data_7HDC
# 
_entry.id   7HDC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   7HDC         pdb_00007hdc 10.2210/pdb7hdc/pdb 
WWPDB D_1001407330 ?            ?                   
# 
_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       2025-06-11 
_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.entry_id                        7HDC 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
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 'Non-structural protein 3'                                                              18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn '(1R,2R)-1-(4-chlorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propane-1,3-diol' 318.758   2   ? ? ? ? 
3 non-polymer syn '(1R,2S)-1-(4-chlorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propane-1,3-diol' 318.758   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                          35.453    1   ? ? ? ? 
5 water       nat water                                                                                   18.015    424 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_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       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_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 '(1R,2R)-1-(4-chlorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propane-1,3-diol' A1A72 
3 '(1R,2S)-1-(4-chlorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propane-1,3-diol' A1A73 
4 'CHLORIDE ION'                                                                          CL    
5 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   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU 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                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_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 
A1A72 non-polymer         . '(1R,2R)-1-(4-chlorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propane-1,3-diol' ? 
'C15 H15 Cl N4 O2' 318.758 
A1A73 non-polymer         . '(1R,2S)-1-(4-chlorophenyl)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]propane-1,3-diol' ? 
'C15 H15 Cl N4 O2' 318.758 
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 
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   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1A72 1   201 201  A1A72 LA1 A . 
D 3 A1A73 1   202 301  A1A73 LA2 A . 
E 2 A1A72 1   203 401  A1A72 LA3 A . 
F 4 CL    1   204 1    CL    CL  A . 
G 5 HOH   1   301 1313 HOH   HOH A . 
G 5 HOH   2   302 1289 HOH   HOH A . 
G 5 HOH   3   303 292  HOH   HOH A . 
G 5 HOH   4   304 409  HOH   HOH A . 
G 5 HOH   5   305 625  HOH   HOH A . 
G 5 HOH   6   306 661  HOH   HOH A . 
G 5 HOH   7   307 1301 HOH   HOH A . 
G 5 HOH   8   308 209  HOH   HOH A . 
G 5 HOH   9   309 109  HOH   HOH A . 
G 5 HOH   10  310 196  HOH   HOH A . 
G 5 HOH   11  311 1310 HOH   HOH A . 
G 5 HOH   12  312 7    HOH   HOH A . 
G 5 HOH   13  313 93   HOH   HOH A . 
G 5 HOH   14  314 229  HOH   HOH A . 
G 5 HOH   15  315 337  HOH   HOH A . 
G 5 HOH   16  316 1283 HOH   HOH A . 
G 5 HOH   17  317 76   HOH   HOH A . 
G 5 HOH   18  318 393  HOH   HOH A . 
G 5 HOH   19  319 192  HOH   HOH A . 
G 5 HOH   20  320 86   HOH   HOH A . 
G 5 HOH   21  321 136  HOH   HOH A . 
G 5 HOH   22  322 151  HOH   HOH A . 
G 5 HOH   23  323 236  HOH   HOH A . 
G 5 HOH   24  324 124  HOH   HOH A . 
G 5 HOH   25  325 49   HOH   HOH A . 
G 5 HOH   26  326 247  HOH   HOH A . 
G 5 HOH   27  327 96   HOH   HOH A . 
G 5 HOH   28  328 1295 HOH   HOH A . 
G 5 HOH   29  329 57   HOH   HOH A . 
G 5 HOH   30  330 105  HOH   HOH A . 
G 5 HOH   31  331 405  HOH   HOH A . 
G 5 HOH   32  332 662  HOH   HOH A . 
G 5 HOH   33  333 15   HOH   HOH A . 
G 5 HOH   34  334 17   HOH   HOH A . 
G 5 HOH   35  335 9    HOH   HOH A . 
G 5 HOH   36  336 164  HOH   HOH A . 
G 5 HOH   37  337 469  HOH   HOH A . 
G 5 HOH   38  338 225  HOH   HOH A . 
G 5 HOH   39  339 1    HOH   HOH A . 
G 5 HOH   40  340 42   HOH   HOH A . 
G 5 HOH   41  341 140  HOH   HOH A . 
G 5 HOH   42  342 155  HOH   HOH A . 
G 5 HOH   43  343 320  HOH   HOH A . 
G 5 HOH   44  344 36   HOH   HOH A . 
G 5 HOH   45  345 1300 HOH   HOH A . 
G 5 HOH   46  346 241  HOH   HOH A . 
G 5 HOH   47  347 354  HOH   HOH A . 
G 5 HOH   48  348 18   HOH   HOH A . 
G 5 HOH   49  349 102  HOH   HOH A . 
G 5 HOH   50  350 1290 HOH   HOH A . 
G 5 HOH   51  351 165  HOH   HOH A . 
G 5 HOH   52  352 153  HOH   HOH A . 
G 5 HOH   53  353 939  HOH   HOH A . 
G 5 HOH   54  354 139  HOH   HOH A . 
G 5 HOH   55  355 630  HOH   HOH A . 
G 5 HOH   56  356 964  HOH   HOH A . 
G 5 HOH   57  357 92   HOH   HOH A . 
G 5 HOH   58  358 17   HOH   HOH A . 
G 5 HOH   59  359 39   HOH   HOH A . 
G 5 HOH   60  360 169  HOH   HOH A . 
G 5 HOH   61  361 2    HOH   HOH A . 
G 5 HOH   62  362 66   HOH   HOH A . 
G 5 HOH   63  363 19   HOH   HOH A . 
G 5 HOH   64  364 1308 HOH   HOH A . 
G 5 HOH   65  365 26   HOH   HOH A . 
G 5 HOH   66  366 396  HOH   HOH A . 
G 5 HOH   67  367 162  HOH   HOH A . 
G 5 HOH   68  368 132  HOH   HOH A . 
G 5 HOH   69  369 4    HOH   HOH A . 
G 5 HOH   70  370 81   HOH   HOH A . 
G 5 HOH   71  371 5    HOH   HOH A . 
G 5 HOH   72  372 159  HOH   HOH A . 
G 5 HOH   73  373 138  HOH   HOH A . 
G 5 HOH   74  374 56   HOH   HOH A . 
G 5 HOH   75  375 45   HOH   HOH A . 
G 5 HOH   76  376 1286 HOH   HOH A . 
G 5 HOH   77  377 381  HOH   HOH A . 
G 5 HOH   78  378 296  HOH   HOH A . 
G 5 HOH   79  379 199  HOH   HOH A . 
G 5 HOH   80  380 1309 HOH   HOH A . 
G 5 HOH   81  381 154  HOH   HOH A . 
G 5 HOH   82  382 70   HOH   HOH A . 
G 5 HOH   83  383 134  HOH   HOH A . 
G 5 HOH   84  384 351  HOH   HOH A . 
G 5 HOH   85  385 12   HOH   HOH A . 
G 5 HOH   86  386 3    HOH   HOH A . 
G 5 HOH   87  387 186  HOH   HOH A . 
G 5 HOH   88  388 218  HOH   HOH A . 
G 5 HOH   89  389 46   HOH   HOH A . 
G 5 HOH   90  390 3    HOH   HOH A . 
G 5 HOH   91  391 366  HOH   HOH A . 
G 5 HOH   92  392 74   HOH   HOH A . 
G 5 HOH   93  393 1275 HOH   HOH A . 
G 5 HOH   94  394 33   HOH   HOH A . 
G 5 HOH   95  395 148  HOH   HOH A . 
G 5 HOH   96  396 24   HOH   HOH A . 
G 5 HOH   97  397 21   HOH   HOH A . 
G 5 HOH   98  398 27   HOH   HOH A . 
G 5 HOH   99  399 35   HOH   HOH A . 
G 5 HOH   100 400 58   HOH   HOH A . 
G 5 HOH   101 401 83   HOH   HOH A . 
G 5 HOH   102 402 116  HOH   HOH A . 
G 5 HOH   103 403 333  HOH   HOH A . 
G 5 HOH   104 404 195  HOH   HOH A . 
G 5 HOH   105 405 582  HOH   HOH A . 
G 5 HOH   106 406 4    HOH   HOH A . 
G 5 HOH   107 407 1315 HOH   HOH A . 
G 5 HOH   108 408 67   HOH   HOH A . 
G 5 HOH   109 409 78   HOH   HOH A . 
G 5 HOH   110 410 6    HOH   HOH A . 
G 5 HOH   111 411 34   HOH   HOH A . 
G 5 HOH   112 412 121  HOH   HOH A . 
G 5 HOH   113 413 6    HOH   HOH A . 
G 5 HOH   114 414 16   HOH   HOH A . 
G 5 HOH   115 415 68   HOH   HOH A . 
G 5 HOH   116 416 397  HOH   HOH A . 
G 5 HOH   117 417 461  HOH   HOH A . 
G 5 HOH   118 418 1068 HOH   HOH A . 
G 5 HOH   119 419 156  HOH   HOH A . 
G 5 HOH   120 420 123  HOH   HOH A . 
G 5 HOH   121 421 303  HOH   HOH A . 
G 5 HOH   122 422 493  HOH   HOH A . 
G 5 HOH   123 423 7    HOH   HOH A . 
G 5 HOH   124 424 125  HOH   HOH A . 
G 5 HOH   125 425 25   HOH   HOH A . 
G 5 HOH   126 426 281  HOH   HOH A . 
G 5 HOH   127 427 122  HOH   HOH A . 
G 5 HOH   128 428 53   HOH   HOH A . 
G 5 HOH   129 429 85   HOH   HOH A . 
G 5 HOH   130 430 278  HOH   HOH A . 
G 5 HOH   131 431 1279 HOH   HOH A . 
G 5 HOH   132 432 8    HOH   HOH A . 
G 5 HOH   133 433 95   HOH   HOH A . 
G 5 HOH   134 434 51   HOH   HOH A . 
G 5 HOH   135 435 212  HOH   HOH A . 
G 5 HOH   136 436 73   HOH   HOH A . 
G 5 HOH   137 437 10   HOH   HOH A . 
G 5 HOH   138 438 18   HOH   HOH A . 
G 5 HOH   139 439 16   HOH   HOH A . 
G 5 HOH   140 440 1222 HOH   HOH A . 
G 5 HOH   141 441 576  HOH   HOH A . 
G 5 HOH   142 442 1238 HOH   HOH A . 
G 5 HOH   143 443 115  HOH   HOH A . 
G 5 HOH   144 444 71   HOH   HOH A . 
G 5 HOH   145 445 188  HOH   HOH A . 
G 5 HOH   146 446 1094 HOH   HOH A . 
G 5 HOH   147 447 80   HOH   HOH A . 
G 5 HOH   148 448 40   HOH   HOH A . 
G 5 HOH   149 449 1296 HOH   HOH A . 
G 5 HOH   150 450 94   HOH   HOH A . 
G 5 HOH   151 451 12   HOH   HOH A . 
G 5 HOH   152 452 944  HOH   HOH A . 
G 5 HOH   153 453 952  HOH   HOH A . 
G 5 HOH   154 454 15   HOH   HOH A . 
G 5 HOH   155 455 5    HOH   HOH A . 
G 5 HOH   156 456 104  HOH   HOH A . 
G 5 HOH   157 457 97   HOH   HOH A . 
G 5 HOH   158 458 1299 HOH   HOH A . 
G 5 HOH   159 459 330  HOH   HOH A . 
G 5 HOH   160 460 79   HOH   HOH A . 
G 5 HOH   161 461 1119 HOH   HOH A . 
G 5 HOH   162 462 509  HOH   HOH A . 
G 5 HOH   163 463 107  HOH   HOH A . 
G 5 HOH   164 464 1134 HOH   HOH A . 
G 5 HOH   165 465 163  HOH   HOH A . 
G 5 HOH   166 466 726  HOH   HOH A . 
G 5 HOH   167 467 408  HOH   HOH A . 
G 5 HOH   168 468 1189 HOH   HOH A . 
G 5 HOH   169 469 280  HOH   HOH A . 
G 5 HOH   170 470 1276 HOH   HOH A . 
G 5 HOH   171 471 756  HOH   HOH A . 
G 5 HOH   172 472 361  HOH   HOH A . 
G 5 HOH   173 473 556  HOH   HOH A . 
G 5 HOH   174 474 63   HOH   HOH A . 
G 5 HOH   175 475 319  HOH   HOH A . 
G 5 HOH   176 476 126  HOH   HOH A . 
G 5 HOH   177 477 342  HOH   HOH A . 
G 5 HOH   178 478 801  HOH   HOH A . 
G 5 HOH   179 479 1307 HOH   HOH A . 
G 5 HOH   180 480 250  HOH   HOH A . 
G 5 HOH   181 481 135  HOH   HOH A . 
G 5 HOH   182 482 1306 HOH   HOH A . 
G 5 HOH   183 483 370  HOH   HOH A . 
G 5 HOH   184 484 1287 HOH   HOH A . 
G 5 HOH   185 485 711  HOH   HOH A . 
G 5 HOH   186 486 695  HOH   HOH A . 
G 5 HOH   187 487 674  HOH   HOH A . 
G 5 HOH   188 488 267  HOH   HOH A . 
G 5 HOH   189 489 919  HOH   HOH A . 
G 5 HOH   190 490 202  HOH   HOH A . 
G 5 HOH   191 491 224  HOH   HOH A . 
G 5 HOH   192 492 521  HOH   HOH A . 
G 5 HOH   193 493 315  HOH   HOH A . 
G 5 HOH   194 494 1314 HOH   HOH A . 
G 5 HOH   195 495 309  HOH   HOH A . 
G 5 HOH   196 496 152  HOH   HOH A . 
G 5 HOH   197 497 318  HOH   HOH A . 
G 5 HOH   198 498 805  HOH   HOH A . 
G 5 HOH   199 499 331  HOH   HOH A . 
G 5 HOH   200 500 981  HOH   HOH A . 
G 5 HOH   201 501 263  HOH   HOH A . 
G 5 HOH   202 502 941  HOH   HOH A . 
G 5 HOH   203 503 1284 HOH   HOH A . 
G 5 HOH   204 504 208  HOH   HOH A . 
G 5 HOH   205 505 1071 HOH   HOH A . 
G 5 HOH   206 506 13   HOH   HOH A . 
G 5 HOH   207 507 8    HOH   HOH A . 
G 5 HOH   208 508 180  HOH   HOH A . 
G 5 HOH   209 509 350  HOH   HOH A . 
G 5 HOH   210 510 326  HOH   HOH A . 
G 5 HOH   211 511 14   HOH   HOH A . 
G 5 HOH   212 512 363  HOH   HOH A . 
G 5 HOH   213 513 356  HOH   HOH A . 
G 5 HOH   214 514 371  HOH   HOH A . 
G 5 HOH   215 515 313  HOH   HOH A . 
G 5 HOH   216 516 429  HOH   HOH A . 
G 5 HOH   217 517 185  HOH   HOH A . 
G 5 HOH   218 518 772  HOH   HOH A . 
G 5 HOH   219 519 376  HOH   HOH A . 
G 5 HOH   220 520 1074 HOH   HOH A . 
G 5 HOH   221 521 11   HOH   HOH A . 
G 5 HOH   222 522 1292 HOH   HOH A . 
G 5 HOH   223 523 346  HOH   HOH A . 
G 5 HOH   224 524 1078 HOH   HOH A . 
H 5 HOH   1   201 64   HOH   HOH B . 
H 5 HOH   2   202 531  HOH   HOH B . 
H 5 HOH   3   203 549  HOH   HOH B . 
H 5 HOH   4   204 398  HOH   HOH B . 
H 5 HOH   5   205 240  HOH   HOH B . 
H 5 HOH   6   206 358  HOH   HOH B . 
H 5 HOH   7   207 1249 HOH   HOH B . 
H 5 HOH   8   208 364  HOH   HOH B . 
H 5 HOH   9   209 758  HOH   HOH B . 
H 5 HOH   10  210 654  HOH   HOH B . 
H 5 HOH   11  211 120  HOH   HOH B . 
H 5 HOH   12  212 353  HOH   HOH B . 
H 5 HOH   13  213 452  HOH   HOH B . 
H 5 HOH   14  214 900  HOH   HOH B . 
H 5 HOH   15  215 264  HOH   HOH B . 
H 5 HOH   16  216 743  HOH   HOH B . 
H 5 HOH   17  217 232  HOH   HOH B . 
H 5 HOH   18  218 50   HOH   HOH B . 
H 5 HOH   19  219 1140 HOH   HOH B . 
H 5 HOH   20  220 75   HOH   HOH B . 
H 5 HOH   21  221 282  HOH   HOH B . 
H 5 HOH   22  222 131  HOH   HOH B . 
H 5 HOH   23  223 1312 HOH   HOH B . 
H 5 HOH   24  224 332  HOH   HOH B . 
H 5 HOH   25  225 82   HOH   HOH B . 
H 5 HOH   26  226 444  HOH   HOH B . 
H 5 HOH   27  227 54   HOH   HOH B . 
H 5 HOH   28  228 205  HOH   HOH B . 
H 5 HOH   29  229 343  HOH   HOH B . 
H 5 HOH   30  230 1278 HOH   HOH B . 
H 5 HOH   31  231 276  HOH   HOH B . 
H 5 HOH   32  232 128  HOH   HOH B . 
H 5 HOH   33  233 272  HOH   HOH B . 
H 5 HOH   34  234 127  HOH   HOH B . 
H 5 HOH   35  235 723  HOH   HOH B . 
H 5 HOH   36  236 110  HOH   HOH B . 
H 5 HOH   37  237 143  HOH   HOH B . 
H 5 HOH   38  238 181  HOH   HOH B . 
H 5 HOH   39  239 69   HOH   HOH B . 
H 5 HOH   40  240 60   HOH   HOH B . 
H 5 HOH   41  241 325  HOH   HOH B . 
H 5 HOH   42  242 1    HOH   HOH B . 
H 5 HOH   43  243 9    HOH   HOH B . 
H 5 HOH   44  244 129  HOH   HOH B . 
H 5 HOH   45  245 300  HOH   HOH B . 
H 5 HOH   46  246 14   HOH   HOH B . 
H 5 HOH   47  247 166  HOH   HOH B . 
H 5 HOH   48  248 133  HOH   HOH B . 
H 5 HOH   49  249 144  HOH   HOH B . 
H 5 HOH   50  250 52   HOH   HOH B . 
H 5 HOH   51  251 172  HOH   HOH B . 
H 5 HOH   52  252 30   HOH   HOH B . 
H 5 HOH   53  253 103  HOH   HOH B . 
H 5 HOH   54  254 47   HOH   HOH B . 
H 5 HOH   55  255 150  HOH   HOH B . 
H 5 HOH   56  256 72   HOH   HOH B . 
H 5 HOH   57  257 271  HOH   HOH B . 
H 5 HOH   58  258 31   HOH   HOH B . 
H 5 HOH   59  259 243  HOH   HOH B . 
H 5 HOH   60  260 391  HOH   HOH B . 
H 5 HOH   61  261 10   HOH   HOH B . 
H 5 HOH   62  262 41   HOH   HOH B . 
H 5 HOH   63  263 347  HOH   HOH B . 
H 5 HOH   64  264 302  HOH   HOH B . 
H 5 HOH   65  265 59   HOH   HOH B . 
H 5 HOH   66  266 231  HOH   HOH B . 
H 5 HOH   67  267 20   HOH   HOH B . 
H 5 HOH   68  268 252  HOH   HOH B . 
H 5 HOH   69  269 61   HOH   HOH B . 
H 5 HOH   70  270 84   HOH   HOH B . 
H 5 HOH   71  271 62   HOH   HOH B . 
H 5 HOH   72  272 117  HOH   HOH B . 
H 5 HOH   73  273 147  HOH   HOH B . 
H 5 HOH   74  274 114  HOH   HOH B . 
H 5 HOH   75  275 11   HOH   HOH B . 
H 5 HOH   76  276 287  HOH   HOH B . 
H 5 HOH   77  277 242  HOH   HOH B . 
H 5 HOH   78  278 175  HOH   HOH B . 
H 5 HOH   79  279 77   HOH   HOH B . 
H 5 HOH   80  280 1277 HOH   HOH B . 
H 5 HOH   81  281 1106 HOH   HOH B . 
H 5 HOH   82  282 235  HOH   HOH B . 
H 5 HOH   83  283 43   HOH   HOH B . 
H 5 HOH   84  284 221  HOH   HOH B . 
H 5 HOH   85  285 22   HOH   HOH B . 
H 5 HOH   86  286 13   HOH   HOH B . 
H 5 HOH   87  287 1305 HOH   HOH B . 
H 5 HOH   88  288 1066 HOH   HOH B . 
H 5 HOH   89  289 137  HOH   HOH B . 
H 5 HOH   90  290 89   HOH   HOH B . 
H 5 HOH   91  291 106  HOH   HOH B . 
H 5 HOH   92  292 416  HOH   HOH B . 
H 5 HOH   93  293 311  HOH   HOH B . 
H 5 HOH   94  294 112  HOH   HOH B . 
H 5 HOH   95  295 99   HOH   HOH B . 
H 5 HOH   96  296 387  HOH   HOH B . 
H 5 HOH   97  297 316  HOH   HOH B . 
H 5 HOH   98  298 299  HOH   HOH B . 
H 5 HOH   99  299 297  HOH   HOH B . 
H 5 HOH   100 300 160  HOH   HOH B . 
H 5 HOH   101 301 88   HOH   HOH B . 
H 5 HOH   102 302 216  HOH   HOH B . 
H 5 HOH   103 303 101  HOH   HOH B . 
H 5 HOH   104 304 141  HOH   HOH B . 
H 5 HOH   105 305 38   HOH   HOH B . 
H 5 HOH   106 306 170  HOH   HOH B . 
H 5 HOH   107 307 220  HOH   HOH B . 
H 5 HOH   108 308 635  HOH   HOH B . 
H 5 HOH   109 309 48   HOH   HOH B . 
H 5 HOH   110 310 32   HOH   HOH B . 
H 5 HOH   111 311 215  HOH   HOH B . 
H 5 HOH   112 312 118  HOH   HOH B . 
H 5 HOH   113 313 1274 HOH   HOH B . 
H 5 HOH   114 314 142  HOH   HOH B . 
H 5 HOH   115 315 37   HOH   HOH B . 
H 5 HOH   116 316 1126 HOH   HOH B . 
H 5 HOH   117 317 91   HOH   HOH B . 
H 5 HOH   118 318 197  HOH   HOH B . 
H 5 HOH   119 319 1285 HOH   HOH B . 
H 5 HOH   120 320 23   HOH   HOH B . 
H 5 HOH   121 321 177  HOH   HOH B . 
H 5 HOH   122 322 44   HOH   HOH B . 
H 5 HOH   123 323 28   HOH   HOH B . 
H 5 HOH   124 324 1291 HOH   HOH B . 
H 5 HOH   125 325 341  HOH   HOH B . 
H 5 HOH   126 326 704  HOH   HOH B . 
H 5 HOH   127 327 100  HOH   HOH B . 
H 5 HOH   128 328 182  HOH   HOH B . 
H 5 HOH   129 329 334  HOH   HOH B . 
H 5 HOH   130 330 55   HOH   HOH B . 
H 5 HOH   131 331 29   HOH   HOH B . 
H 5 HOH   132 332 717  HOH   HOH B . 
H 5 HOH   133 333 161  HOH   HOH B . 
H 5 HOH   134 334 98   HOH   HOH B . 
H 5 HOH   135 335 339  HOH   HOH B . 
H 5 HOH   136 336 1294 HOH   HOH B . 
H 5 HOH   137 337 65   HOH   HOH B . 
H 5 HOH   138 338 207  HOH   HOH B . 
H 5 HOH   139 339 234  HOH   HOH B . 
H 5 HOH   140 340 619  HOH   HOH B . 
H 5 HOH   141 341 1293 HOH   HOH B . 
H 5 HOH   142 342 445  HOH   HOH B . 
H 5 HOH   143 343 178  HOH   HOH B . 
H 5 HOH   144 344 960  HOH   HOH B . 
H 5 HOH   145 345 362  HOH   HOH B . 
H 5 HOH   146 346 90   HOH   HOH B . 
H 5 HOH   147 347 463  HOH   HOH B . 
H 5 HOH   148 348 1304 HOH   HOH B . 
H 5 HOH   149 349 191  HOH   HOH B . 
H 5 HOH   150 350 304  HOH   HOH B . 
H 5 HOH   151 351 87   HOH   HOH B . 
H 5 HOH   152 352 335  HOH   HOH B . 
H 5 HOH   153 353 623  HOH   HOH B . 
H 5 HOH   154 354 1046 HOH   HOH B . 
H 5 HOH   155 355 203  HOH   HOH B . 
H 5 HOH   156 356 1280 HOH   HOH B . 
H 5 HOH   157 357 290  HOH   HOH B . 
H 5 HOH   158 358 1077 HOH   HOH B . 
H 5 HOH   159 359 541  HOH   HOH B . 
H 5 HOH   160 360 479  HOH   HOH B . 
H 5 HOH   161 361 389  HOH   HOH B . 
H 5 HOH   162 362 718  HOH   HOH B . 
H 5 HOH   163 363 283  HOH   HOH B . 
H 5 HOH   164 364 1072 HOH   HOH B . 
H 5 HOH   165 365 1316 HOH   HOH B . 
H 5 HOH   166 366 898  HOH   HOH B . 
H 5 HOH   167 367 340  HOH   HOH B . 
H 5 HOH   168 368 291  HOH   HOH B . 
H 5 HOH   169 369 373  HOH   HOH B . 
H 5 HOH   170 370 667  HOH   HOH B . 
H 5 HOH   171 371 1303 HOH   HOH B . 
H 5 HOH   172 372 615  HOH   HOH B . 
H 5 HOH   173 373 310  HOH   HOH B . 
H 5 HOH   174 374 190  HOH   HOH B . 
H 5 HOH   175 375 431  HOH   HOH B . 
H 5 HOH   176 376 183  HOH   HOH B . 
H 5 HOH   177 377 1173 HOH   HOH B . 
H 5 HOH   178 378 1163 HOH   HOH B . 
H 5 HOH   179 379 149  HOH   HOH B . 
H 5 HOH   180 380 1000 HOH   HOH B . 
H 5 HOH   181 381 418  HOH   HOH B . 
H 5 HOH   182 382 176  HOH   HOH B . 
H 5 HOH   183 383 424  HOH   HOH B . 
H 5 HOH   184 384 1311 HOH   HOH B . 
H 5 HOH   185 385 1298 HOH   HOH B . 
H 5 HOH   186 386 491  HOH   HOH B . 
H 5 HOH   187 387 470  HOH   HOH B . 
H 5 HOH   188 388 248  HOH   HOH B . 
H 5 HOH   189 389 265  HOH   HOH B . 
H 5 HOH   190 390 184  HOH   HOH B . 
H 5 HOH   191 391 360  HOH   HOH B . 
H 5 HOH   192 392 410  HOH   HOH B . 
H 5 HOH   193 393 355  HOH   HOH B . 
H 5 HOH   194 394 566  HOH   HOH B . 
H 5 HOH   195 395 274  HOH   HOH B . 
H 5 HOH   196 396 314  HOH   HOH B . 
H 5 HOH   197 397 157  HOH   HOH B . 
H 5 HOH   198 398 792  HOH   HOH B . 
H 5 HOH   199 399 321  HOH   HOH B . 
H 5 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HDC 
_cell.length_a           88.778 
_cell.length_b           88.778 
_cell.length_c           39.492 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HDC 
_symmetry.space_group_name_H-M             'P 43' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                78 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HDC 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.63 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HDC 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.390 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   164935 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.038 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.700 
_reflns.B_iso_Wilson_estimate        12.020 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.041 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1059925 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 32897 7239 ? 1.566 ? ? ? 4.500 ? 0.800  ? ? ? ? ? ? 88.900 1.765 0.793 0.535 
1 2 5.480 44.390 ? 7489  1093 ? 0.026 ? ? ? 6.900 ? 70.100 ? ? ? ? ? ? 99.800 0.028 0.011 0.999 
# 
_refine.entry_id                                 7HDC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             39.7000 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.2700 
_refine.ls_number_reflns_obs                     164770 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1455 
_refine.ls_R_factor_R_work                       0.1448 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1590 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7939 
_refine.ls_number_reflns_R_work                  156831 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.9751 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1100 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                57.920 
_refine.B_iso_min                                8.630 
_refine.pdbx_overall_phase_error                 19.0000 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        39.7000 
_refine_hist.pdbx_number_atoms_ligand         112 
_refine_hist.number_atoms_solvent             424 
_refine_hist.number_atoms_total               3078 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.64 
_refine_hist.pdbx_B_iso_mean_solvent          30.19 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 85.0000  4483 . 0.4320 0.4049 . 231 0.0000 4714 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 95.0000  5002 . 0.3554 0.3666 . 215 0.0000 5217 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5258 . 0.2997 0.2941 . 250 0.0000 5508 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5164 . 0.2606 0.2657 . 280 0.0000 5444 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5173 . 0.2348 0.2345 . 327 0.0000 5500 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5268 . 0.2218 0.2414 . 247 0.0000 5515 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5262 . 0.2095 0.2290 . 264 0.0000 5526 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5235 . 0.1892 0.2222 . 246 0.0000 5481 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5199 . 0.1810 0.1945 . 280 0.0000 5479 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5284 . 0.1636 0.1777 . 247 0.0000 5531 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5246 . 0.1494 0.1564 . 257 0.0000 5503 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5278 . 0.1418 0.1691 . 269 0.0000 5547 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5158 . 0.1341 0.1682 . 289 0.0000 5447 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5346 . 0.1273 0.1534 . 237 0.0000 5583 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5165 . 0.1272 0.1416 . 256 0.0000 5421 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5285 . 0.1278 0.1494 . 280 0.0000 5565 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5221 . 0.1270 0.1480 . 281 0.0000 5502 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5236 . 0.1290 0.1504 . 276 0.0000 5512 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5280 . 0.1298 0.1558 . 248 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5229 . 0.1270 0.1588 . 266 0.0000 5495 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5302 . 0.1238 0.1272 . 249 0.0000 5551 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5223 . 0.1205 0.1312 . 280 0.0000 5503 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5297 . 0.1177 0.1319 . 261 0.0000 5558 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5298 . 0.1234 0.1460 . 270 0.0000 5568 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5261 . 0.1328 0.1401 . 250 0.0000 5511 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5267 . 0.1319 0.1329 . 281 0.0000 5548 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5300 . 0.1364 0.1361 . 286 0.0000 5586 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5296 . 0.1354 0.1440 . 292 0.0000 5588 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5337 . 0.1480 0.1678 . 256 0.0000 5593 . 'X-RAY DIFFRACTION' 
3.1100 39.7000 30 100.0000 5478 . 0.1486 0.1702 . 268 0.0000 5746 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDC 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003718' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDC 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
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 5 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
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 7HDC A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDC B 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HDC SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDC MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDC SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDC MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G 
2 1 B,H         
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
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 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? 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 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
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 LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDC 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HZ2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    29 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.60 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
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 ASN A 4   ? B -117.40 -159.86 
2 1 HIS A 86  ? ? 55.35   -133.73 
3 1 SER A 128 ? B 65.42   -0.54   
4 1 HIS B 86  ? ? 57.31   -127.48 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O B A HOH 521 ? 5.86 . 
2 1 O ? A HOH 522 ? 5.89 . 
3 1 O ? A HOH 523 ? 5.99 . 
4 1 O ? A HOH 524 ? 7.63 . 
5 1 O ? B HOH 400 ? 6.27 . 
# 
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 1 ? A SER 1 
2 1 Y 1 A MET 2 ? A MET 2 
# 
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 
A1A72 N2   N  Y N 1   
A1A72 C3   C  Y N 2   
A1A72 C6   C  Y N 3   
A1A72 C9   C  N R 4   
A1A72 C12  C  Y N 5   
A1A72 C14  C  Y N 6   
A1A72 C1   C  N N 7   
A1A72 C10  C  Y N 8   
A1A72 C11  C  Y N 9   
A1A72 C13  C  Y N 10  
A1A72 C15  C  Y N 11  
A1A72 C2   C  N R 12  
A1A72 C4   C  Y N 13  
A1A72 C5   C  Y N 14  
A1A72 C7   C  Y N 15  
A1A72 C8   C  Y N 16  
A1A72 N1   N  N N 17  
A1A72 N3   N  Y N 18  
A1A72 N4   N  Y N 19  
A1A72 O1   O  N N 20  
A1A72 O2   O  N N 21  
A1A72 CL1  CL N N 22  
A1A72 H2   H  N N 23  
A1A72 H13  H  N N 24  
A1A72 H14  H  N N 25  
A1A72 H4   H  N N 26  
A1A72 H5   H  N N 27  
A1A72 H12  H  N N 28  
A1A72 H15  H  N N 29  
A1A72 H1   H  N N 30  
A1A72 H7   H  N N 31  
A1A72 H8   H  N N 32  
A1A72 H9   H  N N 33  
A1A72 H6   H  N N 34  
A1A72 H10  H  N N 35  
A1A72 H3   H  N N 36  
A1A72 H11  H  N N 37  
A1A73 O1   O  N N 38  
A1A73 C1   C  N N 39  
A1A73 C2   C  N S 40  
A1A73 C3   C  Y N 41  
A1A73 C4   C  Y N 42  
A1A73 C5   C  Y N 43  
A1A73 C6   C  Y N 44  
A1A73 C7   C  Y N 45  
A1A73 C8   C  Y N 46  
A1A73 C10  C  Y N 47  
A1A73 C11  C  Y N 48  
A1A73 C12  C  Y N 49  
A1A73 C13  C  Y N 50  
A1A73 C14  C  Y N 51  
A1A73 C15  C  Y N 52  
A1A73 C9   C  N R 53  
A1A73 N1   N  N N 54  
A1A73 N2   N  Y N 55  
A1A73 N3   N  Y N 56  
A1A73 N4   N  Y N 57  
A1A73 O2   O  N N 58  
A1A73 CL1  CL N N 59  
A1A73 H3   H  N N 60  
A1A73 H4   H  N N 61  
A1A73 H5   H  N N 62  
A1A73 H1   H  N N 63  
A1A73 H7   H  N N 64  
A1A73 H8   H  N N 65  
A1A73 H9   H  N N 66  
A1A73 H12  H  N N 67  
A1A73 H13  H  N N 68  
A1A73 H14  H  N N 69  
A1A73 H15  H  N N 70  
A1A73 H2   H  N N 71  
A1A73 H6   H  N N 72  
A1A73 H10  H  N N 73  
A1A73 H11  H  N N 74  
ALA   N    N  N N 75  
ALA   CA   C  N S 76  
ALA   C    C  N N 77  
ALA   O    O  N N 78  
ALA   CB   C  N N 79  
ALA   OXT  O  N N 80  
ALA   H    H  N N 81  
ALA   H2   H  N N 82  
ALA   HA   H  N N 83  
ALA   HB1  H  N N 84  
ALA   HB2  H  N N 85  
ALA   HB3  H  N N 86  
ALA   HXT  H  N N 87  
ARG   N    N  N N 88  
ARG   CA   C  N S 89  
ARG   C    C  N N 90  
ARG   O    O  N N 91  
ARG   CB   C  N N 92  
ARG   CG   C  N N 93  
ARG   CD   C  N N 94  
ARG   NE   N  N N 95  
ARG   CZ   C  N N 96  
ARG   NH1  N  N N 97  
ARG   NH2  N  N N 98  
ARG   OXT  O  N N 99  
ARG   H    H  N N 100 
ARG   H2   H  N N 101 
ARG   HA   H  N N 102 
ARG   HB2  H  N N 103 
ARG   HB3  H  N N 104 
ARG   HG2  H  N N 105 
ARG   HG3  H  N N 106 
ARG   HD2  H  N N 107 
ARG   HD3  H  N N 108 
ARG   HE   H  N N 109 
ARG   HH11 H  N N 110 
ARG   HH12 H  N N 111 
ARG   HH21 H  N N 112 
ARG   HH22 H  N N 113 
ARG   HXT  H  N N 114 
ASN   N    N  N N 115 
ASN   CA   C  N S 116 
ASN   C    C  N N 117 
ASN   O    O  N N 118 
ASN   CB   C  N N 119 
ASN   CG   C  N N 120 
ASN   OD1  O  N N 121 
ASN   ND2  N  N N 122 
ASN   OXT  O  N N 123 
ASN   H    H  N N 124 
ASN   H2   H  N N 125 
ASN   HA   H  N N 126 
ASN   HB2  H  N N 127 
ASN   HB3  H  N N 128 
ASN   HD21 H  N N 129 
ASN   HD22 H  N N 130 
ASN   HXT  H  N N 131 
ASP   N    N  N N 132 
ASP   CA   C  N S 133 
ASP   C    C  N N 134 
ASP   O    O  N N 135 
ASP   CB   C  N N 136 
ASP   CG   C  N N 137 
ASP   OD1  O  N N 138 
ASP   OD2  O  N N 139 
ASP   OXT  O  N N 140 
ASP   H    H  N N 141 
ASP   H2   H  N N 142 
ASP   HA   H  N N 143 
ASP   HB2  H  N N 144 
ASP   HB3  H  N N 145 
ASP   HD2  H  N N 146 
ASP   HXT  H  N N 147 
CL    CL   CL N N 148 
CYS   N    N  N N 149 
CYS   CA   C  N R 150 
CYS   C    C  N N 151 
CYS   O    O  N N 152 
CYS   CB   C  N N 153 
CYS   SG   S  N N 154 
CYS   OXT  O  N N 155 
CYS   H    H  N N 156 
CYS   H2   H  N N 157 
CYS   HA   H  N N 158 
CYS   HB2  H  N N 159 
CYS   HB3  H  N N 160 
CYS   HG   H  N N 161 
CYS   HXT  H  N N 162 
GLN   N    N  N N 163 
GLN   CA   C  N S 164 
GLN   C    C  N N 165 
GLN   O    O  N N 166 
GLN   CB   C  N N 167 
GLN   CG   C  N N 168 
GLN   CD   C  N N 169 
GLN   OE1  O  N N 170 
GLN   NE2  N  N N 171 
GLN   OXT  O  N N 172 
GLN   H    H  N N 173 
GLN   H2   H  N N 174 
GLN   HA   H  N N 175 
GLN   HB2  H  N N 176 
GLN   HB3  H  N N 177 
GLN   HG2  H  N N 178 
GLN   HG3  H  N N 179 
GLN   HE21 H  N N 180 
GLN   HE22 H  N N 181 
GLN   HXT  H  N N 182 
GLU   N    N  N N 183 
GLU   CA   C  N S 184 
GLU   C    C  N N 185 
GLU   O    O  N N 186 
GLU   CB   C  N N 187 
GLU   CG   C  N N 188 
GLU   CD   C  N N 189 
GLU   OE1  O  N N 190 
GLU   OE2  O  N N 191 
GLU   OXT  O  N N 192 
GLU   H    H  N N 193 
GLU   H2   H  N N 194 
GLU   HA   H  N N 195 
GLU   HB2  H  N N 196 
GLU   HB3  H  N N 197 
GLU   HG2  H  N N 198 
GLU   HG3  H  N N 199 
GLU   HE2  H  N N 200 
GLU   HXT  H  N N 201 
GLY   N    N  N N 202 
GLY   CA   C  N N 203 
GLY   C    C  N N 204 
GLY   O    O  N N 205 
GLY   OXT  O  N N 206 
GLY   H    H  N N 207 
GLY   H2   H  N N 208 
GLY   HA2  H  N N 209 
GLY   HA3  H  N N 210 
GLY   HXT  H  N N 211 
HIS   N    N  N N 212 
HIS   CA   C  N S 213 
HIS   C    C  N N 214 
HIS   O    O  N N 215 
HIS   CB   C  N N 216 
HIS   CG   C  Y N 217 
HIS   ND1  N  Y N 218 
HIS   CD2  C  Y N 219 
HIS   CE1  C  Y N 220 
HIS   NE2  N  Y N 221 
HIS   OXT  O  N N 222 
HIS   H    H  N N 223 
HIS   H2   H  N N 224 
HIS   HA   H  N N 225 
HIS   HB2  H  N N 226 
HIS   HB3  H  N N 227 
HIS   HD1  H  N N 228 
HIS   HD2  H  N N 229 
HIS   HE1  H  N N 230 
HIS   HE2  H  N N 231 
HIS   HXT  H  N N 232 
HOH   O    O  N N 233 
HOH   H1   H  N N 234 
HOH   H2   H  N N 235 
ILE   N    N  N N 236 
ILE   CA   C  N S 237 
ILE   C    C  N N 238 
ILE   O    O  N N 239 
ILE   CB   C  N S 240 
ILE   CG1  C  N N 241 
ILE   CG2  C  N N 242 
ILE   CD1  C  N N 243 
ILE   OXT  O  N N 244 
ILE   H    H  N N 245 
ILE   H2   H  N N 246 
ILE   HA   H  N N 247 
ILE   HB   H  N N 248 
ILE   HG12 H  N N 249 
ILE   HG13 H  N N 250 
ILE   HG21 H  N N 251 
ILE   HG22 H  N N 252 
ILE   HG23 H  N N 253 
ILE   HD11 H  N N 254 
ILE   HD12 H  N N 255 
ILE   HD13 H  N N 256 
ILE   HXT  H  N N 257 
LEU   N    N  N N 258 
LEU   CA   C  N S 259 
LEU   C    C  N N 260 
LEU   O    O  N N 261 
LEU   CB   C  N N 262 
LEU   CG   C  N N 263 
LEU   CD1  C  N N 264 
LEU   CD2  C  N N 265 
LEU   OXT  O  N N 266 
LEU   H    H  N N 267 
LEU   H2   H  N N 268 
LEU   HA   H  N N 269 
LEU   HB2  H  N N 270 
LEU   HB3  H  N N 271 
LEU   HG   H  N N 272 
LEU   HD11 H  N N 273 
LEU   HD12 H  N N 274 
LEU   HD13 H  N N 275 
LEU   HD21 H  N N 276 
LEU   HD22 H  N N 277 
LEU   HD23 H  N N 278 
LEU   HXT  H  N N 279 
LYS   N    N  N N 280 
LYS   CA   C  N S 281 
LYS   C    C  N N 282 
LYS   O    O  N N 283 
LYS   CB   C  N N 284 
LYS   CG   C  N N 285 
LYS   CD   C  N N 286 
LYS   CE   C  N N 287 
LYS   NZ   N  N N 288 
LYS   OXT  O  N N 289 
LYS   H    H  N N 290 
LYS   H2   H  N N 291 
LYS   HA   H  N N 292 
LYS   HB2  H  N N 293 
LYS   HB3  H  N N 294 
LYS   HG2  H  N N 295 
LYS   HG3  H  N N 296 
LYS   HD2  H  N N 297 
LYS   HD3  H  N N 298 
LYS   HE2  H  N N 299 
LYS   HE3  H  N N 300 
LYS   HZ1  H  N N 301 
LYS   HZ2  H  N N 302 
LYS   HZ3  H  N N 303 
LYS   HXT  H  N N 304 
MET   N    N  N N 305 
MET   CA   C  N S 306 
MET   C    C  N N 307 
MET   O    O  N N 308 
MET   CB   C  N N 309 
MET   CG   C  N N 310 
MET   SD   S  N N 311 
MET   CE   C  N N 312 
MET   OXT  O  N N 313 
MET   H    H  N N 314 
MET   H2   H  N N 315 
MET   HA   H  N N 316 
MET   HB2  H  N N 317 
MET   HB3  H  N N 318 
MET   HG2  H  N N 319 
MET   HG3  H  N N 320 
MET   HE1  H  N N 321 
MET   HE2  H  N N 322 
MET   HE3  H  N N 323 
MET   HXT  H  N N 324 
PHE   N    N  N N 325 
PHE   CA   C  N S 326 
PHE   C    C  N N 327 
PHE   O    O  N N 328 
PHE   CB   C  N N 329 
PHE   CG   C  Y N 330 
PHE   CD1  C  Y N 331 
PHE   CD2  C  Y N 332 
PHE   CE1  C  Y N 333 
PHE   CE2  C  Y N 334 
PHE   CZ   C  Y N 335 
PHE   OXT  O  N N 336 
PHE   H    H  N N 337 
PHE   H2   H  N N 338 
PHE   HA   H  N N 339 
PHE   HB2  H  N N 340 
PHE   HB3  H  N N 341 
PHE   HD1  H  N N 342 
PHE   HD2  H  N N 343 
PHE   HE1  H  N N 344 
PHE   HE2  H  N N 345 
PHE   HZ   H  N N 346 
PHE   HXT  H  N N 347 
PRO   N    N  N N 348 
PRO   CA   C  N S 349 
PRO   C    C  N N 350 
PRO   O    O  N N 351 
PRO   CB   C  N N 352 
PRO   CG   C  N N 353 
PRO   CD   C  N N 354 
PRO   OXT  O  N N 355 
PRO   H    H  N N 356 
PRO   HA   H  N N 357 
PRO   HB2  H  N N 358 
PRO   HB3  H  N N 359 
PRO   HG2  H  N N 360 
PRO   HG3  H  N N 361 
PRO   HD2  H  N N 362 
PRO   HD3  H  N N 363 
PRO   HXT  H  N N 364 
SER   N    N  N N 365 
SER   CA   C  N S 366 
SER   C    C  N N 367 
SER   O    O  N N 368 
SER   CB   C  N N 369 
SER   OG   O  N N 370 
SER   OXT  O  N N 371 
SER   H    H  N N 372 
SER   H2   H  N N 373 
SER   HA   H  N N 374 
SER   HB2  H  N N 375 
SER   HB3  H  N N 376 
SER   HG   H  N N 377 
SER   HXT  H  N N 378 
THR   N    N  N N 379 
THR   CA   C  N S 380 
THR   C    C  N N 381 
THR   O    O  N N 382 
THR   CB   C  N R 383 
THR   OG1  O  N N 384 
THR   CG2  C  N N 385 
THR   OXT  O  N N 386 
THR   H    H  N N 387 
THR   H2   H  N N 388 
THR   HA   H  N N 389 
THR   HB   H  N N 390 
THR   HG1  H  N N 391 
THR   HG21 H  N N 392 
THR   HG22 H  N N 393 
THR   HG23 H  N N 394 
THR   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
# 
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 
A1A72 CL1 C13  sing N N 1   
A1A72 C12 C13  doub Y N 2   
A1A72 C12 C11  sing Y N 3   
A1A72 C13 C14  sing Y N 4   
A1A72 C11 C10  doub Y N 5   
A1A72 C14 C15  doub Y N 6   
A1A72 C10 C15  sing Y N 7   
A1A72 C10 C9   sing N N 8   
A1A72 O2  C9   sing N N 9   
A1A72 C9  C2   sing N N 10  
A1A72 O1  C1   sing N N 11  
A1A72 C2  C1   sing N N 12  
A1A72 C2  N1   sing N N 13  
A1A72 N1  C3   sing N N 14  
A1A72 C3  N2   doub Y N 15  
A1A72 C3  C6   sing Y N 16  
A1A72 C7  C6   sing Y N 17  
A1A72 C7  C8   doub Y N 18  
A1A72 N2  C4   sing Y N 19  
A1A72 C6  C5   doub Y N 20  
A1A72 C8  N4   sing Y N 21  
A1A72 C4  N3   doub Y N 22  
A1A72 C5  N4   sing Y N 23  
A1A72 C5  N3   sing Y N 24  
A1A72 C9  H2   sing N N 25  
A1A72 C12 H13  sing N N 26  
A1A72 C14 H14  sing N N 27  
A1A72 C1  H4   sing N N 28  
A1A72 C1  H5   sing N N 29  
A1A72 C11 H12  sing N N 30  
A1A72 C15 H15  sing N N 31  
A1A72 C2  H1   sing N N 32  
A1A72 C4  H7   sing N N 33  
A1A72 C7  H8   sing N N 34  
A1A72 C8  H9   sing N N 35  
A1A72 N1  H6   sing N N 36  
A1A72 N4  H10  sing N N 37  
A1A72 O1  H3   sing N N 38  
A1A72 O2  H11  sing N N 39  
A1A73 CL1 C13  sing N N 40  
A1A73 C12 C13  doub Y N 41  
A1A73 C12 C11  sing Y N 42  
A1A73 C13 C14  sing Y N 43  
A1A73 C11 C10  doub Y N 44  
A1A73 O1  C1   sing N N 45  
A1A73 C14 C15  doub Y N 46  
A1A73 C10 C15  sing Y N 47  
A1A73 C10 C9   sing N N 48  
A1A73 C2  C1   sing N N 49  
A1A73 C2  C9   sing N N 50  
A1A73 C2  N1   sing N N 51  
A1A73 O2  C9   sing N N 52  
A1A73 N1  C3   sing N N 53  
A1A73 C3  C6   doub Y N 54  
A1A73 C3  N2   sing Y N 55  
A1A73 C7  C6   sing Y N 56  
A1A73 C7  C8   doub Y N 57  
A1A73 C6  C5   sing Y N 58  
A1A73 N2  C4   doub Y N 59  
A1A73 C8  N4   sing Y N 60  
A1A73 C4  N3   sing Y N 61  
A1A73 C5  N4   sing Y N 62  
A1A73 C5  N3   doub Y N 63  
A1A73 O1  H3   sing N N 64  
A1A73 C1  H4   sing N N 65  
A1A73 C1  H5   sing N N 66  
A1A73 C2  H1   sing N N 67  
A1A73 C4  H7   sing N N 68  
A1A73 C7  H8   sing N N 69  
A1A73 C8  H9   sing N N 70  
A1A73 C11 H12  sing N N 71  
A1A73 C12 H13  sing N N 72  
A1A73 C14 H14  sing N N 73  
A1A73 C15 H15  sing N N 74  
A1A73 C9  H2   sing N N 75  
A1A73 N1  H6   sing N N 76  
A1A73 N4  H10  sing N N 77  
A1A73 O2  H11  sing N N 78  
ALA   N   CA   sing N N 79  
ALA   N   H    sing N N 80  
ALA   N   H2   sing N N 81  
ALA   CA  C    sing N N 82  
ALA   CA  CB   sing N N 83  
ALA   CA  HA   sing N N 84  
ALA   C   O    doub N N 85  
ALA   C   OXT  sing N N 86  
ALA   CB  HB1  sing N N 87  
ALA   CB  HB2  sing N N 88  
ALA   CB  HB3  sing N N 89  
ALA   OXT HXT  sing N N 90  
ARG   N   CA   sing N N 91  
ARG   N   H    sing N N 92  
ARG   N   H2   sing N N 93  
ARG   CA  C    sing N N 94  
ARG   CA  CB   sing N N 95  
ARG   CA  HA   sing N N 96  
ARG   C   O    doub N N 97  
ARG   C   OXT  sing N N 98  
ARG   CB  CG   sing N N 99  
ARG   CB  HB2  sing N N 100 
ARG   CB  HB3  sing N N 101 
ARG   CG  CD   sing N N 102 
ARG   CG  HG2  sing N N 103 
ARG   CG  HG3  sing N N 104 
ARG   CD  NE   sing N N 105 
ARG   CD  HD2  sing N N 106 
ARG   CD  HD3  sing N N 107 
ARG   NE  CZ   sing N N 108 
ARG   NE  HE   sing N N 109 
ARG   CZ  NH1  sing N N 110 
ARG   CZ  NH2  doub N N 111 
ARG   NH1 HH11 sing N N 112 
ARG   NH1 HH12 sing N N 113 
ARG   NH2 HH21 sing N N 114 
ARG   NH2 HH22 sing N N 115 
ARG   OXT HXT  sing N N 116 
ASN   N   CA   sing N N 117 
ASN   N   H    sing N N 118 
ASN   N   H2   sing N N 119 
ASN   CA  C    sing N N 120 
ASN   CA  CB   sing N N 121 
ASN   CA  HA   sing N N 122 
ASN   C   O    doub N N 123 
ASN   C   OXT  sing N N 124 
ASN   CB  CG   sing N N 125 
ASN   CB  HB2  sing N N 126 
ASN   CB  HB3  sing N N 127 
ASN   CG  OD1  doub N N 128 
ASN   CG  ND2  sing N N 129 
ASN   ND2 HD21 sing N N 130 
ASN   ND2 HD22 sing N N 131 
ASN   OXT HXT  sing N N 132 
ASP   N   CA   sing N N 133 
ASP   N   H    sing N N 134 
ASP   N   H2   sing N N 135 
ASP   CA  C    sing N N 136 
ASP   CA  CB   sing N N 137 
ASP   CA  HA   sing N N 138 
ASP   C   O    doub N N 139 
ASP   C   OXT  sing N N 140 
ASP   CB  CG   sing N N 141 
ASP   CB  HB2  sing N N 142 
ASP   CB  HB3  sing N N 143 
ASP   CG  OD1  doub N N 144 
ASP   CG  OD2  sing N N 145 
ASP   OD2 HD2  sing N N 146 
ASP   OXT HXT  sing N N 147 
CYS   N   CA   sing N N 148 
CYS   N   H    sing N N 149 
CYS   N   H2   sing N N 150 
CYS   CA  C    sing N N 151 
CYS   CA  CB   sing N N 152 
CYS   CA  HA   sing N N 153 
CYS   C   O    doub N N 154 
CYS   C   OXT  sing N N 155 
CYS   CB  SG   sing N N 156 
CYS   CB  HB2  sing N N 157 
CYS   CB  HB3  sing N N 158 
CYS   SG  HG   sing N N 159 
CYS   OXT HXT  sing N N 160 
GLN   N   CA   sing N N 161 
GLN   N   H    sing N N 162 
GLN   N   H2   sing N N 163 
GLN   CA  C    sing N N 164 
GLN   CA  CB   sing N N 165 
GLN   CA  HA   sing N N 166 
GLN   C   O    doub N N 167 
GLN   C   OXT  sing N N 168 
GLN   CB  CG   sing N N 169 
GLN   CB  HB2  sing N N 170 
GLN   CB  HB3  sing N N 171 
GLN   CG  CD   sing N N 172 
GLN   CG  HG2  sing N N 173 
GLN   CG  HG3  sing N N 174 
GLN   CD  OE1  doub N N 175 
GLN   CD  NE2  sing N N 176 
GLN   NE2 HE21 sing N N 177 
GLN   NE2 HE22 sing N N 178 
GLN   OXT HXT  sing N N 179 
GLU   N   CA   sing N N 180 
GLU   N   H    sing N N 181 
GLU   N   H2   sing N N 182 
GLU   CA  C    sing N N 183 
GLU   CA  CB   sing N N 184 
GLU   CA  HA   sing N N 185 
GLU   C   O    doub N N 186 
GLU   C   OXT  sing N N 187 
GLU   CB  CG   sing N N 188 
GLU   CB  HB2  sing N N 189 
GLU   CB  HB3  sing N N 190 
GLU   CG  CD   sing N N 191 
GLU   CG  HG2  sing N N 192 
GLU   CG  HG3  sing N N 193 
GLU   CD  OE1  doub N N 194 
GLU   CD  OE2  sing N N 195 
GLU   OE2 HE2  sing N N 196 
GLU   OXT HXT  sing N N 197 
GLY   N   CA   sing N N 198 
GLY   N   H    sing N N 199 
GLY   N   H2   sing N N 200 
GLY   CA  C    sing N N 201 
GLY   CA  HA2  sing N N 202 
GLY   CA  HA3  sing N N 203 
GLY   C   O    doub N N 204 
GLY   C   OXT  sing N N 205 
GLY   OXT HXT  sing N N 206 
HIS   N   CA   sing N N 207 
HIS   N   H    sing N N 208 
HIS   N   H2   sing N N 209 
HIS   CA  C    sing N N 210 
HIS   CA  CB   sing N N 211 
HIS   CA  HA   sing N N 212 
HIS   C   O    doub N N 213 
HIS   C   OXT  sing N N 214 
HIS   CB  CG   sing N N 215 
HIS   CB  HB2  sing N N 216 
HIS   CB  HB3  sing N N 217 
HIS   CG  ND1  sing Y N 218 
HIS   CG  CD2  doub Y N 219 
HIS   ND1 CE1  doub Y N 220 
HIS   ND1 HD1  sing N N 221 
HIS   CD2 NE2  sing Y N 222 
HIS   CD2 HD2  sing N N 223 
HIS   CE1 NE2  sing Y N 224 
HIS   CE1 HE1  sing N N 225 
HIS   NE2 HE2  sing N N 226 
HIS   OXT HXT  sing N N 227 
HOH   O   H1   sing N N 228 
HOH   O   H2   sing N N 229 
ILE   N   CA   sing N N 230 
ILE   N   H    sing N N 231 
ILE   N   H2   sing N N 232 
ILE   CA  C    sing N N 233 
ILE   CA  CB   sing N N 234 
ILE   CA  HA   sing N N 235 
ILE   C   O    doub N N 236 
ILE   C   OXT  sing N N 237 
ILE   CB  CG1  sing N N 238 
ILE   CB  CG2  sing N N 239 
ILE   CB  HB   sing N N 240 
ILE   CG1 CD1  sing N N 241 
ILE   CG1 HG12 sing N N 242 
ILE   CG1 HG13 sing N N 243 
ILE   CG2 HG21 sing N N 244 
ILE   CG2 HG22 sing N N 245 
ILE   CG2 HG23 sing N N 246 
ILE   CD1 HD11 sing N N 247 
ILE   CD1 HD12 sing N N 248 
ILE   CD1 HD13 sing N N 249 
ILE   OXT HXT  sing N N 250 
LEU   N   CA   sing N N 251 
LEU   N   H    sing N N 252 
LEU   N   H2   sing N N 253 
LEU   CA  C    sing N N 254 
LEU   CA  CB   sing N N 255 
LEU   CA  HA   sing N N 256 
LEU   C   O    doub N N 257 
LEU   C   OXT  sing N N 258 
LEU   CB  CG   sing N N 259 
LEU   CB  HB2  sing N N 260 
LEU   CB  HB3  sing N N 261 
LEU   CG  CD1  sing N N 262 
LEU   CG  CD2  sing N N 263 
LEU   CG  HG   sing N N 264 
LEU   CD1 HD11 sing N N 265 
LEU   CD1 HD12 sing N N 266 
LEU   CD1 HD13 sing N N 267 
LEU   CD2 HD21 sing N N 268 
LEU   CD2 HD22 sing N N 269 
LEU   CD2 HD23 sing N N 270 
LEU   OXT HXT  sing N N 271 
LYS   N   CA   sing N N 272 
LYS   N   H    sing N N 273 
LYS   N   H2   sing N N 274 
LYS   CA  C    sing N N 275 
LYS   CA  CB   sing N N 276 
LYS   CA  HA   sing N N 277 
LYS   C   O    doub N N 278 
LYS   C   OXT  sing N N 279 
LYS   CB  CG   sing N N 280 
LYS   CB  HB2  sing N N 281 
LYS   CB  HB3  sing N N 282 
LYS   CG  CD   sing N N 283 
LYS   CG  HG2  sing N N 284 
LYS   CG  HG3  sing N N 285 
LYS   CD  CE   sing N N 286 
LYS   CD  HD2  sing N N 287 
LYS   CD  HD3  sing N N 288 
LYS   CE  NZ   sing N N 289 
LYS   CE  HE2  sing N N 290 
LYS   CE  HE3  sing N N 291 
LYS   NZ  HZ1  sing N N 292 
LYS   NZ  HZ2  sing N N 293 
LYS   NZ  HZ3  sing N N 294 
LYS   OXT HXT  sing N N 295 
MET   N   CA   sing N N 296 
MET   N   H    sing N N 297 
MET   N   H2   sing N N 298 
MET   CA  C    sing N N 299 
MET   CA  CB   sing N N 300 
MET   CA  HA   sing N N 301 
MET   C   O    doub N N 302 
MET   C   OXT  sing N N 303 
MET   CB  CG   sing N N 304 
MET   CB  HB2  sing N N 305 
MET   CB  HB3  sing N N 306 
MET   CG  SD   sing N N 307 
MET   CG  HG2  sing N N 308 
MET   CG  HG3  sing N N 309 
MET   SD  CE   sing N N 310 
MET   CE  HE1  sing N N 311 
MET   CE  HE2  sing N N 312 
MET   CE  HE3  sing N N 313 
MET   OXT HXT  sing N N 314 
PHE   N   CA   sing N N 315 
PHE   N   H    sing N N 316 
PHE   N   H2   sing N N 317 
PHE   CA  C    sing N N 318 
PHE   CA  CB   sing N N 319 
PHE   CA  HA   sing N N 320 
PHE   C   O    doub N N 321 
PHE   C   OXT  sing N N 322 
PHE   CB  CG   sing N N 323 
PHE   CB  HB2  sing N N 324 
PHE   CB  HB3  sing N N 325 
PHE   CG  CD1  doub Y N 326 
PHE   CG  CD2  sing Y N 327 
PHE   CD1 CE1  sing Y N 328 
PHE   CD1 HD1  sing N N 329 
PHE   CD2 CE2  doub Y N 330 
PHE   CD2 HD2  sing N N 331 
PHE   CE1 CZ   doub Y N 332 
PHE   CE1 HE1  sing N N 333 
PHE   CE2 CZ   sing Y N 334 
PHE   CE2 HE2  sing N N 335 
PHE   CZ  HZ   sing N N 336 
PHE   OXT HXT  sing N N 337 
PRO   N   CA   sing N N 338 
PRO   N   CD   sing N N 339 
PRO   N   H    sing N N 340 
PRO   CA  C    sing N N 341 
PRO   CA  CB   sing N N 342 
PRO   CA  HA   sing N N 343 
PRO   C   O    doub N N 344 
PRO   C   OXT  sing N N 345 
PRO   CB  CG   sing N N 346 
PRO   CB  HB2  sing N N 347 
PRO   CB  HB3  sing N N 348 
PRO   CG  CD   sing N N 349 
PRO   CG  HG2  sing N N 350 
PRO   CG  HG3  sing N N 351 
PRO   CD  HD2  sing N N 352 
PRO   CD  HD3  sing N N 353 
PRO   OXT HXT  sing N N 354 
SER   N   CA   sing N N 355 
SER   N   H    sing N N 356 
SER   N   H2   sing N N 357 
SER   CA  C    sing N N 358 
SER   CA  CB   sing N N 359 
SER   CA  HA   sing N N 360 
SER   C   O    doub N N 361 
SER   C   OXT  sing N N 362 
SER   CB  OG   sing N N 363 
SER   CB  HB2  sing N N 364 
SER   CB  HB3  sing N N 365 
SER   OG  HG   sing N N 366 
SER   OXT HXT  sing N N 367 
THR   N   CA   sing N N 368 
THR   N   H    sing N N 369 
THR   N   H2   sing N N 370 
THR   CA  C    sing N N 371 
THR   CA  CB   sing N N 372 
THR   CA  HA   sing N N 373 
THR   C   O    doub N N 374 
THR   C   OXT  sing N N 375 
THR   CB  OG1  sing N N 376 
THR   CB  CG2  sing N N 377 
THR   CB  HB   sing N N 378 
THR   OG1 HG1  sing N N 379 
THR   CG2 HG21 sing N N 380 
THR   CG2 HG22 sing N N 381 
THR   CG2 HG23 sing N N 382 
THR   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HDC 
_atom_sites.fract_transf_matrix[1][1]   0.011264 
_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]   0.011264 
_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]   0.025322 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.607 -16.241 22.230  0.60 42.07 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 20.668 -15.846 21.738  0.40 43.48 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.634 -15.173 22.429  0.60 41.70 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 19.683 -14.809 22.016  0.40 43.35 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.276 -13.817 22.164  0.60 40.00 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 20.243 -13.438 21.658  0.40 42.66 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.359 -13.523 22.671  0.60 40.51 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 21.396 -13.131 21.962  0.40 43.08 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.020 -15.233 23.841  0.60 42.66 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 19.213 -14.862 23.482  0.40 43.80 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.013 -14.106 24.033  0.60 42.87 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 18.240 -13.730 23.775  0.40 43.86 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.366 -16.585 24.079  0.60 42.81 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 18.571 -16.207 23.781  0.40 44.01 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.912 -15.282 21.793  0.60 50.21 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 18.907 -14.960 21.458  0.40 52.18 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.724 -15.121 24.500  0.60 51.35 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 19.981 -14.759 24.066  0.40 52.72 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.501 -14.276 24.839  0.60 51.61 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 17.804 -13.903 24.625  0.40 52.80 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.488 -13.265 24.115  0.60 51.61 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 18.727 -12.893 23.820  0.40 52.80 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.420 -14.080 23.266  0.60 51.61 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 17.577 -13.693 23.068  0.40 52.80 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.933 -16.578 24.947  0.60 51.53 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 18.291 -16.223 24.709  0.40 52.97 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.709 -16.744 23.383  0.60 51.53 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 17.802 -16.322 23.200  0.40 52.97 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.047 -17.275 24.055  0.60 51.53 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 19.218 -16.910 23.617  0.40 52.97 ?  3   VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.601 -12.993 21.364  0.60 37.46 ?  4   ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 19.418 -12.618 21.006  0.40 41.39 ?  4   ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.041 -11.635 21.074  0.60 34.73 ?  4   ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 19.829 -11.279 20.600  0.40 39.91 ?  4   ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.872 -10.676 21.288  0.60 31.48 ?  4   ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 18.976 -10.223 21.289  0.40 38.46 ?  4   ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.753 -11.088 21.608  0.60 30.83 ?  4   ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 18.341 -10.496 22.314  0.40 38.60 ?  4   ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.639 -11.520 19.664  0.60 34.90 ?  4   ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.719 -11.122 19.082  0.40 39.69 ?  4   ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.680 -11.958 18.579  0.60 34.80 ?  4   ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.365 -11.535 18.550  0.40 39.41 ?  4   ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.533 -11.513 18.531  0.60 35.11 ?  4   ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.336 -10.975 18.929  0.40 39.26 ?  4   ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.147 -12.838 17.698  0.60 34.69 ?  4   ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 18.358 -12.516 17.656  0.40 39.56 ?  4   ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.865 -13.206 20.972  0.60 45.12 ?  4   ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 18.609 -12.819 20.789  0.40 49.83 ?  4   ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.738 -11.399 21.702  0.60 41.84 ?  4   ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 20.756 -11.143 20.851  0.40 48.06 ?  4   ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.876 -10.594 19.497  0.60 42.04 ?  4   ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.885 -10.200 18.822  0.40 47.80 ?  4   ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.428 -12.079 19.611  0.60 42.04 ?  4   ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.377 -11.692 18.672  0.40 47.80 ?  4   ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.644 -13.119 17.060  0.60 41.79 ?  4   ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 17.616 -12.789 17.320  0.40 47.64 ?  4   ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.956 -13.125 17.763  0.60 41.79 ?  4   ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.099 -12.877 17.413  0.40 47.64 ?  4   ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.139 -9.383  21.106  0.60 29.14 ?  5   SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.949 -9.017  20.723  0.40 36.80 ?  5   SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.199 -8.329  21.466  0.60 27.10 ?  5   SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 18.172 -7.914  21.263  0.40 34.89 ?  5   SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.345 -7.851  20.295  0.60 24.91 ?  5   SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 17.055 -7.459  20.334  0.40 32.18 ?  5   SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.605 -6.873  20.444  0.60 24.93 ?  5   SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 16.377 -6.471  20.643  0.40 32.14 ?  5   SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 17.941 -7.145  22.092  0.60 27.67 ?  5   SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 19.090 -6.731  21.602  0.40 35.65 ?  5   SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 18.908 -6.622  21.199  0.60 28.22 ?  5   SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 20.161 -6.633  20.679  0.40 36.01 ?  5   SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.872 -9.090  20.765  0.60 35.13 ?  5   SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 19.378 -8.813  20.007  0.40 44.32 ?  5   SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.597 -8.675  22.141  0.60 32.68 ?  5   SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 17.763 -8.206  22.088  0.40 42.03 ?  5   SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.300 -6.447  22.307  0.60 33.37 ?  5   SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 18.576 -5.912  21.561  0.40 42.95 ?  5   SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.385 -7.443  22.904  0.60 33.37 ?  5   SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 19.444 -6.857  22.497  0.40 42.95 ?  5   SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.309 -5.975  21.559  0.60 34.03 ?  5   SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 20.663 -5.993  20.891  0.40 43.38 ?  5   SER   A HG   1 
ATOM   81   N  N    A PHE   A 1 6   ? 16.415 -8.513  19.143  0.60 22.35 ?  6   PHE   A N    1 
ATOM   82   N  N    B PHE   A 1 6   ? 16.843 -8.142  19.211  0.40 29.21 ?  6   PHE   A N    1 
ATOM   83   C  CA   A PHE   A 1 6   ? 15.553 -8.146  18.025  0.60 19.72 ?  6   PHE   A CA   1 
ATOM   84   C  CA   B PHE   A 1 6   ? 15.736 -7.809  18.329  0.40 26.18 ?  6   PHE   A CA   1 
ATOM   85   C  C    A PHE   A 1 6   ? 14.104 -8.494  18.358  0.60 19.90 ?  6   PHE   A C    1 
ATOM   86   C  C    B PHE   A 1 6   ? 14.421 -8.284  18.934  0.40 25.31 ?  6   PHE   A C    1 
ATOM   87   O  O    A PHE   A 1 6   ? 13.825 -9.587  18.856  0.60 20.43 ?  6   PHE   A O    1 
ATOM   88   O  O    B PHE   A 1 6   ? 14.377 -9.247  19.704  0.40 25.77 ?  6   PHE   A O    1 
ATOM   89   C  CB   A PHE   A 1 6   ? 15.998 -8.880  16.763  0.60 18.36 ?  6   PHE   A CB   1 
ATOM   90   C  CB   B PHE   A 1 6   ? 15.928 -8.474  16.966  0.40 24.34 ?  6   PHE   A CB   1 
ATOM   91   C  CG   A PHE   A 1 6   ? 17.273 -8.344  16.170  0.60 17.60 ?  6   PHE   A CG   1 
ATOM   92   C  CG   B PHE   A 1 6   ? 17.215 -8.102  16.288  0.40 22.71 ?  6   PHE   A CG   1 
ATOM   93   C  CD1  A PHE   A 1 6   ? 17.271 -7.157  15.457  0.60 17.30 ?  6   PHE   A CD1  1 
ATOM   94   C  CD1  B PHE   A 1 6   ? 17.316 -6.925  15.567  0.40 22.05 ?  6   PHE   A CD1  1 
ATOM   95   C  CD2  A PHE   A 1 6   ? 18.470 -9.025  16.326  0.60 17.82 ?  6   PHE   A CD2  1 
ATOM   96   C  CD2  B PHE   A 1 6   ? 18.322 -8.929  16.369  0.40 22.28 ?  6   PHE   A CD2  1 
ATOM   97   C  CE1  A PHE   A 1 6   ? 18.438 -6.655  14.910  0.60 17.54 ?  6   PHE   A CE1  1 
ATOM   98   C  CE1  B PHE   A 1 6   ? 18.499 -6.577  14.941  0.40 21.79 ?  6   PHE   A CE1  1 
ATOM   99   C  CE2  A PHE   A 1 6   ? 19.639 -8.531  15.780  0.60 17.94 ?  6   PHE   A CE2  1 
ATOM   100  C  CE2  B PHE   A 1 6   ? 19.507 -8.589  15.745  0.40 21.98 ?  6   PHE   A CE2  1 
ATOM   101  C  CZ   A PHE   A 1 6   ? 19.623 -7.342  15.071  0.60 17.72 ?  6   PHE   A CZ   1 
ATOM   102  C  CZ   B PHE   A 1 6   ? 19.596 -7.410  15.030  0.40 21.79 ?  6   PHE   A CZ   1 
ATOM   103  H  H    A PHE   A 1 6   ? 16.935 -9.180  18.991  0.60 26.99 ?  6   PHE   A H    1 
ATOM   104  H  H    B PHE   A 1 6   ? 17.324 -8.800  18.939  0.40 35.21 ?  6   PHE   A H    1 
ATOM   105  H  HA   A PHE   A 1 6   ? 15.607 -7.198  17.874  0.60 23.83 ?  6   PHE   A HA   1 
ATOM   106  H  HA   B PHE   A 1 6   ? 15.694 -6.848  18.205  0.40 31.58 ?  6   PHE   A HA   1 
ATOM   107  H  HB2  A PHE   A 1 6   ? 16.136 -9.820  16.982  0.60 22.20 ?  6   PHE   A HB2  1 
ATOM   108  H  HB2  B PHE   A 1 6   ? 15.920 -9.437  17.085  0.40 29.37 ?  6   PHE   A HB2  1 
ATOM   109  H  HB3  A PHE   A 1 6   ? 15.298 -8.805  16.096  0.60 22.20 ?  6   PHE   A HB3  1 
ATOM   110  H  HB3  B PHE   A 1 6   ? 15.197 -8.209  16.385  0.40 29.37 ?  6   PHE   A HB3  1 
ATOM   111  H  HD1  A PHE   A 1 6   ? 16.470 -6.695  15.348  0.60 20.92 ?  6   PHE   A HD1  1 
ATOM   112  H  HD1  B PHE   A 1 6   ? 16.578 -6.361  15.506  0.40 26.62 ?  6   PHE   A HD1  1 
ATOM   113  H  HD2  A PHE   A 1 6   ? 18.485 -9.826  16.806  0.60 21.55 ?  6   PHE   A HD2  1 
ATOM   114  H  HD2  B PHE   A 1 6   ? 18.267 -9.723  16.850  0.40 26.89 ?  6   PHE   A HD2  1 
ATOM   115  H  HE1  A PHE   A 1 6   ? 18.419 -5.858  14.433  0.60 21.22 ?  6   PHE   A HE1  1 
ATOM   116  H  HE1  B PHE   A 1 6   ? 18.555 -5.783  14.460  0.40 26.31 ?  6   PHE   A HE1  1 
ATOM   117  H  HE2  A PHE   A 1 6   ? 20.439 -8.993  15.892  0.60 21.69 ?  6   PHE   A HE2  1 
ATOM   118  H  HE2  B PHE   A 1 6   ? 20.245 -9.152  15.808  0.40 26.54 ?  6   PHE   A HE2  1 
ATOM   119  H  HZ   A PHE   A 1 6   ? 20.405 -7.005  14.703  0.60 21.43 ?  6   PHE   A HZ   1 
ATOM   120  H  HZ   B PHE   A 1 6   ? 20.392 -7.178  14.610  0.40 26.31 ?  6   PHE   A HZ   1 
ATOM   121  N  N    A SER   A 1 7   ? 13.178 -7.567  18.081  0.60 19.79 ?  7   SER   A N    1 
ATOM   122  N  N    B SER   A 1 7   ? 13.339 -7.598  18.577  0.40 23.90 ?  7   SER   A N    1 
ATOM   123  C  CA   A SER   A 1 7   ? 11.801 -7.663  18.559  0.60 20.10 ?  7   SER   A CA   1 
ATOM   124  C  CA   B SER   A 1 7   ? 12.023 -7.980  19.061  0.40 22.97 ?  7   SER   A CA   1 
ATOM   125  C  C    A SER   A 1 7   ? 10.804 -7.416  17.431  0.60 18.49 ?  7   SER   A C    1 
ATOM   126  C  C    B SER   A 1 7   ? 10.971 -7.527  18.062  0.40 20.79 ?  7   SER   A C    1 
ATOM   127  O  O    A SER   A 1 7   ? 11.002 -6.531  16.597  0.60 17.89 ?  7   SER   A O    1 
ATOM   128  O  O    B SER   A 1 7   ? 11.133 -6.511  17.380  0.40 20.81 ?  7   SER   A O    1 
ATOM   129  C  CB   A SER   A 1 7   ? 11.562 -6.643  19.684  0.60 21.48 ?  7   SER   A CB   1 
ATOM   130  C  CB   B SER   A 1 7   ? 11.735 -7.389  20.446  0.40 24.18 ?  7   SER   A CB   1 
ATOM   131  O  OG   A SER   A 1 7   ? 10.259 -6.760  20.224  0.60 22.89 ?  7   SER   A OG   1 
ATOM   132  O  OG   B SER   A 1 7   ? 10.509 -7.880  20.957  0.40 25.18 ?  7   SER   A OG   1 
ATOM   133  H  H    A SER   A 1 7   ? 13.330 -6.867  17.602  0.60 23.91 ?  7   SER   A H    1 
ATOM   134  H  H    B SER   A 1 7   ? 13.342 -6.913  18.053  0.40 28.85 ?  7   SER   A H    1 
ATOM   135  H  HA   A SER   A 1 7   ? 11.641 -8.549  18.912  0.60 24.28 ?  7   SER   A HA   1 
ATOM   136  H  HA   B SER   A 1 7   ? 11.978 -8.946  19.128  0.40 27.72 ?  7   SER   A HA   1 
ATOM   137  H  HB2  A SER   A 1 7   ? 12.205 -6.804  20.392  0.60 25.95 ?  7   SER   A HB2  1 
ATOM   138  H  HB2  B SER   A 1 7   ? 12.452 -7.640  21.051  0.40 29.18 ?  7   SER   A HB2  1 
ATOM   139  H  HB3  A SER   A 1 7   ? 11.679 -5.748  19.328  0.60 25.95 ?  7   SER   A HB3  1 
ATOM   140  H  HB3  B SER   A 1 7   ? 11.684 -6.424  20.375  0.40 29.18 ?  7   SER   A HB3  1 
ATOM   141  H  HG   A SER   A 1 7   ? 10.146 -6.190  20.833  0.60 27.63 ?  7   SER   A HG   1 
ATOM   142  H  HG   B SER   A 1 7   ? 10.540 -8.718  21.025  0.40 30.38 ?  7   SER   A HG   1 
ATOM   143  N  N    A GLY   A 1 8   ? 9.721  -8.195  17.416  0.60 17.56 ?  8   GLY   A N    1 
ATOM   144  N  N    B GLY   A 1 8   ? 9.896  -8.304  17.975  0.40 18.84 ?  8   GLY   A N    1 
ATOM   145  C  CA   A GLY   A 1 8   ? 8.640  -7.957  16.476  0.60 16.83 ?  8   GLY   A CA   1 
ATOM   146  C  CA   B GLY   A 1 8   ? 8.804  -7.991  17.082  0.40 17.40 ?  8   GLY   A CA   1 
ATOM   147  C  C    A GLY   A 1 8   ? 8.854  -8.486  15.076  0.60 15.92 ?  8   GLY   A C    1 
ATOM   148  C  C    B GLY   A 1 8   ? 8.972  -8.475  15.665  0.40 15.79 ?  8   GLY   A C    1 
ATOM   149  O  O    A GLY   A 1 8   ? 8.133  -8.081  14.158  0.60 16.54 ?  8   GLY   A O    1 
ATOM   150  O  O    B GLY   A 1 8   ? 8.137  -8.144  14.817  0.40 15.83 ?  8   GLY   A O    1 
ATOM   151  H  H    A GLY   A 1 8   ? 9.592  -8.867  17.938  0.60 21.24 ?  8   GLY   A H    1 
ATOM   152  H  H    B GLY   A 1 8   ? 9.783  -9.025  18.422  0.40 22.78 ?  8   GLY   A H    1 
ATOM   153  H  HA2  A GLY   A 1 8   ? 7.825  -8.351  16.833  0.60 20.36 ?  8   GLY   A HA2  1 
ATOM   154  H  HA2  B GLY   A 1 8   ? 7.994  -8.395  17.419  0.40 21.04 ?  8   GLY   A HA2  1 
ATOM   155  H  HA3  A GLY   A 1 8   ? 8.496  -7.001  16.403  0.60 20.36 ?  8   GLY   A HA3  1 
ATOM   156  H  HA3  B GLY   A 1 8   ? 8.680  -7.031  17.057  0.40 21.04 ?  8   GLY   A HA3  1 
ATOM   157  N  N    A TYR   A 1 9   ? 9.819  -9.377  14.877  0.60 14.58 ?  9   TYR   A N    1 
ATOM   158  N  N    B TYR   A 1 9   ? 10.015 -9.249  15.375  0.40 14.68 ?  9   TYR   A N    1 
ATOM   159  C  CA   A TYR   A 1 9   ? 10.088 -9.944  13.565  0.60 13.44 ?  9   TYR   A CA   1 
ATOM   160  C  CA   B TYR   A 1 9   ? 10.227 -9.742  14.022  0.40 13.77 ?  9   TYR   A CA   1 
ATOM   161  C  C    A TYR   A 1 9   ? 9.210  -11.162 13.301  0.60 13.19 ?  9   TYR   A C    1 
ATOM   162  C  C    B TYR   A 1 9   ? 9.376  -10.976 13.751  0.40 13.05 ?  9   TYR   A C    1 
ATOM   163  O  O    A TYR   A 1 9   ? 8.875  -11.932 14.207  0.60 14.77 ?  9   TYR   A O    1 
ATOM   164  O  O    B TYR   A 1 9   ? 9.204  -11.843 14.616  0.40 14.12 ?  9   TYR   A O    1 
ATOM   165  C  CB   A TYR   A 1 9   ? 11.563 -10.349 13.434  0.60 13.61 ?  9   TYR   A CB   1 
ATOM   166  C  CB   B TYR   A 1 9   ? 11.707 -10.064 13.790  0.40 14.37 ?  9   TYR   A CB   1 
ATOM   167  C  CG   A TYR   A 1 9   ? 12.502 -9.171  13.316  0.60 14.06 ?  9   TYR   A CG   1 
ATOM   168  C  CG   B TYR   A 1 9   ? 12.546 -8.834  13.526  0.40 14.45 ?  9   TYR   A CG   1 
ATOM   169  C  CD1  A TYR   A 1 9   ? 12.845 -8.422  14.434  0.60 14.24 ?  9   TYR   A CD1  1 
ATOM   170  C  CD1  B TYR   A 1 9   ? 12.833 -7.939  14.546  0.40 14.77 ?  9   TYR   A CD1  1 
ATOM   171  C  CD2  A TYR   A 1 9   ? 13.028 -8.797  12.087  0.60 14.49 ?  9   TYR   A CD2  1 
ATOM   172  C  CD2  B TYR   A 1 9   ? 13.034 -8.557  12.255  0.40 14.13 ?  9   TYR   A CD2  1 
ATOM   173  C  CE1  A TYR   A 1 9   ? 13.685 -7.330  14.334  0.60 15.03 ?  9   TYR   A CE1  1 
ATOM   174  C  CE1  B TYR   A 1 9   ? 13.587 -6.808  14.312  0.40 14.68 ?  9   TYR   A CE1  1 
ATOM   175  C  CE2  A TYR   A 1 9   ? 13.871 -7.709  11.976  0.60 14.85 ?  9   TYR   A CE2  1 
ATOM   176  C  CE2  B TYR   A 1 9   ? 13.790 -7.425  12.011  0.40 14.02 ?  9   TYR   A CE2  1 
ATOM   177  C  CZ   A TYR   A 1 9   ? 14.192 -6.978  13.102  0.60 15.51 ?  9   TYR   A CZ   1 
ATOM   178  C  CZ   B TYR   A 1 9   ? 14.059 -6.557  13.044  0.40 14.26 ?  9   TYR   A CZ   1 
ATOM   179  O  OH   A TYR   A 1 9   ? 15.025 -5.897  12.994  0.60 16.48 ?  9   TYR   A OH   1 
ATOM   180  O  OH   B TYR   A 1 9   ? 14.805 -5.431  12.804  0.40 14.39 ?  9   TYR   A OH   1 
ATOM   181  H  H    A TYR   A 1 9   ? 10.334 -9.672  15.491  0.60 17.67 ?  9   TYR   A H    1 
ATOM   182  H  H    B TYR   A 1 9   ? 10.618 -9.497  15.939  0.40 17.79 ?  9   TYR   A H    1 
ATOM   183  H  HA   A TYR   A 1 9   ? 9.899  -9.282  12.879  0.60 16.29 ?  9   TYR   A HA   1 
ATOM   184  H  HA   B TYR   A 1 9   ? 9.978  -9.047  13.389  0.40 16.69 ?  9   TYR   A HA   1 
ATOM   185  H  HB2  A TYR   A 1 9   ? 11.825 -10.868 14.210  0.60 16.49 ?  9   TYR   A HB2  1 
ATOM   186  H  HB2  B TYR   A 1 9   ? 12.064 -10.510 14.574  0.40 17.41 ?  9   TYR   A HB2  1 
ATOM   187  H  HB3  A TYR   A 1 9   ? 11.657 -10.883 12.631  0.60 16.49 ?  9   TYR   A HB3  1 
ATOM   188  H  HB3  B TYR   A 1 9   ? 11.783 -10.649 13.017  0.40 17.41 ?  9   TYR   A HB3  1 
ATOM   189  H  HD1  A TYR   A 1 9   ? 12.495 -8.658  15.263  0.60 17.26 ?  9   TYR   A HD1  1 
ATOM   190  H  HD1  B TYR   A 1 9   ? 12.513 -8.107  15.402  0.40 17.88 ?  9   TYR   A HD1  1 
ATOM   191  H  HD2  A TYR   A 1 9   ? 12.811 -9.288  11.324  0.60 17.55 ?  9   TYR   A HD2  1 
ATOM   192  H  HD2  B TYR   A 1 9   ? 12.853 -9.141  11.555  0.40 17.12 ?  9   TYR   A HD2  1 
ATOM   193  H  HE1  A TYR   A 1 9   ? 13.907 -6.841  15.092  0.60 18.20 ?  9   TYR   A HE1  1 
ATOM   194  H  HE1  B TYR   A 1 9   ? 13.771 -6.218  15.005  0.40 17.78 ?  9   TYR   A HE1  1 
ATOM   195  H  HE2  A TYR   A 1 9   ? 14.223 -7.472  11.147  0.60 17.98 ?  9   TYR   A HE2  1 
ATOM   196  H  HE2  B TYR   A 1 9   ? 14.115 -7.249  11.154  0.40 16.99 ?  9   TYR   A HE2  1 
ATOM   197  H  HH   A TYR   A 1 9   ? 15.149 -5.556  13.750  0.60 19.94 ?  9   TYR   A HH   1 
ATOM   198  H  HH   B TYR   A 1 9   ? 14.921 -5.002  13.517  0.40 17.43 ?  9   TYR   A HH   1 
ATOM   199  N  N    A LEU   A 1 10  ? 8.853  -11.332 12.033  0.60 12.29 ?  10  LEU   A N    1 
ATOM   200  N  N    B LEU   A 1 10  ? 8.841  -11.038 12.535  0.40 12.18 ?  10  LEU   A N    1 
ATOM   201  C  CA   A LEU   A 1 10  ? 8.252  -12.564 11.550  0.60 12.13 ?  10  LEU   A CA   1 
ATOM   202  C  CA   B LEU   A 1 10  ? 8.181  -12.232 12.035  0.40 12.13 ?  10  LEU   A CA   1 
ATOM   203  C  C    A LEU   A 1 10  ? 9.373  -13.497 11.102  0.60 11.78 ?  10  LEU   A C    1 
ATOM   204  C  C    B LEU   A 1 10  ? 9.246  -13.194 11.521  0.40 11.72 ?  10  LEU   A C    1 
ATOM   205  O  O    A LEU   A 1 10  ? 10.326 -13.066 10.446  0.60 12.01 ?  10  LEU   A O    1 
ATOM   206  O  O    B LEU   A 1 10  ? 10.130 -12.802 10.753  0.40 11.69 ?  10  LEU   A O    1 
ATOM   207  C  CB   A LEU   A 1 10  ? 7.342  -12.253 10.362  0.60 13.01 ?  10  LEU   A CB   1 
ATOM   208  C  CB   B LEU   A 1 10  ? 7.226  -11.848 10.905  0.40 12.76 ?  10  LEU   A CB   1 
ATOM   209  C  CG   A LEU   A 1 10  ? 6.615  -13.431 9.712   0.60 14.68 ?  10  LEU   A CG   1 
ATOM   210  C  CG   B LEU   A 1 10  ? 6.445  -12.997 10.268  0.40 14.14 ?  10  LEU   A CG   1 
ATOM   211  C  CD1  A LEU   A 1 10  ? 5.558  -13.992 10.640  0.60 16.10 ?  10  LEU   A CD1  1 
ATOM   212  C  CD1  B LEU   A 1 10  ? 5.459  -13.587 11.264  0.40 15.53 ?  10  LEU   A CD1  1 
ATOM   213  C  CD2  A LEU   A 1 10  ? 6.003  -13.009 8.391   0.60 15.69 ?  10  LEU   A CD2  1 
ATOM   214  C  CD2  B LEU   A 1 10  ? 5.732  -12.517 9.012   0.40 15.34 ?  10  LEU   A CD2  1 
ATOM   215  H  H    A LEU   A 1 10  ? 8.957  -10.740 11.413  0.60 14.91 ?  10  LEU   A H    1 
ATOM   216  H  H    B LEU   A 1 10  ? 8.848  -10.383 11.972  0.40 14.78 ?  10  LEU   A H    1 
ATOM   217  H  HA   A LEU   A 1 10  ? 7.735  -12.992 12.254  0.60 14.72 ?  10  LEU   A HA   1 
ATOM   218  H  HA   B LEU   A 1 10  ? 7.671  -12.654 12.746  0.40 14.73 ?  10  LEU   A HA   1 
ATOM   219  H  HB2  A LEU   A 1 10  ? 6.661  -11.634 10.659  0.60 15.78 ?  10  LEU   A HB2  1 
ATOM   220  H  HB2  B LEU   A 1 10  ? 6.571  -11.213 11.251  0.40 15.48 ?  10  LEU   A HB2  1 
ATOM   221  H  HB3  A LEU   A 1 10  ? 7.879  -11.840 9.672   0.60 15.78 ?  10  LEU   A HB3  1 
ATOM   222  H  HB3  B LEU   A 1 10  ? 7.737  -11.419 10.201  0.40 15.48 ?  10  LEU   A HB3  1 
ATOM   223  H  HG   A LEU   A 1 10  ? 7.255  -14.143 9.530   0.60 17.78 ?  10  LEU   A HG   1 
ATOM   224  H  HG   B LEU   A 1 10  ? 7.066  -13.695 10.011  0.40 17.13 ?  10  LEU   A HG   1 
ATOM   225  H  HD11 A LEU   A 1 10  ? 5.153  -14.771 10.228  0.60 19.48 ?  10  LEU   A HD11 1 
ATOM   226  H  HD11 B LEU   A 1 10  ? 4.966  -14.302 10.831  0.40 18.81 ?  10  LEU   A HD11 1 
ATOM   227  H  HD12 A LEU   A 1 10  ? 5.973  -14.241 11.481  0.60 19.48 ?  10  LEU   A HD12 1 
ATOM   228  H  HD12 B LEU   A 1 10  ? 5.948  -13.938 12.025  0.40 18.81 ?  10  LEU   A HD12 1 
ATOM   229  H  HD13 A LEU   A 1 10  ? 4.885  -13.311 10.795  0.60 19.48 ?  10  LEU   A HD13 1 
ATOM   230  H  HD13 B LEU   A 1 10  ? 4.848  -12.892 11.554  0.40 18.81 ?  10  LEU   A HD13 1 
ATOM   231  H  HD21 A LEU   A 1 10  ? 5.543  -13.769 8.002   0.60 19.00 ?  10  LEU   A HD21 1 
ATOM   232  H  HD21 B LEU   A 1 10  ? 5.230  -13.257 8.634   0.40 18.58 ?  10  LEU   A HD21 1 
ATOM   233  H  HD22 A LEU   A 1 10  ? 5.376  -12.290 8.557   0.60 19.00 ?  10  LEU   A HD22 1 
ATOM   234  H  HD22 B LEU   A 1 10  ? 5.130  -11.795 9.247   0.40 18.58 ?  10  LEU   A HD22 1 
ATOM   235  H  HD23 A LEU   A 1 10  ? 6.710  -12.709 7.802   0.60 19.00 ?  10  LEU   A HD23 1 
ATOM   236  H  HD23 B LEU   A 1 10  ? 6.393  -12.205 8.374   0.40 18.58 ?  10  LEU   A HD23 1 
ATOM   237  N  N    A LYS   A 1 11  ? 9.260  -14.775 11.469  0.60 11.85 ?  11  LYS   A N    1 
ATOM   238  N  N    B LYS   A 1 11  ? 9.173  -14.446 11.954  0.40 11.53 ?  11  LYS   A N    1 
ATOM   239  C  CA   A LYS   A 1 11  ? 10.265 -15.778 11.139  0.60 11.66 ?  11  LYS   A CA   1 
ATOM   240  C  CA   B LYS   A 1 11  ? 10.139 -15.454 11.538  0.40 11.71 ?  11  LYS   A CA   1 
ATOM   241  C  C    A LYS   A 1 11  ? 9.916  -16.383 9.786   0.60 12.22 ?  11  LYS   A C    1 
ATOM   242  C  C    B LYS   A 1 11  ? 9.754  -15.983 10.162  0.40 11.15 ?  11  LYS   A C    1 
ATOM   243  O  O    A LYS   A 1 11  ? 8.863  -17.009 9.644   0.60 13.87 ?  11  LYS   A O    1 
ATOM   244  O  O    B LYS   A 1 11  ? 8.622  -16.433 9.961   0.40 11.58 ?  11  LYS   A O    1 
ATOM   245  C  CB   A LYS   A 1 11  ? 10.291 -16.850 12.231  0.60 11.78 ?  11  LYS   A CB   1 
ATOM   246  C  CB   B LYS   A 1 11  ? 10.172 -16.584 12.563  0.40 12.27 ?  11  LYS   A CB   1 
ATOM   247  C  CG   A LYS   A 1 11  ? 11.352 -17.938 12.088  0.60 12.33 ?  11  LYS   A CG   1 
ATOM   248  C  CG   B LYS   A 1 11  ? 11.117 -17.718 12.212  0.40 12.99 ?  11  LYS   A CG   1 
ATOM   249  C  CD   A LYS   A 1 11  ? 11.474 -18.714 13.411  0.60 12.70 ?  11  LYS   A CD   1 
ATOM   250  C  CD   B LYS   A 1 11  ? 11.136 -18.766 13.312  0.40 13.73 ?  11  LYS   A CD   1 
ATOM   251  C  CE   A LYS   A 1 11  ? 12.476 -19.865 13.353  0.60 12.46 ?  11  LYS   A CE   1 
ATOM   252  C  CE   B LYS   A 1 11  ? 12.145 -19.867 13.024  0.40 13.82 ?  11  LYS   A CE   1 
ATOM   253  N  NZ   A LYS   A 1 11  ? 13.845 -19.408 12.999  0.60 12.86 ?  11  LYS   A NZ   1 
ATOM   254  N  NZ   B LYS   A 1 11  ? 13.552 -19.367 13.010  0.40 13.81 ?  11  LYS   A NZ   1 
ATOM   255  H  H    A LYS   A 1 11  ? 8.587  -15.101 11.903  0.60 14.38 ?  11  LYS   A H    1 
ATOM   256  H  H    B LYS   A 1 11  ? 8.563  -14.733 12.487  0.40 14.00 ?  11  LYS   A H    1 
ATOM   257  H  HA   A LYS   A 1 11  ? 11.141 -15.369 11.083  0.60 14.15 ?  11  LYS   A HA   1 
ATOM   258  H  HA   B LYS   A 1 11  ? 11.018 -15.049 11.478  0.40 14.22 ?  11  LYS   A HA   1 
ATOM   259  H  HB2  A LYS   A 1 11  ? 10.449 -16.412 13.081  0.60 14.30 ?  11  LYS   A HB2  1 
ATOM   260  H  HB2  B LYS   A 1 11  ? 10.453 -16.212 13.415  0.40 14.89 ?  11  LYS   A HB2  1 
ATOM   261  H  HB3  A LYS   A 1 11  ? 9.431  -17.293 12.249  0.60 14.30 ?  11  LYS   A HB3  1 
ATOM   262  H  HB3  B LYS   A 1 11  ? 9.280  -16.950 12.645  0.40 14.89 ?  11  LYS   A HB3  1 
ATOM   263  H  HG2  A LYS   A 1 11  ? 11.091 -18.558 11.387  0.60 14.96 ?  11  LYS   A HG2  1 
ATOM   264  H  HG2  B LYS   A 1 11  ? 10.821 -18.141 11.391  0.40 15.75 ?  11  LYS   A HG2  1 
ATOM   265  H  HG3  A LYS   A 1 11  ? 12.210 -17.535 11.885  0.60 14.96 ?  11  LYS   A HG3  1 
ATOM   266  H  HG3  B LYS   A 1 11  ? 12.015 -17.365 12.106  0.40 15.75 ?  11  LYS   A HG3  1 
ATOM   267  H  HD2  A LYS   A 1 11  ? 11.758 -18.103 14.108  0.60 15.41 ?  11  LYS   A HD2  1 
ATOM   268  H  HD2  B LYS   A 1 11  ? 11.375 -18.342 14.151  0.40 16.64 ?  11  LYS   A HD2  1 
ATOM   269  H  HD3  A LYS   A 1 11  ? 10.606 -19.088 13.635  0.60 15.41 ?  11  LYS   A HD3  1 
ATOM   270  H  HD3  B LYS   A 1 11  ? 10.256 -19.170 13.380  0.40 16.64 ?  11  LYS   A HD3  1 
ATOM   271  H  HE2  A LYS   A 1 11  ? 12.521 -20.291 14.224  0.60 15.11 ?  11  LYS   A HE2  1 
ATOM   272  H  HE2  B LYS   A 1 11  ? 12.077 -20.547 13.708  0.40 16.74 ?  11  LYS   A HE2  1 
ATOM   273  H  HE3  A LYS   A 1 11  ? 12.192 -20.503 12.683  0.60 15.11 ?  11  LYS   A HE3  1 
ATOM   274  H  HE3  B LYS   A 1 11  ? 11.957 -20.248 12.151  0.40 16.74 ?  11  LYS   A HE3  1 
ATOM   275  H  HZ1  A LYS   A 1 11  ? 14.391 -20.110 12.928  0.60 15.59 ?  11  LYS   A HZ1  1 
ATOM   276  H  HZ1  B LYS   A 1 11  ? 14.108 -20.026 12.789  0.40 16.74 ?  11  LYS   A HZ1  1 
ATOM   277  H  HZ2  A LYS   A 1 11  ? 13.831 -18.975 12.222  0.60 15.59 ?  11  LYS   A HZ2  1 
ATOM   278  H  HZ2  B LYS   A 1 11  ? 13.639 -18.707 12.418  0.40 16.74 ?  11  LYS   A HZ2  1 
ATOM   279  H  HZ3  A LYS   A 1 11  ? 14.160 -18.863 13.628  0.60 15.59 ?  11  LYS   A HZ3  1 
ATOM   280  H  HZ3  B LYS   A 1 11  ? 13.775 -19.061 13.816  0.40 16.74 ?  11  LYS   A HZ3  1 
ATOM   281  N  N    A LEU   A 1 12  ? 10.784 -16.196 8.789   0.60 11.20 ?  12  LEU   A N    1 
ATOM   282  N  N    B LEU   A 1 12  ? 10.682 -15.915 9.208   0.40 11.34 ?  12  LEU   A N    1 
ATOM   283  C  CA   A LEU   A 1 12  ? 10.532 -16.795 7.480   0.60 11.60 ?  12  LEU   A CA   1 
ATOM   284  C  CA   B LEU   A 1 12  ? 10.431 -16.439 7.869   0.40 11.74 ?  12  LEU   A CA   1 
ATOM   285  C  C    A LEU   A 1 12  ? 11.133 -18.189 7.351   0.60 11.81 ?  12  LEU   A C    1 
ATOM   286  C  C    B LEU   A 1 12  ? 10.990 -17.839 7.662   0.40 11.88 ?  12  LEU   A C    1 
ATOM   287  O  O    A LEU   A 1 12  ? 10.514 -19.070 6.746   0.60 12.03 ?  12  LEU   A O    1 
ATOM   288  O  O    B LEU   A 1 12  ? 10.311 -18.692 7.079   0.40 11.78 ?  12  LEU   A O    1 
ATOM   289  C  CB   A LEU   A 1 12  ? 11.079 -15.909 6.358   0.60 12.00 ?  12  LEU   A CB   1 
ATOM   290  C  CB   B LEU   A 1 12  ? 11.007 -15.505 6.799   0.40 12.33 ?  12  LEU   A CB   1 
ATOM   291  C  CG   A LEU   A 1 12  ? 10.432 -14.539 6.166   0.60 13.03 ?  12  LEU   A CG   1 
ATOM   292  C  CG   B LEU   A 1 12  ? 10.320 -14.150 6.638   0.40 12.66 ?  12  LEU   A CG   1 
ATOM   293  C  CD1  A LEU   A 1 12  ? 11.188 -13.771 5.100   0.60 13.72 ?  12  LEU   A CD1  1 
ATOM   294  C  CD1  B LEU   A 1 12  ? 10.874 -13.415 5.423   0.40 13.29 ?  12  LEU   A CD1  1 
ATOM   295  C  CD2  A LEU   A 1 12  ? 8.963  -14.681 5.791   0.60 13.43 ?  12  LEU   A CD2  1 
ATOM   296  C  CD2  B LEU   A 1 12  ? 8.811  -14.311 6.534   0.40 12.90 ?  12  LEU   A CD2  1 
ATOM   297  H  H    A LEU   A 1 12  ? 11.511 -15.730 8.834   0.60 13.61 ?  12  LEU   A H    1 
ATOM   298  H  H    B LEU   A 1 12  ? 11.461 -15.551 9.305   0.40 13.78 ?  12  LEU   A H    1 
ATOM   299  H  HA   A LEU   A 1 12  ? 9.573  -16.878 7.355   0.60 14.08 ?  12  LEU   A HA   1 
ATOM   300  H  HA   B LEU   A 1 12  ? 9.473  -16.488 7.735   0.40 14.25 ?  12  LEU   A HA   1 
ATOM   301  H  HB2  A LEU   A 1 12  ? 12.019 -15.761 6.526   0.60 14.57 ?  12  LEU   A HB2  1 
ATOM   302  H  HB2  B LEU   A 1 12  ? 11.937 -15.329 7.010   0.40 14.96 ?  12  LEU   A HB2  1 
ATOM   303  H  HB3  A LEU   A 1 12  ? 10.977 -16.393 5.520   0.60 14.57 ?  12  LEU   A HB3  1 
ATOM   304  H  HB3  B LEU   A 1 12  ? 10.953 -15.955 5.942   0.40 14.96 ?  12  LEU   A HB3  1 
ATOM   305  H  HG   A LEU   A 1 12  ? 10.484 -14.043 6.996   0.60 15.80 ?  12  LEU   A HG   1 
ATOM   306  H  HG   B LEU   A 1 12  ? 10.508 -13.611 7.421   0.40 15.36 ?  12  LEU   A HG   1 
ATOM   307  H  HD11 A LEU   A 1 12  ? 10.773 -12.904 4.982   0.60 16.63 ?  12  LEU   A HD11 1 
ATOM   308  H  HD11 B LEU   A 1 12  ? 10.383 -12.587 5.301   0.40 16.11 ?  12  LEU   A HD11 1 
ATOM   309  H  HD12 A LEU   A 1 12  ? 12.109 -13.662 5.386   0.60 16.63 ?  12  LEU   A HD12 1 
ATOM   310  H  HD12 B LEU   A 1 12  ? 11.813 -13.223 5.569   0.40 16.11 ?  12  LEU   A HD12 1 
ATOM   311  H  HD13 A LEU   A 1 12  ? 11.158 -14.271 4.269   0.60 16.63 ?  12  LEU   A HD13 1 
ATOM   312  H  HD13 B LEU   A 1 12  ? 10.770 -13.977 4.638   0.40 16.11 ?  12  LEU   A HD13 1 
ATOM   313  H  HD21 A LEU   A 1 12  ? 8.591  -13.802 5.628   0.60 16.28 ?  12  LEU   A HD21 1 
ATOM   314  H  HD21 B LEU   A 1 12  ? 8.427  -13.487 6.198   0.40 15.64 ?  12  LEU   A HD21 1 
ATOM   315  H  HD22 A LEU   A 1 12  ? 8.892  -15.223 4.988   0.60 16.28 ?  12  LEU   A HD22 1 
ATOM   316  H  HD22 B LEU   A 1 12  ? 8.611  -15.042 5.929   0.40 15.64 ?  12  LEU   A HD22 1 
ATOM   317  H  HD23 A LEU   A 1 12  ? 8.486  -15.112 6.519   0.60 16.28 ?  12  LEU   A HD23 1 
ATOM   318  H  HD23 B LEU   A 1 12  ? 8.453  -14.507 7.416   0.40 15.64 ?  12  LEU   A HD23 1 
ATOM   319  N  N    A THR   A 1 13  ? 12.342 -18.381 7.875   0.60 12.39 ?  13  THR   A N    1 
ATOM   320  N  N    B THR   A 1 13  ? 12.220 -18.086 8.105   0.40 11.99 ?  13  THR   A N    1 
ATOM   321  C  CA   A THR   A 1 13  ? 13.051 -19.655 7.842   0.60 12.83 ?  13  THR   A CA   1 
ATOM   322  C  CA   B THR   A 1 13  ? 12.869 -19.379 7.927   0.40 12.35 ?  13  THR   A CA   1 
ATOM   323  C  C    A THR   A 1 13  ? 13.796 -19.824 9.164   0.60 12.94 ?  13  THR   A C    1 
ATOM   324  C  C    B THR   A 1 13  ? 13.680 -19.691 9.177   0.40 13.15 ?  13  THR   A C    1 
ATOM   325  O  O    A THR   A 1 13  ? 13.662 -19.017 10.088  0.60 13.05 ?  13  THR   A O    1 
ATOM   326  O  O    B THR   A 1 13  ? 13.643 -18.963 10.173  0.40 13.45 ?  13  THR   A O    1 
ATOM   327  C  CB   A THR   A 1 13  ? 14.050 -19.720 6.678   0.60 13.09 ?  13  THR   A CB   1 
ATOM   328  C  CB   B THR   A 1 13  ? 13.788 -19.391 6.699   0.40 12.39 ?  13  THR   A CB   1 
ATOM   329  O  OG1  A THR   A 1 13  ? 15.110 -18.794 6.926   0.60 13.31 ?  13  THR   A OG1  1 
ATOM   330  O  OG1  B THR   A 1 13  ? 14.862 -18.470 6.909   0.40 12.73 ?  13  THR   A OG1  1 
ATOM   331  C  CG2  A THR   A 1 13  ? 13.392 -19.390 5.346   0.60 13.52 ?  13  THR   A CG2  1 
ATOM   332  C  CG2  B THR   A 1 13  ? 13.038 -19.023 5.423   0.40 12.38 ?  13  THR   A CG2  1 
ATOM   333  H  H    A THR   A 1 13  ? 12.789 -17.760 8.254   0.60 15.03 ?  13  THR   A H    1 
ATOM   334  H  H    B THR   A 1 13  ? 12.707 -17.502 8.511   0.40 14.55 ?  13  THR   A H    1 
ATOM   335  H  HA   A THR   A 1 13  ? 12.418 -20.385 7.742   0.60 15.56 ?  13  THR   A HA   1 
ATOM   336  H  HA   B THR   A 1 13  ? 12.195 -20.065 7.819   0.40 14.98 ?  13  THR   A HA   1 
ATOM   337  H  HB   A THR   A 1 13  ? 14.418 -20.619 6.614   0.60 15.88 ?  13  THR   A HB   1 
ATOM   338  H  HB   B THR   A 1 13  ? 14.152 -20.283 6.587   0.40 15.03 ?  13  THR   A HB   1 
ATOM   339  H  HG1  A THR   A 1 13  ? 15.673 -19.135 7.445   0.60 16.14 ?  13  THR   A HG1  1 
ATOM   340  H  HG1  B THR   A 1 13  ? 15.381 -18.474 6.247   0.40 15.44 ?  13  THR   A HG1  1 
ATOM   341  H  HG21 A THR   A 1 13  ? 14.012 -19.568 4.617   0.60 16.39 ?  13  THR   A HG21 1 
ATOM   342  H  HG21 B THR   A 1 13  ? 13.631 -19.100 4.657   0.40 15.02 ?  13  THR   A HG21 1 
ATOM   343  H  HG22 A THR   A 1 13  ? 12.602 -19.938 5.223   0.60 16.39 ?  13  THR   A HG22 1 
ATOM   344  H  HG22 B THR   A 1 13  ? 12.286 -19.622 5.296   0.40 15.02 ?  13  THR   A HG22 1 
ATOM   345  H  HG23 A THR   A 1 13  ? 13.140 -18.456 5.323   0.60 16.39 ?  13  THR   A HG23 1 
ATOM   346  H  HG23 B THR   A 1 13  ? 12.712 -18.113 5.477   0.40 15.02 ?  13  THR   A HG23 1 
ATOM   347  N  N    A ASP   A 1 14  ? 14.622 -20.867 9.236   0.60 13.34 ?  14  ASP   A N    1 
ATOM   348  N  N    B ASP   A 1 14  ? 14.446 -20.780 9.104   0.40 13.60 ?  14  ASP   A N    1 
ATOM   349  C  CA   A ASP   A 1 14  ? 15.437 -21.099 10.423  0.60 13.78 ?  14  ASP   A CA   1 
ATOM   350  C  CA   B ASP   A 1 14  ? 15.336 -21.123 10.205  0.40 13.97 ?  14  ASP   A CA   1 
ATOM   351  C  C    A ASP   A 1 14  ? 16.207 -19.851 10.853  0.60 12.97 ?  14  ASP   A C    1 
ATOM   352  C  C    B ASP   A 1 14  ? 16.273 -19.970 10.544  0.40 12.52 ?  14  ASP   A C    1 
ATOM   353  O  O    A ASP   A 1 14  ? 16.349 -19.583 12.053  0.60 13.45 ?  14  ASP   A O    1 
ATOM   354  O  O    B ASP   A 1 14  ? 16.641 -19.799 11.712  0.40 12.55 ?  14  ASP   A O    1 
ATOM   355  C  CB   A ASP   A 1 14  ? 16.420 -22.229 10.135  0.60 15.56 ?  14  ASP   A CB   1 
ATOM   356  C  CB   B ASP   A 1 14  ? 16.138 -22.383 9.868   0.40 16.31 ?  14  ASP   A CB   1 
ATOM   357  C  CG   A ASP   A 1 14  ? 17.248 -22.575 11.330  0.60 18.96 ?  14  ASP   A CG   1 
ATOM   358  C  CG   B ASP   A 1 14  ? 17.241 -22.656 10.874  0.40 18.65 ?  14  ASP   A CG   1 
ATOM   359  O  OD1  A ASP   A 1 14  ? 16.678 -23.137 12.288  0.60 19.41 ?  14  ASP   A OD1  1 
ATOM   360  O  OD1  B ASP   A 1 14  ? 16.958 -22.636 12.091  0.40 19.56 ?  14  ASP   A OD1  1 
ATOM   361  O  OD2  A ASP   A 1 14  ? 18.455 -22.269 11.313  0.60 20.87 -1 14  ASP   A OD2  1 
ATOM   362  O  OD2  B ASP   A 1 14  ? 18.390 -22.900 10.451  0.40 20.03 -1 14  ASP   A OD2  1 
ATOM   363  H  H    A ASP   A 1 14  ? 14.734 -21.452 8.616   0.60 16.18 ?  14  ASP   A H    1 
ATOM   364  H  H    B ASP   A 1 14  ? 14.472 -21.314 8.432   0.40 16.48 ?  14  ASP   A H    1 
ATOM   365  H  HA   A ASP   A 1 14  ? 14.868 -21.369 11.161  0.60 16.71 ?  14  ASP   A HA   1 
ATOM   366  H  HA   B ASP   A 1 14  ? 14.801 -21.317 10.989  0.40 16.93 ?  14  ASP   A HA   1 
ATOM   367  H  HB2  A ASP   A 1 14  ? 15.925 -23.019 9.870   0.60 18.84 ?  14  ASP   A HB2  1 
ATOM   368  H  HB2  B ASP   A 1 14  ? 15.542 -23.155 9.874   0.40 19.73 ?  14  ASP   A HB2  1 
ATOM   369  H  HB3  A ASP   A 1 14  ? 17.022 -21.958 9.426   0.60 18.84 ?  14  ASP   A HB3  1 
ATOM   370  H  HB3  B ASP   A 1 14  ? 16.536 -22.286 8.988   0.40 19.73 ?  14  ASP   A HB3  1 
ATOM   371  N  N    A ASN   A 1 15  ? 16.721 -19.075 9.894   0.60 12.39 ?  15  ASN   A N    1 
ATOM   372  N  N    B ASN   A 1 15  ? 16.656 -19.154 9.550   0.40 11.30 ?  15  ASN   A N    1 
ATOM   373  C  CA   A ASN   A 1 15  ? 17.685 -18.021 10.195  0.60 12.64 ?  15  ASN   A CA   1 
ATOM   374  C  CA   B ASN   A 1 15  ? 17.679 -18.134 9.766   0.40 11.54 ?  15  ASN   A CA   1 
ATOM   375  C  C    A ASN   A 1 15  ? 17.311 -16.641 9.682   0.60 12.44 ?  15  ASN   A C    1 
ATOM   376  C  C    B ASN   A 1 15  ? 17.326 -16.742 9.236   0.40 11.97 ?  15  ASN   A C    1 
ATOM   377  O  O    A ASN   A 1 15  ? 18.038 -15.691 9.989   0.60 11.85 ?  15  ASN   A O    1 
ATOM   378  O  O    B ASN   A 1 15  ? 18.185 -15.852 9.275   0.40 12.25 ?  15  ASN   A O    1 
ATOM   379  C  CB   A ASN   A 1 15  ? 19.069 -18.373 9.623   0.60 12.95 ?  15  ASN   A CB   1 
ATOM   380  C  CB   B ASN   A 1 15  ? 19.034 -18.592 9.199   0.40 10.77 ?  15  ASN   A CB   1 
ATOM   381  C  CG   A ASN   A 1 15  ? 19.048 -18.530 8.118   0.60 13.05 ?  15  ASN   A CG   1 
ATOM   382  C  CG   B ASN   A 1 15  ? 19.047 -18.620 7.686   0.40 11.18 ?  15  ASN   A CG   1 
ATOM   383  O  OD1  A ASN   A 1 15  ? 18.253 -19.303 7.576   0.60 13.15 ?  15  ASN   A OD1  1 
ATOM   384  O  OD1  B ASN   A 1 15  ? 18.432 -19.489 7.064   0.40 11.59 ?  15  ASN   A OD1  1 
ATOM   385  N  ND2  A ASN   A 1 15  ? 19.905 -17.775 7.428   0.60 13.35 ?  15  ASN   A ND2  1 
ATOM   386  N  ND2  B ASN   A 1 15  ? 19.743 -17.663 7.084   0.40 11.42 ?  15  ASN   A ND2  1 
ATOM   387  H  H    A ASN   A 1 15  ? 16.525 -19.134 9.067   0.60 15.04 ?  15  ASN   A H    1 
ATOM   388  H  H    B ASN   A 1 15  ? 16.337 -19.191 8.750   0.40 13.73 ?  15  ASN   A H    1 
ATOM   389  H  HA   A ASN   A 1 15  ? 17.788 -17.949 11.159  0.60 15.33 ?  15  ASN   A HA   1 
ATOM   390  H  HA   B ASN   A 1 15  ? 17.801 -18.048 10.716  0.40 14.01 ?  15  ASN   A HA   1 
ATOM   391  H  HB2  A ASN   A 1 15  ? 19.699 -17.661 9.845   0.60 15.70 ?  15  ASN   A HB2  1 
ATOM   392  H  HB2  B ASN   A 1 15  ? 19.729 -17.979 9.499   0.40 13.08 ?  15  ASN   A HB2  1 
ATOM   393  H  HB3  A ASN   A 1 15  ? 19.370 -19.208 10.008  0.60 15.70 ?  15  ASN   A HB3  1 
ATOM   394  H  HB3  B ASN   A 1 15  ? 19.242 -19.492 9.525   0.40 13.08 ?  15  ASN   A HB3  1 
ATOM   395  H  HD21 A ASN   A 1 15  ? 19.933 -17.822 6.567   0.60 16.19 ?  15  ASN   A HD21 1 
ATOM   396  H  HD21 B ASN   A 1 15  ? 19.789 -17.639 6.226   0.40 13.87 ?  15  ASN   A HD21 1 
ATOM   397  H  HD22 A ASN   A 1 15  ? 20.445 -17.241 7.839   0.60 16.19 ?  15  ASN   A HD22 1 
ATOM   398  H  HD22 B ASN   A 1 15  ? 20.156 -17.069 7.552   0.40 13.87 ?  15  ASN   A HD22 1 
ATOM   399  N  N    A VAL   A 1 16  ? 16.241 -16.494 8.903   0.60 12.92 ?  16  VAL   A N    1 
ATOM   400  N  N    B VAL   A 1 16  ? 16.098 -16.508 8.775   0.40 12.16 ?  16  VAL   A N    1 
ATOM   401  C  CA   A VAL   A 1 16  ? 15.834 -15.211 8.342   0.60 13.10 ?  16  VAL   A CA   1 
ATOM   402  C  CA   B VAL   A 1 16  ? 15.720 -15.234 8.165   0.40 12.24 ?  16  VAL   A CA   1 
ATOM   403  C  C    A VAL   A 1 16  ? 14.553 -14.745 9.013   0.60 13.14 ?  16  VAL   A C    1 
ATOM   404  C  C    B VAL   A 1 16  ? 14.463 -14.701 8.850   0.40 12.12 ?  16  VAL   A C    1 
ATOM   405  O  O    A VAL   A 1 16  ? 13.588 -15.510 9.162   0.60 13.20 ?  16  VAL   A O    1 
ATOM   406  O  O    B VAL   A 1 16  ? 13.433 -15.388 8.888   0.40 11.50 ?  16  VAL   A O    1 
ATOM   407  C  CB   A VAL   A 1 16  ? 15.668 -15.259 6.815   0.60 13.14 ?  16  VAL   A CB   1 
ATOM   408  C  CB   B VAL   A 1 16  ? 15.511 -15.370 6.646   0.40 12.81 ?  16  VAL   A CB   1 
ATOM   409  C  CG1  A VAL   A 1 16  ? 15.247 -13.880 6.286   0.60 13.62 ?  16  VAL   A CG1  1 
ATOM   410  C  CG1  B VAL   A 1 16  ? 15.057 -14.050 6.044   0.40 13.18 ?  16  VAL   A CG1  1 
ATOM   411  C  CG2  A VAL   A 1 16  ? 16.953 -15.716 6.157   0.60 14.16 ?  16  VAL   A CG2  1 
ATOM   412  C  CG2  B VAL   A 1 16  ? 16.790 -15.866 5.965   0.40 13.30 ?  16  VAL   A CG2  1 
ATOM   413  H  H    A VAL   A 1 16  ? 15.724 -17.142 8.695   0.60 15.67 ?  16  VAL   A H    1 
ATOM   414  H  H    B VAL   A 1 16  ? 15.456 -17.081 8.812   0.40 14.76 ?  16  VAL   A H    1 
ATOM   415  H  HA   A VAL   A 1 16  ? 16.520 -14.555 8.541   0.60 15.89 ?  16  VAL   A HA   1 
ATOM   416  H  HA   B VAL   A 1 16  ? 16.432 -14.592 8.310   0.40 14.86 ?  16  VAL   A HA   1 
ATOM   417  H  HB   A VAL   A 1 16  ? 14.969 -15.893 6.596   0.60 15.93 ?  16  VAL   A HB   1 
ATOM   418  H  HB   B VAL   A 1 16  ? 14.819 -16.028 6.482   0.40 15.54 ?  16  VAL   A HB   1 
ATOM   419  H  HG11 A VAL   A 1 16  ? 15.323 -13.879 5.320   0.60 16.51 ?  16  VAL   A HG11 1 
ATOM   420  H  HG11 B VAL   A 1 16  ? 15.137 -14.104 5.079   0.40 15.99 ?  16  VAL   A HG11 1 
ATOM   421  H  HG12 A VAL   A 1 16  ? 14.326 -13.707 6.543   0.60 16.51 ?  16  VAL   A HG12 1 
ATOM   422  H  HG12 B VAL   A 1 16  ? 14.135 -13.892 6.291   0.40 15.99 ?  16  VAL   A HG12 1 
ATOM   423  H  HG13 A VAL   A 1 16  ? 15.829 -13.204 6.665   0.60 16.51 ?  16  VAL   A HG13 1 
ATOM   424  H  HG13 B VAL   A 1 16  ? 15.623 -13.341 6.383   0.40 15.99 ?  16  VAL   A HG13 1 
ATOM   425  H  HG21 A VAL   A 1 16  ? 16.915 -15.508 5.212   0.60 17.16 ?  16  VAL   A HG21 1 
ATOM   426  H  HG21 B VAL   A 1 16  ? 16.664 -15.855 5.003   0.40 16.13 ?  16  VAL   A HG21 1 
ATOM   427  H  HG22 A VAL   A 1 16  ? 17.699 -15.258 6.570   0.60 17.16 ?  16  VAL   A HG22 1 
ATOM   428  H  HG22 B VAL   A 1 16  ? 17.527 -15.281 6.205   0.40 16.13 ?  16  VAL   A HG22 1 
ATOM   429  H  HG23 A VAL   A 1 16  ? 17.045 -16.673 6.285   0.60 17.16 ?  16  VAL   A HG23 1 
ATOM   430  H  HG23 B VAL   A 1 16  ? 16.981 -16.772 6.261   0.40 16.13 ?  16  VAL   A HG23 1 
ATOM   431  N  N    . TYR   A 1 17  ? 14.552 -13.470 9.376   1.00 12.78 ?  17  TYR   A N    1 
ATOM   432  C  CA   . TYR   A 1 17  ? 13.473 -12.793 10.078  1.00 12.74 ?  17  TYR   A CA   1 
ATOM   433  C  C    . TYR   A 1 17  ? 13.200 -11.466 9.381   1.00 13.31 ?  17  TYR   A C    1 
ATOM   434  O  O    . TYR   A 1 17  ? 14.104 -10.898 8.763   1.00 13.71 ?  17  TYR   A O    1 
ATOM   435  C  CB   . TYR   A 1 17  ? 13.911 -12.521 11.521  1.00 13.44 ?  17  TYR   A CB   1 
ATOM   436  C  CG   . TYR   A 1 17  ? 14.113 -13.784 12.329  1.00 14.15 ?  17  TYR   A CG   1 
ATOM   437  C  CD1  . TYR   A 1 17  ? 15.289 -14.527 12.238  1.00 14.96 ?  17  TYR   A CD1  1 
ATOM   438  C  CD2  . TYR   A 1 17  ? 13.115 -14.252 13.167  1.00 14.42 ?  17  TYR   A CD2  1 
ATOM   439  C  CE1  . TYR   A 1 17  ? 15.459 -15.702 12.969  1.00 15.31 ?  17  TYR   A CE1  1 
ATOM   440  C  CE2  . TYR   A 1 17  ? 13.274 -15.426 13.900  1.00 14.99 ?  17  TYR   A CE2  1 
ATOM   441  C  CZ   . TYR   A 1 17  ? 14.446 -16.146 13.802  1.00 15.40 ?  17  TYR   A CZ   1 
ATOM   442  O  OH   . TYR   A 1 17  ? 14.602 -17.301 14.537  1.00 16.37 ?  17  TYR   A OH   1 
ATOM   443  H  H    A TYR   A 1 17  ? 15.213 -12.943 9.212   0.60 15.49 ?  17  TYR   A H    1 
ATOM   444  H  H    B TYR   A 1 17  ? 15.268 -12.994 9.333   0.40 15.49 ?  17  TYR   A H    1 
ATOM   445  H  HA   . TYR   A 1 17  ? 12.670 -13.339 10.075  1.00 15.45 ?  17  TYR   A HA   1 
ATOM   446  H  HB2  . TYR   A 1 17  ? 14.748 -12.034 11.504  1.00 16.29 ?  17  TYR   A HB2  1 
ATOM   447  H  HB3  . TYR   A 1 17  ? 13.232 -11.992 11.957  1.00 16.29 ?  17  TYR   A HB3  1 
ATOM   448  H  HD1  . TYR   A 1 17  ? 15.974 -14.234 11.676  1.00 18.12 ?  17  TYR   A HD1  1 
ATOM   449  H  HD2  . TYR   A 1 17  ? 12.318 -13.779 13.236  1.00 17.47 ?  17  TYR   A HD2  1 
ATOM   450  H  HE1  . TYR   A 1 17  ? 16.258 -16.185 12.900  1.00 18.53 ?  17  TYR   A HE1  1 
ATOM   451  H  HE2  . TYR   A 1 17  ? 12.592 -15.721 14.460  1.00 18.16 ?  17  TYR   A HE2  1 
ATOM   452  H  HH   . TYR   A 1 17  ? 13.879 -17.492 14.920  1.00 19.81 ?  17  TYR   A HH   1 
ATOM   453  N  N    . ILE   A 1 18  ? 11.967 -10.951 9.483   1.00 13.52 ?  18  ILE   A N    1 
ATOM   454  C  CA   . ILE   A 1 18  ? 11.582 -9.750  8.744   1.00 13.95 ?  18  ILE   A CA   1 
ATOM   455  C  C    . ILE   A 1 18  ? 10.629 -8.885  9.561   1.00 14.24 ?  18  ILE   A C    1 
ATOM   456  O  O    . ILE   A 1 18  ? 9.814  -9.393  10.340  1.00 14.86 ?  18  ILE   A O    1 
ATOM   457  C  CB   . ILE   A 1 18  ? 10.988 -10.131 7.372   1.00 14.32 ?  18  ILE   A CB   1 
ATOM   458  C  CG1  . ILE   A 1 18  ? 10.925 -8.927  6.432   1.00 15.32 ?  18  ILE   A CG1  1 
ATOM   459  C  CG2  . ILE   A 1 18  ? 9.633  -10.812 7.542   1.00 14.86 ?  18  ILE   A CG2  1 
ATOM   460  C  CD1  . ILE   A 1 18  ? 10.679 -9.318  5.003   1.00 17.13 ?  18  ILE   A CD1  1 
ATOM   461  H  H    . ILE   A 1 18  ? 11.338 -11.293 9.962   1.00 16.39 ?  18  ILE   A H    1 
ATOM   462  H  HA   . ILE   A 1 18  ? 12.388 -9.228  8.579   1.00 16.91 ?  18  ILE   A HA   1 
ATOM   463  H  HB   . ILE   A 1 18  ? 11.587 -10.773 6.966   1.00 17.34 ?  18  ILE   A HB   1 
ATOM   464  H  HG12 . ILE   A 1 18  ? 10.207 -8.342  6.705   1.00 18.54 ?  18  ILE   A HG12 1 
ATOM   465  H  HG13 . ILE   A 1 18  ? 11.773 -8.453  6.462   1.00 18.54 ?  18  ILE   A HG13 1 
ATOM   466  H  HG21 . ILE   A 1 18  ? 9.344  -11.154 6.682   1.00 17.99 ?  18  ILE   A HG21 1 
ATOM   467  H  HG22 . ILE   A 1 18  ? 9.724  -11.535 8.176   1.00 17.99 ?  18  ILE   A HG22 1 
ATOM   468  H  HG23 . ILE   A 1 18  ? 8.989  -10.161 7.867   1.00 17.99 ?  18  ILE   A HG23 1 
ATOM   469  H  HD11 . ILE   A 1 18  ? 10.709 -8.521  4.446   1.00 20.72 ?  18  ILE   A HD11 1 
ATOM   470  H  HD12 . ILE   A 1 18  ? 11.365 -9.941  4.719   1.00 20.72 ?  18  ILE   A HD12 1 
ATOM   471  H  HD13 . ILE   A 1 18  ? 9.805  -9.732  4.934   1.00 20.72 ?  18  ILE   A HD13 1 
ATOM   472  N  N    A LYS   A 1 19  ? 10.752 -7.563  9.416   0.60 14.74 ?  19  LYS   A N    1 
ATOM   473  N  N    B LYS   A 1 19  ? 10.703 -7.577  9.307   0.40 14.17 ?  19  LYS   A N    1 
ATOM   474  C  CA   A LYS   A 1 19  ? 9.975  -6.631  10.226  0.60 15.54 ?  19  LYS   A CA   1 
ATOM   475  C  CA   B LYS   A 1 19  ? 9.860  -6.590  9.961   0.40 14.08 ?  19  LYS   A CA   1 
ATOM   476  C  C    A LYS   A 1 19  ? 9.786  -5.333  9.453   0.60 15.24 ?  19  LYS   A C    1 
ATOM   477  C  C    B LYS   A 1 19  ? 9.645  -5.403  9.030   0.40 13.88 ?  19  LYS   A C    1 
ATOM   478  O  O    A LYS   A 1 19  ? 10.693 -4.902  8.740   0.60 15.08 ?  19  LYS   A O    1 
ATOM   479  O  O    B LYS   A 1 19  ? 10.521 -5.056  8.232   0.40 13.48 ?  19  LYS   A O    1 
ATOM   480  C  CB   A LYS   A 1 19  ? 10.700 -6.362  11.556  0.60 16.17 ?  19  LYS   A CB   1 
ATOM   481  C  CB   B LYS   A 1 19  ? 10.541 -6.102  11.239  0.40 14.09 ?  19  LYS   A CB   1 
ATOM   482  C  CG   A LYS   A 1 19  ? 10.054 -5.335  12.478  0.60 17.03 ?  19  LYS   A CG   1 
ATOM   483  C  CG   B LYS   A 1 19  ? 9.669  -5.272  12.154  0.40 15.26 ?  19  LYS   A CG   1 
ATOM   484  C  CD   A LYS   A 1 19  ? 10.970 -5.059  13.663  0.60 17.47 ?  19  LYS   A CD   1 
ATOM   485  C  CD   B LYS   A 1 19  ? 10.454 -4.914  13.402  0.40 16.19 ?  19  LYS   A CD   1 
ATOM   486  C  CE   A LYS   A 1 19  ? 10.363 -4.081  14.648  0.60 17.78 ?  19  LYS   A CE   1 
ATOM   487  C  CE   B LYS   A 1 19  ? 9.680  -4.000  14.330  0.40 16.74 ?  19  LYS   A CE   1 
ATOM   488  N  NZ   A LYS   A 1 19  ? 11.227 -3.933  15.854  0.60 17.83 ?  19  LYS   A NZ   1 
ATOM   489  N  NZ   B LYS   A 1 19  ? 10.540 -3.532  15.455  0.40 16.67 ?  19  LYS   A NZ   1 
ATOM   490  H  H    A LYS   A 1 19  ? 11.285 -7.178  8.854   0.60 17.85 ?  19  LYS   A H    1 
ATOM   491  H  H    B LYS   A 1 19  ? 11.262 -7.237  8.743   0.40 17.17 ?  19  LYS   A H    1 
ATOM   492  H  HA   A LYS   A 1 19  ? 9.105  -7.007  10.419  0.60 18.81 ?  19  LYS   A HA   1 
ATOM   493  H  HA   B LYS   A 1 19  ? 9.008  -6.994  10.181  0.40 17.06 ?  19  LYS   A HA   1 
ATOM   494  H  HB2  A LYS   A 1 19  ? 10.746 -7.198  12.053  0.60 19.57 ?  19  LYS   A HB2  1 
ATOM   495  H  HB2  B LYS   A 1 19  ? 10.841 -6.874  11.739  0.40 17.07 ?  19  LYS   A HB2  1 
ATOM   496  H  HB3  A LYS   A 1 19  ? 11.597 -6.055  11.365  0.60 19.57 ?  19  LYS   A HB3  1 
ATOM   497  H  HB3  B LYS   A 1 19  ? 11.303 -5.558  10.987  0.40 17.07 ?  19  LYS   A HB3  1 
ATOM   498  H  HG2  A LYS   A 1 19  ? 9.917  -4.503  12.000  0.60 20.60 ?  19  LYS   A HG2  1 
ATOM   499  H  HG2  B LYS   A 1 19  ? 9.406  -4.455  11.702  0.40 18.48 ?  19  LYS   A HG2  1 
ATOM   500  H  HG3  A LYS   A 1 19  ? 9.212  -5.680  12.814  0.60 20.60 ?  19  LYS   A HG3  1 
ATOM   501  H  HG3  B LYS   A 1 19  ? 8.886  -5.787  12.412  0.40 18.48 ?  19  LYS   A HG3  1 
ATOM   502  H  HD2  A LYS   A 1 19  ? 11.142 -5.889  14.132  0.60 21.13 ?  19  LYS   A HD2  1 
ATOM   503  H  HD2  B LYS   A 1 19  ? 10.665 -5.729  13.886  0.40 19.59 ?  19  LYS   A HD2  1 
ATOM   504  H  HD3  A LYS   A 1 19  ? 11.803 -4.681  13.339  0.60 21.13 ?  19  LYS   A HD3  1 
ATOM   505  H  HD3  B LYS   A 1 19  ? 11.271 -4.461  13.141  0.40 19.59 ?  19  LYS   A HD3  1 
ATOM   506  H  HE2  A LYS   A 1 19  ? 10.274 -3.210  14.226  0.60 21.50 ?  19  LYS   A HE2  1 
ATOM   507  H  HE2  B LYS   A 1 19  ? 9.374  -3.224  13.834  0.40 20.25 ?  19  LYS   A HE2  1 
ATOM   508  H  HE3  A LYS   A 1 19  ? 9.494  -4.405  14.933  0.60 21.50 ?  19  LYS   A HE3  1 
ATOM   509  H  HE3  B LYS   A 1 19  ? 8.925  -4.482  14.702  0.40 20.25 ?  19  LYS   A HE3  1 
ATOM   510  H  HZ1  A LYS   A 1 19  ? 10.902 -3.298  16.386  0.60 21.56 ?  19  LYS   A HZ1  1 
ATOM   511  H  HZ1  B LYS   A 1 19  ? 10.075 -2.996  15.991  0.40 20.17 ?  19  LYS   A HZ1  1 
ATOM   512  H  HZ2  A LYS   A 1 19  ? 11.257 -4.700  16.302  0.60 21.56 ?  19  LYS   A HZ2  1 
ATOM   513  H  HZ2  B LYS   A 1 19  ? 10.833 -4.229  15.924  0.40 20.17 ?  19  LYS   A HZ2  1 
ATOM   514  H  HZ3  A LYS   A 1 19  ? 12.053 -3.709  15.609  0.60 21.56 ?  19  LYS   A HZ3  1 
ATOM   515  H  HZ3  B LYS   A 1 19  ? 11.241 -3.085  15.135  0.40 20.17 ?  19  LYS   A HZ3  1 
ATOM   516  N  N    A ASN   A 1 20  ? 8.603  -4.722  9.576   0.60 15.83 ?  20  ASN   A N    1 
ATOM   517  N  N    B ASN   A 1 20  ? 8.467  -4.784  9.136   0.40 14.20 ?  20  ASN   A N    1 
ATOM   518  C  CA   A ASN   A 1 20  ? 8.380  -3.384  9.034   0.60 16.30 ?  20  ASN   A CA   1 
ATOM   519  C  CA   B ASN   A 1 20  ? 8.202  -3.498  8.489   0.40 14.64 ?  20  ASN   A CA   1 
ATOM   520  C  C    A ASN   A 1 20  ? 9.008  -2.391  9.999   0.60 16.20 ?  20  ASN   A C    1 
ATOM   521  C  C    B ASN   A 1 20  ? 8.800  -2.415  9.373   0.40 14.98 ?  20  ASN   A C    1 
ATOM   522  O  O    A ASN   A 1 20  ? 8.500  -2.183  11.105  0.60 16.74 ?  20  ASN   A O    1 
ATOM   523  O  O    B ASN   A 1 20  ? 8.187  -1.995  10.359  0.40 15.93 ?  20  ASN   A O    1 
ATOM   524  C  CB   A ASN   A 1 20  ? 6.888  -3.118  8.844   0.60 17.36 ?  20  ASN   A CB   1 
ATOM   525  C  CB   B ASN   A 1 20  ? 6.703  -3.269  8.333   0.40 15.05 ?  20  ASN   A CB   1 
ATOM   526  C  CG   A ASN   A 1 20  ? 6.571  -1.656  8.542   0.60 18.32 ?  20  ASN   A CG   1 
ATOM   527  C  CG   B ASN   A 1 20  ? 6.369  -1.878  7.822   0.40 15.40 ?  20  ASN   A CG   1 
ATOM   528  O  OD1  A ASN   A 1 20  ? 5.641  -1.092  9.121   0.60 19.99 ?  20  ASN   A OD1  1 
ATOM   529  O  OD1  B ASN   A 1 20  ? 5.419  -1.241  8.289   0.40 16.70 ?  20  ASN   A OD1  1 
ATOM   530  N  ND2  A ASN   A 1 20  ? 7.336  -1.042  7.637   0.60 17.95 ?  20  ASN   A ND2  1 
ATOM   531  N  ND2  B ASN   A 1 20  ? 7.142  -1.405  6.851   0.40 15.86 ?  20  ASN   A ND2  1 
ATOM   532  H  H    A ASN   A 1 20  ? 7.915  -5.063  9.962   0.60 19.16 ?  20  ASN   A H    1 
ATOM   533  H  H    B ASN   A 1 20  ? 7.801  -5.105  9.577   0.40 17.20 ?  20  ASN   A H    1 
ATOM   534  H  HA   A ASN   A 1 20  ? 8.821  -3.302  8.179   0.60 19.72 ?  20  ASN   A HA   1 
ATOM   535  H  HA   B ASN   A 1 20  ? 8.627  -3.476  7.615   0.40 17.73 ?  20  ASN   A HA   1 
ATOM   536  H  HB2  A ASN   A 1 20  ? 6.568  -3.653  8.100   0.60 20.99 ?  20  ASN   A HB2  1 
ATOM   537  H  HB2  B ASN   A 1 20  ? 6.345  -3.880  7.692   0.40 18.22 ?  20  ASN   A HB2  1 
ATOM   538  H  HB3  A ASN   A 1 20  ? 6.415  -3.356  9.653   0.60 20.99 ?  20  ASN   A HB3  1 
ATOM   539  H  HB3  B ASN   A 1 20  ? 6.271  -3.407  9.191   0.40 18.22 ?  20  ASN   A HB3  1 
ATOM   540  H  HD21 A ASN   A 1 20  ? 7.186  -0.221  7.428   0.60 21.70 ?  20  ASN   A HD21 1 
ATOM   541  H  HD21 B ASN   A 1 20  ? 6.988  -0.627  6.534   0.40 19.20 ?  20  ASN   A HD21 1 
ATOM   542  H  HD22 A ASN   A 1 20  ? 7.981  -1.469  7.259   0.60 21.70 ?  20  ASN   A HD22 1 
ATOM   543  H  HD22 B ASN   A 1 20  ? 7.790  -1.882  6.542   0.40 19.20 ?  20  ASN   A HD22 1 
ATOM   544  N  N    A ALA   A 1 21  ? 10.133 -1.802  9.601   0.60 16.49 ?  21  ALA   A N    1 
ATOM   545  N  N    B ALA   A 1 21  ? 9.996  -1.950  9.025   0.40 14.83 ?  21  ALA   A N    1 
ATOM   546  C  CA   A ALA   A 1 21  ? 10.841 -0.909  10.502  0.60 16.56 ?  21  ALA   A CA   1 
ATOM   547  C  CA   B ALA   A 1 21  ? 10.679 -0.978  9.865   0.40 14.73 ?  21  ALA   A CA   1 
ATOM   548  C  C    A ALA   A 1 21  ? 11.808 -0.052  9.707   0.60 16.18 ?  21  ALA   A C    1 
ATOM   549  C  C    B ALA   A 1 21  ? 11.733 -0.241  9.054   0.40 13.83 ?  21  ALA   A C    1 
ATOM   550  O  O    A ALA   A 1 21  ? 12.289 -0.455  8.645   0.60 16.35 ?  21  ALA   A O    1 
ATOM   551  O  O    B ALA   A 1 21  ? 12.179 -0.708  8.002   0.40 13.75 ?  21  ALA   A O    1 
ATOM   552  C  CB   A ALA   A 1 21  ? 11.597 -1.697  11.574  0.60 17.79 ?  21  ALA   A CB   1 
ATOM   553  C  CB   B ALA   A 1 21  ? 11.329 -1.642  11.083  0.40 15.57 ?  21  ALA   A CB   1 
ATOM   554  H  H    A ALA   A 1 21  ? 10.503 -1.899  8.827   0.60 19.96 ?  21  ALA   A H    1 
ATOM   555  H  H    B ALA   A 1 21  ? 10.418 -2.180  8.312   0.40 17.96 ?  21  ALA   A H    1 
ATOM   556  H  HA   A ALA   A 1 21  ? 10.208 -0.317  10.938  0.60 20.03 ?  21  ALA   A HA   1 
ATOM   557  H  HA   B ALA   A 1 21  ? 10.025 -0.338  10.184  0.40 17.85 ?  21  ALA   A HA   1 
ATOM   558  H  HB1  A ALA   A 1 21  ? 11.955 -1.073  12.218  0.60 21.51 ?  21  ALA   A HB1  1 
ATOM   559  H  HB1  B ALA   A 1 21  ? 11.769 -0.959  11.613  0.40 18.85 ?  21  ALA   A HB1  1 
ATOM   560  H  HB2  A ALA   A 1 21  ? 10.971 -2.300  12.007  0.60 21.51 ?  21  ALA   A HB2  1 
ATOM   561  H  HB2  B ALA   A 1 21  ? 10.642 -2.080  11.613  0.40 18.85 ?  21  ALA   A HB2  1 
ATOM   562  H  HB3  A ALA   A 1 21  ? 12.306 -2.202  11.152  0.60 21.51 ?  21  ALA   A HB3  1 
ATOM   563  H  HB3  B ALA   A 1 21  ? 11.977 -2.296  10.779  0.40 18.85 ?  21  ALA   A HB3  1 
ATOM   564  N  N    A ASP   A 1 22  ? 12.057 1.145   10.230  0.60 16.05 ?  22  ASP   A N    1 
ATOM   565  N  N    B ASP   A 1 22  ? 12.112 0.927   9.570   0.40 13.59 ?  22  ASP   A N    1 
ATOM   566  C  CA   A ASP   A 1 22  ? 13.099 2.024   9.722   0.60 15.91 ?  22  ASP   A CA   1 
ATOM   567  C  CA   B ASP   A 1 22  ? 13.240 1.694   9.057   0.40 13.70 ?  22  ASP   A CA   1 
ATOM   568  C  C    A ASP   A 1 22  ? 14.433 1.531   10.268  0.60 15.03 ?  22  ASP   A C    1 
ATOM   569  C  C    B ASP   A 1 22  ? 14.511 1.149   9.701   0.40 12.77 ?  22  ASP   A C    1 
ATOM   570  O  O    A ASP   A 1 22  ? 14.649 1.541   11.485  0.60 15.71 ?  22  ASP   A O    1 
ATOM   571  O  O    B ASP   A 1 22  ? 14.616 1.106   10.931  0.40 12.83 ?  22  ASP   A O    1 
ATOM   572  C  CB   A ASP   A 1 22  ? 12.815 3.448   10.195  0.60 17.64 ?  22  ASP   A CB   1 
ATOM   573  C  CB   B ASP   A 1 22  ? 13.044 3.163   9.433   0.40 14.77 ?  22  ASP   A CB   1 
ATOM   574  C  CG   A ASP   A 1 22  ? 13.824 4.458   9.679   0.60 19.22 ?  22  ASP   A CG   1 
ATOM   575  C  CG   B ASP   A 1 22  ? 14.051 4.089   8.772   0.40 15.51 ?  22  ASP   A CG   1 
ATOM   576  O  OD1  A ASP   A 1 22  ? 14.871 4.066   9.129   0.60 19.32 ?  22  ASP   A OD1  1 
ATOM   577  O  OD1  B ASP   A 1 22  ? 15.168 3.633   8.440   0.40 14.57 ?  22  ASP   A OD1  1 
ATOM   578  O  OD2  A ASP   A 1 22  ? 13.563 5.667   9.831   0.60 20.79 -1 22  ASP   A OD2  1 
ATOM   579  O  OD2  B ASP   A 1 22  ? 13.726 5.283   8.594   0.40 16.89 -1 22  ASP   A OD2  1 
ATOM   580  H  H    A ASP   A 1 22  ? 11.615 1.483   10.886  0.60 19.42 ?  22  ASP   A H    1 
ATOM   581  H  H    B ASP   A 1 22  ? 11.712 1.302   10.235  0.40 16.48 ?  22  ASP   A H    1 
ATOM   582  H  HA   A ASP   A 1 22  ? 13.118 2.006   8.749   0.60 19.26 ?  22  ASP   A HA   1 
ATOM   583  H  HA   B ASP   A 1 22  ? 13.293 1.604   8.090   0.40 16.60 ?  22  ASP   A HA   1 
ATOM   584  H  HB2  A ASP   A 1 22  ? 11.928 3.712   9.897   0.60 21.34 ?  22  ASP   A HB2  1 
ATOM   585  H  HB2  B ASP   A 1 22  ? 12.154 3.438   9.170   0.40 17.89 ?  22  ASP   A HB2  1 
ATOM   586  H  HB3  A ASP   A 1 22  ? 12.854 3.472   11.165  0.60 21.34 ?  22  ASP   A HB3  1 
ATOM   587  H  HB3  B ASP   A 1 22  ? 13.149 3.252   10.394  0.40 17.89 ?  22  ASP   A HB3  1 
ATOM   588  N  N    A ILE   A 1 23  ? 15.316 1.079   9.372   0.60 14.63 ?  23  ILE   A N    1 
ATOM   589  N  N    B ILE   A 1 23  ? 15.469 0.714   8.875   0.40 12.31 ?  23  ILE   A N    1 
ATOM   590  C  CA   A ILE   A 1 23  ? 16.585 0.488   9.793   0.60 13.85 ?  23  ILE   A CA   1 
ATOM   591  C  CA   B ILE   A 1 23  ? 16.700 0.122   9.394   0.40 11.99 ?  23  ILE   A CA   1 
ATOM   592  C  C    A ILE   A 1 23  ? 17.389 1.460   10.646  0.60 14.02 ?  23  ILE   A C    1 
ATOM   593  C  C    B ILE   A 1 23  ? 17.422 1.089   10.318  0.40 12.52 ?  23  ILE   A C    1 
ATOM   594  O  O    A ILE   A 1 23  ? 18.125 1.044   11.549  0.60 14.57 ?  23  ILE   A O    1 
ATOM   595  O  O    B ILE   A 1 23  ? 18.100 0.668   11.263  0.40 12.65 ?  23  ILE   A O    1 
ATOM   596  C  CB   A ILE   A 1 23  ? 17.376 -0.015  8.565   0.60 13.45 ?  23  ILE   A CB   1 
ATOM   597  C  CB   B ILE   A 1 23  ? 17.618 -0.374  8.254   0.40 11.53 ?  23  ILE   A CB   1 
ATOM   598  C  CG1  A ILE   A 1 23  ? 18.572 -0.870  9.002   0.60 13.92 ?  23  ILE   A CG1  1 
ATOM   599  C  CG1  B ILE   A 1 23  ? 18.665 -1.337  8.822   0.40 11.60 ?  23  ILE   A CG1  1 
ATOM   600  C  CG2  A ILE   A 1 23  ? 17.804 1.154   7.675   0.60 13.50 ?  23  ILE   A CG2  1 
ATOM   601  C  CG2  B ILE   A 1 23  ? 18.292 0.797   7.534   0.40 11.15 ?  23  ILE   A CG2  1 
ATOM   602  C  CD1  A ILE   A 1 23  ? 19.258 -1.593  7.858   0.60 14.20 ?  23  ILE   A CD1  1 
ATOM   603  C  CD1  B ILE   A 1 23  ? 19.563 -1.969  7.780   0.40 11.41 ?  23  ILE   A CD1  1 
ATOM   604  H  H    A ILE   A 1 23  ? 15.200 1.102   8.523   0.60 17.72 ?  23  ILE   A H    1 
ATOM   605  H  H    B ILE   A 1 23  ? 15.431 0.744   8.032   0.40 14.93 ?  23  ILE   A H    1 
ATOM   606  H  HA   A ILE   A 1 23  ? 16.392 -0.288  10.341  0.60 16.78 ?  23  ILE   A HA   1 
ATOM   607  H  HA   B ILE   A 1 23  ? 16.455 -0.657  9.916   0.40 14.55 ?  23  ILE   A HA   1 
ATOM   608  H  HB   A ILE   A 1 23  ? 16.787 -0.580  8.043   0.60 16.30 ?  23  ILE   A HB   1 
ATOM   609  H  HB   B ILE   A 1 23  ? 17.080 -0.861  7.610   0.40 14.00 ?  23  ILE   A HB   1 
ATOM   610  H  HG12 A ILE   A 1 23  ? 19.230 -0.300  9.427   0.60 16.87 ?  23  ILE   A HG12 1 
ATOM   611  H  HG12 B ILE   A 1 23  ? 19.232 -0.854  9.443   0.40 14.08 ?  23  ILE   A HG12 1 
ATOM   612  H  HG13 A ILE   A 1 23  ? 18.263 -1.542  9.630   0.60 16.87 ?  23  ILE   A HG13 1 
ATOM   613  H  HG13 B ILE   A 1 23  ? 18.209 -2.056  9.289   0.40 14.08 ?  23  ILE   A HG13 1 
ATOM   614  H  HG21 A ILE   A 1 23  ? 18.172 0.806   6.847   0.60 16.37 ?  23  ILE   A HG21 1 
ATOM   615  H  HG21 B ILE   A 1 23  ? 18.684 0.474   6.704   0.40 13.54 ?  23  ILE   A HG21 1 
ATOM   616  H  HG22 A ILE   A 1 23  ? 17.025 1.703   7.479   0.60 16.37 ?  23  ILE   A HG22 1 
ATOM   617  H  HG22 B ILE   A 1 23  ? 17.628 1.474   7.345   0.40 13.54 ?  23  ILE   A HG22 1 
ATOM   618  H  HG23 A ILE   A 1 23  ? 18.470 1.683   8.137   0.60 16.37 ?  23  ILE   A HG23 1 
ATOM   619  H  HG23 B ILE   A 1 23  ? 18.988 1.162   8.103   0.40 13.54 ?  23  ILE   A HG23 1 
ATOM   620  H  HD11 A ILE   A 1 23  ? 19.959 -2.158  8.217   0.60 17.21 ?  23  ILE   A HD11 1 
ATOM   621  H  HD11 B ILE   A 1 23  ? 20.119 -2.641  8.210   0.40 13.86 ?  23  ILE   A HD11 1 
ATOM   622  H  HD12 A ILE   A 1 23  ? 18.602 -2.133  7.390   0.60 17.21 ?  23  ILE   A HD12 1 
ATOM   623  H  HD12 B ILE   A 1 23  ? 19.012 -2.383  7.100   0.40 13.86 ?  23  ILE   A HD12 1 
ATOM   624  H  HD13 A ILE   A 1 23  ? 19.637 -0.936  7.253   0.60 17.21 ?  23  ILE   A HD13 1 
ATOM   625  H  HD13 B ILE   A 1 23  ? 20.121 -1.282  7.387   0.40 13.86 ?  23  ILE   A HD13 1 
ATOM   626  N  N    A VAL   A 1 24  ? 17.260 2.761   10.385  0.60 14.18 ?  24  VAL   A N    1 
ATOM   627  N  N    B VAL   A 1 24  ? 17.292 2.392   10.069  0.40 13.60 ?  24  VAL   A N    1 
ATOM   628  C  CA   A VAL   A 1 24  ? 17.930 3.758   11.216  0.60 15.58 ?  24  VAL   A CA   1 
ATOM   629  C  CA   B VAL   A 1 24  ? 17.936 3.378   10.928  0.40 14.62 ?  24  VAL   A CA   1 
ATOM   630  C  C    A VAL   A 1 24  ? 17.433 3.669   12.651  0.60 16.33 ?  24  VAL   A C    1 
ATOM   631  C  C    B VAL   A 1 24  ? 17.330 3.341   12.324  0.40 15.55 ?  24  VAL   A C    1 
ATOM   632  O  O    A VAL   A 1 24  ? 18.223 3.590   13.601  0.60 16.60 ?  24  VAL   A O    1 
ATOM   633  O  O    B VAL   A 1 24  ? 18.048 3.387   13.329  0.40 16.05 ?  24  VAL   A O    1 
ATOM   634  C  CB   A VAL   A 1 24  ? 17.714 5.165   10.635  0.60 16.35 ?  24  VAL   A CB   1 
ATOM   635  C  CB   B VAL   A 1 24  ? 17.848 4.774   10.288  0.40 15.05 ?  24  VAL   A CB   1 
ATOM   636  C  CG1  A VAL   A 1 24  ? 18.186 6.231   11.617  0.60 16.87 ?  24  VAL   A CG1  1 
ATOM   637  C  CG1  B VAL   A 1 24  ? 18.513 5.809   11.174  0.40 16.11 ?  24  VAL   A CG1  1 
ATOM   638  C  CG2  A VAL   A 1 24  ? 18.425 5.303   9.299   0.60 16.89 ?  24  VAL   A CG2  1 
ATOM   639  C  CG2  B VAL   A 1 24  ? 18.483 4.753   8.908   0.40 14.97 ?  24  VAL   A CG2  1 
ATOM   640  H  H    A VAL   A 1 24  ? 16.800 3.085   9.739   0.60 17.18 ?  24  VAL   A H    1 
ATOM   641  H  H    B VAL   A 1 24  ? 16.835 2.724   9.424   0.40 16.49 ?  24  VAL   A H    1 
ATOM   642  H  HA   A VAL   A 1 24  ? 18.883 3.580   11.219  0.60 18.86 ?  24  VAL   A HA   1 
ATOM   643  H  HA   B VAL   A 1 24  ? 18.872 3.150   11.014  0.40 17.70 ?  24  VAL   A HA   1 
ATOM   644  H  HB   A VAL   A 1 24  ? 16.765 5.300   10.481  0.60 19.78 ?  24  VAL   A HB   1 
ATOM   645  H  HB   B VAL   A 1 24  ? 16.914 5.018   10.187  0.40 18.22 ?  24  VAL   A HB   1 
ATOM   646  H  HG11 A VAL   A 1 24  ? 18.308 7.065   11.138  0.60 20.41 ?  24  VAL   A HG11 1 
ATOM   647  H  HG11 B VAL   A 1 24  ? 18.641 6.625   10.667  0.40 19.50 ?  24  VAL   A HG11 1 
ATOM   648  H  HG12 A VAL   A 1 24  ? 17.518 6.343   12.310  0.60 20.41 ?  24  VAL   A HG12 1 
ATOM   649  H  HG12 B VAL   A 1 24  ? 17.935 5.980   11.933  0.40 19.50 ?  24  VAL   A HG12 1 
ATOM   650  H  HG13 A VAL   A 1 24  ? 19.028 5.948   12.006  0.60 20.41 ?  24  VAL   A HG13 1 
ATOM   651  H  HG13 B VAL   A 1 24  ? 19.368 5.467   11.476  0.40 19.50 ?  24  VAL   A HG13 1 
ATOM   652  H  HG21 A VAL   A 1 24  ? 18.181 6.152   8.898   0.60 20.43 ?  24  VAL   A HG21 1 
ATOM   653  H  HG21 B VAL   A 1 24  ? 18.585 5.663   8.595   0.40 18.13 ?  24  VAL   A HG21 1 
ATOM   654  H  HG22 A VAL   A 1 24  ? 19.383 5.271   9.447   0.60 20.43 ?  24  VAL   A HG22 1 
ATOM   655  H  HG22 B VAL   A 1 24  ? 19.351 4.324   8.969   0.40 18.13 ?  24  VAL   A HG22 1 
ATOM   656  H  HG23 A VAL   A 1 24  ? 18.154 4.575   8.718   0.60 20.43 ?  24  VAL   A HG23 1 
ATOM   657  H  HG23 B VAL   A 1 24  ? 17.911 4.254   8.304   0.40 18.13 ?  24  VAL   A HG23 1 
ATOM   658  N  N    A GLU   A 1 25  ? 16.110 3.693   12.828  0.60 17.12 ?  25  GLU   A N    1 
ATOM   659  N  N    B GLU   A 1 25  ? 16.003 3.228   12.410  0.40 16.27 ?  25  GLU   A N    1 
ATOM   660  C  CA   A GLU   A 1 25  ? 15.539 3.621   14.167  0.60 18.54 ?  25  GLU   A CA   1 
ATOM   661  C  CA   B GLU   A 1 25  ? 15.351 3.160   13.714  0.40 17.26 ?  25  GLU   A CA   1 
ATOM   662  C  C    A GLU   A 1 25  ? 15.775 2.258   14.800  0.60 17.83 ?  25  GLU   A C    1 
ATOM   663  C  C    B GLU   A 1 25  ? 15.652 1.839   14.416  0.40 17.31 ?  25  GLU   A C    1 
ATOM   664  O  O    A GLU   A 1 25  ? 15.995 2.170   16.014  0.60 18.92 ?  25  GLU   A O    1 
ATOM   665  O  O    B GLU   A 1 25  ? 15.903 1.820   15.626  0.40 17.58 ?  25  GLU   A O    1 
ATOM   666  C  CB   A GLU   A 1 25  ? 14.047 3.962   14.117  0.60 20.79 ?  25  GLU   A CB   1 
ATOM   667  C  CB   B GLU   A 1 25  ? 13.846 3.394   13.562  0.40 18.44 ?  25  GLU   A CB   1 
ATOM   668  C  CG   A GLU   A 1 25  ? 13.777 5.411   13.733  0.60 23.31 ?  25  GLU   A CG   1 
ATOM   669  C  CG   B GLU   A 1 25  ? 13.505 4.756   12.973  0.40 20.65 ?  25  GLU   A CG   1 
ATOM   670  C  CD   A GLU   A 1 25  ? 14.555 6.401   14.585  0.60 25.39 ?  25  GLU   A CD   1 
ATOM   671  C  CD   B GLU   A 1 25  ? 14.018 5.895   13.828  0.40 22.62 ?  25  GLU   A CD   1 
ATOM   672  O  OE1  A GLU   A 1 25  ? 14.628 6.204   15.817  0.60 26.02 ?  25  GLU   A OE1  1 
ATOM   673  O  OE1  B GLU   A 1 25  ? 14.023 5.744   15.068  0.40 23.68 ?  25  GLU   A OE1  1 
ATOM   674  O  OE2  A GLU   A 1 25  ? 15.110 7.365   14.018  0.60 26.43 -1 25  GLU   A OE2  1 
ATOM   675  O  OE2  B GLU   A 1 25  ? 14.421 6.932   13.262  0.40 23.44 -1 25  GLU   A OE2  1 
ATOM   676  H  H    A GLU   A 1 25  ? 15.529 3.752   12.193  0.60 20.71 ?  25  GLU   A H    1 
ATOM   677  H  H    B GLU   A 1 25  ? 15.467 3.182   11.739  0.40 19.68 ?  25  GLU   A H    1 
ATOM   678  H  HA   A GLU   A 1 25  ? 15.973 4.278   14.730  0.60 22.42 ?  25  GLU   A HA   1 
ATOM   679  H  HA   B GLU   A 1 25  ? 15.702 3.867   14.272  0.40 20.88 ?  25  GLU   A HA   1 
ATOM   680  H  HB2  A GLU   A 1 25  ? 13.609 3.398   13.454  0.60 25.11 ?  25  GLU   A HB2  1 
ATOM   681  H  HB2  B GLU   A 1 25  ? 13.476 2.719   12.974  0.40 22.29 ?  25  GLU   A HB2  1 
ATOM   682  H  HB3  A GLU   A 1 25  ? 13.648 3.809   14.988  0.60 25.11 ?  25  GLU   A HB3  1 
ATOM   683  H  HB3  B GLU   A 1 25  ? 13.427 3.338   14.436  0.40 22.29 ?  25  GLU   A HB3  1 
ATOM   684  H  HG2  A GLU   A 1 25  ? 14.046 5.547   12.814  0.60 28.14 ?  25  GLU   A HG2  1 
ATOM   685  H  HG2  B GLU   A 1 25  ? 13.908 4.834   12.093  0.40 24.95 ?  25  GLU   A HG2  1 
ATOM   686  H  HG3  A GLU   A 1 25  ? 12.829 5.594   13.837  0.60 28.14 ?  25  GLU   A HG3  1 
ATOM   687  H  HG3  B GLU   A 1 25  ? 12.542 4.846   12.906  0.40 24.95 ?  25  GLU   A HG3  1 
ATOM   688  N  N    A GLU   A 1 26  ? 15.750 1.190   13.999  0.60 17.50 ?  26  GLU   A N    1 
ATOM   689  N  N    B GLU   A 1 26  ? 15.645 0.726   13.678  0.40 17.17 ?  26  GLU   A N    1 
ATOM   690  C  CA   A GLU   A 1 26  ? 16.040 -0.141  14.525  0.60 17.38 ?  26  GLU   A CA   1 
ATOM   691  C  CA   B GLU   A 1 26  ? 16.055 -0.546  14.269  0.40 17.03 ?  26  GLU   A CA   1 
ATOM   692  C  C    A GLU   A 1 26  ? 17.465 -0.221  15.059  0.60 16.29 ?  26  GLU   A C    1 
ATOM   693  C  C    B GLU   A 1 26  ? 17.479 -0.460  14.800  0.40 16.11 ?  26  GLU   A C    1 
ATOM   694  O  O    A GLU   A 1 26  ? 17.696 -0.686  16.180  0.60 16.09 ?  26  GLU   A O    1 
ATOM   695  O  O    B GLU   A 1 26  ? 17.802 -1.049  15.838  0.40 15.77 ?  26  GLU   A O    1 
ATOM   696  C  CB   A GLU   A 1 26  ? 15.836 -1.194  13.435  0.60 18.88 ?  26  GLU   A CB   1 
ATOM   697  C  CB   B GLU   A 1 26  ? 15.941 -1.674  13.240  0.40 17.98 ?  26  GLU   A CB   1 
ATOM   698  C  CG   A GLU   A 1 26  ? 14.451 -1.803  13.370  0.60 21.00 ?  26  GLU   A CG   1 
ATOM   699  C  CG   B GLU   A 1 26  ? 14.522 -2.039  12.858  0.40 18.30 ?  26  GLU   A CG   1 
ATOM   700  C  CD   A GLU   A 1 26  ? 14.087 -2.584  14.625  0.60 21.98 ?  26  GLU   A CD   1 
ATOM   701  C  CD   B GLU   A 1 26  ? 13.770 -2.688  14.000  0.40 18.14 ?  26  GLU   A CD   1 
ATOM   702  O  OE1  A GLU   A 1 26  ? 14.631 -3.689  14.846  0.60 22.23 ?  26  GLU   A OE1  1 
ATOM   703  O  OE1  B GLU   A 1 26  ? 14.148 -3.806  14.422  0.40 18.87 ?  26  GLU   A OE1  1 
ATOM   704  O  OE2  A GLU   A 1 26  ? 13.259 -2.077  15.401  0.60 23.11 -1 26  GLU   A OE2  1 
ATOM   705  O  OE2  B GLU   A 1 26  ? 12.798 -2.073  14.479  0.40 16.98 -1 26  GLU   A OE2  1 
ATOM   706  H  H    A GLU   A 1 26  ? 15.571 1.220   13.158  0.60 21.17 ?  26  GLU   A H    1 
ATOM   707  H  H    B GLU   A 1 26  ? 15.413 0.679   12.853  0.40 20.77 ?  26  GLU   A H    1 
ATOM   708  H  HA   A GLU   A 1 26  ? 15.432 -0.331  15.253  0.60 21.02 ?  26  GLU   A HA   1 
ATOM   709  H  HA   B GLU   A 1 26  ? 15.472 -0.758  15.014  0.40 20.60 ?  26  GLU   A HA   1 
ATOM   710  H  HB2  A GLU   A 1 26  ? 16.019 -0.784  12.574  0.60 22.82 ?  26  GLU   A HB2  1 
ATOM   711  H  HB2  B GLU   A 1 26  ? 16.403 -1.406  12.432  0.40 21.74 ?  26  GLU   A HB2  1 
ATOM   712  H  HB3  A GLU   A 1 26  ? 16.467 -1.914  13.589  0.60 22.82 ?  26  GLU   A HB3  1 
ATOM   713  H  HB3  B GLU   A 1 26  ? 16.359 -2.472  13.605  0.40 21.74 ?  26  GLU   A HB3  1 
ATOM   714  H  HG2  A GLU   A 1 26  ? 13.811 -1.086  13.263  0.60 25.36 ?  26  GLU   A HG2  1 
ATOM   715  H  HG2  B GLU   A 1 26  ? 14.047 -1.233  12.592  0.40 22.12 ?  26  GLU   A HG2  1 
ATOM   716  H  HG3  A GLU   A 1 26  ? 14.408 -2.402  12.605  0.60 25.36 ?  26  GLU   A HG3  1 
ATOM   717  H  HG3  B GLU   A 1 26  ? 14.539 -2.670  12.123  0.40 22.12 ?  26  GLU   A HG3  1 
ATOM   718  N  N    A ALA   A 1 27  ? 18.442 0.212   14.257  0.60 15.46 ?  27  ALA   A N    1 
ATOM   719  N  N    B ALA   A 1 27  ? 18.345 0.279   14.106  0.40 15.49 ?  27  ALA   A N    1 
ATOM   720  C  CA   A ALA   A 1 27  ? 19.836 0.128   14.686  0.60 14.97 ?  27  ALA   A CA   1 
ATOM   721  C  CA   B ALA   A 1 27  ? 19.726 0.413   14.558  0.40 15.59 ?  27  ALA   A CA   1 
ATOM   722  C  C    A ALA   A 1 27  ? 20.072 0.937   15.956  0.60 16.41 ?  27  ALA   A C    1 
ATOM   723  C  C    B ALA   A 1 27  ? 19.805 1.217   15.850  0.40 16.64 ?  27  ALA   A C    1 
ATOM   724  O  O    A ALA   A 1 27  ? 20.762 0.479   16.875  0.60 16.91 ?  27  ALA   A O    1 
ATOM   725  O  O    B ALA   A 1 27  ? 20.443 0.793   16.821  0.40 16.35 ?  27  ALA   A O    1 
ATOM   726  C  CB   A ALA   A 1 27  ? 20.768 0.596   13.564  0.60 14.13 ?  27  ALA   A CB   1 
ATOM   727  C  CB   B ALA   A 1 27  ? 20.572 1.063   13.462  0.40 15.05 ?  27  ALA   A CB   1 
ATOM   728  H  H    A ALA   A 1 27  ? 18.326 0.552   13.475  0.60 18.71 ?  27  ALA   A H    1 
ATOM   729  H  H    B ALA   A 1 27  ? 18.156 0.709   13.384  0.40 18.75 ?  27  ALA   A H    1 
ATOM   730  H  HA   A ALA   A 1 27  ? 20.047 -0.799  14.877  0.60 18.13 ?  27  ALA   A HA   1 
ATOM   731  H  HA   B ALA   A 1 27  ? 20.086 -0.468  14.728  0.40 18.88 ?  27  ALA   A HA   1 
ATOM   732  H  HB1  A ALA   A 1 27  ? 21.689 0.527   13.869  0.60 17.12 ?  27  ALA   A HB1  1 
ATOM   733  H  HB1  B ALA   A 1 27  ? 21.490 1.122   13.769  0.40 18.22 ?  27  ALA   A HB1  1 
ATOM   734  H  HB2  A ALA   A 1 27  ? 20.639 0.026   12.787  0.60 17.12 ?  27  ALA   A HB2  1 
ATOM   735  H  HB2  B ALA   A 1 27  ? 20.525 0.520   12.660  0.40 18.22 ?  27  ALA   A HB2  1 
ATOM   736  H  HB3  A ALA   A 1 27  ? 20.562 1.514   13.340  0.60 17.12 ?  27  ALA   A HB3  1 
ATOM   737  H  HB3  B ALA   A 1 27  ? 20.226 1.953   13.279  0.40 18.22 ?  27  ALA   A HB3  1 
ATOM   738  N  N    A LYS   A 1 28  ? 19.495 2.137   16.035  0.60 18.25 ?  28  LYS   A N    1 
ATOM   739  N  N    B LYS   A 1 28  ? 19.146 2.378   15.888  0.40 18.36 ?  28  LYS   A N    1 
ATOM   740  C  CA   A LYS   A 1 28  ? 19.648 2.946   17.241  0.60 20.90 ?  28  LYS   A CA   1 
ATOM   741  C  CA   B LYS   A 1 28  ? 19.243 3.246   17.058  0.40 20.49 ?  28  LYS   A CA   1 
ATOM   742  C  C    A LYS   A 1 28  ? 19.093 2.225   18.464  0.60 21.99 ?  28  LYS   A C    1 
ATOM   743  C  C    B LYS   A 1 28  ? 18.738 2.563   18.323  0.40 21.96 ?  28  LYS   A C    1 
ATOM   744  O  O    A LYS   A 1 28  ? 19.679 2.293   19.551  0.60 23.24 ?  28  LYS   A O    1 
ATOM   745  O  O    B LYS   A 1 28  ? 19.191 2.892   19.425  0.40 22.57 ?  28  LYS   A O    1 
ATOM   746  C  CB   A LYS   A 1 28  ? 18.972 4.305   17.057  0.60 22.51 ?  28  LYS   A CB   1 
ATOM   747  C  CB   B LYS   A 1 28  ? 18.471 4.544   16.816  0.40 21.56 ?  28  LYS   A CB   1 
ATOM   748  C  CG   A LYS   A 1 28  ? 19.769 5.272   16.196  0.60 23.95 ?  28  LYS   A CG   1 
ATOM   749  C  CG   B LYS   A 1 28  ? 19.007 5.386   15.674  0.40 22.65 ?  28  LYS   A CG   1 
ATOM   750  C  CD   A LYS   A 1 28  ? 19.228 6.690   16.276  0.60 25.90 ?  28  LYS   A CD   1 
ATOM   751  C  CD   B LYS   A 1 28  ? 18.348 6.756   15.651  0.40 24.09 ?  28  LYS   A CD   1 
ATOM   752  C  CE   A LYS   A 1 28  ? 17.916 6.832   15.528  0.60 27.30 ?  28  LYS   A CE   1 
ATOM   753  C  CE   B LYS   A 1 28  ? 18.767 7.558   14.429  0.40 25.27 ?  28  LYS   A CE   1 
ATOM   754  N  NZ   A LYS   A 1 28  ? 17.459 8.249   15.498  0.60 28.13 ?  28  LYS   A NZ   1 
ATOM   755  N  NZ   B LYS   A 1 28  ? 18.306 8.973   14.501  0.40 25.93 ?  28  LYS   A NZ   1 
ATOM   756  H  H    A LYS   A 1 28  ? 19.026 2.495   15.416  0.60 22.07 ?  28  LYS   A H    1 
ATOM   757  H  H    B LYS   A 1 28  ? 18.644 2.680   15.260  0.40 22.20 ?  28  LYS   A H    1 
ATOM   758  H  HA   A LYS   A 1 28  ? 20.591 3.100   17.398  0.60 25.24 ?  28  LYS   A HA   1 
ATOM   759  H  HA   B LYS   A 1 28  ? 20.172 3.480   17.202  0.40 24.76 ?  28  LYS   A HA   1 
ATOM   760  H  HB2  A LYS   A 1 28  ? 18.112 4.173   16.632  0.60 27.18 ?  28  LYS   A HB2  1 
ATOM   761  H  HB2  B LYS   A 1 28  ? 17.548 4.328   16.610  0.40 26.04 ?  28  LYS   A HB2  1 
ATOM   762  H  HB3  A LYS   A 1 28  ? 18.852 4.715   17.927  0.60 27.18 ?  28  LYS   A HB3  1 
ATOM   763  H  HB3  B LYS   A 1 28  ? 18.509 5.088   17.618  0.40 26.04 ?  28  LYS   A HB3  1 
ATOM   764  H  HG2  A LYS   A 1 28  ? 20.690 5.284   16.499  0.60 28.91 ?  28  LYS   A HG2  1 
ATOM   765  H  HG2  B LYS   A 1 28  ? 19.962 5.509   15.784  0.40 27.34 ?  28  LYS   A HG2  1 
ATOM   766  H  HG3  A LYS   A 1 28  ? 19.725 4.985   15.271  0.60 28.91 ?  28  LYS   A HG3  1 
ATOM   767  H  HG3  B LYS   A 1 28  ? 18.823 4.948   14.829  0.40 27.34 ?  28  LYS   A HG3  1 
ATOM   768  H  HD2  A LYS   A 1 28  ? 19.074 6.923   17.205  0.60 31.24 ?  28  LYS   A HD2  1 
ATOM   769  H  HD2  B LYS   A 1 28  ? 17.384 6.648   15.629  0.40 29.07 ?  28  LYS   A HD2  1 
ATOM   770  H  HD3  A LYS   A 1 28  ? 19.870 7.301   15.880  0.60 31.24 ?  28  LYS   A HD3  1 
ATOM   771  H  HD3  B LYS   A 1 28  ? 18.612 7.250   16.443  0.40 29.07 ?  28  LYS   A HD3  1 
ATOM   772  H  HE2  A LYS   A 1 28  ? 18.036 6.531   14.614  0.60 32.93 ?  28  LYS   A HE2  1 
ATOM   773  H  HE2  B LYS   A 1 28  ? 19.734 7.554   14.360  0.40 30.49 ?  28  LYS   A HE2  1 
ATOM   774  H  HE3  A LYS   A 1 28  ? 17.236 6.302   15.971  0.60 32.93 ?  28  LYS   A HE3  1 
ATOM   775  H  HE3  B LYS   A 1 28  ? 18.374 7.156   13.639  0.40 30.49 ?  28  LYS   A HE3  1 
ATOM   776  H  HZ1  A LYS   A 1 28  ? 16.690 8.312   15.055  0.60 33.93 ?  28  LYS   A HZ1  1 
ATOM   777  H  HZ1  B LYS   A 1 28  ? 18.565 9.415   13.773  0.40 31.28 ?  28  LYS   A HZ1  1 
ATOM   778  H  HZ2  A LYS   A 1 28  ? 17.341 8.549   16.328  0.60 33.93 ?  28  LYS   A HZ2  1 
ATOM   779  H  HZ2  B LYS   A 1 28  ? 17.418 9.002   14.556  0.40 31.28 ?  28  LYS   A HZ2  1 
ATOM   780  H  HZ3  A LYS   A 1 28  ? 18.069 8.757   15.092  0.60 33.93 ?  28  LYS   A HZ3  1 
ATOM   781  H  HZ3  B LYS   A 1 28  ? 18.654 9.369   15.218  0.40 31.28 ?  28  LYS   A HZ3  1 
ATOM   782  N  N    A LYS   A 1 29  ? 17.970 1.522   18.307  0.60 22.77 ?  29  LYS   A N    1 
ATOM   783  N  N    B LYS   A 1 29  ? 17.812 1.611   18.192  0.40 23.24 ?  29  LYS   A N    1 
ATOM   784  C  CA   A LYS   A 1 29  ? 17.371 0.817   19.437  0.60 24.15 ?  29  LYS   A CA   1 
ATOM   785  C  CA   B LYS   A 1 29  ? 17.171 0.998   19.349  0.40 24.87 ?  29  LYS   A CA   1 
ATOM   786  C  C    A LYS   A 1 29  ? 18.181 -0.420  19.807  0.60 23.47 ?  29  LYS   A C    1 
ATOM   787  C  C    B LYS   A 1 29  ? 17.815 -0.312  19.783  0.40 24.52 ?  29  LYS   A C    1 
ATOM   788  O  O    A LYS   A 1 29  ? 18.539 -0.616  20.975  0.60 23.92 ?  29  LYS   A O    1 
ATOM   789  O  O    B LYS   A 1 29  ? 17.681 -0.689  20.952  0.40 25.01 ?  29  LYS   A O    1 
ATOM   790  C  CB   A LYS   A 1 29  ? 15.935 0.421   19.091  0.60 26.46 ?  29  LYS   A CB   1 
ATOM   791  C  CB   B LYS   A 1 29  ? 15.686 0.744   19.055  0.40 26.88 ?  29  LYS   A CB   1 
ATOM   792  C  CG   A LYS   A 1 29  ? 15.193 -0.300  20.211  0.60 28.98 ?  29  LYS   A CG   1 
ATOM   793  C  CG   B LYS   A 1 29  ? 14.883 0.154   20.214  0.40 28.92 ?  29  LYS   A CG   1 
ATOM   794  C  CD   A LYS   A 1 29  ? 14.801 0.657   21.326  0.60 31.57 ?  29  LYS   A CD   1 
ATOM   795  C  CD   B LYS   A 1 29  ? 14.827 1.084   21.420  0.40 30.78 ?  29  LYS   A CD   1 
ATOM   796  C  CE   A LYS   A 1 29  ? 13.908 -0.023  22.351  0.60 33.23 ?  29  LYS   A CE   1 
ATOM   797  C  CE   B LYS   A 1 29  ? 14.012 0.467   22.551  0.40 32.05 ?  29  LYS   A CE   1 
ATOM   798  N  NZ   A LYS   A 1 29  ? 13.420 0.934   23.381  0.60 34.27 ?  29  LYS   A NZ   1 
ATOM   799  N  NZ   B LYS   A 1 29  ? 13.939 1.347   23.750  0.40 32.81 ?  29  LYS   A NZ   1 
ATOM   800  H  H    A LYS   A 1 29  ? 17.541 1.437   17.565  0.60 27.49 ?  29  LYS   A H    1 
ATOM   801  H  H    B LYS   A 1 29  ? 17.543 1.301   17.436  0.40 28.05 ?  29  LYS   A H    1 
ATOM   802  H  HA   A LYS   A 1 29  ? 17.346 1.407   20.206  0.60 29.15 ?  29  LYS   A HA   1 
ATOM   803  H  HA   B LYS   A 1 29  ? 17.226 1.614   20.094  0.40 30.01 ?  29  LYS   A HA   1 
ATOM   804  H  HB2  A LYS   A 1 29  ? 15.435 1.223   18.878  0.60 31.92 ?  29  LYS   A HB2  1 
ATOM   805  H  HB2  B LYS   A 1 29  ? 15.274 1.585   18.813  0.40 32.42 ?  29  LYS   A HB2  1 
ATOM   806  H  HB3  A LYS   A 1 29  ? 15.952 -0.170  18.323  0.60 31.92 ?  29  LYS   A HB3  1 
ATOM   807  H  HB3  B LYS   A 1 29  ? 15.623 0.123   18.313  0.40 32.42 ?  29  LYS   A HB3  1 
ATOM   808  H  HG2  A LYS   A 1 29  ? 14.382 -0.693  19.853  0.60 34.94 ?  29  LYS   A HG2  1 
ATOM   809  H  HG2  B LYS   A 1 29  ? 13.971 0.000   19.917  0.40 34.87 ?  29  LYS   A HG2  1 
ATOM   810  H  HG3  A LYS   A 1 29  ? 15.758 -0.993  20.590  0.60 34.94 ?  29  LYS   A HG3  1 
ATOM   811  H  HG3  B LYS   A 1 29  ? 15.282 -0.683  20.496  0.40 34.87 ?  29  LYS   A HG3  1 
ATOM   812  H  HD2  A LYS   A 1 29  ? 15.602 0.970   21.777  0.60 38.05 ?  29  LYS   A HD2  1 
ATOM   813  H  HD2  B LYS   A 1 29  ? 15.726 1.244   21.747  0.40 37.10 ?  29  LYS   A HD2  1 
ATOM   814  H  HD3  A LYS   A 1 29  ? 14.315 1.407   20.947  0.60 38.05 ?  29  LYS   A HD3  1 
ATOM   815  H  HD3  B LYS   A 1 29  ? 14.408 1.921   21.164  0.40 37.10 ?  29  LYS   A HD3  1 
ATOM   816  H  HE2  A LYS   A 1 29  ? 13.137 -0.404  21.901  0.60 40.04 ?  29  LYS   A HE2  1 
ATOM   817  H  HE2  B LYS   A 1 29  ? 13.107 0.307   22.240  0.40 38.62 ?  29  LYS   A HE2  1 
ATOM   818  H  HE3  A LYS   A 1 29  ? 14.411 -0.721  22.800  0.60 40.04 ?  29  LYS   A HE3  1 
ATOM   819  H  HE3  B LYS   A 1 29  ? 14.424 -0.371  22.818  0.40 38.62 ?  29  LYS   A HE3  1 
ATOM   820  H  HZ1  A LYS   A 1 29  ? 12.901 0.511   23.967  0.60 41.28 ?  29  LYS   A HZ1  1 
ATOM   821  H  HZ1  B LYS   A 1 29  ? 13.255 1.103   24.265  0.40 39.53 ?  29  LYS   A HZ1  1 
ATOM   822  H  HZ2  A LYS   A 1 29  ? 14.110 1.294   23.812  0.60 41.28 ?  29  LYS   A HZ2  1 
ATOM   823  H  HZ2  B LYS   A 1 29  ? 14.690 1.281   24.221  0.40 39.53 ?  29  LYS   A HZ2  1 
ATOM   824  H  HZ3  A LYS   A 1 29  ? 12.950 1.583   22.994  0.60 41.28 ?  29  LYS   A HZ3  1 
ATOM   825  H  HZ3  B LYS   A 1 29  ? 13.824 2.193   23.501  0.40 39.53 ?  29  LYS   A HZ3  1 
ATOM   826  N  N    A VAL   A 1 30  ? 18.456 -1.279  18.825  0.60 22.45 ?  30  VAL   A N    1 
ATOM   827  N  N    B VAL   A 1 30  ? 18.517 -1.002  18.886  0.40 23.63 ?  30  VAL   A N    1 
ATOM   828  C  CA   A VAL   A 1 30  ? 19.126 -2.547  19.094  0.60 22.01 ?  30  VAL   A CA   1 
ATOM   829  C  CA   B VAL   A 1 30  ? 19.057 -2.319  19.182  0.40 22.93 ?  30  VAL   A CA   1 
ATOM   830  C  C    A VAL   A 1 30  ? 20.620 -2.346  19.333  0.60 21.23 ?  30  VAL   A C    1 
ATOM   831  C  C    B VAL   A 1 30  ? 20.572 -2.291  19.346  0.40 21.85 ?  30  VAL   A C    1 
ATOM   832  O  O    A VAL   A 1 30  ? 21.223 -3.037  20.162  0.60 21.60 ?  30  VAL   A O    1 
ATOM   833  O  O    B VAL   A 1 30  ? 21.119 -3.074  20.131  0.40 22.17 ?  30  VAL   A O    1 
ATOM   834  C  CB   A VAL   A 1 30  ? 18.858 -3.532  17.938  0.60 22.52 ?  30  VAL   A CB   1 
ATOM   835  C  CB   B VAL   A 1 30  ? 18.649 -3.305  18.070  0.40 23.38 ?  30  VAL   A CB   1 
ATOM   836  C  CG1  A VAL   A 1 30  ? 19.670 -4.814  18.116  0.60 22.61 ?  30  VAL   A CG1  1 
ATOM   837  C  CG1  B VAL   A 1 30  ? 19.287 -4.667  18.289  0.40 23.60 ?  30  VAL   A CG1  1 
ATOM   838  C  CG2  A VAL   A 1 30  ? 17.369 -3.847  17.829  0.60 23.12 ?  30  VAL   A CG2  1 
ATOM   839  C  CG2  B VAL   A 1 30  ? 17.133 -3.413  17.996  0.40 23.68 ?  30  VAL   A CG2  1 
