587 ?  51  GLN   A CD   1 
ATOM   665  O  OE1  . GLN   A 1 48  ? 8.17489  6.38243   1.64491   1.000 14.52575 ?  51  GLN   A OE1  1 
ATOM   666  N  NE2  . GLN   A 1 48  ? 7.52152  8.06313   2.96841   1.000 13.96621 ?  51  GLN   A NE2  1 
ATOM   667  H  H    . GLN   A 1 48  ? 11.92723 7.26163   5.06446   1.000 13.59356 ?  51  GLN   A H    1 
ATOM   668  H  HA   . GLN   A 1 48  ? 12.13735 9.23452   3.24121   1.000 14.50141 ?  51  GLN   A HA   1 
ATOM   669  H  HB2  . GLN   A 1 48  ? 9.72704  8.36431   4.52756   1.000 15.07198 ?  51  GLN   A HB2  1 
ATOM   670  H  HB3  . GLN   A 1 48  ? 9.77705  9.51456   3.43218   1.000 15.07198 ?  51  GLN   A HB3  1 
ATOM   671  H  HG2  . GLN   A 1 48  ? 10.27194 8.00560   1.81161   1.000 16.00026 ?  51  GLN   A HG2  1 
ATOM   672  H  HG3  . GLN   A 1 48  ? 10.37009 6.83977   2.88707   1.000 16.00026 ?  51  GLN   A HG3  1 
ATOM   673  H  HE21 . GLN   A 1 48  ? 6.68907  7.88613   2.84470   1.000 16.75945 ?  51  GLN   A HE21 1 
ATOM   674  H  HE22 . GLN   A 1 48  ? 7.75082  8.72871   3.46240   1.000 16.75945 ?  51  GLN   A HE22 1 
ATOM   675  N  N    . ASN   A 1 49  ? 11.68635 11.19449  4.72494   1.000 13.22454 ?  52  ASN   A N    1 
ATOM   676  C  CA   . ASN   A 1 49  ? 11.45627 12.32004  5.64315   1.000 13.89597 ?  52  ASN   A CA   1 
ATOM   677  C  C    . ASN   A 1 49  ? 9.96134  12.62707  5.59411   1.000 14.57975 ?  52  ASN   A C    1 
ATOM   678  O  O    . ASN   A 1 49  ? 9.47907  13.34434  4.72169   1.000 15.96050 ?  52  ASN   A O    1 
ATOM   679  C  CB   . ASN   A 1 49  ? 12.30215 13.51842  5.23353   1.000 14.60881 ?  52  ASN   A CB   1 
ATOM   680  C  CG   . ASN   A 1 49  ? 12.17722 14.67388  6.18193   1.000 14.97444 ?  52  ASN   A CG   1 
ATOM   681  O  OD1  . ASN   A 1 49  ? 11.33851 14.65907  7.07105   1.000 16.87403 ?  52  ASN   A OD1  1 
ATOM   682  N  ND2  . ASN   A 1 49  ? 13.01752 15.69563  6.00505   1.000 16.37131 ?  52  ASN   A ND2  1 
ATOM   683  H  H    . ASN   A 1 49  ? 11.78154 11.43760  3.90552   1.000 15.86944 ?  52  ASN   A H    1 
ATOM   684  H  HA   . ASN   A 1 49  ? 11.69712 12.07456  6.55014   1.000 16.67516 ?  52  ASN   A HA   1 
ATOM   685  H  HB2  . ASN   A 1 49  ? 13.23454 13.25221  5.20753   1.000 17.53057 ?  52  ASN   A HB2  1 
ATOM   686  H  HB3  . ASN   A 1 49  ? 12.01852 13.81954  4.35616   1.000 17.53057 ?  52  ASN   A HB3  1 
ATOM   687  H  HD21 . ASN   A 1 49  ? 13.59640 15.67122  5.36952   1.000 19.64557 ?  52  ASN   A HD21 1 
ATOM   688  H  HD22 . ASN   A 1 49  ? 12.98009 16.37840  6.52660   1.000 19.64557 ?  52  ASN   A HD22 1 
ATOM   689  N  N    . GLY   A 1 50  ? 9.21871  12.00750  6.49366   1.000 14.99375 ?  53  GLY   A N    1 
ATOM   690  C  CA   . GLY   A 1 50  ? 7.77703  12.13524  6.55512   1.000 15.86718 ?  53  GLY   A CA   1 
ATOM   691  C  C    . GLY   A 1 50  ? 7.06419  11.16590  5.62853   1.000 15.50716 ?  53  GLY   A C    1 
ATOM   692  O  O    . GLY   A 1 50  ? 7.65894  10.33229  4.93431   1.000 14.59363 ?  53  GLY   A O    1 
ATOM   693  H  H    . GLY   A 1 50  ? 9.53761  11.48887  7.10105   1.000 17.99250 ?  53  GLY   A H    1 
ATOM   694  H  HA2  . GLY   A 1 50  ? 7.47907  11.96453  7.46230   1.000 19.04062 ?  53  GLY   A HA2  1 
ATOM   695  H  HA3  . GLY   A 1 50  ? 7.52480  13.03770  6.30442   1.000 19.04062 ?  53  GLY   A HA3  1 
ATOM   696  N  N    . SER   A 1 51  ? 5.73916  11.29769  5.62420   1.000 16.95758 ?  54  SER   A N    1 
ATOM   697  C  CA   . SER   A 1 51  ? 4.83688  10.39165  4.92383   1.000 18.41227 ?  54  SER   A CA   1 
ATOM   698  C  C    . SER   A 1 51  ? 3.92148  11.13403  3.96100   1.000 18.72176 ?  54  SER   A C    1 
ATOM   699  O  O    . SER   A 1 51  ? 2.95422  10.55051  3.45868   1.000 20.53977 ?  54  SER   A O    1 
ATOM   700  C  CB   . SER   A 1 51  ? 3.99370  9.58977   5.92666   1.000 19.89377 ?  54  SER   A CB   1 
ATOM   701  O  OG   . SER   A 1 51  ? 3.20779  10.44729  6.72306   1.000 22.17085 ?  54  SER   A OG   1 
ATOM   702  H  H    . SER   A 1 51  ? 5.32463  11.92875  6.03594   1.000 20.34910 ?  54  SER   A H    1 
ATOM   703  H  HA   . SER   A 1 51  ? 5.36701  9.75992   4.41316   1.000 22.09472 ?  54  SER   A HA   1 
ATOM   704  H  HB2  . SER   A 1 51  ? 3.40918  8.98928   5.43814   1.000 23.87252 ?  54  SER   A HB2  1 
ATOM   705  H  HB3  . SER   A 1 51  ? 4.58664  9.08090   6.50143   1.000 23.87252 ?  54  SER   A HB3  1 
ATOM   706  H  HG   . SER   A 1 51  ? 2.74298  9.99657   7.25823   1.000 26.60502 ?  54  SER   A HG   1 
ATOM   707  N  N    . SER   A 1 52  ? 4.19728  12.40138  3.68820   1.000 17.99178 ?  55  SER   A N    1 
ATOM   708  C  CA   . SER   A 1 52  ? 3.34714  13.15374  2.78199   1.000 20.06821 ?  55  SER   A CA   1 
ATOM   709  C  C    . SER   A 1 52  ? 3.31508  12.49348  1.41098   1.000 19.16870 ?  55  SER   A C    1 
ATOM   710  O  O    . SER   A 1 52  ? 4.34237  12.04629  0.88584   1.000 17.95993 ?  55  SER   A O    1 
ATOM   711  C  CB   . SER   A 1 52  ? 3.85940  14.58561  2.63940   1.000 22.91739 ?  55  SER   A CB   1 
ATOM   712  O  OG   . SER   A 1 52  ? 2.97668  15.34243  1.82981   1.000 27.11443 ?  55  SER   A OG   1 
ATOM   713  H  H    . SER   A 1 52  ? 4.86155  12.84241  4.01044   1.000 21.59014 ?  55  SER   A H    1 
ATOM   714  H  HA   . SER   A 1 52  ? 2.44661  13.17935  3.14157   1.000 24.08186 ?  55  SER   A HA   1 
ATOM   715  H  HB2  . SER   A 1 52  ? 3.91406  14.99315  3.51793   1.000 27.50087 ?  55  SER   A HB2  1 
ATOM   716  H  HB3  . SER   A 1 52  ? 4.73661  14.57019  2.22567   1.000 27.50087 ?  55  SER   A HB3  1 
ATOM   717  H  HG   . SER   A 1 52  ? 3.29256  16.10988  1.70003   1.000 32.53731 ?  55  SER   A HG   1 
ATOM   718  N  N    . MET   A 1 53  ? 2.12086  12.44866  0.83297   1.000 20.87764 ?  56  MET   A N    1 
ATOM   719  C  CA   . MET   A 1 53  ? 1.93440  12.03166  -0.54778  1.000 21.04312 ?  56  MET   A CA   1 
ATOM   720  C  C    . MET   A 1 53  ? 1.81770  13.21045  -1.49357  1.000 22.90612 ?  56  MET   A C    1 
ATOM   721  O  O    . MET   A 1 53  ? 2.17518  13.08904  -2.66343  1.000 23.88494 ?  56  MET   A O    1 
ATOM   722  C  CB   . MET   A 1 53  ? 0.70935  11.11545  -0.65175  1.000 24.23174 ?  56  MET   A CB   1 
ATOM   723  C  CG   . MET   A 1 53  ? 0.96396  9.76909   0.02238   1.000 28.34282 ?  56  MET   A CG   1 
ATOM   724  S  SD   . MET   A 1 53  ? -0.39434 8.60976   -0.15046  1.000 34.69283 ?  56  MET   A SD   1 
ATOM   725  C  CE   . MET   A 1 53  ? -1.63965 9.39075   0.87121   1.000 36.21668 ?  56  MET   A CE   1 
ATOM   726  H  H    . MET   A 1 53  ? 1.38759  12.65990  1.22956   1.000 25.05317 ?  56  MET   A H    1 
ATOM   727  H  HA   . MET   A 1 53  ? 2.69088  11.49951  -0.84008  1.000 25.25175 ?  56  MET   A HA   1 
ATOM   728  N  N    . LYS   A 1 54  ? 1.37860  14.36322  -0.99444  1.000 24.41496 ?  57  LYS   A N    1 
ATOM   729  C  CA   . LYS   A 1 54  ? 1.21477  15.56514  -1.80678  1.000 25.64167 ?  57  LYS   A CA   1 
ATOM   730  C  C    . LYS   A 1 54  ? 1.62985  16.74349  -0.93512  1.000 28.23967 ?  57  LYS   A C    1 
ATOM   731  O  O    . LYS   A 1 54  ? 0.89666  17.11720  -0.00719  1.000 31.80882 ?  57  LYS   A O    1 
ATOM   732  C  CB   . LYS   A 1 54  ? -0.24320 15.68222  -2.24094  1.000 27.48076 ?  57  LYS   A CB   1 
ATOM   733  C  CG   . LYS   A 1 54  ? -0.52457 16.79417  -3.21009  1.000 27.69104 ?  57  LYS   A CG   1 
ATOM   734  C  CD   . LYS   A 1 54  ? -2.01034 16.89645  -3.49979  1.000 28.39990 ?  57  LYS   A CD   1 
ATOM   735  C  CE   . LYS   A 1 54  ? -2.54681 15.67207  -4.21036  1.000 29.81903 ?  57  LYS   A CE   1 
ATOM   736  N  NZ   . LYS   A 1 54  ? -1.98474 15.56027  -5.56891  1.000 30.96010 ?  57  LYS   A NZ   1 
ATOM   737  H  H    . LYS   A 1 54  ? 1.16429  14.47636  -0.16929  1.000 29.29795 ?  57  LYS   A H    1 
ATOM   738  H  HA   . LYS   A 1 54  ? 1.77767  15.55018  -2.59660  1.000 30.77000 ?  57  LYS   A HA   1 
ATOM   739  H  HB2  . LYS   A 1 54  ? -0.50519 14.85097  -2.66670  1.000 32.97691 ?  57  LYS   A HB2  1 
ATOM   740  H  HB3  . LYS   A 1 54  ? -0.78738 15.83733  -1.45309  1.000 32.97691 ?  57  LYS   A HB3  1 
ATOM   741  H  HG2  . LYS   A 1 54  ? -0.22643 17.63620  -2.83195  1.000 33.22925 ?  57  LYS   A HG2  1 
ATOM   742  H  HG3  . LYS   A 1 54  ? -0.05993 16.62195  -4.04397  1.000 33.22925 ?  57  LYS   A HG3  1 
ATOM   743  H  HD2  . LYS   A 1 54  ? -2.49118 16.99335  -2.66295  1.000 34.07987 ?  57  LYS   A HD2  1 
ATOM   744  H  HD3  . LYS   A 1 54  ? -2.17119 17.66742  -4.06603  1.000 34.07987 ?  57  LYS   A HD3  1 
ATOM   745  H  HE2  . LYS   A 1 54  ? -2.30393 14.87664  -3.71116  1.000 35.78284 ?  57  LYS   A HE2  1 
ATOM   746  H  HE3  . LYS   A 1 54  ? -3.51199 15.73711  -4.28178  1.000 35.78284 ?  57  LYS   A HE3  1 
ATOM   747  H  HZ1  . LYS   A 1 54  ? -2.28492 14.82069  -5.96261  1.000 37.15212 ?  57  LYS   A HZ1  1 
ATOM   748  H  HZ2  . LYS   A 1 54  ? -2.22488 16.26495  -6.05662  1.000 37.15212 ?  57  LYS   A HZ2  1 
ATOM   749  H  HZ3  . LYS   A 1 54  ? -1.09630 15.52594  -5.52888  1.000 37.15212 ?  57  LYS   A HZ3  1 
ATOM   750  N  N    . PRO   A 1 55  ? 2.83627  17.30386  -1.14259  1.000 29.44129 ?  58  PRO   A N    1 
ATOM   751  C  CA   . PRO   A 1 55  ? 3.88614  16.88222  -2.08375  1.000 28.09483 ?  58  PRO   A CA   1 
ATOM   752  C  C    . PRO   A 1 55  ? 4.54371  15.60979  -1.58477  1.000 24.60188 ?  58  PRO   A C    1 
ATOM   753  O  O    . PRO   A 1 55  ? 4.48592  15.28872  -0.40278  1.000 25.91630 ?  58  PRO   A O    1 
ATOM   754  C  CB   . PRO   A 1 55  ? 4.85874  18.06672  -2.05964  1.000 31.57716 ?  58  PRO   A CB   1 
ATOM   755  C  CG   . PRO   A 1 55  ? 4.77341  18.55613  -0.63869  1.000 32.39140 ?  58  PRO   A CG   1 
ATOM   756  C  CD   . PRO   A 1 55  ? 3.32094  18.36862  -0.24019  1.000 31.80718 ?  58  PRO   A CD   1 
ATOM   757  H  HA   . PRO   A 1 55  ? 3.54304  16.77156  -2.98428  1.000 33.71380 ?  58  PRO   A HA   1 
ATOM   758  H  HB2  . PRO   A 1 55  ? 5.75612  17.77020  -2.27803  1.000 37.89259 ?  58  PRO   A HB2  1 
ATOM   759  H  HB3  . PRO   A 1 55  ? 4.57329  18.74976  -2.68644  1.000 37.89259 ?  58  PRO   A HB3  1 
ATOM   760  H  HG2  . PRO   A 1 55  ? 5.35854  18.02873  -0.07268  1.000 38.86969 ?  58  PRO   A HG2  1 
ATOM   761  H  HG3  . PRO   A 1 55  ? 5.02595  19.49173  -0.59654  1.000 38.86969 ?  58  PRO   A HG3  1 
ATOM   762  H  HD2  . PRO   A 1 55  ? 3.25341  18.08928  0.68626   1.000 38.16862 ?  58  PRO   A HD2  1 
ATOM   763  H  HD3  . PRO   A 1 55  ? 2.81986  19.18781  -0.37707  1.000 38.16862 ?  58  PRO   A HD3  1 
ATOM   764  N  N    . ARG   A 1 56  ? 5.18892  14.86767  -2.46649  1.000 21.20809 ?  59  ARG   A N    1 
ATOM   765  C  CA   . ARG   A 1 56  ? 5.73561  13.58564  -2.06124  1.000 19.12252 ?  59  ARG   A CA   1 
ATOM   766  C  C    . ARG   A 1 56  ? 6.94092  13.75861  -1.14765  1.000 16.54856 ?  59  ARG   A C    1 
ATOM   767  O  O    . ARG   A 1 56  ? 7.87656  14.50745  -1.46040  1.000 16.98347 ?  59  ARG   A O    1 
ATOM   768  C  CB   . ARG   A 1 56  ? 6.15268  12.80628  -3.28152  1.000 20.58515 ?  59  ARG   A CB   1 
ATOM   769  C  CG   . ARG   A 1 56  ? 6.62090  11.47480  -2.91987  1.000 21.23802 ?  59  ARG   A CG   1 
ATOM   770  C  CD   . ARG   A 1 56  ? 6.71336  10.68840  -4.11107  1.000 22.98089 ?  59  ARG   A CD   1 
ATOM   771  N  NE   . ARG   A 1 56  ? 7.34515  9.42486   -3.81933  1.000 23.17471 ?  59  ARG   A NE   1 
ATOM   772  C  CZ   . ARG   A 1 56  ? 7.57222  8.49952   -4.73326  1.000 24.66555 ?  59  ARG   A CZ   1 
ATOM   773  N  NH1  . ARG   A 1 56  ? 7.20926  8.66353   -5.99212  1.000 27.28391 ?  59  ARG   A NH1  1 
ATOM   774  N  NH2  . ARG   A 1 56  ? 8.19955  7.39781   -4.38551  1.000 23.87907 ?  59  ARG   A NH2  1 
ATOM   775  H  H    . ARG   A 1 56  ? 5.32177  15.07854  -3.28958  1.000 25.44970 ?  59  ARG   A H    1 
ATOM   776  H  HA   . ARG   A 1 56  ? 5.05305  13.09856  -1.57362  1.000 22.94703 ?  59  ARG   A HA   1 
ATOM   777  H  HB2  . ARG   A 1 56  ? 5.39414  12.71343  -3.87893  1.000 24.70218 ?  59  ARG   A HB2  1 
ATOM   778  H  HB3  . ARG   A 1 56  ? 6.87381  13.27391  -3.73116  1.000 24.70218 ?  59  ARG   A HB3  1 
ATOM   779  H  HG2  . ARG   A 1 56  ? 7.49707  11.53072  -2.50744  1.000 25.48563 ?  59  ARG   A HG2  1 
ATOM   780  H  HG3  . ARG   A 1 56  ? 5.99349  11.05549  -2.31042  1.000 25.48563 ?  59  ARG   A HG3  1 
ATOM   781  H  HD2  . ARG   A 1 56  ? 5.82459  10.51889  -4.46071  1.000 27.57707 ?  59  ARG   A HD2  1 
ATOM   782  H  HD3  . ARG   A 1 56  ? 7.24598  11.15770  -4.77211  1.000 27.57707 ?  59  ARG   A HD3  1 
ATOM   783  H  HE   . ARG   A 1 56  ? 7.58608  9.26629   -3.00914  1.000 27.80966 ?  59  ARG   A HE   1 
ATOM   784  H  HH11 . ARG   A 1 56  ? 6.81398  9.38772   -6.23481  1.000 32.74069 ?  59  ARG   A HH11 1 
ATOM   785  H  HH12 . ARG   A 1 56  ? 7.36814  8.04616   -6.56937  1.000 32.74069 ?  59  ARG   A HH12 1 
ATOM   786  H  HH21 . ARG   A 1 56  ? 8.45596  7.28747   -3.57207  1.000 28.65488 ?  59  ARG   A HH21 1 
ATOM   787  H  HH22 . ARG   A 1 56  ? 8.35353  6.78743   -4.97146  1.000 28.65488 ?  59  ARG   A HH22 1 
ATOM   788  N  N    . ALA   A 1 57  ? 6.92315  13.02629  -0.03164  1.000 15.27983 ?  60  ALA   A N    1 
ATOM   789  C  CA   . ALA   A 1 57  ? 8.00197  13.07723  0.95055   1.000 14.78446 ?  60  ALA   A CA   1 
ATOM   790  C  C    . ALA   A 1 57  ? 9.35686  12.78271  0.31686   1.000 14.08937 ?  60  ALA   A C    1 
ATOM   791  O  O    . ALA   A 1 57  ? 9.49930  11.86545  -0.50077  1.000 14.26416 ?  60  ALA   A O    1 
ATOM   792  C  CB   . ALA   A 1 57  ? 7.74054  12.02826  2.03224   1.000 16.30503 ?  60  ALA   A CB   1 
ATOM   793  H  H    . ALA   A 1 57  ? 6.28908  12.48575  0.18138   1.000 18.33579 ?  60  ALA   A H    1 
ATOM   794  H  HA   . ALA   A 1 57  ? 8.03002  13.96701  1.33579   1.000 17.74135 ?  60  ALA   A HA   1 
ATOM   795  H  HB1  . ALA   A 1 57  ? 8.45375  12.06688  2.68855   1.000 19.56604 ?  60  ALA   A HB1  1 
ATOM   796  H  HB2  . ALA   A 1 57  ? 6.88943  12.21807  2.45709   1.000 19.56604 ?  60  ALA   A HB2  1 
ATOM   797  H  HB3  . ALA   A 1 57  ? 7.71646  11.14999  1.62120   1.000 19.56604 ?  60  ALA   A HB3  1 
ATOM   798  N  N    . ASP   A 1 58  ? 10.37867 13.51197  0.76785   1.000 13.93036 ?  61  ASP   A N    1 
ATOM   799  C  CA   . ASP   A 1 58  ? 11.73578 13.18331  0.37000   1.000 13.50802 ?  61  ASP   A CA   1 
ATOM   800  C  C    . ASP   A 1 58  ? 12.05447 11.74413  0.73911   1.000 12.36171 ?  61  ASP   A C    1 
ATOM   801  O  O    . ASP   A 1 58  ? 11.66095 11.24915  1.80474   1.000 13.24008 ?  61  ASP   A O    1 
ATOM   802  C  CB   . ASP   A 1 58  ? 12.75342 14.07861  1.08341   1.000 14.04810 ?  61  ASP   A CB   1 
ATOM   803  C  CG   . ASP   A 1 58  ? 12.72965 15.53986  0.64106   1.000 15.98790 ?  61  ASP   A CG   1 
ATOM   804  O  OD1  . ASP   A 1 58  ? 12.04074 15.90059  -0.32822  1.000 16.90460 ?  61  ASP   A OD1  1 
ATOM   805  O  OD2  . ASP   A 1 58  ? 13.40602 16.34225  1.32284   1.000 18.48809 ?  61  ASP   A OD2  1 
ATOM   806  H  H    . ASP   A 1 58  ? 10.30893 14.18801  1.29482   1.000 16.71643 ?  61  ASP   A H    1 
ATOM   807  H  HA   . ASP   A 1 58  ? 11.80993 13.31588  -0.58803  1.000 16.20962 ?  61  ASP   A HA   1 
ATOM   808  H  HB2  . ASP   A 1 58  ? 12.56978 14.05809  2.03565   1.000 16.85772 ?  61  ASP   A HB2  1 
ATOM   809  H  HB3  . ASP   A 1 58  ? 13.64362 13.73470  0.90972   1.000 16.85772 ?  61  ASP   A HB3  1 
ATOM   810  N  N    . VAL   A 1 59  ? 12.84025 11.10979  -0.11827  1.000 12.38130 ?  62  VAL   A N    1 
ATOM   811  C  CA   . VAL   A 1 59  ? 13.31930 9.75741   0.10207   1.000 12.29694 ?  62  VAL   A CA   1 
ATOM   812  C  C    . VAL   A 1 59  ? 14.83624 9.84243   0.21017   1.000 11.98755 ?  62  VAL   A C    1 
ATOM   813  O  O    . VAL   A 1 59  ? 15.54401 10.03517  -0.78452  1.000 12.36256 ?  62  VAL   A O    1 
ATOM   814  C  CB   . VAL   A 1 59  ? 12.88281 8.79234   -1.00928  1.000 12.73077 ?  62  VAL   A CB   1 
ATOM   815  C  CG1  . VAL   A 1 59  ? 13.40407 7.40390   -0.69453  1.000 12.41999 ?  62  VAL   A CG1  1 
ATOM   816  C  CG2  . VAL   A 1 59  ? 11.35664 8.78630   -1.19716  1.000 13.42703 ?  62  VAL   A CG2  1 
ATOM   817  H  H    . VAL   A 1 59  ? 13.11656 11.45408  -0.85632  1.000 14.85756 ?  62  VAL   A H    1 
ATOM   818  H  HA   . VAL   A 1 59  ? 12.96734 9.41691   0.93937   1.000 14.75633 ?  62  VAL   A HA   1 
ATOM   819  H  HB   . VAL   A 1 59  ? 13.25830 9.08948   -1.85285  1.000 15.27693 ?  62  VAL   A HB   1 
ATOM   820  H  HG11 . VAL   A 1 59  ? 13.05929 6.78040   -1.35277  1.000 14.90398 ?  62  VAL   A HG11 1 
ATOM   821  H  HG12 . VAL   A 1 59  ? 14.37348 7.41584   -0.72616  1.000 14.90398 ?  62  VAL   A HG12 1 
ATOM   822  H  HG13 . VAL   A 1 59  ? 13.10517 7.14782   0.19203   1.000 14.90398 ?  62  VAL   A HG13 1 
ATOM   823  H  HG21 . VAL   A 1 59  ? 11.13347 8.21767   -1.95065  1.000 16.11244 ?  62  VAL   A HG21 1 
ATOM   824  H  HG22 . VAL   A 1 59  ? 10.94048 8.44473   -0.39030  1.000 16.11244 ?  62  VAL   A HG22 1 
ATOM   825  H  HG23 . VAL   A 1 59  ? 11.05569 9.69279   -1.36630  1.000 16.11244 ?  62  VAL   A HG23 1 
ATOM   826  N  N    . ALA   A 1 60  ? 15.34346 9.70400   1.43054   1.000 12.14695 ?  63  ALA   A N    1 
ATOM   827  C  CA   . ALA   A 1 60  ? 16.78414 9.70599   1.63275   1.000 12.11913 ?  63  ALA   A CA   1 
ATOM   828  C  C    . ALA   A 1 60  ? 17.44919 8.52109   0.94915   1.000 12.01004 ?  63  ALA   A C    1 
ATOM   829  O  O    . ALA   A 1 60  ? 18.53536 8.65307   0.36410   1.000 12.68514 ?  63  ALA   A O    1 
ATOM   830  C  CB   . ALA   A 1 60  ? 17.08350 9.67405   3.13250   1.000 12.81851 ?  63  ALA   A CB   1 
ATOM   831  H  H    . ALA   A 1 60  ? 14.88044 9.60850   2.14894   1.000 14.57634 ?  63  ALA   A H    1 
ATOM   832  H  HA   . ALA   A 1 60  ? 17.15181 10.51779  1.24974   1.000 14.54295 ?  63  ALA   A HA   1 
ATOM   833  H  HB1  . ALA   A 1 60  ? 18.04245 9.73632   3.26452   1.000 15.38221 ?  63  ALA   A HB1  1 
ATOM   834  H  HB2  . ALA   A 1 60  ? 16.64147 10.42489  3.55883   1.000 15.38221 ?  63  ALA   A HB2  1 
ATOM   835  H  HB3  . ALA   A 1 60  ? 16.75198 8.84117   3.50304   1.000 15.38221 ?  63  ALA   A HB3  1 
ATOM   836  N  N    . PHE   A 1 61  ? 16.81556 7.35596   1.02367   1.000 11.44786 ?  64  PHE   A N    1 
ATOM   837  C  CA   . PHE   A 1 61  ? 17.37438 6.13136   0.47024   1.000 11.25515 ?  64  PHE   A CA   1 
ATOM   838  C  C    . PHE   A 1 61  ? 16.23109 5.33811   -0.12044  1.000 10.60911 ?  64  PHE   A C    1 
ATOM   839  O  O    . PHE   A 1 61  ? 15.35961 4.86414   0.60500   1.000 11.16969 ?  64  PHE   A O    1 
ATOM   840  C  CB   . PHE   A 1 61  ? 18.11600 5.34134   1.55099   1.000 12.18330 ?  64  PHE   A CB   1 
ATOM   841  C  CG   . PHE   A 1 61  ? 18.76826 4.06367   1.08004   1.000 12.38669 ?  64  PHE   A CG   1 
ATOM   842  C  CD1  . PHE   A 1 61  ? 19.40256 3.95710   -0.13235  1.000 12.80119 ?  64  PHE   A CD1  1 
ATOM   843  C  CD2  . PHE   A 1 61  ? 18.81650 2.97476   1.92452   1.000 15.36976 ?  64  PHE   A CD2  1 
ATOM   844  C  CE1  . PHE   A 1 61  ? 20.01561 2.78098   -0.50952  1.000 12.78134 ?  64  PHE   A CE1  1 
ATOM   845  C  CE2  . PHE   A 1 61  ? 19.44672 1.81698   1.55667   1.000 16.29247 ?  64  PHE   A CE2  1 
ATOM   846  C  CZ   . PHE   A 1 61  ? 20.05042 1.70766   0.34702   1.000 13.66269 ?  64  PHE   A CZ   1 
ATOM   847  H  H    . PHE   A 1 61  ? 16.04797 7.24885   1.39640   1.000 13.73744 ?  64  PHE   A H    1 
ATOM   848  H  HA   . PHE   A 1 61  ? 18.00231 6.33218   -0.24130  1.000 13.50619 ?  64  PHE   A HA   1 
ATOM   849  H  HB2  . PHE   A 1 61  ? 18.81478 5.90548   1.91753   1.000 14.61996 ?  64  PHE   A HB2  1 
ATOM   850  H  HB3  . PHE   A 1 61  ? 17.48236 5.10416   2.24608   1.000 14.61996 ?  64  PHE   A HB3  1 
ATOM   851  H  HD1  . PHE   A 1 61  ? 19.41913 4.68794   -0.70724  1.000 15.36143 ?  64  PHE   A HD1  1 
ATOM   852  H  HD2  . PHE   A 1 61  ? 18.41278 3.02814   2.76062   1.000 18.44371 ?  64  PHE   A HD2  1 
ATOM   853  H  HE1  . PHE   A 1 61  ? 20.40834 2.71393   -1.34985  1.000 15.33761 ?  64  PHE   A HE1  1 
ATOM   854  H  HE2  . PHE   A 1 61  ? 19.46122 1.09583   2.14372   1.000 19.55097 ?  64  PHE   A HE2  1 
ATOM   855  H  HZ   . PHE   A 1 61  ? 20.48021 0.92019   0.10191   1.000 16.39523 ?  64  PHE   A HZ   1 
ATOM   856  N  N    . HIS   A 1 62  ? 16.23236 5.23707   -1.44827  1.000 10.89077 ?  65  HIS   A N    1 
ATOM   857  C  CA   . HIS   A 1 62  ? 15.31657 4.41892   -2.23714  1.000 10.56306 ?  65  HIS   A CA   1 
ATOM   858  C  C    . HIS   A 1 62  ? 16.11226 3.20784   -2.68615  1.000 11.46955 ?  65  HIS   A C    1 
ATOM   859  O  O    . HIS   A 1 62  ? 17.11015 3.36089   -3.39295  1.000 12.20217 ?  65  HIS   A O    1 
ATOM   860  C  CB   . HIS   A 1 62  ? 14.89172 5.25622   -3.44922  1.000 11.22983 ?  65  HIS   A CB   1 
ATOM   861  C  CG   . HIS   A 1 62  ? 14.09934 4.55448   -4.52087  1.000 11.42835 ?  65  HIS   A CG   1 
ATOM   862  N  ND1  . HIS   A 1 62  ? 12.79892 4.14037   -4.36361  1.000 12.18702 ?  65  HIS   A ND1  1 
ATOM   863  C  CD2  . HIS   A 1 62  ? 14.40479 4.33032   -5.82873  1.000 11.91216 ?  65  HIS   A CD2  1 
ATOM   864  C  CE1  . HIS   A 1 62  ? 12.34316 3.67921   -5.52412  1.000 11.91032 ?  65  HIS   A CE1  1 
ATOM   865  N  NE2  . HIS   A 1 62  ? 13.29721 3.79168   -6.43303  1.000 12.58584 ?  65  HIS   A NE2  1 
ATOM   866  H  H    . HIS   A 1 62  ? 16.79112 5.66100   -1.94594  1.000 13.06892 ?  65  HIS   A H    1 
ATOM   867  H  HA   . HIS   A 1 62  ? 14.53438 4.12662   -1.74355  1.000 12.67567 ?  65  HIS   A HA   1 
ATOM   868  H  HB2  . HIS   A 1 62  ? 14.34461 5.99036   -3.12888  1.000 13.47579 ?  65  HIS   A HB2  1 
ATOM   869  H  HB3  . HIS   A 1 62  ? 15.69437 5.60028   -3.87146  1.000 13.47579 ?  65  HIS   A HB3  1 
ATOM   870  H  HD1  . HIS   A 1 62  ? 12.35066 4.17412   -3.63045  1.000 14.62443 ?  65  HIS   A HD1  1 
ATOM   871  H  HD2  . HIS   A 1 62  ? 15.21955 4.51037   -6.23940  1.000 14.29460 ?  65  HIS   A HD2  1 
ATOM   872  H  HE1  . HIS   A 1 62  ? 11.49248 3.33395   -5.67257  1.000 14.29238 ?  65  HIS   A HE1  1 
ATOM   873  N  N    . PHE   A 1 63  ? 15.68189 2.02350   -2.25469  1.000 10.91408 ?  66  PHE   A N    1 
ATOM   874  C  CA   . PHE   A 1 63  ? 16.32334 0.74254   -2.54984  1.000 11.04038 ?  66  PHE   A CA   1 
ATOM   875  C  C    . PHE   A 1 63  ? 15.31622 -0.05897  -3.37131  1.000 11.12815 ?  66  PHE   A C    1 
ATOM   876  O  O    . PHE   A 1 63  ? 14.27669 -0.45998  -2.84709  1.000 11.28536 ?  66  PHE   A O    1 
ATOM   877  C  CB   . PHE   A 1 63  ? 16.68795 0.07714   -1.22333  1.000 11.81586 ?  66  PHE   A CB   1 
ATOM   878  C  CG   . PHE   A 1 63  ? 17.25011 -1.31260  -1.35634  1.000 12.09906 ?  66  PHE   A CG   1 
ATOM   879  C  CD1  . PHE   A 1 63  ? 18.60579 -1.52402  -1.50021  1.000 12.58576 ?  66  PHE   A CD1  1 
ATOM   880  C  CD2  . PHE   A 1 63  ? 16.42207 -2.42183  -1.32221  1.000 12.32831 ?  66  PHE   A CD2  1 
ATOM   881  C  CE1  . PHE   A 1 63  ? 19.10927 -2.78816  -1.58777  1.000 13.36607 ?  66  PHE   A CE1  1 
ATOM   882  C  CE2  . PHE   A 1 63  ? 16.95162 -3.70813  -1.42801  1.000 13.93060 ?  66  PHE   A CE2  1 
ATOM   883  C  CZ   . PHE   A 1 63  ? 18.27471 -3.87262  -1.54812  1.000 13.62061 ?  66  PHE   A CZ   1 
ATOM   884  H  H    . PHE   A 1 63  ? 14.98249 1.93130   -1.76282  1.000 13.09689 ?  66  PHE   A H    1 
ATOM   885  H  HA   . PHE   A 1 63  ? 17.13130 0.82628   -3.08001  1.000 13.24845 ?  66  PHE   A HA   1 
ATOM   886  H  HB2  . PHE   A 1 63  ? 17.35550 0.62174   -0.77760  1.000 14.17903 ?  66  PHE   A HB2  1 
ATOM   887  H  HB3  . PHE   A 1 63  ? 15.88865 0.01875   -0.67688  1.000 14.17903 ?  66  PHE   A HB3  1 
ATOM   888  H  HD1  . PHE   A 1 63  ? 19.18302 -0.79581  -1.53791  1.000 15.10291 ?  66  PHE   A HD1  1 
ATOM   889  H  HD2  . PHE   A 1 63  ? 15.50387 -2.30825  -1.22783  1.000 14.79397 ?  66  PHE   A HD2  1 
ATOM   890  H  HE1  . PHE   A 1 63  ? 20.02649 -2.91461  -1.67507  1.000 16.03928 ?  66  PHE   A HE1  1 
ATOM   891  H  HE2  . PHE   A 1 63  ? 16.38813 -4.44787  -1.41516  1.000 16.71672 ?  66  PHE   A HE2  1 
ATOM   892  H  HZ   . PHE   A 1 63  ? 18.62970 -4.73031  -1.60508  1.000 16.34474 ?  66  PHE   A HZ   1 
ATOM   893  N  N    . ASN   A 1 64  ? 15.58250 -0.25885  -4.67515  1.000 11.53139 ?  67  ASN   A N    1 
ATOM   894  C  CA   . ASN   A 1 64  ? 14.54420 -0.64865  -5.64291  1.000 11.21950 ?  67  ASN   A CA   1 
ATOM   895  C  C    . ASN   A 1 64  ? 14.96265 -1.81523  -6.52417  1.000 12.20926 ?  67  ASN   A C    1 
ATOM   896  O  O    . ASN   A 1 64  ? 15.45942 -1.61820  -7.64630  1.000 12.77523 ?  67  ASN   A O    1 
ATOM   897  C  CB   . ASN   A 1 64  ? 14.24019 0.58073   -6.48788  1.000 11.58058 ?  67  ASN   A CB   1 
ATOM   898  C  CG   . ASN   A 1 64  ? 13.25959 0.36267   -7.62232  1.000 11.95266 ?  67  ASN   A CG   1 
ATOM   899  O  OD1  . ASN   A 1 64  ? 13.36363 1.05829   -8.63730  1.000 13.03899 ?  67  ASN   A OD1  1 
ATOM   900  N  ND2  . ASN   A 1 64  ? 12.29443 -0.51979  -7.46178  1.000 12.97093 ?  67  ASN   A ND2  1 
ATOM   901  H  H    . ASN   A 1 64  ? 16.36427 -0.17337  -5.02317  1.000 13.83767 ?  67  ASN   A H    1 
ATOM   902  H  HA   . ASN   A 1 64  ? 13.77100 -0.98064  -5.16037  1.000 13.46339 ?  67  ASN   A HA   1 
ATOM   903  H  HB2  . ASN   A 1 64  ? 13.86601 1.26419   -5.91016  1.000 13.89669 ?  67  ASN   A HB2  1 
ATOM   904  H  HB3  . ASN   A 1 64  ? 15.06981 0.89539   -6.87983  1.000 13.89669 ?  67  ASN   A HB3  1 
ATOM   905  H  HD21 . ASN   A 1 64  ? 12.23072 -0.95802  -6.72455  1.000 15.56512 ?  67  ASN   A HD21 1 
ATOM   906  H  HD22 . ASN   A 1 64  ? 11.72817 -0.65756  -8.09421  1.000 15.56512 ?  67  ASN   A HD22 1 
ATOM   907  N  N    . PRO   A 1 65  ? 14.75733 -3.05026  -6.05375  1.000 12.20683 ?  68  PRO   A N    1 
ATOM   908  C  CA   . PRO   A 1 65  ? 14.94458 -4.22006  -6.92940  1.000 12.92834 ?  68  PRO   A CA   1 
ATOM   909  C  C    . PRO   A 1 65  ? 13.95595 -4.20874  -8.08165  1.000 13.67408 ?  68  PRO   A C    1 
ATOM   910  O  O    . PRO   A 1 65  ? 12.76535 -3.97549  -7.89510  1.000 14.27624 ?  68  PRO   A O    1 
ATOM   911  C  CB   . PRO   A 1 65  ? 14.69620 -5.39794  -5.98005  1.000 13.33180 ?  68  PRO   A CB   1 
ATOM   912  C  CG   . PRO   A 1 65  ? 15.04961 -4.83131  -4.61130  1.000 12.85612 ?  68  PRO   A CG   1 
ATOM   913  C  CD   . PRO   A 1 65  ? 14.44750 -3.45374  -4.66492  1.000 12.72150 ?  68  PRO   A CD   1 
ATOM   914  H  HA   . PRO   A 1 65  ? 15.84882 -4.25805  -7.27842  1.000 15.51400 ?  68  PRO   A HA   1 
ATOM   915  H  HB2  . PRO   A 1 65  ? 13.76629 -5.67113  -6.01924  1.000 15.99816 ?  68  PRO   A HB2  1 
ATOM   916  H  HB3  . PRO   A 1 65  ? 15.27118 -6.14390  -6.21208  1.000 15.99816 ?  68  PRO   A HB3  1 
ATOM   917  H  HG2  . PRO   A 1 65  ? 14.65100 -5.36675  -3.90751  1.000 15.42734 ?  68  PRO   A HG2  1 
ATOM   918  H  HG3  . PRO   A 1 65  ? 16.01200 -4.79479  -4.49569  1.000 15.42734 ?  68  PRO   A HG3  1 
ATOM   919  H  HD2  . PRO   A 1 65  ? 13.49008 -3.48185  -4.51180  1.000 15.26580 ?  68  PRO   A HD2  1 
ATOM   920  H  HD3  . PRO   A 1 65  ? 14.86876 -2.86026  -4.02366  1.000 15.26580 ?  68  PRO   A HD3  1 
ATOM   921  N  N    . ARG   A 1 66  ? 14.47443 -4.49562  -9.28967  1.000 14.85489 ?  69  ARG   A N    1 
ATOM   922  C  CA   . ARG   A 1 66  ? 13.68516 -4.57037  -10.51278 1.000 15.23122 ?  69  ARG   A CA   1 
ATOM   923  C  C    . ARG   A 1 66  ? 13.97168 -5.91525  -11.14675 1.000 16.93652 ?  69  ARG   A C    1 
ATOM   924  O  O    . ARG   A 1 66  ? 15.11737 -6.36951  -11.14597 1.000 18.31687 ?  69  ARG   A O    1 
ATOM   925  C  CB   . ARG   A 1 66  ? 14.06496 -3.44710  -11.49154 1.000 15.43411 ?  69  ARG   A CB   1 
ATOM   926  C  CG   . ARG   A 1 66  ? 13.82603 -2.07547  -10.89935 1.000 15.92579 ?  69  ARG   A CG   1 
ATOM   927  C  CD   . ARG   A 1 66  ? 14.25206 -0.97829  -11.84735 1.000 15.42552 ?  69  ARG   A CD   1 
ATOM   928  N  NE   . ARG   A 1 66  ? 14.02684 0.31858   -11.23309 1.000 14.51390 ?  69  ARG   A NE   1 
ATOM   929  C  CZ   . ARG   A 1 66  ? 14.16516 1.47294   -11.86101 1.000 14.71408 ?  69  ARG   A CZ   1 
ATOM   930  N  NH1  . ARG   A 1 66  ? 14.55972 1.52469   -13.12128 1.000 16.27187 ?  69  ARG   A NH1  1 
ATOM   931  N  NH2  . ARG   A 1 66  ? 13.91078 2.59715   -11.20782 1.000 14.96051 ?  69  ARG   A NH2  1 
ATOM   932  H  H    . ARG   A 1 66  ? 15.30941 -4.65455  -9.42061  1.000 17.82587 ?  69  ARG   A H    1 
ATOM   933  H  HA   . ARG   A 1 66  ? 12.73799 -4.48683  -10.32100 1.000 18.27746 ?  69  ARG   A HA   1 
ATOM   934  H  HB2  . ARG   A 1 66  ? 15.00626 -3.52240  -11.71330 1.000 18.52093 ?  69  ARG   A HB2  1 
ATOM   935  H  HB3  . ARG   A 1 66  ? 13.52731 -3.52898  -12.29474 1.000 18.52093 ?  69  ARG   A HB3  1 
ATOM   936  H  HG2  . ARG   A 1 66  ? 12.88033 -1.96664  -10.71306 1.000 19.11095 ?  69  ARG   A HG2  1 
ATOM   937  H  HG3  . ARG   A 1 66  ? 14.33796 -1.98591  -10.08032 1.000 19.11095 ?  69  ARG   A HG3  1 
ATOM   938  H  HD2  . ARG   A 1 66  ? 15.19659 -1.06827  -12.04903 1.000 18.51062 ?  69  ARG   A HD2  1 
ATOM   939  H  HD3  . ARG   A 1 66  ? 13.73187 -1.03119  -12.66436 1.000 18.51062 ?  69  ARG   A HD3  1 
ATOM   940  H  HE   . ARG   A 1 66  ? 13.78797 0.33624   -10.40712 1.000 17.41668 ?  69  ARG   A HE   1 
ATOM   941  H  HH11 . ARG   A 1 66  ? 14.73178 0.79822   -13.54817 1.000 19.52624 ?  69  ARG   A HH11 1 
ATOM   942  H  HH12 . ARG   A 1 66  ? 14.64441 2.28484   -13.51448 1.000 19.52624 ?  69  ARG   A HH12 1 
ATOM   943  H  HH21 . ARG   A 1 66  ? 13.65924 2.56942   -10.38590 1.000 17.95261 ?  69  ARG   A HH21 1 
ATOM   944  H  HH22 . ARG   A 1 66  ? 13.99720 3.35464   -11.60573 1.000 17.95261 ?  69  ARG   A HH22 1 
ATOM   945  N  N    . PHE   A 1 67  ? 12.92978 -6.56476  -11.66290 1.000 16.61493 ?  70  PHE   A N    1 
ATOM   946  C  CA   . PHE   A 1 67  ? 13.03107 -7.96404  -12.07226 1.000 18.24927 ?  70  PHE   A CA   1 
ATOM   947  C  C    . PHE   A 1 67  ? 13.08464 -8.21615  -13.56967 1.000 20.37992 ?  70  PHE   A C    1 
ATOM   948  O  O    . PHE   A 1 67  ? 13.38917 -9.35166  -13.97168 1.000 21.98683 ?  70  PHE   A O    1 
ATOM   949  C  CB   . PHE   A 1 67  ? 11.90791 -8.77870  -11.41176 1.000 18.45004 ?  70  PHE   A CB   1 
ATOM   950  C  CG   . PHE   A 1 67  ? 12.03422 -8.74194  -9.93312  1.000 17.65826 ?  70  PHE   A CG   1 
ATOM   951  C  CD1  . PHE   A 1 67  ? 12.92103 -9.61475  -9.32188  1.000 19.03950 ?  70  PHE   A CD1  1 
ATOM   952  C  CD2  . PHE   A 1 67  ? 11.40450 -7.77670  -9.17879  1.000 18.93316 ?  70  PHE   A CD2  1 
ATOM   953  C  CE1  . PHE   A 1 67  ? 13.14230 -9.57484  -7.97838  1.000 19.57877 ?  70  PHE   A CE1  1 
ATOM   954  C  CE2  . PHE   A 1 67  ? 11.63107 -7.70133  -7.81883  1.000 19.17750 ?  70  PHE   A CE2  1 
ATOM   955  C  CZ   . PHE   A 1 67  ? 12.51990 -8.59567  -7.22964  1.000 19.19019 ?  70  PHE   A CZ   1 
ATOM   956  H  H    . PHE   A 1 67  ? 12.15321 -6.21635  -11.78600 1.000 19.93791 ?  70  PHE   A H    1 
ATOM   957  H  HA   . PHE   A 1 67  ? 13.87618 -8.31021  -11.74537 1.000 21.89912 ?  70  PHE   A HA   1 
ATOM   958  H  HB2  . PHE   A 1 67  ? 11.04797 -8.40348  -11.65797 1.000 22.14004 ?  70  PHE   A HB2  1 
ATOM   959  H  HB3  . PHE   A 1 67  ? 11.96288 -9.70204  -11.70384 1.000 22.14004 ?  70  PHE   A HB3  1 
ATOM   960  H  HD1  . PHE   A 1 67  ? 13.37418 -10.24038 -9.83972  1.000 22.84739 ?  70  PHE   A HD1  1 
ATOM   961  H  HD2  . PHE   A 1 67  ? 10.82519 -7.17416  -9.58654  1.000 22.71979 ?  70  PHE   A HD2  1 
ATOM   962  H  HE1  . PHE   A 1 67  ? 13.70275 -10.19618 -7.57251  1.000 23.49453 ?  70  PHE   A HE1  1 
ATOM   963  H  HE2  . PHE   A 1 67  ? 11.19551 -7.06142  -7.30337  1.000 23.01300 ?  70  PHE   A HE2  1 
ATOM   964  H  HZ   . PHE   A 1 67  ? 12.69713 -8.53295  -6.31884  1.000 23.02823 ?  70  PHE   A HZ   1 
ATOM   965  N  N    . LYS   A 1 68  ? 12.80936 -7.21589  -14.40473 1.000 20.20475 ?  71  LYS   A N    1 
ATOM   966  C  CA   . LYS   A 1 68  ? 12.82918 -7.42722  -15.84833 1.000 25.07222 ?  71  LYS   A CA   1 
ATOM   967  C  C    . LYS   A 1 68  ? 14.24488 -7.71568  -16.34342 1.000 26.43650 ?  71  LYS   A C    1 
ATOM   968  O  O    . LYS   A 1 68  ? 15.24996 -7.37512  -15.72294 1.000 24.99548 ?  71  LYS   A O    1 
ATOM   969  C  CB   . LYS   A 1 68  ? 12.21797 -6.21889  -16.56626 1.000 29.68391 ?  71  LYS   A CB   1 
ATOM   970  C  CG   . LYS   A 1 68  ? 10.69481 -6.13103  -16.35467 1.000 34.66231 ?  71  LYS   A CG   1 
ATOM   971  C  CD   . LYS   A 1 68  ? 10.11979 -4.72216  -16.55130 1.000 37.40753 ?  71  LYS   A CD   1 
ATOM   972  C  CE   . LYS   A 1 68  ? 8.65359  -4.66688  -16.10908 1.000 39.12387 ?  71  LYS   A CE   1 
ATOM   973  N  NZ   . LYS   A 1 68  ? 8.11313  -3.26849  -15.87913 1.000 38.75565 ?  71  LYS   A NZ   1 
ATOM   974  H  H    . LYS   A 1 68  ? 12.61048 -6.41492  -14.16288 1.000 24.24570 ?  71  LYS   A H    1 
ATOM   975  H  HA   . LYS   A 1 68  ? 12.29294 -8.20324  -16.07447 1.000 30.08667 ?  71  LYS   A HA   1 
ATOM   976  H  HB2  . LYS   A 1 68  ? 12.61974 -5.40642  -16.22076 1.000 35.62069 ?  71  LYS   A HB2  1 
ATOM   977  H  HB3  . LYS   A 1 68  ? 12.38828 -6.29438  -17.51821 1.000 35.62069 ?  71  LYS   A HB3  1 
ATOM   978  H  HG2  . LYS   A 1 68  ? 10.25709 -6.71915  -16.98982 1.000 41.59477 ?  71  LYS   A HG2  1 
ATOM   979  H  HG3  . LYS   A 1 68  ? 10.48907 -6.40935  -15.44852 1.000 41.59477 ?  71  LYS   A HG3  1 
ATOM   980  H  HD2  . LYS   A 1 68  ? 10.62595 -4.08839  -16.01929 1.000 44.88903 ?  71  LYS   A HD2  1 
ATOM   981  H  HD3  . LYS   A 1 68  ? 10.16772 -4.48061  -17.48952 1.000 44.88903 ?  71  LYS   A HD3  1 
ATOM   982  H  HE2  . LYS   A 1 68  ? 8.10804  -5.08082  -16.79604 1.000 46.94865 ?  71  LYS   A HE2  1 
ATOM   983  H  HE3  . LYS   A 1 68  ? 8.56388  -5.15468  -15.27546 1.000 46.94865 ?  71  LYS   A HE3  1 
ATOM   984  H  HZ1  . LYS   A 1 68  ? 7.26408  -3.30983  -15.61550 1.000 46.50679 ?  71  LYS   A HZ1  1 
ATOM   985  H  HZ2  . LYS   A 1 68  ? 8.59088  -2.85697  -15.25103 1.000 46.50679 ?  71  LYS   A HZ2  1 
ATOM   986  H  HZ3  . LYS   A 1 68  ? 8.15904  -2.79673  -16.63241 1.000 46.50679 ?  71  LYS   A HZ3  1 
ATOM   987  N  N    . ARG   A 1 69  ? 14.31568 -8.37407  -17.48836 1.000 30.20787 ?  72  ARG   A N    1 
ATOM   988  C  CA   . ARG   A 1 69  ? 15.60370 -8.73585  -18.10358 1.000 34.80048 ?  72  ARG   A CA   1 
ATOM   989  C  C    . ARG   A 1 69  ? 16.39119 -9.56886  -17.09128 1.000 33.69214 ?  72  ARG   A C    1 
ATOM   990  O  O    . ARG   A 1 69  ? 15.84151 -10.51019 -16.49728 1.000 34.83822 ?  72  ARG   A O    1 
ATOM   991  C  CB   . ARG   A 1 69  ? 16.30201 -7.47660  -18.61870 1.000 39.01900 ?  72  ARG   A CB   1 
ATOM   992  C  CG   . ARG   A 1 69  ? 15.52318 -6.68566  -19.65454 1.000 42.31028 ?  72  ARG   A CG   1 
ATOM   993  C  CD   . ARG   A 1 69  ? 16.12988 -5.30035  -19.86172 1.000 45.86217 ?  72  ARG   A CD   1 
ATOM   994  N  NE   . ARG   A 1 69  ? 15.28985 -4.47090  -20.72017 1.000 47.65261 ?  72  ARG   A NE   1 
ATOM   995  C  CZ   . ARG   A 1 69  ? 15.73458 -3.51801  -21.53098 1.000 48.72675 ?  72  ARG   A CZ   1 
ATOM   996  N  NH1  . ARG   A 1 69  ? 17.02879 -3.29254  -21.69650 1.000 49.01196 ?  72  ARG   A NH1  1 
ATOM   997  N  NH2  . ARG   A 1 69  ? 14.85757 -2.77670  -22.20237 1.000 48.86745 ?  72  ARG   A NH2  1 
ATOM   998  H  H    . ARG   A 1 69  ? 13.63001 -8.62940  -17.94031 1.000 36.24945 ?  72  ARG   A H    1 
ATOM   999  H  HA   . ARG   A 1 69  ? 15.42773 -9.31275  -18.86326 1.000 41.76058 ?  72  ARG   A HA   1 
ATOM   1000 H  HB2  . ARG   A 1 69  ? 16.46544 -6.88708  -17.86593 1.000 46.82281 ?  72  ARG   A HB2  1 
ATOM   1001 H  HB3  . ARG   A 1 69  ? 17.14348 -7.73716  -19.02483 1.000 46.82281 ?  72  ARG   A HB3  1 
ATOM   1002 H  HG2  . ARG   A 1 69  ? 15.54172 -7.15781  -20.50167 1.000 50.77234 ?  72  ARG   A HG2  1 
ATOM   1003 H  HG3  . ARG   A 1 69  ? 14.60692 -6.57697  -19.35529 1.000 50.77234 ?  72  ARG   A HG3  1 
ATOM   1004 H  HD2  . ARG   A 1 69  ? 16.21980 -4.85761  -19.00335 1.000 55.03460 ?  72  ARG   A HD2  1 
ATOM   1005 H  HD3  . ARG   A 1 69  ? 16.99978 -5.39034  -20.28133 1.000 55.03460 ?  72  ARG   A HD3  1 
ATOM   1006 H  HE   . ARG   A 1 69  ? 14.44145 -4.61009  -20.69920 1.000 57.18314 ?  72  ARG   A HE   1 
ATOM   1007 H  HH11 . ARG   A 1 69  ? 17.60592 -3.76928  -21.27313 1.000 58.81435 ?  72  ARG   A HH11 1 
ATOM   1008 H  HH12 . ARG   A 1 69  ? 17.29226 -2.66936  -22.22738 1.000 58.81435 ?  72  ARG   A HH12 1 
ATOM   1009 H  HH21 . ARG   A 1 69  ? 14.01440 -2.91750  -22.10838 1.000 58.64094 ?  72  ARG   A HH21 1 
ATOM   1010 H  HH22 . ARG   A 1 69  ? 15.13374 -2.15663  -22.73043 1.000 58.64094 ?  72  ARG   A HH22 1 
ATOM   1011 N  N    . ALA   A 1 70  ? 17.66619 -9.28850  -16.86160 1.000 32.63254 ?  73  ALA   A N    1 
ATOM   1012 C  CA   . ALA   A 1 70  ? 18.46125 -10.06355 -15.92160 1.000 30.12675 ?  73  ALA   A CA   1 
ATOM   1013 C  C    . ALA   A 1 70  ? 18.32347 -9.56979  -14.48661 1.000 26.57151 ?  73  ALA   A C    1 
ATOM   1014 O  O    . ALA   A 1 70  ? 18.99625 -10.10702 -13.59873 1.000 27.89913 ?  73  ALA   A O    1 
ATOM   1015 C  CB   . ALA   A 1 70  ? 19.93752 -10.00674 -16.32358 1.000 31.75021 ?  73  ALA   A CB   1 
ATOM   1016 H  H    . ALA   A 1 70  ? 18.09696 -8.64840  -17.24148 1.000 39.15905 ?  73  ALA   A H    1 
ATOM   1017 H  HA   . ALA   A 1 70  ? 18.16674 -10.98717 -15.95472 1.000 36.15209 ?  73  ALA   A HA   1 
ATOM   1018 H  HB1  . ALA   A 1 70  ? 20.43782 -10.63323 -15.77758 1.000 38.10025 ?  73  ALA   A HB1  1 
ATOM   1019 H  HB2  . ALA   A 1 70  ? 20.01922 -10.24560 -17.26015 1.000 38.10025 ?  73  ALA   A HB2  1 
ATOM   1020 H  HB3  . ALA   A 1 70  ? 20.26901 -9.10625  -16.18174 1.000 38.10025 ?  73  ALA   A HB3  1 
ATOM   1021 N  N    . GLY   A 1 71  ? 17.49910 -8.55627  -14.24151 1.000 23.25890 ?  74  GLY   A N    1 
ATOM   1022 C  CA   . GLY   A 1 71  ? 17.33457 -7.98602  -12.91835 1.000 20.99401 ?  74  GLY   A CA   1 
ATOM   1023 C  C    . GLY   A 1 71  ? 18.43495 -6.99530  -12.54316 1.000 19.80782 ?  74  GLY   A C    1 
ATOM   1024 O  O    . GLY   A 1 71  ? 19.54789 -7.03346  -13.02806 1.000 20.81541 ?  74  GLY   A O    1 
ATOM   1025 H  H    . GLY   A 1 71  ? 17.01467 -8.17552  -14.84147 1.000 27.91069 ?  74  GLY   A H    1 
ATOM   1026 H  HA2  . GLY   A 1 71  ? 16.48402 -7.52154  -12.87689 1.000 25.19282 ?  74  GLY   A HA2  1 
ATOM   1027 H  HA3  . GLY   A 1 71  ? 17.33634 -8.70083  -12.26266 1.000 25.19282 ?  74  GLY   A HA3  1 
ATOM   1028 N  N    . CYS   A 1 72  ? 18.08748 -6.10441  -11.61857 1.000 18.31086 ?  75  CYS   A N    1 
ATOM   1029 C  CA   . CYS   A 1 72  ? 19.06496 -5.18122  -11.04617 1.000 18.50524 ?  75  CYS   A CA   1 
ATOM   1030 C  C    . CYS   A 1 72  ? 18.46507 -4.60338  -9.77092  1.000 16.68782 ?  75  CYS   A C    1 
ATOM   1031 O  O    . CYS   A 1 72  ? 17.32770 -4.90848  -9.40505  1.000 16.14513 ?  75  CYS   A O    1 
ATOM   1032 C  CB   . CYS   A 1 72  ? 19.40671 -4.04949  -12.01580 1.000 19.62779 ?  75  CYS   A CB   1 
ATOM   1033 S  SG   . CYS   A 1 72  ? 18.03430 -2.93298  -12.37313 1.000 19.77970 ?  75  CYS   A SG   1 
ATOM   1034 H  H    . CYS   A 1 72  ? 17.29148 -6.01438  -11.30572 1.000 21.97303 ?  75  CYS   A H    1 
ATOM   1035 H  HA   . CYS   A 1 72  ? 19.87308 -5.67699  -10.84110 1.000 22.20629 ?  75  CYS   A HA   1 
ATOM   1036 H  HB2  . CYS   A 1 72  ? 20.12352 -3.52007  -11.63266 1.000 23.55335 ?  75  CYS   A HB2  1 
ATOM   1037 H  HB3  . CYS   A 1 72  ? 19.69460 -4.43889  -12.85626 1.000 23.55335 ?  75  CYS   A HB3  1 
ATOM   1038 H  HG   . CYS   A 1 72  ? 17.74117 -2.34109  -11.37126 1.000 23.73563 ?  75  CYS   A HG   1 
ATOM   1039 N  N    . ILE   A 1 73  ? 19.24540 -3.77097  -9.09093  1.000 15.64327 ?  76  ILE   A N    1 
ATOM   1040 C  CA   . ILE   A 1 73  ? 18.74921 -2.94005  -7.99968  1.000 13.87015 ?  76  ILE   A CA   1 
ATOM   1041 C  C    . ILE   A 1 73  ? 19.12769 -1.50682  -8.33226  1.000 14.59169 ?  76  ILE   A C    1 
ATOM   1042 O  O    . ILE   A 1 73  ? 20.30356 -1.21839  -8.58441  1.000 16.30705 ?  76  ILE   A O    1 
ATOM   1043 C  CB   . ILE   A 1 73  ? 19.35393 -3.30700  -6.63100  1.000 13.92524 ?  76  ILE   A CB   1 
ATOM   1044 C  CG1  . ILE   A 1 73  ? 19.15020 -4.78243  -6.29029  1.000 15.07583 ?  76  ILE   A CG1  1 
ATOM   1045 C  CG2  . ILE   A 1 73  ? 18.75620 -2.42122  -5.52647  1.000 14.32519 ?  76  ILE   A CG2  1 
ATOM   1046 C  CD1  . ILE   A 1 73  ? 20.06791 -5.25173  -5.19802  1.000 15.92164 ?  76  ILE   A CD1  1 
ATOM   1047 H  H    . ILE   A 1 73  ? 20.08482 -3.66772  -9.24683  1.000 18.77192 ?  76  ILE   A H    1 
ATOM   1048 H  HA   . ILE   A 1 73  ? 17.78667 -3.04476  -7.94085  1.000 16.64418 ?  76  ILE   A HA   1 
ATOM   1049 H  HB   . ILE   A 1 73  ? 20.30920 -3.14923  -6.68987  1.000 16.71029 ?  76  ILE   A HB   1 
ATOM   1050 H  HG12 . ILE   A 1 73  ? 18.23620 -4.91590  -5.99417  1.000 18.09099 ?  76  ILE   A HG12 1 
ATOM   1051 H  HG13 . ILE   A 1 73  ? 19.32427 -5.31705  -7.08072  1.000 18.09099 ?  76  ILE   A HG13 1 
ATOM   1052 H  HG21 . ILE   A 1 73  ? 18.85108 -2.87304  -4.67339  1.000 17.19022 ?  76  ILE   A HG21 1 
ATOM   1053 H  HG22 . ILE   A 1 73  ? 19.23156 -1.57589  -5.50774  1.000 17.19022 ?  76  ILE   A HG22 1 
ATOM   1054 H  HG23 . ILE   A 1 73  ? 17.81749 -2.26868  -5.71739  1.000 17.19022 ?  76  ILE   A HG23 1 
ATOM   1055 H  HD11 . ILE   A 1 73  ? 20.10743 -6.22080  -5.21338  1.000 19.10597 ?  76  ILE   A HD11 1 
ATOM   1056 H  HD12 . ILE   A 1 73  ? 20.95214 -4.88220  -5.34796  1.000 19.10597 ?  76  ILE   A HD12 1 
ATOM   1057 H  HD13 . ILE   A 1 73  ? 19.72308 -4.94824  -4.34369  1.000 19.10597 ?  76  ILE   A HD13 1 
ATOM   1058 N  N    . VAL   A 1 74  ? 18.15679 -0.60317  -8.28572  1.000 13.57118 ?  77  VAL   A N    1 
ATOM   1059 C  CA   . VAL   A 1 74  ? 18.40974 0.81957   -8.46654  1.000 13.08464 ?  77  VAL   A CA   1 
ATOM   1060 C  C    . VAL   A 1 74  ? 18.30585 1.47369   -7.09611  1.000 12.52619 ?  77  VAL   A C    1 
ATOM   1061 O  O    . VAL   A 1 74  ? 17.34073 1.23054   -6.36375  1.000 13.07978 ?  77  VAL   A O    1 
ATOM   1062 C  CB   . VAL   A 1 74  ? 17.40293 1.45016   -9.44020  1.000 13.87882 ?  77  VAL   A CB   1 
ATOM   1063 C  CG1  . VAL   A 1 74  ? 17.62150 2.95941   -9.53071  1.000 15.10295 ?  77  VAL   A CG1  1 
ATOM   1064 C  CG2  . VAL   A 1 74  ? 17.56063 0.83484   -10.82266 1.000 15.67978 ?  77  VAL   A CG2  1 
ATOM   1065 H  H    . VAL   A 1 74  ? 17.32960 -0.79413  -8.14832  1.000 16.28541 ?  77  VAL   A H    1 
ATOM   1066 H  HA   . VAL   A 1 74  ? 19.30229 0.95283   -8.82220  1.000 15.70157 ?  77  VAL   A HA   1 
ATOM   1067 H  HB   . VAL   A 1 74  ? 16.50518 1.28168   -9.11375  1.000 16.65458 ?  77  VAL   A HB   1 
ATOM   1068 H  HG11 . VAL   A 1 74  ? 17.17436 3.29631   -10.32284 1.000 18.12354 ?  77  VAL   A HG11 1 
ATOM   1069 H  HG12 . VAL   A 1 74  ? 17.25241 3.38003   -8.73841  1.000 18.12354 ?  77  VAL   A HG12 1 
ATOM   1070 H  HG13 . VAL   A 1 74  ? 18.57328 3.13785   -9.58703  1.000 18.12354 ?  77  VAL   A HG13 1 
ATOM   1071 H  HG21 . VAL   A 1 74  ? 17.10246 1.39254   -11.47070 1.000 18.81574 ?  77  VAL   A HG21 1 
ATOM   1072 H  HG22 . VAL   A 1 74  ? 18.50466 0.78312   -11.03950 1.000 18.81574 ?  77  VAL   A HG22 1 
ATOM   1073 H  HG23 . VAL   A 1 74  ? 17.17296 -0.05432  -10.81867 1.000 18.81574 ?  77  VAL   A HG23 1 
ATOM   1074 N  N    . CYS   A 1 75  ? 19.29805 2.28295   -6.74487  1.000 12.12704 ?  78  CYS   A N    1 
ATOM   1075 C  CA   . CYS   A 1 75  ? 19.23299 3.11695   -5.55300  1.000 11.80082 ?  78  CYS   A CA   1 
ATOM   1076 C  C    . CYS   A 1 75  ? 19.31536 4.58552   -5.93761  1.000 12.38017 ?  78  CYS   A C    1 
ATOM   1077 O  O    . CYS   A 1 75  ? 20.02662 4.96643   -6.87685  1.000 13.54893 ?  78  CYS   A O    1 
ATOM   1078 C  CB   . CYS   A 1 75  ? 20.32434 2.77845   -4.52888  1.000 12.86973 ?  78  CYS   A CB   1 
ATOM   1079 S  SG   . CYS   A 1 75  ? 20.21474 1.10741   -3.88249  1.000 13.73790 ?  78  CYS   A SG   1 
ATOM   1080 H  H    . CYS   A 1 75  ? 20.03000 2.36683   -7.18850  1.000 14.55245 ?  78  CYS   A H    1 
ATOM   1081 H  HA   . CYS   A 1 75  ? 18.37874 2.96030   -5.12102  1.000 14.16099 ?  78  CYS   A HA   1 
ATOM   1082 H  HB2  . CYS   A 1 75  ? 21.19116 2.87586   -4.95317  1.000 15.44368 ?  78  CYS   A HB2  1 
ATOM   1083 H  HB3  . CYS   A 1 75  ? 20.25056 3.39115   -3.78051  1.000 15.44368 ?  78  CYS   A HB3  1 
ATOM   1084 H  HG   . CYS   A 1 75  ? 21.07753 0.94780   -3.06389  1.000 16.48548 ?  78  CYS   A HG   1 
ATOM   1085 N  N    . ASN   A 1 76  ? 18.57871 5.40898   -5.19937  1.000 11.59537 ?  79  ASN   A N    1 
ATOM   1086 C  CA   . ASN   A 1 76  ? 18.54461 6.83454   -5.50634  1.000 11.82448 ?  79  ASN   A CA   1 
ATOM   1087 C  C    . ASN   A 1 76  ? 17.99324 7.59088   -4.29931  1.000 11.74242 ?  79  ASN   A C    1 
ATOM   1088 O  O    . ASN   A 1 76  ? 17.63511 6.99741   -3.27391  1.000 12.00360 ?  79  ASN   A O    1 
ATOM   1089 C  CB   . ASN   A 1 76  ? 17.71702 7.07673   -6.78140  1.000 12.32850 ?  79  ASN   A CB   1 
ATOM   1090 C  CG   . ASN   A 1 76  ? 18.11570 8.33657   -7.55040  1.000 12.78656 ?  79  ASN   A CG   1 
ATOM   1091 O  OD1  . ASN   A 1 76  ? 18.83223 9.19785   -7.05359  1.000 13.34280 ?  79  ASN   A OD1  1 
ATOM   1092 N  ND2  . ASN   A 1 76  ? 17.65083 8.42266   -8.78923  1.000 13.56548 ?  79  ASN   A ND2  1 
ATOM   1093 H  H    . ASN   A 1 76  ? 18.09827 5.17038   -4.52718  1.000 13.91444 ?  79  ASN   A H    1 
ATOM   1094 H  HA   . ASN   A 1 76  ? 19.44671 7.15983   -5.65226  1.000 14.18938 ?  79  ASN   A HA   1 
ATOM   1095 H  HB2  . ASN   A 1 76  ? 17.83255 6.31930   -7.37625  1.000 14.79420 ?  79  ASN   A HB2  1 
ATOM   1096 H  HB3  . ASN   A 1 76  ? 16.78316 7.16522   -6.53445  1.000 14.79420 ?  79  ASN   A HB3  1 
ATOM   1097 H  HD21 . ASN   A 1 76  ? 17.15966 7.79325   -9.10891  1.000 16.27858 ?  79  ASN   A HD21 1 
ATOM   1098 H  HD22 . ASN   A 1 76  ? 17.84049 9.10791   -9.27303  1.000 16.27858 ?  79  ASN   A HD22 1 
ATOM   1099 N  N    . THR   A 1 77  ? 17.88988 8.90770   -4.45922  1.000 12.07953 ?  80  THR   A N    1 
ATOM   1100 C  CA   . THR   A 1 77  ? 17.37642 9.83727   -3.46949  1.000 12.00338 ?  80  THR   A CA   1 
ATOM   1101 C  C    . THR   A 1 77  ? 16.41781 10.77709  -4.17860  1.000 12.63584 ?  80  THR   A C    1 
ATOM   1102 O  O    . THR   A 1 77  ? 16.68936 11.22062  -5.29883  1.000 13.00976 ?  80  THR   A O    1 
ATOM   1103 C  CB   . THR   A 1 77  ? 18.53821 10.63493  -2.84253  1.000 12.76653 ?  80  THR   A CB   1 
ATOM   1104 O  OG1  . THR   A 1 77  ? 19.37545 9.74865   -2.09039  1.000 12.95568 ?  80  THR   A OG1  1 
ATOM   1105 C  CG2  . THR   A 1 77  ? 18.06275 11.80190  -1.98245  1.000 14.21278 ?  80  THR   A CG2  1 
ATOM   1106 H  H    . THR   A 1 77  ? 18.12768 9.30863   -5.18193  1.000 14.49544 ?  80  THR   A H    1 
ATOM   1107 H  HA   . THR   A 1 77  ? 16.90191 9.37950   -2.75803  1.000 14.40405 ?  80  THR   A HA   1 
ATOM   1108 H  HB   . THR   A 1 77  ? 19.05746 11.03625  -3.55682  1.000 15.31983 ?  80  THR   A HB   1 
ATOM   1109 H  HG1  . THR   A 1 77  ? 18.90487 9.26068   -1.59436  1.000 15.54681 ?  80  THR   A HG1  1 
ATOM   1110 H  HG21 . THR   A 1 77  ? 18.76375 12.06754  -1.36687  1.000 17.05534 ?  80  THR   A HG21 1 
ATOM   1111 H  HG22 . THR   A 1 77  ? 17.83526 12.55811  -2.54575  1.000 17.05534 ?  80  THR   A HG22 1 
ATOM   1112 H  HG23 . THR   A 1 77  ? 17.27908 11.54135  -1.47366  1.000 17.05534 ?  80  THR   A HG23 1 
ATOM   1113 N  N    . LEU   A 1 78  ? 15.29795 11.07079  -3.51752  1.000 11.91663 ?  81  LEU   A N    1 
ATOM   1114 C  CA   . LEU   A 1 78  ? 14.29120 12.01584  -3.99907  1.000 12.55862 ?  81  LEU   A CA   1 
ATOM   1115 C  C    . LEU   A 1 78  ? 14.31175 13.21698  -3.06495  1.000 13.27910 ?  81  LEU   A C    1 
ATOM   1116 O  O    . LEU   A 1 78  ? 14.06251 13.07006  -1.86382  1.000 13.72896 ?  81  LEU   A O    1 
ATOM   1117 C  CB   . LEU   A 1 78  ? 12.90413 11.36637  -3.99028  1.000 13.44988 ?  81  LEU   A CB   1 
ATOM   1118 C  CG   . LEU   A 1 78  ? 11.75532 12.19866  -4.54904  1.000 13.52455 ?  81  LEU   A CG   1 
ATOM   1119 C  CD1  . LEU   A 1 78  ? 11.82279 12.23157  -6.07204  1.000 14.37839 ?  81  LEU   A CD1  1 
ATOM   1120 C  CD2  . LEU   A 1 78  ? 10.41105 11.70680  -4.07373  1.000 15.48757 ?  81  LEU   A CD2  1 
ATOM   1121 H  H    . LEU   A 1 78  ? 15.09199 10.72165  -2.75905  1.000 14.29995 ?  81  LEU   A H    1 
ATOM   1122 H  HA   . LEU   A 1 78  ? 14.49468 12.30247  -4.90314  1.000 15.07034 ?  81  LEU   A HA   1 
ATOM   1123 H  HB2  . LEU   A 1 78  ? 12.95006 10.55420  -4.51865  1.000 16.13986 ?  81  LEU   A HB2  1 
ATOM   1124 H  HB3  . LEU   A 1 78  ? 12.67928 11.15207  -3.07136  1.000 16.13986 ?  81  LEU   A HB3  1 
ATOM   1125 H  HG   . LEU   A 1 78  ? 11.84628 13.10549  -4.21696  1.000 16.22946 ?  81  LEU   A HG   1 
ATOM   1126 H  HD11 . LEU   A 1 78  ? 11.15068 12.84679  -6.40471  1.000 17.25407 ?  81  LEU   A HD11 1 
ATOM   1127 H  HD12 . LEU   A 1 78  ? 12.70574 12.52830  -6.34270  1.000 17.25407 ?  81  LEU   A HD12 1 
ATOM   1128 H  HD13 . LEU   A 1 78  ? 11.65388 11.34008  -6.41498  1.000 17.25407 ?  81  LEU   A HD13 1 
ATOM   1129 H  HD21 . LEU   A 1 78  ? 9.71438  12.22815  -4.50239  1.000 18.58508 ?  81  LEU   A HD21 1 
ATOM   1130 H  HD22 . LEU   A 1 78  ? 10.31596 10.77065  -4.30927  1.000 18.58508 ?  81  LEU   A HD22 1 
ATOM   1131 H  HD23 . LEU   A 1 78  ? 10.35841 11.81264  -3.11095  1.000 18.58508 ?  81  LEU   A HD23 1 
ATOM   1132 N  N    . ILE   A 1 79  ? 14.62324 14.39160  -3.60329  1.000 14.26664 ?  82  ILE   A N    1 
ATOM   1133 C  CA   . ILE   A 1 79  ? 14.65056 15.63472  -2.84097  1.000 14.90963 ?  82  ILE   A CA   1 
ATOM   1134 C  C    . ILE   A 1 79  ? 13.75486 16.62797  -3.55803  1.000 15.56816 ?  82  ILE   A C    1 
ATOM   1135 O  O    . ILE   A 1 79  ? 13.97471 16.91938  -4.74288  1.000 15.90406 ?  82  ILE   A O    1 
ATOM   1136 C  CB   . ILE   A 1 79  ? 16.06662 16.22114  -2.70164  1.000 17.45287 ?  82  ILE   A CB   1 
ATOM   1137 C  CG1  . ILE   A 1 79  ? 16.92318 15.32147  -1.81777  1.000 18.33161 ?  82  ILE   A CG1  1 
ATOM   1138 C  CG2  . ILE   A 1 79  ? 16.03098 17.62969  -2.08991  1.000 20.39380 ?  82  ILE   A CG2  1 
ATOM   1139 C  CD1  . ILE   A 1 79  ? 18.40589 15.56837  -1.96426  1.000 20.27479 ?  82  ILE   A CD1  1 
ATOM   1140 H  H    . ILE   A 1 79  ? 14.82818 14.49624  -4.43194  1.000 17.11997 ?  82  ILE   A H    1 
ATOM   1141 H  HA   . ILE   A 1 79  ? 14.30361 15.46343  -1.95149  1.000 17.89156 ?  82  ILE   A HA   1 
ATOM   1142 H  HB   . ILE   A 1 79  ? 16.44702 16.27343  -3.59240  1.000 20.94345 ?  82  ILE   A HB   1 
ATOM   1143 H  HG12 . ILE   A 1 79  ? 16.68628 15.47713  -0.89012  1.000 21.99793 ?  82  ILE   A HG12 1 
ATOM   1144 H  HG13 . ILE   A 1 79  ? 16.75134 14.39632  -2.05331  1.000 21.99793 ?  82  ILE   A HG13 1 
ATOM   1145 H  HG21 . ILE   A 1 79  ? 16.91867 17.85897  -1.77314  1.000 24.47256 ?  82  ILE   A HG21 1 
ATOM   1146 H  HG22 . ILE   A 1 79  ? 15.74862 18.26194  -2.76919  1.000 24.47256 ?  82  ILE   A HG22 1 
ATOM   1147 H  HG23 . ILE   A 1 79  ? 15.40367 17.63690  -1.35009  1.000 24.47256 ?  82  ILE   A HG23 1 
ATOM   1148 H  HD11 . ILE   A 1 79  ? 18.88796 14.93183  -1.41351  1.000 24.32975 ?  82  ILE   A HD11 1 
ATOM   1149 H  HD12 . ILE   A 1 79  ? 18.65442 15.45533  -2.89504  1.000 24.32975 ?  82  ILE   A HD12 1 
ATOM   1150 H  HD13 . ILE   A 1 79  ? 18.60540 16.47284  -1.67611  1.000 24.32975 ?  82  ILE   A HD13 1 
ATOM   1151 N  N    . ASN   A 1 80  ? 12.74594 17.14222  -2.85939  1.000 15.97771 ?  83  ASN   A N    1 
ATOM   1152 C  CA   . ASN   A 1 80  ? 11.82457 18.12405  -3.42970  1.000 17.61241 ?  83  ASN   A CA   1 
ATOM   1153 C  C    . ASN   A 1 80  ? 11.28639 17.62306  -4.76801  1.000 16.76690 ?  83  ASN   A C    1 
ATOM   1154 O  O    . ASN   A 1 80  ? 11.22886 18.34834  -5.76592  1.000 18.57805 ?  83  ASN   A O    1 
ATOM   1155 C  CB   . ASN   A 1 80  ? 12.48403 19.48873  -3.58534  1.000 19.42790 ?  83  ASN   A CB   1 
ATOM   1156 C  CG   . ASN   A 1 80  ? 12.87795 20.08626  -2.25968  1.000 20.63092 ?  83  ASN   A CG   1 
ATOM   1157 O  OD1  . ASN   A 1 80  ? 12.24700 19.82885  -1.22518  1.000 22.74852 ?  83  ASN   A OD1  1 
ATOM   1158 N  ND2  . ASN   A 1 80  ? 13.93747 20.87206  -2.26997  1.000 23.31120 ?  83  ASN   A ND2  1 
ATOM   1159 H  H    . ASN   A 1 80  ? 12.57144 16.93625  -2.04286  1.000 19.17326 ?  83  ASN   A H    1 
ATOM   1160 H  HA   . ASN   A 1 80  ? 11.07851 18.23385  -2.81958  1.000 21.13489 ?  83  ASN   A HA   1 
ATOM   1161 H  HB2  . ASN   A 1 80  ? 13.28491 19.39534  -4.12456  1.000 23.31348 ?  83  ASN   A HB2  1 
ATOM   1162 H  HB3  . ASN   A 1 80  ? 11.86216 20.09510  -4.01719  1.000 23.31348 ?  83  ASN   A HB3  1 
ATOM   1163 H  HD21 . ASN   A 1 80  ? 14.35866 21.01638  -3.00575  1.000 27.97344 ?  83  ASN   A HD21 1 
ATOM   1164 H  HD22 . ASN   A 1 80  ? 14.20701 21.24004  -1.54090  1.000 27.97344 ?  83  ASN   A HD22 1 
ATOM   1165 N  N    . GLU   A 1 81  ? 10.89036 16.35057  -4.78048  1.000 16.30684 ?  84  GLU   A N    1 
ATOM   1166 C  CA   . GLU   A 1 81  ? 10.25357 15.72394  -5.94714  1.000 17.35553 ?  84  GLU   A CA   1 
ATOM   1167 C  C    . GLU   A 1 81  ? 11.17988 15.63783  -7.16395  1.000 18.84670 ?  84  GLU   A C    1 
ATOM   1168 O  O    . GLU   A 1 81  ? 10.72612 15.61589  -8.31164  1.000 22.27821 ?  84  GLU   A O    1 
ATOM   1169 C  CB   . GLU   A 1 81  ? 8.89265  16.33905  -6.29230  1.000 19.38353 ?  84  GLU   A CB   1 
ATOM   1170 C  CG   . GLU   A 1 81  ? 7.84964  16.14388  -5.18857  1.000 21.45430 ?  84  GLU   A CG   1 
ATOM   1171 C  CD   . GLU   A 1 81  ? 6.41706  16.42890  -5.64240  1.000 24.49938 ?  84  GLU   A CD   1 
ATOM   1172 O  OE1  . GLU   A 1 81  ? 6.24985  17.19597  -6.61333  1.000 27.41656 ?  84  GLU   A OE1  1 
ATOM   1173 O  OE2  . GLU   A 1 81  ? 5.45464  15.89978  -5.03606  1.000 26.99266 ?  84  GLU   A OE2  1 
ATOM   1174 H  H    . GLU   A 1 81  ? 10.97999 15.81573  -4.11301  1.000 19.56821 ?  84  GLU   A H    1 
ATOM   1175 H  HA   . GLU   A 1 81  ? 10.06782 14.80502  -5.69816  1.000 20.82663 ?  84  GLU   A HA   1 
ATOM   1176 H  HB2  . GLU   A 1 81  ? 9.00480  17.29225  -6.43281  1.000 23.26023 ?  84  GLU   A HB2  1 
ATOM   1177 H  HB3  . GLU   A 1 81  ? 8.55481  15.92209  -7.10033  1.000 23.26023 ?  84  GLU   A HB3  1 
ATOM   1178 H  HG2  . GLU   A 1 81  ? 7.88614  15.22407  -4.88276  1.000 25.74516 ?  84  GLU   A HG2  1 
ATOM   1179 H  HG3  . GLU   A 1 81  ? 8.05352  16.74555  -4.45555  1.000 25.74516 ?  84  GLU   A HG3  1 
ATOM   1180 N  N    . LYS   A 1 82  ? 12.48375 15.60427  -6.94038  1.000 15.63815 ?  85  LYS   A N    1 
ATOM   1181 C  CA   . LYS   A 1 82  ? 13.45936 15.39880  -8.00684  1.000 16.59962 ?  85  LYS   A CA   1 
ATOM   1182 C  C    . LYS   A 1 82  ? 14.38122 14.24073  -7.66023  1.000 15.51722 ?  85  LYS   A C    1 
ATOM   1183 O  O    . LYS   A 1 82  ? 14.98243 14.22376  -6.58049  1.000 15.56727 ?  85  LYS   A O    1 
ATOM   1184 C  CB   . LYS   A 1 82  ? 14.27181 16.67679  -8.23110  1.000 17.58243 ?  85  LYS   A CB   1 
ATOM   1185 C  CG   . LYS   A 1 82  ? 13.43330 17.85060  -8.73606  1.000 18.49833 ?  85  LYS   A CG   1 
ATOM   1186 C  CD   . LYS   A 1 82  ? 14.18508 19.16801  -8.70021  1.000 19.66628 ?  85  LYS   A CD   1 
ATOM   1187 C  CE   . LYS   A 1 82  ? 14.17704 19.75073  -7.29423  1.000 20.17479 ?  85  LYS   A CE   1 
ATOM   1188 N  NZ   . LYS   A 1 82  ? 14.86252 21.04921  -7.23429  1.000 20.91492 ?  85  LYS   A NZ   1 
ATOM   1189 H  H    . LYS   A 1 82  ? 12.83898 15.69986  -6.16303  1.000 18.76578 ?  85  LYS   A H    1 
ATOM   1190 H  HA   . LYS   A 1 82  ? 12.99864 15.16199  -8.82694  1.000 19.91955 ?  85  LYS   A HA   1 
ATOM   1191 H  HB2  . LYS   A 1 82  ? 14.67761 16.94108  -7.39064  1.000 21.09891 ?  85  LYS   A HB2  1 
ATOM   1192 H  HB3  . LYS   A 1 82  ? 14.96055 16.49804  -8.89033  1.000 21.09891 ?  85  LYS   A HB3  1 
ATOM   1193 H  HG2  . LYS   A 1 82  ? 13.17120 17.68032  -9.65432  1.000 22.19800 ?  85  LYS   A HG2  1 
ATOM   1194 H  HG3  . LYS   A 1 82  ? 12.64545 17.94014  -8.17733  1.000 22.19800 ?  85  LYS   A HG3  1 
ATOM   1195 H  HD2  . LYS   A 1 82  ? 15.10578 19.02398  -8.96940  1.000 23.59953 ?  85  LYS   A HD2  1 
ATOM   1196 H  HD3  . LYS   A 1 82  ? 13.75947 19.80122  -9.29922  1.000 23.59953 ?  85  LYS   A HD3  1 
ATOM   1197 H  HE2  . LYS   A 1 82  ? 13.25952 19.87867  -7.00667  1.000 24.20975 ?  85  LYS   A HE2  1 
ATOM   1198 H  HE3  . LYS   A 1 82  ? 14.63115 19.14009  -6.69273  1.000 24.20975 ?  85  LYS   A HE3  1 
ATOM   1199 H  HZ1  . LYS   A 1 82  ? 14.72414 21.50156  -7.98817  1.000 25.09790 ?  85  LYS   A HZ1  1 
ATOM   1200 H  HZ2  . LYS   A 1 82  ? 15.73755 20.92683  -7.12735  1.000 25.09790 ?  85  LYS   A HZ2  1 
ATOM   1201 H  HZ3  . LYS   A 1 82  ? 14.55183 21.52614  -6.55010  1.000 25.09790 ?  85  LYS   A HZ3  1 
ATOM   1202 N  N    . TRP   A 1 83  ? 14.47748 13.26629  -8.56750  1.000 14.82278 ?  86  TRP   A N    1 
ATOM   1203 C  CA   . TRP   A 1 83  ? 15.37837 12.13305  -8.38258  1.000 14.70973 ?  86  TRP   A CA   1 
ATOM   1204 C  C    . TRP   A 1 83  ? 16.79669 12.53071  -8.76505  1.000 15.01371 ?  86  TRP   A C    1 
ATOM   1205 O  O    . TRP   A 1 83  ? 17.00281 13.28479  -9.71756  1.000 16.96117 ?  86  TRP   A O    1 
ATOM   1206 C  CB   . TRP   A 1 83  ? 14.93083 10.95056  -9.25300  1.000 14.55480 ?  86  TRP   A CB   1 
ATOM   1207 C  CG   . TRP   A 1 83  ? 13.69027 10.27212  -8.76810  1.000 14.59868 ?  86  TRP   A CG   1 
ATOM   1208 C  CD1  . TRP   A 1 83  ? 12.43822 10.33734  -9.30882  1.000 15.72942 ?  86  TRP   A CD1  1 
ATOM   1209 C  CD2  . TRP   A 1 83  ? 13.58777 9.41598   -7.63203  1.000 13.55189 ?  86  TRP   A CD2  1 
ATOM   1210 N  NE1  . TRP   A 1 83  ? 11.55818 9.56652   -8.57429  1.000 15.68763 ?  86  TRP   A NE1  1 
ATOM   1211 C  CE2  . TRP   A 1 83  ? 12.24258 8.99608   -7.53413  1.000 14.60701 ?  86  TRP   A CE2  1 
ATOM   1212 C  CE3  . TRP   A 1 83  ? 14.50584 8.96612   -6.68176  1.000 13.56299 ?  86  TRP   A CE3  1 
ATOM   1213 C  CZ2  . TRP   A 1 83  ? 11.79472 8.15875   -6.51431  1.000 14.54876 ?  86  TRP   A CZ2  1 
ATOM   1214 C  CZ3  . TRP   A 1 83  ? 14.05832 8.13058   -5.67851  1.000 14.23199 ?  86  TRP   A CZ3  1 
ATOM   1215 C  CH2  . TRP   A 1 83  ? 12.72240 7.72548   -5.61001  1.000 14.01884 ?  86  TRP   A CH2  1 
ATOM   1216 H  H    . TRP   A 1 83  ? 14.02894 13.24021  -9.30080  1.000 17.78734 ?  86  TRP   A H    1 
ATOM   1217 H  HA   . TRP   A 1 83  ? 15.36624 11.85521  -7.45331  1.000 17.65167 ?  86  TRP   A HA   1 
ATOM   1218 H  HB2  . TRP   A 1 83  ? 14.75817 11.27362  -10.15118 1.000 17.46576 ?  86  TRP   A HB2  1 
ATOM   1219 H  HB3  . TRP   A 1 83  ? 15.64098 10.29001  -9.26882  1.000 17.46576 ?  86  TRP   A HB3  1 
ATOM   1220 H  HD1  . TRP   A 1 83  ? 12.21044 10.83029  -10.06381 1.000 18.87530 ?  86  TRP   A HD1  1 
ATOM   1221 H  HE1  . TRP   A 1 83  ? 10.72114 9.46234   -8.74197  1.000 18.82515 ?  86  TRP   A HE1  1 
ATOM   1222 H  HE3  . TRP   A 1 83  ? 15.39855 9.22346   -6.72367  1.000 16.27559 ?  86  TRP   A HE3  1 
ATOM   1223 H  HZ2  . TRP   A 1 83  ? 10.90201 7.90559   -6.45197  1.000 17.45852 ?  86  TRP   A HZ2  1 
ATOM   1224 H  HZ3  . TRP   A 1 83  ? 14.65842 7.83077   -5.03439  1.000 17.07839 ?  86  TRP   A HZ3  1 
ATOM   1225 H  HH2  . TRP   A 1 83  ? 12.45844 7.14646   -4.93181  1.000 16.82261 ?  86  TRP   A HH2  1 
ATOM   1226 N  N    . GLY   A 1 84  ? 17.77577 12.00391  -8.04773  1.000 15.35286 ?  87  GLY   A N    1 
ATOM   1227 C  CA   . GLY   A 1 84  ? 19.17513 12.25121  -8.33855  1.000 15.88834 ?  87  GLY   A CA   1 
ATOM   1228 C  C    . GLY   A 1 84  ? 19.77959 11.21235  -9.25292  1.000 15.18804 ?  87  GLY   A C    1 
ATOM   1229 O  O    . GLY   A 1 84  ? 19.08477 10.59007  -10.06120 1.000 15.11131 ?  87  GLY   A O    1 
ATOM   1230 H  H    . GLY   A 1 84  ? 17.65030 11.48761  -7.37151  1.000 18.42343 ?  87  GLY   A H    1 
ATOM   1231 H  HA2  . GLY   A 1 84  ? 19.26378 13.11830  -8.76423  1.000 19.06601 ?  87  GLY   A HA2  1 
ATOM   1232 H  HA3  . GLY   A 1 84  ? 19.67745 12.25395  -7.50874  1.000 19.06601 ?  87  GLY   A HA3  1 
ATOM   1233 N  N    . ARG   A 1 85  ? 21.09957 11.02312  -9.12001  1.000 16.52911 ?  88  ARG   A N    1 
ATOM   1234 C  CA   . ARG   A 1 85  ? 21.83808 10.05984  -9.93292  1.000 17.43582 ?  88  ARG   A CA   1 
ATOM   1235 C  C    . ARG   A 1 85  ? 21.50830 8.64477   -9.47940  1.000 16.69897 ?  88  ARG   A C    1 
ATOM   1236 O  O    . ARG   A 1 85  ? 21.66262 8.30939   -8.30296  1.000 17.62611 ?  88  ARG   A O    1 
ATOM   1237 C  CB   . ARG   A 1 85  ? 23.33509 10.30075  -9.73848  1.000 20.25053 ?  88  ARG   A CB   1 
ATOM   1238 C  CG   . ARG   A 1 85  ? 24.25219 9.31760   -10.45059 1.000 22.14671 ?  88  ARG   A CG   1 
ATOM   1239 C  CD   . ARG   A 1 85  ? 25.69546 9.52519   -9.97580  1.000 26.07550 ?  88  ARG   A CD   1 
ATOM   1240 N  NE   . ARG   A 1 85  ? 26.00184 8.81616   -8.73204  1.000 25.78694 ?  88  ARG   A NE   1 
ATOM   1241 C  CZ   . ARG   A 1 85  ? 27.16677 8.89205   -8.10057  1.000 27.54665 ?  88  ARG   A CZ   1 
ATOM   1242 N  NH1  . ARG   A 1 85  ? 28.17062 9.59827   -8.59379  1.000 29.65125 ?  88  ARG   A NH1  1 
ATOM   1243 N  NH2  . ARG   A 1 85  ? 27.31709 8.26750   -6.93223  1.000 28.42350 ?  88  ARG   A NH2  1 
ATOM   1244 H  H    . ARG   A 1 85  ? 21.59334 11.44735  -8.55803  1.000 19.83494 ?  88  ARG   A H    1 
ATOM   1245 H  HA   . ARG   A 1 85  ? 21.60133 10.15965  -10.86827 1.000 20.92298 ?  88  ARG   A HA   1 
ATOM   1246 H  HB2  . ARG   A 1 85  ? 23.54750 11.18696  -10.07077 1.000 24.30064 ?  88  ARG   A HB2  1 
ATOM   1247 H  HB3  . ARG   A 1 85  ? 23.53267 10.24574  -8.79041  1.000 24.30064 ?  88  ARG   A HB3  1 
ATOM   1248 H  HG2  . ARG   A 1 85  ? 23.98276 8.40875   -10.24493 1.000 26.57605 ?  88  ARG   A HG2  1 
ATOM   1249 H  HG3  . ARG   A 1 85  ? 24.21333 9.46648   -11.40830 1.000 26.57605 ?  88  ARG   A HG3  1 
ATOM   1250 H  HD2  . ARG   A 1 85  ? 26.30140 9.20099   -10.66036 1.000 31.29060 ?  88  ARG   A HD2  1 
ATOM   1251 H  HD3  . ARG   A 1 85  ? 25.84322 10.47164  -9.82313  1.000 31.29060 ?  88  ARG   A HD3  1 
ATOM   1252 H  HE   . ARG   A 1 85  ? 25.38893 8.31967   -8.38935  1.000 30.94432 ?  88  ARG   A HE   1 
ATOM   1253 H  HH11 . ARG   A 1 85  ? 28.07545 10.01959  -9.33745  1.000 35.58150 ?  88  ARG   A HH11 1 
ATOM   1254 H  HH12 . ARG   A 1 85  ? 28.91845 9.63610   -8.17079  1.000 35.58150 ?  88  ARG   A HH12 1 
ATOM   1255 H  HH21 . ARG   A 1 85  ? 26.66320 7.82163   -6.59574  1.000 34.10821 ?  88  ARG   A HH21 1 
ATOM   1256 H  HH22 . ARG   A 1 85  ? 28.06794 8.31052   -6.51513  1.000 34.10821 ?  88  ARG   A HH22 1 
ATOM   1257 N  N    . GLU   A 1 86  ? 21.07256 7.80562   -10.40909 1.000 15.05712 ?  89  GLU   A N    1 
ATOM   1258 C  CA   . GLU   A 1 86  ? 20.84612 6.40124   -10.09730 1.000 14.78649 ?  89  GLU   A CA   1 
ATOM   1259 C  C    . GLU   A 1 86  ? 22.16468 5.67859   -9.86196  1.000 15.33275 ?  89  GLU   A C    1 
ATOM   1260 O  O    . GLU   A 1 86  ? 23.12975 5.84983   -10.60960 1.000 17.24016 ?  89  GLU   A O    1 
ATOM   1261 C  CB   . GLU   A 1 86  ? 20.09802 5.71111   -11.24526 1.000 15.77930 ?  89  GLU   A CB   1 
ATOM   1262 C  CG   . GLU   A 1 86  ? 18.67920 6.22283   -11.39111 1.000 16.75784 ?  89  GLU   A CG   1 
ATOM   1263 C  CD   . GLU   A 1 86  ? 17.85109 5.54568   -12.45849 1.000 16.19490 ?  89  GLU   A CD   1 
ATOM   1264 O  OE1  . GLU   A 1 86  ? 18.40552 5.16107   -13.50880 1.000 19.66585 ?  89  GLU   A OE1  1 
ATOM   1265 O  OE2  . GLU   A 1 86  ? 16.62788 5.40780   -12.25670 1.000 15.49428 ?  89  GLU   A OE2  1 
ATOM   1266 H  H    . GLU   A 1 86  ? 20.90115 8.02209   -11.22356 1.000 18.06854 ?  89  GLU   A H    1 
ATOM   1267 H  HA   . GLU   A 1 86  ? 20.30911 6.34491   -9.29147  1.000 17.74379 ?  89  GLU   A HA   1 
ATOM   1268 H  HB2  . GLU   A 1 86  ? 20.56768 5.87881   -12.07725 1.000 18.93515 ?  89  GLU   A HB2  1 
ATOM   1269 H  HB3  . GLU   A 1 86  ? 20.05992 4.75743   -11.07220 1.000 18.93515 ?  89  GLU   A HB3  1 
ATOM   1270 H  HG2  . GLU   A 1 86  ? 18.22010 6.09591   -10.54611 1.000 20.10941 ?  89  GLU   A HG2  1 
ATOM   1271 H  HG3  . GLU   A 1 86  ? 18.71581 7.16705   -11.61023 1.000 20.10941 ?  89  GLU   A HG3  1 
ATOM   1272 N  N    . GLU   A 1 87  ? 22.19032 4.85033   -8.82768  1.000 15.49615 ?  90  GLU   A N    1 
ATOM   1273 C  CA   . GLU   A 1 87  ? 23.28087 3.91581   -8.57629  1.000 16.03072 ?  90  GLU   A CA   1 
ATOM   1274 C  C    . GLU   A 1 87  ? 22.72241 2.53043   -8.84308  1.000 15.46300 ?  90  GLU   A C    1 
ATOM   1275 O  O    . GLU   A 1 87  ? 21.80025 2.09852   -8.14679  1.000 15.49266 ?  90  GLU   A O    1 
ATOM   1276 C  CB   . GLU   A 1 87  ? 23.81052 4.05962   -7.15044  1.000 17.25681 ?  90  GLU   A CB   1 
ATOM   1277 C  CG   . GLU   A 1 87  ? 24.37106 5.45683   -6.88917  1.000 18.47730 ?  90  GLU   A CG   1 
ATOM   1278 C  CD   . GLU   A 1 87  ? 24.99296 5.64157   -5.51872  1.000 18.82242 ?  90  GLU   A CD   1 
ATOM   1279 O  OE1  . GLU   A 1 87  ? 25.40408 4.63822   -4.89664  1.000 20.06680 ?  90  GLU   A OE1  1 
ATOM   1280 O  OE2  . GLU   A 1 87  ? 25.07896 6.81424   -5.06797  1.000 21.19309 ?  90  GLU   A OE2  1 
ATOM   1281 H  H    . GLU   A 1 87  ? 21.56665 4.80891   -8.23698  1.000 18.59539 ?  90  GLU   A H    1 
ATOM   1282 H  HA   . GLU   A 1 87  ? 24.03402 4.07623   -9.16615  1.000 19.23686 ?  90  GLU   A HA   1 
ATOM   1283 H  HB2  . GLU   A 1 87  ? 23.08739 3.90007   -6.52393  1.000 20.70817 ?  90  GLU   A HB2  1 
ATOM   1284 H  HB3  . GLU   A 1 87  ? 24.52137 3.41525   -7.00771  1.000 20.70817 ?  90  GLU   A HB3  1 
ATOM   1285 H  HG2  . GLU   A 1 87  ? 25.05752 5.64264   -7.54882  1.000 22.17275 ?  90  GLU   A HG2  1 
ATOM   1286 H  HG3  . GLU   A 1 87  ? 23.64928 6.09962   -6.97138  1.000 22.17275 ?  90  GLU   A HG3  1 
ATOM   1287 N  N    . ILE   A 1 88  ? 23.26651 1.83878   -9.84135  1.000 17.18559 ?  91  ILE   A N    1 
ATOM   1288 C  CA   . ILE   A 1 88  ? 22.71744 0.57073   -10.30321 1.000 17.61539 ?  91  ILE   A CA   1 
ATOM   1289 C  C    . ILE   A 1 88  ? 23.64842 -0.56969  -9.91608  1.000 18.93041 ?  91  ILE   A C    1 
ATOM   1290 O  O    . ILE   A 1 88  ? 24.85078 -0.53913  -10.20237 1.000 20.32076 ?  91  ILE   A O    1 
ATOM   1291 C  CB   . ILE   A 1 88  ? 22.44645 0.60242   -11.81655 1.000 19.49990 ?  91  ILE   A CB   1 
ATOM   1292 C  CG1  . ILE   A 1 88  ? 21.58835 1.82394   -12.17330 1.000 21.23045 ?  91  ILE   A CG1  1 
ATOM   1293 C  CG2  . ILE   A 1 88  ? 21.75608 -0.67998  -12.22546 1.000 20.31306 ?  91  ILE   A CG2  1 
ATOM   1294 C  CD1  . ILE   A 1 88  ? 21.47028 2.08534   -13.68042 1.000 23.06900 ?  91  ILE   A CD1  1 
ATOM   1295 H  H    . ILE   A 1 88  ? 23.96664 2.09031   -10.27279 1.000 20.62271 ?  91  ILE   A H    1 
ATOM   1296 H  HA   . ILE   A 1 88  ? 21.87871 0.40779   -9.84400  1.000 21.13846 ?  91  ILE   A HA   1 
ATOM   1297 H  HB   . ILE   A 1 88  ? 23.28684 0.67589   -12.29535 1.000 23.39988 ?  91  ILE   A HB   1 
ATOM   1298 H  HG12 . ILE   A 1 88  ? 20.69284 1.68671   -11.82670 1.000 25.47654 ?  91  ILE   A HG12 1 
ATOM   1299 H  HG13 . ILE   A 1 88  ? 21.98413 2.61110   -11.76753 1.000 25.47654 ?  91  ILE   A HG13 1 
ATOM   1300 H  HG21 . ILE   A 1 88  ? 21.45680 -0.59835  -13.14451 1.000 24.37567 ?  91  ILE   A HG21 1 
ATOM   1301 H  HG22 . ILE   A 1 88  ? 22.38338 -1.41556  -12.14595 1.000 24.37567 ?  91  ILE   A HG22 1 
ATOM   1302 H  HG23 . ILE   A 1 88  ? 20.99568 -0.82920  -11.64199 1.000 24.37567 ?  91  ILE   A HG23 1 
ATOM   1303 H  HD11 . ILE   A 1 88  ? 21.20693 3.00823   -13.82120 1.000 27.68280 ?  91  ILE   A HD11 1 
ATOM   1304 H  HD12 . ILE   A 1 88  ? 22.32989 1.91927   -14.09804 1.000 27.68280 ?  91  ILE   A HD12 1 
ATOM   1305 H  HD13 . ILE   A 1 88  ? 20.80112 1.48994   -14.05274 1.000 27.68280 ?  91  ILE   A HD13 1 
ATOM   1306 N  N    . THR   A 1 89  ? 23.07925 -1.57627  -9.26519  1.000 18.12580 ?  92  THR   A N    1 
ATOM   1307 C  CA   . THR   A 1 89  ? 23.75981 -2.81884  -8.91604  1.000 20.35237 ?  92  THR   A CA   1 
ATOM   1308 C  C    . THR   A 1 89  ? 23.20521 -3.91528  -9.81415  1.000 20.71720 ?  92  THR   A C    1 
ATOM   1309 O  O    . THR   A 1 89  ? 22.00098 -4.19815  -9.79287  1.000 21.05688 ?  92  THR   A O    1 
ATOM   1310 C  CB   . THR   A 1 89  ? 23.52087 -3.12330  -7.43771  1.000 21.55508 ?  92  THR   A CB   1 
ATOM   1311 O  OG1  . THR   A 1 89  ? 24.12853 -2.08804  -6.65453  1.000 22.99203 ?  92  THR   A OG1  1 
ATOM   1312 C  CG2  . THR   A 1 89  ? 24.12605 -4.45254  -7.03167  1.000 22.88670 ?  92  THR   A CG2  1 
ATOM   1313 H  H    . THR   A 1 89  ? 22.26052 -1.56315  -9.00230  1.000 21.75097 ?  92  THR   A H    1 
ATOM   1314 H  HA   . THR   A 1 89  ? 24.71624 -2.76270  -9.06765  1.000 24.42285 ?  92  THR   A HA   1 
ATOM   1315 H  HB   . THR   A 1 89  ? 22.56588 -3.17076  -7.27447  1.000 25.86609 ?  92  THR   A HB   1 
ATOM   1316 H  HG1  . THR   A 1 89  ? 23.91948 -2.17917  -5.84608  1.000 27.59044 ?  92  THR   A HG1  1 
ATOM   1317 H  HG21 . THR   A 1 89  ? 24.39784 -4.42285  -6.10100  1.000 27.46404 ?  92  THR   A HG21 1 
ATOM   1318 H  HG22 . THR   A 1 89  ? 23.47519 -5.16245  -7.14706  1.000 27.46404 ?  92  THR   A HG22 1 
ATOM   1319 H  HG23 . THR   A 1 89  ? 24.90243 -4.64502  -7.58037  1.000 27.46404 ?  92  THR   A HG23 1 
ATOM   1320 N  N    . TYR   A 1 90  ? 24.07703 -4.49609  -10.64314 1.000 24.21022 ?  93  TYR   A N    1 
ATOM   1321 C  CA   . TYR   A 1 90  ? 23.66994 -5.56803  -11.54532 1.000 26.09468 ?  93  TYR   A CA   1 
ATOM   1322 C  C    . TYR   A 1 90  ? 23.75245 -6.93254  -10.89270 1.000 26.79634 ?  93  TYR   A C    1 
ATOM   1323 O  O    . TYR   A 1 90  ? 23.00628 -7.84005  -11.28213 1.000 27.87370 ?  93  TYR   A O    1 
ATOM   1324 C  CB   . TYR   A 1 90  ? 24.52785 -5.53887  -12.81228 1.000 28.08897 ?  93  TYR   A CB   1 
ATOM   1325 C  CG   . TYR   A 1 90  ? 24.42144 -4.20083  -13.46912 1.000 29.39234 ?  93  TYR   A CG   1 
ATOM   1326 C  CD1  . TYR   A 1 90  ? 23.29166 -3.85744  -14.19336 1.000 29.48394 ?  93  TYR   A CD1  1 
ATOM   1327 C  CD2  . TYR   A 1 90  ? 25.41849 -3.24504  -13.30239 1.000 31.05217 ?  93  TYR   A CD2  1 
ATOM   1328 C  CE1  . TYR   A 1 90  ? 23.17142 -2.60358  -14.77276 1.000 31.06715 ?  93  TYR   A CE1  1 
ATOM   1329 C  CE2  . TYR   A 1 90  ? 25.30778 -1.99306  -13.88039 1.000 31.79696 ?  93  TYR   A CE2  1 
ATOM   1330 C  CZ   . TYR   A 1 90  ? 24.17842 -1.68694  -14.60549 1.000 31.52542 ?  93  TYR   A CZ   1 
ATOM   1331 O  OH   . TYR   A 1 90  ? 24.03330 -0.45015  -15.15745 1.000 34.01223 ?  93  TYR   A OH   1 
ATOM   1332 H  H    . TYR   A 1 90  ? 24.90885 -4.28523  -10.69977 1.000 29.05226 ?  93  TYR   A H    1 
ATOM   1333 H  HA   . TYR   A 1 90  ? 22.74901 -5.42730  -11.81548 1.000 31.31362 ?  93  TYR   A HA   1 
ATOM   1334 H  HB2  . TYR   A 1 90  ? 25.45610 -5.70053  -12.58182 1.000 33.70677 ?  93  TYR   A HB2  1 
ATOM   1335 H  HB3  . TYR   A 1 90  ? 24.21714 -6.21673  -13.43265 1.000 33.70677 ?  93  TYR   A HB3  1 
ATOM   1336 H  HD1  . TYR   A 1 90  ? 22.60454 -4.47629  -14.29228 1.000 35.38072 ?  93  TYR   A HD1  1 
ATOM   1337 H  HD2  . TYR   A 1 90  ? 26.17028 -3.45072  -12.79504 1.000 37.26261 ?  93  TYR   A HD2  1 
ATOM   1338 H  HE1  . TYR   A 1 90  ? 22.41596 -2.38614  -15.26966 1.000 37.28058 ?  93  TYR   A HE1  1 
ATOM   1339 H  HE2  . TYR   A 1 90  ? 25.98756 -1.36633  -13.78038 1.000 38.15635 ?  93  TYR   A HE2  1 
ATOM   1340 H  HH   . TYR   A 1 90  ? 24.70197 0.02520   -14.97712 1.000 40.81467 ?  93  TYR   A HH   1 
ATOM   1341 N  N    . ASP   A 1 91  ? 24.64157 -7.07715  -9.90844  1.000 26.76793 ?  94  ASP   A N    1 
ATOM   1342 C  CA   A ASP   A 1 91  ? 24.80442 -8.31605  -9.14795  0.478 27.81140 ?  94  ASP   A CA   1 
ATOM   1343 C  CA   B ASP   A 1 91  ? 24.80808 -8.31041  -9.14855  0.522 27.90160 ?  94  ASP   A CA   1 
ATOM   1344 C  C    . ASP   A 1 91  ? 23.74541 -8.28753  -8.06013  1.000 26.18171 ?  94  ASP   A C    1 
ATOM   1345 O  O    . ASP   A 1 91  ? 23.96304 -7.77124  -6.96192  1.000 27.47798 ?  94  ASP   A O    1 
ATOM   1346 C  CB   A ASP   A 1 91  ? 26.20476 -8.42100  -8.55022  0.478 31.21560 ?  94  ASP   A CB   1 
ATOM   1347 C  CB   B ASP   A 1 91  ? 26.22086 -8.35981  -8.57717  0.522 31.45172 ?  94  ASP   A CB   1 
ATOM   1348 C  CG   A ASP   A 1 91  ? 27.25909 -8.81606  -9.57219  0.478 34.72786 ?  94  ASP   A CG   1 
ATOM   1349 C  CG   B ASP   A 1 91  ? 26.50152 -9.62107  -7.81026  0.522 34.27672 ?  94  ASP   A CG   1 
ATOM   1350 O  OD1  A ASP   A 1 91  ? 26.94231 -9.58613  -10.50387 0.478 35.39251 ?  94  ASP   A OD1  1 
ATOM   1351 O  OD1  B ASP   A 1 91  ? 25.58131 -10.44534 -7.66825  0.522 35.12168 ?  94  ASP   A OD1  1 
ATOM   1352 O  OD2  A ASP   A 1 91  ? 28.41399 -8.36082  -9.43295  0.478 36.87600 ?  94  ASP   A OD2  1 
ATOM   1353 O  OD2  B ASP   A 1 91  ? 27.64780 -9.78095  -7.34129  0.522 35.86803 ?  94  ASP   A OD2  1 
ATOM   1354 H  H    . ASP   A 1 91  ? 25.17567 -6.45172  -9.65709  1.000 32.12151 ?  94  ASP   A H    1 
ATOM   1355 H  HA   . ASP   A 1 91  ? 24.67487 -9.08381  -9.72645  1.000 33.48191 ?  94  ASP   A HA   1 
ATOM   1356 H  HB2  A ASP   A 1 91  ? 26.45489 -7.55986  -8.18037  0.478 37.45872 ?  94  ASP   A HB2  1 
ATOM   1357 H  HB2  B ASP   A 1 91  ? 26.85777 -8.30590  -9.30679  0.522 37.74206 ?  94  ASP   A HB2  1 
ATOM   1358 H  HB3  A ASP   A 1 91  ? 26.19942 -9.09340  -7.85111  0.478 37.45872 ?  94  ASP   A HB3  1 
ATOM   1359 H  HB3  B ASP   A 1 91  ? 26.34308 -7.61003  -7.97402  0.522 37.74206 ?  94  ASP   A HB3  1 
ATOM   1360 N  N    . THR   A 1 92  ? 22.56285 -8.82100  -8.39709  1.000 24.45113 ?  95  THR   A N    1 
ATOM   1361 C  CA   . THR   A 1 92  ? 21.40775 -8.77539  -7.51787  1.000 21.89968 ?  95  THR   A CA   1 
ATOM   1362 C  C    . THR   A 1 92  ? 21.03321 -10.17293 -7.02820  1.000 21.68080 ?  95  THR   A C    1 
ATOM   1363 O  O    . THR   A 1 92  ? 20.99841 -11.12974 -7.81210  1.000 24.06485 ?  95  THR   A O    1 
ATOM   1364 C  CB   . THR   A 1 92  ? 20.17199 -8.15452  -8.18581  1.000 20.92175 ?  95  THR   A CB   1 
ATOM   1365 O  OG1  . THR   A 1 92  ? 19.05328 -8.32147  -7.30886  1.000 19.34491 ?  95  THR   A OG1  1 
ATOM   1366 C  CG2  . THR   A 1 92  ? 19.85924 -8.81930  -9.52222  1.000 23.55656 ?  95  THR   A CG2  1 
ATOM   1367 H  H    . THR   A 1 92  ? 22.41080 -9.21949  -9.14387  1.000 29.34136 ?  95  THR   A H    1 
ATOM   1368 H  HA   . THR   A 1 92  ? 21.64347 -8.21921  -6.75893  1.000 26.27962 ?  95  THR   A HA   1 
ATOM   1369 H  HB   . THR   A 1 92  ? 20.33796 -7.21493  -8.36051  1.000 25.10610 ?  95  THR   A HB   1 
ATOM   1370 H  HG1  . THR   A 1 92  ? 19.16724 -7.87129  -6.60889  1.000 23.21389 ?  95  THR   A HG1  1 
ATOM   1371 H  HG21 . THR   A 1 92  ? 19.14479 -8.34113  -9.97147  1.000 28.26787 ?  95  THR   A HG21 1 
ATOM   1372 H  HG22 . THR   A 1 92  ? 20.64689 -8.81288  -10.08832 1.000 28.26787 ?  95  THR   A HG22 1 
ATOM   1373 H  HG23 . THR   A 1 92  ? 19.58194 -9.73772  -9.37905  1.000 28.26787 ?  95  THR   A HG23 1 
ATOM   1374 N  N    . PRO   A 1 93  ? 20.72036 -10.31015 -5.74289  1.000 21.14335 ?  96  PRO   A N    1 
ATOM   1375 C  CA   . PRO   A 1 93  ? 20.32343 -11.60780 -5.19244  1.000 21.99277 ?  96  PRO   A CA   1 
ATOM   1376 C  C    . PRO   A 1 93  ? 18.82923 -11.86115 -5.24872  1.000 21.06496 ?  96  PRO   A C    1 
ATOM   1377 O  O    . PRO   A 1 93  ? 18.39051 -12.94482 -4.84427  1.000 23.84460 ?  96  PRO   A O    1 
ATOM   1378 C  CB   . PRO   A 1 93  ? 20.76942 -11.47147 -3.73459  1.000 23.37233 ?  96  PRO   A CB   1 
ATOM   1379 C  CG   . PRO   A 1 93  ? 20.52503 -10.04063 -3.43383  1.000 22.96500 ?  96  PRO   A CG   1 
ATOM   1380 C  CD   . PRO   A 1 93  ? 20.86424 -9.28427  -4.69160  1.000 21.94528 ?  96  PRO   A CD   1 
ATOM   1381 H  HA   . PRO   A 1 93  ? 20.80235 -12.33572 -5.61866  1.000 26.39133 ?  96  PRO   A HA   1 
ATOM   1382 H  HB2  . PRO   A 1 93  ? 20.23720 -12.04802 -3.16431  1.000 28.04679 ?  96  PRO   A HB2  1 
ATOM   1383 H  HB3  . PRO   A 1 93  ? 21.70931 -11.69497 -3.64769  1.000 28.04679 ?  96  PRO   A HB3  1 
ATOM   1384 H  HG2  . PRO   A 1 93  ? 19.59312 -9.91178  -3.19753  1.000 27.55800 ?  96  PRO   A HG2  1 
ATOM   1385 H  HG3  . PRO   A 1 93  ? 21.09502 -9.75962  -2.70099  1.000 27.55800 ?  96  PRO   A HG3  1 
ATOM   1386 H  HD2  . PRO   A 1 93  ? 20.24360 -8.55256  -4.83408  1.000 26.33434 ?  96  PRO   A HD2  1 
ATOM   1387 H  HD3  . PRO   A 1 93  ? 21.77305 -8.94680  -4.65868  1.000 26.33434 ?  96  PRO   A HD3  1 
ATOM   1388 N  N    . PHE   A 1 94  ? 18.04299 -10.88623 -5.68752  1.000 18.13910 ?  97  PHE   A N    1 
ATOM   1389 C  CA   . PHE   A 1 94  ? 16.59934 -11.02703 -5.68337  1.000 17.72944 ?  97  PHE   A CA   1 
ATOM   1390 C  C    . PHE   A 1 94  ? 16.13939 -11.74478 -6.93721  1.000 18.35277 ?  97  PHE   A C    1 
ATOM   1391 O  O    . PHE   A 1 94  ? 16.69193 -11.54004 -8.01760  1.000 20.90430 ?  97  PHE   A O    1 
ATOM   1392 C  CB   . PHE   A 1 94  ? 15.94393 -9.65056  -5.62771  1.000 16.55644 ?  97  PHE   A CB   1 
ATOM   1393 C  CG   . PHE   A 1 94  ? 16.26346 -8.88486  -4.37487  1.000 15.35425 ?  97  PHE   A CG   1 
ATOM   1394 C  CD1  . PHE   A 1 94  ? 15.61846 -9.17635  -3.16519  1.000 15.62786 ?  97  PHE   A CD1  1 
ATOM   1395 C  CD2  . PHE   A 1 94  ? 17.21826 -7.88554  -4.39590  1.000 15.70737 ?  97  PHE   A CD2  1 
ATOM   1396 C  CE1  . PHE   A 1 94  ? 15.91745 -8.46970  -2.01027  1.000 15.24194 ?  97  PHE   A CE1  1 
ATOM   1397 C  CE2  . PHE   A 1 94  ? 17.51437 -7.17481  -3.23437  1.000 14.89975 ?  97  PHE   A CE2  1 
ATOM   1398 C  CZ   . PHE   A 1 94  ? 16.86598 -7.47941  -2.03567  1.000 15.00176 ?  97  PHE   A CZ   1 
ATOM   1399 H  H    . PHE   A 1 94  ? 18.32422 -10.13300 -5.99274  1.000 21.76692 ?  97  PHE   A H    1 
ATOM   1400 H  HA   . PHE   A 1 94  ? 16.32454 -11.54113 -4.90808  1.000 21.27533 ?  97  PHE   A HA   1 
ATOM   1401 H  HB2  . PHE   A 1 94  ? 16.25257 -9.12630  -6.38321  1.000 19.86773 ?  97  PHE   A HB2  1 
ATOM   1402 H  HB3  . PHE   A 1 94  ? 14.98116 -9.76047  -5.67135  1.000 19.86773 ?  97  PHE   A HB3  1 
ATOM   1403 H  HD1  . PHE   A 1 94  ? 14.98115 -9.85305  -3.13673  1.000 18.75344 ?  97  PHE   A HD1  1 
ATOM   1404 H  HD2  . PHE   A 1 94  ? 17.66428 -7.68695  -5.18743  1.000 18.84884 ?  97  PHE   A HD2  1 
ATOM   1405 H  HE1  . PHE   A 1 94  ? 15.47406 -8.66757  -1.21708  1.000 18.29032 ?  97  PHE   A HE1  1 
ATOM   1406 H  HE2  . PHE   A 1 94  ? 18.14733 -6.49385  -3.25764  1.000 17.87970 ?  97  PHE   A HE2  1 
ATOM   1407 H  HZ   . PHE   A 1 94  ? 17.07620 -7.01331  -1.25884  1.000 18.00211 ?  97  PHE   A HZ   1 
ATOM   1408 N  N    . LYS   A 1 95  ? 15.12256 -12.59085 -6.78568  1.000 17.53005 ?  98  LYS   A N    1 
ATOM   1409 C  CA   . LYS   A 1 95  ? 14.48889 -13.25965 -7.90940  1.000 19.41850 ?  98  LYS   A CA   1 
ATOM   1410 C  C    . LYS   A 1 95  ? 13.01629 -13.45904 -7.59881  1.000 18.79073 ?  98  LYS   A C    1 
ATOM   1411 O  O    . LYS   A 1 95  ? 12.61899 -13.60077 -6.43540  1.000 18.53946 ?  98  LYS   A O    1 
ATOM   1412 C  CB   . LYS   A 1 95  ? 15.07247 -14.65904 -8.13995  1.000 23.31546 ?  98  LYS   A CB   1 
ATOM   1413 C  CG   . LYS   A 1 95  ? 16.46698 -14.66954 -8.70480  1.000 27.27508 ?  98  LYS   A CG   1 
ATOM   1414 C  CD   . LYS   A 1 95  ? 16.49768 -14.11098 -10.13040 1.000 32.50641 ?  98  LYS   A CD   1 
ATOM   1415 C  CE   . LYS   A 1 95  ? 17.83288 -14.33109 -10.82354 1.000 37.31987 ?  98  LYS   A CE   1 
ATOM   1416 N  NZ   . LYS   A 1 95  ? 18.55117 -15.53258 -10.34383 1.000 39.83343 ?  98  LYS   A NZ   1 
ATOM   1417 H  H    . LYS   A 1 95  ? 14.77727 -12.79576 -6.02516  1.000 21.03606 ?  98  LYS   A H    1 
ATOM   1418 H  HA   . LYS   A 1 95  ? 14.60708 -12.70464 -8.69609  1.000 23.30220 ?  98  LYS   A HA   1 
ATOM   1419 H  HB2  . LYS   A 1 95  ? 15.09709 -15.12702 -7.29066  1.000 27.97855 ?  98  LYS   A HB2  1 
ATOM   1420 H  HB3  . LYS   A 1 95  ? 14.50044 -15.13318 -8.76354  1.000 27.97855 ?  98  LYS   A HB3  1 
ATOM   1421 H  HG2  . LYS   A 1 95  ? 17.04289 -14.12087 -8.14967  1.000 32.73009 ?  98  LYS   A HG2  1 
ATOM   1422 H  HG3  . LYS   A 1 95  ? 16.79802 -15.58104 -8.72705  1.000 32.73009 ?  98  LYS   A HG3  1 
ATOM   1423 H  HD2  . LYS   A 1 95  ? 15.81162 -14.55047 -10.65677 1.000 39.00769 ?  98  LYS   A HD2  1 
ATOM   1424 H  HD3  . LYS   A 1 95  ? 16.33098 -13.15592 -10.09918 1.000 39.00769 ?  98  LYS   A HD3  1 
ATOM   1425 H  HE2  . LYS   A 1 95  ? 17.67897 -14.43702 -11.77537 1.000 44.78384 ?  98  LYS   A HE2  1 
ATOM   1426 H  HE3  . LYS   A 1 95  ? 18.40082 -13.56132 -10.66295 1.000 44.78384 ?  98  LYS   A HE3  1 
ATOM   1427 H  HZ1  . LYS   A 1 95  ? 19.23361 -15.71558 -10.88503 1.000 47.80011 ?  98  LYS   A HZ1  1 
ATOM   1428 H  HZ2  . LYS   A 1 95  ? 18.86354 -15.39271 -9.52226  1.000 47.80011 ?  98  LYS   A HZ2  1 
ATOM   1429 H  HZ3  . LYS   A 1 95  ? 17.99966 -16.23093 -10.32815 1.000 47.80011 ?  98  LYS   A HZ3  1 
ATOM   1430 N  N    . ARG   A 1 96  ? 12.21354 -13.49153 -8.65010  1.000 18.98964 ?  99  ARG   A N    1 
ATOM   1431 C  CA   . ARG   A 1 96  ? 10.82447 -13.88101 -8.51449  1.000 18.89650 ?  99  ARG   A CA   1 
ATOM   1432 C  C    . ARG   A 1 96  ? 10.70791 -15.24723 -7.85125  1.000 17.98719 ?  99  ARG   A C    1 
ATOM   1433 O  O    . ARG   A 1 96  ? 11.43687 -16.19538 -8.16533  1.000 19.87375 ?  99  ARG   A O    1 
ATOM   1434 C  CB   . ARG   A 1 96  ? 10.15147 -13.89345 -9.88881  1.000 19.30635 ?  99  ARG   A CB   1 
ATOM   1435 C  CG   . ARG   A 1 96  ? 9.95961  -12.52851 -10.49461 1.000 20.47702 ?  99  ARG   A CG   1 
ATOM   1436 C  CD   . ARG   A 1 96  ? 9.69223  -12.63775 -11.98042 1.000 21.97040 ?  99  ARG   A CD   1 
ATOM   1437 N  NE   . ARG   A 1 96  ? 9.43665  -11.32840 -12.55808 1.000 22.93651 ?  99  ARG   A NE   1 
ATOM   1438 C  CZ   . ARG   A 1 96  ? 9.81639  -10.94404 -13.76831 1.000 26.03751 ?  99  ARG   A CZ   1 
ATOM   1439 N  NH1  . ARG   A 1 96  ? 10.46807 -11.76077 -14.58079 1.000 29.72388 ?  99  ARG   A NH1  1 
ATOM   1440 N  NH2  . ARG   A 1 96  ? 9.54510  -9.70359  -14.16726 1.000 27.24541 ?  99  ARG   A NH2  1 
ATOM   1441 H  H    . ARG   A 1 96  ? 12.44977 -13.29239 -9.45268  1.000 22.78757 ?  99  ARG   A H    1 
ATOM   1442 H  HA   . ARG   A 1 96  ? 10.36099 -13.23833 -7.95497  1.000 22.67580 ?  99  ARG   A HA   1 
ATOM   1443 H  HB2  . ARG   A 1 96  ? 10.70045 -14.41130 -10.49820 1.000 23.16762 ?  99  ARG   A HB2  1 
ATOM   1444 H  HB3  . ARG   A 1 96  ? 9.27620  -14.30239 -9.80173  1.000 23.16762 ?  99  ARG   A HB3  1 
ATOM   1445 H  HG2  . ARG   A 1 96  ? 9.20173  -12.09112 -10.07603 1.000 24.57242 ?  99  ARG   A HG2  1 
ATOM   1446 H  HG3  . ARG   A 1 96  ? 10.76197 -11.99942 -10.36354 1.000 24.57242 ?  99  ARG   A HG3  1 
ATOM   1447 H  HD2  . ARG   A 1 96  ? 10.46593 -13.02276 -12.42093 1.000 26.36448 ?  99  ARG   A HD2  1 
ATOM   1448 H  HD3  . ARG   A 1 96  ? 8.91360  -13.19688 -12.12878 1.000 26.36448 ?  99  ARG   A HD3  1 
ATOM   1449 H  HE   . ARG   A 1 96  ? 9.00607  -10.75967 -12.07772 1.000 27.52382 ?  99  ARG   A HE   1 
ATOM   1450 H  HH11 . ARG   A 1 96  ? 10.65430 -12.56118 -14.32732 1.000 35.66866 ?  99  ARG   A HH11 1 
ATOM   1451 H  HH12 . ARG   A 1 96  ? 10.70529 -11.49102 -15.36218 1.000 35.66866 ?  99  ARG   A HH12 1 
ATOM   1452 H  HH21 . ARG   A 1 96  ? 9.12903  -9.16434  -13.64220 1.000 32.69449 ?  99  ARG   A HH21 1 
ATOM   1453 H  HH22 . ARG   A 1 96  ? 9.78588  -9.44133  -14.95010 1.000 32.69449 ?  99  ARG   A HH22 1 
ATOM   1454 N  N    . GLU   A 1 97  ? 9.75618  -15.32164 -6.92984  1.000 17.47455 ?  100 GLU   A N    1 
ATOM   1455 C  CA   . GLU   A 1 97  ? 9.44043  -16.52206 -6.18165  1.000 17.50559 ?  100 GLU   A CA   1 
ATOM   1456 C  C    . GLU   A 1 97  ? 10.60848 -16.98218 -5.32174  1.000 18.61634 ?  100 GLU   A C    1 
ATOM   1457 O  O    . GLU   A 1 97  ? 10.81400 -18.18297 -5.12800  1.000 21.80691 ?  100 GLU   A O    1 
ATOM   1458 C  CB   . GLU   A 1 97  ? 8.96836  -17.63991 -7.11346  1.000 18.64562 ?  100 GLU   A CB   1 
ATOM   1459 C  CG   . GLU   A 1 97  ? 8.18075  -18.72308 -6.43162  1.000 21.78652 ?  100 GLU   A CG   1 
ATOM   1460 C  CD   . GLU   A 1 97  ? 6.87674  -18.23511 -5.88043  1.000 25.68910 ?  100 GLU   A CD   1 
ATOM   1461 O  OE1  . GLU   A 1 97  ? 5.87197  -18.19344 -6.62234  1.000 27.65312 ?  100 GLU   A OE1  1 
ATOM   1462 O  OE2  . GLU   A 1 97  ? 6.86421  -17.86760 -4.69666  1.000 31.76110 ?  100 GLU   A OE2  1 
ATOM   1463 H  H    . GLU   A 1 97  ? 9.25728  -14.65586 -6.71209  1.000 20.96946 ?  100 GLU   A H    1 
ATOM   1464 H  HA   . GLU   A 1 97  ? 8.71327  -16.31900 -5.57263  1.000 21.00671 ?  100 GLU   A HA   1 
ATOM   1465 H  HB2  . GLU   A 1 97  ? 8.40237  -17.25272 -7.79949  1.000 22.37474 ?  100 GLU   A HB2  1 
ATOM   1466 H  HB3  . GLU   A 1 97  ? 9.74612  -18.05357 -7.51951  1.000 22.37474 ?  100 GLU   A HB3  1 
ATOM   1467 H  HG2  . GLU   A 1 97  ? 7.99076  -19.42620 -7.07226  1.000 26.14382 ?  100 GLU   A HG2  1 
ATOM   1468 H  HG3  . GLU   A 1 97  ? 8.70329  -19.07751 -5.69526  1.000 26.14382 ?  100 GLU   A HG3  1 
ATOM   1469 N  N    . LYS   A 1 98  ? 11.39166 -16.04897 -4.80659  1.000 17.29714 ?  101 LYS   A N    1 
ATOM   1470 C  CA   . LYS   A 1 98  ? 12.48974 -16.32643 -3.89468  1.000 17.46958 ?  101 LYS   A CA   1 
ATOM   1471 C  C    . LYS   A 1 98  ? 12.39109 -15.43298 -2.65820  1.000 16.44284 ?  101 LYS   A C    1 
ATOM   1472 O  O    . LYS   A 1 98  ? 12.01603 -14.26027 -2.74484  1.000 16.45918 ?  101 LYS   A O    1 
ATOM   1473 C  CB   . LYS   A 1 98  ? 13.82731 -16.10294 -4.61234  1.000 19.23638 ?  101 LYS   A CB   1 
ATOM   1474 C  CG   . LYS   A 1 98  ? 15.05682 -16.38385 -3.80389  1.000 22.33611 ?  101 LYS   A CG   1 
ATOM   1475 C  CD   . LYS   A 1 98  ? 16.32306 -16.08395 -4.61416  1.000 25.57684 ?  101 LYS   A CD   1 
ATOM   1476 C  CE   . LYS   A 1 98  ? 17.57574 -16.30739 -3.79228  1.000 27.09693 ?  101 LYS   A CE   1 
ATOM   1477 N  NZ   . LYS   A 1 98  ? 18.79634 -15.81716 -4.49408  1.000 29.33259 ?  101 LYS   A NZ   1 
ATOM   1478 H  H    . LYS   A 1 98  ? 11.30363 -15.21069 -4.97727  1.000 20.75657 ?  101 LYS   A H    1 
ATOM   1479 H  HA   . LYS   A 1 98  ? 12.44373 -17.24352 -3.58207  1.000 20.96350 ?  101 LYS   A HA   1 
ATOM   1480 H  HB2  . LYS   A 1 98  ? 13.85572 -16.68293 -5.38932  1.000 23.08366 ?  101 LYS   A HB2  1 
ATOM   1481 H  HB3  . LYS   A 1 98  ? 13.87179 -15.17448 -4.88961  1.000 23.08366 ?  101 LYS   A HB3  1 
ATOM   1482 H  HG2  . LYS   A 1 98  ? 15.05856 -15.82371 -3.01197  1.000 26.80333 ?  101 LYS   A HG2  1 
ATOM   1483 H  HG3  . LYS   A 1 98  ? 15.06955 -17.31953 -3.54845  1.000 26.80333 ?  101 LYS   A HG3  1 
ATOM   1484 H  HD2  . LYS   A 1 98  ? 16.35664 -16.67029 -5.38615  1.000 30.69221 ?  101 LYS   A HD2  1 
ATOM   1485 H  HD3  . LYS   A 1 98  ? 16.30849 -15.15761 -4.90151  1.000 30.69221 ?  101 LYS   A HD3  1 
ATOM   1486 H  HE2  . LYS   A 1 98  ? 17.49625 -15.82914 -2.95213  1.000 32.51632 ?  101 LYS   A HE2  1 
ATOM   1487 H  HE3  . LYS   A 1 98  ? 17.68291 -17.25678 -3.62475  1.000 32.51632 ?  101 LYS   A HE3  1 
ATOM   1488 H  HZ1  . LYS   A 1 98  ? 19.47340 -15.75504 -3.91977  1.000 35.19911 ?  101 LYS   A HZ1  1 
ATOM   1489 H  HZ2  . LYS   A 1 98  ? 19.02050 -16.38129 -5.14493  1.000 35.19911 ?  101 LYS   A HZ2  1 
ATOM   1490 H  HZ3  . LYS   A 1 98  ? 18.64277 -15.01486 -4.84740  1.000 35.19911 ?  101 LYS   A HZ3  1 
ATOM   1491 N  N    . SER   A 1 99  ? 12.76335 -15.98790 -1.50633  1.000 16.12428 ?  102 SER   A N    1 
ATOM   1492 C  CA   . SER   A 1 99  ? 12.75587 -15.27307 -0.24120  1.000 16.14054 ?  102 SER   A CA   1 
ATOM   1493 C  C    . SER   A 1 99  ? 14.07052 -14.54445 -0.01984  1.000 15.84359 ?  102 SER   A C    1 
ATOM   1494 O  O    . SER   A 1 99  ? 15.10606 -14.87407 -0.61136  1.000 19.29642 ?  102 SER   A O    1 
ATOM   1495 C  CB   . SER   A 1 99  ? 12.54736 -16.25203 0.90337   1.000 19.75117 ?  102 SER   A CB   1 
ATOM   1496 O  OG   . SER   A 1 99  ? 11.28542 -16.85719 0.79827   1.000 22.71792 ?  102 SER   A OG   1 
ATOM   1497 H  H    . SER   A 1 99  ? 13.03170 -16.80171 -1.43353  1.000 19.34914 ?  102 SER   A H    1 
ATOM   1498 H  HA   . SER   A 1 99  ? 12.03730 -14.62157 -0.25171  1.000 19.36865 ?  102 SER   A HA   1 
ATOM   1499 H  HB2  . SER   A 1 99  ? 13.23318 -16.93695 0.86561   1.000 23.70141 ?  102 SER   A HB2  1 
ATOM   1500 H  HB3  . SER   A 1 99  ? 12.60211 -15.77379 1.74550   1.000 23.70141 ?  102 SER   A HB3  1 
ATOM   1501 H  HG   . SER   A 1 99  ? 11.31058 -17.47773 0.23268   1.000 27.26150 ?  102 SER   A HG   1 
ATOM   1502 N  N    . PHE   A 1 100 ? 14.01734 -13.55322 0.86380   1.000 14.70309 ?  103 PHE   A N    1 
ATOM   1503 C  CA   . PHE   A 1 100 ? 15.17342 -12.73414 1.16088   1.000 14.90175 ?  103 PHE   A CA   1 
ATOM   1504 C  C    . PHE   A 1 100 ? 15.14623 -12.24637 2.59985   1.000 13.94001 ?  103 PHE   A C    1 
ATOM   1505 O  O    . PHE   A 1 100 ? 14.09527 -12.13899 3.23839   1.000 14.06439 ?  103 PHE   A O    1 
ATOM   1506 C  CB   . PHE   A 1 100 ? 15.25544 -11.52040 0.22291   1.000 15.75613 ?  103 PHE   A CB   1 
ATOM   1507 C  CG   . PHE   A 1 100 ? 14.04082 -10.63053 0.29194   1.000 14.01996 ?  103 PHE   A CG   1 
ATOM   1508 C  CD1  . PHE   A 1 100 ? 13.90457 -9.69895  1.32092   1.000 14.48496 ?  103 PHE   A CD1  1 
ATOM   1509 C  CD2  . PHE   A 1 100 ? 13.03519 -10.71350 -0.65781  1.000 14.49719 ?  103 PHE   A CD2  1 
ATOM   1510 C  CE1  . PHE   A 1 100 ? 12.78385 -8.88345  1.39479   1.000 15.15440 ?  103 PHE   A CE1  1 
ATOM   1511 C  CE2  . PHE   A 1 100 ? 11.91463 -9.89240  -0.58882  1.000 14.32954 ?  103 PHE   A CE2  1 
ATOM   1512 C  CZ   . PHE   A 1 100 ? 11.78279 -8.98356  0.45251   1.000 15.04860 ?  103 PHE   A CZ   1 
ATOM   1513 H  H    . PHE   A 1 100 ? 13.31275 -13.33677 1.30685   1.000 17.64371 ?  103 PHE   A H    1 
ATOM   1514 H  HA   . PHE   A 1 100 ? 15.95970 -13.29213 1.05454   1.000 17.88210 ?  103 PHE   A HA   1 
ATOM   1515 H  HB2  . PHE   A 1 100 ? 16.02909 -10.98804 0.46575   1.000 18.90736 ?  103 PHE   A HB2  1 
ATOM   1516 H  HB3  . PHE   A 1 100 ? 15.34276 -11.83515 -0.69044  1.000 18.90736 ?  103 PHE   A HB3  1 
ATOM   1517 H  HD1  . PHE   A 1 100 ? 14.57175 -9.62337  1.96440   1.000 17.38195 ?  103 PHE   A HD1  1 
ATOM   1518 H  HD2  . PHE   A 1 100 ? 13.11069 -11.32768 -1.35206  1.000 17.39663 ?  103 PHE   A HD2  1 
ATOM   1519 H  HE1  . PHE   A 1 100 ? 12.70777 -8.26495  2.08513   1.000 18.18527 ?  103 PHE   A HE1  1 
ATOM   1520 H  HE2  . PHE   A 1 100 ? 11.25363 -9.95215  -1.24028  1.000 17.19545 ?  103 PHE   A HE2  1 
ATOM   1521 H  HZ   . PHE   A 1 100 ? 11.02566 -8.44700  0.51374   1.000 18.05832 ?  103 PHE   A HZ   1 
ATOM   1522 N  N    . GLU   A 1 101 ? 16.33796 -11.90795 3.08484   1.000 15.34610 ?  104 GLU   A N    1 
ATOM   1523 C  CA   . GLU   A 1 101 ? 16.53320 -11.09515 4.28056   1.000 14.69147 ?  104 GLU   A CA   1 
ATOM   1524 C  C    . GLU   A 1 101 ? 17.47700 -9.94713  3.93833   1.000 15.45510 ?  104 GLU   A C    1 
ATOM   1525 O  O    . GLU   A 1 101 ? 18.65277 -10.18124 3.62921   1.000 16.85779 ?  104 GLU   A O    1 
ATOM   1526 C  CB   . GLU   A 1 101 ? 17.08334 -11.91724 5.45727   1.000 16.69167 ?  104 GLU   A CB   1 
ATOM   1527 C  CG   . GLU   A 1 101 ? 17.35521 -11.05729 6.68681   1.000 19.66152 ?  104 GLU   A CG   1 
ATOM   1528 C  CD   . GLU   A 1 101 ? 17.62988 -11.85502 7.95230   1.000 24.62255 ?  104 GLU   A CD   1 
ATOM   1529 O  OE1  . GLU   A 1 101 ? 16.67660 -12.24973 8.65530   1.000 28.50884 ?  104 GLU   A OE1  1 
ATOM   1530 O  OE2  . GLU   A 1 101 ? 18.81254 -12.07565 8.25936   1.000 29.61851 ?  104 GLU   A OE2  1 
ATOM   1531 H  H    . GLU   A 1 101 ? 17.08003 -12.14798 2.72245   1.000 18.41532 ?  104 GLU   A H    1 
ATOM   1532 H  HA   . GLU   A 1 101 ? 15.67850 -10.72678 4.55386   1.000 17.62976 ?  104 GLU   A HA   1 
ATOM   1533 H  HB2  . GLU   A 1 101 ? 16.43488 -12.59633 5.70068   1.000 20.03000 ?  104 GLU   A HB2  1 
ATOM   1534 H  HB3  . GLU   A 1 101 ? 17.91699 -12.33511 5.19026   1.000 20.03000 ?  104 GLU   A HB3  1 
ATOM   1535 H  HG2  . GLU   A 1 101 ? 18.13234 -10.50331 6.51342   1.000 23.59382 ?  104 GLU   A HG2  1 
ATOM   1536 H  HG3  . GLU   A 1 101 ? 16.57998 -10.49856 6.85335   1.000 23.59382 ?  104 GLU   A HG3  1 
ATOM   1537 N  N    . ILE   A 1 102 ? 16.96377 -8.71318  4.00584   1.000 13.66000 ?  105 ILE   A N    1 
ATOM   1538 C  CA   . ILE   A 1 102 ? 17.73554 -7.49813  3.77585   1.000 12.90750 ?  105 ILE   A CA   1 
ATOM   1539 C  C    . ILE   A 1 102 ? 18.17654 -6.97598  5.13142   1.000 12.45498 ?  105 ILE   A C    1 
ATOM   1540 O  O    . ILE   A 1 102 ? 17.34560 -6.82291  6.04106   1.000 14.11385 ?  105 ILE   A O    1 
ATOM   1541 C  CB   . ILE   A 1 102 ? 16.88152 -6.42591  3.07204   1.000 13.24209 ?  105 ILE   A CB   1 
ATOM   1542 C  CG1  . ILE   A 1 102 ? 16.36767 -6.90270  1.71400   1.000 14.14257 ?  105 ILE   A CG1  1 
ATOM   1543 C  CG2  . ILE   A 1 102 ? 17.64842 -5.11234  2.97540   1.000 15.55318 ?  105 ILE   A CG2  1 
ATOM   1544 C  CD1  . ILE   A 1 102 ? 15.19406 -6.09562  1.19139   1.000 13.94845 ?  105 ILE   A CD1  1 
ATOM   1545 H  H    . ILE   A 1 102 ? 16.13905 -8.55418  4.19062   1.000 16.39200 ?  105 ILE   A H    1 
ATOM   1546 H  HA   . ILE   A 1 102 ? 18.50848 -7.70315  3.22682   1.000 15.48900 ?  105 ILE   A HA   1 
ATOM   1547 H  HB   . ILE   A 1 102 ? 16.09328 -6.26919  3.61520   1.000 15.89050 ?  105 ILE   A HB   1 
ATOM   1548 H  HG12 . ILE   A 1 102 ? 17.08656 -6.83454  1.06636   1.000 16.97109 ?  105 ILE   A HG12 1 
ATOM   1549 H  HG13 . ILE   A 1 102 ? 16.08051 -7.82567  1.79500   1.000 16.97109 ?  105 ILE   A HG13 1 
ATOM   1550 H  HG21 . ILE   A 1 102 ? 17.21347 -4.53989  2.32423   1.000 18.66381 ?  105 ILE   A HG21 1 
ATOM   1551 H  HG22 . ILE   A 1 102 ? 17.64966 -4.68266  3.84504   1.000 18.66381 ?  105 ILE   A HG22 1 
ATOM   1552 H  HG23 . ILE   A 1 102 ? 18.55884 -5.29794  2.69686   1.000 18.66381 ?  105 ILE   A HG23 1 
ATOM   1553 H  HD11 . ILE   A 1 102 ? 14.92485 -6.45120  0.33000   1.000 16.73815 ?  105 ILE   A HD11 1 
ATOM   1554 H  HD12 . ILE   A 1 102 ? 14.45933 -6.16258  1.82114   1.000 16.73815 ?  105 ILE   A HD12 1 
ATOM   1555 H  HD13 . ILE   A 1 102 ? 15.46514 -5.16909  1.09669   1.000 16.73815 ?  105 ILE   A HD13 1 
ATOM   1556 N  N    . VAL   A 1 103 ? 19.46233 -6.65082  5.25759   1.000 13.15077 ?  106 VAL   A N    1 
ATOM   1557 C  CA   . VAL   A 1 103 ? 19.97645 -5.94596  6.42102   1.000 12.62079 ?  106 VAL   A CA   1 
ATOM   1558 C  C    . VAL   A 1 103 ? 20.57568 -4.62279  5.94628   1.000 13.22027 ?  106 VAL   A C    1 
ATOM   1559 O  O    . VAL   A 1 103 ? 21.54256 -4.61356  5.17573   1.000 13.92794 ?  106 VAL   A O    1 
ATOM   1560 C  CB   . VAL   A 1 103 ? 21.00224 -6.77314  7.20388   1.000 14.61642 ?  106 VAL   A CB   1 
ATOM   1561 C  CG1  . VAL   A 1 103 ? 21.51751 -5.94638  8.37610   1.000 16.68135 ?  106 VAL   A CG1  1 
ATOM   1562 C  CG2  . VAL   A 1 103 ? 20.38612 -8.07881  7.67351   1.000 16.71780 ?  106 VAL   A CG2  1 
ATOM   1563 H  H    . VAL   A 1 103 ? 20.06297 -6.83300  4.66967   1.000 15.78092 ?  106 VAL   A H    1 
ATOM   1564 H  HA   . VAL   A 1 103 ? 19.23918 -5.74849  7.01964   1.000 15.14494 ?  106 VAL   A HA   1 
ATOM   1565 H  HB   . VAL   A 1 103 ? 21.75252 -7.00155  6.63309   1.000 17.53970 ?  106 VAL   A HB   1 
ATOM   1566 H  HG11 . VAL   A 1 103 ? 22.02517 -6.52183  8.96942   1.000 20.01762 ?  106 VAL   A HG11 1 
ATOM   1567 H  HG12 . VAL   A 1 103 ? 22.08581 -5.23729  8.03680   1.000 20.01762 ?  106 VAL   A HG12 1 
ATOM   1568 H  HG13 . VAL   A 1 103 ? 20.76182 -5.56613  8.85070   1.000 20.01762 ?  106 VAL   A HG13 1 
ATOM   1569 H  HG21 . VAL   A 1 103 ? 20.97722 -8.49151  8.32250   1.000 20.06135 ?  106 VAL   A HG21 1 
ATOM   1570 H  HG22 . VAL   A 1 103 ? 19.52553 -7.89341  8.08084   1.000 20.06135 ?  106 VAL   A HG22 1 
ATOM   1571 H  HG23 . VAL   A 1 103 ? 20.27113 -8.66628  6.91026   1.000 20.06135 ?  106 VAL   A HG23 1 
ATOM   1572 N  N    . ILE   A 1 104 ? 19.99246 -3.51077  6.39206   1.000 12.58711 ?  107 ILE   A N    1 
ATOM   1573 C  CA   . ILE   A 1 104 ? 20.50814 -2.16642  6.14473   1.000 13.00676 ?  107 ILE   A CA   1 
ATOM   1574 C  C    . ILE   A 1 104 ? 21.21645 -1.70967  7.40651   1.000 12.50419 ?  107 ILE   A C    1 
ATOM   1575 O  O    . ILE   A 1 104 ? 20.58503 -1.56663  8.45680   1.000 13.60307 ?  107 ILE   A O    1 
ATOM   1576 C  CB   . ILE   A 1 104 ? 19.39216 -1.17357  5.77355   1.000 12.94468 ?  107 ILE   A CB   1 
ATOM   1577 C  CG1  . ILE   A 1 104 ? 18.61549 -1.63953  4.54237   1.000 14.36717 ?  107 ILE   A CG1  1 
ATOM   1578 C  CG2  . ILE   A 1 104 ? 19.98332 0.20804   5.60067   1.000 13.79395 ?  107 ILE   A CG2  1 
ATOM   1579 C  CD1  . ILE   A 1 104 ? 17.33278 -0.85581  4.30616   1.000 15.86531 ?  107 ILE   A CD1  1 
ATOM   1580 H  H    . ILE   A 1 104 ? 19.26946 -3.51038  6.85775   1.000 15.10454 ?  107 ILE   A H    1 
ATOM   1581 H  HA   . ILE   A 1 104 ? 21.13902 -2.20310  5.40882   1.000 15.60811 ?  107 ILE   A HA   1 
ATOM   1582 H  HB   . ILE   A 1 104 ? 18.74664 -1.13747  6.49667   1.000 15.53361 ?  107 ILE   A HB   1 
ATOM   1583 H  HG12 . ILE   A 1 104 ? 19.17746 -1.53406  3.75882   1.000 17.24060 ?  107 ILE   A HG12 1 
ATOM   1584 H  HG13 . ILE   A 1 104 ? 18.37740 -2.57289  4.65668   1.000 17.24060 ?  107 ILE   A HG13 1 
ATOM   1585 H  HG21 . ILE   A 1 104 ? 19.31775 0.78835   5.19923   1.000 16.55274 ?  107 ILE   A HG21 1 