ATOM   840  H  H    A VAL   A 1 30  ? 18.251 -1.156  18.000  0.60 27.11 ?  30  VAL   A H    1 
ATOM   841  H  H    B VAL   A 1 30  ? 18.721 -0.710  18.095  0.40 28.52 ?  30  VAL   A H    1 
ATOM   842  H  HA   A VAL   A 1 30  ? 18.733 -2.936  19.897  0.60 26.58 ?  30  VAL   A HA   1 
ATOM   843  H  HA   B VAL   A 1 30  ? 18.655 -2.638  20.009  0.40 27.69 ?  30  VAL   A HA   1 
ATOM   844  H  HB   A VAL   A 1 30  ? 19.136 -3.122  17.106  0.60 27.18 ?  30  VAL   A HB   1 
ATOM   845  H  HB   B VAL   A 1 30  ? 18.973 -2.961  17.221  0.40 28.22 ?  30  VAL   A HB   1 
ATOM   846  H  HG11 A VAL   A 1 30  ? 19.329 -5.490  17.508  0.60 27.30 ?  30  VAL   A HG11 1 
ATOM   847  H  HG11 B VAL   A 1 30  ? 18.857 -5.308  17.701  0.40 28.49 ?  30  VAL   A HG11 1 
ATOM   848  H  HG12 A VAL   A 1 30  ? 20.601 -4.632  17.914  0.60 27.30 ?  30  VAL   A HG12 1 
ATOM   849  H  HG12 B VAL   A 1 30  ? 20.234 -4.615  18.081  0.40 28.49 ?  30  VAL   A HG12 1 
ATOM   850  H  HG13 A VAL   A 1 30  ? 19.581 -5.121  19.031  0.60 27.30 ?  30  VAL   A HG13 1 
ATOM   851  H  HG13 B VAL   A 1 30  ? 19.162 -4.928  19.212  0.40 28.49 ?  30  VAL   A HG13 1 
ATOM   852  H  HG21 A VAL   A 1 30  ? 17.234 -4.492  17.116  0.60 27.91 ?  30  VAL   A HG21 1 
ATOM   853  H  HG21 B VAL   A 1 30  ? 16.897 -4.073  17.328  0.40 28.58 ?  30  VAL   A HG21 1 
ATOM   854  H  HG22 A VAL   A 1 30  ? 17.062 -4.215  18.671  0.60 27.91 ?  30  VAL   A HG22 1 
ATOM   855  H  HG22 B VAL   A 1 30  ? 16.795 -3.683  18.864  0.40 28.58 ?  30  VAL   A HG22 1 
ATOM   856  H  HG23 A VAL   A 1 30  ? 16.890 -3.028  17.629  0.60 27.91 ?  30  VAL   A HG23 1 
ATOM   857  H  HG23 B VAL   A 1 30  ? 16.767 -2.548  17.753  0.40 28.58 ?  30  VAL   A HG23 1 
ATOM   858  N  N    . LYS   A 1 31  ? 21.249 -1.412  18.624  1.00 20.72 ?  31  LYS   A N    1 
ATOM   859  C  CA   . LYS   A 1 31  ? 22.702 -1.294  18.609  1.00 21.40 ?  31  LYS   A CA   1 
ATOM   860  C  C    . LYS   A 1 31  ? 23.318 -2.654  18.268  1.00 19.34 ?  31  LYS   A C    1 
ATOM   861  O  O    . LYS   A 1 31  ? 24.094 -3.208  19.052  1.00 20.55 ?  31  LYS   A O    1 
ATOM   862  C  CB   . LYS   A 1 31  ? 23.253 -0.743  19.917  1.00 25.93 ?  31  LYS   A CB   1 
ATOM   863  C  CG   . LYS   A 1 31  ? 22.573 0.542   20.377  1.00 31.32 ?  31  LYS   A CG   1 
ATOM   864  C  CD   . LYS   A 1 31  ? 23.589 1.630   20.703  1.00 35.43 ?  31  LYS   A CD   1 
ATOM   865  C  CE   . LYS   A 1 31  ? 23.012 2.672   21.650  1.00 38.12 ?  31  LYS   A CE   1 
ATOM   866  N  NZ   . LYS   A 1 31  ? 21.728 3.239   21.157  1.00 39.62 ?  31  LYS   A NZ   1 
ATOM   867  H  H    A LYS   A 1 31  ? 20.841 -0.834  18.148  0.60 25.03 ?  31  LYS   A H    1 
ATOM   868  H  H    B LYS   A 1 31  ? 20.858 -0.862  18.106  0.40 25.03 ?  31  LYS   A H    1 
ATOM   869  H  HA   . LYS   A 1 31  ? 22.944 -0.674  17.907  1.00 25.85 ?  31  LYS   A HA   1 
ATOM   870  H  HB2  . LYS   A 1 31  ? 23.122 -1.403  20.605  1.00 31.28 ?  31  LYS   A HB2  1 
ATOM   871  H  HB3  . LYS   A 1 31  ? 24.202 -0.554  19.813  1.00 31.28 ?  31  LYS   A HB3  1 
ATOM   872  H  HG2  . LYS   A 1 31  ? 21.994 0.870   19.670  1.00 37.75 ?  31  LYS   A HG2  1 
ATOM   873  H  HG3  . LYS   A 1 31  ? 22.053 0.363   21.178  1.00 37.75 ?  31  LYS   A HG3  1 
ATOM   874  H  HD2  . LYS   A 1 31  ? 24.362 1.231   21.130  1.00 42.69 ?  31  LYS   A HD2  1 
ATOM   875  H  HD3  . LYS   A 1 31  ? 23.852 2.078   19.882  1.00 42.69 ?  31  LYS   A HD3  1 
ATOM   876  H  HE2  . LYS   A 1 31  ? 22.848 2.261   22.513  1.00 45.91 ?  31  LYS   A HE2  1 
ATOM   877  H  HE3  . LYS   A 1 31  ? 23.645 3.402   21.744  1.00 45.91 ?  31  LYS   A HE3  1 
ATOM   878  H  HZ1  . LYS   A 1 31  ? 21.438 3.866   21.717  1.00 47.71 ?  31  LYS   A HZ1  1 
ATOM   879  H  HZ2  . LYS   A 1 31  ? 21.844 3.599   20.352  1.00 47.71 ?  31  LYS   A HZ2  1 
ATOM   880  H  HZ3  . LYS   A 1 31  ? 21.115 2.596   21.100  1.00 47.71 ?  31  LYS   A HZ3  1 
ATOM   881  N  N    . PRO   A 1 32  ? 22.979 -3.213  17.110  1.00 16.96 ?  32  PRO   A N    1 
ATOM   882  C  CA   . PRO   A 1 32  ? 23.449 -4.554  16.770  1.00 16.79 ?  32  PRO   A CA   1 
ATOM   883  C  C    . PRO   A 1 32  ? 24.949 -4.568  16.555  1.00 16.79 ?  32  PRO   A C    1 
ATOM   884  O  O    . PRO   A 1 32  ? 25.591 -3.540  16.332  1.00 16.80 ?  32  PRO   A O    1 
ATOM   885  C  CB   . PRO   A 1 32  ? 22.715 -4.857  15.460  1.00 17.08 ?  32  PRO   A CB   1 
ATOM   886  C  CG   . PRO   A 1 32  ? 22.548 -3.513  14.833  1.00 15.97 ?  32  PRO   A CG   1 
ATOM   887  C  CD   . PRO   A 1 32  ? 22.257 -2.593  15.988  1.00 16.15 ?  32  PRO   A CD   1 
ATOM   888  H  HA   . PRO   A 1 32  ? 23.199 -5.196  17.451  1.00 20.32 ?  32  PRO   A HA   1 
ATOM   889  H  HB2  . PRO   A 1 32  ? 23.260 -5.439  14.901  1.00 20.66 ?  32  PRO   A HB2  1 
ATOM   890  H  HB3  . PRO   A 1 32  ? 21.855 -5.268  15.647  1.00 20.66 ?  32  PRO   A HB3  1 
ATOM   891  H  HG2  . PRO   A 1 32  ? 23.365 -3.267  14.380  1.00 19.32 ?  32  PRO   A HG2  1 
ATOM   892  H  HG3  . PRO   A 1 32  ? 21.802 -3.544  14.210  1.00 19.32 ?  32  PRO   A HG3  1 
ATOM   893  H  HD2  . PRO   A 1 32  ? 22.609 -1.710  15.795  1.00 19.55 ?  32  PRO   A HD2  1 
ATOM   894  H  HD3  . PRO   A 1 32  ? 21.305 -2.569  16.161  1.00 19.55 ?  32  PRO   A HD3  1 
ATOM   895  N  N    . THR   A 1 33  ? 25.502 -5.776  16.598  1.00 16.82 ?  33  THR   A N    1 
ATOM   896  C  CA   . THR   A 1 33  ? 26.913 -5.939  16.285  1.00 16.67 ?  33  THR   A CA   1 
ATOM   897  C  C    . THR   A 1 33  ? 27.212 -5.482  14.863  1.00 15.19 ?  33  THR   A C    1 
ATOM   898  O  O    . THR   A 1 33  ? 28.246 -4.844  14.613  1.00 15.69 ?  33  THR   A O    1 
ATOM   899  C  CB   . THR   A 1 33  ? 27.313 -7.398  16.489  1.00 18.47 ?  33  THR   A CB   1 
ATOM   900  O  OG1  . THR   A 1 33  ? 27.002 -7.787  17.830  1.00 20.35 ?  33  THR   A OG1  1 
ATOM   901  C  CG2  . THR   A 1 33  ? 28.800 -7.587  16.246  1.00 19.20 ?  33  THR   A CG2  1 
ATOM   902  H  H    . THR   A 1 33  ? 25.090 -6.503  16.798  1.00 20.35 ?  33  THR   A H    1 
ATOM   903  H  HA   . THR   A 1 33  ? 27.440 -5.396  16.891  1.00 20.16 ?  33  THR   A HA   1 
ATOM   904  H  HB   . THR   A 1 33  ? 26.824 -7.963  15.869  1.00 22.33 ?  33  THR   A HB   1 
ATOM   905  H  HG1  . THR   A 1 33  ? 27.425 -7.304  18.377  1.00 24.59 ?  33  THR   A HG1  1 
ATOM   906  H  HG21 . THR   A 1 33  ? 29.071 -8.474  16.533  1.00 23.21 ?  33  THR   A HG21 1 
ATOM   907  H  HG22 . THR   A 1 33  ? 28.999 -7.488  15.303  1.00 23.21 ?  33  THR   A HG22 1 
ATOM   908  H  HG23 . THR   A 1 33  ? 29.302 -6.928  16.749  1.00 23.21 ?  33  THR   A HG23 1 
ATOM   909  N  N    . VAL   A 1 34  ? 26.321 -5.797  13.920  1.00 13.59 ?  34  VAL   A N    1 
ATOM   910  C  CA   . VAL   A 1 34  ? 26.514 -5.467  12.512  1.00 12.46 ?  34  VAL   A CA   1 
ATOM   911  C  C    . VAL   A 1 34  ? 25.218 -4.906  11.943  1.00 11.86 ?  34  VAL   A C    1 
ATOM   912  O  O    . VAL   A 1 34  ? 24.175 -5.573  11.990  1.00 12.72 ?  34  VAL   A O    1 
ATOM   913  C  CB   . VAL   A 1 34  ? 26.960 -6.679  11.672  1.00 13.20 ?  34  VAL   A CB   1 
ATOM   914  C  CG1  . VAL   A 1 34  ? 27.151 -6.270  10.217  1.00 13.45 ?  34  VAL   A CG1  1 
ATOM   915  C  CG2  . VAL   A 1 34  ? 28.231 -7.306  12.237  1.00 14.49 ?  34  VAL   A CG2  1 
ATOM   916  H  H    . VAL   A 1 34  ? 25.581 -6.216  14.078  1.00 16.48 ?  34  VAL   A H    1 
ATOM   917  H  HA   . VAL   A 1 34  ? 27.192 -4.779  12.436  1.00 15.12 ?  34  VAL   A HA   1 
ATOM   918  H  HB   . VAL   A 1 34  ? 26.258 -7.347  11.700  1.00 16.00 ?  34  VAL   A HB   1 
ATOM   919  H  HG11 . VAL   A 1 34  ? 27.641 -6.969  9.758   1.00 16.30 ?  34  VAL   A HG11 1 
ATOM   920  H  HG12 . VAL   A 1 34  ? 26.284 -6.146  9.801   1.00 16.30 ?  34  VAL   A HG12 1 
ATOM   921  H  HG13 . VAL   A 1 34  ? 27.656 -5.440  10.186  1.00 16.30 ?  34  VAL   A HG13 1 
ATOM   922  H  HG21 . VAL   A 1 34  ? 28.498 -8.043  11.666  1.00 17.55 ?  34  VAL   A HG21 1 
ATOM   923  H  HG22 . VAL   A 1 34  ? 28.931 -6.635  12.261  1.00 17.55 ?  34  VAL   A HG22 1 
ATOM   924  H  HG23 . VAL   A 1 34  ? 28.053 -7.630  13.134  1.00 17.55 ?  34  VAL   A HG23 1 
ATOM   925  N  N    . VAL   A 1 35  ? 25.286 -3.698  11.382  1.00 11.26 ?  35  VAL   A N    1 
ATOM   926  C  CA   . VAL   A 1 35  ? 24.250 -3.179  10.499  1.00 10.86 ?  35  VAL   A CA   1 
ATOM   927  C  C    . VAL   A 1 35  ? 24.803 -3.185  9.081   1.00 10.28 ?  35  VAL   A C    1 
ATOM   928  O  O    . VAL   A 1 35  ? 25.950 -2.780  8.847   1.00 11.04 ?  35  VAL   A O    1 
ATOM   929  C  CB   . VAL   A 1 35  ? 23.724 -1.783  10.910  1.00 11.53 ?  35  VAL   A CB   1 
ATOM   930  C  CG1  . VAL   A 1 35  ? 24.793 -0.686  10.775  1.00 11.92 ?  35  VAL   A CG1  1 
ATOM   931  C  CG2  . VAL   A 1 35  ? 22.489 -1.426  10.086  1.00 12.12 ?  35  VAL   A CG2  1 
ATOM   932  H  H    . VAL   A 1 35  ? 25.935 -3.146  11.499  1.00 13.68 ?  35  VAL   A H    1 
ATOM   933  H  HA   . VAL   A 1 35  ? 23.491 -3.786  10.518  1.00 13.19 ?  35  VAL   A HA   1 
ATOM   934  H  HB   . VAL   A 1 35  ? 23.448 -1.815  11.836  1.00 14.00 ?  35  VAL   A HB   1 
ATOM   935  H  HG11 . VAL   A 1 35  ? 24.441 0.146   11.137  1.00 14.47 ?  35  VAL   A HG11 1 
ATOM   936  H  HG12 . VAL   A 1 35  ? 25.581 -0.952  11.272  1.00 14.47 ?  35  VAL   A HG12 1 
ATOM   937  H  HG13 . VAL   A 1 35  ? 25.016 -0.566  9.838   1.00 14.47 ?  35  VAL   A HG13 1 
ATOM   938  H  HG21 . VAL   A 1 35  ? 22.136 -0.581  10.396  1.00 14.71 ?  35  VAL   A HG21 1 
ATOM   939  H  HG22 . VAL   A 1 35  ? 22.745 -1.355  9.150   1.00 14.71 ?  35  VAL   A HG22 1 
ATOM   940  H  HG23 . VAL   A 1 35  ? 21.827 -2.126  10.193  1.00 14.71 ?  35  VAL   A HG23 1 
ATOM   941  N  N    . VAL   A 1 36  ? 23.985 -3.639  8.132   1.00 9.93  ?  36  VAL   A N    1 
ATOM   942  C  CA   . VAL   A 1 36  ? 24.359 -3.647  6.726   1.00 9.58  ?  36  VAL   A CA   1 
ATOM   943  C  C    . VAL   A 1 36  ? 23.901 -2.356  6.064   1.00 9.84  ?  36  VAL   A C    1 
ATOM   944  O  O    . VAL   A 1 36  ? 22.739 -1.951  6.206   1.00 10.75 ?  36  VAL   A O    1 
ATOM   945  C  CB   . VAL   A 1 36  ? 23.748 -4.861  6.007   1.00 9.84  ?  36  VAL   A CB   1 
ATOM   946  C  CG1  . VAL   A 1 36  ? 24.004 -4.786  4.522   1.00 10.55 ?  36  VAL   A CG1  1 
ATOM   947  C  CG2  . VAL   A 1 36  ? 24.287 -6.156  6.584   1.00 10.69 ?  36  VAL   A CG2  1 
ATOM   948  H  H    . VAL   A 1 36  ? 23.193 -3.949  8.285   1.00 12.08 ?  36  VAL   A H    1 
ATOM   949  H  HA   . VAL   A 1 36  ? 25.328 -3.707  6.654   1.00 11.66 ?  36  VAL   A HA   1 
ATOM   950  H  HB   . VAL   A 1 36  ? 22.790 -4.849  6.145   1.00 11.97 ?  36  VAL   A HB   1 
ATOM   951  H  HG11 . VAL   A 1 36  ? 23.864 -5.664  4.134   1.00 12.82 ?  36  VAL   A HG11 1 
ATOM   952  H  HG12 . VAL   A 1 36  ? 23.391 -4.148  4.122   1.00 12.82 ?  36  VAL   A HG12 1 
ATOM   953  H  HG13 . VAL   A 1 36  ? 24.921 -4.503  4.371   1.00 12.82 ?  36  VAL   A HG13 1 
ATOM   954  H  HG21 . VAL   A 1 36  ? 23.893 -6.905  6.109   1.00 13.00 ?  36  VAL   A HG21 1 
ATOM   955  H  HG22 . VAL   A 1 36  ? 25.253 -6.174  6.484   1.00 13.00 ?  36  VAL   A HG22 1 
ATOM   956  H  HG23 . VAL   A 1 36  ? 24.056 -6.209  7.527   1.00 13.00 ?  36  VAL   A HG23 1 
ATOM   957  N  N    . ASN   A 1 37  ? 24.816 -1.726  5.326   1.00 9.32  ?  37  ASN   A N    1 
ATOM   958  C  CA   . ASN   A 1 37  ? 24.489 -0.602  4.463   1.00 9.21  ?  37  ASN   A CA   1 
ATOM   959  C  C    . ASN   A 1 37  ? 24.350 -1.071  3.024   1.00 9.08  ?  37  ASN   A C    1 
ATOM   960  O  O    . ASN   A 1 37  ? 25.128 -1.903  2.548   1.00 9.94  ?  37  ASN   A O    1 
ATOM   961  C  CB   . ASN   A 1 37  ? 25.566 0.476   4.547   1.00 9.40  ?  37  ASN   A CB   1 
ATOM   962  C  CG   . ASN   A 1 37  ? 25.243 1.676   3.697   1.00 9.99  ?  37  ASN   A CG   1 
ATOM   963  O  OD1  . ASN   A 1 37  ? 24.070 2.022   3.521   1.00 10.45 ?  37  ASN   A OD1  1 
ATOM   964  N  ND2  . ASN   A 1 37  ? 26.274 2.322   3.167   1.00 10.22 ?  37  ASN   A ND2  1 
ATOM   965  H  H    . ASN   A 1 37  ? 25.655 -1.932  5.321   1.00 11.35 ?  37  ASN   A H    1 
ATOM   966  H  HA   . ASN   A 1 37  ? 23.652 -0.215  4.750   1.00 11.22 ?  37  ASN   A HA   1 
ATOM   967  H  HB2  . ASN   A 1 37  ? 25.650 0.775   5.470   1.00 11.44 ?  37  ASN   A HB2  1 
ATOM   968  H  HB3  . ASN   A 1 37  ? 26.416 0.106   4.246   1.00 11.44 ?  37  ASN   A HB3  1 
ATOM   969  H  HD21 . ASN   A 1 37  ? 26.138 3.007   2.670   1.00 12.43 ?  37  ASN   A HD21 1 
ATOM   970  H  HD22 . ASN   A 1 37  ? 27.072 2.047   3.307   1.00 12.43 ?  37  ASN   A HD22 1 
ATOM   971  N  N    . ALA   A 1 38  ? 23.337 -0.528  2.342   1.00 9.75  ?  38  ALA   A N    1 
ATOM   972  C  CA   . ALA   A 1 38  ? 23.147 -0.690  0.901   1.00 10.38 ?  38  ALA   A CA   1 
ATOM   973  C  C    . ALA   A 1 38  ? 24.048 0.313   0.178   1.00 10.09 ?  38  ALA   A C    1 
ATOM   974  O  O    . ALA   A 1 38  ? 23.631 1.398   -0.234  1.00 10.33 ?  38  ALA   A O    1 
ATOM   975  C  CB   . ALA   A 1 38  ? 21.683 -0.482  0.541   1.00 11.74 ?  38  ALA   A CB   1 
ATOM   976  H  H    . ALA   A 1 38  ? 22.736 -0.031  2.709   1.00 11.86 ?  38  ALA   A H    1 
ATOM   977  H  HA   . ALA   A 1 38  ? 23.409 -1.588  0.640   1.00 12.63 ?  38  ALA   A HA   1 
ATOM   978  H  HB1  . ALA   A 1 38  ? 21.563 -0.644  -0.406  1.00 14.25 ?  38  ALA   A HB1  1 
ATOM   979  H  HB2  . ALA   A 1 38  ? 21.138 -1.106  1.054   1.00 14.25 ?  38  ALA   A HB2  1 
ATOM   980  H  HB3  . ALA   A 1 38  ? 21.430 0.427   0.758   1.00 14.25 ?  38  ALA   A HB3  1 
ATOM   981  N  N    . ALA   A 1 39  ? 25.319 -0.054  0.041   1.00 10.13 ?  39  ALA   A N    1 
ATOM   982  C  CA   . ALA   A 1 39  ? 26.363 0.831   -0.448  1.00 10.17 ?  39  ALA   A CA   1 
ATOM   983  C  C    . ALA   A 1 39  ? 26.482 0.774   -1.965  1.00 10.18 ?  39  ALA   A C    1 
ATOM   984  O  O    . ALA   A 1 39  ? 26.011 -0.159  -2.619  1.00 10.56 ?  39  ALA   A O    1 
ATOM   985  C  CB   . ALA   A 1 39  ? 27.700 0.440   0.187   1.00 10.99 ?  39  ALA   A CB   1 
ATOM   986  H  H    . ALA   A 1 39  ? 25.609 -0.844  0.241   1.00 12.32 ?  39  ALA   A H    1 
ATOM   987  H  HA   . ALA   A 1 39  ? 26.155 1.741   -0.189  1.00 12.37 ?  39  ALA   A HA   1 
ATOM   988  H  HB1  . ALA   A 1 39  ? 28.391 1.036   -0.143  1.00 13.36 ?  39  ALA   A HB1  1 
ATOM   989  H  HB2  . ALA   A 1 39  ? 27.628 0.526   1.154   1.00 13.36 ?  39  ALA   A HB2  1 
ATOM   990  H  HB3  . ALA   A 1 39  ? 27.908 -0.475  -0.048  1.00 13.36 ?  39  ALA   A HB3  1 
ATOM   991  N  N    . ASN   A 1 40  ? 27.153 1.785   -2.521  1.00 10.44 ?  40  ASN   A N    1 
ATOM   992  C  CA   . ASN   A 1 40  ? 27.684 1.733   -3.877  1.00 10.78 ?  40  ASN   A CA   1 
ATOM   993  C  C    . ASN   A 1 40  ? 29.208 1.617   -3.819  1.00 10.07 ?  40  ASN   A C    1 
ATOM   994  O  O    . ASN   A 1 40  ? 29.810 1.719   -2.747  1.00 10.42 ?  40  ASN   A O    1 
ATOM   995  C  CB   . ASN   A 1 40  ? 27.208 2.923   -4.729  1.00 11.27 ?  40  ASN   A CB   1 
ATOM   996  C  CG   . ASN   A 1 40  ? 27.580 4.263   -4.135  1.00 12.41 ?  40  ASN   A CG   1 
ATOM   997  O  OD1  . ASN   A 1 40  ? 28.751 4.526   -3.847  1.00 13.20 ?  40  ASN   A OD1  1 
ATOM   998  N  ND2  . ASN   A 1 40  ? 26.579 5.129   -3.957  1.00 13.37 ?  40  ASN   A ND2  1 
ATOM   999  H  H    . ASN   A 1 40  ? 27.331 2.518   -2.117  1.00 12.70 ?  40  ASN   A H    1 
ATOM   1000 H  HA   . ASN   A 1 40  ? 27.348 0.925   -4.307  1.00 13.10 ?  40  ASN   A HA   1 
ATOM   1001 H  HB2  . ASN   A 1 40  ? 27.611 2.857   -5.613  1.00 13.69 ?  40  ASN   A HB2  1 
ATOM   1002 H  HB3  . ASN   A 1 40  ? 26.241 2.885   -4.812  1.00 13.69 ?  40  ASN   A HB3  1 
ATOM   1003 H  HD21 . ASN   A 1 40  ? 26.739 5.911   -3.630  1.00 16.21 ?  40  ASN   A HD21 1 
ATOM   1004 H  HD22 . ASN   A 1 40  ? 25.775 4.914   -4.173  1.00 16.21 ?  40  ASN   A HD22 1 
ATOM   1005 N  N    . VAL   A 1 41  ? 29.821 1.372   -4.981  1.00 10.55 ?  41  VAL   A N    1 
ATOM   1006 C  CA   . VAL   A 1 41  ? 31.249 1.058   -5.010  1.00 11.39 ?  41  VAL   A CA   1 
ATOM   1007 C  C    . VAL   A 1 41  ? 32.110 2.210   -4.525  1.00 11.06 ?  41  VAL   A C    1 
ATOM   1008 O  O    . VAL   A 1 41  ? 33.257 1.989   -4.118  1.00 11.74 ?  41  VAL   A O    1 
ATOM   1009 C  CB   . VAL   A 1 41  ? 31.727 0.583   -6.402  1.00 12.45 ?  41  VAL   A CB   1 
ATOM   1010 C  CG1  . VAL   A 1 41  ? 31.031 -0.715  -6.795  1.00 13.30 ?  41  VAL   A CG1  1 
ATOM   1011 C  CG2  . VAL   A 1 41  ? 31.549 1.659   -7.467  1.00 13.28 ?  41  VAL   A CG2  1 
ATOM   1012 H  H    . VAL   A 1 41  ? 29.434 1.365   -5.752  1.00 12.83 ?  41  VAL   A H    1 
ATOM   1013 H  HA   . VAL   A 1 41  ? 31.405 0.319   -4.400  1.00 13.83 ?  41  VAL   A HA   1 
ATOM   1014 H  HB   . VAL   A 1 41  ? 32.676 0.387   -6.347  1.00 15.10 ?  41  VAL   A HB   1 
ATOM   1015 H  HG11 . VAL   A 1 41  ? 31.362 -1.008  -7.658  1.00 16.12 ?  41  VAL   A HG11 1 
ATOM   1016 H  HG12 . VAL   A 1 41  ? 31.216 -1.393  -6.124  1.00 16.12 ?  41  VAL   A HG12 1 
ATOM   1017 H  HG13 . VAL   A 1 41  ? 30.073 -0.558  -6.846  1.00 16.12 ?  41  VAL   A HG13 1 
ATOM   1018 H  HG21 . VAL   A 1 41  ? 31.789 1.287   -8.333  1.00 16.10 ?  41  VAL   A HG21 1 
ATOM   1019 H  HG22 . VAL   A 1 41  ? 30.625 1.945   -7.475  1.00 16.10 ?  41  VAL   A HG22 1 
ATOM   1020 H  HG23 . VAL   A 1 41  ? 32.129 2.407   -7.259  1.00 16.10 ?  41  VAL   A HG23 1 
ATOM   1021 N  N    . TYR   A 1 42  ? 31.600 3.442   -4.589  1.00 11.26 ?  42  TYR   A N    1 
ATOM   1022 C  CA   . TYR   A 1 42  ? 32.342 4.630   -4.183  1.00 11.20 ?  42  TYR   A CA   1 
ATOM   1023 C  C    . TYR   A 1 42  ? 32.091 5.006   -2.734  1.00 10.90 ?  42  TYR   A C    1 
ATOM   1024 O  O    . TYR   A 1 42  ? 32.655 5.999   -2.252  1.00 11.40 ?  42  TYR   A O    1 
ATOM   1025 C  CB   . TYR   A 1 42  ? 31.985 5.817   -5.097  1.00 12.13 ?  42  TYR   A CB   1 
ATOM   1026 C  CG   . TYR   A 1 42  ? 32.178 5.509   -6.566  1.00 12.70 ?  42  TYR   A CG   1 
ATOM   1027 C  CD1  . TYR   A 1 42  ? 33.442 5.308   -7.094  1.00 13.52 ?  42  TYR   A CD1  1 
ATOM   1028 C  CD2  . TYR   A 1 42  ? 31.089 5.383   -7.417  1.00 14.06 ?  42  TYR   A CD2  1 
ATOM   1029 C  CE1  . TYR   A 1 42  ? 33.617 5.000   -8.433  1.00 14.15 ?  42  TYR   A CE1  1 
ATOM   1030 C  CE2  . TYR   A 1 42  ? 31.259 5.089   -8.756  1.00 15.37 ?  42  TYR   A CE2  1 
ATOM   1031 C  CZ   . TYR   A 1 42  ? 32.525 4.893   -9.259  1.00 15.20 ?  42  TYR   A CZ   1 
ATOM   1032 O  OH   . TYR   A 1 42  ? 32.692 4.591   -10.592 1.00 16.82 ?  42  TYR   A OH   1 
ATOM   1033 H  H    . TYR   A 1 42  ? 30.803 3.611   -4.873  1.00 13.68 ?  42  TYR   A H    1 
ATOM   1034 H  HA   . TYR   A 1 42  ? 33.286 4.458   -4.287  1.00 13.60 ?  42  TYR   A HA   1 
ATOM   1035 H  HB2  . TYR   A 1 42  ? 31.049 6.055   -4.960  1.00 14.72 ?  42  TYR   A HB2  1 
ATOM   1036 H  HB3  . TYR   A 1 42  ? 32.549 6.573   -4.873  1.00 14.72 ?  42  TYR   A HB3  1 
ATOM   1037 H  HD1  . TYR   A 1 42  ? 34.182 5.372   -6.535  1.00 16.39 ?  42  TYR   A HD1  1 
ATOM   1038 H  HD2  . TYR   A 1 42  ? 30.229 5.518   -7.084  1.00 17.04 ?  42  TYR   A HD2  1 
ATOM   1039 H  HE1  . TYR   A 1 42  ? 34.471 4.866   -8.771  1.00 17.14 ?  42  TYR   A HE1  1 
ATOM   1040 H  HE2  . TYR   A 1 42  ? 30.519 5.014   -9.316  1.00 18.61 ?  42  TYR   A HE2  1 
ATOM   1041 H  HH   . TYR   A 1 42  ? 33.511 4.489   -10.763 1.00 20.35 ?  42  TYR   A HH   1 
ATOM   1042 N  N    . LEU   A 1 43  ? 31.241 4.246   -2.043  1.00 10.50 ?  43  LEU   A N    1 
ATOM   1043 C  CA   . LEU   A 1 43  ? 30.794 4.586   -0.694  1.00 10.21 ?  43  LEU   A CA   1 
ATOM   1044 C  C    . LEU   A 1 43  ? 30.313 6.034   -0.605  1.00 10.31 ?  43  LEU   A C    1 
ATOM   1045 O  O    . LEU   A 1 43  ? 30.576 6.739   0.373   1.00 11.30 ?  43  LEU   A O    1 
ATOM   1046 C  CB   . LEU   A 1 43  ? 31.841 4.281   0.373   1.00 10.55 ?  43  LEU   A CB   1 
ATOM   1047 C  CG   . LEU   A 1 43  ? 32.330 2.831   0.462   1.00 10.92 ?  43  LEU   A CG   1 
ATOM   1048 C  CD1  . LEU   A 1 43  ? 33.386 2.718   1.548   1.00 11.99 ?  43  LEU   A CD1  1 
ATOM   1049 C  CD2  . LEU   A 1 43  ? 31.190 1.840   0.702   1.00 11.39 ?  43  LEU   A CD2  1 
ATOM   1050 H  H    . LEU   A 1 43  ? 30.900 3.507   -2.336  1.00 12.77 ?  43  LEU   A H    1 
ATOM   1051 H  HA   . LEU   A 1 43  ? 30.024 4.027   -0.489  1.00 12.42 ?  43  LEU   A HA   1 
ATOM   1052 H  HB2  . LEU   A 1 43  ? 32.616 4.838   0.209   1.00 12.83 ?  43  LEU   A HB2  1 
ATOM   1053 H  HB3  . LEU   A 1 43  ? 31.462 4.507   1.241   1.00 12.83 ?  43  LEU   A HB3  1 
ATOM   1054 H  HG   . LEU   A 1 43  ? 32.750 2.596   -0.378  1.00 13.27 ?  43  LEU   A HG   1 
ATOM   1055 H  HD11 . LEU   A 1 43  ? 33.693 1.799   1.599   1.00 14.55 ?  43  LEU   A HD11 1 
ATOM   1056 H  HD12 . LEU   A 1 43  ? 34.130 3.302   1.329   1.00 14.55 ?  43  LEU   A HD12 1 
ATOM   1057 H  HD13 . LEU   A 1 43  ? 32.999 2.984   2.398   1.00 14.55 ?  43  LEU   A HD13 1 
ATOM   1058 H  HD21 . LEU   A 1 43  ? 31.566 0.952   0.831   1.00 13.83 ?  43  LEU   A HD21 1 
ATOM   1059 H  HD22 . LEU   A 1 43  ? 30.698 2.106   1.493   1.00 13.83 ?  43  LEU   A HD22 1 
ATOM   1060 H  HD23 . LEU   A 1 43  ? 30.604 1.838   -0.070  1.00 13.83 ?  43  LEU   A HD23 1 
ATOM   1061 N  N    . LYS   A 1 44  ? 29.583 6.471   -1.632  1.00 10.42 ?  44  LYS   A N    1 
ATOM   1062 C  CA   . LYS   A 1 44  ? 28.935 7.783   -1.636  1.00 11.08 ?  44  LYS   A CA   1 
ATOM   1063 C  C    . LYS   A 1 44  ? 27.513 7.595   -1.128  1.00 10.22 ?  44  LYS   A C    1 
ATOM   1064 O  O    . LYS   A 1 44  ? 26.643 7.090   -1.843  1.00 11.24 ?  44  LYS   A O    1 
ATOM   1065 C  CB   . LYS   A 1 44  ? 28.971 8.401   -3.027  1.00 13.50 ?  44  LYS   A CB   1 
ATOM   1066 C  CG   . LYS   A 1 44  ? 30.345 8.871   -3.454  1.00 16.92 ?  44  LYS   A CG   1 
ATOM   1067 C  CD   . LYS   A 1 44  ? 31.007 9.761   -2.399  1.00 22.70 ?  44  LYS   A CD   1 
ATOM   1068 C  CE   . LYS   A 1 44  ? 32.346 10.291  -2.875  1.00 26.25 ?  44  LYS   A CE   1 
ATOM   1069 N  NZ   . LYS   A 1 44  ? 33.181 10.809  -1.755  1.00 27.96 ?  44  LYS   A NZ   1 
ATOM   1070 H  H    . LYS   A 1 44  ? 29.448 6.016   -2.351  1.00 12.66 ?  44  LYS   A H    1 
ATOM   1071 H  HA   . LYS   A 1 44  ? 29.386 8.362   -1.004  1.00 13.46 ?  44  LYS   A HA   1 
ATOM   1072 H  HB2  . LYS   A 1 44  ? 28.668 7.742   -3.670  1.00 16.36 ?  44  LYS   A HB2  1 
ATOM   1073 H  HB3  . LYS   A 1 44  ? 28.377 9.169   -3.040  1.00 16.36 ?  44  LYS   A HB3  1 
ATOM   1074 H  HG2  . LYS   A 1 44  ? 30.916 8.102   -3.603  1.00 20.46 ?  44  LYS   A HG2  1 
ATOM   1075 H  HG3  . LYS   A 1 44  ? 30.266 9.390   -4.274  1.00 20.46 ?  44  LYS   A HG3  1 
ATOM   1076 H  HD2  . LYS   A 1 44  ? 30.420 10.507  -2.200  1.00 27.40 ?  44  LYS   A HD2  1 
ATOM   1077 H  HD3  . LYS   A 1 44  ? 31.168 9.236   -1.597  1.00 27.40 ?  44  LYS   A HD3  1 
ATOM   1078 H  HE2  . LYS   A 1 44  ? 32.835 9.571   -3.305  1.00 31.66 ?  44  LYS   A HE2  1 
ATOM   1079 H  HE3  . LYS   A 1 44  ? 32.195 11.013  -3.500  1.00 31.66 ?  44  LYS   A HE3  1 
ATOM   1080 H  HZ1  . LYS   A 1 44  ? 33.956 11.112  -2.069  1.00 33.72 ?  44  LYS   A HZ1  1 
ATOM   1081 H  HZ2  . LYS   A 1 44  ? 32.756 11.476  -1.343  1.00 33.72 ?  44  LYS   A HZ2  1 
ATOM   1082 H  HZ3  . LYS   A 1 44  ? 33.339 10.162  -1.166  1.00 33.72 ?  44  LYS   A HZ3  1 
ATOM   1083 N  N    A HIS   A 1 45  ? 27.280 7.992   0.118   0.60 9.77  ?  45  HIS   A N    1 
ATOM   1084 N  N    B HIS   A 1 45  ? 27.278 7.995   0.122   0.40 10.44 ?  45  HIS   A N    1 
ATOM   1085 C  CA   A HIS   A 1 45  ? 26.049 7.635   0.821   0.60 9.65  ?  45  HIS   A CA   1 
ATOM   1086 C  CA   B HIS   A 1 45  ? 26.028 7.692   0.821   0.40 10.87 ?  45  HIS   A CA   1 
ATOM   1087 C  C    A HIS   A 1 45  ? 25.015 8.756   0.677   0.60 10.26 ?  45  HIS   A C    1 
ATOM   1088 C  C    B HIS   A 1 45  ? 25.046 8.837   0.602   0.40 11.70 ?  45  HIS   A C    1 
ATOM   1089 O  O    A HIS   A 1 45  ? 24.650 9.446   1.629   0.60 10.55 ?  45  HIS   A O    1 
ATOM   1090 O  O    B HIS   A 1 45  ? 24.946 9.759   1.412   0.40 12.50 ?  45  HIS   A O    1 
ATOM   1091 C  CB   A HIS   A 1 45  ? 26.362 7.343   2.278   0.60 9.45  ?  45  HIS   A CB   1 
ATOM   1092 C  CB   B HIS   A 1 45  ? 26.295 7.488   2.306   0.40 10.49 ?  45  HIS   A CB   1 
ATOM   1093 C  CG   A HIS   A 1 45  ? 27.474 6.363   2.468   0.60 8.77  ?  45  HIS   A CG   1 
ATOM   1094 C  CG   B HIS   A 1 45  ? 27.418 6.543   2.596   0.40 9.80  ?  45  HIS   A CG   1 
ATOM   1095 N  ND1  A HIS   A 1 45  ? 27.439 5.085   1.949   0.60 8.93  ?  45  HIS   A ND1  1 
ATOM   1096 N  ND1  B HIS   A 1 45  ? 27.432 5.242   2.142   0.40 10.59 ?  45  HIS   A ND1  1 
ATOM   1097 C  CD2  A HIS   A 1 45  ? 28.658 6.484   3.111   0.60 9.57  ?  45  HIS   A CD2  1 
ATOM   1098 C  CD2  B HIS   A 1 45  ? 28.564 6.715   3.295   0.40 8.82  ?  45  HIS   A CD2  1 
ATOM   1099 C  CE1  A HIS   A 1 45  ? 28.557 4.460   2.277   0.60 9.43  ?  45  HIS   A CE1  1 
ATOM   1100 C  CE1  B HIS   A 1 45  ? 28.543 4.654   2.549   0.40 9.53  ?  45  HIS   A CE1  1 
ATOM   1101 N  NE2  A HIS   A 1 45  ? 29.314 5.285   2.981   0.60 9.89  ?  45  HIS   A NE2  1 
ATOM   1102 N  NE2  B HIS   A 1 45  ? 29.248 5.525   3.250   0.40 8.63  ?  45  HIS   A NE2  1 
ATOM   1103 H  H    A HIS   A 1 45  ? 27.814 8.480   0.583   0.60 11.89 ?  45  HIS   A H    1 
ATOM   1104 H  H    B HIS   A 1 45  ? 27.830 8.458   0.594   0.40 12.70 ?  45  HIS   A H    1 
ATOM   1105 H  HA   A HIS   A 1 45  ? 25.674 6.830   0.426   0.60 11.75 ?  45  HIS   A HA   1 
ATOM   1106 H  HA   B HIS   A 1 45  ? 25.639 6.883   0.460   0.40 13.21 ?  45  HIS   A HA   1 
ATOM   1107 H  HB2  A HIS   A 1 45  ? 26.612 8.166   2.718   0.60 11.51 ?  45  HIS   A HB2  1 
ATOM   1108 H  HB2  B HIS   A 1 45  ? 26.511 8.344   2.706   0.40 12.75 ?  45  HIS   A HB2  1 
ATOM   1109 H  HB3  A HIS   A 1 45  ? 25.567 6.972   2.701   0.60 11.51 ?  45  HIS   A HB3  1 
ATOM   1110 H  HB3  B HIS   A 1 45  ? 25.491 7.129   2.719   0.40 12.75 ?  45  HIS   A HB3  1 
ATOM   1111 H  HD2  A HIS   A 1 45  ? 28.972 7.240   3.556   0.60 11.65 ?  45  HIS   A HD2  1 
ATOM   1112 H  HD2  B HIS   A 1 45  ? 28.839 7.497   3.721   0.40 10.74 ?  45  HIS   A HD2  1 
ATOM   1113 H  HE1  A HIS   A 1 45  ? 28.777 3.579   2.064   0.60 11.48 ?  45  HIS   A HE1  1 
ATOM   1114 H  HE1  B HIS   A 1 45  ? 28.788 3.775   2.374   0.40 11.60 ?  45  HIS   A HE1  1 
ATOM   1115 H  HE2  A HIS   A 1 45  ? 30.094 5.103   3.307   0.60 12.03 ?  45  HIS   A HE2  1 
ATOM   1116 H  HE2  B HIS   A 1 45  ? 30.009 5.373   3.619   0.40 10.53 ?  45  HIS   A HE2  1 
ATOM   1117 N  N    A GLY   A 1 46  ? 24.546 8.929   -0.554  0.60 11.46 ?  46  GLY   A N    1 
ATOM   1118 N  N    B GLY   A 1 46  ? 24.301 8.778   -0.498  0.40 11.72 ?  46  GLY   A N    1 
ATOM   1119 C  CA   A GLY   A 1 46  ? 23.755 10.097  -0.894  0.60 11.91 ?  46  GLY   A CA   1 
ATOM   1120 C  CA   B GLY   A 1 46  ? 23.457 9.899   -0.860  0.40 11.74 ?  46  GLY   A CA   1 
ATOM   1121 C  C    A GLY   A 1 46  ? 22.259 9.966   -0.681  0.60 11.72 ?  46  GLY   A C    1 
ATOM   1122 C  C    B GLY   A 1 46  ? 22.011 9.781   -0.430  0.40 11.48 ?  46  GLY   A C    1 
ATOM   1123 O  O    A GLY   A 1 46  ? 21.577 10.964  -0.430  0.60 12.23 ?  46  GLY   A O    1 
ATOM   1124 O  O    B GLY   A 1 46  ? 21.419 10.754  0.048   0.40 11.82 ?  46  GLY   A O    1 
ATOM   1125 H  H    A GLY   A 1 46  ? 24.666 8.382   -1.201  0.60 13.91 ?  46  GLY   A H    1 
ATOM   1126 H  H    B GLY   A 1 46  ? 24.268 8.111   -1.043  0.40 14.23 ?  46  GLY   A H    1 
ATOM   1127 H  HA2  A GLY   A 1 46  ? 24.069 10.852  -0.367  0.60 14.45 ?  46  GLY   A HA2  1 
ATOM   1128 H  HA2  B GLY   A 1 46  ? 23.806 10.705  -0.454  0.40 14.25 ?  46  GLY   A HA2  1 
ATOM   1129 H  HA3  A GLY   A 1 46  ? 23.899 10.308  -1.828  0.60 14.45 ?  46  GLY   A HA3  1 
ATOM   1130 H  HA3  B GLY   A 1 46  ? 23.477 10.011  -1.819  0.40 14.25 ?  46  GLY   A HA3  1 
ATOM   1131 N  N    A GLY   A 1 47  ? 21.728 8.755   -0.801  0.60 11.15 ?  47  GLY   A N    1 
ATOM   1132 N  N    B GLY   A 1 47  ? 21.429 8.598   -0.593  0.40 11.51 ?  47  GLY   A N    1 
ATOM   1133 C  CA   A GLY   A 1 47  ? 20.293 8.553   -0.762  0.60 11.07 ?  47  GLY   A CA   1 
ATOM   1134 C  CA   B GLY   A 1 47  ? 20.007 8.434   -0.369  0.40 11.34 ?  47  GLY   A CA   1 
ATOM   1135 C  C    A GLY   A 1 47  ? 19.976 7.113   -0.421  0.60 10.57 ?  47  GLY   A C    1 
ATOM   1136 C  C    B GLY   A 1 47  ? 19.676 7.001   -0.020  0.40 10.28 ?  47  GLY   A C    1 
ATOM   1137 O  O    A GLY   A 1 47  ? 20.867 6.292   -0.192  0.60 11.01 ?  47  GLY   A O    1 
ATOM   1138 O  O    B GLY   A 1 47  ? 20.559 6.153   0.136   0.40 10.16 ?  47  GLY   A O    1 
ATOM   1139 H  H    A GLY   A 1 47  ? 22.181 8.040   -0.894  0.60 13.55 ?  47  GLY   A H    1 
ATOM   1140 H  H    B GLY   A 1 47  ? 21.837 7.878   -0.818  0.40 13.97 ?  47  GLY   A H    1 
ATOM   1141 H  HA2  A GLY   A 1 47  ? 19.887 9.142   -0.102  0.60 13.45 ?  47  GLY   A HA2  1 
ATOM   1142 H  HA2  B GLY   A 1 47  ? 19.721 8.990   0.368   0.40 13.77 ?  47  GLY   A HA2  1 
ATOM   1143 H  HA3  A GLY   A 1 47  ? 19.911 8.751   -1.631  0.60 13.45 ?  47  GLY   A HA3  1 
ATOM   1144 H  HA3  B GLY   A 1 47  ? 19.516 8.692   -1.166  0.40 13.77 ?  47  GLY   A HA3  1 
ATOM   1145 N  N    A GLY   A 1 48  ? 18.685 6.803   -0.412  0.60 10.38 ?  48  GLY   A N    1 
ATOM   1146 N  N    B GLY   A 1 48  ? 18.377 6.738   0.100   0.40 10.31 ?  48  GLY   A N    1 
ATOM   1147 C  CA   A GLY   A 1 48  ? 18.279 5.465   -0.053  0.60 10.45 ?  48  GLY   A CA   1 
ATOM   1148 C  CA   B GLY   A 1 48  ? 17.949 5.414   0.512   0.40 9.72  ?  48  GLY   A CA   1 
ATOM   1149 C  C    A GLY   A 1 48  ? 18.671 5.144   1.374   0.60 10.46 ?  48  GLY   A C    1 
ATOM   1150 C  C    B GLY   A 1 48  ? 18.559 5.040   1.848   0.40 9.65  ?  48  GLY   A C    1 
ATOM   1151 O  O    A GLY   A 1 48  ? 18.819 6.032   2.225   0.60 10.69 ?  48  GLY   A O    1 
ATOM   1152 O  O    B GLY   A 1 48  ? 18.728 5.878   2.746   0.40 9.77  ?  48  GLY   A O    1 
ATOM   1153 H  H    A GLY   A 1 48  ? 18.048 7.338   -0.604  0.60 12.62 ?  48  GLY   A H    1 
ATOM   1154 H  H    B GLY   A 1 48  ? 17.730 7.297   -0.049  0.40 12.54 ?  48  GLY   A H    1 
ATOM   1155 H  HA2  A GLY   A 1 48  ? 17.323 5.373   -0.140  0.60 12.70 ?  48  GLY   A HA2  1 
ATOM   1156 H  HA2  B GLY   A 1 48  ? 16.978 5.384   0.581   0.40 11.82 ?  48  GLY   A HA2  1 
ATOM   1157 H  HA3  A GLY   A 1 48  ? 18.714 4.820   -0.634  0.60 12.70 ?  48  GLY   A HA3  1 
ATOM   1158 H  HA3  B GLY   A 1 48  ? 18.226 4.756   -0.149  0.40 11.82 ?  48  GLY   A HA3  1 
ATOM   1159 N  N    A VAL   A 1 49  ? 18.850 3.847   1.642   0.60 10.79 ?  49  VAL   A N    1 
ATOM   1160 N  N    B VAL   A 1 49  ? 18.899 3.757   1.979   0.40 9.58  ?  49  VAL   A N    1 
ATOM   1161 C  CA   A VAL   A 1 49  ? 19.284 3.418   2.968   0.60 11.32 ?  49  VAL   A CA   1 
ATOM   1162 C  CA   B VAL   A 1 49  ? 19.509 3.254   3.206   0.40 9.82  ?  49  VAL   A CA   1 
ATOM   1163 C  C    A VAL   A 1 49  ? 20.614 4.066   3.338   0.60 10.37 ?  49  VAL   A C    1 
ATOM   1164 C  C    B VAL   A 1 49  ? 20.774 4.036   3.541   0.40 9.29  ?  49  VAL   A C    1 
ATOM   1165 O  O    A VAL   A 1 49  ? 20.811 4.487   4.481   0.60 10.72 ?  49  VAL   A O    1 
ATOM   1166 O  O    B VAL   A 1 49  ? 20.978 4.453   4.687   0.40 9.48  ?  49  VAL   A O    1 
ATOM   1167 C  CB   A VAL   A 1 49  ? 19.353 1.879   3.045   0.60 12.52 ?  49  VAL   A CB   1 
ATOM   1168 C  CB   B VAL   A 1 49  ? 19.800 1.748   3.071   0.40 9.93  ?  49  VAL   A CB   1 
ATOM   1169 C  CG1  A VAL   A 1 49  ? 20.085 1.436   4.308   0.60 12.81 ?  49  VAL   A CG1  1 
ATOM   1170 C  CG1  B VAL   A 1 49  ? 20.646 1.277   4.241   0.40 9.55  ?  49  VAL   A CG1  1 
ATOM   1171 C  CG2  A VAL   A 1 49  ? 17.950 1.276   3.006   0.60 13.95 ?  49  VAL   A CG2  1 
ATOM   1172 C  CG2  B VAL   A 1 49  ? 18.500 0.946   2.962   0.40 9.97  ?  49  VAL   A CG2  1 
ATOM   1173 H  H    A VAL   A 1 49  ? 18.732 3.200   1.084   0.60 13.11 ?  49  VAL   A H    1 
ATOM   1174 H  H    B VAL   A 1 49  ? 18.788 3.160   1.370   0.40 11.66 ?  49  VAL   A H    1 
ATOM   1175 H  HA   A VAL   A 1 49  ? 18.629 3.701   3.622   0.60 13.74 ?  49  VAL   A HA   1 
ATOM   1176 H  HA   B VAL   A 1 49  ? 18.888 3.371   3.940   0.40 11.95 ?  49  VAL   A HA   1 
ATOM   1177 H  HB   A VAL   A 1 49  ? 19.852 1.538   2.284   0.60 15.19 ?  49  VAL   A HB   1 
ATOM   1178 H  HB   B VAL   A 1 49  ? 20.305 1.599   2.257   0.40 12.08 ?  49  VAL   A HB   1 
ATOM   1179 H  HG11 A VAL   A 1 49  ? 19.878 0.505   4.484   0.60 15.54 ?  49  VAL   A HG11 1 
ATOM   1180 H  HG11 B VAL   A 1 49  ? 20.571 0.314   4.320   0.40 11.63 ?  49  VAL   A HG11 1 
ATOM   1181 H  HG12 A VAL   A 1 49  ? 21.039 1.544   4.181   0.60 15.54 ?  49  VAL   A HG12 1 
ATOM   1182 H  HG12 B VAL   A 1 49  ? 21.574 1.521   4.082   0.40 11.63 ?  49  VAL   A HG12 1 
ATOM   1183 H  HG13 A VAL   A 1 49  ? 19.784 1.984   5.052   0.60 15.54 ?  49  VAL   A HG13 1 
ATOM   1184 H  HG13 B VAL   A 1 49  ? 20.328 1.700   5.054   0.40 11.63 ?  49  VAL   A HG13 1 
ATOM   1185 H  HG21 A VAL   A 1 49  ? 18.018 0.309   3.049   0.60 16.90 ?  49  VAL   A HG21 1 
ATOM   1186 H  HG21 B VAL   A 1 49  ? 18.712 0.004   2.876   0.40 12.13 ?  49  VAL   A HG21 1 
ATOM   1187 H  HG22 A VAL   A 1 49  ? 17.446 1.606   3.766   0.60 16.90 ?  49  VAL   A HG22 1 
ATOM   1188 H  HG22 B VAL   A 1 49  ? 17.969 1.093   3.762   0.40 12.13 ?  49  VAL   A HG22 1 
ATOM   1189 H  HG23 A VAL   A 1 49  ? 17.521 1.543   2.180   0.60 16.90 ?  49  VAL   A HG23 1 
ATOM   1190 H  HG23 B VAL   A 1 49  ? 18.006 1.246   2.181   0.40 12.13 ?  49  VAL   A HG23 1 
ATOM   1191 N  N    A ALA   A 1 50  ? 21.557 4.122   2.393   0.60 10.12 ?  50  ALA   A N    1 
ATOM   1192 N  N    B ALA   A 1 50  ? 21.658 4.213   2.556   0.40 9.31  ?  50  ALA   A N    1 
ATOM   1193 C  CA   A ALA   A 1 50  ? 22.883 4.660   2.688   0.60 9.98  ?  50  ALA   A CA   1 
ATOM   1194 C  CA   B ALA   A 1 50  ? 22.963 4.801   2.837   0.40 9.29  ?  50  ALA   A CA   1 
ATOM   1195 C  C    A ALA   A 1 50  ? 22.806 6.124   3.094   0.60 9.79  ?  50  ALA   A C    1 
ATOM   1196 C  C    B ALA   A 1 50  ? 22.827 6.246   3.292   0.40 8.98  ?  50  ALA   A C    1 
ATOM   1197 O  O    A ALA   A 1 50  ? 23.461 6.550   4.049   0.60 10.28 ?  50  ALA   A O    1 
ATOM   1198 O  O    B ALA   A 1 50  ? 23.425 6.651   4.296   0.40 8.87  ?  50  ALA   A O    1 
ATOM   1199 C  CB   A ALA   A 1 50  ? 23.781 4.512   1.465   0.60 9.97  ?  50  ALA   A CB   1 
ATOM   1200 C  CB   B ALA   A 1 50  ? 23.855 4.705   1.602   0.40 9.23  ?  50  ALA   A CB   1 
ATOM   1201 H  H    A ALA   A 1 50  ? 21.456 3.852   1.589   0.60 12.31 ?  50  ALA   A H    1 
ATOM   1202 H  H    B ALA   A 1 50  ? 21.524 4.013   1.727   0.40 11.34 ?  50  ALA   A H    1 
ATOM   1203 H  HA   A ALA   A 1 50  ? 23.280 4.164   3.428   0.60 12.14 ?  50  ALA   A HA   1 
ATOM   1204 H  HA   B ALA   A 1 50  ? 23.382 4.303   3.554   0.40 11.31 ?  50  ALA   A HA   1 
ATOM   1205 H  HB1  A ALA   A 1 50  ? 24.655 4.876   1.673   0.60 12.13 ?  50  ALA   A HB1  1 
ATOM   1206 H  HB1  B ALA   A 1 50  ? 24.717 5.097   1.807   0.40 11.24 ?  50  ALA   A HB1  1 
ATOM   1207 H  HB2  A ALA   A 1 50  ? 23.851 3.576   1.238   0.60 12.13 ?  50  ALA   A HB2  1 
ATOM   1208 H  HB2  B ALA   A 1 50  ? 23.961 3.771   1.364   0.40 11.24 ?  50  ALA   A HB2  1 
ATOM   1209 H  HB3  A ALA   A 1 50  ? 23.382 5.007   0.731   0.60 12.13 ?  50  ALA   A HB3  1 
ATOM   1210 H  HB3  B ALA   A 1 50  ? 23.435 5.188   0.873   0.40 11.24 ?  50  ALA   A HB3  1 
ATOM   1211 N  N    A GLY   A 1 51  ? 22.029 6.919   2.362   0.60 9.68  ?  51  GLY   A N    1 
ATOM   1212 N  N    B GLY   A 1 51  ? 22.041 7.041   2.566   0.40 9.47  ?  51  GLY   A N    1 
ATOM   1213 C  CA   A GLY   A 1 51  ? 21.898 8.318   2.724   0.60 9.89  ?  51  GLY   A CA   1 
ATOM   1214 C  CA   B GLY   A 1 51  ? 21.834 8.418   2.979   0.40 9.60  ?  51  GLY   A CA   1 
ATOM   1215 C  C    A GLY   A 1 51  ? 21.285 8.497   4.099   0.60 9.72  ?  51  GLY   A C    1 
ATOM   1216 C  C    B GLY   A 1 51  ? 21.220 8.511   4.363   0.40 10.12 ?  51  GLY   A C    1 
ATOM   1217 O  O    A GLY   A 1 51  ? 21.671 9.397   4.849   0.60 10.16 ?  51  GLY   A O    1 
ATOM   1218 O  O    B GLY   A 1 51  ? 21.582 9.382   5.159   0.40 10.55 ?  51  GLY   A O    1 
ATOM   1219 H  H    A GLY   A 1 51  ? 21.592 6.673   1.669   0.60 11.78 ?  51  GLY   A H    1 
ATOM   1220 H  H    B GLY   A 1 51  ? 21.627 6.807   1.846   0.40 11.53 ?  51  GLY   A H    1 
ATOM   1221 H  HA2  A GLY   A 1 51  ? 22.775 8.734   2.724   0.60 12.04 ?  51  GLY   A HA2  1 
ATOM   1222 H  HA2  B GLY   A 1 51  ? 22.687 8.882   2.981   0.40 11.68 ?  51  GLY   A HA2  1 
ATOM   1223 H  HA3  A GLY   A 1 51  ? 21.341 8.767   2.075   0.60 12.04 ?  51  GLY   A HA3  1 
ATOM   1224 H  HA3  B GLY   A 1 51  ? 21.249 8.860   2.339   0.40 11.68 ?  51  GLY   A HA3  1 
ATOM   1225 N  N    A ALA   A 1 52  ? 20.311 7.648   4.444   0.60 10.19 ?  52  ALA   A N    1 
ATOM   1226 N  N    B ALA   A 1 52  ? 20.288 7.607   4.672   0.40 10.37 ?  52  ALA   A N    1 
ATOM   1227 C  CA   A ALA   A 1 52  ? 19.658 7.747   5.746   0.60 10.70 ?  52  ALA   A CA   1 
ATOM   1228 C  CA   B ALA   A 1 52  ? 19.637 7.629   5.977   0.40 10.43 ?  52  ALA   A CA   1 
ATOM   1229 C  C    A ALA   A 1 52  ? 20.593 7.330   6.881   0.60 10.27 ?  52  ALA   A C    1 
ATOM   1230 C  C    B ALA   A 1 52  ? 20.596 7.200   7.084   0.40 9.92  ?  52  ALA   A C    1 
ATOM   1231 O  O    A ALA   A 1 52  ? 20.666 8.004   7.913   0.60 11.10 ?  52  ALA   A O    1 
ATOM   1232 O  O    B ALA   A 1 52  ? 20.650 7.828   8.148   0.40 10.80 ?  52  ALA   A O    1 
ATOM   1233 C  CB   A ALA   A 1 52  ? 18.381 6.907   5.749   0.60 11.90 ?  52  ALA   A CB   1 
ATOM   1234 C  CB   B ALA   A 1 52  ? 18.389 6.746   5.947   0.40 11.56 ?  52  ALA   A CB   1 
ATOM   1235 H  H    A ALA   A 1 52  ? 20.027 7.005   3.949   0.60 12.40 ?  52  ALA   A H    1 
ATOM   1236 H  H    B ALA   A 1 52  ? 20.026 6.974   4.145   0.40 12.61 ?  52  ALA   A H    1 
ATOM   1237 H  HA   A ALA   A 1 52  ? 19.402 8.667   5.894   0.60 13.01 ?  52  ALA   A HA   1 
ATOM   1238 H  HA   B ALA   A 1 52  ? 19.357 8.534   6.162   0.40 12.68 ?  52  ALA   A HA   1 
ATOM   1239 H  HB1  A ALA   A 1 52  ? 17.951 6.983   6.617   0.60 14.45 ?  52  ALA   A HB1  1 
ATOM   1240 H  HB1  B ALA   A 1 52  ? 17.933 6.820   6.798   0.40 14.03 ?  52  ALA   A HB1  1 
ATOM   1241 H  HB2  A ALA   A 1 52  ? 17.782 7.235   5.057   0.60 14.45 ?  52  ALA   A HB2  1 
ATOM   1242 H  HB2  B ALA   A 1 52  ? 17.805 7.054   5.233   0.40 14.03 ?  52  ALA   A HB2  1 
ATOM   1243 H  HB3  A ALA   A 1 52  ? 18.606 5.979   5.575   0.60 14.45 ?  52  ALA   A HB3  1 
ATOM   1244 H  HB3  B ALA   A 1 52  ? 18.651 5.828   5.784   0.40 14.03 ?  52  ALA   A HB3  1 
ATOM   1245 N  N    A LEU   A 1 53  ? 21.302 6.208   6.723   0.60 10.31 ?  53  LEU   A N    1 
ATOM   1246 N  N    B LEU   A 1 53  ? 21.347 6.115   6.868   0.40 9.81  ?  53  LEU   A N    1 
ATOM   1247 C  CA   A LEU   A 1 53  ? 22.235 5.782   7.766   0.60 10.91 ?  53  LEU   A CA   1 
ATOM   1248 C  CA   B LEU   A 1 53  ? 22.370 5.739   7.842   0.40 9.70  ?  53  LEU   A CA   1 
ATOM   1249 C  C    A LEU   A 1 53  ? 23.322 6.825   7.972   0.60 10.35 ?  53  LEU   A C    1 
ATOM   1250 C  C    B LEU   A 1 53  ? 23.375 6.870   8.029   0.40 9.30  ?  53  LEU   A C    1 
ATOM   1251 O  O    A LEU   A 1 53  ? 23.700 7.125   9.109   0.60 11.36 ?  53  LEU   A O    1 
ATOM   1252 O  O    B LEU   A 1 53  ? 23.643 7.298   9.158   0.40 9.89  ?  53  LEU   A O    1 
ATOM   1253 C  CB   A LEU   A 1 53  ? 22.864 4.431   7.407   0.60 11.20 ?  53  LEU   A CB   1 
ATOM   1254 C  CB   B LEU   A 1 53  ? 23.086 4.453   7.414   0.40 9.61  ?  53  LEU   A CB   1 
ATOM   1255 C  CG   A LEU   A 1 53  ? 21.950 3.199   7.427   0.60 11.02 ?  53  LEU   A CG   1 
ATOM   1256 C  CG   B LEU   A 1 53  ? 22.330 3.123   7.515   0.40 9.62  ?  53  LEU   A CG   1 
ATOM   1257 C  CD1  A LEU   A 1 53  ? 22.683 1.991   6.865   0.60 11.14 ?  53  LEU   A CD1  1 
ATOM   1258 C  CD1  B LEU   A 1 53  ? 23.162 2.011   6.893   0.40 10.33 ?  53  LEU   A CD1  1 
ATOM   1259 C  CD2  A LEU   A 1 53  ? 21.451 2.901   8.829   0.60 11.98 ?  53  LEU   A CD2  1 
ATOM   1260 C  CD2  B LEU   A 1 53  ? 21.971 2.773   8.955   0.40 9.48  ?  53  LEU   A CD2  1 
ATOM   1261 H  H    A LEU   A 1 53  ? 21.267 5.694   6.041   0.60 12.53 ?  53  LEU   A H    1 
ATOM   1262 H  H    B LEU   A 1 53  ? 21.278 5.584   6.187   0.40 11.94 ?  53  LEU   A H    1 
ATOM   1263 H  HA   A LEU   A 1 53  ? 21.760 5.678   8.606   0.60 13.26 ?  53  LEU   A HA   1 
ATOM   1264 H  HA   B LEU   A 1 53  ? 21.942 5.572   8.694   0.40 11.80 ?  53  LEU   A HA   1 
ATOM   1265 H  HB2  A LEU   A 1 53  ? 23.232 4.497   6.512   0.60 13.60 ?  53  LEU   A HB2  1 
ATOM   1266 H  HB2  B LEU   A 1 53  ? 23.352 4.553   6.488   0.40 11.70 ?  53  LEU   A HB2  1 
ATOM   1267 H  HB3  A LEU   A 1 53  ? 23.586 4.254   8.033   0.60 13.60 ?  53  LEU   A HB3  1 
ATOM   1268 H  HB3  B LEU   A 1 53  ? 23.882 4.363   7.962   0.40 11.70 ?  53  LEU   A HB3  1 
ATOM   1269 H  HG   A LEU   A 1 53  ? 21.179 3.369   6.860   0.60 13.39 ?  53  LEU   A HG   1 
ATOM   1270 H  HG   B LEU   A 1 53  ? 21.508 3.188   7.009   0.40 11.71 ?  53  LEU   A HG   1 
ATOM   1271 H  HD11 A LEU   A 1 53  ? 22.089 1.225   6.884   0.60 13.54 ?  53  LEU   A HD11 1 
ATOM   1272 H  HD11 B LEU   A 1 53  ? 22.676 1.173   6.963   0.40 12.56 ?  53  LEU   A HD11 1 
ATOM   1273 H  HD12 A LEU   A 1 53  ? 22.951 2.179   5.952   0.60 13.54 ?  53  LEU   A HD12 1 
ATOM   1274 H  HD12 B LEU   A 1 53  ? 23.324 2.221   5.959   0.40 12.56 ?  53  LEU   A HD12 1 
ATOM   1275 H  HD13 A LEU   A 1 53  ? 23.466 1.817   7.411   0.60 13.54 ?  53  LEU   A HD13 1 
ATOM   1276 H  HD13 B LEU   A 1 53  ? 24.006 1.942   7.366   0.40 12.56 ?  53  LEU   A HD13 1 
ATOM   1277 H  HD21 A LEU   A 1 53  ? 20.924 2.086   8.809   0.60 14.54 ?  53  LEU   A HD21 1 
ATOM   1278 H  HD21 B LEU   A 1 53  ? 21.483 1.933   8.966   0.40 11.54 ?  53  LEU   A HD21 1 
ATOM   1279 H  HD22 A LEU   A 1 53  ? 22.214 2.786   9.416   0.60 14.54 ?  53  LEU   A HD22 1 
ATOM   1280 H  HD22 B LEU   A 1 53  ? 22.783 2.690   9.476   0.40 11.54 ?  53  LEU   A HD22 1 
ATOM   1281 H  HD23 A LEU   A 1 53  ? 20.906 3.641   9.134   0.60 14.54 ?  53  LEU   A HD23 1 
ATOM   1282 H  HD23 B LEU   A 1 53  ? 21.413 3.479   9.321   0.40 11.54 ?  53  LEU   A HD23 1 
ATOM   1283 N  N    A ASN   A 1 54  ? 23.839 7.385   6.884   0.60 9.85  ?  54  ASN   A N    1 
ATOM   1284 N  N    B ASN   A 1 54  ? 23.934 7.375   6.929   0.40 9.40  ?  54  ASN   A N    1 
ATOM   1285 C  CA   A ASN   A 1 54  ? 24.911 8.359   7.025   0.60 10.09 ?  54  ASN   A CA   1 
ATOM   1286 C  CA   B ASN   A 1 54  ? 24.958 8.404   7.054   0.40 9.68  ?  54  ASN   A CA   1 
ATOM   1287 C  C    A ASN   A 1 54  ? 24.421 9.620   7.737   0.60 10.69 ?  54  ASN   A C    1 
ATOM   1288 C  C    B ASN   A 1 54  ? 24.417 9.637   7.769   0.40 10.24 ?  54  ASN   A C    1 
ATOM   1289 O  O    A ASN   A 1 54  ? 25.129 10.178  8.585   0.60 11.23 ?  54  ASN   A O    1 
ATOM   1290 O  O    B ASN   A 1 54  ? 25.081 10.191  8.655   0.40 10.27 ?  54  ASN   A O    1 
ATOM   1291 C  CB   A ASN   A 1 54  ? 25.488 8.701   5.659   0.60 10.36 ?  54  ASN   A CB   1 
ATOM   1292 C  CB   B ASN   A 1 54  ? 25.521 8.793   5.691   0.40 9.66  ?  54  ASN   A CB   1 
ATOM   1293 C  CG   A ASN   A 1 54  ? 26.537 9.769   5.753   0.60 10.54 ?  54  ASN   A CG   1 
ATOM   1294 C  CG   B ASN   A 1 54  ? 26.483 9.951   5.797   0.40 9.53  ?  54  ASN   A CG   1 
ATOM   1295 O  OD1  A ASN   A 1 54  ? 27.532 9.605   6.466   0.60 10.60 ?  54  ASN   A OD1  1 
ATOM   1296 O  OD1  B ASN   A 1 54  ? 27.526 9.832   6.444   0.40 9.47  ?  54  ASN   A OD1  1 
ATOM   1297 N  ND2  A ASN   A 1 54  ? 26.331 10.878  5.059   0.60 10.85 ?  54  ASN   A ND2  1 
ATOM   1298 N  ND2  B ASN   A 1 54  ? 26.136 11.086  5.197   0.40 9.77  ?  54  ASN   A ND2  1 
ATOM   1299 H  H    A ASN   A 1 54  ? 23.588 7.221   6.080   0.60 11.99 ?  54  ASN   A H    1 
ATOM   1300 H  H    B ASN   A 1 54  ? 23.735 7.149   6.124   0.40 11.45 ?  54  ASN   A H    1 
ATOM   1301 H  HA   A ASN   A 1 54  ? 25.617 7.967   7.560   0.60 12.27 ?  54  ASN   A HA   1 
ATOM   1302 H  HA   B ASN   A 1 54  ? 25.683 8.055   7.588   0.40 11.78 ?  54  ASN   A HA   1 
ATOM   1303 H  HB2  A ASN   A 1 54  ? 25.895 7.900   5.281   0.60 12.59 ?  54  ASN   A HB2  1 
ATOM   1304 H  HB2  B ASN   A 1 54  ? 26.001 8.033   5.323   0.40 11.76 ?  54  ASN   A HB2  1 
ATOM   1305 H  HB3  A ASN   A 1 54  ? 24.778 9.016   5.083   0.60 12.59 ?  54  ASN   A HB3  1 
ATOM   1306 H  HB3  B ASN   A 1 54  ? 24.794 9.048   5.105   0.40 11.76 ?  54  ASN   A HB3  1 
ATOM   1307 H  HD21 A ASN   A 1 54  ? 26.906 11.512  5.091   0.60 13.19 ?  54  ASN   A HD21 1 
ATOM   1308 H  HD21 B ASN   A 1 54  ? 26.650 11.775  5.245   0.40 11.89 ?  54  ASN   A HD21 1 
ATOM   1309 H  HD22 A ASN   A 1 54  ? 25.622 10.954  4.581   0.60 13.19 ?  54  ASN   A HD22 1 
ATOM   1310 H  HD22 B ASN   A 1 54  ? 25.399 11.131  4.757   0.40 11.89 ?  54  ASN   A HD22 1 
ATOM   1311 N  N    . LYS   A 1 55  ? 23.209 10.080  7.407   1.00 10.76 ?  55  LYS   A N    1 
ATOM   1312 C  CA   . LYS   A 1 55  ? 22.625 11.235  8.081   1.00 11.42 ?  55  LYS   A CA   1 
ATOM   1313 C  C    . LYS   A 1 55  ? 22.528 10.998  9.581   1.00 11.49 ?  55  LYS   A C    1 
ATOM   1314 O  O    . LYS   A 1 55  ? 22.805 11.901  10.381  1.00 12.37 ?  55  LYS   A O    1 
ATOM   1315 C  CB   . LYS   A 1 55  ? 21.257 11.544  7.472   1.00 12.13 ?  55  LYS   A CB   1 
ATOM   1316 C  CG   . LYS   A 1 55  ? 20.503 12.696  8.122   1.00 13.68 ?  55  LYS   A CG   1 
ATOM   1317 C  CD   . LYS   A 1 55  ? 19.184 12.960  7.385   1.00 15.40 ?  55  LYS   A CD   1 
ATOM   1318 C  CE   . LYS   A 1 55  ? 18.322 14.016  8.067   1.00 17.49 ?  55  LYS   A CE   1 
ATOM   1319 N  NZ   . LYS   A 1 55  ? 16.993 14.171  7.393   1.00 18.29 ?  55  LYS   A NZ   1 
ATOM   1320 H  H    A LYS   A 1 55  ? 22.707 9.737   6.796   0.60 13.08 ?  55  LYS   A H    1 
ATOM   1321 H  H    B LYS   A 1 55  ? 22.708 9.719   6.805   0.40 13.08 ?  55  LYS   A H    1 
ATOM   1322 H  HA   . LYS   A 1 55  ? 23.194 12.003  7.937   1.00 13.87 ?  55  LYS   A HA   1 
ATOM   1323 H  HB2  . LYS   A 1 55  ? 21.377 11.773  6.537   1.00 14.72 ?  55  LYS   A HB2  1 
ATOM   1324 H  HB3  . LYS   A 1 55  ? 20.696 10.756  7.544   1.00 14.72 ?  55  LYS   A HB3  1 
ATOM   1325 H  HG2  . LYS   A 1 55  ? 20.295 12.470  9.044   1.00 16.58 ?  55  LYS   A HG2  1 
ATOM   1326 H  HG3  . LYS   A 1 55  ? 21.043 13.500  8.085   1.00 16.58 ?  55  LYS   A HG3  1 
ATOM   1327 H  HD2  . LYS   A 1 55  ? 19.386 13.267  6.487   1.00 18.64 ?  55  LYS   A HD2  1 
ATOM   1328 H  HD3  . LYS   A 1 55  ? 18.677 12.134  7.346   1.00 18.64 ?  55  LYS   A HD3  1 
ATOM   1329 H  HE2  . LYS   A 1 55  ? 18.167 13.754  8.988   1.00 21.15 ?  55  LYS   A HE2  1 
ATOM   1330 H  HE3  . LYS   A 1 55  ? 18.780 14.870  8.035   1.00 21.15 ?  55  LYS   A HE3  1 
ATOM   1331 H  HZ1  . LYS   A 1 55  ? 16.406 14.530  7.957   1.00 22.12 ?  55  LYS   A HZ1  1 
ATOM   1332 H  HZ2  . LYS   A 1 55  ? 17.069 14.701  6.682   1.00 22.12 ?  55  LYS   A HZ2  1 
ATOM   1333 H  HZ3  . LYS   A 1 55  ? 16.687 13.375  7.131   1.00 22.12 ?  55  LYS   A HZ3  1 
ATOM   1334 N  N    . ALA   A 1 56  ? 22.142 9.782   9.982   1.00 11.70 ?  56  ALA   A N    1 
ATOM   1335 C  CA   . ALA   A 1 56  ? 22.020 9.456   11.398  1.00 12.57 ?  56  ALA   A CA   1 
ATOM   1336 C  C    . ALA   A 1 56  ? 23.361 9.485   12.124  1.00 12.51 ?  56  ALA   A C    1 
ATOM   1337 O  O    . ALA   A 1 56  ? 23.383 9.675   13.343  1.00 13.98 ?  56  ALA   A O    1 
ATOM   1338 C  CB   . ALA   A 1 56  ? 21.321 8.102   11.573  1.00 13.44 ?  56  ALA   A CB   1 
ATOM   1339 H  H    . ALA   A 1 56  ? 21.942 9.137   9.450   1.00 14.20 ?  56  ALA   A H    1 
ATOM   1340 H  HA   . ALA   A 1 56  ? 21.461 10.117  11.818  1.00 15.25 ?  56  ALA   A HA   1 
ATOM   1341 H  HB1  . ALA   A 1 56  ? 21.251 7.899   12.522  1.00 16.30 ?  56  ALA   A HB1  1 
ATOM   1342 H  HB2  . ALA   A 1 56  ? 20.429 8.152   11.186  1.00 16.30 ?  56  ALA   A HB2  1 
ATOM   1343 H  HB3  . ALA   A 1 56  ? 21.833 7.410   11.127  1.00 16.30 ?  56  ALA   A HB3  1 
ATOM   1344 N  N    . THR   A 1 57  ? 24.475 9.304   11.407  1.00 11.50 ?  57  THR   A N    1 
ATOM   1345 C  CA   . THR   A 1 57  ? 25.817 9.431   11.983  1.00 11.27 ?  57  THR   A CA   1 
ATOM   1346 C  C    . THR   A 1 57  ? 26.367 10.849  11.903  1.00 11.77 ?  57  THR   A C    1 
ATOM   1347 O  O    . THR   A 1 57  ? 27.551 11.056  12.192  1.00 12.31 ?  57  THR   A O    1 
ATOM   1348 C  CB   . THR   A 1 57  ? 26.829 8.482   11.310  1.00 11.32 ?  57  THR   A CB   1 
ATOM   1349 O  OG1  . THR   A 1 57  ? 27.212 8.986   10.019  1.00 11.15 ?  57  THR   A OG1  1 
ATOM   1350 C  CG2  . THR   A 1 57  ? 26.298 7.065   11.198  1.00 11.20 ?  57  THR   A CG2  1 
ATOM   1351 H  H    . THR   A 1 57  ? 24.480 9.087   10.569  1.00 13.96 ?  57  THR   A H    1 
ATOM   1352 H  HA   . THR   A 1 57  ? 25.768 9.173   12.920  1.00 13.68 ?  57  THR   A HA   1 
ATOM   1353 H  HB   . THR   A 1 57  ? 27.626 8.438   11.869  1.00 13.75 ?  57  THR   A HB   1 
ATOM   1354 H  HG1  . THR   A 1 57  ? 26.536 9.055   9.528   1.00 13.54 ?  57  THR   A HG1  1 
ATOM   1355 H  HG21 . THR   A 1 57  ? 26.978 6.477   10.827  1.00 13.60 ?  57  THR   A HG21 1 
ATOM   1356 H  HG22 . THR   A 1 57  ? 26.039 6.730   12.070  1.00 13.60 ?  57  THR   A HG22 1 
ATOM   1357 H  HG23 . THR   A 1 57  ? 25.523 7.044   10.614  1.00 13.60 ?  57  THR   A HG23 1 
ATOM   1358 N  N    . ASN   A 1 58  ? 25.552 11.824  11.502  1.00 12.37 ?  58  ASN   A N    1 
ATOM   1359 C  CA   . ASN   A 1 58  ? 26.015 13.204  11.404  1.00 13.26 ?  58  ASN   A CA   1 
ATOM   1360 C  C    . ASN   A 1 58  ? 27.166 13.326  10.398  1.00 12.07 ?  58  ASN   A C    1 
ATOM   1361 O  O    . ASN   A 1 58  ? 28.061 14.161  10.553  1.00 12.88 ?  58  ASN   A O    1 
ATOM   1362 C  CB   . ASN   A 1 58  ? 26.384 13.738  12.800  1.00 15.73 ?  58  ASN   A CB   1 
ATOM   1363 C  CG   . ASN   A 1 58  ? 26.795 15.193  12.799  1.00 19.62 ?  58  ASN   A CG   1 
ATOM   1364 O  OD1  . ASN   A 1 58  ? 26.168 16.023  12.148  1.00 21.32 ?  58  ASN   A OD1  1 
ATOM   1365 N  ND2  . ASN   A 1 58  ? 27.851 15.516  13.548  1.00 21.20 ?  58  ASN   A ND2  1 
ATOM   1366 H  H    . ASN   A 1 58  ? 24.728 11.698  11.275  1.00 15.01 ?  58  ASN   A H    1 
ATOM   1367 H  HA   . ASN   A 1 58  ? 25.279 13.737  11.075  1.00 16.07 ?  58  ASN   A HA   1 
ATOM   1368 H  HB2  . ASN   A 1 58  ? 25.610 13.646  13.389  1.00 19.04 ?  58  ASN   A HB2  1 
ATOM   1369 H  HB3  . ASN   A 1 58  ? 27.123 13.226  13.157  1.00 19.04 ?  58  ASN   A HB3  1 
ATOM   1370 H  HD21 . ASN   A 1 58  ? 28.118 16.334  13.583  1.00 25.60 ?  58  ASN   A HD21 1 
ATOM   1371 H  HD22 . ASN   A 1 58  ? 28.255 14.909  13.996  1.00 25.60 ?  58  ASN   A HD22 1 
ATOM   1372 N  N    . ASN   A 1 59  ? 27.145 12.506  9.346   1.00 11.10 ?  59  ASN   A N    1 
ATOM   1373 C  CA   . ASN   A 1 59  ? 28.122 12.485  8.252   1.00 10.72 ?  59  ASN   A CA   1 
ATOM   1374 C  C    . ASN   A 1 59  ? 29.441 11.804  8.635   1.00 10.57 ?  59  ASN   A C    1 
ATOM   1375 O  O    . ASN   A 1 59  ? 30.359 11.762  7.807   1.00 10.95 ?  59  ASN   A O    1 
ATOM   1376 C  CB   . ASN   A 1 59  ? 28.405 13.874  7.650   1.00 11.25 ?  59  ASN   A CB   1 
ATOM   1377 C  CG   . ASN   A 1 59  ? 28.770 13.810  6.180   1.00 11.76 ?  59  ASN   A CG   1 
ATOM   1378 O  OD1  . ASN   A 1 59  ? 28.070 13.188  5.376   1.00 11.66 ?  59  ASN   A OD1  1 
ATOM   1379 N  ND2  . ASN   A 1 59  ? 29.859 14.473  5.814   1.00 11.93 ?  59  ASN   A ND2  1 
ATOM   1380 H  H    . ASN   A 1 59  ? 26.530 11.911  9.235   1.00 13.49 ?  59  ASN   A H    1 
ATOM   1381 H  HA   . ASN   A 1 59  ? 27.739 11.958  7.539   1.00 13.03 ?  59  ASN   A HA   1 
ATOM   1382 H  HB2  . ASN   A 1 59  ? 27.613 14.429  7.734   1.00 13.67 ?  59  ASN   A HB2  1 
ATOM   1383 H  HB3  . ASN   A 1 59  ? 29.148 14.283  8.118   1.00 13.67 ?  59  ASN   A HB3  1 
ATOM   1384 H  HD21 . ASN   A 1 59  ? 30.108 14.479  4.988   1.00 14.48 ?  59  ASN   A HD21 1 
ATOM   1385 H  HD22 . ASN   A 1 59  ? 30.326 14.902  6.400   1.00 14.48 ?  59  ASN   A HD22 1 
ATOM   1386 N  N    . ALA   A 1 60  ? 29.568 11.259  9.843   1.00 10.76 ?  60  ALA   A N    1 
ATOM   1387 C  CA   . ALA   A 1 60  ? 30.807 10.575  10.199  1.00 10.83 ?  60  ALA   A CA   1 
ATOM   1388 C  C    . ALA   A 1 60  ? 31.030 9.339   9.338   1.00 10.79 ?  60  ALA   A C    1 
ATOM   1389 O  O    . ALA   A 1 60  ? 32.176 9.011   9.006   1.00 11.39 ?  60  ALA   A O    1 
ATOM   1390 C  CB   . ALA   A 1 60  ? 30.800 10.211  11.682  1.00 11.87 ?  60  ALA   A CB   1 
ATOM   1391 H  H    . ALA   A 1 60  ? 28.972 11.266  10.458  1.00 13.08 ?  60  ALA   A H    1 
ATOM   1392 H  HA   . ALA   A 1 60  ? 31.555 11.179  10.047  1.00 13.17 ?  60  ALA   A HA   1 
ATOM   1393 H  HB1  . ALA   A 1 60  ? 31.627 9.762   11.906  1.00 14.41 ?  60  ALA   A HB1  1 
ATOM   1394 H  HB2  . ALA   A 1 60  ? 30.714 11.027  12.206  1.00 14.41 ?  60  ALA   A HB2  1 
ATOM   1395 H  HB3  . ALA   A 1 60  ? 30.045 9.629   11.859  1.00 14.41 ?  60  ALA   A HB3  1 
ATOM   1396 N  N    . MET   A 1 61  ? 29.956 8.642   8.962   1.00 10.41 ?  61  MET   A N    1 
ATOM   1397 C  CA   . MET   A 1 61  ? 30.100 7.509   8.053   1.00 10.25 ?  61  MET   A CA   1 
ATOM   1398 C  C    . MET   A 1 61  ? 30.735 7.935   6.730   1.00 10.33 ?  61  MET   A C    1 
ATOM   1399 O  O    . MET   A 1 61  ? 31.627 7.250   6.209   1.00 10.70 ?  61  MET   A O    1 
ATOM   1400 C  CB   . MET   A 1 61  ? 28.738 6.848   7.834   1.00 10.21 ?  61  MET   A CB   1 
ATOM   1401 C  CG   . MET   A 1 61  ? 28.745 5.686   6.849   1.00 10.90 ?  61  MET   A CG   1 
ATOM   1402 S  SD   . MET   A 1 61  ? 27.120 4.936   6.645   1.00 11.99 ?  61  MET   A SD   1 
ATOM   1403 C  CE   . MET   A 1 61  ? 26.992 4.040   8.194   1.00 13.31 ?  61  MET   A CE   1 
ATOM   1404 H  H    . MET   A 1 61  ? 29.151 8.802   9.213   1.00 12.66 ?  61  MET   A H    1 
ATOM   1405 H  HA   . MET   A 1 61  ? 30.677 6.850   8.470   1.00 12.46 ?  61  MET   A HA   1 
ATOM   1406 H  HB2  . MET   A 1 61  ? 28.419 6.510   8.682   1.00 12.41 ?  61  MET   A HB2  1 
ATOM   1407 H  HB3  . MET   A 1 61  ? 28.122 7.514   7.493   1.00 12.41 ?  61  MET   A HB3  1 
ATOM   1408 H  HG2  . MET   A 1 61  ? 29.028 5.998   5.976   1.00 13.25 ?  61  MET   A HG2  1 
ATOM   1409 H  HG3  . MET   A 1 61  ? 29.345 4.996   7.168   1.00 13.25 ?  61  MET   A HG3  1 
ATOM   1410 H  HE1  . MET   A 1 61  ? 26.157 3.551   8.211   1.00 16.14 ?  61  MET   A HE1  1 
ATOM   1411 H  HE2  . MET   A 1 61  ? 27.739 3.420   8.259   1.00 16.14 ?  61  MET   A HE2  1 
ATOM   1412 H  HE3  . MET   A 1 61  ? 27.025 4.670   8.931   1.00 16.14 ?  61  MET   A HE3  1 
ATOM   1413 N  N    . GLN   A 1 62  ? 30.291 9.067   6.173   1.00 10.33 ?  62  GLN   A N    1 
ATOM   1414 C  CA   . GLN   A 1 62  ? 30.853 9.542   4.912   1.00 10.44 ?  62  GLN   A CA   1 
ATOM   1415 C  C    . GLN   A 1 62  ? 32.323 9.916   5.060   1.00 10.34 ?  62  GLN   A C    1 
ATOM   1416 O  O    . GLN   A 1 62  ? 33.134 9.604   4.181   1.00 10.75 ?  62  GLN   A O    1 
ATOM   1417 C  CB   . GLN   A 1 62  ? 30.047 10.723  4.376   1.00 10.36 ?  62  GLN   A CB   1 
ATOM   1418 C  CG   . GLN   A 1 62  ? 30.424 11.089  2.956   1.00 10.30 ?  62  GLN   A CG   1 
ATOM   1419 C  CD   . GLN   A 1 62  ? 30.094 9.961   2.006   1.00 10.85 ?  62  GLN   A CD   1 
ATOM   1420 O  OE1  . GLN   A 1 62  ? 28.919 9.655   1.792   1.00 11.44 ?  62  GLN   A OE1  1 
ATOM   1421 N  NE2  . GLN   A 1 62  ? 31.115 9.289   1.480   1.00 11.39 ?  62  GLN   A NE2  1 
ATOM   1422 H  H    . GLN   A 1 62  ? 29.669 9.560   6.501   1.00 12.56 ?  62  GLN   A H    1 
ATOM   1423 H  HA   . GLN   A 1 62  ? 30.801 8.822   4.264   1.00 12.70 ?  62  GLN   A HA   1 
ATOM   1424 H  HB2  . GLN   A 1 62  ? 29.103 10.495  4.389   1.00 12.60 ?  62  GLN   A HB2  1 
ATOM   1425 H  HB3  . GLN   A 1 62  ? 30.208 11.497  4.938   1.00 12.60 ?  62  GLN   A HB3  1 
ATOM   1426 H  HG2  . GLN   A 1 62  ? 29.920 11.868  2.680   1.00 12.52 ?  62  GLN   A HG2  1 
ATOM   1427 H  HG3  . GLN   A 1 62  ? 31.375 11.262  2.906   1.00 12.52 ?  62  GLN   A HG3  1 
ATOM   1428 H  HE21 . GLN   A 1 62  ? 31.920 9.516   1.668   1.00 13.83 ?  62  GLN   A HE21 1 
ATOM   1429 H  HE22 . GLN   A 1 62  ? 30.963 8.631   0.947   1.00 13.83 ?  62  GLN   A HE22 1 
ATOM   1430 N  N    . VAL   A 1 63  ? 32.682 10.600  6.151   1.00 10.97 ?  63  VAL   A N    1 
ATOM   1431 C  CA   . VAL   A 1 63  ? 34.075 10.989  6.365   1.00 11.81 ?  63  VAL   A CA   1 
ATOM   1432 C  C    . VAL   A 1 63  ? 34.969 9.751   6.422   1.00 11.09 ?  63  VAL   A C    1 
ATOM   1433 O  O    . VAL   A 1 63  ? 36.023 9.685   5.771   1.00 11.61 ?  63  VAL   A O    1 
ATOM   1434 C  CB   . VAL   A 1 63  ? 34.187 11.856  7.633   1.00 13.34 ?  63  VAL   A CB   1 
ATOM   1435 C  CG1  . VAL   A 1 63  ? 35.637 12.094  7.999   1.00 14.93 ?  63  VAL   A CG1  1 
ATOM   1436 C  CG2  . VAL   A 1 63  ? 33.462 13.185  7.416   1.00 13.67 ?  63  VAL   A CG2  1 
ATOM   1437 H  H    . VAL   A 1 63  ? 32.138 10.845  6.775   1.00 13.33 ?  63  VAL   A H    1 
ATOM   1438 H  HA   . VAL   A 1 63  ? 34.361 11.527  5.614   1.00 14.33 ?  63  VAL   A HA   1 
ATOM   1439 H  HB   . VAL   A 1 63  ? 33.759 11.398  8.374   1.00 16.18 ?  63  VAL   A HB   1 
ATOM   1440 H  HG11 . VAL   A 1 63  ? 35.684 12.821  8.638   1.00 18.08 ?  63  VAL   A HG11 1 
ATOM   1441 H  HG12 . VAL   A 1 63  ? 36.002 11.286  8.390   1.00 18.08 ?  63  VAL   A HG12 1 
ATOM   1442 H  HG13 . VAL   A 1 63  ? 36.129 12.329  7.196   1.00 18.08 ?  63  VAL   A HG13 1 
ATOM   1443 H  HG21 . VAL   A 1 63  ? 33.556 13.731  8.214   1.00 16.56 ?  63  VAL   A HG21 1 
ATOM   1444 H  HG22 . VAL   A 1 63  ? 33.861 13.642  6.657   1.00 16.56 ?  63  VAL   A HG22 1 
ATOM   1445 H  HG23 . VAL   A 1 63  ? 32.525 13.012  7.243   1.00 16.56 ?  63  VAL   A HG23 1 
ATOM   1446 N  N    . GLU   A 1 64  ? 34.547 8.742   7.189   1.00 10.93 ?  64  GLU   A N    1 
ATOM   1447 C  CA   . GLU   A 1 64  ? 35.315 7.506   7.285   1.00 11.07 ?  64  GLU   A CA   1 
ATOM   1448 C  C    . GLU   A 1 64  ? 35.401 6.817   5.931   1.00 10.64 ?  64  GLU   A C    1 
ATOM   1449 O  O    . GLU   A 1 64  ? 36.451 6.271   5.554   1.00 11.04 ?  64  GLU   A O    1 
ATOM   1450 C  CB   . GLU   A 1 64  ? 34.630 6.596   8.306   1.00 11.74 ?  64  GLU   A CB   1 
ATOM   1451 C  CG   . GLU   A 1 64  ? 35.288 5.247   8.469   1.00 12.55 ?  64  GLU   A CG   1 
ATOM   1452 C  CD   . GLU   A 1 64  ? 34.400 4.245   9.182   1.00 12.96 ?  64  GLU   A CD   1 
ATOM   1453 O  OE1  . GLU   A 1 64  ? 33.159 4.339   9.046   1.00 13.66 ?  64  GLU   A OE1  1 
ATOM   1454 O  OE2  . GLU   A 1 64  ? 34.945 3.349   9.866   1.00 13.20 -1 64  GLU   A OE2  1 
ATOM   1455 H  H    . GLU   A 1 64  ? 33.818 8.746   7.649   1.00 13.28 ?  64  GLU   A H    1 
ATOM   1456 H  HA   . GLU   A 1 64  ? 36.213 7.710   7.599   1.00 13.45 ?  64  GLU   A HA   1 
ATOM   1457 H  HB2  . GLU   A 1 64  ? 34.644 7.043   9.175   1.00 14.25 ?  64  GLU   A HB2  1 
ATOM   1458 H  HB3  . GLU   A 1 64  ? 33.713 6.461   8.029   1.00 14.25 ?  64  GLU   A HB3  1 
ATOM   1459 H  HG2  . GLU   A 1 64  ? 35.506 4.884   7.597   1.00 15.23 ?  64  GLU   A HG2  1 
ATOM   1460 H  HG3  . GLU   A 1 64  ? 36.096 5.353   8.993   1.00 15.23 ?  64  GLU   A HG3  1 
ATOM   1461 N  N    . SER   A 1 65  ? 34.287 6.814   5.195   1.00 10.29 ?  65  SER   A N    1 
ATOM   1462 C  CA   . SER   A 1 65  ? 34.237 6.156   3.897   1.00 10.41 ?  65  SER   A CA   1 
ATOM   1463 C  C    . SER   A 1 65  ? 35.161 6.825   2.888   1.00 10.77 ?  65  SER   A C    1 
ATOM   1464 O  O    . SER   A 1 65  ? 35.800 6.143   2.079   1.00 11.59 ?  65  SER   A O    1 
ATOM   1465 C  CB   . SER   A 1 65  ? 32.804 6.162   3.370   1.00 10.49 ?  65  SER   A CB   1 
ATOM   1466 O  OG   . SER   A 1 65  ? 31.949 5.349   4.164   1.00 10.89 ?  65  SER   A OG   1 
ATOM   1467 H  H    . SER   A 1 65  ? 33.552 7.189   5.430   1.00 12.52 ?  65  SER   A H    1 
ATOM   1468 H  HA   . SER   A 1 65  ? 34.524 5.237   3.997   1.00 12.66 ?  65  SER   A HA   1 
ATOM   1469 H  HB2  . SER   A 1 65  ? 32.469 7.070   3.384   1.00 12.75 ?  65  SER   A HB2  1 
ATOM   1470 H  HB3  . SER   A 1 65  ? 32.806 5.820   2.465   1.00 12.75 ?  65  SER   A HB3  1 
ATOM   1471 H  HG   . SER   A 1 65  ? 31.946 5.631   4.960   1.00 13.23 ?  65  SER   A HG   1 
ATOM   1472 N  N    . ASP   A 1 66  ? 35.232 8.158   2.903   1.00 10.89 ?  66  ASP   A N    1 
ATOM   1473 C  CA   . ASP   A 1 66  ? 36.091 8.853   1.951   1.00 11.91 ?  66  ASP   A CA   1 
ATOM   1474 C  C    . ASP   A 1 66  ? 37.555 8.500   2.191   1.00 11.57 ?  66  ASP   A C    1 
ATOM   1475 O  O    . ASP   A 1 66  ? 38.330 8.331   1.241   1.00 12.54 ?  66  ASP   A O    1 
ATOM   1476 C  CB   . ASP   A 1 66  ? 35.875 10.361  2.050   1.00 13.03 ?  66  ASP   A CB   1 
ATOM   1477 C  CG   . ASP   A 1 66  ? 34.535 10.819  1.456   1.00 14.67 ?  66  ASP   A CG   1 
ATOM   1478 O  OD1  . ASP   A 1 66  ? 33.819 10.020  0.811   1.00 15.04 ?  66  ASP   A OD1  1 
ATOM   1479 O  OD2  . ASP   A 1 66  ? 34.220 12.014  1.620   1.00 17.74 -1 66  ASP   A OD2  1 
ATOM   1480 H  H    . ASP   A 1 66  ? 34.796 8.675   3.440   1.00 13.23 ?  66  ASP   A H    1 
ATOM   1481 H  HA   . ASP   A 1 66  ? 35.856 8.574   1.053   1.00 14.45 ?  66  ASP   A HA   1 
ATOM   1482 H  HB2  . ASP   A 1 66  ? 35.894 10.622  2.984   1.00 15.80 ?  66  ASP   A HB2  1 
ATOM   1483 H  HB3  . ASP   A 1 66  ? 36.591 10.811  1.569   1.00 15.80 ?  66  ASP   A HB3  1 
ATOM   1484 N  N    . ASP   A 1 67  ? 37.950 8.369   3.457   1.00 11.84 ?  67  ASP   A N    1 
ATOM   1485 C  CA   . ASP   A 1 67  ? 39.305 7.922   3.759   1.00 12.68 ?  67  ASP   A CA   1 
ATOM   1486 C  C    . ASP   A 1 67  ? 39.526 6.488   3.288   1.00 12.67 ?  67  ASP   A C    1 
ATOM   1487 O  O    . ASP   A 1 67  ? 40.584 6.165   2.738   1.00 13.14 ?  67  ASP   A O    1 
ATOM   1488 C  CB   . ASP   A 1 67  ? 39.567 8.052   5.257   1.00 13.87 ?  67  ASP   A CB   1 
ATOM   1489 C  CG   . ASP   A 1 67  ? 40.866 7.397   5.682   1.00 15.08 ?  67  ASP   A CG   1 
ATOM   1490 O  OD1  . ASP   A 1 67  ? 41.936 8.034   5.552   1.00 17.88 ?  67  ASP   A OD1  1 
ATOM   1491 O  OD2  . ASP   A 1 67  ? 40.822 6.236   6.147   1.00 14.68 -1 67  ASP   A OD2  1 
ATOM   1492 H  H    . ASP   A 1 67  ? 37.466 8.529   4.143   1.00 14.37 ?  67  ASP   A H    1 
ATOM   1493 H  HA   . ASP   A 1 67  ? 39.940 8.488   3.289   1.00 15.37 ?  67  ASP   A HA   1 
ATOM   1494 H  HB2  . ASP   A 1 67  ? 39.617 8.988   5.485   1.00 16.81 ?  67  ASP   A HB2  1 
ATOM   1495 H  HB3  . ASP   A 1 67  ? 38.843 7.623   5.740   1.00 16.81 ?  67  ASP   A HB3  1 
ATOM   1496 N  N    . TYR   A 1 68  ? 38.536 5.612   3.485   1.00 11.91 ?  68  TYR   A N    1 
ATOM   1497 C  CA   . TYR   A 1 68  ? 38.657 4.233   3.012   1.00 11.90 ?  68  TYR   A CA   1 
ATOM   1498 C  C    . TYR   A 1 68  ? 38.898 4.183   1.504   1.00 11.80 ?  68  TYR   A C    1 
ATOM   1499 O  O    . TYR   A 1 68  ? 39.778 3.448   1.030   1.00 12.55 ?  68  TYR   A O    1 
ATOM   1500 C  CB   . TYR   A 1 68  ? 37.407 3.412   3.394   1.00 12.48 ?  68  TYR   A CB   1 
ATOM   1501 C  CG   . TYR   A 1 68  ? 37.433 2.023   2.770   1.00 13.54 ?  68  TYR   A CG   1 
ATOM   1502 C  CD1  . TYR   A 1 68  ? 36.978 1.825   1.472   1.00 15.04 ?  68  TYR   A CD1  1 
ATOM   1503 C  CD2  . TYR   A 1 68  ? 37.976 0.940   3.442   1.00 15.68 ?  68  TYR   A CD2  1 
ATOM   1504 C  CE1  . TYR   A 1 68  ? 37.043 0.607   0.862   1.00 16.73 ?  68  TYR   A CE1  1 
ATOM   1505 C  CE2  . TYR   A 1 68  ? 38.038 -0.321  2.831   1.00 16.35 ?  68  TYR   A CE2  1 
ATOM   1506 C  CZ   . TYR   A 1 68  ? 37.574 -0.462  1.538   1.00 16.85 ?  68  TYR   A CZ   1 
ATOM   1507 O  OH   . TYR   A 1 68  ? 37.643 -1.672  0.901   1.00 18.26 ?  68  TYR   A OH   1 
ATOM   1508 H  H    . TYR   A 1 68  ? 37.796 5.786   3.889   1.00 14.45 ?  68  TYR   A H    1 
ATOM   1509 H  HA   . TYR   A 1 68  ? 39.421 3.819   3.444   1.00 14.44 ?  68  TYR   A HA   1 
ATOM   1510 H  HB2  . TYR   A 1 68  ? 37.376 3.310   4.357   1.00 15.14 ?  68  TYR   A HB2  1 
ATOM   1511 H  HB3  . TYR   A 1 68  ? 36.615 3.871   3.077   1.00 15.14 ?  68  TYR   A HB3  1 
ATOM   1512 H  HD1  . TYR   A 1 68  ? 36.630 2.547   1.001   1.00 18.22 ?  68  TYR   A HD1  1 
ATOM   1513 H  HD2  . TYR   A 1 68  ? 38.309 1.049   4.301   1.00 18.98 ?  68  TYR   A HD2  1 
ATOM   1514 H  HE1  . TYR   A 1 68  ? 36.728 0.503   -0.007  1.00 20.24 ?  68  TYR   A HE1  1 
ATOM   1515 H  HE2  . TYR   A 1 68  ? 38.411 -1.047  3.275   1.00 19.79 ?  68  TYR   A HE2  1 
ATOM   1516 H  HH   . TYR   A 1 68  ? 37.985 -2.246  1.411   1.00 22.07 ?  68  TYR   A HH   1 
ATOM   1517 N  N    . ILE   A 1 69  ? 38.108 4.941   0.733   1.00 11.26 ?  69  ILE   A N    1 
ATOM   1518 C  CA   . ILE   A 1 69  ? 38.243 4.932   -0.723  1.00 11.60 ?  69  ILE   A CA   1 
ATOM   1519 C  C    . ILE   A 1 69  ? 39.574 5.539   -1.154  1.00 11.56 ?  69  ILE   A C    1 
ATOM   1520 O  O    . ILE   A 1 69  ? 40.213 5.054   -2.094  1.00 12.12 ?  69  ILE   A O    1 
ATOM   1521 C  CB   . ILE   A 1 69  ? 37.044 5.644   -1.386  1.00 12.28 ?  69  ILE   A CB   1 
ATOM   1522 C  CG1  . ILE   A 1 69  ? 35.732 4.910   -1.104  1.00 12.90 ?  69  ILE   A CG1  1 
ATOM   1523 C  CG2  . ILE   A 1 69  ? 37.274 5.826   -2.892  1.00 13.65 ?  69  ILE   A CG2  1 
ATOM   1524 C  CD1  . ILE   A 1 69  ? 35.575 3.602   -1.849  1.00 13.63 ?  69  ILE   A CD1  1 
ATOM   1525 H  H    . ILE   A 1 69  ? 37.497 5.469   1.028   1.00 13.68 ?  69  ILE   A H    1 
ATOM   1526 H  HA   . ILE   A 1 69  ? 38.237 4.009   -1.024  1.00 14.08 ?  69  ILE   A HA   1 
ATOM   1527 H  HB   . ILE   A 1 69  ? 36.975 6.523   -0.994  1.00 14.90 ?  69  ILE   A HB   1 
ATOM   1528 H  HG12 . ILE   A 1 69  ? 35.683 4.716   -0.153  1.00 15.64 ?  69  ILE   A HG12 1 
ATOM   1529 H  HG13 . ILE   A 1 69  ? 34.995 5.486   -1.357  1.00 15.64 ?  69  ILE   A HG13 1 
ATOM   1530 H  HG21 . ILE   A 1 69  ? 36.427 6.043   -3.318  1.00 16.54 ?  69  ILE   A HG21 1 
ATOM   1531 H  HG22 . ILE   A 1 69  ? 37.902 6.556   -3.033  1.00 16.54 ?  69  ILE   A HG22 1 
ATOM   1532 H  HG23 . ILE   A 1 69  ? 37.629 5.007   -3.267  1.00 16.54 ?  69  ILE   A HG23 1 
ATOM   1533 H  HD11 . ILE   A 1 69  ? 34.764 3.165   -1.546  1.00 16.52 ?  69  ILE   A HD11 1 
ATOM   1534 H  HD12 . ILE   A 1 69  ? 35.515 3.783   -2.800  1.00 16.52 ?  69  ILE   A HD12 1 
ATOM   1535 H  HD13 . ILE   A 1 69  ? 36.341 3.037   -1.667  1.00 16.52 ?  69  ILE   A HD13 1 
ATOM   1536 N  N    . ALA   A 1 70  ? 39.995 6.622   -0.502  1.00 12.18 ?  70  ALA   A N    1 
ATOM   1537 C  CA   . ALA   A 1 70  ? 41.274 7.229   -0.852  1.00 12.97 ?  70  ALA   A CA   1 
ATOM   1538 C  C    . ALA   A 1 70  ? 42.421 6.243   -0.677  1.00 13.44 ?  70  ALA   A C    1 
ATOM   1539 O  O    . ALA   A 1 70  ? 43.389 6.275   -1.441  1.00 15.16 ?  70  ALA   A O    1 
ATOM   1540 C  CB   . ALA   A 1 70  ? 41.512 8.480   -0.007  1.00 13.74 ?  70  ALA   A CB   1 
ATOM   1541 H  H    . ALA   A 1 70  ? 39.569 7.014   0.127   1.00 14.78 ?  70  ALA   A H    1 
ATOM   1542 H  HA   . ALA   A 1 70  ? 41.252 7.502   -1.786  1.00 15.73 ?  70  ALA   A HA   1 
ATOM   1543 H  HB1  . ALA   A 1 70  ? 42.370 8.866   -0.253  1.00 16.65 ?  70  ALA   A HB1  1 
ATOM   1544 H  HB2  . ALA   A 1 70  ? 40.803 9.115   -0.172  1.00 16.65 ?  70  ALA   A HB2  1 
ATOM   1545 H  HB3  . ALA   A 1 70  ? 41.524 8.226   0.930   1.00 16.65 ?  70  ALA   A HB3  1 
ATOM   1546 N  N    . THR   A 1 71  ? 42.317 5.347   0.301   1.00 12.92 ?  71  THR   A N    1 
ATOM   1547 C  CA   . THR   A 1 71  ? 43.369 4.368   0.553   1.00 14.31 ?  71  THR   A CA   1 
ATOM   1548 C  C    . THR   A 1 71  ? 43.248 3.144   -0.344  1.00 14.35 ?  71  THR   A C    1 
ATOM   1549 O  O    . THR   A 1 71  ? 44.260 2.634   -0.844  1.00 16.36 ?  71  THR   A O    1 
ATOM   1550 C  CB   . THR   A 1 71  ? 43.303 3.923   2.010   1.00 16.53 ?  71  THR   A CB   1 
ATOM   1551 O  OG1  . THR   A 1 71  ? 43.564 5.047   2.855   1.00 18.00 ?  71  THR   A OG1  1 
ATOM   1552 C  CG2  . THR   A 1 71  ? 44.311 2.817   2.296   1.00 18.09 ?  71  THR   A CG2  1 
ATOM   1553 H  H    . THR   A 1 71  ? 41.641 5.281   0.829   1.00 15.67 ?  71  THR   A H    1 
ATOM   1554 H  HA   . THR   A 1 71  ? 44.232 4.777   0.395   1.00 17.33 ?  71  THR   A HA   1 
ATOM   1555 H  HB   . THR   A 1 71  ? 42.414 3.573   2.195   1.00 20.01 ?  71  THR   A HB   1 
ATOM   1556 H  HG1  . THR   A 1 71  ? 42.983 5.637   2.727   1.00 21.76 ?  71  THR   A HG1  1 
ATOM   1557 H  HG21 . THR   A 1 71  ? 44.451 2.738   3.253   1.00 21.87 ?  71  THR   A HG21 1 
ATOM   1558 H  HG22 . THR   A 1 71  ? 43.988 1.967   1.956   1.00 21.87 ?  71  THR   A HG22 1 
ATOM   1559 H  HG23 . THR   A 1 71  ? 45.160 3.025   1.873   1.00 21.87 ?  71  THR   A HG23 1 
ATOM   1560 N  N    . ASN   A 1 72  ? 42.025 2.644   -0.540  1.00 13.67 ?  72  ASN   A N    1 
ATOM   1561 C  CA   . ASN   A 1 72  ? 41.804 1.317   -1.096  1.00 13.77 ?  72  ASN   A CA   1 
ATOM   1562 C  C    . ASN   A 1 72  ? 41.182 1.304   -2.480  1.00 13.96 ?  72  ASN   A C    1 
ATOM   1563 O  O    . ASN   A 1 72  ? 41.187 0.247   -3.125  1.00 15.31 ?  72  ASN   A O    1 
ATOM   1564 C  CB   . ASN   A 1 72  ? 40.914 0.503   -0.151  1.00 14.50 ?  72  ASN   A CB   1 
ATOM   1565 C  CG   . ASN   A 1 72  ? 41.537 0.340   1.207   1.00 15.51 ?  72  ASN   A CG   1 
ATOM   1566 O  OD1  . ASN   A 1 72  ? 41.089 0.935   2.186   1.00 17.39 ?  72  ASN   A OD1  1 
ATOM   1567 N  ND2  . ASN   A 1 72  ? 42.589 -0.448  1.274   1.00 15.89 ?  72  ASN   A ND2  1 
ATOM   1568 H  H    . ASN   A 1 72  ? 41.297 3.074   -0.364  1.00 16.56 ?  72  ASN   A H    1 
ATOM   1569 H  HA   . ASN   A 1 72  ? 42.658 0.869   -1.164  1.00 16.69 ?  72  ASN   A HA   1 
ATOM   1570 H  HB2  . ASN   A 1 72  ? 40.066 0.962   -0.047  1.00 17.56 ?  72  ASN   A HB2  1 
ATOM   1571 H  HB3  . ASN   A 1 72  ? 40.778 -0.376  -0.531  1.00 17.56 ?  72  ASN   A HB3  1 
ATOM   1572 H  HD21 . ASN   A 1 72  ? 42.986 -0.569  2.027   1.00 19.24 ?  72  ASN   A HD21 1 
ATOM   1573 H  HD22 . ASN   A 1 72  ? 42.880 -0.839  0.566   1.00 19.24 ?  72  ASN   A HD22 1 
ATOM   1574 N  N    . GLY   A 1 73  ? 40.631 2.417   -2.945  1.00 13.23 ?  73  GLY   A N    1 
ATOM   1575 C  CA   . GLY   A 1 73  ? 39.896 2.419   -4.183  1.00 13.11 ?  73  GLY   A CA   1 
ATOM   1576 C  C    . GLY   A 1 73  ? 38.503 1.842   -4.015  1.00 12.58 ?  73  GLY   A C    1 
ATOM   1577 O  O    . GLY   A 1 73  ? 38.113 1.385   -2.934  1.00 13.02 ?  73  GLY   A O    1 
ATOM   1578 H  H    . GLY   A 1 73  ? 40.670 3.193   -2.562  1.00 16.05 ?  73  GLY   A H    1 
ATOM   1579 H  HA2  . GLY   A 1 73  ? 39.820 3.332   -4.514  1.00 15.89 ?  73  GLY   A HA2  1 
ATOM   1580 H  HA3  . GLY   A 1 73  ? 40.375 1.896   -4.847  1.00 15.89 ?  73  GLY   A HA3  1 
ATOM   1581 N  N    . PRO   A 1 74  ? 37.724 1.870   -5.097  1.00 13.03 ?  74  PRO   A N    1 
ATOM   1582 C  CA   . PRO   A 1 74  ? 36.328 1.435   -5.019  1.00 13.15 ?  74  PRO   A CA   1 
ATOM   1583 C  C    . PRO   A 1 74  ? 36.182 -0.048  -4.704  1.00 12.43 ?  74  PRO   A C    1 
ATOM   1584 O  O    . PRO   A 1 74  ? 37.050 -0.877  -4.993  1.00 13.32 ?  74  PRO   A O    1 
ATOM   1585 C  CB   . PRO   A 1 74  ? 35.786 1.737   -6.421  1.00 14.78 ?  74  PRO   A CB   1 
ATOM   1586 C  CG   . PRO   A 1 74  ? 36.717 2.760   -6.996  1.00 17.63 ?  74  PRO   A CG   1 
ATOM   1587 C  CD   . PRO   A 1 74  ? 38.059 2.412   -6.426  1.00 15.23 ?  74  PRO   A CD   1 
ATOM   1588 H  HA   . PRO   A 1 74  ? 35.843 1.962   -4.361  1.00 15.95 ?  74  PRO   A HA   1 
ATOM   1589 H  HB2  . PRO   A 1 74  ? 35.791 0.927   -6.954  1.00 17.91 ?  74  PRO   A HB2  1 
ATOM   1590 H  HB3  . PRO   A 1 74  ? 34.884 2.094   -6.352  1.00 17.91 ?  74  PRO   A HB3  1 
ATOM   1591 H  HG2  . PRO   A 1 74  ? 36.725 2.693   -7.963  1.00 21.32 ?  74  PRO   A HG2  1 
ATOM   1592 H  HG3  . PRO   A 1 74  ? 36.446 3.647   -6.713  1.00 21.32 ?  74  PRO   A HG3  1 
ATOM   1593 H  HD2  . PRO   A 1 74  ? 38.497 1.735   -6.972  1.00 18.44 ?  74  PRO   A HD2  1 
ATOM   1594 H  HD3  . PRO   A 1 74  ? 38.609 3.211   -6.352  1.00 18.44 ?  74  PRO   A HD3  1 
ATOM   1595 N  N    . LEU   A 1 75  ? 35.039 -0.372  -4.109  1.00 11.74 ?  75  LEU   A N    1 
ATOM   1596 C  CA   . LEU   A 1 75  ? 34.643 -1.761  -3.958  1.00 11.24 ?  75  LEU   A CA   1 
ATOM   1597 C  C    . LEU   A 1 75  ? 34.253 -2.341  -5.316  1.00 12.15 ?  75  LEU   A C    1 
ATOM   1598 O  O    . LEU   A 1 75  ? 34.119 -1.631  -6.317  1.00 13.38 ?  75  LEU   A O    1 
ATOM   1599 C  CB   . LEU   A 1 75  ? 33.460 -1.885  -2.999  1.00 11.58 ?  75  LEU   A CB   1 
ATOM   1600 C  CG   . LEU   A 1 75  ? 33.663 -1.460  -1.551  1.00 13.18 ?  75  LEU   A CG   1 
ATOM   1601 C  CD1  . LEU   A 1 75  ? 32.370 -1.651  -0.767  1.00 15.34 ?  75  LEU   A CD1  1 
ATOM   1602 C  CD2  . LEU   A 1 75  ? 34.797 -2.181  -0.882  1.00 16.13 ?  75  LEU   A CD2  1 
ATOM   1603 H  H    . LEU   A 1 75  ? 34.480 0.196   -3.788  1.00 14.26 ?  75  LEU   A H    1 
ATOM   1604 H  HA   . LEU   A 1 75  ? 35.386 -2.272  -3.610  1.00 13.65 ?  75  LEU   A HA   1 
ATOM   1605 H  HB2  . LEU   A 1 75  ? 32.735 -1.351  -3.351  1.00 14.06 ?  75  LEU   A HB2  1 
ATOM   1606 H  HB3  . LEU   A 1 75  ? 33.192 -2.817  -2.984  1.00 14.06 ?  75  LEU   A HB3  1 
ATOM   1607 H  HG   . LEU   A 1 75  ? 33.881 -0.512  -1.539  1.00 15.98 ?  75  LEU   A HG   1 
ATOM   1608 H  HD11 . LEU   A 1 75  ? 32.514 -1.374  0.150   1.00 18.58 ?  75  LEU   A HD11 1 
ATOM   1609 H  HD12 . LEU   A 1 75  ? 31.677 -1.106  -1.174  1.00 18.58 ?  75  LEU   A HD12 1 
ATOM   1610 H  HD13 . LEU   A 1 75  ? 32.119 -2.585  -0.799  1.00 18.58 ?  75  LEU   A HD13 1 
ATOM   1611 H  HD21 . LEU   A 1 75  ? 34.854 -1.893  0.043   1.00 19.52 ?  75  LEU   A HD21 1 
ATOM   1612 H  HD22 . LEU   A 1 75  ? 34.636 -3.135  -0.923  1.00 19.52 ?  75  LEU   A HD22 1 
ATOM   1613 H  HD23 . LEU   A 1 75  ? 35.629 -1.967  -1.342  1.00 19.52 ?  75  LEU   A HD23 1 
ATOM   1614 N  N    . LYS   A 1 76  ? 34.076 -3.660  -5.332  1.00 12.27 ?  76  LYS   A N    1 
ATOM   1615 C  CA   . LYS   A 1 76  ? 33.474 -4.380  -6.448  1.00 12.77 ?  76  LYS   A CA   1 
ATOM   1616 C  C    . LYS   A 1 76  ? 31.961 -4.459  -6.254  1.00 11.55 ?  76  LYS   A C    1 
ATOM   1617 O  O    . LYS   A 1 76  ? 31.477 -4.577  -5.129  1.00 11.54 ?  76  LYS   A O    1 
ATOM   1618 C  CB   . LYS   A 1 76  ? 34.018 -5.819  -6.495  1.00 14.19 ?  76  LYS   A CB   1 
ATOM   1619 C  CG   . LYS   A 1 76  ? 35.523 -5.931  -6.694  1.00 15.52 ?  76  LYS   A CG   1 
ATOM   1620 C  CD   . LYS   A 1 76  ? 36.032 -7.337  -6.480  1.00 17.24 ?  76  LYS   A CD   1 
ATOM   1621 C  CE   . LYS   A 1 76  ? 37.528 -7.405  -6.696  1.00 19.73 ?  76  LYS   A CE   1 
ATOM   1622 N  NZ   . LYS   A 1 76  ? 38.063 -8.753  -6.437  1.00 20.74 ?  76  LYS   A NZ   1 
ATOM   1623 H  H    . LYS   A 1 76  ? 34.308 -4.177  -4.683  1.00 14.88 ?  76  LYS   A H    1 
ATOM   1624 H  HA   . LYS   A 1 76  ? 33.672 -3.930  -7.285  1.00 15.49 ?  76  LYS   A HA   1 
ATOM   1625 H  HB2  . LYS   A 1 76  ? 33.796 -6.255  -5.657  1.00 17.19 ?  76  LYS   A HB2  1 
ATOM   1626 H  HB3  . LYS   A 1 76  ? 33.585 -6.283  -7.228  1.00 17.19 ?  76  LYS   A HB3  1 
ATOM   1627 H  HG2  . LYS   A 1 76  ? 35.740 -5.664  -7.601  1.00 18.79 ?  76  LYS   A HG2  1 
ATOM   1628 H  HG3  . LYS   A 1 76  ? 35.969 -5.348  -6.060  1.00 18.79 ?  76  LYS   A HG3  1 
ATOM   1629 H  HD2  . LYS   A 1 76  ? 35.834 -7.614  -5.571  1.00 20.85 ?  76  LYS   A HD2  1 
ATOM   1630 H  HD3  . LYS   A 1 76  ? 35.598 -7.934  -7.114  1.00 20.85 ?  76  LYS   A HD3  1 
ATOM   1631 H  HE2  . LYS   A 1 76  ? 37.724 -7.172  -7.615  1.00 23.84 ?  76  LYS   A HE2  1 
ATOM   1632 H  HE3  . LYS   A 1 76  ? 37.961 -6.787  -6.090  1.00 23.84 ?  76  LYS   A HE3  1 
ATOM   1633 H  HZ1  . LYS   A 1 76  ? 38.942 -8.767  -6.571  1.00 25.06 ?  76  LYS   A HZ1  1 
ATOM   1634 H  HZ2  . LYS   A 1 76  ? 37.896 -8.997  -5.596  1.00 25.06 ?  76  LYS   A HZ2  1 
ATOM   1635 H  HZ3  . LYS   A 1 76  ? 37.680 -9.347  -6.985  1.00 25.06 ?  76  LYS   A HZ3  1 
ATOM   1636 N  N    . VAL   A 1 77  ? 31.213 -4.434  -7.364  1.00 12.01 ?  77  VAL   A N    1 
ATOM   1637 C  CA   . VAL   A 1 77  ? 29.803 -4.813  -7.285  1.00 11.88 ?  77  VAL   A CA   1 
ATOM   1638 C  C    . VAL   A 1 77  ? 29.731 -6.265  -6.842  1.00 11.55 ?  77  VAL   A C    1 
ATOM   1639 O  O    . VAL   A 1 77  ? 30.391 -7.138  -7.419  1.00 11.92 ?  77  VAL   A O    1 
ATOM   1640 C  CB   . VAL   A 1 77  ? 29.083 -4.597  -8.624  1.00 13.00 ?  77  VAL   A CB   1 
ATOM   1641 C  CG1  . VAL   A 1 77  ? 27.619 -5.016  -8.512  1.00 13.87 ?  77  VAL   A CG1  1 
ATOM   1642 C  CG2  . VAL   A 1 77  ? 29.178 -3.139  -9.051  1.00 14.82 ?  77  VAL   A CG2  1 
ATOM   1643 H  H    . VAL   A 1 77  ? 31.497 -4.211  -8.147  1.00 14.58 ?  77  VAL   A H    1 
ATOM   1644 H  HA   . VAL   A 1 77  ? 29.369 -4.270  -6.614  1.00 14.42 ?  77  VAL   A HA   1 
ATOM   1645 H  HB   . VAL   A 1 77  ? 29.506 -5.138  -9.309  1.00 15.77 ?  77  VAL   A HB   1 
ATOM   1646 H  HG11 . VAL   A 1 77  ? 27.154 -4.736  -9.314  1.00 16.81 ?  77  VAL   A HG11 1 
ATOM   1647 H  HG12 . VAL   A 1 77  ? 27.572 -5.977  -8.416  1.00 16.81 ?  77  VAL   A HG12 1 
ATOM   1648 H  HG13 . VAL   A 1 77  ? 27.231 -4.582  -7.735  1.00 16.81 ?  77  VAL   A HG13 1 
ATOM   1649 H  HG21 . VAL   A 1 77  ? 28.675 -3.017  -9.871  1.00 17.95 ?  77  VAL   A HG21 1 
ATOM   1650 H  HG22 . VAL   A 1 77  ? 28.807 -2.580  -8.350  1.00 17.95 ?  77  VAL   A HG22 1 
ATOM   1651 H  HG23 . VAL   A 1 77  ? 30.109 -2.909  -9.198  1.00 17.95 ?  77  VAL   A HG23 1 
ATOM   1652 N  N    . GLY   A 1 78  ? 28.945 -6.529  -5.795  1.00 11.40 ?  78  GLY   A N    1 
ATOM   1653 C  CA   . GLY   A 1 78  ? 28.919 -7.820  -5.138  1.00 11.53 ?  78  GLY   A CA   1 
ATOM   1654 C  C    . GLY   A 1 78  ? 29.838 -7.916  -3.942  1.00 10.89 ?  78  GLY   A C    1 
ATOM   1655 O  O    . GLY   A 1 78  ? 29.780 -8.922  -3.214  1.00 11.60 ?  78  GLY   A O    1 
ATOM   1656 H  H    . GLY   A 1 78  ? 28.398 -5.956  -5.451  1.00 13.85 ?  78  GLY   A H    1 
ATOM   1657 H  HA2  . GLY   A 1 78  ? 28.013 -8.007  -4.843  1.00 14.00 ?  78  GLY   A HA2  1 
ATOM   1658 H  HA3  . GLY   A 1 78  ? 29.173 -8.505  -5.777  1.00 14.00 ?  78  GLY   A HA3  1 
ATOM   1659 N  N    . GLY   A 1 79  ? 30.691 -6.911  -3.722  1.00 10.96 ?  79  GLY   A N    1 
ATOM   1660 C  CA   . GLY   A 1 79  ? 31.654 -6.930  -2.646  1.00 11.34 ?  79  GLY   A CA   1 
ATOM   1661 C  C    . GLY   A 1 79  ? 31.213 -6.133  -1.433  1.00 10.49 ?  79  GLY   A C    1 
ATOM   1662 O  O    . GLY   A 1 79  ? 30.090 -5.628  -1.350  1.00 11.21 ?  79  GLY   A O    1 
ATOM   1663 H  H    . GLY   A 1 79  ? 30.724 -6.195  -4.199  1.00 13.32 ?  79  GLY   A H    1 
ATOM   1664 H  HA2  . GLY   A 1 79  ? 31.805 -7.857  -2.373  1.00 13.78 ?  79  GLY   A HA2  1 
ATOM   1665 H  HA3  . GLY   A 1 79  ? 32.495 -6.572  -2.962  1.00 13.78 ?  79  GLY   A HA3  1 
ATOM   1666 N  N    . SER   A 1 80  ? 32.119 -6.043  -0.462  1.00 11.43 ?  80  SER   A N    1 
ATOM   1667 C  CA   . SER   A 1 80  ? 31.805 -5.414  0.810   1.00 10.90 ?  80  SER   A CA   1 
ATOM   1668 C  C    . SER   A 1 80  ? 33.076 -4.961  1.505   1.00 10.92 ?  80  SER   A C    1 
ATOM   1669 O  O    . SER   A 1 80  ? 34.187 -5.394  1.180   1.00 12.47 ?  80  SER   A O    1 
ATOM   1670 C  CB   . SER   A 1 80  ? 31.044 -6.372  1.735   1.00 11.99 ?  80  SER   A CB   1 
ATOM   1671 O  OG   . SER   A 1 80  ? 31.874 -7.425  2.199   1.00 13.43 ?  80  SER   A OG   1 
ATOM   1672 H  H    . SER   A 1 80  ? 32.931 -6.322  -0.529  1.00 13.88 ?  80  SER   A H    1 
ATOM   1673 H  HA   . SER   A 1 80  ? 31.252 -4.638  0.639   1.00 13.24 ?  80  SER   A HA   1 
ATOM   1674 H  HB2  . SER   A 1 80  ? 30.714 -5.875  2.497   1.00 14.55 ?  80  SER   A HB2  1 
ATOM   1675 H  HB3  . SER   A 1 80  ? 30.294 -6.750  1.241   1.00 14.55 ?  80  SER   A HB3  1 
ATOM   1676 H  HG   . SER   A 1 80  ? 32.154 -7.874  1.540   1.00 16.28 ?  80  SER   A HG   1 
ATOM   1677 N  N    . CYS   A 1 81  ? 32.886 -4.114  2.511   1.00 10.52 ?  81  CYS   A N    1 
ATOM   1678 C  CA   . CYS   A 1 81  ? 33.938 -3.829  3.474   1.00 10.65 ?  81  CYS   A CA   1 
ATOM   1679 C  C    . CYS   A 1 81  ? 33.298 -3.592  4.832   1.00 10.46 ?  81  CYS   A C    1 
ATOM   1680 O  O    . CYS   A 1 81  ? 32.132 -3.194  4.924   1.00 11.67 ?  81  CYS   A O    1 
ATOM   1681 C  CB   . CYS   A 1 81  ? 34.813 -2.639  3.052   1.00 11.59 ?  81  CYS   A CB   1 
ATOM   1682 S  SG   . CYS   A 1 81  ? 33.917 -1.056  3.077   1.00 11.76 ?  81  CYS   A SG   1 
ATOM   1683 H  H    . CYS   A 1 81  ? 32.147 -3.696  2.661   1.00 12.79 ?  81  CYS   A H    1 
ATOM   1684 H  HA   . CYS   A 1 81  ? 34.513 -4.605  3.546   1.00 12.95 ?  81  CYS   A HA   1 
ATOM   1685 H  HB2  . CYS   A 1 81  ? 35.568 -2.575  3.659   1.00 14.07 ?  81  CYS   A HB2  1 
ATOM   1686 H  HB3  . CYS   A 1 81  ? 35.135 -2.793  2.146   1.00 14.07 ?  81  CYS   A HB3  1 
ATOM   1687 H  HG   . CYS   A 1 81  ? 34.665 -0.181  2.739   1.00 14.28 ?  81  CYS   A HG   1 
ATOM   1688 N  N    . VAL   A 1 82  ? 34.067 -3.847  5.886   1.00 10.88 ?  82  VAL   A N    1 
ATOM   1689 C  CA   . VAL   A 1 82  ? 33.641 -3.609  7.257   1.00 11.33 ?  82  VAL   A CA   1 
ATOM   1690 C  C    . VAL   A 1 82  ? 34.246 -2.297  7.731   1.00 11.63 ?  82  VAL   A C    1 
ATOM   1691 O  O    . VAL   A 1 82  ? 35.471 -2.129  7.717   1.00 12.30 ?  82  VAL   A O    1 
ATOM   1692 C  CB   . VAL   A 1 82  ? 34.063 -4.751  8.192   1.00 12.93 ?  82  VAL   A CB   1 
ATOM   1693 C  CG1  . VAL   A 1 82  ? 33.613 -4.457  9.616   1.00 14.20 ?  82  VAL   A CG1  1 
ATOM   1694 C  CG2  . VAL   A 1 82  ? 33.515 -6.082  7.712   1.00 13.88 ?  82  VAL   A CG2  1 
ATOM   1695 H  H    . VAL   A 1 82  ? 34.865 -4.180  5.830   1.00 13.22 ?  82  VAL   A H    1 
ATOM   1696 H  HA   . VAL   A 1 82  ? 32.673 -3.530  7.282   1.00 13.76 ?  82  VAL   A HA   1 
ATOM   1697 H  HB   . VAL   A 1 82  ? 35.031 -4.804  8.195   1.00 15.68 ?  82  VAL   A HB   1 
ATOM   1698 H  HG11 . VAL   A 1 82  ? 33.701 -5.265  10.145  1.00 17.20 ?  82  VAL   A HG11 1 
ATOM   1699 H  HG12 . VAL   A 1 82  ? 34.167 -3.755  9.992   1.00 17.20 ?  82  VAL   A HG12 1 
ATOM   1700 H  HG13 . VAL   A 1 82  ? 32.683 -4.174  9.602   1.00 17.20 ?  82  VAL   A HG13 1 
ATOM   1701 H  HG21 . VAL   A 1 82  ? 33.764 -6.770  8.348   1.00 16.82 ?  82  VAL   A HG21 1 
ATOM   1702 H  HG22 . VAL   A 1 82  ? 32.550 -6.020  7.648   1.00 16.82 ?  82  VAL   A HG22 1 
ATOM   1703 H  HG23 . VAL   A 1 82  ? 33.893 -6.281  6.841   1.00 16.82 ?  82  VAL   A HG23 1 
ATOM   1704 N  N    . LEU   A 1 83  ? 33.393 -1.372  8.156   1.00 11.00 ?  83  LEU   A N    1 
ATOM   1705 C  CA   . LEU   A 1 83  ? 33.815 -0.108  8.737   1.00 10.93 ?  83  LEU   A CA   1 
ATOM   1706 C  C    . LEU   A 1 83  ? 33.102 0.072   10.071  1.00 11.16 ?  83  LEU   A C    1 
ATOM   1707 O  O    . LEU   A 1 83  ? 32.379 -0.814  10.536  1.00 11.81 ?  83  LEU   A O    1 
ATOM   1708 C  CB   . LEU   A 1 83  ? 33.564 1.053   7.764   1.00 11.59 ?  83  LEU   A CB   1 
ATOM   1709 C  CG   . LEU   A 1 83  ? 34.461 1.048   6.522   1.00 12.22 ?  83  LEU   A CG   1 
ATOM   1710 C  CD1  . LEU   A 1 83  ? 34.027 2.092   5.516   1.00 12.55 ?  83  LEU   A CD1  1 
ATOM   1711 C  CD2  . LEU   A 1 83  ? 35.935 1.252   6.900   1.00 12.91 ?  83  LEU   A CD2  1 
ATOM   1712 H  H    . LEU   A 1 83  ? 32.537 -1.457  8.114   1.00 13.37 ?  83  LEU   A H    1 
ATOM   1713 H  HA   . LEU   A 1 83  ? 34.767 -0.139  8.914   1.00 13.28 ?  83  LEU   A HA   1 
ATOM   1714 H  HB2  . LEU   A 1 83  ? 32.642 1.010   7.455   1.00 14.07 ?  83  LEU   A HB2  1 
ATOM   1715 H  HB3  . LEU   A 1 83  ? 33.708 1.893   8.227   1.00 14.07 ?  83  LEU   A HB3  1 
ATOM   1716 H  HG   . LEU   A 1 83  ? 34.392 0.178   6.099   1.00 14.82 ?  83  LEU   A HG   1 
ATOM   1717 H  HD11 . LEU   A 1 83  ? 34.620 2.045   4.747   1.00 15.23 ?  83  LEU   A HD11 1 
ATOM   1718 H  HD12 . LEU   A 1 83  ? 33.118 1.902   5.245   1.00 15.23 ?  83  LEU   A HD12 1 
ATOM   1719 H  HD13 . LEU   A 1 83  ? 34.083 2.965   5.926   1.00 15.23 ?  83  LEU   A HD13 1 
ATOM   1720 H  HD21 . LEU   A 1 83  ? 36.452 1.405   6.092   1.00 15.65 ?  83  LEU   A HD21 1 
ATOM   1721 H  HD22 . LEU   A 1 83  ? 36.011 2.021   7.488   1.00 15.65 ?  83  LEU   A HD22 1 
ATOM   1722 H  HD23 . LEU   A 1 83  ? 36.266 0.459   7.354   1.00 15.65 ?  83  LEU   A HD23 1 
ATOM   1723 N  N    . SER   A 1 84  ? 33.312 1.224   10.701  1.00 11.85 ?  84  SER   A N    1 
ATOM   1724 C  CA   . SER   A 1 84  ? 32.665 1.480   11.978  1.00 11.98 ?  84  SER   A CA   1 
ATOM   1725 C  C    . SER   A 1 84  ? 31.147 1.562   11.829  1.00 11.69 ?  84  SER   A C    1 
ATOM   1726 O  O    . SER   A 1 84  ? 30.621 2.017   10.814  1.00 12.05 ?  84  SER   A O    1 
ATOM   1727 C  CB   . SER   A 1 84  ? 33.159 2.801   12.556  1.00 13.05 ?  84  SER   A CB   1 
ATOM   1728 O  OG   . SER   A 1 84  ? 32.530 3.071   13.792  1.00 14.05 ?  84  SER   A OG   1 
ATOM   1729 H  H    . SER   A 1 84  ? 33.814 1.863   10.410  1.00 14.38 ?  84  SER   A H    1 
ATOM   1730 H  HA   . SER   A 1 84  ? 32.883 0.767   12.595  1.00 14.54 ?  84  SER   A HA   1 
ATOM   1731 H  HB2  . SER   A 1 84  ? 34.119 2.747   12.692  1.00 15.82 ?  84  SER   A HB2  1 
ATOM   1732 H  HB3  . SER   A 1 84  ? 32.953 3.515   11.933  1.00 15.82 ?  84  SER   A HB3  1 
ATOM   1733 H  HG   . SER   A 1 84  ? 32.810 3.799   14.103  1.00 17.02 ?  84  SER   A HG   1 
ATOM   1734 N  N    . GLY   A 1 85  ? 30.442 1.142   12.876  1.00 12.70 ?  85  GLY   A N    1 
ATOM   1735 C  CA   . GLY   A 1 85  ? 29.018 1.371   12.979  1.00 13.17 ?  85  GLY   A CA   1 
ATOM   1736 C  C    . GLY   A 1 85  ? 28.649 2.690   13.619  1.00 12.99 ?  85  GLY   A C    1 
ATOM   1737 O  O    . GLY   A 1 85  ? 27.457 3.005   13.728  1.00 13.51 ?  85  GLY   A O    1 
ATOM   1738 H  H    . GLY   A 1 85  ? 30.781 0.712   13.544  1.00 15.41 ?  85  GLY   A H    1 
ATOM   1739 H  HA2  . GLY   A 1 85  ? 28.633 1.340   12.089  1.00 15.97 ?  85  GLY   A HA2  1 
ATOM   1740 H  HA3  . GLY   A 1 85  ? 28.623 0.660   13.503  1.00 15.97 ?  85  GLY   A HA3  1 
ATOM   1741 N  N    . HIS   A 1 86  ? 29.635 3.473   14.049  1.00 12.83 ?  86  HIS   A N    1 
ATOM   1742 C  CA   . HIS   A 1 86  ? 29.406 4.809   14.611  1.00 13.26 ?  86  HIS   A CA   1 
ATOM   1743 C  C    . HIS   A 1 86  ? 28.424 4.684   15.770  1.00 14.04 ?  86  HIS   A C    1 
ATOM   1744 O  O    . HIS   A 1 86  ? 28.611 3.806   16.628  1.00 15.28 ?  86  HIS   A O    1 
ATOM   1745 C  CB   . HIS   A 1 86  ? 29.025 5.785   13.502  1.00 13.14 ?  86  HIS   A CB   1 
ATOM   1746 C  CG   . HIS   A 1 86  ? 30.083 5.891   12.465  1.00 13.39 ?  86  HIS   A CG   1 
ATOM   1747 N  ND1  . HIS   A 1 86  ? 31.170 6.727   12.602  1.00 14.36 ?  86  HIS   A ND1  1 
ATOM   1748 C  CD2  . HIS   A 1 86  ? 30.274 5.202   11.317  1.00 13.07 ?  86  HIS   A CD2  1 
ATOM   1749 C  CE1  . HIS   A 1 86  ? 31.969 6.568   11.564  1.00 14.30 ?  86  HIS   A CE1  1 
ATOM   1750 N  NE2  . HIS   A 1 86  ? 31.455 5.641   10.776  1.00 13.39 ?  86  HIS   A NE2  1 
ATOM   1751 H  H    . HIS   A 1 86  ? 30.461 3.252   14.030  1.00 15.56 ?  86  HIS   A H    1 
ATOM   1752 H  HA   . HIS   A 1 86  ? 30.241 5.125   14.982  1.00 16.08 ?  86  HIS   A HA   1 
ATOM   1753 H  HB2  . HIS   A 1 86  ? 28.208 5.486   13.071  1.00 15.93 ?  86  HIS   A HB2  1 
ATOM   1754 H  HB3  . HIS   A 1 86  ? 28.891 6.671   13.881  1.00 15.93 ?  86  HIS   A HB3  1 
ATOM   1755 H  HD2  . HIS   A 1 86  ? 29.717 4.542   10.961  1.00 15.85 ?  86  HIS   A HD2  1 
ATOM   1756 H  HE1  . HIS   A 1 86  ? 32.763 7.028   11.404  1.00 17.32 ?  86  HIS   A HE1  1 
ATOM   1757 H  HE2  . HIS   A 1 86  ? 31.797 5.369   10.026  1.00 16.23 ?  86  HIS   A HE2  1 
ATOM   1758 N  N    . ASN   A 1 87  ? 27.412 5.538   15.846  1.00 14.87 ?  87  ASN   A N    1 
ATOM   1759 C  CA   . ASN   A 1 87  ? 26.427 5.519   16.912  1.00 15.83 ?  87  ASN   A CA   1 
ATOM   1760 C  C    . ASN   A 1 87  ? 25.304 4.527   16.664  1.00 17.00 ?  87  ASN   A C    1 
ATOM   1761 O  O    . ASN   A 1 87  ? 24.378 4.460   17.475  1.00 19.51 ?  87  ASN   A O    1 
ATOM   1762 C  CB   . ASN   A 1 87  ? 25.828 6.923   17.081  1.00 17.00 ?  87  ASN   A CB   1 
ATOM   1763 C  CG   . ASN   A 1 87  ? 25.318 7.511   15.768  1.00 17.97 ?  87  ASN   A CG   1 
ATOM   1764 O  OD1  . ASN   A 1 87  ? 25.950 7.382   14.723  1.00 18.50 ?  87  ASN   A OD1  1 
ATOM   1765 N  ND2  . ASN   A 1 87  ? 24.169 8.160   15.824  1.00 19.08 ?  87  ASN   A ND2  1 
ATOM   1766 H  H    . ASN   A 1 87  ? 27.273 6.160   15.276  1.00 18.01 ?  87  ASN   A H    1 
ATOM   1767 H  HA   . ASN   A 1 87  ? 26.859 5.273   17.750  1.00 19.16 ?  87  ASN   A HA   1 
ATOM   1768 H  HB2  . ASN   A 1 87  ? 25.081 6.872   17.705  1.00 20.57 ?  87  ASN   A HB2  1 
ATOM   1769 H  HB3  . ASN   A 1 87  ? 26.510 7.513   17.435  1.00 20.57 ?  87  ASN   A HB3  1 
ATOM   1770 H  HD21 . ASN   A 1 87  ? 23.841 8.505   15.112  1.00 23.06 ?  87  ASN   A HD21 1 
ATOM   1771 H  HD22 . ASN   A 1 87  ? 23.753 8.236   16.575  1.00 23.06 ?  87  ASN   A HD22 1 
ATOM   1772 N  N    . LEU   A 1 88  ? 25.363 3.748   15.587  1.00 15.93 ?  88  LEU   A N    1 
ATOM   1773 C  CA   . LEU   A 1 88  ? 24.246 2.893   15.197  1.00 15.58 ?  88  LEU   A CA   1 
ATOM   1774 C  C    . LEU   A 1 88  ? 24.458 1.416   15.496  1.00 15.32 ?  88  LEU   A C    1 
ATOM   1775 O  O    . LEU   A 1 88  ? 23.479 0.686   15.662  1.00 16.40 ?  88  LEU   A O    1 
ATOM   1776 C  CB   . LEU   A 1 88  ? 23.987 3.045   13.699  1.00 16.07 ?  88  LEU   A CB   1 
ATOM   1777 C  CG   . LEU   A 1 88  ? 23.706 4.471   13.219  1.00 17.95 ?  88  LEU   A CG   1 
ATOM   1778 C  CD1  . LEU   A 1 88  ? 23.537 4.489   11.712  1.00 18.60 ?  88  LEU   A CD1  1 
ATOM   1779 C  CD2  . LEU   A 1 88  ? 22.475 5.057   13.908  1.00 19.64 ?  88  LEU   A CD2  1 
ATOM   1780 H  H    . LEU   A 1 88  ? 26.048 3.695   15.066  1.00 19.28 ?  88  LEU   A H    1 
ATOM   1781 H  HA   . LEU   A 1 88  ? 23.452 3.186   15.669  1.00 18.86 ?  88  LEU   A HA   1 
ATOM   1782 H  HB2  . LEU   A 1 88  ? 24.763 2.727   13.217  1.00 19.44 ?  88  LEU   A HB2  1 
ATOM   1783 H  HB3  . LEU   A 1 88  ? 23.215 2.507   13.467  1.00 19.44 ?  88  LEU   A HB3  1 
ATOM   1784 H  HG   . LEU   A 1 88  ? 24.465 5.033   13.439  1.00 21.70 ?  88  LEU   A HG   1 
ATOM   1785 H  HD11 . LEU   A 1 88  ? 23.373 5.402   11.423  1.00 22.49 ?  88  LEU   A HD11 1 
ATOM   1786 H  HD12 . LEU   A 1 88  ? 24.348 4.153   11.299  1.00 22.49 ?  88  LEU   A HD12 1 
ATOM   1787 H  HD13 . LEU   A 1 88  ? 22.785 3.926   11.471  1.00 22.49 ?  88  LEU   A HD13 1 
ATOM   1788 H  HD21 . LEU   A 1 88  ? 22.264 5.911   13.499  1.00 23.73 ?  88  LEU   A HD21 1 
ATOM   1789 H  HD22 . LEU   A 1 88  ? 21.733 4.444   13.800  1.00 23.73 ?  88  LEU   A HD22 1 
ATOM   1790 H  HD23 . LEU   A 1 88  ? 22.671 5.180   14.849  1.00 23.73 ?  88  LEU   A HD23 1 
ATOM   1791 N  N    . ALA   A 1 89  ? 25.704 0.961   15.546  1.00 14.49 ?  89  ALA   A N    1 
ATOM   1792 C  CA   . ALA   A 1 89  ? 26.047 -0.450  15.641  1.00 14.19 ?  89  ALA   A CA   1 
ATOM   1793 C  C    . ALA   A 1 89  ? 27.532 -0.515  15.958  1.00 14.61 ?  89  ALA   A C    1 
ATOM   1794 O  O    . ALA   A 1 89  ? 28.245 0.484   15.849  1.00 15.56 ?  89  ALA   A O    1 
ATOM   1795 C  CB   . ALA   A 1 89  ? 25.773 -1.159  14.317  1.00 13.65 ?  89  ALA   A CB   1 
ATOM   1796 H  H    . ALA   A 1 89  ? 26.390 1.473   15.515  1.00 17.55 ?  89  ALA   A H    1 
ATOM   1797 H  HA   . ALA   A 1 89  ? 25.536 -0.876  16.352  1.00 17.20 ?  89  ALA   A HA   1 
ATOM   1798 H  HB1  . ALA   A 1 89  ? 26.020 -2.094  14.400  1.00 16.54 ?  89  ALA   A HB1  1 
ATOM   1799 H  HB2  . ALA   A 1 89  ? 24.826 -1.089  14.105  1.00 16.54 ?  89  ALA   A HB2  1 
ATOM   1800 H  HB3  . ALA   A 1 89  ? 26.298 -0.740  13.619  1.00 16.54 ?  89  ALA   A HB3  1 
ATOM   1801 N  N    . LYS   A 1 90  ? 28.010 -1.698  16.337  1.00 15.20 ?  90  LYS   A N    1 
ATOM   1802 C  CA   . LYS   A 1 90  ? 29.454 -1.846  16.492  1.00 15.81 ?  90  LYS   A CA   1 
ATOM   1803 C  C    . LYS   A 1 90  ? 30.158 -1.658  15.151  1.00 14.81 ?  90  LYS   A C    1 
ATOM   1804 O  O    . LYS   A 1 90  ? 31.095 -0.851  15.027  1.00 16.25 ?  90  LYS   A O    1 
ATOM   1805 C  CB   . LYS   A 1 90  ? 29.792 -3.204  17.108  1.00 18.55 ?  90  LYS   A CB   1 
ATOM   1806 C  CG   . LYS   A 1 90  ? 31.261 -3.337  17.474  1.00 23.41 ?  90  LYS   A CG   1 
ATOM   1807 C  CD   . LYS   A 1 90  ? 31.511 -4.584  18.302  1.00 28.48 ?  90  LYS   A CD   1 
ATOM   1808 C  CE   . LYS   A 1 90  ? 32.914 -4.594  18.889  1.00 32.56 ?  90  LYS   A CE   1 
ATOM   1809 N  NZ   . LYS   A 1 90  ? 33.961 -4.802  17.852  1.00 35.29 ?  90  LYS   A NZ   1 
ATOM   1810 H  H    . LYS   A 1 90  ? 27.538 -2.396  16.509  1.00 18.41 ?  90  LYS   A H    1 
ATOM   1811 H  HA   . LYS   A 1 90  ? 29.775 -1.159  17.091  1.00 19.13 ?  90  LYS   A HA   1 
ATOM   1812 H  HB2  . LYS   A 1 90  ? 29.266 -3.323  17.917  1.00 22.43 ?  90  LYS   A HB2  1 
ATOM   1813 H  HB3  . LYS   A 1 90  ? 29.575 -3.904  16.471  1.00 22.43 ?  90  LYS   A HB3  1 
ATOM   1814 H  HG2  . LYS   A 1 90  ? 31.790 -3.397  16.664  1.00 28.26 ?  90  LYS   A HG2  1 
ATOM   1815 H  HG3  . LYS   A 1 90  ? 31.532 -2.564  17.997  1.00 28.26 ?  90  LYS   A HG3  1 
ATOM   1816 H  HD2  . LYS   A 1 90  ? 30.875 -4.615  19.035  1.00 34.34 ?  90  LYS   A HD2  1 
ATOM   1817 H  HD3  . LYS   A 1 90  ? 31.411 -5.367  17.739  1.00 34.34 ?  90  LYS   A HD3  1 
ATOM   1818 H  HE2  . LYS   A 1 90  ? 33.083 -3.741  19.320  1.00 39.23 ?  90  LYS   A HE2  1 
ATOM   1819 H  HE3  . LYS   A 1 90  ? 32.983 -5.313  19.536  1.00 39.23 ?  90  LYS   A HE3  1 
ATOM   1820 H  HZ1  . LYS   A 1 90  ? 34.767 -4.802  18.230  1.00 42.51 ?  90  LYS   A HZ1  1 
ATOM   1821 H  HZ2  . LYS   A 1 90  ? 33.833 -5.582  17.443  1.00 42.51 ?  90  LYS   A HZ2  1 
ATOM   1822 H  HZ3  . LYS   A 1 90  ? 33.925 -4.150  17.248  1.00 42.51 ?  90  LYS   A HZ3  1 
ATOM   1823 N  N    . HIS   A 1 91  ? 29.694 -2.379  14.130  1.00 13.26 ?  91  HIS   A N    1 
ATOM   1824 C  CA   . HIS   A 1 91  ? 30.271 -2.357  12.801  1.00 12.74 ?  91  HIS   A CA   1 
ATOM   1825 C  C    . HIS   A 1 91  ? 29.185 -2.083  11.775  1.00 11.31 ?  91  HIS   A C    1 
ATOM   1826 O  O    . HIS   A 1 91  ? 28.022 -2.451  11.968  1.00 12.33 ?  91  HIS   A O    1 
ATOM   1827 C  CB   . HIS   A 1 91  ? 30.873 -3.724  12.438  1.00 15.28 ?  91  HIS   A CB   1 
ATOM   1828 C  CG   . HIS   A 1 91  ? 31.856 -4.248  13.437  1.00 19.18 ?  91  HIS   A CG   1 
ATOM   1829 N  ND1  . HIS   A 1 91  ? 33.136 -3.753  13.550  1.00 21.36 ?  91  HIS   A ND1  1 
ATOM   1830 C  CD2  . HIS   A 1 91  ? 31.753 -5.236  14.357  1.00 21.04 ?  91  HIS   A CD2  1 
ATOM   1831 C  CE1  . HIS   A 1 91  ? 33.779 -4.408  14.501  1.00 22.18 ?  91  HIS   A CE1  1 
ATOM   1832 N  NE2  . HIS   A 1 91  ? 32.961 -5.315  15.007  1.00 22.28 ?  91  HIS   A NE2  1 
ATOM   1833 H  H    . HIS   A 1 91  ? 29.017 -2.923  14.194  1.00 16.07 ?  91  HIS   A H    1 
ATOM   1834 H  HA   . HIS   A 1 91  ? 30.958 -1.681  12.741  1.00 15.46 ?  91  HIS   A HA   1 
ATOM   1835 H  HB2  . HIS   A 1 91  ? 30.157 -4.376  12.366  1.00 18.50 ?  91  HIS   A HB2  1 
ATOM   1836 H  HB3  . HIS   A 1 91  ? 31.332 -3.649  11.587  1.00 18.50 ?  91  HIS   A HB3  1 
ATOM   1837 H  HD1  . HIS   A 1 91  ? 33.467 -3.116  13.073  1.00 25.80 ?  91  HIS   A HD1  1 
ATOM   1838 H  HD2  . HIS   A 1 91  ? 31.009 -5.764  14.523  1.00 25.41 ?  91  HIS   A HD2  1 
ATOM   1839 H  HE1  . HIS   A 1 91  ? 34.659 -4.253  14.766  1.00 26.78 ?  91  HIS   A HE1  1 
ATOM   1840 N  N    . CYS   A 1 92  ? 29.589 -1.486  10.659  1.00 11.28 ?  92  CYS   A N    1 
ATOM   1841 C  CA   . CYS   A 1 92  ? 28.757 -1.403  9.467   1.00 10.88 ?  92  CYS   A CA   1 
ATOM   1842 C  C    . CYS   A 1 92  ? 29.401 -2.227  8.361   1.00 10.60 ?  92  CYS   A C    1 
ATOM   1843 O  O    . CYS   A 1 92  ? 30.559 -1.980  7.992   1.00 11.26 ?  92  CYS   A O    1 
ATOM   1844 C  CB   . CYS   A 1 92  ? 28.555 0.041   9.007   1.00 11.47 ?  92  CYS   A CB   1 
ATOM   1845 S  SG   . CYS   A 1 92  ? 27.533 0.152   7.509   1.00 11.15 ?  92  CYS   A SG   1 
ATOM   1846 H  H    . CYS   A 1 92  ? 30.361 -1.109  10.569  1.00 13.70 ?  92  CYS   A H    1 
ATOM   1847 H  HA   . CYS   A 1 92  ? 27.889 -1.780  9.660   1.00 13.23 ?  92  CYS   A HA   1 
ATOM   1848 H  HB2  . CYS   A 1 92  ? 28.111 0.544   9.710   1.00 13.92 ?  92  CYS   A HB2  1 
ATOM   1849 H  HB3  . CYS   A 1 92  ? 29.417 0.441   8.809   1.00 13.92 ?  92  CYS   A HB3  1 
ATOM   1850 H  HG   . CYS   A 1 92  ? 27.396 1.302   7.214   1.00 13.55 ?  92  CYS   A HG   1 
ATOM   1851 N  N    . LEU   A 1 93  ? 28.659 -3.213  7.859   1.00 10.25 ?  93  LEU   A N    1 
ATOM   1852 C  CA   . LEU   A 1 93  ? 29.060 -3.972  6.682   1.00 10.14 ?  93  LEU   A CA   1 
ATOM   1853 C  C    . LEU   A 1 93  ? 28.465 -3.273  5.465   1.00 9.54  ?  93  LEU   A C    1 
ATOM   1854 O  O    . LEU   A 1 93  ? 27.247 -3.325  5.240   1.00 9.89  ?  93  LEU   A O    1 
ATOM   1855 C  CB   . LEU   A 1 93  ? 28.571 -5.415  6.784   1.00 10.62 ?  93  LEU   A CB   1 
ATOM   1856 C  CG   . LEU   A 1 93  ? 28.969 -6.314  5.615   1.00 10.67 ?  93  LEU   A CG   1 
ATOM   1857 C  CD1  . LEU   A 1 93  ? 30.467 -6.574  5.622   1.00 11.83 ?  93  LEU   A CD1  1 
ATOM   1858 C  CD2  . LEU   A 1 93  ? 28.192 -7.629  5.653   1.00 11.69 ?  93  LEU   A CD2  1 
ATOM   1859 H  H    . LEU   A 1 93  ? 27.903 -3.457  8.191   1.00 12.47 ?  93  LEU   A H    1 
ATOM   1860 H  HA   . LEU   A 1 93  ? 30.024 -3.967  6.607   1.00 12.34 ?  93  LEU   A HA   1 
ATOM   1861 H  HB2  . LEU   A 1 93  ? 28.935 -5.805  7.595   1.00 12.90 ?  93  LEU   A HB2  1 
ATOM   1862 H  HB3  . LEU   A 1 93  ? 27.603 -5.411  6.832   1.00 12.90 ?  93  LEU   A HB3  1 
ATOM   1863 H  HG   . LEU   A 1 93  ? 28.756 -5.872  4.787   1.00 12.97 ?  93  LEU   A HG   1 
ATOM   1864 H  HD11 . LEU   A 1 93  ? 30.692 -7.199  4.916   1.00 14.36 ?  93  LEU   A HD11 1 
ATOM   1865 H  HD12 . LEU   A 1 93  ? 30.942 -5.738  5.487   1.00 14.36 ?  93  LEU   A HD12 1 
ATOM   1866 H  HD13 . LEU   A 1 93  ? 30.726 -6.955  6.485   1.00 14.36 ?  93  LEU   A HD13 1 
ATOM   1867 H  HD21 . LEU   A 1 93  ? 28.470 -8.182  4.903   1.00 14.19 ?  93  LEU   A HD21 1 
ATOM   1868 H  HD22 . LEU   A 1 93  ? 28.382 -8.090  6.487   1.00 14.19 ?  93  LEU   A HD22 1 
ATOM   1869 H  HD23 . LEU   A 1 93  ? 27.245 -7.438  5.589   1.00 14.19 ?  93  LEU   A HD23 1 
ATOM   1870 N  N    . HIS   A 1 94  ? 29.319 -2.585  4.704   1.00 9.59  ?  94  HIS   A N    1 
ATOM   1871 C  CA   . HIS   A 1 94  ? 28.901 -1.906  3.481   1.00 9.69  ?  94  HIS   A CA   1 
ATOM   1872 C  C    . HIS   A 1 94  ? 28.902 -2.935  2.365   1.00 9.62  ?  94  HIS   A C    1 
ATOM   1873 O  O    . HIS   A 1 94  ? 29.966 -3.455  2.017   1.00 11.19 ?  94  HIS   A O    1 
ATOM   1874 C  CB   . HIS   A 1 94  ? 29.861 -0.760  3.157   1.00 9.87  ?  94  HIS   A CB   1 
ATOM   1875 C  CG   . HIS   A 1 94  ? 29.844 0.333   4.171   1.00 9.69  ?  94  HIS   A CG   1 
ATOM   1876 N  ND1  . HIS   A 1 94  ? 28.968 1.398   4.113   1.00 9.99  ?  94  HIS   A ND1  1 
ATOM   1877 C  CD2  . HIS   A 1 94  ? 30.585 0.502   5.289   1.00 10.48 ?  94  HIS   A CD2  1 
ATOM   1878 C  CE1  . HIS   A 1 94  ? 29.184 2.178   5.158   1.00 10.24 ?  94  HIS   A CE1  1 
ATOM   1879 N  NE2  . HIS   A 1 94  ? 30.159 1.657   5.884   1.00 10.35 ?  94  HIS   A NE2  1 
ATOM   1880 H  H    . HIS   A 1 94  ? 30.156 -2.493  4.880   1.00 11.68 ?  94  HIS   A H    1 
ATOM   1881 H  HA   . HIS   A 1 94  ? 28.001 -1.553  3.586   1.00 11.79 ?  94  HIS   A HA   1 
ATOM   1882 H  HB2  . HIS   A 1 94  ? 30.758 -1.108  3.113   1.00 12.01 ?  94  HIS   A HB2  1 
ATOM   1883 H  HB3  . HIS   A 1 94  ? 29.605 -0.374  2.305   1.00 12.01 ?  94  HIS   A HB3  1 
ATOM   1884 H  HD2  . HIS   A 1 94  ? 31.256 -0.057  5.596   1.00 12.74 ?  94  HIS   A HD2  1 
ATOM   1885 H  HE1  . HIS   A 1 94  ? 28.720 2.964   5.346   1.00 12.45 ?  94  HIS   A HE1  1 
ATOM   1886 H  HE2  . HIS   A 1 94  ? 30.472 2.000   6.607   1.00 12.58 ?  94  HIS   A HE2  1 
ATOM   1887 N  N    . VAL   A 1 95  ? 27.727 -3.252  1.820   1.00 9.08  ?  95  VAL   A N    1 
ATOM   1888 C  CA   . VAL   A 1 95  ? 27.576 -4.290  0.802   1.00 9.31  ?  95  VAL   A CA   1 
ATOM   1889 C  C    . VAL   A 1 95  ? 27.037 -3.647  -0.464  1.00 9.19  ?  95  VAL   A C    1 
ATOM   1890 O  O    . VAL   A 1 95  ? 26.036 -2.921  -0.416  1.00 10.04 ?  95  VAL   A O    1 
ATOM   1891 C  CB   . VAL   A 1 95  ? 26.639 -5.429  1.252   1.00 10.29 ?  95  VAL   A CB   1 
ATOM   1892 C  CG1  . VAL   A 1 95  ? 26.524 -6.467  0.143   1.00 10.76 ?  95  VAL   A CG1  1 
ATOM   1893 C  CG2  . VAL   A 1 95  ? 27.141 -6.053  2.531   1.00 10.31 ?  95  VAL   A CG2  1 
ATOM   1894 H  H    . VAL   A 1 95  ? 26.980 -2.876  2.035   1.00 11.06 ?  95  VAL   A H    1 
ATOM   1895 H  HA   . VAL   A 1 95  ? 28.442 -4.670  0.602   1.00 11.34 ?  95  VAL   A HA   1 
ATOM   1896 H  HB   . VAL   A 1 95  ? 25.756 -5.070  1.416   1.00 12.51 ?  95  VAL   A HB   1 
ATOM   1897 H  HG11 . VAL   A 1 95  ? 26.130 -7.278  0.505   1.00 13.07 ?  95  VAL   A HG11 1 
ATOM   1898 H  HG12 . VAL   A 1 95  ? 25.962 -6.120  -0.569  1.00 13.07 ?  95  VAL   A HG12 1 
ATOM   1899 H  HG13 . VAL   A 1 95  ? 27.411 -6.665  -0.205  1.00 13.07 ?  95  VAL   A HG13 1 
ATOM   1900 H  HG21 . VAL   A 1 95  ? 26.569 -6.804  2.758   1.00 12.53 ?  95  VAL   A HG21 1 
ATOM   1901 H  HG22 . VAL   A 1 95  ? 28.050 -6.355  2.400   1.00 12.53 ?  95  VAL   A HG22 1 
ATOM   1902 H  HG23 . VAL   A 1 95  ? 27.107 -5.388  3.236   1.00 12.53 ?  95  VAL   A HG23 1 
ATOM   1903 N  N    . VAL   A 1 96  ? 27.665 -3.947  -1.597  1.00 9.33  ?  96  VAL   A N    1 
ATOM   1904 C  CA   . VAL   A 1 96  ? 27.261 -3.394  -2.884  1.00 9.87  ?  96  VAL   A CA   1 
ATOM   1905 C  C    . VAL   A 1 96  ? 26.452 -4.441  -3.643  1.00 10.36 ?  96  VAL   A C    1 
ATOM   1906 O  O    . VAL   A 1 96  ? 27.007 -5.385  -4.211  1.00 11.14 ?  96  VAL   A O    1 
ATOM   1907 C  CB   . VAL   A 1 96  ? 28.459 -2.922  -3.710  1.00 10.42 ?  96  VAL   A CB   1 
ATOM   1908 C  CG1  . VAL   A 1 96  ? 27.961 -2.288  -4.990  1.00 10.56 ?  96  VAL   A CG1  1 
ATOM   1909 C  CG2  . VAL   A 1 96  ? 29.323 -1.948  -2.923  1.00 11.14 ?  96  VAL   A CG2  1 
ATOM   1910 H  H    . VAL   A 1 96  ? 28.354 -4.468  -1.642  1.00 11.37 ?  96  VAL   A H    1 
ATOM   1911 H  HA   . VAL   A 1 96  ? 26.689 -2.630  -2.731  1.00 12.00 ?  96  VAL   A HA   1 
ATOM   1912 H  HB   . VAL   A 1 96  ? 29.005 -3.681  -3.948  1.00 12.67 ?  96  VAL   A HB   1 
ATOM   1913 H  HG11 . VAL   A 1 96  ? 28.696 -1.813  -5.413  1.00 12.84 ?  96  VAL   A HG11 1 
ATOM   1914 H  HG12 . VAL   A 1 96  ? 27.633 -2.980  -5.583  1.00 12.84 ?  96  VAL   A HG12 1 
ATOM   1915 H  HG13 . VAL   A 1 96  ? 27.247 -1.663  -4.780  1.00 12.84 ?  96  VAL   A HG13 1 
ATOM   1916 H  HG21 . VAL   A 1 96  ? 30.028 -1.613  -3.497  1.00 13.54 ?  96  VAL   A HG21 1 
ATOM   1917 H  HG22 . VAL   A 1 96  ? 28.769 -1.210  -2.616  1.00 13.54 ?  96  VAL   A HG22 1 
ATOM   1918 H  HG23 . VAL   A 1 96  ? 29.704 -2.410  -2.162  1.00 13.54 ?  96  VAL   A HG23 1 
ATOM   1919 N  N    A GLY   A 1 97  ? 25.135 -4.285  -3.641  0.60 10.65 ?  97  GLY   A N    1 
ATOM   1920 N  N    B GLY   A 1 97  ? 25.139 -4.262  -3.699  0.40 10.43 ?  97  GLY   A N    1 
ATOM   1921 C  CA   A GLY   A 1 97  ? 24.298 -5.024  -4.550  0.60 11.36 ?  97  GLY   A CA   1 
ATOM   1922 C  CA   B GLY   A 1 97  ? 24.322 -5.049  -4.590  0.40 10.79 ?  97  GLY   A CA   1 
ATOM   1923 C  C    A GLY   A 1 97  ? 24.286 -4.332  -5.897  0.60 11.23 ?  97  GLY   A C    1 
ATOM   1924 C  C    B GLY   A 1 97  ? 24.371 -4.488  -5.999  0.40 10.88 ?  97  GLY   A C    1 
ATOM   1925 O  O    A GLY   A 1 97  ? 24.557 -3.129  -5.998  0.60 11.88 ?  97  GLY   A O    1 
ATOM   1926 O  O    B GLY   A 1 97  ? 24.712 -3.318  -6.210  0.40 11.09 ?  97  GLY   A O    1 
ATOM   1927 H  H    A GLY   A 1 97  ? 24.706 -3.749  -3.119  0.60 12.95 ?  97  GLY   A H    1 
ATOM   1928 H  H    B GLY   A 1 97  ? 24.701 -3.690  -3.227  0.40 12.68 ?  97  GLY   A H    1 
ATOM   1929 H  HA2  A GLY   A 1 97  ? 24.642 -5.925  -4.649  0.60 13.80 ?  97  GLY   A HA2  1 
ATOM   1930 H  HA2  B GLY   A 1 97  ? 24.647 -5.964  -4.601  0.40 13.11 ?  97  GLY   A HA2  1 
ATOM   1931 H  HA3  A GLY   A 1 97  ? 23.391 -5.069  -4.203  0.60 13.80 ?  97  GLY   A HA3  1 
ATOM   1932 H  HA3  B GLY   A 1 97  ? 23.403 -5.051  -4.279  0.40 13.11 ?  97  GLY   A HA3  1 
ATOM   1933 N  N    A PRO   A 1 98  ? 23.968 -5.065  -6.962  0.60 10.91 ?  98  PRO   A N    1 
ATOM   1934 N  N    B PRO   A 1 98  ? 24.029 -5.307  -6.993  0.40 11.48 ?  98  PRO   A N    1 
ATOM   1935 C  CA   A PRO   A 1 98  ? 23.855 -4.423  -8.276  0.60 11.18 ?  98  PRO   A CA   1 
ATOM   1936 C  CA   B PRO   A 1 98  ? 23.989 -4.805  -8.372  0.40 12.29 ?  98  PRO   A CA   1 
ATOM   1937 C  C    A PRO   A 1 98  ? 22.742 -3.385  -8.295  0.60 11.22 ?  98  PRO   A C    1 
ATOM   1938 C  C    B PRO   A 1 98  ? 22.901 -3.753  -8.543  0.40 12.37 ?  98  PRO   A C    1 
ATOM   1939 O  O    A PRO   A 1 98  ? 21.665 -3.582  -7.728  0.60 11.57 ?  98  PRO   A O    1 
ATOM   1940 O  O    B PRO   A 1 98  ? 21.808 -3.861  -7.981  0.40 13.28 ?  98  PRO   A O    1 
ATOM   1941 C  CB   A PRO   A 1 98  ? 23.555 -5.594  -9.219  0.60 11.44 ?  98  PRO   A CB   1 
ATOM   1942 C  CB   B PRO   A 1 98  ? 23.679 -6.060  -9.197  0.40 12.28 ?  98  PRO   A CB   1 
ATOM   1943 C  CG   A PRO   A 1 98  ? 22.948 -6.647  -8.339  0.60 12.17 ?  98  PRO   A CG   1 
ATOM   1944 C  CG   B PRO   A 1 98  ? 22.958 -6.968  -8.244  0.40 12.30 ?  98  PRO   A CG   1 
ATOM   1945 C  CD   A PRO   A 1 98  ? 23.686 -6.513  -7.030  0.60 11.62 ?  98  PRO   A CD   1 
ATOM   1946 C  CD   B PRO   A 1 98  ? 23.621 -6.723  -6.910  0.40 11.53 ?  98  PRO   A CD   1 
ATOM   1947 H  HA   A PRO   A 1 98  ? 24.693 -4.013  -8.517  0.60 13.58 ?  98  PRO   A HA   1 
ATOM   1948 H  HA   B PRO   A 1 98  ? 24.854 -4.445  -8.635  0.40 14.92 ?  98  PRO   A HA   1 
ATOM   1949 H  HB2  A PRO   A 1 98  ? 22.924 -5.317  -9.897  0.60 13.89 ?  98  PRO   A HB2  1 
ATOM   1950 H  HB2  B PRO   A 1 98  ? 23.110 -5.824  -9.947  0.40 14.90 ?  98  PRO   A HB2  1 
ATOM   1951 H  HB3  A PRO   A 1 98  ? 24.377 -5.917  -9.616  0.60 13.89 ?  98  PRO   A HB3  1 
ATOM   1952 H  HB3  B PRO   A 1 98  ? 24.504 -6.468  -9.505  0.40 14.90 ?  98  PRO   A HB3  1 
ATOM   1953 H  HG2  A PRO   A 1 98  ? 22.002 -6.474  -8.220  0.60 14.77 ?  98  PRO   A HG2  1 
ATOM   1954 H  HG2  B PRO   A 1 98  ? 22.019 -6.727  -8.212  0.40 14.93 ?  98  PRO   A HG2  1 
ATOM   1955 H  HG3  A PRO   A 1 98  ? 23.093 -7.525  -8.728  0.60 14.77 ?  98  PRO   A HG3  1 
ATOM   1956 H  HG3  B PRO   A 1 98  ? 23.069 -7.890  -8.524  0.40 14.93 ?  98  PRO   A HG3  1 
ATOM   1957 H  HD2  A PRO   A 1 98  ? 23.119 -6.796  -6.290  0.60 14.11 ?  98  PRO   A HD2  1 
ATOM   1958 H  HD2  B PRO   A 1 98  ? 22.984 -6.850  -6.189  0.40 14.00 ?  98  PRO   A HD2  1 
ATOM   1959 H  HD3  A PRO   A 1 98  ? 24.516 -7.020  -7.050  0.60 14.11 ?  98  PRO   A HD3  1 
ATOM   1960 H  HD3  B PRO   A 1 98  ? 24.394 -7.303  -6.806  0.40 14.00 ?  98  PRO   A HD3  1 
ATOM   1961 N  N    A ASN   A 1 99  ? 23.020 -2.261  -8.943  0.60 11.73 ?  99  ASN   A N    1 
ATOM   1962 N  N    B ASN   A 1 99  ? 23.208 -2.727  -9.329  0.40 12.46 ?  99  ASN   A N    1 
ATOM   1963 C  CA   A ASN   A 1 99  ? 22.039 -1.202  -9.151  0.60 12.38 ?  99  ASN   A CA   1 
ATOM   1964 C  CA   B ASN   A 1 99  ? 22.259 -1.665  -9.644  0.40 13.49 ?  99  ASN   A CA   1 
ATOM   1965 C  C    A ASN   A 1 99  ? 21.484 -1.353  -10.565 0.60 13.89 ?  99  ASN   A C    1 
ATOM   1966 C  C    B ASN   A 1 99  ? 21.679 -1.949  -11.025 0.40 13.79 ?  99  ASN   A C    1 
ATOM   1967 O  O    A ASN   A 1 99  ? 22.172 -1.053  -11.549 0.60 15.16 ?  99  ASN   A O    1 
ATOM   1968 O  O    B ASN   A 1 99  ? 22.362 -1.782  -12.040 0.40 13.33 ?  99  ASN   A O    1 
ATOM   1969 C  CB   A ASN   A 1 99  ? 22.675 0.172   -8.948  0.60 12.42 ?  99  ASN   A CB   1 
ATOM   1970 C  CB   B ASN   A 1 99  ? 22.944 -0.302  -9.607  0.40 14.63 ?  99  ASN   A CB   1 
ATOM   1971 C  CG   A ASN   A 1 99  ? 21.654 1.300   -8.953  0.60 12.75 ?  99  ASN   A CG   1 
ATOM   1972 C  CG   B ASN   A 1 99  ? 21.968 0.845   -9.776  0.40 15.92 ?  99  ASN   A CG   1 
ATOM   1973 O  OD1  A ASN   A 1 99  ? 20.675 1.258   -9.695  0.60 13.54 ?  99  ASN   A OD1  1 
ATOM   1974 O  OD1  B ASN   A 1 99  ? 20.981 0.732   -10.502 0.40 16.21 ?  99  ASN   A OD1  1 
ATOM   1975 N  ND2  A ASN   A 1 99  ? 21.882 2.315   -8.128  0.60 12.82 ?  99  ASN   A ND2  1 
ATOM   1976 N  ND2  B ASN   A 1 99  ? 22.233 1.952   -9.095  0.40 16.77 ?  99  ASN   A ND2  1 
ATOM   1977 H  H    A ASN   A 1 99  ? 23.794 -2.083  -9.257  0.60 14.25 ?  99  ASN   A H    1 
ATOM   1978 H  H    B ASN   A 1 99  ? 23.981 -2.623  -9.690  0.40 15.12 ?  99  ASN   A H    1 
ATOM   1979 H  HA   A ASN   A 1 99  ? 21.310 -1.305  -8.511  0.60 15.02 ?  99  ASN   A HA   1 
ATOM   1980 H  HA   B ASN   A 1 99  ? 21.536 -1.676  -8.992  0.40 16.35 ?  99  ASN   A HA   1 
ATOM   1981 H  HB2  A ASN   A 1 99  ? 23.137 0.186   -8.097  0.60 15.06 ?  99  ASN   A HB2  1 
ATOM   1982 H  HB2  B ASN   A 1 99  ? 23.395 -0.198  -8.754  0.40 17.72 ?  99  ASN   A HB2  1 
ATOM   1983 H  HB3  A ASN   A 1 99  ? 23.301 0.332   -9.671  0.60 15.06 ?  99  ASN   A HB3  1 
ATOM   1984 H  HB3  B ASN   A 1 99  ? 23.582 -0.265  -10.332 0.40 17.72 ?  99  ASN   A HB3  1 
ATOM   1985 H  HD21 A ASN   A 1 99  ? 21.329 2.974   -8.093  0.60 15.54 ?  99  ASN   A HD21 1 
ATOM   1986 H  HD21 B ASN   A 1 99  ? 21.708 2.627   -9.154  0.40 20.29 ?  99  ASN   A HD21 1 
ATOM   1987 H  HD22 A ASN   A 1 99  ? 22.577 2.308   -7.625  0.60 15.54 ?  99  ASN   A HD22 1 
ATOM   1988 H  HD22 B ASN   A 1 99  ? 22.933 1.991   -8.595  0.40 20.29 ?  99  ASN   A HD22 1 
ATOM   1989 N  N    A VAL   A 1 100 ? 20.237 -1.827  -10.655 0.60 14.39 ?  100 VAL   A N    1 
ATOM   1990 N  N    B VAL   A 1 100 ? 20.419 -2.390  -11.054 0.40 15.83 ?  100 VAL   A N    1 
ATOM   1991 C  CA   A VAL   A 1 100 ? 19.611 -2.073  -11.951 0.60 16.09 ?  100 VAL   A CA   1 
ATOM   1992 C  CA   B VAL   A 1 100 ? 19.773 -2.751  -12.313 0.40 17.79 ?  100 VAL   A CA   1 
ATOM   1993 C  C    A VAL   A 1 100 ? 19.513 -0.787  -12.754 0.60 16.43 ?  100 VAL   A C    1 
ATOM   1994 C  C    B VAL   A 1 100 ? 19.698 -1.558  -13.252 0.40 18.55 ?  100 VAL   A C    1 
ATOM   1995 O  O    A VAL   A 1 100 ? 19.624 -0.801  -13.985 0.60 17.05 ?  100 VAL   A O    1 
ATOM   1996 O  O    B VAL   A 1 100 ? 19.728 -1.722  -14.478 0.40 18.94 ?  100 VAL   A O    1 
ATOM   1997 C  CB   A VAL   A 1 100 ? 18.238 -2.756  -11.759 0.60 17.92 ?  100 VAL   A CB   1 
ATOM   1998 C  CB   B VAL   A 1 100 ? 18.380 -3.348  -12.043 0.40 19.29 ?  100 VAL   A CB   1 
ATOM   1999 C  CG1  A VAL   A 1 100 ? 17.494 -2.869  -13.083 0.60 18.55 ?  100 VAL   A CG1  1 
ATOM   2000 C  CG1  B VAL   A 1 100 ? 17.695 -3.717  -13.351 0.40 19.71 ?  100 VAL   A CG1  1 
ATOM   2001 C  CG2  A VAL   A 1 100 ? 18.424 -4.133  -11.143 0.60 18.77 ?  100 VAL   A CG2  1 
ATOM   2002 C  CG2  B VAL   A 1 100 ? 18.495 -4.555  -11.132 0.40 19.87 ?  100 VAL   A CG2  1 
ATOM   2003 H  H    A VAL   A 1 100 ? 19.730 -2.017  -9.976  0.60 17.44 ?  100 VAL   A H    1 
ATOM   2004 H  H    B VAL   A 1 100 ? 19.925 -2.499  -10.357 0.40 19.16 ?  100 VAL   A H    1 
ATOM   2005 H  HA   A VAL   A 1 100 ? 20.166 -2.690  -12.448 0.60 19.47 ?  100 VAL   A HA   1 
ATOM   2006 H  HA   B VAL   A 1 100 ? 20.306 -3.432  -12.751 0.40 21.52 ?  100 VAL   A HA   1 
ATOM   2007 H  HB   A VAL   A 1 100 ? 17.696 -2.230  -11.152 0.60 21.66 ?  100 VAL   A HB   1 
ATOM   2008 H  HB   B VAL   A 1 100 ? 17.834 -2.680  -11.598 0.40 23.32 ?  100 VAL   A HB   1 
ATOM   2009 H  HG11 A VAL   A 1 100 ? 16.755 -3.492  -12.978 0.60 22.43 ?  100 VAL   A HG11 1 
ATOM   2010 H  HG11 B VAL   A 1 100 ? 16.903 -4.239  -13.152 0.40 23.82 ?  100 VAL   A HG11 1 
ATOM   2011 H  HG12 A VAL   A 1 100 ? 17.155 -1.997  -13.332 0.60 22.43 ?  100 VAL   A HG12 1 
ATOM   2012 H  HG12 B VAL   A 1 100 ? 17.445 -2.906  -13.821 0.40 23.82 ?  100 VAL   A HG12 1 
ATOM   2013 H  HG13 A VAL   A 1 100 ? 18.105 -3.198  -13.761 0.60 22.43 ?  100 VAL   A HG13 1 
ATOM   2014 H  HG13 B VAL   A 1 100 ? 18.308 -4.238  -13.892 0.40 23.82 ?  100 VAL   A HG13 1 
ATOM   2015 H  HG21 A VAL   A 1 100 ? 17.557 -4.563  -11.052 0.60 22.69 ?  100 VAL   A HG21 1 
ATOM   2016 H  HG21 B VAL   A 1 100 ? 17.629 -4.985  -11.073 0.40 24.01 ?  100 VAL   A HG21 1 
ATOM   2017 H  HG22 A VAL   A 1 100 ? 18.995 -4.665  -11.721 0.60 22.69 ?  100 VAL   A HG22 1 
ATOM   2018 H  HG22 B VAL   A 1 100 ? 19.147 -5.167  -11.504 0.40 24.01 ?  100 VAL   A HG22 1 
ATOM   2019 H  HG23 A VAL   A 1 100 ? 18.836 -4.038  -10.270 0.60 22.69 ?  100 VAL   A HG23 1 
ATOM   2020 H  HG23 B VAL   A 1 100 ? 18.779 -4.260  -10.253 0.40 24.01 ?  100 VAL   A HG23 1 
ATOM   2021 N  N    A ASN   A 1 101 ? 19.312 0.343   -12.083 0.60 17.80 ?  101 ASN   A N    1 
ATOM   2022 N  N    B ASN   A 1 101 ? 19.575 -0.346  -12.704 0.40 19.37 ?  101 ASN   A N    1 
ATOM   2023 C  CA   A ASN   A 1 101 ? 19.244 1.616   -12.786 0.60 19.39 ?  101 ASN   A CA   1 
ATOM   2024 C  CA   B ASN   A 1 101 ? 19.538 0.851   -13.536 0.40 20.70 ?  101 ASN   A CA   1 
ATOM   2025 C  C    A ASN   A 1 101 ? 20.600 2.065   -13.330 0.60 21.66 ?  101 ASN   A C    1 
ATOM   2026 C  C    B ASN   A 1 101 ? 20.881 1.141   -14.195 0.40 21.94 ?  101 ASN   A C    1 
ATOM   2027 O  O    A ASN   A 1 101 ? 20.668 3.121   -13.970 0.60 23.06 ?  101 ASN   A O    1 
ATOM   2028 O  O    B ASN   A 1 101 ? 20.915 1.822   -15.226 0.40 22.25 ?  101 ASN   A O    1 
ATOM   2029 C  CB   A ASN   A 1 101 ? 18.601 2.663   -11.875 0.60 18.62 ?  101 ASN   A CB   1 
ATOM   2030 C  CB   B ASN   A 1 101 ? 19.080 2.050   -12.704 0.40 20.72 ?  101 ASN   A CB   1 
ATOM   2031 C  CG   A ASN   A 1 101 ? 17.232 2.222   -11.370 0.60 18.29 ?  101 ASN   A CG   1 
ATOM   2032 C  CG   B ASN   A 1 101 ? 17.780 1.782   -11.966 0.40 21.21 ?  101 ASN   A CG   1 
ATOM   2033 O  OD1  A ASN   A 1 101 ? 16.416 1.701   -12.131 0.60 18.47 ?  101 ASN   A OD1  1 
ATOM   2034 O  OD1  B ASN   A 1 101 ? 16.861 1.161   -12.505 0.40 22.09 ?  101 ASN   A OD1  1 
ATOM   2035 N  ND2  A ASN   A 1 101 ? 16.986 2.403   -10.078 0.60 18.07 ?  101 ASN   A ND2  1 
ATOM   2036 N  ND2  B ASN   A 1 101 ? 17.703 2.234   -10.721 0.40 21.17 ?  101 ASN   A ND2  1 
ATOM   2037 H  H    A ASN   A 1 101 ? 19.210 0.397   -11.233 0.60 21.52 ?  101 ASN   A H    1 
ATOM   2038 H  H    B ASN   A 1 101 ? 19.496 -0.194  -11.859 0.40 23.40 ?  101 ASN   A H    1 
ATOM   2039 H  HA   A ASN   A 1 101 ? 18.660 1.505   -13.549 0.60 23.43 ?  101 ASN   A HA   1 
ATOM   2040 H  HA   B ASN   A 1 101 ? 18.891 0.718   -14.241 0.40 25.01 ?  101 ASN   A HA   1 
ATOM   2041 H  HB2  A ASN   A 1 101 ? 19.174 2.815   -11.110 0.60 22.51 ?  101 ASN   A HB2  1 
ATOM   2042 H  HB2  B ASN   A 1 101 ? 19.761 2.264   -12.046 0.40 25.03 ?  101 ASN   A HB2  1 
ATOM   2043 H  HB3  A ASN   A 1 101 ? 18.487 3.488   -12.377 0.60 22.51 ?  101 ASN   A HB3  1 
ATOM   2044 H  HB3  B ASN   A 1 101 ? 18.939 2.810   -13.293 0.40 25.03 ?  101 ASN   A HB3  1 
ATOM   2045 H  HD21 A ASN   A 1 101 ? 16.227 2.164   -9.751  0.60 21.85 ?  101 ASN   A HD21 1 
ATOM   2046 H  HD21 B ASN   A 1 101 ? 16.988 2.104   -10.263 0.40 25.57 ?  101 ASN   A HD21 1 
ATOM   2047 H  HD22 A ASN   A 1 101 ? 17.577 2.769   -9.577  0.60 21.85 ?  101 ASN   A HD22 1 
ATOM   2048 H  HD22 B ASN   A 1 101 ? 18.365 2.659   -10.376 0.40 25.57 ?  101 ASN   A HD22 1 
ATOM   2049 N  N    A LYS   A 1 102 ? 21.664 1.285   -13.108 0.60 23.28 ?  102 LYS   A N    1 
ATOM   2050 N  N    B LYS   A 1 102 ? 21.980 0.645   -13.627 0.40 23.33 ?  102 LYS   A N    1 
ATOM   2051 C  CA   A LYS   A 1 102 ? 22.947 1.469   -13.775 0.60 24.91 ?  102 LYS   A CA   1 
ATOM   2052 C  CA   B LYS   A 1 102 ? 23.308 0.790   -14.210 0.40 24.22 ?  102 LYS   A CA   1 
ATOM   2053 C  C    A LYS   A 1 102 ? 23.249 0.370   -14.785 0.60 25.41 ?  102 LYS   A C    1 
ATOM   2054 C  C    B LYS   A 1 102 ? 23.675 -0.372  -15.128 0.40 24.16 ?  102 LYS   A C    1 
ATOM   2055 O  O    A LYS   A 1 102 ? 24.303 0.414   -15.427 0.60 25.93 ?  102 LYS   A O    1 
ATOM   2056 O  O    B LYS   A 1 102 ? 24.829 -0.466  -15.558 0.40 24.25 ?  102 LYS   A O    1 
ATOM   2057 C  CB   A LYS   A 1 102 ? 24.088 1.517   -12.749 0.60 26.53 ?  102 LYS   A CB   1 
ATOM   2058 C  CB   B LYS   A 1 102 ? 24.365 0.919   -13.106 0.40 25.51 ?  102 LYS   A CB   1 
ATOM   2059 C  CG   A LYS   A 1 102 ? 23.978 2.620   -11.714 0.60 27.98 ?  102 LYS   A CG   1 
ATOM   2060 C  CG   B LYS   A 1 102 ? 24.221 2.155   -12.229 0.40 26.61 ?  102 LYS   A CG   1 
ATOM   2061 C  CD   A LYS   A 1 102 ? 25.177 2.591   -10.774 0.60 29.47 ?  102 LYS   A CD   1 
ATOM   2062 C  CD   B LYS   A 1 102 ? 25.193 2.125   -11.054 0.40 27.94 ?  102 LYS   A CD   1 
ATOM   2063 C  CE   A LYS   A 1 102 ? 25.114 3.703   -9.739  0.60 30.66 ?  102 LYS   A CE   1 
ATOM   2064 C  CE   B LYS   A 1 102 ? 25.001 3.327   -10.140 0.40 29.00 ?  102 LYS   A CE   1 
ATOM   2065 N  NZ   A LYS   A 1 102 ? 26.256 3.632   -8.780  0.60 31.09 ?  102 LYS   A NZ   1 
ATOM   2066 N  NZ   B LYS   A 1 102 ? 25.409 3.033   -8.736  0.40 29.70 ?  102 LYS   A NZ   1 
ATOM   2067 H  H    A LYS   A 1 102 ? 21.663 0.619   -12.562 0.60 28.11 ?  102 LYS   A H    1 
ATOM   2068 H  H    B LYS   A 1 102 ? 21.981 0.212   -12.884 0.40 28.16 ?  102 LYS   A H    1 
ATOM   2069 H  HA   A LYS   A 1 102 ? 22.939 2.311   -14.250 0.60 30.06 ?  102 LYS   A HA   1 
ATOM   2070 H  HA   B LYS   A 1 102 ? 23.331 1.608   -14.730 0.40 29.22 ?  102 LYS   A HA   1 
ATOM   2071 H  HB2  A LYS   A 1 102 ? 24.112 0.672   -12.274 0.60 32.01 ?  102 LYS   A HB2  1 
ATOM   2072 H  HB2  B LYS   A 1 102 ? 24.308 0.143   -12.528 0.40 30.78 ?  102 LYS   A HB2  1 
ATOM   2073 H  HB3  A LYS   A 1 102 ? 24.924 1.646   -13.225 0.60 32.01 ?  102 LYS   A HB3  1 
ATOM   2074 H  HB3  B LYS   A 1 102 ? 25.244 0.954   -13.518 0.40 30.78 ?  102 LYS   A HB3  1 
ATOM   2075 H  HG2  A LYS   A 1 102 ? 23.957 3.481   -12.161 0.60 33.74 ?  102 LYS   A HG2  1 
ATOM   2076 H  HG2  B LYS   A 1 102 ? 24.410 2.947   -12.757 0.40 32.09 ?  102 LYS   A HG2  1 
ATOM   2077 H  HG3  A LYS   A 1 102 ? 23.172 2.491   -11.190 0.60 33.74 ?  102 LYS   A HG3  1 
ATOM   2078 H  HG3  B LYS   A 1 102 ? 23.319 2.194   -11.875 0.40 32.09 ?  102 LYS   A HG3  1 
ATOM   2079 H  HD2  A LYS   A 1 102 ? 25.194 1.741   -10.306 0.60 35.53 ?  102 LYS   A HD2  1 
ATOM   2080 H  HD2  B LYS   A 1 102 ? 25.048 1.321   -10.532 0.40 33.69 ?  102 LYS   A HD2  1 
ATOM   2081 H  HD3  A LYS   A 1 102 ? 25.990 2.703   -11.292 0.60 35.53 ?  102 LYS   A HD3  1 
ATOM   2082 H  HD3  B LYS   A 1 102 ? 26.103 2.143   -11.391 0.40 33.69 ?  102 LYS   A HD3  1 
ATOM   2083 H  HE2  A LYS   A 1 102 ? 25.149 4.561   -10.191 0.60 36.96 ?  102 LYS   A HE2  1 
ATOM   2084 H  HE2  B LYS   A 1 102 ? 25.544 4.064   -10.464 0.40 34.97 ?  102 LYS   A HE2  1 
ATOM   2085 H  HE3  A LYS   A 1 102 ? 24.288 3.624   -9.236  0.60 36.96 ?  102 LYS   A HE3  1 
ATOM   2086 H  HE3  B LYS   A 1 102 ? 24.064 3.579   -10.137 0.40 34.97 ?  102 LYS   A HE3  1 
ATOM   2087 H  HZ1  A LYS   A 1 102 ? 26.196 4.291   -8.186  0.60 37.47 ?  102 LYS   A HZ1  1 
ATOM   2088 H  HZ1  B LYS   A 1 102 ? 25.282 3.751   -8.225  0.40 35.80 ?  102 LYS   A HZ1  1 
ATOM   2089 H  HZ2  A LYS   A 1 102 ? 26.243 2.852   -8.349  0.60 37.47 ?  102 LYS   A HZ2  1 
ATOM   2090 H  HZ2  B LYS   A 1 102 ? 24.924 2.360   -8.413  0.40 35.80 ?  102 LYS   A HZ2  1 
ATOM   2091 H  HZ3  A LYS   A 1 102 ? 27.027 3.706   -9.219  0.60 37.47 ?  102 LYS   A HZ3  1 
ATOM   2092 H  HZ3  B LYS   A 1 102 ? 26.270 2.808   -8.709  0.40 35.80 ?  102 LYS   A HZ3  1 
ATOM   2093 N  N    A GLY   A 1 103 ? 22.368 -0.620  -14.933 0.60 26.20 ?  103 GLY   A N    1 
ATOM   2094 N  N    B GLY   A 1 103 ? 22.729 -1.259  -15.430 0.40 23.96 ?  103 GLY   A N    1 
ATOM   2095 C  CA   A GLY   A 1 103 ? 22.590 -1.713  -15.860 0.60 26.30 ?  103 GLY   A CA   1 
ATOM   2096 C  CA   B GLY   A 1 103 ? 23.018 -2.402  -16.274 0.40 23.61 ?  103 GLY   A CA   1 
ATOM   2097 C  C    A GLY   A 1 103 ? 23.422 -2.856  -15.323 0.60 26.50 ?  103 GLY   A C    1 
ATOM   2098 C  C    B GLY   A 1 103 ? 23.811 -3.503  -15.610 0.40 22.70 ?  103 GLY   A C    1 
ATOM   2099 O  O    A GLY   A 1 103 ? 23.913 -3.669  -16.112 0.60 27.43 ?  103 GLY   A O    1 
ATOM   2100 O  O    B GLY   A 1 103 ? 24.377 -4.353  -16.303 0.40 23.15 ?  103 GLY   A O    1 
ATOM   2101 H  H    A GLY   A 1 103 ? 21.630 -0.679  -14.505 0.60 31.60 ?  103 GLY   A H    1 
ATOM   2102 H  H    B GLY   A 1 103 ? 21.915 -1.210  -15.161 0.40 28.91 ?  103 GLY   A H    1 
ATOM   2103 H  HA2  A GLY   A 1 103 ? 21.729 -2.070  -16.140 0.60 31.72 ?  103 GLY   A HA2  1 
ATOM   2104 H  HA2  B GLY   A 1 103 ? 22.186 -2.784  -16.590 0.40 28.50 ?  103 GLY   A HA2  1 
ATOM   2105 H  HA3  A GLY   A 1 103 ? 23.039 -1.375  -16.650 0.60 31.72 ?  103 GLY   A HA3  1 
ATOM   2106 H  HA3  B GLY   A 1 103 ? 23.523 -2.092  -17.042 0.40 28.50 ?  103 GLY   A HA3  1 
ATOM   2107 N  N    A GLU   A 1 104 ? 23.593 -2.952  -14.008 0.60 25.20 ?  104 GLU   A N    1 
ATOM   2108 N  N    B GLU   A 1 104 ? 23.855 -3.528  -14.283 0.40 21.09 ?  104 GLU   A N    1 
ATOM   2109 C  CA   A GLU   A 1 104 ? 24.457 -3.966  -13.423 0.60 24.04 ?  104 GLU   A CA   1 
ATOM   2110 C  CA   B GLU   A 1 104 ? 24.724 -4.455  -13.576 0.40 19.53 ?  104 GLU   A CA   1 
ATOM   2111 C  C    A GLU   A 1 104 ? 23.752 -5.318  -13.338 0.60 24.62 ?  104 GLU   A C    1 
ATOM   2112 C  C    B GLU   A 1 104 ? 24.058 -5.821  -13.423 0.40 19.30 ?  104 GLU   A C    1 
ATOM   2113 O  O    A GLU   A 1 104 ? 22.531 -5.404  -13.172 0.60 24.83 ?  104 GLU   A O    1 
ATOM   2114 O  O    B GLU   A 1 104 ? 22.834 -5.936  -13.296 0.40 19.48 ?  104 GLU   A O    1 
ATOM   2115 C  CB   A GLU   A 1 104 ? 24.960 -3.503  -12.051 0.60 22.46 ?  104 GLU   A CB   1 
ATOM   2116 C  CB   B GLU   A 1 104 ? 25.126 -3.865  -12.222 0.40 19.23 ?  104 GLU   A CB   1 
ATOM   2117 C  CG   A GLU   A 1 104 ? 25.970 -2.360  -12.192 0.60 21.79 ?  104 GLU   A CG   1 
ATOM   2118 C  CG   B GLU   A 1 104 ? 25.845 -2.525  -12.380 0.40 19.86 ?  104 GLU   A CG   1 
ATOM   2119 C  CD   A GLU   A 1 104 ? 26.280 -1.588  -10.920 0.60 20.59 ?  104 GLU   A CD   1 
ATOM   2120 C  CD   B GLU   A 1 104 ? 26.224 -1.858  -11.075 0.40 20.09 ?  104 GLU   A CD   1 
ATOM   2121 O  OE1  A GLU   A 1 104 ? 25.643 -1.820  -9.875  0.60 18.55 ?  104 GLU   A OE1  1 
ATOM   2122 O  OE1  B GLU   A 1 104 ? 25.793 -2.321  -10.000 0.40 20.16 ?  104 GLU   A OE1  1 
ATOM   2123 O  OE2  A GLU   A 1 104 ? 27.183 -0.718  -10.992 0.60 21.69 -1 104 GLU   A OE2  1 
ATOM   2124 O  OE2  B GLU   A 1 104 ? 26.956 -0.847  -11.137 0.40 20.64 -1 104 GLU   A OE2  1 
ATOM   2125 H  H    A GLU   A 1 104 ? 23.220 -2.436  -13.434 0.60 30.41 ?  104 GLU   A H    1 
ATOM   2126 H  H    B GLU   A 1 104 ? 23.385 -3.018  -13.775 0.40 25.47 ?  104 GLU   A H    1 
ATOM   2127 H  HA   A GLU   A 1 104 ? 25.229 -4.079  -13.997 0.60 29.01 ?  104 GLU   A HA   1 
ATOM   2128 H  HA   B GLU   A 1 104 ? 25.536 -4.574  -14.095 0.40 23.60 ?  104 GLU   A HA   1 
ATOM   2129 H  HB2  A GLU   A 1 104 ? 24.207 -3.193  -11.526 0.60 27.11 ?  104 GLU   A HB2  1 
ATOM   2130 H  HB2  B GLU   A 1 104 ? 24.331 -3.721  -11.688 0.40 23.23 ?  104 GLU   A HB2  1 
ATOM   2131 H  HB3  A GLU   A 1 104 ? 25.396 -4.248  -11.606 0.60 27.11 ?  104 GLU   A HB3  1 
ATOM   2132 H  HB3  B GLU   A 1 104 ? 25.727 -4.480  -11.774 0.40 23.23 ?  104 GLU   A HB3  1 
ATOM   2133 H  HG2  A GLU   A 1 104 ? 26.805 -2.728  -12.509 0.60 26.32 ?  104 GLU   A HG2  1 
ATOM   2134 H  HG2  B GLU   A 1 104 ? 26.656 -2.663  -12.894 0.40 23.99 ?  104 GLU   A HG2  1 
ATOM   2135 H  HG3  A GLU   A 1 104 ? 25.622 -1.725  -12.836 0.60 26.32 ?  104 GLU   A HG3  1 
ATOM   2136 H  HG3  B GLU   A 1 104 ? 25.262 -1.908  -12.847 0.40 23.99 ?  104 GLU   A HG3  1 
ATOM   2137 N  N    A ASP   A 1 105 ? 24.549 -6.380  -13.457 0.60 25.23 ?  105 ASP   A N    1 
ATOM   2138 N  N    B ASP   A 1 105 ? 24.892 -6.860  -13.440 0.40 19.73 ?  105 ASP   A N    1 
ATOM   2139 C  CA   A ASP   A 1 105 ? 24.028 -7.734  -13.588 0.60 26.02 ?  105 ASP   A CA   1 
ATOM   2140 C  CA   B ASP   A 1 105 ? 24.430 -8.241  -13.533 0.40 20.18 ?  105 ASP   A CA   1 
ATOM   2141 C  C    A ASP   A 1 105 ? 23.351 -8.167  -12.292 0.60 24.00 ?  105 ASP   A C    1 
ATOM   2142 C  C    B ASP   A 1 105 ? 23.628 -8.639  -12.302 0.40 19.25 ?  105 ASP   A C    1 
ATOM   2143 O  O    A ASP   A 1 105 ? 23.993 -8.227  -11.240 0.60 22.77 ?  105 ASP   A O    1 
ATOM   2144 O  O    B ASP   A 1 105 ? 24.135 -8.605  -11.178 0.40 17.48 ?  105 ASP   A O    1 
ATOM   2145 C  CB   A ASP   A 1 105 ? 25.177 -8.680  -13.927 0.60 28.70 ?  105 ASP   A CB   1 
ATOM   2146 C  CB   B ASP   A 1 105 ? 25.649 -9.150  -13.679 0.40 21.88 ?  105 ASP   A CB   1 
ATOM   2147 C  CG   A ASP   A 1 105 ? 24.705 -10.090 -14.201 0.60 30.96 ?  105 ASP   A CG   1 
ATOM   2148 C  CG   B ASP   A 1 105 ? 25.281 -10.603 -13.872 0.40 23.24 ?  105 ASP   A CG   1 
ATOM   2149 O  OD1  A ASP   A 1 105 ? 23.476 -10.292 -14.298 0.60 31.37 ?  105 ASP   A OD1  1 
ATOM   2150 O  OD1  B ASP   A 1 105 ? 24.076 -10.912 -13.986 0.40 23.40 ?  105 ASP   A OD1  1 
ATOM   2151 O  OD2  A ASP   A 1 105 ? 25.559 -10.994 -14.324 0.60 32.33 -1 105 ASP   A OD2  1 
ATOM   2152 O  OD2  B ASP   A 1 105 ? 26.211 -11.438 -13.904 0.40 23.80 -1 105 ASP   A OD2  1 
ATOM   2153 H  H    A ASP   A 1 105 ? 25.408 -6.343  -13.460 0.60 30.44 ?  105 ASP   A H    1 
ATOM   2154 H  H    B ASP   A 1 105 ? 25.747 -6.787  -13.402 0.40 23.84 ?  105 ASP   A H    1 
ATOM   2155 H  HA   A ASP   A 1 105 ? 23.379 -7.777  -14.307 0.60 31.39 ?  105 ASP   A HA   1 
ATOM   2156 H  HA   B ASP   A 1 105 ? 23.866 -8.345  -14.316 0.40 24.38 ?  105 ASP   A HA   1 
ATOM   2157 H  HB2  A ASP   A 1 105 ? 25.629 -8.362  -14.727 0.60 34.60 ?  105 ASP   A HB2  1 
ATOM   2158 H  HB2  B ASP   A 1 105 ? 26.172 -8.856  -14.441 0.40 26.42 ?  105 ASP   A HB2  1 
ATOM   2159 H  HB3  A ASP   A 1 105 ? 25.807 -8.697  -13.184 0.60 34.60 ?  105 ASP   A HB3  1 
ATOM   2160 H  HB3  B ASP   A 1 105 ? 26.180 -9.099  -12.871 0.40 26.42 ?  105 ASP   A HB3  1 
ATOM   2161 N  N    A ILE   A 1 106 ? 22.057 -8.488  -12.374 0.60 23.16 ?  106 ILE   A N    1 
ATOM   2162 N  N    B ILE   A 1 106 ? 22.380 -9.055  -12.524 0.40 20.02 ?  106 ILE   A N    1 
ATOM   2163 C  CA   A ILE   A 1 106 ? 21.309 -8.901  -11.192 0.60 22.12 ?  106 ILE   A CA   1 
ATOM   2164 C  CA   B ILE   A 1 106 ? 21.516 -9.447  -11.416 0.40 20.62 ?  106 ILE   A CA   1 
ATOM   2165 C  C    A ILE   A 1 106 ? 21.845 -10.200 -10.614 0.60 20.77 ?  106 ILE   A C    1 
ATOM   2166 C  C    B ILE   A 1 106 ? 22.068 -10.670 -10.692 0.40 20.40 ?  106 ILE   A C    1 
ATOM   2167 O  O    A ILE   A 1 106 ? 21.647 -10.474 -9.426  0.60 20.28 ?  106 ILE   A O    1 
ATOM   2168 O  O    B ILE   A 1 106 ? 21.809 -10.859 -9.496  0.40 20.65 ?  106 ILE   A O    1 
ATOM   2169 C  CB   A ILE   A 1 106 ? 19.798 -8.992  -11.503 0.60 22.99 ?  106 ILE   A CB   1 
ATOM   2170 C  CB   B ILE   A 1 106 ? 20.076 -9.657  -11.928 0.40 21.71 ?  106 ILE   A CB   1 
ATOM   2171 C  CG1  A ILE   A 1 106 ? 18.983 -9.078  -10.211 0.60 23.57 ?  106 ILE   A CG1  1 
ATOM   2172 C  CG1  B ILE   A 1 106 ? 19.105 -9.845  -10.760 0.40 22.10 ?  106 ILE   A CG1  1 
ATOM   2173 C  CG2  A ILE   A 1 106 ? 19.499 -10.207 -12.365 0.60 23.49 ?  106 ILE   A CG2  1 
ATOM   2174 C  CG2  B ILE   A 1 106 ? 20.015 -10.828 -12.903 0.40 22.01 ?  106 ILE   A CG2  1 
ATOM   2175 C  CD1  A ILE   A 1 106 ? 19.209 -7.923  -9.268  0.60 23.48 ?  106 ILE   A CD1  1 
ATOM   2176 C  CD1  B ILE   A 1 106 ? 18.908 -8.592  -9.931  0.40 22.37 ?  106 ILE   A CD1  1 
ATOM   2177 H  H    A ILE   A 1 106 ? 21.598 -8.471  -13.097 0.60 27.95 ?  106 ILE   A H    1 
ATOM   2178 H  H    B ILE   A 1 106 ? 22.017 -9.119  -13.299 0.40 24.19 ?  106 ILE   A H    1 
ATOM   2179 H  HA   A ILE   A 1 106 ? 21.433 -8.223  -10.518 0.60 26.70 ?  106 ILE   A HA   1 
ATOM   2180 H  HA   B ILE   A 1 106 ? 21.495 -8.725  -10.776 0.40 24.91 ?  106 ILE   A HA   1 
ATOM   2181 H  HB   A ILE   A 1 106 ? 19.531 -8.195  -11.988 0.60 27.75 ?  106 ILE   A HB   1 
ATOM   2182 H  HB   B ILE   A 1 106 ? 19.812 -8.858  -12.407 0.40 26.21 ?  106 ILE   A HB   1 
ATOM   2183 H  HG12 A ILE   A 1 106 ? 18.039 -9.092  -10.438 0.60 28.45 ?  106 ILE   A HG12 1 
ATOM   2184 H  HG12 B ILE   A 1 106 ? 18.239 -10.105 -11.114 0.40 26.68 ?  106 ILE   A HG12 1 
ATOM   2185 H  HG13 A ILE   A 1 106 ? 19.219 -9.894  -9.745  0.60 28.45 ?  106 ILE   A HG13 1 
ATOM   2186 H  HG13 B ILE   A 1 106 ? 19.440 -10.541 -10.175 0.40 26.68 ?  106 ILE   A HG13 1 
ATOM   2187 H  HG21 A ILE   A 1 106 ? 18.609 -10.116 -12.737 0.60 28.35 ?  106 ILE   A HG21 1 
ATOM   2188 H  HG21 B ILE   A 1 106 ? 19.119 -10.884 -13.271 0.40 26.58 ?  106 ILE   A HG21 1 
ATOM   2189 H  HG22 A ILE   A 1 106 ? 20.155 -10.252 -13.077 0.60 28.35 ?  106 ILE   A HG22 1 
ATOM   2190 H  HG22 B ILE   A 1 106 ? 20.654 -10.678 -13.619 0.40 26.58 ?  106 ILE   A HG22 1 
ATOM   2191 H  HG23 A ILE   A 1 106 ? 19.550 -11.004 -11.815 0.60 28.35 ?  106 ILE   A HG23 1 
ATOM   2192 H  HG23 B ILE   A 1 106 ? 20.231 -11.647 -12.434 0.40 26.58 ?  106 ILE   A HG23 1 
ATOM   2193 H  HD11 A ILE   A 1 106 ? 18.470 -7.876  -8.645  0.60 28.34 ?  106 ILE   A HD11 1 
ATOM   2194 H  HD11 B ILE   A 1 106 ? 18.171 -8.736  -9.318  0.40 27.01 ?  106 ILE   A HD11 1 
ATOM   2195 H  HD12 A ILE   A 1 106 ? 20.040 -8.066  -8.786  0.60 28.34 ?  106 ILE   A HD12 1 
ATOM   2196 H  HD12 B ILE   A 1 106 ? 19.721 -8.411  -9.436  0.40 27.01 ?  106 ILE   A HD12 1 
ATOM   2197 H  HD13 A ILE   A 1 106 ? 19.262 -7.102  -9.782  0.60 28.34 ?  106 ILE   A HD13 1 
ATOM   2198 H  HD13 B ILE   A 1 106 ? 18.706 -7.852  -10.524 0.40 27.01 ?  106 ILE   A HD13 1 
ATOM   2199 N  N    A GLN   A 1 107 ? 22.532 -11.008 -11.428 0.60 21.78 ?  107 GLN   A N    1 
ATOM   2200 N  N    B GLN   A 1 107 ? 22.838 -11.515 -11.389 0.40 20.30 ?  107 GLN   A N    1 
ATOM   2201 C  CA   A GLN   A 1 107 ? 23.147 -12.232 -10.928 0.60 23.31 ?  107 GLN   A CA   1 
ATOM   2202 C  CA   B GLN   A 1 107 ? 23.471 -12.655 -10.730 0.40 21.46 ?  107 GLN   A CA   1 
ATOM   2203 C  C    A GLN   A 1 107 ? 24.141 -11.955 -9.809  0.60 21.30 ?  107 GLN   A C    1 
ATOM   2204 C  C    B GLN   A 1 107 ? 24.365 -12.205 -9.582  0.40 19.33 ?  107 GLN   A C    1 
ATOM   2205 O  O    A GLN   A 1 107 ? 24.385 -12.838 -8.981  0.60 22.93 ?  107 GLN   A O    1 
ATOM   2206 O  O    B GLN   A 1 107 ? 24.578 -12.957 -8.622  0.40 19.43 ?  107 GLN   A O    1 
ATOM   2207 C  CB   A GLN   A 1 107 ? 23.841 -12.977 -12.075 0.60 27.10 ?  107 GLN   A CB   1 
ATOM   2208 C  CB   B GLN   A 1 107 ? 24.283 -13.463 -11.746 0.40 24.70 ?  107 GLN   A CB   1 
ATOM   2209 C  CG   A GLN   A 1 107 ? 22.940 -13.255 -13.272 0.60 30.94 ?  107 GLN   A CG   1 
ATOM   2210 C  CG   B GLN   A 1 107 ? 23.465 -13.992 -12.911 0.40 27.68 ?  107 GLN   A CG   1 
ATOM   2211 C  CD   A GLN   A 1 107 ? 21.691 -14.024 -12.896 0.60 34.06 ?  107 GLN   A CD   1 
ATOM   2212 C  CD   B GLN   A 1 107 ? 22.411 -14.989 -12.474 0.40 30.23 ?  107 GLN   A CD   1 
ATOM   2213 O  OE1  A GLN   A 1 107 ? 21.758 -15.047 -12.215 0.60 35.33 ?  107 GLN   A OE1  1 
ATOM   2214 O  OE1  B GLN   A 1 107 ? 22.626 -15.774 -11.551 0.40 31.05 ?  107 GLN   A OE1  1 
ATOM   2215 N  NE2  A GLN   A 1 107 ? 20.540 -13.528 -13.332 0.60 35.09 ?  107 GLN   A NE2  1 
ATOM   2216 N  NE2  B GLN   A 1 107 ? 21.259 -14.956 -13.132 0.40 30.96 ?  107 GLN   A NE2  1 
ATOM   2217 H  H    A GLN   A 1 107 ? 22.663 -10.865 -12.263 0.60 26.31 ?  107 GLN   A H    1 
ATOM   2218 H  H    B GLN   A 1 107 ? 23.007 -11.451 -12.231 0.40 24.53 ?  107 GLN   A H    1 
ATOM   2219 H  HA   A GLN   A 1 107 ? 22.460 -12.814 -10.572 0.60 28.13 ?  107 GLN   A HA   1 
ATOM   2220 H  HA   B GLN   A 1 107 ? 22.786 -13.237 -10.369 0.40 25.91 ?  107 GLN   A HA   1 
ATOM   2221 H  HB2  A GLN   A 1 107 ? 24.589 -12.445 -12.390 0.60 32.68 ?  107 GLN   A HB2  1 
ATOM   2222 H  HB2  B GLN   A 1 107 ? 24.983 -12.899 -12.111 0.40 29.81 ?  107 GLN   A HB2  1 
ATOM   2223 H  HB3  A GLN   A 1 107 ? 24.164 -13.832 -11.749 0.60 32.68 ?  107 GLN   A HB3  1 
ATOM   2224 H  HB3  B GLN   A 1 107 ? 24.680 -14.228 -11.298 0.40 29.81 ?  107 GLN   A HB3  1 
ATOM   2225 H  HG2  A GLN   A 1 107 ? 22.665 -12.414 -13.667 0.60 37.29 ?  107 GLN   A HG2  1 
ATOM   2226 H  HG2  B GLN   A 1 107 ? 23.017 -13.251 -13.348 0.40 33.39 ?  107 GLN   A HG2  1 
ATOM   2227 H  HG3  A GLN   A 1 107 ? 23.433 -13.780 -13.924 0.60 37.29 ?  107 GLN   A HG3  1 
ATOM   2228 H  HG3  B GLN   A 1 107 ? 24.058 -14.437 -13.539 0.40 33.39 ?  107 GLN   A HG3  1 
ATOM   2229 H  HE21 A GLN   A 1 107 ? 20.533 -12.810 -13.804 0.60 42.27 ?  107 GLN   A HE21 1 
ATOM   2230 H  HE21 B GLN   A 1 107 ? 21.146 -14.392 -13.770 0.40 37.32 ?  107 GLN   A HE21 1 
ATOM   2231 H  HE22 A GLN   A 1 107 ? 19.803 -13.929 -13.145 0.60 42.27 ?  107 GLN   A HE22 1 
ATOM   2232 H  HE22 B GLN   A 1 107 ? 20.629 -15.502 -12.922 0.40 37.32 ?  107 GLN   A HE22 1 
ATOM   2233 N  N    A LEU   A 1 108 ? 24.702 -10.744 -9.749  0.60 17.27 ?  108 LEU   A N    1 
ATOM   2234 N  N    B LEU   A 1 108 ? 24.886 -10.979 -9.657  0.40 17.37 ?  108 LEU   A N    1 
ATOM   2235 C  CA   A LEU   A 1 108 ? 25.648 -10.405 -8.692  0.60 15.02 ?  108 LEU   A CA   1 
ATOM   2236 C  CA   B LEU   A 1 108 ? 25.728 -10.440 -8.599  0.40 15.75 ?  108 LEU   A CA   1 
ATOM   2237 C  C    A LEU   A 1 108 ? 24.972 -10.248 -7.339  0.60 13.36 ?  108 LEU   A C    1 
ATOM   2238 C  C    B LEU   A 1 108 ? 24.975 -10.233 -7.293  0.40 13.98 ?  108 LEU   A C    1 
ATOM   2239 O  O    A LEU   A 1 108 ? 25.666 -10.111 -6.329  0.60 13.33 ?  108 LEU   A O    1 
ATOM   2240 O  O    B LEU   A 1 108 ? 25.621 -10.028 -6.261  0.40 14.12 ?  108 LEU   A O    1 
ATOM   2241 C  CB   A LEU   A 1 108 ? 26.431 -9.142  -9.065  0.60 14.81 ?  108 LEU   A CB   1 
ATOM   2242 C  CB   B LEU   A 1 108 ? 26.386 -9.133  -9.055  0.40 15.84 ?  108 LEU   A CB   1 
ATOM   2243 C  CG   A LEU   A 1 108 ? 27.379 -9.355  -10.247 0.60 16.54 ?  108 LEU   A CG   1 
ATOM   2244 C  CG   B LEU   A 1 108 ? 27.486 -9.311  -10.103 0.40 16.96 ?  108 LEU   A CG   1 
ATOM   2245 C  CD1  A LEU   A 1 108 ? 27.937 -8.034  -10.751 0.60 17.63 ?  108 LEU   A CD1  1 
ATOM   2246 C  CD1  B LEU   A 1 108 ? 27.859 -7.979  -10.733 0.40 17.69 ?  108 LEU   A CD1  1 
ATOM   2247 C  CD2  A LEU   A 1 108 ? 28.513 -10.300 -9.865  0.60 17.65 ?  108 LEU   A CD2  1 
ATOM   2248 C  CD2  B LEU   A 1 108 ? 28.709 -9.961  -9.474  0.40 17.62 ?  108 LEU   A CD2  1 
ATOM   2249 H  H    A LEU   A 1 108 ? 24.543 -10.110 -10.300 0.60 20.89 ?  108 LEU   A H    1 
ATOM   2250 H  H    B LEU   A 1 108 ? 24.766 -10.447 -10.315 0.40 21.00 ?  108 LEU   A H    1 
ATOM   2251 H  HA   A LEU   A 1 108 ? 26.284 -11.130 -8.606  0.60 18.18 ?  108 LEU   A HA   1 
ATOM   2252 H  HA   B LEU   A 1 108 ? 26.436 -11.074 -8.418  0.40 19.06 ?  108 LEU   A HA   1 
ATOM   2253 H  HB2  A LEU   A 1 108 ? 25.805 -8.443  -9.308  0.60 17.93 ?  108 LEU   A HB2  1 
ATOM   2254 H  HB2  B LEU   A 1 108 ? 25.708 -8.554  -9.434  0.40 19.17 ?  108 LEU   A HB2  1 
ATOM   2255 H  HB3  A LEU   A 1 108 ? 26.961 -8.864  -8.303  0.60 17.93 ?  108 LEU   A HB3  1 
ATOM   2256 H  HB3  B LEU   A 1 108 ? 26.786 -8.703  -8.284  0.40 19.17 ?  108 LEU   A HB3  1 
ATOM   2257 H  HG   A LEU   A 1 108 ? 26.885 -9.766  -10.974 0.60 20.02 ?  108 LEU   A HG   1 
ATOM   2258 H  HG   B LEU   A 1 108 ? 27.164 -9.897  -10.807 0.40 20.51 ?  108 LEU   A HG   1 
ATOM   2259 H  HD11 A LEU   A 1 108 ? 28.526 -8.206  -11.505 0.60 21.32 ?  108 LEU   A HD11 1 
ATOM   2260 H  HD11 B LEU   A 1 108 ? 28.502 -8.135  -11.445 0.40 21.40 ?  108 LEU   A HD11 1 
ATOM   2261 H  HD12 A LEU   A 1 108 ? 27.202 -7.466  -11.032 0.60 21.32 ?  108 LEU   A HD12 1 
ATOM   2262 H  HD12 B LEU   A 1 108 ? 27.060 -7.566  -11.095 0.40 21.40 ?  108 LEU   A HD12 1 
ATOM   2263 H  HD13 A LEU   A 1 108 ? 28.433 -7.605  -10.037 0.60 21.32 ?  108 LEU   A HD13 1 
ATOM   2264 H  HD13 B LEU   A 1 108 ? 28.250 -7.407  -10.055 0.40 21.40 ?  108 LEU   A HD13 1 
ATOM   2265 H  HD21 A LEU   A 1 108 ? 29.200 -10.255 -10.545 0.60 21.35 ?  108 LEU   A HD21 1 
ATOM   2266 H  HD21 B LEU   A 1 108 ? 29.442 -9.932  -10.107 0.40 21.30 ?  108 LEU   A HD21 1 
ATOM   2267 H  HD22 A LEU   A 1 108 ? 28.874 -10.022 -9.008  0.60 21.35 ?  108 LEU   A HD22 1 
ATOM   2268 H  HD22 B LEU   A 1 108 ? 28.945 -9.473  -8.670  0.40 21.30 ?  108 LEU   A HD22 1 
ATOM   2269 H  HD23 A LEU   A 1 108 ? 28.165 -11.202 -9.801  0.60 21.35 ?  108 LEU   A HD23 1 
ATOM   2270 H  HD23 B LEU   A 1 108 ? 28.500 -10.882 -9.252  0.40 21.30 ?  108 LEU   A HD23 1 
ATOM   2271 N  N    . LEU   A 1 109 ? 23.641 -10.298 -7.296  1.00 13.08 ?  109 LEU   A N    1 
ATOM   2272 C  CA   . LEU   A 1 109 ? 22.929 -10.178 -6.032  1.00 12.14 ?  109 LEU   A CA   1 
ATOM   2273 C  C    . LEU   A 1 109 ? 23.274 -11.328 -5.092  1.00 11.70 ?  109 LEU   A C    1 
ATOM   2274 O  O    . LEU   A 1 109 ? 23.411 -11.126 -3.881  1.00 12.21 ?  109 LEU   A O    1 
ATOM   2275 C  CB   . LEU   A 1 109 ? 21.428 -10.105 -6.295  1.00 13.41 ?  109 LEU   A CB   1 
ATOM   2276 C  CG   . LEU   A 1 109 ? 20.533 -9.809  -5.093  1.00 13.43 ?  109 LEU   A CG   1 
ATOM   2277 C  CD1  . LEU   A 1 109 ? 20.991 -8.544  -4.376  1.00 13.62 ?  109 LEU   A CD1  1 
ATOM   2278 C  CD2  . LEU   A 1 109 ? 19.077 -9.679  -5.531  1.00 14.61 ?  109 LEU   A CD2  1 
ATOM   2279 H  H    A LEU   A 1 109 ? 23.129 -10.394 -7.981  0.60 15.86 ?  109 LEU   A H    1 
ATOM   2280 H  H    B LEU   A 1 109 ? 23.143 -10.406 -7.990  0.40 15.86 ?  109 LEU   A H    1 
ATOM   2281 H  HA   . LEU   A 1 109 ? 23.199 -9.353  -5.603  1.00 14.73 ?  109 LEU   A HA   1 
ATOM   2282 H  HB2  . LEU   A 1 109 ? 21.270 -9.405  -6.949  1.00 16.25 ?  109 LEU   A HB2  1 
ATOM   2283 H  HB3  . LEU   A 1 109 ? 21.142 -10.955 -6.662  1.00 16.25 ?  109 LEU   A HB3  1 
ATOM   2284 H  HG   . LEU   A 1 109 ? 20.593 -10.545 -4.469  1.00 16.28 ?  109 LEU   A HG   1 
ATOM   2285 H  HD11 . LEU   A 1 109 ? 20.305 -8.263  -3.756  1.00 16.50 ?  109 LEU   A HD11 1 
ATOM   2286 H  HD12 . LEU   A 1 109 ? 21.816 -8.731  -3.897  1.00 16.50 ?  109 LEU   A HD12 1 
ATOM   2287 H  HD13 . LEU   A 1 109 ? 21.147 -7.844  -5.035  1.00 16.50 ?  109 LEU   A HD13 1 
ATOM   2288 H  HD21 . LEU   A 1 109 ? 18.542 -9.387  -4.774  1.00 17.70 ?  109 LEU   A HD21 1 
ATOM   2289 H  HD22 . LEU   A 1 109 ? 19.013 -9.031  -6.249  1.00 17.70 ?  109 LEU   A HD22 1 
ATOM   2290 H  HD23 . LEU   A 1 109 ? 18.758 -10.545 -5.840  1.00 17.70 ?  109 LEU   A HD23 1 
ATOM   2291 N  N    . LYS   A 1 110 ? 23.432 -12.544 -5.624  1.00 11.50 ?  110 LYS   A N    1 
ATOM   2292 C  CA   . LYS   A 1 110 ? 23.808 -13.663 -4.765  1.00 11.75 ?  110 LYS   A CA   1 
ATOM   2293 C  C    . LYS   A 1 110 ? 25.189 -13.440 -4.158  1.00 11.17 ?  110 LYS   A C    1 
ATOM   2294 O  O    . LYS   A 1 110 ? 25.385 -13.639 -2.956  1.00 11.56 ?  110 LYS   A O    1 
ATOM   2295 C  CB   . LYS   A 1 110 ? 23.730 -14.985 -5.529  1.00 12.67 ?  110 LYS   A CB   1 
ATOM   2296 C  CG   . LYS   A 1 110 ? 23.931 -16.196 -4.623  1.00 12.93 ?  110 LYS   A CG   1 
ATOM   2297 C  CD   . LYS   A 1 110 ? 23.696 -17.516 -5.340  1.00 13.63 ?  110 LYS   A CD   1 
ATOM   2298 C  CE   . LYS   A 1 110 ? 23.813 -18.695 -4.392  1.00 14.09 ?  110 LYS   A CE   1 
ATOM   2299 N  NZ   . LYS   A 1 110 ? 22.624 -18.842 -3.517  1.00 14.33 ?  110 LYS   A NZ   1 
ATOM   2300 H  H    . LYS   A 1 110 ? 23.331 -12.741 -6.454  1.00 13.96 ?  110 LYS   A H    1 
ATOM   2301 H  HA   . LYS   A 1 110 ? 23.166 -13.714 -4.035  1.00 14.26 ?  110 LYS   A HA   1 
ATOM   2302 H  HB2  . LYS   A 1 110 ? 22.855 -15.065 -5.945  1.00 15.37 ?  110 LYS   A HB2  1 
ATOM   2303 H  HB3  . LYS   A 1 110 ? 24.422 -15.003 -6.205  1.00 15.37 ?  110 LYS   A HB3  1 
ATOM   2304 H  HG2  . LYS   A 1 110 ? 24.837 -16.194 -4.284  1.00 15.68 ?  110 LYS   A HG2  1 
ATOM   2305 H  HG3  . LYS   A 1 110 ? 23.300 -16.144 -3.884  1.00 15.68 ?  110 LYS   A HG3  1 
ATOM   2306 H  HD2  . LYS   A 1 110 ? 22.807 -17.522 -5.721  1.00 16.52 ?  110 LYS   A HD2  1 
ATOM   2307 H  HD3  . LYS   A 1 110 ? 24.363 -17.620 -6.037  1.00 16.52 ?  110 LYS   A HD3  1 
ATOM   2308 H  HE2  . LYS   A 1 110 ? 23.913 -19.509 -4.907  1.00 17.07 ?  110 LYS   A HE2  1 
ATOM   2309 H  HE3  . LYS   A 1 110 ? 24.591 -18.566 -3.821  1.00 17.07 ?  110 LYS   A HE3  1 
ATOM   2310 H  HZ1  . LYS   A 1 110 ? 22.725 -19.538 -2.976  1.00 17.36 ?  110 LYS   A HZ1  1 
ATOM   2311 H  HZ2  . LYS   A 1 110 ? 22.513 -18.106 -3.027  1.00 17.36 ?  110 LYS   A HZ2  1 
ATOM   2312 H  HZ3  . LYS   A 1 110 ? 21.895 -18.965 -4.016  1.00 17.36 ?  110 LYS   A HZ3  1 
ATOM   2313 N  N    . SER   A 1 111 ? 26.151 -12.998 -4.973  1.00 11.28 ?  111 SER   A N    1 
ATOM   2314 C  CA   . SER   A 1 111 ? 27.480 -12.686 -4.454  1.00 11.60 ?  111 SER   A CA   1 
ATOM   2315 C  C    . SER   A 1 111 ? 27.413 -11.636 -3.349  1.00 11.06 ?  111 SER   A C    1 
ATOM   2316 O  O    . SER   A 1 111 ? 28.107 -11.738 -2.332  1.00 11.70 ?  111 SER   A O    1 
ATOM   2317 C  CB   . SER   A 1 111 ? 28.373 -12.195 -5.594  1.00 13.16 ?  111 SER   A CB   1 
ATOM   2318 O  OG   . SER   A 1 111 ? 28.476 -13.177 -6.611  1.00 14.91 ?  111 SER   A OG   1 
ATOM   2319 H  H    . SER   A 1 111 ? 26.050 -12.875 -5.817  1.00 13.71 ?  111 SER   A H    1 
ATOM   2320 H  HA   . SER   A 1 111 ? 27.872 -13.493 -4.088  1.00 14.08 ?  111 SER   A HA   1 
ATOM   2321 H  HB2  . SER   A 1 111 ? 27.981 -11.396 -5.981  1.00 15.96 ?  111 SER   A HB2  1 
ATOM   2322 H  HB3  . SER   A 1 111 ? 29.252 -11.995 -5.239  1.00 15.96 ?  111 SER   A HB3  1 
ATOM   2323 H  HG   . SER   A 1 111 ? 28.991 -12.898 -7.224  1.00 18.05 ?  111 SER   A HG   1 
ATOM   2324 N  N    . ALA   A 1 112 ? 26.566 -10.621 -3.530  1.00 11.29 ?  112 ALA   A N    1 
ATOM   2325 C  CA   . ALA   A 1 112 ? 26.415 -9.584  -2.513  1.00 10.98 ?  112 ALA   A CA   1 
ATOM   2326 C  C    . ALA   A 1 112 ? 25.937 -10.182 -1.191  1.00 10.82 ?  112 ALA   A C    1 
ATOM   2327 O  O    . ALA   A 1 112 ? 26.484 -9.887  -0.124  1.00 11.17 ?  112 ALA   A O    1 
ATOM   2328 C  CB   . ALA   A 1 112 ? 25.454 -8.499  -3.008  1.00 11.38 ?  112 ALA   A CB   1 
ATOM   2329 H  H    . ALA   A 1 112 ? 26.075 -10.508 -4.226  1.00 13.71 ?  112 ALA   A H    1 
ATOM   2330 H  HA   . ALA   A 1 112 ? 27.277 -9.165  -2.356  1.00 13.35 ?  112 ALA   A HA   1 
ATOM   2331 H  HB1  . ALA   A 1 112 ? 25.390 -7.797  -2.333  1.00 13.83 ?  112 ALA   A HB1  1 
ATOM   2332 H  HB2  . ALA   A 1 112 ? 25.795 -8.122  -3.834  1.00 13.83 ?  112 ALA   A HB2  1 
ATOM   2333 H  HB3  . ALA   A 1 112 ? 24.579 -8.889  -3.157  1.00 13.83 ?  112 ALA   A HB3  1 
ATOM   2334 N  N    . TYR   A 1 113 ? 24.903 -11.029 -1.241  1.00 10.84 ?  113 TYR   A N    1 
ATOM   2335 C  CA   . TYR   A 1 113 ? 24.389 -11.640 -0.016  1.00 10.75 ?  113 TYR   A CA   1 
ATOM   2336 C  C    . TYR   A 1 113 ? 25.392 -12.591 0.634   1.00 10.27 ?  113 TYR   A C    1 
ATOM   2337 O  O    . TYR   A 1 113 ? 25.356 -12.771 1.855   1.00 11.11 ?  113 TYR   A O    1 
ATOM   2338 C  CB   . TYR   A 1 113 ? 23.077 -12.371 -0.301  1.00 11.21 ?  113 TYR   A CB   1 
ATOM   2339 C  CG   . TYR   A 1 113 ? 21.856 -11.483 -0.214  1.00 11.31 ?  113 TYR   A CG   1 
ATOM   2340 C  CD1  . TYR   A 1 113 ? 21.488 -10.898 0.991   1.00 11.63 ?  113 TYR   A CD1  1 
ATOM   2341 C  CD2  . TYR   A 1 113 ? 21.053 -11.251 -1.325  1.00 11.66 ?  113 TYR   A CD2  1 
ATOM   2342 C  CE1  . TYR   A 1 113 ? 20.359 -10.103 1.090   1.00 11.88 ?  113 TYR   A CE1  1 
ATOM   2343 C  CE2  . TYR   A 1 113 ? 19.904 -10.452 -1.233  1.00 11.82 ?  113 TYR   A CE2  1 
ATOM   2344 C  CZ   . TYR   A 1 113 ? 19.571 -9.887  -0.022  1.00 11.58 ?  113 TYR   A CZ   1 
ATOM   2345 O  OH   . TYR   A 1 113 ? 18.441 -9.098  0.098   1.00 12.48 ?  113 TYR   A OH   1 
ATOM   2346 H  H    . TYR   A 1 113 ? 24.497 -11.261 -1.962  1.00 13.18 ?  113 TYR   A H    1 
ATOM   2347 H  HA   . TYR   A 1 113 ? 24.207 -10.936 0.621   1.00 13.07 ?  113 TYR   A HA   1 
ATOM   2348 H  HB2  . TYR   A 1 113 ? 23.109 -12.734 -1.199  1.00 13.62 ?  113 TYR   A HB2  1 
ATOM   2349 H  HB3  . TYR   A 1 113 ? 22.972 -13.083 0.343   1.00 13.62 ?  113 TYR   A HB3  1 
ATOM   2350 H  HD1  . TYR   A 1 113 ? 22.013 -11.050 1.746   1.00 14.12 ?  113 TYR   A HD1  1 
ATOM   2351 H  HD2  . TYR   A 1 113 ? 21.271 -11.640 -2.140  1.00 14.15 ?  113 TYR   A HD2  1 
ATOM   2352 H  HE1  . TYR   A 1 113 ? 20.129 -9.723  1.906   1.00 14.42 ?  113 TYR   A HE1  1 
ATOM   2353 H  HE2  . TYR   A 1 113 ? 19.369 -10.302 -1.981  1.00 14.34 ?  113 TYR   A HE2  1 
ATOM   2354 H  HH   . TYR   A 1 113 ? 18.054 -9.049  -0.653  1.00 15.14 ?  113 TYR   A HH   1 
ATOM   2355 N  N    . GLU   A 1 114 ? 26.298 -13.198 -0.149  1.00 10.70 ?  114 GLU   A N    1 
ATOM   2356 C  CA   . GLU   A 1 114 ? 27.290 -14.097 0.441   1.00 10.94 ?  114 GLU   A CA   1 
ATOM   2357 C  C    . GLU   A 1 114 ? 28.135 -13.385 1.492   1.00 10.70 ?  114 GLU   A C    1 
ATOM   2358 O  O    . GLU   A 1 114 ? 28.616 -14.024 2.437   1.00 11.11 ?  114 GLU   A O    1 
ATOM   2359 C  CB   . GLU   A 1 114 ? 28.157 -14.734 -0.653  1.00 11.21 ?  114 GLU   A CB   1 
ATOM   2360 C  CG   . GLU   A 1 114 ? 27.398 -15.787 -1.429  1.00 11.63 ?  114 GLU   A CG   1 
ATOM   2361 C  CD   . GLU   A 1 114 ? 28.111 -16.317 -2.667  1.00 12.10 ?  114 GLU   A CD   1 
ATOM   2362 O  OE1  . GLU   A 1 114 ? 29.066 -15.682 -3.170  1.00 12.32 ?  114 GLU   A OE1  1 
ATOM   2363 O  OE2  . GLU   A 1 114 ? 27.670 -17.384 -3.154  1.00 13.30 -1 114 GLU   A OE2  1 
ATOM   2364 H  H    . GLU   A 1 114 ? 26.360 -13.098 -1.011  1.00 13.00 ?  114 GLU   A H    1 
ATOM   2365 H  HA   . GLU   A 1 114 ? 26.818 -14.809 0.884   1.00 13.29 ?  114 GLU   A HA   1 
ATOM   2366 H  HB2  . GLU   A 1 114 ? 28.444 -14.050 -1.283  1.00 13.62 ?  114 GLU   A HB2  1 
ATOM   2367 H  HB3  . GLU   A 1 114 ? 28.927 -15.157 -0.247  1.00 13.62 ?  114 GLU   A HB3  1 
ATOM   2368 H  HG2  . GLU   A 1 114 ? 27.238 -16.544 -0.845  1.00 14.12 ?  114 GLU   A HG2  1 
ATOM   2369 H  HG3  . GLU   A 1 114 ? 26.552 -15.412 -1.716  1.00 14.12 ?  114 GLU   A HG3  1 
ATOM   2370 N  N    . ASN   A 1 115 ? 28.318 -12.065 1.361   1.00 10.60 ?  115 ASN   A N    1 
ATOM   2371 C  CA   . ASN   A 1 115 ? 29.088 -11.337 2.366   1.00 10.92 ?  115 ASN   A CA   1 
ATOM   2372 C  C    . ASN   A 1 115 ? 28.475 -11.468 3.754   1.00 10.66 ?  115 ASN   A C    1 
ATOM   2373 O  O    . ASN   A 1 115 ? 29.190 -11.397 4.759   1.00 11.13 ?  115 ASN   A O    1 
ATOM   2374 C  CB   . ASN   A 1 115 ? 29.199 -9.860  1.989   1.00 11.20 ?  115 ASN   A CB   1 
ATOM   2375 C  CG   . ASN   A 1 115 ? 29.988 -9.641  0.722   1.00 11.96 ?  115 ASN   A CG   1 
ATOM   2376 O  OD1  . ASN   A 1 115 ? 31.205 -9.744  0.730   1.00 15.14 ?  115 ASN   A OD1  1 
ATOM   2377 N  ND2  . ASN   A 1 115 ? 29.311 -9.335  -0.363  1.00 11.36 ?  115 ASN   A ND2  1 
ATOM   2378 H  H    . ASN   A 1 115 ? 28.010 -11.575 0.719   1.00 12.89 ?  115 ASN   A H    1 
ATOM   2379 H  HA   . ASN   A 1 115 ? 29.981 -11.704 2.400   1.00 13.27 ?  115 ASN   A HA   1 
ATOM   2380 H  HB2  . ASN   A 1 115 ? 28.308 -9.496  1.868   1.00 13.61 ?  115 ASN   A HB2  1 
ATOM   2381 H  HB3  . ASN   A 1 115 ? 29.649 -9.387  2.713   1.00 13.61 ?  115 ASN   A HB3  1 
ATOM   2382 H  HD21 . ASN   A 1 115 ? 29.723 -9.200  -1.103  1.00 13.79 ?  115 ASN   A HD21 1 
ATOM   2383 H  HD22 . ASN   A 1 115 ? 28.451 -9.281  -0.333  1.00 13.79 ?  115 ASN   A HD22 1 
ATOM   2384 N  N    . PHE   A 1 116 ? 27.150 -11.637 3.834   1.00 11.01 ?  116 PHE   A N    1 
ATOM   2385 C  CA   . PHE   A 1 116 ? 26.494 -11.737 5.134   1.00 10.88 ?  116 PHE   A CA   1 
ATOM   2386 C  C    . PHE   A 1 116 ? 26.968 -12.969 5.904   1.00 11.07 ?  116 PHE   A C    1 
ATOM   2387 O  O    . PHE   A 1 116 ? 26.900 -12.989 7.133   1.00 11.54 ?  116 PHE   A O    1 
ATOM   2388 C  CB   . PHE   A 1 116 ? 24.969 -11.865 4.989   1.00 11.09 ?  116 PHE   A CB   1 
ATOM   2389 C  CG   . PHE   A 1 116 ? 24.215 -10.616 4.534   1.00 10.73 ?  116 PHE   A CG   1 
ATOM   2390 C  CD1  . PHE   A 1 116 ? 24.786 -9.590  3.794   1.00 10.93 ?  116 PHE   A CD1  1 
ATOM   2391 C  CD2  . PHE   A 1 116 ? 22.864 -10.518 4.849   1.00 11.30 ?  116 PHE   A CD2  1 
ATOM   2392 C  CE1  . PHE   A 1 116 ? 24.017 -8.514  3.381   1.00 11.08 ?  116 PHE   A CE1  1 
ATOM   2393 C  CE2  . PHE   A 1 116 ? 22.097 -9.446  4.449   1.00 11.75 ?  116 PHE   A CE2  1 
ATOM   2394 C  CZ   . PHE   A 1 116 ? 22.667 -8.437  3.714   1.00 11.42 ?  116 PHE   A CZ   1 
ATOM   2395 H  H    . PHE   A 1 116 ? 26.616 -11.683 3.154   1.00 13.38 ?  116 PHE   A H    1 
ATOM   2396 H  HA   . PHE   A 1 116 ? 26.689 -10.946 5.658   1.00 13.22 ?  116 PHE   A HA   1 
ATOM   2397 H  HB2  . PHE   A 1 116 ? 24.785 -12.564 4.341   1.00 13.47 ?  116 PHE   A HB2  1 
ATOM   2398 H  HB3  . PHE   A 1 116 ? 24.607 -12.125 5.850   1.00 13.47 ?  116 PHE   A HB3  1 
ATOM   2399 H  HD1  . PHE   A 1 116 ? 25.682 -9.646  3.561   1.00 13.28 ?  116 PHE   A HD1  1 
ATOM   2400 H  HD2  . PHE   A 1 116 ? 22.464 -11.205 5.338   1.00 13.73 ?  116 PHE   A HD2  1 
ATOM   2401 H  HE1  . PHE   A 1 116 ? 24.418 -7.833  2.892   1.00 13.46 ?  116 PHE   A HE1  1 
ATOM   2402 H  HE2  . PHE   A 1 116 ? 21.196 -9.408  4.679   1.00 14.26 ?  116 PHE   A HE2  1 
ATOM   2403 H  HZ   . PHE   A 1 116 ? 22.163 -7.704  3.450   1.00 13.87 ?  116 PHE   A HZ   1 
ATOM   2404 N  N    . ASN   A 1 117 ? 27.413 -14.017 5.201   1.00 11.23 ?  117 ASN   A N    1 
ATOM   2405 C  CA   . ASN   A 1 117 ? 27.782 -15.261 5.872   1.00 11.25 ?  117 ASN   A CA   1 
ATOM   2406 C  C    . ASN   A 1 117 ? 29.039 -15.140 6.711   1.00 11.85 ?  117 ASN   A C    1 
ATOM   2407 O  O    . ASN   A 1 117 ? 29.340 -16.062 7.476   1.00 12.76 ?  117 ASN   A O    1 
ATOM   2408 C  CB   . ASN   A 1 117 ? 27.900 -16.396 4.857   1.00 11.51 ?  117 ASN   A CB   1 
ATOM   2409 C  CG   . ASN   A 1 117 ? 26.546 -16.778 4.308   1.00 11.51 ?  117 ASN   A CG   1 
ATOM   2410 O  OD1  . ASN   A 1 117 ? 25.571 -16.810 5.052   1.00 12.47 ?  117 ASN   A OD1  1 
ATOM   2411 N  ND2  . ASN   A 1 117 ? 26.466 -17.032 3.018   1.00 11.54 ?  117 ASN   A ND2  1 
ATOM   2412 H  H    . ASN   A 1 117 ? 27.489 -14.035 4.340   1.00 13.64 ?  117 ASN   A H    1 
ATOM   2413 H  HA   . ASN   A 1 117 ? 27.057 -15.493 6.474   1.00 13.66 ?  117 ASN   A HA   1 
ATOM   2414 H  HB2  . ASN   A 1 117 ? 28.465 -16.110 4.121   1.00 13.98 ?  117 ASN   A HB2  1 
ATOM   2415 H  HB3  . ASN   A 1 117 ? 28.283 -17.171 5.295   1.00 13.98 ?  117 ASN   A HB3  1 
ATOM   2416 H  HD21 . ASN   A 1 117 ? 25.712 -17.245 2.671   1.00 14.02 ?  117 ASN   A HD21 1 
ATOM   2417 H  HD22 . ASN   A 1 117 ? 27.172 -16.986 2.527   1.00 14.02 ?  117 ASN   A HD22 1 
ATOM   2418 N  N    . GLN   A 1 118 ? 29.771 -14.033 6.592   1.00 11.86 ?  118 GLN   A N    1 
ATOM   2419 C  CA   . GLN   A 1 118 ? 30.948 -13.801 7.413   1.00 12.48 ?  118 GLN   A CA   1 
ATOM   2420 C  C    . GLN   A 1 118 ? 30.608 -13.229 8.783   1.00 12.43 ?  118 GLN   A C    1 
ATOM   2421 O  O    . GLN   A 1 118 ? 31.523 -12.941 9.562   1.00 13.94 ?  118 GLN   A O    1 
ATOM   2422 C  CB   . GLN   A 1 118 ? 31.938 -12.894 6.674   1.00 12.79 ?  118 GLN   A CB   1 
ATOM   2423 C  CG   . GLN   A 1 118 ? 32.410 -13.472 5.347   1.00 12.83 ?  118 GLN   A CG   1 
ATOM   2424 C  CD   . GLN   A 1 118 ? 33.246 -14.732 5.519   1.00 13.11 ?  118 GLN   A CD   1 
ATOM   2425 O  OE1  . GLN   A 1 118 ? 34.114 -14.798 6.398   1.00 14.23 ?  118 GLN   A OE1  1 
ATOM   2426 N  NE2  . GLN   A 1 118 ? 32.999 -15.729 4.672   1.00 13.21 ?  118 GLN   A NE2  1 
ATOM   2427 H  H    . GLN   A 1 118 ? 29.596 -13.389 6.038   1.00 14.40 ?  118 GLN   A H    1 
ATOM   2428 H  HA   . GLN   A 1 118 ? 31.379 -14.656 7.556   1.00 15.13 ?  118 GLN   A HA   1 
ATOM   2429 H  HB2  . GLN   A 1 118 ? 31.509 -12.045 6.496   1.00 15.51 ?  118 GLN   A HB2  1 
ATOM   2430 H  HB3  . GLN   A 1 118 ? 32.714 -12.765 7.238   1.00 15.51 ?  118 GLN   A HB3  1 
ATOM   2431 H  HG2  . GLN   A 1 118 ? 31.639 -13.692 4.800   1.00 15.56 ?  118 GLN   A HG2  1 
ATOM   2432 H  HG3  . GLN   A 1 118 ? 32.959 -12.813 4.894   1.00 15.56 ?  118 GLN   A HG3  1 
ATOM   2433 H  HE21 . GLN   A 1 118 ? 32.386 -15.641 4.066   1.00 16.02 ?  118 GLN   A HE21 1 
ATOM   2434 H  HE22 . GLN   A 1 118 ? 33.441 -16.462 4.723   1.00 16.02 ?  118 GLN   A HE22 1 
ATOM   2435 N  N    . HIS   A 1 119 ? 29.320 -13.072 9.095   1.00 12.10 ?  119 HIS   A N    1 
ATOM   2436 C  CA   . HIS   A 1 119 ? 28.866 -12.464 10.340  1.00 12.87 ?  119 HIS   A CA   1 
ATOM   2437 C  C    . HIS   A 1 119 ? 27.725 -13.290 10.911  1.00 12.68 ?  119 HIS   A C    1 
ATOM   2438 O  O    . HIS   A 1 119 ? 26.775 -13.620 10.196  1.00 13.43 ?  119 HIS   A O    1 
ATOM   2439 C  CB   . HIS   A 1 119 ? 28.406 -11.032 10.061  1.00 13.40 ?  119 HIS   A CB   1 
ATOM   2440 C  CG   . HIS   A 1 119 ? 29.491 -10.217 9.456   1.00 14.59 ?  119 HIS   A CG   1 
ATOM   2441 N  ND1  . HIS   A 1 119 ? 30.462 -9.611  10.220  1.00 16.79 ?  119 HIS   A ND1  1 
ATOM   2442 C  CD2  . HIS   A 1 119 ? 29.844 -10.023 8.165   1.00 15.52 ?  119 HIS   A CD2  1 
ATOM   2443 C  CE1  . HIS   A 1 119 ? 31.336 -9.023  9.422   1.00 17.07 ?  119 HIS   A CE1  1 
ATOM   2444 N  NE2  . HIS   A 1 119 ? 30.994 -9.271  8.170   1.00 16.76 ?  119 HIS   A NE2  1 
ATOM   2445 H  H    . HIS   A 1 119 ? 28.668 -13.322 8.587   1.00 14.69 ?  119 HIS   A H    1 
ATOM   2446 H  HA   . HIS   A 1 119 ? 29.601 -12.445 10.979  1.00 15.60 ?  119 HIS   A HA   1 
ATOM   2447 H  HB2  . HIS   A 1 119 ? 27.662 -11.056 9.442   1.00 16.24 ?  119 HIS   A HB2  1 
ATOM   2448 H  HB3  . HIS   A 1 119 ? 28.146 -10.617 10.894  1.00 16.24 ?  119 HIS   A HB3  1 
ATOM   2449 H  HD2  . HIS   A 1 119 ? 29.400 -10.341 7.410   1.00 18.79 ?  119 HIS   A HD2  1 
ATOM   2450 H  HE1  . HIS   A 1 119 ? 32.073 -8.523  9.694   1.00 20.65 ?  119 HIS   A HE1  1 
ATOM   2451 H  HE2  . HIS   A 1 119 ? 31.412 -8.982  7.471   1.00 20.28 ?  119 HIS   A HE2  1 
ATOM   2452 N  N    . GLU   A 1 120 ? 27.810 -13.602 12.204  1.00 13.76 ?  120 GLU   A N    1 
ATOM   2453 C  CA   . GLU   A 1 120 ? 26.857 -14.539 12.795  1.00 15.78 ?  120 GLU   A CA   1 
ATOM   2454 C  C    . GLU   A 1 120 ? 25.439 -13.979 12.860  1.00 14.63 ?  120 GLU   A C    1 
ATOM   2455 O  O    . GLU   A 1 120 ? 24.468 -14.744 12.756  1.00 14.75 ?  120 GLU   A O    1 
ATOM   2456 C  CB   . GLU   A 1 120 ? 27.323 -14.945 14.195  1.00 20.65 ?  120 GLU   A CB   1 
ATOM   2457 C  CG   . GLU   A 1 120 ? 28.519 -15.882 14.202  1.00 27.71 ?  120 GLU   A CG   1 
ATOM   2458 C  CD   . GLU   A 1 120 ? 28.672 -16.621 15.514  1.00 35.24 ?  120 GLU   A CD   1 
ATOM   2459 O  OE1  . GLU   A 1 120 ? 28.273 -16.068 16.561  1.00 36.75 ?  120 GLU   A OE1  1 
ATOM   2460 O  OE2  . GLU   A 1 120 ? 29.188 -17.758 15.496  1.00 38.66 -1 120 GLU   A OE2  1 
ATOM   2461 H  H    . GLU   A 1 120 ? 28.410 -13.299 12.753  1.00 16.68 ?  120 GLU   A H    1 
ATOM   2462 H  HA   . GLU   A 1 120 ? 26.840 -15.343 12.257  1.00 19.10 ?  120 GLU   A HA   1 
ATOM   2463 H  HB2  . GLU   A 1 120 ? 27.575 -14.152 14.693  1.00 24.94 ?  120 GLU   A HB2  1 
ATOM   2464 H  HB3  . GLU   A 1 120 ? 26.595 -15.399 14.652  1.00 24.94 ?  120 GLU   A HB3  1 
ATOM   2465 H  HG2  . GLU   A 1 120 ? 28.420 -16.535 13.492  1.00 33.42 ?  120 GLU   A HG2  1 
ATOM   2466 H  HG3  . GLU   A 1 120 ? 29.331 -15.371 14.080  1.00 33.42 ?  120 GLU   A HG3  1 
ATOM   2467 N  N    . VAL   A 1 121 ? 25.305 -12.670 13.072  1.00 13.71 ?  121 VAL   A N    1 
ATOM   2468 C  CA   . VAL   A 1 121 ? 24.014 -11.999 13.200  1.00 13.66 ?  121 VAL   A CA   1 
ATOM   2469 C  C    . VAL   A 1 121 ? 24.130 -10.617 12.566  1.00 12.63 ?  121 VAL   A C    1 
ATOM   2470 O  O    . VAL   A 1 121 ? 25.104 -9.897  12.810  1.00 13.48 ?  121 VAL   A O    1 
ATOM   2471 C  CB   . VAL   A 1 121 ? 23.585 -11.857 14.677  1.00 16.64 ?  121 VAL   A CB   1 
ATOM   2472 C  CG1  . VAL   A 1 121 ? 22.203 -11.220 14.774  1.00 17.46 ?  121 VAL   A CG1  1 
ATOM   2473 C  CG2  . VAL   A 1 121 ? 23.602 -13.192 15.399  1.00 18.83 ?  121 VAL   A CG2  1 
ATOM   2474 H  H    . VAL   A 1 121 ? 25.971 -12.131 13.157  1.00 16.62 ?  121 VAL   A H    1 
ATOM   2475 H  HA   . VAL   A 1 121 ? 23.335 -12.509 12.731  1.00 16.56 ?  121 VAL   A HA   1 
ATOM   2476 H  HB   . VAL   A 1 121 ? 24.208 -11.271 15.129  1.00 20.13 ?  121 VAL   A HB   1 
ATOM   2477 H  HG11 . VAL   A 1 121 ? 21.886 -11.288 15.689  1.00 21.12 ?  121 VAL   A HG11 1 
ATOM   2478 H  HG12 . VAL   A 1 121 ? 22.263 -10.287 14.516  1.00 21.12 ?  121 VAL   A HG12 1 
ATOM   2479 H  HG13 . VAL   A 1 121 ? 21.595 -11.690 14.180  1.00 21.12 ?  121 VAL   A HG13 1 
ATOM   2480 H  HG21 . VAL   A 1 121 ? 23.253 -13.071 16.301  1.00 22.76 ?  121 VAL   A HG21 1 
ATOM   2481 H  HG22 . VAL   A 1 121 ? 23.041 -13.823 14.918  1.00 22.76 ?  121 VAL   A HG22 1 
ATOM   2482 H  HG23 . VAL   A 1 121 ? 24.510 -13.521 15.442  1.00 22.76 ?  121 VAL   A HG23 1 
ATOM   2483 N  N    . LEU   A 1 122 ? 23.121 -10.229 11.776  1.00 12.26 ?  122 LEU   A N    1 
ATOM   2484 C  CA   . LEU   A 1 122 ? 23.124 -8.929  11.108  1.00 12.03 ?  122 LEU   A CA   1 
ATOM   2485 C  C    . LEU   A 1 122 ? 21.723 -8.342  11.075  1.00 11.95 ?  122 LEU   A C    1 
ATOM   2486 O  O    . LEU   A 1 122 ? 20.734 -9.064  10.932  1.00 12.83 ?  122 LEU   A O    1 
ATOM   2487 C  CB   . LEU   A 1 122 ? 23.545 -9.017  9.634   1.00 13.53 ?  122 LEU   A CB   1 
ATOM   2488 C  CG   . LEU   A 1 122 ? 24.749 -9.867  9.271   1.00 13.37 ?  122 LEU   A CG   1 
ATOM   2489 C  CD1  . LEU   A 1 122 ? 24.343 -11.320 9.049   1.00 14.19 ?  122 LEU   A CD1  1 
ATOM   2490 C  CD2  . LEU   A 1 122 ? 25.412 -9.296  8.037   1.00 12.72 ?  122 LEU   A CD2  1 
ATOM   2491 H  H    . LEU   A 1 122 ? 22.416 -10.702 11.614  1.00 14.87 ?  122 LEU   A H    1 
ATOM   2492 H  HA   . LEU   A 1 122 ? 23.720 -8.316  11.572  1.00 14.60 ?  122 LEU   A HA   1 
ATOM   2493 H  HB2  . LEU   A 1 122 ? 22.798 -9.373  9.133   1.00 16.41 ?  122 LEU   A HB2  1 
ATOM   2494 H  HB3  . LEU   A 1 122 ? 23.740 -8.122  9.324   1.00 16.41 ?  122 LEU   A HB3  1 
ATOM   2495 H  HG   . LEU   A 1 122 ? 25.399 -9.847  9.993   1.00 16.20 ?  122 LEU   A HG   1 
ATOM   2496 H  HD11 . LEU   A 1 122 ? 25.118 -11.835 8.768   1.00 17.19 ?  122 LEU   A HD11 1 
ATOM   2497 H  HD12 . LEU   A 1 122 ? 23.995 -11.686 9.880   1.00 17.19 ?  122 LEU   A HD12 1 
ATOM   2498 H  HD13 . LEU   A 1 122 ? 23.658 -11.360 8.362   1.00 17.19 ?  122 LEU   A HD13 1 
ATOM   2499 H  HD21 . LEU   A 1 122 ? 26.148 -9.873  7.770   1.00 15.43 ?  122 LEU   A HD21 1 
ATOM   2500 H  HD22 . LEU   A 1 122 ? 24.759 -9.245  7.322   1.00 15.43 ?  122 LEU   A HD22 1 
ATOM   2501 H  HD23 . LEU   A 1 122 ? 25.749 -8.409  8.242   1.00 15.43 ?  122 LEU   A HD23 1 
ATOM   2502 N  N    . LEU   A 1 123 ? 21.659 -7.016  11.181  1.00 11.52 ?  123 LEU   A N    1 
ATOM   2503 C  CA   . LEU   A 1 123 ? 20.491 -6.215  10.815  1.00 11.28 ?  123 LEU   A CA   1 
ATOM   2504 C  C    . LEU   A 1 123 ? 20.733 -5.685  9.408   1.00 10.77 ?  123 LEU   A C    1 
ATOM   2505 O  O    . LEU   A 1 123 ? 21.785 -5.093  9.157   1.00 11.57 ?  123 LEU   A O    1 
ATOM   2506 C  CB   . LEU   A 1 123 ? 20.368 -5.034  11.779  1.00 11.99 ?  123 LEU   A CB   1 
ATOM   2507 C  CG   . LEU   A 1 123 ? 19.328 -3.964  11.436  1.00 12.79 ?  123 LEU   A CG   1 
ATOM   2508 C  CD1  . LEU   A 1 123 ? 17.928 -4.562  11.433  1.00 13.78 ?  123 LEU   A CD1  1 
ATOM   2509 C  CD2  . LEU   A 1 123 ? 19.415 -2.783  12.404  1.00 13.62 ?  123 LEU   A CD2  1 
ATOM   2510 H  H    . LEU   A 1 123 ? 22.313 -6.536  11.472  1.00 13.99 ?  123 LEU   A H    1 
ATOM   2511 H  HA   . LEU   A 1 123 ? 19.684 -6.754  10.836  1.00 13.70 ?  123 LEU   A HA   1 
ATOM   2512 H  HB2  . LEU   A 1 123 ? 20.134 -5.384  12.655  1.00 14.55 ?  123 LEU   A HB2  1 
ATOM   2513 H  HB3  . LEU   A 1 123 ? 21.224 -4.592  11.828  1.00 14.55 ?  123 LEU   A HB3  1 
ATOM   2514 H  HG   . LEU   A 1 123 ? 19.500 -3.621  10.545  1.00 15.51 ?  123 LEU   A HG   1 
ATOM   2515 H  HD11 . LEU   A 1 123 ? 17.281 -3.865  11.264  1.00 16.70 ?  123 LEU   A HD11 1 
ATOM   2516 H  HD12 . LEU   A 1 123 ? 17.876 -5.241  10.738  1.00 16.70 ?  123 LEU   A HD12 1 
ATOM   2517 H  HD13 . LEU   A 1 123 ? 17.759 -4.970  12.300  1.00 16.70 ?  123 LEU   A HD13 1 
ATOM   2518 H  HD21 . LEU   A 1 123 ? 18.746 -2.126  12.165  1.00 16.51 ?  123 LEU   A HD21 1 
ATOM   2519 H  HD22 . LEU   A 1 123 ? 19.251 -3.109  13.306  1.00 16.51 ?  123 LEU   A HD22 1 
ATOM   2520 H  HD23 . LEU   A 1 123 ? 20.301 -2.398  12.348  1.00 16.51 ?  123 LEU   A HD23 1 
ATOM   2521 N  N    A ALA   A 1 124 ? 19.763 -5.841  8.504   0.60 10.68 ?  124 ALA   A N    1 
ATOM   2522 N  N    B ALA   A 1 124 ? 19.797 -5.925  8.497   0.40 10.48 ?  124 ALA   A N    1 
ATOM   2523 C  CA   A ALA   A 1 124 ? 20.047 -5.552  7.104   0.60 10.71 ?  124 ALA   A CA   1 
ATOM   2524 C  CA   B ALA   A 1 124 ? 20.067 -5.662  7.097   0.40 10.33 ?  124 ALA   A CA   1 
ATOM   2525 C  C    A ALA   A 1 124 ? 18.795 -5.114  6.355   0.60 10.90 ?  124 ALA   A C    1 
ATOM   2526 C  C    B ALA   A 1 124 ? 18.839 -5.136  6.374   0.40 10.33 ?  124 ALA   A C    1 
ATOM   2527 O  O    A ALA   A 1 124 ? 17.670 -5.457  6.746   0.60 11.45 ?  124 ALA   A O    1 
ATOM   2528 O  O    B ALA   A 1 124 ? 17.700 -5.473  6.725   0.40 11.06 ?  124 ALA   A O    1 
ATOM   2529 C  CB   A ALA   A 1 124 ? 20.653 -6.768  6.398   0.60 11.13 ?  124 ALA   A CB   1 
ATOM   2530 C  CB   B ALA   A 1 124 ? 20.553 -6.926  6.372   0.40 10.39 ?  124 ALA   A CB   1 
ATOM   2531 H  H    A ALA   A 1 124 ? 18.960 -6.108  8.670   0.60 12.98 ?  124 ALA   A H    1 
ATOM   2532 H  H    B ALA   A 1 124 ? 19.013 -6.239  8.659   0.40 12.74 ?  124 ALA   A H    1 
ATOM   2533 H  HA   A ALA   A 1 124 ? 20.697 -4.834  7.070   0.60 13.02 ?  124 ALA   A HA   1 
ATOM   2534 H  HA   B ALA   A 1 124 ? 20.774 -4.998  7.041   0.40 12.56 ?  124 ALA   A HA   1 
ATOM   2535 H  HB1  A ALA   A 1 124 ? 20.836 -6.540  5.472   0.60 13.52 ?  124 ALA   A HB1  1 
ATOM   2536 H  HB1  B ALA   A 1 124 ? 20.730 -6.716  5.440   0.40 12.64 ?  124 ALA   A HB1  1 
ATOM   2537 H  HB2  A ALA   A 1 124 ? 21.485 -7.011  6.844   0.60 13.52 ?  124 ALA   A HB2  1 
ATOM   2538 H  HB2  B ALA   A 1 124 ? 21.372 -7.242  6.795   0.40 12.64 ?  124 ALA   A HB2  1 
ATOM   2539 H  HB3  A ALA   A 1 124 ? 20.029 -7.506  6.442   0.60 13.52 ?  124 ALA   A HB3  1 
ATOM   2540 H  HB3  B ALA   A 1 124 ? 19.870 -7.610  6.433   0.40 12.64 ?  124 ALA   A HB3  1 
ATOM   2541 N  N    A PRO   A 1 125 ? 18.968 -4.380  5.254   0.60 11.08 ?  125 PRO   A N    1 
ATOM   2542 N  N    B PRO   A 1 125 ? 19.052 -4.328  5.343   0.40 9.69  ?  125 PRO   A N    1 
ATOM   2543 C  CA   A PRO   A 1 125 ? 17.904 -4.179  4.270   0.60 11.07 ?  125 PRO   A CA   1 
ATOM   2544 C  CA   B PRO   A 1 125 ? 17.967 -3.960  4.438   0.40 10.26 ?  125 PRO   A CA   1 
ATOM   2545 C  C    A PRO   A 1 125 ? 17.981 -5.240  3.177   0.60 10.36 ?  125 PRO   A C    1 
ATOM   2546 C  C    B PRO   A 1 125 ? 17.885 -5.005  3.344   0.40 11.06 ?  125 PRO   A C    1 
ATOM   2547 O  O    A PRO   A 1 125 ? 18.967 -5.968  3.045   0.60 10.28 ?  125 PRO   A O    1 
ATOM   2548 O  O    B PRO   A 1 125 ? 18.723 -5.913  3.280   0.40 11.71 ?  125 PRO   A O    1 
ATOM   2549 C  CB   A PRO   A 1 125 ? 18.290 -2.822  3.666   0.60 11.79 ?  125 PRO   A CB   1 
ATOM   2550 C  CB   B PRO   A 1 125 ? 18.472 -2.635  3.865   0.40 9.74  ?  125 PRO   A CB   1 
ATOM   2551 C  CG   A PRO   A 1 125 ? 19.797 -2.888  3.630   0.60 12.16 ?  125 PRO   A CG   1 
ATOM   2552 C  CG   B PRO   A 1 125 ? 19.971 -2.909  3.692   0.40 9.63  ?  125 PRO   A CG   1 
ATOM   2553 C  CD   A PRO   A 1 125 ? 20.180 -3.610  4.910   0.60 11.88 ?  125 PRO   A CD   1 
ATOM   2554 C  CD   B PRO   A 1 125 ? 20.352 -3.844  4.840   0.40 9.57  ?  125 PRO   A CD   1 
ATOM   2555 H  HA   A PRO   A 1 125 ? 17.025 -4.153  4.675   0.60 13.45 ?  125 PRO   A HA   1 
ATOM   2556 H  HA   B PRO   A 1 125 ? 17.105 -3.850  4.894   0.40 12.47 ?  125 PRO   A HA   1 
ATOM   2557 H  HB2  A PRO   A 1 125 ? 17.918 -2.736  2.769   0.60 14.31 ?  125 PRO   A HB2  1 
ATOM   2558 H  HB2  B PRO   A 1 125 ? 18.045 -2.452  3.013   0.40 11.85 ?  125 PRO   A HB2  1 
ATOM   2559 H  HB3  A PRO   A 1 125 ? 17.980 -2.104  4.239   0.60 14.31 ?  125 PRO   A HB3  1 
ATOM   2560 H  HB3  B PRO   A 1 125 ? 18.317 -1.911  4.496   0.40 11.85 ?  125 PRO   A HB3  1 
ATOM   2561 H  HG2  A PRO   A 1 125 ? 20.087 -3.392  2.851   0.60 14.76 ?  125 PRO   A HG2  1 
ATOM   2562 H  HG2  B PRO   A 1 125 ? 20.128 -3.341  2.836   0.40 11.72 ?  125 PRO   A HG2  1 
ATOM   2563 H  HG3  A PRO   A 1 125 ? 20.165 -1.990  3.613   0.60 14.76 ?  125 PRO   A HG3  1 
ATOM   2564 H  HG3  B PRO   A 1 125 ? 20.466 -2.077  3.749   0.40 11.72 ?  125 PRO   A HG3  1 
ATOM   2565 H  HD2  A PRO   A 1 125 ? 20.934 -4.198  4.756   0.60 14.42 ?  125 PRO   A HD2  1 
ATOM   2566 H  HD2  B PRO   A 1 125 ? 20.882 -4.586  4.511   0.40 11.65 ?  125 PRO   A HD2  1 
ATOM   2567 H  HD3  A PRO   A 1 125 ? 20.371 -2.966  5.615   0.60 14.42 ?  125 PRO   A HD3  1 
ATOM   2568 H  HD3  B PRO   A 1 125 ? 20.824 -3.349  5.530   0.40 11.65 ?  125 PRO   A HD3  1 
ATOM   2569 N  N    A LEU   A 1 126 ? 16.928 -5.293  2.367   0.60 10.35 ?  126 LEU   A N    1 
ATOM   2570 N  N    B LEU   A 1 126 ? 16.903 -4.875  2.464   0.40 11.86 ?  126 LEU   A N    1 
ATOM   2571 C  CA   A LEU   A 1 126 ? 16.965 -6.102  1.156   0.60 10.82 ?  126 LEU   A CA   1 
ATOM   2572 C  CA   B LEU   A 1 126 ? 16.796 -5.750  1.301   0.40 12.48 ?  126 LEU   A CA   1 
ATOM   2573 C  C    A LEU   A 1 126 ? 17.915 -5.471  0.145   0.60 11.02 ?  126 LEU   A C    1 
ATOM   2574 C  C    B LEU   A 1 126 ? 17.736 -5.232  0.215   0.40 11.91 ?  126 LEU   A C    1 
ATOM   2575 O  O    A LEU   A 1 126 ? 17.745 -4.310  -0.245  0.60 11.76 ?  126 LEU   A O    1 
ATOM   2576 O  O    B LEU   A 1 126 ? 17.479 -4.187  -0.391  0.40 12.39 ?  126 LEU   A O    1 
ATOM   2577 C  CB   A LEU   A 1 126 ? 15.567 -6.229  0.567   0.60 11.07 ?  126 LEU   A CB   1 
ATOM   2578 C  CB   B LEU   A 1 126 ? 15.347 -5.762  0.823   0.40 15.22 ?  126 LEU   A CB   1 
ATOM   2579 C  CG   A LEU   A 1 126 ? 14.613 -7.097  1.386   0.60 12.04 ?  126 LEU   A CG   1 
ATOM   2580 C  CG   B LEU   A 1 126 ? 14.829 -6.927  -0.022  0.40 17.59 ?  126 LEU   A CG   1 
ATOM   2581 C  CD1  A LEU   A 1 126 ? 13.191 -6.943  0.873   0.60 12.67 ?  126 LEU   A CD1  1 
ATOM   2582 C  CD1  B LEU   A 1 126 ? 14.992 -8.251  0.699   0.40 18.01 ?  126 LEU   A CD1  1 
ATOM   2583 C  CD2  A LEU   A 1 126 ? 15.051 -8.561  1.344   0.60 12.68 ?  126 LEU   A CD2  1 
ATOM   2584 C  CD2  B LEU   A 1 126 ? 13.367 -6.691  -0.371  0.40 18.12 ?  126 LEU   A CD2  1 
ATOM   2585 H  H    A LEU   A 1 126 ? 16.187 -4.875  2.487   0.60 12.59 ?  126 LEU   A H    1 
ATOM   2586 H  H    B LEU   A 1 126 ? 16.282 -4.281  2.537   0.40 14.40 ?  126 LEU   A H    1 
ATOM   2587 H  HA   A LEU   A 1 126 ? 17.293 -6.994  1.368   0.60 13.15 ?  126 LEU   A HA   1 
ATOM   2588 H  HA   B LEU   A 1 126 ? 17.061 -6.646  1.552   0.40 15.14 ?  126 LEU   A HA   1 
ATOM   2589 H  HB2  A LEU   A 1 126 ? 15.176 -5.346  0.502   0.60 13.45 ?  126 LEU   A HB2  1 
ATOM   2590 H  HB2  B LEU   A 1 126 ? 14.782 -5.721  1.610   0.40 18.42 ?  126 LEU   A HB2  1 
ATOM   2591 H  HB3  A LEU   A 1 126 ? 15.633 -6.624  -0.318  0.60 13.45 ?  126 LEU   A HB3  1 
ATOM   2592 H  HB3  B LEU   A 1 126 ? 15.211 -4.958  0.301   0.40 18.42 ?  126 LEU   A HB3  1 
ATOM   2593 H  HG   A LEU   A 1 126 ? 14.628 -6.804  2.309   0.60 14.62 ?  126 LEU   A HG   1 
ATOM   2594 H  HG   B LEU   A 1 126 ? 15.335 -6.962  -0.847  0.40 21.27 ?  126 LEU   A HG   1 
ATOM   2595 H  HD11 A LEU   A 1 126 ? 12.602 -7.503  1.402   0.60 15.37 ?  126 LEU   A HD11 1 
ATOM   2596 H  HD11 B LEU   A 1 126 ? 14.538 -8.941  0.193   0.40 21.78 ?  126 LEU   A HD11 1 
ATOM   2597 H  HD12 A LEU   A 1 126 ? 12.926 -6.014  0.952   0.60 15.37 ?  126 LEU   A HD12 1 
ATOM   2598 H  HD12 B LEU   A 1 126 ? 15.936 -8.457  0.770   0.40 21.78 ?  126 LEU   A HD12 1 
ATOM   2599 H  HD13 A LEU   A 1 126 ? 13.161 -7.218  -0.058  0.60 15.37 ?  126 LEU   A HD13 1 
ATOM   2600 H  HD13 B LEU   A 1 126 ? 14.599 -8.177  1.583   0.40 21.78 ?  126 LEU   A HD13 1 
ATOM   2601 H  HD21 A LEU   A 1 126 ? 14.352 -9.113  1.735   0.60 15.39 ?  126 LEU   A HD21 1 
ATOM   2602 H  HD21 B LEU   A 1 126 ? 13.048 -7.433  -0.909  0.40 21.91 ?  126 LEU   A HD21 1 
ATOM   2603 H  HD22 A LEU   A 1 126 ? 15.198 -8.822  0.422   0.60 15.39 ?  126 LEU   A HD22 1 
ATOM   2604 H  HD22 B LEU   A 1 126 ? 12.852 -6.633  0.450   0.40 21.91 ?  126 LEU   A HD22 1 
ATOM   2605 H  HD23 A LEU   A 1 126 ? 15.871 -8.661  1.852   0.60 15.39 ?  126 LEU   A HD23 1 
ATOM   2606 H  HD23 B LEU   A 1 126 ? 13.289 -5.863  -0.870  0.40 21.91 ?  126 LEU   A HD23 1 
ATOM   2607 N  N    A LEU   A 1 127 ? 18.913 -6.238  -0.283  0.60 10.56 ?  127 LEU   A N    1 
ATOM   2608 N  N    B LEU   A 1 127 ? 18.827 -5.955  -0.041  0.40 11.43 ?  127 LEU   A N    1 
ATOM   2609 C  CA   A LEU   A 1 127 ? 19.904 -5.728  -1.217  0.60 10.70 ?  127 LEU   A CA   1 
ATOM   2610 C  CA   B LEU   A 1 127 ? 19.825 -5.477  -0.990  0.40 11.57 ?  127 LEU   A CA   1 
ATOM   2611 C  C    A LEU   A 1 127 ? 19.289 -5.506  -2.590  0.60 10.43 ?  127 LEU   A C    1 
ATOM   2612 C  C    B LEU   A 1 127 ? 19.237 -5.357  -2.391  0.40 11.48 ?  127 LEU   A C    1 
ATOM   2613 O  O    A LEU   A 1 127 ? 18.449 -6.282  -3.060  0.60 10.29 ?  127 LEU   A O    1 
ATOM   2614 O  O    B LEU   A 1 127 ? 18.382 -6.145  -2.806  0.40 11.99 ?  127 LEU   A O    1 
ATOM   2615 C  CB   A LEU   A 1 127 ? 21.075 -6.701  -1.326  0.60 10.93 ?  127 LEU   A CB   1 
ATOM   2616 C  CB   B LEU   A 1 127 ? 21.030 -6.418  -1.030  0.40 11.59 ?  127 LEU   A CB   1 
ATOM   2617 C  CG   A LEU   A 1 127 ? 21.868 -6.970  -0.048  0.60 11.21 ?  127 LEU   A CG   1 
ATOM   2618 C  CG   B LEU   A 1 127 ? 21.850 -6.519  0.255   0.40 11.81 ?  127 LEU   A CG   1 
ATOM   2619 C  CD1  A LEU   A 1 127 ? 22.973 -7.956  -0.340  0.60 11.50 ?  127 LEU   A CD1  1 
ATOM   2620 C  CD1  B LEU   A 1 127 ? 23.005 -7.491  0.073   0.40 12.07 ?  127 LEU   A CD1  1 
ATOM   2621 C  CD2  A LEU   A 1 127 ? 22.450 -5.691  0.525   0.60 11.98 ?  127 LEU   A CD2  1 
ATOM   2622 C  CD2  B LEU   A 1 127 ? 22.355 -5.148  0.680   0.40 12.24 ?  127 LEU   A CD2  1 
ATOM   2623 H  H    A LEU   A 1 127 ? 19.038 -7.058  -0.039  0.60 12.83 ?  127 LEU   A H    1 
ATOM   2624 H  H    B LEU   A 1 127 ? 19.010 -6.715  0.321   0.40 13.88 ?  127 LEU   A H    1 
ATOM   2625 H  HA   A LEU   A 1 127 ? 20.243 -4.882  -0.888  0.60 13.01 ?  127 LEU   A HA   1 
ATOM   2626 H  HA   B LEU   A 1 127 ? 20.129 -4.601  -0.715  0.40 14.05 ?  127 LEU   A HA   1 
ATOM   2627 H  HB2  A LEU   A 1 127 ? 20.733 -7.556  -1.632  0.60 13.28 ?  127 LEU   A HB2  1 
ATOM   2628 H  HB2  B LEU   A 1 127 ? 20.712 -7.309  -1.244  0.40 14.07 ?  127 LEU   A HB2  1 
ATOM   2629 H  HB3  A LEU   A 1 127 ? 21.700 -6.352  -1.977  0.60 13.28 ?  127 LEU   A HB3  1 
ATOM   2630 H  HB3  B LEU   A 1 127 ? 21.626 -6.113  -1.733  0.40 14.07 ?  127 LEU   A HB3  1 
ATOM   2631 H  HG   A LEU   A 1 127 ? 21.282 -7.368  0.621   0.60 13.62 ?  127 LEU   A HG   1 
ATOM   2632 H  HG   B LEU   A 1 127 ? 21.282 -6.860  0.964   0.40 14.34 ?  127 LEU   A HG   1 
ATOM   2633 H  HD11 A LEU   A 1 127 ? 23.449 -8.155  0.482   0.60 13.96 ?  127 LEU   A HD11 1 
ATOM   2634 H  HD11 B LEU   A 1 127 ? 23.576 -7.453  0.856   0.40 14.65 ?  127 LEU   A HD11 1 
ATOM   2635 H  HD12 A LEU   A 1 127 ? 22.583 -8.772  -0.699  0.60 13.96 ?  127 LEU   A HD12 1 
ATOM   2636 H  HD12 B LEU   A 1 127 ? 22.650 -8.387  -0.035  0.40 14.65 ?  127 LEU   A HD12 1 
ATOM   2637 H  HD13 A LEU   A 1 127 ? 23.577 -7.567  -0.989  0.60 13.96 ?  127 LEU   A HD13 1 
ATOM   2638 H  HD13 B LEU   A 1 127 ? 23.509 -7.237  -0.716  0.40 14.65 ?  127 LEU   A HD13 1 
ATOM   2639 H  HD21 A LEU   A 1 127 ? 23.040 -5.913  1.264   0.60 14.54 ?  127 LEU   A HD21 1 
ATOM   2640 H  HD21 B LEU   A 1 127 ? 23.005 -5.258  1.391   0.40 14.85 ?  127 LEU   A HD21 1 
ATOM   2641 H  HD22 A LEU   A 1 127 ? 22.952 -5.237  -0.171  0.60 14.54 ?  127 LEU   A HD22 1 
ATOM   2642 H  HD22 B LEU   A 1 127 ? 22.769 -4.715  -0.083  0.40 14.85 ?  127 LEU   A HD22 1 
ATOM   2643 H  HD23 A LEU   A 1 127 ? 21.728 -5.126  0.836   0.60 14.54 ?  127 LEU   A HD23 1 
ATOM   2644 H  HD23 B LEU   A 1 127 ? 21.606 -4.618  0.995   0.40 14.85 ?  127 LEU   A HD23 1 
ATOM   2645 N  N    A SER   A 1 128 ? 19.732 -4.436  -3.234  0.60 10.82 ?  128 SER   A N    1 
ATOM   2646 N  N    B SER   A 1 128 ? 19.720 -4.349  -3.119  0.40 11.11 ?  128 SER   A N    1 
ATOM   2647 C  CA   A SER   A 1 128 ? 19.305 -4.016  -4.560  0.60 11.56 ?  128 SER   A CA   1 
ATOM   2648 C  CA   B SER   A 1 128 ? 19.364 -4.007  -4.495  0.40 11.04 ?  128 SER   A CA   1 
ATOM   2649 C  C    A SER   A 1 128 ? 17.847 -3.569  -4.613  0.60 12.48 ?  128 SER   A C    1 
ATOM   2650 C  C    B SER   A 1 128 ? 17.918 -3.556  -4.671  0.40 11.17 ?  128 SER   A C    1 
ATOM   2651 O  O    A SER   A 1 128 ? 17.333 -3.312  -5.706  0.60 14.04 ?  128 SER   A O    1 
ATOM   2652 O  O    B SER   A 1 128 ? 17.539 -3.205  -5.791  0.40 11.24 ?  128 SER   A O    1 
ATOM   2653 C  CB   A SER   A 1 128 ? 19.627 -5.050  -5.647  0.60 11.57 ?  128 SER   A CB   1 
ATOM   2654 C  CB   B SER   A 1 128 ? 19.720 -5.097  -5.519  0.40 11.08 ?  128 SER   A CB   1 
ATOM   2655 O  OG   A SER   A 1 128 ? 21.026 -5.310  -5.692  0.60 12.13 ?  128 SER   A OG   1 
ATOM   2656 O  OG   B SER   A 1 128 ? 21.130 -5.236  -5.627  0.40 11.31 ?  128 SER   A OG   1 
ATOM   2657 H  H    A SER   A 1 128 ? 20.337 -3.920  -2.898  0.60 13.14 ?  128 SER   A H    1 
ATOM   2658 H  H    B SER   A 1 128 ? 20.316 -3.806  -2.811  0.40 13.50 ?  128 SER   A H    1 
ATOM   2659 H  HA   A SER   A 1 128 ? 19.838 -3.244  -4.768  0.60 14.03 ?  128 SER   A HA   1 
ATOM   2660 H  HA   B SER   A 1 128 ? 19.894 -3.237  -4.734  0.40 13.41 ?  128 SER   A HA   1 
ATOM   2661 H  HB2  A SER   A 1 128 ? 19.157 -5.873  -5.459  0.60 14.04 ?  128 SER   A HB2  1 
ATOM   2662 H  HB2  B SER   A 1 128 ? 19.335 -5.936  -5.237  0.40 13.47 ?  128 SER   A HB2  1 
ATOM   2663 H  HB3  A SER   A 1 128 ? 19.351 -4.691  -6.505  0.60 14.04 ?  128 SER   A HB3  1 
ATOM   2664 H  HB3  B SER   A 1 128 ? 19.363 -4.838  -6.387  0.40 13.47 ?  128 SER   A HB3  1 
ATOM   2665 H  HG   A SER   A 1 128 ? 21.454 -4.602  -5.846  0.60 14.72 ?  128 SER   A HG   1 
ATOM   2666 H  HG   B SER   A 1 128 ? 21.474 -4.506  -5.863  0.40 13.74 ?  128 SER   A HG   1 
ATOM   2667 N  N    A ALA   A 1 129 ? 17.177 -3.446  -3.465  0.60 12.62 ?  129 ALA   A N    1 
ATOM   2668 N  N    B ALA   A 1 129 ? 17.115 -3.518  -3.610  0.40 11.77 ?  129 ALA   A N    1 
ATOM   2669 C  CA   A ALA   A 1 129 ? 15.813 -2.934  -3.415  0.60 12.54 ?  129 ALA   A CA   1 
ATOM   2670 C  CA   B ALA   A 1 129 ? 15.742 -3.050  -3.707  0.40 12.52 ?  129 ALA   A CA   1 
ATOM   2671 C  C    A ALA   A 1 129 ? 15.837 -1.404  -3.450  0.60 11.64 ?  129 ALA   A C    1 
ATOM   2672 C  C    B ALA   A 1 129 ? 15.694 -1.522  -3.655  0.40 13.03 ?  129 ALA   A C    1 
ATOM   2673 O  O    A ALA   A 1 129 ? 16.885 -0.774  -3.629  0.60 11.52 ?  129 ALA   A O    1 
ATOM   2674 O  O    B ALA   A 1 129 ? 16.710 -0.838  -3.494  0.40 13.50 ?  129 ALA   A O    1 
ATOM   2675 C  CB   A ALA   A 1 129 ? 15.075 -3.490  -2.198  0.60 13.53 ?  129 ALA   A CB   1 
ATOM   2676 C  CB   B ALA   A 1 129 ? 14.883 -3.693  -2.617  0.40 12.89 ?  129 ALA   A CB   1 
ATOM   2677 H  H    A ALA   A 1 129 ? 17.499 -3.657  -2.688  0.60 15.30 ?  129 ALA   A H    1 
ATOM   2678 H  H    B ALA   A 1 129 ? 17.347 -3.760  -2.813  0.40 14.29 ?  129 ALA   A H    1 
ATOM   2679 H  HA   A ALA   A 1 129 ? 15.349 -3.230  -4.205  0.60 15.21 ?  129 ALA   A HA   1 
ATOM   2680 H  HA   B ALA   A 1 129 ? 15.383 -3.320  -4.561  0.40 15.19 ?  129 ALA   A HA   1 
ATOM   2681 H  HB1  A ALA   A 1 129 ? 14.170 -3.141  -2.195  0.60 16.40 ?  129 ALA   A HB1  1 
ATOM   2682 H  HB1  B ALA   A 1 129 ? 13.993 -3.308  -2.650  0.40 15.63 ?  129 ALA   A HB1  1 
ATOM   2683 H  HB2  A ALA   A 1 129 ? 15.057 -4.457  -2.259  0.60 16.40 ?  129 ALA   A HB2  1 
ATOM   2684 H  HB2  B ALA   A 1 129 ? 14.838 -4.648  -2.772  0.40 15.63 ?  129 ALA   A HB2  1 
ATOM   2685 H  HB3  A ALA   A 1 129 ? 15.539 -3.216  -1.392  0.60 16.40 ?  129 ALA   A HB3  1 
ATOM   2686 H  HB3  B ALA   A 1 129 ? 15.284 -3.518  -1.751  0.40 15.63 ?  129 ALA   A HB3  1 
ATOM   2687 N  N    A GLY   A 1 130 ? 14.667 -0.791  -3.294  0.60 11.29 ?  130 GLY   A N    1 
ATOM   2688 N  N    B GLY   A 1 130 ? 14.488 -0.986  -3.818  0.40 12.79 ?  130 GLY   A N    1 
ATOM   2689 C  CA   A GLY   A 1 130 ? 14.612 0.663   -3.282  0.60 11.82 ?  130 GLY   A CA   1 
ATOM   2690 C  CA   B GLY   A 1 130 ? 14.300 0.452   -3.779  0.40 13.03 ?  130 GLY   A CA   1 
ATOM   2691 C  C    A GLY   A 1 130 ? 15.177 1.242   -4.564  0.60 12.61 ?  130 GLY   A C    1 
ATOM   2692 C  C    B GLY   A 1 130 ? 15.067 1.144   -4.882  0.40 13.65 ?  130 GLY   A C    1 
ATOM   2693 O  O    A GLY   A 1 130 ? 14.844 0.798   -5.668  0.60 13.01 ?  130 GLY   A O    1 
ATOM   2694 O  O    B GLY   A 1 130 ? 15.080 0.706   -6.038  0.40 14.35 ?  130 GLY   A O    1 
ATOM   2695 H  H    A GLY   A 1 130 ? 13.911 -1.180  -3.196  0.60 13.71 ?  130 GLY   A H    1 
ATOM   2696 H  H    B GLY   A 1 130 ? 13.773 -1.439  -3.961  0.40 15.51 ?  130 GLY   A H    1 
ATOM   2697 H  HA2  A GLY   A 1 130 ? 13.693 0.959   -3.180  0.60 14.35 ?  130 GLY   A HA2  1 
ATOM   2698 H  HA2  B GLY   A 1 130 ? 13.356 0.657   -3.887  0.40 15.80 ?  130 GLY   A HA2  1 
ATOM   2699 H  HA3  A GLY   A 1 130 ? 15.131 1.009   -2.537  0.60 14.35 ?  130 GLY   A HA3  1 
ATOM   2700 H  HA3  B GLY   A 1 130 ? 14.602 0.806   -2.937  0.40 15.80 ?  130 GLY   A HA3  1 
ATOM   2701 N  N    A ILE   A 1 131 ? 16.060 2.240   -4.417  0.60 12.88 ?  131 ILE   A N    1 
ATOM   2702 N  N    B ILE   A 1 131 ? 15.731 2.244   -4.517  0.40 13.79 ?  131 ILE   A N    1 
ATOM   2703 C  CA   A ILE   A 1 131 ? 16.605 2.969   -5.564  0.60 13.34 ?  131 ILE   A CA   1 
ATOM   2704 C  CA   B ILE   A 1 131 ? 16.421 3.075   -5.494  0.40 13.95 ?  131 ILE   A CA   1 
ATOM   2705 C  C    A ILE   A 1 131 ? 17.596 2.161   -6.388  0.60 13.25 ?  131 ILE   A C    1 
ATOM   2706 C  C    B ILE   A 1 131 ? 17.476 2.311   -6.287  0.40 13.81 ?  131 ILE   A C    1 
ATOM   2707 O  O    A ILE   A 1 131 ? 17.979 2.612   -7.475  0.60 14.12 ?  131 ILE   A O    1 
ATOM   2708 O  O    B ILE   A 1 131 ? 17.978 2.833   -7.288  0.40 14.04 ?  131 ILE   A O    1 
ATOM   2709 C  CB   A ILE   A 1 131 ? 17.216 4.336   -5.179  0.60 14.19 ?  131 ILE   A CB   1 
ATOM   2710 C  CB   B ILE   A 1 131 ? 16.996 4.357   -4.846  0.40 14.83 ?  131 ILE   A CB   1 
ATOM   2711 C  CG1  A ILE   A 1 131 ? 18.482 4.174   -4.326  0.60 15.07 ?  131 ILE   A CG1  1 
ATOM   2712 C  CG1  B ILE   A 1 131 ? 18.157 4.031   -3.902  0.40 15.77 ?  131 ILE   A CG1  1 
ATOM   2713 C  CG2  A ILE   A 1 131 ? 16.190 5.189   -4.455  0.60 14.64 ?  131 ILE   A CG2  1 
ATOM   2714 C  CG2  B ILE   A 1 131 ? 15.898 5.124   -4.111  0.40 15.26 ?  131 ILE   A CG2  1 
ATOM   2715 C  CD1  A ILE   A 1 131 ? 19.119 5.509   -3.907  0.60 15.94 ?  131 ILE   A CD1  1 
ATOM   2716 C  CD1  B ILE   A 1 131 ? 18.807 5.263   -3.282  0.40 16.35 ?  131 ILE   A CD1  1 
ATOM   2717 H  H    A ILE   A 1 131 ? 16.358 2.511   -3.660  0.60 15.62 ?  131 ILE   A H    1 
ATOM   2718 H  H    B ILE   A 1 131 ? 15.777 2.533   -3.707  0.40 16.72 ?  131 ILE   A H    1 
ATOM   2719 H  HA   A ILE   A 1 131 ? 15.875 3.160   -6.160  0.60 16.17 ?  131 ILE   A HA   1 
ATOM   2720 H  HA   B ILE   A 1 131 ? 15.760 3.368   -6.132  0.40 16.90 ?  131 ILE   A HA   1 
ATOM   2721 H  HB   A ILE   A 1 131 ? 17.464 4.796   -5.997  0.60 17.19 ?  131 ILE   A HB   1 
ATOM   2722 H  HB   B ILE   A 1 131 ? 17.331 4.923   -5.555  0.40 17.96 ?  131 ILE   A HB   1 
ATOM   2723 H  HG12 A ILE   A 1 131 ? 18.259 3.687   -3.520  0.60 18.25 ?  131 ILE   A HG12 1 
ATOM   2724 H  HG12 B ILE   A 1 131 ? 17.828 3.474   -3.181  0.40 19.09 ?  131 ILE   A HG12 1 
ATOM   2725 H  HG13 A ILE   A 1 131 ? 19.148 3.684   -4.835  0.60 18.25 ?  131 ILE   A HG13 1 
ATOM   2726 H  HG13 B ILE   A 1 131 ? 18.842 3.558   -4.398  0.40 19.09 ?  131 ILE   A HG13 1 
ATOM   2727 H  HG21 A ILE   A 1 131 ? 16.513 6.102   -4.409  0.60 17.73 ?  131 ILE   A HG21 1 
ATOM   2728 H  HG21 B ILE   A 1 131 ? 16.229 6.007   -3.880  0.40 18.48 ?  131 ILE   A HG21 1 
ATOM   2729 H  HG22 A ILE   A 1 131 ? 15.356 5.157   -4.947  0.60 17.73 ?  131 ILE   A HG22 1 
ATOM   2730 H  HG22 B ILE   A 1 131 ? 15.126 5.204   -4.693  0.40 18.48 ?  131 ILE   A HG22 1 
ATOM   2731 H  HG23 A ILE   A 1 131 ? 16.062 4.834   -3.562  0.60 17.73 ?  131 ILE   A HG23 1 
ATOM   2732 H  HG23 B ILE   A 1 131 ? 15.656 4.640   -3.307  0.40 18.48 ?  131 ILE   A HG23 1 
ATOM   2733 H  HD11 A ILE   A 1 131 ? 19.985 5.334   -3.504  0.60 19.30 ?  131 ILE   A HD11 1 
ATOM   2734 H  HD11 B ILE   A 1 131 ? 19.605 4.991   -2.804  0.40 19.79 ?  131 ILE   A HD11 1 
ATOM   2735 H  HD12 A ILE   A 1 131 ? 19.229 6.068   -4.693  0.60 19.30 ?  131 ILE   A HD12 1 
ATOM   2736 H  HD12 B ILE   A 1 131 ? 19.041 5.886   -3.988  0.40 19.79 ?  131 ILE   A HD12 1 
ATOM   2737 H  HD13 A ILE   A 1 131 ? 18.540 5.950   -3.266  0.60 19.30 ?  131 ILE   A HD13 1 
ATOM   2738 H  HD13 B ILE   A 1 131 ? 18.180 5.679   -2.669  0.40 19.79 ?  131 ILE   A HD13 1 
ATOM   2739 N  N    A PHE   A 1 132 ? 18.028 0.986   -5.915  0.60 12.42 ?  132 PHE   A N    1 
ATOM   2740 N  N    B PHE   A 1 132 ? 17.821 1.087   -5.874  0.40 13.58 ?  132 PHE   A N    1 
ATOM   2741 C  CA   A PHE   A 1 132 ? 18.854 0.119   -6.750  0.60 12.68 ?  132 PHE   A CA   1 
ATOM   2742 C  CA   B PHE   A 1 132 ? 18.752 0.267   -6.640  0.40 13.68 ?  132 PHE   A CA   1 
ATOM   2743 C  C    A PHE   A 1 132 ? 18.036 -0.649  -7.786  0.60 13.28 ?  132 PHE   A C    1 
ATOM   2744 C  C    B PHE   A 1 132 ? 18.096 -0.461  -7.813  0.40 14.47 ?  132 PHE   A C    1 
ATOM   2745 O  O    A PHE   A 1 132 ? 18.625 -1.321  -8.639  0.60 13.42 ?  132 PHE   A O    1 
ATOM   2746 O  O    B PHE   A 1 132 ? 18.816 -0.964  -8.682  0.40 15.10 ?  132 PHE   A O    1 
ATOM   2747 C  CB   A PHE   A 1 132 ? 19.687 -0.856  -5.901  0.60 11.83 ?  132 PHE   A CB   1 
ATOM   2748 C  CB   B PHE   A 1 132 ? 19.478 -0.725  -5.724  0.40 13.12 ?  132 PHE   A CB   1 
ATOM   2749 C  CG   A PHE   A 1 132 ? 20.911 -0.238  -5.246  0.60 11.62 ?  132 PHE   A CG   1 
ATOM   2750 C  CG   B PHE   A 1 132 ? 20.687 -0.149  -5.021  0.40 12.46 ?  132 PHE   A CG   1 
ATOM   2751 C  CD1  A PHE   A 1 132 ? 20.797 0.818   -4.355  0.60 12.13 ?  132 PHE   A CD1  1 
ATOM   2752 C  CD1  B PHE   A 1 132 ? 20.550 0.845   -4.065  0.40 12.76 ?  132 PHE   A CD1  1 
ATOM   2753 C  CD2  A PHE   A 1 132 ? 22.173 -0.762  -5.489  0.60 12.40 ?  132 PHE   A CD2  1 
ATOM   2754 C  CD2  B PHE   A 1 132 ? 21.958 -0.628  -5.301  0.40 12.45 ?  132 PHE   A CD2  1 
ATOM   2755 C  CE1  A PHE   A 1 132 ? 21.923 1.358   -3.745  0.60 12.08 ?  132 PHE   A CE1  1 
ATOM   2756 C  CE1  B PHE   A 1 132 ? 21.661 1.363   -3.415  0.40 12.93 ?  132 PHE   A CE1  1 
ATOM   2757 C  CE2  A PHE   A 1 132 ? 23.297 -0.231  -4.881  0.60 12.86 ?  132 PHE   A CE2  1 
ATOM   2758 C  CE2  B PHE   A 1 132 ? 23.071 -0.118  -4.652  0.40 12.85 ?  132 PHE   A CE2  1 
ATOM   2759 C  CZ   A PHE   A 1 132 ? 23.169 0.833   -4.008  0.60 12.27 ?  132 PHE   A CZ   1 
ATOM   2760 C  CZ   B PHE   A 1 132 ? 22.921 0.881   -3.710  0.40 12.68 ?  132 PHE   A CZ   1 
ATOM   2761 H  H    A PHE   A 1 132 ? 17.867 0.674   -5.126  0.60 15.06 ?  132 PHE   A H    1 
ATOM   2762 H  H    B PHE   A 1 132 ? 17.540 0.719   -5.148  0.40 16.46 ?  132 PHE   A H    1 
ATOM   2763 H  HA   A PHE   A 1 132 ? 19.485 0.672   -7.231  0.60 15.38 ?  132 PHE   A HA   1 
ATOM   2764 H  HA   B PHE   A 1 132 ? 19.425 0.852   -7.014  0.40 16.58 ?  132 PHE   A HA   1 
ATOM   2765 H  HB2  A PHE   A 1 132 ? 19.131 -1.210  -5.193  0.60 14.36 ?  132 PHE   A HB2  1 
ATOM   2766 H  HB2  B PHE   A 1 132 ? 18.862 -1.029  -5.041  0.40 15.91 ?  132 PHE   A HB2  1 
ATOM   2767 H  HB3  A PHE   A 1 132 ? 19.999 -1.587  -6.467  0.60 14.36 ?  132 PHE   A HB3  1 
ATOM   2768 H  HB3  B PHE   A 1 132 ? 19.779 -1.477  -6.256  0.40 15.91 ?  132 PHE   A HB3  1 
ATOM   2769 H  HD1  A PHE   A 1 132 ? 19.962 1.177   -4.169  0.60 14.73 ?  132 PHE   A HD1  1 
ATOM   2770 H  HD1  B PHE   A 1 132 ? 19.704 1.175   -3.863  0.40 15.48 ?  132 PHE   A HD1  1 
ATOM   2771 H  HD2  A PHE   A 1 132 ? 22.271 -1.480  -6.073  0.60 15.05 ?  132 PHE   A HD2  1 
ATOM   2772 H  HD2  B PHE   A 1 132 ? 22.067 -1.300  -5.936  0.40 15.11 ?  132 PHE   A HD2  1 
ATOM   2773 H  HE1  A PHE   A 1 132 ? 21.839 2.073   -3.154  0.60 14.67 ?  132 PHE   A HE1  1 
ATOM   2774 H  HE1  B PHE   A 1 132 ? 21.557 2.034   -2.780  0.40 15.68 ?  132 PHE   A HE1  1 
ATOM   2775 H  HE2  A PHE   A 1 132 ? 24.140 -0.587  -5.062  0.60 15.60 ?  132 PHE   A HE2  1 
ATOM   2776 H  HE2  B PHE   A 1 132 ? 23.920 -0.445  -4.856  0.40 15.58 ?  132 PHE   A HE2  1 
ATOM   2777 H  HZ   A PHE   A 1 132 ? 23.927 1.195   -3.600  0.60 14.89 ?  132 PHE   A HZ   1 
ATOM   2778 H  HZ   B PHE   A 1 132 ? 23.667 1.227   -3.274  0.40 15.38 ?  132 PHE   A HZ   1 
ATOM   2779 N  N    A GLY   A 1 133 ? 16.704 -0.587  -7.722  0.60 13.71 ?  133 GLY   A N    1 
ATOM   2780 N  N    B GLY   A 1 133 ? 16.766 -0.542  -7.865  0.40 14.49 ?  133 GLY   A N    1 
ATOM   2781 C  CA   A GLY   A 1 133 ? 15.860 -0.949  -8.842  0.60 13.83 ?  133 GLY   A CA   1 
ATOM   2782 C  CA   B GLY   A 1 133 ? 16.080 -0.905  -9.089  0.40 14.59 ?  133 GLY   A CA   1 
ATOM   2783 C  C    A GLY   A 1 133 ? 15.473 -2.406  -8.981  0.60 13.78 ?  133 GLY   A C    1 
ATOM   2784 C  C    B GLY   A 1 133 ? 15.754 -2.370  -9.305  0.40 14.67 ?  133 GLY   A C    1 
ATOM   2785 O  O    A GLY   A 1 133 ? 14.716 -2.729  -9.905  0.60 14.67 ?  133 GLY   A O    1 
ATOM   2786 O  O    B GLY   A 1 133 ? 15.180 -2.699  -10.350 0.40 14.55 ?  133 GLY   A O    1 
ATOM   2787 H  H    A GLY   A 1 133 ? 16.266 -0.337  -7.024  0.60 16.62 ?  133 GLY   A H    1 
ATOM   2788 H  H    B GLY   A 1 133 ? 16.239 -0.381  -7.201  0.40 17.55 ?  133 GLY   A H    1 
ATOM   2789 H  HA2  A GLY   A 1 133 ? 15.036 -0.441  -8.783  0.60 16.76 ?  133 GLY   A HA2  1 
ATOM   2790 H  HA2  B GLY   A 1 133 ? 15.244 -0.420  -9.127  0.40 17.68 ?  133 GLY   A HA2  1 
ATOM   2791 H  HA3  A GLY   A 1 133 ? 16.307 -0.691  -9.663  0.60 16.76 ?  133 GLY   A HA3  1 
ATOM   2792 H  HA3  B GLY   A 1 133 ? 16.623 -0.619  -9.840  0.40 17.68 ?  133 GLY   A HA3  1 
ATOM   2793 N  N    A ALA   A 1 134 ? 15.951 -3.299  -8.116  0.60 13.22 ?  134 ALA   A N    1 
ATOM   2794 N  N    B ALA   A 1 134 ? 16.089 -3.260  -8.375  0.40 14.93 ?  134 ALA   A N    1 
ATOM   2795 C  CA   A ALA   A 1 134 ? 15.567 -4.694  -8.255  0.60 13.67 ?  134 ALA   A CA   1 
ATOM   2796 C  CA   B ALA   A 1 134 ? 15.798 -4.674  -8.569  0.40 15.21 ?  134 ALA   A CA   1 
ATOM   2797 C  C    A ALA   A 1 134 ? 14.222 -4.955  -7.582  0.60 14.04 ?  134 ALA   A C    1 
ATOM   2798 C  C    B ALA   A 1 134 ? 14.429 -5.035  -7.992  0.40 15.41 ?  134 ALA   A C    1 
ATOM   2799 O  O    A ALA   A 1 134 ? 13.746 -4.173  -6.753  0.60 14.78 ?  134 ALA   A O    1 
ATOM   2800 O  O    B ALA   A 1 134 ? 13.800 -4.257  -7.274  0.40 16.01 ?  134 ALA   A O    1 
ATOM   2801 C  CB   A ALA   A 1 134 ? 16.626 -5.623  -7.663  0.60 14.46 ?  134 ALA   A CB   1 
ATOM   2802 C  CB   B ALA   A 1 134 ? 16.893 -5.545  -7.954  0.40 15.52 ?  134 ALA   A CB   1 
ATOM   2803 H  H    A ALA   A 1 134 ? 16.488 -3.123  -7.463  0.60 16.03 ?  134 ALA   A H    1 
ATOM   2804 H  H    B ALA   A 1 134 ? 16.487 -3.071  -7.633  0.40 18.08 ?  134 ALA   A H    1 
ATOM   2805 H  HA   A ALA   A 1 134 ? 15.480 -4.900  -9.199  0.60 16.56 ?  134 ALA   A HA   1 
ATOM   2806 H  HA   B ALA   A 1 134 ? 15.772 -4.859  -9.518  0.40 18.42 ?  134 ALA   A HA   1 
ATOM   2807 H  HB1  A ALA   A 1 134 ? 16.342 -6.540  -7.793  0.60 17.52 ?  134 ALA   A HB1  1 
ATOM   2808 H  HB1  B ALA   A 1 134 ? 16.673 -6.478  -8.105  0.40 18.79 ?  134 ALA   A HB1  1 
ATOM   2809 H  HB2  A ALA   A 1 134 ? 17.468 -5.467  -8.117  0.60 17.52 ?  134 ALA   A HB2  1 
ATOM   2810 H  HB2  B ALA   A 1 134 ? 17.739 -5.332  -8.379  0.40 18.79 ?  134 ALA   A HB2  1 
ATOM   2811 H  HB3  A ALA   A 1 134 ? 16.717 -5.433  -6.717  0.60 17.52 ?  134 ALA   A HB3  1 
ATOM   2812 H  HB3  B ALA   A 1 134 ? 16.945 -5.366  -7.003  0.40 18.79 ?  134 ALA   A HB3  1 
ATOM   2813 N  N    A ASP   A 1 135 ? 13.615 -6.076  -7.954  0.60 14.66 ?  135 ASP   A N    1 
ATOM   2814 N  N    B ASP   A 1 135 ? 13.968 -6.239  -8.326  0.40 15.92 ?  135 ASP   A N    1 
ATOM   2815 C  CA   A ASP   A 1 135 ? 12.362 -6.527  -7.357  0.60 15.81 ?  135 ASP   A CA   1 
ATOM   2816 C  CA   B ASP   A 1 135 ? 12.684 -6.724  -7.831  0.40 16.97 ?  135 ASP   A CA   1 
ATOM   2817 C  C    A ASP   A 1 135 ? 12.625 -6.977  -5.925  0.60 15.08 ?  135 ASP   A C    1 
ATOM   2818 C  C    B ASP   A 1 135 ? 12.838 -7.182  -6.386  0.40 16.10 ?  135 ASP   A C    1 
ATOM   2819 O  O    A ASP   A 1 135 ? 13.384 -7.935  -5.721  0.60 14.77 ?  135 ASP   A O    1 
ATOM   2820 O  O    B ASP   A 1 135 ? 13.656 -8.067  -6.112  0.40 15.67 ?  135 ASP   A O    1 
ATOM   2821 C  CB   A ASP   A 1 135 ? 11.855 -7.705  -8.185  0.60 17.75 ?  135 ASP   A CB   1 
ATOM   2822 C  CB   B ASP   A 1 135 ? 12.186 -7.878  -8.690  0.40 19.45 ?  135 ASP   A CB   1 
ATOM   2823 C  CG   A ASP   A 1 135 ? 10.561 -8.300  -7.654  0.60 19.77 ?  135 ASP   A CG   1 
ATOM   2824 C  CG   B ASP   A 1 135 ? 10.973 -8.576  -8.091  0.40 21.74 ?  135 ASP   A CG   1 
ATOM   2825 O  OD1  A ASP   A 1 135 ? 10.064 -7.845  -6.604  0.60 20.36 ?  135 ASP   A OD1  1 
ATOM   2826 O  OD1  B ASP   A 1 135 ? 10.006 -7.882  -7.714  0.40 22.87 ?  135 ASP   A OD1  1 
ATOM   2827 O  OD2  A ASP   A 1 135 ? 10.033 -9.221  -8.315  0.60 22.30 -1 135 ASP   A OD2  1 
ATOM   2828 O  OD2  B ASP   A 1 135 ? 10.984 -9.822  -8.008  0.40 22.78 -1 135 ASP   A OD2  1 
ATOM   2829 H  H    A ASP   A 1 135 ? 13.910 -6.603  -8.561  0.60 17.75 ?  135 ASP   A H    1 
ATOM   2830 H  H    B ASP   A 1 135 ? 14.382 -6.794  -8.836  0.40 19.26 ?  135 ASP   A H    1 
ATOM   2831 H  HA   A ASP   A 1 135 ? 11.696 -5.813  -7.379  0.60 19.14 ?  135 ASP   A HA   1 
ATOM   2832 H  HA   B ASP   A 1 135 ? 12.038 -6.006  -7.879  0.40 20.52 ?  135 ASP   A HA   1 
ATOM   2833 H  HB2  A ASP   A 1 135 ? 11.689 -7.408  -9.091  0.60 21.46 ?  135 ASP   A HB2  1 
ATOM   2834 H  HB2  B ASP   A 1 135 ? 11.935 -7.533  -9.562  0.40 23.50 ?  135 ASP   A HB2  1 
ATOM   2835 H  HB3  A ASP   A 1 135 ? 12.528 -8.402  -8.180  0.60 21.46 ?  135 ASP   A HB3  1 
ATOM   2836 H  HB3  B ASP   A 1 135 ? 12.893 -8.533  -8.781  0.40 23.50 ?  135 ASP   A HB3  1 
ATOM   2837 N  N    A PRO   A 1 136 ? 12.050 -6.324  -4.911  0.60 14.83 ?  136 PRO   A N    1 
ATOM   2838 N  N    B PRO   A 1 136 ? 12.083 -6.616  -5.439  0.40 15.60 ?  136 PRO   A N    1 
ATOM   2839 C  CA   A PRO   A 1 136 ? 12.307 -6.763  -3.528  0.60 15.00 ?  136 PRO   A CA   1 
ATOM   2840 C  CA   B PRO   A 1 136 ? 12.311 -6.966  -4.027  0.40 15.41 ?  136 PRO   A CA   1 
ATOM   2841 C  C    A PRO   A 1 136 ? 11.880 -8.195  -3.242  0.60 14.44 ?  136 PRO   A C    1 
ATOM   2842 C  C    B PRO   A 1 136 ? 11.904 -8.383  -3.675  0.40 15.15 ?  136 PRO   A C    1 
ATOM   2843 O  O    A PRO   A 1 136 ? 12.451 -8.828  -2.346  0.60 13.29 ?  136 PRO   A O    1 
ATOM   2844 O  O    B PRO   A 1 136 ? 12.585 -9.028  -2.872  0.40 14.72 ?  136 PRO   A O    1 
ATOM   2845 C  CB   A PRO   A 1 136 ? 11.539 -5.735  -2.679  0.60 15.82 ?  136 PRO   A CB   1 
ATOM   2846 C  CB   B PRO   A 1 136 ? 11.478 -5.921  -3.274  0.40 15.58 ?  136 PRO   A CB   1 
ATOM   2847 C  CG   A PRO   A 1 136 ? 10.536 -5.132  -3.615  0.60 16.43 ?  136 PRO   A CG   1 
ATOM   2848 C  CG   B PRO   A 1 136 ? 10.395 -5.556  -4.234  0.40 15.80 ?  136 PRO   A CG   1 
ATOM   2849 C  CD   A PRO   A 1 136 ? 11.195 -5.123  -4.956  0.60 15.46 ?  136 PRO   A CD   1 
ATOM   2850 C  CD   B PRO   A 1 136 ? 10.999 -5.633  -5.602  0.40 15.74 ?  136 PRO   A CD   1 
ATOM   2851 H  HA   A PRO   A 1 136 ? 13.254 -6.672  -3.329  0.60 18.16 ?  136 PRO   A HA   1 
ATOM   2852 H  HA   B PRO   A 1 136 ? 13.248 -6.848  -3.797  0.40 18.66 ?  136 PRO   A HA   1 
ATOM   2853 H  HB2  A PRO   A 1 136 ? 11.096 -6.182  -1.942  0.60 19.15 ?  136 PRO   A HB2  1 
ATOM   2854 H  HB2  B PRO   A 1 136 ? 11.109 -6.316  -2.468  0.40 18.86 ?  136 PRO   A HB2  1 
ATOM   2855 H  HB3  A PRO   A 1 136 ? 12.151 -5.055  -2.349  0.60 19.15 ?  136 PRO   A HB3  1 
ATOM   2856 H  HB3  B PRO   A 1 136 ? 12.032 -5.154  -3.061  0.40 18.86 ?  136 PRO   A HB3  1 
ATOM   2857 H  HG2  A PRO   A 1 136 ? 9.738  -5.682  -3.635  0.60 19.88 ?  136 PRO   A HG2  1 
ATOM   2858 H  HG2  B PRO   A 1 136 ? 9.666  -6.186  -4.150  0.40 19.12 ?  136 PRO   A HG2  1 
ATOM   2859 H  HG3  A PRO   A 1 136 ? 10.324 -4.229  -3.333  0.60 19.88 ?  136 PRO   A HG3  1 
ATOM   2860 H  HG3  B PRO   A 1 136 ? 10.096 -4.655  -4.048  0.40 19.12 ?  136 PRO   A HG3  1 
ATOM   2861 H  HD2  A PRO   A 1 136 ? 10.527 -5.202  -5.657  0.60 18.72 ?  136 PRO   A HD2  1 
ATOM   2862 H  HD2  B PRO   A 1 136 ? 10.350 -5.960  -6.243  0.40 19.05 ?  136 PRO   A HD2  1 
ATOM   2863 H  HD3  A PRO   A 1 136 ? 11.732 -4.320  -5.067  0.60 18.72 ?  136 PRO   A HD3  1 
ATOM   2864 H  HD3  B PRO   A 1 136 ? 11.359 -4.772  -5.868  0.40 19.05 ?  136 PRO   A HD3  1 
ATOM   2865 N  N    A ILE   A 1 137 ? 10.886 -8.724  -3.960  0.60 15.10 ?  137 ILE   A N    1 
ATOM   2866 N  N    B ILE   A 1 137 ? 10.795 -8.879  -4.226  0.40 15.65 ?  137 ILE   A N    1 
ATOM   2867 C  CA   A ILE   A 1 137 ? 10.496 -10.122 -3.771  0.60 15.81 ?  137 ILE   A CA   1 
ATOM   2868 C  CA   B ILE   A 1 137 ? 10.433 -10.279 -4.018  0.40 16.28 ?  137 ILE   A CA   1 
ATOM   2869 C  C    A ILE   A 1 137 ? 11.638 -11.049 -4.180  0.60 15.60 ?  137 ILE   A C    1 
ATOM   2870 C  C    B ILE   A 1 137 ? 11.608 -11.170 -4.385  0.40 15.87 ?  137 ILE   A C    1 
ATOM   2871 O  O    A ILE   A 1 137 ? 11.970 -12.010 -3.472  0.60 15.66 ?  137 ILE   A O    1 
ATOM   2872 O  O    B ILE   A 1 137 ? 11.903 -12.163 -3.708  0.40 15.75 ?  137 ILE   A O    1 
ATOM   2873 C  CB   A ILE   A 1 137 ? 9.195  -10.428 -4.538  0.60 17.14 ?  137 ILE   A CB   1 
ATOM   2874 C  CB   B ILE   A 1 137 ? 9.175  -10.631 -4.835  0.40 17.53 ?  137 ILE   A CB   1 
ATOM   2875 C  CG1  A ILE   A 1 137 ? 8.007  -9.656  -3.941  0.60 18.27 ?  137 ILE   A CG1  1 
ATOM   2876 C  CG1  B ILE   A 1 137 ? 8.066  -9.600  -4.590  0.40 18.50 ?  137 ILE   A CG1  1 
ATOM   2877 C  CG2  A ILE   A 1 137 ? 8.920  -11.932 -4.548  0.60 17.93 ?  137 ILE   A CG2  1 
ATOM   2878 C  CG2  B ILE   A 1 137 ? 8.695  -12.030 -4.484  0.40 18.04 ?  137 ILE   A CG2  1 
ATOM   2879 C  CD1  A ILE   A 1 137 ? 6.710  -9.851  -4.697  0.60 19.44 ?  137 ILE   A CD1  1 
ATOM   2880 C  CD1  B ILE   A 1 137 ? 6.817  -9.837  -5.404  0.40 19.31 ?  137 ILE   A CD1  1 
ATOM   2881 H  H    A ILE   A 1 137 ? 10.436 -8.296  -4.552  0.60 18.29 ?  137 ILE   A H    1 
ATOM   2882 H  H    B ILE   A 1 137 ? 10.253 -8.430  -4.714  0.40 18.95 ?  137 ILE   A H    1 
ATOM   2883 H  HA   A ILE   A 1 137 ? 10.329 -10.268 -2.830  0.60 19.14 ?  137 ILE   A HA   1 
ATOM   2884 H  HA   B ILE   A 1 137 ? 10.234 -10.426 -3.082  0.40 19.70 ?  137 ILE   A HA   1 
ATOM   2885 H  HB   A ILE   A 1 137 ? 9.308  -10.133 -5.452  0.60 20.73 ?  137 ILE   A HB   1 
ATOM   2886 H  HB   B ILE   A 1 137 ? 9.406  -10.616 -5.775  0.40 21.20 ?  137 ILE   A HB   1 
ATOM   2887 H  HG12 A ILE   A 1 137 ? 7.867  -9.949  -3.027  0.60 22.08 ?  137 ILE   A HG12 1 
ATOM   2888 H  HG12 B ILE   A 1 137 ? 7.828  -9.621  -3.650  0.40 22.37 ?  137 ILE   A HG12 1 
ATOM   2889 H  HG13 A ILE   A 1 137 ? 8.216  -8.703  -3.948  0.60 22.08 ?  137 ILE   A HG13 1 
ATOM   2890 H  HG13 B ILE   A 1 137 ? 8.391  -8.715  -4.823  0.40 22.37 ?  137 ILE   A HG13 1 
ATOM   2891 H  HG21 A ILE   A 1 137 ? 8.082  -12.103 -5.004  0.60 21.69 ?  137 ILE   A HG21 1 
ATOM   2892 H  HG21 B ILE   A 1 137 ? 7.935  -12.255 -5.041  0.40 21.82 ?  137 ILE   A HG21 1 
ATOM   2893 H  HG22 A ILE   A 1 137 ? 9.632  -12.384 -5.019  0.60 21.69 ?  137 ILE   A HG22 1 
ATOM   2894 H  HG22 B ILE   A 1 137 ? 9.414  -12.661 -4.643  0.40 21.82 ?  137 ILE   A HG22 1 
ATOM   2895 H  HG23 A ILE   A 1 137 ? 8.868  -12.247 -3.633  0.60 21.69 ?  137 ILE   A HG23 1 
ATOM   2896 H  HG23 B ILE   A 1 137 ? 8.440  -12.049 -3.550  0.40 21.82 ?  137 ILE   A HG23 1 
ATOM   2897 H  HD11 A ILE   A 1 137 ? 6.024  -9.359  -4.234  0.60 23.50 ?  137 ILE   A HD11 1 
ATOM   2898 H  HD11 B ILE   A 1 137 ? 6.567  -9.008  -5.837  0.40 23.34 ?  137 ILE   A HD11 1 
ATOM   2899 H  HD12 A ILE   A 1 137 ? 6.816  -9.516  -5.604  0.60 23.50 ?  137 ILE   A HD12 1 
ATOM   2900 H  HD12 B ILE   A 1 137 ? 6.999  -10.516 -6.071  0.40 23.34 ?  137 ILE   A HD12 1 
ATOM   2901 H  HD13 A ILE   A 1 137 ? 6.479  -10.792 -4.715  0.60 23.50 ?  137 ILE   A HD13 1 
ATOM   2902 H  HD13 B ILE   A 1 137 ? 6.109  -10.133 -4.811  0.40 23.34 ?  137 ILE   A HD13 1 
ATOM   2903 N  N    A HIS   A 1 138 ? 12.250 -10.776 -5.335  0.60 15.68 ?  138 HIS   A N    1 
ATOM   2904 N  N    B HIS   A 1 138 ? 12.302 -10.816 -5.465  0.40 15.88 ?  138 HIS   A N    1 
ATOM   2905 C  CA   A HIS   A 1 138 ? 13.402 -11.561 -5.770  0.60 15.63 ?  138 HIS   A CA   1 
ATOM   2906 C  CA   B HIS   A 1 138 ? 13.486 -11.556 -5.874  0.40 15.43 ?  138 HIS   A CA   1 
ATOM   2907 C  C    A HIS   A 1 138 ? 14.562 -11.422 -4.792  0.60 15.01 ?  138 HIS   A C    1 
ATOM   2908 C  C    B HIS   A 1 138 ? 14.617 -11.410 -4.858  0.40 14.86 ?  138 HIS   A C    1 
ATOM   2909 O  O    A HIS   A 1 138 ? 15.217 -12.413 -4.445  0.60 15.02 ?  138 HIS   A O    1 
ATOM   2910 O  O    B HIS   A 1 138 ? 15.301 -12.391 -4.540  0.40 14.74 ?  138 HIS   A O    1 
ATOM   2911 C  CB   A HIS   A 1 138 ? 13.824 -11.137 -7.176  0.60 16.35 ?  138 HIS   A CB   1 
ATOM   2912 C  CB   B HIS   A 1 138 ? 13.916 -11.072 -7.255  0.40 16.11 ?  138 HIS   A CB   1 
ATOM   2913 C  CG   A HIS   A 1 138 ? 15.083 -11.795 -7.647  0.60 17.38 ?  138 HIS   A CG   1 
ATOM   2914 C  CG   B HIS   A 1 138 ? 15.209 -11.655 -7.717  0.40 16.96 ?  138 HIS   A CG   1 
ATOM   2915 N  ND1  A HIS   A 1 138 ? 15.169 -13.148 -7.899  0.60 18.35 ?  138 HIS   A ND1  1 
ATOM   2916 N  ND1  B HIS   A 1 138 ? 15.367 -12.997 -7.983  0.40 17.66 ?  138 HIS   A ND1  1 
ATOM   2917 C  CD2  A HIS   A 1 138 ? 16.312 -11.287 -7.900  0.60 17.47 ?  138 HIS   A CD2  1 
ATOM   2918 C  CD2  B HIS   A 1 138 ? 16.410 -11.078 -7.948  0.40 17.11 ?  138 HIS   A CD2  1 
ATOM   2919 C  CE1  A HIS   A 1 138 ? 16.394 -13.443 -8.295  0.60 18.43 ?  138 HIS   A CE1  1 
ATOM   2920 C  CE1  B HIS   A 1 138 ? 16.611 -13.221 -8.365  0.40 17.61 ?  138 HIS   A CE1  1 
ATOM   2921 N  NE2  A HIS   A 1 138 ? 17.108 -12.332 -8.303  0.60 17.76 ?  138 HIS   A NE2  1 
ATOM   2922 N  NE2  B HIS   A 1 138 ? 17.264 -12.074 -8.353  0.40 17.25 ?  138 HIS   A NE2  1 
ATOM   2923 H  H    A HIS   A 1 138 ? 12.024 -10.147 -5.882  0.60 18.99 ?  138 HIS   A H    1 
ATOM   2924 H  H    B HIS   A 1 138 ? 12.101 -10.157 -5.982  0.40 19.22 ?  138 HIS   A H    1 
ATOM   2925 H  HA   A HIS   A 1 138 ? 13.151 -12.495 -5.807  0.60 18.92 ?  138 HIS   A HA   1 
ATOM   2926 H  HA   B HIS   A 1 138 ? 13.260 -12.496 -5.946  0.40 18.68 ?  138 HIS   A HA   1 
ATOM   2927 H  HB2  A HIS   A 1 138 ? 13.118 -11.369 -7.801  0.60 19.79 ?  138 HIS   A HB2  1 
ATOM   2928 H  HB2  B HIS   A 1 138 ? 13.229 -11.317 -7.898  0.40 19.49 ?  138 HIS   A HB2  1 
ATOM   2929 H  HB3  A HIS   A 1 138 ? 13.969 -10.178 -7.188  0.60 19.79 ?  138 HIS   A HB3  1 
ATOM   2930 H  HB3  B HIS   A 1 138 ? 14.013 -10.108 -7.235  0.40 19.49 ?  138 HIS   A HB3  1 
ATOM   2931 H  HD1  A HIS   A 1 138 ? 14.526 -13.710 -7.819  0.60 22.18 ?  138 HIS   A HD1  1 
ATOM   2932 H  HD2  A HIS   A 1 138 ? 16.572 -10.397 -7.819  0.60 21.12 ?  138 HIS   A HD2  1 
ATOM   2933 H  HD2  B HIS   A 1 138 ? 16.614 -10.175 -7.853  0.40 20.69 ?  138 HIS   A HD2  1 
ATOM   2934 H  HE1  A HIS   A 1 138 ? 16.704 -14.290 -8.527  0.60 22.27 ?  138 HIS   A HE1  1 
ATOM   2935 H  HE1  B HIS   A 1 138 ? 16.961 -14.047 -8.601  0.40 21.29 ?  138 HIS   A HE1  1 
ATOM   2936 H  HE2  B HIS   A 1 138 ? 18.087 -11.967 -8.562  0.40 20.87 ?  138 HIS   A HE2  1 
ATOM   2937 N  N    . SER   A 1 139 ? 14.829 -10.200 -4.335  1.00 14.60 ?  139 SER   A N    1 
ATOM   2938 C  CA   . SER   A 1 139 ? 15.900 -10.003 -3.368  1.00 13.98 ?  139 SER   A CA   1 
ATOM   2939 C  C    . SER   A 1 139 ? 15.680 -10.846 -2.116  1.00 13.46 ?  139 SER   A C    1 
ATOM   2940 O  O    . SER   A 1 139 ? 16.629 -11.437 -1.586  1.00 13.49 ?  139 SER   A O    1 
ATOM   2941 C  CB   . SER   A 1 139 ? 16.028 -8.523  -3.020  1.00 13.78 ?  139 SER   A CB   1 
ATOM   2942 O  OG   . SER   A 1 139 ? 17.106 -8.349  -2.116  1.00 14.05 ?  139 SER   A OG   1 
ATOM   2943 H  H    A SER   A 1 139 ? 14.404 -9.486  -4.558  0.60 17.68 ?  139 SER   A H    1 
ATOM   2944 H  H    B SER   A 1 139 ? 14.373 -9.495  -4.521  0.40 17.68 ?  139 SER   A H    1 
ATOM   2945 H  HA   . SER   A 1 139 ? 16.737 -10.282 -3.768  1.00 16.95 ?  139 SER   A HA   1 
ATOM   2946 H  HB2  . SER   A 1 139 ? 16.202 -8.012  -3.829  1.00 16.71 ?  139 SER   A HB2  1 
ATOM   2947 H  HB3  . SER   A 1 139 ? 15.202 -8.217  -2.608  1.00 16.71 ?  139 SER   A HB3  1 
ATOM   2948 H  HG   . SER   A 1 139 ? 17.190 -7.535  -1.916  1.00 17.03 ?  139 SER   A HG   1 
ATOM   2949 N  N    . LEU   A 1 140 ? 14.441 -10.902 -1.622  1.00 13.40 ?  140 LEU   A N    1 
ATOM   2950 C  CA   . LEU   A 1 140 ? 14.168 -11.717 -0.442  1.00 13.32 ?  140 LEU   A CA   1 
ATOM   2951 C  C    . LEU   A 1 140 ? 14.436 -13.193 -0.721  1.00 13.13 ?  140 LEU   A C    1 
ATOM   2952 O  O    . LEU   A 1 140 ? 14.989 -13.905 0.126   1.00 13.66 ?  140 LEU   A O    1 
ATOM   2953 C  CB   . LEU   A 1 140 ? 12.726 -11.499 0.016   1.00 13.58 ?  140 LEU   A CB   1 
ATOM   2954 C  CG   . LEU   A 1 140 ? 12.267 -12.355 1.195   1.00 14.03 ?  140 LEU   A CG   1 
ATOM   2955 C  CD1  . LEU   A 1 140 ? 13.181 -12.173 2.399   1.00 14.21 ?  140 LEU   A CD1  1 
ATOM   2956 C  CD2  . LEU   A 1 140 ? 10.811 -12.033 1.563   1.00 14.89 ?  140 LEU   A CD2  1 
ATOM   2957 H  H    . LEU   A 1 140 ? 13.761 -10.480 -1.937  1.00 16.25 ?  140 LEU   A H    1 
ATOM   2958 H  HA   . LEU   A 1 140 ? 14.753 -11.439 0.280   1.00 16.14 ?  140 LEU   A HA   1 
ATOM   2959 H  HB2  . LEU   A 1 140 ? 12.620 -10.576 0.279   1.00 16.46 ?  140 LEU   A HB2  1 
ATOM   2960 H  HB3  . LEU   A 1 140 ? 12.135 -11.698 -0.726  1.00 16.46 ?  140 LEU   A HB3  1 
ATOM   2961 H  HG   . LEU   A 1 140 ? 12.295 -13.294 0.940   1.00 17.01 ?  140 LEU   A HG   1 
ATOM   2962 H  HD11 . LEU   A 1 140 ? 12.800 -12.639 3.161   1.00 17.22 ?  140 LEU   A HD11 1 
ATOM   2963 H  HD12 . LEU   A 1 140 ? 14.053 -12.547 2.190   1.00 17.22 ?  140 LEU   A HD12 1 
ATOM   2964 H  HD13 . LEU   A 1 140 ? 13.260 -11.229 2.593   1.00 17.22 ?  140 LEU   A HD13 1 
ATOM   2965 H  HD21 . LEU   A 1 140 ? 10.540 -12.590 2.313   1.00 18.03 ?  140 LEU   A HD21 1 
ATOM   2966 H  HD22 . LEU   A 1 140 ? 10.746 -11.098 1.808   1.00 18.03 ?  140 LEU   A HD22 1 
ATOM   2967 H  HD23 . LEU   A 1 140 ? 10.242 -12.216 0.798   1.00 18.03 ?  140 LEU   A HD23 1 
ATOM   2968 N  N    . ARG   A 1 141 ? 14.038 -13.670 -1.904  1.00 14.15 ?  141 ARG   A N    1 
ATOM   2969 C  CA   . ARG   A 1 141 ? 14.284 -15.059 -2.277  1.00 14.94 ?  141 ARG   A CA   1 
ATOM   2970 C  C    . ARG   A 1 141 ? 15.781 -15.361 -2.286  1.00 13.98 ?  141 ARG   A C    1 
ATOM   2971 O  O    . ARG   A 1 141 ? 16.228 -16.377 -1.738  1.00 14.03 ?  141 ARG   A O    1 
ATOM   2972 C  CB   . ARG   A 1 141 ? 13.669 -15.306 -3.656  1.00 16.96 ?  141 ARG   A CB   1 
ATOM   2973 C  CG   . ARG   A 1 141 ? 13.649 -16.748 -4.109  1.00 19.68 ?  141 ARG   A CG   1 
ATOM   2974 C  CD   . ARG   A 1 141 ? 12.619 -17.517 -3.343  1.00 21.62 ?  141 ARG   A CD   1 
ATOM   2975 N  NE   . ARG   A 1 141 ? 13.234 -18.296 -2.282  1.00 22.28 ?  141 ARG   A NE   1 
ATOM   2976 C  CZ   . ARG   A 1 141 ? 12.556 -18.875 -1.301  1.00 23.19 ?  141 ARG   A CZ   1 
ATOM   2977 N  NH1  . ARG   A 1 141 ? 11.260 -18.666 -1.138  1.00 22.80 ?  141 ARG   A NH1  1 
ATOM   2978 N  NH2  . ARG   A 1 141 ? 13.197 -19.671 -0.452  1.00 23.69 ?  141 ARG   A NH2  1 
ATOM   2979 H  H    . ARG   A 1 141 ? 13.630 -13.209 -2.504  1.00 17.15 ?  141 ARG   A H    1 
ATOM   2980 H  HA   . ARG   A 1 141 ? 13.856 -15.648 -1.639  1.00 18.09 ?  141 ARG   A HA   1 
ATOM   2981 H  HB2  . ARG   A 1 141 ? 12.754 -14.984 -3.650  1.00 20.52 ?  141 ARG   A HB2  1 
ATOM   2982 H  HB3  . ARG   A 1 141 ? 14.179 -14.803 -4.312  1.00 20.52 ?  141 ARG   A HB3  1 
ATOM   2983 H  HG2  . ARG   A 1 141 ? 13.427 -16.788 -5.055  1.00 23.78 ?  141 ARG   A HG2  1 
ATOM   2984 H  HG3  . ARG   A 1 141 ? 14.520 -17.151 -3.952  1.00 23.78 ?  141 ARG   A HG3  1 
ATOM   2985 H  HD2  . ARG   A 1 141 ? 11.990 -16.900 -2.934  1.00 26.11 ?  141 ARG   A HD2  1 
ATOM   2986 H  HD3  . ARG   A 1 141 ? 12.152 -18.118 -3.946  1.00 26.11 ?  141 ARG   A HD3  1 
ATOM   2987 H  HE   . ARG   A 1 141 ? 14.067 -18.486 -2.357  1.00 26.90 ?  141 ARG   A HE   1 
ATOM   2988 H  HH11 . ARG   A 1 141 ? 10.827 -18.165 -1.686  1.00 27.52 ?  141 ARG   A HH11 1 
ATOM   2989 H  HH12 . ARG   A 1 141 ? 10.840 -19.051 -0.490  1.00 27.52 ?  141 ARG   A HH12 1 
ATOM   2990 H  HH21 . ARG   A 1 141 ? 14.041 -19.807 -0.546  1.00 28.60 ?  141 ARG   A HH21 1 
ATOM   2991 H  HH22 . ARG   A 1 141 ? 12.772 -20.040 0.198   1.00 28.60 ?  141 ARG   A HH22 1 
ATOM   2992 N  N    . VAL   A 1 142 ? 16.573 -14.488 -2.914  1.00 13.48 ?  142 VAL   A N    1 
ATOM   2993 C  CA   . VAL   A 1 142 ? 18.019 -14.700 -2.944  1.00 13.25 ?  142 VAL   A CA   1 
ATOM   2994 C  C    . VAL   A 1 142 ? 18.584 -14.687 -1.531  1.00 12.53 ?  142 VAL   A C    1 
ATOM   2995 O  O    . VAL   A 1 142 ? 19.443 -15.504 -1.182  1.00 12.75 ?  142 VAL   A O    1 
ATOM   2996 C  CB   . VAL   A 1 142 ? 18.711 -13.673 -3.860  1.00 13.40 ?  142 VAL   A CB   1 
ATOM   2997 C  CG1  . VAL   A 1 142 ? 20.219 -13.873 -3.826  1.00 13.20 ?  142 VAL   A CG1  1 
ATOM   2998 C  CG2  . VAL   A 1 142 ? 18.204 -13.809 -5.286  1.00 14.65 ?  142 VAL   A CG2  1 
ATOM   2999 H  H    . VAL   A 1 142 ? 16.305 -13.771 -3.319  1.00 16.34 ?  142 VAL   A H    1 
ATOM   3000 H  HA   . VAL   A 1 142 ? 18.189 -15.571 -3.323  1.00 16.07 ?  142 VAL   A HA   1 
ATOM   3001 H  HB   . VAL   A 1 142 ? 18.516 -12.769 -3.549  1.00 16.25 ?  142 VAL   A HB   1 
ATOM   3002 H  HG11 . VAL   A 1 142 ? 20.620 -13.375 -4.555  1.00 16.01 ?  142 VAL   A HG11 1 
ATOM   3003 H  HG12 . VAL   A 1 142 ? 20.564 -13.548 -2.978  1.00 16.01 ?  142 VAL   A HG12 1 
ATOM   3004 H  HG13 . VAL   A 1 142 ? 20.410 -14.817 -3.923  1.00 16.01 ?  142 VAL   A HG13 1 
ATOM   3005 H  HG21 . VAL   A 1 142 ? 18.660 -13.159 -5.845  1.00 17.74 ?  142 VAL   A HG21 1 
ATOM   3006 H  HG22 . VAL   A 1 142 ? 18.398 -14.706 -5.598  1.00 17.74 ?  142 VAL   A HG22 1 
ATOM   3007 H  HG23 . VAL   A 1 142 ? 17.252 -13.648 -5.298  1.00 17.74 ?  142 VAL   A HG23 1 
ATOM   3008 N  N    . CYS   A 1 143 ? 18.118 -13.757 -0.698  1.00 12.51 ?  143 CYS   A N    1 
ATOM   3009 C  CA   . CYS   A 1 143 ? 18.574 -13.710 0.686   1.00 12.50 ?  143 CYS   A CA   1 
ATOM   3010 C  C    . CYS   A 1 143 ? 18.348 -15.051 1.375   1.00 12.42 ?  143 CYS   A C    1 
ATOM   3011 O  O    . CYS   A 1 143 ? 19.268 -15.635 1.952   1.00 12.22 ?  143 CYS   A O    1 
ATOM   3012 C  CB   . CYS   A 1 143 ? 17.828 -12.602 1.426   1.00 12.73 ?  143 CYS   A CB   1 
ATOM   3013 S  SG   . CYS   A 1 143 ? 18.322 -12.418 3.150   1.00 13.51 ?  143 CYS   A SG   1 
ATOM   3014 H  H    . CYS   A 1 143 ? 17.552 -13.152 -0.910  1.00 15.18 ?  143 CYS   A H    1 
ATOM   3015 H  HA   . CYS   A 1 143 ? 19.522 -13.517 0.709   1.00 15.17 ?  143 CYS   A HA   1 
ATOM   3016 H  HB2  . CYS   A 1 143 ? 17.994 -11.760 0.974   1.00 15.44 ?  143 CYS   A HB2  1 
ATOM   3017 H  HB3  . CYS   A 1 143 ? 16.883 -12.800 1.409   1.00 15.44 ?  143 CYS   A HB3  1 
ATOM   3018 H  HG   . CYS   A 1 143 ? 17.724 -11.490 3.619   1.00 16.38 ?  143 CYS   A HG   1 
ATOM   3019 N  N    . VAL   A 1 144 ? 17.120 -15.560 1.316   1.00 13.15 ?  144 VAL   A N    1 
ATOM   3020 C  CA   . VAL   A 1 144 ? 16.784 -16.793 2.019   1.00 14.26 ?  144 VAL   A CA   1 
ATOM   3021 C  C    . VAL   A 1 144 ? 17.604 -17.959 1.491   1.00 13.94 ?  144 VAL   A C    1 
ATOM   3022 O  O    . VAL   A 1 144 ? 17.970 -18.871 2.246   1.00 14.33 ?  144 VAL   A O    1 
ATOM   3023 C  CB   . VAL   A 1 144 ? 15.268 -17.038 1.895   1.00 17.16 ?  144 VAL   A CB   1 
ATOM   3024 C  CG1  . VAL   A 1 144 ? 14.910 -18.469 2.232   1.00 18.83 ?  144 VAL   A CG1  1 
ATOM   3025 C  CG2  . VAL   A 1 144 ? 14.517 -16.033 2.770   1.00 17.27 ?  144 VAL   A CG2  1 
ATOM   3026 H  H    . VAL   A 1 144 ? 16.466 -15.214 0.872   1.00 15.95 ?  144 VAL   A H    1 
ATOM   3027 H  HA   . VAL   A 1 144 ? 16.986 -16.681 2.957   1.00 17.27 ?  144 VAL   A HA   1 
ATOM   3028 H  HB   . VAL   A 1 144 ? 14.998 -16.875 0.975   1.00 20.76 ?  144 VAL   A HB   1 
ATOM   3029 H  HG11 . VAL   A 1 144 ? 13.957 -18.518 2.417   1.00 22.76 ?  144 VAL   A HG11 1 
ATOM   3030 H  HG12 . VAL   A 1 144 ? 15.128 -19.035 1.478   1.00 22.76 ?  144 VAL   A HG12 1 
ATOM   3031 H  HG13 . VAL   A 1 144 ? 15.411 -18.740 3.014   1.00 22.76 ?  144 VAL   A HG13 1 
ATOM   3032 H  HG21 . VAL   A 1 144 ? 13.559 -16.175 2.672   1.00 20.89 ?  144 VAL   A HG21 1 
ATOM   3033 H  HG22 . VAL   A 1 144 ? 14.774 -16.161 3.696   1.00 20.89 ?  144 VAL   A HG22 1 
ATOM   3034 H  HG23 . VAL   A 1 144 ? 14.742 -15.130 2.488   1.00 20.89 ?  144 VAL   A HG23 1 
ATOM   3035 N  N    . ASP   A 1 145 ? 17.871 -17.974 0.190   1.00 14.22 ?  145 ASP   A N    1 
ATOM   3036 C  CA   . ASP   A 1 145 ? 18.583 -19.081 -0.441  1.00 14.82 ?  145 ASP   A CA   1 
ATOM   3037 C  C    . ASP   A 1 145 ? 20.102 -18.934 -0.393  1.00 14.49 ?  145 ASP   A C    1 
ATOM   3038 O  O    . ASP   A 1 145 ? 20.809 -19.833 -0.863  1.00 16.52 ?  145 ASP   A O    1 
ATOM   3039 C  CB   . ASP   A 1 145 ? 18.140 -19.232 -1.899  1.00 16.55 ?  145 ASP   A CB   1 
ATOM   3040 C  CG   . ASP   A 1 145 ? 16.687 -19.666 -2.034  1.00 18.79 ?  145 ASP   A CG   1 
ATOM   3041 O  OD1  . ASP   A 1 145 ? 16.109 -20.195 -1.060  1.00 19.02 ?  145 ASP   A OD1  1 
ATOM   3042 O  OD2  . ASP   A 1 145 ? 16.125 -19.468 -3.127  1.00 20.42 -1 145 ASP   A OD2  1 
ATOM   3043 H  H    . ASP   A 1 145 ? 17.634 -17.354 -0.359  1.00 17.22 ?  145 ASP   A H    1 
ATOM   3044 H  HA   . ASP   A 1 145 ? 18.347 -19.902 0.021   1.00 17.95 ?  145 ASP   A HA   1 
ATOM   3045 H  HB2  . ASP   A 1 145 ? 18.253 -18.380 -2.352  1.00 20.02 ?  145 ASP   A HB2  1 
ATOM   3046 H  HB3  . ASP   A 1 145 ? 18.689 -19.909 -2.325  1.00 20.02 ?  145 ASP   A HB3  1 
ATOM   3047 N  N    . THR   A 1 146 ? 20.623 -17.837 0.150   1.00 12.80 ?  146 THR   A N    1 
ATOM   3048 C  CA   . THR   A 1 146 ? 22.063 -17.587 0.171   1.00 12.05 ?  146 THR   A CA   1 
ATOM   3049 C  C    . THR   A 1 146 ? 22.617 -17.403 1.569   1.00 12.08 ?  146 THR   A C    1 
ATOM   3050 O  O    . THR   A 1 146 ? 23.699 -17.924 1.878   1.00 13.22 ?  146 THR   A O    1 
ATOM   3051 C  CB   . THR   A 1 146 ? 22.385 -16.335 -0.670  1.00 12.26 ?  146 THR   A CB   1 
ATOM   3052 O  OG1  . THR   A 1 146 ? 21.856 -16.499 -1.988  1.00 13.04 ?  146 THR   A OG1  1 
ATOM   3053 C  CG2  . THR   A 1 146 ? 23.888 -16.104 -0.762  1.00 12.62 ?  146 THR   A CG2  1 
ATOM   3054 H  H    . THR   A 1 146 ? 20.155 -17.206 0.509   1.00 15.52 ?  146 THR   A H    1 
ATOM   3055 H  HA   . THR   A 1 146 ? 22.520 -18.337 -0.232  1.00 14.62 ?  146 THR   A HA   1 
ATOM   3056 H  HB   . THR   A 1 146 ? 21.988 -15.553 -0.258  1.00 14.88 ?  146 THR   A HB   1 
ATOM   3057 H  HG1  . THR   A 1 146 ? 21.019 -16.570 -1.953  1.00 15.81 ?  146 THR   A HG1  1 
ATOM   3058 H  HG21 . THR   A 1 146 ? 24.079 -15.436 -1.437  1.00 15.31 ?  146 THR   A HG21 1 
ATOM   3059 H  HG22 . THR   A 1 146 ? 24.230 -15.799 0.092   1.00 15.31 ?  146 THR   A HG22 1 
ATOM   3060 H  HG23 . THR   A 1 146 ? 24.333 -16.932 -1.004  1.00 15.31 ?  146 THR   A HG23 1 
ATOM   3061 N  N    . VAL   A 1 147 ? 21.933 -16.624 2.402   1.00 11.90 ?  147 VAL   A N    1 
ATOM   3062 C  CA   . VAL   A 1 147 ? 22.419 -16.323 3.741   1.00 12.20 ?  147 VAL   A CA   1 
ATOM   3063 C  C    . VAL   A 1 147 ? 22.101 -17.493 4.660   1.00 12.69 ?  147 VAL   A C    1 
ATOM   3064 O  O    . VAL   A 1 147 ? 20.960 -17.974 4.706   1.00 13.23 ?  147 VAL   A O    1 
ATOM   3065 C  CB   . VAL   A 1 147 ? 21.799 -15.018 4.262   1.00 12.30 ?  147 VAL   A CB   1 
ATOM   3066 C  CG1  . VAL   A 1 147 ? 22.350 -14.701 5.633   1.00 13.46 ?  147 VAL   A CG1  1 
ATOM   3067 C  CG2  . VAL   A 1 147 ? 22.050 -13.873 3.291   1.00 12.45 ?  147 VAL   A CG2  1 
ATOM   3068 H  H    . VAL   A 1 147 ? 21.175 -16.258 2.215   1.00 14.44 ?  147 VAL   A H    1 
ATOM   3069 H  HA   . VAL   A 1 147 ? 23.380 -16.214 3.712   1.00 14.81 ?  147 VAL   A HA   1 
ATOM   3070 H  HB   . VAL   A 1 147 ? 20.841 -15.138 4.348   1.00 14.92 ?  147 VAL   A HB   1 
ATOM   3071 H  HG11 . VAL   A 1 147 ? 22.101 -13.799 5.871   1.00 16.32 ?  147 VAL   A HG11 1 
ATOM   3072 H  HG12 . VAL   A 1 147 ? 21.978 -15.329 6.276   1.00 16.32 ?  147 VAL   A HG12 1 
ATOM   3073 H  HG13 . VAL   A 1 147 ? 23.316 -14.787 5.611   1.00 16.32 ?  147 VAL   A HG13 1 
ATOM   3074 H  HG21 . VAL   A 1 147 ? 21.719 -13.050 3.686   1.00 15.11 ?  147 VAL   A HG21 1 
ATOM   3075 H  HG22 . VAL   A 1 147 ? 22.998 -13.804 3.122   1.00 15.11 ?  147 VAL   A HG22 1 
ATOM   3076 H  HG23 . VAL   A 1 147 ? 21.574 -14.054 2.464   1.00 15.11 ?  147 VAL   A HG23 1 
ATOM   3077 N  N    . ARG   A 1 148 ? 23.124 -17.961 5.379   1.00 12.65 ?  148 ARG   A N    1 
ATOM   3078 C  CA   . ARG   A 1 148 ? 23.000 -19.040 6.347   1.00 12.81 ?  148 ARG   A CA   1 
ATOM   3079 C  C    . ARG   A 1 148 ? 23.123 -18.564 7.783   1.00 13.12 ?  148 ARG   A C    1 
ATOM   3080 O  O    . ARG   A 1 148 ? 22.716 -19.290 8.700   1.00 14.89 ?  148 ARG   A O    1 
ATOM   3081 C  CB   . ARG   A 1 148 ? 24.044 -20.134 6.070   1.00 13.27 ?  148 ARG   A CB   1 
ATOM   3082 C  CG   . ARG   A 1 148 ? 23.885 -20.771 4.700   1.00 14.73 ?  148 ARG   A CG   1 
ATOM   3083 C  CD   . ARG   A 1 148 ? 24.964 -21.806 4.407   1.00 15.68 ?  148 ARG   A CD   1 
ATOM   3084 N  NE   . ARG   A 1 148 ? 26.303 -21.226 4.429   1.00 15.83 ?  148 ARG   A NE   1 
ATOM   3085 C  CZ   . ARG   A 1 148 ? 26.812 -20.487 3.454   1.00 14.99 ?  148 ARG   A CZ   1 
ATOM   3086 N  NH1  . ARG   A 1 148 ? 26.136 -20.249 2.343   1.00 15.25 ?  148 ARG   A NH1  1 
ATOM   3087 N  NH2  . ARG   A 1 148 ? 28.029 -19.964 3.600   1.00 15.28 ?  148 ARG   A NH2  1 
ATOM   3088 H  H    . ARG   A 1 148 ? 23.929 -17.656 5.307   1.00 15.34 ?  148 ARG   A H    1 
ATOM   3089 H  HA   . ARG   A 1 148 ? 22.129 -19.442 6.248   1.00 15.53 ?  148 ARG   A HA   1 
ATOM   3090 H  HB2  . ARG   A 1 148 ? 24.933 -19.757 6.122   1.00 16.08 ?  148 ARG   A HB2  1 
ATOM   3091 H  HB3  . ARG   A 1 148 ? 23.945 -20.841 6.733   1.00 16.08 ?  148 ARG   A HB3  1 
ATOM   3092 H  HG2  . ARG   A 1 148 ? 23.020 -21.204 4.655   1.00 17.84 ?  148 ARG   A HG2  1 
ATOM   3093 H  HG3  . ARG   A 1 148 ? 23.943 -20.072 4.028   1.00 17.84 ?  148 ARG   A HG3  1 
ATOM   3094 H  HD2  . ARG   A 1 148 ? 24.924 -22.504 5.080   1.00 18.98 ?  148 ARG   A HD2  1 
ATOM   3095 H  HD3  . ARG   A 1 148 ? 24.806 -22.186 3.526   1.00 18.98 ?  148 ARG   A HD3  1 
ATOM   3096 H  HE   . ARG   A 1 148 ? 26.792 -21.378 5.114   1.00 19.16 ?  148 ARG   A HE   1 
ATOM   3097 H  HH11 . ARG   A 1 148 ? 25.349 -20.572 2.237   1.00 18.46 ?  148 ARG   A HH11 1 
ATOM   3098 H  HH12 . ARG   A 1 148 ? 26.486 -19.758 1.726   1.00 18.46 ?  148 ARG   A HH12 1 
ATOM   3099 H  HH21 . ARG   A 1 148 ? 28.472 -20.110 4.318   1.00 18.50 ?  148 ARG   A HH21 1 
ATOM   3100 H  HH22 . ARG   A 1 148 ? 28.365 -19.478 2.974   1.00 18.50 ?  148 ARG   A HH22 1 
ATOM   3101 N  N    . THR   A 1 149 ? 23.668 -17.370 7.993   1.00 13.05 ?  149 THR   A N    1 
ATOM   3102 C  CA   . THR   A 1 149 ? 23.746 -16.769 9.309   1.00 13.28 ?  149 THR   A CA   1 
ATOM   3103 C  C    . THR   A 1 149 ? 22.421 -16.073 9.614   1.00 12.83 ?  149 THR   A C    1 
ATOM   3104 O  O    . THR   A 1 149 ? 21.489 -16.071 8.802   1.00 13.42 ?  149 THR   A O    1 
ATOM   3105 C  CB   . THR   A 1 149 ? 24.947 -15.835 9.367   1.00 13.67 ?  149 THR   A CB   1 
ATOM   3106 O  OG1  . THR   A 1 149 ? 24.820 -14.902 8.293   1.00 13.86 ?  149 THR   A OG1  1 
ATOM   3107 C  CG2  . THR   A 1 149 ? 26.256 -16.635 9.240   1.00 14.26 ?  149 THR   A CG2  1 
ATOM   3108 H  H    . THR   A 1 149 ? 24.009 -16.875 7.368   1.00 15.82 ?  149 THR   A H    1 
ATOM   3109 H  HA   . THR   A 1 149 ? 23.874 -17.469 9.964   1.00 16.11 ?  149 THR   A HA   1 
ATOM   3110 H  HB   . THR   A 1 149 ? 24.947 -15.363 10.210  1.00 16.57 ?  149 THR   A HB   1 
ATOM   3111 H  HG1  . THR   A 1 149 ? 25.471 -14.370 8.292   1.00 16.79 ?  149 THR   A HG1  1 
ATOM   3112 H  HG21 . THR   A 1 149 ? 27.019 -16.038 9.297   1.00 17.27 ?  149 THR   A HG21 1 
ATOM   3113 H  HG22 . THR   A 1 149 ? 26.318 -17.291 9.954   1.00 17.27 ?  149 THR   A HG22 1 
ATOM   3114 H  HG23 . THR   A 1 149 ? 26.286 -17.100 8.387   1.00 17.27 ?  149 THR   A HG23 1 
ATOM   3115 N  N    . ASN   A 1 150 ? 22.300 -15.533 10.818  1.00 13.17 ?  150 ASN   A N    1 
ATOM   3116 C  CA   . ASN   A 1 150 ? 21.017 -15.019 11.300  1.00 13.82 ?  150 ASN   A CA   1 
ATOM   3117 C  C    . ASN   A 1 150 ? 20.837 -13.579 10.839  1.00 12.98 ?  150 ASN   A C    1 
ATOM   3118 O  O    . ASN   A 1 150 ? 21.587 -12.685 11.253  1.00 14.37 ?  150 ASN   A O    1 
ATOM   3119 C  CB   . ASN   A 1 150 ? 20.950 -15.134 12.817  1.00 16.36 ?  150 ASN   A CB   1 
ATOM   3120 C  CG   . ASN   A 1 150 ? 20.838 -16.565 13.273  1.00 19.93 ?  150 ASN   A CG   1 
ATOM   3121 O  OD1  . ASN   A 1 150 ? 20.233 -17.391 12.593  1.00 21.41 ?  150 ASN   A OD1  1 
ATOM   3122 N  ND2  . ASN   A 1 150 ? 21.434 -16.877 14.416  1.00 22.25 ?  150 ASN   A ND2  1 
ATOM   3123 H  H    . ASN   A 1 150 ? 22.945 -15.453 11.379  1.00 15.97 ?  150 ASN   A H    1 
ATOM   3124 H  HA   . ASN   A 1 150 ? 20.298 -15.554 10.925  1.00 16.75 ?  150 ASN   A HA   1 
ATOM   3125 H  HB2  . ASN   A 1 150 ? 21.757 -14.760 13.201  1.00 19.80 ?  150 ASN   A HB2  1 
ATOM   3126 H  HB3  . ASN   A 1 150 ? 20.171 -14.654 13.139  1.00 19.80 ?  150 ASN   A HB3  1 
ATOM   3127 H  HD21 . ASN   A 1 150 ? 21.399 -17.685 14.719  1.00 26.87 ?  150 ASN   A HD21 1 
ATOM   3128 H  HD22 . ASN   A 1 150 ? 21.852 -16.274 14.864  1.00 26.87 ?  150 ASN   A HD22 1 
ATOM   3129 N  N    . VAL   A 1 151 ? 19.848 -13.350 9.981   1.00 12.45 ?  151 VAL   A N    1 
ATOM   3130 C  CA   . VAL   A 1 151 ? 19.633 -12.044 9.378   1.00 12.66 ?  151 VAL   A CA   1 
ATOM   3131 C  C    . VAL   A 1 151 ? 18.246 -11.526 9.739   1.00 12.65 ?  151 VAL   A C    1 
ATOM   3132 O  O    . VAL   A 1 151 ? 17.237 -12.236 9.602   1.00 14.06 ?  151 VAL   A O    1 
ATOM   3133 C  CB   . VAL   A 1 151 ? 19.921 -12.041 7.862   1.00 13.88 ?  151 VAL   A CB   1 
ATOM   3134 C  CG1  . VAL   A 1 151 ? 19.093 -13.064 7.118   1.00 14.98 ?  151 VAL   A CG1  1 
ATOM   3135 C  CG2  . VAL   A 1 151 ? 19.728 -10.636 7.280   1.00 13.88 ?  151 VAL   A CG2  1 
ATOM   3136 H  H    . VAL   A 1 151 ? 19.290 -13.950 9.720   1.00 15.11 ?  151 VAL   A H    1 
ATOM   3137 H  HA   . VAL   A 1 151 ? 20.273 -11.428 9.768   1.00 15.35 ?  151 VAL   A HA   1 
ATOM   3138 H  HB   . VAL   A 1 151 ? 20.854 -12.280 7.723   1.00 16.82 ?  151 VAL   A HB   1 
ATOM   3139 H  HG11 . VAL   A 1 151 ? 19.278 -13.000 6.167   1.00 18.15 ?  151 VAL   A HG11 1 
ATOM   3140 H  HG12 . VAL   A 1 151 ? 19.328 -13.954 7.436   1.00 18.15 ?  151 VAL   A HG12 1 
ATOM   3141 H  HG13 . VAL   A 1 151 ? 18.152 -12.895 7.283   1.00 18.15 ?  151 VAL   A HG13 1 
ATOM   3142 H  HG21 . VAL   A 1 151 ? 20.047 -10.625 6.361   1.00 16.82 ?  151 VAL   A HG21 1 
ATOM   3143 H  HG22 . VAL   A 1 151 ? 18.784 -10.410 7.300   1.00 16.82 ?  151 VAL   A HG22 1 
ATOM   3144 H  HG23 . VAL   A 1 151 ? 20.233 -10.002 7.810   1.00 16.82 ?  151 VAL   A HG23 1 
ATOM   3145 N  N    . TYR   A 1 152 ? 18.231 -10.285 10.227  1.00 12.38 ?  152 TYR   A N    1 
ATOM   3146 C  CA   . TYR   A 1 152 ? 17.037 -9.550  10.613  1.00 12.30 ?  152 TYR   A CA   1 
ATOM   3147 C  C    . TYR   A 1 152 ? 16.838 -8.449  9.586   1.00 12.06 ?  152 TYR   A C    1 
ATOM   3148 O  O    . TYR   A 1 152 ? 17.610 -7.483  9.538   1.00 12.48 ?  152 TYR   A O    1 
ATOM   3149 C  CB   . TYR   A 1 152 ? 17.222 -9.007  12.026  1.00 13.21 ?  152 TYR   A CB   1 
ATOM   3150 C  CG   . TYR   A 1 152 ? 17.182 -10.136 13.024  1.00 13.78 ?  152 TYR   A CG   1 
ATOM   3151 C  CD1  . TYR   A 1 152 ? 18.309 -10.903 13.289  1.00 15.20 ?  152 TYR   A CD1  1 
ATOM   3152 C  CD2  . TYR   A 1 152 ? 15.998 -10.485 13.657  1.00 14.04 ?  152 TYR   A CD2  1 
ATOM   3153 C  CE1  . TYR   A 1 152 ? 18.269 -11.965 14.172  1.00 16.61 ?  152 TYR   A CE1  1 
ATOM   3154 C  CE2  . TYR   A 1 152 ? 15.946 -11.553 14.548  1.00 15.46 ?  152 TYR   A CE2  1 
ATOM   3155 C  CZ   . TYR   A 1 152 ? 17.086 -12.286 14.800  1.00 16.37 ?  152 TYR   A CZ   1 
ATOM   3156 O  OH   . TYR   A 1 152 ? 17.049 -13.353 15.678  1.00 19.03 ?  152 TYR   A OH   1 
ATOM   3157 H  H    . TYR   A 1 152 ? 18.952 -9.818  10.327  1.00 15.02 ?  152 TYR   A H    1 
ATOM   3158 H  HA   . TYR   A 1 152 ? 16.272 -10.142 10.597  1.00 14.93 ?  152 TYR   A HA   1 
ATOM   3159 H  HB2  . TYR   A 1 152 ? 18.083 -8.573  12.095  1.00 16.02 ?  152 TYR   A HB2  1 
ATOM   3160 H  HB3  . TYR   A 1 152 ? 16.508 -8.388  12.230  1.00 16.02 ?  152 TYR   A HB3  1 
ATOM   3161 H  HD1  . TYR   A 1 152 ? 19.108 -10.692 12.863  1.00 18.40 ?  152 TYR   A HD1  1 
ATOM   3162 H  HD2  . TYR   A 1 152 ? 15.220 -9.995  13.485  1.00 17.01 ?  152 TYR   A HD2  1 
ATOM   3163 H  HE1  . TYR   A 1 152 ? 19.036 -12.457 14.344  1.00 20.10 ?  152 TYR   A HE1  1 
ATOM   3164 H  HE2  . TYR   A 1 152 ? 15.146 -11.769 14.974  1.00 18.71 ?  152 TYR   A HE2  1 
ATOM   3165 H  HH   . TYR   A 1 152 ? 17.726 -13.833 15.570  1.00 23.00 ?  152 TYR   A HH   1 
ATOM   3166 N  N    . LEU   A 1 153 ? 15.830 -8.621  8.739   1.00 12.21 ?  153 LEU   A N    1 
ATOM   3167 C  CA   . LEU   A 1 153 ? 15.567 -7.712  7.634   1.00 12.54 ?  153 LEU   A CA   1 
ATOM   3168 C  C    . LEU   A 1 153 ? 14.568 -6.640  8.042   1.00 12.71 ?  153 LEU   A C    1 
ATOM   3169 O  O    . LEU   A 1 153 ? 13.471 -6.948  8.525   1.00 14.09 ?  153 LEU   A O    1 
ATOM   3170 C  CB   . LEU   A 1 153 ? 15.000 -8.477  6.440   1.00 12.65 ?  153 LEU   A CB   1 
ATOM   3171 C  CG   . LEU   A 1 153 ? 15.933 -9.498  5.792   1.00 12.92 ?  153 LEU   A CG   1 
ATOM   3172 C  CD1  . LEU   A 1 153 ? 15.141 -10.370 4.830   1.00 13.41 ?  153 LEU   A CD1  1 
ATOM   3173 C  CD2  . LEU   A 1 153 ? 17.068 -8.793  5.066   1.00 13.30 ?  153 LEU   A CD2  1 
ATOM   3174 H  H    . LEU   A 1 153 ? 15.264 -9.273  8.787   1.00 14.82 ?  153 LEU   A H    1 
ATOM   3175 H  HA   . LEU   A 1 153 ? 16.392 -7.286  7.373   1.00 15.21 ?  153 LEU   A HA   1 
ATOM   3176 H  HB2  . LEU   A 1 153 ? 14.206 -8.947  6.731   1.00 15.35 ?  153 LEU   A HB2  1 
ATOM   3177 H  HB3  . LEU   A 1 153 ? 14.759 -7.828  5.757   1.00 15.35 ?  153 LEU   A HB3  1 
ATOM   3178 H  HG   . LEU   A 1 153 ? 16.322 -10.065 6.485   1.00 15.66 ?  153 LEU   A HG   1 
ATOM   3179 H  HD11 . LEU   A 1 153 ? 15.716 -11.073 4.495   1.00 16.26 ?  153 LEU   A HD11 1 
ATOM   3180 H  HD12 . LEU   A 1 153 ? 14.387 -10.751 5.302   1.00 16.26 ?  153 LEU   A HD12 1 
ATOM   3181 H  HD13 . LEU   A 1 153 ? 14.829 -9.817  4.096   1.00 16.26 ?  153 LEU   A HD13 1 
ATOM   3182 H  HD21 . LEU   A 1 153 ? 17.630 -9.465  4.647   1.00 16.12 ?  153 LEU   A HD21 1 
ATOM   3183 H  HD22 . LEU   A 1 153 ? 16.689 -8.210  4.395   1.00 16.12 ?  153 LEU   A HD22 1 
ATOM   3184 H  HD23 . LEU   A 1 153 ? 17.584 -8.282  5.705   1.00 16.12 ?  153 LEU   A HD23 1 
ATOM   3185 N  N    A ALA   A 1 154 ? 14.985 -5.386  7.901   0.60 12.75 ?  154 ALA   A N    1 
ATOM   3186 N  N    B ALA   A 1 154 ? 14.900 -5.382  7.761   0.40 12.56 ?  154 ALA   A N    1 
ATOM   3187 C  CA   A ALA   A 1 154 ? 14.144 -4.228  8.150   0.60 13.55 ?  154 ALA   A CA   1 
ATOM   3188 C  CA   B ALA   A 1 154 ? 14.000 -4.253  7.992   0.40 12.95 ?  154 ALA   A CA   1 
ATOM   3189 C  C    A ALA   A 1 154 ? 13.636 -3.719  6.814   0.60 13.27 ?  154 ALA   A C    1 
ATOM   3190 C  C    B ALA   A 1 154 ? 13.547 -3.705  6.639   0.40 12.77 ?  154 ALA   A C    1 
ATOM   3191 O  O    A ALA   A 1 154 ? 14.431 -3.441  5.908   0.60 13.41 ?  154 ALA   A O    1 
ATOM   3192 O  O    B ALA   A 1 154 ? 14.363 -3.181  5.871   0.40 13.68 ?  154 ALA   A O    1 
ATOM   3193 C  CB   A ALA   A 1 154 ? 14.936 -3.123  8.847   0.60 14.20 ?  154 ALA   A CB   1 
ATOM   3194 C  CB   B ALA   A 1 154 ? 14.703 -3.175  8.814   0.40 13.61 ?  154 ALA   A CB   1 
ATOM   3195 H  H    A ALA   A 1 154 ? 15.781 -5.175  7.646   0.60 15.46 ?  154 ALA   A H    1 
ATOM   3196 H  H    B ALA   A 1 154 ? 15.656 -5.154  7.427   0.40 15.23 ?  154 ALA   A H    1 
ATOM   3197 H  HA   A ALA   A 1 154 ? 13.386 -4.474  8.701   0.60 16.43 ?  154 ALA   A HA   1 
ATOM   3198 H  HA   B ALA   A 1 154 ? 13.218 -4.557  8.489   0.40 15.71 ?  154 ALA   A HA   1 
ATOM   3199 H  HB1  A ALA   A 1 154 ? 14.350 -2.363  8.997   0.60 17.21 ?  154 ALA   A HB1  1 
ATOM   3200 H  HB1  B ALA   A 1 154 ? 14.090 -2.438  8.959   0.40 16.50 ?  154 ALA   A HB1  1 
ATOM   3201 H  HB2  A ALA   A 1 154 ? 15.265 -3.461  9.692   0.60 17.21 ?  154 ALA   A HB2  1 
ATOM   3202 H  HB2  B ALA   A 1 154 ? 14.977 -3.550  9.668   0.40 16.50 ?  154 ALA   A HB2  1 
ATOM   3203 H  HB3  A ALA   A 1 154 ? 15.677 -2.862  8.279   0.60 17.21 ?  154 ALA   A HB3  1 
ATOM   3204 H  HB3  B ALA   A 1 154 ? 15.483 -2.867  8.326   0.40 16.50 ?  154 ALA   A HB3  1 
ATOM   3205 N  N    A VAL   A 1 155 ? 12.317 -3.607  6.697   0.60 13.77 ?  155 VAL   A N    1 
ATOM   3206 N  N    B VAL   A 1 155 ? 12.246 -3.818  6.360   0.40 12.75 ?  155 VAL   A N    1 
ATOM   3207 C  CA   A VAL   A 1 155 ? 11.659 -3.111  5.499   0.60 14.36 ?  155 VAL   A CA   1 
ATOM   3208 C  CA   B VAL   A 1 155 ? 11.646 -3.395  5.094   0.40 12.90 ?  155 VAL   A CA   1 
ATOM   3209 C  C    A VAL   A 1 155 ? 10.937 -1.830  5.880   0.60 15.31 ?  155 VAL   A C    1 
ATOM   3210 C  C    B VAL   A 1 155 ? 10.888 -2.089  5.322   0.40 13.02 ?  155 VAL   A C    1 
ATOM   3211 O  O    A VAL   A 1 155 ? 10.010 -1.853  6.700   0.60 15.95 ?  155 VAL   A O    1 
ATOM   3212 O  O    B VAL   A 1 155 ? 9.913  -2.053  6.082   0.40 13.22 ?  155 VAL   A O    1 
ATOM   3213 C  CB   A VAL   A 1 155 ? 10.702 -4.152  4.899   0.60 14.29 ?  155 VAL   A CB   1 
ATOM   3214 C  CB   B VAL   A 1 155 ? 10.719 -4.485  4.527   0.40 12.68 ?  155 VAL   A CB   1 
ATOM   3215 C  CG1  A VAL   A 1 155 ? 9.957  -3.565  3.716   0.60 14.74 ?  155 VAL   A CG1  1 
ATOM   3216 C  CG1  B VAL   A 1 155 ? 10.060 -4.017  3.237   0.40 12.79 ?  155 VAL   A CG1  1 
ATOM   3217 C  CG2  A VAL   A 1 155 ? 11.487 -5.393  4.477   0.60 14.74 ?  155 VAL   A CG2  1 
ATOM   3218 C  CG2  B VAL   A 1 155 ? 11.495 -5.779  4.286   0.40 13.33 ?  155 VAL   A CG2  1 
ATOM   3219 H  H    A VAL   A 1 155 ? 11.765 -3.817  7.323   0.60 16.69 ?  155 VAL   A H    1 
ATOM   3220 H  H    B VAL   A 1 155 ? 11.676 -4.159  6.907   0.40 15.47 ?  155 VAL   A H    1 
ATOM   3221 H  HA   A VAL   A 1 155 ? 12.323 -2.891  4.830   0.60 17.40 ?  155 VAL   A HA   1 
ATOM   3222 H  HA   B VAL   A 1 155 ? 12.347 -3.238  4.445   0.40 15.65 ?  155 VAL   A HA   1 
ATOM   3223 H  HB   A VAL   A 1 155 ? 10.050 -4.416  5.570   0.60 17.32 ?  155 VAL   A HB   1 
ATOM   3224 H  HB   B VAL   A 1 155 ? 10.018 -4.680  5.170   0.40 15.38 ?  155 VAL   A HB   1 
ATOM   3225 H  HG11 A VAL   A 1 155 ? 9.518  -4.283  3.234   0.60 17.85 ?  155 VAL   A HG11 1 
ATOM   3226 H  HG11 B VAL   A 1 155 ? 9.614  -4.771  2.816   0.40 15.52 ?  155 VAL   A HG11 1 
ATOM   3227 H  HG12 A VAL   A 1 155 ? 9.294  -2.933  4.039   0.60 17.85 ?  155 VAL   A HG12 1 
ATOM   3228 H  HG12 B VAL   A 1 155 ? 9.409  -3.330  3.446   0.40 15.52 ?  155 VAL   A HG12 1 
ATOM   3229 H  HG13 A VAL   A 1 155 ? 10.591 -3.116  3.137   0.60 17.85 ?  155 VAL   A HG13 1 
ATOM   3230 H  HG13 B VAL   A 1 155 ? 10.740 -3.667  2.645   0.40 15.52 ?  155 VAL   A HG13 1 
ATOM   3231 H  HG21 A VAL   A 1 155 ? 10.879 -6.033  4.074   0.60 17.86 ?  155 VAL   A HG21 1 
ATOM   3232 H  HG21 B VAL   A 1 155 ? 10.934 -6.399  3.793   0.40 16.17 ?  155 VAL   A HG21 1 
ATOM   3233 H  HG22 A VAL   A 1 155 ? 12.167 -5.134  3.833   0.60 17.86 ?  155 VAL   A HG22 1 
ATOM   3234 H  HG22 B VAL   A 1 155 ? 12.292 -5.576  3.773   0.40 16.17 ?  155 VAL   A HG22 1 
ATOM   3235 H  HG23 A VAL   A 1 155 ? 11.908 -5.785  5.259   0.60 17.86 ?  155 VAL   A HG23 1 
ATOM   3236 H  HG23 B VAL   A 1 155 ? 11.742 -6.164  5.142   0.40 16.17 ?  155 VAL   A HG23 1 
ATOM   3237 N  N    A PHE   A 1 156 ? 11.379 -0.711  5.300   0.60 15.49 ?  156 PHE   A N    1 
ATOM   3238 N  N    B PHE   A 1 156 ? 11.314 -1.028  4.625   0.40 13.75 ?  156 PHE   A N    1 
ATOM   3239 C  CA   A PHE   A 1 156 ? 10.845 0.594   5.677   0.60 16.99 ?  156 PHE   A CA   1 
ATOM   3240 C  CA   B PHE   A 1 156 ? 10.816 0.326   4.890   0.40 14.25 ?  156 PHE   A CA   1 
ATOM   3241 C  C    A PHE   A 1 156 ? 9.379  0.738   5.289   0.60 17.04 ?  156 PHE   A C    1 
ATOM   3242 C  C    B PHE   A 1 156 ? 9.355  0.497   4.476   0.40 14.77 ?  156 PHE   A C    1 
ATOM   3243 O  O    A PHE   A 1 156 ? 8.570  1.253   6.072   0.60 17.79 ?  156 PHE   A O    1 
ATOM   3244 O  O    B PHE   A 1 156 ? 8.601  1.226   5.135   0.40 15.90 ?  156 PHE   A O    1 
ATOM   3245 C  CB   A PHE   A 1 156 ? 11.682 1.693   5.017   0.60 18.75 ?  156 PHE   A CB   1 
ATOM   3246 C  CB   B PHE   A 1 156 ? 11.715 1.333   4.159   0.40 14.09 ?  156 PHE   A CB   1 
ATOM   3247 C  CG   A PHE   A 1 156 ? 11.186 3.081   5.293   0.60 20.74 ?  156 PHE   A CG   1 
ATOM   3248 C  CG   B PHE   A 1 156 ? 11.422 2.797   4.454   0.40 14.04 ?  156 PHE   A CG   1 
ATOM   3249 C  CD1  A PHE   A 1 156 ? 11.112 3.549   6.591   0.60 21.93 ?  156 PHE   A CD1  1 
ATOM   3250 C  CD1  B PHE   A 1 156 ? 12.018 3.442   5.535   0.40 14.66 ?  156 PHE   A CD1  1 
ATOM   3251 C  CD2  A PHE   A 1 156 ? 10.806 3.924   4.257   0.60 21.76 ?  156 PHE   A CD2  1 
ATOM   3252 C  CD2  B PHE   A 1 156 ? 10.608 3.540   3.613   0.40 14.55 ?  156 PHE   A CD2  1 
ATOM   3253 C  CE1  A PHE   A 1 156 ? 10.658 4.824   6.857   0.60 23.03 ?  156 PHE   A CE1  1 
ATOM   3254 C  CE1  B PHE   A 1 156 ? 11.771 4.791   5.794   0.40 15.20 ?  156 PHE   A CE1  1 
ATOM   3255 C  CE2  A PHE   A 1 156 ? 10.351 5.205   4.515   0.60 22.76 ?  156 PHE   A CE2  1 
ATOM   3256 C  CE2  B PHE   A 1 156 ? 10.360 4.886   3.864   0.40 15.23 ?  156 PHE   A CE2  1 
ATOM   3257 C  CZ   A PHE   A 1 156 ? 10.281 5.657   5.818   0.60 23.16 ?  156 PHE   A CZ   1 
ATOM   3258 C  CZ   B PHE   A 1 156 ? 10.947 5.513   4.957   0.40 15.32 ?  156 PHE   A CZ   1 
ATOM   3259 H  H    A PHE   A 1 156 ? 11.988 -0.682  4.688   0.60 18.75 ?  156 PHE   A H    1 
ATOM   3260 H  H    B PHE   A 1 156 ? 11.897 -1.075  3.995   0.40 16.67 ?  156 PHE   A H    1 
ATOM   3261 H  HA   A PHE   A 1 156 ? 10.920 0.706   6.634   0.60 20.56 ?  156 PHE   A HA   1 
ATOM   3262 H  HA   B PHE   A 1 156 ? 10.882 0.498   5.839   0.40 17.26 ?  156 PHE   A HA   1 
ATOM   3263 H  HB2  A PHE   A 1 156 ? 12.595 1.638   5.344   0.60 22.66 ?  156 PHE   A HB2  1 
ATOM   3264 H  HB2  B PHE   A 1 156 ? 12.629 1.164   4.427   0.40 17.07 ?  156 PHE   A HB2  1 
ATOM   3265 H  HB3  A PHE   A 1 156 ? 11.674 1.565   4.054   0.60 22.66 ?  156 PHE   A HB3  1 
ATOM   3266 H  HB3  B PHE   A 1 156 ? 11.625 1.197   3.202   0.40 17.07 ?  156 PHE   A HB3  1 
ATOM   3267 H  HD1  A PHE   A 1 156 ? 11.366 2.996   7.293   0.60 26.48 ?  156 PHE   A HD1  1 
ATOM   3268 H  HD1  B PHE   A 1 156 ? 12.572 2.959   6.106   0.40 17.75 ?  156 PHE   A HD1  1 
ATOM   3269 H  HD2  A PHE   A 1 156 ? 10.854 3.622   3.377   0.60 26.27 ?  156 PHE   A HD2  1 
ATOM   3270 H  HD2  B PHE   A 1 156 ? 10.211 3.131   2.880   0.40 17.62 ?  156 PHE   A HD2  1 
ATOM   3271 H  HE1  A PHE   A 1 156 ? 10.610 5.129   7.734   0.60 27.80 ?  156 PHE   A HE1  1 
ATOM   3272 H  HE1  B PHE   A 1 156 ? 12.166 5.200   6.531   0.40 18.40 ?  156 PHE   A HE1  1 
ATOM   3273 H  HE2  A PHE   A 1 156 ? 10.096 5.760   3.812   0.60 27.48 ?  156 PHE   A HE2  1 
ATOM   3274 H  HE2  B PHE   A 1 156 ? 9.802  5.371   3.300   0.40 18.44 ?  156 PHE   A HE2  1 
ATOM   3275 H  HZ   A PHE   A 1 156 ? 9.973  6.516   5.996   0.60 27.96 ?  156 PHE   A HZ   1 
ATOM   3276 H  HZ   B PHE   A 1 156 ? 10.779 6.412   5.131   0.40 18.55 ?  156 PHE   A HZ   1 
ATOM   3277 N  N    A ASP   A 1 157 ? 9.022  0.302   4.086   0.60 16.52 ?  157 ASP   A N    1 
ATOM   3278 N  N    B ASP   A 1 157 ? 8.935  -0.157  3.396   0.40 15.46 ?  157 ASP   A N    1 
ATOM   3279 C  CA   A ASP   A 1 157 ? 7.704  0.557   3.520   0.60 17.36 ?  157 ASP   A CA   1 
ATOM   3280 C  CA   B ASP   A 1 157 ? 7.629  0.084   2.790   0.40 15.98 ?  157 ASP   A CA   1 
ATOM   3281 C  C    A ASP   A 1 157 ? 6.714  -0.486  4.028   0.60 17.71 ?  157 ASP   A C    1 
ATOM   3282 C  C    B ASP   A 1 157 ? 6.618  -0.938  3.308   0.40 15.36 ?  157 ASP   A C    1 
ATOM   3283 O  O    A ASP   A 1 157 ? 6.899  -1.685  3.793   0.60 16.97 ?  157 ASP   A O    1 
ATOM   3284 O  O    B ASP   A 1 157 ? 6.815  -2.146  3.143   0.40 14.75 ?  157 ASP   A O    1 
ATOM   3285 C  CB   A ASP   A 1 157 ? 7.804  0.481   1.999   0.60 18.40 ?  157 ASP   A CB   1 
ATOM   3286 C  CB   B ASP   A 1 157 ? 7.747  0.001   1.269   0.40 16.88 ?  157 ASP   A CB   1 
ATOM   3287 C  CG   A ASP   A 1 157 ? 6.581  1.019   1.313   0.60 20.10 ?  157 ASP   A CG   1 
ATOM   3288 C  CG   B ASP   A 1 157 ? 6.523  0.525   0.556   0.40 17.85 ?  157 ASP   A CG   1 
ATOM   3289 O  OD1  A ASP   A 1 157 ? 6.503  2.249   1.132   0.60 21.87 ?  157 ASP   A OD1  1 
ATOM   3290 O  OD1  B ASP   A 1 157 ? 6.338  1.757   0.538   0.40 18.50 ?  157 ASP   A OD1  1 
ATOM   3291 O  OD2  A ASP   A 1 157 ? 5.692  0.217   0.961   0.60 20.06 -1 157 ASP   A OD2  1 
ATOM   3292 O  OD2  B ASP   A 1 157 ? 5.754  -0.291  0.004   0.40 17.97 -1 157 ASP   A OD2  1 
ATOM   3293 H  H    A ASP   A 1 157 ? 9.534  -0.150  3.569   0.60 19.99 ?  157 ASP   A H    1 
ATOM   3294 H  H    B ASP   A 1 157 ? 9.392  -0.767  2.989   0.40 18.72 ?  157 ASP   A H    1 
ATOM   3295 H  HA   A ASP   A 1 157 ? 7.392  1.443   3.769   0.60 20.99 ?  157 ASP   A HA   1 
ATOM   3296 H  HA   B ASP   A 1 157 ? 7.317  0.969   3.031   0.40 19.34 ?  157 ASP   A HA   1 
ATOM   3297 H  HB2  A ASP   A 1 157 ? 8.556  1.008   1.697   0.60 22.24 ?  157 ASP   A HB2  1 
ATOM   3298 H  HB2  B ASP   A 1 157 ? 8.518  0.517   0.990   0.40 20.42 ?  157 ASP   A HB2  1 
ATOM   3299 H  HB3  A ASP   A 1 157 ? 7.923  -0.446  1.735   0.60 22.24 ?  157 ASP   A HB3  1 
ATOM   3300 H  HB3  B ASP   A 1 157 ? 7.851  -0.920  1.005   0.40 20.42 ?  157 ASP   A HB3  1 
ATOM   3301 N  N    A LYS   A 1 158 ? 5.658  -0.037  4.717   0.60 19.34 ?  158 LYS   A N    1 
ATOM   3302 N  N    B LYS   A 1 158 ? 5.529  -0.447  3.913   0.40 15.95 ?  158 LYS   A N    1 
ATOM   3303 C  CA   A LYS   A 1 158 ? 4.687  -0.987  5.259   0.60 20.88 ?  158 LYS   A CA   1 
ATOM   3304 C  CA   B LYS   A 1 158 ? 4.548  -1.324  4.555   0.40 17.05 ?  158 LYS   A CA   1 
ATOM   3305 C  C    A LYS   A 1 158 ? 3.966  -1.734  4.145   0.60 20.38 ?  158 LYS   A C    1 
ATOM   3306 C  C    B LYS   A 1 158 ? 3.854  -2.227  3.537   0.40 16.28 ?  158 LYS   A C    1 
ATOM   3307 O  O    A LYS   A 1 158 ? 3.737  -2.944  4.249   0.60 20.55 ?  158 LYS   A O    1 
ATOM   3308 O  O    B LYS   A 1 158 ? 3.744  -3.444  3.737   0.40 16.04 ?  158 LYS   A O    1 
ATOM   3309 C  CB   A LYS   A 1 158 ? 3.684  -0.285  6.177   0.60 22.33 ?  158 LYS   A CB   1 
ATOM   3310 C  CB   B LYS   A 1 158 ? 3.533  -0.466  5.324   0.40 19.23 ?  158 LYS   A CB   1 
ATOM   3311 C  CG   A LYS   A 1 158 ? 2.441  -1.131  6.522   0.60 23.79 ?  158 LYS   A CG   1 
ATOM   3312 C  CG   B LYS   A 1 158 ? 2.361  -1.219  5.951   0.40 21.62 ?  158 LYS   A CG   1 
ATOM   3313 C  CD   A LYS   A 1 158 ? 2.775  -2.443  7.251   0.60 24.65 ?  158 LYS   A CD   1 
ATOM   3314 C  CD   B LYS   A 1 158 ? 2.808  -2.187  7.030   0.40 23.37 ?  158 LYS   A CD   1 
ATOM   3315 C  CE   A LYS   A 1 158 ? 1.501  -3.229  7.581   0.60 24.92 ?  158 LYS   A CE   1 
ATOM   3316 C  CE   B LYS   A 1 158 ? 1.638  -2.643  7.885   0.40 24.27 ?  158 LYS   A CE   1 
ATOM   3317 N  NZ   A LYS   A 1 158 ? 1.770  -4.540  8.243   0.60 24.90 ?  158 LYS   A NZ   1 
ATOM   3318 N  NZ   B LYS   A 1 158 ? 2.050  -3.660  8.890   0.40 25.04 ?  158 LYS   A NZ   1 
ATOM   3319 H  H    A LYS   A 1 158 ? 5.491  0.791   4.876   0.60 23.37 ?  158 LYS   A H    1 
ATOM   3320 H  H    B LYS   A 1 158 ? 5.340  0.390   3.975   0.40 19.31 ?  158 LYS   A H    1 
ATOM   3321 H  HA   A LYS   A 1 158 ? 5.163  -1.639  5.793   0.60 25.22 ?  158 LYS   A HA   1 
ATOM   3322 H  HA   B LYS   A 1 158 ? 5.001  -1.888  5.202   0.40 20.62 ?  158 LYS   A HA   1 
ATOM   3323 H  HB2  A LYS   A 1 158 ? 4.127  -0.061  7.012   0.60 26.97 ?  158 LYS   A HB2  1 
ATOM   3324 H  HB2  B LYS   A 1 158 ? 3.997  -0.008  6.048   0.40 23.24 ?  158 LYS   A HB2  1 
ATOM   3325 H  HB3  A LYS   A 1 158 ? 3.378  0.529   5.744   0.60 26.97 ?  158 LYS   A HB3  1 
ATOM   3326 H  HB3  B LYS   A 1 158 ? 3.159  0.193   4.719   0.40 23.24 ?  158 LYS   A HB3  1 
ATOM   3327 H  HG2  A LYS   A 1 158 ? 1.868  -0.610  7.103   0.60 28.71 ?  158 LYS   A HG2  1 
ATOM   3328 H  HG2  B LYS   A 1 158 ? 1.758  -0.576  6.362   0.40 26.10 ?  158 LYS   A HG2  1 
ATOM   3329 H  HG3  A LYS   A 1 158 ? 1.959  -1.350  5.707   0.60 28.71 ?  158 LYS   A HG3  1 
ATOM   3330 H  HG3  B LYS   A 1 158 ? 1.894  -1.718  5.267   0.40 26.10 ?  158 LYS   A HG3  1 
ATOM   3331 H  HD2  A LYS   A 1 158 ? 3.338  -2.993  6.685   0.60 29.75 ?  158 LYS   A HD2  1 
ATOM   3332 H  HD2  B LYS   A 1 158 ? 3.219  -2.966  6.621   0.40 28.21 ?  158 LYS   A HD2  1 
ATOM   3333 H  HD3  A LYS   A 1 158 ? 3.232  -2.237  8.082   0.60 29.75 ?  158 LYS   A HD3  1 
ATOM   3334 H  HD3  B LYS   A 1 158 ? 3.434  -1.740  7.612   0.40 28.21 ?  158 LYS   A HD3  1 
ATOM   3335 H  HE2  A LYS   A 1 158 ? 0.952  -2.700  8.180   0.60 30.07 ?  158 LYS   A HE2  1 
ATOM   3336 H  HE2  B LYS   A 1 158 ? 1.275  -1.877  8.361   0.40 29.29 ?  158 LYS   A HE2  1 
ATOM   3337 H  HE3  A LYS   A 1 158 ? 1.018  -3.403  6.758   0.60 30.07 ?  158 LYS   A HE3  1 
ATOM   3338 H  HE3  B LYS   A 1 158 ? 0.959  -3.035  7.315   0.40 29.29 ?  158 LYS   A HE3  1 
ATOM   3339 H  HZ1  A LYS   A 1 158 ? 1.000  -4.958  8.414   0.60 30.05 ?  158 LYS   A HZ1  1 
ATOM   3340 H  HZ1  B LYS   A 1 158 ? 1.348  -3.908  9.376   0.40 30.21 ?  158 LYS   A HZ1  1 
ATOM   3341 H  HZ2  A LYS   A 1 158 ? 2.264  -5.055  7.713   0.60 30.05 ?  158 LYS   A HZ2  1 
ATOM   3342 H  HZ2  B LYS   A 1 158 ? 2.384  -4.374  8.477   0.40 30.21 ?  158 LYS   A HZ2  1 
ATOM   3343 H  HZ3  A LYS   A 1 158 ? 2.203  -4.413  9.010   0.60 30.05 ?  158 LYS   A HZ3  1 
ATOM   3344 H  HZ3  B LYS   A 1 158 ? 2.671  -3.320  9.429   0.40 30.21 ?  158 LYS   A HZ3  1 
ATOM   3345 N  N    A ASN   A 1 159 ? 3.581  -1.030  3.080   0.60 20.37 ?  159 ASN   A N    1 
ATOM   3346 N  N    B ASN   A 1 159 ? 3.364  -1.648  2.440   0.40 16.95 ?  159 ASN   A N    1 
ATOM   3347 C  CA   A ASN   A 1 159 ? 2.914  -1.707  1.973   0.60 20.64 ?  159 ASN   A CA   1 
ATOM   3348 C  CA   B ASN   A 1 159 ? 2.726  -2.465  1.413   0.40 17.47 ?  159 ASN   A CA   1 
ATOM   3349 C  C    A ASN   A 1 159 ? 3.802  -2.795  1.378   0.60 19.80 ?  159 ASN   A C    1 
ATOM   3350 C  C    B ASN   A 1 159 ? 3.692  -3.517  0.876   0.40 16.27 ?  159 ASN   A C    1 
ATOM   3351 O  O    A ASN   A 1 159 ? 3.334  -3.906  1.104   0.60 19.38 ?  159 ASN   A O    1 
ATOM   3352 O  O    B ASN   A 1 159 ? 3.305  -4.668  0.638   0.40 16.15 ?  159 ASN   A O    1 
ATOM   3353 C  CB   A ASN   A 1 159 ? 2.482  -0.693  0.911   0.60 22.32 ?  159 ASN   A CB   1 
ATOM   3354 C  CB   B ASN   A 1 159 ? 2.189  -1.570  0.295   0.40 19.70 ?  159 ASN   A CB   1 
ATOM   3355 C  CG   A ASN   A 1 159 ? 1.181  0.005   1.268   0.60 24.80 ?  159 ASN   A CG   1 
ATOM   3356 C  CG   B ASN   A 1 159 ? 0.955  -0.793  0.716   0.40 22.22 ?  159 ASN   A CG   1 
ATOM   3357 O  OD1  A ASN   A 1 159 ? 0.315  -0.582  1.915   0.60 25.34 ?  159 ASN   A OD1  1 
ATOM   3358 O  OD1  B ASN   A 1 159 ? 1.007  0.033   1.631   0.40 23.59 ?  159 ASN   A OD1  1 
ATOM   3359 N  ND2  A ASN   A 1 159 ? 1.034  1.256   0.842   0.60 25.26 ?  159 ASN   A ND2  1 
ATOM   3360 N  ND2  B ASN   A 1 159 ? -0.160 -1.043  0.041   0.40 23.24 ?  159 ASN   A ND2  1 
ATOM   3361 H  H    A ASN   A 1 159 ? 3.687  -0.183  2.978   0.60 24.61 ?  159 ASN   A H    1 
ATOM   3362 H  H    B ASN   A 1 159 ? 3.390  -0.804  2.277   0.40 20.50 ?  159 ASN   A H    1 
ATOM   3363 H  HA   A ASN   A 1 159 ? 2.114  -2.137  2.310   0.60 24.94 ?  159 ASN   A HA   1 
ATOM   3364 H  HA   B ASN   A 1 159 ? 1.968  -2.924  1.809   0.40 21.13 ?  159 ASN   A HA   1 
ATOM   3365 H  HB2  A ASN   A 1 159 ? 3.164  -0.013  0.819   0.60 26.95 ?  159 ASN   A HB2  1 
ATOM   3366 H  HB2  B ASN   A 1 159 ? 2.873  -0.928  0.045   0.40 23.80 ?  159 ASN   A HB2  1 
ATOM   3367 H  HB3  A ASN   A 1 159 ? 2.352  -1.153  0.066   0.60 26.95 ?  159 ASN   A HB3  1 
ATOM   3368 H  HB3  B ASN   A 1 159 ? 1.952  -2.120  -0.464  0.40 23.80 ?  159 ASN   A HB3  1 
ATOM   3369 H  HD21 A ASN   A 1 159 ? 0.309  1.690   1.017   0.60 30.48 ?  159 ASN   A HD21 1 
ATOM   3370 H  HD21 B ASN   A 1 159 ? -0.887 -0.629  0.242   0.40 28.06 ?  159 ASN   A HD21 1 
ATOM   3371 H  HD22 A ASN   A 1 159 ? 1.660  1.633   0.393   0.60 30.48 ?  159 ASN   A HD22 1 
ATOM   3372 H  HD22 B ASN   A 1 159 ? -0.157 -1.621  -0.595  0.40 28.06 ?  159 ASN   A HD22 1 
ATOM   3373 N  N    A LEU   A 1 160 ? 5.090  -2.505  1.194   0.60 19.05 ?  160 LEU   A N    1 
ATOM   3374 N  N    B LEU   A 1 160 ? 4.961  -3.146  0.698   0.40 15.78 ?  160 LEU   A N    1 
ATOM   3375 C  CA   A LEU   A 1 160 ? 5.980  -3.495  0.596   0.60 18.64 ?  160 LEU   A CA   1 
ATOM   3376 C  CA   B LEU   A 1 160 ? 5.965  -4.136  0.319   0.40 15.70 ?  160 LEU   A CA   1 
ATOM   3377 C  C    A LEU   A 1 160 ? 6.147  -4.707  1.500   0.60 18.50 ?  160 LEU   A C    1 
ATOM   3378 C  C    B LEU   A 1 160 ? 6.172  -5.167  1.429   0.40 15.62 ?  160 LEU   A C    1 
ATOM   3379 O  O    A LEU   A 1 160 ? 6.202  -5.847  1.022   0.60 19.23 ?  160 LEU   A O    1 
ATOM   3380 O  O    B LEU   A 1 160 ? 6.170  -6.376  1.169   0.40 15.75 ?  160 LEU   A O    1 
ATOM   3381 C  CB   A LEU   A 1 160 ? 7.336  -2.867  0.290   0.60 18.56 ?  160 LEU   A CB   1 
ATOM   3382 C  CB   B LEU   A 1 160 ? 7.282  -3.453  -0.049  0.40 15.73 ?  160 LEU   A CB   1 
ATOM   3383 C  CG   A LEU   A 1 160 ? 8.391  -3.880  -0.155  0.60 18.99 ?  160 LEU   A CG   1 
ATOM   3384 C  CG   B LEU   A 1 160 ? 8.398  -4.418  -0.460  0.40 16.20 ?  160 LEU   A CG   1 
ATOM   3385 C  CD1  A LEU   A 1 160 ? 7.911  -4.662  -1.370  0.60 19.27 ?  160 LEU   A CD1  1 
ATOM   3386 C  CD1  B LEU   A 1 160 ? 7.977  -5.222  -1.677  0.40 16.80 ?  160 LEU   A CD1  1 
ATOM   3387 C  CD2  A LEU   A 1 160 ? 9.712  -3.194  -0.441  0.60 19.01 ?  160 LEU   A CD2  1 
ATOM   3388 C  CD2  B LEU   A 1 160 ? 9.707  -3.678  -0.714  0.40 16.34 ?  160 LEU   A CD2  1 
ATOM   3389 H  H    A LEU   A 1 160 ? 5.464  -1.760  1.413   0.60 23.03 ?  160 LEU   A H    1 
ATOM   3390 H  H    B LEU   A 1 160 ? 5.253  -2.344  0.779   0.40 19.10 ?  160 LEU   A H    1 
ATOM   3391 H  HA   A LEU   A 1 160 ? 5.591  -3.795  -0.235  0.60 22.53 ?  160 LEU   A HA   1 
ATOM   3392 H  HA   B LEU   A 1 160 ? 5.643  -4.607  -0.466  0.40 19.01 ?  160 LEU   A HA   1 
ATOM   3393 H  HB2  A LEU   A 1 160 ? 7.228  -2.209  -0.418  0.60 22.43 ?  160 LEU   A HB2  1 
ATOM   3394 H  HB2  B LEU   A 1 160 ? 7.124  -2.839  -0.787  0.40 19.04 ?  160 LEU   A HB2  1 
ATOM   3395 H  HB3  A LEU   A 1 160 ? 7.667  -2.437  1.093   0.60 22.43 ?  160 LEU   A HB3  1 
ATOM   3396 H  HB3  B LEU   A 1 160 ? 7.594  -2.967  0.725   0.40 19.04 ?  160 LEU   A HB3  1 
ATOM   3397 H  HG   A LEU   A 1 160 ? 8.545  -4.513  0.563   0.60 22.95 ?  160 LEU   A HG   1 
ATOM   3398 H  HG   B LEU   A 1 160 ? 8.552  -5.039  0.265   0.40 19.61 ?  160 LEU   A HG   1 
ATOM   3399 H  HD11 A LEU   A 1 160 ? 8.628  -5.237  -1.675  0.60 23.29 ?  160 LEU   A HD11 1 
ATOM   3400 H  HD11 B LEU   A 1 160 ? 8.744  -5.708  -2.010  0.40 20.32 ?  160 LEU   A HD11 1 
ATOM   3401 H  HD12 A LEU   A 1 160 ? 7.142  -5.204  -1.123  0.60 23.29 ?  160 LEU   A HD12 1 
ATOM   3402 H  HD12 B LEU   A 1 160 ? 7.277  -5.842  -1.420  0.40 20.32 ?  160 LEU   A HD12 1 
ATOM   3403 H  HD13 A LEU   A 1 160 ? 7.662  -4.040  -2.071  0.60 23.29 ?  160 LEU   A HD13 1 
ATOM   3404 H  HD13 B LEU   A 1 160 ? 7.648  -4.613  -2.358  0.40 20.32 ?  160 LEU   A HD13 1 
ATOM   3405 H  HD21 A LEU   A 1 160 ? 10.357 -3.863  -0.718  0.60 22.98 ?  160 LEU   A HD21 1 
ATOM   3406 H  HD21 B LEU   A 1 160 ? 10.388 -4.320  -0.968  0.40 19.77 ?  160 LEU   A HD21 1 
ATOM   3407 H  HD22 A LEU   A 1 160 ? 9.581  -2.544  -1.147  0.60 22.98 ?  160 LEU   A HD22 1 
ATOM   3408 H  HD22 B LEU   A 1 160 ? 9.575  -3.036  -1.430  0.40 19.77 ?  160 LEU   A HD22 1 
ATOM   3409 H  HD23 A LEU   A 1 160 ? 10.017 -2.753  0.367   0.60 22.98 ?  160 LEU   A HD23 1 
ATOM   3410 H  HD23 B LEU   A 1 160 ? 9.973  -3.217  0.098   0.40 19.77 ?  160 LEU   A HD23 1 
ATOM   3411 N  N    A TYR   A 1 161 ? 6.236  -4.479  2.806   0.60 18.44 ?  161 TYR   A N    1 
ATOM   3412 N  N    B TYR   A 1 161 ? 6.358  -4.712  2.676   0.40 15.75 ?  161 TYR   A N    1 
ATOM   3413 C  CA   A TYR   A 1 161 ? 6.397  -5.581  3.744   0.60 18.32 ?  161 TYR   A CA   1 
ATOM   3414 C  CA   B TYR   A 1 161 ? 6.452  -5.651  3.795   0.40 15.86 ?  161 TYR   A CA   1 
ATOM   3415 C  C    A TYR   A 1 161 ? 5.273  -6.604  3.608   0.60 18.74 ?  161 TYR   A C    1 
ATOM   3416 C  C    B TYR   A 1 161 ? 5.249  -6.578  3.814   0.40 16.93 ?  161 TYR   A C    1 
ATOM   3417 O  O    A TYR   A 1 161 ? 5.523  -7.815  3.574   0.60 18.48 ?  161 TYR   A O    1 
ATOM   3418 O  O    B TYR   A 1 161 ? 5.390  -7.805  3.867   0.40 16.95 ?  161 TYR   A O    1 
ATOM   3419 C  CB   A TYR   A 1 161 ? 6.460  -5.021  5.158   0.60 18.68 ?  161 TYR   A CB   1 
ATOM   3420 C  CB   B TYR   A 1 161 ? 6.556  -4.925  5.142   0.40 15.57 ?  161 TYR   A CB   1 
ATOM   3421 C  CG   A TYR   A 1 161 ? 6.352  -6.067  6.219   0.60 18.41 ?  161 TYR   A CG   1 
ATOM   3422 C  CG   B TYR   A 1 161 ? 6.403  -5.865  6.343   0.40 14.88 ?  161 TYR   A CG   1 
ATOM   3423 C  CD1  A TYR   A 1 161 ? 7.469  -6.771  6.632   0.60 18.38 ?  161 TYR   A CD1  1 
ATOM   3424 C  CD1  B TYR   A 1 161 ? 7.474  -6.617  6.802   0.40 14.82 ?  161 TYR   A CD1  1 
ATOM   3425 C  CD2  A TYR   A 1 161 ? 5.129  -6.356  6.811   0.60 18.34 ?  161 TYR   A CD2  1 
ATOM   3426 C  CD2  B TYR   A 1 161 ? 5.188  -5.979  7.031   0.40 14.52 ?  161 TYR   A CD2  1 
ATOM   3427 C  CE1  A TYR   A 1 161 ? 7.376  -7.732  7.597   0.60 18.06 ?  161 TYR   A CE1  1 
ATOM   3428 C  CE1  B TYR   A 1 161 ? 7.348  -7.471  7.892   0.40 14.85 ?  161 TYR   A CE1  1 
ATOM   3429 C  CE2  A TYR   A 1 161 ? 5.025  -7.315  7.781   0.60 17.93 ?  161 TYR   A CE2  1 
ATOM   3430 C  CE2  B TYR   A 1 161 ? 5.055  -6.831  8.133   0.40 14.54 ?  161 TYR   A CE2  1 
ATOM   3431 C  CZ   A TYR   A 1 161 ? 6.155  -8.000  8.171   0.60 18.03 ?  161 TYR   A CZ   1 
ATOM   3432 C  CZ   B TYR   A 1 161 ? 6.140  -7.571  8.555   0.40 14.97 ?  161 TYR   A CZ   1 
ATOM   3433 O  OH   A TYR   A 1 161 ? 6.070  -8.959  9.143   0.60 18.18 ?  161 TYR   A OH   1 
ATOM   3434 O  OH   B TYR   A 1 161 ? 6.024  -8.421  9.639   0.40 15.74 ?  161 TYR   A OH   1 
ATOM   3435 H  H    A TYR   A 1 161 ? 6.206  -3.706  3.177   0.60 22.30 ?  161 TYR   A H    1 
ATOM   3436 H  H    B TYR   A 1 161 ? 6.425  -3.886  2.889   0.40 19.06 ?  161 TYR   A H    1 
ATOM   3437 H  HA   A TYR   A 1 161 ? 7.227  -6.040  3.564   0.60 22.15 ?  161 TYR   A HA   1 
ATOM   3438 H  HA   B TYR   A 1 161 ? 7.247  -6.192  3.692   0.40 19.19 ?  161 TYR   A HA   1 
ATOM   3439 H  HB2  A TYR   A 1 161 ? 7.308  -4.571  5.274   0.60 22.58 ?  161 TYR   A HB2  1 
ATOM   3440 H  HB2  B TYR   A 1 161 ? 7.425  -4.495  5.207   0.40 18.85 ?  161 TYR   A HB2  1 
ATOM   3441 H  HB3  A TYR   A 1 161 ? 5.730  -4.397  5.283   0.60 22.58 ?  161 TYR   A HB3  1 
ATOM   3442 H  HB3  B TYR   A 1 161 ? 5.856  -4.250  5.196   0.40 18.85 ?  161 TYR   A HB3  1 
ATOM   3443 H  HD1  A TYR   A 1 161 ? 8.291  -6.592  6.241   0.60 22.22 ?  161 TYR   A HD1  1 
ATOM   3444 H  HD1  B TYR   A 1 161 ? 8.287  -6.556  6.366   0.40 17.95 ?  161 TYR   A HD1  1 
ATOM   3445 H  HD2  A TYR   A 1 161 ? 4.365  -5.892  6.543   0.60 22.17 ?  161 TYR   A HD2  1 
ATOM   3446 H  HD2  B TYR   A 1 161 ? 4.452  -5.476  6.761   0.40 17.59 ?  161 TYR   A HD2  1 
ATOM   3447 H  HE1  A TYR   A 1 161 ? 8.130  -8.202  7.864   0.60 21.83 ?  161 TYR   A HE1  1 
ATOM   3448 H  HE1  B TYR   A 1 161 ? 8.076  -7.971  8.182   0.40 17.98 ?  161 TYR   A HE1  1 
ATOM   3449 H  HE2  A TYR   A 1 161 ? 4.196  -7.503  8.169   0.60 21.68 ?  161 TYR   A HE2  1 
ATOM   3450 H  HE2  B TYR   A 1 161 ? 4.239  -6.898  8.586   0.40 17.62 ?  161 TYR   A HE2  1 
ATOM   3451 H  HH   A TYR   A 1 161 ? 5.270  -9.029  9.408   0.60 21.99 ?  161 TYR   A HH   1 
ATOM   3452 H  HH   B TYR   A 1 161 ? 5.241  -8.392  9.960   0.40 19.05 ?  161 TYR   A HH   1 
ATOM   3453 N  N    A ASP   A 1 162 ? 4.023  -6.137  3.531   0.60 19.33 ?  162 ASP   A N    1 
ATOM   3454 N  N    B ASP   A 1 162 ? 4.048  -5.998  3.791   0.40 18.05 ?  162 ASP   A N    1 
ATOM   3455 C  CA   A ASP   A 1 162 ? 2.890  -7.061  3.484   0.60 19.67 ?  162 ASP   A CA   1 
ATOM   3456 C  CA   B ASP   A 1 162 ? 2.839  -6.811  3.717   0.40 18.99 ?  162 ASP   A CA   1 
ATOM   3457 C  C    A ASP   A 1 162 ? 2.929  -7.913  2.221   0.60 19.54 ?  162 ASP   A C    1 
ATOM   3458 C  C    B ASP   A 1 162 ? 2.877  -7.741  2.509   0.40 19.50 ?  162 ASP   A C    1 
ATOM   3459 O  O    A ASP   A 1 162 ? 2.587  -9.102  2.252   0.60 19.78 ?  162 ASP   A O    1 
ATOM   3460 O  O    B ASP   A 1 162 ? 2.462  -8.903  2.596   0.40 19.75 ?  162 ASP   A O    1 
ATOM   3461 C  CB   A ASP   A 1 162 ? 1.566  -6.289  3.562   0.60 20.36 ?  162 ASP   A CB   1 
ATOM   3462 C  CB   B ASP   A 1 162 ? 1.604  -5.909  3.650   0.40 19.60 ?  162 ASP   A CB   1 
ATOM   3463 C  CG   A ASP   A 1 162 ? 1.259  -5.757  4.955   0.60 21.22 ?  162 ASP   A CG   1 
ATOM   3464 C  CG   B ASP   A 1 162 ? 1.313  -5.195  4.959   0.40 20.40 ?  162 ASP   A CG   1 
ATOM   3465 O  OD1  A ASP   A 1 162 ? 1.958  -6.130  5.918   0.60 22.15 ?  162 ASP   A OD1  1 
ATOM   3466 O  OD1  B ASP   A 1 162 ? 1.887  -5.573  5.999   0.40 20.62 ?  162 ASP   A OD1  1 
ATOM   3467 O  OD2  A ASP   A 1 162 ? 0.290  -4.967  5.083   0.60 21.72 -1 162 ASP   A OD2  1 
ATOM   3468 O  OD2  B ASP   A 1 162 ? 0.498  -4.246  4.943   0.40 21.03 -1 162 ASP   A OD2  1 
ATOM   3469 H  H    A ASP   A 1 162 ? 3.799  -5.313  3.498   0.60 23.36 ?  162 ASP   A H    1 
ATOM   3470 H  H    B ASP   A 1 162 ? 3.910  -5.148  3.824   0.40 21.83 ?  162 ASP   A H    1 
ATOM   3471 H  HA   A ASP   A 1 162 ? 2.926  -7.668  4.239   0.60 23.77 ?  162 ASP   A HA   1 
ATOM   3472 H  HA   B ASP   A 1 162 ? 2.773  -7.355  4.517   0.40 22.95 ?  162 ASP   A HA   1 
ATOM   3473 H  HB2  A ASP   A 1 162 ? 1.605  -5.532  2.966   0.60 24.59 ?  162 ASP   A HB2  1 
ATOM   3474 H  HB2  B ASP   A 1 162 ? 1.743  -5.232  2.973   0.40 23.68 ?  162 ASP   A HB2  1 
ATOM   3475 H  HB3  A ASP   A 1 162 ? 0.833  -6.877  3.313   0.60 24.59 ?  162 ASP   A HB3  1 
ATOM   3476 H  HB3  B ASP   A 1 162 ? 0.832  -6.451  3.432   0.40 23.68 ?  162 ASP   A HB3  1 
ATOM   3477 N  N    A LYS   A 1 163 ? 3.342  -7.325  1.100   0.60 20.40 ?  163 LYS   A N    1 
ATOM   3478 N  N    B LYS   A 1 163 ? 3.376  -7.249  1.372   0.40 20.60 ?  163 LYS   A N    1 
ATOM   3479 C  CA   A LYS   A 1 163 ? 3.470  -8.095  -0.130  0.60 21.10 ?  163 LYS   A CA   1 
ATOM   3480 C  CA   B LYS   A 1 163 ? 3.404  -8.059  0.155   0.40 21.33 ?  163 LYS   A CA   1 