ATOM   1586 H  HG22 . ILE   A 1 104 ? 20.24113 0.55228   6.47012   1.000 16.55274 ?  107 ILE   A HG22 1 
ATOM   1587 H  HG23 . ILE   A 1 104 ? 20.76132 0.14880   5.02440   1.000 16.55274 ?  107 ILE   A HG23 1 
ATOM   1588 H  HD11 . ILE   A 1 104 ? 16.79195 -1.32506  3.65178   1.000 19.03837 ?  107 ILE   A HD11 1 
ATOM   1589 H  HD12 . ILE   A 1 104 ? 16.84890 -0.78221  5.14362   1.000 19.03837 ?  107 ILE   A HD12 1 
ATOM   1590 H  HD13 . ILE   A 1 104 ? 17.55884 0.02781   3.97599   1.000 19.03837 ?  107 ILE   A HD13 1 
ATOM   1591 N  N    . MET   A 1 105 ? 22.51992 -1.49315  7.30344   1.000 12.55267 ?  108 MET   A N    1 
ATOM   1592 C  CA   . MET   A 1 105 ? 23.33202 -0.98455  8.39489   1.000 12.66953 ?  108 MET   A CA   1 
ATOM   1593 C  C    . MET   A 1 105 ? 23.59982 0.49633   8.14322   1.000 12.50337 ?  108 MET   A C    1 
ATOM   1594 O  O    . MET   A 1 105 ? 24.16142 0.86993   7.11046   1.000 13.79595 ?  108 MET   A O    1 
ATOM   1595 C  CB   . MET   A 1 105 ? 24.62876 -1.78121  8.50143   1.000 13.58165 ?  108 MET   A CB   1 
ATOM   1596 C  CG   . MET   A 1 105 ? 25.54105 -1.33274  9.62698   1.000 15.02270 ?  108 MET   A CG   1 
ATOM   1597 S  SD   . MET   A 1 105 ? 26.93625 -2.44473  9.95486   1.000 17.11268 ?  108 MET   A SD   1 
ATOM   1598 C  CE   . MET   A 1 105 ? 27.72200 -2.46169  8.37338   1.000 18.05949 ?  108 MET   A CE   1 
ATOM   1599 H  H    . MET   A 1 105 ? 22.97083 -1.63879  6.58575   1.000 15.06320 ?  108 MET   A H    1 
ATOM   1600 H  HA   . MET   A 1 105 ? 22.86221 -1.07659  9.23852   1.000 15.20344 ?  108 MET   A HA   1 
ATOM   1601 H  HB2  . MET   A 1 105 ? 24.40864 -2.71344  8.65435   1.000 16.29798 ?  108 MET   A HB2  1 
ATOM   1602 H  HB3  . MET   A 1 105 ? 25.11935 -1.68826  7.66982   1.000 16.29798 ?  108 MET   A HB3  1 
ATOM   1603 H  HG2  . MET   A 1 105 ? 25.90705 -0.46346  9.40052   1.000 18.02724 ?  108 MET   A HG2  1 
ATOM   1604 H  HG3  . MET   A 1 105 ? 25.01886 -1.27074  10.44207  1.000 18.02724 ?  108 MET   A HG3  1 
ATOM   1605 H  HE1  . MET   A 1 105 ? 28.49026 -3.05281  8.40878   1.000 21.67139 ?  108 MET   A HE1  1 
ATOM   1606 H  HE2  . MET   A 1 105 ? 27.08990 -2.78014  7.71010   1.000 21.67139 ?  108 MET   A HE2  1 
ATOM   1607 H  HE3  . MET   A 1 105 ? 28.00736 -1.56122  8.15285   1.000 21.67139 ?  108 MET   A HE3  1 
ATOM   1608 N  N    . VAL   A 1 106 ? 23.19166 1.33670   9.07864   1.000 12.79279 ?  109 VAL   A N    1 
ATOM   1609 C  CA   . VAL   A 1 106 ? 23.40690 2.77665   8.98512   1.000 13.72036 ?  109 VAL   A CA   1 
ATOM   1610 C  C    . VAL   A 1 106 ? 24.78404 3.08484   9.55027   1.000 14.59375 ?  109 VAL   A C    1 
ATOM   1611 O  O    . VAL   A 1 106 ? 25.07730 2.76569   10.70758  1.000 16.31279 ?  109 VAL   A O    1 
ATOM   1612 C  CB   . VAL   A 1 106 ? 22.32685 3.54451   9.75719   1.000 15.66880 ?  109 VAL   A CB   1 
ATOM   1613 C  CG1  . VAL   A 1 106 ? 22.50414 5.03029   9.54672   1.000 16.83534 ?  109 VAL   A CG1  1 
ATOM   1614 C  CG2  . VAL   A 1 106 ? 20.95713 3.05842   9.33006   1.000 15.93447 ?  109 VAL   A CG2  1 
ATOM   1615 H  H    . VAL   A 1 106 ? 22.77868 1.09573   9.79347   1.000 15.35134 ?  109 VAL   A H    1 
ATOM   1616 H  HA   . VAL   A 1 106 ? 23.37928 3.04797   8.05424   1.000 16.46443 ?  109 VAL   A HA   1 
ATOM   1617 H  HB   . VAL   A 1 106 ? 22.40677 3.38196   10.71013  1.000 18.80256 ?  109 VAL   A HB   1 
ATOM   1618 H  HG11 . VAL   A 1 106 ? 21.65720 5.47521   9.70687   1.000 20.20241 ?  109 VAL   A HG11 1 
ATOM   1619 H  HG12 . VAL   A 1 106 ? 23.17323 5.35951   10.16707  1.000 20.20241 ?  109 VAL   A HG12 1 
ATOM   1620 H  HG13 . VAL   A 1 106 ? 22.79313 5.18772   8.63425   1.000 20.20241 ?  109 VAL   A HG13 1 
ATOM   1621 H  HG21 . VAL   A 1 106 ? 20.27992 3.59377   9.77244   1.000 19.12136 ?  109 VAL   A HG21 1 
ATOM   1622 H  HG22 . VAL   A 1 106 ? 20.87521 3.15052   8.36792   1.000 19.12136 ?  109 VAL   A HG22 1 
ATOM   1623 H  HG23 . VAL   A 1 106 ? 20.85963 2.12699   9.58269   1.000 19.12136 ?  109 VAL   A HG23 1 
ATOM   1624 N  N    . LEU   A 1 107 ? 25.65115 3.65223   8.72918   1.000 14.53740 ?  110 LEU   A N    1 
ATOM   1625 C  CA   . LEU   A 1 107 ? 26.97294 4.09365   9.15023   1.000 14.51287 ?  110 LEU   A CA   1 
ATOM   1626 C  C    . LEU   A 1 107 ? 27.04775 5.60942   9.06618   1.000 14.74469 ?  110 LEU   A C    1 
ATOM   1627 O  O    . LEU   A 1 107 ? 26.15318 6.27502   8.54053   1.000 15.21166 ?  110 LEU   A O    1 
ATOM   1628 C  CB   . LEU   A 1 107 ? 28.06400 3.43085   8.30109   1.000 14.76239 ?  110 LEU   A CB   1 
ATOM   1629 C  CG   . LEU   A 1 107 ? 28.04846 1.89566   8.29436   1.000 14.31014 ?  110 LEU   A CG   1 
ATOM   1630 C  CD1  . LEU   A 1 107 ? 29.02505 1.40433   7.23802   1.000 15.15041 ?  110 LEU   A CD1  1 
ATOM   1631 C  CD2  . LEU   A 1 107 ? 28.39677 1.33734   9.68361   1.000 15.22568 ?  110 LEU   A CD2  1 
ATOM   1632 H  H    . LEU   A 1 107 ? 25.49324 3.79761   7.89640   1.000 17.44488 ?  110 LEU   A H    1 
ATOM   1633 H  HA   . LEU   A 1 107 ? 27.13172 3.83542   10.07165  1.000 17.41544 ?  110 LEU   A HA   1 
ATOM   1634 H  HB2  . LEU   A 1 107 ? 27.95780 3.72613   7.38325   1.000 17.71486 ?  110 LEU   A HB2  1 
ATOM   1635 H  HB3  . LEU   A 1 107 ? 28.92797 3.71080   8.64180   1.000 17.71486 ?  110 LEU   A HB3  1 
ATOM   1636 H  HG   . LEU   A 1 107 ? 27.16091 1.56887   8.07905   1.000 17.17217 ?  110 LEU   A HG   1 
ATOM   1637 H  HD11 . LEU   A 1 107 ? 29.06516 0.43573   7.27114   1.000 18.18049 ?  110 LEU   A HD11 1 
ATOM   1638 H  HD12 . LEU   A 1 107 ? 28.71715 1.69297   6.36464   1.000 18.18049 ?  110 LEU   A HD12 1 
ATOM   1639 H  HD13 . LEU   A 1 107 ? 29.90147 1.77810   7.41994   1.000 18.18049 ?  110 LEU   A HD13 1 
ATOM   1640 H  HD21 . LEU   A 1 107 ? 28.42379 0.36883   9.63704   1.000 18.27082 ?  110 LEU   A HD21 1 
ATOM   1641 H  HD22 . LEU   A 1 107 ? 29.26325 1.67982   9.95345   1.000 18.27082 ?  110 LEU   A HD22 1 
ATOM   1642 H  HD23 . LEU   A 1 107 ? 27.71794 1.61926   10.31654  1.000 18.27082 ?  110 LEU   A HD23 1 
ATOM   1643 N  N    . LYS   A 1 108 ? 28.15587 6.16037   9.56508   1.000 15.32554 ?  111 LYS   A N    1 
ATOM   1644 C  CA   . LYS   A 1 108 ? 28.32434 7.61364   9.55433   1.000 15.23363 ?  111 LYS   A CA   1 
ATOM   1645 C  C    . LYS   A 1 108 ? 28.09253 8.22065   8.17381   1.000 14.76928 ?  111 LYS   A C    1 
ATOM   1646 O  O    . LYS   A 1 108 ? 27.37074 9.21004   8.03946   1.000 15.82299 ?  111 LYS   A O    1 
ATOM   1647 C  CB   . LYS   A 1 108 ? 29.71141 8.00391   10.06286  1.000 15.98188 ?  111 LYS   A CB   1 
ATOM   1648 C  CG   . LYS   A 1 108 ? 29.91500 9.51559   10.06030  1.000 17.29331 ?  111 LYS   A CG   1 
ATOM   1649 C  CD   . LYS   A 1 108 ? 31.35593 9.93793   10.38307  1.000 17.96909 ?  111 LYS   A CD   1 
ATOM   1650 C  CE   . LYS   A 1 108 ? 31.46037 11.45843  10.38033  1.000 18.58573 ?  111 LYS   A CE   1 
ATOM   1651 N  NZ   . LYS   A 1 108 ? 32.83456 11.95798  10.61600  1.000 19.36682 ?  111 LYS   A NZ   1 
ATOM   1652 H  H    . LYS   A 1 108 ? 28.81230 5.72388   9.90885   1.000 18.39065 ?  111 LYS   A H    1 
ATOM   1653 H  HA   . LYS   A 1 108 ? 27.65858 7.97856   10.15807  1.000 18.28036 ?  111 LYS   A HA   1 
ATOM   1654 H  HB2  . LYS   A 1 108 ? 29.81903 7.68440   10.97239  1.000 19.17825 ?  111 LYS   A HB2  1 
ATOM   1655 H  HB3  . LYS   A 1 108 ? 30.38486 7.60568   9.48946   1.000 19.17825 ?  111 LYS   A HB3  1 
ATOM   1656 H  HG2  . LYS   A 1 108 ? 29.69460 9.86058   9.18092   1.000 20.75197 ?  111 LYS   A HG2  1 
ATOM   1657 H  HG3  . LYS   A 1 108 ? 29.33311 9.91189   10.72757  1.000 20.75197 ?  111 LYS   A HG3  1 
ATOM   1658 H  HD2  . LYS   A 1 108 ? 31.60494 9.60957   11.26117  1.000 21.56291 ?  111 LYS   A HD2  1 
ATOM   1659 H  HD3  . LYS   A 1 108 ? 31.95983 9.58240   9.71239   1.000 21.56291 ?  111 LYS   A HD3  1 
ATOM   1660 H  HE2  . LYS   A 1 108 ? 31.16824 11.79088  9.51718   1.000 22.30288 ?  111 LYS   A HE2  1 
ATOM   1661 H  HE3  . LYS   A 1 108 ? 30.89195 11.81268  11.08198  1.000 22.30288 ?  111 LYS   A HE3  1 
ATOM   1662 H  HZ1  . LYS   A 1 108 ? 33.02417 11.92886  11.48508  1.000 23.24018 ?  111 LYS   A HZ1  1 
ATOM   1663 H  HZ2  . LYS   A 1 108 ? 32.90553 12.79877  10.33291  1.000 23.24018 ?  111 LYS   A HZ2  1 
ATOM   1664 H  HZ3  . LYS   A 1 108 ? 33.42129 11.45434  10.17533  1.000 23.24018 ?  111 LYS   A HZ3  1 
ATOM   1665 N  N    . ASP   A 1 109 ? 28.71403 7.65377   7.14436   1.000 15.14581 ?  112 ASP   A N    1 
ATOM   1666 C  CA   . ASP   A 1 109 ? 28.71747 8.27454   5.83010   1.000 15.61303 ?  112 ASP   A CA   1 
ATOM   1667 C  C    . ASP   A 1 109 ? 27.90425 7.54029   4.77757   1.000 14.87759 ?  112 ASP   A C    1 
ATOM   1668 O  O    . ASP   A 1 109 ? 27.76094 8.05550   3.66931   1.000 16.16501 ?  112 ASP   A O    1 
ATOM   1669 C  CB   . ASP   A 1 109 ? 30.15259 8.46219   5.32126   1.000 18.56603 ?  112 ASP   A CB   1 
ATOM   1670 C  CG   . ASP   A 1 109 ? 30.87727 9.55466   6.06470   1.000 24.01156 ?  112 ASP   A CG   1 
ATOM   1671 O  OD1  . ASP   A 1 109 ? 30.22918 10.52809  6.50473   1.000 26.18747 ?  112 ASP   A OD1  1 
ATOM   1672 O  OD2  . ASP   A 1 109 ? 32.10132 9.46558   6.17575   1.000 27.10458 ?  112 ASP   A OD2  1 
ATOM   1673 H  H    . ASP   A 1 109 ? 29.14075 6.90821   7.18493   1.000 18.17498 ?  112 ASP   A H    1 
ATOM   1674 H  HA   . ASP   A 1 109 ? 28.32021 9.15421   5.92634   1.000 18.73564 ?  112 ASP   A HA   1 
ATOM   1675 H  HB2  . ASP   A 1 109 ? 30.64469 7.63513   5.44253   1.000 22.27923 ?  112 ASP   A HB2  1 
ATOM   1676 H  HB3  . ASP   A 1 109 ? 30.12915 8.69947   4.38103   1.000 22.27923 ?  112 ASP   A HB3  1 
ATOM   1677 N  N    . LYS   A 1 110 ? 27.34936 6.38034   5.08564   1.000 14.65344 ?  113 LYS   A N    1 
ATOM   1678 C  CA   . LYS   A 1 110 ? 26.65690 5.58901   4.08361   1.000 14.30415 ?  113 LYS   A CA   1 
ATOM   1679 C  C    . LYS   A 1 110 ? 25.76288 4.57424   4.76854   1.000 14.23214 ?  113 LYS   A C    1 
ATOM   1680 O  O    . LYS   A 1 110 ? 25.90742 4.28327   5.96535   1.000 14.83485 ?  113 LYS   A O    1 
ATOM   1681 C  CB   . LYS   A 1 110 ? 27.66421 4.85355   3.19877   1.000 15.74565 ?  113 LYS   A CB   1 
ATOM   1682 C  CG   . LYS   A 1 110 ? 28.53902 3.88708   3.97174   1.000 20.29600 ?  113 LYS   A CG   1 
ATOM   1683 C  CD   . LYS   A 1 110 ? 29.52352 3.16404   3.06974   1.000 22.63569 ?  113 LYS   A CD   1 
ATOM   1684 C  CE   . LYS   A 1 110 ? 30.94361 3.62636   3.27406   1.000 27.16796 ?  113 LYS   A CE   1 
ATOM   1685 N  NZ   . LYS   A 1 110 ? 31.44480 3.35661   4.62042   1.000 28.41622 ?  113 LYS   A NZ   1 
ATOM   1686 H  H    . LYS   A 1 110 ? 27.35991 6.02830   5.87021   1.000 17.58413 ?  113 LYS   A H    1 
ATOM   1687 H  HA   . LYS   A 1 110 ? 26.10230 6.18018   3.55084   1.000 17.16498 ?  113 LYS   A HA   1 
ATOM   1688 H  HB2  . LYS   A 1 110 ? 27.18162 4.34784   2.52626   1.000 18.89478 ?  113 LYS   A HB2  1 
ATOM   1689 H  HB3  . LYS   A 1 110 ? 28.24265 5.50503   2.77231   1.000 18.89478 ?  113 LYS   A HB3  1 
ATOM   1690 H  HG2  . LYS   A 1 110 ? 29.04391 4.37729   4.63933   1.000 24.35520 ?  113 LYS   A HG2  1 
ATOM   1691 H  HG3  . LYS   A 1 110 ? 27.97821 3.22263   4.40173   1.000 24.35520 ?  113 LYS   A HG3  1 
ATOM   1692 H  HD2  . LYS   A 1 110 ? 29.48725 2.21327   3.25847   1.000 27.16282 ?  113 LYS   A HD2  1 
ATOM   1693 H  HD3  . LYS   A 1 110 ? 29.28473 3.32785   2.14398   1.000 27.16282 ?  113 LYS   A HD3  1 
ATOM   1694 H  HE2  . LYS   A 1 110 ? 31.51894 3.16567   2.64346   1.000 32.60156 ?  113 LYS   A HE2  1 
ATOM   1695 H  HE3  . LYS   A 1 110 ? 30.98791 4.58386   3.12528   1.000 32.60156 ?  113 LYS   A HE3  1 
ATOM   1696 H  HZ1  . LYS   A 1 110 ? 32.33325 3.30522   4.60987   1.000 34.09947 ?  113 LYS   A HZ1  1 
ATOM   1697 H  HZ2  . LYS   A 1 110 ? 31.19981 4.00987   5.17298   1.000 34.09947 ?  113 LYS   A HZ2  1 
ATOM   1698 H  HZ3  . LYS   A 1 110 ? 31.11445 2.58622   4.91952   1.000 34.09947 ?  113 LYS   A HZ3  1 
ATOM   1699 N  N    . PHE   A 1 111 ? 24.88032 3.98818   3.96514   1.000 13.79586 ?  114 PHE   A N    1 
ATOM   1700 C  CA   . PHE   A 1 111 ? 24.23777 2.72344   4.27453   1.000 13.70320 ?  114 PHE   A CA   1 
ATOM   1701 C  C    . PHE   A 1 111 ? 25.04920 1.58119   3.67445   1.000 13.34833 ?  114 PHE   A C    1 
ATOM   1702 O  O    . PHE   A 1 111 ? 25.58139 1.69443   2.55780   1.000 15.27920 ?  114 PHE   A O    1 
ATOM   1703 C  CB   . PHE   A 1 111 ? 22.83811 2.66012   3.66143   1.000 13.34702 ?  114 PHE   A CB   1 
ATOM   1704 C  CG   . PHE   A 1 111 ? 21.93462 3.76158   4.11414   1.000 13.98784 ?  114 PHE   A CG   1 
ATOM   1705 C  CD1  . PHE   A 1 111 ? 21.24538 3.69380   5.31009   1.000 14.02028 ?  114 PHE   A CD1  1 
ATOM   1706 C  CD2  . PHE   A 1 111 ? 21.75875 4.87962   3.32172   1.000 14.14947 ?  114 PHE   A CD2  1 
ATOM   1707 C  CE1  . PHE   A 1 111 ? 20.41439 4.72244   5.70076   1.000 15.25416 ?  114 PHE   A CE1  1 
ATOM   1708 C  CE2  . PHE   A 1 111 ? 20.94567 5.91791   3.71137   1.000 15.30773 ?  114 PHE   A CE2  1 
ATOM   1709 C  CZ   . PHE   A 1 111 ? 20.26591 5.84155   4.90514   1.000 14.72200 ?  114 PHE   A CZ   1 
ATOM   1710 H  H    . PHE   A 1 111 ? 24.63111 4.31715   3.21064   1.000 16.55503 ?  114 PHE   A H    1 
ATOM   1711 H  HA   . PHE   A 1 111 ? 24.17532 2.63029   5.23803   1.000 16.44384 ?  114 PHE   A HA   1 
ATOM   1712 H  HB2  . PHE   A 1 111 ? 22.91693 2.71904   2.69644   1.000 16.01642 ?  114 PHE   A HB2  1 
ATOM   1713 H  HB3  . PHE   A 1 111 ? 22.42619 1.81779   3.90984   1.000 16.01642 ?  114 PHE   A HB3  1 
ATOM   1714 H  HD1  . PHE   A 1 111 ? 21.34295 2.94754   5.85642   1.000 16.82434 ?  114 PHE   A HD1  1 
ATOM   1715 H  HD2  . PHE   A 1 111 ? 22.20088 4.93125   2.50518   1.000 16.97936 ?  114 PHE   A HD2  1 
ATOM   1716 H  HE1  . PHE   A 1 111 ? 19.95107 4.66228   6.50489   1.000 18.30499 ?  114 PHE   A HE1  1 
ATOM   1717 H  HE2  . PHE   A 1 111 ? 20.85561 6.66878   3.17009   1.000 18.36927 ?  114 PHE   A HE2  1 
ATOM   1718 H  HZ   . PHE   A 1 111 ? 19.71105 6.53775   5.17409   1.000 17.66640 ?  114 PHE   A HZ   1 
ATOM   1719 N  N    . GLN   A 1 112 ? 25.12118 0.47344   4.40865   1.000 12.58357 ?  115 GLN   A N    1 
ATOM   1720 C  CA   . GLN   A 1 112 ? 25.72536 -0.75113  3.92111   1.000 13.13420 ?  115 GLN   A CA   1 
ATOM   1721 C  C    . GLN   A 1 112 ? 24.65090 -1.82364  3.93780   1.000 13.07809 ?  115 GLN   A C    1 
ATOM   1722 O  O    . GLN   A 1 112 ? 24.05818 -2.08812  4.98522   1.000 14.71963 ?  115 GLN   A O    1 
ATOM   1723 C  CB   . GLN   A 1 112 ? 26.91939 -1.15433  4.79186   1.000 14.42196 ?  115 GLN   A CB   1 
ATOM   1724 C  CG   . GLN   A 1 112 ? 27.53337 -2.48292  4.41465   1.000 16.16835 ?  115 GLN   A CG   1 
ATOM   1725 C  CD   . GLN   A 1 112 ? 28.76513 -2.81605  5.21120   1.000 20.87405 ?  115 GLN   A CD   1 
ATOM   1726 O  OE1  . GLN   A 1 112 ? 29.58944 -1.94628  5.48967   1.000 22.80552 ?  115 GLN   A OE1  1 
ATOM   1727 N  NE2  . GLN   A 1 112 ? 28.90509 -4.08610  5.58317   1.000 24.11386 ?  115 GLN   A NE2  1 
ATOM   1728 H  H    . GLN   A 1 112 ? 24.81792 0.41109   5.21098   1.000 15.10028 ?  115 GLN   A H    1 
ATOM   1729 H  HA   . GLN   A 1 112 ? 26.04596 -0.63815  3.01263   1.000 15.76104 ?  115 GLN   A HA   1 
ATOM   1730 H  HB2  . GLN   A 1 112 ? 27.60815 -0.47644  4.70838   1.000 17.30635 ?  115 GLN   A HB2  1 
ATOM   1731 H  HB3  . GLN   A 1 112 ? 26.62495 -1.21632  5.71401   1.000 17.30635 ?  115 GLN   A HB3  1 
ATOM   1732 H  HG2  . GLN   A 1 112 ? 26.88142 -3.18480  4.56703   1.000 19.40202 ?  115 GLN   A HG2  1 
ATOM   1733 H  HG3  . GLN   A 1 112 ? 27.78230 -2.45912  3.47743   1.000 19.40202 ?  115 GLN   A HG3  1 
ATOM   1734 H  HE21 . GLN   A 1 112 ? 28.30808 -4.66593  5.36642   1.000 28.93663 ?  115 GLN   A HE21 1 
ATOM   1735 H  HE22 . GLN   A 1 112 ? 29.59254 -4.32702  6.04030   1.000 28.93663 ?  115 GLN   A HE22 1 
ATOM   1736 N  N    . VAL   A 1 113 ? 24.38415 -2.43204  2.78835   1.000 12.89376 ?  116 VAL   A N    1 
ATOM   1737 C  CA   . VAL   A 1 113 ? 23.27252 -3.36100  2.64432   1.000 13.04264 ?  116 VAL   A CA   1 
ATOM   1738 C  C    . VAL   A 1 113 ? 23.78620 -4.74554  2.30306   1.000 13.78085 ?  116 VAL   A C    1 
ATOM   1739 O  O    . VAL   A 1 113 ? 24.58463 -4.90947  1.37172   1.000 14.79964 ?  116 VAL   A O    1 
ATOM   1740 C  CB   . VAL   A 1 113 ? 22.27040 -2.89651  1.57429   1.000 12.73008 ?  116 VAL   A CB   1 
ATOM   1741 C  CG1  . VAL   A 1 113 ? 21.09784 -3.84405  1.50365   1.000 14.59766 ?  116 VAL   A CG1  1 
ATOM   1742 C  CG2  . VAL   A 1 113 ? 21.82402 -1.44926  1.84653   1.000 13.82295 ?  116 VAL   A CG2  1 
ATOM   1743 H  H    . VAL   A 1 113 ? 24.84044 -2.32023  2.06801   1.000 15.47251 ?  116 VAL   A H    1 
ATOM   1744 H  HA   . VAL   A 1 113 ? 22.82570 -3.41491  3.50359   1.000 15.65117 ?  116 VAL   A HA   1 
ATOM   1745 H  HB   . VAL   A 1 113 ? 22.70049 -2.90548  0.70490   1.000 15.27609 ?  116 VAL   A HB   1 
ATOM   1746 H  HG11 . VAL   A 1 113 ? 20.36826 -3.40928  1.03504   1.000 17.51719 ?  116 VAL   A HG11 1 
ATOM   1747 H  HG12 . VAL   A 1 113 ? 21.36701 -4.64457  1.02655   1.000 17.51719 ?  116 VAL   A HG12 1 
ATOM   1748 H  HG13 . VAL   A 1 113 ? 20.82218 -4.07312  2.40500   1.000 17.51719 ?  116 VAL   A HG13 1 
ATOM   1749 H  HG21 . VAL   A 1 113 ? 21.10007 -1.22304  1.24188   1.000 16.58754 ?  116 VAL   A HG21 1 
ATOM   1750 H  HG22 . VAL   A 1 113 ? 21.52143 -1.37968  2.76550   1.000 16.58754 ?  116 VAL   A HG22 1 
ATOM   1751 H  HG23 . VAL   A 1 113 ? 22.57574 -0.85404  1.69983   1.000 16.58754 ?  116 VAL   A HG23 1 
ATOM   1752 N  N    . ALA   A 1 114 ? 23.30810 -5.73305  3.04176   1.000 14.90091 ?  117 ALA   A N    1 
ATOM   1753 C  CA   . ALA   A 1 114 ? 23.59444 -7.13679  2.80191   1.000 15.96702 ?  117 ALA   A CA   1 
ATOM   1754 C  C    . ALA   A 1 114 ? 22.27980 -7.87838  2.68711   1.000 16.07472 ?  117 ALA   A C    1 
ATOM   1755 O  O    . ALA   A 1 114 ? 21.34025 -7.60216  3.43893   1.000 18.20595 ?  117 ALA   A O    1 
ATOM   1756 C  CB   . ALA   A 1 114 ? 24.39839 -7.74062  3.95121   1.000 18.09740 ?  117 ALA   A CB   1 
ATOM   1757 H  H    . ALA   A 1 114 ? 22.79193 -5.60966  3.71848   1.000 17.88109 ?  117 ALA   A H    1 
ATOM   1758 H  HA   . ALA   A 1 114 ? 24.10157 -7.23564  1.98096   1.000 19.16043 ?  117 ALA   A HA   1 
ATOM   1759 H  HB1  . ALA   A 1 114 ? 24.53654 -8.68498  3.77801   1.000 21.71688 ?  117 ALA   A HB1  1 
ATOM   1760 H  HB2  . ALA   A 1 114 ? 25.25355 -7.28674  4.01108   1.000 21.71688 ?  117 ALA   A HB2  1 
ATOM   1761 H  HB3  . ALA   A 1 114 ? 23.90385 -7.62478  4.77760   1.000 21.71688 ?  117 ALA   A HB3  1 
ATOM   1762 N  N    . VAL   A 1 115 ? 22.23294 -8.83605  1.77031   1.000 16.70945 ?  118 VAL   A N    1 
ATOM   1763 C  CA   . VAL   A 1 115 ? 21.04300 -9.63994  1.54109   1.000 18.40862 ?  118 VAL   A CA   1 
ATOM   1764 C  C    . VAL   A 1 115 ? 21.43189 -11.09884 1.70891   1.000 19.56394 ?  118 VAL   A C    1 
ATOM   1765 O  O    . VAL   A 1 115 ? 22.39221 -11.57179 1.08808   1.000 20.96428 ?  118 VAL   A O    1 
ATOM   1766 C  CB   . VAL   A 1 115 ? 20.42823 -9.38275  0.15478   1.000 19.64425 ?  118 VAL   A CB   1 
ATOM   1767 C  CG1  . VAL   A 1 115 ? 19.18355 -10.22383 -0.03320  1.000 21.47957 ?  118 VAL   A CG1  1 
ATOM   1768 C  CG2  . VAL   A 1 115 ? 20.11116 -7.91618  -0.01299  1.000 21.10093 ?  118 VAL   A CG2  1 
ATOM   1769 H  H    . VAL   A 1 115 ? 22.89277 -9.04193  1.25861   1.000 20.05134 ?  118 VAL   A H    1 
ATOM   1770 H  HA   . VAL   A 1 115 ? 20.37012 -9.41990  2.20420   1.000 22.09035 ?  118 VAL   A HA   1 
ATOM   1771 H  HB   . VAL   A 1 115 ? 21.06873 -9.63443  -0.52882  1.000 23.57310 ?  118 VAL   A HB   1 
ATOM   1772 H  HG11 . VAL   A 1 115 ? 18.58771 -9.77235  -0.65130  1.000 25.77548 ?  118 VAL   A HG11 1 
ATOM   1773 H  HG12 . VAL   A 1 115 ? 19.43795 -11.08875 -0.39110  1.000 25.77548 ?  118 VAL   A HG12 1 
ATOM   1774 H  HG13 . VAL   A 1 115 ? 18.74608 -10.33672 0.82515   1.000 25.77548 ?  118 VAL   A HG13 1 
ATOM   1775 H  HG21 . VAL   A 1 115 ? 19.71799 -7.77625  -0.88863  1.000 25.32112 ?  118 VAL   A HG21 1 
ATOM   1776 H  HG22 . VAL   A 1 115 ? 19.48513 -7.64743  0.67748   1.000 25.32112 ?  118 VAL   A HG22 1 
ATOM   1777 H  HG23 . VAL   A 1 115 ? 20.93141 -7.40460  0.06688   1.000 25.32112 ?  118 VAL   A HG23 1 
ATOM   1778 N  N    . ASN   A 1 116 ? 20.69756 -11.80439 2.56246   1.000 21.21444 ?  119 ASN   A N    1 
ATOM   1779 C  CA   . ASN   A 1 116 ? 20.94562 -13.22203 2.78504   1.000 24.20220 ?  119 ASN   A CA   1 
ATOM   1780 C  C    . ASN   A 1 116 ? 22.38409 -13.46582 3.24055   1.000 25.27700 ?  119 ASN   A C    1 
ATOM   1781 O  O    . ASN   A 1 116 ? 22.98908 -14.49465 2.91891   1.000 27.89526 ?  119 ASN   A O    1 
ATOM   1782 C  CB   . ASN   A 1 116 ? 20.62174 -14.04243 1.52897   1.000 25.41760 ?  119 ASN   A CB   1 
ATOM   1783 C  CG   . ASN   A 1 116 ? 19.20043 -13.83637 1.05575   1.000 27.62432 ?  119 ASN   A CG   1 
ATOM   1784 O  OD1  . ASN   A 1 116 ? 18.32940 -13.50420 1.84893   1.000 25.51913 ?  119 ASN   A OD1  1 
ATOM   1785 N  ND2  . ASN   A 1 116 ? 18.95785 -14.03775 -0.24313  1.000 31.42790 ?  119 ASN   A ND2  1 
ATOM   1786 H  H    . ASN   A 1 116 ? 20.04824 -11.48238 3.02537   1.000 25.45733 ?  119 ASN   A H    1 
ATOM   1787 H  HA   . ASN   A 1 116 ? 20.36206 -13.53340 3.49455   1.000 29.04264 ?  119 ASN   A HA   1 
ATOM   1788 H  HB2  . ASN   A 1 116 ? 21.21934 -13.77579 0.81295   1.000 30.50111 ?  119 ASN   A HB2  1 
ATOM   1789 H  HB3  . ASN   A 1 116 ? 20.74001 -14.98477 1.72620   1.000 30.50111 ?  119 ASN   A HB3  1 
ATOM   1790 H  HD21 . ASN   A 1 116 ? 19.59666 -14.27367 -0.76835  1.000 37.71348 ?  119 ASN   A HD21 1 
ATOM   1791 H  HD22 . ASN   A 1 116 ? 18.16294 -13.93142 -0.55364  1.000 37.71348 ?  119 ASN   A HD22 1 
ATOM   1792 N  N    . GLY   A 1 117 ? 22.93726 -12.52166 3.99863   1.000 25.30992 ?  120 GLY   A N    1 
ATOM   1793 C  CA   . GLY   A 1 117 ? 24.25563 -12.63539 4.58035   1.000 26.25820 ?  120 GLY   A CA   1 
ATOM   1794 C  C    . GLY   A 1 117 ? 25.40502 -12.29568 3.66454   1.000 26.44753 ?  120 GLY   A C    1 
ATOM   1795 O  O    . GLY   A 1 117 ? 26.56165 -12.49960 4.05290   1.000 30.35481 ?  120 GLY   A O    1 
ATOM   1796 H  H    . GLY   A 1 117 ? 22.54801 -11.78004 4.19380   1.000 30.37191 ?  120 GLY   A H    1 
ATOM   1797 H  HA2  . GLY   A 1 117 ? 24.30617 -12.04158 5.34568   1.000 31.50984 ?  120 GLY   A HA2  1 
ATOM   1798 H  HA3  . GLY   A 1 117 ? 24.38127 -13.54911 4.88074   1.000 31.50984 ?  120 GLY   A HA3  1 
ATOM   1799 N  N    . LYS   A 1 118 ? 25.13205 -11.83813 2.45072   1.000 23.30887 ?  121 LYS   A N    1 
ATOM   1800 C  CA   . LYS   A 1 118 ? 26.15561 -11.50642 1.46728   1.000 23.90195 ?  121 LYS   A CA   1 
ATOM   1801 C  C    . LYS   A 1 118 ? 26.07641 -10.01497 1.17329   1.000 20.97431 ?  121 LYS   A C    1 
ATOM   1802 O  O    . LYS   A 1 118 ? 24.98718 -9.46314  1.00290   1.000 20.83616 ?  121 LYS   A O    1 
ATOM   1803 C  CB   . LYS   A 1 118 ? 25.92638 -12.32451 0.18940   1.000 28.44050 ?  121 LYS   A CB   1 
ATOM   1804 C  CG   . LYS   A 1 118 ? 26.78672 -11.94424 -1.00791  1.000 33.40330 ?  121 LYS   A CG   1 
ATOM   1805 C  CD   . LYS   A 1 118 ? 26.54376 -12.90427 -2.17452  1.000 37.77823 ?  121 LYS   A CD   1 
ATOM   1806 C  CE   . LYS   A 1 118 ? 27.36049 -12.53321 -3.40649  1.000 41.23658 ?  121 LYS   A CE   1 
ATOM   1807 N  NZ   . LYS   A 1 118 ? 26.66365 -11.52530 -4.25689  1.000 44.31860 ?  121 LYS   A NZ   1 
ATOM   1808 H  H    . LYS   A 1 118 ? 24.33263 -11.70640 2.16231   1.000 27.97064 ?  121 LYS   A H    1 
ATOM   1809 H  HA   . LYS   A 1 118 ? 27.04343 -11.70006 1.80665   1.000 28.68234 ?  121 LYS   A HA   1 
ATOM   1810 H  HB2  . LYS   A 1 118 ? 26.10829 -13.25617 0.38895   1.000 34.12860 ?  121 LYS   A HB2  1 
ATOM   1811 H  HB3  . LYS   A 1 118 ? 25.00000 -12.21713 -0.07742  1.000 34.12860 ?  121 LYS   A HB3  1 
ATOM   1812 H  HG2  . LYS   A 1 118 ? 26.56244 -11.04566 -1.29625  1.000 40.08396 ?  121 LYS   A HG2  1 
ATOM   1813 H  HG3  . LYS   A 1 118 ? 27.72380 -11.98941 -0.76148  1.000 40.08396 ?  121 LYS   A HG3  1 
ATOM   1814 H  HD2  . LYS   A 1 118 ? 26.79415 -13.80200 -1.90566  1.000 45.33387 ?  121 LYS   A HD2  1 
ATOM   1815 H  HD3  . LYS   A 1 118 ? 25.60475 -12.88019 -2.41654  1.000 45.33387 ?  121 LYS   A HD3  1 
ATOM   1816 H  HE2  . LYS   A 1 118 ? 28.20928 -12.15721 -3.12527  1.000 49.48390 ?  121 LYS   A HE2  1 
ATOM   1817 H  HE3  . LYS   A 1 118 ? 27.51079 -13.32849 -3.94112  1.000 49.48390 ?  121 LYS   A HE3  1 
ATOM   1818 H  HZ1  . LYS   A 1 118 ? 27.16603 -11.32351 -4.96328  1.000 53.18232 ?  121 LYS   A HZ1  1 
ATOM   1819 H  HZ2  . LYS   A 1 118 ? 25.88537 -11.85152 -4.53967  1.000 53.18232 ?  121 LYS   A HZ2  1 
ATOM   1820 H  HZ3  . LYS   A 1 118 ? 26.51289 -10.78377 -3.78837  1.000 53.18232 ?  121 LYS   A HZ3  1 
ATOM   1821 N  N    . HIS   A 1 119 ? 27.22535 -9.35855  1.15459   1.000 20.38429 ?  122 HIS   A N    1 
ATOM   1822 C  CA   . HIS   A 1 119 ? 27.25974 -7.94839  0.81582   1.000 19.76573 ?  122 HIS   A CA   1 
ATOM   1823 C  C    . HIS   A 1 119 ? 26.56461 -7.70886  -0.51844  1.000 19.23212 ?  122 HIS   A C    1 
ATOM   1824 O  O    . HIS   A 1 119 ? 26.78003 -8.44978  -1.48356  1.000 21.56525 ?  122 HIS   A O    1 
ATOM   1825 C  CB   . HIS   A 1 119 ? 28.70503 -7.48182  0.70818   1.000 21.88409 ?  122 HIS   A CB   1 
ATOM   1826 C  CG   . HIS   A 1 119 ? 28.80799 -6.07311  0.24986   1.000 24.32886 ?  122 HIS   A CG   1 
ATOM   1827 N  ND1  . HIS   A 1 119 ? 28.34386 -5.02720  1.01285   1.000 26.02585 ?  122 HIS   A ND1  1 
ATOM   1828 C  CD2  . HIS   A 1 119 ? 29.24250 -5.53736  -0.91295  1.000 25.07507 ?  122 HIS   A CD2  1 
ATOM   1829 C  CE1  . HIS   A 1 119 ? 28.51175 -3.89931  0.34868   1.000 26.12757 ?  122 HIS   A CE1  1 
ATOM   1830 N  NE2  . HIS   A 1 119 ? 29.06363 -4.17918  -0.81966  1.000 24.90043 ?  122 HIS   A NE2  1 
ATOM   1831 H  H    . HIS   A 1 119 ? 27.99243 -9.70416  1.33277   1.000 24.46114 ?  122 HIS   A H    1 
ATOM   1832 H  HA   . HIS   A 1 119 ? 26.80885 -7.43964  1.50776   1.000 23.71888 ?  122 HIS   A HA   1 
ATOM   1833 H  HB2  . HIS   A 1 119 ? 29.12604 -7.54799  1.57954   1.000 26.26090 ?  122 HIS   A HB2  1 
ATOM   1834 H  HB3  . HIS   A 1 119 ? 29.17328 -8.04255  0.07004   1.000 26.26090 ?  122 HIS   A HB3  1 
ATOM   1835 H  HD2  . HIS   A 1 119 ? 29.59540 -6.00061  -1.63804  1.000 30.09008 ?  122 HIS   A HD2  1 
ATOM   1836 H  HE1  . HIS   A 1 119 ? 28.28083 -3.05080  0.65137   1.000 31.35308 ?  122 HIS   A HE1  1 
ATOM   1837 H  HE2  . HIS   A 1 119 ? 29.27599 -3.60423  -1.42293  1.000 29.88051 ?  122 HIS   A HE2  1 
ATOM   1838 N  N    . THR   A 1 120 ? 25.76842 -6.64441  -0.58495  1.000 17.12403 ?  123 THR   A N    1 
ATOM   1839 C  CA   . THR   A 1 120 ? 25.06383 -6.29150  -1.80649  1.000 16.85425 ?  123 THR   A CA   1 
ATOM   1840 C  C    . THR   A 1 120 ? 25.50072 -4.94707  -2.35357  1.000 16.13789 ?  123 THR   A C    1 
ATOM   1841 O  O    . THR   A 1 120 ? 25.87962 -4.87467  -3.53142  1.000 17.40522 ?  123 THR   A O    1 
ATOM   1842 C  CB   . THR   A 1 120 ? 23.54429 -6.33612  -1.57936  1.000 17.90016 ?  123 THR   A CB   1 
ATOM   1843 O  OG1  . THR   A 1 120 ? 23.17805 -7.63958  -1.09993  1.000 19.76875 ?  123 THR   A OG1  1 
ATOM   1844 C  CG2  . THR   A 1 120 ? 22.77604 -6.04585  -2.85100  1.000 18.53405 ?  123 THR   A CG2  1 
ATOM   1845 H  H    . THR   A 1 120 ? 25.62138 -6.10891  0.07172   1.000 20.54884 ?  123 THR   A H    1 
ATOM   1846 H  HA   . THR   A 1 120 ? 25.26123 -6.95288  -2.48804  1.000 20.22510 ?  123 THR   A HA   1 
ATOM   1847 H  HB   . THR   A 1 120 ? 23.30521 -5.65598  -0.93041  1.000 21.48019 ?  123 THR   A HB   1 
ATOM   1848 H  HG1  . THR   A 1 120 ? 22.66216 -8.01274  -1.64784  1.000 23.72249 ?  123 THR   A HG1  1 
ATOM   1849 H  HG21 . THR   A 1 120 ? 21.83452 -6.23991  -2.72142  1.000 22.24086 ?  123 THR   A HG21 1 
ATOM   1850 H  HG22 . THR   A 1 120 ? 22.87458 -5.11149  -3.09218  1.000 22.24086 ?  123 THR   A HG22 1 
ATOM   1851 H  HG23 . THR   A 1 120 ? 23.11390 -6.59529  -3.57547  1.000 22.24086 ?  123 THR   A HG23 1 
ATOM   1852 N  N    . LEU   A 1 121 ? 25.45711 -3.88185  -1.55308  1.000 15.14909 ?  124 LEU   A N    1 
ATOM   1853 C  CA   . LEU   A 1 121 ? 25.79722 -2.56380  -2.06917  1.000 15.22220 ?  124 LEU   A CA   1 
ATOM   1854 C  C    . LEU   A 1 121 ? 26.04709 -1.60878  -0.91294  1.000 14.55731 ?  124 LEU   A C    1 
ATOM   1855 O  O    . LEU   A 1 121 ? 25.66200 -1.87169  0.22563   1.000 15.49842 ?  124 LEU   A O    1 
ATOM   1856 C  CB   . LEU   A 1 121 ? 24.71806 -2.01234  -3.01129  1.000 15.29878 ?  124 LEU   A CB   1 
ATOM   1857 C  CG   . LEU   A 1 121 ? 23.30513 -1.86427  -2.45758  1.000 14.60099 ?  124 LEU   A CG   1 
ATOM   1858 C  CD1  . LEU   A 1 121 ? 23.08808 -0.58918  -1.64567  1.000 14.94378 ?  124 LEU   A CD1  1 
ATOM   1859 C  CD2  . LEU   A 1 121 ? 22.32047 -1.98355  -3.58087  1.000 15.54717 ?  124 LEU   A CD2  1 
ATOM   1860 H  H    . LEU   A 1 121 ? 25.23696 -3.89953  -0.72192  1.000 18.17891 ?  124 LEU   A H    1 
ATOM   1861 H  HA   . LEU   A 1 121 ? 26.62311 -2.63890  -2.57233  1.000 18.26664 ?  124 LEU   A HA   1 
ATOM   1862 H  HB2  . LEU   A 1 121 ? 24.99977 -1.13019  -3.29997  1.000 18.35854 ?  124 LEU   A HB2  1 
ATOM   1863 H  HB3  . LEU   A 1 121 ? 24.65892 -2.60802  -3.77456  1.000 18.35854 ?  124 LEU   A HB3  1 
ATOM   1864 H  HG   . LEU   A 1 121 ? 23.15601 -2.58034  -1.82047  1.000 17.52119 ?  124 LEU   A HG   1 
ATOM   1865 H  HD11 . LEU   A 1 121 ? 22.14527 -0.50685  -1.43301  1.000 17.93254 ?  124 LEU   A HD11 1 
ATOM   1866 H  HD12 . LEU   A 1 121 ? 23.60803 -0.64274  -0.82855  1.000 17.93254 ?  124 LEU   A HD12 1 
ATOM   1867 H  HD13 . LEU   A 1 121 ? 23.37630 0.17309   -2.17176  1.000 17.93254 ?  124 LEU   A HD13 1 
ATOM   1868 H  HD21 . LEU   A 1 121 ? 21.42575 -1.84562  -3.23250  1.000 18.65660 ?  124 LEU   A HD21 1 
ATOM   1869 H  HD22 . LEU   A 1 121 ? 22.52209 -1.31116  -4.25030  1.000 18.65660 ?  124 LEU   A HD22 1 
ATOM   1870 H  HD23 . LEU   A 1 121 ? 22.39103 -2.86928  -3.96997  1.000 18.65660 ?  124 LEU   A HD23 1 
ATOM   1871 N  N    . LEU   A 1 122 ? 26.68520 -0.48772  -1.22985  1.000 15.18015 ?  125 LEU   A N    1 
ATOM   1872 C  CA   . LEU   A 1 122 ? 26.81492 0.65311   -0.34175  1.000 15.13802 ?  125 LEU   A CA   1 
ATOM   1873 C  C    . LEU   A 1 122 ? 26.07094 1.82646   -0.97091  1.000 14.57765 ?  125 LEU   A C    1 
ATOM   1874 O  O    . LEU   A 1 122 ? 25.95447 1.91412   -2.20265  1.000 16.37461 ?  125 LEU   A O    1 
ATOM   1875 C  CB   . LEU   A 1 122 ? 28.27661 1.06446   -0.17070  1.000 16.83144 ?  125 LEU   A CB   1 
ATOM   1876 C  CG   . LEU   A 1 122 ? 29.23751 0.01700   0.36648   1.000 18.38873 ?  125 LEU   A CG   1 
ATOM   1877 C  CD1  . LEU   A 1 122 ? 30.63280 0.60041   0.49351   1.000 20.33947 ?  125 LEU   A CD1  1 
ATOM   1878 C  CD2  . LEU   A 1 122 ? 28.75294 -0.50447  1.71589   1.000 19.44616 ?  125 LEU   A CD2  1 
ATOM   1879 H  H    . LEU   A 1 122 ? 27.06783 -0.36160  -1.98964  1.000 18.21617 ?  125 LEU   A H    1 
ATOM   1880 H  HA   . LEU   A 1 122 ? 26.44726 0.43716   0.52950   1.000 18.16562 ?  125 LEU   A HA   1 
ATOM   1881 H  HB2  . LEU   A 1 122 ? 28.61264 1.33566   -1.03928  1.000 20.19772 ?  125 LEU   A HB2  1 
ATOM   1882 H  HB3  . LEU   A 1 122 ? 28.30442 1.81386   0.44455   1.000 20.19772 ?  125 LEU   A HB3  1 
ATOM   1883 H  HG   . LEU   A 1 122 ? 29.27497 -0.72996  -0.25122  1.000 22.06647 ?  125 LEU   A HG   1 
ATOM   1884 H  HD11 . LEU   A 1 122 ? 31.26003 -0.11731  0.67341   1.000 24.40737 ?  125 LEU   A HD11 1 
ATOM   1885 H  HD12 . LEU   A 1 122 ? 30.86661 1.04361   -0.33704  1.000 24.40737 ?  125 LEU   A HD12 1 
ATOM   1886 H  HD13 . LEU   A 1 122 ? 30.64277 1.23913   1.22347   1.000 24.40737 ?  125 LEU   A HD13 1 
ATOM   1887 H  HD21 . LEU   A 1 122 ? 29.45098 -1.04810  2.11352   1.000 23.33539 ?  125 LEU   A HD21 1 
ATOM   1888 H  HD22 . LEU   A 1 122 ? 28.55217 0.24949   2.29220   1.000 23.33539 ?  125 LEU   A HD22 1 
ATOM   1889 H  HD23 . LEU   A 1 122 ? 27.95476 -1.03862  1.57990   1.000 23.33539 ?  125 LEU   A HD23 1 
ATOM   1890 N  N    . TYR   A 1 123 ? 25.60466 2.76902   -0.14990  1.000 13.75015 ?  126 TYR   A N    1 
ATOM   1891 C  CA   . TYR   A 1 123 ? 24.94141 3.97012   -0.65635  1.000 14.05713 ?  126 TYR   A CA   1 
ATOM   1892 C  C    . TYR   A 1 123 ? 25.29209 5.15021   0.24069   1.000 14.25469 ?  126 TYR   A C    1 
ATOM   1893 O  O    . TYR   A 1 123 ? 24.86572 5.20729   1.40151   1.000 14.29638 ?  126 TYR   A O    1 
ATOM   1894 C  CB   . TYR   A 1 123 ? 23.43235 3.76443   -0.72338  1.000 14.00307 ?  126 TYR   A CB   1 
ATOM   1895 C  CG   . TYR   A 1 123 ? 22.72065 4.89637   -1.44092  1.000 13.78047 ?  126 TYR   A CG   1 
ATOM   1896 C  CD1  . TYR   A 1 123 ? 22.59944 4.88962   -2.82434  1.000 13.67467 ?  126 TYR   A CD1  1 
ATOM   1897 C  CD2  . TYR   A 1 123 ? 22.18484 5.97483   -0.75870  1.000 14.73815 ?  126 TYR   A CD2  1 
ATOM   1898 C  CE1  . TYR   A 1 123 ? 21.95898 5.89523   -3.49245  1.000 13.38769 ?  126 TYR   A CE1  1 
ATOM   1899 C  CE2  . TYR   A 1 123 ? 21.53455 7.00324   -1.43876  1.000 14.17447 ?  126 TYR   A CE2  1 
ATOM   1900 C  CZ   . TYR   A 1 123 ? 21.41565 6.94172   -2.81194  1.000 13.30935 ?  126 TYR   A CZ   1 
ATOM   1901 O  OH   . TYR   A 1 123 ? 20.78832 7.92381   -3.52787  1.000 13.72649 ?  126 TYR   A OH   1 
ATOM   1902 H  H    . TYR   A 1 123 ? 25.66115 2.73463   0.70755   1.000 16.50018 ?  126 TYR   A H    1 
ATOM   1903 H  HA   . TYR   A 1 123 ? 25.27579 4.16858   -1.54500  1.000 16.86856 ?  126 TYR   A HA   1 
ATOM   1904 H  HB2  . TYR   A 1 123 ? 23.24628 2.94106   -1.20124  1.000 16.80368 ?  126 TYR   A HB2  1 
ATOM   1905 H  HB3  . TYR   A 1 123 ? 23.07999 3.71131   0.17879   1.000 16.80368 ?  126 TYR   A HB3  1 
ATOM   1906 H  HD1  . TYR   A 1 123 ? 22.96305 4.18343   -3.30805  1.000 16.40960 ?  126 TYR   A HD1  1 
ATOM   1907 H  HD2  . TYR   A 1 123 ? 22.25981 6.01395   0.16744   1.000 17.68577 ?  126 TYR   A HD2  1 
ATOM   1908 H  HE1  . TYR   A 1 123 ? 21.89377 5.86439   -4.41965  1.000 16.06523 ?  126 TYR   A HE1  1 
ATOM   1909 H  HE2  . TYR   A 1 123 ? 21.18332 7.72573   -0.97020  1.000 17.00936 ?  126 TYR   A HE2  1 
ATOM   1910 H  HH   . TYR   A 1 123 ? 20.35663 8.42534   -3.01046  1.000 16.47179 ?  126 TYR   A HH   1 
ATOM   1911 N  N    . GLY   A 1 124 ? 26.07634 6.08699   -0.27904  1.000 14.61845 ?  127 GLY   A N    1 
ATOM   1912 C  CA   . GLY   A 1 124 ? 26.45625 7.23963   0.51762   1.000 15.14779 ?  127 GLY   A CA   1 
ATOM   1913 C  C    . GLY   A 1 124 ? 25.27162 8.13129   0.84505   1.000 14.74613 ?  127 GLY   A C    1 
ATOM   1914 O  O    . GLY   A 1 124 ? 24.37091 8.33264   0.02804   1.000 15.66227 ?  127 GLY   A O    1 
ATOM   1915 H  H    . GLY   A 1 124 ? 26.39591 6.07769   -1.07741  1.000 17.54215 ?  127 GLY   A H    1 
ATOM   1916 H  HA2  . GLY   A 1 124 ? 26.85141 6.93844   1.35071   1.000 18.17734 ?  127 GLY   A HA2  1 
ATOM   1917 H  HA3  . GLY   A 1 124 ? 27.10934 7.76595   0.03042   1.000 18.17734 ?  127 GLY   A HA3  1 
ATOM   1918 N  N    . HIS   A 1 125 ? 25.28134 8.69273   2.06027   1.000 14.69998 ?  128 HIS   A N    1 
ATOM   1919 C  CA   . HIS   A 1 125 ? 24.18607 9.58002   2.43871   1.000 14.97136 ?  128 HIS   A CA   1 
ATOM   1920 C  C    . HIS   A 1 125 ? 24.19148 10.81189  1.55103   1.000 15.43981 ?  128 HIS   A C    1 
ATOM   1921 O  O    . HIS   A 1 125 ? 25.23515 11.44984  1.35797   1.000 17.04993 ?  128 HIS   A O    1 
ATOM   1922 C  CB   . HIS   A 1 125 ? 24.29747 10.03571  3.89557   1.000 15.21810 ?  128 HIS   A CB   1 
ATOM   1923 C  CG   . HIS   A 1 125 ? 24.22752 8.91941   4.87703   1.000 15.02741 ?  128 HIS   A CG   1 
ATOM   1924 N  ND1  . HIS   A 1 125 ? 23.18972 8.01619   4.87221   1.000 15.38146 ?  128 HIS   A ND1  1 
ATOM   1925 C  CD2  . HIS   A 1 125 ? 25.04211 8.57190   5.90452   1.000 15.88595 ?  128 HIS   A CD2  1 
ATOM   1926 C  CE1  . HIS   A 1 125 ? 23.38861 7.13742   5.83479   1.000 15.62506 ?  128 HIS   A CE1  1 
ATOM   1927 N  NE2  . HIS   A 1 125 ? 24.48953 7.46338   6.48803   1.000 15.76426 ?  128 HIS   A NE2  1 
ATOM   1928 H  H    . HIS   A 1 125 ? 25.88884 8.57795   2.65808   1.000 17.63997 ?  128 HIS   A H    1 
ATOM   1929 H  HA   . HIS   A 1 125 ? 23.35609 9.08811   2.33840   1.000 17.96563 ?  128 HIS   A HA   1 
ATOM   1930 H  HB2  . HIS   A 1 125 ? 25.14821 10.48532  4.01800   1.000 18.26173 ?  128 HIS   A HB2  1 
ATOM   1931 H  HB3  . HIS   A 1 125 ? 23.56879 10.64622  4.08844   1.000 18.26173 ?  128 HIS   A HB3  1 
ATOM   1932 H  HD2  . HIS   A 1 125 ? 25.82457 9.00318   6.16269   1.000 19.06314 ?  128 HIS   A HD2  1 
ATOM   1933 H  HE1  . HIS   A 1 125 ? 22.84337 6.40789   6.02296   1.000 18.75007 ?  128 HIS   A HE1  1 
ATOM   1934 H  HE2  . HIS   A 1 125 ? 24.80776 7.04664   7.16969   1.000 18.91711 ?  128 HIS   A HE2  1 
ATOM   1935 N  N    . ARG   A 1 126 ? 23.00868 11.16138  1.05899   1.000 14.58402 ?  129 ARG   A N    1 
ATOM   1936 C  CA   . ARG   A 1 126 ? 22.75462 12.40295  0.34403   1.000 14.53370 ?  129 ARG   A CA   1 
ATOM   1937 C  C    . ARG   A 1 126 ? 21.88886 13.35708  1.15230   1.000 16.61988 ?  129 ARG   A C    1 
ATOM   1938 O  O    . ARG   A 1 126 ? 21.99732 14.56779  0.96838   1.000 19.84453 ?  129 ARG   A O    1 
ATOM   1939 C  CB   . ARG   A 1 126 ? 22.10511 12.10950  -1.01869  1.000 15.37429 ?  129 ARG   A CB   1 
ATOM   1940 C  CG   . ARG   A 1 126 ? 22.94248 11.19284  -1.89878  1.000 15.15370 ?  129 ARG   A CG   1 
ATOM   1941 C  CD   . ARG   A 1 126 ? 22.37785 11.10676  -3.27536  1.000 14.99482 ?  129 ARG   A CD   1 
ATOM   1942 N  NE   . ARG   A 1 126 ? 23.00102 10.07979  -4.09653  1.000 14.93750 ?  129 ARG   A NE   1 
ATOM   1943 C  CZ   . ARG   A 1 126 ? 22.48005 9.66617   -5.24071  1.000 14.95512 ?  129 ARG   A CZ   1 
ATOM   1944 N  NH1  . ARG   A 1 126 ? 21.43582 10.27126  -5.76420  1.000 15.13847 ?  129 ARG   A NH1  1 
ATOM   1945 N  NH2  . ARG   A 1 126 ? 23.01282 8.61817   -5.86157  1.000 16.23225 ?  129 ARG   A NH2  1 
ATOM   1946 H  H    . ARG   A 1 126 ? 22.30505 10.67210  1.13043   1.000 17.50082 ?  129 ARG   A H    1 
ATOM   1947 H  HA   . ARG   A 1 126 ? 23.58924 12.85674  0.14813   1.000 17.44044 ?  129 ARG   A HA   1 
ATOM   1948 H  HB2  . ARG   A 1 126 ? 21.24777 11.68025  -0.87164  1.000 18.44914 ?  129 ARG   A HB2  1 
ATOM   1949 H  HB3  . ARG   A 1 126 ? 21.98016 12.94617  -1.49331  1.000 18.44914 ?  129 ARG   A HB3  1 
ATOM   1950 H  HG2  . ARG   A 1 126 ? 23.84597 11.54060  -1.95938  1.000 18.18444 ?  129 ARG   A HG2  1 
ATOM   1951 H  HG3  . ARG   A 1 126 ? 22.95504 10.30146  -1.51645  1.000 18.18444 ?  129 ARG   A HG3  1 
ATOM   1952 H  HD2  . ARG   A 1 126 ? 21.43152 10.90293  -3.21352  1.000 17.99379 ?  129 ARG   A HD2  1 
ATOM   1953 H  HD3  . ARG   A 1 126 ? 22.50520 11.95940  -3.71998  1.000 17.99379 ?  129 ARG   A HD3  1 
ATOM   1954 H  HE   . ARG   A 1 126 ? 23.73783 9.72724   -3.82743  1.000 17.92500 ?  129 ARG   A HE   1 
ATOM   1955 H  HH11 . ARG   A 1 126 ? 21.08291 10.94474  -5.36235  1.000 18.16616 ?  129 ARG   A HH11 1 
ATOM   1956 H  HH12 . ARG   A 1 126 ? 21.10609 9.99335   -6.50827  1.000 18.16616 ?  129 ARG   A HH12 1 
ATOM   1957 H  HH21 . ARG   A 1 126 ? 23.69076 8.21457   -5.51935  1.000 19.47870 ?  129 ARG   A HH21 1 
ATOM   1958 H  HH22 . ARG   A 1 126 ? 22.67951 8.34387   -6.60538  1.000 19.47870 ?  129 ARG   A HH22 1 
ATOM   1959 N  N    . ILE   A 1 127 ? 21.00166 12.82760  1.99001   1.000 17.11678 ?  130 ILE   A N    1 
ATOM   1960 C  CA   . ILE   A 1 127 ? 20.25577 13.54786  3.01333   1.000 17.76099 ?  130 ILE   A CA   1 
ATOM   1961 C  C    . ILE   A 1 127 ? 20.80770 13.03716  4.34055   1.000 18.21159 ?  130 ILE   A C    1 
ATOM   1962 O  O    . ILE   A 1 127 ? 21.07105 11.83954  4.48250   1.000 17.53129 ?  130 ILE   A O    1 
ATOM   1963 C  CB   . ILE   A 1 127 ? 18.74604 13.22828  2.88375   1.000 16.87982 ?  130 ILE   A CB   1 
ATOM   1964 C  CG1  . ILE   A 1 127 ? 18.16442 13.71132  1.54636   1.000 17.84709 ?  130 ILE   A CG1  1 
ATOM   1965 C  CG2  . ILE   A 1 127 ? 17.95609 13.84657  4.01713   1.000 19.29393 ?  130 ILE   A CG2  1 
ATOM   1966 C  CD1  . ILE   A 1 127 ? 16.66198 13.45989  1.37333   1.000 17.93354 ?  130 ILE   A CD1  1 
ATOM   1967 H  H    . ILE   A 1 127 ? 20.80139 11.99128  1.98286   1.000 20.54014 ?  130 ILE   A H    1 
ATOM   1968 H  HA   . ILE   A 1 127 ? 20.36970 14.50906  2.94999   1.000 21.31319 ?  130 ILE   A HA   1 
ATOM   1969 H  HB   . ILE   A 1 127 ? 18.67180 12.26190  2.92256   1.000 20.25579 ?  130 ILE   A HB   1 
ATOM   1970 H  HG12 . ILE   A 1 127 ? 18.31078 14.66748  1.47394   1.000 21.41651 ?  130 ILE   A HG12 1 
ATOM   1971 H  HG13 . ILE   A 1 127 ? 18.62255 13.25011  0.82642   1.000 21.41651 ?  130 ILE   A HG13 1 
ATOM   1972 H  HG21 . ILE   A 1 127 ? 17.01340 13.66177  3.88263   1.000 23.15271 ?  130 ILE   A HG21 1 
ATOM   1973 H  HG22 . ILE   A 1 127 ? 18.25246 13.46036  4.85612   1.000 23.15271 ?  130 ILE   A HG22 1 
ATOM   1974 H  HG23 . ILE   A 1 127 ? 18.10794 14.80460  4.02206   1.000 23.15271 ?  130 ILE   A HG23 1 
ATOM   1975 H  HD11 . ILE   A 1 127 ? 16.42231 13.60542  0.44474   1.000 21.52025 ?  130 ILE   A HD11 1 
ATOM   1976 H  HD12 . ILE   A 1 127 ? 16.46371 12.54477  1.62661   1.000 21.52025 ?  130 ILE   A HD12 1 
ATOM   1977 H  HD13 . ILE   A 1 127 ? 16.17148 14.07409  1.94172   1.000 21.52025 ?  130 ILE   A HD13 1 
ATOM   1978 N  N    . GLY   A 1 128 ? 20.99700 13.92093  5.31711   1.000 18.07620 ?  131 GLY   A N    1 
ATOM   1979 C  CA   . GLY   A 1 128 ? 21.45776 13.45438  6.60820   1.000 19.38533 ?  131 GLY   A CA   1 
ATOM   1980 C  C    . GLY   A 1 128 ? 20.51570 12.40478  7.17039   1.000 17.49478 ?  131 GLY   A C    1 
ATOM   1981 O  O    . GLY   A 1 128 ? 19.30147 12.60159  7.17954   1.000 17.32718 ?  131 GLY   A O    1 
ATOM   1982 H  H    . GLY   A 1 128 ? 20.86785 14.76874  5.25269   1.000 21.69144 ?  131 GLY   A H    1 
ATOM   1983 H  HA2  . GLY   A 1 128 ? 22.34168 13.06497  6.51898   1.000 23.26240 ?  131 GLY   A HA2  1 
ATOM   1984 H  HA3  . GLY   A 1 128 ? 21.50178 14.19884  7.22847   1.000 23.26240 ?  131 GLY   A HA3  1 
ATOM   1985 N  N    . PRO   A 1 129 ? 21.04137 11.28448  7.68537   1.000 18.19019 ?  132 PRO   A N    1 
ATOM   1986 C  CA   . PRO   A 1 129 ? 20.13208 10.22432  8.15864   1.000 17.61745 ?  132 PRO   A CA   1 
ATOM   1987 C  C    . PRO   A 1 129 ? 19.28518 10.64671  9.34720   1.000 16.60411 ?  132 PRO   A C    1 
ATOM   1988 O  O    . PRO   A 1 129 ? 18.25467 10.01716  9.60935   1.000 16.14198 ?  132 PRO   A O    1 
ATOM   1989 C  CB   . PRO   A 1 129 ? 21.06861 9.05434   8.48536   1.000 20.11306 ?  132 PRO   A CB   1 
ATOM   1990 C  CG   . PRO   A 1 129 ? 22.41099 9.68073   8.69357   1.000 21.02225 ?  132 PRO   A CG   1 
ATOM   1991 C  CD   . PRO   A 1 129 ? 22.45007 10.85681  7.75236   1.000 20.04014 ?  132 PRO   A CD   1 
ATOM   1992 H  HA   . PRO   A 1 129 ? 19.54385 9.93885   7.44212   1.000 21.14094 ?  132 PRO   A HA   1 
ATOM   1993 H  HB2  . PRO   A 1 129 ? 20.76678 8.60441   9.28995   1.000 24.13567 ?  132 PRO   A HB2  1 
ATOM   1994 H  HB3  . PRO   A 1 129 ? 21.08813 8.42977   7.74345   1.000 24.13567 ?  132 PRO   A HB3  1 
ATOM   1995 H  HG2  . PRO   A 1 129 ? 22.49953 9.97192   9.61458   1.000 25.22670 ?  132 PRO   A HG2  1 
ATOM   1996 H  HG3  . PRO   A 1 129 ? 23.10930 9.04267   8.47876   1.000 25.22670 ?  132 PRO   A HG3  1 
ATOM   1997 H  HD2  . PRO   A 1 129 ? 23.00931 11.56510  8.10799   1.000 24.04817 ?  132 PRO   A HD2  1 
ATOM   1998 H  HD3  . PRO   A 1 129 ? 22.77125 10.58818  6.87739   1.000 24.04817 ?  132 PRO   A HD3  1 
ATOM   1999 N  N    . GLU   A 1 130 ? 19.66813 11.71513  10.05039  1.000 17.52102 ?  133 GLU   A N    1 
ATOM   2000 C  CA   . GLU   A 1 130 ? 18.85910 12.23753  11.14573  1.000 17.49138 ?  133 GLU   A CA   1 
ATOM   2001 C  C    . GLU   A 1 130 ? 17.50999 12.77523  10.67569  1.000 17.55200 ?  133 GLU   A C    1 
ATOM   2002 O  O    . GLU   A 1 130 ? 16.59601 12.93888  11.48877  1.000 19.34977 ?  133 GLU   A O    1 
ATOM   2003 C  CB   . GLU   A 1 130 ? 19.64317 13.32847  11.88610  1.000 20.93300 ?  133 GLU   A CB   1 
ATOM   2004 C  CG   . GLU   A 1 130 ? 19.83111 14.64241  11.10694  1.000 24.48952 ?  133 GLU   A CG   1 
ATOM   2005 C  CD   . GLU   A 1 130 ? 20.93484 14.64237  10.04707  1.000 28.82734 ?  133 GLU   A CD   1 
ATOM   2006 O  OE1  . GLU   A 1 130 ? 21.70664 13.65534  9.91235   1.000 28.49405 ?  133 GLU   A OE1  1 
ATOM   2007 O  OE2  . GLU   A 1 130 ? 21.02638 15.68420  9.35252   1.000 32.10946 ?  133 GLU   A OE2  1 
ATOM   2008 H  H    . GLU   A 1 130 ? 20.39395 12.15494  9.91128   1.000 21.02522 ?  133 GLU   A H    1 
ATOM   2009 H  HA   . GLU   A 1 130 ? 18.67551 11.51954  11.77158  1.000 20.98966 ?  133 GLU   A HA   1 
ATOM   2010 H  HB2  . GLU   A 1 130 ? 19.17081 13.54233  12.70589  1.000 25.11960 ?  133 GLU   A HB2  1 
ATOM   2011 H  HB3  . GLU   A 1 130 ? 20.52641 12.98452  12.09221  1.000 25.11960 ?  133 GLU   A HB3  1 
ATOM   2012 H  HG2  . GLU   A 1 130 ? 18.99883 14.84775  10.65303  1.000 29.38742 ?  133 GLU   A HG2  1 
ATOM   2013 H  HG3  . GLU   A 1 130 ? 20.04451 15.34392  11.74196  1.000 29.38742 ?  133 GLU   A HG3  1 
ATOM   2014 N  N    . LYS   A 1 131 ? 17.34998 13.02068  9.38074   1.000 17.21916 ?  134 LYS   A N    1 
ATOM   2015 C  CA   . LYS   A 1 131 ? 16.09073 13.50917  8.83435   1.000 17.34768 ?  134 LYS   A CA   1 
ATOM   2016 C  C    . LYS   A 1 131 ? 15.11594 12.39861  8.50032   1.000 15.86775 ?  134 LYS   A C    1 
ATOM   2017 O  O    . LYS   A 1 131 ? 13.96343 12.69428  8.17839   1.000 18.07562 ?  134 LYS   A O    1 
ATOM   2018 C  CB   . LYS   A 1 131 ? 16.34730 14.33827  7.58610   1.000 19.32749 ?  134 LYS   A CB   1 
ATOM   2019 C  CG   . LYS   A 1 131 ? 17.13260 15.59154  7.92169   1.000 24.47766 ?  134 LYS   A CG   1 
ATOM   2020 C  CD   . LYS   A 1 131 ? 17.14536 16.58698  6.80761   1.000 26.25965 ?  134 LYS   A CD   1 
ATOM   2021 C  CE   . LYS   A 1 131 ? 17.70483 17.92064  7.28779   1.000 29.09392 ?  134 LYS   A CE   1 
ATOM   2022 N  NZ   . LYS   A 1 131 ? 19.02107 17.75649  7.95419   1.000 34.69621 ?  134 LYS   A NZ   1 
ATOM   2023 H  H    . LYS   A 1 131 ? 17.96487 12.91052  8.78967   1.000 20.66299 ?  134 LYS   A H    1 
ATOM   2024 H  HA   . LYS   A 1 131 ? 15.67246 14.08299  9.49517   1.000 20.81722 ?  134 LYS   A HA   1 
ATOM   2025 H  HB2  . LYS   A 1 131 ? 16.85947 13.81453  6.95027   1.000 23.19298 ?  134 LYS   A HB2  1 
ATOM   2026 H  HB3  . LYS   A 1 131 ? 15.50022 14.60115  7.19335   1.000 23.19298 ?  134 LYS   A HB3  1 
ATOM   2027 H  HG2  . LYS   A 1 131 ? 16.73335 16.01615  8.69707   1.000 29.37319 ?  134 LYS   A HG2  1 
ATOM   2028 H  HG3  . LYS   A 1 131 ? 18.05126 15.34652  8.11385   1.000 29.37319 ?  134 LYS   A HG3  1 
ATOM   2029 H  HD2  . LYS   A 1 131 ? 17.70447 16.25951  6.08576   1.000 31.51158 ?  134 LYS   A HD2  1 
ATOM   2030 H  HD3  . LYS   A 1 131 ? 16.24049 16.72873  6.48824   1.000 31.51158 ?  134 LYS   A HD3  1 
ATOM   2031 H  HE2  . LYS   A 1 131 ? 17.82056 18.51176  6.52748   1.000 34.91270 ?  134 LYS   A HE2  1 
ATOM   2032 H  HE3  . LYS   A 1 131 ? 17.08884 18.31574  7.92446   1.000 34.91270 ?  134 LYS   A HE3  1 
ATOM   2033 H  HZ1  . LYS   A 1 131 ? 19.38512 18.55363  8.10955   1.000 41.63545 ?  134 LYS   A HZ1  1 
ATOM   2034 H  HZ2  . LYS   A 1 131 ? 18.91911 17.32967  8.72848   1.000 41.63545 ?  134 LYS   A HZ2  1 
ATOM   2035 H  HZ3  . LYS   A 1 131 ? 19.56870 17.28519  7.43450   1.000 41.63545 ?  134 LYS   A HZ3  1 
ATOM   2036 N  N    . ILE   A 1 132 ? 15.53949 11.14505  8.58927   1.000 14.02849 ?  135 ILE   A N    1 
ATOM   2037 C  CA   . ILE   A 1 132 ? 14.67162 10.03169  8.25146   1.000 13.25769 ?  135 ILE   A CA   1 
ATOM   2038 C  C    . ILE   A 1 132 ? 13.78935 9.72404   9.44907   1.000 13.83749 ?  135 ILE   A C    1 
ATOM   2039 O  O    . ILE   A 1 132 ? 14.28271 9.51429   10.56655  1.000 15.65231 ?  135 ILE   A O    1 
ATOM   2040 C  CB   . ILE   A 1 132 ? 15.49718 8.79620   7.86621   1.000 13.45410 ?  135 ILE   A CB   1 
ATOM   2041 C  CG1  . ILE   A 1 132 ? 16.33575 9.08556   6.62807   1.000 13.85965 ?  135 ILE   A CG1  1 
ATOM   2042 C  CG2  . ILE   A 1 132 ? 14.57142 7.61033   7.68956   1.000 13.56055 ?  135 ILE   A CG2  1 
ATOM   2043 C  CD1  . ILE   A 1 132 ? 17.44028 8.08643   6.40088   1.000 14.01353 ?  135 ILE   A CD1  1 
ATOM   2044 H  H    . ILE   A 1 132 ? 16.32792 10.91430  8.84369   1.000 16.83419 ?  135 ILE   A H    1 
ATOM   2045 H  HA   . ILE   A 1 132 ? 14.11334 10.28074  7.49833   1.000 15.90923 ?  135 ILE   A HA   1 
ATOM   2046 H  HB   . ILE   A 1 132 ? 16.12158 8.57784   8.57568   1.000 16.14492 ?  135 ILE   A HB   1 
ATOM   2047 H  HG12 . ILE   A 1 132 ? 15.75801 9.07149   5.84902   1.000 16.63158 ?  135 ILE   A HG12 1 
ATOM   2048 H  HG13 . ILE   A 1 132 ? 16.74250 9.96096   6.72369   1.000 16.63158 ?  135 ILE   A HG13 1 
ATOM   2049 H  HG21 . ILE   A 1 132 ? 15.08515 6.85423   7.36508   1.000 16.27266 ?  135 ILE   A HG21 1 
ATOM   2050 H  HG22 . ILE   A 1 132 ? 14.16869 7.39391   8.54505   1.000 16.27266 ?  135 ILE   A HG22 1 
ATOM   2051 H  HG23 . ILE   A 1 132 ? 13.88142 7.84116   7.04807   1.000 16.27266 ?  135 ILE   A HG23 1 
ATOM   2052 H  HD11 . ILE   A 1 132 ? 17.97241 8.37117   5.64151   1.000 16.81624 ?  135 ILE   A HD11 1 
ATOM   2053 H  HD12 . ILE   A 1 132 ? 17.99480 8.04256   7.19554   1.000 16.81624 ?  135 ILE   A HD12 1 
ATOM   2054 H  HD13 . ILE   A 1 132 ? 17.04818 7.21728   6.22275   1.000 16.81624 ?  135 ILE   A HD13 1 
ATOM   2055 N  N    . ASP   A 1 133 ? 12.49513 9.64849   9.22535   1.000 13.07012 ?  136 ASP   A N    1 
ATOM   2056 C  CA   . ASP   A 1 133 ? 11.57814 9.28422   10.29634  1.000 13.50988 ?  136 ASP   A CA   1 
ATOM   2057 C  C    . ASP   A 1 133 ? 10.50726 8.29781   9.87089   1.000 13.17019 ?  136 ASP   A C    1 
ATOM   2058 O  O    . ASP   A 1 133 ? 9.65682  7.95364   10.69844  1.000 14.04397 ?  136 ASP   A O    1 
ATOM   2059 C  CB   . ASP   A 1 133 ? 10.94298 10.53168  10.94670  1.000 16.16889 ?  136 ASP   A CB   1 
ATOM   2060 C  CG   . ASP   A 1 133 ? 10.05495 11.30487  9.99186   1.000 17.82953 ?  136 ASP   A CG   1 
ATOM   2061 O  OD1  . ASP   A 1 133 ? 9.78161  10.78618  8.90466   1.000 16.19922 ?  136 ASP   A OD1  1 
ATOM   2062 O  OD2  . ASP   A 1 133 ? 9.60336  12.42535  10.33708  1.000 23.07031 ?  136 ASP   A OD2  1 
ATOM   2063 H  H    . ASP   A 1 133 ? 12.11866 9.80163   8.46745   1.000 15.68414 ?  136 ASP   A H    1 
ATOM   2064 H  HA   . ASP   A 1 133 ? 12.09101 8.85514   10.99902  1.000 16.21186 ?  136 ASP   A HA   1 
ATOM   2065 H  HB2  . ASP   A 1 133 ? 10.40072 10.25306  11.70117  1.000 19.40267 ?  136 ASP   A HB2  1 
ATOM   2066 H  HB3  . ASP   A 1 133 ? 11.64887 11.12546  11.24679  1.000 19.40267 ?  136 ASP   A HB3  1 
ATOM   2067 N  N    . THR   A 1 134 ? 10.53978 7.80092   8.62429   1.000 12.69652 ?  137 THR   A N    1 
ATOM   2068 C  CA   . THR   A 1 134 ? 9.45812  6.99773   8.06749   1.000 12.62717 ?  137 THR   A CA   1 
ATOM   2069 C  C    . THR   A 1 134 ? 10.05785 5.92971   7.17082   1.000 11.80790 ?  137 THR   A C    1 
ATOM   2070 O  O    . THR   A 1 134 ? 11.01762 6.19295   6.43898   1.000 12.47785 ?  137 THR   A O    1 
ATOM   2071 C  CB   . THR   A 1 134 ? 8.49140  7.89513   7.27721   1.000 13.54380 ?  137 THR   A CB   1 
ATOM   2072 O  OG1  . THR   A 1 134 ? 7.92024  8.86791   8.15880   1.000 14.83036 ?  137 THR   A OG1  1 
ATOM   2073 C  CG2  . THR   A 1 134 ? 7.36329  7.11684   6.64851   1.000 15.11019 ?  137 THR   A CG2  1 
ATOM   2074 H  H    . THR   A 1 134 ? 11.19266 7.92168   8.07769   1.000 15.23582 ?  137 THR   A H    1 
ATOM   2075 H  HA   . THR   A 1 134 ? 8.95805  6.54792   8.76642   1.000 15.15261 ?  137 THR   A HA   1 
ATOM   2076 H  HB   . THR   A 1 134 ? 8.99413  8.31878   6.56399   1.000 16.25256 ?  137 THR   A HB   1 
ATOM   2077 H  HG1  . THR   A 1 134 ? 8.29394  9.61180   8.04665   1.000 17.79643 ?  137 THR   A HG1  1 
ATOM   2078 H  HG21 . THR   A 1 134 ? 6.68361  7.72542   6.31902   1.000 18.13222 ?  137 THR   A HG21 1 
ATOM   2079 H  HG22 . THR   A 1 134 ? 7.69785  6.58763   5.90763   1.000 18.13222 ?  137 THR   A HG22 1 
ATOM   2080 H  HG23 . THR   A 1 134 ? 6.96378  6.52375   7.30390   1.000 18.13222 ?  137 THR   A HG23 1 
ATOM   2081 N  N    . LEU   A 1 135 ? 9.49886  4.72438   7.23639   1.000 12.03843 ?  138 LEU   A N    1 
ATOM   2082 C  CA   A LEU   A 1 135 ? 9.85884  3.62801   6.34563   0.564 12.07750 ?  138 LEU   A CA   1 
ATOM   2083 C  CA   B LEU   A 1 135 ? 9.86631  3.64019   6.33849   0.436 11.83412 ?  138 LEU   A CA   1 
ATOM   2084 C  C    . LEU   A 1 135 ? 8.65154  3.28897   5.49116   1.000 11.88764 ?  138 LEU   A C    1 
ATOM   2085 O  O    . LEU   A 1 135 ? 7.56101  3.07078   6.03535   1.000 12.60327 ?  138 LEU   A O    1 
ATOM   2086 C  CB   A LEU   A 1 135 ? 10.23177 2.39759   7.18054   0.564 14.06367 ?  138 LEU   A CB   1 
ATOM   2087 C  CB   B LEU   A 1 135 ? 10.36956 2.43945   7.13839   0.436 12.94472 ?  138 LEU   A CB   1 
ATOM   2088 C  CG   A LEU   A 1 135 ? 10.32757 1.05302   6.44310   0.564 13.98560 ?  138 LEU   A CG   1 
ATOM   2089 C  CG   B LEU   A 1 135 ? 11.00293 1.36463   6.25013   0.436 12.57679 ?  138 LEU   A CG   1 
ATOM   2090 C  CD1  A LEU   A 1 135 ? 11.47617 1.11973   5.47276   0.564 13.24912 ?  138 LEU   A CD1  1 
ATOM   2091 C  CD1  B LEU   A 1 135 ? 12.17387 0.65488   6.89611   0.436 12.97540 ?  138 LEU   A CD1  1 
ATOM   2092 C  CD2  A LEU   A 1 135 ? 10.48780 -0.12617  7.40907   0.564 14.18035 ?  138 LEU   A CD2  1 
ATOM   2093 C  CD2  B LEU   A 1 135 ? 9.94125  0.36445   5.89514   0.436 13.38287 ?  138 LEU   A CD2  1 
ATOM   2094 H  H    . LEU   A 1 135 ? 8.89062  4.51556   7.80740   1.000 14.44611 ?  138 LEU   A H    1 
ATOM   2095 H  HA   . LEU   A 1 135 ? 10.59906 3.88104   5.77208   1.000 14.20094 ?  138 LEU   A HA   1 
ATOM   2096 H  HB2  A LEU   A 1 135 ? 11.09940 2.56180   7.58198   0.564 16.87640 ?  138 LEU   A HB2  1 
ATOM   2097 H  HB2  B LEU   A 1 135 ? 11.03949 2.74055   7.77197   0.436 15.53366 ?  138 LEU   A HB2  1 
ATOM   2098 H  HB3  A LEU   A 1 135 ? 9.56043  2.29267   7.87277   0.564 16.87640 ?  138 LEU   A HB3  1 
ATOM   2099 H  HB3  B LEU   A 1 135 ? 9.62268  2.03914   7.61044   0.436 15.53366 ?  138 LEU   A HB3  1 
ATOM   2100 H  HG   A LEU   A 1 135 ? 9.50205  0.88994   5.96058   0.564 16.78272 ?  138 LEU   A HG   1 
ATOM   2101 H  HG   B LEU   A 1 135 ? 11.36093 1.79849   5.45988   0.436 15.09215 ?  138 LEU   A HG   1 
ATOM   2102 H  HD11 A LEU   A 1 135 ? 11.64613 0.23109   5.12302   0.564 15.89894 ?  138 LEU   A HD11 1 
ATOM   2103 H  HD11 B LEU   A 1 135 ? 12.56869 0.04642   6.25206   0.436 15.57048 ?  138 LEU   A HD11 1 
ATOM   2104 H  HD12 A LEU   A 1 135 ? 11.24311 1.72130   4.74840   0.564 15.89894 ?  138 LEU   A HD12 1 
ATOM   2105 H  HD12 B LEU   A 1 135 ? 12.82914 1.31432   7.17300   0.436 15.57048 ?  138 LEU   A HD12 1 
ATOM   2106 H  HD13 A LEU   A 1 135 ? 12.26227 1.44880   5.93607   0.564 15.89894 ?  138 LEU   A HD13 1 
ATOM   2107 H  HD13 B LEU   A 1 135 ? 11.85652 0.15977   7.66751   0.436 15.57048 ?  138 LEU   A HD13 1 
ATOM   2108 H  HD21 A LEU   A 1 135 ? 10.48317 -0.95290  6.90172   0.564 17.01642 ?  138 LEU   A HD21 1 
ATOM   2109 H  HD21 B LEU   A 1 135 ? 10.36344 -0.42565  5.52313   0.436 16.05945 ?  138 LEU   A HD21 1 
ATOM   2110 H  HD22 A LEU   A 1 135 ? 11.32890 -0.03384  7.88335   0.564 17.01642 ?  138 LEU   A HD22 1 
ATOM   2111 H  HD22 B LEU   A 1 135 ? 9.44798  0.12958   6.69665   0.436 16.05945 ?  138 LEU   A HD22 1 
ATOM   2112 H  HD23 A LEU   A 1 135 ? 9.75039  -0.12065  8.03922   0.564 17.01642 ?  138 LEU   A HD23 1 
ATOM   2113 H  HD23 B LEU   A 1 135 ? 9.34230  0.75821   5.24160   0.436 16.05945 ?  138 LEU   A HD23 1 
ATOM   2114 N  N    . GLY   A 1 136 ? 8.84635  3.24333   4.17716   1.000 11.14698 ?  139 GLY   A N    1 
ATOM   2115 C  CA   . GLY   A 1 136 ? 7.81775  2.79678   3.25653   1.000 11.09869 ?  139 GLY   A CA   1 
ATOM   2116 C  C    . GLY   A 1 136 ? 8.29555  1.58298   2.48778   1.000 11.29165 ?  139 GLY   A C    1 
ATOM   2117 O  O    . GLY   A 1 136 ? 9.46354  1.50145   2.11118   1.000 11.79768 ?  139 GLY   A O    1 
ATOM   2118 H  H    . GLY   A 1 136 ? 9.58062  3.47087   3.79158   1.000 13.37638 ?  139 GLY   A H    1 
ATOM   2119 H  HA2  . GLY   A 1 136 ? 7.01476  2.56213   3.74751   1.000 13.31843 ?  139 GLY   A HA2  1 
ATOM   2120 H  HA3  . GLY   A 1 136 ? 7.60781  3.50483   2.62765   1.000 13.31843 ?  139 GLY   A HA3  1 
ATOM   2121 N  N    . ILE   A 1 137 ? 7.38052  0.65242   2.24918   1.000 10.92355 ?  140 ILE   A N    1 
ATOM   2122 C  CA   . ILE   A 1 137 ? 7.62981  -0.47351  1.36063   1.000 10.70053 ?  140 ILE   A CA   1 
ATOM   2123 C  C    . ILE   A 1 137 ? 6.47356  -0.55877  0.38441   1.000 11.52740 ?  140 ILE   A C    1 
ATOM   2124 O  O    . ILE   A 1 137 ? 5.31472  -0.60556  0.81048   1.000 11.99087 ?  140 ILE   A O    1 
ATOM   2125 C  CB   . ILE   A 1 137 ? 7.82565  -1.81051  2.10300   1.000 11.13173 ?  140 ILE   A CB   1 
ATOM   2126 C  CG1  . ILE   A 1 137 ? 8.97295  -1.68421  3.10867   1.000 11.86661 ?  140 ILE   A CG1  1 
ATOM   2127 C  CG2  . ILE   A 1 137 ? 8.07270  -2.92131  1.08496   1.000 12.18957 ?  140 ILE   A CG2  1 
ATOM   2128 C  CD1  . ILE   A 1 137 ? 9.29722  -2.94790  3.88367   1.000 13.96270 ?  140 ILE   A CD1  1 
ATOM   2129 H  H    . ILE   A 1 137 ? 6.59396  0.65225   2.59691   1.000 13.10826 ?  140 ILE   A H    1 
ATOM   2130 H  HA   . ILE   A 1 137 ? 8.44841  -0.30548  0.86814   1.000 12.84063 ?  140 ILE   A HA   1 
ATOM   2131 H  HB   . ILE   A 1 137 ? 7.02547  -2.03403  2.60366   1.000 13.35807 ?  140 ILE   A HB   1 
ATOM   2132 H  HG12 . ILE   A 1 137 ? 9.77460  -1.42591  2.62748   1.000 14.23994 ?  140 ILE   A HG12 1 
ATOM   2133 H  HG13 . ILE   A 1 137 ? 8.73916  -0.99997  3.75525   1.000 14.23994 ?  140 ILE   A HG13 1 
ATOM   2134 H  HG21 . ILE   A 1 137 ? 8.24841  -3.74977  1.55790   1.000 14.62748 ?  140 ILE   A HG21 1 
ATOM   2135 H  HG22 . ILE   A 1 137 ? 7.28515  -3.01943  0.52726   1.000 14.62748 ?  140 ILE   A HG22 1 
ATOM   2136 H  HG23 . ILE   A 1 137 ? 8.83784  -2.68396  0.53803   1.000 14.62748 ?  140 ILE   A HG23 1 
ATOM   2137 H  HD11 . ILE   A 1 137 ? 9.76538  -2.70731  4.69843   1.000 16.75524 ?  140 ILE   A HD11 1 
ATOM   2138 H  HD12 . ILE   A 1 137 ? 8.47035  -3.40640  4.10038   1.000 16.75524 ?  140 ILE   A HD12 1 
ATOM   2139 H  HD13 . ILE   A 1 137 ? 9.85839  -3.51896  3.33605   1.000 16.75524 ?  140 ILE   A HD13 1 
ATOM   2140 N  N    . TYR   A 1 138 ? 6.79208  -0.55122  -0.91228  1.000 11.45317 ?  141 TYR   A N    1 
ATOM   2141 C  CA   . TYR   A 1 138 ? 5.78400  -0.45271  -1.95979  1.000 11.38604 ?  141 TYR   A CA   1 
ATOM   2142 C  C    . TYR   A 1 138 ? 6.11114  -1.44620  -3.05770  1.000 12.01555 ?  141 TYR   A C    1 
ATOM   2143 O  O    . TYR   A 1 138 ? 7.26994  -1.81352  -3.25485  1.000 12.57967 ?  141 TYR   A O    1 
ATOM   2144 C  CB   . TYR   A 1 138 ? 5.74980  0.95442   -2.57791  1.000 12.35390 ?  141 TYR   A CB   1 
ATOM   2145 C  CG   . TYR   A 1 138 ? 5.78057  2.08292   -1.57062  1.000 12.53647 ?  141 TYR   A CG   1 
ATOM   2146 C  CD1  . TYR   A 1 138 ? 4.62982  2.52624   -0.96515  1.000 15.94678 ?  141 TYR   A CD1  1 
ATOM   2147 C  CD2  . TYR   A 1 138 ? 6.96469  2.72700   -1.23857  1.000 13.22433 ?  141 TYR   A CD2  1 
ATOM   2148 C  CE1  . TYR   A 1 138 ? 4.64566  3.55397   -0.04277  1.000 17.17023 ?  141 TYR   A CE1  1 
ATOM   2149 C  CE2  . TYR   A 1 138 ? 6.99583  3.76656   -0.31497  1.000 13.44445 ?  141 TYR   A CE2  1 
ATOM   2150 C  CZ   . TYR   A 1 138 ? 5.83909  4.17051   0.29715   1.000 13.72810 ?  141 TYR   A CZ   1 
ATOM   2151 O  OH   . TYR   A 1 138 ? 5.84790  5.20450   1.20733   1.000 15.18761 ?  141 TYR   A OH   1 
ATOM   2152 H  H    . TYR   A 1 138 ? 7.59706  -0.60292  -1.21048  1.000 13.74380 ?  141 TYR   A H    1 
ATOM   2153 H  HA   . TYR   A 1 138 ? 4.91615  -0.66188  -1.58034  1.000 13.66324 ?  141 TYR   A HA   1 
ATOM   2154 H  HB2  . TYR   A 1 138 ? 6.52185  1.05675   -3.15615  1.000 14.82468 ?  141 TYR   A HB2  1 
ATOM   2155 H  HB3  . TYR   A 1 138 ? 4.93393  1.04517   -3.09466  1.000 14.82468 ?  141 TYR   A HB3  1 
ATOM   2156 H  HD1  . TYR   A 1 138 ? 3.81973  2.12413   -1.18188  1.000 19.13614 ?  141 TYR   A HD1  1 
ATOM   2157 H  HD2  . TYR   A 1 138 ? 7.75691  2.45665   -1.64378  1.000 15.86920 ?  141 TYR   A HD2  1 
ATOM   2158 H  HE1  . TYR   A 1 138 ? 3.85146  3.83359   0.35215   1.000 20.60428 ?  141 TYR   A HE1  1 
ATOM   2159 H  HE2  . TYR   A 1 138 ? 7.80071  4.18662   -0.11342  1.000 16.13334 ?  141 TYR   A HE2  1 
ATOM   2160 H  HH   . TYR   A 1 138 ? 5.06211  5.38975   1.43930   1.000 18.22514 ?  141 TYR   A HH   1 
ATOM   2161 N  N    . GLY   A 1 139 ? 5.08687  -1.82986  -3.81780  1.000 12.46028 ?  142 GLY   A N    1 
ATOM   2162 C  CA   . GLY   A 1 139 ? 5.26304  -2.64111  -5.01057  1.000 12.68238 ?  142 GLY   A CA   1 
ATOM   2163 C  C    . GLY   A 1 139 ? 4.90216  -4.09172  -4.77624  1.000 13.60182 ?  142 GLY   A C    1 
ATOM   2164 O  O    . GLY   A 1 139 ? 4.14610  -4.44030  -3.86900  1.000 15.94648 ?  142 GLY   A O    1 
ATOM   2165 H  H    . GLY   A 1 139 ? 4.26667  -1.62718  -3.65719  1.000 14.95234 ?  142 GLY   A H    1 
ATOM   2166 H  HA2  . GLY   A 1 139 ? 4.69889  -2.29599  -5.72017  1.000 15.21886 ?  142 GLY   A HA2  1 
ATOM   2167 H  HA3  . GLY   A 1 139 ? 6.18954  -2.59807  -5.29454  1.000 15.21886 ?  142 GLY   A HA3  1 
ATOM   2168 N  N    . LYS   A 1 140 ? 5.42481  -4.95111  -5.63971  1.000 13.59646 ?  143 LYS   A N    1 
ATOM   2169 C  CA   . LYS   A 1 140 ? 5.03349  -6.36162  -5.66058  1.000 14.03611 ?  143 LYS   A CA   1 
ATOM   2170 C  C    . LYS   A 1 140 ? 6.04121  -7.15164  -4.82437  1.000 13.96840 ?  143 LYS   A C    1 
ATOM   2171 O  O    . LYS   A 1 140 ? 7.07131  -7.62269  -5.30317  1.000 15.32134 ?  143 LYS   A O    1 
ATOM   2172 C  CB   . LYS   A 1 140 ? 4.84060  -6.87047  -7.09321  1.000 15.72663 ?  143 LYS   A CB   1 
ATOM   2173 C  CG   . LYS   A 1 140 ? 3.57562  -6.26512  -7.77156  1.000 17.92207 ?  143 LYS   A CG   1 
ATOM   2174 C  CD   . LYS   A 1 140 ? 3.19610  -6.92527  -9.09758  1.000 18.90584 ?  143 LYS   A CD   1 
ATOM   2175 C  CE   . LYS   A 1 140 ? 2.08004  -6.15304  -9.80144  1.000 22.12070 ?  143 LYS   A CE   1 
ATOM   2176 N  NZ   . LYS   A 1 140 ? 1.66435  -6.77349  -11.09802 1.000 24.85961 ?  143 LYS   A NZ   1 
ATOM   2177 H  H    . LYS   A 1 140 ? 6.01395  -4.74294  -6.23062  1.000 16.31576 ?  143 LYS   A H    1 
ATOM   2178 H  HA   . LYS   A 1 140 ? 4.17547  -6.47013  -5.22134  1.000 16.84334 ?  143 LYS   A HA   1 
ATOM   2179 H  HB2  . LYS   A 1 140 ? 5.61462  -6.62517  -7.62389  1.000 18.87195 ?  143 LYS   A HB2  1 
ATOM   2180 H  HB3  . LYS   A 1 140 ? 4.74202  -7.83531  -7.07659  1.000 18.87195 ?  143 LYS   A HB3  1 
ATOM   2181 H  HG2  . LYS   A 1 140 ? 2.82227  -6.36448  -7.16865  1.000 21.50649 ?  143 LYS   A HG2  1 
ATOM   2182 H  HG3  . LYS   A 1 140 ? 3.73758  -5.32516  -7.94804  1.000 21.50649 ?  143 LYS   A HG3  1 
ATOM   2183 H  HD2  . LYS   A 1 140 ? 3.97044  -6.94403  -9.68150  1.000 22.68701 ?  143 LYS   A HD2  1 
ATOM   2184 H  HD3  . LYS   A 1 140 ? 2.88470  -7.82858  -8.93039  1.000 22.68701 ?  143 LYS   A HD3  1 
ATOM   2185 H  HE2  . LYS   A 1 140 ? 1.30281  -6.12434  -9.22178  1.000 26.54484 ?  143 LYS   A HE2  1 
ATOM   2186 H  HE3  . LYS   A 1 140 ? 2.38880  -5.25245  -9.98718  1.000 26.54484 ?  143 LYS   A HE3  1 
ATOM   2187 H  HZ1  . LYS   A 1 140 ? 1.02659  -6.28359  -11.47927 1.000 29.83153 ?  143 LYS   A HZ1  1 
ATOM   2188 H  HZ2  . LYS   A 1 140 ? 2.36094  -6.82091  -11.64994 1.000 29.83153 ?  143 LYS   A HZ2  1 
ATOM   2189 H  HZ3  . LYS   A 1 140 ? 1.35183  -7.59466  -10.95615 1.000 29.83153 ?  143 LYS   A HZ3  1 
ATOM   2190 N  N    . VAL   A 1 141 ? 5.72570  -7.26092  -3.53353  1.000 13.60697 ?  144 VAL   A N    1 
ATOM   2191 C  CA   . VAL   A 1 141 ? 6.56883  -7.93319  -2.55531  1.000 12.77922 ?  144 VAL   A CA   1 
ATOM   2192 C  C    . VAL   A 1 141 ? 5.68670  -8.35667  -1.39257  1.000 12.82365 ?  144 VAL   A C    1 
ATOM   2193 O  O    . VAL   A 1 141 ? 4.69038  -7.69803  -1.08796  1.000 14.06180 ?  144 VAL   A O    1 
ATOM   2194 C  CB   . VAL   A 1 141 ? 7.73166  -7.01401  -2.10865  1.000 12.55698 ?  144 VAL   A CB   1 
ATOM   2195 C  CG1  . VAL   A 1 141 ? 7.26590  -5.82571  -1.32254  1.000 13.27260 ?  144 VAL   A CG1  1 
ATOM   2196 C  CG2  . VAL   A 1 141 ? 8.77042  -7.77663  -1.33084  1.000 13.58768 ?  144 VAL   A CG2  1 
ATOM   2197 H  H    . VAL   A 1 141 ? 5.00381  -6.94219  -3.19163  1.000 16.32837 ?  144 VAL   A H    1 
ATOM   2198 H  HA   . VAL   A 1 141 ? 6.95026  -8.73444  -2.94697  1.000 15.33507 ?  144 VAL   A HA   1 
ATOM   2199 H  HB   . VAL   A 1 141 ? 8.13967  -6.67652  -2.92138  1.000 15.06838 ?  144 VAL   A HB   1 
ATOM   2200 H  HG11 . VAL   A 1 141 ? 8.02191  -5.24128  -1.15588  1.000 15.92712 ?  144 VAL   A HG11 1 
ATOM   2201 H  HG12 . VAL   A 1 141 ? 6.58969  -5.35421  -1.83374  1.000 15.92712 ?  144 VAL   A HG12 1 
ATOM   2202 H  HG13 . VAL   A 1 141 ? 6.89172  -6.13062  -0.48116  1.000 15.92712 ?  144 VAL   A HG13 1 
ATOM   2203 H  HG21 . VAL   A 1 141 ? 9.56403  -7.22632  -1.24002  1.000 16.30521 ?  144 VAL   A HG21 1 
ATOM   2204 H  HG22 . VAL   A 1 141 ? 8.41441  -7.99091  -0.45435  1.000 16.30521 ?  144 VAL   A HG22 1 
ATOM   2205 H  HG23 . VAL   A 1 141 ? 8.98666  -8.59266  -1.80858  1.000 16.30521 ?  144 VAL   A HG23 1 
ATOM   2206 N  N    . ASN   A 1 142 ? 6.05220  -9.47582  -0.75502  1.000 12.50046 ?  145 ASN   A N    1 
ATOM   2207 C  CA   A ASN   A 1 142 ? 5.43625  -9.94243  0.47895   0.544 12.48168 ?  145 ASN   A CA   1 
ATOM   2208 C  CA   B ASN   A 1 142 ? 5.43679  -9.94550  0.48316   0.456 13.27854 ?  145 ASN   A CA   1 
ATOM   2209 C  C    . ASN   A 1 142 ? 6.46579  -9.75388  1.58641   1.000 12.64298 ?  145 ASN   A C    1 
ATOM   2210 O  O    . ASN   A 1 142 ? 7.57889  -10.26354 1.49236   1.000 14.88535 ?  145 ASN   A O    1 
ATOM   2211 C  CB   A ASN   A 1 142 ? 5.04868  -11.41335 0.32895   0.544 14.91926 ?  145 ASN   A CB   1 
ATOM   2212 C  CB   B ASN   A 1 142 ? 5.07072  -11.42843 0.38055   0.456 16.82389 ?  145 ASN   A CB   1 
ATOM   2213 C  CG   A ASN   A 1 142 ? 4.23226  -11.90989 1.49109   0.544 18.51933 ?  145 ASN   A CG   1 
ATOM   2214 C  CG   B ASN   A 1 142 ? 4.23033  -11.74437 -0.83290  0.456 21.04995 ?  145 ASN   A CG   1 
ATOM   2215 O  OD1  A ASN   A 1 142 ? 4.59954  -11.70606 2.64022   0.544 20.62410 ?  145 ASN   A OD1  1 
ATOM   2216 O  OD1  B ASN   A 1 142 ? 4.47632  -12.72702 -1.53190  0.456 25.29902 ?  145 ASN   A OD1  1 
ATOM   2217 N  ND2  A ASN   A 1 142 ? 3.09122  -12.53056 1.19794   0.544 23.21035 ?  145 ASN   A ND2  1 
ATOM   2218 N  ND2  B ASN   A 1 142 ? 3.23860  -10.91624 -1.09263  0.456 22.62182 ?  145 ASN   A ND2  1 
ATOM   2219 H  H    . ASN   A 1 142 ? 6.67862  -9.99358  -1.03631  1.000 15.00056 ?  145 ASN   A H    1 
ATOM   2220 H  HA   . ASN   A 1 142 ? 4.63908  -9.43641  0.70112   1.000 15.93424 ?  145 ASN   A HA   1 
ATOM   2221 H  HB2  A ASN   A 1 142 ? 4.52225  -11.52263 -0.47841  0.544 17.90312 ?  145 ASN   A HB2  1 
ATOM   2222 H  HB2  B ASN   A 1 142 ? 5.88578  -11.95133 0.32436   0.456 20.18867 ?  145 ASN   A HB2  1 
ATOM   2223 H  HB3  A ASN   A 1 142 ? 5.85457  -11.95048 0.27477   0.544 17.90312 ?  145 ASN   A HB3  1 
ATOM   2224 H  HB3  B ASN   A 1 142 ? 4.56625  -11.68403 1.16863   0.456 20.18867 ?  145 ASN   A HB3  1 
ATOM   2225 H  HD21 A ASN   A 1 142 ? 2.85451  -12.63027 0.37719   0.544 27.85242 ?  145 ASN   A HD21 1 
ATOM   2226 H  HD21 B ASN   A 1 142 ? 2.73095  -11.05332 -1.77314  0.456 27.14618 ?  145 ASN   A HD21 1 
ATOM   2227 H  HD22 A ASN   A 1 142 ? 2.59100  -12.83170 1.82936   0.544 27.85242 ?  145 ASN   A HD22 1 
ATOM   2228 H  HD22 B ASN   A 1 142 ? 3.09909  -10.23875 -0.58161  0.456 27.14618 ?  145 ASN   A HD22 1 
ATOM   2229 N  N    . ILE   A 1 143 ? 6.10462  -9.01675  2.62579   1.000 12.10496 ?  146 ILE   A N    1 
ATOM   2230 C  CA   . ILE   A 1 143 ? 7.00470  -8.75335  3.73978   1.000 12.33220 ?  146 ILE   A CA   1 
ATOM   2231 C  C    . ILE   A 1 143 ? 6.57495  -9.59628  4.93524   1.000 12.78206 ?  146 ILE   A C    1 
ATOM   2232 O  O    . ILE   A 1 143 ? 5.43876  -9.49469  5.41387   1.000 13.76499 ?  146 ILE   A O    1 
ATOM   2233 C  CB   . ILE   A 1 143 ? 7.06444  -7.25542  4.07807   1.000 12.06585 ?  146 ILE   A CB   1 
ATOM   2234 C  CG1  . ILE   A 1 143 ? 7.57404  -6.44466  2.87330   1.000 12.57163 ?  146 ILE   A CG1  1 
ATOM   2235 C  CG2  . ILE   A 1 143 ? 7.93603  -7.01027  5.31465   1.000 12.58711 ?  146 ILE   A CG2  1 
ATOM   2236 C  CD1  . ILE   A 1 143 ? 9.00094  -6.79418  2.41831   1.000 12.89213 ?  146 ILE   A CD1  1 
ATOM   2237 H  H    . ILE   A 1 143 ? 5.33039  -8.65204  2.71033   1.000 14.52595 ?  146 ILE   A H    1 
ATOM   2238 H  HA   . ILE   A 1 143 ? 7.89871  -9.04235  3.49867   1.000 14.79865 ?  146 ILE   A HA   1 
ATOM   2239 H  HB   . ILE   A 1 143 ? 6.16408  -6.95725  4.28140   1.000 14.47902 ?  146 ILE   A HB   1 
ATOM   2240 H  HG12 . ILE   A 1 143 ? 6.98120  -6.60367  2.12220   1.000 15.08596 ?  146 ILE   A HG12 1 
ATOM   2241 H  HG13 . ILE   A 1 143 ? 7.56539  -5.50388  3.10941   1.000 15.08596 ?  146 ILE   A HG13 1 
ATOM   2242 H  HG21 . ILE   A 1 143 ? 8.05180  -6.05476  5.43502   1.000 15.10453 ?  146 ILE   A HG21 1 
ATOM   2243 H  HG22 . ILE   A 1 143 ? 7.49655  -7.39065  6.09122   1.000 15.10453 ?  146 ILE   A HG22 1 
ATOM   2244 H  HG23 . ILE   A 1 143 ? 8.79853  -7.43387  5.18211   1.000 15.10453 ?  146 ILE   A HG23 1 
ATOM   2245 H  HD11 . ILE   A 1 143 ? 9.28324  -6.15520  1.74533   1.000 15.47056 ?  146 ILE   A HD11 1 
ATOM   2246 H  HD12 . ILE   A 1 143 ? 9.59546  -6.75292  3.18364   1.000 15.47056 ?  146 ILE   A HD12 1 
ATOM   2247 H  HD13 . ILE   A 1 143 ? 9.00311  -7.68975  2.04566   1.000 15.47056 ?  146 ILE   A HD13 1 
ATOM   2248 N  N    . HIS   A 1 144 ? 7.49790  -10.42786 5.42085   1.000 13.01519 ?  147 HIS   A N    1 
ATOM   2249 C  CA   . HIS   A 1 144 ? 7.26532  -11.23667 6.60852   1.000 14.11575 ?  147 HIS   A CA   1 
ATOM   2250 C  C    . HIS   A 1 144 ? 7.51400  -10.44752 7.89610   1.000 13.09869 ?  147 HIS   A C    1 
ATOM   2251 O  O    . HIS   A 1 144 ? 6.76886  -10.60599 8.87470   1.000 14.42666 ?  147 HIS   A O    1 
ATOM   2252 C  CB   . HIS   A 1 144 ? 8.17971  -12.46265 6.59585   1.000 15.37468 ?  147 HIS   A CB   1 
ATOM   2253 C  CG   . HIS   A 1 144 ? 8.12512  -13.28832 5.34687   1.000 17.83116 ?  147 HIS   A CG   1 
ATOM   2254 N  ND1  . HIS   A 1 144 ? 7.02914  -13.34640 4.51124   1.000 22.01624 ?  147 HIS   A ND1  1 
ATOM   2255 C  CD2  . HIS   A 1 144 ? 9.05431  -14.10882 4.80446   1.000 20.31102 ?  147 HIS   A CD2  1 
ATOM   2256 C  CE1  . HIS   A 1 144 ? 7.29557  -14.15198 3.49718   1.000 21.94324 ?  147 HIS   A CE1  1 
ATOM   2257 N  NE2  . HIS   A 1 144 ? 8.51337  -14.63394 3.65705   1.000 22.85672 ?  147 HIS   A NE2  1 
ATOM   2258 H  H    . HIS   A 1 144 ? 8.27671  -10.54164 5.07430   1.000 15.61823 ?  147 HIS   A H    1 
ATOM   2259 H  HA   . HIS   A 1 144 ? 6.34022  -11.52807 6.59476   1.000 16.93890 ?  147 HIS   A HA   1 
ATOM   2260 H  HB2  . HIS   A 1 144 ? 9.09562  -12.16240 6.70469   1.000 18.44962 ?  147 HIS   A HB2  1 
ATOM   2261 H  HB3  . HIS   A 1 144 ? 7.92938  -13.03875 7.33500   1.000 18.44962 ?  147 HIS   A HB3  1 
ATOM   2262 H  HD2  . HIS   A 1 144 ? 9.90157  -14.28436 5.14540   1.000 24.37323 ?  147 HIS   A HD2  1 
ATOM   2263 H  HE1  . HIS   A 1 144 ? 6.72207  -14.34593 2.79123   1.000 26.33189 ?  147 HIS   A HE1  1 
ATOM   2264 H  HE2  . HIS   A 1 144 ? 8.90496  -15.18750 3.12806   1.000 27.42807 ?  147 HIS   A HE2  1 
ATOM   2265 N  N    . SER   A 1 145 ? 8.54353  -9.60262  7.92464   1.000 13.82515 ?  148 SER   A N    1 
ATOM   2266 C  CA   . SER   A 1 145 ? 8.83551  -8.83007  9.12042   1.000 14.21032 ?  148 SER   A CA   1 
ATOM   2267 C  C    . SER   A 1 145 ? 9.74754  -7.65920  8.79013   1.000 14.99463 ?  148 SER   A C    1 
ATOM   2268 O  O    . SER   A 1 145 ? 10.54189 -7.70794  7.84444   1.000 14.22698 ?  148 SER   A O    1 
ATOM   2269 C  CB   . SER   A 1 145 ? 9.49903  -9.69722  10.20451  1.000 17.04413 ?  148 SER   A CB   1 
ATOM   2270 O  OG   . SER   A 1 145 ? 10.71476 -10.27044 9.75185   1.000 18.18569 ?  148 SER   A OG   1 
ATOM   2271 H  H    . SER   A 1 145 ? 9.08091  -9.46301  7.26788   1.000 16.59018 ?  148 SER   A H    1 
ATOM   2272 H  HA   . SER   A 1 145 ? 7.99820  -8.47233  9.45485   1.000 17.05239 ?  148 SER   A HA   1 
ATOM   2273 H  HB2  . SER   A 1 145 ? 9.68530  -9.14143  10.97736  1.000 20.45295 ?  148 SER   A HB2  1 
ATOM   2274 H  HB3  . SER   A 1 145 ? 8.88964  -10.41135 10.44856  1.000 20.45295 ?  148 SER   A HB3  1 
ATOM   2275 H  HG   . SER   A 1 145 ? 11.25748 -9.66459  9.54207   1.000 21.82283 ?  148 SER   A HG   1 
ATOM   2276 N  N    . ILE   A 1 146 ? 9.63592  -6.61722  9.61182   1.000 15.34150 ?  149 ILE   A N    1 
ATOM   2277 C  CA   . ILE   A 1 146 ? 10.53112 -5.46780  9.62928   1.000 16.85095 ?  149 ILE   A CA   1 
ATOM   2278 C  C    . ILE   A 1 146 ? 10.94982 -5.27889  11.07977  1.000 18.33304 ?  149 ILE   A C    1 
ATOM   2279 O  O    . ILE   A 1 146 ? 10.08829 -5.16725  11.95467  1.000 21.77239 ?  149 ILE   A O    1 
ATOM   2280 C  CB   . ILE   A 1 146 ? 9.81694  -4.18280  9.15959   1.000 17.28647 ?  149 ILE   A CB   1 
ATOM   2281 C  CG1  . ILE   A 1 146 ? 9.16555  -4.36416  7.78718   1.000 16.21690 ?  149 ILE   A CG1  1 
ATOM   2282 C  CG2  . ILE   A 1 146 ? 10.78546 -2.98710  9.15644   1.000 19.59664 ?  149 ILE   A CG2  1 
ATOM   2283 C  CD1  . ILE   A 1 146 ? 8.20553  -3.25997  7.41184   1.000 16.21799 ?  149 ILE   A CD1  1 
ATOM   2284 H  H    . ILE   A 1 146 ? 9.01292  -6.55191  10.20106  1.000 18.40979 ?  149 ILE   A H    1 
ATOM   2285 H  HA   . ILE   A 1 146 ? 11.29799 -5.63373  9.05896   1.000 20.22114 ?  149 ILE   A HA   1 
ATOM   2286 H  HB   . ILE   A 1 146 ? 9.10673  -4.00032  9.79457   1.000 20.74377 ?  149 ILE   A HB   1 
ATOM   2287 H  HG12 . ILE   A 1 146 ? 9.86266  -4.39071  7.11321   1.000 19.46028 ?  149 ILE   A HG12 1 
ATOM   2288 H  HG13 . ILE   A 1 146 ? 8.67071  -5.19844  7.78569   1.000 19.46028 ?  149 ILE   A HG13 1 
ATOM   2289 H  HG21 . ILE   A 1 146 ? 10.28172 -2.17307  8.99992   1.000 23.51597 ?  149 ILE   A HG21 1 
ATOM   2290 H  HG22 . ILE   A 1 146 ? 11.23160 -2.93980  10.01646  1.000 23.51597 ?  149 ILE   A HG22 1 
ATOM   2291 H  HG23 . ILE   A 1 146 ? 11.43939 -3.11223  8.45102   1.000 23.51597 ?  149 ILE   A HG23 1 
ATOM   2292 H  HD11 . ILE   A 1 146 ? 7.58570  -3.11788  8.14431   1.000 19.46159 ?  149 ILE   A HD11 1 
ATOM   2293 H  HD12 . ILE   A 1 146 ? 8.70866  -2.44822  7.24208   1.000 19.46159 ?  149 ILE   A HD12 1 
ATOM   2294 H  HD13 . ILE   A 1 146 ? 7.72012  -3.52128  6.61372   1.000 19.46159 ?  149 ILE   A HD13 1 
ATOM   2295 N  N    . GLY   A 1 147 ? 12.24558 -5.23979  11.34115  1.000 16.79405 ?  150 GLY   A N    1 
ATOM   2296 C  CA   . GLY   A 1 147 ? 12.73638 -5.01393  12.68720  1.000 16.16014 ?  150 GLY   A CA   1 
ATOM   2297 C  C    . GLY   A 1 147 ? 13.85695 -3.99761  12.68889  1.000 15.04722 ?  150 GLY   A C    1 
ATOM   2298 O  O    . GLY   A 1 147 ? 14.63652 -3.90679  11.74998  1.000 17.33911 ?  150 GLY   A O    1 
ATOM   2299 H  H    . GLY   A 1 147 ? 12.86412 -5.34188  10.75244  1.000 20.15286 ?  150 GLY   A H    1 
ATOM   2300 H  HA2  . GLY   A 1 147 ? 12.01603 -4.68473  13.24723  1.000 19.39216 ?  150 GLY   A HA2  1 
ATOM   2301 H  HA3  . GLY   A 1 147 ? 13.06959 -5.84604  13.05795  1.000 19.39216 ?  150 GLY   A HA3  1 
ATOM   2302 N  N    . PHE   A 1 148 ? 13.92275 -3.22197  13.75721  1.000 15.33765 ?  151 PHE   A N    1 
ATOM   2303 C  CA   . PHE   A 1 148 ? 14.96937 -2.23933  13.96396  1.000 15.74600 ?  151 PHE   A CA   1 
ATOM   2304 C  C    . PHE   A 1 148 ? 15.77472 -2.61140  15.18953  1.000 16.72569 ?  151 PHE   A C    1 
ATOM   2305 O  O    . PHE   A 1 148 ? 15.21514 -2.96763  16.22354  1.000 19.38467 ?  151 PHE   A O    1 
ATOM   2306 C  CB   . PHE   A 1 148 ? 14.39275 -0.84670  14.19161  1.000 16.95089 ?  151 PHE   A CB   1 
ATOM   2307 C  CG   . PHE   A 1 148 ? 13.68659 -0.29315  12.99821  1.000 17.10895 ?  151 PHE   A CG   1 
ATOM   2308 C  CD1  . PHE   A 1 148 ? 12.37307 -0.63590  12.74143  1.000 21.90962 ?  151 PHE   A CD1  1 
ATOM   2309 C  CD2  . PHE   A 1 148 ? 14.33278 0.58687   12.13949  1.000 17.59737 ?  151 PHE   A CD2  1 
ATOM   2310 C  CE1  . PHE   A 1 148 ? 11.72259 -0.12566  11.65308  1.000 22.89501 ?  151 PHE   A CE1  1 
ATOM   2311 C  CE2  . PHE   A 1 148 ? 13.68997 1.11083   11.05714  1.000 19.99907 ?  151 PHE   A CE2  1 
ATOM   2312 C  CZ   . PHE   A 1 148 ? 12.38699 0.73751   10.79576  1.000 21.44399 ?  151 PHE   A CZ   1 
ATOM   2313 H  H    . PHE   A 1 148 ? 13.35119 -3.24788  14.39928  1.000 18.40517 ?  151 PHE   A H    1 
ATOM   2314 H  HA   . PHE   A 1 148 ? 15.54202 -2.22601  13.18115  1.000 18.89520 ?  151 PHE   A HA   1 
ATOM   2315 H  HB2  . PHE   A 1 148 ? 13.75549 -0.88730  14.92179  1.000 20.34107 ?  151 PHE   A HB2  1 
ATOM   2316 H  HB3  . PHE   A 1 148 ? 15.11647 -0.24114  14.41618  1.000 20.34107 ?  151 PHE   A HB3  1 
ATOM   2317 H  HD1  . PHE   A 1 148 ? 11.92798 -1.21842  13.31367  1.000 26.29154 ?  151 PHE   A HD1  1 
ATOM   2318 H  HD2  . PHE   A 1 148 ? 15.21711 0.82222   12.30525  1.000 21.11684 ?  151 PHE   A HD2  1 
ATOM   2319 H  HE1  . PHE   A 1 148 ? 10.83700 -0.35685  11.48822  1.000 27.47401 ?  151 PHE   A HE1  1 
ATOM   2320 H  HE2  . PHE   A 1 148 ? 14.12566 1.71453   10.49980  1.000 23.99889 ?  151 PHE   A HE2  1 
ATOM   2321 H  HZ   . PHE   A 1 148 ? 11.95326 1.06634   10.04167  1.000 25.73279 ?  151 PHE   A HZ   1 
ATOM   2322 N  N    . SER   A 1 149 ? 17.08327 -2.48733  15.07308  1.000 15.96463 ?  152 SER   A N    1 
ATOM   2323 C  CA   . SER   A 1 149 ? 17.98934 -2.54273  16.21656  1.000 16.86063 ?  152 SER   A CA   1 
ATOM   2324 C  C    . SER   A 1 149 ? 18.66781 -1.18143  16.29691  1.000 16.19811 ?  152 SER   A C    1 
ATOM   2325 O  O    . SER   A 1 149 ? 19.56214 -0.88659  15.49709  1.000 16.44397 ?  152 SER   A O    1 
ATOM   2326 C  CB   . SER   A 1 149 ? 19.00783 -3.65616  16.05125  1.000 21.21184 ?  152 SER   A CB   1 
ATOM   2327 O  OG   . SER   A 1 149 ? 19.91951 -3.61812  17.12995  1.000 26.71533 ?  152 SER   A OG   1 
ATOM   2328 H  H    . SER   A 1 149 ? 17.48609 -2.36666  14.32289  1.000 19.15756 ?  152 SER   A H    1 
ATOM   2329 H  HA   . SER   A 1 149 ? 17.49164 -2.70800  17.03257  1.000 20.23275 ?  152 SER   A HA   1 
ATOM   2330 H  HB2  . SER   A 1 149 ? 18.55126 -4.51197  16.04553  1.000 25.45421 ?  152 SER   A HB2  1 
ATOM   2331 H  HB3  . SER   A 1 149 ? 19.48907 -3.53131  15.21835  1.000 25.45421 ?  152 SER   A HB3  1 
ATOM   2332 H  HG   . SER   A 1 149 ? 20.49184 -4.22693  17.04400  1.000 32.05839 ?  152 SER   A HG   1 
ATOM   2333 N  N    . PHE   A 1 150 ? 18.20267 -0.33528  17.21971  1.000 16.94087 ?  153 PHE   A N    1 
ATOM   2334 C  CA   . PHE   A 1 150 ? 18.68829 1.03446   17.29531  1.000 17.14281 ?  153 PHE   A CA   1 
ATOM   2335 C  C    . PHE   A 1 150 ? 19.97157 1.06489   18.09590  1.000 18.07690 ?  153 PHE   A C    1 
ATOM   2336 O  O    . PHE   A 1 150 ? 20.06525 0.46255   19.16789  1.000 19.51766 ?  153 PHE   A O    1 
ATOM   2337 C  CB   . PHE   A 1 150 ? 17.65039 1.95285   17.93248  1.000 17.48987 ?  153 PHE   A CB   1 
ATOM   2338 C  CG   . PHE   A 1 150 ? 16.41039 2.10641   17.11415  1.000 17.10839 ?  153 PHE   A CG   1 
ATOM   2339 C  CD1  . PHE   A 1 150 ? 16.42620 2.84206   15.92045  1.000 17.92730 ?  153 PHE   A CD1  1 
ATOM   2340 C  CD2  . PHE   A 1 150 ? 15.23506 1.51848   17.50939  1.000 17.32370 ?  153 PHE   A CD2  1 
ATOM   2341 C  CE1  . PHE   A 1 150 ? 15.27508 2.99220   15.15548  1.000 18.47782 ?  153 PHE   A CE1  1 
ATOM   2342 C  CE2  . PHE   A 1 150 ? 14.07966 1.67219   16.73334  1.000 18.33838 ?  153 PHE   A CE2  1 
ATOM   2343 C  CZ   . PHE   A 1 150 ? 14.11391 2.40102   15.55327  1.000 18.44016 ?  153 PHE   A CZ   1 
ATOM   2344 H  H    . PHE   A 1 150 ? 17.60831 -0.53388  17.80869  1.000 20.32905 ?  153 PHE   A H    1 
ATOM   2345 H  HA   . PHE   A 1 150 ? 18.85907 1.37177   16.40203  1.000 20.57138 ?  153 PHE   A HA   1 
ATOM   2346 H  HB2  . PHE   A 1 150 ? 17.39492 1.58666   18.79361  1.000 20.98785 ?  153 PHE   A HB2  1 
ATOM   2347 H  HB3  . PHE   A 1 150 ? 18.04073 2.83317   18.04893  1.000 20.98785 ?  153 PHE   A HB3  1 
ATOM   2348 H  HD1  . PHE   A 1 150 ? 17.21928 3.23576   15.63598  1.000 21.51275 ?  153 PHE   A HD1  1 
ATOM   2349 H  HD2  . PHE   A 1 150 ? 15.20591 1.01796   18.29267  1.000 20.78844 ?  153 PHE   A HD2  1 
ATOM   2350 H  HE1  . PHE   A 1 150 ? 15.29766 3.49528   14.37363  1.000 22.17338 ?  153 PHE   A HE1  1 
ATOM   2351 H  HE2  . PHE   A 1 150 ? 13.28241 1.28234   17.01137  1.000 22.00606 ?  153 PHE   A HE2  1 
ATOM   2352 H  HZ   . PHE   A 1 150 ? 13.34625 2.48577   15.03518  1.000 22.12819 ?  153 PHE   A HZ   1 
ATOM   2353 N  N    . SER   A 1 151 ? 20.95749 1.79423   17.59218  1.000 17.82999 ?  154 SER   A N    1 
ATOM   2354 C  CA   . SER   A 1 151 ? 22.20613 1.83576   18.33652  1.000 19.39110 ?  154 SER   A CA   1 
ATOM   2355 C  C    . SER   A 1 151 ? 22.08902 2.63097   19.62880  1.000 21.55611 ?  154 SER   A C    1 
ATOM   2356 O  O    . SER   A 1 151 ? 23.00750 2.57660   20.44709  1.000 25.66678 ?  154 SER   A O    1 
ATOM   2357 C  CB   . SER   A 1 151 ? 23.35368 2.32235   17.46220  1.000 22.77379 ?  154 SER   A CB   1 
ATOM   2358 O  OG   . SER   A 1 151 ? 23.01144 3.53680   16.87808  1.000 22.88823 ?  154 SER   A OG   1 
ATOM   2359 H  H    . SER   A 1 151 ? 20.92982 2.24848   16.86246  1.000 21.39598 ?  154 SER   A H    1 
ATOM   2360 H  HA   . SER   A 1 151 ? 22.44993 0.93169   18.58974  1.000 23.26931 ?  154 SER   A HA   1 
ATOM   2361 H  HB2  . SER   A 1 151 ? 24.14576 2.44138   18.00932  1.000 27.32855 ?  154 SER   A HB2  1 
ATOM   2362 H  HB3  . SER   A 1 151 ? 23.52625 1.66896   16.76635  1.000 27.32855 ?  154 SER   A HB3  1 
ATOM   2363 H  HG   . SER   A 1 151 ? 23.68809 3.88565   16.52304  1.000 27.46588 ?  154 SER   A HG   1 
ATOM   2364 N  N    . SER   A 1 152 ? 20.98247 3.33321   19.84979  1.000 20.68873 ?  155 SER   A N    1 
ATOM   2365 C  CA   . SER   A 1 152 ? 20.76225 4.01745   21.11893  1.000 24.96904 ?  155 SER   A CA   1 
ATOM   2366 C  C    . SER   A 1 152 ? 20.16568 3.11429   22.19095  1.000 27.79931 ?  155 SER   A C    1 
ATOM   2367 O  O    . SER   A 1 152 ? 20.09931 3.52200   23.36312  1.000 29.09257 ?  155 SER   A O    1 
ATOM   2368 C  CB   . SER   A 1 152 ? 19.82937 5.20953   20.89968  1.000 27.67227 ?  155 SER   A CB   1 
ATOM   2369 O  OG   . SER   A 1 152 ? 18.56580 4.78405   20.40983  1.000 29.34585 ?  155 SER   A OG   1 
ATOM   2370 H  H    . SER   A 1 152 ? 20.34442 3.42878   19.28114  1.000 24.82647 ?  155 SER   A H    1 
ATOM   2371 H  HA   . SER   A 1 152 ? 21.61510 4.34323   21.44667  1.000 29.96285 ?  155 SER   A HA   1 
ATOM   2372 H  HB2  . SER   A 1 152 ? 19.70141 5.66901   21.74431  1.000 33.20673 ?  155 SER   A HB2  1 
ATOM   2373 H  HB3  . SER   A 1 152 ? 20.23206 5.81001   20.25302  1.000 33.20673 ?  155 SER   A HB3  1 
ATOM   2374 H  HG   . SER   A 1 152 ? 18.02316 5.42518   20.41961  1.000 35.21502 ?  155 SER   A HG   1 
ATOM   2375 N  N    . ASP   A 1 153 ? 19.72761 1.91018   21.83821  1.000 30.45440 ?  156 ASP   A N    1 
ATOM   2376 C  CA   . ASP   A 1 153 ? 19.08252 1.03729   22.81999  1.000 40.95790 ?  156 ASP   A CA   1 
ATOM   2377 C  C    . ASP   A 1 153 ? 20.06670 0.12860   23.55258  1.000 36.80676 ?  156 ASP   A C    1 
ATOM   2378 O  O    . ASP   A 1 153 ? 19.79803 -0.33567  24.66677  1.000 38.11772 ?  156 ASP   A O    1 
ATOM   2379 C  CB   . ASP   A 1 153 ? 18.00224 0.18753   22.15235  1.000 59.49750 ?  156 ASP   A CB   1 
ATOM   2380 C  CG   . ASP   A 1 153 ? 16.74149 0.97405   21.86670  1.000 75.23458 ?  156 ASP   A CG   1 
ATOM   2381 O  OD1  . ASP   A 1 153 ? 16.47385 1.95563   22.59349  1.000 79.86639 ?  156 ASP   A OD1  1 
ATOM   2382 O  OD2  . ASP   A 1 153 ? 16.01825 0.60981   20.91799  1.000 79.58122 ?  156 ASP   A OD2  1 
ATOM   2383 O  OXT  . ASP   A 1 153 ? 21.14762 -0.16257  23.05794  1.000 34.56097 ?  156 ASP   A OXT  1 
ATOM   2384 H  H    . ASP   A 1 153 ? 19.79012 1.57770   21.04755  1.000 36.54528 ?  156 ASP   A H    1 
ATOM   2385 H  HA   . ASP   A 1 153 ? 18.67248 1.60762   23.48894  1.000 49.14948 ?  156 ASP   A HA   1 
ATOM   2386 H  HB2  . ASP   A 1 153 ? 18.34205 -0.15294  21.31003  1.000 71.39700 ?  156 ASP   A HB2  1 
ATOM   2387 H  HB3  . ASP   A 1 153 ? 17.77088 -0.54952  22.73898  1.000 71.39700 ?  156 ASP   A HB3  1 
ATOM   2388 N  N    . ASN   B 1 4   ? 53.23692 -16.11453 11.10588  1.000 36.91179 ?  7   ASN   B N    1 
ATOM   2389 C  CA   . ASN   B 1 4   ? 52.80289 -15.50105 9.82551   1.000 33.15348 ?  7   ASN   B CA   1 
ATOM   2390 C  C    . ASN   B 1 4   ? 52.19237 -14.11568 10.01737  1.000 26.65984 ?  7   ASN   B C    1 
ATOM   2391 O  O    . ASN   B 1 4   ? 51.78757 -13.48887 9.03711   1.000 28.11970 ?  7   ASN   B O    1 
ATOM   2392 C  CB   . ASN   B 1 4   ? 51.76948 -16.38715 9.12332   1.000 36.44503 ?  7   ASN   B CB   1 
ATOM   2393 C  CG   . ASN   B 1 4   ? 52.39361 -17.52804 8.35859   1.000 36.79903 ?  7   ASN   B CG   1 
ATOM   2394 O  OD1  . ASN   B 1 4   ? 53.42016 -17.37212 7.69226   1.000 41.30206 ?  7   ASN   B OD1  1 
ATOM   2395 N  ND2  . ASN   B 1 4   ? 51.76877 -18.69236 8.44697   1.000 37.52489 ?  7   ASN   B ND2  1 
ATOM   2396 H  H    . ASN   B 1 4   ? 53.66495 -16.87689 10.93947  1.000 44.29415 ?  7   ASN   B H    1 
ATOM   2397 H  HA   . ASN   B 1 4   ? 53.59201 -15.41247 9.26844   1.000 39.78418 ?  7   ASN   B HA   1 
ATOM   2398 H  HB2  . ASN   B 1 4   ? 51.17335 -16.76430 9.78911   1.000 43.73404 ?  7   ASN   B HB2  1 
ATOM   2399 H  HB3  . ASN   B 1 4   ? 51.26561 -15.84646 8.49510   1.000 43.73404 ?  7   ASN   B HB3  1 
ATOM   2400 H  HD21 . ASN   B 1 4   ? 51.05338 -18.76169 8.91921   1.000 45.02986 ?  7   ASN   B HD21 1 
ATOM   2401 H  HD22 . ASN   B 1 4   ? 52.07840 -19.37911 8.03213   1.000 45.02986 ?  7   ASN   B HD22 1 
ATOM   2402 N  N    . LEU   B 1 5   ? 52.10487 -13.61888 11.25100  1.000 22.28089 ?  8   LEU   B N    1 
ATOM   2403 C  CA   . LEU   B 1 5   ? 51.56587 -12.27797 11.40469  1.000 17.98236 ?  8   LEU   B CA   1 
ATOM   2404 C  C    . LEU   B 1 5   ? 52.45971 -11.26086 10.70347  1.000 17.55174 ?  8   LEU   B C    1 
ATOM   2405 O  O    . LEU   B 1 5   ? 53.65718 -11.46482 10.49071  1.000 19.60453 ?  8   LEU   B O    1 
ATOM   2406 C  CB   . LEU   B 1 5   ? 51.37329 -11.89683 12.86754  1.000 18.14227 ?  8   LEU   B CB   1 
ATOM   2407 C  CG   . LEU   B 1 5   ? 50.29798 -12.68134 13.60681  1.000 20.20283 ?  8   LEU   B CG   1 
ATOM   2408 C  CD1  . LEU   B 1 5   ? 50.29920 -12.27223 15.06690  1.000 22.67080 ?  8   LEU   B CD1  1 
ATOM   2409 C  CD2  . LEU   B 1 5   ? 48.92448 -12.46120 13.03842  1.000 21.96816 ?  8   LEU   B CD2  1 
ATOM   2410 H  H    . LEU   B 1 5   ? 52.33948 -14.01999 11.97465  1.000 26.73706 ?  8   LEU   B H    1 
ATOM   2411 H  HA   . LEU   B 1 5   ? 50.68685 -12.25328 10.99528  1.000 21.57883 ?  8   LEU   B HA   1 
ATOM   2412 H  HB2  . LEU   B 1 5   ? 52.21130 -12.04232 13.33387  1.000 21.77072 ?  8   LEU   B HB2  1 
ATOM   2413 H  HB3  . LEU   B 1 5   ? 51.12895 -10.95903 12.90913  1.000 21.77072 ?  8   LEU   B HB3  1 
ATOM   2414 H  HG   . LEU   B 1 5   ? 50.49935 -13.62545 13.51190  1.000 24.24339 ?  8   LEU   B HG   1 
ATOM   2415 H  HD11 . LEU   B 1 5   ? 49.52228 -12.65581 15.50299  1.000 27.20496 ?  8   LEU   B HD11 1 
ATOM   2416 H  HD12 . LEU   B 1 5   ? 51.10979 -12.60082 15.48626  1.000 27.20496 ?  8   LEU   B HD12 1 
ATOM   2417 H  HD13 . LEU   B 1 5   ? 50.26627 -11.30446 15.12373  1.000 27.20496 ?  8   LEU   B HD13 1 
ATOM   2418 H  HD21 . LEU   B 1 5   ? 48.26885 -12.85403 13.63569  1.000 26.36179 ?  8   LEU   B HD21 1 
ATOM   2419 H  HD22 . LEU   B 1 5   ? 48.76641 -11.50784 12.95474  1.000 26.36179 ?  8   LEU   B HD22 1 
ATOM   2420 H  HD23 . LEU   B 1 5   ? 48.87223 -12.88295 12.16647  1.000 26.36179 ?  8   LEU   B HD23 1 
ATOM   2421 N  N    . GLN   B 1 6   ? 51.84617 -10.14568 10.35933  1.000 15.03967 ?  9   GLN   B N    1 
ATOM   2422 C  CA   . GLN   B 1 6   ? 52.45484 -9.10105  9.56404   1.000 14.10065 ?  9   GLN   B CA   1 
ATOM   2423 C  C    . GLN   B 1 6   ? 52.68906 -7.86844  10.42008  1.000 13.52484 ?  9   GLN   B C    1 
ATOM   2424 O  O    . GLN   B 1 6   ? 51.91271 -7.55002  11.32890  1.000 14.26238 ?  9   GLN   B O    1 
ATOM   2425 C  CB   . GLN   B 1 6   ? 51.52229 -8.76764  8.39861   1.000 14.56622 ?  9   GLN   B CB   1 
ATOM   2426 C  CG   . GLN   B 1 6   ? 51.19932 -9.97983  7.53282   1.000 15.76118 ?  9   GLN   B CG   1 
ATOM   2427 C  CD   . GLN   B 1 6   ? 50.13606 -9.68430  6.51546   1.000 16.44916 ?  9   GLN   B CD   1 
ATOM   2428 O  OE1  . GLN   B 1 6   ? 48.95887 -10.02178 6.69420   1.000 17.80903 ?  9   GLN   B OE1  1 
ATOM   2429 N  NE2  . GLN   B 1 6   ? 50.53243 -9.00439  5.44764   1.000 17.74234 ?  9   GLN   B NE2  1 
ATOM   2430 H  H    . GLN   B 1 6   ? 51.03701 -9.96269  10.58599  1.000 18.04760 ?  9   GLN   B H    1 
ATOM   2431 H  HA   . GLN   B 1 6   ? 53.31751 -9.37884  9.21831   1.000 16.92078 ?  9   GLN   B HA   1 
ATOM   2432 H  HB2  . GLN   B 1 6   ? 50.68819 -8.42049  8.75169   1.000 17.47946 ?  9   GLN   B HB2  1 
ATOM   2433 H  HB3  . GLN   B 1 6   ? 51.94700 -8.10161  7.83565   1.000 17.47946 ?  9   GLN   B HB3  1 
ATOM   2434 H  HG2  . GLN   B 1 6   ? 52.00048 -10.25622 7.06096   1.000 18.91342 ?  9   GLN   B HG2  1 
ATOM   2435 H  HG3  . GLN   B 1 6   ? 50.88298 -10.70047 8.09983   1.000 18.91342 ?  9   GLN   B HG3  1 
ATOM   2436 H  HE21 . GLN   B 1 6   ? 51.35428 -8.76248  5.37257   1.000 21.29081 ?  9   GLN   B HE21 1 
ATOM   2437 H  HE22 . GLN   B 1 6   ? 49.96755 -8.80550  4.83043   1.000 21.29081 ?  9   GLN   B HE22 1 
ATOM   2438 N  N    . ASN   B 1 7   ? 53.76257 -7.16279  10.09810  1.000 13.64520 ?  10  ASN   B N    1 
ATOM   2439 C  CA   . ASN   B 1 7   ? 54.12809 -5.92563  10.77722  1.000 14.11746 ?  10  ASN   B CA   1 
ATOM   2440 C  C    . ASN   B 1 7   ? 54.18052 -6.12924  12.29319  1.000 14.71275 ?  10  ASN   B C    1 
ATOM   2441 O  O    . ASN   B 1 7   ? 53.61578 -5.35690  13.07345  1.000 16.57557 ?  10  ASN   B O    1 
ATOM   2442 C  CB   . ASN   B 1 7   ? 53.22035 -4.75870  10.39999  1.000 15.43657 ?  10  ASN   B CB   1 
ATOM   2443 C  CG   . ASN   B 1 7   ? 53.41437 -4.32026  8.97397   1.000 14.90672 ?  10  ASN   B CG   1 
ATOM   2444 O  OD1  . ASN   B 1 7   ? 52.97780 -5.00877  8.04111   1.000 14.56643 ?  10  ASN   B OD1  1 
ATOM   2445 N  ND2  . ASN   B 1 7   ? 54.11806 -3.20971  8.77631   1.000 16.52961 ?  10  ASN   B ND2  1 
ATOM   2446 H  H    . ASN   B 1 7   ? 54.31072 -7.38411  9.47348   1.000 16.37424 ?  10  ASN   B H    1 
ATOM   2447 H  HA   . ASN   B 1 7   ? 55.01912 -5.68502  10.47876  1.000 16.94095 ?  10  ASN   B HA   1 
ATOM   2448 H  HB2  . ASN   B 1 7   ? 52.29491 -5.02791  10.50950  1.000 18.52389 ?  10  ASN   B HB2  1 
ATOM   2449 H  HB3  . ASN   B 1 7   ? 53.41683 -4.00409  10.97693  1.000 18.52389 ?  10  ASN   B HB3  1 
ATOM   2450 H  HD21 . ASN   B 1 7   ? 54.43803 -2.77815  9.44786   1.000 19.83553 ?  10  ASN   B HD21 1 
ATOM   2451 H  HD22 . ASN   B 1 7   ? 54.25328 -2.92289  7.97690   1.000 19.83553 ?  10  ASN   B HD22 1 
ATOM   2452 N  N    . ILE   B 1 8   ? 54.88376 -7.17553  12.71546  1.000 14.02557 ?  11  ILE   B N    1 
ATOM   2453 C  CA   . ILE   B 1 8   ? 54.98415 -7.48522  14.14043  1.000 14.73824 ?  11  ILE   B CA   1 
ATOM   2454 C  C    . ILE   B 1 8   ? 56.02189 -6.56929  14.76633  1.000 15.32295 ?  11  ILE   B C    1 
ATOM   2455 O  O    . ILE   B 1 8   ? 57.19374 -6.60106  14.37728  1.000 15.96533 ?  11  ILE   B O    1 
ATOM   2456 C  CB   . ILE   B 1 8   ? 55.36355 -8.94885  14.39045  1.000 17.07696 ?  11  ILE   B CB   1 
ATOM   2457 C  CG1  . ILE   B 1 8   ? 54.52089 -9.91949  13.58060  1.000 16.88574 ?  11  ILE   B CG1  1 
ATOM   2458 C  CG2  . ILE   B 1 8   ? 55.22933 -9.25084  15.87195  1.000 19.89545 ?  11  ILE   B CG2  1 
ATOM   2459 C  CD1  . ILE   B 1 8   ? 55.03290 -11.34166 13.69860  1.000 18.06771 ?  11  ILE   B CD1  1 
ATOM   2460 H  H    . ILE   B 1 8   ? 55.30917 -7.71806  12.20137  1.000 16.83069 ?  11  ILE   B H    1 
ATOM   2461 H  HA   . ILE   B 1 8   ? 54.11788 -7.31952  14.54419  1.000 17.68589 ?  11  ILE   B HA   1 
ATOM   2462 H  HB   . ILE   B 1 8   ? 56.28154 -9.06708  14.10026  1.000 20.49235 ?  11  ILE   B HB   1 
ATOM   2463 H  HG12 . ILE   B 1 8   ? 53.60698 -9.89692  13.90488  1.000 20.26289 ?  11  ILE   B HG12 1 
ATOM   2464 H  HG13 . ILE   B 1 8   ? 54.54757 -9.66278  12.64556  1.000 20.26289 ?  11  ILE   B HG13 1 
ATOM   2465 H  HG21 . ILE   B 1 8   ? 55.29071 -10.20962 16.00563  1.000 23.87454 ?  11  ILE   B HG21 1 
ATOM   2466 H  HG22 . ILE   B 1 8   ? 55.94414 -8.80358  16.35143  1.000 23.87454 ?  11  ILE   B HG22 1 
ATOM   2467 H  HG23 . ILE   B 1 8   ? 54.36938 -8.92780  16.18345  1.000 23.87454 ?  11  ILE   B HG23 1 
ATOM   2468 H  HD11 . ILE   B 1 8   ? 54.73124 -11.85071 12.92999  1.000 21.68125 ?  11  ILE   B HD11 1 
ATOM   2469 H  HD12 . ILE   B 1 8   ? 56.00241 -11.32703 13.72585  1.000 21.68125 ?  11  ILE   B HD12 1 
ATOM   2470 H  HD13 . ILE   B 1 8   ? 54.68500 -11.73594 14.51372  1.000 21.68125 ?  11  ILE   B HD13 1 
ATOM   2471 N  N    . ILE   B 1 9   ? 55.60004 -5.78607  15.75553  1.000 15.61635 ?  12  ILE   B N    1 
ATOM   2472 C  CA   . ILE   B 1 9   ? 56.48705 -4.94456  16.54182  1.000 16.87396 ?  12  ILE   B CA   1 
ATOM   2473 C  C    . ILE   B 1 9   ? 56.34052 -5.29952  18.01613  1.000 16.72301 ?  12  ILE   B C    1 
ATOM   2474 O  O    . ILE   B 1 9   ? 55.35083 -5.89766  18.44603  1.000 16.62052 ?  12  ILE   B O    1 
ATOM   2475 C  CB   . ILE   B 1 9   ? 56.25325 -3.43801  16.30102  1.000 18.33919 ?  12  ILE   B CB   1 
ATOM   2476 C  CG1  . ILE   B 1 9   ? 54.86284 -3.01064  16.76580  1.000 17.96256 ?  12  ILE   B CG1  1 
ATOM   2477 C  CG2  . ILE   B 1 9   ? 56.48505 -3.09192  14.82788  1.000 18.47972 ?  12  ILE   B CG2  1 
ATOM   2478 C  CD1  . ILE   B 1 9   ? 54.66341 -1.49600  16.79358  1.000 20.81255 ?  12  ILE   B CD1  1 
ATOM   2479 H  H    . ILE   B 1 9   ? 54.77647 -5.72518  15.99558  1.000 18.73962 ?  12  ILE   B H    1 
ATOM   2480 H  HA   . ILE   B 1 9   ? 57.40209 -5.13959  16.28576  1.000 20.24875 ?  12  ILE   B HA   1 
ATOM   2481 H  HB   . ILE   B 1 9   ? 56.89598 -2.94365  16.83338  1.000 22.00702 ?  12  ILE   B HB   1 
ATOM   2482 H  HG12 . ILE   B 1 9   ? 54.20290 -3.38540  16.16170  1.000 21.55507 ?  12  ILE   B HG12 1 
ATOM   2483 H  HG13 . ILE   B 1 9   ? 54.71765 -3.34518  17.66464  1.000 21.55507 ?  12  ILE   B HG13 1 
ATOM   2484 H  HG21 . ILE   B 1 9   ? 56.72676 -2.15513  14.75781  1.000 22.17566 ?  12  ILE   B HG21 1 
ATOM   2485 H  HG22 . ILE   B 1 9   ? 57.20288 -3.64546  14.48260  1.000 22.17566 ?  12  ILE   B HG22 1 
ATOM   2486 H  HG23 . ILE   B 1 9   ? 55.66897 -3.26099  14.33156  1.000 22.17566 ?  12  ILE   B HG23 1 
ATOM   2487 H  HD11 . ILE   B 1 9   ? 53.92207 -1.28584  17.38277  1.000 24.97506 ?  12  ILE   B HD11 1 
ATOM   2488 H  HD12 . ILE   B 1 9   ? 55.47475 -1.07659  17.12027  1.000 24.97506 ?  12  ILE   B HD12 1 
ATOM   2489 H  HD13 . ILE   B 1 9   ? 54.46977 -1.18644  15.89493  1.000 24.97506 ?  12  ILE   B HD13 1 
ATOM   2490 N  N    . TYR   B 1 10  ? 57.33658 -4.88930  18.79969  1.000 16.92004 ?  13  TYR   B N    1 
ATOM   2491 C  CA   . TYR   B 1 10  ? 57.43892 -5.25358  20.21043  1.000 16.50580 ?  13  TYR   B CA   1 
ATOM   2492 C  C    . TYR   B 1 10  ? 57.65016 -4.02748  21.07875  1.000 16.72742 ?  13  TYR   B C    1 
ATOM   2493 O  O    . TYR   B 1 10  ? 58.32724 -3.07694  20.68706  1.000 18.28202 ?  13  TYR   B O    1 
ATOM   2494 C  CB   . TYR   B 1 10  ? 58.61757 -6.20879  20.43718  1.000 17.87530 ?  13  TYR   B CB   1 
ATOM   2495 C  CG   . TYR   B 1 10  ? 58.45526 -7.47204  19.65841  1.000 19.05139 ?  13  TYR   B CG   1 
ATOM   2496 C  CD1  . TYR   B 1 10  ? 58.91747 -7.55843  18.35551  1.000 22.01823 ?  13  TYR   B CD1  1 
ATOM   2497 C  CD2  . TYR   B 1 10  ? 57.77385 -8.55778  20.19239  1.000 20.78231 ?  13  TYR   B CD2  1 
ATOM   2498 C  CE1  . TYR   B 1 10  ? 58.74287 -8.69364  17.62472  1.000 24.79243 ?  13  TYR   B CE1  1 
ATOM   2499 C  CE2  . TYR   B 1 10  ? 57.60153 -9.70753  19.47317  1.000 22.90365 ?  13  TYR   B CE2  1 
ATOM   2500 C  CZ   . TYR   B 1 10  ? 58.08238 -9.77185  18.18044  1.000 24.59995 ?  13  TYR   B CZ   1 
ATOM   2501 O  OH   . TYR   B 1 10  ? 57.91649 -10.91324 17.42262  1.000 27.16541 ?  13  TYR   B OH   1 
ATOM   2502 H  H    . TYR   B 1 10  ? 57.98036 -4.38699  18.52983  1.000 20.30404 ?  13  TYR   B H    1 
ATOM   2503 H  HA   . TYR   B 1 10  ? 56.60686 -5.67213  20.48138  1.000 19.80696 ?  13  TYR   B HA   1 
ATOM   2504 H  HB2  . TYR   B 1 10  ? 59.43877 -5.77782  20.15293  1.000 21.45036 ?  13  TYR   B HB2  1 
ATOM   2505 H  HB3  . TYR   B 1 10  ? 58.67036 -6.43493  21.37897  1.000 21.45036 ?  13  TYR   B HB3  1 
ATOM   2506 H  HD1  . TYR   B 1 10  ? 59.35328 -6.83054  17.97455  1.000 26.42187 ?  13  TYR   B HD1  1 
ATOM   2507 H  HD2  . TYR   B 1 10  ? 57.42876 -8.50181  21.05418  1.000 24.93877 ?  13  TYR   B HD2  1 
ATOM   2508 H  HE1  . TYR   B 1 10  ? 59.06714 -8.74297  16.75448  1.000 29.75092 ?  13  TYR   B HE1  1 
ATOM   2509 H  HE2  . TYR   B 1 10  ? 57.16570 -10.43753 19.85005  1.000 27.48438 ?  13  TYR   B HE2  1 
ATOM   2510 H  HH   . TYR   B 1 10  ? 57.74464 -10.70714 16.62664  1.000 32.59849 ?  13  TYR   B HH   1 
ATOM   2511 N  N    . ASN   B 1 11  ? 57.07849 -4.07494  22.27595  1.000 16.33109 ?  14  ASN   B N    1 
ATOM   2512 C  CA   . ASN   B 1 11  ? 57.31541 -3.07730  23.30799  1.000 17.86699 ?  14  ASN   B CA   1 
ATOM   2513 C  C    . ASN   B 1 11  ? 57.22830 -1.63298  22.79542  1.000 18.33435 ?  14  ASN   B C    1 
ATOM   2514 O  O    . ASN   B 1 11  ? 58.07537 -0.80565  23.11543  1.000 20.10129 ?  14  ASN   B O    1 
ATOM   2515 C  CB   . ASN   B 1 11  ? 58.65660 -3.30332  23.99157  1.000 19.47287 ?  14  ASN   B CB   1 
ATOM   2516 C  CG   . ASN   B 1 11  ? 58.68542 -4.55549  24.81426  1.000 21.77139 ?  14  ASN   B CG   1 
ATOM   2517 O  OD1  . ASN   B 1 11  ? 57.66678 -5.15358  25.11459  1.000 21.62464 ?  14  ASN   B OD1  1 
ATOM   2518 N  ND2  . ASN   B 1 11  ? 59.87028 -4.92270  25.24865  1.000 25.35097 ?  14  ASN   B ND2  1 
ATOM   2519 H  H    . ASN   B 1 11  ? 56.53380 -4.69434  22.51941  1.000 19.59731 ?  14  ASN   B H    1 
ATOM   2520 H  HA   . ASN   B 1 11  ? 56.61331 -3.17818  23.96963  1.000 21.44039 ?  14  ASN   B HA   1 
ATOM   2521 H  HB2  . ASN   B 1 11  ? 59.34821 -3.37317  23.31505  1.000 23.36745 ?  14  ASN   B HB2  1 
ATOM   2522 H  HB3  . ASN   B 1 11  ? 58.84186 -2.55421  24.57929  1.000 23.36745 ?  14  ASN   B HB3  1 
ATOM   2523 H  HD21 . ASN   B 1 11  ? 60.56388 -4.45244  25.05533  1.000 30.42116 ?  14  ASN   B HD21 1 
ATOM   2524 H  HD22 . ASN   B 1 11  ? 59.95197 -5.63324  25.72620  1.000 30.42116 ?  14  ASN   B HD22 1 
ATOM   2525 N  N    . PRO   B 1 12  ? 56.16314 -1.28101  22.08097  1.000 18.23587 ?  15  PRO   B N    1 
ATOM   2526 C  CA   . PRO   B 1 12  ? 55.99592 0.13133   21.71999  1.000 19.41617 ?  15  PRO   B CA   1 
ATOM   2527 C  C    . PRO   B 1 12  ? 55.83692 0.99096   22.96506  1.000 18.97020 ?  15  PRO   B C    1 
ATOM   2528 O  O    . PRO   B 1 12  ? 55.22936 0.58551   23.96253  1.000 19.45320 ?  15  PRO   B O    1 
ATOM   2529 C  CB   . PRO   B 1 12  ? 54.70696 0.13635   20.89582  1.000 19.86048 ?  15  PRO   B CB   1 
ATOM   2530 C  CG   . PRO   B 1 12  ? 53.93975 -1.04799  21.43197  1.000 18.59722 ?  15  PRO   B CG   1 
ATOM   2531 C  CD   . PRO   B 1 12  ? 54.99503 -2.08766  21.66117  1.000 17.80413 ?  15  PRO   B CD   1 
ATOM   2532 H  HA   . PRO   B 1 12  ? 56.73980 0.44370   21.18150  1.000 23.29941 ?  15  PRO   B HA   1 
ATOM   2533 H  HB2  . PRO   B 1 12  ? 54.22120 0.96403   21.03685  1.000 23.83257 ?  15  PRO   B HB2  1 
ATOM   2534 H  HB3  . PRO   B 1 12  ? 54.91016 0.02734   19.95363  1.000 23.83257 ?  15  PRO   B HB3  1 
ATOM   2535 H  HG2  . PRO   B 1 12  ? 53.49478 -0.81146  22.26080  1.000 22.31666 ?  15  PRO   B HG2  1 
ATOM   2536 H  HG3  . PRO   B 1 12  ? 53.28786 -1.34807  20.77937  1.000 22.31666 ?  15  PRO   B HG3  1 
ATOM   2537 H  HD2  . PRO   B 1 12  ? 54.72898 -2.70402  22.36132  1.000 21.36495 ?  15  PRO   B HD2  1 
ATOM   2538 H  HD3  . PRO   B 1 12  ? 55.18521 -2.57531  20.84451  1.000 21.36495 ?  15  PRO   B HD3  1 
ATOM   2539 N  N    . VAL   B 1 13  ? 56.35818 2.21147   22.88239  1.000 19.21387 ?  16  VAL   B N    1 
ATOM   2540 C  CA   . VAL   B 1 13  ? 56.13367 3.19382   23.93148  1.000 19.21937 ?  16  VAL   B CA   1 
ATOM   2541 C  C    . VAL   B 1 13  ? 54.65247 3.53439   23.96474  1.000 18.30885 ?  16  VAL   B C    1 
ATOM   2542 O  O    . VAL   B 1 13  ? 54.00864 3.68746   22.91641  1.000 18.47075 ?  16  VAL   B O    1 
ATOM   2543 C  CB   . VAL   B 1 13  ? 56.98604 4.44740   23.67182  1.000 21.13202 ?  16  VAL   B CB   1 
ATOM   2544 C  CG1  . VAL   B 1 13  ? 56.63338 5.54786   24.65559  1.000 21.83886 ?  16  VAL   B CG1  1 
ATOM   2545 C  CG2  . VAL   B 1 13  ? 58.46487 4.12115   23.76352  1.000 23.29057 ?  16  VAL   B CG2  1 
ATOM   2546 H  H    . VAL   B 1 13  ? 56.84363 2.49304   22.23073  1.000 23.05664 ?  16  VAL   B H    1 
ATOM   2547 H  HA   . VAL   B 1 13  ? 56.39371 2.82644   24.79073  1.000 23.06325 ?  16  VAL   B HA   1 
ATOM   2548 H  HB   . VAL   B 1 13  ? 56.79779 4.76450   22.77465  1.000 25.35843 ?  16  VAL   B HB   1 
ATOM   2549 H  HG11 . VAL   B 1 13  ? 57.35403 6.19684   24.67513  1.000 26.20663 ?  16  VAL   B HG11 1 
ATOM   2550 H  HG12 . VAL   B 1 13  ? 55.81093 5.97535   24.36973  1.000 26.20663 ?  16  VAL   B HG12 1 
ATOM   2551 H  HG13 . VAL   B 1 13  ? 56.51504 5.15836   25.53603  1.000 26.20663 ?  16  VAL   B HG13 1 
ATOM   2552 H  HG21 . VAL   B 1 13  ? 58.96896 4.94889   23.80399  1.000 27.94868 ?  16  VAL   B HG21 1 
ATOM   2553 H  HG22 . VAL   B 1 13  ? 58.62369 3.59764   24.56454  1.000 27.94868 ?  16  VAL   B HG22 1 
ATOM   2554 H  HG23 . VAL   B 1 13  ? 58.72542 3.61318   22.97932  1.000 27.94868 ?  16  VAL   B HG23 1 
ATOM   2555 N  N    . ILE   B 1 14  ? 54.10633 3.64051   25.16302  1.000 17.32040 ?  17  ILE   B N    1 
ATOM   2556 C  CA   . ILE   B 1 14  ? 52.71819 4.02260   25.38910  1.000 17.01653 ?  17  ILE   B CA   1 
ATOM   2557 C  C    . ILE   B 1 14  ? 52.71368 5.45910   25.89485  1.000 17.86670 ?  17  ILE   B C    1 
ATOM   2558 O  O    . ILE   B 1 14  ? 53.45193 5.77102   26.83580  1.000 19.54647 ?  17  ILE   B O    1 
ATOM   2559 C  CB   . ILE   B 1 14  ? 52.03185 3.07210   26.39071  1.000 18.01276 ?  17  ILE   B CB   1 
ATOM   2560 C  CG1  . ILE   B 1 14  ? 52.17090 1.60888   25.94855  1.000 17.70945 ?  17  ILE   B CG1  1 
ATOM   2561 C  CG2  . ILE   B 1 14  ? 50.58766 3.46195   26.60651  1.000 20.24464 ?  17  ILE   B CG2  1 
ATOM   2562 C  CD1  . ILE   B 1 14  ? 51.58955 1.29152   24.58277  1.000 17.64256 ?  17  ILE   B CD1  1 
ATOM   2563 H  H    . ILE   B 1 14  ? 54.53585 3.49043   25.89280  1.000 20.78448 ?  17  ILE   B H    1 
ATOM   2564 H  HA   . ILE   B 1 14  ? 52.21975 3.99483   24.55742  1.000 20.41984 ?  17  ILE   B HA   1 
ATOM   2565 H  HB   . ILE   B 1 14  ? 52.48576 3.15829   27.24361  1.000 21.61532 ?  17  ILE   B HB   1 
ATOM   2566 H  HG12 . ILE   B 1 14  ? 53.11429 1.38483   25.92180  1.000 21.25134 ?  17  ILE   B HG12 1 
ATOM   2567 H  HG13 . ILE   B 1 14  ? 51.71499 1.04823   26.59564  1.000 21.25134 ?  17  ILE   B HG13 1 
ATOM   2568 H  HG21 . ILE   B 1 14  ? 50.16476 2.80280   27.17886  1.000 24.29357 ?  17  ILE   B HG21 1 
ATOM   2569 H  HG22 . ILE   B 1 14  ? 50.55583 4.33505   27.02791  1.000 24.29357 ?  17  ILE   B HG22 1 
ATOM   2570 H  HG23 . ILE   B 1 14  ? 50.13710 3.49237   25.74804  1.000 24.29357 ?  17  ILE   B HG23 1 
ATOM   2571 H  HD11 . ILE   B 1 14  ? 51.63107 0.33348   24.43674  1.000 21.17107 ?  17  ILE   B HD11 1 
ATOM   2572 H  HD12 . ILE   B 1 14  ? 50.66726 1.59071   24.55486  1.000 21.17107 ?  17  ILE   B HD12 1 
ATOM   2573 H  HD13 . ILE   B 1 14  ? 52.10745 1.75230   23.90428  1.000 21.17107 ?  17  ILE   B HD13 1 
ATOM   2574 N  N    . PRO   B 1 15  ? 51.88786 6.36274   25.32193  1.000 20.07241 ?  18  PRO   B N    1 
ATOM   2575 C  CA   . PRO   B 1 15  ? 50.88262 6.11928   24.27136  1.000 20.17442 ?  18  PRO   B CA   1 
ATOM   2576 C  C    . PRO   B 1 15  ? 51.50852 5.79785   22.93535  1.000 19.00281 ?  18  PRO   B C    1 
ATOM   2577 O  O    . PRO   B 1 15  ? 52.52821 6.35748   22.51081  1.000 20.07881 ?  18  PRO   B O    1 
ATOM   2578 C  CB   . PRO   B 1 15  ? 50.09319 7.44029   24.21853  1.000 21.91428 ?  18  PRO   B CB   1 
ATOM   2579 C  CG   . PRO   B 1 15  ? 51.02997 8.48501   24.75838  1.000 24.01392 ?  18  PRO   B CG   1 
ATOM   2580 C  CD   . PRO   B 1 15  ? 51.85877 7.76255   25.79953  1.000 23.51323 ?  18  PRO   B CD   1 
ATOM   2581 H  HA   . PRO   B 1 15  ? 50.29395 5.39824   24.54424  1.000 24.20930 ?  18  PRO   B HA   1 
ATOM   2582 H  HB2  . PRO   B 1 15  ? 49.84501 7.63839   23.30198  1.000 26.29714 ?  18  PRO   B HB2  1 
ATOM   2583 H  HB3  . PRO   B 1 15  ? 49.29814 7.37028   24.76979  1.000 26.29714 ?  18  PRO   B HB3  1 
ATOM   2584 H  HG2  . PRO   B 1 15  ? 51.59048 8.82756   24.04467  1.000 28.81671 ?  18  PRO   B HG2  1 
ATOM   2585 H  HG3  . PRO   B 1 15  ? 50.52329 9.20880   25.15874  1.000 28.81671 ?  18  PRO   B HG3  1 
ATOM   2586 H  HD2  . PRO   B 1 15  ? 52.75560 8.13000   25.83932  1.000 28.21588 ?  18  PRO   B HD2  1 
ATOM   2587 H  HD3  . PRO   B 1 15  ? 51.43828 7.81857   26.67186  1.000 28.21588 ?  18  PRO   B HD3  1 
ATOM   2588 N  N    . PHE   B 1 16  ? 50.83140 4.89418   22.23630  1.000 18.07456 ?  19  PHE   B N    1 
ATOM   2589 C  CA   . PHE   B 1 16  ? 51.22391 4.43753   20.91756  1.000 17.83435 ?  19  PHE   B CA   1 
ATOM   2590 C  C    . PHE   B 1 16  ? 50.18922 4.91380   19.91089  1.000 17.28374 ?  19  PHE   B C    1 
ATOM   2591 O  O    . PHE   B 1 16  ? 48.99220 4.71806   20.11433  1.000 16.66906 ?  19  PHE   B O    1 
ATOM   2592 C  CB   . PHE   B 1 16  ? 51.27272 2.91150   20.88709  1.000 18.29323 ?  19  PHE   B CB   1 
ATOM   2593 C  CG   . PHE   B 1 16  ? 51.45752 2.35710   19.52099  1.000 18.48522 ?  19  PHE   B CG   1 
ATOM   2594 C  CD1  . PHE   B 1 16  ? 52.71337 2.35196   18.93414  1.000 19.21508 ?  19  PHE   B CD1  1 
ATOM   2595 C  CD2  . PHE   B 1 16  ? 50.37182 1.87880   18.79001  1.000 18.44459 ?  19  PHE   B CD2  1 
ATOM   2596 C  CE1  . PHE   B 1 16  ? 52.89214 1.85183   17.65717  1.000 20.65515 ?  19  PHE   B CE1  1 
ATOM   2597 C  CE2  . PHE   B 1 16  ? 50.55057 1.39054   17.51327  1.000 20.69348 ?  19  PHE   B CE2  1 
ATOM   2598 C  CZ   . PHE   B 1 16  ? 51.80782 1.38445   16.95160  1.000 20.73427 ?  19  PHE   B CZ   1 
ATOM   2599 H  H    . PHE   B 1 16  ? 50.11207 4.51815   22.52050  1.000 21.68948 ?  19  PHE   B H    1 
ATOM   2600 H  HA   . PHE   B 1 16  ? 52.09397 4.79737   20.68431  1.000 21.40122 ?  19  PHE   B HA   1 
ATOM   2601 N  N    . VAL   B 1 17  ? 50.64140 5.53464   18.82850  1.000 16.80648 ?  20  VAL   B N    1 
ATOM   2602 C  CA   . VAL   B 1 17  ? 49.77220 5.89970   17.70697  1.000 16.94539 ?  20  VAL   B CA   1 
ATOM   2603 C  C    . VAL   B 1 17  ? 50.49983 5.48057   16.43690  1.000 17.66685 ?  20  VAL   B C    1 
ATOM   2604 O  O    . VAL   B 1 17  ? 51.56426 6.02247   16.12076  1.000 20.59749 ?  20  VAL   B O    1 
ATOM   2605 C  CB   . VAL   B 1 17  ? 49.45238 7.40039   17.67704  1.000 19.66537 ?  20  VAL   B CB   1 
ATOM   2606 C  CG1  . VAL   B 1 17  ? 48.48283 7.70171   16.55428  1.000 20.96449 ?  20  VAL   B CG1  1 
ATOM   2607 C  CG2  . VAL   B 1 17  ? 48.89081 7.85449   19.00693  1.000 22.12841 ?  20  VAL   B CG2  1 
ATOM   2608 H  H    . VAL   B 1 17  ? 51.46333 5.76082   18.71502  1.000 20.16778 ?  20  VAL   B H    1 
ATOM   2609 H  HA   . VAL   B 1 17  ? 48.93558 5.41293   17.77049  1.000 20.33447 ?  20  VAL   B HA   1 
ATOM   2610 H  HB   . VAL   B 1 17  ? 50.27080 7.89587   17.51707  1.000 23.59845 ?  20  VAL   B HB   1 
ATOM   2611 H  HG11 . VAL   B 1 17  ? 48.09361 8.57820   16.69985  1.000 25.15739 ?  20  VAL   B HG11 1 
ATOM   2612 H  HG12 . VAL   B 1 17  ? 48.96212 7.68852   15.71107  1.000 25.15739 ?  20  VAL   B HG12 1 
ATOM   2613 H  HG13 . VAL   B 1 17  ? 47.78594 7.02702   16.54923  1.000 25.15739 ?  20  VAL   B HG13 1 
ATOM   2614 H  HG21 . VAL   B 1 17  ? 48.55352 8.75930   18.91491  1.000 26.55409 ?  20  VAL   B HG21 1 
ATOM   2615 H  HG22 . VAL   B 1 17  ? 48.17116 7.25797   19.26610  1.000 26.55409 ?  20  VAL   B HG22 1 
ATOM   2616 H  HG23 . VAL   B 1 17  ? 49.59618 7.83050   19.67234  1.000 26.55409 ?  20  VAL   B HG23 1 
ATOM   2617 N  N    . GLY   B 1 18  ? 49.95257 4.51937   15.72627  1.000 17.52758 ?  21  GLY   B N    1 
ATOM   2618 C  CA   . GLY   B 1 18  ? 50.61424 3.97752   14.55144  1.000 19.91892 ?  21  GLY   B CA   1 
ATOM   2619 C  C    . GLY   B 1 18  ? 49.68799 3.89138   13.36178  1.000 17.69543 ?  21  GLY   B C    1 
ATOM   2620 O  O    . GLY   B 1 18  ? 48.51278 3.59607   13.49892  1.000 17.13049 ?  21  GLY   B O    1 
ATOM   2621 H  H    . GLY   B 1 18  ? 49.19223 4.15757   15.90119  1.000 21.03310 ?  21  GLY   B H    1 
ATOM   2622 H  HA2  . GLY   B 1 18  ? 51.36464 4.54464   14.31443  1.000 23.90270 ?  21  GLY   B HA2  1 
ATOM   2623 H  HA3  . GLY   B 1 18  ? 50.94204 3.08623   14.74906  1.000 23.90270 ?  21  GLY   B HA3  1 
ATOM   2624 N  N    . THR   B 1 19  ? 50.24413 4.13321   12.18793  1.000 18.75289 ?  22  THR   B N    1 
ATOM   2625 C  CA   . THR   B 1 19  ? 49.49886 3.93532   10.95554  1.000 18.16585 ?  22  THR   B CA   1 
ATOM   2626 C  C    . THR   B 1 19  ? 49.38110 2.44924   10.67618  1.000 19.36629 ?  22  THR   B C    1 
ATOM   2627 O  O    . THR   B 1 19  ? 50.36959 1.71097   10.73108  1.000 23.34276 ?  22  THR   B O    1 
ATOM   2628 C  CB   . THR   B 1 19  ? 50.20943 4.63638   9.80851   1.000 21.70298 ?  22  THR   B CB   1 
ATOM   2629 O  OG1  . THR   B 1 19  ? 50.25449 6.03514   10.09093  1.000 23.79061 ?  22  THR   B OG1  1 
ATOM   2630 C  CG2  . THR   B 1 19  ? 49.46270 4.41892   8.50385   1.000 22.29934 ?  22  THR   B CG2  1 
ATOM   2631 H  H    . THR   B 1 19  ? 51.04987 4.41212   12.07575  1.000 22.50347 ?  22  THR   B H    1 
ATOM   2632 H  HA   . THR   B 1 19  ? 48.60768 4.31017   11.03423  1.000 21.79902 ?  22  THR   B HA   1 
ATOM   2633 H  HB   . THR   B 1 19  ? 51.10662 4.28186   9.70716   1.000 26.04358 ?  22  THR   B HB   1 
ATOM   2634 H  HG1  . THR   B 1 19  ? 50.86915 6.19774   10.63988  1.000 28.54873 ?  22  THR   B HG1  1 
ATOM   2635 H  HG21 . THR   B 1 19  ? 49.70250 5.10868   7.86539   1.000 26.75921 ?  22  THR   B HG21 1 
ATOM   2636 H  HG22 . THR   B 1 19  ? 49.69040 3.55258   8.13169   1.000 26.75921 ?  22  THR   B HG22 1 
ATOM   2637 H  HG23 . THR   B 1 19  ? 48.50589 4.45300   8.65957   1.000 26.75921 ?  22  THR   B HG23 1 
ATOM   2638 N  N    . ILE   B 1 20  ? 48.16172 2.00985   10.40900  1.000 16.81191 ?  23  ILE   B N    1 
ATOM   2639 C  CA   . ILE   B 1 20  ? 47.92017 0.60301   10.11902  1.000 18.21851 ?  23  ILE   B CA   1 
ATOM   2640 C  C    . ILE   B 1 20  ? 48.36617 0.32982   8.69219   1.000 18.56996 ?  23  ILE   B C    1 
ATOM   2641 O  O    . ILE   B 1 20  ? 48.02542 1.10307   7.76947   1.000 19.85717 ?  23  ILE   B O    1 
ATOM   2642 C  CB   . ILE   B 1 20  ? 46.45910 0.25251   10.32639  1.000 17.39125 ?  23  ILE   B CB   1 
ATOM   2643 C  CG1  . ILE   B 1 20  ? 46.09786 0.49174   11.79056  1.000 17.93668 ?  23  ILE   B CG1  1 
ATOM   2644 C  CG2  . ILE   B 1 20  ? 46.16338 -1.18292  9.91867   1.000 17.94518 ?  23  ILE   B CG2  1 
ATOM   2645 C  CD1  . ILE   B 1 20  ? 44.63055 0.28691   12.10242  1.000 19.58698 ?  23  ILE   B CD1  1 
ATOM   2646 H  H    . ILE   B 1 20  ? 47.45755 2.50314   10.38889  1.000 20.17429 ?  23  ILE   B H    1 
ATOM   2647 H  HA   . ILE   B 1 20  ? 48.44294 0.04890   10.71951  1.000 21.86221 ?  23  ILE   B HA   1 
ATOM   2648 H  HB   . ILE   B 1 20  ? 45.91704 0.82303   9.75931   1.000 20.86950 ?  23  ILE   B HB   1 
ATOM   2649 H  HG12 . ILE   B 1 20  ? 46.60565 -0.12466  12.34110  1.000 21.52401 ?  23  ILE   B HG12 1 
ATOM   2650 H  HG13 . ILE   B 1 20  ? 46.32398 1.40632   12.02146  1.000 21.52401 ?  23  ILE   B HG13 1 
ATOM   2651 H  HG21 . ILE   B 1 20  ? 45.21273 -1.34937  10.01596  1.000 21.53422 ?  23  ILE   B HG21 1 
ATOM   2652 H  HG22 . ILE   B 1 20  ? 46.42847 -1.30964  8.99425   1.000 21.53422 ?  23  ILE   B HG22 1 
ATOM   2653 H  HG23 . ILE   B 1 20  ? 46.66475 -1.78370  10.49190  1.000 21.53422 ?  23  ILE   B HG23 1 
ATOM   2654 H  HD11 . ILE   B 1 20  ? 44.45243 0.59993   13.00308  1.000 23.50438 ?  23  ILE   B HD11 1 
ATOM   2655 H  HD12 . ILE   B 1 20  ? 44.09915 0.79047   11.46608  1.000 23.50438 ?  23  ILE   B HD12 1 
ATOM   2656 H  HD13 . ILE   B 1 20  ? 44.42189 -0.65786  12.03327  1.000 23.50438 ?  23  ILE   B HD13 1 
ATOM   2657 N  N    . PRO   B 1 21  ? 49.12001 -0.74216  8.48713   1.000 19.39085 ?  24  PRO   B N    1 
ATOM   2658 C  CA   . PRO   B 1 21  ? 49.86649 -0.88975  7.24186   1.000 20.16383 ?  24  PRO   B CA   1 
ATOM   2659 C  C    . PRO   B 1 21  ? 49.06364 -1.37392  6.03592   1.000 18.84045 ?  24  PRO   B C    1 
ATOM   2660 O  O    . PRO   B 1 21  ? 49.60472 -1.40702  4.92473   1.000 18.91693 ?  24  PRO   B O    1 
ATOM   2661 C  CB   . PRO   B 1 21  ? 50.97656 -1.88300  7.63760   1.000 20.71342 ?  24  PRO   B CB   1 
ATOM   2662 C  CG   . PRO   B 1 21  ? 50.52528 -2.54430  8.87644   1.000 22.15493 ?  24  PRO   B CG   1 
ATOM   2663 C  CD   . PRO   B 1 21  ? 49.61517 -1.62750  9.56279   1.000 19.04621 ?  24  PRO   B CD   1 
ATOM   2664 H  HA   . PRO   B 1 21  ? 50.26661 -0.04122  6.99529   1.000 24.19659 ?  24  PRO   B HA   1 
ATOM   2665 H  HB2  . PRO   B 1 21  ? 51.09763 -2.53311  6.92795   1.000 24.85610 ?  24  PRO   B HB2  1 
ATOM   2666 H  HB3  . PRO   B 1 21  ? 51.80397 -1.40024  7.78999   1.000 24.85610 ?  24  PRO   B HB3  1 
ATOM   2667 H  HG2  . PRO   B 1 21  ? 50.06604 -3.36816  8.65005   1.000 26.58592 ?  24  PRO   B HG2  1 
ATOM   2668 H  HG3  . PRO   B 1 21  ? 51.29475 -2.73610  9.43503   1.000 26.58592 ?  24  PRO   B HG3  1 
ATOM   2669 H  HD2  . PRO   B 1 21  ? 48.88184 -2.11425  9.97045   1.000 22.85545 ?  24  PRO   B HD2  1 
ATOM   2670 H  HD3  . PRO   B 1 21  ? 50.08886 -1.11549  10.23686  1.000 22.85545 ?  24  PRO   B HD3  1 
ATOM   2671 N  N    . ASP   B 1 22  ? 47.81103 -1.75324  6.19440   1.000 16.22658 ?  25  ASP   B N    1 
ATOM   2672 C  CA   . ASP   B 1 22  ? 46.97148 -2.19723  5.08451   1.000 15.76061 ?  25  ASP   B CA   1 
ATOM   2673 C  C    . ASP   B 1 22  ? 45.54609 -2.01517  5.57424   1.000 15.31046 ?  25  ASP   B C    1 
ATOM   2674 O  O    . ASP   B 1 22  ? 45.30911 -1.64385  6.73014   1.000 15.90164 ?  25  ASP   B O    1 
ATOM   2675 C  CB   . ASP   B 1 22  ? 47.32967 -3.64639  4.71595   1.000 16.33166 ?  25  ASP   B CB   1 
ATOM   2676 C  CG   . ASP   B 1 22  ? 46.91499 -4.06596  3.31777   1.000 20.59287 ?  25  ASP   B CG   1 
ATOM   2677 O  OD1  . ASP   B 1 22  ? 46.11166 -3.36567  2.66393   1.000 22.01290 ?  25  ASP   B OD1  1 
ATOM   2678 O  OD2  . ASP   B 1 22  ? 47.40396 -5.14927  2.89012   1.000 23.71936 ?  25  ASP   B OD2  1 
ATOM   2679 H  H    . ASP   B 1 22  ? 47.40700 -1.76513  6.95349   1.000 19.47190 ?  25  ASP   B H    1 
ATOM   2680 H  HA   . ASP   B 1 22  ? 47.08840 -1.66824  4.27990   1.000 18.91273 ?  25  ASP   B HA   1 
ATOM   2681 H  HB2  . ASP   B 1 22  ? 48.29185 -3.75201  4.77884   1.000 19.59799 ?  25  ASP   B HB2  1 
ATOM   2682 H  HB3  . ASP   B 1 22  ? 46.88891 -4.24199  5.34196   1.000 19.59799 ?  25  ASP   B HB3  1 
ATOM   2683 N  N    . GLN   B 1 23  ? 44.59627 -2.27662  4.68885   1.000 16.05433 ?  26  GLN   B N    1 
ATOM   2684 C  CA   A GLN   B 1 23  ? 43.19462 -2.05265  4.98538   0.568 15.28288 ?  26  GLN   B CA   1 
ATOM   2685 C  CA   B GLN   B 1 23  ? 43.19599 -2.04185  4.98941   0.432 16.57571 ?  26  GLN   B CA   1 
ATOM   2686 C  C    . GLN   B 1 23  ? 42.65873 -3.09993  5.94566   1.000 14.80368 ?  26  GLN   B C    1 
ATOM   2687 O  O    . GLN   B 1 23  ? 43.03260 -4.27137  5.88292   1.000 16.42045 ?  26  GLN   B O    1 
ATOM   2688 C  CB   A GLN   B 1 23  ? 42.38234 -2.21488  3.70151   0.568 16.45485 ?  26  GLN   B CB   1 
ATOM   2689 C  CB   B GLN   B 1 23  ? 42.36639 -2.08566  3.70421   0.432 20.44352 ?  26  GLN   B CB   1 
ATOM   2690 C  CG   A GLN   B 1 23  ? 42.55144 -1.10154  2.73168   0.568 18.96658 ?  26  GLN   B CG   1 
ATOM   2691 C  CG   B GLN   B 1 23  ? 42.68825 -0.98539  2.70387   0.432 24.84198 ?  26  GLN   B CG   1 
ATOM   2692 C  CD   A GLN   B 1 23  ? 42.17589 0.18927   3.37803   0.568 18.55876 ?  26  GLN   B CD   1 
ATOM   2693 C  CD   B GLN   B 1 23  ? 41.69441 -0.92179  1.55757   0.432 28.17208 ?  26  GLN   B CD   1 
ATOM   2694 O  OE1  A GLN   B 1 23  ? 43.03394 1.00883   3.71114   0.568 20.72252 ?  26  GLN   B OE1  1 
ATOM   2695 O  OE1  B GLN   B 1 23  ? 40.70985 -1.66332  1.53025   0.432 29.54312 ?  26  GLN   B OE1  1 
ATOM   2696 N  NE2  A GLN   B 1 23  ? 40.88596 0.36159   3.61570   0.568 18.80605 ?  26  GLN   B NE2  1 
ATOM   2697 N  NE2  B GLN   B 1 23  ? 41.94983 -0.03165  0.60104   0.432 29.81286 ?  26  GLN   B NE2  1 
ATOM   2698 H  H    . GLN   B 1 23  ? 44.73827 -2.58800  3.89988   1.000 19.26520 ?  26  GLN   B H    1 
ATOM   2699 H  HA   . GLN   B 1 23  ? 43.09899 -1.16696  5.36919   1.000 19.89085 ?  26  GLN   B HA   1 
ATOM   2700 H  HB2  A GLN   B 1 23  ? 42.65820 -3.03388  3.26100   0.568 19.74582 ?  26  GLN   B HB2  1 
ATOM   2701 H  HB2  B GLN   B 1 23  ? 42.52367 -2.93582  3.26445   0.432 24.53223 ?  26  GLN   B HB2  1 
ATOM   2702 H  HB3  A GLN   B 1 23  ? 41.44170 -2.26347  3.93330   0.568 19.74582 ?  26  GLN   B HB3  1 
ATOM   2703 H  HB3  B GLN   B 1 23  ? 41.42901 -2.00211  3.93923   0.432 24.53223 ?  26  GLN   B HB3  1 
ATOM   2704 H  HG2  A GLN   B 1 23  ? 43.47774 -1.05159  2.44818   0.568 22.75990 ?  26  GLN   B HG2  1 
ATOM   2705 H  HG2  B GLN   B 1 23  ? 42.67425 -0.12962  3.16034   0.432 29.81038 ?  26  GLN   B HG2  1 
ATOM   2706 H  HG3  A GLN   B 1 23  ? 41.97675 -1.24567  1.96366   0.568 22.75990 ?  26  GLN   B HG3  1 
ATOM   2707 H  HG3  B GLN   B 1 23  ? 43.56812 -1.14703  2.32890   0.432 29.81038 ?  26  GLN   B HG3  1 
ATOM   2708 H  HE21 A GLN   B 1 23  ? 40.32315 -0.25157  3.39918   0.568 22.56726 ?  26  GLN   B HE21 1 
ATOM   2709 H  HE21 B GLN   B 1 23  ? 42.64755 0.46832   0.65411   0.432 35.77544 ?  26  GLN   B HE21 1 
ATOM   2710 H  HE22 A GLN   B 1 23  ? 40.61021 1.08678   3.98673   0.568 22.56726 ?  26  GLN   B HE22 1 
ATOM   2711 H  HE22 B GLN   B 1 23  ? 41.41710 0.04337   -0.06991  0.432 35.77544 ?  26  GLN   B HE22 1 
ATOM   2712 N  N    . LEU   B 1 24  ? 41.72406 -2.68003  6.80046   1.000 14.48155 ?  27  LEU   B N    1 
ATOM   2713 C  CA   . LEU   B 1 24  ? 41.01218 -3.61494  7.67163   1.000 14.20380 ?  27  LEU   B CA   1 
ATOM   2714 C  C    . LEU   B 1 24  ? 39.81571 -4.19764  6.91243   1.000 15.81145 ?  27  LEU   B C    1 
ATOM   2715 O  O    . LEU   B 1 24  ? 38.65358 -3.92958  7.20425   1.000 17.53565 ?  27  LEU   B O    1 
ATOM   2716 C  CB   . LEU   B 1 24  ? 40.57738 -2.93632  8.96297   1.000 15.58911 ?  27  LEU   B CB   1 
ATOM   2717 C  CG   . LEU   B 1 24  ? 41.67982 -2.39046  9.87535   1.000 15.84169 ?  27  LEU   B CG   1 
ATOM   2718 C  CD1  . LEU   B 1 24  ? 41.08295 -1.88714  11.18126  1.000 16.43100 ?  27  LEU   B CD1  1 
ATOM   2719 C  CD2  . LEU   B 1 24  ? 42.78921 -3.37956  10.13645  1.000 17.22556 ?  27  LEU   B CD2  1 
ATOM   2720 H  H    . LEU   B 1 24  ? 41.48504 -1.85922  6.89390   1.000 17.37786 ?  27  LEU   B H    1 
ATOM   2721 H  HA   . LEU   B 1 24  ? 41.61513 -4.33766  7.90619   1.000 17.04456 ?  27  LEU   B HA   1 
ATOM   2722 H  HB2  . LEU   B 1 24  ? 40.00931 -2.18605  8.72784   1.000 18.70694 ?  27  LEU   B HB2  1 
ATOM   2723 H  HB3  . LEU   B 1 24  ? 40.07508 -3.58236  9.48376   1.000 18.70694 ?  27  LEU   B HB3  1 
ATOM   2724 H  HG   . LEU   B 1 24  ? 42.09630 -1.64838  9.40979   1.000 19.01003 ?  27  LEU   B HG   1 
ATOM   2725 H  HD11 . LEU   B 1 24  ? 41.76740 -1.41373  11.67956  1.000 19.71720 ?  27  LEU   B HD11 1 
ATOM   2726 H  HD12 . LEU   B 1 24  ? 40.34577 -1.28910  10.98176  1.000 19.71720 ?  27  LEU   B HD12 1 
ATOM   2727 H  HD13 . LEU   B 1 24  ? 40.76404 -2.64519  11.69560  1.000 19.71720 ?  27  LEU   B HD13 1 
ATOM   2728 H  HD21 . LEU   B 1 24  ? 43.31408 -3.07311  10.89243  1.000 20.67068 ?  27  LEU   B HD21 1 
ATOM   2729 H  HD22 . LEU   B 1 24  ? 42.39999 -4.24593  10.33345  1.000 20.67068 ?  27  LEU   B HD22 1 
ATOM   2730 H  HD23 . LEU   B 1 24  ? 43.35006 -3.44060  9.34738   1.000 20.67068 ?  27  LEU   B HD23 1 
ATOM   2731 N  N    . ASP   B 1 25  ? 40.12834 -5.03042  5.92550   1.000 15.51485 ?  28  ASP   B N    1 
ATOM   2732 C  CA   . ASP   B 1 25  ? 39.10439 -5.76084  5.19096   1.000 15.83459 ?  28  ASP   B CA   1 
ATOM   2733 C  C    . ASP   B 1 25  ? 38.48747 -6.86188  6.06729   1.000 15.89758 ?  28  ASP   B C    1 
ATOM   2734 O  O    . ASP   B 1 25  ? 39.11289 -7.34369  7.00879   1.000 14.76595 ?  28  ASP   B O    1 
ATOM   2735 C  CB   . ASP   B 1 25  ? 39.73316 -6.43350  3.96688   1.000 18.18904 ?  28  ASP   B CB   1 
ATOM   2736 C  CG   . ASP   B 1 25  ? 40.24543 -5.43884  2.93874   1.000 22.36622 ?  28  ASP   B CG   1 
ATOM   2737 O  OD1  . ASP   B 1 25  ? 39.50572 -4.50734  2.59705   1.000 25.72300 ?  28  ASP   B OD1  1 
ATOM   2738 O  OD2  . ASP   B 1 25  ? 41.40567 -5.57615  2.49588   1.000 23.96860 ?  28  ASP   B OD2  1 
ATOM   2739 H  H    . ASP   B 1 25  ? 40.93062 -5.19080  5.66050   1.000 18.61782 ?  28  ASP   B H    1 
ATOM   2740 H  HA   . ASP   B 1 25  ? 38.40935 -5.14253  4.91619   1.000 19.00151 ?  28  ASP   B HA   1 
ATOM   2741 H  HB2  . ASP   B 1 25  ? 40.48288 -6.97665  4.25636   1.000 21.82685 ?  28  ASP   B HB2  1 
ATOM   2742 H  HB3  . ASP   B 1 25  ? 39.06617 -6.99104  3.53655   1.000 21.82685 ?  28  ASP   B HB3  1 
ATOM   2743 N  N    . PRO   B 1 26  ? 37.27210 -7.31195  5.75709   1.000 16.80702 ?  29  PRO   B N    1 
ATOM   2744 C  CA   . PRO   B 1 26  ? 36.70019 -8.43505  6.51568   1.000 16.27471 ?  29  PRO   B CA   1 
ATOM   2745 C  C    . PRO   B 1 26  ? 37.65686 -9.61791  6.53643   1.000 14.24295 ?  29  PRO   B C    1 
ATOM   2746 O  O    . PRO   B 1 26  ? 38.26508 -9.96122  5.52338   1.000 15.33385 ?  29  PRO   B O    1 
ATOM   2747 C  CB   . PRO   B 1 26  ? 35.40519 -8.74520  5.75904   1.000 18.90767 ?  29  PRO   B CB   1 
ATOM   2748 C  CG   . PRO   B 1 26  ? 35.01941 -7.40308  5.19540   1.000 20.87153 ?  29  PRO   B CG   1 
ATOM   2749 C  CD   . PRO   B 1 26  ? 36.31479 -6.76782  4.77553   1.000 20.42199 ?  29  PRO   B CD   1 
ATOM   2750 H  HA   . PRO   B 1 26  ? 36.48484 -8.17564  7.42520   1.000 19.52965 ?  29  PRO   B HA   1 
ATOM   2751 H  HB2  . PRO   B 1 26  ? 35.57025 -9.39190  5.05517   1.000 22.68920 ?  29  PRO   B HB2  1 
ATOM   2752 H  HB3  . PRO   B 1 26  ? 34.72931 -9.08246  6.36760   1.000 22.68920 ?  29  PRO   B HB3  1 
ATOM   2753 H  HG2  . PRO   B 1 26  ? 34.42930 -7.52163  4.43474   1.000 25.04584 ?  29  PRO   B HG2  1 
ATOM   2754 H  HG3  . PRO   B 1 26  ? 34.57877 -6.87271  5.87764   1.000 25.04584 ?  29  PRO   B HG3  1 
ATOM   2755 H  HD2  . PRO   B 1 26  ? 36.55468 -7.03035  3.87307   1.000 24.50638 ?  29  PRO   B HD2  1 
ATOM   2756 H  HD3  . PRO   B 1 26  ? 36.26448 -5.80112  4.83752   1.000 24.50638 ?  29  PRO   B HD3  1 
ATOM   2757 N  N    . GLY   B 1 27  ? 37.79351 -10.23603 7.71038   1.000 13.70675 ?  30  GLY   B N    1 
ATOM   2758 C  CA   . GLY   B 1 27  ? 38.73793 -11.29933 7.93231   1.000 13.46842 ?  30  GLY   B CA   1 
ATOM   2759 C  C    . GLY   B 1 27  ? 40.03755 -10.85164 8.56033   1.000 13.62672 ?  30  GLY   B C    1 
ATOM   2760 O  O    . GLY   B 1 27  ? 40.79890 -11.69669 9.04868   1.000 14.79746 ?  30  GLY   B O    1 
ATOM   2761 H  H    . GLY   B 1 27  ? 37.32967 -10.04177 8.40803   1.000 16.44810 ?  30  GLY   B H    1 
ATOM   2762 H  HA2  . GLY   B 1 27  ? 38.33498 -11.95927 8.51797   1.000 16.16210 ?  30  GLY   B HA2  1 
ATOM   2763 H  HA3  . GLY   B 1 27  ? 38.94551 -11.71678 7.08169   1.000 16.16210 ?  30  GLY   B HA3  1 
ATOM   2764 N  N    . THR   B 1 28  ? 40.31744 -9.55333  8.54800   1.000 12.78996 ?  31  THR   B N    1 
ATOM   2765 C  CA   . THR   B 1 28  ? 41.56097 -9.05372  9.11010   1.000 12.03235 ?  31  THR   B CA   1 
ATOM   2766 C  C    . THR   B 1 28  ? 41.58398 -9.23656  10.61671  1.000 11.89081 ?  31  THR   B C    1 
ATOM   2767 O  O    . THR   B 1 28  ? 40.57720 -9.02546  11.30142  1.000 12.88422 ?  31  THR   B O    1 
ATOM   2768 C  CB   . THR   B 1 28  ? 41.74261 -7.58417  8.72992   1.000 13.70582 ?  31  THR   B CB   1 
ATOM   2769 O  OG1  . THR   B 1 28  ? 41.92933 -7.49640  7.30658   1.000 15.05132 ?  31  THR   B OG1  1 
ATOM   2770 C  CG2  . THR   B 1 28  ? 42.95700 -6.99153  9.44453   1.000 14.61757 ?  31  THR   B CG2  1 
ATOM   2771 H  H    . THR   B 1 28  ? 39.80513 -8.94484  8.22107   1.000 15.34795 ?  31  THR   B H    1 
ATOM   2772 H  HA   . THR   B 1 28  ? 42.31178 -9.55177  8.75075   1.000 14.43882 ?  31  THR   B HA   1 
ATOM   2773 H  HB   . THR   B 1 28  ? 40.96222 -7.07158  8.99287   1.000 16.44698 ?  31  THR   B HB   1 
ATOM   2774 H  HG1  . THR   B 1 28  ? 42.12443 -6.70847  7.09047   1.000 18.06159 ?  31  THR   B HG1  1 
ATOM   2775 H  HG21 . THR   B 1 28  ? 43.18477 -6.13287  9.05501   1.000 17.54109 ?  31  THR   B HG21 1 
ATOM   2776 H  HG22 . THR   B 1 28  ? 42.76005 -6.86772  10.38622  1.000 17.54109 ?  31  THR   B HG22 1 
ATOM   2777 H  HG23 . THR   B 1 28  ? 43.71689 -7.58813  9.35764   1.000 17.54109 ?  31  THR   B HG23 1 
ATOM   2778 N  N    . LEU   B 1 29  ? 42.75221 -9.62382  11.12658  1.000 12.22169 ?  32  LEU   B N    1 
ATOM   2779 C  CA   . LEU   B 1 29  ? 42.98849 -9.71285  12.55674  1.000 12.92800 ?  32  LEU   B CA   1 
ATOM   2780 C  C    . LEU   B 1 29  ? 43.98786 -8.65349  13.00624  1.000 12.44434 ?  32  LEU   B C    1 
ATOM   2781 O  O    . LEU   B 1 29  ? 44.98807 -8.38884  12.32603  1.000 13.39976 ?  32  LEU   B O    1 
ATOM   2782 C  CB   . LEU   B 1 29  ? 43.58417 -11.06773 12.94845  1.000 13.86815 ?  32  LEU   B CB   1 
ATOM   2783 C  CG   . LEU   B 1 29  ? 42.80762 -12.29525 12.48770  1.000 14.85032 ?  32  LEU   B CG   1 
ATOM   2784 C  CD1  . LEU   B 1 29  ? 43.50535 -13.55872 12.92217  1.000 17.23679 ?  32  LEU   B CD1  1 
ATOM   2785 C  CD2  . LEU   B 1 29  ? 41.38511 -12.29310 12.99397  1.000 15.14077 ?  32  LEU   B CD2  1 
ATOM   2786 H  H    . LEU   B 1 29  ? 43.43364 -9.84347  10.65012  1.000 14.66603 ?  32  LEU   B H    1 
ATOM   2787 H  HA   . LEU   B 1 29  ? 42.13591 -9.57844  12.99940  1.000 15.51360 ?  32  LEU   B HA   1 
ATOM   2788 H  HB2  . LEU   B 1 29  ? 44.47326 -11.12956 12.56557  1.000 16.64178 ?  32  LEU   B HB2  1 
ATOM   2789 H  HB3  . LEU   B 1 29  ? 43.63628 -11.10705 13.91626  1.000 16.64178 ?  32  LEU   B HB3  1 
ATOM   2790 H  HG   . LEU   B 1 29  ? 42.77051 -12.27118 11.51871  1.000 17.82039 ?  32  LEU   B HG   1 
ATOM   2791 H  HD11 . LEU   B 1 29  ? 43.08514 -14.31709 12.48721  1.000 20.68414 ?  32  LEU   B HD11 1 
ATOM   2792 H  HD12 . LEU   B 1 29  ? 44.43980 -13.50714 12.66713  1.000 20.68414 ?  32  LEU   B HD12 1 
ATOM   2793 H  HD13 . LEU   B 1 29  ? 43.42968 -13.64608 13.88526  1.000 20.68414 ?  32  LEU   B HD13 1 
ATOM   2794 H  HD21 . LEU   B 1 29  ? 40.97742 -13.15024 12.79395  1.000 18.16892 ?  32  LEU   B HD21 1 
ATOM   2795 H  HD22 . LEU   B 1 29  ? 41.39132 -12.14544 13.95264  1.000 18.16892 ?  32  LEU   B HD22 1 
ATOM   2796 H  HD23 . LEU   B 1 29  ? 40.89403 -11.58228 12.55297  1.000 18.16892 ?  32  LEU   B HD23 1 
ATOM   2797 N  N    . ILE   B 1 30  ? 43.73126 -8.09072  14.17927  1.000 11.83081 ?  33  ILE   B N    1 
ATOM   2798 C  CA   . ILE   B 1 30  ? 44.69544 -7.30229  14.93632  1.000 11.59564 ?  33  ILE   B CA   1 
ATOM   2799 C  C    . ILE   B 1 30  ? 44.97425 -8.06991  16.21900  1.000 11.43511 ?  33  ILE   B C    1 
ATOM   2800 O  O    . ILE   B 1 30  ? 44.04420 -8.37329  16.97423  1.000 12.62642 ?  33  ILE   B O    1 
ATOM   2801 C  CB   . ILE   B 1 30  ? 44.14862 -5.90247  15.24720  1.000 12.75683 ?  33  ILE   B CB   1 
ATOM   2802 C  CG1  . ILE   B 1 30  ? 43.61684 -5.21050  13.98417  1.000 13.67524 ?  33  ILE   B CG1  1 
ATOM   2803 C  CG2  . ILE   B 1 30  ? 45.20947 -5.06619  15.96150  1.000 14.67252 ?  33  ILE   B CG2  1 
ATOM   2804 C  CD1  . ILE   B 1 30  ? 42.92951 -3.90362  14.27823  1.000 17.27165 ?  33  ILE   B CD1  1 
ATOM   2805 H  H    . ILE   B 1 30  ? 42.97070 -8.15417  14.57567  1.000 14.19698 ?  33  ILE   B H    1 
ATOM   2806 H  HA   . ILE   B 1 30  ? 45.52138 -7.20484  14.43710  1.000 13.91477 ?  33  ILE   B HA   1 
ATOM   2807 H  HB   . ILE   B 1 30  ? 43.39144 -5.99790  15.84593  1.000 15.30820 ?  33  ILE   B HB   1 
ATOM   2808 H  HG12 . ILE   B 1 30  ? 44.35954 -5.03084  13.38666  1.000 16.41029 ?  33  ILE   B HG12 1 
ATOM   2809 H  HG13 . ILE   B 1 30  ? 42.97600 -5.79532  13.55034  1.000 16.41029 ?  33  ILE   B HG13 1 
ATOM   2810 H  HG21 . ILE   B 1 30  ? 44.85323 -4.17947  16.12801  1.000 17.60702 ?  33  ILE   B HG21 1 
ATOM   2811 H  HG22 . ILE   B 1 30  ? 45.43641 -5.49463  16.80164  1.000 17.60702 ?  33  ILE   B HG22 1 
ATOM   2812 H  HG23 . ILE   B 1 30  ? 45.99650 -5.00597  15.39771  1.000 17.60702 ?  33  ILE   B HG23 1 
ATOM   2813 H  HD11 . ILE   B 1 30  ? 42.46573 -3.60424  13.48062  1.000 20.72598 ?  33  ILE   B HD11 1 
ATOM   2814 H  HD12 . ILE   B 1 30  ? 42.29493 -4.03591  14.99983  1.000 20.72598 ?  33  ILE   B HD12 1 
ATOM   2815 H  HD13 . ILE   B 1 30  ? 43.59537 -3.24834  14.53928  1.000 20.72598 ?  33  ILE   B HD13 1 
ATOM   2816 N  N    . VAL   B 1 31  ? 46.23991 -8.39496  16.45858  1.000 11.55086 ?  34  VAL   B N    1 
ATOM   2817 C  CA   . VAL   B 1 31  ? 46.64539 -9.24107  17.57413  1.000 11.82789 ?  34  VAL   B CA   1 
ATOM   2818 C  C    . VAL   B 1 31  ? 47.55365 -8.43039  18.49192  1.000 12.22648 ?  34  VAL   B C    1 
ATOM   2819 O  O    . VAL   B 1 31  ? 48.61638 -7.96238  18.06418  1.000 12.91868 ?  34  VAL   B O    1 
ATOM   2820 C  CB   . VAL   B 1 31  ? 47.36874 -10.50016 17.06951  1.000 12.94338 ?  34  VAL   B CB   1 
ATOM   2821 C  CG1  . VAL   B 1 31  ? 47.72187 -11.38164 18.22328  1.000 14.34642 ?  34  VAL   B CG1  1 
ATOM   2822 C  CG2  . VAL   B 1 31  ? 46.51208 -11.25590 16.06882  1.000 13.90402 ?  34  VAL   B CG2  1 
ATOM   2823 H  H    . VAL   B 1 31  ? 46.89956 -8.12963  15.97477  1.000 13.86103 ?  34  VAL   B H    1 
ATOM   2824 H  HA   . VAL   B 1 31  ? 45.86309 -9.50107  18.08530  1.000 14.19347 ?  34  VAL   B HA   1 
ATOM   2825 H  HB   . VAL   B 1 31  ? 48.18446 -10.23260 16.61795  1.000 15.53205 ?  34  VAL   B HB   1 
ATOM   2826 H  HG11 . VAL   B 1 31  ? 48.08676 -12.21413 17.88458  1.000 17.21570 ?  34  VAL   B HG11 1 
ATOM   2827 H  HG12 . VAL   B 1 31  ? 48.38107 -10.93152 18.77441  1.000 17.21570 ?  34  VAL   B HG12 1 
ATOM   2828 H  HG13 . VAL   B 1 31  ? 46.92168 -11.55814 18.74235  1.000 17.21570 ?  34  VAL   B HG13 1 
ATOM   2829 H  HG21 . VAL   B 1 31  ? 46.99341 -12.04438 15.77298  1.000 16.68482 ?  34  VAL   B HG21 1 
ATOM   2830 H  HG22 . VAL   B 1 31  ? 45.68177 -11.51658 16.49722  1.000 16.68482 ?  34  VAL   B HG22 1 
ATOM   2831 H  HG23 . VAL   B 1 31  ? 46.32665 -10.67820 15.31200  1.000 16.68482 ?  34  VAL   B HG23 1 
ATOM   2832 N  N    . ILE   B 1 32  ? 47.12723 -8.25312  19.74231  1.000 11.81966 ?  35  ILE   B N    1 
ATOM   2833 C  CA   . ILE   B 1 32  ? 47.81464 -7.39297  20.69082  1.000 12.01203 ?  35  ILE   B CA   1 
ATOM   2834 C  C    . ILE   B 1 32  ? 48.07326 -8.19832  21.95900  1.000 12.33181 ?  35  ILE   B C    1 
ATOM   2835 O  O    . ILE   B 1 32  ? 47.12888 -8.65780  22.60775  1.000 13.43585 ?  35  ILE   B O    1 
ATOM   2836 C  CB   . ILE   B 1 32  ? 46.97904 -6.14158  21.01165  1.000 12.54918 ?  35  ILE   B CB   1 
ATOM   2837 C  CG1  . ILE   B 1 32  ? 46.69959 -5.34152  19.73151  1.000 13.44079 ?  35  ILE   B CG1  1 
ATOM   2838 C  CG2  . ILE   B 1 32  ? 47.64968 -5.28530  22.05529  1.000 13.79119 ?  35  ILE   B CG2  1 
ATOM   2839 C  CD1  . ILE   B 1 32  ? 45.61773 -4.27198  19.90990  1.000 14.92022 ?  35  ILE   B CD1  1 
ATOM   2840 H  H    . ILE   B 1 32  ? 46.42610 -8.63107  20.06661  1.000 14.18359 ?  35  ILE   B H    1 
ATOM   2841 H  HA   . ILE   B 1 32  ? 48.67093 -7.11961  20.32620  1.000 14.41444 ?  35  ILE   B HA   1 
ATOM   2842 H  HB   . ILE   B 1 32  ? 46.13061 -6.43502  21.37903  1.000 15.05902 ?  35  ILE   B HB   1 
ATOM   2843 H  HG12 . ILE   B 1 32  ? 47.51599 -4.89648  19.45522  1.000 16.12894 ?  35  ILE   B HG12 1 
ATOM   2844 H  HG13 . ILE   B 1 32  ? 46.40365 -5.95208  19.03830  1.000 16.12894 ?  35  ILE   B HG13 1 
ATOM   2845 H  HG21 . ILE   B 1 32  ? 47.15329 -4.45747  22.15118  1.000 16.54943 ?  35  ILE   B HG21 1 
ATOM   2846 H  HG22 . ILE   B 1 32  ? 47.65943 -5.76471  22.89848  1.000 16.54943 ?  35  ILE   B HG22 1 
ATOM   2847 H  HG23 . ILE   B 1 32  ? 48.55782 -5.09554  21.77215  1.000 16.54943 ?  35  ILE   B HG23 1 
ATOM   2848 H  HD11 . ILE   B 1 32  ? 45.38246 -3.91262  19.04018  1.000 17.90427 ?  35  ILE   B HD11 1 
ATOM   2849 H  HD12 . ILE   B 1 32  ? 44.83862 -4.67660  20.32240  1.000 17.90427 ?  35  ILE   B HD12 1 
ATOM   2850 H  HD13 . ILE   B 1 32  ? 45.96297 -3.56517  20.47747  1.000 17.90427 ?  35  ILE   B HD13 1 
ATOM   2851 N  N    . ARG   B 1 33  ? 49.34377 -8.38187  22.30595  1.000 12.67007 ?  36  ARG   B N    1 
ATOM   2852 C  CA   . ARG   B 1 33  ? 49.72200 -9.08205  23.52279  1.000 13.33412 ?  36  ARG   B CA   1 
ATOM   2853 C  C    . ARG   B 1 33  ? 50.24956 -8.06473  24.52074  1.000 13.83002 ?  36  ARG   B C    1 
ATOM   2854 O  O    . ARG   B 1 33  ? 50.96014 -7.13462  24.13622  1.000 14.14889 ?  36  ARG   B O    1 
ATOM   2855 C  CB   . ARG   B 1 33  ? 50.79766 -10.12824 23.24395  1.000 15.21408 ?  36  ARG   B CB   1 
ATOM   2856 C  CG   . ARG   B 1 33  ? 50.25143 -11.30012 22.45471  1.000 19.09910 ?  36  ARG   B CG   1 
ATOM   2857 C  CD   . ARG   B 1 33  ? 51.30007 -12.40093 22.31723  1.000 25.18064 ?  36  ARG   B CD   1 
ATOM   2858 N  NE   . ARG   B 1 33  ? 50.69991 -13.63731 21.82613  1.000 32.46420 ?  36  ARG   B NE   1 
ATOM   2859 C  CZ   . ARG   B 1 33  ? 51.32112 -14.80871 21.77631  1.000 38.02625 ?  36  ARG   B CZ   1 
ATOM   2860 N  NH1  . ARG   B 1 33  ? 52.55910 -14.95579 22.22274  1.000 39.94643 ?  36  ARG   B NH1  1 
ATOM   2861 N  NH2  . ARG   B 1 33  ? 50.68544 -15.85879 21.26208  1.000 40.03484 ?  36  ARG   B NH2  1 
ATOM   2862 H  H    . ARG   B 1 33  ? 50.01315 -8.10417  21.84290  1.000 15.20409 ?  36  ARG   B H    1 
ATOM   2863 H  HA   . ARG   B 1 33  ? 48.95268 -9.53697  23.89975  1.000 16.00094 ?  36  ARG   B HA   1 
ATOM   2864 N  N    . GLY   B 1 34  ? 49.93015 -8.24040  25.79846  1.000 14.10840 ?  37  GLY   B N    1 
ATOM   2865 C  CA   . GLY   B 1 34  ? 50.40051 -7.29617  26.79598  1.000 15.13082 ?  37  GLY   B CA   1 
ATOM   2866 C  C    . GLY   B 1 34  ? 50.02833 -7.73670  28.18664  1.000 16.29141 ?  37  GLY   B C    1 
ATOM   2867 O  O    . GLY   B 1 34  ? 49.67192 -8.89631  28.40781  1.000 17.43544 ?  37  GLY   B O    1 
ATOM   2868 H  H    . GLY   B 1 34  ? 49.45190 -8.88588  26.10543  1.000 16.93008 ?  37  GLY   B H    1 
ATOM   2869 H  HA2  . GLY   B 1 34  ? 51.36614 -7.22089  26.74306  1.000 18.15698 ?  37  GLY   B HA2  1 
ATOM   2870 H  HA3  . GLY   B 1 34  ? 50.00636 -6.42532  26.63116  1.000 18.15698 ?  37  GLY   B HA3  1 
ATOM   2871 N  N    . HIS   B 1 35  ? 50.12740 -6.78548  29.12269  1.000 16.93716 ?  38  HIS   B N    1 
ATOM   2872 C  CA   . HIS   B 1 35  ? 49.73514 -7.03307  30.49693  1.000 18.20163 ?  38  HIS   B CA   1 
ATOM   2873 C  C    . HIS   B 1 35  ? 49.23853 -5.75190  31.13277  1.000 19.55788 ?  38  HIS   B C    1 
ATOM   2874 O  O    . HIS   B 1 35  ? 49.54541 -4.64881  30.68418  1.000 19.82241 ?  38  HIS   B O    1 
ATOM   2875 C  CB   . HIS   B 1 35  ? 50.89045 -7.63821  31.31353  1.000 19.91687 ?  38  HIS   B CB   1 
ATOM   2876 C  CG   . HIS   B 1 35  ? 51.94545 -6.66176  31.76749  1.000 22.59381 ?  38  HIS   B CG   1 
ATOM   2877 N  ND1  . HIS   B 1 35  ? 53.18882 -6.56510  31.17535  1.000 23.29141 ?  38  HIS   B ND1  1 
ATOM   2878 C  CD2  . HIS   B 1 35  ? 51.98621 -5.83429  32.83639  1.000 24.27713 ?  38  HIS   B CD2  1 
ATOM   2879 C  CE1  . HIS   B 1 35  ? 53.92989 -5.68914  31.83242  1.000 24.34862 ?  38  HIS   B CE1  1 
ATOM   2880 N  NE2  . HIS   B 1 35  ? 53.21302 -5.21207  32.83051  1.000 24.82515 ?  38  HIS   B NE2  1 
ATOM   2881 H  H    . HIS   B 1 35  ? 50.42036 -5.98998  28.97798  1.000 20.32459 ?  38  HIS   B H    1 
ATOM   2882 H  HA   . HIS   B 1 35  ? 48.99582 -7.66099  30.50225  1.000 21.84196 ?  38  HIS   B HA   1 
ATOM   2883 H  HB2  . HIS   B 1 35  ? 50.51854 -8.05145  32.10840  1.000 23.90025 ?  38  HIS   B HB2  1 
ATOM   2884 H  HB3  . HIS   B 1 35  ? 51.33226 -8.30727  30.76757  1.000 23.90025 ?  38  HIS   B HB3  1 
ATOM   2885 H  HD1  . HIS   B 1 35  ? 53.44305 -7.00793  30.48335  1.000 27.94970 ?  38  HIS   B HD1  1 
ATOM   2886 H  HD2  . HIS   B 1 35  ? 51.30879 -5.70886  33.46111  1.000 29.13255 ?  38  HIS   B HD2  1 
ATOM   2887 H  HE1  . HIS   B 1 35  ? 54.80491 -5.45095  31.62623  1.000 29.21834 ?  38  HIS   B HE1  1 
ATOM   2888 N  N    . VAL   B 1 36  ? 48.45039 -5.91767  32.18566  1.000 20.03288 ?  39  VAL   B N    1 
ATOM   2889 C  CA   . VAL   B 1 36  ? 47.84436 -4.79949  32.90184  1.000 19.72160 ?  39  VAL   B CA   1 
ATOM   2890 C  C    . VAL   B 1 36  ? 48.71150 -4.47292  34.11407  1.000 19.94189 ?  39  VAL   B C    1 
ATOM   2891 O  O    . VAL   B 1 36  ? 48.89134 -5.34573  34.98064  1.000 20.76036 ?  39  VAL   B O    1 
ATOM   2892 C  CB   . VAL   B 1 36  ? 46.41959 -5.15480  33.34298  1.000 20.58986 ?  39  VAL   B CB   1 
ATOM   2893 C  CG1  . VAL   B 1 36  ? 45.81043 -3.99891  34.10767  1.000 20.23562 ?  39  VAL   B CG1  1 
ATOM   2894 C  CG2  . VAL   B 1 36  ? 45.55018 -5.50665  32.11596  1.000 20.96467 ?  39  VAL   B CG2  1 
ATOM   2895 H  H    . VAL   B 1 36  ? 48.24594 -6.68612  32.51320  1.000 24.03945 ?  39  VAL   B H    1 
ATOM   2896 H  HA   . VAL   B 1 36  ? 47.82302 -4.01868  32.32670  1.000 23.66592 ?  39  VAL   B HA   1 
ATOM   2897 H  HB   . VAL   B 1 36  ? 46.44952 -5.92932  33.92617  1.000 24.70783 ?  39  VAL   B HB   1 
ATOM   2898 H  HG11 . VAL   B 1 36  ? 44.88896 -4.21284  34.32220  1.000 24.28274 ?  39  VAL   B HG11 1 
ATOM   2899 H  HG12 . VAL   B 1 36  ? 46.31600 -3.85860  34.92353  1.000 24.28274 ?  39  VAL   B HG12 1 
ATOM   2900 H  HG13 . VAL   B 1 36  ? 45.84513 -3.20193  33.55583  1.000 24.28274 ?  39  VAL   B HG13 1 
ATOM   2901 H  HG21 . VAL   B 1 36  ? 44.62464 -5.58281  32.39610  1.000 25.15761 ?  39  VAL   B HG21 1 
ATOM   2902 H  HG22 . VAL   B 1 36  ? 45.63861 -4.80311  31.45406  1.000 25.15761 ?  39  VAL   B HG22 1 
ATOM   2903 H  HG23 . VAL   B 1 36  ? 45.85395 -6.34988  31.74502  1.000 25.15761 ?  39  VAL   B HG23 1 
ATOM   2904 N  N    . PRO   B 1 37  ? 49.24175 -3.24833  34.22674  1.000 21.69759 ?  40  PRO   B N    1 
ATOM   2905 C  CA   . PRO   B 1 37  ? 50.00884 -2.86454  35.41441  1.000 22.85930 ?  40  PRO   B CA   1 
ATOM   2906 C  C    . PRO   B 1 37  ? 49.19801 -2.95046  36.69956  1.000 21.58858 ?  40  PRO   B C    1 
ATOM   2907 O  O    . PRO   B 1 37  ? 47.96693 -2.84550  36.71908  1.000 20.71803 ?  40  PRO   B O    1 
ATOM   2908 C  CB   . PRO   B 1 37  ? 50.41416 -1.41260  35.11389  1.000 23.65304 ?  40  PRO   B CB   1 
ATOM   2909 C  CG   . PRO   B 1 37  ? 50.41049 -1.31158  33.61658  1.000 23.62696 ?  40  PRO   B CG   1 
ATOM   2910 C  CD   . PRO   B 1 37  ? 49.27912 -2.19997  33.18638  1.000 22.79055 ?  40  PRO   B CD   1 
ATOM   2911 H  HA   . PRO   B 1 37  ? 50.79291 -3.42923  35.49969  1.000 27.43116 ?  40  PRO   B HA   1 
ATOM   2912 H  HB2  . PRO   B 1 37  ? 49.76967 -0.80207  35.50476  1.000 28.38365 ?  40  PRO   B HB2  1 
ATOM   2913 H  HB3  . PRO   B 1 37  ? 51.29819 -1.23561  35.47175  1.000 28.38365 ?  40  PRO   B HB3  1 
ATOM   2914 H  HG2  . PRO   B 1 37  ? 50.25591 -0.39331  33.34492  1.000 28.35235 ?  40  PRO   B HG2  1 
ATOM   2915 H  HG3  . PRO   B 1 37  ? 51.25594 -1.62540  33.25933  1.000 28.35235 ?  40  PRO   B HG3  1 
ATOM   2916 H  HD2  . PRO   B 1 37  ? 48.44402 -1.70696  33.16522  1.000 27.34866 ?  40  PRO   B HD2  1 
ATOM   2917 H  HD3  . PRO   B 1 37  ? 49.45818 -2.58679  32.31505  1.000 27.34866 ?  40  PRO   B HD3  1 
ATOM   2918 N  N    . SER   B 1 38  ? 49.93004 -3.12086  37.79911  1.000 22.85752 ?  41  SER   B N    1 
ATOM   2919 C  CA   . SER   B 1 38  ? 49.27942 -3.33412  39.08367  1.000 23.24330 ?  41  SER   B CA   1 
ATOM   2920 C  C    . SER   B 1 38  ? 48.45455 -2.13419  39.53786  1.000 22.33073 ?  41  SER   B C    1 
ATOM   2921 O  O    . SER   B 1 38  ? 47.50938 -2.30830  40.31688  1.000 24.32101 ?  41  SER   B O    1 
ATOM   2922 C  CB   . SER   B 1 38  ? 50.32151 -3.66099  40.16227  1.000 27.14458 ?  41  SER   B CB   1 
ATOM   2923 O  OG   . SER   B 1 38  ? 50.88850 -4.93061  39.91410  1.000 28.83190 ?  41  SER   B OG   1 
ATOM   2924 H  H    . SER   B 1 38  ? 50.78961 -3.11712  37.82611  1.000 27.42902 ?  41  SER   B H    1 
ATOM   2925 H  HA   . SER   B 1 38  ? 48.67993 -4.08948  38.97909  1.000 27.89196 ?  41  SER   B HA   1 
ATOM   2926 H  HB2  . SER   B 1 38  ? 51.02130 -2.98953  40.14433  1.000 32.57350 ?  41  SER   B HB2  1 
ATOM   2927 H  HB3  . SER   B 1 38  ? 49.89053 -3.66788  41.03125  1.000 32.57350 ?  41  SER   B HB3  1 
ATOM   2928 H  HG   . SER   B 1 38  ? 51.28431 -5.20777  40.60121  1.000 34.59828 ?  41  SER   B HG   1 
ATOM   2929 N  N    . ASP   B 1 39  ? 48.79969 -0.91483  39.10334  1.000 21.55536 ?  42  ASP   B N    1 
ATOM   2930 C  CA   . ASP   B 1 39  ? 48.06025 0.28205   39.49015  1.000 20.87625 ?  42  ASP   B CA   1 
ATOM   2931 C  C    . ASP   B 1 39  ? 47.16895 0.79401   38.36293  1.000 19.92739 ?  42  ASP   B C    1 
ATOM   2932 O  O    . ASP   B 1 39  ? 46.74777 1.95492   38.38423  1.000 21.75560 ?  42  ASP   B O    1 
ATOM   2933 C  CB   . ASP   B 1 39  ? 48.97651 1.40813   39.97832  1.000 21.58113 ?  42  ASP   B CB   1 
ATOM   2934 C  CG   . ASP   B 1 39  ? 50.12637 1.70039   39.03573  1.000 22.53382 ?  42  ASP   B CG   1 
ATOM   2935 O  OD1  . ASP   B 1 39  ? 50.23084 1.01136   37.99415  1.000 23.35759 ?  42  ASP   B OD1  1 
ATOM   2936 O  OD2  . ASP   B 1 39  ? 50.95095 2.60431   39.35995  1.000 25.02946 ?  42  ASP   B OD2  1 
ATOM   2937 H  H    . ASP   B 1 39  ? 49.46430 -0.76016  38.57992  1.000 25.86644 ?  42  ASP   B H    1 
ATOM   2938 H  HA   . ASP   B 1 39  ? 47.50548 0.03488   40.24648  1.000 25.05149 ?  42  ASP   B HA   1 
ATOM   2939 H  HB2  . ASP   B 1 39  ? 48.45383 2.22009   40.07009  1.000 25.89735 ?  42  ASP   B HB2  1 
ATOM   2940 H  HB3  . ASP   B 1 39  ? 49.35236 1.15674   40.83648  1.000 25.89735 ?  42  ASP   B HB3  1 
ATOM   2941 N  N    . ALA   B 1 40  ? 46.87320 -0.03350  37.36565  1.000 18.60894 ?  43  ALA   B N    1 
ATOM   2942 C  CA   . ALA   B 1 40  ? 46.08516 0.45418   36.24212  1.000 18.19493 ?  43  ALA   B CA   1 
ATOM   2943 C  C    . ALA   B 1 40  ? 44.64512 0.73452   36.64939  1.000 18.23664 ?  43  ALA   B C    1 
ATOM   2944 O  O    . ALA   B 1 40  ? 44.01596 -0.04518  37.36346  1.000 19.71167 ?  43  ALA   B O    1 
ATOM   2945 C  CB   . ALA   B 1 40  ? 46.08324 -0.58496  35.12780  1.000 19.21652 ?  43  ALA   B CB   1 
ATOM   2946 H  H    . ALA   B 1 40  ? 47.11049 -0.85871  37.31756  1.000 22.33073 ?  43  ALA   B H    1 
ATOM   2947 H  HA   . ALA   B 1 40  ? 46.47875 1.28125   35.92284  1.000 21.83392 ?  43  ALA   B HA   1 
ATOM   2948 H  HB1  . ALA   B 1 40  ? 45.63352 -0.21520  34.35196  1.000 23.05983 ?  43  ALA   B HB1  1 
ATOM   2949 H  HB2  . ALA   B 1 40  ? 46.99993 -0.80891  34.90326  1.000 23.05983 ?  43  ALA   B HB2  1 
ATOM   2950 H  HB3  . ALA   B 1 40  ? 45.61508 -1.37689  35.43531  1.000 23.05983 ?  43  ALA   B HB3  1 
ATOM   2951 N  N    . ASP   B 1 41  ? 44.10544 1.83216   36.13510  1.000 18.55167 ?  44  ASP   B N    1 
ATOM   2952 C  CA   . ASP   B 1 41  ? 42.69218 2.14853   36.22692  1.000 20.94843 ?  44  ASP   B CA   1 
ATOM   2953 C  C    . ASP   B 1 41  ? 41.94506 1.77748   34.95230  1.000 18.09239 ?  44  ASP   B C    1 
ATOM   2954 O  O    . ASP   B 1 41  ? 40.80257 1.29302   35.01733  1.000 17.75047 ?  44  ASP   B O    1 
ATOM   2955 C  CB   . ASP   B 1 41  ? 42.52985 3.65333   36.50311  1.000 25.12615 ?  44  ASP   B CB   1 
ATOM   2956 C  CG   . ASP   B 1 41  ? 43.35536 4.55617   35.51741  1.000 29.57441 ?  44  ASP   B CG   1 
ATOM   2957 O  OD1  . ASP   B 1 41  ? 44.23591 4.06266   34.74287  1.000 26.20822 ?  44  ASP   B OD1  1 
ATOM   2958 O  OD2  . ASP   B 1 41  ? 43.10358 5.78578   35.51341  1.000 35.79506 ?  44  ASP   B OD2  1 
ATOM   2959 H  H    . ASP   B 1 41  ? 44.55681 2.43004   35.71272  1.000 22.26201 ?  44  ASP   B H    1 
ATOM   2960 H  HA   . ASP   B 1 41  ? 42.28694 1.66366   36.96284  1.000 25.13811 ?  44  ASP   B HA   1 
ATOM   2961 H  HB2  . ASP   B 1 41  ? 41.59378 3.89059   36.41151  1.000 30.15138 ?  44  ASP   B HB2  1 
ATOM   2962 H  HB3  . ASP   B 1 41  ? 42.83319 3.84195   37.40495  1.000 30.15138 ?  44  ASP   B HB3  1 
ATOM   2963 N  N    . ARG   B 1 42  ? 42.57508 1.97430   33.79014  1.000 16.98179 ?  45  ARG   B N    1 
ATOM   2964 C  CA   . ARG   B 1 42  ? 41.96799 1.69899   32.49205  1.000 16.08052 ?  45  ARG   B CA   1 
ATOM   2965 C  C    . ARG   B 1 42  ? 43.06140 1.78909   31.44352  1.000 14.32115 ?  45  ARG   B C    1 
ATOM   2966 O  O    . ARG   B 1 42  ? 44.09342 2.42861   31.65351  1.000 16.36662 ?  45  ARG   B O    1 
ATOM   2967 C  CB   . ARG   B 1 42  ? 40.84540 2.69206   32.16170  1.000 15.93758 ?  45  ARG   B CB   1 
ATOM   2968 C  CG   . ARG   B 1 42  ? 41.22387 4.14800   32.29758  1.000 18.05480 ?  45  ARG   B CG   1 
ATOM   2969 C  CD   . ARG   B 1 42  ? 40.09610 5.04639   31.80441  1.000 17.78327 ?  45  ARG   B CD   1 
ATOM   2970 N  NE   . ARG   B 1 42  ? 40.02397 5.09416   30.34196  1.000 16.92832 ?  45  ARG   B NE   1 
ATOM   2971 C  CZ   . ARG   B 1 42  ? 39.00240 5.59683   29.66046  1.000 17.04038 ?  45  ARG   B CZ   1 
ATOM   2972 N  NH1  . ARG   B 1 42  ? 37.86000 5.88158   30.25396  1.000 18.49380 ?  45  ARG   B NH1  1 
ATOM   2973 N  NH2  . ARG   B 1 42  ? 39.12927 5.80321   28.34809  1.000 17.52497 ?  45  ARG   B NH2  1 
ATOM   2974 H  H    . ARG   B 1 42  ? 43.37826 2.27552   33.72877  1.000 20.37814 ?  45  ARG   B H    1 
ATOM   2975 H  HA   . ARG   B 1 42  ? 41.59337 0.80425   32.49341  1.000 19.29662 ?  45  ARG   B HA   1 
ATOM   2976 H  HB2  . ARG   B 1 42  ? 40.56776 2.54777   31.24355  1.000 19.12509 ?  45  ARG   B HB2  1 
ATOM   2977 H  HB3  . ARG   B 1 42  ? 40.10227 2.52697   32.76286  1.000 19.12509 ?  45  ARG   B HB3  1 
ATOM   2978 H  HG2  . ARG   B 1 42  ? 41.39560 4.35277   33.23004  1.000 21.66576 ?  45  ARG   B HG2  1 
ATOM   2979 H  HG3  . ARG   B 1 42  ? 42.01572 4.32811   31.76708  1.000 21.66576 ?  45  ARG   B HG3  1 
ATOM   2980 H  HD2  . ARG   B 1 42  ? 39.25048 4.70742   32.13745  1.000 21.33993 ?  45  ARG   B HD2  1 
ATOM   2981 H  HD3  . ARG   B 1 42  ? 40.24287 5.94859   32.12904  1.000 21.33993 ?  45  ARG   B HD3  1 
ATOM   2982 H  HE   . ARG   B 1 42  ? 40.68686 4.77570   29.89615  1.000 20.31398 ?  45  ARG   B HE   1 
ATOM   2983 H  HH11 . ARG   B 1 42  ? 37.76715 5.74201   31.09747  1.000 22.19256 ?  45  ARG   B HH11 1 
ATOM   2984 H  HH12 . ARG   B 1 42  ? 37.20770 6.20688   29.79758  1.000 22.19256 ?  45  ARG   B HH12 1 
ATOM   2985 H  HH21 . ARG   B 1 42  ? 39.86796 5.61078   27.95197  1.000 21.02996 ?  45  ARG   B HH21 1 
ATOM   2986 H  HH22 . ARG   B 1 42  ? 38.47233 6.12864   27.89850  1.000 21.02996 ?  45  ARG   B HH22 1 
ATOM   2987 N  N    . PHE   B 1 43  ? 42.79887 1.17689   30.28571  1.000 14.47286 ?  46  PHE   B N    1 
ATOM   2988 C  CA   . PHE   B 1 43  ? 43.53269 1.47021   29.05531  1.000 13.97248 ?  46  PHE   B CA   1 
ATOM   2989 C  C    . PHE   B 1 43  ? 42.54150 1.33962   27.90612  1.000 13.94884 ?  46  PHE   B C    1 
ATOM   2990 O  O    . PHE   B 1 43  ? 41.40829 0.87934   28.09378  1.000 13.47580 ?  46  PHE   B O    1 
ATOM   2991 C  CB   . PHE   B 1 43  ? 44.77041 0.57537   28.87992  1.000 14.19180 ?  46  PHE   B CB   1 
ATOM   2992 C  CG   . PHE   B 1 43  ? 44.48334 -0.85737  28.49497  1.000 14.24768 ?  46  PHE   B CG   1 
ATOM   2993 C  CD1  . PHE   B 1 43  ? 44.43628 -1.24367  27.15194  1.000 15.65808 ?  46  PHE   B CD1  1 
ATOM   2994 C  CD2  . PHE   B 1 43  ? 44.32837 -1.83817  29.45298  1.000 15.64493 ?  46  PHE   B CD2  1 
ATOM   2995 C  CE1  . PHE   B 1 43  ? 44.20318 -2.56840  26.81096  1.000 16.51285 ?  46  PHE   B CE1  1 
ATOM   2996 C  CE2  . PHE   B 1 43  ? 44.08648 -3.14922  29.08746  1.000 16.92812 ?  46  PHE   B CE2  1 
ATOM   2997 C  CZ   . PHE   B 1 43  ? 44.03846 -3.50769  27.78091  1.000 16.80510 ?  46  PHE   B CZ   1 
ATOM   2998 H  H    . PHE   B 1 43  ? 42.18980 0.57785   30.18677  1.000 17.36743 ?  46  PHE   B H    1 
ATOM   2999 H  HA   . PHE   B 1 43  ? 43.87018 2.37946   29.07185  1.000 16.76698 ?  46  PHE   B HA   1 
ATOM   3000 H  HB2  . PHE   B 1 43  ? 45.32676 0.95633   28.18260  1.000 17.03016 ?  46  PHE   B HB2  1 
ATOM   3001 H  HB3  . PHE   B 1 43  ? 45.25623 0.55758   29.71930  1.000 17.03016 ?  46  PHE   B HB3  1 
ATOM   3002 H  HD1  . PHE   B 1 43  ? 44.56189 -0.60931  26.48358  1.000 18.78969 ?  46  PHE   B HD1  1 
ATOM   3003 H  HD2  . PHE   B 1 43  ? 44.38725 -1.61495  30.35387  1.000 18.77391 ?  46  PHE   B HD2  1 
ATOM   3004 H  HE1  . PHE   B 1 43  ? 44.15938 -2.81512  25.91536  1.000 19.81542 ?  46  PHE   B HE1  1 
ATOM   3005 H  HE2  . PHE   B 1 43  ? 43.95513 -3.79296  29.74567  1.000 20.31374 ?  46  PHE   B HE2  1 
ATOM   3006 H  HZ   . PHE   B 1 43  ? 43.89285 -4.39613  27.54770  1.000 20.16612 ?  46  PHE   B HZ   1 
ATOM   3007 N  N    . GLN   B 1 44  ? 42.96783 1.74453   26.71143  1.000 13.45765 ?  47  GLN   B N    1 
ATOM   3008 C  CA   . GLN   B 1 44  ? 42.08359 1.61525   25.56737  1.000 13.52342 ?  47  GLN   B CA   1 
ATOM   3009 C  C    . GLN   B 1 44  ? 42.88267 1.29011   24.32447  1.000 12.38894 ?  47  GLN   B C    1 
ATOM   3010 O  O    . GLN   B 1 44  ? 44.03473 1.70125   24.17257  1.000 13.73250 ?  47  GLN   B O    1 
ATOM   3011 C  CB   . GLN   B 1 44  ? 41.25671 2.88608   25.35060  1.000 14.08434 ?  47  GLN   B CB   1 
ATOM   3012 C  CG   . GLN   B 1 44  ? 42.05122 4.09754   24.91732  1.000 15.04362 ?  47  GLN   B CG   1 
ATOM   3013 C  CD   . GLN   B 1 44  ? 41.42575 5.40376   25.36909  1.000 15.87650 ?  47  GLN   B CD   1 
ATOM   3014 O  OE1  . GLN   B 1 44  ? 41.32965 5.65900   26.57356  1.000 18.12310 ?  47  GLN   B OE1  1 
ATOM   3015 N  NE2  . GLN   B 1 44  ? 40.98383 6.22406   24.42162  1.000 16.04939 ?  47  GLN   B NE2  1 
ATOM   3016 H  H    . GLN   B 1 44  ? 43.74022 2.08556   26.54797  1.000 16.14918 ?  47  GLN   B H    1 
ATOM   3017 H  HA   . GLN   B 1 44  ? 41.47749 0.87415   25.72331  1.000 16.22810 ?  47  GLN   B HA   1 
ATOM   3018 H  HB2  . GLN   B 1 44  ? 40.59665 2.70939   24.66212  1.000 16.90121 ?  47  GLN   B HB2  1 
ATOM   3019 H  HB3  . GLN   B 1 44  ? 40.81458 3.11084   26.18421  1.000 16.90121 ?  47  GLN   B HB3  1 
ATOM   3020 H  HG2  . GLN   B 1 44  ? 42.94165 4.04409   25.29835  1.000 18.05234 ?  47  GLN   B HG2  1 
ATOM   3021 H  HG3  . GLN   B 1 44  ? 42.10498 4.11018   23.94889  1.000 18.05234 ?  47  GLN   B HG3  1 
ATOM   3022 H  HE21 . GLN   B 1 44  ? 41.05891 6.00458   23.59349  1.000 19.25926 ?  47  GLN   B HE21 1 
ATOM   3023 H  HE22 . GLN   B 1 44  ? 40.62276 6.97440   24.63657  1.000 19.25926 ?  47  GLN   B HE22 1 
ATOM   3024 N  N    . VAL   B 1 45  ? 42.22123 0.54164   23.44585  1.000 12.40893 ?  48  VAL   B N    1 
ATOM   3025 C  CA   . VAL   B 1 45  ? 42.65296 0.28393   22.07924  1.000 12.25699 ?  48  VAL   B CA   1 
ATOM   3026 C  C    . VAL   B 1 45  ? 41.64539 0.98823   21.18133  1.000 12.63023 ?  48  VAL   B C    1 
ATOM   3027 O  O    . VAL   B 1 45  ? 40.45492 0.65961   21.21989  1.000 12.84652 ?  48  VAL   B O    1 
ATOM   3028 C  CB   . VAL   B 1 45  ? 42.70158 -1.22436  21.78813  1.000 13.35923 ?  48  VAL   B CB   1 
ATOM   3029 C  CG1  . VAL   B 1 45  ? 43.07366 -1.46928  20.33245  1.000 14.34588 ?  48  VAL   B CG1  1 
ATOM   3030 C  CG2  . VAL   B 1 45  ? 43.68909 -1.92467  22.71341  1.000 13.71433 ?  48  VAL   B CG2  1 
ATOM   3031 H  H    . VAL   B 1 45  ? 41.47760 0.15130   23.63092  1.000 14.89072 ?  48  VAL   B H    1 
ATOM   3032 H  HA   . VAL   B 1 45  ? 43.53780 0.64777   21.91930  1.000 14.70839 ?  48  VAL   B HA   1 
ATOM   3033 H  HB   . VAL   B 1 45  ? 41.82203 -1.60002  21.94988  1.000 16.03107 ?  48  VAL   B HB   1 
ATOM   3034 H  HG11 . VAL   B 1 45  ? 43.13432 -2.42507  20.17851  1.000 17.21506 ?  48  VAL   B HG11 1 
ATOM   3035 H  HG12 . VAL   B 1 45  ? 42.38905 -1.08526  19.76259  1.000 17.21506 ?  48  VAL   B HG12 1 
ATOM   3036 H  HG13 . VAL   B 1 45  ? 43.92916 -1.04996  20.15030  1.000 17.21506 ?  48  VAL   B HG13 1 
ATOM   3037 H  HG21 . VAL   B 1 45  ? 43.63684 -2.88180  22.56482  1.000 16.45720 ?  48  VAL   B HG21 1 
ATOM   3038 H  HG22 . VAL   B 1 45  ? 44.58471 -1.60790  22.51737  1.000 16.45720 ?  48  VAL   B HG22 1 
ATOM   3039 H  HG23 . VAL   B 1 45  ? 43.45973 -1.71974  23.63336  1.000 16.45720 ?  48  VAL   B HG23 1 
ATOM   3040 N  N    . ASP   B 1 46  ? 42.11355 1.95654   20.39698  1.000 12.20477 ?  49  ASP   B N    1 
ATOM   3041 C  CA   . ASP   B 1 46  ? 41.26232 2.77447   19.54414  1.000 12.75240 ?  49  ASP   B CA   1 
ATOM   3042 C  C    . ASP   B 1 46  ? 41.62214 2.54780   18.08102  1.000 12.12662 ?  49  ASP   B C    1 
ATOM   3043 O  O    . ASP   B 1 46  ? 42.77761 2.71936   17.67832  1.000 12.97441 ?  49  ASP   B O    1 
ATOM   3044 C  CB   . ASP   B 1 46  ? 41.43245 4.26579   19.86291  1.000 13.24015 ?  49  ASP   B CB   1 
ATOM   3045 C  CG   . ASP   B 1 46  ? 40.84281 4.67471   21.20471  1.000 14.24034 ?  49  ASP   B CG   1 
ATOM   3046 O  OD1  . ASP   B 1 46  ? 40.06350 3.89797   21.79141  1.000 14.70656 ?  49  ASP   B OD1  1 
ATOM   3047 O  OD2  . ASP   B 1 46  ? 41.17314 5.78234   21.66972  1.000 16.05696 ?  49  ASP   B OD2  1 
ATOM   3048 H  H    . ASP   B 1 46  ? 42.94666 2.16270   20.34192  1.000 14.64573 ?  49  ASP   B H    1 
ATOM   3049 H  HA   . ASP   B 1 46  ? 40.34235 2.50389   19.69025  1.000 15.30288 ?  49  ASP   B HA   1 
ATOM   3050 H  HB2  . ASP   B 1 46  ? 42.37927 4.47594   19.87919  1.000 15.88819 ?  49  ASP   B HB2  1 
ATOM   3051 H  HB3  . ASP   B 1 46  ? 40.98912 4.78525   19.17405  1.000 15.88819 ?  49  ASP   B HB3  1 
ATOM   3052 N  N    . LEU   B 1 47  ? 40.62513 2.17636   17.28403  1.000 11.61144 ?  50  LEU   B N    1 
ATOM   3053 C  CA   . LEU   B 1 47  ? 40.76014 2.05793   15.82908  1.000 11.05892 ?  50  LEU   B CA   1 
ATOM   3054 C  C    . LEU   B 1 47  ? 40.21038 3.34663   15.24100  1.000 11.53276 ?  50  LEU   B C    1 
ATOM   3055 O  O    . LEU   B 1 47  ? 39.00582 3.61509   15.33922  1.000 12.51336 ?  50  LEU   B O    1 
ATOM   3056 C  CB   . LEU   B 1 47  ? 40.02348 0.83306   15.30558  1.000 11.65089 ?  50  LEU   B CB   1 
ATOM   3057 C  CG   . LEU   B 1 47  ? 40.44269 -0.47697  15.96115  1.000 12.96136 ?  50  LEU   B CG   1 
ATOM   3058 C  CD1  . LEU   B 1 47  ? 39.75310 -1.64703  15.24566  1.000 13.06012 ?  50  LEU   B CD1  1 
ATOM   3059 C  CD2  . LEU   B 1 47  ? 41.93716 -0.70766  16.02823  1.000 14.47576 ?  50  LEU   B CD2  1 
ATOM   3060 H  H    . LEU   B 1 47  ? 39.83703 1.98139   17.56774  1.000 13.93373 ?  50  LEU   B H    1 
ATOM   3061 H  HA   . LEU   B 1 47  ? 41.69085 1.95676   15.57524  1.000 13.27071 ?  50  LEU   B HA   1 
ATOM   3062 H  HB2  . LEU   B 1 47  ? 39.07403 0.95170   15.46487  1.000 13.98107 ?  50  LEU   B HB2  1 
ATOM   3063 H  HB3  . LEU   B 1 47  ? 40.19283 0.75371   14.35378  1.000 13.98107 ?  50  LEU   B HB3  1 
ATOM   3064 H  HG   . LEU   B 1 47  ? 40.16110 -0.42709  16.88804  1.000 15.55363 ?  50  LEU   B HG   1 
ATOM   3065 H  HD11 . LEU   B 1 47  ? 39.93382 -2.46595  15.73312  1.000 15.67214 ?  50  LEU   B HD11 1 
ATOM   3066 H  HD12 . LEU   B 1 47  ? 38.79762 -1.48194  15.21903  1.000 15.67214 ?  50  LEU   B HD12 1 
ATOM   3067 H  HD13 . LEU   B 1 47  ? 40.10226 -1.71532  14.34326  1.000 15.67214 ?  50  LEU   B HD13 1 
ATOM   3068 H  HD21 . LEU   B 1 47  ? 42.10423 -1.59287  16.38796  1.000 17.37091 ?  50  LEU   B HD21 1 
ATOM   3069 H  HD22 . LEU   B 1 47  ? 42.30781 -0.63843  15.13451  1.000 17.37091 ?  50  LEU   B HD22 1 
ATOM   3070 H  HD23 . LEU   B 1 47  ? 42.33483 -0.03608  16.60419  1.000 17.37091 ?  50  LEU   B HD23 1 
ATOM   3071 N  N    . GLN   B 1 48  ? 41.11779 4.18219   14.73212  1.000 11.45627 ?  51  GLN   B N    1 
ATOM   3072 C  CA   . GLN   B 1 48  ? 40.82814 5.57528   14.43033  1.000 12.21059 ?  51  GLN   B CA   1 
ATOM   3073 C  C    . GLN   B 1 48  ? 40.86219 5.85951   12.93385  1.000 12.29661 ?  51  GLN   B C    1 
ATOM   3074 O  O    . GLN   B 1 48  ? 41.59732 5.22261   12.17568  1.000 12.68423 ?  51  GLN   B O    1 
ATOM   3075 C  CB   . GLN   B 1 48  ? 41.87576 6.50947   15.05436  1.000 12.87322 ?  51  GLN   B CB   1 
ATOM   3076 C  CG   . GLN   B 1 48  ? 42.05727 6.29686   16.54674  1.000 13.64126 ?  51  GLN   B CG   1 
ATOM   3077 C  CD   . GLN   B 1 48  ? 43.15633 7.10536   17.21217  1.000 15.16185 ?  51  GLN   B CD   1 
ATOM   3078 O  OE1  . GLN   B 1 48  ? 43.41539 6.89542   18.40308  1.000 16.98884 ?  51  GLN   B OE1  1 
ATOM   3079 N  NE2  . GLN   B 1 48  ? 43.75684 8.04690   16.51175  1.000 16.30223 ?  51  GLN   B NE2  1 
ATOM   3080 H  H    . GLN   B 1 48  ? 41.92699 3.95466   14.55036  1.000 13.74753 ?  51  GLN   B H    1 
ATOM   3081 H  HA   . GLN   B 1 48  ? 39.93993 5.75436   14.77662  1.000 14.65271 ?  51  GLN   B HA   1 
ATOM   3082 H  HB2  . GLN   B 1 48  ? 42.73118 6.35270   14.62474  1.000 15.44786 ?  51  GLN   B HB2  1 
ATOM   3083 H  HB3  . GLN   B 1 48  ? 41.59841 7.42859   14.91579  1.000 15.44786 ?  51  GLN   B HB3  1 
ATOM   3084 H  HG2  . GLN   B 1 48  ? 41.22558 6.52903   16.98865  1.000 16.36951 ?  51  GLN   B HG2  1 
ATOM   3085 H  HG3  . GLN   B 1 48  ? 42.26222 5.36060   16.69611  1.000 16.36951 ?  51  GLN   B HG3  1 
ATOM   3086 H  HE21 . GLN   B 1 48  ? 43.52338 8.19157   15.69678  1.000 19.56267 ?  51  GLN   B HE21 1 
ATOM   3087 H  HE22 . GLN   B 1 48  ? 44.38208 8.51648   16.86976  1.000 19.56267 ?  51  GLN   B HE22 1 
ATOM   3088 N  N    . ASN   B 1 49  ? 40.09832 6.87332   12.53729  1.000 12.84710 ?  52  ASN   B N    1 
ATOM   3089 C  CA   . ASN   B 1 49  ? 40.15818 7.46422   11.20128  1.000 13.54610 ?  52  ASN   B CA   1 
ATOM   3090 C  C    . ASN   B 1 49  ? 41.01819 8.71462   11.33978  1.000 14.79296 ?  52  ASN   B C    1 
ATOM   3091 O  O    . ASN   B 1 49  ? 40.53477 9.80279   11.65167  1.000 16.50769 ?  52  ASN   B O    1 
ATOM   3092 C  CB   . ASN   B 1 49  ? 38.76990 7.77785   10.68748  1.000 15.39702 ?  52  ASN   B CB   1 
ATOM   3093 C  CG   . ASN   B 1 49  ? 38.80395 8.44953   9.33767   1.000 15.89467 ?  52  ASN   B CG   1 
ATOM   3094 O  OD1  . ASN   B 1 49  ? 39.87428 8.59097   8.72564   1.000 15.82285 ?  52  ASN   B OD1  1 
ATOM   3095 N  ND2  . ASN   B 1 49  ? 37.64348 8.89615   8.86249   1.000 15.78195 ?  52  ASN   B ND2  1 
ATOM   3096 H  H    . ASN   B 1 49  ? 39.51458 7.25140   13.04316  1.000 15.41652 ?  52  ASN   B H    1 
ATOM   3097 H  HA   . ASN   B 1 49  ? 40.57098 6.85260   10.57166  1.000 16.25532 ?  52  ASN   B HA   1 
ATOM   3098 H  HB2  . ASN   B 1 49  ? 38.26743 6.95250   10.60251  1.000 18.47643 ?  52  ASN   B HB2  1 
ATOM   3099 H  HB3  . ASN   B 1 49  ? 38.32620 8.37367   11.31119  1.000 18.47643 ?  52  ASN   B HB3  1 
ATOM   3100 H  HD21 . ASN   B 1 49  ? 36.92329 8.79478   9.32146   1.000 18.93834 ?  52  ASN   B HD21 1 
ATOM   3101 H  HD22 . ASN   B 1 49  ? 37.61393 9.28606   8.09653   1.000 18.93834 ?  52  ASN   B HD22 1 
ATOM   3102 N  N    . GLY   B 1 50  ? 42.31491 8.54006   11.14230  1.000 14.92510 ?  53  GLY   B N    1 
ATOM   3103 C  CA   . GLY   B 1 50  ? 43.26972 9.61088   11.33423  1.000 17.22609 ?  53  GLY   B CA   1 
ATOM   3104 C  C    . GLY   B 1 50  ? 43.88294 9.62743   12.72892  1.000 15.12009 ?  53  GLY   B C    1 
ATOM   3105 O  O    . GLY   B 1 50  ? 43.50835 8.87751   13.63151  1.000 14.77507 ?  53  GLY   B O    1 
ATOM   3106 H  H    . GLY   B 1 50  ? 42.66981 7.79749   10.89282  1.000 17.91012 ?  53  GLY   B H    1 
ATOM   3107 H  HA2  . GLY   B 1 50  ? 43.98813 9.51510   10.68955  1.000 20.67130 ?  53  GLY   B HA2  1 
ATOM   3108 H  HA3  . GLY   B 1 50  ? 42.82646 10.46138  11.18908  1.000 20.67130 ?  53  GLY   B HA3  1 
ATOM   3109 N  N    . SER   B 1 51  ? 44.85916 10.51553  12.89274  1.000 15.97245 ?  54  SER   B N    1 
ATOM   3110 C  CA   . SER   B 1 51  ? 45.62082 10.63937  14.12825  1.000 16.37895 ?  54  SER   B CA   1 
ATOM   3111 C  C    . SER   B 1 51  ? 45.53951 12.02095  14.75158  1.000 16.72540 ?  54  SER   B C    1 
ATOM   3112 O  O    . SER   B 1 51  ? 46.19992 12.26885  15.76133  1.000 19.01962 ?  54  SER   B O    1 
ATOM   3113 C  CB   . SER   B 1 51  ? 47.09370 10.30714  13.85972  1.000 19.21411 ?  54  SER   B CB   1 
ATOM   3114 O  OG   . SER   B 1 51  ? 47.61392 11.22456  12.92287  1.000 20.89399 ?  54  SER   B OG   1 
ATOM   3115 H  H    . SER   B 1 51  ? 45.10483 11.07236  12.28513  1.000 19.16694 ?  54  SER   B H    1 
ATOM   3116 H  HA   . SER   B 1 51  ? 45.26831 10.00446  14.77131  1.000 19.65474 ?  54  SER   B HA   1 
ATOM   3117 H  HB2  . SER   B 1 51  ? 47.59490 10.37302  14.68759  1.000 23.05693 ?  54  SER   B HB2  1 
ATOM   3118 H  HB3  . SER   B 1 51  ? 47.16105 9.40812   13.50178  1.000 23.05693 ?  54  SER   B HB3  1 
ATOM   3119 H  HG   . SER   B 1 51  ? 48.28487 10.89478  12.53990  1.000 25.07278 ?  54  SER   B HG   1 
ATOM   3120 N  N    . SER   B 1 52  ? 44.76820 12.92815  14.18513  1.000 16.58271 ?  55  SER   B N    1 
ATOM   3121 C  CA   . SER   B 1 52  ? 44.75316 14.26858  14.72558  1.000 16.98149 ?  55  SER   B CA   1 
ATOM   3122 C  C    . SER   B 1 52  ? 44.20036 14.26400  16.14170  1.000 16.66988 ?  55  SER   B C    1 
ATOM   3123 O  O    . SER   B 1 52  ? 43.28445 13.50738  16.48187  1.000 17.01619 ?  55  SER   B O    1 
ATOM   3124 C  CB   . SER   B 1 52  ? 43.88873 15.18433  13.88487  1.000 19.83824 ?  55  SER   B CB   1 
ATOM   3125 O  OG   . SER   B 1 52  ? 43.95941 16.48792  14.43907  1.000 20.40101 ?  55  SER   B OG   1 
ATOM   3126 H  H    . SER   B 1 52  ? 44.25817 12.79612  13.50539  1.000 19.89925 ?  55  SER   B H    1 
ATOM   3127 H  HA   . SER   B 1 52  ? 45.66209 14.60733  14.72731  1.000 20.37778 ?  55  SER   B HA   1 
ATOM   3128 H  HB2  . SER   B 1 52  ? 44.21878 15.19875  12.97286  1.000 23.80589 ?  55  SER   B HB2  1 
ATOM   3129 H  HB3  . SER   B 1 52  ? 42.97051 14.87205  13.90049  1.000 23.80589 ?  55  SER   B HB3  1 
ATOM   3130 H  HG   . SER   B 1 52  ? 43.21195 16.86650  14.37914  1.000 24.48122 ?  55  SER   B HG   1 
ATOM   3131 N  N    . MET   B 1 53  ? 44.72577 15.17153  16.95365  1.000 18.34597 ?  56  MET   B N    1 
ATOM   3132 C  CA   . MET   B 1 53  ? 44.18209 15.40763  18.28133  1.000 20.76353 ?  56  MET   B CA   1 
ATOM   3133 C  C    . MET   B 1 53  ? 43.25008 16.60756  18.30845  1.000 19.07842 ?  56  MET   B C    1 
ATOM   3134 O  O    . MET   B 1 53  ? 42.55226 16.79907  19.31183  1.000 20.95242 ?  56  MET   B O    1 
ATOM   3135 C  CB   . MET   B 1 53  ? 45.31128 15.57793  19.30927  1.000 26.67253 ?  56  MET   B CB   1 
ATOM   3136 C  CG   . MET   B 1 53  ? 46.10557 14.28820  19.50682  1.000 34.32665 ?  56  MET   B CG   1 
ATOM   3137 S  SD   . MET   B 1 53  ? 47.60762 14.46328  20.47097  1.000 42.53823 ?  56  MET   B SD   1 
ATOM   3138 C  CE   . MET   B 1 53  ? 48.76337 13.51240  19.47877  1.000 44.70273 ?  56  MET   B CE   1 
ATOM   3139 H  H    . MET   B 1 53  ? 45.40144 15.66566  16.75641  1.000 22.01516 ?  56  MET   B H    1 
ATOM   3140 H  HA   . MET   B 1 53  ? 43.68353 14.62541  18.56500  1.000 24.91623 ?  56  MET   B HA   1 
ATOM   3141 N  N    . LYS   B 1 54  ? 43.19505 17.38808  17.22082  1.000 19.58058 ?  57  LYS   B N    1 
ATOM   3142 C  CA   . LYS   B 1 54  ? 42.36949 18.58238  17.19368  1.000 18.66752 ?  57  LYS   B CA   1 
ATOM   3143 C  C    . LYS   B 1 54  ? 42.09659 18.99582  15.75152  1.000 18.34898 ?  57  LYS   B C    1 
ATOM   3144 O  O    . LYS   B 1 54  ? 43.01855 19.42324  15.04542  1.000 18.67107 ?  57  LYS   B O    1 
ATOM   3145 C  CB   . LYS   B 1 54  ? 43.06486 19.73593  17.91695  1.000 21.28855 ?  57  LYS   B CB   1 
ATOM   3146 C  CG   . LYS   B 1 54  ? 42.27764 21.00936  17.83304  1.000 25.23706 ?  57  LYS   B CG   1 
ATOM   3147 C  CD   . LYS   B 1 54  ? 41.05872 20.99719  18.71588  1.000 30.64818 ?  57  LYS   B CD   1 
ATOM   3148 C  CE   . LYS   B 1 54  ? 40.42938 22.38071  18.77479  1.000 34.46862 ?  57  LYS   B CE   1 
ATOM   3149 N  NZ   . LYS   B 1 54  ? 39.20310 22.39997  19.62997  1.000 36.26123 ?  57  LYS   B NZ   1 
ATOM   3150 H  H    . LYS   B 1 54  ? 43.62838 17.24031  16.49282  1.000 23.49670 ?  57  LYS   B H    1 
ATOM   3151 H  HA   . LYS   B 1 54  ? 41.52843 18.38891  17.63649  1.000 22.40103 ?  57  LYS   B HA   1 
ATOM   3152 H  HB2  . LYS   B 1 54  ? 43.17157 19.50640  18.85334  1.000 25.54626 ?  57  LYS   B HB2  1 
ATOM   3153 H  HB3  . LYS   B 1 54  ? 43.93286 19.88864  17.51180  1.000 25.54626 ?  57  LYS   B HB3  1 
ATOM   3154 H  HG2  . LYS   B 1 54  ? 42.84099 21.74891  18.10981  1.000 30.28447 ?  57  LYS   B HG2  1 
ATOM   3155 H  HG3  . LYS   B 1 54  ? 41.98383 21.14048  16.91796  1.000 30.28447 ?  57  LYS   B HG3  1 
ATOM   3156 H  HD2  . LYS   B 1 54  ? 40.40522 20.37539  18.35920  1.000 36.77782 ?  57  LYS   B HD2  1 
ATOM   3157 H  HD3  . LYS   B 1 54  ? 41.31101 20.73396  19.61475  1.000 36.77782 ?  57  LYS   B HD3  1 
ATOM   3158 H  HE2  . LYS   B 1 54  ? 41.06915 23.00716  19.14782  1.000 41.36234 ?  57  LYS   B HE2  1 
ATOM   3159 H  HE3  . LYS   B 1 54  ? 40.17887 22.65620  17.87911  1.000 41.36234 ?  57  LYS   B HE3  1 
ATOM   3160 H  HZ1  . LYS   B 1 54  ? 38.85249 23.21793  19.64100  1.000 43.51347 ?  57  LYS   B HZ1  1 
ATOM   3161 H  HZ2  . LYS   B 1 54  ? 38.59886 21.83104  19.30854  1.000 43.51347 ?  57  LYS   B HZ2  1 
ATOM   3162 H  HZ3  . LYS   B 1 54  ? 39.40895 22.16271  20.46270  1.000 43.51347 ?  57  LYS   B HZ3  1 
ATOM   3163 N  N    . PRO   B 1 55  ? 40.85522 18.92259  15.28343  1.000 18.47465 ?  58  PRO   B N    1 
ATOM   3164 C  CA   . PRO   B 1 55  ? 39.72600 18.20651  15.87761  1.000 18.02547 ?  58  PRO   B CA   1 
ATOM   3165 C  C    . PRO   B 1 55  ? 40.10456 16.73965  16.10953  1.000 17.60853 ?  58  PRO   B C    1 
ATOM   3166 O  O    . PRO   B 1 55  ? 40.81410 16.13149  15.29624  1.000 17.87472 ?  58  PRO   B O    1 
ATOM   3167 C  CB   . PRO   B 1 55  ? 38.62542 18.36378  14.80920  1.000 20.18014 ?  58  PRO   B CB   1 
ATOM   3168 C  CG   . PRO   B 1 55  ? 39.01217 19.59651  14.04274  1.000 21.07750 ?  58  PRO   B CG   1 
ATOM   3169 C  CD   . PRO   B 1 55  ? 40.49590 19.50600  13.97935  1.000 19.55758 ?  58  PRO   B CD   1 
ATOM   3170 H  HA   . PRO   B 1 55  ? 39.42142 18.61925  16.70088  1.000 21.63057 ?  58  PRO   B HA   1 
ATOM   3171 H  HB2  . PRO   B 1 55  ? 38.61070 17.58465  14.23158  1.000 24.21617 ?  58  PRO   B HB2  1 
ATOM   3172 H  HB3  . PRO   B 1 55  ? 37.76209 18.47600  15.23696  1.000 24.21617 ?  58  PRO   B HB3  1 
ATOM   3173 H  HG2  . PRO   B 1 55  ? 38.61896 19.58005  13.15616  1.000 25.29300 ?  58  PRO   B HG2  1 
ATOM   3174 H  HG3  . PRO   B 1 55  ? 38.72668 20.39272  14.51755  1.000 25.29300 ?  58  PRO   B HG3  1 
ATOM   3175 H  HD2  . PRO   B 1 55  ? 40.77582 18.92706  13.25316  1.000 23.46910 ?  58  PRO   B HD2  1 
ATOM   3176 H  HD3  . PRO   B 1 55  ? 40.89129 20.38545  13.87378  1.000 23.46910 ?  58  PRO   B HD3  1 
ATOM   3177 N  N    . ARG   B 1 56  ? 39.67370 16.14979  17.21381  1.000 16.11249 ?  59  ARG   B N    1 
ATOM   3178 C  CA   . ARG   B 1 56  ? 40.06503 14.78279  17.51840  1.000 14.89734 ?  59  ARG   B CA   1 
ATOM   3179 C  C    . ARG   B 1 56  ? 39.52813 13.81951  16.46674  1.000 14.09103 ?  59  ARG   B C    1 
ATOM   3180 O  O    . ARG   B 1 56  ? 38.33880 13.83242  16.13577  1.000 15.87797 ?  59  ARG   B O    1 
ATOM   3181 C  CB   . ARG   B 1 56  ? 39.54728 14.39550  18.89447  1.000 16.36666 ?  59  ARG   B CB   1 
ATOM   3182 C  CG   . ARG   B 1 56  ? 39.97427 13.01544  19.30478  1.000 17.26421 ?  59  ARG   B CG   1 
ATOM   3183 C  CD   . ARG   B 1 56  ? 39.59057 12.74695  20.71570  1.000 19.05811 ?  59  ARG   B CD   1 
ATOM   3184 N  NE   . ARG   B 1 56  ? 39.87205 11.38125  21.11028  1.000 20.43602 ?  59  ARG   B NE   1 
ATOM   3185 C  CZ   . ARG   B 1 56  ? 39.68707 10.93078  22.34044  1.000 22.19706 ?  59  ARG   B CZ   1 
ATOM   3186 N  NH1  . ARG   B 1 56  ? 39.25443 11.72359  23.30382  1.000 24.68188 ?  59  ARG   B NH1  1 
ATOM   3187 N  NH2  . ARG   B 1 56  ? 39.93020 9.65334   22.60948  1.000 22.84992 ?  59  ARG   B NH2  1 
ATOM   3188 H  H    . ARG   B 1 56  ? 39.15890 16.51484  17.79804  1.000 19.33498 ?  59  ARG   B H    1 
ATOM   3189 H  HA   . ARG   B 1 56  ? 41.03295 14.71923  17.51944  1.000 17.87680 ?  59  ARG   B HA   1 
ATOM   3190 H  HB2  . ARG   B 1 56  ? 39.88969 15.02370  19.54947  1.000 19.63999 ?  59  ARG   B HB2  1 
ATOM   3191 H  HB3  . ARG   B 1 56  ? 38.57764 14.42052  18.88605  1.000 19.63999 ?  59  ARG   B HB3  1 
ATOM   3192 H  HG2  . ARG   B 1 56  ? 39.54098 12.35919  18.73689  1.000 20.71705 ?  59  ARG   B HG2  1 
ATOM   3193 H  HG3  . ARG   B 1 56  ? 40.93794 12.93705  19.22676  1.000 20.71705 ?  59  ARG   B HG3  1 
ATOM   3194 H  HD2  . ARG   B 1 56  ? 40.09008 13.33898  21.29955  1.000 22.86974 ?  59  ARG   B HD2  1 
ATOM   3195 H  HD3  . ARG   B 1 56  ? 38.63889 12.90181  20.82170  1.000 22.86974 ?  59  ARG   B HD3  1 
ATOM   3196 H  HE   . ARG   B 1 56  ? 40.17384 10.83748  20.51628  1.000 24.52322 ?  59  ARG   B HE   1 
ATOM   3197 H  HH11 . ARG   B 1 56  ? 39.08700 12.55057  23.13748  1.000 29.61826 ?  59  ARG   B HH11 1 
ATOM   3198 H  HH12 . ARG   B 1 56  ? 39.14010 11.41292  24.09755  1.000 29.61826 ?  59  ARG   B HH12 1 
ATOM   3199 H  HH21 . ARG   B 1 56  ? 40.20513 9.12756   21.98693  1.000 27.41991 ?  59  ARG   B HH21 1 
ATOM   3200 H  HH22 . ARG   B 1 56  ? 39.81273 9.35180   23.40627  1.000 27.41991 ?  59  ARG   B HH22 1 
ATOM   3201 N  N    . ALA   B 1 57  ? 40.41359 12.95413  15.98564  1.000 14.40428 ?  60  ALA   B N    1 
ATOM   3202 C  CA   . ALA   B 1 57  ? 40.05072 11.95481  14.99838  1.000 13.96868 ?  60  ALA   B CA   1 
ATOM   3203 C  C    . ALA   B 1 57  ? 38.90268 11.07738  15.46712  1.000 13.52134 ?  60  ALA   B C    1 
ATOM   3204 O  O    . ALA   B 1 57  ? 38.86114 10.62658  16.61525  1.000 13.67249 ?  60  ALA   B O    1 
ATOM   3205 C  CB   . ALA   B 1 57  ? 41.26111 11.07177  14.73983  1.000 15.54463 ?  60  ALA   B CB   1 
ATOM   3206 H  H    . ALA   B 1 57  ? 41.24082 12.92639  16.21914  1.000 17.28514 ?  60  ALA   B H    1 
ATOM   3207 H  HA   . ALA   B 1 57  ? 39.76683 12.40322  14.18645  1.000 16.76241 ?  60  ALA   B HA   1 
ATOM   3208 H  HB1  . ALA   B 1 57  ? 41.01692 10.37872  14.10662  1.000 18.65356 ?  60  ALA   B HB1  1 
ATOM   3209 H  HB2  . ALA   B 1 57  ? 41.97674 11.61569  14.37525  1.000 18.65356 ?  60  ALA   B HB2  1 
ATOM   3210 H  HB3  . ALA   B 1 57  ? 41.54388 10.67065  15.57652  1.000 18.65356 ?  60  ALA   B HB3  1 
ATOM   3211 N  N    . ASP   B 1 58  ? 38.00915 10.76827  14.53668  1.000 13.78844 ?  61  ASP   B N    1 
ATOM   3212 C  CA   . ASP   B 1 58  ? 36.96486 9.80393   14.81773  1.000 13.21730 ?  61  ASP   B CA   1 
ATOM   3213 C  C    . ASP   B 1 58  ? 37.57579 8.48375   15.28733  1.000 13.05217 ?  61  ASP   B C    1 
ATOM   3214 O  O    . ASP   B 1 58  ? 38.61925 8.03568   14.79254  1.000 13.05643 ?  61  ASP   B O    1 
ATOM   3215 C  CB   . ASP   B 1 58  ? 36.14372 9.50828   13.55857  1.000 14.42281 ?  61  ASP   B CB   1 
ATOM   3216 C  CG   . ASP   B 1 58  ? 35.12052 10.58688  13.21010  1.000 15.34620 ?  61  ASP   B CG   1 
ATOM   3217 O  OD1  . ASP   B 1 58  ? 35.05628 11.65083  13.85969  1.000 15.98706 ?  61  ASP   B OD1  1 
ATOM   3218 O  OD2  . ASP   B 1 58  ? 34.35802 10.34052  12.23326  1.000 17.46499 ?  61  ASP   B OD2  1 
ATOM   3219 H  H    . ASP   B 1 58  ? 37.98817 11.10077  13.74383  1.000 16.54613 ?  61  ASP   B H    1 
ATOM   3220 H  HA   . ASP   B 1 58  ? 36.38661 10.17365  15.50317  1.000 15.86075 ?  61  ASP   B HA   1 
ATOM   3221 H  HB2  . ASP   B 1 58  ? 36.74945 9.42391   12.80566  1.000 17.30737 ?  61  ASP   B HB2  1 
ATOM   3222 H  HB3  . ASP   B 1 58  ? 35.66103 8.67735   13.69076  1.000 17.30737 ?  61  ASP   B HB3  1 
ATOM   3223 N  N    . VAL   B 1 59  ? 36.88588 7.82912   16.21222  1.000 12.59321 ?  62  VAL   B N    1 
ATOM   3224 C  CA   . VAL   B 1 59  ? 37.27745 6.51837   16.72666  1.000 12.82179 ?  62  VAL   B CA   1 
ATOM   3225 C  C    . VAL   B 1 59  ? 36.17259 5.55605   16.31967  1.000 12.39552 ?  62  VAL   B C    1 
ATOM   3226 O  O    . VAL   B 1 59  ? 35.07451 5.56589   16.88679  1.000 12.64677 ?  62  VAL   B O    1 
ATOM   3227 C  CB   . VAL   B 1 59  ? 37.51835 6.49095   18.24036  1.000 13.62003 ?  62  VAL   B CB   1 
ATOM   3228 C  CG1  . VAL   B 1 59  ? 37.95854 5.09602   18.64168  1.000 13.62176 ?  62  VAL   B CG1  1 
ATOM   3229 C  CG2  . VAL   B 1 59  ? 38.55574 7.54387   18.63425  1.000 14.50845 ?  62  VAL   B CG2  1 
ATOM   3230 H  H    . VAL   B 1 59  ? 36.16447 8.13156   16.56957  1.000 15.11185 ?  62  VAL   B H    1 
ATOM   3231 H  HA   . VAL   B 1 59  ? 38.10828 6.25300   16.30214  1.000 15.38615 ?  62  VAL   B HA   1 
ATOM   3232 H  HB   . VAL   B 1 59  ? 36.70113 6.70614   18.71654  1.000 16.34404 ?  62  VAL   B HB   1 
ATOM   3233 H  HG11 . VAL   B 1 59  ? 38.24457 5.10952   19.56845  1.000 16.34611 ?  62  VAL   B HG11 1 
ATOM   3234 H  HG12 . VAL   B 1 59  ? 37.21178 4.48624   18.53483  1.000 16.34611 ?  62  VAL   B HG12 1 
ATOM   3235 H  HG13 . VAL   B 1 59  ? 38.69422 4.82101   18.07243  1.000 16.34611 ?  62  VAL   B HG13 1 
ATOM   3236 H  HG21 . VAL   B 1 59  ? 38.73982 7.46622   19.58345  1.000 17.41013 ?  62  VAL   B HG21 1 
ATOM   3237 H  HG22 . VAL   B 1 59  ? 39.36809 7.39233   18.12629  1.000 17.41013 ?  62  VAL   B HG22 1 
ATOM   3238 H  HG23 . VAL   B 1 59  ? 38.20182 8.42518   18.43696  1.000 17.41013 ?  62  VAL   B HG23 1 
ATOM   3239 N  N    . ALA   B 1 60  ? 36.45038 4.73580   15.30583  1.000 11.52673 ?  63  ALA   B N    1 
ATOM   3240 C  CA   . ALA   B 1 60  ? 35.46039 3.76139   14.86331  1.000 11.52645 ?  63  ALA   B CA   1 
ATOM   3241 C  C    . ALA   B 1 60  ? 35.17968 2.73944   15.95431  1.000 11.77049 ?  63  ALA   B C    1 
ATOM   3242 O  O    . ALA   B 1 60  ? 34.02872 2.32608   16.14150  1.000 12.39619 ?  63  ALA   B O    1 
ATOM   3243 C  CB   . ALA   B 1 60  ? 35.95890 3.05457   13.60879  1.000 12.23622 ?  63  ALA   B CB   1 
ATOM   3244 H  H    . ALA   B 1 60  ? 37.19001 4.72448   14.86716  1.000 13.83207 ?  63  ALA   B H    1 
ATOM   3245 H  HA   . ALA   B 1 60  ? 34.63466 4.22429   14.65167  1.000 13.83174 ?  63  ALA   B HA   1 
ATOM   3246 H  HB1  . ALA   B 1 60  ? 35.32728 2.35967   13.36574  1.000 14.68346 ?  63  ALA   B HB1  1 
ATOM   3247 H  HB2  . ALA   B 1 60  ? 36.03186 3.70149   12.88971  1.000 14.68346 ?  63  ALA   B HB2  1 
ATOM   3248 H  HB3  . ALA   B 1 60  ? 36.82750 2.66309   13.79093  1.000 14.68346 ?  63  ALA   B HB3  1 
ATOM   3249 N  N    . PHE   B 1 61  ? 36.22194 2.29270   16.65875  1.000 11.48014 ?  64  PHE   B N    1 
ATOM   3250 C  CA   . PHE   B 1 61  ? 36.07073 1.28153   17.69890  1.000 11.32611 ?  64  PHE   B CA   1 
ATOM   3251 C  C    . PHE   B 1 61  ? 36.99661 1.65686   18.82973  1.000 11.70090 ?  64  PHE   B C    1 
ATOM   3252 O  O    . PHE   B 1 61  ? 38.21232 1.63752   18.66760  1.000 12.36518 ?  64  PHE   B O    1 
ATOM   3253 C  CB   . PHE   B 1 61  ? 36.42621 -0.08612  17.14819  1.000 11.69315 ?  64  PHE   B CB   1 
ATOM   3254 C  CG   . PHE   B 1 61  ? 36.23691 -1.24173  18.12051  1.000 11.99391 ?  64  PHE   B CG   1 
ATOM   3255 C  CD1  . PHE   B 1 61  ? 35.13024 -1.33541  18.93385  1.000 12.98548 ?  64  PHE   B CD1  1 
ATOM   3256 C  CD2  . PHE   B 1 61  ? 37.13551 -2.28438  18.13040  1.000 13.88864 ?  64  PHE   B CD2  1 
ATOM   3257 C  CE1  . PHE   B 1 61  ? 34.95793 -2.42907  19.76985  1.000 13.50597 ?  64  PHE   B CE1  1 
ATOM   3258 C  CE2  . PHE   B 1 61  ? 36.96048 -3.37647  18.95237  1.000 14.01502 ?  64  PHE   B CE2  1 
ATOM   3259 C  CZ   . PHE   B 1 61  ? 35.87813 -3.44974  19.76493  1.000 13.21851 ?  64  PHE   B CZ   1 
ATOM   3260 H  H    . PHE   B 1 61  ? 37.03072 2.56385   16.54946  1.000 13.77617 ?  64  PHE   B H    1 
ATOM   3261 H  HA   . PHE   B 1 61  ? 35.15998 1.26557   18.03233  1.000 13.59134 ?  64  PHE   B HA   1 
ATOM   3262 H  HB2  . PHE   B 1 61  ? 35.86560 -0.26123  16.37621  1.000 14.03178 ?  64  PHE   B HB2  1 
ATOM   3263 H  HB3  . PHE   B 1 61  ? 37.35983 -0.07778  16.88515  1.000 14.03178 ?  64  PHE   B HB3  1 
ATOM   3264 H  HD1  . PHE   B 1 61  ? 34.49199 -0.65908  18.92279  1.000 15.58258 ?  64  PHE   B HD1  1 
ATOM   3265 H  HD2  . PHE   B 1 61  ? 37.87702 -2.25107  17.57008  1.000 16.66637 ?  64  PHE   B HD2  1 
ATOM   3266 H  HE1  . PHE   B 1 61  ? 34.21956 -2.47149  20.33369  1.000 16.20717 ?  64  PHE   B HE1  1 
ATOM   3267 H  HE2  . PHE   B 1 61  ? 37.58617 -4.06451  18.94955  1.000 16.81802 ?  64  PHE   B HE2  1 
ATOM   3268 H  HZ   . PHE   B 1 61  ? 35.75860 -4.18831  20.31732  1.000 15.86222 ?  64  PHE   B HZ   1 
ATOM   3269 N  N    . HIS   B 1 62  ? 36.40348 2.00935   19.95684  1.000 11.83132 ?  65  HIS   B N    1 
ATOM   3270 C  CA   . HIS   B 1 62  ? 37.07421 2.27819   21.22323  1.000 12.42163 ?  65  HIS   B CA   1 
ATOM   3271 C  C    . HIS   B 1 62  ? 36.79852 1.06933   22.10122  1.000 12.03681 ?  65  HIS   B C    1 
ATOM   3272 O  O    . HIS   B 1 62  ? 35.64086 0.80023   22.43740  1.000 13.14260 ?  65  HIS   B O    1 
ATOM   3273 C  CB   . HIS   B 1 62  ? 36.45032 3.52837   21.83564  1.000 12.89389 ?  65  HIS   B CB   1 
ATOM   3274 C  CG   . HIS   B 1 62  ? 36.84283 3.87619   23.24795  1.000 13.06376 ?  65  HIS   B CG   1 
ATOM   3275 N  ND1  . HIS   B 1 62  ? 38.09122 4.33512   23.60509  1.000 14.05279 ?  65  HIS   B ND1  1 
ATOM   3276 C  CD2  . HIS   B 1 62  ? 36.07967 3.96074   24.36910  1.000 14.00160 ?  65  HIS   B CD2  1 
ATOM   3277 C  CE1  . HIS   B 1 62  ? 38.08406 4.66966   24.88675  1.000 13.81012 ?  65  HIS   B CE1  1 
ATOM   3278 N  NE2  . HIS   B 1 62  ? 36.87523 4.45541   25.37326  1.000 14.45685 ?  65  HIS   B NE2  1 
ATOM   3279 H  H    . HIS   B 1 62  ? 35.55149 2.10728   20.02107  1.000 14.19758 ?  65  HIS   B H    1 
ATOM   3280 H  HA   . HIS   B 1 62  ? 38.03101 2.40623   21.12817  1.000 14.90596 ?  65  HIS   B HA   1 
ATOM   3281 H  HB2  . HIS   B 1 62  ? 36.69559 4.28580   21.28154  1.000 15.47267 ?  65  HIS   B HB2  1 
ATOM   3282 H  HB3  . HIS   B 1 62  ? 35.48721 3.41296   21.83233  1.000 15.47267 ?  65  HIS   B HB3  1 
ATOM   3283 H  HD1  . HIS   B 1 62  ? 38.76877 4.39506   23.07885  1.000 16.86335 ?  65  HIS   B HD1  1 
ATOM   3284 H  HD2  . HIS   B 1 62  ? 35.18269 3.72647   24.44289  1.000 16.80192 ?  65  HIS   B HD2  1 
ATOM   3285 H  HE1  . HIS   B 1 62  ? 38.80999 5.00056   25.36470  1.000 16.57215 ?  65  HIS   B HE1  1 
ATOM   3286 N  N    . PHE   B 1 63  ? 37.85204 0.34425   22.46744  1.000 11.62361 ?  66  PHE   B N    1 
ATOM   3287 C  CA   . PHE   B 1 63  ? 37.79374 -0.87845  23.27546  1.000 12.07079 ?  66  PHE   B CA   1 
ATOM   3288 C  C    . PHE   B 1 63  ? 38.52357 -0.56160  24.57413  1.000 12.46894 ?  66  PHE   B C    1 
ATOM   3289 O  O    . PHE   B 1 63  ? 39.74384 -0.36785  24.57648  1.000 12.90971 ?  66  PHE   B O    1 
ATOM   3290 C  CB   . PHE   B 1 63  ? 38.46979 -2.00268  22.49997  1.000 12.37005 ?  66  PHE   B CB   1 
ATOM   3291 C  CG   . PHE   B 1 63  ? 38.58462 -3.31051  23.25696  1.000 12.80289 ?  66  PHE   B CG   1 
ATOM   3292 C  CD1  . PHE   B 1 63  ? 37.54281 -4.23179  23.25817  1.000 13.51231 ?  66  PHE   B CD1  1 
ATOM   3293 C  CD2  . PHE   B 1 63  ? 39.72217 -3.61673  23.98675  1.000 13.48758 ?  66  PHE   B CD2  1 
ATOM   3294 C  CE1  . PHE   B 1 63  ? 37.67243 -5.45106  23.93682  1.000 14.14733 ?  66  PHE   B CE1  1 
ATOM   3295 C  CE2  . PHE   B 1 63  ? 39.83520 -4.81728  24.65105  1.000 14.40857 ?  66  PHE   B CE2  1 
ATOM   3296 C  CZ   . PHE   B 1 63  ? 38.81533 -5.72712  24.60943  1.000 14.41908 ?  66  PHE   B CZ   1 
ATOM   3297 H  H    . PHE   B 1 63  ? 38.65812 0.54958   22.24908  1.000 13.94833 ?  66  PHE   B H    1 
ATOM   3298 H  HA   . PHE   B 1 63  ? 36.88643 -1.14716  23.48873  1.000 14.48495 ?  66  PHE   B HA   1 
ATOM   3299 H  HB2  . PHE   B 1 63  ? 37.95639 -2.17465  21.69515  1.000 14.84405 ?  66  PHE   B HB2  1 
ATOM   3300 H  HB3  . PHE   B 1 63  ? 39.36785 -1.72001  22.26653  1.000 14.84405 ?  66  PHE   B HB3  1 
ATOM   3301 H  HD1  . PHE   B 1 63  ? 36.75421 -4.03728  22.80522  1.000 16.21477 ?  66  PHE   B HD1  1 
ATOM   3302 H  HD2  . PHE   B 1 63  ? 40.41919 -3.00247  24.02837  1.000 16.18509 ?  66  PHE   B HD2  1 
ATOM   3303 H  HE1  . PHE   B 1 63  ? 36.97667 -6.06807  23.92543  1.000 16.97680 ?  66  PHE   B HE1  1 
ATOM   3304 H  HE2  . PHE   B 1 63  ? 40.60856 -5.01028  25.13019  1.000 17.29028 ?  66  PHE   B HE2  1 
ATOM   3305 H  HZ   . PHE   B 1 63  ? 38.90717 -6.54270  25.04680  1.000 17.30290 ?  66  PHE   B HZ   1 
ATOM   3306 N  N    . ASN   B 1 64  ? 37.77098 -0.44373  25.67435  1.000 12.25986 ?  67  ASN   B N    1 
ATOM   3307 C  CA   . ASN   B 1 64  ? 38.24772 0.23731   26.88659  1.000 13.00248 ?  67  ASN   B CA   1 
ATOM   3308 C  C    . ASN   B 1 64  ? 38.03390 -0.58416  28.14426  1.000 13.99840 ?  67  ASN   B C    1 
ATOM   3309 O  O    . ASN   B 1 64  ? 37.05691 -0.37979  28.88084  1.000 14.16730 ?  67  ASN   B O    1 
ATOM   3310 C  CB   . ASN   B 1 64  ? 37.54040 1.59630   26.96086  1.000 13.07978 ?  67  ASN   B CB   1 
ATOM   3311 C  CG   . ASN   B 1 64  ? 37.82739 2.41027   28.22029  1.000 14.16080 ?  67  ASN   B CG   1 
ATOM   3312 O  OD1  . ASN   B 1 64  ? 36.95312 3.15572   28.67015  1.000 15.06340 ?  67  ASN   B OD1  1 
ATOM   3313 N  ND2  . ASN   B 1 64  ? 39.02630 2.31833   28.75686  1.000 14.76193 ?  67  ASN   B ND2  1 
ATOM   3314 H  H    . ASN   B 1 64  ? 36.97175 -0.75366  25.74355  1.000 14.71183 ?  67  ASN   B H    1 
ATOM   3315 H  HA   . ASN   B 1 64  ? 39.21194 0.33239   26.84028  1.000 15.60298 ?  67  ASN   B HA   1 
ATOM   3316 H  HB2  . ASN   B 1 64  ? 37.82093 2.12999   26.20102  1.000 15.69573 ?  67  ASN   B HB2  1 
ATOM   3317 H  HB3  . ASN   B 1 64  ? 36.58278 1.44598   26.92524  1.000 15.69573 ?  67  ASN   B HB3  1 
ATOM   3318 H  HD21 . ASN   B 1 64  ? 39.21527 2.76587   29.46651  1.000 17.71432 ?  67  ASN   B HD21 1 
ATOM   3319 H  HD22 . ASN   B 1 64  ? 39.62038 1.81074   28.39767  1.000 17.71432 ?  67  ASN   B HD22 1 
ATOM   3320 N  N    . PRO   B 1 65  ? 38.96925 -1.48990  28.45749  1.000 13.73060 ?  68  PRO   B N    1 
ATOM   3321 C  CA   . PRO   B 1 65  ? 38.92896 -2.16738  29.75596  1.000 14.11018 ?  68  PRO   B CA   1 
ATOM   3322 C  C    . PRO   B 1 65  ? 39.12638 -1.17513  30.90120  1.000 13.81452 ?  68  PRO   B C    1 
ATOM   3323 O  O    . PRO   B 1 65  ? 40.03053 -0.33671  30.88082  1.000 15.38004 ?  68  PRO   B O    1 
ATOM   3324 C  CB   . PRO   B 1 65  ? 40.08358 -3.17019  29.65384  1.000 14.70077 ?  68  PRO   B CB   1 
ATOM   3325 C  CG   . PRO   B 1 65  ? 40.25435 -3.40797  28.16049  1.000 13.62623 ?  68  PRO   B CG   1 
ATOM   3326 C  CD   . PRO   B 1 65  ? 40.07254 -2.01542  27.62002  1.000 14.23060 ?  68  PRO   B CD   1 
ATOM   3327 H  HA   . PRO   B 1 65  ? 38.09311 -2.64287  29.88308  1.000 16.93222 ?  68  PRO   B HA   1 
ATOM   3328 H  HB2  . PRO   B 1 65  ? 40.88801 -2.79041  30.04057  1.000 17.64092 ?  68  PRO   B HB2  1 
ATOM   3329 H  HB3  . PRO   B 1 65  ? 39.85071 -3.99213  30.11328  1.000 17.64092 ?  68  PRO   B HB3  1 
ATOM   3330 H  HG2  . PRO   B 1 65  ? 41.13759 -3.75799  27.96487  1.000 16.35148 ?  68  PRO   B HG2  1 
ATOM   3331 H  HG3  . PRO   B 1 65  ? 39.57548 -4.01537  27.82721  1.000 16.35148 ?  68  PRO   B HG3  1 
ATOM   3332 H  HD2  . PRO   B 1 65  ? 40.87892 -1.48877  27.73535  1.000 17.07672 ?  68  PRO   B HD2  1 
ATOM   3333 H  HD3  . PRO   B 1 65  ? 39.82031 -2.03519  26.68360  1.000 17.07672 ?  68  PRO   B HD3  1 
ATOM   3334 N  N    . ARG   B 1 66  ? 38.30237 -1.33254  31.95058  1.000 15.44328 ?  69  ARG   B N    1 
ATOM   3335 C  CA   . ARG   B 1 66  ? 38.34479 -0.51896  33.16446  1.000 16.04598 ?  69  ARG   B CA   1 
ATOM   3336 C  C    . ARG   B 1 66  ? 38.41856 -1.47617  34.34800  1.000 16.99929 ?  69  ARG   B C    1 
ATOM   3337 O  O    . ARG   B 1 66  ? 37.74702 -2.50969  34.36641  1.000 18.56523 ?  69  ARG   B O    1 
ATOM   3338 C  CB   . ARG   B 1 66  ? 37.10021 0.35318   33.26622  1.000 16.68670 ?  69  ARG   B CB   1 
ATOM   3339 C  CG   . ARG   B 1 66  ? 36.93869 1.30064   32.08621  1.000 17.12531 ?  69  ARG   B CG   1 
ATOM   3340 C  CD   . ARG   B 1 66  ? 35.71395 2.17868   32.24167  1.000 17.27430 ?  69  ARG   B CD   1 
ATOM   3341 N  NE   . ARG   B 1 66  ? 35.58116 3.06270   31.08813  1.000 16.52023 ?  69  ARG   B NE   1 
ATOM   3342 C  CZ   . ARG   B 1 66  ? 34.64686 3.98996   30.95372  1.000 16.34723 ?  69  ARG   B CZ   1 
ATOM   3343 N  NH1  . ARG   B 1 66  ? 33.74562 4.20657   31.89570  1.000 18.17253 ?  69  ARG   B NH1  1 
ATOM   3344 N  NH2  . ARG   B 1 66  ? 34.61975 4.72252   29.84867  1.000 17.07540 ?  69  ARG   B NH2  1 
ATOM   3345 H  H    . ARG   B 1 66  ? 37.68589 -1.93152  31.97818  1.000 18.53194 ?  69  ARG   B H    1 
ATOM   3346 H  HA   . ARG   B 1 66  ? 39.11852 0.06593   33.17657  1.000 19.25517 ?  69  ARG   B HA   1 
ATOM   3347 H  HB2  . ARG   B 1 66  ? 36.31737 -0.21858  33.30017  1.000 20.02404 ?  69  ARG   B HB2  1 
ATOM   3348 H  HB3  . ARG   B 1 66  ? 37.15587 0.88775   34.07370  1.000 20.02404 ?  69  ARG   B HB3  1 
ATOM   3349 H  HG2  . ARG   B 1 66  ? 37.71884 1.87386   32.02544  1.000 20.55037 ?  69  ARG   B HG2  1 
ATOM   3350 H  HG3  . ARG   B 1 66  ? 36.84199 0.78440   31.27071  1.000 20.55037 ?  69  ARG   B HG3  1 
ATOM   3351 H  HD2  . ARG   B 1 66  ? 34.92027 1.62426   32.30156  1.000 20.72916 ?  69  ARG   B HD2  1 
ATOM   3352 H  HD3  . ARG   B 1 66  ? 35.80065 2.72135   33.04098  1.000 20.72916 ?  69  ARG   B HD3  1 
ATOM   3353 H  HE   . ARG   B 1 66  ? 36.15096 2.97468   30.45002  1.000 19.82428 ?  69  ARG   B HE   1 
ATOM   3354 H  HH11 . ARG   B 1 66  ? 33.14740 4.81474   31.78677  1.000 21.80703 ?  69  ARG   B HH11 1 
ATOM   3355 H  HH12 . ARG   B 1 66  ? 33.75736 3.73937   32.61763  1.000 21.80703 ?  69  ARG   B HH12 1 
ATOM   3356 H  HH21 . ARG   B 1 66  ? 35.20431 4.59171   29.23160  1.000 20.49048 ?  69  ARG   B HH21 1 
ATOM   3357 H  HH22 . ARG   B 1 66  ? 34.01761 5.32842   29.74910  1.000 20.49048 ?  69  ARG   B HH22 1 
ATOM   3358 N  N    . PHE   B 1 67  ? 39.22360 -1.14783  35.34241  1.000 17.63347 ?  70  PHE   B N    1 
ATOM   3359 C  CA   A PHE   B 1 67  ? 39.55940 -2.11725  36.37567  0.554 18.24641 ?  70  PHE   B CA   1 
ATOM   3360 C  CA   B PHE   B 1 67  ? 39.57139 -2.12063  36.36790  0.446 18.38669 ?  70  PHE   B CA   1 
ATOM   3361 C  C    . PHE   B 1 67  ? 38.98470 -1.82918  37.74398  1.000 20.13572 ?  70  PHE   B C    1 
ATOM   3362 O  O    . PHE   B 1 67  ? 39.08934 -2.68939  38.62506  1.000 23.33580 ?  70  PHE   B O    1 
ATOM   3363 C  CB   A PHE   B 1 67  ? 41.07179 -2.24964  36.45618  0.554 19.02630 ?  70  PHE   B CB   1 
ATOM   3364 C  CB   B PHE   B 1 67  ? 41.10324 -2.26995  36.41757  0.446 18.83387 ?  70  PHE   B CB   1 
ATOM   3365 C  CG   A PHE   B 1 67  ? 41.61861 -2.81920  35.22742  0.554 18.67933 ?  70  PHE   B CG   1 
ATOM   3366 C  CG   B PHE   B 1 67  ? 41.71566 -2.45060  35.04780  0.446 17.81962 ?  70  PHE   B CG   1 
ATOM   3367 C  CD1  A PHE   B 1 67  ? 41.70383 -4.19059  35.08084  0.554 20.02547 ?  70  PHE   B CD1  1 
ATOM   3368 C  CD1  B PHE   B 1 67  ? 41.34023 -3.52119  34.24185  0.446 18.27969 ?  70  PHE   B CD1  1 
ATOM   3369 C  CD2  A PHE   B 1 67  ? 41.93014 -1.99534  34.15428  0.554 19.60352 ?  70  PHE   B CD2  1 
ATOM   3370 C  CD2  B PHE   B 1 67  ? 42.61767 -1.53126  34.53731  0.446 17.34579 ?  70  PHE   B CD2  1 
ATOM   3371 C  CE1  A PHE   B 1 67  ? 42.16405 -4.72725  33.91393  0.554 19.51485 ?  70  PHE   B CE1  1 
ATOM   3372 C  CE1  B PHE   B 1 67  ? 41.86742 -3.67656  32.96532  0.446 17.04212 ?  70  PHE   B CE1  1 
ATOM   3373 C  CE2  A PHE   B 1 67  ? 42.38365 -2.52406  32.98135  0.554 18.81164 ?  70  PHE   B CE2  1 
ATOM   3374 C  CE2  B PHE   B 1 67  ? 43.14803 -1.68223  33.26605  0.446 17.17359 ?  70  PHE   B CE2  1 
ATOM   3375 C  CZ   A PHE   B 1 67  ? 42.49991 -3.88904  32.85585  0.554 19.84211 ?  70  PHE   B CZ   1 
ATOM   3376 C  CZ   B PHE   B 1 67  ? 42.77476 -2.76183  32.48212  0.446 16.65954 ?  70  PHE   B CZ   1 
ATOM   3377 H  H    . PHE   B 1 67  ? 39.58666 -0.37453  35.44139  1.000 21.16016 ?  70  PHE   B H    1 
ATOM   3378 H  HA   . PHE   B 1 67  ? 39.18691 -2.97670  36.12368  1.000 22.06402 ?  70  PHE   B HA   1 
ATOM   3379 H  HB2  A PHE   B 1 67  ? 41.46479 -1.37288  36.58935  0.554 22.83156 ?  70  PHE   B HB2  1 
ATOM   3380 H  HB2  B PHE   B 1 67  ? 41.48584 -1.47217  36.81514  0.446 22.60065 ?  70  PHE   B HB2  1 
ATOM   3381 H  HB3  A PHE   B 1 67  ? 41.30471 -2.83332  37.19507  0.554 22.83156 ?  70  PHE   B HB3  1 
ATOM   3382 H  HB3  B PHE   B 1 67  ? 41.32784 -3.04749  36.95225  0.446 22.60065 ?  70  PHE   B HB3  1 
ATOM   3383 H  HD1  A PHE   B 1 67  ? 41.44699 -4.74882  35.77892  0.554 24.03057 ?  70  PHE   B HD1  1 
ATOM   3384 H  HD1  B PHE   B 1 67  ? 40.72692 -4.14244  34.56249  0.446 21.93562 ?  70  PHE   B HD1  1 
ATOM   3385 H  HD2  A PHE   B 1 67  ? 41.82872 -1.07448  34.23578  0.554 23.52422 ?  70  PHE   B HD2  1 
ATOM   3386 H  HD2  B PHE   B 1 67  ? 42.87104 -0.80184  35.05562  0.446 20.81495 ?  70  PHE   B HD2  1 
ATOM   3387 H  HE1  A PHE   B 1 67  ? 42.25276 -5.64886  33.82637  0.554 23.41783 ?  70  PHE   B HE1  1 
ATOM   3388 H  HE1  B PHE   B 1 67  ? 41.60739 -4.39755  32.43858  0.446 20.45054 ?  70  PHE   B HE1  1 
ATOM   3389 H  HE2  A PHE   B 1 67  ? 42.61220 -1.96667  32.27285  0.554 22.57397 ?  70  PHE   B HE2  1 
ATOM   3390 H  HE2  B PHE   B 1 67  ? 43.75507 -1.05829  32.93879  0.446 20.60831 ?  70  PHE   B HE2  1 
ATOM   3391 H  HZ   A PHE   B 1 67  ? 42.80555 -4.25439  32.05709  0.554 23.81054 ?  70  PHE   B HZ   1 
ATOM   3392 H  HZ   B PHE   B 1 67  ? 43.13633 -2.86799  31.63189  0.446 19.99145 ?  70  PHE   B HZ   1 
ATOM   3393 N  N    . LYS   B 1 68  ? 38.33745 -0.68706  37.93867  1.000 21.31725 ?  71  LYS   B N    1 
ATOM   3394 C  CA   . LYS   B 1 68  ? 37.78719 -0.37555  39.25141  1.000 25.90616 ?  71  LYS   B CA   1 
ATOM   3395 C  C    . LYS   B 1 68  ? 36.64681 -1.32444  39.60587  1.000 28.18884 ?  71  LYS   B C    1 
ATOM   3396 O  O    . LYS   B 1 68  ? 35.87474 -1.75982  38.75874  1.000 28.08623 ?  71  LYS   B O    1 
ATOM   3397 C  CB   . LYS   B 1 68  ? 37.28629 1.06732   39.29599  1.000 29.05933 ?  71  LYS   B CB   1 
ATOM   3398 C  CG   . LYS   B 1 68  ? 38.40535 2.10621   39.20275  1.000 34.85100 ?  71  LYS   B CG   1 
ATOM   3399 C  CD   . LYS   B 1 68  ? 37.84979 3.51983   39.04954  1.000 39.16020 ?  71  LYS   B CD   1 
ATOM   3400 C  CE   . LYS   B 1 68  ? 38.95796 4.56287   39.07788  1.000 42.15341 ?  71  LYS   B CE   1 
ATOM   3401 N  NZ   . LYS   B 1 68  ? 39.49457 4.76308   40.45814  1.000 43.84757 ?  71  LYS   B NZ   1 
ATOM   3402 H  H    . LYS   B 1 68  ? 38.20528 -0.08578  37.33818  1.000 25.58071 ?  71  LYS   B H    1 
ATOM   3403 H  HA   . LYS   B 1 68  ? 38.48551 -0.47726  39.91691  1.000 31.08739 ?  71  LYS   B HA   1 
ATOM   3404 H  HB2  . LYS   B 1 68  ? 36.68366 1.21216   38.54982  1.000 34.87120 ?  71  LYS   B HB2  1 
ATOM   3405 H  HB3  . LYS   B 1 68  ? 36.81779 1.20980   40.13331  1.000 34.87120 ?  71  LYS   B HB3  1 
ATOM   3406 H  HG2  . LYS   B 1 68  ? 38.93989 2.07537   40.01158  1.000 41.82120 ?  71  LYS   B HG2  1 
ATOM   3407 H  HG3  . LYS   B 1 68  ? 38.95991 1.91194   38.43098  1.000 41.82120 ?  71  LYS   B HG3  1 
ATOM   3408 H  HD2  . LYS   B 1 68  ? 37.38529 3.59199   38.20105  1.000 46.99224 ?  71  LYS   B HD2  1 
ATOM   3409 H  HD3  . LYS   B 1 68  ? 37.23831 3.70528   39.77934  1.000 46.99224 ?  71  LYS   B HD3  1 
ATOM   3410 H  HE2  . LYS   B 1 68  ? 39.68660 4.27148   38.50772  1.000 50.58409 ?  71  LYS   B HE2  1 
ATOM   3411 H  HE3  . LYS   B 1 68  ? 38.60799 5.41054   38.76183  1.000 50.58409 ?  71  LYS   B HE3  1 
ATOM   3412 H  HZ1  . LYS   B 1 68  ? 40.14322 5.37236   40.44714  1.000 52.61709 ?  71  LYS   B HZ1  1 
ATOM   3413 H  HZ2  . LYS   B 1 68  ? 38.84556 5.04189   40.99958  1.000 52.61709 ?  71  LYS   B HZ2  1 
ATOM   3414 H  HZ3  . LYS   B 1 68  ? 39.82284 3.99734   40.77115  1.000 52.61709 ?  71  LYS   B HZ3  1 
ATOM   3415 N  N    . ARG   B 1 69  ? 36.52101 -1.61536  40.89194  1.000 32.48060 ?  72  ARG   B N    1 
ATOM   3416 C  CA   . ARG   B 1 69  ? 35.43838 -2.47650  41.40517  1.000 35.50175 ?  72  ARG   B CA   1 
ATOM   3417 C  C    . ARG   B 1 69  ? 35.54629 -3.84487  40.72691  1.000 33.05902 ?  72  ARG   B C    1 
ATOM   3418 O  O    . ARG   B 1 69  ? 36.63832 -4.43475  40.69728  1.000 32.26214 ?  72  ARG   B O    1 
ATOM   3419 C  CB   . ARG   B 1 69  ? 34.08140 -1.76681  41.28838  1.000 40.03283 ?  72  ARG   B CB   1 
ATOM   3420 C  CG   . ARG   B 1 69  ? 33.96017 -0.42506  42.03206  1.000 43.21972 ?  72  ARG   B CG   1 
ATOM   3421 C  CD   . ARG   B 1 69  ? 34.37219 -0.49543  43.51423  1.000 45.56460 ?  72  ARG   B CD   1 
ATOM   3422 N  NE   . ARG   B 1 69  ? 33.31391 -0.98325  44.39392  1.000 47.13428 ?  72  ARG   B NE   1 
ATOM   3423 C  CZ   . ARG   B 1 69  ? 33.48442 -1.27990  45.67618  1.000 47.88959 ?  72  ARG   B CZ   1 
ATOM   3424 N  NH1  . ARG   B 1 69  ? 34.66969 -1.18500  46.25654  1.000 47.65963 ?  72  ARG   B NH1  1 
ATOM   3425 N  NH2  . ARG   B 1 69  ? 32.43971 -1.68151  46.39506  1.000 48.35743 ?  72  ARG   B NH2  1 
ATOM   3426 H  H    . ARG   B 1 69  ? 37.05244 -1.32702  41.50352  1.000 38.97672 ?  72  ARG   B H    1 
ATOM   3427 H  HA   . ARG   B 1 69  ? 35.60732 -2.62388  42.34891  1.000 42.60210 ?  72  ARG   B HA   1 