ATOM   3481 C  C    A LYS   A 1 163 ? 4.572  -9.139  -0.014  0.60 20.60 ?  163 LYS   A C    1 
ATOM   3482 C  C    B LYS   A 1 163 ? 4.457  -9.163  0.245   0.40 20.80 ?  163 LYS   A C    1 
ATOM   3483 O  O    A LYS   A 1 163 ? 4.447  -10.240 -0.561  0.60 20.51 ?  163 LYS   A O    1 
ATOM   3484 O  O    B LYS   A 1 163 ? 4.187  -10.323 -0.084  0.40 20.98 ?  163 LYS   A O    1 
ATOM   3485 C  CB   A LYS   A 1 163 ? 3.742  -7.160  -1.307  0.60 23.81 ?  163 LYS   A CB   1 
ATOM   3486 C  CB   B LYS   A 1 163 ? 3.653  -7.148  -1.049  0.40 23.50 ?  163 LYS   A CB   1 
ATOM   3487 C  CG   A LYS   A 1 163 ? 3.736  -7.853  -2.655  0.60 26.70 ?  163 LYS   A CG   1 
ATOM   3488 C  CG   B LYS   A 1 163 ? 3.902  -7.854  -2.370  0.40 25.64 ?  163 LYS   A CG   1 
ATOM   3489 C  CD   A LYS   A 1 163 ? 4.102  -6.892  -3.768  0.60 29.45 ?  163 LYS   A CD   1 
ATOM   3490 C  CD   B LYS   A 1 163 ? 4.446  -6.860  -3.382  0.40 27.82 ?  163 LYS   A CD   1 
ATOM   3491 C  CE   A LYS   A 1 163 ? 4.002  -7.560  -5.127  0.60 31.75 ?  163 LYS   A CE   1 
ATOM   3492 C  CE   B LYS   A 1 163 ? 4.273  -7.344  -4.807  0.40 29.49 ?  163 LYS   A CE   1 
ATOM   3493 N  NZ   A LYS   A 1 163 ? 4.637  -6.741  -6.192  0.60 32.93 ?  163 LYS   A NZ   1 
ATOM   3494 N  NZ   B LYS   A 1 163 ? 4.781  -6.343  -5.785  0.40 30.40 ?  163 LYS   A NZ   1 
ATOM   3495 H  H    A LYS   A 1 163 ? 3.554  -6.498  1.028   0.60 24.65 ?  163 LYS   A H    1 
ATOM   3496 H  H    B LYS   A 1 163 ? 3.697  -6.451  1.278   0.40 24.89 ?  163 LYS   A H    1 
ATOM   3497 H  HA   A LYS   A 1 163 ? 2.634  -8.560  -0.303  0.60 25.48 ?  163 LYS   A HA   1 
ATOM   3498 H  HA   B LYS   A 1 163 ? 2.542  -8.478  0.037   0.40 25.75 ?  163 LYS   A HA   1 
ATOM   3499 H  HB2  A LYS   A 1 163 ? 3.056  -6.474  -1.326  0.60 28.73 ?  163 LYS   A HB2  1 
ATOM   3500 H  HB2  B LYS   A 1 163 ? 2.872  -6.581  -1.173  0.40 28.36 ?  163 LYS   A HB2  1 
ATOM   3501 H  HB3  A LYS   A 1 163 ? 4.613  -6.753  -1.188  0.60 28.73 ?  163 LYS   A HB3  1 
ATOM   3502 H  HB3  B LYS   A 1 163 ? 4.426  -6.595  -0.868  0.40 28.36 ?  163 LYS   A HB3  1 
ATOM   3503 H  HG2  A LYS   A 1 163 ? 4.386  -8.573  -2.652  0.60 32.20 ?  163 LYS   A HG2  1 
ATOM   3504 H  HG2  B LYS   A 1 163 ? 4.558  -8.559  -2.258  0.40 30.94 ?  163 LYS   A HG2  1 
ATOM   3505 H  HG3  A LYS   A 1 163 ? 2.849  -8.203  -2.833  0.60 32.20 ?  163 LYS   A HG3  1 
ATOM   3506 H  HG3  B LYS   A 1 163 ? 3.067  -8.216  -2.708  0.40 30.94 ?  163 LYS   A HG3  1 
ATOM   3507 H  HD2  A LYS   A 1 163 ? 3.490  -6.138  -3.755  0.60 35.51 ?  163 LYS   A HD2  1 
ATOM   3508 H  HD2  B LYS   A 1 163 ? 3.973  -6.019  -3.287  0.40 33.55 ?  163 LYS   A HD2  1 
ATOM   3509 H  HD3  A LYS   A 1 163 ? 5.014  -6.585  -3.641  0.60 35.51 ?  163 LYS   A HD3  1 
ATOM   3510 H  HD3  B LYS   A 1 163 ? 5.395  -6.729  -3.219  0.40 33.55 ?  163 LYS   A HD3  1 
ATOM   3511 H  HE2  A LYS   A 1 163 ? 4.437  -8.426  -5.102  0.60 38.27 ?  163 LYS   A HE2  1 
ATOM   3512 H  HE2  B LYS   A 1 163 ? 4.763  -8.171  -4.926  0.40 35.55 ?  163 LYS   A HE2  1 
ATOM   3513 H  HE3  A LYS   A 1 163 ? 3.069  -7.672  -5.351  0.60 38.27 ?  163 LYS   A HE3  1 
ATOM   3514 H  HE3  B LYS   A 1 163 ? 3.330  -7.488  -4.981  0.40 35.55 ?  163 LYS   A HE3  1 
ATOM   3515 H  HZ1  A LYS   A 1 163 ? 4.569  -7.156  -6.975  0.60 39.68 ?  163 LYS   A HZ1  1 
ATOM   3516 H  HZ1  B LYS   A 1 163 ? 4.670  -6.644  -6.615  0.40 36.64 ?  163 LYS   A HZ1  1 
ATOM   3517 H  HZ2  A LYS   A 1 163 ? 4.233  -5.950  -6.245  0.60 39.68 ?  163 LYS   A HZ2  1 
ATOM   3518 H  HZ2  B LYS   A 1 163 ? 4.336  -5.576  -5.694  0.40 36.64 ?  163 LYS   A HZ2  1 
ATOM   3519 H  HZ3  A LYS   A 1 163 ? 5.499  -6.613  -6.006  0.60 39.68 ?  163 LYS   A HZ3  1 
ATOM   3520 H  HZ3  B LYS   A 1 163 ? 5.647  -6.192  -5.645  0.40 36.64 ?  163 LYS   A HZ3  1 
ATOM   3521 N  N    . LEU   A 1 164 ? 5.666  -8.811  0.685   1.00 20.02 ?  164 LEU   A N    1 
ATOM   3522 C  CA   . LEU   A 1 164 ? 6.750  -9.785  0.828   1.00 19.13 ?  164 LEU   A CA   1 
ATOM   3523 C  C    . LEU   A 1 164 ? 6.322  -10.960 1.695   1.00 19.07 ?  164 LEU   A C    1 
ATOM   3524 O  O    . LEU   A 1 164 ? 6.626  -12.117 1.385   1.00 19.68 ?  164 LEU   A O    1 
ATOM   3525 C  CB   . LEU   A 1 164 ? 7.966  -9.110  1.457   1.00 18.86 ?  164 LEU   A CB   1 
ATOM   3526 C  CG   . LEU   A 1 164 ? 8.702  -8.091  0.590   1.00 18.97 ?  164 LEU   A CG   1 
ATOM   3527 C  CD1  . LEU   A 1 164 ? 9.638  -7.238  1.440   1.00 19.11 ?  164 LEU   A CD1  1 
ATOM   3528 C  CD2  . LEU   A 1 164 ? 9.473  -8.787  -0.512  1.00 19.48 ?  164 LEU   A CD2  1 
ATOM   3529 H  H    A LEU   A 1 164 ? 5.807  -8.053  1.065   0.60 24.19 ?  164 LEU   A H    1 
ATOM   3530 H  H    B LEU   A 1 164 ? 5.885  -8.015  0.925   0.40 24.19 ?  164 LEU   A H    1 
ATOM   3531 H  HA   . LEU   A 1 164 ? 6.999  -10.126 -0.043  1.00 23.12 ?  164 LEU   A HA   1 
ATOM   3532 H  HB2  . LEU   A 1 164 ? 7.678  -8.650  2.258   1.00 22.79 ?  164 LEU   A HB2  1 
ATOM   3533 H  HB3  . LEU   A 1 164 ? 8.607  -9.798  1.694   1.00 22.79 ?  164 LEU   A HB3  1 
ATOM   3534 H  HG   . LEU   A 1 164 ? 8.055  -7.501  0.176   1.00 22.93 ?  164 LEU   A HG   1 
ATOM   3535 H  HD11 . LEU   A 1 164 ? 10.074 -6.582  0.876   1.00 23.10 ?  164 LEU   A HD11 1 
ATOM   3536 H  HD12 . LEU   A 1 164 ? 9.115  -6.791  2.127   1.00 23.10 ?  164 LEU   A HD12 1 
ATOM   3537 H  HD13 . LEU   A 1 164 ? 10.300 -7.812  1.856   1.00 23.10 ?  164 LEU   A HD13 1 
ATOM   3538 H  HD21 . LEU   A 1 164 ? 9.946  -8.118  -1.034  1.00 23.54 ?  164 LEU   A HD21 1 
ATOM   3539 H  HD22 . LEU   A 1 164 ? 10.105 -9.404  -0.114  1.00 23.54 ?  164 LEU   A HD22 1 
ATOM   3540 H  HD23 . LEU   A 1 164 ? 8.849  -9.267  -1.077  1.00 23.54 ?  164 LEU   A HD23 1 
ATOM   3541 N  N    . VAL   A 1 165 ? 5.631  -10.676 2.796   1.00 18.50 ?  165 VAL   A N    1 
ATOM   3542 C  CA   . VAL   A 1 165 ? 5.148  -11.738 3.673   1.00 18.51 ?  165 VAL   A CA   1 
ATOM   3543 C  C    . VAL   A 1 165 ? 4.110  -12.589 2.953   1.00 18.68 ?  165 VAL   A C    1 
ATOM   3544 O  O    . VAL   A 1 165 ? 4.202  -13.823 2.919   1.00 18.61 ?  165 VAL   A O    1 
ATOM   3545 C  CB   . VAL   A 1 165 ? 4.589  -11.129 4.972   1.00 18.90 ?  165 VAL   A CB   1 
ATOM   3546 C  CG1  . VAL   A 1 165 ? 3.819  -12.172 5.771   1.00 19.46 ?  165 VAL   A CG1  1 
ATOM   3547 C  CG2  . VAL   A 1 165 ? 5.708  -10.505 5.798   1.00 19.56 ?  165 VAL   A CG2  1 
ATOM   3548 H  H    . VAL   A 1 165 ? 5.428  -9.886  3.058   1.00 22.36 ?  165 VAL   A H    1 
ATOM   3549 H  HA   . VAL   A 1 165 ? 5.888  -12.315 3.917   1.00 22.38 ?  165 VAL   A HA   1 
ATOM   3550 H  HB   . VAL   A 1 165 ? 3.966  -10.421 4.743   1.00 22.85 ?  165 VAL   A HB   1 
ATOM   3551 H  HG11 . VAL   A 1 165 ? 3.723  -11.861 6.685   1.00 23.52 ?  165 VAL   A HG11 1 
ATOM   3552 H  HG12 . VAL   A 1 165 ? 2.939  -12.290 5.373   1.00 23.52 ?  165 VAL   A HG12 1 
ATOM   3553 H  HG13 . VAL   A 1 165 ? 4.307  -13.006 5.755   1.00 23.52 ?  165 VAL   A HG13 1 
ATOM   3554 H  HG21 . VAL   A 1 165 ? 5.339  -10.171 6.631   1.00 23.64 ?  165 VAL   A HG21 1 
ATOM   3555 H  HG22 . VAL   A 1 165 ? 6.380  -11.178 5.980   1.00 23.64 ?  165 VAL   A HG22 1 
ATOM   3556 H  HG23 . VAL   A 1 165 ? 6.100  -9.773  5.294   1.00 23.64 ?  165 VAL   A HG23 1 
ATOM   3557 N  N    . SER   A 1 166 ? 3.107  -11.940 2.364   1.00 19.15 ?  166 SER   A N    1 
ATOM   3558 C  CA   . SER   A 1 166 ? 1.985  -12.677 1.797   1.00 20.35 ?  166 SER   A CA   1 
ATOM   3559 C  C    . SER   A 1 166 ? 2.403  -13.523 0.607   1.00 20.96 ?  166 SER   A C    1 
ATOM   3560 O  O    . SER   A 1 166 ? 1.759  -14.542 0.321   1.00 23.20 ?  166 SER   A O    1 
ATOM   3561 C  CB   . SER   A 1 166 ? 0.874  -11.711 1.381   1.00 22.73 ?  166 SER   A CB   1 
ATOM   3562 O  OG   . SER   A 1 166 ? 0.340  -11.025 2.500   1.00 25.78 ?  166 SER   A OG   1 
ATOM   3563 H  H    . SER   A 1 166 ? 3.044  -11.090 2.295   1.00 23.14 ?  166 SER   A H    1 
ATOM   3564 H  HA   . SER   A 1 166 ? 1.615  -13.277 2.463   1.00 24.58 ?  166 SER   A HA   1 
ATOM   3565 H  HB2  . SER   A 1 166 ? 1.228  -11.063 0.756   1.00 27.44 ?  166 SER   A HB2  1 
ATOM   3566 H  HB3  . SER   A 1 166 ? 0.152  -12.213 0.959   1.00 27.44 ?  166 SER   A HB3  1 
ATOM   3567 H  HG   . SER   A 1 166 ? 0.951  -10.581 2.879   1.00 31.10 ?  166 SER   A HG   1 
ATOM   3568 N  N    . SER   A 1 167 ? 3.461  -13.122 -0.098  1.00 20.67 ?  167 SER   A N    1 
ATOM   3569 C  CA   . SER   A 1 167 ? 3.909  -13.838 -1.281  1.00 21.81 ?  167 SER   A CA   1 
ATOM   3570 C  C    . SER   A 1 167 ? 5.062  -14.789 -0.994  1.00 22.04 ?  167 SER   A C    1 
ATOM   3571 O  O    . SER   A 1 167 ? 5.578  -15.411 -1.928  1.00 22.82 ?  167 SER   A O    1 
ATOM   3572 C  CB   . SER   A 1 167 ? 4.313  -12.848 -2.383  1.00 22.74 ?  167 SER   A CB   1 
ATOM   3573 O  OG   . SER   A 1 167 ? 5.389  -12.022 -1.956  1.00 23.42 ?  167 SER   A OG   1 
ATOM   3574 H  H    . SER   A 1 167 ? 3.936  -12.423 0.093   1.00 24.97 ?  167 SER   A H    1 
ATOM   3575 H  HA   . SER   A 1 167 ? 3.170  -14.362 -1.618  1.00 26.33 ?  167 SER   A HA   1 
ATOM   3576 H  HB2  . SER   A 1 167 ? 4.594  -13.350 -3.166  1.00 27.45 ?  167 SER   A HB2  1 
ATOM   3577 H  HB3  . SER   A 1 167 ? 3.539  -12.299 -2.612  1.00 27.45 ?  167 SER   A HB3  1 
ATOM   3578 H  HG   . SER   A 1 167 ? 5.150  -11.592 -1.269  1.00 28.27 ?  167 SER   A HG   1 
ATOM   3579 N  N    . PHE   A 1 168 ? 5.480  -14.919 0.263   1.00 21.60 ?  168 PHE   A N    1 
ATOM   3580 C  CA   . PHE   A 1 168 ? 6.670  -15.703 0.567   1.00 21.94 ?  168 PHE   A CA   1 
ATOM   3581 C  C    . PHE   A 1 168 ? 6.380  -17.191 0.460   1.00 24.75 ?  168 PHE   A C    1 
ATOM   3582 O  O    . PHE   A 1 168 ? 5.424  -17.698 1.057   1.00 25.69 ?  168 PHE   A O    1 
ATOM   3583 C  CB   . PHE   A 1 168 ? 7.183  -15.405 1.971   1.00 20.55 ?  168 PHE   A CB   1 
ATOM   3584 C  CG   . PHE   A 1 168 ? 8.463  -16.126 2.294   1.00 19.09 ?  168 PHE   A CG   1 
ATOM   3585 C  CD1  . PHE   A 1 168 ? 9.636  -15.753 1.674   1.00 19.40 ?  168 PHE   A CD1  1 
ATOM   3586 C  CD2  . PHE   A 1 168 ? 8.495  -17.191 3.185   1.00 18.53 ?  168 PHE   A CD2  1 
ATOM   3587 C  CE1  . PHE   A 1 168 ? 10.819 -16.403 1.941   1.00 19.04 ?  168 PHE   A CE1  1 
ATOM   3588 C  CE2  . PHE   A 1 168 ? 9.688  -17.845 3.459   1.00 18.80 ?  168 PHE   A CE2  1 
ATOM   3589 C  CZ   . PHE   A 1 168 ? 10.845 -17.449 2.835   1.00 19.13 ?  168 PHE   A CZ   1 
ATOM   3590 H  H    . PHE   A 1 168 ? 5.103  -14.558 0.946   1.00 26.09 ?  168 PHE   A H    1 
ATOM   3591 H  HA   . PHE   A 1 168 ? 7.371  -15.478 -0.069  1.00 26.50 ?  168 PHE   A HA   1 
ATOM   3592 H  HB2  . PHE   A 1 168 ? 7.348  -14.453 2.049   1.00 24.83 ?  168 PHE   A HB2  1 
ATOM   3593 H  HB3  . PHE   A 1 168 ? 6.510  -15.679 2.613   1.00 24.83 ?  168 PHE   A HB3  1 
ATOM   3594 H  HD1  . PHE   A 1 168 ? 9.630  -15.046 1.070   1.00 23.45 ?  168 PHE   A HD1  1 
ATOM   3595 H  HD2  . PHE   A 1 168 ? 7.710  -17.461 3.610   1.00 22.40 ?  168 PHE   A HD2  1 
ATOM   3596 H  HE1  . PHE   A 1 168 ? 11.607 -16.135 1.521   1.00 23.01 ?  168 PHE   A HE1  1 
ATOM   3597 H  HE2  . PHE   A 1 168 ? 9.700  -18.554 4.062   1.00 22.72 ?  168 PHE   A HE2  1 
ATOM   3598 H  HZ   . PHE   A 1 168 ? 11.646 -17.888 3.017   1.00 23.12 ?  168 PHE   A HZ   1 
ATOM   3599 N  N    . LEU   A 1 169 ? 7.246  -17.901 -0.259  1.00 29.21 ?  169 LEU   A N    1 
ATOM   3600 C  CA   . LEU   A 1 169 ? 7.083  -19.333 -0.419  1.00 35.62 ?  169 LEU   A CA   1 
ATOM   3601 C  C    . LEU   A 1 169 ? 7.990  -20.057 0.563   1.00 37.79 ?  169 LEU   A C    1 
ATOM   3602 O  O    . LEU   A 1 169 ? 7.539  -20.483 1.627   1.00 38.53 ?  169 LEU   A O    1 
ATOM   3603 C  CB   . LEU   A 1 169 ? 7.388  -19.757 -1.858  1.00 38.56 ?  169 LEU   A CB   1 
ATOM   3604 C  CG   . LEU   A 1 169 ? 7.044  -21.206 -2.217  1.00 41.20 ?  169 LEU   A CG   1 
ATOM   3605 C  CD1  . LEU   A 1 169 ? 5.644  -21.565 -1.739  1.00 42.09 ?  169 LEU   A CD1  1 
ATOM   3606 C  CD2  . LEU   A 1 169 ? 7.167  -21.427 -3.718  1.00 42.09 ?  169 LEU   A CD2  1 
ATOM   3607 O  OXT  . LEU   A 1 169 ? 9.188  -20.214 0.326   1.00 37.80 -1 169 LEU   A OXT  1 
ATOM   3608 H  H    . LEU   A 1 169 ? 7.944  -17.578 -0.655  1.00 35.22 ?  169 LEU   A H    1 
ATOM   3609 H  HA   . LEU   A 1 169 ? 6.168  -19.565 -0.214  1.00 42.91 ?  169 LEU   A HA   1 
ATOM   3610 H  HB2  . LEU   A 1 169 ? 6.883  -19.186 -2.456  1.00 46.44 ?  169 LEU   A HB2  1 
ATOM   3611 H  HB3  . LEU   A 1 169 ? 8.336  -19.639 -2.020  1.00 46.44 ?  169 LEU   A HB3  1 
ATOM   3612 H  HG   . LEU   A 1 169 ? 7.672  -21.799 -1.776  1.00 49.60 ?  169 LEU   A HG   1 
ATOM   3613 H  HD11 . LEU   A 1 169 ? 5.360  -22.380 -2.179  1.00 50.68 ?  169 LEU   A HD11 1 
ATOM   3614 H  HD12 . LEU   A 1 169 ? 5.662  -21.697 -0.777  1.00 50.68 ?  169 LEU   A HD12 1 
ATOM   3615 H  HD13 . LEU   A 1 169 ? 5.039  -20.840 -1.963  1.00 50.68 ?  169 LEU   A HD13 1 
ATOM   3616 H  HD21 . LEU   A 1 169 ? 6.954  -22.352 -3.920  1.00 50.67 ?  169 LEU   A HD21 1 
ATOM   3617 H  HD22 . LEU   A 1 169 ? 6.547  -20.837 -4.175  1.00 50.67 ?  169 LEU   A HD22 1 
ATOM   3618 H  HD23 . LEU   A 1 169 ? 8.076  -21.229 -3.992  1.00 50.67 ?  169 LEU   A HD23 1 
ATOM   3619 N  N    A SER   B 1 1   ? 50.814 -9.226  -23.699 0.60 28.97 ?  1   SER   B N    1 
ATOM   3620 N  N    B SER   B 1 1   ? 50.775 -9.265  -23.665 0.40 27.19 ?  1   SER   B N    1 
ATOM   3621 C  CA   A SER   B 1 1   ? 51.322 -10.294 -22.816 0.60 29.14 ?  1   SER   B CA   1 
ATOM   3622 C  CA   B SER   B 1 1   ? 51.237 -10.275 -22.691 0.40 27.21 ?  1   SER   B CA   1 
ATOM   3623 C  C    A SER   B 1 1   ? 50.257 -11.351 -22.577 0.60 28.08 ?  1   SER   B C    1 
ATOM   3624 C  C    B SER   B 1 1   ? 50.171 -11.341 -22.477 0.40 26.11 ?  1   SER   B C    1 
ATOM   3625 O  O    A SER   B 1 1   ? 49.061 -11.135 -22.810 0.60 28.07 ?  1   SER   B O    1 
ATOM   3626 O  O    B SER   B 1 1   ? 49.000 -11.165 -22.833 0.40 25.71 ?  1   SER   B O    1 
ATOM   3627 C  CB   A SER   B 1 1   ? 51.786 -9.718  -21.480 0.60 29.78 ?  1   SER   B CB   1 
ATOM   3628 C  CB   B SER   B 1 1   ? 51.577 -9.618  -21.357 0.40 27.85 ?  1   SER   B CB   1 
ATOM   3629 O  OG   A SER   B 1 1   ? 50.683 -9.388  -20.658 0.60 31.35 ?  1   SER   B OG   1 
ATOM   3630 O  OG   B SER   B 1 1   ? 50.402 -9.395  -20.598 0.40 29.08 ?  1   SER   B OG   1 
ATOM   3631 H  H1   A SER   B 1 1   ? 50.719 -9.552  -24.519 0.60 34.93 ?  1   SER   B H1   1 
ATOM   3632 H  H1   B SER   B 1 1   ? 50.717 -9.642  -24.466 0.40 32.79 ?  1   SER   B H1   1 
ATOM   3633 H  H2   A SER   B 1 1   ? 50.034 -8.943  -23.391 0.60 34.93 ?  1   SER   B H2   1 
ATOM   3634 H  H2   B SER   B 1 1   ? 49.981 -8.963  -23.413 0.40 32.79 ?  1   SER   B H2   1 
ATOM   3635 H  H3   A SER   B 1 1   ? 51.400 -8.559  -23.705 0.60 34.93 ?  1   SER   B H3   1 
ATOM   3636 H  H3   B SER   B 1 1   ? 51.361 -8.598  -23.687 0.40 32.79 ?  1   SER   B H3   1 
ATOM   3637 H  HA   A SER   B 1 1   ? 52.078 -10.711 -23.248 0.60 35.14 ?  1   SER   B HA   1 
ATOM   3638 H  HA   B SER   B 1 1   ? 52.036 -10.694 -23.042 0.40 32.81 ?  1   SER   B HA   1 
ATOM   3639 H  HB2  A SER   B 1 1   ? 52.329 -10.383 -21.030 0.60 35.90 ?  1   SER   B HB2  1 
ATOM   3640 H  HB2  B SER   B 1 1   ? 52.173 -10.205 -20.868 0.40 33.59 ?  1   SER   B HB2  1 
ATOM   3641 H  HB3  A SER   B 1 1   ? 52.306 -8.918  -21.644 0.60 35.90 ?  1   SER   B HB3  1 
ATOM   3642 H  HB3  B SER   B 1 1   ? 52.008 -8.766  -21.522 0.40 33.59 ?  1   SER   B HB3  1 
ATOM   3643 H  HG   A SER   B 1 1   ? 50.946 -8.931  -20.003 0.60 37.78 ?  1   SER   B HG   1 
ATOM   3644 H  HG   B SER   B 1 1   ? 50.544 -8.798  -20.026 0.40 35.06 ?  1   SER   B HG   1 
ATOM   3645 N  N    A MET   B 1 2   ? 50.715 -12.498 -22.096 0.60 26.84 ?  2   MET   B N    1 
ATOM   3646 N  N    B MET   B 1 2   ? 50.592 -12.446 -21.877 0.40 25.27 ?  2   MET   B N    1 
ATOM   3647 C  CA   A MET   B 1 2   ? 49.884 -13.676 -21.911 0.60 26.37 ?  2   MET   B CA   1 
ATOM   3648 C  CA   B MET   B 1 2   ? 49.768 -13.639 -21.723 0.40 24.77 ?  2   MET   B CA   1 
ATOM   3649 C  C    A MET   B 1 2   ? 49.640 -13.858 -20.422 0.60 23.36 ?  2   MET   B C    1 
ATOM   3650 C  C    B MET   B 1 2   ? 49.484 -13.844 -20.241 0.40 22.92 ?  2   MET   B C    1 
ATOM   3651 O  O    A MET   B 1 2   ? 50.588 -14.044 -19.653 0.60 22.97 ?  2   MET   B O    1 
ATOM   3652 O  O    B MET   B 1 2   ? 50.354 -14.294 -19.489 0.40 23.31 ?  2   MET   B O    1 
ATOM   3653 C  CB   A MET   B 1 2   ? 50.593 -14.891 -22.499 0.60 29.98 ?  2   MET   B CB   1 
ATOM   3654 C  CB   B MET   B 1 2   ? 50.516 -14.826 -22.306 0.40 26.77 ?  2   MET   B CB   1 
ATOM   3655 C  CG   A MET   B 1 2   ? 49.729 -16.132 -22.628 0.60 33.34 ?  2   MET   B CG   1 
ATOM   3656 C  CG   B MET   B 1 2   ? 49.640 -15.982 -22.761 0.40 28.48 ?  2   MET   B CG   1 
ATOM   3657 S  SD   A MET   B 1 2   ? 50.549 -17.399 -23.612 0.60 36.70 ?  2   MET   B SD   1 
ATOM   3658 S  SD   B MET   B 1 2   ? 50.529 -17.069 -23.881 0.40 30.19 ?  2   MET   B SD   1 
ATOM   3659 C  CE   A MET   B 1 2   ? 51.094 -16.394 -24.990 0.60 37.00 ?  2   MET   B CE   1 
ATOM   3660 C  CE   B MET   B 1 2   ? 51.438 -15.869 -24.830 0.40 30.61 ?  2   MET   B CE   1 
ATOM   3661 H  H    A MET   B 1 2   ? 51.533 -12.625 -21.857 0.60 32.38 ?  2   MET   B H    1 
ATOM   3662 H  H    B MET   B 1 2   ? 51.385 -12.537 -21.552 0.40 30.49 ?  2   MET   B H    1 
ATOM   3663 H  HA   A MET   B 1 2   ? 49.040 -13.569 -22.374 0.60 31.81 ?  2   MET   B HA   1 
ATOM   3664 H  HA   B MET   B 1 2   ? 48.940 -13.534 -22.217 0.40 29.89 ?  2   MET   B HA   1 
ATOM   3665 H  HB2  A MET   B 1 2   ? 50.906 -14.628 -23.376 0.60 36.14 ?  2   MET   B HB2  1 
ATOM   3666 H  HB2  B MET   B 1 2   ? 51.027 -14.472 -23.043 0.40 32.29 ?  2   MET   B HB2  1 
ATOM   3667 H  HB3  A MET   B 1 2   ? 51.349 -15.129 -21.944 0.60 36.14 ?  2   MET   B HB3  1 
ATOM   3668 H  HB3  B MET   B 1 2   ? 51.121 -15.190 -21.649 0.40 32.29 ?  2   MET   B HB3  1 
ATOM   3669 H  HG2  A MET   B 1 2   ? 49.558 -16.492 -21.741 0.60 40.17 ?  2   MET   B HG2  1 
ATOM   3670 H  HG2  B MET   B 1 2   ? 49.364 -16.502 -21.985 0.40 34.34 ?  2   MET   B HG2  1 
ATOM   3671 H  HG3  A MET   B 1 2   ? 48.895 -15.904 -23.067 0.60 40.17 ?  2   MET   B HG3  1 
ATOM   3672 H  HG3  B MET   B 1 2   ? 48.864 -15.651 -23.231 0.40 34.34 ?  2   MET   B HG3  1 
ATOM   3673 H  HE1  A MET   B 1 2   ? 51.240 -16.965 -25.747 0.60 44.57 ?  2   MET   B HE1  1 
ATOM   3674 H  HE1  B MET   B 1 2   ? 51.654 -16.284 -25.654 0.40 36.90 ?  2   MET   B HE1  1 
ATOM   3675 H  HE2  A MET   B 1 2   ? 50.400 -15.741 -25.189 0.60 44.57 ?  2   MET   B HE2  1 
ATOM   3676 H  HE2  B MET   B 1 2   ? 50.875 -15.091 -24.991 0.40 36.90 ?  2   MET   B HE2  1 
ATOM   3677 H  HE3  A MET   B 1 2   ? 51.918 -15.932 -24.752 0.60 44.57 ?  2   MET   B HE3  1 
ATOM   3678 H  HE3  B MET   B 1 2   ? 52.249 -15.607 -24.350 0.40 36.90 ?  2   MET   B HE3  1 
ATOM   3679 N  N    A VAL   B 1 3   ? 48.377 -13.769 -20.016 0.60 20.82 ?  3   VAL   B N    1 
ATOM   3680 N  N    B VAL   B 1 3   ? 48.265 -13.520 -19.823 0.40 20.87 ?  3   VAL   B N    1 
ATOM   3681 C  CA   A VAL   B 1 3   ? 47.970 -14.008 -18.639 0.60 19.55 ?  3   VAL   B CA   1 
ATOM   3682 C  CA   B VAL   B 1 3   ? 47.817 -13.754 -18.456 0.40 19.45 ?  3   VAL   B CA   1 
ATOM   3683 C  C    A VAL   B 1 3   ? 46.732 -14.893 -18.652 0.60 17.56 ?  3   VAL   B C    1 
ATOM   3684 C  C    B VAL   B 1 3   ? 46.565 -14.616 -18.488 0.40 17.73 ?  3   VAL   B C    1 
ATOM   3685 O  O    A VAL   B 1 3   ? 46.039 -15.024 -19.664 0.60 17.00 ?  3   VAL   B O    1 
ATOM   3686 O  O    B VAL   B 1 3   ? 45.730 -14.491 -19.389 0.40 17.67 ?  3   VAL   B O    1 
ATOM   3687 C  CB   A VAL   B 1 3   ? 47.680 -12.699 -17.872 0.60 21.19 ?  3   VAL   B CB   1 
ATOM   3688 C  CB   B VAL   B 1 3   ? 47.568 -12.451 -17.666 0.40 20.03 ?  3   VAL   B CB   1 
ATOM   3689 C  CG1  A VAL   B 1 3   ? 48.940 -11.843 -17.762 0.60 21.75 ?  3   VAL   B CG1  1 
ATOM   3690 C  CG1  B VAL   B 1 3   ? 48.849 -11.633 -17.562 0.40 20.29 ?  3   VAL   B CG1  1 
ATOM   3691 C  CG2  A VAL   B 1 3   ? 46.552 -11.932 -18.547 0.60 21.90 ?  3   VAL   B CG2  1 
ATOM   3692 C  CG2  B VAL   B 1 3   ? 46.446 -11.641 -18.294 0.40 20.22 ?  3   VAL   B CG2  1 
ATOM   3693 H  H    A VAL   B 1 3   ? 47.725 -13.566 -20.536 0.60 25.15 ?  3   VAL   B H    1 
ATOM   3694 H  H    B VAL   B 1 3   ? 47.668 -13.172 -20.336 0.40 25.21 ?  3   VAL   B H    1 
ATOM   3695 H  HA   A VAL   B 1 3   ? 48.683 -14.482 -18.175 0.60 23.62 ?  3   VAL   B HA   1 
ATOM   3696 H  HA   B VAL   B 1 3   ? 48.498 -14.256 -17.992 0.40 23.51 ?  3   VAL   B HA   1 
ATOM   3697 H  HB   A VAL   B 1 3   ? 47.392 -12.928 -16.973 0.60 25.59 ?  3   VAL   B HB   1 
ATOM   3698 H  HB   B VAL   B 1 3   ? 47.295 -12.688 -16.766 0.40 24.20 ?  3   VAL   B HB   1 
ATOM   3699 H  HG11 A VAL   B 1 3   ? 48.726 -11.037 -17.268 0.60 26.26 ?  3   VAL   B HG11 1 
ATOM   3700 H  HG11 B VAL   B 1 3   ? 48.667 -10.832 -17.047 0.40 24.52 ?  3   VAL   B HG11 1 
ATOM   3701 H  HG12 A VAL   B 1 3   ? 49.623 -12.348 -17.293 0.60 26.26 ?  3   VAL   B HG12 1 
ATOM   3702 H  HG12 B VAL   B 1 3   ? 49.527 -12.166 -17.117 0.40 24.52 ?  3   VAL   B HG12 1 
ATOM   3703 H  HG13 A VAL   B 1 3   ? 49.245 -11.618 -18.653 0.60 26.26 ?  3   VAL   B HG13 1 
ATOM   3704 H  HG13 B VAL   B 1 3   ? 49.144 -11.396 -18.453 0.40 24.52 ?  3   VAL   B HG13 1 
ATOM   3705 H  HG21 A VAL   B 1 3   ? 46.479 -11.059 -18.137 0.60 26.44 ?  3   VAL   B HG21 1 
ATOM   3706 H  HG21 B VAL   B 1 3   ? 46.423 -10.766 -17.880 0.40 24.43 ?  3   VAL   B HG21 1 
ATOM   3707 H  HG22 A VAL   B 1 3   ? 46.751 -11.841 -19.491 0.60 26.44 ?  3   VAL   B HG22 1 
ATOM   3708 H  HG22 B VAL   B 1 3   ? 46.613 -11.556 -19.244 0.40 24.43 ?  3   VAL   B HG22 1 
ATOM   3709 H  HG23 A VAL   B 1 3   ? 45.720 -12.422 -18.432 0.60 26.44 ?  3   VAL   B HG23 1 
ATOM   3710 H  HG23 B VAL   B 1 3   ? 45.603 -12.100 -18.146 0.40 24.43 ?  3   VAL   B HG23 1 
ATOM   3711 N  N    . ASN   B 1 4   ? 46.449 -15.495 -17.498 1.00 16.43 ?  4   ASN   B N    1 
ATOM   3712 C  CA   . ASN   B 1 4   ? 45.312 -16.407 -17.369 1.00 15.39 ?  4   ASN   B CA   1 
ATOM   3713 C  C    . ASN   B 1 4   ? 45.253 -17.379 -18.543 1.00 15.90 ?  4   ASN   B C    1 
ATOM   3714 O  O    . ASN   B 1 4   ? 44.192 -17.635 -19.109 1.00 16.46 ?  4   ASN   B O    1 
ATOM   3715 C  CB   . ASN   B 1 4   ? 43.991 -15.652 -17.198 1.00 14.72 ?  4   ASN   B CB   1 
ATOM   3716 C  CG   . ASN   B 1 4   ? 43.951 -14.838 -15.921 1.00 14.22 ?  4   ASN   B CG   1 
ATOM   3717 O  OD1  . ASN   B 1 4   ? 44.247 -15.345 -14.841 1.00 13.91 ?  4   ASN   B OD1  1 
ATOM   3718 N  ND2  . ASN   B 1 4   ? 43.603 -13.559 -16.040 1.00 15.26 ?  4   ASN   B ND2  1 
ATOM   3719 H  H    A ASN   B 1 4   ? 46.895 -15.385 -16.776 0.60 19.88 ?  4   ASN   B H    1 
ATOM   3720 H  H    B ASN   B 1 4   ? 47.037 -15.589 -16.881 0.40 19.88 ?  4   ASN   B H    1 
ATOM   3721 H  HA   . ASN   B 1 4   ? 45.447 -16.935 -16.569 1.00 18.63 ?  4   ASN   B HA   1 
ATOM   3722 H  HB2  . ASN   B 1 4   ? 43.864 -15.050 -17.944 1.00 17.83 ?  4   ASN   B HB2  1 
ATOM   3723 H  HB3  . ASN   B 1 4   ? 43.264 -16.298 -17.166 1.00 17.83 ?  4   ASN   B HB3  1 
ATOM   3724 H  HD21 . ASN   B 1 4   ? 43.567 -13.053 -15.341 1.00 18.48 ?  4   ASN   B HD21 1 
ATOM   3725 H  HD22 . ASN   B 1 4   ? 43.408 -13.234 -16.811 1.00 18.48 ?  4   ASN   B HD22 1 
ATOM   3726 N  N    . SER   B 1 5   ? 46.414 -17.915 -18.920 1.00 17.10 ?  5   SER   B N    1 
ATOM   3727 C  CA   . SER   B 1 5   ? 46.517 -18.829 -20.057 1.00 19.29 ?  5   SER   B CA   1 
ATOM   3728 C  C    . SER   B 1 5   ? 46.504 -20.263 -19.540 1.00 20.90 ?  5   SER   B C    1 
ATOM   3729 O  O    . SER   B 1 5   ? 47.512 -20.964 -19.519 1.00 23.24 ?  5   SER   B O    1 
ATOM   3730 C  CB   . SER   B 1 5   ? 47.775 -18.531 -20.869 1.00 20.82 ?  5   SER   B CB   1 
ATOM   3731 O  OG   . SER   B 1 5   ? 48.947 -18.746 -20.101 1.00 23.38 ?  5   SER   B OG   1 
ATOM   3732 H  H    . SER   B 1 5   ? 47.165 -17.767 -18.529 1.00 20.69 ?  5   SER   B H    1 
ATOM   3733 H  HA   . SER   B 1 5   ? 45.751 -18.710 -20.636 1.00 23.32 ?  5   SER   B HA   1 
ATOM   3734 H  HB2  . SER   B 1 5   ? 47.792 -19.109 -21.651 1.00 25.15 ?  5   SER   B HB2  1 
ATOM   3735 H  HB3  . SER   B 1 5   ? 47.740 -17.604 -21.148 1.00 25.15 ?  5   SER   B HB3  1 
ATOM   3736 H  HG   . SER   B 1 5   ? 49.000 -19.556 -19.882 1.00 28.22 ?  5   SER   B HG   1 
ATOM   3737 N  N    . PHE   B 1 6   ? 45.322 -20.672 -19.092 1.00 21.17 ?  6   PHE   B N    1 
ATOM   3738 C  CA   . PHE   B 1 6   ? 45.113 -22.019 -18.584 1.00 20.93 ?  6   PHE   B CA   1 
ATOM   3739 C  C    . PHE   B 1 6   ? 45.029 -22.986 -19.754 1.00 24.22 ?  6   PHE   B C    1 
ATOM   3740 O  O    . PHE   B 1 6   ? 44.366 -22.699 -20.755 1.00 26.31 ?  6   PHE   B O    1 
ATOM   3741 C  CB   . PHE   B 1 6   ? 43.822 -22.066 -17.769 1.00 18.69 ?  6   PHE   B CB   1 
ATOM   3742 C  CG   . PHE   B 1 6   ? 43.852 -21.209 -16.535 1.00 16.85 ?  6   PHE   B CG   1 
ATOM   3743 C  CD1  . PHE   B 1 6   ? 44.366 -21.705 -15.353 1.00 15.78 ?  6   PHE   B CD1  1 
ATOM   3744 C  CD2  . PHE   B 1 6   ? 43.369 -19.904 -16.560 1.00 16.10 ?  6   PHE   B CD2  1 
ATOM   3745 C  CE1  . PHE   B 1 6   ? 44.391 -20.922 -14.210 1.00 15.53 ?  6   PHE   B CE1  1 
ATOM   3746 C  CE2  . PHE   B 1 6   ? 43.391 -19.117 -15.423 1.00 16.60 ?  6   PHE   B CE2  1 
ATOM   3747 C  CZ   . PHE   B 1 6   ? 43.910 -19.618 -14.249 1.00 15.70 ?  6   PHE   B CZ   1 
ATOM   3748 H  H    . PHE   B 1 6   ? 44.617 -20.184 -19.077 1.00 25.57 ?  6   PHE   B H    1 
ATOM   3749 H  HA   . PHE   B 1 6   ? 45.852 -22.281 -18.016 1.00 25.28 ?  6   PHE   B HA   1 
ATOM   3750 H  HB2  . PHE   B 1 6   ? 43.088 -21.761 -18.325 1.00 22.60 ?  6   PHE   B HB2  1 
ATOM   3751 H  HB3  . PHE   B 1 6   ? 43.660 -22.981 -17.487 1.00 22.60 ?  6   PHE   B HB3  1 
ATOM   3752 H  HD1  . PHE   B 1 6   ? 44.698 -22.574 -15.324 1.00 19.10 ?  6   PHE   B HD1  1 
ATOM   3753 H  HD2  . PHE   B 1 6   ? 43.016 -19.563 -17.349 1.00 19.49 ?  6   PHE   B HD2  1 
ATOM   3754 H  HE1  . PHE   B 1 6   ? 44.749 -21.263 -13.418 1.00 18.80 ?  6   PHE   B HE1  1 
ATOM   3755 H  HE2  . PHE   B 1 6   ? 43.063 -18.245 -15.451 1.00 20.09 ?  6   PHE   B HE2  1 
ATOM   3756 H  HZ   . PHE   B 1 6   ? 43.930 -19.094 -13.481 1.00 19.00 ?  6   PHE   B HZ   1 
ATOM   3757 N  N    . SER   B 1 7   ? 45.714 -24.123 -19.634 1.00 25.52 ?  7   SER   B N    1 
ATOM   3758 C  CA   . SER   B 1 7   ? 45.786 -25.101 -20.709 1.00 28.00 ?  7   SER   B CA   1 
ATOM   3759 C  C    . SER   B 1 7   ? 45.722 -26.507 -20.135 1.00 27.29 ?  7   SER   B C    1 
ATOM   3760 O  O    . SER   B 1 7   ? 46.330 -26.796 -19.100 1.00 27.98 ?  7   SER   B O    1 
ATOM   3761 C  CB   . SER   B 1 7   ? 47.081 -24.931 -21.517 1.00 30.78 ?  7   SER   B CB   1 
ATOM   3762 O  OG   . SER   B 1 7   ? 47.081 -25.762 -22.663 1.00 32.69 ?  7   SER   B OG   1 
ATOM   3763 H  H    . SER   B 1 7   ? 46.159 -24.348 -18.929 1.00 30.79 ?  7   SER   B H    1 
ATOM   3764 H  HA   . SER   B 1 7   ? 45.036 -24.981 -21.307 1.00 33.76 ?  7   SER   B HA   1 
ATOM   3765 H  HB2  . SER   B 1 7   ? 47.158 -24.005 -21.800 1.00 37.10 ?  7   SER   B HB2  1 
ATOM   3766 H  HB3  . SER   B 1 7   ? 47.838 -25.167 -20.957 1.00 37.10 ?  7   SER   B HB3  1 
ATOM   3767 H  HG   . SER   B 1 7   ? 47.796 -25.656 -23.095 1.00 39.39 ?  7   SER   B HG   1 
ATOM   3768 N  N    . GLY   B 1 8   ? 44.983 -27.379 -20.818 1.00 27.15 ?  8   GLY   B N    1 
ATOM   3769 C  CA   . GLY   B 1 8   ? 44.941 -28.776 -20.447 1.00 26.14 ?  8   GLY   B CA   1 
ATOM   3770 C  C    . GLY   B 1 8   ? 44.017 -29.107 -19.304 1.00 24.61 ?  8   GLY   B C    1 
ATOM   3771 O  O    . GLY   B 1 8   ? 44.162 -30.177 -18.699 1.00 25.89 ?  8   GLY   B O    1 
ATOM   3772 H  H    . GLY   B 1 8   ? 44.501 -27.176 -21.499 1.00 32.74 ?  8   GLY   B H    1 
ATOM   3773 H  HA2  . GLY   B 1 8   ? 44.654 -29.294 -21.212 1.00 31.53 ?  8   GLY   B HA2  1 
ATOM   3774 H  HA3  . GLY   B 1 8   ? 45.831 -29.065 -20.201 1.00 31.53 ?  8   GLY   B HA3  1 
ATOM   3775 N  N    . TYR   B 1 9   ? 43.050 -28.246 -19.002 1.00 22.58 ?  9   TYR   B N    1 
ATOM   3776 C  CA   . TYR   B 1 9   ? 42.108 -28.530 -17.934 1.00 20.39 ?  9   TYR   B CA   1 
ATOM   3777 C  C    . TYR   B 1 9   ? 40.927 -29.325 -18.453 1.00 20.16 ?  9   TYR   B C    1 
ATOM   3778 O  O    . TYR   B 1 9   ? 40.501 -29.179 -19.602 1.00 22.16 ?  9   TYR   B O    1 
ATOM   3779 C  CB   . TYR   B 1 9   ? 41.597 -27.251 -17.276 1.00 19.68 ?  9   TYR   B CB   1 
ATOM   3780 C  CG   . TYR   B 1 9   ? 42.626 -26.627 -16.367 1.00 18.91 ?  9   TYR   B CG   1 
ATOM   3781 C  CD1  . TYR   B 1 9   ? 43.715 -25.951 -16.894 1.00 19.49 ?  9   TYR   B CD1  1 
ATOM   3782 C  CD2  . TYR   B 1 9   ? 42.526 -26.732 -14.987 1.00 17.91 ?  9   TYR   B CD2  1 
ATOM   3783 C  CE1  . TYR   B 1 9   ? 44.674 -25.392 -16.076 1.00 19.61 ?  9   TYR   B CE1  1 
ATOM   3784 C  CE2  . TYR   B 1 9   ? 43.482 -26.173 -14.157 1.00 18.33 ?  9   TYR   B CE2  1 
ATOM   3785 C  CZ   . TYR   B 1 9   ? 44.555 -25.501 -14.711 1.00 19.32 ?  9   TYR   B CZ   1 
ATOM   3786 O  OH   . TYR   B 1 9   ? 45.515 -24.946 -13.900 1.00 20.18 ?  9   TYR   B OH   1 
ATOM   3787 H  H    . TYR   B 1 9   ? 42.900 -27.507 -19.416 1.00 27.26 ?  9   TYR   B H    1 
ATOM   3788 H  HA   . TYR   B 1 9   ? 42.540 -29.061 -17.255 1.00 24.64 ?  9   TYR   B HA   1 
ATOM   3789 H  HB2  . TYR   B 1 9   ? 41.355 -26.602 -17.957 1.00 23.78 ?  9   TYR   B HB2  1 
ATOM   3790 H  HB3  . TYR   B 1 9   ? 40.823 -27.475 -16.738 1.00 23.78 ?  9   TYR   B HB3  1 
ATOM   3791 H  HD1  . TYR   B 1 9   ? 43.797 -25.876 -17.818 1.00 23.55 ?  9   TYR   B HD1  1 
ATOM   3792 H  HD2  . TYR   B 1 9   ? 41.800 -27.189 -14.613 1.00 21.65 ?  9   TYR   B HD2  1 
ATOM   3793 H  HE1  . TYR   B 1 9   ? 45.391 -24.942 -16.448 1.00 23.69 ?  9   TYR   B HE1  1 
ATOM   3794 H  HE2  . TYR   B 1 9   ? 43.395 -26.254 -13.234 1.00 22.17 ?  9   TYR   B HE2  1 
ATOM   3795 H  HH   . TYR   B 1 9   ? 46.097 -24.573 -14.372 1.00 24.38 ?  9   TYR   B HH   1 
ATOM   3796 N  N    . LEU   B 1 10  ? 40.412 -30.184 -17.583 1.00 18.56 ?  10  LEU   B N    1 
ATOM   3797 C  CA   . LEU   B 1 10  ? 39.203 -30.941 -17.845 1.00 18.46 ?  10  LEU   B CA   1 
ATOM   3798 C  C    . LEU   B 1 10  ? 38.022 -30.166 -17.276 1.00 17.92 ?  10  LEU   B C    1 
ATOM   3799 O  O    . LEU   B 1 10  ? 38.048 -29.744 -16.117 1.00 17.48 ?  10  LEU   B O    1 
ATOM   3800 C  CB   . LEU   B 1 10  ? 39.310 -32.308 -17.170 1.00 19.24 ?  10  LEU   B CB   1 
ATOM   3801 C  CG   . LEU   B 1 10  ? 38.177 -33.278 -17.479 1.00 21.03 ?  10  LEU   B CG   1 
ATOM   3802 C  CD1  . LEU   B 1 10  ? 38.291 -33.790 -18.907 1.00 22.22 ?  10  LEU   B CD1  1 
ATOM   3803 C  CD2  . LEU   B 1 10  ? 38.176 -34.429 -16.488 1.00 22.12 ?  10  LEU   B CD2  1 
ATOM   3804 H  H    . LEU   B 1 10  ? 40.751 -30.348 -16.808 1.00 22.44 ?  10  LEU   B H    1 
ATOM   3805 H  HA   . LEU   B 1 10  ? 39.074 -31.066 -18.796 1.00 22.32 ?  10  LEU   B HA   1 
ATOM   3806 H  HB2  . LEU   B 1 10  ? 40.137 -32.730 -17.455 1.00 23.25 ?  10  LEU   B HB2  1 
ATOM   3807 H  HB3  . LEU   B 1 10  ? 39.328 -32.182 -16.207 1.00 23.25 ?  10  LEU   B HB3  1 
ATOM   3808 H  HG   . LEU   B 1 10  ? 37.329 -32.815 -17.394 1.00 25.40 ?  10  LEU   B HG   1 
ATOM   3809 H  HD11 . LEU   B 1 10  ? 37.593 -34.446 -19.063 1.00 26.83 ?  10  LEU   B HD11 1 
ATOM   3810 H  HD12 . LEU   B 1 10  ? 38.186 -33.044 -19.517 1.00 26.83 ?  10  LEU   B HD12 1 
ATOM   3811 H  HD13 . LEU   B 1 10  ? 39.161 -34.199 -19.027 1.00 26.83 ?  10  LEU   B HD13 1 
ATOM   3812 H  HD21 . LEU   B 1 10  ? 37.452 -35.033 -16.710 1.00 26.71 ?  10  LEU   B HD21 1 
ATOM   3813 H  HD22 . LEU   B 1 10  ? 39.025 -34.890 -16.543 1.00 26.71 ?  10  LEU   B HD22 1 
ATOM   3814 H  HD23 . LEU   B 1 10  ? 38.048 -34.071 -15.595 1.00 26.71 ?  10  LEU   B HD23 1 
ATOM   3815 N  N    . LYS   B 1 11  ? 36.990 -29.990 -18.090 1.00 19.12 ?  11  LYS   B N    1 
ATOM   3816 C  CA   . LYS   B 1 11  ? 35.797 -29.271 -17.669 1.00 21.38 ?  11  LYS   B CA   1 
ATOM   3817 C  C    . LYS   B 1 11  ? 34.920 -30.197 -16.833 1.00 20.61 ?  11  LYS   B C    1 
ATOM   3818 O  O    . LYS   B 1 11  ? 34.543 -31.282 -17.290 1.00 22.40 ?  11  LYS   B O    1 
ATOM   3819 C  CB   . LYS   B 1 11  ? 35.047 -28.796 -18.911 1.00 25.39 ?  11  LYS   B CB   1 
ATOM   3820 C  CG   . LYS   B 1 11  ? 33.920 -27.810 -18.662 1.00 28.95 ?  11  LYS   B CG   1 
ATOM   3821 C  CD   . LYS   B 1 11  ? 33.173 -27.530 -19.963 1.00 31.88 ?  11  LYS   B CD   1 
ATOM   3822 C  CE   . LYS   B 1 11  ? 32.130 -26.439 -19.803 1.00 34.11 ?  11  LYS   B CE   1 
ATOM   3823 N  NZ   . LYS   B 1 11  ? 32.752 -25.104 -19.598 1.00 35.36 ?  11  LYS   B NZ   1 
ATOM   3824 H  H    . LYS   B 1 11  ? 36.947 -30.293 -18.893 1.00 23.11 ?  11  LYS   B H    1 
ATOM   3825 H  HA   . LYS   B 1 11  ? 36.045 -28.505 -17.133 1.00 25.82 ?  11  LYS   B HA   1 
ATOM   3826 H  HB2  . LYS   B 1 11  ? 35.682 -28.365 -19.504 1.00 30.63 ?  11  LYS   B HB2  1 
ATOM   3827 H  HB3  . LYS   B 1 11  ? 34.663 -29.568 -19.354 1.00 30.63 ?  11  LYS   B HB3  1 
ATOM   3828 H  HG2  . LYS   B 1 11  ? 33.294 -28.186 -18.024 1.00 34.90 ?  11  LYS   B HG2  1 
ATOM   3829 H  HG3  . LYS   B 1 11  ? 34.285 -26.975 -18.331 1.00 34.90 ?  11  LYS   B HG3  1 
ATOM   3830 H  HD2  . LYS   B 1 11  ? 33.809 -27.245 -20.639 1.00 38.42 ?  11  LYS   B HD2  1 
ATOM   3831 H  HD3  . LYS   B 1 11  ? 32.723 -28.340 -20.252 1.00 38.42 ?  11  LYS   B HD3  1 
ATOM   3832 H  HE2  . LYS   B 1 11  ? 31.584 -26.399 -20.604 1.00 41.10 ?  11  LYS   B HE2  1 
ATOM   3833 H  HE3  . LYS   B 1 11  ? 31.578 -26.641 -19.032 1.00 41.10 ?  11  LYS   B HE3  1 
ATOM   3834 H  HZ1  . LYS   B 1 11  ? 32.120 -24.483 -19.520 1.00 42.60 ?  11  LYS   B HZ1  1 
ATOM   3835 H  HZ2  . LYS   B 1 11  ? 33.247 -25.109 -18.859 1.00 42.60 ?  11  LYS   B HZ2  1 
ATOM   3836 H  HZ3  . LYS   B 1 11  ? 33.271 -24.901 -20.293 1.00 42.60 ?  11  LYS   B HZ3  1 
ATOM   3837 N  N    . LEU   B 1 12  ? 34.593 -29.772 -15.612 1.00 18.70 ?  12  LEU   B N    1 
ATOM   3838 C  CA   . LEU   B 1 12  ? 33.634 -30.476 -14.766 1.00 17.95 ?  12  LEU   B CA   1 
ATOM   3839 C  C    . LEU   B 1 12  ? 32.244 -29.865 -14.849 1.00 17.77 ?  12  LEU   B C    1 
ATOM   3840 O  O    . LEU   B 1 12  ? 31.257 -30.581 -15.018 1.00 18.37 ?  12  LEU   B O    1 
ATOM   3841 C  CB   . LEU   B 1 12  ? 34.107 -30.500 -13.307 1.00 17.32 ?  12  LEU   B CB   1 
ATOM   3842 C  CG   . LEU   B 1 12  ? 35.452 -31.175 -13.049 1.00 17.13 ?  12  LEU   B CG   1 
ATOM   3843 C  CD1  . LEU   B 1 12  ? 35.804 -31.119 -11.576 1.00 17.17 ?  12  LEU   B CD1  1 
ATOM   3844 C  CD2  . LEU   B 1 12  ? 35.448 -32.620 -13.541 1.00 17.50 ?  12  LEU   B CD2  1 
ATOM   3845 H  H    . LEU   B 1 12  ? 34.914 -29.060 -15.247 1.00 22.60 ?  12  LEU   B H    1 
ATOM   3846 H  HA   . LEU   B 1 12  ? 33.558 -31.389 -15.071 1.00 21.71 ?  12  LEU   B HA   1 
ATOM   3847 H  HB2  . LEU   B 1 12  ? 34.175 -29.588 -12.992 1.00 20.95 ?  12  LEU   B HB2  1 
ATOM   3848 H  HB3  . LEU   B 1 12  ? 33.440 -30.973 -12.780 1.00 20.95 ?  12  LEU   B HB3  1 
ATOM   3849 H  HG   . LEU   B 1 12  ? 36.138 -30.698 -13.540 1.00 20.72 ?  12  LEU   B HG   1 
ATOM   3850 H  HD11 . LEU   B 1 12  ? 36.664 -31.551 -11.440 1.00 20.76 ?  12  LEU   B HD11 1 
ATOM   3851 H  HD12 . LEU   B 1 12  ? 35.855 -30.191 -11.297 1.00 20.76 ?  12  LEU   B HD12 1 
ATOM   3852 H  HD13 . LEU   B 1 12  ? 35.120 -31.580 -11.066 1.00 20.76 ?  12  LEU   B HD13 1 
ATOM   3853 H  HD21 . LEU   B 1 12  ? 36.265 -33.054 -13.251 1.00 21.17 ?  12  LEU   B HD21 1 
ATOM   3854 H  HD22 . LEU   B 1 12  ? 34.678 -33.079 -13.168 1.00 21.17 ?  12  LEU   B HD22 1 
ATOM   3855 H  HD23 . LEU   B 1 12  ? 35.396 -32.626 -14.511 1.00 21.17 ?  12  LEU   B HD23 1 
ATOM   3856 N  N    . THR   B 1 13  ? 32.156 -28.546 -14.732 1.00 17.82 ?  13  THR   B N    1 
ATOM   3857 C  CA   . THR   B 1 13  ? 30.929 -27.798 -14.939 1.00 17.63 ?  13  THR   B CA   1 
ATOM   3858 C  C    . THR   B 1 13  ? 31.264 -26.606 -15.826 1.00 19.62 ?  13  THR   B C    1 
ATOM   3859 O  O    . THR   B 1 13  ? 32.410 -26.421 -16.253 1.00 20.43 ?  13  THR   B O    1 
ATOM   3860 C  CB   . THR   B 1 13  ? 30.335 -27.319 -13.611 1.00 17.06 ?  13  THR   B CB   1 
ATOM   3861 O  OG1  . THR   B 1 13  ? 31.188 -26.301 -13.069 1.00 17.01 ?  13  THR   B OG1  1 
ATOM   3862 C  CG2  . THR   B 1 13  ? 30.221 -28.468 -12.617 1.00 17.85 ?  13  THR   B CG2  1 
ATOM   3863 H  H    . THR   B 1 13  ? 32.820 -28.043 -14.524 1.00 21.54 ?  13  THR   B H    1 
ATOM   3864 H  HA   . THR   B 1 13  ? 30.272 -28.355 -15.385 1.00 21.33 ?  13  THR   B HA   1 
ATOM   3865 H  HB   . THR   B 1 13  ? 29.442 -26.952 -13.760 1.00 20.63 ?  13  THR   B HB   1 
ATOM   3866 H  HG1  . THR   B 1 13  ? 30.875 -25.537 -13.246 1.00 20.58 ?  13  THR   B HG1  1 
ATOM   3867 H  HG21 . THR   B 1 13  ? 29.687 -28.199 -11.852 1.00 21.58 ?  13  THR   B HG21 1 
ATOM   3868 H  HG22 . THR   B 1 13  ? 29.795 -29.231 -13.041 1.00 21.58 ?  13  THR   B HG22 1 
ATOM   3869 H  HG23 . THR   B 1 13  ? 31.102 -28.730 -12.311 1.00 21.58 ?  13  THR   B HG23 1 
ATOM   3870 N  N    A ASP   B 1 14  ? 30.253 -25.783 -16.099 0.60 20.58 ?  14  ASP   B N    1 
ATOM   3871 N  N    B ASP   B 1 14  ? 30.257 -25.770 -16.088 0.40 20.40 ?  14  ASP   B N    1 
ATOM   3872 C  CA   A ASP   B 1 14  ? 30.475 -24.623 -16.954 0.60 21.91 ?  14  ASP   B CA   1 
ATOM   3873 C  CA   B ASP   B 1 14  ? 30.460 -24.614 -16.955 0.40 21.35 ?  14  ASP   B CA   1 
ATOM   3874 C  C    A ASP   B 1 14  ? 31.587 -23.728 -16.418 0.60 20.28 ?  14  ASP   B C    1 
ATOM   3875 C  C    B ASP   B 1 14  ? 31.459 -23.613 -16.388 0.40 19.82 ?  14  ASP   B C    1 
ATOM   3876 O  O    A ASP   B 1 14  ? 32.284 -23.074 -17.204 0.60 21.21 ?  14  ASP   B O    1 
ATOM   3877 O  O    B ASP   B 1 14  ? 31.907 -22.728 -17.126 0.40 20.27 ?  14  ASP   B O    1 
ATOM   3878 C  CB   A ASP   B 1 14  ? 29.174 -23.838 -17.127 0.60 25.38 ?  14  ASP   B CB   1 
ATOM   3879 C  CB   B ASP   B 1 14  ? 29.137 -23.893 -17.207 0.40 24.16 ?  14  ASP   B CB   1 
ATOM   3880 C  CG   A ASP   B 1 14  ? 28.204 -24.508 -18.077 0.60 28.71 ?  14  ASP   B CG   1 
ATOM   3881 C  CG   B ASP   B 1 14  ? 28.252 -24.633 -18.192 0.40 26.83 ?  14  ASP   B CG   1 
ATOM   3882 O  OD1  A ASP   B 1 14  ? 28.542 -25.569 -18.649 0.60 29.87 ?  14  ASP   B OD1  1 
ATOM   3883 O  OD1  B ASP   B 1 14  ? 28.799 -25.290 -19.104 0.40 27.78 ?  14  ASP   B OD1  1 
ATOM   3884 O  OD2  A ASP   B 1 14  ? 27.091 -23.969 -18.248 0.60 29.93 -1 14  ASP   B OD2  1 
ATOM   3885 O  OD2  B ASP   B 1 14  ? 27.013 -24.565 -18.053 0.40 27.66 -1 14  ASP   B OD2  1 
ATOM   3886 H  H    A ASP   B 1 14  ? 29.451 -25.865 -15.798 0.60 24.86 ?  14  ASP   B H    1 
ATOM   3887 H  H    B ASP   B 1 14  ? 29.457 -25.852 -15.780 0.40 24.64 ?  14  ASP   B H    1 
ATOM   3888 H  HA   A ASP   B 1 14  ? 30.754 -24.928 -17.827 0.60 26.46 ?  14  ASP   B HA   1 
ATOM   3889 H  HA   B ASP   B 1 14  ? 30.794 -24.927 -17.810 0.40 25.79 ?  14  ASP   B HA   1 
ATOM   3890 H  HB2  A ASP   B 1 14  ? 28.723 -23.767 -16.275 0.60 30.62 ?  14  ASP   B HB2  1 
ATOM   3891 H  HB2  B ASP   B 1 14  ? 28.657 -23.813 -16.368 0.40 29.15 ?  14  ASP   B HB2  1 
ATOM   3892 H  HB3  A ASP   B 1 14  ? 29.374 -22.957 -17.477 0.60 30.62 ?  14  ASP   B HB3  1 
ATOM   3893 H  HB3  B ASP   B 1 14  ? 29.331 -23.004 -17.559 0.40 29.15 ?  14  ASP   B HB3  1 
ATOM   3894 N  N    . ASN   B 1 15  ? 31.790 -23.701 -15.097 1.00 18.11 ?  15  ASN   B N    1 
ATOM   3895 C  CA   . ASN   B 1 15  ? 32.753 -22.781 -14.493 1.00 15.85 ?  15  ASN   B CA   1 
ATOM   3896 C  C    . ASN   B 1 15  ? 33.850 -23.436 -13.660 1.00 14.33 ?  15  ASN   B C    1 
ATOM   3897 O  O    . ASN   B 1 15  ? 34.696 -22.709 -13.125 1.00 14.08 ?  15  ASN   B O    1 
ATOM   3898 C  CB   . ASN   B 1 15  ? 32.037 -21.727 -13.631 1.00 16.06 ?  15  ASN   B CB   1 
ATOM   3899 C  CG   . ASN   B 1 15  ? 31.424 -22.326 -12.386 1.00 15.45 ?  15  ASN   B CG   1 
ATOM   3900 O  OD1  . ASN   B 1 15  ? 30.480 -23.123 -12.467 1.00 17.13 ?  15  ASN   B OD1  1 
ATOM   3901 N  ND2  . ASN   B 1 15  ? 31.953 -21.971 -11.229 1.00 14.54 ?  15  ASN   B ND2  1 
ATOM   3902 H  H    A ASN   B 1 15  ? 31.385 -24.215 -14.533 0.60 21.90 ?  15  ASN   B H    1 
ATOM   3903 H  H    B ASN   B 1 15  ? 31.440 -24.264 -14.544 0.40 21.90 ?  15  ASN   B H    1 
ATOM   3904 H  HA   . ASN   B 1 15  ? 33.195 -22.298 -15.200 1.00 19.18 ?  15  ASN   B HA   1 
ATOM   3905 H  HB2  . ASN   B 1 15  ? 32.682 -21.049 -13.358 1.00 19.44 ?  15  ASN   B HB2  1 
ATOM   3906 H  HB3  . ASN   B 1 15  ? 31.327 -21.312 -14.147 1.00 19.44 ?  15  ASN   B HB3  1 
ATOM   3907 H  HD21 . ASN   B 1 15  ? 31.639 -22.287 -10.491 1.00 17.61 ?  15  ASN   B HD21 1 
ATOM   3908 H  HD22 . ASN   B 1 15  ? 32.619 -21.419 -11.201 1.00 17.61 ?  15  ASN   B HD22 1 
ATOM   3909 N  N    . VAL   B 1 16  ? 33.865 -24.762 -13.519 1.00 14.27 ?  16  VAL   B N    1 
ATOM   3910 C  CA   . VAL   B 1 16  ? 34.865 -25.452 -12.708 1.00 14.19 ?  16  VAL   B CA   1 
ATOM   3911 C  C    . VAL   B 1 16  ? 35.658 -26.389 -13.603 1.00 14.25 ?  16  VAL   B C    1 
ATOM   3912 O  O    . VAL   B 1 16  ? 35.081 -27.271 -14.260 1.00 14.88 ?  16  VAL   B O    1 
ATOM   3913 C  CB   . VAL   B 1 16  ? 34.234 -26.218 -11.536 1.00 14.36 ?  16  VAL   B CB   1 
ATOM   3914 C  CG1  . VAL   B 1 16  ? 35.313 -26.946 -10.741 1.00 14.44 ?  16  VAL   B CG1  1 
ATOM   3915 C  CG2  . VAL   B 1 16  ? 33.435 -25.266 -10.650 1.00 15.04 ?  16  VAL   B CG2  1 
ATOM   3916 H  H    . VAL   B 1 16  ? 33.290 -25.293 -13.888 1.00 17.29 ?  16  VAL   B H    1 
ATOM   3917 H  HA   . VAL   B 1 16  ? 35.477 -24.798 -12.339 1.00 17.19 ?  16  VAL   B HA   1 
ATOM   3918 H  HB   . VAL   B 1 16  ? 33.622 -26.882 -11.888 1.00 17.40 ?  16  VAL   B HB   1 
ATOM   3919 H  HG11 . VAL   B 1 16  ? 34.933 -27.242 -9.898  1.00 17.49 ?  16  VAL   B HG11 1 
ATOM   3920 H  HG12 . VAL   B 1 16  ? 35.622 -27.711 -11.249 1.00 17.49 ?  16  VAL   B HG12 1 
ATOM   3921 H  HG13 . VAL   B 1 16  ? 36.048 -26.336 -10.574 1.00 17.49 ?  16  VAL   B HG13 1 
ATOM   3922 H  HG21 . VAL   B 1 16  ? 33.096 -25.757 -9.884  1.00 18.22 ?  16  VAL   B HG21 1 
ATOM   3923 H  HG22 . VAL   B 1 16  ? 34.012 -24.547 -10.354 1.00 18.22 ?  16  VAL   B HG22 1 
ATOM   3924 H  HG23 . VAL   B 1 16  ? 32.693 -24.904 -11.163 1.00 18.22 ?  16  VAL   B HG23 1 
ATOM   3925 N  N    . TYR   B 1 17  ? 36.981 -26.220 -13.586 1.00 14.43 ?  17  TYR   B N    1 
ATOM   3926 C  CA   . TYR   B 1 17  ? 37.926 -26.967 -14.397 1.00 14.84 ?  17  TYR   B CA   1 
ATOM   3927 C  C    . TYR   B 1 17  ? 38.977 -27.579 -13.481 1.00 13.83 ?  17  TYR   B C    1 
ATOM   3928 O  O    . TYR   B 1 17  ? 39.255 -27.051 -12.400 1.00 14.23 ?  17  TYR   B O    1 
ATOM   3929 C  CB   . TYR   B 1 17  ? 38.631 -26.031 -15.383 1.00 17.23 ?  17  TYR   B CB   1 
ATOM   3930 C  CG   . TYR   B 1 17  ? 37.701 -25.266 -16.293 1.00 20.53 ?  17  TYR   B CG   1 
ATOM   3931 C  CD1  . TYR   B 1 17  ? 37.125 -24.067 -15.889 1.00 22.28 ?  17  TYR   B CD1  1 
ATOM   3932 C  CD2  . TYR   B 1 17  ? 37.401 -25.743 -17.561 1.00 22.72 ?  17  TYR   B CD2  1 
ATOM   3933 C  CE1  . TYR   B 1 17  ? 36.269 -23.367 -16.725 1.00 23.82 ?  17  TYR   B CE1  1 
ATOM   3934 C  CE2  . TYR   B 1 17  ? 36.553 -25.051 -18.403 1.00 24.10 ?  17  TYR   B CE2  1 
ATOM   3935 C  CZ   . TYR   B 1 17  ? 35.989 -23.866 -17.980 1.00 25.01 ?  17  TYR   B CZ   1 
ATOM   3936 O  OH   . TYR   B 1 17  ? 35.146 -23.177 -18.819 1.00 26.25 ?  17  TYR   B OH   1 
ATOM   3937 H  H    . TYR   B 1 17  ? 37.372 -25.639 -13.081 1.00 17.48 ?  17  TYR   B H    1 
ATOM   3938 H  HA   . TYR   B 1 17  ? 37.469 -27.671 -14.886 1.00 17.97 ?  17  TYR   B HA   1 
ATOM   3939 H  HB2  . TYR   B 1 17  ? 39.157 -25.387 -14.883 1.00 20.85 ?  17  TYR   B HB2  1 
ATOM   3940 H  HB3  . TYR   B 1 17  ? 39.208 -26.560 -15.946 1.00 20.85 ?  17  TYR   B HB3  1 
ATOM   3941 H  HD1  . TYR   B 1 17  ? 37.312 -23.730 -15.043 1.00 26.90 ?  17  TYR   B HD1  1 
ATOM   3942 H  HD2  . TYR   B 1 17  ? 37.775 -26.543 -17.849 1.00 27.43 ?  17  TYR   B HD2  1 
ATOM   3943 H  HE1  . TYR   B 1 17  ? 35.889 -22.564 -16.444 1.00 28.74 ?  17  TYR   B HE1  1 
ATOM   3944 H  HE2  . TYR   B 1 17  ? 36.357 -25.384 -19.251 1.00 29.08 ?  17  TYR   B HE2  1 
ATOM   3945 H  HH   . TYR   B 1 17  ? 35.059 -23.585 -19.549 1.00 31.66 ?  17  TYR   B HH   1 
ATOM   3946 N  N    . ILE   B 1 18  ? 39.582 -28.686 -13.915 1.00 13.67 ?  18  ILE   B N    1 
ATOM   3947 C  CA   . ILE   B 1 18  ? 40.511 -29.410 -13.054 1.00 13.75 ?  18  ILE   B CA   1 
ATOM   3948 C  C    . ILE   B 1 18  ? 41.672 -29.964 -13.873 1.00 14.28 ?  18  ILE   B C    1 
ATOM   3949 O  O    . ILE   B 1 18  ? 41.513 -30.356 -15.034 1.00 15.46 ?  18  ILE   B O    1 
ATOM   3950 C  CB   . ILE   B 1 18  ? 39.758 -30.506 -12.251 1.00 14.46 ?  18  ILE   B CB   1 
ATOM   3951 C  CG1  . ILE   B 1 18  ? 40.617 -31.055 -11.108 1.00 14.96 ?  18  ILE   B CG1  1 
ATOM   3952 C  CG2  . ILE   B 1 18  ? 39.253 -31.626 -13.176 1.00 14.99 ?  18  ILE   B CG2  1 
ATOM   3953 C  CD1  . ILE   B 1 18  ? 39.810 -31.853 -10.092 1.00 16.41 ?  18  ILE   B CD1  1 
ATOM   3954 H  H    . ILE   B 1 18  ? 39.471 -29.032 -14.693 1.00 16.57 ?  18  ILE   B H    1 
ATOM   3955 H  HA   . ILE   B 1 18  ? 40.874 -28.792 -12.406 1.00 16.67 ?  18  ILE   B HA   1 
ATOM   3956 H  HB   . ILE   B 1 18  ? 38.976 -30.095 -11.847 1.00 17.52 ?  18  ILE   B HB   1 
ATOM   3957 H  HG12 . ILE   B 1 18  ? 41.298 -31.635 -11.473 1.00 18.12 ?  18  ILE   B HG12 1 
ATOM   3958 H  HG13 . ILE   B 1 18  ? 41.029 -30.308 -10.641 1.00 18.12 ?  18  ILE   B HG13 1 
ATOM   3959 H  HG21 . ILE   B 1 18  ? 38.667 -32.213 -12.672 1.00 18.16 ?  18  ILE   B HG21 1 
ATOM   3960 H  HG22 . ILE   B 1 18  ? 38.764 -31.224 -13.911 1.00 18.16 ?  18  ILE   B HG22 1 
ATOM   3961 H  HG23 . ILE   B 1 18  ? 40.012 -32.123 -13.513 1.00 18.16 ?  18  ILE   B HG23 1 
ATOM   3962 H  HD11 . ILE   B 1 18  ? 40.396 -32.129 -9.370  1.00 19.86 ?  18  ILE   B HD11 1 
ATOM   3963 H  HD12 . ILE   B 1 18  ? 39.098 -31.292 -9.742  1.00 19.86 ?  18  ILE   B HD12 1 
ATOM   3964 H  HD13 . ILE   B 1 18  ? 39.433 -32.631 -10.530 1.00 19.86 ?  18  ILE   B HD13 1 
ATOM   3965 N  N    . LYS   B 1 19  ? 42.853 -29.998 -13.252 1.00 14.71 ?  19  LYS   B N    1 
ATOM   3966 C  CA   . LYS   B 1 19  ? 44.067 -30.466 -13.906 1.00 15.73 ?  19  LYS   B CA   1 
ATOM   3967 C  C    . LYS   B 1 19  ? 44.962 -31.147 -12.883 1.00 15.39 ?  19  LYS   B C    1 
ATOM   3968 O  O    . LYS   B 1 19  ? 45.050 -30.713 -11.733 1.00 15.04 ?  19  LYS   B O    1 
ATOM   3969 C  CB   . LYS   B 1 19  ? 44.845 -29.299 -14.532 1.00 17.15 ?  19  LYS   B CB   1 
ATOM   3970 C  CG   . LYS   B 1 19  ? 46.022 -29.711 -15.399 1.00 19.13 ?  19  LYS   B CG   1 
ATOM   3971 C  CD   . LYS   B 1 19  ? 46.758 -28.481 -15.915 1.00 20.96 ?  19  LYS   B CD   1 
ATOM   3972 C  CE   . LYS   B 1 19  ? 47.921 -28.860 -16.810 1.00 22.91 ?  19  LYS   B CE   1 
ATOM   3973 N  NZ   . LYS   B 1 19  ? 48.676 -27.669 -17.280 1.00 23.77 ?  19  LYS   B NZ   1 
ATOM   3974 H  H    . LYS   B 1 19  ? 42.966 -29.744 -12.436 1.00 17.81 ?  19  LYS   B H    1 
ATOM   3975 H  HA   . LYS   B 1 19  ? 43.834 -31.100 -14.601 1.00 19.03 ?  19  LYS   B HA   1 
ATOM   3976 H  HB2  . LYS   B 1 19  ? 44.236 -28.789 -15.088 1.00 20.74 ?  19  LYS   B HB2  1 
ATOM   3977 H  HB3  . LYS   B 1 19  ? 45.182 -28.734 -13.816 1.00 20.74 ?  19  LYS   B HB3  1 
ATOM   3978 H  HG2  . LYS   B 1 19  ? 46.635 -30.246 -14.873 1.00 23.12 ?  19  LYS   B HG2  1 
ATOM   3979 H  HG3  . LYS   B 1 19  ? 45.693 -30.220 -16.159 1.00 23.12 ?  19  LYS   B HG3  1 
ATOM   3980 H  HD2  . LYS   B 1 19  ? 46.142 -27.933 -16.428 1.00 25.32 ?  19  LYS   B HD2  1 
ATOM   3981 H  HD3  . LYS   B 1 19  ? 47.103 -27.978 -15.160 1.00 25.32 ?  19  LYS   B HD3  1 
ATOM   3982 H  HE2  . LYS   B 1 19  ? 48.529 -29.430 -16.314 1.00 27.65 ?  19  LYS   B HE2  1 
ATOM   3983 H  HE3  . LYS   B 1 19  ? 47.581 -29.333 -17.587 1.00 27.65 ?  19  LYS   B HE3  1 
ATOM   3984 H  HZ1  . LYS   B 1 19  ? 49.296 -27.916 -17.870 1.00 28.68 ?  19  LYS   B HZ1  1 
ATOM   3985 H  HZ2  . LYS   B 1 19  ? 48.122 -27.092 -17.670 1.00 28.68 ?  19  LYS   B HZ2  1 
ATOM   3986 H  HZ3  . LYS   B 1 19  ? 49.074 -27.269 -16.593 1.00 28.68 ?  19  LYS   B HZ3  1 
ATOM   3987 N  N    . ASN   B 1 20  ? 45.644 -32.202 -13.317 1.00 16.52 ?  20  ASN   B N    1 
ATOM   3988 C  CA   . ASN   B 1 20  ? 46.678 -32.837 -12.504 1.00 17.64 ?  20  ASN   B CA   1 
ATOM   3989 C  C    . ASN   B 1 20  ? 47.951 -32.017 -12.689 1.00 18.16 ?  20  ASN   B C    1 
ATOM   3990 O  O    . ASN   B 1 20  ? 48.596 -32.084 -13.739 1.00 20.07 ?  20  ASN   B O    1 
ATOM   3991 C  CB   . ASN   B 1 20  ? 46.851 -34.288 -12.945 1.00 19.43 ?  20  ASN   B CB   1 
ATOM   3992 C  CG   . ASN   B 1 20  ? 48.014 -34.994 -12.265 1.00 20.99 ?  20  ASN   B CG   1 
ATOM   3993 O  OD1  . ASN   B 1 20  ? 48.683 -35.834 -12.878 1.00 23.12 ?  20  ASN   B OD1  1 
ATOM   3994 N  ND2  . ASN   B 1 20  ? 48.254 -34.677 -11.002 1.00 20.50 ?  20  ASN   B ND2  1 
ATOM   3995 H  H    . ASN   B 1 20  ? 45.525 -32.571 -14.085 1.00 19.99 ?  20  ASN   B H    1 
ATOM   3996 H  HA   . ASN   B 1 20  ? 46.407 -32.819 -11.570 1.00 21.33 ?  20  ASN   B HA   1 
ATOM   3997 H  HB2  . ASN   B 1 20  ? 46.039 -34.779 -12.734 1.00 23.48 ?  20  ASN   B HB2  1 
ATOM   3998 H  HB3  . ASN   B 1 20  ? 47.003 -34.303 -13.902 1.00 23.48 ?  20  ASN   B HB3  1 
ATOM   3999 H  HD21 . ASN   B 1 20  ? 48.904 -35.049 -10.585 1.00 24.76 ?  20  ASN   B HD21 1 
ATOM   4000 H  HD22 . ASN   B 1 20  ? 47.764 -34.092 -10.599 1.00 24.76 ?  20  ASN   B HD22 1 
ATOM   4001 N  N    . ALA   B 1 21  ? 48.311 -31.223 -11.677 1.00 17.55 ?  21  ALA   B N    1 
ATOM   4002 C  CA   . ALA   B 1 21  ? 49.424 -30.298 -11.825 1.00 18.10 ?  21  ALA   B CA   1 
ATOM   4003 C  C    . ALA   B 1 21  ? 49.883 -29.795 -10.465 1.00 17.22 ?  21  ALA   B C    1 
ATOM   4004 O  O    . ALA   B 1 21  ? 49.139 -29.815 -9.481  1.00 16.99 ?  21  ALA   B O    1 
ATOM   4005 C  CB   . ALA   B 1 21  ? 49.037 -29.127 -12.727 1.00 19.37 ?  21  ALA   B CB   1 
ATOM   4006 H  H    . ALA   B 1 21  ? 47.925 -31.205 -10.902 1.00 21.23 ?  21  ALA   B H    1 
ATOM   4007 H  HA   . ALA   B 1 21  ? 50.163 -30.771 -12.234 1.00 21.88 ?  21  ALA   B HA   1 
ATOM   4008 H  HB1  . ALA   B 1 21  ? 49.826 -28.600 -12.888 1.00 23.41 ?  21  ALA   B HB1  1 
ATOM   4009 H  HB2  . ALA   B 1 21  ? 48.695 -29.486 -13.561 1.00 23.41 ?  21  ALA   B HB2  1 
ATOM   4010 H  HB3  . ALA   B 1 21  ? 48.354 -28.605 -12.284 1.00 23.41 ?  21  ALA   B HB3  1 
ATOM   4011 N  N    . ASP   B 1 22  ? 51.141 -29.354 -10.443 1.00 16.60 ?  22  ASP   B N    1 
ATOM   4012 C  CA   . ASP   B 1 22  ? 51.754 -28.655 -9.318  1.00 15.98 ?  22  ASP   B CA   1 
ATOM   4013 C  C    . ASP   B 1 22  ? 51.348 -27.184 -9.401  1.00 14.58 ?  22  ASP   B C    1 
ATOM   4014 O  O    . ASP   B 1 22  ? 51.657 -26.511 -10.390 1.00 14.63 ?  22  ASP   B O    1 
ATOM   4015 C  CB   . ASP   B 1 22  ? 53.271 -28.835 -9.469  1.00 17.06 ?  22  ASP   B CB   1 
ATOM   4016 C  CG   . ASP   B 1 22  ? 54.097 -28.070 -8.442  1.00 18.75 ?  22  ASP   B CG   1 
ATOM   4017 O  OD1  . ASP   B 1 22  ? 53.729 -26.952 -8.046  1.00 18.56 ?  22  ASP   B OD1  1 
ATOM   4018 O  OD2  . ASP   B 1 22  ? 55.170 -28.587 -8.057  1.00 21.01 -1 22  ASP   B OD2  1 
ATOM   4019 H  H    . ASP   B 1 22  ? 51.683 -29.457 -11.105 1.00 20.08 ?  22  ASP   B H    1 
ATOM   4020 H  HA   . ASP   B 1 22  ? 51.461 -29.038 -8.473  1.00 19.34 ?  22  ASP   B HA   1 
ATOM   4021 H  HB2  . ASP   B 1 22  ? 53.490 -29.772 -9.385  1.00 20.64 ?  22  ASP   B HB2  1 
ATOM   4022 H  HB3  . ASP   B 1 22  ? 53.536 -28.508 -10.343 1.00 20.64 ?  22  ASP   B HB3  1 
ATOM   4023 N  N    . ILE   B 1 23  ? 50.637 -26.690 -8.380  1.00 13.65 ?  23  ILE   B N    1 
ATOM   4024 C  CA   . ILE   B 1 23  ? 50.049 -25.349 -8.451  1.00 12.92 ?  23  ILE   B CA   1 
ATOM   4025 C  C    . ILE   B 1 23  ? 51.107 -24.260 -8.588  1.00 12.44 ?  23  ILE   B C    1 
ATOM   4026 O  O    . ILE   B 1 23  ? 50.843 -23.215 -9.190  1.00 12.06 ?  23  ILE   B O    1 
ATOM   4027 C  CB   . ILE   B 1 23  ? 49.108 -25.102 -7.255  1.00 13.09 ?  23  ILE   B CB   1 
ATOM   4028 C  CG1  . ILE   B 1 23  ? 48.285 -23.825 -7.458  1.00 13.80 ?  23  ILE   B CG1  1 
ATOM   4029 C  CG2  . ILE   B 1 23  ? 49.874 -25.078 -5.943  1.00 13.87 ?  23  ILE   B CG2  1 
ATOM   4030 C  CD1  . ILE   B 1 23  ? 47.142 -23.678 -6.461  1.00 14.43 ?  23  ILE   B CD1  1 
ATOM   4031 H  H    . ILE   B 1 23  ? 50.485 -27.110 -7.644  1.00 16.55 ?  23  ILE   B H    1 
ATOM   4032 H  HA   . ILE   B 1 23  ? 49.502 -25.312 -9.249  1.00 15.67 ?  23  ILE   B HA   1 
ATOM   4033 H  HB   . ILE   B 1 23  ? 48.483 -25.844 -7.218  1.00 15.87 ?  23  ILE   B HB   1 
ATOM   4034 H  HG12 . ILE   B 1 23  ? 48.871 -23.056 -7.358  1.00 16.72 ?  23  ILE   B HG12 1 
ATOM   4035 H  HG13 . ILE   B 1 23  ? 47.906 -23.833 -8.353  1.00 16.72 ?  23  ILE   B HG13 1 
ATOM   4036 H  HG21 . ILE   B 1 23  ? 49.243 -25.057 -5.208  1.00 16.80 ?  23  ILE   B HG21 1 
ATOM   4037 H  HG22 . ILE   B 1 23  ? 50.422 -25.879 -5.885  1.00 16.80 ?  23  ILE   B HG22 1 
ATOM   4038 H  HG23 . ILE   B 1 23  ? 50.439 -24.291 -5.921  1.00 16.80 ?  23  ILE   B HG23 1 
ATOM   4039 H  HD11 . ILE   B 1 23  ? 46.625 -22.890 -6.690  1.00 17.49 ?  23  ILE   B HD11 1 
ATOM   4040 H  HD12 . ILE   B 1 23  ? 46.580 -24.468 -6.513  1.00 17.49 ?  23  ILE   B HD12 1 
ATOM   4041 H  HD13 . ILE   B 1 23  ? 47.510 -23.589 -5.571  1.00 17.49 ?  23  ILE   B HD13 1 
ATOM   4042 N  N    . VAL   B 1 24  ? 52.301 -24.465 -8.028  1.00 12.73 ?  24  VAL   B N    1 
ATOM   4043 C  CA   . VAL   B 1 24  ? 53.375 -23.487 -8.193  1.00 13.30 ?  24  VAL   B CA   1 
ATOM   4044 C  C    . VAL   B 1 24  ? 53.830 -23.444 -9.644  1.00 13.45 ?  24  VAL   B C    1 
ATOM   4045 O  O    . VAL   B 1 24  ? 53.969 -22.367 -10.238 1.00 13.93 ?  24  VAL   B O    1 
ATOM   4046 C  CB   . VAL   B 1 24  ? 54.550 -23.803 -7.248  1.00 14.61 ?  24  VAL   B CB   1 
ATOM   4047 C  CG1  . VAL   B 1 24  ? 55.753 -22.916 -7.570  1.00 15.31 ?  24  VAL   B CG1  1 
ATOM   4048 C  CG2  . VAL   B 1 24  ? 54.132 -23.633 -5.807  1.00 15.70 ?  24  VAL   B CG2  1 
ATOM   4049 H  H    . VAL   B 1 24  ? 52.511 -25.152 -7.557  1.00 15.45 ?  24  VAL   B H    1 
ATOM   4050 H  HA   . VAL   B 1 24  ? 53.038 -22.610 -7.963  1.00 16.13 ?  24  VAL   B HA   1 
ATOM   4051 H  HB   . VAL   B 1 24  ? 54.818 -24.728 -7.374  1.00 17.69 ?  24  VAL   B HB   1 
ATOM   4052 H  HG11 . VAL   B 1 24  ? 56.339 -22.890 -6.797  1.00 18.54 ?  24  VAL   B HG11 1 
ATOM   4053 H  HG12 . VAL   B 1 24  ? 56.225 -23.288 -8.329  1.00 18.54 ?  24  VAL   B HG12 1 
ATOM   4054 H  HG13 . VAL   B 1 24  ? 55.438 -22.020 -7.775  1.00 18.54 ?  24  VAL   B HG13 1 
ATOM   4055 H  HG21 . VAL   B 1 24  ? 54.857 -23.919 -5.231  1.00 19.00 ?  24  VAL   B HG21 1 
ATOM   4056 H  HG22 . VAL   B 1 24  ? 53.929 -22.699 -5.646  1.00 19.00 ?  24  VAL   B HG22 1 
ATOM   4057 H  HG23 . VAL   B 1 24  ? 53.344 -24.177 -5.639  1.00 19.00 ?  24  VAL   B HG23 1 
ATOM   4058 N  N    . GLU   B 1 25  ? 54.089 -24.616 -10.232 1.00 14.51 ?  25  GLU   B N    1 
ATOM   4059 C  CA   . GLU   B 1 25  ? 54.482 -24.655 -11.635 1.00 15.88 ?  25  GLU   B CA   1 
ATOM   4060 C  C    . GLU   B 1 25  ? 53.373 -24.109 -12.522 1.00 14.67 ?  25  GLU   B C    1 
ATOM   4061 O  O    . GLU   B 1 25  ? 53.639 -23.399 -13.502 1.00 15.77 ?  25  GLU   B O    1 
ATOM   4062 C  CB   . GLU   B 1 25  ? 54.869 -26.078 -12.030 1.00 19.66 ?  25  GLU   B CB   1 
ATOM   4063 C  CG   . GLU   B 1 25  ? 56.163 -26.542 -11.377 1.00 25.29 ?  25  GLU   B CG   1 
ATOM   4064 C  CD   . GLU   B 1 25  ? 57.286 -25.521 -11.480 1.00 30.37 ?  25  GLU   B CD   1 
ATOM   4065 O  OE1  . GLU   B 1 25  ? 57.655 -25.150 -12.615 1.00 32.24 ?  25  GLU   B OE1  1 
ATOM   4066 O  OE2  . GLU   B 1 25  ? 57.794 -25.073 -10.425 1.00 32.04 -1 25  GLU   B OE2  1 
ATOM   4067 H  H    . GLU   B 1 25  ? 54.041 -25.387 -9.845  1.00 17.58 ?  25  GLU   B H    1 
ATOM   4068 H  HA   . GLU   B 1 25  ? 55.243 -24.076 -11.759 1.00 19.22 ?  25  GLU   B HA   1 
ATOM   4069 H  HB2  . GLU   B 1 25  ? 54.164 -26.689 -11.755 1.00 23.76 ?  25  GLU   B HB2  1 
ATOM   4070 H  HB3  . GLU   B 1 25  ? 54.984 -26.120 -12.992 1.00 23.76 ?  25  GLU   B HB3  1 
ATOM   4071 H  HG2  . GLU   B 1 25  ? 56.007 -26.701 -10.438 1.00 30.52 ?  25  GLU   B HG2  1 
ATOM   4072 H  HG3  . GLU   B 1 25  ? 56.467 -27.351 -11.815 1.00 30.52 ?  25  GLU   B HG3  1 
ATOM   4073 N  N    A GLU   B 1 26  ? 52.119 -24.417 -12.188 0.60 14.11 ?  26  GLU   B N    1 
ATOM   4074 N  N    B GLU   B 1 26  ? 52.118 -24.420 -12.187 0.40 14.24 ?  26  GLU   B N    1 
ATOM   4075 C  CA   A GLU   B 1 26  ? 50.998 -23.890 -12.957 0.60 14.58 ?  26  GLU   B CA   1 
ATOM   4076 C  CA   B GLU   B 1 26  ? 50.992 -23.896 -12.953 0.40 14.56 ?  26  GLU   B CA   1 
ATOM   4077 C  C    A GLU   B 1 26  ? 50.949 -22.373 -12.880 0.60 13.88 ?  26  GLU   B C    1 
ATOM   4078 C  C    B GLU   B 1 26  ? 50.941 -22.377 -12.879 0.40 13.81 ?  26  GLU   B C    1 
ATOM   4079 O  O    A GLU   B 1 26  ? 50.757 -21.698 -13.896 0.60 15.21 ?  26  GLU   B O    1 
ATOM   4080 O  O    B GLU   B 1 26  ? 50.743 -21.703 -13.895 0.40 14.65 ?  26  GLU   B O    1 
ATOM   4081 C  CB   A GLU   B 1 26  ? 49.685 -24.477 -12.443 0.60 16.30 ?  26  GLU   B CB   1 
ATOM   4082 C  CB   B GLU   B 1 26  ? 49.680 -24.489 -12.436 0.40 15.98 ?  26  GLU   B CB   1 
ATOM   4083 C  CG   A GLU   B 1 26  ? 49.331 -25.816 -13.040 0.60 19.15 ?  26  GLU   B CG   1 
ATOM   4084 C  CG   B GLU   B 1 26  ? 49.210 -25.724 -13.182 0.40 18.20 ?  26  GLU   B CG   1 
ATOM   4085 C  CD   A GLU   B 1 26  ? 49.131 -25.768 -14.547 0.60 20.01 ?  26  GLU   B CD   1 
ATOM   4086 C  CD   B GLU   B 1 26  ? 48.855 -25.433 -14.639 0.40 18.49 ?  26  GLU   B CD   1 
ATOM   4087 O  OE1  A GLU   B 1 26  ? 48.317 -24.949 -15.024 0.60 19.74 ?  26  GLU   B OE1  1 
ATOM   4088 O  OE1  B GLU   B 1 26  ? 47.731 -24.958 -14.917 0.40 18.76 ?  26  GLU   B OE1  1 
ATOM   4089 O  OE2  A GLU   B 1 26  ? 49.793 -26.554 -15.253 0.60 21.47 -1 26  GLU   B OE2  1 
ATOM   4090 O  OE2  B GLU   B 1 26  ? 49.711 -25.668 -15.508 0.40 18.55 -1 26  GLU   B OE2  1 
ATOM   4091 H  H    A GLU   B 1 26  ? 51.892 -24.923 -11.527 0.60 17.10 ?  26  GLU   B H    1 
ATOM   4092 H  H    B GLU   B 1 26  ? 51.894 -24.929 -11.527 0.40 17.26 ?  26  GLU   B H    1 
ATOM   4093 H  HA   A GLU   B 1 26  ? 51.103 -24.141 -13.885 0.60 17.65 ?  26  GLU   B HA   1 
ATOM   4094 H  HA   B GLU   B 1 26  ? 51.098 -24.147 -13.881 0.40 17.64 ?  26  GLU   B HA   1 
ATOM   4095 H  HB2  A GLU   B 1 26  ? 49.748 -24.589 -11.480 0.60 19.72 ?  26  GLU   B HB2  1 
ATOM   4096 H  HB2  B GLU   B 1 26  ? 49.792 -24.729 -11.503 0.40 19.34 ?  26  GLU   B HB2  1 
ATOM   4097 H  HB3  A GLU   B 1 26  ? 48.965 -23.856 -12.649 0.60 19.72 ?  26  GLU   B HB3  1 
ATOM   4098 H  HB3  B GLU   B 1 26  ? 48.984 -23.818 -12.518 0.40 19.34 ?  26  GLU   B HB3  1 
ATOM   4099 H  HG2  A GLU   B 1 26  ? 50.055 -26.425 -12.869 0.60 23.15 ?  26  GLU   B HG2  1 
ATOM   4100 H  HG2  B GLU   B 1 26  ? 49.913 -26.395 -13.131 0.40 22.00 ?  26  GLU   B HG2  1 
ATOM   4101 H  HG3  A GLU   B 1 26  ? 48.512 -26.131 -12.627 0.60 23.15 ?  26  GLU   B HG3  1 
ATOM   4102 H  HG3  B GLU   B 1 26  ? 48.405 -26.056 -12.761 0.40 22.00 ?  26  GLU   B HG3  1 
ATOM   4103 N  N    . ALA   B 1 27  ? 51.095 -21.820 -11.675 1.00 13.12 ?  27  ALA   B N    1 
ATOM   4104 C  CA   . ALA   B 1 27  ? 51.054 -20.371 -11.528 1.00 13.54 ?  27  ALA   B CA   1 
ATOM   4105 C  C    . ALA   B 1 27  ? 52.122 -19.708 -12.385 1.00 14.26 ?  27  ALA   B C    1 
ATOM   4106 O  O    . ALA   B 1 27  ? 51.857 -18.705 -13.062 1.00 15.02 ?  27  ALA   B O    1 
ATOM   4107 C  CB   . ALA   B 1 27  ? 51.219 -19.990 -10.057 1.00 13.56 ?  27  ALA   B CB   1 
ATOM   4108 H  H    A ALA   B 1 27  ? 51.210 -22.253 -10.940 0.60 15.91 ?  27  ALA   B H    1 
ATOM   4109 H  H    B ALA   B 1 27  ? 51.217 -22.252 -10.941 0.40 15.91 ?  27  ALA   B H    1 
ATOM   4110 H  HA   . ALA   B 1 27  ? 50.196 -20.042 -11.824 1.00 16.41 ?  27  ALA   B HA   1 
ATOM   4111 H  HB1  . ALA   B 1 27  ? 51.185 -19.024 -9.973  1.00 16.43 ?  27  ALA   B HB1  1 
ATOM   4112 H  HB2  . ALA   B 1 27  ? 50.492 -20.389 -9.548  1.00 16.43 ?  27  ALA   B HB2  1 
ATOM   4113 H  HB3  . ALA   B 1 27  ? 52.069 -20.323 -9.733  1.00 16.43 ?  27  ALA   B HB3  1 
ATOM   4114 N  N    . LYS   B 1 28  ? 53.337 -20.261 -12.381 1.00 15.64 ?  28  LYS   B N    1 
ATOM   4115 C  CA   . LYS   B 1 28  ? 54.416 -19.648 -13.147 1.00 17.73 ?  28  LYS   B CA   1 
ATOM   4116 C  C    . LYS   B 1 28  ? 54.166 -19.731 -14.647 1.00 18.59 ?  28  LYS   B C    1 
ATOM   4117 O  O    . LYS   B 1 28  ? 54.581 -18.832 -15.390 1.00 20.23 ?  28  LYS   B O    1 
ATOM   4118 C  CB   . LYS   B 1 28  ? 55.765 -20.255 -12.754 1.00 20.80 ?  28  LYS   B CB   1 
ATOM   4119 C  CG   . LYS   B 1 28  ? 56.165 -19.912 -11.323 1.00 23.96 ?  28  LYS   B CG   1 
ATOM   4120 C  CD   . LYS   B 1 28  ? 57.593 -20.307 -10.988 1.00 28.45 ?  28  LYS   B CD   1 
ATOM   4121 C  CE   . LYS   B 1 28  ? 57.696 -21.758 -10.590 1.00 32.69 ?  28  LYS   B CE   1 
ATOM   4122 N  NZ   . LYS   B 1 28  ? 59.054 -22.078 -10.066 1.00 34.74 ?  28  LYS   B NZ   1 
ATOM   4123 H  H    . LYS   B 1 28  ? 53.559 -20.974 -11.951 1.00 18.93 ?  28  LYS   B H    1 
ATOM   4124 H  HA   . LYS   B 1 28  ? 54.454 -18.709 -12.921 1.00 21.44 ?  28  LYS   B HA   1 
ATOM   4125 H  HB2  . LYS   B 1 28  ? 55.714 -21.221 -12.826 1.00 25.12 ?  28  LYS   B HB2  1 
ATOM   4126 H  HB3  . LYS   B 1 28  ? 56.453 -19.913 -13.347 1.00 25.12 ?  28  LYS   B HB3  1 
ATOM   4127 H  HG2  . LYS   B 1 28  ? 56.079 -18.952 -11.198 1.00 28.92 ?  28  LYS   B HG2  1 
ATOM   4128 H  HG3  . LYS   B 1 28  ? 55.571 -20.376 -10.713 1.00 28.92 ?  28  LYS   B HG3  1 
ATOM   4129 H  HD2  . LYS   B 1 28  ? 58.150 -20.162 -11.768 1.00 34.31 ?  28  LYS   B HD2  1 
ATOM   4130 H  HD3  . LYS   B 1 28  ? 57.903 -19.762 -10.248 1.00 34.31 ?  28  LYS   B HD3  1 
ATOM   4131 H  HE2  . LYS   B 1 28  ? 57.047 -21.946 -9.893  1.00 39.39 ?  28  LYS   B HE2  1 
ATOM   4132 H  HE3  . LYS   B 1 28  ? 57.527 -22.318 -11.365 1.00 39.39 ?  28  LYS   B HE3  1 
ATOM   4133 H  HZ1  . LYS   B 1 28  ? 59.098 -22.936 -9.836  1.00 41.85 ?  28  LYS   B HZ1  1 
ATOM   4134 H  HZ2  . LYS   B 1 28  ? 59.666 -21.913 -10.691 1.00 41.85 ?  28  LYS   B HZ2  1 
ATOM   4135 H  HZ3  . LYS   B 1 28  ? 59.229 -21.577 -9.351  1.00 41.85 ?  28  LYS   B HZ3  1 
ATOM   4136 N  N    . LYS   B 1 29  ? 53.467 -20.768 -15.107 1.00 19.84 ?  29  LYS   B N    1 
ATOM   4137 C  CA   . LYS   B 1 29  ? 53.176 -20.911 -16.530 1.00 22.55 ?  29  LYS   B CA   1 
ATOM   4138 C  C    . LYS   B 1 29  ? 51.923 -20.152 -16.961 1.00 21.41 ?  29  LYS   B C    1 
ATOM   4139 O  O    . LYS   B 1 29  ? 51.920 -19.524 -18.025 1.00 22.72 ?  29  LYS   B O    1 
ATOM   4140 C  CB   . LYS   B 1 29  ? 53.028 -22.393 -16.887 1.00 27.35 ?  29  LYS   B CB   1 
ATOM   4141 C  CG   . LYS   B 1 29  ? 52.862 -22.658 -18.375 1.00 32.04 ?  29  LYS   B CG   1 
ATOM   4142 C  CD   . LYS   B 1 29  ? 53.095 -24.126 -18.707 1.00 35.74 ?  29  LYS   B CD   1 
ATOM   4143 C  CE   . LYS   B 1 29  ? 52.037 -25.025 -18.082 1.00 38.15 ?  29  LYS   B CE   1 
ATOM   4144 N  NZ   . LYS   B 1 29  ? 52.272 -26.463 -18.407 1.00 39.85 ?  29  LYS   B NZ   1 
ATOM   4145 H  H    . LYS   B 1 29  ? 53.152 -21.405 -14.614 1.00 23.97 ?  29  LYS   B H    1 
ATOM   4146 H  HA   . LYS   B 1 29  ? 53.924 -20.561 -17.036 1.00 27.22 ?  29  LYS   B HA   1 
ATOM   4147 H  HB2  . LYS   B 1 29  ? 53.823 -22.866 -16.592 1.00 32.99 ?  29  LYS   B HB2  1 
ATOM   4148 H  HB3  . LYS   B 1 29  ? 52.249 -22.747 -16.436 1.00 32.99 ?  29  LYS   B HB3  1 
ATOM   4149 H  HG2  . LYS   B 1 29  ? 51.959 -22.424 -18.643 1.00 38.62 ?  29  LYS   B HG2  1 
ATOM   4150 H  HG3  . LYS   B 1 29  ? 53.507 -22.127 -18.871 1.00 38.62 ?  29  LYS   B HG3  1 
ATOM   4151 H  HD2  . LYS   B 1 29  ? 53.063 -24.245 -19.669 1.00 43.05 ?  29  LYS   B HD2  1 
ATOM   4152 H  HD3  . LYS   B 1 29  ? 53.962 -24.396 -18.366 1.00 43.05 ?  29  LYS   B HD3  1 
ATOM   4153 H  HE2  . LYS   B 1 29  ? 52.060 -24.926 -17.117 1.00 45.95 ?  29  LYS   B HE2  1 
ATOM   4154 H  HE3  . LYS   B 1 29  ? 51.164 -24.774 -18.423 1.00 45.95 ?  29  LYS   B HE3  1 
ATOM   4155 H  HZ1  . LYS   B 1 29  ? 51.642 -26.967 -18.031 1.00 47.99 ?  29  LYS   B HZ1  1 
ATOM   4156 H  HZ2  . LYS   B 1 29  ? 52.250 -26.584 -19.289 1.00 47.99 ?  29  LYS   B HZ2  1 
ATOM   4157 H  HZ3  . LYS   B 1 29  ? 53.067 -26.719 -18.100 1.00 47.99 ?  29  LYS   B HZ3  1 
ATOM   4158 N  N    . VAL   B 1 30  ? 50.855 -20.213 -16.160 1.00 19.67 ?  30  VAL   B N    1 
ATOM   4159 C  CA   . VAL   B 1 30  ? 49.565 -19.619 -16.524 1.00 19.64 ?  30  VAL   B CA   1 
ATOM   4160 C  C    . VAL   B 1 30  ? 49.572 -18.104 -16.379 1.00 18.53 ?  30  VAL   B C    1 
ATOM   4161 O  O    . VAL   B 1 30  ? 48.831 -17.400 -17.084 1.00 19.74 ?  30  VAL   B O    1 
ATOM   4162 C  CB   . VAL   B 1 30  ? 48.465 -20.228 -15.632 1.00 20.79 ?  30  VAL   B CB   1 
ATOM   4163 C  CG1  . VAL   B 1 30  ? 47.180 -19.406 -15.701 1.00 21.16 ?  30  VAL   B CG1  1 
ATOM   4164 C  CG2  . VAL   B 1 30  ? 48.216 -21.680 -16.010 1.00 21.78 ?  30  VAL   B CG2  1 
ATOM   4165 H  H    . VAL   B 1 30  ? 50.842 -20.622 -15.394 1.00 23.77 ?  30  VAL   B H    1 
ATOM   4166 H  HA   . VAL   B 1 30  ? 49.358 -19.856 -17.445 1.00 23.74 ?  30  VAL   B HA   1 
ATOM   4167 H  HB   . VAL   B 1 30  ? 48.766 -20.219 -14.709 1.00 25.11 ?  30  VAL   B HB   1 
ATOM   4168 H  HG11 . VAL   B 1 30  ? 46.435 -19.978 -15.459 1.00 25.56 ?  30  VAL   B HG11 1 
ATOM   4169 H  HG12 . VAL   B 1 30  ? 47.239 -18.666 -15.078 1.00 25.56 ?  30  VAL   B HG12 1 
ATOM   4170 H  HG13 . VAL   B 1 30  ? 47.057 -19.083 -16.603 1.00 25.56 ?  30  VAL   B HG13 1 
ATOM   4171 H  HG21 . VAL   B 1 30  ? 47.524 -22.047 -15.432 1.00 26.29 ?  30  VAL   B HG21 1 
ATOM   4172 H  HG22 . VAL   B 1 30  ? 47.922 -21.720 -16.935 1.00 26.29 ?  30  VAL   B HG22 1 
ATOM   4173 H  HG23 . VAL   B 1 30  ? 49.036 -22.182 -15.901 1.00 26.29 ?  30  VAL   B HG23 1 
ATOM   4174 N  N    . LYS   B 1 31  ? 50.354 -17.593 -15.440 1.00 18.02 ?  31  LYS   B N    1 
ATOM   4175 C  CA   . LYS   B 1 31  ? 50.380 -16.178 -15.096 1.00 18.75 ?  31  LYS   B CA   1 
ATOM   4176 C  C    . LYS   B 1 31  ? 48.981 -15.702 -14.699 1.00 16.59 ?  31  LYS   B C    1 
ATOM   4177 O  O    . LYS   B 1 31  ? 48.441 -14.777 -15.321 1.00 17.58 ?  31  LYS   B O    1 
ATOM   4178 C  CB   . LYS   B 1 31  ? 51.004 -15.368 -16.242 1.00 21.87 ?  31  LYS   B CB   1 
ATOM   4179 C  CG   . LYS   B 1 31  ? 52.454 -15.779 -16.554 1.00 24.95 ?  31  LYS   B CG   1 
ATOM   4180 C  CD   . LYS   B 1 31  ? 53.041 -14.979 -17.706 1.00 28.45 ?  31  LYS   B CD   1 
ATOM   4181 C  CE   . LYS   B 1 31  ? 54.526 -15.245 -17.877 1.00 31.54 ?  31  LYS   B CE   1 
ATOM   4182 N  NZ   . LYS   B 1 31  ? 55.293 -14.870 -16.654 1.00 33.37 ?  31  LYS   B NZ   1 
ATOM   4183 H  H    . LYS   B 1 31  ? 50.899 -18.072 -14.979 1.00 21.79 ?  31  LYS   B H    1 
ATOM   4184 H  HA   . LYS   B 1 31  ? 50.947 -16.077 -14.330 1.00 22.67 ?  31  LYS   B HA   1 
ATOM   4185 H  HB2  . LYS   B 1 31  ? 50.481 -15.496 -17.051 1.00 26.41 ?  31  LYS   B HB2  1 
ATOM   4186 H  HB3  . LYS   B 1 31  ? 51.007 -14.433 -15.995 1.00 26.41 ?  31  LYS   B HB3  1 
ATOM   4187 H  HG2  . LYS   B 1 31  ? 53.001 -15.628 -15.767 1.00 30.10 ?  31  LYS   B HG2  1 
ATOM   4188 H  HG3  . LYS   B 1 31  ? 52.476 -16.720 -16.797 1.00 30.10 ?  31  LYS   B HG3  1 
ATOM   4189 H  HD2  . LYS   B 1 31  ? 52.591 -15.231 -18.526 1.00 34.31 ?  31  LYS   B HD2  1 
ATOM   4190 H  HD3  . LYS   B 1 31  ? 52.920 -14.036 -17.529 1.00 34.31 ?  31  LYS   B HD3  1 
ATOM   4191 H  HE2  . LYS   B 1 31  ? 54.670 -16.191 -18.047 1.00 38.02 ?  31  LYS   B HE2  1 
ATOM   4192 H  HE3  . LYS   B 1 31  ? 54.864 -14.718 -18.620 1.00 38.02 ?  31  LYS   B HE3  1 
ATOM   4193 H  HZ1  . LYS   B 1 31  ? 56.167 -14.939 -16.807 1.00 40.21 ?  31  LYS   B HZ1  1 
ATOM   4194 H  HZ2  . LYS   B 1 31  ? 55.105 -14.031 -16.424 1.00 40.21 ?  31  LYS   B HZ2  1 
ATOM   4195 H  HZ3  . LYS   B 1 31  ? 55.075 -15.409 -15.980 1.00 40.21 ?  31  LYS   B HZ3  1 
ATOM   4196 N  N    . PRO   B 1 32  ? 48.375 -16.290 -13.662 1.00 14.29 ?  32  PRO   B N    1 
ATOM   4197 C  CA   . PRO   B 1 32  ? 46.998 -15.931 -13.305 1.00 13.44 ?  32  PRO   B CA   1 
ATOM   4198 C  C    . PRO   B 1 32  ? 46.923 -14.588 -12.595 1.00 13.49 ?  32  PRO   B C    1 
ATOM   4199 O  O    . PRO   B 1 32  ? 47.848 -14.171 -11.895 1.00 14.75 ?  32  PRO   B O    1 
ATOM   4200 C  CB   . PRO   B 1 32  ? 46.595 -17.050 -12.339 1.00 13.83 ?  32  PRO   B CB   1 
ATOM   4201 C  CG   . PRO   B 1 32  ? 47.893 -17.388 -11.652 1.00 13.83 ?  32  PRO   B CG   1 
ATOM   4202 C  CD   . PRO   B 1 32  ? 48.954 -17.261 -12.711 1.00 13.98 ?  32  PRO   B CD   1 
ATOM   4203 H  HA   . PRO   B 1 32  ? 46.417 -15.938 -14.088 1.00 16.29 ?  32  PRO   B HA   1 
ATOM   4204 H  HB2  . PRO   B 1 32  ? 45.936 -16.721 -11.705 1.00 16.77 ?  32  PRO   B HB2  1 
ATOM   4205 H  HB3  . PRO   B 1 32  ? 46.251 -17.812 -12.832 1.00 16.77 ?  32  PRO   B HB3  1 
ATOM   4206 H  HG2  . PRO   B 1 32  ? 48.054 -16.757 -10.929 1.00 16.76 ?  32  PRO   B HG2  1 
ATOM   4207 H  HG3  . PRO   B 1 32  ? 47.861 -18.294 -11.311 1.00 16.76 ?  32  PRO   B HG3  1 
ATOM   4208 H  HD2  . PRO   B 1 32  ? 49.770 -16.903 -12.331 1.00 16.94 ?  32  PRO   B HD2  1 
ATOM   4209 H  HD3  . PRO   B 1 32  ? 49.099 -18.109 -13.146 1.00 16.94 ?  32  PRO   B HD3  1 
ATOM   4210 N  N    . THR   B 1 33  ? 45.771 -13.930 -12.762 1.00 13.14 ?  33  THR   B N    1 
ATOM   4211 C  CA   . THR   B 1 33  ? 45.471 -12.754 -11.952 1.00 13.08 ?  33  THR   B CA   1 
ATOM   4212 C  C    . THR   B 1 33  ? 45.429 -13.108 -10.471 1.00 13.01 ?  33  THR   B C    1 
ATOM   4213 O  O    . THR   B 1 33  ? 45.905 -12.331 -9.627  1.00 13.80 ?  33  THR   B O    1 
ATOM   4214 C  CB   . THR   B 1 33  ? 44.150 -12.121 -12.400 1.00 13.70 ?  33  THR   B CB   1 
ATOM   4215 O  OG1  . THR   B 1 33  ? 44.194 -11.857 -13.806 1.00 13.86 ?  33  THR   B OG1  1 
ATOM   4216 C  CG2  . THR   B 1 33  ? 43.902 -10.826 -11.646 1.00 15.41 ?  33  THR   B CG2  1 
ATOM   4217 H  H    . THR   B 1 33  ? 45.152 -14.149 -13.326 1.00 15.93 ?  33  THR   B H    1 
ATOM   4218 H  HA   . THR   B 1 33  ? 46.168 -12.102 -12.081 1.00 15.86 ?  33  THR   B HA   1 
ATOM   4219 H  HB   . THR   B 1 33  ? 43.415 -12.732 -12.210 1.00 16.61 ?  33  THR   B HB   1 
ATOM   4220 H  HG1  . THR   B 1 33  ? 43.470 -11.498 -14.057 1.00 16.80 ?  33  THR   B HG1  1 
ATOM   4221 H  HG21 . THR   B 1 33  ? 43.154 -10.353 -12.035 1.00 18.66 ?  33  THR   B HG21 1 
ATOM   4222 H  HG22 . THR   B 1 33  ? 43.708 -11.014 -10.714 1.00 18.66 ?  33  THR   B HG22 1 
ATOM   4223 H  HG23 . THR   B 1 33  ? 44.692 -10.263 -11.695 1.00 18.66 ?  33  THR   B HG23 1 
ATOM   4224 N  N    . VAL   B 1 34  ? 44.874 -14.278 -10.134 1.00 12.17 ?  34  VAL   B N    1 
ATOM   4225 C  CA   . VAL   B 1 34  ? 44.676 -14.673 -8.743  1.00 11.67 ?  34  VAL   B CA   1 
ATOM   4226 C  C    . VAL   B 1 34  ? 45.108 -16.121 -8.569  1.00 10.65 ?  34  VAL   B C    1 
ATOM   4227 O  O    . VAL   B 1 34  ? 44.588 -17.011 -9.253  1.00 11.49 ?  34  VAL   B O    1 
ATOM   4228 C  CB   . VAL   B 1 34  ? 43.204 -14.527 -8.301  1.00 12.54 ?  34  VAL   B CB   1 
ATOM   4229 C  CG1  . VAL   B 1 34  ? 43.028 -14.988 -6.862  1.00 13.00 ?  34  VAL   B CG1  1 
ATOM   4230 C  CG2  . VAL   B 1 34  ? 42.705 -13.099 -8.487  1.00 13.83 ?  34  VAL   B CG2  1 
ATOM   4231 H  H    . VAL   B 1 34  ? 44.613 -14.876 -10.702 1.00 14.77 ?  34  VAL   B H    1 
ATOM   4232 H  HA   . VAL   B 1 34  ? 45.222 -14.119 -8.166  1.00 14.17 ?  34  VAL   B HA   1 
ATOM   4233 H  HB   . VAL   B 1 34  ? 42.656 -15.101 -8.864  1.00 15.22 ?  34  VAL   B HB   1 
ATOM   4234 H  HG11 . VAL   B 1 34  ? 42.171 -14.673 -6.532  1.00 15.77 ?  34  VAL   B HG11 1 
ATOM   4235 H  HG12 . VAL   B 1 34  ? 43.050 -15.960 -6.832  1.00 15.77 ?  34  VAL   B HG12 1 
ATOM   4236 H  HG13 . VAL   B 1 34  ? 43.744 -14.623 -6.322  1.00 15.77 ?  34  VAL   B HG13 1 
ATOM   4237 H  HG21 . VAL   B 1 34  ? 41.784 -13.042 -8.185  1.00 16.76 ?  34  VAL   B HG21 1 
ATOM   4238 H  HG22 . VAL   B 1 34  ? 43.261 -12.499 -7.968  1.00 16.76 ?  34  VAL   B HG22 1 
ATOM   4239 H  HG23 . VAL   B 1 34  ? 42.755 -12.863 -9.429  1.00 16.76 ?  34  VAL   B HG23 1 
ATOM   4240 N  N    . VAL   B 1 35  ? 46.013 -16.369 -7.625  1.00 10.24 ?  35  VAL   B N    1 
ATOM   4241 C  CA   . VAL   B 1 35  ? 46.239 -17.712 -7.105  1.00 10.10 ?  35  VAL   B CA   1 
ATOM   4242 C  C    . VAL   B 1 35  ? 45.700 -17.768 -5.685  1.00 9.74  ?  35  VAL   B C    1 
ATOM   4243 O  O    . VAL   B 1 35  ? 45.919 -16.843 -4.896  1.00 10.21 ?  35  VAL   B O    1 
ATOM   4244 C  CB   . VAL   B 1 35  ? 47.723 -18.141 -7.186  1.00 11.01 ?  35  VAL   B CB   1 
ATOM   4245 C  CG1  . VAL   B 1 35  ? 48.622 -17.299 -6.268  1.00 11.82 ?  35  VAL   B CG1  1 
ATOM   4246 C  CG2  . VAL   B 1 35  ? 47.870 -19.638 -6.870  1.00 11.43 ?  35  VAL   B CG2  1 
ATOM   4247 H  H    . VAL   B 1 35  ? 46.521 -15.771 -7.274  1.00 12.46 ?  35  VAL   B H    1 
ATOM   4248 H  HA   . VAL   B 1 35  ? 45.729 -18.344 -7.634  1.00 12.29 ?  35  VAL   B HA   1 
ATOM   4249 H  HB   . VAL   B 1 35  ? 48.033 -18.009 -8.096  1.00 13.38 ?  35  VAL   B HB   1 
ATOM   4250 H  HG11 . VAL   B 1 35  ? 49.546 -17.523 -6.444  1.00 14.34 ?  35  VAL   B HG11 1 
ATOM   4251 H  HG12 . VAL   B 1 35  ? 48.460 -16.363 -6.450  1.00 14.34 ?  35  VAL   B HG12 1 
ATOM   4252 H  HG13 . VAL   B 1 35  ? 48.401 -17.502 -5.344  1.00 14.34 ?  35  VAL   B HG13 1 
ATOM   4253 H  HG21 . VAL   B 1 35  ? 48.797 -19.901 -6.971  1.00 13.89 ?  35  VAL   B HG21 1 
ATOM   4254 H  HG22 . VAL   B 1 35  ? 47.575 -19.807 -5.960  1.00 13.89 ?  35  VAL   B HG22 1 
ATOM   4255 H  HG23 . VAL   B 1 35  ? 47.317 -20.152 -7.489  1.00 13.89 ?  35  VAL   B HG23 1 
ATOM   4256 N  N    . VAL   B 1 36  ? 44.978 -18.845 -5.369  1.00 9.79  ?  36  VAL   B N    1 
ATOM   4257 C  CA   . VAL   B 1 36  ? 44.434 -19.052 -4.036  1.00 9.58  ?  36  VAL   B CA   1 
ATOM   4258 C  C    . VAL   B 1 36  ? 45.442 -19.814 -3.185  1.00 9.45  ?  36  VAL   B C    1 
ATOM   4259 O  O    . VAL   B 1 36  ? 45.987 -20.841 -3.610  1.00 10.52 ?  36  VAL   B O    1 
ATOM   4260 C  CB   . VAL   B 1 36  ? 43.105 -19.819 -4.117  1.00 10.02 ?  36  VAL   B CB   1 
ATOM   4261 C  CG1  . VAL   B 1 36  ? 42.596 -20.171 -2.729  1.00 10.81 ?  36  VAL   B CG1  1 
ATOM   4262 C  CG2  . VAL   B 1 36  ? 42.078 -18.989 -4.873  1.00 10.74 ?  36  VAL   B CG2  1 
ATOM   4263 H  H    . VAL   B 1 36  ? 44.797 -19.479 -5.919  1.00 11.91 ?  36  VAL   B H    1 
ATOM   4264 H  HA   . VAL   B 1 36  ? 44.265 -18.194 -3.616  1.00 11.66 ?  36  VAL   B HA   1 
ATOM   4265 H  HB   . VAL   B 1 36  ? 43.241 -20.643 -4.608  1.00 12.19 ?  36  VAL   B HB   1 
ATOM   4266 H  HG11 . VAL   B 1 36  ? 41.655 -20.405 -2.789  1.00 13.14 ?  36  VAL   B HG11 1 
ATOM   4267 H  HG12 . VAL   B 1 36  ? 43.101 -20.921 -2.385  1.00 13.14 ?  36  VAL   B HG12 1 
ATOM   4268 H  HG13 . VAL   B 1 36  ? 42.703 -19.399 -2.149  1.00 13.14 ?  36  VAL   B HG13 1 
ATOM   4269 H  HG21 . VAL   B 1 36  ? 41.234 -19.468 -4.894  1.00 13.06 ?  36  VAL   B HG21 1 
ATOM   4270 H  HG22 . VAL   B 1 36  ? 41.963 -18.138 -4.423  1.00 13.06 ?  36  VAL   B HG22 1 
ATOM   4271 H  HG23 . VAL   B 1 36  ? 42.392 -18.842 -5.781  1.00 13.06 ?  36  VAL   B HG23 1 
ATOM   4272 N  N    . ASN   B 1 37  ? 45.664 -19.326 -1.970  1.00 9.68  ?  37  ASN   B N    1 
ATOM   4273 C  CA   . ASN   B 1 37  ? 46.417 -20.052 -0.960  1.00 10.07 ?  37  ASN   B CA   1 
ATOM   4274 C  C    . ASN   B 1 37  ? 45.467 -20.722 0.025   1.00 10.12 ?  37  ASN   B C    1 
ATOM   4275 O  O    . ASN   B 1 37  ? 44.460 -20.139 0.438   1.00 10.67 ?  37  ASN   B O    1 
ATOM   4276 C  CB   . ASN   B 1 37  ? 47.349 -19.104 -0.204  1.00 10.19 ?  37  ASN   B CB   1 
ATOM   4277 C  CG   . ASN   B 1 37  ? 48.201 -19.816 0.811   1.00 10.47 ?  37  ASN   B CG   1 
ATOM   4278 O  OD1  . ASN   B 1 37  ? 48.537 -20.994 0.637   1.00 11.08 ?  37  ASN   B OD1  1 
ATOM   4279 N  ND2  . ASN   B 1 37  ? 48.548 -19.118 1.889   1.00 10.73 ?  37  ASN   B ND2  1 
ATOM   4280 H  H    . ASN   B 1 37  ? 45.393 -18.557 -1.696  1.00 11.78 ?  37  ASN   B H    1 
ATOM   4281 H  HA   . ASN   B 1 37  ? 46.953 -20.744 -1.376  1.00 12.25 ?  37  ASN   B HA   1 
ATOM   4282 H  HB2  . ASN   B 1 37  ? 47.947 -18.680 -0.835  1.00 12.39 ?  37  ASN   B HB2  1 
ATOM   4283 H  HB3  . ASN   B 1 37  ? 46.827 -18.443 0.267   1.00 12.39 ?  37  ASN   B HB3  1 
ATOM   4284 H  HD21 . ASN   B 1 37  ? 49.042 -19.480 2.500   1.00 13.04 ?  37  ASN   B HD21 1 
ATOM   4285 H  HD22 . ASN   B 1 37  ? 48.299 -18.307 1.977   1.00 13.04 ?  37  ASN   B HD22 1 
ATOM   4286 N  N    . ALA   B 1 38  ? 45.815 -21.953 0.403   1.00 10.52 ?  38  ALA   B N    1 
ATOM   4287 C  CA   . ALA   B 1 38  ? 45.163 -22.698 1.481   1.00 10.79 ?  38  ALA   B CA   1 
ATOM   4288 C  C    . ALA   B 1 38  ? 45.753 -22.209 2.802   1.00 10.41 ?  38  ALA   B C    1 
ATOM   4289 O  O    . ALA   B 1 38  ? 46.653 -22.819 3.387   1.00 11.48 ?  38  ALA   B O    1 
ATOM   4290 C  CB   . ALA   B 1 38  ? 45.384 -24.192 1.290   1.00 11.96 ?  38  ALA   B CB   1 
ATOM   4291 H  H    . ALA   B 1 38  ? 46.464 -22.389 0.051   1.00 12.79 ?  38  ALA   B H    1 
ATOM   4292 H  HA   . ALA   B 1 38  ? 44.208 -22.516 1.480   1.00 13.11 ?  38  ALA   B HA   1 
ATOM   4293 H  HB1  . ALA   B 1 38  ? 44.938 -24.674 2.014   1.00 14.52 ?  38  ALA   B HB1  1 
ATOM   4294 H  HB2  . ALA   B 1 38  ? 45.001 -24.463 0.441   1.00 14.52 ?  38  ALA   B HB2  1 
ATOM   4295 H  HB3  . ALA   B 1 38  ? 46.330 -24.382 1.308   1.00 14.52 ?  38  ALA   B HB3  1 
ATOM   4296 N  N    . ALA   B 1 39  ? 45.236 -21.067 3.260   1.00 10.33 ?  39  ALA   B N    1 
ATOM   4297 C  CA   . ALA   B 1 39  ? 45.785 -20.333 4.389   1.00 10.59 ?  39  ALA   B CA   1 
ATOM   4298 C  C    . ALA   B 1 39  ? 45.167 -20.777 5.712   1.00 10.56 ?  39  ALA   B C    1 
ATOM   4299 O  O    . ALA   B 1 39  ? 44.142 -21.458 5.761   1.00 11.67 ?  39  ALA   B O    1 
ATOM   4300 C  CB   . ALA   B 1 39  ? 45.548 -18.833 4.196   1.00 11.43 ?  39  ALA   B CB   1 
ATOM   4301 H  H    . ALA   B 1 39  ? 44.547 -20.687 2.914   1.00 12.56 ?  39  ALA   B H    1 
ATOM   4302 H  HA   . ALA   B 1 39  ? 46.739 -20.487 4.437   1.00 12.87 ?  39  ALA   B HA   1 
ATOM   4303 H  HB1  . ALA   B 1 39  ? 45.917 -18.356 4.954   1.00 13.88 ?  39  ALA   B HB1  1 
ATOM   4304 H  HB2  . ALA   B 1 39  ? 45.990 -18.550 3.378   1.00 13.88 ?  39  ALA   B HB2  1 
ATOM   4305 H  HB3  . ALA   B 1 39  ? 44.595 -18.670 4.129   1.00 13.88 ?  39  ALA   B HB3  1 
ATOM   4306 N  N    . ASN   B 1 40  ? 45.809 -20.357 6.800   1.00 11.34 ?  40  ASN   B N    1 
ATOM   4307 C  CA   . ASN   B 1 40  ? 45.243 -20.410 8.138   1.00 11.77 ?  40  ASN   B CA   1 
ATOM   4308 C  C    . ASN   B 1 40  ? 45.061 -18.984 8.662   1.00 11.57 ?  40  ASN   B C    1 
ATOM   4309 O  O    . ASN   B 1 40  ? 45.478 -18.006 8.034   1.00 11.70 ?  40  ASN   B O    1 
ATOM   4310 C  CB   . ASN   B 1 40  ? 46.093 -21.281 9.080   1.00 13.01 ?  40  ASN   B CB   1 
ATOM   4311 C  CG   . ASN   B 1 40  ? 47.546 -20.871 9.109   1.00 14.28 ?  40  ASN   B CG   1 
ATOM   4312 O  OD1  . ASN   B 1 40  ? 47.857 -19.688 9.184   1.00 16.03 ?  40  ASN   B OD1  1 
ATOM   4313 N  ND2  . ASN   B 1 40  ? 48.446 -21.840 9.047   1.00 14.18 ?  40  ASN   B ND2  1 
ATOM   4314 H  H    . ASN   B 1 40  ? 46.605 -20.035 6.781   1.00 13.78 ?  40  ASN   B H    1 
ATOM   4315 H  HA   . ASN   B 1 40  ? 44.360 -20.807 8.090   1.00 14.29 ?  40  ASN   B HA   1 
ATOM   4316 H  HB2  . ASN   B 1 40  ? 45.741 -21.208 9.980   1.00 15.77 ?  40  ASN   B HB2  1 
ATOM   4317 H  HB3  . ASN   B 1 40  ? 46.047 -22.201 8.777   1.00 15.77 ?  40  ASN   B HB3  1 
ATOM   4318 H  HD21 . ASN   B 1 40  ? 49.285 -21.650 9.060   1.00 17.18 ?  40  ASN   B HD21 1 
ATOM   4319 H  HD22 . ASN   B 1 40  ? 48.190 -22.658 8.994   1.00 17.18 ?  40  ASN   B HD22 1 
ATOM   4320 N  N    . VAL   B 1 41  ? 44.396 -18.856 9.813   1.00 12.21 ?  41  VAL   B N    1 
ATOM   4321 C  CA   . VAL   B 1 41  ? 43.944 -17.534 10.257  1.00 12.87 ?  41  VAL   B CA   1 
ATOM   4322 C  C    . VAL   B 1 41  ? 45.098 -16.585 10.554  1.00 12.73 ?  41  VAL   B C    1 
ATOM   4323 O  O    . VAL   B 1 41  ? 44.925 -15.363 10.474  1.00 12.99 ?  41  VAL   B O    1 
ATOM   4324 C  CB   . VAL   B 1 41  ? 42.966 -17.609 11.449  1.00 14.45 ?  41  VAL   B CB   1 
ATOM   4325 C  CG1  . VAL   B 1 41  ? 41.661 -18.279 11.040  1.00 15.10 ?  41  VAL   B CG1  1 
ATOM   4326 C  CG2  . VAL   B 1 41  ? 43.606 -18.306 12.637  1.00 15.60 ?  41  VAL   B CG2  1 
ATOM   4327 H  H    . VAL   B 1 41  ? 44.198 -19.501 10.339  1.00 14.81 ?  41  VAL   B H    1 
ATOM   4328 H  HA   . VAL   B 1 41  ? 43.447 -17.137 9.528   1.00 15.60 ?  41  VAL   B HA   1 
ATOM   4329 H  HB   . VAL   B 1 41  ? 42.747 -16.704 11.727  1.00 17.51 ?  41  VAL   B HB   1 
ATOM   4330 H  HG11 . VAL   B 1 41  ? 41.052 -18.275 11.797  1.00 18.28 ?  41  VAL   B HG11 1 
ATOM   4331 H  HG12 . VAL   B 1 41  ? 41.271 -17.788 10.300  1.00 18.28 ?  41  VAL   B HG12 1 
ATOM   4332 H  HG13 . VAL   B 1 41  ? 41.847 -19.192 10.771  1.00 18.28 ?  41  VAL   B HG13 1 
ATOM   4333 H  HG21 . VAL   B 1 41  ? 42.970 -18.330 13.370  1.00 18.88 ?  41  VAL   B HG21 1 
ATOM   4334 H  HG22 . VAL   B 1 41  ? 43.846 -19.211 12.381  1.00 18.88 ?  41  VAL   B HG22 1 
ATOM   4335 H  HG23 . VAL   B 1 41  ? 44.398 -17.815 12.903  1.00 18.88 ?  41  VAL   B HG23 1 
ATOM   4336 N  N    . TYR   B 1 42  ? 46.267 -17.105 10.931  1.00 13.18 ?  42  TYR   B N    1 
ATOM   4337 C  CA   . TYR   B 1 42  ? 47.418 -16.256 11.210  1.00 13.55 ?  42  TYR   B CA   1 
ATOM   4338 C  C    . TYR   B 1 42  ? 48.389 -16.179 10.036  1.00 12.87 ?  42  TYR   B C    1 
ATOM   4339 O  O    . TYR   B 1 42  ? 49.480 -15.612 10.176  1.00 14.06 ?  42  TYR   B O    1 
ATOM   4340 C  CB   . TYR   B 1 42  ? 48.101 -16.672 12.519  1.00 15.46 ?  42  TYR   B CB   1 
ATOM   4341 C  CG   . TYR   B 1 42  ? 47.512 -15.974 13.742  1.00 15.49 ?  42  TYR   B CG   1 
ATOM   4342 C  CD1  . TYR   B 1 42  ? 47.743 -14.620 13.960  1.00 14.89 ?  42  TYR   B CD1  1 
ATOM   4343 C  CD2  . TYR   B 1 42  ? 46.729 -16.658 14.664  1.00 17.07 ?  42  TYR   B CD2  1 
ATOM   4344 C  CE1  . TYR   B 1 42  ? 47.216 -13.966 15.056  1.00 15.94 ?  42  TYR   B CE1  1 
ATOM   4345 C  CE2  . TYR   B 1 42  ? 46.196 -16.007 15.771  1.00 17.20 ?  42  TYR   B CE2  1 
ATOM   4346 C  CZ   . TYR   B 1 42  ? 46.445 -14.656 15.961  1.00 17.82 ?  42  TYR   B CZ   1 
ATOM   4347 O  OH   . TYR   B 1 42  ? 45.934 -13.986 17.055  1.00 20.77 ?  42  TYR   B OH   1 
ATOM   4348 H  H    . TYR   B 1 42  ? 46.416 -17.950 11.018  1.00 15.98 ?  42  TYR   B H    1 
ATOM   4349 H  HA   . TYR   B 1 42  ? 47.086 -15.358 11.347  1.00 16.42 ?  42  TYR   B HA   1 
ATOM   4350 H  HB2  . TYR   B 1 42  ? 47.997 -17.628 12.641  1.00 18.72 ?  42  TYR   B HB2  1 
ATOM   4351 H  HB3  . TYR   B 1 42  ? 49.041 -16.443 12.466  1.00 18.72 ?  42  TYR   B HB3  1 
ATOM   4352 H  HD1  . TYR   B 1 42  ? 48.267 -14.146 13.347  1.00 18.04 ?  42  TYR   B HD1  1 
ATOM   4353 H  HD2  . TYR   B 1 42  ? 46.559 -17.565 14.534  1.00 20.65 ?  42  TYR   B HD2  1 
ATOM   4354 H  HE1  . TYR   B 1 42  ? 47.390 -13.061 15.179  1.00 19.29 ?  42  TYR   B HE1  1 
ATOM   4355 H  HE2  . TYR   B 1 42  ? 45.673 -16.478 16.380  1.00 20.81 ?  42  TYR   B HE2  1 
ATOM   4356 H  HH   . TYR   B 1 42  ? 46.172 -13.182 17.025  1.00 25.09 ?  42  TYR   B HH   1 
ATOM   4357 N  N    . LEU   B 1 43  ? 47.993 -16.690 8.872   1.00 11.72 ?  43  LEU   B N    1 
ATOM   4358 C  CA   . LEU   B 1 43  ? 48.810 -16.621 7.665   1.00 11.54 ?  43  LEU   B CA   1 
ATOM   4359 C  C    . LEU   B 1 43  ? 50.223 -17.127 7.924   1.00 11.85 ?  43  LEU   B C    1 
ATOM   4360 O  O    . LEU   B 1 43  ? 51.202 -16.534 7.472   1.00 12.80 ?  43  LEU   B O    1 
ATOM   4361 C  CB   . LEU   B 1 43  ? 48.826 -15.217 7.060   1.00 11.50 ?  43  LEU   B CB   1 
ATOM   4362 C  CG   . LEU   B 1 43  ? 47.472 -14.601 6.686   1.00 11.81 ?  43  LEU   B CG   1 
ATOM   4363 C  CD1  . LEU   B 1 43  ? 47.686 -13.205 6.107   1.00 13.23 ?  43  LEU   B CD1  1 
ATOM   4364 C  CD2  . LEU   B 1 43  ? 46.705 -15.491 5.710   1.00 12.35 ?  43  LEU   B CD2  1 
ATOM   4365 H  H    . LEU   B 1 43  ? 47.249 -17.102 8.756   1.00 14.23 ?  43  LEU   B H    1 
ATOM   4366 H  HA   . LEU   B 1 43  ? 48.414 -17.208 7.003   1.00 14.01 ?  43  LEU   B HA   1 
ATOM   4367 H  HB2  . LEU   B 1 43  ? 49.245 -14.616 7.697   1.00 13.97 ?  43  LEU   B HB2  1 
ATOM   4368 H  HB3  . LEU   B 1 43  ? 49.358 -15.244 6.250   1.00 13.97 ?  43  LEU   B HB3  1 
ATOM   4369 H  HG   . LEU   B 1 43  ? 46.934 -14.511 7.486   1.00 14.33 ?  43  LEU   B HG   1 
ATOM   4370 H  HD11 . LEU   B 1 43  ? 46.825 -12.822 5.872   1.00 16.04 ?  43  LEU   B HD11 1 
ATOM   4371 H  HD12 . LEU   B 1 43  ? 48.121 -12.650 6.775   1.00 16.04 ?  43  LEU   B HD12 1 
ATOM   4372 H  HD13 . LEU   B 1 43  ? 48.245 -13.270 5.317   1.00 16.04 ?  43  LEU   B HD13 1 
ATOM   4373 H  HD21 . LEU   B 1 43  ? 45.902 -15.031 5.421   1.00 14.99 ?  43  LEU   B HD21 1 
ATOM   4374 H  HD22 . LEU   B 1 43  ? 47.269 -15.683 4.944   1.00 14.99 ?  43  LEU   B HD22 1 
ATOM   4375 H  HD23 . LEU   B 1 43  ? 46.466 -16.320 6.158   1.00 14.99 ?  43  LEU   B HD23 1 
ATOM   4376 N  N    . LYS   B 1 44  ? 50.325 -18.246 8.645   1.00 11.99 ?  44  LYS   B N    1 
ATOM   4377 C  CA   . LYS   B 1 44  ? 51.595 -18.921 8.880   1.00 12.66 ?  44  LYS   B CA   1 
ATOM   4378 C  C    . LYS   B 1 44  ? 51.709 -20.038 7.850   1.00 12.13 ?  44  LYS   B C    1 
ATOM   4379 O  O    . LYS   B 1 44  ? 51.014 -21.056 7.942   1.00 13.27 ?  44  LYS   B O    1 
ATOM   4380 C  CB   . LYS   B 1 44  ? 51.653 -19.441 10.314  1.00 14.54 ?  44  LYS   B CB   1 
ATOM   4381 C  CG   . LYS   B 1 44  ? 51.829 -18.338 11.343  1.00 17.12 ?  44  LYS   B CG   1 
ATOM   4382 C  CD   . LYS   B 1 44  ? 52.983 -17.426 10.925  1.00 20.27 ?  44  LYS   B CD   1 
ATOM   4383 C  CE   . LYS   B 1 44  ? 53.570 -16.633 12.063  1.00 23.15 ?  44  LYS   B CE   1 
ATOM   4384 N  NZ   . LYS   B 1 44  ? 54.694 -15.773 11.621  1.00 24.47 ?  44  LYS   B NZ   1 
ATOM   4385 H  H    . LYS   B 1 44  ? 49.655 -18.634 9.019   1.00 14.55 ?  44  LYS   B H    1 
ATOM   4386 H  HA   . LYS   B 1 44  ? 52.325 -18.302 8.716   1.00 15.35 ?  44  LYS   B HA   1 
ATOM   4387 H  HB2  . LYS   B 1 44  ? 50.819 -19.902 10.512  1.00 17.62 ?  44  LYS   B HB2  1 
ATOM   4388 H  HB3  . LYS   B 1 44  ? 52.397 -20.052 10.397  1.00 17.62 ?  44  LYS   B HB3  1 
ATOM   4389 H  HG2  . LYS   B 1 44  ? 51.017 -17.815 11.404  1.00 20.71 ?  44  LYS   B HG2  1 
ATOM   4390 H  HG3  . LYS   B 1 44  ? 52.045 -18.736 12.205  1.00 20.71 ?  44  LYS   B HG3  1 
ATOM   4391 H  HD2  . LYS   B 1 44  ? 53.684 -17.975 10.532  1.00 24.48 ?  44  LYS   B HD2  1 
ATOM   4392 H  HD3  . LYS   B 1 44  ? 52.650 -16.797 10.264  1.00 24.48 ?  44  LYS   B HD3  1 
ATOM   4393 H  HE2  . LYS   B 1 44  ? 52.893 -16.039 12.390  1.00 27.94 ?  44  LYS   B HE2  1 
ATOM   4394 H  HE3  . LYS   B 1 44  ? 53.878 -17.237 12.764  1.00 27.94 ?  44  LYS   B HE3  1 
ATOM   4395 H  HZ1  . LYS   B 1 44  ? 55.016 -15.315 12.311  1.00 29.53 ?  44  LYS   B HZ1  1 
ATOM   4396 H  HZ2  . LYS   B 1 44  ? 55.342 -16.268 11.270  1.00 29.53 ?  44  LYS   B HZ2  1 
ATOM   4397 H  HZ3  . LYS   B 1 44  ? 54.405 -15.196 11.003  1.00 29.53 ?  44  LYS   B HZ3  1 
ATOM   4398 N  N    . HIS   B 1 45  ? 52.564 -19.828 6.852   1.00 11.84 ?  45  HIS   B N    1 
ATOM   4399 C  CA   . HIS   B 1 45  ? 52.581 -20.660 5.651   1.00 12.21 ?  45  HIS   B CA   1 
ATOM   4400 C  C    . HIS   B 1 45  ? 53.599 -21.783 5.814   1.00 14.19 ?  45  HIS   B C    1 
ATOM   4401 O  O    . HIS   B 1 45  ? 54.662 -21.799 5.203   1.00 16.28 ?  45  HIS   B O    1 
ATOM   4402 C  CB   . HIS   B 1 45  ? 52.897 -19.810 4.433   1.00 12.31 ?  45  HIS   B CB   1 
ATOM   4403 C  CG   . HIS   B 1 45  ? 52.031 -18.605 4.322   1.00 12.04 ?  45  HIS   B CG   1 
ATOM   4404 N  ND1  . HIS   B 1 45  ? 50.654 -18.683 4.290   1.00 12.14 ?  45  HIS   B ND1  1 
ATOM   4405 C  CD2  . HIS   B 1 45  ? 52.346 -17.291 4.250   1.00 12.61 ?  45  HIS   B CD2  1 
ATOM   4406 C  CE1  . HIS   B 1 45  ? 50.165 -17.460 4.185   1.00 11.62 ?  45  HIS   B CE1  1 
ATOM   4407 N  NE2  . HIS   B 1 45  ? 51.167 -16.598 4.160   1.00 12.31 ?  45  HIS   B NE2  1 
ATOM   4408 H  H    . HIS   B 1 45  ? 53.146 -19.192 6.841   1.00 14.37 ?  45  HIS   B H    1 
ATOM   4409 H  HA   . HIS   B 1 45  ? 51.698 -21.053 5.525   1.00 14.82 ?  45  HIS   B HA   1 
ATOM   4410 H  HB2  . HIS   B 1 45  ? 53.815 -19.516 4.483   1.00 14.93 ?  45  HIS   B HB2  1 
ATOM   4411 H  HB3  . HIS   B 1 45  ? 52.764 -20.350 3.632   1.00 14.93 ?  45  HIS   B HB3  1 
ATOM   4412 H  HD2  . HIS   B 1 45  ? 53.202 -16.926 4.255   1.00 15.29 ?  45  HIS   B HD2  1 
ATOM   4413 H  HE1  . HIS   B 1 45  ? 49.262 -17.240 4.137   1.00 14.10 ?  45  HIS   B HE1  1 
ATOM   4414 H  HE2  . HIS   B 1 45  ? 51.090 -15.742 4.106   1.00 14.93 ?  45  HIS   B HE2  1 
ATOM   4415 N  N    A GLY   B 1 46  ? 53.226 -22.756 6.641   0.60 15.12 ?  46  GLY   B N    1 
ATOM   4416 N  N    B GLY   B 1 46  ? 53.243 -22.738 6.664   0.40 14.93 ?  46  GLY   B N    1 
ATOM   4417 C  CA   A GLY   B 1 46  ? 54.142 -23.812 7.033   0.60 17.13 ?  46  GLY   B CA   1 
ATOM   4418 C  CA   B GLY   B 1 46  ? 54.160 -23.810 6.991   0.40 16.45 ?  46  GLY   B CA   1 
ATOM   4419 C  C    A GLY   B 1 46  ? 54.201 -25.045 6.153   0.60 18.62 ?  46  GLY   B C    1 
ATOM   4420 C  C    B GLY   B 1 46  ? 54.187 -24.948 5.991   0.40 17.87 ?  46  GLY   B C    1 
ATOM   4421 O  O    A GLY   B 1 46  ? 55.291 -25.510 5.807   0.60 20.89 ?  46  GLY   B O    1 
ATOM   4422 O  O    B GLY   B 1 46  ? 55.221 -25.223 5.374   0.40 19.01 ?  46  GLY   B O    1 
ATOM   4423 H  H    A GLY   B 1 46  ? 52.446 -22.810 7.006   0.60 18.31 ?  46  GLY   B H    1 
ATOM   4424 H  H    B GLY   B 1 46  ? 52.483 -22.777 7.071   0.40 18.09 ?  46  GLY   B H    1 
ATOM   4425 H  HA2  A GLY   B 1 46  ? 55.035 -23.441 7.079   0.60 20.72 ?  46  GLY   B HA2  1 
ATOM   4426 H  HA2  B GLY   B 1 46  ? 55.056 -23.447 7.053   0.40 19.90 ?  46  GLY   B HA2  1 
ATOM   4427 H  HA3  A GLY   B 1 46  ? 53.899 -24.113 7.921   0.60 20.72 ?  46  GLY   B HA3  1 
ATOM   4428 H  HA3  B GLY   B 1 46  ? 53.921 -24.171 7.859   0.40 19.90 ?  46  GLY   B HA3  1 
ATOM   4429 N  N    . GLY   B 1 47  ? 53.047 -25.610 5.803   1.00 18.04 ?  47  GLY   B N    1 
ATOM   4430 C  CA   . GLY   B 1 47  ? 52.996 -26.881 5.108   1.00 15.99 ?  47  GLY   B CA   1 
ATOM   4431 C  C    . GLY   B 1 47  ? 52.077 -26.867 3.902   1.00 13.70 ?  47  GLY   B C    1 
ATOM   4432 O  O    . GLY   B 1 47  ? 51.428 -25.865 3.604   1.00 14.06 ?  47  GLY   B O    1 
ATOM   4433 H  H    A GLY   B 1 47  ? 52.272 -25.279 5.978   0.60 21.81 ?  47  GLY   B H    1 
ATOM   4434 H  H    B GLY   B 1 47  ? 52.278 -25.332 6.071   0.40 21.81 ?  47  GLY   B H    1 
ATOM   4435 H  HA2  . GLY   B 1 47  ? 53.883 -27.126 4.804   1.00 19.35 ?  47  GLY   B HA2  1 
ATOM   4436 H  HA3  . GLY   B 1 47  ? 52.686 -27.567 5.721   1.00 19.35 ?  47  GLY   B HA3  1 
ATOM   4437 N  N    . GLY   B 1 48  ? 52.028 -28.011 3.220   1.00 12.76 ?  48  GLY   B N    1 
ATOM   4438 C  CA   . GLY   B 1 48  ? 51.102 -28.149 2.113   1.00 12.82 ?  48  GLY   B CA   1 
ATOM   4439 C  C    . GLY   B 1 48  ? 51.242 -27.036 1.101   1.00 12.50 ?  48  GLY   B C    1 
ATOM   4440 O  O    . GLY   B 1 48  ? 52.347 -26.573 0.792   1.00 12.79 ?  48  GLY   B O    1 
ATOM   4441 H  H    . GLY   B 1 48  ? 52.519 -28.700 3.373   1.00 15.47 ?  48  GLY   B H    1 
ATOM   4442 H  HA2  . GLY   B 1 48  ? 51.257 -28.998 1.666   1.00 15.55 ?  48  GLY   B HA2  1 
ATOM   4443 H  HA3  . GLY   B 1 48  ? 50.193 -28.142 2.448   1.00 15.55 ?  48  GLY   B HA3  1 
ATOM   4444 N  N    . VAL   B 1 49  ? 50.096 -26.601 0.572   1.00 12.18 ?  49  VAL   B N    1 
ATOM   4445 C  CA   . VAL   B 1 49  ? 50.081 -25.579 -0.471  1.00 12.23 ?  49  VAL   B CA   1 
ATOM   4446 C  C    . VAL   B 1 49  ? 50.735 -24.292 0.019   1.00 11.42 ?  49  VAL   B C    1 
ATOM   4447 O  O    . VAL   B 1 49  ? 51.528 -23.674 -0.698  1.00 12.04 ?  49  VAL   B O    1 
ATOM   4448 C  CB   . VAL   B 1 49  ? 48.640 -25.330 -0.956  1.00 13.50 ?  49  VAL   B CB   1 
ATOM   4449 C  CG1  . VAL   B 1 49  ? 48.577 -24.087 -1.836  1.00 13.48 ?  49  VAL   B CG1  1 
ATOM   4450 C  CG2  . VAL   B 1 49  ? 48.106 -26.543 -1.706  1.00 15.03 ?  49  VAL   B CG2  1 
ATOM   4451 H  H    . VAL   B 1 49  ? 49.314 -26.880 0.796   1.00 14.78 ?  49  VAL   B H    1 
ATOM   4452 H  HA   . VAL   B 1 49  ? 50.591 -25.897 -1.233  1.00 14.84 ?  49  VAL   B HA   1 
ATOM   4453 H  HB   . VAL   B 1 49  ? 48.069 -25.178 -0.190  1.00 16.37 ?  49  VAL   B HB   1 
ATOM   4454 H  HG11 . VAL   B 1 49  ? 47.751 -24.104 -2.347  1.00 16.34 ?  49  VAL   B HG11 1 
ATOM   4455 H  HG12 . VAL   B 1 49  ? 48.599 -23.296 -1.275  1.00 16.34 ?  49  VAL   B HG12 1 
ATOM   4456 H  HG13 . VAL   B 1 49  ? 49.335 -24.088 -2.442  1.00 16.34 ?  49  VAL   B HG13 1 
ATOM   4457 H  HG21 . VAL   B 1 49  ? 47.199 -26.361 -1.997  1.00 18.20 ?  49  VAL   B HG21 1 
ATOM   4458 H  HG22 . VAL   B 1 49  ? 48.673 -26.711 -2.478  1.00 18.20 ?  49  VAL   B HG22 1 
ATOM   4459 H  HG23 . VAL   B 1 49  ? 48.119 -27.309 -1.114  1.00 18.20 ?  49  VAL   B HG23 1 
ATOM   4460 N  N    . ALA   B 1 50  ? 50.397 -23.856 1.234   1.00 11.21 ?  50  ALA   B N    1 
ATOM   4461 C  CA   . ALA   B 1 50  ? 50.917 -22.577 1.710   1.00 11.00 ?  50  ALA   B CA   1 
ATOM   4462 C  C    . ALA   B 1 50  ? 52.437 -22.604 1.815   1.00 11.05 ?  50  ALA   B C    1 
ATOM   4463 O  O    . ALA   B 1 50  ? 53.116 -21.636 1.449   1.00 11.40 ?  50  ALA   B O    1 
ATOM   4464 C  CB   . ALA   B 1 50  ? 50.289 -22.209 3.053   1.00 11.35 ?  50  ALA   B CB   1 
ATOM   4465 H  H    . ALA   B 1 50  ? 49.886 -24.271 1.785   1.00 13.62 ?  50  ALA   B H    1 
ATOM   4466 H  HA   . ALA   B 1 50  ? 50.686 -21.888 1.075   1.00 13.36 ?  50  ALA   B HA   1 
ATOM   4467 H  HB1  . ALA   B 1 50  ? 50.651 -21.354 3.347   1.00 13.79 ?  50  ALA   B HB1  1 
ATOM   4468 H  HB2  . ALA   B 1 50  ? 49.330 -22.139 2.944   1.00 13.79 ?  50  ALA   B HB2  1 
ATOM   4469 H  HB3  . ALA   B 1 50  ? 50.502 -22.895 3.704   1.00 13.79 ?  50  ALA   B HB3  1 
ATOM   4470 N  N    . GLY   B 1 51  ? 52.992 -23.697 2.330   1.00 11.87 ?  51  GLY   B N    1 
ATOM   4471 C  CA   . GLY   B 1 51  ? 54.436 -23.797 2.401   1.00 12.64 ?  51  GLY   B CA   1 
ATOM   4472 C  C    . GLY   B 1 51  ? 55.079 -23.745 1.031   1.00 12.33 ?  51  GLY   B C    1 
ATOM   4473 O  O    . GLY   B 1 51  ? 56.124 -23.113 0.848   1.00 13.08 ?  51  GLY   B O    1 
ATOM   4474 H  H    . GLY   B 1 51  ? 52.567 -24.381 2.637   1.00 14.41 ?  51  GLY   B H    1 
ATOM   4475 H  HA2  . GLY   B 1 51  ? 54.788 -23.065 2.933   1.00 15.34 ?  51  GLY   B HA2  1 
ATOM   4476 H  HA3  . GLY   B 1 51  ? 54.687 -24.633 2.828   1.00 15.34 ?  51  GLY   B HA3  1 
ATOM   4477 N  N    . ALA   B 1 52  ? 54.469 -24.408 0.049   1.00 11.86 ?  52  ALA   B N    1 
ATOM   4478 C  CA   . ALA   B 1 52  ? 55.035 -24.416 -1.291  1.00 12.35 ?  52  ALA   B CA   1 
ATOM   4479 C  C    . ALA   B 1 52  ? 54.955 -23.040 -1.942  1.00 11.82 ?  52  ALA   B C    1 
ATOM   4480 O  O    . ALA   B 1 52  ? 55.925 -22.594 -2.573  1.00 12.56 ?  52  ALA   B O    1 
ATOM   4481 C  CB   . ALA   B 1 52  ? 54.345 -25.470 -2.151  1.00 13.09 ?  52  ALA   B CB   1 
ATOM   4482 H  H    . ALA   B 1 52  ? 53.733 -24.848 0.134   1.00 14.40 ?  52  ALA   B H    1 
ATOM   4483 H  HA   . ALA   B 1 52  ? 55.972 -24.654 -1.227  1.00 14.99 ?  52  ALA   B HA   1 
ATOM   4484 H  HB1  . ALA   B 1 52  ? 54.743 -25.460 -3.038  1.00 15.87 ?  52  ALA   B HB1  1 
ATOM   4485 H  HB2  . ALA   B 1 52  ? 54.479 -26.343 -1.743  1.00 15.87 ?  52  ALA   B HB2  1 
ATOM   4486 H  HB3  . ALA   B 1 52  ? 53.403 -25.269 -2.206  1.00 15.87 ?  52  ALA   B HB3  1 
ATOM   4487 N  N    . LEU   B 1 53  ? 53.810 -22.359 -1.823  1.00 11.50 ?  53  LEU   B N    1 
ATOM   4488 C  CA   . LEU   B 1 53  ? 53.701 -21.017 -2.391  1.00 11.64 ?  53  LEU   B CA   1 
ATOM   4489 C  C    . LEU   B 1 53  ? 54.707 -20.077 -1.740  1.00 11.40 ?  53  LEU   B C    1 
ATOM   4490 O  O    . LEU   B 1 53  ? 55.411 -19.323 -2.426  1.00 12.16 ?  53  LEU   B O    1 
ATOM   4491 C  CB   . LEU   B 1 53  ? 52.275 -20.481 -2.223  1.00 12.10 ?  53  LEU   B CB   1 
ATOM   4492 C  CG   . LEU   B 1 53  ? 51.144 -21.210 -2.959  1.00 12.27 ?  53  LEU   B CG   1 
ATOM   4493 C  CD1  . LEU   B 1 53  ? 49.796 -20.595 -2.609  1.00 13.78 ?  53  LEU   B CD1  1 
ATOM   4494 C  CD2  . LEU   B 1 53  ? 51.355 -21.206 -4.465  1.00 14.28 ?  53  LEU   B CD2  1 
ATOM   4495 H  H    . LEU   B 1 53  ? 53.103 -22.645 -1.425  1.00 13.97 ?  53  LEU   B H    1 
ATOM   4496 H  HA   . LEU   B 1 53  ? 53.898 -21.062 -3.342  1.00 14.13 ?  53  LEU   B HA   1 
ATOM   4497 H  HB2  . LEU   B 1 53  ? 52.057 -20.505 -1.280  1.00 14.69 ?  53  LEU   B HB2  1 
ATOM   4498 H  HB3  . LEU   B 1 53  ? 52.263 -19.565 -2.532  1.00 14.69 ?  53  LEU   B HB3  1 
ATOM   4499 H  HG   . LEU   B 1 53  ? 51.122 -22.134 -2.665  1.00 14.89 ?  53  LEU   B HG   1 
ATOM   4500 H  HD11 . LEU   B 1 53  ? 49.094 -21.078 -3.081  1.00 16.70 ?  53  LEU   B HD11 1 
ATOM   4501 H  HD12 . LEU   B 1 53  ? 49.651 -20.674 -1.649  1.00 16.70 ?  53  LEU   B HD12 1 
ATOM   4502 H  HD13 . LEU   B 1 53  ? 49.790 -19.665 -2.869  1.00 16.70 ?  53  LEU   B HD13 1 
ATOM   4503 H  HD21 . LEU   B 1 53  ? 50.615 -21.665 -4.894  1.00 17.30 ?  53  LEU   B HD21 1 
ATOM   4504 H  HD22 . LEU   B 1 53  ? 51.400 -20.290 -4.779  1.00 17.30 ?  53  LEU   B HD22 1 
ATOM   4505 H  HD23 . LEU   B 1 53  ? 52.186 -21.666 -4.668  1.00 17.30 ?  53  LEU   B HD23 1 
ATOM   4506 N  N    . ASN   B 1 54  ? 54.798 -20.112 -0.412  1.00 11.22 ?  54  ASN   B N    1 
ATOM   4507 C  CA   . ASN   B 1 54  ? 55.716 -19.205 0.260   1.00 11.79 ?  54  ASN   B CA   1 
ATOM   4508 C  C    . ASN   B 1 54  ? 57.160 -19.482 -0.142  1.00 12.30 ?  54  ASN   B C    1 
ATOM   4509 O  O    . ASN   B 1 54  ? 57.933 -18.545 -0.386  1.00 12.71 ?  54  ASN   B O    1 
ATOM   4510 C  CB   . ASN   B 1 54  ? 55.552 -19.282 1.771   1.00 12.65 ?  54  ASN   B CB   1 
ATOM   4511 C  CG   . ASN   B 1 54  ? 56.526 -18.365 2.484   1.00 12.82 ?  54  ASN   B CG   1 
ATOM   4512 O  OD1  . ASN   B 1 54  ? 56.545 -17.158 2.237   1.00 12.92 ?  54  ASN   B OD1  1 
ATOM   4513 N  ND2  . ASN   B 1 54  ? 57.375 -18.934 3.332   1.00 14.57 ?  54  ASN   B ND2  1 
ATOM   4514 H  H    . ASN   B 1 54  ? 54.353 -20.639 0.103   1.00 13.62 ?  54  ASN   B H    1 
ATOM   4515 H  HA   . ASN   B 1 54  ? 55.504 -18.300 -0.013  1.00 14.31 ?  54  ASN   B HA   1 
ATOM   4516 H  HB2  . ASN   B 1 54  ? 54.649 -19.007 2.009   1.00 15.34 ?  54  ASN   B HB2  1 
ATOM   4517 H  HB3  . ASN   B 1 54  ? 55.714 -20.188 2.069   1.00 15.34 ?  54  ASN   B HB3  1 
ATOM   4518 H  HD21 . ASN   B 1 54  ? 57.954 -18.454 3.752   1.00 17.65 ?  54  ASN   B HD21 1 
ATOM   4519 H  HD22 . ASN   B 1 54  ? 57.347 -19.783 3.467   1.00 17.65 ?  54  ASN   B HD22 1 
ATOM   4520 N  N    . LYS   B 1 55  ? 57.548 -20.759 -0.210  1.00 12.96 ?  55  LYS   B N    1 
ATOM   4521 C  CA   . LYS   B 1 55  ? 58.903 -21.099 -0.628  1.00 13.90 ?  55  LYS   B CA   1 
ATOM   4522 C  C    . LYS   B 1 55  ? 59.196 -20.551 -2.018  1.00 13.67 ?  55  LYS   B C    1 
ATOM   4523 O  O    . LYS   B 1 55  ? 60.290 -20.036 -2.271  1.00 14.15 ?  55  LYS   B O    1 
ATOM   4524 C  CB   . LYS   B 1 55  ? 59.097 -22.615 -0.581  1.00 15.79 ?  55  LYS   B CB   1 
ATOM   4525 C  CG   . LYS   B 1 55  ? 60.482 -23.077 -0.982  1.00 19.76 ?  55  LYS   B CG   1 
ATOM   4526 C  CD   . LYS   B 1 55  ? 60.644 -24.581 -0.800  1.00 23.27 ?  55  LYS   B CD   1 
ATOM   4527 C  CE   . LYS   B 1 55  ? 60.746 -24.971 0.675   1.00 26.41 ?  55  LYS   B CE   1 
ATOM   4528 N  NZ   . LYS   B 1 55  ? 61.045 -26.414 0.855   1.00 27.84 ?  55  LYS   B NZ   1 
ATOM   4529 H  H    . LYS   B 1 55  ? 57.048 -21.433 -0.026  1.00 15.72 ?  55  LYS   B H    1 
ATOM   4530 H  HA   . LYS   B 1 55  ? 59.533 -20.697 -0.012  1.00 16.85 ?  55  LYS   B HA   1 
ATOM   4531 H  HB2  . LYS   B 1 55  ? 58.934 -22.918 0.327   1.00 19.11 ?  55  LYS   B HB2  1 
ATOM   4532 H  HB3  . LYS   B 1 55  ? 58.462 -23.030 -1.184  1.00 19.11 ?  55  LYS   B HB3  1 
ATOM   4533 H  HG2  . LYS   B 1 55  ? 60.634 -22.868 -1.917  1.00 23.87 ?  55  LYS   B HG2  1 
ATOM   4534 H  HG3  . LYS   B 1 55  ? 61.143 -22.630 -0.428  1.00 23.87 ?  55  LYS   B HG3  1 
ATOM   4535 H  HD2  . LYS   B 1 55  ? 59.875 -25.035 -1.179  1.00 28.09 ?  55  LYS   B HD2  1 
ATOM   4536 H  HD3  . LYS   B 1 55  ? 61.457 -24.874 -1.243  1.00 28.09 ?  55  LYS   B HD3  1 
ATOM   4537 H  HE2  . LYS   B 1 55  ? 61.457 -24.455 1.089   1.00 31.86 ?  55  LYS   B HE2  1 
ATOM   4538 H  HE3  . LYS   B 1 55  ? 59.899 -24.777 1.111   1.00 31.86 ?  55  LYS   B HE3  1 
ATOM   4539 H  HZ1  . LYS   B 1 55  ? 61.064 -26.613 1.723   1.00 33.57 ?  55  LYS   B HZ1  1 
ATOM   4540 H  HZ2  . LYS   B 1 55  ? 60.415 -26.904 0.461   1.00 33.57 ?  55  LYS   B HZ2  1 
ATOM   4541 H  HZ3  . LYS   B 1 55  ? 61.833 -26.608 0.495   1.00 33.57 ?  55  LYS   B HZ3  1 
ATOM   4542 N  N    . ALA   B 1 56  ? 58.226 -20.640 -2.932  1.00 13.05 ?  56  ALA   B N    1 
ATOM   4543 C  CA   . ALA   B 1 56  ? 58.442 -20.135 -4.283  1.00 14.03 ?  56  ALA   B CA   1 
ATOM   4544 C  C    . ALA   B 1 56  ? 58.717 -18.639 -4.283  1.00 13.79 ?  56  ALA   B C    1 
ATOM   4545 O  O    . ALA   B 1 56  ? 59.456 -18.145 -5.147  1.00 14.68 ?  56  ALA   B O    1 
ATOM   4546 C  CB   . ALA   B 1 56  ? 57.247 -20.470 -5.176  1.00 15.09 ?  56  ALA   B CB   1 
ATOM   4547 H  H    . ALA   B 1 56  ? 57.449 -20.982 -2.799  1.00 15.83 ?  56  ALA   B H    1 
ATOM   4548 H  HA   . ALA   B 1 56  ? 59.221 -20.571 -4.659  1.00 17.00 ?  56  ALA   B HA   1 
ATOM   4549 H  HB1  . ALA   B 1 56  ? 57.417 -20.132 -6.071  1.00 18.28 ?  56  ALA   B HB1  1 
ATOM   4550 H  HB2  . ALA   B 1 56  ? 57.140 -21.434 -5.205  1.00 18.28 ?  56  ALA   B HB2  1 
ATOM   4551 H  HB3  . ALA   B 1 56  ? 56.452 -20.058 -4.811  1.00 18.28 ?  56  ALA   B HB3  1 
ATOM   4552 N  N    . THR   B 1 57  ? 58.148 -17.905 -3.323  1.00 13.50 ?  57  THR   B N    1 
ATOM   4553 C  CA   . THR   B 1 57  ? 58.391 -16.472 -3.195  1.00 13.48 ?  57  THR   B CA   1 
ATOM   4554 C  C    . THR   B 1 57  ? 59.643 -16.151 -2.387  1.00 14.04 ?  57  THR   B C    1 
ATOM   4555 O  O    . THR   B 1 57  ? 59.882 -14.978 -2.081  1.00 14.52 ?  57  THR   B O    1 
ATOM   4556 C  CB   . THR   B 1 57  ? 57.189 -15.745 -2.559  1.00 12.81 ?  57  THR   B CB   1 
ATOM   4557 O  OG1  . THR   B 1 57  ? 57.167 -15.960 -1.140  1.00 13.09 ?  57  THR   B OG1  1 
ATOM   4558 C  CG2  . THR   B 1 57  ? 55.874 -16.168 -3.189  1.00 13.00 ?  57  THR   B CG2  1 
ATOM   4559 H  H    . THR   B 1 57  ? 57.601 -18.216 -2.736  1.00 16.37 ?  57  THR   B H    1 
ATOM   4560 H  HA   . THR   B 1 57  ? 58.513 -16.103 -4.085  1.00 16.34 ?  57  THR   B HA   1 
ATOM   4561 H  HB   . THR   B 1 57  ? 57.294 -14.793 -2.725  1.00 15.54 ?  57  THR   B HB   1 
ATOM   4562 H  HG1  . THR   B 1 57  ? 57.108 -16.778 -0.974  1.00 15.87 ?  57  THR   B HG1  1 
ATOM   4563 H  HG21 . THR   B 1 57  ? 55.151 -15.616 -2.855  1.00 15.77 ?  57  THR   B HG21 1 
ATOM   4564 H  HG22 . THR   B 1 57  ? 55.919 -16.077 -4.155  1.00 15.77 ?  57  THR   B HG22 1 
ATOM   4565 H  HG23 . THR   B 1 57  ? 55.684 -17.095 -2.975  1.00 15.77 ?  57  THR   B HG23 1 
ATOM   4566 N  N    . ASN   B 1 58  ? 60.440 -17.155 -2.030  1.00 14.59 ?  58  ASN   B N    1 
ATOM   4567 C  CA   . ASN   B 1 58  ? 61.637 -16.938 -1.220  1.00 16.92 ?  58  ASN   B CA   1 
ATOM   4568 C  C    . ASN   B 1 58  ? 61.297 -16.223 0.087   1.00 15.28 ?  58  ASN   B C    1 
ATOM   4569 O  O    . ASN   B 1 58  ? 62.031 -15.344 0.548   1.00 16.10 ?  58  ASN   B O    1 
ATOM   4570 C  CB   . ASN   B 1 58  ? 62.727 -16.194 -1.997  1.00 23.43 ?  58  ASN   B CB   1 
ATOM   4571 C  CG   . ASN   B 1 58  ? 64.092 -16.315 -1.344  1.00 31.88 ?  58  ASN   B CG   1 
ATOM   4572 O  OD1  . ASN   B 1 58  ? 64.399 -17.322 -0.707  1.00 34.07 ?  58  ASN   B OD1  1 
ATOM   4573 N  ND2  . ASN   B 1 58  ? 64.916 -15.285 -1.494  1.00 35.74 ?  58  ASN   B ND2  1 
ATOM   4574 H  H    . ASN   B 1 58  ? 60.303 -17.980 -2.239  1.00 17.67 ?  58  ASN   B H    1 
ATOM   4575 H  HA   . ASN   B 1 58  ? 61.998 -17.809 -0.992  1.00 20.47 ?  58  ASN   B HA   1 
ATOM   4576 H  HB2  . ASN   B 1 58  ? 62.786 -16.565 -2.896  1.00 28.29 ?  58  ASN   B HB2  1 
ATOM   4577 H  HB3  . ASN   B 1 58  ? 62.499 -15.254 -2.044  1.00 28.29 ?  58  ASN   B HB3  1 
ATOM   4578 H  HD21 . ASN   B 1 58  ? 65.701 -15.308 -1.143  1.00 43.05 ?  58  ASN   B HD21 1 
ATOM   4579 H  HD22 . ASN   B 1 58  ? 64.665 -14.596 -1.942  1.00 43.05 ?  58  ASN   B HD22 1 
ATOM   4580 N  N    . ASN   B 1 59  ? 60.172 -16.607 0.692   1.00 14.28 ?  59  ASN   B N    1 
ATOM   4581 C  CA   . ASN   B 1 59  ? 59.697 -16.133 1.992   1.00 14.42 ?  59  ASN   B CA   1 
ATOM   4582 C  C    . ASN   B 1 59  ? 59.095 -14.730 1.935   1.00 13.79 ?  59  ASN   B C    1 
ATOM   4583 O  O    . ASN   B 1 59  ? 58.663 -14.228 2.977   1.00 13.99 ?  59  ASN   B O    1 
ATOM   4584 C  CB   . ASN   B 1 59  ? 60.769 -16.181 3.097   1.00 15.50 ?  59  ASN   B CB   1 
ATOM   4585 C  CG   . ASN   B 1 59  ? 60.181 -16.366 4.479   1.00 16.73 ?  59  ASN   B CG   1 
ATOM   4586 O  OD1  . ASN   B 1 59  ? 59.351 -17.251 4.699   1.00 17.09 ?  59  ASN   B OD1  1 
ATOM   4587 N  ND2  . ASN   B 1 59  ? 60.600 -15.528 5.419   1.00 17.31 ?  59  ASN   B ND2  1 
ATOM   4588 H  H    . ASN   B 1 59  ? 59.633 -17.187 0.347   1.00 17.30 ?  59  ASN   B H    1 
ATOM   4589 H  HA   . ASN   B 1 59  ? 58.988 -16.728 2.276   1.00 17.47 ?  59  ASN   B HA   1 
ATOM   4590 H  HB2  . ASN   B 1 59  ? 61.366 -16.925 2.934   1.00 18.76 ?  59  ASN   B HB2  1 
ATOM   4591 H  HB3  . ASN   B 1 59  ? 61.263 -15.349 3.101   1.00 18.76 ?  59  ASN   B HB3  1 
ATOM   4592 H  HD21 . ASN   B 1 59  ? 60.292 -15.592 6.221   1.00 20.94 ?  59  ASN   B HD21 1 
ATOM   4593 H  HD22 . ASN   B 1 59  ? 61.175 -14.922 5.227   1.00 20.94 ?  59  ASN   B HD22 1 
ATOM   4594 N  N    . ALA   B 1 60  ? 59.036 -14.086 0.766   1.00 13.27 ?  60  ALA   B N    1 
ATOM   4595 C  CA   . ALA   B 1 60  ? 58.441 -12.754 0.695   1.00 13.59 ?  60  ALA   B CA   1 
ATOM   4596 C  C    . ALA   B 1 60  ? 56.974 -12.781 1.101   1.00 12.69 ?  60  ALA   B C    1 
ATOM   4597 O  O    . ALA   B 1 60  ? 56.469 -11.827 1.708   1.00 13.28 ?  60  ALA   B O    1 
ATOM   4598 C  CB   . ALA   B 1 60  ? 58.605 -12.171 -0.708  1.00 14.76 ?  60  ALA   B CB   1 
ATOM   4599 H  H    . ALA   B 1 60  ? 59.325 -14.398 0.018   1.00 16.09 ?  60  ALA   B H    1 
ATOM   4600 H  HA   . ALA   B 1 60  ? 58.904 -12.176 1.317   1.00 16.47 ?  60  ALA   B HA   1 
ATOM   4601 H  HB1  . ALA   B 1 60  ? 58.207 -11.289 -0.730  1.00 17.88 ?  60  ALA   B HB1  1 
ATOM   4602 H  HB2  . ALA   B 1 60  ? 59.554 -12.111 -0.914  1.00 17.88 ?  60  ALA   B HB2  1 
ATOM   4603 H  HB3  . ALA   B 1 60  ? 58.166 -12.752 -1.347  1.00 17.88 ?  60  ALA   B HB3  1 
ATOM   4604 N  N    . MET   B 1 61  ? 56.266 -13.860 0.761   1.00 12.26 ?  61  MET   B N    1 
ATOM   4605 C  CA   . MET   B 1 61  ? 54.869 -13.976 1.154   1.00 11.62 ?  61  MET   B CA   1 
ATOM   4606 C  C    . MET   B 1 61  ? 54.730 -13.984 2.674   1.00 12.05 ?  61  MET   B C    1 
ATOM   4607 O  O    . MET   B 1 61  ? 53.825 -13.341 3.225   1.00 11.91 ?  61  MET   B O    1 
ATOM   4608 C  CB   . MET   B 1 61  ? 54.286 -15.243 0.524   1.00 11.59 ?  61  MET   B CB   1 
ATOM   4609 C  CG   . MET   B 1 61  ? 52.841 -15.533 0.920   1.00 11.31 ?  61  MET   B CG   1 
ATOM   4610 S  SD   . MET   B 1 61  ? 52.205 -17.045 0.167   1.00 12.52 ?  61  MET   B SD   1 
ATOM   4611 C  CE   . MET   B 1 61  ? 51.949 -16.471 -1.510  1.00 13.78 ?  61  MET   B CE   1 
ATOM   4612 H  H    . MET   B 1 61  ? 56.568 -14.532 0.308   1.00 14.87 ?  61  MET   B H    1 
ATOM   4613 H  HA   . MET   B 1 61  ? 54.377 -13.221 0.796   1.00 14.11 ?  61  MET   B HA   1 
ATOM   4614 H  HB2  . MET   B 1 61  ? 54.313 -15.152 -0.444  1.00 14.08 ?  61  MET   B HB2  1 
ATOM   4615 H  HB3  . MET   B 1 61  ? 54.825 -16.002 0.793   1.00 14.08 ?  61  MET   B HB3  1 
ATOM   4616 H  HG2  . MET   B 1 61  ? 52.788 -15.637 1.883   1.00 13.73 ?  61  MET   B HG2  1 
ATOM   4617 H  HG3  . MET   B 1 61  ? 52.280 -14.794 0.635   1.00 13.73 ?  61  MET   B HG3  1 
ATOM   4618 H  HE1  . MET   B 1 61  ? 51.579 -17.196 -2.037  1.00 16.70 ?  61  MET   B HE1  1 
ATOM   4619 H  HE2  . MET   B 1 61  ? 51.335 -15.721 -1.498  1.00 16.70 ?  61  MET   B HE2  1 
ATOM   4620 H  HE3  . MET   B 1 61  ? 52.802 -16.194 -1.881  1.00 16.70 ?  61  MET   B HE3  1 
ATOM   4621 N  N    . GLN   B 1 62  ? 55.612 -14.704 3.371   1.00 11.93 ?  62  GLN   B N    1 
ATOM   4622 C  CA   . GLN   B 1 62  ? 55.506 -14.764 4.824   1.00 12.22 ?  62  GLN   B CA   1 
ATOM   4623 C  C    . GLN   B 1 62  ? 55.788 -13.407 5.456   1.00 12.52 ?  62  GLN   B C    1 
ATOM   4624 O  O    . GLN   B 1 62  ? 55.102 -13.006 6.402   1.00 12.95 ?  62  GLN   B O    1 
ATOM   4625 C  CB   . GLN   B 1 62  ? 56.460 -15.815 5.388   1.00 12.58 ?  62  GLN   B CB   1 
ATOM   4626 C  CG   . GLN   B 1 62  ? 56.237 -16.086 6.868   1.00 12.76 ?  62  GLN   B CG   1 
ATOM   4627 C  CD   . GLN   B 1 62  ? 54.860 -16.678 7.112   1.00 12.46 ?  62  GLN   B CD   1 
ATOM   4628 O  OE1  . GLN   B 1 62  ? 54.599 -17.827 6.755   1.00 13.09 ?  62  GLN   B OE1  1 
ATOM   4629 N  NE2  . GLN   B 1 62  ? 53.953 -15.884 7.673   1.00 13.14 ?  62  GLN   B NE2  1 
ATOM   4630 H  H    . GLN   B 1 62  ? 56.257 -15.164 3.032   1.00 14.47 ?  62  GLN   B H    1 
ATOM   4631 H  HA   . GLN   B 1 62  ? 54.601 -15.026 5.061   1.00 14.83 ?  62  GLN   B HA   1 
ATOM   4632 H  HB2  . GLN   B 1 62  ? 56.336 -16.651 4.909   1.00 15.26 ?  62  GLN   B HB2  1 
ATOM   4633 H  HB3  . GLN   B 1 62  ? 57.374 -15.505 5.274   1.00 15.26 ?  62  GLN   B HB3  1 
ATOM   4634 H  HG2  . GLN   B 1 62  ? 56.903 -16.724 7.178   1.00 15.47 ?  62  GLN   B HG2  1 
ATOM   4635 H  HG3  . GLN   B 1 62  ? 56.312 -15.257 7.363   1.00 15.47 ?  62  GLN   B HG3  1 
ATOM   4636 H  HE21 . GLN   B 1 62  ? 54.169 -15.082 7.901   1.00 15.93 ?  62  GLN   B HE21 1 
ATOM   4637 H  HE22 . GLN   B 1 62  ? 53.163 -16.178 7.827   1.00 15.93 ?  62  GLN   B HE22 1 
ATOM   4638 N  N    . VAL   B 1 63  ? 56.801 -12.692 4.962   1.00 12.99 ?  63  VAL   B N    1 
ATOM   4639 C  CA   . VAL   B 1 63  ? 57.107 -11.375 5.515   1.00 13.90 ?  63  VAL   B CA   1 
ATOM   4640 C  C    . VAL   B 1 63  ? 55.917 -10.439 5.334   1.00 13.06 ?  63  VAL   B C    1 
ATOM   4641 O  O    . VAL   B 1 63  ? 55.499 -9.739  6.268   1.00 13.90 ?  63  VAL   B O    1 
ATOM   4642 C  CB   . VAL   B 1 63  ? 58.395 -10.815 4.889   1.00 15.44 ?  63  VAL   B CB   1 
ATOM   4643 C  CG1  . VAL   B 1 63  ? 58.626 -9.374  5.340   1.00 16.10 ?  63  VAL   B CG1  1 
ATOM   4644 C  CG2  . VAL   B 1 63  ? 59.581 -11.692 5.271   1.00 15.86 ?  63  VAL   B CG2  1 
ATOM   4645 H  H    . VAL   B 1 63  ? 57.308 -12.944 4.312   1.00 15.76 ?  63  VAL   B H    1 
ATOM   4646 H  HA   . VAL   B 1 63  ? 57.263 -11.474 6.464   1.00 16.85 ?  63  VAL   B HA   1 
ATOM   4647 H  HB   . VAL   B 1 63  ? 58.320 -10.827 3.922   1.00 18.69 ?  63  VAL   B HB   1 
ATOM   4648 H  HG11 . VAL   B 1 63  ? 59.543 -9.126  5.148   1.00 19.48 ?  63  VAL   B HG11 1 
ATOM   4649 H  HG12 . VAL   B 1 63  ? 58.017 -8.793  4.862   1.00 19.48 ?  63  VAL   B HG12 1 
ATOM   4650 H  HG13 . VAL   B 1 63  ? 58.463 -9.316  6.296   1.00 19.48 ?  63  VAL   B HG13 1 
ATOM   4651 H  HG21 . VAL   B 1 63  ? 60.392 -11.316 4.892   1.00 19.19 ?  63  VAL   B HG21 1 
ATOM   4652 H  HG22 . VAL   B 1 63  ? 59.656 -11.718 6.241   1.00 19.19 ?  63  VAL   B HG22 1 
ATOM   4653 H  HG23 . VAL   B 1 63  ? 59.441 -12.588 4.929   1.00 19.19 ?  63  VAL   B HG23 1 
ATOM   4654 N  N    . GLU   B 1 64  ? 55.346 -10.425 4.128   1.00 12.68 ?  64  GLU   B N    1 
ATOM   4655 C  CA   . GLU   B 1 64  ? 54.177 -9.593  3.859   1.00 12.55 ?  64  GLU   B CA   1 
ATOM   4656 C  C    . GLU   B 1 64  ? 52.994 -9.999  4.734   1.00 12.20 ?  64  GLU   B C    1 
ATOM   4657 O  O    . GLU   B 1 64  ? 52.246 -9.139  5.232   1.00 12.78 ?  64  GLU   B O    1 
ATOM   4658 C  CB   . GLU   B 1 64  ? 53.818 -9.726  2.377   1.00 12.56 ?  64  GLU   B CB   1 
ATOM   4659 C  CG   . GLU   B 1 64  ? 52.549 -9.000  1.950   1.00 12.96 ?  64  GLU   B CG   1 
ATOM   4660 C  CD   . GLU   B 1 64  ? 52.012 -9.499  0.615   1.00 13.61 ?  64  GLU   B CD   1 
ATOM   4661 O  OE1  . GLU   B 1 64  ? 52.192 -10.707 0.297   1.00 14.27 ?  64  GLU   B OE1  1 
ATOM   4662 O  OE2  . GLU   B 1 64  ? 51.394 -8.681  -0.108  1.00 14.25 -1 64  GLU   B OE2  1 
ATOM   4663 H  H    . GLU   B 1 64  ? 55.616 -10.891 3.450   1.00 15.38 ?  64  GLU   B H    1 
ATOM   4664 H  HA   . GLU   B 1 64  ? 54.391 -8.668  4.040   1.00 15.23 ?  64  GLU   B HA   1 
ATOM   4665 H  HB2  . GLU   B 1 64  ? 54.547 -9.358  1.846   1.00 15.24 ?  64  GLU   B HB2  1 
ATOM   4666 H  HB3  . GLU   B 1 64  ? 53.703 -10.662 2.165   1.00 15.24 ?  64  GLU   B HB3  1 
ATOM   4667 H  HG2  . GLU   B 1 64  ? 51.852 -9.133  2.614   1.00 15.72 ?  64  GLU   B HG2  1 
ATOM   4668 H  HG3  . GLU   B 1 64  ? 52.737 -8.051  1.861   1.00 15.72 ?  64  GLU   B HG3  1 
ATOM   4669 N  N    . SER   B 1 65  ? 52.813 -11.308 4.922   1.00 11.88 ?  65  SER   B N    1 
ATOM   4670 C  CA   . SER   B 1 65  ? 51.706 -11.814 5.722   1.00 11.97 ?  65  SER   B CA   1 
ATOM   4671 C  C    . SER   B 1 65  ? 51.841 -11.415 7.185   1.00 12.09 ?  65  SER   B C    1 
ATOM   4672 O  O    . SER   B 1 65  ? 50.840 -11.053 7.821   1.00 12.66 ?  65  SER   B O    1 
ATOM   4673 C  CB   . SER   B 1 65  ? 51.616 -13.335 5.589   1.00 12.12 ?  65  SER   B CB   1 
ATOM   4674 O  OG   . SER   B 1 65  ? 51.272 -13.731 4.271   1.00 12.26 ?  65  SER   B OG   1 
ATOM   4675 H  H    . SER   B 1 65  ? 53.322 -11.930 4.598   1.00 14.42 ?  65  SER   B H    1 
ATOM   4676 H  HA   . SER   B 1 65  ? 50.877 -11.440 5.385   1.00 14.53 ?  65  SER   B HA   1 
ATOM   4677 H  HB2  . SER   B 1 65  ? 52.472 -13.724 5.809   1.00 14.70 ?  65  SER   B HB2  1 
ATOM   4678 H  HB3  . SER   B 1 65  ? 50.934 -13.663 6.200   1.00 14.70 ?  65  SER   B HB3  1 
ATOM   4679 H  HG   . SER   B 1 65  ? 51.841 -13.438 3.720   1.00 14.88 ?  65  SER   B HG   1 
ATOM   4680 N  N    . ASP   B 1 66  ? 53.049 -11.519 7.751   1.00 12.49 ?  66  ASP   B N    1 
ATOM   4681 C  CA   . ASP   B 1 66  ? 53.237 -11.123 9.143   1.00 12.54 ?  66  ASP   B CA   1 
ATOM   4682 C  C    . ASP   B 1 66  ? 52.921 -9.644  9.344   1.00 12.95 ?  66  ASP   B C    1 
ATOM   4683 O  O    . ASP   B 1 66  ? 52.345 -9.256  10.369  1.00 13.45 ?  66  ASP   B O    1 
ATOM   4684 C  CB   . ASP   B 1 66  ? 54.670 -11.426 9.589   1.00 13.77 ?  66  ASP   B CB   1 
ATOM   4685 C  CG   . ASP   B 1 66  ? 54.938 -12.915 9.750   1.00 16.09 ?  66  ASP   B CG   1 
ATOM   4686 O  OD1  . ASP   B 1 66  ? 53.988 -13.729 9.670   1.00 16.69 ?  66  ASP   B OD1  1 
ATOM   4687 O  OD2  . ASP   B 1 66  ? 56.116 -13.280 9.973   1.00 18.64 -1 66  ASP   B OD2  1 
ATOM   4688 H  H    . ASP   B 1 66  ? 53.751 -11.818 7.360   1.00 15.16 ?  66  ASP   B H    1 
ATOM   4689 H  HA   . ASP   B 1 66  ? 52.635 -11.630 9.707   1.00 15.22 ?  66  ASP   B HA   1 
ATOM   4690 H  HB2  . ASP   B 1 66  ? 55.287 -11.088 8.923   1.00 16.68 ?  66  ASP   B HB2  1 
ATOM   4691 H  HB3  . ASP   B 1 66  ? 54.833 -10.992 10.444  1.00 16.68 ?  66  ASP   B HB3  1 
ATOM   4692 N  N    . ASP   B 1 67  ? 53.296 -8.802  8.382   1.00 12.61 ?  67  ASP   B N    1 
ATOM   4693 C  CA   . ASP   B 1 67  ? 52.947 -7.390  8.466   1.00 13.49 ?  67  ASP   B CA   1 
ATOM   4694 C  C    . ASP   B 1 67  ? 51.436 -7.185  8.382   1.00 13.69 ?  67  ASP   B C    1 
ATOM   4695 O  O    . ASP   B 1 67  ? 50.874 -6.370  9.125   1.00 14.02 ?  67  ASP   B O    1 
ATOM   4696 C  CB   . ASP   B 1 67  ? 53.665 -6.618  7.366   1.00 14.72 ?  67  ASP   B CB   1 
ATOM   4697 C  CG   . ASP   B 1 67  ? 53.235 -5.175  7.321   1.00 16.13 ?  67  ASP   B CG   1 
ATOM   4698 O  OD1  . ASP   B 1 67  ? 53.727 -4.359  8.137   1.00 17.59 ?  67  ASP   B OD1  1 
ATOM   4699 O  OD2  . ASP   B 1 67  ? 52.367 -4.875  6.488   1.00 17.34 -1 67  ASP   B OD2  1 
ATOM   4700 H  H    . ASP   B 1 67  ? 53.756 -9.019  7.686   1.00 15.29 ?  67  ASP   B H    1 
ATOM   4701 H  HA   . ASP   B 1 67  ? 53.251 -7.039  9.317   1.00 16.35 ?  67  ASP   B HA   1 
ATOM   4702 H  HB2  . ASP   B 1 67  ? 54.624 -6.647  7.527   1.00 17.83 ?  67  ASP   B HB2  1 
ATOM   4703 H  HB3  . ASP   B 1 67  ? 53.468 -7.031  6.505   1.00 17.83 ?  67  ASP   B HB3  1 
ATOM   4704 N  N    . TYR   B 1 68  ? 50.758 -7.920  7.494   1.00 13.28 ?  68  TYR   B N    1 
ATOM   4705 C  CA   . TYR   B 1 68  ? 49.301 -7.842  7.419   1.00 13.74 ?  68  TYR   B CA   1 
ATOM   4706 C  C    . TYR   B 1 68  ? 48.662 -8.180  8.764   1.00 13.28 ?  68  TYR   B C    1 
ATOM   4707 O  O    . TYR   B 1 68  ? 47.730 -7.500  9.214   1.00 13.80 ?  68  TYR   B O    1 
ATOM   4708 C  CB   . TYR   B 1 68  ? 48.767 -8.773  6.325   1.00 14.49 ?  68  TYR   B CB   1 
ATOM   4709 C  CG   . TYR   B 1 68  ? 47.262 -8.923  6.387   1.00 15.60 ?  68  TYR   B CG   1 
ATOM   4710 C  CD1  . TYR   B 1 68  ? 46.674 -9.882  7.204   1.00 16.41 ?  68  TYR   B CD1  1 
ATOM   4711 C  CD2  . TYR   B 1 68  ? 46.435 -8.080  5.670   1.00 16.73 ?  68  TYR   B CD2  1 
ATOM   4712 C  CE1  . TYR   B 1 68  ? 45.311 -10.004 7.297   1.00 17.48 ?  68  TYR   B CE1  1 
ATOM   4713 C  CE2  . TYR   B 1 68  ? 45.054 -8.203  5.748   1.00 17.13 ?  68  TYR   B CE2  1 
ATOM   4714 C  CZ   . TYR   B 1 68  ? 44.510 -9.165  6.565   1.00 17.23 ?  68  TYR   B CZ   1 
ATOM   4715 O  OH   . TYR   B 1 68  ? 43.143 -9.277  6.661   1.00 18.17 ?  68  TYR   B OH   1 
ATOM   4716 H  H    . TYR   B 1 68  ? 51.120 -8.470  6.930   1.00 16.10 ?  68  TYR   B H    1 
ATOM   4717 H  HA   . TYR   B 1 68  ? 49.053 -6.935  7.192   1.00 16.65 ?  68  TYR   B HA   1 
ATOM   4718 H  HB2  . TYR   B 1 68  ? 48.993 -8.406  5.458   1.00 17.55 ?  68  TYR   B HB2  1 
ATOM   4719 H  HB3  . TYR   B 1 68  ? 49.161 -9.651  6.433   1.00 17.55 ?  68  TYR   B HB3  1 
ATOM   4720 H  HD1  . TYR   B 1 68  ? 47.217 -10.455 7.704   1.00 19.85 ?  68  TYR   B HD1  1 
ATOM   4721 H  HD2  . TYR   B 1 68  ? 46.810 -7.425  5.132   1.00 20.25 ?  68  TYR   B HD2  1 
ATOM   4722 H  HE1  . TYR   B 1 68  ? 44.931 -10.661 7.842   1.00 21.15 ?  68  TYR   B HE1  1 
ATOM   4723 H  HE2  . TYR   B 1 68  ? 44.501 -7.632  5.269   1.00 20.72 ?  68  TYR   B HE2  1 
ATOM   4724 H  HH   . TYR   B 1 68  ? 42.756 -8.715  6.162   1.00 21.97 ?  68  TYR   B HH   1 
ATOM   4725 N  N    . ILE   B 1 69  ? 49.141 -9.250  9.409   1.00 12.94 ?  69  ILE   B N    1 
ATOM   4726 C  CA   . ILE   B 1 69  ? 48.591 -9.678  10.694  1.00 13.83 ?  69  ILE   B CA   1 
ATOM   4727 C  C    . ILE   B 1 69  ? 48.845 -8.630  11.771  1.00 13.30 ?  69  ILE   B C    1 
ATOM   4728 O  O    . ILE   B 1 69  ? 47.974 -8.354  12.605  1.00 13.87 ?  69  ILE   B O    1 
ATOM   4729 C  CB   . ILE   B 1 69  ? 49.172 -11.052 11.079  1.00 14.56 ?  69  ILE   B CB   1 
ATOM   4730 C  CG1  . ILE   B 1 69  ? 48.639 -12.153 10.151  1.00 14.80 ?  69  ILE   B CG1  1 
ATOM   4731 C  CG2  . ILE   B 1 69  ? 48.898 -11.373 12.542  1.00 15.53 ?  69  ILE   B CG2  1 
ATOM   4732 C  CD1  . ILE   B 1 69  ? 47.161 -12.467 10.314  1.00 15.04 ?  69  ILE   B CD1  1 
ATOM   4733 H  H    . ILE   B 1 69  ? 49.785 -9.743  9.125   1.00 15.69 ?  69  ILE   B H    1 
ATOM   4734 H  HA   . ILE   B 1 69  ? 47.634 -9.778  10.605  1.00 16.76 ?  69  ILE   B HA   1 
ATOM   4735 H  HB   . ILE   B 1 69  ? 50.136 -11.011 10.963  1.00 17.64 ?  69  ILE   B HB   1 
ATOM   4736 H  HG12 . ILE   B 1 69  ? 48.782 -11.875 9.232   1.00 17.93 ?  69  ILE   B HG12 1 
ATOM   4737 H  HG13 . ILE   B 1 69  ? 49.134 -12.969 10.324  1.00 17.93 ?  69  ILE   B HG13 1 
ATOM   4738 H  HG21 . ILE   B 1 69  ? 49.041 -12.324 12.685  1.00 18.80 ?  69  ILE   B HG21 1 
ATOM   4739 H  HG22 . ILE   B 1 69  ? 49.508 -10.865 13.100  1.00 18.80 ?  69  ILE   B HG22 1 
ATOM   4740 H  HG23 . ILE   B 1 69  ? 47.981 -11.143 12.750  1.00 18.80 ?  69  ILE   B HG23 1 
ATOM   4741 H  HD11 . ILE   B 1 69  ? 46.926 -13.185 9.707   1.00 18.22 ?  69  ILE   B HD11 1 
ATOM   4742 H  HD12 . ILE   B 1 69  ? 46.993 -12.740 11.229  1.00 18.22 ?  69  ILE   B HD12 1 
ATOM   4743 H  HD13 . ILE   B 1 69  ? 46.642 -11.675 10.104  1.00 18.22 ?  69  ILE   B HD13 1 
ATOM   4744 N  N    . ALA   B 1 70  ? 50.040 -8.041  11.790  1.00 13.51 ?  70  ALA   B N    1 
ATOM   4745 C  CA   . ALA   B 1 70  ? 50.319 -7.001  12.776  1.00 13.17 ?  70  ALA   B CA   1 
ATOM   4746 C  C    . ALA   B 1 70  ? 49.318 -5.859  12.667  1.00 13.50 ?  70  ALA   B C    1 
ATOM   4747 O  O    . ALA   B 1 70  ? 48.877 -5.312  13.683  1.00 14.00 ?  70  ALA   B O    1 
ATOM   4748 C  CB   . ALA   B 1 70  ? 51.748 -6.483  12.607  1.00 13.72 ?  70  ALA   B CB   1 
ATOM   4749 H  H    . ALA   B 1 70  ? 50.686 -8.221  11.262  1.00 16.37 ?  70  ALA   B H    1 
ATOM   4750 H  HA   . ALA   B 1 70  ? 50.247 -7.378  13.669  1.00 15.97 ?  70  ALA   B HA   1 
ATOM   4751 H  HB1  . ALA   B 1 70  ? 51.934 -5.831  13.301  1.00 16.62 ?  70  ALA   B HB1  1 
ATOM   4752 H  HB2  . ALA   B 1 70  ? 52.366 -7.228  12.682  1.00 16.62 ?  70  ALA   B HB2  1 
ATOM   4753 H  HB3  . ALA   B 1 70  ? 51.834 -6.071  11.733  1.00 16.62 ?  70  ALA   B HB3  1 
ATOM   4754 N  N    . THR   B 1 71  ? 48.948 -5.491  11.445  1.00 14.02 ?  71  THR   B N    1 
ATOM   4755 C  CA   . THR   B 1 71  ? 48.050 -4.361  11.236  1.00 14.91 ?  71  THR   B CA   1 
ATOM   4756 C  C    . THR   B 1 71  ? 46.583 -4.734  11.440  1.00 15.64 ?  71  THR   B C    1 
ATOM   4757 O  O    . THR   B 1 71  ? 45.799 -3.918  11.943  1.00 17.21 ?  71  THR   B O    1 
ATOM   4758 C  CB   . THR   B 1 71  ? 48.268 -3.798  9.830   1.00 16.82 ?  71  THR   B CB   1 
ATOM   4759 O  OG1  . THR   B 1 71  ? 49.597 -3.271  9.732   1.00 19.02 ?  71  THR   B OG1  1 
ATOM   4760 C  CG2  . THR   B 1 71  ? 47.255 -2.708  9.506   1.00 17.87 ?  71  THR   B CG2  1 
ATOM   4761 H  H    . THR   B 1 71  ? 49.200 -5.883  10.722  1.00 16.99 ?  71  THR   B H    1 
ATOM   4762 H  HA   . THR   B 1 71  ? 48.273 -3.665  11.871  1.00 18.05 ?  71  THR   B HA   1 
ATOM   4763 H  HB   . THR   B 1 71  ? 48.170 -4.508  9.178   1.00 20.34 ?  71  THR   B HB   1 
ATOM   4764 H  HG1  . THR   B 1 71  ? 49.725 -2.940  8.967   1.00 22.99 ?  71  THR   B HG1  1 
ATOM   4765 H  HG21 . THR   B 1 71  ? 47.555 -2.192  8.740   1.00 21.61 ?  71  THR   B HG21 1 
ATOM   4766 H  HG22 . THR   B 1 71  ? 46.394 -3.102  9.300   1.00 21.61 ?  71  THR   B HG22 1 
ATOM   4767 H  HG23 . THR   B 1 71  ? 47.157 -2.109  10.264  1.00 21.61 ?  71  THR   B HG23 1 
ATOM   4768 N  N    . ASN   B 1 72  ? 46.191 -5.952  11.057  1.00 15.19 ?  72  ASN   B N    1 
ATOM   4769 C  CA   . ASN   B 1 72  ? 44.787 -6.310  10.928  1.00 15.87 ?  72  ASN   B CA   1 
ATOM   4770 C  C    . ASN   B 1 72  ? 44.314 -7.404  11.873  1.00 16.27 ?  72  ASN   B C    1 
ATOM   4771 O  O    . ASN   B 1 72  ? 43.097 -7.562  12.038  1.00 17.37 ?  72  ASN   B O    1 
ATOM   4772 C  CB   . ASN   B 1 72  ? 44.488 -6.738  9.484   1.00 16.31 ?  72  ASN   B CB   1 
ATOM   4773 C  CG   . ASN   B 1 72  ? 44.756 -5.633  8.488   1.00 17.45 ?  72  ASN   B CG   1 
ATOM   4774 O  OD1  . ASN   B 1 72  ? 45.769 -5.640  7.782   1.00 18.78 ?  72  ASN   B OD1  1 
ATOM   4775 N  ND2  . ASN   B 1 72  ? 43.871 -4.656  8.450   1.00 19.26 ?  72  ASN   B ND2  1 
ATOM   4776 H  H    . ASN   B 1 72  ? 46.735 -6.598  10.863  1.00 18.39 ?  72  ASN   B H    1 
ATOM   4777 H  HA   . ASN   B 1 72  ? 44.257 -5.522  11.112  1.00 19.21 ?  72  ASN   B HA   1 
ATOM   4778 H  HB2  . ASN   B 1 72  ? 45.055 -7.494  9.254   1.00 19.73 ?  72  ASN   B HB2  1 
ATOM   4779 H  HB3  . ASN   B 1 72  ? 43.557 -6.987  9.414   1.00 19.73 ?  72  ASN   B HB3  1 
ATOM   4780 H  HD21 . ASN   B 1 72  ? 43.974 -4.002  7.901   1.00 23.27 ?  72  ASN   B HD21 1 
ATOM   4781 H  HD22 . ASN   B 1 72  ? 43.177 -4.684  8.959   1.00 23.27 ?  72  ASN   B HD22 1 
ATOM   4782 N  N    . GLY   B 1 73  ? 45.217 -8.156  12.496  1.00 15.68 ?  73  GLY   B N    1 
ATOM   4783 C  CA   . GLY   B 1 73  ? 44.824 -9.299  13.284  1.00 15.07 ?  73  GLY   B CA   1 
ATOM   4784 C  C    . GLY   B 1 73  ? 44.463 -10.481 12.411  1.00 13.87 ?  73  GLY   B C    1 
ATOM   4785 O  O    . GLY   B 1 73  ? 44.450 -10.395 11.181  1.00 13.72 ?  73  GLY   B O    1 
ATOM   4786 H  H    . GLY   B 1 73  ? 46.070 -8.022  12.473  1.00 18.98 ?  73  GLY   B H    1 
ATOM   4787 H  HA2  . GLY   B 1 73  ? 45.555 -9.556  13.872  1.00 18.25 ?  73  GLY   B HA2  1 
ATOM   4788 H  HA3  . GLY   B 1 73  ? 44.058 -9.066  13.834  1.00 18.25 ?  73  GLY   B HA3  1 
ATOM   4789 N  N    . PRO   B 1 74  ? 44.159 -11.609 13.046  1.00 14.27 ?  74  PRO   B N    1 
ATOM   4790 C  CA   . PRO   B 1 74  ? 43.907 -12.840 12.295  1.00 13.64 ?  74  PRO   B CA   1 
ATOM   4791 C  C    . PRO   B 1 74  ? 42.607 -12.785 11.505  1.00 13.06 ?  74  PRO   B C    1 
ATOM   4792 O  O    . PRO   B 1 74  ? 41.668 -12.046 11.822  1.00 14.37 ?  74  PRO   B O    1 
ATOM   4793 C  CB   . PRO   B 1 74  ? 43.831 -13.905 13.394  1.00 14.78 ?  74  PRO   B CB   1 
ATOM   4794 C  CG   . PRO   B 1 74  ? 43.368 -13.157 14.600  1.00 16.13 ?  74  PRO   B CG   1 
ATOM   4795 C  CD   . PRO   B 1 74  ? 44.043 -11.816 14.499  1.00 15.65 ?  74  PRO   B CD   1 
ATOM   4796 H  HA   . PRO   B 1 74  ? 44.649 -13.027 11.699  1.00 16.53 ?  74  PRO   B HA   1 
ATOM   4797 H  HB2  . PRO   B 1 74  ? 43.191 -14.587 13.141  1.00 17.90 ?  74  PRO   B HB2  1 
ATOM   4798 H  HB3  . PRO   B 1 74  ? 44.709 -14.286 13.538  1.00 17.90 ?  74  PRO   B HB3  1 
ATOM   4799 H  HG2  . PRO   B 1 74  ? 42.402 -13.060 14.575  1.00 19.52 ?  74  PRO   B HG2  1 
ATOM   4800 H  HG3  . PRO   B 1 74  ? 43.647 -13.624 15.401  1.00 19.52 ?  74  PRO   B HG3  1 