ATOM   3428 H  HB2  . ARG   B 1 69  ? 33.91012 -1.59152  40.34986  1.000 48.03939 ?  72  ARG   B HB2  1 
ATOM   3429 H  HB3  . ARG   B 1 69  ? 33.39877 -2.35602  41.64580  1.000 48.03939 ?  72  ARG   B HB3  1 
ATOM   3430 H  HG2  . ARG   B 1 69  ? 34.53304 0.22587   41.59731  1.000 51.86366 ?  72  ARG   B HG2  1 
ATOM   3431 H  HG3  . ARG   B 1 69  ? 33.03666 -0.13052  41.99637  1.000 51.86366 ?  72  ARG   B HG3  1 
ATOM   3432 H  HD2  . ARG   B 1 69  ? 35.12895 -1.09609  43.60037  1.000 54.67752 ?  72  ARG   B HD2  1 
ATOM   3433 H  HD3  . ARG   B 1 69  ? 34.61881 0.39388   43.81292  1.000 54.67752 ?  72  ARG   B HD3  1 
ATOM   3434 H  HE   . ARG   B 1 69  ? 32.52833 -1.08506  44.05909  1.000 56.56114 ?  72  ARG   B HE   1 
ATOM   3435 H  HH11 . ARG   B 1 69  ? 35.35186 -0.92610  45.80135  1.000 57.19155 ?  72  ARG   B HH11 1 
ATOM   3436 H  HH12 . ARG   B 1 69  ? 34.75791 -1.38223  47.08896  1.000 57.19155 ?  72  ARG   B HH12 1 
ATOM   3437 H  HH21 . ARG   B 1 69  ? 31.66466 -1.74648  46.02809  1.000 58.02891 ?  72  ARG   B HH21 1 
ATOM   3438 H  HH22 . ARG   B 1 69  ? 32.53936 -1.87619  47.22678  1.000 58.02891 ?  72  ARG   B HH22 1 
ATOM   3439 N  N    . ALA   B 1 70  ? 34.45962 -4.41736  40.21682  1.000 31.11134 ?  73  ALA   B N    1 
ATOM   3440 C  CA   . ALA   B 1 70  ? 34.54010 -5.71784  39.56783  1.000 28.81921 ?  73  ALA   B CA   1 
ATOM   3441 C  C    . ALA   B 1 70  ? 35.08042 -5.63407  38.14407  1.000 25.92033 ?  73  ALA   B C    1 
ATOM   3442 O  O    . ALA   B 1 70  ? 35.25546 -6.67918  37.50698  1.000 28.13268 ?  73  ALA   B O    1 
ATOM   3443 C  CB   . ALA   B 1 70  ? 33.16580 -6.38102  39.53617  1.000 30.19709 ?  73  ALA   B CB   1 
ATOM   3444 H  H    . ALA   B 1 70  ? 33.67139 -4.07390  40.23483  1.000 37.33361 ?  73  ALA   B H    1 
ATOM   3445 H  HA   . ALA   B 1 70  ? 35.13432 -6.27966  40.08952  1.000 34.58305 ?  73  ALA   B HA   1 
ATOM   3446 H  HB1  . ALA   B 1 70  ? 33.26919 -7.30964  39.27564  1.000 36.23651 ?  73  ALA   B HB1  1 
ATOM   3447 H  HB2  . ALA   B 1 70  ? 32.76892 -6.32755  40.41965  1.000 36.23651 ?  73  ALA   B HB2  1 
ATOM   3448 H  HB3  . ALA   B 1 70  ? 32.60621 -5.91751  38.89358  1.000 36.23651 ?  73  ALA   B HB3  1 
ATOM   3449 N  N    . GLY   B 1 71  ? 35.34876 -4.43580  37.63231  1.000 21.93350 ?  74  GLY   B N    1 
ATOM   3450 C  CA   . GLY   B 1 71  ? 35.86447 -4.28031  36.29034  1.000 20.17219 ?  74  GLY   B CA   1 
ATOM   3451 C  C    . GLY   B 1 71  ? 34.78620 -4.38655  35.22409  1.000 18.32387 ?  74  GLY   B C    1 
ATOM   3452 O  O    . GLY   B 1 71  ? 33.68441 -4.89570  35.43739  1.000 19.98012 ?  74  GLY   B O    1 
ATOM   3453 H  H    . GLY   B 1 71  ? 35.23709 -3.69372  38.05236  1.000 26.32020 ?  74  GLY   B H    1 
ATOM   3454 H  HA2  . GLY   B 1 71  ? 36.28590 -3.41038  36.20969  1.000 24.20663 ?  74  GLY   B HA2  1 
ATOM   3455 H  HA3  . GLY   B 1 71  ? 36.52656 -4.96883  36.12161  1.000 24.20663 ?  74  GLY   B HA3  1 
ATOM   3456 N  N    . CYS   B 1 72  ? 35.12718 -3.90384  34.03383  1.000 16.99267 ?  75  CYS   B N    1 
ATOM   3457 C  CA   . CYS   B 1 72  ? 34.23538 -4.01758  32.88118  1.000 16.52053 ?  75  CYS   B CA   1 
ATOM   3458 C  C    . CYS   B 1 72  ? 35.05113 -3.70106  31.63064  1.000 15.55320 ?  75  CYS   B C    1 
ATOM   3459 O  O    . CYS   B 1 72  ? 36.22187 -3.33177  31.71514  1.000 16.04544 ?  75  CYS   B O    1 
ATOM   3460 C  CB   . CYS   B 1 72  ? 33.02979 -3.07875  32.99649  1.000 18.08839 ?  75  CYS   B CB   1 
ATOM   3461 S  SG   . CYS   B 1 72  ? 33.41562 -1.33278  32.94170  1.000 19.76353 ?  75  CYS   B SG   1 
ATOM   3462 H  H    . CYS   B 1 72  ? 35.87076 -3.50527  33.86700  1.000 20.39121 ?  75  CYS   B H    1 
ATOM   3463 H  HA   . CYS   B 1 72  ? 33.91144 -4.93034  32.82793  1.000 19.82463 ?  75  CYS   B HA   1 
ATOM   3464 H  HB2  . CYS   B 1 72  ? 32.42517 -3.26535  32.26130  1.000 21.70607 ?  75  CYS   B HB2  1 
ATOM   3465 H  HB3  . CYS   B 1 72  ? 32.58712 -3.25153  33.84212  1.000 21.70607 ?  75  CYS   B HB3  1 
ATOM   3466 H  HG   . CYS   B 1 72  ? 33.77685 -1.04708  31.83360  1.000 23.71624 ?  75  CYS   B HG   1 
ATOM   3467 N  N    . ILE   B 1 73  ? 34.41431 -3.80623  30.46670  1.000 15.41360 ?  76  ILE   B N    1 
ATOM   3468 C  CA   . ILE   B 1 73  ? 34.96060 -3.25642  29.22998  1.000 14.31960 ?  76  ILE   B CA   1 
ATOM   3469 C  C    . ILE   B 1 73  ? 33.89174 -2.35468  28.64674  1.000 14.92164 ?  76  ILE   B C    1 
ATOM   3470 O  O    . ILE   B 1 73  ? 32.76566 -2.80674  28.42303  1.000 15.73043 ?  76  ILE   B O    1 
ATOM   3471 C  CB   . ILE   B 1 73  ? 35.30188 -4.35064  28.19565  1.000 14.46687 ?  76  ILE   B CB   1 
ATOM   3472 C  CG1  . ILE   B 1 73  ? 36.30803 -5.36080  28.74993  1.000 15.82729 ?  76  ILE   B CG1  1 
ATOM   3473 C  CG2  . ILE   B 1 73  ? 35.86357 -3.69798  26.90315  1.000 15.00840 ?  76  ILE   B CG2  1 
ATOM   3474 C  CD1  . ILE   B 1 73  ? 36.33627 -6.66083  27.96988  1.000 16.50382 ?  76  ILE   B CD1  1 
ATOM   3475 H  H    . ILE   B 1 73  ? 33.65457 -4.19693  30.36798  1.000 18.49632 ?  76  ILE   B H    1 
ATOM   3476 H  HA   . ILE   B 1 73  ? 35.76821 -2.75764  29.42970  1.000 17.18352 ?  76  ILE   B HA   1 
ATOM   3477 H  HB   . ILE   B 1 73  ? 34.48293 -4.82950  27.99337  1.000 17.36024 ?  76  ILE   B HB   1 
ATOM   3478 H  HG12 . ILE   B 1 73  ? 37.19595 -4.97185  28.71495  1.000 18.99274 ?  76  ILE   B HG12 1 
ATOM   3479 H  HG13 . ILE   B 1 73  ? 36.07252 -5.56799  29.66781  1.000 18.99274 ?  76  ILE   B HG13 1 
ATOM   3480 H  HG21 . ILE   B 1 73  ? 36.31791 -4.37588  26.37882  1.000 18.01008 ?  76  ILE   B HG21 1 
ATOM   3481 H  HG22 . ILE   B 1 73  ? 35.12831 -3.32319  26.39341  1.000 18.01008 ?  76  ILE   B HG22 1 
ATOM   3482 H  HG23 . ILE   B 1 73  ? 36.48713 -2.99673  27.14877  1.000 18.01008 ?  76  ILE   B HG23 1 
ATOM   3483 H  HD11 . ILE   B 1 73  ? 36.80018 -7.33307  28.49312  1.000 19.80458 ?  76  ILE   B HD11 1 
ATOM   3484 H  HD12 . ILE   B 1 73  ? 35.42515 -6.94595  27.79817  1.000 19.80458 ?  76  ILE   B HD12 1 
ATOM   3485 H  HD13 . ILE   B 1 73  ? 36.80111 -6.51572  27.13097  1.000 19.80458 ?  76  ILE   B HD13 1 
ATOM   3486 N  N    . VAL   B 1 74  ? 34.24666 -1.10959  28.35896  1.000 13.93079 ?  77  VAL   B N    1 
ATOM   3487 C  CA   . VAL   B 1 74  ? 33.34824 -0.19255  27.66560  1.000 14.34773 ?  77  VAL   B CA   1 
ATOM   3488 C  C    . VAL   B 1 74  ? 33.78526 -0.12866  26.21018  1.000 13.53238 ?  77  VAL   B C    1 
ATOM   3489 O  O    . VAL   B 1 74  ? 34.96864 0.07006   25.92703  1.000 14.12133 ?  77  VAL   B O    1 
ATOM   3490 C  CB   . VAL   B 1 74  ? 33.35992 1.20407   28.30994  1.000 15.55741 ?  77  VAL   B CB   1 
ATOM   3491 C  CG1  . VAL   B 1 74  ? 32.49710 2.15999   27.49429  1.000 17.22699 ?  77  VAL   B CG1  1 
ATOM   3492 C  CG2  . VAL   B 1 74  ? 32.88994 1.11986   29.76580  1.000 17.32467 ?  77  VAL   B CG2  1 
ATOM   3493 H  H    . VAL   B 1 74  ? 35.01078 -0.76817  28.55682  1.000 16.71695 ?  77  VAL   B H    1 
ATOM   3494 H  HA   . VAL   B 1 74  ? 32.43997 -0.53044  27.70770  1.000 17.21727 ?  77  VAL   B HA   1 
ATOM   3495 H  HB   . VAL   B 1 74  ? 34.26406 1.55533   28.31677  1.000 18.66889 ?  77  VAL   B HB   1 
ATOM   3496 H  HG11 . VAL   B 1 74  ? 32.28872 2.93741   28.03566  1.000 20.67238 ?  77  VAL   B HG11 1 
ATOM   3497 H  HG12 . VAL   B 1 74  ? 32.98744 2.43029   26.70220  1.000 20.67238 ?  77  VAL   B HG12 1 
ATOM   3498 H  HG13 . VAL   B 1 74  ? 31.67887 1.70639   27.23806  1.000 20.67238 ?  77  VAL   B HG13 1 
ATOM   3499 H  HG21 . VAL   B 1 74  ? 32.90066 2.00914   30.15305  1.000 20.78960 ?  77  VAL   B HG21 1 
ATOM   3500 H  HG22 . VAL   B 1 74  ? 31.98906 0.76087   29.78657  1.000 20.78960 ?  77  VAL   B HG22 1 
ATOM   3501 H  HG23 . VAL   B 1 74  ? 33.48951 0.53749   30.25802  1.000 20.78960 ?  77  VAL   B HG23 1 
ATOM   3502 N  N    . CYS   B 1 75  ? 32.83277 -0.27875  25.29032  1.000 13.21687 ?  78  CYS   B N    1 
ATOM   3503 C  CA   . CYS   B 1 75  ? 33.07993 -0.02589  23.87474  1.000 13.20529 ?  78  CYS   B CA   1 
ATOM   3504 C  C    . CYS   B 1 75  ? 32.19429 1.11160   23.38165  1.000 13.92712 ?  78  CYS   B C    1 
ATOM   3505 O  O    . CYS   B 1 75  ? 31.04216 1.25862   23.80183  1.000 14.37204 ?  78  CYS   B O    1 
ATOM   3506 C  CB   . CYS   B 1 75  ? 32.83189 -1.27360  23.03045  1.000 13.66156 ?  78  CYS   B CB   1 
ATOM   3507 S  SG   . CYS   B 1 75  ? 33.95672 -2.64720  23.40078  1.000 14.53037 ?  78  CYS   B SG   1 
ATOM   3508 H  H    . CYS   B 1 75  ? 32.02873 -0.52853  25.46562  1.000 15.86024 ?  78  CYS   B H    1 
ATOM   3509 H  HA   . CYS   B 1 75  ? 34.00596 0.23951   23.76107  1.000 15.84634 ?  78  CYS   B HA   1 
ATOM   3510 H  HB2  . CYS   B 1 75  ? 31.92615 -1.58207  23.18979  1.000 16.39387 ?  78  CYS   B HB2  1 
ATOM   3511 H  HB3  . CYS   B 1 75  ? 32.94425 -1.04355  22.09485  1.000 16.39387 ?  78  CYS   B HB3  1 
ATOM   3512 H  HG   . CYS   B 1 75  ? 35.05287 -2.37463  22.99560  1.000 17.43645 ?  78  CYS   B HG   1 
ATOM   3513 N  N    . ASN   B 1 76  ? 32.73642 1.91780   22.47892  1.000 13.10997 ?  79  ASN   B N    1 
ATOM   3514 C  CA   . ASN   B 1 76  ? 31.99737 3.05403   21.94374  1.000 13.04362 ?  79  ASN   B CA   1 
ATOM   3515 C  C    . ASN   B 1 76  ? 32.67377 3.50602   20.65458  1.000 12.58776 ?  79  ASN   B C    1 
ATOM   3516 O  O    . ASN   B 1 76  ? 33.67658 2.93545   20.20842  1.000 12.79064 ?  79  ASN   B O    1 
ATOM   3517 C  CB   . ASN   B 1 76  ? 31.92822 4.18026   22.99251  1.000 13.39537 ?  79  ASN   B CB   1 
ATOM   3518 C  CG   . ASN   B 1 76  ? 30.68483 5.06305   22.86828  1.000 14.13881 ?  79  ASN   B CG   1 
ATOM   3519 O  OD1  . ASN   B 1 76  ? 30.01650 5.10778   21.83238  1.000 14.20917 ?  79  ASN   B OD1  1 
ATOM   3520 N  ND2  . ASN   B 1 76  ? 30.37225 5.78584   23.93408  1.000 15.23514 ?  79  ASN   B ND2  1 
ATOM   3521 H  H    . ASN   B 1 76  ? 33.53019 1.82839   22.16029  1.000 15.73196 ?  79  ASN   B H    1 
ATOM   3522 H  HA   . ASN   B 1 76  ? 31.09361 2.78395   21.71751  1.000 15.65234 ?  79  ASN   B HA   1 
ATOM   3523 H  HB2  . ASN   B 1 76  ? 31.92144 3.78289   23.87736  1.000 16.07445 ?  79  ASN   B HB2  1 
ATOM   3524 H  HB3  . ASN   B 1 76  ? 32.70665 4.74997   22.89063  1.000 16.07445 ?  79  ASN   B HB3  1 
ATOM   3525 H  HD21 . ASN   B 1 76  ? 29.68273 6.29955   23.91812  1.000 18.28216 ?  79  ASN   B HD21 1 
ATOM   3526 H  HD22 . ASN   B 1 76  ? 30.85892 5.74119   24.64173  1.000 18.28216 ?  79  ASN   B HD22 1 
ATOM   3527 N  N    . THR   B 1 77  ? 32.09192 4.55023   20.06590  1.000 12.73009 ?  80  THR   B N    1 
ATOM   3528 C  CA   . THR   B 1 77  ? 32.54803 5.20749   18.84890  1.000 12.53389 ?  80  THR   B CA   1 
ATOM   3529 C  C    . THR   B 1 77  ? 32.51351 6.70737   19.08885  1.000 12.76488 ?  80  THR   B C    1 
ATOM   3530 O  O    . THR   B 1 77  ? 31.56884 7.22762   19.70217  1.000 13.65888 ?  80  THR   B O    1 
ATOM   3531 C  CB   . THR   B 1 77  ? 31.61268 4.82968   17.68788  1.000 12.88454 ?  80  THR   B CB   1 
ATOM   3532 O  OG1  . THR   B 1 77  ? 31.75413 3.42852   17.40800  1.000 12.82128 ?  80  THR   B OG1  1 
ATOM   3533 C  CG2  . THR   B 1 77  ? 31.89474 5.60578   16.39491  1.000 13.80304 ?  80  THR   B CG2  1 
ATOM   3534 H  H    . THR   B 1 77  ? 31.38071 4.92013   20.37729  1.000 15.27611 ?  80  THR   B H    1 
ATOM   3535 H  HA   . THR   B 1 77  ? 33.45490 4.95465   18.61528  1.000 15.04067 ?  80  THR   B HA   1 
ATOM   3536 H  HB   . THR   B 1 77  ? 30.70861 5.05227   17.95994  1.000 15.46145 ?  80  THR   B HB   1 
ATOM   3537 H  HG1  . THR   B 1 77  ? 31.19940 3.19517   16.82197  1.000 15.38553 ?  80  THR   B HG1  1 
ATOM   3538 H  HG21 . THR   B 1 77  ? 31.26262 5.34508   15.70689  1.000 16.56365 ?  80  THR   B HG21 1 
ATOM   3539 H  HG22 . THR   B 1 77  ? 31.81059 6.55878   16.55494  1.000 16.56365 ?  80  THR   B HG22 1 
ATOM   3540 H  HG23 . THR   B 1 77  ? 32.79398 5.41695   16.08409  1.000 16.56365 ?  80  THR   B HG23 1 
ATOM   3541 N  N    . LEU   B 1 78  ? 33.54013 7.39815   18.59229  1.000 12.86805 ?  81  LEU   B N    1 
ATOM   3542 C  CA   . LEU   B 1 78  ? 33.61700 8.85196   18.63416  1.000 13.24569 ?  81  LEU   B CA   1 
ATOM   3543 C  C    . LEU   B 1 78  ? 33.43562 9.36361   17.21416  1.000 13.59428 ?  81  LEU   B C    1 
ATOM   3544 O  O    . LEU   B 1 78  ? 34.22592 9.02202   16.32847  1.000 13.60311 ?  81  LEU   B O    1 
ATOM   3545 C  CB   . LEU   B 1 78  ? 34.96858 9.30146   19.18184  1.000 13.80827 ?  81  LEU   B CB   1 
ATOM   3546 C  CG   . LEU   B 1 78  ? 35.11467 10.79605  19.44348  1.000 14.69799 ?  81  LEU   B CG   1 
ATOM   3547 C  CD1  . LEU   B 1 78  ? 34.45766 11.21096  20.75057  1.000 16.02371 ?  81  LEU   B CD1  1 
ATOM   3548 C  CD2  . LEU   B 1 78  ? 36.58176 11.17884  19.41581  1.000 16.26999 ?  81  LEU   B CD2  1 
ATOM   3549 H  H    . LEU   B 1 78  ? 34.22177 7.03279   18.21614  1.000 15.44166 ?  81  LEU   B H    1 
ATOM   3550 H  HA   . LEU   B 1 78  ? 32.91669 9.21074   19.20138  1.000 15.89483 ?  81  LEU   B HA   1 
ATOM   3551 H  HB2  . LEU   B 1 78  ? 35.12126 8.84531   20.02416  1.000 16.56993 ?  81  LEU   B HB2  1 
ATOM   3552 H  HB3  . LEU   B 1 78  ? 35.65315 9.05294   18.54113  1.000 16.56993 ?  81  LEU   B HB3  1 
ATOM   3553 H  HG   . LEU   B 1 78  ? 34.65457 11.28409  18.74274  1.000 17.63758 ?  81  LEU   B HG   1 
ATOM   3554 H  HD11 . LEU   B 1 78  ? 34.37929 12.17756  20.77174  1.000 19.22845 ?  81  LEU   B HD11 1 
ATOM   3555 H  HD12 . LEU   B 1 78  ? 33.57763 10.80650  20.80400  1.000 19.22845 ?  81  LEU   B HD12 1 
ATOM   3556 H  HD13 . LEU   B 1 78  ? 35.00672 10.90733  21.49032  1.000 19.22845 ?  81  LEU   B HD13 1 
ATOM   3557 H  HD21 . LEU   B 1 78  ? 36.66678 12.11995  19.63484  1.000 19.52399 ?  81  LEU   B HD21 1 
ATOM   3558 H  HD22 . LEU   B 1 78  ? 37.06029 10.64299  20.06757  1.000 19.52399 ?  81  LEU   B HD22 1 
ATOM   3559 H  HD23 . LEU   B 1 78  ? 36.93479 11.01270  18.52774  1.000 19.52399 ?  81  LEU   B HD23 1 
ATOM   3560 N  N    . ILE   B 1 79  ? 32.38773 10.15415  16.99641  1.000 14.14938 ?  82  ILE   B N    1 
ATOM   3561 C  CA   . ILE   B 1 79  ? 32.06981 10.74637  15.69517  1.000 14.90333 ?  82  ILE   B CA   1 
ATOM   3562 C  C    . ILE   B 1 79  ? 31.99300 12.25039  15.88690  1.000 15.29576 ?  82  ILE   B C    1 
ATOM   3563 O  O    . ILE   B 1 79  ? 31.19420 12.74023  16.69742  1.000 16.57818 ?  82  ILE   B O    1 
ATOM   3564 C  CB   . ILE   B 1 79  ? 30.75781 10.21522  15.09589  1.000 15.60755 ?  82  ILE   B CB   1 
ATOM   3565 C  CG1  . ILE   B 1 79  ? 30.91840 8.75992   14.67157  1.000 17.32982 ?  82  ILE   B CG1  1 
ATOM   3566 C  CG2  . ILE   B 1 79  ? 30.37487 11.04431  13.87936  1.000 17.27912 ?  82  ILE   B CG2  1 
ATOM   3567 C  CD1  . ILE   B 1 79  ? 29.62224 8.03999   14.38176  1.000 18.11135 ?  82  ILE   B CD1  1 
ATOM   3568 H  H    . ILE   B 1 79  ? 31.82431 10.37108  17.60886  1.000 16.97926 ?  82  ILE   B H    1 
ATOM   3569 H  HA   . ILE   B 1 79  ? 32.78495 10.53422  15.07511  1.000 17.88399 ?  82  ILE   B HA   1 
ATOM   3570 H  HB   . ILE   B 1 79  ? 30.06619 10.27828  15.77308  1.000 18.72906 ?  82  ILE   B HB   1 
ATOM   3571 H  HG12 . ILE   B 1 79  ? 31.45494 8.73176   13.86397  1.000 20.79578 ?  82  ILE   B HG12 1 
ATOM   3572 H  HG13 . ILE   B 1 79  ? 31.36661 8.27866   15.38459  1.000 20.79578 ?  82  ILE   B HG13 1 
ATOM   3573 H  HG21 . ILE   B 1 79  ? 29.67212 10.58552  13.39300  1.000 20.73494 ?  82  ILE   B HG21 1 
ATOM   3574 H  HG22 . ILE   B 1 79  ? 30.05969 11.91259  14.17543  1.000 20.73494 ?  82  ILE   B HG22 1 
ATOM   3575 H  HG23 . ILE   B 1 79  ? 31.15433 11.15120  13.31197  1.000 20.73494 ?  82  ILE   B HG23 1 
ATOM   3576 H  HD11 . ILE   B 1 79  ? 29.81481 7.10999   14.18450  1.000 21.73362 ?  82  ILE   B HD11 1 
ATOM   3577 H  HD12 . ILE   B 1 79  ? 29.04643 8.10070   15.16000  1.000 21.73362 ?  82  ILE   B HD12 1 
ATOM   3578 H  HD13 . ILE   B 1 79  ? 29.19263 8.45781   13.61902  1.000 21.73362 ?  82  ILE   B HD13 1 
ATOM   3579 N  N    . ASN   B 1 80  ? 32.80418 12.98159  15.13271  1.000 17.20608 ?  83  ASN   B N    1 
ATOM   3580 C  CA   . ASN   B 1 80  ? 32.78225 14.44448  15.19868  1.000 18.44879 ?  83  ASN   B CA   1 
ATOM   3581 C  C    . ASN   B 1 80  ? 32.91182 14.91456  16.65018  1.000 17.57788 ?  83  ASN   B C    1 
ATOM   3582 O  O    . ASN   B 1 80  ? 32.21302 15.81468  17.11530  1.000 19.81058 ?  83  ASN   B O    1 
ATOM   3583 C  CB   . ASN   B 1 80  ? 31.53640 15.01818  14.51361  1.000 20.08098 ?  83  ASN   B CB   1 
ATOM   3584 C  CG   . ASN   B 1 80  ? 31.48085 14.67930  13.02409  1.000 21.02019 ?  83  ASN   B CG   1 
ATOM   3585 O  OD1  . ASN   B 1 80  ? 32.49963 14.35738  12.40805  1.000 22.76574 ?  83  ASN   B OD1  1 
ATOM   3586 N  ND2  . ASN   B 1 80  ? 30.29440 14.74766  12.44423  1.000 23.95980 ?  83  ASN   B ND2  1 
ATOM   3587 H  H    . ASN   B 1 80  ? 33.37502 12.65903  14.57621  1.000 20.64730 ?  83  ASN   B H    1 
ATOM   3588 H  HA   . ASN   B 1 80  ? 33.54669 14.79295  14.71380  1.000 22.13855 ?  83  ASN   B HA   1 
ATOM   3589 H  HB2  . ASN   B 1 80  ? 30.74439 14.65038  14.93593  1.000 24.09718 ?  83  ASN   B HB2  1 
ATOM   3590 H  HB3  . ASN   B 1 80  ? 31.54172 15.98406  14.60278  1.000 24.09718 ?  83  ASN   B HB3  1 
ATOM   3591 H  HD21 . ASN   B 1 80  ? 29.60359 14.97393  12.90378  1.000 28.75176 ?  83  ASN   B HD21 1 
ATOM   3592 H  HD22 . ASN   B 1 80  ? 30.21358 14.56584  11.60756  1.000 28.75176 ?  83  ASN   B HD22 1 
ATOM   3593 N  N    . GLU   B 1 81  ? 33.81494 14.27139  17.38069  1.000 17.13847 ?  84  GLU   B N    1 
ATOM   3594 C  CA   . GLU   B 1 81  ? 34.16214 14.62356  18.75493  1.000 18.70031 ?  84  GLU   B CA   1 
ATOM   3595 C  C    . GLU   B 1 81  ? 33.05785 14.34466  19.77141  1.000 18.73480 ?  84  GLU   B C    1 
ATOM   3596 O  O    . GLU   B 1 81  ? 33.10524 14.87662  20.88374  1.000 21.38859 ?  84  GLU   B O    1 
ATOM   3597 C  CB   . GLU   B 1 81  ? 34.68034 16.06185  18.86757  1.000 20.82799 ?  84  GLU   B CB   1 
ATOM   3598 C  CG   . GLU   B 1 81  ? 35.90087 16.30041  17.99636  1.000 23.36977 ?  84  GLU   B CG   1 
ATOM   3599 C  CD   . GLU   B 1 81  ? 36.55255 17.63959  18.24801  1.000 26.64874 ?  84  GLU   B CD   1 
ATOM   3600 O  OE1  . GLU   B 1 81  ? 35.87614 18.67245  18.04904  1.000 30.52183 ?  84  GLU   B OE1  1 
ATOM   3601 O  OE2  . GLU   B 1 81  ? 37.73154 17.65933  18.65969  1.000 25.30914 ?  84  GLU   B OE2  1 
ATOM   3602 H  H    . GLU   B 1 81  ? 34.26079 13.59627  17.08908  1.000 20.56617 ?  84  GLU   B H    1 
ATOM   3603 H  HA   . GLU   B 1 81  ? 34.89355 14.04223  19.01565  1.000 22.44037 ?  84  GLU   B HA   1 
ATOM   3604 H  HB2  . GLU   B 1 81  ? 33.98274 16.67418  18.58597  1.000 24.99359 ?  84  GLU   B HB2  1 
ATOM   3605 H  HB3  . GLU   B 1 81  ? 34.92618 16.24006  19.78882  1.000 24.99359 ?  84  GLU   B HB3  1 
ATOM   3606 H  HG2  . GLU   B 1 81  ? 36.55736 15.60970  18.17756  1.000 28.04373 ?  84  GLU   B HG2  1 
ATOM   3607 H  HG3  . GLU   B 1 81  ? 35.63404 16.26820  17.06434  1.000 28.04373 ?  84  GLU   B HG3  1 
ATOM   3608 N  N    . LYS   B 1 82  ? 32.08004 13.49621  19.44381  1.000 17.34368 ?  85  LYS   B N    1 
ATOM   3609 C  CA   . LYS   B 1 82  ? 31.00962 13.12004  20.36376  1.000 18.68482 ?  85  LYS   B CA   1 
ATOM   3610 C  C    . LYS   B 1 82  ? 30.93690 11.60214  20.49683  1.000 16.47266 ?  85  LYS   B C    1 
ATOM   3611 O  O    . LYS   B 1 82  ? 30.95479 10.87782  19.49083  1.000 15.95070 ?  85  LYS   B O    1 
ATOM   3612 C  CB   . LYS   B 1 82  ? 29.65474 13.63371  19.87363  1.000 20.84737 ?  85  LYS   B CB   1 
ATOM   3613 C  CG   . LYS   B 1 82  ? 29.60825 15.16060  19.70140  1.000 27.72830 ?  85  LYS   B CG   1 
ATOM   3614 C  CD   . LYS   B 1 82  ? 28.20111 15.68328  19.42304  1.000 34.43905 ?  85  LYS   B CD   1 
ATOM   3615 C  CE   . LYS   B 1 82  ? 27.59731 15.10920  18.14177  1.000 39.61233 ?  85  LYS   B CE   1 
ATOM   3616 N  NZ   . LYS   B 1 82  ? 26.32689 14.35128  18.41354  1.000 42.91174 ?  85  LYS   B NZ   1 
ATOM   3617 H  H    . LYS   B 1 82  ? 32.01581 13.11725  18.67448  1.000 20.81242 ?  85  LYS   B H    1 
ATOM   3618 H  HA   . LYS   B 1 82  ? 31.20965 13.49870  21.23410  1.000 22.42178 ?  85  LYS   B HA   1 
ATOM   3619 H  HB2  . LYS   B 1 82  ? 29.45943 13.23078  19.01316  1.000 25.01685 ?  85  LYS   B HB2  1 
ATOM   3620 H  HB3  . LYS   B 1 82  ? 28.97370 13.38576  20.51831  1.000 25.01685 ?  85  LYS   B HB3  1 
ATOM   3621 H  HG2  . LYS   B 1 82  ? 29.92769 15.58043  20.51541  1.000 33.27396 ?  85  LYS   B HG2  1 
ATOM   3622 H  HG3  . LYS   B 1 82  ? 30.17386 15.41186  18.95451  1.000 33.27396 ?  85  LYS   B HG3  1 
ATOM   3623 H  HD2  . LYS   B 1 82  ? 27.62162 15.44003  20.16190  1.000 41.32686 ?  85  LYS   B HD2  1 
ATOM   3624 H  HD3  . LYS   B 1 82  ? 28.23471 16.64837  19.33158  1.000 41.32686 ?  85  LYS   B HD3  1 
ATOM   3625 H  HE2  . LYS   B 1 82  ? 27.39342 15.83477  17.53113  1.000 47.53480 ?  85  LYS   B HE2  1 
ATOM   3626 H  HE3  . LYS   B 1 82  ? 28.23268 14.50055  17.73342  1.000 47.53480 ?  85  LYS   B HE3  1 
ATOM   3627 H  HZ1  . LYS   B 1 82  ? 26.00674 14.01205  17.65556  1.000 51.49409 ?  85  LYS   B HZ1  1 
ATOM   3628 H  HZ2  . LYS   B 1 82  ? 26.48516 13.68627  18.98346  1.000 51.49409 ?  85  LYS   B HZ2  1 
ATOM   3629 H  HZ3  . LYS   B 1 82  ? 25.71743 14.89536  18.76659  1.000 51.49409 ?  85  LYS   B HZ3  1 
ATOM   3630 N  N    . TRP   B 1 83  ? 30.84573 11.11837  21.73303  1.000 16.33937 ?  86  TRP   B N    1 
ATOM   3631 C  CA   . TRP   B 1 83  ? 30.70206 9.69045   21.98252  1.000 15.84952 ?  86  TRP   B CA   1 
ATOM   3632 C  C    . TRP   B 1 83  ? 29.26086 9.26542   21.75584  1.000 16.56215 ?  86  TRP   B C    1 
ATOM   3633 O  O    . TRP   B 1 83  ? 28.33795 10.01353  22.06117  1.000 18.75983 ?  86  TRP   B O    1 
ATOM   3634 C  CB   . TRP   B 1 83  ? 31.11351 9.36528   23.42026  1.000 16.74166 ?  86  TRP   B CB   1 
ATOM   3635 C  CG   . TRP   B 1 83  ? 32.58327 9.49859   23.64886  1.000 16.67938 ?  86  TRP   B CG   1 
ATOM   3636 C  CD1  . TRP   B 1 83  ? 33.22631 10.47932  24.34623  1.000 18.56228 ?  86  TRP   B CD1  1 
ATOM   3637 C  CD2  . TRP   B 1 83  ? 33.60120 8.60995   23.17761  1.000 15.93212 ?  86  TRP   B CD2  1 
ATOM   3638 N  NE1  . TRP   B 1 83  ? 34.58695 10.25145  24.33362  1.000 18.29695 ?  86  TRP   B NE1  1 
ATOM   3639 C  CE2  . TRP   B 1 83  ? 34.84112 9.11523   23.61396  1.000 16.72625 ?  86  TRP   B CE2  1 
ATOM   3640 C  CE3  . TRP   B 1 83  ? 33.58433 7.44272   22.42638  1.000 15.06069 ?  86  TRP   B CE3  1 
ATOM   3641 C  CZ2  . TRP   B 1 83  ? 36.05844 8.49507   23.31096  1.000 16.11390 ?  86  TRP   B CZ2  1 
ATOM   3642 C  CZ3  . TRP   B 1 83  ? 34.79799 6.81783   22.12682  1.000 15.42380 ?  86  TRP   B CZ3  1 
ATOM   3643 C  CH2  . TRP   B 1 83  ? 36.01461 7.34135   22.57407  1.000 15.42294 ?  86  TRP   B CH2  1 
ATOM   3644 H  H    . TRP   B 1 83  ? 30.86471 11.59923  22.44577  1.000 19.60725 ?  86  TRP   B H    1 
ATOM   3645 H  HA   . TRP   B 1 83  ? 31.27302 9.19162   21.37748  1.000 19.01942 ?  86  TRP   B HA   1 
ATOM   3646 H  HB2  . TRP   B 1 83  ? 30.66005 9.97481   24.02338  1.000 20.08999 ?  86  TRP   B HB2  1 
ATOM   3647 H  HB3  . TRP   B 1 83  ? 30.86085 8.45057   23.62118  1.000 20.08999 ?  86  TRP   B HB3  1 
ATOM   3648 H  HD1  . TRP   B 1 83  ? 32.80905 11.19561  24.76780  1.000 22.27473 ?  86  TRP   B HD1  1 
ATOM   3649 H  HE1  . TRP   B 1 83  ? 35.17950 10.74364  24.71603  1.000 21.95634 ?  86  TRP   B HE1  1 
ATOM   3650 H  HE3  . TRP   B 1 83  ? 32.78023 7.08320   22.12794  1.000 18.07282 ?  86  TRP   B HE3  1 
ATOM   3651 H  HZ2  . TRP   B 1 83  ? 36.86700 8.85292   23.59917  1.000 19.33668 ?  86  TRP   B HZ2  1 
ATOM   3652 H  HZ3  . TRP   B 1 83  ? 34.79621 6.03817   21.61984  1.000 18.50856 ?  86  TRP   B HZ3  1 
ATOM   3653 H  HH2  . TRP   B 1 83  ? 36.80652 6.89939   22.36806  1.000 18.50753 ?  86  TRP   B HH2  1 
ATOM   3654 N  N    . GLY   B 1 84  ? 29.07332 8.06172   21.21700  1.000 15.33027 ?  87  GLY   B N    1 
ATOM   3655 C  CA   . GLY   B 1 84  ? 27.76421 7.46882   21.07495  1.000 15.83096 ?  87  GLY   B CA   1 
ATOM   3656 C  C    . GLY   B 1 84  ? 27.35084 6.71872   22.31920  1.000 14.91895 ?  87  GLY   B C    1 
ATOM   3657 O  O    . GLY   B 1 84  ? 27.79996 6.99898   23.43052  1.000 16.25043 ?  87  GLY   B O    1 
ATOM   3658 H  H    . GLY   B 1 84  ? 29.70981 7.56431   20.92194  1.000 18.39632 ?  87  GLY   B H    1 
ATOM   3659 H  HA2  . GLY   B 1 84  ? 27.11082 8.16487   20.90321  1.000 18.99715 ?  87  GLY   B HA2  1 
ATOM   3660 H  HA3  . GLY   B 1 84  ? 27.76906 6.84915   20.32871  1.000 18.99715 ?  87  GLY   B HA3  1 
ATOM   3661 N  N    . ARG   B 1 85  ? 26.46389 5.75132   22.11282  1.000 15.82621 ?  88  ARG   B N    1 
ATOM   3662 C  CA   . ARG   B 1 85  ? 25.97482 4.91774   23.20585  1.000 16.24409 ?  88  ARG   B CA   1 
ATOM   3663 C  C    . ARG   B 1 85  ? 27.07784 3.97887   23.68339  1.000 15.79082 ?  88  ARG   B C    1 
ATOM   3664 O  O    . ARG   B 1 85  ? 27.69132 3.26912   22.88227  1.000 16.82389 ?  88  ARG   B O    1 
ATOM   3665 C  CB   . ARG   B 1 85  ? 24.80665 4.08405   22.68488  1.000 19.82787 ?  88  ARG   B CB   1 
ATOM   3666 C  CG   . ARG   B 1 85  ? 24.25205 3.07034   23.65382  1.000 26.09292 ?  88  ARG   B CG   1 
ATOM   3667 C  CD   . ARG   B 1 85  ? 23.39366 3.71109   24.69367  1.000 31.32339 ?  88  ARG   B CD   1 
ATOM   3668 N  NE   . ARG   B 1 85  ? 22.63833 2.69784   25.42384  1.000 35.49624 ?  88  ARG   B NE   1 
ATOM   3669 C  CZ   . ARG   B 1 85  ? 22.25079 2.79860   26.68914  1.000 38.46361 ?  88  ARG   B CZ   1 
ATOM   3670 N  NH1  . ARG   B 1 85  ? 22.52140 3.87504   27.41841  1.000 39.18276 ?  88  ARG   B NH1  1 
ATOM   3671 N  NH2  . ARG   B 1 85  ? 21.57513 1.79366   27.23829  1.000 38.60294 ?  88  ARG   B NH2  1 
ATOM   3672 H  H    . ARG   B 1 85  ? 26.12741 5.55556   21.34597  1.000 18.99145 ?  88  ARG   B H    1 
ATOM   3673 H  HA   . ARG   B 1 85  ? 25.69199 5.47084   23.95082  1.000 19.49291 ?  88  ARG   B HA   1 
ATOM   3674 H  HB2  . ARG   B 1 85  ? 24.08287 4.68569   22.45021  1.000 23.79345 ?  88  ARG   B HB2  1 
ATOM   3675 H  HB3  . ARG   B 1 85  ? 25.10376 3.59991   21.89860  1.000 23.79345 ?  88  ARG   B HB3  1 
ATOM   3676 H  HG2  . ARG   B 1 85  ? 23.71262 2.42590   23.16945  1.000 31.31150 ?  88  ARG   B HG2  1 
ATOM   3677 H  HG3  . ARG   B 1 85  ? 24.98556 2.61973   24.10083  1.000 31.31150 ?  88  ARG   B HG3  1 
ATOM   3678 H  HD2  . ARG   B 1 85  ? 23.95117 4.19514   25.32278  1.000 37.58806 ?  88  ARG   B HD2  1 
ATOM   3679 H  HD3  . ARG   B 1 85  ? 22.76752 4.31857   24.26962  1.000 37.58806 ?  88  ARG   B HD3  1 
ATOM   3680 H  HE   . ARG   B 1 85  ? 22.42789 1.97916   25.00098  1.000 42.59549 ?  88  ARG   B HE   1 
ATOM   3681 H  HH11 . ARG   B 1 85  ? 22.95839 4.53003   27.07253  1.000 47.01931 ?  88  ARG   B HH11 1 
ATOM   3682 H  HH12 . ARG   B 1 85  ? 22.25963 3.91711   28.23652  1.000 47.01931 ?  88  ARG   B HH12 1 
ATOM   3683 H  HH21 . ARG   B 1 85  ? 21.39552 1.09205   26.77452  1.000 46.32353 ?  88  ARG   B HH21 1 
ATOM   3684 H  HH22 . ARG   B 1 85  ? 21.31773 1.84530   28.05724  1.000 46.32353 ?  88  ARG   B HH22 1 
ATOM   3685 N  N    . GLU   B 1 86  ? 27.30280 3.93162   24.99403  1.000 16.04583 ?  89  GLU   B N    1 
ATOM   3686 C  CA   . GLU   B 1 86  ? 28.23737 2.96234   25.54609  1.000 16.45910 ?  89  GLU   B CA   1 
ATOM   3687 C  C    . GLU   B 1 86  ? 27.65773 1.55775   25.45861  1.000 16.91687 ?  89  GLU   B C    1 
ATOM   3688 O  O    . GLU   B 1 86  ? 26.48635 1.32870   25.78471  1.000 19.73409 ?  89  GLU   B O    1 
ATOM   3689 C  CB   . GLU   B 1 86  ? 28.53298 3.29294   27.01245  1.000 17.92449 ?  89  GLU   B CB   1 
ATOM   3690 C  CG   . GLU   B 1 86  ? 29.27932 4.57664   27.16596  1.000 19.03776 ?  89  GLU   B CG   1 
ATOM   3691 C  CD   . GLU   B 1 86  ? 29.75560 4.85988   28.56749  1.000 18.31345 ?  89  GLU   B CD   1 
ATOM   3692 O  OE1  . GLU   B 1 86  ? 29.02586 4.57780   29.54945  1.000 21.73583 ?  89  GLU   B OE1  1 
ATOM   3693 O  OE2  . GLU   B 1 86  ? 30.86585 5.41997   28.67926  1.000 18.12502 ?  89  GLU   B OE2  1 
ATOM   3694 H  H    . GLU   B 1 86  ? 26.93084 4.44405   25.57597  1.000 19.25500 ?  89  GLU   B H    1 
ATOM   3695 H  HA   . GLU   B 1 86  ? 29.06601 2.99328   25.04281  1.000 19.75092 ?  89  GLU   B HA   1 
ATOM   3696 H  HB2  . GLU   B 1 86  ? 27.69521 3.37104   27.49509  1.000 21.50939 ?  89  GLU   B HB2  1 
ATOM   3697 H  HB3  . GLU   B 1 86  ? 29.07149 2.58281   27.39535  1.000 21.50939 ?  89  GLU   B HB3  1 
ATOM   3698 H  HG2  . GLU   B 1 86  ? 30.06040 4.55084   26.59137  1.000 22.84531 ?  89  GLU   B HG2  1 
ATOM   3699 H  HG3  . GLU   B 1 86  ? 28.69720 5.30626   26.90196  1.000 22.84531 ?  89  GLU   B HG3  1 
ATOM   3700 N  N    . GLU   B 1 87  ? 28.50044 0.60536   25.06304  1.000 15.34052 ?  90  GLU   B N    1 
ATOM   3701 C  CA   . GLU   B 1 87  ? 28.17098 -0.81374  25.13919  1.000 14.84884 ?  90  GLU   B CA   1 
ATOM   3702 C  C    . GLU   B 1 87  ? 29.08775 -1.39352  26.20526  1.000 15.90649 ?  90  GLU   B C    1 
ATOM   3703 O  O    . GLU   B 1 87  ? 30.30536 -1.47517  26.01035  1.000 15.96546 ?  90  GLU   B O    1 
ATOM   3704 C  CB   . GLU   B 1 87  ? 28.34892 -1.48534  23.78056  1.000 15.46955 ?  90  GLU   B CB   1 
ATOM   3705 C  CG   . GLU   B 1 87  ? 27.49380 -0.84660  22.69761  1.000 16.29019 ?  90  GLU   B CG   1 
ATOM   3706 C  CD   . GLU   B 1 87  ? 27.50679 -1.59350  21.38400  1.000 16.38442 ?  90  GLU   B CD   1 
ATOM   3707 O  OE1  . GLU   B 1 87  ? 27.80151 -2.80994  21.34316  1.000 17.73271 ?  90  GLU   B OE1  1 
ATOM   3708 O  OE2  . GLU   B 1 87  ? 27.20530 -0.96044  20.34496  1.000 17.75841 ?  90  GLU   B OE2  1 
ATOM   3709 H  H    . GLU   B 1 87  ? 29.28264 0.76139   24.74144  1.000 18.40862 ?  90  GLU   B H    1 
ATOM   3710 H  HA   . GLU   B 1 87  ? 27.24771 -0.95571  25.40055  1.000 17.81860 ?  90  GLU   B HA   1 
ATOM   3711 H  HB2  . GLU   B 1 87  ? 29.27819 -1.41417  23.51170  1.000 18.56346 ?  90  GLU   B HB2  1 
ATOM   3712 H  HB3  . GLU   B 1 87  ? 28.09516 -2.41873  23.85334  1.000 18.56346 ?  90  GLU   B HB3  1 
ATOM   3713 H  HG2  . GLU   B 1 87  ? 26.57519 -0.81065  23.00706  1.000 19.54823 ?  90  GLU   B HG2  1 
ATOM   3714 H  HG3  . GLU   B 1 87  ? 27.82271 0.05037   22.52983  1.000 19.54823 ?  90  GLU   B HG3  1 
ATOM   3715 N  N    . ILE   B 1 88  ? 28.51459 -1.78050  27.34009  1.000 16.80352 ?  91  ILE   B N    1 
ATOM   3716 C  CA   . ILE   B 1 88  ? 29.29057 -2.16536  28.51290  1.000 16.99290 ?  91  ILE   B CA   1 
ATOM   3717 C  C    . ILE   B 1 88  ? 29.22654 -3.68145  28.65894  1.000 17.84456 ?  91  ILE   B C    1 
ATOM   3718 O  O    . ILE   B 1 88  ? 28.14002 -4.26019  28.76727  1.000 19.85017 ?  91  ILE   B O    1 
ATOM   3719 C  CB   . ILE   B 1 88  ? 28.79934 -1.45157  29.78071  1.000 18.97842 ?  91  ILE   B CB   1 
ATOM   3720 C  CG1  . ILE   B 1 88  ? 28.73261 0.06827   29.58732  1.000 20.86705 ?  91  ILE   B CG1  1 
ATOM   3721 C  CG2  . ILE   B 1 88  ? 29.72091 -1.78471  30.94318  1.000 21.30188 ?  91  ILE   B CG2  1 
ATOM   3722 C  CD1  . ILE   B 1 88  ? 28.01719 0.80359   30.72150  1.000 24.08385 ?  91  ILE   B CD1  1 
ATOM   3723 H  H    . ILE   B 1 88  ? 27.66379 -1.82871  27.45589  1.000 20.16422 ?  91  ILE   B H    1 
ATOM   3724 H  HA   . ILE   B 1 88  ? 30.21917 -1.92291  28.37214  1.000 20.39148 ?  91  ILE   B HA   1 
ATOM   3725 H  HB   . ILE   B 1 88  ? 27.90080 -1.76516  29.96827  1.000 22.77411 ?  91  ILE   B HB   1 
ATOM   3726 H  HG12 . ILE   B 1 88  ? 29.63665 0.41567   29.53332  1.000 25.04046 ?  91  ILE   B HG12 1 
ATOM   3727 H  HG13 . ILE   B 1 88  ? 28.25491 0.25717   28.76450  1.000 25.04046 ?  91  ILE   B HG13 1 
ATOM   3728 H  HG21 . ILE   B 1 88  ? 29.46453 -1.25195  31.71216  1.000 25.56226 ?  91  ILE   B HG21 1 
ATOM   3729 H  HG22 . ILE   B 1 88  ? 29.63755 -2.72832  31.15188  1.000 25.56226 ?  91  ILE   B HG22 1 
ATOM   3730 H  HG23 . ILE   B 1 88  ? 30.63493 -1.58146  30.68986  1.000 25.56226 ?  91  ILE   B HG23 1 
ATOM   3731 H  HD11 . ILE   B 1 88  ? 27.95523 1.74537   30.49767  1.000 28.90062 ?  91  ILE   B HD11 1 
ATOM   3732 H  HD12 . ILE   B 1 88  ? 27.12850 0.42998   30.82898  1.000 28.90062 ?  91  ILE   B HD12 1 
ATOM   3733 H  HD13 . ILE   B 1 88  ? 28.52464 0.69092   31.54046  1.000 28.90062 ?  91  ILE   B HD13 1 
ATOM   3734 N  N    . THR   B 1 89  ? 30.39209 -4.31808  28.64877  1.000 16.43176 ?  92  THR   B N    1 
ATOM   3735 C  CA   . THR   B 1 89  ? 30.53761 -5.75415  28.86993  1.000 17.79079 ?  92  THR   B CA   1 
ATOM   3736 C  C    . THR   B 1 89  ? 31.05256 -5.95904  30.28714  1.000 17.75919 ?  92  THR   B C    1 
ATOM   3737 O  O    . THR   B 1 89  ? 32.14786 -5.51355  30.62988  1.000 18.76551 ?  92  THR   B O    1 
ATOM   3738 C  CB   . THR   B 1 89  ? 31.49315 -6.34431  27.82584  1.000 18.49245 ?  92  THR   B CB   1 
ATOM   3739 O  OG1  . THR   B 1 89  ? 30.87446 -6.26748  26.53295  1.000 19.83442 ?  92  THR   B OG1  1 
ATOM   3740 C  CG2  . THR   B 1 89  ? 31.84796 -7.80789  28.10624  1.000 20.82878 ?  92  THR   B CG2  1 
ATOM   3741 H  H    . THR   B 1 89  ? 31.14416 -3.92460  28.51035  1.000 19.71811 ?  92  THR   B H    1 
ATOM   3742 H  HA   . THR   B 1 89  ? 29.68669 -6.21283  28.78965  1.000 21.34895 ?  92  THR   B HA   1 
ATOM   3743 H  HB   . THR   B 1 89  ? 32.31980 -5.83751  27.85270  1.000 22.19094 ?  92  THR   B HB   1 
ATOM   3744 H  HG1  . THR   B 1 89  ? 31.35296 -6.65554  25.96195  1.000 23.80130 ?  92  THR   B HG1  1 
ATOM   3745 H  HG21 . THR   B 1 89  ? 32.31584 -8.18735  27.34598  1.000 24.99453 ?  92  THR   B HG21 1 
ATOM   3746 H  HG22 . THR   B 1 89  ? 32.41850 -7.86695  28.88848  1.000 24.99453 ?  92  THR   B HG22 1 
ATOM   3747 H  HG23 . THR   B 1 89  ? 31.04007 -8.32028  28.26644  1.000 24.99453 ?  92  THR   B HG23 1 
ATOM   3748 N  N    . TYR   B 1 90  ? 30.23549 -6.58817  31.12191  1.000 19.38809 ?  93  TYR   B N    1 
ATOM   3749 C  CA   . TYR   B 1 90  ? 30.60107 -6.82271  32.50982  1.000 20.10675 ?  93  TYR   B CA   1 
ATOM   3750 C  C    . TYR   B 1 90  ? 31.33650 -8.14073  32.71147  1.000 20.93838 ?  93  TYR   B C    1 
ATOM   3751 O  O    . TYR   B 1 90  ? 32.00389 -8.31118  33.73958  1.000 23.20381 ?  93  TYR   B O    1 
ATOM   3752 C  CB   . TYR   B 1 90  ? 29.35647 -6.75734  33.40265  1.000 21.35883 ?  93  TYR   B CB   1 
ATOM   3753 C  CG   . TYR   B 1 90  ? 28.86481 -5.33234  33.58070  1.000 22.06613 ?  93  TYR   B CG   1 
ATOM   3754 C  CD1  . TYR   B 1 90  ? 29.55053 -4.44423  34.40557  1.000 23.95398 ?  93  TYR   B CD1  1 
ATOM   3755 C  CD2  . TYR   B 1 90  ? 27.73734 -4.86830  32.91053  1.000 24.31593 ?  93  TYR   B CD2  1 
ATOM   3756 C  CE1  . TYR   B 1 90  ? 29.11661 -3.15317  34.57860  1.000 25.59728 ?  93  TYR   B CE1  1 
ATOM   3757 C  CE2  . TYR   B 1 90  ? 27.30020 -3.55518  33.06771  1.000 24.32898 ?  93  TYR   B CE2  1 
ATOM   3758 C  CZ   . TYR   B 1 90  ? 27.99386 -2.70941  33.91428  1.000 26.31806 ?  93  TYR   B CZ   1 
ATOM   3759 O  OH   . TYR   B 1 90  ? 27.57304 -1.40575  34.09525  1.000 28.28605 ?  93  TYR   B OH   1 
ATOM   3760 H  H    . TYR   B 1 90  ? 29.45959 -6.89034  30.90681  1.000 23.26571 ?  93  TYR   B H    1 
ATOM   3761 H  HA   . TYR   B 1 90  ? 31.19662 -6.11744  32.80782  1.000 24.12811 ?  93  TYR   B HA   1 
ATOM   3762 H  HB2  . TYR   B 1 90  ? 28.64463 -7.27647  32.99682  1.000 25.63059 ?  93  TYR   B HB2  1 
ATOM   3763 H  HB3  . TYR   B 1 90  ? 29.57177 -7.11662  34.27756  1.000 25.63059 ?  93  TYR   B HB3  1 
ATOM   3764 H  HD1  . TYR   B 1 90  ? 30.31685 -4.73108  34.84757  1.000 28.74477 ?  93  TYR   B HD1  1 
ATOM   3765 H  HD2  . TYR   B 1 90  ? 27.26875 -5.44321  32.34946  1.000 29.17912 ?  93  TYR   B HD2  1 
ATOM   3766 H  HE1  . TYR   B 1 90  ? 29.58025 -2.57840  35.14391  1.000 30.71674 ?  93  TYR   B HE1  1 
ATOM   3767 H  HE2  . TYR   B 1 90  ? 26.55077 -3.25068  32.60886  1.000 29.19478 ?  93  TYR   B HE2  1 
ATOM   3768 H  HH   . TYR   B 1 90  ? 26.86772 -1.26851  33.66018  1.000 33.94326 ?  93  TYR   B HH   1 
ATOM   3769 N  N    . ASP   B 1 91  ? 31.25706 -9.06076  31.74933  1.000 21.59438 ?  94  ASP   B N    1 
ATOM   3770 C  CA   . ASP   B 1 91  ? 32.01681 -10.31089 31.80501  1.000 22.24631 ?  94  ASP   B CA   1 
ATOM   3771 C  C    . ASP   B 1 91  ? 33.36384 -10.02422 31.15727  1.000 20.24346 ?  94  ASP   B C    1 
ATOM   3772 O  O    . ASP   B 1 91  ? 33.51721 -10.06779 29.93435  1.000 23.92249 ?  94  ASP   B O    1 
ATOM   3773 C  CB   . ASP   B 1 91  ? 31.28541 -11.43586 31.08318  1.000 24.87158 ?  94  ASP   B CB   1 
ATOM   3774 C  CG   . ASP   B 1 91  ? 30.04256 -11.88542 31.80585  1.000 30.69071 ?  94  ASP   B CG   1 
ATOM   3775 O  OD1  . ASP   B 1 91  ? 30.05677 -11.95679 33.05005  1.000 31.85919 ?  94  ASP   B OD1  1 
ATOM   3776 O  OD2  . ASP   B 1 91  ? 29.04551 -12.17872 31.11917  1.000 34.61628 ?  94  ASP   B OD2  1 
ATOM   3777 H  H    . ASP   B 1 91  ? 30.76566 -8.98341  31.04780  1.000 25.91325 ?  94  ASP   B H    1 
ATOM   3778 H  HA   . ASP   B 1 91  ? 32.13975 -10.58161 32.72832  1.000 26.69557 ?  94  ASP   B HA   1 
ATOM   3779 H  HB2  . ASP   B 1 91  ? 31.02396 -11.12749 30.20145  1.000 29.84590 ?  94  ASP   B HB2  1 
ATOM   3780 H  HB3  . ASP   B 1 91  ? 31.87895 -12.19910 31.00523  1.000 29.84590 ?  94  ASP   B HB3  1 
ATOM   3781 N  N    . THR   B 1 92  ? 34.33353 -9.66587  31.98028  1.000 19.84828 ?  95  THR   B N    1 
ATOM   3782 C  CA   . THR   B 1 92  ? 35.61856 -9.23147  31.48905  1.000 19.25771 ?  95  THR   B CA   1 
ATOM   3783 C  C    . THR   B 1 92  ? 36.71242 -10.20872 31.85349  1.000 21.19150 ?  95  THR   B C    1 
ATOM   3784 O  O    . THR   B 1 92  ? 36.78595 -10.66230 33.00916  1.000 22.19999 ?  95  THR   B O    1 
ATOM   3785 C  CB   . THR   B 1 92  ? 36.00290 -7.83599  31.99542  1.000 19.05069 ?  95  THR   B CB   1 
ATOM   3786 O  OG1  . THR   B 1 92  ? 37.35249 -7.57006  31.57566  1.000 18.60374 ?  95  THR   B OG1  1 
ATOM   3787 C  CG2  . THR   B 1 92  ? 35.88283 -7.69813  33.50137  1.000 20.41606 ?  95  THR   B CG2  1 
ATOM   3788 H  H    . THR   B 1 92  ? 34.26665 -9.66719  32.83767  1.000 23.81793 ?  95  THR   B H    1 
ATOM   3789 H  HA   . THR   B 1 92  ? 35.54651 -9.18976  30.52263  1.000 23.10925 ?  95  THR   B HA   1 
ATOM   3790 H  HB   . THR   B 1 92  ? 35.39052 -7.18037  31.62657  1.000 22.86083 ?  95  THR   B HB   1 
ATOM   3791 H  HG1  . THR   B 1 92  ? 37.56595 -6.78283  31.77639  1.000 22.32448 ?  95  THR   B HG1  1 
ATOM   3792 H  HG21 . THR   B 1 92  ? 36.16482 -6.81187  33.77692  1.000 24.49927 ?  95  THR   B HG21 1 
ATOM   3793 H  HG22 . THR   B 1 92  ? 34.96220 -7.83471  33.77466  1.000 24.49927 ?  95  THR   B HG22 1 
ATOM   3794 H  HG23 . THR   B 1 92  ? 36.44269 -8.35736  33.94055  1.000 24.49927 ?  95  THR   B HG23 1 
ATOM   3795 N  N    . PRO   B 1 93  ? 37.56888 -10.54466 30.88162  1.000 21.51760 ?  96  PRO   B N    1 
ATOM   3796 C  CA   . PRO   B 1 93  ? 38.70214 -11.43034 31.14608  1.000 22.91452 ?  96  PRO   B CA   1 
ATOM   3797 C  C    . PRO   B 1 93  ? 39.92205 -10.72927 31.71967  1.000 23.42827 ?  96  PRO   B C    1 
ATOM   3798 O  O    . PRO   B 1 93  ? 40.86700 -11.42801 32.09824  1.000 26.67417 ?  96  PRO   B O    1 
ATOM   3799 C  CB   . PRO   B 1 93  ? 39.01663 -11.99165 29.74843  1.000 23.91519 ?  96  PRO   B CB   1 
ATOM   3800 C  CG   . PRO   B 1 93  ? 38.66716 -10.85720 28.82407  1.000 24.20956 ?  96  PRO   B CG   1 
ATOM   3801 C  CD   . PRO   B 1 93  ? 37.46726 -10.19985 29.44386  1.000 22.81662 ?  96  PRO   B CD   1 
ATOM   3802 H  HA   . PRO   B 1 93  ? 38.43635 -12.14814 31.74192  1.000 27.49743 ?  96  PRO   B HA   1 
ATOM   3803 H  HB2  . PRO   B 1 93  ? 39.95652 -12.22240 29.68303  1.000 28.69822 ?  96  PRO   B HB2  1 
ATOM   3804 H  HB3  . PRO   B 1 93  ? 38.47003 -12.77276 29.56957  1.000 28.69822 ?  96  PRO   B HB3  1 
ATOM   3805 H  HG2  . PRO   B 1 93  ? 39.41075 -10.23691 28.76735  1.000 29.05147 ?  96  PRO   B HG2  1 
ATOM   3806 H  HG3  . PRO   B 1 93  ? 38.45561 -11.20297 27.94283  1.000 29.05147 ?  96  PRO   B HG3  1 
ATOM   3807 H  HD2  . PRO   B 1 93  ? 37.50136 -9.23848  29.31935  1.000 27.37994 ?  96  PRO   B HD2  1 
ATOM   3808 H  HD3  . PRO   B 1 93  ? 36.64834 -10.55474 29.06396  1.000 27.37994 ?  96  PRO   B HD3  1 
ATOM   3809 N  N    . PHE   B 1 94  ? 39.96456 -9.39374  31.77420  1.000 21.00455 ?  97  PHE   B N    1 
ATOM   3810 C  CA   . PHE   B 1 94  ? 41.17915 -8.68753  32.15682  1.000 20.19058 ?  97  PHE   B CA   1 
ATOM   3811 C  C    . PHE   B 1 94  ? 41.30807 -8.58009  33.67219  1.000 21.92646 ?  97  PHE   B C    1 
ATOM   3812 O  O    . PHE   B 1 94  ? 40.31578 -8.47019  34.39113  1.000 22.99023 ?  97  PHE   B O    1 
ATOM   3813 C  CB   . PHE   B 1 94  ? 41.18746 -7.26817  31.56010  1.000 18.88382 ?  97  PHE   B CB   1 
ATOM   3814 C  CG   . PHE   B 1 94  ? 41.22485 -7.23729  30.05765  1.000 17.26548 ?  97  PHE   B CG   1 
ATOM   3815 C  CD1  . PHE   B 1 94  ? 42.41474 -7.44970  29.37962  1.000 18.14911 ?  97  PHE   B CD1  1 
ATOM   3816 C  CD2  . PHE   B 1 94  ? 40.07754 -7.02464  29.33461  1.000 15.63081 ?  97  PHE   B CD2  1 
ATOM   3817 C  CE1  . PHE   B 1 94  ? 42.45148 -7.44611  27.99339  1.000 18.08475 ?  97  PHE   B CE1  1 
ATOM   3818 C  CE2  . PHE   B 1 94  ? 40.10650 -7.02487  27.95752  1.000 16.19853 ?  97  PHE   B CE2  1 
ATOM   3819 C  CZ   . PHE   B 1 94  ? 41.28356 -7.23619  27.28027  1.000 16.21233 ?  97  PHE   B CZ   1 
ATOM   3820 H  H    . PHE   B 1 94  ? 39.30039 -8.87824  31.59327  1.000 25.20546 ?  97  PHE   B H    1 
ATOM   3821 H  HA   . PHE   B 1 94  ? 41.94157 -9.18226  31.81791  1.000 24.22870 ?  97  PHE   B HA   1 
ATOM   3822 H  HB2  . PHE   B 1 94  ? 40.38336 -6.80637  31.84483  1.000 22.66058 ?  97  PHE   B HB2  1 
ATOM   3823 H  HB3  . PHE   B 1 94  ? 41.97200 -6.79898  31.88452  1.000 22.66058 ?  97  PHE   B HB3  1 
ATOM   3824 H  HD1  . PHE   B 1 94  ? 43.19756 -7.59633  29.85981  1.000 21.77893 ?  97  PHE   B HD1  1 
ATOM   3825 H  HD2  . PHE   B 1 94  ? 39.27341 -6.87909  29.77856  1.000 18.75697 ?  97  PHE   B HD2  1 
ATOM   3826 H  HE1  . PHE   B 1 94  ? 43.25504 -7.58375  27.54591  1.000 21.70170 ?  97  PHE   B HE1  1 
ATOM   3827 H  HE2  . PHE   B 1 94  ? 39.32109 -6.88049  27.48088  1.000 19.43823 ?  97  PHE   B HE2  1 
ATOM   3828 H  HZ   . PHE   B 1 94  ? 41.29542 -7.23815  26.35035  1.000 19.45480 ?  97  PHE   B HZ   1 
ATOM   3829 N  N    . LYS   B 1 95  ? 42.55477 -8.54140  34.14345  1.000 23.05772 ?  98  LYS   B N    1 
ATOM   3830 C  CA   . LYS   B 1 95  ? 42.85269 -8.45151  35.56828  1.000 26.92855 ?  98  LYS   B CA   1 
ATOM   3831 C  C    . LYS   B 1 95  ? 44.17629 -7.71405  35.74724  1.000 27.22202 ?  98  LYS   B C    1 
ATOM   3832 O  O    . LYS   B 1 95  ? 45.13308 -7.98387  35.01826  1.000 26.64591 ?  98  LYS   B O    1 
ATOM   3833 C  CB   . LYS   B 1 95  ? 43.01791 -9.84882  36.20278  1.000 30.27792 ?  98  LYS   B CB   1 
ATOM   3834 C  CG   . LYS   B 1 95  ? 41.85009 -10.40905 37.00531  1.000 35.04389 ?  98  LYS   B CG   1 
ATOM   3835 C  CD   . LYS   B 1 95  ? 42.11736 -11.87154 37.44999  1.000 37.92619 ?  98  LYS   B CD   1 
ATOM   3836 C  CE   . LYS   B 1 95  ? 41.90242 -12.10488 38.94602  1.000 40.92501 ?  98  LYS   B CE   1 
ATOM   3837 N  NZ   . LYS   B 1 95  ? 43.12886 -11.81566 39.76484  1.000 41.64783 ?  98  LYS   B NZ   1 
ATOM   3838 H  H    . LYS   B 1 95  ? 43.25667 -8.56643  33.64715  1.000 27.66927 ?  98  LYS   B H    1 
ATOM   3839 H  HA   . LYS   B 1 95  ? 42.13288 -7.97048  36.00575  1.000 32.31426 ?  98  LYS   B HA   1 
ATOM   3840 H  HB2  . LYS   B 1 95  ? 43.19208 -10.47993 35.48705  1.000 36.33350 ?  98  LYS   B HB2  1 
ATOM   3841 H  HB3  . LYS   B 1 95  ? 43.77747 -9.81225  36.80498  1.000 36.33350 ?  98  LYS   B HB3  1 
ATOM   3842 H  HG2  . LYS   B 1 95  ? 41.71680 -9.86820  37.79942  1.000 42.05266 ?  98  LYS   B HG2  1 
ATOM   3843 H  HG3  . LYS   B 1 95  ? 41.04923 -10.39802 36.45813  1.000 42.05266 ?  98  LYS   B HG3  1 
ATOM   3844 H  HD2  . LYS   B 1 95  ? 41.51503 -12.46037 36.96898  1.000 45.51143 ?  98  LYS   B HD2  1 
ATOM   3845 H  HD3  . LYS   B 1 95  ? 43.03774 -12.09840 37.24421  1.000 45.51143 ?  98  LYS   B HD3  1 
ATOM   3846 H  HE2  . LYS   B 1 95  ? 41.19098 -11.52363 39.25729  1.000 49.11001 ?  98  LYS   B HE2  1 
ATOM   3847 H  HE3  . LYS   B 1 95  ? 41.65917 -13.03292 39.08915  1.000 49.11001 ?  98  LYS   B HE3  1 
ATOM   3848 H  HZ1  . LYS   B 1 95  ? 42.96345 -11.96973 40.62566  1.000 49.97740 ?  98  LYS   B HZ1  1 
ATOM   3849 H  HZ2  . LYS   B 1 95  ? 43.80038 -12.33721 39.50190  1.000 49.97740 ?  98  LYS   B HZ2  1 
ATOM   3850 H  HZ3  . LYS   B 1 95  ? 43.36802 -10.96428 39.66455  1.000 49.97740 ?  98  LYS   B HZ3  1 
ATOM   3851 N  N    . ARG   B 1 96  ? 44.25158 -6.82549  36.74362  1.000 26.71702 ?  99  ARG   B N    1 
ATOM   3852 C  CA   . ARG   B 1 96  ? 45.53546 -6.24142  37.10549  1.000 28.17859 ?  99  ARG   B CA   1 
ATOM   3853 C  C    . ARG   B 1 96  ? 46.52306 -7.37474  37.35243  1.000 29.66577 ?  99  ARG   B C    1 
ATOM   3854 O  O    . ARG   B 1 96  ? 46.20843 -8.34632  38.04673  1.000 31.52796 ?  99  ARG   B O    1 
ATOM   3855 C  CB   . ARG   B 1 96  ? 45.39434 -5.38694  38.37452  1.000 28.30774 ?  99  ARG   B CB   1 
ATOM   3856 C  CG   . ARG   B 1 96  ? 44.67435 -4.04514  38.14601  1.000 28.72610 ?  99  ARG   B CG   1 
ATOM   3857 C  CD   . ARG   B 1 96  ? 44.40952 -3.34786  39.47563  1.000 28.79437 ?  99  ARG   B CD   1 
ATOM   3858 N  NE   . ARG   B 1 96  ? 43.75523 -2.05735  39.30674  1.000 30.10490 ?  99  ARG   B NE   1 
ATOM   3859 C  CZ   . ARG   B 1 96  ? 42.63288 -1.68434  39.91062  1.000 34.55685 ?  99  ARG   B CZ   1 
ATOM   3860 N  NH1  . ARG   B 1 96  ? 41.99021 -2.48545  40.75233  1.000 38.39173 ?  99  ARG   B NH1  1 
ATOM   3861 N  NH2  . ARG   B 1 96  ? 42.15082 -0.46848  39.67762  1.000 36.58703 ?  99  ARG   B NH2  1 
ATOM   3862 H  H    . ARG   B 1 96  ? 43.58454 -6.55296  37.21308  1.000 32.06042 ?  99  ARG   B H    1 
ATOM   3863 H  HA   . ARG   B 1 96  ? 45.85669 -5.66193  36.39704  1.000 33.81431 ?  99  ARG   B HA   1 
ATOM   3864 H  HB2  . ARG   B 1 96  ? 44.88558 -5.88720  39.03164  1.000 33.96929 ?  99  ARG   B HB2  1 
ATOM   3865 H  HB3  . ARG   B 1 96  ? 46.28005 -5.19224  38.71876  1.000 33.96929 ?  99  ARG   B HB3  1 
ATOM   3866 H  HG2  . ARG   B 1 96  ? 45.22944 -3.46736  37.59925  1.000 34.47132 ?  99  ARG   B HG2  1 
ATOM   3867 H  HG3  . ARG   B 1 96  ? 43.82481 -4.20301  37.70527  1.000 34.47132 ?  99  ARG   B HG3  1 
ATOM   3868 H  HD2  . ARG   B 1 96  ? 43.83373 -3.90845  40.01887  1.000 34.55324 ?  99  ARG   B HD2  1 
ATOM   3869 H  HD3  . ARG   B 1 96  ? 45.25357 -3.20019  39.93025  1.000 34.55324 ?  99  ARG   B HD3  1 
ATOM   3870 H  HE   . ARG   B 1 96  ? 44.12494 -1.49251  38.77395  1.000 36.12588 ?  99  ARG   B HE   1 
ATOM   3871 H  HH11 . ARG   B 1 96  ? 42.29920 -3.27041  40.91953  1.000 46.07008 ?  99  ARG   B HH11 1 
ATOM   3872 H  HH12 . ARG   B 1 96  ? 41.26499 -2.21932  41.13026  1.000 46.07008 ?  99  ARG   B HH12 1 
ATOM   3873 H  HH21 . ARG   B 1 96  ? 42.56466 0.06298   39.14292  1.000 43.90444 ?  99  ARG   B HH21 1 
ATOM   3874 H  HH22 . ARG   B 1 96  ? 41.42494 -0.21286  40.06148  1.000 43.90444 ?  99  ARG   B HH22 1 
ATOM   3875 N  N    . GLU   B 1 97  ? 47.71226 -7.26126  36.77592  1.000 30.97518 ?  100 GLU   B N    1 
ATOM   3876 C  CA   . GLU   B 1 97  ? 48.81099 -8.23341  36.89121  1.000 34.07089 ?  100 GLU   B CA   1 
ATOM   3877 C  C    . GLU   B 1 97  ? 48.67506 -9.45783  35.96966  1.000 35.64941 ?  100 GLU   B C    1 
ATOM   3878 O  O    . GLU   B 1 97  ? 49.54789 -10.33168 36.01983  1.000 39.95339 ?  100 GLU   B O    1 
ATOM   3879 C  CB   . GLU   B 1 97  ? 49.06966 -8.70881  38.33592  1.000 36.98934 ?  100 GLU   B CB   1 
ATOM   3880 C  CG   . GLU   B 1 97  ? 49.18306 -7.57551  39.32951  1.000 40.77081 ?  100 GLU   B CG   1 
ATOM   3881 C  CD   . GLU   B 1 97  ? 50.00727 -7.93838  40.56370  1.000 45.01915 ?  100 GLU   B CD   1 
ATOM   3882 O  OE1  . GLU   B 1 97  ? 50.18886 -9.14385  40.85854  1.000 47.20488 ?  100 GLU   B OE1  1 
ATOM   3883 O  OE2  . GLU   B 1 97  ? 50.48501 -7.00521  41.24655  1.000 45.35967 ?  100 GLU   B OE2  1 
ATOM   3884 H  H    . GLU   B 1 97  ? 47.92311 -6.58971  36.28180  1.000 37.17022 ?  100 GLU   B H    1 
ATOM   3885 H  HA   . GLU   B 1 97  ? 49.60778 -7.76905  36.59054  1.000 40.88506 ?  100 GLU   B HA   1 
ATOM   3886 H  HB2  . GLU   B 1 97  ? 48.33465 -9.27694  38.61501  1.000 44.38721 ?  100 GLU   B HB2  1 
ATOM   3887 H  HB3  . GLU   B 1 97  ? 49.90124 -9.20773  38.35728  1.000 44.38721 ?  100 GLU   B HB3  1 
ATOM   3888 H  HG2  . GLU   B 1 97  ? 49.61053 -6.81973  38.89711  1.000 48.92497 ?  100 GLU   B HG2  1 
ATOM   3889 H  HG3  . GLU   B 1 97  ? 48.29364 -7.32798  39.62712  1.000 48.92497 ?  100 GLU   B HG3  1 
ATOM   3890 N  N    . LYS   B 1 98  ? 47.64288 -9.55877  35.13081  1.000 32.29333 ?  101 LYS   B N    1 
ATOM   3891 C  CA   . LYS   B 1 98  ? 47.46516 -10.71377 34.25812  1.000 29.95518 ?  101 LYS   B CA   1 
ATOM   3892 C  C    . LYS   B 1 98  ? 47.83289 -10.31657 32.82733  1.000 27.71374 ?  101 LYS   B C    1 
ATOM   3893 O  O    . LYS   B 1 98  ? 47.46350 -9.22693  32.34781  1.000 27.88355 ?  101 LYS   B O    1 
ATOM   3894 C  CB   . LYS   B 1 98  ? 46.02255 -11.25185 34.29795  1.000 31.45749 ?  101 LYS   B CB   1 
ATOM   3895 C  CG   . LYS   B 1 98  ? 45.76767 -12.57595 33.50626  1.000 33.00454 ?  101 LYS   B CG   1 
ATOM   3896 C  CD   . LYS   B 1 98  ? 44.33826 -13.17689 33.66373  1.000 36.07197 ?  101 LYS   B CD   1 
ATOM   3897 C  CE   . LYS   B 1 98  ? 44.20765 -14.49127 32.86207  1.000 37.66421 ?  101 LYS   B CE   1 
ATOM   3898 N  NZ   . LYS   B 1 98  ? 42.86079 -15.14561 32.90145  1.000 39.62247 ?  101 LYS   B NZ   1 
ATOM   3899 H  H    . LYS   B 1 98  ? 47.02771 -8.96317  35.05066  1.000 38.75200 ?  101 LYS   B H    1 
ATOM   3900 H  HA   . LYS   B 1 98  ? 48.04772 -11.43185 34.55116  1.000 35.94622 ?  101 LYS   B HA   1 
ATOM   3901 H  HB2  . LYS   B 1 98  ? 45.78671 -11.42059 35.22359  1.000 37.74899 ?  101 LYS   B HB2  1 
ATOM   3902 H  HB3  . LYS   B 1 98  ? 45.43580 -10.57600 33.92400  1.000 37.74899 ?  101 LYS   B HB3  1 
ATOM   3903 H  HG2  . LYS   B 1 98  ? 45.90553 -12.40092 32.56219  1.000 39.60544 ?  101 LYS   B HG2  1 
ATOM   3904 H  HG3  . LYS   B 1 98  ? 46.39841 -13.24499 33.81520  1.000 39.60544 ?  101 LYS   B HG3  1 
ATOM   3905 H  HD2  . LYS   B 1 98  ? 44.16799 -13.36816 34.59931  1.000 43.28637 ?  101 LYS   B HD2  1 
ATOM   3906 H  HD3  . LYS   B 1 98  ? 43.68221 -12.54540 33.32947  1.000 43.28637 ?  101 LYS   B HD3  1 
ATOM   3907 H  HE2  . LYS   B 1 98  ? 44.40781 -14.30225 31.93196  1.000 45.19705 ?  101 LYS   B HE2  1 
ATOM   3908 H  HE3  . LYS   B 1 98  ? 44.84704 -15.12907 33.21604  1.000 45.19705 ?  101 LYS   B HE3  1 
ATOM   3909 H  HZ1  . LYS   B 1 98  ? 42.89133 -15.93050 32.48297  1.000 47.54697 ?  101 LYS   B HZ1  1 
ATOM   3910 H  HZ2  . LYS   B 1 98  ? 42.61115 -15.27780 33.74544  1.000 47.54697 ?  101 LYS   B HZ2  1 
ATOM   3911 H  HZ3  . LYS   B 1 98  ? 42.25878 -14.62746 32.49996  1.000 47.54697 ?  101 LYS   B HZ3  1 
ATOM   3912 N  N    . SER   B 1 99  ? 48.55926 -11.19769 32.14496  1.000 27.41829 ?  102 SER   B N    1 
ATOM   3913 C  CA   . SER   B 1 99  ? 48.87822 -10.97022 30.74157  1.000 25.98020 ?  102 SER   B CA   1 
ATOM   3914 C  C    . SER   B 1 99  ? 47.70149 -11.39141 29.86965  1.000 24.35167 ?  102 SER   B C    1 
ATOM   3915 O  O    . SER   B 1 99  ? 46.85681 -12.20820 30.25994  1.000 28.53283 ?  102 SER   B O    1 
ATOM   3916 C  CB   . SER   B 1 99  ? 50.11643 -11.76467 30.33430  1.000 28.44862 ?  102 SER   B CB   1 
ATOM   3917 O  OG   . SER   B 1 99  ? 51.27988 -11.24886 30.96388  1.000 32.06041 ?  102 SER   B OG   1 
ATOM   3918 H  H    . SER   B 1 99  ? 48.87591 -11.92828 32.46990  1.000 32.90195 ?  102 SER   B H    1 
ATOM   3919 H  HA   . SER   B 1 99  ? 49.06091 -10.02816 30.60000  1.000 31.17624 ?  102 SER   B HA   1 
ATOM   3920 H  HB2  . SER   B 1 99  ? 49.99851 -12.69030 30.59926  1.000 34.13834 ?  102 SER   B HB2  1 
ATOM   3921 H  HB3  . SER   B 1 99  ? 50.22624 -11.70637 29.37230  1.000 34.13834 ?  102 SER   B HB3  1 
ATOM   3922 H  HG   . SER   B 1 99  ? 51.44356 -10.47664 30.67667  1.000 38.47249 ?  102 SER   B HG   1 
ATOM   3923 N  N    . PHE   B 1 100 ? 47.63731 -10.80001 28.67820  1.000 19.89799 ?  103 PHE   B N    1 
ATOM   3924 C  CA   . PHE   B 1 100 ? 46.52555 -11.03872 27.77711  1.000 18.07997 ?  103 PHE   B CA   1 
ATOM   3925 C  C    . PHE   B 1 100 ? 47.01436 -11.12540 26.34360  1.000 16.39614 ?  103 PHE   B C    1 
ATOM   3926 O  O    . PHE   B 1 100 ? 48.06663 -10.58719 25.98941  1.000 15.57823 ?  103 PHE   B O    1 
ATOM   3927 C  CB   . PHE   B 1 100 ? 45.46749 -9.92346  27.87721  1.000 18.00335 ?  103 PHE   B CB   1 
ATOM   3928 C  CG   . PHE   B 1 100 ? 46.01030 -8.53521  27.63906  1.000 15.81636 ?  103 PHE   B CG   1 
ATOM   3929 C  CD1  . PHE   B 1 100 ? 46.25877 -8.07773  26.35698  1.000 14.76839 ?  103 PHE   B CD1  1 
ATOM   3930 C  CD2  . PHE   B 1 100 ? 46.23862 -7.67395  28.69399  1.000 16.38083 ?  103 PHE   B CD2  1 
ATOM   3931 C  CE1  . PHE   B 1 100 ? 46.74329 -6.80684  26.14727  1.000 13.83303 ?  103 PHE   B CE1  1 
ATOM   3932 C  CE2  . PHE   B 1 100 ? 46.73524 -6.40324  28.48271  1.000 15.76989 ?  103 PHE   B CE2  1 
ATOM   3933 C  CZ   . PHE   B 1 100 ? 46.97966 -5.97080  27.21003  1.000 14.80770 ?  103 PHE   B CZ   1 
ATOM   3934 H  H    . PHE   B 1 100 ? 48.22943 -10.25598 28.37321  1.000 23.87759 ?  103 PHE   B H    1 
ATOM   3935 H  HA   . PHE   B 1 100 ? 46.12402 -11.88992 28.01192  1.000 21.69597 ?  103 PHE   B HA   1 
ATOM   3936 H  HB2  . PHE   B 1 100 ? 44.77898 -10.08824 27.21412  1.000 21.60402 ?  103 PHE   B HB2  1 
ATOM   3937 H  HB3  . PHE   B 1 100 ? 45.08187 -9.94027  28.76710  1.000 21.60402 ?  103 PHE   B HB3  1 
ATOM   3938 H  HD1  . PHE   B 1 100 ? 46.09676 -8.63454  25.62993  1.000 17.72207 ?  103 PHE   B HD1  1 
ATOM   3939 H  HD2  . PHE   B 1 100 ? 46.05478 -7.95461  29.56137  1.000 19.65699 ?  103 PHE   B HD2  1 
ATOM   3940 H  HE1  . PHE   B 1 100 ? 46.91144 -6.51292  25.28111  1.000 16.59964 ?  103 PHE   B HE1  1 
ATOM   3941 H  HE2  . PHE   B 1 100 ? 46.90310 -5.84260  29.20548  1.000 18.92387 ?  103 PHE   B HE2  1 
ATOM   3942 H  HZ   . PHE   B 1 100 ? 47.30541 -5.11203  27.06405  1.000 17.76924 ?  103 PHE   B HZ   1 
ATOM   3943 N  N    . GLU   B 1 101 ? 46.18458 -11.76163 25.51468  1.000 17.66677 ?  104 GLU   B N    1 
ATOM   3944 C  CA   . GLU   B 1 101 ? 46.27358 -11.68171 24.06171  1.000 17.64366 ?  104 GLU   B CA   1 
ATOM   3945 C  C    . GLU   B 1 101 ? 44.89665 -11.31223 23.53311  1.000 17.36878 ?  104 GLU   B C    1 
ATOM   3946 O  O    . GLU   B 1 101 ? 43.96151 -12.11762 23.62940  1.000 20.45973 ?  104 GLU   B O    1 
ATOM   3947 C  CB   . GLU   B 1 101 ? 46.72262 -12.99991 23.44165  1.000 19.69187 ?  104 GLU   B CB   1 
ATOM   3948 C  CG   . GLU   B 1 101 ? 46.72737 -12.92830 21.92275  1.000 22.47205 ?  104 GLU   B CG   1 
ATOM   3949 C  CD   . GLU   B 1 101 ? 47.05450 -14.24037 21.26830  1.000 30.28062 ?  104 GLU   B CD   1 
ATOM   3950 O  OE1  . GLU   B 1 101 ? 46.12867 -15.07415 21.09484  1.000 34.74896 ?  104 GLU   B OE1  1 
ATOM   3951 O  OE2  . GLU   B 1 101 ? 48.23583 -14.42678 20.92115  1.000 33.59516 ?  104 GLU   B OE2  1 
ATOM   3952 H  H    . GLU   B 1 101 ? 45.53963 -12.26305 25.78339  1.000 21.20012 ?  104 GLU   B H    1 
ATOM   3953 H  HA   . GLU   B 1 101 ? 46.91676 -10.99506 23.82565  1.000 21.17239 ?  104 GLU   B HA   1 
ATOM   3954 H  HB2  . GLU   B 1 101 ? 47.62230 -13.20478 23.74083  1.000 23.63024 ?  104 GLU   B HB2  1 
ATOM   3955 H  HB3  . GLU   B 1 101 ? 46.11426 -13.70519 23.71253  1.000 23.63024 ?  104 GLU   B HB3  1 
ATOM   3956 H  HG2  . GLU   B 1 101 ? 45.84795 -12.65470 21.61834  1.000 26.96646 ?  104 GLU   B HG2  1 
ATOM   3957 H  HG3  . GLU   B 1 101 ? 47.39234 -12.28084 21.64078  1.000 26.96646 ?  104 GLU   B HG3  1 
ATOM   3958 N  N    . ILE   B 1 102 ? 44.78586 -10.10141 22.98409  1.000 13.50420 ?  105 ILE   B N    1 
ATOM   3959 C  CA   . ILE   B 1 102 ? 43.56667 -9.60745  22.36432  1.000 13.26053 ?  105 ILE   B CA   1 
ATOM   3960 C  C    . ILE   B 1 102 ? 43.65275 -9.91633  20.88374  1.000 12.58064 ?  105 ILE   B C    1 
ATOM   3961 O  O    . ILE   B 1 102 ? 44.65177 -9.58109  20.23556  1.000 13.32740 ?  105 ILE   B O    1 
ATOM   3962 C  CB   . ILE   B 1 102 ? 43.44543 -8.09024  22.55638  1.000 13.43127 ?  105 ILE   B CB   1 
ATOM   3963 C  CG1  . ILE   B 1 102 ? 43.33128 -7.70326  24.02206  1.000 14.44955 ?  105 ILE   B CG1  1 
ATOM   3964 C  CG2  . ILE   B 1 102 ? 42.24335 -7.55700  21.77609  1.000 15.48480 ?  105 ILE   B CG2  1 
ATOM   3965 C  CD1  . ILE   B 1 102 ? 43.56997 -6.21408  24.27885  1.000 15.26197 ?  105 ILE   B CD1  1 
ATOM   3966 H  H    . ILE   B 1 102 ? 45.42886 -9.53083  22.95975  1.000 16.20504 ?  105 ILE   B H    1 
ATOM   3967 H  HA   . ILE   B 1 102 ? 42.79579 -10.04629 22.75681  1.000 15.91264 ?  105 ILE   B HA   1 
ATOM   3968 H  HB   . ILE   B 1 102 ? 44.26098 -7.69162  22.21453  1.000 16.11753 ?  105 ILE   B HB   1 
ATOM   3969 H  HG12 . ILE   B 1 102 ? 42.43878 -7.91957  24.33439  1.000 17.33946 ?  105 ILE   B HG12 1 
ATOM   3970 H  HG13 . ILE   B 1 102 ? 43.99039 -8.20195  24.52978  1.000 17.33946 ?  105 ILE   B HG13 1 
ATOM   3971 H  HG21 . ILE   B 1 102 ? 42.08942 -6.63251  22.02614  1.000 18.58176 ?  105 ILE   B HG21 1 
ATOM   3972 H  HG22 . ILE   B 1 102 ? 42.43199 -7.61579  20.82643  1.000 18.58176 ?  105 ILE   B HG22 1 
ATOM   3973 H  HG23 . ILE   B 1 102 ? 41.46385 -8.09230  21.99226  1.000 18.58176 ?  105 ILE   B HG23 1 
ATOM   3974 H  HD11 . ILE   B 1 102 ? 43.64899 -6.06707  25.23439  1.000 18.31437 ?  105 ILE   B HD11 1 
ATOM   3975 H  HD12 . ILE   B 1 102 ? 44.38850 -5.94410  23.83385  1.000 18.31437 ?  105 ILE   B HD12 1 
ATOM   3976 H  HD13 . ILE   B 1 102 ? 42.82024 -5.70886  23.92734  1.000 18.31437 ?  105 ILE   B HD13 1 
ATOM   3977 N  N    . VAL   B 1 103 ? 42.60925 -10.53794 20.34685  1.000 12.73049 ?  106 VAL   B N    1 
ATOM   3978 C  CA   . VAL   B 1 103 ? 42.46963 -10.70655 18.90556  1.000 12.88496 ?  106 VAL   B CA   1 
ATOM   3979 C  C    . VAL   B 1 103 ? 41.19396 -9.99157  18.49066  1.000 12.20918 ?  106 VAL   B C    1 
ATOM   3980 O  O    . VAL   B 1 103 ? 40.09639 -10.39273 18.89867  1.000 13.23141 ?  106 VAL   B O    1 
ATOM   3981 C  CB   . VAL   B 1 103 ? 42.46625 -12.18176 18.47721  1.000 13.83224 ?  106 VAL   B CB   1 
ATOM   3982 C  CG1  . VAL   B 1 103 ? 42.29613 -12.27188 16.96633  1.000 15.34449 ?  106 VAL   B CG1  1 
ATOM   3983 C  CG2  . VAL   B 1 103 ? 43.74315 -12.86632 18.91132  1.000 14.95398 ?  106 VAL   B CG2  1 
ATOM   3984 H  H    . VAL   B 1 103 ? 41.96214 -10.87422 20.80267  1.000 15.27659 ?  106 VAL   B H    1 
ATOM   3985 H  HA   . VAL   B 1 103 ? 43.21864 -10.28547 18.45549  1.000 15.46195 ?  106 VAL   B HA   1 
ATOM   3986 H  HB   . VAL   B 1 103 ? 41.72597 -12.64027 18.90460  1.000 16.59869 ?  106 VAL   B HB   1 
ATOM   3987 H  HG11 . VAL   B 1 103 ? 42.48015 -13.18067 16.68147  1.000 18.41339 ?  106 VAL   B HG11 1 
ATOM   3988 H  HG12 . VAL   B 1 103 ? 41.38509 -12.03116 16.73620  1.000 18.41339 ?  106 VAL   B HG12 1 
ATOM   3989 H  HG13 . VAL   B 1 103 ? 42.91733 -11.65988 16.54153  1.000 18.41339 ?  106 VAL   B HG13 1 
ATOM   3990 H  HG21 . VAL   B 1 103 ? 43.72355 -13.78933 18.61369  1.000 17.94478 ?  106 VAL   B HG21 1 
ATOM   3991 H  HG22 . VAL   B 1 103 ? 44.49895 -12.40649 18.51356  1.000 17.94478 ?  106 VAL   B HG22 1 
ATOM   3992 H  HG23 . VAL   B 1 103 ? 43.80678 -12.83196 19.87862  1.000 17.94478 ?  106 VAL   B HG23 1 
ATOM   3993 N  N    . ILE   B 1 104 ? 41.33428 -8.94275  17.68733  1.000 12.01702 ?  107 ILE   B N    1 
ATOM   3994 C  CA   . ILE   B 1 104 ? 40.20012 -8.24690  17.09858  1.000 11.77507 ?  107 ILE   B CA   1 
ATOM   3995 C  C    . ILE   B 1 104 ? 40.05681 -8.76704  15.67354  1.000 11.59550 ?  107 ILE   B C    1 
ATOM   3996 O  O    . ILE   B 1 104 ? 40.96280 -8.59882  14.84794  1.000 12.84259 ?  107 ILE   B O    1 
ATOM   3997 C  CB   . ILE   B 1 104 ? 40.41234 -6.72503  17.08104  1.000 12.43974 ?  107 ILE   B CB   1 
ATOM   3998 C  CG1  . ILE   B 1 104 ? 40.61756 -6.17229  18.49513  1.000 13.60391 ?  107 ILE   B CG1  1 
ATOM   3999 C  CG2  . ILE   B 1 104 ? 39.22422 -6.05396  16.39459  1.000 13.68966 ?  107 ILE   B CG2  1 
ATOM   4000 C  CD1  . ILE   B 1 104 ? 41.11546 -4.76389  18.53549  1.000 14.98836 ?  107 ILE   B CD1  1 
ATOM   4001 H  H    . ILE   B 1 104 ? 42.09508 -8.60937  17.46453  1.000 14.42043 ?  107 ILE   B H    1 
ATOM   4002 H  HA   . ILE   B 1 104 ? 39.39874 -8.44013  17.60980  1.000 14.13009 ?  107 ILE   B HA   1 
ATOM   4003 H  HB   . ILE   B 1 104 ? 41.22055 -6.53159  16.58075  1.000 14.92769 ?  107 ILE   B HB   1 
ATOM   4004 H  HG12 . ILE   B 1 104 ? 39.76904 -6.19798  18.96445  1.000 16.32469 ?  107 ILE   B HG12 1 
ATOM   4005 H  HG13 . ILE   B 1 104 ? 41.26739 -6.72738  18.95393  1.000 16.32469 ?  107 ILE   B HG13 1 
ATOM   4006 H  HG21 . ILE   B 1 104 ? 39.39716 -5.10219  16.32298  1.000 16.42759 ?  107 ILE   B HG21 1 
ATOM   4007 H  HG22 . ILE   B 1 104 ? 39.11246 -6.43728  15.51058  1.000 16.42759 ?  107 ILE   B HG22 1 
ATOM   4008 H  HG23 . ILE   B 1 104 ? 38.42611 -6.20619  16.92445  1.000 16.42759 ?  107 ILE   B HG23 1 
ATOM   4009 H  HD11 . ILE   B 1 104 ? 41.28265 -4.51435  19.45782  1.000 17.98603 ?  107 ILE   B HD11 1 
ATOM   4010 H  HD12 . ILE   B 1 104 ? 41.93667 -4.70444  18.02268  1.000 17.98603 ?  107 ILE   B HD12 1 
ATOM   4011 H  HD13 . ILE   B 1 104 ? 40.44274 -4.17999  18.15158  1.000 17.98603 ?  107 ILE   B HD13 1 
ATOM   4012 N  N    . MET   B 1 105 ? 38.92519 -9.38450  15.38524  1.000 12.23550 ?  108 MET   B N    1 
ATOM   4013 C  CA   A MET   B 1 105 ? 38.59034 -9.83964  14.04564  0.617 12.77514 ?  108 MET   B CA   1 
ATOM   4014 C  CA   B MET   B 1 105 ? 38.59598 -9.83809  14.03975  0.383 12.96157 ?  108 MET   B CA   1 
ATOM   4015 C  C    . MET   B 1 105 ? 37.60955 -8.86015  13.42236  1.000 12.34120 ?  108 MET   B C    1 
ATOM   4016 O  O    . MET   B 1 105 ? 36.56499 -8.56628  14.01250  1.000 13.40654 ?  108 MET   B O    1 
ATOM   4017 C  CB   A MET   B 1 105 ? 37.95356 -11.22575 14.11947  0.617 13.98831 ?  108 MET   B CB   1 
ATOM   4018 C  CB   B MET   B 1 105 ? 38.00374 -11.24912 14.03015  0.383 14.58752 ?  108 MET   B CB   1 
ATOM   4019 C  CG   A MET   B 1 105 ? 37.49956 -11.75650 12.80421  0.617 15.90707 ?  108 MET   B CG   1 
ATOM   4020 C  CG   B MET   B 1 105 ? 37.79111 -11.78490 12.61257  0.383 16.89824 ?  108 MET   B CG   1 
ATOM   4021 S  SD   A MET   B 1 105 ? 36.67625 -13.32778 12.96178  0.617 18.00172 ?  108 MET   B SD   1 
ATOM   4022 S  SD   B MET   B 1 105 ? 37.29475 -13.50725 12.50609  0.383 18.81359 ?  108 MET   B SD   1 
ATOM   4023 C  CE   A MET   B 1 105 ? 36.61812 -13.76571 11.22835  0.617 19.00365 ?  108 MET   B CE   1 
ATOM   4024 C  CE   B MET   B 1 105 ? 35.80694 -13.48538 13.50752  0.383 20.59229 ?  108 MET   B CE   1 
ATOM   4025 H  H    . MET   B 1 105 ? 38.31638 -9.55649  15.96779  1.000 14.68260 ?  108 MET   B H    1 
ATOM   4026 H  HA   . MET   B 1 105 ? 39.39046 -9.88766  13.49939  1.000 15.55389 ?  108 MET   B HA   1 
ATOM   4027 H  HB2  A MET   B 1 105 ? 38.60483 -11.84794 14.47951  0.617 16.78597 ?  108 MET   B HB2  1 
ATOM   4028 H  HB2  B MET   B 1 105 ? 38.60931 -11.84992 14.49192  0.383 17.50502 ?  108 MET   B HB2  1 
ATOM   4029 H  HB3  A MET   B 1 105 ? 37.17959 -11.18131 14.70248  0.617 16.78597 ?  108 MET   B HB3  1 
ATOM   4030 H  HB3  B MET   B 1 105 ? 37.14406 -11.23484 14.47922  0.383 17.50502 ?  108 MET   B HB3  1 
ATOM   4031 H  HG2  A MET   B 1 105 ? 36.87800 -11.12805 12.40471  0.617 19.08848 ?  108 MET   B HG2  1 
ATOM   4032 H  HG2  B MET   B 1 105 ? 37.09678 -11.25766 12.18734  0.383 20.27789 ?  108 MET   B HG2  1 
ATOM   4033 H  HG3  A MET   B 1 105 ? 38.26924 -11.87496 12.22589  0.617 19.08848 ?  108 MET   B HG3  1 
ATOM   4034 H  HG3  B MET   B 1 105 ? 38.62360 -11.69370 12.12314  0.383 20.27789 ?  108 MET   B HG3  1 
ATOM   4035 H  HE1  A MET   B 1 105 ? 36.74073 -12.96426 10.69586  0.617 22.80438 ?  108 MET   B HE1  1 
ATOM   4036 H  HE1  B MET   B 1 105 ? 35.23369 -14.21980 13.23749  0.383 24.71075 ?  108 MET   B HE1  1 
ATOM   4037 H  HE2  A MET   B 1 105 ? 37.32690 -14.40028 11.03900  0.617 22.80438 ?  108 MET   B HE2  1 
ATOM   4038 H  HE2  B MET   B 1 105 ? 36.05289 -13.58357 14.44067  0.383 24.71075 ?  108 MET   B HE2  1 
ATOM   4039 H  HE3  A MET   B 1 105 ? 35.75595 -14.16453 11.03212  0.617 22.80438 ?  108 MET   B HE3  1 
ATOM   4040 H  HE3  B MET   B 1 105 ? 35.34835 -12.64122 13.37337  0.383 24.71075 ?  108 MET   B HE3  1 
ATOM   4041 N  N    . VAL   B 1 106 ? 37.94608 -8.36055  12.23976  1.000 12.46978 ?  109 VAL   B N    1 
ATOM   4042 C  CA   . VAL   B 1 106 ? 37.06555 -7.45585  11.51728  1.000 14.03195 ?  109 VAL   B CA   1 
ATOM   4043 C  C    . VAL   B 1 106 ? 36.11236 -8.30983  10.68318  1.000 15.55373 ?  109 VAL   B C    1 
ATOM   4044 O  O    . VAL   B 1 106 ? 36.54436 -9.11118  9.84953   1.000 19.00344 ?  109 VAL   B O    1 
ATOM   4045 C  CB   . VAL   B 1 106 ? 37.87569 -6.49451  10.63863  1.000 16.00143 ?  109 VAL   B CB   1 
ATOM   4046 C  CG1  . VAL   B 1 106 ? 36.95004 -5.49348  9.97661   1.000 19.27601 ?  109 VAL   B CG1  1 
ATOM   4047 C  CG2  . VAL   B 1 106 ? 38.91524 -5.81005  11.46930  1.000 16.19429 ?  109 VAL   B CG2  1 
ATOM   4048 H  H    . VAL   B 1 106 ? 38.68427 -8.53252  11.83343  1.000 14.96373 ?  109 VAL   B H    1 
ATOM   4049 H  HA   . VAL   B 1 106 ? 36.54189 -6.92665  12.13908  1.000 16.83834 ?  109 VAL   B HA   1 
ATOM   4050 H  HB   . VAL   B 1 106 ? 38.32840 -6.98665  9.93596   1.000 19.20171 ?  109 VAL   B HB   1 
ATOM   4051 H  HG11 . VAL   B 1 106 ? 37.44174 -4.67559  9.80284   1.000 23.13121 ?  109 VAL   B HG11 1 
ATOM   4052 H  HG12 . VAL   B 1 106 ? 36.62488 -5.86747  9.14276   1.000 23.13121 ?  109 VAL   B HG12 1 
ATOM   4053 H  HG13 . VAL   B 1 106 ? 36.20490 -5.31165  10.57042  1.000 23.13121 ?  109 VAL   B HG13 1 
ATOM   4054 H  HG21 . VAL   B 1 106 ? 39.26778 -5.05413  10.97411  1.000 19.43315 ?  109 VAL   B HG21 1 
ATOM   4055 H  HG22 . VAL   B 1 106 ? 38.50849 -5.50392  12.29497  1.000 19.43315 ?  109 VAL   B HG22 1 
ATOM   4056 H  HG23 . VAL   B 1 106 ? 39.62761 -6.43873  11.66471  1.000 19.43315 ?  109 VAL   B HG23 1 
ATOM   4057 N  N    . LEU   B 1 107 ? 34.81702 -8.16693  10.91087  1.000 16.41147 ?  110 LEU   B N    1 
ATOM   4058 C  CA   . LEU   B 1 107 ? 33.82064 -8.81380  10.07278  1.000 19.12863 ?  110 LEU   B CA   1 
ATOM   4059 C  C    . LEU   B 1 107 ? 33.14477 -7.75369  9.22826   1.000 19.96765 ?  110 LEU   B C    1 
ATOM   4060 O  O    . LEU   B 1 107 ? 33.36736 -6.56009  9.40195   1.000 18.57310 ?  110 LEU   B O    1 
ATOM   4061 C  CB   . LEU   B 1 107 ? 32.80003 -9.57680  10.91530  1.000 21.29013 ?  110 LEU   B CB   1 
ATOM   4062 C  CG   . LEU   B 1 107 ? 33.41247 -10.72720 11.71233  1.000 24.86293 ?  110 LEU   B CG   1 
ATOM   4063 C  CD1  . LEU   B 1 107 ? 32.32343 -11.43248 12.48595  1.000 28.45294 ?  110 LEU   B CD1  1 
ATOM   4064 C  CD2  . LEU   B 1 107 ? 34.13672 -11.70624 10.81619  1.000 28.10280 ?  110 LEU   B CD2  1 
ATOM   4065 H  H    . LEU   B 1 107 ? 34.48769 -7.69596  11.55066  1.000 19.69376 ?  110 LEU   B H    1 
ATOM   4066 H  HA   . LEU   B 1 107 ? 34.24388 -9.46298  9.48940   1.000 22.95436 ?  110 LEU   B HA   1 
ATOM   4067 H  HB2  . LEU   B 1 107 ? 32.39147 -8.96188  11.54447  1.000 25.54815 ?  110 LEU   B HB2  1 
ATOM   4068 H  HB3  . LEU   B 1 107 ? 32.12369 -9.94779  10.32723  1.000 25.54815 ?  110 LEU   B HB3  1 
ATOM   4069 H  HG   . LEU   B 1 107 ? 34.06928 -10.36810 12.32922  1.000 29.83552 ?  110 LEU   B HG   1 
ATOM   4070 H  HD11 . LEU   B 1 107 ? 32.72027 -12.14360 13.01294  1.000 34.14353 ?  110 LEU   B HD11 1 
ATOM   4071 H  HD12 . LEU   B 1 107 ? 31.88581 -10.79305 13.06949  1.000 34.14353 ?  110 LEU   B HD12 1 
ATOM   4072 H  HD13 . LEU   B 1 107 ? 31.68119 -11.80312 11.86061  1.000 34.14353 ?  110 LEU   B HD13 1 
ATOM   4073 H  HD21 . LEU   B 1 107 ? 34.40777 -12.47487 11.34216  1.000 33.72336 ?  110 LEU   B HD21 1 
ATOM   4074 H  HD22 . LEU   B 1 107 ? 33.53863 -11.98597 10.10560  1.000 33.72336 ?  110 LEU   B HD22 1 
ATOM   4075 H  HD23 . LEU   B 1 107 ? 34.91757 -11.27134 10.43931  1.000 33.72336 ?  110 LEU   B HD23 1 
ATOM   4076 N  N    . LYS   B 1 108 ? 32.29320 -8.19015  8.30984   1.000 22.00252 ?  111 LYS   B N    1 
ATOM   4077 C  CA   . LYS   B 1 108 ? 31.66635 -7.21089  7.43514   1.000 24.04921 ?  111 LYS   B CA   1 
ATOM   4078 C  C    . LYS   B 1 108 ? 30.76330 -6.26615  8.21397   1.000 21.41274 ?  111 LYS   B C    1 
ATOM   4079 O  O    . LYS   B 1 108 ? 30.58646 -5.11064  7.80766   1.000 21.04874 ?  111 LYS   B O    1 
ATOM   4080 C  CB   . LYS   B 1 108 ? 30.89654 -7.88602  6.30071   1.000 30.01575 ?  111 LYS   B CB   1 
ATOM   4081 C  CG   . LYS   B 1 108 ? 29.45801 -8.25247  6.58102   1.000 34.67602 ?  111 LYS   B CG   1 
ATOM   4082 C  CD   . LYS   B 1 108 ? 28.74876 -8.50285  5.24355   1.000 38.07097 ?  111 LYS   B CD   1 
ATOM   4083 C  CE   . LYS   B 1 108 ? 27.80328 -9.68881  5.28581   1.000 41.40293 ?  111 LYS   B CE   1 
ATOM   4084 N  NZ   . LYS   B 1 108 ? 26.71160 -9.53827  6.29385   1.000 42.92007 ?  111 LYS   B NZ   1 
ATOM   4085 H  H    . LYS   B 1 108 ? 32.07092 -9.01040  8.17800   1.000 26.40302 ?  111 LYS   B H    1 
ATOM   4086 H  HA   . LYS   B 1 108 ? 32.36841 -6.68604  7.01976   1.000 28.85905 ?  111 LYS   B HA   1 
ATOM   4087 H  HB2  . LYS   B 1 108 ? 30.89272 -7.28383  5.54029   1.000 36.01890 ?  111 LYS   B HB2  1 
ATOM   4088 H  HB3  . LYS   B 1 108 ? 31.35879 -8.70732  6.07119   1.000 36.01890 ?  111 LYS   B HB3  1 
ATOM   4089 H  HG2  . LYS   B 1 108 ? 29.41897 -9.06010  7.11684   1.000 41.61122 ?  111 LYS   B HG2  1 
ATOM   4090 H  HG3  . LYS   B 1 108 ? 29.01384 -7.52517  7.04433   1.000 41.61122 ?  111 LYS   B HG3  1 
ATOM   4091 H  HD2  . LYS   B 1 108 ? 28.23107 -7.71679  5.00903   1.000 45.68516 ?  111 LYS   B HD2  1 
ATOM   4092 H  HD3  . LYS   B 1 108 ? 29.41538 -8.67693  4.56075   1.000 45.68516 ?  111 LYS   B HD3  1 
ATOM   4093 H  HE2  . LYS   B 1 108 ? 27.39085 -9.79310  4.41407   1.000 49.68351 ?  111 LYS   B HE2  1 
ATOM   4094 H  HE3  . LYS   B 1 108 ? 28.30849 -10.48558 5.51126   1.000 49.68351 ?  111 LYS   B HE3  1 
ATOM   4095 H  HZ1  . LYS   B 1 108 ? 26.05086 -10.10682 6.11418   1.000 51.50408 ?  111 LYS   B HZ1  1 
ATOM   4096 H  HZ2  . LYS   B 1 108 ? 27.02486 -9.70793  7.10944   1.000 51.50408 ?  111 LYS   B HZ2  1 
ATOM   4097 H  HZ3  . LYS   B 1 108 ? 26.39158 -8.70803  6.27428   1.000 51.50408 ?  111 LYS   B HZ3  1 
ATOM   4098 N  N    . ASP   B 1 109 ? 30.14891 -6.74149  9.30459   1.000 20.88230 ?  112 ASP   B N    1 
ATOM   4099 C  CA   . ASP   B 1 109 ? 29.14596 -5.96186  10.01351  1.000 21.70981 ?  112 ASP   B CA   1 
ATOM   4100 C  C    . ASP   B 1 109 ? 29.51054 -5.63771  11.45093  1.000 16.60157 ?  112 ASP   B C    1 
ATOM   4101 O  O    . ASP   B 1 109 ? 28.76149 -4.90590  12.10833  1.000 15.71677 ?  112 ASP   B O    1 
ATOM   4102 C  CB   . ASP   B 1 109 ? 27.79166 -6.67631  9.98598   1.000 26.63600 ?  112 ASP   B CB   1 
ATOM   4103 C  CG   . ASP   B 1 109 ? 27.84886 -8.06810  10.56312  1.000 29.80528 ?  112 ASP   B CG   1 
ATOM   4104 O  OD1  . ASP   B 1 109 ? 28.94617 -8.65996  10.64095  1.000 31.01447 ?  112 ASP   B OD1  1 
ATOM   4105 O  OD2  . ASP   B 1 109 ? 26.75773 -8.59061  10.90015  1.000 34.14291 ?  112 ASP   B OD2  1 
ATOM   4106 H  H    . ASP   B 1 109 ? 30.30112 -7.51500  9.64827   1.000 25.05876 ?  112 ASP   B H    1 
ATOM   4107 H  HA   . ASP   B 1 109 ? 29.05040 -5.11729  9.54610   1.000 26.05177 ?  112 ASP   B HA   1 
ATOM   4108 H  HB2  . ASP   B 1 109 ? 27.15373 -6.16293  10.50596  1.000 31.96320 ?  112 ASP   B HB2  1 
ATOM   4109 H  HB3  . ASP   B 1 109 ? 27.49058 -6.74599  9.06652   1.000 31.96320 ?  112 ASP   B HB3  1 
ATOM   4110 N  N    . LYS   B 1 110 ? 30.63959 -6.13478  11.95616  1.000 15.64692 ?  113 LYS   B N    1 
ATOM   4111 C  CA   . LYS   B 1 110 ? 30.96606 -5.96558  13.36284  1.000 14.36984 ?  113 LYS   B CA   1 
ATOM   4112 C  C    . LYS   B 1 110 ? 32.42837 -6.32801  13.56476  1.000 13.10301 ?  113 LYS   B C    1 
ATOM   4113 O  O    . LYS   B 1 110 ? 33.07870 -6.89698  12.68446  1.000 14.31579 ?  113 LYS   B O    1 
ATOM   4114 C  CB   . LYS   B 1 110 ? 30.09464 -6.86898  14.24088  1.000 15.32110 ?  113 LYS   B CB   1 
ATOM   4115 C  CG   . LYS   B 1 110 ? 30.28735 -8.34838  13.97503  1.000 17.52148 ?  113 LYS   B CG   1 
ATOM   4116 C  CD   . LYS   B 1 110 ? 29.22734 -9.17014  14.67135  1.000 22.41299 ?  113 LYS   B CD   1 
ATOM   4117 C  CE   . LYS   B 1 110 ? 27.85194 -8.96902  14.04635  1.000 27.19867 ?  113 LYS   B CE   1 
ATOM   4118 N  NZ   . LYS   B 1 110 ? 26.77677 -9.63243  14.84282  1.000 33.04312 ?  113 LYS   B NZ   1 
ATOM   4119 H  H    . LYS   B 1 110 ? 31.22653 -6.57077  11.50339  1.000 18.77631 ?  113 LYS   B H    1 
ATOM   4120 H  HA   . LYS   B 1 110 ? 30.83218 -5.03667  13.60802  1.000 17.24381 ?  113 LYS   B HA   1 
ATOM   4121 H  HB2  . LYS   B 1 110 ? 30.31348 -6.70434  15.17142  1.000 18.38532 ?  113 LYS   B HB2  1 
ATOM   4122 H  HB3  . LYS   B 1 110 ? 29.16225 -6.65763  14.07694  1.000 18.38532 ?  113 LYS   B HB3  1 
ATOM   4123 H  HG2  . LYS   B 1 110 ? 30.22708 -8.51535  13.02142  1.000 21.02578 ?  113 LYS   B HG2  1 
ATOM   4124 H  HG3  . LYS   B 1 110 ? 31.15610 -8.62518  14.30605  1.000 21.02578 ?  113 LYS   B HG3  1 
ATOM   4125 H  HD2  . LYS   B 1 110 ? 29.45630 -10.11037 14.60464  1.000 26.89559 ?  113 LYS   B HD2  1 
ATOM   4126 H  HD3  . LYS   B 1 110 ? 29.17859 -8.90587  15.60338  1.000 26.89559 ?  113 LYS   B HD3  1 
ATOM   4127 H  HE2  . LYS   B 1 110 ? 27.65601 -8.01999  14.00322  1.000 32.63841 ?  113 LYS   B HE2  1 
ATOM   4128 H  HE3  . LYS   B 1 110 ? 27.84742 -9.34959  13.15414  1.000 32.63841 ?  113 LYS   B HE3  1 
ATOM   4129 H  HZ1  . LYS   B 1 110 ? 25.98645 -9.50293  14.45460  1.000 39.65174 ?  113 LYS   B HZ1  1 
ATOM   4130 H  HZ2  . LYS   B 1 110 ? 26.93277 -10.50706 14.89567  1.000 39.65174 ?  113 LYS   B HZ2  1 
ATOM   4131 H  HZ3  . LYS   B 1 110 ? 26.75369 -9.29295  15.66521  1.000 39.65174 ?  113 LYS   B HZ3  1 
ATOM   4132 N  N    . PHE   B 1 111 ? 32.93825 -5.99095  14.74332  1.000 12.25591 ?  114 PHE   B N    1 
ATOM   4133 C  CA   . PHE   B 1 111 ? 34.16584 -6.56012  15.27023  1.000 11.89890 ?  114 PHE   B CA   1 
ATOM   4134 C  C    . PHE   B 1 111 ? 33.80377 -7.69574  16.21519  1.000 12.24981 ?  114 PHE   B C    1 
ATOM   4135 O  O    . PHE   B 1 111 ? 32.81274 -7.62336  16.95710  1.000 13.53696 ?  114 PHE   B O    1 
ATOM   4136 C  CB   . PHE   B 1 111 ? 34.96353 -5.52459  16.07134  1.000 12.25908 ?  114 PHE   B CB   1 
ATOM   4137 C  CG   . PHE   B 1 111 ? 35.34186 -4.31859  15.27101  1.000 11.99558 ?  114 PHE   B CG   1 
ATOM   4138 C  CD1  . PHE   B 1 111 ? 36.45552 -4.33959  14.45594  1.000 12.60060 ?  114 PHE   B CD1  1 
ATOM   4139 C  CD2  . PHE   B 1 111 ? 34.57607 -3.17261  15.30624  1.000 12.69822 ?  114 PHE   B CD2  1 
ATOM   4140 C  CE1  . PHE   B 1 111 ? 36.80806 -3.22837  13.70626  1.000 13.21462 ?  114 PHE   B CE1  1 
ATOM   4141 C  CE2  . PHE   B 1 111 ? 34.91265 -2.06605  14.54339  1.000 13.03760 ?  114 PHE   B CE2  1 
ATOM   4142 C  CZ   . PHE   B 1 111 ? 36.03689 -2.09313  13.76054  1.000 13.03936 ?  114 PHE   B CZ   1 
ATOM   4143 H  H    . PHE   B 1 111 ? 32.57756 -5.41577  15.27122  1.000 14.70709 ?  114 PHE   B H    1 
ATOM   4144 H  HA   . PHE   B 1 111 ? 34.71479 -6.87780  14.53631  1.000 14.27868 ?  114 PHE   B HA   1 
ATOM   4145 H  HB2  . PHE   B 1 111 ? 34.42592 -5.22715  16.82195  1.000 14.71090 ?  114 PHE   B HB2  1 
ATOM   4146 H  HB3  . PHE   B 1 111 ? 35.78063 -5.93775  16.39156  1.000 14.71090 ?  114 PHE   B HB3  1 
ATOM   4147 H  HD1  . PHE   B 1 111 ? 36.97587 -5.10897  14.40918  1.000 15.12073 ?  114 PHE   B HD1  1 
ATOM   4148 H  HD2  . PHE   B 1 111 ? 33.82235 -3.14191  15.85016  1.000 15.23786 ?  114 PHE   B HD2  1 
ATOM   4149 H  HE1  . PHE   B 1 111 ? 37.56562 -3.25143  13.16731  1.000 15.85754 ?  114 PHE   B HE1  1 
ATOM   4150 H  HE2  . PHE   B 1 111 ? 34.37654 -1.30637  14.56266  1.000 15.64512 ?  114 PHE   B HE2  1 
ATOM   4151 H  HZ   . PHE   B 1 111 ? 36.27766 -1.34312  13.26616  1.000 15.64723 ?  114 PHE   B HZ   1 
ATOM   4152 N  N    A GLN   B 1 112 ? 34.58014 -8.76874  16.15725  0.469 12.80103 ?  115 GLN   B N    1 
ATOM   4153 N  N    B GLN   B 1 112 ? 34.66178 -8.70721  16.23181  0.531 12.10980 ?  115 GLN   B N    1 
ATOM   4154 C  CA   A GLN   B 1 112 ? 34.54462 -9.81215  17.17300  0.469 13.74547 ?  115 GLN   B CA   1 
ATOM   4155 C  CA   B GLN   B 1 112 ? 34.55947 -9.84002  17.14338  0.531 13.47392 ?  115 GLN   B CA   1 
ATOM   4156 C  C    A GLN   B 1 112 ? 35.87270 -9.77423  17.91195  0.469 13.00218 ?  115 GLN   B C    1 
ATOM   4157 C  C    B GLN   B 1 112 ? 35.87238 -9.92132  17.90794  0.531 13.86673 ?  115 GLN   B C    1 
ATOM   4158 O  O    A GLN   B 1 112 ? 36.93528 -9.68511  17.29044  0.469 14.17617 ?  115 GLN   B O    1 
ATOM   4159 O  O    B GLN   B 1 112 ? 36.92937 -10.11376 17.30133  0.531 14.27509 ?  115 GLN   B O    1 
ATOM   4160 C  CB   A GLN   B 1 112 ? 34.27912 -11.18822 16.56257  0.469 15.73034 ?  115 GLN   B CB   1 
ATOM   4161 C  CB   B GLN   B 1 112 ? 34.30784 -11.11630 16.34199  0.531 15.54405 ?  115 GLN   B CB   1 
ATOM   4162 C  CG   A GLN   B 1 112 ? 34.12787 -12.30481 17.59718  0.469 16.47560 ?  115 GLN   B CG   1 
ATOM   4163 C  CG   B GLN   B 1 112 ? 34.17507 -12.37492 17.16104  0.531 19.10972 ?  115 GLN   B CG   1 
ATOM   4164 C  CD   A GLN   B 1 112 ? 35.40500 -13.11200 17.76287  0.469 16.43508 ?  115 GLN   B CD   1 
ATOM   4165 C  CD   B GLN   B 1 112 ? 34.23320 -13.62177 16.30206  0.531 24.35441 ?  115 GLN   B CD   1 
ATOM   4166 O  OE1  A GLN   B 1 112 ? 36.23290 -13.14132 16.85207  0.469 17.78092 ?  115 GLN   B OE1  1 
ATOM   4167 O  OE1  B GLN   B 1 112 ? 33.46106 -13.77356 15.35724  0.531 26.50605 ?  115 GLN   B OE1  1 
ATOM   4168 N  NE2  A GLN   B 1 112 ? 35.58024 -13.76911 18.92606  0.469 16.40588 ?  115 GLN   B NE2  1 
ATOM   4169 N  NE2  B GLN   B 1 112 ? 35.17157 -14.50996 16.60981  0.531 28.67574 ?  115 GLN   B NE2  1 
ATOM   4170 H  H    A GLN   B 1 112 ? 35.14642 -8.91774  15.52738  0.469 15.36123 ?  115 GLN   B H    1 
ATOM   4171 H  H    B GLN   B 1 112 ? 35.33835 -8.76233  15.70378  0.531 14.53176 ?  115 GLN   B H    1 
ATOM   4172 H  HA   A GLN   B 1 112 ? 33.82585 -9.65332  17.80469  0.469 16.49456 ?  115 GLN   B HA   1 
ATOM   4173 H  HA   B GLN   B 1 112 ? 33.83649 -9.72626  17.77999  0.531 16.16870 ?  115 GLN   B HA   1 
ATOM   4174 H  HB2  A GLN   B 1 112 ? 33.45737 -11.14775 16.04877  0.469 18.87641 ?  115 GLN   B HB2  1 
ATOM   4175 H  HB2  B GLN   B 1 112 ? 33.48301 -11.00681 15.84342  0.531 18.65286 ?  115 GLN   B HB2  1 
ATOM   4176 H  HB3  A GLN   B 1 112 ? 35.02158 -11.42044 15.98315  0.469 18.87641 ?  115 GLN   B HB3  1 
ATOM   4177 H  HB3  B GLN   B 1 112 ? 35.05016 -11.24525 15.73107  0.531 18.65286 ?  115 GLN   B HB3  1 
ATOM   4178 H  HG2  A GLN   B 1 112 ? 33.90366 -11.91423 18.45629  0.469 19.77072 ?  115 GLN   B HG2  1 
ATOM   4179 H  HG2  B GLN   B 1 112 ? 34.90095 -12.41541 17.80318  0.531 22.93166 ?  115 GLN   B HG2  1 
ATOM   4180 H  HG3  A GLN   B 1 112 ? 33.42362 -12.90838 17.31320  0.469 19.77072 ?  115 GLN   B HG3  1 
ATOM   4181 H  HG3  B GLN   B 1 112 ? 33.32272 -12.36554 17.62398  0.531 22.93166 ?  115 GLN   B HG3  1 
ATOM   4182 H  HE21 A GLN   B 1 112 ? 34.98087 -13.72213 19.54100  0.469 19.68706 ?  115 GLN   B HE21 1 
ATOM   4183 H  HE21 B GLN   B 1 112 ? 35.70566 -14.36095 17.26719  0.531 34.41088 ?  115 GLN   B HE21 1 
ATOM   4184 H  HE22 A GLN   B 1 112 ? 36.29146 -14.23549 19.05354  0.469 19.68706 ?  115 GLN   B HE22 1 
ATOM   4185 H  HE22 B GLN   B 1 112 ? 35.24507 -15.23407 16.15170  0.531 34.41088 ?  115 GLN   B HE22 1 
ATOM   4186 N  N    . VAL   B 1 113 ? 35.81566 -9.77743  19.23139  1.000 12.89166 ?  116 VAL   B N    1 
ATOM   4187 C  CA   . VAL   B 1 113 ? 37.01830 -9.70039  20.04721  1.000 12.43304 ?  116 VAL   B CA   1 
ATOM   4188 C  C    . VAL   B 1 113 ? 37.10251 -10.93105 20.92230  1.000 12.68007 ?  116 VAL   B C    1 
ATOM   4189 O  O    . VAL   B 1 113 ? 36.12998 -11.27870 21.59461  1.000 14.55026 ?  116 VAL   B O    1 
ATOM   4190 C  CB   . VAL   B 1 113 ? 37.05120 -8.42634  20.90622  1.000 13.29899 ?  116 VAL   B CB   1 
ATOM   4191 C  CG1  . VAL   B 1 113 ? 38.34506 -8.37900  21.68568  1.000 14.43531 ?  116 VAL   B CG1  1 
ATOM   4192 C  CG2  . VAL   B 1 113 ? 36.86077 -7.20348  20.03442  1.000 14.38626 ?  116 VAL   B CG2  1 
ATOM   4193 H  H    . VAL   B 1 113 ? 35.08547 -9.72172  19.68231  1.000 15.46999 ?  116 VAL   B H    1 
ATOM   4194 H  HA   . VAL   B 1 113 ? 37.78663 -9.69432  19.45517  1.000 14.91964 ?  116 VAL   B HA   1 
ATOM   4195 H  HB   . VAL   B 1 113 ? 36.32255 -8.43097  21.54649  1.000 15.95879 ?  116 VAL   B HB   1 
ATOM   4196 H  HG11 . VAL   B 1 113 ? 38.46731 -7.48463  22.04073  1.000 17.32237 ?  116 VAL   B HG11 1 
ATOM   4197 H  HG12 . VAL   B 1 113 ? 38.29964 -9.02000  22.41229  1.000 17.32237 ?  116 VAL   B HG12 1 
ATOM   4198 H  HG13 . VAL   B 1 113 ? 39.07936 -8.60269  21.09266  1.000 17.32237 ?  116 VAL   B HG13 1 
ATOM   4199 H  HG21 . VAL   B 1 113 ? 36.96928 -6.40778  20.57847  1.000 17.26351 ?  116 VAL   B HG21 1 
ATOM   4200 H  HG22 . VAL   B 1 113 ? 37.52436 -7.21352  19.32700  1.000 17.26351 ?  116 VAL   B HG22 1 
ATOM   4201 H  HG23 . VAL   B 1 113 ? 35.96948 -7.22383  19.65219  1.000 17.26351 ?  116 VAL   B HG23 1 
ATOM   4202 N  N    . ALA   B 1 114 ? 38.26141 -11.57109 20.91771  1.000 12.75267 ?  117 ALA   B N    1 
ATOM   4203 C  CA   . ALA   B 1 114 ? 38.57803 -12.68926 21.78113  1.000 13.40714 ?  117 ALA   B CA   1 
ATOM   4204 C  C    . ALA   B 1 114 ? 39.79922 -12.31404 22.60066  1.000 14.24616 ?  117 ALA   B C    1 
ATOM   4205 O  O    . ALA   B 1 114 ? 40.71734 -11.65582 22.11023  1.000 15.99053 ?  117 ALA   B O    1 
ATOM   4206 C  CB   . ALA   B 1 114 ? 38.91784 -13.93584 20.97688  1.000 16.29378 ?  117 ALA   B CB   1 
ATOM   4207 H  H    . ALA   B 1 114 ? 38.91194 -11.36304 20.39510  1.000 15.30320 ?  117 ALA   B H    1 
ATOM   4208 H  HA   . ALA   B 1 114 ? 37.82299 -12.88824 22.35664  1.000 16.08856 ?  117 ALA   B HA   1 
ATOM   4209 H  HB1  . ALA   B 1 114 ? 39.13101 -14.65789 21.58852  1.000 19.55254 ?  117 ALA   B HB1  1 
ATOM   4210 H  HB2  . ALA   B 1 114 ? 38.15272 -14.17864 20.43233  1.000 19.55254 ?  117 ALA   B HB2  1 
ATOM   4211 H  HB3  . ALA   B 1 114 ? 39.68133 -13.74699 20.40914  1.000 19.55254 ?  117 ALA   B HB3  1 
ATOM   4212 N  N    . VAL   B 1 115 ? 39.83136 -12.80032 23.82838  1.000 14.85580 ?  118 VAL   B N    1 
ATOM   4213 C  CA   . VAL   B 1 115 ? 40.95728 -12.59715 24.72700  1.000 16.10802 ?  118 VAL   B CA   1 
ATOM   4214 C  C    . VAL   B 1 115 ? 41.39983 -13.95922 25.21847  1.000 17.47733 ?  118 VAL   B C    1 
ATOM   4215 O  O    . VAL   B 1 115 ? 40.58149 -14.73838 25.71430  1.000 17.70706 ?  118 VAL   B O    1 
ATOM   4216 C  CB   . VAL   B 1 115 ? 40.58312 -11.65335 25.88456  1.000 17.58765 ?  118 VAL   B CB   1 
ATOM   4217 C  CG1  . VAL   B 1 115 ? 41.74872 -11.47857 26.85824  1.000 21.08688 ?  118 VAL   B CG1  1 
ATOM   4218 C  CG2  . VAL   B 1 115 ? 40.11474 -10.29927 25.30562  1.000 18.51074 ?  118 VAL   B CG2  1 
ATOM   4219 H  H    . VAL   B 1 115 ? 39.19579 -13.26454 24.17500  1.000 17.82697 ?  118 VAL   B H    1 
ATOM   4220 H  HA   . VAL   B 1 115 ? 41.70626 -12.19711 24.25806  1.000 19.32962 ?  118 VAL   B HA   1 
ATOM   4221 H  HB   . VAL   B 1 115 ? 39.85506 -12.03951 26.39613  1.000 21.10518 ?  118 VAL   B HB   1 
ATOM   4222 H  HG11 . VAL   B 1 115 ? 41.63790 -10.64203 27.33659  1.000 25.30426 ?  118 VAL   B HG11 1 
ATOM   4223 H  HG12 . VAL   B 1 115 ? 41.75124 -12.21966 27.48409  1.000 25.30426 ?  118 VAL   B HG12 1 
ATOM   4224 H  HG13 . VAL   B 1 115 ? 42.57934 -11.46572 26.35744  1.000 25.30426 ?  118 VAL   B HG13 1 
ATOM   4225 H  HG21 . VAL   B 1 115 ? 39.91218 -9.69595  26.03765  1.000 22.21289 ?  118 VAL   B HG21 1 
ATOM   4226 H  HG22 . VAL   B 1 115 ? 40.82368 -9.92799  24.75748  1.000 22.21289 ?  118 VAL   B HG22 1 
ATOM   4227 H  HG23 . VAL   B 1 115 ? 39.32120 -10.44372 24.76679  1.000 22.21289 ?  118 VAL   B HG23 1 
ATOM   4228 N  N    . ASN   B 1 116 ? 42.68728 -14.25197 25.03713  1.000 19.81690 ?  119 ASN   B N    1 
ATOM   4229 C  CA   A ASN   B 1 116 ? 43.27225 -15.52957 25.45842  0.598 21.58669 ?  119 ASN   B CA   1 
ATOM   4230 C  CA   B ASN   B 1 116 ? 43.27331 -15.52060 25.46174  0.402 22.05443 ?  119 ASN   B CA   1 
ATOM   4231 C  C    . ASN   B 1 116 ? 42.51353 -16.71123 24.88170  1.000 21.75912 ?  119 ASN   B C    1 
ATOM   4232 O  O    . ASN   B 1 116 ? 42.32181 -17.73634 25.53556  1.000 22.81819 ?  119 ASN   B O    1 
ATOM   4233 C  CB   A ASN   B 1 116 ? 43.37091 -15.65464 26.97245  0.598 23.00022 ?  119 ASN   B CB   1 
ATOM   4234 C  CB   B ASN   B 1 116 ? 43.38520 -15.57674 26.98499  0.402 24.46506 ?  119 ASN   B CB   1 
ATOM   4235 C  CG   A ASN   B 1 116 ? 44.41613 -14.77256 27.53515  0.598 23.06440 ?  119 ASN   B CG   1 
ATOM   4236 C  CG   B ASN   B 1 116 ? 44.09358 -14.35490 27.53891  0.402 26.54853 ?  119 ASN   B CG   1 
ATOM   4237 O  OD1  A ASN   B 1 116 ? 44.80832 -13.78397 26.92122  0.598 24.85283 ?  119 ASN   B OD1  1 
ATOM   4238 O  OD1  B ASN   B 1 116 ? 45.06842 -13.89010 26.94635  0.402 26.09226 ?  119 ASN   B OD1  1 
ATOM   4239 N  ND2  A ASN   B 1 116 ? 44.87181 -15.10300 28.71403  0.598 22.17547 ?  119 ASN   B ND2  1 
ATOM   4240 N  ND2  B ASN   B 1 116 ? 43.59133 -13.80303 28.64689  0.402 26.07632 ?  119 ASN   B ND2  1 
ATOM   4241 H  H    . ASN   B 1 116 ? 43.25232 -13.71981 24.66682  1.000 23.78027 ?  119 ASN   B H    1 
ATOM   4242 H  HA   . ASN   B 1 116 ? 44.17521 -15.54979 25.10465  1.000 26.46532 ?  119 ASN   B HA   1 
ATOM   4243 H  HB2  A ASN   B 1 116 ? 42.52065 -15.40800 27.36885  0.598 27.60026 ?  119 ASN   B HB2  1 
ATOM   4244 H  HB2  B ASN   B 1 116 ? 42.49587 -15.61426 27.37046  0.402 29.35807 ?  119 ASN   B HB2  1 
ATOM   4245 H  HB3  A ASN   B 1 116 ? 43.59116 -16.57073 27.20304  0.598 27.60026 ?  119 ASN   B HB3  1 
ATOM   4246 H  HB3  B ASN   B 1 116 ? 43.89095 -16.36409 27.24035  0.402 29.35807 ?  119 ASN   B HB3  1 
ATOM   4247 H  HD21 A ASN   B 1 116 ? 44.56289 -15.79822 29.11507  0.598 26.61057 ?  119 ASN   B HD21 1 
ATOM   4248 H  HD21 B ASN   B 1 116 ? 42.89292 -14.14154 29.01733  0.402 31.29158 ?  119 ASN   B HD21 1 
ATOM   4249 H  HD22 A ASN   B 1 116 ? 45.48071 -14.62530 29.08906  0.598 26.61057 ?  119 ASN   B HD22 1 
ATOM   4250 H  HD22 B ASN   B 1 116 ? 43.96640 -13.10923 28.98976  0.402 31.29158 ?  119 ASN   B HD22 1 
ATOM   4251 N  N    . GLY   B 1 117 ? 42.09870 -16.56953 23.62911  1.000 20.61581 ?  120 GLY   B N    1 
ATOM   4252 C  CA   . GLY   B 1 117 ? 41.47955 -17.63061 22.88629  1.000 21.81534 ?  120 GLY   B CA   1 
ATOM   4253 C  C    . GLY   B 1 117 ? 40.01052 -17.80824 23.13101  1.000 20.72012 ?  120 GLY   B C    1 
ATOM   4254 O  O    . GLY   B 1 117 ? 39.42353 -18.73828 22.55572  1.000 25.43832 ?  120 GLY   B O    1 
ATOM   4255 H  H    . GLY   B 1 117 ? 42.17179 -15.83914 23.18101  1.000 24.73897 ?  120 GLY   B H    1 
ATOM   4256 H  HA2  . GLY   B 1 117 ? 41.60157 -17.45753 21.93969  1.000 26.17841 ?  120 GLY   B HA2  1 
ATOM   4257 H  HA3  . GLY   B 1 117 ? 41.91899 -18.46484 23.11401  1.000 26.17841 ?  120 GLY   B HA3  1 
ATOM   4258 N  N    . LYS   B 1 118 ? 39.38680 -16.94233 23.93090  1.000 16.98644 ?  121 LYS   B N    1 
ATOM   4259 C  CA   A LYS   B 1 118 ? 37.98595 -17.08273 24.29514  0.586 16.69418 ?  121 LYS   B CA   1 
ATOM   4260 C  CA   B LYS   B 1 118 ? 37.98518 -17.08408 24.28304  0.414 16.36789 ?  121 LYS   B CA   1 
ATOM   4261 C  C    . LYS   B 1 118 ? 37.20347 -15.85795 23.85326  1.000 16.01293 ?  121 LYS   B C    1 
ATOM   4262 O  O    . LYS   B 1 118 ? 37.63504 -14.72058 24.06082  1.000 15.82827 ?  121 LYS   B O    1 
ATOM   4263 C  CB   A LYS   B 1 118 ? 37.84292 -17.25414 25.80246  0.586 16.99483 ?  121 LYS   B CB   1 
ATOM   4264 C  CB   B LYS   B 1 118 ? 37.83476 -17.28234 25.76919  0.414 16.01768 ?  121 LYS   B CB   1 
ATOM   4265 C  CG   A LYS   B 1 118 ? 38.52141 -18.51662 26.32511  0.586 19.01552 ?  121 LYS   B CG   1 
ATOM   4266 C  CG   B LYS   B 1 118 ? 38.52067 -18.54305 26.21429  0.414 16.67386 ?  121 LYS   B CG   1 
ATOM   4267 C  CD   A LYS   B 1 118 ? 38.36008 -18.67503 27.83599  0.586 20.88357 ?  121 LYS   B CD   1 
ATOM   4268 C  CD   B LYS   B 1 118 ? 38.36148 -18.77129 27.68587  0.414 17.63895 ?  121 LYS   B CD   1 
ATOM   4269 C  CE   A LYS   B 1 118 ? 38.88061 -20.01607 28.35059  0.586 21.79826 ?  121 LYS   B CE   1 
ATOM   4270 C  CE   B LYS   B 1 118 ? 39.18773 -19.93577 28.14139  0.414 18.32727 ?  121 LYS   B CE   1 
ATOM   4271 N  NZ   A LYS   B 1 118 ? 40.36160 -20.10120 28.28555  0.586 21.12168 ?  121 LYS   B NZ   1 
ATOM   4272 N  NZ   B LYS   B 1 118 ? 39.45059 -19.76347 29.57317  0.414 17.80198 ?  121 LYS   B NZ   1 
ATOM   4273 H  H    . LYS   B 1 118 ? 39.76853 -16.25428 24.27798  1.000 20.38373 ?  121 LYS   B H    1 
ATOM   4274 H  HA   . LYS   B 1 118 ? 37.61774 -17.85664 23.84084  1.000 19.64147 ?  121 LYS   B HA   1 
ATOM   4275 H  HB2  A LYS   B 1 118 ? 38.24675 -16.49170 26.24575  0.586 20.39380 ?  121 LYS   B HB2  1 
ATOM   4276 H  HB2  B LYS   B 1 118 ? 38.23451 -16.53245 26.23692  0.414 19.22121 ?  121 LYS   B HB2  1 
ATOM   4277 H  HB3  A LYS   B 1 118 ? 36.90033 -17.30655 26.02533  0.586 20.39380 ?  121 LYS   B HB3  1 
ATOM   4278 H  HB3  B LYS   B 1 118 ? 36.89309 -17.34863 25.99227  0.414 19.22121 ?  121 LYS   B HB3  1 
ATOM   4279 H  HG2  A LYS   B 1 118 ? 38.12604 -19.29170 25.89633  0.586 22.81863 ?  121 LYS   B HG2  1 
ATOM   4280 H  HG2  B LYS   B 1 118 ? 38.13517 -19.30000 25.74596  0.414 20.00863 ?  121 LYS   B HG2  1 
ATOM   4281 H  HG3  A LYS   B 1 118 ? 39.46972 -18.47471 26.12546  0.586 22.81863 ?  121 LYS   B HG3  1 
ATOM   4282 H  HG3  B LYS   B 1 118 ? 39.46833 -18.47880 26.01754  0.414 20.00863 ?  121 LYS   B HG3  1 
ATOM   4283 H  HD2  A LYS   B 1 118 ? 38.85543 -17.97061 28.28244  0.586 25.06028 ?  121 LYS   B HD2  1 
ATOM   4284 H  HD2  B LYS   B 1 118 ? 38.65158 -17.98157 28.16865  0.414 21.16674 ?  121 LYS   B HD2  1 
ATOM   4285 H  HD3  A LYS   B 1 118 ? 37.41875 -18.61296 28.06169  0.586 25.06028 ?  121 LYS   B HD3  1 
ATOM   4286 H  HD3  B LYS   B 1 118 ? 37.43083 -18.95868 27.88505  0.414 21.16674 ?  121 LYS   B HD3  1 
ATOM   4287 H  HE2  A LYS   B 1 118 ? 38.61122 -20.12916 29.27554  0.586 26.15791 ?  121 LYS   B HE2  1 
ATOM   4288 H  HE2  B LYS   B 1 118 ? 38.70442 -20.76508 28.00154  0.414 21.99273 ?  121 LYS   B HE2  1 
ATOM   4289 H  HE3  A LYS   B 1 118 ? 38.51218 -20.73074 27.80799  0.586 26.15791 ?  121 LYS   B HE3  1 
ATOM   4290 H  HE3  B LYS   B 1 118 ? 40.03013 -19.95766 27.66099  0.414 21.99273 ?  121 LYS   B HE3  1 
ATOM   4291 H  HZ1  A LYS   B 1 118 ? 40.62438 -20.19331 27.44023  0.586 25.34602 ?  121 LYS   B HZ1  1 
ATOM   4292 H  HZ1  B LYS   B 1 118 ? 39.96566 -19.04961 29.70435  0.414 21.36237 ?  121 LYS   B HZ1  1 
ATOM   4293 H  HZ2  A LYS   B 1 118 ? 40.64715 -20.80151 28.75472  0.586 25.34602 ?  121 LYS   B HZ2  1 
ATOM   4294 H  HZ2  B LYS   B 1 118 ? 39.86542 -20.48205 29.89513  0.414 21.36237 ?  121 LYS   B HZ2  1 
ATOM   4295 H  HZ3  A LYS   B 1 118 ? 40.72410 -19.36112 28.62169  0.586 25.34602 ?  121 LYS   B HZ3  1 
ATOM   4296 H  HZ3  B LYS   B 1 118 ? 38.68444 -19.65141 30.01198  0.414 21.36237 ?  121 LYS   B HZ3  1 
ATOM   4297 N  N    . HIS   B 1 119 ? 36.05260 -16.09442 23.25798  1.000 17.00666 ?  122 HIS   B N    1 
ATOM   4298 C  CA   . HIS   B 1 119 ? 35.22463 -14.98842 22.81608  1.000 16.03516 ?  122 HIS   B CA   1 
ATOM   4299 C  C    . HIS   B 1 119 ? 34.90638 -14.05130 23.96968  1.000 15.86059 ?  122 HIS   B C    1 
ATOM   4300 O  O    . HIS   B 1 119 ? 34.53217 -14.49461 25.05837  1.000 18.51852 ?  122 HIS   B O    1 
ATOM   4301 C  CB   . HIS   B 1 119 ? 33.92321 -15.52747 22.25747  1.000 19.13485 ?  122 HIS   B CB   1 
ATOM   4302 C  CG   . HIS   B 1 119 ? 32.97546 -14.44345 21.89511  1.000 19.64437 ?  122 HIS   B CG   1 
ATOM   4303 N  ND1  . HIS   B 1 119 ? 33.22313 -13.57681 20.85669  1.000 21.38150 ?  122 HIS   B ND1  1 
ATOM   4304 C  CD2  . HIS   B 1 119 ? 31.81877 -14.03531 22.46196  1.000 21.98434 ?  122 HIS   B CD2  1 
ATOM   4305 C  CE1  . HIS   B 1 119 ? 32.24715 -12.69096 20.78456  1.000 21.56348 ?  122 HIS   B CE1  1 
ATOM   4306 N  NE2  . HIS   B 1 119 ? 31.38182 -12.94606 21.74817  1.000 22.28660 ?  122 HIS   B NE2  1 
ATOM   4307 H  H    . HIS   B 1 119 ? 35.72973 -16.87542 23.09862  1.000 20.40799 ?  122 HIS   B H    1 
ATOM   4308 H  HA   . HIS   B 1 119 ? 35.69880 -14.49056 22.13182  1.000 19.24219 ?  122 HIS   B HA   1 
ATOM   4309 H  HB2  . HIS   B 1 119 ? 34.11046 -16.04508 21.45877  1.000 22.96183 ?  122 HIS   B HB2  1 
ATOM   4310 H  HB3  . HIS   B 1 119 ? 33.49936 -16.08922 22.92506  1.000 22.96183 ?  122 HIS   B HB3  1 
ATOM   4311 H  HD2  . HIS   B 1 119 ? 31.39782 -14.41948 23.19688  1.000 26.38121 ?  122 HIS   B HD2  1 
ATOM   4312 H  HE1  . HIS   B 1 119 ? 32.18054 -12.00415 20.16106  1.000 25.87618 ?  122 HIS   B HE1  1 
ATOM   4313 H  HE2  . HIS   B 1 119 ? 30.66167 -12.50249 21.90377  1.000 26.74392 ?  122 HIS   B HE2  1 
ATOM   4314 N  N    . THR   B 1 120 ? 35.01755 -12.74634 23.71561  1.000 14.38839 ?  123 THR   B N    1 
ATOM   4315 C  CA   . THR   B 1 120 ? 34.75761 -11.71807 24.71344  1.000 14.64813 ?  123 THR   B CA   1 
ATOM   4316 C  C    . THR   B 1 120 ? 33.55477 -10.84959 24.37705  1.000 14.84019 ?  123 THR   B C    1 
ATOM   4317 O  O    . THR   B 1 120 ? 32.66698 -10.68094 25.22431  1.000 16.20725 ?  123 THR   B O    1 
ATOM   4318 C  CB   . THR   B 1 120 ? 36.00330 -10.84947 24.91018  1.000 17.03803 ?  123 THR   B CB   1 
ATOM   4319 O  OG1  . THR   B 1 120 ? 37.10067 -11.67301 25.30275  1.000 21.05158 ?  123 THR   B OG1  1 
ATOM   4320 C  CG2  . THR   B 1 120 ? 35.76714 -9.80716  25.96172  1.000 17.68835 ?  123 THR   B CG2  1 
ATOM   4321 H  H    . THR   B 1 120 ? 35.24852 -12.42766 22.95096  1.000 17.26607 ?  123 THR   B H    1 
ATOM   4322 H  HA   . THR   B 1 120 ? 34.56722 -12.15158 25.56003  1.000 17.57775 ?  123 THR   B HA   1 
ATOM   4323 H  HB   . THR   B 1 120 ? 36.21387 -10.39801 24.07787  1.000 20.44563 ?  123 THR   B HB   1 
ATOM   4324 H  HG1  . THR   B 1 120 ? 37.28904 -12.21308 24.68758  1.000 25.26190 ?  123 THR   B HG1  1 
ATOM   4325 H  HG21 . THR   B 1 120 ? 36.61278 -9.43023  26.25106  1.000 21.22602 ?  123 THR   B HG21 1 
ATOM   4326 H  HG22 . THR   B 1 120 ? 35.21119 -9.09656  25.60553  1.000 21.22602 ?  123 THR   B HG22 1 
ATOM   4327 H  HG23 . THR   B 1 120 ? 35.32067 -10.20277 26.72661  1.000 21.22602 ?  123 THR   B HG23 1 
ATOM   4328 N  N    . LEU   B 1 121 ? 33.51085 -10.27228 23.17754  1.000 14.18586 ?  124 LEU   B N    1 
ATOM   4329 C  CA   . LEU   B 1 121 ? 32.40463 -9.39643  22.83005  1.000 14.32551 ?  124 LEU   B CA   1 
ATOM   4330 C  C    . LEU   B 1 121 ? 32.31926 -9.20135  21.32398  1.000 13.44399 ?  124 LEU   B C    1 
ATOM   4331 O  O    . LEU   B 1 121 ? 33.25948 -9.49083  20.57759  1.000 13.96503 ?  124 LEU   B O    1 
ATOM   4332 C  CB   . LEU   B 1 121 ? 32.48803 -8.06086  23.58105  1.000 14.71093 ?  124 LEU   B CB   1 
ATOM   4333 C  CG   . LEU   B 1 121 ? 33.71709 -7.17129  23.34478  1.000 14.74532 ?  124 LEU   B CG   1 
ATOM   4334 C  CD1  . LEU   B 1 121 ? 33.62484 -6.37951  22.03315  1.000 15.47395 ?  124 LEU   B CD1  1 
ATOM   4335 C  CD2  . LEU   B 1 121 ? 33.93166 -6.24629  24.54312  1.000 15.47332 ?  124 LEU   B CD2  1 
ATOM   4336 H  H    . LEU   B 1 121 ? 34.10155 -10.37280 22.56064  1.000 17.02303 ?  124 LEU   B H    1 
ATOM   4337 H  HA   . LEU   B 1 121 ? 31.57679 -9.83352  23.08406  1.000 17.19062 ?  124 LEU   B HA   1 
ATOM   4338 H  HB2  . LEU   B 1 121 ? 31.71229 -7.53465  23.33158  1.000 17.65311 ?  124 LEU   B HB2  1 
ATOM   4339 H  HB3  . LEU   B 1 121 ? 32.46499 -8.25606  24.53093  1.000 17.65311 ?  124 LEU   B HB3  1 
ATOM   4340 H  HG   . LEU   B 1 121 ? 34.49513 -7.74346  23.25435  1.000 17.69438 ?  124 LEU   B HG   1 
ATOM   4341 H  HD11 . LEU   B 1 121 ? 34.26100 -5.64777  22.06058  1.000 18.56875 ?  124 LEU   B HD11 1 
ATOM   4342 H  HD12 . LEU   B 1 121 ? 33.83207 -6.97039  21.29233  1.000 18.56875 ?  124 LEU   B HD12 1 
ATOM   4343 H  HD13 . LEU   B 1 121 ? 32.72449 -6.03164  21.93693  1.000 18.56875 ?  124 LEU   B HD13 1 
ATOM   4344 H  HD21 . LEU   B 1 121 ? 34.65992 -5.63688  24.34523  1.000 18.56798 ?  124 LEU   B HD21 1 
ATOM   4345 H  HD22 . LEU   B 1 121 ? 33.11669 -5.74605  24.70584  1.000 18.56798 ?  124 LEU   B HD22 1 
ATOM   4346 H  HD23 . LEU   B 1 121 ? 34.15134 -6.78278  25.32082  1.000 18.56798 ?  124 LEU   B HD23 1 
ATOM   4347 N  N    . LEU   B 1 122 ? 31.15827 -8.69423  20.89916  1.000 13.81300 ?  125 LEU   B N    1 
ATOM   4348 C  CA   . LEU   B 1 122 ? 30.88366 -8.23364  19.55166  1.000 13.92285 ?  125 LEU   B CA   1 
ATOM   4349 C  C    . LEU   B 1 122 ? 30.57296 -6.74453  19.60955  1.000 13.36239 ?  125 LEU   B C    1 
ATOM   4350 O  O    . LEU   B 1 122 ? 30.00719 -6.25874  20.59451  1.000 15.53767 ?  125 LEU   B O    1 
ATOM   4351 C  CB   . LEU   B 1 122 ? 29.64154 -8.93631  19.00157  1.000 15.89548 ?  125 LEU   B CB   1 
ATOM   4352 C  CG   . LEU   B 1 122 ? 29.73604 -10.45271 18.90966  1.000 16.87295 ?  125 LEU   B CG   1 
ATOM   4353 C  CD1  . LEU   B 1 122 ? 28.37943 -11.03534 18.52674  1.000 19.75985 ?  125 LEU   B CD1  1 
ATOM   4354 C  CD2  . LEU   B 1 122 ? 30.79997 -10.89182 17.93108  1.000 18.42381 ?  125 LEU   B CD2  1 
ATOM   4355 H  H    . LEU   B 1 122 ? 30.47463 -8.60435  21.41313  1.000 16.57560 ?  125 LEU   B H    1 
ATOM   4356 H  HA   . LEU   B 1 122 ? 31.64520 -8.40023  18.97441  1.000 16.70742 ?  125 LEU   B HA   1 
ATOM   4357 H  HB2  . LEU   B 1 122 ? 28.89174 -8.72727  19.58036  1.000 19.07458 ?  125 LEU   B HB2  1 
ATOM   4358 H  HB3  . LEU   B 1 122 ? 29.47331 -8.60171  18.10678  1.000 19.07458 ?  125 LEU   B HB3  1 
ATOM   4359 H  HG   . LEU   B 1 122 ? 29.99315 -10.79884 19.77856  1.000 20.24754 ?  125 LEU   B HG   1 
ATOM   4360 H  HD11 . LEU   B 1 122 ? 28.43420 -12.00356 18.54798  1.000 23.71181 ?  125 LEU   B HD11 1 
ATOM   4361 H  HD12 . LEU   B 1 122 ? 27.71320 -10.72771 19.16109  1.000 23.71181 ?  125 LEU   B HD12 1 
ATOM   4362 H  HD13 . LEU   B 1 122 ? 28.14827 -10.73663 17.63330  1.000 23.71181 ?  125 LEU   B HD13 1 
ATOM   4363 H  HD21 . LEU   B 1 122 ? 30.72175 -11.84795 17.78755  1.000 22.10858 ?  125 LEU   B HD21 1 
ATOM   4364 H  HD22 . LEU   B 1 122 ? 30.67245 -10.42003 17.09320  1.000 22.10858 ?  125 LEU   B HD22 1 
ATOM   4365 H  HD23 . LEU   B 1 122 ? 31.67289 -10.68286 18.29882  1.000 22.10858 ?  125 LEU   B HD23 1 
ATOM   4366 N  N    . TYR   B 1 123 ? 30.89694 -6.02404  18.53720  1.000 12.73186 ?  126 TYR   B N    1 
ATOM   4367 C  CA   . TYR   B 1 123 ? 30.59839 -4.59708  18.45375  1.000 13.29047 ?  126 TYR   B CA   1 
ATOM   4368 C  C    . TYR   B 1 123 ? 30.23959 -4.25627  17.01324  1.000 12.90331 ?  126 TYR   B C    1 
ATOM   4369 O  O    . TYR   B 1 123 ? 31.09554 -4.33686  16.12339  1.000 12.94684 ?  126 TYR   B O    1 
ATOM   4370 C  CB   . TYR   B 1 123 ? 31.78091 -3.75999  18.90958  1.000 12.64023 ?  126 TYR   B CB   1 
ATOM   4371 C  CG   . TYR   B 1 123 ? 31.48538 -2.28300  18.98008  1.000 12.53586 ?  126 TYR   B CG   1 
ATOM   4372 C  CD1  . TYR   B 1 123 ? 30.92866 -1.72668  20.12305  1.000 13.23539 ?  126 TYR   B CD1  1 
ATOM   4373 C  CD2  . TYR   B 1 123 ? 31.77369 -1.43574  17.91987  1.000 13.09644 ?  126 TYR   B CD2  1 
ATOM   4374 C  CE1  . TYR   B 1 123 ? 30.68039 -0.36794  20.20812  1.000 13.64190 ?  126 TYR   B CE1  1 
ATOM   4375 C  CE2  . TYR   B 1 123 ? 31.52548 -0.06780  18.00439  1.000 13.56239 ?  126 TYR   B CE2  1 
ATOM   4376 C  CZ   . TYR   B 1 123 ? 30.98003 0.45272   19.15719  1.000 12.54489 ?  126 TYR   B CZ   1 
ATOM   4377 O  OH   . TYR   B 1 123 ? 30.70883 1.79230   19.31835  1.000 13.50610 ?  126 TYR   B OH   1 
ATOM   4378 H  H    . TYR   B 1 123 ? 31.29207 -6.34138  17.84238  1.000 15.27823 ?  126 TYR   B H    1 
ATOM   4379 H  HA   . TYR   B 1 123 ? 29.83349 -4.40408  19.01818  1.000 15.94857 ?  126 TYR   B HA   1 
ATOM   4380 H  HB2  . TYR   B 1 123 ? 32.04695 -4.05176  19.79558  1.000 15.16828 ?  126 TYR   B HB2  1 
ATOM   4381 H  HB3  . TYR   B 1 123 ? 32.51227 -3.88656  18.28508  1.000 15.16828 ?  126 TYR   B HB3  1 
ATOM   4382 H  HD1  . TYR   B 1 123 ? 30.71899 -2.27596  20.84363  1.000 15.88246 ?  126 TYR   B HD1  1 
ATOM   4383 H  HD2  . TYR   B 1 123 ? 32.13868 -1.78699  17.13993  1.000 15.71572 ?  126 TYR   B HD2  1 
ATOM   4384 H  HE1  . TYR   B 1 123 ? 30.30852 -0.01221  20.98276  1.000 16.37028 ?  126 TYR   B HE1  1 
ATOM   4385 H  HE2  . TYR   B 1 123 ? 31.72651 0.48995   17.28787  1.000 16.27487 ?  126 TYR   B HE2  1 
ATOM   4386 H  HH   . TYR   B 1 123 ? 31.07061 2.23476   18.70276  1.000 16.20732 ?  126 TYR   B HH   1 
ATOM   4387 N  N    . GLY   B 1 124 ? 28.98217 -3.89100  16.77844  1.000 13.66092 ?  127 GLY   B N    1 
ATOM   4388 C  CA   . GLY   B 1 124 ? 28.55868 -3.56942  15.42224  1.000 13.88341 ?  127 GLY   B CA   1 
ATOM   4389 C  C    . GLY   B 1 124 ? 29.21215 -2.30529  14.88302  1.000 12.86165 ?  127 GLY   B C    1 
ATOM   4390 O  O    . GLY   B 1 124 ? 29.42037 -1.33606  15.60817  1.000 13.47922 ?  127 GLY   B O    1 
ATOM   4391 H  H    . GLY   B 1 124 ? 28.36696 -3.82298  17.37551  1.000 16.39310 ?  127 GLY   B H    1 
ATOM   4392 H  HA2  . GLY   B 1 124 ? 28.78849 -4.30481  14.83292  1.000 16.66009 ?  127 GLY   B HA2  1 
ATOM   4393 H  HA3  . GLY   B 1 124 ? 27.59703 -3.44303  15.40931  1.000 16.66009 ?  127 GLY   B HA3  1 
ATOM   4394 N  N    . HIS   B 1 125 ? 29.49698 -2.29992  13.58321  1.000 12.85517 ?  128 HIS   B N    1 
ATOM   4395 C  CA   . HIS   B 1 125 ? 30.10893 -1.11542  13.00037  1.000 12.66085 ?  128 HIS   B CA   1 
ATOM   4396 C  C    . HIS   B 1 125 ? 29.17545 0.08457   13.05533  1.000 13.12418 ?  128 HIS   B C    1 
ATOM   4397 O  O    . HIS   B 1 125 ? 27.96680 -0.01872  12.83569  1.000 13.30055 ?  128 HIS   B O    1 
ATOM   4398 C  CB   . HIS   B 1 125 ? 30.50153 -1.33738  11.53871  1.000 13.11405 ?  128 HIS   B CB   1 
ATOM   4399 C  CG   . HIS   B 1 125 ? 31.55890 -2.36532  11.35656  1.000 13.00799 ?  128 HIS   B CG   1 
ATOM   4400 N  ND1  . HIS   B 1 125 ? 32.71804 -2.38423  12.10471  1.000 13.67749 ?  128 HIS   B ND1  1 
ATOM   4401 C  CD2  . HIS   B 1 125 ? 31.63414 -3.40307  10.49097  1.000 14.53260 ?  128 HIS   B CD2  1 
ATOM   4402 C  CE1  . HIS   B 1 125 ? 33.44974 -3.40915  11.70424  1.000 13.64565 ?  128 HIS   B CE1  1 
ATOM   4403 N  NE2  . HIS   B 1 125 ? 32.80971 -4.04850  10.74061  1.000 15.05783 ?  128 HIS   B NE2  1 
ATOM   4404 H  H    . HIS   B 1 125 ? 29.35017 -2.94804  13.03732  1.000 15.42620 ?  128 HIS   B H    1 
ATOM   4405 H  HA   . HIS   B 1 125 ? 30.90794 -0.93172  13.51877  1.000 15.19302 ?  128 HIS   B HA   1 
ATOM   4406 H  HB2  . HIS   B 1 125 ? 29.71819 -1.62670  11.04518  1.000 15.73686 ?  128 HIS   B HB2  1 
ATOM   4407 H  HB3  . HIS   B 1 125 ? 30.83363 -0.50215  11.17402  1.000 15.73686 ?  128 HIS   B HB3  1 
ATOM   4408 H  HD2  . HIS   B 1 125 ? 31.00334 -3.63280  9.84737   1.000 17.43912 ?  128 HIS   B HD2  1 
ATOM   4409 H  HE1  . HIS   B 1 125 ? 34.28238 -3.64330  12.04598  1.000 16.37478 ?  128 HIS   B HE1  1 
ATOM   4410 H  HE2  . HIS   B 1 125 ? 33.08850 -4.75509  10.33737  1.000 18.06940 ?  128 HIS   B HE2  1 
ATOM   4411 N  N    . ARG   B 1 126 ? 29.77342 1.23076   13.30275  1.000 12.53020 ?  129 ARG   B N    1 
ATOM   4412 C  CA   . ARG   B 1 126 ? 29.12507 2.52948   13.23721  1.000 12.71114 ?  129 ARG   B CA   1 
ATOM   4413 C  C    . ARG   B 1 126 ? 29.76571 3.44815   12.20656  1.000 13.46421 ?  129 ARG   B C    1 
ATOM   4414 O  O    . ARG   B 1 126 ? 29.07496 4.29088   11.61996  1.000 14.10262 ?  129 ARG   B O    1 
ATOM   4415 C  CB   . ARG   B 1 126 ? 29.12259 3.20280   14.61917  1.000 13.36684 ?  129 ARG   B CB   1 
ATOM   4416 C  CG   . ARG   B 1 126 ? 28.48741 2.35534   15.73236  1.000 13.97209 ?  129 ARG   B CG   1 
ATOM   4417 C  CD   . ARG   B 1 126 ? 28.28109 3.15001   16.99355  1.000 14.00979 ?  129 ARG   B CD   1 
ATOM   4418 N  NE   . ARG   B 1 126 ? 27.85203 2.32048   18.11583  1.000 13.99261 ?  129 ARG   B NE   1 
ATOM   4419 C  CZ   . ARG   B 1 126 ? 27.88973 2.73588   19.37471  1.000 14.39064 ?  129 ARG   B CZ   1 
ATOM   4420 N  NH1  . ARG   B 1 126 ? 28.22457 3.97095   19.67178  1.000 14.61870 ?  129 ARG   B NH1  1 
ATOM   4421 N  NH2  . ARG   B 1 126 ? 27.60068 1.88866   20.35894  1.000 15.41974 ?  129 ARG   B NH2  1 
ATOM   4422 H  H    . ARG   B 1 126 ? 30.60242 1.29002   13.52373  1.000 15.03624 ?  129 ARG   B H    1 
ATOM   4423 H  HA   . ARG   B 1 126 ? 28.19343 2.41812   12.99114  1.000 15.25336 ?  129 ARG   B HA   1 
ATOM   4424 H  HB2  . ARG   B 1 126 ? 30.03974 3.38629   14.87620  1.000 16.04021 ?  129 ARG   B HB2  1 
ATOM   4425 H  HB3  . ARG   B 1 126 ? 28.62267 4.03188   14.55911  1.000 16.04021 ?  129 ARG   B HB3  1 
ATOM   4426 H  HG2  . ARG   B 1 126 ? 27.62351 2.03066   15.43375  1.000 16.76651 ?  129 ARG   B HG2  1 
ATOM   4427 H  HG3  . ARG   B 1 126 ? 29.07023 1.60747   15.93707  1.000 16.76651 ?  129 ARG   B HG3  1 
ATOM   4428 H  HD2  . ARG   B 1 126 ? 29.11633 3.57810   17.23851  1.000 16.81175 ?  129 ARG   B HD2  1 
ATOM   4429 H  HD3  . ARG   B 1 126 ? 27.59791 3.82065   16.83728  1.000 16.81175 ?  129 ARG   B HD3  1 
ATOM   4430 H  HE   . ARG   B 1 126 ? 27.56200 1.52734   17.95332  1.000 16.79114 ?  129 ARG   B HE   1 
ATOM   4431 H  HH11 . ARG   B 1 126 ? 28.42391 4.52503   19.04499  1.000 17.54244 ?  129 ARG   B HH11 1 
ATOM   4432 H  HH12 . ARG   B 1 126 ? 28.24442 4.22540   20.49303  1.000 17.54244 ?  129 ARG   B HH12 1 
ATOM   4433 H  HH21 . ARG   B 1 126 ? 27.39028 1.07471   20.17775  1.000 18.50369 ?  129 ARG   B HH21 1 
ATOM   4434 H  HH22 . ARG   B 1 126 ? 27.62423 2.15495   21.17633  1.000 18.50369 ?  129 ARG   B HH22 1 
ATOM   4435 N  N    . ILE   B 1 127 ? 31.06814 3.29268   11.99526  1.000 13.21391 ?  130 ILE   B N    1 
ATOM   4436 C  CA   . ILE   B 1 127 ? 31.83624 3.88873   10.91796  1.000 13.45803 ?  130 ILE   B CA   1 
ATOM   4437 C  C    . ILE   B 1 127 ? 32.33193 2.73557   10.05501  1.000 13.15409 ?  130 ILE   B C    1 
ATOM   4438 O  O    . ILE   B 1 127 ? 32.70144 1.68854   10.57936  1.000 13.72939 ?  130 ILE   B O    1 
ATOM   4439 C  CB   . ILE   B 1 127 ? 33.04347 4.68273   11.46143  1.000 13.71298 ?  130 ILE   B CB   1 
ATOM   4440 C  CG1  . ILE   B 1 127 ? 32.57906 5.86015   12.31582  1.000 14.91064 ?  130 ILE   B CG1  1 
ATOM   4441 C  CG2  . ILE   B 1 127 ? 33.93582 5.15028   10.32677  1.000 16.78365 ?  130 ILE   B CG2  1 
ATOM   4442 C  CD1  . ILE   B 1 127 ? 33.68126 6.64026   12.97199  1.000 13.86947 ?  130 ILE   B CD1  1 
ATOM   4443 H  H    . ILE   B 1 127 ? 31.56358 2.80798   12.50438  1.000 15.85669 ?  130 ILE   B H    1 
ATOM   4444 H  HA   . ILE   B 1 127 ? 31.28065 4.49016   10.39787  1.000 16.14964 ?  130 ILE   B HA   1 
ATOM   4445 H  HB   . ILE   B 1 127 ? 33.56217 4.08967   12.02722  1.000 16.45558 ?  130 ILE   B HB   1 
ATOM   4446 H  HG12 . ILE   B 1 127 ? 32.08493 6.47409   11.75029  1.000 17.89277 ?  130 ILE   B HG12 1 
ATOM   4447 H  HG13 . ILE   B 1 127 ? 32.00383 5.52115   13.01944  1.000 17.89277 ?  130 ILE   B HG13 1 
ATOM   4448 H  HG21 . ILE   B 1 127 ? 34.48808 5.88327   10.64082  1.000 20.14039 ?  130 ILE   B HG21 1 
ATOM   4449 H  HG22 . ILE   B 1 127 ? 34.49676 4.41215   10.04146  1.000 20.14039 ?  130 ILE   B HG22 1 
ATOM   4450 H  HG23 . ILE   B 1 127 ? 33.37977 5.44734   9.58957   1.000 20.14039 ?  130 ILE   B HG23 1 
ATOM   4451 H  HD11 . ILE   B 1 127 ? 33.30460 7.18236   13.68273  1.000 16.64337 ?  130 ILE   B HD11 1 
ATOM   4452 H  HD12 . ILE   B 1 127 ? 34.33200 6.02089   13.33782  1.000 16.64337 ?  130 ILE   B HD12 1 
ATOM   4453 H  HD13 . ILE   B 1 127 ? 34.10271 7.20980   12.30950  1.000 16.64337 ?  130 ILE   B HD13 1 
ATOM   4454 N  N    . GLY   B 1 128 ? 32.33448 2.89758   8.73742   1.000 13.72500 ?  131 GLY   B N    1 
ATOM   4455 C  CA   . GLY   B 1 128 ? 32.82863 1.83171   7.89275   1.000 14.82943 ?  131 GLY   B CA   1 
ATOM   4456 C  C    . GLY   B 1 128 ? 34.27314 1.50884   8.21407   1.000 14.42928 ?  131 GLY   B C    1 
ATOM   4457 O  O    . GLY   B 1 128 ? 35.10287 2.41556   8.35386   1.000 14.42810 ?  131 GLY   B O    1 
ATOM   4458 H  H    . GLY   B 1 128 ? 32.06092 3.60007   8.32356   1.000 16.47000 ?  131 GLY   B H    1 
ATOM   4459 H  HA2  . GLY   B 1 128 ? 32.29378 1.03381   8.02762   1.000 17.79531 ?  131 GLY   B HA2  1 
ATOM   4460 H  HA3  . GLY   B 1 128 ? 32.76877 2.09844   6.96207   1.000 17.79531 ?  131 GLY   B HA3  1 
ATOM   4461 N  N    . PRO   B 1 129 ? 34.62159 0.22117   8.32327   1.000 14.38276 ?  132 PRO   B N    1 
ATOM   4462 C  CA   . PRO   B 1 129 ? 35.98432 -0.11667  8.75438   1.000 14.81669 ?  132 PRO   B CA   1 
ATOM   4463 C  C    . PRO   B 1 129 ? 37.04161 0.22782   7.72869   1.000 14.33342 ?  132 PRO   B C    1 
ATOM   4464 O  O    . PRO   B 1 129 ? 38.22049 0.32208   8.08852   1.000 14.75246 ?  132 PRO   B O    1 
ATOM   4465 C  CB   . PRO   B 1 129 ? 35.91038 -1.61923  9.06084   1.000 16.55979 ?  132 PRO   B CB   1 
ATOM   4466 C  CG   . PRO   B 1 129 ? 34.76822 -2.10736  8.26619   1.000 17.42573 ?  132 PRO   B CG   1 
ATOM   4467 C  CD   . PRO   B 1 129 ? 33.76917 -0.97620  8.22995   1.000 15.97159 ?  132 PRO   B CD   1 
ATOM   4468 H  HA   . PRO   B 1 129 ? 36.20101 0.33897   9.58283   1.000 17.78003 ?  132 PRO   B HA   1 
ATOM   4469 H  HB2  . PRO   B 1 129 ? 36.73421 -2.05364  8.78975   1.000 19.87175 ?  132 PRO   B HB2  1 
ATOM   4470 H  HB3  . PRO   B 1 129 ? 35.75913 -1.75698  10.00902  1.000 19.87175 ?  132 PRO   B HB3  1 
ATOM   4471 H  HG2  . PRO   B 1 129 ? 35.06584 -2.33041  7.37032   1.000 20.91088 ?  132 PRO   B HG2  1 
ATOM   4472 H  HG3  . PRO   B 1 129 ? 34.38474 -2.88959  8.69276   1.000 20.91088 ?  132 PRO   B HG3  1 
ATOM   4473 H  HD2  . PRO   B 1 129 ? 33.26953 -0.98180  7.39854   1.000 19.16590 ?  132 PRO   B HD2  1 
ATOM   4474 H  HD3  . PRO   B 1 129 ? 33.16027 -1.02753  8.98328   1.000 19.16590 ?  132 PRO   B HD3  1 
ATOM   4475 N  N    . GLU   B 1 130 ? 36.65523 0.47980   6.47911   1.000 15.44088 ?  133 GLU   B N    1 
ATOM   4476 C  CA   . GLU   B 1 130 ? 37.62980 0.90266   5.48530   1.000 15.70009 ?  133 GLU   B CA   1 
ATOM   4477 C  C    . GLU   B 1 130 ? 38.17917 2.29319   5.77640   1.000 16.22070 ?  133 GLU   B C    1 
ATOM   4478 O  O    . GLU   B 1 130 ? 39.19804 2.68344   5.19390   1.000 17.61435 ?  133 GLU   B O    1 
ATOM   4479 C  CB   . GLU   B 1 130 ? 37.00345 0.83000   4.09903   1.000 18.22212 ?  133 GLU   B CB   1 
ATOM   4480 C  CG   . GLU   B 1 130 ? 36.13300 2.01638   3.71469   1.000 19.80185 ?  133 GLU   B CG   1 
ATOM   4481 C  CD   . GLU   B 1 130 ? 34.77914 2.10283   4.38564   1.000 20.48410 ?  133 GLU   B CD   1 
ATOM   4482 O  OE1  . GLU   B 1 130 ? 34.34228 1.16688   5.08826   1.000 20.74704 ?  133 GLU   B OE1  1 
ATOM   4483 O  OE2  . GLU   B 1 130 ? 34.12510 3.14331   4.16650   1.000 22.48377 ?  133 GLU   B OE2  1 
ATOM   4484 H  H    . GLU   B 1 130 ? 35.84832 0.41383   6.18904   1.000 18.52906 ?  133 GLU   B H    1 
ATOM   4485 H  HA   . GLU   B 1 130 ? 38.38779 0.29742   5.49023   1.000 18.84011 ?  133 GLU   B HA   1 
ATOM   4486 H  HB2  . GLU   B 1 130 ? 37.71660 0.77026   3.44424   1.000 21.86654 ?  133 GLU   B HB2  1 
ATOM   4487 H  HB3  . GLU   B 1 130 ? 36.44668 0.03684   4.05646   1.000 21.86654 ?  133 GLU   B HB3  1 
ATOM   4488 H  HG2  . GLU   B 1 130 ? 36.61362 2.82867   3.93850   1.000 23.76222 ?  133 GLU   B HG2  1 
ATOM   4489 H  HG3  . GLU   B 1 130 ? 35.97448 1.97746   2.75852   1.000 23.76222 ?  133 GLU   B HG3  1 
ATOM   4490 N  N    . LYS   B 1 131 ? 37.52204 3.05171   6.65122   1.000 15.53255 ?  134 LYS   B N    1 
ATOM   4491 C  CA   . LYS   B 1 131 ? 37.97676 4.37599   7.04697   1.000 16.45511 ?  134 LYS   B CA   1 
ATOM   4492 C  C    . LYS   B 1 131 ? 39.04577 4.33599   8.12972   1.000 14.57969 ?  134 LYS   B C    1 
ATOM   4493 O  O    . LYS   B 1 131 ? 39.61902 5.37660   8.47686   1.000 16.25340 ?  134 LYS   B O    1 
ATOM   4494 C  CB   . LYS   B 1 131 ? 36.80368 5.20893   7.59129   1.000 19.58452 ?  134 LYS   B CB   1 
ATOM   4495 C  CG   . LYS   B 1 131 ? 35.65826 5.41255   6.62580   1.000 24.94340 ?  134 LYS   B CG   1 
ATOM   4496 C  CD   . LYS   B 1 131 ? 36.01844 6.46099   5.60260   1.000 29.94212 ?  134 LYS   B CD   1 
ATOM   4497 C  CE   . LYS   B 1 131 ? 34.80310 7.01462   4.88588   1.000 34.16071 ?  134 LYS   B CE   1 
ATOM   4498 N  NZ   . LYS   B 1 131 ? 33.70503 6.03183   4.78582   1.000 37.21754 ?  134 LYS   B NZ   1 
ATOM   4499 H  H    . LYS   B 1 131 ? 36.79182 2.81360   7.03811   1.000 18.63906 ?  134 LYS   B H    1 
ATOM   4500 H  HA   . LYS   B 1 131 ? 38.33428 4.81023   6.25671   1.000 19.74613 ?  134 LYS   B HA   1 
ATOM   4501 H  HB2  . LYS   B 1 131 ? 36.44713 4.76099   8.37431   1.000 23.50143 ?  134 LYS   B HB2  1 
ATOM   4502 H  HB3  . LYS   B 1 131 ? 37.13780 6.08650   7.83447   1.000 23.50143 ?  134 LYS   B HB3  1 
ATOM   4503 H  HG2  . LYS   B 1 131 ? 35.46908 4.58069   6.16414   1.000 29.93208 ?  134 LYS   B HG2  1 
ATOM   4504 H  HG3  . LYS   B 1 131 ? 34.87210 5.70925   7.11039   1.000 29.93208 ?  134 LYS   B HG3  1 
ATOM   4505 H  HD2  . LYS   B 1 131 ? 36.46657 7.19753   6.04711   1.000 35.93054 ?  134 LYS   B HD2  1 
ATOM   4506 H  HD3  . LYS   B 1 131 ? 36.60574 6.06763   4.93834   1.000 35.93054 ?  134 LYS   B HD3  1 
ATOM   4507 H  HE2  . LYS   B 1 131 ? 34.47235 7.78574   5.37260   1.000 40.99285 ?  134 LYS   B HE2  1 
ATOM   4508 H  HE3  . LYS   B 1 131 ? 35.05676 7.27393   3.98626   1.000 40.99285 ?  134 LYS   B HE3  1 
ATOM   4509 H  HZ1  . LYS   B 1 131 ? 33.03783 6.36898   4.30285   1.000 44.66105 ?  134 LYS   B HZ1  1 
ATOM   4510 H  HZ2  . LYS   B 1 131 ? 33.99728 5.28763   4.39485   1.000 44.66105 ?  134 LYS   B HZ2  1 
ATOM   4511 H  HZ3  . LYS   B 1 131 ? 33.40110 5.83125   5.59792   1.000 44.66105 ?  134 LYS   B HZ3  1 
ATOM   4512 N  N    . ILE   B 1 132 ? 39.30453 3.17417   8.71069   1.000 13.55796 ?  135 ILE   B N    1 
ATOM   4513 C  CA   . ILE   B 1 132 ? 40.25289 3.07026   9.80716   1.000 13.07457 ?  135 ILE   B CA   1 
ATOM   4514 C  C    . ILE   B 1 132 ? 41.65570 2.99938   9.23641   1.000 13.54788 ?  135 ILE   B C    1 
ATOM   4515 O  O    . ILE   B 1 132 ? 41.96181 2.10884   8.43766   1.000 16.43015 ?  135 ILE   B O    1 
ATOM   4516 C  CB   . ILE   B 1 132 ? 39.96268 1.82174   10.64851  1.000 13.23217 ?  135 ILE   B CB   1 
ATOM   4517 C  CG1  . ILE   B 1 132 ? 38.56606 1.90743   11.27510  1.000 13.92435 ?  135 ILE   B CG1  1 
ATOM   4518 C  CG2  . ILE   B 1 132 ? 41.06981 1.63783   11.69176  1.000 14.09096 ?  135 ILE   B CG2  1 
ATOM   4519 C  CD1  . ILE   B 1 132 ? 38.05226 0.61674   11.82761  1.000 13.73135 ?  135 ILE   B CD1  1 
ATOM   4520 H  H    . ILE   B 1 132 ? 38.94164 2.42735   8.48669   1.000 16.26955 ?  135 ILE   B H    1 
ATOM   4521 H  HA   . ILE   B 1 132 ? 40.18357 3.86071   10.36508  1.000 15.68949 ?  135 ILE   B HA   1 
ATOM   4522 H  HB   . ILE   B 1 132 ? 39.96136 1.03673   10.07871  1.000 15.87860 ?  135 ILE   B HB   1 
ATOM   4523 H  HG12 . ILE   B 1 132 ? 38.59327 2.54733   12.00358  1.000 16.70922 ?  135 ILE   B HG12 1 
ATOM   4524 H  HG13 . ILE   B 1 132 ? 37.94062 2.20448   10.59578  1.000 16.70922 ?  135 ILE   B HG13 1 
ATOM   4525 H  HG21 . ILE   B 1 132 ? 40.84184 0.88978   12.26565  1.000 16.90915 ?  135 ILE   B HG21 1 
ATOM   4526 H  HG22 . ILE   B 1 132 ? 41.90747 1.46148   11.23556  1.000 16.90915 ?  135 ILE   B HG22 1 
ATOM   4527 H  HG23 . ILE   B 1 132 ? 41.14464 2.44852   12.21910  1.000 16.90915 ?  135 ILE   B HG23 1 
ATOM   4528 H  HD11 . ILE   B 1 132 ? 37.13678 0.74176   12.12284  1.000 16.47762 ?  135 ILE   B HD11 1 
ATOM   4529 H  HD12 . ILE   B 1 132 ? 38.08647 -0.05986  11.13339  1.000 16.47762 ?  135 ILE   B HD12 1 
ATOM   4530 H  HD13 . ILE   B 1 132 ? 38.60795 0.35042   12.57674  1.000 16.47762 ?  135 ILE   B HD13 1 
ATOM   4531 N  N    . ASP   B 1 133 ? 42.51707 3.90168   9.66759   1.000 13.36130 ?  136 ASP   B N    1 
ATOM   4532 C  CA   . ASP   B 1 133 ? 43.89253 3.87490   9.22669   1.000 13.78474 ?  136 ASP   B CA   1 
ATOM   4533 C  C    . ASP   B 1 133 ? 44.90759 3.99625   10.35786  1.000 13.57251 ?  136 ASP   B C    1 
ATOM   4534 O  O    . ASP   B 1 133 ? 46.10119 3.96785   10.07168  1.000 14.08176 ?  136 ASP   B O    1 
ATOM   4535 C  CB   . ASP   B 1 133 ? 44.14579 4.95396   8.15744   1.000 15.22241 ?  136 ASP   B CB   1 
ATOM   4536 C  CG   . ASP   B 1 133 ? 44.01883 6.34080   8.69160   1.000 18.11216 ?  136 ASP   B CG   1 
ATOM   4537 O  OD1  . ASP   B 1 133 ? 43.80753 6.54504   9.89288   1.000 15.87852 ?  136 ASP   B OD1  1 
ATOM   4538 O  OD2  . ASP   B 1 133 ? 44.15088 7.26500   7.87681   1.000 24.25970 ?  136 ASP   B OD2  1 
ATOM   4539 H  H    . ASP   B 1 133 ? 42.32748 4.53745   10.21480  1.000 16.03356 ?  136 ASP   B H    1 
ATOM   4540 H  HA   . ASP   B 1 133 ? 44.05797 3.01917   8.80096   1.000 16.54168 ?  136 ASP   B HA   1 
ATOM   4541 H  HB2  . ASP   B 1 133 ? 45.04496 4.84837   7.80926   1.000 18.26689 ?  136 ASP   B HB2  1 
ATOM   4542 H  HB3  . ASP   B 1 133 ? 43.49867 4.84802   7.44266   1.000 18.26689 ?  136 ASP   B HB3  1 
ATOM   4543 N  N    . THR   B 1 134 ? 44.48172 4.07228   11.62401  1.000 13.40081 ?  137 THR   B N    1 
ATOM   4544 C  CA   . THR   B 1 134 ? 45.36609 4.37098   12.74273  1.000 13.36917 ?  137 THR   B CA   1 
ATOM   4545 C  C    . THR   B 1 134 ? 44.96523 3.52181   13.93889  1.000 13.15774 ?  137 THR   B C    1 
ATOM   4546 O  O    . THR   B 1 134 ? 43.77992 3.38667   14.25108  1.000 13.98071 ?  137 THR   B O    1 
ATOM   4547 C  CB   . THR   B 1 134 ? 45.27471 5.87414   13.06674  1.000 14.63638 ?  137 THR   B CB   1 
ATOM   4548 O  OG1  . THR   B 1 134 ? 45.68226 6.64297   11.92617  1.000 15.82726 ?  137 THR   B OG1  1 
ATOM   4549 C  CG2  . THR   B 1 134 ? 46.13290 6.24536   14.22717  1.000 15.96269 ?  137 THR   B CG2  1 
ATOM   4550 H  H    . THR   B 1 134 ? 43.66385 3.95090   11.86055  1.000 16.08098 ?  137 THR   B H    1 
ATOM   4551 H  HA   . THR   B 1 134 ? 46.28816 4.14725   12.54114  1.000 16.04301 ?  137 THR   B HA   1 
ATOM   4552 H  HB   . THR   B 1 134 ? 44.35528 6.07966   13.29760  1.000 17.56366 ?  137 THR   B HB   1 
ATOM   4553 H  HG1  . THR   B 1 134 ? 45.12706 6.54872   11.30289  1.000 18.99271 ?  137 THR   B HG1  1 
ATOM   4554 H  HG21 . THR   B 1 134 ? 46.12868 7.20773   14.34849  1.000 19.15523 ?  137 THR   B HG21 1 
ATOM   4555 H  HG22 . THR   B 1 134 ? 45.79877 5.82478   15.03487  1.000 19.15523 ?  137 THR   B HG22 1 
ATOM   4556 H  HG23 . THR   B 1 134 ? 47.04439 5.95148   14.07316  1.000 19.15523 ?  137 THR   B HG23 1 
ATOM   4557 N  N    . LEU   B 1 135 ? 45.97070 2.96913   14.60804  1.000 13.03886 ?  138 LEU   B N    1 
ATOM   4558 C  CA   . LEU   B 1 135 ? 45.81642 2.21528   15.84038  1.000 13.26198 ?  138 LEU   B CA   1 
ATOM   4559 C  C    . LEU   B 1 135 ? 46.39191 3.04657   16.97337  1.000 13.80178 ?  138 LEU   B C    1 
ATOM   4560 O  O    . LEU   B 1 135 ? 47.57007 3.40691   16.94589  1.000 15.62861 ?  138 LEU   B O    1 
ATOM   4561 C  CB   . LEU   B 1 135 ? 46.57787 0.90442   15.72901  1.000 14.15146 ?  138 LEU   B CB   1 
ATOM   4562 C  CG   . LEU   B 1 135 ? 46.66310 0.06061   17.00381  1.000 14.69089 ?  138 LEU   B CG   1 
ATOM   4563 C  CD1  . LEU   B 1 135 ? 45.31946 -0.33067  17.53535  1.000 15.71478 ?  138 LEU   B CD1  1 
ATOM   4564 C  CD2  . LEU   B 1 135 ? 47.49054 -1.17143  16.74414  1.000 15.41100 ?  138 LEU   B CD2  1 
ATOM   4565 H  H    . LEU   B 1 135 ? 46.79038 3.02139   14.35311  1.000 15.64663 ?  138 LEU   B H    1 
ATOM   4566 H  HA   . LEU   B 1 135 ? 44.88005 2.03656   16.01971  1.000 15.91438 ?  138 LEU   B HA   1 
ATOM   4567 H  HB2  . LEU   B 1 135 ? 46.14351 0.35990   15.05393  1.000 16.98175 ?  138 LEU   B HB2  1 
ATOM   4568 H  HB3  . LEU   B 1 135 ? 47.48715 1.10607   15.45800  1.000 16.98175 ?  138 LEU   B HB3  1 
ATOM   4569 H  HG   . LEU   B 1 135 ? 47.08385 0.60388   17.68844  1.000 17.62907 ?  138 LEU   B HG   1 
ATOM   4570 H  HD11 . LEU   B 1 135 ? 45.43959 -0.94678  18.27486  1.000 18.85774 ?  138 LEU   B HD11 1 
ATOM   4571 H  HD12 . LEU   B 1 135 ? 44.85629 0.46533   17.83990  1.000 18.85774 ?  138 LEU   B HD12 1 
ATOM   4572 H  HD13 . LEU   B 1 135 ? 44.81217 -0.75820  16.82770  1.000 18.85774 ?  138 LEU   B HD13 1 
ATOM   4573 H  HD21 . LEU   B 1 135 ? 47.55569 -1.68655  17.56347  1.000 18.49320 ?  138 LEU   B HD21 1 
ATOM   4574 H  HD22 . LEU   B 1 135 ? 47.06100 -1.70064  16.05397  1.000 18.49320 ?  138 LEU   B HD22 1 
ATOM   4575 H  HD23 . LEU   B 1 135 ? 48.37523 -0.90181  16.45168  1.000 18.49320 ?  138 LEU   B HD23 1 
ATOM   4576 N  N    . GLY   B 1 136 ? 45.55722 3.37531   17.94248  1.000 13.22676 ?  139 GLY   B N    1 
ATOM   4577 C  CA   . GLY   B 1 136 ? 45.98741 4.08570   19.13419  1.000 13.61757 ?  139 GLY   B CA   1 
ATOM   4578 C  C    . GLY   B 1 136 ? 45.86175 3.16899   20.33697  1.000 13.47831 ?  139 GLY   B C    1 
ATOM   4579 O  O    . GLY   B 1 136 ? 44.87284 2.45877   20.47431  1.000 14.45845 ?  139 GLY   B O    1 
ATOM   4580 H  H    . GLY   B 1 136 ? 44.71662 3.19391   17.93340  1.000 15.87212 ?  139 GLY   B H    1 
ATOM   4581 H  HA2  . GLY   B 1 136 ? 46.91202 4.36379   19.04117  1.000 16.34108 ?  139 GLY   B HA2  1 
ATOM   4582 H  HA3  . GLY   B 1 136 ? 45.43408 4.87025   19.27277  1.000 16.34108 ?  139 GLY   B HA3  1 
ATOM   4583 N  N    . ILE   B 1 137 ? 46.87180 3.17546   21.20560  1.000 13.45075 ?  140 ILE   B N    1 
ATOM   4584 C  CA   . ILE   B 1 137 ? 46.80804 2.44456   22.46963  1.000 13.37616 ?  140 ILE   B CA   1 
ATOM   4585 C  C    . ILE   B 1 137 ? 47.25810 3.39058   23.56207  1.000 14.44273 ?  140 ILE   B C    1 
ATOM   4586 O  O    . ILE   B 1 137 ? 48.37201 3.92476   23.50654  1.000 15.61399 ?  140 ILE   B O    1 
ATOM   4587 C  CB   . ILE   B 1 137 ? 47.64945 1.16118   22.48276  1.000 14.04014 ?  140 ILE   B CB   1 
ATOM   4588 C  CG1  . ILE   B 1 137 ? 47.22222 0.21399   21.34797  1.000 14.31793 ?  140 ILE   B CG1  1 
ATOM   4589 C  CG2  . ILE   B 1 137 ? 47.50762 0.45775   23.85007  1.000 14.94239 ?  140 ILE   B CG2  1 
ATOM   4590 C  CD1  . ILE   B 1 137 ? 48.11179 -1.00065  21.20520  1.000 15.55384 ?  140 ILE   B CD1  1 
ATOM   4591 H  H    . ILE   B 1 137 ? 47.60993 3.59950   21.08336  1.000 16.14090 ?  140 ILE   B H    1 
ATOM   4592 H  HA   . ILE   B 1 137 ? 45.88810 2.18241   22.63057  1.000 16.05139 ?  140 ILE   B HA   1 
ATOM   4593 H  HB   . ILE   B 1 137 ? 48.57829 1.40181   22.34040  1.000 16.84817 ?  140 ILE   B HB   1 
ATOM   4594 H  HG12 . ILE   B 1 137 ? 46.32066 -0.09765  21.52394  1.000 17.18151 ?  140 ILE   B HG12 1 
ATOM   4595 H  HG13 . ILE   B 1 137 ? 47.24732 0.70029   20.50905  1.000 17.18151 ?  140 ILE   B HG13 1 
ATOM   4596 H  HG21 . ILE   B 1 137 ? 47.88232 -0.43469  23.78646  1.000 17.93087 ?  140 ILE   B HG21 1 
ATOM   4597 H  HG22 . ILE   B 1 137 ? 47.98621 0.97046   24.52013  1.000 17.93087 ?  140 ILE   B HG22 1 
ATOM   4598 H  HG23 . ILE   B 1 137 ? 46.56731 0.40591   24.08250  1.000 17.93087 ?  140 ILE   B HG23 1 
ATOM   4599 H  HD11 . ILE   B 1 137 ? 47.92569 -1.43028  20.35568  1.000 18.66461 ?  140 ILE   B HD11 1 
ATOM   4600 H  HD12 . ILE   B 1 137 ? 49.03925 -0.71833  21.23693  1.000 18.66461 ?  140 ILE   B HD12 1 
ATOM   4601 H  HD13 . ILE   B 1 137 ? 47.92771 -1.61427  21.93354  1.000 18.66461 ?  140 ILE   B HD13 1 
ATOM   4602 N  N    . TYR   B 1 138 ? 46.36250 3.64476   24.50745  1.000 14.73367 ?  141 TYR   B N    1 
ATOM   4603 C  CA   . TYR   B 1 138 ? 46.54790 4.68797   25.49185  1.000 15.19905 ?  141 TYR   B CA   1 
ATOM   4604 C  C    . TYR   B 1 138 ? 46.20444 4.17120   26.87966  1.000 16.41644 ?  141 TYR   B C    1 
ATOM   4605 O  O    . TYR   B 1 138 ? 45.43108 3.23462   27.04192  1.000 15.55799 ?  141 TYR   B O    1 
ATOM   4606 C  CB   . TYR   B 1 138 ? 45.61870 5.87520   25.22154  1.000 16.89307 ?  141 TYR   B CB   1 
ATOM   4607 C  CG   . TYR   B 1 138 ? 45.59145 6.35223   23.78857  1.000 15.91745 ?  141 TYR   B CG   1 
ATOM   4608 C  CD1  . TYR   B 1 138 ? 46.58698 7.15381   23.28879  1.000 19.03497 ?  141 TYR   B CD1  1 
ATOM   4609 C  CD2  . TYR   B 1 138 ? 44.55457 6.00846   22.92750  1.000 17.05774 ?  141 TYR   B CD2  1 
ATOM   4610 C  CE1  . TYR   B 1 138 ? 46.56019 7.60089   21.98726  1.000 19.36803 ?  141 TYR   B CE1  1 
ATOM   4611 C  CE2  . TYR   B 1 138 ? 44.52100 6.47161   21.62145  1.000 16.08738 ?  141 TYR   B CE2  1 
ATOM   4612 C  CZ   . TYR   B 1 138 ? 45.53413 7.23662   21.14834  1.000 17.25619 ?  141 TYR   B CZ   1 
ATOM   4613 O  OH   . TYR   B 1 138 ? 45.50754 7.70382   19.85419  1.000 18.23447 ?  141 TYR   B OH   1 
ATOM   4614 H  H    . TYR   B 1 138 ? 45.62385 3.21352   24.59699  1.000 17.68040 ?  141 TYR   B H    1 
ATOM   4615 H  HA   . TYR   B 1 138 ? 47.47757 4.96345   25.46501  1.000 18.23886 ?  141 TYR   B HA   1 
ATOM   4616 H  HB2  . TYR   B 1 138 ? 44.71430 5.61742   25.45927  1.000 20.27168 ?  141 TYR   B HB2  1 
ATOM   4617 H  HB3  . TYR   B 1 138 ? 45.90625 6.62123   25.77077  1.000 20.27168 ?  141 TYR   B HB3  1 
ATOM   4618 H  HD1  . TYR   B 1 138 ? 47.29396 7.39991   23.84062  1.000 22.84196 ?  141 TYR   B HD1  1 
ATOM   4619 H  HD2  . TYR   B 1 138 ? 43.87088 5.45743   23.23384  1.000 20.46928 ?  141 TYR   B HD2  1 
ATOM   4620 H  HE1  . TYR   B 1 138 ? 47.24013 8.15251   21.67374  1.000 23.24163 ?  141 TYR   B HE1  1 
ATOM   4621 H  HE2  . TYR   B 1 138 ? 43.80332 6.25731   21.07017  1.000 19.30485 ?  141 TYR   B HE2  1 
ATOM   4622 H  HH   . TYR   B 1 138 ? 45.67537 7.07819   19.31938  1.000 21.88136 ?  141 TYR   B HH   1 
ATOM   4623 N  N    . GLY   B 1 139 ? 46.73435 4.83079   27.89540  1.000 17.51540 ?  142 GLY   B N    1 
ATOM   4624 C  CA   . GLY   B 1 139 ? 46.40288 4.49748   29.26340  1.000 17.93421 ?  142 GLY   B CA   1 
ATOM   4625 C  C    . GLY   B 1 139 ? 47.43825 3.61662   29.92122  1.000 18.45661 ?  142 GLY   B C    1 
ATOM   4626 O  O    . GLY   B 1 139 ? 48.60143 3.53858   29.52136  1.000 20.77618 ?  142 GLY   B O    1 
ATOM   4627 H  H    . GLY   B 1 139 ? 47.29254 5.48008   27.81513  1.000 21.01848 ?  142 GLY   B H    1 
ATOM   4628 H  HA2  . GLY   B 1 139 ? 46.32612 5.31422   29.78102  1.000 21.52105 ?  142 GLY   B HA2  1 
ATOM   4629 H  HA3  . GLY   B 1 139 ? 45.55240 4.03135   29.28098  1.000 21.52105 ?  142 GLY   B HA3  1 
ATOM   4630 N  N    . LYS   B 1 140 ? 47.00571 2.96887   30.98373  1.000 16.90010 ?  143 LYS   B N    1 
ATOM   4631 C  CA   . LYS   B 1 140 ? 47.93471 2.23623   31.83205  1.000 18.11682 ?  143 LYS   B CA   1 
ATOM   4632 C  C    . LYS   B 1 140 ? 47.96890 0.78823   31.37660  1.000 17.54928 ?  143 LYS   B C    1 
ATOM   4633 O  O    . LYS   B 1 140 ? 47.13876 -0.02399  31.79916  1.000 17.68135 ?  143 LYS   B O    1 
ATOM   4634 C  CB   . LYS   B 1 140 ? 47.54071 2.38361   33.29183  1.000 19.95940 ?  143 LYS   B CB   1 
ATOM   4635 C  CG   . LYS   B 1 140 ? 48.10672 3.61774   33.91549  1.000 27.37113 ?  143 LYS   B CG   1 
ATOM   4636 C  CD   . LYS   B 1 140 ? 49.59029 3.43357   34.23976  1.000 33.95790 ?  143 LYS   B CD   1 
ATOM   4637 C  CE   . LYS   B 1 140 ? 49.98661 4.23091   35.48018  1.000 38.55568 ?  143 LYS   B CE   1 
ATOM   4638 N  NZ   . LYS   B 1 140 ? 51.46410 4.42361   35.56288  1.000 41.68475 ?  143 LYS   B NZ   1 
ATOM   4639 H  H    . LYS   B 1 140 ? 46.18433 2.93630   31.23644  1.000 20.28012 ?  143 LYS   B H    1 
ATOM   4640 H  HA   . LYS   B 1 140 ? 48.83063 2.59222   31.72483  1.000 21.74018 ?  143 LYS   B HA   1 
ATOM   4641 H  HB2  . LYS   B 1 140 ? 46.57392 2.42985   33.35569  1.000 23.95128 ?  143 LYS   B HB2  1 
ATOM   4642 H  HB3  . LYS   B 1 140 ? 47.86966 1.61740   33.78743  1.000 23.95128 ?  143 LYS   B HB3  1 
ATOM   4643 H  HG2  . LYS   B 1 140 ? 48.01663 4.36196   33.29993  1.000 32.84536 ?  143 LYS   B HG2  1 
ATOM   4644 H  HG3  . LYS   B 1 140 ? 47.63335 3.81001   34.74002  1.000 32.84536 ?  143 LYS   B HG3  1 
ATOM   4645 H  HD2  . LYS   B 1 140 ? 49.76953 2.49534   34.40858  1.000 40.74947 ?  143 LYS   B HD2  1 
ATOM   4646 H  HD3  . LYS   B 1 140 ? 50.12483 3.74418   33.49231  1.000 40.74947 ?  143 LYS   B HD3  1 
ATOM   4647 H  HE2  . LYS   B 1 140 ? 49.56717 5.10490   35.44684  1.000 46.26681 ?  143 LYS   B HE2  1 
ATOM   4648 H  HE3  . LYS   B 1 140 ? 49.69707 3.75402   36.27368  1.000 46.26681 ?  143 LYS   B HE3  1 
ATOM   4649 H  HZ1  . LYS   B 1 140 ? 51.67378 4.85036   36.31523  1.000 50.02170 ?  143 LYS   B HZ1  1 
ATOM   4650 H  HZ2  . LYS   B 1 140 ? 51.87498 3.63418   35.55448  1.000 50.02170 ?  143 LYS   B HZ2  1 
ATOM   4651 H  HZ3  . LYS   B 1 140 ? 51.74768 4.90421   34.86956  1.000 50.02170 ?  143 LYS   B HZ3  1 
ATOM   4652 N  N    . VAL   B 1 141 ? 48.95818 0.47142   30.54130  1.000 17.26506 ?  144 VAL   B N    1 
ATOM   4653 C  CA   . VAL   B 1 141 ? 49.08617 -0.84674  29.93072  1.000 17.14803 ?  144 VAL   B CA   1 
ATOM   4654 C  C    . VAL   B 1 141 ? 50.52428 -0.99892  29.47837  1.000 17.14625 ?  144 VAL   B C    1 
ATOM   4655 O  O    . VAL   B 1 141 ? 51.21068 -0.01516  29.20910  1.000 18.86838 ?  144 VAL   B O    1 
ATOM   4656 C  CB   . VAL   B 1 141 ? 48.07251 -1.00418  28.76366  1.000 16.25317 ?  144 VAL   B CB   1 
ATOM   4657 C  CG1  . VAL   B 1 141 ? 48.38646 -0.05831  27.59793  1.000 17.18144 ?  144 VAL   B CG1  1 
ATOM   4658 C  CG2  . VAL   B 1 141 ? 47.97933 -2.45208  28.29541  1.000 17.55272 ?  144 VAL   B CG2  1 
ATOM   4659 H  H    . VAL   B 1 141 ? 49.58110 1.01668   30.30836  1.000 20.71807 ?  144 VAL   B H    1 
ATOM   4660 H  HA   . VAL   B 1 141 ? 48.90391 -1.54071  30.58348  1.000 20.57763 ?  144 VAL   B HA   1 
ATOM   4661 H  HB   . VAL   B 1 141 ? 47.19939 -0.75225  29.10292  1.000 19.50380 ?  144 VAL   B HB   1 
ATOM   4662 H  HG11 . VAL   B 1 141 ? 47.60561 0.00848   27.02634  1.000 20.61773 ?  144 VAL   B HG11 1 
ATOM   4663 H  HG12 . VAL   B 1 141 ? 48.61253 0.81578   27.95256  1.000 20.61773 ?  144 VAL   B HG12 1 
ATOM   4664 H  HG13 . VAL   B 1 141 ? 49.13518 -0.41488  27.09476  1.000 20.61773 ?  144 VAL   B HG13 1 
ATOM   4665 H  HG21 . VAL   B 1 141 ? 47.19151 -2.55388  27.73874  1.000 21.06326 ?  144 VAL   B HG21 1 
ATOM   4666 H  HG22 . VAL   B 1 141 ? 48.77505 -2.67098  27.78569  1.000 21.06326 ?  144 VAL   B HG22 1 
ATOM   4667 H  HG23 . VAL   B 1 141 ? 47.91351 -3.03114  29.07082  1.000 21.06326 ?  144 VAL   B HG23 1 
ATOM   4668 N  N    . ASN   B 1 142 ? 50.98644 -2.24389  29.40411  1.000 17.57411 ?  145 ASN   B N    1 
ATOM   4669 C  CA   . ASN   B 1 142 ? 52.22670 -2.57447  28.72786  1.000 17.55155 ?  145 ASN   B CA   1 
ATOM   4670 C  C    . ASN   B 1 142 ? 51.84549 -3.46380  27.55711  1.000 16.55937 ?  145 ASN   B C    1 
ATOM   4671 O  O    . ASN   B 1 142 ? 51.10268 -4.44316  27.72658  1.000 17.68883 ?  145 ASN   B O    1 
ATOM   4672 C  CB   . ASN   B 1 142 ? 53.19214 -3.34270  29.63244  1.000 19.63121 ?  145 ASN   B CB   1 
ATOM   4673 C  CG   . ASN   B 1 142 ? 54.09673 -2.44380  30.50186  1.000 21.17558 ?  145 ASN   B CG   1 
ATOM   4674 O  OD1  . ASN   B 1 142 ? 55.02348 -2.96024  31.11630  1.000 22.12249 ?  145 ASN   B OD1  1 
ATOM   4675 N  ND2  . ASN   B 1 142 ? 53.82555 -1.14802  30.58936  1.000 22.20724 ?  145 ASN   B ND2  1 
ATOM   4676 H  H    . ASN   B 1 142 ? 50.58743 -2.92452  29.74635  1.000 21.08893 ?  145 ASN   B H    1 
ATOM   4677 H  HA   . ASN   B 1 142 ? 52.67674 -1.76589  28.43704  1.000 21.06186 ?  145 ASN   B HA   1 
ATOM   4678 H  HB2  . ASN   B 1 142 ? 52.67588 -3.90563  30.23033  1.000 23.55745 ?  145 ASN   B HB2  1 
ATOM   4679 H  HB3  . ASN   B 1 142 ? 53.76896 -3.89005  29.07693  1.000 23.55745 ?  145 ASN   B HB3  1 
ATOM   4680 H  HD21 . ASN   B 1 142 ? 53.15346 -0.81974  30.16494  1.000 26.64869 ?  145 ASN   B HD21 1 
ATOM   4681 H  HD22 . ASN   B 1 142 ? 54.32186 -0.63637  31.07048  1.000 26.64869 ?  145 ASN   B HD22 1 
ATOM   4682 N  N    . ILE   B 1 143 ? 52.31875 -3.10241  26.37943  1.000 15.82169 ?  146 ILE   B N    1 
ATOM   4683 C  CA   . ILE   B 1 143 ? 52.05558 -3.85217  25.16391  1.000 15.29091 ?  146 ILE   B CA   1 
ATOM   4684 C  C    . ILE   B 1 143 ? 53.33967 -4.57059  24.78084  1.000 15.96301 ?  146 ILE   B C    1 
ATOM   4685 O  O    . ILE   B 1 143 ? 54.35655 -3.94639  24.44655  1.000 17.95989 ?  146 ILE   B O    1 
ATOM   4686 C  CB   . ILE   B 1 143 ? 51.54025 -2.95251  24.03455  1.000 15.18165 ?  146 ILE   B CB   1 
ATOM   4687 C  CG1  . ILE   B 1 143 ? 50.23199 -2.27133  24.44698  1.000 15.57303 ?  146 ILE   B CG1  1 
ATOM   4688 C  CG2  . ILE   B 1 143 ? 51.40806 -3.74940  22.73437  1.000 15.64455 ?  146 ILE   B CG2  1 
ATOM   4689 C  CD1  . ILE   B 1 143 ? 49.09189 -3.19176  24.73936  1.000 15.63049 ?  146 ILE   B CD1  1 
ATOM   4690 H  H    . ILE   B 1 143 ? 52.80890 -2.40689  26.25448  1.000 18.98602 ?  146 ILE   B H    1 
ATOM   4691 H  HA   . ILE   B 1 143 ? 51.37901 -4.52478  25.33925  1.000 18.34910 ?  146 ILE   B HA   1 
ATOM   4692 H  HB   . ILE   B 1 143 ? 52.18549 -2.24701  23.87070  1.000 18.21798 ?  146 ILE   B HB   1 
ATOM   4693 H  HG12 . ILE   B 1 143 ? 50.39778 -1.75314  25.25003  1.000 18.68764 ?  146 ILE   B HG12 1 
ATOM   4694 H  HG13 . ILE   B 1 143 ? 49.95247 -1.68566  23.72603  1.000 18.68764 ?  146 ILE   B HG13 1 
ATOM   4695 H  HG21 . ILE   B 1 143 ? 50.93498 -3.21104  22.08071  1.000 18.77346 ?  146 ILE   B HG21 1 
ATOM   4696 H  HG22 . ILE   B 1 143 ? 52.29442 -3.96608  22.40527  1.000 18.77346 ?  146 ILE   B HG22 1 
ATOM   4697 H  HG23 . ILE   B 1 143 ? 50.91295 -4.56431  22.91238  1.000 18.77346 ?  146 ILE   B HG23 1 
ATOM   4698 H  HD11 . ILE   B 1 143 ? 48.28993 -2.66537  24.88314  1.000 18.75659 ?  146 ILE   B HD11 1 
ATOM   4699 H  HD12 . ILE   B 1 143 ? 48.96550 -3.78765  23.98448  1.000 18.75659 ?  146 ILE   B HD12 1 
ATOM   4700 H  HD13 . ILE   B 1 143 ? 49.29733 -3.70587  25.53583  1.000 18.75659 ?  146 ILE   B HD13 1 
ATOM   4701 N  N    . HIS   B 1 144 ? 53.28851 -5.89604  24.86008  1.000 14.65298 ?  147 HIS   B N    1 
ATOM   4702 C  CA   . HIS   B 1 144 ? 54.43290 -6.71214  24.48615  1.000 15.12318 ?  147 HIS   B CA   1 
ATOM   4703 C  C    . HIS   B 1 144 ? 54.62438 -6.75806  22.97947  1.000 14.42603 ?  147 HIS   B C    1 
ATOM   4704 O  O    . HIS   B 1 144 ? 55.75906 -6.70383  22.49852  1.000 15.48340 ?  147 HIS   B O    1 
ATOM   4705 C  CB   . HIS   B 1 144 ? 54.25172 -8.13242  25.01392  1.000 16.22544 ?  147 HIS   B CB   1 
ATOM   4706 C  CG   . HIS   B 1 144 ? 53.94279 -8.21364  26.47478  1.000 17.96108 ?  147 HIS   B CG   1 
ATOM   4707 N  ND1  . HIS   B 1 144 ? 53.39098 -9.34628  27.03324  1.000 20.05242 ?  147 HIS   B ND1  1 
ATOM   4708 C  CD2  . HIS   B 1 144 ? 54.09492 -7.32543  27.48461  1.000 18.35960 ?  147 HIS   B CD2  1 
ATOM   4709 C  CE1  . HIS   B 1 144 ? 53.21573 -9.16005  28.32159  1.000 21.50288 ?  147 HIS   B CE1  1 
ATOM   4710 N  NE2  . HIS   B 1 144 ? 53.63328 -7.94181  28.62571  1.000 20.24815 ?  147 HIS   B NE2  1 
ATOM   4711 H  H    . HIS   B 1 144 ? 52.60515 -6.34518  25.12635  1.000 17.58358 ?  147 HIS   B H    1 
ATOM   4712 H  HA   . HIS   B 1 144 ? 55.22544 -6.32074  24.88565  1.000 18.14782 ?  147 HIS   B HA   1 
ATOM   4713 H  HB2  . HIS   B 1 144 ? 53.51809 -8.54912  24.53533  1.000 19.47053 ?  147 HIS   B HB2  1 
ATOM   4714 H  HB3  . HIS   B 1 144 ? 55.07186 -8.62684  24.85959  1.000 19.47053 ?  147 HIS   B HB3  1 
ATOM   4715 H  HD1  . HIS   B 1 144 ? 53.19198 -10.06456 26.60419  1.000 24.06290 ?  147 HIS   B HD1  1 
ATOM   4716 H  HD2  . HIS   B 1 144 ? 54.44360 -6.46568  27.42014  1.000 22.03153 ?  147 HIS   B HD2  1 
ATOM   4717 H  HE1  . HIS   B 1 144 ? 52.85929 -9.77839  28.91784  1.000 25.80345 ?  147 HIS   B HE1  1 
ATOM   4718 N  N    . SER   B 1 145 ? 53.53752 -6.89660  22.22049  1.000 14.23233 ?  148 SER   B N    1 
ATOM   4719 C  CA   . SER   B 1 145 ? 53.62815 -6.99415  20.76847  1.000 14.30414 ?  148 SER   B CA   1 
ATOM   4720 C  C    . SER   B 1 145 ? 52.30051 -6.64825  20.10812  1.000 13.72440 ?  148 SER   B C    1 
ATOM   4721 O  O    . SER   B 1 145 ? 51.22777 -6.78307  20.71176  1.000 12.99104 ?  148 SER   B O    1 
ATOM   4722 C  CB   . SER   B 1 145 ? 54.07749 -8.39174  20.33700  1.000 15.59253 ?  148 SER   B CB   1 
ATOM   4723 O  OG   . SER   B 1 145 ? 53.11610 -9.35368  20.69751  1.000 17.67262 ?  148 SER   B OG   1 
ATOM   4724 H  H    . SER   B 1 145 ? 52.73439 -6.93665  22.52541  1.000 17.07880 ?  148 SER   B H    1 
ATOM   4725 H  HA   . SER   B 1 145 ? 54.27185 -6.33514  20.46476  1.000 17.16497 ?  148 SER   B HA   1 
ATOM   4726 H  HB2  . SER   B 1 145 ? 54.19251 -8.40428  19.37392  1.000 18.71104 ?  148 SER   B HB2  1 
ATOM   4727 H  HB3  . SER   B 1 145 ? 54.91706 -8.60363  20.77418  1.000 18.71104 ?  148 SER   B HB3  1 
ATOM   4728 H  HG   . SER   B 1 145 ? 53.49305 -10.02397 21.03548  1.000 21.20714 ?  148 SER   B HG   1 
ATOM   4729 N  N    . ILE   B 1 146 ? 52.40505 -6.18932  18.85794  1.000 13.50195 ?  149 ILE   B N    1 
ATOM   4730 C  CA   . ILE   B 1 146 ? 51.27425 -5.91544  17.97730  1.000 13.41273 ?  149 ILE   B CA   1 
ATOM   4731 C  C    . ILE   B 1 146 ? 51.58821 -6.57194  16.64424  1.000 14.02215 ?  149 ILE   B C    1 
ATOM   4732 O  O    . ILE   B 1 146 ? 52.70334 -6.42615  16.14853  1.000 16.25090 ?  149 ILE   B O    1 
ATOM   4733 C  CB   . ILE   B 1 146 ? 51.06299 -4.40762  17.73869  1.000 13.88086 ?  149 ILE   B CB   1 
ATOM   4734 C  CG1  . ILE   B 1 146 ? 50.84733 -3.67326  19.06608  1.000 14.99102 ?  149 ILE   B CG1  1 
ATOM   4735 C  CG2  . ILE   B 1 146 ? 49.91616 -4.17908  16.77414  1.000 15.45009 ?  149 ILE   B CG2  1 
ATOM   4736 C  CD1  . ILE   B 1 146 ? 50.94228 -2.17766  18.92117  1.000 16.28185 ?  149 ILE   B CD1  1 
ATOM   4737 H  H    . ILE   B 1 146 ? 53.16018 -6.02167  18.48207  1.000 16.20235 ?  149 ILE   B H    1 
ATOM   4738 H  HA   . ILE   B 1 146 ? 50.46813 -6.28550  18.36988  1.000 16.09527 ?  149 ILE   B HA   1 
ATOM   4739 H  HB   . ILE   B 1 146 ? 51.86575 -4.04309  17.33421  1.000 16.65704 ?  149 ILE   B HB   1 
ATOM   4740 H  HG12 . ILE   B 1 146 ? 49.96458 -3.88734  19.40640  1.000 17.98923 ?  149 ILE   B HG12 1 
ATOM   4741 H  HG13 . ILE   B 1 146 ? 51.52496 -3.95804  19.69903  1.000 17.98923 ?  149 ILE   B HG13 1 
ATOM   4742 H  HG21 . ILE   B 1 146 ? 49.67897 -3.23857  16.78270  1.000 18.54011 ?  149 ILE   B HG21 1 
ATOM   4743 H  HG22 . ILE   B 1 146 ? 50.19578 -4.44159  15.88318  1.000 18.54011 ?  149 ILE   B HG22 1 
ATOM   4744 H  HG23 . ILE   B 1 146 ? 49.15698 -4.71424  17.05368  1.000 18.54011 ?  149 ILE   B HG23 1 
ATOM   4745 H  HD11 . ILE   B 1 146 ? 50.97745 -1.77648  19.80362  1.000 19.53822 ?  149 ILE   B HD11 1 
ATOM   4746 H  HD12 . ILE   B 1 146 ? 51.74714 -1.95882  18.42600  1.000 19.53822 ?  149 ILE   B HD12 1 
ATOM   4747 H  HD13 . ILE   B 1 146 ? 50.16197 -1.85657  18.44271  1.000 19.53822 ?  149 ILE   B HD13 1 
ATOM   4748 N  N    . GLY   B 1 147 ? 50.61883 -7.27139  16.05129  1.000 12.99820 ?  150 GLY   B N    1 
ATOM   4749 C  CA   . GLY   B 1 147 ? 50.76896 -7.76929  14.69628  1.000 13.41817 ?  150 GLY   B CA   1 
ATOM   4750 C  C    . GLY   B 1 147 ? 49.41476 -7.86515  14.03548  1.000 12.36809 ?  150 GLY   B C    1 
ATOM   4751 O  O    . GLY   B 1 147 ? 48.37583 -7.74454  14.69349  1.000 12.89697 ?  150 GLY   B O    1 
ATOM   4752 H  H    . GLY   B 1 147 ? 49.86615 -7.46792  16.41797  1.000 15.59784 ?  150 GLY   B H    1 
ATOM   4753 H  HA2  . GLY   B 1 147 ? 51.33015 -7.16794  14.18214  1.000 16.10181 ?  150 GLY   B HA2  1 
ATOM   4754 H  HA3  . GLY   B 1 147 ? 51.17768 -8.64888  14.70942  1.000 16.10181 ?  150 GLY   B HA3  1 
ATOM   4755 N  N    . PHE   B 1 148 ? 49.43615 -8.10487  12.72495  1.000 12.00497 ?  151 PHE   B N    1 
ATOM   4756 C  CA   . PHE   B 1 148 ? 48.22653 -8.09713  11.92404  1.000 12.55672 ?  151 PHE   B CA   1 
ATOM   4757 C  C    . PHE   B 1 148 ? 48.15570 -9.34514  11.05966  1.000 12.62676 ?  151 PHE   B C    1 
ATOM   4758 O  O    . PHE   B 1 148 ? 49.17013 -9.90979  10.65967  1.000 14.11925 ?  151 PHE   B O    1 
ATOM   4759 C  CB   . PHE   B 1 148 ? 48.20892 -6.87470  11.00247  1.000 13.32030 ?  151 PHE   B CB   1 
ATOM   4760 C  CG   . PHE   B 1 148 ? 48.21429 -5.56434  11.73613  1.000 13.45182 ?  151 PHE   B CG   1 
ATOM   4761 C  CD1  . PHE   B 1 148 ? 49.40632 -4.97587  12.11439  1.000 14.34318 ?  151 PHE   B CD1  1 
ATOM   4762 C  CD2  . PHE   B 1 148 ? 47.02865 -4.91174  12.05182  1.000 13.96378 ?  151 PHE   B CD2  1 
ATOM   4763 C  CE1  . PHE   B 1 148 ? 49.41536 -3.76242  12.78294  1.000 16.13527 ?  151 PHE   B CE1  1 
ATOM   4764 C  CE2  . PHE   B 1 148 ? 47.03600 -3.69763  12.71792  1.000 15.52542 ?  151 PHE   B CE2  1 
ATOM   4765 C  CZ   . PHE   B 1 148 ? 48.23489 -3.12468  13.08598  1.000 16.14789 ?  151 PHE   B CZ   1 
ATOM   4766 H  H    . PHE   B 1 148 ? 50.15033 -8.27590  12.27739  1.000 14.40597 ?  151 PHE   B H    1 
ATOM   4767 H  HA   . PHE   B 1 148 ? 47.45649 -8.08967  12.51385  1.000 15.06806 ?  151 PHE   B HA   1 
ATOM   4768 H  HB2  . PHE   B 1 148 ? 48.99569 -6.89997  10.43568  1.000 15.98436 ?  151 PHE   B HB2  1 
ATOM   4769 H  HB3  . PHE   B 1 148 ? 47.40671 -6.90599  10.45806  1.000 15.98436 ?  151 PHE   B HB3  1 
ATOM   4770 H  HD1  . PHE   B 1 148 ? 50.21090 -5.39895  11.91804  1.000 17.21182 ?  151 PHE   B HD1  1 
ATOM   4771 H  HD2  . PHE   B 1 148 ? 46.21682 -5.29674  11.81179  1.000 16.75653 ?  151 PHE   B HD2  1 
ATOM   4772 H  HE1  . PHE   B 1 148 ? 50.22506 -3.37644  13.02849  1.000 19.36232 ?  151 PHE   B HE1  1 
ATOM   4773 H  HE2  . PHE   B 1 148 ? 46.23443 -3.26989  12.91646  1.000 18.63050 ?  151 PHE   B HE2  1 
ATOM   4774 H  HZ   . PHE   B 1 148 ? 48.24536 -2.31130  13.53676  1.000 19.37747 ?  151 PHE   B HZ   1 
ATOM   4775 N  N    . SER   B 1 149 ? 46.93865 -9.73331  10.68335  1.000 13.48017 ?  152 SER   B N    1 
ATOM   4776 C  CA   . SER   B 1 149 ? 46.74488 -10.72340 9.62470   1.000 14.30673 ?  152 SER   B CA   1 
ATOM   4777 C  C    . SER   B 1 149 ? 45.75370 -10.11244 8.64463   1.000 14.16085 ?  152 SER   B C    1 
ATOM   4778 O  O    . SER   B 1 149 ? 44.55576 -10.05866 8.92914   1.000 15.00120 ?  152 SER   B O    1 
ATOM   4779 C  CB   . SER   B 1 149 ? 46.22554 -12.03489 10.17680  1.000 17.02059 ?  152 SER   B CB   1 
ATOM   4780 O  OG   . SER   B 1 149 ? 46.12547 -12.98055 9.14849   1.000 21.59040 ?  152 SER   B OG   1 
ATOM   4781 H  H    . SER   B 1 149 ? 46.20831 -9.43673  11.02722  1.000 16.17621 ?  152 SER   B H    1 
ATOM   4782 H  HA   . SER   B 1 149 ? 47.58675 -10.90155 9.17702   1.000 17.16808 ?  152 SER   B HA   1 
ATOM   4783 H  HB2  . SER   B 1 149 ? 46.83939 -12.36212 10.85283  1.000 20.42471 ?  152 SER   B HB2  1 
ATOM   4784 H  HB3  . SER   B 1 149 ? 45.34855 -11.89250 10.56604  1.000 20.42471 ?  152 SER   B HB3  1 
ATOM   4785 H  HG   . SER   B 1 149 ? 45.34612 -12.98282 8.83511   1.000 25.90848 ?  152 SER   B HG   1 
ATOM   4786 N  N    . PHE   B 1 150 ? 46.25760 -9.61388  7.52868   1.000 15.02315 ?  153 PHE   B N    1 
ATOM   4787 C  CA   . PHE   B 1 150 ? 45.40053 -8.90294  6.59614   1.000 16.30725 ?  153 PHE   B CA   1 
ATOM   4788 C  C    . PHE   B 1 150 ? 44.69922 -9.89495  5.68265   1.000 18.89310 ?  153 PHE   B C    1 
ATOM   4789 O  O    . PHE   B 1 150 ? 45.21968 -10.95820 5.36785   1.000 22.56691 ?  153 PHE   B O    1 
ATOM   4790 C  CB   . PHE   B 1 150 ? 46.22583 -7.87711  5.81482   1.000 16.11421 ?  153 PHE   B CB   1 
ATOM   4791 C  CG   . PHE   B 1 150 ? 46.72433 -6.75791  6.68640   1.000 14.87370 ?  153 PHE   B CG   1 
ATOM   4792 C  CD1  . PHE   B 1 150 ? 45.81898 -5.87487  7.24406   1.000 15.86939 ?  153 PHE   B CD1  1 
ATOM   4793 C  CD2  . PHE   B 1 150 ? 48.07878 -6.60208  6.98158   1.000 15.06912 ?  153 PHE   B CD2  1 
ATOM   4794 C  CE1  . PHE   B 1 150 ? 46.24572 -4.85720  8.06950   1.000 16.12269 ?  153 PHE   B CE1  1 
ATOM   4795 C  CE2  . PHE   B 1 150 ? 48.50134 -5.59038  7.80400   1.000 15.47845 ?  153 PHE   B CE2  1 
ATOM   4796 C  CZ   . PHE   B 1 150 ? 47.59082 -4.71507  8.33961   1.000 15.53981 ?  153 PHE   B CZ   1 
ATOM   4797 H  H    . PHE   B 1 150 ? 47.08194 -9.67267  7.29079   1.000 18.02778 ?  153 PHE   B H    1 
ATOM   4798 H  HA   . PHE   B 1 150 ? 44.70683 -8.40838  7.05992   1.000 19.56870 ?  153 PHE   B HA   1 
ATOM   4799 H  HB2  . PHE   B 1 150 ? 46.99491 -8.32051  5.42392   1.000 19.33705 ?  153 PHE   B HB2  1 
ATOM   4800 H  HB3  . PHE   B 1 150 ? 45.67402 -7.49236  5.11599   1.000 19.33705 ?  153 PHE   B HB3  1 
ATOM   4801 H  HD1  . PHE   B 1 150 ? 44.91214 -5.96849  7.06027   1.000 19.04327 ?  153 PHE   B HD1  1 
ATOM   4802 H  HD2  . PHE   B 1 150 ? 48.70052 -7.18987  6.61711   1.000 18.08294 ?  153 PHE   B HD2  1 
ATOM   4803 H  HE1  . PHE   B 1 150 ? 45.62961 -4.26896  8.44270   1.000 19.34723 ?  153 PHE   B HE1  1 
ATOM   4804 H  HE2  . PHE   B 1 150 ? 49.40586 -5.49719  7.99907   1.000 18.57414 ?  153 PHE   B HE2  1 
ATOM   4805 H  HZ   . PHE   B 1 150 ? 47.88200 -4.02238  8.88760   1.000 18.64778 ?  153 PHE   B HZ   1 
ATOM   4806 N  N    . SER   B 1 151 ? 43.47942 -9.54913  5.29287   1.000 22.23830 ?  154 SER   B N    1 
ATOM   4807 C  CA   A SER   B 1 151 ? 42.68012 -10.37460 4.39288   0.413 25.83785 ?  154 SER   B CA   1 
ATOM   4808 C  CA   B SER   B 1 151 ? 42.67555 -10.37036 4.39721   0.587 24.48779 ?  154 SER   B CA   1 
ATOM   4809 C  C    . SER   B 1 151 ? 42.67618 -9.72420  3.01712   1.000 30.69487 ?  154 SER   B C    1 
ATOM   4810 O  O    . SER   B 1 151 ? 41.63611 -9.28234  2.50757   1.000 31.24499 ?  154 SER   B O    1 
ATOM   4811 C  CB   A SER   B 1 151 ? 41.26889 -10.52352 4.93657   0.413 25.04349 ?  154 SER   B CB   1 
ATOM   4812 C  CB   B SER   B 1 151 ? 41.26624 -10.50110 4.96731   0.587 22.67435 ?  154 SER   B CB   1 
ATOM   4813 O  OG   A SER   B 1 151 ? 40.65223 -9.25668  4.98450   0.413 23.89729 ?  154 SER   B OG   1 
ATOM   4814 O  OG   B SER   B 1 151 ? 40.49972 -11.47868 4.29943   0.587 23.03036 ?  154 SER   B OG   1 
ATOM   4815 H  H    . SER   B 1 151 ? 43.08404 -8.82601  5.53857   1.000 26.68596 ?  154 SER   B H    1 
ATOM   4816 H  HA   . SER   B 1 151 ? 43.05020 -11.26804 4.31737   1.000 29.38534 ?  154 SER   B HA   1 
ATOM   4817 H  HB2  A SER   B 1 151 ? 40.75928 -11.10780 4.35364   0.413 30.05218 ?  154 SER   B HB2  1 
ATOM   4818 H  HB2  B SER   B 1 151 ? 41.33345 -10.74774 5.90302   0.587 27.20922 ?  154 SER   B HB2  1 
ATOM   4819 H  HB3  A SER   B 1 151 ? 41.30619 -10.89747 5.83082   0.413 30.05218 ?  154 SER   B HB3  1 
ATOM   4820 H  HB3  B SER   B 1 151 ? 40.81782 -9.64530  4.88118   0.587 27.20922 ?  154 SER   B HB3  1 
ATOM   4821 H  HG   A SER   B 1 151 ? 40.87244 -8.85644  5.68942   0.413 28.67675 ?  154 SER   B HG   1 
ATOM   4822 H  HG   B SER   B 1 151 ? 39.73656 -11.53182 4.64638   0.587 27.63644 ?  154 SER   B HG   1 
ATOM   4823 N  N    . SER   B 1 152 ? 43.86659 -9.64254  2.44438   1.000 39.33200 ?  155 SER   B N    1 
ATOM   4824 C  CA   . SER   B 1 152 ? 44.10977 -9.01822  1.15595   1.000 45.16369 ?  155 SER   B CA   1 
ATOM   4825 C  C    . SER   B 1 152 ? 45.45583 -9.52232  0.64704   1.000 48.83389 ?  155 SER   B C    1 
ATOM   4826 O  O    . SER   B 1 152 ? 46.32042 -9.88811  1.44977   1.000 51.16639 ?  155 SER   B O    1 
ATOM   4827 C  CB   . SER   B 1 152 ? 44.13719 -7.48952  1.29018   1.000 44.74608 ?  155 SER   B CB   1 
ATOM   4828 O  OG   . SER   B 1 152 ? 45.27246 -7.02211  2.01193   1.000 42.59946 ?  155 SER   B OG   1 
ATOM   4829 H  H    . SER   B 1 152 ? 44.58443 -9.95642  2.79904   1.000 47.19840 ?  155 SER   B H    1 
ATOM   4830 H  HA   . SER   B 1 152 ? 43.40520 -9.23293  0.52478   1.000 54.19642 ?  155 SER   B HA   1 
ATOM   4831 H  HB2  . SER   B 1 152 ? 44.15605 -7.10214  0.40109   1.000 53.69529 ?  155 SER   B HB2  1 
ATOM   4832 H  HB3  . SER   B 1 152 ? 43.33616 -7.20662  1.75840   1.000 53.69529 ?  155 SER   B HB3  1 
ATOM   4833 H  HG   . SER   B 1 152 ? 45.22463 -7.26843  2.81358   1.000 51.11935 ?  155 SER   B HG   1 
HETATM 4834 C  C2   . A1IHE C 2 .   ? 14.79320 5.78661   -9.26820  1.000 13.34809 ?  201 A1IHE A C2   1 
HETATM 4835 C  C3   . A1IHE C 2 .   ? 13.41825 6.09575   -9.80215  1.000 13.12724 ?  201 A1IHE A C3   1 
HETATM 4836 O  O1   . A1IHE C 2 .   ? 15.81474 6.51402   -9.91483  1.000 13.62803 ?  201 A1IHE A O1   1 
HETATM 4837 C  C5   . A1IHE C 2 .   ? 12.15399 5.98438   -11.82499 1.000 14.20321 ?  201 A1IHE A C5   1 
HETATM 4838 C  C7   . A1IHE C 2 .   ? 13.51043 8.00967   -12.99382 1.000 14.83523 ?  201 A1IHE A C7   1 
HETATM 4839 O  O4   . A1IHE C 2 .   ? 13.36899 5.63460   -11.16409 1.000 13.04936 ?  201 A1IHE A O4   1 
HETATM 4840 C  C11  . A1IHE C 2 .   ? 15.94227 8.36166   -14.26079 1.000 16.36232 ?  201 A1IHE A C11  1 
HETATM 4841 C  C13  . A1IHE C 2 .   ? 14.88565 7.79795   -14.94808 1.000 17.05331 ?  201 A1IHE A C13  1 
HETATM 4842 C  C14  . A1IHE C 2 .   ? 13.66972 7.62082   -14.31761 1.000 16.23363 ?  201 A1IHE A C14  1 
HETATM 4843 C  C15  . A1IHE C 2 .   ? 10.93169 5.44089   -11.08456 1.000 14.82262 ?  201 A1IHE A C15  1 
HETATM 4844 C  C17  . A1IHE C 2 .   ? 9.41207  5.44941   -12.90439 1.000 29.62121 ?  201 A1IHE A C17  1 
HETATM 4845 C  C18  . A1IHE C 2 .   ? 9.05575  4.03540   -12.86912 1.000 50.83356 ?  201 A1IHE A C18  1 
HETATM 4846 C  C19  . A1IHE C 2 .   ? 8.81789  2.88360   -12.86094 1.000 66.70122 ?  201 A1IHE A C19  1 
HETATM 4847 C  C20  . A1IHE C 2 .   ? 10.96024 5.82883   -9.61524  1.000 13.95385 ?  201 A1IHE A C20  1 
HETATM 4848 C  C22  . A1IHE C 2 .   ? 8.79250  5.94132   -8.58384  1.000 15.14385 ?  201 A1IHE A C22  1 
HETATM 4849 C  C23  . A1IHE C 2 .   ? 7.82396  5.17407   -7.75865  1.000 14.54242 ?  201 A1IHE A C23  1 
HETATM 4850 C  C25  . A1IHE C 2 .   ? 6.54016  4.55055   -6.15605  1.000 14.22357 ?  201 A1IHE A C25  1 
HETATM 4851 C  C26  . A1IHE C 2 .   ? 5.84346  4.39598   -4.95986  1.000 14.82559 ?  201 A1IHE A C26  1 
HETATM 4852 C  C27  . A1IHE C 2 .   ? 4.87239  3.41591   -4.87259  1.000 14.44851 ?  201 A1IHE A C27  1 
HETATM 4853 C  C28  . A1IHE C 2 .   ? 4.58341  2.58288   -5.95691  1.000 14.97086 ?  201 A1IHE A C28  1 
HETATM 4854 C  C29  . A1IHE C 2 .   ? 3.53303  1.51036   -5.82396  1.000 16.75574 ?  201 A1IHE A C29  1 
HETATM 4855 C  C32  . A1IHE C 2 .   ? 5.27667  2.73393   -7.15875  1.000 14.95320 ?  201 A1IHE A C32  1 
HETATM 4856 C  C33  . A1IHE C 2 .   ? 6.24463  3.71981   -7.23263  1.000 14.10173 ?  201 A1IHE A C33  1 
HETATM 4857 C  C35  . A1IHE C 2 .   ? 7.13641  3.56455   -9.60615  1.000 16.33908 ?  201 A1IHE A C35  1 
HETATM 4858 C  C36  . A1IHE C 2 .   ? 12.29648 5.44888   -8.99952  1.000 13.00451 ?  201 A1IHE A C36  1 
HETATM 4859 C  C8   . A1IHE C 2 .   ? 14.57512 8.57525   -12.31068 1.000 14.02570 ?  201 A1IHE A C8   1 
HETATM 4860 C  C9   . A1IHE C 2 .   ? 15.78358 8.75177   -12.94723 1.000 15.26508 ?  201 A1IHE A C9   1 
HETATM 4861 N  N24  . A1IHE C 2 .   ? 7.53387  5.45614   -6.50353  1.000 14.52846 ?  201 A1IHE A N24  1 
HETATM 4862 N  N34  . A1IHE C 2 .   ? 7.08483  4.13844   -8.25708  1.000 14.69134 ?  201 A1IHE A N34  1 
HETATM 4863 O  O16  . A1IHE C 2 .   ? 9.71011  5.95772   -11.60329 1.000 17.32912 ?  201 A1IHE A O16  1 
HETATM 4864 O  O21  . A1IHE C 2 .   ? 9.93365  5.13613   -8.90588  1.000 14.60033 ?  201 A1IHE A O21  1 
HETATM 4865 O  O30  . A1IHE C 2 .   ? 2.79985  1.54589   -4.79873  1.000 17.83881 -1 201 A1IHE A O30  1 
HETATM 4866 O  O31  . A1IHE C 2 .   ? 3.46200  0.63530   -6.71874  1.000 16.50974 ?  201 A1IHE A O31  1 
HETATM 4867 O  O37  . A1IHE C 2 .   ? 12.39803 4.02467   -8.98529  1.000 12.65576 ?  201 A1IHE A O37  1 
HETATM 4868 S  S6   . A1IHE C 2 .   ? 11.97261 7.77129   -12.15209 1.000 15.29789 ?  201 A1IHE A S6   1 
HETATM 4869 CL CL10 . A1IHE C 2 .   ? 17.07609 9.51128   -12.08234 0.766 14.43304 ?  201 A1IHE A CL10 1 
HETATM 4870 CL CL12 . A1IHE C 2 .   ? 17.46809 8.52553   -15.05008 0.494 16.23081 ?  201 A1IHE A CL12 1 
HETATM 4871 H  H2A  . A1IHE C 2 .   ? 14.83773 6.00021   -8.31383  1.000 16.01770 ?  201 A1IHE A H2A  1 
HETATM 4872 H  H2B  . A1IHE C 2 .   ? 14.99088 4.83467   -9.38302  1.000 16.01770 ?  201 A1IHE A H2B  1 
HETATM 4873 H  H3   . A1IHE C 2 .   ? 13.31593 7.06916   -9.78139  1.000 15.75269 ?  201 A1IHE A H3   1 
HETATM 4874 H  H1   . A1IHE C 2 .   ? 15.52958 7.30440   -10.04318 1.000 16.35364 ?  201 A1IHE A H1   1 
HETATM 4875 H  H5   . A1IHE C 2 .   ? 12.18570 5.56839   -12.71065 1.000 17.04385 ?  201 A1IHE A H5   1 
HETATM 4876 H  H13  . A1IHE C 2 .   ? 14.98864 7.52102   -15.88143 1.000 20.46397 ?  201 A1IHE A H13  1 
HETATM 4877 H  H14  . A1IHE C 2 .   ? 12.92637 7.22015   -14.81293 1.000 19.48035 ?  201 A1IHE A H14  1 
HETATM 4878 H  H15  . A1IHE C 2 .   ? 10.98467 4.46870   -11.18694 1.000 17.78715 ?  201 A1IHE A H15  1 
HETATM 4879 H  H17A . A1IHE C 2 .   ? 10.19125 5.58177   -13.48213 1.000 35.54545 ?  201 A1IHE A H17A 1 
HETATM 4880 H  H17B . A1IHE C 2 .   ? 8.67510  5.96873   -13.28601 1.000 35.54545 ?  201 A1IHE A H17B 1 
HETATM 4881 H  H19  . A1IHE C 2 .   ? 8.61929  1.92501   -12.85078 1.000 80.04146 ?  201 A1IHE A H19  1 
HETATM 4882 H  H20  . A1IHE C 2 .   ? 10.80040 6.78998   -9.51997  1.000 16.74462 ?  201 A1IHE A H20  1 
HETATM 4883 H  H22A . A1IHE C 2 .   ? 8.33483  6.23516   -9.39787  1.000 18.17262 ?  201 A1IHE A H22A 1 
HETATM 4884 H  H22B . A1IHE C 2 .   ? 9.06061  6.73659   -8.07977  1.000 18.17262 ?  201 A1IHE A H22B 1 
HETATM 4885 H  H26  . A1IHE C 2 .   ? 6.03956  4.97315   -4.19380  1.000 17.79071 ?  201 A1IHE A H26  1 
HETATM 4886 H  H27  . A1IHE C 2 .   ? 4.37407  3.29798   -4.03820  1.000 17.33821 ?  201 A1IHE A H27  1 
HETATM 4887 H  H32  . A1IHE C 2 .   ? 5.06959  2.14943   -7.91632  1.000 17.94383 ?  201 A1IHE A H32  1 
HETATM 4888 H  H35B . A1IHE C 2 .   ? 6.62769  2.72891   -9.64294  1.000 19.60689 ?  201 A1IHE A H35B 1 
HETATM 4889 H  H35A . A1IHE C 2 .   ? 8.06191  3.37490   -9.86291  1.000 19.60689 ?  201 A1IHE A H35A 1 
HETATM 4890 H  H35C . A1IHE C 2 .   ? 6.75579  4.18745   -10.25850 1.000 19.60689 ?  201 A1IHE A H35C 1 
HETATM 4891 H  H36  . A1IHE C 2 .   ? 12.37835 5.72827   -8.06481  1.000 15.60541 ?  201 A1IHE A H36  1 
HETATM 4892 H  H8   . A1IHE C 2 .   ? 14.47984 8.85269   -11.37666 1.000 16.83084 ?  201 A1IHE A H8   1 
HETATM 4893 H  H37  . A1IHE C 2 .   ? 13.21353 3.84234   -8.82970  1.000 15.18691 ?  201 A1IHE A H37  1 
HETATM 4894 CL CL   . CL    D 3 .   ? 31.09554 5.39827   7.18169   1.000 20.07438 ?  202 CL    A CL   1 
HETATM 4895 C  C2   . A1IHE E 2 .   ? 33.46283 5.83652   26.31038  1.000 15.40664 ?  201 A1IHE B C2   1 
HETATM 4896 C  C3   . A1IHE E 2 .   ? 34.09955 7.09022   26.86137  1.000 15.68060 ?  201 A1IHE B C3   1 
HETATM 4897 O  O1   . A1IHE E 2 .   ? 32.04858 5.91232   26.30821  1.000 16.27674 ?  201 A1IHE B O1   1 
HETATM 4898 C  C5   . A1IHE E 2 .   ? 34.10660 8.44261   28.83408  1.000 18.50021 ?  201 A1IHE B C5   1 
HETATM 4899 C  C7   . A1IHE E 2 .   ? 31.57858 9.38972   28.38508  1.000 19.06691 ?  201 A1IHE B C7   1 
HETATM 4900 O  O4   . A1IHE E 2 .   ? 33.68430 7.22007   28.23401  1.000 16.62975 ?  201 A1IHE B O4   1 
HETATM 4901 C  C11  . A1IHE E 2 .   ? 28.94189 8.56638   28.68736  1.000 20.55191 ?  201 A1IHE B C11  1 
HETATM 4902 C  C13  . A1IHE E 2 .   ? 29.66369 8.99449   29.79151  1.000 21.09662 ?  201 A1IHE B C13  1 
HETATM 4903 C  C14  . A1IHE E 2 .   ? 30.97841 9.40644   29.64105  1.000 21.56798 ?  201 A1IHE B C14  1 
HETATM 4904 C  C15  . A1IHE E 2 .   ? 35.62534 8.59986   28.75648  1.000 18.58866 ?  201 A1IHE B C15  1 
HETATM 4905 C  C17  . A1IHE E 2 .   ? 35.96994 10.24179  30.52212  1.000 31.69881 ?  201 A1IHE B C17  1 
HETATM 4906 C  C18  . A1IHE E 2 .   ? 36.90046 9.45646   31.32540  1.000 40.45177 ?  201 A1IHE B C18  1 
HETATM 4907 C  C19  . A1IHE E 2 .   ? 37.68881 8.84096   31.94456  1.000 44.39041 ?  201 A1IHE B C19  1 
HETATM 4908 C  C20  . A1IHE E 2 .   ? 36.14360 8.37583   27.34678  1.000 17.53568 ?  201 A1IHE B C20  1 
HETATM 4909 C  C22  . A1IHE E 2 .   ? 38.16663 9.46662   26.73758  1.000 19.97414 ?  201 A1IHE B C22  1 
HETATM 4910 C  C23  . A1IHE E 2 .   ? 39.63639 9.27944   26.69538  1.000 19.28452 ?  201 A1IHE B C23  1 
HETATM 4911 C  C25  . A1IHE E 2 .   ? 41.65692 9.10602   25.98797  1.000 18.91786 ?  201 A1IHE B C25  1 
HETATM 4912 C  C26  . A1IHE E 2 .   ? 42.83065 9.04611   25.24312  1.000 20.18284 ?  201 A1IHE B C26  1 
HETATM 4913 C  C27  . A1IHE E 2 .   ? 44.04423 8.93454   25.90261  1.000 19.97573 ?  201 A1IHE B C27  1 
HETATM 4914 C  C28  . A1IHE E 2 .   ? 44.10758 8.88041   27.29925  1.000 20.82608 ?  201 A1IHE B C28  1 
HETATM 4915 C  C29  . A1IHE E 2 .   ? 45.43847 8.73886   27.99639  1.000 23.76275 ?  201 A1IHE B C29  1 
HETATM 4916 C  C32  . A1IHE E 2 .   ? 42.93447 8.94325   28.05068  1.000 20.24842 ?  201 A1IHE B C32  1 
HETATM 4917 C  C33  . A1IHE E 2 .   ? 41.72721 9.05768   27.37568  1.000 18.77914 ?  201 A1IHE B C33  1 
HETATM 4918 C  C35  . A1IHE E 2 .   ? 39.99084 9.21746   29.21866  1.000 21.36647 ?  201 A1IHE B C35  1 
HETATM 4919 C  C36  . A1IHE E 2 .   ? 35.62188 7.07078   26.78205  1.000 15.69657 ?  201 A1IHE B C36  1 
HETATM 4920 C  C8   . A1IHE E 2 .   ? 30.85191 8.95939   27.28497  1.000 19.03864 ?  201 A1IHE B C8   1 
HETATM 4921 C  C9   . A1IHE E 2 .   ? 29.54363 8.55238   27.44082  1.000 19.46648 ?  201 A1IHE B C9   1 
HETATM 4922 N  N24  . A1IHE E 2 .   ? 40.33036 9.24411   25.57842  1.000 19.79071 ?  201 A1IHE B N24  1 
HETATM 4923 N  N34  . A1IHE E 2 .   ? 40.41511 9.17177   27.81729  1.000 19.51521 ?  201 A1IHE B N34  1 
HETATM 4924 O  O16  . A1IHE E 2 .   ? 36.04012 9.90966   29.13487  1.000 23.18471 ?  201 A1IHE B O16  1 
HETATM 4925 O  O21  . A1IHE E 2 .   ? 37.56403 8.32040   27.33394  1.000 18.30982 ?  201 A1IHE B O21  1 
HETATM 4926 O  O30  . A1IHE E 2 .   ? 46.47782 8.91146   27.30493  1.000 26.54702 -1 201 A1IHE B O30  1 
HETATM 4927 O  O31  . A1IHE E 2 .   ? 45.43789 8.44347   29.21772  1.000 25.82052 ?  201 A1IHE B O31  1 
HETATM 4928 O  O37  . A1IHE E 2 .   ? 36.17099 5.98641   27.52534  1.000 15.29219 ?  201 A1IHE B O37  1 
HETATM 4929 S  S6   . A1IHE E 2 .   ? 33.25939 9.91087   28.15894  1.000 20.29940 ?  201 A1IHE B S6   1 
HETATM 4930 CL CL10 . A1IHE E 2 .   ? 28.65891 8.07339   26.03809  0.875 19.15236 ?  201 A1IHE B CL10 1 
HETATM 4931 CL CL12 . A1IHE E 2 .   ? 27.29090 8.06380   28.87217  0.496 22.39094 ?  201 A1IHE B CL12 1 
HETATM 4932 H  H2A  . A1IHE E 2 .   ? 33.75598 5.68503   25.38867  1.000 18.48797 ?  201 A1IHE B H2A  1 
HETATM 4933 H  H2B  . A1IHE E 2 .   ? 33.72029 5.06106   26.84967  1.000 18.48797 ?  201 A1IHE B H2B  1 
HETATM 4934 H  H3   . A1IHE E 2 .   ? 33.75127 7.84482   26.34397  1.000 18.81672 ?  201 A1IHE B H3   1 
HETATM 4935 H  H1   . A1IHE E 2 .   ? 31.82961 6.68927   26.57450  1.000 19.53209 ?  201 A1IHE B H1   1 
HETATM 4936 H  H5   . A1IHE E 2 .   ? 33.85096 8.41367   29.77867  1.000 22.20025 ?  201 A1IHE B H5   1 
HETATM 4937 H  H13  . A1IHE E 2 .   ? 29.25356 9.00925   30.68033  1.000 25.31594 ?  201 A1IHE B H13  1 
HETATM 4938 H  H14  . A1IHE E 2 .   ? 31.47781 9.70834   30.42712  1.000 25.88158 ?  201 A1IHE B H14  1 
HETATM 4939 H  H15  . A1IHE E 2 .   ? 35.98549 7.91450   29.35566  1.000 22.30640 ?  201 A1IHE B H15  1 
HETATM 4940 H  H17A . A1IHE E 2 .   ? 36.16353 11.19557  30.62828  1.000 38.03857 ?  201 A1IHE B H17A 1 
HETATM 4941 H  H17B . A1IHE E 2 .   ? 35.05447 10.09385  30.83593  1.000 38.03857 ?  201 A1IHE B H17B 1 
HETATM 4942 H  H19  . A1IHE E 2 .   ? 38.34508 8.32638   32.45736  1.000 53.26849 ?  201 A1IHE B H19  1 
HETATM 4943 H  H20  . A1IHE E 2 .   ? 35.86651 9.12625   26.78238  1.000 21.04282 ?  201 A1IHE B H20  1 
HETATM 4944 H  H22A . A1IHE E 2 .   ? 37.96952 10.27574  27.25228  1.000 23.96896 ?  201 A1IHE B H22A 1 
HETATM 4945 H  H22B . A1IHE E 2 .   ? 37.84233 9.59918   25.82341  1.000 23.96896 ?  201 A1IHE B H22B 1 
HETATM 4946 H  H26  . A1IHE E 2 .   ? 42.79784 9.08244   24.26535  1.000 24.21941 ?  201 A1IHE B H26  1 
HETATM 4947 H  H27  . A1IHE E 2 .   ? 44.87591 8.89237   25.38786  1.000 23.97088 ?  201 A1IHE B H27  1 
HETATM 4948 H  H32  . A1IHE E 2 .   ? 42.98202 8.90608   29.02782  1.000 24.29810 ?  201 A1IHE B H32  1 
HETATM 4949 H  H35B . A1IHE E 2 .   ? 40.68806 8.85103   29.80008  1.000 25.63977 ?  201 A1IHE B H35B 1 
HETATM 4950 H  H35A . A1IHE E 2 .   ? 39.81257 10.14017  29.49299  1.000 25.63977 ?  201 A1IHE B H35A 1 
HETATM 4951 H  H35C . A1IHE E 2 .   ? 39.17401 8.69326   29.34685  1.000 25.63977 ?  201 A1IHE B H35C 1 
HETATM 4952 H  H36  . A1IHE E 2 .   ? 35.90512 6.91794   25.85747  1.000 18.83588 ?  201 A1IHE B H36  1 
HETATM 4953 H  H8   . A1IHE E 2 .   ? 31.25714 8.94039   26.39398  1.000 22.84636 ?  201 A1IHE B H8   1 
HETATM 4954 H  H37  . A1IHE E 2 .   ? 35.53300 5.44269   27.66618  1.000 18.35062 ?  201 A1IHE B H37  1 
HETATM 4955 O  O    . HOH   F 4 .   ? 0.05360  -9.03168  -10.06293 1.000 43.60977 ?  301 HOH   A O    1 
HETATM 4956 O  O    . HOH   F 4 .   ? 3.08455  -10.87215 4.39906   1.000 37.99083 ?  302 HOH   A O    1 
HETATM 4957 O  O    . HOH   F 4 .   ? 9.57330  -16.92075 2.59579   1.000 36.39365 ?  303 HOH   A O    1 
HETATM 4958 O  O    . HOH   F 4 .   ? 18.65397 -11.63385 -11.63833 1.000 37.11631 ?  304 HOH   A O    1 
HETATM 4959 O  O    . HOH   F 4 .   ? 22.01260 -0.23722  -16.63110 1.000 38.72823 ?  305 HOH   A O    1 
HETATM 4960 O  O    . HOH   F 4 .   ? 16.85271 -1.33476  19.54239  1.000 32.13716 ?  306 HOH   A O    1 
HETATM 4961 O  O    . HOH   F 4 .   ? 20.60770 -12.13315 6.43092   1.000 30.46842 ?  307 HOH   A O    1 
HETATM 4962 O  O    . HOH   F 4 .   ? 25.24529 -11.26450 -11.46067 1.000 45.86516 ?  308 HOH   A O    1 
HETATM 4963 O  O    . HOH   F 4 .   ? 14.94474 -2.74695  18.96830  1.000 34.32134 ?  309 HOH   A O    1 
HETATM 4964 O  O    . HOH   F 4 .   ? 24.23203 -10.90533 -5.50352  1.000 39.99195 ?  310 HOH   A O    1 
HETATM 4965 O  O    . HOH   F 4 .   ? 26.64337 -1.49735  -6.24319  1.000 26.26251 ?  311 HOH   A O    1 
HETATM 4966 O  O    . HOH   F 4 .   ? 19.24630 5.14395   17.71655  1.000 28.64122 ?  312 HOH   A O    1 
HETATM 4967 O  O    . HOH   F 4 .   ? 10.63097 -12.84503 10.36042  1.000 42.36131 ?  313 HOH   A O    1 
HETATM 4968 O  O    . HOH   F 4 .   ? 3.49539  -7.80130  -12.74944 1.000 34.70600 ?  314 HOH   A O    1 
HETATM 4969 O  O    . HOH   F 4 .   ? 13.93829 18.89061  0.83229   1.000 29.71633 ?  315 HOH   A O    1 
HETATM 4970 O  O    . HOH   F 4 .   ? 1.57558  -1.20535  -6.35665  1.000 33.42932 ?  316 HOH   A O    1 
HETATM 4971 O  O    . HOH   F 4 .   ? 7.08975  19.71928  -6.51585  1.000 41.62835 ?  317 HOH   A O    1 
HETATM 4972 O  O    . HOH   F 4 .   ? 8.27422  6.90673   -1.70552  1.000 19.95418 ?  318 HOH   A O    1 
HETATM 4973 O  O    . HOH   F 4 .   ? 4.10673  10.90594  9.19250   1.000 42.75745 ?  319 HOH   A O    1 
HETATM 4974 O  O    . HOH   F 4 .   ? 14.86082 4.24101   -13.88037 1.000 19.20398 ?  320 HOH   A O    1 
HETATM 4975 O  O    . HOH   F 4 .   ? 3.36787  8.59837   13.63730  1.000 39.76086 ?  321 HOH   A O    1 
HETATM 4976 O  O    . HOH   F 4 .   ? 1.59041  -5.21921  -3.60825  1.000 37.57714 ?  322 HOH   A O    1 
HETATM 4977 O  O    . HOH   F 4 .   ? 30.62409 13.09753  7.17812   1.000 29.47191 ?  323 HOH   A O    1 
HETATM 4978 O  O    . HOH   F 4 .   ? 5.78778  9.08628   9.81223   1.000 33.09315 ?  324 HOH   A O    1 
HETATM 4979 O  O    . HOH   F 4 .   ? 21.64754 -9.07405  -13.25956 1.000 26.99197 ?  325 HOH   A O    1 
HETATM 4980 O  O    . HOH   F 4 .   ? 23.08777 15.62639  -1.26154  1.000 36.07747 ?  326 HOH   A O    1 
HETATM 4981 O  O    . HOH   F 4 .   ? 26.84406 0.12387   -8.50467  1.000 35.67523 ?  327 HOH   A O    1 
HETATM 4982 O  O    . HOH   F 4 .   ? 33.07855 7.84577   8.10413   1.000 21.74199 ?  328 HOH   A O    1 
HETATM 4983 O  O    . HOH   F 4 .   ? 12.84552 -8.67400  10.22249  1.000 21.86085 ?  329 HOH   A O    1 
HETATM 4984 O  O    . HOH   F 4 .   ? 18.97805 8.49829   19.36629  1.000 43.23103 ?  330 HOH   A O    1 
HETATM 4985 O  O    B HOH   F 4 .   ? -1.82428 -0.23712  2.91941   1.000 35.74697 ?  331 HOH   A O    1 
HETATM 4986 O  O    . HOH   F 4 .   ? 3.35641  -8.44182  3.25702   1.000 17.83936 ?  332 HOH   A O    1 
HETATM 4987 O  O    . HOH   F 4 .   ? 20.85411 -6.43941  -15.34065 1.000 39.59339 ?  333 HOH   A O    1 
HETATM 4988 O  O    . HOH   F 4 .   ? 17.91008 15.84076  -9.47894  1.000 35.65548 ?  334 HOH   A O    1 
HETATM 4989 O  O    . HOH   F 4 .   ? 20.59138 9.86298   1.68208   1.000 16.01290 ?  335 HOH   A O    1 
HETATM 4990 O  O    . HOH   F 4 .   ? 20.61819 9.15445   4.31762   1.000 15.32939 ?  336 HOH   A O    1 
HETATM 4991 O  O    . HOH   F 4 .   ? 23.05683 -11.72255 -1.56293  1.000 30.71911 ?  337 HOH   A O    1 
HETATM 4992 O  O    . HOH   F 4 .   ? 5.61525  -0.56586  -7.92585  1.000 15.91850 ?  338 HOH   A O    1 
HETATM 4993 O  O    . HOH   F 4 .   ? 7.05140  13.28116  9.78634   1.000 51.76481 ?  339 HOH   A O    1 
HETATM 4994 O  O    . HOH   F 4 .   ? 21.24423 17.10497  1.70846   1.000 35.52765 ?  340 HOH   A O    1 
HETATM 4995 O  O    . HOH   F 4 .   ? 26.12168 -6.96600  -5.29849  1.000 32.26903 ?  341 HOH   A O    1 
HETATM 4996 O  O    . HOH   F 4 .   ? 16.76068 9.15251   11.74919  1.000 15.27715 ?  342 HOH   A O    1 
HETATM 4997 O  O    . HOH   F 4 .   ? 4.70318  7.55738   2.07139   1.000 17.48798 ?  343 HOH   A O    1 
HETATM 4998 O  O    . HOH   F 4 .   ? 16.41785 -9.85972  -10.19642 1.000 22.54447 ?  344 HOH   A O    1 
HETATM 4999 O  O    . HOH   F 4 .   ? 2.17355  7.92509   3.07357   1.000 22.86449 ?  345 HOH   A O    1 
HETATM 5000 O  O    . HOH   F 4 .   ? 15.57845 21.45147  -4.59198  1.000 28.42253 ?  346 HOH   A O    1 
HETATM 5001 O  O    . HOH   F 4 .   ? 27.02942 5.67688   -2.90934  1.000 21.13377 ?  347 HOH   A O    1 
HETATM 5002 O  O    . HOH   F 4 .   ? 14.90640 -10.97828 -12.31284 1.000 25.64170 ?  348 HOH   A O    1 
HETATM 5003 O  O    . HOH   F 4 .   ? 8.12592  -0.42893  -6.71180  1.000 14.60900 ?  349 HOH   A O    1 
HETATM 5004 O  O    . HOH   F 4 .   ? 25.82104 6.20771   16.97826  1.000 17.86036 ?  350 HOH   A O    1 
HETATM 5005 O  O    . HOH   F 4 .   ? 10.53456 14.85248  -2.41776  1.000 16.59131 ?  351 HOH   A O    1 
HETATM 5006 O  O    . HOH   F 4 .   ? 16.64491 -7.60487  -8.50225  1.000 18.81849 ?  352 HOH   A O    1 
HETATM 5007 O  O    . HOH   F 4 .   ? 22.87428 0.35021   -6.18398  1.000 20.32160 ?  353 HOH   A O    1 
HETATM 5008 O  O    . HOH   F 4 .   ? 9.83188  9.30142   15.42386  1.000 44.76015 ?  354 HOH   A O    1 
HETATM 5009 O  O    . HOH   F 4 .   ? 8.47319  -2.05846  -13.39825 1.000 26.63149 ?  355 HOH   A O    1 
HETATM 5010 O  O    . HOH   F 4 .   ? 24.81786 8.28873   -2.71980  1.000 17.88807 ?  356 HOH   A O    1 
HETATM 5011 O  O    . HOH   F 4 .   ? 11.27379 -4.82462  -13.86251 1.000 28.45511 ?  357 HOH   A O    1 
HETATM 5012 O  O    . HOH   F 4 .   ? 5.34549  9.50756   0.32759   1.000 19.00783 ?  358 HOH   A O    1 
HETATM 5013 O  O    . HOH   F 4 .   ? 2.55189  -0.68907  -3.15169  1.000 16.92066 ?  359 HOH   A O    1 
HETATM 5014 O  O    . HOH   F 4 .   ? 17.04960 4.46614   -15.85092 1.000 30.85433 ?  360 HOH   A O    1 
HETATM 5015 O  O    . HOH   F 4 .   ? 23.28117 6.07096   -13.39083 1.000 32.19814 ?  361 HOH   A O    1 
HETATM 5016 O  O    . HOH   F 4 .   ? 9.97991  15.42865  2.92408   1.000 19.63581 ?  362 HOH   A O    1 
HETATM 5017 O  O    . HOH   F 4 .   ? 6.42857  4.07483   15.55922  1.000 35.64657 ?  363 HOH   A O    1 
HETATM 5018 O  O    . HOH   F 4 .   ? 4.57678  -3.01431  -8.53996  1.000 20.45287 ?  364 HOH   A O    1 
HETATM 5019 O  O    . HOH   F 4 .   ? 5.31594  -14.92759 0.21676   1.000 38.03202 ?  365 HOH   A O    1 
HETATM 5020 O  O    . HOH   F 4 .   ? 2.51007  10.53768  -3.77284  1.000 30.04862 ?  366 HOH   A O    1 
HETATM 5021 O  O    . HOH   F 4 .   ? 14.74452 15.85262  3.74196   1.000 20.70416 ?  367 HOH   A O    1 
HETATM 5022 O  O    . HOH   F 4 .   ? 16.51374 -13.25360 -2.43062  1.000 31.09431 ?  368 HOH   A O    1 
HETATM 5023 O  O    . HOH   F 4 .   ? 24.37231 2.02838   -4.53504  1.000 18.98484 ?  369 HOH   A O    1 
HETATM 5024 O  O    . HOH   F 4 .   ? 31.06436 0.25972   4.53237   1.000 31.30062 ?  370 HOH   A O    1 
HETATM 5025 O  O    . HOH   F 4 .   ? 2.11201  2.44824   10.35885  1.000 25.52603 ?  371 HOH   A O    1 
HETATM 5026 O  O    . HOH   F 4 .   ? 2.20174  -8.28752  0.12321   1.000 41.58706 ?  372 HOH   A O    1 
HETATM 5027 O  O    . HOH   F 4 .   ? 19.71924 20.47795  7.59990   1.000 27.63771 ?  373 HOH   A O    1 
HETATM 5028 O  O    . HOH   F 4 .   ? 21.44499 9.78653   12.41668  1.000 24.95559 ?  374 HOH   A O    1 
HETATM 5029 O  O    . HOH   F 4 .   ? 26.83837 -4.60573  -10.01667 1.000 38.00204 ?  375 HOH   A O    1 
HETATM 5030 O  O    . HOH   F 4 .   ? 16.47257 -17.36086 -0.59138  1.000 45.22159 ?  376 HOH   A O    1 
HETATM 5031 O  O    . HOH   F 4 .   ? -0.28340 13.54851  1.86728   1.000 41.44576 ?  377 HOH   A O    1 
HETATM 5032 O  O    . HOH   F 4 .   ? 25.87283 10.58671  10.01980  1.000 36.46851 ?  378 HOH   A O    1 
HETATM 5033 O  O    . HOH   F 4 .   ? 4.11027  -16.00901 -6.14135  1.000 29.58220 ?  379 HOH   A O    1 
HETATM 5034 O  O    . HOH   F 4 .   ? 7.98599  9.46408   -0.73094  1.000 16.87469 ?  380 HOH   A O    1 
HETATM 5035 O  O    . HOH   F 4 .   ? 13.06137 13.61508  -11.01847 1.000 28.20846 ?  381 HOH   A O    1 
HETATM 5036 O  O    . HOH   F 4 .   ? 8.76928  9.51241   -9.18030  1.000 34.57651 ?  382 HOH   A O    1 
HETATM 5037 O  O    . HOH   F 4 .   ? 2.27085  -2.89836  -11.97081 1.000 27.08417 ?  383 HOH   A O    1 
HETATM 5038 O  O    . HOH   F 4 .   ? 13.29934 -12.89874 -11.23002 1.000 23.07123 ?  384 HOH   A O    1 
HETATM 5039 O  O    . HOH   F 4 .   ? 15.66016 15.56556  12.14376  1.000 31.31556 ?  385 HOH   A O    1 
HETATM 5040 O  O    . HOH   F 4 .   ? 4.66478  13.30947  7.35789   1.000 35.27522 ?  386 HOH   A O    1 
HETATM 5041 O  O    . HOH   F 4 .   ? 24.43796 -9.60767  -2.75961  1.000 35.69332 ?  387 HOH   A O    1 
HETATM 5042 O  O    . HOH   F 4 .   ? 0.55159  -4.84370  -12.90741 1.000 22.38009 ?  388 HOH   A O    1 
HETATM 5043 O  O    . HOH   F 4 .   ? 16.14116 -4.90173  -14.56587 1.000 38.47582 ?  389 HOH   A O    1 
HETATM 5044 O  O    . HOH   F 4 .   ? 29.66239 -10.87436 1.33555   1.000 28.99527 ?  390 HOH   A O    1 
HETATM 5045 O  O    . HOH   F 4 .   ? 3.47890  4.33091   12.13434  1.000 26.07925 ?  391 HOH   A O    1 
HETATM 5046 O  O    . HOH   F 4 .   ? 22.74232 6.60974   19.99308  1.000 41.29494 ?  392 HOH   A O    1 
HETATM 5047 O  O    . HOH   F 4 .   ? 25.56624 -1.40559  16.15535  1.000 31.72450 ?  393 HOH   A O    1 
HETATM 5048 O  O    . HOH   F 4 .   ? 1.91935  -9.97228  -6.83262  1.000 39.37672 ?  394 HOH   A O    1 
HETATM 5049 O  O    . HOH   F 4 .   ? 20.81499 8.75855   -13.12412 1.000 21.54923 ?  395 HOH   A O    1 
HETATM 5050 O  O    . HOH   F 4 .   ? 13.52781 -18.77364 -1.54274  1.000 23.10675 ?  396 HOH   A O    1 
HETATM 5051 O  O    . HOH   F 4 .   ? 15.52124 -0.41440  -15.04495 1.000 29.94715 ?  397 HOH   A O    1 
HETATM 5052 O  O    . HOH   F 4 .   ? 33.11140 14.54865  9.34036   1.000 38.70597 ?  398 HOH   A O    1 
HETATM 5053 O  O    . HOH   F 4 .   ? 10.94295 -20.01358 -2.87383  1.000 39.52440 ?  399 HOH   A O    1 
HETATM 5054 O  O    . HOH   F 4 .   ? 17.66970 21.24821  -8.05120  1.000 26.85763 ?  400 HOH   A O    1 
HETATM 5055 O  O    . HOH   F 4 .   ? 0.32965  4.32445   7.83808   1.000 74.87989 ?  401 HOH   A O    1 
HETATM 5056 O  O    . HOH   F 4 .   ? 22.41103 13.03994  -7.42994  1.000 27.54393 ?  402 HOH   A O    1 
HETATM 5057 O  O    . HOH   F 4 .   ? 34.84469 11.43253  8.53543   1.000 46.96914 ?  403 HOH   A O    1 
HETATM 5058 O  O    . HOH   F 4 .   ? -0.04247 -6.88296  0.98005   1.000 23.97793 ?  404 HOH   A O    1 
HETATM 5059 O  O    . HOH   F 4 .   ? 22.64303 -11.37072 -10.24315 1.000 45.21748 ?  405 HOH   A O    1 
HETATM 5060 O  O    . HOH   F 4 .   ? 8.19324  8.48189   -11.42781 1.000 42.08327 ?  406 HOH   A O    1 
HETATM 5061 O  O    . HOH   F 4 .   ? 21.85405 -10.05294 5.20989   1.000 23.09201 ?  407 HOH   A O    1 
HETATM 5062 O  O    . HOH   F 4 .   ? 17.82537 13.95174  -5.25389  1.000 19.85296 ?  408 HOH   A O    1 
HETATM 5063 O  O    . HOH   F 4 .   ? 6.00887  -13.50695 9.41496   1.000 36.62859 ?  409 HOH   A O    1 
HETATM 5064 O  O    . HOH   F 4 .   ? 27.15570 -5.75931  3.63342   1.000 31.50034 ?  410 HOH   A O    1 
HETATM 5065 O  O    . HOH   F 4 .   ? 6.68325  14.21745  4.21677   1.000 22.05898 ?  411 HOH   A O    1 
HETATM 5066 O  O    . HOH   F 4 .   ? 24.97089 -4.78314  5.87142   1.000 33.41845 ?  412 HOH   A O    1 
HETATM 5067 O  O    . HOH   F 4 .   ? 10.23646 -2.56181  23.04111  1.000 89.39376 ?  413 HOH   A O    1 
HETATM 5068 O  O    . HOH   F 4 .   ? 13.51472 17.74999  8.12761   1.000 24.38619 ?  414 HOH   A O    1 
HETATM 5069 O  O    . HOH   F 4 .   ? 19.97099 11.32066  -12.83135 1.000 24.07075 ?  415 HOH   A O    1 
HETATM 5070 O  O    . HOH   F 4 .   ? -1.55092 18.41236  -6.40615  1.000 37.20888 ?  416 HOH   A O    1 
HETATM 5071 O  O    . HOH   F 4 .   ? 0.83460  0.90548   6.17053   1.000 20.40624 ?  417 HOH   A O    1 
HETATM 5072 O  O    . HOH   F 4 .   ? 22.30926 -1.81080  16.48082  1.000 38.91731 ?  418 HOH   A O    1 
HETATM 5073 O  O    . HOH   F 4 .   ? 20.28922 12.98279  -5.05529  1.000 20.65454 ?  419 HOH   A O    1 
HETATM 5074 O  O    . HOH   F 4 .   ? 10.24605 -1.44762  -17.04406 1.000 37.63011 ?  420 HOH   A O    1 
HETATM 5075 O  O    . HOH   F 4 .   ? -0.39230 2.25647   3.84664   1.000 41.89384 ?  421 HOH   A O    1 
HETATM 5076 O  O    . HOH   F 4 .   ? 14.35031 -12.65174 -3.83568  1.000 17.94368 ?  422 HOH   A O    1 
HETATM 5077 O  O    . HOH   F 4 .   ? 27.74551 11.92848  5.44779   1.000 47.89846 ?  423 HOH   A O    1 
HETATM 5078 O  O    . HOH   F 4 .   ? 17.75462 10.66193  18.73898  1.000 32.74119 ?  424 HOH   A O    1 
HETATM 5079 O  O    . HOH   F 4 .   ? 2.44634  16.45162  -5.34796  1.000 38.00115 ?  425 HOH   A O    1 
HETATM 5080 O  O    . HOH   F 4 .   ? 13.04941 -14.59927 4.76087   1.000 45.65545 ?  426 HOH   A O    1 
HETATM 5081 O  O    . HOH   F 4 .   ? 10.05502 18.24001  -9.77704  1.000 24.79481 ?  427 HOH   A O    1 
HETATM 5082 O  O    . HOH   F 4 .   ? 27.66591 -0.10568  -4.12399  1.000 20.95399 ?  428 HOH   A O    1 
HETATM 5083 O  O    . HOH   F 4 .   ? 20.42207 16.89292  4.71843   1.000 30.11389 ?  429 HOH   A O    1 
HETATM 5084 O  O    . HOH   F 4 .   ? 10.50485 -10.07071 -17.19516 1.000 45.70834 ?  430 HOH   A O    1 
HETATM 5085 O  O    . HOH   F 4 .   ? 3.34587  -14.86607 -3.53123  1.000 41.49232 ?  431 HOH   A O    1 
HETATM 5086 O  O    . HOH   F 4 .   ? 11.55656 -14.68085 -14.13427 1.000 47.86483 ?  432 HOH   A O    1 
HETATM 5087 O  O    . HOH   F 4 .   ? 16.79979 18.14069  -5.60675  1.000 39.87139 ?  433 HOH   A O    1 
HETATM 5088 O  O    . HOH   F 4 .   ? 10.91274 0.07598   -13.16525 1.000 19.01931 ?  434 HOH   A O    1 
HETATM 5089 O  O    . HOH   F 4 .   ? 19.37960 -6.57868  -17.26197 1.000 59.00063 ?  435 HOH   A O    1 
HETATM 5090 O  O    . HOH   F 4 .   ? 17.55759 16.20024  -6.62124  1.000 41.92943 ?  436 HOH   A O    1 
HETATM 5091 O  O    . HOH   F 4 .   ? 8.79612  -1.87379  13.36837  1.000 32.05802 ?  437 HOH   A O    1 
HETATM 5092 O  O    . HOH   F 4 .   ? 14.71618 -1.89581  22.75896  1.000 40.18953 ?  438 HOH   A O    1 
HETATM 5093 O  O    . HOH   F 4 .   ? 27.05768 8.22584   -11.94657 1.000 51.78008 ?  439 HOH   A O    1 
HETATM 5094 O  O    . HOH   F 4 .   ? 17.80033 17.61090  11.20790  1.000 81.13708 ?  440 HOH   A O    1 
HETATM 5095 O  O    . HOH   F 4 .   ? 15.44983 -15.77726 3.26019   1.000 50.63816 ?  441 HOH   A O    1 
HETATM 5096 O  O    . HOH   F 4 .   ? 7.88301  0.91588   11.51839  1.000 30.63482 ?  442 HOH   A O    1 
HETATM 5097 O  O    . HOH   F 4 .   ? 5.37626  6.57371   -2.13308  1.000 25.97488 ?  443 HOH   A O    1 
HETATM 5098 O  O    . HOH   F 4 .   ? 12.32043 22.57914  -5.12251  1.000 30.51847 ?  444 HOH   A O    1 
HETATM 5099 O  O    . HOH   F 4 .   ? 1.02434  20.14056  -2.65751  1.000 28.28876 ?  445 HOH   A O    1 
HETATM 5100 O  O    . HOH   F 4 .   ? 11.54398 1.87076   -15.27335 1.000 35.34030 ?  446 HOH   A O    1 
HETATM 5101 O  O    . HOH   F 4 .   ? 4.31987  2.94956   14.20591  1.000 28.47825 ?  447 HOH   A O    1 
HETATM 5102 O  O    . HOH   F 4 .   ? 6.59642  2.15920   17.17673  1.000 36.03656 ?  448 HOH   A O    1 
HETATM 5103 O  O    . HOH   F 4 .   ? 5.93328  0.93172   12.32268  1.000 41.38348 ?  449 HOH   A O    1 
HETATM 5104 O  O    . HOH   F 4 .   ? 26.99212 2.91700   -7.90387  1.000 31.94101 ?  450 HOH   A O    1 
HETATM 5105 O  O    . HOH   F 4 .   ? 7.22597  16.50402  2.03972   1.000 36.83687 ?  451 HOH   A O    1 
HETATM 5106 O  O    . HOH   F 4 .   ? 3.86738  8.66415   -2.29468  1.000 32.73964 ?  452 HOH   A O    1 
HETATM 5107 O  O    . HOH   F 4 .   ? 17.93058 -0.04237  -14.38840 1.000 40.59175 ?  453 HOH   A O    1 
HETATM 5108 O  O    . HOH   F 4 .   ? 18.97508 -4.37313  -15.93214 1.000 41.68448 ?  454 HOH   A O    1 
HETATM 5109 O  O    . HOH   F 4 .   ? 22.23894 12.91321  -12.43629 1.000 32.44529 ?  455 HOH   A O    1 
HETATM 5110 O  O    . HOH   F 4 .   ? 14.11653 16.23068  10.04398  1.000 50.08425 ?  456 HOH   A O    1 
HETATM 5111 O  O    . HOH   F 4 .   ? 1.95874  5.74154   13.66277  1.000 55.59031 ?  457 HOH   A O    1 
HETATM 5112 O  O    . HOH   F 4 .   ? 8.52515  11.32260  14.09944  1.000 41.54970 ?  458 HOH   A O    1 
HETATM 5113 O  O    . HOH   F 4 .   ? 8.11457  -14.26651 10.09605  1.000 34.73426 ?  459 HOH   A O    1 
HETATM 5114 O  O    . HOH   F 4 .   ? 2.09528  -9.70713  -14.54378 1.000 49.93083 ?  460 HOH   A O    1 
HETATM 5115 O  O    . HOH   F 4 .   ? 0.36657  -2.04251  -3.94108  1.000 39.40564 ?  461 HOH   A O    1 
HETATM 5116 O  O    . HOH   F 4 .   ? 12.39340 4.52268   -15.01432 1.000 30.01522 ?  462 HOH   A O    1 
HETATM 5117 O  O    . HOH   F 4 .   ? 11.99050 -2.36476  -14.75710 1.000 29.91967 ?  463 HOH   A O    1 
HETATM 5118 O  O    . HOH   F 4 .   ? 0.33984  -11.40615 5.19781   1.000 56.08774 ?  464 HOH   A O    1 
HETATM 5119 O  O    . HOH   F 4 .   ? 8.31609  -4.05651  25.45568  1.000 51.27423 ?  465 HOH   A O    1 
HETATM 5120 O  O    . HOH   F 4 .   ? 23.99399 10.74308  11.76618  1.000 38.17256 ?  466 HOH   A O    1 
HETATM 5121 O  O    . HOH   F 4 .   ? 5.53366  0.52329   -10.49882 1.000 21.70811 ?  467 HOH   A O    1 
HETATM 5122 O  O    . HOH   F 4 .   ? 17.58217 20.05429  -4.10456  1.000 44.54441 ?  468 HOH   A O    1 
HETATM 5123 O  O    . HOH   F 4 .   ? 25.37311 8.92292   16.82882  1.000 33.40954 ?  469 HOH   A O    1 
HETATM 5124 O  O    . HOH   F 4 .   ? 7.52982  -0.42576  13.89845  1.000 44.27633 ?  470 HOH   A O    1 
HETATM 5125 O  O    . HOH   F 4 .   ? 1.80438  -2.28698  -9.32222  1.000 31.66646 ?  471 HOH   A O    1 
HETATM 5126 O  O    . HOH   F 4 .   ? 22.85649 -8.18746  -15.61865 1.000 29.94583 ?  472 HOH   A O    1 
HETATM 5127 O  O    . HOH   F 4 .   ? 14.22143 -9.43535  12.33130  1.000 41.63781 ?  473 HOH   A O    1 
HETATM 5128 O  O    . HOH   F 4 .   ? 16.90038 17.74220  3.72558   1.000 29.41209 ?  474 HOH   A O    1 
HETATM 5129 O  O    . HOH   F 4 .   ? -2.53552 12.98975  0.67442   1.000 33.92110 ?  475 HOH   A O    1 
HETATM 5130 O  O    . HOH   F 4 .   ? -0.30447 3.89492   1.75217   1.000 47.86610 ?  476 HOH   A O    1 
HETATM 5131 O  O    . HOH   F 4 .   ? 27.19404 11.11980  12.20186  1.000 50.25178 ?  477 HOH   A O    1 
HETATM 5132 O  O    . HOH   F 4 .   ? 14.49993 -2.83868  -15.30774 1.000 29.68746 ?  478 HOH   A O    1 
HETATM 5133 O  O    . HOH   F 4 .   ? 25.24768 -7.85850  -15.33182 1.000 37.89406 ?  479 HOH   A O    1 
HETATM 5134 O  O    . HOH   F 4 .   ? 5.96318  5.93496   17.00154  1.000 40.56203 ?  480 HOH   A O    1 
HETATM 5135 O  O    . HOH   F 4 .   ? 21.98268 14.94239  -3.68002  1.000 32.38475 ?  481 HOH   A O    1 
HETATM 5136 O  O    . HOH   F 4 .   ? 23.54398 8.96375   -14.25799 1.000 30.12549 ?  482 HOH   A O    1 
HETATM 5137 O  O    . HOH   F 4 .   ? -3.07391 12.36814  -1.61545  1.000 37.84883 ?  483 HOH   A O    1 
HETATM 5138 O  O    . HOH   F 4 .   ? 2.69782  0.26415   11.86896  1.000 33.31899 ?  484 HOH   A O    1 
HETATM 5139 O  O    . HOH   F 4 .   ? -2.84689 -7.56782  1.46696   1.000 35.00298 ?  485 HOH   A O    1 
HETATM 5140 O  O    . HOH   F 4 .   ? 15.65057 5.95073   -17.99833 1.000 33.35603 ?  486 HOH   A O    1 
HETATM 5141 O  O    . HOH   F 4 .   ? 24.34413 11.20662  -13.62735 1.000 36.71609 ?  487 HOH   A O    1 
HETATM 5142 O  O    . HOH   G 4 .   ? 53.01896 5.25101   34.13540  1.000 65.29709 ?  301 HOH   B O    1 
HETATM 5143 O  O    . HOH   G 4 .   ? 52.63545 3.69532   37.39505  1.000 31.49971 ?  302 HOH   B O    1 
HETATM 5144 O  O    . HOH   G 4 .   ? 52.37143 0.91722   9.76984   1.000 36.07236 ?  303 HOH   B O    1 
HETATM 5145 O  O    . HOH   G 4 .   ? 41.19483 -16.78639 32.48918  1.000 34.25467 ?  304 HOH   B O    1 
HETATM 5146 O  O    . HOH   G 4 .   ? 34.26089 15.68959  11.34598  1.000 24.16727 ?  305 HOH   B O    1 
HETATM 5147 O  O    a HOH   G 4 .   ? 51.80986 -0.34034  4.84812   0.421 20.01334 ?  306 HOH   B O    1 
HETATM 5148 O  O    . HOH   G 4 .   ? 41.87307 -13.93461 30.43177  1.000 33.52870 ?  307 HOH   B O    1 
HETATM 5149 O  O    . HOH   G 4 .   ? 42.95848 2.74839   5.52243   1.000 44.15288 ?  308 HOH   B O    1 
HETATM 5150 O  O    . HOH   G 4 .   ? 38.82453 -1.90928  3.21172   1.000 31.16266 ?  309 HOH   B O    1 
HETATM 5151 O  O    . HOH   G 4 .   ? 48.07406 7.32220   10.66198  1.000 36.03305 ?  310 HOH   B O    1 
HETATM 5152 O  O    . HOH   G 4 .   ? 54.42940 -1.33605  25.53176  1.000 27.53003 ?  311 HOH   B O    1 
HETATM 5153 O  O    . HOH   G 4 .   ? 33.36613 -0.87221  3.75679   1.000 30.83802 ?  312 HOH   B O    1 
HETATM 5154 O  O    . HOH   G 4 .   ? 45.12346 -13.51304 6.76976   1.000 39.58094 ?  313 HOH   B O    1 
HETATM 5155 O  O    . HOH   G 4 .   ? 33.90408 -16.71554 26.33646  1.000 36.04893 ?  314 HOH   B O    1 
HETATM 5156 O  O    . HOH   G 4 .   ? 32.43668 -7.32859  36.16185  1.000 31.54870 ?  315 HOH   B O    1 
HETATM 5157 O  O    . HOH   G 4 .   ? 56.02026 -12.54639 18.31701  1.000 44.93885 ?  316 HOH   B O    1 
HETATM 5158 O  O    . HOH   G 4 .   ? 38.77031 -12.60702 17.43736  1.000 23.90201 ?  317 HOH   B O    1 
HETATM 5159 O  O    . HOH   G 4 .   ? 42.10507 -4.28823  0.27595   1.000 35.58833 ?  318 HOH   B O    1 
HETATM 5160 O  O    . HOH   G 4 .   ? 31.06307 -4.03849  25.08900  1.000 19.96848 ?  319 HOH   B O    1 
HETATM 5161 O  O    . HOH   G 4 .   ? 41.51123 8.23064   20.66458  1.000 23.01970 ?  320 HOH   B O    1 
HETATM 5162 O  O    . HOH   G 4 .   ? 38.55950 -10.58522 35.01064  1.000 37.47275 ?  321 HOH   B O    1 
HETATM 5163 O  O    . HOH   G 4 .   ? 58.36580 -1.20359  18.76685  1.000 26.37639 ?  322 HOH   B O    1 
HETATM 5164 O  O    . HOH   G 4 .   ? 32.62317 -11.48503 27.83221  1.000 26.63143 ?  323 HOH   B O    1 
HETATM 5165 O  O    . HOH   G 4 .   ? 34.95443 -0.87138  36.38207  1.000 38.44736 ?  324 HOH   B O    1 
HETATM 5166 O  O    . HOH   G 4 .   ? 29.16281 -8.11408  25.54188  1.000 28.35055 ?  325 HOH   B O    1 
HETATM 5167 O  O    . HOH   G 4 .   ? 53.09313 -11.71524 25.74510  1.000 42.34064 ?  326 HOH   B O    1 
HETATM 5168 O  O    . HOH   G 4 .   ? 55.01870 4.83102   20.67306  1.000 27.42533 ?  327 HOH   B O    1 
HETATM 5169 O  O    . HOH   G 4 .   ? 26.15192 -4.69298  12.82362  1.000 17.62301 ?  328 HOH   B O    1 
HETATM 5170 O  O    . HOH   G 4 .   ? 43.35281 18.24503  12.45947  1.000 32.64985 ?  329 HOH   B O    1 
HETATM 5171 O  O    . HOH   G 4 .   ? 31.97063 6.21715   31.02868  1.000 20.25234 ?  330 HOH   B O    1 
HETATM 5172 O  O    . HOH   G 4 .   ? 47.86409 8.29420   30.43000  1.000 36.26953 ?  331 HOH   B O    1 
HETATM 5173 O  O    . HOH   G 4 .   ? 45.73490 19.27619  15.24784  1.000 25.21034 ?  332 HOH   B O    1 
HETATM 5174 O  O    . HOH   G 4 .   ? 36.51509 -13.54331 27.20064  1.000 39.50787 ?  333 HOH   B O    1 
HETATM 5175 O  O    . HOH   G 4 .   ? 38.32363 -5.22513  32.57737  1.000 19.18532 ?  334 HOH   B O    1 
HETATM 5176 O  O    . HOH   G 4 .   ? 38.45750 11.57705  11.77851  1.000 18.69038 ?  335 HOH   B O    1 
HETATM 5177 O  O    . HOH   G 4 .   ? 34.12701 0.12062   12.30866  1.000 13.98599 ?  336 HOH   B O    1 
HETATM 5178 O  O    . HOH   G 4 .   ? 31.67291 -4.06757  37.09845  1.000 38.00554 ?  337 HOH   B O    1 
HETATM 5179 O  O    . HOH   G 4 .   ? 27.09892 -3.93628  18.94931  1.000 18.60258 ?  338 HOH   B O    1 
HETATM 5180 O  O    . HOH   G 4 .   ? 34.70272 4.49011   1.85201   1.000 36.86135 ?  339 HOH   B O    1 
HETATM 5181 O  O    . HOH   G 4 .   ? 41.25671 -17.70359 29.66498  1.000 31.91878 ?  340 HOH   B O    1 
HETATM 5182 O  O    . HOH   G 4 .   ? 27.72989 -0.57085  17.68042  1.000 15.85180 ?  341 HOH   B O    1 
HETATM 5183 O  O    . HOH   G 4 .   ? 43.81771 6.62312   30.48550  1.000 22.41042 ?  342 HOH   B O    1 
HETATM 5184 O  O    . HOH   G 4 .   ? 25.00776 -0.67423  33.43099  1.000 29.13279 ?  343 HOH   B O    1 
HETATM 5185 O  O    . HOH   G 4 .   ? 29.76185 -4.35769  22.57028  1.000 21.37832 ?  344 HOH   B O    1 
HETATM 5186 O  O    . HOH   G 4 .   ? 32.01139 -3.16939  6.46470   1.000 34.53086 ?  345 HOH   B O    1 
HETATM 5187 O  O    A HOH   G 4 .   ? 51.01087 4.41954   30.53276  0.931 44.10663 ?  346 HOH   B O    1 
HETATM 5188 O  O    . HOH   G 4 .   ? 48.02567 13.93175  12.59430  1.000 70.36619 ?  347 HOH   B O    1 
HETATM 5189 O  O    . HOH   G 4 .   ? 44.57495 -9.29672  40.05562  1.000 44.67987 ?  348 HOH   B O    1 
HETATM 5190 O  O    . HOH   G 4 .   ? 32.51176 1.53644   13.97706  1.000 13.79233 ?  349 HOH   B O    1 
HETATM 5191 O  O    . HOH   G 4 .   ? 57.88257 -7.79945  24.36248  1.000 36.93393 ?  350 HOH   B O    1 
HETATM 5192 O  O    . HOH   G 4 .   ? 42.87357 -18.99913 27.96151  1.000 39.53757 ?  351 HOH   B O    1 
HETATM 5193 O  O    . HOH   G 4 .   ? 44.33312 0.87774   7.32983   1.000 27.65232 ?  352 HOH   B O    1 
HETATM 5194 O  O    . HOH   G 4 .   ? 43.39772 -6.50843  4.18738   1.000 22.62147 ?  353 HOH   B O    1 
HETATM 5195 O  O    . HOH   G 4 .   ? 47.97930 11.32727  17.67265  1.000 28.76256 ?  354 HOH   B O    1 
HETATM 5196 O  O    . HOH   G 4 .   ? 54.39400 8.17618   23.47220  1.000 38.03392 ?  355 HOH   B O    1 
HETATM 5197 O  O    . HOH   G 4 .   ? 35.13973 -18.71729 23.23015  1.000 39.70360 ?  356 HOH   B O    1 
HETATM 5198 O  O    . HOH   G 4 .   ? 35.81599 12.64097  16.35190  1.000 16.80071 ?  357 HOH   B O    1 
HETATM 5199 O  O    . HOH   G 4 .   ? 37.84501 20.63023  17.85993  1.000 38.54846 ?  358 HOH   B O    1 
HETATM 5200 O  O    . HOH   G 4 .   ? 35.04166 8.72581   10.07157  1.000 19.65635 ?  359 HOH   B O    1 
HETATM 5201 O  O    . HOH   G 4 .   ? 42.42646 15.12395  21.53452  1.000 29.54715 ?  360 HOH   B O    1 
HETATM 5202 O  O    . HOH   G 4 .   ? 44.13537 -11.67734 30.53524  1.000 35.57378 ?  361 HOH   B O    1 
HETATM 5203 O  O    . HOH   G 4 .   ? 39.88727 -15.16064 28.38068  1.000 35.28859 ?  362 HOH   B O    1 
HETATM 5204 O  O    . HOH   G 4 .   ? 42.44531 4.75265   28.96301  1.000 18.88665 ?  363 HOH   B O    1 
HETATM 5205 O  O    . HOH   G 4 .   ? 47.96095 10.05626  10.41364  1.000 38.04109 ?  364 HOH   B O    1 
HETATM 5206 O  O    . HOH   G 4 .   ? 43.35827 11.27234  18.15001  1.000 20.74019 ?  365 HOH   B O    1 
HETATM 5207 O  O    . HOH   G 4 .   ? 53.79710 -12.29508 30.35092  1.000 38.43807 ?  366 HOH   B O    1 
HETATM 5208 O  O    . HOH   G 4 .   ? 37.33469 15.08740  13.84939  1.000 29.59252 ?  367 HOH   B O    1 
HETATM 5209 O  O    . HOH   G 4 .   ? 27.16828 -4.72821  26.18592  1.000 52.42751 ?  368 HOH   B O    1 
HETATM 5210 O  O    . HOH   G 4 .   ? 39.97450 -14.12113 10.17652  1.000 18.62082 ?  369 HOH   B O    1 
HETATM 5211 O  O    . HOH   G 4 .   ? 40.78749 0.01082   7.00452   1.000 15.30829 ?  370 HOH   B O    1 
HETATM 5212 O  O    . HOH   G 4 .   ? 40.71854 -22.76497 29.08184  1.000 22.15797 ?  371 HOH   B O    1 
HETATM 5213 O  O    . HOH   G 4 .   ? 26.05163 -2.00410  13.35560  1.000 17.02745 ?  372 HOH   B O    1 
HETATM 5214 O  O    . HOH   G 4 .   ? 39.43023 -5.37935  37.88474  1.000 25.18273 ?  373 HOH   B O    1 
HETATM 5215 O  O    . HOH   G 4 .   ? 20.88537 1.38439   29.93287  1.000 22.63653 ?  374 HOH   B O    1 
HETATM 5216 O  O    . HOH   G 4 .   ? 40.95144 6.93296   6.54713   1.000 24.50204 ?  375 HOH   B O    1 
HETATM 5217 O  O    . HOH   G 4 .   ? 50.97083 -9.63361  18.89613  1.000 21.05586 ?  376 HOH   B O    1 
HETATM 5218 O  O    . HOH   G 4 .   ? 29.05289 -11.60477 22.63161  1.000 27.37562 ?  377 HOH   B O    1 
HETATM 5219 O  O    . HOH   G 4 .   ? 35.61196 13.84212  12.15210  1.000 24.04134 ?  378 HOH   B O    1 
HETATM 5220 O  O    . HOH   G 4 .   ? 45.67559 9.81718   17.97348  1.000 21.47286 ?  379 HOH   B O    1 
HETATM 5221 O  O    . HOH   G 4 .   ? 25.49008 -3.62841  29.55702  1.000 33.53949 ?  380 HOH   B O    1 
HETATM 5222 O  O    B HOH   G 4 .   ? 51.61337 2.52515   30.40725  0.860 44.01968 ?  381 HOH   B O    1 
HETATM 5223 O  O    . HOH   G 4 .   ? 42.64214 -14.44413 21.82726  1.000 27.20347 ?  382 HOH   B O    1 
HETATM 5224 O  O    . HOH   G 4 .   ? 46.80176 16.95718  16.18274  1.000 26.44754 ?  383 HOH   B O    1 
HETATM 5225 O  O    . HOH   G 4 .   ? 37.03652 -2.71732  5.20159   1.000 27.46335 ?  384 HOH   B O    1 
HETATM 5226 O  O    . HOH   G 4 .   ? 43.24648 -13.02344 42.33914  1.000 22.79254 ?  385 HOH   B O    1 
HETATM 5227 O  O    . HOH   G 4 .   ? 44.68929 -2.98710  0.22732   1.000 32.56915 ?  386 HOH   B O    1 
HETATM 5228 O  O    . HOH   G 4 .   ? 56.02098 -4.29852  27.27836  1.000 24.72308 ?  387 HOH   B O    1 
HETATM 5229 O  O    . HOH   G 4 .   ? 48.84461 -7.57220  3.33212   1.000 25.15537 ?  388 HOH   B O    1 
HETATM 5230 O  O    . HOH   G 4 .   ? 54.51181 -10.88142 22.66460  1.000 30.78950 ?  389 HOH   B O    1 
HETATM 5231 O  O    . HOH   G 4 .   ? 38.34112 1.84252   36.36536  1.000 38.62805 ?  390 HOH   B O    1 
HETATM 5232 O  O    . HOH   G 4 .   ? 36.31955 12.14519  25.59812  1.000 32.68371 ?  391 HOH   B O    1 
HETATM 5233 O  O    . HOH   G 4 .   ? 28.34548 12.57126  16.46703  1.000 30.05445 ?  392 HOH   B O    1 
HETATM 5234 O  O    . HOH   G 4 .   ? 52.94694 5.08703   12.09662  1.000 41.95923 ?  393 HOH   B O    1 
HETATM 5235 O  O    . HOH   G 4 .   ? 48.62056 6.99560   27.32294  1.000 29.74034 ?  394 HOH   B O    1 
HETATM 5236 O  O    . HOH   G 4 .   ? 50.32815 -12.35445 26.18635  1.000 44.46233 ?  395 HOH   B O    1 
HETATM 5237 O  O    . HOH   G 4 .   ? 59.66316 -3.67873  17.60721  1.000 20.77919 ?  396 HOH   B O    1 
HETATM 5238 O  O    . HOH   G 4 .   ? 38.88355 -6.10905  35.21416  1.000 23.71860 ?  397 HOH   B O    1 
HETATM 5239 O  O    . HOH   G 4 .   ? 45.34898 5.46999   32.48405  1.000 29.54823 ?  398 HOH   B O    1 
HETATM 5240 O  O    . HOH   G 4 .   ? 40.90534 9.92679   18.53988  1.000 18.12612 ?  399 HOH   B O    1 
HETATM 5241 O  O    . HOH   G 4 .   ? 41.95832 -6.17749  38.39672  1.000 31.12630 ?  400 HOH   B O    1 
HETATM 5242 O  O    . HOH   G 4 .   ? 33.07080 2.89224   34.39216  1.000 34.12428 ?  401 HOH   B O    1 
HETATM 5243 O  O    . HOH   G 4 .   ? 24.42759 -0.10102  20.37611  1.000 36.92512 ?  402 HOH   B O    1 
HETATM 5244 O  O    . HOH   G 4 .   ? 31.82351 -11.04878 8.02225   1.000 33.14362 ?  403 HOH   B O    1 
HETATM 5245 O  O    . HOH   G 4 .   ? 54.24600 -1.87112  6.19288   1.000 17.72453 ?  404 HOH   B O    1 
HETATM 5246 O  O    . HOH   G 4 .   ? 25.61314 -1.61983  27.59776  1.000 27.01374 ?  405 HOH   B O    1 
HETATM 5247 O  O    . HOH   G 4 .   ? 36.90581 5.71856   33.00950  1.000 28.33273 ?  406 HOH   B O    1 
HETATM 5248 O  O    . HOH   G 4 .   ? 53.43684 -8.74969  5.25146   1.000 20.54152 ?  407 HOH   B O    1 
HETATM 5249 O  O    . HOH   G 4 .   ? 52.80419 -2.70874  37.46913  1.000 31.86254 ?  408 HOH   B O    1 
HETATM 5250 O  O    . HOH   G 4 .   ? 30.62430 13.08686  23.88327  1.000 27.91840 ?  409 HOH   B O    1 
HETATM 5251 O  O    . HOH   G 4 .   ? 26.88419 -0.95678  36.90362  1.000 39.51017 ?  410 HOH   B O    1 
HETATM 5252 O  O    . HOH   G 4 .   ? 53.52528 6.02836   18.68156  1.000 30.24820 ?  411 HOH   B O    1 
HETATM 5253 O  O    . HOH   G 4 .   ? 28.98031 -8.85230  22.85240  1.000 20.31623 ?  412 HOH   B O    1 
HETATM 5254 O  O    . HOH   G 4 .   ? 28.52249 6.27033   17.88068  1.000 16.05669 ?  413 HOH   B O    1 
HETATM 5255 O  O    . HOH   G 4 .   ? 43.25366 -12.62124 7.74245   1.000 27.73809 ?  414 HOH   B O    1 
HETATM 5256 O  O    . HOH   G 4 .   ? 60.15147 -6.54412  27.68049  1.000 21.61535 ?  415 HOH   B O    1 
HETATM 5257 O  O    . HOH   G 4 .   ? 27.59000 -7.51047  30.23831  1.000 36.84276 ?  416 HOH   B O    1 
HETATM 5258 O  O    . HOH   G 4 .   ? 37.28573 10.22204  6.26486   1.000 23.93601 ?  417 HOH   B O    1 
HETATM 5259 O  O    . HOH   G 4 .   ? 51.21267 -17.33492 12.85214  1.000 53.21549 ?  418 HOH   B O    1 
HETATM 5260 O  O    . HOH   G 4 .   ? 41.41954 4.53455   5.75042   1.000 44.02526 ?  419 HOH   B O    1 
HETATM 5261 O  O    . HOH   G 4 .   ? 40.32721 14.97032  12.62075  1.000 27.40308 ?  420 HOH   B O    1 
HETATM 5262 O  O    . HOH   G 4 .   ? 54.22460 -1.14908  10.89893  1.000 24.76383 ?  421 HOH   B O    1 
HETATM 5263 O  O    . HOH   G 4 .   ? 27.13164 -7.51775  16.89780  1.000 28.88216 ?  422 HOH   B O    1 
HETATM 5264 O  O    . HOH   G 4 .   ? 44.48538 -9.07695  31.94304  1.000 26.11422 ?  423 HOH   B O    1 
HETATM 5265 O  O    . HOH   G 4 .   ? 50.48336 -12.63400 33.91697  1.000 31.30018 ?  424 HOH   B O    1 
HETATM 5266 O  O    . HOH   G 4 .   ? 29.39019 8.77834   18.03663  1.000 21.40843 ?  425 HOH   B O    1 
HETATM 5267 O  O    . HOH   G 4 .   ? 25.01237 5.32245   19.51302  1.000 23.75522 ?  426 HOH   B O    1 
HETATM 5268 O  O    . HOH   G 4 .   ? 43.75556 -17.74116 29.63887  1.000 28.64202 ?  427 HOH   B O    1 
HETATM 5269 O  O    . HOH   G 4 .   ? 43.36339 -4.05883  42.92504  1.000 30.38560 ?  428 HOH   B O    1 
HETATM 5270 O  O    . HOH   G 4 .   ? 39.81018 -1.76566  42.71407  1.000 41.23438 ?  429 HOH   B O    1 