ATOM   4801 H  HD2  . PRO   B 1 74  ? 43.485 -11.128 14.908  1.00 18.94 ?  74  PRO   B HD2  1 
ATOM   4802 H  HD3  . PRO   B 1 74  ? 44.921 -11.846 14.906  1.00 18.94 ?  74  PRO   B HD3  1 
ATOM   4803 N  N    . LEU   B 1 75  ? 42.574 -13.601 10.455  1.00 12.50 ?  75  LEU   B N    1 
ATOM   4804 C  CA   . LEU   B 1 75  ? 41.365 -13.812 9.681   1.00 12.50 ?  75  LEU   B CA   1 
ATOM   4805 C  C    . LEU   B 1 75  ? 40.387 -14.667 10.483  1.00 12.96 ?  75  LEU   B C    1 
ATOM   4806 O  O    . LEU   B 1 75  ? 40.727 -15.236 11.522  1.00 14.18 ?  75  LEU   B O    1 
ATOM   4807 C  CB   . LEU   B 1 75  ? 41.692 -14.529 8.370   1.00 12.73 ?  75  LEU   B CB   1 
ATOM   4808 C  CG   . LEU   B 1 75  ? 42.532 -13.780 7.327   1.00 14.56 ?  75  LEU   B CG   1 
ATOM   4809 C  CD1  . LEU   B 1 75  ? 42.760 -14.632 6.080   1.00 15.79 ?  75  LEU   B CD1  1 
ATOM   4810 C  CD2  . LEU   B 1 75  ? 41.919 -12.459 6.947   1.00 17.82 ?  75  LEU   B CD2  1 
ATOM   4811 H  H    . LEU   B 1 75  ? 43.247 -14.057 10.170  1.00 15.16 ?  75  LEU   B H    1 
ATOM   4812 H  HA   . LEU   B 1 75  ? 40.946 -12.963 9.478   1.00 15.16 ?  75  LEU   B HA   1 
ATOM   4813 H  HB2  . LEU   B 1 75  ? 42.176 -15.345 8.584   1.00 15.44 ?  75  LEU   B HB2  1 
ATOM   4814 H  HB3  . LEU   B 1 75  ? 40.857 -14.767 7.936   1.00 15.44 ?  75  LEU   B HB3  1 
ATOM   4815 H  HG   . LEU   B 1 75  ? 43.403 -13.597 7.713   1.00 17.63 ?  75  LEU   B HG   1 
ATOM   4816 H  HD11 . LEU   B 1 75  ? 43.300 -14.129 5.447   1.00 19.12 ?  75  LEU   B HD11 1 
ATOM   4817 H  HD12 . LEU   B 1 75  ? 43.227 -15.446 6.332   1.00 19.12 ?  75  LEU   B HD12 1 
ATOM   4818 H  HD13 . LEU   B 1 75  ? 41.905 -14.851 5.683   1.00 19.12 ?  75  LEU   B HD13 1 
ATOM   4819 H  HD21 . LEU   B 1 75  ? 42.445 -12.061 6.238   1.00 21.55 ?  75  LEU   B HD21 1 
ATOM   4820 H  HD22 . LEU   B 1 75  ? 41.011 -12.610 6.645   1.00 21.55 ?  75  LEU   B HD22 1 
ATOM   4821 H  HD23 . LEU   B 1 75  ? 41.918 -11.879 7.725   1.00 21.55 ?  75  LEU   B HD23 1 
ATOM   4822 N  N    . LYS   B 1 76  ? 39.157 -14.754 9.980   1.00 14.20 ?  76  LYS   B N    1 
ATOM   4823 C  CA   . LYS   B 1 76  ? 38.174 -15.719 10.457  1.00 15.34 ?  76  LYS   B CA   1 
ATOM   4824 C  C    . LYS   B 1 76  ? 38.266 -16.991 9.617   1.00 13.86 ?  76  LYS   B C    1 
ATOM   4825 O  O    . LYS   B 1 76  ? 38.531 -16.934 8.418   1.00 13.51 ?  76  LYS   B O    1 
ATOM   4826 C  CB   . LYS   B 1 76  ? 36.752 -15.156 10.289  1.00 17.74 ?  76  LYS   B CB   1 
ATOM   4827 C  CG   . LYS   B 1 76  ? 36.486 -13.758 10.877  1.00 19.63 ?  76  LYS   B CG   1 
ATOM   4828 C  CD   . LYS   B 1 76  ? 35.084 -13.233 10.515  1.00 21.18 ?  76  LYS   B CD   1 
ATOM   4829 C  CE   . LYS   B 1 76  ? 34.823 -11.858 11.115  1.00 23.33 ?  76  LYS   B CE   1 
ATOM   4830 N  NZ   . LYS   B 1 76  ? 33.517 -11.286 10.692  1.00 24.02 ?  76  LYS   B NZ   1 
ATOM   4831 H  H    . LYS   B 1 76  ? 38.862 -14.253 9.348   1.00 17.20 ?  76  LYS   B H    1 
ATOM   4832 H  HA   . LYS   B 1 76  ? 38.327 -15.937 11.391  1.00 18.57 ?  76  LYS   B HA   1 
ATOM   4833 H  HB2  . LYS   B 1 76  ? 36.553 -15.109 9.341   1.00 21.45 ?  76  LYS   B HB2  1 
ATOM   4834 H  HB3  . LYS   B 1 76  ? 36.129 -15.766 10.716  1.00 21.45 ?  76  LYS   B HB3  1 
ATOM   4835 H  HG2  . LYS   B 1 76  ? 36.553 -13.801 11.843  1.00 23.72 ?  76  LYS   B HG2  1 
ATOM   4836 H  HG3  . LYS   B 1 76  ? 37.143 -13.136 10.524  1.00 23.72 ?  76  LYS   B HG3  1 
ATOM   4837 H  HD2  . LYS   B 1 76  ? 35.010 -13.160 9.549   1.00 25.57 ?  76  LYS   B HD2  1 
ATOM   4838 H  HD3  . LYS   B 1 76  ? 34.415 -13.845 10.856  1.00 25.57 ?  76  LYS   B HD3  1 
ATOM   4839 H  HE2  . LYS   B 1 76  ? 34.823 -11.932 12.082  1.00 28.16 ?  76  LYS   B HE2  1 
ATOM   4840 H  HE3  . LYS   B 1 76  ? 35.525 -11.250 10.830  1.00 28.16 ?  76  LYS   B HE3  1 
ATOM   4841 H  HZ1  . LYS   B 1 76  ? 33.400 -10.484 11.063  1.00 28.99 ?  76  LYS   B HZ1  1 
ATOM   4842 H  HZ2  . LYS   B 1 76  ? 33.492 -11.200 9.806   1.00 28.99 ?  76  LYS   B HZ2  1 
ATOM   4843 H  HZ3  . LYS   B 1 76  ? 32.852 -11.821 10.948  1.00 28.99 ?  76  LYS   B HZ3  1 
ATOM   4844 N  N    . VAL   B 1 77  ? 38.023 -18.146 10.247  1.00 14.67 ?  77  VAL   B N    1 
ATOM   4845 C  CA   . VAL   B 1 77  ? 37.819 -19.359 9.461   1.00 15.08 ?  77  VAL   B CA   1 
ATOM   4846 C  C    . VAL   B 1 77  ? 36.623 -19.131 8.547   1.00 13.80 ?  77  VAL   B C    1 
ATOM   4847 O  O    . VAL   B 1 77  ? 35.559 -18.687 8.996   1.00 13.79 ?  77  VAL   B O    1 
ATOM   4848 C  CB   . VAL   B 1 77  ? 37.624 -20.580 10.372  1.00 16.80 ?  77  VAL   B CB   1 
ATOM   4849 C  CG1  . VAL   B 1 77  ? 37.336 -21.816 9.527   1.00 17.36 ?  77  VAL   B CG1  1 
ATOM   4850 C  CG2  . VAL   B 1 77  ? 38.856 -20.802 11.251  1.00 18.02 ?  77  VAL   B CG2  1 
ATOM   4851 H  H    . VAL   B 1 77  ? 37.980 -18.246 11.096  1.00 17.77 ?  77  VAL   B H    1 
ATOM   4852 H  HA   . VAL   B 1 77  ? 38.595 -19.512 8.903   1.00 18.26 ?  77  VAL   B HA   1 
ATOM   4853 H  HB   . VAL   B 1 77  ? 36.858 -20.423 10.949  1.00 20.32 ?  77  VAL   B HB   1 
ATOM   4854 H  HG11 . VAL   B 1 77  ? 37.400 -22.600 10.092  1.00 20.99 ?  77  VAL   B HG11 1 
ATOM   4855 H  HG12 . VAL   B 1 77  ? 36.440 -21.749 9.157   1.00 20.99 ?  77  VAL   B HG12 1 
ATOM   4856 H  HG13 . VAL   B 1 77  ? 37.987 -21.866 8.812   1.00 20.99 ?  77  VAL   B HG13 1 
ATOM   4857 H  HG21 . VAL   B 1 77  ? 38.716 -21.599 11.783  1.00 21.79 ?  77  VAL   B HG21 1 
ATOM   4858 H  HG22 . VAL   B 1 77  ? 39.629 -20.911 10.680  1.00 21.79 ?  77  VAL   B HG22 1 
ATOM   4859 H  HG23 . VAL   B 1 77  ? 38.970 -20.032 11.828  1.00 21.79 ?  77  VAL   B HG23 1 
ATOM   4860 N  N    . GLY   B 1 78  ? 36.799 -19.407 7.258   1.00 13.04 ?  78  GLY   B N    1 
ATOM   4861 C  CA   . GLY   B 1 78  ? 35.821 -19.082 6.244   1.00 12.84 ?  78  GLY   B CA   1 
ATOM   4862 C  C    . GLY   B 1 78  ? 36.071 -17.767 5.542   1.00 12.19 ?  78  GLY   B C    1 
ATOM   4863 O  O    . GLY   B 1 78  ? 35.389 -17.479 4.552   1.00 12.52 ?  78  GLY   B O    1 
ATOM   4864 H  H    . GLY   B 1 78  ? 37.496 -19.799 6.941   1.00 15.81 ?  78  GLY   B H    1 
ATOM   4865 H  HA2  . GLY   B 1 78  ? 35.809 -19.778 5.573   1.00 15.57 ?  78  GLY   B HA2  1 
ATOM   4866 H  HA3  . GLY   B 1 78  ? 34.941 -19.037 6.651   1.00 15.57 ?  78  GLY   B HA3  1 
ATOM   4867 N  N    . GLY   B 1 79  ? 37.021 -16.963 6.029   1.00 12.39 ?  79  GLY   B N    1 
ATOM   4868 C  CA   . GLY   B 1 79  ? 37.322 -15.667 5.458   1.00 12.11 ?  79  GLY   B CA   1 
ATOM   4869 C  C    . GLY   B 1 79  ? 38.555 -15.683 4.565   1.00 11.70 ?  79  GLY   B C    1 
ATOM   4870 O  O    . GLY   B 1 79  ? 39.173 -16.716 4.317   1.00 11.97 ?  79  GLY   B O    1 
ATOM   4871 H  H    . GLY   B 1 79  ? 37.516 -17.159 6.702   1.00 15.03 ?  79  GLY   B H    1 
ATOM   4872 H  HA2  . GLY   B 1 79  ? 36.569 -15.360 4.927   1.00 14.69 ?  79  GLY   B HA2  1 
ATOM   4873 H  HA3  . GLY   B 1 79  ? 37.472 -15.026 6.171   1.00 14.69 ?  79  GLY   B HA3  1 
ATOM   4874 N  N    . SER   B 1 80  ? 38.917 -14.489 4.087   1.00 11.43 ?  80  SER   B N    1 
ATOM   4875 C  CA   . SER   B 1 80  ? 40.027 -14.357 3.151   1.00 11.06 ?  80  SER   B CA   1 
ATOM   4876 C  C    . SER   B 1 80  ? 40.604 -12.949 3.210   1.00 11.22 ?  80  SER   B C    1 
ATOM   4877 O  O    . SER   B 1 80  ? 39.990 -12.019 3.736   1.00 12.48 ?  80  SER   B O    1 
ATOM   4878 C  CB   . SER   B 1 80  ? 39.584 -14.655 1.715   1.00 11.71 ?  80  SER   B CB   1 
ATOM   4879 O  OG   . SER   B 1 80  ? 38.748 -13.631 1.212   1.00 12.94 ?  80  SER   B OG   1 
ATOM   4880 H  H    . SER   B 1 80  ? 38.548 -13.746 4.301   1.00 13.89 ?  80  SER   B H    1 
ATOM   4881 H  HA   . SER   B 1 80  ? 40.720 -14.989 3.397   1.00 13.44 ?  80  SER   B HA   1 
ATOM   4882 H  HB2  . SER   B 1 80  ? 40.367 -14.722 1.149   1.00 14.22 ?  80  SER   B HB2  1 
ATOM   4883 H  HB3  . SER   B 1 80  ? 39.094 -15.493 1.703   1.00 14.22 ?  80  SER   B HB3  1 
ATOM   4884 H  HG   . SER   B 1 80  ? 38.058 -13.562 1.696   1.00 15.69 ?  80  SER   B HG   1 
ATOM   4885 N  N    . CYS   B 1 81  ? 41.794 -12.805 2.630   1.00 11.05 ?  81  CYS   B N    1 
ATOM   4886 C  CA   . CYS   B 1 81  ? 42.340 -11.493 2.318   1.00 11.30 ?  81  CYS   B CA   1 
ATOM   4887 C  C    . CYS   B 1 81  ? 43.115 -11.579 1.012   1.00 10.46 ?  81  CYS   B C    1 
ATOM   4888 O  O    . CYS   B 1 81  ? 43.625 -12.644 0.641   1.00 11.64 ?  81  CYS   B O    1 
ATOM   4889 C  CB   . CYS   B 1 81  ? 43.236 -10.938 3.438   1.00 12.01 ?  81  CYS   B CB   1 
ATOM   4890 S  SG   . CYS   B 1 81  ? 44.752 -11.878 3.690   1.00 12.51 ?  81  CYS   B SG   1 
ATOM   4891 H  H    . CYS   B 1 81  ? 42.306 -13.461 2.393   1.00 13.42 ?  81  CYS   B H    1 
ATOM   4892 H  HA   . CYS   B 1 81  ? 41.609 -10.872 2.187   1.00 13.72 ?  81  CYS   B HA   1 
ATOM   4893 H  HB2  . CYS   B 1 81  ? 43.486 -10.028 3.219   1.00 14.58 ?  81  CYS   B HB2  1 
ATOM   4894 H  HB3  . CYS   B 1 81  ? 42.731 -10.947 4.271   1.00 14.58 ?  81  CYS   B HB3  1 
ATOM   4895 H  HG   . CYS   B 1 81  ? 45.372 -11.379 4.588   1.00 15.18 ?  81  CYS   B HG   1 
ATOM   4896 N  N    . VAL   B 1 82  ? 43.213 -10.437 0.332   1.00 10.86 ?  82  VAL   B N    1 
ATOM   4897 C  CA   . VAL   B 1 82  ? 43.979 -10.309 -0.905  1.00 10.95 ?  82  VAL   B CA   1 
ATOM   4898 C  C    . VAL   B 1 82  ? 45.317 -9.667  -0.582  1.00 11.29 ?  82  VAL   B C    1 
ATOM   4899 O  O    . VAL   B 1 82  ? 45.365 -8.549  -0.047  1.00 12.18 ?  82  VAL   B O    1 
ATOM   4900 C  CB   . VAL   B 1 82  ? 43.230 -9.471  -1.954  1.00 12.22 ?  82  VAL   B CB   1 
ATOM   4901 C  CG1  . VAL   B 1 82  ? 44.077 -9.320  -3.212  1.00 13.53 ?  82  VAL   B CG1  1 
ATOM   4902 C  CG2  . VAL   B 1 82  ? 41.881 -10.081 -2.271  1.00 13.23 ?  82  VAL   B CG2  1 
ATOM   4903 H  H    . VAL   B 1 82  ? 42.826 -9.702  0.568   1.00 13.20 ?  82  VAL   B H    1 
ATOM   4904 H  HA   . VAL   B 1 82  ? 44.141 -11.187 -1.279  1.00 13.30 ?  82  VAL   B HA   1 
ATOM   4905 H  HB   . VAL   B 1 82  ? 43.074 -8.585  -1.598  1.00 14.83 ?  82  VAL   B HB   1 
ATOM   4906 H  HG11 . VAL   B 1 82  ? 43.514 -9.005  -3.937  1.00 16.39 ?  82  VAL   B HG11 1 
ATOM   4907 H  HG12 . VAL   B 1 82  ? 44.784 -8.675  -3.044  1.00 16.39 ?  82  VAL   B HG12 1 
ATOM   4908 H  HG13 . VAL   B 1 82  ? 44.460 -10.180 -3.442  1.00 16.39 ?  82  VAL   B HG13 1 
ATOM   4909 H  HG21 . VAL   B 1 82  ? 41.445 -9.561  -2.966  1.00 16.04 ?  82  VAL   B HG21 1 
ATOM   4910 H  HG22 . VAL   B 1 82  ? 42.007 -10.996 -2.582  1.00 16.04 ?  82  VAL   B HG22 1 
ATOM   4911 H  HG23 . VAL   B 1 82  ? 41.333 -10.083 -1.470  1.00 16.04 ?  82  VAL   B HG23 1 
ATOM   4912 N  N    . LEU   B 1 83  ? 46.399 -10.352 -0.943  1.00 11.06 ?  83  LEU   B N    1 
ATOM   4913 C  CA   . LEU   B 1 83  ? 47.754 -9.831  -0.825  1.00 11.02 ?  83  LEU   B CA   1 
ATOM   4914 C  C    . LEU   B 1 83  ? 48.453 -9.976  -2.176  1.00 11.07 ?  83  LEU   B C    1 
ATOM   4915 O  O    . LEU   B 1 83  ? 47.850 -10.395 -3.168  1.00 10.94 ?  83  LEU   B O    1 
ATOM   4916 C  CB   . LEU   B 1 83  ? 48.511 -10.501 0.329   1.00 11.63 ?  83  LEU   B CB   1 
ATOM   4917 C  CG   . LEU   B 1 83  ? 47.994 -10.150 1.732   1.00 12.84 ?  83  LEU   B CG   1 
ATOM   4918 C  CD1  . LEU   B 1 83  ? 48.634 -11.015 2.802   1.00 13.21 ?  83  LEU   B CD1  1 
ATOM   4919 C  CD2  . LEU   B 1 83  ? 48.177 -8.661  2.068   1.00 13.61 ?  83  LEU   B CD2  1 
ATOM   4920 H  H    . LEU   B 1 83  ? 46.364 -11.150 -1.270  1.00 13.44 ?  83  LEU   B H    1 
ATOM   4921 H  HA   . LEU   B 1 83  ? 47.700 -8.888  -0.630  1.00 13.39 ?  83  LEU   B HA   1 
ATOM   4922 H  HB2  . LEU   B 1 83  ? 48.452 -11.460 0.230   1.00 14.12 ?  83  LEU   B HB2  1 
ATOM   4923 H  HB3  . LEU   B 1 83  ? 49.441 -10.224 0.288   1.00 14.12 ?  83  LEU   B HB3  1 
ATOM   4924 H  HG   . LEU   B 1 83  ? 47.041 -10.330 1.753   1.00 15.58 ?  83  LEU   B HG   1 
ATOM   4925 H  HD11 . LEU   B 1 83  ? 48.273 -10.765 3.670   1.00 16.01 ?  83  LEU   B HD11 1 
ATOM   4926 H  HD12 . LEU   B 1 83  ? 48.431 -11.946 2.619   1.00 16.01 ?  83  LEU   B HD12 1 
ATOM   4927 H  HD13 . LEU   B 1 83  ? 49.593 -10.877 2.793   1.00 16.01 ?  83  LEU   B HD13 1 
ATOM   4928 H  HD21 . LEU   B 1 83  ? 47.941 -8.519  2.999   1.00 16.50 ?  83  LEU   B HD21 1 
ATOM   4929 H  HD22 . LEU   B 1 83  ? 49.097 -8.413  1.914   1.00 16.50 ?  83  LEU   B HD22 1 
ATOM   4930 H  HD23 . LEU   B 1 83  ? 47.589 -8.137  1.498   1.00 16.50 ?  83  LEU   B HD23 1 
ATOM   4931 N  N    . SER   B 1 84  ? 49.732 -9.603  -2.232  1.00 12.06 ?  84  SER   B N    1 
ATOM   4932 C  CA   . SER   B 1 84  ? 50.463 -9.718  -3.485  1.00 12.19 ?  84  SER   B CA   1 
ATOM   4933 C  C    . SER   B 1 84  ? 50.623 -11.179 -3.894  1.00 11.51 ?  84  SER   B C    1 
ATOM   4934 O  O    . SER   B 1 84  ? 50.742 -12.074 -3.059  1.00 11.32 ?  84  SER   B O    1 
ATOM   4935 C  CB   . SER   B 1 84  ? 51.853 -9.103  -3.349  1.00 13.94 ?  84  SER   B CB   1 
ATOM   4936 O  OG   . SER   B 1 84  ? 52.602 -9.323  -4.529  1.00 15.63 ?  84  SER   B OG   1 
ATOM   4937 H  H    . SER   B 1 84  ? 50.184 -9.276  -1.575  1.00 14.63 ?  84  SER   B H    1 
ATOM   4938 H  HA   . SER   B 1 84  ? 49.985 -9.253  -4.188  1.00 14.79 ?  84  SER   B HA   1 
ATOM   4939 H  HB2  . SER   B 1 84  ? 51.763 -8.144  -3.196  1.00 16.89 ?  84  SER   B HB2  1 
ATOM   4940 H  HB3  . SER   B 1 84  ? 52.315 -9.512  -2.603  1.00 16.89 ?  84  SER   B HB3  1 
ATOM   4941 H  HG   . SER   B 1 84  ? 53.367 -8.967  -4.456  1.00 18.92 ?  84  SER   B HG   1 
ATOM   4942 N  N    . GLY   B 1 85  ? 50.681 -11.408 -5.198  1.00 12.66 ?  85  GLY   B N    1 
ATOM   4943 C  CA   . GLY   B 1 85  ? 51.034 -12.698 -5.739  1.00 13.04 ?  85  GLY   B CA   1 
ATOM   4944 C  C    . GLY   B 1 85  ? 52.505 -12.888 -6.044  1.00 12.44 ?  85  GLY   B C    1 
ATOM   4945 O  O    . GLY   B 1 85  ? 52.883 -13.967 -6.505  1.00 12.96 ?  85  GLY   B O    1 
ATOM   4946 H  H    . GLY   B 1 85  ? 50.527 -10.821 -5.799  1.00 15.35 ?  85  GLY   B H    1 
ATOM   4947 H  HA2  . GLY   B 1 85  ? 50.773 -13.391 -5.110  1.00 15.82 ?  85  GLY   B HA2  1 
ATOM   4948 H  HA3  . GLY   B 1 85  ? 50.548 -12.845 -6.561  1.00 15.82 ?  85  GLY   B HA3  1 
ATOM   4949 N  N    . HIS   B 1 86  ? 53.355 -11.888 -5.815  1.00 12.31 ?  86  HIS   B N    1 
ATOM   4950 C  CA   . HIS   B 1 86  ? 54.818 -12.054 -5.899  1.00 12.18 ?  86  HIS   B CA   1 
ATOM   4951 C  C    . HIS   B 1 86  ? 55.193 -12.562 -7.288  1.00 12.39 ?  86  HIS   B C    1 
ATOM   4952 O  O    . HIS   B 1 86  ? 54.802 -11.946 -8.292  1.00 13.34 ?  86  HIS   B O    1 
ATOM   4953 C  CB   . HIS   B 1 86  ? 55.317 -12.893 -4.725  1.00 12.41 ?  86  HIS   B CB   1 
ATOM   4954 C  CG   . HIS   B 1 86  ? 55.000 -12.291 -3.398  1.00 12.73 ?  86  HIS   B CG   1 
ATOM   4955 N  ND1  . HIS   B 1 86  ? 55.817 -11.366 -2.786  1.00 14.24 ?  86  HIS   B ND1  1 
ATOM   4956 C  CD2  . HIS   B 1 86  ? 53.928 -12.448 -2.586  1.00 13.32 ?  86  HIS   B CD2  1 
ATOM   4957 C  CE1  . HIS   B 1 86  ? 55.259 -10.981 -1.652  1.00 14.28 ?  86  HIS   B CE1  1 
ATOM   4958 N  NE2  . HIS   B 1 86  ? 54.111 -11.619 -1.508  1.00 13.56 ?  86  HIS   B NE2  1 
ATOM   4959 H  H    . HIS   B 1 86  ? 53.115 -11.095 -5.604  1.00 14.94 ?  86  HIS   B H    1 
ATOM   4960 H  HA   . HIS   B 1 86  ? 55.225 -11.182 -5.803  1.00 14.78 ?  86  HIS   B HA   1 
ATOM   4961 H  HB2  . HIS   B 1 86  ? 54.910 -13.771 -4.762  1.00 15.06 ?  86  HIS   B HB2  1 
ATOM   4962 H  HB3  . HIS   B 1 86  ? 56.286 -12.978 -4.784  1.00 15.06 ?  86  HIS   B HB3  1 
ATOM   4963 H  HD2  . HIS   B 1 86  ? 53.195 -13.006 -2.739  1.00 16.15 ?  86  HIS   B HD2  1 
ATOM   4964 H  HE1  . HIS   B 1 86  ? 55.616 -10.374 -1.046  1.00 17.30 ?  86  HIS   B HE1  1 
ATOM   4965 H  HE2  . HIS   B 1 86  ? 53.571 -11.548 -0.839  1.00 16.44 ?  86  HIS   B HE2  1 
ATOM   4966 N  N    . ASN   B 1 87  ? 55.954 -13.650 -7.395  1.00 12.88 ?  87  ASN   B N    1 
ATOM   4967 C  CA   . ASN   B 1 87  ? 56.352 -14.221 -8.672  1.00 13.71 ?  87  ASN   B CA   1 
ATOM   4968 C  C    . ASN   B 1 87  ? 55.371 -15.269 -9.174  1.00 13.49 ?  87  ASN   B C    1 
ATOM   4969 O  O    . ASN   B 1 87  ? 55.688 -15.984 -10.129 1.00 15.13 ?  87  ASN   B O    1 
ATOM   4970 C  CB   . ASN   B 1 87  ? 57.750 -14.841 -8.556  1.00 15.73 ?  87  ASN   B CB   1 
ATOM   4971 C  CG   . ASN   B 1 87  ? 57.814 -15.957 -7.521  1.00 16.77 ?  87  ASN   B CG   1 
ATOM   4972 O  OD1  . ASN   B 1 87  ? 57.172 -15.888 -6.469  1.00 15.56 ?  87  ASN   B OD1  1 
ATOM   4973 N  ND2  . ASN   B 1 87  ? 58.572 -17.011 -7.834  1.00 19.20 ?  87  ASN   B ND2  1 
ATOM   4974 H  H    . ASN   B 1 87  ? 56.255 -14.090 -6.720  1.00 15.62 ?  87  ASN   B H    1 
ATOM   4975 H  HA   . ASN   B 1 87  ? 56.394 -13.513 -9.330  1.00 16.62 ?  87  ASN   B HA   1 
ATOM   4976 H  HB2  . ASN   B 1 87  ? 58.002 -15.212 -9.417  1.00 19.04 ?  87  ASN   B HB2  1 
ATOM   4977 H  HB3  . ASN   B 1 87  ? 58.378 -14.152 -8.294  1.00 19.04 ?  87  ASN   B HB3  1 
ATOM   4978 H  HD21 . ASN   B 1 87  ? 58.644 -17.668 -7.287  1.00 23.20 ?  87  ASN   B HD21 1 
ATOM   4979 H  HD22 . ASN   B 1 87  ? 59.001 -17.027 -8.584  1.00 23.20 ?  87  ASN   B HD22 1 
ATOM   4980 N  N    . LEU   B 1 88  ? 54.194 -15.372 -8.555  1.00 12.72 ?  88  LEU   B N    1 
ATOM   4981 C  CA   . LEU   B 1 88  ? 53.215 -16.401 -8.885  1.00 12.89 ?  88  LEU   B CA   1 
ATOM   4982 C  C    . LEU   B 1 88  ? 51.979 -15.882 -9.600  1.00 12.71 ?  88  LEU   B C    1 
ATOM   4983 O  O    . LEU   B 1 88  ? 51.377 -16.627 -10.384 1.00 14.21 ?  88  LEU   B O    1 
ATOM   4984 C  CB   . LEU   B 1 88  ? 52.747 -17.088 -7.602  1.00 13.86 ?  88  LEU   B CB   1 
ATOM   4985 C  CG   . LEU   B 1 88  ? 53.852 -17.761 -6.804  1.00 15.96 ?  88  LEU   B CG   1 
ATOM   4986 C  CD1  . LEU   B 1 88  ? 53.349 -18.048 -5.402  1.00 17.37 ?  88  LEU   B CD1  1 
ATOM   4987 C  CD2  . LEU   B 1 88  ? 54.265 -19.038 -7.503  1.00 19.04 ?  88  LEU   B CD2  1 
ATOM   4988 H  H    . LEU   B 1 88  ? 53.936 -14.846 -7.920  1.00 15.43 ?  88  LEU   B H    1 
ATOM   4989 H  HA   . LEU   B 1 88  ? 53.631 -17.062 -9.450  1.00 15.63 ?  88  LEU   B HA   1 
ATOM   4990 H  HB2  . LEU   B 1 88  ? 52.331 -16.428 -7.028  1.00 16.80 ?  88  LEU   B HB2  1 
ATOM   4991 H  HB3  . LEU   B 1 88  ? 52.099 -17.771 -7.839  1.00 16.80 ?  88  LEU   B HB3  1 
ATOM   4992 H  HG   . LEU   B 1 88  ? 54.623 -17.174 -6.747  1.00 19.32 ?  88  LEU   B HG   1 
ATOM   4993 H  HD11 . LEU   B 1 88  ? 53.980 -18.630 -4.954  1.00 21.01 ?  88  LEU   B HD11 1 
ATOM   4994 H  HD12 . LEU   B 1 88  ? 53.269 -17.210 -4.921  1.00 21.01 ?  88  LEU   B HD12 1 
ATOM   4995 H  HD13 . LEU   B 1 88  ? 52.483 -18.479 -5.464  1.00 21.01 ?  88  LEU   B HD13 1 
ATOM   4996 H  HD21 . LEU   B 1 88  ? 54.944 -19.481 -6.973  1.00 23.01 ?  88  LEU   B HD21 1 
ATOM   4997 H  HD22 . LEU   B 1 88  ? 53.489 -19.611 -7.596  1.00 23.01 ?  88  LEU   B HD22 1 
ATOM   4998 H  HD23 . LEU   B 1 88  ? 54.621 -18.818 -8.379  1.00 23.01 ?  88  LEU   B HD23 1 
ATOM   4999 N  N    . ALA   B 1 89  ? 51.575 -14.646 -9.332  1.00 12.10 ?  89  ALA   B N    1 
ATOM   5000 C  CA   . ALA   B 1 89  ? 50.285 -14.146 -9.785  1.00 11.45 ?  89  ALA   B CA   1 
ATOM   5001 C  C    . ALA   B 1 89  ? 50.258 -12.656 -9.495  1.00 11.64 ?  89  ALA   B C    1 
ATOM   5002 O  O    . ALA   B 1 89  ? 51.093 -12.142 -8.749  1.00 12.58 ?  89  ALA   B O    1 
ATOM   5003 C  CB   . ALA   B 1 89  ? 49.145 -14.833 -9.036  1.00 11.81 ?  89  ALA   B CB   1 
ATOM   5004 H  H    . ALA   B 1 89  ? 52.019 -14.071 -8.874  1.00 14.68 ?  89  ALA   B H    1 
ATOM   5005 H  HA   . ALA   B 1 89  ? 50.174 -14.293 -10.740 1.00 13.90 ?  89  ALA   B HA   1 
ATOM   5006 H  HB1  . ALA   B 1 89  ? 48.296 -14.498 -9.373  1.00 14.34 ?  89  ALA   B HB1  1 
ATOM   5007 H  HB2  . ALA   B 1 89  ? 49.201 -15.791 -9.188  1.00 14.34 ?  89  ALA   B HB2  1 
ATOM   5008 H  HB3  . ALA   B 1 89  ? 49.227 -14.640 -8.093  1.00 14.34 ?  89  ALA   B HB3  1 
ATOM   5009 N  N    . LYS   B 1 90  ? 49.272 -11.961 -10.060 1.00 12.61 ?  90  LYS   B N    1 
ATOM   5010 C  CA   . LYS   B 1 90  ? 49.082 -10.572 -9.657  1.00 12.78 ?  90  LYS   B CA   1 
ATOM   5011 C  C    . LYS   B 1 90  ? 48.761 -10.495 -8.169  1.00 12.37 ?  90  LYS   B C    1 
ATOM   5012 O  O    . LYS   B 1 90  ? 49.404 -9.742  -7.419  1.00 13.60 ?  90  LYS   B O    1 
ATOM   5013 C  CB   . LYS   B 1 90  ? 47.998 -9.915  -10.509 1.00 14.39 ?  90  LYS   B CB   1 
ATOM   5014 C  CG   . LYS   B 1 90  ? 47.695 -8.478  -10.127 1.00 15.03 ?  90  LYS   B CG   1 
ATOM   5015 C  CD   . LYS   B 1 90  ? 48.904 -7.581  -10.224 1.00 17.61 ?  90  LYS   B CD   1 
ATOM   5016 C  CE   . LYS   B 1 90  ? 48.477 -6.166  -9.936  1.00 19.78 ?  90  LYS   B CE   1 
ATOM   5017 N  NZ   . LYS   B 1 90  ? 49.627 -5.234  -9.846  1.00 19.95 ?  90  LYS   B NZ   1 
ATOM   5018 H  H    . LYS   B 1 90  ? 48.719 -12.261 -10.651 1.00 15.30 ?  90  LYS   B H    1 
ATOM   5019 H  HA   . LYS   B 1 90  ? 49.907 -10.095 -9.808  1.00 15.51 ?  90  LYS   B HA   1 
ATOM   5020 H  HB2  . LYS   B 1 90  ? 48.287 -9.918  -11.437 1.00 17.43 ?  90  LYS   B HB2  1 
ATOM   5021 H  HB3  . LYS   B 1 90  ? 47.177 -10.429 -10.426 1.00 17.43 ?  90  LYS   B HB3  1 
ATOM   5022 H  HG2  . LYS   B 1 90  ? 47.010 -8.132  -10.723 1.00 18.20 ?  90  LYS   B HG2  1 
ATOM   5023 H  HG3  . LYS   B 1 90  ? 47.367 -8.455  -9.210  1.00 18.20 ?  90  LYS   B HG3  1 
ATOM   5024 H  HD2  . LYS   B 1 90  ? 49.565 -7.847  -9.565  1.00 21.29 ?  90  LYS   B HD2  1 
ATOM   5025 H  HD3  . LYS   B 1 90  ? 49.272 -7.624  -11.119 1.00 21.29 ?  90  LYS   B HD3  1 
ATOM   5026 H  HE2  . LYS   B 1 90  ? 47.898 -5.850  -10.650 1.00 23.90 ?  90  LYS   B HE2  1 
ATOM   5027 H  HE3  . LYS   B 1 90  ? 48.004 -6.133  -9.089  1.00 23.90 ?  90  LYS   B HE3  1 
ATOM   5028 H  HZ1  . LYS   B 1 90  ? 49.344 -4.405  -9.678  1.00 24.11 ?  90  LYS   B HZ1  1 
ATOM   5029 H  HZ2  . LYS   B 1 90  ? 50.176 -5.487  -9.193  1.00 24.11 ?  90  LYS   B HZ2  1 
ATOM   5030 H  HZ3  . LYS   B 1 90  ? 50.079 -5.230  -10.615 1.00 24.11 ?  90  LYS   B HZ3  1 
ATOM   5031 N  N    . HIS   B 1 91  ? 47.799 -11.310 -7.722  1.00 11.07 ?  91  HIS   B N    1 
ATOM   5032 C  CA   . HIS   B 1 91  ? 47.340 -11.338 -6.348  1.00 11.08 ?  91  HIS   B CA   1 
ATOM   5033 C  C    . HIS   B 1 91  ? 47.334 -12.767 -5.834  1.00 10.59 ?  91  HIS   B C    1 
ATOM   5034 O  O    . HIS   B 1 91  ? 47.093 -13.719 -6.588  1.00 11.16 ?  91  HIS   B O    1 
ATOM   5035 C  CB   . HIS   B 1 91  ? 45.885 -10.859 -6.227  1.00 12.58 ?  91  HIS   B CB   1 
ATOM   5036 C  CG   . HIS   B 1 91  ? 45.671 -9.449  -6.655  1.00 16.03 ?  91  HIS   B CG   1 
ATOM   5037 N  ND1  . HIS   B 1 91  ? 46.275 -8.377  -6.032  1.00 18.60 ?  91  HIS   B ND1  1 
ATOM   5038 C  CD2  . HIS   B 1 91  ? 44.890 -8.929  -7.627  1.00 18.35 ?  91  HIS   B CD2  1 
ATOM   5039 C  CE1  . HIS   B 1 91  ? 45.890 -7.256  -6.616  1.00 19.49 ?  91  HIS   B CE1  1 
ATOM   5040 N  NE2  . HIS   B 1 91  ? 45.044 -7.564  -7.584  1.00 19.53 ?  91  HIS   B NE2  1 
ATOM   5041 H  H    . HIS   B 1 91  ? 47.386 -11.877 -8.222  1.00 13.45 ?  91  HIS   B H    1 
ATOM   5042 H  HA   . HIS   B 1 91  ? 47.913 -10.785 -5.785  1.00 13.46 ?  91  HIS   B HA   1 
ATOM   5043 H  HB2  . HIS   B 1 91  ? 45.323 -11.422 -6.780  1.00 15.26 ?  91  HIS   B HB2  1 
ATOM   5044 H  HB3  . HIS   B 1 91  ? 45.607 -10.930 -5.298  1.00 15.26 ?  91  HIS   B HB3  1 
ATOM   5045 H  HD1  . HIS   B 1 91  ? 46.823 -8.431  -5.368  1.00 22.48 ?  91  HIS   B HD1  1 
ATOM   5046 H  HD2  . HIS   B 1 91  ? 44.355 -9.397  -8.222  1.00 22.19 ?  91  HIS   B HD2  1 
ATOM   5047 H  HE1  . HIS   B 1 91  ? 46.165 -6.397  -6.378  1.00 23.56 ?  91  HIS   B HE1  1 
ATOM   5048 N  N    . CYS   B 1 92  ? 47.529 -12.905 -4.530  1.00 10.63 ?  92  CYS   B N    1 
ATOM   5049 C  CA   . CYS   B 1 92  ? 47.222 -14.139 -3.819  1.00 9.98  ?  92  CYS   B CA   1 
ATOM   5050 C  C    . CYS   B 1 92  ? 46.001 -13.905 -2.938  1.00 9.56  ?  92  CYS   B C    1 
ATOM   5051 O  O    . CYS   B 1 92  ? 45.999 -12.997 -2.091  1.00 10.89 ?  92  CYS   B O    1 
ATOM   5052 C  CB   . CYS   B 1 92  ? 48.404 -14.601 -2.970  1.00 10.51 ?  92  CYS   B CB   1 
ATOM   5053 S  SG   . CYS   B 1 92  ? 48.051 -16.135 -2.072  1.00 10.83 ?  92  CYS   B SG   1 
ATOM   5054 H  H    . CYS   B 1 92  ? 47.862 -12.288 -4.023  1.00 12.92 ?  92  CYS   B H    1 
ATOM   5055 H  HA   . CYS   B 1 92  ? 47.022 -14.835 -4.463  1.00 12.15 ?  92  CYS   B HA   1 
ATOM   5056 H  HB2  . CYS   B 1 92  ? 49.168 -14.757 -3.541  1.00 12.78 ?  92  CYS   B HB2  1 
ATOM   5057 H  HB3  . CYS   B 1 92  ? 48.608 -13.915 -2.315  1.00 12.78 ?  92  CYS   B HB3  1 
ATOM   5058 H  HG   . CYS   B 1 92  ? 49.024 -16.449 -1.444  1.00 13.16 ?  92  CYS   B HG   1 
ATOM   5059 N  N    . LEU   B 1 93  ? 44.967 -14.714 -3.151  1.00 9.67  ?  93  LEU   B N    1 
ATOM   5060 C  CA   . LEU   B 1 93  ? 43.790 -14.728 -2.292  1.00 10.22 ?  93  LEU   B CA   1 
ATOM   5061 C  C    . LEU   B 1 93  ? 44.020 -15.789 -1.224  1.00 9.64  ?  93  LEU   B C    1 
ATOM   5062 O  O    . LEU   B 1 93  ? 43.972 -16.991 -1.512  1.00 10.33 ?  93  LEU   B O    1 
ATOM   5063 C  CB   . LEU   B 1 93  ? 42.531 -15.019 -3.102  1.00 10.43 ?  93  LEU   B CB   1 
ATOM   5064 C  CG   . LEU   B 1 93  ? 41.230 -15.042 -2.292  1.00 11.18 ?  93  LEU   B CG   1 
ATOM   5065 C  CD1  . LEU   B 1 93  ? 40.869 -13.659 -1.779  1.00 11.59 ?  93  LEU   B CD1  1 
ATOM   5066 C  CD2  . LEU   B 1 93  ? 40.102 -15.628 -3.126  1.00 11.46 ?  93  LEU   B CD2  1 
ATOM   5067 H  H    . LEU   B 1 93  ? 44.927 -15.285 -3.805  1.00 11.77 ?  93  LEU   B H    1 
ATOM   5068 H  HA   . LEU   B 1 93  ? 43.699 -13.867 -1.861  1.00 12.43 ?  93  LEU   B HA   1 
ATOM   5069 H  HB2  . LEU   B 1 93  ? 42.442 -14.328 -3.779  1.00 12.68 ?  93  LEU   B HB2  1 
ATOM   5070 H  HB3  . LEU   B 1 93  ? 42.629 -15.880 -3.526  1.00 12.68 ?  93  LEU   B HB3  1 
ATOM   5071 H  HG   . LEU   B 1 93  ? 41.353 -15.614 -1.524  1.00 13.58 ?  93  LEU   B HG   1 
ATOM   5072 H  HD11 . LEU   B 1 93  ? 40.018 -13.705 -1.317  1.00 14.07 ?  93  LEU   B HD11 1 
ATOM   5073 H  HD12 . LEU   B 1 93  ? 41.561 -13.355 -1.170  1.00 14.07 ?  93  LEU   B HD12 1 
ATOM   5074 H  HD13 . LEU   B 1 93  ? 40.802 -13.047 -2.532  1.00 14.07 ?  93  LEU   B HD13 1 
ATOM   5075 H  HD21 . LEU   B 1 93  ? 39.286 -15.626 -2.601  1.00 13.92 ?  93  LEU   B HD21 1 
ATOM   5076 H  HD22 . LEU   B 1 93  ? 39.981 -15.089 -3.925  1.00 13.92 ?  93  LEU   B HD22 1 
ATOM   5077 H  HD23 . LEU   B 1 93  ? 40.331 -16.538 -3.376  1.00 13.92 ?  93  LEU   B HD23 1 
ATOM   5078 N  N    . HIS   B 1 94  ? 44.293 -15.354 -0.002  1.00 9.51  ?  94  HIS   B N    1 
ATOM   5079 C  CA   . HIS   B 1 94  ? 44.516 -16.265 1.114   1.00 9.50  ?  94  HIS   B CA   1 
ATOM   5080 C  C    . HIS   B 1 94  ? 43.156 -16.622 1.692   1.00 10.15 ?  94  HIS   B C    1 
ATOM   5081 O  O    . HIS   B 1 94  ? 42.482 -15.745 2.239   1.00 11.67 ?  94  HIS   B O    1 
ATOM   5082 C  CB   . HIS   B 1 94  ? 45.385 -15.588 2.174   1.00 10.19 ?  94  HIS   B CB   1 
ATOM   5083 C  CG   . HIS   B 1 94  ? 46.767 -15.285 1.705   1.00 10.17 ?  94  HIS   B CG   1 
ATOM   5084 N  ND1  . HIS   B 1 94  ? 47.793 -16.200 1.786   1.00 10.38 ?  94  HIS   B ND1  1 
ATOM   5085 C  CD2  . HIS   B 1 94  ? 47.276 -14.173 1.119   1.00 10.41 ?  94  HIS   B CD2  1 
ATOM   5086 C  CE1  . HIS   B 1 94  ? 48.882 -15.649 1.280   1.00 10.49 ?  94  HIS   B CE1  1 
ATOM   5087 N  NE2  . HIS   B 1 94  ? 48.597 -14.424 0.869   1.00 10.72 ?  94  HIS   B NE2  1 
ATOM   5088 H  H    . HIS   B 1 94  ? 44.360 -14.520 0.207   1.00 11.57 ?  94  HIS   B H    1 
ATOM   5089 H  HA   . HIS   B 1 94  ? 44.959 -17.068 0.805   1.00 11.56 ?  94  HIS   B HA   1 
ATOM   5090 H  HB2  . HIS   B 1 94  ? 44.971 -14.753 2.435   1.00 12.40 ?  94  HIS   B HB2  1 
ATOM   5091 H  HB3  . HIS   B 1 94  ? 45.458 -16.178 2.940   1.00 12.40 ?  94  HIS   B HB3  1 
ATOM   5092 H  HD2  . HIS   B 1 94  ? 46.818 -13.386 0.928   1.00 12.65 ?  94  HIS   B HD2  1 
ATOM   5093 H  HE1  . HIS   B 1 94  ? 49.715 -16.062 1.225   1.00 12.76 ?  94  HIS   B HE1  1 
ATOM   5094 H  HE2  . HIS   B 1 94  ? 49.155 -13.877 0.508   1.00 13.03 ?  94  HIS   B HE2  1 
ATOM   5095 N  N    . VAL   B 1 95  ? 42.725 -17.877 1.541   1.00 10.04 ?  95  VAL   B N    1 
ATOM   5096 C  CA   . VAL   B 1 95  ? 41.397 -18.315 1.971   1.00 10.34 ?  95  VAL   B CA   1 
ATOM   5097 C  C    . VAL   B 1 95  ? 41.562 -19.351 3.070   1.00 10.62 ?  95  VAL   B C    1 
ATOM   5098 O  O    . VAL   B 1 95  ? 42.335 -20.304 2.917   1.00 11.14 ?  95  VAL   B O    1 
ATOM   5099 C  CB   . VAL   B 1 95  ? 40.576 -18.917 0.812   1.00 10.45 ?  95  VAL   B CB   1 
ATOM   5100 C  CG1  . VAL   B 1 95  ? 39.194 -19.355 1.296   1.00 11.63 ?  95  VAL   B CG1  1 
ATOM   5101 C  CG2  . VAL   B 1 95  ? 40.458 -17.939 -0.333  1.00 10.76 ?  95  VAL   B CG2  1 
ATOM   5102 H  H    . VAL   B 1 95  ? 43.196 -18.506 1.188   1.00 12.22 ?  95  VAL   B H    1 
ATOM   5103 H  HA   . VAL   B 1 95  ? 40.907 -17.563 2.335   1.00 12.57 ?  95  VAL   B HA   1 
ATOM   5104 H  HB   . VAL   B 1 95  ? 41.032 -19.704 0.482   1.00 12.70 ?  95  VAL   B HB   1 
ATOM   5105 H  HG11 . VAL   B 1 95  ? 38.637 -19.558 0.523   1.00 14.13 ?  95  VAL   B HG11 1 
ATOM   5106 H  HG12 . VAL   B 1 95  ? 39.281 -20.148 1.849   1.00 14.13 ?  95  VAL   B HG12 1 
ATOM   5107 H  HG13 . VAL   B 1 95  ? 38.790 -18.637 1.808   1.00 14.13 ?  95  VAL   B HG13 1 
ATOM   5108 H  HG21 . VAL   B 1 95  ? 39.886 -18.325 -1.015  1.00 13.08 ?  95  VAL   B HG21 1 
ATOM   5109 H  HG22 . VAL   B 1 95  ? 40.071 -17.115 -0.001  1.00 13.08 ?  95  VAL   B HG22 1 
ATOM   5110 H  HG23 . VAL   B 1 95  ? 41.341 -17.774 -0.692  1.00 13.08 ?  95  VAL   B HG23 1 
ATOM   5111 N  N    . VAL   B 1 96  ? 40.825 -19.184 4.163   1.00 10.87 ?  96  VAL   B N    1 
ATOM   5112 C  CA   . VAL   B 1 96  ? 40.907 -20.092 5.307   1.00 11.14 ?  96  VAL   B CA   1 
ATOM   5113 C  C    . VAL   B 1 96  ? 39.719 -21.053 5.259   1.00 11.65 ?  96  VAL   B C    1 
ATOM   5114 O  O    . VAL   B 1 96  ? 38.600 -20.697 5.639   1.00 12.28 ?  96  VAL   B O    1 
ATOM   5115 C  CB   . VAL   B 1 96  ? 40.958 -19.340 6.641   1.00 11.62 ?  96  VAL   B CB   1 
ATOM   5116 C  CG1  . VAL   B 1 96  ? 41.135 -20.330 7.788   1.00 12.51 ?  96  VAL   B CG1  1 
ATOM   5117 C  CG2  . VAL   B 1 96  ? 42.075 -18.301 6.650   1.00 12.90 ?  96  VAL   B CG2  1 
ATOM   5118 H  H    . VAL   B 1 96  ? 40.260 -18.548 4.268   1.00 13.21 ?  96  VAL   B H    1 
ATOM   5119 H  HA   . VAL   B 1 96  ? 41.718 -20.622 5.235   1.00 13.53 ?  96  VAL   B HA   1 
ATOM   5120 H  HB   . VAL   B 1 96  ? 40.116 -18.880 6.776   1.00 14.10 ?  96  VAL   B HB   1 
ATOM   5121 H  HG11 . VAL   B 1 96  ? 41.319 -19.837 8.605   1.00 15.18 ?  96  VAL   B HG11 1 
ATOM   5122 H  HG12 . VAL   B 1 96  ? 40.324 -20.849 7.894   1.00 15.18 ?  96  VAL   B HG12 1 
ATOM   5123 H  HG13 . VAL   B 1 96  ? 41.882 -20.918 7.588   1.00 15.18 ?  96  VAL   B HG13 1 
ATOM   5124 H  HG21 . VAL   B 1 96  ? 42.115 -17.883 7.528   1.00 15.64 ?  96  VAL   B HG21 1 
ATOM   5125 H  HG22 . VAL   B 1 96  ? 42.919 -18.736 6.454   1.00 15.64 ?  96  VAL   B HG22 1 
ATOM   5126 H  HG23 . VAL   B 1 96  ? 41.887 -17.626 5.977   1.00 15.64 ?  96  VAL   B HG23 1 
ATOM   5127 N  N    . GLY   B 1 97  ? 39.953 -22.284 4.812   1.00 11.72 ?  97  GLY   B N    1 
ATOM   5128 C  CA   . GLY   B 1 97  ? 38.984 -23.344 4.972   1.00 12.46 ?  97  GLY   B CA   1 
ATOM   5129 C  C    . GLY   B 1 97  ? 39.113 -23.954 6.349   1.00 13.59 ?  97  GLY   B C    1 
ATOM   5130 O  O    . GLY   B 1 97  ? 40.155 -23.833 7.005   1.00 14.07 ?  97  GLY   B O    1 
ATOM   5131 H  H    . GLY   B 1 97  ? 40.678 -22.522 4.410   1.00 14.23 ?  97  GLY   B H    1 
ATOM   5132 H  HA2  . GLY   B 1 97  ? 38.091 -22.981 4.858   1.00 15.12 ?  97  GLY   B HA2  1 
ATOM   5133 H  HA3  . GLY   B 1 97  ? 39.133 -24.027 4.300   1.00 15.12 ?  97  GLY   B HA3  1 
ATOM   5134 N  N    . PRO   B 1 98  ? 38.068 -24.637 6.812   1.00 14.35 ?  98  PRO   B N    1 
ATOM   5135 C  CA   . PRO   B 1 98  ? 38.163 -25.338 8.096   1.00 15.27 ?  98  PRO   B CA   1 
ATOM   5136 C  C    . PRO   B 1 98  ? 39.189 -26.460 8.053   1.00 14.86 ?  98  PRO   B C    1 
ATOM   5137 O  O    . PRO   B 1 98  ? 39.296 -27.198 7.075   1.00 15.22 ?  98  PRO   B O    1 
ATOM   5138 C  CB   . PRO   B 1 98  ? 36.746 -25.882 8.305   1.00 15.47 ?  98  PRO   B CB   1 
ATOM   5139 C  CG   . PRO   B 1 98  ? 36.176 -26.002 6.933   1.00 15.11 ?  98  PRO   B CG   1 
ATOM   5140 C  CD   . PRO   B 1 98  ? 36.750 -24.825 6.179   1.00 14.26 ?  98  PRO   B CD   1 
ATOM   5141 H  HA   . PRO   B 1 98  ? 38.385 -24.720 8.804   1.00 18.49 ?  98  PRO   B HA   1 
ATOM   5142 H  HB2  . PRO   B 1 98  ? 36.787 -26.752 8.736   1.00 18.73 ?  98  PRO   B HB2  1 
ATOM   5143 H  HB3  . PRO   B 1 98  ? 36.230 -25.258 8.836   1.00 18.73 ?  98  PRO   B HB3  1 
ATOM   5144 H  HG2  . PRO   B 1 98  ? 36.461 -26.840 6.530   1.00 18.30 ?  98  PRO   B HG2  1 
ATOM   5145 H  HG3  . PRO   B 1 98  ? 35.210 -25.950 6.970   1.00 18.30 ?  98  PRO   B HG3  1 
ATOM   5146 H  HD2  . PRO   B 1 98  ? 36.847 -25.040 5.233   1.00 17.28 ?  98  PRO   B HD2  1 
ATOM   5147 H  HD3  . PRO   B 1 98  ? 36.202 -24.036 6.306   1.00 17.28 ?  98  PRO   B HD3  1 
ATOM   5148 N  N    . ASN   B 1 99  ? 39.938 -26.585 9.138   1.00 16.10 ?  99  ASN   B N    1 
ATOM   5149 C  CA   . ASN   B 1 99  ? 40.912 -27.660 9.303   1.00 17.39 ?  99  ASN   B CA   1 
ATOM   5150 C  C    . ASN   B 1 99  ? 40.276 -28.743 10.176  1.00 19.80 ?  99  ASN   B C    1 
ATOM   5151 O  O    . ASN   B 1 99  ? 40.199 -28.601 11.398  1.00 20.28 ?  99  ASN   B O    1 
ATOM   5152 C  CB   . ASN   B 1 99  ? 42.184 -27.110 9.936   1.00 17.38 ?  99  ASN   B CB   1 
ATOM   5153 C  CG   . ASN   B 1 99  ? 43.318 -28.114 9.930   1.00 17.94 ?  99  ASN   B CG   1 
ATOM   5154 O  OD1  . ASN   B 1 99  ? 43.099 -29.306 10.094  1.00 18.82 ?  99  ASN   B OD1  1 
ATOM   5155 N  ND2  . ASN   B 1 99  ? 44.535 -27.635 9.731   1.00 18.33 ?  99  ASN   B ND2  1 
ATOM   5156 H  H    . ASN   B 1 99  ? 39.902 -26.048 9.805   1.00 19.48 ?  99  ASN   B H    1 
ATOM   5157 H  HA   . ASN   B 1 99  ? 41.128 -28.050 8.442   1.00 21.04 ?  99  ASN   B HA   1 
ATOM   5158 H  HB2  . ASN   B 1 99  ? 42.466 -26.332 9.445   1.00 21.03 ?  99  ASN   B HB2  1 
ATOM   5159 H  HB3  . ASN   B 1 99  ? 41.995 -26.879 10.861  1.00 21.03 ?  99  ASN   B HB3  1 
ATOM   5160 H  HD21 . ASN   B 1 99  ? 45.209 -28.166 9.714   1.00 22.16 ?  99  ASN   B HD21 1 
ATOM   5161 H  HD22 . ASN   B 1 99  ? 44.643 -26.792 9.618   1.00 22.16 ?  99  ASN   B HD22 1 
ATOM   5162 N  N    A VAL   B 1 100 ? 39.810 -29.822 9.540   0.60 21.87 ?  100 VAL   B N    1 
ATOM   5163 N  N    B VAL   B 1 100 ? 39.815 -29.823 9.538   0.40 21.90 ?  100 VAL   B N    1 
ATOM   5164 C  CA   A VAL   B 1 100 ? 39.194 -30.920 10.285  0.60 24.44 ?  100 VAL   B CA   1 
ATOM   5165 C  CA   B VAL   B 1 100 ? 39.198 -30.927 10.272  0.40 24.21 ?  100 VAL   B CA   1 
ATOM   5166 C  C    A VAL   B 1 100 ? 40.201 -31.586 11.215  0.60 24.70 ?  100 VAL   B C    1 
ATOM   5167 C  C    B VAL   B 1 100 ? 40.200 -31.588 11.209  0.40 24.68 ?  100 VAL   B C    1 
ATOM   5168 O  O    A VAL   B 1 100 ? 39.830 -32.099 12.277  0.60 25.29 ?  100 VAL   B O    1 
ATOM   5169 O  O    B VAL   B 1 100 ? 39.826 -32.094 12.274  0.40 25.11 ?  100 VAL   B O    1 
ATOM   5170 C  CB   A VAL   B 1 100 ? 38.537 -31.930 9.321   0.60 26.73 ?  100 VAL   B CB   1 
ATOM   5171 C  CB   B VAL   B 1 100 ? 38.572 -31.936 9.287   0.40 26.02 ?  100 VAL   B CB   1 
ATOM   5172 C  CG1  A VAL   B 1 100 ? 38.049 -33.161 10.078  0.60 27.63 ?  100 VAL   B CG1  1 
ATOM   5173 C  CG1  B VAL   B 1 100 ? 38.061 -33.170 10.024  0.40 26.71 ?  100 VAL   B CG1  1 
ATOM   5174 C  CG2  A VAL   B 1 100 ? 37.381 -31.279 8.574   0.60 27.27 ?  100 VAL   B CG2  1 
ATOM   5175 C  CG2  B VAL   B 1 100 ? 37.446 -31.279 8.506   0.40 26.52 ?  100 VAL   B CG2  1 
ATOM   5176 H  H    A VAL   B 1 100 ? 39.827 -29.937 8.688   0.60 26.41 ?  100 VAL   B H    1 
ATOM   5177 H  H    B VAL   B 1 100 ? 39.839 -29.938 8.685   0.40 26.45 ?  100 VAL   B H    1 
ATOM   5178 H  HA   A VAL   B 1 100 ? 38.485 -30.554 10.837  0.60 29.49 ?  100 VAL   B HA   1 
ATOM   5179 H  HA   B VAL   B 1 100 ? 38.478 -30.575 10.818  0.40 29.21 ?  100 VAL   B HA   1 
ATOM   5180 H  HB   A VAL   B 1 100 ? 39.192 -32.223 8.670   0.60 32.24 ?  100 VAL   B HB   1 
ATOM   5181 H  HB   B VAL   B 1 100 ? 39.248 -32.226 8.656   0.40 31.39 ?  100 VAL   B HB   1 
ATOM   5182 H  HG11 A VAL   B 1 100 ? 37.456 -33.671 9.501   0.60 33.32 ?  100 VAL   B HG11 1 
ATOM   5183 H  HG11 B VAL   B 1 100 ? 37.488 -33.679 9.427   0.40 32.22 ?  100 VAL   B HG11 1 
ATOM   5184 H  HG12 A VAL   B 1 100 ? 38.811 -33.707 10.328  0.60 33.32 ?  100 VAL   B HG12 1 
ATOM   5185 H  HG12 B VAL   B 1 100 ? 38.815 -33.716 10.297  0.40 32.22 ?  100 VAL   B HG12 1 
ATOM   5186 H  HG13 A VAL   B 1 100 ? 37.569 -32.876 10.871  0.60 33.32 ?  100 VAL   B HG13 1 
ATOM   5187 H  HG13 B VAL   B 1 100 ? 37.555 -32.889 10.802  0.40 32.22 ?  100 VAL   B HG13 1 
ATOM   5188 H  HG21 A VAL   B 1 100 ? 36.999 -31.926 7.959   0.60 32.89 ?  100 VAL   B HG21 1 
ATOM   5189 H  HG21 B VAL   B 1 100 ? 37.060 -31.931 7.901   0.40 31.98 ?  100 VAL   B HG21 1 
ATOM   5190 H  HG22 A VAL   B 1 100 ? 36.709 -30.999 9.216   0.60 32.89 ?  100 VAL   B HG22 1 
ATOM   5191 H  HG22 B VAL   B 1 100 ? 36.771 -30.966 9.129   0.40 31.98 ?  100 VAL   B HG22 1 
ATOM   5192 H  HG23 A VAL   B 1 100 ? 37.714 -30.513 8.085   0.60 32.89 ?  100 VAL   B HG23 1 
ATOM   5193 H  HG23 B VAL   B 1 100 ? 37.806 -30.533 8.004   0.40 31.98 ?  100 VAL   B HG23 1 
ATOM   5194 N  N    . ASN   B 1 101 ? 41.481 -31.611 10.831  1.00 25.19 ?  101 ASN   B N    1 
ATOM   5195 C  CA   . ASN   B 1 101 ? 42.517 -32.145 11.713  1.00 26.79 ?  101 ASN   B CA   1 
ATOM   5196 C  C    . ASN   B 1 101 ? 42.706 -31.307 12.972  1.00 29.17 ?  101 ASN   B C    1 
ATOM   5197 O  O    . ASN   B 1 101 ? 43.362 -31.773 13.913  1.00 30.49 ?  101 ASN   B O    1 
ATOM   5198 C  CB   . ASN   B 1 101 ? 43.846 -32.280 10.967  1.00 26.83 ?  101 ASN   B CB   1 
ATOM   5199 C  CG   . ASN   B 1 101 ? 43.840 -33.420 9.968   1.00 26.48 ?  101 ASN   B CG   1 
ATOM   5200 O  OD1  . ASN   B 1 101 ? 43.169 -34.427 10.170  1.00 26.94 ?  101 ASN   B OD1  1 
ATOM   5201 N  ND2  . ASN   B 1 101 ? 44.582 -33.261 8.879   1.00 26.06 ?  101 ASN   B ND2  1 
ATOM   5202 H  H    A ASN   B 1 101 ? 41.765 -31.344 10.064  0.60 30.40 ?  101 ASN   B H    1 
ATOM   5203 H  H    B ASN   B 1 101 ? 41.769 -31.333 10.069  0.40 30.40 ?  101 ASN   B H    1 
ATOM   5204 H  HA   . ASN   B 1 101 ? 42.251 -33.029 11.997  1.00 32.31 ?  101 ASN   B HA   1 
ATOM   5205 H  HB2  . ASN   B 1 101 ? 44.031 -31.462 10.482  1.00 32.36 ?  101 ASN   B HB2  1 
ATOM   5206 H  HB3  . ASN   B 1 101 ? 44.554 -32.450 11.610  1.00 32.36 ?  101 ASN   B HB3  1 
ATOM   5207 H  HD21 . ASN   B 1 101 ? 44.610 -33.880 8.284   1.00 31.44 ?  101 ASN   B HD21 1 
ATOM   5208 H  HD22 . ASN   B 1 101 ? 45.032 -32.536 8.768   1.00 31.44 ?  101 ASN   B HD22 1 
ATOM   5209 N  N    . LYS   B 1 102 ? 42.157 -30.090 13.005  1.00 31.70 ?  102 LYS   B N    1 
ATOM   5210 C  CA   . LYS   B 1 102 ? 42.126 -29.256 14.199  1.00 34.39 ?  102 LYS   B CA   1 
ATOM   5211 C  C    . LYS   B 1 102 ? 40.740 -29.206 14.830  1.00 33.86 ?  102 LYS   B C    1 
ATOM   5212 O  O    . LYS   B 1 102 ? 40.504 -28.383 15.721  1.00 34.63 ?  102 LYS   B O    1 
ATOM   5213 C  CB   . LYS   B 1 102 ? 42.576 -27.831 13.870  1.00 38.12 ?  102 LYS   B CB   1 
ATOM   5214 C  CG   . LYS   B 1 102 ? 44.041 -27.685 13.499  1.00 41.38 ?  102 LYS   B CG   1 
ATOM   5215 C  CD   . LYS   B 1 102 ? 44.322 -26.260 13.047  1.00 44.56 ?  102 LYS   B CD   1 
ATOM   5216 C  CE   . LYS   B 1 102 ? 45.805 -25.998 12.856  1.00 46.85 ?  102 LYS   B CE   1 
ATOM   5217 N  NZ   . LYS   B 1 102 ? 46.055 -24.596 12.409  1.00 48.13 ?  102 LYS   B NZ   1 
ATOM   5218 H  H    . LYS   B 1 102 ? 41.777 -29.717 12.327  1.00 38.20 ?  102 LYS   B H    1 
ATOM   5219 H  HA   . LYS   B 1 102 ? 42.745 -29.618 14.851  1.00 41.43 ?  102 LYS   B HA   1 
ATOM   5220 H  HB2  . LYS   B 1 102 ? 42.050 -27.506 13.122  1.00 45.91 ?  102 LYS   B HB2  1 
ATOM   5221 H  HB3  . LYS   B 1 102 ? 42.415 -27.269 14.646  1.00 45.91 ?  102 LYS   B HB3  1 
ATOM   5222 H  HG2  . LYS   B 1 102 ? 44.594 -27.878 14.273  1.00 49.82 ?  102 LYS   B HG2  1 
ATOM   5223 H  HG3  . LYS   B 1 102 ? 44.253 -28.288 12.770  1.00 49.82 ?  102 LYS   B HG3  1 
ATOM   5224 H  HD2  . LYS   B 1 102 ? 43.876 -26.102 12.199  1.00 53.63 ?  102 LYS   B HD2  1 
ATOM   5225 H  HD3  . LYS   B 1 102 ? 43.989 -25.642 13.717  1.00 53.63 ?  102 LYS   B HD3  1 
ATOM   5226 H  HE2  . LYS   B 1 102 ? 46.266 -26.136 13.698  1.00 56.38 ?  102 LYS   B HE2  1 
ATOM   5227 H  HE3  . LYS   B 1 102 ? 46.153 -26.600 12.180  1.00 56.38 ?  102 LYS   B HE3  1 
ATOM   5228 H  HZ1  . LYS   B 1 102 ? 46.928 -24.462 12.303  1.00 57.92 ?  102 LYS   B HZ1  1 
ATOM   5229 H  HZ2  . LYS   B 1 102 ? 45.643 -24.446 11.634  1.00 57.92 ?  102 LYS   B HZ2  1 
ATOM   5230 H  HZ3  . LYS   B 1 102 ? 45.746 -24.024 13.016  1.00 57.92 ?  102 LYS   B HZ3  1 
ATOM   5231 N  N    . GLY   B 1 103 ? 39.813 -30.047 14.377  1.00 33.19 ?  103 GLY   B N    1 
ATOM   5232 C  CA   . GLY   B 1 103 ? 38.478 -30.091 14.938  1.00 32.66 ?  103 GLY   B CA   1 
ATOM   5233 C  C    . GLY   B 1 103 ? 37.550 -28.989 14.484  1.00 31.53 ?  103 GLY   B C    1 
ATOM   5234 O  O    . GLY   B 1 103 ? 36.471 -28.833 15.067  1.00 32.20 ?  103 GLY   B O    1 
ATOM   5235 H  H    . GLY   B 1 103 ? 39.938 -30.604 13.737  1.00 39.99 ?  103 GLY   B H    1 
ATOM   5236 H  HA2  . GLY   B 1 103 ? 38.067 -30.938 14.705  1.00 39.36 ?  103 GLY   B HA2  1 
ATOM   5237 H  HA3  . GLY   B 1 103 ? 38.540 -30.045 15.906  1.00 39.36 ?  103 GLY   B HA3  1 
ATOM   5238 N  N    A GLU   B 1 104 ? 37.934 -28.216 13.472  0.60 30.36 ?  104 GLU   B N    1 
ATOM   5239 N  N    B GLU   B 1 104 ? 37.922 -28.227 13.461  0.40 30.53 ?  104 GLU   B N    1 
ATOM   5240 C  CA   A GLU   B 1 104 ? 37.111 -27.108 13.014  0.60 28.98 ?  104 GLU   B CA   1 
ATOM   5241 C  CA   B GLU   B 1 104 ? 37.075 -27.143 12.988  0.40 29.31 ?  104 GLU   B CA   1 
ATOM   5242 C  C    A GLU   B 1 104 ? 35.928 -27.617 12.197  0.60 29.49 ?  104 GLU   B C    1 
ATOM   5243 C  C    B GLU   B 1 104 ? 35.918 -27.685 12.154  0.40 29.43 ?  104 GLU   B C    1 
ATOM   5244 O  O    A GLU   B 1 104 ? 35.969 -28.701 11.606  0.60 30.07 ?  104 GLU   B O    1 
ATOM   5245 O  O    B GLU   B 1 104 ? 36.003 -28.758 11.550  0.40 29.76 ?  104 GLU   B O    1 
ATOM   5246 C  CB   A GLU   B 1 104 ? 37.958 -26.118 12.211  0.60 27.57 ?  104 GLU   B CB   1 
ATOM   5247 C  CB   B GLU   B 1 104 ? 37.905 -26.132 12.197  0.40 28.24 ?  104 GLU   B CB   1 
ATOM   5248 C  CG   A GLU   B 1 104 ? 39.065 -25.497 13.053  0.60 26.19 ?  104 GLU   B CG   1 
ATOM   5249 C  CG   B GLU   B 1 104 ? 38.988 -25.485 13.049  0.40 27.30 ?  104 GLU   B CG   1 
ATOM   5250 C  CD   A GLU   B 1 104 ? 39.991 -24.588 12.272  0.60 24.85 ?  104 GLU   B CD   1 
ATOM   5251 C  CD   B GLU   B 1 104 ? 39.942 -24.615 12.257  0.40 26.52 ?  104 GLU   B CD   1 
ATOM   5252 O  OE1  A GLU   B 1 104 ? 39.986 -24.630 11.024  0.60 23.00 ?  104 GLU   B OE1  1 
ATOM   5253 O  OE1  B GLU   B 1 104 ? 39.892 -24.637 11.010  0.40 25.71 ?  104 GLU   B OE1  1 
ATOM   5254 O  OE2  A GLU   B 1 104 ? 40.732 -23.825 12.924  0.60 24.80 -1 104 GLU   B OE2  1 
ATOM   5255 O  OE2  B GLU   B 1 104 ? 40.749 -23.907 12.894  0.40 26.38 -1 104 GLU   B OE2  1 
ATOM   5256 H  H    A GLU   B 1 104 ? 38.672 -28.309 13.040  0.60 36.59 ?  104 GLU   B H    1 
ATOM   5257 H  H    B GLU   B 1 104 ? 38.661 -28.313 13.030  0.40 36.81 ?  104 GLU   B H    1 
ATOM   5258 H  HA   A GLU   B 1 104 ? 36.762 -26.638 13.786  0.60 34.94 ?  104 GLU   B HA   1 
ATOM   5259 H  HA   B GLU   B 1 104 ? 36.702 -26.683 13.753  0.40 35.34 ?  104 GLU   B HA   1 
ATOM   5260 H  HB2  A GLU   B 1 104 ? 38.370 -26.580 11.464  0.60 33.25 ?  104 GLU   B HB2  1 
ATOM   5261 H  HB2  B GLU   B 1 104 ? 38.335 -26.582 11.454  0.40 34.06 ?  104 GLU   B HB2  1 
ATOM   5262 H  HB3  A GLU   B 1 104 ? 37.389 -25.401 11.887  0.60 33.25 ?  104 GLU   B HB3  1 
ATOM   5263 H  HB3  B GLU   B 1 104 ? 37.321 -25.430 11.869  0.40 34.06 ?  104 GLU   B HB3  1 
ATOM   5264 H  HG2  A GLU   B 1 104 ? 38.667 -24.967 13.761  0.60 31.60 ?  104 GLU   B HG2  1 
ATOM   5265 H  HG2  B GLU   B 1 104 ? 38.567 -24.929 13.724  0.40 32.92 ?  104 GLU   B HG2  1 
ATOM   5266 H  HG3  A GLU   B 1 104 ? 39.605 -26.205 13.438  0.60 31.60 ?  104 GLU   B HG3  1 
ATOM   5267 H  HG3  B GLU   B 1 104 ? 39.509 -26.182 13.478  0.40 32.92 ?  104 GLU   B HG3  1 
ATOM   5268 N  N    A ASP   B 1 105 ? 34.862 -26.820 12.179  0.60 29.11 ?  105 ASP   B N    1 
ATOM   5269 N  N    B ASP   B 1 105 ? 34.826 -26.924 12.133  0.40 28.87 ?  105 ASP   B N    1 
ATOM   5270 C  CA   A ASP   B 1 105 ? 33.583 -27.267 11.641  0.60 29.52 ?  105 ASP   B CA   1 
ATOM   5271 C  CA   B ASP   B 1 105 ? 33.567 -27.401 11.575  0.40 28.82 ?  105 ASP   B CA   1 
ATOM   5272 C  C    A ASP   B 1 105 ? 33.634 -27.328 10.119  0.60 27.51 ?  105 ASP   B C    1 
ATOM   5273 C  C    B ASP   B 1 105 ? 33.633 -27.413 10.052  0.40 27.66 ?  105 ASP   B C    1 
ATOM   5274 O  O    A ASP   B 1 105 ? 33.783 -26.298 9.453   0.60 26.56 ?  105 ASP   B O    1 
ATOM   5275 O  O    B ASP   B 1 105 ? 33.824 -26.368 9.421   0.40 27.11 ?  105 ASP   B O    1 
ATOM   5276 C  CB   A ASP   B 1 105 ? 32.479 -26.316 12.097  0.60 32.20 ?  105 ASP   B CB   1 
ATOM   5277 C  CB   B ASP   B 1 105 ? 32.422 -26.510 12.052  0.40 29.97 ?  105 ASP   B CB   1 
ATOM   5278 C  CG   A ASP   B 1 105 ? 31.102 -26.762 11.649  0.60 34.74 ?  105 ASP   B CG   1 
ATOM   5279 C  CG   B ASP   B 1 105 ? 31.057 -27.093 11.729  0.40 31.10 ?  105 ASP   B CG   1 
ATOM   5280 O  OD1  A ASP   B 1 105 ? 30.980 -27.884 11.114  0.60 35.04 ?  105 ASP   B OD1  1 
ATOM   5281 O  OD1  B ASP   B 1 105 ? 30.996 -28.085 10.971  0.40 31.32 ?  105 ASP   B OD1  1 
ATOM   5282 O  OD2  A ASP   B 1 105 ? 30.139 -25.983 11.824  0.60 36.20 -1 105 ASP   B OD2  1 
ATOM   5283 O  OD2  B ASP   B 1 105 ? 30.045 -26.570 12.244  0.40 31.28 -1 105 ASP   B OD2  1 
ATOM   5284 H  H    A ASP   B 1 105 ? 34.859 -26.011 12.472  0.60 35.09 ?  105 ASP   B H    1 
ATOM   5285 H  H    B ASP   B 1 105 ? 34.793 -26.123 12.433  0.40 34.81 ?  105 ASP   B H    1 
ATOM   5286 H  HA   A ASP   B 1 105 ? 33.383 -28.155 11.979  0.60 35.59 ?  105 ASP   B HA   1 
ATOM   5287 H  HA   B ASP   B 1 105 ? 33.393 -28.305 11.882  0.40 34.75 ?  105 ASP   B HA   1 
ATOM   5288 H  HB2  A ASP   B 1 105 ? 32.496 -26.253 13.068  0.60 38.81 ?  105 ASP   B HB2  1 
ATOM   5289 H  HB2  B ASP   B 1 105 ? 32.479 -26.405 13.016  0.40 36.12 ?  105 ASP   B HB2  1 
ATOM   5290 H  HB3  A ASP   B 1 105 ? 32.630 -25.444 11.706  0.60 38.81 ?  105 ASP   B HB3  1 
ATOM   5291 H  HB3  B ASP   B 1 105 ? 32.496 -25.640 11.623  0.40 36.12 ?  105 ASP   B HB3  1 
ATOM   5292 N  N    A ILE   B 1 106 ? 33.476 -28.536 9.571   0.60 26.95 ?  106 ILE   B N    1 
ATOM   5293 N  N    B ILE   B 1 106 ? 33.456 -28.599 9.464   0.40 27.09 ?  106 ILE   B N    1 
ATOM   5294 C  CA   A ILE   B 1 106 ? 33.482 -28.725 8.125   0.60 25.80 ?  106 ILE   B CA   1 
ATOM   5295 C  CA   B ILE   B 1 106 ? 33.468 -28.743 8.014   0.40 26.43 ?  106 ILE   B CA   1 
ATOM   5296 C  C    A ILE   B 1 106 ? 32.390 -27.907 7.443   0.60 24.21 ?  106 ILE   B C    1 
ATOM   5297 C  C    B ILE   B 1 106 ? 32.371 -27.918 7.354   0.40 25.46 ?  106 ILE   B C    1 
ATOM   5298 O  O    A ILE   B 1 106 ? 32.504 -27.588 6.256   0.60 23.40 ?  106 ILE   B O    1 
ATOM   5299 O  O    B ILE   B 1 106 ? 32.457 -27.617 6.158   0.40 25.11 ?  106 ILE   B O    1 
ATOM   5300 C  CB   A ILE   B 1 106 ? 33.390 -30.235 7.798   0.60 26.54 ?  106 ILE   B CB   1 
ATOM   5301 C  CB   B ILE   B 1 106 ? 33.376 -30.242 7.641   0.40 26.90 ?  106 ILE   B CB   1 
ATOM   5302 C  CG1  A ILE   B 1 106 ? 33.644 -30.492 6.312   0.60 26.96 ?  106 ILE   B CG1  1 
ATOM   5303 C  CG1  B ILE   B 1 106 ? 33.673 -30.456 6.155   0.40 27.14 ?  106 ILE   B CG1  1 
ATOM   5304 C  CG2  A ILE   B 1 106 ? 32.036 -30.797 8.213   0.60 27.08 ?  106 ILE   B CG2  1 
ATOM   5305 C  CG2  B ILE   B 1 106 ? 32.006 -30.803 8.001   0.40 27.33 ?  106 ILE   B CG2  1 
ATOM   5306 C  CD1  A ILE   B 1 106 ? 35.001 -30.023 5.841   0.60 27.05 ?  106 ILE   B CD1  1 
ATOM   5307 C  CD1  B ILE   B 1 106 ? 35.040 -29.967 5.735   0.40 27.20 ?  106 ILE   B CD1  1 
ATOM   5308 H  H    A ILE   B 1 106 ? 33.365 -29.259 10.021  0.60 32.50 ?  106 ILE   B H    1 
ATOM   5309 H  H    B ILE   B 1 106 ? 33.333 -29.334 9.888   0.40 32.67 ?  106 ILE   B H    1 
ATOM   5310 H  HA   A ILE   B 1 106 ? 34.329 -28.405 7.788   0.60 31.12 ?  106 ILE   B HA   1 
ATOM   5311 H  HA   B ILE   B 1 106 ? 34.314 -28.408 7.687   0.40 31.88 ?  106 ILE   B HA   1 
ATOM   5312 H  HB   A ILE   B 1 106 ? 34.075 -30.699 8.306   0.60 32.02 ?  106 ILE   B HB   1 
ATOM   5313 H  HB   B ILE   B 1 106 ? 34.042 -30.723 8.155   0.40 32.45 ?  106 ILE   B HB   1 
ATOM   5314 H  HG12 A ILE   B 1 106 ? 33.591 -31.448 6.146   0.60 32.52 ?  106 ILE   B HG12 1 
ATOM   5315 H  HG12 B ILE   B 1 106 ? 33.629 -31.407 5.962   0.40 32.73 ?  106 ILE   B HG12 1 
ATOM   5316 H  HG13 A ILE   B 1 106 ? 32.972 -30.031 5.791   0.60 32.52 ?  106 ILE   B HG13 1 
ATOM   5317 H  HG13 B ILE   B 1 106 ? 33.012 -29.984 5.628   0.40 32.73 ?  106 ILE   B HG13 1 
ATOM   5318 H  HG21 A ILE   B 1 106 ? 32.051 -31.762 8.115   0.60 32.67 ?  106 ILE   B HG21 1 
ATOM   5319 H  HG21 B ILE   B 1 106 ? 32.028 -31.769 7.908   0.40 32.96 ?  106 ILE   B HG21 1 
ATOM   5320 H  HG22 A ILE   B 1 106 ? 31.867 -30.562 9.139   0.60 32.67 ?  106 ILE   B HG22 1 
ATOM   5321 H  HG22 B ILE   B 1 106 ? 31.798 -30.565 8.918   0.40 32.96 ?  106 ILE   B HG22 1 
ATOM   5322 H  HG23 A ILE   B 1 106 ? 31.348 -30.418 7.645   0.60 32.67 ?  106 ILE   B HG23 1 
ATOM   5323 H  HG23 B ILE   B 1 106 ? 31.341 -30.430 7.403   0.40 32.96 ?  106 ILE   B HG23 1 
ATOM   5324 H  HD11 A ILE   B 1 106 ? 35.195 -30.431 4.984   0.60 32.62 ?  106 ILE   B HD11 1 
ATOM   5325 H  HD11 B ILE   B 1 106 ? 35.269 -30.368 4.884   0.40 32.81 ?  106 ILE   B HD11 1 
ATOM   5326 H  HD12 A ILE   B 1 106 ? 34.988 -29.056 5.751   0.60 32.62 ?  106 ILE   B HD12 1 
ATOM   5327 H  HD12 B ILE   B 1 106 ? 35.017 -29.001 5.651   0.40 32.81 ?  106 ILE   B HD12 1 
ATOM   5328 H  HD13 A ILE   B 1 106 ? 35.670 -30.287 6.492   0.60 32.62 ?  106 ILE   B HD13 1 
ATOM   5329 H  HD13 B ILE   B 1 106 ? 35.688 -30.228 6.409   0.40 32.81 ?  106 ILE   B HD13 1 
ATOM   5330 N  N    A GLN   B 1 107 ? 31.335 -27.540 8.175   0.60 24.63 ?  107 GLN   B N    1 
ATOM   5331 N  N    B GLN   B 1 107 ? 31.337 -27.536 8.107   0.40 25.51 ?  107 GLN   B N    1 
ATOM   5332 C  CA   A GLN   B 1 107 ? 30.261 -26.738 7.595   0.60 25.07 ?  107 GLN   B CA   1 
ATOM   5333 C  CA   B GLN   B 1 107 ? 30.258 -26.732 7.544   0.40 25.52 ?  107 GLN   B CA   1 
ATOM   5334 C  C    A GLN   B 1 107 ? 30.753 -25.392 7.075   0.60 22.78 ?  107 GLN   B C    1 
ATOM   5335 C  C    B GLN   B 1 107 ? 30.741 -25.365 7.075   0.40 23.12 ?  107 GLN   B C    1 
ATOM   5336 O  O    A GLN   B 1 107 ? 30.119 -24.821 6.182   0.60 23.23 ?  107 GLN   B O    1 
ATOM   5337 O  O    B GLN   B 1 107 ? 30.087 -24.751 6.226   0.40 23.52 ?  107 GLN   B O    1 
ATOM   5338 C  CB   A GLN   B 1 107 ? 29.153 -26.533 8.633   0.60 28.86 ?  107 GLN   B CB   1 
ATOM   5339 C  CB   B GLN   B 1 107 ? 29.137 -26.574 8.575   0.40 28.44 ?  107 GLN   B CB   1 
ATOM   5340 C  CG   A GLN   B 1 107 ? 27.827 -26.020 8.071   0.60 32.56 ?  107 GLN   B CG   1 
ATOM   5341 C  CG   B GLN   B 1 107 ? 27.812 -26.079 8.005   0.40 31.26 ?  107 GLN   B CG   1 
ATOM   5342 C  CD   A GLN   B 1 107 ? 27.771 -24.506 7.959   0.60 35.37 ?  107 GLN   B CD   1 
ATOM   5343 C  CD   B GLN   B 1 107 ? 27.696 -24.566 8.008   0.40 33.46 ?  107 GLN   B CD   1 
ATOM   5344 O  OE1  A GLN   B 1 107 ? 28.611 -23.797 8.515   0.60 36.37 ?  107 GLN   B OE1  1 
ATOM   5345 O  OE1  B GLN   B 1 107 ? 28.528 -23.867 8.589   0.40 34.27 ?  107 GLN   B OE1  1 
ATOM   5346 N  NE2  A GLN   B 1 107 ? 26.770 -24.003 7.238   0.60 36.32 ?  107 GLN   B NE2  1 
ATOM   5347 N  NE2  B GLN   B 1 107 ? 26.656 -24.052 7.359   0.40 34.19 ?  107 GLN   B NE2  1 
ATOM   5348 H  H    A GLN   B 1 107 ? 31.220 -27.740 8.999   0.60 29.72 ?  107 GLN   B H    1 
ATOM   5349 H  H    B GLN   B 1 107 ? 31.237 -27.727 8.938   0.40 30.78 ?  107 GLN   B H    1 
ATOM   5350 H  HA   A GLN   B 1 107 ? 29.879 -27.224 6.847   0.60 30.25 ?  107 GLN   B HA   1 
ATOM   5351 H  HA   B GLN   B 1 107 ? 29.889 -27.197 6.776   0.40 30.79 ?  107 GLN   B HA   1 
ATOM   5352 H  HB2  A GLN   B 1 107 ? 28.976 -27.381 9.064   0.60 34.79 ?  107 GLN   B HB2  1 
ATOM   5353 H  HB2  B GLN   B 1 107 ? 28.972 -27.435 8.984   0.40 34.29 ?  107 GLN   B HB2  1 
ATOM   5354 H  HB3  A GLN   B 1 107 ? 29.462 -25.892 9.292   0.60 34.79 ?  107 GLN   B HB3  1 
ATOM   5355 H  HB3  B GLN   B 1 107 ? 29.424 -25.941 9.252   0.40 34.29 ?  107 GLN   B HB3  1 
ATOM   5356 H  HG2  A GLN   B 1 107 ? 27.694 -26.387 7.185   0.60 39.24 ?  107 GLN   B HG2  1 
ATOM   5357 H  HG2  B GLN   B 1 107 ? 27.726 -26.382 7.088   0.40 37.67 ?  107 GLN   B HG2  1 
ATOM   5358 H  HG3  A GLN   B 1 107 ? 27.105 -26.306 8.658   0.60 39.24 ?  107 GLN   B HG3  1 
ATOM   5359 H  HG3  B GLN   B 1 107 ? 27.084 -26.439 8.541   0.40 37.67 ?  107 GLN   B HG3  1 
ATOM   5360 H  HE21 A GLN   B 1 107 ? 26.202 -24.529 6.862   0.60 43.75 ?  107 GLN   B HE21 1 
ATOM   5361 H  HE21 B GLN   B 1 107 ? 26.096 -24.571 6.963   0.40 41.19 ?  107 GLN   B HE21 1 
ATOM   5362 H  HE22 A GLN   B 1 107 ? 26.688 -23.151 7.147   0.60 43.75 ?  107 GLN   B HE22 1 
ATOM   5363 H  HE22 B GLN   B 1 107 ? 26.543 -23.200 7.334   0.40 41.19 ?  107 GLN   B HE22 1 
ATOM   5364 N  N    . LEU   B 1 108 ? 31.872 -24.879 7.595   1.00 20.80 ?  108 LEU   B N    1 
ATOM   5365 C  CA   . LEU   B 1 108 ? 32.409 -23.579 7.184   1.00 18.20 ?  108 LEU   B CA   1 
ATOM   5366 C  C    . LEU   B 1 108 ? 33.056 -23.600 5.809   1.00 16.01 ?  108 LEU   B C    1 
ATOM   5367 O  O    . LEU   B 1 108 ? 33.485 -22.543 5.320   1.00 15.53 ?  108 LEU   B O    1 
ATOM   5368 C  CB   . LEU   B 1 108 ? 33.411 -23.080 8.222   1.00 19.14 ?  108 LEU   B CB   1 
ATOM   5369 C  CG   . LEU   B 1 108 ? 32.783 -22.604 9.530   1.00 20.65 ?  108 LEU   B CG   1 
ATOM   5370 C  CD1  . LEU   B 1 108 ? 33.800 -22.595 10.656  1.00 20.90 ?  108 LEU   B CD1  1 
ATOM   5371 C  CD2  . LEU   B 1 108 ? 32.204 -21.215 9.336   1.00 21.62 ?  108 LEU   B CD2  1 
ATOM   5372 H  H    A LEU   B 1 108 ? 32.333 -25.268 8.204   0.60 25.12 ?  108 LEU   B H    1 
ATOM   5373 H  H    B LEU   B 1 108 ? 32.336 -25.281 8.194   0.40 25.12 ?  108 LEU   B H    1 
ATOM   5374 H  HA   . LEU   B 1 108 ? 31.677 -22.946 7.153   1.00 22.01 ?  108 LEU   B HA   1 
ATOM   5375 H  HB2  . LEU   B 1 108 ? 34.019 -23.802 8.439   1.00 23.13 ?  108 LEU   B HB2  1 
ATOM   5376 H  HB3  . LEU   B 1 108 ? 33.901 -22.337 7.845   1.00 23.13 ?  108 LEU   B HB3  1 
ATOM   5377 H  HG   . LEU   B 1 108 ? 32.058 -23.201 9.777   1.00 24.94 ?  108 LEU   B HG   1 
ATOM   5378 H  HD11 . LEU   B 1 108 ? 33.363 -22.306 11.474  1.00 25.25 ?  108 LEU   B HD11 1 
ATOM   5379 H  HD12 . LEU   B 1 108 ? 34.153 -23.490 10.769  1.00 25.25 ?  108 LEU   B HD12 1 
ATOM   5380 H  HD13 . LEU   B 1 108 ? 34.515 -21.981 10.430  1.00 25.25 ?  108 LEU   B HD13 1 
ATOM   5381 H  HD21 . LEU   B 1 108 ? 31.830 -20.908 10.176  1.00 26.11 ?  108 LEU   B HD21 1 
ATOM   5382 H  HD22 . LEU   B 1 108 ? 32.911 -20.616 9.049   1.00 26.11 ?  108 LEU   B HD22 1 
ATOM   5383 H  HD23 . LEU   B 1 108 ? 31.508 -21.253 8.660   1.00 26.11 ?  108 LEU   B HD23 1 
ATOM   5384 N  N    . LEU   B 1 109 ? 33.124 -24.767 5.175   1.00 14.96 ?  109 LEU   B N    1 
ATOM   5385 C  CA   . LEU   B 1 109 ? 33.762 -24.867 3.872   1.00 13.99 ?  109 LEU   B CA   1 
ATOM   5386 C  C    . LEU   B 1 109 ? 32.999 -24.084 2.811   1.00 13.30 ?  109 LEU   B C    1 
ATOM   5387 O  O    . LEU   B 1 109 ? 33.616 -23.493 1.917   1.00 13.05 ?  109 LEU   B O    1 
ATOM   5388 C  CB   . LEU   B 1 109 ? 33.877 -26.339 3.491   1.00 14.19 ?  109 LEU   B CB   1 
ATOM   5389 C  CG   . LEU   B 1 109 ? 34.667 -26.686 2.235   1.00 13.85 ?  109 LEU   B CG   1 
ATOM   5390 C  CD1  . LEU   B 1 109 ? 36.040 -26.032 2.248   1.00 13.77 ?  109 LEU   B CD1  1 
ATOM   5391 C  CD2  . LEU   B 1 109 ? 34.795 -28.201 2.118   1.00 14.74 ?  109 LEU   B CD2  1 
ATOM   5392 H  H    . LEU   B 1 109 ? 32.813 -25.510 5.472   1.00 18.11 ?  109 LEU   B H    1 
ATOM   5393 H  HA   . LEU   B 1 109 ? 34.658 -24.501 3.927   1.00 16.95 ?  109 LEU   B HA   1 
ATOM   5394 H  HB2  . LEU   B 1 109 ? 34.301 -26.809 4.225   1.00 17.20 ?  109 LEU   B HB2  1 
ATOM   5395 H  HB3  . LEU   B 1 109 ? 32.982 -26.691 3.364   1.00 17.20 ?  109 LEU   B HB3  1 
ATOM   5396 H  HG   . LEU   B 1 109 ? 34.186 -26.374 1.452   1.00 16.78 ?  109 LEU   B HG   1 
ATOM   5397 H  HD11 . LEU   B 1 109 ? 36.576 -26.401 1.527   1.00 16.68 ?  109 LEU   B HD11 1 
ATOM   5398 H  HD12 . LEU   B 1 109 ? 35.934 -25.078 2.126   1.00 16.68 ?  109 LEU   B HD12 1 
ATOM   5399 H  HD13 . LEU   B 1 109 ? 36.467 -26.215 3.100   1.00 16.68 ?  109 LEU   B HD13 1 
ATOM   5400 H  HD21 . LEU   B 1 109 ? 35.356 -28.417 1.354   1.00 17.85 ?  109 LEU   B HD21 1 
ATOM   5401 H  HD22 . LEU   B 1 109 ? 35.197 -28.550 2.929   1.00 17.85 ?  109 LEU   B HD22 1 
ATOM   5402 H  HD23 . LEU   B 1 109 ? 33.912 -28.588 1.995   1.00 17.85 ?  109 LEU   B HD23 1 
ATOM   5403 N  N    . LYS   B 1 110 ? 31.664 -24.058 2.887   1.00 13.15 ?  110 LYS   B N    1 
ATOM   5404 C  CA   . LYS   B 1 110 ? 30.906 -23.295 1.901   1.00 13.01 ?  110 LYS   B CA   1 
ATOM   5405 C  C    . LYS   B 1 110 ? 31.245 -21.808 1.990   1.00 12.90 ?  110 LYS   B C    1 
ATOM   5406 O  O    . LYS   B 1 110 ? 31.500 -21.156 0.972   1.00 12.59 ?  110 LYS   B O    1 
ATOM   5407 C  CB   . LYS   B 1 110 ? 29.400 -23.544 2.050   1.00 13.47 ?  110 LYS   B CB   1 
ATOM   5408 C  CG   . LYS   B 1 110 ? 28.589 -22.913 0.913   1.00 14.04 ?  110 LYS   B CG   1 
ATOM   5409 C  CD   . LYS   B 1 110 ? 27.125 -23.353 0.916   1.00 14.36 ?  110 LYS   B CD   1 
ATOM   5410 C  CE   . LYS   B 1 110 ? 26.367 -22.809 -0.301  1.00 14.99 ?  110 LYS   B CE   1 
ATOM   5411 N  NZ   . LYS   B 1 110 ? 26.696 -23.530 -1.562  1.00 15.22 ?  110 LYS   B NZ   1 
ATOM   5412 H  H    . LYS   B 1 110 ? 31.197 -24.469 3.476   1.00 15.95 ?  110 LYS   B H    1 
ATOM   5413 H  HA   . LYS   B 1 110 ? 31.161 -23.597 1.015   1.00 15.78 ?  110 LYS   B HA   1 
ATOM   5414 H  HB2  . LYS   B 1 110 ? 29.232 -24.505 2.039   1.00 16.33 ?  110 LYS   B HB2  1 
ATOM   5415 H  HB3  . LYS   B 1 110 ? 29.092 -23.167 2.888   1.00 16.33 ?  110 LYS   B HB3  1 
ATOM   5416 H  HG2  . LYS   B 1 110 ? 28.609 -21.947 1.007   1.00 17.01 ?  110 LYS   B HG2  1 
ATOM   5417 H  HG3  . LYS   B 1 110 ? 28.977 -23.171 0.062   1.00 17.01 ?  110 LYS   B HG3  1 
ATOM   5418 H  HD2  . LYS   B 1 110 ? 27.080 -24.325 0.890   1.00 17.39 ?  110 LYS   B HD2  1 
ATOM   5419 H  HD3  . LYS   B 1 110 ? 26.689 -23.022 1.718   1.00 17.39 ?  110 LYS   B HD3  1 
ATOM   5420 H  HE2  . LYS   B 1 110 ? 25.415 -22.893 -0.150  1.00 18.15 ?  110 LYS   B HE2  1 
ATOM   5421 H  HE3  . LYS   B 1 110 ? 26.602 -21.873 -0.424  1.00 18.15 ?  110 LYS   B HE3  1 
ATOM   5422 H  HZ1  . LYS   B 1 110 ? 26.242 -23.180 -2.241  1.00 18.42 ?  110 LYS   B HZ1  1 
ATOM   5423 H  HZ2  . LYS   B 1 110 ? 27.570 -23.460 -1.733  1.00 18.42 ?  110 LYS   B HZ2  1 
ATOM   5424 H  HZ3  . LYS   B 1 110 ? 26.487 -24.390 -1.483  1.00 18.42 ?  110 LYS   B HZ3  1 
ATOM   5425 N  N    . SER   B 1 111 ? 31.255 -21.254 3.208   1.00 13.38 ?  111 SER   B N    1 
ATOM   5426 C  CA   . SER   B 1 111 ? 31.654 -19.857 3.387   1.00 13.26 ?  111 SER   B CA   1 
ATOM   5427 C  C    . SER   B 1 111 ? 33.037 -19.597 2.798   1.00 12.33 ?  111 SER   B C    1 
ATOM   5428 O  O    . SER   B 1 111 ? 33.266 -18.561 2.155   1.00 12.78 ?  111 SER   B O    1 
ATOM   5429 C  CB   . SER   B 1 111 ? 31.645 -19.498 4.872   1.00 14.42 ?  111 SER   B CB   1 
ATOM   5430 O  OG   . SER   B 1 111 ? 30.340 -19.488 5.404   1.00 15.65 ?  111 SER   B OG   1 
ATOM   5431 H  H    . SER   B 1 111 ? 31.036 -21.665 3.932   1.00 16.22 ?  111 SER   B H    1 
ATOM   5432 H  HA   . SER   B 1 111 ? 31.022 -19.286 2.932   1.00 16.08 ?  111 SER   B HA   1 
ATOM   5433 H  HB2  . SER   B 1 111 ? 32.171 -20.155 5.357   1.00 17.47 ?  111 SER   B HB2  1 
ATOM   5434 H  HB3  . SER   B 1 111 ? 32.034 -18.620 4.982   1.00 17.47 ?  111 SER   B HB3  1 
ATOM   5435 H  HG   . SER   B 1 111 ? 30.361 -19.286 6.225   1.00 18.94 ?  111 SER   B HG   1 
ATOM   5436 N  N    . ALA   B 1 112 ? 33.978 -20.515 3.020   1.00 12.51 ?  112 ALA   B N    1 
ATOM   5437 C  CA   . ALA   B 1 112 ? 35.320 -20.344 2.473   1.00 12.10 ?  112 ALA   B CA   1 
ATOM   5438 C  C    . ALA   B 1 112 ? 35.286 -20.241 0.952   1.00 11.38 ?  112 ALA   B C    1 
ATOM   5439 O  O    . ALA   B 1 112 ? 35.919 -19.355 0.361   1.00 11.68 ?  112 ALA   B O    1 
ATOM   5440 C  CB   . ALA   B 1 112 ? 36.223 -21.489 2.938   1.00 12.63 ?  112 ALA   B CB   1 
ATOM   5441 H  H    . ALA   B 1 112 ? 33.867 -21.238 3.483   1.00 15.18 ?  112 ALA   B H    1 
ATOM   5442 H  HA   . ALA   B 1 112 ? 35.691 -19.519 2.819   1.00 14.69 ?  112 ALA   B HA   1 
ATOM   5443 H  HB1  . ALA   B 1 112 ? 37.115 -21.354 2.575   1.00 15.32 ?  112 ALA   B HB1  1 
ATOM   5444 H  HB2  . ALA   B 1 112 ? 36.264 -21.486 3.910   1.00 15.32 ?  112 ALA   B HB2  1 
ATOM   5445 H  HB3  . ALA   B 1 112 ? 35.862 -22.330 2.626   1.00 15.32 ?  112 ALA   B HB3  1 
ATOM   5446 N  N    . TYR   B 1 113 ? 34.554 -21.145 0.294   1.00 11.53 ?  113 TYR   B N    1 
ATOM   5447 C  CA   . TYR   B 1 113 ? 34.482 -21.102 -1.159  1.00 11.48 ?  113 TYR   B CA   1 
ATOM   5448 C  C    . TYR   B 1 113 ? 33.773 -19.852 -1.676  1.00 11.42 ?  113 TYR   B C    1 
ATOM   5449 O  O    . TYR   B 1 113 ? 34.041 -19.426 -2.804  1.00 11.31 ?  113 TYR   B O    1 
ATOM   5450 C  CB   . TYR   B 1 113 ? 33.807 -22.362 -1.702  1.00 11.52 ?  113 TYR   B CB   1 
ATOM   5451 C  CG   . TYR   B 1 113 ? 34.771 -23.511 -1.964  1.00 11.91 ?  113 TYR   B CG   1 
ATOM   5452 C  CD1  . TYR   B 1 113 ? 35.761 -23.412 -2.935  1.00 12.72 ?  113 TYR   B CD1  1 
ATOM   5453 C  CD2  . TYR   B 1 113 ? 34.676 -24.699 -1.255  1.00 12.20 ?  113 TYR   B CD2  1 
ATOM   5454 C  CE1  . TYR   B 1 113 ? 36.646 -24.446 -3.178  1.00 12.58 ?  113 TYR   B CE1  1 
ATOM   5455 C  CE2  . TYR   B 1 113 ? 35.549 -25.755 -1.497  1.00 12.45 ?  113 TYR   B CE2  1 
ATOM   5456 C  CZ   . TYR   B 1 113 ? 36.526 -25.621 -2.464  1.00 12.53 ?  113 TYR   B CZ   1 
ATOM   5457 O  OH   . TYR   B 1 113 ? 37.404 -26.639 -2.734  1.00 13.51 ?  113 TYR   B OH   1 
ATOM   5458 H  H    . TYR   B 1 113 ? 34.091 -21.772 0.667   1.00 14.00 ?  113 TYR   B H    1 
ATOM   5459 H  HA   . TYR   B 1 113 ? 35.382 -21.087 -1.498  1.00 13.94 ?  113 TYR   B HA   1 
ATOM   5460 H  HB2  . TYR   B 1 113 ? 33.149 -22.679 -1.057  1.00 13.99 ?  113 TYR   B HB2  1 
ATOM   5461 H  HB3  . TYR   B 1 113 ? 33.365 -22.150 -2.537  1.00 13.99 ?  113 TYR   B HB3  1 
ATOM   5462 H  HD1  . TYR   B 1 113 ? 35.845 -22.620 -3.421  1.00 15.43 ?  113 TYR   B HD1  1 
ATOM   5463 H  HD2  . TYR   B 1 113 ? 34.013 -24.791 -0.613  1.00 14.81 ?  113 TYR   B HD2  1 
ATOM   5464 H  HE1  . TYR   B 1 113 ? 37.302 -24.360 -3.837  1.00 15.26 ?  113 TYR   B HE1  1 
ATOM   5465 H  HE2  . TYR   B 1 113 ? 35.468 -26.548 -1.020  1.00 15.11 ?  113 TYR   B HE2  1 
ATOM   5466 H  HH   . TYR   B 1 113 ? 37.226 -27.305 -2.253  1.00 16.38 ?  113 TYR   B HH   1 
ATOM   5467 N  N    . GLU   B 1 114 ? 32.849 -19.272 -0.896  1.00 11.51 ?  114 GLU   B N    1 
ATOM   5468 C  CA   . GLU   B 1 114 ? 32.161 -18.066 -1.350  1.00 11.20 ?  114 GLU   B CA   1 
ATOM   5469 C  C    . GLU   B 1 114 ? 33.145 -16.946 -1.652  1.00 11.01 ?  114 GLU   B C    1 
ATOM   5470 O  O    . GLU   B 1 114 ? 32.871 -16.092 -2.499  1.00 11.53 ?  114 GLU   B O    1 
ATOM   5471 C  CB   . GLU   B 1 114 ? 31.099 -17.641 -0.332  1.00 11.79 ?  114 GLU   B CB   1 
ATOM   5472 C  CG   . GLU   B 1 114 ? 29.886 -18.560 -0.404  1.00 12.15 ?  114 GLU   B CG   1 
ATOM   5473 C  CD   . GLU   B 1 114 ? 28.866 -18.376 0.706   1.00 12.52 ?  114 GLU   B CD   1 
ATOM   5474 O  OE1  . GLU   B 1 114 ? 29.157 -17.757 1.753   1.00 12.46 ?  114 GLU   B OE1  1 
ATOM   5475 O  OE2  . GLU   B 1 114 ? 27.747 -18.914 0.536   1.00 13.28 -1 114 GLU   B OE2  1 
ATOM   5476 H  H    . GLU   B 1 114 ? 32.597 -19.566 -0.123  1.00 13.98 ?  114 GLU   B H    1 
ATOM   5477 H  HA   . GLU   B 1 114 ? 31.703 -18.270 -2.174  1.00 13.60 ?  114 GLU   B HA   1 
ATOM   5478 H  HB2  . GLU   B 1 114 ? 31.470 -17.694 0.567   1.00 14.31 ?  114 GLU   B HB2  1 
ATOM   5479 H  HB3  . GLU   B 1 114 ? 30.811 -16.737 -0.523  1.00 14.31 ?  114 GLU   B HB3  1 
ATOM   5480 H  HG2  . GLU   B 1 114 ? 29.436 -18.406 -1.246  1.00 14.75 ?  114 GLU   B HG2  1 
ATOM   5481 H  HG3  . GLU   B 1 114 ? 30.196 -19.480 -0.363  1.00 14.75 ?  114 GLU   B HG3  1 
ATOM   5482 N  N    . ASN   B 1 115 ? 34.308 -16.938 -0.996  1.00 10.88 ?  115 ASN   B N    1 
ATOM   5483 C  CA   . ASN   B 1 115 ? 35.301 -15.906 -1.294  1.00 10.86 ?  115 ASN   B CA   1 
ATOM   5484 C  C    . ASN   B 1 115 ? 35.715 -15.929 -2.759  1.00 10.56 ?  115 ASN   B C    1 
ATOM   5485 O  O    . ASN   B 1 115 ? 36.103 -14.891 -3.314  1.00 11.50 ?  115 ASN   B O    1 
ATOM   5486 C  CB   . ASN   B 1 115 ? 36.539 -16.085 -0.409  1.00 11.22 ?  115 ASN   B CB   1 
ATOM   5487 C  CG   . ASN   B 1 115 ? 36.269 -15.819 1.051   1.00 11.84 ?  115 ASN   B CG   1 
ATOM   5488 O  OD1  . ASN   B 1 115 ? 36.260 -14.670 1.490   1.00 13.97 ?  115 ASN   B OD1  1 
ATOM   5489 N  ND2  . ASN   B 1 115 ? 36.115 -16.886 1.831   1.00 12.04 ?  115 ASN   B ND2  1 
ATOM   5490 H  H    . ASN   B 1 115 ? 34.545 -17.506 -0.384  1.00 13.22 ?  115 ASN   B H    1 
ATOM   5491 H  HA   . ASN   B 1 115 ? 34.920 -15.036 -1.101  1.00 13.19 ?  115 ASN   B HA   1 
ATOM   5492 H  HB2  . ASN   B 1 115 ? 36.863 -16.995 -0.497  1.00 13.63 ?  115 ASN   B HB2  1 
ATOM   5493 H  HB3  . ASN   B 1 115 ? 37.225 -15.462 -0.701  1.00 13.63 ?  115 ASN   B HB3  1 
ATOM   5494 H  HD21 . ASN   B 1 115 ? 35.974 -16.788 2.676   1.00 14.62 ?  115 ASN   B HD21 1 
ATOM   5495 H  HD22 . ASN   B 1 115 ? 36.148 -17.678 1.494   1.00 14.62 ?  115 ASN   B HD22 1 
ATOM   5496 N  N    . PHE   B 1 116 ? 35.686 -17.108 -3.393  1.00 10.67 ?  116 PHE   B N    1 
ATOM   5497 C  CA   . PHE   B 1 116 ? 36.116 -17.201 -4.785  1.00 10.86 ?  116 PHE   B CA   1 
ATOM   5498 C  C    . PHE   B 1 116 ? 35.215 -16.376 -5.699  1.00 10.56 ?  116 PHE   B C    1 
ATOM   5499 O  O    . PHE   B 1 116 ? 35.654 -15.945 -6.771  1.00 11.14 ?  116 PHE   B O    1 
ATOM   5500 C  CB   . PHE   B 1 116 ? 36.082 -18.650 -5.305  1.00 10.64 ?  116 PHE   B CB   1 
ATOM   5501 C  CG   . PHE   B 1 116 ? 37.154 -19.601 -4.755  1.00 10.47 ?  116 PHE   B CG   1 
ATOM   5502 C  CD1  . PHE   B 1 116 ? 37.804 -19.412 -3.547  1.00 11.29 ?  116 PHE   B CD1  1 
ATOM   5503 C  CD2  . PHE   B 1 116 ? 37.460 -20.737 -5.490  1.00 10.78 ?  116 PHE   B CD2  1 
ATOM   5504 C  CE1  . PHE   B 1 116 ? 38.739 -20.353 -3.097  1.00 11.42 ?  116 PHE   B CE1  1 
ATOM   5505 C  CE2  . PHE   B 1 116 ? 38.387 -21.670 -5.047  1.00 10.87 ?  116 PHE   B CE2  1 
ATOM   5506 C  CZ   . PHE   B 1 116 ? 39.021 -21.485 -3.855  1.00 11.05 ?  116 PHE   B CZ   1 
ATOM   5507 H  H    . PHE   B 1 116 ? 35.427 -17.858 -3.044  1.00 12.97 ?  116 PHE   B H    1 
ATOM   5508 H  HA   . PHE   B 1 116 ? 37.024 -16.873 -4.866  1.00 13.19 ?  116 PHE   B HA   1 
ATOM   5509 H  HB2  . PHE   B 1 116 ? 35.214 -19.032 -5.085  1.00 12.93 ?  116 PHE   B HB2  1 
ATOM   5510 H  HB3  . PHE   B 1 116 ? 36.182 -18.630 -6.270  1.00 12.93 ?  116 PHE   B HB3  1 
ATOM   5511 H  HD1  . PHE   B 1 116 ? 37.609 -18.664 -3.029  1.00 13.71 ?  116 PHE   B HD1  1 
ATOM   5512 H  HD2  . PHE   B 1 116 ? 37.020 -20.889 -6.296  1.00 13.10 ?  116 PHE   B HD2  1 
ATOM   5513 H  HE1  . PHE   B 1 116 ? 39.178 -20.218 -2.290  1.00 13.86 ?  116 PHE   B HE1  1 
ATOM   5514 H  HE2  . PHE   B 1 116 ? 38.572 -22.423 -5.564  1.00 13.21 ?  116 PHE   B HE2  1 
ATOM   5515 H  HZ   . PHE   B 1 116 ? 39.656 -22.099 -3.562  1.00 13.42 ?  116 PHE   B HZ   1 
ATOM   5516 N  N    . ASN   B 1 117 ? 33.946 -16.177 -5.315  1.00 11.12 ?  117 ASN   B N    1 
ATOM   5517 C  CA   . ASN   B 1 117 ? 33.000 -15.474 -6.179  1.00 11.43 ?  117 ASN   B CA   1 
ATOM   5518 C  C    . ASN   B 1 117 ? 33.318 -13.995 -6.329  1.00 11.82 ?  117 ASN   B C    1 
ATOM   5519 O  O    . ASN   B 1 117 ? 32.723 -13.341 -7.189  1.00 12.79 ?  117 ASN   B O    1 
ATOM   5520 C  CB   . ASN   B 1 117 ? 31.573 -15.693 -5.688  1.00 11.90 ?  117 ASN   B CB   1 
ATOM   5521 C  CG   . ASN   B 1 117 ? 31.123 -17.103 -5.937  1.00 12.13 ?  117 ASN   B CG   1 
ATOM   5522 O  OD1  . ASN   B 1 117 ? 31.481 -17.697 -6.956  1.00 12.91 ?  117 ASN   B OD1  1 
ATOM   5523 N  ND2  . ASN   B 1 117 ? 30.387 -17.674 -4.995  1.00 11.97 ?  117 ASN   B ND2  1 
ATOM   5524 H  H    . ASN   B 1 117 ? 33.619 -16.441 -4.563  1.00 13.51 ?  117 ASN   B H    1 
ATOM   5525 H  HA   . ASN   B 1 117 ? 33.059 -15.868 -7.059  1.00 13.88 ?  117 ASN   B HA   1 
ATOM   5526 H  HB2  . ASN   B 1 117 ? 31.530 -15.522 -4.729  1.00 14.45 ?  117 ASN   B HB2  1 
ATOM   5527 H  HB3  . ASN   B 1 117 ? 30.976 -15.086 -6.157  1.00 14.45 ?  117 ASN   B HB3  1 
ATOM   5528 H  HD21 . ASN   B 1 117 ? 30.107 -18.480 -5.096  1.00 14.53 ?  117 ASN   B HD21 1 
ATOM   5529 H  HD22 . ASN   B 1 117 ? 30.165 -17.228 -4.291  1.00 14.53 ?  117 ASN   B HD22 1 
ATOM   5530 N  N    . GLN   B 1 118 ? 34.259 -13.466 -5.552  1.00 11.72 ?  118 GLN   B N    1 
ATOM   5531 C  CA   . GLN   B 1 118 ? 34.681 -12.077 -5.689  1.00 11.99 ?  118 GLN   B CA   1 
ATOM   5532 C  C    . GLN   B 1 118 ? 35.747 -11.885 -6.761  1.00 11.97 ?  118 GLN   B C    1 
ATOM   5533 O  O    . GLN   B 1 118 ? 36.220 -10.756 -6.938  1.00 13.75 ?  118 GLN   B O    1 
ATOM   5534 C  CB   . GLN   B 1 118 ? 35.162 -11.545 -4.334  1.00 12.64 ?  118 GLN   B CB   1 
ATOM   5535 C  CG   . GLN   B 1 118 ? 34.080 -11.584 -3.263  1.00 12.68 ?  118 GLN   B CG   1 
ATOM   5536 C  CD   . GLN   B 1 118 ? 32.908 -10.679 -3.595  1.00 12.70 ?  118 GLN   B CD   1 
ATOM   5537 O  OE1  . GLN   B 1 118 ? 33.094 -9.539  -4.036  1.00 13.48 ?  118 GLN   B OE1  1 
ATOM   5538 N  NE2  . GLN   B 1 118 ? 31.695 -11.177 -3.392  1.00 13.11 ?  118 GLN   B NE2  1 
ATOM   5539 H  H    . GLN   B 1 118 ? 34.684 -13.897 -4.934  1.00 14.23 ?  118 GLN   B H    1 
ATOM   5540 H  HA   . GLN   B 1 118 ? 33.911 -11.554 -5.953  1.00 14.55 ?  118 GLN   B HA   1 
ATOM   5541 H  HB2  . GLN   B 1 118 ? 35.908 -12.074 -4.026  1.00 15.33 ?  118 GLN   B HB2  1 
ATOM   5542 H  HB3  . GLN   B 1 118 ? 35.434 -10.615 -4.439  1.00 15.33 ?  118 GLN   B HB3  1 
ATOM   5543 H  HG2  . GLN   B 1 118 ? 33.750 -12.495 -3.183  1.00 15.38 ?  118 GLN   B HG2  1 
ATOM   5544 H  HG3  . GLN   B 1 118 ? 34.460 -11.295 -2.418  1.00 15.38 ?  118 GLN   B HG3  1 
ATOM   5545 H  HE21 . GLN   B 1 118 ? 31.605 -11.977 -3.083  1.00 15.89 ?  118 GLN   B HE21 1 
ATOM   5546 H  HE22 . GLN   B 1 118 ? 31.007 -10.701 -3.567  1.00 15.89 ?  118 GLN   B HE22 1 
ATOM   5547 N  N    . HIS   B 1 119 ? 36.105 -12.939 -7.494  1.00 11.43 ?  119 HIS   B N    1 
ATOM   5548 C  CA   . HIS   B 1 119 ? 37.144 -12.891 -8.513  1.00 11.77 ?  119 HIS   B CA   1 
ATOM   5549 C  C    . HIS   B 1 119 ? 36.666 -13.631 -9.747  1.00 11.95 ?  119 HIS   B C    1 
ATOM   5550 O  O    . HIS   B 1 119 ? 36.162 -14.751 -9.641  1.00 12.47 ?  119 HIS   B O    1 
ATOM   5551 C  CB   . HIS   B 1 119 ? 38.428 -13.515 -7.971  1.00 12.38 ?  119 HIS   B CB   1 
ATOM   5552 C  CG   . HIS   B 1 119 ? 38.907 -12.824 -6.740  1.00 13.52 ?  119 HIS   B CG   1 
ATOM   5553 N  ND1  . HIS   B 1 119 ? 39.703 -11.699 -6.784  1.00 15.14 ?  119 HIS   B ND1  1 
ATOM   5554 C  CD2  . HIS   B 1 119 ? 38.619 -13.034 -5.436  1.00 14.42 ?  119 HIS   B CD2  1 
ATOM   5555 C  CE1  . HIS   B 1 119 ? 39.915 -11.269 -5.554  1.00 16.19 ?  119 HIS   B CE1  1 
ATOM   5556 N  NE2  . HIS   B 1 119 ? 39.265 -12.057 -4.718  1.00 15.94 ?  119 HIS   B NE2  1 
ATOM   5557 H  H    . HIS   B 1 119 ? 35.743 -13.718 -7.417  1.00 13.88 ?  119 HIS   B H    1 
ATOM   5558 H  HA   . HIS   B 1 119 ? 37.319 -11.963 -8.755  1.00 14.28 ?  119 HIS   B HA   1 
ATOM   5559 H  HB2  . HIS   B 1 119 ? 38.261 -14.443 -7.760  1.00 15.02 ?  119 HIS   B HB2  1 
ATOM   5560 H  HB3  . HIS   B 1 119 ? 39.119 -13.445 -8.653  1.00 15.02 ?  119 HIS   B HB3  1 
ATOM   5561 H  HD2  . HIS   B 1 119 ? 38.096 -13.720 -5.093  1.00 17.46 ?  119 HIS   B HD2  1 
ATOM   5562 H  HE1  . HIS   B 1 119 ? 40.446 -10.542 -5.314  1.00 19.59 ?  119 HIS   B HE1  1 
ATOM   5563 H  HE2  . HIS   B 1 119 ? 39.274 -11.991 -3.859  1.00 19.29 ?  119 HIS   B HE2  1 
ATOM   5564 N  N    . GLU   B 1 120 ? 36.819 -13.015 -10.919 1.00 12.66 ?  120 GLU   B N    1 
ATOM   5565 C  CA   . GLU   B 1 120 ? 36.230 -13.596 -12.122 1.00 13.81 ?  120 GLU   B CA   1 
ATOM   5566 C  C    . GLU   B 1 120 ? 36.907 -14.899 -12.535 1.00 12.93 ?  120 GLU   B C    1 
ATOM   5567 O  O    . GLU   B 1 120 ? 36.246 -15.774 -13.107 1.00 13.33 ?  120 GLU   B O    1 
ATOM   5568 C  CB   . GLU   B 1 120 ? 36.243 -12.586 -13.267 1.00 17.78 ?  120 GLU   B CB   1 
ATOM   5569 C  CG   . GLU   B 1 120 ? 35.285 -11.429 -13.049 1.00 23.62 ?  120 GLU   B CG   1 
ATOM   5570 C  CD   . GLU   B 1 120 ? 35.135 -10.541 -14.269 1.00 29.52 ?  120 GLU   B CD   1 
ATOM   5571 O  OE1  . GLU   B 1 120 ? 36.127 -10.372 -15.011 1.00 31.83 ?  120 GLU   B OE1  1 
ATOM   5572 O  OE2  . GLU   B 1 120 ? 34.024 -10.013 -14.482 1.00 32.44 -1 120 GLU   B OE2  1 
ATOM   5573 H  H    . GLU   B 1 120 ? 37.246 -12.274 -11.047 1.00 15.35 ?  120 GLU   B H    1 
ATOM   5574 H  HA   . GLU   B 1 120 ? 35.305 -13.805 -11.936 1.00 16.74 ?  120 GLU   B HA   1 
ATOM   5575 H  HB2  . GLU   B 1 120 ? 37.134 -12.219 -13.360 1.00 21.50 ?  120 GLU   B HB2  1 
ATOM   5576 H  HB3  . GLU   B 1 120 ? 35.981 -13.035 -14.089 1.00 21.50 ?  120 GLU   B HB3  1 
ATOM   5577 H  HG2  . GLU   B 1 120 ? 34.405 -11.782 -12.835 1.00 28.51 ?  120 GLU   B HG2  1 
ATOM   5578 H  HG3  . GLU   B 1 120 ? 35.609 -10.884 -12.316 1.00 28.51 ?  120 GLU   B HG3  1 
ATOM   5579 N  N    . VAL   B 1 121 ? 38.209 -15.036 -12.283 1.00 12.48 ?  121 VAL   B N    1 
ATOM   5580 C  CA   . VAL   B 1 121 ? 38.958 -16.244 -12.627 1.00 12.19 ?  121 VAL   B CA   1 
ATOM   5581 C  C    . VAL   B 1 121 ? 40.065 -16.446 -11.600 1.00 11.68 ?  121 VAL   B C    1 
ATOM   5582 O  O    . VAL   B 1 121 ? 40.742 -15.490 -11.206 1.00 12.52 ?  121 VAL   B O    1 
ATOM   5583 C  CB   . VAL   B 1 121 ? 39.485 -16.201 -14.082 1.00 14.25 ?  121 VAL   B CB   1 
ATOM   5584 C  CG1  . VAL   B 1 121 ? 40.356 -14.974 -14.330 1.00 15.40 ?  121 VAL   B CG1  1 
ATOM   5585 C  CG2  . VAL   B 1 121 ? 40.233 -17.484 -14.430 1.00 15.51 ?  121 VAL   B CG2  1 
ATOM   5586 H  H    . VAL   B 1 121 ? 38.694 -14.429 -11.914 1.00 15.14 ?  121 VAL   B H    1 
ATOM   5587 H  HA   . VAL   B 1 121 ? 38.353 -17.000 -12.567 1.00 14.79 ?  121 VAL   B HA   1 
ATOM   5588 H  HB   . VAL   B 1 121 ? 38.725 -16.143 -14.686 1.00 17.26 ?  121 VAL   B HB   1 
ATOM   5589 H  HG11 . VAL   B 1 121 ? 40.668 -14.987 -15.249 1.00 18.65 ?  121 VAL   B HG11 1 
ATOM   5590 H  HG12 . VAL   B 1 121 ? 39.828 -14.176 -14.173 1.00 18.65 ?  121 VAL   B HG12 1 
ATOM   5591 H  HG13 . VAL   B 1 121 ? 41.112 -14.997 -13.724 1.00 18.65 ?  121 VAL   B HG13 1 
ATOM   5592 H  HG21 . VAL   B 1 121 ? 40.443 -17.481 -15.380 1.00 18.78 ?  121 VAL   B HG21 1 
ATOM   5593 H  HG22 . VAL   B 1 121 ? 41.056 -17.521 -13.915 1.00 18.78 ?  121 VAL   B HG22 1 
ATOM   5594 H  HG23 . VAL   B 1 121 ? 39.674 -18.246 -14.219 1.00 18.78 ?  121 VAL   B HG23 1 
ATOM   5595 N  N    . LEU   B 1 122 ? 40.244 -17.697 -11.162 1.00 11.24 ?  122 LEU   B N    1 
ATOM   5596 C  CA   . LEU   B 1 122 ? 41.231 -18.042 -10.141 1.00 10.98 ?  122 LEU   B CA   1 
ATOM   5597 C  C    . LEU   B 1 122 ? 41.884 -19.377 -10.465 1.00 10.86 ?  122 LEU   B C    1 
ATOM   5598 O  O    . LEU   B 1 122 ? 41.220 -20.301 -10.960 1.00 12.06 ?  122 LEU   B O    1 
ATOM   5599 C  CB   . LEU   B 1 122 ? 40.588 -18.271 -8.764  1.00 12.75 ?  122 LEU   B CB   1 
ATOM   5600 C  CG   . LEU   B 1 122 ? 39.549 -17.261 -8.275  1.00 12.94 ?  122 LEU   B CG   1 
ATOM   5601 C  CD1  . LEU   B 1 122 ? 38.156 -17.637 -8.763  1.00 13.34 ?  122 LEU   B CD1  1 
ATOM   5602 C  CD2  . LEU   B 1 122 ? 39.588 -17.160 -6.760  1.00 12.45 ?  122 LEU   B CD2  1 
ATOM   5603 H  H    . LEU   B 1 122 ? 39.800 -18.378 -11.448 1.00 13.66 ?  122 LEU   B H    1 
ATOM   5604 H  HA   . LEU   B 1 122 ? 41.910 -17.348 -10.072 1.00 13.34 ?  122 LEU   B HA   1 
ATOM   5605 H  HB2  . LEU   B 1 122 ? 40.152 -19.134 -8.780  1.00 15.47 ?  122 LEU   B HB2  1 
ATOM   5606 H  HB3  . LEU   B 1 122 ? 41.296 -18.283 -8.102  1.00 15.47 ?  122 LEU   B HB3  1 
ATOM   5607 H  HG   . LEU   B 1 122 ? 39.762 -16.384 -8.635  1.00 15.70 ?  122 LEU   B HG   1 
ATOM   5608 H  HD11 . LEU   B 1 122 ? 37.513 -17.010 -8.395  1.00 16.17 ?  122 LEU   B HD11 1 
ATOM   5609 H  HD12 . LEU   B 1 122 ? 38.137 -17.594 -9.732  1.00 16.17 ?  122 LEU   B HD12 1 
ATOM   5610 H  HD13 . LEU   B 1 122 ? 37.950 -18.535 -8.467  1.00 16.17 ?  122 LEU   B HD13 1 
ATOM   5611 H  HD21 . LEU   B 1 122 ? 38.901 -16.543 -6.463  1.00 15.11 ?  122 LEU   B HD21 1 
ATOM   5612 H  HD22 . LEU   B 1 122 ? 39.428 -18.039 -6.381  1.00 15.11 ?  122 LEU   B HD22 1 
ATOM   5613 H  HD23 . LEU   B 1 122 ? 40.462 -16.837 -6.486  1.00 15.11 ?  122 LEU   B HD23 1 
ATOM   5614 N  N    . LEU   B 1 123 ? 43.172 -19.486 -10.112 1.00 10.66 ?  123 LEU   B N    1 
ATOM   5615 C  CA   . LEU   B 1 123 ? 43.884 -20.755 -9.989  1.00 10.71 ?  123 LEU   B CA   1 
ATOM   5616 C  C    . LEU   B 1 123 ? 43.855 -21.153 -8.517  1.00 10.52 ?  123 LEU   B C    1 
ATOM   5617 O  O    . LEU   B 1 123 ? 44.208 -20.331 -7.661  1.00 10.82 ?  123 LEU   B O    1 
ATOM   5618 C  CB   . LEU   B 1 123 ? 45.332 -20.582 -10.453 1.00 11.25 ?  123 LEU   B CB   1 
ATOM   5619 C  CG   . LEU   B 1 123 ? 46.277 -21.758 -10.198 1.00 11.79 ?  123 LEU   B CG   1 
ATOM   5620 C  CD1  . LEU   B 1 123 ? 45.851 -23.007 -10.972 1.00 12.53 ?  123 LEU   B CD1  1 
ATOM   5621 C  CD2  . LEU   B 1 123 ? 47.692 -21.358 -10.573 1.00 12.43 ?  123 LEU   B CD2  1 
ATOM   5622 H  H    . LEU   B 1 123 ? 43.673 -18.807 -9.926  1.00 12.95 ?  123 LEU   B H    1 
ATOM   5623 H  HA   . LEU   B 1 123 ? 43.447 -21.443 -10.519 1.00 13.02 ?  123 LEU   B HA   1 
ATOM   5624 H  HB2  . LEU   B 1 123 ? 45.325 -20.425 -11.412 1.00 13.67 ?  123 LEU   B HB2  1 
ATOM   5625 H  HB3  . LEU   B 1 123 ? 45.707 -19.813 -10.003 1.00 13.67 ?  123 LEU   B HB3  1 
ATOM   5626 H  HG   . LEU   B 1 123 ? 46.269 -21.980 -9.253  1.00 14.32 ?  123 LEU   B HG   1 
ATOM   5627 H  HD11 . LEU   B 1 123 ? 46.484 -23.720 -10.793 1.00 15.20 ?  123 LEU   B HD11 1 
ATOM   5628 H  HD12 . LEU   B 1 123 ? 44.963 -23.272 -10.681 1.00 15.20 ?  123 LEU   B HD12 1 
ATOM   5629 H  HD13 . LEU   B 1 123 ? 45.840 -22.801 -11.919 1.00 15.20 ?  123 LEU   B HD13 1 
ATOM   5630 H  HD21 . LEU   B 1 123 ? 48.287 -22.104 -10.413 1.00 15.09 ?  123 LEU   B HD21 1 
ATOM   5631 H  HD22 . LEU   B 1 123 ? 47.711 -21.112 -11.512 1.00 15.09 ?  123 LEU   B HD22 1 
ATOM   5632 H  HD23 . LEU   B 1 123 ? 47.956 -20.599 -10.028 1.00 15.09 ?  123 LEU   B HD23 1 
ATOM   5633 N  N    . ALA   B 1 124 ? 43.423 -22.383 -8.208  1.00 10.33 ?  124 ALA   B N    1 
ATOM   5634 C  CA   . ALA   B 1 124 ? 43.166 -22.700 -6.810  1.00 10.46 ?  124 ALA   B CA   1 
ATOM   5635 C  C    . ALA   B 1 124 ? 43.447 -24.159 -6.486  1.00 10.11 ?  124 ALA   B C    1 
ATOM   5636 O  O    . ALA   B 1 124 ? 43.309 -25.039 -7.347  1.00 10.80 ?  124 ALA   B O    1 
ATOM   5637 C  CB   . ALA   B 1 124 ? 41.713 -22.397 -6.438  1.00 10.83 ?  124 ALA   B CB   1 
ATOM   5638 H  H    . ALA   B 1 124 ? 43.253 -23.020 -8.772  1.00 12.55 ?  124 ALA   B H    1 
ATOM   5639 H  HA   . ALA   B 1 124 ? 43.744 -22.154 -6.266  1.00 12.72 ?  124 ALA   B HA   1 
ATOM   5640 H  HB1  . ALA   B 1 124 ? 41.569 -22.619 -5.504  1.00 13.16 ?  124 ALA   B HB1  1 
ATOM   5641 H  HB2  . ALA   B 1 124 ? 41.544 -21.452 -6.583  1.00 13.16 ?  124 ALA   B HB2  1 
ATOM   5642 H  HB3  . ALA   B 1 124 ? 41.122 -22.927 -6.998  1.00 13.16 ?  124 ALA   B HB3  1 
ATOM   5643 N  N    . PRO   B 1 125 ? 43.746 -24.453 -5.225  1.00 10.49 ?  125 PRO   B N    1 
ATOM   5644 C  CA   . PRO   B 1 125 ? 43.677 -25.819 -4.701  1.00 11.33 ?  125 PRO   B CA   1 
ATOM   5645 C  C    . PRO   B 1 125 ? 42.276 -26.095 -4.155  1.00 11.54 ?  125 PRO   B C    1 
ATOM   5646 O  O    . PRO   B 1 125 ? 41.478 -25.180 -3.947  1.00 11.93 ?  125 PRO   B O    1 
ATOM   5647 C  CB   . PRO   B 1 125 ? 44.665 -25.743 -3.531  1.00 12.02 ?  125 PRO   B CB   1 
ATOM   5648 C  CG   . PRO   B 1 125 ? 44.421 -24.365 -2.965  1.00 12.04 ?  125 PRO   B CG   1 
ATOM   5649 C  CD   . PRO   B 1 125 ? 44.086 -23.489 -4.162  1.00 11.23 ?  125 PRO   B CD   1 
ATOM   5650 H  HA   . PRO   B 1 125 ? 43.951 -26.489 -5.345  1.00 13.76 ?  125 PRO   B HA   1 
ATOM   5651 H  HB2  . PRO   B 1 125 ? 44.460 -26.426 -2.869  1.00 14.58 ?  125 PRO   B HB2  1 
ATOM   5652 H  HB3  . PRO   B 1 125 ? 45.575 -25.832 -3.851  1.00 14.58 ?  125 PRO   B HB3  1 
ATOM   5653 H  HG2  . PRO   B 1 125 ? 43.680 -24.385 -2.341  1.00 14.61 ?  125 PRO   B HG2  1 
ATOM   5654 H  HG3  . PRO   B 1 125 ? 45.227 -24.041 -2.521  1.00 14.61 ?  125 PRO   B HG3  1 
ATOM   5655 H  HD2  . PRO   B 1 125 ? 43.328 -22.919 -3.967  1.00 13.64 ?  125 PRO   B HD2  1 
ATOM   5656 H  HD3  . PRO   B 1 125 ? 44.864 -22.963 -4.425  1.00 13.64 ?  125 PRO   B HD3  1 
ATOM   5657 N  N    . LEU   B 1 126 ? 42.007 -27.373 -3.873  1.00 11.82 ?  126 LEU   B N    1 
ATOM   5658 C  CA   . LEU   B 1 126 ? 40.786 -27.740 -3.162  1.00 12.30 ?  126 LEU   B CA   1 
ATOM   5659 C  C    . LEU   B 1 126 ? 40.904 -27.343 -1.699  1.00 12.56 ?  126 LEU   B C    1 
ATOM   5660 O  O    . LEU   B 1 126 ? 41.797 -27.808 -0.984  1.00 14.44 ?  126 LEU   B O    1 
ATOM   5661 C  CB   . LEU   B 1 126 ? 40.532 -29.237 -3.279  1.00 13.85 ?  126 LEU   B CB   1 
ATOM   5662 C  CG   . LEU   B 1 126 ? 40.000 -29.724 -4.625  1.00 14.34 ?  126 LEU   B CG   1 
ATOM   5663 C  CD1  . LEU   B 1 126 ? 40.043 -31.234 -4.694  1.00 16.26 ?  126 LEU   B CD1  1 
ATOM   5664 C  CD2  . LEU   B 1 126 ? 38.584 -29.224 -4.865  1.00 14.37 ?  126 LEU   B CD2  1 
ATOM   5665 H  H    . LEU   B 1 126 ? 42.515 -28.039 -4.072  1.00 14.35 ?  126 LEU   B H    1 
ATOM   5666 H  HA   . LEU   B 1 126 ? 40.034 -27.263 -3.550  1.00 14.93 ?  126 LEU   B HA   1 
ATOM   5667 H  HB2  . LEU   B 1 126 ? 41.364 -29.699 -3.111  1.00 16.79 ?  126 LEU   B HB2  1 
ATOM   5668 H  HB3  . LEU   B 1 126 ? 39.880 -29.486 -2.604  1.00 16.79 ?  126 LEU   B HB3  1 
ATOM   5669 H  HG   . LEU   B 1 126 ? 40.565 -29.372 -5.332  1.00 17.37 ?  126 LEU   B HG   1 
ATOM   5670 H  HD11 . LEU   B 1 126 ? 39.699 -31.521 -5.555  1.00 19.68 ?  126 LEU   B HD11 1 
ATOM   5671 H  HD12 . LEU   B 1 126 ? 40.956 -31.532 -4.584  1.00 19.68 ?  126 LEU   B HD12 1 
ATOM   5672 H  HD13 . LEU   B 1 126 ? 39.487 -31.597 -3.982  1.00 19.68 ?  126 LEU   B HD13 1 
ATOM   5673 H  HD21 . LEU   B 1 126 ? 38.235 -29.641 -5.669  1.00 17.40 ?  126 LEU   B HD21 1 
ATOM   5674 H  HD22 . LEU   B 1 126 ? 38.032 -29.460 -4.104  1.00 17.40 ?  126 LEU   B HD22 1 
ATOM   5675 H  HD23 . LEU   B 1 126 ? 38.599 -28.260 -4.975  1.00 17.40 ?  126 LEU   B HD23 1 
ATOM   5676 N  N    . LEU   B 1 127 ? 39.976 -26.510 -1.239  1.00 12.47 ?  127 LEU   B N    1 
ATOM   5677 C  CA   . LEU   B 1 127 ? 40.031 -26.022 0.126   1.00 12.92 ?  127 LEU   B CA   1 
ATOM   5678 C  C    . LEU   B 1 127 ? 39.755 -27.142 1.121   1.00 12.70 ?  127 LEU   B C    1 
ATOM   5679 O  O    . LEU   B 1 127 ? 38.935 -28.040 0.893   1.00 12.94 ?  127 LEU   B O    1 
ATOM   5680 C  CB   . LEU   B 1 127 ? 39.016 -24.898 0.341   1.00 13.61 ?  127 LEU   B CB   1 
ATOM   5681 C  CG   . LEU   B 1 127 ? 39.188 -23.633 -0.500  1.00 13.90 ?  127 LEU   B CG   1 
ATOM   5682 C  CD1  . LEU   B 1 127 ? 38.077 -22.661 -0.167  1.00 14.05 ?  127 LEU   B CD1  1 
ATOM   5683 C  CD2  . LEU   B 1 127 ? 40.553 -22.997 -0.275  1.00 14.96 ?  127 LEU   B CD2  1 
ATOM   5684 H  H    . LEU   B 1 127 ? 39.304 -26.212 -1.698  1.00 15.13 ?  127 LEU   B H    1 
ATOM   5685 H  HA   . LEU   B 1 127 ? 40.919 -25.667 0.299   1.00 15.67 ?  127 LEU   B HA   1 
ATOM   5686 H  HB2  . LEU   B 1 127 ? 38.133 -25.253 0.150   1.00 16.50 ?  127 LEU   B HB2  1 
ATOM   5687 H  HB3  . LEU   B 1 127 ? 39.057 -24.633 1.273   1.00 16.50 ?  127 LEU   B HB3  1 
ATOM   5688 H  HG   . LEU   B 1 127 ? 39.106 -23.859 -1.435  1.00 16.84 ?  127 LEU   B HG   1 
ATOM   5689 H  HD11 . LEU   B 1 127 ? 38.194 -21.852 -0.699  1.00 17.02 ?  127 LEU   B HD11 1 
ATOM   5690 H  HD12 . LEU   B 1 127 ? 37.222 -23.064 -0.367  1.00 17.02 ?  127 LEU   B HD12 1 
ATOM   5691 H  HD13 . LEU   B 1 127 ? 38.124 -22.432 0.778   1.00 17.02 ?  127 LEU   B HD13 1 
ATOM   5692 H  HD21 . LEU   B 1 127 ? 40.588 -22.146 -0.736  1.00 18.11 ?  127 LEU   B HD21 1 
ATOM   5693 H  HD22 . LEU   B 1 127 ? 40.689 -22.864 0.677   1.00 18.11 ?  127 LEU   B HD22 1 
ATOM   5694 H  HD23 . LEU   B 1 127 ? 41.236 -23.592 -0.625  1.00 18.11 ?  127 LEU   B HD23 1 
ATOM   5695 N  N    . SER   B 1 128 ? 40.433 -27.055 2.254   1.00 12.70 ?  128 SER   B N    1 
ATOM   5696 C  CA   . SER   B 1 128 ? 40.318 -27.974 3.373   1.00 13.04 ?  128 SER   B CA   1 
ATOM   5697 C  C    . SER   B 1 128 ? 40.812 -29.382 3.050   1.00 14.31 ?  128 SER   B C    1 
ATOM   5698 O  O    . SER   B 1 128 ? 40.723 -30.259 3.909   1.00 15.75 ?  128 SER   B O    1 
ATOM   5699 C  CB   . SER   B 1 128 ? 38.917 -27.980 4.003   1.00 13.51 ?  128 SER   B CB   1 
ATOM   5700 O  OG   . SER   B 1 128 ? 38.609 -26.702 4.547   1.00 14.28 ?  128 SER   B OG   1 
ATOM   5701 H  H    . SER   B 1 128 ? 41.003 -26.427 2.407   1.00 15.41 ?  128 SER   B H    1 
ATOM   5702 H  HA   . SER   B 1 128 ? 40.907 -27.644 4.061   1.00 15.82 ?  128 SER   B HA   1 
ATOM   5703 H  HB2  . SER   B 1 128 ? 38.258 -28.217 3.331   1.00 16.38 ?  128 SER   B HB2  1 
ATOM   5704 H  HB3  . SER   B 1 128 ? 38.897 -28.646 4.723   1.00 16.38 ?  128 SER   B HB3  1 
ATOM   5705 H  HG   . SER   B 1 128 ? 39.178 -26.500 5.129   1.00 17.30 ?  128 SER   B HG   1 
ATOM   5706 N  N    . ALA   B 1 129 ? 41.383 -29.609 1.862   1.00 15.56 ?  129 ALA   B N    1 
ATOM   5707 C  CA   . ALA   B 1 129 ? 41.932 -30.906 1.501   1.00 16.58 ?  129 ALA   B CA   1 
ATOM   5708 C  C    . ALA   B 1 129 ? 43.325 -31.085 2.096   1.00 15.71 ?  129 ALA   B C    1 
ATOM   5709 O  O    . ALA   B 1 129 ? 43.892 -30.182 2.728   1.00 15.42 ?  129 ALA   B O    1 
ATOM   5710 C  CB   . ALA   B 1 129 ? 41.990 -31.059 -0.018  1.00 18.73 ?  129 ALA   B CB   1 
ATOM   5711 H  H    . ALA   B 1 129 ? 41.462 -29.019 1.238   1.00 18.83 ?  129 ALA   B H    1 
ATOM   5712 H  HA   . ALA   B 1 129 ? 41.360 -31.605 1.849   1.00 20.06 ?  129 ALA   B HA   1 
ATOM   5713 H  HB1  . ALA   B 1 129 ? 42.350 -31.936 -0.236  1.00 22.64 ?  129 ALA   B HB1  1 
ATOM   5714 H  HB2  . ALA   B 1 129 ? 41.095 -30.973 -0.379  1.00 22.64 ?  129 ALA   B HB2  1 
ATOM   5715 H  HB3  . ALA   B 1 129 ? 42.565 -30.369 -0.386  1.00 22.64 ?  129 ALA   B HB3  1 
ATOM   5716 N  N    . GLY   B 1 130 ? 43.883 -32.272 1.872   1.00 15.60 ?  130 GLY   B N    1 
ATOM   5717 C  CA   . GLY   B 1 130 ? 45.271 -32.506 2.221   1.00 15.86 ?  130 GLY   B CA   1 
ATOM   5718 C  C    . GLY   B 1 130 ? 45.487 -32.413 3.712   1.00 15.78 ?  130 GLY   B C    1 
ATOM   5719 O  O    . GLY   B 1 130 ? 44.790 -33.057 4.509   1.00 16.61 ?  130 GLY   B O    1 
ATOM   5720 H  H    . GLY   B 1 130 ? 43.480 -32.950 1.520   1.00 18.88 ?  130 GLY   B H    1 
ATOM   5721 H  HA2  . GLY   B 1 130 ? 45.537 -33.390 1.922   1.00 19.19 ?  130 GLY   B HA2  1 
ATOM   5722 H  HA3  . GLY   B 1 130 ? 45.830 -31.849 1.781   1.00 19.19 ?  130 GLY   B HA3  1 
ATOM   5723 N  N    . ILE   B 1 131 ? 46.465 -31.587 4.099   1.00 16.28 ?  131 ILE   B N    1 
ATOM   5724 C  CA   . ILE   B 1 131 ? 46.822 -31.454 5.503   1.00 17.15 ?  131 ILE   B CA   1 
ATOM   5725 C  C    . ILE   B 1 131 ? 45.704 -30.850 6.335   1.00 16.46 ?  131 ILE   B C    1 
ATOM   5726 O  O    . ILE   B 1 131 ? 45.772 -30.918 7.565   1.00 18.16 ?  131 ILE   B O    1 
ATOM   5727 C  CB   . ILE   B 1 131 ? 48.144 -30.679 5.701   1.00 19.08 ?  131 ILE   B CB   1 
ATOM   5728 C  CG1  . ILE   B 1 131 ? 47.986 -29.196 5.327   1.00 20.08 ?  131 ILE   B CG1  1 
ATOM   5729 C  CG2  . ILE   B 1 131 ? 49.260 -31.314 4.883   1.00 20.22 ?  131 ILE   B CG2  1 
ATOM   5730 C  CD1  . ILE   B 1 131 ? 49.207 -28.340 5.648   1.00 20.80 ?  131 ILE   B CD1  1 
ATOM   5731 H  H    . ILE   B 1 131 ? 46.931 -31.096 3.568   1.00 19.70 ?  131 ILE   B H    1 
ATOM   5732 H  HA   . ILE   B 1 131 ? 46.963 -32.344 5.853   1.00 20.75 ?  131 ILE   B HA   1 
ATOM   5733 H  HB   . ILE   B 1 131 ? 48.382 -30.732 6.639   1.00 23.07 ?  131 ILE   B HB   1 
ATOM   5734 H  HG12 . ILE   B 1 131 ? 47.817 -29.133 4.374   1.00 24.26 ?  131 ILE   B HG12 1 
ATOM   5735 H  HG13 . ILE   B 1 131 ? 47.232 -28.822 5.815   1.00 24.26 ?  131 ILE   B HG13 1 
ATOM   5736 H  HG21 . ILE   B 1 131 ? 50.102 -30.917 5.145   1.00 24.43 ?  131 ILE   B HG21 1 
ATOM   5737 H  HG22 . ILE   B 1 131 ? 49.269 -32.266 5.056   1.00 24.43 ?  131 ILE   B HG22 1 
ATOM   5738 H  HG23 . ILE   B 1 131 ? 49.088 -31.149 3.943   1.00 24.43 ?  131 ILE   B HG23 1 
ATOM   5739 H  HD11 . ILE   B 1 131 ? 48.991 -27.411 5.476   1.00 25.12 ?  131 ILE   B HD11 1 
ATOM   5740 H  HD12 . ILE   B 1 131 ? 49.435 -28.460 6.583   1.00 25.12 ?  131 ILE   B HD12 1 
ATOM   5741 H  HD13 . ILE   B 1 131 ? 49.943 -28.621 5.087   1.00 25.12 ?  131 ILE   B HD13 1 
ATOM   5742 N  N    . PHE   B 1 132 ? 44.675 -30.268 5.702   1.00 15.39 ?  132 PHE   B N    1 
ATOM   5743 C  CA   . PHE   B 1 132 ? 43.515 -29.763 6.430   1.00 15.63 ?  132 PHE   B CA   1 
ATOM   5744 C  C    . PHE   B 1 132 ? 42.493 -30.854 6.759   1.00 16.99 ?  132 PHE   B C    1 
ATOM   5745 O  O    . PHE   B 1 132 ? 41.586 -30.602 7.558   1.00 18.58 ?  132 PHE   B O    1 
ATOM   5746 C  CB   . PHE   B 1 132 ? 42.841 -28.627 5.648   1.00 14.90 ?  132 PHE   B CB   1 
ATOM   5747 C  CG   . PHE   B 1 132 ? 43.539 -27.284 5.762   1.00 14.83 ?  132 PHE   B CG   1 
ATOM   5748 C  CD1  . PHE   B 1 132 ? 44.835 -27.105 5.298   1.00 15.91 ?  132 PHE   B CD1  1 
ATOM   5749 C  CD2  . PHE   B 1 132 ? 42.864 -26.185 6.281   1.00 14.28 ?  132 PHE   B CD2  1 
ATOM   5750 C  CE1  . PHE   B 1 132 ? 45.454 -25.868 5.390   1.00 16.22 ?  132 PHE   B CE1  1 
ATOM   5751 C  CE2  . PHE   B 1 132 ? 43.473 -24.947 6.368   1.00 14.82 ?  132 PHE   B CE2  1 
ATOM   5752 C  CZ   . PHE   B 1 132 ? 44.767 -24.790 5.922   1.00 15.73 ?  132 PHE   B CZ   1 
ATOM   5753 H  H    . PHE   B 1 132 ? 44.623 -30.161 4.848   1.00 18.63 ?  132 PHE   B H    1 
ATOM   5754 H  HA   . PHE   B 1 132 ? 43.820 -29.392 7.270   1.00 18.92 ?  132 PHE   B HA   1 
ATOM   5755 H  HB2  . PHE   B 1 132 ? 42.826 -28.867 4.711   1.00 18.04 ?  132 PHE   B HB2  1 
ATOM   5756 H  HB3  . PHE   B 1 132 ? 41.934 -28.517 5.976   1.00 18.04 ?  132 PHE   B HB3  1 
ATOM   5757 H  HD1  . PHE   B 1 132 ? 45.302 -27.831 4.944   1.00 19.26 ?  132 PHE   B HD1  1 
ATOM   5758 H  HD2  . PHE   B 1 132 ? 41.991 -26.291 6.584   1.00 17.30 ?  132 PHE   B HD2  1 
ATOM   5759 H  HE1  . PHE   B 1 132 ? 46.327 -25.762 5.089   1.00 19.63 ?  132 PHE   B HE1  1 
ATOM   5760 H  HE2  . PHE   B 1 132 ? 43.009 -24.224 6.731   1.00 17.95 ?  132 PHE   B HE2  1 
ATOM   5761 H  HZ   . PHE   B 1 132 ? 45.178 -23.955 5.986   1.00 19.04 ?  132 PHE   B HZ   1 
ATOM   5762 N  N    . GLY   B 1 133 ? 42.604 -32.049 6.166   1.00 16.85 ?  133 GLY   B N    1 
ATOM   5763 C  CA   . GLY   B 1 133 ? 41.890 -33.217 6.655   1.00 17.42 ?  133 GLY   B CA   1 
ATOM   5764 C  C    . GLY   B 1 133 ? 40.500 -33.483 6.104   1.00 17.68 ?  133 GLY   B C    1 
ATOM   5765 O  O    . GLY   B 1 133 ? 39.918 -34.514 6.450   1.00 19.88 ?  133 GLY   B O    1 
ATOM   5766 H  H    . GLY   B 1 133 ? 43.101 -32.203 5.479   1.00 20.38 ?  133 GLY   B H    1 
ATOM   5767 H  HA2  . GLY   B 1 133 ? 42.430 -34.000 6.471   1.00 21.07 ?  133 GLY   B HA2  1 
ATOM   5768 H  HA3  . GLY   B 1 133 ? 41.806 -33.137 7.616   1.00 21.07 ?  133 GLY   B HA3  1 
ATOM   5769 N  N    . ALA   B 1 134 ? 39.936 -32.607 5.281   1.00 16.66 ?  134 ALA   B N    1 
ATOM   5770 C  CA   . ALA   B 1 134 ? 38.611 -32.892 4.751   1.00 16.86 ?  134 ALA   B CA   1 
ATOM   5771 C  C    . ALA   B 1 134 ? 38.695 -33.880 3.592   1.00 16.99 ?  134 ALA   B C    1 
ATOM   5772 O  O    . ALA   B 1 134 ? 39.748 -34.068 2.976   1.00 17.97 ?  134 ALA   B O    1 
ATOM   5773 C  CB   . ALA   B 1 134 ? 37.925 -31.609 4.286   1.00 17.32 ?  134 ALA   B CB   1 
ATOM   5774 H  H    . ALA   B 1 134 ? 40.283 -31.857 5.030   1.00 20.16 ?  134 ALA   B H    1 
ATOM   5775 H  HA   . ALA   B 1 134 ? 38.069 -33.286 5.453   1.00 20.40 ?  134 ALA   B HA   1 
ATOM   5776 H  HB1  . ALA   B 1 134 ? 37.042 -31.831 3.954   1.00 20.95 ?  134 ALA   B HB1  1 
ATOM   5777 H  HB2  . ALA   B 1 134 ? 37.855 -31.000 5.037   1.00 20.95 ?  134 ALA   B HB2  1 
ATOM   5778 H  HB3  . ALA   B 1 134 ? 38.455 -31.208 3.581   1.00 20.95 ?  134 ALA   B HB3  1 
ATOM   5779 N  N    . ASP   B 1 135 ? 37.560 -34.504 3.299   1.00 17.16 ?  135 ASP   B N    1 
ATOM   5780 C  CA   . ASP   B 1 135 ? 37.466 -35.398 2.157   1.00 17.98 ?  135 ASP   B CA   1 
ATOM   5781 C  C    . ASP   B 1 135 ? 37.564 -34.563 0.887   1.00 16.80 ?  135 ASP   B C    1 
ATOM   5782 O  O    . ASP   B 1 135 ? 36.710 -33.691 0.664   1.00 16.71 ?  135 ASP   B O    1 
ATOM   5783 C  CB   . ASP   B 1 135 ? 36.127 -36.131 2.214   1.00 19.98 ?  135 ASP   B CB   1 
ATOM   5784 C  CG   . ASP   B 1 135 ? 35.947 -37.123 1.085   1.00 22.20 ?  135 ASP   B CG   1 
ATOM   5785 O  OD1  . ASP   B 1 135 ? 36.812 -37.176 0.185   1.00 21.69 ?  135 ASP   B OD1  1 
ATOM   5786 O  OD2  . ASP   B 1 135 ? 34.943 -37.873 1.113   1.00 25.19 -1 135 ASP   B OD2  1 
ATOM   5787 H  H    . ASP   B 1 135 ? 36.828 -34.420 3.744   1.00 20.75 ?  135 ASP   B H    1 
ATOM   5788 H  HA   . ASP   B 1 135 ? 38.185 -36.050 2.190   1.00 21.75 ?  135 ASP   B HA   1 
ATOM   5789 H  HB2  . ASP   B 1 135 ? 36.075 -36.620 3.047   1.00 24.14 ?  135 ASP   B HB2  1 
ATOM   5790 H  HB3  . ASP   B 1 135 ? 35.414 -35.479 2.162   1.00 24.14 ?  135 ASP   B HB3  1 
ATOM   5791 N  N    . PRO   B 1 136 ? 38.576 -34.766 0.042   1.00 17.02 ?  136 PRO   B N    1 
ATOM   5792 C  CA   . PRO   B 1 136 ? 38.675 -33.943 -1.174  1.00 16.19 ?  136 PRO   B CA   1 
ATOM   5793 C  C    . PRO   B 1 136 ? 37.485 -34.101 -2.096  1.00 15.77 ?  136 PRO   B C    1 
ATOM   5794 O  O    . PRO   B 1 136 ? 37.156 -33.154 -2.817  1.00 15.00 ?  136 PRO   B O    1 
ATOM   5795 C  CB   . PRO   B 1 136 ? 39.983 -34.422 -1.822  1.00 17.19 ?  136 PRO   B CB   1 
ATOM   5796 C  CG   . PRO   B 1 136 ? 40.172 -35.814 -1.283  1.00 18.70 ?  136 PRO   B CG   1 
ATOM   5797 C  CD   . PRO   B 1 136 ? 39.659 -35.759 0.123   1.00 17.94 ?  136 PRO   B CD   1 
ATOM   5798 H  HA   . PRO   B 1 136 ? 38.764 -33.007 -0.942  1.00 19.59 ?  136 PRO   B HA   1 
ATOM   5799 H  HB2  . PRO   B 1 136 ? 39.890 -34.436 -2.789  1.00 20.80 ?  136 PRO   B HB2  1 
ATOM   5800 H  HB3  . PRO   B 1 136 ? 40.714 -33.844 -1.554  1.00 20.80 ?  136 PRO   B HB3  1 
ATOM   5801 H  HG2  . PRO   B 1 136 ? 39.657 -36.446 -1.810  1.00 22.60 ?  136 PRO   B HG2  1 
ATOM   5802 H  HG3  . PRO   B 1 136 ? 41.114 -36.047 -1.293  1.00 22.60 ?  136 PRO   B HG3  1 
ATOM   5803 H  HD2  . PRO   B 1 136 ? 39.304 -36.621 0.393   1.00 21.69 ?  136 PRO   B HD2  1 
ATOM   5804 H  HD3  . PRO   B 1 136 ? 40.350 -35.452 0.733   1.00 21.69 ?  136 PRO   B HD3  1 
ATOM   5805 N  N    . ILE   B 1 137 ? 36.826 -35.265 -2.096  1.00 16.21 ?  137 ILE   B N    1 
ATOM   5806 C  CA   . ILE   B 1 137 ? 35.610 -35.434 -2.890  1.00 16.47 ?  137 ILE   B CA   1 
ATOM   5807 C  C    . ILE   B 1 137 ? 34.533 -34.466 -2.414  1.00 15.86 ?  137 ILE   B C    1 
ATOM   5808 O  O    . ILE   B 1 137 ? 33.815 -33.855 -3.217  1.00 15.31 ?  137 ILE   B O    1 
ATOM   5809 C  CB   . ILE   B 1 137 ? 35.136 -36.901 -2.830  1.00 18.82 ?  137 ILE   B CB   1 
ATOM   5810 C  CG1  . ILE   B 1 137 ? 36.124 -37.805 -3.568  1.00 21.31 ?  137 ILE   B CG1  1 
ATOM   5811 C  CG2  . ILE   B 1 137 ? 33.724 -37.048 -3.405  1.00 19.20 ?  137 ILE   B CG2  1 
ATOM   5812 C  CD1  . ILE   B 1 137 ? 35.830 -39.287 -3.415  1.00 23.88 ?  137 ILE   B CD1  1 
ATOM   5813 H  H    . ILE   B 1 137 ? 37.058 -35.964 -1.655  1.00 19.62 ?  137 ILE   B H    1 
ATOM   5814 H  HA   . ILE   B 1 137 ? 35.805 -35.224 -3.819  1.00 19.93 ?  137 ILE   B HA   1 
ATOM   5815 H  HB   . ILE   B 1 137 ? 35.111 -37.171 -1.904  1.00 22.75 ?  137 ILE   B HB   1 
ATOM   5816 H  HG12 . ILE   B 1 137 ? 36.098 -37.597 -4.515  1.00 25.74 ?  137 ILE   B HG12 1 
ATOM   5817 H  HG13 . ILE   B 1 137 ? 37.014 -37.645 -3.219  1.00 25.74 ?  137 ILE   B HG13 1 
ATOM   5818 H  HG21 . ILE   B 1 137 ? 33.492 -37.989 -3.459  1.00 23.21 ?  137 ILE   B HG21 1 
ATOM   5819 H  HG22 . ILE   B 1 137 ? 33.092 -36.599 -2.824  1.00 23.21 ?  137 ILE   B HG22 1 
ATOM   5820 H  HG23 . ILE   B 1 137 ? 33.699 -36.654 -4.291  1.00 23.21 ?  137 ILE   B HG23 1 
ATOM   5821 H  HD11 . ILE   B 1 137 ? 36.504 -39.783 -3.901  1.00 28.82 ?  137 ILE   B HD11 1 
ATOM   5822 H  HD12 . ILE   B 1 137 ? 35.857 -39.523 -2.473  1.00 28.82 ?  137 ILE   B HD12 1 
ATOM   5823 H  HD13 . ILE   B 1 137 ? 34.955 -39.488 -3.782  1.00 28.82 ?  137 ILE   B HD13 1 
ATOM   5824 N  N    . HIS   B 1 138 ? 34.401 -34.315 -1.099  1.00 15.91 ?  138 HIS   B N    1 
ATOM   5825 C  CA   . HIS   B 1 138 ? 33.452 -33.349 -0.564  1.00 16.14 ?  138 HIS   B CA   1 
ATOM   5826 C  C    . HIS   B 1 138 ? 33.870 -31.920 -0.884  1.00 15.34 ?  138 HIS   B C    1 
ATOM   5827 O  O    . HIS   B 1 138 ? 33.021 -31.076 -1.191  1.00 15.87 ?  138 HIS   B O    1 
ATOM   5828 C  CB   . HIS   B 1 138 ? 33.330 -33.528 0.941   1.00 17.49 ?  138 HIS   B CB   1 
ATOM   5829 C  CG   . HIS   B 1 138 ? 32.393 -32.551 1.574   1.00 18.67 ?  138 HIS   B CG   1 
ATOM   5830 N  ND1  . HIS   B 1 138 ? 31.053 -32.493 1.254   1.00 19.94 ?  138 HIS   B ND1  1 
ATOM   5831 C  CD2  . HIS   B 1 138 ? 32.607 -31.572 2.483   1.00 19.28 ?  138 HIS   B CD2  1 
ATOM   5832 C  CE1  . HIS   B 1 138 ? 30.479 -31.529 1.950   1.00 20.28 ?  138 HIS   B CE1  1 
ATOM   5833 N  NE2  . HIS   B 1 138 ? 31.399 -30.957 2.707   1.00 19.47 ?  138 HIS   B NE2  1 
ATOM   5834 H  H    . HIS   B 1 138 ? 34.847 -34.749 -0.509  1.00 19.26 ?  138 HIS   B H    1 
ATOM   5835 H  HA   . HIS   B 1 138 ? 32.581 -33.509 -0.963  1.00 19.53 ?  138 HIS   B HA   1 
ATOM   5836 H  HB2  . HIS   B 1 138 ? 32.995 -34.421 1.123   1.00 21.15 ?  138 HIS   B HB2  1 
ATOM   5837 H  HB3  . HIS   B 1 138 ? 34.201 -33.410 1.342   1.00 21.15 ?  138 HIS   B HB3  1 
ATOM   5838 H  HD1  . HIS   B 1 138 ? 30.654 -33.013 0.692   1.00 24.09 ?  138 HIS   B HD1  1 
ATOM   5839 H  HD2  . HIS   B 1 138 ? 33.412 -31.359 2.889   1.00 23.30 ?  138 HIS   B HD2  1 
ATOM   5840 H  HE1  . HIS   B 1 138 ? 29.574 -31.305 1.917   1.00 24.50 ?  138 HIS   B HE1  1 
ATOM   5841 N  N    . SER   B 1 139 ? 35.163 -31.619 -0.798  1.00 15.08 ?  139 SER   B N    1 
ATOM   5842 C  CA   . SER   B 1 139 ? 35.603 -30.268 -1.118  1.00 14.58 ?  139 SER   B CA   1 
ATOM   5843 C  C    . SER   B 1 139 ? 35.266 -29.917 -2.558  1.00 13.56 ?  139 SER   B C    1 
ATOM   5844 O  O    . SER   B 1 139 ? 34.818 -28.802 -2.840  1.00 13.81 ?  139 SER   B O    1 
ATOM   5845 C  CB   . SER   B 1 139 ? 37.098 -30.136 -0.861  1.00 14.92 ?  139 SER   B CB   1 
ATOM   5846 O  OG   . SER   B 1 139 ? 37.509 -28.798 -1.097  1.00 15.09 ?  139 SER   B OG   1 
ATOM   5847 H  H    . SER   B 1 139 ? 35.783 -32.159 -0.565  1.00 18.27 ?  139 SER   B H    1 
ATOM   5848 H  HA   . SER   B 1 139 ? 35.136 -29.639 -0.548  1.00 17.66 ?  139 SER   B HA   1 
ATOM   5849 H  HB2  . SER   B 1 139 ? 37.280 -30.374 0.061   1.00 18.07 ?  139 SER   B HB2  1 
ATOM   5850 H  HB3  . SER   B 1 139 ? 37.578 -30.724 -1.462  1.00 18.07 ?  139 SER   B HB3  1 
ATOM   5851 H  HG   . SER   B 1 139 ? 38.336 -28.723 -0.944  1.00 18.27 ?  139 SER   B HG   1 
ATOM   5852 N  N    . LEU   B 1 140 ? 35.456 -30.861 -3.482  1.00 13.51 ?  140 LEU   B N    1 
ATOM   5853 C  CA   . LEU   B 1 140 ? 35.090 -30.612 -4.870  1.00 13.52 ?  140 LEU   B CA   1 
ATOM   5854 C  C    . LEU   B 1 140 ? 33.587 -30.383 -5.004  1.00 13.61 ?  140 LEU   B C    1 
ATOM   5855 O  O    . LEU   B 1 140 ? 33.149 -29.499 -5.748  1.00 13.57 ?  140 LEU   B O    1 
ATOM   5856 C  CB   . LEU   B 1 140 ? 35.568 -31.771 -5.748  1.00 13.35 ?  140 LEU   B CB   1 
ATOM   5857 C  CG   . LEU   B 1 140 ? 35.201 -31.673 -7.220  1.00 13.66 ?  140 LEU   B CG   1 
ATOM   5858 C  CD1  . LEU   B 1 140 ? 35.754 -30.394 -7.818  1.00 14.79 ?  140 LEU   B CD1  1 
ATOM   5859 C  CD2  . LEU   B 1 140 ? 35.694 -32.900 -7.972  1.00 14.74 ?  140 LEU   B CD2  1 
ATOM   5860 H  H    . LEU   B 1 140 ? 35.795 -31.638 -3.334  1.00 16.38 ?  140 LEU   B H    1 
ATOM   5861 H  HA   . LEU   B 1 140 ? 35.544 -29.810 -5.171  1.00 16.38 ?  140 LEU   B HA   1 
ATOM   5862 H  HB2  . LEU   B 1 140 ? 36.537 -31.820 -5.695  1.00 16.18 ?  140 LEU   B HB2  1 
ATOM   5863 H  HB3  . LEU   B 1 140 ? 35.184 -32.593 -5.412  1.00 16.18 ?  140 LEU   B HB3  1 
ATOM   5864 H  HG   . LEU   B 1 140 ? 34.238 -31.638 -7.298  1.00 16.56 ?  140 LEU   B HG   1 
ATOM   5865 H  HD11 . LEU   B 1 140 ? 35.635 -30.422 -8.779  1.00 17.91 ?  140 LEU   B HD11 1 
ATOM   5866 H  HD12 . LEU   B 1 140 ? 35.268 -29.635 -7.449  1.00 17.91 ?  140 LEU   B HD12 1 
ATOM   5867 H  HD13 . LEU   B 1 140 ? 36.694 -30.321 -7.599  1.00 17.91 ?  140 LEU   B HD13 1 
ATOM   5868 H  HD21 . LEU   B 1 140 ? 35.444 -32.809 -8.906  1.00 17.85 ?  140 LEU   B HD21 1 
ATOM   5869 H  HD22 . LEU   B 1 140 ? 36.653 -32.957 -7.886  1.00 17.85 ?  140 LEU   B HD22 1 
ATOM   5870 H  HD23 . LEU   B 1 140 ? 35.272 -33.684 -7.590  1.00 17.85 ?  140 LEU   B HD23 1 
ATOM   5871 N  N    . ARG   B 1 141 ? 32.786 -31.174 -4.287  1.00 13.84 ?  141 ARG   B N    1 
ATOM   5872 C  CA   . ARG   B 1 141 ? 31.336 -31.000 -4.276  1.00 14.68 ?  141 ARG   B CA   1 
ATOM   5873 C  C    . ARG   B 1 141 ? 30.951 -29.590 -3.842  1.00 14.40 ?  141 ARG   B C    1 
ATOM   5874 O  O    . ARG   B 1 141 ? 30.146 -28.913 -4.501  1.00 14.40 ?  141 ARG   B O    1 
ATOM   5875 C  CB   . ARG   B 1 141 ? 30.753 -32.037 -3.309  1.00 15.98 ?  141 ARG   B CB   1 
ATOM   5876 C  CG   . ARG   B 1 141 ? 29.289 -31.926 -2.982  1.00 18.26 ?  141 ARG   B CG   1 
ATOM   5877 C  CD   . ARG   B 1 141 ? 28.494 -32.562 -4.051  1.00 20.06 ?  141 ARG   B CD   1 
ATOM   5878 N  NE   . ARG   B 1 141 ? 28.216 -31.649 -5.148  1.00 20.53 ?  141 ARG   B NE   1 
ATOM   5879 C  CZ   . ARG   B 1 141 ? 28.215 -31.992 -6.428  1.00 20.08 ?  141 ARG   B CZ   1 
ATOM   5880 N  NH1  . ARG   B 1 141 ? 28.660 -33.173 -6.831  1.00 19.88 ?  141 ARG   B NH1  1 
ATOM   5881 N  NH2  . ARG   B 1 141 ? 27.750 -31.129 -7.326  1.00 20.75 ?  141 ARG   B NH2  1 
ATOM   5882 H  H    . ARG   B 1 141 ? 33.064 -31.820 -3.794  1.00 16.77 ?  141 ARG   B H    1 
ATOM   5883 H  HA   . ARG   B 1 141 ? 30.982 -31.156 -5.162  1.00 17.78 ?  141 ARG   B HA   1 
ATOM   5884 H  HB2  . ARG   B 1 141 ? 30.909 -32.916 -3.686  1.00 19.34 ?  141 ARG   B HB2  1 
ATOM   5885 H  HB3  . ARG   B 1 141 ? 31.235 -31.967 -2.473  1.00 19.34 ?  141 ARG   B HB3  1 
ATOM   5886 H  HG2  . ARG   B 1 141 ? 29.116 -32.384 -2.146  1.00 22.07 ?  141 ARG   B HG2  1 
ATOM   5887 H  HG3  . ARG   B 1 141 ? 29.029 -30.991 -2.911  1.00 22.07 ?  141 ARG   B HG3  1 
ATOM   5888 H  HD2  . ARG   B 1 141 ? 28.980 -33.332 -4.394  1.00 24.23 ?  141 ARG   B HD2  1 
ATOM   5889 H  HD3  . ARG   B 1 141 ? 27.654 -32.852 -3.677  1.00 24.23 ?  141 ARG   B HD3  1 
ATOM   5890 H  HE   . ARG   B 1 141 ? 28.039 -30.830 -4.950  1.00 24.80 ?  141 ARG   B HE   1 
ATOM   5891 H  HH11 . ARG   B 1 141 ? 28.958 -33.744 -6.263  1.00 24.02 ?  141 ARG   B HH11 1 
ATOM   5892 H  HH12 . ARG   B 1 141 ? 28.658 -33.364 -7.667  1.00 24.02 ?  141 ARG   B HH12 1 
ATOM   5893 H  HH21 . ARG   B 1 141 ? 27.463 -30.358 -7.076  1.00 25.06 ?  141 ARG   B HH21 1 
ATOM   5894 H  HH22 . ARG   B 1 141 ? 27.761 -31.332 -8.162  1.00 25.06 ?  141 ARG   B HH22 1 
ATOM   5895 N  N    . VAL   B 1 142 ? 31.500 -29.141 -2.716  1.00 14.10 ?  142 VAL   B N    1 
ATOM   5896 C  CA   . VAL   B 1 142 ? 31.165 -27.809 -2.230  1.00 13.69 ?  142 VAL   B CA   1 
ATOM   5897 C  C    . VAL   B 1 142 ? 31.642 -26.749 -3.218  1.00 13.44 ?  142 VAL   B C    1 
ATOM   5898 O  O    . VAL   B 1 142 ? 30.942 -25.764 -3.479  1.00 14.16 ?  142 VAL   B O    1 
ATOM   5899 C  CB   . VAL   B 1 142 ? 31.719 -27.585 -0.810  1.00 14.41 ?  142 VAL   B CB   1 
ATOM   5900 C  CG1  . VAL   B 1 142 ? 31.405 -26.165 -0.329  1.00 14.29 ?  142 VAL   B CG1  1 
ATOM   5901 C  CG2  . VAL   B 1 142 ? 31.149 -28.618 0.155   1.00 15.24 ?  142 VAL   B CG2  1 
ATOM   5902 H  H    . VAL   B 1 142 ? 32.059 -29.576 -2.224  1.00 17.08 ?  142 VAL   B H    1 
ATOM   5903 H  HA   . VAL   B 1 142 ? 30.204 -27.735 -2.173  1.00 16.59 ?  142 VAL   B HA   1 
ATOM   5904 H  HB   . VAL   B 1 142 ? 32.683 -27.688 -0.822  1.00 17.45 ?  142 VAL   B HB   1 
ATOM   5905 H  HG11 . VAL   B 1 142 ? 31.593 -26.105 0.620   1.00 17.31 ?  142 VAL   B HG11 1 
ATOM   5906 H  HG12 . VAL   B 1 142 ? 31.963 -25.536 -0.815  1.00 17.31 ?  142 VAL   B HG12 1 
ATOM   5907 H  HG13 . VAL   B 1 142 ? 30.470 -25.976 -0.495  1.00 17.31 ?  142 VAL   B HG13 1 
ATOM   5908 H  HG21 . VAL   B 1 142 ? 31.474 -28.427 1.048   1.00 18.45 ?  142 VAL   B HG21 1 
ATOM   5909 H  HG22 . VAL   B 1 142 ? 30.181 -28.563 0.135   1.00 18.45 ?  142 VAL   B HG22 1 
ATOM   5910 H  HG23 . VAL   B 1 142 ? 31.437 -29.500 -0.123  1.00 18.45 ?  142 VAL   B HG23 1 
ATOM   5911 N  N    . CYS   B 1 143 ? 32.828 -26.944 -3.797  1.00 13.18 ?  143 CYS   B N    1 
ATOM   5912 C  CA   . CYS   B 1 143 ? 33.320 -26.008 -4.804  1.00 13.23 ?  143 CYS   B CA   1 
ATOM   5913 C  C    . CYS   B 1 143 ? 32.316 -25.863 -5.944  1.00 13.17 ?  143 CYS   B C    1 
ATOM   5914 O  O    . CYS   B 1 143 ? 31.917 -24.753 -6.308  1.00 13.15 ?  143 CYS   B O    1 
ATOM   5915 C  CB   . CYS   B 1 143 ? 34.677 -26.495 -5.328  1.00 13.66 ?  143 CYS   B CB   1 
ATOM   5916 S  SG   . CYS   B 1 143 ? 35.425 -25.393 -6.554  1.00 13.89 ?  143 CYS   B SG   1 
ATOM   5917 H  H    . CYS   B 1 143 ? 33.360 -27.599 -3.626  1.00 15.98 ?  143 CYS   B H    1 
ATOM   5918 H  HA   . CYS   B 1 143 ? 33.450 -25.136 -4.396  1.00 16.04 ?  143 CYS   B HA   1 
ATOM   5919 H  HB2  . CYS   B 1 143 ? 35.299 -26.574 -4.584  1.00 16.56 ?  143 CYS   B HB2  1 
ATOM   5920 H  HB3  . CYS   B 1 143 ? 34.561 -27.361 -5.741  1.00 16.56 ?  143 CYS   B HB3  1 
ATOM   5921 H  HG   . CYS   B 1 143 ? 36.497 -25.828 -6.876  1.00 16.84 ?  143 CYS   B HG   1 
ATOM   5922 N  N    . VAL   B 1 144 ? 31.915 -26.986 -6.537  1.00 13.67 ?  144 VAL   B N    1 
ATOM   5923 C  CA   . VAL   B 1 144 ? 31.006 -26.927 -7.679  1.00 14.62 ?  144 VAL   B CA   1 
ATOM   5924 C  C    . VAL   B 1 144 ? 29.663 -26.316 -7.301  1.00 14.67 ?  144 VAL   B C    1 
ATOM   5925 O  O    . VAL   B 1 144 ? 29.042 -25.612 -8.110  1.00 16.11 ?  144 VAL   B O    1 
ATOM   5926 C  CB   . VAL   B 1 144 ? 30.853 -28.336 -8.265  1.00 17.17 ?  144 VAL   B CB   1 
ATOM   5927 C  CG1  . VAL   B 1 144 ? 29.593 -28.452 -9.113  1.00 19.74 ?  144 VAL   B CG1  1 
ATOM   5928 C  CG2  . VAL   B 1 144 ? 32.111 -28.733 -9.043  1.00 17.42 ?  144 VAL   B CG2  1 
ATOM   5929 H  H    . VAL   B 1 144 ? 32.149 -27.780 -6.300  1.00 16.57 ?  144 VAL   B H    1 
ATOM   5930 H  HA   . VAL   B 1 144 ? 31.399 -26.364 -8.362  1.00 17.71 ?  144 VAL   B HA   1 
ATOM   5931 H  HB   . VAL   B 1 144 ? 30.763 -28.962 -7.531  1.00 20.77 ?  144 VAL   B HB   1 
ATOM   5932 H  HG11 . VAL   B 1 144 ? 29.680 -29.230 -9.689  1.00 23.85 ?  144 VAL   B HG11 1 
ATOM   5933 H  HG12 . VAL   B 1 144 ? 28.830 -28.562 -8.528  1.00 23.85 ?  144 VAL   B HG12 1 
ATOM   5934 H  HG13 . VAL   B 1 144 ? 29.498 -27.654 -9.650  1.00 23.85 ?  144 VAL   B HG13 1 
ATOM   5935 H  HG21 . VAL   B 1 144 ? 31.994 -29.629 -9.401  1.00 21.07 ?  144 VAL   B HG21 1 
ATOM   5936 H  HG22 . VAL   B 1 144 ? 32.245 -28.105 -9.772  1.00 21.07 ?  144 VAL   B HG22 1 
ATOM   5937 H  HG23 . VAL   B 1 144 ? 32.874 -28.714 -8.446  1.00 21.07 ?  144 VAL   B HG23 1 
ATOM   5938 N  N    . ASP   B 1 145 ? 29.198 -26.558 -6.080  1.00 14.89 ?  145 ASP   B N    1 
ATOM   5939 C  CA   . ASP   B 1 145 ? 27.888 -26.092 -5.645  1.00 15.38 ?  145 ASP   B CA   1 
ATOM   5940 C  C    . ASP   B 1 145 ? 27.918 -24.669 -5.104  1.00 15.13 ?  145 ASP   B C    1 
ATOM   5941 O  O    . ASP   B 1 145 ? 26.856 -24.126 -4.778  1.00 17.04 ?  145 ASP   B O    1 
ATOM   5942 C  CB   . ASP   B 1 145 ? 27.309 -27.016 -4.564  1.00 17.51 ?  145 ASP   B CB   1 
ATOM   5943 C  CG   . ASP   B 1 145 ? 26.948 -28.389 -5.079  1.00 19.48 ?  145 ASP   B CG   1 
ATOM   5944 O  OD1  . ASP   B 1 145 ? 26.831 -28.579 -6.307  1.00 19.65 ?  145 ASP   B OD1  1 
ATOM   5945 O  OD2  . ASP   B 1 145 ? 26.769 -29.279 -4.229  1.00 21.51 -1 145 ASP   B OD2  1 
ATOM   5946 H  H    . ASP   B 1 145 ? 29.639 -26.979 -5.475  1.00 18.03 ?  145 ASP   B H    1 
ATOM   5947 H  HA   . ASP   B 1 145 ? 27.293 -26.093 -6.404  1.00 18.62 ?  145 ASP   B HA   1 
ATOM   5948 H  HB2  . ASP   B 1 145 ? 27.962 -27.134 -3.866  1.00 21.18 ?  145 ASP   B HB2  1 
ATOM   5949 H  HB3  . ASP   B 1 145 ? 26.504 -26.607 -4.209  1.00 21.18 ?  145 ASP   B HB3  1 
ATOM   5950 N  N    . THR   B 1 146 ? 29.096 -24.056 -4.996  1.00 13.17 ?  146 THR   B N    1 
ATOM   5951 C  CA   . THR   B 1 146 ? 29.230 -22.731 -4.395  1.00 13.03 ?  146 THR   B CA   1 
ATOM   5952 C  C    . THR   B 1 146 ? 29.858 -21.702 -5.319  1.00 12.70 ?  146 THR   B C    1 
ATOM   5953 O  O    . THR   B 1 146 ? 29.404 -20.543 -5.363  1.00 12.99 ?  146 THR   B O    1 
ATOM   5954 C  CB   . THR   B 1 146 ? 30.056 -22.829 -3.106  1.00 13.06 ?  146 THR   B CB   1 
ATOM   5955 O  OG1  . THR   B 1 146 ? 29.484 -23.826 -2.251  1.00 13.39 ?  146 THR   B OG1  1 
ATOM   5956 C  CG2  . THR   B 1 146 ? 30.130 -21.491 -2.386  1.00 13.54 ?  146 THR   B CG2  1 
ATOM   5957 H  H    . THR   B 1 146 ? 29.848 -24.383 -5.271  1.00 15.97 ?  146 THR   B H    1 
ATOM   5958 H  HA   . THR   B 1 146 ? 28.358 -22.402 -4.156  1.00 15.80 ?  146 THR   B HA   1 
ATOM   5959 H  HB   . THR   B 1 146 ? 30.965 -23.089 -3.328  1.00 15.84 ?  146 THR   B HB   1 
ATOM   5960 H  HG1  . THR   B 1 146 ? 29.528 -24.584 -2.628  1.00 16.24 ?  146 THR   B HG1  1 
ATOM   5961 H  HG21 . THR   B 1 146 ? 30.485 -21.615 -1.492  1.00 16.41 ?  146 THR   B HG21 1 
ATOM   5962 H  HG22 . THR   B 1 146 ? 30.710 -20.883 -2.872  1.00 16.41 ?  146 THR   B HG22 1 
ATOM   5963 H  HG23 . THR   B 1 146 ? 29.245 -21.102 -2.323  1.00 16.41 ?  146 THR   B HG23 1 
ATOM   5964 N  N    . VAL   B 1 147 ? 30.923 -22.074 -6.021  1.00 12.92 ?  147 VAL   B N    1 
ATOM   5965 C  CA   . VAL   B 1 147 ? 31.648 -21.130 -6.858  1.00 12.49 ?  147 VAL   B CA   1 
ATOM   5966 C  C    . VAL   B 1 147 ? 30.917 -20.992 -8.180  1.00 12.68 ?  147 VAL   B C    1 
ATOM   5967 O  O    . VAL   B 1 147 ? 30.545 -21.995 -8.805  1.00 13.63 ?  147 VAL   B O    1 
ATOM   5968 C  CB   . VAL   B 1 147 ? 33.100 -21.587 -7.066  1.00 12.52 ?  147 VAL   B CB   1 
ATOM   5969 C  CG1  . VAL   B 1 147 ? 33.853 -20.558 -7.881  1.00 12.59 ?  147 VAL   B CG1  1 
ATOM   5970 C  CG2  . VAL   B 1 147 ? 33.780 -21.800 -5.728  1.00 12.59 ?  147 VAL   B CG2  1 
ATOM   5971 H  H    . VAL   B 1 147 ? 31.248 -22.874 -6.035  1.00 15.67 ?  147 VAL   B H    1 
ATOM   5972 H  HA   . VAL   B 1 147 ? 31.667 -20.264 -6.428  1.00 15.16 ?  147 VAL   B HA   1 
ATOM   5973 H  HB   . VAL   B 1 147 ? 33.110 -22.430 -7.556  1.00 15.19 ?  147 VAL   B HB   1 
ATOM   5974 H  HG11 . VAL   B 1 147 ? 34.798 -20.769 -7.864  1.00 15.28 ?  147 VAL   B HG11 1 
ATOM   5975 H  HG12 . VAL   B 1 147 ? 33.528 -20.571 -8.795  1.00 15.28 ?  147 VAL   B HG12 1 
ATOM   5976 H  HG13 . VAL   B 1 147 ? 33.704 -19.681 -7.490  1.00 15.28 ?  147 VAL   B HG13 1 
ATOM   5977 H  HG21 . VAL   B 1 147 ? 34.720 -21.994 -5.878  1.00 15.27 ?  147 VAL   B HG21 1 
ATOM   5978 H  HG22 . VAL   B 1 147 ? 33.688 -20.995 -5.199  1.00 15.27 ?  147 VAL   B HG22 1 
ATOM   5979 H  HG23 . VAL   B 1 147 ? 33.359 -22.547 -5.274  1.00 15.27 ?  147 VAL   B HG23 1 
ATOM   5980 N  N    . ARG   B 1 148 ? 30.705 -19.744 -8.601  1.00 12.64 ?  148 ARG   B N    1 
ATOM   5981 C  CA   . ARG   B 1 148 ? 30.083 -19.433 -9.876  1.00 12.88 ?  148 ARG   B CA   1 
ATOM   5982 C  C    . ARG   B 1 148 ? 31.039 -18.759 -10.848 1.00 12.75 ?  148 ARG   B C    1 
ATOM   5983 O  O    . ARG   B 1 148 ? 30.750 -18.730 -12.047 1.00 14.09 ?  148 ARG   B O    1 
ATOM   5984 C  CB   . ARG   B 1 148 ? 28.843 -18.549 -9.661  1.00 13.37 ?  148 ARG   B CB   1 
ATOM   5985 C  CG   . ARG   B 1 148 ? 27.778 -19.250 -8.829  1.00 13.99 ?  148 ARG   B CG   1 
ATOM   5986 C  CD   . ARG   B 1 148 ? 26.566 -18.361 -8.534  1.00 15.03 ?  148 ARG   B CD   1 
ATOM   5987 N  NE   . ARG   B 1 148 ? 26.947 -17.159 -7.802  1.00 14.53 ?  148 ARG   B NE   1 
ATOM   5988 C  CZ   . ARG   B 1 148 ? 27.252 -17.126 -6.511  1.00 13.80 ?  148 ARG   B CZ   1 
ATOM   5989 N  NH1  . ARG   B 1 148 ? 27.177 -18.210 -5.752  1.00 14.05 ?  148 ARG   B NH1  1 
ATOM   5990 N  NH2  . ARG   B 1 148 ? 27.652 -15.976 -5.969  1.00 13.94 ?  148 ARG   B NH2  1 
ATOM   5991 H  H    . ARG   B 1 148 ? 30.923 -19.045 -8.146  1.00 15.33 ?  148 ARG   B H    1 
ATOM   5992 H  HA   . ARG   B 1 148 ? 29.786 -20.259 -10.285 1.00 15.62 ?  148 ARG   B HA   1 
ATOM   5993 H  HB2  . ARG   B 1 148 ? 29.104 -17.740 -9.195  1.00 16.21 ?  148 ARG   B HB2  1 
ATOM   5994 H  HB3  . ARG   B 1 148 ? 28.456 -18.330 -10.522 1.00 16.21 ?  148 ARG   B HB3  1 
ATOM   5995 H  HG2  . ARG   B 1 148 ? 27.465 -20.032 -9.312  1.00 16.95 ?  148 ARG   B HG2  1 
ATOM   5996 H  HG3  . ARG   B 1 148 ? 28.165 -19.519 -7.981  1.00 16.95 ?  148 ARG   B HG3  1 
ATOM   5997 H  HD2  . ARG   B 1 148 ? 26.159 -18.087 -9.370  1.00 18.20 ?  148 ARG   B HD2  1 
ATOM   5998 H  HD3  . ARG   B 1 148 ? 25.928 -18.855 -7.996  1.00 18.20 ?  148 ARG   B HD3  1 
ATOM   5999 H  HE   . ARG   B 1 148 ? 26.981 -16.419 -8.236  1.00 17.59 ?  148 ARG   B HE   1 
ATOM   6000 H  HH11 . ARG   B 1 148 ? 26.914 -18.957 -6.087  1.00 17.03 ?  148 ARG   B HH11 1 
ATOM   6001 H  HH12 . ARG   B 1 148 ? 27.372 -18.164 -4.913  1.00 17.03 ?  148 ARG   B HH12 1 
ATOM   6002 H  HH21 . ARG   B 1 148 ? 27.712 -15.268 -6.453  1.00 16.89 ?  148 ARG   B HH21 1 
ATOM   6003 H  HH22 . ARG   B 1 148 ? 27.855 -15.939 -5.132  1.00 16.89 ?  148 ARG   B HH22 1 
ATOM   6004 N  N    . THR   B 1 149 ? 32.146 -18.202 -10.359 1.00 12.79 ?  149 THR   B N    1 
ATOM   6005 C  CA   . THR   B 1 149 ? 33.189 -17.640 -11.204 1.00 12.74 ?  149 THR   B CA   1 
ATOM   6006 C  C    . THR   B 1 149 ? 34.073 -18.779 -11.716 1.00 12.29 ?  149 THR   B C    1 
ATOM   6007 O  O    . THR   B 1 149 ? 33.880 -19.949 -11.375 1.00 13.02 ?  149 THR   B O    1 
ATOM   6008 C  CB   . THR   B 1 149 ? 33.958 -16.586 -10.418 1.00 12.92 ?  149 THR   B CB   1 
ATOM   6009 O  OG1  . THR   B 1 149 ? 34.418 -17.184 -9.204  1.00 12.88 ?  149 THR   B OG1  1 
ATOM   6010 C  CG2  . THR   B 1 149 ? 33.058 -15.390 -10.115 1.00 13.72 ?  149 THR   B CG2  1 
ATOM   6011 H  H    . THR   B 1 149 ? 32.306 -18.126 -9.515  1.00 15.51 ?  149 THR   B H    1 
ATOM   6012 H  HA   . THR   B 1 149 ? 32.776 -17.204 -11.967 1.00 15.45 ?  149 THR   B HA   1 
ATOM   6013 H  HB   . THR   B 1 149 ? 34.713 -16.281 -10.937 1.00 15.66 ?  149 THR   B HB   1 
ATOM   6014 H  HG1  . THR   B 1 149 ? 34.831 -16.609 -8.744  1.00 15.62 ?  149 THR   B HG1  1 
ATOM   6015 H  HG21 . THR   B 1 149 ? 33.558 -14.712 -9.637  1.00 16.63 ?  149 THR   B HG21 1 
ATOM   6016 H  HG22 . THR   B 1 149 ? 32.721 -15.009 -10.942 1.00 16.63 ?  149 THR   B HG22 1 
ATOM   6017 H  HG23 . THR   B 1 149 ? 32.305 -15.669 -9.569  1.00 16.63 ?  149 THR   B HG23 1 
ATOM   6018 N  N    . ASN   B 1 150 ? 35.038 -18.458 -12.566 1.00 12.46 ?  150 ASN   B N    1 
ATOM   6019 C  CA   . ASN   B 1 150 ? 35.804 -19.485 -13.260 1.00 12.96 ?  150 ASN   B CA   1 
ATOM   6020 C  C    . ASN   B 1 150 ? 36.968 -19.934 -12.386 1.00 12.49 ?  150 ASN   B C    1 
ATOM   6021 O  O    . ASN   B 1 150 ? 37.904 -19.165 -12.138 1.00 13.09 ?  150 ASN   B O    1 
ATOM   6022 C  CB   . ASN   B 1 150 ? 36.275 -18.959 -14.608 1.00 14.76 ?  150 ASN   B CB   1 
ATOM   6023 C  CG   . ASN   B 1 150 ? 35.129 -18.738 -15.553 1.00 17.45 ?  150 ASN   B CG   1 
ATOM   6024 O  OD1  . ASN   B 1 150 ? 34.237 -19.571 -15.649 1.00 18.54 ?  150 ASN   B OD1  1 
ATOM   6025 N  ND2  . ASN   B 1 150 ? 35.122 -17.603 -16.231 1.00 19.11 ?  150 ASN   B ND2  1 
ATOM   6026 H  H    . ASN   B 1 150 ? 35.276 -17.651 -12.752 1.00 15.12 ?  150 ASN   B H    1 
ATOM   6027 H  HA   . ASN   B 1 150 ? 35.224 -20.253 -13.418 1.00 15.72 ?  150 ASN   B HA   1 
ATOM   6028 H  HB2  . ASN   B 1 150 ? 36.722 -18.108 -14.473 1.00 17.88 ?  150 ASN   B HB2  1 
ATOM   6029 H  HB3  . ASN   B 1 150 ? 36.876 -19.599 -15.005 1.00 17.88 ?  150 ASN   B HB3  1 
ATOM   6030 H  HD21 . ASN   B 1 150 ? 34.482 -17.432 -16.784 1.00 23.09 ?  150 ASN   B HD21 1 
ATOM   6031 H  HD22 . ASN   B 1 150 ? 35.761 -17.036 -16.132 1.00 23.09 ?  150 ASN   B HD22 1 
ATOM   6032 N  N    . VAL   B 1 151 ? 36.920 -21.180 -11.924 1.00 12.27 ?  151 VAL   B N    1 
ATOM   6033 C  CA   . VAL   B 1 151 ? 37.939 -21.708 -11.032 1.00 12.74 ?  151 VAL   B CA   1 
ATOM   6034 C  C    . VAL   B 1 151 ? 38.645 -22.877 -11.706 1.00 12.24 ?  151 VAL   B C    1 
ATOM   6035 O  O    . VAL   B 1 151 ? 38.003 -23.814 -12.205 1.00 13.10 ?  151 VAL   B O    1 
ATOM   6036 C  CB   . VAL   B 1 151 ? 37.380 -22.049 -9.636  1.00 13.56 ?  151 VAL   B CB   1 
ATOM   6037 C  CG1  . VAL   B 1 151 ? 36.215 -23.043 -9.719  1.00 14.65 ?  151 VAL   B CG1  1 
ATOM   6038 C  CG2  . VAL   B 1 151 ? 38.488 -22.547 -8.723  1.00 13.95 ?  151 VAL   B CG2  1 
ATOM   6039 H  H    . VAL   B 1 151 ? 36.294 -21.742 -12.117 1.00 14.88 ?  151 VAL   B H    1 
ATOM   6040 H  HA   . VAL   B 1 151 ? 38.606 -21.015 -10.899 1.00 15.45 ?  151 VAL   B HA   1 
ATOM   6041 H  HB   . VAL   B 1 151 ? 37.030 -21.233 -9.242  1.00 16.44 ?  151 VAL   B HB   1 
ATOM   6042 H  HG11 . VAL   B 1 151 ? 35.895 -23.235 -8.822  1.00 17.75 ?  151 VAL   B HG11 1 
ATOM   6043 H  HG12 . VAL   B 1 151 ? 35.497 -22.652 -10.245 1.00 17.75 ?  151 VAL   B HG12 1 
ATOM   6044 H  HG13 . VAL   B 1 151 ? 36.522 -23.862 -10.140 1.00 17.75 ?  151 VAL   B HG13 1 
ATOM   6045 H  HG21 . VAL   B 1 151 ? 38.138 -22.622 -7.820  1.00 16.90 ?  151 VAL   B HG21 1 
ATOM   6046 H  HG22 . VAL   B 1 151 ? 38.788 -23.415 -9.033  1.00 16.90 ?  151 VAL   B HG22 1 
ATOM   6047 H  HG23 . VAL   B 1 151 ? 39.220 -21.913 -8.741  1.00 16.90 ?  151 VAL   B HG23 1 
ATOM   6048 N  N    . TYR   B 1 152 ? 39.974 -22.789 -11.731 1.00 11.62 ?  152 TYR   B N    1 
ATOM   6049 C  CA   . TYR   B 1 152 ? 40.875 -23.772 -12.317 1.00 12.13 ?  152 TYR   B CA   1 
ATOM   6050 C  C    . TYR   B 1 152 ? 41.594 -24.451 -11.158 1.00 11.29 ?  152 TYR   B C    1 
ATOM   6051 O  O    . TYR   B 1 152 ? 42.442 -23.834 -10.503 1.00 11.97 ?  152 TYR   B O    1 
ATOM   6052 C  CB   . TYR   B 1 152 ? 41.850 -23.064 -13.264 1.00 12.93 ?  152 TYR   B CB   1 
ATOM   6053 C  CG   . TYR   B 1 152 ? 41.171 -22.603 -14.530 1.00 13.39 ?  152 TYR   B CG   1 
ATOM   6054 C  CD1  . TYR   B 1 152 ? 40.495 -21.387 -14.593 1.00 14.05 ?  152 TYR   B CD1  1 
ATOM   6055 C  CD2  . TYR   B 1 152 ? 41.177 -23.407 -15.658 1.00 14.65 ?  152 TYR   B CD2  1 
ATOM   6056 C  CE1  . TYR   B 1 152 ? 39.853 -20.990 -15.756 1.00 15.29 ?  152 TYR   B CE1  1 
ATOM   6057 C  CE2  . TYR   B 1 152 ? 40.539 -23.023 -16.818 1.00 15.57 ?  152 TYR   B CE2  1 
ATOM   6058 C  CZ   . TYR   B 1 152 ? 39.884 -21.811 -16.867 1.00 16.02 ?  152 TYR   B CZ   1 
ATOM   6059 O  OH   . TYR   B 1 152 ? 39.254 -21.440 -18.031 1.00 18.80 ?  152 TYR   B OH   1 
ATOM   6060 H  H    . TYR   B 1 152 ? 40.404 -22.127 -11.381 1.00 14.11 ?  152 TYR   B H    1 
ATOM   6061 H  HA   . TYR   B 1 152 ? 40.367 -24.432 -12.818 1.00 14.72 ?  152 TYR   B HA   1 
ATOM   6062 H  HB2  . TYR   B 1 152 ? 42.217 -22.285 -12.813 1.00 15.68 ?  152 TYR   B HB2  1 
ATOM   6063 H  HB3  . TYR   B 1 152 ? 42.563 -23.675 -13.504 1.00 15.68 ?  152 TYR   B HB3  1 
ATOM   6064 H  HD1  . TYR   B 1 152 ? 40.469 -20.834 -13.843 1.00 17.03 ?  152 TYR   B HD1  1 
ATOM   6065 H  HD2  . TYR   B 1 152 ? 41.616 -24.226 -15.631 1.00 17.74 ?  152 TYR   B HD2  1 
ATOM   6066 H  HE1  . TYR   B 1 152 ? 39.407 -20.175 -15.789 1.00 18.52 ?  152 TYR   B HE1  1 
ATOM   6067 H  HE2  . TYR   B 1 152 ? 40.562 -23.574 -17.566 1.00 18.85 ?  152 TYR   B HE2  1 
ATOM   6068 H  HH   . TYR   B 1 152 ? 38.889 -20.690 -17.927 1.00 22.72 ?  152 TYR   B HH   1 
ATOM   6069 N  N    . LEU   B 1 153 ? 41.232 -25.709 -10.890 1.00 11.66 ?  153 LEU   B N    1 
ATOM   6070 C  CA   . LEU   B 1 153 ? 41.740 -26.452 -9.746  1.00 11.42 ?  153 LEU   B CA   1 
ATOM   6071 C  C    . LEU   B 1 153 ? 42.974 -27.253 -10.140 1.00 11.64 ?  153 LEU   B C    1 
ATOM   6072 O  O    . LEU   B 1 153 ? 42.956 -27.985 -11.134 1.00 12.79 ?  153 LEU   B O    1 
ATOM   6073 C  CB   . LEU   B 1 153 ? 40.661 -27.405 -9.221  1.00 12.12 ?  153 LEU   B CB   1 
ATOM   6074 C  CG   . LEU   B 1 153 ? 39.400 -26.753 -8.652  1.00 12.69 ?  153 LEU   B CG   1 
ATOM   6075 C  CD1  . LEU   B 1 153 ? 38.311 -27.810 -8.496  1.00 13.41 ?  153 LEU   B CD1  1 
ATOM   6076 C  CD2  . LEU   B 1 153 ? 39.706 -26.091 -7.313  1.00 13.04 ?  153 LEU   B CD2  1 
ATOM   6077 H  H    . LEU   B 1 153 ? 40.668 -26.161 -11.371 1.00 14.15 ?  153 LEU   B H    1 
ATOM   6078 H  HA   . LEU   B 1 153 ? 41.973 -25.831 -9.044  1.00 13.87 ?  153 LEU   B HA   1 
ATOM   6079 H  HB2  . LEU   B 1 153 ? 40.380 -27.982 -9.945  1.00 14.71 ?  153 LEU   B HB2  1 
ATOM   6080 H  HB3  . LEU   B 1 153 ? 41.048 -27.940 -8.511  1.00 14.71 ?  153 LEU   B HB3  1 
ATOM   6081 H  HG   . LEU   B 1 153 ? 39.077 -26.064 -9.261  1.00 15.39 ?  153 LEU   B HG   1 
ATOM   6082 H  HD11 . LEU   B 1 153 ? 37.505 -27.384 -8.161  1.00 16.26 ?  153 LEU   B HD11 1 
ATOM   6083 H  HD12 . LEU   B 1 153 ? 38.142 -28.208 -9.360  1.00 16.26 ?  153 LEU   B HD12 1 
ATOM   6084 H  HD13 . LEU   B 1 153 ? 38.619 -28.479 -7.869  1.00 16.26 ?  153 LEU   B HD13 1 
ATOM   6085 H  HD21 . LEU   B 1 153 ? 38.893 -25.711 -6.948  1.00 15.81 ?  153 LEU   B HD21 1 
ATOM   6086 H  HD22 . LEU   B 1 153 ? 40.059 -26.763 -6.705  1.00 15.81 ?  153 LEU   B HD22 1 
ATOM   6087 H  HD23 . LEU   B 1 153 ? 40.367 -25.392 -7.448  1.00 15.81 ?  153 LEU   B HD23 1 
ATOM   6088 N  N    . ALA   B 1 154 ? 44.026 -27.143 -9.338  1.00 12.03 ?  154 ALA   B N    1 
ATOM   6089 C  CA   . ALA   B 1 154 ? 45.255 -27.904 -9.524  1.00 13.15 ?  154 ALA   B CA   1 
ATOM   6090 C  C    . ALA   B 1 154 ? 45.321 -28.983 -8.451  1.00 13.57 ?  154 ALA   B C    1 
ATOM   6091 O  O    . ALA   B 1 154 ? 45.251 -28.683 -7.252  1.00 15.07 ?  154 ALA   B O    1 
ATOM   6092 C  CB   . ALA   B 1 154 ? 46.478 -26.989 -9.465  1.00 14.10 ?  154 ALA   B CB   1 
ATOM   6093 H  H    . ALA   B 1 154 ? 44.043 -26.618 -8.652  1.00 14.61 ?  154 ALA   B H    1 
ATOM   6094 H  HA   . ALA   B 1 154 ? 45.239 -28.331 -10.388 1.00 15.94 ?  154 ALA   B HA   1 
ATOM   6095 H  HB1  . ALA   B 1 154 ? 47.279 -27.519 -9.590  1.00 17.08 ?  154 ALA   B HB1  1 
ATOM   6096 H  HB2  . ALA   B 1 154 ? 46.411 -26.321 -10.169 1.00 17.08 ?  154 ALA   B HB2  1 
ATOM   6097 H  HB3  . ALA   B 1 154 ? 46.508 -26.546 -8.599  1.00 17.08 ?  154 ALA   B HB3  1 
ATOM   6098 N  N    . VAL   B 1 155 ? 45.441 -30.233 -8.885  1.00 13.09 ?  155 VAL   B N    1 
ATOM   6099 C  CA   . VAL   B 1 155 ? 45.543 -31.382 -7.994  1.00 13.21 ?  155 VAL   B CA   1 
ATOM   6100 C  C    . VAL   B 1 155 ? 46.883 -32.055 -8.273  1.00 13.18 ?  155 VAL   B C    1 
ATOM   6101 O  O    . VAL   B 1 155 ? 47.119 -32.541 -9.387  1.00 14.98 ?  155 VAL   B O    1 
ATOM   6102 C  CB   . VAL   B 1 155 ? 44.382 -32.373 -8.190  1.00 14.59 ?  155 VAL   B CB   1 
ATOM   6103 C  CG1  . VAL   B 1 155 ? 44.555 -33.568 -7.275  1.00 14.64 ?  155 VAL   B CG1  1 
ATOM   6104 C  CG2  . VAL   B 1 155 ? 43.053 -31.676 -7.927  1.00 15.52 ?  155 VAL   B CG2  1 
ATOM   6105 H  H    . VAL   B 1 155 ? 45.475 -30.443 -9.719  1.00 15.87 ?  155 VAL   B H    1 
ATOM   6106 H  HA   . VAL   B 1 155 ? 45.537 -31.082 -7.073  1.00 16.01 ?  155 VAL   B HA   1 
ATOM   6107 H  HB   . VAL   B 1 155 ? 44.382 -32.684 -9.110  1.00 17.68 ?  155 VAL   B HB   1 
ATOM   6108 H  HG11 . VAL   B 1 155 ? 43.725 -34.069 -7.254  1.00 17.73 ?  155 VAL   B HG11 1 
ATOM   6109 H  HG12 . VAL   B 1 155 ? 45.270 -34.129 -7.614  1.00 17.73 ?  155 VAL   B HG12 1 
ATOM   6110 H  HG13 . VAL   B 1 155 ? 44.773 -33.254 -6.383  1.00 17.73 ?  155 VAL   B HG13 1 
ATOM   6111 H  HG21 . VAL   B 1 155 ? 42.338 -32.324 -8.016  1.00 18.78 ?  155 VAL   B HG21 1 
ATOM   6112 H  HG22 . VAL   B 1 155 ? 43.062 -31.313 -7.027  1.00 18.78 ?  155 VAL   B HG22 1 
ATOM   6113 H  HG23 . VAL   B 1 155 ? 42.936 -30.961 -8.571  1.00 18.78 ?  155 VAL   B HG23 1 
ATOM   6114 N  N    . PHE   B 1 156 ? 47.753 -32.088 -7.261  1.00 13.46 ?  156 PHE   B N    1 
ATOM   6115 C  CA   . PHE   B 1 156 ? 49.133 -32.543 -7.459  1.00 14.92 ?  156 PHE   B CA   1 
ATOM   6116 C  C    . PHE   B 1 156 ? 49.231 -34.042 -7.749  1.00 15.83 ?  156 PHE   B C    1 
ATOM   6117 O  O    . PHE   B 1 156 ? 49.959 -34.462 -8.659  1.00 17.39 ?  156 PHE   B O    1 
ATOM   6118 C  CB   . PHE   B 1 156 ? 49.960 -32.178 -6.228  1.00 14.86 ?  156 PHE   B CB   1 
ATOM   6119 C  CG   . PHE   B 1 156 ? 51.384 -32.640 -6.289  1.00 15.39 ?  156 PHE   B CG   1 
ATOM   6120 C  CD1  . PHE   B 1 156 ? 52.263 -32.100 -7.209  1.00 16.79 ?  156 PHE   B CD1  1 
ATOM   6121 C  CD2  . PHE   B 1 156 ? 51.847 -33.598 -5.413  1.00 15.94 ?  156 PHE   B CD2  1 