HETATM 5271 O  O    . HOH   G 4 .   ? 24.65280 -6.42665  11.06027  1.000 42.78515 ?  430 HOH   B O    1 
HETATM 5272 O  O    . HOH   G 4 .   ? 29.07921 -9.48036  29.69004  1.000 40.82001 ?  431 HOH   B O    1 
HETATM 5273 O  O    . HOH   G 4 .   ? 60.93453 -7.75611  25.29040  1.000 45.80900 ?  432 HOH   B O    1 
HETATM 5274 O  O    . HOH   G 4 .   ? 45.75014 11.41002  10.13980  1.000 27.27274 ?  433 HOH   B O    1 
HETATM 5275 O  O    . HOH   G 4 .   ? 25.54251 5.51508   26.88289  1.000 22.11001 ?  434 HOH   B O    1 
HETATM 5276 O  O    . HOH   G 4 .   ? 49.14846 -13.95545 33.32074  1.000 34.85129 ?  435 HOH   B O    1 
HETATM 5277 O  O    . HOH   G 4 .   ? 53.25013 -14.52515 13.96332  1.000 48.24597 ?  436 HOH   B O    1 
HETATM 5278 O  O    . HOH   G 4 .   ? 34.61085 -12.86452 29.21748  1.000 41.59067 ?  437 HOH   B O    1 
HETATM 5279 O  O    . HOH   G 4 .   ? 37.17447 -16.42086 18.67958  1.000 40.71902 ?  438 HOH   B O    1 
HETATM 5280 O  O    . HOH   G 4 .   ? 29.75904 -2.54727  47.70607  1.000 55.09920 ?  439 HOH   B O    1 
HETATM 5281 O  O    . HOH   G 4 .   ? 23.69676 -9.44281  7.06386   1.000 30.08162 ?  440 HOH   B O    1 
HETATM 5282 O  O    . HOH   G 4 .   ? 50.92745 -9.25629  43.88976  1.000 33.18865 ?  441 HOH   B O    1 
HETATM 5283 O  O    . HOH   G 4 .   ? 54.52270 4.93526   16.14979  1.000 52.99794 ?  442 HOH   B O    1 
HETATM 5284 O  O    . HOH   G 4 .   ? 47.09397 10.76509  24.75434  1.000 46.53071 ?  443 HOH   B O    1 
HETATM 5285 O  O    . HOH   G 4 .   ? 44.03923 13.20970  11.05771  1.000 91.85196 ?  444 HOH   B O    1 
HETATM 5286 O  O    . HOH   G 4 .   ? 47.25631 -15.33473 30.94980  1.000 47.05934 ?  445 HOH   B O    1 
HETATM 5287 O  O    . HOH   G 4 .   ? 47.37942 7.42336   7.84407   1.000 39.70355 ?  446 HOH   B O    1 
HETATM 5288 O  O    . HOH   G 4 .   ? 52.57304 -2.29195  12.93910  1.000 37.57194 ?  447 HOH   B O    1 
HETATM 5289 O  O    . HOH   G 4 .   ? 23.96791 -7.99672  14.71674  1.000 46.03721 ?  448 HOH   B O    1 
HETATM 5290 O  O    A HOH   G 4 .   ? 53.26570 2.91374   12.01968  0.855 51.40989 ?  449 HOH   B O    1 
HETATM 5291 O  O    . HOH   G 4 .   ? 39.13501 12.75312  26.42546  1.000 47.79340 ?  450 HOH   B O    1 
HETATM 5292 O  O    . HOH   G 4 .   ? 51.42180 0.24924   13.49988  1.000 32.72206 ?  451 HOH   B O    1 
HETATM 5293 O  O    . HOH   G 4 .   ? 41.78028 12.85074  12.01345  1.000 35.10168 ?  452 HOH   B O    1 
HETATM 5294 O  O    . HOH   G 4 .   ? 39.76415 5.95412   35.45443  1.000 48.60281 ?  453 HOH   B O    1 
HETATM 5295 O  O    . HOH   G 4 .   ? 36.31189 14.43777  22.07480  1.000 42.77254 ?  454 HOH   B O    1 
HETATM 5296 O  O    . HOH   G 4 .   ? 24.89276 -6.89199  7.64109   1.000 29.85324 ?  455 HOH   B O    1 
HETATM 5297 O  O    . HOH   G 4 .   ? 25.16741 7.94096   25.50750  1.000 34.01336 ?  456 HOH   B O    1 
HETATM 5298 O  O    . HOH   G 4 .   ? 62.11213 -2.25352  25.15116  1.000 83.47175 ?  457 HOH   B O    1 
HETATM 5299 O  O    . HOH   G 4 .   ? 26.74305 -6.60217  19.39995  1.000 28.56402 ?  458 HOH   B O    1 
HETATM 5300 O  O    . HOH   G 4 .   ? 32.08030 -1.98863  36.66327  1.000 43.73410 ?  459 HOH   B O    1 
HETATM 5301 O  O    . HOH   G 4 .   ? 53.01611 -16.89373 14.60944  1.000 43.84611 ?  460 HOH   B O    1 
HETATM 5302 O  O    . HOH   G 4 .   ? 43.40326 10.12215  21.78891  1.000 34.36012 ?  461 HOH   B O    1 
HETATM 5303 O  O    . HOH   G 4 .   ? 26.85042 -7.62311  21.73786  1.000 38.48453 ?  462 HOH   B O    1 
HETATM 5304 O  O    . HOH   G 4 .   ? 42.78052 -6.03304  41.19511  1.000 39.22751 ?  463 HOH   B O    1 
HETATM 5305 O  O    . HOH   G 4 .   ? 24.40351 0.57980   29.24550  1.000 35.28444 ?  464 HOH   B O    1 
HETATM 5306 O  O    . HOH   G 4 .   ? 43.35564 12.67674  20.88225  1.000 32.65418 ?  465 HOH   B O    1 
HETATM 5307 O  O    . HOH   G 4 .   ? 27.24096 -5.59853  23.81093  1.000 41.76759 ?  466 HOH   B O    1 
HETATM 5308 O  O    . HOH   G 4 .   ? 51.72671 -12.37585 18.42555  1.000 34.95177 ?  467 HOH   B O    1 
HETATM 5309 O  O    . HOH   G 4 .   ? 27.44945 10.60465  17.99814  1.000 35.91420 ?  468 HOH   B O    1 
HETATM 5310 O  O    . HOH   G 4 .   ? 57.02502 -10.18758 23.44697  1.000 38.51288 ?  469 HOH   B O    1 
HETATM 5311 O  O    . HOH   G 4 .   ? 35.40004 16.57892  13.56911  1.000 39.22041 ?  470 HOH   B O    1 
HETATM 5312 O  O    . HOH   G 4 .   ? 31.26360 1.54696   33.15958  1.000 32.52771 ?  471 HOH   B O    1 
HETATM 5313 O  O    . HOH   G 4 .   ? 25.66405 -5.89672  15.22096  1.000 27.07014 ?  472 HOH   B O    1 
HETATM 5314 O  O    . HOH   G 4 .   ? 52.36104 2.20604   7.30336   1.000 40.00540 ?  473 HOH   B O    1 
HETATM 5315 O  O    . HOH   G 4 .   ? 41.87984 8.27883   32.00402  1.000 35.37090 ?  474 HOH   B O    1 
HETATM 5316 O  O    . HOH   G 4 .   ? 41.67387 -15.83995 19.65600  1.000 25.56284 ?  475 HOH   B O    1 
HETATM 5317 O  O    . HOH   G 4 .   ? 24.90719 -3.87184  17.09892  1.000 36.23634 ?  476 HOH   B O    1 
HETATM 5318 O  O    . HOH   G 4 .   ? 48.05625 16.20491  13.69529  1.000 93.91893 ?  477 HOH   B O    1 
HETATM 5319 O  O    . HOH   G 4 .   ? 39.94186 -14.95138 17.52040  1.000 34.09807 ?  478 HOH   B O    1 
HETATM 5320 O  O    . HOH   G 4 .   ? 42.67174 12.85882  26.00313  1.000 51.04287 ?  479 HOH   B O    1 
HETATM 5321 O  O    . HOH   G 4 .   ? 34.66555 1.62952   36.09852  1.000 37.01048 ?  480 HOH   B O    1 
HETATM 5322 O  O    . HOH   G 4 .   ? 29.97908 -6.57576  37.37252  1.000 38.83689 ?  481 HOH   B O    1 
HETATM 5323 O  O    . HOH   G 4 .   ? 23.90159 -1.63894  31.40066  1.000 36.76651 ?  482 HOH   B O    1 
HETATM 5324 O  O    . HOH   G 4 .   ? 34.22044 -3.42791  4.85389   1.000 41.14074 ?  483 HOH   B O    1 
HETATM 5325 O  O    B HOH   G 4 .   ? 54.00042 1.77174   13.86753  1.000 54.21146 ?  484 HOH   B O    1 
HETATM 5326 O  O    . HOH   G 4 .   ? 57.56288 1.35609   18.20200  1.000 37.04242 ?  485 HOH   B O    1 
HETATM 5327 O  O    . HOH   G 4 .   ? 34.22967 -10.71569 2.79639   1.000 44.94867 ?  486 HOH   B O    1 
HETATM 5328 O  O    . HOH   G 4 .   ? 26.75334 10.61209  14.83154  1.000 45.40665 ?  487 HOH   B O    1 
HETATM 5329 O  O    . HOH   G 4 .   ? 40.17917 -15.79117 12.36524  1.000 25.79488 ?  488 HOH   B O    1 
HETATM 5330 O  O    . HOH   G 4 .   ? 37.19183 18.03716  11.27105  1.000 45.16729 ?  489 HOH   B O    1 
HETATM 5331 O  O    . HOH   G 4 .   ? 55.96263 2.40318   15.93182  1.000 41.03381 ?  490 HOH   B O    1 
HETATM 5332 O  O    . HOH   G 4 .   ? 42.28177 -16.55140 13.94447  1.000 36.47467 ?  491 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    . LEU   A 5   ? 0.45681 0.49714 0.42711 -0.02865 -0.02907 0.03832  8   LEU   A N    
2    C  CA   . LEU   A 5   ? 0.33100 0.46874 0.37191 -0.09274 0.01416  0.06250  8   LEU   A CA   
3    C  C    . LEU   A 5   ? 0.27672 0.46716 0.28413 -0.08668 0.05682  0.05472  8   LEU   A C    
4    O  O    . LEU   A 5   ? 0.26459 0.45982 0.28492 -0.08983 -0.02004 0.03735  8   LEU   A O    
5    C  CB   . LEU   A 5   ? 0.39656 0.48678 0.43644 -0.06905 0.01426  0.05443  8   LEU   A CB   
6    C  CG   . LEU   A 5   ? 0.41962 0.51138 0.46739 -0.05260 -0.03780 0.01893  8   LEU   A CG   
7    C  CD1  . LEU   A 5   ? 0.44513 0.52433 0.46949 -0.07416 -0.04985 -0.00253 8   LEU   A CD1  
8    C  CD2  . LEU   A 5   ? 0.43713 0.52077 0.48610 -0.02254 -0.03315 0.02067  8   LEU   A CD2  
9    N  N    . GLN   A 6   ? 0.32956 0.46615 0.21383 -0.02640 0.05043  0.05287  9   GLN   A N    
10   C  CA   . GLN   A 6   ? 0.35448 0.49411 0.18804 -0.01622 0.06188  -0.01170 9   GLN   A CA   
11   C  C    . GLN   A 6   ? 0.31929 0.44640 0.18520 -0.03038 0.01724  -0.02591 9   GLN   A C    
12   O  O    . GLN   A 6   ? 0.34703 0.47107 0.21967 0.01682  0.01152  -0.00424 9   GLN   A O    
13   C  CB   . GLN   A 6   ? 0.42169 0.57861 0.22303 0.01192  0.08932  -0.06359 9   GLN   A CB   
14   C  CG   . GLN   A 6   ? 0.51572 0.67042 0.28421 -0.02989 0.06318  -0.06152 9   GLN   A CG   
15   C  CD   . GLN   A 6   ? 0.60557 0.74346 0.35303 -0.03490 0.01957  -0.03987 9   GLN   A CD   
16   O  OE1  . GLN   A 6   ? 0.64145 0.76849 0.39295 -0.03133 0.01772  -0.03154 9   GLN   A OE1  
17   N  NE2  . GLN   A 6   ? 0.63764 0.76964 0.37111 -0.04611 -0.00052 -0.02201 9   GLN   A NE2  
25   N  N    . ASN   A 7   ? 0.27654 0.38950 0.18092 -0.08515 0.01669  -0.02706 10  ASN   A N    
26   C  CA   . ASN   A 7   ? 0.28091 0.37235 0.16459 -0.09228 0.02814  -0.04363 10  ASN   A CA   
27   C  C    . ASN   A 7   ? 0.22856 0.37148 0.15018 -0.06943 0.02907  -0.04595 10  ASN   A C    
28   O  O    . ASN   A 7   ? 0.22075 0.37043 0.16694 -0.05598 0.03188  -0.02250 10  ASN   A O    
29   C  CB   . ASN   A 7   ? 0.30122 0.39350 0.19138 -0.11852 0.01728  -0.04709 10  ASN   A CB   
30   C  CG   . ASN   A 7   ? 0.39827 0.42237 0.20846 -0.12210 0.01144  -0.04365 10  ASN   A CG   
31   O  OD1  . ASN   A 7   ? 0.45285 0.40175 0.20605 -0.13034 -0.00058 -0.03946 10  ASN   A OD1  
32   N  ND2  . ASN   A 7   ? 0.43780 0.46385 0.24425 -0.12560 -0.00071 -0.05182 10  ASN   A ND2  
39   N  N    . ILE   A 8   ? 0.21107 0.36848 0.14967 -0.06340 0.01855  -0.05656 11  ILE   A N    
40   C  CA   . ILE   A 8   ? 0.21529 0.35628 0.16804 -0.03970 0.01825  -0.04300 11  ILE   A CA   
41   C  C    . ILE   A 8   ? 0.21002 0.33248 0.15875 -0.06007 0.02486  -0.06030 11  ILE   A C    
42   O  O    . ILE   A 8   ? 0.21694 0.42615 0.15459 -0.04729 0.04605  -0.07856 11  ILE   A O    
43   C  CB   . ILE   A 8   ? 0.28258 0.37813 0.23113 -0.03805 -0.00972 -0.01577 11  ILE   A CB   
44   C  CG1  . ILE   A 8   ? 0.38081 0.42284 0.28211 -0.01859 -0.00311 -0.01337 11  ILE   A CG1  
45   C  CG2  . ILE   A 8   ? 0.31763 0.37442 0.24755 -0.02363 -0.01280 0.01564  11  ILE   A CG2  
46   C  CD1  . ILE   A 8   ? 0.41100 0.42776 0.30251 -0.02978 0.02855  0.01020  11  ILE   A CD1  
58   N  N    . ILE   A 9   ? 0.18595 0.28652 0.13640 -0.04267 0.02052  -0.05331 12  ILE   A N    
59   C  CA   . ILE   A 9   ? 0.19033 0.24417 0.14386 -0.04060 0.02377  -0.01810 12  ILE   A CA   
60   C  C    . ILE   A 9   ? 0.18187 0.24468 0.13023 -0.04295 0.00855  -0.01735 12  ILE   A C    
61   O  O    . ILE   A 9   ? 0.18922 0.26729 0.14780 -0.04479 0.03287  -0.02453 12  ILE   A O    
62   C  CB   . ILE   A 9   ? 0.19201 0.23429 0.14959 -0.04833 0.02495  -0.02344 12  ILE   A CB   
63   C  CG1  . ILE   A 9   ? 0.21194 0.22920 0.16516 -0.02622 0.01653  -0.01584 12  ILE   A CG1  
64   C  CG2  . ILE   A 9   ? 0.22581 0.27660 0.17978 -0.04463 0.05956  -0.03496 12  ILE   A CG2  
65   C  CD1  . ILE   A 9   ? 0.23713 0.24995 0.17423 -0.03900 0.03272  -0.00009 12  ILE   A CD1  
77   N  N    . TYR   A 10  ? 0.18218 0.23372 0.12873 -0.02507 0.02416  -0.01230 13  TYR   A N    
78   C  CA   . TYR   A 10  ? 0.17697 0.23756 0.13121 -0.02007 0.02263  -0.00012 13  TYR   A CA   
79   C  C    . TYR   A 10  ? 0.16557 0.22737 0.13775 -0.03000 0.02431  -0.00040 13  TYR   A C    
80   O  O    . TYR   A 10  ? 0.17385 0.25813 0.12825 -0.02868 0.02119  -0.01751 13  TYR   A O    
81   C  CB   . TYR   A 10  ? 0.20617 0.26253 0.14618 -0.02312 0.02331  0.00299  13  TYR   A CB   
82   C  CG   . TYR   A 10  ? 0.23646 0.30009 0.15453 -0.00728 0.00992  0.01978  13  TYR   A CG   
83   C  CD1  . TYR   A 10  ? 0.23313 0.34211 0.17639 0.02613  0.01295  0.03505  13  TYR   A CD1  
84   C  CD2  . TYR   A 10  ? 0.28568 0.39344 0.16911 0.04657  -0.01078 0.00261  13  TYR   A CD2  
85   C  CE1  . TYR   A 10  ? 0.27986 0.37667 0.19910 0.01749  0.00407  0.04508  13  TYR   A CE1  
86   C  CE2  . TYR   A 10  ? 0.33328 0.43091 0.18798 0.05717  -0.03505 0.02064  13  TYR   A CE2  
87   C  CZ   . TYR   A 10  ? 0.29068 0.42692 0.20355 0.03706  -0.02881 0.06314  13  TYR   A CZ   
88   O  OH   . TYR   A 10  ? 0.30001 0.47542 0.23805 0.01772  -0.04558 0.07048  13  TYR   A OH   
98   N  N    . ASN   A 11  ? 0.17442 0.20920 0.13799 -0.01867 0.02556  -0.00928 14  ASN   A N    
99   C  CA   . ASN   A 11  ? 0.17508 0.18739 0.14250 -0.02496 0.01987  -0.01216 14  ASN   A CA   
100  C  C    . ASN   A 11  ? 0.17650 0.19688 0.12565 -0.01329 0.02793  -0.01345 14  ASN   A C    
101  O  O    . ASN   A 11  ? 0.18063 0.20432 0.12639 -0.02113 0.02286  -0.01882 14  ASN   A O    
102  C  CB   . ASN   A 11  ? 0.20285 0.19722 0.17430 -0.02295 0.02231  0.00095  14  ASN   A CB   
103  C  CG   . ASN   A 11  ? 0.23543 0.25048 0.22084 -0.01504 0.03351  0.02885  14  ASN   A CG   
104  O  OD1  . ASN   A 11  ? 0.24430 0.25016 0.25420 -0.01339 0.06076  0.00176  14  ASN   A OD1  
105  N  ND2  . ASN   A 11  ? 0.26306 0.27642 0.25823 0.00605  0.04946  0.05490  14  ASN   A ND2  
112  N  N    . PRO   A 12  ? 0.18049 0.18738 0.14105 -0.01955 0.03552  -0.01627 15  PRO   A N    
113  C  CA   . PRO   A 12  ? 0.18698 0.18784 0.15432 -0.02263 0.03871  -0.01260 15  PRO   A CA   
114  C  C    . PRO   A 12  ? 0.19946 0.17974 0.13836 -0.01269 0.02004  -0.01590 15  PRO   A C    
115  O  O    . PRO   A 12  ? 0.22663 0.19700 0.14002 0.00550  0.04515  -0.02886 15  PRO   A O    
116  C  CB   . PRO   A 12  ? 0.21597 0.19134 0.16956 -0.01161 0.04222  -0.02469 15  PRO   A CB   
117  C  CG   . PRO   A 12  ? 0.18802 0.18741 0.16981 -0.01848 0.03990  -0.02248 15  PRO   A CG   
118  C  CD   . PRO   A 12  ? 0.17859 0.19685 0.15691 -0.01642 0.04131  -0.01689 15  PRO   A CD   
126  N  N    . VAL   A 13  ? 0.19149 0.19510 0.13954 -0.02267 0.03197  -0.02069 16  VAL   A N    
127  C  CA   . VAL   A 13  ? 0.17469 0.20942 0.14896 -0.03097 0.01623  -0.01960 16  VAL   A CA   
128  C  C    . VAL   A 13  ? 0.18884 0.21903 0.12764 -0.02392 0.01113  -0.03375 16  VAL   A C    
129  O  O    . VAL   A 13  ? 0.19912 0.20566 0.12687 -0.03421 0.02877  -0.01959 16  VAL   A O    
130  C  CB   . VAL   A 13  ? 0.19352 0.23104 0.15581 -0.04334 0.01183  -0.00274 16  VAL   A CB   
131  C  CG1  . VAL   A 13  ? 0.20359 0.26476 0.18227 -0.00998 0.00771  -0.02124 16  VAL   A CG1  
132  C  CG2  . VAL   A 13  ? 0.21513 0.25384 0.18651 -0.04304 0.01560  0.00208  16  VAL   A CG2  
142  N  N    . ILE   A 14  ? 0.19809 0.19459 0.12776 -0.01859 0.01625  -0.02467 17  ILE   A N    
143  C  CA   . ILE   A 14  ? 0.20654 0.18528 0.13863 -0.00926 0.01560  -0.02343 17  ILE   A CA   
144  C  C    . ILE   A 14  ? 0.20644 0.22225 0.14239 -0.01176 -0.00834 -0.02788 17  ILE   A C    
145  O  O    . ILE   A 14  ? 0.24531 0.24021 0.16560 -0.03514 -0.03821 -0.01468 17  ILE   A O    
146  C  CB   . ILE   A 14  ? 0.24413 0.17266 0.15039 -0.00786 0.03950  -0.03835 17  ILE   A CB   
147  C  CG1  . ILE   A 14  ? 0.23897 0.17702 0.17620 0.00492  0.05296  -0.02137 17  ILE   A CG1  
148  C  CG2  . ILE   A 14  ? 0.24924 0.20171 0.13885 -0.01357 0.05030  -0.01221 17  ILE   A CG2  
149  C  CD1  . ILE   A 14  ? 0.19397 0.18769 0.17451 0.01339  0.04795  -0.01800 17  ILE   A CD1  
161  N  N    . PRO   A 15  ? 0.22895 0.22392 0.15905 0.00582  -0.04154 -0.03522 18  PRO   A N    
162  C  CA   . PRO   A 15  ? 0.20780 0.20832 0.16405 -0.00066 -0.01815 -0.02011 18  PRO   A CA   
163  C  C    . PRO   A 15  ? 0.18810 0.20774 0.14780 0.01975  -0.00289 -0.03950 18  PRO   A C    
164  O  O    . PRO   A 15  ? 0.18792 0.23817 0.16440 0.03071  -0.00664 -0.04295 18  PRO   A O    
165  C  CB   . PRO   A 15  ? 0.27895 0.22594 0.21276 0.01161  -0.05889 -0.01038 18  PRO   A CB   
166  C  CG   . PRO   A 15  ? 0.31848 0.24066 0.23556 0.03018  -0.09465 -0.01433 18  PRO   A CG   
167  C  CD   . PRO   A 15  ? 0.30121 0.26589 0.20313 0.02819  -0.08610 -0.02466 18  PRO   A CD   
175  N  N    . PHE   A 16  ? 0.17678 0.18918 0.12534 0.00542  0.01023  -0.03779 19  PHE   A N    
176  C  CA   . PHE   A 16  ? 0.16722 0.17740 0.13729 -0.00124 0.01540  -0.02729 19  PHE   A CA   
177  C  C    . PHE   A 16  ? 0.17453 0.17100 0.11917 0.02843  0.00412  -0.02950 19  PHE   A C    
178  O  O    . PHE   A 16  ? 0.19052 0.15389 0.12893 0.00837  0.02014  -0.02499 19  PHE   A O    
179  C  CB   . PHE   A 16  ? 0.18538 0.15778 0.13557 -0.00139 0.01260  -0.01499 19  PHE   A CB   
180  C  CG   . PHE   A 16  ? 0.20143 0.15625 0.13332 -0.00158 0.01029  -0.01836 19  PHE   A CG   
181  C  CD1  . PHE   A 16  ? 0.24194 0.18708 0.13380 -0.02243 0.01064  -0.02349 19  PHE   A CD1  
182  C  CD2  . PHE   A 16  ? 0.21482 0.19982 0.15784 0.00090  -0.01655 -0.03156 19  PHE   A CD2  
183  C  CE1  . PHE   A 16  ? 0.27768 0.20945 0.13944 -0.04445 -0.00279 -0.02560 19  PHE   A CE1  
184  C  CE2  . PHE   A 16  ? 0.22436 0.25187 0.15953 -0.00744 -0.01847 -0.02194 19  PHE   A CE2  
185  C  CZ   . PHE   A 16  ? 0.26101 0.23498 0.14088 -0.02059 -0.02755 -0.01969 19  PHE   A CZ   
188  N  N    . VAL   A 17  ? 0.16929 0.19702 0.12680 0.03366  -0.00105 -0.04337 20  VAL   A N    
189  C  CA   . VAL   A 17  ? 0.19848 0.18578 0.13418 0.04191  -0.01871 -0.05001 20  VAL   A CA   
190  C  C    . VAL   A 17  ? 0.19024 0.22317 0.13068 0.04677  0.00555  -0.05964 20  VAL   A C    
191  O  O    . VAL   A 17  ? 0.19977 0.27822 0.15255 0.04812  0.00597  -0.06612 20  VAL   A O    
192  C  CB   . VAL   A 17  ? 0.26813 0.17674 0.18000 0.05030  -0.05828 -0.03610 20  VAL   A CB   
193  C  CG1  . VAL   A 17  ? 0.33180 0.18431 0.21123 0.05331  -0.08595 -0.02591 20  VAL   A CG1  
194  C  CG2  . VAL   A 17  ? 0.26764 0.18933 0.18827 0.04837  -0.04411 -0.01649 20  VAL   A CG2  
204  N  N    . GLY   A 18  ? 0.19061 0.23491 0.12995 0.02161  -0.00035 -0.04045 21  GLY   A N    
205  C  CA   . GLY   A 18  ? 0.21186 0.25241 0.12149 -0.00388 0.00119  -0.03860 21  GLY   A CA   
206  C  C    . GLY   A 18  ? 0.20432 0.23603 0.12420 0.01720  0.00521  -0.03941 21  GLY   A C    
207  O  O    . GLY   A 18  ? 0.21486 0.23285 0.12324 0.00450  0.00970  -0.05614 21  GLY   A O    
211  N  N    . THR   A 19  ? 0.19968 0.26173 0.13151 0.02500  0.00627  -0.04696 22  THR   A N    
212  C  CA   . THR   A 19  ? 0.20819 0.24933 0.13620 0.02833  0.01221  -0.04442 22  THR   A CA   
213  C  C    . THR   A 19  ? 0.23548 0.23449 0.14787 0.00771  -0.00759 -0.02158 22  THR   A C    
214  O  O    . THR   A 19  ? 0.24338 0.28951 0.19704 -0.02058 -0.02734 0.00070  22  THR   A O    
215  C  CB   . THR   A 19  ? 0.25626 0.28210 0.17503 0.02591  0.01169  -0.07758 22  THR   A CB   
216  O  OG1  . THR   A 19  ? 0.28556 0.29755 0.20209 0.06964  0.02650  -0.06348 22  THR   A OG1  
217  C  CG2  . THR   A 19  ? 0.30736 0.28684 0.20154 0.01373  0.01741  -0.10764 22  THR   A CG2  
225  N  N    . ILE   A 20  ? 0.23389 0.23843 0.13858 0.02954  -0.02249 -0.00927 23  ILE   A N    
226  C  CA   . ILE   A 20  ? 0.23673 0.25691 0.13401 0.02586  -0.00865 0.00415  23  ILE   A CA   
227  C  C    . ILE   A 20  ? 0.25650 0.24590 0.16274 0.02709  -0.03828 -0.00674 23  ILE   A C    
228  O  O    . ILE   A 20  ? 0.29237 0.28135 0.17661 0.02321  -0.02593 -0.04601 23  ILE   A O    
229  C  CB   . ILE   A 20  ? 0.22166 0.22669 0.14801 0.04458  -0.02920 -0.01649 23  ILE   A CB   
230  C  CG1  . ILE   A 20  ? 0.22191 0.20271 0.14028 0.03674  -0.02637 -0.01693 23  ILE   A CG1  
231  C  CG2  . ILE   A 20  ? 0.24999 0.26215 0.15403 0.06228  -0.02578 -0.01380 23  ILE   A CG2  
232  C  CD1  . ILE   A 20  ? 0.23902 0.18606 0.15708 0.04752  -0.03021 -0.01071 23  ILE   A CD1  
244  N  N    . PRO   A 21  ? 0.24393 0.29565 0.19026 -0.01019 -0.00275 -0.01839 24  PRO   A N    
245  C  CA   . PRO   A 21  ? 0.24492 0.33354 0.17286 -0.01819 0.00623  -0.02764 24  PRO   A CA   
246  C  C    . PRO   A 21  ? 0.26298 0.38227 0.16117 0.04191  0.01015  -0.03405 24  PRO   A C    
247  O  O    . PRO   A 21  ? 0.26109 0.46514 0.19656 0.03700  0.00872  -0.05576 24  PRO   A O    
248  C  CB   . PRO   A 21  ? 0.26045 0.35890 0.20979 -0.03757 0.00204  -0.00279 24  PRO   A CB   
249  C  CG   . PRO   A 21  ? 0.27303 0.34199 0.21123 -0.00976 0.00005  -0.02371 24  PRO   A CG   
250  C  CD   . PRO   A 21  ? 0.22228 0.24861 0.19719 -0.02093 -0.02293 -0.00004 24  PRO   A CD   
258  N  N    . ASP   A 22  ? 0.25680 0.35864 0.15009 0.05873  0.00747  -0.02050 25  ASP   A N    
259  C  CA   . ASP   A 22  ? 0.27243 0.34573 0.15105 0.07847  -0.01300 -0.01489 25  ASP   A CA   
260  C  C    . ASP   A 22  ? 0.25507 0.29169 0.14927 0.05617  -0.00087 -0.02773 25  ASP   A C    
261  O  O    . ASP   A 22  ? 0.29088 0.30223 0.13659 0.02863  -0.01997 -0.02309 25  ASP   A O    
262  C  CB   . ASP   A 22  ? 0.35130 0.44822 0.17476 0.05163  -0.03829 -0.00981 25  ASP   A CB   
263  C  CG   . ASP   A 22  ? 0.48760 0.55874 0.23016 0.05554  -0.04920 0.01412  25  ASP   A CG   
264  O  OD1  . ASP   A 22  ? 0.48474 0.59525 0.18699 0.10755  -0.01234 -0.00339 25  ASP   A OD1  
265  O  OD2  . ASP   A 22  ? 0.59296 0.60265 0.28204 0.03094  -0.05181 0.01798  25  ASP   A OD2  
270  N  N    . GLN   A 23  ? 0.23485 0.30136 0.14225 0.06531  -0.01647 -0.02027 26  GLN   A N    
271  C  CA   . GLN   A 23  ? 0.24490 0.25311 0.15947 0.06937  -0.02923 -0.03534 26  GLN   A CA   
272  C  C    . GLN   A 23  ? 0.22993 0.23465 0.15388 0.07096  -0.03147 -0.01725 26  GLN   A C    
273  O  O    . GLN   A 23  ? 0.24279 0.23684 0.16366 0.06513  -0.02640 -0.00976 26  GLN   A O    
274  C  CB   . GLN   A 23  ? 0.25579 0.23881 0.18203 0.05854  -0.03221 -0.05206 26  GLN   A CB   
275  C  CG   . GLN   A 23  ? 0.26498 0.23122 0.22551 0.06587  -0.03978 -0.07584 26  GLN   A CG   
276  C  CD   . GLN   A 23  ? 0.25555 0.24560 0.25580 0.06900  -0.02226 -0.04988 26  GLN   A CD   
277  O  OE1  . GLN   A 23  ? 0.26578 0.28229 0.31971 0.02696  -0.00731 -0.07837 26  GLN   A OE1  
278  N  NE2  . GLN   A 23  ? 0.29107 0.28743 0.28100 0.04077  -0.00912 -0.03344 26  GLN   A NE2  
287  N  N    . LEU   A 24  ? 0.23119 0.19977 0.14482 0.05330  -0.01169 -0.01583 27  LEU   A N    
288  C  CA   . LEU   A 24  ? 0.22125 0.17879 0.15865 0.04497  -0.01035 -0.01078 27  LEU   A CA   
289  C  C    . LEU   A 24  ? 0.24312 0.18100 0.18067 0.03300  -0.02157 -0.01661 27  LEU   A C    
290  O  O    . LEU   A 24  ? 0.26892 0.22102 0.18821 -0.00637 -0.01312 -0.00807 27  LEU   A O    
291  C  CB   . LEU   A 24  ? 0.22964 0.19747 0.14881 0.04108  -0.01082 -0.00993 27  LEU   A CB   
292  C  CG   . LEU   A 24  ? 0.24136 0.18573 0.14602 0.03276  -0.01871 -0.01063 27  LEU   A CG   
293  C  CD1  . LEU   A 24  ? 0.27892 0.18715 0.14544 0.02692  -0.02496 -0.00098 27  LEU   A CD1  
294  C  CD2  . LEU   A 24  ? 0.23388 0.21418 0.16598 0.02055  -0.01637 0.01971  27  LEU   A CD2  
306  N  N    . ASP   A 25  ? 0.21959 0.18441 0.21223 0.04878  -0.03347 -0.01688 28  ASP   A N    
307  C  CA   . ASP   A 25  ? 0.24762 0.18944 0.21010 0.04418  -0.03051 -0.03077 28  ASP   A CA   
308  C  C    . ASP   A 25  ? 0.21253 0.16433 0.19643 0.02817  -0.03182 -0.00499 28  ASP   A C    
309  O  O    . ASP   A 25  ? 0.20878 0.16012 0.18092 0.02554  -0.02412 -0.00849 28  ASP   A O    
310  C  CB   . ASP   A 25  ? 0.25055 0.24476 0.20455 0.03977  -0.03836 -0.01732 28  ASP   A CB   
311  C  CG   . ASP   A 25  ? 0.32684 0.28295 0.24324 0.04632  -0.02652 -0.01678 28  ASP   A CG   
312  O  OD1  . ASP   A 25  ? 0.36968 0.29717 0.26468 0.05488  -0.01454 -0.02646 28  ASP   A OD1  
313  O  OD2  . ASP   A 25  ? 0.38009 0.32773 0.26509 0.04458  -0.00804 -0.02966 28  ASP   A OD2  
318  N  N    . PRO   A 26  ? 0.21864 0.15751 0.19649 0.02397  -0.02620 0.02557  29  PRO   A N    
319  C  CA   . PRO   A 26  ? 0.20806 0.15954 0.18372 0.01382  -0.01149 0.02687  29  PRO   A CA   
320  C  C    . PRO   A 26  ? 0.18765 0.17616 0.17278 0.01682  -0.00887 0.03877  29  PRO   A C    
321  O  O    . PRO   A 26  ? 0.20458 0.19030 0.15339 0.01752  -0.01801 0.02682  29  PRO   A O    
322  C  CB   . PRO   A 26  ? 0.23182 0.16791 0.22038 0.00393  -0.00807 0.04475  29  PRO   A CB   
323  C  CG   . PRO   A 26  ? 0.26361 0.17645 0.24399 0.00002  -0.00194 0.03995  29  PRO   A CG   
324  C  CD   . PRO   A 26  ? 0.24832 0.16482 0.23611 0.01202  -0.01420 0.03578  29  PRO   A CD   
332  N  N    . GLY   A 27  ? 0.18163 0.17027 0.17442 0.00509  -0.00440 0.03114  30  GLY   A N    
333  C  CA   . GLY   A 27  ? 0.17193 0.17113 0.20726 0.00265  -0.00309 0.04827  30  GLY   A CA   
334  C  C    . GLY   A 27  ? 0.17774 0.17507 0.23229 0.01322  0.00132  0.07684  30  GLY   A C    
335  O  O    . GLY   A 27  ? 0.18818 0.21091 0.33710 0.00783  -0.03136 0.09054  30  GLY   A O    
339  N  N    . THR   A 28  ? 0.18213 0.16521 0.16686 0.01621  -0.01051 0.03528  31  THR   A N    
340  C  CA   . THR   A 28  ? 0.17830 0.17756 0.15105 0.01828  -0.00997 0.01715  31  THR   A CA   
341  C  C    . THR   A 28  ? 0.16474 0.18130 0.14857 0.01572  0.00627  0.02891  31  THR   A C    
342  O  O    . THR   A 28  ? 0.18290 0.18344 0.15263 0.00353  0.01730  0.03814  31  THR   A O    
343  C  CB   . THR   A 28  ? 0.18002 0.18927 0.15678 0.01893  -0.00217 0.01865  31  THR   A CB   
344  O  OG1  . THR   A 28  ? 0.19937 0.19734 0.17911 0.02492  -0.01528 -0.00042 31  THR   A OG1  
345  C  CG2  . THR   A 28  ? 0.19022 0.20271 0.17535 0.02374  0.00490  0.01575  31  THR   A CG2  
353  N  N    . LEU   A 29  ? 0.17178 0.18615 0.13378 0.00750  -0.00112 0.03459  32  LEU   A N    
354  C  CA   . LEU   A 29  ? 0.17945 0.18114 0.14250 0.01707  -0.00531 0.03366  32  LEU   A CA   
355  C  C    . LEU   A 29  ? 0.17207 0.17542 0.14506 0.00517  -0.00357 0.02724  32  LEU   A C    
356  O  O    . LEU   A 29  ? 0.18109 0.22970 0.13553 0.00293  0.01002  0.02171  32  LEU   A O    
357  C  CB   . LEU   A 29  ? 0.18585 0.20316 0.16916 0.00945  0.00662  0.04670  32  LEU   A CB   
358  C  CG   . LEU   A 29  ? 0.21232 0.20617 0.19636 0.02409  -0.01193 0.06818  32  LEU   A CG   
359  C  CD1  . LEU   A 29  ? 0.25407 0.24459 0.25194 0.05944  0.04058  0.08522  32  LEU   A CD1  
360  C  CD2  . LEU   A 29  ? 0.18430 0.24355 0.20114 0.00522  -0.01190 0.07311  32  LEU   A CD2  
372  N  N    . ILE   A 30  ? 0.17386 0.18575 0.13570 0.00044  0.00013  0.01365  33  ILE   A N    
373  C  CA   . ILE   A 30  ? 0.17567 0.17902 0.13695 0.01422  0.01044  0.00690  33  ILE   A CA   
374  C  C    . ILE   A 30  ? 0.16364 0.17368 0.14232 0.00899  0.01880  0.02127  33  ILE   A C    
375  O  O    . ILE   A 30  ? 0.19387 0.18108 0.15961 -0.00470 0.04558  0.00599  33  ILE   A O    
376  C  CB   . ILE   A 30  ? 0.19964 0.18347 0.14764 0.01657  -0.00085 -0.00116 33  ILE   A CB   
377  C  CG1  . ILE   A 30  ? 0.21964 0.20533 0.16232 -0.00422 -0.02228 0.01692  33  ILE   A CG1  
378  C  CG2  . ILE   A 30  ? 0.20105 0.19450 0.18614 0.03577  -0.01100 -0.00648 33  ILE   A CG2  
379  C  CD1  . ILE   A 30  ? 0.29564 0.20765 0.17322 0.02439  -0.01586 0.03705  33  ILE   A CD1  
391  N  N    . VAL   A 31  ? 0.15882 0.18438 0.14765 -0.00987 0.01741  0.01703  34  VAL   A N    
392  C  CA   . VAL   A 31  ? 0.19575 0.17890 0.14885 0.00028  0.00969  0.01913  34  VAL   A CA   
393  C  C    . VAL   A 31  ? 0.16119 0.17844 0.13494 0.00403  -0.00057 0.01764  34  VAL   A C    
394  O  O    . VAL   A 31  ? 0.17426 0.20846 0.14567 -0.00767 0.02116  0.01580  34  VAL   A O    
395  C  CB   . VAL   A 31  ? 0.19322 0.20561 0.17385 -0.00380 -0.00358 0.02945  34  VAL   A CB   
396  C  CG1  . VAL   A 31  ? 0.22527 0.20563 0.18728 0.01345  -0.01295 0.03601  34  VAL   A CG1  
397  C  CG2  . VAL   A 31  ? 0.22046 0.24986 0.20481 0.00695  -0.02690 0.04592  34  VAL   A CG2  
407  N  N    . ILE   A 32  ? 0.16822 0.16906 0.14021 0.00717  0.01983  0.01950  35  ILE   A N    
408  C  CA   . ILE   A 32  ? 0.15998 0.15287 0.13404 0.00648  0.01890  0.01079  35  ILE   A CA   
409  C  C    . ILE   A 32  ? 0.17396 0.15962 0.14824 0.01771  0.02298  0.01224  35  ILE   A C    
410  O  O    . ILE   A 32  ? 0.18761 0.15180 0.17719 0.00503  0.04224  0.00121  35  ILE   A O    
411  C  CB   . ILE   A 32  ? 0.17977 0.16936 0.14529 0.02396  0.02221  0.00350  35  ILE   A CB   
412  C  CG1  . ILE   A 32  ? 0.18862 0.15917 0.15966 0.01322  0.02479  0.02199  35  ILE   A CG1  
413  C  CG2  . ILE   A 32  ? 0.18379 0.18053 0.15810 0.01585  0.02164  -0.01138 35  ILE   A CG2  
414  C  CD1  . ILE   A 32  ? 0.21955 0.18726 0.16610 0.01170  0.01607  0.01878  35  ILE   A CD1  
426  N  N    . ARG   A 33  ? 0.17864 0.16036 0.15474 0.00420  0.02486  0.00290  36  ARG   A N    
427  C  CA   . ARG   A 33  ? 0.17522 0.15361 0.15948 0.01043  0.01920  0.02693  36  ARG   A CA   
428  C  C    . ARG   A 33  ? 0.18006 0.14523 0.15840 -0.00656 0.02198  0.00797  36  ARG   A C    
429  O  O    . ARG   A 33  ? 0.17403 0.17934 0.16857 -0.00257 0.02530  -0.01336 36  ARG   A O    
430  C  CB   . ARG   A 33  ? 0.22277 0.18110 0.20098 0.01606  -0.01003 0.03844  36  ARG   A CB   
431  C  CG   . ARG   A 33  ? 0.28277 0.23189 0.22862 0.02937  -0.01880 0.06984  36  ARG   A CG   
432  C  CD   . ARG   A 33  ? 0.32639 0.30078 0.29607 0.02463  -0.04825 0.07762  36  ARG   A CD   
433  N  NE   . ARG   A 33  ? 0.40479 0.34690 0.38832 -0.00190 -0.04504 0.06030  36  ARG   A NE   
434  C  CZ   . ARG   A 33  ? 0.48632 0.43188 0.47008 0.00221  -0.02712 0.02322  36  ARG   A CZ   
435  N  NH1  . ARG   A 33  ? 0.49964 0.46203 0.49161 -0.00438 -0.01977 0.01668  36  ARG   A NH1  
436  N  NH2  . ARG   A 33  ? 0.52574 0.44466 0.49971 -0.01593 -0.02117 0.01589  36  ARG   A NH2  
439  N  N    . GLY   A 34  ? 0.18886 0.13855 0.17071 0.01067  0.02231  0.00600  37  GLY   A N    
440  C  CA   . GLY   A 34  ? 0.19318 0.15561 0.17428 0.01223  0.02628  0.00042  37  GLY   A CA   
441  C  C    . GLY   A 34  ? 0.19529 0.13435 0.15949 0.02090  0.02993  -0.00829 37  GLY   A C    
442  O  O    . GLY   A 34  ? 0.22577 0.14329 0.17449 0.01926  0.02342  0.00003  37  GLY   A O    
446  N  N    . HIS   A 35  ? 0.21662 0.13856 0.16741 0.00420  0.03202  -0.00481 38  HIS   A N    
447  C  CA   A HIS   A 35  ? 0.22670 0.10827 0.16483 0.00832  0.02296  -0.00826 38  HIS   A CA   
448  C  CA   B HIS   A 35  ? 0.23899 0.12882 0.18274 -0.00222 0.02187  -0.00741 38  HIS   A CA   
449  C  C    . HIS   A 35  ? 0.21254 0.11279 0.17122 0.00567  0.04145  -0.00986 38  HIS   A C    
450  O  O    . HIS   A 35  ? 0.21583 0.15663 0.16740 0.02794  0.03768  -0.00911 38  HIS   A O    
451  C  CB   A HIS   A 35  ? 0.30816 0.15603 0.17702 -0.02015 0.02652  0.00729  38  HIS   A CB   
452  C  CB   B HIS   A 35  ? 0.32557 0.19278 0.22754 -0.04402 0.00827  0.00808  38  HIS   A CB   
453  C  CG   A HIS   A 35  ? 0.29608 0.15969 0.17634 -0.01764 0.01711  0.01335  38  HIS   A CG   
454  C  CG   B HIS   A 35  ? 0.37614 0.23692 0.26810 -0.06822 -0.01018 0.01651  38  HIS   A CG   
455  N  ND1  A HIS   A 35  ? 0.30712 0.14971 0.19808 -0.02780 0.03044  0.00562  38  HIS   A ND1  
456  N  ND1  B HIS   A 35  ? 0.38364 0.24908 0.28479 -0.06311 -0.02741 0.01469  38  HIS   A ND1  
457  C  CD2  A HIS   A 35  ? 0.27669 0.16962 0.17248 -0.01110 -0.01624 -0.01283 38  HIS   A CD2  
458  C  CD2  B HIS   A 35  ? 0.40534 0.27847 0.28914 -0.05047 -0.00293 0.02029  38  HIS   A CD2  
459  C  CE1  A HIS   A 35  ? 0.30916 0.15821 0.19219 -0.02727 0.02001  -0.02019 38  HIS   A CE1  
460  C  CE1  B HIS   A 35  ? 0.40657 0.28562 0.29625 -0.04121 -0.02011 0.00677  38  HIS   A CE1  
461  N  NE2  A HIS   A 35  ? 0.31881 0.17516 0.18432 -0.06107 0.01098  -0.02391 38  HIS   A NE2  
462  N  NE2  B HIS   A 35  ? 0.41983 0.28772 0.29887 -0.04869 -0.00719 0.00697  38  HIS   A NE2  
475  N  N    . VAL   A 36  ? 0.22773 0.12864 0.16288 0.02915  0.03067  -0.01053 39  VAL   A N    
476  C  CA   . VAL   A 36  ? 0.24361 0.12873 0.16009 0.01771  0.03662  -0.00255 39  VAL   A CA   
477  C  C    . VAL   A 36  ? 0.26736 0.12330 0.16804 0.01905  0.03739  -0.01567 39  VAL   A C    
478  O  O    . VAL   A 36  ? 0.33083 0.12945 0.18485 0.02932  0.04263  -0.03306 39  VAL   A O    
479  C  CB   . VAL   A 36  ? 0.25826 0.15050 0.16619 0.02970  0.03818  -0.00915 39  VAL   A CB   
480  C  CG1  . VAL   A 36  ? 0.27271 0.16367 0.15618 0.03107  0.04435  0.00696  39  VAL   A CG1  
481  C  CG2  . VAL   A 36  ? 0.25042 0.19026 0.18755 0.00742  0.04888  0.00482  39  VAL   A CG2  
491  N  N    . PRO   A 37  ? 0.26976 0.13844 0.16711 0.01039  0.01537  -0.03396 40  PRO   A N    
492  C  CA   . PRO   A 37  ? 0.29575 0.16642 0.20477 -0.02010 0.00889  -0.04355 40  PRO   A CA   
493  C  C    . PRO   A 37  ? 0.30941 0.14062 0.18978 -0.00721 -0.01888 -0.02328 40  PRO   A C    
494  O  O    . PRO   A 37  ? 0.35090 0.16317 0.17495 -0.00338 0.00030  -0.02263 40  PRO   A O    
495  C  CB   . PRO   A 37  ? 0.29143 0.21804 0.25764 -0.01291 -0.00196 -0.06431 40  PRO   A CB   
496  C  CG   . PRO   A 37  ? 0.29015 0.21009 0.28041 -0.00157 -0.03892 -0.04747 40  PRO   A CG   
497  C  CD   . PRO   A 37  ? 0.25727 0.15320 0.20323 0.01005  0.00488  -0.02012 40  PRO   A CD   
505  N  N    . SER   A 38  ? 0.37293 0.15849 0.21140 -0.01726 -0.03713 -0.04344 41  SER   A N    
506  C  CA   . SER   A 38  ? 0.40912 0.17179 0.23365 -0.01426 -0.03181 -0.04259 41  SER   A CA   
507  C  C    . SER   A 38  ? 0.38374 0.22010 0.22556 -0.01900 -0.01480 -0.03606 41  SER   A C    
508  O  O    . SER   A 38  ? 0.43620 0.27487 0.21509 -0.02636 -0.00801 -0.03675 41  SER   A O    
509  C  CB   . SER   A 38  ? 0.41181 0.19100 0.29362 -0.03252 -0.05580 -0.06315 41  SER   A CB   
510  O  OG   . SER   A 38  ? 0.39226 0.23356 0.33985 -0.06513 -0.05716 -0.04494 41  SER   A OG   
516  N  N    . ASP   A 39  ? 0.37958 0.19739 0.27044 -0.03300 -0.08498 -0.01028 42  ASP   A N    
517  C  CA   . ASP   A 39  ? 0.37522 0.23150 0.31776 -0.01911 -0.08608 0.02428  42  ASP   A CA   
518  C  C    . ASP   A 39  ? 0.36538 0.20775 0.27708 0.00980  -0.08401 0.01516  42  ASP   A C    
519  O  O    . ASP   A 39  ? 0.36521 0.22172 0.30176 -0.01884 -0.10465 0.02087  42  ASP   A O    
520  C  CB   . ASP   A 39  ? 0.38562 0.31953 0.38978 -0.00540 -0.07750 0.03817  42  ASP   A CB   
521  C  CG   . ASP   A 39  ? 0.39748 0.40485 0.43730 0.00122  -0.04767 0.04926  42  ASP   A CG   
522  O  OD1  . ASP   A 39  ? 0.38378 0.42365 0.45309 0.00118  -0.02073 0.07700  42  ASP   A OD1  
523  O  OD2  . ASP   A 39  ? 0.45148 0.47772 0.46438 0.01014  -0.03684 0.02946  42  ASP   A OD2  
528  N  N    . ALA   A 40  ? 0.31049 0.17569 0.21629 0.01568  -0.02910 0.00226  43  ALA   A N    
529  C  CA   . ALA   A 40  ? 0.31828 0.15145 0.17682 0.01676  -0.00036 -0.01724 43  ALA   A CA   
530  C  C    . ALA   A 40  ? 0.33995 0.15869 0.16307 0.02275  0.00265  -0.04876 43  ALA   A C    
531  O  O    . ALA   A 40  ? 0.38978 0.15925 0.16261 0.00624  0.04123  -0.04165 43  ALA   A O    
532  C  CB   . ALA   A 40  ? 0.34405 0.16781 0.18173 0.00391  -0.00465 -0.01309 43  ALA   A CB   
538  N  N    . ASP   A 41  ? 0.32636 0.13942 0.15350 0.01111  -0.00773 -0.03179 44  ASP   A N    
539  C  CA   . ASP   A 41  ? 0.36133 0.17285 0.14297 -0.01078 -0.01244 -0.03223 44  ASP   A CA   
540  C  C    . ASP   A 41  ? 0.34292 0.17000 0.12794 0.00267  0.01251  -0.03327 44  ASP   A C    
541  O  O    . ASP   A 41  ? 0.35549 0.14828 0.13299 0.02977  0.02265  -0.03376 44  ASP   A O    
542  C  CB   . ASP   A 41  ? 0.39906 0.21633 0.15656 0.02041  -0.04863 -0.00096 44  ASP   A CB   
543  C  CG   . ASP   A 41  ? 0.34561 0.24409 0.18244 0.03729  -0.03190 -0.00954 44  ASP   A CG   
544  O  OD1  . ASP   A 41  ? 0.28173 0.19216 0.20758 0.00007  0.01335  -0.05724 44  ASP   A OD1  
545  O  OD2  . ASP   A 41  ? 0.36040 0.28909 0.20790 0.04642  -0.02519 -0.01384 44  ASP   A OD2  
550  N  N    . ARG   A 42  ? 0.32004 0.13424 0.12155 -0.02287 0.02882  -0.02571 45  ARG   A N    
551  C  CA   . ARG   A 42  ? 0.28436 0.12787 0.11356 -0.00942 0.03421  -0.01872 45  ARG   A CA   
552  C  C    . ARG   A 42  ? 0.25060 0.12319 0.11822 -0.00200 0.01978  -0.00880 45  ARG   A C    
553  O  O    . ARG   A 42  ? 0.26883 0.15082 0.11317 -0.02388 0.00980  -0.01844 45  ARG   A O    
554  C  CB   . ARG   A 42  ? 0.28164 0.12168 0.12504 -0.00489 0.03541  -0.02072 45  ARG   A CB   
555  C  CG   . ARG   A 42  ? 0.28825 0.12067 0.14342 -0.00084 -0.00423 -0.01329 45  ARG   A CG   
556  C  CD   . ARG   A 42  ? 0.31180 0.14682 0.13533 -0.00885 -0.01968 -0.00847 45  ARG   A CD   
557  N  NE   . ARG   A 42  ? 0.26109 0.13766 0.12597 -0.00033 -0.01440 -0.00655 45  ARG   A NE   
558  C  CZ   . ARG   A 42  ? 0.24592 0.11577 0.16281 -0.01181 0.01150  0.00667  45  ARG   A CZ   
559  N  NH1  . ARG   A 42  ? 0.27533 0.15885 0.18571 -0.00669 0.01896  0.02941  45  ARG   A NH1  
560  N  NH2  . ARG   A 42  ? 0.25435 0.12712 0.16357 -0.00804 -0.00459 -0.00273 45  ARG   A NH2  
574  N  N    . PHE   A 43  ? 0.22866 0.12002 0.12077 0.00017  0.01050  -0.01234 46  PHE   A N    
575  C  CA   . PHE   A 43  ? 0.21273 0.11738 0.11802 0.00272  0.02150  -0.01771 46  PHE   A CA   
576  C  C    . PHE   A 43  ? 0.19834 0.12156 0.10413 0.01211  0.01778  -0.00007 46  PHE   A C    
577  O  O    . PHE   A 43  ? 0.21415 0.11249 0.11211 0.00814  0.02657  -0.00239 46  PHE   A O    
578  C  CB   . PHE   A 43  ? 0.22330 0.11350 0.12187 -0.00861 0.00727  0.00387  46  PHE   A CB   
579  C  CG   . PHE   A 43  ? 0.22674 0.11410 0.12742 0.00167  0.04912  -0.01003 46  PHE   A CG   
580  C  CD1  . PHE   A 43  ? 0.22550 0.12574 0.14727 0.01344  0.01939  0.00174  46  PHE   A CD1  
581  C  CD2  . PHE   A 43  ? 0.24865 0.10592 0.13873 0.02705  0.03086  0.01250  46  PHE   A CD2  
582  C  CE1  . PHE   A 43  ? 0.23302 0.13271 0.15291 0.00921  0.03911  0.00775  46  PHE   A CE1  
583  C  CE2  . PHE   A 43  ? 0.27596 0.11638 0.14921 0.01532  0.05202  0.01690  46  PHE   A CE2  
584  C  CZ   . PHE   A 43  ? 0.24069 0.13855 0.15839 0.01312  0.03931  0.02653  46  PHE   A CZ   
594  N  N    . GLN   A 44  ? 0.19872 0.11815 0.10390 0.00448  0.01988  -0.01584 47  GLN   A N    
595  C  CA   . GLN   A 44  ? 0.20026 0.11978 0.10257 0.00970  0.01306  -0.00841 47  GLN   A CA   
596  C  C    . GLN   A 44  ? 0.18292 0.11731 0.10086 0.00710  0.02369  -0.00885 47  GLN   A C    
597  O  O    . GLN   A 44  ? 0.18747 0.14358 0.10308 0.00587  0.01553  -0.01752 47  GLN   A O    
598  C  CB   . GLN   A 44  ? 0.21762 0.11455 0.11707 0.01345  0.02361  -0.00370 47  GLN   A CB   
599  C  CG   . GLN   A 44  ? 0.22227 0.12193 0.12862 0.01674  0.02246  -0.01182 47  GLN   A CG   
600  C  CD   . GLN   A 44  ? 0.21475 0.13604 0.12323 0.01035  -0.00447 -0.02017 47  GLN   A CD   
601  O  OE1  . GLN   A 44  ? 0.25822 0.14012 0.13250 0.01618  -0.01752 -0.03412 47  GLN   A OE1  
602  N  NE2  . GLN   A 44  ? 0.22700 0.12469 0.12572 0.02447  -0.01911 -0.01917 47  GLN   A NE2  
611  N  N    . VAL   A 45  ? 0.19265 0.11429 0.10161 0.01905  0.02383  -0.00493 48  VAL   A N    
612  C  CA   . VAL   A 45  ? 0.18949 0.12408 0.10575 0.02248  0.01647  -0.00659 48  VAL   A CA   
613  C  C    . VAL   A 45  ? 0.19057 0.12298 0.10390 0.02156  0.00997  -0.00113 48  VAL   A C    
614  O  O    . VAL   A 45  ? 0.19878 0.12419 0.12762 0.01000  0.02791  -0.00402 48  VAL   A O    
615  C  CB   . VAL   A 45  ? 0.19823 0.12834 0.11638 0.02219  0.01828  0.01088  48  VAL   A CB   
616  C  CG1  . VAL   A 45  ? 0.21885 0.15026 0.13023 0.01272  -0.00268 0.00796  48  VAL   A CG1  
617  C  CG2  . VAL   A 45  ? 0.21093 0.13429 0.14533 0.02325  0.00824  0.01386  48  VAL   A CG2  
627  N  N    . ASP   A 46  ? 0.17635 0.12470 0.10096 0.02231  0.01141  -0.01562 49  ASP   A N    
628  C  CA   . ASP   A 46  ? 0.18152 0.10985 0.10732 0.00957  -0.00225 -0.02068 49  ASP   A CA   
629  C  C    . ASP   A 46  ? 0.18909 0.11931 0.10573 0.01773  0.00216  -0.00933 49  ASP   A C    
630  O  O    . ASP   A 46  ? 0.18948 0.14952 0.11048 0.01159  0.00503  -0.02542 49  ASP   A O    
631  C  CB   . ASP   A 46  ? 0.20453 0.11871 0.11957 0.02715  0.00848  -0.01260 49  ASP   A CB   
632  C  CG   . ASP   A 46  ? 0.21017 0.13499 0.13217 0.02084  0.00292  -0.01715 49  ASP   A CG   
633  O  OD1  . ASP   A 46  ? 0.22105 0.15285 0.12554 0.01977  0.00100  -0.00590 49  ASP   A OD1  
634  O  OD2  . ASP   A 46  ? 0.22662 0.16262 0.14221 0.03621  -0.01281 -0.02556 49  ASP   A OD2  
639  N  N    . LEU   A 47  ? 0.17174 0.10787 0.10716 0.01267  -0.00139 -0.01147 50  LEU   A N    
640  C  CA   . LEU   A 47  ? 0.18120 0.11355 0.10355 0.02195  -0.00856 -0.00670 50  LEU   A CA   
641  C  C    . LEU   A 47  ? 0.18599 0.13060 0.10069 0.01936  -0.00965 -0.01364 50  LEU   A C    
642  O  O    . LEU   A 47  ? 0.20739 0.12799 0.12767 0.02032  -0.00147 0.00132  50  LEU   A O    
643  C  CB   . LEU   A 47  ? 0.19503 0.13073 0.12023 0.02635  -0.01169 0.01100  50  LEU   A CB   
644  C  CG   . LEU   A 47  ? 0.19634 0.15072 0.16276 0.02117  -0.01234 0.01773  50  LEU   A CG   
645  C  CD1  . LEU   A 47  ? 0.18975 0.15007 0.16193 0.01949  -0.00480 0.02589  50  LEU   A CD1  
646  C  CD2  . LEU   A 47  ? 0.21147 0.16745 0.19839 0.01298  -0.00738 0.04032  50  LEU   A CD2  
658  N  N    . GLN   A 48  ? 0.20168 0.11944 0.10929 0.02992  -0.00895 -0.01252 51  GLN   A N    
659  C  CA   . GLN   A 48  ? 0.20377 0.13257 0.12281 0.02958  -0.01651 -0.01285 51  GLN   A CA   
660  C  C    . GLN   A 48  ? 0.22473 0.13424 0.11393 0.03943  -0.02121 -0.02099 51  GLN   A C    
661  O  O    . GLN   A 48  ? 0.22622 0.14182 0.11761 0.03251  -0.02030 -0.02170 51  GLN   A O    
662  C  CB   . GLN   A 48  ? 0.20817 0.14052 0.12853 0.04261  -0.02068 -0.02944 51  GLN   A CB   
663  C  CG   . GLN   A 48  ? 0.22468 0.14197 0.13997 0.04474  -0.03314 -0.04023 51  GLN   A CG   
664  C  CD   . GLN   A 48  ? 0.21653 0.15242 0.14041 0.04253  -0.03612 -0.04975 51  GLN   A CD   
665  O  OE1  . GLN   A 48  ? 0.22019 0.16883 0.16289 0.04290  -0.02367 -0.06356 51  GLN   A OE1  
666  N  NE2  . GLN   A 48  ? 0.21550 0.15686 0.15829 0.04663  -0.02667 -0.06172 51  GLN   A NE2  
675  N  N    . ASN   A 49  ? 0.24139 0.13610 0.12499 0.03370  -0.01507 -0.02924 52  ASN   A N    
676  C  CA   . ASN   A 49  ? 0.25632 0.12966 0.14200 0.03443  -0.01995 -0.04121 52  ASN   A CA   
677  C  C    . ASN   A 49  ? 0.26490 0.13784 0.15123 0.05662  -0.03785 -0.03137 52  ASN   A C    
678  O  O    . ASN   A 49  ? 0.28084 0.16471 0.16087 0.07185  -0.02559 -0.02501 52  ASN   A O    
679  C  CB   . ASN   A 49  ? 0.26374 0.14310 0.14823 0.02506  -0.01061 -0.02644 52  ASN   A CB   
680  C  CG   . ASN   A 49  ? 0.26967 0.14128 0.15801 0.00381  -0.01605 -0.03130 52  ASN   A CG   
681  O  OD1  . ASN   A 49  ? 0.30447 0.17025 0.16642 0.00666  0.00717  -0.04540 52  ASN   A OD1  
682  N  ND2  . ASN   A 49  ? 0.30252 0.14525 0.17427 0.02436  -0.02351 -0.03196 52  ASN   A ND2  
689  N  N    . GLY   A 50  ? 0.24074 0.17236 0.15659 0.03847  -0.02208 -0.04487 53  GLY   A N    
690  C  CA   . GLY   A 50  ? 0.24206 0.18183 0.17899 0.04563  -0.01354 -0.05139 53  GLY   A CA   
691  C  C    . GLY   A 50  ? 0.24147 0.16901 0.17872 0.07782  -0.02056 -0.05261 53  GLY   A C    
692  O  O    . GLY   A 50  ? 0.23382 0.15550 0.16517 0.05833  -0.03271 -0.03805 53  GLY   A O    
696  N  N    . SER   A 51  ? 0.23695 0.19292 0.21444 0.07916  -0.03037 -0.07093 54  SER   A N    
697  C  CA   . SER   A 51  ? 0.24400 0.22366 0.23192 0.06795  -0.03579 -0.04496 54  SER   A CA   
698  C  C    . SER   A 51  ? 0.26728 0.21363 0.23043 0.07824  -0.04445 -0.07528 54  SER   A C    
699  O  O    . SER   A 51  ? 0.26443 0.25859 0.25739 0.06734  -0.05461 -0.06525 54  SER   A O    
700  C  CB   . SER   A 51  ? 0.25813 0.24325 0.25449 0.05276  -0.02192 -0.03085 54  SER   A CB   
701  O  OG   . SER   A 51  ? 0.28321 0.29977 0.25941 0.03899  0.00115  0.00357  54  SER   A OG   
707  N  N    . SER   A 52  ? 0.25552 0.20283 0.22525 0.08709  -0.03626 -0.06195 55  SER   A N    
708  C  CA   . SER   A 52  ? 0.32198 0.20718 0.23334 0.10958  -0.04964 -0.04057 55  SER   A CA   
709  C  C    . SER   A 52  ? 0.27886 0.21147 0.23799 0.09397  -0.06690 -0.04929 55  SER   A C    
710  O  O    . SER   A 52  ? 0.27638 0.17837 0.22764 0.07204  -0.04042 -0.04218 55  SER   A O    
711  C  CB   . SER   A 52  ? 0.39170 0.21184 0.26721 0.14031  -0.08014 -0.04574 55  SER   A CB   
712  O  OG   . SER   A 52  ? 0.45921 0.24989 0.32112 0.16877  -0.08317 -0.05295 55  SER   A OG   
718  N  N    . MET   A 53  ? 0.26933 0.26740 0.25652 0.09002  -0.05727 -0.06790 56  MET   A N    
719  C  CA   . MET   A 53  ? 0.25891 0.27791 0.26272 0.06626  -0.06231 -0.05063 56  MET   A CA   
720  C  C    . MET   A 53  ? 0.29032 0.31847 0.26154 0.11092  -0.04706 -0.04584 56  MET   A C    
721  O  O    . MET   A 53  ? 0.35703 0.30716 0.24333 0.09458  -0.03742 -0.03528 56  MET   A O    
722  C  CB   . MET   A 53  ? 0.31287 0.31518 0.29266 0.05190  -0.08036 -0.02687 56  MET   A CB   
723  C  CG   . MET   A 53  ? 0.39040 0.35820 0.32829 -0.01688 -0.10108 -0.02266 56  MET   A CG   
724  S  SD   . MET   A 53  ? 0.49760 0.42786 0.39271 -0.05258 -0.06967 -0.02598 56  MET   A SD   
725  C  CE   . MET   A 53  ? 0.51419 0.44858 0.41330 -0.03998 -0.03942 -0.04018 56  MET   A CE   
728  N  N    . LYS   A 54  ? 0.33577 0.31482 0.27708 0.13815  -0.06949 -0.04357 57  LYS   A N    
729  C  CA   . LYS   A 54  ? 0.35564 0.29933 0.31930 0.16236  -0.06317 -0.02468 57  LYS   A CA   
730  C  C    . LYS   A 54  ? 0.42421 0.29328 0.35548 0.19566  -0.07134 -0.02660 57  LYS   A C    
731  O  O    . LYS   A 54  ? 0.49462 0.35361 0.36036 0.20737  -0.06173 -0.04692 57  LYS   A O    
732  C  CB   . LYS   A 54  ? 0.36314 0.33075 0.35025 0.14507  -0.03607 -0.00097 57  LYS   A CB   
733  C  CG   . LYS   A 54  ? 0.36164 0.33574 0.35475 0.12828  -0.02159 -0.00409 57  LYS   A CG   
734  C  CD   . LYS   A 54  ? 0.34345 0.36865 0.36696 0.12622  -0.01421 -0.01493 57  LYS   A CD   
735  C  CE   . LYS   A 54  ? 0.37087 0.38833 0.37379 0.12703  -0.03797 -0.00334 57  LYS   A CE   
736  N  NZ   . LYS   A 54  ? 0.43214 0.37927 0.36493 0.07488  -0.07536 -0.02246 57  LYS   A NZ   
750  N  N    . PRO   A 55  ? 0.44561 0.27903 0.39400 0.15990  -0.08180 -0.01520 58  PRO   A N    
751  C  CA   . PRO   A 55  ? 0.42485 0.25191 0.39072 0.11568  -0.09169 0.00618  58  PRO   A CA   
752  C  C    . PRO   A 55  ? 0.37375 0.21418 0.34682 0.09960  -0.10148 0.01185  58  PRO   A C    
753  O  O    . PRO   A 55  ? 0.37520 0.25891 0.35059 0.12855  -0.08388 -0.02356 58  PRO   A O    
754  C  CB   . PRO   A 55  ? 0.47528 0.30681 0.41770 0.06806  -0.09738 0.02099  58  PRO   A CB   
755  C  CG   . PRO   A 55  ? 0.47997 0.31856 0.43220 0.08640  -0.10091 0.00642  58  PRO   A CG   
756  C  CD   . PRO   A 55  ? 0.48121 0.30345 0.42387 0.12437  -0.09008 -0.01113 58  PRO   A CD   
764  N  N    . ARG   A 56  ? 0.33053 0.18888 0.28641 0.04872  -0.10699 0.04644  59  ARG   A N    
765  C  CA   . ARG   A 56  ? 0.32769 0.17436 0.22452 0.03212  -0.11014 0.00486  59  ARG   A CA   
766  C  C    . ARG   A 56  ? 0.28442 0.14405 0.20030 0.03479  -0.06455 -0.00677 59  ARG   A C    
767  O  O    . ARG   A 56  ? 0.29442 0.13996 0.21091 0.03936  -0.05566 0.00798  59  ARG   A O    
768  C  CB   . ARG   A 56  ? 0.38734 0.17662 0.21818 0.00739  -0.10939 0.00232  59  ARG   A CB   
769  C  CG   . ARG   A 56  ? 0.37326 0.20629 0.22740 0.05203  -0.08354 0.00645  59  ARG   A CG   
770  C  CD   . ARG   A 56  ? 0.42751 0.20484 0.24081 0.04433  -0.08983 -0.01031 59  ARG   A CD   
771  N  NE   . ARG   A 56  ? 0.43660 0.18717 0.25676 0.03199  -0.07799 -0.03223 59  ARG   A NE   
772  C  CZ   . ARG   A 56  ? 0.43238 0.22768 0.27712 -0.00441 -0.08745 -0.06966 59  ARG   A CZ   
773  N  NH1  . ARG   A 56  ? 0.46171 0.30593 0.26902 0.00939  -0.09670 -0.06826 59  ARG   A NH1  
774  N  NH2  . ARG   A 56  ? 0.40779 0.17581 0.32369 0.04217  -0.08230 -0.07455 59  ARG   A NH2  
788  N  N    . ALA   A 57  ? 0.27194 0.14291 0.16571 0.05445  -0.05167 -0.00897 60  ALA   A N    
789  C  CA   . ALA   A 57  ? 0.25838 0.14209 0.16127 0.04353  -0.03923 -0.03214 60  ALA   A CA   
790  C  C    . ALA   A 57  ? 0.26105 0.13024 0.14404 0.06653  -0.02738 -0.01324 60  ALA   A C    
791  O  O    . ALA   A 57  ? 0.27139 0.12633 0.14426 0.05167  -0.02697 -0.01703 60  ALA   A O    
792  C  CB   . ALA   A 57  ? 0.25236 0.19857 0.16859 0.05434  -0.03477 -0.02666 60  ALA   A CB   
798  N  N    . ASP   A 58  ? 0.26539 0.12442 0.13948 0.03908  -0.03018 -0.02206 61  ASP   A N    
799  C  CA   . ASP   A 58  ? 0.25361 0.12790 0.13173 0.04773  -0.02461 -0.00882 61  ASP   A CA   
800  C  C    . ASP   A 58  ? 0.23285 0.13139 0.10545 0.03222  -0.02197 0.00771  61  ASP   A C    
801  O  O    . ASP   A 58  ? 0.25237 0.13272 0.11798 0.04087  -0.01516 -0.00973 61  ASP   A O    
802  C  CB   . ASP   A 58  ? 0.27566 0.11269 0.14541 0.02588  -0.04341 0.00528  61  ASP   A CB   
803  C  CG   . ASP   A 58  ? 0.31817 0.13061 0.15869 0.02560  -0.04274 -0.00699 61  ASP   A CG   
804  O  OD1  . ASP   A 58  ? 0.34849 0.12653 0.16728 0.04814  -0.03075 -0.00529 61  ASP   A OD1  
805  O  OD2  . ASP   A 58  ? 0.36673 0.14086 0.19487 -0.00995 -0.04573 0.00525  61  ASP   A OD2  
810  N  N    . VAL   A 59  ? 0.23351 0.12146 0.11546 0.03824  -0.00729 -0.00022 62  VAL   A N    
811  C  CA   . VAL   A 59  ? 0.23805 0.11120 0.11797 0.03229  -0.01194 -0.00074 62  VAL   A CA   
812  C  C    . VAL   A 59  ? 0.20778 0.12166 0.12603 0.02112  -0.00752 -0.00227 62  VAL   A C    
813  O  O    . VAL   A 59  ? 0.22618 0.12014 0.12341 0.01354  -0.01541 0.01541  62  VAL   A O    
814  C  CB   . VAL   A 59  ? 0.22110 0.13159 0.13102 0.03424  -0.01482 -0.00326 62  VAL   A CB   
815  C  CG1  . VAL   A 59  ? 0.22434 0.11266 0.13490 0.02942  -0.01123 0.00048  62  VAL   A CG1  
816  C  CG2  . VAL   A 59  ? 0.23633 0.13789 0.13595 0.01960  -0.02149 -0.00445 62  VAL   A CG2  
826  N  N    . ALA   A 60  ? 0.21603 0.12683 0.11867 0.01083  -0.01189 0.00378  63  ALA   A N    
827  C  CA   . ALA   A 60  ? 0.20878 0.12898 0.12271 0.00317  -0.00580 0.01320  63  ALA   A CA   
828  C  C    . ALA   A 60  ? 0.19890 0.14273 0.11470 0.00209  -0.01344 0.03262  63  ALA   A C    
829  O  O    . ALA   A 60  ? 0.20217 0.14612 0.13369 -0.00202 -0.00960 0.02456  63  ALA   A O    
830  C  CB   . ALA   A 60  ? 0.21569 0.14710 0.12425 0.01075  -0.02537 0.00108  63  ALA   A CB   
836  N  N    . PHE   A 61  ? 0.19543 0.11610 0.12344 0.01461  -0.00026 0.00918  64  PHE   A N    
837  C  CA   . PHE   A 61  ? 0.19020 0.10877 0.12868 0.01735  0.00669  0.00733  64  PHE   A CA   
838  C  C    . PHE   A 61  ? 0.19403 0.09654 0.11253 0.02213  0.00125  0.00837  64  PHE   A C    
839  O  O    . PHE   A 61  ? 0.20027 0.12056 0.10357 0.01349  0.00924  0.00534  64  PHE   A O    
840  C  CB   . PHE   A 61  ? 0.18976 0.14423 0.12892 0.03320  -0.00070 0.01359  64  PHE   A CB   
841  C  CG   . PHE   A 61  ? 0.19833 0.13559 0.13672 0.01785  0.00923  0.03108  64  PHE   A CG   
842  C  CD1  . PHE   A 61  ? 0.21300 0.13702 0.13637 0.02389  0.02327  0.02607  64  PHE   A CD1  
843  C  CD2  . PHE   A 61  ? 0.25967 0.16536 0.15895 0.06544  0.04748  0.04094  64  PHE   A CD2  
844  C  CE1  . PHE   A 61  ? 0.20416 0.14154 0.13993 0.02349  0.01674  0.00926  64  PHE   A CE1  
845  C  CE2  . PHE   A 61  ? 0.28372 0.15806 0.17726 0.05284  0.06215  0.04213  64  PHE   A CE2  
846  C  CZ   . PHE   A 61  ? 0.21770 0.14073 0.16070 0.04678  0.01171  0.02450  64  PHE   A CZ   
856  N  N    . HIS   A 62  ? 0.18452 0.11480 0.11448 0.01490  0.01457  0.01252  65  HIS   A N    
857  C  CA   . HIS   A 62  ? 0.18681 0.10422 0.11032 0.01735  0.00537  0.00434  65  HIS   A CA   
858  C  C    . HIS   A 62  ? 0.20123 0.12723 0.10733 0.01402  0.02467  0.02132  65  HIS   A C    
859  O  O    . HIS   A 62  ? 0.21347 0.12066 0.12949 0.01948  0.03848  0.02317  65  HIS   A O    
860  C  CB   . HIS   A 62  ? 0.19415 0.11034 0.12220 0.01126  0.00060  0.00247  65  HIS   A CB   
861  C  CG   . HIS   A 62  ? 0.20628 0.10015 0.12780 0.00855  0.01209  0.00128  65  HIS   A CG   
862  N  ND1  . HIS   A 62  ? 0.21713 0.13029 0.11563 0.00985  0.00030  0.00404  65  HIS   A ND1  
863  C  CD2  . HIS   A 62  ? 0.20750 0.12197 0.12314 0.01188  0.01448  -0.00597 65  HIS   A CD2  
864  C  CE1  . HIS   A 62  ? 0.21551 0.11320 0.12382 -0.00093 0.00858  0.00398  65  HIS   A CE1  
865  N  NE2  . HIS   A 62  ? 0.23258 0.11822 0.12741 0.01210  0.00453  0.00596  65  HIS   A NE2  
873  N  N    . PHE   A 63  ? 0.18540 0.11393 0.11535 0.01503  0.03036  0.01125  66  PHE   A N    
874  C  CA   . PHE   A 63  ? 0.17903 0.11255 0.12791 0.03198  0.03125  0.02378  66  PHE   A CA   
875  C  C    . PHE   A 63  ? 0.18309 0.10863 0.13110 0.01887  0.04125  0.00732  66  PHE   A C    
876  O  O    . PHE   A 63  ? 0.20283 0.11381 0.11216 0.01746  0.02910  -0.00233 66  PHE   A O    
877  C  CB   . PHE   A 63  ? 0.19101 0.12671 0.13123 0.02487  0.02736  0.01184  66  PHE   A CB   
878  C  CG   . PHE   A 63  ? 0.20913 0.11991 0.13067 0.02836  0.03675  0.02184  66  PHE   A CG   
879  C  CD1  . PHE   A 63  ? 0.20589 0.12743 0.14488 0.02925  0.03699  0.01681  66  PHE   A CD1  
880  C  CD2  . PHE   A 63  ? 0.19957 0.12690 0.14195 0.03521  0.04026  0.01750  66  PHE   A CD2  
881  C  CE1  . PHE   A 63  ? 0.22513 0.13963 0.14309 0.02375  0.04890  0.02691  66  PHE   A CE1  
882  C  CE2  . PHE   A 63  ? 0.22779 0.14678 0.15473 0.03456  0.04618  0.02738  66  PHE   A CE2  
883  C  CZ   . PHE   A 63  ? 0.23823 0.12877 0.15052 0.03401  0.03620  0.02005  66  PHE   A CZ   
893  N  N    . ASN   A 64  ? 0.19432 0.11734 0.12649 0.02663  0.04330  0.00730  67  ASN   A N    
894  C  CA   . ASN   A 64  ? 0.20107 0.11287 0.11235 0.01054  0.03465  -0.00230 67  ASN   A CA   
895  C  C    . ASN   A 64  ? 0.21614 0.12878 0.11897 0.01399  0.04613  0.01029  67  ASN   A C    
896  O  O    . ASN   A 64  ? 0.24457 0.12722 0.11361 0.01940  0.05108  0.00726  67  ASN   A O    
897  C  CB   . ASN   A 64  ? 0.21665 0.10692 0.11643 0.01519  0.02441  0.00008  67  ASN   A CB   
898  C  CG   . ASN   A 64  ? 0.22229 0.11504 0.11681 0.01312  0.03235  -0.00071 67  ASN   A CG   
899  O  OD1  . ASN   A 64  ? 0.26476 0.11646 0.11420 0.00831  0.02704  0.00411  67  ASN   A OD1  
900  N  ND2  . ASN   A 64  ? 0.23815 0.13509 0.11960 0.00634  0.01545  0.00265  67  ASN   A ND2  
907  N  N    . PRO   A 65  ? 0.22810 0.10773 0.12798 0.01990  0.05265  0.00589  68  PRO   A N    
908  C  CA   . PRO   A 65  ? 0.23102 0.11428 0.14592 0.01948  0.05994  -0.00482 68  PRO   A CA   
909  C  C    . PRO   A 65  ? 0.24919 0.12228 0.14809 0.01695  0.05338  0.00177  68  PRO   A C    
910  O  O    . PRO   A 65  ? 0.27871 0.13954 0.12419 0.01786  0.03334  -0.01110 68  PRO   A O    
911  C  CB   . PRO   A 65  ? 0.24474 0.11191 0.14989 0.01862  0.06316  0.00007  68  PRO   A CB   
912  C  CG   . PRO   A 65  ? 0.24100 0.10396 0.14351 0.02762  0.05399  0.00290  68  PRO   A CG   
913  C  CD   . PRO   A 65  ? 0.22399 0.12907 0.13030 0.01754  0.04187  0.00434  68  PRO   A CD   
921  N  N    . ARG   A 66  ? 0.30643 0.12253 0.13545 0.01075  0.06744  -0.01079 69  ARG   A N    
922  C  CA   . ARG   A 66  ? 0.30632 0.13992 0.13248 -0.00124 0.05366  -0.03676 69  ARG   A CA   
923  C  C    . ARG   A 66  ? 0.33180 0.16514 0.14656 0.00108  0.07360  -0.02468 69  ARG   A C    
924  O  O    . ARG   A 66  ? 0.35960 0.15379 0.18257 0.00749  0.07996  -0.03437 69  ARG   A O    
925  C  CB   . ARG   A 66  ? 0.30764 0.13865 0.14014 -0.00288 0.04432  -0.01649 69  ARG   A CB   
926  C  CG   . ARG   A 66  ? 0.31371 0.13467 0.15673 -0.00238 0.05015  -0.01507 69  ARG   A CG   
927  C  CD   . ARG   A 66  ? 0.31734 0.13389 0.13488 0.00363  0.05028  -0.00539 69  ARG   A CD   
928  N  NE   . ARG   A 66  ? 0.29469 0.13506 0.12171 0.00387  0.03902  -0.00528 69  ARG   A NE   
929  C  CZ   . ARG   A 66  ? 0.28948 0.14970 0.11989 0.00330  0.03268  -0.00001 69  ARG   A CZ   
930  N  NH1  . ARG   A 66  ? 0.33212 0.16248 0.12366 -0.00374 0.04082  0.01005  69  ARG   A NH1  
931  N  NH2  . ARG   A 66  ? 0.29825 0.14121 0.12897 0.00902  0.03134  -0.01128 69  ARG   A NH2  
945  N  N    . PHE   A 67  ? 0.33191 0.14110 0.15828 0.00160  0.05810  -0.04183 70  PHE   A N    
946  C  CA   . PHE   A 67  ? 0.36393 0.17161 0.15785 -0.00460 0.06812  -0.05846 70  PHE   A CA   
947  C  C    . PHE   A 67  ? 0.41249 0.18749 0.17436 0.01317  0.07006  -0.06004 70  PHE   A C    
948  O  O    . PHE   A 67  ? 0.43430 0.20253 0.19857 -0.01301 0.08288  -0.07542 70  PHE   A O    
949  C  CB   . PHE   A 67  ? 0.36981 0.16873 0.16248 -0.00748 0.06344  -0.04203 70  PHE   A CB   
950  C  CG   . PHE   A 67  ? 0.35627 0.14605 0.16862 0.01769  0.05460  -0.01478 70  PHE   A CG   
951  C  CD1  . PHE   A 67  ? 0.33426 0.21390 0.17526 0.04982  0.05224  -0.01406 70  PHE   A CD1  
952  C  CD2  . PHE   A 67  ? 0.37237 0.17684 0.17016 0.05710  0.05558  -0.01817 70  PHE   A CD2  
953  C  CE1  . PHE   A 67  ? 0.34551 0.21437 0.18402 0.01649  0.04454  -0.01070 70  PHE   A CE1  
954  C  CE2  . PHE   A 67  ? 0.40077 0.16269 0.16520 0.03012  0.05174  -0.01677 70  PHE   A CE2  
955  C  CZ   . PHE   A 67  ? 0.35712 0.20255 0.16947 0.02638  0.03142  -0.02600 70  PHE   A CZ   
965  N  N    . LYS   A 68  ? 0.40932 0.20257 0.15580 0.00154  0.05377  -0.05255 71  LYS   A N    
966  C  CA   . LYS   A 68  ? 0.47104 0.30256 0.17903 -0.00208 0.03572  -0.05096 71  LYS   A CA   
967  C  C    . LYS   A 68  ? 0.49969 0.31869 0.18608 -0.04013 0.06090  -0.08922 71  LYS   A C    
968  O  O    . LYS   A 68  ? 0.48267 0.30736 0.15968 -0.06448 0.07011  -0.04612 71  LYS   A O    
969  C  CB   . LYS   A 68  ? 0.52835 0.39110 0.20840 0.05000  0.05280  -0.03345 71  LYS   A CB   
970  C  CG   . LYS   A 68  ? 0.58086 0.44943 0.28672 0.06805  0.05570  -0.04252 71  LYS   A CG   
971  C  CD   . LYS   A 68  ? 0.60811 0.47861 0.33460 0.07434  0.05698  -0.06476 71  LYS   A CD   
972  C  CE   . LYS   A 68  ? 0.62733 0.49504 0.36415 0.06879  0.04228  -0.08264 71  LYS   A CE   
973  N  NZ   . LYS   A 68  ? 0.62049 0.49521 0.35683 0.05449  0.01935  -0.09351 71  LYS   A NZ   
987  N  N    . ARG   A 69  ? 0.53713 0.37767 0.23297 -0.02765 0.08618  -0.12437 72  ARG   A N    
988  C  CA   . ARG   A 69  ? 0.58037 0.44666 0.29523 -0.00927 0.10075  -0.10605 72  ARG   A CA   
989  C  C    . ARG   A 69  ? 0.55899 0.42973 0.29143 0.01215  0.09998  -0.16477 72  ARG   A C    
990  O  O    . ARG   A 69  ? 0.58405 0.38697 0.35268 -0.00282 0.08690  -0.18174 72  ARG   A O    
991  C  CB   . ARG   A 69  ? 0.64415 0.51084 0.32755 -0.01591 0.10811  -0.06797 72  ARG   A CB   
992  C  CG   . ARG   A 69  ? 0.69739 0.55307 0.35713 -0.02428 0.10490  -0.04865 72  ARG   A CG   
993  C  CD   . ARG   A 69  ? 0.74853 0.60193 0.39209 -0.01792 0.09544  -0.02424 72  ARG   A CD   
994  N  NE   . ARG   A 69  ? 0.77557 0.63994 0.39507 -0.01995 0.11328  -0.03085 72  ARG   A NE   
995  C  CZ   . ARG   A 69  ? 0.80532 0.66754 0.37854 -0.01845 0.10480  -0.06196 72  ARG   A CZ   
996  N  NH1  . ARG   A 69  ? 0.81273 0.67620 0.37329 -0.04254 0.10160  -0.06679 72  ARG   A NH1  
997  N  NH2  . ARG   A 69  ? 0.81596 0.65959 0.38119 -0.00336 0.11391  -0.06281 72  ARG   A NH2  
1011 N  N    . ALA   A 70  ? 0.52151 0.43966 0.27872 0.05667  0.09251  -0.17236 73  ALA   A N    
1012 C  CA   . ALA   A 70  ? 0.50359 0.36242 0.27867 0.07689  0.09439  -0.13803 73  ALA   A CA   
1013 C  C    . ALA   A 70  ? 0.48862 0.27743 0.24355 0.06047  0.10925  -0.08261 73  ALA   A C    
1014 O  O    . ALA   A 70  ? 0.53704 0.24287 0.28013 0.09911  0.09215  -0.06643 73  ALA   A O    
1015 C  CB   . ALA   A 70  ? 0.53286 0.38702 0.28649 0.07657  0.10007  -0.12844 73  ALA   A CB   
1021 N  N    . GLY   A 71  ? 0.43344 0.23447 0.21582 0.03583  0.10838  -0.06833 74  GLY   A N    
1022 C  CA   . GLY   A 71  ? 0.39260 0.20274 0.20234 0.02339  0.11033  -0.05681 74  GLY   A CA   
1023 C  C    . GLY   A 71  ? 0.36422 0.20759 0.18080 0.01385  0.11804  -0.04025 74  GLY   A C    
1024 O  O    . GLY   A 71  ? 0.36063 0.22517 0.20509 0.02661  0.11673  -0.05542 74  GLY   A O    
1028 N  N    . CYS   A 72  ? 0.33904 0.18911 0.16758 0.03564  0.10200  -0.02110 75  CYS   A N    
1029 C  CA   . CYS   A 72  ? 0.33349 0.20523 0.16439 0.02368  0.10238  -0.01276 75  CYS   A CA   
1030 C  C    . CYS   A 72  ? 0.29354 0.16489 0.17563 0.03816  0.09851  -0.00102 75  CYS   A C    
1031 O  O    . CYS   A 72  ? 0.30746 0.15256 0.15342 0.02480  0.08478  -0.01799 75  CYS   A O    
1032 C  CB   . CYS   A 72  ? 0.35270 0.21235 0.18072 0.02298  0.11332  -0.00455 75  CYS   A CB   
1033 S  SG   . CYS   A 72  ? 0.38856 0.18445 0.17853 0.01745  0.08754  0.00269  75  CYS   A SG   
1039 N  N    . ILE   A 73  ? 0.28187 0.16203 0.15048 0.02178  0.08475  -0.00183 76  ILE   A N    
1040 C  CA   . ILE   A 73  ? 0.25316 0.14004 0.13380 0.03385  0.06565  0.01633  76  ILE   A CA   
1041 C  C    . ILE   A 73  ? 0.25446 0.15070 0.14925 0.02134  0.08451  0.03055  76  ILE   A C    
1042 O  O    . ILE   A 73  ? 0.25692 0.16706 0.19561 0.03023  0.08795  0.02888  76  ILE   A O    
1043 C  CB   . ILE   A 73  ? 0.23427 0.14383 0.15100 0.03165  0.05406  0.00853  76  ILE   A CB   
1044 C  CG1  . ILE   A 73  ? 0.25693 0.13830 0.17758 0.04373  0.06150  0.02614  76  ILE   A CG1  
1045 C  CG2  . ILE   A 73  ? 0.24156 0.15433 0.14840 0.02956  0.04438  0.01960  76  ILE   A CG2  
1046 C  CD1  . ILE   A 73  ? 0.24511 0.16205 0.19780 0.03318  0.06183  0.01753  76  ILE   A CD1  
1058 N  N    . VAL   A 74  ? 0.24461 0.12979 0.14124 0.02096  0.06345  -0.00175 77  VAL   A N    
1059 C  CA   . VAL   A 74  ? 0.24011 0.12414 0.13290 0.02176  0.05757  -0.00059 77  VAL   A CA   
1060 C  C    . VAL   A 74  ? 0.21908 0.12204 0.13482 0.01852  0.04404  0.01595  77  VAL   A C    
1061 O  O    . VAL   A 74  ? 0.22349 0.13905 0.13443 0.00189  0.04941  0.00669  77  VAL   A O    
1062 C  CB   . VAL   A 74  ? 0.25241 0.14790 0.12702 0.01477  0.03137  0.00599  77  VAL   A CB   
1063 C  CG1  . VAL   A 74  ? 0.26521 0.14821 0.16043 0.01889  0.00658  0.01005  77  VAL   A CG1  
1064 C  CG2  . VAL   A 74  ? 0.28300 0.17390 0.13885 0.01137  0.01641  -0.01149 77  VAL   A CG2  
1074 N  N    . CYS   A 75  ? 0.20573 0.12788 0.12716 0.01892  0.04286  0.00674  78  CYS   A N    
1075 C  CA   . CYS   A 75  ? 0.19372 0.12063 0.13403 0.01940  0.04528  0.01620  78  CYS   A CA   
1076 C  C    . CYS   A 75  ? 0.21307 0.13047 0.12684 0.01696  0.03544  0.02602  78  CYS   A C    
1077 O  O    . CYS   A 75  ? 0.23284 0.14504 0.13692 0.01143  0.04205  0.02753  78  CYS   A O    
1078 C  CB   . CYS   A 75  ? 0.20880 0.13531 0.14489 0.03078  0.02865  0.01625  78  CYS   A CB   
1079 S  SG   . CYS   A 75  ? 0.23183 0.13760 0.15254 0.02695  0.03078  0.02725  78  CYS   A SG   
1085 N  N    . ASN   A 76  ? 0.20219 0.11421 0.12418 0.01182  0.02446  0.02133  79  ASN   A N    
1086 C  CA   . ASN   A 76  ? 0.20341 0.12437 0.12150 0.01451  -0.00839 0.02482  79  ASN   A CA   
1087 C  C    . ASN   A 76  ? 0.20338 0.11674 0.12604 -0.00037 0.00388  0.01708  79  ASN   A C    
1088 O  O    . ASN   A 76  ? 0.20860 0.11818 0.12930 0.00422  0.01665  0.01501  79  ASN   A O    
1089 C  CB   . ASN   A 76  ? 0.22908 0.12129 0.11806 0.00939  0.00267  0.01875  79  ASN   A CB   
1090 C  CG   . ASN   A 76  ? 0.23593 0.12257 0.12732 0.00221  0.00251  0.00971  79  ASN   A CG   
1091 O  OD1  . ASN   A 76  ? 0.24848 0.13559 0.12290 -0.00677 -0.00451 0.02643  79  ASN   A OD1  
1092 N  ND2  . ASN   A 76  ? 0.25242 0.13721 0.12580 -0.01227 0.00126  0.02127  79  ASN   A ND2  
1099 N  N    . THR   A 77  ? 0.22174 0.11121 0.12601 0.00935  -0.00121 0.01734  80  THR   A N    
1100 C  CA   . THR   A 77  ? 0.22705 0.10908 0.11994 0.01237  -0.00852 0.01927  80  THR   A CA   
1101 C  C    . THR   A 77  ? 0.23634 0.11296 0.13081 0.00431  -0.00812 0.00580  80  THR   A C    
1102 O  O    . THR   A 77  ? 0.24589 0.12153 0.12689 0.01011  -0.01350 0.02096  80  THR   A O    
1103 C  CB   . THR   A 77  ? 0.23320 0.12239 0.12948 -0.00108 -0.01752 0.01266  80  THR   A CB   
1104 O  OG1  . THR   A 77  ? 0.22148 0.13649 0.13429 0.00247  -0.01224 0.03367  80  THR   A OG1  
1105 C  CG2  . THR   A 77  ? 0.24916 0.14550 0.14536 -0.00993 -0.02548 0.00935  80  THR   A CG2  
1113 N  N    . LEU   A 78  ? 0.23636 0.09817 0.11824 0.01414  -0.01092 0.01296  81  LEU   A N    
1114 C  CA   . LEU   A 78  ? 0.24935 0.10063 0.12719 0.02087  -0.02700 0.00050  81  LEU   A CA   
1115 C  C    . LEU   A 78  ? 0.25901 0.11506 0.13047 0.02850  -0.02301 0.00247  81  LEU   A C    
1116 O  O    . LEU   A 78  ? 0.27679 0.12026 0.12459 0.02334  -0.02061 -0.00050 81  LEU   A O    
1117 C  CB   . LEU   A 78  ? 0.26582 0.11135 0.13387 0.03764  -0.03381 0.00603  81  LEU   A CB   
1118 C  CG   . LEU   A 78  ? 0.25530 0.12993 0.12864 0.02816  -0.03688 0.00594  81  LEU   A CG   
1119 C  CD1  . LEU   A 78  ? 0.27502 0.13685 0.13445 0.03312  -0.04937 -0.00017 81  LEU   A CD1  
1120 C  CD2  . LEU   A 78  ? 0.25926 0.17122 0.15798 0.04528  -0.04124 0.00811  81  LEU   A CD2  
1132 N  N    . ILE   A 79  ? 0.29530 0.11251 0.13426 0.01475  -0.02047 0.00833  82  ILE   A N    
1133 C  CA   . ILE   A 79  ? 0.30897 0.10895 0.14858 0.01498  -0.02636 -0.00101 82  ILE   A CA   
1134 C  C    . ILE   A 79  ? 0.33358 0.11277 0.14517 0.02161  -0.01145 -0.00146 82  ILE   A C    
1135 O  O    . ILE   A 79  ? 0.34305 0.11711 0.14412 0.02887  -0.01570 0.01274  82  ILE   A O    
1136 C  CB   . ILE   A 79  ? 0.33319 0.12036 0.20958 0.00795  -0.04686 0.00174  82  ILE   A CB   
1137 C  CG1  . ILE   A 79  ? 0.32956 0.14311 0.22385 -0.00856 -0.05729 0.01663  82  ILE   A CG1  
1138 C  CG2  . ILE   A 79  ? 0.37688 0.13561 0.26238 -0.01392 -0.06460 -0.01732 82  ILE   A CG2  
1139 C  CD1  . ILE   A 79  ? 0.34944 0.18615 0.23475 -0.03315 -0.06521 0.00760  82  ILE   A CD1  
1151 N  N    . ASN   A 80  ? 0.35379 0.11384 0.13945 0.03486  -0.02428 0.00308  83  ASN   A N    
1152 C  CA   . ASN   A 80  ? 0.39083 0.11955 0.15881 0.05799  -0.02640 -0.00374 83  ASN   A CA   
1153 C  C    . ASN   A 80  ? 0.34913 0.12859 0.15934 0.08249  -0.02890 0.00399  83  ASN   A C    
1154 O  O    . ASN   A 80  ? 0.38487 0.14396 0.17705 0.07589  -0.05483 0.01201  83  ASN   A O    
1155 C  CB   . ASN   A 80  ? 0.44298 0.12217 0.17302 0.05274  -0.02869 -0.00381 83  ASN   A CB   
1156 C  CG   . ASN   A 80  ? 0.46768 0.12765 0.18855 0.03089  0.00334  0.00275  83  ASN   A CG   
1157 O  OD1  . ASN   A 80  ? 0.52616 0.13911 0.19908 0.01084  -0.00172 -0.02118 83  ASN   A OD1  
1158 N  ND2  . ASN   A 80  ? 0.50631 0.17875 0.20065 -0.01463 -0.01528 -0.01069 83  ASN   A ND2  
1165 N  N    . GLU   A 81  ? 0.33227 0.13332 0.15400 0.05368  -0.02824 -0.00761 84  GLU   A N    
1166 C  CA   . GLU   A 81  ? 0.32735 0.15612 0.17597 0.07422  -0.05527 -0.00142 84  GLU   A CA   
1167 C  C    . GLU   A 81  ? 0.35766 0.20260 0.15582 0.09507  -0.03924 -0.03769 84  GLU   A C    
1168 O  O    . GLU   A 81  ? 0.36038 0.30677 0.17932 0.08724  -0.05423 -0.05881 84  GLU   A O    
1169 C  CB   . GLU   A 81  ? 0.34470 0.18257 0.20922 0.07060  -0.05002 0.02496  84  GLU   A CB   
1170 C  CG   . GLU   A 81  ? 0.31942 0.23099 0.26476 0.06653  -0.03820 0.07691  84  GLU   A CG   
1171 C  CD   . GLU   A 81  ? 0.33104 0.29250 0.30732 0.05412  -0.02528 0.15386  84  GLU   A CD   
1172 O  OE1  . GLU   A 81  ? 0.37009 0.33800 0.33361 0.08484  0.01353  0.15100  84  GLU   A OE1  
1173 O  OE2  . GLU   A 81  ? 0.34522 0.35194 0.32844 0.03140  -0.04625 0.16944  84  GLU   A OE2  
1180 N  N    . LYS   A 82  ? 0.33695 0.12237 0.13485 0.05014  -0.02658 0.00311  85  LYS   A N    
1181 C  CA   . LYS   A 82  ? 0.35217 0.13879 0.13975 0.03972  -0.02094 0.01552  85  LYS   A CA   
1182 C  C    . LYS   A 82  ? 0.32753 0.13218 0.12988 0.02816  -0.03501 0.01949  85  LYS   A C    
1183 O  O    . LYS   A 82  ? 0.32491 0.13041 0.13616 0.02375  -0.03031 0.01617  85  LYS   A O    
1184 C  CB   . LYS   A 82  ? 0.38850 0.13193 0.14762 0.03302  -0.02381 0.01910  85  LYS   A CB   
1185 C  CG   . LYS   A 82  ? 0.40173 0.13737 0.16376 0.03232  -0.03883 0.02667  85  LYS   A CG   
1186 C  CD   . LYS   A 82  ? 0.40561 0.14736 0.19426 0.03300  -0.03183 0.04034  85  LYS   A CD   
1187 C  CE   . LYS   A 82  ? 0.38952 0.15638 0.22065 0.02524  -0.04914 0.02697  85  LYS   A CE   
1188 N  NZ   . LYS   A 82  ? 0.40070 0.16257 0.23141 0.04005  -0.05861 0.03468  85  LYS   A NZ   
1202 N  N    . TRP   A 83  ? 0.31674 0.11796 0.12850 0.02228  -0.03242 0.00126  86  TRP   A N    
1203 C  CA   . TRP   A 83  ? 0.30014 0.12870 0.13007 0.03035  -0.01046 0.01736  86  TRP   A CA   
1204 C  C    . TRP   A 83  ? 0.31499 0.11685 0.13861 0.01529  -0.01224 0.02816  86  TRP   A C    
1205 O  O    . TRP   A 83  ? 0.31945 0.16282 0.16218 -0.00708 -0.02461 0.05746  86  TRP   A O    
1206 C  CB   . TRP   A 83  ? 0.30962 0.11646 0.12693 0.01829  -0.02514 0.00121  86  TRP   A CB   
1207 C  CG   . TRP   A 83  ? 0.30338 0.12002 0.13128 0.02200  -0.03222 -0.00151 86  TRP   A CG   
1208 C  CD1  . TRP   A 83  ? 0.30689 0.13891 0.15185 0.02225  -0.04034 -0.00775 86  TRP   A CD1  
1209 C  CD2  . TRP   A 83  ? 0.27048 0.11113 0.13330 0.01808  -0.00067 -0.00433 86  TRP   A CD2  
1210 N  NE1  . TRP   A 83  ? 0.28107 0.14570 0.16929 0.01983  -0.02645 -0.02589 86  TRP   A NE1  
1211 C  CE2  . TRP   A 83  ? 0.27911 0.12122 0.15467 0.03247  -0.01553 -0.00306 86  TRP   A CE2  
1212 C  CE3  . TRP   A 83  ? 0.27059 0.10950 0.13524 0.02191  0.00572  -0.00084 86  TRP   A CE3  
1213 C  CZ2  . TRP   A 83  ? 0.26496 0.12196 0.16586 0.01902  0.00199  -0.00878 86  TRP   A CZ2  
1214 C  CZ3  . TRP   A 83  ? 0.27519 0.10536 0.16021 0.01830  0.00967  -0.00714 86  TRP   A CZ3  
1215 C  CH2  . TRP   A 83  ? 0.26540 0.10657 0.16068 0.01921  -0.00086 0.00613  86  TRP   A CH2  
1226 N  N    . GLY   A 84  ? 0.30778 0.13388 0.14168 0.00903  -0.00021 0.03913  87  GLY   A N    
1227 C  CA   . GLY   A 84  ? 0.28491 0.15919 0.15959 -0.01470 0.00096  0.03996  87  GLY   A CA   
1228 C  C    . GLY   A 84  ? 0.28272 0.14221 0.15215 -0.01729 0.01341  0.04144  87  GLY   A C    
1229 O  O    . GLY   A 84  ? 0.27484 0.15551 0.14381 -0.01601 0.00062  0.03252  87  GLY   A O    
1233 N  N    . ARG   A 85  ? 0.27962 0.17661 0.17180 -0.02983 0.01560  0.03359  88  ARG   A N    
1234 C  CA   . ARG   A 85  ? 0.28383 0.19366 0.18500 -0.03110 0.03768  0.02564  88  ARG   A CA   
1235 C  C    . ARG   A 85  ? 0.26708 0.19965 0.16776 -0.02433 0.01730  0.05168  88  ARG   A C    
1236 O  O    . ARG   A 85  ? 0.28566 0.23279 0.15126 -0.01595 -0.00776 0.04952  88  ARG   A O    
1237 C  CB   . ARG   A 85  ? 0.27966 0.25641 0.23336 -0.04956 0.05333  0.00290  88  ARG   A CB   
1238 C  CG   . ARG   A 85  ? 0.27568 0.29494 0.27085 -0.07063 0.03452  0.00574  88  ARG   A CG   
1239 C  CD   . ARG   A 85  ? 0.31856 0.38696 0.28523 -0.04310 0.03191  0.01138  88  ARG   A CD   
1240 N  NE   . ARG   A 85  ? 0.28313 0.42412 0.27253 -0.03669 0.01502  -0.00901 88  ARG   A NE   
1241 C  CZ   . ARG   A 85  ? 0.33187 0.41778 0.29700 -0.05639 0.03594  -0.02631 88  ARG   A CZ   
1242 N  NH1  . ARG   A 85  ? 0.34439 0.45213 0.33009 -0.08326 0.04122  -0.04108 88  ARG   A NH1  
1243 N  NH2  . ARG   A 85  ? 0.38275 0.39228 0.30493 -0.02291 0.01396  -0.05256 88  ARG   A NH2  
1257 N  N    . GLU   A 86  ? 0.24184 0.19237 0.13789 -0.00660 0.02138  0.05278  89  GLU   A N    
1258 C  CA   . GLU   A 86  ? 0.23161 0.18728 0.14293 -0.00025 0.03437  0.04517  89  GLU   A CA   
1259 C  C    . GLU   A 86  ? 0.22891 0.20130 0.15236 0.00810  0.03736  0.05989  89  GLU   A C    
1260 O  O    . GLU   A 86  ? 0.25209 0.24067 0.16228 0.01258  0.06407  0.06853  89  GLU   A O    
1261 C  CB   . GLU   A 86  ? 0.25737 0.18167 0.16050 0.00800  0.03099  0.02847  89  GLU   A CB   
1262 C  CG   . GLU   A 86  ? 0.26292 0.19508 0.17872 0.00791  0.02426  0.00440  89  GLU   A CG   
1263 C  CD   . GLU   A 86  ? 0.25606 0.18424 0.17504 0.00401  0.02529  -0.02045 89  GLU   A CD   
1264 O  OE1  . GLU   A 86  ? 0.28495 0.24638 0.21589 -0.00900 0.03475  -0.04345 89  GLU   A OE1  
1265 O  OE2  . GLU   A 86  ? 0.27605 0.16440 0.14826 0.01225  0.01525  0.00679  89  GLU   A OE2  
1272 N  N    . GLU   A 87  ? 0.22797 0.20317 0.15765 0.02205  0.06165  0.05879  90  GLU   A N    
1273 C  CA   . GLU   A 87  ? 0.22456 0.21638 0.16816 0.03757  0.04663  0.05649  90  GLU   A CA   
1274 C  C    . GLU   A 87  ? 0.22505 0.19780 0.16468 0.02880  0.06086  0.04185  90  GLU   A C    
1275 O  O    . GLU   A 87  ? 0.22865 0.18691 0.17309 0.02266  0.07464  0.04492  90  GLU   A O    
1276 C  CB   . GLU   A 87  ? 0.22888 0.22435 0.20245 0.02754  0.03175  0.07123  90  GLU   A CB   
1277 C  CG   . GLU   A 87  ? 0.25459 0.22452 0.22294 0.01592  0.01792  0.06030  90  GLU   A CG   
1278 C  CD   . GLU   A 87  ? 0.24017 0.22350 0.25149 -0.03640 -0.01416 0.06574  90  GLU   A CD   
1279 O  OE1  . GLU   A 87  ? 0.25893 0.22991 0.27360 0.00958  0.01161  0.06633  90  GLU   A OE1  
1280 O  OE2  . GLU   A 87  ? 0.27774 0.22959 0.29791 -0.05130 -0.05576 0.07728  90  GLU   A OE2  
1287 N  N    . ILE   A 88  ? 0.23247 0.24643 0.17407 0.01895  0.07177  0.04041  91  ILE   A N    
1288 C  CA   . ILE   A 88  ? 0.24844 0.24933 0.17153 0.00734  0.07810  0.04005  91  ILE   A CA   
1289 C  C    . ILE   A 88  ? 0.27460 0.26499 0.17967 0.05503  0.11392  0.04094  91  ILE   A C    
1290 O  O    . ILE   A 88  ? 0.25043 0.30736 0.21430 0.04313  0.11394  0.05236  91  ILE   A O    
1291 C  CB   . ILE   A 88  ? 0.30982 0.26135 0.16973 -0.00044 0.06980  0.03431  91  ILE   A CB   
1292 C  CG1  . ILE   A 88  ? 0.33936 0.27887 0.18843 -0.03122 0.02409  0.05945  91  ILE   A CG1  
1293 C  CG2  . ILE   A 88  ? 0.32471 0.25286 0.19423 -0.01546 0.06047  0.00970  91  ILE   A CG2  
1294 C  CD1  . ILE   A 88  ? 0.35824 0.29563 0.22265 -0.00236 0.03274  0.04699  91  ILE   A CD1  
1306 N  N    . THR   A 89  ? 0.24558 0.25328 0.18984 0.04670  0.10797  0.04279  92  THR   A N    
1307 C  CA   . THR   A 89  ? 0.29079 0.25383 0.22868 0.07490  0.11227  0.05929  92  THR   A CA   
1308 C  C    . THR   A 89  ? 0.29925 0.23937 0.24854 0.07956  0.13379  0.04127  92  THR   A C    
1309 O  O    . THR   A 89  ? 0.31319 0.22876 0.25812 0.05649  0.13844  -0.00104 92  THR   A O    
1310 C  CB   . THR   A 89  ? 0.29026 0.29891 0.22983 0.09318  0.09723  0.05995  92  THR   A CB   
1311 O  OG1  . THR   A 89  ? 0.32398 0.32217 0.22744 0.10435  0.09599  0.07722  92  THR   A OG1  
1312 C  CG2  . THR   A 89  ? 0.31123 0.31272 0.24564 0.11276  0.09934  0.08975  92  THR   A CG2  
1320 N  N    . TYR   A 90  ? 0.36475 0.30080 0.25433 0.09267  0.16435  0.03410  93  TYR   A N    
1321 C  CA   . TYR   A 90  ? 0.38963 0.33500 0.26685 0.08691  0.17077  0.00150  93  TYR   A CA   
1322 C  C    . TYR   A 90  ? 0.40965 0.32939 0.27911 0.08996  0.16095  0.01735  93  TYR   A C    
1323 O  O    . TYR   A 90  ? 0.45408 0.34390 0.26109 0.08389  0.14596  0.01523  93  TYR   A O    
1324 C  CB   . TYR   A 90  ? 0.41805 0.37592 0.27328 0.07575  0.18209  -0.00393 93  TYR   A CB   
1325 C  CG   . TYR   A 90  ? 0.45441 0.40672 0.25565 0.04813  0.18321  -0.00660 93  TYR   A CG   
1326 C  CD1  . TYR   A 90  ? 0.49987 0.39787 0.22251 0.03992  0.16057  -0.01890 93  TYR   A CD1  
1327 C  CD2  . TYR   A 90  ? 0.47662 0.43879 0.26443 0.01836  0.19286  0.03174  93  TYR   A CD2  
1328 C  CE1  . TYR   A 90  ? 0.55764 0.41541 0.20736 0.03523  0.14580  0.00617  93  TYR   A CE1  
1329 C  CE2  . TYR   A 90  ? 0.50306 0.45260 0.25249 0.00024  0.18235  0.04778  93  TYR   A CE2  
1330 C  CZ   . TYR   A 90  ? 0.53153 0.44309 0.22319 0.01219  0.15966  0.04368  93  TYR   A CZ   
1331 O  OH   . TYR   A 90  ? 0.60124 0.47009 0.22098 0.00053  0.14367  0.04332  93  TYR   A OH   
1341 N  N    . ASP   A 91  ? 0.38817 0.33055 0.29835 0.10429  0.18132  0.01978  94  ASP   A N    
1342 C  CA   A ASP   A 91  ? 0.40116 0.34567 0.30988 0.10306  0.18113  0.02098  94  ASP   A CA   
1343 C  CA   B ASP   A 91  ? 0.39869 0.34588 0.31557 0.11239  0.17014  0.01203  94  ASP   A CA   
1344 C  C    . ASP   A 91  ? 0.38261 0.31139 0.30079 0.10157  0.17602  0.00472  94  ASP   A C    
1345 O  O    . ASP   A 91  ? 0.36567 0.35642 0.32195 0.06632  0.14839  0.03649  94  ASP   A O    
1346 C  CB   A ASP   A 91  ? 0.44612 0.40206 0.33788 0.07461  0.18305  0.03459  94  ASP   A CB   
1347 C  CB   B ASP   A 91  ? 0.43816 0.40339 0.35348 0.10091  0.15063  0.00896  94  ASP   A CB   
1348 C  CG   A ASP   A 91  ? 0.50239 0.44287 0.37425 0.08524  0.16684  0.03268  94  ASP   A CG   
1349 C  CG   B ASP   A 91  ? 0.47423 0.43802 0.39011 0.13307  0.12882  -0.00197 94  ASP   A CG   
1350 O  OD1  A ASP   A 91  ? 0.51524 0.43824 0.39127 0.11568  0.17226  0.02765  94  ASP   A OD1  
1351 O  OD1  B ASP   A 91  ? 0.48065 0.44716 0.40666 0.13996  0.12186  0.00845  94  ASP   A OD1  
1352 O  OD2  A ASP   A 91  ? 0.53405 0.47357 0.39351 0.09061  0.14580  0.03518  94  ASP   A OD2  
1353 O  OD2  B ASP   A 91  ? 0.49694 0.46542 0.40046 0.11956  0.12030  -0.01220 94  ASP   A OD2  
1360 N  N    . THR   A 92  ? 0.39439 0.24806 0.28658 0.05078  0.17918  -0.02284 95  THR   A N    
1361 C  CA   . THR   A 92  ? 0.37166 0.20227 0.25816 0.05681  0.14527  -0.00487 95  THR   A CA   
1362 C  C    . THR   A 92  ? 0.35721 0.19207 0.27449 0.08336  0.13423  -0.00173 95  THR   A C    
1363 O  O    . THR   A 92  ? 0.42460 0.20053 0.28923 0.08893  0.13094  -0.02796 95  THR   A O    
1364 C  CB   . THR   A 92  ? 0.38104 0.18481 0.22908 0.05219  0.14118  -0.00295 95  THR   A CB   
1365 O  OG1  . THR   A 92  ? 0.33930 0.17273 0.22299 0.04651  0.12408  -0.01637 95  THR   A OG1  
1366 C  CG2  . THR   A 92  ? 0.42178 0.24708 0.22618 0.05857  0.13520  0.00745  95  THR   A CG2  
1374 N  N    . PRO   A 93  ? 0.33180 0.20093 0.27062 0.08535  0.11938  0.02172  96  PRO   A N    
1375 C  CA   . PRO   A 93  ? 0.32786 0.22571 0.28206 0.08554  0.06812  0.03070  96  PRO   A CA   
1376 C  C    . PRO   A 93  ? 0.30888 0.20810 0.28340 0.07739  0.07714  0.04351  96  PRO   A C    
1377 O  O    . PRO   A 93  ? 0.35914 0.19503 0.35181 0.07259  0.08226  0.06135  96  PRO   A O    
1378 C  CB   . PRO   A 93  ? 0.32875 0.26819 0.29110 0.06030  0.04633  0.06568  96  PRO   A CB   
1379 C  CG   . PRO   A 93  ? 0.31868 0.27220 0.28169 0.04140  0.08507  0.04705  96  PRO   A CG   
1380 C  CD   . PRO   A 93  ? 0.33613 0.23431 0.26338 0.06708  0.10744  0.00995  96  PRO   A CD   
1388 N  N    . PHE   A 94  ? 0.30052 0.15356 0.23513 0.07008  0.06848  -0.00432 97  PHE   A N    
1389 C  CA   . PHE   A 94  ? 0.30957 0.15420 0.20987 0.03588  0.06302  -0.02077 97  PHE   A CA   
1390 C  C    . PHE   A 94  ? 0.32127 0.16637 0.20968 0.03466  0.06580  -0.02693 97  PHE   A C    
1391 O  O    . PHE   A 94  ? 0.38715 0.19415 0.21297 0.01085  0.10063  -0.02294 97  PHE   A O    
1392 C  CB   . PHE   A 94  ? 0.28429 0.15319 0.19159 0.05999  0.07244  -0.01991 97  PHE   A CB   
1393 C  CG   . PHE   A 94  ? 0.26584 0.13205 0.18550 0.05566  0.06676  0.00162  97  PHE   A CG   
1394 C  CD1  . PHE   A 94  ? 0.25485 0.14403 0.19491 0.03521  0.06693  0.01357  97  PHE   A CD1  
1395 C  CD2  . PHE   A 94  ? 0.26569 0.12996 0.20115 0.02989  0.07550  0.01197  97  PHE   A CD2  
1396 C  CE1  . PHE   A 94  ? 0.26668 0.13557 0.17687 0.03699  0.07608  0.01085  97  PHE   A CE1  
1397 C  CE2  . PHE   A 94  ? 0.25379 0.12849 0.18384 0.02729  0.07136  0.01429  97  PHE   A CE2  
1398 C  CZ   . PHE   A 94  ? 0.25576 0.12332 0.19092 0.05181  0.07084  0.02973  97  PHE   A CZ   
1408 N  N    . LYS   A 95  ? 0.30521 0.16391 0.19695 0.03828  0.05660  -0.02969 98  LYS   A N    
1409 C  CA   . LYS   A 95  ? 0.32232 0.19006 0.22544 0.06086  0.03888  -0.05948 98  LYS   A CA   
1410 C  C    . LYS   A 95  ? 0.29368 0.19815 0.22213 0.06246  0.02695  -0.04696 98  LYS   A C    
1411 O  O    . LYS   A 95  ? 0.28381 0.21503 0.20558 0.04789  0.03263  -0.05591 98  LYS   A O    
1412 C  CB   . LYS   A 95  ? 0.34035 0.24756 0.29798 0.05187  0.06145  -0.08801 98  LYS   A CB   
1413 C  CG   . LYS   A 95  ? 0.40137 0.30363 0.33134 0.04874  0.08416  -0.10252 98  LYS   A CG   
1414 C  CD   . LYS   A 95  ? 0.46868 0.39994 0.36648 0.05202  0.10313  -0.08313 98  LYS   A CD   
1415 C  CE   . LYS   A 95  ? 0.53070 0.47596 0.41133 0.03712  0.09710  -0.04241 98  LYS   A CE   
1416 N  NZ   . LYS   A 95  ? 0.56834 0.51193 0.43322 0.02681  0.10862  -0.02511 98  LYS   A NZ   
1430 N  N    . ARG   A 96  ? 0.30862 0.19995 0.21295 0.03638  0.05478  -0.05618 99  ARG   A N    
1431 C  CA   . ARG   A 96  ? 0.32359 0.19787 0.19652 0.02796  0.05003  -0.04562 99  ARG   A CA   
1432 C  C    . ARG   A 96  ? 0.30912 0.17296 0.20135 0.01146  0.03907  -0.06049 99  ARG   A C    
1433 O  O    . ARG   A 96  ? 0.34764 0.18754 0.21993 0.05372  0.05500  -0.06598 99  ARG   A O    
1434 C  CB   . ARG   A 96  ? 0.34861 0.19856 0.18639 0.05606  0.03910  -0.03949 99  ARG   A CB   
1435 C  CG   . ARG   A 96  ? 0.37502 0.20612 0.19689 0.04552  0.01808  -0.03320 99  ARG   A CG   
1436 C  CD   . ARG   A 96  ? 0.41168 0.21920 0.20390 -0.00239 -0.01365 -0.01841 99  ARG   A CD   
1437 N  NE   . ARG   A 96  ? 0.43753 0.21582 0.21814 0.02281  -0.00649 -0.03052 99  ARG   A NE   
1438 C  CZ   . ARG   A 96  ? 0.52445 0.22562 0.23925 0.00999  0.00225  -0.05769 99  ARG   A CZ   
1439 N  NH1  . ARG   A 96  ? 0.57137 0.28551 0.27249 0.01007  0.06387  -0.05898 99  ARG   A NH1  
1440 N  NH2  . ARG   A 96  ? 0.55099 0.22957 0.25464 -0.02077 -0.01353 -0.03791 99  ARG   A NH2  
1454 N  N    . GLU   A 97  ? 0.29833 0.15746 0.20816 0.03061  0.02624  -0.03747 100 GLU   A N    
1455 C  CA   . GLU   A 97  ? 0.27350 0.16337 0.22827 0.01151  0.02146  -0.06005 100 GLU   A CA   
1456 C  C    . GLU   A 97  ? 0.28683 0.16708 0.25343 0.01199  0.00192  -0.04578 100 GLU   A C    
1457 O  O    . GLU   A 97  ? 0.35188 0.15727 0.31941 0.02105  -0.02174 -0.01146 100 GLU   A O    
1458 C  CB   . GLU   A 97  ? 0.26989 0.16901 0.26954 -0.00668 0.03268  -0.05483 100 GLU   A CB   
1459 C  CG   . GLU   A 97  ? 0.30039 0.23314 0.29426 0.01632  0.02943  -0.04564 100 GLU   A CG   
1460 C  CD   . GLU   A 97  ? 0.32007 0.31766 0.33834 -0.00792 0.00083  -0.08583 100 GLU   A CD   
1461 O  OE1  . GLU   A 97  ? 0.36986 0.32824 0.35259 0.01422  -0.00689 -0.09288 100 GLU   A OE1  
1462 O  OE2  . GLU   A 97  ? 0.38091 0.44664 0.37923 -0.03608 -0.01257 -0.06581 100 GLU   A OE2  
1469 N  N    . LYS   A 98  ? 0.25171 0.18301 0.22249 0.01679  0.00722  -0.03672 101 LYS   A N    
1470 C  CA   . LYS   A 98  ? 0.25065 0.17532 0.23780 0.02079  0.02749  -0.04640 101 LYS   A CA   
1471 C  C    . LYS   A 98  ? 0.25197 0.15425 0.21853 0.03714  0.01911  -0.03304 101 LYS   A C    
1472 O  O    . LYS   A 98  ? 0.26822 0.15426 0.20290 0.04079  0.03595  -0.01225 101 LYS   A O    
1473 C  CB   . LYS   A 98  ? 0.27448 0.18704 0.26938 0.03982  0.03396  -0.06984 101 LYS   A CB   
1474 C  CG   . LYS   A 98  ? 0.28989 0.26807 0.29071 0.02656  0.03810  -0.04981 101 LYS   A CG   
1475 C  CD   . LYS   A 98  ? 0.31496 0.32670 0.33015 0.06988  0.04369  -0.01178 101 LYS   A CD   
1476 C  CE   . LYS   A 98  ? 0.30160 0.36081 0.36715 0.07534  0.04202  0.00416  101 LYS   A CE   
1477 N  NZ   . LYS   A 98  ? 0.35845 0.35182 0.40423 0.07165  0.01884  0.01676  101 LYS   A NZ   
1491 N  N    . SER   A 99  ? 0.25021 0.13901 0.22343 0.04037  -0.00756 -0.01560 102 SER   A N    
1492 C  CA   . SER   A 99  ? 0.25276 0.14573 0.21478 0.00903  0.00260  -0.01372 102 SER   A CA   
1493 C  C    . SER   A 99  ? 0.22876 0.15844 0.21478 0.04886  0.00441  -0.03247 102 SER   A C    
1494 O  O    . SER   A 99  ? 0.25084 0.21214 0.27019 0.04695  0.02321  -0.06828 102 SER   A O    
1495 C  CB   . SER   A 99  ? 0.32668 0.17092 0.25285 -0.01743 -0.00948 0.01480  102 SER   A CB   
1496 O  OG   . SER   A 99  ? 0.36353 0.21241 0.28724 -0.05138 0.00106  0.02542  102 SER   A OG   
1502 N  N    . PHE   A 100 ? 0.22125 0.13972 0.19768 0.02958  0.02860  -0.01598 103 PHE   A N    
1503 C  CA   . PHE   A 100 ? 0.20708 0.15212 0.20700 0.03374  0.03171  -0.00470 103 PHE   A CA   
1504 C  C    . PHE   A 100 ? 0.19119 0.12842 0.21005 0.01167  0.01122  0.00799  103 PHE   A C    
1505 O  O    . PHE   A 100 ? 0.19759 0.13945 0.19734 0.01074  0.01172  0.00988  103 PHE   A O    
1506 C  CB   . PHE   A 100 ? 0.22872 0.16631 0.20363 0.03510  0.03457  0.01403  103 PHE   A CB   
1507 C  CG   . PHE   A 100 ? 0.20639 0.13425 0.19205 0.00246  0.04064  0.01406  103 PHE   A CG   
1508 C  CD1  . PHE   A 100 ? 0.22782 0.13332 0.18922 0.01173  0.03381  0.02005  103 PHE   A CD1  
1509 C  CD2  . PHE   A 100 ? 0.22984 0.14255 0.17844 0.00429  0.03508  0.01824  103 PHE   A CD2  
1510 C  CE1  . PHE   A 100 ? 0.26148 0.12548 0.18885 0.02710  0.03861  0.02439  103 PHE   A CE1  
1511 C  CE2  . PHE   A 100 ? 0.23405 0.13725 0.17316 0.02583  0.04918  0.02033  103 PHE   A CE2  
1512 C  CZ   . PHE   A 100 ? 0.24218 0.15412 0.17548 0.03509  0.05689  0.02776  103 PHE   A CZ   
1522 N  N    . GLU   A 101 ? 0.20660 0.14881 0.22767 0.03056  0.02014  -0.01533 104 GLU   A N    
1523 C  CA   . GLU   A 101 ? 0.18908 0.14752 0.22161 0.01209  0.01626  0.01273  104 GLU   A CA   
1524 C  C    . GLU   A 101 ? 0.19550 0.16562 0.22610 0.02448  0.04159  0.01336  104 GLU   A C    
1525 O  O    . GLU   A 101 ? 0.19607 0.16412 0.28033 0.03325  0.05493  0.01015  104 GLU   A O    
1526 C  CB   . GLU   A 101 ? 0.23413 0.16704 0.23304 0.01190  0.00124  0.01470  104 GLU   A CB   
1527 C  CG   . GLU   A 101 ? 0.26888 0.23109 0.24708 -0.01891 -0.01033 0.04890  104 GLU   A CG   
1528 C  CD   . GLU   A 101 ? 0.31229 0.32761 0.29565 0.00589  0.01470  0.08157  104 GLU   A CD   
1529 O  OE1  . GLU   A 101 ? 0.39811 0.36036 0.32474 -0.00914 0.02616  0.08481  104 GLU   A OE1  
1530 O  OE2  . GLU   A 101 ? 0.36764 0.42072 0.33700 0.00412  0.00079  0.08481  104 GLU   A OE2  
1537 N  N    . ILE   A 102 ? 0.17433 0.14908 0.19560 0.02271  0.03502  0.00481  105 ILE   A N    
1538 C  CA   . ILE   A 102 ? 0.16868 0.14365 0.17810 0.01352  0.03263  0.00748  105 ILE   A CA   
1539 C  C    . ILE   A 102 ? 0.16887 0.13022 0.17415 0.01592  0.02291  0.01666  105 ILE   A C    
1540 O  O    . ILE   A 102 ? 0.17509 0.18261 0.17857 0.01601  0.03180  0.00937  105 ILE   A O    
1541 C  CB   . ILE   A 102 ? 0.18060 0.14187 0.18067 0.01815  0.02533  0.01988  105 ILE   A CB   
1542 C  CG1  . ILE   A 102 ? 0.19877 0.17038 0.16820 0.01925  0.02920  0.01490  105 ILE   A CG1  
1543 C  CG2  . ILE   A 102 ? 0.22004 0.14691 0.22400 0.00233  0.00873  0.03717  105 ILE   A CG2  
1544 C  CD1  . ILE   A 102 ? 0.19721 0.17711 0.15566 0.01957  0.02581  0.00915  105 ILE   A CD1  
1556 N  N    . VAL   A 103 ? 0.18121 0.14866 0.16980 0.01359  0.02519  0.02005  106 VAL   A N    
1557 C  CA   . VAL   A 103 ? 0.16232 0.14517 0.17204 0.01453  0.02806  0.04180  106 VAL   A CA   
1558 C  C    . VAL   A 103 ? 0.15441 0.17253 0.17537 0.01998  0.02576  0.04390  106 VAL   A C    
1559 O  O    . VAL   A 103 ? 0.18019 0.15309 0.19592 0.02333  0.05119  0.03188  106 VAL   A O    
1560 C  CB   . VAL   A 103 ? 0.19474 0.17525 0.18536 0.01103  0.01592  0.05031  106 VAL   A CB   
1561 C  CG1  . VAL   A 103 ? 0.19618 0.21882 0.21882 0.01182  0.00353  0.05877  106 VAL   A CG1  
1562 C  CG2  . VAL   A 103 ? 0.22842 0.19765 0.20913 0.01745  0.00340  0.08494  106 VAL   A CG2  
1572 N  N    . ILE   A 104 ? 0.16497 0.14947 0.16382 0.01457  0.03143  0.03321  107 ILE   A N    
1573 C  CA   . ILE   A 104 ? 0.17684 0.15605 0.16131 0.00525  0.02419  0.03134  107 ILE   A CA   
1574 C  C    . ILE   A 104 ? 0.16655 0.15058 0.15798 0.00919  0.01518  0.02948  107 ILE   A C    
1575 O  O    . ILE   A 104 ? 0.17659 0.18480 0.15546 0.00950  0.03259  0.01460  107 ILE   A O    
1576 C  CB   . ILE   A 104 ? 0.17759 0.15211 0.16214 0.01056  0.01533  0.02399  107 ILE   A CB   
1577 C  CG1  . ILE   A 104 ? 0.18245 0.18506 0.17838 0.01636  0.00304  0.01227  107 ILE   A CG1  
1578 C  CG2  . ILE   A 104 ? 0.19715 0.16653 0.16042 -0.00178 0.01546  0.01962  107 ILE   A CG2  
1579 C  CD1  . ILE   A 104 ? 0.19579 0.22007 0.18695 0.02286  0.01311  0.00639  107 ILE   A CD1  
1591 N  N    . MET   A 105 ? 0.16970 0.15604 0.15120 0.00142  0.01162  0.02703  108 MET   A N    
1592 C  CA   . MET   A 105 ? 0.17676 0.14837 0.15625 -0.00072 0.01796  0.04500  108 MET   A CA   
1593 C  C    . MET   A 105 ? 0.16390 0.13958 0.17159 0.01735  0.01131  0.04763  108 MET   A C    
1594 O  O    . MET   A 105 ? 0.20647 0.15264 0.16507 -0.00629 0.03479  0.04545  108 MET   A O    
1595 C  CB   . MET   A 105 ? 0.18633 0.16483 0.16488 0.02205  0.00560  0.04187  108 MET   A CB   
1596 C  CG   . MET   A 105 ? 0.19326 0.18936 0.18818 0.01289  0.00642  0.04074  108 MET   A CG   
1597 S  SD   . MET   A 105 ? 0.21898 0.21027 0.22095 0.03087  -0.03018 0.03606  108 MET   A SD   
1598 C  CE   . MET   A 105 ? 0.23560 0.19813 0.25245 0.01755  -0.05433 0.02497  108 MET   A CE   
1608 N  N    . VAL   A 106 ? 0.18360 0.15138 0.15109 0.01893  0.02281  0.02910  109 VAL   A N    
1609 C  CA   . VAL   A 106 ? 0.20762 0.14388 0.16981 0.02095  0.01880  0.02636  109 VAL   A CA   
1610 C  C    . VAL   A 106 ? 0.22459 0.15393 0.17597 0.01135  0.00006  0.04737  109 VAL   A C    
1611 O  O    . VAL   A 106 ? 0.27244 0.19766 0.14971 -0.00977 -0.00917 0.04306  109 VAL   A O    
1612 C  CB   . VAL   A 106 ? 0.23295 0.17348 0.18891 0.02951  0.03713  0.02561  109 VAL   A CB   
1613 C  CG1  . VAL   A 106 ? 0.27277 0.15974 0.20716 0.03822  0.02878  0.04075  109 VAL   A CG1  
1614 C  CG2  . VAL   A 106 ? 0.22258 0.19287 0.18999 0.05054  0.03063  0.03426  109 VAL   A CG2  
1624 N  N    . LEU   A 107 ? 0.21738 0.17321 0.16177 0.01533  -0.01890 0.06291  110 LEU   A N    
1625 C  CA   . LEU   A 107 ? 0.21395 0.18318 0.15430 0.00993  -0.01735 0.04953  110 LEU   A CA   
1626 C  C    . LEU   A 107 ? 0.21835 0.16620 0.17569 0.01629  -0.01672 0.05573  110 LEU   A C    
1627 O  O    . LEU   A 107 ? 0.21614 0.17531 0.18653 0.01680  -0.03423 0.05722  110 LEU   A O    
1628 C  CB   . LEU   A 107 ? 0.21497 0.17835 0.16758 -0.00110 -0.02482 0.05559  110 LEU   A CB   
1629 C  CG   . LEU   A 107 ? 0.19864 0.17548 0.16960 0.00612  -0.02554 0.04253  110 LEU   A CG   
1630 C  CD1  . LEU   A 107 ? 0.19754 0.18500 0.19311 0.01233  -0.03984 0.03479  110 LEU   A CD1  
1631 C  CD2  . LEU   A 107 ? 0.21589 0.18834 0.17428 0.01203  -0.03579 0.05752  110 LEU   A CD2  
1643 N  N    . LYS   A 108 ? 0.22128 0.18344 0.17758 0.01541  -0.03828 0.04925  111 LYS   A N    
1644 C  CA   . LYS   A 108 ? 0.22785 0.16604 0.18491 0.01132  -0.03581 0.04719  111 LYS   A CA   
1645 C  C    . LYS   A 108 ? 0.21232 0.16485 0.18400 -0.00054 -0.04437 0.04558  111 LYS   A C    
1646 O  O    . LYS   A 108 ? 0.23523 0.16906 0.19692 0.00864  -0.06121 0.04789  111 LYS   A O    
1647 C  CB   . LYS   A 108 ? 0.23333 0.18357 0.19033 0.01290  -0.03961 0.04921  111 LYS   A CB   
1648 C  CG   . LYS   A 108 ? 0.26168 0.20712 0.18827 -0.00154 -0.04267 0.03433  111 LYS   A CG   
1649 C  CD   . LYS   A 108 ? 0.27329 0.22547 0.18398 -0.00130 -0.06603 0.04292  111 LYS   A CD   
1650 C  CE   . LYS   A 108 ? 0.27824 0.20060 0.22734 -0.01034 -0.07974 0.05138  111 LYS   A CE   
1651 N  NZ   . LYS   A 108 ? 0.28863 0.20515 0.24208 0.00542  -0.07119 0.06971  111 LYS   A NZ   
1665 N  N    . ASP   A 109 ? 0.22253 0.18136 0.17159 -0.00126 -0.03677 0.04823  112 ASP   A N    
1666 C  CA   . ASP   A 109 ? 0.21853 0.18688 0.18781 -0.01081 -0.04531 0.06486  112 ASP   A CA   
1667 C  C    . ASP   A 109 ? 0.20904 0.17785 0.17839 -0.01406 -0.02932 0.06021  112 ASP   A C    
1668 O  O    . ASP   A 109 ? 0.23312 0.20484 0.17624 -0.02903 -0.03127 0.07574  112 ASP   A O    
1669 C  CB   . ASP   A 109 ? 0.22045 0.23724 0.24774 -0.05081 -0.05637 0.07555  112 ASP   A CB   
1670 C  CG   . ASP   A 109 ? 0.28000 0.30592 0.32641 -0.06126 -0.05944 0.07625  112 ASP   A CG   
1671 O  OD1  . ASP   A 109 ? 0.32493 0.32253 0.34754 -0.09058 -0.05320 0.01632  112 ASP   A OD1  
1672 O  OD2  . ASP   A 109 ? 0.31127 0.34214 0.37644 -0.08896 -0.09741 0.12135  112 ASP   A OD2  
1677 N  N    . LYS   A 110 ? 0.20825 0.17809 0.17042 -0.01065 -0.02119 0.06130  113 LYS   A N    
1678 C  CA   . LYS   A 110 ? 0.18442 0.18932 0.16976 -0.01459 -0.02560 0.06117  113 LYS   A CA   
1679 C  C    . LYS   A 110 ? 0.19219 0.17556 0.17301 0.00805  -0.01097 0.06583  113 LYS   A C    
1680 O  O    . LYS   A 110 ? 0.20659 0.19249 0.16458 0.00284  -0.01802 0.06882  113 LYS   A O    
1681 C  CB   . LYS   A 110 ? 0.19156 0.21212 0.19459 -0.00151 -0.01012 0.05339  113 LYS   A CB   
1682 C  CG   . LYS   A 110 ? 0.25060 0.29023 0.23032 0.06915  -0.01391 0.04130  113 LYS   A CG   
1683 C  CD   . LYS   A 110 ? 0.24895 0.36345 0.24766 0.07180  -0.04138 0.03015  113 LYS   A CD   
1684 C  CE   . LYS   A 110 ? 0.31328 0.45025 0.26872 0.06601  -0.03021 0.03360  113 LYS   A CE   
1685 N  NZ   . LYS   A 110 ? 0.31025 0.51308 0.25635 0.12741  0.00779  0.04781  113 LYS   A NZ   
1699 N  N    . PHE   A 111 ? 0.17709 0.17610 0.17099 -0.00006 -0.01175 0.06395  114 PHE   A N    
1700 C  CA   . PHE   A 111 ? 0.19264 0.15903 0.16899 -0.00402 0.01271  0.04189  114 PHE   A CA   
1701 C  C    . PHE   A 111 ? 0.16825 0.17493 0.16399 0.00253  0.01430  0.05338  114 PHE   A C    
1702 O  O    . PHE   A 111 ? 0.21643 0.18710 0.17700 0.01339  0.02525  0.06834  114 PHE   A O    
1703 C  CB   . PHE   A 111 ? 0.18515 0.14761 0.17437 0.00405  0.00440  0.03933  114 PHE   A CB   
1704 C  CG   . PHE   A 111 ? 0.17787 0.15109 0.20251 0.00951  0.00302  0.05112  114 PHE   A CG   
1705 C  CD1  . PHE   A 111 ? 0.18541 0.14450 0.20280 0.01943  -0.00480 0.03711  114 PHE   A CD1  
1706 C  CD2  . PHE   A 111 ? 0.18682 0.16031 0.19049 0.01163  -0.01115 0.04789  114 PHE   A CD2  
1707 C  CE1  . PHE   A 111 ? 0.19408 0.16292 0.22260 0.03265  -0.00336 0.02436  114 PHE   A CE1  
1708 C  CE2  . PHE   A 111 ? 0.20027 0.18272 0.19863 -0.00452 -0.03798 0.04904  114 PHE   A CE2  
1709 C  CZ   . PHE   A 111 ? 0.19020 0.15410 0.21507 0.02734  -0.02483 0.01767  114 PHE   A CZ   
1719 N  N    . GLN   A 112 ? 0.17521 0.14830 0.15461 0.01211  0.02097  0.03596  115 GLN   A N    
1720 C  CA   . GLN   A 112 ? 0.17456 0.17708 0.14740 0.02128  0.02444  0.04864  115 GLN   A CA   
1721 C  C    . GLN   A 112 ? 0.17579 0.15902 0.16209 0.00469  0.01223  0.04515  115 GLN   A C    
1722 O  O    . GLN   A 112 ? 0.20246 0.19909 0.15773 -0.00504 0.03986  0.04155  115 GLN   A O    
1723 C  CB   . GLN   A 112 ? 0.18792 0.20205 0.15800 0.04662  0.02223  0.03741  115 GLN   A CB   
1724 C  CG   . GLN   A 112 ? 0.18403 0.22818 0.20212 0.04776  0.02033  0.01506  115 GLN   A CG   
1725 C  CD   . GLN   A 112 ? 0.24595 0.27648 0.27069 0.07887  -0.01116 -0.01783 115 GLN   A CD   
1726 O  OE1  . GLN   A 112 ? 0.21951 0.35856 0.28844 0.03800  -0.00500 -0.02352 115 GLN   A OE1  
1727 N  NE2  . GLN   A 112 ? 0.30416 0.28266 0.32940 0.08903  -0.09475 -0.02178 115 GLN   A NE2  
1736 N  N    . VAL   A 113 ? 0.16634 0.15404 0.16952 0.02269  0.02353  0.04147  116 VAL   A N    
1737 C  CA   . VAL   A 113 ? 0.17160 0.14980 0.17416 0.02656  0.02521  0.03654  116 VAL   A CA   
1738 C  C    . VAL   A 113 ? 0.17324 0.15790 0.19246 0.02843  0.04618  0.04437  116 VAL   A C    
1739 O  O    . VAL   A 113 ? 0.19279 0.16957 0.19995 0.03262  0.05344  0.03441  116 VAL   A O    
1740 C  CB   . VAL   A 113 ? 0.17225 0.14619 0.16525 0.02249  0.02234  0.02957  116 VAL   A CB   
1741 C  CG1  . VAL   A 113 ? 0.19148 0.17282 0.19034 0.02224  0.01649  0.01994  116 VAL   A CG1  
1742 C  CG2  . VAL   A 113 ? 0.20499 0.16480 0.15542 0.04271  0.02173  0.03509  116 VAL   A CG2  
1752 N  N    . ALA   A 114 ? 0.19653 0.13819 0.23145 0.04129  0.06346  0.04997  117 ALA   A N    
1753 C  CA   . ALA   A 114 ? 0.21655 0.13903 0.25109 0.04795  0.05438  0.05982  117 ALA   A CA   
1754 C  C    . ALA   A 114 ? 0.22254 0.13120 0.25703 0.04376  0.06937  0.03948  117 ALA   A C    
1755 O  O    . ALA   A 114 ? 0.23545 0.17572 0.28058 0.02415  0.11279  -0.00271 117 ALA   A O    
1756 C  CB   . ALA   A 114 ? 0.24151 0.17988 0.26623 0.05882  0.04929  0.08073  117 ALA   A CB   
1762 N  N    . VAL   A 115 ? 0.21128 0.16922 0.25438 0.05850  0.07011  0.02852  118 VAL   A N    
1763 C  CA   . VAL   A 115 ? 0.22825 0.18491 0.28629 0.06761  0.07593  0.01138  118 VAL   A CA   
1764 C  C    . VAL   A 115 ? 0.21490 0.17728 0.35117 0.06267  0.06439  0.00217  118 VAL   A C    
1765 O  O    . VAL   A 115 ? 0.22665 0.20353 0.36637 0.07647  0.06199  -0.02499 118 VAL   A O    
1766 C  CB   . VAL   A 115 ? 0.25404 0.22185 0.27051 0.07810  0.08699  -0.00992 118 VAL   A CB   
1767 C  CG1  . VAL   A 115 ? 0.27851 0.26688 0.27074 0.05103  0.07619  -0.01596 118 VAL   A CG1  
1768 C  CG2  . VAL   A 115 ? 0.28143 0.24698 0.27333 0.10840  0.08298  -0.01005 118 VAL   A CG2  
1778 N  N    . ASN   A 116 ? 0.21596 0.17105 0.41903 0.05465  0.06761  0.01012  119 ASN   A N    
1779 C  CA   . ASN   A 116 ? 0.27058 0.17529 0.47371 0.06506  0.06712  0.00816  119 ASN   A CA   
1780 C  C    . ASN   A 116 ? 0.27859 0.19120 0.49061 0.08148  0.08234  0.08889  119 ASN   A C    
1781 O  O    . ASN   A 116 ? 0.32126 0.19916 0.53947 0.09042  0.08508  0.07620  119 ASN   A O    
1782 C  CB   . ASN   A 116 ? 0.28220 0.19463 0.48892 0.08645  0.05265  -0.04623 119 ASN   A CB   
1783 C  CG   . ASN   A 116 ? 0.31620 0.24722 0.48618 0.09483  0.03349  -0.08763 119 ASN   A CG   
1784 O  OD1  . ASN   A 116 ? 0.25841 0.24546 0.46574 0.07533  0.04426  -0.10643 119 ASN   A OD1  
1785 N  ND2  . ASN   A 116 ? 0.38739 0.30458 0.50214 0.12279  0.03839  -0.07196 119 ASN   A ND2  
1792 N  N    . GLY   A 117 ? 0.25901 0.23103 0.47162 0.08157  0.08962  0.14189  120 GLY   A N    
1793 C  CA   . GLY   A 117 ? 0.26170 0.28145 0.45454 0.07104  0.06806  0.14915  120 GLY   A CA   
1794 C  C    . GLY   A 117 ? 0.25924 0.29927 0.44637 0.10797  0.05629  0.15258  120 GLY   A C    
1795 O  O    . GLY   A 117 ? 0.27481 0.41099 0.46754 0.06930  0.01969  0.18405  120 GLY   A O    
1799 N  N    . LYS   A 118 ? 0.25787 0.22078 0.40699 0.09443  0.07078  0.12582  121 LYS   A N    
1800 C  CA   . LYS   A 118 ? 0.28928 0.22812 0.39077 0.11108  0.09771  0.09653  121 LYS   A CA   
1801 C  C    . LYS   A 118 ? 0.23392 0.22572 0.33729 0.09307  0.10722  0.09377  121 LYS   A C    
1802 O  O    . LYS   A 118 ? 0.22451 0.22658 0.34059 0.09226  0.09745  0.08080  121 LYS   A O    
1803 C  CB   . LYS   A 118 ? 0.37226 0.27588 0.43247 0.10399  0.11348  0.06494  121 LYS   A CB   
1804 C  CG   . LYS   A 118 ? 0.44505 0.35840 0.46572 0.08552  0.11531  0.02199  121 LYS   A CG   
1805 C  CD   . LYS   A 118 ? 0.50657 0.43919 0.48964 0.05413  0.11001  0.02350  121 LYS   A CD   
1806 C  CE   . LYS   A 118 ? 0.56745 0.49602 0.50334 0.04915  0.09192  0.03294  121 LYS   A CE   
1807 N  NZ   . LYS   A 118 ? 0.61089 0.54539 0.52763 0.03722  0.07451  0.02237  121 LYS   A NZ   
1821 N  N    . HIS   A 119 ? 0.21804 0.21987 0.33660 0.08787  0.06445  0.07794  122 HIS   A N    
1822 C  CA   . HIS   A 119 ? 0.22303 0.21649 0.31149 0.07979  0.06234  0.07720  122 HIS   A CA   
1823 C  C    . HIS   A 119 ? 0.24313 0.20222 0.28538 0.10136  0.09673  0.05360  122 HIS   A C    
1824 O  O    . HIS   A 119 ? 0.28213 0.22247 0.31477 0.11575  0.11867  0.03176  122 HIS   A O    
1825 C  CB   . HIS   A 119 ? 0.23499 0.23587 0.36063 0.06661  0.03821  0.09495  122 HIS   A CB   
1826 C  CG   . HIS   A 119 ? 0.24103 0.27955 0.40380 0.07505  0.02469  0.11316  122 HIS   A CG   
1827 N  ND1  . HIS   A 119 ? 0.27695 0.30179 0.41013 0.07652  -0.00422 0.10963  122 HIS   A ND1  
1828 C  CD2  . HIS   A 119 ? 0.23553 0.29676 0.42045 0.06437  0.03028  0.09839  122 HIS   A CD2  
1829 C  CE1  . HIS   A 119 ? 0.28344 0.30370 0.40559 0.04667  -0.01192 0.13488  122 HIS   A CE1  
1830 N  NE2  . HIS   A 119 ? 0.24064 0.29057 0.41488 0.03948  0.01729  0.11298  122 HIS   A NE2  
1838 N  N    . THR   A 120 ? 0.20556 0.19031 0.25477 0.07153  0.07027  0.04955  123 THR   A N    
1839 C  CA   . THR   A 120 ? 0.22953 0.18887 0.22198 0.06058  0.05956  0.04583  123 THR   A CA   
1840 C  C    . THR   A 120 ? 0.21153 0.19830 0.20334 0.06650  0.06291  0.03719  123 THR   A C    
1841 O  O    . THR   A 120 ? 0.23906 0.21682 0.20545 0.05422  0.08048  0.03284  123 THR   A O    
1842 C  CB   . THR   A 120 ? 0.24422 0.19526 0.24064 0.01193  0.04131  0.06310  123 THR   A CB   
1843 O  OG1  . THR   A 120 ? 0.26879 0.21160 0.27073 0.00502  0.02231  0.05210  123 THR   A OG1  
1844 C  CG2  . THR   A 120 ? 0.27645 0.19169 0.23607 0.02259  0.03540  0.04830  123 THR   A CG2  
1852 N  N    . LEU   A 121 ? 0.20625 0.18366 0.18569 0.04314  0.05499  0.03952  124 LEU   A N    
1853 C  CA   . LEU   A 121 ? 0.20854 0.19208 0.17775 0.04687  0.05722  0.03852  124 LEU   A CA   
1854 C  C    . LEU   A 121 ? 0.19814 0.18788 0.16709 0.02315  0.05855  0.05605  124 LEU   A C    
1855 O  O    . LEU   A 121 ? 0.21062 0.19021 0.18804 0.03566  0.05255  0.06648  124 LEU   A O    
1856 C  CB   . LEU   A 121 ? 0.21335 0.19365 0.17429 0.04061  0.05260  0.04528  124 LEU   A CB   
1857 C  CG   . LEU   A 121 ? 0.20632 0.17730 0.17115 0.03688  0.05188  0.03603  124 LEU   A CG   
1858 C  CD1  . LEU   A 121 ? 0.20291 0.20744 0.15744 0.03597  0.04538  0.03175  124 LEU   A CD1  
1859 C  CD2  . LEU   A 121 ? 0.22543 0.18017 0.18513 0.03798  0.04579  0.03749  124 LEU   A CD2  
1871 N  N    . LEU   A 122 ? 0.21703 0.19012 0.16963 0.03258  0.05426  0.05939  125 LEU   A N    
1872 C  CA   . LEU   A 122 ? 0.20938 0.20093 0.16486 0.02100  0.04401  0.06040  125 LEU   A CA   
1873 C  C    . LEU   A 122 ? 0.21550 0.18670 0.15169 0.02122  0.02190  0.05294  125 LEU   A C    
1874 O  O    . LEU   A 122 ? 0.25885 0.19173 0.17157 0.01567  0.02334  0.05552  125 LEU   A O    
1875 C  CB   . LEU   A 122 ? 0.20861 0.25105 0.17985 0.00546  0.03949  0.06108  125 LEU   A CB   
1876 C  CG   . LEU   A 122 ? 0.20181 0.31296 0.18392 0.04527  0.04781  0.07960  125 LEU   A CG   
1877 C  CD1  . LEU   A 122 ? 0.19791 0.37104 0.20386 0.02448  0.04477  0.09475  125 LEU   A CD1  
1878 C  CD2  . LEU   A 122 ? 0.22501 0.31803 0.19582 0.07978  0.06128  0.09444  125 LEU   A CD2  
1890 N  N    . TYR   A 123 ? 0.20446 0.16881 0.14918 -0.00113 0.00946  0.05404  126 TYR   A N    
1891 C  CA   . TYR   A 123 ? 0.21764 0.15580 0.16066 -0.00135 -0.01176 0.05078  126 TYR   A CA   
1892 C  C    . TYR   A 123 ? 0.20569 0.16944 0.16648 -0.01250 -0.01837 0.06254  126 TYR   A C    
1893 O  O    . TYR   A 123 ? 0.22121 0.16178 0.16021 -0.00856 -0.02212 0.05410  126 TYR   A O    
1894 C  CB   . TYR   A 123 ? 0.21983 0.13624 0.17599 0.00630  -0.01267 0.03524  126 TYR   A CB   
1895 C  CG   . TYR   A 123 ? 0.21104 0.14473 0.16783 0.00174  -0.01039 0.02568  126 TYR   A CG   
1896 C  CD1  . TYR   A 123 ? 0.20590 0.14967 0.16400 0.01377  -0.00129 0.03732  126 TYR   A CD1  
1897 C  CD2  . TYR   A 123 ? 0.23701 0.16466 0.15831 -0.00007 -0.01631 0.03455  126 TYR   A CD2  
1898 C  CE1  . TYR   A 123 ? 0.20107 0.14806 0.15954 0.01660  0.00838  0.02569  126 TYR   A CE1  
1899 C  CE2  . TYR   A 123 ? 0.24174 0.13737 0.15945 0.00701  -0.02237 0.03623  126 TYR   A CE2  
1900 C  CZ   . TYR   A 123 ? 0.20462 0.14618 0.15489 -0.00060 -0.01665 0.04923  126 TYR   A CZ   
1901 O  OH   . TYR   A 123 ? 0.22137 0.14695 0.15323 0.01405  -0.00229 0.03442  126 TYR   A OH   
1911 N  N    . GLY   A 124 ? 0.20939 0.16794 0.17811 -0.00840 -0.01442 0.05577  127 GLY   A N    
1912 C  CA   . GLY   A 124 ? 0.22951 0.16122 0.18481 -0.02753 -0.03916 0.04833  127 GLY   A CA   
1913 C  C    . GLY   A 124 ? 0.22476 0.14950 0.18603 -0.02554 -0.03517 0.05670  127 GLY   A C    
1914 O  O    . GLY   A 124 ? 0.24787 0.15469 0.19253 -0.00681 -0.04947 0.05095  127 GLY   A O    
1918 N  N    . HIS   A 125 ? 0.21770 0.15909 0.18174 -0.01374 -0.03104 0.05240  128 HIS   A N    
1919 C  CA   . HIS   A 125 ? 0.23233 0.15937 0.17714 -0.02628 -0.04246 0.04894  128 HIS   A CA   
1920 C  C    . HIS   A 125 ? 0.24085 0.15726 0.18854 -0.03068 -0.03342 0.07113  128 HIS   A C    
1921 O  O    . HIS   A 125 ? 0.24826 0.16932 0.23024 -0.03150 -0.04113 0.07467  128 HIS   A O    
1922 C  CB   . HIS   A 125 ? 0.22116 0.17275 0.18432 -0.01615 -0.03206 0.03292  128 HIS   A CB   
1923 C  CG   . HIS   A 125 ? 0.21828 0.16424 0.18845 0.00216  -0.02089 0.05881  128 HIS   A CG   
1924 N  ND1  . HIS   A 125 ? 0.22271 0.18106 0.18065 -0.00004 -0.03161 0.06835  128 HIS   A ND1  
1925 C  CD2  . HIS   A 125 ? 0.22126 0.20618 0.17615 0.01024  -0.01653 0.06545  128 HIS   A CD2  
1926 C  CE1  . HIS   A 125 ? 0.21116 0.20138 0.18114 0.01523  -0.02895 0.07280  128 HIS   A CE1  
1927 N  NE2  . HIS   A 125 ? 0.21168 0.20561 0.18168 0.01493  -0.02088 0.07008  128 HIS   A NE2  
1935 N  N    . ARG   A 126 ? 0.25207 0.14807 0.15399 -0.00709 -0.02930 0.03565  129 ARG   A N    
1936 C  CA   . ARG   A 126 ? 0.26829 0.13320 0.15072 0.00176  -0.02939 0.03721  129 ARG   A CA   
1937 C  C    . ARG   A 126 ? 0.31189 0.14146 0.17813 0.00091  -0.01419 0.03499  129 ARG   A C    
1938 O  O    . ARG   A 126 ? 0.37807 0.14882 0.22711 0.01547  0.02847  0.04606  129 ARG   A O    
1939 C  CB   . ARG   A 126 ? 0.27725 0.14643 0.16047 -0.00355 -0.02307 0.03115  129 ARG   A CB   
1940 C  CG   . ARG   A 126 ? 0.24290 0.16314 0.16974 -0.01692 -0.03247 0.03301  129 ARG   A CG   
1941 C  CD   . ARG   A 126 ? 0.24003 0.16440 0.16531 -0.02130 -0.02888 0.04130  129 ARG   A CD   
1942 N  NE   . ARG   A 126 ? 0.22740 0.16636 0.17379 -0.01294 -0.02032 0.05280  129 ARG   A NE   
1943 C  CZ   . ARG   A 126 ? 0.22652 0.18325 0.15846 -0.02291 -0.00579 0.05798  129 ARG   A CZ   
1944 N  NH1  . ARG   A 126 ? 0.24569 0.18938 0.14013 -0.01473 -0.00740 0.03798  129 ARG   A NH1  
1945 N  NH2  . ARG   A 126 ? 0.26367 0.18383 0.16925 -0.00826 -0.00270 0.05092  129 ARG   A NH2  
1959 N  N    . ILE   A 127 ? 0.29271 0.15644 0.20121 0.00965  -0.00872 0.01683  130 ILE   A N    
1960 C  CA   . ILE   A 127 ? 0.30234 0.16755 0.20494 0.01296  0.00176  0.03562  130 ILE   A CA   
1961 C  C    . ILE   A 127 ? 0.30609 0.18373 0.20214 -0.00904 -0.02874 0.03093  130 ILE   A C    
1962 O  O    . ILE   A 127 ? 0.30554 0.17185 0.18872 0.01394  -0.03660 0.02868  130 ILE   A O    
1963 C  CB   . ILE   A 127 ? 0.28288 0.16612 0.19236 0.02306  -0.03069 0.00120  130 ILE   A CB   
1964 C  CG1  . ILE   A 127 ? 0.29318 0.18557 0.19935 0.01719  -0.02513 0.00480  130 ILE   A CG1  
1965 C  CG2  . ILE   A 127 ? 0.30482 0.22966 0.19861 0.00856  -0.03436 0.00499  130 ILE   A CG2  
1966 C  CD1  . ILE   A 127 ? 0.31505 0.17957 0.18677 0.02403  -0.02452 0.00601  130 ILE   A CD1  
1978 N  N    . GLY   A 128 ? 0.29350 0.19468 0.19863 -0.02450 -0.01316 -0.00499 131 GLY   A N    
1979 C  CA   . GLY   A 128 ? 0.29511 0.24250 0.19894 -0.05700 -0.03055 0.00614  131 GLY   A CA   
1980 C  C    . GLY   A 128 ? 0.25369 0.23617 0.17486 -0.03145 -0.04323 0.01139  131 GLY   A C    
1981 O  O    . GLY   A 128 ? 0.25840 0.22472 0.17524 -0.03643 -0.04732 0.02833  131 GLY   A O    
1985 N  N    . PRO   A 129 ? 0.24628 0.25183 0.19303 -0.00896 -0.03865 0.00610  132 PRO   A N    
1986 C  CA   . PRO   A 129 ? 0.26647 0.21045 0.19246 -0.00148 -0.05518 0.01869  132 PRO   A CA   
1987 C  C    . PRO   A 129 ? 0.25244 0.20036 0.17808 0.00175  -0.06269 0.01366  132 PRO   A C    
1988 O  O    . PRO   A 129 ? 0.25286 0.18906 0.17141 0.00742  -0.04680 0.01118  132 PRO   A O    
1989 C  CB   . PRO   A 129 ? 0.28609 0.25632 0.22180 0.00769  -0.03140 0.03933  132 PRO   A CB   
1990 C  CG   . PRO   A 129 ? 0.26570 0.30220 0.23085 0.04231  -0.04357 0.03389  132 PRO   A CG   
1991 C  CD   . PRO   A 129 ? 0.24639 0.31072 0.20432 0.00788  -0.03187 0.01135  132 PRO   A CD   
1999 N  N    . GLU   A 130 ? 0.25760 0.23816 0.16996 -0.02501 -0.05406 0.01253  133 GLU   A N    
2000 C  CA   . GLU   A 130 ? 0.28428 0.20537 0.17494 -0.01727 -0.03760 -0.00898 133 GLU   A CA   
2001 C  C    . GLU   A 130 ? 0.29555 0.18784 0.18351 0.00969  -0.02840 -0.03858 133 GLU   A C    
2002 O  O    . GLU   A 130 ? 0.31252 0.21195 0.21073 0.03213  -0.01736 -0.05149 133 GLU   A O    
2003 C  CB   . GLU   A 130 ? 0.34011 0.25937 0.19589 -0.05760 -0.03428 -0.01482 133 GLU   A CB   
2004 C  CG   . GLU   A 130 ? 0.38830 0.30854 0.23366 -0.10177 -0.06265 -0.00946 133 GLU   A CG   
2005 C  CD   . GLU   A 130 ? 0.45552 0.36299 0.27680 -0.15434 -0.02724 -0.01469 133 GLU   A CD   
2006 O  OE1  . GLU   A 130 ? 0.40565 0.44021 0.23678 -0.18649 -0.00543 -0.04732 133 GLU   A OE1  
2007 O  OE2  . GLU   A 130 ? 0.52702 0.35345 0.33954 -0.16932 0.00358  0.01564  133 GLU   A OE2  
2014 N  N    . LYS   A 131 ? 0.29838 0.17895 0.17692 -0.00865 -0.04840 -0.01504 134 LYS   A N    
2015 C  CA   . LYS   A 131 ? 0.28201 0.17797 0.19915 0.00758  -0.04699 -0.00553 134 LYS   A CA   
2016 C  C    . LYS   A 131 ? 0.25212 0.16718 0.18360 0.02132  -0.02747 -0.01056 134 LYS   A C    
2017 O  O    . LYS   A 131 ? 0.26655 0.18398 0.23626 0.03404  -0.02850 -0.00208 134 LYS   A O    
2018 C  CB   . LYS   A 131 ? 0.28866 0.19083 0.25487 -0.01338 -0.06103 0.03165  134 LYS   A CB   
2019 C  CG   . LYS   A 131 ? 0.37693 0.21770 0.33542 -0.03572 -0.04673 0.04125  134 LYS   A CG   
2020 C  CD   . LYS   A 131 ? 0.40836 0.20658 0.38281 -0.04856 -0.02147 0.04248  134 LYS   A CD   
2021 C  CE   . LYS   A 131 ? 0.44626 0.24426 0.41492 -0.08065 -0.02647 0.04424  134 LYS   A CE   
2022 N  NZ   . LYS   A 131 ? 0.52923 0.33331 0.45576 -0.08599 -0.03594 0.04629  134 LYS   A NZ   
2036 N  N    . ILE   A 132 ? 0.22766 0.16037 0.14498 0.02325  -0.02445 -0.02023 135 ILE   A N    
2037 C  CA   . ILE   A 132 ? 0.20918 0.15697 0.13759 0.01300  -0.02248 -0.00593 135 ILE   A CA   
2038 C  C    . ILE   A 132 ? 0.21615 0.17400 0.13561 0.02620  -0.02416 -0.00937 135 ILE   A C    
2039 O  O    . ILE   A 132 ? 0.21708 0.23902 0.13862 0.02352  -0.03304 -0.00739 135 ILE   A O    
2040 C  CB   . ILE   A 132 ? 0.21117 0.17038 0.12964 0.01722  -0.01861 -0.01105 135 ILE   A CB   
2041 C  CG1  . ILE   A 132 ? 0.21411 0.17151 0.14098 0.02642  -0.01017 -0.00143 135 ILE   A CG1  
2042 C  CG2  . ILE   A 132 ? 0.23036 0.14981 0.13507 0.02602  -0.03760 -0.01665 135 ILE   A CG2  
2043 C  CD1  . ILE   A 132 ? 0.21677 0.17500 0.14068 0.02303  -0.02274 0.00562  135 ILE   A CD1  
2055 N  N    . ASP   A 133 ? 0.21398 0.17003 0.11259 0.02956  -0.02048 -0.02652 136 ASP   A N    
2056 C  CA   . ASP   A 133 ? 0.21526 0.18628 0.11177 0.04371  -0.02594 -0.04375 136 ASP   A CA   
2057 C  C    . ASP   A 133 ? 0.20048 0.18424 0.11569 0.03962  -0.00231 -0.03767 136 ASP   A C    
2058 O  O    . ASP   A 133 ? 0.21141 0.19984 0.12236 0.02736  -0.00237 -0.04155 136 ASP   A O    
2059 C  CB   . ASP   A 133 ? 0.25103 0.21557 0.14774 0.05375  -0.01156 -0.05213 136 ASP   A CB   
2060 C  CG   . ASP   A 133 ? 0.30112 0.21020 0.16612 0.08334  -0.02367 -0.06595 136 ASP   A CG   
2061 O  OD1  . ASP   A 133 ? 0.27675 0.18090 0.15784 0.05937  -0.03355 -0.04524 136 ASP   A OD1  
2062 O  OD2  . ASP   A 133 ? 0.41225 0.25136 0.21296 0.13895  -0.04697 -0.08432 136 ASP   A OD2  
2067 N  N    . THR   A 134 ? 0.20366 0.16558 0.11316 0.03521  -0.01193 -0.03925 137 THR   A N    
2068 C  CA   . THR   A 134 ? 0.20537 0.15388 0.12052 0.03683  -0.01560 -0.02738 137 THR   A CA   
2069 C  C    . THR   A 134 ? 0.19466 0.14218 0.11181 0.03332  -0.00291 -0.01642 137 THR   A C    
2070 O  O    . THR   A 134 ? 0.21226 0.14241 0.11943 0.02464  0.00825  -0.01641 137 THR   A O    
2071 C  CB   . THR   A 134 ? 0.22133 0.15904 0.13424 0.03872  -0.01554 -0.03706 137 THR   A CB   
2072 O  OG1  . THR   A 134 ? 0.23451 0.18264 0.14634 0.06226  -0.01187 -0.04224 137 THR   A OG1  
2073 C  CG2  . THR   A 134 ? 0.23170 0.17452 0.16790 0.03772  -0.04283 -0.04269 137 THR   A CG2  
2081 N  N    . LEU   A 135 ? 0.18845 0.15489 0.11406 0.02747  0.00178  -0.02297 138 LEU   A N    
2082 C  CA   A LEU   A 135 ? 0.19276 0.14575 0.12038 0.02931  -0.02376 -0.02663 138 LEU   A CA   
2083 C  CA   B LEU   A 135 ? 0.18592 0.14465 0.11907 0.02859  0.00895  -0.03756 138 LEU   A CA   
2084 C  C    . LEU   A 135 ? 0.18263 0.14729 0.12176 0.02594  0.01089  -0.01195 138 LEU   A C    
2085 O  O    . LEU   A 135 ? 0.19128 0.17527 0.11232 0.01387  0.00436  -0.02970 138 LEU   A O    
2086 C  CB   A LEU   A 135 ? 0.23000 0.17268 0.13168 0.04916  -0.04385 -0.01191 138 LEU   A CB   
2087 C  CB   B LEU   A 135 ? 0.20683 0.16034 0.12466 0.04491  0.03000  -0.03928 138 LEU   A CB   
2088 C  CG   A LEU   A 135 ? 0.21422 0.16543 0.15173 0.03645  -0.00487 -0.00242 138 LEU   A CG   
2089 C  CG   B LEU   A 135 ? 0.18552 0.14657 0.14577 0.01842  0.02091  -0.01590 138 LEU   A CG   
2090 C  CD1  A LEU   A 135 ? 0.21197 0.13830 0.15314 0.02964  0.00018  -0.01009 138 LEU   A CD1  
2091 C  CD1  B LEU   A 135 ? 0.18998 0.14241 0.16061 0.01094  -0.00832 -0.01132 138 LEU   A CD1  
2092 C  CD2  A LEU   A 135 ? 0.24160 0.14169 0.15550 0.01237  0.00226  -0.02462 138 LEU   A CD2  
2093 C  CD2  B LEU   A 135 ? 0.19309 0.14809 0.16731 0.01365  -0.00145 0.00502  138 LEU   A CD2  
2114 N  N    . GLY   A 136 ? 0.17864 0.13743 0.10746 0.02231  0.00956  -0.01787 139 GLY   A N    
2115 C  CA   . GLY   A 136 ? 0.16267 0.14146 0.11757 0.01726  -0.00262 -0.02370 139 GLY   A CA   
2116 C  C    . GLY   A 136 ? 0.18410 0.13643 0.10850 0.01733  0.00163  -0.01717 139 GLY   A C    
2117 O  O    . GLY   A 136 ? 0.17620 0.14886 0.12320 0.01134  0.01251  -0.02873 139 GLY   A O    
2121 N  N    . ILE   A 137 ? 0.16979 0.13214 0.11311 0.01924  0.01600  -0.01982 140 ILE   A N    
2122 C  CA   . ILE   A 137 ? 0.17104 0.12230 0.11323 0.00515  0.01157  -0.02032 140 ILE   A CA   
2123 C  C    . ILE   A 137 ? 0.18246 0.13472 0.12082 0.02040  0.02153  -0.01357 140 ILE   A C    
2124 O  O    . ILE   A 137 ? 0.18028 0.17226 0.10307 0.01259  0.00574  -0.02105 140 ILE   A O    
2125 C  CB   . ILE   A 137 ? 0.17253 0.13943 0.11100 0.01404  0.01605  -0.00262 140 ILE   A CB   
2126 C  CG1  . ILE   A 137 ? 0.18720 0.13961 0.12407 0.01019  0.00770  0.00344  140 ILE   A CG1  
2127 C  CG2  . ILE   A 137 ? 0.20117 0.13535 0.12662 0.01811  0.02315  -0.01846 140 ILE   A CG2  
2128 C  CD1  . ILE   A 137 ? 0.20962 0.16388 0.15702 0.00668  -0.00153 0.01181  140 ILE   A CD1  
2140 N  N    . TYR   A 138 ? 0.18633 0.13479 0.11404 0.02086  0.02495  -0.01813 141 TYR   A N    
2141 C  CA   . TYR   A 138 ? 0.17946 0.13346 0.11970 0.00661  0.00111  -0.02073 141 TYR   A CA   
2142 C  C    . TYR   A 138 ? 0.20978 0.12901 0.11774 0.01338  0.01525  -0.02842 141 TYR   A C    
2143 O  O    . TYR   A 138 ? 0.20884 0.15164 0.11749 0.00375  0.01823  -0.03395 141 TYR   A O    
2144 C  CB   . TYR   A 138 ? 0.19557 0.14387 0.12995 0.00921  -0.00249 -0.02946 141 TYR   A CB   
2145 C  CG   . TYR   A 138 ? 0.19989 0.14802 0.12842 0.02262  -0.00213 -0.04639 141 TYR   A CG   
2146 C  CD1  . TYR   A 138 ? 0.19682 0.21766 0.19143 0.02128  -0.01685 -0.09534 141 TYR   A CD1  
2147 C  CD2  . TYR   A 138 ? 0.20676 0.15200 0.14370 0.00337  0.01622  -0.04326 141 TYR   A CD2  
2148 C  CE1  . TYR   A 138 ? 0.22347 0.21699 0.21193 0.03571  -0.00761 -0.10715 141 TYR   A CE1  
2149 C  CE2  . TYR   A 138 ? 0.19531 0.15854 0.15698 0.01151  0.00689  -0.05068 141 TYR   A CE2  
2150 C  CZ   . TYR   A 138 ? 0.20559 0.16246 0.15355 0.03814  -0.02623 -0.05974 141 TYR   A CZ   
2151 O  OH   . TYR   A 138 ? 0.22562 0.17699 0.17446 0.05810  -0.02018 -0.07398 141 TYR   A OH   
2161 N  N    . GLY   A 139 ? 0.20275 0.13923 0.13145 0.01045  0.00045  -0.03739 142 GLY   A N    
2162 C  CA   . GLY   A 139 ? 0.22032 0.13977 0.12178 0.00448  0.00097  -0.02668 142 GLY   A CA   
2163 C  C    . GLY   A 139 ? 0.23057 0.15251 0.13373 -0.01077 0.01236  -0.03101 142 GLY   A C    
2164 O  O    . GLY   A 139 ? 0.27064 0.18191 0.15334 -0.03405 0.04600  -0.04320 142 GLY   A O    
2168 N  N    . LYS   A 140 ? 0.25647 0.13536 0.12477 0.01085  0.00829  -0.01564 143 LYS   A N    
2169 C  CA   . LYS   A 140 ? 0.25661 0.13398 0.14272 -0.00711 0.00003  -0.03311 143 LYS   A CA   
2170 C  C    . LYS   A 140 ? 0.26211 0.12653 0.14209 -0.00900 0.02369  -0.03101 143 LYS   A C    
2171 O  O    . LYS   A 140 ? 0.28486 0.15355 0.14373 0.00980  0.03641  -0.01295 143 LYS   A O    
2172 C  CB   . LYS   A 140 ? 0.29513 0.14529 0.15711 0.00165  -0.01261 -0.01896 143 LYS   A CB   
2173 C  CG   . LYS   A 140 ? 0.30258 0.21037 0.16801 -0.01040 -0.03725 0.00164  143 LYS   A CG   
2174 C  CD   . LYS   A 140 ? 0.28196 0.24948 0.18690 0.00648  -0.06392 -0.02031 143 LYS   A CD   
2175 C  CE   . LYS   A 140 ? 0.31602 0.28905 0.23542 0.00329  -0.09842 -0.04195 143 LYS   A CE   
2176 N  NZ   . LYS   A 140 ? 0.34940 0.32901 0.26615 0.02490  -0.09953 -0.05634 143 LYS   A NZ   
2190 N  N    . VAL   A 141 ? 0.24078 0.14024 0.13599 0.00455  0.03031  -0.01727 144 VAL   A N    
2191 C  CA   . VAL   A 141 ? 0.22809 0.12477 0.13270 0.01543  0.02675  -0.01827 144 VAL   A CA   
2192 C  C    . VAL   A 141 ? 0.20732 0.13009 0.14983 -0.00292 0.02344  -0.01338 144 VAL   A C    
2193 O  O    . VAL   A 141 ? 0.22884 0.15556 0.14988 0.02658  0.03447  -0.00852 144 VAL   A O    
2194 C  CB   . VAL   A 141 ? 0.21760 0.13077 0.12873 0.00238  0.00843  -0.01080 144 VAL   A CB   
2195 C  CG1  . VAL   A 141 ? 0.22294 0.14588 0.13548 -0.00457 0.02068  -0.01721 144 VAL   A CG1  
2196 C  CG2  . VAL   A 141 ? 0.20873 0.16638 0.14116 -0.02252 0.03216  0.00741  144 VAL   A CG2  
2206 N  N    . ASN   A 142 ? 0.20764 0.14155 0.12577 0.00029  0.02657  -0.01624 145 ASN   A N    
2207 C  CA   A ASN   A 142 ? 0.19659 0.14122 0.13644 -0.01074 0.02267  -0.00420 145 ASN   A CA   
2208 C  CA   B ASN   A 142 ? 0.21156 0.14311 0.14985 0.00056  0.01459  -0.00010 145 ASN   A CA   
2209 C  C    . ASN   A 142 ? 0.21273 0.13524 0.13241 0.01400  0.02928  -0.00392 145 ASN   A C    
2210 O  O    . ASN   A 142 ? 0.21321 0.19679 0.15558 0.03511  0.01616  -0.02635 145 ASN   A O    
2211 C  CB   A ASN   A 142 ? 0.22195 0.17427 0.17064 -0.04357 0.01650  0.01015  145 ASN   A CB   
2212 C  CB   B ASN   A 142 ? 0.25831 0.17297 0.20795 -0.02196 -0.01385 0.01970  145 ASN   A CB   
2213 C  CG   A ASN   A 142 ? 0.28413 0.20683 0.21269 -0.07041 0.03142  0.00617  145 ASN   A CG   
2214 C  CG   B ASN   A 142 ? 0.32247 0.20753 0.26980 -0.05017 -0.02183 0.01555  145 ASN   A CG   
2215 O  OD1  A ASN   A 142 ? 0.32888 0.22744 0.22729 -0.09130 0.04705  0.02228  145 ASN   A OD1  
2216 O  OD1  B ASN   A 142 ? 0.38535 0.27859 0.29731 -0.01352 -0.01005 -0.00839 145 ASN   A OD1  
2217 N  ND2  A ASN   A 142 ? 0.35234 0.27590 0.25364 -0.06244 0.04903  0.02176  145 ASN   A ND2  
2218 N  ND2  B ASN   A 142 ? 0.33572 0.22594 0.29786 -0.05564 -0.04168 0.02495  145 ASN   A ND2  
2229 N  N    . ILE   A 143 ? 0.18009 0.14512 0.13473 0.00311  0.01371  -0.00513 146 ILE   A N    
2230 C  CA   . ILE   A 143 ? 0.17329 0.15532 0.13996 0.00077  0.03161  0.00164  146 ILE   A CA   
2231 C  C    . ILE   A 143 ? 0.17664 0.15824 0.15078 -0.00166 0.02478  0.00333  146 ILE   A C    
2232 O  O    . ILE   A 143 ? 0.18823 0.18075 0.15403 0.00038  0.03779  0.01386  146 ILE   A O    
2233 C  CB   . ILE   A 143 ? 0.17558 0.13980 0.14306 -0.00002 0.02373  -0.00297 146 ILE   A CB   
2234 C  CG1  . ILE   A 143 ? 0.18739 0.14545 0.14483 0.00620  0.02094  -0.00255 146 ILE   A CG1  
2235 C  CG2  . ILE   A 143 ? 0.16660 0.15542 0.15624 0.00175  0.01769  -0.00180 146 ILE   A CG2  
2236 C  CD1  . ILE   A 143 ? 0.18705 0.15067 0.15211 0.00008  0.04125  0.00653  146 ILE   A CD1  
2248 N  N    . HIS   A 144 ? 0.19074 0.15224 0.15154 -0.00644 0.01959  0.00926  147 HIS   A N    
2249 C  CA   . HIS   A 144 ? 0.20319 0.16991 0.16323 -0.00997 0.02915  0.02380  147 HIS   A CA   
2250 C  C    . HIS   A 144 ? 0.16923 0.17287 0.15559 -0.01051 0.03056  0.02193  147 HIS   A C    
2251 O  O    . HIS   A 144 ? 0.18231 0.20804 0.15780 -0.01233 0.02518  0.02804  147 HIS   A O    
2252 C  CB   . HIS   A 144 ? 0.23164 0.17671 0.17582 -0.00886 0.02036  0.03451  147 HIS   A CB   
2253 C  CG   . HIS   A 144 ? 0.27706 0.18537 0.21507 -0.03179 0.02444  -0.00278 147 HIS   A CG   
2254 N  ND1  . HIS   A 144 ? 0.33099 0.22343 0.28209 -0.00956 0.00315  -0.04571 147 HIS   A ND1  
2255 C  CD2  . HIS   A 144 ? 0.31121 0.21670 0.24381 0.00017  0.07954  -0.00384 147 HIS   A CD2  
2256 C  CE1  . HIS   A 144 ? 0.34860 0.21556 0.26958 -0.00983 0.03715  -0.02346 147 HIS   A CE1  
2257 N  NE2  . HIS   A 144 ? 0.37570 0.22619 0.26656 -0.00644 0.07786  -0.03559 147 HIS   A NE2  
2265 N  N    . SER   A 145 ? 0.18142 0.19526 0.14861 -0.01062 0.02756  0.00190  148 SER   A N    
2266 C  CA   . SER   A 145 ? 0.17788 0.21448 0.14757 -0.01270 0.02216  -0.00415 148 SER   A CA   
2267 C  C    . SER   A 145 ? 0.17826 0.24539 0.14607 -0.02618 0.01794  -0.00364 148 SER   A C    
2268 O  O    . SER   A 145 ? 0.18111 0.20944 0.15001 -0.01655 0.02679  -0.01065 148 SER   A O    
2269 C  CB   . SER   A 145 ? 0.20139 0.27130 0.17491 -0.02716 0.00279  0.03269  148 SER   A CB   
2270 O  OG   . SER   A 145 ? 0.21234 0.28238 0.19625 -0.01599 0.00272  0.05934  148 SER   A OG   
2276 N  N    . ILE   A 146 ? 0.17648 0.25888 0.14754 -0.04265 0.03192  -0.03557 149 ILE   A N    
2277 C  CA   . ILE   A 146 ? 0.19884 0.26799 0.17343 -0.03530 0.03634  -0.08257 149 ILE   A CA   
2278 C  C    . ILE   A 146 ? 0.18146 0.33247 0.18265 -0.05565 0.04529  -0.08283 149 ILE   A C    
2279 O  O    . ILE   A 146 ? 0.19271 0.45570 0.17884 -0.07469 0.04632  -0.11433 149 ILE   A O    
2280 C  CB   . ILE   A 146 ? 0.19134 0.26488 0.20059 -0.04883 0.04703  -0.08671 149 ILE   A CB   
2281 C  CG1  . ILE   A 146 ? 0.19843 0.23654 0.18119 -0.03594 0.04025  -0.05707 149 ILE   A CG1  
2282 C  CG2  . ILE   A 146 ? 0.22847 0.26953 0.24658 -0.06497 0.04444  -0.11831 149 ILE   A CG2  
2283 C  CD1  . ILE   A 146 ? 0.20636 0.22906 0.18079 -0.02335 0.04326  -0.03957 149 ILE   A CD1  
2295 N  N    . GLY   A 147 ? 0.17979 0.29120 0.16710 -0.04010 0.03706  -0.04183 150 GLY   A N    
2296 C  CA   . GLY   A 147 ? 0.19546 0.26417 0.15438 -0.03633 0.02489  -0.01169 150 GLY   A CA   
2297 C  C    . GLY   A 147 ? 0.18827 0.23006 0.15339 -0.02194 0.03151  -0.01528 150 GLY   A C    
2298 O  O    . GLY   A 147 ? 0.21234 0.27438 0.17209 -0.04317 0.04784  -0.04699 150 GLY   A O    
2302 N  N    . PHE   A 148 ? 0.18874 0.24700 0.14702 -0.02953 0.01687  -0.02697 151 PHE   A N    
2303 C  CA   . PHE   A 148 ? 0.20891 0.25646 0.13291 -0.02721 0.01126  -0.01673 151 PHE   A CA   
2304 C  C    . PHE   A 148 ? 0.22980 0.25798 0.14772 -0.04109 0.01670  0.01382  151 PHE   A C    
2305 O  O    . PHE   A 148 ? 0.26578 0.33180 0.13896 -0.07257 0.02166  0.02665  151 PHE   A O    
2306 C  CB   . PHE   A 148 ? 0.25128 0.23551 0.15727 -0.00471 0.01122  -0.01808 151 PHE   A CB   
2307 C  CG   . PHE   A 148 ? 0.23079 0.23927 0.18001 0.01623  -0.01574 -0.03281 151 PHE   A CG   
2308 C  CD1  . PHE   A 148 ? 0.30376 0.27373 0.25497 0.02392  -0.02879 -0.03736 151 PHE   A CD1  
2309 C  CD2  . PHE   A 148 ? 0.28566 0.23616 0.14679 0.03663  0.00195  -0.00788 151 PHE   A CD2  
2310 C  CE1  . PHE   A 148 ? 0.33537 0.28575 0.24879 0.07588  -0.07086 -0.04080 151 PHE   A CE1  
2311 C  CE2  . PHE   A 148 ? 0.35104 0.24134 0.16749 0.10097  -0.04079 -0.03745 151 PHE   A CE2  
2312 C  CZ   . PHE   A 148 ? 0.35287 0.26724 0.19466 0.10146  -0.07460 -0.04252 151 PHE   A CZ   
2322 N  N    . SER   A 149 ? 0.22409 0.24335 0.13914 -0.02066 -0.00190 0.03828  152 SER   A N    
2323 C  CA   . SER   A 149 ? 0.22628 0.25490 0.15945 -0.01534 -0.02065 0.04938  152 SER   A CA   
2324 C  C    . SER   A 149 ? 0.21152 0.25467 0.14926 -0.02904 -0.02142 0.03582  152 SER   A C    
2325 O  O    . SER   A 149 ? 0.22286 0.24505 0.15689 -0.02009 0.00467  0.03281  152 SER   A O    
2326 C  CB   . SER   A 149 ? 0.29292 0.30384 0.20920 0.04686  -0.05314 0.07176  152 SER   A CB   
2327 O  OG   . SER   A 149 ? 0.38520 0.36584 0.26402 0.06400  -0.05107 0.05487  152 SER   A OG   
2333 N  N    . PHE   A 150 ? 0.22797 0.25594 0.15976 -0.02782 0.00189  0.02110  153 PHE   A N    
2334 C  CA   . PHE   A 150 ? 0.22620 0.26498 0.16017 -0.01862 0.00853  0.01635  153 PHE   A CA   
2335 C  C    . PHE   A 150 ? 0.21797 0.29757 0.17130 -0.01157 -0.00586 0.02112  153 PHE   A C    
2336 O  O    . PHE   A 150 ? 0.24159 0.32897 0.17102 -0.00981 -0.01814 0.03962  153 PHE   A O    
2337 C  CB   . PHE   A 150 ? 0.24520 0.25897 0.16037 0.00280  0.00599  -0.00920 153 PHE   A CB   
2338 C  CG   . PHE   A 150 ? 0.22842 0.26919 0.15242 -0.00118 -0.00185 0.00217  153 PHE   A CG   
2339 C  CD1  . PHE   A 150 ? 0.23668 0.29046 0.15402 0.02187  0.00471  0.00444  153 PHE   A CD1  
2340 C  CD2  . PHE   A 150 ? 0.24425 0.25924 0.15473 0.01495  -0.01455 0.02051  153 PHE   A CD2  
2341 C  CE1  . PHE   A 150 ? 0.24676 0.29749 0.15782 0.04054  0.00850  -0.00872 153 PHE   A CE1  
2342 C  CE2  . PHE   A 150 ? 0.25373 0.28604 0.15701 0.01052  -0.00085 0.01100  153 PHE   A CE2  
2343 C  CZ   . PHE   A 150 ? 0.24834 0.29568 0.15662 0.02581  0.00321  -0.00435 153 PHE   A CZ   
2353 N  N    . SER   A 151 ? 0.20753 0.28914 0.18079 -0.01748 -0.01238 0.03242  154 SER   A N    
2354 C  CA   . SER   A 151 ? 0.22624 0.31853 0.19200 0.00015  -0.01457 0.04097  154 SER   A CA   
2355 C  C    . SER   A 151 ? 0.27887 0.34154 0.19862 -0.00508 -0.04122 0.01291  154 SER   A C    
2356 O  O    . SER   A 151 ? 0.35752 0.39081 0.22689 0.06910  -0.09922 -0.02297 154 SER   A O    
2357 C  CB   . SER   A 151 ? 0.27535 0.34055 0.24940 -0.00017 -0.01516 0.06352  154 SER   A CB   
2358 O  OG   . SER   A 151 ? 0.25728 0.31839 0.29398 -0.01422 -0.02513 0.01717  154 SER   A OG   
2364 N  N    . SER   A 152 ? 0.25712 0.35443 0.17453 -0.00359 -0.02567 0.00216  155 SER   A N    
2365 C  CA   . SER   A 152 ? 0.32997 0.41884 0.19990 0.04571  -0.02143 -0.01089 155 SER   A CA   
2366 C  C    . SER   A 152 ? 0.35075 0.49314 0.21235 0.06465  0.05789  0.04072  155 SER   A C    
2367 O  O    . SER   A 152 ? 0.38738 0.52767 0.19033 0.06835  0.04383  -0.00327 155 SER   A O    
2368 C  CB   . SER   A 152 ? 0.37447 0.43239 0.24456 0.08245  -0.02441 -0.01749 155 SER   A CB   
2369 O  OG   . SER   A 152 ? 0.37209 0.46342 0.27950 0.11565  -0.01545 0.01012  155 SER   A OG   
2375 N  N    . ASP   A 153 ? 0.36225 0.52030 0.27458 0.03204  0.11852  0.12963  156 ASP   A N    
2376 C  CA   . ASP   A 153 ? 0.48580 0.61122 0.45919 0.02310  0.07630  0.12215  156 ASP   A CA   
2377 C  C    . ASP   A 153 ? 0.45069 0.55857 0.38923 0.00530  0.00591  0.13105  156 ASP   A C    
2378 O  O    . ASP   A 153 ? 0.47296 0.58410 0.39124 -0.01669 0.00386  0.13726  156 ASP   A O    
2379 C  CB   . ASP   A 153 ? 0.70901 0.78491 0.76671 0.01540  0.05845  0.09447  156 ASP   A CB   
2380 C  CG   . ASP   A 153 ? 0.90935 0.93794 1.01128 0.01056  0.03581  0.05927  156 ASP   A CG   
2381 O  OD1  . ASP   A 153 ? 0.95148 0.99257 1.09050 0.00938  0.02611  0.04760  156 ASP   A OD1  
2382 O  OD2  . ASP   A 153 ? 0.94650 0.98472 1.09250 0.00771  0.02851  0.04250  156 ASP   A OD2  
2383 O  OXT  . ASP   A 153 ? 0.45080 0.50730 0.35506 0.03078  -0.05687 0.12223  156 ASP   A OXT  
2388 N  N    . ASN   B 4   ? 0.59081 0.39555 0.41612 0.01690  0.01057  0.01193  7   ASN   B N    
2389 C  CA   . ASN   B 4   ? 0.48944 0.37471 0.39553 -0.00375 0.02241  -0.00242 7   ASN   B CA   
2390 C  C    . ASN   B 4   ? 0.42817 0.27688 0.30790 0.00181  0.05085  -0.02250 7   ASN   B C    
2391 O  O    . ASN   B 4   ? 0.46655 0.31240 0.28947 -0.01841 0.04930  -0.04526 7   ASN   B O    
2392 C  CB   . ASN   B 4   ? 0.52751 0.42088 0.43635 0.03058  0.03514  -0.02157 7   ASN   B CB   
2393 C  CG   . ASN   B 4   ? 0.47921 0.44804 0.47094 -0.00765 0.04498  -0.00015 7   ASN   B CG   
2394 O  OD1  . ASN   B 4   ? 0.53935 0.52397 0.50597 0.04097  0.04600  0.02801  7   ASN   B OD1  
2395 N  ND2  . ASN   B 4   ? 0.50315 0.45219 0.47044 -0.01116 0.02473  -0.00374 7   ASN   B ND2  
2402 N  N    . LEU   B 5   ? 0.33796 0.24490 0.26371 -0.01883 0.08317  0.01566  8   LEU   B N    
2403 C  CA   . LEU   B 5   ? 0.24314 0.24657 0.19353 -0.02797 0.06296  -0.00317 8   LEU   B CA   
2404 C  C    . LEU   B 5   ? 0.22951 0.25229 0.18508 -0.01288 0.05902  -0.01590 8   LEU   B C    
2405 O  O    . LEU   B 5   ? 0.23494 0.29359 0.21635 0.01445  0.06688  0.03600  8   LEU   B O    
2406 C  CB   . LEU   B 5   ? 0.21039 0.29796 0.18097 -0.04299 0.03774  0.01658  8   LEU   B CB   
2407 C  CG   . LEU   B 5   ? 0.23129 0.35193 0.18439 -0.02948 0.03628  0.07233  8   LEU   B CG   
2408 C  CD1  . LEU   B 5   ? 0.28316 0.38814 0.19008 -0.05705 0.03166  0.06563  8   LEU   B CD1  
2409 C  CD2  . LEU   B 5   ? 0.23062 0.38207 0.22200 -0.03453 0.04308  0.08255  8   LEU   B CD2  
2421 N  N    . GLN   B 6   ? 0.18704 0.21802 0.16637 -0.01724 0.03368  -0.01501 9   GLN   B N    
2422 C  CA   . GLN   B 6   ? 0.19004 0.21904 0.12668 -0.01891 0.02174  -0.00523 9   GLN   B CA   
2423 C  C    . GLN   B 6   ? 0.18919 0.20431 0.12038 -0.02305 0.01313  -0.01140 9   GLN   B C    
2424 O  O    . GLN   B 6   ? 0.18419 0.23126 0.12645 -0.03006 0.02743  -0.01720 9   GLN   B O    
2425 C  CB   . GLN   B 6   ? 0.21930 0.21366 0.12049 -0.02435 0.01750  -0.02532 9   GLN   B CB   
2426 C  CG   . GLN   B 6   ? 0.23938 0.22478 0.13469 -0.01067 0.00471  -0.01812 9   GLN   B CG   
2427 C  CD   . GLN   B 6   ? 0.24119 0.24376 0.14005 -0.03608 0.01230  -0.03221 9   GLN   B CD   
2428 O  OE1  . GLN   B 6   ? 0.23889 0.26398 0.17380 -0.02711 0.02317  -0.00916 9   GLN   B OE1  
2429 N  NE2  . GLN   B 6   ? 0.25062 0.28689 0.13662 -0.05326 -0.00529 -0.01922 9   GLN   B NE2  
2438 N  N    . ASN   B 7   ? 0.16940 0.22239 0.12667 -0.02497 0.02281  -0.00131 10  ASN   B N    
2439 C  CA   . ASN   B 7   ? 0.17238 0.22692 0.13710 -0.02325 0.01473  -0.02048 10  ASN   B CA   
2440 C  C    . ASN   B 7   ? 0.19886 0.23836 0.12180 -0.03241 0.03053  -0.01674 10  ASN   B C    
2441 O  O    . ASN   B 7   ? 0.22858 0.26417 0.13705 -0.00575 0.03538  -0.03582 10  ASN   B O    
2442 C  CB   . ASN   B 7   ? 0.19428 0.23542 0.15682 -0.04028 0.02761  -0.01165 10  ASN   B CB   
2443 C  CG   . ASN   B 7   ? 0.19237 0.22683 0.14719 -0.00897 0.02795  -0.01666 10  ASN   B CG   
2444 O  OD1  . ASN   B 7   ? 0.19997 0.21093 0.14256 -0.01750 0.03483  -0.01318 10  ASN   B OD1  
2445 N  ND2  . ASN   B 7   ? 0.21442 0.25948 0.15414 -0.04542 0.03733  -0.00636 10  ASN   B ND2  
2452 N  N    . ILE   B 8   ? 0.18292 0.22597 0.12402 -0.02809 0.01206  -0.01684 11  ILE   B N    
2453 C  CA   . ILE   B 8   ? 0.18001 0.26860 0.11137 -0.05129 0.02386  -0.00385 11  ILE   B CA   
2454 C  C    . ILE   B 8   ? 0.18951 0.27677 0.11593 -0.06715 0.02394  -0.00445 11  ILE   B C    
2455 O  O    . ILE   B 8   ? 0.19158 0.28306 0.13197 -0.05698 0.02736  -0.01459 11  ILE   B O    
2456 C  CB   . ILE   B 8   ? 0.23261 0.28011 0.13612 -0.05207 0.01644  0.00528  11  ILE   B CB   
2457 C  CG1  . ILE   B 8   ? 0.22323 0.24702 0.17133 -0.03379 0.02008  -0.00746 11  ILE   B CG1  
2458 C  CG2  . ILE   B 8   ? 0.31869 0.28805 0.14920 -0.07867 -0.00561 0.03038  11  ILE   B CG2  
2459 C  CD1  . ILE   B 8   ? 0.21064 0.24859 0.22726 -0.02412 0.01902  0.00556  11  ILE   B CD1  
2471 N  N    . ILE   B 9   ? 0.18543 0.28199 0.12593 -0.06396 0.02824  -0.02999 12  ILE   B N    
2472 C  CA   . ILE   B 9   ? 0.20348 0.30288 0.13477 -0.08046 0.02390  -0.02967 12  ILE   B CA   
2473 C  C    . ILE   B 9   ? 0.19872 0.30481 0.13187 -0.07850 0.02271  -0.02699 12  ILE   B C    
2474 O  O    . ILE   B 9   ? 0.19396 0.31768 0.11986 -0.06841 -0.00160 -0.01560 12  ILE   B O    
2475 C  CB   . ILE   B 9   ? 0.24906 0.29672 0.15103 -0.08080 0.03976  -0.01374 12  ILE   B CB   
2476 C  CG1  . ILE   B 9   ? 0.24617 0.27840 0.15793 -0.04747 0.02827  -0.02572 12  ILE   B CG1  
2477 C  CG2  . ILE   B 9   ? 0.26458 0.28655 0.15102 -0.07069 0.04138  -0.02836 12  ILE   B CG2  
2478 C  CD1  . ILE   B 9   ? 0.33165 0.26604 0.19309 -0.03354 0.05083  -0.02758 12  ILE   B CD1  
2490 N  N    . TYR   B 10  ? 0.18444 0.31740 0.14104 -0.06587 0.01506  -0.03220 13  TYR   B N    
2491 C  CA   . TYR   B 10  ? 0.17616 0.30626 0.14473 -0.04027 0.01085  -0.02251 13  TYR   B CA   
2492 C  C    . TYR   B 10  ? 0.18185 0.30821 0.14550 -0.05345 0.00369  -0.01566 13  TYR   B C    
2493 O  O    . TYR   B 10  ? 0.20819 0.33153 0.15491 -0.06706 0.01699  -0.03328 13  TYR   B O    
2494 C  CB   . TYR   B 10  ? 0.19235 0.31629 0.17054 -0.02970 0.01906  -0.03316 13  TYR   B CB   
2495 C  CG   . TYR   B 10  ? 0.20001 0.32302 0.20084 0.00775  0.01540  -0.05902 13  TYR   B CG   
2496 C  CD1  . TYR   B 10  ? 0.25460 0.35382 0.22817 -0.00010 0.01252  -0.07375 13  TYR   B CD1  
2497 C  CD2  . TYR   B 10  ? 0.21345 0.33266 0.24352 -0.00765 0.01931  -0.05476 13  TYR   B CD2  
2498 C  CE1  . TYR   B 10  ? 0.30506 0.36109 0.27585 -0.02534 0.01873  -0.08851 13  TYR   B CE1  
2499 C  CE2  . TYR   B 10  ? 0.24918 0.33551 0.28554 -0.01726 0.02188  -0.05555 13  TYR   B CE2  
2500 C  CZ   . TYR   B 10  ? 0.27598 0.35859 0.30011 -0.01275 0.02100  -0.10149 13  TYR   B CZ   
2501 O  OH   . TYR   B 10  ? 0.32820 0.37228 0.33168 0.00544  0.00423  -0.11876 13  TYR   B OH   
2511 N  N    . ASN   B 11  ? 0.18216 0.31451 0.12384 -0.04960 -0.00363 -0.02076 14  ASN   B N    
2512 C  CA   . ASN   B 11  ? 0.18669 0.34817 0.14400 -0.05349 -0.01636 -0.03204 14  ASN   B CA   
2513 C  C    . ASN   B 11  ? 0.21367 0.33717 0.14577 -0.03533 -0.00288 -0.03180 14  ASN   B C    
2514 O  O    . ASN   B 11  ? 0.23566 0.35560 0.17250 -0.05818 -0.01920 -0.04286 14  ASN   B O    
2515 C  CB   . ASN   B 11  ? 0.20795 0.36168 0.17025 -0.01894 -0.02159 -0.03441 14  ASN   B CB   
2516 C  CG   . ASN   B 11  ? 0.20906 0.39831 0.21984 0.01137  -0.03122 -0.00976 14  ASN   B CG   
2517 O  OD1  . ASN   B 11  ? 0.21850 0.38342 0.21972 -0.02057 -0.03633 -0.01375 14  ASN   B OD1  
2518 N  ND2  . ASN   B 11  ? 0.24794 0.43771 0.27757 0.01662  -0.02797 0.04862  14  ASN   B ND2  
2525 N  N    . PRO   B 12  ? 0.21053 0.32790 0.15445 -0.01502 -0.01733 -0.03281 15  PRO   B N    
2526 C  CA   . PRO   B 12  ? 0.24759 0.33361 0.15653 -0.01834 -0.01659 -0.01915 15  PRO   B CA   
2527 C  C    . PRO   B 12  ? 0.24741 0.32241 0.15096 -0.01975 -0.00715 -0.01561 15  PRO   B C    
2528 O  O    . PRO   B 12  ? 0.26620 0.31487 0.15806 -0.02216 -0.00483 -0.03037 15  PRO   B O    
2529 C  CB   . PRO   B 12  ? 0.26061 0.34365 0.15034 -0.00131 -0.01462 -0.02976 15  PRO   B CB   
2530 C  CG   . PRO   B 12  ? 0.21882 0.33087 0.15692 -0.01121 -0.01598 -0.03279 15  PRO   B CG   
2531 C  CD   . PRO   B 12  ? 0.20326 0.31929 0.15392 -0.01660 -0.01956 -0.02188 15  PRO   B CD   
2539 N  N    . VAL   B 13  ? 0.24354 0.30923 0.17727 -0.02540 -0.01431 -0.01988 16  VAL   B N    
2540 C  CA   . VAL   B 13  ? 0.23563 0.31670 0.17792 -0.03729 -0.01777 -0.00659 16  VAL   B CA   
2541 C  C    . VAL   B 13  ? 0.23814 0.30230 0.15521 -0.04187 -0.02074 -0.01247 16  VAL   B C    
2542 O  O    . VAL   B 13  ? 0.24533 0.31091 0.14556 -0.03461 -0.03227 -0.00186 16  VAL   B O    
2543 C  CB   . VAL   B 13  ? 0.24240 0.34243 0.21810 -0.05925 -0.02526 -0.02595 16  VAL   B CB   
2544 C  CG1  . VAL   B 13  ? 0.26788 0.35086 0.21104 -0.07100 -0.01577 -0.04052 16  VAL   B CG1  
2545 C  CG2  . VAL   B 13  ? 0.23985 0.38572 0.25937 -0.04327 -0.01680 -0.03829 16  VAL   B CG2  
2555 N  N    . ILE   B 14  ? 0.23025 0.26746 0.16038 -0.02512 -0.02233 -0.01718 17  ILE   B N    
2556 C  CA   . ILE   B 14  ? 0.24892 0.24482 0.15280 -0.04772 -0.02699 -0.01831 17  ILE   B CA   
2557 C  C    . ILE   B 14  ? 0.26751 0.25009 0.16125 -0.02735 -0.05462 -0.02421 17  ILE   B C    
2558 O  O    . ILE   B 14  ? 0.29538 0.28014 0.16716 -0.03899 -0.07249 -0.03379 17  ILE   B O    
2559 C  CB   . ILE   B 14  ? 0.24869 0.28476 0.15095 -0.04497 -0.03577 -0.02287 17  ILE   B CB   
2560 C  CG1  . ILE   B 14  ? 0.23441 0.28094 0.15753 -0.03511 -0.02517 0.00935  17  ILE   B CG1  
2561 C  CG2  . ILE   B 14  ? 0.28161 0.32755 0.16005 -0.04468 -0.02523 -0.02247 17  ILE   B CG2  
2562 C  CD1  . ILE   B 14  ? 0.24376 0.24543 0.18114 -0.02452 -0.01902 -0.01019 17  ILE   B CD1  
2574 N  N    . PRO   B 15  ? 0.30336 0.24491 0.21439 -0.02485 -0.10189 -0.03706 18  PRO   B N    
2575 C  CA   . PRO   B 15  ? 0.28761 0.25718 0.22175 -0.02205 -0.10347 0.00230  18  PRO   B CA   
2576 C  C    . PRO   B 15  ? 0.26379 0.26535 0.19288 -0.07228 -0.06902 0.02430  18  PRO   B C    
2577 O  O    . PRO   B 15  ? 0.29083 0.25619 0.21588 -0.09495 -0.07131 0.02225  18  PRO   B O    
2578 C  CB   . PRO   B 15  ? 0.30942 0.25668 0.26655 -0.00322 -0.11867 -0.02087 18  PRO   B CB   
2579 C  CG   . PRO   B 15  ? 0.34653 0.27860 0.28729 0.00382  -0.11878 -0.02213 18  PRO   B CG   
2580 C  CD   . PRO   B 15  ? 0.33725 0.28004 0.27610 -0.00377 -0.11539 -0.03243 18  PRO   B CD   
2588 N  N    . PHE   B 16  ? 0.25426 0.26055 0.17194 -0.05110 -0.06586 -0.00164 19  PHE   B N    
2589 C  CA   . PHE   B 16  ? 0.26147 0.26193 0.15422 -0.04183 -0.06599 0.01204  19  PHE   B CA   
2590 C  C    . PHE   B 16  ? 0.26035 0.23500 0.16135 -0.06828 -0.04517 0.02125  19  PHE   B C    
2591 O  O    . PHE   B 16  ? 0.23326 0.24187 0.15821 -0.05991 -0.04686 0.03934  19  PHE   B O    
2592 C  CB   . PHE   B 16  ? 0.26957 0.26891 0.15658 -0.02780 -0.04675 0.02202  19  PHE   B CB   
2593 C  CG   . PHE   B 16  ? 0.27776 0.25181 0.17278 -0.01926 -0.04912 0.02442  19  PHE   B CG   
2594 C  CD1  . PHE   B 16  ? 0.29349 0.26746 0.16913 -0.02518 -0.03450 0.01143  19  PHE   B CD1  
2595 C  CD2  . PHE   B 16  ? 0.27356 0.24356 0.18369 -0.01286 -0.07671 -0.00019 19  PHE   B CD2  
2596 C  CE1  . PHE   B 16  ? 0.33401 0.27177 0.17903 0.01064  -0.03784 0.00127  19  PHE   B CE1  
2597 C  CE2  . PHE   B 16  ? 0.29978 0.29951 0.18697 -0.00735 -0.08173 -0.01227 19  PHE   B CE2  
2598 C  CZ   . PHE   B 16  ? 0.31453 0.28686 0.18641 0.00129  -0.05133 -0.02560 19  PHE   B CZ   
2601 N  N    . VAL   B 17  ? 0.24222 0.23012 0.16623 -0.07779 -0.04993 0.00183  20  VAL   B N    
2602 C  CA   . VAL   B 17  ? 0.25389 0.22038 0.16958 -0.07782 -0.04824 -0.00483 20  VAL   B CA   
2603 C  C    . VAL   B 17  ? 0.26169 0.23090 0.17866 -0.07508 -0.04990 0.00649  20  VAL   B C    
2604 O  O    . VAL   B 17  ? 0.29673 0.27608 0.20981 -0.11513 -0.01457 0.00357  20  VAL   B O    
2605 C  CB   . VAL   B 17  ? 0.31854 0.22484 0.20382 -0.05659 -0.06550 0.01427  20  VAL   B CB   
2606 C  CG1  . VAL   B 17  ? 0.36777 0.20780 0.22099 -0.02485 -0.09625 0.01499  20  VAL   B CG1  
2607 C  CG2  . VAL   B 17  ? 0.35566 0.24743 0.23769 -0.01685 -0.03784 -0.00536 20  VAL   B CG2  
2617 N  N    . GLY   B 18  ? 0.22537 0.25135 0.18924 -0.05023 -0.04317 -0.00868 21  GLY   B N    
2618 C  CA   . GLY   B 18  ? 0.25092 0.28911 0.21680 -0.00528 -0.03812 -0.05052 21  GLY   B CA   
2619 C  C    . GLY   B 18  ? 0.23319 0.23179 0.20737 -0.03195 -0.03829 -0.02914 21  GLY   B C    
2620 O  O    . GLY   B 18  ? 0.21802 0.23209 0.20077 -0.05248 -0.04209 -0.00016 21  GLY   B O    
2624 N  N    . THR   B 19  ? 0.24204 0.25587 0.21461 -0.05813 -0.01434 -0.05609 22  THR   B N    
2625 C  CA   . THR   B 19  ? 0.25674 0.21870 0.21478 -0.04565 -0.01737 -0.05201 22  THR   B CA   
2626 C  C    . THR   B 19  ? 0.28298 0.20649 0.24636 -0.00942 -0.06910 -0.05450 22  THR   B C    
2627 O  O    . THR   B 19  ? 0.28162 0.27029 0.33501 0.00807  -0.08672 -0.08088 22  THR   B O    
2628 C  CB   . THR   B 19  ? 0.34823 0.26341 0.21297 -0.05214 0.02597  -0.04699 22  THR   B CB   
2629 O  OG1  . THR   B 19  ? 0.38663 0.28376 0.23354 -0.08378 0.04712  -0.04382 22  THR   B OG1  
2630 C  CG2  . THR   B 19  ? 0.37354 0.26416 0.20957 -0.03418 0.05599  -0.05632 22  THR   B CG2  
2638 N  N    . ILE   B 20  ? 0.26734 0.16429 0.20714 -0.01855 -0.06379 -0.02629 23  ILE   B N    
2639 C  CA   . ILE   B 20  ? 0.30264 0.18315 0.20643 -0.00405 -0.07972 -0.03003 23  ILE   B CA   
2640 C  C    . ILE   B 20  ? 0.31063 0.18336 0.21159 0.00931  -0.08054 -0.04719 23  ILE   B C    
2641 O  O    . ILE   B 20  ? 0.35193 0.19695 0.20560 0.00170  -0.06296 -0.03414 23  ILE   B O    
2642 C  CB   . ILE   B 20  ? 0.30986 0.16306 0.18787 -0.00671 -0.08587 -0.01480 23  ILE   B CB   
2643 C  CG1  . ILE   B 20  ? 0.30979 0.18289 0.18883 -0.02042 -0.07977 -0.02566 23  ILE   B CG1  
2644 C  CG2  . ILE   B 20  ? 0.32992 0.17766 0.17425 -0.00874 -0.06979 -0.01226 23  ILE   B CG2  
2645 C  CD1  . ILE   B 20  ? 0.31749 0.20997 0.21676 -0.03980 -0.07068 -0.00955 23  ILE   B CD1  
2657 N  N    . PRO   B 21  ? 0.27954 0.21489 0.24234 0.00759  -0.08034 -0.05854 24  PRO   B N    
2658 C  CA   . PRO   B 21  ? 0.27862 0.25340 0.23411 -0.03377 -0.04971 -0.06262 24  PRO   B CA   
2659 C  C    . PRO   B 21  ? 0.28801 0.20894 0.21890 -0.00728 -0.02716 -0.04181 24  PRO   B C    
2660 O  O    . PRO   B 21  ? 0.27093 0.22707 0.22076 -0.02693 -0.01822 -0.03219 24  PRO   B O    
2661 C  CB   . PRO   B 21  ? 0.24716 0.33189 0.20797 0.01284  -0.03417 -0.03250 24  PRO   B CB   
2662 C  CG   . PRO   B 21  ? 0.28881 0.30959 0.24338 0.02039  -0.01946 -0.02988 24  PRO   B CG   
2663 C  CD   . PRO   B 21  ? 0.25536 0.22080 0.24752 0.03367  -0.09373 -0.03950 24  PRO   B CD   
2671 N  N    . ASP   B 22  ? 0.25520 0.18637 0.17496 -0.01272 -0.03501 -0.00548 25  ASP   B N    
2672 C  CA   . ASP   B 22  ? 0.25340 0.18599 0.15944 -0.01843 -0.03695 0.00748  25  ASP   B CA   
2673 C  C    . ASP   B 22  ? 0.25715 0.18644 0.13814 -0.02147 -0.03850 0.01686  25  ASP   B C    
2674 O  O    . ASP   B 22  ? 0.25735 0.19944 0.14739 -0.01419 -0.03718 0.00082  25  ASP   B O    
2675 C  CB   . ASP   B 22  ? 0.25847 0.21211 0.14995 -0.00910 -0.01752 -0.00230 25  ASP   B CB   
2676 C  CG   . ASP   B 22  ? 0.31293 0.29826 0.17125 0.01345  -0.01024 -0.02771 25  ASP   B CG   
2677 O  OD1  . ASP   B 22  ? 0.32708 0.34974 0.15957 -0.00690 -0.03082 -0.01748 25  ASP   B OD1  
2678 O  OD2  . ASP   B 22  ? 0.37172 0.32292 0.20659 0.01874  -0.03401 -0.06716 25  ASP   B OD2  
2683 N  N    . GLN   B 23  ? 0.25407 0.20976 0.14616 -0.03064 -0.02395 0.01428  26  GLN   B N    
2684 C  CA   A GLN   B 23  ? 0.24296 0.19744 0.14027 -0.01398 -0.03522 0.01260  26  GLN   B CA   
2685 C  CA   B GLN   B 23  ? 0.26472 0.21490 0.15018 -0.02079 -0.03690 0.01672  26  GLN   B CA   
2686 C  C    . GLN   B 23  ? 0.25471 0.16330 0.14446 -0.02165 -0.02862 0.00560  26  GLN   B C    
2687 O  O    . GLN   B 23  ? 0.26431 0.18770 0.17189 -0.00360 -0.00399 0.00083  26  GLN   B O    
2688 C  CB   A GLN   B 23  ? 0.24147 0.23206 0.15168 0.00611  -0.03220 0.01029  26  GLN   B CB   
2689 C  CB   B GLN   B 23  ? 0.30704 0.28926 0.18046 -0.01052 -0.04023 0.02307  26  GLN   B CB   
2690 C  CG   A GLN   B 23  ? 0.29627 0.22791 0.19647 0.00369  -0.03061 0.03905  26  GLN   B CG   
2691 C  CG   B GLN   B 23  ? 0.36365 0.33501 0.24523 -0.01235 -0.04659 0.03949  26  GLN   B CG   
2692 C  CD   A GLN   B 23  ? 0.30786 0.19827 0.19901 0.01097  -0.04807 0.04169  26  GLN   B CD   
2693 C  CD   B GLN   B 23  ? 0.40913 0.37132 0.28996 -0.01939 -0.05237 0.04916  26  GLN   B CD   
2694 O  OE1  A GLN   B 23  ? 0.33851 0.21849 0.23035 -0.01131 -0.02292 0.05106  26  GLN   B OE1  
2695 O  OE1  B GLN   B 23  ? 0.41676 0.38557 0.32017 0.01948  -0.06795 0.05986  26  GLN   B OE1  
2696 N  NE2  A GLN   B 23  ? 0.29779 0.21762 0.19913 -0.00746 -0.05536 0.00888  26  GLN   B NE2  
2697 N  NE2  B GLN   B 23  ? 0.44021 0.38876 0.30378 -0.02200 -0.03466 0.03927  26  GLN   B NE2  
2712 N  N    . LEU   B 24  ? 0.23395 0.16371 0.15257 -0.01924 -0.01344 0.00813  27  LEU   B N    
2713 C  CA   . LEU   B 24  ? 0.24045 0.14392 0.15531 -0.03492 -0.02376 0.00311  27  LEU   B CA   
2714 C  C    . LEU   B 24  ? 0.25689 0.16913 0.17474 -0.00978 -0.02449 0.00388  27  LEU   B C    
2715 O  O    . LEU   B 24  ? 0.26613 0.22261 0.17753 -0.01980 -0.02679 -0.01282 27  LEU   B O    
2716 C  CB   . LEU   B 24  ? 0.27075 0.15601 0.16555 -0.04041 -0.01632 0.02412  27  LEU   B CB   
2717 C  CG   . LEU   B 24  ? 0.28079 0.15572 0.16540 -0.01809 -0.03880 0.01902  27  LEU   B CG   
2718 C  CD1  . LEU   B 24  ? 0.30626 0.16100 0.15704 -0.01156 -0.01098 0.00039  27  LEU   B CD1  
2719 C  CD2  . LEU   B 24  ? 0.28845 0.18655 0.17949 -0.03843 -0.03965 0.00087  27  LEU   B CD2  
2731 N  N    . ASP   B 25  ? 0.25579 0.14710 0.18660 -0.01916 -0.04269 -0.01022 28  ASP   B N    
2732 C  CA   . ASP   B 25  ? 0.25501 0.14986 0.19677 -0.00536 -0.05798 -0.00405 28  ASP   B CA   
2733 C  C    . ASP   B 25  ? 0.25821 0.14138 0.20444 0.00050  -0.08571 -0.00946 28  ASP   B C    
2734 O  O    . ASP   B 25  ? 0.22623 0.14779 0.18703 0.00485  -0.06519 -0.01319 28  ASP   B O    
2735 C  CB   . ASP   B 25  ? 0.29558 0.20083 0.19468 -0.01005 -0.06004 0.00506  28  ASP   B CB   
2736 C  CG   . ASP   B 25  ? 0.37909 0.25043 0.22030 0.01270  -0.07135 -0.00961 28  ASP   B CG   
2737 O  OD1  . ASP   B 25  ? 0.45394 0.26800 0.25541 0.03295  -0.06742 0.05131  28  ASP   B OD1  
2738 O  OD2  . ASP   B 25  ? 0.40803 0.27787 0.22480 -0.01262 -0.06320 0.01556  28  ASP   B OD2  
2743 N  N    . PRO   B 26  ? 0.24163 0.16712 0.22983 -0.00096 -0.09421 0.01544  29  PRO   B N    
2744 C  CA   . PRO   B 26  ? 0.21594 0.17242 0.23001 -0.00146 -0.07514 0.00194  29  PRO   B CA   
2745 C  C    . PRO   B 26  ? 0.20514 0.14131 0.19472 -0.00510 -0.05347 -0.02327 29  PRO   B C    
2746 O  O    . PRO   B 26  ? 0.24313 0.15909 0.18039 -0.00097 -0.05147 -0.02340 29  PRO   B O    
2747 C  CB   . PRO   B 26  ? 0.22431 0.20577 0.28833 0.00008  -0.09639 0.01609  29  PRO   B CB   
2748 C  CG   . PRO   B 26  ? 0.25008 0.23513 0.30782 0.00286  -0.11166 0.04663  29  PRO   B CG   
2749 C  CD   . PRO   B 26  ? 0.26835 0.21998 0.28761 0.01105  -0.10283 0.05052  29  PRO   B CD   
2757 N  N    . GLY   B 27  ? 0.19285 0.13566 0.19228 -0.00673 -0.04665 -0.01223 30  GLY   B N    
2758 C  CA   . GLY   B 27  ? 0.19857 0.12855 0.18462 -0.00888 -0.04362 -0.00789 30  GLY   B CA   
2759 C  C    . GLY   B 27  ? 0.19830 0.14187 0.17758 -0.00706 -0.03808 -0.00953 30  GLY   B C    
2760 O  O    . GLY   B 27  ? 0.21137 0.14475 0.20611 0.00106  -0.04650 0.01341  30  GLY   B O    
2764 N  N    . THR   B 28  ? 0.19170 0.13867 0.15559 -0.00556 -0.03631 -0.00362 31  THR   B N    
2765 C  CA   . THR   B 28  ? 0.18147 0.14092 0.13479 -0.00706 -0.02313 -0.00496 31  THR   B CA   
2766 C  C    . THR   B 28  ? 0.18167 0.12373 0.14640 -0.00878 -0.02157 -0.01699 31  THR   B C    
2767 O  O    . THR   B 28  ? 0.17247 0.16839 0.14868 -0.00074 -0.01931 0.00965  31  THR   B O    
2768 C  CB   . THR   B 28  ? 0.20654 0.16066 0.15355 -0.01872 -0.02491 -0.00288 31  THR   B CB   
2769 O  OG1  . THR   B 28  ? 0.23440 0.18192 0.15556 -0.03256 -0.02997 0.02941  31  THR   B OG1  
2770 C  CG2  . THR   B 28  ? 0.21217 0.17415 0.16908 -0.03441 -0.02563 0.00410  31  THR   B CG2  
2778 N  N    . LEU   B 29  ? 0.16638 0.15926 0.13872 -0.00386 -0.03162 -0.00516 32  LEU   B N    
2779 C  CA   . LEU   B 29  ? 0.18031 0.17521 0.13569 -0.00899 -0.03307 -0.00169 32  LEU   B CA   
2780 C  C    . LEU   B 29  ? 0.17879 0.17746 0.11658 -0.01346 -0.02328 -0.00497 32  LEU   B C    
2781 O  O    . LEU   B 29  ? 0.17031 0.20999 0.12883 -0.02042 -0.00372 -0.02472 32  LEU   B O    
2782 C  CB   . LEU   B 29  ? 0.19909 0.17909 0.14874 0.00128  -0.03283 0.00336  32  LEU   B CB   
2783 C  CG   . LEU   B 29  ? 0.22715 0.16362 0.17348 0.00729  -0.03265 -0.00509 32  LEU   B CG   
2784 C  CD1  . LEU   B 29  ? 0.24978 0.19852 0.20662 0.03767  -0.01796 0.00220  32  LEU   B CD1  
2785 C  CD2  . LEU   B 29  ? 0.21963 0.15340 0.20226 -0.00958 -0.04063 -0.01243 32  LEU   B CD2  
2797 N  N    . ILE   B 30  ? 0.17170 0.16358 0.11424 -0.02253 -0.01067 0.00082  33  ILE   B N    
2798 C  CA   . ILE   B 30  ? 0.17077 0.16272 0.10710 -0.01844 -0.00632 0.00237  33  ILE   B CA   
2799 C  C    . ILE   B 30  ? 0.17415 0.15891 0.10142 -0.02414 -0.01558 0.01464  33  ILE   B C    
2800 O  O    . ILE   B 30  ? 0.16870 0.18499 0.12605 -0.01729 0.00344  0.02394  33  ILE   B O    
2801 C  CB   . ILE   B 30  ? 0.19932 0.17087 0.11451 -0.01555 0.00333  0.02333  33  ILE   B CB   
2802 C  CG1  . ILE   B 30  ? 0.21272 0.17215 0.13473 -0.00981 -0.00101 0.01093  33  ILE   B CG1  
2803 C  CG2  . ILE   B 30  ? 0.24654 0.17789 0.13306 -0.04225 -0.01587 0.00981  33  ILE   B CG2  
2804 C  CD1  . ILE   B 30  ? 0.28693 0.20337 0.16595 0.03303  -0.02041 0.01774  33  ILE   B CD1  
2816 N  N    . VAL   B 31  ? 0.16162 0.16642 0.11084 -0.01838 -0.00654 0.01146  34  VAL   B N    
2817 C  CA   . VAL   B 31  ? 0.15984 0.16286 0.12671 -0.01874 -0.00437 0.00528  34  VAL   B CA   
2818 C  C    . VAL   B 31  ? 0.16548 0.17764 0.12142 -0.02044 0.00653  0.01259  34  VAL   B C    
2819 O  O    . VAL   B 31  ? 0.17318 0.20216 0.11551 -0.03304 -0.00154 0.00573  34  VAL   B O    
2820 C  CB   . VAL   B 31  ? 0.17856 0.16570 0.14753 -0.00721 0.00305  0.01255  34  VAL   B CB   
2821 C  CG1  . VAL   B 31  ? 0.19337 0.17642 0.17531 0.00020  -0.00319 -0.00002 34  VAL   B CG1  
2822 C  CG2  . VAL   B 31  ? 0.19858 0.17266 0.15705 -0.03039 0.00849  -0.01301 34  VAL   B CG2  
2832 N  N    . ILE   B 32  ? 0.15542 0.19098 0.10269 -0.02161 -0.00269 0.00957  35  ILE   B N    
2833 C  CA   . ILE   B 32  ? 0.17685 0.17808 0.10147 -0.02290 -0.00950 0.00993  35  ILE   B CA   
2834 C  C    . ILE   B 32  ? 0.18040 0.18473 0.10341 -0.02888 -0.00186 0.01450  35  ILE   B C    
2835 O  O    . ILE   B 32  ? 0.17401 0.21831 0.11819 -0.01367 -0.00431 0.04169  35  ILE   B O    
2836 C  CB   . ILE   B 32  ? 0.18711 0.18156 0.10815 -0.02157 -0.00940 0.00631  35  ILE   B CB   
2837 C  CG1  . ILE   B 32  ? 0.20707 0.18040 0.12322 -0.00564 -0.02060 0.00605  35  ILE   B CG1  
2838 C  CG2  . ILE   B 32  ? 0.21165 0.19412 0.11824 -0.01842 -0.01177 0.01630  35  ILE   B CG2  
2839 C  CD1  . ILE   B 32  ? 0.24582 0.17473 0.14634 0.00889  -0.01841 -0.00416 35  ILE   B CD1  
2851 N  N    . ARG   B 33  ? 0.16576 0.20267 0.11298 -0.01707 -0.00883 0.02041  36  ARG   B N    
2852 C  CA   . ARG   B 33  ? 0.18052 0.19969 0.12642 -0.00535 -0.01458 0.02223  36  ARG   B CA   
2853 C  C    . ARG   B 33  ? 0.18371 0.22727 0.11450 0.01242  0.00148  0.03084  36  ARG   B C    
2854 O  O    . ARG   B 33  ? 0.18033 0.24939 0.10788 -0.02217 -0.01016 0.01530  36  ARG   B O    
2855 C  CB   . ARG   B 33  ? 0.19336 0.20781 0.17689 -0.00123 -0.01033 0.00288  36  ARG   B CB   
2856 C  CG   . ARG   B 33  ? 0.23755 0.24089 0.24724 0.01215  0.02325  -0.03685 36  ARG   B CG   
2857 C  CD   . ARG   B 33  ? 0.31919 0.29456 0.34300 0.01658  0.04128  -0.08349 36  ARG   B CD   
2858 N  NE   . ARG   B 33  ? 0.44488 0.38168 0.40693 0.03923  0.03389  -0.09183 36  ARG   B NE   
2859 C  CZ   . ARG   B 33  ? 0.51848 0.45838 0.46796 0.02112  -0.00629 -0.05130 36  ARG   B CZ   
2860 N  NH1  . ARG   B 33  ? 0.53317 0.48933 0.49528 0.01891  -0.00310 -0.03750 36  ARG   B NH1  
2861 N  NH2  . ARG   B 33  ? 0.56647 0.46586 0.48882 0.02675  -0.01050 -0.03432 36  ARG   B NH2  
2864 N  N    . GLY   B 34  ? 0.18110 0.23419 0.12076 0.01385  -0.01727 0.02677  37  GLY   B N    
2865 C  CA   . GLY   B 34  ? 0.20578 0.24035 0.12877 0.01273  -0.01417 0.03288  37  GLY   B CA   
2866 C  C    . GLY   B 34  ? 0.21473 0.28178 0.12249 0.05525  -0.02318 0.02236  37  GLY   B C    
2867 O  O    . GLY   B 34  ? 0.23647 0.30368 0.12232 0.07024  -0.00889 0.03024  37  GLY   B O    
2871 N  N    . HIS   B 35  ? 0.21148 0.31878 0.11328 0.05050  -0.01598 0.02117  38  HIS   B N    
2872 C  CA   . HIS   B 35  ? 0.20839 0.36678 0.11640 0.05465  -0.01038 0.04543  38  HIS   B CA   
2873 C  C    . HIS   B 35  ? 0.22313 0.38888 0.13110 0.06795  -0.01657 0.02069  38  HIS   B C    
2874 O  O    . HIS   B 35  ? 0.23157 0.39048 0.13112 0.06228  -0.03359 -0.02954 38  HIS   B O    
2875 C  CB   . HIS   B 35  ? 0.23247 0.38880 0.13548 0.06306  -0.02111 0.05005  38  HIS   B CB   
2876 C  CG   . HIS   B 35  ? 0.22938 0.47741 0.15167 0.07710  -0.03537 0.01700  38  HIS   B CG   
2877 N  ND1  . HIS   B 35  ? 0.23506 0.49992 0.14998 0.08073  -0.01810 -0.02198 38  HIS   B ND1  
2878 C  CD2  . HIS   B 35  ? 0.23501 0.52559 0.16182 0.06009  -0.03920 -0.01034 38  HIS   B CD2  
2879 C  CE1  . HIS   B 35  ? 0.26367 0.50082 0.16064 0.04565  -0.06615 -0.00315 38  HIS   B CE1  
2880 N  NE2  . HIS   B 35  ? 0.24701 0.53391 0.16232 0.08261  -0.04132 -0.00480 38  HIS   B NE2  
2888 N  N    . VAL   B 36  ? 0.23657 0.40104 0.12355 0.07619  -0.02078 0.00746  39  VAL   B N    
2889 C  CA   . VAL   B 36  ? 0.24138 0.38045 0.12750 0.07528  -0.02114 -0.00182 39  VAL   B CA   
2890 C  C    . VAL   B 36  ? 0.26481 0.36807 0.12483 0.09185  -0.04809 0.00003  39  VAL   B C    
2891 O  O    . VAL   B 36  ? 0.27391 0.38469 0.13020 0.10412  -0.04230 0.01139  39  VAL   B O    
2892 C  CB   . VAL   B 36  ? 0.25906 0.38560 0.13766 0.06444  -0.02092 0.02888  39  VAL   B CB   
2893 C  CG1  . VAL   B 36  ? 0.23485 0.40285 0.13116 0.06315  -0.01163 0.02552  39  VAL   B CG1  
2894 C  CG2  . VAL   B 36  ? 0.25438 0.39788 0.14430 0.07127  -0.01314 0.03019  39  VAL   B CG2  
2904 N  N    . PRO   B 37  ? 0.24462 0.43070 0.14909 0.10711  -0.04144 -0.01793 40  PRO   B N    
2905 C  CA   . PRO   B 37  ? 0.27392 0.42268 0.17195 0.08758  -0.03890 -0.04020 40  PRO   B CA   
2906 C  C    . PRO   B 37  ? 0.30367 0.36140 0.15520 0.06708  -0.06925 -0.02177 40  PRO   B C    
2907 O  O    . PRO   B 37  ? 0.25804 0.39563 0.13352 0.04298  -0.03559 -0.02796 40  PRO   B O    
2908 C  CB   . PRO   B 37  ? 0.24718 0.46257 0.18896 0.04575  -0.03288 -0.03010 40  PRO   B CB   
2909 C  CG   . PRO   B 37  ? 0.25989 0.45794 0.17990 0.03567  -0.04009 -0.03058 40  PRO   B CG   
2910 C  CD   . PRO   B 37  ? 0.26987 0.43017 0.16591 0.09351  -0.04944 -0.02537 40  PRO   B CD   
2918 N  N    . SER   B 38  ? 0.34855 0.35199 0.16795 0.06557  -0.08121 -0.01319 41  SER   B N    
2919 C  CA   . SER   B 38  ? 0.39576 0.32388 0.16350 0.05622  -0.11024 -0.01876 41  SER   B CA   
2920 C  C    . SER   B 38  ? 0.35282 0.30075 0.19489 0.01674  -0.08258 -0.02958 41  SER   B C    
2921 O  O    . SER   B 38  ? 0.39197 0.32240 0.20972 -0.00748 -0.05505 -0.01562 41  SER   B O    
2922 C  CB   . SER   B 38  ? 0.50075 0.32854 0.20208 0.06183  -0.10679 -0.04377 41  SER   B CB   
2923 O  OG   . SER   B 38  ? 0.47669 0.37558 0.24321 0.06053  -0.07422 -0.03843 41  SER   B OG   
2929 N  N    . ASP   B 39  ? 0.32306 0.31091 0.18504 0.00866  -0.08720 -0.03639 42  ASP   B N    
2930 C  CA   . ASP   B 39  ? 0.29908 0.30597 0.18815 0.02895  -0.07286 -0.03015 42  ASP   B CA   
2931 C  C    . ASP   B 39  ? 0.27496 0.30586 0.17633 0.03749  -0.06201 -0.01433 42  ASP   B C    
2932 O  O    . ASP   B 39  ? 0.28635 0.32688 0.21338 0.03318  -0.06588 -0.02601 42  ASP   B O    
2933 C  CB   . ASP   B 39  ? 0.28045 0.30988 0.22965 0.03132  -0.05770 -0.06366 42  ASP   B CB   
2934 C  CG   . ASP   B 39  ? 0.26790 0.30720 0.28108 0.01645  -0.05059 -0.11077 42  ASP   B CG   
2935 O  OD1  . ASP   B 39  ? 0.25430 0.34362 0.28956 0.00566  -0.04092 -0.08361 42  ASP   B OD1  
2936 O  OD2  . ASP   B 39  ? 0.28695 0.32341 0.34065 -0.00966 -0.01734 -0.10463 42  ASP   B OD2  
2941 N  N    . ALA   B 40  ? 0.25713 0.29779 0.15214 0.02343  -0.04022 -0.01049 43  ALA   B N    
2942 C  CA   . ALA   B 40  ? 0.25783 0.31049 0.12300 0.01975  -0.02157 -0.00327 43  ALA   B CA   
2943 C  C    . ALA   B 40  ? 0.23810 0.33321 0.12160 0.01515  -0.01726 0.01845  43  ALA   B C    
2944 O  O    . ALA   B 40  ? 0.25988 0.33548 0.15359 0.01613  -0.00568 0.02374  43  ALA   B O    
2945 C  CB   . ALA   B 40  ? 0.25480 0.33072 0.14461 0.02115  -0.02444 -0.00540 43  ALA   B CB   
2951 N  N    . ASP   B 41  ? 0.25125 0.33445 0.11918 0.05463  -0.02751 0.00158  44  ASP   B N    
2952 C  CA   . ASP   B 41  ? 0.31528 0.34941 0.13125 0.08070  -0.02891 -0.01901 44  ASP   B CA   
2953 C  C    . ASP   B 41  ? 0.27034 0.28617 0.13092 0.06066  -0.01020 0.00756  44  ASP   B C    
2954 O  O    . ASP   B 41  ? 0.29058 0.26128 0.12257 0.06569  0.00470  0.02340  44  ASP   B O    
2955 C  CB   . ASP   B 41  ? 0.41958 0.36436 0.17075 0.10886  -0.05732 -0.07681 44  ASP   B CB   
2956 C  CG   . ASP   B 41  ? 0.49499 0.38012 0.24857 0.10936  -0.03343 -0.04746 44  ASP   B CG   
2957 O  OD1  . ASP   B 41  ? 0.43782 0.35626 0.20172 0.10495  -0.07056 -0.02833 44  ASP   B OD1  
2958 O  OD2  . ASP   B 41  ? 0.57359 0.43330 0.35316 0.06664  0.02423  -0.04269 44  ASP   B OD2  
2963 N  N    . ARG   B 42  ? 0.25999 0.26167 0.12357 0.04195  -0.02596 0.00087  45  ARG   B N    
2964 C  CA   . ARG   B 42  ? 0.25574 0.22801 0.12724 0.03282  -0.03436 0.01880  45  ARG   B CA   
2965 C  C    . ARG   B 42  ? 0.21980 0.19775 0.12659 0.01264  -0.02606 0.00666  45  ARG   B C    
2966 O  O    . ARG   B 42  ? 0.25817 0.24235 0.12133 0.01085  -0.02928 -0.01044 45  ARG   B O    
2967 C  CB   . ARG   B 42  ? 0.25522 0.22123 0.12910 0.02670  -0.02709 0.00815  45  ARG   B CB   
2968 C  CG   . ARG   B 42  ? 0.30279 0.24178 0.14143 0.05055  -0.03992 -0.00321 45  ARG   B CG   
2969 C  CD   . ARG   B 42  ? 0.30184 0.22397 0.14987 0.03507  -0.03419 0.00073  45  ARG   B CD   
2970 N  NE   . ARG   B 42  ? 0.32070 0.17946 0.14304 0.03703  -0.04224 -0.01076 45  ARG   B NE   
2971 C  CZ   . ARG   B 42  ? 0.30477 0.17849 0.16419 0.04786  -0.05055 -0.01136 45  ARG   B CZ   
2972 N  NH1  . ARG   B 42  ? 0.31138 0.20035 0.19095 0.04971  -0.02791 -0.00209 45  ARG   B NH1  
2973 N  NH2  . ARG   B 42  ? 0.31819 0.18978 0.15791 0.04173  -0.05108 0.00734  45  ARG   B NH2  
2987 N  N    . PHE   B 43  ? 0.23166 0.20133 0.11691 0.00132  -0.02351 0.00739  46  PHE   B N    
2988 C  CA   . PHE   B 43  ? 0.22616 0.18936 0.11537 0.00525  -0.02354 0.00817  46  PHE   B CA   
2989 C  C    . PHE   B 43  ? 0.23322 0.16677 0.13000 0.01799  -0.01696 0.01721  46  PHE   B C    
2990 O  O    . PHE   B 43  ? 0.23347 0.16934 0.10921 0.01440  -0.01595 0.01232  46  PHE   B O    
2991 C  CB   . PHE   B 43  ? 0.21076 0.19642 0.13204 0.01303  -0.03276 -0.00055 46  PHE   B CB   
2992 C  CG   . PHE   B 43  ? 0.21121 0.19829 0.13184 0.02257  -0.02161 0.01858  46  PHE   B CG   
2993 C  CD1  . PHE   B 43  ? 0.23510 0.20060 0.15924 0.03713  -0.01779 0.02354  46  PHE   B CD1  
2994 C  CD2  . PHE   B 43  ? 0.23431 0.21236 0.14777 0.03117  -0.02321 0.00060  46  PHE   B CD2  
2995 C  CE1  . PHE   B 43  ? 0.23483 0.21304 0.17954 0.02954  -0.03102 0.03118  46  PHE   B CE1  
2996 C  CE2  . PHE   B 43  ? 0.24215 0.23544 0.16559 0.02851  -0.03476 0.00014  46  PHE   B CE2  
2997 C  CZ   . PHE   B 43  ? 0.22772 0.22316 0.18764 0.02940  -0.02767 0.00973  46  PHE   B CZ   
3007 N  N    . GLN   B 44  ? 0.22821 0.16639 0.11674 0.00398  -0.02443 0.01650  47  GLN   B N    
3008 C  CA   . GLN   B 44  ? 0.22856 0.16364 0.12163 0.01025  -0.02891 0.00779  47  GLN   B CA   
3009 C  C    . GLN   B 44  ? 0.21272 0.14388 0.11412 -0.00761 -0.01899 0.02261  47  GLN   B C    
3010 O  O    . GLN   B 44  ? 0.23268 0.17137 0.11772 -0.01324 -0.02537 0.00022  47  GLN   B O    
3011 C  CB   . GLN   B 44  ? 0.23471 0.17286 0.12758 0.01701  -0.01934 -0.00400 47  GLN   B CB   
3012 C  CG   . GLN   B 44  ? 0.26443 0.16886 0.13830 0.00226  -0.01441 0.01611  47  GLN   B CG   
3013 C  CD   . GLN   B 44  ? 0.28758 0.17489 0.14076 0.01654  -0.03733 -0.00667 47  GLN   B CD   
3014 O  OE1  . GLN   B 44  ? 0.35413 0.19472 0.13974 0.01451  -0.03355 -0.02619 47  GLN   B OE1  
3015 N  NE2  . GLN   B 44  ? 0.30124 0.16131 0.14725 0.01342  -0.03057 0.00047  47  GLN   B NE2  
3024 N  N    . VAL   B 45  ? 0.20516 0.14954 0.11678 -0.00513 -0.01481 0.01297  48  VAL   B N    
3025 C  CA   . VAL   B 45  ? 0.20625 0.15453 0.10493 0.00234  -0.01623 0.01423  48  VAL   B CA   
3026 C  C    . VAL   B 45  ? 0.21813 0.14808 0.11368 -0.01085 -0.01243 0.01151  48  VAL   B C    
3027 O  O    . VAL   B 45  ? 0.21617 0.15385 0.11809 -0.00235 -0.02488 0.02641  48  VAL   B O    
3028 C  CB   . VAL   B 45  ? 0.22900 0.15397 0.12462 0.00182  -0.00824 0.00781  48  VAL   B CB   
3029 C  CG1  . VAL   B 45  ? 0.23813 0.17024 0.13672 -0.00663 -0.02551 0.00391  48  VAL   B CG1  
3030 C  CG2  . VAL   B 45  ? 0.23978 0.15319 0.12812 0.01801  -0.01897 0.01541  48  VAL   B CG2  
3040 N  N    . ASP   B 46  ? 0.21138 0.14197 0.11038 -0.01137 -0.03089 0.00983  49  ASP   B N    
3041 C  CA   . ASP   B 46  ? 0.23111 0.13433 0.11910 -0.00938 -0.03182 0.01039  49  ASP   B CA   
3042 C  C    . ASP   B 46  ? 0.21238 0.13216 0.11622 -0.01587 -0.01661 0.01504  49  ASP   B C    
3043 O  O    . ASP   B 46  ? 0.21336 0.16483 0.11478 -0.02605 -0.03067 0.01400  49  ASP   B O    
3044 C  CB   . ASP   B 46  ? 0.23085 0.14763 0.12458 -0.00791 -0.03390 0.01485  49  ASP   B CB   
3045 C  CG   . ASP   B 46  ? 0.26086 0.14675 0.13347 -0.01733 -0.02992 0.01244  49  ASP   B CG   
3046 O  OD1  . ASP   B 46  ? 0.25797 0.15854 0.14228 -0.00656 -0.01750 0.00487  49  ASP   B OD1  
3047 O  OD2  . ASP   B 46  ? 0.30374 0.15167 0.15468 -0.02525 -0.03079 -0.00300 49  ASP   B OD2  
3052 N  N    . LEU   B 47  ? 0.20428 0.12535 0.11154 -0.01462 -0.02808 0.02136  50  LEU   B N    
3053 C  CA   . LEU   B 47  ? 0.21054 0.10576 0.10389 -0.01207 -0.02152 0.01565  50  LEU   B CA   
3054 C  C    . LEU   B 47  ? 0.20949 0.12019 0.10851 -0.02608 -0.02569 0.01650  50  LEU   B C    
3055 O  O    . LEU   B 47  ? 0.20346 0.12601 0.14597 -0.01265 -0.03054 0.03107  50  LEU   B O    
3056 C  CB   . LEU   B 47  ? 0.19613 0.11891 0.12765 -0.01420 -0.02255 0.02309  50  LEU   B CB   
3057 C  CG   . LEU   B 47  ? 0.21623 0.12473 0.15151 -0.01913 -0.03458 0.01564  50  LEU   B CG   
3058 C  CD1  . LEU   B 47  ? 0.23158 0.11833 0.14632 -0.01226 -0.02491 0.00404  50  LEU   B CD1  
3059 C  CD2  . LEU   B 47  ? 0.22984 0.14242 0.17776 -0.01101 -0.04068 0.01779  50  LEU   B CD2  
3071 N  N    . GLN   B 48  ? 0.21289 0.11086 0.11154 -0.01464 -0.02461 0.02340  51  GLN   B N    
3072 C  CA   . GLN   B 48  ? 0.21986 0.12836 0.11572 -0.01250 -0.02164 0.01742  51  GLN   B CA   
3073 C  C    . GLN   B 48  ? 0.22465 0.11946 0.12310 -0.00635 -0.03151 0.01871  51  GLN   B C    
3074 O  O    . GLN   B 48  ? 0.23408 0.12773 0.12013 -0.01023 -0.01492 0.02069  51  GLN   B O    
3075 C  CB   . GLN   B 48  ? 0.24144 0.12296 0.12472 -0.02143 -0.03471 0.01726  51  GLN   B CB   
3076 C  CG   . GLN   B 48  ? 0.25337 0.14470 0.12023 -0.02000 -0.02107 0.01372  51  GLN   B CG   
3077 C  CD   . GLN   B 48  ? 0.27717 0.15082 0.14809 -0.04460 -0.03700 0.00725  51  GLN   B CD   
3078 O  OE1  . GLN   B 48  ? 0.31515 0.18953 0.14082 -0.05484 -0.05913 0.01441  51  GLN   B OE1  
3079 N  NE2  . GLN   B 48  ? 0.31299 0.16005 0.14637 -0.06608 -0.03505 0.01454  51  GLN   B NE2  
3088 N  N    . ASN   B 49  ? 0.24220 0.11852 0.12741 -0.01290 -0.01261 0.02986  52  ASN   B N    
3089 C  CA   . ASN   B 49  ? 0.25773 0.12014 0.13682 -0.00933 -0.02855 0.03968  52  ASN   B CA   
3090 C  C    . ASN   B 49  ? 0.30402 0.13145 0.12659 0.00759  -0.01487 0.03203  52  ASN   B C    
3091 O  O    . ASN   B 49  ? 0.33972 0.13810 0.14940 0.00171  -0.00344 0.03111  52  ASN   B O    
3092 C  CB   . ASN   B 49  ? 0.28062 0.15390 0.15050 -0.00015 -0.02889 0.06799  52  ASN   B CB   
3093 C  CG   . ASN   B 49  ? 0.28341 0.16121 0.15930 -0.00862 -0.03982 0.04534  52  ASN   B CG   
3094 O  OD1  . ASN   B 49  ? 0.29378 0.17019 0.13723 -0.01451 -0.02150 0.04801  52  ASN   B OD1  
3095 N  ND2  . ASN   B 49  ? 0.27803 0.16701 0.15460 -0.00739 -0.03445 0.04973  52  ASN   B ND2  
3102 N  N    . GLY   B 50  ? 0.26964 0.15437 0.14307 -0.02994 -0.02158 0.02677  53  GLY   B N    
3103 C  CA   . GLY   B 50  ? 0.32245 0.17684 0.15522 -0.08051 -0.02354 0.02413  53  GLY   B CA   
3104 C  C    . GLY   B 50  ? 0.27720 0.13462 0.16268 -0.04603 -0.01769 0.03252  53  GLY   B C    
3105 O  O    . GLY   B 50  ? 0.25643 0.14070 0.16426 -0.03947 -0.02639 0.02724  53  GLY   B O    
3109 N  N    . SER   B 51  ? 0.27236 0.15491 0.17961 -0.05016 -0.01598 0.02387  54  SER   B N    
3110 C  CA   . SER   B 51  ? 0.25039 0.16189 0.21004 -0.04520 -0.01582 0.01790  54  SER   B CA   
3111 C  C    . SER   B 51  ? 0.24966 0.17544 0.21039 -0.04005 -0.04661 0.00973  54  SER   B C    
3112 O  O    . SER   B 51  ? 0.28710 0.19717 0.23839 -0.00797 -0.05930 0.01038  54  SER   B O    
3113 C  CB   . SER   B 51  ? 0.30124 0.17369 0.25511 -0.03414 -0.01120 0.00549  54  SER   B CB   
3114 O  OG   . SER   B 51  ? 0.30184 0.20386 0.28817 -0.04715 0.02296  -0.01753 54  SER   B OG   
3120 N  N    . SER   B 52  ? 0.27348 0.16154 0.19505 -0.04725 -0.04666 0.02453  55  SER   B N    
3121 C  CA   . SER   B 52  ? 0.29264 0.15743 0.19515 -0.04254 -0.02912 0.02729  55  SER   B CA   
3122 C  C    . SER   B 52  ? 0.29137 0.15244 0.18957 -0.03049 -0.05210 0.03180  55  SER   B C    
3123 O  O    . SER   B 52  ? 0.28321 0.16613 0.19720 -0.01075 -0.02908 0.03728  55  SER   B O    
3124 C  CB   . SER   B 52  ? 0.39359 0.15401 0.20616 -0.01048 -0.02355 0.02263  55  SER   B CB   
3125 O  OG   . SER   B 52  ? 0.40733 0.16796 0.19986 0.00121  0.00654  0.04081  55  SER   B OG   
3131 N  N    . MET   B 53  ? 0.33403 0.17872 0.18432 -0.02123 -0.07832 0.01275  56  MET   B N    
3132 C  CA   . MET   B 53  ? 0.37466 0.22350 0.19076 -0.01425 -0.10678 0.01858  56  MET   B CA   
3133 C  C    . MET   B 53  ? 0.34863 0.19835 0.17791 -0.03625 -0.06839 0.01491  56  MET   B C    
3134 O  O    . MET   B 53  ? 0.41096 0.22089 0.16424 -0.01914 -0.04555 0.01880  56  MET   B O    
3135 C  CB   . MET   B 53  ? 0.41019 0.33549 0.26775 0.02094  -0.13998 -0.01851 56  MET   B CB   
3136 C  CG   . MET   B 53  ? 0.44884 0.48479 0.37062 0.06167  -0.19047 -0.01511 56  MET   B CG   
3137 S  SD   . MET   B 53  ? 0.55145 0.59994 0.46486 0.08059  -0.17819 -0.01735 56  MET   B SD   
3138 C  CE   . MET   B 53  ? 0.58398 0.60921 0.50531 0.05940  -0.13583 -0.01860 56  MET   B CE   
3141 N  N    . LYS   B 54  ? 0.35587 0.17638 0.21173 -0.02764 -0.02190 0.01409  57  LYS   B N    
3142 C  CA   . LYS   B 54  ? 0.33763 0.15368 0.21797 -0.02376 -0.01434 -0.00875 57  LYS   B CA   
3143 C  C    . LYS   B 54  ? 0.32273 0.15994 0.21451 -0.03686 -0.00723 0.02388  57  LYS   B C    
3144 O  O    . LYS   B 54  ? 0.32800 0.17174 0.20967 -0.03250 0.00167  0.02610  57  LYS   B O    
3145 C  CB   . LYS   B 54  ? 0.37829 0.17852 0.25206 -0.01997 -0.01089 -0.03262 57  LYS   B CB   
3146 C  CG   . LYS   B 54  ? 0.42960 0.23402 0.29528 0.00069  0.00487  -0.06268 57  LYS   B CG   
3147 C  CD   . LYS   B 54  ? 0.48066 0.31970 0.36413 -0.01307 0.02821  -0.02651 57  LYS   B CD   
3148 C  CE   . LYS   B 54  ? 0.51856 0.38585 0.40523 -0.01530 0.04520  -0.01923 57  LYS   B CE   
3149 N  NZ   . LYS   B 54  ? 0.53517 0.41798 0.42461 -0.02918 0.05875  -0.01777 57  LYS   B NZ   
3163 N  N    . PRO   B 55  ? 0.33761 0.14219 0.22216 -0.02425 0.00035  0.03360  58  PRO   B N    
3164 C  CA   . PRO   B 55  ? 0.31712 0.13664 0.23112 -0.01677 -0.00759 0.03777  58  PRO   B CA   
3165 C  C    . PRO   B 55  ? 0.32558 0.14239 0.20107 -0.02589 0.01564  0.02052  58  PRO   B C    
3166 O  O    . PRO   B 55  ? 0.33242 0.14353 0.20320 -0.02168 0.01288  0.03719  58  PRO   B O    
3167 C  CB   . PRO   B 55  ? 0.31277 0.18851 0.26547 -0.02517 -0.05018 0.03992  58  PRO   B CB   
3168 C  CG   . PRO   B 55  ? 0.36000 0.18946 0.25139 -0.00499 -0.03148 0.06102  58  PRO   B CG   
3169 C  CD   . PRO   B 55  ? 0.35458 0.16898 0.21954 -0.02691 -0.01690 0.05143  58  PRO   B CD   
3177 N  N    . ARG   B 56  ? 0.29862 0.13643 0.17715 -0.02965 0.00583  0.01601  59  ARG   B N    
3178 C  CA   . ARG   B 56  ? 0.28589 0.11989 0.16026 -0.02796 -0.01713 0.02228  59  ARG   B CA   
3179 C  C    . ARG   B 56  ? 0.26087 0.12133 0.15319 -0.02569 -0.01376 0.02533  59  ARG   B C    
3180 O  O    . ARG   B 56  ? 0.27885 0.14166 0.18278 -0.02504 -0.02526 0.01549  59  ARG   B O    
3181 C  CB   . ARG   B 56  ? 0.31522 0.14713 0.15951 -0.02717 -0.01723 0.01226  59  ARG   B CB   
3182 C  CG   . ARG   B 56  ? 0.35553 0.14073 0.15970 -0.04283 -0.03422 0.04181  59  ARG   B CG   
3183 C  CD   . ARG   B 56  ? 0.37348 0.16029 0.19035 -0.03324 -0.01621 0.03140  59  ARG   B CD   
3184 N  NE   . ARG   B 56  ? 0.40134 0.18294 0.19220 -0.02807 -0.03096 0.03805  59  ARG   B NE   
3185 C  CZ   . ARG   B 56  ? 0.43225 0.22251 0.18863 -0.00860 -0.04155 0.03986  59  ARG   B CZ   
3186 N  NH1  . ARG   B 56  ? 0.47994 0.26676 0.19110 -0.03194 -0.00699 0.03753  59  ARG   B NH1  
3187 N  NH2  . ARG   B 56  ? 0.44193 0.21832 0.20794 -0.00442 -0.04243 0.05517  59  ARG   B NH2  
3201 N  N    . ALA   B 57  ? 0.26891 0.12958 0.14881 -0.01909 -0.01322 0.01748  60  ALA   B N    
3202 C  CA   . ALA   B 57  ? 0.25350 0.12252 0.15473 -0.02211 -0.01261 0.00688  60  ALA   B CA   
3203 C  C    . ALA   B 57  ? 0.24812 0.11633 0.14930 -0.01572 -0.02236 0.02686  60  ALA   B C    
3204 O  O    . ALA   B 57  ? 0.26241 0.12148 0.13560 -0.01715 -0.02498 0.01554  60  ALA   B O    
3205 C  CB   . ALA   B 57  ? 0.24896 0.16154 0.18013 -0.04536 -0.01552 -0.01200 60  ALA   B CB   
3211 N  N    . ASP   B 58  ? 0.26323 0.11904 0.14163 -0.02737 -0.02466 0.03080  61  ASP   B N    
3212 C  CA   . ASP   B 58  ? 0.23540 0.11442 0.15238 -0.00940 -0.02971 0.03384  61  ASP   B CA   
3213 C  C    . ASP   B 58  ? 0.23423 0.11757 0.14412 -0.00876 -0.02525 0.00605  61  ASP   B C    
3214 O  O    . ASP   B 58  ? 0.24043 0.12059 0.13506 -0.01777 -0.01482 0.02772  61  ASP   B O    
3215 C  CB   . ASP   B 58  ? 0.25439 0.13018 0.16342 -0.00743 -0.04181 0.03006  61  ASP   B CB   
3216 C  CG   . ASP   B 58  ? 0.25422 0.14810 0.18076 -0.00428 -0.03362 0.03556  61  ASP   B CG   
3217 O  OD1  . ASP   B 58  ? 0.26611 0.14602 0.19530 0.01288  -0.02108 0.04492  61  ASP   B OD1  
3218 O  OD2  . ASP   B 58  ? 0.28255 0.19145 0.18960 0.00703  -0.05120 0.03676  61  ASP   B OD2  
3223 N  N    . VAL   B 59  ? 0.21633 0.11664 0.14552 -0.01059 -0.01584 0.02153  62  VAL   B N    
3224 C  CA   . VAL   B 59  ? 0.23173 0.10985 0.14559 -0.00812 -0.03021 0.02461  62  VAL   B CA   
3225 C  C    . VAL   B 59  ? 0.22766 0.10885 0.13446 0.01349  -0.02610 0.02294  62  VAL   B C    
3226 O  O    . VAL   B 59  ? 0.21899 0.12505 0.13648 0.00383  -0.01421 0.01961  62  VAL   B O    
3227 C  CB   . VAL   B 59  ? 0.24446 0.13082 0.14222 -0.00839 -0.03423 0.01882  62  VAL   B CB   
3228 C  CG1  . VAL   B 59  ? 0.25010 0.12663 0.14083 0.00119  -0.03390 0.02765  62  VAL   B CG1  
3229 C  CG2  . VAL   B 59  ? 0.25566 0.14475 0.15084 -0.02454 -0.03463 0.00913  62  VAL   B CG2  
3239 N  N    . ALA   B 60  ? 0.19950 0.11689 0.12157 -0.00456 -0.01879 0.02712  63  ALA   B N    
3240 C  CA   . ALA   B 60  ? 0.19335 0.11910 0.12551 -0.00017 -0.01968 0.02012  63  ALA   B CA   
3241 C  C    . ALA   B 60  ? 0.19905 0.12365 0.12452 -0.00262 -0.02151 0.02149  63  ALA   B C    
3242 O  O    . ALA   B 60  ? 0.20388 0.13113 0.13598 -0.00360 -0.02549 0.02306  63  ALA   B O    
3243 C  CB   . ALA   B 60  ? 0.20717 0.12864 0.12911 0.00020  -0.01912 0.02688  63  ALA   B CB   
3249 N  N    . PHE   B 61  ? 0.19563 0.11783 0.12273 -0.00321 -0.03060 0.02673  64  PHE   B N    
3250 C  CA   . PHE   B 61  ? 0.19552 0.11444 0.12037 0.00229  -0.01621 0.02641  64  PHE   B CA   
3251 C  C    . PHE   B 61  ? 0.21158 0.10694 0.12605 0.00639  -0.00657 0.03162  64  PHE   B C    
3252 O  O    . PHE   B 61  ? 0.22089 0.13269 0.11624 -0.00520 -0.01476 0.02135  64  PHE   B O    
3253 C  CB   . PHE   B 61  ? 0.20784 0.11477 0.12168 -0.00244 -0.01547 0.01643  64  PHE   B CB   
3254 C  CG   . PHE   B 61  ? 0.20264 0.11534 0.13773 -0.00552 -0.01776 0.02560  64  PHE   B CG   
3255 C  CD1  . PHE   B 61  ? 0.19703 0.13761 0.15875 0.00034  -0.00722 0.03938  64  PHE   B CD1  
3256 C  CD2  . PHE   B 61  ? 0.20955 0.14093 0.17722 0.00563  0.01665  0.02977  64  PHE   B CD2  
3257 C  CE1  . PHE   B 61  ? 0.22028 0.13555 0.15733 -0.00014 0.00108  0.03651  64  PHE   B CE1  
3258 C  CE2  . PHE   B 61  ? 0.23125 0.13711 0.16415 0.01888  0.01897  0.05645  64  PHE   B CE2  
3259 C  CZ   . PHE   B 61  ? 0.22505 0.12510 0.15210 0.00591  -0.00925 0.02514  64  PHE   B CZ   
3269 N  N    . HIS   B 62  ? 0.20519 0.12469 0.11965 0.00604  -0.01809 0.02756  65  HIS   B N    
3270 C  CA   . HIS   B 62  ? 0.22321 0.13099 0.11777 0.01013  -0.01549 0.02878  65  HIS   B CA   
3271 C  C    . HIS   B 62  ? 0.21668 0.13069 0.10997 0.01130  -0.00155 0.02157  65  HIS   B C    
3272 O  O    . HIS   B 62  ? 0.22130 0.14174 0.13632 0.01465  0.00411  0.04800  65  HIS   B O    
3273 C  CB   . HIS   B 62  ? 0.23033 0.13870 0.12088 0.01944  -0.00862 0.02967  65  HIS   B CB   
3274 C  CG   . HIS   B 62  ? 0.23071 0.14035 0.12531 0.02335  -0.01799 0.01851  65  HIS   B CG   
3275 N  ND1  . HIS   B 62  ? 0.24460 0.16246 0.12688 0.02619  -0.02388 0.00278  65  HIS   B ND1  
3276 C  CD2  . HIS   B 62  ? 0.24924 0.15065 0.13211 0.02202  -0.01309 0.01150  65  HIS   B CD2  
3277 C  CE1  . HIS   B 62  ? 0.23407 0.15025 0.14041 0.00722  -0.02413 0.00442  65  HIS   B CE1  
3278 N  NE2  . HIS   B 62  ? 0.26576 0.13974 0.14379 0.02762  -0.03196 0.01856  65  HIS   B NE2  
3286 N  N    . PHE   B 63  ? 0.19949 0.12385 0.11831 0.00760  -0.01622 0.02249  66  PHE   B N    
3287 C  CA   . PHE   B 63  ? 0.20161 0.12705 0.12997 0.00785  -0.01472 0.03169  66  PHE   B CA   
3288 C  C    . PHE   B 63  ? 0.21850 0.12299 0.13228 0.00127  -0.01600 0.04225  66  PHE   B C    
3289 O  O    . PHE   B 63  ? 0.22292 0.15063 0.11696 0.01339  -0.00697 0.02678  66  PHE   B O    
3290 C  CB   . PHE   B 63  ? 0.21067 0.14013 0.11921 0.00802  0.00038  0.03674  66  PHE   B CB   
3291 C  CG   . PHE   B 63  ? 0.23176 0.13060 0.12409 0.01507  -0.00218 0.02929  66  PHE   B CG   
3292 C  CD1  . PHE   B 63  ? 0.21822 0.14318 0.15200 0.01553  0.00394  0.02503  66  PHE   B CD1  
3293 C  CD2  . PHE   B 63  ? 0.22396 0.14899 0.13952 0.02174  0.00391  0.04543  66  PHE   B CD2  
3294 C  CE1  . PHE   B 63  ? 0.22214 0.14743 0.16796 0.01220  0.02120  0.04155  66  PHE   B CE1  
3295 C  CE2  . PHE   B 63  ? 0.23047 0.16343 0.15355 0.04190  -0.00597 0.03843  66  PHE   B CE2  
3296 C  CZ   . PHE   B 63  ? 0.24206 0.14374 0.16206 0.02884  0.01126  0.04320  66  PHE   B CZ   
3306 N  N    . ASN   B 64  ? 0.21146 0.13721 0.11715 0.01004  0.00405  0.03200  67  ASN   B N    
3307 C  CA   . ASN   B 64  ? 0.23317 0.15150 0.10937 0.02326  -0.00682 0.03528  67  ASN   B CA   
3308 C  C    . ASN   B 64  ? 0.24217 0.16648 0.12322 0.02589  -0.00362 0.03607  67  ASN   B C    
3309 O  O    . ASN   B 64  ? 0.22904 0.17749 0.13177 0.03304  0.01288  0.03344  67  ASN   B O    
3310 C  CB   . ASN   B 64  ? 0.23096 0.14318 0.12283 0.01933  -0.00649 0.02231  67  ASN   B CB   
3311 C  CG   . ASN   B 64  ? 0.25374 0.15963 0.12468 0.03672  -0.00450 0.01405  67  ASN   B CG   
3312 O  OD1  . ASN   B 64  ? 0.26645 0.17418 0.13171 0.05247  -0.00036 0.01069  67  ASN   B OD1  
3313 N  ND2  . ASN   B 64  ? 0.24328 0.18423 0.13337 0.04439  -0.01261 -0.00453 67  ASN   B ND2  
3320 N  N    . PRO   B 65  ? 0.23553 0.16544 0.12073 0.03582  0.00400  0.04383  68  PRO   B N    
3321 C  CA   . PRO   B 65  ? 0.23203 0.16927 0.13482 0.04986  -0.00532 0.03583  68  PRO   B CA   
3322 C  C    . PRO   B 65  ? 0.21727 0.18178 0.12584 0.02474  0.00111  0.03757  68  PRO   B C    
3323 O  O    . PRO   B 65  ? 0.24591 0.21112 0.12734 0.02737  -0.00243 0.02062  68  PRO   B O    
3324 C  CB   . PRO   B 65  ? 0.23226 0.18789 0.13841 0.03201  0.00517  0.04409  68  PRO   B CB   
3325 C  CG   . PRO   B 65  ? 0.21325 0.17024 0.13425 0.03142  0.00727  0.04379  68  PRO   B CG   
3326 C  CD   . PRO   B 65  ? 0.24188 0.16931 0.12951 0.02857  0.00173  0.03208  68  PRO   B CD   
3334 N  N    . ARG   B 66  ? 0.24531 0.21229 0.12917 0.03580  0.01106  0.04443  69  ARG   B N    
3335 C  CA   . ARG   B 66  ? 0.25074 0.23146 0.12747 0.03550  0.01345  0.05409  69  ARG   B CA   
3336 C  C    . ARG   B 66  ? 0.24243 0.25558 0.14788 0.03172  0.01625  0.05155  69  ARG   B C    
3337 O  O    . ARG   B 66  ? 0.28243 0.26801 0.15496 0.00681  0.00924  0.06906  69  ARG   B O    
3338 C  CB   . ARG   B 66  ? 0.29010 0.21422 0.12970 0.05680  0.00511  0.02926  69  ARG   B CB   
3339 C  CG   . ARG   B 66  ? 0.27214 0.23447 0.14408 0.05243  0.01131  0.03594  69  ARG   B CG   
3340 C  CD   . ARG   B 66  ? 0.30319 0.20975 0.14341 0.06650  0.00927  0.02283  69  ARG   B CD   
3341 N  NE   . ARG   B 66  ? 0.28958 0.19619 0.14193 0.05299  0.00859  0.02285  69  ARG   B NE   
3342 C  CZ   . ARG   B 66  ? 0.29790 0.17937 0.14385 0.07615  0.00359  0.02056  69  ARG   B CZ   
3343 N  NH1  . ARG   B 66  ? 0.30731 0.22411 0.15905 0.09120  0.00939  0.00807  69  ARG   B NH1  
3344 N  NH2  . ARG   B 66  ? 0.28528 0.21074 0.15277 0.05706  0.00243  0.02042  69  ARG   B NH2  
3358 N  N    . PHE   B 67  ? 0.27478 0.26513 0.13008 0.04626  0.00039  0.05300  70  PHE   B N    
3359 C  CA   A PHE   B 67  ? 0.28298 0.28870 0.12159 0.06006  0.02734  0.05260  70  PHE   B CA   
3360 C  CA   B PHE   B 67  ? 0.28434 0.28304 0.13123 0.04716  0.00941  0.04223  70  PHE   B CA   
3361 C  C    . PHE   B 67  ? 0.30544 0.31253 0.14709 0.05530  0.02011  0.05535  70  PHE   B C    
3362 O  O    . PHE   B 67  ? 0.35843 0.37604 0.15219 0.07901  0.02300  0.08681  70  PHE   B O    
3363 C  CB   A PHE   B 67  ? 0.29827 0.29810 0.12654 0.07990  0.01820  0.05215  70  PHE   B CB   
3364 C  CB   B PHE   B 67  ? 0.29598 0.27772 0.14190 0.03706  -0.02087 0.02693  70  PHE   B CB   
3365 C  CG   A PHE   B 67  ? 0.27170 0.30327 0.13476 0.09944  0.01950  0.07767  70  PHE   B CG   
3366 C  CG   B PHE   B 67  ? 0.27553 0.26549 0.13604 0.01980  -0.03733 0.02289  70  PHE   B CG   
3367 C  CD1  A PHE   B 67  ? 0.28616 0.31974 0.15498 0.09271  0.01411  0.09641  70  PHE   B CD1  
3368 C  CD1  B PHE   B 67  ? 0.28905 0.26764 0.13785 0.01164  -0.00586 0.03349  70  PHE   B CD1  
3369 C  CD2  A PHE   B 67  ? 0.30352 0.30474 0.13658 0.08895  0.03444  0.08046  70  PHE   B CD2  
3370 C  CD2  B PHE   B 67  ? 0.27470 0.25262 0.13173 0.02122  -0.03232 -0.00255 70  PHE   B CD2  
3371 C  CE1  A PHE   B 67  ? 0.28076 0.32571 0.13501 0.09511  0.01536  0.07829  70  PHE   B CE1  
3372 C  CE1  B PHE   B 67  ? 0.25859 0.27103 0.11790 0.03178  0.04184  0.04750  70  PHE   B CE1  
3373 C  CE2  A PHE   B 67  ? 0.24862 0.32338 0.14276 0.10314  0.02121  0.08575  70  PHE   B CE2  
3374 C  CE2  B PHE   B 67  ? 0.27029 0.24718 0.13505 0.04538  -0.02744 0.03106  70  PHE   B CE2  
3375 C  CZ   A PHE   B 67  ? 0.27129 0.33296 0.14966 0.09916  0.03908  0.07722  70  PHE   B CZ   
3376 C  CZ   B PHE   B 67  ? 0.26734 0.26050 0.10515 0.03780  -0.00831 0.05239  70  PHE   B CZ   
3393 N  N    . LYS   B 68  ? 0.33395 0.32931 0.14670 0.05684  0.03949  0.02957  71  LYS   B N    
3394 C  CA   . LYS   B 68  ? 0.40563 0.41060 0.16808 0.03886  0.06978  0.00869  71  LYS   B CA   
3395 C  C    . LYS   B 68  ? 0.41842 0.46998 0.18265 0.05001  0.10429  0.03316  71  LYS   B C    
3396 O  O    . LYS   B 68  ? 0.39137 0.46355 0.21224 0.12114  0.09649  0.02800  71  LYS   B O    
3397 C  CB   . LYS   B 68  ? 0.43245 0.45445 0.21722 0.05455  0.08402  -0.00647 71  LYS   B CB   
3398 C  CG   . LYS   B 68  ? 0.51599 0.50558 0.30262 0.03691  0.03784  -0.00422 71  LYS   B CG   
3399 C  CD   . LYS   B 68  ? 0.57452 0.55009 0.36330 0.02705  0.00534  0.00090  71  LYS   B CD   
3400 C  CE   . LYS   B 68  ? 0.61380 0.59313 0.39471 0.01468  0.00018  0.00509  71  LYS   B CE   
3401 N  NZ   . LYS   B 68  ? 0.63661 0.62359 0.40581 0.01362  -0.01022 0.00499  71  LYS   B NZ   
3415 N  N    . ARG   B 69  ? 0.49293 0.54873 0.19246 0.00262  0.11446  0.03130  72  ARG   B N    
3416 C  CA   . ARG   B 69  ? 0.49203 0.58601 0.27086 -0.01515 0.10103  0.03856  72  ARG   B CA   
3417 C  C    . ARG   B 69  ? 0.46495 0.57530 0.21584 -0.05152 0.08599  0.08035  72  ARG   B C    
3418 O  O    . ARG   B 69  ? 0.46632 0.55318 0.20632 -0.04651 0.01363  0.13691  72  ARG   B O    
3419 C  CB   . ARG   B 69  ? 0.55559 0.62747 0.33800 0.01479  0.08298  0.01745  72  ARG   B CB   
3420 C  CG   . ARG   B 69  ? 0.60818 0.66009 0.37388 0.03523  0.07206  0.01387  72  ARG   B CG   
3421 C  CD   . ARG   B 69  ? 0.65420 0.67511 0.40194 0.05220  0.06497  0.00734  72  ARG   B CD   
3422 N  NE   . ARG   B 69  ? 0.68847 0.67847 0.42394 0.06827  0.05062  -0.00021 72  ARG   B NE   
3423 C  CZ   . ARG   B 69  ? 0.70802 0.66981 0.44176 0.07777  0.04626  -0.01605 72  ARG   B CZ   
3424 N  NH1  . ARG   B 69  ? 0.71185 0.66107 0.43792 0.08587  0.04261  -0.01761 72  ARG   B NH1  
3425 N  NH2  . ARG   B 69  ? 0.71188 0.66754 0.45794 0.08049  0.03096  -0.00428 72  ARG   B NH2  
3439 N  N    . ALA   B 70  ? 0.44920 0.52979 0.20309 -0.04462 0.10019  0.09451  73  ALA   B N    
3440 C  CA   . ALA   B 70  ? 0.41061 0.46904 0.21535 -0.03694 0.07570  0.11830  73  ALA   B CA   
3441 C  C    . ALA   B 70  ? 0.36350 0.41476 0.20660 0.00521  0.03467  0.11554  73  ALA   B C    
3442 O  O    . ALA   B 70  ? 0.42506 0.41138 0.23248 0.05028  0.01218  0.14297  73  ALA   B O    
3443 C  CB   . ALA   B 70  ? 0.42584 0.48638 0.23513 -0.07081 0.06992  0.10188  73  ALA   B CB   
3449 N  N    . GLY   B 71  ? 0.31888 0.34469 0.16980 0.02994  0.03693  0.09982  74  GLY   B N    
3450 C  CA   . GLY   B 71  ? 0.28533 0.30684 0.17428 0.03363  0.02354  0.07248  74  GLY   B CA   
3451 C  C    . GLY   B 71  ? 0.25729 0.26286 0.17607 0.01914  0.03984  0.06206  74  GLY   B C    
3452 O  O    . GLY   B 71  ? 0.29669 0.27874 0.18372 0.01069  0.03600  0.08457  74  GLY   B O    
3456 N  N    . CYS   B 72  ? 0.24959 0.23100 0.16505 0.02631  0.03190  0.05254  75  CYS   B N    
3457 C  CA   . CYS   B 72  ? 0.23113 0.23119 0.16538 0.04049  0.02028  0.03410  75  CYS   B CA   
3458 C  C    . CYS   B 72  ? 0.21561 0.20310 0.17224 0.01799  -0.01743 0.06538  75  CYS   B C    
3459 O  O    . CYS   B 72  ? 0.24005 0.20965 0.15995 0.04336  0.00278  0.04934  75  CYS   B O    
3460 C  CB   . CYS   B 72  ? 0.26706 0.23570 0.18452 0.02914  0.03184  0.04247  75  CYS   B CB   
3461 S  SG   . CYS   B 72  ? 0.30312 0.23929 0.20851 0.06826  0.04012  0.05529  75  CYS   B SG   
3467 N  N    . ILE   B 73  ? 0.22860 0.18225 0.17480 0.02307  0.00298  0.05278  76  ILE   B N    
3468 C  CA   . ILE   B 73  ? 0.22217 0.16161 0.16029 0.02891  0.02557  0.05725  76  ILE   B CA   
3469 C  C    . ILE   B 73  ? 0.23127 0.16780 0.16788 0.01325  0.02417  0.04382  76  ILE   B C    
3470 O  O    . ILE   B 73  ? 0.23372 0.16270 0.20126 0.01292  -0.00263 0.05304  76  ILE   B O    
3471 C  CB   . ILE   B 73  ? 0.23435 0.15515 0.16017 0.02335  0.01847  0.05209  76  ILE   B CB   
3472 C  CG1  . ILE   B 73  ? 0.23861 0.17921 0.18355 0.04504  0.02456  0.06286  76  ILE   B CG1  
3473 C  CG2  . ILE   B 73  ? 0.26741 0.15922 0.14363 0.02052  0.01329  0.03206  76  ILE   B CG2  
3474 C  CD1  . ILE   B 73  ? 0.23727 0.17612 0.21368 0.03471  0.03662  0.05171  76  ILE   B CD1  
3486 N  N    . VAL   B 74  ? 0.23019 0.15575 0.14337 0.01253  0.00415  0.04314  77  VAL   B N    
3487 C  CA   . VAL   B 74  ? 0.24250 0.14768 0.15497 0.02550  0.00246  0.05109  77  VAL   B CA   
3488 C  C    . VAL   B 74  ? 0.20704 0.14895 0.15817 0.02186  -0.00603 0.04215  77  VAL   B C    
3489 O  O    . VAL   B 74  ? 0.23282 0.15525 0.14848 0.01814  -0.00724 0.03199  77  VAL   B O    
3490 C  CB   . VAL   B 74  ? 0.26669 0.14909 0.17532 0.03641  -0.00550 0.03552  77  VAL   B CB   
3491 C  CG1  . VAL   B 74  ? 0.30422 0.15993 0.19040 0.04637  -0.00896 0.01863  77  VAL   B CG1  
3492 C  CG2  . VAL   B 74  ? 0.30896 0.18308 0.16622 0.05400  0.02394  0.02073  77  VAL   B CG2  
3502 N  N    . CYS   B 75  ? 0.19902 0.14696 0.15620 0.02557  0.01030  0.04780  78  CYS   B N    
3503 C  CA   . CYS   B 75  ? 0.20681 0.14391 0.15102 0.02127  0.00775  0.04640  78  CYS   B CA   
3504 C  C    . CYS   B 75  ? 0.23057 0.15656 0.14204 0.02591  0.01233  0.03085  78  CYS   B C    
3505 O  O    . CYS   B 75  ? 0.22287 0.16551 0.15769 0.02643  0.01775  0.04984  78  CYS   B O    
3506 C  CB   . CYS   B 75  ? 0.22334 0.14182 0.15392 0.02203  0.00887  0.03827  78  CYS   B CB   
3507 S  SG   . CYS   B 75  ? 0.23492 0.14388 0.17329 0.02497  0.01245  0.05088  78  CYS   B SG   
3513 N  N    . ASN   B 76  ? 0.21864 0.13505 0.14443 0.00994  0.00373  0.04360  79  ASN   B N    
3514 C  CA   . ASN   B 76  ? 0.22779 0.12948 0.13833 0.01959  -0.00190 0.03443  79  ASN   B CA   
3515 C  C    . ASN   B 76  ? 0.21574 0.12761 0.13494 0.00907  -0.00990 0.00960  79  ASN   B C    
3516 O  O    . ASN   B 76  ? 0.22343 0.12711 0.13545 0.00550  -0.01232 0.02624  79  ASN   B O    
3517 C  CB   . ASN   B 76  ? 0.22763 0.14528 0.13605 0.03221  -0.00931 0.02462  79  ASN   B CB   
3518 C  CG   . ASN   B 76  ? 0.23426 0.15073 0.15222 0.02464  -0.00015 0.02668  79  ASN   B CG   
3519 O  OD1  . ASN   B 76  ? 0.24246 0.15297 0.14445 0.03774  -0.00844 0.01977  79  ASN   B OD1  
3520 N  ND2  . ASN   B 76  ? 0.25348 0.16032 0.16506 0.03624  -0.00813 0.01231  79  ASN   B ND2  
3527 N  N    . THR   B 77  ? 0.21050 0.12797 0.14522 0.01447  -0.00901 0.02699  80  THR   B N    
3528 C  CA   . THR   B 77  ? 0.21114 0.11407 0.15103 0.00167  -0.01236 0.03039  80  THR   B CA   
3529 C  C    . THR   B 77  ? 0.21794 0.11734 0.14972 0.01553  -0.01477 0.02436  80  THR   B C    
3530 O  O    . THR   B 77  ? 0.23767 0.12019 0.16111 0.02051  -0.01088 0.02300  80  THR   B O    
3531 C  CB   . THR   B 77  ? 0.21723 0.11799 0.15433 0.00243  -0.02835 0.01896  80  THR   B CB   
3532 O  OG1  . THR   B 77  ? 0.21566 0.13025 0.14125 -0.00274 -0.02665 0.02515  80  THR   B OG1  
3533 C  CG2  . THR   B 77  ? 0.24238 0.13080 0.15127 0.00200  -0.02304 0.03470  80  THR   B CG2  
3541 N  N    . LEU   B 78  ? 0.21777 0.12321 0.14794 0.01728  -0.00797 0.02580  81  LEU   B N    
3542 C  CA   . LEU   B 78  ? 0.23415 0.10516 0.16397 0.01061  -0.01583 0.02837  81  LEU   B CA   
3543 C  C    . LEU   B 78  ? 0.24579 0.11094 0.15979 0.00789  -0.02637 0.03827  81  LEU   B C    
3544 O  O    . LEU   B 78  ? 0.22697 0.13450 0.15539 0.00724  -0.02395 0.02816  81  LEU   B O    
3545 C  CB   . LEU   B 78  ? 0.24411 0.12182 0.15873 0.00621  -0.02428 0.02261  81  LEU   B CB   
3546 C  CG   . LEU   B 78  ? 0.25447 0.12780 0.17619 -0.00026 -0.02843 0.02164  81  LEU   B CG   
3547 C  CD1  . LEU   B 78  ? 0.29398 0.13370 0.18115 0.01480  -0.02310 0.00648  81  LEU   B CD1  
3548 C  CD2  . LEU   B 78  ? 0.28510 0.15031 0.18277 0.00152  -0.02452 -0.00764 81  LEU   B CD2  
3560 N  N    . ILE   B 79  ? 0.25023 0.11897 0.16841 0.02031  -0.02727 0.04271  82  ILE   B N    
3561 C  CA   . ILE   B 79  ? 0.25679 0.13001 0.17946 0.02209  -0.02910 0.04327  82  ILE   B CA   
3562 C  C    . ILE   B 79  ? 0.26884 0.13603 0.17631 0.03493  -0.02552 0.04728  82  ILE   B C    
3563 O  O    . ILE   B 79  ? 0.28231 0.14909 0.19850 0.04536  -0.00860 0.04035  82  ILE   B O    
3564 C  CB   . ILE   B 79  ? 0.26833 0.14887 0.17582 0.02748  -0.03632 0.03642  82  ILE   B CB   
3565 C  CG1  . ILE   B 79  ? 0.27352 0.16569 0.21924 0.01194  -0.06126 0.02489  82  ILE   B CG1  
3566 C  CG2  . ILE   B 79  ? 0.29219 0.18036 0.18398 0.04119  -0.02686 0.04172  82  ILE   B CG2  
3567 C  CD1  . ILE   B 79  ? 0.28680 0.18298 0.21836 0.01340  -0.08027 0.00685  82  ILE   B CD1  
3579 N  N    . ASN   B 80  ? 0.30352 0.14534 0.20490 0.02054  -0.01058 0.06332  83  ASN   B N    
3580 C  CA   . ASN   B 80  ? 0.31609 0.15677 0.22811 0.02953  -0.00717 0.05968  83  ASN   B CA   
3581 C  C    . ASN   B 80  ? 0.30560 0.13606 0.22622 0.04215  0.00702  0.03092  83  ASN   B C    
3582 O  O    . ASN   B 80  ? 0.35812 0.14282 0.25177 0.05014  0.00958  0.03883  83  ASN   B O    
3583 C  CB   . ASN   B 80  ? 0.34941 0.15718 0.25640 0.03273  -0.02398 0.06785  83  ASN   B CB   
3584 C  CG   . ASN   B 80  ? 0.33445 0.21066 0.25355 0.04949  -0.00321 0.07731  83  ASN   B CG   
3585 O  OD1  . ASN   B 80  ? 0.36677 0.25262 0.24561 0.05797  -0.00309 0.07508  83  ASN   B OD1  
3586 N  ND2  . ASN   B 80  ? 0.35323 0.27182 0.28531 0.06666  -0.03949 0.08021  83  ASN   B ND2  
3593 N  N    . GLU   B 81  ? 0.29396 0.14582 0.21140 0.01451  -0.00375 0.02745  84  GLU   B N    
3594 C  CA   . GLU   B 81  ? 0.31171 0.14625 0.25256 0.00237  -0.02855 -0.00227 84  GLU   B CA   
3595 C  C    . GLU   B 81  ? 0.33070 0.15176 0.22937 0.00960  -0.00994 0.00012  84  GLU   B C    
3596 O  O    . GLU   B 81  ? 0.38395 0.19699 0.23173 -0.02034 0.00963  -0.00641 84  GLU   B O    
3597 C  CB   . GLU   B 81  ? 0.34666 0.15115 0.29356 -0.01404 -0.00522 -0.02220 84  GLU   B CB   
3598 C  CG   . GLU   B 81  ? 0.36409 0.16944 0.35441 -0.01473 0.02595  -0.02123 84  GLU   B CG   
3599 C  CD   . GLU   B 81  ? 0.41220 0.19028 0.41006 0.00076  0.02349  -0.00997 84  GLU   B CD   
3600 O  OE1  . GLU   B 81  ? 0.46240 0.20232 0.49497 0.03752  -0.01368 0.01884  84  GLU   B OE1  
3601 O  OE2  . GLU   B 81  ? 0.40954 0.18043 0.37166 -0.01832 0.05988  -0.02737 84  GLU   B OE2  
3608 N  N    . LYS   B 82  ? 0.30125 0.13395 0.22378 0.02970  -0.01219 0.02135  85  LYS   B N    
3609 C  CA   . LYS   B 82  ? 0.31994 0.14269 0.24731 0.03722  0.01576  0.01981  85  LYS   B CA   
3610 C  C    . LYS   B 82  ? 0.28025 0.13827 0.20737 0.02754  0.00965  0.02302  85  LYS   B C    
3611 O  O    . LYS   B 82  ? 0.28219 0.13823 0.18564 0.03183  0.00599  0.01045  85  LYS   B O    
3612 C  CB   . LYS   B 82  ? 0.32687 0.16667 0.29856 0.05301  0.01713  0.04621  85  LYS   B CB   
3613 C  CG   . LYS   B 82  ? 0.41041 0.27362 0.36953 0.09755  -0.00690 0.07371  85  LYS   B CG   
3614 C  CD   . LYS   B 82  ? 0.49776 0.37047 0.44029 0.09034  -0.01232 0.05039  85  LYS   B CD   
3615 C  CE   . LYS   B 82  ? 0.57482 0.44621 0.48406 0.09298  0.00579  0.03854  85  LYS   B CE   
3616 N  NZ   . LYS   B 82  ? 0.62018 0.49662 0.51364 0.07142  0.02127  0.03209  85  LYS   B NZ   
3630 N  N    . TRP   B 83  ? 0.27595 0.14598 0.19889 0.02932  0.01060  0.01996  86  TRP   B N    
3631 C  CA   . TRP   B 83  ? 0.27435 0.14603 0.18183 0.03601  0.00380  0.02342  86  TRP   B CA   
3632 C  C    . TRP   B 83  ? 0.28109 0.15209 0.19611 0.04473  0.01722  0.01617  86  TRP   B C    
3633 O  O    . TRP   B 83  ? 0.30952 0.16226 0.24100 0.05938  0.01772  -0.00728 86  TRP   B O    
3634 C  CB   . TRP   B 83  ? 0.29617 0.16933 0.17061 0.02810  0.00866  0.02401  86  TRP   B CB   
3635 C  CG   . TRP   B 83  ? 0.32750 0.14169 0.16455 0.03791  -0.01138 0.01249  86  TRP   B CG   
3636 C  CD1  . TRP   B 83  ? 0.34635 0.18472 0.17421 0.02920  -0.01821 -0.00397 86  TRP   B CD1  
3637 C  CD2  . TRP   B 83  ? 0.30062 0.14988 0.15485 0.02089  -0.00440 0.02911  86  TRP   B CD2  
3638 N  NE1  . TRP   B 83  ? 0.33131 0.18256 0.18133 0.00548  -0.03684 -0.00735 86  TRP   B NE1  
3639 C  CE2  . TRP   B 83  ? 0.29860 0.17048 0.16644 0.00729  -0.04731 0.01273  86  TRP   B CE2  
3640 C  CE3  . TRP   B 83  ? 0.26879 0.14516 0.15829 0.01260  -0.00932 0.02209  86  TRP   B CE3  
3641 C  CZ2  . TRP   B 83  ? 0.26525 0.16834 0.17867 -0.00196 -0.05312 0.01662  86  TRP   B CZ2  
3642 C  CZ3  . TRP   B 83  ? 0.28300 0.14210 0.16094 0.01237  -0.01655 0.03617  86  TRP   B CZ3  
3643 C  CH2  . TRP   B 83  ? 0.24587 0.16400 0.17613 0.01113  -0.03639 0.04104  86  TRP   B CH2  
3654 N  N    . GLY   B 84  ? 0.25259 0.15133 0.17856 0.04177  0.01830  0.02765  87  GLY   B N    
3655 C  CA   . GLY   B 84  ? 0.25759 0.15338 0.19053 0.04636  0.00255  0.01755  87  GLY   B CA   
3656 C  C    . GLY   B 84  ? 0.22519 0.16158 0.18008 0.03135  -0.00785 0.01343  87  GLY   B C    
3657 O  O    . GLY   B 84  ? 0.25663 0.18021 0.18060 0.04089  -0.00833 0.00044  87  GLY   B O    
3661 N  N    . ARG   B 85  ? 0.23223 0.19096 0.17813 0.02070  -0.00360 0.01329  88  ARG   B N    
3662 C  CA   . ARG   B 85  ? 0.24233 0.20135 0.17351 0.01947  0.00474  0.03519  88  ARG   B CA   
3663 C  C    . ARG   B 85  ? 0.25147 0.17468 0.17383 0.01957  0.02049  0.02135  88  ARG   B C    
3664 O  O    . ARG   B 85  ? 0.28421 0.17142 0.18360 0.02337  0.04281  0.01716  88  ARG   B O    
3665 C  CB   . ARG   B 85  ? 0.26637 0.27711 0.20989 -0.00363 0.00605  0.02869  88  ARG   B CB   
3666 C  CG   . ARG   B 85  ? 0.35020 0.37635 0.26486 -0.04799 0.00438  0.03124  88  ARG   B CG   
3667 C  CD   . ARG   B 85  ? 0.45170 0.45724 0.28120 -0.03254 0.05089  0.04136  88  ARG   B CD   
3668 N  NE   . ARG   B 85  ? 0.52066 0.51887 0.30917 -0.03374 0.10832  0.06954  88  ARG   B NE   
3669 C  CZ   . ARG   B 85  ? 0.59972 0.54073 0.32099 -0.04714 0.10379  0.05190  88  ARG   B CZ   
3670 N  NH1  . ARG   B 85  ? 0.60967 0.56095 0.31815 -0.00141 0.08685  0.01983  88  ARG   B NH1  
3671 N  NH2  . ARG   B 85  ? 0.61235 0.51871 0.33567 -0.09639 0.10403  0.06238  88  ARG   B NH2  
3685 N  N    . GLU   B 86  ? 0.26676 0.15690 0.18602 0.02478  0.01269  0.02346  89  GLU   B N    
3686 C  CA   . GLU   B 86  ? 0.25692 0.16745 0.20100 0.02373  0.00030  0.02938  89  GLU   B CA   
3687 C  C    . GLU   B 86  ? 0.23923 0.17942 0.22411 0.03116  0.04811  0.03536  89  GLU   B C    
3688 O  O    . GLU   B 86  ? 0.25274 0.20112 0.29595 0.02960  0.05737  0.02378  89  GLU   B O    
3689 C  CB   . GLU   B 86  ? 0.27338 0.20109 0.20658 0.02806  -0.01022 0.03133  89  GLU   B CB   
3690 C  CG   . GLU   B 86  ? 0.29826 0.21199 0.21309 -0.00500 -0.02104 0.03236  89  GLU   B CG   
3691 C  CD   . GLU   B 86  ? 0.27284 0.23058 0.19240 0.00434  0.01094  0.03364  89  GLU   B CD   
3692 O  OE1  . GLU   B 86  ? 0.31809 0.31161 0.19617 0.00412  -0.00275 0.04115  89  GLU   B OE1  
3693 O  OE2  . GLU   B 86  ? 0.27658 0.22098 0.19111 0.03664  0.00182  0.01965  89  GLU   B OE2  
3700 N  N    . GLU   B 87  ? 0.21808 0.16616 0.19863 0.02486  0.02327  0.04449  90  GLU   B N    
3701 C  CA   . GLU   B 87  ? 0.20700 0.16515 0.19204 0.00995  0.01220  0.03256  90  GLU   B CA   
3702 C  C    . GLU   B 87  ? 0.21920 0.17270 0.21248 0.00813  0.00448  0.06488  90  GLU   B C    
3703 O  O    . GLU   B 87  ? 0.22371 0.17730 0.20560 0.01980  0.00797  0.04789  90  GLU   B O    
3704 C  CB   . GLU   B 87  ? 0.23094 0.16311 0.19373 0.02555  0.00616  0.03766  90  GLU   B CB   
3705 C  CG   . GLU   B 87  ? 0.23042 0.21324 0.17530 0.03897  0.01380  0.02715  90  GLU   B CG   
3706 C  CD   . GLU   B 87  ? 0.23636 0.19994 0.18623 0.01972  0.00310  0.04201  90  GLU   B CD   
3707 O  OE1  . GLU   B 87  ? 0.25849 0.19463 0.22064 0.02150  0.00853  0.03344  90  GLU   B OE1  
3708 O  OE2  . GLU   B 87  ? 0.27108 0.21044 0.19322 0.01372  0.00976  0.03517  90  GLU   B OE2  
3715 N  N    . ILE   B 88  ? 0.23590 0.20434 0.19821 0.01352  0.01399  0.07075  91  ILE   B N    
3716 C  CA   . ILE   B 88  ? 0.23757 0.20205 0.20603 0.02455  -0.00325 0.06508  91  ILE   B CA   
3717 C  C    . ILE   B 88  ? 0.23102 0.21053 0.23646 -0.00651 0.00745  0.06385  91  ILE   B C    
3718 O  O    . ILE   B 88  ? 0.23966 0.21666 0.29790 0.00601  0.01015  0.08406  91  ILE   B O    
3719 C  CB   . ILE   B 88  ? 0.28292 0.21776 0.22042 0.02347  -0.01022 0.04469  91  ILE   B CB   
3720 C  CG1  . ILE   B 88  ? 0.31412 0.23232 0.24641 0.03946  -0.01206 0.02842  91  ILE   B CG1  
3721 C  CG2  . ILE   B 88  ? 0.31816 0.26328 0.22793 0.04645  -0.01869 0.07503  91  ILE   B CG2  
3722 C  CD1  . ILE   B 88  ? 0.39064 0.26632 0.25812 0.06094  -0.03989 -0.00498 91  ILE   B CD1  
3734 N  N    . THR   B 89  ? 0.21505 0.18116 0.22812 0.00074  0.00488  0.06093  92  THR   B N    
3735 C  CA   . THR   B 89  ? 0.23578 0.20624 0.23394 0.02283  0.02054  0.06974  92  THR   B CA   
3736 C  C    . THR   B 89  ? 0.21659 0.22311 0.23507 0.00715  0.03142  0.09217  92  THR   B C    
3737 O  O    . THR   B 89  ? 0.25241 0.22818 0.23242 -0.00167 0.02693  0.09696  92  THR   B O    
3738 C  CB   . THR   B 89  ? 0.27132 0.20429 0.22702 0.01564  0.01166  0.06034  92  THR   B CB   
3739 O  OG1  . THR   B 89  ? 0.30888 0.22177 0.22296 -0.00727 0.01855  0.03751  92  THR   B OG1  
3740 C  CG2  . THR   B 89  ? 0.28932 0.24173 0.26035 0.02631  0.02264  0.06634  92  THR   B CG2  
3748 N  N    . TYR   B 90  ? 0.23734 0.26423 0.23509 0.01099  0.03377  0.09723  93  TYR   B N    