ATOM   6122 C  CE1  . PHE   B 1 156 ? 53.581 -32.510 -7.260  1.00 17.65 ?  156 PHE   B CE1  1 
ATOM   6123 C  CE2  . PHE   B 1 156 ? 53.163 -34.013 -5.462  1.00 16.82 ?  156 PHE   B CE2  1 
ATOM   6124 C  CZ   . PHE   B 1 156 ? 54.025 -33.467 -6.391  1.00 17.43 ?  156 PHE   B CZ   1 
ATOM   6125 H  H    . PHE   B 1 156 ? 47.570 -31.852 -6.453  1.00 16.31 ?  156 PHE   B H    1 
ATOM   6126 H  HA   . PHE   B 1 156 ? 49.506 -32.071 -8.214  1.00 18.06 ?  156 PHE   B HA   1 
ATOM   6127 H  HB2  . PHE   B 1 156 ? 49.968 -31.212 -6.136  1.00 17.99 ?  156 PHE   B HB2  1 
ATOM   6128 H  HB3  . PHE   B 1 156 ? 49.554 -32.579 -5.444  1.00 17.99 ?  156 PHE   B HB3  1 
ATOM   6129 H  HD1  . PHE   B 1 156 ? 51.969 -31.442 -7.801  1.00 20.32 ?  156 PHE   B HD1  1 
ATOM   6130 H  HD2  . PHE   B 1 156 ? 51.263 -33.972 -4.791  1.00 19.30 ?  156 PHE   B HD2  1 
ATOM   6131 H  HE1  . PHE   B 1 156 ? 54.164 -32.137 -7.886  1.00 21.34 ?  156 PHE   B HE1  1 
ATOM   6132 H  HE2  . PHE   B 1 156 ? 53.461 -34.669 -4.874  1.00 20.35 ?  156 PHE   B HE2  1 
ATOM   6133 H  HZ   . PHE   B 1 156 ? 54.908 -33.749 -6.424  1.00 21.08 ?  156 PHE   B HZ   1 
ATOM   6134 N  N    . ASP   B 1 157 ? 48.557 -34.866 -6.959  1.00 15.99 ?  157 ASP   B N    1 
ATOM   6135 C  CA   . ASP   B 1 157 ? 48.714 -36.312 -7.057  1.00 17.33 ?  157 ASP   B CA   1 
ATOM   6136 C  C    . ASP   B 1 157 ? 47.796 -36.861 -8.144  1.00 17.51 ?  157 ASP   B C    1 
ATOM   6137 O  O    . ASP   B 1 157 ? 46.569 -36.741 -8.041  1.00 16.99 ?  157 ASP   B O    1 
ATOM   6138 C  CB   . ASP   B 1 157 ? 48.357 -36.928 -5.710  1.00 19.07 ?  157 ASP   B CB   1 
ATOM   6139 C  CG   . ASP   B 1 157 ? 48.484 -38.438 -5.701  1.00 20.90 ?  157 ASP   B CG   1 
ATOM   6140 O  OD1  . ASP   B 1 157 ? 48.828 -39.037 -6.747  1.00 21.31 ?  157 ASP   B OD1  1 
ATOM   6141 O  OD2  . ASP   B 1 157 ? 48.245 -39.026 -4.630  1.00 22.88 -1 157 ASP   B OD2  1 
ATOM   6142 H  H    . ASP   B 1 157 ? 48.005 -34.618 -6.355  1.00 19.35 ?  157 ASP   B H    1 
ATOM   6143 H  HA   . ASP   B 1 157 ? 49.638 -36.539 -7.274  1.00 20.96 ?  157 ASP   B HA   1 
ATOM   6144 H  HB2  . ASP   B 1 157 ? 48.937 -36.553 -5.032  1.00 23.04 ?  157 ASP   B HB2  1 
ATOM   6145 H  HB3  . ASP   B 1 157 ? 47.432 -36.710 -5.508  1.00 23.04 ?  157 ASP   B HB3  1 
ATOM   6146 N  N    . LYS   B 1 158 ? 48.389 -37.488 -9.169  1.00 18.71 ?  158 LYS   B N    1 
ATOM   6147 C  CA   . LYS   B 1 158 ? 47.606 -38.090 -10.250 1.00 19.92 ?  158 LYS   B CA   1 
ATOM   6148 C  C    . LYS   B 1 158 ? 46.548 -39.055 -9.719  1.00 19.80 ?  158 LYS   B C    1 
ATOM   6149 O  O    . LYS   B 1 158 ? 45.445 -39.149 -10.272 1.00 19.83 ?  158 LYS   B O    1 
ATOM   6150 C  CB   . LYS   B 1 158 ? 48.547 -38.804 -11.228 1.00 21.93 ?  158 LYS   B CB   1 
ATOM   6151 C  CG   . LYS   B 1 158 ? 47.862 -39.714 -12.239 1.00 24.26 ?  158 LYS   B CG   1 
ATOM   6152 C  CD   . LYS   B 1 158 ? 47.012 -38.941 -13.224 1.00 26.56 ?  158 LYS   B CD   1 
ATOM   6153 C  CE   . LYS   B 1 158 ? 46.416 -39.875 -14.267 1.00 28.36 ?  158 LYS   B CE   1 
ATOM   6154 N  NZ   . LYS   B 1 158 ? 45.346 -39.212 -15.065 1.00 28.91 ?  158 LYS   B NZ   1 
ATOM   6155 H  H    . LYS   B 1 158 ? 49.245 -37.583 -9.261  1.00 22.62 ?  158 LYS   B H    1 
ATOM   6156 H  HA   . LYS   B 1 158 ? 47.156 -37.387 -10.743 1.00 24.06 ?  158 LYS   B HA   1 
ATOM   6157 H  HB2  . LYS   B 1 158 ? 49.040 -38.136 -11.736 1.00 26.48 ?  158 LYS   B HB2  1 
ATOM   6158 H  HB3  . LYS   B 1 158 ? 49.170 -39.349 -10.724 1.00 26.48 ?  158 LYS   B HB3  1 
ATOM   6159 H  HG2  . LYS   B 1 158 ? 48.542 -40.187 -12.744 1.00 29.27 ?  158 LYS   B HG2  1 
ATOM   6160 H  HG3  . LYS   B 1 158 ? 47.295 -40.359 -11.783 1.00 29.27 ?  158 LYS   B HG3  1 
ATOM   6161 H  HD2  . LYS   B 1 158 ? 46.286 -38.503 -12.754 1.00 32.03 ?  158 LYS   B HD2  1 
ATOM   6162 H  HD3  . LYS   B 1 158 ? 47.564 -38.287 -13.682 1.00 32.03 ?  158 LYS   B HD3  1 
ATOM   6163 H  HE2  . LYS   B 1 158 ? 47.113 -40.161 -14.877 1.00 34.20 ?  158 LYS   B HE2  1 
ATOM   6164 H  HE3  . LYS   B 1 158 ? 46.027 -40.646 -13.822 1.00 34.20 ?  158 LYS   B HE3  1 
ATOM   6165 H  HZ1  . LYS   B 1 158 ? 45.015 -39.780 -15.664 1.00 34.86 ?  158 LYS   B HZ1  1 
ATOM   6166 H  HZ2  . LYS   B 1 158 ? 44.689 -38.941 -14.528 1.00 34.86 ?  158 LYS   B HZ2  1 
ATOM   6167 H  HZ3  . LYS   B 1 158 ? 45.680 -38.505 -15.491 1.00 34.86 ?  158 LYS   B HZ3  1 
ATOM   6168 N  N    . ASN   B 1 159 ? 46.871 -39.807 -8.665  1.00 20.04 ?  159 ASN   B N    1 
ATOM   6169 C  CA   . ASN   B 1 159 ? 45.917 -40.786 -8.153  1.00 20.89 ?  159 ASN   B CA   1 
ATOM   6170 C  C    . ASN   B 1 159 ? 44.724 -40.118 -7.471  1.00 19.57 ?  159 ASN   B C    1 
ATOM   6171 O  O    . ASN   B 1 159 ? 43.594 -40.616 -7.571  1.00 20.08 ?  159 ASN   B O    1 
ATOM   6172 C  CB   . ASN   B 1 159 ? 46.625 -41.765 -7.223  1.00 22.87 ?  159 ASN   B CB   1 
ATOM   6173 C  CG   . ASN   B 1 159 ? 47.645 -42.610 -7.953  1.00 24.82 ?  159 ASN   B CG   1 
ATOM   6174 O  OD1  . ASN   B 1 159 ? 47.381 -43.122 -9.047  1.00 25.47 ?  159 ASN   B OD1  1 
ATOM   6175 N  ND2  . ASN   B 1 159 ? 48.822 -42.763 -7.354  1.00 25.48 ?  159 ASN   B ND2  1 
ATOM   6176 H  H    . ASN   B 1 159 ? 47.615 -39.756 -8.240  1.00 24.21 ?  159 ASN   B H    1 
ATOM   6177 H  HA   . ASN   B 1 159 ? 45.576 -41.292 -8.906  1.00 25.23 ?  159 ASN   B HA   1 
ATOM   6178 H  HB2  . ASN   B 1 159 ? 47.085 -41.270 -6.529  1.00 27.61 ?  159 ASN   B HB2  1 
ATOM   6179 H  HB3  . ASN   B 1 159 ? 45.969 -42.361 -6.835  1.00 27.61 ?  159 ASN   B HB3  1 
ATOM   6180 H  HD21 . ASN   B 1 159 ? 49.443 -43.233 -7.729  1.00 30.74 ?  159 ASN   B HD21 1 
ATOM   6181 H  HD22 . ASN   B 1 159 ? 48.969 -42.402 -6.587  1.00 30.74 ?  159 ASN   B HD22 1 
ATOM   6182 N  N    . LEU   B 1 160 ? 44.938 -38.985 -6.796  1.00 18.61 ?  160 LEU   B N    1 
ATOM   6183 C  CA   . LEU   B 1 160 ? 43.802 -38.252 -6.251  1.00 17.60 ?  160 LEU   B CA   1 
ATOM   6184 C  C    . LEU   B 1 160 ? 43.012 -37.583 -7.364  1.00 16.86 ?  160 LEU   B C    1 
ATOM   6185 O  O    . LEU   B 1 160 ? 41.775 -37.592 -7.345  1.00 16.56 ?  160 LEU   B O    1 
ATOM   6186 C  CB   . LEU   B 1 160 ? 44.263 -37.226 -5.219  1.00 17.23 ?  160 LEU   B CB   1 
ATOM   6187 C  CG   . LEU   B 1 160 ? 43.132 -36.332 -4.693  1.00 17.09 ?  160 LEU   B CG   1 
ATOM   6188 C  CD1  . LEU   B 1 160 ? 42.020 -37.160 -4.064  1.00 17.70 ?  160 LEU   B CD1  1 
ATOM   6189 C  CD2  . LEU   B 1 160 ? 43.678 -35.324 -3.701  1.00 17.09 ?  160 LEU   B CD2  1 
ATOM   6190 H  H    . LEU   B 1 160 ? 45.710 -38.627 -6.653  1.00 22.49 ?  160 LEU   B H    1 
ATOM   6191 H  HA   . LEU   B 1 160 ? 43.216 -38.881 -5.811  1.00 21.28 ?  160 LEU   B HA   1 
ATOM   6192 H  HB2  . LEU   B 1 160 ? 44.652 -37.700 -4.463  1.00 20.84 ?  160 LEU   B HB2  1 
ATOM   6193 H  HB3  . LEU   B 1 160 ? 44.939 -36.655 -5.624  1.00 20.84 ?  160 LEU   B HB3  1 
ATOM   6194 H  HG   . LEU   B 1 160 ? 42.755 -35.838 -5.436  1.00 20.67 ?  160 LEU   B HG   1 
ATOM   6195 H  HD11 . LEU   B 1 160 ? 41.385 -36.561 -3.644  1.00 21.40 ?  160 LEU   B HD11 1 
ATOM   6196 H  HD12 . LEU   B 1 160 ? 41.577 -37.679 -4.754  1.00 21.40 ?  160 LEU   B HD12 1 
ATOM   6197 H  HD13 . LEU   B 1 160 ? 42.403 -37.755 -3.399  1.00 21.40 ?  160 LEU   B HD13 1 
ATOM   6198 H  HD21 . LEU   B 1 160 ? 42.952 -34.757 -3.403  1.00 20.67 ?  160 LEU   B HD21 1 
ATOM   6199 H  HD22 . LEU   B 1 160 ? 44.062 -35.798 -2.948  1.00 20.67 ?  160 LEU   B HD22 1 
ATOM   6200 H  HD23 . LEU   B 1 160 ? 44.360 -34.789 -4.138  1.00 20.67 ?  160 LEU   B HD23 1 
ATOM   6201 N  N    . TYR   B 1 161 ? 43.710 -37.006 -8.347  1.00 17.20 ?  161 TYR   B N    1 
ATOM   6202 C  CA   . TYR   B 1 161 ? 43.038 -36.447 -9.515  1.00 16.75 ?  161 TYR   B CA   1 
ATOM   6203 C  C    . TYR   B 1 161 ? 42.089 -37.468 -10.130 1.00 16.46 ?  161 TYR   B C    1 
ATOM   6204 O  O    . TYR   B 1 161 ? 40.917 -37.171 -10.384 1.00 16.34 ?  161 TYR   B O    1 
ATOM   6205 C  CB   . TYR   B 1 161 ? 44.079 -35.978 -10.541 1.00 17.33 ?  161 TYR   B CB   1 
ATOM   6206 C  CG   . TYR   B 1 161 ? 43.494 -35.507 -11.855 1.00 17.91 ?  161 TYR   B CG   1 
ATOM   6207 C  CD1  . TYR   B 1 161 ? 43.107 -34.182 -12.023 1.00 17.87 ?  161 TYR   B CD1  1 
ATOM   6208 C  CD2  . TYR   B 1 161 ? 43.321 -36.382 -12.926 1.00 18.57 ?  161 TYR   B CD2  1 
ATOM   6209 C  CE1  . TYR   B 1 161 ? 42.569 -33.742 -13.209 1.00 19.14 ?  161 TYR   B CE1  1 
ATOM   6210 C  CE2  . TYR   B 1 161 ? 42.779 -35.948 -14.120 1.00 19.81 ?  161 TYR   B CE2  1 
ATOM   6211 C  CZ   . TYR   B 1 161 ? 42.409 -34.626 -14.256 1.00 19.77 ?  161 TYR   B CZ   1 
ATOM   6212 O  OH   . TYR   B 1 161 ? 41.867 -34.178 -15.437 1.00 21.81 ?  161 TYR   B OH   1 
ATOM   6213 H  H    . TYR   B 1 161 ? 44.564 -36.938 -8.367  1.00 20.81 ?  161 TYR   B H    1 
ATOM   6214 H  HA   . TYR   B 1 161 ? 42.516 -35.676 -9.247  1.00 20.27 ?  161 TYR   B HA   1 
ATOM   6215 H  HB2  . TYR   B 1 161 ? 44.581 -35.237 -10.162 1.00 20.96 ?  161 TYR   B HB2  1 
ATOM   6216 H  HB3  . TYR   B 1 161 ? 44.682 -36.712 -10.737 1.00 20.96 ?  161 TYR   B HB3  1 
ATOM   6217 H  HD1  . TYR   B 1 161 ? 43.219 -33.575 -11.325 1.00 21.61 ?  161 TYR   B HD1  1 
ATOM   6218 H  HD2  . TYR   B 1 161 ? 43.566 -37.272 -12.840 1.00 22.45 ?  161 TYR   B HD2  1 
ATOM   6219 H  HE1  . TYR   B 1 161 ? 42.321 -32.845 -13.305 1.00 23.13 ?  161 TYR   B HE1  1 
ATOM   6220 H  HE2  . TYR   B 1 161 ? 42.662 -36.536 -14.831 1.00 23.94 ?  161 TYR   B HE2  1 
ATOM   6221 H  HH   . TYR   B 1 161 ? 41.814 -34.808 -15.990 1.00 26.33 ?  161 TYR   B HH   1 
ATOM   6222 N  N    . ASP   B 1 162 ? 42.583 -38.687 -10.363 1.00 17.14 ?  162 ASP   B N    1 
ATOM   6223 C  CA   . ASP   B 1 162 ? 41.751 -39.720 -10.974 1.00 17.57 ?  162 ASP   B CA   1 
ATOM   6224 C  C    . ASP   B 1 162 ? 40.550 -40.064 -10.097 1.00 16.92 ?  162 ASP   B C    1 
ATOM   6225 O  O    . ASP   B 1 162 ? 39.444 -40.286 -10.606 1.00 17.33 ?  162 ASP   B O    1 
ATOM   6226 C  CB   . ASP   B 1 162 ? 42.579 -40.982 -11.237 1.00 19.06 ?  162 ASP   B CB   1 
ATOM   6227 C  CG   . ASP   B 1 162 ? 43.575 -40.817 -12.374 1.00 20.55 ?  162 ASP   B CG   1 
ATOM   6228 O  OD1  . ASP   B 1 162 ? 43.437 -39.875 -13.176 1.00 20.91 ?  162 ASP   B OD1  1 
ATOM   6229 O  OD2  . ASP   B 1 162 ? 44.488 -41.665 -12.483 1.00 22.17 -1 162 ASP   B OD2  1 
ATOM   6230 H  H    . ASP   B 1 162 ? 43.384 -38.932 -10.185 1.00 20.73 ?  162 ASP   B H    1 
ATOM   6231 H  HA   . ASP   B 1 162 ? 41.415 -39.397 -11.823 1.00 21.25 ?  162 ASP   B HA   1 
ATOM   6232 H  HB2  . ASP   B 1 162 ? 43.075 -41.205 -10.437 1.00 23.04 ?  162 ASP   B HB2  1 
ATOM   6233 H  HB3  . ASP   B 1 162 ? 41.980 -41.706 -11.474 1.00 23.04 ?  162 ASP   B HB3  1 
ATOM   6234 N  N    . LYS   B 1 163 ? 40.747 -40.135 -8.779  1.00 16.45 ?  163 LYS   B N    1 
ATOM   6235 C  CA   . LYS   B 1 163 ? 39.627 -40.412 -7.884  1.00 17.01 ?  163 LYS   B CA   1 
ATOM   6236 C  C    . LYS   B 1 163 ? 38.581 -39.305 -7.953  1.00 15.78 ?  163 LYS   B C    1 
ATOM   6237 O  O    . LYS   B 1 163 ? 37.371 -39.575 -7.954  1.00 16.72 ?  163 LYS   B O    1 
ATOM   6238 C  CB   . LYS   B 1 163 ? 40.119 -40.586 -6.449  1.00 20.40 ?  163 LYS   B CB   1 
ATOM   6239 C  CG   . LYS   B 1 163 ? 39.034 -41.088 -5.521  1.00 26.16 ?  163 LYS   B CG   1 
ATOM   6240 C  CD   . LYS   B 1 163 ? 39.504 -41.249 -4.090  1.00 31.71 ?  163 LYS   B CD   1 
ATOM   6241 C  CE   . LYS   B 1 163 ? 38.418 -41.905 -3.248  1.00 36.03 ?  163 LYS   B CE   1 
ATOM   6242 N  NZ   . LYS   B 1 163 ? 38.607 -41.671 -1.790  1.00 38.68 ?  163 LYS   B NZ   1 
ATOM   6243 H  H    . LYS   B 1 163 ? 41.509 -40.027 -8.388  1.00 19.90 ?  163 LYS   B H    1 
ATOM   6244 H  HA   . LYS   B 1 163 ? 39.208 -41.236 -8.157  1.00 20.58 ?  163 LYS   B HA   1 
ATOM   6245 H  HB2  . LYS   B 1 163 ? 40.846 -41.230 -6.440  1.00 24.65 ?  163 LYS   B HB2  1 
ATOM   6246 H  HB3  . LYS   B 1 163 ? 40.431 -39.731 -6.112  1.00 24.65 ?  163 LYS   B HB3  1 
ATOM   6247 H  HG2  . LYS   B 1 163 ? 38.299 -40.458 -5.523  1.00 31.56 ?  163 LYS   B HG2  1 
ATOM   6248 H  HG3  . LYS   B 1 163 ? 38.729 -41.955 -5.835  1.00 31.56 ?  163 LYS   B HG3  1 
ATOM   6249 H  HD2  . LYS   B 1 163 ? 40.292 -41.816 -4.070  1.00 38.21 ?  163 LYS   B HD2  1 
ATOM   6250 H  HD3  . LYS   B 1 163 ? 39.703 -40.378 -3.715  1.00 38.21 ?  163 LYS   B HD3  1 
ATOM   6251 H  HE2  . LYS   B 1 163 ? 37.552 -41.552 -3.506  1.00 43.40 ?  163 LYS   B HE2  1 
ATOM   6252 H  HE3  . LYS   B 1 163 ? 38.438 -42.862 -3.402  1.00 43.40 ?  163 LYS   B HE3  1 
ATOM   6253 H  HZ1  . LYS   B 1 163 ? 37.954 -42.066 -1.333  1.00 46.58 ?  163 LYS   B HZ1  1 
ATOM   6254 H  HZ2  . LYS   B 1 163 ? 39.388 -42.006 -1.529  1.00 46.58 ?  163 LYS   B HZ2  1 
ATOM   6255 H  HZ3  . LYS   B 1 163 ? 38.593 -40.798 -1.618  1.00 46.58 ?  163 LYS   B HZ3  1 
ATOM   6256 N  N    . LEU   B 1 164 ? 39.033 -38.052 -8.010  1.00 14.73 ?  164 LEU   B N    1 
ATOM   6257 C  CA   . LEU   B 1 164 ? 38.125 -36.912 -8.065  1.00 14.44 ?  164 LEU   B CA   1 
ATOM   6258 C  C    . LEU   B 1 164 ? 37.341 -36.896 -9.371  1.00 14.91 ?  164 LEU   B C    1 
ATOM   6259 O  O    . LEU   B 1 164 ? 36.119 -36.699 -9.371  1.00 15.97 ?  164 LEU   B O    1 
ATOM   6260 C  CB   . LEU   B 1 164 ? 38.929 -35.623 -7.909  1.00 13.68 ?  164 LEU   B CB   1 
ATOM   6261 C  CG   . LEU   B 1 164 ? 39.454 -35.347 -6.504  1.00 14.61 ?  164 LEU   B CG   1 
ATOM   6262 C  CD1  . LEU   B 1 164 ? 40.546 -34.289 -6.556  1.00 14.70 ?  164 LEU   B CD1  1 
ATOM   6263 C  CD2  . LEU   B 1 164 ? 38.335 -34.897 -5.589  1.00 16.77 ?  164 LEU   B CD2  1 
ATOM   6264 H  H    . LEU   B 1 164 ? 39.867 -37.832 -8.021  1.00 17.84 ?  164 LEU   B H    1 
ATOM   6265 H  HA   . LEU   B 1 164 ? 37.496 -36.965 -7.336  1.00 17.50 ?  164 LEU   B HA   1 
ATOM   6266 H  HB2  . LEU   B 1 164 ? 39.701 -35.663 -8.503  1.00 16.58 ?  164 LEU   B HB2  1 
ATOM   6267 H  HB3  . LEU   B 1 164 ? 38.372 -34.872 -8.163  1.00 16.58 ?  164 LEU   B HB3  1 
ATOM   6268 H  HG   . LEU   B 1 164 ? 39.841 -36.156 -6.143  1.00 17.70 ?  164 LEU   B HG   1 
ATOM   6269 H  HD11 . LEU   B 1 164 ? 40.866 -34.116 -5.655  1.00 17.80 ?  164 LEU   B HD11 1 
ATOM   6270 H  HD12 . LEU   B 1 164 ? 41.282 -34.616 -7.105  1.00 17.80 ?  164 LEU   B HD12 1 
ATOM   6271 H  HD13 . LEU   B 1 164 ? 40.189 -33.475 -6.942  1.00 17.80 ?  164 LEU   B HD13 1 
ATOM   6272 H  HD21 . LEU   B 1 164 ? 38.705 -34.672 -4.721  1.00 20.29 ?  164 LEU   B HD21 1 
ATOM   6273 H  HD22 . LEU   B 1 164 ? 37.901 -34.118 -5.974  1.00 20.29 ?  164 LEU   B HD22 1 
ATOM   6274 H  HD23 . LEU   B 1 164 ? 37.694 -35.619 -5.497  1.00 20.29 ?  164 LEU   B HD23 1 
ATOM   6275 N  N    . VAL   B 1 165 ? 38.029 -37.070 -10.499 1.00 16.75 ?  165 VAL   B N    1 
ATOM   6276 C  CA   . VAL   B 1 165 ? 37.372 -37.004 -11.799 1.00 17.80 ?  165 VAL   B CA   1 
ATOM   6277 C  C    . VAL   B 1 165 ? 36.451 -38.202 -11.985 1.00 19.62 ?  165 VAL   B C    1 
ATOM   6278 O  O    . VAL   B 1 165 ? 35.291 -38.064 -12.394 1.00 20.75 ?  165 VAL   B O    1 
ATOM   6279 C  CB   . VAL   B 1 165 ? 38.419 -36.923 -12.925 1.00 18.70 ?  165 VAL   B CB   1 
ATOM   6280 C  CG1  . VAL   B 1 165 ? 37.759 -37.039 -14.280 1.00 19.82 ?  165 VAL   B CG1  1 
ATOM   6281 C  CG2  . VAL   B 1 165 ? 39.208 -35.638 -12.824 1.00 18.65 ?  165 VAL   B CG2  1 
ATOM   6282 H  H    . VAL   B 1 165 ? 38.875 -37.215 -10.538 1.00 20.27 ?  165 VAL   B H    1 
ATOM   6283 H  HA   . VAL   B 1 165 ? 36.829 -36.202 -11.844 1.00 21.53 ?  165 VAL   B HA   1 
ATOM   6284 H  HB   . VAL   B 1 165 ? 39.044 -37.660 -12.829 1.00 22.61 ?  165 VAL   B HB   1 
ATOM   6285 H  HG11 . VAL   B 1 165 ? 38.380 -36.743 -14.961 1.00 23.95 ?  165 VAL   B HG11 1 
ATOM   6286 H  HG12 . VAL   B 1 165 ? 37.525 -37.970 -14.435 1.00 23.95 ?  165 VAL   B HG12 1 
ATOM   6287 H  HG13 . VAL   B 1 165 ? 36.962 -36.491 -14.292 1.00 23.95 ?  165 VAL   B HG13 1 
ATOM   6288 H  HG21 . VAL   B 1 165 ? 39.845 -35.597 -13.557 1.00 22.55 ?  165 VAL   B HG21 1 
ATOM   6289 H  HG22 . VAL   B 1 165 ? 38.597 -34.885 -12.879 1.00 22.55 ?  165 VAL   B HG22 1 
ATOM   6290 H  HG23 . VAL   B 1 165 ? 39.681 -35.618 -11.977 1.00 22.55 ?  165 VAL   B HG23 1 
ATOM   6291 N  N    . SER   B 1 166 ? 36.964 -39.401 -11.692 1.00 20.41 ?  166 SER   B N    1 
ATOM   6292 C  CA   . SER   B 1 166 ? 36.213 -40.614 -11.978 1.00 21.69 ?  166 SER   B CA   1 
ATOM   6293 C  C    . SER   B 1 166 ? 34.954 -40.708 -11.129 1.00 21.89 ?  166 SER   B C    1 
ATOM   6294 O  O    . SER   B 1 166 ? 33.983 -41.336 -11.552 1.00 23.30 ?  166 SER   B O    1 
ATOM   6295 C  CB   . SER   B 1 166 ? 37.094 -41.861 -11.808 1.00 22.91 ?  166 SER   B CB   1 
ATOM   6296 O  OG   . SER   B 1 166 ? 37.431 -42.087 -10.449 1.00 22.94 ?  166 SER   B OG   1 
ATOM   6297 H  H    . SER   B 1 166 ? 37.742 -39.532 -11.343 1.00 24.66 ?  166 SER   B H    1 
ATOM   6298 H  HA   . SER   B 1 166 ? 35.940 -40.590 -12.908 1.00 26.20 ?  166 SER   B HA   1 
ATOM   6299 H  HB2  . SER   B 1 166 ? 36.613 -42.632 -12.145 1.00 27.66 ?  166 SER   B HB2  1 
ATOM   6300 H  HB3  . SER   B 1 166 ? 37.913 -41.739 -12.321 1.00 27.66 ?  166 SER   B HB3  1 
ATOM   6301 H  HG   . SER   B 1 166 ? 37.861 -41.431 -10.152 1.00 27.69 ?  166 SER   B HG   1 
ATOM   6302 N  N    . SER   B 1 167 ? 34.936 -40.095 -9.948  1.00 20.33 ?  167 SER   B N    1 
ATOM   6303 C  CA   . SER   B 1 167 ? 33.779 -40.151 -9.063  1.00 19.78 ?  167 SER   B CA   1 
ATOM   6304 C  C    . SER   B 1 167 ? 32.866 -38.930 -9.162  1.00 19.32 ?  167 SER   B C    1 
ATOM   6305 O  O    . SER   B 1 167 ? 31.790 -38.932 -8.552  1.00 19.25 ?  167 SER   B O    1 
ATOM   6306 C  CB   . SER   B 1 167 ? 34.219 -40.329 -7.604  1.00 19.63 ?  167 SER   B CB   1 
ATOM   6307 O  OG   . SER   B 1 167 ? 34.892 -39.169 -7.134  1.00 19.23 ?  167 SER   B OG   1 
ATOM   6308 H  H    . SER   B 1 167 ? 35.589 -39.641 -9.635  1.00 24.56 ?  167 SER   B H    1 
ATOM   6309 H  HA   . SER   B 1 167 ? 33.248 -40.929 -9.304  1.00 23.90 ?  167 SER   B HA   1 
ATOM   6310 H  HB2  . SER   B 1 167 ? 33.432 -40.488 -7.057  1.00 23.72 ?  167 SER   B HB2  1 
ATOM   6311 H  HB3  . SER   B 1 167 ? 34.814 -41.098 -7.549  1.00 23.72 ?  167 SER   B HB3  1 
ATOM   6312 H  HG   . SER   B 1 167 ? 35.577 -39.040 -7.600  1.00 23.24 ?  167 SER   B HG   1 
ATOM   6313 N  N    . PHE   B 1 168 ? 33.247 -37.893 -9.909  1.00 18.86 ?  168 PHE   B N    1 
ATOM   6314 C  CA   . PHE   B 1 168 ? 32.411 -36.694 -9.965  1.00 18.26 ?  168 PHE   B CA   1 
ATOM   6315 C  C    . PHE   B 1 168 ? 31.094 -36.957 -10.692 1.00 16.27 ?  168 PHE   B C    1 
ATOM   6316 O  O    . PHE   B 1 168 ? 30.052 -36.360 -10.355 1.00 16.69 ?  168 PHE   B O    1 
ATOM   6317 C  CB   . PHE   B 1 168 ? 33.169 -35.549 -10.632 1.00 18.82 ?  168 PHE   B CB   1 
ATOM   6318 C  CG   . PHE   B 1 168 ? 32.359 -34.299 -10.756 1.00 18.78 ?  168 PHE   B CG   1 
ATOM   6319 C  CD1  . PHE   B 1 168 ? 32.030 -33.565 -9.625  1.00 19.77 ?  168 PHE   B CD1  1 
ATOM   6320 C  CD2  . PHE   B 1 168 ? 31.898 -33.873 -11.984 1.00 17.92 ?  168 PHE   B CD2  1 
ATOM   6321 C  CE1  . PHE   B 1 168 ? 31.263 -32.421 -9.716  1.00 20.02 ?  168 PHE   B CE1  1 
ATOM   6322 C  CE2  . PHE   B 1 168 ? 31.140 -32.714 -12.090 1.00 19.08 ?  168 PHE   B CE2  1 
ATOM   6323 C  CZ   . PHE   B 1 168 ? 30.815 -31.988 -10.950 1.00 19.42 ?  168 PHE   B CZ   1 
ATOM   6324 H  H    . PHE   B 1 168 ? 33.967 -37.859 -10.379 1.00 22.79 ?  168 PHE   B H    1 
ATOM   6325 H  HA   . PHE   B 1 168 ? 32.198 -36.424 -9.063  1.00 22.08 ?  168 PHE   B HA   1 
ATOM   6326 H  HB2  . PHE   B 1 168 ? 33.953 -35.342 -10.100 1.00 22.75 ?  168 PHE   B HB2  1 
ATOM   6327 H  HB3  . PHE   B 1 168 ? 33.434 -35.819 -11.523 1.00 22.75 ?  168 PHE   B HB3  1 
ATOM   6328 H  HD1  . PHE   B 1 168 ? 32.325 -33.858 -8.792  1.00 23.89 ?  168 PHE   B HD1  1 
ATOM   6329 H  HD2  . PHE   B 1 168 ? 32.111 -34.351 -12.750 1.00 21.67 ?  168 PHE   B HD2  1 
ATOM   6330 H  HE1  . PHE   B 1 168 ? 31.052 -31.941 -8.948  1.00 24.19 ?  168 PHE   B HE1  1 
ATOM   6331 H  HE2  . PHE   B 1 168 ? 30.834 -32.431 -12.924 1.00 23.06 ?  168 PHE   B HE2  1 
ATOM   6332 H  HZ   . PHE   B 1 168 ? 30.299 -31.216 -11.018 1.00 23.47 ?  168 PHE   B HZ   1 
ATOM   6333 N  N    . LEU   B 1 169 ? 31.124 -37.845 -11.682 1.00 16.53 ?  169 LEU   B N    1 
ATOM   6334 C  CA   . LEU   B 1 169 ? 29.948 -38.150 -12.481 1.00 18.60 ?  169 LEU   B CA   1 
ATOM   6335 C  C    . LEU   B 1 169 ? 29.940 -39.587 -12.985 1.00 21.51 ?  169 LEU   B C    1 
ATOM   6336 O  O    . LEU   B 1 169 ? 29.031 -39.995 -13.711 1.00 23.95 ?  169 LEU   B O    1 
ATOM   6337 C  CB   . LEU   B 1 169 ? 29.868 -37.201 -13.676 1.00 20.42 ?  169 LEU   B CB   1 
ATOM   6338 C  CG   . LEU   B 1 169 ? 28.604 -36.349 -13.778 1.00 23.53 ?  169 LEU   B CG   1 
ATOM   6339 C  CD1  . LEU   B 1 169 ? 28.542 -35.697 -15.143 1.00 24.48 ?  169 LEU   B CD1  1 
ATOM   6340 C  CD2  . LEU   B 1 169 ? 27.351 -37.165 -13.513 1.00 23.75 ?  169 LEU   B CD2  1 
ATOM   6341 O  OXT  . LEU   B 1 169 ? 30.842 -40.358 -12.683 1.00 22.49 -1 169 LEU   B OXT  1 
ATOM   6342 H  H    . LEU   B 1 169 ? 31.826 -38.284 -11.919 1.00 20.00 ?  169 LEU   B H    1 
ATOM   6343 H  HA   . LEU   B 1 169 ? 29.166 -38.019 -11.930 1.00 22.48 ?  169 LEU   B HA   1 
ATOM   6344 H  HB2  . LEU   B 1 169 ? 30.623 -36.592 -13.636 1.00 24.67 ?  169 LEU   B HB2  1 
ATOM   6345 H  HB3  . LEU   B 1 169 ? 29.924 -37.727 -14.490 1.00 24.67 ?  169 LEU   B HB3  1 
ATOM   6346 H  HG   . LEU   B 1 169 ? 28.646 -35.641 -13.114 1.00 28.40 ?  169 LEU   B HG   1 
ATOM   6347 H  HD11 . LEU   B 1 169 ? 27.753 -35.135 -15.187 1.00 29.54 ?  169 LEU   B HD11 1 
ATOM   6348 H  HD12 . LEU   B 1 169 ? 29.339 -35.160 -15.271 1.00 29.54 ?  169 LEU   B HD12 1 
ATOM   6349 H  HD13 . LEU   B 1 169 ? 28.496 -36.390 -15.819 1.00 29.54 ?  169 LEU   B HD13 1 
ATOM   6350 H  HD21 . LEU   B 1 169 ? 26.596 -36.737 -13.940 1.00 28.67 ?  169 LEU   B HD21 1 
ATOM   6351 H  HD22 . LEU   B 1 169 ? 27.476 -38.058 -13.875 1.00 28.67 ?  169 LEU   B HD22 1 
ATOM   6352 H  HD23 . LEU   B 1 169 ? 27.208 -37.216 -12.555 1.00 28.67 ?  169 LEU   B HD23 1 
HETATM 6353 N  N2   B A1A72 C 2 .   ? 14.841 -0.051  3.968   0.12 12.96 ?  201 A1A72 A N2   1 
HETATM 6354 C  C3   B A1A72 C 2 .   ? 15.031 1.118   3.298   0.12 12.75 ?  201 A1A72 A C3   1 
HETATM 6355 C  C6   B A1A72 C 2 .   ? 15.322 2.346   3.984   0.12 12.49 ?  201 A1A72 A C6   1 
HETATM 6356 C  C9   B A1A72 C 2 .   ? 14.348 0.301   -0.448  0.12 14.22 ?  201 A1A72 A C9   1 
HETATM 6357 C  C12  B A1A72 C 2 .   ? 10.700 0.003   -1.565  0.12 14.72 ?  201 A1A72 A C12  1 
HETATM 6358 C  C14  B A1A72 C 2 .   ? 11.066 2.284   -0.815  0.12 14.74 ?  201 A1A72 A C14  1 
HETATM 6359 C  C1   B A1A72 C 2 .   ? 15.688 -1.117  1.125   0.12 14.24 ?  201 A1A72 A C1   1 
HETATM 6360 C  C10  B A1A72 C 2 .   ? 12.904 0.679   -0.751  0.12 14.38 ?  201 A1A72 A C10  1 
HETATM 6361 C  C11  B A1A72 C 2 .   ? 12.029 -0.288  -1.267  0.12 14.58 ?  201 A1A72 A C11  1 
HETATM 6362 C  C13  B A1A72 C 2 .   ? 10.244 1.290   -1.330  0.12 14.77 ?  201 A1A72 A C13  1 
HETATM 6363 C  C15  B A1A72 C 2 .   ? 12.397 1.960   -0.529  0.12 14.41 ?  201 A1A72 A C15  1 
HETATM 6364 C  C2   B A1A72 C 2 .   ? 14.527 -0.087  1.107   0.12 13.90 ?  201 A1A72 A C2   1 
HETATM 6365 C  C4   B A1A72 C 2 .   ? 14.936 -0.013  5.334   0.12 12.88 ?  201 A1A72 A C4   1 
HETATM 6366 C  C5   B A1A72 C 2 .   ? 15.380 2.177   5.403   0.12 12.40 ?  201 A1A72 A C5   1 
HETATM 6367 C  C7   B A1A72 C 2 .   ? 15.590 3.748   3.745   0.12 12.51 ?  201 A1A72 A C7   1 
HETATM 6368 C  C8   B A1A72 C 2 .   ? 15.791 4.362   4.984   0.12 12.30 ?  201 A1A72 A C8   1 
HETATM 6369 N  N1   B A1A72 C 2 .   ? 14.931 1.086   1.886   0.12 13.05 ?  201 A1A72 A N1   1 
HETATM 6370 N  N3   B A1A72 C 2 .   ? 15.196 1.048   6.098   0.12 12.53 ?  201 A1A72 A N3   1 
HETATM 6371 N  N4   B A1A72 C 2 .   ? 15.668 3.417   5.972   0.12 12.40 ?  201 A1A72 A N4   1 
HETATM 6372 O  O1   B A1A72 C 2 .   ? 15.445 -2.041  0.085   0.12 14.09 ?  201 A1A72 A O1   1 
HETATM 6373 O  O2   B A1A72 C 2 .   ? 15.214 1.402   -0.681  0.12 14.45 ?  201 A1A72 A O2   1 
HETATM 6374 CL CL1  B A1A72 C 2 .   ? 8.583  1.640   -1.705  0.12 15.02 ?  201 A1A72 A CL1  1 
HETATM 6375 H  H2   B A1A72 C 2 .   ? 14.656 -0.526  -1.117  0.12 17.23 ?  201 A1A72 A H2   1 
HETATM 6376 H  H13  B A1A72 C 2 .   ? 10.022 -0.751  -1.973  0.12 17.83 ?  201 A1A72 A H13  1 
HETATM 6377 H  H14  B A1A72 C 2 .   ? 10.682 3.297   -0.641  0.12 17.85 ?  201 A1A72 A H14  1 
HETATM 6378 H  H4   B A1A72 C 2 .   ? 16.620 -0.598  1.036   0.12 17.25 ?  201 A1A72 A H4   1 
HETATM 6379 H  H5   B A1A72 C 2 .   ? 15.750 -1.676  2.036   0.12 17.25 ?  201 A1A72 A H5   1 
HETATM 6380 H  H12  B A1A72 C 2 .   ? 12.372 -1.310  -1.452  0.12 17.66 ?  201 A1A72 A H12  1 
HETATM 6381 H  H15  B A1A72 C 2 .   ? 13.057 2.733   -0.114  0.12 17.46 ?  201 A1A72 A H15  1 
HETATM 6382 H  H1   B A1A72 C 2 .   ? 13.569 -0.529  1.449   0.12 16.84 ?  201 A1A72 A H1   1 
HETATM 6383 H  H7   B A1A72 C 2 .   ? 14.781 -0.959  5.934   0.12 15.62 ?  201 A1A72 A H7   1 
HETATM 6384 H  H8   B A1A72 C 2 .   ? 15.632 4.260   2.830   0.12 15.18 ?  201 A1A72 A H8   1 
HETATM 6385 H  H9   B A1A72 C 2 .   ? 16.013 5.369   5.283   0.12 14.92 ?  201 A1A72 A H9   1 
HETATM 6386 H  H6   B A1A72 C 2 .   ? 15.155 1.910   1.409   0.12 15.82 ?  201 A1A72 A H6   1 
HETATM 6387 H  H10  B A1A72 C 2 .   ? 15.763 3.575   6.983   0.12 15.04 ?  201 A1A72 A H10  1 
HETATM 6388 H  H3   B A1A72 C 2 .   ? 16.227 -2.553  -0.045  0.12 17.07 ?  201 A1A72 A H3   1 
HETATM 6389 H  H11  B A1A72 C 2 .   ? 15.856 1.151   -1.360  0.12 17.50 ?  201 A1A72 A H11  1 
HETATM 6390 O  O1   C A1A73 D 3 .   ? 15.945 -2.303  -0.067  0.12 14.76 ?  202 A1A73 A O1   1 
HETATM 6391 C  C1   C A1A73 D 3 .   ? 15.956 -1.453  1.067   0.12 14.47 ?  202 A1A73 A C1   1 
HETATM 6392 C  C2   C A1A73 D 3 .   ? 14.863 -0.304  0.915   0.12 14.13 ?  202 A1A73 A C2   1 
HETATM 6393 C  C3   C A1A73 D 3 .   ? 15.229 0.997   3.171   0.12 12.51 ?  202 A1A73 A C3   1 
HETATM 6394 C  C4   C A1A73 D 3 .   ? 14.979 -0.091  5.313   0.12 12.41 ?  202 A1A73 A C4   1 
HETATM 6395 C  C5   C A1A73 D 3 .   ? 15.347 2.126   5.322   0.12 11.77 ?  202 A1A73 A C5   1 
HETATM 6396 C  C6   C A1A73 D 3 .   ? 15.416 2.245   3.877   0.12 11.97 ?  202 A1A73 A C6   1 
HETATM 6397 C  C7   C A1A73 D 3 .   ? 15.663 3.664   3.623   0.12 11.83 ?  202 A1A73 A C7   1 
HETATM 6398 C  C8   C A1A73 D 3 .   ? 15.727 4.314   4.861   0.12 11.57 ?  202 A1A73 A C8   1 
HETATM 6399 C  C10  C A1A73 D 3 .   ? 12.265 -0.097  0.421   0.12 15.38 ?  202 A1A73 A C10  1 
HETATM 6400 C  C11  C A1A73 D 3 .   ? 11.764 -0.685  -0.774  0.12 15.46 ?  202 A1A73 A C11  1 
HETATM 6401 C  C12  C A1A73 D 3 .   ? 10.787 -0.038  -1.567  0.12 15.75 ?  202 A1A73 A C12  1 
HETATM 6402 C  C13  C A1A73 D 3 .   ? 10.311 1.215   -1.152  0.12 16.07 ?  202 A1A73 A C13  1 
HETATM 6403 C  C14  C A1A73 D 3 .   ? 10.772 1.842   0.014   0.12 15.76 ?  202 A1A73 A C14  1 
HETATM 6404 C  C15  C A1A73 D 3 .   ? 11.752 1.172   0.796   0.12 15.63 ?  202 A1A73 A C15  1 
HETATM 6405 C  C9   C A1A73 D 3 .   ? 13.356 -0.840  1.287   0.12 15.17 ?  202 A1A73 A C9   1 
HETATM 6406 N  N1   C A1A73 D 3 .   ? 15.268 0.902   1.728   0.12 13.28 ?  202 A1A73 A N1   1 
HETATM 6407 N  N2   C A1A73 D 3 .   ? 15.023 -0.137  3.921   0.12 12.52 ?  202 A1A73 A N2   1 
HETATM 6408 N  N3   C A1A73 D 3 .   ? 15.134 0.999   6.084   0.12 12.01 ?  202 A1A73 A N3   1 
HETATM 6409 N  N4   C A1A73 D 3 .   ? 15.539 3.375   5.819   0.12 11.66 ?  202 A1A73 A N4   1 
HETATM 6410 O  O2   C A1A73 D 3 .   ? 13.280 -2.240  1.088   0.12 15.65 ?  202 A1A73 A O2   1 
HETATM 6411 CL CL1  C A1A73 D 3 .   ? 9.052  2.046   -2.173  0.12 17.16 ?  202 A1A73 A CL1  1 
HETATM 6412 H  H3   C A1A73 D 3 .   ? 16.766 -2.824  -0.099  0.12 17.88 ?  202 A1A73 A H3   1 
HETATM 6413 H  H4   C A1A73 D 3 .   ? 16.950 -0.979  1.195   0.12 17.53 ?  202 A1A73 A H4   1 
HETATM 6414 H  H5   C A1A73 D 3 .   ? 15.728 -2.053  1.983   0.12 17.53 ?  202 A1A73 A H5   1 
HETATM 6415 H  H1   C A1A73 D 3 .   ? 14.802 0.007   -0.167  0.12 17.13 ?  202 A1A73 A H1   1 
HETATM 6416 H  H7   C A1A73 D 3 .   ? 14.796 -1.050  5.879   0.12 15.06 ?  202 A1A73 A H7   1 
HETATM 6417 H  H8   C A1A73 D 3 .   ? 15.780 4.193   2.687   0.12 14.36 ?  202 A1A73 A H8   1 
HETATM 6418 H  H9   C A1A73 D 3 .   ? 15.887 5.346   5.199   0.12 14.05 ?  202 A1A73 A H9   1 
HETATM 6419 H  H12  C A1A73 D 3 .   ? 12.141 -1.684  -1.101  0.12 18.71 ?  202 A1A73 A H12  1 
HETATM 6420 H  H13  C A1A73 D 3 .   ? 10.400 -0.513  -2.504  0.12 19.06 ?  202 A1A73 A H13  1 
HETATM 6421 H  H14  C A1A73 D 3 .   ? 10.380 2.846   0.330   0.12 19.08 ?  202 A1A73 A H14  1 
HETATM 6422 H  H15  C A1A73 D 3 .   ? 12.127 1.663   1.730   0.12 18.93 ?  202 A1A73 A H15  1 
HETATM 6423 H  H2   C A1A73 D 3 .   ? 13.184 -0.630  2.374   0.12 18.37 ?  202 A1A73 A H2   1 
HETATM 6424 H  H6   C A1A73 D 3 .   ? 15.590 1.707   1.185   0.12 16.11 ?  202 A1A73 A H6   1 
HETATM 6425 H  H10  C A1A73 D 3 .   ? 15.538 3.587   6.843   0.12 14.16 ?  202 A1A73 A H10  1 
HETATM 6426 H  H11  C A1A73 D 3 .   ? 12.589 -2.653  1.634   0.12 18.94 ?  202 A1A73 A H11  1 
HETATM 6427 N  N2   D A1A72 E 2 .   ? 14.944 -0.178  3.940   0.16 11.63 ?  203 A1A72 A N2   1 
HETATM 6428 C  C3   D A1A72 E 2 .   ? 15.115 0.955   3.212   0.16 11.27 ?  203 A1A72 A C3   1 
HETATM 6429 C  C6   D A1A72 E 2 .   ? 15.353 2.210   3.867   0.16 10.60 ?  203 A1A72 A C6   1 
HETATM 6430 C  C9   D A1A72 E 2 .   ? 13.091 -0.902  1.360   0.16 13.46 ?  203 A1A72 A C9   1 
HETATM 6431 C  C12  D A1A72 E 2 .   ? 10.644 -0.027  -1.501  0.16 15.13 ?  203 A1A72 A C12  1 
HETATM 6432 C  C14  D A1A72 E 2 .   ? 10.905 1.944   -0.111  0.16 14.80 ?  203 A1A72 A C14  1 
HETATM 6433 C  C1   D A1A72 E 2 .   ? 14.964 -0.387  -0.421  0.16 13.20 ?  203 A1A72 A C1   1 
HETATM 6434 C  C10  D A1A72 E 2 .   ? 12.120 -0.104  0.465   0.16 14.16 ?  203 A1A72 A C10  1 
HETATM 6435 C  C11  D A1A72 E 2 .   ? 11.527 -0.711  -0.659  0.16 14.45 ?  203 A1A72 A C11  1 
HETATM 6436 C  C13  D A1A72 E 2 .   ? 10.350 1.296   -1.201  0.16 15.50 ?  203 A1A72 A C13  1 
HETATM 6437 C  C15  D A1A72 E 2 .   ? 11.787 1.234   0.712   0.16 14.61 ?  203 A1A72 A C15  1 
HETATM 6438 C  C2   D A1A72 E 2 .   ? 14.699 -0.479  1.144   0.16 12.92 ?  203 A1A72 A C2   1 
HETATM 6439 C  C4   D A1A72 E 2 .   ? 14.991 -0.099  5.311   0.16 11.49 ?  203 A1A72 A C4   1 
HETATM 6440 C  C5   D A1A72 E 2 .   ? 15.370 2.091   5.307   0.16 10.39 ?  203 A1A72 A C5   1 
HETATM 6441 C  C7   D A1A72 E 2 .   ? 15.589 3.609   3.580   0.16 10.43 ?  203 A1A72 A C7   1 
HETATM 6442 C  C8   D A1A72 E 2 .   ? 15.736 4.273   4.802   0.16 10.05 ?  203 A1A72 A C8   1 
HETATM 6443 N  N1   D A1A72 E 2 .   ? 15.051 0.816   1.790   0.16 12.00 ?  203 A1A72 A N1   1 
HETATM 6444 N  N3   D A1A72 E 2 .   ? 15.200 0.987   6.072   0.16 10.85 ?  203 A1A72 A N3   1 
HETATM 6445 N  N4   D A1A72 E 2 .   ? 15.607 3.360   5.824   0.16 10.20 ?  203 A1A72 A N4   1 
HETATM 6446 O  O1   D A1A72 E 2 .   ? 16.318 -0.011  -0.568  0.16 13.37 ?  203 A1A72 A O1   1 
HETATM 6447 O  O2   D A1A72 E 2 .   ? 12.930 -2.276  1.042   0.16 12.46 ?  203 A1A72 A O2   1 
HETATM 6448 CL CL1  D A1A72 E 2 .   ? 9.252  2.178   -2.227  0.16 17.08 ?  203 A1A72 A CL1  1 
HETATM 6449 H  H2   D A1A72 E 2 .   ? 12.822 -0.749  2.430   0.16 16.32 ?  203 A1A72 A H2   1 
HETATM 6450 H  H13  D A1A72 E 2 .   ? 10.186 -0.514  -2.374  0.16 18.32 ?  203 A1A72 A H13  1 
HETATM 6451 H  H14  D A1A72 E 2 .   ? 10.646 2.993   0.092   0.16 17.93 ?  203 A1A72 A H14  1 
HETATM 6452 H  H4   D A1A72 E 2 .   ? 14.776 -1.330  -0.938  0.16 16.01 ?  203 A1A72 A H4   1 
HETATM 6453 H  H5   D A1A72 E 2 .   ? 14.322 0.381   -0.906  0.16 16.01 ?  203 A1A72 A H5   1 
HETATM 6454 H  H12  D A1A72 E 2 .   ? 11.747 -1.750  -0.908  0.16 17.51 ?  203 A1A72 A H12  1 
HETATM 6455 H  H15  D A1A72 E 2 .   ? 12.220 1.749   1.570   0.16 17.70 ?  203 A1A72 A H15  1 
HETATM 6456 H  H1   D A1A72 E 2 .   ? 15.276 -1.309  1.576   0.16 15.66 ?  203 A1A72 A H1   1 
HETATM 6457 H  H7   D A1A72 E 2 .   ? 14.840 -1.038  5.910   0.16 13.96 ?  203 A1A72 A H7   1 
HETATM 6458 H  H8   D A1A72 E 2 .   ? 15.647 4.095   2.645   0.16 12.68 ?  203 A1A72 A H8   1 
HETATM 6459 H  H9   D A1A72 E 2 .   ? 15.919 5.297   5.068   0.16 12.23 ?  203 A1A72 A H9   1 
HETATM 6460 H  H6   D A1A72 E 2 .   ? 15.251 1.603   1.234   0.16 14.57 ?  203 A1A72 A H6   1 
HETATM 6461 H  H10  D A1A72 E 2 .   ? 15.663 3.556   6.830   0.16 12.41 ?  203 A1A72 A H10  1 
HETATM 6462 H  H3   D A1A72 E 2 .   ? 16.529 -0.029  -1.509  0.16 16.21 ?  203 A1A72 A H3   1 
HETATM 6463 H  H11  D A1A72 E 2 .   ? 12.234 -2.648  1.580   0.16 15.12 ?  203 A1A72 A H11  1 
HETATM 6464 CL CL   C CL    F 4 .   ? 16.020 2.850   -0.946  0.28 13.92 ?  204 CL    A CL   1 
HETATM 6465 O  O    . HOH   G 5 .   ? 15.942 2.139   24.718  1.00 44.07 ?  301 HOH   A O    1 
HETATM 6466 O  O    . HOH   G 5 .   ? 18.607 -2.384  -16.450 1.00 44.11 ?  302 HOH   A O    1 
HETATM 6467 O  O    . HOH   G 5 .   ? 14.769 -4.600  20.550  1.00 44.39 ?  303 HOH   A O    1 
HETATM 6468 O  O    . HOH   G 5 .   ? -0.420 -2.980  3.065   1.00 41.27 ?  304 HOH   A O    1 
HETATM 6469 O  O    . HOH   G 5 .   ? 34.312 -1.886  12.494  1.00 35.33 ?  305 HOH   A O    1 
HETATM 6470 O  O    . HOH   G 5 .   ? 9.197  -10.165 19.417  1.00 45.89 ?  306 HOH   A O    1 
HETATM 6471 O  O    . HOH   G 5 .   ? 11.743 -10.869 -10.100 1.00 46.96 ?  307 HOH   A O    1 
HETATM 6472 O  O    . HOH   G 5 .   ? 15.158 -12.208 18.684  1.00 39.99 ?  308 HOH   A O    1 
HETATM 6473 O  O    . HOH   G 5 .   ? 28.966 0.454   -9.697  1.00 21.59 ?  309 HOH   A O    1 
HETATM 6474 O  O    . HOH   G 5 .   ? 4.648  3.879   0.696   1.00 23.59 ?  310 HOH   A O    1 
HETATM 6475 O  O    . HOH   G 5 .   ? 28.613 -10.679 -14.025 1.00 41.39 ?  311 HOH   A O    1 
HETATM 6476 O  O    B HOH   G 5 .   ? 14.840 -2.862  3.415   0.40 13.94 ?  312 HOH   A O    1 
HETATM 6477 O  O    . HOH   G 5 .   ? 26.835 11.413  1.684   1.00 16.44 ?  313 HOH   A O    1 
HETATM 6478 O  O    . HOH   G 5 .   ? 12.040 0.335   14.805  1.00 37.40 ?  314 HOH   A O    1 
HETATM 6479 O  O    . HOH   G 5 .   ? 18.903 -21.994 6.946   1.00 32.04 ?  315 HOH   A O    1 
HETATM 6480 O  O    . HOH   G 5 .   ? 15.068 3.921   17.631  1.00 43.62 ?  316 HOH   A O    1 
HETATM 6481 O  O    . HOH   G 5 .   ? 42.435 10.535  5.140   1.00 19.99 ?  317 HOH   A O    1 
HETATM 6482 O  O    A HOH   G 5 .   ? 3.596  -9.470  9.730   0.60 33.70 ?  318 HOH   A O    1 
HETATM 6483 O  O    . HOH   G 5 .   ? 14.158 -4.522  -11.891 1.00 29.77 ?  319 HOH   A O    1 
HETATM 6484 O  O    A HOH   G 5 .   ? 6.945  -8.168  11.849  0.60 17.19 ?  320 HOH   A O    1 
HETATM 6485 O  O    . HOH   G 5 .   ? 14.714 -13.938 16.674  1.00 24.49 ?  321 HOH   A O    1 
HETATM 6486 O  O    . HOH   G 5 .   ? 19.899 -12.532 -8.910  1.00 26.44 ?  322 HOH   A O    1 
HETATM 6487 O  O    . HOH   G 5 .   ? 36.134 -5.103  -0.530  1.00 29.54 ?  323 HOH   A O    1 
HETATM 6488 O  O    . HOH   G 5 .   ? 30.236 -13.310 -8.536  1.00 20.77 ?  324 HOH   A O    1 
HETATM 6489 O  O    . HOH   G 5 .   ? 16.993 -19.280 4.890   1.00 15.27 ?  325 HOH   A O    1 
HETATM 6490 O  O    . HOH   G 5 .   ? 0.728  -4.610  0.178   1.00 32.79 ?  326 HOH   A O    1 
HETATM 6491 O  O    . HOH   G 5 .   ? 15.206 -8.071  -9.739  1.00 24.26 ?  327 HOH   A O    1 
HETATM 6492 O  O    . HOH   G 5 .   ? 28.208 -6.301  19.629  1.00 44.31 ?  328 HOH   A O    1 
HETATM 6493 O  O    . HOH   G 5 .   ? 9.855  -21.379 5.668   1.00 18.79 ?  329 HOH   A O    1 
HETATM 6494 O  O    . HOH   G 5 .   ? 7.936  -12.640 -0.849  1.00 23.57 ?  330 HOH   A O    1 
HETATM 6495 O  O    . HOH   G 5 .   ? 8.837  -11.936 17.238  1.00 40.59 ?  331 HOH   A O    1 
HETATM 6496 O  O    . HOH   G 5 .   ? 8.085  -21.527 4.007   1.00 51.58 ?  332 HOH   A O    1 
HETATM 6497 O  O    . HOH   G 5 .   ? 26.498 -19.333 -1.779  1.00 14.10 ?  333 HOH   A O    1 
HETATM 6498 O  O    . HOH   G 5 .   ? 21.254 -2.413  -2.123  1.00 15.73 ?  334 HOH   A O    1 
HETATM 6499 O  O    B HOH   G 5 .   ? 15.265 6.862   7.088   0.40 18.32 ?  335 HOH   A O    1 
HETATM 6500 O  O    . HOH   G 5 .   ? 37.542 2.813   10.216  1.00 29.13 ?  336 HOH   A O    1 
HETATM 6501 O  O    . HOH   G 5 .   ? 38.286 10.138  7.132   1.00 45.18 ?  337 HOH   A O    1 
HETATM 6502 O  O    . HOH   G 5 .   ? 34.005 -1.047  -8.932  1.00 26.46 ?  338 HOH   A O    1 
HETATM 6503 O  O    B HOH   G 5 .   ? 12.153 -2.215  -4.300  0.40 20.16 ?  339 HOH   A O    1 
HETATM 6504 O  O    . HOH   G 5 .   ? 38.580 4.998   6.964   1.00 15.45 ?  340 HOH   A O    1 
HETATM 6505 O  O    . HOH   G 5 .   ? 31.022 -18.137 7.785   1.00 19.65 ?  341 HOH   A O    1 
HETATM 6506 O  O    . HOH   G 5 .   ? 13.521 -15.243 -7.521  1.00 27.40 ?  342 HOH   A O    1 
HETATM 6507 O  O    . HOH   G 5 .   ? 20.632 -19.736 -5.098  1.00 27.57 ?  343 HOH   A O    1 
HETATM 6508 O  O    A HOH   G 5 .   ? 17.493 -1.716  0.446   0.60 18.23 ?  344 HOH   A O    1 
HETATM 6509 O  O    . HOH   G 5 .   ? 22.347 5.385   18.989  1.00 44.78 ?  345 HOH   A O    1 
HETATM 6510 O  O    . HOH   G 5 .   ? 27.301 13.790  2.862   1.00 29.36 ?  346 HOH   A O    1 
HETATM 6511 O  O    . HOH   G 5 .   ? 42.558 4.294   5.426   1.00 30.23 ?  347 HOH   A O    1 
HETATM 6512 O  O    . HOH   G 5 .   ? 22.745 12.516  1.612   1.00 14.62 ?  348 HOH   A O    1 
HETATM 6513 O  O    . HOH   G 5 .   ? 31.727 8.193   14.816  1.00 24.53 ?  349 HOH   A O    1 
HETATM 6514 O  O    . HOH   G 5 .   ? -0.727 -8.547  2.170   1.00 45.22 ?  350 HOH   A O    1 
HETATM 6515 O  O    . HOH   G 5 .   ? 44.343 7.134   6.439   1.00 26.71 ?  351 HOH   A O    1 
HETATM 6516 O  O    . HOH   G 5 .   ? 17.182 -18.054 14.948  1.00 26.31 ?  352 HOH   A O    1 
HETATM 6517 O  O    . HOH   G 5 .   ? 37.242 -2.831  9.660   1.00 40.19 ?  353 HOH   A O    1 
HETATM 6518 O  O    . HOH   G 5 .   ? 17.148 -17.824 -5.039  1.00 27.02 ?  354 HOH   A O    1 
HETATM 6519 O  O    . HOH   G 5 .   ? 18.646 -19.385 13.556  1.00 36.27 ?  355 HOH   A O    1 
HETATM 6520 O  O    . HOH   G 5 .   ? 28.371 -0.206  -13.391 1.00 36.15 ?  356 HOH   A O    1 
HETATM 6521 O  O    . HOH   G 5 .   ? 39.769 -1.026  -5.155  1.00 20.81 ?  357 HOH   A O    1 
HETATM 6522 O  O    B HOH   G 5 .   ? 11.283 6.434   8.996   0.40 25.49 ?  358 HOH   A O    1 
HETATM 6523 O  O    . HOH   G 5 .   ? 13.325 -1.468  -6.635  1.00 18.19 ?  359 HOH   A O    1 
HETATM 6524 O  O    . HOH   G 5 .   ? 14.370 -21.215 -4.305  1.00 29.54 ?  360 HOH   A O    1 
HETATM 6525 O  O    . HOH   G 5 .   ? 24.034 -2.100  -2.101  1.00 10.92 ?  361 HOH   A O    1 
HETATM 6526 O  O    . HOH   G 5 .   ? 35.773 -12.658 6.847   1.00 15.96 ?  362 HOH   A O    1 
HETATM 6527 O  O    . HOH   G 5 .   ? 31.074 -13.948 -2.464  1.00 13.75 ?  363 HOH   A O    1 
HETATM 6528 O  O    . HOH   G 5 .   ? 27.488 -6.174  -14.015 1.00 39.82 ?  364 HOH   A O    1 
HETATM 6529 O  O    . HOH   G 5 .   ? 25.720 -0.793  -7.328  1.00 16.52 ?  365 HOH   A O    1 
HETATM 6530 O  O    . HOH   G 5 .   ? 22.154 -19.251 11.391  1.00 34.02 ?  366 HOH   A O    1 
HETATM 6531 O  O    . HOH   G 5 .   ? 37.348 11.944  4.924   1.00 29.31 ?  367 HOH   A O    1 
HETATM 6532 O  O    A HOH   G 5 .   ? 11.030 1.545   12.756  0.60 18.71 ?  368 HOH   A O    1 
HETATM 6533 O  O    B HOH   G 5 .   ? 21.369 2.951   0.031   0.40 17.40 ?  369 HOH   A O    1 
HETATM 6534 O  O    . HOH   G 5 .   ? 31.851 -9.355  -6.666  1.00 22.20 ?  370 HOH   A O    1 
HETATM 6535 O  O    . HOH   G 5 .   ? 30.812 3.078   8.270   1.00 11.87 ?  371 HOH   A O    1 
HETATM 6536 O  O    . HOH   G 5 .   ? 43.914 8.452   -3.061  1.00 28.05 ?  372 HOH   A O    1 
HETATM 6537 O  O    . HOH   G 5 .   ? 21.912 -21.924 8.439   1.00 28.66 ?  373 HOH   A O    1 
HETATM 6538 O  O    . HOH   G 5 .   ? 18.592 9.466   9.018   1.00 21.00 ?  374 HOH   A O    1 
HETATM 6539 O  O    . HOH   G 5 .   ? 33.660 -7.159  4.298   1.00 16.39 ?  375 HOH   A O    1 
HETATM 6540 O  O    . HOH   G 5 .   ? 21.738 -8.809  21.357  1.00 57.00 ?  376 HOH   A O    1 
HETATM 6541 O  O    . HOH   G 5 .   ? 5.209  2.670   5.112   1.00 31.27 ?  377 HOH   A O    1 
HETATM 6542 O  O    . HOH   G 5 .   ? 15.470 11.913  7.922   1.00 38.65 ?  378 HOH   A O    1 
HETATM 6543 O  O    . HOH   G 5 .   ? 23.966 -15.693 -9.121  1.00 32.09 ?  379 HOH   A O    1 
HETATM 6544 O  O    . HOH   G 5 .   ? 10.349 -22.169 -1.281  1.00 48.80 ?  380 HOH   A O    1 
HETATM 6545 O  O    . HOH   G 5 .   ? 24.715 -17.518 12.702  1.00 24.05 ?  381 HOH   A O    1 
HETATM 6546 O  O    . HOH   G 5 .   ? 11.736 -10.725 17.000  1.00 25.81 ?  382 HOH   A O    1 
HETATM 6547 O  O    . HOH   G 5 .   ? 31.815 -7.279  -9.818  1.00 21.05 ?  383 HOH   A O    1 
HETATM 6548 O  O    . HOH   G 5 .   ? 6.755  -3.332  12.964  1.00 31.71 ?  384 HOH   A O    1 
HETATM 6549 O  O    . HOH   G 5 .   ? 23.485 11.385  4.087   1.00 12.19 ?  385 HOH   A O    1 
HETATM 6550 O  O    B HOH   G 5 .   ? 22.667 5.709   -1.648  0.40 18.69 ?  386 HOH   A O    1 
HETATM 6551 O  O    . HOH   G 5 .   ? 16.536 -22.074 0.975   1.00 27.99 ?  387 HOH   A O    1 
HETATM 6552 O  O    . HOH   G 5 .   ? 43.371 7.839   2.694   1.00 27.60 ?  388 HOH   A O    1 
HETATM 6553 O  O    . HOH   G 5 .   ? 27.497 -10.631 14.075  1.00 17.22 ?  389 HOH   A O    1 
HETATM 6554 O  O    . HOH   G 5 .   ? 26.962 4.161   -0.656  1.00 12.55 ?  390 HOH   A O    1 
HETATM 6555 O  O    . HOH   G 5 .   ? 21.221 10.252  15.050  1.00 37.64 ?  391 HOH   A O    1 
HETATM 6556 O  O    . HOH   G 5 .   ? 15.199 -21.571 14.190  1.00 17.51 ?  392 HOH   A O    1 
HETATM 6557 O  O    . HOH   G 5 .   ? 14.467 -24.731 11.575  1.00 30.44 ?  393 HOH   A O    1 
HETATM 6558 O  O    A HOH   G 5 .   ? 14.271 0.569   6.804   0.60 22.11 ?  394 HOH   A O    1 
HETATM 6559 O  O    . HOH   G 5 .   ? 13.953 -4.934  17.434  1.00 26.04 ?  395 HOH   A O    1 
HETATM 6560 O  O    . HOH   G 5 .   ? 6.435  -5.528  11.192  1.00 21.17 ?  396 HOH   A O    1 
HETATM 6561 O  O    A HOH   G 5 .   ? 14.632 -3.657  3.101   0.60 15.95 ?  397 HOH   A O    1 
HETATM 6562 O  O    . HOH   G 5 .   ? 24.421 3.593   -1.826  1.00 14.91 ?  398 HOH   A O    1 
HETATM 6563 O  O    . HOH   G 5 .   ? 24.229 -7.763  14.453  1.00 16.68 ?  399 HOH   A O    1 
HETATM 6564 O  O    . HOH   G 5 .   ? 32.780 -9.242  5.964   1.00 19.68 ?  400 HOH   A O    1 
HETATM 6565 O  O    . HOH   G 5 .   ? 30.682 1.861   16.690  1.00 21.02 ?  401 HOH   A O    1 
HETATM 6566 O  O    . HOH   G 5 .   ? 37.550 -1.994  5.776   1.00 26.03 ?  402 HOH   A O    1 
HETATM 6567 O  O    . HOH   G 5 .   ? 21.825 -13.750 -8.128  1.00 46.32 ?  403 HOH   A O    1 
HETATM 6568 O  O    . HOH   G 5 .   ? 14.554 -0.477  -12.098 1.00 27.13 ?  404 HOH   A O    1 
HETATM 6569 O  O    . HOH   G 5 .   ? 16.243 -14.132 20.217  1.00 45.41 ?  405 HOH   A O    1 
HETATM 6570 O  O    . HOH   G 5 .   ? 18.980 -0.690  -1.684  1.00 14.01 ?  406 HOH   A O    1 
HETATM 6571 O  O    . HOH   G 5 .   ? 27.306 2.336   18.711  1.00 32.04 ?  407 HOH   A O    1 
HETATM 6572 O  O    . HOH   G 5 .   ? 20.572 -20.042 2.758   1.00 17.72 ?  408 HOH   A O    1 
HETATM 6573 O  O    A HOH   G 5 .   ? 20.097 4.544   -7.539  0.60 15.83 ?  409 HOH   A O    1 
HETATM 6574 O  O    B HOH   G 5 .   ? 18.428 -1.647  0.546   0.40 22.94 ?  410 HOH   A O    1 
HETATM 6575 O  O    . HOH   G 5 .   ? 14.079 -23.092 7.422   1.00 17.96 ?  411 HOH   A O    1 
HETATM 6576 O  O    . HOH   G 5 .   ? 30.053 -10.098 13.033  1.00 22.07 ?  412 HOH   A O    1 
HETATM 6577 O  O    A HOH   G 5 .   ? 21.345 3.154   -0.342  0.60 9.77  ?  413 HOH   A O    1 
HETATM 6578 O  O    B HOH   G 5 .   ? 10.969 1.998   11.999  0.40 20.09 ?  414 HOH   A O    1 
HETATM 6579 O  O    . HOH   G 5 .   ? 38.125 -1.335  -1.929  1.00 18.71 ?  415 HOH   A O    1 
HETATM 6580 O  O    . HOH   G 5 .   ? 41.632 1.522   4.970   1.00 34.82 ?  416 HOH   A O    1 
HETATM 6581 O  O    A HOH   G 5 .   ? 22.729 -12.058 21.877  0.60 34.16 ?  417 HOH   A O    1 
HETATM 6582 O  O    . HOH   G 5 .   ? 40.910 -8.302  -6.746  1.00 37.08 ?  418 HOH   A O    1 
HETATM 6583 O  O    . HOH   G 5 .   ? 32.513 -10.621 3.170   1.00 30.70 ?  419 HOH   A O    1 
HETATM 6584 O  O    . HOH   G 5 .   ? 30.329 -12.946 13.508  1.00 19.75 ?  420 HOH   A O    1 
HETATM 6585 O  O    A HOH   G 5 .   ? 15.797 -0.949  5.275   0.60 25.48 ?  421 HOH   A O    1 
HETATM 6586 O  O    . HOH   G 5 .   ? 7.597  -6.300  -6.531  1.00 40.33 ?  422 HOH   A O    1 
HETATM 6587 O  O    . HOH   G 5 .   ? 16.030 6.965   2.923   1.00 17.65 ?  423 HOH   A O    1 
HETATM 6588 O  O    . HOH   G 5 .   ? 32.666 -4.325  -9.891  1.00 27.82 ?  424 HOH   A O    1 
HETATM 6589 O  O    . HOH   G 5 .   ? 23.928 -20.288 -1.345  1.00 16.51 ?  425 HOH   A O    1 
HETATM 6590 O  O    . HOH   G 5 .   ? 30.943 6.209   -12.282 1.00 28.79 ?  426 HOH   A O    1 
HETATM 6591 O  O    . HOH   G 5 .   ? 24.063 3.925   -4.848  1.00 23.45 ?  427 HOH   A O    1 
HETATM 6592 O  O    . HOH   G 5 .   ? 35.088 -5.223  -3.072  1.00 17.38 ?  428 HOH   A O    1 
HETATM 6593 O  O    A HOH   G 5 .   ? 24.581 2.041   -6.980  0.60 14.84 ?  429 HOH   A O    1 
HETATM 6594 O  O    . HOH   G 5 .   ? 16.200 16.688  8.668   1.00 32.96 ?  430 HOH   A O    1 
HETATM 6595 O  O    . HOH   G 5 .   ? 44.941 -0.671  3.011   1.00 41.27 ?  431 HOH   A O    1 
HETATM 6596 O  O    . HOH   G 5 .   ? 27.924 0.816   -7.160  1.00 14.57 ?  432 HOH   A O    1 
HETATM 6597 O  O    . HOH   G 5 .   ? 36.744 -4.958  5.375   1.00 23.90 ?  433 HOH   A O    1 
HETATM 6598 O  O    . HOH   G 5 .   ? 10.385 -13.761 -1.712  1.00 18.44 ?  434 HOH   A O    1 
HETATM 6599 O  O    . HOH   G 5 .   ? 27.057 -3.229  19.380  1.00 36.52 ?  435 HOH   A O    1 
HETATM 6600 O  O    . HOH   G 5 .   ? 37.736 -8.827  -3.469  1.00 23.18 ?  436 HOH   A O    1 
HETATM 6601 O  O    B HOH   G 5 .   ? 8.241  3.910   1.364   0.40 19.59 ?  437 HOH   A O    1 
HETATM 6602 O  O    B HOH   G 5 .   ? 19.784 5.196   -6.915  0.40 33.34 ?  438 HOH   A O    1 
HETATM 6603 O  O    A HOH   G 5 .   ? 18.860 2.032   -0.745  0.60 10.78 ?  439 HOH   A O    1 
HETATM 6604 O  O    . HOH   G 5 .   ? 22.617 8.149   18.404  1.00 49.35 ?  440 HOH   A O    1 
HETATM 6605 O  O    A HOH   G 5 .   ? 21.508 -14.691 18.035  0.60 35.20 ?  441 HOH   A O    1 
HETATM 6606 O  O    . HOH   G 5 .   ? 18.500 4.887   -15.119 1.00 51.59 ?  442 HOH   A O    1 
HETATM 6607 O  O    A HOH   G 5 .   ? 11.064 -0.383  1.937   0.72 23.00 ?  443 HOH   A O    1 
HETATM 6608 O  O    . HOH   G 5 .   ? 23.518 -8.043  17.072  1.00 21.80 ?  444 HOH   A O    1 
HETATM 6609 O  O    . HOH   G 5 .   ? 23.240 7.614   -3.199  1.00 28.87 ?  445 HOH   A O    1 
HETATM 6610 O  O    . HOH   G 5 .   ? -1.368 -5.044  7.653   1.00 42.88 ?  446 HOH   A O    1 
HETATM 6611 O  O    . HOH   G 5 .   ? 23.334 -20.954 1.333   1.00 18.73 ?  447 HOH   A O    1 
HETATM 6612 O  O    A HOH   G 5 .   ? 16.255 2.946   -1.435  0.60 14.74 ?  448 HOH   A O    1 
HETATM 6613 O  O    A HOH   G 5 .   ? 19.307 -11.048 24.155  0.60 45.45 ?  449 HOH   A O    1 
HETATM 6614 O  O    . HOH   G 5 .   ? 34.407 -8.103  -0.508  1.00 27.65 ?  450 HOH   A O    1 
HETATM 6615 O  O    B HOH   G 5 .   ? 7.284  3.777   4.017   0.40 23.61 ?  451 HOH   A O    1 
HETATM 6616 O  O    A HOH   G 5 .   ? 18.340 -16.064 16.431  0.60 28.91 ?  452 HOH   A O    1 
HETATM 6617 O  O    . HOH   G 5 .   ? 9.448  -16.327 -2.058  1.00 44.23 ?  453 HOH   A O    1 
HETATM 6618 O  O    B HOH   G 5 .   ? 9.310  2.344   7.942   0.40 24.52 ?  454 HOH   A O    1 
HETATM 6619 O  O    B HOH   G 5 .   ? 18.629 1.858   -0.461  0.40 17.89 ?  455 HOH   A O    1 
HETATM 6620 O  O    . HOH   G 5 .   ? 31.332 -12.773 0.005   1.00 19.10 ?  456 HOH   A O    1 
HETATM 6621 O  O    . HOH   G 5 .   ? 30.599 14.782  2.776   1.00 18.93 ?  457 HOH   A O    1 
HETATM 6622 O  O    . HOH   G 5 .   ? 23.250 -12.918 19.346  1.00 48.34 ?  458 HOH   A O    1 
HETATM 6623 O  O    . HOH   G 5 .   ? 29.723 -16.019 10.675  1.00 33.22 ?  459 HOH   A O    1 
HETATM 6624 O  O    A HOH   G 5 .   ? 14.024 -0.342  3.466   0.60 21.51 ?  460 HOH   A O    1 
HETATM 6625 O  O    . HOH   G 5 .   ? 27.759 6.968   -6.495  1.00 37.38 ?  461 HOH   A O    1 
HETATM 6626 O  O    . HOH   G 5 .   ? 32.454 -15.918 10.828  1.00 31.81 ?  462 HOH   A O    1 
HETATM 6627 O  O    . HOH   G 5 .   ? 25.400 8.229   -4.799  1.00 23.48 ?  463 HOH   A O    1 
HETATM 6628 O  O    . HOH   G 5 .   ? 29.914 -1.970  -12.660 1.00 46.74 ?  464 HOH   A O    1 
HETATM 6629 O  O    . HOH   G 5 .   ? 19.915 -17.361 -5.112  1.00 24.31 ?  465 HOH   A O    1 
HETATM 6630 O  O    . HOH   G 5 .   ? 24.926 5.638   20.741  1.00 54.02 ?  466 HOH   A O    1 
HETATM 6631 O  O    . HOH   G 5 .   ? 23.175 -22.344 -3.380  1.00 34.81 ?  467 HOH   A O    1 
HETATM 6632 O  O    . HOH   G 5 .   ? 20.901 -18.055 24.999  1.00 54.66 ?  468 HOH   A O    1 
HETATM 6633 O  O    . HOH   G 5 .   ? 22.051 5.232   -6.052  1.00 29.12 ?  469 HOH   A O    1 
HETATM 6634 O  O    . HOH   G 5 .   ? 11.965 -13.378 16.327  1.00 48.23 ?  470 HOH   A O    1 
HETATM 6635 O  O    . HOH   G 5 .   ? 24.638 14.590  7.835   1.00 35.80 ?  471 HOH   A O    1 
HETATM 6636 O  O    . HOH   G 5 .   ? 26.908 11.650  -1.363  1.00 29.90 ?  472 HOH   A O    1 
HETATM 6637 O  O    . HOH   G 5 .   ? 39.618 -7.036  -3.534  1.00 47.33 ?  473 HOH   A O    1 
HETATM 6638 O  O    . HOH   G 5 .   ? 23.494 13.722  5.521   1.00 18.44 ?  474 HOH   A O    1 
HETATM 6639 O  O    . HOH   G 5 .   ? 18.798 10.892  11.316  1.00 33.50 ?  475 HOH   A O    1 
HETATM 6640 O  O    . HOH   G 5 .   ? 15.744 -21.529 3.681   1.00 22.22 ?  476 HOH   A O    1 
HETATM 6641 O  O    . HOH   G 5 .   ? 11.027 -15.045 -6.091  1.00 35.97 ?  477 HOH   A O    1 
HETATM 6642 O  O    . HOH   G 5 .   ? 27.462 -11.423 16.578  1.00 36.71 ?  478 HOH   A O    1 
HETATM 6643 O  O    . HOH   G 5 .   ? 12.370 1.667   17.317  1.00 40.05 ?  479 HOH   A O    1 
HETATM 6644 O  O    . HOH   G 5 .   ? 25.841 10.789  -3.759  1.00 24.80 ?  480 HOH   A O    1 
HETATM 6645 O  O    . HOH   G 5 .   ? 23.161 11.858  -4.050  1.00 19.49 ?  481 HOH   A O    1 
HETATM 6646 O  O    . HOH   G 5 .   ? 35.159 7.447   12.248  1.00 44.74 ?  482 HOH   A O    1 
HETATM 6647 O  O    . HOH   G 5 .   ? 18.111 -16.259 -8.814  1.00 39.72 ?  483 HOH   A O    1 
HETATM 6648 O  O    . HOH   G 5 .   ? 28.827 8.998   17.535  1.00 37.22 ?  484 HOH   A O    1 
HETATM 6649 O  O    . HOH   G 5 .   ? 16.001 -6.780  -11.896 1.00 44.95 ?  485 HOH   A O    1 
HETATM 6650 O  O    . HOH   G 5 .   ? 17.385 -18.726 19.752  1.00 48.97 ?  486 HOH   A O    1 
HETATM 6651 O  O    . HOH   G 5 .   ? 41.011 -3.970  -0.330  1.00 38.20 ?  487 HOH   A O    1 
HETATM 6652 O  O    . HOH   G 5 .   ? 14.022 -10.342 -10.928 1.00 33.35 ?  488 HOH   A O    1 
HETATM 6653 O  O    . HOH   G 5 .   ? 30.785 0.727   19.172  1.00 40.02 ?  489 HOH   A O    1 
HETATM 6654 O  O    . HOH   G 5 .   ? 16.856 -20.597 16.106  1.00 28.01 ?  490 HOH   A O    1 
HETATM 6655 O  O    . HOH   G 5 .   ? 15.747 -17.216 -6.988  1.00 31.72 ?  491 HOH   A O    1 
HETATM 6656 O  O    . HOH   G 5 .   ? 28.557 -4.671  -12.341 1.00 39.50 ?  492 HOH   A O    1 
HETATM 6657 O  O    . HOH   G 5 .   ? 31.484 -0.610  -10.561 1.00 28.82 ?  493 HOH   A O    1 
HETATM 6658 O  O    . HOH   G 5 .   ? 28.663 -7.988  -15.237 1.00 52.58 ?  494 HOH   A O    1 
HETATM 6659 O  O    . HOH   G 5 .   ? 41.729 9.321   -4.048  1.00 33.17 ?  495 HOH   A O    1 
HETATM 6660 O  O    . HOH   G 5 .   ? 20.040 -22.336 4.194   1.00 29.03 ?  496 HOH   A O    1 
HETATM 6661 O  O    . HOH   G 5 .   ? 44.533 10.481  -1.569  1.00 31.73 ?  497 HOH   A O    1 
HETATM 6662 O  O    . HOH   G 5 .   ? 18.490 -23.231 1.896   1.00 41.01 ?  498 HOH   A O    1 
HETATM 6663 O  O    . HOH   G 5 .   ? 39.194 2.377   7.518   1.00 31.49 ?  499 HOH   A O    1 
HETATM 6664 O  O    . HOH   G 5 .   ? 25.773 -18.907 -11.902 1.00 39.09 ?  500 HOH   A O    1 
HETATM 6665 O  O    . HOH   G 5 .   ? 40.527 -0.279  -7.824  1.00 33.17 ?  501 HOH   A O    1 
HETATM 6666 O  O    . HOH   G 5 .   ? 14.030 -25.283 8.941   1.00 31.56 ?  502 HOH   A O    1 
HETATM 6667 O  O    . HOH   G 5 .   ? 8.085  -3.162  -5.748  1.00 49.17 ?  503 HOH   A O    1 
HETATM 6668 O  O    . HOH   G 5 .   ? 16.164 -23.400 5.728   1.00 27.48 ?  504 HOH   A O    1 
HETATM 6669 O  O    . HOH   G 5 .   ? 30.723 -5.844  -11.820 1.00 49.42 ?  505 HOH   A O    1 
HETATM 6670 O  O    B HOH   G 5 .   ? 7.418  5.668   5.638   0.40 32.24 ?  506 HOH   A O    1 
HETATM 6671 O  O    B HOH   G 5 .   ? 14.590 8.003   4.944   0.40 23.61 ?  507 HOH   A O    1 
HETATM 6672 O  O    . HOH   G 5 .   ? 37.395 -6.650  7.503   1.00 24.93 ?  508 HOH   A O    1 
HETATM 6673 O  O    . HOH   G 5 .   ? 23.186 -23.783 1.701   1.00 30.04 ?  509 HOH   A O    1 
HETATM 6674 O  O    . HOH   G 5 .   ? 20.548 -16.104 -7.384  1.00 29.01 ?  510 HOH   A O    1 
HETATM 6675 O  O    B HOH   G 5 .   ? 9.069  5.290   7.971   0.40 28.93 ?  511 HOH   A O    1 
HETATM 6676 O  O    . HOH   G 5 .   ? 39.546 -0.018  6.607   1.00 29.74 ?  512 HOH   A O    1 
HETATM 6677 O  O    . HOH   G 5 .   ? 30.671 5.820   -14.722 1.00 36.39 ?  513 HOH   A O    1 
HETATM 6678 O  O    . HOH   G 5 .   ? 29.029 14.404  0.868   1.00 49.50 ?  514 HOH   A O    1 
HETATM 6679 O  O    . HOH   G 5 .   ? 38.030 13.946  6.716   1.00 47.88 ?  515 HOH   A O    1 
HETATM 6680 O  O    . HOH   G 5 .   ? 36.434 -6.544  10.108  1.00 43.81 ?  516 HOH   A O    1 
HETATM 6681 O  O    . HOH   G 5 .   ? 22.012 -24.058 4.450   1.00 24.36 ?  517 HOH   A O    1 
HETATM 6682 O  O    . HOH   G 5 .   ? 17.363 -6.824  -14.162 1.00 41.79 ?  518 HOH   A O    1 
HETATM 6683 O  O    A HOH   G 5 .   ? 14.846 8.647   4.896   0.60 32.97 ?  519 HOH   A O    1 
HETATM 6684 O  O    . HOH   G 5 .   ? 24.088 9.041   -7.212  1.00 36.50 ?  520 HOH   A O    1 
HETATM 6685 O  O    B HOH   G 5 .   ? 7.911  7.053   2.490   0.40 24.11 ?  521 HOH   A O    1 
HETATM 6686 O  O    . HOH   G 5 .   ? 15.859 -12.214 27.370  1.00 45.82 ?  522 HOH   A O    1 
HETATM 6687 O  O    . HOH   G 5 .   ? 16.395 -21.133 18.777  1.00 38.66 ?  523 HOH   A O    1 
HETATM 6688 O  O    . HOH   G 5 .   ? 14.717 -22.808 19.820  1.00 35.69 ?  524 HOH   A O    1 
HETATM 6689 O  O    . HOH   H 5 .   ? 29.832 -22.432 5.479   1.00 20.35 ?  201 HOH   B O    1 
HETATM 6690 O  O    . HOH   H 5 .   ? 52.880 -13.456 -20.320 1.00 34.71 ?  202 HOH   B O    1 
HETATM 6691 O  O    . HOH   H 5 .   ? 41.767 -35.955 -17.226 1.00 30.97 ?  203 HOH   B O    1 
HETATM 6692 O  O    . HOH   H 5 .   ? 27.837 -41.751 -15.149 1.00 35.93 ?  204 HOH   B O    1 
HETATM 6693 O  O    . HOH   H 5 .   ? 27.736 -29.207 -1.853  1.00 35.69 ?  205 HOH   B O    1 
HETATM 6694 O  O    . HOH   H 5 .   ? 48.123 -6.904  15.558  1.00 34.71 ?  206 HOH   B O    1 
HETATM 6695 O  O    . HOH   H 5 .   ? 37.968 -39.464 -0.140  1.00 39.70 ?  207 HOH   B O    1 
HETATM 6696 O  O    . HOH   H 5 .   ? 59.169 -18.650 6.871   1.00 38.28 ?  208 HOH   B O    1 
HETATM 6697 O  O    . HOH   H 5 .   ? 41.383 -7.780  5.460   1.00 38.89 ?  209 HOH   B O    1 
HETATM 6698 O  O    . HOH   H 5 .   ? 47.407 -7.388  -3.904  1.00 40.60 ?  210 HOH   B O    1 
HETATM 6699 O  O    . HOH   H 5 .   ? 54.494 -9.388  -8.707  1.00 19.43 ?  211 HOH   B O    1 
HETATM 6700 O  O    . HOH   H 5 .   ? 50.215 -3.332  7.194   1.00 36.03 ?  212 HOH   B O    1 
HETATM 6701 O  O    . HOH   H 5 .   ? 57.728 -24.501 5.069   1.00 36.20 ?  213 HOH   B O    1 
HETATM 6702 O  O    . HOH   H 5 .   ? 49.472 -22.705 -19.740 1.00 51.19 ?  214 HOH   B O    1 
HETATM 6703 O  O    . HOH   H 5 .   ? 58.211 -12.988 8.394   1.00 31.01 ?  215 HOH   B O    1 
HETATM 6704 O  O    . HOH   H 5 .   ? 56.363 -19.743 7.227   1.00 31.79 ?  216 HOH   B O    1 
HETATM 6705 O  O    . HOH   H 5 .   ? 29.920 -26.322 4.006   1.00 28.71 ?  217 HOH   B O    1 
HETATM 6706 O  O    . HOH   H 5 .   ? 30.213 -41.019 -8.115  1.00 16.87 ?  218 HOH   B O    1 
HETATM 6707 O  O    . HOH   H 5 .   ? 57.180 -26.886 -7.606  1.00 41.01 ?  219 HOH   B O    1 
HETATM 6708 O  O    . HOH   H 5 .   ? 34.579 -36.394 -7.201  1.00 18.09 ?  220 HOH   B O    1 
HETATM 6709 O  O    . HOH   H 5 .   ? 35.975 -43.291 -8.543  1.00 36.33 ?  221 HOH   B O    1 
HETATM 6710 O  O    . HOH   H 5 .   ? 50.744 -6.091  0.195   1.00 25.59 ?  222 HOH   B O    1 
HETATM 6711 O  O    . HOH   H 5 .   ? 48.593 -36.500 -15.482 1.00 44.80 ?  223 HOH   B O    1 
HETATM 6712 O  O    . HOH   H 5 .   ? 56.682 -30.793 -7.770  1.00 30.88 ?  224 HOH   B O    1 
HETATM 6713 O  O    . HOH   H 5 .   ? 41.505 -39.178 -14.916 1.00 21.82 ?  225 HOH   B O    1 
HETATM 6714 O  O    . HOH   H 5 .   ? 44.452 -7.200  2.097   1.00 33.76 ?  226 HOH   B O    1 
HETATM 6715 O  O    . HOH   H 5 .   ? 57.388 -16.257 -12.205 1.00 18.61 ?  227 HOH   B O    1 
HETATM 6716 O  O    . HOH   H 5 .   ? 30.888 -28.785 4.296   1.00 26.30 ?  228 HOH   B O    1 
HETATM 6717 O  O    . HOH   H 5 .   ? 55.362 -16.483 -14.296 1.00 33.82 ?  229 HOH   B O    1 
HETATM 6718 O  O    . HOH   H 5 .   ? 37.086 -19.817 -18.061 1.00 40.48 ?  230 HOH   B O    1 
HETATM 6719 O  O    . HOH   H 5 .   ? 29.789 -34.188 -0.441  1.00 36.18 ?  231 HOH   B O    1 
HETATM 6720 O  O    . HOH   H 5 .   ? 40.607 -16.054 14.103  1.00 23.57 ?  232 HOH   B O    1 
HETATM 6721 O  O    . HOH   H 5 .   ? 39.313 -10.894 6.119   1.00 24.90 ?  233 HOH   B O    1 
HETATM 6722 O  O    . HOH   H 5 .   ? 41.370 -9.632  13.065  1.00 21.60 ?  234 HOH   B O    1 
HETATM 6723 O  O    . HOH   H 5 .   ? 45.190 -34.967 6.828   1.00 40.53 ?  235 HOH   B O    1 
HETATM 6724 O  O    . HOH   H 5 .   ? 35.114 -8.013  -2.996  1.00 18.22 ?  236 HOH   B O    1 
HETATM 6725 O  O    . HOH   H 5 .   ? 43.169 -32.385 -17.044 1.00 24.38 ?  237 HOH   B O    1 
HETATM 6726 O  O    . HOH   H 5 .   ? 28.420 -19.705 -13.103 1.00 24.18 ?  238 HOH   B O    1 
HETATM 6727 O  O    . HOH   H 5 .   ? 32.828 -43.811 -11.317 1.00 20.65 ?  239 HOH   B O    1 
HETATM 6728 O  O    . HOH   H 5 .   ? 51.673 -6.498  4.386   1.00 19.46 ?  240 HOH   B O    1 
HETATM 6729 O  O    . HOH   H 5 .   ? 46.378 -1.587  13.276  1.00 27.51 ?  241 HOH   B O    1 
HETATM 6730 O  O    . HOH   H 5 .   ? 50.746 -12.974 -0.460  1.00 11.76 ?  242 HOH   B O    1 
HETATM 6731 O  O    . HOH   H 5 .   ? 42.644 -22.873 3.854   1.00 11.93 ?  243 HOH   B O    1 
HETATM 6732 O  O    . HOH   H 5 .   ? 43.076 -43.235 -8.239  1.00 29.77 ?  244 HOH   B O    1 
HETATM 6733 O  O    . HOH   H 5 .   ? 25.421 -25.963 -1.377  1.00 32.36 ?  245 HOH   B O    1 
HETATM 6734 O  O    . HOH   H 5 .   ? 42.582 -25.377 2.656   1.00 15.21 ?  246 HOH   B O    1 
HETATM 6735 O  O    . HOH   H 5 .   ? 44.952 -43.547 -10.521 1.00 27.58 ?  247 HOH   B O    1 
HETATM 6736 O  O    . HOH   H 5 .   ? 44.541 -27.788 -0.693  1.00 22.12 ?  248 HOH   B O    1 
HETATM 6737 O  O    . HOH   H 5 .   ? 34.220 -18.522 11.406  1.00 24.19 ?  249 HOH   B O    1 
HETATM 6738 O  O    . HOH   H 5 .   ? 57.632 -24.386 -3.801  1.00 21.59 ?  250 HOH   B O    1 
HETATM 6739 O  O    . HOH   H 5 .   ? 34.913 -24.635 13.878  1.00 31.70 ?  251 HOH   B O    1 
HETATM 6740 O  O    . HOH   H 5 .   ? 39.519 -11.121 0.327   1.00 16.73 ?  252 HOH   B O    1 
HETATM 6741 O  O    . HOH   H 5 .   ? 27.137 -31.845 -9.935  1.00 21.42 ?  253 HOH   B O    1 
HETATM 6742 O  O    . HOH   H 5 .   ? 29.722 -25.215 -10.771 1.00 16.85 ?  254 HOH   B O    1 
HETATM 6743 O  O    . HOH   H 5 .   ? 58.181 -10.635 -4.058  1.00 19.90 ?  255 HOH   B O    1 
HETATM 6744 O  O    . HOH   H 5 .   ? 41.880 -23.529 9.308   1.00 17.82 ?  256 HOH   B O    1 
HETATM 6745 O  O    . HOH   H 5 .   ? 31.840 -17.975 -14.497 1.00 31.13 ?  257 HOH   B O    1 
HETATM 6746 O  O    . HOH   H 5 .   ? 40.353 -12.747 -11.519 1.00 15.44 ?  258 HOH   B O    1 
HETATM 6747 O  O    . HOH   H 5 .   ? 28.486 -30.814 -14.757 1.00 30.33 ?  259 HOH   B O    1 
HETATM 6748 O  O    . HOH   H 5 .   ? 50.991 -39.962 -8.254  1.00 36.54 ?  260 HOH   B O    1 
HETATM 6749 O  O    . HOH   H 5 .   ? 30.858 -15.734 2.662   1.00 13.33 ?  261 HOH   B O    1 
HETATM 6750 O  O    . HOH   H 5 .   ? 38.466 -11.063 -2.228  1.00 18.84 ?  262 HOH   B O    1 
HETATM 6751 O  O    . HOH   H 5 .   ? 38.927 -11.983 12.391  1.00 34.30 ?  263 HOH   B O    1 
HETATM 6752 O  O    . HOH   H 5 .   ? 49.743 -0.519  10.240  1.00 31.46 ?  264 HOH   B O    1 
HETATM 6753 O  O    . HOH   H 5 .   ? 48.025 -22.795 5.836   1.00 17.35 ?  265 HOH   B O    1 
HETATM 6754 O  O    . HOH   H 5 .   ? 51.510 -13.810 10.989  1.00 28.78 ?  266 HOH   B O    1 
HETATM 6755 O  O    . HOH   H 5 .   ? 49.323 -28.711 -6.898  1.00 15.36 ?  267 HOH   B O    1 
HETATM 6756 O  O    . HOH   H 5 .   ? 47.984 -24.498 -17.783 1.00 31.30 ?  268 HOH   B O    1 
HETATM 6757 O  O    . HOH   H 5 .   ? 57.481 -9.215  1.410   1.00 19.01 ?  269 HOH   B O    1 
HETATM 6758 O  O    . HOH   H 5 .   ? 56.946 -8.642  8.422   1.00 19.34 ?  270 HOH   B O    1 
HETATM 6759 O  O    . HOH   H 5 .   ? 33.502 -17.000 8.060   1.00 19.12 ?  271 HOH   B O    1 
HETATM 6760 O  O    . HOH   H 5 .   ? 42.343 -9.904  9.370   1.00 20.57 ?  272 HOH   B O    1 
HETATM 6761 O  O    . HOH   H 5 .   ? 42.386 -34.700 3.758   1.00 25.96 ?  273 HOH   B O    1 
HETATM 6762 O  O    . HOH   H 5 .   ? 46.631 -31.259 -4.806  1.00 20.01 ?  274 HOH   B O    1 
HETATM 6763 O  O    . HOH   H 5 .   ? 43.380 -15.803 -12.171 1.00 14.27 ?  275 HOH   B O    1 
HETATM 6764 O  O    . HOH   H 5 .   ? 46.879 -29.593 9.821   1.00 31.55 ?  276 HOH   B O    1 
HETATM 6765 O  O    . HOH   H 5 .   ? 56.195 -23.518 -14.740 1.00 27.16 ?  277 HOH   B O    1 
HETATM 6766 O  O    . HOH   H 5 .   ? 34.482 -12.775 2.643   1.00 25.06 ?  278 HOH   B O    1 
HETATM 6767 O  O    . HOH   H 5 .   ? 28.256 -34.371 -9.405  1.00 19.61 ?  279 HOH   B O    1 
HETATM 6768 O  O    . HOH   H 5 .   ? 34.948 -33.345 -19.206 1.00 34.85 ?  280 HOH   B O    1 
HETATM 6769 O  O    . HOH   H 5 .   ? 57.203 -12.091 12.321  1.00 35.50 ?  281 HOH   B O    1 
HETATM 6770 O  O    . HOH   H 5 .   ? 27.600 -26.709 -15.638 1.00 31.58 ?  282 HOH   B O    1 
HETATM 6771 O  O    . HOH   H 5 .   ? 27.962 -22.888 -7.993  1.00 17.55 ?  283 HOH   B O    1 
HETATM 6772 O  O    . HOH   H 5 .   ? 30.546 -42.268 -10.579 1.00 29.68 ?  284 HOH   B O    1 
HETATM 6773 O  O    . HOH   H 5 .   ? 48.416 -25.066 3.120   1.00 13.46 ?  285 HOH   B O    1 
HETATM 6774 O  O    . HOH   H 5 .   ? 48.719 -20.033 5.923   1.00 13.79 ?  286 HOH   B O    1 
HETATM 6775 O  O    . HOH   H 5 .   ? 41.165 -5.500  11.536  1.00 47.86 ?  287 HOH   B O    1 
HETATM 6776 O  O    . HOH   H 5 .   ? 36.842 -12.768 -1.523  1.00 26.67 ?  288 HOH   B O    1 
HETATM 6777 O  O    . HOH   H 5 .   ? 51.240 -37.605 -9.629  1.00 26.05 ?  289 HOH   B O    1 
HETATM 6778 O  O    . HOH   H 5 .   ? 47.100 -33.973 -4.627  1.00 17.68 ?  290 HOH   B O    1 
HETATM 6779 O  O    . HOH   H 5 .   ? 33.517 -15.315 -13.949 1.00 21.06 ?  291 HOH   B O    1 
HETATM 6780 O  O    . HOH   H 5 .   ? 42.850 -20.235 -20.713 1.00 37.77 ?  292 HOH   B O    1 
HETATM 6781 O  O    . HOH   H 5 .   ? 37.526 -18.181 13.101  1.00 30.58 ?  293 HOH   B O    1 
HETATM 6782 O  O    . HOH   H 5 .   ? 44.638 -27.473 2.006   1.00 15.54 ?  294 HOH   B O    1 
HETATM 6783 O  O    . HOH   H 5 .   ? 45.344 -33.400 -15.945 1.00 24.11 ?  295 HOH   B O    1 
HETATM 6784 O  O    . HOH   H 5 .   ? 42.317 -9.931  -14.909 1.00 37.75 ?  296 HOH   B O    1 
HETATM 6785 O  O    . HOH   H 5 .   ? 52.611 -35.665 -8.625  1.00 28.47 ?  297 HOH   B O    1 
HETATM 6786 O  O    . HOH   H 5 .   ? 45.893 -40.429 -3.637  1.00 29.28 ?  298 HOH   B O    1 
HETATM 6787 O  O    . HOH   H 5 .   ? 35.077 -33.589 4.524   1.00 29.22 ?  299 HOH   B O    1 
HETATM 6788 O  O    . HOH   H 5 .   ? 42.773 -12.220 -18.495 1.00 27.90 ?  300 HOH   B O    1 
HETATM 6789 O  O    . HOH   H 5 .   ? 52.515 -10.390 13.052  1.00 21.92 ?  301 HOH   B O    1 
HETATM 6790 O  O    . HOH   H 5 .   ? 59.787 -15.295 8.212   1.00 31.54 ?  302 HOH   B O    1 
HETATM 6791 O  O    . HOH   H 5 .   ? 53.474 -30.202 4.500   1.00 18.81 ?  303 HOH   B O    1 
HETATM 6792 O  O    . HOH   H 5 .   ? 57.674 -22.131 3.121   1.00 28.47 ?  304 HOH   B O    1 
HETATM 6793 O  O    . HOH   H 5 .   ? 25.950 -21.478 -3.512  1.00 16.64 ?  305 HOH   B O    1 
HETATM 6794 O  O    . HOH   H 5 .   ? 62.675 -13.551 4.791   1.00 27.91 ?  306 HOH   B O    1 
HETATM 6795 O  O    . HOH   H 5 .   ? 49.944 -24.665 5.834   1.00 34.28 ?  307 HOH   B O    1 
HETATM 6796 O  O    . HOH   H 5 .   ? 37.329 -35.637 7.266   1.00 34.42 ?  308 HOH   B O    1 
HETATM 6797 O  O    . HOH   H 5 .   ? 32.820 -34.622 -5.874  1.00 17.26 ?  309 HOH   B O    1 
HETATM 6798 O  O    . HOH   H 5 .   ? 40.266 -10.834 -9.536  1.00 17.22 ?  310 HOH   B O    1 
HETATM 6799 O  O    . HOH   H 5 .   ? 53.038 -16.026 -12.735 1.00 27.42 ?  311 HOH   B O    1 
HETATM 6800 O  O    . HOH   H 5 .   ? 52.561 -29.231 -13.016 1.00 23.92 ?  312 HOH   B O    1 
HETATM 6801 O  O    . HOH   H 5 .   ? 51.366 -32.892 -10.719 1.00 39.01 ?  313 HOH   B O    1 
HETATM 6802 O  O    . HOH   H 5 .   ? 44.052 -29.364 -4.636  1.00 23.15 ?  314 HOH   B O    1 
HETATM 6803 O  O    . HOH   H 5 .   ? 37.859 -10.253 -10.757 1.00 17.27 ?  315 HOH   B O    1 
HETATM 6804 O  O    . HOH   H 5 .   ? 41.225 -24.480 15.778  1.00 45.52 ?  316 HOH   B O    1 
HETATM 6805 O  O    . HOH   H 5 .   ? 41.742 -8.085  1.396   1.00 23.77 ?  317 HOH   B O    1 
HETATM 6806 O  O    . HOH   H 5 .   ? 53.683 -12.585 -22.204 1.00 36.30 ?  318 HOH   B O    1 
HETATM 6807 O  O    . HOH   H 5 .   ? 51.747 -5.939  -7.887  1.00 45.66 ?  319 HOH   B O    1 
HETATM 6808 O  O    . HOH   H 5 .   ? 43.214 -21.440 10.686  1.00 16.13 ?  320 HOH   B O    1 
HETATM 6809 O  O    . HOH   H 5 .   ? 37.110 -30.585 -21.005 1.00 30.71 ?  321 HOH   B O    1 
HETATM 6810 O  O    . HOH   H 5 .   ? 38.343 -12.734 7.940   1.00 18.48 ?  322 HOH   B O    1 
HETATM 6811 O  O    . HOH   H 5 .   ? 26.336 -21.035 -6.250  1.00 16.34 ?  323 HOH   B O    1 
HETATM 6812 O  O    . HOH   H 5 .   ? 48.114 -32.672 -16.638 1.00 43.35 ?  324 HOH   B O    1 
HETATM 6813 O  O    . HOH   H 5 .   ? 43.515 -15.367 18.166  1.00 30.60 ?  325 HOH   B O    1 
HETATM 6814 O  O    . HOH   H 5 .   ? 62.867 -20.136 -0.738  1.00 38.32 ?  326 HOH   B O    1 
HETATM 6815 O  O    . HOH   H 5 .   ? 44.618 -24.629 9.576   1.00 20.76 ?  327 HOH   B O    1 
HETATM 6816 O  O    . HOH   H 5 .   ? 38.361 -9.349  -13.251 1.00 26.89 ?  328 HOH   B O    1 
HETATM 6817 O  O    . HOH   H 5 .   ? 27.895 -14.790 -9.434  1.00 34.21 ?  329 HOH   B O    1 
HETATM 6818 O  O    . HOH   H 5 .   ? 43.138 -34.603 0.085   1.00 21.03 ?  330 HOH   B O    1 
HETATM 6819 O  O    . HOH   H 5 .   ? 36.718 -12.412 4.296   1.00 17.51 ?  331 HOH   B O    1 
HETATM 6820 O  O    . HOH   H 5 .   ? 33.660 -31.194 11.056  1.00 33.95 ?  332 HOH   B O    1 
HETATM 6821 O  O    . HOH   H 5 .   ? 59.962 -17.209 -10.549 1.00 34.62 ?  333 HOH   B O    1 
HETATM 6822 O  O    . HOH   H 5 .   ? 47.178 -24.492 8.182   1.00 25.86 ?  334 HOH   B O    1 
HETATM 6823 O  O    . HOH   H 5 .   ? 39.541 -23.485 -20.296 1.00 35.25 ?  335 HOH   B O    1 
HETATM 6824 O  O    . HOH   H 5 .   ? 44.139 -1.688  7.656   1.00 45.77 ?  336 HOH   B O    1 
HETATM 6825 O  O    . HOH   H 5 .   ? 47.481 -27.450 2.014   1.00 14.84 ?  337 HOH   B O    1 
HETATM 6826 O  O    . HOH   H 5 .   ? 48.603 -11.961 -13.993 1.00 27.27 ?  338 HOH   B O    1 
HETATM 6827 O  O    . HOH   H 5 .   ? 42.835 -43.513 -14.377 1.00 43.61 ?  339 HOH   B O    1 
HETATM 6828 O  O    . HOH   H 5 .   ? 46.843 -19.868 12.267  1.00 31.87 ?  340 HOH   B O    1 
HETATM 6829 O  O    . HOH   H 5 .   ? 37.023 -15.132 -16.517 1.00 38.27 ?  341 HOH   B O    1 
HETATM 6830 O  O    . HOH   H 5 .   ? 45.711 -36.258 -16.076 1.00 33.96 ?  342 HOH   B O    1 
HETATM 6831 O  O    . HOH   H 5 .   ? 37.065 -45.147 -9.774  1.00 36.96 ?  343 HOH   B O    1 
HETATM 6832 O  O    . HOH   H 5 .   ? 38.409 -12.282 -16.241 1.00 45.10 ?  344 HOH   B O    1 
HETATM 6833 O  O    . HOH   H 5 .   ? 28.890 -42.948 -12.284 1.00 39.02 ?  345 HOH   B O    1 
HETATM 6834 O  O    . HOH   H 5 .   ? 32.996 -14.680 1.037   1.00 18.98 ?  346 HOH   B O    1 
HETATM 6835 O  O    . HOH   H 5 .   ? 39.794 -44.315 -11.197 1.00 40.03 ?  347 HOH   B O    1 
HETATM 6836 O  O    . HOH   H 5 .   ? 38.552 -22.330 15.033  1.00 39.92 ?  348 HOH   B O    1 
HETATM 6837 O  O    . HOH   H 5 .   ? 40.403 -43.486 -9.139  1.00 26.19 ?  349 HOH   B O    1 
HETATM 6838 O  O    . HOH   H 5 .   ? 55.633 -8.264  10.816  1.00 24.68 ?  350 HOH   B O    1 
HETATM 6839 O  O    . HOH   H 5 .   ? 34.590 -10.329 7.588   1.00 23.06 ?  351 HOH   B O    1 
HETATM 6840 O  O    . HOH   H 5 .   ? 27.811 -26.611 -0.568  1.00 30.09 ?  352 HOH   B O    1 
HETATM 6841 O  O    . HOH   H 5 .   ? 33.806 -9.224  -8.836  1.00 33.51 ?  353 HOH   B O    1 
HETATM 6842 O  O    . HOH   H 5 .   ? 62.609 -20.149 -4.813  1.00 47.85 ?  354 HOH   B O    1 
HETATM 6843 O  O    . HOH   H 5 .   ? 23.214 -23.706 6.799   1.00 34.33 ?  355 HOH   B O    1 
HETATM 6844 O  O    . HOH   H 5 .   ? 44.143 -37.335 -17.805 1.00 34.21 ?  356 HOH   B O    1 
HETATM 6845 O  O    . HOH   H 5 .   ? 56.621 -7.298  3.072   1.00 27.81 ?  357 HOH   B O    1 
HETATM 6846 O  O    . HOH   H 5 .   ? 34.068 -7.868  11.430  1.00 39.08 ?  358 HOH   B O    1 
HETATM 6847 O  O    . HOH   H 5 .   ? 36.100 -8.533  -9.718  1.00 33.43 ?  359 HOH   B O    1 
HETATM 6848 O  O    . HOH   H 5 .   ? 43.193 -12.711 -21.177 1.00 40.56 ?  360 HOH   B O    1 
HETATM 6849 O  O    . HOH   H 5 .   ? 61.477 -19.917 1.642   1.00 35.87 ?  361 HOH   B O    1 
HETATM 6850 O  O    . HOH   H 5 .   ? 56.929 -21.559 -16.445 1.00 40.76 ?  362 HOH   B O    1 
HETATM 6851 O  O    . HOH   H 5 .   ? 40.243 -8.833  9.911   1.00 37.25 ?  363 HOH   B O    1 
HETATM 6852 O  O    . HOH   H 5 .   ? 27.174 -25.943 -11.395 1.00 33.66 ?  364 HOH   B O    1 
HETATM 6853 O  O    . HOH   H 5 .   ? 54.160 -5.688  3.011   1.00 35.10 ?  365 HOH   B O    1 
HETATM 6854 O  O    . HOH   H 5 .   ? 32.579 -23.599 14.068  1.00 38.99 ?  366 HOH   B O    1 
HETATM 6855 O  O    . HOH   H 5 .   ? 36.220 -8.723  8.987   1.00 37.87 ?  367 HOH   B O    1 
HETATM 6856 O  O    . HOH   H 5 .   ? 40.120 -11.348 -13.944 1.00 33.33 ?  368 HOH   B O    1 
HETATM 6857 O  O    . HOH   H 5 .   ? 59.032 -10.480 9.176   1.00 39.37 ?  369 HOH   B O    1 
HETATM 6858 O  O    . HOH   H 5 .   ? 39.891 -6.943  7.847   1.00 39.68 ?  370 HOH   B O    1 
HETATM 6859 O  O    . HOH   H 5 .   ? 41.861 -10.003 -17.420 1.00 52.51 ?  371 HOH   B O    1 
HETATM 6860 O  O    . HOH   H 5 .   ? 48.462 -26.492 8.779   1.00 39.62 ?  372 HOH   B O    1 
HETATM 6861 O  O    . HOH   H 5 .   ? 52.067 -12.953 13.337  1.00 29.37 ?  373 HOH   B O    1 
HETATM 6862 O  O    . HOH   H 5 .   ? 56.054 -7.779  -0.569  1.00 34.86 ?  374 HOH   B O    1 
HETATM 6863 O  O    . HOH   H 5 .   ? 63.046 -12.427 6.970   1.00 36.70 ?  375 HOH   B O    1 
HETATM 6864 O  O    . HOH   H 5 .   ? 36.523 -22.866 13.281  1.00 29.03 ?  376 HOH   B O    1 
HETATM 6865 O  O    . HOH   H 5 .   ? 41.782 -6.749  -4.843  1.00 47.22 ?  377 HOH   B O    1 
HETATM 6866 O  O    . HOH   H 5 .   ? 44.081 -5.586  -3.529  1.00 40.44 ?  378 HOH   B O    1 
HETATM 6867 O  O    . HOH   H 5 .   ? 37.971 -10.547 10.067  1.00 28.76 ?  379 HOH   B O    1 
HETATM 6868 O  O    . HOH   H 5 .   ? 42.647 -17.058 -23.175 1.00 42.42 ?  380 HOH   B O    1 
HETATM 6869 O  O    . HOH   H 5 .   ? 40.148 -7.589  3.183   1.00 37.18 ?  381 HOH   B O    1 
HETATM 6870 O  O    . HOH   H 5 .   ? 52.853 -29.910 7.212   1.00 23.02 ?  382 HOH   B O    1 
HETATM 6871 O  O    . HOH   H 5 .   ? 60.495 -22.259 2.860   1.00 51.19 ?  383 HOH   B O    1 
HETATM 6872 O  O    . HOH   H 5 .   ? 39.664 -13.973 15.731  1.00 50.23 ?  384 HOH   B O    1 
HETATM 6873 O  O    . HOH   H 5 .   ? 41.048 -9.774  15.840  1.00 44.58 ?  385 HOH   B O    1 
HETATM 6874 O  O    . HOH   H 5 .   ? 46.783 -5.404  2.946   1.00 39.73 ?  386 HOH   B O    1 
HETATM 6875 O  O    . HOH   H 5 .   ? 35.438 -33.719 7.320   1.00 41.27 ?  387 HOH   B O    1 
HETATM 6876 O  O    . HOH   H 5 .   ? 23.926 -20.878 -7.676  1.00 28.13 ?  388 HOH   B O    1 
HETATM 6877 O  O    . HOH   H 5 .   ? 35.354 -20.353 13.357  1.00 31.03 ?  389 HOH   B O    1 
HETATM 6878 O  O    . HOH   H 5 .   ? 40.731 -6.606  -0.836  1.00 25.11 ?  390 HOH   B O    1 
HETATM 6879 O  O    . HOH   H 5 .   ? 44.042 -31.811 -3.836  1.00 36.86 ?  391 HOH   B O    1 
HETATM 6880 O  O    . HOH   H 5 .   ? 27.915 -27.094 2.252   1.00 30.30 ?  392 HOH   B O    1 
HETATM 6881 O  O    . HOH   H 5 .   ? 26.632 -27.974 -13.500 1.00 37.27 ?  393 HOH   B O    1 
HETATM 6882 O  O    . HOH   H 5 .   ? 34.384 -33.497 9.581   1.00 33.84 ?  394 HOH   B O    1 
HETATM 6883 O  O    . HOH   H 5 .   ? 24.648 -20.719 -10.446 1.00 39.90 ?  395 HOH   B O    1 
HETATM 6884 O  O    . HOH   H 5 .   ? 50.651 -30.829 8.683   1.00 28.75 ?  396 HOH   B O    1 
HETATM 6885 O  O    . HOH   H 5 .   ? 26.842 -30.678 -12.612 1.00 29.75 ?  397 HOH   B O    1 
HETATM 6886 O  O    . HOH   H 5 .   ? 45.749 -20.204 15.255  1.00 52.71 ?  398 HOH   B O    1 
HETATM 6887 O  O    . HOH   H 5 .   ? 57.612 -6.430  -2.323  1.00 33.92 ?  399 HOH   B O    1 
HETATM 6888 O  O    . HOH   H 5 .   ? 40.852 -11.822 -22.276 1.00 40.89 ?  400 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   A VAL   A 3   ? 0.4868 0.5126 0.5991 -0.0284 -0.0328 0.1049  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.5223 0.5400 0.5896 0.0069  -0.0052 0.0511  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.4841 0.5108 0.5897 -0.0309 -0.0318 0.1044  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.5225 0.5400 0.5844 0.0065  -0.0075 0.0500  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.4678 0.5021 0.5498 -0.0405 -0.0375 0.1062  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.5183 0.5353 0.5672 0.0039  -0.0145 0.0458  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.4708 0.5047 0.5639 -0.0398 -0.0397 0.1103  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.5200 0.5385 0.5785 0.0056  -0.0152 0.0477  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.4950 0.5161 0.6097 -0.0261 -0.0262 0.1019  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.5264 0.5444 0.5934 0.0081  -0.0020 0.0507  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.4996 0.5181 0.6111 -0.0235 -0.0247 0.1006  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.5278 0.5445 0.5943 0.0083  0.0006  0.0502  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.4976 0.5177 0.6113 -0.0256 -0.0243 0.1018  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.5277 0.5472 0.5971 0.0087  0.0001  0.0506  3   VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.4454 0.4886 0.4893 -0.0513 -0.0413 0.1009  4   ASN   A N   
32   N  N   B ASN   A 4   ? 0.5111 0.5255 0.5359 -0.0011 -0.0201 0.0382  4   ASN   A N   
33   C  CA  A ASN   A 4   ? 0.4192 0.4734 0.4270 -0.0633 -0.0459 0.0917  4   ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.5023 0.5140 0.5002 -0.0072 -0.0229 0.0299  4   ASN   A CA  
35   C  C   A ASN   A 4   ? 0.3822 0.4558 0.3580 -0.0796 -0.0359 0.0698  4   ASN   A C   
36   C  C   B ASN   A 4   ? 0.4814 0.4983 0.4813 -0.0118 -0.0117 0.0215  4   ASN   A C   
37   O  O   A ASN   A 4   ? 0.3783 0.4555 0.3378 -0.0841 -0.0381 0.0722  4   ASN   A O   
38   O  O   B ASN   A 4   ? 0.4842 0.5017 0.4806 -0.0111 -0.0101 0.0221  4   ASN   A O   
39   C  CB  A ASN   A 4   ? 0.4257 0.4752 0.4250 -0.0599 -0.0592 0.1045  4   ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.5125 0.5162 0.4796 -0.0091 -0.0354 0.0297  4   ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.4278 0.4746 0.4199 -0.0592 -0.0688 0.1164  4   ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.5201 0.5169 0.4606 -0.0109 -0.0476 0.0292  4   ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.4328 0.4763 0.4249 -0.0595 -0.0701 0.1179  4   ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.5217 0.5159 0.4540 -0.0123 -0.0546 0.0294  4   ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.4242 0.4722 0.4216 -0.0572 -0.0743 0.1248  4   ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.5242 0.5183 0.4608 -0.0102 -0.0489 0.0299  4   ASN   A ND2 
59   N  N   A SER   A 5   ? 0.3495 0.4361 0.3214 -0.0917 -0.0208 0.0464  5   SER   A N   
60   N  N   B SER   A 5   ? 0.4551 0.4780 0.4651 -0.0167 -0.0009 0.0118  5   SER   A N   
61   C  CA  A SER   A 5   ? 0.3189 0.4182 0.2924 -0.0996 -0.0024 0.0177  5   SER   A CA  
62   C  CA  B SER   A 5   ? 0.4264 0.4561 0.4432 -0.0234 0.0158  0.0023  5   SER   A CA  
63   C  C   A SER   A 5   ? 0.2918 0.3916 0.2631 -0.0973 0.0132  0.0003  5   SER   A C   
64   C  C   B SER   A 5   ? 0.3901 0.4248 0.4076 -0.0312 0.0280  -0.0026 5   SER   A C   
65   O  O   A SER   A 5   ? 0.2963 0.3976 0.2535 -0.0874 0.0095  -0.0174 5   SER   A O   
66   O  O   B SER   A 5   ? 0.3886 0.4249 0.4078 -0.0309 0.0332  -0.0069 5   SER   A O   
67   C  CB  A SER   A 5   ? 0.3207 0.4272 0.3033 -0.1047 -0.0016 0.0059  5   SER   A CB  
68   C  CB  B SER   A 5   ? 0.4314 0.4641 0.4591 -0.0230 0.0217  0.0004  5   SER   A CB  
69   O  OG  A SER   A 5   ? 0.3240 0.4333 0.3150 -0.1064 -0.0010 0.0008  5   SER   A OG  
70   O  OG  B SER   A 5   ? 0.4338 0.4688 0.4658 -0.0228 0.0264  -0.0003 5   SER   A OG  
81   N  N   A PHE   A 6   ? 0.2585 0.3561 0.2347 -0.1032 0.0400  0.0077  6   PHE   A N   
82   N  N   B PHE   A 6   ? 0.3550 0.3921 0.3627 -0.0392 0.0343  0.0009  6   PHE   A N   
83   C  CA  A PHE   A 6   ? 0.2303 0.3186 0.2005 -0.1017 0.0490  0.0210  6   PHE   A CA  
84   C  CA  B PHE   A 6   ? 0.3215 0.3571 0.3163 -0.0463 0.0415  0.0088  6   PHE   A CA  
85   C  C   A PHE   A 6   ? 0.2294 0.3142 0.2126 -0.0998 0.0471  0.0197  6   PHE   A C   
86   C  C   B PHE   A 6   ? 0.3073 0.3466 0.3078 -0.0463 0.0496  0.0049  6   PHE   A C   
87   O  O   A PHE   A 6   ? 0.2315 0.3136 0.2311 -0.1065 0.0425  0.0307  6   PHE   A O   
88   O  O   B PHE   A 6   ? 0.3114 0.3483 0.3192 -0.0483 0.0500  0.0045  6   PHE   A O   
89   C  CB  A PHE   A 6   ? 0.2149 0.2885 0.1942 -0.0893 0.0504  0.0353  6   PHE   A CB  
90   C  CB  B PHE   A 6   ? 0.3055 0.3329 0.2863 -0.0507 0.0360  0.0171  6   PHE   A CB  
91   C  CG  A PHE   A 6   ? 0.2021 0.2645 0.2020 -0.0755 0.0411  0.0345  6   PHE   A CG  
92   C  CG  B PHE   A 6   ? 0.2912 0.3109 0.2608 -0.0533 0.0288  0.0178  6   PHE   A CG  
93   C  CD1 A PHE   A 6   ? 0.1959 0.2548 0.2064 -0.0684 0.0293  0.0323  6   PHE   A CD1 
94   C  CD1 B PHE   A 6   ? 0.2851 0.3018 0.2508 -0.0536 0.0241  0.0215  6   PHE   A CD1 
95   C  CD2 A PHE   A 6   ? 0.2060 0.2569 0.2142 -0.0601 0.0409  0.0298  6   PHE   A CD2 
96   C  CD2 B PHE   A 6   ? 0.2883 0.3019 0.2562 -0.0520 0.0257  0.0161  6   PHE   A CD2 
97   C  CE1 A PHE   A 6   ? 0.1950 0.2503 0.2212 -0.0605 0.0297  0.0340  6   PHE   A CE1 
98   C  CE1 B PHE   A 6   ? 0.2821 0.2961 0.2496 -0.0533 0.0238  0.0227  6   PHE   A CE1 
99   C  CE2 A PHE   A 6   ? 0.2048 0.2509 0.2258 -0.0551 0.0417  0.0315  6   PHE   A CE2 
100  C  CE2 B PHE   A 6   ? 0.2849 0.2955 0.2547 -0.0524 0.0245  0.0174  6   PHE   A CE2 
101  C  CZ  A PHE   A 6   ? 0.2001 0.2477 0.2255 -0.0572 0.0356  0.0329  6   PHE   A CZ  
102  C  CZ  B PHE   A 6   ? 0.2831 0.2938 0.2509 -0.0529 0.0231  0.0200  6   PHE   A CZ  
121  N  N   A SER   A 7   ? 0.2273 0.3087 0.2157 -0.0922 0.0626  0.0186  7   SER   A N   
122  N  N   B SER   A 7   ? 0.2872 0.3333 0.2875 -0.0449 0.0579  0.0032  7   SER   A N   
123  C  CA  A SER   A 7   ? 0.2330 0.3028 0.2278 -0.0783 0.0680  0.0125  7   SER   A CA  
124  C  CA  B SER   A 7   ? 0.2726 0.3203 0.2798 -0.0429 0.0590  0.0025  7   SER   A CA  
125  C  C   A SER   A 7   ? 0.2198 0.2727 0.2100 -0.0750 0.0675  -0.0009 7   SER   A C   
126  C  C   B SER   A 7   ? 0.2513 0.2984 0.2403 -0.0458 0.0628  0.0078  7   SER   A C   
127  O  O   A SER   A 7   ? 0.2283 0.2614 0.1899 -0.0800 0.0763  -0.0040 7   SER   A O   
128  O  O   B SER   A 7   ? 0.2547 0.2968 0.2391 -0.0466 0.0606  0.0089  7   SER   A O   
129  C  CB  A SER   A 7   ? 0.2531 0.3231 0.2402 -0.0635 0.0752  0.0244  7   SER   A CB  
130  C  CB  B SER   A 7   ? 0.2805 0.3261 0.3121 -0.0376 0.0558  0.0002  7   SER   A CB  
131  O  OG  A SER   A 7   ? 0.2697 0.3354 0.2646 -0.0508 0.0689  0.0222  7   SER   A OG  
132  O  OG  B SER   A 7   ? 0.2867 0.3307 0.3393 -0.0337 0.0527  0.0021  7   SER   A OG  
143  N  N   A GLY   A 8   ? 0.2039 0.2520 0.2113 -0.0651 0.0584  -0.0117 8   GLY   A N   
144  N  N   B GLY   A 8   ? 0.2311 0.2793 0.2056 -0.0482 0.0657  0.0082  8   GLY   A N   
145  C  CA  A GLY   A 8   ? 0.1934 0.2310 0.2151 -0.0448 0.0565  -0.0167 8   GLY   A CA  
146  C  CA  B GLY   A 8   ? 0.2134 0.2603 0.1874 -0.0429 0.0599  0.0102  8   GLY   A CA  
147  C  C   A GLY   A 8   ? 0.1791 0.2118 0.2139 -0.0314 0.0472  -0.0141 8   GLY   A C   
148  C  C   B GLY   A 8   ? 0.1918 0.2412 0.1671 -0.0397 0.0578  0.0142  8   GLY   A C   
149  O  O   A GLY   A 8   ? 0.1810 0.2187 0.2287 -0.0169 0.0494  -0.0214 8   GLY   A O   
150  O  O   B GLY   A 8   ? 0.1914 0.2425 0.1676 -0.0312 0.0634  0.0068  8   GLY   A O   
157  N  N   A TYR   A 9   ? 0.1648 0.1864 0.2030 -0.0273 0.0411  -0.0014 9   TYR   A N   
158  N  N   B TYR   A 9   ? 0.1693 0.2188 0.1698 -0.0376 0.0392  0.0302  9   TYR   A N   
159  C  CA  A TYR   A 9   ? 0.1514 0.1676 0.1917 -0.0197 0.0334  -0.0004 9   TYR   A CA  
160  C  CA  B TYR   A 9   ? 0.1550 0.1969 0.1713 -0.0304 0.0308  0.0364  9   TYR   A CA  
161  C  C   A TYR   A 9   ? 0.1476 0.1548 0.1988 -0.0141 0.0246  0.0187  9   TYR   A C   
162  C  C   B TYR   A 9   ? 0.1509 0.1776 0.1674 -0.0257 0.0258  0.0397  9   TYR   A C   
163  O  O   A TYR   A 9   ? 0.1599 0.1773 0.2240 -0.0209 0.0087  0.0227  9   TYR   A O   
164  O  O   B TYR   A 9   ? 0.1569 0.1934 0.1862 -0.0304 0.0099  0.0507  9   TYR   A O   
165  C  CB  A TYR   A 9   ? 0.1474 0.1712 0.1985 -0.0132 0.0307  -0.0101 9   TYR   A CB  
166  C  CB  B TYR   A 9   ? 0.1513 0.1981 0.1968 -0.0254 0.0233  0.0319  9   TYR   A CB  
167  C  CG  A TYR   A 9   ? 0.1472 0.1701 0.2171 -0.0050 0.0400  -0.0093 9   TYR   A CG  
168  C  CG  B TYR   A 9   ? 0.1482 0.1938 0.2072 -0.0198 0.0277  0.0252  9   TYR   A CG  
169  C  CD1 A TYR   A 9   ? 0.1485 0.1678 0.2248 -0.0080 0.0504  -0.0110 9   TYR   A CD1 
170  C  CD1 B TYR   A 9   ? 0.1497 0.1911 0.2202 -0.0206 0.0370  0.0173  9   TYR   A CD1 
171  C  CD2 A TYR   A 9   ? 0.1468 0.1694 0.2343 -0.0002 0.0361  0.0062  9   TYR   A CD2 
172  C  CD2 B TYR   A 9   ? 0.1448 0.1885 0.2034 -0.0142 0.0277  0.0312  9   TYR   A CD2 
173  C  CE1 A TYR   A 9   ? 0.1539 0.1726 0.2445 -0.0044 0.0501  -0.0153 9   TYR   A CE1 
174  C  CE1 B TYR   A 9   ? 0.1494 0.1837 0.2245 -0.0138 0.0423  0.0191  9   TYR   A CE1 
175  C  CE2 A TYR   A 9   ? 0.1476 0.1750 0.2415 -0.0030 0.0403  -0.0052 9   TYR   A CE2 
176  C  CE2 B TYR   A 9   ? 0.1402 0.1854 0.2072 -0.0078 0.0359  0.0332  9   TYR   A CE2 
177  C  CZ  A TYR   A 9   ? 0.1531 0.1770 0.2594 -0.0115 0.0479  -0.0061 9   TYR   A CZ  
178  C  CZ  B TYR   A 9   ? 0.1369 0.1794 0.2256 -0.0085 0.0510  0.0321  9   TYR   A CZ  
179  O  OH  A TYR   A 9   ? 0.1619 0.1836 0.2806 -0.0181 0.0438  0.0009  9   TYR   A OH  
180  O  OH  B TYR   A 9   ? 0.1303 0.1765 0.2399 -0.0103 0.0614  0.0409  9   TYR   A OH  
199  N  N   A LEU   A 10  ? 0.1434 0.1373 0.1863 -0.0110 0.0300  0.0127  10  LEU   A N   
200  N  N   B LEU   A 10  ? 0.1476 0.1565 0.1587 -0.0186 0.0266  0.0300  10  LEU   A N   
201  C  CA  A LEU   A 10  ? 0.1346 0.1334 0.1928 -0.0083 0.0282  0.0298  10  LEU   A CA  
202  C  CA  B LEU   A 10  ? 0.1416 0.1491 0.1704 -0.0147 0.0319  0.0167  10  LEU   A CA  
203  C  C   A LEU   A 10  ? 0.1274 0.1276 0.1926 -0.0071 0.0311  0.0294  10  LEU   A C   
204  C  C   B LEU   A 10  ? 0.1388 0.1386 0.1679 -0.0155 0.0262  0.0184  10  LEU   A C   
205  O  O   A LEU   A 10  ? 0.1348 0.1224 0.1992 -0.0035 0.0448  0.0229  10  LEU   A O   
206  O  O   B LEU   A 10  ? 0.1420 0.1307 0.1713 -0.0151 0.0447  0.0217  10  LEU   A O   
207  C  CB  A LEU   A 10  ? 0.1360 0.1406 0.2177 -0.0020 0.0232  0.0429  10  LEU   A CB  
208  C  CB  B LEU   A 10  ? 0.1459 0.1537 0.1854 -0.0166 0.0208  0.0175  10  LEU   A CB  
209  C  CG  A LEU   A 10  ? 0.1574 0.1505 0.2497 0.0013  0.0048  0.0516  10  LEU   A CG  
210  C  CG  B LEU   A 10  ? 0.1564 0.1712 0.2095 -0.0115 0.0067  0.0125  10  LEU   A CG  
211  C  CD1 A LEU   A 10  ? 0.1755 0.1617 0.2744 -0.0059 0.0121  0.0441  10  LEU   A CD1 
212  C  CD1 B LEU   A 10  ? 0.1686 0.1834 0.2382 -0.0189 0.0085  0.0057  10  LEU   A CD1 
213  C  CD2 A LEU   A 10  ? 0.1700 0.1622 0.2642 0.0082  0.0187  0.0365  10  LEU   A CD2 
214  C  CD2 B LEU   A 10  ? 0.1711 0.1813 0.2306 -0.0014 -0.0087 0.0061  10  LEU   A CD2 
237  N  N   A LYS   A 11  ? 0.1283 0.1295 0.1923 -0.0049 0.0317  0.0287  11  LYS   A N   
238  N  N   B LYS   A 11  ? 0.1435 0.1352 0.1593 -0.0175 0.0145  0.0210  11  LYS   A N   
239  C  CA  A LYS   A 11  ? 0.1274 0.1265 0.1890 -0.0158 0.0286  0.0242  11  LYS   A CA  
240  C  CA  B LYS   A 11  ? 0.1477 0.1320 0.1653 -0.0208 0.0119  0.0259  11  LYS   A CA  
241  C  C   A LYS   A 11  ? 0.1311 0.1344 0.1989 -0.0146 0.0299  0.0099  11  LYS   A C   
242  C  C   B LYS   A 11  ? 0.1368 0.1206 0.1663 -0.0271 0.0130  0.0153  11  LYS   A C   
243  O  O   A LYS   A 11  ? 0.1404 0.1507 0.2359 -0.0366 0.0314  0.0015  11  LYS   A O   
244  O  O   B LYS   A 11  ? 0.1307 0.1143 0.1949 -0.0253 0.0190  -0.0042 11  LYS   A O   
245  C  CB  A LYS   A 11  ? 0.1350 0.1236 0.1888 -0.0154 0.0155  0.0250  11  LYS   A CB  
246  C  CB  B LYS   A 11  ? 0.1622 0.1293 0.1748 -0.0168 0.0076  0.0306  11  LYS   A CB  
247  C  CG  A LYS   A 11  ? 0.1415 0.1283 0.1987 -0.0108 0.0132  0.0254  11  LYS   A CG  
248  C  CG  B LYS   A 11  ? 0.1723 0.1387 0.1825 -0.0130 0.0043  0.0429  11  LYS   A CG  
249  C  CD  A LYS   A 11  ? 0.1479 0.1395 0.1952 -0.0146 0.0077  0.0286  11  LYS   A CD  
250  C  CD  B LYS   A 11  ? 0.1783 0.1497 0.1936 -0.0146 0.0057  0.0512  11  LYS   A CD  
251  C  CE  A LYS   A 11  ? 0.1584 0.1432 0.1717 -0.0050 -0.0006 0.0309  11  LYS   A CE  
252  C  CE  B LYS   A 11  ? 0.1774 0.1537 0.1938 -0.0196 0.0031  0.0559  11  LYS   A CE  
253  N  NZ  A LYS   A 11  ? 0.1554 0.1424 0.1908 0.0054  -0.0033 0.0253  11  LYS   A NZ  
254  N  NZ  B LYS   A 11  ? 0.1730 0.1537 0.1980 -0.0145 0.0017  0.0564  11  LYS   A NZ  
281  N  N   A LEU   A 12  ? 0.1230 0.1307 0.1720 -0.0176 0.0272  0.0154  12  LEU   A N   
282  N  N   B LEU   A 12  ? 0.1294 0.1335 0.1682 -0.0148 0.0065  0.0127  12  LEU   A N   
283  C  CA  A LEU   A 12  ? 0.1364 0.1386 0.1657 -0.0194 0.0127  0.0288  12  LEU   A CA  
284  C  CA  B LEU   A 12  ? 0.1313 0.1486 0.1661 -0.0097 0.0127  0.0118  12  LEU   A CA  
285  C  C   A LEU   A 12  ? 0.1382 0.1300 0.1806 -0.0190 0.0119  0.0235  12  LEU   A C   
286  C  C   B LEU   A 12  ? 0.1312 0.1508 0.1694 -0.0106 0.0182  0.0166  12  LEU   A C   
287  O  O   A LEU   A 12  ? 0.1392 0.1301 0.1879 -0.0109 0.0255  0.0130  12  LEU   A O   
288  O  O   B LEU   A 12  ? 0.1359 0.1487 0.1631 -0.0019 0.0113  0.0162  12  LEU   A O   
289  C  CB  A LEU   A 12  ? 0.1454 0.1383 0.1724 -0.0244 0.0059  0.0273  12  LEU   A CB  
290  C  CB  B LEU   A 12  ? 0.1365 0.1586 0.1734 -0.0029 0.0148  0.0154  12  LEU   A CB  
291  C  CG  A LEU   A 12  ? 0.1559 0.1484 0.1906 -0.0113 0.0161  0.0291  12  LEU   A CG  
292  C  CG  B LEU   A 12  ? 0.1347 0.1615 0.1849 0.0011  0.0231  0.0155  12  LEU   A CG  
293  C  CD1 A LEU   A 12  ? 0.1631 0.1535 0.2047 0.0053  0.0275  0.0413  12  LEU   A CD1 
294  C  CD1 B LEU   A 12  ? 0.1369 0.1691 0.1989 0.0080  0.0388  0.0201  12  LEU   A CD1 
295  C  CD2 A LEU   A 12  ? 0.1561 0.1538 0.2003 -0.0130 0.0187  0.0206  12  LEU   A CD2 
296  C  CD2 B LEU   A 12  ? 0.1302 0.1634 0.1965 0.0007  0.0170  0.0038  12  LEU   A CD2 
319  N  N   A THR   A 13  ? 0.1343 0.1315 0.2047 -0.0183 0.0089  0.0230  13  THR   A N   
320  N  N   B THR   A 13  ? 0.1281 0.1498 0.1776 -0.0120 0.0198  0.0221  13  THR   A N   
321  C  CA  A THR   A 13  ? 0.1333 0.1361 0.2181 -0.0141 0.0142  0.0308  13  THR   A CA  
322  C  CA  B THR   A 13  ? 0.1299 0.1509 0.1883 -0.0131 0.0214  0.0281  13  THR   A CA  
323  C  C   A THR   A 13  ? 0.1339 0.1334 0.2243 -0.0218 0.0140  0.0473  13  THR   A C   
324  C  C   B THR   A 13  ? 0.1397 0.1638 0.1959 -0.0259 0.0172  0.0302  13  THR   A C   
325  O  O   A THR   A 13  ? 0.1375 0.1345 0.2238 -0.0090 0.0094  0.0368  13  THR   A O   
326  O  O   B THR   A 13  ? 0.1414 0.1701 0.1997 -0.0251 0.0096  0.0307  13  THR   A O   
327  C  CB  A THR   A 13  ? 0.1329 0.1429 0.2216 -0.0082 0.0149  0.0400  13  THR   A CB  
328  C  CB  B THR   A 13  ? 0.1243 0.1515 0.1949 -0.0034 0.0190  0.0295  13  THR   A CB  
329  O  OG1 A THR   A 13  ? 0.1370 0.1359 0.2330 -0.0078 0.0006  0.0538  13  THR   A OG1 
330  O  OG1 B THR   A 13  ? 0.1152 0.1550 0.2134 -0.0051 0.0269  0.0296  13  THR   A OG1 
331  C  CG2 A THR   A 13  ? 0.1350 0.1533 0.2256 -0.0051 0.0209  0.0222  13  THR   A CG2 
332  C  CG2 B THR   A 13  ? 0.1237 0.1536 0.1932 0.0062  0.0155  0.0275  13  THR   A CG2 
347  N  N   A ASP   A 14  ? 0.1358 0.1356 0.2356 -0.0242 0.0071  0.0583  14  ASP   A N   
348  N  N   B ASP   A 14  ? 0.1442 0.1669 0.2056 -0.0279 0.0076  0.0260  14  ASP   A N   
349  C  CA  A ASP   A 14  ? 0.1408 0.1456 0.2374 -0.0221 -0.0041 0.0655  14  ASP   A CA  
350  C  CA  B ASP   A 14  ? 0.1535 0.1707 0.2066 -0.0212 0.0021  0.0229  14  ASP   A CA  
351  C  C   A ASP   A 14  ? 0.1398 0.1524 0.2007 -0.0167 -0.0084 0.0619  14  ASP   A C   
352  C  C   B ASP   A 14  ? 0.1412 0.1557 0.1790 -0.0140 0.0082  0.0283  14  ASP   A C   
353  O  O   A ASP   A 14  ? 0.1462 0.1611 0.2038 -0.0268 0.0028  0.0539  14  ASP   A O   
354  O  O   B ASP   A 14  ? 0.1401 0.1619 0.1750 -0.0111 0.0213  0.0256  14  ASP   A O   
355  C  CB  A ASP   A 14  ? 0.1532 0.1543 0.2838 -0.0241 -0.0066 0.0730  14  ASP   A CB  
356  C  CB  B ASP   A 14  ? 0.1779 0.1964 0.2453 -0.0153 -0.0056 0.0179  14  ASP   A CB  
357  C  CG  A ASP   A 14  ? 0.1764 0.1956 0.3485 -0.0216 0.0021  0.0564  14  ASP   A CG  
358  C  CG  B ASP   A 14  ? 0.1974 0.2279 0.2832 -0.0080 -0.0023 0.0158  14  ASP   A CG  
359  O  OD1 A ASP   A 14  ? 0.1782 0.1978 0.3613 -0.0252 0.0008  0.0728  14  ASP   A OD1 
360  O  OD1 B ASP   A 14  ? 0.2123 0.2352 0.2958 -0.0019 -0.0027 0.0302  14  ASP   A OD1 
361  O  OD2 A ASP   A 14  ? 0.1925 0.2169 0.3835 -0.0193 -0.0068 0.0279  14  ASP   A OD2 
362  O  OD2 B ASP   A 14  ? 0.1998 0.2453 0.3160 -0.0066 -0.0066 0.0032  14  ASP   A OD2 
371  N  N   A ASN   A 15  ? 0.1361 0.1476 0.1872 -0.0194 -0.0116 0.0563  15  ASN   A N   
372  N  N   B ASN   A 15  ? 0.1322 0.1378 0.1595 -0.0200 0.0115  0.0349  15  ASN   A N   
373  C  CA  A ASN   A 15  ? 0.1368 0.1503 0.1931 -0.0158 -0.0168 0.0404  15  ASN   A CA  
374  C  CA  B ASN   A 15  ? 0.1284 0.1371 0.1729 -0.0190 0.0123  0.0233  15  ASN   A CA  
375  C  C   A ASN   A 15  ? 0.1303 0.1472 0.1952 -0.0174 -0.0034 0.0381  15  ASN   A C   
376  C  C   B ASN   A 15  ? 0.1276 0.1396 0.1874 -0.0165 0.0196  0.0259  15  ASN   A C   
377  O  O   A ASN   A 15  ? 0.1229 0.1439 0.1834 -0.0128 0.0052  0.0270  15  ASN   A O   
378  O  O   B ASN   A 15  ? 0.1275 0.1399 0.1980 -0.0078 0.0241  0.0170  15  ASN   A O   
379  C  CB  A ASN   A 15  ? 0.1398 0.1543 0.1978 -0.0143 -0.0115 0.0404  15  ASN   A CB  
380  C  CB  B ASN   A 15  ? 0.1202 0.1330 0.1559 -0.0214 0.0183  0.0116  15  ASN   A CB  
381  C  CG  A ASN   A 15  ? 0.1394 0.1634 0.1931 -0.0101 0.0041  0.0318  15  ASN   A CG  
382  C  CG  B ASN   A 15  ? 0.1176 0.1445 0.1628 -0.0143 0.0230  0.0043  15  ASN   A CG  
383  O  OD1 A ASN   A 15  ? 0.1453 0.1611 0.1930 -0.0147 0.0283  0.0283  15  ASN   A OD1 
384  O  OD1 B ASN   A 15  ? 0.1245 0.1503 0.1657 -0.0222 0.0300  -0.0116 15  ASN   A OD1 
385  N  ND2 A ASN   A 15  ? 0.1453 0.1733 0.1887 -0.0155 -0.0006 0.0406  15  ASN   A ND2 
386  N  ND2 B ASN   A 15  ? 0.1205 0.1498 0.1636 -0.0090 0.0129  0.0152  15  ASN   A ND2 
399  N  N   A VAL   A 16  ? 0.1331 0.1438 0.2140 -0.0224 -0.0031 0.0487  16  VAL   A N   
400  N  N   B VAL   A 16  ? 0.1266 0.1416 0.1938 -0.0136 0.0081  0.0343  16  VAL   A N   
401  C  CA  A VAL   A 16  ? 0.1319 0.1456 0.2202 -0.0172 -0.0003 0.0503  16  VAL   A CA  
402  C  CA  B VAL   A 16  ? 0.1232 0.1405 0.2015 -0.0176 0.0057  0.0358  16  VAL   A CA  
403  C  C   A VAL   A 16  ? 0.1297 0.1480 0.2215 -0.0163 0.0035  0.0546  16  VAL   A C   
404  C  C   B VAL   A 16  ? 0.1178 0.1393 0.2035 -0.0173 -0.0025 0.0472  16  VAL   A C   
405  O  O   A VAL   A 16  ? 0.1228 0.1503 0.2282 -0.0112 0.0055  0.0535  16  VAL   A O   
406  O  O   B VAL   A 16  ? 0.1084 0.1311 0.1974 -0.0171 -0.0085 0.0566  16  VAL   A O   
407  C  CB  A VAL   A 16  ? 0.1359 0.1535 0.2099 -0.0031 0.0044  0.0539  16  VAL   A CB  
408  C  CB  B VAL   A 16  ? 0.1340 0.1508 0.2020 -0.0129 0.0206  0.0378  16  VAL   A CB  
409  C  CG1 A VAL   A 16  ? 0.1479 0.1608 0.2089 0.0029  0.0095  0.0461  16  VAL   A CG1 
410  C  CG1 B VAL   A 16  ? 0.1444 0.1587 0.1977 -0.0089 0.0212  0.0330  16  VAL   A CG1 
411  C  CG2 A VAL   A 16  ? 0.1443 0.1661 0.2276 0.0025  0.0156  0.0475  16  VAL   A CG2 
412  C  CG2 B VAL   A 16  ? 0.1369 0.1586 0.2099 -0.0117 0.0325  0.0323  16  VAL   A CG2 
431  N  N   . TYR   A 17  ? 0.1248 0.1422 0.2184 -0.0143 0.0111  0.0510  17  TYR   A N   
432  C  CA  . TYR   A 17  ? 0.1302 0.1476 0.2062 -0.0180 0.0120  0.0533  17  TYR   A CA  
433  C  C   . TYR   A 17  ? 0.1309 0.1438 0.2309 -0.0163 0.0123  0.0523  17  TYR   A C   
434  O  O   . TYR   A 17  ? 0.1262 0.1500 0.2449 -0.0161 0.0172  0.0619  17  TYR   A O   
435  C  CB  . TYR   A 17  ? 0.1503 0.1471 0.2132 -0.0244 0.0047  0.0529  17  TYR   A CB  
436  C  CG  . TYR   A 17  ? 0.1713 0.1539 0.2125 -0.0258 -0.0067 0.0421  17  TYR   A CG  
437  C  CD1 . TYR   A 17  ? 0.1846 0.1615 0.2223 -0.0104 -0.0141 0.0423  17  TYR   A CD1 
438  C  CD2 . TYR   A 17  ? 0.1877 0.1607 0.1996 -0.0397 -0.0052 0.0387  17  TYR   A CD2 
439  C  CE1 . TYR   A 17  ? 0.1989 0.1605 0.2221 -0.0147 -0.0237 0.0467  17  TYR   A CE1 
440  C  CE2 . TYR   A 17  ? 0.2084 0.1596 0.2018 -0.0369 -0.0097 0.0250  17  TYR   A CE2 
441  C  CZ  . TYR   A 17  ? 0.2166 0.1579 0.2106 -0.0305 -0.0237 0.0408  17  TYR   A CZ  
442  O  OH  . TYR   A 17  ? 0.2410 0.1578 0.2232 -0.0327 -0.0269 0.0381  17  TYR   A OH  
453  N  N   . ILE   A 18  ? 0.1333 0.1454 0.2351 -0.0136 0.0169  0.0582  18  ILE   A N   
454  C  CA  . ILE   A 18  ? 0.1381 0.1460 0.2461 -0.0099 0.0237  0.0563  18  ILE   A CA  
455  C  C   . ILE   A 18  ? 0.1350 0.1512 0.2550 -0.0163 0.0336  0.0564  18  ILE   A C   
456  O  O   . ILE   A 18  ? 0.1365 0.1643 0.2638 -0.0186 0.0331  0.0607  18  ILE   A O   
457  C  CB  . ILE   A 18  ? 0.1494 0.1592 0.2353 -0.0038 0.0156  0.0736  18  ILE   A CB  
458  C  CG1 . ILE   A 18  ? 0.1614 0.1721 0.2484 -0.0039 0.0139  0.0791  18  ILE   A CG1 
459  C  CG2 . ILE   A 18  ? 0.1523 0.1712 0.2410 -0.0115 0.0099  0.0707  18  ILE   A CG2 
460  C  CD1 . ILE   A 18  ? 0.1915 0.1918 0.2677 -0.0001 0.0042  0.0830  18  ILE   A CD1 
472  N  N   A LYS   A 19  ? 0.1445 0.1534 0.2622 -0.0063 0.0425  0.0471  19  LYS   A N   
473  N  N   B LYS   A 19  ? 0.1378 0.1484 0.2523 -0.0143 0.0423  0.0572  19  LYS   A N   
474  C  CA  A LYS   A 19  ? 0.1585 0.1675 0.2642 0.0060  0.0404  0.0446  19  LYS   A CA  
475  C  CA  B LYS   A 19  ? 0.1393 0.1537 0.2420 -0.0098 0.0413  0.0608  19  LYS   A CA  
476  C  C   A LYS   A 19  ? 0.1509 0.1662 0.2618 0.0114  0.0327  0.0430  19  LYS   A C   
477  C  C   B LYS   A 19  ? 0.1294 0.1480 0.2499 -0.0113 0.0389  0.0584  19  LYS   A C   
478  O  O   A LYS   A 19  ? 0.1456 0.1689 0.2584 0.0099  0.0258  0.0413  19  LYS   A O   
479  O  O   B LYS   A 19  ? 0.1235 0.1370 0.2519 -0.0123 0.0333  0.0534  19  LYS   A O   
480  C  CB  A LYS   A 19  ? 0.1650 0.1837 0.2658 0.0071  0.0461  0.0396  19  LYS   A CB  
481  C  CB  B LYS   A 19  ? 0.1444 0.1653 0.2255 -0.0050 0.0394  0.0650  19  LYS   A CB  
482  C  CG  A LYS   A 19  ? 0.1851 0.1996 0.2624 0.0110  0.0373  0.0314  19  LYS   A CG  
483  C  CG  B LYS   A 19  ? 0.1555 0.1868 0.2376 0.0048  0.0255  0.0399  19  LYS   A CG  
484  C  CD  A LYS   A 19  ? 0.1991 0.2101 0.2547 0.0172  0.0422  0.0348  19  LYS   A CD  
485  C  CD  B LYS   A 19  ? 0.1692 0.2078 0.2381 0.0086  0.0234  0.0242  19  LYS   A CD  
486  C  CE  A LYS   A 19  ? 0.2078 0.2112 0.2566 0.0152  0.0439  0.0303  19  LYS   A CE  
487  C  CE  B LYS   A 19  ? 0.1775 0.2197 0.2388 0.0076  0.0202  0.0185  19  LYS   A CE  
488  N  NZ  A LYS   A 19  ? 0.2122 0.2152 0.2499 0.0089  0.0555  0.0289  19  LYS   A NZ  
489  N  NZ  B LYS   A 19  ? 0.1844 0.2278 0.2212 0.0117  0.0188  0.0136  19  LYS   A NZ  
516  N  N   A ASN   A 20  ? 0.1566 0.1682 0.2766 0.0098  0.0302  0.0418  20  ASN   A N   
517  N  N   B ASN   A 20  ? 0.1311 0.1550 0.2534 -0.0143 0.0344  0.0623  20  ASN   A N   
518  C  CA  A ASN   A 20  ? 0.1663 0.1785 0.2745 0.0207  0.0308  0.0375  20  ASN   A CA  
519  C  CA  B ASN   A 20  ? 0.1400 0.1735 0.2429 0.0005  0.0332  0.0497  20  ASN   A CA  
520  C  C   A ASN   A 20  ? 0.1812 0.1778 0.2566 0.0187  0.0341  0.0412  20  ASN   A C   
521  C  C   B ASN   A 20  ? 0.1578 0.1798 0.2317 -0.0036 0.0430  0.0412  20  ASN   A C   
522  O  O   A ASN   A 20  ? 0.1987 0.1874 0.2501 0.0065  0.0351  0.0492  20  ASN   A O   
523  O  O   B ASN   A 20  ? 0.1787 0.1933 0.2332 -0.0091 0.0347  0.0350  20  ASN   A O   
524  C  CB  A ASN   A 20  ? 0.1794 0.1883 0.2917 0.0256  0.0319  0.0405  20  ASN   A CB  
525  C  CB  B ASN   A 20  ? 0.1435 0.1864 0.2418 0.0112  0.0263  0.0520  20  ASN   A CB  
526  C  CG  A ASN   A 20  ? 0.1975 0.1933 0.3052 0.0325  0.0367  0.0366  20  ASN   A CG  
527  C  CG  B ASN   A 20  ? 0.1514 0.1940 0.2398 0.0297  0.0186  0.0553  20  ASN   A CG  
528  O  OD1 A ASN   A 20  ? 0.2259 0.2090 0.3246 0.0381  0.0454  0.0336  20  ASN   A OD1 
529  O  OD1 B ASN   A 20  ? 0.1714 0.1972 0.2660 0.0435  0.0378  0.0421  20  ASN   A OD1 
530  N  ND2 A ASN   A 20  ? 0.1947 0.1839 0.3033 0.0326  0.0280  0.0316  20  ASN   A ND2 
531  N  ND2 B ASN   A 20  ? 0.1594 0.1982 0.2451 0.0316  -0.0095 0.0641  20  ASN   A ND2 
544  N  N   A ALA   A 21  ? 0.1858 0.1803 0.2606 0.0160  0.0274  0.0260  21  ALA   A N   
545  N  N   B ALA   A 21  ? 0.1607 0.1775 0.2253 -0.0100 0.0504  0.0338  21  ALA   A N   
546  C  CA  A ALA   A 21  ? 0.1949 0.1822 0.2519 0.0114  0.0248  0.0272  21  ALA   A CA  
547  C  CA  B ALA   A 21  ? 0.1677 0.1739 0.2182 -0.0157 0.0463  0.0384  21  ALA   A CA  
548  C  C   A ALA   A 21  ? 0.1943 0.1832 0.2371 0.0054  0.0343  0.0223  21  ALA   A C   
549  C  C   B ALA   A 21  ? 0.1543 0.1603 0.2110 -0.0151 0.0438  0.0269  21  ALA   A C   
550  O  O   A ALA   A 21  ? 0.1972 0.1971 0.2270 0.0039  0.0352  0.0117  21  ALA   A O   
551  O  O   B ALA   A 21  ? 0.1442 0.1626 0.2158 -0.0131 0.0268  0.0174  21  ALA   A O   
552  C  CB  A ALA   A 21  ? 0.2075 0.1930 0.2755 0.0054  0.0116  0.0324  21  ALA   A CB  
553  C  CB  B ALA   A 21  ? 0.1842 0.1861 0.2214 -0.0222 0.0401  0.0486  21  ALA   A CB  
564  N  N   A ASP   A 22  ? 0.1935 0.1728 0.2433 -0.0029 0.0407  0.0194  22  ASP   A N   
565  N  N   B ASP   A 22  ? 0.1556 0.1525 0.2084 -0.0150 0.0543  0.0236  22  ASP   A N   
566  C  CA  A ASP   A 22  ? 0.1972 0.1696 0.2378 -0.0003 0.0318  0.0163  22  ASP   A CA  
567  C  CA  B ASP   A 22  ? 0.1636 0.1543 0.2026 -0.0102 0.0444  0.0167  22  ASP   A CA  
568  C  C   A ASP   A 22  ? 0.1876 0.1723 0.2113 -0.0076 0.0306  0.0131  22  ASP   A C   
569  C  C   B ASP   A 22  ? 0.1509 0.1583 0.1761 -0.0188 0.0488  0.0095  22  ASP   A C   
570  O  O   A ASP   A 22  ? 0.1927 0.1823 0.2219 -0.0160 0.0414  0.0165  22  ASP   A O   
571  O  O   B ASP   A 22  ? 0.1461 0.1648 0.1767 -0.0232 0.0483  -0.0017 22  ASP   A O   
572  C  CB  A ASP   A 22  ? 0.2181 0.1728 0.2795 0.0049  0.0228  0.0103  22  ASP   A CB  
573  C  CB  B ASP   A 22  ? 0.1828 0.1551 0.2234 0.0012  0.0500  0.0116  22  ASP   A CB  
574  C  CG  A ASP   A 22  ? 0.2347 0.1796 0.3161 -0.0014 0.0122  0.0129  22  ASP   A CG  
575  C  CG  B ASP   A 22  ? 0.1977 0.1541 0.2373 0.0065  0.0505  0.0157  22  ASP   A CG  
576  O  OD1 A ASP   A 22  ? 0.2270 0.1710 0.3362 -0.0190 0.0018  0.0292  22  ASP   A OD1 
577  O  OD1 B ASP   A 22  ? 0.1936 0.1441 0.2159 0.0028  0.0553  0.0221  22  ASP   A OD1 
578  O  OD2 A ASP   A 22  ? 0.2556 0.1929 0.3415 0.0074  0.0131  -0.0028 22  ASP   A OD2 
579  O  OD2 B ASP   A 22  ? 0.2133 0.1654 0.2630 0.0035  0.0552  0.0150  22  ASP   A OD2 
588  N  N   A ILE   A 23  ? 0.1841 0.1705 0.2012 -0.0025 0.0258  0.0127  23  ILE   A N   
589  N  N   B ILE   A 23  ? 0.1486 0.1521 0.1669 -0.0151 0.0416  0.0131  23  ILE   A N   
590  C  CA  A ILE   A 23  ? 0.1784 0.1641 0.1837 -0.0022 0.0262  0.0156  23  ILE   A CA  
591  C  CA  B ILE   A 23  ? 0.1441 0.1512 0.1601 -0.0119 0.0292  0.0178  23  ILE   A CA  
592  C  C   A ILE   A 23  ? 0.1761 0.1723 0.1843 -0.0016 0.0336  0.0142  23  ILE   A C   
593  C  C   B ILE   A 23  ? 0.1514 0.1614 0.1631 -0.0196 0.0364  0.0088  23  ILE   A C   
594  O  O   A ILE   A 23  ? 0.1795 0.1780 0.1960 -0.0011 0.0272  0.0063  23  ILE   A O   
595  O  O   B ILE   A 23  ? 0.1492 0.1612 0.1704 -0.0207 0.0318  0.0032  23  ILE   A O   
596  C  CB  A ILE   A 23  ? 0.1868 0.1577 0.1665 -0.0008 0.0265  0.0157  23  ILE   A CB  
597  C  CB  B ILE   A 23  ? 0.1418 0.1446 0.1516 0.0008  0.0166  0.0241  23  ILE   A CB  
598  C  CG1 A ILE   A 23  ? 0.1910 0.1540 0.1838 0.0016  0.0273  0.0132  23  ILE   A CG1 
599  C  CG1 B ILE   A 23  ? 0.1441 0.1441 0.1524 -0.0021 0.0085  0.0116  23  ILE   A CG1 
600  C  CG2 A ILE   A 23  ? 0.1828 0.1646 0.1656 0.0003  0.0227  0.0206  23  ILE   A CG2 
601  C  CG2 B ILE   A 23  ? 0.1403 0.1404 0.1427 0.0130  0.0131  0.0258  23  ILE   A CG2 
602  C  CD1 A ILE   A 23  ? 0.1914 0.1541 0.1941 0.0009  0.0211  0.0087  23  ILE   A CD1 
603  C  CD1 B ILE   A 23  ? 0.1376 0.1420 0.1541 -0.0018 -0.0051 0.0086  23  ILE   A CD1 
626  N  N   A VAL   A 24  ? 0.1756 0.1798 0.1834 -0.0072 0.0349  0.0087  24  VAL   A N   
627  N  N   B VAL   A 24  ? 0.1636 0.1707 0.1826 -0.0278 0.0293  0.0063  24  VAL   A N   
628  C  CA  A VAL   A 24  ? 0.1927 0.1936 0.2057 -0.0150 0.0331  -0.0015 24  VAL   A CA  
629  C  CA  B VAL   A 24  ? 0.1857 0.1778 0.1918 -0.0316 0.0336  -0.0025 24  VAL   A CA  
630  C  C   A VAL   A 24  ? 0.1966 0.2125 0.2115 -0.0272 0.0321  -0.0055 24  VAL   A C   
631  C  C   B VAL   A 24  ? 0.1938 0.1961 0.2011 -0.0332 0.0388  -0.0141 24  VAL   A C   
632  O  O   A VAL   A 24  ? 0.2027 0.2141 0.2141 -0.0248 0.0382  -0.0057 24  VAL   A O   
633  O  O   B VAL   A 24  ? 0.2013 0.2017 0.2066 -0.0304 0.0401  -0.0109 24  VAL   A O   
634  C  CB  A VAL   A 24  ? 0.2042 0.1930 0.2239 -0.0108 0.0466  0.0003  24  VAL   A CB  
635  C  CB  B VAL   A 24  ? 0.1939 0.1734 0.2043 -0.0336 0.0392  0.0045  24  VAL   A CB  
636  C  CG1 A VAL   A 24  ? 0.2118 0.2005 0.2288 -0.0030 0.0602  -0.0059 24  VAL   A CG1 
637  C  CG1 B VAL   A 24  ? 0.2067 0.1773 0.2281 -0.0277 0.0356  0.0028  24  VAL   A CG1 
638  C  CG2 A VAL   A 24  ? 0.2140 0.1938 0.2339 -0.0078 0.0554  0.0100  24  VAL   A CG2 
639  C  CG2 B VAL   A 24  ? 0.1998 0.1706 0.1986 -0.0366 0.0426  -0.0006 24  VAL   A CG2 
658  N  N   A GLU   A 25  ? 0.2005 0.2374 0.2126 -0.0346 0.0453  -0.0113 25  GLU   A N   
659  N  N   B GLU   A 25  ? 0.1939 0.2116 0.2124 -0.0359 0.0521  -0.0275 25  GLU   A N   
660  C  CA  A GLU   A 25  ? 0.2184 0.2629 0.2233 -0.0323 0.0590  -0.0142 25  GLU   A CA  
661  C  CA  B GLU   A 25  ? 0.2030 0.2316 0.2213 -0.0437 0.0596  -0.0261 25  GLU   A CA  
662  C  C   A GLU   A 25  ? 0.2113 0.2650 0.2011 -0.0419 0.0689  -0.0130 25  GLU   A C   
663  C  C   B GLU   A 25  ? 0.2060 0.2382 0.2135 -0.0454 0.0667  -0.0262 25  GLU   A C   
664  O  O   A GLU   A 25  ? 0.2207 0.2736 0.2245 -0.0442 0.0641  -0.0144 25  GLU   A O   
665  O  O   B GLU   A 25  ? 0.2129 0.2430 0.2120 -0.0459 0.0717  -0.0358 25  GLU   A O   
666  C  CB  A GLU   A 25  ? 0.2430 0.2872 0.2598 -0.0262 0.0574  -0.0176 25  GLU   A CB  
667  C  CB  B GLU   A 25  ? 0.2128 0.2448 0.2431 -0.0463 0.0597  -0.0256 25  GLU   A CB  
668  C  CG  A GLU   A 25  ? 0.2682 0.3084 0.3092 -0.0276 0.0377  -0.0267 25  GLU   A CG  
669  C  CG  B GLU   A 25  ? 0.2335 0.2634 0.2878 -0.0441 0.0492  -0.0246 25  GLU   A CG  
670  C  CD  A GLU   A 25  ? 0.2867 0.3279 0.3501 -0.0292 0.0210  -0.0303 25  GLU   A CD  
671  C  CD  B GLU   A 25  ? 0.2500 0.2797 0.3299 -0.0388 0.0336  -0.0220 25  GLU   A CD  
672  O  OE1 A GLU   A 25  ? 0.2967 0.3381 0.3536 -0.0269 0.0034  -0.0376 25  GLU   A OE1 
673  O  OE1 B GLU   A 25  ? 0.2570 0.2869 0.3556 -0.0377 0.0284  -0.0214 25  GLU   A OE1 
674  O  OE2 A GLU   A 25  ? 0.2912 0.3348 0.3781 -0.0304 0.0214  -0.0336 25  GLU   A OE2 
675  O  OE2 B GLU   A 25  ? 0.2574 0.2866 0.3468 -0.0352 0.0271  -0.0181 25  GLU   A OE2 
688  N  N   A GLU   A 26  ? 0.2018 0.2589 0.2043 -0.0525 0.0698  -0.0174 26  GLU   A N   
689  N  N   B GLU   A 26  ? 0.2036 0.2361 0.2128 -0.0471 0.0701  -0.0251 26  GLU   A N   
690  C  CA  A GLU   A 26  ? 0.2124 0.2607 0.1872 -0.0577 0.0601  -0.0058 26  GLU   A CA  
691  C  CA  B GLU   A 26  ? 0.2059 0.2345 0.2066 -0.0460 0.0699  -0.0134 26  GLU   A CA  
692  C  C   A GLU   A 26  ? 0.2095 0.2417 0.1677 -0.0540 0.0588  -0.0030 26  GLU   A C   
693  C  C   B GLU   A 26  ? 0.2005 0.2264 0.1851 -0.0406 0.0606  -0.0041 26  GLU   A C   
694  O  O   A GLU   A 26  ? 0.2157 0.2400 0.1556 -0.0557 0.0590  -0.0031 26  GLU   A O   
695  O  O   B GLU   A 26  ? 0.2061 0.2207 0.1723 -0.0437 0.0597  -0.0095 26  GLU   A O   
696  C  CB  A GLU   A 26  ? 0.2331 0.2741 0.2100 -0.0625 0.0492  0.0052  26  GLU   A CB  
697  C  CB  B GLU   A 26  ? 0.2168 0.2386 0.2278 -0.0551 0.0616  -0.0133 26  GLU   A CB  
698  C  CG  A GLU   A 26  ? 0.2495 0.2888 0.2595 -0.0658 0.0431  0.0010  26  GLU   A CG  
699  C  CG  B GLU   A 26  ? 0.2205 0.2383 0.2364 -0.0680 0.0703  -0.0208 26  GLU   A CG  
700  C  CD  A GLU   A 26  ? 0.2526 0.2988 0.2840 -0.0754 0.0469  0.0014  26  GLU   A CD  
701  C  CD  B GLU   A 26  ? 0.2188 0.2339 0.2366 -0.0863 0.0782  -0.0343 26  GLU   A CD  
702  O  OE1 A GLU   A 26  ? 0.2343 0.3172 0.2932 -0.0668 0.0577  -0.0255 26  GLU   A OE1 
703  O  OE1 B GLU   A 26  ? 0.2175 0.2412 0.2582 -0.0878 0.0849  -0.0461 26  GLU   A OE1 
704  O  OE2 A GLU   A 26  ? 0.2783 0.2994 0.3005 -0.0786 0.0408  0.0179  26  GLU   A OE2 
705  O  OE2 B GLU   A 26  ? 0.2204 0.2318 0.1929 -0.0904 0.0940  -0.0376 26  GLU   A OE2 
718  N  N   A ALA   A 27  ? 0.1971 0.2207 0.1695 -0.0552 0.0607  0.0029  27  ALA   A N   
719  N  N   B ALA   A 27  ? 0.1895 0.2236 0.1754 -0.0324 0.0519  0.0138  27  ALA   A N   
720  C  CA  A ALA   A 27  ? 0.2023 0.2123 0.1542 -0.0492 0.0593  0.0024  27  ALA   A CA  
721  C  CA  B ALA   A 27  ? 0.1930 0.2286 0.1709 -0.0237 0.0420  0.0209  27  ALA   A CA  
722  C  C   A ALA   A 27  ? 0.2272 0.2283 0.1681 -0.0528 0.0662  -0.0154 27  ALA   A C   
723  C  C   B ALA   A 27  ? 0.2119 0.2430 0.1773 -0.0095 0.0373  0.0134  27  ALA   A C   
724  O  O   A ALA   A 27  ? 0.2351 0.2306 0.1767 -0.0551 0.0595  -0.0244 27  ALA   A O   
725  O  O   B ALA   A 27  ? 0.2066 0.2376 0.1771 -0.0008 0.0294  0.0130  27  ALA   A O   
726  C  CB  A ALA   A 27  ? 0.1878 0.1943 0.1548 -0.0455 0.0405  0.0095  27  ALA   A CB  
727  C  CB  B ALA   A 27  ? 0.1815 0.2222 0.1681 -0.0320 0.0356  0.0226  27  ALA   A CB  
738  N  N   A LYS   A 28  ? 0.2537 0.2506 0.1893 -0.0505 0.0585  -0.0330 28  LYS   A N   
739  N  N   B LYS   A 28  ? 0.2413 0.2619 0.1944 -0.0016 0.0362  -0.0002 28  LYS   A N   
740  C  CA  A LYS   A 28  ? 0.2852 0.2832 0.2255 -0.0452 0.0628  -0.0363 28  LYS   A CA  
741  C  CA  B LYS   A 28  ? 0.2711 0.2869 0.2207 0.0062  0.0361  -0.0151 28  LYS   A CA  
742  C  C   A LYS   A 28  ? 0.3021 0.3118 0.2216 -0.0484 0.0798  -0.0247 28  LYS   A C   
743  C  C   B LYS   A 28  ? 0.2977 0.3101 0.2268 0.0039  0.0413  -0.0114 28  LYS   A C   
744  O  O   A LYS   A 28  ? 0.3074 0.3174 0.2583 -0.0450 0.0625  -0.0257 28  LYS   A O   
745  O  O   B LYS   A 28  ? 0.3051 0.3151 0.2373 0.0095  0.0320  -0.0144 28  LYS   A O   
746  C  CB  A LYS   A 28  ? 0.2982 0.2924 0.2648 -0.0329 0.0575  -0.0451 28  LYS   A CB  
747  C  CB  B LYS   A 28  ? 0.2773 0.2927 0.2491 0.0129  0.0343  -0.0284 28  LYS   A CB  
748  C  CG  A LYS   A 28  ? 0.3099 0.3005 0.2997 -0.0248 0.0581  -0.0459 28  LYS   A CG  
749  C  CG  B LYS   A 28  ? 0.2847 0.3005 0.2755 0.0149  0.0365  -0.0312 28  LYS   A CG  
750  C  CD  A LYS   A 28  ? 0.3194 0.3143 0.3504 -0.0208 0.0565  -0.0348 28  LYS   A CD  
751  C  CD  B LYS   A 28  ? 0.2949 0.3103 0.3101 0.0174  0.0349  -0.0299 28  LYS   A CD  
752  C  CE  A LYS   A 28  ? 0.3275 0.3255 0.3844 -0.0201 0.0592  -0.0290 28  LYS   A CE  
753  C  CE  B LYS   A 28  ? 0.3047 0.3178 0.3378 0.0182  0.0351  -0.0324 28  LYS   A CE  
754  N  NZ  A LYS   A 28  ? 0.3337 0.3312 0.4040 -0.0172 0.0664  -0.0327 28  LYS   A NZ  
755  N  NZ  B LYS   A 28  ? 0.3115 0.3218 0.3521 0.0196  0.0345  -0.0398 28  LYS   A NZ  
782  N  N   A LYS   A 29  ? 0.3117 0.3354 0.2181 -0.0567 0.1092  -0.0070 29  LYS   A N   
783  N  N   B LYS   A 29  ? 0.3143 0.3284 0.2403 -0.0076 0.0575  -0.0010 29  LYS   A N   
784  C  CA  A LYS   A 29  ? 0.3260 0.3601 0.2315 -0.0625 0.1254  0.0018  29  LYS   A CA  
785  C  CA  B LYS   A 29  ? 0.3324 0.3481 0.2645 -0.0198 0.0658  0.0036  29  LYS   A CA  
786  C  C   A LYS   A 29  ? 0.3236 0.3585 0.2096 -0.0755 0.1198  0.0060  29  LYS   A C   
787  C  C   B LYS   A 29  ? 0.3345 0.3471 0.2501 -0.0311 0.0655  0.0123  29  LYS   A C   
788  O  O   A LYS   A 29  ? 0.3280 0.3705 0.2104 -0.0708 0.1206  -0.0030 29  LYS   A O   
789  O  O   B LYS   A 29  ? 0.3377 0.3527 0.2597 -0.0283 0.0712  0.0209  29  LYS   A O   
790  C  CB  A LYS   A 29  ? 0.3390 0.3854 0.2811 -0.0548 0.1432  0.0056  29  LYS   A CB  
791  C  CB  B LYS   A 29  ? 0.3465 0.3672 0.3078 -0.0200 0.0721  -0.0014 29  LYS   A CB  
792  C  CG  A LYS   A 29  ? 0.3530 0.4087 0.3394 -0.0471 0.1455  0.0073  29  LYS   A CG  
793  C  CG  B LYS   A 29  ? 0.3616 0.3855 0.3518 -0.0199 0.0719  -0.0061 29  LYS   A CG  
794  C  CD  A LYS   A 29  ? 0.3662 0.4300 0.4034 -0.0417 0.1417  0.0054  29  LYS   A CD  
795  C  CD  B LYS   A 29  ? 0.3740 0.4017 0.3937 -0.0202 0.0719  -0.0101 29  LYS   A CD  
796  C  CE  A LYS   A 29  ? 0.3744 0.4455 0.4426 -0.0388 0.1430  0.0025  29  LYS   A CE  
797  C  CE  B LYS   A 29  ? 0.3828 0.4138 0.4210 -0.0217 0.0740  -0.0151 29  LYS   A CE  
798  N  NZ  A LYS   A 29  ? 0.3767 0.4540 0.4713 -0.0371 0.1412  -0.0003 29  LYS   A NZ  
799  N  NZ  B LYS   A 29  ? 0.3870 0.4201 0.4394 -0.0225 0.0723  -0.0176 29  LYS   A NZ  
826  N  N   A VAL   A 30  ? 0.3170 0.3440 0.1921 -0.0888 0.1130  0.0141  30  VAL   A N   
827  N  N   B VAL   A 30  ? 0.3313 0.3383 0.2283 -0.0464 0.0607  0.0136  30  VAL   A N   
828  C  CA  A VAL   A 30  ? 0.3182 0.3317 0.1865 -0.0970 0.0865  0.0260  30  VAL   A CA  
829  C  CA  B VAL   A 30  ? 0.3310 0.3277 0.2126 -0.0607 0.0490  0.0204  30  VAL   A CA  
830  C  C   A VAL   A 30  ? 0.3251 0.3216 0.1597 -0.0981 0.0643  0.0309  30  VAL   A C   
831  C  C   B VAL   A 30  ? 0.3305 0.3206 0.1792 -0.0772 0.0454  0.0221  30  VAL   A C   
832  O  O   A VAL   A 30  ? 0.3333 0.3224 0.1651 -0.1000 0.0500  0.0345  30  VAL   A O   
833  O  O   B VAL   A 30  ? 0.3363 0.3221 0.1841 -0.0774 0.0363  0.0223  30  VAL   A O   
834  C  CB  A VAL   A 30  ? 0.3116 0.3274 0.2165 -0.1055 0.0745  0.0284  30  VAL   A CB  
835  C  CB  B VAL   A 30  ? 0.3307 0.3229 0.2346 -0.0588 0.0400  0.0237  30  VAL   A CB  
836  C  CG1 A VAL   A 30  ? 0.3110 0.3237 0.2245 -0.1082 0.0632  0.0275  30  VAL   A CG1 
837  C  CG1 B VAL   A 30  ? 0.3309 0.3217 0.2442 -0.0572 0.0343  0.0225  30  VAL   A CG1 
838  C  CG2 A VAL   A 30  ? 0.3095 0.3304 0.2386 -0.1090 0.0732  0.0288  30  VAL   A CG2 
839  C  CG2 B VAL   A 30  ? 0.3321 0.3226 0.2450 -0.0587 0.0382  0.0266  30  VAL   A CG2 
858  N  N   . LYS   A 31  ? 0.3226 0.3118 0.1529 -0.0927 0.0445  0.0210  31  LYS   A N   
859  C  CA  . LYS   A 31  ? 0.3311 0.3097 0.1724 -0.0847 0.0138  0.0148  31  LYS   A CA  
860  C  C   . LYS   A 31  ? 0.3045 0.2900 0.1404 -0.0708 0.0009  0.0491  31  LYS   A C   
861  O  O   . LYS   A 31  ? 0.3130 0.3076 0.1601 -0.0664 -0.0202 0.0647  31  LYS   A O   
862  C  CB  . LYS   A 31  ? 0.3702 0.3372 0.2777 -0.0828 -0.0097 -0.0119 31  LYS   A CB  
863  C  CG  . LYS   A 31  ? 0.4127 0.3674 0.4101 -0.0743 -0.0333 -0.0260 31  LYS   A CG  
864  C  CD  . LYS   A 31  ? 0.4456 0.3913 0.5095 -0.0676 -0.0531 -0.0375 31  LYS   A CD  
865  C  CE  . LYS   A 31  ? 0.4692 0.4098 0.5694 -0.0618 -0.0676 -0.0511 31  LYS   A CE  
866  N  NZ  . LYS   A 31  ? 0.4809 0.4173 0.6071 -0.0570 -0.0749 -0.0606 31  LYS   A NZ  
881  N  N   . PRO   A 32  ? 0.2644 0.2556 0.1242 -0.0672 0.0074  0.0334  32  PRO   A N   
882  C  CA  . PRO   A 32  ? 0.2525 0.2362 0.1494 -0.0590 -0.0062 0.0509  32  PRO   A CA  
883  C  C   . PRO   A 32  ? 0.2475 0.2321 0.1582 -0.0457 -0.0153 0.0589  32  PRO   A C   
884  O  O   . PRO   A 32  ? 0.2391 0.2240 0.1751 -0.0459 -0.0252 0.0606  32  PRO   A O   
885  C  CB  . PRO   A 32  ? 0.2411 0.2409 0.1669 -0.0568 -0.0093 0.0411  32  PRO   A CB  
886  C  CG  . PRO   A 32  ? 0.2371 0.2477 0.1218 -0.0501 -0.0226 0.0278  32  PRO   A CG  
887  C  CD  . PRO   A 32  ? 0.2445 0.2499 0.1193 -0.0581 -0.0070 0.0305  32  PRO   A CD  
895  N  N   . THR   A 33  ? 0.2530 0.2340 0.1522 -0.0382 -0.0174 0.0564  33  THR   A N   
896  C  CA  . THR   A 33  ? 0.2517 0.2363 0.1453 -0.0297 -0.0349 0.0567  33  THR   A CA  
897  C  C   . THR   A 33  ? 0.2199 0.2160 0.1411 -0.0325 -0.0341 0.0422  33  THR   A C   
898  O  O   . THR   A 33  ? 0.2133 0.2166 0.1662 -0.0364 -0.0443 0.0480  33  THR   A O   
899  C  CB  . THR   A 33  ? 0.2774 0.2568 0.1675 -0.0215 -0.0412 0.0742  33  THR   A CB  
900  O  OG1 . THR   A 33  ? 0.3052 0.2705 0.1976 -0.0075 -0.0249 0.0897  33  THR   A OG1 
901  C  CG2 . THR   A 33  ? 0.2791 0.2647 0.1858 -0.0186 -0.0516 0.0722  33  THR   A CG2 
909  N  N   . VAL   A 34  ? 0.1955 0.1975 0.1235 -0.0380 -0.0163 0.0379  34  VAL   A N   
910  C  CA  . VAL   A 34  ? 0.1761 0.1794 0.1181 -0.0301 -0.0082 0.0341  34  VAL   A CA  
911  C  C   . VAL   A 34  ? 0.1636 0.1675 0.1194 -0.0297 0.0024  0.0291  34  VAL   A C   
912  O  O   . VAL   A 34  ? 0.1650 0.1728 0.1454 -0.0328 0.0027  0.0368  34  VAL   A O   
913  C  CB  . VAL   A 34  ? 0.1786 0.1750 0.1478 -0.0253 -0.0079 0.0247  34  VAL   A CB  
914  C  CG1 . VAL   A 34  ? 0.1778 0.1785 0.1546 -0.0163 0.0039  0.0186  34  VAL   A CG1 
915  C  CG2 . VAL   A 34  ? 0.1868 0.1831 0.1805 -0.0189 -0.0172 0.0219  34  VAL   A CG2 
925  N  N   . VAL   A 35  ? 0.1477 0.1538 0.1264 -0.0300 -0.0081 0.0272  35  VAL   A N   
926  C  CA  . VAL   A 35  ? 0.1420 0.1545 0.1161 -0.0224 -0.0041 0.0239  35  VAL   A CA  
927  C  C   . VAL   A 35  ? 0.1362 0.1397 0.1146 -0.0187 -0.0007 0.0233  35  VAL   A C   
928  O  O   . VAL   A 35  ? 0.1253 0.1497 0.1443 -0.0279 0.0097  0.0180  35  VAL   A O   
929  C  CB  . VAL   A 35  ? 0.1476 0.1616 0.1290 -0.0132 0.0049  0.0080  35  VAL   A CB  
930  C  CG1 . VAL   A 35  ? 0.1530 0.1615 0.1384 -0.0117 0.0132  0.0009  35  VAL   A CG1 
931  C  CG2 . VAL   A 35  ? 0.1486 0.1624 0.1495 -0.0099 0.0122  0.0077  35  VAL   A CG2 
941  N  N   . VAL   A 36  ? 0.1208 0.1402 0.1163 -0.0168 0.0027  0.0234  36  VAL   A N   
942  C  CA  . VAL   A 36  ? 0.1194 0.1270 0.1175 -0.0091 0.0013  0.0141  36  VAL   A CA  
943  C  C   . VAL   A 36  ? 0.1179 0.1335 0.1223 -0.0144 0.0069  0.0140  36  VAL   A C   
944  O  O   . VAL   A 36  ? 0.1222 0.1301 0.1561 -0.0068 0.0136  0.0216  36  VAL   A O   
945  C  CB  . VAL   A 36  ? 0.1209 0.1226 0.1302 -0.0096 0.0009  0.0222  36  VAL   A CB  
946  C  CG1 . VAL   A 36  ? 0.1300 0.1295 0.1413 -0.0112 0.0021  0.0030  36  VAL   A CG1 
947  C  CG2 . VAL   A 36  ? 0.1281 0.1221 0.1562 -0.0078 0.0005  0.0196  36  VAL   A CG2 
957  N  N   . ASN   A 37  ? 0.1120 0.1176 0.1246 -0.0063 0.0041  0.0179  37  ASN   A N   
958  C  CA  . ASN   A 37  ? 0.1110 0.1176 0.1214 -0.0004 0.0086  0.0216  37  ASN   A CA  
959  C  C   . ASN   A 37  ? 0.1133 0.1157 0.1160 -0.0034 0.0102  0.0306  37  ASN   A C   
960  O  O   . ASN   A 37  ? 0.1234 0.1221 0.1323 0.0049  0.0116  0.0133  37  ASN   A O   
961  C  CB  . ASN   A 37  ? 0.1129 0.1161 0.1280 0.0008  0.0096  0.0163  37  ASN   A CB  
962  C  CG  . ASN   A 37  ? 0.1143 0.1232 0.1419 -0.0008 0.0078  0.0135  37  ASN   A CG  
963  O  OD1 . ASN   A 37  ? 0.1130 0.1240 0.1599 -0.0020 0.0078  0.0219  37  ASN   A OD1 
964  N  ND2 . ASN   A 37  ? 0.1184 0.1230 0.1469 -0.0027 0.0015  0.0278  37  ASN   A ND2 
971  N  N   . ALA   A 38  ? 0.1137 0.1262 0.1305 -0.0013 0.0109  0.0199  38  ALA   A N   
972  C  CA  . ALA   A 38  ? 0.1241 0.1335 0.1370 -0.0047 -0.0007 0.0202  38  ALA   A CA  
973  C  C   . ALA   A 38  ? 0.1225 0.1308 0.1300 0.0025  -0.0033 0.0141  38  ALA   A C   
974  O  O   . ALA   A 38  ? 0.1251 0.1243 0.1430 0.0068  -0.0011 0.0158  38  ALA   A O   
975  C  CB  . ALA   A 38  ? 0.1269 0.1628 0.1562 -0.0129 -0.0078 0.0132  38  ALA   A CB  
981  N  N   . ALA   A 39  ? 0.1224 0.1223 0.1403 -0.0003 0.0038  0.0194  39  ALA   A N   
982  C  CA  . ALA   A 39  ? 0.1242 0.1241 0.1381 -0.0018 0.0078  0.0112  39  ALA   A CA  
983  C  C   . ALA   A 39  ? 0.1285 0.1233 0.1352 -0.0034 0.0044  0.0062  39  ALA   A C   
984  O  O   . ALA   A 39  ? 0.1338 0.1257 0.1416 -0.0063 0.0068  0.0076  39  ALA   A O   
985  C  CB  . ALA   A 39  ? 0.1291 0.1439 0.1447 -0.0033 0.0001  0.0026  39  ALA   A CB  
991  N  N   . ASN   A 40  ? 0.1379 0.1232 0.1357 -0.0107 0.0192  0.0059  40  ASN   A N   
992  C  CA  . ASN   A 40  ? 0.1482 0.1196 0.1418 -0.0043 0.0118  0.0060  40  ASN   A CA  
993  C  C   . ASN   A 40  ? 0.1516 0.1122 0.1188 -0.0045 0.0226  0.0159  40  ASN   A C   
994  O  O   . ASN   A 40  ? 0.1412 0.1189 0.1356 -0.0068 0.0260  0.0166  40  ASN   A O   
995  C  CB  . ASN   A 40  ? 0.1581 0.1240 0.1461 -0.0019 0.0025  0.0119  40  ASN   A CB  
996  C  CG  . ASN   A 40  ? 0.1641 0.1283 0.1791 0.0046  -0.0002 0.0106  40  ASN   A CG  
997  O  OD1 . ASN   A 40  ? 0.1673 0.1322 0.2020 -0.0037 0.0088  0.0043  40  ASN   A OD1 
998  N  ND2 . ASN   A 40  ? 0.1710 0.1399 0.1973 0.0048  0.0028  -0.0044 40  ASN   A ND2 
1005 N  N   . VAL   A 41  ? 0.1576 0.1207 0.1228 -0.0068 0.0189  0.0140  41  VAL   A N   
1006 C  CA  . VAL   A 41  ? 0.1608 0.1289 0.1430 -0.0043 0.0329  0.0153  41  VAL   A CA  
1007 C  C   . VAL   A 41  ? 0.1541 0.1208 0.1453 0.0025  0.0321  0.0178  41  VAL   A C   
1008 O  O   . VAL   A 41  ? 0.1551 0.1161 0.1748 0.0039  0.0293  0.0101  41  VAL   A O   
1009 C  CB  . VAL   A 41  ? 0.1804 0.1392 0.1534 -0.0121 0.0431  0.0096  41  VAL   A CB  
1010 C  CG1 . VAL   A 41  ? 0.1908 0.1436 0.1707 -0.0077 0.0395  0.0013  41  VAL   A CG1 
1011 C  CG2 . VAL   A 41  ? 0.2029 0.1532 0.1483 -0.0225 0.0537  0.0137  41  VAL   A CG2 
1021 N  N   . TYR   A 42  ? 0.1420 0.1195 0.1666 -0.0011 0.0335  0.0218  42  TYR   A N   
1022 C  CA  . TYR   A 42  ? 0.1440 0.1180 0.1635 -0.0031 0.0343  0.0310  42  TYR   A CA  
1023 C  C   . TYR   A 42  ? 0.1344 0.1223 0.1576 -0.0016 0.0276  0.0292  42  TYR   A C   
1024 O  O   . TYR   A 42  ? 0.1314 0.1227 0.1789 -0.0111 0.0252  0.0089  42  TYR   A O   
1025 C  CB  . TYR   A 42  ? 0.1652 0.1318 0.1637 0.0007  0.0425  0.0333  42  TYR   A CB  
1026 C  CG  . TYR   A 42  ? 0.1814 0.1386 0.1627 -0.0008 0.0325  0.0378  42  TYR   A CG  
1027 C  CD1 . TYR   A 42  ? 0.1886 0.1480 0.1771 -0.0081 0.0395  0.0326  42  TYR   A CD1 
1028 C  CD2 . TYR   A 42  ? 0.1971 0.1618 0.1754 -0.0021 0.0228  0.0291  42  TYR   A CD2 
1029 C  CE1 . TYR   A 42  ? 0.1998 0.1629 0.1749 -0.0172 0.0361  0.0283  42  TYR   A CE1 
1030 C  CE2 . TYR   A 42  ? 0.2132 0.1793 0.1917 -0.0172 0.0244  0.0279  42  TYR   A CE2 
1031 C  CZ  . TYR   A 42  ? 0.2203 0.1813 0.1761 -0.0254 0.0370  0.0232  42  TYR   A CZ  
1032 O  OH  . TYR   A 42  ? 0.2382 0.1980 0.2029 -0.0367 0.0349  0.0151  42  TYR   A OH  
1042 N  N   . LEU   A 43  ? 0.1328 0.1211 0.1452 -0.0055 0.0144  0.0172  43  LEU   A N   
1043 C  CA  . LEU   A 43  ? 0.1245 0.1197 0.1438 -0.0074 0.0126  0.0143  43  LEU   A CA  
1044 C  C   . LEU   A 43  ? 0.1218 0.1250 0.1450 -0.0077 0.0083  0.0038  43  LEU   A C   
1045 O  O   . LEU   A 43  ? 0.1370 0.1283 0.1642 0.0038  -0.0017 0.0062  43  LEU   A O   
1046 C  CB  . LEU   A 43  ? 0.1284 0.1147 0.1580 -0.0096 0.0061  0.0106  43  LEU   A CB  
1047 C  CG  . LEU   A 43  ? 0.1356 0.1163 0.1629 -0.0027 0.0115  0.0080  43  LEU   A CG  
1048 C  CD1 . LEU   A 43  ? 0.1445 0.1329 0.1781 0.0001  0.0002  0.0182  43  LEU   A CD1 
1049 C  CD2 . LEU   A 43  ? 0.1495 0.1220 0.1611 -0.0042 0.0144  0.0167  43  LEU   A CD2 
1061 N  N   . LYS   A 44  ? 0.1290 0.1221 0.1447 -0.0013 0.0100  0.0094  44  LYS   A N   
1062 C  CA  . LYS   A 44  ? 0.1453 0.1243 0.1514 -0.0020 0.0142  0.0201  44  LYS   A CA  
1063 C  C   . LYS   A 44  ? 0.1312 0.1251 0.1319 0.0057  0.0032  0.0142  44  LYS   A C   
1064 O  O   . LYS   A 44  ? 0.1383 0.1395 0.1494 0.0019  0.0014  -0.0012 44  LYS   A O   
1065 C  CB  . LYS   A 44  ? 0.1768 0.1372 0.1987 -0.0013 0.0274  0.0273  44  LYS   A CB  
1066 C  CG  . LYS   A 44  ? 0.2082 0.1724 0.2621 -0.0036 0.0494  0.0315  44  LYS   A CG  
1067 C  CD  . LYS   A 44  ? 0.2455 0.2320 0.3849 -0.0058 0.0448  0.0234  44  LYS   A CD  
1068 C  CE  . LYS   A 44  ? 0.2585 0.2765 0.4624 -0.0070 0.0409  0.0185  44  LYS   A CE  
1069 N  NZ  . LYS   A 44  ? 0.2664 0.3014 0.4947 -0.0092 0.0327  0.0134  44  LYS   A NZ  
1083 N  N   A HIS   A 45  ? 0.1177 0.1215 0.1319 0.0013  -0.0016 0.0152  45  HIS   A N   
1084 N  N   B HIS   A 45  ? 0.1275 0.1286 0.1407 -0.0001 -0.0093 0.0153  45  HIS   A N   
1085 C  CA  A HIS   A 45  ? 0.1119 0.1134 0.1415 0.0008  0.0091  0.0043  45  HIS   A CA  
1086 C  CA  B HIS   A 45  ? 0.1292 0.1295 0.1545 -0.0039 -0.0104 0.0079  45  HIS   A CA  
1087 C  C   A HIS   A 45  ? 0.1120 0.1240 0.1538 0.0013  0.0107  0.0144  45  HIS   A C   
1088 C  C   B HIS   A 45  ? 0.1402 0.1390 0.1654 -0.0024 -0.0130 0.0173  45  HIS   A C   
1089 O  O   A HIS   A 45  ? 0.1185 0.1165 0.1658 -0.0022 0.0113  0.0080  45  HIS   A O   
1090 O  O   B HIS   A 45  ? 0.1489 0.1436 0.1823 0.0053  -0.0071 0.0226  45  HIS   A O   
1091 C  CB  A HIS   A 45  ? 0.1167 0.1083 0.1342 0.0061  0.0159  0.0021  45  HIS   A CB  
1092 C  CB  B HIS   A 45  ? 0.1233 0.1262 0.1490 -0.0031 -0.0081 0.0018  45  HIS   A CB  
1093 C  CG  A HIS   A 45  ? 0.1176 0.1022 0.1135 -0.0003 0.0140  0.0116  45  HIS   A CG  
1094 C  CG  B HIS   A 45  ? 0.1147 0.1277 0.1300 -0.0074 0.0012  0.0006  45  HIS   A CG  
1095 N  ND1 A HIS   A 45  ? 0.1125 0.1109 0.1157 -0.0009 0.0030  0.0073  45  HIS   A ND1 
1096 N  ND1 B HIS   A 45  ? 0.1112 0.1325 0.1586 -0.0033 0.0003  0.0109  45  HIS   A ND1 
1097 C  CD2 A HIS   A 45  ? 0.1245 0.1063 0.1327 -0.0036 0.0058  0.0194  45  HIS   A CD2 
1098 C  CD2 B HIS   A 45  ? 0.1061 0.1202 0.1087 -0.0036 0.0030  -0.0084 45  HIS   A CD2 
1099 C  CE1 A HIS   A 45  ? 0.1235 0.1178 0.1170 -0.0018 0.0105  0.0170  45  HIS   A CE1 
1100 C  CE1 B HIS   A 45  ? 0.1101 0.1230 0.1290 -0.0080 0.0052  -0.0026 45  HIS   A CE1 
1101 N  NE2 A HIS   A 45  ? 0.1292 0.1189 0.1275 0.0017  0.0104  0.0193  45  HIS   A NE2 
1102 N  NE2 B HIS   A 45  ? 0.1081 0.1187 0.1012 -0.0089 -0.0034 -0.0133 45  HIS   A NE2 
1117 N  N   A GLY   A 46  ? 0.1223 0.1393 0.1737 0.0112  -0.0054 0.0256  46  GLY   A N   
1118 N  N   B GLY   A 46  ? 0.1447 0.1386 0.1619 -0.0084 -0.0172 0.0208  46  GLY   A N   
1119 C  CA  A GLY   A 46  ? 0.1231 0.1400 0.1893 0.0064  -0.0133 0.0324  46  GLY   A CA  
1120 C  CA  B GLY   A 46  ? 0.1405 0.1404 0.1652 -0.0063 -0.0103 0.0214  46  GLY   A CA  
1121 C  C   A GLY   A 46  ? 0.1326 0.1326 0.1799 0.0130  -0.0135 0.0483  46  GLY   A C   
1122 C  C   B GLY   A 46  ? 0.1365 0.1439 0.1558 0.0017  -0.0032 0.0303  46  GLY   A C   
1123 O  O   A GLY   A 46  ? 0.1425 0.1287 0.1934 0.0177  -0.0188 0.0566  46  GLY   A O   
1124 O  O   B GLY   A 46  ? 0.1376 0.1472 0.1642 -0.0010 -0.0054 0.0262  46  GLY   A O   
1131 N  N   A GLY   A 47  ? 0.1276 0.1343 0.1619 0.0133  -0.0127 0.0348  47  GLY   A N   
1132 N  N   B GLY   A 47  ? 0.1347 0.1494 0.1532 0.0074  0.0049  0.0202  47  GLY   A N   
1133 C  CA  A GLY   A 47  ? 0.1290 0.1376 0.1541 0.0198  -0.0157 0.0260  47  GLY   A CA  
1134 C  CA  B GLY   A 47  ? 0.1306 0.1514 0.1489 0.0080  0.0026  0.0230  47  GLY   A CA  
1135 C  C   A GLY   A 47  ? 0.1282 0.1335 0.1401 0.0178  -0.0100 0.0188  47  GLY   A C   
1136 C  C   B GLY   A 47  ? 0.1294 0.1379 0.1232 0.0093  0.0034  0.0205  47  GLY   A C   
1137 O  O   A GLY   A 47  ? 0.1283 0.1312 0.1587 0.0181  -0.0055 0.0216  47  GLY   A O   
1138 O  O   B GLY   A 47  ? 0.1298 0.1302 0.1259 0.0087  0.0064  0.0255  47  GLY   A O   
1145 N  N   A GLY   A 48  ? 0.1285 0.1374 0.1283 0.0165  -0.0027 0.0099  48  GLY   A N   
1146 N  N   B GLY   A 48  ? 0.1267 0.1387 0.1262 0.0054  0.0065  0.0160  48  GLY   A N   
1147 C  CA  A GLY   A 48  ? 0.1261 0.1373 0.1335 0.0109  -0.0056 0.0033  48  GLY   A CA  
1148 C  CA  B GLY   A 48  ? 0.1246 0.1271 0.1174 0.0026  0.0056  -0.0020 48  GLY   A CA  
1149 C  C   A GLY   A 48  ? 0.1261 0.1346 0.1368 0.0012  0.0059  0.0052  48  GLY   A C   
1150 C  C   B GLY   A 48  ? 0.1241 0.1212 0.1216 -0.0011 0.0050  0.0080  48  GLY   A C   
1151 O  O   A GLY   A 48  ? 0.1408 0.1334 0.1319 -0.0021 0.0070  0.0112  48  GLY   A O   
1152 O  O   B GLY   A 48  ? 0.1365 0.1221 0.1125 -0.0019 0.0099  0.0058  48  GLY   A O   
1159 N  N   A VAL   A 49  ? 0.1259 0.1301 0.1539 -0.0031 -0.0098 0.0087  49  VAL   A N   
1160 N  N   B VAL   A 49  ? 0.1104 0.1188 0.1349 -0.0012 -0.0036 0.0039  49  VAL   A N   
1161 C  CA  A VAL   A 49  ? 0.1437 0.1242 0.1620 -0.0092 -0.0040 0.0079  49  VAL   A CA  
1162 C  CA  B VAL   A 49  ? 0.1093 0.1223 0.1416 -0.0024 0.0009  0.0072  49  VAL   A CA  
1163 C  C   A VAL   A 49  ? 0.1397 0.1137 0.1408 -0.0061 -0.0043 0.0184  49  VAL   A C   
1164 C  C   B VAL   A 49  ? 0.1142 0.1198 0.1190 0.0020  0.0064  -0.0070 49  VAL   A C   
1165 O  O   A VAL   A 49  ? 0.1406 0.1201 0.1466 -0.0194 -0.0032 0.0135  49  VAL   A O   
1166 O  O   B VAL   A 49  ? 0.1211 0.1267 0.1123 0.0023  0.0140  -0.0001 49  VAL   A O   