3749 C  CA   . TYR   B 90  ? 0.25717 0.28242 0.22437 0.03330  0.06531  0.08242  93  TYR   B CA   
3750 C  C    . TYR   B 90  ? 0.27798 0.28746 0.23012 0.04867  0.06125  0.08810  93  TYR   B C    
3751 O  O    . TYR   B 90  ? 0.34742 0.31379 0.22043 0.08320  0.03500  0.07436  93  TYR   B O    
3752 C  CB   . TYR   B 90  ? 0.29812 0.28168 0.23174 0.05503  0.06373  0.08114  93  TYR   B CB   
3753 C  CG   . TYR   B 90  ? 0.29676 0.28921 0.25245 0.07620  0.07316  0.07741  93  TYR   B CG   
3754 C  CD1  . TYR   B 90  ? 0.31798 0.31316 0.27900 0.06991  0.06235  0.09350  93  TYR   B CD1  
3755 C  CD2  . TYR   B 90  ? 0.31875 0.29937 0.30577 0.07038  0.07075  0.08010  93  TYR   B CD2  
3756 C  CE1  . TYR   B 90  ? 0.33879 0.32553 0.30826 0.07692  0.05310  0.08231  93  TYR   B CE1  
3757 C  CE2  . TYR   B 90  ? 0.32267 0.28019 0.32153 0.07515  0.06420  0.07793  93  TYR   B CE2  
3758 C  CZ   . TYR   B 90  ? 0.36335 0.30706 0.32955 0.08013  0.03371  0.07338  93  TYR   B CZ   
3759 O  OH   . TYR   B 90  ? 0.37215 0.34645 0.35615 0.07050  0.03411  0.05816  93  TYR   B OH   
3769 N  N    . ASP   B 91  ? 0.29535 0.26543 0.25971 0.05487  0.07357  0.10566  94  ASP   B N    
3770 C  CA   . ASP   B 91  ? 0.27410 0.28031 0.29085 0.02033  0.06402  0.10889  94  ASP   B CA   
3771 C  C    . ASP   B 91  ? 0.25314 0.26572 0.25030 0.01941  0.06734  0.12531  94  ASP   B C    
3772 O  O    . ASP   B 91  ? 0.29743 0.34422 0.26730 -0.03111 0.06314  0.09752  94  ASP   B O    
3773 C  CB   . ASP   B 91  ? 0.30533 0.28594 0.35374 -0.01399 0.06892  0.09728  94  ASP   B CB   
3774 C  CG   . ASP   B 91  ? 0.37688 0.38568 0.40355 -0.03338 0.05191  0.09451  94  ASP   B CG   
3775 O  OD1  . ASP   B 91  ? 0.37200 0.42080 0.41770 -0.03121 0.10429  0.07618  94  ASP   B OD1  
3776 O  OD2  . ASP   B 91  ? 0.43099 0.44544 0.43883 -0.07559 0.02412  0.07250  94  ASP   B OD2  
3781 N  N    . THR   B 92  ? 0.27022 0.23454 0.24938 0.04798  0.06853  0.10656  95  THR   B N    
3782 C  CA   . THR   B 92  ? 0.25983 0.21872 0.25316 0.05690  0.07335  0.09598  95  THR   B CA   
3783 C  C    . THR   B 92  ? 0.30826 0.21331 0.28361 0.05575  0.10257  0.12225  95  THR   B C    
3784 O  O    . THR   B 92  ? 0.30125 0.25483 0.28742 0.07576  0.10793  0.14291  95  THR   B O    
3785 C  CB   . THR   B 92  ? 0.27223 0.22494 0.22668 0.05736  0.06954  0.08643  95  THR   B CB   
3786 O  OG1  . THR   B 92  ? 0.27631 0.21053 0.22001 0.06583  0.07378  0.08746  95  THR   B OG1  
3787 C  CG2  . THR   B 92  ? 0.29534 0.25612 0.22426 0.03512  0.05422  0.09612  95  THR   B CG2  
3795 N  N    . PRO   B 93  ? 0.30311 0.19500 0.31946 0.06340  0.12228  0.11698  96  PRO   B N    
3796 C  CA   . PRO   B 93  ? 0.30799 0.21664 0.34602 0.07868  0.10809  0.13616  96  PRO   B CA   
3797 C  C    . PRO   B 93  ? 0.29185 0.23396 0.36435 0.08128  0.08978  0.15141  96  PRO   B C    
3798 O  O    . PRO   B 93  ? 0.29728 0.26396 0.45225 0.08171  0.07499  0.17726  96  PRO   B O    
3799 C  CB   . PRO   B 93  ? 0.31569 0.21811 0.37487 0.07009  0.13504  0.07884  96  PRO   B CB   
3800 C  CG   . PRO   B 93  ? 0.32954 0.21509 0.37523 0.05594  0.13721  0.05515  96  PRO   B CG   
3801 C  CD   . PRO   B 93  ? 0.32198 0.21419 0.33076 0.04499  0.13208  0.08373  96  PRO   B CD   
3809 N  N    . PHE   B 94  ? 0.29847 0.22599 0.27362 0.08158  0.09606  0.12946  97  PHE   B N    
3810 C  CA   . PHE   B 94  ? 0.28329 0.25791 0.22595 0.09517  0.08958  0.12499  97  PHE   B CA   
3811 C  C    . PHE   B 94  ? 0.29276 0.31439 0.22595 0.11939  0.08948  0.13477  97  PHE   B C    
3812 O  O    . PHE   B 94  ? 0.31149 0.31708 0.24495 0.12052  0.09468  0.13373  97  PHE   B O    
3813 C  CB   . PHE   B 94  ? 0.27748 0.24307 0.19694 0.08502  0.05654  0.09275  97  PHE   B CB   
3814 C  CG   . PHE   B 94  ? 0.25839 0.20221 0.19541 0.07133  0.06009  0.10066  97  PHE   B CG   
3815 C  CD1  . PHE   B 94  ? 0.24926 0.23479 0.20553 0.07386  0.05521  0.09850  97  PHE   B CD1  
3816 C  CD2  . PHE   B 94  ? 0.23006 0.17787 0.18597 0.04168  0.05803  0.07527  97  PHE   B CD2  
3817 C  CE1  . PHE   B 94  ? 0.26159 0.22218 0.20337 0.06874  0.05349  0.10009  97  PHE   B CE1  
3818 C  CE2  . PHE   B 94  ? 0.23897 0.18466 0.19183 0.04001  0.04870  0.08587  97  PHE   B CE2  
3819 C  CZ   . PHE   B 94  ? 0.23208 0.18811 0.19580 0.04130  0.03979  0.08857  97  PHE   B CZ   
3829 N  N    . LYS   B 95  ? 0.30285 0.35286 0.22038 0.13524  0.08107  0.13579  98  LYS   B N    
3830 C  CA   . LYS   B 95  ? 0.37231 0.41553 0.23532 0.11758  0.06043  0.15437  98  LYS   B CA   
3831 C  C    . LYS   B 95  ? 0.36327 0.46547 0.20557 0.12702  0.03730  0.13216  98  LYS   B C    
3832 O  O    . LYS   B 95  ? 0.33746 0.46559 0.20937 0.14111  0.04822  0.13372  98  LYS   B O    
3833 C  CB   . LYS   B 95  ? 0.45132 0.43392 0.26519 0.10414  0.04073  0.17441  98  LYS   B CB   
3834 C  CG   . LYS   B 95  ? 0.53147 0.48978 0.31025 0.05909  0.04540  0.14630  98  LYS   B CG   
3835 C  CD   . LYS   B 95  ? 0.57468 0.54272 0.32362 0.04952  0.04792  0.13369  98  LYS   B CD   
3836 C  CE   . LYS   B 95  ? 0.62307 0.59638 0.33551 0.06703  0.04371  0.11849  98  LYS   B CE   
3837 N  NZ   . LYS   B 95  ? 0.64311 0.61113 0.32819 0.05775  0.07030  0.14697  98  LYS   B NZ   
3851 N  N    . ARG   B 96  ? 0.34182 0.49120 0.18210 0.11907  0.01730  0.10779  99  ARG   B N    
3852 C  CA   . ARG   B 96  ? 0.36906 0.50951 0.19209 0.14060  0.01580  0.10743  99  ARG   B CA   
3853 C  C    . ARG   B 96  ? 0.37983 0.52913 0.21820 0.17147  0.01730  0.11940  99  ARG   B C    
3854 O  O    . ARG   B 96  ? 0.41530 0.55634 0.22628 0.17766  0.04073  0.13091  99  ARG   B O    
3855 C  CB   . ARG   B 96  ? 0.38436 0.51174 0.17946 0.13937  0.01625  0.09035  99  ARG   B CB   
3856 C  CG   . ARG   B 96  ? 0.38920 0.52260 0.17966 0.12943  0.02827  0.09316  99  ARG   B CG   
3857 C  CD   . ARG   B 96  ? 0.37010 0.53581 0.18814 0.09952  0.01695  0.07774  99  ARG   B CD   
3858 N  NE   . ARG   B 96  ? 0.40240 0.54994 0.19151 0.11269  0.02043  0.08280  99  ARG   B NE   
3859 C  CZ   . ARG   B 96  ? 0.50806 0.57844 0.22650 0.14069  0.06302  0.13074  99  ARG   B CZ   
3860 N  NH1  . ARG   B 96  ? 0.57580 0.61221 0.27070 0.13638  0.09765  0.14347  99  ARG   B NH1  
3861 N  NH2  . ARG   B 96  ? 0.53877 0.60649 0.24488 0.18506  0.05444  0.12273  99  ARG   B NH2  
3875 N  N    . GLU   B 97  ? 0.38157 0.57621 0.21913 0.19796  0.01465  0.10288  100 GLU   B N    
3876 C  CA   . GLU   B 97  ? 0.44724 0.59216 0.25513 0.19874  -0.02679 0.11005  100 GLU   B CA   
3877 C  C    . GLU   B 97  ? 0.48334 0.59630 0.27488 0.22544  -0.01897 0.10488  100 GLU   B C    
3878 O  O    . GLU   B 97  ? 0.53473 0.64428 0.33903 0.25023  -0.05961 0.06399  100 GLU   B O    
3879 C  CB   . GLU   B 97  ? 0.47651 0.63582 0.29310 0.20515  -0.04538 0.12613  100 GLU   B CB   
3880 C  CG   . GLU   B 97  ? 0.53548 0.68698 0.32665 0.19522  -0.04866 0.12475  100 GLU   B CG   
3881 C  CD   . GLU   B 97  ? 0.60284 0.73601 0.37167 0.15588  -0.04316 0.10313  100 GLU   B CD   
3882 O  OE1  . GLU   B 97  ? 0.62773 0.75588 0.40997 0.14654  -0.01872 0.08807  100 GLU   B OE1  
3883 O  OE2  . GLU   B 97  ? 0.60596 0.75630 0.36120 0.12711  -0.04786 0.10050  100 GLU   B OE2  
3890 N  N    . LYS   B 98  ? 0.44828 0.53333 0.24539 0.18129  0.00356  0.13111  101 LYS   B N    
3891 C  CA   . LYS   B 98  ? 0.41612 0.47953 0.24250 0.15073  0.00800  0.14315  101 LYS   B CA   
3892 C  C    . LYS   B 98  ? 0.35008 0.47777 0.22515 0.18723  0.04004  0.12381  101 LYS   B C    
3893 O  O    . LYS   B 98  ? 0.33847 0.50782 0.21316 0.19438  0.04048  0.11313  101 LYS   B O    
3894 C  CB   . LYS   B 98  ? 0.44128 0.51704 0.23692 0.11830  0.06159  0.15673  101 LYS   B CB   
3895 C  CG   . LYS   B 98  ? 0.42490 0.56999 0.25913 0.01355  0.09342  0.16306  101 LYS   B CG   
3896 C  CD   . LYS   B 98  ? 0.47656 0.60069 0.29332 -0.05472 0.08547  0.14997  101 LYS   B CD   
3897 C  CE   . LYS   B 98  ? 0.48602 0.61840 0.32665 -0.09766 0.09061  0.15092  101 LYS   B CE   
3898 N  NZ   . LYS   B 98  ? 0.53166 0.63001 0.34380 -0.08698 0.05570  0.15675  101 LYS   B NZ   
3912 N  N    . SER   B 99  ? 0.38753 0.44052 0.21372 0.17655  0.03239  0.11471  102 SER   B N    
3913 C  CA   . SER   B 99  ? 0.35987 0.42164 0.20563 0.17482  0.06342  0.11736  102 SER   B CA   
3914 C  C    . SER   B 99  ? 0.32500 0.36365 0.23660 0.12412  0.07622  0.14840  102 SER   B C    
3915 O  O    . SER   B 99  ? 0.37420 0.42146 0.28846 0.12613  0.09068  0.18313  102 SER   B O    
3916 C  CB   . SER   B 99  ? 0.37414 0.49344 0.21334 0.22006  0.03876  0.09644  102 SER   B CB   
3917 O  OG   . SER   B 99  ? 0.43373 0.54261 0.24180 0.24254  0.01397  0.09269  102 SER   B OG   
3923 N  N    . PHE   B 100 ? 0.29025 0.27746 0.18832 0.10491  0.05797  0.11199  103 PHE   B N    
3924 C  CA   . PHE   B 100 ? 0.25320 0.20579 0.22797 0.05124  0.05942  0.09848  103 PHE   B CA   
3925 C  C    . PHE   B 100 ? 0.20675 0.20550 0.21073 0.03817  0.05462  0.09928  103 PHE   B C    
3926 O  O    . PHE   B 100 ? 0.20469 0.20518 0.18203 0.02666  0.02127  0.07365  103 PHE   B O    
3927 C  CB   . PHE   B 100 ? 0.23930 0.19604 0.24871 0.03952  0.05631  0.07945  103 PHE   B CB   
3928 C  CG   . PHE   B 100 ? 0.20228 0.19795 0.20072 0.02930  0.02355  0.06525  103 PHE   B CG   
3929 C  CD1  . PHE   B 100 ? 0.20857 0.18024 0.17232 0.00159  -0.00695 0.05103  103 PHE   B CD1  
3930 C  CD2  . PHE   B 100 ? 0.21702 0.23101 0.17437 0.04465  0.03098  0.06321  103 PHE   B CD2  
3931 C  CE1  . PHE   B 100 ? 0.20961 0.18089 0.13509 -0.00073 -0.01659 0.03678  103 PHE   B CE1  
3932 C  CE2  . PHE   B 100 ? 0.22561 0.23400 0.13957 0.03686  -0.01664 0.01387  103 PHE   B CE2  
3933 C  CZ   . PHE   B 100 ? 0.20918 0.21336 0.14008 0.01591  -0.00960 0.03084  103 PHE   B CZ   
3943 N  N    . GLU   B 101 ? 0.18647 0.24790 0.23689 0.00125  0.00230  0.12775  104 GLU   B N    
3944 C  CA   . GLU   B 101 ? 0.18320 0.25389 0.23329 0.00029  -0.01397 0.13454  104 GLU   B CA   
3945 C  C    . GLU   B 101 ? 0.17594 0.25409 0.22990 -0.01869 -0.01035 0.12055  104 GLU   B C    
3946 O  O    . GLU   B 101 ? 0.19724 0.26715 0.31298 -0.01321 -0.02102 0.17141  104 GLU   B O    
3947 C  CB   . GLU   B 101 ? 0.23145 0.26198 0.25477 0.00208  -0.04062 0.10958  104 GLU   B CB   
3948 C  CG   . GLU   B 101 ? 0.29115 0.29044 0.27225 -0.01875 -0.07031 0.07797  104 GLU   B CG   
3949 C  CD   . GLU   B 101 ? 0.43086 0.35709 0.36258 -0.02906 -0.08162 0.02220  104 GLU   B CD   
3950 O  OE1  . GLU   B 101 ? 0.53972 0.37792 0.40266 -0.03522 -0.09819 -0.00285 104 GLU   B OE1  
3951 O  OE2  . GLU   B 101 ? 0.48192 0.39894 0.39561 0.02637  -0.06884 -0.01908 104 GLU   B OE2  
3958 N  N    . ILE   B 102 ? 0.16447 0.19267 0.15596 -0.00904 -0.00957 0.07405  105 ILE   B N    
3959 C  CA   . ILE   B 102 ? 0.16445 0.19330 0.14609 -0.01791 -0.00874 0.06846  105 ILE   B CA   
3960 C  C    . ILE   B 102 ? 0.17439 0.16552 0.13810 -0.00503 -0.00435 0.04832  105 ILE   B C    
3961 O  O    . ILE   B 102 ? 0.17240 0.19717 0.13682 -0.02306 -0.00039 0.03840  105 ILE   B O    
3962 C  CB   . ILE   B 102 ? 0.18197 0.18026 0.14810 -0.00952 -0.00268 0.05408  105 ILE   B CB   
3963 C  CG1  . ILE   B 102 ? 0.19743 0.20474 0.14685 0.00029  0.00808  0.04069  105 ILE   B CG1  
3964 C  CG2  . ILE   B 102 ? 0.21041 0.19368 0.18427 0.01807  -0.03972 0.02689  105 ILE   B CG2  
3965 C  CD1  . ILE   B 102 ? 0.21730 0.21168 0.15090 -0.01098 0.00135  0.03032  105 ILE   B CD1  
3977 N  N    . VAL   B 103 ? 0.16374 0.18019 0.13977 -0.00775 0.00569  0.04908  106 VAL   B N    
3978 C  CA   . VAL   B 103 ? 0.16854 0.16690 0.15413 -0.00512 -0.00017 0.04639  106 VAL   B CA   
3979 C  C    . VAL   B 103 ? 0.16723 0.15268 0.14398 -0.01587 -0.00842 0.05543  106 VAL   B C    
3980 O  O    . VAL   B 103 ? 0.17739 0.15735 0.16799 -0.00932 0.00049  0.06074  106 VAL   B O    
3981 C  CB   . VAL   B 103 ? 0.18151 0.16875 0.17531 -0.00353 -0.00007 0.04277  106 VAL   B CB   
3982 C  CG1  . VAL   B 103 ? 0.20103 0.17673 0.20526 0.00273  -0.00965 0.02519  106 VAL   B CG1  
3983 C  CG2  . VAL   B 103 ? 0.20087 0.17567 0.19164 0.02138  0.00731  0.04206  106 VAL   B CG2  
3993 N  N    . ILE   B 104 ? 0.16401 0.15787 0.13471 -0.01050 -0.00878 0.03993  107 ILE   B N    
3994 C  CA   . ILE   B 104 ? 0.16276 0.15260 0.13204 -0.00638 -0.01050 0.03178  107 ILE   B CA   
3995 C  C    . ILE   B 104 ? 0.16702 0.13940 0.13416 -0.01319 -0.01378 0.03349  107 ILE   B C    
3996 O  O    . ILE   B 104 ? 0.17582 0.18049 0.13165 -0.02665 -0.00749 0.01937  107 ILE   B O    
3997 C  CB   . ILE   B 104 ? 0.18498 0.15466 0.13302 -0.00681 -0.00607 0.04607  107 ILE   B CB   
3998 C  CG1  . ILE   B 104 ? 0.20040 0.17285 0.14364 -0.01465 -0.00918 0.03533  107 ILE   B CG1  
3999 C  CG2  . ILE   B 104 ? 0.20768 0.16390 0.14856 0.00051  -0.00880 0.03304  107 ILE   B CG2  
4000 C  CD1  . ILE   B 104 ? 0.23489 0.16636 0.16824 -0.03263 -0.01179 0.01513  107 ILE   B CD1  
4012 N  N    . MET   B 105 ? 0.17200 0.14877 0.14412 -0.01014 -0.01747 0.02595  108 MET   B N    
4013 C  CA   A MET   B 105 ? 0.17300 0.14690 0.16550 0.00074  -0.02092 0.00756  108 MET   B CA   
4014 C  CA   B MET   B 105 ? 0.17248 0.14907 0.17093 -0.01020 -0.02865 0.01687  108 MET   B CA   
4015 C  C    . MET   B 105 ? 0.17526 0.13877 0.15489 -0.00391 -0.01249 0.01153  108 MET   B C    
4016 O  O    . MET   B 105 ? 0.17977 0.16155 0.16807 0.00554  -0.01363 0.03255  108 MET   B O    
4017 C  CB   A MET   B 105 ? 0.18352 0.13963 0.20834 0.00159  -0.02261 -0.00091 108 MET   B CB   
4018 C  CB   B MET   B 105 ? 0.17662 0.15556 0.22208 -0.02639 -0.04433 0.02141  108 MET   B CB   
4019 C  CG   A MET   B 105 ? 0.20472 0.15164 0.24804 -0.00279 -0.00169 -0.01681 108 MET   B CG   
4020 C  CG   B MET   B 105 ? 0.17789 0.18423 0.27994 -0.02455 -0.05385 0.02889  108 MET   B CG   
4021 S  SD   A MET   B 105 ? 0.24449 0.17267 0.26682 -0.01845 0.03028  -0.03156 108 MET   B SD   
4022 S  SD   B MET   B 105 ? 0.22702 0.17218 0.31563 -0.01874 0.00159  0.02050  108 MET   B SD   
4023 C  CE   A MET   B 105 ? 0.25794 0.17077 0.29334 -0.00963 0.01204  -0.05624 108 MET   B CE   
4024 C  CE   B MET   B 105 ? 0.26536 0.20634 0.31072 -0.02765 0.02348  0.03069  108 MET   B CE   
4041 N  N    . VAL   B 106 ? 0.17439 0.15137 0.14804 -0.00007 -0.01601 0.00504  109 VAL   B N    
4042 C  CA   . VAL   B 106 ? 0.21193 0.16406 0.15717 0.01369  -0.02659 0.01228  109 VAL   B CA   
4043 C  C    . VAL   B 106 ? 0.23037 0.19049 0.17011 0.04906  -0.04221 -0.03239 109 VAL   B C    
4044 O  O    . VAL   B 106 ? 0.25103 0.27364 0.19737 0.06727  -0.04220 -0.07441 109 VAL   B O    
4045 C  CB   . VAL   B 106 ? 0.23733 0.18931 0.18134 0.02076  0.01447  0.05716  109 VAL   B CB   
4046 C  CG1  . VAL   B 106 ? 0.29095 0.22727 0.21418 0.05070  -0.00166 0.08763  109 VAL   B CG1  
4047 C  CG2  . VAL   B 106 ? 0.23810 0.15692 0.22030 -0.02380 0.03916  0.04719  109 VAL   B CG2  
4057 N  N    . LEU   B 107 ? 0.22536 0.18675 0.21145 0.02244  -0.05124 -0.03983 110 LEU   B N    
4058 C  CA   . LEU   B 107 ? 0.25121 0.21537 0.26022 0.01927  -0.09735 -0.06199 110 LEU   B CA   
4059 C  C    . LEU   B 107 ? 0.27075 0.25595 0.23198 0.05352  -0.08058 -0.09397 110 LEU   B C    
4060 O  O    . LEU   B 107 ? 0.26931 0.23383 0.20255 0.05136  -0.07856 -0.05142 110 LEU   B O    
4061 C  CB   . LEU   B 107 ? 0.27257 0.19488 0.34147 0.00614  -0.08851 -0.05801 110 LEU   B CB   
4062 C  CG   . LEU   B 107 ? 0.34606 0.18732 0.41130 0.01299  -0.06707 -0.04366 110 LEU   B CG   
4063 C  CD1  . LEU   B 107 ? 0.38366 0.23486 0.46255 -0.03677 -0.05306 0.00034  110 LEU   B CD1  
4064 C  CD2  . LEU   B 107 ? 0.39427 0.24867 0.42484 0.03783  -0.09534 -0.02662 110 LEU   B CD2  
4076 N  N    . LYS   B 108 ? 0.27499 0.32841 0.23260 0.06687  -0.08950 -0.08630 111 LYS   B N    
4077 C  CA   . LYS   B 108 ? 0.31505 0.39420 0.20451 0.04660  -0.11093 -0.08798 111 LYS   B CA   
4078 C  C    . LYS   B 108 ? 0.25685 0.36005 0.19669 0.08163  -0.08692 -0.05153 111 LYS   B C    
4079 O  O    . LYS   B 108 ? 0.28505 0.31374 0.20096 0.06812  -0.06735 -0.02538 111 LYS   B O    
4080 C  CB   . LYS   B 108 ? 0.42815 0.43890 0.27341 0.04292  -0.07306 -0.14459 111 LYS   B CB   
4081 C  CG   . LYS   B 108 ? 0.51111 0.47630 0.33012 0.03400  -0.06092 -0.15058 111 LYS   B CG   
4082 C  CD   . LYS   B 108 ? 0.55301 0.51386 0.37964 0.03675  -0.05908 -0.12601 111 LYS   B CD   
4083 C  CE   . LYS   B 108 ? 0.58157 0.56558 0.42597 0.04606  -0.04361 -0.09109 111 LYS   B CE   
4084 N  NZ   . LYS   B 108 ? 0.59014 0.59441 0.44622 0.07460  -0.04233 -0.06730 111 LYS   B NZ   
4098 N  N    . ASP   B 109 ? 0.25782 0.31865 0.21695 0.05191  -0.08014 -0.07717 112 ASP   B N    
4099 C  CA   . ASP   B 109 ? 0.24286 0.32752 0.25450 0.04513  -0.07832 -0.07481 112 ASP   B CA   
4100 C  C    . ASP   B 109 ? 0.19813 0.22353 0.20913 0.01723  -0.04808 -0.02239 112 ASP   B C    
4101 O  O    . ASP   B 109 ? 0.18887 0.19928 0.20901 0.01375  -0.04233 -0.00296 112 ASP   B O    
4102 C  CB   . ASP   B 109 ? 0.26221 0.40847 0.34137 -0.01416 -0.09319 -0.11635 112 ASP   B CB   
4103 C  CG   . ASP   B 109 ? 0.26342 0.44589 0.42315 -0.08209 -0.07630 -0.12488 112 ASP   B CG   
4104 O  OD1  . ASP   B 109 ? 0.30899 0.43930 0.43011 -0.07681 -0.08143 -0.14733 112 ASP   B OD1  
4105 O  OD2  . ASP   B 109 ? 0.34630 0.47139 0.47959 -0.09339 -0.00346 -0.11010 112 ASP   B OD2  
4110 N  N    . LYS   B 110 ? 0.19372 0.20383 0.19697 0.01985  -0.05135 -0.00110 113 LYS   B N    
4111 C  CA   . LYS   B 110 ? 0.18150 0.16897 0.19552 0.00165  -0.03829 0.00900  113 LYS   B CA   
4112 C  C    . LYS   B 110 ? 0.17971 0.13824 0.17991 -0.00283 -0.02522 0.01678  113 LYS   B C    
4113 O  O    . LYS   B 110 ? 0.19411 0.17060 0.17922 0.01730  -0.03165 -0.01218 113 LYS   B O    
4114 C  CB   . LYS   B 110 ? 0.18286 0.16139 0.23789 -0.00952 -0.01995 0.01744  113 LYS   B CB   
4115 C  CG   . LYS   B 110 ? 0.21572 0.15767 0.29234 -0.01752 -0.02196 0.00919  113 LYS   B CG   
4116 C  CD   . LYS   B 110 ? 0.30221 0.19819 0.35118 -0.05503 -0.04150 0.02245  113 LYS   B CD   
4117 C  CE   . LYS   B 110 ? 0.34036 0.28108 0.41198 -0.07894 -0.02186 0.04776  113 LYS   B CE   
4118 N  NZ   . LYS   B 110 ? 0.43627 0.36145 0.45776 -0.04178 -0.01256 0.03437  113 LYS   B NZ   
4132 N  N    . PHE   B 111 ? 0.17247 0.13171 0.16148 -0.00388 -0.02405 0.02216  114 PHE   B N    
4133 C  CA   . PHE   B 111 ? 0.17899 0.12534 0.14778 0.00147  -0.01451 0.02759  114 PHE   B CA   
4134 C  C    . PHE   B 111 ? 0.17079 0.12999 0.16466 0.00760  -0.01619 0.02211  114 PHE   B C    
4135 O  O    . PHE   B 111 ? 0.18750 0.15154 0.17530 0.01177  0.01052  0.03891  114 PHE   B O    
4136 C  CB   . PHE   B 111 ? 0.18052 0.13674 0.14852 -0.00855 -0.01448 0.03662  114 PHE   B CB   
4137 C  CG   . PHE   B 111 ? 0.17882 0.13137 0.14558 -0.01209 -0.02338 0.01107  114 PHE   B CG   
4138 C  CD1  . PHE   B 111 ? 0.18473 0.13376 0.16028 -0.01458 -0.02488 0.01764  114 PHE   B CD1  
4139 C  CD2  . PHE   B 111 ? 0.18188 0.13414 0.16646 0.00295  -0.03517 0.01402  114 PHE   B CD2  
4140 C  CE1  . PHE   B 111 ? 0.20087 0.12661 0.17461 -0.02787 -0.02262 0.03446  114 PHE   B CE1  
4141 C  CE2  . PHE   B 111 ? 0.21312 0.12897 0.15328 -0.01430 -0.03474 0.03317  114 PHE   B CE2  
4142 C  CZ   . PHE   B 111 ? 0.20703 0.13072 0.15769 -0.03097 -0.02975 0.03361  114 PHE   B CZ   
4152 N  N    A GLN   B 112 ? 0.16141 0.14938 0.17559 0.00975  -0.02969 0.05576  115 GLN   B N    
4153 N  N    B GLN   B 112 ? 0.17281 0.11517 0.17214 -0.00937 0.00013  -0.00008 115 GLN   B N    
4154 C  CA   A GLN   B 112 ? 0.18251 0.14559 0.19417 0.00856  -0.02736 0.07867  115 GLN   B CA   
4155 C  CA   B GLN   B 112 ? 0.19012 0.11432 0.20751 -0.01187 -0.00109 0.01569  115 GLN   B CA   
4156 C  C    A GLN   B 112 ? 0.16002 0.15544 0.17856 0.01684  -0.01666 0.08038  115 GLN   B C    
4157 C  C    B GLN   B 112 ? 0.17679 0.15858 0.19150 -0.00702 -0.01531 0.04112  115 GLN   B C    
4158 O  O    A GLN   B 112 ? 0.15496 0.21048 0.17318 0.02523  0.00266  0.07237  115 GLN   B O    
4159 O  O    B GLN   B 112 ? 0.17049 0.17919 0.19271 -0.00398 -0.00842 0.04393  115 GLN   B O    
4160 C  CB   A GLN   B 112 ? 0.19254 0.16632 0.23882 -0.01825 -0.01390 0.05674  115 GLN   B CB   
4161 C  CB   B GLN   B 112 ? 0.20285 0.12243 0.26532 0.00952  -0.00112 0.00001  115 GLN   B CB   
4162 C  CG   A GLN   B 112 ? 0.19782 0.15213 0.27605 -0.01572 -0.01187 0.05781  115 GLN   B CG   
4163 C  CG   B GLN   B 112 ? 0.26669 0.15490 0.30449 -0.00823 -0.00532 0.01337  115 GLN   B CG   
4164 C  CD   A GLN   B 112 ? 0.19942 0.14717 0.27787 0.00061  -0.01249 0.04391  115 GLN   B CD   
4165 C  CD   B GLN   B 112 ? 0.37160 0.20560 0.34816 -0.03073 -0.01058 0.00968  115 GLN   B CD   
4166 O  OE1  A GLN   B 112 ? 0.21897 0.15987 0.29675 -0.00307 -0.01534 0.05339  115 GLN   B OE1  
4167 O  OE1  B GLN   B 112 ? 0.40996 0.23314 0.36401 -0.05631 -0.01744 0.01494  115 GLN   B OE1  
4168 N  NE2  A GLN   B 112 ? 0.19138 0.16210 0.26986 -0.02124 -0.01900 0.00206  115 GLN   B NE2  
4169 N  NE2  B GLN   B 112 ? 0.43623 0.28021 0.37311 0.00946  0.00745  -0.01933 115 GLN   B NE2  
4186 N  N    . VAL   B 113 ? 0.16801 0.14665 0.17516 0.01113  0.00772  0.06397  116 VAL   B N    
4187 C  CA   . VAL   B 113 ? 0.15912 0.15029 0.16299 -0.00402 0.00508  0.04961  116 VAL   B CA   
4188 C  C    . VAL   B 113 ? 0.16612 0.15158 0.16409 -0.00780 0.00509  0.06489  116 VAL   B C    
4189 O  O    . VAL   B 113 ? 0.18060 0.17239 0.19985 0.00237  0.01979  0.08296  116 VAL   B O    
4190 C  CB   . VAL   B 113 ? 0.17453 0.15104 0.17974 0.00466  0.01254  0.04594  116 VAL   B CB   
4191 C  CG1  . VAL   B 113 ? 0.20495 0.17030 0.17322 -0.00249 0.00764  0.01085  116 VAL   B CG1  
4192 C  CG2  . VAL   B 113 ? 0.20783 0.13715 0.20164 0.00004  0.02928  0.05302  116 VAL   B CG2  
4202 N  N    . ALA   B 114 ? 0.16871 0.14708 0.16875 -0.00038 0.00144  0.05265  117 ALA   B N    
4203 C  CA   . ALA   B 114 ? 0.19012 0.15055 0.16874 0.01421  0.00502  0.05337  117 ALA   B CA   
4204 C  C    . ALA   B 114 ? 0.18846 0.18583 0.16700 0.00474  0.00186  0.07694  117 ALA   B C    
4205 O  O    . ALA   B 114 ? 0.18781 0.24200 0.17776 -0.01898 0.00080  0.09317  117 ALA   B O    
4206 C  CB   . ALA   B 114 ? 0.23752 0.16846 0.21311 0.04458  -0.01141 0.05127  117 ALA   B CB   
4212 N  N    . VAL   B 115 ? 0.18947 0.19441 0.18057 -0.01883 -0.00062 0.07487  118 VAL   B N    
4213 C  CA   . VAL   B 115 ? 0.19190 0.23597 0.18415 -0.02971 -0.01166 0.08469  118 VAL   B CA   
4214 C  C    . VAL   B 115 ? 0.19385 0.24775 0.22245 -0.02622 -0.02628 0.11866  118 VAL   B C    
4215 O  O    . VAL   B 115 ? 0.21802 0.23942 0.21534 -0.04021 -0.00547 0.11765  118 VAL   B O    
4216 C  CB   . VAL   B 115 ? 0.21646 0.27163 0.18015 -0.04313 -0.00332 0.07880  118 VAL   B CB   
4217 C  CG1  . VAL   B 115 ? 0.25252 0.35189 0.19680 -0.02606 -0.01728 0.06397  118 VAL   B CG1  
4218 C  CG2  . VAL   B 115 ? 0.26092 0.25059 0.19181 -0.05017 0.02570  0.05932  118 VAL   B CG2  
4228 N  N    . ASN   B 116 ? 0.19225 0.28362 0.27708 -0.01755 -0.02399 0.16727  119 ASN   B N    
4229 C  CA   A ASN   B 116 ? 0.22897 0.29974 0.29149 0.00569  -0.02610 0.17345  119 ASN   B CA   
4230 C  CA   B ASN   B 116 ? 0.22462 0.30691 0.30644 -0.00183 -0.03021 0.18042  119 ASN   B CA   
4231 C  C    . ASN   B 116 ? 0.21639 0.29016 0.32019 0.03907  0.00487  0.16951  119 ASN   B C    
4232 O  O    . ASN   B 116 ? 0.23864 0.26591 0.36244 0.02537  0.00683  0.17999  119 ASN   B O    
4233 C  CB   A ASN   B 116 ? 0.23782 0.34496 0.29113 -0.03604 -0.03578 0.17363  119 ASN   B CB   
4234 C  CB   B ASN   B 116 ? 0.23980 0.35817 0.33159 -0.04726 -0.05431 0.17716  119 ASN   B CB   
4235 C  CG   A ASN   B 116 ? 0.25620 0.34931 0.27083 -0.06182 -0.01785 0.17477  119 ASN   B CG   
4236 C  CG   B ASN   B 116 ? 0.28487 0.37718 0.34668 -0.06671 -0.06643 0.18212  119 ASN   B CG   
4237 O  OD1  A ASN   B 116 ? 0.28544 0.35293 0.30593 -0.08670 -0.04078 0.18516  119 ASN   B OD1  
4238 O  OD1  B ASN   B 116 ? 0.26451 0.38915 0.33773 -0.06357 -0.10386 0.19540  119 ASN   B OD1  
4239 N  ND2  A ASN   B 116 ? 0.27893 0.33664 0.22700 -0.06540 -0.03284 0.15170  119 ASN   B ND2  
4240 N  ND2  B ASN   B 116 ? 0.26754 0.34428 0.37896 -0.06738 -0.06219 0.15880  119 ASN   B ND2  
4251 N  N    . GLY   B 117 ? 0.22909 0.25829 0.29592 0.05795  0.04048  0.12476  120 GLY   B N    
4252 C  CA   . GLY   B 117 ? 0.30684 0.22962 0.29242 0.05156  0.06250  0.08221  120 GLY   B CA   
4253 C  C    . GLY   B 117 ? 0.29644 0.19148 0.29935 0.03197  0.05969  0.05524  120 GLY   B C    
4254 O  O    . GLY   B 117 ? 0.39802 0.22130 0.34723 0.03403  0.08106  0.01075  120 GLY   B O    
4258 N  N    . LYS   B 118 ? 0.23494 0.15562 0.25484 0.00918  0.02427  0.05918  121 LYS   B N    
4259 C  CA   A LYS   B 118 ? 0.23811 0.14999 0.24621 -0.00071 0.02269  0.05695  121 LYS   B CA   
4260 C  CA   B LYS   B 118 ? 0.22935 0.15612 0.23644 -0.00226 0.01655  0.06289  121 LYS   B CA   
4261 C  C    . LYS   B 118 ? 0.23314 0.13617 0.23911 -0.00198 0.01018  0.05293  121 LYS   B C    
4262 O  O    . LYS   B 118 ? 0.21650 0.15575 0.22915 -0.00379 0.00204  0.07316  121 LYS   B O    
4263 C  CB   A LYS   B 118 ? 0.21788 0.17514 0.25271 0.00545  0.01428  0.06188  121 LYS   B CB   
4264 C  CB   B LYS   B 118 ? 0.19993 0.18771 0.22096 -0.00368 -0.00338 0.07899  121 LYS   B CB   
4265 C  CG   A LYS   B 118 ? 0.26250 0.18998 0.27002 0.00534  0.00728  0.05564  121 LYS   B CG   
4266 C  CG   B LYS   B 118 ? 0.21254 0.20836 0.21263 -0.01324 -0.03098 0.09462  121 LYS   B CG   
4267 C  CD   A LYS   B 118 ? 0.30265 0.21247 0.27836 0.00037  0.00618  0.05966  121 LYS   B CD   
4268 C  CD   B LYS   B 118 ? 0.22782 0.23740 0.20498 -0.02125 -0.03127 0.11388  121 LYS   B CD   
4269 C  CE   A LYS   B 118 ? 0.33753 0.20066 0.29005 0.01650  -0.00965 0.03738  121 LYS   B CE   
4270 C  CE   B LYS   B 118 ? 0.23859 0.24594 0.21182 -0.02379 -0.04939 0.10236  121 LYS   B CE   
4271 N  NZ   A LYS   B 118 ? 0.33920 0.17834 0.28499 0.03286  -0.01536 0.04620  121 LYS   B NZ   
4272 N  NZ   B LYS   B 118 ? 0.23245 0.25107 0.19287 -0.02102 -0.04005 0.10990  121 LYS   B NZ   
4297 N  N    . HIS   B 119 ? 0.22838 0.15146 0.26633 -0.01305 -0.01704 0.05411  122 HIS   B N    
4298 C  CA   . HIS   B 119 ? 0.21326 0.12921 0.26679 0.00635  -0.00505 0.05852  122 HIS   B CA   
4299 C  C    . HIS   B 119 ? 0.19487 0.15157 0.25619 -0.00329 0.03571  0.08849  122 HIS   B C    
4300 O  O    . HIS   B 119 ? 0.25212 0.17112 0.28039 -0.00270 0.05777  0.11099  122 HIS   B O    
4301 C  CB   . HIS   B 119 ? 0.23410 0.17463 0.31831 -0.02764 -0.03764 0.06645  122 HIS   B CB   
4302 C  CG   . HIS   B 119 ? 0.22151 0.16892 0.35597 -0.03024 -0.02678 0.07935  122 HIS   B CG   
4303 N  ND1  . HIS   B 119 ? 0.26511 0.18819 0.35910 -0.01978 -0.04263 0.08120  122 HIS   B ND1  
4304 C  CD2  . HIS   B 119 ? 0.22934 0.22580 0.38016 -0.02523 -0.02590 0.07965  122 HIS   B CD2  
4305 C  CE1  . HIS   B 119 ? 0.25425 0.18825 0.37681 0.00880  -0.04214 0.08995  122 HIS   B CE1  
4306 N  NE2  . HIS   B 119 ? 0.23499 0.22369 0.38810 0.00201  -0.02251 0.08621  122 HIS   B NE2  
4314 N  N    . THR   B 120 ? 0.19514 0.14500 0.20656 -0.00637 0.01737  0.07378  123 THR   B N    
4315 C  CA   . THR   B 120 ? 0.20035 0.15095 0.20526 0.01095  0.01100  0.06873  123 THR   B CA   
4316 C  C    . THR   B 120 ? 0.18968 0.16768 0.20650 0.00288  0.01467  0.07188  123 THR   B C    
4317 O  O    . THR   B 120 ? 0.21031 0.19712 0.20837 0.00718  0.02680  0.08444  123 THR   B O    
4318 C  CB   . THR   B 120 ? 0.20587 0.17582 0.26568 0.02258  0.01024  0.03900  123 THR   B CB   
4319 O  OG1  . THR   B 120 ? 0.22729 0.22179 0.35079 0.03789  -0.02729 -0.03190 123 THR   B OG1  
4320 C  CG2  . THR   B 120 ? 0.22314 0.18829 0.26064 0.03592  0.00239  0.00941  123 THR   B CG2  
4328 N  N    . LEU   B 121 ? 0.19606 0.14223 0.20071 0.01140  0.01567  0.06450  124 LEU   B N    
4329 C  CA   . LEU   B 121 ? 0.19322 0.14951 0.20157 0.00331  0.02414  0.05885  124 LEU   B CA   
4330 C  C    . LEU   B 121 ? 0.17606 0.13566 0.19909 0.00023  0.01863  0.05018  124 LEU   B C    
4331 O  O    . LEU   B 121 ? 0.17713 0.15111 0.20237 0.01478  0.01001  0.05511  124 LEU   B O    
4332 C  CB   . LEU   B 121 ? 0.20116 0.16266 0.19513 0.01806  0.02931  0.05627  124 LEU   B CB   
4333 C  CG   . LEU   B 121 ? 0.20191 0.16114 0.19720 0.01793  0.02299  0.05331  124 LEU   B CG   
4334 C  CD1  . LEU   B 121 ? 0.21784 0.15413 0.21597 0.00509  0.03877  0.06036  124 LEU   B CD1  
4335 C  CD2  . LEU   B 121 ? 0.21434 0.16675 0.20683 0.01288  0.01393  0.02977  124 LEU   B CD2  
4347 N  N    . LEU   B 122 ? 0.18087 0.13993 0.20403 0.00846  0.01905  0.06386  125 LEU   B N    
4348 C  CA   . LEU   B 122 ? 0.17757 0.14672 0.20471 -0.00114 -0.00496 0.04100  125 LEU   B CA   
4349 C  C    . LEU   B 122 ? 0.20316 0.13014 0.17441 -0.00262 0.00102  0.04448  125 LEU   B C    
4350 O  O    . LEU   B 122 ? 0.23520 0.16790 0.18726 0.02234  0.03380  0.04275  125 LEU   B O    
4351 C  CB   . LEU   B 122 ? 0.20177 0.15710 0.24509 -0.01244 0.00708  0.04992  125 LEU   B CB   
4352 C  CG   . LEU   B 122 ? 0.20088 0.15861 0.28161 -0.02273 -0.00923 0.03330  125 LEU   B CG   
4353 C  CD1  . LEU   B 122 ? 0.22258 0.21522 0.31298 -0.04554 -0.01967 0.02507  125 LEU   B CD1  
4354 C  CD2  . LEU   B 122 ? 0.23590 0.15564 0.30847 -0.02130 -0.00623 0.01971  125 LEU   B CD2  
4366 N  N    . TYR   B 123 ? 0.19255 0.11933 0.17187 0.00436  0.00046  0.03341  126 TYR   B N    
4367 C  CA   . TYR   B 123 ? 0.18793 0.13622 0.18082 0.01464  -0.00261 0.04603  126 TYR   B CA   
4368 C  C    . TYR   B 123 ? 0.17695 0.13506 0.17825 0.00968  -0.01191 0.03051  126 TYR   B C    
4369 O  O    . TYR   B 123 ? 0.18234 0.13878 0.17081 0.00930  -0.00986 0.02558  126 TYR   B O    
4370 C  CB   . TYR   B 123 ? 0.18613 0.13419 0.15995 0.01742  -0.00155 0.03652  126 TYR   B CB   
4371 C  CG   . TYR   B 123 ? 0.19002 0.13290 0.15339 0.01061  -0.00234 0.04218  126 TYR   B CG   
4372 C  CD1  . TYR   B 123 ? 0.19751 0.14887 0.15650 0.01374  0.00611  0.04036  126 TYR   B CD1  
4373 C  CD2  . TYR   B 123 ? 0.21600 0.14134 0.14027 0.01409  -0.00283 0.01978  126 TYR   B CD2  
4374 C  CE1  . TYR   B 123 ? 0.20799 0.14740 0.16294 0.01600  -0.00115 0.02836  126 TYR   B CE1  
4375 C  CE2  . TYR   B 123 ? 0.21693 0.13903 0.15935 0.01931  -0.00392 0.02906  126 TYR   B CE2  
4376 C  CZ   . TYR   B 123 ? 0.18062 0.13437 0.16166 0.02628  -0.00180 0.02999  126 TYR   B CZ   
4377 O  OH   . TYR   B 123 ? 0.20983 0.13800 0.16534 0.01981  0.00541  0.02552  126 TYR   B OH   
4387 N  N    . GLY   B 124 ? 0.17117 0.16004 0.18784 0.00997  -0.00678 0.03912  127 GLY   B N    
4388 C  CA   . GLY   B 124 ? 0.19002 0.14850 0.18899 0.00181  -0.00741 0.02775  127 GLY   B CA   
4389 C  C    . GLY   B 124 ? 0.17968 0.14517 0.16384 0.00955  -0.01467 0.02788  127 GLY   B C    
4390 O  O    . GLY   B 124 ? 0.19835 0.15131 0.16248 0.00128  -0.01333 0.03491  127 GLY   B O    
4394 N  N    . HIS   B 125 ? 0.17401 0.15983 0.15459 0.00195  -0.01799 0.02450  128 HIS   B N    
4395 C  CA   . HIS   B 125 ? 0.17795 0.14534 0.15777 0.00182  -0.01863 0.02797  128 HIS   B CA   
4396 C  C    . HIS   B 125 ? 0.17842 0.15830 0.16194 -0.00397 -0.03160 0.04368  128 HIS   B C    
4397 O  O    . HIS   B 125 ? 0.18540 0.14548 0.17448 0.00767  -0.02458 0.02431  128 HIS   B O    
4398 C  CB   . HIS   B 125 ? 0.19029 0.14874 0.15924 -0.00034 -0.02557 0.03013  128 HIS   B CB   
4399 C  CG   . HIS   B 125 ? 0.18523 0.15550 0.15351 0.00627  -0.02279 0.02164  128 HIS   B CG   
4400 N  ND1  . HIS   B 125 ? 0.19960 0.13948 0.18061 0.00181  -0.02793 0.02322  128 HIS   B ND1  
4401 C  CD2  . HIS   B 125 ? 0.20832 0.17245 0.17141 0.01895  -0.03181 -0.00568 128 HIS   B CD2  
4402 C  CE1  . HIS   B 125 ? 0.19199 0.14488 0.18160 0.00330  -0.03329 0.01415  128 HIS   B CE1  
4403 N  NE2  . HIS   B 125 ? 0.21237 0.17605 0.18371 0.02535  -0.03012 0.00110  128 HIS   B NE2  
4411 N  N    . ARG   B 126 ? 0.17849 0.14659 0.15101 -0.00770 -0.01862 0.02730  129 ARG   B N    
4412 C  CA   . ARG   B 126 ? 0.19869 0.13796 0.14632 0.00783  -0.03154 0.02800  129 ARG   B CA   
4413 C  C    . ARG   B 126 ? 0.21194 0.15234 0.14730 0.01895  -0.03361 0.01713  129 ARG   B C    
4414 O  O    . ARG   B 126 ? 0.22091 0.15696 0.15796 0.03200  -0.03462 0.03512  129 ARG   B O    
4415 C  CB   . ARG   B 126 ? 0.20794 0.14457 0.15536 0.01141  -0.02241 0.03265  129 ARG   B CB   
4416 C  CG   . ARG   B 126 ? 0.19934 0.16504 0.16649 0.02196  -0.01761 0.02791  129 ARG   B CG   
4417 C  CD   . ARG   B 126 ? 0.21128 0.16328 0.15775 0.01857  -0.00882 0.02670  129 ARG   B CD   
4418 N  NE   . ARG   B 126 ? 0.20232 0.16292 0.16641 0.00511  -0.00872 0.02101  129 ARG   B NE   
4419 C  CZ   . ARG   B 126 ? 0.22046 0.15882 0.16750 0.02109  -0.00927 0.02691  129 ARG   B CZ   
4420 N  NH1  . ARG   B 126 ? 0.23406 0.16367 0.15771 0.02642  0.00902  0.02544  129 ARG   B NH1  
4421 N  NH2  . ARG   B 126 ? 0.24755 0.16735 0.17097 0.01514  0.00509  0.03529  129 ARG   B NH2  
4435 N  N    . ILE   B 127 ? 0.20874 0.14367 0.14966 0.00423  -0.02114 0.04050  130 ILE   B N    
4436 C  CA   . ILE   B 127 ? 0.22081 0.14347 0.14707 0.00457  -0.03100 0.02094  130 ILE   B CA   
4437 C  C    . ILE   B 127 ? 0.19570 0.15996 0.14413 0.00820  -0.02912 0.01952  130 ILE   B C    
4438 O  O    . ILE   B 127 ? 0.21238 0.14598 0.16329 0.01099  -0.02896 0.02768  130 ILE   B O    
4439 C  CB   . ILE   B 127 ? 0.21621 0.14913 0.15569 -0.00066 -0.01495 0.02152  130 ILE   B CB   
4440 C  CG1  . ILE   B 127 ? 0.23847 0.17369 0.15438 -0.00126 -0.02317 0.02118  130 ILE   B CG1  
4441 C  CG2  . ILE   B 127 ? 0.25575 0.19632 0.18564 -0.03967 -0.00259 -0.00181 130 ILE   B CG2  
4442 C  CD1  . ILE   B 127 ? 0.22697 0.14588 0.15412 0.01100  -0.01999 0.01410  130 ILE   B CD1  
4454 N  N    . GLY   B 128 ? 0.20687 0.17362 0.14100 0.01007  -0.03466 0.00694  131 GLY   B N    
4455 C  CA   . GLY   B 128 ? 0.21423 0.19630 0.15292 0.00591  -0.02557 0.00045  131 GLY   B CA   
4456 C  C    . GLY   B 128 ? 0.22509 0.16784 0.15531 -0.00296 -0.03915 0.00532  131 GLY   B C    
4457 O  O    . GLY   B 128 ? 0.22525 0.16235 0.16060 -0.00431 -0.02761 -0.00381 131 GLY   B O    
4461 N  N    . PRO   B 129 ? 0.21624 0.16221 0.16803 -0.00668 -0.03475 0.00052  132 PRO   B N    
4462 C  CA   . PRO   B 129 ? 0.21910 0.16676 0.17711 -0.00580 -0.03493 -0.00020 132 PRO   B CA   
4463 C  C    . PRO   B 129 ? 0.20682 0.17610 0.16169 -0.00904 -0.03307 -0.00765 132 PRO   B C    
4464 O  O    . PRO   B 129 ? 0.21928 0.17647 0.16478 -0.01434 -0.03076 0.00208  132 PRO   B O    
4465 C  CB   . PRO   B 129 ? 0.23551 0.19155 0.20214 -0.00129 -0.02068 0.00922  132 PRO   B CB   
4466 C  CG   . PRO   B 129 ? 0.26284 0.18713 0.21213 -0.02415 -0.00957 -0.00348 132 PRO   B CG   
4467 C  CD   . PRO   B 129 ? 0.22677 0.17189 0.20818 -0.01792 -0.00649 -0.00829 132 PRO   B CD   
4475 N  N    . GLU   B 130 ? 0.21544 0.21231 0.15893 -0.00806 -0.03445 -0.01081 133 GLU   B N    
4476 C  CA   . GLU   B 130 ? 0.22245 0.22450 0.14957 -0.01638 -0.03658 -0.00875 133 GLU   B CA   
4477 C  C    . GLU   B 130 ? 0.24607 0.22443 0.14581 -0.02363 -0.03331 0.02179  133 GLU   B C    
4478 O  O    . GLU   B 130 ? 0.27184 0.23978 0.15765 -0.02810 -0.01665 0.03733  133 GLU   B O    
4479 C  CB   . GLU   B 130 ? 0.25596 0.27571 0.16069 0.00203  -0.03126 0.00022  133 GLU   B CB   
4480 C  CG   . GLU   B 130 ? 0.26029 0.33017 0.16191 -0.00605 -0.02765 0.03295  133 GLU   B CG   
4481 C  CD   . GLU   B 130 ? 0.25653 0.33717 0.18460 -0.00809 -0.05149 0.01931  133 GLU   B CD   
4482 O  OE1  . GLU   B 130 ? 0.24608 0.35715 0.18506 -0.00208 -0.02787 -0.00310 133 GLU   B OE1  
4483 O  OE2  . GLU   B 130 ? 0.26981 0.34019 0.24428 0.02636  -0.05159 0.01572  133 GLU   B OE2  
4490 N  N    . LYS   B 131 ? 0.24784 0.19552 0.14680 -0.01921 -0.03233 0.02141  134 LYS   B N    
4491 C  CA   . LYS   B 131 ? 0.26638 0.18399 0.17486 -0.02897 -0.04279 0.04281  134 LYS   B CA   
4492 C  C    . LYS   B 131 ? 0.24268 0.14221 0.16908 -0.03098 -0.03714 0.03118  134 LYS   B C    
4493 O  O    . LYS   B 131 ? 0.28370 0.14281 0.19105 -0.03562 -0.03937 0.04759  134 LYS   B O    
4494 C  CB   . LYS   B 131 ? 0.31291 0.18994 0.24128 0.00348  -0.07407 0.02241  134 LYS   B CB   
4495 C  CG   . LYS   B 131 ? 0.39261 0.26789 0.28724 0.04171  -0.10858 0.05688  134 LYS   B CG   
4496 C  CD   . LYS   B 131 ? 0.46982 0.36804 0.29980 0.03323  -0.14268 0.09520  134 LYS   B CD   
4497 C  CE   . LYS   B 131 ? 0.54571 0.41032 0.34192 0.03834  -0.13205 0.09948  134 LYS   B CE   
4498 N  NZ   . LYS   B 131 ? 0.58127 0.45812 0.37471 0.01286  -0.11175 0.08510  134 LYS   B NZ   
4512 N  N    . ILE   B 132 ? 0.23997 0.14244 0.13274 -0.02049 -0.02194 0.02033  135 ILE   B N    
4513 C  CA   . ILE   B 132 ? 0.22716 0.14687 0.12274 -0.02207 -0.01873 0.01680  135 ILE   B CA   
4514 C  C    . ILE   B 132 ? 0.24413 0.14329 0.12734 -0.03988 -0.02865 0.00517  135 ILE   B C    
4515 O  O    . ILE   B 132 ? 0.25897 0.18246 0.18284 -0.05855 -0.00096 -0.03759 135 ILE   B O    
4516 C  CB   . ILE   B 132 ? 0.23642 0.13520 0.13114 -0.01910 -0.01579 0.00745  135 ILE   B CB   
4517 C  CG1  . ILE   B 132 ? 0.23793 0.14410 0.14703 -0.01941 -0.00528 0.00875  135 ILE   B CG1  
4518 C  CG2  . ILE   B 132 ? 0.28424 0.13197 0.11919 -0.01572 -0.02997 0.01708  135 ILE   B CG2  
4519 C  CD1  . ILE   B 132 ? 0.22947 0.14916 0.14310 -0.03326 -0.01386 0.02141  135 ILE   B CD1  
4531 N  N    . ASP   B 133 ? 0.23304 0.15668 0.11795 -0.02823 -0.01917 0.01540  136 ASP   B N    
4532 C  CA   . ASP   B 133 ? 0.23242 0.16366 0.12767 -0.02460 -0.00874 0.00798  136 ASP   B CA   
4533 C  C    . ASP   B 133 ? 0.22200 0.15585 0.13784 -0.02894 0.00538  0.01081  136 ASP   B C    
4534 O  O    . ASP   B 133 ? 0.23692 0.15440 0.14372 -0.01614 -0.00358 0.00990  136 ASP   B O    
4535 C  CB   . ASP   B 133 ? 0.25149 0.18471 0.14219 -0.02952 -0.00735 0.00981  136 ASP   B CB   
4536 C  CG   . ASP   B 133 ? 0.34745 0.18898 0.15176 -0.06222 0.02282  0.03636  136 ASP   B CG   
4537 O  OD1  . ASP   B 133 ? 0.29014 0.16192 0.15126 -0.03114 -0.01144 0.01720  136 ASP   B OD1  
4538 O  OD2  . ASP   B 133 ? 0.52243 0.21538 0.18395 -0.06006 0.04061  0.05083  136 ASP   B OD2  
4543 N  N    . THR   B 134 ? 0.21908 0.15218 0.13791 -0.02863 -0.00947 0.01068  137 THR   B N    
4544 C  CA   . THR   B 134 ? 0.22808 0.14854 0.13135 -0.03724 -0.03666 0.00961  137 THR   B CA   
4545 C  C    . THR   B 134 ? 0.22582 0.14518 0.12893 -0.02751 -0.03237 0.00805  137 THR   B C    
4546 O  O    . THR   B 134 ? 0.22044 0.17025 0.14051 -0.01777 -0.02547 0.02697  137 THR   B O    
4547 C  CB   . THR   B 134 ? 0.25781 0.15705 0.14125 -0.03922 -0.02709 0.01164  137 THR   B CB   
4548 O  OG1  . THR   B 134 ? 0.28265 0.15078 0.16793 -0.04396 -0.00914 0.01716  137 THR   B OG1  
4549 C  CG2  . THR   B 134 ? 0.26672 0.18250 0.15729 -0.03923 -0.03324 -0.00013 137 THR   B CG2  
4557 N  N    . LEU   B 135 ? 0.20363 0.15558 0.13621 -0.02558 -0.03069 0.01586  138 LEU   B N    
4558 C  CA   . LEU   B 135 ? 0.21539 0.15593 0.13257 -0.02341 -0.03252 0.02411  138 LEU   B CA   
4559 C  C    . LEU   B 135 ? 0.20906 0.16922 0.14613 -0.02210 -0.03885 0.01710  138 LEU   B C    
4560 O  O    . LEU   B 135 ? 0.22974 0.20649 0.15759 -0.03641 -0.04303 -0.00733 138 LEU   B O    
4561 C  CB   . LEU   B 135 ? 0.22931 0.18310 0.12527 -0.02934 -0.02363 0.01678  138 LEU   B CB   
4562 C  CG   . LEU   B 135 ? 0.23414 0.17355 0.15050 -0.01582 -0.02505 0.02110  138 LEU   B CG   
4563 C  CD1  . LEU   B 135 ? 0.23521 0.18352 0.17836 -0.02231 -0.01884 0.02781  138 LEU   B CD1  
4564 C  CD2  . LEU   B 135 ? 0.24306 0.19006 0.15243 -0.00578 -0.03749 0.03037  138 LEU   B CD2  
4576 N  N    . GLY   B 136 ? 0.20159 0.17771 0.12325 -0.02385 -0.03425 0.01512  139 GLY   B N    
4577 C  CA   . GLY   B 136 ? 0.23270 0.16063 0.12407 -0.02820 -0.04165 0.00958  139 GLY   B CA   
4578 C  C    . GLY   B 136 ? 0.22049 0.16828 0.12334 -0.02855 -0.03204 -0.00835 139 GLY   B C    
4579 O  O    . GLY   B 136 ? 0.22425 0.19350 0.13160 -0.03256 -0.03856 0.01526  139 GLY   B O    
4583 N  N    . ILE   B 137 ? 0.20840 0.17704 0.12562 -0.02784 -0.03638 0.00400  140 ILE   B N    
4584 C  CA   . ILE   B 137 ? 0.21447 0.17671 0.11705 -0.01266 -0.03089 0.00095  140 ILE   B CA   
4585 C  C    . ILE   B 137 ? 0.22429 0.18797 0.13650 -0.00494 -0.04031 -0.00233 140 ILE   B C    
4586 O  O    . ILE   B 137 ? 0.23580 0.21806 0.13939 -0.01647 -0.03588 -0.00774 140 ILE   B O    
4587 C  CB   . ILE   B 137 ? 0.22170 0.19196 0.11980 -0.00392 -0.02386 0.00230  140 ILE   B CB   
4588 C  CG1  . ILE   B 137 ? 0.23494 0.18595 0.12312 -0.00199 -0.03359 -0.00791 140 ILE   B CG1  
4589 C  CG2  . ILE   B 137 ? 0.23393 0.19384 0.13997 -0.01232 -0.03482 0.00096  140 ILE   B CG2  
4590 C  CD1  . ILE   B 137 ? 0.24342 0.20992 0.13764 -0.00693 -0.02637 -0.01299 140 ILE   B CD1  
4602 N  N    . TYR   B 138 ? 0.23661 0.19456 0.12864 -0.01367 -0.03482 -0.01189 141 TYR   B N    
4603 C  CA   . TYR   B 138 ? 0.25966 0.18798 0.12985 -0.03430 -0.03467 -0.01170 141 TYR   B CA   
4604 C  C    . TYR   B 138 ? 0.27630 0.21666 0.13079 -0.03028 -0.01732 -0.00671 141 TYR   B C    
4605 O  O    . TYR   B 138 ? 0.26014 0.21366 0.11734 -0.00645 -0.04134 0.00684  141 TYR   B O    
4606 C  CB   . TYR   B 138 ? 0.29376 0.20469 0.14341 -0.02085 -0.03708 -0.01191 141 TYR   B CB   
4607 C  CG   . TYR   B 138 ? 0.27142 0.20216 0.13121 -0.01264 -0.03560 0.00958  141 TYR   B CG   
4608 C  CD1  . TYR   B 138 ? 0.27833 0.28239 0.16252 -0.07427 -0.03707 0.01500  141 TYR   B CD1  
4609 C  CD2  . TYR   B 138 ? 0.27680 0.22349 0.14783 -0.03514 -0.05185 0.00726  141 TYR   B CD2  
4610 C  CE1  . TYR   B 138 ? 0.28430 0.28203 0.16957 -0.07363 -0.03362 0.01726  141 TYR   B CE1  
4611 C  CE2  . TYR   B 138 ? 0.26378 0.19232 0.15515 -0.03687 -0.03761 0.00862  141 TYR   B CE2  
4612 C  CZ   . TYR   B 138 ? 0.28853 0.21450 0.15263 -0.03692 -0.02884 0.00675  141 TYR   B CZ   
4613 O  OH   . TYR   B 138 ? 0.31476 0.22158 0.15648 -0.04867 -0.04249 0.03858  141 TYR   B OH   
4623 N  N    . GLY   B 139 ? 0.29659 0.23770 0.13122 -0.05275 -0.03656 -0.00890 142 GLY   B N    
4624 C  CA   . GLY   B 139 ? 0.29164 0.25802 0.13175 -0.02877 -0.03856 -0.00437 142 GLY   B CA   
4625 C  C    . GLY   B 139 ? 0.27712 0.29336 0.13079 -0.03036 -0.01806 -0.03755 142 GLY   B C    
4626 O  O    . GLY   B 139 ? 0.29706 0.33443 0.15791 -0.01356 -0.02296 -0.01541 142 GLY   B O    
4630 N  N    . LYS   B 140 ? 0.26602 0.24894 0.12717 0.01709  -0.02082 -0.01972 143 LYS   B N    
4631 C  CA   . LYS   B 140 ? 0.27321 0.28507 0.13008 0.01706  -0.02726 -0.04287 143 LYS   B CA   
4632 C  C    . LYS   B 140 ? 0.25141 0.28874 0.12665 0.01867  -0.01755 0.00144  143 LYS   B C    
4633 O  O    . LYS   B 140 ? 0.25259 0.28404 0.13518 0.03053  -0.00834 -0.00742 143 LYS   B O    
4634 C  CB   . LYS   B 140 ? 0.31800 0.29718 0.14319 0.03160  -0.05140 -0.03037 143 LYS   B CB   
4635 C  CG   . LYS   B 140 ? 0.42673 0.41313 0.20012 -0.02076 -0.01732 -0.04653 143 LYS   B CG   
4636 C  CD   . LYS   B 140 ? 0.49734 0.50035 0.29256 -0.03484 -0.02258 -0.01631 143 LYS   B CD   
4637 C  CE   . LYS   B 140 ? 0.54929 0.55303 0.36262 -0.04447 -0.01709 -0.03254 143 LYS   B CE   
4638 N  NZ   . LYS   B 140 ? 0.59928 0.57845 0.40610 -0.03150 -0.00673 -0.04588 143 LYS   B NZ   
4652 N  N    . VAL   B 141 ? 0.22596 0.29875 0.13128 0.00852  -0.02324 -0.02825 144 VAL   B N    
4653 C  CA   . VAL   B 141 ? 0.22590 0.29435 0.13130 0.01217  -0.03346 -0.03709 144 VAL   B CA   
4654 C  C    . VAL   B 141 ? 0.22033 0.29443 0.13672 -0.01270 -0.02754 -0.05611 144 VAL   B C    
4655 O  O    . VAL   B 141 ? 0.23994 0.30663 0.17034 0.00269  -0.02949 -0.04466 144 VAL   B O    
4656 C  CB   . VAL   B 141 ? 0.22088 0.25946 0.13721 0.01229  -0.03550 -0.00315 144 VAL   B CB   
4657 C  CG1  . VAL   B 141 ? 0.25960 0.25308 0.14013 0.01120  -0.04029 -0.01190 144 VAL   B CG1  
4658 C  CG2  . VAL   B 141 ? 0.23429 0.27476 0.15788 0.00971  -0.04388 -0.00902 144 VAL   B CG2  
4668 N  N    . ASN   B 142 ? 0.22294 0.31054 0.13426 0.01655  -0.04388 -0.04541 145 ASN   B N    
4669 C  CA   . ASN   B 142 ? 0.20426 0.32883 0.13379 0.02623  -0.03879 -0.06741 145 ASN   B CA   
4670 C  C    . ASN   B 142 ? 0.19462 0.30040 0.13416 0.00249  -0.02649 -0.03407 145 ASN   B C    
4671 O  O    . ASN   B 142 ? 0.23133 0.32693 0.11383 -0.01514 -0.02168 -0.01371 145 ASN   B O    
4672 C  CB   . ASN   B 142 ? 0.22911 0.35997 0.15682 0.03510  -0.07111 -0.07510 145 ASN   B CB   
4673 C  CG   . ASN   B 142 ? 0.25026 0.37931 0.17501 0.08380  -0.05982 -0.09670 145 ASN   B CG   
4674 O  OD1  . ASN   B 142 ? 0.23481 0.38723 0.21852 0.03292  -0.06589 -0.07998 145 ASN   B OD1  
4675 N  ND2  . ASN   B 142 ? 0.23709 0.41176 0.19493 0.04568  -0.07670 -0.10157 145 ASN   B ND2  
4682 N  N    . ILE   B 143 ? 0.18612 0.27430 0.14073 -0.00437 -0.02475 -0.02376 146 ILE   B N    
4683 C  CA   . ILE   B 143 ? 0.17933 0.24741 0.15424 -0.01460 -0.03742 -0.02006 146 ILE   B CA   
4684 C  C    . ILE   B 143 ? 0.18017 0.26870 0.15765 -0.00274 -0.04495 -0.01011 146 ILE   B C    
4685 O  O    . ILE   B 143 ? 0.19451 0.28371 0.20418 -0.01860 -0.00968 -0.02522 146 ILE   B O    
4686 C  CB   . ILE   B 143 ? 0.18790 0.23834 0.15059 -0.01570 -0.03584 0.00275  146 ILE   B CB   
4687 C  CG1  . ILE   B 143 ? 0.19440 0.24539 0.15191 -0.00161 -0.03718 -0.00745 146 ILE   B CG1  
4688 C  CG2  . ILE   B 143 ? 0.20523 0.24434 0.14485 -0.02169 -0.03700 -0.00368 146 ILE   B CG2  
4689 C  CD1  . ILE   B 143 ? 0.17918 0.25156 0.16315 -0.01293 -0.03531 -0.01910 146 ILE   B CD1  
4701 N  N    . HIS   B 144 ? 0.18492 0.26079 0.11104 0.00469  -0.01349 -0.01095 147 HIS   B N    
4702 C  CA   . HIS   B 144 ? 0.17442 0.27827 0.12192 0.01230  -0.01478 -0.01115 147 HIS   B CA   
4703 C  C    . HIS   B 144 ? 0.15781 0.25622 0.13409 0.00649  -0.01743 -0.00832 147 HIS   B C    
4704 O  O    . HIS   B 144 ? 0.16570 0.28606 0.13654 -0.00333 -0.01241 -0.02307 147 HIS   B O    
4705 C  CB   . HIS   B 144 ? 0.18754 0.30462 0.12433 0.02886  -0.00970 0.00293  147 HIS   B CB   
4706 C  CG   . HIS   B 144 ? 0.21341 0.34164 0.12739 0.02990  -0.01666 0.01225  147 HIS   B CG   
4707 N  ND1  . HIS   B 144 ? 0.23660 0.37593 0.14937 0.05553  -0.01490 -0.00190 147 HIS   B ND1  
4708 C  CD2  . HIS   B 144 ? 0.22362 0.34225 0.13171 0.04301  -0.02277 0.02403  147 HIS   B CD2  
4709 C  CE1  . HIS   B 144 ? 0.26290 0.37961 0.17450 0.05544  -0.00949 0.01979  147 HIS   B CE1  
4710 N  NE2  . HIS   B 144 ? 0.23676 0.38465 0.14792 0.07874  -0.02405 0.00458  147 HIS   B NE2  
4718 N  N    . SER   B 145 ? 0.16804 0.25274 0.11998 -0.00812 -0.00603 -0.00724 148 SER   B N    
4719 C  CA   . SER   B 145 ? 0.17428 0.24750 0.12172 -0.02214 0.00346  -0.00635 148 SER   B CA   
4720 C  C    . SER   B 145 ? 0.15799 0.24518 0.11829 -0.03034 -0.00388 0.00329  148 SER   B C    
4721 O  O    . SER   B 145 ? 0.17281 0.21243 0.10837 -0.02292 -0.00359 -0.00451 148 SER   B O    
4722 C  CB   . SER   B 145 ? 0.19045 0.24750 0.15449 0.00912  0.00349  0.01444  148 SER   B CB   
4723 O  OG   . SER   B 145 ? 0.23326 0.23889 0.19933 0.00020  0.01669  -0.00842 148 SER   B OG   
4729 N  N    . ILE   B 146 ? 0.16434 0.23880 0.10987 -0.02915 0.00233  0.00358  149 ILE   B N    
4730 C  CA   . ILE   B 146 ? 0.16073 0.24009 0.10881 -0.02772 0.00203  -0.00803 149 ILE   B CA   
4731 C  C    . ILE   B 146 ? 0.17911 0.24272 0.11095 -0.03635 0.00759  -0.01729 149 ILE   B C    
4732 O  O    . ILE   B 146 ? 0.18681 0.30666 0.12398 -0.06475 0.01988  -0.04433 149 ILE   B O    
4733 C  CB   . ILE   B 146 ? 0.19236 0.21960 0.11544 -0.02831 -0.00662 -0.00829 149 ILE   B CB   
4734 C  CG1  . ILE   B 146 ? 0.19940 0.23329 0.13690 -0.02530 -0.01267 -0.01506 149 ILE   B CG1  
4735 C  CG2  . ILE   B 146 ? 0.21917 0.22823 0.13963 -0.02621 -0.01106 -0.01785 149 ILE   B CG2  
4736 C  CD1  . ILE   B 146 ? 0.23114 0.25408 0.13342 -0.02382 -0.02609 -0.00499 149 ILE   B CD1  
4748 N  N    . GLY   B 147 ? 0.16692 0.22373 0.10321 -0.03434 0.00490  -0.01164 150 GLY   B N    
4749 C  CA   . GLY   B 147 ? 0.16984 0.22961 0.11037 -0.01855 -0.00050 -0.02233 150 GLY   B CA   
4750 C  C    . GLY   B 147 ? 0.17065 0.18988 0.10940 -0.02723 0.00607  -0.00159 150 GLY   B C    
4751 O  O    . GLY   B 147 ? 0.16942 0.21488 0.10573 -0.02765 0.00531  -0.00373 150 GLY   B O    
4755 N  N    . PHE   B 148 ? 0.16818 0.18625 0.10170 -0.02338 0.00184  -0.00659 151 PHE   B N    
4756 C  CA   . PHE   B 148 ? 0.17259 0.19749 0.10702 -0.02821 -0.00173 -0.00166 151 PHE   B CA   
4757 C  C    . PHE   B 148 ? 0.17235 0.19261 0.11479 -0.02692 -0.00659 -0.00379 151 PHE   B C    
4758 O  O    . PHE   B 148 ? 0.16897 0.21819 0.14931 -0.02090 0.00513  -0.02948 151 PHE   B O    
4759 C  CB   . PHE   B 148 ? 0.19839 0.20261 0.10511 -0.01930 -0.00631 -0.00361 151 PHE   B CB   
4760 C  CG   . PHE   B 148 ? 0.20166 0.20359 0.10586 -0.02407 0.00792  0.00133  151 PHE   B CG   
4761 C  CD1  . PHE   B 148 ? 0.20559 0.20227 0.13712 -0.02513 0.01131  -0.01026 151 PHE   B CD1  
4762 C  CD2  . PHE   B 148 ? 0.21841 0.19669 0.11546 -0.01679 0.00706  0.02194  151 PHE   B CD2  
4763 C  CE1  . PHE   B 148 ? 0.25692 0.19878 0.15737 -0.03931 0.01157  0.00665  151 PHE   B CE1  
4764 C  CE2  . PHE   B 148 ? 0.25772 0.18201 0.15016 0.00365  0.01907  0.03138  151 PHE   B CE2  
4765 C  CZ   . PHE   B 148 ? 0.27768 0.18465 0.15122 -0.02452 0.02714  0.01709  151 PHE   B CZ   
4775 N  N    . SER   B 149 ? 0.17721 0.21197 0.12301 -0.01938 -0.00814 -0.02980 152 SER   B N    
4776 C  CA   . SER   B 149 ? 0.18668 0.20672 0.15019 -0.00301 -0.02140 -0.03726 152 SER   B CA   
4777 C  C    . SER   B 149 ? 0.19805 0.18526 0.15474 -0.00793 -0.01900 -0.03300 152 SER   B C    
4778 O  O    . SER   B 149 ? 0.19030 0.22350 0.15618 0.00186  -0.03114 -0.02496 152 SER   B O    
4779 C  CB   . SER   B 149 ? 0.24557 0.19861 0.20253 -0.01640 -0.03576 -0.05290 152 SER   B CB   
4780 O  OG   . SER   B 149 ? 0.35081 0.21703 0.25250 -0.03594 -0.02869 -0.05286 152 SER   B OG   
4786 N  N    . PHE   B 150 ? 0.22045 0.18439 0.16598 -0.03414 -0.02868 -0.01815 153 PHE   B N    
4787 C  CA   . PHE   B 150 ? 0.24481 0.20536 0.16943 -0.01134 -0.04393 -0.02228 153 PHE   B CA   
4788 C  C    . PHE   B 150 ? 0.28361 0.23403 0.20021 0.03822  -0.06181 -0.04316 153 PHE   B C    
4789 O  O    . PHE   B 150 ? 0.34435 0.25168 0.26141 0.03841  -0.10890 -0.06963 153 PHE   B O    
4790 C  CB   . PHE   B 150 ? 0.26810 0.19995 0.14422 -0.00933 -0.02132 -0.01355 153 PHE   B CB   
4791 C  CG   . PHE   B 150 ? 0.25469 0.17620 0.13424 -0.01040 -0.00636 0.00372  153 PHE   B CG   
4792 C  CD1  . PHE   B 150 ? 0.27083 0.18201 0.15012 -0.02096 0.00975  0.00156  153 PHE   B CD1  
4793 C  CD2  . PHE   B 150 ? 0.26426 0.17819 0.13011 -0.01929 0.00135  0.00839  153 PHE   B CD2  
4794 C  CE1  . PHE   B 150 ? 0.28448 0.16966 0.15845 -0.00727 0.01268  0.01553  153 PHE   B CE1  
4795 C  CE2  . PHE   B 150 ? 0.27381 0.17634 0.13797 -0.02482 0.00946  0.01075  153 PHE   B CE2  
4796 C  CZ   . PHE   B 150 ? 0.27748 0.17080 0.14217 -0.02167 0.01889  0.00188  153 PHE   B CZ   
4806 N  N    . SER   B 151 ? 0.29867 0.26642 0.27986 0.02661  -0.07941 -0.08720 154 SER   B N    
4807 C  CA   A SER   B 151 ? 0.35279 0.32578 0.30315 -0.00610 -0.07004 -0.06993 154 SER   B CA   
4808 C  CA   B SER   B 151 ? 0.31774 0.32215 0.29054 -0.00399 -0.09379 -0.08322 154 SER   B CA   
4809 C  C    . SER   B 151 ? 0.43309 0.40371 0.32946 -0.01561 -0.06222 -0.06061 154 SER   B C    
4810 O  O    . SER   B 151 ? 0.43953 0.39821 0.34942 0.01109  -0.03778 -0.03984 154 SER   B O    
4811 C  CB   A SER   B 151 ? 0.33785 0.30986 0.30383 -0.02604 -0.04220 -0.05749 154 SER   B CB   
4812 C  CB   B SER   B 151 ? 0.25644 0.32630 0.27878 -0.02672 -0.07370 -0.10267 154 SER   B CB   
4813 O  OG   A SER   B 151 ? 0.34363 0.26148 0.30288 -0.02594 -0.01787 -0.03525 154 SER   B OG   
4814 O  OG   B SER   B 151 ? 0.28881 0.31922 0.26702 -0.02505 -0.04002 -0.08764 154 SER   B OG   
4823 N  N    . SER   B 152 ? 0.56907 0.53399 0.39137 -0.05906 -0.03757 -0.02141 155 SER   B N    
4824 C  CA   . SER   B 152 ? 0.67091 0.61084 0.43426 -0.10551 -0.03978 -0.03184 155 SER   B CA   
4825 C  C    . SER   B 152 ? 0.72669 0.64765 0.48113 -0.09849 -0.03469 -0.02610 155 SER   B C    
4826 O  O    . SER   B 152 ? 0.76054 0.67169 0.51187 -0.11232 -0.04007 -0.03092 155 SER   B O    
4827 C  CB   . SER   B 152 ? 0.67746 0.61137 0.41132 -0.15719 -0.07998 -0.07379 155 SER   B CB   
4828 O  OG   . SER   B 152 ? 0.65337 0.58192 0.38329 -0.20364 -0.11622 -0.10410 155 SER   B OG   
4834 C  C2   . A1IHE C .   ? 0.24685 0.13604 0.12427 -0.01174 0.01318  0.01307  201 A1IHE A C2   
4835 C  C3   . A1IHE C .   ? 0.25526 0.11759 0.12593 -0.00543 0.01035  0.00884  201 A1IHE A C3   
4836 O  O1   . A1IHE C .   ? 0.25539 0.13677 0.12564 -0.00423 0.00754  0.01605  201 A1IHE A O1   
4837 C  C5   . A1IHE C .   ? 0.27003 0.13434 0.13529 0.00013  -0.02015 0.01468  201 A1IHE A C5   
4838 C  C7   . A1IHE C .   ? 0.30539 0.12377 0.13450 -0.01281 -0.01402 0.01955  201 A1IHE A C7   
4839 O  O4   . A1IHE C .   ? 0.25689 0.11903 0.11989 0.00238  -0.00264 0.00795  201 A1IHE A O4   
4840 C  C11  . A1IHE C .   ? 0.31328 0.15727 0.15114 0.01128  0.00343  0.01703  201 A1IHE A C11  
4841 C  C13  . A1IHE C .   ? 0.34299 0.14993 0.15503 -0.02957 -0.01351 0.01971  201 A1IHE A C13  
4842 C  C14  . A1IHE C .   ? 0.32799 0.14860 0.14022 -0.02152 -0.00591 0.02048  201 A1IHE A C14  
4843 C  C15  . A1IHE C .   ? 0.24967 0.16186 0.15166 -0.00649 -0.02830 0.01642  201 A1IHE A C15  
4844 C  C17  . A1IHE C .   ? 0.34800 0.37203 0.40544 -0.00672 -0.15980 0.05762  201 A1IHE A C17  
4845 C  C18  . A1IHE C .   ? 0.62499 0.63618 0.67027 0.00590  -0.11334 0.05091  201 A1IHE A C18  
4846 C  C19  . A1IHE C .   ? 0.85893 0.84781 0.82760 0.00514  -0.07933 0.05136  201 A1IHE A C19  
4847 C  C20  . A1IHE C .   ? 0.24644 0.13144 0.15230 0.00879  -0.00431 0.00575  201 A1IHE A C20  
4848 C  C22  . A1IHE C .   ? 0.24711 0.15191 0.17637 0.02240  -0.00136 -0.00924 201 A1IHE A C22  
4849 C  C23  . A1IHE C .   ? 0.24786 0.14980 0.15488 0.02206  0.00854  -0.00126 201 A1IHE A C23  
4850 C  C25  . A1IHE C .   ? 0.23443 0.14285 0.16315 0.02176  -0.02710 -0.01835 201 A1IHE A C25  
4851 C  C26  . A1IHE C .   ? 0.25562 0.15758 0.15011 0.02596  -0.01348 -0.01120 201 A1IHE A C26  
4852 C  C27  . A1IHE C .   ? 0.22471 0.16360 0.16066 0.01861  -0.00375 -0.00698 201 A1IHE A C27  
4853 C  C28  . A1IHE C .   ? 0.24289 0.16289 0.16305 0.02174  -0.00110 -0.00948 201 A1IHE A C28  
4854 C  C29  . A1IHE C .   ? 0.27403 0.18310 0.17952 0.02353  0.00048  -0.01468 201 A1IHE A C29  
4855 C  C32  . A1IHE C .   ? 0.25304 0.15891 0.15621 0.01683  -0.02964 -0.02447 201 A1IHE A C32  
4856 C  C33  . A1IHE C .   ? 0.23412 0.13728 0.16440 0.01858  -0.02039 -0.01498 201 A1IHE A C33  
4857 C  C35  . A1IHE C .   ? 0.27952 0.18067 0.16062 0.01954  -0.02533 -0.02970 201 A1IHE A C35  
4858 C  C36  . A1IHE C .   ? 0.24434 0.11259 0.13718 0.01304  -0.00683 0.00809  201 A1IHE A C36  
4859 C  C8   . A1IHE C .   ? 0.27413 0.11779 0.14099 -0.00118 0.01407  0.02084  201 A1IHE A C8   
4860 C  C9   . A1IHE C .   ? 0.29968 0.12720 0.15312 0.00566  -0.00728 0.03290  201 A1IHE A C9   
4861 N  N24  . A1IHE C .   ? 0.22726 0.15366 0.17109 0.01722  -0.01231 -0.01299 201 A1IHE A N24  
4862 N  N34  . A1IHE C .   ? 0.24490 0.15062 0.16269 0.00816  -0.00614 -0.00566 201 A1IHE A N34  
4863 O  O16  . A1IHE C .   ? 0.26613 0.19642 0.19587 -0.00302 -0.05419 0.02697  201 A1IHE A O16  
4864 O  O21  . A1IHE C .   ? 0.24777 0.13626 0.17071 0.00477  0.00322  0.00230  201 A1IHE A O21  
4865 O  O30  . A1IHE C .   ? 0.26382 0.20773 0.20625 -0.00155 0.00205  -0.01531 201 A1IHE A O30  
4866 O  O31  . A1IHE C .   ? 0.25363 0.19083 0.18283 0.00392  -0.00327 -0.02341 201 A1IHE A O31  
4867 O  O37  . A1IHE C .   ? 0.23902 0.12151 0.12034 0.00097  0.00188  0.00495  201 A1IHE A O37  
4868 S  S6   . A1IHE C .   ? 0.28896 0.14082 0.15146 0.00685  -0.01824 0.02059  201 A1IHE A S6   
4869 CL CL10 . A1IHE C .   ? 0.27018 0.14759 0.13062 0.00402  -0.00614 0.03162  201 A1IHE A CL10 
4870 CL CL12 . A1IHE C .   ? 0.29436 0.15425 0.16809 0.02805  0.03309  0.01556  201 A1IHE A CL12 
4894 CL CL   . CL    D .   ? 0.24731 0.23570 0.27972 0.02682  -0.00660 0.11439  202 CL    A CL   
4895 C  C2   . A1IHE E .   ? 0.25704 0.18394 0.14440 0.01846  0.00263  0.00219  201 A1IHE B C2   
4896 C  C3   . A1IHE E .   ? 0.27539 0.17029 0.15011 0.02188  -0.01110 0.00455  201 A1IHE B C3   
4897 O  O1   . A1IHE E .   ? 0.26607 0.19092 0.16145 0.03590  -0.01517 0.00194  201 A1IHE B O1   
4898 C  C5   . A1IHE E .   ? 0.31153 0.20170 0.18969 0.04637  -0.03492 -0.02202 201 A1IHE B C5   
4899 C  C7   . A1IHE E .   ? 0.31563 0.19294 0.21588 0.04687  -0.04149 -0.00609 201 A1IHE B C7   
4900 O  O4   . A1IHE E .   ? 0.29200 0.18146 0.15839 0.04124  -0.01696 -0.01196 201 A1IHE B O4   
4901 C  C11  . A1IHE E .   ? 0.34849 0.23120 0.20119 0.04262  0.01016  0.00158  201 A1IHE B C11  
4902 C  C13  . A1IHE E .   ? 0.34751 0.24262 0.21145 0.03979  -0.00969 -0.01464 201 A1IHE B C13  
4903 C  C14  . A1IHE E .   ? 0.35613 0.25265 0.21070 0.05203  -0.01360 -0.00413 201 A1IHE B C14  
4904 C  C15  . A1IHE E .   ? 0.32249 0.18131 0.20249 0.03086  -0.05077 -0.03777 201 A1IHE B C15  
4905 C  C17  . A1IHE E .   ? 0.47451 0.35797 0.37193 0.01515  -0.02762 -0.12372 201 A1IHE B C17  
4906 C  C18  . A1IHE E .   ? 0.55527 0.50013 0.48158 0.00834  0.00136  -0.11441 201 A1IHE B C18  
4907 C  C19  . A1IHE E .   ? 0.59432 0.56237 0.52994 -0.00932 0.01046  -0.09744 201 A1IHE B C19  
4908 C  C20  . A1IHE E .   ? 0.29771 0.18313 0.18543 0.01059  -0.03776 -0.00504 201 A1IHE B C20  
4909 C  C22  . A1IHE E .   ? 0.34444 0.20410 0.21039 -0.00179 -0.03150 0.01583  201 A1IHE B C22  
4910 C  C23  . A1IHE E .   ? 0.33466 0.20499 0.19308 0.00645  -0.04663 0.00313  201 A1IHE B C23  
4911 C  C25  . A1IHE E .   ? 0.33204 0.19299 0.19376 -0.00452 -0.04092 -0.01475 201 A1IHE B C25  
4912 C  C26  . A1IHE E .   ? 0.34218 0.19835 0.22633 0.01220  -0.02111 -0.01155 201 A1IHE B C26  
4913 C  C27  . A1IHE E .   ? 0.32509 0.20274 0.23116 0.00524  -0.01465 -0.02489 201 A1IHE B C27  
4914 C  C28  . A1IHE E .   ? 0.30361 0.24828 0.23940 -0.00513 -0.03579 -0.02622 201 A1IHE B C28  
4915 C  C29  . A1IHE E .   ? 0.33715 0.29526 0.27046 -0.03120 -0.03607 -0.02095 201 A1IHE B C29  
4916 C  C32  . A1IHE E .   ? 0.31595 0.24939 0.20401 -0.01284 -0.02855 -0.02742 201 A1IHE B C32  
4917 C  C33  . A1IHE E .   ? 0.32997 0.20648 0.17707 -0.00945 -0.03901 -0.02235 201 A1IHE B C33  
4918 C  C35  . A1IHE E .   ? 0.37454 0.25704 0.18025 0.00368  -0.01851 -0.03355 201 A1IHE B C35  
4919 C  C36  . A1IHE E .   ? 0.27850 0.16304 0.15485 0.02139  -0.02438 0.00529  201 A1IHE B C36  
4920 C  C8   . A1IHE E .   ? 0.30538 0.18320 0.23480 0.05554  -0.02418 -0.01217 201 A1IHE B C8   
4921 C  C9   . A1IHE E .   ? 0.32923 0.19959 0.21082 0.06367  0.01002  -0.00225 201 A1IHE B C9   
4922 N  N24  . A1IHE E .   ? 0.34909 0.20651 0.19636 0.00602  -0.03556 0.00592  201 A1IHE B N24  
4923 N  N34  . A1IHE E .   ? 0.33509 0.22394 0.18246 -0.00367 -0.03678 -0.02016 201 A1IHE B N34  
4924 O  O16  . A1IHE E .   ? 0.39806 0.22591 0.25694 0.03911  -0.05127 -0.07725 201 A1IHE B O16  
4925 O  O21  . A1IHE E .   ? 0.31898 0.17257 0.20414 0.00611  -0.03947 0.00991  201 A1IHE B O21  
4926 O  O30  . A1IHE E .   ? 0.38243 0.33172 0.29452 -0.04060 -0.03144 -0.03382 201 A1IHE B O30  
4927 O  O31  . A1IHE E .   ? 0.36846 0.34171 0.27089 -0.00292 -0.04502 -0.02587 201 A1IHE B O31  
4928 O  O37  . A1IHE E .   ? 0.27749 0.15895 0.14459 0.02512  -0.02761 0.01129  201 A1IHE B O37  
4929 S  S6   . A1IHE E .   ? 0.36512 0.18507 0.22109 0.06863  -0.02789 -0.01446 201 A1IHE B S6   
4930 CL CL10 . A1IHE E .   ? 0.32801 0.20518 0.19452 0.04076  0.01258  0.00425  201 A1IHE B CL10 
4931 CL CL12 . A1IHE E .   ? 0.38386 0.25366 0.21324 -0.00991 0.03996  0.00111  201 A1IHE B CL12 
4955 O  O    . HOH   F .   ? 0.54648 0.54514 0.56535 -0.10741 0.00177  0.09131  301 HOH   A O    
4956 O  O    . HOH   F .   ? 0.44237 0.59728 0.40383 0.03468  0.09830  -0.18223 302 HOH   A O    
4957 O  O    . HOH   F .   ? 0.48846 0.44663 0.44770 -0.06364 0.14886  -0.08332 303 HOH   A O    
4958 O  O    . HOH   F .   ? 0.53839 0.45775 0.41411 0.03866  0.08806  0.05427  304 HOH   A O    
4959 O  O    . HOH   F .   ? 0.53384 0.58524 0.35241 -0.06815 0.15712  0.13968  305 HOH   A O    
4960 O  O    . HOH   F .   ? 0.46832 0.48557 0.26718 -0.08902 0.12761  0.06941  306 HOH   A O    
4961 O  O    . HOH   F .   ? 0.36404 0.34887 0.44475 -0.00822 0.01280  0.17800  307 HOH   A O    
4962 O  O    . HOH   F .   ? 0.55309 0.58393 0.60564 0.02739  0.08377  -0.06736 308 HOH   A O    
4963 O  O    . HOH   F .   ? 0.44946 0.57689 0.27770 -0.12886 0.03437  0.04815  309 HOH   A O    
4964 O  O    . HOH   F .   ? 0.53738 0.51096 0.47117 0.06206  0.03054  0.11403  310 HOH   A O    
4965 O  O    . HOH   F .   ? 0.30170 0.46461 0.23155 0.01400  0.05956  0.04097  311 HOH   A O    
4966 O  O    . HOH   F .   ? 0.36470 0.51287 0.21067 -0.07717 -0.09875 0.07553  312 HOH   A O    
4967 O  O    . HOH   F .   ? 0.51941 0.32192 0.76820 0.04165  0.25574  0.18193  313 HOH   A O    
4968 O  O    . HOH   F .   ? 0.47598 0.45404 0.38865 0.15679  -0.05717 -0.04343 314 HOH   A O    
4969 O  O    . HOH   F .   ? 0.69105 0.19003 0.24801 -0.06470 -0.05097 -0.01323 315 HOH   A O    
4970 O  O    . HOH   F .   ? 0.44327 0.41719 0.40971 -0.10189 -0.06783 -0.05527 316 HOH   A O    
4971 O  O    . HOH   F .   ? 0.46628 0.31738 0.79803 0.12389  0.25999  0.12858  317 HOH   A O    
4972 O  O    . HOH   F .   ? 0.28004 0.17094 0.30719 0.05290  -0.00870 -0.03547 318 HOH   A O    
4973 O  O    . HOH   F .   ? 0.65707 0.63787 0.32965 0.32718  0.01387  -0.07770 319 HOH   A O    
4974 O  O    . HOH   F .   ? 0.38929 0.15425 0.18612 -0.00977 -0.01939 0.02442  320 HOH   A O    
4975 O  O    . HOH   F .   ? 0.49527 0.55871 0.45675 0.10226  0.21579  -0.14707 321 HOH   A O    
4976 O  O    . HOH   F .   ? 0.34957 0.56027 0.51792 -0.08318 0.05064  -0.09005 322 HOH   A O    
4977 O  O    . HOH   F .   ? 0.39083 0.39906 0.32991 -0.03736 -0.04654 0.05515  323 HOH   A O    
4978 O  O    . HOH   F .   ? 0.39981 0.49015 0.36743 0.19832  0.14629  0.11731  324 HOH   A O    
4979 O  O    . HOH   F .   ? 0.41071 0.28186 0.33300 0.01440  0.14045  -0.06942 325 HOH   A O    
4980 O  O    . HOH   F .   ? 0.73631 0.28556 0.34891 -0.15514 0.15571  0.01036  326 HOH   A O    
4981 O  O    . HOH   F .   ? 0.32338 0.75992 0.27219 -0.07051 -0.01581 0.12538  327 HOH   A O    
4982 O  O    . HOH   F .   ? 0.30908 0.24945 0.26757 -0.00095 -0.05180 0.00442  328 HOH   A O    
4983 O  O    . HOH   F .   ? 0.22459 0.29709 0.30894 -0.03545 -0.00794 0.10271  329 HOH   A O    
4984 O  O    . HOH   F .   ? 0.66356 0.64806 0.33096 0.35052  0.06456  -0.01244 330 HOH   A O    
4985 O  O    B HOH   F .   ? 0.23004 0.33649 0.79169 0.04967  -0.08388 -0.03091 331 HOH   A O    
4986 O  O    . HOH   F .   ? 0.21683 0.19733 0.26365 0.00485  0.06738  -0.01994 332 HOH   A O    
4987 O  O    . HOH   F .   ? 0.59355 0.62062 0.29021 -0.00248 0.21717  0.01112  333 HOH   A O    
4988 O  O    . HOH   F .   ? 0.43546 0.20448 0.71480 -0.03713 -0.09709 0.08101  334 HOH   A O    
4989 O  O    . HOH   F .   ? 0.22982 0.20299 0.17561 -0.02277 -0.02919 0.03611  335 HOH   A O    
4990 O  O    . HOH   F .   ? 0.22620 0.18094 0.17531 0.00911  -0.02835 0.04582  336 HOH   A O    
4991 O  O    . HOH   F .   ? 0.36566 0.39388 0.40765 0.09792  0.01840  -0.06462 337 HOH   A O    
4992 O  O    . HOH   F .   ? 0.26124 0.17581 0.16778 -0.00089 -0.00558 -0.00997 338 HOH   A O    
4993 O  O    . HOH   F .   ? 0.77429 0.72705 0.46549 0.12522  -0.01003 -0.31451 339 HOH   A O    
4994 O  O    . HOH   F .   ? 0.69172 0.22076 0.43741 0.06969  0.21721  0.00508  340 HOH   A O    
4995 O  O    . HOH   F .   ? 0.51191 0.33128 0.38289 0.16831  0.09843  -0.05754 341 HOH   A O    
4996 O  O    . HOH   F .   ? 0.24941 0.16894 0.16211 0.02982  -0.04635 -0.00667 342 HOH   A O    
4997 O  O    . HOH   F .   ? 0.24675 0.19987 0.21784 0.03986  -0.04304 -0.05365 343 HOH   A O    
4998 O  O    . HOH   F .   ? 0.38762 0.21255 0.25642 0.02442  0.08835  -0.00009 344 HOH   A O    
4999 O  O    . HOH   F .   ? 0.27369 0.27662 0.31844 0.06226  -0.02028 -0.07886 345 HOH   A O    
5000 O  O    . HOH   F .   ? 0.43839 0.38491 0.25663 -0.03263 -0.06431 -0.00158 346 HOH   A O    
5001 O  O    . HOH   F .   ? 0.25619 0.28817 0.25863 0.02418  0.03243  0.06049  347 HOH   A O    
5002 O  O    . HOH   F .   ? 0.53670 0.18874 0.24882 0.01423  0.08980  -0.03509 348 HOH   A O    
5003 O  O    . HOH   F .   ? 0.27365 0.14143 0.14000 0.00131  -0.00149 -0.00423 349 HOH   A O    
5004 O  O    . HOH   F .   ? 0.26104 0.22166 0.19591 0.03916  -0.03716 -0.01277 350 HOH   A O    
5005 O  O    . HOH   F .   ? 0.32476 0.14492 0.16071 0.05036  -0.02907 0.00532  351 HOH   A O    
5006 O  O    . HOH   F .   ? 0.34177 0.16987 0.20337 0.03838  0.08202  0.00623  352 HOH   A O    
5007 O  O    . HOH   F .   ? 0.32880 0.24159 0.20174 0.08399  0.06494  0.05955  353 HOH   A O    
5008 O  O    . HOH   F .   ? 0.79191 0.42293 0.48584 0.06025  -0.16406 -0.21694 354 HOH   A O    
5009 O  O    . HOH   F .   ? 0.44656 0.32422 0.24110 0.00262  -0.06306 -0.02088 355 HOH   A O    
5010 O  O    . HOH   F .   ? 0.25061 0.20021 0.22885 0.01551  -0.01510 0.06526  356 HOH   A O    
5011 O  O    . HOH   F .   ? 0.55048 0.32164 0.20905 0.12396  0.11153  0.04884  357 HOH   A O    
5012 O  O    . HOH   F .   ? 0.28666 0.19270 0.24285 0.06694  -0.00757 -0.05063 358 HOH   A O    
5013 O  O    . HOH   F .   ? 0.21428 0.22848 0.20016 0.02858  -0.01315 -0.01721 359 HOH   A O    
5014 O  O    . HOH   F .   ? 0.34321 0.54443 0.28468 -0.04595 -0.01901 -0.11681 360 HOH   A O    
5015 O  O    . HOH   F .   ? 0.57486 0.42931 0.21921 0.00345  0.13793  0.06990  361 HOH   A O    
5016 O  O    . HOH   F .   ? 0.35070 0.19141 0.20397 0.02972  -0.01629 -0.06122 362 HOH   A O    
5017 O  O    . HOH   F .   ? 0.42515 0.56927 0.35998 -0.05318 0.10575  0.00789  363 HOH   A O    
5018 O  O    . HOH   F .   ? 0.32977 0.21126 0.23609 -0.01713 0.04077  -0.04901 364 HOH   A O    
5019 O  O    . HOH   F .   ? 0.39347 0.38762 0.66395 -0.02671 0.02690  -0.04775 365 HOH   A O    
5020 O  O    . HOH   F .   ? 0.44778 0.34704 0.34689 0.15232  -0.08488 -0.08525 366 HOH   A O    
5021 O  O    . HOH   F .   ? 0.31756 0.27955 0.18956 -0.00087 -0.01203 -0.02920 367 HOH   A O    
5022 O  O    . HOH   F .   ? 0.46040 0.44337 0.27766 -0.02768 0.09976  -0.02274 368 HOH   A O    
5023 O  O    . HOH   F .   ? 0.26523 0.25861 0.19749 0.02451  0.01658  0.06332  369 HOH   A O    
5024 O  O    . HOH   F .   ? 0.41295 0.44492 0.33141 -0.05101 0.02722  0.09069  370 HOH   A O    
5025 O  O    . HOH   F .   ? 0.25564 0.44033 0.27390 -0.01304 0.02467  -0.01259 371 HOH   A O    
5026 O  O    . HOH   F .   ? 0.28568 0.38458 0.90986 0.00786  0.02172  -0.27374 372 HOH   A O    
5027 O  O    . HOH   F .   ? 0.45859 0.31669 0.27483 -0.08671 0.10341  -0.12350 373 HOH   A O    
5028 O  O    . HOH   F .   ? 0.42374 0.26406 0.26039 0.02849  -0.02119 -0.01721 374 HOH   A O    
5029 O  O    . HOH   F .   ? 0.31187 0.63740 0.49463 0.12434  0.14064  -0.06176 375 HOH   A O    
5030 O  O    . HOH   F .   ? 0.48611 0.34095 0.89115 0.16553  0.09510  0.06640  376 HOH   A O    
5031 O  O    . HOH   F .   ? 0.32795 0.68188 0.56492 0.16929  0.02511  -0.15389 377 HOH   A O    
5032 O  O    . HOH   F .   ? 0.41254 0.59798 0.37512 0.21310  -0.10465 -0.18357 378 HOH   A O    
5033 O  O    . HOH   F .   ? 0.39944 0.26747 0.45708 -0.06252 0.06570  0.00813  379 HOH   A O    
5034 O  O    . HOH   F .   ? 0.26364 0.15429 0.22323 0.03594  0.01456  -0.03958 380 HOH   A O    
5035 O  O    . HOH   F .   ? 0.57976 0.27222 0.21981 0.15362  -0.13549 -0.03873 381 HOH   A O    
5036 O  O    . HOH   F .   ? 0.36724 0.42697 0.51955 0.00897  -0.13514 0.06974  382 HOH   A O    
5037 O  O    . HOH   F .   ? 0.28438 0.31598 0.42871 0.01421  -0.05835 -0.02501 383 HOH   A O    
5038 O  O    . HOH   F .   ? 0.47263 0.17333 0.23064 0.02977  0.07851  -0.01016 384 HOH   A O    
5039 O  O    . HOH   F .   ? 0.44392 0.21961 0.52632 -0.03833 0.18658  -0.10393 385 HOH   A O    
5040 O  O    . HOH   F .   ? 0.39543 0.34424 0.60062 0.02031  0.13789  -0.20872 386 HOH   A O    
5041 O  O    . HOH   F .   ? 0.42923 0.24595 0.68101 0.09190  0.12023  -0.03541 387 HOH   A O    
5042 O  O    . HOH   F .   ? 0.33114 0.31538 0.20382 0.04162  -0.03172 -0.00187 388 HOH   A O    
5043 O  O    . HOH   F .   ? 0.87473 0.27326 0.31392 -0.07741 -0.04075 -0.04121 389 HOH   A O    
5044 O  O    . HOH   F .   ? 0.26321 0.37913 0.45935 0.13567  0.03011  0.13213  390 HOH   A O    
5045 O  O    . HOH   F .   ? 0.27484 0.43126 0.28479 -0.07862 0.09870  -0.14553 391 HOH   A O    
5046 O  O    . HOH   F .   ? 0.53594 0.59983 0.43325 0.31866  0.14880  0.11648  392 HOH   A O    
5047 O  O    . HOH   F .   ? 0.27965 0.41738 0.50836 -0.05259 -0.06798 0.25571  393 HOH   A O    
5048 O  O    . HOH   F .   ? 0.38414 0.54032 0.57167 0.07249  0.02273  0.02731  394 HOH   A O    
5049 O  O    . HOH   F .   ? 0.37319 0.26858 0.17700 0.02638  0.02374  0.07742  395 HOH   A O    
5050 O  O    . HOH   F .   ? 0.40509 0.19159 0.28127 0.04837  0.01943  -0.03713 396 HOH   A O    
5051 O  O    . HOH   F .   ? 0.58880 0.29518 0.25387 0.00319  0.16893  -0.05168 397 HOH   A O    
5052 O  O    . HOH   F .   ? 0.76219 0.37275 0.33571 0.01196  0.15532  0.11723  398 HOH   A O    
5053 O  O    . HOH   F .   ? 0.56721 0.51015 0.42438 -0.02823 0.07232  -0.07376 399 HOH   A O    
5054 O  O    . HOH   F .   ? 0.45665 0.29655 0.26726 0.03271  0.00192  0.06604  400 HOH   A O    
5055 O  O    . HOH   F .   ? 0.89499 1.15910 0.79100 0.33485  -0.22020 0.31515  401 HOH   A O    
5056 O  O    . HOH   F .   ? 0.49258 0.28131 0.27265 -0.14365 -0.06316 0.03273  402 HOH   A O    
5057 O  O    . HOH   F .   ? 0.58705 0.57272 0.62484 -0.03640 0.03265  0.06313  403 HOH   A O    
5058 O  O    . HOH   F .   ? 0.29399 0.30274 0.31432 -0.01920 0.02255  -0.09080 404 HOH   A O    
5059 O  O    . HOH   F .   ? 0.60698 0.58398 0.52710 0.14758  0.10459  -0.17576 405 HOH   A O    
5060 O  O    . HOH   F .   ? 0.52827 0.53604 0.53466 -0.01607 -0.07416 -0.04285 406 HOH   A O    
5061 O  O    . HOH   F .   ? 0.31689 0.23191 0.32859 0.07290  0.04497  0.08662  407 HOH   A O    
5062 O  O    . HOH   F .   ? 0.32395 0.19724 0.23313 -0.01576 -0.03441 -0.03004 408 HOH   A O    
5063 O  O    . HOH   F .   ? 0.43463 0.43162 0.52547 -0.03320 0.08591  0.15500  409 HOH   A O    
5064 O  O    . HOH   F .   ? 0.29771 0.29991 0.59925 0.05144  0.00273  -0.05413 410 HOH   A O    
5065 O  O    . HOH   F .   ? 0.35848 0.24767 0.23199 0.05687  -0.05349 -0.05249 411 HOH   A O    
5066 O  O    . HOH   F .   ? 0.50926 0.22335 0.53714 -0.01399 -0.22985 0.07344  412 HOH   A O    
5067 O  O    . HOH   F .   ? 1.13858 1.13840 1.11957 0.00038  -0.01691 0.00796  413 HOH   A O    
5068 O  O    . HOH   F .   ? 0.36155 0.25292 0.31209 -0.00427 -0.01610 -0.11792 414 HOH   A O    
5069 O  O    . HOH   F .   ? 0.33275 0.30584 0.27600 -0.00149 -0.01666 0.05243  415 HOH   A O    
5070 O  O    . HOH   F .   ? 0.46849 0.41923 0.52604 0.11780  0.07844  0.00503  416 HOH   A O    
5071 O  O    . HOH   F .   ? 0.25122 0.24338 0.28075 0.04614  0.09437  -0.00463 417 HOH   A O    
5072 O  O    . HOH   F .   ? 0.37322 0.65154 0.45391 0.01653  -0.04721 0.23796  418 HOH   A O    
5073 O  O    . HOH   F .   ? 0.38138 0.21485 0.18855 0.05947  -0.04558 0.03301  419 HOH   A O    
5074 O  O    . HOH   F .   ? 0.50870 0.54153 0.37954 0.06079  -0.12143 -0.03187 420 HOH   A O    
5075 O  O    . HOH   F .   ? 0.59725 0.45039 0.54413 0.19998  -0.21143 -0.18117 421 HOH   A O    
5076 O  O    . HOH   F .   ? 0.28644 0.17661 0.21872 0.01561  0.05709  -0.03648 422 HOH   A O    
5077 O  O    . HOH   F .   ? 0.63135 0.34619 0.84238 0.11869  -0.37274 -0.07449 423 HOH   A O    
5078 O  O    . HOH   F .   ? 0.50634 0.36466 0.37302 0.03567  -0.00488 -0.02603 424 HOH   A O    
5079 O  O    . HOH   F .   ? 0.54518 0.46474 0.43395 0.01845  0.03312  0.09548  425 HOH   A O    
5080 O  O    . HOH   F .   ? 0.77740 0.42801 0.52929 0.01142  0.35702  -0.02051 426 HOH   A O    
5081 O  O    . HOH   F .   ? 0.34521 0.28924 0.30764 -0.04943 0.01008  0.09317  427 HOH   A O    
5082 O  O    . HOH   F .   ? 0.25392 0.32174 0.22050 0.03682  0.07115  0.04789  428 HOH   A O    
5083 O  O    . HOH   F .   ? 0.45755 0.20810 0.47854 -0.04750 0.10535  -0.07521 429 HOH   A O    
5084 O  O    . HOH   F .   ? 0.87763 0.59923 0.25985 -0.23970 -0.03834 0.04055  430 HOH   A O    
5085 O  O    . HOH   F .   ? 0.53218 0.51353 0.53081 -0.11042 0.00157  0.02886  431 HOH   A O    
5086 O  O    . HOH   F .   ? 0.86913 0.28225 0.66726 0.01383  -0.04064 -0.11061 432 HOH   A O    
5087 O  O    . HOH   F .   ? 0.61903 0.52147 0.37443 0.16276  0.12287  0.22187  433 HOH   A O    
5088 O  O    . HOH   F .   ? 0.26666 0.26924 0.18674 0.02742  0.03459  0.00976  434 HOH   A O    
5089 O  O    . HOH   F .   ? 0.75533 0.72653 0.75989 -0.11243 0.40235  0.12614  435 HOH   A O    
5090 O  O    . HOH   F .   ? 0.79629 0.28610 0.51073 0.06578  -0.24451 0.05774  436 HOH   A O    
5091 O  O    . HOH   F .   ? 0.43473 0.33492 0.44840 -0.05061 -0.11378 -0.04141 437 HOH   A O    
5092 O  O    . HOH   F .   ? 0.52003 0.53824 0.46875 0.00622  0.00187  0.03385  438 HOH   A O    
5093 O  O    . HOH   F .   ? 0.66932 0.63050 0.66759 0.02765  0.03523  -0.02980 439 HOH   A O    
5094 O  O    . HOH   F .   ? 1.03373 1.02222 1.02689 0.01186  -0.00059 -0.00070 440 HOH   A O    
5095 O  O    . HOH   F .   ? 0.68180 0.58285 0.65937 0.02090  -0.05939 -0.01171 441 HOH   A O    
5096 O  O    . HOH   F .   ? 0.36781 0.39619 0.39998 0.09488  -0.17305 -0.15682 442 HOH   A O    
5097 O  O    . HOH   F .   ? 0.32651 0.38350 0.27691 0.07503  -0.03057 0.04150  443 HOH   A O    
5098 O  O    . HOH   F .   ? 0.66031 0.22520 0.27406 -0.01537 0.02560  0.06299  444 HOH   A O    
5099 O  O    . HOH   F .   ? 0.30372 0.40638 0.36475 0.07322  0.06582  0.04523  445 HOH   A O    
5100 O  O    . HOH   F .   ? 0.53857 0.34626 0.45794 -0.01360 -0.05735 0.01484  446 HOH   A O    
5101 O  O    . HOH   F .   ? 0.36580 0.35336 0.36288 -0.07589 -0.01331 0.05919  447 HOH   A O    
5102 O  O    . HOH   F .   ? 0.46101 0.49025 0.41796 -0.11066 0.11697  -0.01516 448 HOH   A O    
5103 O  O    . HOH   F .   ? 0.57931 0.50593 0.48715 0.05025  -0.09937 -0.19214 449 HOH   A O    
5104 O  O    . HOH   F .   ? 0.29168 0.62444 0.29749 0.11215  0.07466  0.06041  450 HOH   A O    
5105 O  O    . HOH   F .   ? 0.55904 0.32583 0.51477 0.21286  -0.01268 -0.09334 451 HOH   A O    
5106 O  O    . HOH   F .   ? 0.39057 0.41062 0.44277 0.16652  0.02001  0.06378  452 HOH   A O    
5107 O  O    . HOH   F .   ? 0.65845 0.40520 0.47865 -0.07899 0.23094  0.07374  453 HOH   A O    
5108 O  O    . HOH   F .   ? 0.69100 0.41907 0.47375 -0.00909 0.26000  0.03804  454 HOH   A O    
5109 O  O    . HOH   F .   ? 0.44255 0.42058 0.36964 -0.06384 0.01299  0.03372  455 HOH   A O    
5110 O  O    . HOH   F .   ? 0.69197 0.79431 0.41669 -0.10286 0.28509  0.00085  456 HOH   A O    
5111 O  O    . HOH   F .   ? 0.77738 0.85894 0.47586 0.21884  0.17837  -0.20229 457 HOH   A O    
5112 O  O    . HOH   F .   ? 0.48847 0.56412 0.52611 -0.04808 0.09128  -0.05375 458 HOH   A O    
5113 O  O    . HOH   F .   ? 0.47604 0.41560 0.42810 -0.03495 0.01248  0.14302  459 HOH   A O    
5114 O  O    . HOH   F .   ? 0.64423 0.64444 0.60847 0.01500  -0.01838 0.00343  460 HOH   A O    
5115 O  O    . HOH   F .   ? 0.42843 0.53923 0.52958 -0.13975 -0.08864 -0.16915 461 HOH   A O    
5116 O  O    . HOH   F .   ? 0.49219 0.32794 0.32031 -0.01046 0.01187  -0.07923 462 HOH   A O    
5117 O  O    . HOH   F .   ? 0.52324 0.36820 0.24537 -0.00142 0.03879  0.03125  463 HOH   A O    
5118 O  O    . HOH   F .   ? 0.57755 0.45730 1.09622 0.12531  0.14676  -0.03537 464 HOH   A O    
5119 O  O    . HOH   F .   ? 0.59273 0.71123 0.64422 -0.00067 -0.09668 -0.04383 465 HOH   A O    
5120 O  O    . HOH   F .   ? 0.51258 0.39731 0.54049 -0.17445 -0.00390 -0.04634 466 HOH   A O    
5121 O  O    . HOH   F .   ? 0.34298 0.26589 0.21594 -0.01640 -0.01805 0.01275  467 HOH   A O    
5122 O  O    . HOH   F .   ? 0.57596 0.53766 0.57886 -0.01418 -0.03009 0.06542  468 HOH   A O    
5123 O  O    . HOH   F .   ? 0.48766 0.26313 0.51863 0.12233  -0.12943 -0.11126 469 HOH   A O    
5124 O  O    . HOH   F .   ? 0.48510 0.62760 0.56960 -0.01941 -0.00871 -0.03142 470 HOH   A O    
5125 O  O    . HOH   F .   ? 0.39530 0.39824 0.40964 0.05616  -0.08767 -0.16028 471 HOH   A O    
5126 O  O    . HOH   F .   ? 0.40483 0.36246 0.37052 -0.00923 0.14574  0.02329  472 HOH   A O    
5127 O  O    . HOH   F .   ? 0.39434 0.73893 0.44878 -0.05342 -0.01596 0.23377  473 HOH   A O    
5128 O  O    . HOH   F .   ? 0.47076 0.31200 0.33476 -0.10158 -0.04153 -0.02107 474 HOH   A O    
5129 O  O    . HOH   F .   ? 0.41014 0.36946 0.50924 0.10973  -0.05812 0.06060  475 HOH   A O    
5130 O  O    . HOH   F .   ? 0.65142 0.60136 0.56592 0.18642  -0.04443 0.11848  476 HOH   A O    
5131 O  O    . HOH   F .   ? 0.59904 0.69605 0.61425 0.18313  -0.29354 -0.29356 477 HOH   A O    
5132 O  O    . HOH   F .   ? 0.50758 0.34618 0.27423 -0.02709 0.06918  -0.05715 478 HOH   A O    
5133 O  O    . HOH   F .   ? 0.54912 0.51128 0.37940 -0.24652 0.03915  -0.01681 479 HOH   A O    
5134 O  O    . HOH   F .   ? 0.48231 0.58753 0.47133 -0.08020 0.03505  -0.05072 480 HOH   A O    
5135 O  O    . HOH   F .   ? 0.55460 0.27951 0.39636 -0.09338 -0.17472 0.12973  481 HOH   A O    
5136 O  O    . HOH   F .   ? 0.31393 0.43497 0.39573 0.11361  0.14323  0.10855  482 HOH   A O    
5137 O  O    . HOH   F .   ? 0.51614 0.39473 0.52721 0.07661  -0.05141 0.08102  483 HOH   A O    
5138 O  O    . HOH   F .   ? 0.64519 0.38431 0.23647 -0.16156 0.04730  -0.07783 484 HOH   A O    
5139 O  O    . HOH   F .   ? 0.39024 0.49064 0.44907 -0.05865 0.04902  -0.04751 485 HOH   A O    
5140 O  O    . HOH   F .   ? 0.54895 0.43458 0.28385 0.02043  -0.01715 -0.05947 486 HOH   A O    
5141 O  O    . HOH   F .   ? 0.32790 0.51439 0.55275 0.05003  0.04322  -0.07305 487 HOH   A O    
5142 O  O    . HOH   G .   ? 0.70241 0.86586 0.91272 0.31460  0.21028  0.24804  301 HOH   B O    
5143 O  O    . HOH   G .   ? 0.39267 0.45549 0.34868 -0.00619 -0.14050 -0.02158 302 HOH   B O    
5144 O  O    . HOH   G .   ? 0.52440 0.40810 0.43808 0.07887  0.10732  -0.02170 303 HOH   B O    
5145 O  O    . HOH   G .   ? 0.52389 0.42303 0.35460 -0.17913 0.00360  0.06538  304 HOH   B O    
5146 O  O    . HOH   G .   ? 0.38740 0.22327 0.30757 0.00543  0.01659  -0.01054 305 HOH   B O    
5147 O  O    a HOH   G .   ? 0.35179 0.23565 0.17298 -0.04680 0.04475  0.00741  306 HOH   B O    
5148 O  O    . HOH   G .   ? 0.45305 0.32908 0.49181 0.10888  -0.05187 0.01453  307 HOH   B O    
5149 O  O    . HOH   G .   ? 0.62904 0.56101 0.48755 -0.03370 0.08037  0.00728  308 HOH   B O    
5150 O  O    . HOH   G .   ? 0.38635 0.32143 0.47626 0.05105  -0.06926 -0.05050 309 HOH   B O    
5151 O  O    . HOH   G .   ? 0.35917 0.48471 0.52521 -0.12456 0.09585  0.12725  310 HOH   B O    
5152 O  O    . HOH   G .   ? 0.25916 0.30884 0.47802 -0.04218 0.05859  -0.07721 311 HOH   B O    
5153 O  O    . HOH   G .   ? 0.45620 0.37152 0.34398 -0.04574 -0.09752 0.04659  312 HOH   B O    
5154 O  O    . HOH   G .   ? 0.58325 0.44467 0.47597 -0.09995 -0.12784 0.00949  313 HOH   B O    
5155 O  O    . HOH   G .   ? 0.45395 0.34601 0.56973 0.09417  0.19946  0.21926  314 HOH   B O    
5156 O  O    . HOH   G .   ? 0.48095 0.44924 0.26852 -0.12430 0.05384  0.05178  315 HOH   B O    
5157 O  O    . HOH   G .   ? 0.59856 0.56624 0.54267 -0.07074 -0.01083 -0.03634 316 HOH   B O    
5158 O  O    . HOH   G .   ? 0.41360 0.23301 0.26156 0.00293  -0.06007 0.04712  317 HOH   B O    
5159 O  O    . HOH   G .   ? 0.52402 0.55651 0.27167 -0.08800 -0.03782 0.05167  318 HOH   B O    
5160 O  O    . HOH   G .   ? 0.30700 0.20117 0.25055 0.04851  0.08331  0.08033  319 HOH   B O    
5161 O  O    . HOH   G .   ? 0.35508 0.19459 0.32497 -0.03777 -0.08699 0.08544  320 HOH   B O    
5162 O  O    . HOH   G .   ? 0.33463 0.72366 0.36550 -0.02383 0.04326  0.25379  321 HOH   B O    
5163 O  O    . HOH   G .   ? 0.40682 0.37110 0.22426 -0.05830 0.04333  0.01528  322 HOH   B O    
5164 O  O    . HOH   G .   ? 0.41120 0.32908 0.27159 0.00890  0.06627  0.11697  323 HOH   B O    
5165 O  O    . HOH   G .   ? 0.80802 0.35200 0.30080 0.22634  -0.08988 -0.01283 324 HOH   B O    
5166 O  O    . HOH   G .   ? 0.37533 0.39046 0.31140 -0.07432 0.10079  -0.00664 325 HOH   B O    
5167 O  O    . HOH   G .   ? 0.55999 0.50617 0.54259 0.17661  -0.28140 -0.04061 326 HOH   B O    
5168 O  O    . HOH   G .   ? 0.29443 0.52223 0.22538 -0.12170 -0.04117 0.11309  327 HOH   B O    
5169 O  O    . HOH   G .   ? 0.20095 0.16821 0.30044 -0.00346 -0.03804 0.02361  328 HOH   B O    
5170 O  O    . HOH   G .   ? 0.73617 0.27095 0.23342 0.12628  0.05451  0.05280  329 HOH   B O    
5171 O  O    . HOH   G .   ? 0.32070 0.22646 0.22234 0.06179  -0.04107 -0.00326 330 HOH   B O    
5172 O  O    . HOH   G .   ? 0.46896 0.57101 0.33810 -0.05611 -0.14556 -0.01088 331 HOH   B O    
5173 O  O    . HOH   G .   ? 0.35288 0.26856 0.33643 -0.03754 0.01429  0.03194  332 HOH   B O    
5174 O  O    . HOH   G .   ? 0.68140 0.31011 0.50961 0.05780  -0.29492 0.04714  333 HOH   B O    
5175 O  O    . HOH   G .   ? 0.28358 0.23140 0.21398 0.04365  0.03568  0.04477  334 HOH   B O    
5176 O  O    . HOH   G .   ? 0.32109 0.21126 0.17780 0.00981  0.00751  0.04221  335 HOH   B O    
5177 O  O    . HOH   G .   ? 0.21256 0.15120 0.16765 0.00298  -0.03749 0.01326  336 HOH   B O    
5178 O  O    . HOH   G .   ? 0.44870 0.52749 0.46785 0.08187  0.09185  -0.05626 337 HOH   B O    
5179 O  O    . HOH   G .   ? 0.22810 0.23849 0.24022 -0.00254 0.03306  0.03368  338 HOH   B O    
5180 O  O    . HOH   G .   ? 0.51769 0.48805 0.39483 0.08201  0.00909  0.16308  339 HOH   B O    
5181 O  O    . HOH   G .   ? 0.41479 0.27495 0.52303 -0.06375 -0.11321 0.07932  340 HOH   B O    
5182 O  O    . HOH   G .   ? 0.23848 0.16807 0.19574 -0.00403 0.01612  0.01915  341 HOH   B O    
5183 O  O    . HOH   G .   ? 0.35349 0.28951 0.20849 0.02894  -0.06133 -0.03393 342 HOH   B O    
5184 O  O    . HOH   G .   ? 0.42164 0.38205 0.30322 0.12939  0.09286  0.07332  343 HOH   B O    
5185 O  O    . HOH   G .   ? 0.33363 0.22607 0.25258 0.08333  0.02391  0.04483  344 HOH   B O    
5186 O  O    . HOH   G .   ? 0.29651 0.51852 0.49698 -0.03316 -0.08195 -0.12944 345 HOH   B O    
5187 O  O    A HOH   G .   ? 0.49698 0.75235 0.42652 0.03248  -0.15092 -0.13475 346 HOH   B O    
5188 O  O    . HOH   G .   ? 0.89396 0.88506 0.89457 -0.02093 0.00272  -0.02015 347 HOH   B O    
5189 O  O    . HOH   G .   ? 0.81713 0.57349 0.30701 0.10495  0.15488  0.13674  348 HOH   B O    
5190 O  O    . HOH   G .   ? 0.20548 0.16599 0.15257 -0.00232 -0.03425 0.02630  349 HOH   B O    
5191 O  O    . HOH   G .   ? 0.28985 0.51513 0.59834 -0.00228 -0.05424 -0.07360 350 HOH   B O    
5192 O  O    . HOH   G .   ? 0.60369 0.52289 0.37567 -0.05615 -0.01348 0.21865  351 HOH   B O    
5193 O  O    . HOH   G .   ? 0.41365 0.31463 0.32238 0.09021  -0.09209 -0.10141 352 HOH   B O    
5194 O  O    . HOH   G .   ? 0.36120 0.22740 0.27091 0.00649  -0.03993 -0.02678 353 HOH   B O    
5195 O  O    . HOH   G .   ? 0.42465 0.29723 0.37096 -0.07552 -0.06687 0.04432  354 HOH   B O    
5196 O  O    . HOH   G .   ? 0.41341 0.35006 0.68164 -0.10596 -0.17671 0.01903  355 HOH   B O    
5197 O  O    . HOH   G .   ? 0.55481 0.21369 0.74006 -0.08831 -0.06378 -0.01984 356 HOH   B O    
5198 O  O    . HOH   G .   ? 0.27606 0.15525 0.20704 -0.00345 -0.00968 0.01429  357 HOH   B O    
5199 O  O    . HOH   G .   ? 0.48126 0.43491 0.54850 -0.01276 0.07907  -0.01527 358 HOH   B O    
5200 O  O    . HOH   G .   ? 0.28715 0.23908 0.22062 -0.03835 -0.02600 0.02956  359 HOH   B O    
5201 O  O    . HOH   G .   ? 0.50233 0.35517 0.26515 -0.08233 -0.02644 0.04234  360 HOH   B O    
5202 O  O    . HOH   G .   ? 0.45441 0.39726 0.49997 0.11112  0.23275  0.20543  361 HOH   B O    
5203 O  O    . HOH   G .   ? 0.66301 0.36311 0.31468 -0.23755 0.16488  -0.05384 362 HOH   B O    
5204 O  O    . HOH   G .   ? 0.32098 0.24880 0.14783 0.03532  -0.02832 -0.00214 363 HOH   B O    
5205 O  O    . HOH   G .   ? 0.60126 0.42735 0.41678 -0.10508 0.05134  0.02407  364 HOH   B O    
5206 O  O    . HOH   G .   ? 0.32185 0.21074 0.25544 -0.07227 -0.06193 0.06546  365 HOH   B O    
5207 O  O    . HOH   G .   ? 0.39529 0.42617 0.63900 0.07500  0.04156  -0.07199 366 HOH   B O    
5208 O  O    . HOH   G .   ? 0.47713 0.33458 0.31267 -0.13607 -0.16419 0.12685  367 HOH   B O    
5209 O  O    . HOH   G .   ? 0.63036 0.57244 0.78921 -0.21636 -0.00537 -0.02799 368 HOH   B O    
5210 O  O    . HOH   G .   ? 0.33674 0.16278 0.20799 -0.02834 -0.06958 -0.03175 369 HOH   B O    
5211 O  O    . HOH   G .   ? 0.24481 0.17191 0.16492 -0.01524 -0.03700 0.00767  370 HOH   B O    
5212 O  O    . HOH   G .   ? 0.42342 0.23369 0.18479 -0.00045 -0.07798 0.00603  371 HOH   B O    
5213 O  O    . HOH   G .   ? 0.20286 0.15903 0.28507 0.00232  -0.02601 0.03649  372 HOH   B O    
5214 O  O    . HOH   G .   ? 0.37598 0.35282 0.22802 0.04309  -0.06511 0.08171  373 HOH   B O    
5215 O  O    . HOH   G .   ? 0.36374 0.26617 0.23017 0.04467  0.03427  0.01508  374 HOH   B O    
5216 O  O    . HOH   G .   ? 0.41550 0.23743 0.27803 -0.05476 0.07210  0.04606  375 HOH   B O    
5217 O  O    . HOH   G .   ? 0.24344 0.30296 0.25363 -0.01742 -0.01900 -0.00603 376 HOH   B O    
5218 O  O    . HOH   G .   ? 0.30235 0.29002 0.44778 0.02254  0.05179  0.10117  377 HOH   B O    
5219 O  O    . HOH   G .   ? 0.40660 0.20123 0.30564 -0.05248 -0.05742 0.09346  378 HOH   B O    
5220 O  O    . HOH   G .   ? 0.33205 0.22546 0.25836 -0.06415 -0.03653 -0.04151 379 HOH   B O    
5221 O  O    . HOH   G .   ? 0.34006 0.49669 0.43760 -0.04985 0.01144  0.10395  380 HOH   B O    
5222 O  O    B HOH   G .   ? 0.34631 0.34126 0.98498 -0.01733 0.09869  -0.06421 381 HOH   B O    
5223 O  O    . HOH   G .   ? 0.48317 0.24249 0.30795 0.01673  0.09193  0.12296  382 HOH   B O    
5224 O  O    . HOH   G .   ? 0.37707 0.28133 0.34649 -0.12077 -0.02613 0.01905  383 HOH   B O    
5225 O  O    . HOH   G .   ? 0.42103 0.35935 0.26310 0.14700  -0.05392 -0.03219 384 HOH   B O    
5226 O  O    . HOH   G .   ? 0.41655 0.20333 0.24613 -0.08652 0.00504  0.01214  385 HOH   B O    
5227 O  O    . HOH   G .   ? 0.47881 0.54840 0.21027 -0.05759 -0.11301 -0.03686 386 HOH   B O    
5228 O  O    . HOH   G .   ? 0.25664 0.45298 0.22975 -0.01370 -0.03024 -0.08297 387 HOH   B O    
5229 O  O    . HOH   G .   ? 0.35591 0.40703 0.19285 -0.03621 -0.05805 -0.00415 388 HOH   B O    
5230 O  O    . HOH   G .   ? 0.43214 0.36888 0.36884 -0.00431 -0.08722 0.07098  389 HOH   B O    
5231 O  O    . HOH   G .   ? 0.61368 0.42311 0.43090 0.05043  0.20701  -0.06390 390 HOH   B O    
5232 O  O    . HOH   G .   ? 0.50385 0.27188 0.46611 -0.07873 -0.16276 -0.01215 391 HOH   B O    
5233 O  O    . HOH   G .   ? 0.30821 0.51209 0.32163 0.08420  -0.02371 -0.11208 392 HOH   B O    
5234 O  O    . HOH   G .   ? 0.31059 0.89700 0.38667 -0.13075 0.02600  -0.14165 393 HOH   B O    
5235 O  O    . HOH   G .   ? 0.51719 0.35627 0.25654 -0.19378 0.00820  -0.06263 394 HOH   B O    
5236 O  O    . HOH   G .   ? 0.48806 0.58414 0.61717 0.24742  0.20379  0.30457  395 HOH   B O    
5237 O  O    . HOH   G .   ? 0.21898 0.35784 0.21269 -0.06268 0.05021  -0.08967 396 HOH   B O    
5238 O  O    . HOH   G .   ? 0.33834 0.32728 0.23558 0.08559  0.02589  0.05946  397 HOH   B O    
5239 O  O    . HOH   G .   ? 0.46858 0.46249 0.19163 0.08255  -0.03431 0.01043  398 HOH   B O    
5240 O  O    . HOH   G .   ? 0.31703 0.17346 0.19822 -0.03046 -0.05733 0.05201  399 HOH   B O    
5241 O  O    . HOH   G .   ? 0.35655 0.62475 0.20136 0.13216  0.05745  0.09347  400 HOH   B O    
5242 O  O    . HOH   G .   ? 0.49718 0.49700 0.30238 0.21266  0.15589  0.16225  401 HOH   B O    
5243 O  O    . HOH   G .   ? 0.38299 0.45630 0.56370 0.09243  -0.00172 0.15337  402 HOH   B O    
5244 O  O    . HOH   G .   ? 0.40984 0.36392 0.48555 0.06636  -0.11259 -0.20552 403 HOH   B O    
5245 O  O    . HOH   G .   ? 0.22809 0.27018 0.17518 -0.06486 0.06361  -0.07245 404 HOH   B O    
5246 O  O    . HOH   G .   ? 0.24652 0.41205 0.36783 0.02373  0.01533  0.14721  405 HOH   B O    
5247 O  O    . HOH   G .   ? 0.37070 0.41138 0.29444 0.02759  0.03232  -0.09382 406 HOH   B O    
5248 O  O    . HOH   G .   ? 0.26665 0.33024 0.18360 -0.06628 0.00904  -0.01242 407 HOH   B O    
5249 O  O    . HOH   G .   ? 0.28476 0.37659 0.54928 0.01317  -0.11800 0.06299  408 HOH   B O    
5250 O  O    . HOH   G .   ? 0.53329 0.23458 0.29291 0.09593  0.03610  -0.04861 409 HOH   B O    
5251 O  O    . HOH   G .   ? 0.48426 0.53373 0.48322 0.02449  0.02240  -0.04239 410 HOH   B O    
5252 O  O    . HOH   G .   ? 0.29104 0.60391 0.25434 -0.10367 -0.03772 0.10602  411 HOH   B O    
5253 O  O    . HOH   G .   ? 0.21527 0.28093 0.27572 -0.00982 0.06113  0.07783  412 HOH   B O    
5254 O  O    . HOH   G .   ? 0.26598 0.16798 0.17612 0.03270  -0.00186 0.03627  413 HOH   B O    
5255 O  O    . HOH   G .   ? 0.30221 0.36690 0.38481 0.01728  0.02479  0.01178  414 HOH   B O    
5256 O  O    . HOH   G .   ? 0.35710 0.27855 0.18564 -0.00884 -0.07143 -0.00877 415 HOH   B O    
5257 O  O    . HOH   G .   ? 0.34725 0.50184 0.55077 -0.08562 -0.02345 0.00485  416 HOH   B O    
5258 O  O    . HOH   G .   ? 0.42580 0.24696 0.23670 -0.13067 -0.11150 0.10087  417 HOH   B O    
5259 O  O    . HOH   G .   ? 0.49594 0.48490 1.04111 -0.08733 0.08915  -0.32122 418 HOH   B O    
5260 O  O    . HOH   G .   ? 0.42639 0.86419 0.38217 -0.26076 0.00780  0.09554  419 HOH   B O    
5261 O  O    . HOH   G .   ? 0.41561 0.38859 0.23699 -0.03537 -0.04574 0.08644  420 HOH   B O    
5262 O  O    . HOH   G .   ? 0.34775 0.34501 0.24815 -0.07419 0.04114  -0.08742 421 HOH   B O    
5263 O  O    . HOH   G .   ? 0.32855 0.38244 0.38640 0.07610  -0.03019 0.16186  422 HOH   B O    
5264 O  O    . HOH   G .   ? 0.31009 0.43430 0.24784 0.15847  0.08408  0.15855  423 HOH   B O    
5265 O  O    . HOH   G .   ? 0.40962 0.39681 0.38284 0.09276  0.07804  0.11732  424 HOH   B O    
5266 O  O    . HOH   G .   ? 0.35886 0.23016 0.22440 -0.06319 -0.05670 0.07261  425 HOH   B O    
5267 O  O    . HOH   G .   ? 0.29767 0.41745 0.18747 0.04092  -0.02231 -0.01585 426 HOH   B O    
5268 O  O    . HOH   G .   ? 0.49102 0.31440 0.28285 -0.13472 -0.03177 0.13435  427 HOH   B O    
5269 O  O    . HOH   G .   ? 0.43461 0.38719 0.33271 0.01038  -0.03476 0.08612  428 HOH   B O    
5270 O  O    . HOH   G .   ? 0.44461 0.71951 0.40260 -0.13376 0.07462  -0.28607 429 HOH   B O    
5271 O  O    . HOH   G .   ? 0.26842 0.48569 0.87153 -0.01178 -0.02002 -0.30901 430 HOH   B O    
5272 O  O    . HOH   G .   ? 0.37037 0.55176 0.62885 -0.10869 -0.08007 0.31836  431 HOH   B O    
5273 O  O    . HOH   G .   ? 0.49846 0.32025 0.92182 -0.02803 0.06547  -0.07715 432 HOH   B O    
5274 O  O    . HOH   G .   ? 0.40799 0.29710 0.33115 0.05501  0.11472  0.08199  433 HOH   B O    
5275 O  O    . HOH   G .   ? 0.35949 0.27381 0.20678 0.09418  -0.01351 -0.01264 434 HOH   B O    
5276 O  O    . HOH   G .   ? 0.53869 0.39781 0.38769 0.06549  0.07336  0.22205  435 HOH   B O    
5277 O  O    . HOH   G .   ? 0.45433 0.87141 0.50739 -0.21478 -0.19255 0.27934  436 HOH   B O    
5278 O  O    . HOH   G .   ? 0.53003 0.48489 0.56534 0.13584  -0.02007 0.11274  437 HOH   B O    
5279 O  O    . HOH   G .   ? 0.51883 0.42894 0.59937 0.13375  -0.14946 0.04293  438 HOH   B O    
5280 O  O    . HOH   G .   ? 0.81950 0.92436 0.34966 0.29834  0.00336  0.03702  439 HOH   B O    
5281 O  O    . HOH   G .   ? 0.31177 0.32953 0.50167 0.04363  0.01032  0.20274  440 HOH   B O    
5282 O  O    . HOH   G .   ? 0.46803 0.38738 0.40561 -0.01876 0.02285  -0.02751 441 HOH   B O    
5283 O  O    . HOH   G .   ? 0.60902 0.47528 0.92938 -0.10477 0.25816  0.17231  442 HOH   B O    
5284 O  O    . HOH   G .   ? 0.60136 0.56741 0.59918 -0.05791 -0.02136 0.00560  443 HOH   B O    
5285 O  O    . HOH   G .   ? 1.16353 1.15625 1.17017 0.00623  -0.02127 -0.00354 444 HOH   B O    
5286 O  O    . HOH   G .   ? 0.67253 0.64675 0.46875 -0.13358 0.02209  0.23845  445 HOH   B O    
5287 O  O    . HOH   G .   ? 0.45232 0.57636 0.47988 0.00125  -0.00349 0.06303  446 HOH   B O    
5288 O  O    . HOH   G .   ? 0.36454 0.68824 0.37478 0.00477  0.16187  -0.06195 447 HOH   B O    
5289 O  O    . HOH   G .   ? 0.43265 0.51789 0.79867 -0.17587 -0.26331 0.33964  448 HOH   B O    
5290 O  O    A HOH   G .   ? 0.36999 0.70329 0.88006 -0.11330 0.18562  0.14047  449 HOH   B O    
5291 O  O    . HOH   G .   ? 0.67805 0.53031 0.60757 0.00944  0.03088  0.02933  450 HOH   B O    
5292 O  O    . HOH   G .   ? 0.42449 0.54946 0.26933 0.07266  0.00419  -0.00323 451 HOH   B O    
5293 O  O    . HOH   G .   ? 0.70661 0.40686 0.22024 -0.23297 0.06794  -0.02597 452 HOH   B O    
5294 O  O    . HOH   G .   ? 0.65736 0.58600 0.60333 0.07986  -0.00219 -0.01037 453 HOH   B O    
5295 O  O    . HOH   G .   ? 0.58415 0.49714 0.54387 -0.08318 0.03017  0.02876  454 HOH   B O    
5296 O  O    . HOH   G .   ? 0.29561 0.40434 0.43434 0.03820  -0.04583 0.13385  455 HOH   B O    
5297 O  O    . HOH   G .   ? 0.51558 0.31665 0.46012 0.10808  -0.03193 0.04062  456 HOH   B O    
5298 O  O    . HOH   G .   ? 1.05826 1.05061 1.06267 0.00693  -0.01803 0.03555  457 HOH   B O    
5299 O  O    . HOH   G .   ? 0.35475 0.27997 0.45059 0.00258  -0.00522 0.12241  458 HOH   B O    
5300 O  O    . HOH   G .   ? 0.52385 0.62082 0.51703 -0.03695 0.11688  0.00065  459 HOH   B O    
5301 O  O    . HOH   G .   ? 0.54790 0.55189 0.56617 0.05646  -0.01500 0.03017  460 HOH   B O    
5302 O  O    . HOH   G .   ? 0.47158 0.36871 0.46524 -0.06250 0.00116  -0.09875 461 HOH   B O    
5303 O  O    . HOH   G .   ? 0.36805 0.60963 0.48455 0.15893  0.02355  0.05603  462 HOH   B O    
5304 O  O    . HOH   G .   ? 0.53722 0.52301 0.43024 -0.09674 0.01627  0.08952  463 HOH   B O    
5305 O  O    . HOH   G .   ? 0.43053 0.44523 0.46489 0.06911  -0.06290 -0.04756 464 HOH   B O    
5306 O  O    . HOH   G .   ? 0.52852 0.40176 0.31043 0.09456  -0.09468 -0.01346 465 HOH   B O    
5307 O  O    . HOH   G .   ? 0.50153 0.50936 0.57609 -0.09973 0.03815  0.00370  466 HOH   B O    
5308 O  O    . HOH   G .   ? 0.57603 0.46746 0.28451 0.15237  -0.05902 -0.05439 467 HOH   B O    
5309 O  O    . HOH   G .   ? 0.51835 0.26811 0.57811 0.09230  -0.14189 -0.07886 468 HOH   B O    
5310 O  O    . HOH   G .   ? 0.39119 0.51896 0.55317 0.02208  0.03955  -0.09607 469 HOH   B O    
5311 O  O    . HOH   G .   ? 0.54875 0.44000 0.50144 0.04001  -0.10867 0.09731  470 HOH   B O    
5312 O  O    . HOH   G .   ? 0.42401 0.41553 0.39637 0.07214  0.02404  0.01357  471 HOH   B O    
5313 O  O    . HOH   G .   ? 0.25948 0.31091 0.45815 0.00523  -0.04909 0.17356  472 HOH   B O    
5314 O  O    . HOH   G .   ? 0.36012 0.30725 0.85266 0.08850  0.19512  0.08533  473 HOH   B O    
5315 O  O    . HOH   G .   ? 0.52569 0.49475 0.32349 0.04809  0.01522  -0.06347 474 HOH   B O    
5316 O  O    . HOH   G .   ? 0.34550 0.23905 0.38672 0.02301  0.05329  0.03886  475 HOH   B O    
5317 O  O    . HOH   G .   ? 0.29509 0.41196 0.66977 -0.03093 -0.08400 0.28968  476 HOH   B O    
5318 O  O    . HOH   G .   ? 1.18967 1.18674 1.19208 0.00163  0.00474  0.01158  477 HOH   B O    
5319 O  O    . HOH   G .   ? 0.54151 0.27360 0.48046 -0.02738 0.09891  -0.03263 478 HOH   B O    
5320 O  O    . HOH   G .   ? 0.66834 0.62901 0.64204 0.01392  0.02353  0.01578  479 HOH   B O    
5321 O  O    . HOH   G .   ? 0.66478 0.45877 0.28268 0.17446  0.00246  0.01327  480 HOH   B O    
5322 O  O    . HOH   G .   ? 0.53642 0.51596 0.42324 -0.08421 0.07711  0.04222  481 HOH   B O    
5323 O  O    . HOH   G .   ? 0.47613 0.54662 0.37421 0.17610  -0.05564 -0.06947 482 HOH   B O    
5324 O  O    . HOH   G .   ? 0.54182 0.69410 0.32724 0.15574  -0.17453 -0.13086 483 HOH   B O    
5325 O  O    B HOH   G .   ? 0.67630 0.78577 0.59772 -0.20312 0.27564  0.16221  484 HOH   B O    
5326 O  O    . HOH   G .   ? 0.66927 0.45976 0.27841 -0.08459 0.03472  -0.00363 485 HOH   B O    
5327 O  O    . HOH   G .   ? 0.58314 0.73143 0.39327 0.07241  -0.04292 -0.02531 486 HOH   B O    
5328 O  O    . HOH   G .   ? 0.59014 0.38708 0.74803 -0.03532 0.11957  -0.23206 487 HOH   B O    
5329 O  O    . HOH   G .   ? 0.57192 0.18039 0.22778 -0.03142 -0.11631 -0.02477 488 HOH   B O    
5330 O  O    . HOH   G .   ? 0.58467 0.58087 0.55061 -0.00936 -0.08289 0.04096  489 HOH   B O    
5331 O  O    . HOH   G .   ? 0.73789 0.51451 0.30670 -0.30064 0.08639  -0.02905 490 HOH   B O    
5332 O  O    . HOH   G .   ? 0.51384 0.41364 0.45839 -0.05186 -0.13614 0.10907  491 HOH   B O    
# 