1167 C  CB  A VAL   A 49  ? 0.1586 0.1316 0.1855 -0.0074 -0.0059 0.0009  49  VAL   A CB  
1168 C  CB  B VAL   A 49  ? 0.1030 0.1182 0.1559 -0.0037 0.0002  0.0128  49  VAL   A CB  
1169 C  CG1 A VAL   A 49  ? 0.1667 0.1267 0.1934 0.0004  0.0004  0.0022  49  VAL   A CG1 
1170 C  CG1 B VAL   A 49  ? 0.0935 0.1096 0.1599 0.0010  -0.0038 0.0237  49  VAL   A CG1 
1171 C  CG2 A VAL   A 49  ? 0.1623 0.1417 0.2258 -0.0203 -0.0058 -0.0035 49  VAL   A CG2 
1172 C  CG2 B VAL   A 49  ? 0.1036 0.1156 0.1596 -0.0050 0.0185  0.0136  49  VAL   A CG2 
1191 N  N   A ALA   A 50  ? 0.1297 0.1136 0.1412 -0.0073 -0.0180 0.0187  50  ALA   A N   
1192 N  N   B ALA   A 50  ? 0.1161 0.1188 0.1189 0.0019  -0.0010 -0.0100 50  ALA   A N   
1193 C  CA  A ALA   A 50  ? 0.1189 0.1119 0.1483 -0.0116 -0.0094 0.0170  50  ALA   A CA  
1194 C  CA  B ALA   A 50  ? 0.1153 0.1168 0.1209 -0.0030 -0.0007 -0.0070 50  ALA   A CA  
1195 C  C   A ALA   A 50  ? 0.1102 0.1163 0.1455 -0.0099 -0.0019 0.0183  50  ALA   A C   
1196 C  C   B ALA   A 50  ? 0.1217 0.1145 0.1048 -0.0013 -0.0062 -0.0054 50  ALA   A C   
1197 O  O   A ALA   A 50  ? 0.1113 0.1208 0.1583 -0.0042 0.0013  0.0136  50  ALA   A O   
1198 O  O   B ALA   A 50  ? 0.1256 0.1176 0.0940 0.0061  -0.0072 -0.0106 50  ALA   A O   
1199 C  CB  A ALA   A 50  ? 0.1190 0.1120 0.1479 -0.0047 -0.0128 0.0133  50  ALA   A CB  
1200 C  CB  B ALA   A 50  ? 0.1176 0.1119 0.1211 -0.0026 0.0116  -0.0202 50  ALA   A CB  
1211 N  N   A GLY   A 51  ? 0.1195 0.1110 0.1371 0.0055  -0.0059 0.0105  51  GLY   A N   
1212 N  N   B GLY   A 51  ? 0.1300 0.1116 0.1182 0.0012  -0.0147 -0.0123 51  GLY   A N   
1213 C  CA  A GLY   A 51  ? 0.1236 0.1093 0.1430 0.0077  -0.0046 0.0122  51  GLY   A CA  
1214 C  CA  B GLY   A 51  ? 0.1383 0.1155 0.1109 -0.0031 -0.0192 -0.0142 51  GLY   A CA  
1215 C  C   A GLY   A 51  ? 0.1129 0.1177 0.1387 0.0070  -0.0022 0.0018  51  GLY   A C   
1216 C  C   B GLY   A 51  ? 0.1355 0.1262 0.1227 -0.0003 -0.0097 -0.0124 51  GLY   A C   
1217 O  O   A GLY   A 51  ? 0.1164 0.1285 0.1411 -0.0003 0.0017  -0.0001 51  GLY   A O   
1218 O  O   B GLY   A 51  ? 0.1430 0.1327 0.1251 0.0039  -0.0055 -0.0134 51  GLY   A O   
1225 N  N   A ALA   A 52  ? 0.1114 0.1296 0.1463 0.0048  -0.0032 0.0098  52  ALA   A N   
1226 N  N   B ALA   A 52  ? 0.1322 0.1317 0.1302 -0.0043 0.0038  -0.0186 52  ALA   A N   
1227 C  CA  A ALA   A 52  ? 0.1170 0.1381 0.1517 -0.0000 -0.0026 0.0085  52  ALA   A CA  
1228 C  CA  B ALA   A 52  ? 0.1280 0.1375 0.1307 -0.0044 0.0050  -0.0190 52  ALA   A CA  
1229 C  C   A ALA   A 52  ? 0.1168 0.1377 0.1357 -0.0093 0.0041  0.0126  52  ALA   A C   
1230 C  C   B ALA   A 52  ? 0.1227 0.1317 0.1224 -0.0114 0.0073  -0.0158 52  ALA   A C   
1231 O  O   A ALA   A 52  ? 0.1254 0.1480 0.1484 -0.0058 0.0022  0.0124  52  ALA   A O   
1232 O  O   B ALA   A 52  ? 0.1313 0.1290 0.1502 -0.0105 0.0112  -0.0127 52  ALA   A O   
1233 C  CB  A ALA   A 52  ? 0.1223 0.1599 0.1699 -0.0057 0.0001  0.0169  52  ALA   A CB  
1234 C  CB  B ALA   A 52  ? 0.1304 0.1544 0.1543 -0.0037 -0.0001 -0.0109 52  ALA   A CB  
1245 N  N   A LEU   A 53  ? 0.1151 0.1376 0.1388 -0.0056 -0.0010 0.0116  53  LEU   A N   
1246 N  N   B LEU   A 53  ? 0.1157 0.1332 0.1239 -0.0060 0.0026  -0.0159 53  LEU   A N   
1247 C  CA  A LEU   A 53  ? 0.1260 0.1428 0.1458 -0.0090 -0.0002 0.0092  53  LEU   A CA  
1248 C  CA  B LEU   A 53  ? 0.1144 0.1350 0.1190 -0.0044 0.0015  -0.0113 53  LEU   A CA  
1249 C  C   A LEU   A 53  ? 0.1311 0.1417 0.1205 0.0008  -0.0004 0.0097  53  LEU   A C   
1250 C  C   B LEU   A 53  ? 0.1196 0.1360 0.0977 -0.0002 0.0064  -0.0111 53  LEU   A C   
1251 O  O   A LEU   A 53  ? 0.1478 0.1421 0.1417 -0.0106 0.0069  0.0066  53  LEU   A O   
1252 O  O   B LEU   A 53  ? 0.1295 0.1397 0.1064 -0.0124 0.0080  -0.0028 53  LEU   A O   
1253 C  CB  A LEU   A 53  ? 0.1290 0.1448 0.1517 -0.0134 0.0030  0.0139  53  LEU   A CB  
1254 C  CB  B LEU   A 53  ? 0.1107 0.1328 0.1216 -0.0037 0.0038  -0.0075 53  LEU   A CB  
1255 C  CG  A LEU   A 53  ? 0.1263 0.1428 0.1496 -0.0131 0.0007  0.0134  53  LEU   A CG  
1256 C  CG  B LEU   A 53  ? 0.1120 0.1309 0.1227 -0.0060 -0.0041 -0.0039 53  LEU   A CG  
1257 C  CD1 A LEU   A 53  ? 0.1204 0.1505 0.1525 0.0014  0.0038  0.0192  53  LEU   A CD1 
1258 C  CD1 B LEU   A 53  ? 0.1163 0.1368 0.1392 -0.0065 -0.0031 -0.0121 53  LEU   A CD1 
1259 C  CD2 A LEU   A 53  ? 0.1364 0.1589 0.1599 -0.0131 -0.0059 0.0141  53  LEU   A CD2 
1260 C  CD2 B LEU   A 53  ? 0.1091 0.1342 0.1169 -0.0044 0.0028  -0.0068 53  LEU   A CD2 
1283 N  N   A ASN   A 54  ? 0.1183 0.1358 0.1204 -0.0045 -0.0102 0.0125  54  ASN   A N   
1284 N  N   B ASN   A 54  ? 0.1164 0.1331 0.1077 0.0006  0.0087  -0.0129 54  ASN   A N   
1285 C  CA  A ASN   A 54  ? 0.1088 0.1257 0.1490 -0.0070 -0.0105 0.0099  54  ASN   A CA  
1286 C  CA  B ASN   A 54  ? 0.1125 0.1295 0.1258 0.0026  0.0049  -0.0093 54  ASN   A CA  
1287 C  C   A ASN   A 54  ? 0.1178 0.1299 0.1586 -0.0125 -0.0032 0.0051  54  ASN   A C   
1288 C  C   B ASN   A 54  ? 0.1196 0.1318 0.1375 -0.0074 0.0057  -0.0042 54  ASN   A C   
1289 O  O   A ASN   A 54  ? 0.1265 0.1400 0.1604 -0.0077 -0.0125 -0.0057 54  ASN   A O   
1290 O  O   B ASN   A 54  ? 0.1258 0.1388 0.1258 -0.0065 0.0045  -0.0107 54  ASN   A O   
1291 C  CB  A ASN   A 54  ? 0.1097 0.1192 0.1647 -0.0144 -0.0126 0.0062  54  ASN   A CB  
1292 C  CB  B ASN   A 54  ? 0.1159 0.1258 0.1255 0.0081  0.0016  -0.0125 54  ASN   A CB  
1293 C  CG  A ASN   A 54  ? 0.1110 0.1173 0.1722 -0.0139 -0.0046 0.0074  54  ASN   A CG  
1294 C  CG  B ASN   A 54  ? 0.1148 0.1242 0.1230 0.0137  0.0021  -0.0162 54  ASN   A CG  
1295 O  OD1 A ASN   A 54  ? 0.1136 0.1176 0.1715 -0.0123 -0.0075 0.0239  54  ASN   A OD1 
1296 O  OD1 B ASN   A 54  ? 0.1117 0.1238 0.1243 0.0137  -0.0007 -0.0268 54  ASN   A OD1 
1297 N  ND2 A ASN   A 54  ? 0.1058 0.1240 0.1825 -0.0104 -0.0073 0.0101  54  ASN   A ND2 
1298 N  ND2 B ASN   A 54  ? 0.1192 0.1246 0.1275 0.0114  -0.0033 -0.0016 54  ASN   A ND2 
1311 N  N   . LYS   A 55  ? 0.1231 0.1287 0.1572 -0.0059 0.0012  -0.0012 55  LYS   A N   
1312 C  CA  . LYS   A 55  ? 0.1320 0.1406 0.1613 0.0037  -0.0030 -0.0105 55  LYS   A CA  
1313 C  C   . LYS   A 55  ? 0.1312 0.1447 0.1607 -0.0048 0.0017  -0.0169 55  LYS   A C   
1314 O  O   . LYS   A 55  ? 0.1379 0.1572 0.1750 0.0024  -0.0047 -0.0250 55  LYS   A O   
1315 C  CB  . LYS   A 55  ? 0.1380 0.1489 0.1739 0.0145  -0.0065 -0.0155 55  LYS   A CB  
1316 C  CG  . LYS   A 55  ? 0.1522 0.1734 0.1942 0.0244  -0.0111 -0.0273 55  LYS   A CG  
1317 C  CD  . LYS   A 55  ? 0.1693 0.2066 0.2091 0.0354  -0.0087 -0.0262 55  LYS   A CD  
1318 C  CE  . LYS   A 55  ? 0.1899 0.2425 0.2322 0.0426  -0.0291 -0.0246 55  LYS   A CE  
1319 N  NZ  . LYS   A 55  ? 0.1974 0.2667 0.2310 0.0521  -0.0384 -0.0208 55  LYS   A NZ  
1334 N  N   . ALA   A 56  ? 0.1356 0.1552 0.1537 -0.0089 0.0040  -0.0166 56  ALA   A N   
1335 C  CA  . ALA   A 56  ? 0.1450 0.1762 0.1566 -0.0116 0.0128  -0.0177 56  ALA   A CA  
1336 C  C   . ALA   A 56  ? 0.1535 0.1884 0.1334 -0.0122 0.0212  -0.0243 56  ALA   A C   
1337 O  O   . ALA   A 56  ? 0.1593 0.2192 0.1526 0.0040  0.0204  -0.0189 56  ALA   A O   
1338 C  CB  . ALA   A 56  ? 0.1500 0.1945 0.1663 -0.0205 0.0111  -0.0080 56  ALA   A CB  
1344 N  N   . THR   A 57  ? 0.1378 0.1726 0.1266 -0.0130 0.0159  -0.0155 57  THR   A N   
1345 C  CA  . THR   A 57  ? 0.1387 0.1678 0.1217 -0.0145 0.0045  -0.0102 57  THR   A CA  
1346 C  C   . THR   A 57  ? 0.1405 0.1678 0.1390 -0.0109 -0.0039 -0.0159 57  THR   A C   
1347 O  O   . THR   A 57  ? 0.1386 0.1739 0.1553 -0.0137 -0.0103 -0.0266 57  THR   A O   
1348 C  CB  . THR   A 57  ? 0.1355 0.1655 0.1293 -0.0135 -0.0004 -0.0101 57  THR   A CB  
1349 O  OG1 . THR   A 57  ? 0.1270 0.1585 0.1380 -0.0077 0.0009  -0.0105 57  THR   A OG1 
1350 C  CG2 . THR   A 57  ? 0.1422 0.1629 0.1203 -0.0061 -0.0012 0.0002  57  THR   A CG2 
1358 N  N   . ASN   A 58  ? 0.1444 0.1600 0.1657 -0.0077 0.0065  -0.0270 58  ASN   A N   
1359 C  CA  . ASN   A 58  ? 0.1627 0.1535 0.1876 -0.0121 0.0089  -0.0377 58  ASN   A CA  
1360 C  C   . ASN   A 58  ? 0.1408 0.1468 0.1708 -0.0009 -0.0018 -0.0232 58  ASN   A C   
1361 O  O   . ASN   A 58  ? 0.1426 0.1594 0.1873 -0.0167 -0.0001 -0.0293 58  ASN   A O   
1362 C  CB  . ASN   A 58  ? 0.2088 0.1756 0.2133 -0.0160 0.0305  -0.0479 58  ASN   A CB  
1363 C  CG  . ASN   A 58  ? 0.2569 0.2000 0.2884 -0.0123 0.0386  -0.0375 58  ASN   A CG  
1364 O  OD1 . ASN   A 58  ? 0.2834 0.1930 0.3335 0.0193  0.0722  -0.0245 58  ASN   A OD1 
1365 N  ND2 . ASN   A 58  ? 0.2722 0.2157 0.3174 -0.0161 0.0248  -0.0486 58  ASN   A ND2 
1372 N  N   . ASN   A 59  ? 0.1284 0.1395 0.1539 -0.0044 -0.0058 -0.0118 59  ASN   A N   
1373 C  CA  . ASN   A 59  ? 0.1236 0.1276 0.1561 -0.0026 -0.0029 -0.0091 59  ASN   A CA  
1374 C  C   . ASN   A 59  ? 0.1250 0.1297 0.1468 -0.0058 0.0003  -0.0029 59  ASN   A C   
1375 O  O   . ASN   A 59  ? 0.1299 0.1319 0.1545 -0.0068 0.0013  0.0016  59  ASN   A O   
1376 C  CB  . ASN   A 59  ? 0.1288 0.1239 0.1748 -0.0006 -0.0129 -0.0130 59  ASN   A CB  
1377 C  CG  . ASN   A 59  ? 0.1353 0.1351 0.1763 -0.0035 -0.0232 0.0010  59  ASN   A CG  
1378 O  OD1 . ASN   A 59  ? 0.1446 0.1376 0.1609 -0.0114 -0.0231 0.0068  59  ASN   A OD1 
1379 N  ND2 . ASN   A 59  ? 0.1390 0.1378 0.1767 -0.0140 -0.0148 0.0078  59  ASN   A ND2 
1386 N  N   . ALA   A 60  ? 0.1181 0.1389 0.1521 -0.0052 -0.0032 -0.0007 60  ALA   A N   
1387 C  CA  . ALA   A 60  ? 0.1204 0.1341 0.1572 -0.0044 -0.0114 -0.0043 60  ALA   A CA  
1388 C  C   . ALA   A 60  ? 0.1243 0.1315 0.1541 -0.0060 -0.0043 -0.0007 60  ALA   A C   
1389 O  O   . ALA   A 60  ? 0.1185 0.1340 0.1803 -0.0070 -0.0109 -0.0032 60  ALA   A O   
1390 C  CB  . ALA   A 60  ? 0.1383 0.1449 0.1678 -0.0034 -0.0112 -0.0154 60  ALA   A CB  
1396 N  N   . MET   A 61  ? 0.1180 0.1277 0.1499 -0.0059 0.0006  -0.0086 61  MET   A N   
1397 C  CA  . MET   A 61  ? 0.1196 0.1212 0.1486 -0.0083 0.0021  0.0011  61  MET   A CA  
1398 C  C   . MET   A 61  ? 0.1192 0.1226 0.1507 -0.0045 -0.0023 -0.0049 61  MET   A C   
1399 O  O   . MET   A 61  ? 0.1268 0.1207 0.1590 -0.0048 0.0053  0.0022  61  MET   A O   
1400 C  CB  . MET   A 61  ? 0.1256 0.1254 0.1368 -0.0097 0.0048  -0.0025 61  MET   A CB  
1401 C  CG  . MET   A 61  ? 0.1236 0.1387 0.1521 -0.0060 0.0029  0.0069  61  MET   A CG  
1402 S  SD  . MET   A 61  ? 0.1267 0.1343 0.1945 -0.0136 0.0014  -0.0150 61  MET   A SD  
1403 C  CE  . MET   A 61  ? 0.1521 0.1517 0.2020 -0.0168 0.0171  -0.0161 61  MET   A CE  
1413 N  N   . GLN   A 62  ? 0.1175 0.1205 0.1543 -0.0101 -0.0022 -0.0027 62  GLN   A N   
1414 C  CA  . GLN   A 62  ? 0.1221 0.1199 0.1548 -0.0051 0.0038  0.0042  62  GLN   A CA  
1415 C  C   . GLN   A 62  ? 0.1268 0.1107 0.1555 -0.0025 0.0072  0.0081  62  GLN   A C   
1416 O  O   . GLN   A 62  ? 0.1254 0.1256 0.1573 -0.0044 0.0069  0.0050  62  GLN   A O   
1417 C  CB  . GLN   A 62  ? 0.1214 0.1132 0.1591 0.0010  0.0031  -0.0014 62  GLN   A CB  
1418 C  CG  . GLN   A 62  ? 0.1250 0.1119 0.1542 -0.0036 -0.0011 0.0111  62  GLN   A CG  
1419 C  CD  . GLN   A 62  ? 0.1337 0.1193 0.1592 -0.0013 0.0024  0.0102  62  GLN   A CD  
1420 O  OE1 . GLN   A 62  ? 0.1369 0.1340 0.1639 -0.0023 -0.0004 0.0010  62  GLN   A OE1 
1421 N  NE2 . GLN   A 62  ? 0.1409 0.1255 0.1665 0.0005  0.0020  -0.0007 62  GLN   A NE2 
1430 N  N   . VAL   A 63  ? 0.1201 0.1195 0.1771 -0.0056 0.0087  -0.0094 63  VAL   A N   
1431 C  CA  . VAL   A 63  ? 0.1204 0.1298 0.1984 -0.0117 0.0007  -0.0139 63  VAL   A CA  
1432 C  C   . VAL   A 63  ? 0.1152 0.1300 0.1763 -0.0157 -0.0022 -0.0113 63  VAL   A C   
1433 O  O   . VAL   A 63  ? 0.1133 0.1327 0.1951 -0.0141 0.0021  -0.0055 63  VAL   A O   
1434 C  CB  . VAL   A 63  ? 0.1332 0.1450 0.2287 -0.0139 0.0005  -0.0332 63  VAL   A CB  
1435 C  CG1 . VAL   A 63  ? 0.1460 0.1657 0.2556 -0.0100 -0.0074 -0.0535 63  VAL   A CG1 
1436 C  CG2 . VAL   A 63  ? 0.1417 0.1403 0.2373 -0.0129 0.0184  -0.0293 63  VAL   A CG2 
1446 N  N   . GLU   A 64  ? 0.1143 0.1357 0.1654 -0.0105 -0.0015 -0.0005 64  GLU   A N   
1447 C  CA  . GLU   A 64  ? 0.1162 0.1342 0.1702 -0.0099 -0.0043 0.0028  64  GLU   A CA  
1448 C  C   . GLU   A 64  ? 0.1096 0.1278 0.1669 -0.0138 0.0021  0.0053  64  GLU   A C   
1449 O  O   . GLU   A 64  ? 0.1194 0.1319 0.1680 -0.0036 0.0017  0.0030  64  GLU   A O   
1450 C  CB  . GLU   A 64  ? 0.1268 0.1477 0.1715 -0.0054 0.0010  -0.0001 64  GLU   A CB  
1451 C  CG  . GLU   A 64  ? 0.1376 0.1487 0.1907 -0.0086 0.0017  0.0061  64  GLU   A CG  
1452 C  CD  . GLU   A 64  ? 0.1471 0.1534 0.1917 -0.0156 0.0075  0.0028  64  GLU   A CD  
1453 O  OE1 . GLU   A 64  ? 0.1419 0.1642 0.2128 -0.0180 0.0117  0.0038  64  GLU   A OE1 
1454 O  OE2 . GLU   A 64  ? 0.1658 0.1550 0.1806 -0.0245 -0.0033 0.0096  64  GLU   A OE2 
1461 N  N   . SER   A 65  ? 0.1034 0.1309 0.1569 -0.0025 0.0037  0.0062  65  SER   A N   
1462 C  CA  . SER   A 65  ? 0.1169 0.1279 0.1507 -0.0055 -0.0023 0.0047  65  SER   A CA  
1463 C  C   . SER   A 65  ? 0.1177 0.1341 0.1573 -0.0055 -0.0005 0.0015  65  SER   A C   
1464 O  O   . SER   A 65  ? 0.1273 0.1378 0.1753 0.0032  0.0164  -0.0031 65  SER   A O   
1465 C  CB  . SER   A 65  ? 0.1176 0.1228 0.1581 -0.0094 0.0008  0.0074  65  SER   A CB  
1466 O  OG  . SER   A 65  ? 0.1178 0.1333 0.1625 -0.0083 -0.0043 0.0116  65  SER   A OG  
1472 N  N   . ASP   A 66  ? 0.1223 0.1267 0.1647 -0.0028 0.0154  0.0074  66  ASP   A N   
1473 C  CA  . ASP   A 66  ? 0.1311 0.1403 0.1810 -0.0010 0.0138  0.0182  66  ASP   A CA  
1474 C  C   . ASP   A 66  ? 0.1236 0.1334 0.1828 -0.0056 0.0131  0.0199  66  ASP   A C   
1475 O  O   . ASP   A 66  ? 0.1309 0.1432 0.2023 -0.0006 0.0244  0.0240  66  ASP   A O   
1476 C  CB  . ASP   A 66  ? 0.1382 0.1479 0.2091 0.0075  0.0157  0.0308  66  ASP   A CB  
1477 C  CG  . ASP   A 66  ? 0.1586 0.1601 0.2387 0.0051  0.0008  0.0465  66  ASP   A CG  
1478 O  OD1 . ASP   A 66  ? 0.1577 0.1871 0.2267 -0.0069 -0.0075 0.0488  66  ASP   A OD1 
1479 O  OD2 . ASP   A 66  ? 0.1808 0.1685 0.3247 0.0244  -0.0168 0.0249  66  ASP   A OD2 
1484 N  N   . ASP   A 67  ? 0.1205 0.1369 0.1925 -0.0031 0.0101  0.0190  67  ASP   A N   
1485 C  CA  . ASP   A 67  ? 0.1207 0.1529 0.2080 -0.0014 0.0015  0.0322  67  ASP   A CA  
1486 C  C   . ASP   A 67  ? 0.1248 0.1546 0.2018 -0.0023 0.0146  0.0296  67  ASP   A C   
1487 O  O   . ASP   A 67  ? 0.1213 0.1580 0.2202 -0.0003 0.0251  0.0315  67  ASP   A O   
1488 C  CB  . ASP   A 67  ? 0.1299 0.1639 0.2334 -0.0081 -0.0096 0.0358  67  ASP   A CB  
1489 C  CG  . ASP   A 67  ? 0.1260 0.1766 0.2702 -0.0081 -0.0219 0.0462  67  ASP   A CG  
1490 O  OD1 . ASP   A 67  ? 0.1347 0.1925 0.3522 -0.0138 -0.0370 0.0533  67  ASP   A OD1 
1491 O  OD2 . ASP   A 67  ? 0.1271 0.1803 0.2504 -0.0020 -0.0149 0.0327  67  ASP   A OD2 
1496 N  N   . TYR   A 68  ? 0.1246 0.1402 0.1876 0.0023  0.0132  0.0308  68  TYR   A N   
1497 C  CA  . TYR   A 68  ? 0.1373 0.1361 0.1786 0.0009  0.0156  0.0293  68  TYR   A CA  
1498 C  C   . TYR   A 68  ? 0.1307 0.1357 0.1819 -0.0003 0.0155  0.0185  68  TYR   A C   
1499 O  O   . TYR   A 68  ? 0.1368 0.1435 0.1964 0.0080  0.0309  0.0211  68  TYR   A O   
1500 C  CB  . TYR   A 68  ? 0.1376 0.1386 0.1980 0.0083  0.0357  0.0260  68  TYR   A CB  
1501 C  CG  . TYR   A 68  ? 0.1392 0.1487 0.2266 0.0062  0.0498  0.0356  68  TYR   A CG  
1502 C  CD1 . TYR   A 68  ? 0.1467 0.1580 0.2668 -0.0201 0.0374  -0.0031 68  TYR   A CD1 
1503 C  CD2 . TYR   A 68  ? 0.1636 0.1537 0.2783 0.0123  0.0597  0.0386  68  TYR   A CD2 
1504 C  CE1 . TYR   A 68  ? 0.1572 0.1665 0.3121 -0.0171 0.0447  -0.0097 68  TYR   A CE1 
1505 C  CE2 . TYR   A 68  ? 0.1630 0.1574 0.3008 0.0011  0.0689  0.0159  68  TYR   A CE2 
1506 C  CZ  . TYR   A 68  ? 0.1665 0.1588 0.3148 -0.0147 0.0530  -0.0148 68  TYR   A CZ  
1507 O  OH  . TYR   A 68  ? 0.1976 0.1612 0.3348 -0.0114 0.0273  -0.0335 68  TYR   A OH  
1517 N  N   . ILE   A 69  ? 0.1254 0.1295 0.1731 -0.0018 0.0170  0.0220  69  ILE   A N   
1518 C  CA  . ILE   A 69  ? 0.1349 0.1365 0.1692 0.0028  0.0121  0.0092  69  ILE   A CA  
1519 C  C   . ILE   A 69  ? 0.1384 0.1357 0.1651 0.0025  0.0209  0.0165  69  ILE   A C   
1520 O  O   . ILE   A 69  ? 0.1458 0.1423 0.1725 -0.0024 0.0241  0.0209  69  ILE   A O   
1521 C  CB  . ILE   A 69  ? 0.1400 0.1574 0.1693 0.0040  0.0134  0.0035  69  ILE   A CB  
1522 C  CG1 . ILE   A 69  ? 0.1416 0.1639 0.1845 0.0102  0.0170  -0.0170 69  ILE   A CG1 
1523 C  CG2 . ILE   A 69  ? 0.1584 0.1749 0.1853 0.0146  0.0049  -0.0105 69  ILE   A CG2 
1524 C  CD1 . ILE   A 69  ? 0.1388 0.1718 0.2072 -0.0070 0.0193  -0.0175 69  ILE   A CD1 
1536 N  N   . ALA   A 70  ? 0.1415 0.1368 0.1844 -0.0046 0.0197  0.0176  70  ALA   A N   
1537 C  CA  . ALA   A 70  ? 0.1422 0.1483 0.2025 -0.0157 0.0330  0.0220  70  ALA   A CA  
1538 C  C   . ALA   A 70  ? 0.1409 0.1647 0.2050 -0.0074 0.0279  0.0266  70  ALA   A C   
1539 O  O   . ALA   A 70  ? 0.1571 0.1969 0.2218 0.0071  0.0500  0.0406  70  ALA   A O   
1540 C  CB  . ALA   A 70  ? 0.1489 0.1456 0.2274 -0.0151 0.0247  0.0175  70  ALA   A CB  
1546 N  N   . THR   A 71  ? 0.1348 0.1569 0.1991 0.0002  0.0154  0.0272  71  THR   A N   
1547 C  CA  . THR   A 71  ? 0.1456 0.1784 0.2196 0.0136  0.0195  0.0224  71  THR   A CA  
1548 C  C   . THR   A 71  ? 0.1333 0.1712 0.2406 0.0160  0.0396  0.0184  71  THR   A C   
1549 O  O   . THR   A 71  ? 0.1431 0.1977 0.2809 0.0127  0.0464  -0.0051 71  THR   A O   
1550 C  CB  . THR   A 71  ? 0.1730 0.2061 0.2491 0.0248  -0.0188 0.0377  71  THR   A CB  
1551 O  OG1 . THR   A 71  ? 0.1993 0.2239 0.2606 0.0123  -0.0358 0.0314  71  THR   A OG1 
1552 C  CG2 . THR   A 71  ? 0.1873 0.2245 0.2755 0.0301  -0.0299 0.0529  71  THR   A CG2 
1560 N  N   . ASN   A 72  ? 0.1379 0.1525 0.2289 0.0143  0.0333  0.0243  72  ASN   A N   
1561 C  CA  . ASN   A 72  ? 0.1440 0.1538 0.2255 0.0182  0.0399  0.0226  72  ASN   A CA  
1562 C  C   . ASN   A 72  ? 0.1559 0.1532 0.2214 0.0119  0.0513  0.0116  72  ASN   A C   
1563 O  O   . ASN   A 72  ? 0.1718 0.1536 0.2564 0.0164  0.0475  0.0046  72  ASN   A O   
1564 C  CB  . ASN   A 72  ? 0.1638 0.1610 0.2260 0.0141  0.0408  0.0248  72  ASN   A CB  
1565 C  CG  . ASN   A 72  ? 0.1858 0.1717 0.2320 0.0256  0.0360  0.0313  72  ASN   A CG  
1566 O  OD1 . ASN   A 72  ? 0.2026 0.2112 0.2468 0.0259  0.0417  0.0282  72  ASN   A OD1 
1567 N  ND2 . ASN   A 72  ? 0.2017 0.1714 0.2308 0.0498  0.0153  0.0211  72  ASN   A ND2 
1574 N  N   . GLY   A 73  ? 0.1605 0.1451 0.1972 0.0037  0.0470  0.0129  73  GLY   A N   
1575 C  CA  . GLY   A 73  ? 0.1639 0.1456 0.1885 -0.0053 0.0399  0.0058  73  GLY   A CA  
1576 C  C   . GLY   A 73  ? 0.1625 0.1371 0.1783 0.0018  0.0497  0.0246  73  GLY   A C   
1577 O  O   . GLY   A 73  ? 0.1616 0.1409 0.1922 0.0071  0.0367  0.0267  73  GLY   A O   
1581 N  N   . PRO   A 74  ? 0.1696 0.1394 0.1861 -0.0080 0.0466  0.0172  74  PRO   A N   
1582 C  CA  . PRO   A 74  ? 0.1681 0.1405 0.1911 -0.0015 0.0451  0.0187  74  PRO   A CA  
1583 C  C   . PRO   A 74  ? 0.1606 0.1247 0.1872 0.0011  0.0330  0.0076  74  PRO   A C   
1584 O  O   . PRO   A 74  ? 0.1688 0.1296 0.2077 0.0029  0.0346  0.0008  74  PRO   A O   
1585 C  CB  . PRO   A 74  ? 0.1809 0.1699 0.2110 0.0021  0.0488  0.0296  74  PRO   A CB  
1586 C  CG  . PRO   A 74  ? 0.2044 0.2000 0.2654 -0.0137 0.0398  0.0222  74  PRO   A CG  
1587 C  CD  . PRO   A 74  ? 0.1891 0.1802 0.2092 -0.0166 0.0420  0.0114  74  PRO   A CD  
1595 N  N   . LEU   A 75  ? 0.1594 0.1195 0.1673 0.0021  0.0284  0.0116  75  LEU   A N   
1596 C  CA  . LEU   A 75  ? 0.1600 0.1202 0.1469 -0.0019 0.0126  0.0124  75  LEU   A CA  
1597 C  C   . LEU   A 75  ? 0.1735 0.1309 0.1573 0.0072  0.0096  0.0131  75  LEU   A C   
1598 O  O   . LEU   A 75  ? 0.2041 0.1505 0.1539 0.0126  0.0080  0.0066  75  LEU   A O   
1599 C  CB  . LEU   A 75  ? 0.1638 0.1301 0.1462 -0.0072 0.0073  0.0204  75  LEU   A CB  
1600 C  CG  . LEU   A 75  ? 0.1780 0.1692 0.1537 -0.0322 0.0107  0.0144  75  LEU   A CG  
1601 C  CD1 . LEU   A 75  ? 0.1882 0.2157 0.1792 -0.0391 0.0118  -0.0035 75  LEU   A CD1 
1602 C  CD2 . LEU   A 75  ? 0.2025 0.2085 0.2017 -0.0125 0.0139  0.0148  75  LEU   A CD2 
1614 N  N   . LYS   A 76  ? 0.1705 0.1300 0.1655 -0.0019 0.0099  0.0019  76  LYS   A N   
1615 C  CA  . LYS   A 76  ? 0.1660 0.1517 0.1676 -0.0043 0.0154  -0.0068 76  LYS   A CA  
1616 C  C   . LYS   A 76  ? 0.1614 0.1340 0.1433 0.0006  0.0098  0.0019  76  LYS   A C   
1617 O  O   . LYS   A 76  ? 0.1619 0.1274 0.1491 0.0009  0.0158  0.0101  76  LYS   A O   
1618 C  CB  . LYS   A 76  ? 0.1655 0.1721 0.2014 0.0069  0.0146  -0.0270 76  LYS   A CB  
1619 C  CG  . LYS   A 76  ? 0.1748 0.1681 0.2468 0.0111  0.0042  -0.0260 76  LYS   A CG  
1620 C  CD  . LYS   A 76  ? 0.1855 0.1704 0.2991 0.0109  -0.0055 -0.0337 76  LYS   A CD  
1621 C  CE  . LYS   A 76  ? 0.2034 0.1895 0.3566 -0.0006 0.0051  -0.0420 76  LYS   A CE  
1622 N  NZ  . LYS   A 76  ? 0.2055 0.1862 0.3964 -0.0209 -0.0006 -0.0493 76  LYS   A NZ  
1636 N  N   . VAL   A 77  ? 0.1709 0.1418 0.1438 -0.0003 0.0220  0.0122  77  VAL   A N   
1637 C  CA  . VAL   A 77  ? 0.1689 0.1421 0.1403 0.0031  0.0176  0.0127  77  VAL   A CA  
1638 C  C   . VAL   A 77  ? 0.1630 0.1354 0.1405 0.0079  0.0121  0.0024  77  VAL   A C   
1639 O  O   . VAL   A 77  ? 0.1693 0.1400 0.1437 0.0081  0.0243  -0.0006 77  VAL   A O   
1640 C  CB  . VAL   A 77  ? 0.1791 0.1608 0.1541 0.0035  0.0110  0.0232  77  VAL   A CB  
1641 C  CG1 . VAL   A 77  ? 0.1759 0.1765 0.1748 0.0180  -0.0025 0.0141  77  VAL   A CG1 
1642 C  CG2 . VAL   A 77  ? 0.2033 0.1773 0.1825 -0.0011 -0.0003 0.0318  77  VAL   A CG2 
1652 N  N   . GLY   A 78  ? 0.1600 0.1318 0.1414 0.0047  0.0212  0.0061  78  GLY   A N   
1653 C  CA  . GLY   A 78  ? 0.1577 0.1275 0.1530 0.0052  0.0221  0.0167  78  GLY   A CA  
1654 C  C   . GLY   A 78  ? 0.1421 0.1234 0.1484 0.0069  0.0189  0.0120  78  GLY   A C   
1655 O  O   . GLY   A 78  ? 0.1386 0.1301 0.1719 0.0019  0.0171  0.0243  78  GLY   A O   
1659 N  N   . GLY   A 79  ? 0.1470 0.1213 0.1481 -0.0006 0.0141  0.0154  79  GLY   A N   
1660 C  CA  . GLY   A 79  ? 0.1438 0.1288 0.1584 -0.0004 0.0134  0.0117  79  GLY   A CA  
1661 C  C   . GLY   A 79  ? 0.1269 0.1265 0.1451 0.0023  0.0139  0.0079  79  GLY   A C   
1662 O  O   . GLY   A 79  ? 0.1333 0.1311 0.1617 0.0153  0.0111  0.0098  79  GLY   A O   
1666 N  N   . SER   A 80  ? 0.1250 0.1380 0.1712 -0.0014 0.0155  0.0050  80  SER   A N   
1667 C  CA  . SER   A 80  ? 0.1225 0.1301 0.1614 -0.0015 0.0086  0.0111  80  SER   A CA  
1668 C  C   . SER   A 80  ? 0.1180 0.1351 0.1617 -0.0060 0.0091  0.0120  80  SER   A C   
1669 O  O   . SER   A 80  ? 0.1209 0.1511 0.2019 0.0052  0.0138  -0.0000 80  SER   A O   
1670 C  CB  . SER   A 80  ? 0.1378 0.1289 0.1888 -0.0041 0.0049  0.0112  80  SER   A CB  
1671 O  OG  . SER   A 80  ? 0.1599 0.1304 0.2199 0.0055  -0.0038 0.0199  80  SER   A OG  
1677 N  N   . CYS   A 81  ? 0.1154 0.1279 0.1563 0.0013  -0.0004 0.0136  81  CYS   A N   
1678 C  CA  . CYS   A 81  ? 0.1154 0.1385 0.1508 -0.0052 -0.0071 0.0197  81  CYS   A CA  
1679 C  C   . CYS   A 81  ? 0.1209 0.1330 0.1435 -0.0102 -0.0074 0.0263  81  CYS   A C   
1680 O  O   . CYS   A 81  ? 0.1178 0.1609 0.1649 -0.0027 0.0021  0.0330  81  CYS   A O   
1681 C  CB  . CYS   A 81  ? 0.1217 0.1474 0.1712 -0.0111 -0.0033 0.0271  81  CYS   A CB  
1682 S  SG  . CYS   A 81  ? 0.1371 0.1311 0.1787 -0.0132 0.0022  0.0178  81  CYS   A SG  
1688 N  N   . VAL   A 82  ? 0.1280 0.1401 0.1451 -0.0042 -0.0115 0.0209  82  VAL   A N   
1689 C  CA  . VAL   A 82  ? 0.1380 0.1446 0.1480 0.0001  -0.0118 0.0284  82  VAL   A CA  
1690 C  C   . VAL   A 82  ? 0.1324 0.1464 0.1631 -0.0010 -0.0048 0.0254  82  VAL   A C   
1691 O  O   . VAL   A 82  ? 0.1264 0.1545 0.1866 -0.0007 -0.0054 0.0052  82  VAL   A O   
1692 C  CB  . VAL   A 82  ? 0.1651 0.1540 0.1720 -0.0020 -0.0034 0.0352  82  VAL   A CB  
1693 C  CG1 . VAL   A 82  ? 0.1832 0.1669 0.1892 0.0059  0.0031  0.0316  82  VAL   A CG1 
1694 C  CG2 . VAL   A 82  ? 0.1751 0.1556 0.1967 -0.0069 -0.0091 0.0367  82  VAL   A CG2 
1704 N  N   . LEU   A 83  ? 0.1277 0.1410 0.1494 -0.0101 -0.0090 0.0164  83  LEU   A N   
1705 C  CA  . LEU   A 83  ? 0.1330 0.1431 0.1391 -0.0093 -0.0111 0.0149  83  LEU   A CA  
1706 C  C   . LEU   A 83  ? 0.1399 0.1469 0.1373 -0.0106 -0.0131 0.0166  83  LEU   A C   
1707 O  O   . LEU   A 83  ? 0.1451 0.1508 0.1530 -0.0138 -0.0080 0.0277  83  LEU   A O   
1708 C  CB  . LEU   A 83  ? 0.1420 0.1518 0.1465 -0.0095 -0.0107 0.0158  83  LEU   A CB  
1709 C  CG  . LEU   A 83  ? 0.1516 0.1624 0.1502 -0.0155 0.0019  0.0094  83  LEU   A CG  
1710 C  CD1 . LEU   A 83  ? 0.1659 0.1587 0.1525 -0.0321 0.0010  0.0234  83  LEU   A CD1 
1711 C  CD2 . LEU   A 83  ? 0.1481 0.1768 0.1655 -0.0148 0.0151  0.0171  83  LEU   A CD2 
1723 N  N   . SER   A 84  ? 0.1513 0.1515 0.1472 -0.0139 -0.0149 0.0187  84  SER   A N   
1724 C  CA  . SER   A 84  ? 0.1603 0.1581 0.1367 -0.0157 -0.0185 0.0192  84  SER   A CA  
1725 C  C   . SER   A 84  ? 0.1672 0.1541 0.1231 -0.0237 0.0025  0.0135  84  SER   A C   
1726 O  O   . SER   A 84  ? 0.1578 0.1681 0.1319 -0.0136 -0.0033 0.0076  84  SER   A O   
1727 C  CB  . SER   A 84  ? 0.1621 0.1835 0.1501 -0.0155 -0.0162 0.0060  84  SER   A CB  
1728 O  OG  . SER   A 84  ? 0.1692 0.2063 0.1583 -0.0133 -0.0189 -0.0009 84  SER   A OG  
1734 N  N   . GLY   A 85  ? 0.1769 0.1671 0.1386 -0.0214 0.0074  0.0139  85  GLY   A N   
1735 C  CA  . GLY   A 85  ? 0.1769 0.1742 0.1494 -0.0245 0.0125  0.0026  85  GLY   A CA  
1736 C  C   . GLY   A 85  ? 0.1718 0.1844 0.1375 -0.0210 0.0024  0.0024  85  GLY   A C   
1737 O  O   . GLY   A 85  ? 0.1718 0.1944 0.1470 -0.0267 0.0099  -0.0090 85  GLY   A O   
1741 N  N   . HIS   A 86  ? 0.1758 0.1788 0.1329 -0.0206 -0.0058 0.0000  86  HIS   A N   
1742 C  CA  . HIS   A 86  ? 0.1920 0.1841 0.1277 -0.0237 -0.0005 0.0052  86  HIS   A CA  
1743 C  C   . HIS   A 86  ? 0.2163 0.2008 0.1163 -0.0222 -0.0034 0.0040  86  HIS   A C   
1744 O  O   . HIS   A 86  ? 0.2263 0.2298 0.1245 -0.0177 0.0045  0.0034  86  HIS   A O   
1745 C  CB  . HIS   A 86  ? 0.1918 0.1731 0.1344 -0.0210 0.0019  0.0049  86  HIS   A CB  
1746 C  CG  . HIS   A 86  ? 0.1882 0.1722 0.1485 -0.0132 0.0064  0.0137  86  HIS   A CG  
1747 N  ND1 . HIS   A 86  ? 0.1932 0.1725 0.1798 -0.0218 0.0021  0.0113  86  HIS   A ND1 
1748 C  CD2 . HIS   A 86  ? 0.1878 0.1660 0.1429 0.0010  0.0127  0.0161  86  HIS   A CD2 
1749 C  CE1 . HIS   A 86  ? 0.1916 0.1714 0.1803 -0.0172 0.0189  0.0188  86  HIS   A CE1 
1750 N  NE2 . HIS   A 86  ? 0.1862 0.1657 0.1568 0.0000  0.0200  0.0257  86  HIS   A NE2 
1758 N  N   . ASN   A 87  ? 0.2295 0.2046 0.1309 -0.0178 0.0160  -0.0081 87  ASN   A N   
1759 C  CA  . ASN   A 87  ? 0.2492 0.2148 0.1373 -0.0155 0.0342  -0.0143 87  ASN   A CA  
1760 C  C   . ASN   A 87  ? 0.2480 0.2279 0.1699 -0.0214 0.0555  -0.0093 87  ASN   A C   
1761 O  O   . ASN   A 87  ? 0.2746 0.2478 0.2191 -0.0342 0.0918  -0.0149 87  ASN   A O   
1762 C  CB  . ASN   A 87  ? 0.2675 0.2248 0.1538 -0.0061 0.0406  -0.0149 87  ASN   A CB  
1763 C  CG  . ASN   A 87  ? 0.2828 0.2374 0.1624 0.0046  0.0569  -0.0096 87  ASN   A CG  
1764 O  OD1 . ASN   A 87  ? 0.2987 0.2323 0.1719 0.0215  0.0534  0.0011  87  ASN   A OD1 
1765 N  ND2 . ASN   A 87  ? 0.2861 0.2623 0.1766 0.0018  0.0644  -0.0004 87  ASN   A ND2 
1772 N  N   . LEU   A 88  ? 0.2188 0.2213 0.1652 -0.0249 0.0313  0.0095  88  LEU   A N   
1773 C  CA  . LEU   A 88  ? 0.1955 0.2176 0.1789 -0.0299 0.0296  0.0182  88  LEU   A CA  
1774 C  C   . LEU   A 88  ? 0.1876 0.2192 0.1753 -0.0298 0.0261  0.0322  88  LEU   A C   
1775 O  O   . LEU   A 88  ? 0.1904 0.2257 0.2069 -0.0269 0.0312  0.0489  88  LEU   A O   
1776 C  CB  . LEU   A 88  ? 0.1994 0.2259 0.1851 -0.0376 -0.0004 0.0270  88  LEU   A CB  
1777 C  CG  . LEU   A 88  ? 0.2167 0.2446 0.2206 -0.0403 -0.0119 0.0271  88  LEU   A CG  
1778 C  CD1 . LEU   A 88  ? 0.2259 0.2554 0.2255 -0.0456 -0.0140 0.0150  88  LEU   A CD1 
1779 C  CD2 . LEU   A 88  ? 0.2334 0.2558 0.2569 -0.0320 -0.0081 0.0177  88  LEU   A CD2 
1791 N  N   . ALA   A 89  ? 0.1866 0.2107 0.1533 -0.0311 0.0131  0.0101  89  ALA   A N   
1792 C  CA  . ALA   A 89  ? 0.1930 0.2091 0.1371 -0.0238 0.0086  0.0248  89  ALA   A CA  
1793 C  C   . ALA   A 89  ? 0.2029 0.2113 0.1407 -0.0173 -0.0037 0.0236  89  ALA   A C   
1794 O  O   . ALA   A 89  ? 0.2034 0.2117 0.1760 -0.0272 -0.0109 -0.0066 89  ALA   A O   
1795 C  CB  . ALA   A 89  ? 0.1865 0.2052 0.1268 -0.0280 0.0071  0.0203  89  ALA   A CB  
1801 N  N   . LYS   A 90  ? 0.2111 0.2241 0.1424 -0.0234 -0.0193 0.0247  90  LYS   A N   
1802 C  CA  . LYS   A 90  ? 0.2183 0.2393 0.1429 -0.0212 -0.0304 0.0219  90  LYS   A CA  
1803 C  C   . LYS   A 90  ? 0.1942 0.2241 0.1446 -0.0218 -0.0281 0.0148  90  LYS   A C   
1804 O  O   . LYS   A 90  ? 0.1969 0.2432 0.1775 -0.0277 -0.0310 0.0058  90  LYS   A O   
1805 C  CB  . LYS   A 90  ? 0.2455 0.2758 0.1836 -0.0174 -0.0369 0.0472  90  LYS   A CB  
1806 C  CG  . LYS   A 90  ? 0.2893 0.3144 0.2858 -0.0178 -0.0316 0.0621  90  LYS   A CG  
1807 C  CD  . LYS   A 90  ? 0.3399 0.3524 0.3898 -0.0234 -0.0176 0.0666  90  LYS   A CD  
1808 C  CE  . LYS   A 90  ? 0.3825 0.3912 0.4633 -0.0261 -0.0075 0.0660  90  LYS   A CE  
1809 N  NZ  . LYS   A 90  ? 0.4120 0.4113 0.5175 -0.0271 -0.0029 0.0680  90  LYS   A NZ  
1823 N  N   . HIS   A 91  ? 0.1837 0.1975 0.1224 -0.0189 -0.0261 0.0171  91  HIS   A N   
1824 C  CA  . HIS   A 91  ? 0.1741 0.1822 0.1279 -0.0162 -0.0201 0.0221  91  HIS   A CA  
1825 C  C   . HIS   A 91  ? 0.1508 0.1672 0.1116 -0.0157 -0.0121 0.0250  91  HIS   A C   
1826 O  O   . HIS   A 91  ? 0.1449 0.1799 0.1438 -0.0180 0.0004  0.0236  91  HIS   A O   
1827 C  CB  . HIS   A 91  ? 0.1954 0.2091 0.1761 0.0058  -0.0329 0.0246  91  HIS   A CB  
1828 C  CG  . HIS   A 91  ? 0.2396 0.2568 0.2325 0.0185  -0.0638 0.0117  91  HIS   A CG  
1829 N  ND1 . HIS   A 91  ? 0.2526 0.2850 0.2740 0.0267  -0.0701 -0.0064 91  HIS   A ND1 
1830 C  CD2 . HIS   A 91  ? 0.2668 0.2792 0.2533 0.0268  -0.0799 0.0218  91  HIS   A CD2 
1831 C  CE1 . HIS   A 91  ? 0.2664 0.2954 0.2810 0.0316  -0.0735 0.0079  91  HIS   A CE1 
1832 N  NE2 . HIS   A 91  ? 0.2784 0.2937 0.2744 0.0351  -0.0835 0.0169  91  HIS   A NE2 
1840 N  N   . CYS   A 92  ? 0.1420 0.1603 0.1263 -0.0186 -0.0082 0.0221  92  CYS   A N   
1841 C  CA  . CYS   A 92  ? 0.1347 0.1488 0.1300 -0.0116 -0.0030 0.0183  92  CYS   A CA  
1842 C  C   . CYS   A 92  ? 0.1279 0.1421 0.1326 -0.0108 0.0049  0.0200  92  CYS   A C   
1843 O  O   . CYS   A 92  ? 0.1323 0.1469 0.1485 -0.0168 -0.0032 0.0173  92  CYS   A O   
1844 C  CB  . CYS   A 92  ? 0.1324 0.1471 0.1562 -0.0089 -0.0071 0.0171  92  CYS   A CB  
1845 S  SG  . CYS   A 92  ? 0.1362 0.1378 0.1497 -0.0123 -0.0044 0.0158  92  CYS   A SG  
1851 N  N   . LEU   A 93  ? 0.1260 0.1272 0.1363 -0.0128 0.0075  0.0187  93  LEU   A N   
1852 C  CA  . LEU   A 93  ? 0.1158 0.1278 0.1418 -0.0052 0.0010  0.0143  93  LEU   A CA  
1853 C  C   . LEU   A 93  ? 0.1140 0.1171 0.1314 -0.0000 0.0055  0.0146  93  LEU   A C   
1854 O  O   . LEU   A 93  ? 0.1123 0.1246 0.1389 -0.0026 -0.0005 0.0164  93  LEU   A O   
1855 C  CB  . LEU   A 93  ? 0.1263 0.1265 0.1506 -0.0102 -0.0065 0.0244  93  LEU   A CB  
1856 C  CG  . LEU   A 93  ? 0.1329 0.1272 0.1452 -0.0074 -0.0042 0.0236  93  LEU   A CG  
1857 C  CD1 . LEU   A 93  ? 0.1388 0.1356 0.1749 -0.0066 0.0035  0.0166  93  LEU   A CD1 
1858 C  CD2 . LEU   A 93  ? 0.1452 0.1271 0.1719 -0.0110 -0.0015 0.0163  93  LEU   A CD2 
1870 N  N   . HIS   A 94  ? 0.1108 0.1151 0.1386 0.0002  0.0054  0.0190  94  HIS   A N   
1871 C  CA  . HIS   A 94  ? 0.1120 0.1173 0.1386 -0.0013 0.0032  0.0179  94  HIS   A CA  
1872 C  C   . HIS   A 94  ? 0.1086 0.1174 0.1393 -0.0081 0.0007  0.0149  94  HIS   A C   
1873 O  O   . HIS   A 94  ? 0.1130 0.1369 0.1753 -0.0015 -0.0009 -0.0006 94  HIS   A O   
1874 C  CB  . HIS   A 94  ? 0.1129 0.1163 0.1458 -0.0046 -0.0039 0.0166  94  HIS   A CB  
1875 C  CG  . HIS   A 94  ? 0.1170 0.1164 0.1349 -0.0044 -0.0000 0.0161  94  HIS   A CG  
1876 N  ND1 . HIS   A 94  ? 0.1187 0.1167 0.1440 -0.0029 -0.0006 0.0175  94  HIS   A ND1 
1877 C  CD2 . HIS   A 94  ? 0.1255 0.1269 0.1457 -0.0068 -0.0017 0.0078  94  HIS   A CD2 
1878 C  CE1 . HIS   A 94  ? 0.1191 0.1217 0.1482 -0.0103 -0.0084 0.0063  94  HIS   A CE1 
1879 N  NE2 . HIS   A 94  ? 0.1267 0.1236 0.1430 -0.0114 -0.0093 0.0070  94  HIS   A NE2 
1887 N  N   . VAL   A 95  ? 0.1068 0.1105 0.1277 -0.0015 0.0082  0.0078  95  VAL   A N   
1888 C  CA  . VAL   A 95  ? 0.1182 0.1151 0.1206 -0.0048 0.0084  0.0113  95  VAL   A CA  
1889 C  C   . VAL   A 95  ? 0.1194 0.1180 0.1118 -0.0117 0.0033  0.0077  95  VAL   A C   
1890 O  O   . VAL   A 95  ? 0.1198 0.1260 0.1356 0.0101  0.0047  0.0076  95  VAL   A O   
1891 C  CB  . VAL   A 95  ? 0.1233 0.1201 0.1477 -0.0099 0.0057  0.0128  95  VAL   A CB  
1892 C  CG1 . VAL   A 95  ? 0.1334 0.1204 0.1548 -0.0132 0.0030  0.0045  95  VAL   A CG1 
1893 C  CG2 . VAL   A 95  ? 0.1190 0.1230 0.1496 -0.0124 0.0057  0.0210  95  VAL   A CG2 
1903 N  N   . VAL   A 96  ? 0.1227 0.1157 0.1163 -0.0033 0.0036  0.0193  96  VAL   A N   
1904 C  CA  . VAL   A 96  ? 0.1325 0.1177 0.1247 0.0009  0.0086  0.0164  96  VAL   A CA  
1905 C  C   . VAL   A 96  ? 0.1295 0.1256 0.1385 -0.0041 0.0083  0.0195  96  VAL   A C   
1906 O  O   . VAL   A 96  ? 0.1424 0.1274 0.1535 -0.0071 0.0113  0.0025  96  VAL   A O   
1907 C  CB  . VAL   A 96  ? 0.1348 0.1254 0.1357 -0.0008 0.0219  0.0145  96  VAL   A CB  
1908 C  CG1 . VAL   A 96  ? 0.1417 0.1313 0.1283 0.0034  0.0114  0.0122  96  VAL   A CG1 
1909 C  CG2 . VAL   A 96  ? 0.1359 0.1314 0.1562 -0.0095 0.0136  0.0181  96  VAL   A CG2 
1919 N  N   A GLY   A 97  ? 0.1307 0.1298 0.1443 -0.0063 0.0063  0.0118  97  GLY   A N   
1920 N  N   B GLY   A 97  ? 0.1330 0.1319 0.1314 -0.0063 0.0037  0.0131  97  GLY   A N   
1921 C  CA  A GLY   A 97  ? 0.1432 0.1442 0.1443 -0.0047 -0.0004 0.0130  97  GLY   A CA  
1922 C  CA  B GLY   A 97  ? 0.1439 0.1414 0.1247 -0.0046 -0.0004 0.0158  97  GLY   A CA  
1923 C  C   A GLY   A 97  ? 0.1431 0.1522 0.1315 -0.0049 0.0031  0.0144  97  GLY   A C   
1924 C  C   B GLY   A 97  ? 0.1469 0.1451 0.1213 -0.0026 0.0022  0.0207  97  GLY   A C   
1925 O  O   A GLY   A 97  ? 0.1520 0.1476 0.1517 -0.0001 0.0006  0.0107  97  GLY   A O   
1926 O  O   B GLY   A 97  ? 0.1522 0.1472 0.1220 -0.0025 0.0096  0.0184  97  GLY   A O   
1933 N  N   A PRO   A 98  ? 0.1496 0.1568 0.1081 -0.0010 0.0003  0.0131  98  PRO   A N   
1934 N  N   B PRO   A 98  ? 0.1610 0.1442 0.1309 0.0016  -0.0027 0.0221  98  PRO   A N   
1935 C  CA  A PRO   A 98  ? 0.1579 0.1666 0.1003 -0.0002 0.0063  0.0086  98  PRO   A CA  
1936 C  CA  B PRO   A 98  ? 0.1791 0.1506 0.1374 0.0039  -0.0059 0.0094  98  PRO   A CA  
1937 C  C   A PRO   A 98  ? 0.1515 0.1699 0.1051 -0.0087 0.0054  0.0107  98  PRO   A C   
1938 C  C   B PRO   A 98  ? 0.1930 0.1443 0.1327 0.0002  -0.0102 0.0200  98  PRO   A C   
1939 O  O   A PRO   A 98  ? 0.1441 0.1607 0.1347 -0.0092 0.0070  0.0103  98  PRO   A O   
1940 O  O   B PRO   A 98  ? 0.1907 0.1426 0.1712 0.0016  0.0012  0.0195  98  PRO   A O   
1941 C  CB  A PRO   A 98  ? 0.1750 0.1748 0.0847 0.0088  -0.0011 -0.0029 98  PRO   A CB  
1942 C  CB  B PRO   A 98  ? 0.1853 0.1463 0.1348 0.0091  -0.0052 0.0167  98  PRO   A CB  
1943 C  CG  A PRO   A 98  ? 0.1746 0.1732 0.1146 0.0074  -0.0023 -0.0011 98  PRO   A CG  
1944 C  CG  B PRO   A 98  ? 0.1833 0.1436 0.1406 0.0029  -0.0013 0.0218  98  PRO   A CG  
1945 C  CD  A PRO   A 98  ? 0.1605 0.1604 0.1207 -0.0002 -0.0014 0.0123  98  PRO   A CD  
1946 C  CD  B PRO   A 98  ? 0.1709 0.1403 0.1268 -0.0001 0.0002  0.0272  98  PRO   A CD  
1961 N  N   A ASN   A 99  ? 0.1559 0.1886 0.1013 -0.0047 0.0129  0.0181  99  ASN   A N   
1962 N  N   B ASN   A 99  ? 0.2153 0.1435 0.1147 0.0029  -0.0154 0.0223  99  ASN   A N   
1963 C  CA  A ASN   A 99  ? 0.1744 0.2021 0.0939 -0.0046 0.0161  0.0194  99  ASN   A CA  
1964 C  CA  B ASN   A 99  ? 0.2428 0.1488 0.1209 0.0124  -0.0204 0.0356  99  ASN   A CA  
1965 C  C   A ASN   A 99  ? 0.1921 0.2279 0.1079 -0.0133 0.0147  0.0200  99  ASN   A C   
1966 C  C   B ASN   A 99  ? 0.2559 0.1565 0.1115 0.0103  -0.0268 0.0448  99  ASN   A C   
1967 O  O   A ASN   A 99  ? 0.2042 0.2487 0.1232 -0.0035 0.0024  0.0114  99  ASN   A O   
1968 O  O   B ASN   A 99  ? 0.2573 0.1446 0.1045 0.0153  -0.0281 0.0302  99  ASN   A O   
1969 C  CB  A ASN   A 99  ? 0.1753 0.1959 0.1006 -0.0092 0.0033  0.0250  99  ASN   A CB  
1970 C  CB  B ASN   A 99  ? 0.2546 0.1492 0.1520 0.0209  -0.0269 0.0381  99  ASN   A CB  
1971 C  CG  A ASN   A 99  ? 0.1758 0.1934 0.1152 -0.0056 -0.0058 0.0138  99  ASN   A CG  
1972 C  CG  B ASN   A 99  ? 0.2657 0.1596 0.1797 0.0231  -0.0303 0.0380  99  ASN   A CG  
1973 O  OD1 A ASN   A 99  ? 0.1814 0.2059 0.1272 0.0047  -0.0096 0.0024  99  ASN   A OD1 
1974 O  OD1 B ASN   A 99  ? 0.2685 0.1651 0.1822 0.0252  -0.0354 0.0497  99  ASN   A OD1 
1975 N  ND2 A ASN   A 99  ? 0.1781 0.1904 0.1185 -0.0066 -0.0160 0.0170  99  ASN   A ND2 
1976 N  ND2 B ASN   A 99  ? 0.2710 0.1677 0.1984 0.0313  -0.0354 0.0219  99  ASN   A ND2 
1989 N  N   A VAL   A 100 ? 0.2034 0.2334 0.1100 -0.0283 -0.0072 0.0169  100 VAL   A N   
1990 N  N   B VAL   A 100 ? 0.2698 0.1902 0.1414 0.0038  -0.0318 0.0437  100 VAL   A N   
1991 C  CA  A VAL   A 100 ? 0.2300 0.2497 0.1316 -0.0335 -0.0216 0.0220  100 VAL   A CA  
1992 C  CA  B VAL   A 100 ? 0.2838 0.2157 0.1766 0.0007  -0.0391 0.0346  100 VAL   A CA  
1993 C  C   A VAL   A 100 ? 0.2382 0.2676 0.1186 -0.0419 -0.0197 0.0442  100 VAL   A C   
1994 C  C   B VAL   A 100 ? 0.2870 0.2270 0.1907 0.0070  -0.0453 0.0356  100 VAL   A C   
1995 O  O   A VAL   A 100 ? 0.2423 0.2753 0.1303 -0.0396 -0.0009 0.0421  100 VAL   A O   
1996 O  O   B VAL   A 100 ? 0.2869 0.2307 0.2021 0.0056  -0.0432 0.0239  100 VAL   A O   
1997 C  CB  A VAL   A 100 ? 0.2504 0.2477 0.1826 -0.0369 -0.0336 0.0123  100 VAL   A CB  
1998 C  CB  B VAL   A 100 ? 0.2935 0.2319 0.2077 -0.0035 -0.0376 0.0158  100 VAL   A CB  
1999 C  CG1 A VAL   A 100 ? 0.2530 0.2500 0.2019 -0.0372 -0.0276 0.0057  100 VAL   A CG1 
2000 C  CG1 B VAL   A 100 ? 0.2953 0.2297 0.2239 -0.0076 -0.0337 0.0104  100 VAL   A CG1 
2001 C  CG2 A VAL   A 100 ? 0.2625 0.2503 0.2003 -0.0407 -0.0377 0.0158  100 VAL   A CG2 
2002 C  CG2 B VAL   A 100 ? 0.2964 0.2415 0.2171 -0.0014 -0.0378 0.0082  100 VAL   A CG2 
2021 N  N   A ASN   A 101 ? 0.2488 0.2780 0.1494 -0.0465 -0.0280 0.0697  101 ASN   A N   
2022 N  N   B ASN   A 101 ? 0.2961 0.2392 0.2006 0.0113  -0.0493 0.0388  101 ASN   A N   
2023 C  CA  A ASN   A 101 ? 0.2717 0.2933 0.1718 -0.0491 -0.0249 0.0900  101 ASN   A CA  
2024 C  CA  B ASN   A 101 ? 0.3081 0.2536 0.2248 0.0183  -0.0447 0.0425  101 ASN   A CA  
2025 C  C   A ASN   A 101 ? 0.3011 0.3257 0.1960 -0.0535 -0.0029 0.1101  101 ASN   A C   
2026 C  C   B ASN   A 101 ? 0.3243 0.2730 0.2364 0.0181  -0.0266 0.0556  101 ASN   A C   
2027 O  O   A ASN   A 101 ? 0.3166 0.3326 0.2268 -0.0556 -0.0031 0.0991  101 ASN   A O   
2028 O  O   B ASN   A 101 ? 0.3300 0.2760 0.2393 0.0163  -0.0280 0.0633  101 ASN   A O   
2029 C  CB  A ASN   A 101 ? 0.2666 0.2760 0.1650 -0.0452 -0.0442 0.0824  101 ASN   A CB  
2030 C  CB  B ASN   A 101 ? 0.3028 0.2502 0.2344 0.0205  -0.0534 0.0331  101 ASN   A CB  
2031 C  CG  A ASN   A 101 ? 0.2626 0.2648 0.1676 -0.0403 -0.0576 0.0530  101 ASN   A CG  
2032 C  CG  B ASN   A 101 ? 0.2989 0.2529 0.2542 0.0203  -0.0625 0.0223  101 ASN   A CG  
2033 O  OD1 A ASN   A 101 ? 0.2539 0.2664 0.1814 -0.0250 -0.0558 0.0220  101 ASN   A OD1 
2034 O  OD1 B ASN   A 101 ? 0.3042 0.2609 0.2740 0.0142  -0.0603 0.0205  101 ASN   A OD1 
2035 N  ND2 A ASN   A 101 ? 0.2664 0.2585 0.1617 -0.0478 -0.0613 0.0531  101 ASN   A ND2 
2036 N  ND2 B ASN   A 101 ? 0.2942 0.2472 0.2629 0.0255  -0.0647 0.0127  101 ASN   A ND2 
2049 N  N   A LYS   A 102 ? 0.3088 0.3537 0.2222 -0.0569 0.0086  0.1153  102 LYS   A N   
2050 N  N   B LYS   A 102 ? 0.3318 0.2895 0.2652 0.0188  -0.0054 0.0516  102 LYS   A N   
2051 C  CA  A LYS   A 102 ? 0.3229 0.3818 0.2419 -0.0536 0.0050  0.1025  102 LYS   A CA  
2052 C  CA  B LYS   A 102 ? 0.3406 0.3071 0.2724 0.0128  0.0114  0.0466  102 LYS   A CA  
2053 C  C   A LYS   A 102 ? 0.3299 0.4026 0.2329 -0.0369 0.0056  0.0928  102 LYS   A C   
2054 C  C   B LYS   A 102 ? 0.3428 0.3117 0.2635 0.0167  0.0106  0.0589  102 LYS   A C   
2055 O  O   A LYS   A 102 ? 0.3305 0.4126 0.2420 -0.0317 0.0073  0.0898  102 LYS   A O   
2056 O  O   B LYS   A 102 ? 0.3455 0.3120 0.2638 0.0191  0.0162  0.0698  102 LYS   A O   
2057 C  CB  A LYS   A 102 ? 0.3344 0.3892 0.2845 -0.0648 -0.0072 0.0878  102 LYS   A CB  
2058 C  CB  B LYS   A 102 ? 0.3471 0.3192 0.3030 0.0060  0.0174  0.0291  102 LYS   A CB  
2059 C  CG  A LYS   A 102 ? 0.3460 0.3958 0.3213 -0.0731 -0.0219 0.0722  102 LYS   A CG  
2060 C  CG  B LYS   A 102 ? 0.3543 0.3316 0.3250 -0.0003 0.0202  0.0124  102 LYS   A CG  
2061 C  CD  A LYS   A 102 ? 0.3579 0.4014 0.3605 -0.0767 -0.0301 0.0535  102 LYS   A CD  
2062 C  CD  B LYS   A 102 ? 0.3635 0.3456 0.3526 -0.0038 0.0224  -0.0047 102 LYS   A CD  
2063 C  CE  A LYS   A 102 ? 0.3664 0.4043 0.3942 -0.0766 -0.0374 0.0426  102 LYS   A CE  
2064 C  CE  B LYS   A 102 ? 0.3713 0.3574 0.3732 -0.0049 0.0212  -0.0171 102 LYS   A CE  
2065 N  NZ  A LYS   A 102 ? 0.3690 0.4043 0.4079 -0.0795 -0.0444 0.0352  102 LYS   A NZ  
2066 N  NZ  B LYS   A 102 ? 0.3763 0.3654 0.3867 -0.0042 0.0207  -0.0257 102 LYS   A NZ  
2093 N  N   A GLY   A 103 ? 0.3340 0.4142 0.2473 -0.0230 0.0002  0.0688  103 GLY   A N   
2094 N  N   B GLY   A 103 ? 0.3404 0.3184 0.2514 0.0200  -0.0014 0.0511  103 GLY   A N   
2095 C  CA  A GLY   A 103 ? 0.3366 0.4219 0.2406 -0.0117 0.0030  0.0521  103 GLY   A CA  
2096 C  CA  B GLY   A 103 ? 0.3340 0.3182 0.2449 0.0249  -0.0096 0.0550  103 GLY   A CA  
2097 C  C   A GLY   A 103 ? 0.3333 0.4289 0.2447 -0.0035 0.0100  0.0390  103 GLY   A C   
2098 C  C   B GLY   A 103 ? 0.3212 0.3153 0.2261 0.0289  -0.0149 0.0513  103 GLY   A C   
2099 O  O   A GLY   A 103 ? 0.3399 0.4365 0.2659 0.0048  0.0063  0.0315  103 GLY   A O   
2100 O  O   B GLY   A 103 ? 0.3281 0.3201 0.2314 0.0330  -0.0156 0.0513  103 GLY   A O   
2107 N  N   A GLU   A 104 ? 0.3186 0.4243 0.2147 -0.0082 0.0237  0.0337  104 GLU   A N   
2108 N  N   B GLU   A 104 ? 0.2982 0.3041 0.1989 0.0269  -0.0223 0.0532  104 GLU   A N   
2109 C  CA  A GLU   A 104 ? 0.3004 0.4165 0.1965 -0.0186 0.0292  0.0336  104 GLU   A CA  
2110 C  CA  B GLU   A 104 ? 0.2774 0.2923 0.1724 0.0203  -0.0274 0.0505  104 GLU   A CA  
2111 C  C   A GLU   A 104 ? 0.3058 0.4267 0.2030 -0.0148 0.0224  0.0056  104 GLU   A C   
2112 C  C   B GLU   A 104 ? 0.2659 0.2877 0.1796 0.0277  -0.0258 0.0353  104 GLU   A C   
2113 O  O   A GLU   A 104 ? 0.3025 0.4299 0.2110 -0.0145 0.0134  -0.0040 104 GLU   A O   
2114 O  O   B GLU   A 104 ? 0.2643 0.2826 0.1933 0.0271  -0.0297 0.0426  104 GLU   A O   
2115 C  CB  A GLU   A 104 ? 0.2711 0.3983 0.1839 -0.0333 0.0414  0.0613  104 GLU   A CB  
2116 C  CB  B GLU   A 104 ? 0.2723 0.2893 0.1689 0.0049  -0.0291 0.0563  104 GLU   A CB  
2117 C  CG  A GLU   A 104 ? 0.2468 0.3810 0.2002 -0.0438 0.0374  0.0769  104 GLU   A CG  
2118 C  CG  B GLU   A 104 ? 0.2744 0.2946 0.1855 -0.0081 -0.0383 0.0563  104 GLU   A CG  
2119 C  CD  A GLU   A 104 ? 0.2237 0.3637 0.1948 -0.0517 0.0340  0.0957  104 GLU   A CD  
2120 C  CD  B GLU   A 104 ? 0.2758 0.3014 0.1860 -0.0146 -0.0522 0.0577  104 GLU   A CD  
2121 O  OE1 A GLU   A 104 ? 0.1998 0.3483 0.1566 -0.0497 0.0174  0.1007  104 GLU   A OE1 
2122 O  OE1 B GLU   A 104 ? 0.2736 0.3060 0.1865 -0.0153 -0.0583 0.0530  104 GLU   A OE1 
2123 O  OE2 A GLU   A 104 ? 0.2342 0.3658 0.2243 -0.0615 0.0390  0.1057  104 GLU   A OE2 
2124 O  OE2 B GLU   A 104 ? 0.2850 0.3056 0.1937 -0.0203 -0.0540 0.0575  104 GLU   A OE2 
2137 N  N   A ASP   A 105 ? 0.3145 0.4327 0.2113 -0.0097 0.0234  -0.0137 105 ASP   A N   
2138 N  N   B ASP   A 105 ? 0.2656 0.2883 0.1957 0.0330  -0.0216 0.0178  105 ASP   A N   
2139 C  CA  A ASP   A 105 ? 0.3151 0.4395 0.2341 -0.0052 0.0276  -0.0367 105 ASP   A CA  
2140 C  CA  B ASP   A 105 ? 0.2618 0.2897 0.2151 0.0381  -0.0084 -0.0146 105 ASP   A CA  
2141 C  C   A ASP   A 105 ? 0.2854 0.4290 0.1973 -0.0191 0.0192  -0.0572 105 ASP   A C   
2142 C  C   B ASP   A 105 ? 0.2588 0.2803 0.1924 0.0267  -0.0066 -0.0259 105 ASP   A C   
2143 O  O   A ASP   A 105 ? 0.2755 0.4342 0.1553 -0.0193 0.0222  -0.0701 105 ASP   A O   
2144 O  O   B ASP   A 105 ? 0.2492 0.2737 0.1412 0.0243  -0.0019 -0.0316 105 ASP   A O   
2145 C  CB  A ASP   A 105 ? 0.3397 0.4554 0.2953 0.0115  0.0360  -0.0396 105 ASP   A CB  
2146 C  CB  B ASP   A 105 ? 0.2622 0.3022 0.2669 0.0524  0.0010  -0.0326 105 ASP   A CB  
2147 C  CG  A ASP   A 105 ? 0.3576 0.4703 0.3484 0.0246  0.0387  -0.0440 105 ASP   A CG  
2148 C  CG  B ASP   A 105 ? 0.2614 0.3113 0.3104 0.0646  0.0086  -0.0548 105 ASP   A CG  
2149 O  OD1 A ASP   A 105 ? 0.3605 0.4750 0.3565 0.0310  0.0428  -0.0534 105 ASP   A OD1 
2150 O  OD1 B ASP   A 105 ? 0.2622 0.3141 0.3129 0.0624  0.0062  -0.0640 105 ASP   A OD1 
2151 O  OD2 A ASP   A 105 ? 0.3660 0.4775 0.3850 0.0269  0.0361  -0.0383 105 ASP   A OD2 
2152 O  OD2 B ASP   A 105 ? 0.2599 0.3141 0.3301 0.0737  0.0123  -0.0590 105 ASP   A OD2 
2161 N  N   A ILE   A 106 ? 0.2629 0.4096 0.2073 -0.0334 -0.0018 -0.0682 106 ILE   A N   
2162 N  N   B ILE   A 106 ? 0.2640 0.2814 0.2153 0.0186  -0.0200 -0.0267 106 ILE   A N   
2163 C  CA  A ILE   A 106 ? 0.2349 0.3850 0.2204 -0.0479 -0.0223 -0.0889 106 ILE   A CA  
2164 C  CA  B ILE   A 106 ? 0.2673 0.2797 0.2366 0.0088  -0.0269 -0.0323 106 ILE   A CA  
2165 C  C   A ILE   A 106 ? 0.2098 0.3552 0.2243 -0.0698 -0.0296 -0.1127 106 ILE   A C   
2166 C  C   B ILE   A 106 ? 0.2687 0.2651 0.2415 0.0058  -0.0186 -0.0170 106 ILE   A C   
2167 O  O   A ILE   A 106 ? 0.1846 0.3425 0.2433 -0.0775 -0.0155 -0.1139 106 ILE   A O   
2168 O  O   B ILE   A 106 ? 0.2646 0.2676 0.2523 0.0024  -0.0144 -0.0147 106 ILE   A O   
2169 C  CB  A ILE   A 106 ? 0.2371 0.3879 0.2485 -0.0355 -0.0322 -0.0706 106 ILE   A CB  
2170 C  CB  B ILE   A 106 ? 0.2698 0.2948 0.2601 0.0021  -0.0383 -0.0447 106 ILE   A CB  
2171 C  CG1 A ILE   A 106 ? 0.2341 0.3826 0.2788 -0.0240 -0.0382 -0.0545 106 ILE   A CG1 
2172 C  CG1 B ILE   A 106 ? 0.2661 0.3008 0.2726 0.0035  -0.0396 -0.0488 106 ILE   A CG1 
2173 C  CG2 A ILE   A 106 ? 0.2413 0.3922 0.2589 -0.0322 -0.0353 -0.0666 106 ILE   A CG2 
2174 C  CG2 B ILE   A 106 ? 0.2743 0.3010 0.2611 -0.0023 -0.0423 -0.0501 106 ILE   A CG2 
2175 C  CD1 A ILE   A 106 ? 0.2313 0.3760 0.2848 -0.0150 -0.0400 -0.0431 106 ILE   A CD1 
2176 C  CD1 B ILE   A 106 ? 0.2617 0.3045 0.2839 0.0049  -0.0419 -0.0473 106 ILE   A CD1 
2199 N  N   A GLN   A 107 ? 0.2253 0.3410 0.2614 -0.0718 -0.0243 -0.1201 107 GLN   A N   
2200 N  N   B GLN   A 107 ? 0.2753 0.2466 0.2495 0.0085  -0.0136 -0.0034 107 GLN   A N   
2201 C  CA  A GLN   A 107 ? 0.2440 0.3205 0.3210 -0.0633 -0.0035 -0.1145 107 GLN   A CA  
2202 C  CA  B GLN   A 107 ? 0.2852 0.2420 0.2880 0.0035  -0.0108 0.0128  107 GLN   A CA  
2203 C  C   A GLN   A 107 ? 0.2213 0.2738 0.3140 -0.0575 0.0213  -0.0909 107 GLN   A C   
2204 C  C   B GLN   A 107 ? 0.2637 0.2101 0.2605 -0.0008 -0.0011 0.0249  107 GLN   A C   
2205 O  O   A GLN   A 107 ? 0.2323 0.2691 0.3700 -0.0527 0.0403  -0.0932 107 GLN   A O   
2206 O  O   B GLN   A 107 ? 0.2689 0.2032 0.2662 -0.0058 -0.0062 0.0221  107 GLN   A O   
2207 C  CB  A GLN   A 107 ? 0.2826 0.3457 0.4012 -0.0610 -0.0099 -0.1157 107 GLN   A CB  
2208 C  CB  B GLN   A 107 ? 0.3122 0.2738 0.3526 -0.0011 -0.0228 0.0157  107 GLN   A CB  
2209 C  CG  A GLN   A 107 ? 0.3187 0.3706 0.4862 -0.0544 -0.0198 -0.1066 107 GLN   A CG  
2210 C  CG  B GLN   A 107 ? 0.3363 0.3005 0.4151 -0.0036 -0.0368 0.0261  107 GLN   A CG  
2211 C  CD  A GLN   A 107 ? 0.3474 0.3887 0.5580 -0.0488 -0.0248 -0.0950 107 GLN   A CD  
2212 C  CD  B GLN   A 107 ? 0.3549 0.3219 0.4720 -0.0057 -0.0464 0.0371  107 GLN   A CD  
2213 O  OE1 A GLN   A 107 ? 0.3574 0.3963 0.5888 -0.0490 -0.0272 -0.0899 107 GLN   A OE1 
2214 O  OE1 B GLN   A 107 ? 0.3627 0.3273 0.4899 -0.0047 -0.0484 0.0429  107 GLN   A OE1 
2215 N  NE2 A GLN   A 107 ? 0.3565 0.3945 0.5822 -0.0450 -0.0251 -0.0944 107 GLN   A NE2 
2216 N  NE2 B GLN   A 107 ? 0.3606 0.3291 0.4869 -0.0071 -0.0534 0.0402  107 GLN   A NE2 
2233 N  N   A LEU   A 108 ? 0.1889 0.2261 0.2411 -0.0510 0.0261  -0.0797 108 LEU   A N   
2234 N  N   B LEU   A 108 ? 0.2378 0.1932 0.2288 -0.0086 0.0115  0.0202  108 LEU   A N   
2235 C  CA  A LEU   A 108 ? 0.1743 0.1883 0.2079 -0.0246 0.0246  -0.0385 108 LEU   A CA  
2236 C  CA  B LEU   A 108 ? 0.2129 0.1762 0.2093 -0.0077 0.0182  0.0116  108 LEU   A CA  
2237 C  C   A LEU   A 108 ? 0.1566 0.1509 0.2002 -0.0101 0.0194  -0.0091 108 LEU   A C   
2238 C  C   B LEU   A 108 ? 0.1809 0.1507 0.1997 -0.0020 0.0170  0.0166  108 LEU   A C   
2239 O  O   A LEU   A 108 ? 0.1470 0.1478 0.2115 -0.0085 0.0278  -0.0067 108 LEU   A O   
2240 O  O   B LEU   A 108 ? 0.1788 0.1487 0.2091 0.0006  0.0263  0.0216  108 LEU   A O   
2241 C  CB  A LEU   A 108 ? 0.1817 0.1987 0.1821 -0.0207 0.0314  -0.0269 108 LEU   A CB  
2242 C  CB  B LEU   A 108 ? 0.2197 0.1894 0.1927 -0.0134 0.0240  -0.0030 108 LEU   A CB  
2243 C  CG  A LEU   A 108 ? 0.1998 0.2211 0.2078 -0.0130 0.0328  -0.0221 108 LEU   A CG  
2244 C  CG  B LEU   A 108 ? 0.2306 0.2066 0.2070 -0.0170 0.0242  -0.0197 108 LEU   A CG  
2245 C  CD1 A LEU   A 108 ? 0.2179 0.2317 0.2202 -0.0166 0.0443  -0.0148 108 LEU   A CD1 
2246 C  CD1 B LEU   A 108 ? 0.2406 0.2155 0.2161 -0.0201 0.0350  -0.0182 108 LEU   A CD1 
2247 C  CD2 A LEU   A 108 ? 0.2032 0.2327 0.2348 -0.0041 0.0223  -0.0243 108 LEU   A CD2 
2248 C  CD2 B LEU   A 108 ? 0.2301 0.2150 0.2242 -0.0200 0.0154  -0.0298 108 LEU   A CD2 
2271 N  N   . LEU   A 109 ? 0.1547 0.1452 0.1971 -0.0013 0.0101  0.0136  109 LEU   A N   
2272 C  CA  . LEU   A 109 ? 0.1467 0.1386 0.1760 0.0020  0.0002  0.0169  109 LEU   A CA  
2273 C  C   . LEU   A 109 ? 0.1337 0.1311 0.1799 -0.0099 0.0045  0.0096  109 LEU   A C   
2274 O  O   . LEU   A 109 ? 0.1454 0.1282 0.1903 -0.0059 -0.0084 0.0088  109 LEU   A O   
2275 C  CB  . LEU   A 109 ? 0.1524 0.1474 0.2095 0.0106  -0.0057 0.0309  109 LEU   A CB  
2276 C  CG  . LEU   A 109 ? 0.1456 0.1520 0.2127 0.0020  0.0057  0.0333  109 LEU   A CG  
2277 C  CD1 . LEU   A 109 ? 0.1525 0.1473 0.2175 -0.0020 0.0110  0.0150  109 LEU   A CD1 
2278 C  CD2 . LEU   A 109 ? 0.1460 0.1708 0.2385 0.0026  0.0007  0.0382  109 LEU   A CD2 
2291 N  N   . LYS   A 110 ? 0.1343 0.1276 0.1750 -0.0081 -0.0001 0.0032  110 LYS   A N   
2292 C  CA  . LYS   A 110 ? 0.1361 0.1252 0.1850 -0.0090 -0.0023 0.0116  110 LYS   A CA  
2293 C  C   . LYS   A 110 ? 0.1341 0.1193 0.1708 -0.0055 0.0035  0.0024  110 LYS   A C   
2294 O  O   . LYS   A 110 ? 0.1305 0.1252 0.1835 -0.0062 0.0026  -0.0030 110 LYS   A O   
2295 C  CB  . LYS   A 110 ? 0.1432 0.1305 0.2078 -0.0076 -0.0119 -0.0041 110 LYS   A CB  
2296 C  CG  . LYS   A 110 ? 0.1450 0.1276 0.2187 -0.0060 -0.0131 -0.0038 110 LYS   A CG  
2297 C  CD  . LYS   A 110 ? 0.1480 0.1348 0.2349 -0.0059 -0.0100 -0.0063 110 LYS   A CD  
2298 C  CE  . LYS   A 110 ? 0.1544 0.1395 0.2415 -0.0078 0.0083  -0.0099 110 LYS   A CE  
2299 N  NZ  . LYS   A 110 ? 0.1545 0.1420 0.2480 -0.0131 0.0127  -0.0009 110 LYS   A NZ  
2313 N  N   . SER   A 111 ? 0.1352 0.1251 0.1684 -0.0009 0.0010  0.0046  111 SER   A N   
2314 C  CA  . SER   A 111 ? 0.1267 0.1330 0.1809 -0.0032 0.0000  0.0025  111 SER   A CA  
2315 C  C   . SER   A 111 ? 0.1207 0.1244 0.1750 -0.0115 0.0077  0.0089  111 SER   A C   
2316 O  O   . SER   A 111 ? 0.1358 0.1188 0.1898 -0.0056 0.0101  0.0092  111 SER   A O   
2317 C  CB  . SER   A 111 ? 0.1487 0.1494 0.2018 -0.0026 0.0210  -0.0073 111 SER   A CB  
2318 O  OG  . SER   A 111 ? 0.1963 0.1653 0.2047 0.0047  0.0263  -0.0129 111 SER   A OG  
2324 N  N   . ALA   A 112 ? 0.1285 0.1169 0.1835 -0.0050 0.0135  0.0095  112 ALA   A N   
2325 C  CA  . ALA   A 112 ? 0.1339 0.1153 0.1682 -0.0034 0.0137  0.0034  112 ALA   A CA  
2326 C  C   . ALA   A 112 ? 0.1252 0.1129 0.1733 -0.0003 0.0080  0.0038  112 ALA   A C   
2327 O  O   . ALA   A 112 ? 0.1312 0.1099 0.1833 -0.0091 0.0150  0.0101  112 ALA   A O   
2328 C  CB  . ALA   A 112 ? 0.1393 0.1191 0.1742 -0.0046 0.0113  0.0102  112 ALA   A CB  
2334 N  N   . TYR   A 113 ? 0.1154 0.1185 0.1782 -0.0046 0.0108  0.0114  113 TYR   A N   
2335 C  CA  . TYR   A 113 ? 0.1148 0.1160 0.1777 -0.0048 0.0097  0.0115  113 TYR   A CA  
2336 C  C   . TYR   A 113 ? 0.1124 0.1154 0.1624 -0.0097 0.0127  0.0065  113 TYR   A C   
2337 O  O   . TYR   A 113 ? 0.1202 0.1199 0.1820 -0.0059 0.0126  0.0069  113 TYR   A O   
2338 C  CB  . TYR   A 113 ? 0.1134 0.1210 0.1915 -0.0039 -0.0025 0.0170  113 TYR   A CB  
2339 C  CG  . TYR   A 113 ? 0.1204 0.1268 0.1826 -0.0083 0.0091  0.0264  113 TYR   A CG  
2340 C  CD1 . TYR   A 113 ? 0.1224 0.1357 0.1838 -0.0005 0.0074  0.0275  113 TYR   A CD1 
2341 C  CD2 . TYR   A 113 ? 0.1284 0.1318 0.1827 -0.0102 -0.0003 0.0259  113 TYR   A CD2 
2342 C  CE1 . TYR   A 113 ? 0.1283 0.1418 0.1812 -0.0041 0.0060  0.0267  113 TYR   A CE1 
2343 C  CE2 . TYR   A 113 ? 0.1273 0.1392 0.1824 -0.0079 -0.0038 0.0313  113 TYR   A CE2 
2344 C  CZ  . TYR   A 113 ? 0.1236 0.1426 0.1739 0.0017  0.0110  0.0307  113 TYR   A CZ  
2345 O  OH  . TYR   A 113 ? 0.1242 0.1518 0.1982 0.0081  0.0082  0.0312  113 TYR   A OH  
2355 N  N   . GLU   A 114 ? 0.1165 0.1145 0.1755 -0.0087 0.0083  0.0152  114 GLU   A N   
2356 C  CA  . GLU   A 114 ? 0.1200 0.1100 0.1856 0.0025  0.0077  0.0148  114 GLU   A CA  
2357 C  C   . GLU   A 114 ? 0.1161 0.1150 0.1754 0.0023  0.0126  0.0140  114 GLU   A C   
2358 O  O   . GLU   A 114 ? 0.1245 0.1183 0.1793 0.0003  0.0056  0.0128  114 GLU   A O   
2359 C  CB  . GLU   A 114 ? 0.1252 0.1176 0.1832 -0.0019 0.0091  0.0175  114 GLU   A CB  
2360 C  CG  . GLU   A 114 ? 0.1307 0.1173 0.1939 -0.0017 0.0135  0.0023  114 GLU   A CG  
2361 C  CD  . GLU   A 114 ? 0.1398 0.1154 0.2048 -0.0004 0.0010  0.0047  114 GLU   A CD  
2362 O  OE1 . GLU   A 114 ? 0.1407 0.1219 0.2056 -0.0099 0.0131  -0.0024 114 GLU   A OE1 
2363 O  OE2 . GLU   A 114 ? 0.1563 0.1264 0.2228 -0.0069 0.0019  -0.0097 114 GLU   A OE2 
2370 N  N   . ASN   A 115 ? 0.1203 0.1187 0.1639 -0.0040 0.0082  0.0082  115 ASN   A N   
2371 C  CA  . ASN   A 115 ? 0.1176 0.1205 0.1767 -0.0080 0.0102  0.0144  115 ASN   A CA  
2372 C  C   . ASN   A 115 ? 0.1194 0.1139 0.1718 -0.0095 0.0029  0.0053  115 ASN   A C   
2373 O  O   . ASN   A 115 ? 0.1238 0.1269 0.1724 -0.0086 0.0123  0.0211  115 ASN   A O   
2374 C  CB  . ASN   A 115 ? 0.1273 0.1274 0.1708 -0.0083 0.0087  0.0151  115 ASN   A CB  
2375 C  CG  . ASN   A 115 ? 0.1282 0.1462 0.1799 -0.0161 0.0153  0.0152  115 ASN   A CG  
2376 O  OD1 . ASN   A 115 ? 0.1289 0.2371 0.2093 -0.0103 0.0212  0.0269  115 ASN   A OD1 
2377 N  ND2 . ASN   A 115 ? 0.1319 0.1305 0.1690 -0.0137 0.0278  0.0173  115 ASN   A ND2 
2384 N  N   . PHE   A 116 ? 0.1142 0.1162 0.1878 -0.0024 0.0148  0.0172  116 PHE   A N   
2385 C  CA  . PHE   A 116 ? 0.1177 0.1247 0.1711 -0.0009 0.0105  0.0180  116 PHE   A CA  
2386 C  C   . PHE   A 116 ? 0.1186 0.1328 0.1694 -0.0076 0.0130  0.0182  116 PHE   A C   
2387 O  O   . PHE   A 116 ? 0.1246 0.1403 0.1735 0.0029  0.0123  0.0273  116 PHE   A O   
2388 C  CB  . PHE   A 116 ? 0.1199 0.1192 0.1822 -0.0005 0.0137  0.0203  116 PHE   A CB  
2389 C  CG  . PHE   A 116 ? 0.1191 0.1153 0.1732 -0.0021 0.0104  0.0135  116 PHE   A CG  
2390 C  CD1 . PHE   A 116 ? 0.1216 0.1198 0.1740 -0.0058 0.0097  0.0166  116 PHE   A CD1 
2391 C  CD2 . PHE   A 116 ? 0.1278 0.1249 0.1768 -0.0028 0.0175  0.0172  116 PHE   A CD2 
2392 C  CE1 . PHE   A 116 ? 0.1259 0.1140 0.1811 -0.0117 0.0050  0.0137  116 PHE   A CE1 
2393 C  CE2 . PHE   A 116 ? 0.1278 0.1246 0.1940 -0.0024 0.0200  0.0129  116 PHE   A CE2 
2394 C  CZ  . PHE   A 116 ? 0.1344 0.1083 0.1912 0.0036  0.0003  0.0171  116 PHE   A CZ  
2404 N  N   . ASN   A 117 ? 0.1194 0.1231 0.1842 -0.0063 0.0166  0.0221  117 ASN   A N   
2405 C  CA  . ASN   A 117 ? 0.1237 0.1223 0.1813 -0.0048 0.0119  0.0280  117 ASN   A CA  
2406 C  C   . ASN   A 117 ? 0.1245 0.1283 0.1975 0.0018  0.0147  0.0250  117 ASN   A C   
2407 O  O   . ASN   A 117 ? 0.1318 0.1316 0.2215 -0.0040 -0.0032 0.0382  117 ASN   A O   
2408 C  CB  . ASN   A 117 ? 0.1197 0.1289 0.1888 -0.0024 0.0143  0.0328  117 ASN   A CB  
2409 C  CG  . ASN   A 117 ? 0.1216 0.1238 0.1919 -0.0022 0.0162  0.0344  117 ASN   A CG  
2410 O  OD1 . ASN   A 117 ? 0.1242 0.1466 0.2029 -0.0104 0.0141  0.0225  117 ASN   A OD1 
2411 N  ND2 . ASN   A 117 ? 0.1173 0.1254 0.1959 -0.0017 0.0072  0.0257  117 ASN   A ND2 
2418 N  N   . GLN   A 118 ? 0.1196 0.1311 0.1999 -0.0034 0.0037  0.0289  118 GLN   A N   
2419 C  CA  . GLN   A 118 ? 0.1251 0.1414 0.2075 -0.0037 -0.0032 0.0302  118 GLN   A CA  
2420 C  C   . GLN   A 118 ? 0.1292 0.1522 0.1909 -0.0076 -0.0061 0.0339  118 GLN   A C   
2421 O  O   . GLN   A 118 ? 0.1320 0.1817 0.2161 -0.0007 -0.0104 0.0109  118 GLN   A O   
2422 C  CB  . GLN   A 118 ? 0.1238 0.1492 0.2128 -0.0045 0.0068  0.0273  118 GLN   A CB  
2423 C  CG  . GLN   A 118 ? 0.1213 0.1509 0.2154 -0.0025 0.0096  0.0336  118 GLN   A CG  
2424 C  CD  . GLN   A 118 ? 0.1180 0.1519 0.2283 0.0033  0.0131  0.0208  118 GLN   A CD  
2425 O  OE1 . GLN   A 118 ? 0.1264 0.1672 0.2473 0.0124  0.0057  0.0132  118 GLN   A OE1 
2426 N  NE2 . GLN   A 118 ? 0.1280 0.1512 0.2227 0.0055  0.0119  0.0275  118 GLN   A NE2 
2435 N  N   . HIS   A 119 ? 0.1318 0.1462 0.1819 -0.0051 0.0016  0.0369  119 HIS   A N   
2436 C  CA  . HIS   A 119 ? 0.1408 0.1566 0.1914 -0.0042 0.0031  0.0396  119 HIS   A CA  
2437 C  C   . HIS   A 119 ? 0.1471 0.1591 0.1756 -0.0043 0.0107  0.0388  119 HIS   A C   
2438 O  O   . HIS   A 119 ? 0.1534 0.1686 0.1885 -0.0219 -0.0013 0.0388  119 HIS   A O   
2439 C  CB  . HIS   A 119 ? 0.1437 0.1550 0.2105 -0.0030 0.0215  0.0408  119 HIS   A CB  
2440 C  CG  . HIS   A 119 ? 0.1439 0.1602 0.2503 0.0038  0.0140  0.0437  119 HIS   A CG  
2441 N  ND1 . HIS   A 119 ? 0.1544 0.1755 0.3081 -0.0050 0.0131  0.0301  119 HIS   A ND1 
2442 C  CD2 . HIS   A 119 ? 0.1573 0.1653 0.2672 0.0146  0.0342  0.0608  119 HIS   A CD2 
2443 C  CE1 . HIS   A 119 ? 0.1575 0.1740 0.3170 -0.0104 0.0375  0.0509  119 HIS   A CE1 
2444 N  NE2 . HIS   A 119 ? 0.1642 0.1662 0.3065 0.0022  0.0506  0.0687  119 HIS   A NE2 
2452 N  N   . GLU   A 120 ? 0.1542 0.1851 0.1835 0.0021  0.0026  0.0575  120 GLU   A N   
2453 C  CA  . GLU   A 120 ? 0.1772 0.2160 0.2062 0.0108  0.0052  0.0971  120 GLU   A CA  
2454 C  C   . GLU   A 120 ? 0.1608 0.2021 0.1930 -0.0012 0.0064  0.0903  120 GLU   A C   
2455 O  O   . GLU   A 120 ? 0.1585 0.1955 0.2063 -0.0065 -0.0004 0.0870  120 GLU   A O   
2456 C  CB  . GLU   A 120 ? 0.2417 0.2787 0.2642 0.0328  0.0105  0.1397  120 GLU   A CB  
2457 C  CG  . GLU   A 120 ? 0.3324 0.3516 0.3690 0.0487  0.0091  0.1450  120 GLU   A CG  
2458 C  CD  . GLU   A 120 ? 0.4293 0.4236 0.4861 0.0590  0.0159  0.1327  120 GLU   A CD  
2459 O  OE1 . GLU   A 120 ? 0.4530 0.4321 0.5110 0.0602  0.0173  0.1259  120 GLU   A OE1 
2460 O  OE2 . GLU   A 120 ? 0.4708 0.4652 0.5327 0.0613  0.0180  0.1294  120 GLU   A OE2 
2467 N  N   . VAL   A 121 ? 0.1555 0.1974 0.1682 -0.0053 0.0071  0.0685  121 VAL   A N   
2468 C  CA  . VAL   A 121 ? 0.1645 0.2020 0.1527 -0.0043 0.0181  0.0629  121 VAL   A CA  
2469 C  C   . VAL   A 121 ? 0.1496 0.1855 0.1447 -0.0158 0.0082  0.0536  121 VAL   A C   
2470 O  O   . VAL   A 121 ? 0.1528 0.1889 0.1704 -0.0254 -0.0045 0.0448  121 VAL   A O   
2471 C  CB  . VAL   A 121 ? 0.2058 0.2383 0.1880 0.0095  0.0293  0.0708  121 VAL   A CB  
2472 C  CG1 . VAL   A 121 ? 0.2078 0.2527 0.2030 0.0158  0.0370  0.0740  121 VAL   A CG1 
2473 C  CG2 . VAL   A 121 ? 0.2307 0.2564 0.2285 0.0023  0.0281  0.0514  121 VAL   A CG2 
2483 N  N   . LEU   A 122 ? 0.1413 0.1621 0.1622 -0.0160 0.0070  0.0506  122 LEU   A N   
2484 C  CA  . LEU   A 122 ? 0.1467 0.1478 0.1626 -0.0178 0.0229  0.0439  122 LEU   A CA  
2485 C  C   . LEU   A 122 ? 0.1434 0.1499 0.1609 -0.0222 0.0083  0.0374  122 LEU   A C   
2486 O  O   . LEU   A 122 ? 0.1439 0.1554 0.1884 -0.0258 0.0096  0.0366  122 LEU   A O   
2487 C  CB  . LEU   A 122 ? 0.1669 0.1481 0.1992 -0.0087 0.0130  0.0575  122 LEU   A CB  
2488 C  CG  . LEU   A 122 ? 0.1666 0.1574 0.1839 -0.0053 0.0188  0.0394  122 LEU   A CG  
2489 C  CD1 . LEU   A 122 ? 0.1831 0.1573 0.1986 -0.0119 0.0247  0.0325  122 LEU   A CD1 
2490 C  CD2 . LEU   A 122 ? 0.1590 0.1558 0.1685 0.0034  0.0253  0.0313  122 LEU   A CD2 
2502 N  N   . LEU   A 123 ? 0.1343 0.1459 0.1575 -0.0209 0.0043  0.0291  123 LEU   A N   
2503 C  CA  . LEU   A 123 ? 0.1336 0.1444 0.1506 -0.0202 0.0041  0.0279  123 LEU   A CA  
2504 C  C   . LEU   A 123 ? 0.1310 0.1375 0.1405 -0.0112 0.0073  0.0376  123 LEU   A C   
2505 O  O   . LEU   A 123 ? 0.1282 0.1526 0.1589 -0.0215 0.0040  0.0374  123 LEU   A O   
2506 C  CB  . LEU   A 123 ? 0.1452 0.1514 0.1589 -0.0204 0.0129  0.0264  123 LEU   A CB  
2507 C  CG  . LEU   A 123 ? 0.1500 0.1630 0.1729 -0.0181 0.0190  0.0158  123 LEU   A CG  
2508 C  CD1 . LEU   A 123 ? 0.1550 0.1723 0.1963 -0.0057 0.0196  0.0101  123 LEU   A CD1 
2509 C  CD2 . LEU   A 123 ? 0.1646 0.1708 0.1821 -0.0145 0.0059  0.0146  123 LEU   A CD2 
2521 N  N   A ALA   A 124 ? 0.1339 0.1357 0.1362 -0.0125 0.0050  0.0299  124 ALA   A N   
2522 N  N   B ALA   A 124 ? 0.1296 0.1359 0.1326 -0.0102 -0.0003 0.0319  124 ALA   A N   
2523 C  CA  A ALA   A 124 ? 0.1258 0.1325 0.1487 -0.0112 0.0044  0.0257  124 ALA   A CA  
2524 C  CA  B ALA   A 124 ? 0.1216 0.1342 0.1366 -0.0139 -0.0028 0.0321  124 ALA   A CA  
2525 C  C   A ALA   A 124 ? 0.1178 0.1357 0.1608 -0.0137 0.0087  0.0266  124 ALA   A C   
2526 C  C   B ALA   A 124 ? 0.1194 0.1325 0.1404 -0.0116 0.0027  0.0329  124 ALA   A C   
2527 O  O   A ALA   A 124 ? 0.1180 0.1427 0.1745 -0.0143 0.0163  0.0363  124 ALA   A O   
2528 O  O   B ALA   A 124 ? 0.1217 0.1369 0.1615 -0.0075 0.0091  0.0373  124 ALA   A O   
2529 C  CB  A ALA   A 124 ? 0.1269 0.1245 0.1717 -0.0055 0.0069  0.0245  124 ALA   A CB  
2530 C  CB  B ALA   A 124 ? 0.1171 0.1303 0.1475 -0.0124 -0.0024 0.0371  124 ALA   A CB  
2541 N  N   A PRO   A 125 ? 0.1179 0.1336 0.1693 -0.0120 0.0050  0.0300  125 PRO   A N   
2542 N  N   B PRO   A 125 ? 0.1154 0.1273 0.1255 -0.0078 0.0026  0.0410  125 PRO   A N   
2543 C  CA  A PRO   A 125 ? 0.1213 0.1290 0.1704 -0.0092 -0.0004 0.0229  125 PRO   A CA  
2544 C  CA  B PRO   A 125 ? 0.1240 0.1322 0.1334 -0.0101 0.0034  0.0270  125 PRO   A CA  
2545 C  C   A PRO   A 125 ? 0.1080 0.1257 0.1598 -0.0065 0.0021  0.0313  125 PRO   A C   
2546 C  C   B PRO   A 125 ? 0.1314 0.1448 0.1440 -0.0047 0.0041  0.0166  125 PRO   A C   
2547 O  O   A PRO   A 125 ? 0.1107 0.1272 0.1527 0.0022  0.0075  0.0311  125 PRO   A O   
2548 O  O   B PRO   A 125 ? 0.1358 0.1537 0.1555 -0.0054 0.0089  0.0213  125 PRO   A O   
2549 C  CB  A PRO   A 125 ? 0.1371 0.1330 0.1778 -0.0210 0.0018  0.0251  125 PRO   A CB  
2550 C  CB  B PRO   A 125 ? 0.1198 0.1265 0.1237 -0.0165 0.0028  0.0395  125 PRO   A CB  
2551 C  CG  A PRO   A 125 ? 0.1425 0.1354 0.1843 -0.0201 0.0015  0.0334  125 PRO   A CG  
2552 C  CG  B PRO   A 125 ? 0.1142 0.1216 0.1301 -0.0102 0.0018  0.0405  125 PRO   A CG  
2553 C  CD  A PRO   A 125 ? 0.1294 0.1417 0.1803 -0.0164 0.0050  0.0272  125 PRO   A CD  
2554 C  CD  B PRO   A 125 ? 0.1103 0.1207 0.1327 -0.0097 0.0083  0.0382  125 PRO   A CD  
2569 N  N   A LEU   A 126 ? 0.0988 0.1270 0.1676 -0.0056 0.0067  0.0338  126 LEU   A N   
2570 N  N   B LEU   A 126 ? 0.1421 0.1496 0.1589 -0.0010 -0.0015 0.0064  126 LEU   A N   
2571 C  CA  A LEU   A 126 ? 0.1086 0.1356 0.1670 -0.0080 0.0107  0.0263  126 LEU   A CA  
2572 C  CA  B LEU   A 126 ? 0.1485 0.1531 0.1726 0.0046  -0.0004 0.0023  126 LEU   A CA  
2573 C  C   A LEU   A 126 ? 0.1207 0.1306 0.1673 0.0037  -0.0008 0.0298  126 LEU   A C   
2574 C  C   B LEU   A 126 ? 0.1419 0.1439 0.1669 0.0058  0.0092  -0.0038 126 LEU   A C   
2575 O  O   A LEU   A 126 ? 0.1292 0.1316 0.1860 0.0079  0.0094  0.0325  126 LEU   A O   
2576 O  O   B LEU   A 126 ? 0.1444 0.1421 0.1844 0.0014  0.0025  0.0035  126 LEU   A O   
2577 C  CB  A LEU   A 126 ? 0.1094 0.1494 0.1620 -0.0132 0.0075  0.0208  126 LEU   A CB  
2578 C  CB  B LEU   A 126 ? 0.1695 0.1816 0.2271 -0.0048 -0.0147 0.0055  126 LEU   A CB  
2579 C  CG  A LEU   A 126 ? 0.1115 0.1748 0.1713 -0.0205 0.0072  0.0261  126 LEU   A CG  
2580 C  CG  B LEU   A 126 ? 0.1867 0.2059 0.2757 -0.0151 -0.0310 0.0167  126 LEU   A CG  
2581 C  CD1 A LEU   A 126 ? 0.1127 0.1891 0.1796 -0.0207 0.0037  0.0262  126 LEU   A CD1 
2582 C  CD1 B LEU   A 126 ? 0.1883 0.2119 0.2842 -0.0223 -0.0341 0.0186  126 LEU   A CD1 
2583 C  CD2 A LEU   A 126 ? 0.1315 0.1704 0.1800 -0.0273 0.0029  0.0539  126 LEU   A CD2 
2584 C  CD2 B LEU   A 126 ? 0.1905 0.2134 0.2846 -0.0200 -0.0399 0.0238  126 LEU   A CD2 
2607 N  N   A LEU   A 127 ? 0.1264 0.1246 0.1500 0.0028  0.0037  0.0182  127 LEU   A N   
2608 N  N   B LEU   A 127 ? 0.1367 0.1413 0.1562 0.0052  0.0183  0.0004  127 LEU   A N   
2609 C  CA  A LEU   A 127 ? 0.1336 0.1290 0.1441 -0.0004 0.0011  0.0113  127 LEU   A CA  
2610 C  CA  B LEU   A 127 ? 0.1366 0.1484 0.1548 0.0087  0.0160  0.0084  127 LEU   A CA  
2611 C  C   A LEU   A 127 ? 0.1309 0.1244 0.1411 -0.0046 -0.0054 0.0112  127 LEU   A C   
2612 C  C   B LEU   A 127 ? 0.1374 0.1474 0.1515 0.0074  0.0160  0.0070  127 LEU   A C   
2613 O  O   A LEU   A 127 ? 0.1365 0.1204 0.1342 -0.0146 -0.0052 0.0159  127 LEU   A O   
2614 O  O   B LEU   A 127 ? 0.1491 0.1496 0.1569 0.0085  0.0224  0.0058  127 LEU   A O   
2615 C  CB  A LEU   A 127 ? 0.1400 0.1316 0.1436 0.0043  0.0070  0.0115  127 LEU   A CB  
2616 C  CB  B LEU   A 127 ? 0.1394 0.1560 0.1448 0.0113  0.0088  0.0042  127 LEU   A CB  
2617 C  CG  A LEU   A 127 ? 0.1417 0.1258 0.1586 0.0035  0.0047  0.0088  127 LEU   A CG  
2618 C  CG  B LEU   A 127 ? 0.1398 0.1648 0.1441 0.0145  -0.0083 0.0051  127 LEU   A CG  
2619 C  CD1 A LEU   A 127 ? 0.1469 0.1227 0.1672 -0.0013 0.0038  0.0038  127 LEU   A CD1 
2620 C  CD1 B LEU   A 127 ? 0.1410 0.1646 0.1529 0.0214  -0.0032 0.0076  127 LEU   A CD1 
2621 C  CD2 A LEU   A 127 ? 0.1521 0.1223 0.1806 0.0131  -0.0009 0.0055  127 LEU   A CD2 
2622 C  CD2 B LEU   A 127 ? 0.1506 0.1743 0.1402 0.0144  -0.0200 -0.0024 127 LEU   A CD2 
2645 N  N   A SER   A 128 ? 0.1401 0.1269 0.1440 -0.0039 -0.0050 0.0090  128 SER   A N   
2646 N  N   B SER   A 128 ? 0.1338 0.1430 0.1454 0.0013  0.0043  0.0143  128 SER   A N   
2647 C  CA  A SER   A 128 ? 0.1515 0.1392 0.1484 -0.0049 -0.0021 0.0106  128 SER   A CA  
2648 C  CA  B SER   A 128 ? 0.1336 0.1444 0.1414 -0.0041 -0.0160 0.0242  128 SER   A CA  
2649 C  C   A SER   A 128 ? 0.1599 0.1434 0.1707 0.0028  0.0005  0.0140  128 SER   A C   
2650 C  C   B SER   A 128 ? 0.1393 0.1400 0.1453 -0.0034 -0.0321 0.0301  128 SER   A C   
2651 O  O   A SER   A 128 ? 0.1740 0.1630 0.1966 0.0039  0.0102  0.0069  128 SER   A O   
2652 O  O   B SER   A 128 ? 0.1376 0.1459 0.1433 -0.0128 -0.0398 0.0305  128 SER   A O   
2653 C  CB  A SER   A 128 ? 0.1523 0.1501 0.1371 -0.0097 -0.0013 0.0129  128 SER   A CB  
2654 C  CB  B SER   A 128 ? 0.1286 0.1515 0.1411 -0.0084 -0.0180 0.0241  128 SER   A CB  
2655 O  OG  A SER   A 128 ? 0.1541 0.1568 0.1501 -0.0080 0.0045  0.0126  128 SER   A OG  
2656 O  OG  B SER   A 128 ? 0.1220 0.1549 0.1530 -0.0114 -0.0177 0.0106  128 SER   A OG  
2667 N  N   A ALA   A 129 ? 0.1469 0.1437 0.1887 -0.0002 0.0008  0.0239  129 ALA   A N   
2668 N  N   B ALA   A 129 ? 0.1389 0.1415 0.1667 0.0003  -0.0312 0.0281  129 ALA   A N   
2669 C  CA  A ALA   A 129 ? 0.1362 0.1473 0.1930 -0.0022 -0.0078 0.0205  129 ALA   A CA  
2670 C  CA  B ALA   A 129 ? 0.1459 0.1507 0.1792 -0.0006 -0.0255 0.0211  129 ALA   A CA  
2671 C  C   A ALA   A 129 ? 0.1290 0.1404 0.1727 -0.0056 -0.0190 0.0032  129 ALA   A C   
2672 C  C   B ALA   A 129 ? 0.1608 0.1600 0.1742 0.0020  -0.0259 0.0123  129 ALA   A C   
2673 O  O   A ALA   A 129 ? 0.1273 0.1408 0.1696 -0.0038 -0.0112 0.0211  129 ALA   A O   
2674 O  O   B ALA   A 129 ? 0.1706 0.1653 0.1770 -0.0012 -0.0138 0.0226  129 ALA   A O   
2675 C  CB  A ALA   A 129 ? 0.1395 0.1647 0.2099 0.0041  -0.0028 0.0266  129 ALA   A CB  
2676 C  CB  B ALA   A 129 ? 0.1437 0.1593 0.1866 -0.0071 -0.0201 0.0190  129 ALA   A CB  
2687 N  N   A GLY   A 130 ? 0.1338 0.1344 0.1608 -0.0041 -0.0253 -0.0164 130 GLY   A N   
2688 N  N   B GLY   A 130 ? 0.1656 0.1584 0.1618 0.0003  -0.0469 -0.0006 130 GLY   A N   
2689 C  CA  A GLY   A 130 ? 0.1487 0.1363 0.1642 -0.0054 -0.0298 -0.0141 130 GLY   A CA  
2690 C  CA  B GLY   A 130 ? 0.1769 0.1595 0.1585 0.0059  -0.0613 -0.0059 130 GLY   A CA  
2691 C  C   A GLY   A 130 ? 0.1634 0.1408 0.1749 0.0007  -0.0260 -0.0037 130 GLY   A C   
2692 C  C   B GLY   A 130 ? 0.1870 0.1565 0.1753 0.0125  -0.0603 -0.0003 130 GLY   A C   
2693 O  O   A GLY   A 130 ? 0.1706 0.1435 0.1803 0.0034  -0.0140 -0.0095 130 GLY   A O   
2694 O  O   B GLY   A 130 ? 0.1916 0.1589 0.1947 0.0186  -0.0638 0.0110  130 GLY   A O   
2701 N  N   A ILE   A 131 ? 0.1683 0.1388 0.1824 -0.0059 -0.0325 0.0179  131 ILE   A N   
2702 N  N   B ILE   A 131 ? 0.1932 0.1497 0.1812 0.0120  -0.0393 0.0019  131 ILE   A N   
2703 C  CA  A ILE   A 131 ? 0.1867 0.1428 0.1774 -0.0115 -0.0440 0.0215  131 ILE   A CA  
2704 C  CA  B ILE   A 131 ? 0.2051 0.1510 0.1739 0.0046  -0.0354 0.0001  131 ILE   A CA  
2705 C  C   A ILE   A 131 ? 0.1836 0.1450 0.1751 -0.0071 -0.0371 0.0341  131 ILE   A C   
2706 C  C   B ILE   A 131 ? 0.2066 0.1492 0.1687 0.0011  -0.0272 -0.0009 131 ILE   A C   
2707 O  O   A ILE   A 131 ? 0.1940 0.1511 0.1914 -0.0046 -0.0361 0.0381  131 ILE   A O   
2708 O  O   B ILE   A 131 ? 0.2113 0.1406 0.1814 -0.0039 -0.0337 0.0029  131 ILE   A O   
2709 C  CB  A ILE   A 131 ? 0.2085 0.1504 0.1801 -0.0230 -0.0402 0.0128  131 ILE   A CB  
2710 C  CB  B ILE   A 131 ? 0.2139 0.1637 0.1858 -0.0025 -0.0270 -0.0028 131 ILE   A CB  
2711 C  CG1 A ILE   A 131 ? 0.2151 0.1750 0.1824 -0.0375 -0.0405 0.0203  131 ILE   A CG1 
2712 C  CG1 B ILE   A 131 ? 0.2196 0.1870 0.1926 -0.0119 -0.0345 0.0007  131 ILE   A CG1 
2713 C  CG2 A ILE   A 131 ? 0.2195 0.1407 0.1959 -0.0163 -0.0295 0.0034  131 ILE   A CG2 
2714 C  CG2 B ILE   A 131 ? 0.2169 0.1570 0.2060 0.0020  -0.0184 -0.0091 131 ILE   A CG2 
2715 C  CD1 A ILE   A 131 ? 0.2225 0.1834 0.1999 -0.0466 -0.0333 0.0163  131 ILE   A CD1 
2716 C  CD1 B ILE   A 131 ? 0.2244 0.1984 0.1986 -0.0143 -0.0319 0.0058  131 ILE   A CD1 
2739 N  N   A PHE   A 132 ? 0.1672 0.1396 0.1650 -0.0007 -0.0344 0.0331  132 PHE   A N   
2740 N  N   B PHE   A 132 ? 0.1999 0.1546 0.1615 0.0048  -0.0121 0.0006  132 PHE   A N   
2741 C  CA  A PHE   A 132 ? 0.1709 0.1463 0.1647 -0.0074 -0.0225 0.0202  132 PHE   A CA  
2742 C  CA  B PHE   A 132 ? 0.2000 0.1663 0.1535 0.0027  -0.0063 0.0011  132 PHE   A CA  
2743 C  C   A PHE   A 132 ? 0.1754 0.1569 0.1721 -0.0134 -0.0261 0.0162  132 PHE   A C   
2744 C  C   B PHE   A 132 ? 0.2022 0.1837 0.1640 -0.0040 -0.0227 0.0193  132 PHE   A C   
2745 O  O   A PHE   A 132 ? 0.1811 0.1575 0.1713 -0.0211 -0.0196 0.0137  132 PHE   A O   
2746 O  O   B PHE   A 132 ? 0.2083 0.1917 0.1738 -0.0104 -0.0239 0.0198  132 PHE   A O   
2747 C  CB  A PHE   A 132 ? 0.1633 0.1447 0.1416 -0.0002 -0.0173 0.0350  132 PHE   A CB  
2748 C  CB  B PHE   A 132 ? 0.1961 0.1622 0.1401 0.0081  0.0047  -0.0064 132 PHE   A CB  
2749 C  CG  A PHE   A 132 ? 0.1597 0.1445 0.1372 0.0040  -0.0230 0.0271  132 PHE   A CG  
2750 C  CG  B PHE   A 132 ? 0.1910 0.1594 0.1228 0.0109  0.0112  -0.0179 132 PHE   A CG  
2751 C  CD1 A PHE   A 132 ? 0.1569 0.1571 0.1470 0.0168  -0.0181 0.0091  132 PHE   A CD1 
2752 C  CD1 B PHE   A 132 ? 0.1902 0.1676 0.1271 0.0126  0.0120  -0.0215 132 PHE   A CD1 
2753 C  CD2 A PHE   A 132 ? 0.1581 0.1574 0.1557 0.0088  -0.0286 0.0172  132 PHE   A CD2 
2754 C  CD2 B PHE   A 132 ? 0.1872 0.1592 0.1268 0.0119  0.0174  -0.0318 132 PHE   A CD2 
2755 C  CE1 A PHE   A 132 ? 0.1515 0.1637 0.1439 0.0184  -0.0235 -0.0049 132 PHE   A CE1 
2756 C  CE1 B PHE   A 132 ? 0.1869 0.1724 0.1319 0.0099  0.0130  -0.0193 132 PHE   A CE1 
2757 C  CE2 A PHE   A 132 ? 0.1537 0.1649 0.1702 0.0127  -0.0264 0.0102  132 PHE   A CE2 
2758 C  CE2 B PHE   A 132 ? 0.1840 0.1650 0.1391 0.0141  0.0165  -0.0231 132 PHE   A CE2 
2759 C  CZ  A PHE   A 132 ? 0.1474 0.1656 0.1533 0.0134  -0.0319 0.0046  132 PHE   A CZ  
2760 C  CZ  B PHE   A 132 ? 0.1809 0.1680 0.1329 0.0110  0.0169  -0.0187 132 PHE   A CZ  
2779 N  N   A GLY   A 133 ? 0.1786 0.1715 0.1708 -0.0073 -0.0372 0.0212  133 GLY   A N   
2780 N  N   B GLY   A 133 ? 0.1999 0.1923 0.1582 -0.0062 -0.0338 0.0339  133 GLY   A N   
2781 C  CA  A GLY   A 133 ? 0.1817 0.1791 0.1646 -0.0052 -0.0440 0.0095  133 GLY   A CA  
2782 C  CA  B GLY   A 133 ? 0.1974 0.1994 0.1577 -0.0104 -0.0323 0.0283  133 GLY   A CA  
2783 C  C   A GLY   A 133 ? 0.1768 0.1881 0.1586 -0.0108 -0.0394 -0.0023 133 GLY   A C   
2784 C  C   B GLY   A 133 ? 0.1923 0.2086 0.1566 -0.0163 -0.0304 0.0211  133 GLY   A C   
2785 O  O   A GLY   A 133 ? 0.1865 0.2057 0.1651 -0.0110 -0.0350 -0.0203 133 GLY   A O   
2786 O  O   B GLY   A 133 ? 0.1917 0.2160 0.1452 -0.0246 -0.0181 0.0162  133 GLY   A O   
2793 N  N   A ALA   A 134 ? 0.1709 0.1738 0.1575 -0.0182 -0.0308 0.0025  134 ALA   A N   
2794 N  N   B ALA   A 134 ? 0.1913 0.2085 0.1674 -0.0130 -0.0342 0.0207  134 ALA   A N   
2795 C  CA  A ALA   A 134 ? 0.1698 0.1735 0.1760 -0.0171 -0.0214 -0.0005 134 ALA   A CA  
2796 C  CA  B ALA   A 134 ? 0.1876 0.2114 0.1789 -0.0107 -0.0333 0.0226  134 ALA   A CA  
2797 C  C   A ALA   A 134 ? 0.1761 0.1781 0.1794 -0.0082 -0.0155 0.0039  134 ALA   A C   
2798 C  C   B ALA   A 134 ? 0.1887 0.2128 0.1840 -0.0104 -0.0269 0.0341  134 ALA   A C   
2799 O  O   A ALA   A 134 ? 0.1918 0.1868 0.1831 0.0028  0.0088  0.0022  134 ALA   A O   
2800 O  O   B ALA   A 134 ? 0.1987 0.2176 0.1919 -0.0127 -0.0263 0.0384  134 ALA   A O   
2801 C  CB  A ALA   A 134 ? 0.1737 0.1710 0.2047 -0.0216 -0.0163 -0.0058 134 ALA   A CB  
2802 C  CB  B ALA   A 134 ? 0.1892 0.2119 0.1886 -0.0080 -0.0309 0.0164  134 ALA   A CB  
2813 N  N   A ASP   A 135 ? 0.1732 0.1855 0.1982 -0.0199 -0.0281 0.0211  135 ASP   A N   
2814 N  N   B ASP   A 135 ? 0.1839 0.2148 0.2061 -0.0058 -0.0201 0.0350  135 ASP   A N   
2815 C  CA  A ASP   A 135 ? 0.1686 0.2023 0.2299 -0.0262 -0.0433 0.0304  135 ASP   A CA  
2816 C  CA  B ASP   A 135 ? 0.1858 0.2232 0.2356 -0.0070 -0.0252 0.0409  135 ASP   A CA  
2817 C  C   A ASP   A 135 ? 0.1593 0.1891 0.2245 -0.0144 -0.0279 0.0444  135 ASP   A C   
2818 C  C   B ASP   A 135 ? 0.1800 0.2127 0.2191 -0.0083 -0.0234 0.0402  135 ASP   A C   
2819 O  O   A ASP   A 135 ? 0.1552 0.1749 0.2313 -0.0144 -0.0246 0.0479  135 ASP   A O   
2820 O  O   B ASP   A 135 ? 0.1742 0.2038 0.2174 -0.0121 -0.0209 0.0472  135 ASP   A O   
2821 C  CB  A ASP   A 135 ? 0.1815 0.2382 0.2545 -0.0496 -0.0701 0.0259  135 ASP   A CB  
2822 C  CB  B ASP   A 135 ? 0.2021 0.2428 0.2939 -0.0106 -0.0276 0.0434  135 ASP   A CB  
2823 C  CG  A ASP   A 135 ? 0.1940 0.2734 0.2836 -0.0630 -0.0836 0.0323  135 ASP   A CG  
2824 C  CG  B ASP   A 135 ? 0.2159 0.2591 0.3510 -0.0136 -0.0264 0.0463  135 ASP   A CG  
2825 O  OD1 A ASP   A 135 ? 0.2011 0.2904 0.2823 -0.0663 -0.0857 0.0577  135 ASP   A OD1 
2826 O  OD1 B ASP   A 135 ? 0.2285 0.2667 0.3739 -0.0143 -0.0120 0.0486  135 ASP   A OD1 
2827 O  OD2 A ASP   A 135 ? 0.2212 0.2907 0.3353 -0.0653 -0.0615 0.0296  135 ASP   A OD2 
2828 O  OD2 B ASP   A 135 ? 0.2181 0.2679 0.3795 -0.0119 -0.0291 0.0467  135 ASP   A OD2 
2837 N  N   A PRO   A 136 ? 0.1566 0.1870 0.2199 -0.0018 -0.0198 0.0567  136 PRO   A N   
2838 N  N   B PRO   A 136 ? 0.1772 0.2074 0.2081 -0.0029 -0.0218 0.0340  136 PRO   A N   
2839 C  CA  A PRO   A 136 ? 0.1484 0.1899 0.2314 -0.0001 -0.0085 0.0497  136 PRO   A CA  
2840 C  CA  B PRO   A 136 ? 0.1725 0.2051 0.2080 -0.0032 -0.0205 0.0325  136 PRO   A CA  
2841 C  C   A PRO   A 136 ? 0.1269 0.1917 0.2301 -0.0031 0.0023  0.0497  136 PRO   A C   
2842 C  C   B PRO   A 136 ? 0.1610 0.2023 0.2122 -0.0021 -0.0227 0.0377  136 PRO   A C   
2843 O  O   A PRO   A 136 ? 0.1194 0.1819 0.2035 0.0003  0.0184  0.0425  136 PRO   A O   
2844 O  O   B PRO   A 136 ? 0.1565 0.2034 0.1995 0.0007  -0.0209 0.0438  136 PRO   A O   
2845 C  CB  A PRO   A 136 ? 0.1673 0.1892 0.2447 0.0074  -0.0124 0.0450  136 PRO   A CB  
2846 C  CB  B PRO   A 136 ? 0.1821 0.2054 0.2045 0.0007  -0.0179 0.0302  136 PRO   A CB  
2847 C  CG  A PRO   A 136 ? 0.1773 0.1917 0.2551 0.0092  -0.0177 0.0466  136 PRO   A CG  
2848 C  CG  B PRO   A 136 ? 0.1864 0.2067 0.2073 0.0014  -0.0233 0.0227  136 PRO   A CG  
2849 C  CD  A PRO   A 136 ? 0.1670 0.1873 0.2332 0.0053  -0.0155 0.0666  136 PRO   A CD  
2850 C  CD  B PRO   A 136 ? 0.1844 0.2064 0.2072 0.0013  -0.0256 0.0282  136 PRO   A CD  
2865 N  N   A ILE   A 137 ? 0.1212 0.2012 0.2514 -0.0064 -0.0154 0.0541  137 ILE   A N   
2866 N  N   B ILE   A 137 ? 0.1618 0.2031 0.2298 -0.0040 -0.0342 0.0407  137 ILE   A N   
2867 C  CA  A ILE   A 137 ? 0.1239 0.2205 0.2565 -0.0171 -0.0262 0.0585  137 ILE   A CA  
2868 C  CA  B ILE   A 137 ? 0.1679 0.2088 0.2418 -0.0107 -0.0388 0.0385  137 ILE   A CA  
2869 C  C   A ILE   A 137 ? 0.1303 0.2175 0.2448 -0.0231 -0.0290 0.0588  137 ILE   A C   
2870 C  C   B ILE   A 137 ? 0.1649 0.2022 0.2359 -0.0148 -0.0401 0.0359  137 ILE   A C   
2871 O  O   A ILE   A 137 ? 0.1359 0.2106 0.2483 -0.0349 -0.0238 0.0534  137 ILE   A O   
2872 O  O   B ILE   A 137 ? 0.1691 0.1930 0.2365 -0.0173 -0.0407 0.0329  137 ILE   A O   
2873 C  CB  A ILE   A 137 ? 0.1335 0.2465 0.2713 -0.0183 -0.0398 0.0638  137 ILE   A CB  
2874 C  CB  B ILE   A 137 ? 0.1835 0.2259 0.2567 -0.0097 -0.0441 0.0363  137 ILE   A CB  
2875 C  CG1 A ILE   A 137 ? 0.1480 0.2710 0.2750 -0.0111 -0.0413 0.0731  137 ILE   A CG1 
2876 C  CG1 B ILE   A 137 ? 0.1959 0.2428 0.2643 0.0044  -0.0470 0.0390  137 ILE   A CG1 
2877 C  CG2 A ILE   A 137 ? 0.1407 0.2491 0.2915 -0.0247 -0.0425 0.0594  137 ILE   A CG2 
2878 C  CG2 B ILE   A 137 ? 0.1903 0.2263 0.2690 -0.0210 -0.0398 0.0307  137 ILE   A CG2 
2879 C  CD1 A ILE   A 137 ? 0.1643 0.2880 0.2864 -0.0047 -0.0328 0.0737  137 ILE   A CD1 
2880 C  CD1 B ILE   A 137 ? 0.2065 0.2531 0.2740 0.0116  -0.0436 0.0375  137 ILE   A CD1 
2903 N  N   A HIS   A 138 ? 0.1342 0.2257 0.2360 -0.0206 -0.0133 0.0570  138 HIS   A N   
2904 N  N   B HIS   A 138 ? 0.1598 0.2089 0.2347 -0.0146 -0.0305 0.0343  138 HIS   A N   
2905 C  CA  A HIS   A 138 ? 0.1468 0.2234 0.2238 -0.0187 -0.0130 0.0541  138 HIS   A CA  
2906 C  CA  B HIS   A 138 ? 0.1574 0.2079 0.2209 -0.0170 -0.0272 0.0348  138 HIS   A CA  
2907 C  C   A HIS   A 138 ? 0.1420 0.2047 0.2236 -0.0155 -0.0103 0.0581  138 HIS   A C   
2908 C  C   B HIS   A 138 ? 0.1464 0.1989 0.2192 -0.0125 -0.0215 0.0471  138 HIS   A C   
2909 O  O   A HIS   A 138 ? 0.1485 0.2008 0.2216 -0.0177 -0.0022 0.0538  138 HIS   A O   
2910 O  O   B HIS   A 138 ? 0.1498 0.1977 0.2127 -0.0115 -0.0192 0.0413  138 HIS   A O   
2911 C  CB  A HIS   A 138 ? 0.1655 0.2414 0.2144 -0.0227 -0.0181 0.0487  138 HIS   A CB  
2912 C  CB  B HIS   A 138 ? 0.1722 0.2202 0.2195 -0.0247 -0.0351 0.0191  138 HIS   A CB  
2913 C  CG  A HIS   A 138 ? 0.1822 0.2519 0.2261 -0.0283 -0.0166 0.0424  138 HIS   A CG  
2914 C  CG  B HIS   A 138 ? 0.1838 0.2282 0.2325 -0.0319 -0.0337 0.0010  138 HIS   A CG  
2915 N  ND1 A HIS   A 138 ? 0.1923 0.2601 0.2446 -0.0308 -0.0166 0.0313  138 HIS   A ND1 
2916 N  ND1 B HIS   A 138 ? 0.1898 0.2355 0.2457 -0.0348 -0.0322 -0.0132 138 HIS   A ND1 
2917 C  CD2 A HIS   A 138 ? 0.1843 0.2558 0.2236 -0.0238 -0.0118 0.0447  138 HIS   A CD2 
2918 C  CD2 B HIS   A 138 ? 0.1843 0.2290 0.2367 -0.0298 -0.0348 -0.0030 138 HIS   A CD2 
2919 C  CE1 A HIS   A 138 ? 0.1946 0.2602 0.2453 -0.0241 -0.0165 0.0318  138 HIS   A CE1 
2920 C  CE1 B HIS   A 138 ? 0.1898 0.2332 0.2460 -0.0329 -0.0318 -0.0150 138 HIS   A CE1 
2921 N  NE2 A HIS   A 138 ? 0.1892 0.2584 0.2270 -0.0237 -0.0067 0.0360  138 HIS   A NE2 
2922 N  NE2 B HIS   A 138 ? 0.1851 0.2306 0.2397 -0.0309 -0.0332 -0.0126 138 HIS   A NE2 
2937 N  N   . SER   A 139 ? 0.1347 0.1901 0.2299 -0.0089 -0.0122 0.0611  139 SER   A N   
2938 C  CA  . SER   A 139 ? 0.1281 0.1768 0.2264 -0.0119 -0.0074 0.0554  139 SER   A CA  
2939 C  C   . SER   A 139 ? 0.1223 0.1615 0.2274 -0.0128 -0.0051 0.0458  139 SER   A C   
2940 O  O   . SER   A 139 ? 0.1170 0.1574 0.2380 -0.0106 -0.0034 0.0425  139 SER   A O   
2941 C  CB  . SER   A 139 ? 0.1251 0.1758 0.2228 -0.0139 -0.0111 0.0576  139 SER   A CB  
2942 O  OG  . SER   A 139 ? 0.1329 0.1693 0.2318 -0.0151 -0.0185 0.0593  139 SER   A OG  
2949 N  N   . LEU   A 140 ? 0.1200 0.1659 0.2234 -0.0091 -0.0067 0.0527  140 LEU   A N   
2950 C  CA  . LEU   A 140 ? 0.1226 0.1608 0.2225 -0.0132 -0.0060 0.0469  140 LEU   A CA  
2951 C  C   . LEU   A 140 ? 0.1141 0.1674 0.2176 -0.0179 -0.0059 0.0447  140 LEU   A C   
2952 O  O   . LEU   A 140 ? 0.1241 0.1651 0.2298 -0.0075 -0.0063 0.0448  140 LEU   A O   
2953 C  CB  . LEU   A 140 ? 0.1252 0.1655 0.2252 -0.0142 -0.0050 0.0438  140 LEU   A CB  
2954 C  CG  . LEU   A 140 ? 0.1245 0.1770 0.2318 -0.0206 -0.0028 0.0567  140 LEU   A CG  
2955 C  CD1 . LEU   A 140 ? 0.1269 0.1765 0.2366 -0.0110 -0.0060 0.0478  140 LEU   A CD1 
2956 C  CD2 . LEU   A 140 ? 0.1280 0.1952 0.2427 -0.0198 0.0043  0.0601  140 LEU   A CD2 
2968 N  N   . ARG   A 141 ? 0.1218 0.1743 0.2416 -0.0155 -0.0062 0.0394  141 ARG   A N   
2969 C  CA  . ARG   A 141 ? 0.1367 0.1879 0.2430 -0.0244 -0.0143 0.0251  141 ARG   A CA  
2970 C  C   . ARG   A 141 ? 0.1345 0.1698 0.2268 -0.0188 -0.0135 0.0263  141 ARG   A C   
2971 O  O   . ARG   A 141 ? 0.1337 0.1637 0.2356 -0.0173 -0.0006 0.0197  141 ARG   A O   
2972 C  CB  . ARG   A 141 ? 0.1535 0.2231 0.2679 -0.0336 -0.0174 0.0092  141 ARG   A CB  
2973 C  CG  . ARG   A 141 ? 0.1880 0.2640 0.2959 -0.0361 0.0032  0.0042  141 ARG   A CG  
2974 C  CD  . ARG   A 141 ? 0.2157 0.2916 0.3141 -0.0459 0.0043  -0.0041 141 ARG   A CD  
2975 N  NE  . ARG   A 141 ? 0.2042 0.3125 0.3299 -0.0543 -0.0052 -0.0025 141 ARG   A NE  
2976 C  CZ  . ARG   A 141 ? 0.2051 0.3353 0.3407 -0.0675 0.0010  0.0017  141 ARG   A CZ  
2977 N  NH1 . ARG   A 141 ? 0.1963 0.3392 0.3308 -0.0759 0.0276  -0.0152 141 ARG   A NH1 
2978 N  NH2 . ARG   A 141 ? 0.2082 0.3406 0.3515 -0.0615 -0.0204 0.0149  141 ARG   A NH2 
2992 N  N   . VAL   A 142 ? 0.1298 0.1630 0.2193 -0.0163 -0.0104 0.0192  142 VAL   A N   
2993 C  CA  . VAL   A 142 ? 0.1331 0.1550 0.2155 -0.0116 0.0049  0.0207  142 VAL   A CA  
2994 C  C   . VAL   A 142 ? 0.1203 0.1491 0.2068 -0.0122 -0.0067 0.0239  142 VAL   A C   
2995 O  O   . VAL   A 142 ? 0.1272 0.1517 0.2056 -0.0046 0.0020  0.0204  142 VAL   A O   
2996 C  CB  . VAL   A 142 ? 0.1413 0.1667 0.2012 -0.0133 0.0052  0.0231  142 VAL   A CB  
2997 C  CG1 . VAL   A 142 ? 0.1399 0.1604 0.2012 -0.0170 0.0130  0.0204  142 VAL   A CG1 
2998 C  CG2 . VAL   A 142 ? 0.1582 0.1833 0.2151 -0.0121 0.0025  0.0220  142 VAL   A CG2 
3008 N  N   . CYS   A 143 ? 0.1263 0.1476 0.2014 -0.0132 -0.0028 0.0245  143 CYS   A N   
3009 C  CA  . CYS   A 143 ? 0.1242 0.1430 0.2078 -0.0106 0.0054  0.0301  143 CYS   A CA  
3010 C  C   . CYS   A 143 ? 0.1195 0.1412 0.2112 -0.0088 0.0027  0.0317  143 CYS   A C   
3011 O  O   . CYS   A 143 ? 0.1187 0.1383 0.2072 -0.0071 0.0009  0.0280  143 CYS   A O   
3012 C  CB  . CYS   A 143 ? 0.1316 0.1394 0.2125 -0.0055 0.0088  0.0389  143 CYS   A CB  
3013 S  SG  . CYS   A 143 ? 0.1466 0.1518 0.2149 0.0047  0.0112  0.0281  143 CYS   A SG  
3019 N  N   . VAL   A 144 ? 0.1207 0.1460 0.2330 -0.0090 0.0057  0.0426  144 VAL   A N   
3020 C  CA  . VAL   A 144 ? 0.1287 0.1524 0.2607 -0.0112 0.0202  0.0382  144 VAL   A CA  
3021 C  C   . VAL   A 144 ? 0.1306 0.1418 0.2574 -0.0187 -0.0019 0.0320  144 VAL   A C   
3022 O  O   . VAL   A 144 ? 0.1403 0.1466 0.2577 -0.0089 -0.0056 0.0373  144 VAL   A O   
3023 C  CB  . VAL   A 144 ? 0.1558 0.1757 0.3204 -0.0019 0.0455  0.0381  144 VAL   A CB  
3024 C  CG1 . VAL   A 144 ? 0.1659 0.1902 0.3592 -0.0131 0.0306  0.0349  144 VAL   A CG1 
3025 C  CG2 . VAL   A 144 ? 0.1449 0.1806 0.3308 0.0022  0.0565  0.0489  144 VAL   A CG2 
3035 N  N   . ASP   A 145 ? 0.1335 0.1435 0.2632 -0.0207 -0.0041 0.0209  145 ASP   A N   
3036 C  CA  . ASP   A 145 ? 0.1485 0.1506 0.2641 -0.0260 -0.0039 0.0132  145 ASP   A CA  
3037 C  C   . ASP   A 145 ? 0.1500 0.1397 0.2609 -0.0163 -0.0005 0.0014  145 ASP   A C   
3038 O  O   . ASP   A 145 ? 0.1625 0.1462 0.3190 -0.0202 -0.0012 -0.0324 145 ASP   A O   
3039 C  CB  . ASP   A 145 ? 0.1632 0.1824 0.2832 -0.0349 -0.0142 0.0085  145 ASP   A CB  
3040 C  CG  . ASP   A 145 ? 0.1791 0.2242 0.3108 -0.0525 -0.0282 0.0207  145 ASP   A CG  
3041 O  OD1 . ASP   A 145 ? 0.1699 0.2364 0.3165 -0.0608 -0.0215 0.0273  145 ASP   A OD1 
3042 O  OD2 . ASP   A 145 ? 0.2030 0.2487 0.3243 -0.0621 -0.0526 0.0216  145 ASP   A OD2 
3047 N  N   . THR   A 146 ? 0.1336 0.1322 0.2205 -0.0128 0.0024  0.0096  146 THR   A N   
3048 C  CA  . THR   A 146 ? 0.1281 0.1298 0.1999 -0.0063 0.0025  0.0146  146 THR   A CA  
3049 C  C   . THR   A 146 ? 0.1233 0.1256 0.2100 -0.0029 0.0092  0.0181  146 THR   A C   
3050 O  O   . THR   A 146 ? 0.1340 0.1397 0.2287 0.0068  0.0016  0.0163  146 THR   A O   
3051 C  CB  . THR   A 146 ? 0.1267 0.1405 0.1987 -0.0053 0.0041  0.0187  146 THR   A CB  
3052 O  OG1 . THR   A 146 ? 0.1280 0.1553 0.2120 -0.0057 -0.0018 0.0132  146 THR   A OG1 
3053 C  CG2 . THR   A 146 ? 0.1253 0.1438 0.2104 -0.0074 0.0010  0.0177  146 THR   A CG2 
3061 N  N   . VAL   A 147 ? 0.1211 0.1323 0.1987 -0.0003 0.0097  0.0168  147 VAL   A N   
3062 C  CA  . VAL   A 147 ? 0.1222 0.1345 0.2070 -0.0082 0.0202  0.0257  147 VAL   A CA  
3063 C  C   . VAL   A 147 ? 0.1260 0.1305 0.2255 -0.0114 0.0177  0.0322  147 VAL   A C   
3064 O  O   . VAL   A 147 ? 0.1288 0.1397 0.2340 -0.0146 0.0097  0.0316  147 VAL   A O   
3065 C  CB  . VAL   A 147 ? 0.1343 0.1386 0.1945 -0.0074 0.0187  0.0344  147 VAL   A CB  
3066 C  CG1 . VAL   A 147 ? 0.1627 0.1452 0.2036 -0.0032 0.0188  0.0427  147 VAL   A CG1 
3067 C  CG2 . VAL   A 147 ? 0.1358 0.1374 0.2001 -0.0064 0.0067  0.0257  147 VAL   A CG2 
3077 N  N   . ARG   A 148 ? 0.1265 0.1335 0.2205 -0.0114 0.0165  0.0447  148 ARG   A N   
3078 C  CA  . ARG   A 148 ? 0.1355 0.1345 0.2165 -0.0127 0.0104  0.0466  148 ARG   A CA  
3079 C  C   . ARG   A 148 ? 0.1434 0.1392 0.2159 -0.0134 0.0141  0.0619  148 ARG   A C   
3080 O  O   . ARG   A 148 ? 0.1711 0.1507 0.2438 -0.0200 0.0166  0.0539  148 ARG   A O   
3081 C  CB  . ARG   A 148 ? 0.1413 0.1323 0.2304 -0.0089 0.0203  0.0390  148 ARG   A CB  
3082 C  CG  . ARG   A 148 ? 0.1559 0.1344 0.2693 -0.0093 0.0337  0.0280  148 ARG   A CG  
3083 C  CD  . ARG   A 148 ? 0.1684 0.1345 0.2929 -0.0008 0.0461  0.0479  148 ARG   A CD  
3084 N  NE  . ARG   A 148 ? 0.1621 0.1445 0.2949 0.0094  0.0521  0.0551  148 ARG   A NE  
3085 C  CZ  . ARG   A 148 ? 0.1606 0.1361 0.2728 0.0090  0.0477  0.0491  148 ARG   A CZ  
3086 N  NH1 . ARG   A 148 ? 0.1674 0.1359 0.2760 -0.0027 0.0440  0.0214  148 ARG   A NH1 
3087 N  NH2 . ARG   A 148 ? 0.1544 0.1557 0.2706 0.0157  0.0429  0.0570  148 ARG   A NH2 
3101 N  N   . THR   A 149 ? 0.1435 0.1468 0.2053 -0.0121 0.0021  0.0544  149 THR   A N   
3102 C  CA  . THR   A 149 ? 0.1399 0.1523 0.2126 -0.0133 0.0064  0.0552  149 THR   A CA  
3103 C  C   . THR   A 149 ? 0.1388 0.1483 0.2003 -0.0179 0.0054  0.0567  149 THR   A C   
3104 O  O   . THR   A 149 ? 0.1368 0.1582 0.2150 -0.0184 0.0076  0.0486  149 THR   A O   
3105 C  CB  . THR   A 149 ? 0.1379 0.1640 0.2175 -0.0151 0.0072  0.0441  149 THR   A CB  
3106 O  OG1 . THR   A 149 ? 0.1426 0.1535 0.2304 -0.0221 0.0097  0.0405  149 THR   A OG1 
3107 C  CG2 . THR   A 149 ? 0.1353 0.1813 0.2251 -0.0095 -0.0046 0.0465  149 THR   A CG2 
3115 N  N   . ASN   A 150 ? 0.1416 0.1495 0.2094 -0.0050 0.0015  0.0578  150 ASN   A N   
3116 C  CA  . ASN   A 150 ? 0.1562 0.1606 0.2085 -0.0117 0.0100  0.0517  150 ASN   A CA  
3117 C  C   . ASN   A 150 ? 0.1360 0.1519 0.2052 -0.0127 0.0040  0.0507  150 ASN   A C   
3118 O  O   . ASN   A 150 ? 0.1459 0.1625 0.2376 -0.0165 -0.0075 0.0433  150 ASN   A O   
3119 C  CB  . ASN   A 150 ? 0.2073 0.1873 0.2270 -0.0167 0.0268  0.0654  150 ASN   A CB  
3120 C  CG  . ASN   A 150 ? 0.2579 0.2207 0.2784 -0.0118 0.0170  0.0811  150 ASN   A CG  
3121 O  OD1 . ASN   A 150 ? 0.2789 0.2259 0.3089 -0.0148 0.0245  0.0982  150 ASN   A OD1 
3122 N  ND2 . ASN   A 150 ? 0.2852 0.2503 0.3100 -0.0112 0.0027  0.0821  150 ASN   A ND2 
3129 N  N   . VAL   A 151 ? 0.1350 0.1417 0.1964 -0.0115 0.0003  0.0441  151 VAL   A N   
3130 C  CA  . VAL   A 151 ? 0.1406 0.1440 0.1964 -0.0161 0.0048  0.0444  151 VAL   A CA  
3131 C  C   . VAL   A 151 ? 0.1320 0.1391 0.2095 -0.0238 0.0104  0.0473  151 VAL   A C   
3132 O  O   . VAL   A 151 ? 0.1426 0.1476 0.2442 -0.0196 0.0114  0.0434  151 VAL   A O   
3133 C  CB  . VAL   A 151 ? 0.1689 0.1628 0.1958 -0.0035 0.0074  0.0422  151 VAL   A CB  
3134 C  CG1 . VAL   A 151 ? 0.1654 0.1833 0.2207 -0.0088 -0.0010 0.0436  151 VAL   A CG1 
3135 C  CG2 . VAL   A 151 ? 0.1764 0.1610 0.1900 -0.0003 0.0257  0.0389  151 VAL   A CG2 
3145 N  N   . TYR   A 152 ? 0.1273 0.1432 0.1998 -0.0191 0.0098  0.0450  152 TYR   A N   
3146 C  CA  . TYR   A 152 ? 0.1309 0.1526 0.1839 -0.0160 0.0081  0.0483  152 TYR   A CA  
3147 C  C   . TYR   A 152 ? 0.1325 0.1470 0.1789 -0.0171 0.0157  0.0476  152 TYR   A C   
3148 O  O   . TYR   A 152 ? 0.1410 0.1448 0.1886 -0.0243 0.0210  0.0384  152 TYR   A O   
3149 C  CB  . TYR   A 152 ? 0.1474 0.1615 0.1931 -0.0124 0.0180  0.0533  152 TYR   A CB  
3150 C  CG  . TYR   A 152 ? 0.1597 0.1804 0.1833 -0.0152 0.0247  0.0528  152 TYR   A CG  
3151 C  CD1 . TYR   A 152 ? 0.1784 0.2002 0.1989 -0.0009 0.0393  0.0587  152 TYR   A CD1 
3152 C  CD2 . TYR   A 152 ? 0.1680 0.1910 0.1743 -0.0258 0.0208  0.0468  152 TYR   A CD2 
3153 C  CE1 . TYR   A 152 ? 0.2107 0.2115 0.2090 -0.0016 0.0263  0.0665  152 TYR   A CE1 
3154 C  CE2 . TYR   A 152 ? 0.1945 0.2057 0.1871 -0.0254 0.0225  0.0542  152 TYR   A CE2 
3155 C  CZ  . TYR   A 152 ? 0.2250 0.2070 0.1898 -0.0149 0.0149  0.0753  152 TYR   A CZ  
3156 O  OH  . TYR   A 152 ? 0.2614 0.2279 0.2338 -0.0075 0.0176  0.0782  152 TYR   A OH  
3166 N  N   . LEU   A 153 ? 0.1263 0.1434 0.1944 -0.0184 0.0167  0.0496  153 LEU   A N   
3167 C  CA  . LEU   A 153 ? 0.1237 0.1407 0.2121 -0.0114 0.0157  0.0492  153 LEU   A CA  
3168 C  C   . LEU   A 153 ? 0.1256 0.1426 0.2146 -0.0064 0.0270  0.0468  153 LEU   A C   
3169 O  O   . LEU   A 153 ? 0.1314 0.1492 0.2547 -0.0067 0.0425  0.0439  153 LEU   A O   
3170 C  CB  . LEU   A 153 ? 0.1215 0.1507 0.2084 -0.0095 0.0045  0.0477  153 LEU   A CB  
3171 C  CG  . LEU   A 153 ? 0.1288 0.1513 0.2107 -0.0153 0.0110  0.0382  153 LEU   A CG  
3172 C  CD1 . LEU   A 153 ? 0.1351 0.1567 0.2178 -0.0145 -0.0041 0.0400  153 LEU   A CD1 
3173 C  CD2 . LEU   A 153 ? 0.1400 0.1546 0.2107 -0.0189 0.0244  0.0185  153 LEU   A CD2 
3185 N  N   A ALA   A 154 ? 0.1284 0.1381 0.2178 0.0005  0.0291  0.0530  154 ALA   A N   
3186 N  N   B ALA   A 154 ? 0.1229 0.1407 0.2135 -0.0129 0.0267  0.0436  154 ALA   A N   
3187 C  CA  A ALA   A 154 ? 0.1414 0.1417 0.2319 0.0075  0.0275  0.0516  154 ALA   A CA  
3188 C  CA  B ALA   A 154 ? 0.1307 0.1423 0.2191 -0.0159 0.0195  0.0379  154 ALA   A CA  
3189 C  C   A ALA   A 154 ? 0.1398 0.1431 0.2213 0.0122  0.0303  0.0559  154 ALA   A C   
3190 C  C   B ALA   A 154 ? 0.1335 0.1367 0.2151 -0.0151 0.0196  0.0432  154 ALA   A C   
3191 O  O   A ALA   A 154 ? 0.1419 0.1474 0.2203 0.0146  0.0314  0.0591  154 ALA   A O   
3192 O  O   B ALA   A 154 ? 0.1435 0.1413 0.2349 -0.0185 0.0197  0.0496  154 ALA   A O   
3193 C  CB  A ALA   A 154 ? 0.1488 0.1462 0.2445 0.0134  0.0166  0.0429  154 ALA   A CB  
3194 C  CB  B ALA   A 154 ? 0.1311 0.1522 0.2340 -0.0144 0.0183  0.0296  154 ALA   A CB  
3205 N  N   A VAL   A 155 ? 0.1518 0.1460 0.2256 0.0139  0.0257  0.0553  155 VAL   A N   
3206 N  N   B VAL   A 155 ? 0.1366 0.1332 0.2147 -0.0114 0.0213  0.0409  155 VAL   A N   
3207 C  CA  A VAL   A 155 ? 0.1690 0.1503 0.2263 0.0191  0.0116  0.0553  155 VAL   A CA  
3208 C  CA  B VAL   A 155 ? 0.1406 0.1316 0.2181 -0.0115 0.0223  0.0385  155 VAL   A CA  
3209 C  C   A VAL   A 155 ? 0.1814 0.1627 0.2377 0.0278  -0.0043 0.0535  155 VAL   A C   
3210 C  C   B VAL   A 155 ? 0.1443 0.1363 0.2140 -0.0102 0.0285  0.0356  155 VAL   A C   
3211 O  O   A VAL   A 155 ? 0.1797 0.1779 0.2482 0.0413  -0.0062 0.0373  155 VAL   A O   
3212 O  O   B VAL   A 155 ? 0.1428 0.1409 0.2187 -0.0054 0.0329  0.0328  155 VAL   A O   
3213 C  CB  A VAL   A 155 ? 0.1748 0.1558 0.2125 0.0228  0.0032  0.0416  155 VAL   A CB  
3214 C  CB  B VAL   A 155 ? 0.1411 0.1305 0.2103 -0.0025 0.0140  0.0315  155 VAL   A CB  
3215 C  CG1 A VAL   A 155 ? 0.1828 0.1620 0.2151 0.0245  -0.0021 0.0402  155 VAL   A CG1 
3216 C  CG1 B VAL   A 155 ? 0.1443 0.1342 0.2076 0.0088  0.0165  0.0191  155 VAL   A CG1 
3217 C  CG2 A VAL   A 155 ? 0.1800 0.1618 0.2184 0.0290  -0.0102 0.0374  155 VAL   A CG2 
3218 C  CG2 B VAL   A 155 ? 0.1494 0.1336 0.2236 0.0065  0.0005  0.0331  155 VAL   A CG2 
3237 N  N   A PHE   A 156 ? 0.1959 0.1619 0.2307 0.0227  -0.0115 0.0606  156 PHE   A N   
3238 N  N   B PHE   A 156 ? 0.1518 0.1435 0.2274 -0.0145 0.0313  0.0373  156 PHE   A N   
3239 C  CA  A PHE   A 156 ? 0.2209 0.1664 0.2584 0.0286  -0.0133 0.0610  156 PHE   A CA  
3240 C  CA  B PHE   A 156 ? 0.1613 0.1510 0.2290 -0.0144 0.0220  0.0376  156 PHE   A CA  
3241 C  C   A PHE   A 156 ? 0.2140 0.1686 0.2648 0.0367  -0.0122 0.0631  156 PHE   A C   
3242 C  C   B PHE   A 156 ? 0.1688 0.1627 0.2297 -0.0071 0.0261  0.0361  156 PHE   A C   
3243 O  O   A PHE   A 156 ? 0.2215 0.1816 0.2729 0.0382  -0.0045 0.0480  156 PHE   A O   
3244 O  O   B PHE   A 156 ? 0.1788 0.1826 0.2426 0.0042  0.0278  0.0357  156 PHE   A O   
3245 C  CB  A PHE   A 156 ? 0.2532 0.1768 0.2824 0.0273  -0.0223 0.0674  156 PHE   A CB  
3246 C  CB  B PHE   A 156 ? 0.1653 0.1476 0.2223 -0.0120 0.0162  0.0476  156 PHE   A CB  
3247 C  CG  A PHE   A 156 ? 0.2824 0.1891 0.3167 0.0435  -0.0361 0.0561  156 PHE   A CG  
3248 C  CG  B PHE   A 156 ? 0.1684 0.1508 0.2143 -0.0071 0.0081  0.0543  156 PHE   A CG  
3249 C  CD1 A PHE   A 156 ? 0.2986 0.2003 0.3344 0.0491  -0.0333 0.0484  156 PHE   A CD1 
3250 C  CD1 B PHE   A 156 ? 0.1667 0.1623 0.2280 0.0003  0.0084  0.0566  156 PHE   A CD1 
3251 C  CD2 A PHE   A 156 ? 0.2948 0.1996 0.3322 0.0562  -0.0485 0.0517  156 PHE   A CD2 
3252 C  CD2 B PHE   A 156 ? 0.1773 0.1512 0.2241 -0.0061 0.0078  0.0524  156 PHE   A CD2 
3253 C  CE1 A PHE   A 156 ? 0.3106 0.2087 0.3558 0.0534  -0.0299 0.0394  156 PHE   A CE1 
3254 C  CE1 B PHE   A 156 ? 0.1680 0.1685 0.2411 -0.0002 0.0101  0.0449  156 PHE   A CE1 
3255 C  CE2 A PHE   A 156 ? 0.3086 0.2084 0.3480 0.0625  -0.0471 0.0373  156 PHE   A CE2 
3256 C  CE2 B PHE   A 156 ? 0.1830 0.1557 0.2399 -0.0093 0.0015  0.0476  156 PHE   A CE2 
3257 C  CZ  A PHE   A 156 ? 0.3131 0.2102 0.3567 0.0634  -0.0368 0.0334  156 PHE   A CZ  
3258 C  CZ  B PHE   A 156 ? 0.1752 0.1605 0.2463 -0.0090 0.0072  0.0475  156 PHE   A CZ  
3277 N  N   A ASP   A 157 ? 0.2056 0.1642 0.2580 0.0336  -0.0170 0.0709  157 ASP   A N   
3278 N  N   B ASP   A 157 ? 0.1823 0.1601 0.2450 -0.0155 0.0146  0.0425  157 ASP   A N   
3279 C  CA  A ASP   A 157 ? 0.2108 0.1795 0.2691 0.0236  -0.0211 0.0745  157 ASP   A CA  
3280 C  CA  B ASP   A 157 ? 0.1952 0.1633 0.2485 -0.0164 -0.0013 0.0351  157 ASP   A CA  
3281 C  C   A ASP   A 157 ? 0.1983 0.1931 0.2815 0.0312  -0.0030 0.0735  157 ASP   A C   
3282 C  C   B ASP   A 157 ? 0.1811 0.1627 0.2400 -0.0140 0.0036  0.0392  157 ASP   A C   
3283 O  O   A ASP   A 157 ? 0.1888 0.1845 0.2713 0.0307  0.0049  0.0817  157 ASP   A O   
3284 O  O   B ASP   A 157 ? 0.1738 0.1552 0.2314 -0.0105 0.0083  0.0344  157 ASP   A O   
3285 C  CB  A ASP   A 157 ? 0.2273 0.1858 0.2860 0.0162  -0.0397 0.0707  157 ASP   A CB  
3286 C  CB  B ASP   A 157 ? 0.2169 0.1663 0.2582 -0.0165 -0.0138 0.0284  157 ASP   A CB  
3287 C  CG  A ASP   A 157 ? 0.2492 0.1965 0.3181 0.0200  -0.0529 0.0657  157 ASP   A CG  
3288 C  CG  B ASP   A 157 ? 0.2406 0.1660 0.2715 -0.0131 -0.0358 0.0175  157 ASP   A CG  
3289 O  OD1 A ASP   A 157 ? 0.2753 0.2103 0.3453 0.0183  -0.0707 0.0457  157 ASP   A OD1 
3290 O  OD1 B ASP   A 157 ? 0.2597 0.1623 0.2810 -0.0144 -0.0594 0.0150  157 ASP   A OD1 
3291 O  OD2 A ASP   A 157 ? 0.2392 0.1874 0.3355 0.0208  -0.0460 0.0756  157 ASP   A OD2 
3292 O  OD2 B ASP   A 157 ? 0.2380 0.1710 0.2738 -0.0095 -0.0352 0.0115  157 ASP   A OD2 
3301 N  N   A LYS   A 158 ? 0.2068 0.2191 0.3089 0.0379  0.0072  0.0626  158 LYS   A N   
3302 N  N   B LYS   A 158 ? 0.1792 0.1747 0.2521 -0.0136 0.0066  0.0437  158 LYS   A N   
3303 C  CA  A LYS   A 158 ? 0.2112 0.2394 0.3428 0.0431  0.0202  0.0643  158 LYS   A CA  
3304 C  CA  B LYS   A 158 ? 0.1804 0.1944 0.2729 -0.0042 0.0144  0.0393  158 LYS   A CA  
3305 C  C   A LYS   A 158 ? 0.2015 0.2352 0.3375 0.0463  0.0104  0.0739  158 LYS   A C   
3306 C  C   B LYS   A 158 ? 0.1613 0.1871 0.2702 -0.0051 -0.0013 0.0399  158 LYS   A C   
3307 O  O   A LYS   A 158 ? 0.2009 0.2374 0.3423 0.0466  0.0268  0.0666  158 LYS   A O   
3308 O  O   B LYS   A 158 ? 0.1473 0.1885 0.2736 -0.0084 0.0065  0.0511  158 LYS   A O   
3309 C  CB  A LYS   A 158 ? 0.2273 0.2526 0.3686 0.0385  0.0505  0.0679  158 LYS   A CB  
3310 C  CB  B LYS   A 158 ? 0.2041 0.2241 0.3026 0.0019  0.0344  0.0432  158 LYS   A CB  
3311 C  CG  A LYS   A 158 ? 0.2419 0.2643 0.3976 0.0354  0.0685  0.0748  158 LYS   A CG  
3312 C  CG  B LYS   A 158 ? 0.2302 0.2498 0.3413 0.0099  0.0434  0.0473  158 LYS   A CG  
3313 C  CD  A LYS   A 158 ? 0.2488 0.2701 0.4180 0.0289  0.0953  0.0883  158 LYS   A CD  
3314 C  CD  B LYS   A 158 ? 0.2506 0.2672 0.3702 0.0167  0.0534  0.0505  158 LYS   A CD  
3315 C  CE  A LYS   A 158 ? 0.2486 0.2697 0.4285 0.0216  0.1160  0.1027  158 LYS   A CE  
3316 C  CE  B LYS   A 158 ? 0.2618 0.2752 0.3851 0.0225  0.0612  0.0575  158 LYS   A CE  
3317 N  NZ  A LYS   A 158 ? 0.2442 0.2672 0.4349 0.0119  0.1297  0.1061  158 LYS   A NZ  
3318 N  NZ  B LYS   A 158 ? 0.2707 0.2813 0.3994 0.0234  0.0624  0.0632  158 LYS   A NZ  
3345 N  N   A ASN   A 159 ? 0.1964 0.2276 0.3501 0.0452  -0.0149 0.0785  159 ASN   A N   
3346 N  N   B ASN   A 159 ? 0.1703 0.1870 0.2866 -0.0048 -0.0234 0.0319  159 ASN   A N   
3347 C  CA  A ASN   A 159 ? 0.1989 0.2272 0.3582 0.0380  -0.0240 0.0912  159 ASN   A CA  
3348 C  CA  B ASN   A 159 ? 0.1748 0.1878 0.3013 -0.0001 -0.0412 0.0360  159 ASN   A CA  
3349 C  C   A ASN   A 159 ? 0.1867 0.2219 0.3439 0.0264  -0.0034 0.0811  159 ASN   A C   
3350 C  C   B ASN   A 159 ? 0.1568 0.1758 0.2858 -0.0045 -0.0427 0.0460  159 ASN   A C   
3351 O  O   A ASN   A 159 ? 0.1810 0.2155 0.3401 0.0281  -0.0013 0.0572  159 ASN   A O   
3352 O  O   B ASN   A 159 ? 0.1477 0.1768 0.2891 -0.0086 -0.0523 0.0524  159 ASN   A O   
3353 C  CB  A ASN   A 159 ? 0.2175 0.2394 0.3911 0.0325  -0.0286 0.1063  159 ASN   A CB  
3354 C  CB  B ASN   A 159 ? 0.2045 0.2062 0.3376 0.0038  -0.0470 0.0265  159 ASN   A CB  
3355 C  CG  A ASN   A 159 ? 0.2373 0.2617 0.4433 0.0256  -0.0159 0.1013  159 ASN   A CG  
3356 C  CG  B ASN   A 159 ? 0.2351 0.2286 0.3806 0.0035  -0.0489 0.0116  159 ASN   A CG  
3357 O  OD1 A ASN   A 159 ? 0.2358 0.2729 0.4541 0.0150  0.0006  0.1030  159 ASN   A OD1 
3358 O  OD1 B ASN   A 159 ? 0.2521 0.2400 0.4041 0.0061  -0.0470 0.0026  159 ASN   A OD1 
3359 N  ND2 A ASN   A 159 ? 0.2424 0.2646 0.4527 0.0270  -0.0197 0.0986  159 ASN   A ND2 
3360 N  ND2 B ASN   A 159 ? 0.2464 0.2402 0.3965 0.0047  -0.0531 0.0074  159 ASN   A ND2 
3373 N  N   A LEU   A 160 ? 0.1783 0.2187 0.3268 0.0237  -0.0021 0.0946  160 LEU   A N   
3374 N  N   B LEU   A 160 ? 0.1512 0.1680 0.2805 -0.0096 -0.0389 0.0555  160 LEU   A N   
3375 C  CA  A LEU   A 160 ? 0.1789 0.2200 0.3092 0.0121  0.0052  0.1178  160 LEU   A CA  
3376 C  CA  B LEU   A 160 ? 0.1519 0.1713 0.2735 -0.0107 -0.0196 0.0742  160 LEU   A CA  
3377 C  C   A LEU   A 160 ? 0.1621 0.2337 0.3071 0.0120  0.0115  0.1361  160 LEU   A C   
3378 C  C   B LEU   A 160 ? 0.1418 0.1840 0.2676 -0.0024 -0.0030 0.0822  160 LEU   A C   
3379 O  O   A LEU   A 160 ? 0.1589 0.2385 0.3332 0.0116  0.0118  0.1463  160 LEU   A O   
3380 O  O   B LEU   A 160 ? 0.1417 0.1775 0.2792 -0.0082 -0.0066 0.1023  160 LEU   A O   
3381 C  CB  A LEU   A 160 ? 0.1926 0.2172 0.2953 0.0004  0.0125  0.1069  160 LEU   A CB  
3382 C  CB  B LEU   A 160 ? 0.1658 0.1716 0.2601 -0.0216 -0.0197 0.0742  160 LEU   A CB  
3383 C  CG  A LEU   A 160 ? 0.2046 0.2216 0.2952 -0.0110 0.0171  0.0745  160 LEU   A CG  
3384 C  CG  B LEU   A 160 ? 0.1745 0.1789 0.2622 -0.0235 -0.0141 0.0668  160 LEU   A CG  
3385 C  CD1 A LEU   A 160 ? 0.2126 0.2250 0.2946 -0.0143 0.0197  0.0523  160 LEU   A CD1 
3386 C  CD1 B LEU   A 160 ? 0.1808 0.1854 0.2720 -0.0190 -0.0067 0.0625  160 LEU   A CD1 
3387 C  CD2 A LEU   A 160 ? 0.2071 0.2214 0.2939 -0.0148 0.0225  0.0631  160 LEU   A CD2 
3388 C  CD2 B LEU   A 160 ? 0.1808 0.1791 0.2608 -0.0261 -0.0092 0.0607  160 LEU   A CD2 
3411 N  N   A TYR   A 161 ? 0.1566 0.2404 0.3038 0.0091  0.0142  0.1253  161 TYR   A N   
3412 N  N   B TYR   A 161 ? 0.1375 0.2040 0.2568 0.0113  0.0116  0.0850  161 TYR   A N   
3413 C  CA  A TYR   A 161 ? 0.1532 0.2407 0.3022 -0.0012 0.0126  0.1204  161 TYR   A CA  
3414 C  CA  B TYR   A 161 ? 0.1387 0.2114 0.2523 0.0135  0.0233  0.0881  161 TYR   A CA  
3415 C  C   A TYR   A 161 ? 0.1422 0.2574 0.3124 -0.0020 0.0101  0.1216  161 TYR   A C   
3416 C  C   B TYR   A 161 ? 0.1444 0.2367 0.2622 0.0148  0.0267  0.0875  161 TYR   A C   
3417 O  O   A TYR   A 161 ? 0.1300 0.2646 0.3077 -0.0075 0.0111  0.1212  161 TYR   A O   
3418 O  O   B TYR   A 161 ? 0.1385 0.2418 0.2635 0.0129  0.0340  0.0878  161 TYR   A O   
3419 C  CB  A TYR   A 161 ? 0.1648 0.2278 0.3171 -0.0061 0.0042  0.1018  161 TYR   A CB  
3420 C  CB  B TYR   A 161 ? 0.1375 0.1940 0.2602 0.0148  0.0284  0.0794  161 TYR   A CB  
3421 C  CG  A TYR   A 161 ? 0.1670 0.2162 0.3164 -0.0080 -0.0098 0.0804  161 TYR   A CG  
3422 C  CG  B TYR   A 161 ? 0.1324 0.1782 0.2547 0.0169  0.0245  0.0644  161 TYR   A CG  
3423 C  CD1 A TYR   A 161 ? 0.1682 0.2102 0.3201 -0.0077 -0.0108 0.0704  161 TYR   A CD1 
3424 C  CD1 B TYR   A 161 ? 0.1320 0.1735 0.2577 0.0123  0.0254  0.0536  161 TYR   A CD1 
3425 C  CD2 A TYR   A 161 ? 0.1686 0.2117 0.3165 -0.0076 -0.0184 0.0639  161 TYR   A CD2 
3426 C  CD2 B TYR   A 161 ? 0.1320 0.1697 0.2502 0.0227  0.0200  0.0571  161 TYR   A CD2 
3427 C  CE1 A TYR   A 161 ? 0.1747 0.1947 0.3167 -0.0074 -0.0103 0.0697  161 TYR   A CE1 
3428 C  CE1 B TYR   A 161 ? 0.1412 0.1682 0.2547 0.0090  0.0251  0.0523  161 TYR   A CE1 
3429 C  CE2 A TYR   A 161 ? 0.1732 0.1969 0.3111 -0.0084 -0.0227 0.0626  161 TYR   A CE2 
3430 C  CE2 B TYR   A 161 ? 0.1391 0.1651 0.2484 0.0097  0.0237  0.0534  161 TYR   A CE2 
3431 C  CZ  A TYR   A 161 ? 0.1826 0.1840 0.3185 -0.0117 -0.0199 0.0706  161 TYR   A CZ  
3432 C  CZ  B TYR   A 161 ? 0.1512 0.1629 0.2546 0.0034  0.0219  0.0482  161 TYR   A CZ  
3433 O  OH  A TYR   A 161 ? 0.1989 0.1622 0.3298 -0.0190 -0.0220 0.0828  161 TYR   A OH  
3434 O  OH  B TYR   A 161 ? 0.1722 0.1595 0.2664 -0.0032 0.0149  0.0378  161 TYR   A OH  
3453 N  N   A ASP   A 162 ? 0.1394 0.2651 0.3299 0.0007  0.0124  0.1260  162 ASP   A N   
3454 N  N   B ASP   A 162 ? 0.1518 0.2555 0.2785 0.0156  0.0256  0.0841  162 ASP   A N   
3455 C  CA  A ASP   A 162 ? 0.1358 0.2787 0.3328 -0.0019 0.0097  0.1206  162 ASP   A CA  
3456 C  CA  B ASP   A 162 ? 0.1590 0.2759 0.2866 0.0142  0.0289  0.0773  162 ASP   A CA  
3457 C  C   A ASP   A 162 ? 0.1232 0.3031 0.3162 -0.0068 0.0099  0.1226  162 ASP   A C   
3458 C  C   B ASP   A 162 ? 0.1664 0.2947 0.2799 0.0135  0.0281  0.0799  162 ASP   A C   
3459 O  O   A ASP   A 162 ? 0.1206 0.3048 0.3259 -0.0138 0.0160  0.1158  162 ASP   A O   
3460 O  O   B ASP   A 162 ? 0.1706 0.2955 0.2842 0.0150  0.0348  0.0747  162 ASP   A O   
3461 C  CB  A ASP   A 162 ? 0.1490 0.2702 0.3543 -0.0020 0.0125  0.1092  162 ASP   A CB  
3462 C  CB  B ASP   A 162 ? 0.1592 0.2765 0.3089 0.0109  0.0352  0.0697  162 ASP   A CB  
3463 C  CG  A ASP   A 162 ? 0.1690 0.2669 0.3704 0.0021  0.0164  0.0948  162 ASP   A CG  
3464 C  CG  B ASP   A 162 ? 0.1636 0.2807 0.3308 0.0081  0.0377  0.0674  162 ASP   A CG  
3465 O  OD1 A ASP   A 162 ? 0.1844 0.2717 0.3855 0.0027  0.0207  0.0846  162 ASP   A OD1 
3466 O  OD1 B ASP   A 162 ? 0.1695 0.2811 0.3329 0.0108  0.0411  0.0719  162 ASP   A OD1 
3467 O  OD2 A ASP   A 162 ? 0.1793 0.2633 0.3826 0.0049  0.0287  0.0888  162 ASP   A OD2 
3468 O  OD2 B ASP   A 162 ? 0.1707 0.2835 0.3446 0.0103  0.0339  0.0662  162 ASP   A OD2 
3477 N  N   A LYS   A 163 ? 0.1323 0.3262 0.3168 -0.0098 -0.0118 0.1191  163 LYS   A N   
3478 N  N   B LYS   A 163 ? 0.1781 0.3135 0.2913 0.0092  0.0108  0.0836  163 LYS   A N   
3479 C  CA  A LYS   A 163 ? 0.1494 0.3465 0.3057 -0.0145 -0.0124 0.1181  163 LYS   A CA  
3480 C  CA  B LYS   A 163 ? 0.1878 0.3309 0.2916 0.0006  0.0030  0.0870  163 LYS   A CA  
3481 C  C   A LYS   A 163 ? 0.1432 0.3441 0.2953 -0.0145 0.0065  0.1155  163 LYS   A C   
3482 C  C   B LYS   A 163 ? 0.1672 0.3334 0.2898 -0.0086 0.0112  0.0961  163 LYS   A C   
3483 O  O   A LYS   A 163 ? 0.1288 0.3584 0.2921 -0.0210 0.0169  0.1122  163 LYS   A O   
3484 O  O   B LYS   A 163 ? 0.1681 0.3425 0.2865 -0.0105 0.0243  0.0889  163 LYS   A O   
3485 C  CB  A LYS   A 163 ? 0.1899 0.3702 0.3445 -0.0075 -0.0282 0.1126  163 LYS   A CB  
3486 C  CB  B LYS   A 163 ? 0.2213 0.3467 0.3249 0.0046  -0.0073 0.0795  163 LYS   A CB  
3487 C  CG  A LYS   A 163 ? 0.2322 0.3907 0.3914 -0.0087 -0.0226 0.1025  163 LYS   A CG  
3488 C  CG  B LYS   A 163 ? 0.2530 0.3614 0.3600 0.0049  -0.0098 0.0700  163 LYS   A CG  
3489 C  CD  A LYS   A 163 ? 0.2691 0.4074 0.4426 -0.0087 -0.0213 0.0906  163 LYS   A CD  
3490 C  CD  B LYS   A 163 ? 0.2807 0.3737 0.4027 0.0048  -0.0116 0.0591  163 LYS   A CD  
3491 C  CE  A LYS   A 163 ? 0.3058 0.4187 0.4819 -0.0104 -0.0173 0.0870  163 LYS   A CE  
3492 C  CE  B LYS   A 163 ? 0.3024 0.3822 0.4359 0.0035  -0.0097 0.0542  163 LYS   A CE  
3493 N  NZ  A LYS   A 163 ? 0.3218 0.4244 0.5049 -0.0114 -0.0139 0.0899  163 LYS   A NZ  
3494 N  NZ  B LYS   A 163 ? 0.3134 0.3866 0.4549 0.0024  -0.0068 0.0533  163 LYS   A NZ  
3521 N  N   . LEU   A 164 ? 0.1429 0.3239 0.2939 -0.0161 0.0006  0.1089  164 LEU   A N   
3522 C  CA  . LEU   A 164 ? 0.1407 0.2969 0.2893 -0.0220 0.0135  0.1083  164 LEU   A CA  
3523 C  C   . LEU   A 164 ? 0.1487 0.2897 0.2861 -0.0195 0.0169  0.0993  164 LEU   A C   
3524 O  O   . LEU   A 164 ? 0.1550 0.2977 0.2950 -0.0252 0.0393  0.0771  164 LEU   A O   
3525 C  CB  . LEU   A 164 ? 0.1407 0.2848 0.2911 -0.0264 0.0144  0.1110  164 LEU   A CB  
3526 C  CG  . LEU   A 164 ? 0.1488 0.2778 0.2942 -0.0204 0.0131  0.1059  164 LEU   A CG  
3527 C  CD1 . LEU   A 164 ? 0.1466 0.2735 0.3059 -0.0202 0.0000  0.0987  164 LEU   A CD1 
3528 C  CD2 . LEU   A 164 ? 0.1642 0.2788 0.2970 -0.0142 0.0220  0.1019  164 LEU   A CD2 
3541 N  N   . VAL   A 165 ? 0.1454 0.2775 0.2800 -0.0219 0.0142  0.1026  165 VAL   A N   
3542 C  CA  . VAL   A 165 ? 0.1530 0.2732 0.2771 -0.0220 0.0227  0.1023  165 VAL   A CA  
3543 C  C   . VAL   A 165 ? 0.1470 0.2866 0.2760 -0.0135 0.0230  0.1062  165 VAL   A C   
3544 O  O   . VAL   A 165 ? 0.1469 0.2883 0.2719 -0.0146 0.0243  0.1038  165 VAL   A O   
3545 C  CB  . VAL   A 165 ? 0.1668 0.2656 0.2859 -0.0237 0.0272  0.0869  165 VAL   A CB  
3546 C  CG1 . VAL   A 165 ? 0.1736 0.2694 0.2966 -0.0288 0.0319  0.0769  165 VAL   A CG1 
3547 C  CG2 . VAL   A 165 ? 0.1826 0.2635 0.2971 -0.0208 0.0189  0.0826  165 VAL   A CG2 
3557 N  N   . SER   A 166 ? 0.1358 0.3016 0.2901 -0.0101 0.0237  0.1003  166 SER   A N   
3558 C  CA  . SER   A 166 ? 0.1378 0.3332 0.3021 -0.0099 0.0258  0.0828  166 SER   A CA  
3559 C  C   . SER   A 166 ? 0.1420 0.3627 0.2917 -0.0234 0.0083  0.0727  166 SER   A C   
3560 O  O   . SER   A 166 ? 0.1681 0.3816 0.3319 -0.0393 0.0148  0.0393  166 SER   A O   
3561 C  CB  . SER   A 166 ? 0.1670 0.3459 0.3508 0.0095  0.0164  0.0605  166 SER   A CB  
3562 O  OG  . SER   A 166 ? 0.2208 0.3593 0.3994 0.0062  0.0112  0.0638  166 SER   A OG  
3568 N  N   . SER   A 167 ? 0.1494 0.3763 0.2597 -0.0058 -0.0039 0.0801  167 SER   A N   
3569 C  CA  . SER   A 167 ? 0.1779 0.3883 0.2623 0.0052  -0.0056 0.0668  167 SER   A CA  
3570 C  C   . SER   A 167 ? 0.1852 0.3878 0.2643 0.0156  0.0062  0.0548  167 SER   A C   
3571 O  O   . SER   A 167 ? 0.2020 0.3896 0.2756 0.0193  -0.0012 0.0448  167 SER   A O   
3572 C  CB  . SER   A 167 ? 0.1864 0.4013 0.2764 0.0081  0.0113  0.0694  167 SER   A CB  
3573 O  OG  . SER   A 167 ? 0.1897 0.4067 0.2937 0.0083  0.0252  0.0826  167 SER   A OG  
3579 N  N   . PHE   A 168 ? 0.1752 0.3857 0.2600 0.0273  0.0104  0.0521  168 PHE   A N   
3580 C  CA  . PHE   A 168 ? 0.1748 0.3838 0.2751 0.0204  0.0244  0.0395  168 PHE   A CA  
3581 C  C   . PHE   A 168 ? 0.1978 0.4169 0.3258 0.0044  0.0683  0.0197  168 PHE   A C   
3582 O  O   . PHE   A 168 ? 0.1957 0.4273 0.3530 -0.0140 0.0769  0.0320  168 PHE   A O   
3583 C  CB  . PHE   A 168 ? 0.1687 0.3516 0.2605 0.0081  0.0005  0.0458  168 PHE   A CB  
3584 C  CG  . PHE   A 168 ? 0.1589 0.3238 0.2428 -0.0044 -0.0078 0.0589  168 PHE   A CG  
3585 C  CD1 . PHE   A 168 ? 0.1628 0.3222 0.2522 -0.0126 -0.0091 0.0722  168 PHE   A CD1 
3586 C  CD2 . PHE   A 168 ? 0.1548 0.3079 0.2413 -0.0063 0.0030  0.0500  168 PHE   A CD2 
3587 C  CE1 . PHE   A 168 ? 0.1557 0.3164 0.2513 -0.0147 -0.0130 0.0753  168 PHE   A CE1 
3588 C  CE2 . PHE   A 168 ? 0.1590 0.3034 0.2519 -0.0059 0.0059  0.0587  168 PHE   A CE2 
3589 C  CZ  . PHE   A 168 ? 0.1590 0.3105 0.2573 -0.0141 -0.0017 0.0676  168 PHE   A CZ  
3599 N  N   . LEU   A 169 ? 0.2696 0.4412 0.3991 -0.0093 0.0530  -0.0101 169 LEU   A N   
3600 C  CA  . LEU   A 169 ? 0.3718 0.4720 0.5095 -0.0174 0.0058  -0.0297 169 LEU   A CA  
3601 C  C   . LEU   A 169 ? 0.4107 0.4803 0.5448 -0.0225 -0.0076 -0.0279 169 LEU   A C   
3602 O  O   . LEU   A 169 ? 0.4246 0.4869 0.5525 -0.0227 -0.0073 -0.0287 169 LEU   A O   
3603 C  CB  . LEU   A 169 ? 0.4243 0.4931 0.5478 -0.0226 -0.0177 -0.0512 169 LEU   A CB  
3604 C  CG  . LEU   A 169 ? 0.4697 0.5111 0.5844 -0.0289 -0.0327 -0.0748 169 LEU   A CG  
3605 C  CD1 . LEU   A 169 ? 0.4817 0.5162 0.6014 -0.0313 -0.0370 -0.0821 169 LEU   A CD1 
3606 C  CD2 . LEU   A 169 ? 0.4845 0.5189 0.5958 -0.0305 -0.0361 -0.0831 169 LEU   A CD2 
3607 O  OXT . LEU   A 169 ? 0.4115 0.4788 0.5460 -0.0267 -0.0060 -0.0290 169 LEU   A OXT 
3619 N  N   A SER   B 1   ? 0.3727 0.3529 0.3750 -0.1023 -0.0789 0.0335  1   SER   B N   
3620 N  N   B SER   B 1   ? 0.3366 0.3405 0.3560 -0.0869 -0.0586 0.0301  1   SER   B N   
3621 C  CA  A SER   B 1   ? 0.3669 0.3561 0.3843 -0.1059 -0.0788 0.0312  1   SER   B CA  
3622 C  CA  B SER   B 1   ? 0.3306 0.3443 0.3587 -0.0884 -0.0579 0.0281  1   SER   B CA  
3623 C  C   A SER   B 1   ? 0.3448 0.3542 0.3680 -0.1085 -0.0818 0.0502  1   SER   B C   
3624 C  C   B SER   B 1   ? 0.3114 0.3438 0.3367 -0.0881 -0.0649 0.0424  1   SER   B C   
3625 O  O   A SER   B 1   ? 0.3555 0.3585 0.3526 -0.1037 -0.0754 0.0470  1   SER   B O   
3626 O  O   B SER   B 1   ? 0.3145 0.3447 0.3177 -0.0880 -0.0666 0.0377  1   SER   B O   
3627 C  CB  A SER   B 1   ? 0.3802 0.3586 0.3925 -0.1058 -0.0739 0.0160  1   SER   B CB  
3628 C  CB  B SER   B 1   ? 0.3409 0.3469 0.3705 -0.0882 -0.0500 0.0155  1   SER   B CB  
3629 O  OG  A SER   B 1   ? 0.3919 0.3661 0.4331 -0.1039 -0.0701 0.0127  1   SER   B OG  
3630 O  OG  B SER   B 1   ? 0.3490 0.3526 0.4032 -0.0877 -0.0468 0.0128  1   SER   B OG  
3645 N  N   A MET   B 2   ? 0.3163 0.3470 0.3567 -0.1120 -0.0839 0.0845  2   MET   B N   
3646 N  N   B MET   B 2   ? 0.2937 0.3422 0.3243 -0.0840 -0.0650 0.0709  2   MET   B N   
3647 C  CA  A MET   B 2   ? 0.2938 0.3444 0.3639 -0.1007 -0.0856 0.1033  2   MET   B CA  
3648 C  CA  B MET   B 2   ? 0.2800 0.3413 0.3200 -0.0701 -0.0651 0.0896  2   MET   B CA  
3649 C  C   A MET   B 2   ? 0.2518 0.3193 0.3165 -0.0911 -0.1000 0.1264  2   MET   B C   
3650 C  C   B MET   B 2   ? 0.2564 0.3257 0.2887 -0.0603 -0.0598 0.1019  2   MET   B C   
3651 O  O   A MET   B 2   ? 0.2423 0.3273 0.3031 -0.0833 -0.1163 0.1361  2   MET   B O   
3652 O  O   B MET   B 2   ? 0.2558 0.3374 0.2925 -0.0533 -0.0523 0.1025  2   MET   B O   
3653 C  CB  A MET   B 2   ? 0.3237 0.3753 0.4403 -0.0814 -0.0637 0.0806  2   MET   B CB  
3654 C  CB  B MET   B 2   ? 0.2955 0.3598 0.3618 -0.0563 -0.0640 0.0874  2   MET   B CB  
3655 C  CG  A MET   B 2   ? 0.3536 0.4033 0.5098 -0.0585 -0.0420 0.0646  2   MET   B CG  
3656 C  CG  B MET   B 2   ? 0.3100 0.3781 0.3941 -0.0413 -0.0603 0.0957  2   MET   B CG  
3657 S  SD  A MET   B 2   ? 0.3814 0.4287 0.5844 -0.0379 -0.0278 0.0540  2   MET   B SD  
3658 S  SD  B MET   B 2   ? 0.3243 0.3979 0.4248 -0.0276 -0.0606 0.1033  2   MET   B SD  
3659 C  CE  A MET   B 2   ? 0.3875 0.4346 0.5837 -0.0347 -0.0238 0.0566  2   MET   B CE  
3660 C  CE  B MET   B 2   ? 0.3260 0.4025 0.4348 -0.0278 -0.0589 0.0943  2   MET   B CE  
3679 N  N   A VAL   B 3   ? 0.2228 0.2792 0.2893 -0.0959 -0.0885 0.1333  3   VAL   B N   
3680 N  N   B VAL   B 3   ? 0.2337 0.2943 0.2650 -0.0618 -0.0571 0.1071  3   VAL   B N   
3681 C  CA  A VAL   B 3   ? 0.2132 0.2474 0.2822 -0.0836 -0.0779 0.1164  3   VAL   B CA  
3682 C  CA  B VAL   B 3   ? 0.2185 0.2641 0.2566 -0.0562 -0.0515 0.0951  3   VAL   B CA  
3683 C  C   A VAL   B 3   ? 0.1931 0.2318 0.2423 -0.0690 -0.0698 0.1005  3   VAL   B C   
3684 C  C   B VAL   B 3   ? 0.1979 0.2459 0.2296 -0.0518 -0.0496 0.0914  3   VAL   B C   
3685 O  O   A VAL   B 3   ? 0.1893 0.2250 0.2317 -0.0649 -0.0683 0.1079  3   VAL   B O   
3686 O  O   B VAL   B 3   ? 0.1938 0.2499 0.2277 -0.0384 -0.0473 0.0933  3   VAL   B O   
3687 C  CB  A VAL   B 3   ? 0.2304 0.2456 0.3289 -0.0791 -0.0766 0.0952  3   VAL   B CB  
3688 C  CB  B VAL   B 3   ? 0.2267 0.2546 0.2796 -0.0530 -0.0479 0.0850  3   VAL   B CB  
3689 C  CG1 A VAL   B 3   ? 0.2391 0.2404 0.3468 -0.0823 -0.0755 0.0896  3   VAL   B CG1 
3690 C  CG1 B VAL   B 3   ? 0.2313 0.2494 0.2903 -0.0560 -0.0459 0.0800  3   VAL   B CG1 
3691 C  CG2 A VAL   B 3   ? 0.2337 0.2509 0.3475 -0.0730 -0.0657 0.0974  3   VAL   B CG2 
3692 C  CG2 B VAL   B 3   ? 0.2271 0.2536 0.2876 -0.0502 -0.0444 0.0874  3   VAL   B CG2 
3711 N  N   . ASN   B 4   ? 0.1848 0.2233 0.2163 -0.0593 -0.0604 0.0819  4   ASN   B N   
3712 C  CA  . ASN   B 4   ? 0.1853 0.2191 0.1803 -0.0534 -0.0464 0.0439  4   ASN   B CA  
3713 C  C   . ASN   B 4   ? 0.1890 0.2340 0.1809 -0.0564 -0.0384 0.0326  4   ASN   B C   
3714 O  O   . ASN   B 4   ? 0.1889 0.2372 0.1994 -0.0521 -0.0329 0.0108  4   ASN   B O   
3715 C  CB  . ASN   B 4   ? 0.1854 0.2119 0.1621 -0.0465 -0.0534 0.0336  4   ASN   B CB  
3716 C  CG  . ASN   B 4   ? 0.1851 0.1968 0.1583 -0.0460 -0.0489 0.0281  4   ASN   B CG  
3717 O  OD1 . ASN   B 4   ? 0.1853 0.1825 0.1608 -0.0465 -0.0478 0.0257  4   ASN   B OD1 
3718 N  ND2 . ASN   B 4   ? 0.2022 0.1994 0.1783 -0.0256 -0.0333 0.0235  4   ASN   B ND2 
3726 N  N   . SER   B 5   ? 0.2018 0.2564 0.1916 -0.0607 -0.0375 0.0324  5   SER   B N   
3727 C  CA  . SER   B 5   ? 0.2317 0.2873 0.2140 -0.0528 -0.0160 0.0333  5   SER   B CA  
3728 C  C   . SER   B 5   ? 0.2518 0.2927 0.2498 -0.0682 0.0150  0.0307  5   SER   B C   
3729 O  O   . SER   B 5   ? 0.2701 0.2898 0.3231 -0.0641 0.0572  0.0291  5   SER   B O   
3730 C  CB  . SER   B 5   ? 0.2495 0.3071 0.2345 -0.0391 -0.0169 0.0385  5   SER   B CB  
3731 O  OG  . SER   B 5   ? 0.2746 0.3272 0.2864 -0.0277 -0.0136 0.0408  5   SER   B OG  
3737 N  N   . PHE   B 6   ? 0.2667 0.3084 0.2292 -0.0729 0.0230  0.0400  6   PHE   B N   
3738 C  CA  . PHE   B 6   ? 0.2795 0.3147 0.2010 -0.0880 0.0271  0.0216  6   PHE   B CA  
3739 C  C   . PHE   B 6   ? 0.3340 0.3473 0.2388 -0.0959 0.0552  -0.0066 6   PHE   B C   
3740 O  O   . PHE   B 6   ? 0.3452 0.3780 0.2766 -0.0908 0.0418  -0.0226 6   PHE   B O   
3741 C  CB  . PHE   B 6   ? 0.2492 0.2899 0.1712 -0.0812 0.0077  0.0204  6   PHE   B CB  
3742 C  CG  . PHE   B 6   ? 0.2175 0.2593 0.1632 -0.0810 -0.0081 0.0150  6   PHE   B CG  
3743 C  CD1 . PHE   B 6   ? 0.2206 0.2334 0.1455 -0.0726 -0.0200 0.0120  6   PHE   B CD1 
3744 C  CD2 . PHE   B 6   ? 0.1937 0.2585 0.1594 -0.0686 -0.0032 0.0379  6   PHE   B CD2 
3745 C  CE1 . PHE   B 6   ? 0.2178 0.2124 0.1598 -0.0621 -0.0276 0.0100  6   PHE   B CE1 
3746 C  CE2 . PHE   B 6   ? 0.1976 0.2468 0.1865 -0.0559 -0.0049 0.0326  6   PHE   B CE2 
3747 C  CZ  . PHE   B 6   ? 0.2054 0.2205 0.1705 -0.0569 -0.0127 0.0206  6   PHE   B CZ  
3757 N  N   . SER   B 7   ? 0.3733 0.3308 0.2655 -0.1171 0.0892  -0.0264 7   SER   B N   
3758 C  CA  . SER   B 7   ? 0.4078 0.3363 0.3198 -0.1177 0.1127  -0.0376 7   SER   B CA  
3759 C  C   . SER   B 7   ? 0.4091 0.3242 0.3038 -0.1202 0.1287  -0.0541 7   SER   B C   
3760 O  O   . SER   B 7   ? 0.4121 0.3223 0.3286 -0.1256 0.1240  -0.0600 7   SER   B O   
3761 C  CB  . SER   B 7   ? 0.4306 0.3531 0.3859 -0.1144 0.1221  -0.0309 7   SER   B CB  
3762 O  OG  . SER   B 7   ? 0.4440 0.3622 0.4358 -0.1135 0.1226  -0.0213 7   SER   B OG  
3768 N  N   . GLY   B 8   ? 0.4093 0.3172 0.3048 -0.1069 0.1438  -0.0614 8   GLY   B N   
3769 C  CA  . GLY   B 8   ? 0.3966 0.3002 0.2964 -0.1002 0.1485  -0.0699 8   GLY   B CA  
3770 C  C   . GLY   B 8   ? 0.3745 0.2725 0.2882 -0.0997 0.1433  -0.0670 8   GLY   B C   
3771 O  O   . GLY   B 8   ? 0.3825 0.2778 0.3235 -0.0902 0.1456  -0.0768 8   GLY   B O   
3775 N  N   . TYR   B 9   ? 0.3549 0.2495 0.2533 -0.0900 0.1124  -0.0760 9   TYR   B N   
3776 C  CA  . TYR   B 9   ? 0.3313 0.2235 0.2201 -0.0777 0.0840  -0.0552 9   TYR   B CA  
3777 C  C   . TYR   B 9   ? 0.3279 0.2215 0.2167 -0.0752 0.0501  -0.0416 9   TYR   B C   
3778 O  O   . TYR   B 9   ? 0.3436 0.2437 0.2546 -0.0797 0.0527  -0.0329 9   TYR   B O   
3779 C  CB  . TYR   B 9   ? 0.3168 0.1981 0.2328 -0.0699 0.0777  -0.0488 9   TYR   B CB  
3780 C  CG  . TYR   B 9   ? 0.3045 0.1786 0.2354 -0.0724 0.0662  -0.0545 9   TYR   B CG  
3781 C  CD1 . TYR   B 9   ? 0.3083 0.1793 0.2528 -0.0857 0.0659  -0.0426 9   TYR   B CD1 
3782 C  CD2 . TYR   B 9   ? 0.2870 0.1729 0.2204 -0.0627 0.0641  -0.0602 9   TYR   B CD2 
3783 C  CE1 . TYR   B 9   ? 0.3027 0.1905 0.2519 -0.0880 0.0724  -0.0539 9   TYR   B CE1 
3784 C  CE2 . TYR   B 9   ? 0.2873 0.1772 0.2321 -0.0670 0.0614  -0.0540 9   TYR   B CE2 
3785 C  CZ  . TYR   B 9   ? 0.2943 0.1927 0.2471 -0.0814 0.0670  -0.0693 9   TYR   B CZ  
3786 O  OH  . TYR   B 9   ? 0.2921 0.2105 0.2641 -0.0918 0.0714  -0.0853 9   TYR   B OH  
3796 N  N   . LEU   B 10  ? 0.3069 0.1949 0.2035 -0.0748 0.0230  -0.0393 10  LEU   B N   
3797 C  CA  . LEU   B 10  ? 0.3030 0.1902 0.2082 -0.0819 -0.0094 -0.0359 10  LEU   B CA  
3798 C  C   . LEU   B 10  ? 0.2863 0.1903 0.2042 -0.0789 -0.0271 -0.0305 10  LEU   B C   
3799 O  O   . LEU   B 10  ? 0.2707 0.1913 0.2023 -0.0608 -0.0167 -0.0229 10  LEU   B O   
3800 C  CB  . LEU   B 10  ? 0.3207 0.1842 0.2261 -0.0856 -0.0254 -0.0168 10  LEU   B CB  
3801 C  CG  . LEU   B 10  ? 0.3441 0.1930 0.2620 -0.0776 -0.0550 -0.0106 10  LEU   B CG  
3802 C  CD1 . LEU   B 10  ? 0.3590 0.2050 0.2804 -0.0738 -0.0564 -0.0207 10  LEU   B CD1 
3803 C  CD2 . LEU   B 10  ? 0.3530 0.1979 0.2896 -0.0737 -0.0542 0.0125  10  LEU   B CD2 
3815 N  N   . LYS   B 11  ? 0.3014 0.2157 0.2094 -0.0751 -0.0431 -0.0208 11  LYS   B N   
3816 C  CA  . LYS   B 11  ? 0.3214 0.2434 0.2474 -0.0609 -0.0572 -0.0270 11  LYS   B CA  
3817 C  C   . LYS   B 11  ? 0.3009 0.2250 0.2572 -0.0796 -0.0522 -0.0337 11  LYS   B C   
3818 O  O   . LYS   B 11  ? 0.3138 0.2415 0.2961 -0.0988 -0.0485 -0.0672 11  LYS   B O   
3819 C  CB  . LYS   B 11  ? 0.3584 0.2936 0.3125 -0.0323 -0.0639 -0.0320 11  LYS   B CB  
3820 C  CG  . LYS   B 11  ? 0.3907 0.3275 0.3816 -0.0135 -0.0611 -0.0360 11  LYS   B CG  
3821 C  CD  . LYS   B 11  ? 0.4155 0.3497 0.4459 -0.0024 -0.0563 -0.0388 11  LYS   B CD  
3822 C  CE  . LYS   B 11  ? 0.4332 0.3660 0.4968 -0.0014 -0.0587 -0.0435 11  LYS   B CE  
3823 N  NZ  . LYS   B 11  ? 0.4427 0.3765 0.5245 -0.0032 -0.0638 -0.0453 11  LYS   B NZ  
3837 N  N   . LEU   B 12  ? 0.2663 0.1936 0.2506 -0.0701 -0.0501 -0.0376 12  LEU   B N   
3838 C  CA  . LEU   B 12  ? 0.2443 0.1741 0.2636 -0.0584 -0.0365 -0.0276 12  LEU   B CA  
3839 C  C   . LEU   B 12  ? 0.2255 0.1796 0.2701 -0.0625 -0.0512 -0.0233 12  LEU   B C   
3840 O  O   . LEU   B 12  ? 0.2283 0.1814 0.2882 -0.0683 -0.0592 -0.0193 12  LEU   B O   
3841 C  CB  . LEU   B 12  ? 0.2427 0.1536 0.2619 -0.0423 -0.0216 -0.0275 12  LEU   B CB  
3842 C  CG  . LEU   B 12  ? 0.2408 0.1534 0.2566 -0.0399 -0.0141 -0.0168 12  LEU   B CG  
3843 C  CD1 . LEU   B 12  ? 0.2497 0.1576 0.2450 -0.0304 -0.0116 -0.0010 12  LEU   B CD1 
3844 C  CD2 . LEU   B 12  ? 0.2432 0.1580 0.2638 -0.0382 -0.0087 -0.0233 12  LEU   B CD2 
3856 N  N   . THR   B 13  ? 0.2149 0.1900 0.2720 -0.0603 -0.0566 -0.0310 13  THR   B N   
3857 C  CA  . THR   B 13  ? 0.2125 0.1971 0.2605 -0.0675 -0.0699 -0.0157 13  THR   B CA  
3858 C  C   . THR   B 13  ? 0.2510 0.2133 0.2811 -0.0760 -0.0797 -0.0077 13  THR   B C   
3859 O  O   . THR   B 13  ? 0.2695 0.2134 0.2933 -0.0735 -0.0448 -0.0120 13  THR   B O   
3860 C  CB  . THR   B 13  ? 0.1960 0.1950 0.2571 -0.0632 -0.0618 -0.0052 13  THR   B CB  
3861 O  OG1 . THR   B 13  ? 0.1909 0.1849 0.2705 -0.0516 -0.0432 -0.0084 13  THR   B OG1 
3862 C  CG2 . THR   B 13  ? 0.2057 0.2014 0.2710 -0.0523 -0.0493 0.0045  13  THR   B CG2 
3870 N  N   A ASP   B 14  ? 0.2618 0.2264 0.2938 -0.0809 -0.1091 -0.0009 14  ASP   B N   
3871 N  N   B ASP   B 14  ? 0.2604 0.2242 0.2904 -0.0749 -0.0933 0.0031  14  ASP   B N   
3872 C  CA  A ASP   B 14  ? 0.2755 0.2384 0.3186 -0.0778 -0.1142 0.0144  14  ASP   B CA  
3873 C  CA  B ASP   B 14  ? 0.2714 0.2339 0.3060 -0.0695 -0.0933 0.0157  14  ASP   B CA  
3874 C  C   A ASP   B 14  ? 0.2645 0.2197 0.2863 -0.0768 -0.0958 0.0178  14  ASP   B C   
3875 C  C   B ASP   B 14  ? 0.2582 0.2155 0.2795 -0.0705 -0.0874 0.0171  14  ASP   B C   
3876 O  O   A ASP   B 14  ? 0.2865 0.2309 0.2884 -0.0751 -0.0889 0.0264  14  ASP   B O   
3877 O  O   B ASP   B 14  ? 0.2715 0.2183 0.2803 -0.0696 -0.0847 0.0231  14  ASP   B O   
3878 C  CB  A ASP   B 14  ? 0.2974 0.2692 0.3975 -0.0771 -0.1244 0.0137  14  ASP   B CB  
3879 C  CB  B ASP   B 14  ? 0.2935 0.2623 0.3621 -0.0643 -0.0923 0.0188  14  ASP   B CB  
3880 C  CG  A ASP   B 14  ? 0.3240 0.2958 0.4711 -0.0696 -0.1156 0.0048  14  ASP   B CG  
3881 C  CG  B ASP   B 14  ? 0.3170 0.2877 0.4148 -0.0558 -0.0837 0.0149  14  ASP   B CG  
3882 O  OD1 A ASP   B 14  ? 0.3408 0.3030 0.4911 -0.0713 -0.1123 -0.0053 14  ASP   B OD1 
3883 O  OD1 B ASP   B 14  ? 0.3292 0.2998 0.4266 -0.0526 -0.0771 0.0107  14  ASP   B OD1 
3884 O  OD2 A ASP   B 14  ? 0.3268 0.3063 0.5040 -0.0668 -0.1073 0.0074  14  ASP   B OD2 
3885 O  OD2 B ASP   B 14  ? 0.3212 0.2936 0.4362 -0.0576 -0.0826 0.0154  14  ASP   B OD2 
3894 N  N   . ASN   B 15  ? 0.2316 0.1961 0.2603 -0.0654 -0.0844 0.0160  15  ASN   B N   
3895 C  CA  . ASN   B 15  ? 0.1898 0.1703 0.2421 -0.0420 -0.0637 0.0027  15  ASN   B CA  
3896 C  C   . ASN   B 15  ? 0.1721 0.1562 0.2163 -0.0284 -0.0496 -0.0010 15  ASN   B C   
3897 O  O   . ASN   B 15  ? 0.1654 0.1471 0.2224 -0.0268 -0.0488 -0.0128 15  ASN   B O   
3898 C  CB  . ASN   B 15  ? 0.1794 0.1648 0.2662 -0.0227 -0.0643 0.0091  15  ASN   B CB  
3899 C  CG  . ASN   B 15  ? 0.1630 0.1660 0.2580 -0.0270 -0.0343 0.0133  15  ASN   B CG  
3900 O  OD1 . ASN   B 15  ? 0.1674 0.1922 0.2912 -0.0454 -0.0334 0.0172  15  ASN   B OD1 
3901 N  ND2 . ASN   B 15  ? 0.1628 0.1390 0.2506 -0.0169 -0.0065 0.0014  15  ASN   B ND2 
3909 N  N   . VAL   B 16  ? 0.1772 0.1477 0.2174 -0.0335 -0.0590 -0.0004 16  VAL   B N   
3910 C  CA  . VAL   B 16  ? 0.1776 0.1513 0.2101 -0.0312 -0.0442 -0.0154 16  VAL   B CA  
3911 C  C   . VAL   B 16  ? 0.1759 0.1628 0.2026 -0.0412 -0.0391 -0.0089 16  VAL   B C   
3912 O  O   . VAL   B 16  ? 0.1754 0.1692 0.2209 -0.0386 -0.0290 -0.0186 16  VAL   B O   
3913 C  CB  . VAL   B 16  ? 0.1836 0.1442 0.2177 -0.0182 -0.0322 -0.0172 16  VAL   B CB  
3914 C  CG1 . VAL   B 16  ? 0.1948 0.1403 0.2134 -0.0057 -0.0245 -0.0111 16  VAL   B CG1 
3915 C  CG2 . VAL   B 16  ? 0.1872 0.1522 0.2322 -0.0059 -0.0251 -0.0141 16  VAL   B CG2 
3925 N  N   . TYR   B 17  ? 0.1851 0.1691 0.1941 -0.0406 -0.0322 -0.0194 17  TYR   B N   
3926 C  CA  . TYR   B 17  ? 0.1935 0.1827 0.1876 -0.0439 -0.0322 -0.0015 17  TYR   B CA  
3927 C  C   . TYR   B 17  ? 0.1835 0.1553 0.1868 -0.0429 -0.0211 -0.0067 17  TYR   B C   
3928 O  O   . TYR   B 17  ? 0.1807 0.1592 0.2006 -0.0329 -0.0309 -0.0286 17  TYR   B O   
3929 C  CB  . TYR   B 17  ? 0.2225 0.2276 0.2047 -0.0317 -0.0316 0.0320  17  TYR   B CB  
3930 C  CG  . TYR   B 17  ? 0.2496 0.2803 0.2501 -0.0216 -0.0487 0.0490  17  TYR   B CG  
3931 C  CD1 . TYR   B 17  ? 0.2655 0.2990 0.2819 -0.0195 -0.0575 0.0579  17  TYR   B CD1 
3932 C  CD2 . TYR   B 17  ? 0.2705 0.3077 0.2852 -0.0124 -0.0572 0.0511  17  TYR   B CD2 
3933 C  CE1 . TYR   B 17  ? 0.2833 0.3215 0.3000 -0.0117 -0.0661 0.0539  17  TYR   B CE1 
3934 C  CE2 . TYR   B 17  ? 0.2857 0.3281 0.3018 -0.0038 -0.0717 0.0568  17  TYR   B CE2 
3935 C  CZ  . TYR   B 17  ? 0.2964 0.3408 0.3131 -0.0035 -0.0749 0.0573  17  TYR   B CZ  
3936 O  OH  . TYR   B 17  ? 0.3110 0.3578 0.3285 0.0035  -0.0839 0.0602  17  TYR   B OH  
3946 N  N   . ILE   B 18  ? 0.1885 0.1567 0.1743 -0.0375 -0.0084 -0.0184 18  ILE   B N   
3947 C  CA  . ILE   B 18  ? 0.1961 0.1507 0.1757 -0.0391 -0.0048 -0.0246 18  ILE   B CA  
3948 C  C   . ILE   B 18  ? 0.2052 0.1568 0.1804 -0.0460 -0.0055 -0.0314 18  ILE   B C   
3949 O  O   . ILE   B 18  ? 0.2251 0.1718 0.1904 -0.0431 0.0088  -0.0320 18  ILE   B O   
3950 C  CB  . ILE   B 18  ? 0.2010 0.1520 0.1963 -0.0439 -0.0067 -0.0155 18  ILE   B CB  
3951 C  CG1 . ILE   B 18  ? 0.1988 0.1602 0.2094 -0.0445 -0.0069 -0.0113 18  ILE   B CG1 
3952 C  CG2 . ILE   B 18  ? 0.2067 0.1540 0.2089 -0.0497 -0.0155 -0.0125 18  ILE   B CG2 
3953 C  CD1 . ILE   B 18  ? 0.2052 0.1852 0.2333 -0.0410 -0.0222 0.0128  18  ILE   B CD1 
3965 N  N   . LYS   B 19  ? 0.2054 0.1565 0.1969 -0.0266 0.0221  -0.0368 19  LYS   B N   
3966 C  CA  . LYS   B 19  ? 0.2160 0.1628 0.2187 -0.0307 0.0254  -0.0435 19  LYS   B CA  
3967 C  C   . LYS   B 19  ? 0.1949 0.1584 0.2316 -0.0281 0.0372  -0.0536 19  LYS   B C   
3968 O  O   . LYS   B 19  ? 0.1905 0.1603 0.2206 -0.0203 0.0254  -0.0459 19  LYS   B O   
3969 C  CB  . LYS   B 19  ? 0.2405 0.1797 0.2313 -0.0409 0.0347  -0.0381 19  LYS   B CB  
3970 C  CG  . LYS   B 19  ? 0.2663 0.2007 0.2600 -0.0546 0.0421  -0.0498 19  LYS   B CG  
3971 C  CD  . LYS   B 19  ? 0.2969 0.2346 0.2650 -0.0588 0.0582  -0.0404 19  LYS   B CD  
3972 C  CE  . LYS   B 19  ? 0.3225 0.2598 0.2882 -0.0566 0.0615  -0.0404 19  LYS   B CE  
3973 N  NZ  . LYS   B 19  ? 0.3358 0.2774 0.2898 -0.0570 0.0634  -0.0385 19  LYS   B NZ  
3987 N  N   . ASN   B 20  ? 0.1960 0.1710 0.2607 -0.0217 0.0393  -0.0611 20  ASN   B N   
3988 C  CA  . ASN   B 20  ? 0.1952 0.1874 0.2874 -0.0177 0.0459  -0.0792 20  ASN   B CA  
3989 C  C   . ASN   B 20  ? 0.1926 0.2071 0.2904 -0.0278 0.0555  -0.0910 20  ASN   B C   
3990 O  O   . ASN   B 20  ? 0.2123 0.2410 0.3094 -0.0419 0.0597  -0.0907 20  ASN   B O   
3991 C  CB  . ASN   B 20  ? 0.2213 0.1889 0.3279 0.0056  0.0378  -0.0796 20  ASN   B CB  
3992 C  CG  . ASN   B 20  ? 0.2475 0.1954 0.3547 0.0359  0.0354  -0.0855 20  ASN   B CG  
3993 O  OD1 . ASN   B 20  ? 0.2810 0.2186 0.3790 0.0505  0.0333  -0.0906 20  ASN   B OD1 
3994 N  ND2 . ASN   B 20  ? 0.2366 0.1970 0.3452 0.0382  0.0233  -0.0750 20  ASN   B ND2 
4001 N  N   . ALA   B 21  ? 0.1906 0.1914 0.2850 -0.0370 0.0529  -0.0710 21  ALA   B N   
4002 C  CA  . ALA   B 21  ? 0.1988 0.1948 0.2940 -0.0370 0.0459  -0.0540 21  ALA   B CA  
4003 C  C   . ALA   B 21  ? 0.1981 0.1693 0.2870 -0.0240 0.0456  -0.0380 21  ALA   B C   
4004 O  O   . ALA   B 21  ? 0.2033 0.1566 0.2856 -0.0362 0.0463  -0.0364 21  ALA   B O   
4005 C  CB  . ALA   B 21  ? 0.2149 0.2207 0.3005 -0.0483 0.0514  -0.0434 21  ALA   B CB  
4011 N  N   . ASP   B 22  ? 0.1890 0.1613 0.2803 -0.0261 0.0349  -0.0272 22  ASP   B N   
4012 C  CA  . ASP   B 22  ? 0.1856 0.1524 0.2691 -0.0137 0.0255  -0.0214 22  ASP   B CA  
4013 C  C   . ASP   B 22  ? 0.1786 0.1487 0.2266 -0.0173 0.0243  -0.0158 22  ASP   B C   
4014 O  O   . ASP   B 22  ? 0.1820 0.1489 0.2249 -0.0104 0.0148  -0.0163 22  ASP   B O   
4015 C  CB  . ASP   B 22  ? 0.1888 0.1628 0.2967 -0.0073 0.0301  -0.0077 22  ASP   B CB  
4016 C  CG  . ASP   B 22  ? 0.1925 0.1832 0.3368 -0.0019 0.0058  -0.0062 22  ASP   B CG  
4017 O  OD1 . ASP   B 22  ? 0.2040 0.1730 0.3282 -0.0037 -0.0199 -0.0028 22  ASP   B OD1 
4018 O  OD2 . ASP   B 22  ? 0.1997 0.2115 0.3869 0.0037  -0.0085 -0.0217 22  ASP   B OD2 
4023 N  N   . ILE   B 23  ? 0.1770 0.1426 0.1991 -0.0146 0.0036  0.0118  23  ILE   B N   
4024 C  CA  . ILE   B 23  ? 0.1691 0.1396 0.1821 -0.0138 -0.0040 0.0034  23  ILE   B CA  
4025 C  C   . ILE   B 23  ? 0.1577 0.1397 0.1753 -0.0082 -0.0108 0.0039  23  ILE   B C   
4026 O  O   . ILE   B 23  ? 0.1520 0.1425 0.1636 -0.0123 -0.0046 0.0084  23  ILE   B O   
4027 C  CB  . ILE   B 23  ? 0.1642 0.1461 0.1870 -0.0215 -0.0002 0.0122  23  ILE   B CB  
4028 C  CG1 . ILE   B 23  ? 0.1697 0.1530 0.2016 -0.0161 0.0061  0.0244  23  ILE   B CG1 
4029 C  CG2 . ILE   B 23  ? 0.1726 0.1650 0.1892 -0.0223 0.0028  0.0016  23  ILE   B CG2 
4030 C  CD1 . ILE   B 23  ? 0.1731 0.1612 0.2140 -0.0108 0.0022  0.0163  23  ILE   B CD1 
4042 N  N   . VAL   B 24  ? 0.1599 0.1352 0.1887 -0.0122 -0.0099 -0.0016 24  VAL   B N   
4043 C  CA  . VAL   B 24  ? 0.1560 0.1422 0.2073 -0.0082 -0.0210 -0.0023 24  VAL   B CA  
4044 C  C   . VAL   B 24  ? 0.1545 0.1496 0.2068 -0.0122 -0.0098 0.0005  24  VAL   B C   
4045 O  O   . VAL   B 24  ? 0.1517 0.1582 0.2195 -0.0165 -0.0049 0.0072  24  VAL   B O   
4046 C  CB  . VAL   B 24  ? 0.1687 0.1619 0.2244 0.0019  -0.0229 -0.0043 24  VAL   B CB  
4047 C  CG1 . VAL   B 24  ? 0.1714 0.1637 0.2468 -0.0121 -0.0269 -0.0003 24  VAL   B CG1 
4048 C  CG2 . VAL   B 24  ? 0.1718 0.1928 0.2319 0.0116  -0.0173 -0.0095 24  VAL   B CG2 
4058 N  N   . GLU   B 25  ? 0.1785 0.1607 0.2121 -0.0176 0.0053  -0.0020 25  GLU   B N   
4059 C  CA  . GLU   B 25  ? 0.1844 0.1866 0.2322 -0.0059 0.0135  -0.0115 25  GLU   B CA  
4060 C  C   . GLU   B 25  ? 0.1854 0.1767 0.1953 -0.0183 0.0107  0.0019  25  GLU   B C   
4061 O  O   . GLU   B 25  ? 0.1975 0.1941 0.2075 -0.0180 0.0194  0.0057  25  GLU   B O   
4062 C  CB  . GLU   B 25  ? 0.2194 0.2301 0.2975 0.0153  0.0333  -0.0180 25  GLU   B CB  
4063 C  CG  . GLU   B 25  ? 0.2621 0.2888 0.4101 0.0192  0.0362  -0.0201 25  GLU   B CG  
4064 C  CD  . GLU   B 25  ? 0.2943 0.3536 0.5059 0.0145  0.0360  -0.0231 25  GLU   B CD  
4065 O  OE1 . GLU   B 25  ? 0.3195 0.3744 0.5311 0.0172  0.0423  -0.0195 25  GLU   B OE1 
4066 O  OE2 . GLU   B 25  ? 0.3144 0.3701 0.5330 0.0118  0.0271  -0.0314 25  GLU   B OE2 
4073 N  N   A GLU   B 26  ? 0.1868 0.1700 0.1794 -0.0319 0.0058  -0.0034 26  GLU   B N   
4074 N  N   B GLU   B 26  ? 0.1827 0.1710 0.1874 -0.0268 0.0053  0.0035  26  GLU   B N   
4075 C  CA  A GLU   B 26  ? 0.1867 0.1839 0.1833 -0.0380 -0.0021 -0.0014 26  GLU   B CA  
4076 C  CA  B GLU   B 26  ? 0.1777 0.1795 0.1961 -0.0316 -0.0016 0.0075  26  GLU   B CA  
4077 C  C   A GLU   B 26  ? 0.1661 0.1843 0.1771 -0.0260 0.0008  0.0145  26  GLU   B C   
4078 C  C   B GLU   B 26  ? 0.1630 0.1798 0.1819 -0.0241 0.0023  0.0185  26  GLU   B C   
4079 O  O   A GLU   B 26  ? 0.1841 0.2029 0.1907 -0.0227 0.0008  0.0264  26  GLU   B O   
4080 O  O   B GLU   B 26  ? 0.1763 0.1928 0.1876 -0.0219 0.0031  0.0287  26  GLU   B O   
4081 C  CB  A GLU   B 26  ? 0.2200 0.2013 0.1980 -0.0471 0.0085  0.0110  26  GLU   B CB  
4082 C  CB  B GLU   B 26  ? 0.1948 0.1898 0.2224 -0.0390 -0.0009 0.0150  26  GLU   B CB  
4083 C  CG  A GLU   B 26  ? 0.2584 0.2252 0.2441 -0.0489 0.0217  0.0008  26  GLU   B CG  
4084 C  CG  B GLU   B 26  ? 0.2144 0.2050 0.2721 -0.0414 0.0012  0.0011  26  GLU   B CG  
4085 C  CD  A GLU   B 26  ? 0.2790 0.2358 0.2455 -0.0620 0.0473  -0.0067 26  GLU   B CD  
4086 C  CD  B GLU   B 26  ? 0.2152 0.2055 0.2819 -0.0534 0.0047  -0.0223 26  GLU   B CD  
4087 O  OE1 A GLU   B 26  ? 0.2840 0.2281 0.2380 -0.0642 0.0869  0.0018  26  GLU   B OE1 
4088 O  OE1 B GLU   B 26  ? 0.2022 0.2032 0.3074 -0.0717 0.0220  -0.0441 26  GLU   B OE1 
4089 O  OE2 A GLU   B 26  ? 0.2859 0.2509 0.2791 -0.0718 0.0456  0.0026  26  GLU   B OE2 
4090 O  OE2 B GLU   B 26  ? 0.2195 0.2056 0.2796 -0.0458 0.0064  -0.0285 26  GLU   B OE2 
4103 N  N   . ALA   B 27  ? 0.1499 0.1688 0.1799 -0.0232 0.0071  0.0181  27  ALA   B N   
4104 C  CA  . ALA   B 27  ? 0.1523 0.1640 0.1981 -0.0147 0.0033  0.0286  27  ALA   B CA  
4105 C  C   . ALA   B 27  ? 0.1542 0.1699 0.2177 -0.0131 0.0159  0.0396  27  ALA   B C   
4106 O  O   . ALA   B 27  ? 0.1627 0.1784 0.2295 -0.0042 0.0115  0.0471  27  ALA   B O   
4107 C  CB  . ALA   B 27  ? 0.1717 0.1505 0.1929 -0.0189 0.0041  0.0311  27  ALA   B CB  
4114 N  N   . LYS   B 28  ? 0.1529 0.1860 0.2553 -0.0183 0.0196  0.0568  28  LYS   B N   
4115 C  CA  . LYS   B 28  ? 0.1698 0.2260 0.2778 -0.0039 0.0521  0.0884  28  LYS   B CA  
4116 C  C   . LYS   B 28  ? 0.1934 0.2471 0.2659 0.0003  0.0665  0.0749  28  LYS   B C   
4117 O  O   . LYS   B 28  ? 0.2213 0.2586 0.2888 -0.0044 0.0595  0.0742  28  LYS   B O   
4118 C  CB  . LYS   B 28  ? 0.1908 0.2647 0.3347 0.0105  0.0770  0.1074  28  LYS   B CB  
4119 C  CG  . LYS   B 28  ? 0.2235 0.3155 0.3713 0.0236  0.0837  0.1202  28  LYS   B CG  
4120 C  CD  . LYS   B 28  ? 0.2733 0.3808 0.4270 0.0337  0.1025  0.1193  28  LYS   B CD  
4121 C  CE  . LYS   B 28  ? 0.3255 0.4358 0.4806 0.0428  0.1045  0.1225  28  LYS   B CE  
4122 N  NZ  . LYS   B 28  ? 0.3563 0.4673 0.4963 0.0482  0.0984  0.1288  28  LYS   B NZ  
4136 N  N   . LYS   B 29  ? 0.2136 0.2734 0.2667 0.0169  0.0692  0.0621  29  LYS   B N   
4137 C  CA  . LYS   B 29  ? 0.2597 0.3084 0.2885 0.0177  0.0614  0.0633  29  LYS   B CA  
4138 C  C   . LYS   B 29  ? 0.2525 0.3087 0.2525 0.0148  0.0432  0.0746  29  LYS   B C   
4139 O  O   . LYS   B 29  ? 0.2747 0.3283 0.2603 0.0219  0.0474  0.0782  29  LYS   B O   
4140 C  CB  . LYS   B 29  ? 0.3201 0.3468 0.3724 0.0169  0.0562  0.0483  29  LYS   B CB  
4141 C  CG  . LYS   B 29  ? 0.3729 0.3785 0.4661 0.0141  0.0508  0.0422  29  LYS   B CG  
4142 C  CD  . LYS   B 29  ? 0.4200 0.4010 0.5368 0.0076  0.0585  0.0382  29  LYS   B CD  
4143 C  CE  . LYS   B 29  ? 0.4559 0.4150 0.5786 0.0022  0.0673  0.0335  29  LYS   B CE  
4144 N  NZ  . LYS   B 29  ? 0.4783 0.4227 0.6131 -0.0003 0.0687  0.0301  29  LYS   B NZ  
4158 N  N   . VAL   B 30  ? 0.2190 0.2904 0.2381 -0.0003 0.0263  0.0682  30  VAL   B N   
4159 C  CA  . VAL   B 30  ? 0.2037 0.2805 0.2622 -0.0131 -0.0023 0.0721  30  VAL   B CA  
4160 C  C   . VAL   B 30  ? 0.1819 0.2735 0.2488 -0.0141 0.0074  0.0898  30  VAL   B C   
4161 O  O   . VAL   B 30  ? 0.1976 0.2908 0.2616 -0.0073 0.0029  0.1022  30  VAL   B O   
4162 C  CB  . VAL   B 30  ? 0.2083 0.2737 0.3078 -0.0295 -0.0277 0.0679  30  VAL   B CB  
4163 C  CG1 . VAL   B 30  ? 0.2170 0.2777 0.3094 -0.0286 -0.0185 0.0639  30  VAL   B CG1 
4164 C  CG2 . VAL   B 30  ? 0.2198 0.2762 0.3314 -0.0394 -0.0433 0.0497  30  VAL   B CG2 
4174 N  N   . LYS   B 31  ? 0.1709 0.2366 0.2772 -0.0267 0.0036  0.0933  31  LYS   B N   
4175 C  CA  . LYS   B 31  ? 0.1629 0.2306 0.3190 -0.0396 -0.0056 0.0985  31  LYS   B CA  
4176 C  C   . LYS   B 31  ? 0.1577 0.1938 0.2789 -0.0371 -0.0268 0.0865  31  LYS   B C   
4177 O  O   . LYS   B 31  ? 0.1649 0.2098 0.2934 -0.0304 -0.0169 0.0999  31  LYS   B O   
4178 C  CB  . LYS   B 31  ? 0.1784 0.2796 0.3728 -0.0325 0.0158  0.1083  31  LYS   B CB  
4179 C  CG  . LYS   B 31  ? 0.2033 0.3260 0.4187 -0.0302 0.0381  0.1103  31  LYS   B CG  
4180 C  CD  . LYS   B 31  ? 0.2363 0.3797 0.4650 -0.0235 0.0411  0.0953  31  LYS   B CD  
4181 C  CE  . LYS   B 31  ? 0.2679 0.4188 0.5118 -0.0198 0.0346  0.0810  31  LYS   B CE  
4182 N  NZ  . LYS   B 31  ? 0.2910 0.4489 0.5280 -0.0118 0.0232  0.0725  31  LYS   B NZ  
4196 N  N   . PRO   B 32  ? 0.1703 0.1554 0.2173 -0.0326 -0.0382 0.0498  32  PRO   B N   
4197 C  CA  . PRO   B 32  ? 0.1794 0.1545 0.1768 -0.0348 -0.0407 0.0323  32  PRO   B CA  
4198 C  C   . PRO   B 32  ? 0.1838 0.1464 0.1824 -0.0400 -0.0544 0.0322  32  PRO   B C   
4199 O  O   . PRO   B 32  ? 0.1932 0.1469 0.2205 -0.0452 -0.0703 0.0320  32  PRO   B O   
4200 C  CB  . PRO   B 32  ? 0.1927 0.1483 0.1847 -0.0389 -0.0283 0.0192  32  PRO   B CB  
4201 C  CG  . PRO   B 32  ? 0.2075 0.1359 0.1819 -0.0345 -0.0435 0.0225  32  PRO   B CG  
4202 C  CD  . PRO   B 32  ? 0.1929 0.1394 0.1988 -0.0235 -0.0531 0.0249  32  PRO   B CD  
4210 N  N   . THR   B 33  ? 0.1895 0.1328 0.1770 -0.0347 -0.0471 0.0224  33  THR   B N   
4211 C  CA  . THR   B 33  ? 0.1914 0.1421 0.1633 -0.0361 -0.0471 0.0232  33  THR   B CA  
4212 C  C   . THR   B 33  ? 0.1978 0.1350 0.1615 -0.0344 -0.0481 0.0156  33  THR   B C   
4213 O  O   . THR   B 33  ? 0.2181 0.1356 0.1705 -0.0438 -0.0484 0.0184  33  THR   B O   
4214 C  CB  . THR   B 33  ? 0.1980 0.1525 0.1701 -0.0214 -0.0530 0.0255  33  THR   B CB  
4215 O  OG1 . THR   B 33  ? 0.1882 0.1596 0.1788 -0.0253 -0.0475 0.0319  33  THR   B OG1 
4216 C  CG2 . THR   B 33  ? 0.2206 0.1574 0.2075 -0.0160 -0.0478 0.0244  33  THR   B CG2 
4224 N  N   . VAL   B 34  ? 0.1807 0.1306 0.1511 -0.0373 -0.0436 0.0138  34  VAL   B N   
4225 C  CA  . VAL   B 34  ? 0.1659 0.1287 0.1487 -0.0300 -0.0343 0.0049  34  VAL   B CA  
4226 C  C   . VAL   B 34  ? 0.1453 0.1239 0.1354 -0.0290 -0.0208 0.0038  34  VAL   B C   
4227 O  O   . VAL   B 34  ? 0.1666 0.1266 0.1434 -0.0306 -0.0284 0.0082  34  VAL   B O   
4228 C  CB  . VAL   B 34  ? 0.1688 0.1351 0.1727 -0.0116 -0.0290 0.0032  34  VAL   B CB  
4229 C  CG1 . VAL   B 34  ? 0.1684 0.1486 0.1771 -0.0100 -0.0108 -0.0013 34  VAL   B CG1 
4230 C  CG2 . VAL   B 34  ? 0.1712 0.1415 0.2129 -0.0075 -0.0273 0.0049  34  VAL   B CG2 
4240 N  N   . VAL   B 35  ? 0.1430 0.1213 0.1249 -0.0269 -0.0122 0.0094  35  VAL   B N   
4241 C  CA  . VAL   B 35  ? 0.1385 0.1188 0.1265 -0.0202 -0.0118 0.0048  35  VAL   B CA  
4242 C  C   . VAL   B 35  ? 0.1261 0.1140 0.1299 -0.0154 -0.0209 0.0006  35  VAL   B C   
4243 O  O   . VAL   B 35  ? 0.1318 0.1214 0.1346 -0.0223 -0.0037 -0.0061 35  VAL   B O   
4244 C  CB  . VAL   B 35  ? 0.1366 0.1390 0.1428 -0.0162 0.0020  0.0029  35  VAL   B CB  
4245 C  CG1 . VAL   B 35  ? 0.1288 0.1507 0.1695 -0.0206 0.0022  -0.0040 35  VAL   B CG1 
4246 C  CG2 . VAL   B 35  ? 0.1373 0.1379 0.1592 -0.0061 0.0002  -0.0038 35  VAL   B CG2 
4256 N  N   . VAL   B 36  ? 0.1300 0.1149 0.1271 -0.0182 -0.0185 0.0101  36  VAL   B N   
4257 C  CA  . VAL   B 36  ? 0.1268 0.1122 0.1249 -0.0119 -0.0104 0.0059  36  VAL   B CA  
4258 C  C   . VAL   B 36  ? 0.1244 0.1132 0.1215 -0.0102 -0.0042 0.0023  36  VAL   B C   
4259 O  O   . VAL   B 36  ? 0.1299 0.1224 0.1474 -0.0127 -0.0025 -0.0008 36  VAL   B O   
4260 C  CB  . VAL   B 36  ? 0.1246 0.1194 0.1369 -0.0155 -0.0062 0.0093  36  VAL   B CB  
4261 C  CG1 . VAL   B 36  ? 0.1276 0.1345 0.1486 -0.0208 -0.0088 0.0035  36  VAL   B CG1 
4262 C  CG2 . VAL   B 36  ? 0.1311 0.1277 0.1493 -0.0133 -0.0133 0.0113  36  VAL   B CG2 
4272 N  N   . ASN   B 37  ? 0.1257 0.1171 0.1250 -0.0027 -0.0093 0.0025  37  ASN   B N   
4273 C  CA  . ASN   B 37  ? 0.1229 0.1210 0.1389 -0.0010 -0.0101 0.0055  37  ASN   B CA  
4274 C  C   . ASN   B 37  ? 0.1218 0.1248 0.1378 0.0008  -0.0080 0.0041  37  ASN   B C   
4275 O  O   . ASN   B 37  ? 0.1302 0.1294 0.1458 -0.0007 -0.0008 0.0076  37  ASN   B O   
4276 C  CB  . ASN   B 37  ? 0.1293 0.1279 0.1298 -0.0017 -0.0112 0.0087  37  ASN   B CB  
4277 C  CG  . ASN   B 37  ? 0.1319 0.1257 0.1401 -0.0018 -0.0073 0.0039  37  ASN   B CG  
4278 O  OD1 . ASN   B 37  ? 0.1379 0.1332 0.1499 0.0086  -0.0136 0.0008  37  ASN   B OD1 
4279 N  ND2 . ASN   B 37  ? 0.1371 0.1237 0.1467 -0.0010 -0.0183 0.0091  37  ASN   B ND2 
4286 N  N   . ALA   B 38  ? 0.1351 0.1221 0.1427 0.0059  0.0023  0.0057  38  ALA   B N   
4287 C  CA  . ALA   B 38  ? 0.1464 0.1248 0.1386 -0.0009 0.0034  0.0131  38  ALA   B CA  
4288 C  C   . ALA   B 38  ? 0.1399 0.1211 0.1346 -0.0006 0.0030  0.0124  38  ALA   B C   
4289 O  O   . ALA   B 38  ? 0.1516 0.1322 0.1525 0.0055  -0.0047 0.0103  38  ALA   B O   
4290 C  CB  . ALA   B 38  ? 0.1665 0.1324 0.1555 -0.0093 0.0101  0.0100  38  ALA   B CB  
4296 N  N   . ALA   B 39  ? 0.1422 0.1255 0.1248 0.0101  -0.0036 0.0077  39  ALA   B N   
4297 C  CA  . ALA   B 39  ? 0.1511 0.1326 0.1185 0.0076  -0.0070 0.0050  39  ALA   B CA  
4298 C  C   . ALA   B 39  ? 0.1514 0.1396 0.1102 0.0108  -0.0093 0.0020  39  ALA   B C   
4299 O  O   . ALA   B 39  ? 0.1516 0.1452 0.1464 0.0015  -0.0051 0.0089  39  ALA   B O   
4300 C  CB  . ALA   B 39  ? 0.1517 0.1346 0.1478 0.0006  -0.0013 -0.0008 39  ALA   B CB  
4306 N  N   . ASN   B 40  ? 0.1600 0.1593 0.1118 0.0017  -0.0023 -0.0040 40  ASN   B N   
4307 C  CA  . ASN   B 40  ? 0.1650 0.1608 0.1214 0.0063  -0.0069 -0.0076 40  ASN   B CA  
4308 C  C   . ASN   B 40  ? 0.1679 0.1624 0.1095 0.0098  -0.0063 0.0070  40  ASN   B C   
4309 O  O   . ASN   B 40  ? 0.1627 0.1512 0.1305 0.0082  -0.0078 0.0044  40  ASN   B O   
4310 C  CB  . ASN   B 40  ? 0.1804 0.1615 0.1523 0.0120  -0.0139 0.0080  40  ASN   B CB  
4311 C  CG  . ASN   B 40  ? 0.1848 0.1691 0.1886 0.0071  -0.0290 0.0149  40  ASN   B CG  
4312 O  OD1 . ASN   B 40  ? 0.1824 0.1635 0.2633 0.0052  -0.0396 0.0210  40  ASN   B OD1 
4313 N  ND2 . ASN   B 40  ? 0.1882 0.1661 0.1843 0.0016  -0.0192 0.0176  40  ASN   B ND2 
4320 N  N   . VAL   B 41  ? 0.1790 0.1675 0.1173 0.0147  0.0010  0.0033  41  VAL   B N   
4321 C  CA  . VAL   B 41  ? 0.1823 0.1770 0.1295 0.0123  0.0041  -0.0049 41  VAL   B CA  
4322 C  C   . VAL   B 41  ? 0.1775 0.1769 0.1292 0.0158  -0.0023 -0.0053 41  VAL   B C   
4323 O  O   . VAL   B 41  ? 0.1791 0.1743 0.1401 0.0117  -0.0089 -0.0067 41  VAL   B O   
4324 C  CB  . VAL   B 41  ? 0.2005 0.1901 0.1585 -0.0026 0.0222  -0.0196 41  VAL   B CB  
4325 C  CG1 . VAL   B 41  ? 0.1983 0.1916 0.1836 -0.0055 0.0316  -0.0217 41  VAL   B CG1 
4326 C  CG2 . VAL   B 41  ? 0.2079 0.2078 0.1769 -0.0098 0.0238  -0.0156 41  VAL   B CG2 
4336 N  N   . TYR   B 42  ? 0.1855 0.1791 0.1363 0.0123  -0.0082 0.0061  42  TYR   B N   
4337 C  CA  . TYR   B 42  ? 0.1882 0.1824 0.1443 0.0198  -0.0236 -0.0094 42  TYR   B CA  
4338 C  C   . TYR   B 42  ? 0.1720 0.1649 0.1519 0.0242  -0.0234 -0.0056 42  TYR   B C   
4339 O  O   . TYR   B 42  ? 0.1735 0.1754 0.1853 0.0160  -0.0264 -0.0161 42  TYR   B O   
4340 C  CB  . TYR   B 42  ? 0.2124 0.2116 0.1635 0.0117  -0.0256 -0.0024 42  TYR   B CB  
4341 C  CG  . TYR   B 42  ? 0.2089 0.2262 0.1535 0.0036  -0.0265 0.0126  42  TYR   B CG  
4342 C  CD1 . TYR   B 42  ? 0.2087 0.2258 0.1314 0.0024  -0.0099 0.0089  42  TYR   B CD1 
4343 C  CD2 . TYR   B 42  ? 0.2216 0.2368 0.1902 -0.0007 -0.0117 0.0183  42  TYR   B CD2 
4344 C  CE1 . TYR   B 42  ? 0.2235 0.2418 0.1403 0.0061  -0.0000 0.0082  42  TYR   B CE1 
4345 C  CE2 . TYR   B 42  ? 0.2268 0.2476 0.1792 0.0012  0.0152  0.0297  42  TYR   B CE2 
4346 C  CZ  . TYR   B 42  ? 0.2418 0.2639 0.1714 0.0161  0.0202  0.0100  42  TYR   B CZ  
4347 O  OH  . TYR   B 42  ? 0.2758 0.2933 0.2201 0.0311  0.0285  0.0171  42  TYR   B OH  
4357 N  N   . LEU   B 43  ? 0.1624 0.1442 0.1389 0.0096  -0.0161 -0.0129 43  LEU   B N   
4358 C  CA  . LEU   B 43  ? 0.1644 0.1475 0.1265 0.0041  -0.0179 -0.0084 43  LEU   B CA  
4359 C  C   . LEU   B 43  ? 0.1658 0.1482 0.1363 0.0070  -0.0135 0.0032  43  LEU   B C   
4360 O  O   . LEU   B 43  ? 0.1645 0.1531 0.1689 0.0067  -0.0176 0.0124  43  LEU   B O   
4361 C  CB  . LEU   B 43  ? 0.1581 0.1415 0.1374 0.0010  -0.0251 -0.0101 43  LEU   B CB  
4362 C  CG  . LEU   B 43  ? 0.1633 0.1397 0.1456 0.0032  -0.0279 -0.0035 43  LEU   B CG  
4363 C  CD1 . LEU   B 43  ? 0.1763 0.1486 0.1779 -0.0024 -0.0432 -0.0066 43  LEU   B CD1 
4364 C  CD2 . LEU   B 43  ? 0.1615 0.1434 0.1644 -0.0065 -0.0298 -0.0037 43  LEU   B CD2 
4376 N  N   . LYS   B 44  ? 0.1633 0.1446 0.1476 0.0063  -0.0126 -0.0044 44  LYS   B N   
4377 C  CA  . LYS   B 44  ? 0.1739 0.1563 0.1507 0.0075  -0.0175 0.0075  44  LYS   B CA  
4378 C  C   . LYS   B 44  ? 0.1631 0.1491 0.1486 0.0128  -0.0155 0.0040  44  LYS   B C   
4379 O  O   . LYS   B 44  ? 0.1833 0.1512 0.1696 0.0065  -0.0068 0.0076  44  LYS   B O   
4380 C  CB  . LYS   B 44  ? 0.2060 0.1803 0.1663 0.0130  -0.0284 0.0075  44  LYS   B CB  
4381 C  CG  . LYS   B 44  ? 0.2453 0.2043 0.2010 0.0113  -0.0566 0.0098  44  LYS   B CG  
4382 C  CD  . LYS   B 44  ? 0.2799 0.2240 0.2661 0.0032  -0.0605 0.0072  44  LYS   B CD  
4383 C  CE  . LYS   B 44  ? 0.3105 0.2526 0.3163 -0.0036 -0.0657 0.0224  44  LYS   B CE  
4384 N  NZ  . LYS   B 44  ? 0.3202 0.2661 0.3435 -0.0043 -0.0765 0.0394  44  LYS   B NZ  
4398 N  N   . HIS   B 45  ? 0.1571 0.1545 0.1381 0.0095  -0.0103 0.0091  45  HIS   B N   
4399 C  CA  . HIS   B 45  ? 0.1628 0.1533 0.1480 0.0155  -0.0111 0.0021  45  HIS   B CA  
4400 C  C   . HIS   B 45  ? 0.1837 0.1658 0.1898 0.0220  -0.0172 -0.0056 45  HIS   B C   
4401 O  O   . HIS   B 45  ? 0.1928 0.1951 0.2305 0.0486  0.0077  -0.0024 45  HIS   B O   
4402 C  CB  . HIS   B 45  ? 0.1581 0.1547 0.1548 0.0057  -0.0139 -0.0042 45  HIS   B CB  
4403 C  CG  . HIS   B 45  ? 0.1550 0.1489 0.1534 -0.0055 -0.0121 -0.0036 45  HIS   B CG  
4404 N  ND1 . HIS   B 45  ? 0.1621 0.1405 0.1585 0.0006  -0.0193 -0.0011 45  HIS   B ND1 
4405 C  CD2 . HIS   B 45  ? 0.1602 0.1535 0.1653 -0.0063 -0.0213 -0.0025 45  HIS   B CD2 
4406 C  CE1 . HIS   B 45  ? 0.1679 0.1356 0.1379 -0.0034 -0.0264 -0.0048 45  HIS   B CE1 
4407 N  NE2 . HIS   B 45  ? 0.1721 0.1449 0.1506 -0.0023 -0.0192 -0.0037 45  HIS   B NE2 
4415 N  N   A GLY   B 46  ? 0.1941 0.1597 0.2208 0.0193  -0.0360 0.0067  46  GLY   B N   
4416 N  N   B GLY   B 46  ? 0.1930 0.1668 0.2076 0.0188  -0.0291 0.0065  46  GLY   B N   
4417 C  CA  A GLY   B 46  ? 0.2096 0.1762 0.2652 0.0154  -0.0446 0.0103  46  GLY   B CA  
4418 C  CA  B GLY   B 46  ? 0.2067 0.1829 0.2354 0.0155  -0.0361 0.0134  46  GLY   B CA  
4419 C  C   A GLY   B 46  ? 0.2120 0.1937 0.3018 0.0200  -0.0373 0.0108  46  GLY   B C   
4420 C  C   B GLY   B 46  ? 0.2130 0.2011 0.2649 0.0179  -0.0309 0.0184  46  GLY   B C   
4421 O  O   A GLY   B 46  ? 0.2168 0.2019 0.3751 0.0285  -0.0193 -0.0093 46  GLY   B O   
4422 O  O   B GLY   B 46  ? 0.2202 0.2146 0.2876 0.0226  -0.0223 0.0236  46  GLY   B O   
4429 N  N   . GLY   B 47  ? 0.2108 0.2026 0.2721 0.0074  -0.0222 0.0078  47  GLY   B N   
4430 C  CA  . GLY   B 47  ? 0.1976 0.1746 0.2353 0.0005  -0.0203 0.0089  47  GLY   B CA  
4431 C  C   . GLY   B 47  ? 0.1771 0.1514 0.1921 0.0028  -0.0031 0.0122  47  GLY   B C   
4432 O  O   . GLY   B 47  ? 0.1881 0.1412 0.2049 0.0049  -0.0088 0.0123  47  GLY   B O   
4437 N  N   . GLY   B 48  ? 0.1543 0.1409 0.1895 0.0014  -0.0109 0.0123  48  GLY   B N   
4438 C  CA  . GLY   B 48  ? 0.1509 0.1410 0.1952 -0.0052 -0.0040 0.0098  48  GLY   B CA  
4439 C  C   . GLY   B 48  ? 0.1464 0.1397 0.1887 -0.0017 0.0052  0.0048  48  GLY   B C   
4440 O  O   . GLY   B 48  ? 0.1431 0.1394 0.2036 0.0046  -0.0067 0.0094  48  GLY   B O   
4444 N  N   . VAL   B 49  ? 0.1452 0.1448 0.1727 0.0119  0.0001  0.0041  49  VAL   B N   
4445 C  CA  . VAL   B 49  ? 0.1487 0.1538 0.1621 0.0122  -0.0095 -0.0050 49  VAL   B CA  
4446 C  C   . VAL   B 49  ? 0.1448 0.1444 0.1445 0.0097  -0.0072 0.0130  49  VAL   B C   
4447 O  O   . VAL   B 49  ? 0.1543 0.1481 0.1550 0.0052  -0.0023 0.0067  49  VAL   B O   
4448 C  CB  . VAL   B 49  ? 0.1523 0.1734 0.1873 0.0081  -0.0269 -0.0069 49  VAL   B CB  
4449 C  CG1 . VAL   B 49  ? 0.1494 0.1842 0.1786 0.0094  -0.0343 -0.0010 49  VAL   B CG1 
4450 C  CG2 . VAL   B 49  ? 0.1698 0.1857 0.2155 -0.0034 -0.0422 -0.0095 49  VAL   B CG2 
4460 N  N   . ALA   B 50  ? 0.1403 0.1367 0.1491 0.0012  -0.0072 0.0071  50  ALA   B N   
4461 C  CA  . ALA   B 50  ? 0.1443 0.1282 0.1453 0.0091  -0.0094 0.0077  50  ALA   B CA  
4462 C  C   . ALA   B 50  ? 0.1458 0.1316 0.1426 0.0055  -0.0054 0.0045  50  ALA   B C   
4463 O  O   . ALA   B 50  ? 0.1438 0.1350 0.1542 0.0052  -0.0026 0.0006  50  ALA   B O   
4464 C  CB  . ALA   B 50  ? 0.1462 0.1346 0.1505 0.0018  -0.0033 0.0149  50  ALA   B CB  
4470 N  N   . GLY   B 51  ? 0.1444 0.1443 0.1623 0.0094  -0.0154 0.0071  51  GLY   B N   
4471 C  CA  . GLY   B 51  ? 0.1425 0.1499 0.1880 0.0190  -0.0183 0.0083  51  GLY   B CA  
4472 C  C   . GLY   B 51  ? 0.1453 0.1482 0.1749 0.0218  -0.0062 0.0067  51  GLY   B C   
4473 O  O   . GLY   B 51  ? 0.1440 0.1600 0.1930 0.0122  -0.0082 -0.0023 51  GLY   B O   
4477 N  N   . ALA   B 52  ? 0.1512 0.1404 0.1592 0.0181  -0.0079 0.0076  52  ALA   B N   
4478 C  CA  . ALA   B 52  ? 0.1544 0.1470 0.1680 0.0166  0.0006  -0.0046 52  ALA   B CA  
4479 C  C   . ALA   B 52  ? 0.1405 0.1438 0.1649 0.0097  0.0044  -0.0012 52  ALA   B C   
4480 O  O   . ALA   B 52  ? 0.1424 0.1495 0.1851 0.0117  -0.0007 0.0012  52  ALA   B O   
4481 C  CB  . ALA   B 52  ? 0.1720 0.1504 0.1749 0.0072  0.0058  -0.0072 52  ALA   B CB  
4487 N  N   . LEU   B 53  ? 0.1344 0.1459 0.1567 0.0150  -0.0000 -0.0022 53  LEU   B N   
4488 C  CA  . LEU   B 53  ? 0.1358 0.1556 0.1508 0.0145  -0.0037 -0.0023 53  LEU   B CA  
4489 C  C   . LEU   B 53  ? 0.1417 0.1472 0.1441 0.0108  0.0044  0.0028  53  LEU   B C   
4490 O  O   . LEU   B 53  ? 0.1463 0.1562 0.1594 0.0034  0.0073  0.0162  53  LEU   B O   
4491 C  CB  . LEU   B 53  ? 0.1349 0.1630 0.1620 0.0080  -0.0014 0.0130  53  LEU   B CB  
4492 C  CG  . LEU   B 53  ? 0.1324 0.1722 0.1616 0.0036  -0.0067 0.0250  53  LEU   B CG  
4493 C  CD1 . LEU   B 53  ? 0.1411 0.1932 0.1892 0.0113  -0.0039 0.0046  53  LEU   B CD1 
4494 C  CD2 . LEU   B 53  ? 0.1503 0.1977 0.1945 -0.0060 -0.0138 -0.0089 53  LEU   B CD2 
4506 N  N   . ASN   B 54  ? 0.1412 0.1390 0.1460 0.0052  -0.0017 0.0020  54  ASN   B N   
4507 C  CA  . ASN   B 54  ? 0.1440 0.1518 0.1522 0.0044  -0.0105 -0.0033 54  ASN   B CA  
4508 C  C   . ASN   B 54  ? 0.1368 0.1518 0.1787 -0.0001 -0.0068 0.0013  54  ASN   B C   
4509 O  O   . ASN   B 54  ? 0.1344 0.1580 0.1905 -0.0026 0.0026  -0.0034 54  ASN   B O   
4510 C  CB  . ASN   B 54  ? 0.1505 0.1598 0.1702 0.0068  -0.0096 -0.0035 54  ASN   B CB  
4511 C  CG  . ASN   B 54  ? 0.1432 0.1675 0.1764 0.0082  -0.0100 -0.0003 54  ASN   B CG  
4512 O  OD1 . ASN   B 54  ? 0.1415 0.1664 0.1831 0.0024  -0.0119 -0.0140 54  ASN   B OD1 
4513 N  ND2 . ASN   B 54  ? 0.1555 0.1903 0.2077 0.0030  -0.0333 0.0127  54  ASN   B ND2 
4520 N  N   . LYS   B 55  ? 0.1369 0.1568 0.1988 0.0101  -0.0031 0.0069  55  LYS   B N   
4521 C  CA  . LYS   B 55  ? 0.1406 0.1700 0.2177 0.0165  -0.0023 -0.0025 55  LYS   B CA  
4522 C  C   . LYS   B 55  ? 0.1378 0.1682 0.2133 0.0113  0.0023  -0.0065 55  LYS   B C   
4523 O  O   . LYS   B 55  ? 0.1333 0.1819 0.2225 0.0072  0.0030  -0.0062 55  LYS   B O   
4524 C  CB  . LYS   B 55  ? 0.1586 0.1824 0.2589 0.0296  0.0095  0.0102  55  LYS   B CB  
4525 C  CG  . LYS   B 55  ? 0.1997 0.2153 0.3357 0.0379  0.0166  0.0285  55  LYS   B CG  
4526 C  CD  . LYS   B 55  ? 0.2382 0.2413 0.4047 0.0453  0.0213  0.0420  55  LYS   B CD  
4527 C  CE  . LYS   B 55  ? 0.2657 0.2626 0.4753 0.0421  0.0350  0.0446  55  LYS   B CE  
4528 N  NZ  . LYS   B 55  ? 0.2719 0.2780 0.5079 0.0399  0.0232  0.0527  55  LYS   B NZ  
4542 N  N   . ALA   B 56  ? 0.1373 0.1674 0.1912 0.0099  0.0009  -0.0093 56  ALA   B N   
4543 C  CA  . ALA   B 56  ? 0.1546 0.1857 0.1926 0.0041  0.0021  -0.0066 56  ALA   B CA  
4544 C  C   . ALA   B 56  ? 0.1542 0.1842 0.1857 0.0051  0.0143  0.0075  56  ALA   B C   
4545 O  O   . ALA   B 56  ? 0.1661 0.1926 0.1991 0.0056  0.0271  0.0011  56  ALA   B O   
4546 C  CB  . ALA   B 56  ? 0.1653 0.2033 0.2048 -0.0107 0.0099  -0.0044 56  ALA   B CB  
4552 N  N   . THR   B 57  ? 0.1486 0.1727 0.1917 0.0048  0.0133  0.0064  57  THR   B N   
4553 C  CA  . THR   B 57  ? 0.1525 0.1723 0.1874 -0.0030 0.0217  0.0115  57  THR   B CA  
4554 C  C   . THR   B 57  ? 0.1503 0.1793 0.2040 -0.0018 0.0183  0.0014  57  THR   B C   
4555 O  O   . THR   B 57  ? 0.1610 0.1796 0.2110 -0.0151 0.0117  0.0016  57  THR   B O   
4556 C  CB  . THR   B 57  ? 0.1610 0.1598 0.1659 -0.0021 0.0204  0.0087  57  THR   B CB  
4557 O  OG1 . THR   B 57  ? 0.1574 0.1493 0.1907 -0.0050 0.0132  0.0003  57  THR   B OG1 
4558 C  CG2 . THR   B 57  ? 0.1580 0.1678 0.1682 -0.0010 0.0201  0.0029  57  THR   B CG2 
4566 N  N   . ASN   B 58  ? 0.1363 0.1919 0.2261 -0.0091 0.0076  -0.0148 58  ASN   B N   
4567 C  CA  . ASN   B 58  ? 0.1493 0.2284 0.2652 -0.0206 0.0257  -0.0130 58  ASN   B CA  
4568 C  C   . ASN   B 58  ? 0.1381 0.2130 0.2295 -0.0136 -0.0006 -0.0113 58  ASN   B C   
4569 O  O   . ASN   B 58  ? 0.1483 0.2240 0.2397 -0.0167 -0.0041 -0.0175 58  ASN   B O   
4570 C  CB  . ASN   B 58  ? 0.2182 0.2870 0.3851 -0.0349 0.0567  -0.0064 58  ASN   B CB  
4571 C  CG  . ASN   B 58  ? 0.3286 0.3582 0.5245 -0.0402 0.0817  0.0169  58  ASN   B CG  
4572 O  OD1 . ASN   B 58  ? 0.3490 0.3677 0.5778 -0.0416 0.0841  0.0209  58  ASN   B OD1 
4573 N  ND2 . ASN   B 58  ? 0.3842 0.4006 0.5732 -0.0421 0.0932  0.0220  58  ASN   B ND2 
4580 N  N   . ASN   B 59  ? 0.1395 0.1980 0.2051 -0.0107 -0.0061 0.0023  59  ASN   B N   
4581 C  CA  . ASN   B 59  ? 0.1454 0.2017 0.2010 -0.0121 -0.0172 0.0130  59  ASN   B CA  
4582 C  C   . ASN   B 59  ? 0.1396 0.1931 0.1911 -0.0154 -0.0156 0.0016  59  ASN   B C   
4583 O  O   . ASN   B 59  ? 0.1467 0.1925 0.1923 -0.0144 -0.0108 0.0037  59  ASN   B O   
4584 C  CB  . ASN   B 59  ? 0.1554 0.2222 0.2113 -0.0061 -0.0253 0.0072  59  ASN   B CB  
4585 C  CG  . ASN   B 59  ? 0.1707 0.2413 0.2238 0.0004  -0.0427 0.0104  59  ASN   B CG  
4586 O  OD1 . ASN   B 59  ? 0.1741 0.2459 0.2294 0.0029  -0.0226 0.0222  59  ASN   B OD1 
4587 N  ND2 . ASN   B 59  ? 0.1799 0.2486 0.2292 -0.0044 -0.0436 -0.0039 59  ASN   B ND2 
4594 N  N   . ALA   B 60  ? 0.1373 0.1814 0.1857 -0.0124 -0.0037 -0.0004 60  ALA   B N   
4595 C  CA  . ALA   B 60  ? 0.1502 0.1698 0.1964 -0.0162 -0.0023 0.0092  60  ALA   B CA  
4596 C  C   . ALA   B 60  ? 0.1509 0.1571 0.1741 -0.0091 -0.0054 0.0084  60  ALA   B C   
4597 O  O   . ALA   B 60  ? 0.1558 0.1582 0.1906 -0.0147 -0.0023 -0.0119 60  ALA   B O   
4598 C  CB  . ALA   B 60  ? 0.1641 0.1697 0.2271 -0.0147 0.0043  0.0103  60  ALA   B CB  
4604 N  N   . MET   B 61  ? 0.1440 0.1500 0.1716 -0.0106 -0.0028 0.0072  61  MET   B N   
4605 C  CA  . MET   B 61  ? 0.1372 0.1450 0.1594 -0.0087 -0.0138 0.0020  61  MET   B CA  
4606 C  C   . MET   B 61  ? 0.1463 0.1471 0.1642 -0.0154 -0.0117 0.0023  61  MET   B C   
4607 O  O   . MET   B 61  ? 0.1507 0.1458 0.1560 -0.0059 -0.0060 -0.0101 61  MET   B O   
4608 C  CB  . MET   B 61  ? 0.1364 0.1498 0.1543 -0.0026 -0.0092 0.0025  61  MET   B CB  
4609 C  CG  . MET   B 61  ? 0.1390 0.1477 0.1430 -0.0023 -0.0102 0.0025  61  MET   B CG  
4610 S  SD  . MET   B 61  ? 0.1381 0.1475 0.1899 -0.0034 -0.0080 -0.0089 61  MET   B SD  
4611 C  CE  . MET   B 61  ? 0.1477 0.1708 0.2052 0.0013  -0.0018 -0.0201 61  MET   B CE  
4621 N  N   . GLN   B 62  ? 0.1447 0.1542 0.1542 -0.0038 -0.0178 0.0077  62  GLN   B N   
4622 C  CA  . GLN   B 62  ? 0.1471 0.1557 0.1615 0.0047  -0.0167 0.0006  62  GLN   B CA  
4623 C  C   . GLN   B 62  ? 0.1444 0.1658 0.1655 -0.0054 -0.0279 -0.0002 62  GLN   B C   
4624 O  O   . GLN   B 62  ? 0.1583 0.1648 0.1688 -0.0068 -0.0306 -0.0064 62  GLN   B O   
4625 C  CB  . GLN   B 62  ? 0.1556 0.1596 0.1630 0.0047  -0.0148 0.0024  62  GLN   B CB  
4626 C  CG  . GLN   B 62  ? 0.1571 0.1634 0.1642 0.0010  -0.0272 -0.0071 62  GLN   B CG  
4627 C  CD  . GLN   B 62  ? 0.1546 0.1574 0.1614 0.0032  -0.0266 0.0043  62  GLN   B CD  
4628 O  OE1 . GLN   B 62  ? 0.1578 0.1547 0.1847 -0.0005 -0.0305 -0.0029 62  GLN   B OE1 
4629 N  NE2 . GLN   B 62  ? 0.1548 0.1649 0.1795 0.0049  -0.0224 -0.0051 62  GLN   B NE2 
4638 N  N   . VAL   B 63  ? 0.1429 0.1680 0.1828 -0.0093 -0.0255 -0.0106 63  VAL   B N   
4639 C  CA  . VAL   B 63  ? 0.1588 0.1684 0.2011 -0.0140 -0.0343 -0.0074 63  VAL   B CA  
4640 C  C   . VAL   B 63  ? 0.1632 0.1541 0.1788 -0.0185 -0.0359 -0.0135 63  VAL   B C   
4641 O  O   . VAL   B 63  ? 0.1729 0.1604 0.1949 -0.0117 -0.0437 -0.0106 63  VAL   B O   
4642 C  CB  . VAL   B 63  ? 0.1581 0.1836 0.2448 -0.0164 -0.0371 -0.0133 63  VAL   B CB  
4643 C  CG1 . VAL   B 63  ? 0.1622 0.1862 0.2632 -0.0237 -0.0272 -0.0047 63  VAL   B CG1 
4644 C  CG2 . VAL   B 63  ? 0.1504 0.1985 0.2536 -0.0096 -0.0411 -0.0157 63  VAL   B CG2 
4654 N  N   . GLU   B 64  ? 0.1607 0.1466 0.1746 -0.0108 -0.0288 -0.0106 64  GLU   B N   
4655 C  CA  . GLU   B 64  ? 0.1617 0.1446 0.1707 -0.0081 -0.0283 -0.0026 64  GLU   B CA  
4656 C  C   . GLU   B 64  ? 0.1545 0.1417 0.1672 -0.0044 -0.0328 -0.0134 64  GLU   B C   
4657 O  O   . GLU   B 64  ? 0.1653 0.1486 0.1718 -0.0075 -0.0267 -0.0128 64  GLU   B O   
4658 C  CB  . GLU   B 64  ? 0.1582 0.1530 0.1661 -0.0125 -0.0180 0.0022  64  GLU   B CB  
4659 C  CG  . GLU   B 64  ? 0.1602 0.1533 0.1791 -0.0241 -0.0231 -0.0064 64  GLU   B CG  
4660 C  CD  . GLU   B 64  ? 0.1674 0.1675 0.1823 -0.0272 -0.0307 -0.0052 64  GLU   B CD  
4661 O  OE1 . GLU   B 64  ? 0.1695 0.1832 0.1894 -0.0324 -0.0210 -0.0202 64  GLU   B OE1 
4662 O  OE2 . GLU   B 64  ? 0.1824 0.1739 0.1853 -0.0322 -0.0413 -0.0063 64  GLU   B OE2 
4669 N  N   . SER   B 65  ? 0.1546 0.1372 0.1594 -0.0057 -0.0186 -0.0148 65  SER   B N   
4670 C  CA  . SER   B 65  ? 0.1522 0.1391 0.1637 -0.0029 -0.0231 -0.0127 65  SER   B CA  
4671 C  C   . SER   B 65  ? 0.1583 0.1381 0.1632 -0.0035 -0.0231 -0.0155 65  SER   B C   
4672 O  O   . SER   B 65  ? 0.1619 0.1519 0.1671 -0.0003 -0.0276 -0.0260 65  SER   B O   
4673 C  CB  . SER   B 65  ? 0.1509 0.1447 0.1648 -0.0058 -0.0170 -0.0117 65  SER   B CB  
4674 O  OG  . SER   B 65  ? 0.1512 0.1437 0.1709 -0.0082 -0.0193 -0.0196 65  SER   B OG  
4680 N  N   . ASP   B 66  ? 0.1674 0.1467 0.1606 -0.0048 -0.0327 -0.0117 66  ASP   B N   
4681 C  CA  . ASP   B 66  ? 0.1764 0.1542 0.1461 0.0012  -0.0357 -0.0079 66  ASP   B CA  
4682 C  C   . ASP   B 66  ? 0.1780 0.1627 0.1513 -0.0034 -0.0277 -0.0125 66  ASP   B C   
4683 O  O   . ASP   B 66  ? 0.1800 0.1636 0.1674 0.0065  -0.0274 -0.0160 66  ASP   B O   
4684 C  CB  . ASP   B 66  ? 0.1879 0.1683 0.1669 0.0098  -0.0471 -0.0163 66  ASP   B CB  
4685 C  CG  . ASP   B 66  ? 0.2150 0.1871 0.2091 0.0129  -0.0603 -0.0059 66  ASP   B CG  
4686 O  OD1 . ASP   B 66  ? 0.2330 0.1823 0.2189 0.0097  -0.0504 0.0032  66  ASP   B OD1 
4687 O  OD2 . ASP   B 66  ? 0.2322 0.2079 0.2681 0.0340  -0.0625 -0.0036 66  ASP   B OD2 
4692 N  N   . ASP   B 67  ? 0.1720 0.1512 0.1558 -0.0051 -0.0259 -0.0173 67  ASP   B N   
4693 C  CA  . ASP   B 67  ? 0.1844 0.1508 0.1774 -0.0052 -0.0242 -0.0109 67  ASP   B CA  
4694 C  C   . ASP   B 67  ? 0.1775 0.1527 0.1899 0.0040  -0.0264 -0.0159 67  ASP   B C   
4695 O  O   . ASP   B 67  ? 0.1810 0.1601 0.1915 0.0033  -0.0195 -0.0198 67  ASP   B O   
4696 C  CB  . ASP   B 67  ? 0.2090 0.1606 0.1898 -0.0153 -0.0358 -0.0107 67  ASP   B CB  
4697 C  CG  . ASP   B 67  ? 0.2495 0.1670 0.1963 -0.0121 -0.0656 -0.0123 67  ASP   B CG  
4698 O  OD1 . ASP   B 67  ? 0.2704 0.1744 0.2235 -0.0185 -0.0667 -0.0068 67  ASP   B OD1 
4699 O  OD2 . ASP   B 67  ? 0.2664 0.1757 0.2166 0.0039  -0.0718 -0.0091 67  ASP   B OD2 
4704 N  N   . TYR   B 68  ? 0.1722 0.1543 0.1779 0.0045  -0.0409 -0.0242 68  TYR   B N   
4705 C  CA  . TYR   B 68  ? 0.1719 0.1651 0.1849 0.0070  -0.0385 -0.0327 68  TYR   B CA  
4706 C  C   . TYR   B 68  ? 0.1666 0.1617 0.1762 0.0053  -0.0316 -0.0358 68  TYR   B C   
4707 O  O   . TYR   B 68  ? 0.1708 0.1723 0.1813 0.0053  -0.0276 -0.0487 68  TYR   B O   
4708 C  CB  . TYR   B 68  ? 0.1726 0.1882 0.1897 0.0085  -0.0420 -0.0406 68  TYR   B CB  
4709 C  CG  . TYR   B 68  ? 0.1836 0.2050 0.2041 0.0135  -0.0358 -0.0604 68  TYR   B CG  
4710 C  CD1 . TYR   B 68  ? 0.1858 0.2109 0.2266 -0.0023 -0.0297 -0.0619 68  TYR   B CD1 
4711 C  CD2 . TYR   B 68  ? 0.1894 0.2269 0.2195 0.0235  -0.0516 -0.0549 68  TYR   B CD2 
4712 C  CE1 . TYR   B 68  ? 0.1903 0.2242 0.2499 0.0024  -0.0309 -0.0569 68  TYR   B CE1 
4713 C  CE2 . TYR   B 68  ? 0.1912 0.2350 0.2247 0.0231  -0.0422 -0.0594 68  TYR   B CE2 
4714 C  CZ  . TYR   B 68  ? 0.1844 0.2308 0.2393 0.0083  -0.0389 -0.0638 68  TYR   B CZ  
4715 O  OH  . TYR   B 68  ? 0.1787 0.2464 0.2653 0.0028  -0.0265 -0.0472 68  TYR   B OH  
4725 N  N   . ILE   B 69  ? 0.1674 0.1510 0.1730 0.0030  -0.0303 -0.0315 69  ILE   B N   
4726 C  CA  . ILE   B 69  ? 0.1753 0.1605 0.1896 -0.0004 -0.0203 -0.0315 69  ILE   B CA  
4727 C  C   . ILE   B 69  ? 0.1742 0.1575 0.1737 0.0096  -0.0312 -0.0258 69  ILE   B C   
4728 O  O   . ILE   B 69  ? 0.1827 0.1737 0.1705 0.0027  -0.0221 -0.0319 69  ILE   B O   
4729 C  CB  . ILE   B 69  ? 0.1806 0.1637 0.2090 -0.0015 0.0040  -0.0300 69  ILE   B CB  
4730 C  CG1 . ILE   B 69  ? 0.1793 0.1678 0.2153 -0.0030 0.0157  -0.0339 69  ILE   B CG1 
4731 C  CG2 . ILE   B 69  ? 0.1923 0.1752 0.2225 0.0058  0.0017  -0.0206 69  ILE   B CG2 
4732 C  CD1 . ILE   B 69  ? 0.1720 0.1754 0.2242 -0.0173 0.0185  -0.0320 69  ILE   B CD1 
4744 N  N   . ALA   B 70  ? 0.1697 0.1607 0.1828 0.0062  -0.0393 -0.0239 70  ALA   B N   
4745 C  CA  . ALA   B 70  ? 0.1721 0.1620 0.1664 0.0046  -0.0387 -0.0251 70  ALA   B CA  
4746 C  C   . ALA   B 70  ? 0.1800 0.1593 0.1735 0.0007  -0.0423 -0.0316 70  ALA   B C   
4747 O  O   . ALA   B 70  ? 0.1914 0.1654 0.1754 0.0050  -0.0419 -0.0323 70  ALA   B O   
4748 C  CB  . ALA   B 70  ? 0.1719 0.1735 0.1758 0.0002  -0.0360 -0.0237 70  ALA   B CB  
4754 N  N   . THR   B 71  ? 0.1896 0.1598 0.1833 0.0006  -0.0519 -0.0327 71  THR   B N   
4755 C  CA  . THR   B 71  ? 0.2000 0.1645 0.2018 0.0096  -0.0638 -0.0316 71  THR   B CA  
4756 C  C   . THR   B 71  ? 0.1919 0.1706 0.2319 0.0279  -0.0605 -0.0500 71  THR   B C   
4757 O  O   . THR   B 71  ? 0.2027 0.1745 0.2768 0.0285  -0.0554 -0.0669 71  THR   B O   
4758 C  CB  . THR   B 71  ? 0.2277 0.1883 0.2229 -0.0017 -0.0747 -0.0136 71  THR   B CB  
4759 O  OG1 . THR   B 71  ? 0.2463 0.2143 0.2622 -0.0217 -0.0745 0.0065  71  THR   B OG1 
4760 C  CG2 . THR   B 71  ? 0.2466 0.1870 0.2455 -0.0020 -0.0634 -0.0029 71  THR   B CG2 
4768 N  N   . ASN   B 72  ? 0.1778 0.1721 0.2273 0.0191  -0.0669 -0.0661 72  ASN   B N   
4769 C  CA  . ASN   B 72  ? 0.1844 0.1870 0.2316 0.0188  -0.0484 -0.0692 72  ASN   B CA  
4770 C  C   . ASN   B 72  ? 0.1864 0.1975 0.2343 0.0054  -0.0303 -0.0677 72  ASN   B C   
4771 O  O   . ASN   B 72  ? 0.1844 0.2147 0.2607 0.0075  -0.0130 -0.0756 72  ASN   B O   
4772 C  CB  . ASN   B 72  ? 0.1882 0.2023 0.2290 0.0165  -0.0601 -0.0596 72  ASN   B CB  
4773 C  CG  . ASN   B 72  ? 0.2041 0.2176 0.2411 0.0346  -0.0619 -0.0374 72  ASN   B CG  
4774 O  OD1 . ASN   B 72  ? 0.2224 0.2362 0.2551 0.0188  -0.0529 -0.0432 72  ASN   B OD1 
4775 N  ND2 . ASN   B 72  ? 0.2172 0.2263 0.2882 0.0517  -0.0517 -0.0010 72  ASN   B ND2 
4782 N  N   . GLY   B 73  ? 0.1915 0.1954 0.2089 0.0007  -0.0307 -0.0631 73  GLY   B N   
4783 C  CA  . GLY   B 73  ? 0.1881 0.2002 0.1844 -0.0007 -0.0237 -0.0540 73  GLY   B CA  
4784 C  C   . GLY   B 73  ? 0.1799 0.1981 0.1489 0.0085  -0.0234 -0.0459 73  GLY   B C   
4785 O  O   . GLY   B 73  ? 0.1714 0.1834 0.1667 0.0087  -0.0205 -0.0351 73  GLY   B O   
4789 N  N   . PRO   B 74  ? 0.1830 0.2096 0.1495 0.0036  -0.0236 -0.0336 74  PRO   B N   
4790 C  CA  . PRO   B 74  ? 0.1725 0.2094 0.1363 0.0083  -0.0200 -0.0196 74  PRO   B CA  
4791 C  C   . PRO   B 74  ? 0.1580 0.1920 0.1461 0.0076  -0.0167 -0.0207 74  PRO   B C   
4792 O  O   . PRO   B 74  ? 0.1604 0.1959 0.1898 0.0059  -0.0113 -0.0276 74  PRO   B O   
4793 C  CB  . PRO   B 74  ? 0.1877 0.2273 0.1464 0.0013  -0.0179 -0.0157 74  PRO   B CB  
4794 C  CG  . PRO   B 74  ? 0.2070 0.2372 0.1686 0.0022  -0.0122 -0.0119 74  PRO   B CG  
4795 C  CD  . PRO   B 74  ? 0.2077 0.2283 0.1585 0.0057  -0.0072 -0.0260 74  PRO   B CD  
4803 N  N   . LEU   B 75  ? 0.1592 0.1807 0.1349 0.0082  -0.0222 -0.0196 75  LEU   B N   
4804 C  CA  . LEU   B 75  ? 0.1635 0.1862 0.1251 0.0040  -0.0186 -0.0063 75  LEU   B CA  
4805 C  C   . LEU   B 75  ? 0.1692 0.1970 0.1262 0.0039  -0.0038 -0.0053 75  LEU   B C   
4806 O  O   . LEU   B 75  ? 0.1844 0.2074 0.1469 -0.0012 -0.0022 0.0010  75  LEU   B O   
4807 C  CB  . LEU   B 75  ? 0.1718 0.1895 0.1223 -0.0071 -0.0210 0.0124  75  LEU   B CB  
4808 C  CG  . LEU   B 75  ? 0.2034 0.2027 0.1470 -0.0275 -0.0030 0.0100  75  LEU   B CG  
4809 C  CD1 . LEU   B 75  ? 0.2315 0.2155 0.1531 -0.0383 0.0194  -0.0058 75  LEU   B CD1 
4810 C  CD2 . LEU   B 75  ? 0.2403 0.2186 0.2181 -0.0220 0.0095  0.0191  75  LEU   B CD2 
4822 N  N   . LYS   B 76  ? 0.1665 0.2142 0.1588 0.0001  -0.0000 0.0069  76  LYS   B N   
4823 C  CA  . LYS   B 76  ? 0.1762 0.2198 0.1868 -0.0012 0.0246  0.0044  76  LYS   B CA  
4824 C  C   . LYS   B 76  ? 0.1698 0.2052 0.1517 0.0081  0.0067  0.0241  76  LYS   B C   
4825 O  O   . LYS   B 76  ? 0.1707 0.1879 0.1547 -0.0004 0.0018  0.0175  76  LYS   B O   
4826 C  CB  . LYS   B 76  ? 0.1918 0.2296 0.2526 -0.0054 0.0426  -0.0286 76  LYS   B CB  
4827 C  CG  . LYS   B 76  ? 0.1995 0.2505 0.2958 0.0032  0.0307  -0.0407 76  LYS   B CG  
4828 C  CD  . LYS   B 76  ? 0.2038 0.2653 0.3354 0.0108  0.0174  -0.0584 76  LYS   B CD  
4829 C  CE  . LYS   B 76  ? 0.2093 0.2875 0.3895 0.0117  0.0027  -0.0704 76  LYS   B CE  
4830 N  NZ  . LYS   B 76  ? 0.2095 0.2970 0.4060 0.0074  -0.0167 -0.0895 76  LYS   B NZ  
4844 N  N   . VAL   B 77  ? 0.1798 0.2159 0.1617 0.0187  0.0121  0.0254  77  VAL   B N   
4845 C  CA  . VAL   B 77  ? 0.1766 0.2081 0.1883 0.0197  0.0193  0.0541  77  VAL   B CA  
4846 C  C   . VAL   B 77  ? 0.1623 0.1837 0.1785 0.0184  0.0258  0.0391  77  VAL   B C   
4847 O  O   . VAL   B 77  ? 0.1666 0.1820 0.1752 0.0259  0.0290  0.0319  77  VAL   B O   
4848 C  CB  . VAL   B 77  ? 0.1857 0.2232 0.2293 0.0159  0.0316  0.0676  77  VAL   B CB  
4849 C  CG1 . VAL   B 77  ? 0.1848 0.2185 0.2562 0.0097  0.0386  0.0876  77  VAL   B CG1 
4850 C  CG2 . VAL   B 77  ? 0.1994 0.2386 0.2467 0.0140  0.0110  0.0677  77  VAL   B CG2 
4860 N  N   . GLY   B 78  ? 0.1577 0.1687 0.1691 0.0133  0.0214  0.0305  78  GLY   B N   
4861 C  CA  . GLY   B 78  ? 0.1590 0.1659 0.1629 0.0122  0.0299  0.0207  78  GLY   B CA  
4862 C  C   . GLY   B 78  ? 0.1517 0.1569 0.1545 0.0111  0.0193  0.0254  78  GLY   B C   
4863 O  O   . GLY   B 78  ? 0.1537 0.1525 0.1693 0.0181  0.0170  0.0219  78  GLY   B O   
4867 N  N   . GLY   B 79  ? 0.1442 0.1625 0.1639 0.0093  0.0095  0.0118  79  GLY   B N   
4868 C  CA  . GLY   B 79  ? 0.1450 0.1549 0.1601 0.0131  0.0066  0.0154  79  GLY   B CA  
4869 C  C   . GLY   B 79  ? 0.1369 0.1470 0.1607 0.0171  0.0068  0.0083  79  GLY   B C   
4870 O  O   . GLY   B 79  ? 0.1436 0.1441 0.1671 0.0142  0.0207  0.0191  79  GLY   B O   
4874 N  N   . SER   B 80  ? 0.1372 0.1389 0.1584 0.0091  0.0118  0.0055  80  SER   B N   
4875 C  CA  . SER   B 80  ? 0.1327 0.1331 0.1544 0.0044  0.0040  0.0100  80  SER   B CA  
4876 C  C   . SER   B 80  ? 0.1379 0.1289 0.1597 0.0061  -0.0079 0.0013  80  SER   B C   
4877 O  O   . SER   B 80  ? 0.1496 0.1321 0.1923 0.0101  0.0042  -0.0027 80  SER   B O   
4878 C  CB  . SER   B 80  ? 0.1364 0.1392 0.1693 0.0021  0.0027  0.0084  80  SER   B CB  
4879 O  OG  . SER   B 80  ? 0.1470 0.1574 0.1871 -0.0022 -0.0096 0.0073  80  SER   B OG  
4885 N  N   . CYS   B 81  ? 0.1391 0.1175 0.1631 -0.0012 -0.0059 -0.0028 81  CYS   B N   
4886 C  CA  . CYS   B 81  ? 0.1462 0.1237 0.1593 0.0072  -0.0147 -0.0028 81  CYS   B CA  
4887 C  C   . CYS   B 81  ? 0.1418 0.1188 0.1367 0.0032  -0.0119 -0.0023 81  CYS   B C   
4888 O  O   . CYS   B 81  ? 0.1604 0.1244 0.1574 0.0073  -0.0018 -0.0014 81  CYS   B O   
4889 C  CB  . CYS   B 81  ? 0.1568 0.1383 0.1614 0.0039  -0.0083 -0.0066 81  CYS   B CB  
4890 S  SG  . CYS   B 81  ? 0.1542 0.1517 0.1695 -0.0026 -0.0262 -0.0096 81  CYS   B SG  
4896 N  N   . VAL   B 82  ? 0.1411 0.1190 0.1525 0.0020  -0.0136 -0.0029 82  VAL   B N   
4897 C  CA  . VAL   B 82  ? 0.1505 0.1244 0.1411 -0.0030 -0.0122 0.0017  82  VAL   B CA  
4898 C  C   . VAL   B 82  ? 0.1541 0.1189 0.1559 -0.0032 -0.0103 -0.0006 82  VAL   B C   
4899 O  O   . VAL   B 82  ? 0.1615 0.1202 0.1812 -0.0022 -0.0084 -0.0134 82  VAL   B O   
4900 C  CB  . VAL   B 82  ? 0.1617 0.1446 0.1579 -0.0020 -0.0205 0.0018  82  VAL   B CB  
4901 C  CG1 . VAL   B 82  ? 0.1790 0.1641 0.1708 -0.0004 -0.0146 0.0197  82  VAL   B CG1 
4902 C  CG2 . VAL   B 82  ? 0.1672 0.1614 0.1741 -0.0055 -0.0333 0.0108  82  VAL   B CG2 
4912 N  N   . LEU   B 83  ? 0.1412 0.1187 0.1604 -0.0138 -0.0205 -0.0083 83  LEU   B N   
4913 C  CA  . LEU   B 83  ? 0.1462 0.1267 0.1458 -0.0120 -0.0191 -0.0020 83  LEU   B CA  
4914 C  C   . LEU   B 83  ? 0.1461 0.1264 0.1483 -0.0181 -0.0202 0.0018  83  LEU   B C   
4915 O  O   . LEU   B 83  ? 0.1487 0.1321 0.1348 -0.0222 -0.0133 0.0074  83  LEU   B O   
4916 C  CB  . LEU   B 83  ? 0.1557 0.1404 0.1458 -0.0109 -0.0230 -0.0063 83  LEU   B CB  
4917 C  CG  . LEU   B 83  ? 0.1714 0.1592 0.1573 -0.0127 -0.0171 -0.0064 83  LEU   B CG  
4918 C  CD1 . LEU   B 83  ? 0.1788 0.1657 0.1573 -0.0110 -0.0187 -0.0000 83  LEU   B CD1 
4919 C  CD2 . LEU   B 83  ? 0.1882 0.1617 0.1673 -0.0018 -0.0195 -0.0218 83  LEU   B CD2 
4931 N  N   . SER   B 84  ? 0.1506 0.1343 0.1732 -0.0244 -0.0177 0.0056  84  SER   B N   
4932 C  CA  . SER   B 84  ? 0.1509 0.1564 0.1559 -0.0276 -0.0176 0.0182  84  SER   B CA  
4933 C  C   . SER   B 84  ? 0.1432 0.1754 0.1187 -0.0249 -0.0166 0.0172  84  SER   B C   
4934 O  O   . SER   B 84  ? 0.1441 0.1579 0.1281 -0.0248 -0.0096 0.0042  84  SER   B O   
4935 C  CB  . SER   B 84  ? 0.1678 0.1585 0.2033 -0.0305 0.0035  0.0129  84  SER   B CB  
4936 O  OG  . SER   B 84  ? 0.1654 0.1730 0.2553 -0.0360 0.0016  0.0178  84  SER   B OG  
4942 N  N   . GLY   B 85  ? 0.1470 0.1957 0.1381 -0.0272 -0.0174 0.0177  85  GLY   B N   
4943 C  CA  . GLY   B 85  ? 0.1477 0.2006 0.1472 -0.0368 -0.0053 -0.0090 85  GLY   B CA  
4944 C  C   . GLY   B 85  ? 0.1464 0.1820 0.1443 -0.0415 -0.0036 0.0046  85  GLY   B C   
4945 O  O   . GLY   B 85  ? 0.1545 0.1804 0.1577 -0.0542 0.0096  -0.0088 85  GLY   B O   
4949 N  N   . HIS   B 86  ? 0.1421 0.1638 0.1620 -0.0315 -0.0106 0.0156  86  HIS   B N   
4950 C  CA  . HIS   B 86  ? 0.1487 0.1635 0.1504 -0.0334 -0.0218 0.0152  86  HIS   B CA  
4951 C  C   . HIS   B 86  ? 0.1486 0.1801 0.1421 -0.0441 -0.0157 0.0248  86  HIS   B C   
4952 O  O   . HIS   B 86  ? 0.1590 0.1916 0.1562 -0.0343 0.0003  0.0212  86  HIS   B O   
4953 C  CB  . HIS   B 86  ? 0.1570 0.1672 0.1474 -0.0208 -0.0201 0.0077  86  HIS   B CB  
4954 C  CG  . HIS   B 86  ? 0.1609 0.1736 0.1490 -0.0165 -0.0230 0.0140  86  HIS   B CG  
4955 N  ND1 . HIS   B 86  ? 0.1708 0.1937 0.1766 -0.0237 -0.0239 -0.0052 86  HIS   B ND1 
4956 C  CD2 . HIS   B 86  ? 0.1618 0.1791 0.1652 -0.0092 -0.0214 0.0143  86  HIS   B CD2 
4957 C  CE1 . HIS   B 86  ? 0.1767 0.1933 0.1727 -0.0165 -0.0113 -0.0176 86  HIS   B CE1 
4958 N  NE2 . HIS   B 86  ? 0.1691 0.1853 0.1609 -0.0027 -0.0151 0.0079  86  HIS   B NE2 
4966 N  N   . ASN   B 87  ? 0.1524 0.1817 0.1552 -0.0379 -0.0086 0.0179  87  ASN   B N   
4967 C  CA  . ASN   B 87  ? 0.1548 0.1964 0.1698 -0.0335 0.0154  0.0152  87  ASN   B CA  
4968 C  C   . ASN   B 87  ? 0.1676 0.1791 0.1657 -0.0294 0.0237  0.0110  87  ASN   B C   
4969 O  O   . ASN   B 87  ? 0.1933 0.1821 0.1994 -0.0224 0.0466  0.0088  87  ASN   B O   
4970 C  CB  . ASN   B 87  ? 0.1578 0.2312 0.2087 -0.0305 0.0202  0.0134  87  ASN   B CB  
4971 C  CG  . ASN   B 87  ? 0.1690 0.2536 0.2146 0.0055  0.0254  0.0258  87  ASN   B CG  
4972 O  OD1 . ASN   B 87  ? 0.1606 0.2355 0.1952 0.0082  0.0395  0.0389  87  ASN   B OD1 
4973 N  ND2 . ASN   B 87  ? 0.2063 0.2730 0.2501 0.0134  0.0330  0.0214  87  ASN   B ND2 
4980 N  N   . LEU   B 88  ? 0.1578 0.1741 0.1514 -0.0346 0.0059  0.0081  88  LEU   B N   
4981 C  CA  . LEU   B 88  ? 0.1708 0.1669 0.1520 -0.0353 0.0033  0.0006  88  LEU   B CA  
4982 C  C   . LEU   B 88  ? 0.1709 0.1552 0.1567 -0.0407 -0.0007 0.0022  88  LEU   B C   
4983 O  O   . LEU   B 88  ? 0.1942 0.1632 0.1826 -0.0245 -0.0263 -0.0019 88  LEU   B O   
4984 C  CB  . LEU   B 88  ? 0.1854 0.1746 0.1666 -0.0409 -0.0060 0.0152  88  LEU   B CB  
4985 C  CG  . LEU   B 88  ? 0.2191 0.2046 0.1827 -0.0364 -0.0235 0.0301  88  LEU   B CG  
4986 C  CD1 . LEU   B 88  ? 0.2297 0.2302 0.2002 -0.0492 -0.0186 0.0473  88  LEU   B CD1 
4987 C  CD2 . LEU   B 88  ? 0.2520 0.2299 0.2414 -0.0011 -0.0491 0.0051  88  LEU   B CD2 
4999 N  N   . ALA   B 89  ? 0.1569 0.1567 0.1462 -0.0406 0.0143  -0.0023 89  ALA   B N   
5000 C  CA  . ALA   B 89  ? 0.1527 0.1537 0.1285 -0.0385 0.0043  0.0063  89  ALA   B CA  
5001 C  C   . ALA   B 89  ? 0.1594 0.1523 0.1307 -0.0440 0.0132  0.0044  89  ALA   B C   
5002 O  O   . ALA   B 89  ? 0.1483 0.1617 0.1679 -0.0428 0.0092  -0.0202 89  ALA   B O   
5003 C  CB  . ALA   B 89  ? 0.1442 0.1507 0.1540 -0.0366 0.0040  0.0169  89  ALA   B CB  
5009 N  N   . LYS   B 90  ? 0.1956 0.1405 0.1430 -0.0481 -0.0074 0.0080  90  LYS   B N   
5010 C  CA  . LYS   B 90  ? 0.2125 0.1399 0.1333 -0.0422 -0.0113 0.0096  90  LYS   B CA  
5011 C  C   . LYS   B 90  ? 0.1948 0.1320 0.1431 -0.0433 -0.0134 0.0013  90  LYS   B C   
5012 O  O   . LYS   B 90  ? 0.2039 0.1513 0.1613 -0.0588 -0.0019 0.0004  90  LYS   B O   
5013 C  CB  . LYS   B 90  ? 0.2334 0.1467 0.1667 -0.0372 0.0020  0.0196  90  LYS   B CB  
5014 C  CG  . LYS   B 90  ? 0.2391 0.1625 0.1694 -0.0224 0.0310  0.0143  90  LYS   B CG  
5015 C  CD  . LYS   B 90  ? 0.2710 0.1800 0.2181 -0.0130 0.0569  -0.0072 90  LYS   B CD  
5016 C  CE  . LYS   B 90  ? 0.2863 0.1932 0.2719 -0.0164 0.0755  -0.0065 90  LYS   B CE  
5017 N  NZ  . LYS   B 90  ? 0.3026 0.1848 0.2706 -0.0237 0.0931  -0.0001 90  LYS   B NZ  
5031 N  N   . HIS   B 91  ? 0.1678 0.1242 0.1285 -0.0319 -0.0227 0.0078  91  HIS   B N   
5032 C  CA  . HIS   B 91  ? 0.1569 0.1231 0.1411 -0.0253 -0.0178 0.0038  91  HIS   B CA  
5033 C  C   . HIS   B 91  ? 0.1477 0.1282 0.1263 -0.0293 -0.0065 0.0007  91  HIS   B C   
5034 O  O   . HIS   B 91  ? 0.1589 0.1312 0.1340 -0.0316 -0.0160 0.0032  91  HIS   B O   
5035 C  CB  . HIS   B 91  ? 0.1765 0.1300 0.1715 -0.0098 -0.0065 0.0137  91  HIS   B CB  
5036 C  CG  . HIS   B 91  ? 0.2187 0.1461 0.2444 0.0016  0.0223  0.0272  91  HIS   B CG  
5037 N  ND1 . HIS   B 91  ? 0.2486 0.1512 0.3067 -0.0021 0.0246  0.0140  91  HIS   B ND1 
5038 C  CD2 . HIS   B 91  ? 0.2305 0.1754 0.2915 0.0142  0.0151  0.0596  91  HIS   B CD2 
5039 C  CE1 . HIS   B 91  ? 0.2537 0.1690 0.3180 0.0155  0.0256  0.0189  91  HIS   B CE1 
5040 N  NE2 . HIS   B 91  ? 0.2436 0.1806 0.3179 0.0252  0.0258  0.0594  91  HIS   B NE2 
5048 N  N   . CYS   B 92  ? 0.1417 0.1294 0.1327 -0.0213 -0.0137 -0.0003 92  CYS   B N   
5049 C  CA  . CYS   B 92  ? 0.1388 0.1192 0.1214 -0.0206 -0.0063 0.0019  92  CYS   B CA  
5050 C  C   . CYS   B 92  ? 0.1345 0.1134 0.1153 -0.0120 -0.0068 0.0068  92  CYS   B C   
5051 O  O   . CYS   B 92  ? 0.1427 0.1228 0.1483 -0.0145 -0.0046 0.0008  92  CYS   B O   
5052 C  CB  . CYS   B 92  ? 0.1411 0.1329 0.1256 -0.0141 -0.0085 0.0011  92  CYS   B CB  
5053 S  SG  . CYS   B 92  ? 0.1370 0.1323 0.1420 -0.0129 -0.0113 0.0049  92  CYS   B SG  
5059 N  N   . LEU   B 93  ? 0.1257 0.1179 0.1238 -0.0123 -0.0067 -0.0007 93  LEU   B N   
5060 C  CA  . LEU   B 93  ? 0.1274 0.1213 0.1397 -0.0044 -0.0094 0.0077  93  LEU   B CA  
5061 C  C   . LEU   B 93  ? 0.1222 0.1189 0.1251 -0.0039 -0.0063 0.0073  93  LEU   B C   
5062 O  O   . LEU   B 93  ? 0.1288 0.1164 0.1472 -0.0080 -0.0075 0.0023  93  LEU   B O   
5063 C  CB  . LEU   B 93  ? 0.1333 0.1200 0.1429 -0.0017 -0.0079 0.0119  93  LEU   B CB  
5064 C  CG  . LEU   B 93  ? 0.1294 0.1333 0.1619 -0.0030 -0.0098 0.0154  93  LEU   B CG  
5065 C  CD1 . LEU   B 93  ? 0.1376 0.1406 0.1620 0.0056  -0.0016 0.0032  93  LEU   B CD1 
5066 C  CD2 . LEU   B 93  ? 0.1254 0.1369 0.1731 -0.0019 -0.0094 0.0060  93  LEU   B CD2 
5078 N  N   . HIS   B 94  ? 0.1262 0.1175 0.1176 -0.0074 -0.0088 0.0077  94  HIS   B N   
5079 C  CA  . HIS   B 94  ? 0.1271 0.1173 0.1165 -0.0029 -0.0019 0.0098  94  HIS   B CA  
5080 C  C   . HIS   B 94  ? 0.1293 0.1191 0.1372 -0.0015 -0.0052 0.0093  94  HIS   B C   
5081 O  O   . HIS   B 94  ? 0.1303 0.1278 0.1855 -0.0039 0.0140  -0.0041 94  HIS   B O   
5082 C  CB  . HIS   B 94  ? 0.1285 0.1254 0.1335 -0.0010 -0.0036 0.0000  94  HIS   B CB  
5083 C  CG  . HIS   B 94  ? 0.1327 0.1198 0.1339 -0.0069 -0.0206 0.0053  94  HIS   B CG  
5084 N  ND1 . HIS   B 94  ? 0.1345 0.1258 0.1342 -0.0038 -0.0200 0.0040  94  HIS   B ND1 
5085 C  CD2 . HIS   B 94  ? 0.1343 0.1214 0.1397 -0.0035 -0.0155 0.0020  94  HIS   B CD2 
5086 C  CE1 . HIS   B 94  ? 0.1380 0.1269 0.1339 -0.0116 -0.0184 0.0049  94  HIS   B CE1 
5087 N  NE2 . HIS   B 94  ? 0.1314 0.1312 0.1449 -0.0144 -0.0164 0.0056  94  HIS   B NE2 
5095 N  N   . VAL   B 95  ? 0.1210 0.1156 0.1449 0.0026  -0.0012 0.0073  95  VAL   B N   
5096 C  CA  . VAL   B 95  ? 0.1240 0.1254 0.1433 0.0028  0.0007  0.0113  95  VAL   B CA  
5097 C  C   . VAL   B 95  ? 0.1358 0.1245 0.1431 -0.0028 0.0009  0.0097  95  VAL   B C   
5098 O  O   . VAL   B 95  ? 0.1402 0.1206 0.1626 0.0039  -0.0012 0.0166  95  VAL   B O   
5099 C  CB  . VAL   B 95  ? 0.1309 0.1216 0.1444 -0.0025 -0.0095 0.0023  95  VAL   B CB  
5100 C  CG1 . VAL   B 95  ? 0.1366 0.1378 0.1676 -0.0103 -0.0054 0.0165  95  VAL   B CG1 
5101 C  CG2 . VAL   B 95  ? 0.1359 0.1194 0.1535 0.0076  -0.0076 0.0060  95  VAL   B CG2 
5111 N  N   . VAL   B 96  ? 0.1436 0.1316 0.1378 0.0114  0.0068  0.0190  96  VAL   B N   
5112 C  CA  . VAL   B 96  ? 0.1469 0.1486 0.1277 0.0109  0.0100  0.0227  96  VAL   B CA  
5113 C  C   . VAL   B 96  ? 0.1486 0.1449 0.1492 0.0068  0.0137  0.0197  96  VAL   B C   
5114 O  O   . VAL   B 96  ? 0.1507 0.1494 0.1666 0.0049  0.0158  0.0075  96  VAL   B O   
5115 C  CB  . VAL   B 96  ? 0.1523 0.1646 0.1244 0.0091  0.0052  0.0151  96  VAL   B CB  
5116 C  CG1 . VAL   B 96  ? 0.1501 0.1779 0.1474 0.0152  0.0144  0.0170  96  VAL   B CG1 
5117 C  CG2 . VAL   B 96  ? 0.1634 0.1681 0.1584 0.0063  0.0076  0.0117  96  VAL   B CG2 
5127 N  N   . GLY   B 97  ? 0.1545 0.1447 0.1461 0.0051  0.0060  0.0229  97  GLY   B N   
5128 C  CA  . GLY   B 97  ? 0.1725 0.1448 0.1561 0.0055  0.0127  0.0249  97  GLY   B CA  
5129 C  C   . GLY   B 97  ? 0.1883 0.1564 0.1715 0.0116  0.0086  0.0164  97  GLY   B C   
5130 O  O   . GLY   B 97  ? 0.1985 0.1596 0.1764 0.0048  0.0053  0.0123  97  GLY   B O   
5134 N  N   . PRO   B 98  ? 0.2023 0.1628 0.1801 0.0141  0.0270  0.0363  98  PRO   B N   
5135 C  CA  . PRO   B 98  ? 0.2151 0.1784 0.1868 0.0250  0.0469  0.0307  98  PRO   B CA  
5136 C  C   . PRO   B 98  ? 0.2300 0.1787 0.1561 0.0397  0.0486  0.0507  98  PRO   B C   
5137 O  O   . PRO   B 98  ? 0.2177 0.1794 0.1810 0.0332  0.0466  0.0448  98  PRO   B O   
5138 C  CB  . PRO   B 98  ? 0.2070 0.1840 0.1967 0.0191  0.0555  0.0405  98  PRO   B CB  
5139 C  CG  . PRO   B 98  ? 0.2019 0.1787 0.1937 0.0160  0.0410  0.0514  98  PRO   B CG  
5140 C  CD  . PRO   B 98  ? 0.1883 0.1661 0.1875 0.0201  0.0359  0.0434  98  PRO   B CD  
5148 N  N   . ASN   B 99  ? 0.2431 0.1940 0.1745 0.0519  0.0445  0.0345  99  ASN   B N   
5149 C  CA  . ASN   B 99  ? 0.2675 0.2058 0.1875 0.0582  0.0390  0.0543  99  ASN   B CA  
5150 C  C   . ASN   B 99  ? 0.2980 0.2405 0.2139 0.0553  0.0632  0.0857  99  ASN   B C   
5151 O  O   . ASN   B 99  ? 0.3093 0.2479 0.2133 0.0641  0.0609  0.0808  99  ASN   B O   
5152 C  CB  . ASN   B 99  ? 0.2756 0.2002 0.1848 0.0561  0.0253  0.0425  99  ASN   B CB  
5153 C  CG  . ASN   B 99  ? 0.2758 0.2070 0.1988 0.0521  0.0183  0.0394  99  ASN   B CG  
5154 O  OD1 . ASN   B 99  ? 0.2758 0.2110 0.2282 0.0527  0.0250  0.0495  99  ASN   B OD1 
5155 N  ND2 . ASN   B 99  ? 0.2745 0.2110 0.2110 0.0535  -0.0076 0.0303  99  ASN   B ND2 
5162 N  N   A VAL   B 100 ? 0.3172 0.2577 0.2560 0.0398  0.0641  0.1056  100 VAL   B N   
5163 N  N   B VAL   B 100 ? 0.3185 0.2581 0.2557 0.0424  0.0581  0.1004  100 VAL   B N   
5164 C  CA  A VAL   B 100 ? 0.3440 0.2783 0.3062 0.0308  0.0597  0.1209  100 VAL   B CA  
5165 C  CA  B VAL   B 100 ? 0.3440 0.2770 0.2988 0.0342  0.0501  0.1124  100 VAL   B CA  
5166 C  C   A VAL   B 100 ? 0.3638 0.2838 0.2907 0.0381  0.0561  0.1374  100 VAL   B C   
5167 C  C   B VAL   B 100 ? 0.3633 0.2834 0.2911 0.0404  0.0476  0.1303  100 VAL   B C   
5168 O  O   A VAL   B 100 ? 0.3722 0.2945 0.2943 0.0372  0.0648  0.1309  100 VAL   B O   
5169 O  O   B VAL   B 100 ? 0.3695 0.2912 0.2934 0.0397  0.0524  0.1249  100 VAL   B O   
5170 C  CB  A VAL   B 100 ? 0.3531 0.2937 0.3688 0.0144  0.0599  0.1292  100 VAL   B CB  
5171 C  CB  B VAL   B 100 ? 0.3513 0.2895 0.3479 0.0202  0.0466  0.1132  100 VAL   B CB  
5172 C  CG1 A VAL   B 100 ? 0.3576 0.2996 0.3927 0.0135  0.0605  0.1325  100 VAL   B CG1 
5173 C  CG1 B VAL   B 100 ? 0.3546 0.2938 0.3664 0.0191  0.0461  0.1143  100 VAL   B CG1 
5174 C  CG2 A VAL   B 100 ? 0.3541 0.2972 0.3849 0.0049  0.0627  0.1386  100 VAL   B CG2 
5175 C  CG2 B VAL   B 100 ? 0.3526 0.2930 0.3619 0.0127  0.0465  0.1171  100 VAL   B CG2 
5194 N  N   . ASN   B 101 ? 0.3773 0.2863 0.2936 0.0487  0.0395  0.1413  101 ASN   B N   
5195 C  CA  . ASN   B 101 ? 0.4139 0.2993 0.3048 0.0610  0.0105  0.1442  101 ASN   B CA  
5196 C  C   . ASN   B 101 ? 0.4572 0.3367 0.3143 0.0638  -0.0010 0.1571  101 ASN   B C   
5197 O  O   . ASN   B 101 ? 0.4640 0.3501 0.3444 0.0683  0.0051  0.1271  101 ASN   B O   
5198 C  CB  . ASN   B 101 ? 0.4109 0.2810 0.3275 0.0581  0.0089  0.1237  101 ASN   B CB  
5199 C  CG  . ASN   B 101 ? 0.4087 0.2632 0.3344 0.0568  0.0111  0.1202  101 ASN   B CG  
5200 O  OD1 . ASN   B 101 ? 0.4111 0.2605 0.3520 0.0465  0.0313  0.1078  101 ASN   B OD1 
5201 N  ND2 . ASN   B 101 ? 0.4065 0.2589 0.3248 0.0592  0.0069  0.1097  101 ASN   B ND2 
5209 N  N   . LYS   B 102 ? 0.4905 0.3695 0.3445 0.0520  0.0043  0.1596  102 LYS   B N   
5210 C  CA  . LYS   B 102 ? 0.5222 0.4113 0.3732 0.0330  0.0165  0.1301  102 LYS   B CA  
5211 C  C   . LYS   B 102 ? 0.5204 0.4168 0.3494 0.0296  0.0237  0.1344  102 LYS   B C   
5212 O  O   . LYS   B 102 ? 0.5303 0.4237 0.3617 0.0324  0.0072  0.1264  102 LYS   B O   
5213 C  CB  . LYS   B 102 ? 0.5520 0.4472 0.4491 0.0178  0.0303  0.0827  102 LYS   B CB  
5214 C  CG  . LYS   B 102 ? 0.5783 0.4797 0.5144 0.0055  0.0441  0.0404  102 LYS   B CG  
5215 C  CD  . LYS   B 102 ? 0.6004 0.5061 0.5864 -0.0031 0.0573  0.0073  102 LYS   B CD  
5216 C  CE  . LYS   B 102 ? 0.6170 0.5248 0.6381 -0.0093 0.0644  -0.0176 102 LYS   B CE  
5217 N  NZ  . LYS   B 102 ? 0.6254 0.5352 0.6681 -0.0115 0.0649  -0.0318 102 LYS   B NZ  
5231 N  N   . GLY   B 103 ? 0.5036 0.4103 0.3472 0.0232  0.0464  0.1338  103 GLY   B N   
5232 C  CA  . GLY   B 103 ? 0.4844 0.4028 0.3538 0.0222  0.0620  0.1119  103 GLY   B CA  
5233 C  C   . GLY   B 103 ? 0.4604 0.3899 0.3477 0.0209  0.0755  0.0894  103 GLY   B C   
5234 O  O   . GLY   B 103 ? 0.4677 0.3975 0.3581 0.0231  0.0781  0.0881  103 GLY   B O   
5238 N  N   A GLU   B 104 ? 0.4433 0.3775 0.3326 0.0209  0.0876  0.0767  104 GLU   B N   
5239 N  N   B GLU   B 104 ? 0.4431 0.3775 0.3396 0.0169  0.0720  0.0744  104 GLU   B N   
5240 C  CA  A GLU   B 104 ? 0.4239 0.3651 0.3119 0.0240  0.0970  0.0615  104 GLU   B CA  
5241 C  CA  B GLU   B 104 ? 0.4237 0.3646 0.3256 0.0144  0.0677  0.0570  104 GLU   B CA  
5242 C  C   A GLU   B 104 ? 0.4233 0.3702 0.3270 0.0089  0.1345  0.0624  104 GLU   B C   
5243 C  C   B GLU   B 104 ? 0.4177 0.3637 0.3366 0.0063  0.0878  0.0533  104 GLU   B C   
5244 O  O   A GLU   B 104 ? 0.4264 0.3766 0.3396 0.0034  0.1332  0.0599  104 GLU   B O   
5245 O  O   B GLU   B 104 ? 0.4201 0.3668 0.3438 0.0035  0.0864  0.0495  104 GLU   B O   
5246 C  CB  A GLU   B 104 ? 0.4077 0.3460 0.2937 0.0440  0.0623  0.0362  104 GLU   B CB  
5247 C  CB  B GLU   B 104 ? 0.4120 0.3514 0.3096 0.0206  0.0412  0.0371  104 GLU   B CB  
5248 C  CG  A GLU   B 104 ? 0.3926 0.3297 0.2728 0.0654  0.0261  0.0064  104 GLU   B CG  
5249 C  CG  B GLU   B 104 ? 0.4023 0.3408 0.2941 0.0275  0.0148  0.0146  104 GLU   B CG  
5250 C  CD  A GLU   B 104 ? 0.3789 0.3143 0.2508 0.0872  -0.0072 -0.0130 104 GLU   B CD  
5251 C  CD  B GLU   B 104 ? 0.3956 0.3318 0.2802 0.0335  -0.0083 -0.0003 104 GLU   B CD  
5252 O  OE1 A GLU   B 104 ? 0.3644 0.2969 0.2127 0.1063  -0.0024 -0.0214 104 GLU   B OE1 
5253 O  OE1 B GLU   B 104 ? 0.3906 0.3245 0.2619 0.0370  -0.0082 -0.0044 104 GLU   B OE1 
5254 O  OE2 A GLU   B 104 ? 0.3801 0.3187 0.2436 0.0864  -0.0350 -0.0246 104 GLU   B OE2 
5255 O  OE2 B GLU   B 104 ? 0.3951 0.3324 0.2747 0.0339  -0.0262 -0.0085 104 GLU   B OE2 
5268 N  N   A ASP   B 105 ? 0.4172 0.3677 0.3210 -0.0001 0.1668  0.0634  105 ASP   B N   
5269 N  N   B ASP   B 105 ? 0.4080 0.3592 0.3296 0.0008  0.1060  0.0520  105 ASP   B N   
5270 C  CA  A ASP   B 105 ? 0.4154 0.3671 0.3391 -0.0070 0.1859  0.0462  105 ASP   B CA  
5271 C  CA  B ASP   B 105 ? 0.4011 0.3553 0.3385 -0.0041 0.1162  0.0414  105 ASP   B CA  
5272 C  C   A ASP   B 105 ? 0.3976 0.3416 0.3060 -0.0190 0.1924  0.0437  105 ASP   B C   
5273 C  C   B ASP   B 105 ? 0.3911 0.3420 0.3180 -0.0113 0.1194  0.0336  105 ASP   B C   
5274 O  O   A ASP   B 105 ? 0.3850 0.3364 0.2878 -0.0176 0.1884  0.0402  105 ASP   B O   
5275 O  O   B ASP   B 105 ? 0.3886 0.3390 0.3023 -0.0120 0.1242  0.0343  105 ASP   B O   
5276 C  CB  A ASP   B 105 ? 0.4297 0.3896 0.4042 0.0002  0.1906  0.0267  105 ASP   B CB  
5277 C  CB  B ASP   B 105 ? 0.4034 0.3644 0.3708 -0.0012 0.1219  0.0375  105 ASP   B CB  
5278 C  CG  A ASP   B 105 ? 0.4421 0.4084 0.4694 0.0020  0.1996  0.0154  105 ASP   B CG  
5279 C  CG  B ASP   B 105 ? 0.4058 0.3709 0.4047 -0.0023 0.1312  0.0403  105 ASP   B CG  
5280 O  OD1 A ASP   B 105 ? 0.4418 0.4123 0.4772 -0.0021 0.2137  0.0200  105 ASP   B OD1 
5281 O  OD1 B ASP   B 105 ? 0.4044 0.3747 0.4109 -0.0059 0.1353  0.0442  105 ASP   B OD1 
5282 O  OD2 A ASP   B 105 ? 0.4501 0.4182 0.5071 0.0061  0.1914  0.0038  105 ASP   B OD2 
5283 O  OD2 B ASP   B 105 ? 0.4058 0.3721 0.4105 -0.0028 0.1399  0.0428  105 ASP   B OD2 
5292 N  N   A ILE   B 106 ? 0.3900 0.3197 0.3143 -0.0288 0.1805  0.0431  106 ILE   B N   
5293 N  N   B ILE   B 106 ? 0.3824 0.3311 0.3158 -0.0146 0.1113  0.0266  106 ILE   B N   
5294 C  CA  A ILE   B 106 ? 0.3708 0.2908 0.3186 -0.0429 0.1785  0.0398  106 ILE   B CA  
5295 C  CA  B ILE   B 106 ? 0.3680 0.3181 0.3182 -0.0194 0.1080  0.0170  106 ILE   B CA  
5296 C  C   A ILE   B 106 ? 0.3389 0.2793 0.3016 -0.0395 0.1778  0.0319  106 ILE   B C   
5297 C  C   B ILE   B 106 ? 0.3446 0.3114 0.3114 -0.0156 0.1045  0.0060  106 ILE   B C   
5298 O  O   A ILE   B 106 ? 0.3291 0.2572 0.3029 -0.0442 0.1712  0.0338  106 ILE   B O   
5299 O  O   B ILE   B 106 ? 0.3401 0.3021 0.3120 -0.0184 0.0987  0.0008  106 ILE   B O   
5300 C  CB  A ILE   B 106 ? 0.3859 0.2785 0.3442 -0.0551 0.1694  0.0424  106 ILE   B CB  
5301 C  CB  B ILE   B 106 ? 0.3773 0.3147 0.3301 -0.0264 0.1071  0.0168  106 ILE   B CB  
5302 C  CG1 A ILE   B 106 ? 0.3941 0.2767 0.3537 -0.0453 0.1592  0.0336  106 ILE   B CG1 
5303 C  CG1 B ILE   B 106 ? 0.3816 0.3132 0.3362 -0.0215 0.1028  0.0142  106 ILE   B CG1 
5304 C  CG2 A ILE   B 106 ? 0.3896 0.2768 0.3627 -0.0686 0.1706  0.0502  106 ILE   B CG2 
5305 C  CG2 B ILE   B 106 ? 0.3804 0.3166 0.3415 -0.0332 0.1088  0.0180  106 ILE   B CG2 
5306 C  CD1 A ILE   B 106 ? 0.3979 0.2775 0.3522 -0.0366 0.1548  0.0326  106 ILE   B CD1 
5307 C  CD1 B ILE   B 106 ? 0.3835 0.3130 0.3372 -0.0169 0.1002  0.0140  106 ILE   B CD1 
5330 N  N   A GLN   B 107 ? 0.3217 0.2943 0.3197 -0.0328 0.1658  0.0246  107 GLN   B N   
5331 N  N   B GLN   B 107 ? 0.3285 0.3162 0.3246 -0.0113 0.1026  0.0028  107 GLN   B N   
5332 C  CA  A GLN   B 107 ? 0.3037 0.3094 0.3393 -0.0240 0.1435  0.0204  107 GLN   B CA  
5333 C  CA  B GLN   B 107 ? 0.3127 0.3197 0.3373 -0.0061 0.0964  0.0056  107 GLN   B CA  
5334 C  C   A GLN   B 107 ? 0.2711 0.2858 0.3084 -0.0101 0.1127  0.0104  107 GLN   B C   
5335 C  C   B GLN   B 107 ? 0.2792 0.2941 0.3050 0.0007  0.0922  0.0041  107 GLN   B C   
5336 O  O   A GLN   B 107 ? 0.2617 0.2845 0.3364 -0.0053 0.0868  -0.0100 107 GLN   B O   
5337 O  O   B GLN   B 107 ? 0.2749 0.2971 0.3216 0.0032  0.0765  -0.0100 107 GLN   B O   
5338 C  CB  A GLN   B 107 ? 0.3325 0.3510 0.4129 -0.0205 0.1196  0.0204  107 GLN   B CB  
5339 C  CB  B GLN   B 107 ? 0.3353 0.3493 0.3960 -0.0043 0.0817  0.0078  107 GLN   B CB  
5340 C  CG  A GLN   B 107 ? 0.3619 0.3884 0.4870 -0.0139 0.0859  0.0187  107 GLN   B CG  
5341 C  CG  B GLN   B 107 ? 0.3567 0.3760 0.4550 -0.0011 0.0611  0.0093  107 GLN   B CG  
5342 C  CD  A GLN   B 107 ? 0.3812 0.4171 0.5458 -0.0129 0.0649  0.0205  107 GLN   B CD  
5343 C  CD  B GLN   B 107 ? 0.3714 0.3966 0.5034 -0.0012 0.0474  0.0118  107 GLN   B CD  
5344 O  OE1 A GLN   B 107 ? 0.3891 0.4264 0.5663 -0.0151 0.0634  0.0179  107 GLN   B OE1 
5345 O  OE1 B GLN   B 107 ? 0.3776 0.4050 0.5194 -0.0033 0.0471  0.0109  107 GLN   B OE1 
5346 N  NE2 A GLN   B 107 ? 0.3876 0.4271 0.5652 -0.0082 0.0542  0.0251  107 GLN   B NE2 
5347 N  NE2 B GLN   B 107 ? 0.3759 0.4030 0.5201 0.0019  0.0406  0.0147  107 GLN   B NE2 
5364 N  N   . LEU   B 108 ? 0.2503 0.2652 0.2747 0.0126  0.0987  0.0110  108 LEU   B N   
5365 C  CA  . LEU   B 108 ? 0.2261 0.2332 0.2322 0.0305  0.0762  0.0270  108 LEU   B CA  
5366 C  C   . LEU   B 108 ? 0.1888 0.1882 0.2312 0.0273  0.0489  0.0301  108 LEU   B C   
5367 O  O   . LEU   B 108 ? 0.1872 0.1793 0.2236 0.0215  0.0392  0.0293  108 LEU   B O   
5368 C  CB  . LEU   B 108 ? 0.2458 0.2567 0.2246 0.0325  0.0712  0.0342  108 LEU   B CB  
5369 C  CG  . LEU   B 108 ? 0.2628 0.2872 0.2346 0.0353  0.0586  0.0146  108 LEU   B CG  
5370 C  CD1 . LEU   B 108 ? 0.2741 0.3000 0.2202 0.0275  0.0618  0.0124  108 LEU   B CD1 
5371 C  CD2 . LEU   B 108 ? 0.2748 0.3012 0.2454 0.0419  0.0402  0.0017  108 LEU   B CD2 
5384 N  N   . LEU   B 109 ? 0.1728 0.1689 0.2267 0.0176  0.0395  0.0251  109 LEU   B N   
5385 C  CA  . LEU   B 109 ? 0.1539 0.1430 0.2347 0.0107  0.0352  0.0251  109 LEU   B CA  
5386 C  C   . LEU   B 109 ? 0.1432 0.1306 0.2317 0.0028  0.0335  0.0181  109 LEU   B C   
5387 O  O   . LEU   B 109 ? 0.1425 0.1283 0.2251 0.0050  0.0278  0.0283  109 LEU   B O   
5388 C  CB  . LEU   B 109 ? 0.1623 0.1341 0.2429 0.0084  0.0246  0.0366  109 LEU   B CB  
5389 C  CG  . LEU   B 109 ? 0.1604 0.1333 0.2325 0.0059  0.0177  0.0257  109 LEU   B CG  
5390 C  CD1 . LEU   B 109 ? 0.1637 0.1475 0.2119 0.0116  0.0178  0.0222  109 LEU   B CD1 
5391 C  CD2 . LEU   B 109 ? 0.1663 0.1397 0.2539 0.0065  0.0151  0.0285  109 LEU   B CD2 
5403 N  N   . LYS   B 110 ? 0.1417 0.1344 0.2237 -0.0027 0.0306  0.0223  110 LYS   B N   
5404 C  CA  . LYS   B 110 ? 0.1388 0.1320 0.2236 -0.0008 0.0255  0.0218  110 LYS   B CA  
5405 C  C   . LYS   B 110 ? 0.1344 0.1316 0.2243 -0.0032 0.0260  0.0196  110 LYS   B C   
5406 O  O   . LYS   B 110 ? 0.1306 0.1325 0.2153 -0.0030 0.0193  0.0102  110 LYS   B O   
5407 C  CB  . LYS   B 110 ? 0.1420 0.1288 0.2409 -0.0019 0.0264  0.0137  110 LYS   B CB  
5408 C  CG  . LYS   B 110 ? 0.1459 0.1320 0.2554 -0.0056 0.0091  0.0217  110 LYS   B CG  
5409 C  CD  . LYS   B 110 ? 0.1509 0.1368 0.2578 -0.0080 0.0119  0.0174  110 LYS   B CD  
5410 C  CE  . LYS   B 110 ? 0.1456 0.1480 0.2760 -0.0059 0.0160  0.0076  110 LYS   B CE  
5411 N  NZ  . LYS   B 110 ? 0.1441 0.1627 0.2713 -0.0027 0.0091  0.0048  110 LYS   B NZ  
5425 N  N   . SER   B 111 ? 0.1434 0.1298 0.2354 -0.0034 0.0306  0.0204  111 SER   B N   
5426 C  CA  . SER   B 111 ? 0.1508 0.1353 0.2178 0.0051  0.0207  0.0200  111 SER   B CA  
5427 C  C   . SER   B 111 ? 0.1442 0.1255 0.1987 0.0072  0.0138  0.0132  111 SER   B C   
5428 O  O   . SER   B 111 ? 0.1374 0.1343 0.2138 0.0037  0.0054  0.0098  111 SER   B O   
5429 C  CB  . SER   B 111 ? 0.1620 0.1559 0.2301 0.0071  0.0346  0.0292  111 SER   B CB  
5430 O  OG  . SER   B 111 ? 0.1802 0.1878 0.2265 0.0120  0.0445  0.0329  111 SER   B OG  
5436 N  N   . ALA   B 112 ? 0.1324 0.1300 0.2129 0.0076  0.0219  0.0212  112 ALA   B N   
5437 C  CA  . ALA   B 112 ? 0.1300 0.1373 0.1926 0.0012  0.0081  0.0092  112 ALA   B CA  
5438 C  C   . ALA   B 112 ? 0.1228 0.1313 0.1783 0.0024  0.0069  0.0089  112 ALA   B C   
5439 O  O   . ALA   B 112 ? 0.1239 0.1312 0.1889 -0.0027 0.0128  0.0023  112 ALA   B O   
5440 C  CB  . ALA   B 112 ? 0.1300 0.1413 0.2085 0.0097  0.0050  0.0191  112 ALA   B CB  
5446 N  N   . TYR   B 113 ? 0.1242 0.1211 0.1929 -0.0007 0.0126  0.0132  113 TYR   B N   
5447 C  CA  . TYR   B 113 ? 0.1224 0.1188 0.1948 -0.0032 0.0177  0.0017  113 TYR   B CA  
5448 C  C   . TYR   B 113 ? 0.1210 0.1183 0.1945 -0.0122 0.0100  0.0025  113 TYR   B C   
5449 O  O   . TYR   B 113 ? 0.1250 0.1168 0.1878 -0.0082 0.0005  0.0013  113 TYR   B O   
5450 C  CB  . TYR   B 113 ? 0.1286 0.1144 0.1947 -0.0024 0.0182  0.0068  113 TYR   B CB  
5451 C  CG  . TYR   B 113 ? 0.1309 0.1127 0.2091 -0.0076 0.0103  0.0133  113 TYR   B CG  
5452 C  CD1 . TYR   B 113 ? 0.1388 0.1165 0.2280 -0.0091 0.0141  0.0171  113 TYR   B CD1 
5453 C  CD2 . TYR   B 113 ? 0.1388 0.1164 0.2084 -0.0043 0.0076  0.0097  113 TYR   B CD2 
5454 C  CE1 . TYR   B 113 ? 0.1372 0.1189 0.2218 -0.0030 0.0159  0.0060  113 TYR   B CE1 
5455 C  CE2 . TYR   B 113 ? 0.1438 0.1081 0.2213 -0.0015 0.0085  0.0176  113 TYR   B CE2 
5456 C  CZ  . TYR   B 113 ? 0.1357 0.1138 0.2267 0.0051  0.0096  0.0064  113 TYR   B CZ  
5457 O  OH  . TYR   B 113 ? 0.1416 0.1147 0.2570 0.0065  0.0201  0.0089  113 TYR   B OH  
5467 N  N   . GLU   B 114 ? 0.1169 0.1130 0.2076 -0.0039 0.0104  0.0086  114 GLU   B N   
5468 C  CA  . GLU   B 114 ? 0.1157 0.1090 0.2008 0.0036  0.0024  0.0042  114 GLU   B CA  
5469 C  C   . GLU   B 114 ? 0.1178 0.1118 0.1886 0.0019  0.0068  0.0014  114 GLU   B C   
5470 O  O   . GLU   B 114 ? 0.1198 0.1179 0.2004 0.0036  -0.0015 0.0118  114 GLU   B O   
5471 C  CB  . GLU   B 114 ? 0.1168 0.1194 0.2119 -0.0001 0.0085  0.0030  114 GLU   B CB  
5472 C  CG  . GLU   B 114 ? 0.1251 0.1177 0.2189 -0.0041 0.0083  0.0107  114 GLU   B CG  
5473 C  CD  . GLU   B 114 ? 0.1228 0.1239 0.2292 -0.0087 0.0078  0.0116  114 GLU   B CD  
5474 O  OE1 . GLU   B 114 ? 0.1208 0.1364 0.2164 -0.0071 0.0197  0.0109  114 GLU   B OE1 
5475 O  OE2 . GLU   B 114 ? 0.1220 0.1436 0.2389 -0.0171 0.0081  0.0104  114 GLU   B OE2 
5482 N  N   . ASN   B 115 ? 0.1225 0.1097 0.1811 -0.0015 -0.0011 0.0094  115 ASN   B N   
5483 C  CA  . ASN   B 115 ? 0.1273 0.1136 0.1716 -0.0036 0.0007  0.0070  115 ASN   B CA  
5484 C  C   . ASN   B 115 ? 0.1209 0.1110 0.1692 -0.0094 -0.0040 0.0024  115 ASN   B C   
5485 O  O   . ASN   B 115 ? 0.1286 0.1174 0.1908 -0.0111 0.0018  0.0051  115 ASN   B O   
5486 C  CB  . ASN   B 115 ? 0.1343 0.1215 0.1705 -0.0112 0.0003  0.0090  115 ASN   B CB  
5487 C  CG  . ASN   B 115 ? 0.1457 0.1339 0.1704 0.0031  -0.0025 0.0016  115 ASN   B CG  
5488 O  OD1 . ASN   B 115 ? 0.1894 0.1481 0.1934 0.0036  0.0158  -0.0056 115 ASN   B OD1 
5489 N  ND2 . ASN   B 115 ? 0.1420 0.1437 0.1719 -0.0041 0.0011  0.0073  115 ASN   B ND2 
5496 N  N   . PHE   B 116 ? 0.1202 0.1164 0.1690 -0.0035 -0.0014 0.0051  116 PHE   B N   
5497 C  CA  . PHE   B 116 ? 0.1243 0.1213 0.1670 -0.0119 -0.0050 0.0074  116 PHE   B CA  
5498 C  C   . PHE   B 116 ? 0.1273 0.1071 0.1667 -0.0118 -0.0065 0.0108  116 PHE   B C   
5499 O  O   . PHE   B 116 ? 0.1309 0.1187 0.1737 -0.0026 -0.0065 0.0083  116 PHE   B O   
5500 C  CB  . PHE   B 116 ? 0.1207 0.1150 0.1686 -0.0048 -0.0101 0.0078  116 PHE   B CB  
5501 C  CG  . PHE   B 116 ? 0.1182 0.1162 0.1636 -0.0042 -0.0025 0.0107  116 PHE   B CG  
5502 C  CD1 . PHE   B 116 ? 0.1263 0.1188 0.1839 0.0003  -0.0021 0.0116  116 PHE   B CD1 
5503 C  CD2 . PHE   B 116 ? 0.1244 0.1254 0.1596 -0.0051 0.0042  0.0012  116 PHE   B CD2 
5504 C  CE1 . PHE   B 116 ? 0.1299 0.1239 0.1799 -0.0014 -0.0071 0.0049  116 PHE   B CE1 
5505 C  CE2 . PHE   B 116 ? 0.1236 0.1235 0.1659 -0.0023 0.0048  0.0062  116 PHE   B CE2 
5506 C  CZ  . PHE   B 116 ? 0.1204 0.1251 0.1743 -0.0030 -0.0091 0.0092  116 PHE   B CZ  
5516 N  N   . ASN   B 117 ? 0.1266 0.1154 0.1807 -0.0033 -0.0094 0.0045  117 ASN   B N   
5517 C  CA  . ASN   B 117 ? 0.1336 0.1155 0.1851 -0.0001 -0.0117 0.0025  117 ASN   B CA  
5518 C  C   . ASN   B 117 ? 0.1336 0.1152 0.2001 0.0024  -0.0104 0.0055  117 ASN   B C   
5519 O  O   . ASN   B 117 ? 0.1410 0.1208 0.2241 -0.0044 -0.0280 0.0104  117 ASN   B O   
5520 C  CB  . ASN   B 117 ? 0.1313 0.1185 0.2023 -0.0014 -0.0082 -0.0052 117 ASN   B CB  
5521 C  CG  . ASN   B 117 ? 0.1273 0.1211 0.2124 -0.0007 -0.0029 -0.0071 117 ASN   B CG  
5522 O  OD1 . ASN   B 117 ? 0.1499 0.1214 0.2191 -0.0115 0.0046  -0.0036 117 ASN   B OD1 
5523 N  ND2 . ASN   B 117 ? 0.1265 0.1241 0.2044 -0.0048 0.0017  -0.0018 117 ASN   B ND2 
5530 N  N   . GLN   B 118 ? 0.1364 0.1096 0.1993 -0.0048 -0.0167 0.0031  118 GLN   B N   
5531 C  CA  . GLN   B 118 ? 0.1352 0.1140 0.2063 -0.0042 -0.0117 0.0005  118 GLN   B CA  
5532 C  C   . GLN   B 118 ? 0.1382 0.1125 0.2042 -0.0012 -0.0048 -0.0010 118 GLN   B C   
5533 O  O   . GLN   B 118 ? 0.1582 0.1157 0.2487 -0.0063 0.0035  0.0046  118 GLN   B O   
5534 C  CB  . GLN   B 118 ? 0.1434 0.1211 0.2158 -0.0018 -0.0139 -0.0003 118 GLN   B CB  
5535 C  CG  . GLN   B 118 ? 0.1486 0.1230 0.2103 0.0043  -0.0112 -0.0118 118 GLN   B CG  
5536 C  CD  . GLN   B 118 ? 0.1549 0.1187 0.2089 0.0037  -0.0128 -0.0136 118 GLN   B CD  
5537 O  OE1 . GLN   B 118 ? 0.1659 0.1172 0.2290 0.0047  0.0064  0.0004  118 GLN   B OE1 
5538 N  NE2 . GLN   B 118 ? 0.1595 0.1226 0.2159 0.0004  -0.0163 0.0024  118 GLN   B NE2 
5547 N  N   . HIS   B 119 ? 0.1375 0.1191 0.1777 -0.0073 -0.0089 0.0102  119 HIS   B N   
5548 C  CA  . HIS   B 119 ? 0.1508 0.1325 0.1638 -0.0035 -0.0181 0.0140  119 HIS   B CA  
5549 C  C   . HIS   B 119 ? 0.1570 0.1313 0.1659 -0.0023 -0.0343 0.0100  119 HIS   B C   
5550 O  O   . HIS   B 119 ? 0.1648 0.1249 0.1841 -0.0222 -0.0268 0.0112  119 HIS   B O   
5551 C  CB  . HIS   B 119 ? 0.1577 0.1466 0.1660 -0.0034 -0.0201 0.0060  119 HIS   B CB  
5552 C  CG  . HIS   B 119 ? 0.1654 0.1664 0.1820 0.0050  -0.0452 -0.0114 119 HIS   B CG  
5553 N  ND1 . HIS   B 119 ? 0.1751 0.1778 0.2224 0.0001  -0.0519 -0.0342 119 HIS   B ND1 
5554 C  CD2 . HIS   B 119 ? 0.1800 0.1850 0.1827 0.0362  -0.0520 -0.0168 119 HIS   B CD2 
5555 C  CE1 . HIS   B 119 ? 0.1942 0.1968 0.2241 0.0168  -0.0574 -0.0426 119 HIS   B CE1 
5556 N  NE2 . HIS   B 119 ? 0.1986 0.2077 0.1994 0.0322  -0.0513 -0.0345 119 HIS   B NE2 
5564 N  N   . GLU   B 120 ? 0.1714 0.1363 0.1731 -0.0113 -0.0404 0.0170  120 GLU   B N   
5565 C  CA  . GLU   B 120 ? 0.1986 0.1504 0.1757 -0.0050 -0.0490 0.0309  120 GLU   B CA  
5566 C  C   . GLU   B 120 ? 0.1773 0.1417 0.1724 -0.0119 -0.0403 0.0295  120 GLU   B C   
5567 O  O   . GLU   B 120 ? 0.1683 0.1512 0.1870 -0.0152 -0.0381 0.0158  120 GLU   B O   
5568 C  CB  . GLU   B 120 ? 0.2611 0.1793 0.2350 0.0114  -0.0751 0.0521  120 GLU   B CB  
5569 C  CG  . GLU   B 120 ? 0.3157 0.2467 0.3352 0.0231  -0.0999 0.0706  120 GLU   B CG  
5570 C  CD  . GLU   B 120 ? 0.3606 0.3221 0.4388 0.0234  -0.1056 0.0803  120 GLU   B CD  
5571 O  OE1 . GLU   B 120 ? 0.3852 0.3455 0.4786 0.0162  -0.0977 0.0917  120 GLU   B OE1 
5572 O  OE2 . GLU   B 120 ? 0.3797 0.3572 0.4958 0.0237  -0.1049 0.0704  120 GLU   B OE2 
5579 N  N   . VAL   B 121 ? 0.1673 0.1338 0.1730 -0.0215 -0.0299 0.0218  121 VAL   B N   
5580 C  CA  . VAL   B 121 ? 0.1641 0.1443 0.1547 -0.0234 -0.0256 0.0162  121 VAL   B CA  
5581 C  C   . VAL   B 121 ? 0.1565 0.1391 0.1484 -0.0303 -0.0180 0.0142  121 VAL   B C   
5582 O  O   . VAL   B 121 ? 0.1679 0.1365 0.1711 -0.0317 -0.0247 0.0096  121 VAL   B O   
5583 C  CB  . VAL   B 121 ? 0.1880 0.1876 0.1657 -0.0092 -0.0231 0.0233  121 VAL   B CB  
5584 C  CG1 . VAL   B 121 ? 0.1923 0.1997 0.1932 -0.0119 -0.0115 0.0221  121 VAL   B CG1 
5585 C  CG2 . VAL   B 121 ? 0.2091 0.2141 0.1662 -0.0008 -0.0199 0.0125  121 VAL   B CG2 
5595 N  N   . LEU   B 122 ? 0.1469 0.1333 0.1470 -0.0257 -0.0270 0.0093  122 LEU   B N   
5596 C  CA  . LEU   B 122 ? 0.1411 0.1378 0.1381 -0.0229 -0.0164 0.0074  122 LEU   B CA  
5597 C  C   . LEU   B 122 ? 0.1407 0.1295 0.1425 -0.0324 -0.0136 0.0054  122 LEU   B C   
5598 O  O   . LEU   B 122 ? 0.1509 0.1328 0.1746 -0.0316 -0.0192 0.0046  122 LEU   B O   
5599 C  CB  . LEU   B 122 ? 0.1629 0.1508 0.1708 -0.0029 -0.0302 0.0114  122 LEU   B CB  
5600 C  CG  . LEU   B 122 ? 0.1512 0.1572 0.1834 -0.0130 -0.0137 0.0115  122 LEU   B CG  
5601 C  CD1 . LEU   B 122 ? 0.1514 0.1762 0.1792 -0.0234 -0.0239 0.0051  122 LEU   B CD1 
5602 C  CD2 . LEU   B 122 ? 0.1532 0.1602 0.1597 -0.0125 -0.0128 0.0018  122 LEU   B CD2 
5614 N  N   . LEU   B 123 ? 0.1426 0.1180 0.1442 -0.0247 -0.0130 0.0054  123 LEU   B N   
5615 C  CA  . LEU   B 123 ? 0.1446 0.1184 0.1442 -0.0223 -0.0203 -0.0067 123 LEU   B CA  
5616 C  C   . LEU   B 123 ? 0.1412 0.1218 0.1368 -0.0240 -0.0171 -0.0060 123 LEU   B C   
5617 O  O   . LEU   B 123 ? 0.1493 0.1209 0.1408 -0.0283 -0.0152 0.0001  123 LEU   B O   
5618 C  CB  . LEU   B 123 ? 0.1496 0.1263 0.1516 -0.0227 -0.0151 -0.0056 123 LEU   B CB  
5619 C  CG  . LEU   B 123 ? 0.1473 0.1311 0.1697 -0.0200 -0.0073 0.0049  123 LEU   B CG  
5620 C  CD1 . LEU   B 123 ? 0.1590 0.1366 0.1804 -0.0229 -0.0028 -0.0107 123 LEU   B CD1 
5621 C  CD2 . LEU   B 123 ? 0.1558 0.1385 0.1781 -0.0167 0.0008  0.0157  123 LEU   B CD2 
5633 N  N   . ALA   B 124 ? 0.1384 0.1177 0.1362 -0.0188 -0.0038 -0.0011 124 ALA   B N   
5634 C  CA  . ALA   B 124 ? 0.1298 0.1155 0.1521 -0.0140 -0.0076 -0.0078 124 ALA   B CA  
5635 C  C   . ALA   B 124 ? 0.1224 0.1204 0.1411 -0.0180 -0.0048 -0.0079 124 ALA   B C   
5636 O  O   . ALA   B 124 ? 0.1353 0.1239 0.1512 -0.0127 -0.0131 0.0023  124 ALA   B O   
5637 C  CB  . ALA   B 124 ? 0.1334 0.1217 0.1564 -0.0013 0.0014  0.0014  124 ALA   B CB  
5643 N  N   . PRO   B 125 ? 0.1369 0.1208 0.1409 -0.0130 -0.0118 0.0080  125 PRO   B N   
5644 C  CA  . PRO   B 125 ? 0.1445 0.1252 0.1609 -0.0159 -0.0149 0.0174  125 PRO   B CA  
5645 C  C   . PRO   B 125 ? 0.1384 0.1185 0.1814 -0.0126 -0.0100 0.0080  125 PRO   B C   
5646 O  O   . PRO   B 125 ? 0.1408 0.1137 0.1988 -0.0086 -0.0012 0.0154  125 PRO   B O   
5647 C  CB  . PRO   B 125 ? 0.1475 0.1480 0.1610 -0.0185 -0.0208 0.0339  125 PRO   B CB  
5648 C  CG  . PRO   B 125 ? 0.1526 0.1496 0.1551 -0.0253 -0.0230 0.0202  125 PRO   B CG  
5649 C  CD  . PRO   B 125 ? 0.1499 0.1327 0.1440 -0.0293 -0.0096 0.0017  125 PRO   B CD  
5657 N  N   . LEU   B 126 ? 0.1412 0.1137 0.1944 -0.0114 0.0085  0.0104  126 LEU   B N   
5658 C  CA  . LEU   B 126 ? 0.1489 0.1246 0.1941 -0.0128 0.0208  0.0163  126 LEU   B CA  
5659 C  C   . LEU   B 126 ? 0.1437 0.1355 0.1980 0.0016  0.0241  0.0243  126 LEU   B C   
5660 O  O   . LEU   B 126 ? 0.1632 0.1628 0.2227 0.0175  -0.0065 0.0022  126 LEU   B O   
5661 C  CB  . LEU   B 126 ? 0.1690 0.1304 0.2270 -0.0177 0.0232  0.0170  126 LEU   B CB  
5662 C  CG  . LEU   B 126 ? 0.1805 0.1339 0.2304 -0.0245 0.0193  -0.0007 126 LEU   B CG  
5663 C  CD1 . LEU   B 126 ? 0.1944 0.1407 0.2828 -0.0263 0.0064  -0.0219 126 LEU   B CD1 
5664 C  CD2 . LEU   B 126 ? 0.1751 0.1486 0.2222 -0.0294 0.0109  -0.0059 126 LEU   B CD2 
5676 N  N   . LEU   B 127 ? 0.1409 0.1238 0.2093 0.0023  0.0253  0.0163  127 LEU   B N   
5677 C  CA  . LEU   B 127 ? 0.1404 0.1317 0.2189 -0.0006 0.0265  0.0294  127 LEU   B CA  
5678 C  C   . LEU   B 127 ? 0.1346 0.1282 0.2198 0.0044  0.0182  0.0264  127 LEU   B C   
5679 O  O   . LEU   B 127 ? 0.1409 0.1323 0.2186 -0.0086 0.0096  0.0181  127 LEU   B O   
5680 C  CB  . LEU   B 127 ? 0.1572 0.1284 0.2315 -0.0002 0.0222  0.0252  127 LEU   B CB  
5681 C  CG  . LEU   B 127 ? 0.1644 0.1271 0.2367 0.0036  0.0240  0.0206  127 LEU   B CG  
5682 C  CD1 . LEU   B 127 ? 0.1717 0.1233 0.2387 0.0085  0.0221  0.0145  127 LEU   B CD1 
5683 C  CD2 . LEU   B 127 ? 0.1717 0.1387 0.2580 -0.0119 0.0297  0.0339  127 LEU   B CD2 
5695 N  N   . SER   B 128 ? 0.1382 0.1271 0.2173 0.0013  0.0069  0.0222  128 SER   B N   
5696 C  CA  . SER   B 128 ? 0.1532 0.1342 0.2082 0.0094  -0.0070 0.0261  128 SER   B CA  
5697 C  C   . SER   B 128 ? 0.1706 0.1406 0.2326 0.0117  -0.0256 0.0219  128 SER   B C   
5698 O  O   . SER   B 128 ? 0.1857 0.1416 0.2713 0.0101  -0.0221 0.0333  128 SER   B O   
5699 C  CB  . SER   B 128 ? 0.1653 0.1371 0.2109 0.0041  0.0034  0.0310  128 SER   B CB  
5700 O  OG  . SER   B 128 ? 0.1734 0.1542 0.2152 0.0096  0.0128  0.0346  128 SER   B OG  
5706 N  N   . ALA   B 129 ? 0.1848 0.1454 0.2610 0.0259  -0.0113 0.0098  129 ALA   B N   
5707 C  CA  . ALA   B 129 ? 0.2071 0.1510 0.2717 0.0335  -0.0130 -0.0043 129 ALA   B CA  
5708 C  C   . ALA   B 129 ? 0.1923 0.1433 0.2613 0.0250  0.0010  0.0038  129 ALA   B C   
5709 O  O   . ALA   B 129 ? 0.1789 0.1477 0.2593 0.0212  -0.0048 0.0055  129 ALA   B O   
5710 C  CB  . ALA   B 129 ? 0.2310 0.1729 0.3079 0.0394  -0.0001 -0.0108 129 ALA   B CB  
5716 N  N   . GLY   B 130 ? 0.1869 0.1391 0.2667 0.0278  0.0060  -0.0014 130 GLY   B N   
5717 C  CA  . GLY   B 130 ? 0.1839 0.1512 0.2675 0.0248  0.0295  -0.0011 130 GLY   B CA  
5718 C  C   . GLY   B 130 ? 0.1856 0.1577 0.2562 0.0204  0.0191  0.0089  130 GLY   B C   
5719 O  O   . GLY   B 130 ? 0.2039 0.1704 0.2569 0.0192  0.0196  0.0193  130 GLY   B O   
5723 N  N   . ILE   B 131 ? 0.1826 0.1696 0.2663 0.0305  0.0185  0.0017  131 ILE   B N   
5724 C  CA  . ILE   B 131 ? 0.2032 0.1816 0.2669 0.0296  0.0068  0.0114  131 ILE   B CA  
5725 C  C   . ILE   B 131 ? 0.2186 0.1713 0.2354 0.0214  0.0063  0.0182  131 ILE   B C   
5726 O  O   . ILE   B 131 ? 0.2483 0.1881 0.2536 0.0217  -0.0148 0.0158  131 ILE   B O   
5727 C  CB  . ILE   B 131 ? 0.1999 0.2179 0.3073 0.0290  -0.0077 0.0240  131 ILE   B CB  
5728 C  CG1 . ILE   B 131 ? 0.2010 0.2461 0.3159 0.0005  0.0023  0.0277  131 ILE   B CG1 
5729 C  CG2 . ILE   B 131 ? 0.2030 0.2324 0.3328 0.0341  -0.0083 0.0215  131 ILE   B CG2 
5730 C  CD1 . ILE   B 131 ? 0.2012 0.2659 0.3232 -0.0208 0.0002  0.0371  131 ILE   B CD1 
5742 N  N   . PHE   B 132 ? 0.2009 0.1559 0.2278 0.0167  0.0217  0.0193  132 PHE   B N   
5743 C  CA  . PHE   B 132 ? 0.2102 0.1551 0.2285 0.0108  0.0368  0.0135  132 PHE   B CA  
5744 C  C   . PHE   B 132 ? 0.2296 0.1723 0.2436 0.0081  0.0481  0.0156  132 PHE   B C   
5745 O  O   . PHE   B 132 ? 0.2474 0.1964 0.2623 0.0032  0.0625  0.0164  132 PHE   B O   
5746 C  CB  . PHE   B 132 ? 0.1965 0.1528 0.2167 0.0142  0.0343  0.0233  132 PHE   B CB  
5747 C  CG  . PHE   B 132 ? 0.1925 0.1570 0.2140 0.0182  0.0274  0.0272  132 PHE   B CG  
5748 C  CD1 . PHE   B 132 ? 0.1994 0.1578 0.2475 0.0133  0.0269  0.0230  132 PHE   B CD1 
5749 C  CD2 . PHE   B 132 ? 0.1903 0.1587 0.1935 0.0258  0.0206  0.0346  132 PHE   B CD2 
5750 C  CE1 . PHE   B 132 ? 0.2041 0.1585 0.2537 0.0039  0.0207  0.0243  132 PHE   B CE1 
5751 C  CE2 . PHE   B 132 ? 0.1953 0.1652 0.2027 0.0171  0.0122  0.0296  132 PHE   B CE2 
5752 C  CZ  . PHE   B 132 ? 0.2008 0.1618 0.2349 0.0056  0.0016  0.0309  132 PHE   B CZ  
5762 N  N   . GLY   B 133 ? 0.2265 0.1663 0.2474 0.0033  0.0336  0.0334  133 GLY   B N   
5763 C  CA  . GLY   B 133 ? 0.2346 0.1786 0.2488 -0.0200 0.0322  0.0438  133 GLY   B CA  
5764 C  C   . GLY   B 133 ? 0.2397 0.1886 0.2435 -0.0326 0.0358  0.0495  133 GLY   B C   
5765 O  O   . GLY   B 133 ? 0.2584 0.2037 0.2932 -0.0461 0.0331  0.0612  133 GLY   B O   
5769 N  N   . ALA   B 134 ? 0.2196 0.1849 0.2286 -0.0276 0.0297  0.0283  134 ALA   B N   
5770 C  CA  . ALA   B 134 ? 0.2156 0.1818 0.2432 -0.0184 0.0383  0.0142  134 ALA   B CA  
5771 C  C   . ALA   B 134 ? 0.2233 0.1711 0.2511 -0.0111 0.0383  0.0252  134 ALA   B C   
5772 O  O   . ALA   B 134 ? 0.2269 0.1829 0.2728 -0.0010 0.0329  0.0212  134 ALA   B O   
5773 C  CB  . ALA   B 134 ? 0.2100 0.1857 0.2624 -0.0089 0.0342  0.0111  134 ALA   B CB  
5779 N  N   . ASP   B 135 ? 0.2367 0.1645 0.2506 -0.0152 0.0243  0.0281  135 ASP   B N   
5780 C  CA  . ASP   B 135 ? 0.2518 0.1569 0.2746 -0.0140 0.0102  0.0331  135 ASP   B CA  
5781 C  C   . ASP   B 135 ? 0.2335 0.1449 0.2602 -0.0023 0.0086  0.0290  135 ASP   B C   
5782 O  O   . ASP   B 135 ? 0.2279 0.1355 0.2716 -0.0031 0.0037  0.0323  135 ASP   B O   
5783 C  CB  . ASP   B 135 ? 0.2844 0.1697 0.3052 -0.0365 0.0083  0.0337  135 ASP   B CB  
5784 C  CG  . ASP   B 135 ? 0.3166 0.1731 0.3537 -0.0562 0.0050  0.0320  135 ASP   B CG  
5785 O  OD1 . ASP   B 135 ? 0.3210 0.1580 0.3452 -0.0392 -0.0011 0.0320  135 ASP   B OD1 
5786 O  OD2 . ASP   B 135 ? 0.3429 0.2083 0.4059 -0.0733 -0.0016 0.0147  135 ASP   B OD2 
5791 N  N   . PRO   B 136 ? 0.2233 0.1491 0.2745 0.0174  -0.0051 0.0255  136 PRO   B N   
5792 C  CA  . PRO   B 136 ? 0.1998 0.1397 0.2755 0.0150  -0.0050 0.0136  136 PRO   B CA  
5793 C  C   . PRO   B 136 ? 0.1797 0.1276 0.2917 0.0097  -0.0007 0.0108  136 PRO   B C   
5794 O  O   . PRO   B 136 ? 0.1581 0.1246 0.2875 0.0030  0.0012  0.0159  136 PRO   B O   
5795 C  CB  . PRO   B 136 ? 0.2059 0.1645 0.2829 0.0304  -0.0092 0.0073  136 PRO   B CB  
5796 C  CG  . PRO   B 136 ? 0.2273 0.1751 0.3081 0.0315  -0.0030 0.0057  136 PRO   B CG  
5797 C  CD  . PRO   B 136 ? 0.2313 0.1640 0.2863 0.0375  -0.0013 0.0167  136 PRO   B CD  
5805 N  N   . ILE   B 137 ? 0.1867 0.1236 0.3058 0.0124  -0.0030 0.0080  137 ILE   B N   
5806 C  CA  . ILE   B 137 ? 0.1954 0.1236 0.3067 -0.0003 0.0043  0.0111  137 ILE   B CA  
5807 C  C   . ILE   B 137 ? 0.1874 0.1272 0.2879 -0.0076 0.0129  0.0211  137 ILE   B C   
5808 O  O   . ILE   B 137 ? 0.1761 0.1305 0.2751 -0.0111 0.0077  0.0154  137 ILE   B O   
5809 C  CB  . ILE   B 137 ? 0.2226 0.1327 0.3598 -0.0059 0.0102  0.0132  137 ILE   B CB  
5810 C  CG1 . ILE   B 137 ? 0.2498 0.1445 0.4155 0.0028  0.0154  -0.0041 137 ILE   B CG1 
5811 C  CG2 . ILE   B 137 ? 0.2302 0.1359 0.3635 -0.0249 0.0153  0.0148  137 ILE   B CG2 
5812 C  CD1 . ILE   B 137 ? 0.2724 0.1724 0.4626 0.0114  0.0122  -0.0009 137 ILE   B CD1 
5824 N  N   . HIS   B 138 ? 0.1903 0.1249 0.2893 -0.0066 0.0184  0.0170  138 HIS   B N   
5825 C  CA  . HIS   B 138 ? 0.1971 0.1359 0.2803 -0.0042 0.0352  0.0132  138 HIS   B CA  
5826 C  C   . HIS   B 138 ? 0.1807 0.1319 0.2702 -0.0025 0.0265  0.0258  138 HIS   B C   
5827 O  O   . HIS   B 138 ? 0.1721 0.1432 0.2875 0.0019  0.0354  0.0401  138 HIS   B O   
5828 C  CB  . HIS   B 138 ? 0.2233 0.1497 0.2915 -0.0083 0.0523  0.0102  138 HIS   B CB  
5829 C  CG  . HIS   B 138 ? 0.2478 0.1700 0.2917 -0.0101 0.0708  0.0319  138 HIS   B CG  
5830 N  ND1 . HIS   B 138 ? 0.2576 0.1859 0.3140 -0.0057 0.0768  0.0206  138 HIS   B ND1 
5831 C  CD2 . HIS   B 138 ? 0.2674 0.1805 0.2844 -0.0095 0.0796  0.0258  138 HIS   B CD2 
5832 C  CE1 . HIS   B 138 ? 0.2686 0.1896 0.3124 -0.0051 0.0862  0.0196  138 HIS   B CE1 
5833 N  NE2 . HIS   B 138 ? 0.2761 0.1755 0.2883 -0.0042 0.0892  0.0127  138 HIS   B NE2 
5841 N  N   . SER   B 139 ? 0.1807 0.1242 0.2683 0.0022  0.0187  0.0156  139 SER   B N   
5842 C  CA  . SER   B 139 ? 0.1755 0.1150 0.2634 -0.0008 0.0213  0.0071  139 SER   B CA  
5843 C  C   . SER   B 139 ? 0.1494 0.1098 0.2560 -0.0043 0.0168  0.0056  139 SER   B C   
5844 O  O   . SER   B 139 ? 0.1501 0.1126 0.2619 -0.0012 0.0049  0.0092  139 SER   B O   
5845 C  CB  . SER   B 139 ? 0.1817 0.1182 0.2672 0.0013  0.0042  0.0094  139 SER   B CB  
5846 O  OG  . SER   B 139 ? 0.1847 0.1204 0.2681 -0.0031 -0.0037 0.0215  139 SER   B OG  
5852 N  N   . LEU   B 140 ? 0.1504 0.1065 0.2565 -0.0037 0.0245  0.0066  140 LEU   B N   
5853 C  CA  . LEU   B 140 ? 0.1455 0.1108 0.2572 -0.0035 0.0189  0.0099  140 LEU   B CA  
5854 C  C   . LEU   B 140 ? 0.1406 0.1147 0.2619 -0.0068 0.0028  0.0035  140 LEU   B C   
5855 O  O   . LEU   B 140 ? 0.1410 0.1253 0.2492 -0.0072 -0.0017 0.0086  140 LEU   B O   
5856 C  CB  . LEU   B 140 ? 0.1465 0.1074 0.2533 -0.0100 0.0183  -0.0005 140 LEU   B CB  
5857 C  CG  . LEU   B 140 ? 0.1562 0.1154 0.2475 -0.0100 0.0093  0.0113  140 LEU   B CG  
5858 C  CD1 . LEU   B 140 ? 0.1648 0.1256 0.2715 -0.0135 0.0111  0.0114  140 LEU   B CD1 
5859 C  CD2 . LEU   B 140 ? 0.1745 0.1262 0.2592 -0.0111 0.0020  -0.0011 140 LEU   B CD2 
5871 N  N   . ARG   B 141 ? 0.1352 0.1167 0.2739 -0.0073 0.0100  -0.0021 141 ARG   B N   
5872 C  CA  . ARG   B 141 ? 0.1397 0.1172 0.3010 -0.0152 0.0258  -0.0037 141 ARG   B CA  
5873 C  C   . ARG   B 141 ? 0.1343 0.1226 0.2901 -0.0123 0.0138  -0.0027 141 ARG   B C   
5874 O  O   . ARG   B 141 ? 0.1414 0.1244 0.2813 -0.0154 0.0028  -0.0105 141 ARG   B O   
5875 C  CB  . ARG   B 141 ? 0.1562 0.1265 0.3243 -0.0178 0.0328  -0.0077 141 ARG   B CB  
5876 C  CG  . ARG   B 141 ? 0.1878 0.1599 0.3460 -0.0200 0.0306  -0.0046 141 ARG   B CG  
5877 C  CD  . ARG   B 141 ? 0.2283 0.1826 0.3511 -0.0190 0.0147  -0.0114 141 ARG   B CD  
5878 N  NE  . ARG   B 141 ? 0.2548 0.1794 0.3458 -0.0295 0.0231  -0.0165 141 ARG   B NE  
5879 C  CZ  . ARG   B 141 ? 0.2741 0.1638 0.3251 -0.0221 0.0321  -0.0245 141 ARG   B CZ  
5880 N  NH1 . ARG   B 141 ? 0.2843 0.1554 0.3157 -0.0239 0.0295  -0.0299 141 ARG   B NH1 
5881 N  NH2 . ARG   B 141 ? 0.2887 0.1683 0.3314 -0.0099 0.0213  -0.0181 141 ARG   B NH2 
5895 N  N   . VAL   B 142 ? 0.1407 0.1177 0.2773 -0.0097 0.0147  -0.0024 142 VAL   B N   
5896 C  CA  . VAL   B 142 ? 0.1366 0.1159 0.2676 -0.0058 0.0149  0.0006  142 VAL   B CA  
5897 C  C   . VAL   B 142 ? 0.1322 0.1133 0.2650 -0.0038 0.0098  -0.0059 142 VAL   B C   
5898 O  O   . VAL   B 142 ? 0.1425 0.1144 0.2811 0.0018  0.0129  -0.0021 142 VAL   B O   
5899 C  CB  . VAL   B 142 ? 0.1498 0.1279 0.2698 0.0000  0.0167  0.0120  142 VAL   B CB  
5900 C  CG1 . VAL   B 142 ? 0.1437 0.1298 0.2694 0.0087  0.0278  0.0057  142 VAL   B CG1 
5901 C  CG2 . VAL   B 142 ? 0.1713 0.1312 0.2766 0.0050  0.0146  0.0156  142 VAL   B CG2 
5911 N  N   . CYS   B 143 ? 0.1292 0.1145 0.2571 -0.0014 0.0085  0.0049  143 CYS   B N   
5912 C  CA  . CYS   B 143 ? 0.1252 0.1182 0.2593 -0.0059 0.0032  0.0054  143 CYS   B CA  
5913 C  C   . CYS   B 143 ? 0.1247 0.1182 0.2575 -0.0086 0.0097  -0.0025 143 CYS   B C   
5914 O  O   . CYS   B 143 ? 0.1296 0.1221 0.2479 -0.0068 0.0020  0.0011  143 CYS   B O   
5915 C  CB  . CYS   B 143 ? 0.1351 0.1252 0.2587 -0.0077 0.0035  0.0016  143 CYS   B CB  
5916 S  SG  . CYS   B 143 ? 0.1371 0.1395 0.2513 -0.0061 0.0059  0.0074  143 CYS   B SG  
5922 N  N   . VAL   B 144 ? 0.1312 0.1186 0.2696 -0.0095 0.0095  -0.0149 144 VAL   B N   
5923 C  CA  . VAL   B 144 ? 0.1381 0.1272 0.2902 -0.0170 -0.0087 -0.0245 144 VAL   B CA  
5924 C  C   . VAL   B 144 ? 0.1320 0.1303 0.2952 -0.0153 -0.0107 -0.0044 144 VAL   B C   
5925 O  O   . VAL   B 144 ? 0.1444 0.1520 0.3155 -0.0051 -0.0091 0.0191  144 VAL   B O   
5926 C  CB  . VAL   B 144 ? 0.1677 0.1462 0.3386 -0.0139 -0.0185 -0.0389 144 VAL   B CB  
5927 C  CG1 . VAL   B 144 ? 0.1968 0.1829 0.3703 -0.0129 -0.0234 -0.0337 144 VAL   B CG1 
5928 C  CG2 . VAL   B 144 ? 0.1781 0.1478 0.3361 0.0010  -0.0348 -0.0466 144 VAL   B CG2 
5938 N  N   . ASP   B 145 ? 0.1333 0.1242 0.3081 -0.0085 -0.0047 -0.0091 145 ASP   B N   
5939 C  CA  . ASP   B 145 ? 0.1310 0.1275 0.3260 -0.0067 0.0009  -0.0101 145 ASP   B CA  
5940 C  C   . ASP   B 145 ? 0.1301 0.1343 0.3107 -0.0096 0.0019  -0.0070 145 ASP   B C   
5941 O  O   . ASP   B 145 ? 0.1325 0.1454 0.3694 -0.0133 0.0047  -0.0253 145 ASP   B O   
5942 C  CB  . ASP   B 145 ? 0.1513 0.1378 0.3762 -0.0161 0.0167  -0.0058 145 ASP   B CB  
5943 C  CG  . ASP   B 145 ? 0.1654 0.1417 0.4331 -0.0270 0.0273  0.0026  145 ASP   B CG  
5944 O  OD1 . ASP   B 145 ? 0.1648 0.1451 0.4365 -0.0264 -0.0070 -0.0088 145 ASP   B OD1 
5945 O  OD2 . ASP   B 145 ? 0.1918 0.1488 0.4767 -0.0315 0.0510  0.0168  145 ASP   B OD2 
5950 N  N   . THR   B 146 ? 0.1248 0.1234 0.2521 -0.0076 -0.0006 -0.0024 146 THR   B N   
5951 C  CA  . THR   B 146 ? 0.1382 0.1224 0.2345 -0.0063 0.0061  0.0003  146 THR   B CA  
5952 C  C   . THR   B 146 ? 0.1352 0.1197 0.2277 -0.0055 -0.0021 0.0063  146 THR   B C   
5953 O  O   . THR   B 146 ? 0.1390 0.1225 0.2321 -0.0042 -0.0008 0.0012  146 THR   B O   
5954 C  CB  . THR   B 146 ? 0.1374 0.1182 0.2406 -0.0022 0.0210  0.0054  146 THR   B CB  
5955 O  OG1 . THR   B 146 ? 0.1396 0.1220 0.2472 -0.0049 0.0142  0.0107  146 THR   B OG1 
5956 C  CG2 . THR   B 146 ? 0.1543 0.1225 0.2376 -0.0052 0.0206  0.0013  146 THR   B CG2 
5964 N  N   . VAL   B 147 ? 0.1392 0.1220 0.2298 -0.0054 0.0095  0.0052  147 VAL   B N   
5965 C  CA  . VAL   B 147 ? 0.1355 0.1189 0.2202 -0.0134 -0.0016 0.0047  147 VAL   B CA  
5966 C  C   . VAL   B 147 ? 0.1300 0.1176 0.2340 -0.0151 -0.0127 -0.0044 147 VAL   B C   
5967 O  O   . VAL   B 147 ? 0.1410 0.1317 0.2453 -0.0208 -0.0304 0.0014  147 VAL   B O   
5968 C  CB  . VAL   B 147 ? 0.1385 0.1291 0.2081 -0.0091 -0.0086 0.0011  147 VAL   B CB  
5969 C  CG1 . VAL   B 147 ? 0.1362 0.1457 0.1966 -0.0156 -0.0041 0.0038  147 VAL   B CG1 
5970 C  CG2 . VAL   B 147 ? 0.1411 0.1257 0.2115 -0.0118 -0.0044 0.0016  147 VAL   B CG2 
5980 N  N   . ARG   B 148 ? 0.1351 0.1216 0.2234 -0.0075 -0.0204 -0.0067 148 ARG   B N   
5981 C  CA  . ARG   B 148 ? 0.1402 0.1331 0.2160 -0.0085 -0.0271 -0.0092 148 ARG   B CA  
5982 C  C   . ARG   B 148 ? 0.1459 0.1425 0.1961 -0.0101 -0.0244 -0.0078 148 ARG   B C   
5983 O  O   . ARG   B 148 ? 0.1654 0.1722 0.1976 -0.0269 -0.0305 -0.0019 148 ARG   B O   
5984 C  CB  . ARG   B 148 ? 0.1403 0.1442 0.2236 -0.0044 -0.0296 -0.0173 148 ARG   B CB  
5985 C  CG  . ARG   B 148 ? 0.1394 0.1556 0.2365 -0.0066 -0.0329 -0.0391 148 ARG   B CG  
5986 C  CD  . ARG   B 148 ? 0.1486 0.1700 0.2525 0.0053  -0.0309 -0.0363 148 ARG   B CD  
5987 N  NE  . ARG   B 148 ? 0.1528 0.1620 0.2370 0.0219  -0.0356 -0.0275 148 ARG   B NE  
5988 C  CZ  . ARG   B 148 ? 0.1478 0.1567 0.2198 0.0170  -0.0290 -0.0217 148 ARG   B CZ  
5989 N  NH1 . ARG   B 148 ? 0.1364 0.1635 0.2340 -0.0037 -0.0057 -0.0198 148 ARG   B NH1 
5990 N  NH2 . ARG   B 148 ? 0.1721 0.1458 0.2116 0.0178  -0.0246 -0.0173 148 ARG   B NH2 
6004 N  N   . THR   B 149 ? 0.1498 0.1343 0.2018 -0.0117 -0.0285 0.0005  149 THR   B N   
6005 C  CA  . THR   B 149 ? 0.1527 0.1354 0.1959 -0.0143 -0.0274 0.0063  149 THR   B CA  
6006 C  C   . THR   B 149 ? 0.1525 0.1312 0.1832 -0.0120 -0.0286 0.0000  149 THR   B C   
6007 O  O   . THR   B 149 ? 0.1591 0.1316 0.2040 -0.0193 -0.0128 0.0060  149 THR   B O   
6008 C  CB  . THR   B 149 ? 0.1561 0.1320 0.2027 -0.0172 -0.0240 -0.0027 149 THR   B CB  
6009 O  OG1 . THR   B 149 ? 0.1591 0.1425 0.1876 -0.0240 -0.0297 0.0004  149 THR   B OG1 
6010 C  CG2 . THR   B 149 ? 0.1589 0.1339 0.2287 -0.0107 -0.0149 0.0003  149 THR   B CG2 
6018 N  N   . ASN   B 150 ? 0.1594 0.1317 0.1825 -0.0176 -0.0323 -0.0041 150 ASN   B N   
6019 C  CA  . ASN   B 150 ? 0.1677 0.1505 0.1743 -0.0213 -0.0293 -0.0043 150 ASN   B CA  
6020 C  C   . ASN   B 150 ? 0.1538 0.1451 0.1756 -0.0170 -0.0283 -0.0011 150 ASN   B C   
6021 O  O   . ASN   B 150 ? 0.1620 0.1415 0.1937 -0.0280 -0.0434 0.0015  150 ASN   B O   
6022 C  CB  . ASN   B 150 ? 0.1910 0.1885 0.1814 -0.0217 -0.0433 0.0086  150 ASN   B CB  
6023 C  CG  . ASN   B 150 ? 0.2160 0.2262 0.2209 -0.0238 -0.0458 0.0246  150 ASN   B CG  
6024 O  OD1 . ASN   B 150 ? 0.2232 0.2427 0.2384 -0.0321 -0.0603 0.0200  150 ASN   B OD1 
6025 N  ND2 . ASN   B 150 ? 0.2273 0.2417 0.2570 -0.0135 -0.0506 0.0606  150 ASN   B ND2 
6032 N  N   . VAL   B 151 ? 0.1439 0.1432 0.1789 -0.0189 -0.0297 0.0059  151 VAL   B N   
6033 C  CA  . VAL   B 151 ? 0.1530 0.1400 0.1909 -0.0248 -0.0222 -0.0005 151 VAL   B CA  
6034 C  C   . VAL   B 151 ? 0.1535 0.1319 0.1796 -0.0330 -0.0306 -0.0041 151 VAL   B C   
6035 O  O   . VAL   B 151 ? 0.1589 0.1434 0.1954 -0.0265 -0.0224 -0.0098 151 VAL   B O   
6036 C  CB  . VAL   B 151 ? 0.1677 0.1502 0.1973 -0.0142 -0.0206 0.0011  151 VAL   B CB  
6037 C  CG1 . VAL   B 151 ? 0.1760 0.1544 0.2264 -0.0179 -0.0125 -0.0079 151 VAL   B CG1 
6038 C  CG2 . VAL   B 151 ? 0.1764 0.1681 0.1855 -0.0046 -0.0163 0.0091  151 VAL   B CG2 
6048 N  N   . TYR   B 152 ? 0.1477 0.1217 0.1723 -0.0249 -0.0240 -0.0063 152 TYR   B N   
6049 C  CA  . TYR   B 152 ? 0.1528 0.1431 0.1649 -0.0312 -0.0145 -0.0048 152 TYR   B CA  
6050 C  C   . TYR   B 152 ? 0.1484 0.1284 0.1523 -0.0215 -0.0121 -0.0130 152 TYR   B C   
6051 O  O   . TYR   B 152 ? 0.1536 0.1322 0.1689 -0.0239 -0.0137 -0.0070 152 TYR   B O   
6052 C  CB  . TYR   B 152 ? 0.1687 0.1572 0.1652 -0.0314 -0.0186 0.0078  152 TYR   B CB  
6053 C  CG  . TYR   B 152 ? 0.1848 0.1701 0.1539 -0.0416 -0.0158 0.0060  152 TYR   B CG  
6054 C  CD1 . TYR   B 152 ? 0.1951 0.1871 0.1517 -0.0329 -0.0257 0.0062  152 TYR   B CD1 
6055 C  CD2 . TYR   B 152 ? 0.2097 0.1894 0.1575 -0.0441 -0.0160 -0.0050 152 TYR   B CD2 
6056 C  CE1 . TYR   B 152 ? 0.2119 0.2084 0.1608 -0.0315 -0.0319 0.0153  152 TYR   B CE1 
6057 C  CE2 . TYR   B 152 ? 0.2208 0.2110 0.1599 -0.0399 -0.0229 -0.0121 152 TYR   B CE2 
6058 C  CZ  . TYR   B 152 ? 0.2238 0.2269 0.1582 -0.0346 -0.0491 0.0149  152 TYR   B CZ  
6059 O  OH  . TYR   B 152 ? 0.2463 0.2599 0.2080 -0.0258 -0.0519 0.0270  152 TYR   B OH  
6069 N  N   . LEU   B 153 ? 0.1534 0.1226 0.1669 -0.0270 -0.0111 -0.0097 153 LEU   B N   
6070 C  CA  . LEU   B 153 ? 0.1560 0.1185 0.1595 -0.0216 -0.0042 -0.0098 153 LEU   B CA  
6071 C  C   . LEU   B 153 ? 0.1571 0.1181 0.1671 -0.0274 -0.0062 -0.0138 153 LEU   B C   
6072 O  O   . LEU   B 153 ? 0.1628 0.1421 0.1809 -0.0180 -0.0092 -0.0285 153 LEU   B O   
6073 C  CB  . LEU   B 153 ? 0.1552 0.1225 0.1829 -0.0259 -0.0025 -0.0046 153 LEU   B CB  
6074 C  CG  . LEU   B 153 ? 0.1469 0.1346 0.2005 -0.0240 -0.0028 -0.0048 153 LEU   B CG  
6075 C  CD1 . LEU   B 153 ? 0.1560 0.1446 0.2090 -0.0276 0.0024  0.0042  153 LEU   B CD1 
6076 C  CD2 . LEU   B 153 ? 0.1506 0.1453 0.1996 -0.0217 0.0050  0.0064  153 LEU   B CD2 
6088 N  N   . ALA   B 154 ? 0.1504 0.1259 0.1809 -0.0102 -0.0143 -0.0141 154 ALA   B N   
6089 C  CA  . ALA   B 154 ? 0.1584 0.1340 0.2072 -0.0008 -0.0175 -0.0194 154 ALA   B CA  
6090 C  C   . ALA   B 154 ? 0.1693 0.1341 0.2123 0.0018  -0.0311 -0.0249 154 ALA   B C   
6091 O  O   . ALA   B 154 ? 0.2028 0.1390 0.2309 0.0056  -0.0126 -0.0099 154 ALA   B O   
6092 C  CB  . ALA   B 154 ? 0.1552 0.1517 0.2287 -0.0003 -0.0205 -0.0324 154 ALA   B CB  
6098 N  N   . VAL   B 155 ? 0.1411 0.1286 0.2276 -0.0027 -0.0056 -0.0189 155 VAL   B N   
6099 C  CA  . VAL   B 155 ? 0.1337 0.1312 0.2369 -0.0028 -0.0086 -0.0113 155 VAL   B CA  
6100 C  C   . VAL   B 155 ? 0.1384 0.1301 0.2322 -0.0069 -0.0100 -0.0246 155 VAL   B C   
6101 O  O   . VAL   B 155 ? 0.1513 0.1484 0.2693 -0.0002 -0.0088 -0.0432 155 VAL   B O   
6102 C  CB  . VAL   B 155 ? 0.1380 0.1421 0.2744 -0.0073 -0.0152 -0.0004 155 VAL   B CB  
6103 C  CG1 . VAL   B 155 ? 0.1454 0.1400 0.2708 -0.0114 -0.0133 0.0026  155 VAL   B CG1 
6104 C  CG2 . VAL   B 155 ? 0.1335 0.1534 0.3026 -0.0103 -0.0097 0.0244  155 VAL   B CG2 
6114 N  N   . PHE   B 156 ? 0.1287 0.1401 0.2426 0.0012  0.0007  -0.0212 156 PHE   B N   
6115 C  CA  . PHE   B 156 ? 0.1344 0.1469 0.2854 0.0046  -0.0024 -0.0247 156 PHE   B CA  
6116 C  C   . PHE   B 156 ? 0.1362 0.1582 0.3073 0.0115  -0.0071 -0.0399 156 PHE   B C   
6117 O  O   . PHE   B 156 ? 0.1548 0.1775 0.3285 0.0206  0.0000  -0.0490 156 PHE   B O   
6118 C  CB  . PHE   B 156 ? 0.1416 0.1429 0.2801 0.0027  -0.0069 -0.0106 156 PHE   B CB  
6119 C  CG  . PHE   B 156 ? 0.1410 0.1550 0.2889 0.0043  -0.0069 0.0086  156 PHE   B CG  
6120 C  CD1 . PHE   B 156 ? 0.1454 0.1760 0.3166 0.0054  0.0003  0.0360  156 PHE   B CD1 
6121 C  CD2 . PHE   B 156 ? 0.1490 0.1655 0.2913 0.0105  -0.0199 0.0104  156 PHE   B CD2 
6122 C  CE1 . PHE   B 156 ? 0.1513 0.1907 0.3285 0.0060  -0.0005 0.0356  156 PHE   B CE1 
6123 C  CE2 . PHE   B 156 ? 0.1523 0.1857 0.3012 0.0133  -0.0194 0.0112  156 PHE   B CE2 
6124 C  CZ  . PHE   B 156 ? 0.1465 0.1902 0.3255 0.0141  -0.0167 0.0204  156 PHE   B CZ  
6134 N  N   . ASP   B 157 ? 0.1384 0.1442 0.3249 0.0136  -0.0178 -0.0209 157 ASP   B N   
6135 C  CA  . ASP   B 157 ? 0.1466 0.1513 0.3607 0.0082  -0.0202 -0.0270 157 ASP   B CA  
6136 C  C   . ASP   B 157 ? 0.1469 0.1513 0.3673 0.0052  -0.0152 -0.0453 157 ASP   B C   
6137 O  O   . ASP   B 157 ? 0.1356 0.1508 0.3591 0.0006  -0.0112 -0.0302 157 ASP   B O   
6138 C  CB  . ASP   B 157 ? 0.1702 0.1806 0.3737 0.0079  -0.0460 -0.0112 157 ASP   B CB  
6139 C  CG  . ASP   B 157 ? 0.2056 0.1956 0.3928 0.0013  -0.0308 -0.0142 157 ASP   B CG  
6140 O  OD1 . ASP   B 157 ? 0.2140 0.1886 0.4071 0.0047  -0.0134 -0.0127 157 ASP   B OD1 
6141 O  OD2 . ASP   B 157 ? 0.2361 0.2139 0.4192 -0.0021 -0.0196 -0.0104 157 ASP   B OD2 
6146 N  N   . LYS   B 158 ? 0.1545 0.1795 0.3769 0.0057  -0.0021 -0.0761 158 LYS   B N   
6147 C  CA  . LYS   B 158 ? 0.1710 0.1986 0.3872 0.0056  0.0066  -0.0975 158 LYS   B CA  
6148 C  C   . LYS   B 158 ? 0.1718 0.1813 0.3991 0.0017  -0.0006 -0.0871 158 LYS   B C   
6149 O  O   . LYS   B 158 ? 0.1758 0.1769 0.4008 -0.0109 -0.0008 -0.0981 158 LYS   B O   
6150 C  CB  . LYS   B 158 ? 0.1992 0.2443 0.3897 0.0110  0.0130  -0.1161 158 LYS   B CB  
6151 C  CG  . LYS   B 158 ? 0.2332 0.2885 0.3999 0.0118  0.0179  -0.1260 158 LYS   B CG  
6152 C  CD  . LYS   B 158 ? 0.2559 0.3410 0.4121 0.0097  0.0253  -0.1251 158 LYS   B CD  
6153 C  CE  . LYS   B 158 ? 0.2727 0.3755 0.4295 0.0105  0.0234  -0.1209 158 LYS   B CE  
6154 N  NZ  . LYS   B 158 ? 0.2725 0.3978 0.4282 0.0077  0.0215  -0.1195 158 LYS   B NZ  
6168 N  N   . ASN   B 159 ? 0.1717 0.1699 0.4197 0.0049  -0.0173 -0.0658 159 ASN   B N   
6169 C  CA  . ASN   B 159 ? 0.1812 0.1703 0.4422 0.0159  -0.0327 -0.0537 159 ASN   B CA  
6170 C  C   . ASN   B 159 ? 0.1617 0.1545 0.4274 0.0142  -0.0491 -0.0492 159 ASN   B C   
6171 O  O   . ASN   B 159 ? 0.1660 0.1428 0.4541 0.0014  -0.0504 -0.0348 159 ASN   B O   
6172 C  CB  . ASN   B 159 ? 0.2052 0.1865 0.4774 0.0253  -0.0355 -0.0502 159 ASN   B CB  
6173 C  CG  . ASN   B 159 ? 0.2286 0.2026 0.5117 0.0265  -0.0491 -0.0634 159 ASN   B CG  
6174 O  OD1 . ASN   B 159 ? 0.2424 0.2109 0.5144 0.0343  -0.0526 -0.0681 159 ASN   B OD1 
6175 N  ND2 . ASN   B 159 ? 0.2322 0.2094 0.5266 0.0302  -0.0542 -0.0623 159 ASN   B ND2 
6182 N  N   . LEU   B 160 ? 0.1572 0.1524 0.3973 0.0129  -0.0486 -0.0440 160 LEU   B N   
6183 C  CA  . LEU   B 160 ? 0.1578 0.1492 0.3616 0.0104  -0.0388 -0.0300 160 LEU   B CA  
6184 C  C   . LEU   B 160 ? 0.1496 0.1373 0.3539 0.0021  -0.0296 -0.0320 160 LEU   B C   
6185 O  O   . LEU   B 160 ? 0.1375 0.1396 0.3520 -0.0042 -0.0275 -0.0201 160 LEU   B O   
6186 C  CB  . LEU   B 160 ? 0.1549 0.1559 0.3439 0.0022  -0.0394 -0.0156 160 LEU   B CB  
6187 C  CG  . LEU   B 160 ? 0.1528 0.1700 0.3266 0.0047  -0.0287 -0.0004 160 LEU   B CG  
6188 C  CD1 . LEU   B 160 ? 0.1638 0.1874 0.3212 -0.0071 -0.0092 -0.0034 160 LEU   B CD1 
6189 C  CD2 . LEU   B 160 ? 0.1599 0.1697 0.3197 0.0232  -0.0283 -0.0048 160 LEU   B CD2 
6201 N  N   . TYR   B 161 ? 0.1514 0.1414 0.3608 -0.0033 -0.0037 -0.0399 161 TYR   B N   
6202 C  CA  . TYR   B 161 ? 0.1574 0.1430 0.3362 -0.0138 0.0166  -0.0471 161 TYR   B CA  
6203 C  C   . TYR   B 161 ? 0.1586 0.1436 0.3232 -0.0109 0.0221  -0.0431 161 TYR   B C   
6204 O  O   . TYR   B 161 ? 0.1588 0.1434 0.3187 -0.0241 0.0124  -0.0350 161 TYR   B O   
6205 C  CB  . TYR   B 161 ? 0.1742 0.1524 0.3317 -0.0244 0.0347  -0.0507 161 TYR   B CB  
6206 C  CG  . TYR   B 161 ? 0.1985 0.1588 0.3233 -0.0279 0.0415  -0.0554 161 TYR   B CG  
6207 C  CD1 . TYR   B 161 ? 0.2041 0.1551 0.3198 -0.0431 0.0444  -0.0530 161 TYR   B CD1 
6208 C  CD2 . TYR   B 161 ? 0.2217 0.1672 0.3169 -0.0229 0.0288  -0.0601 161 TYR   B CD2 
6209 C  CE1 . TYR   B 161 ? 0.2242 0.1773 0.3257 -0.0423 0.0415  -0.0544 161 TYR   B CE1 
6210 C  CE2 . TYR   B 161 ? 0.2438 0.1835 0.3253 -0.0293 0.0312  -0.0604 161 TYR   B CE2 
6211 C  CZ  . TYR   B 161 ? 0.2426 0.1888 0.3199 -0.0447 0.0273  -0.0528 161 TYR   B CZ  
6212 O  OH  . TYR   B 161 ? 0.2702 0.2190 0.3394 -0.0489 0.0231  -0.0469 161 TYR   B OH  
6222 N  N   . ASP   B 162 ? 0.1644 0.1416 0.3453 -0.0080 0.0057  -0.0553 162 ASP   B N   
6223 C  CA  . ASP   B 162 ? 0.1735 0.1495 0.3445 -0.0099 -0.0021 -0.0535 162 ASP   B CA  
6224 C  C   . ASP   B 162 ? 0.1689 0.1364 0.3377 -0.0154 -0.0098 -0.0409 162 ASP   B C   
6225 O  O   . ASP   B 162 ? 0.1763 0.1446 0.3375 -0.0193 -0.0255 -0.0329 162 ASP   B O   
6226 C  CB  . ASP   B 162 ? 0.1952 0.1658 0.3632 0.0003  -0.0004 -0.0760 162 ASP   B CB  
6227 C  CG  . ASP   B 162 ? 0.2021 0.1947 0.3841 0.0072  -0.0016 -0.0898 162 ASP   B CG  
6228 O  OD1 . ASP   B 162 ? 0.2000 0.2181 0.3764 -0.0048 0.0170  -0.0849 162 ASP   B OD1 
6229 O  OD2 . ASP   B 162 ? 0.2159 0.2139 0.4125 0.0229  -0.0088 -0.0901 162 ASP   B OD2 
6234 N  N   . LYS   B 163 ? 0.1655 0.1280 0.3314 -0.0094 -0.0263 -0.0279 163 LYS   B N   
6235 C  CA  . LYS   B 163 ? 0.1751 0.1392 0.3322 -0.0176 -0.0211 -0.0122 163 LYS   B CA  
6236 C  C   . LYS   B 163 ? 0.1495 0.1333 0.3167 -0.0173 -0.0228 0.0012  163 LYS   B C   
6237 O  O   . LYS   B 163 ? 0.1467 0.1449 0.3435 -0.0206 -0.0197 0.0098  163 LYS   B O   
6238 C  CB  . LYS   B 163 ? 0.2207 0.1754 0.3791 -0.0181 -0.0190 0.0035  163 LYS   B CB  
6239 C  CG  . LYS   B 163 ? 0.2994 0.2570 0.4377 -0.0236 -0.0113 0.0177  163 LYS   B CG  
6240 C  CD  . LYS   B 163 ? 0.3707 0.3365 0.4975 -0.0372 -0.0135 0.0227  163 LYS   B CD  
6241 C  CE  . LYS   B 163 ? 0.4330 0.4020 0.5338 -0.0455 -0.0080 0.0282  163 LYS   B CE  
6242 N  NZ  . LYS   B 163 ? 0.4644 0.4445 0.5606 -0.0489 -0.0044 0.0241  163 LYS   B NZ  
6256 N  N   . LEU   B 164 ? 0.1379 0.1250 0.2968 -0.0125 -0.0134 -0.0029 164 LEU   B N   
6257 C  CA  . LEU   B 164 ? 0.1435 0.1292 0.2761 -0.0161 -0.0221 -0.0024 164 LEU   B CA  
6258 C  C   . LEU   B 164 ? 0.1510 0.1343 0.2812 -0.0201 -0.0333 0.0001  164 LEU   B C   
6259 O  O   . LEU   B 164 ? 0.1521 0.1524 0.3025 -0.0202 -0.0300 0.0004  164 LEU   B O   
6260 C  CB  . LEU   B 164 ? 0.1406 0.1288 0.2502 -0.0142 -0.0097 -0.0010 164 LEU   B CB  
6261 C  CG  . LEU   B 164 ? 0.1530 0.1461 0.2562 -0.0144 -0.0038 0.0010  164 LEU   B CG  
6262 C  CD1 . LEU   B 164 ? 0.1545 0.1454 0.2586 -0.0160 -0.0172 -0.0059 164 LEU   B CD1 
6263 C  CD2 . LEU   B 164 ? 0.1701 0.1835 0.2836 -0.0110 0.0063  -0.0093 164 LEU   B CD2 
6275 N  N   . VAL   B 165 ? 0.1850 0.1422 0.3092 -0.0285 -0.0343 -0.0099 165 VAL   B N   
6276 C  CA  . VAL   B 165 ? 0.2178 0.1538 0.3047 -0.0418 -0.0494 -0.0084 165 VAL   B CA  
6277 C  C   . VAL   B 165 ? 0.2463 0.1648 0.3344 -0.0471 -0.0785 -0.0031 165 VAL   B C   
6278 O  O   . VAL   B 165 ? 0.2646 0.1821 0.3417 -0.0534 -0.0830 0.0094  165 VAL   B O   
6279 C  CB  . VAL   B 165 ? 0.2383 0.1706 0.3017 -0.0285 -0.0177 -0.0232 165 VAL   B CB  
6280 C  CG1 . VAL   B 165 ? 0.2493 0.1818 0.3221 -0.0316 -0.0020 -0.0150 165 VAL   B CG1 
6281 C  CG2 . VAL   B 165 ? 0.2341 0.1785 0.2960 -0.0244 -0.0074 -0.0166 165 VAL   B CG2 
6291 N  N   . SER   B 166 ? 0.2541 0.1532 0.3684 -0.0421 -0.0890 -0.0254 166 SER   B N   
6292 C  CA  . SER   B 166 ? 0.2449 0.1572 0.4222 -0.0451 -0.0747 -0.0288 166 SER   B CA  
6293 C  C   . SER   B 166 ? 0.2249 0.1711 0.4356 -0.0419 -0.0765 -0.0027 166 SER   B C   
6294 O  O   . SER   B 166 ? 0.2289 0.1917 0.4648 -0.0525 -0.0837 -0.0270 166 SER   B O   
6295 C  CB  . SER   B 166 ? 0.2492 0.1696 0.4519 -0.0336 -0.0648 -0.0313 166 SER   B CB  
6296 O  OG  . SER   B 166 ? 0.2388 0.1642 0.4684 -0.0279 -0.0645 -0.0161 166 SER   B OG  
6302 N  N   . SER   B 167 ? 0.2050 0.1581 0.4094 -0.0449 -0.0808 0.0381  167 SER   B N   
6303 C  CA  . SER   B 167 ? 0.2004 0.1643 0.3867 -0.0373 -0.0518 0.0335  167 SER   B CA  
6304 C  C   . SER   B 167 ? 0.1977 0.1711 0.3651 -0.0459 -0.0389 0.0493  167 SER   B C   
6305 O  O   . SER   B 167 ? 0.1978 0.1849 0.3488 -0.0515 -0.0300 0.0481  167 SER   B O   
6306 C  CB  . SER   B 167 ? 0.1864 0.1746 0.3848 -0.0339 -0.0216 0.0189  167 SER   B CB  
6307 O  OG  . SER   B 167 ? 0.1805 0.1825 0.3675 -0.0262 -0.0049 0.0177  167 SER   B OG  
6313 N  N   . PHE   B 168 ? 0.1961 0.1699 0.3506 -0.0428 -0.0328 0.0531  168 PHE   B N   
6314 C  CA  . PHE   B 168 ? 0.2014 0.1691 0.3233 -0.0463 -0.0333 0.0334  168 PHE   B CA  
6315 C  C   . PHE   B 168 ? 0.1772 0.1566 0.2843 -0.0275 -0.0082 0.0193  168 PHE   B C   
6316 O  O   . PHE   B 168 ? 0.2098 0.1462 0.2780 -0.0032 -0.0113 0.0047  168 PHE   B O   
6317 C  CB  . PHE   B 168 ? 0.2176 0.1740 0.3233 -0.0529 -0.0565 0.0427  168 PHE   B CB  
6318 C  CG  . PHE   B 168 ? 0.2433 0.1596 0.3106 -0.0533 -0.0546 0.0208  168 PHE   B CG  
6319 C  CD1 . PHE   B 168 ? 0.2742 0.1613 0.3159 -0.0498 -0.0638 0.0176  168 PHE   B CD1 
6320 C  CD2 . PHE   B 168 ? 0.2299 0.1521 0.2989 -0.0468 -0.0514 0.0165  168 PHE   B CD2 
6321 C  CE1 . PHE   B 168 ? 0.2860 0.1685 0.3061 -0.0369 -0.0549 0.0194  168 PHE   B CE1 
6322 C  CE2 . PHE   B 168 ? 0.2579 0.1589 0.3082 -0.0317 -0.0524 0.0153  168 PHE   B CE2 
6323 C  CZ  . PHE   B 168 ? 0.2739 0.1557 0.3083 -0.0238 -0.0578 0.0254  168 PHE   B CZ  
6333 N  N   . LEU   B 169 ? 0.1764 0.1702 0.2813 -0.0013 0.0010  0.0074  169 LEU   B N   
6334 C  CA  . LEU   B 169 ? 0.2023 0.1962 0.3081 -0.0033 0.0014  -0.0241 169 LEU   B CA  
6335 C  C   . LEU   B 169 ? 0.2334 0.2219 0.3620 0.0103  -0.0038 -0.0495 169 LEU   B C   
6336 O  O   . LEU   B 169 ? 0.2543 0.2449 0.4108 0.0029  -0.0086 -0.0724 169 LEU   B O   
6337 C  CB  . LEU   B 169 ? 0.2240 0.2369 0.3151 -0.0132 -0.0023 -0.0042 169 LEU   B CB  
6338 C  CG  . LEU   B 169 ? 0.2638 0.2810 0.3493 -0.0047 -0.0029 0.0016  169 LEU   B CG  
6339 C  CD1 . LEU   B 169 ? 0.2783 0.3008 0.3512 -0.0005 -0.0085 0.0160  169 LEU   B CD1 
6340 C  CD2 . LEU   B 169 ? 0.2628 0.2899 0.3499 0.0044  0.0084  -0.0118 169 LEU   B CD2 
6341 O  OXT . LEU   B 169 ? 0.2540 0.2359 0.3645 0.0383  0.0027  -0.0526 169 LEU   B OXT 
6353 N  N2  B A1A72 C .   ? 0.1581 0.1678 0.1664 -0.0053 0.0013  0.0121  201 A1A72 A N2  
6354 C  C3  B A1A72 C .   ? 0.1563 0.1674 0.1606 -0.0070 0.0007  0.0178  201 A1A72 A C3  
6355 C  C6  B A1A72 C .   ? 0.1486 0.1653 0.1607 -0.0084 0.0055  0.0241  201 A1A72 A C6  
6356 C  C9  B A1A72 C .   ? 0.1885 0.1917 0.1602 -0.0162 -0.0037 0.0168  201 A1A72 A C9  
6357 C  C12 B A1A72 C .   ? 0.1899 0.1954 0.1742 -0.0078 0.0054  0.0190  201 A1A72 A C12 
6358 C  C14 B A1A72 C .   ? 0.1884 0.1934 0.1783 -0.0075 0.0058  0.0188  201 A1A72 A C14 
6359 C  C1  B A1A72 C .   ? 0.1850 0.1854 0.1706 -0.0204 -0.0006 0.0053  201 A1A72 A C1  
6360 C  C10 B A1A72 C .   ? 0.1894 0.1914 0.1655 -0.0107 0.0037  0.0211  201 A1A72 A C10 
6361 C  C11 B A1A72 C .   ? 0.1909 0.1934 0.1696 -0.0088 0.0034  0.0198  201 A1A72 A C11 
6362 C  C13 B A1A72 C .   ? 0.1872 0.1945 0.1795 -0.0048 0.0065  0.0257  201 A1A72 A C13 
6363 C  C15 B A1A72 C .   ? 0.1880 0.1904 0.1692 -0.0085 0.0053  0.0190  201 A1A72 A C15 
6364 C  C2  B A1A72 C .   ? 0.1820 0.1828 0.1634 -0.0161 -0.0047 0.0123  201 A1A72 A C2  
6365 C  C4  B A1A72 C .   ? 0.1557 0.1683 0.1652 -0.0052 0.0043  0.0196  201 A1A72 A C4  
6366 C  C5  B A1A72 C .   ? 0.1479 0.1638 0.1593 -0.0074 0.0064  0.0255  201 A1A72 A C5  
6367 C  C7  B A1A72 C .   ? 0.1458 0.1663 0.1632 -0.0105 0.0080  0.0306  201 A1A72 A C7  
6368 C  C8  B A1A72 C .   ? 0.1414 0.1638 0.1621 -0.0123 0.0029  0.0305  201 A1A72 A C8  
6369 N  N1  B A1A72 C .   ? 0.1662 0.1706 0.1589 -0.0090 -0.0012 0.0181  201 A1A72 A N1  
6370 N  N3  B A1A72 C .   ? 0.1516 0.1656 0.1589 -0.0083 0.0100  0.0283  201 A1A72 A N3  
6371 N  N4  B A1A72 C .   ? 0.1459 0.1640 0.1612 -0.0057 0.0028  0.0262  201 A1A72 A N4  
6372 O  O1  B A1A72 C .   ? 0.1830 0.1845 0.1679 -0.0204 0.0065  -0.0004 201 A1A72 A O1  
6373 O  O2  B A1A72 C .   ? 0.1933 0.2001 0.1555 -0.0208 -0.0134 0.0190  201 A1A72 A O2  
6374 CL CL1 B A1A72 C .   ? 0.1857 0.1960 0.1890 0.0017  0.0086  0.0371  201 A1A72 A CL1 
6390 O  O1  C A1A73 D .   ? 0.1839 0.1866 0.1903 0.0061  0.0035  0.0045  202 A1A73 A O1  
6391 C  C1  C A1A73 D .   ? 0.1806 0.1832 0.1861 0.0048  0.0002  0.0063  202 A1A73 A C1  
6392 C  C2  C A1A73 D .   ? 0.1761 0.1771 0.1838 -0.0013 -0.0034 0.0103  202 A1A73 A C2  
6393 C  C3  C A1A73 D .   ? 0.1465 0.1595 0.1692 -0.0071 -0.0045 0.0114  202 A1A73 A C3  
6394 C  C4  C A1A73 D .   ? 0.1408 0.1593 0.1714 -0.0085 -0.0055 0.0143  202 A1A73 A C4  
6395 C  C5  C A1A73 D .   ? 0.1357 0.1524 0.1590 -0.0058 -0.0048 0.0202  202 A1A73 A C5  
6396 C  C6  C A1A73 D .   ? 0.1373 0.1541 0.1634 -0.0067 -0.0033 0.0194  202 A1A73 A C6  
6397 C  C7  C A1A73 D .   ? 0.1337 0.1538 0.1620 -0.0077 0.0000  0.0252  202 A1A73 A C7  
6398 C  C8  C A1A73 D .   ? 0.1290 0.1517 0.1590 -0.0097 -0.0069 0.0251  202 A1A73 A C8  
6399 C  C10 C A1A73 D .   ? 0.1905 0.1920 0.2019 0.0000  -0.0041 0.0179  202 A1A73 A C10 
6400 C  C11 C A1A73 D .   ? 0.1901 0.1953 0.2018 0.0007  -0.0015 0.0172  202 A1A73 A C11 
6401 C  C12 C A1A73 D .   ? 0.1875 0.1994 0.2113 0.0031  0.0021  0.0183  202 A1A73 A C12 
6402 C  C13 C A1A73 D .   ? 0.1846 0.2021 0.2240 0.0077  0.0050  0.0281  202 A1A73 A C13 
6403 C  C14 C A1A73 D .   ? 0.1883 0.1987 0.2118 0.0052  0.0033  0.0242  202 A1A73 A C14 
6404 C  C15 C A1A73 D .   ? 0.1910 0.1953 0.2077 0.0030  -0.0008 0.0190  202 A1A73 A C15 
6405 C  C9  C A1A73 D .   ? 0.1901 0.1883 0.1979 -0.0003 -0.0067 0.0165  202 A1A73 A C9  
6406 N  N1  C A1A73 D .   ? 0.1614 0.1651 0.1782 -0.0060 -0.0029 0.0137  202 A1A73 A N1  
6407 N  N2  C A1A73 D .   ? 0.1418 0.1594 0.1745 -0.0098 -0.0081 0.0080  202 A1A73 A N2  
6408 N  N3  C A1A73 D .   ? 0.1382 0.1556 0.1626 -0.0089 -0.0014 0.0221  202 A1A73 A N3  
6409 N  N4  C A1A73 D .   ? 0.1343 0.1516 0.1572 -0.0031 -0.0092 0.0213  202 A1A73 A N4  
6410 O  O2  C A1A73 D .   ? 0.1999 0.1931 0.2015 0.0012  -0.0084 0.0264  202 A1A73 A O2  
6411 CL CL1 C A1A73 D .   ? 0.1810 0.2099 0.2611 0.0142  0.0139  0.0393  202 A1A73 A CL1 
6427 N  N2  D A1A72 E .   ? 0.1233 0.1357 0.1830 0.0056  -0.0187 0.0028  203 A1A72 A N2  
6428 C  C3  D A1A72 E .   ? 0.1223 0.1338 0.1722 0.0062  -0.0166 0.0074  203 A1A72 A C3  
6429 C  C6  D A1A72 E .   ? 0.1116 0.1237 0.1673 0.0074  -0.0102 0.0181  203 A1A72 A C6  
6430 C  C9  D A1A72 E .   ? 0.1548 0.1678 0.1888 -0.0085 -0.0256 0.0135  203 A1A72 A C9  
6431 C  C12 D A1A72 E .   ? 0.1766 0.1831 0.2152 0.0031  -0.0189 0.0217  203 A1A72 A C12 
6432 C  C14 D A1A72 E .   ? 0.1758 0.1801 0.2065 0.0021  -0.0108 0.0355  203 A1A72 A C14 
6433 C  C1  D A1A72 E .   ? 0.1588 0.1584 0.1844 0.0110  -0.0118 0.0183  203 A1A72 A C1  
6434 C  C10 D A1A72 E .   ? 0.1688 0.1722 0.1972 -0.0049 -0.0198 0.0204  203 A1A72 A C10 
6435 C  C11 D A1A72 E .   ? 0.1727 0.1765 0.1999 -0.0009 -0.0191 0.0192  203 A1A72 A C11 
6436 C  C13 D A1A72 E .   ? 0.1754 0.1866 0.2269 0.0080  -0.0201 0.0365  203 A1A72 A C13 
6437 C  C15 D A1A72 E .   ? 0.1752 0.1767 0.2034 -0.0011 -0.0132 0.0258  203 A1A72 A C15 
6438 C  C2  D A1A72 E .   ? 0.1529 0.1540 0.1839 0.0045  -0.0210 0.0133  203 A1A72 A C2  
6439 C  C4  D A1A72 E .   ? 0.1220 0.1346 0.1802 0.0063  -0.0101 0.0131  203 A1A72 A C4  
6440 C  C5  D A1A72 E .   ? 0.1112 0.1208 0.1627 0.0096  -0.0075 0.0192  203 A1A72 A C5  
6441 C  C7  D A1A72 E .   ? 0.1081 0.1228 0.1652 0.0055  -0.0059 0.0231  203 A1A72 A C7  
6442 C  C8  D A1A72 E .   ? 0.1011 0.1201 0.1608 0.0017  -0.0155 0.0239  203 A1A72 A C8  
6443 N  N1  D A1A72 E .   ? 0.1359 0.1403 0.1799 0.0065  -0.0187 0.0141  203 A1A72 A N1  
6444 N  N3  D A1A72 E .   ? 0.1171 0.1270 0.1679 0.0051  -0.0013 0.0247  203 A1A72 A N3  
6445 N  N4  D A1A72 E .   ? 0.1090 0.1191 0.1596 0.0131  -0.0133 0.0194  203 A1A72 A N4  
6446 O  O1  D A1A72 E .   ? 0.1650 0.1638 0.1793 0.0145  -0.0070 0.0194  203 A1A72 A O1  
6447 O  O2  D A1A72 E .   ? 0.1349 0.1713 0.1673 -0.0222 -0.0313 0.0199  203 A1A72 A O2  
6448 CL CL1 D A1A72 E .   ? 0.1773 0.1987 0.2728 0.0174  -0.0258 0.0475  203 A1A72 A CL1 
6464 CL CL  C CL    F .   ? 0.1538 0.1365 0.2388 -0.0115 0.0076  0.0130  204 CL    A CL  
6465 O  O   . HOH   G .   ? 0.4413 0.7070 0.5263 0.1060  -0.0064 0.0466  301 HOH   A O   
6466 O  O   . HOH   G .   ? 0.7001 0.6251 0.3506 -0.1522 -0.0457 0.1940  302 HOH   A O   
6467 O  O   . HOH   G .   ? 0.4117 0.8153 0.4597 -0.1193 0.0477  0.0679  303 HOH   A O   
6468 O  O   . HOH   G .   ? 0.3046 0.6113 0.6523 0.0885  0.0865  0.1182  304 HOH   A O   
6469 O  O   . HOH   G .   ? 0.5485 0.4675 0.3264 0.1677  -0.0987 0.0620  305 HOH   A O   
6470 O  O   . HOH   G .   ? 0.7541 0.4400 0.5494 -0.1161 0.2028  0.1701  306 HOH   A O   
6471 O  O   . HOH   G .   ? 0.6296 0.7122 0.4426 -0.1290 -0.1200 -0.1075 307 HOH   A O   
6472 O  O   . HOH   G .   ? 0.5563 0.3951 0.5681 -0.0204 0.1899  0.1509  308 HOH   A O   
6473 O  O   . HOH   G .   ? 0.3157 0.3105 0.1943 -0.0199 0.0590  0.0552  309 HOH   A O   
6474 O  O   . HOH   G .   ? 0.2610 0.2231 0.4123 -0.0135 -0.0531 0.0404  310 HOH   A O   
6475 O  O   . HOH   G .   ? 0.5393 0.6414 0.3921 0.2048  -0.0454 -0.0645 311 HOH   A O   
6476 O  O   B HOH   G .   ? 0.1757 0.1690 0.1850 -0.0018 0.0225  0.0145  312 HOH   A O   
6477 O  O   . HOH   G .   ? 0.2031 0.1680 0.2534 0.0202  -0.0325 -0.0072 313 HOH   A O   
6478 O  O   . HOH   G .   ? 0.4522 0.3508 0.6181 -0.0002 0.1924  -0.0168 314 HOH   A O   
6479 O  O   . HOH   G .   ? 0.4937 0.1921 0.5314 0.0700  -0.0004 -0.0017 315 HOH   A O   
6480 O  O   . HOH   G .   ? 0.4808 0.5710 0.6056 0.2139  0.1271  -0.0723 316 HOH   A O   
6481 O  O   . HOH   G .   ? 0.2047 0.1963 0.3585 -0.0460 0.0029  -0.0332 317 HOH   A O   
6482 O  O   A HOH   G .   ? 0.3107 0.3944 0.5752 -0.0279 0.1507  0.1821  318 HOH   A O   
6483 O  O   . HOH   G .   ? 0.4348 0.4022 0.2942 -0.0532 -0.0694 -0.0048 319 HOH   A O   
6484 O  O   A HOH   G .   ? 0.1934 0.1884 0.2715 -0.0114 0.0473  0.0625  320 HOH   A O   
6485 O  O   . HOH   G .   ? 0.3250 0.2999 0.3056 -0.0914 0.0254  0.0631  321 HOH   A O   
6486 O  O   . HOH   G .   ? 0.2058 0.3690 0.4297 -0.0378 0.0318  -0.1099 322 HOH   A O   
6487 O  O   . HOH   G .   ? 0.3695 0.3745 0.3783 -0.0671 0.1638  0.0417  323 HOH   A O   
6488 O  O   . HOH   G .   ? 0.1746 0.3245 0.2901 0.0265  -0.0253 -0.0028 324 HOH   A O   
6489 O  O   . HOH   G .   ? 0.1625 0.1677 0.2502 -0.0184 0.0177  0.0402  325 HOH   A O   
6490 O  O   . HOH   G .   ? 0.2583 0.5798 0.4077 -0.0341 -0.0746 0.1173  326 HOH   A O   
6491 O  O   . HOH   G .   ? 0.2927 0.2848 0.3442 -0.0069 -0.0531 -0.0516 327 HOH   A O   
6492 O  O   . HOH   G .   ? 0.6990 0.6173 0.3673 -0.0994 -0.0334 0.1430  328 HOH   A O   
6493 O  O   . HOH   G .   ? 0.2525 0.1994 0.2619 -0.0287 0.0212  0.0048  329 HOH   A O   
6494 O  O   . HOH   G .   ? 0.1500 0.4500 0.2955 0.0007  0.0203  0.1087  330 HOH   A O   
6495 O  O   . HOH   G .   ? 0.5755 0.4994 0.4673 -0.1433 0.0242  0.1835  331 HOH   A O   
6496 O  O   . HOH   G .   ? 0.8819 0.4832 0.5945 -0.0537 -0.1315 0.1223  332 HOH   A O   
6497 O  O   . HOH   G .   ? 0.1515 0.1548 0.2294 -0.0207 0.0070  0.0101  333 HOH   A O   
6498 O  O   . HOH   G .   ? 0.1486 0.1659 0.2832 0.0077  -0.0405 -0.0363 334 HOH   A O   
6499 O  O   B HOH   G .   ? 0.1858 0.2528 0.2575 -0.0450 -0.0022 0.0355  335 HOH   A O   
6500 O  O   . HOH   G .   ? 0.2125 0.4941 0.4000 -0.0405 -0.0592 0.2072  336 HOH   A O   
6501 O  O   . HOH   G .   ? 0.6226 0.6141 0.4798 -0.0140 -0.0220 -0.0385 337 HOH   A O   
6502 O  O   . HOH   G .   ? 0.3091 0.4436 0.2526 -0.0183 0.0438  0.0429  338 HOH   A O   
6503 O  O   B HOH   G .   ? 0.1466 0.2138 0.4057 -0.0330 -0.0770 0.0396  339 HOH   A O   
6504 O  O   . HOH   G .   ? 0.1407 0.2172 0.2290 0.0048  -0.0073 0.0512  340 HOH   A O   
6505 O  O   . HOH   G .   ? 0.2533 0.2287 0.2644 0.0438  0.0414  0.0432  341 HOH   A O   
6506 O  O   . HOH   G .   ? 0.3657 0.3006 0.3749 -0.0938 -0.0316 -0.0157 342 HOH   A O   
6507 O  O   . HOH   G .   ? 0.2981 0.3716 0.3780 -0.0976 -0.0972 -0.0248 343 HOH   A O   
6508 O  O   A HOH   G .   ? 0.3579 0.1448 0.1901 0.0269  0.0571  0.0294  344 HOH   A O   
6509 O  O   . HOH   G .   ? 0.7195 0.4427 0.5393 0.0655  0.2332  -0.1117 345 HOH   A O   
6510 O  O   . HOH   G .   ? 0.4512 0.2223 0.4420 0.0461  -0.1569 0.0783  346 HOH   A O   
6511 O  O   . HOH   G .   ? 0.3516 0.4100 0.3870 0.1606  0.0707  0.0629  347 HOH   A O   
6512 O  O   . HOH   G .   ? 0.1686 0.1658 0.2211 0.0121  -0.0218 0.0310  348 HOH   A O   
6513 O  O   . HOH   G .   ? 0.3307 0.3721 0.2292 -0.1148 -0.0105 -0.0648 349 HOH   A O   
6514 O  O   . HOH   G .   ? 0.6627 0.5332 0.5220 0.0747  -0.0911 -0.0404 350 HOH   A O   
6515 O  O   . HOH   G .   ? 0.2534 0.4131 0.3485 0.1002  -0.0849 -0.0519 351 HOH   A O   
6516 O  O   . HOH   G .   ? 0.2929 0.2382 0.4687 -0.0253 -0.1176 0.0938  352 HOH   A O   
6517 O  O   . HOH   G .   ? 0.3475 0.6845 0.4949 -0.0457 -0.1379 0.0658  353 HOH   A O   
6518 O  O   . HOH   G .   ? 0.2623 0.4405 0.3240 -0.0591 0.0429  0.0227  354 HOH   A O   
6519 O  O   . HOH   G .   ? 0.5204 0.3916 0.4663 -0.1722 -0.0858 0.2099  355 HOH   A O   
6520 O  O   . HOH   G .   ? 0.5056 0.5547 0.3134 -0.1399 0.1452  0.0467  356 HOH   A O   
6521 O  O   . HOH   G .   ? 0.2023 0.1905 0.3978 0.0188  0.1024  -0.0139 357 HOH   A O   
6522 O  O   B HOH   G .   ? 0.2571 0.2881 0.4231 0.0314  0.0229  0.0437  358 HOH   A O   
6523 O  O   . HOH   G .   ? 0.2096 0.1883 0.2934 -0.0009 -0.0610 -0.0173 359 HOH   A O   
6524 O  O   . HOH   G .   ? 0.3022 0.3477 0.4724 -0.0697 -0.0806 -0.0939 360 HOH   A O   
6525 O  O   . HOH   G .   ? 0.1323 0.1300 0.1526 -0.0018 0.0062  0.0127  361 HOH   A O   
6526 O  O   . HOH   G .   ? 0.1423 0.1939 0.2703 0.0078  -0.0044 0.0120  362 HOH   A O   
6527 O  O   . HOH   G .   ? 0.1558 0.1289 0.2377 -0.0092 0.0217  -0.0078 363 HOH   A O   
6528 O  O   . HOH   G .   ? 0.4108 0.6768 0.4254 -0.0489 0.0252  0.1848  364 HOH   A O   
6529 O  O   . HOH   G .   ? 0.1742 0.2361 0.2175 -0.0193 0.0002  0.0780  365 HOH   A O   
6530 O  O   . HOH   G .   ? 0.6015 0.3788 0.3122 0.0654  0.0714  0.1273  366 HOH   A O   
6531 O  O   . HOH   G .   ? 0.4677 0.2317 0.4141 -0.1299 0.1766  -0.0411 367 HOH   A O   
6532 O  O   A HOH   G .   ? 0.2288 0.2523 0.2298 -0.0158 0.0848  0.0350  368 HOH   A O   
6533 O  O   B HOH   G .   ? 0.1878 0.2017 0.2715 0.0581  -0.0975 -0.0285 369 HOH   A O   
6534 O  O   . HOH   G .   ? 0.3910 0.2042 0.2483 0.1139  0.0539  0.0107  370 HOH   A O   
6535 O  O   . HOH   G .   ? 0.1434 0.1500 0.1576 -0.0032 -0.0149 -0.0035 371 HOH   A O   
6536 O  O   . HOH   G .   ? 0.2751 0.4671 0.3235 0.0616  0.0764  0.2149  372 HOH   A O   
6537 O  O   . HOH   G .   ? 0.3795 0.2281 0.4815 -0.1059 0.0692  0.0476  373 HOH   A O   
6538 O  O   . HOH   G .   ? 0.1892 0.2422 0.3665 0.0159  0.0830  -0.0503 374 HOH   A O   
6539 O  O   . HOH   G .   ? 0.1847 0.1904 0.2475 -0.0286 0.0072  0.0359  375 HOH   A O   
6540 O  O   . HOH   G .   ? 0.7199 0.7268 0.7191 -0.0789 -0.0107 -0.1284 376 HOH   A O   
6541 O  O   . HOH   G .   ? 0.3416 0.2922 0.5545 0.0792  0.0747  0.0461  377 HOH   A O   
6542 O  O   . HOH   G .   ? 0.3191 0.5461 0.6035 0.0632  -0.0483 0.1889  378 HOH   A O   
6543 O  O   . HOH   G .   ? 0.4996 0.2536 0.4663 0.0605  -0.0296 0.0025  379 HOH   A O   
6544 O  O   . HOH   G .   ? 0.5906 0.6576 0.6061 -0.0790 0.0716  0.0459  380 HOH   A O   
6545 O  O   . HOH   G .   ? 0.3296 0.2473 0.3370 -0.0046 -0.0308 0.0854  381 HOH   A O   
6546 O  O   . HOH   G .   ? 0.4341 0.2822 0.2645 -0.0129 0.0096  0.0198  382 HOH   A O   
6547 O  O   . HOH   G .   ? 0.2988 0.2875 0.2137 0.0306  0.0712  0.0102  383 HOH   A O   
6548 O  O   . HOH   G .   ? 0.2965 0.3621 0.5464 -0.0343 0.1370  -0.0472 384 HOH   A O   
6549 O  O   . HOH   G .   ? 0.1316 0.1407 0.1909 -0.0015 -0.0142 0.0128  385 HOH   A O   
6550 O  O   B HOH   G .   ? 0.2073 0.2739 0.2291 0.1197  0.0410  0.1018  386 HOH   A O   
6551 O  O   . HOH   G .   ? 0.3212 0.2310 0.5113 -0.0586 -0.0172 -0.0262 387 HOH   A O   
6552 O  O   . HOH   G .   ? 0.2566 0.3937 0.3984 -0.0101 0.0125  0.0907  388 HOH   A O   
6553 O  O   . HOH   G .   ? 0.1966 0.2220 0.2356 -0.0240 -0.0371 0.0453  389 HOH   A O   
6554 O  O   . HOH   G .   ? 0.1769 0.1372 0.1627 -0.0191 0.0135  0.0049  390 HOH   A O   
6555 O  O   . HOH   G .   ? 0.3538 0.6936 0.3828 0.1670  0.1086  -0.0861 391 HOH   A O   
6556 O  O   . HOH   G .   ? 0.1793 0.2019 0.2842 -0.0025 -0.0146 0.0740  392 HOH   A O   
6557 O  O   . HOH   G .   ? 0.3361 0.3324 0.4881 0.0309  0.1182  -0.0810 393 HOH   A O   
6558 O  O   A HOH   G .   ? 0.1898 0.4255 0.2246 0.0709  0.0212  0.0120  394 HOH   A O   
6559 O  O   . HOH   G .   ? 0.2859 0.3149 0.3887 -0.1008 0.1065  -0.0255 395 HOH   A O   
6560 O  O   . HOH   G .   ? 0.1601 0.2402 0.4040 -0.0094 0.0711  0.0836  396 HOH   A O   
6561 O  O   A HOH   G .   ? 0.1406 0.2508 0.2145 0.0445  0.0311  0.0708  397 HOH   A O   
6562 O  O   . HOH   G .   ? 0.1969 0.1802 0.1895 0.0085  0.0103  0.0254  398 HOH   A O   
6563 O  O   . HOH   G .   ? 0.2428 0.1984 0.1926 -0.0515 0.0264  0.0247  399 HOH   A O   
6564 O  O   . HOH   G .   ? 0.1795 0.1827 0.3857 0.0359  0.1029  0.1025  400 HOH   A O   
6565 O  O   . HOH   G .   ? 0.2976 0.2634 0.2375 -0.0599 -0.0866 0.0233  401 HOH   A O   
6566 O  O   . HOH   G .   ? 0.2391 0.3825 0.3676 -0.0316 0.1054  -0.0865 402 HOH   A O   
6567 O  O   . HOH   G .   ? 0.4674 0.7084 0.5841 0.0898  0.0077  0.0789  403 HOH   A O   
6568 O  O   . HOH   G .   ? 0.3864 0.4057 0.2389 0.0088  -0.1067 0.0364  404 HOH   A O   
6569 O  O   . HOH   G .   ? 0.5414 0.6038 0.5802 -0.0868 -0.0615 -0.0720 405 HOH   A O   
6570 O  O   . HOH   G .   ? 0.1580 0.1635 0.2107 0.0149  -0.0335 -0.0012 406 HOH   A O   
6571 O  O   . HOH   G .   ? 0.5069 0.4917 0.2187 -0.0263 0.1080  0.1157  407 HOH   A O   
6572 O  O   . HOH   G .   ? 0.2072 0.1663 0.2997 0.0033  -0.0246 0.0079  408 HOH   A O   
6573 O  O   A HOH   G .   ? 0.2076 0.1912 0.2027 0.0075  -0.0206 0.0502  409 HOH   A O   
6574 O  O   B HOH   G .   ? 0.3172 0.2937 0.2606 -0.0519 0.0263  -0.0748 410 HOH   A O   
6575 O  O   . HOH   G .   ? 0.2479 0.1806 0.2540 0.0030  0.0193  0.0306  411 HOH   A O   
6576 O  O   . HOH   G .   ? 0.1788 0.2543 0.4055 -0.0065 -0.0303 0.0175  412 HOH   A O   
6577 O  O   A HOH   G .   ? 0.1181 0.1296 0.1236 -0.0010 -0.0064 -0.0030 413 HOH   A O   
6578 O  O   B HOH   G .   ? 0.2595 0.3284 0.1754 -0.0083 0.0535  0.0989  414 HOH   A O   
6579 O  O   . HOH   G .   ? 0.2454 0.2090 0.2567 -0.0525 0.0106  0.0561  415 HOH   A O   
6580 O  O   . HOH   G .   ? 0.4520 0.5538 0.3173 -0.0587 -0.0072 0.1171  416 HOH   A O   
6581 O  O   A HOH   G .   ? 0.3944 0.4573 0.4462 -0.0946 -0.0102 0.1010  417 HOH   A O   
6582 O  O   . HOH   G .   ? 0.3097 0.3604 0.7388 -0.0358 0.1351  -0.0546 418 HOH   A O   
6583 O  O   . HOH   G .   ? 0.4162 0.2253 0.5248 -0.0904 -0.2305 0.1093  419 HOH   A O   
6584 O  O   . HOH   G .   ? 0.2164 0.2790 0.2549 -0.0046 -0.0523 0.0584  420 HOH   A O   
6585 O  O   A HOH   G .   ? 0.3643 0.2197 0.3841 -0.0619 0.1076  -0.0188 421 HOH   A O   
6586 O  O   . HOH   G .   ? 0.3501 0.6194 0.5628 -0.0593 -0.1016 0.1667  422 HOH   A O   
6587 O  O   . HOH   G .   ? 0.1824 0.1863 0.3020 0.0140  -0.0438 0.0388  423 HOH   A O   
6588 O  O   . HOH   G .   ? 0.2833 0.5994 0.1743 -0.0405 0.0502  0.0259  424 HOH   A O   
6589 O  O   . HOH   G .   ? 0.1480 0.1645 0.3147 0.0005  -0.0014 0.0180  425 HOH   A O   
6590 O  O   . HOH   G .   ? 0.5111 0.2652 0.3175 -0.1135 0.0586  0.0410  426 HOH   A O   
6591 O  O   . HOH   G .   ? 0.2292 0.2435 0.4180 0.0146  -0.0481 -0.0448 427 HOH   A O   
6592 O  O   . HOH   G .   ? 0.3228 0.1285 0.2089 0.0073  -0.0472 0.0149  428 HOH   A O   
6593 O  O   A HOH   G .   ? 0.1692 0.1657 0.2289 -0.0003 -0.0386 0.0311  429 HOH   A O   
6594 O  O   . HOH   G .   ? 0.3832 0.5062 0.3628 0.1093  -0.0926 -0.1371 430 HOH   A O   
6595 O  O   . HOH   G .   ? 0.6722 0.4028 0.4929 0.1861  -0.0913 0.1632  431 HOH   A O   
6596 O  O   . HOH   G .   ? 0.2160 0.1698 0.1679 -0.0064 0.0153  0.0151  432 HOH   A O   
6597 O  O   . HOH   G .   ? 0.2321 0.4113 0.2648 0.1507  -0.0029 0.0368  433 HOH   A O   
6598 O  O   . HOH   G .   ? 0.1641 0.2225 0.3139 -0.0230 -0.0148 0.0604  434 HOH   A O   
6599 O  O   . HOH   G .   ? 0.5427 0.4710 0.3737 -0.0210 -0.1480 0.0126  435 HOH   A O   
6600 O  O   . HOH   G .   ? 0.1928 0.2258 0.4620 -0.0303 -0.0846 0.0770  436 HOH   A O   
6601 O  O   B HOH   G .   ? 0.3105 0.1790 0.2549 0.0780  -0.0565 0.0316  437 HOH   A O   
6602 O  O   B HOH   G .   ? 0.4895 0.3311 0.4462 -0.0229 -0.0052 -0.0356 438 HOH   A O   
6603 O  O   A HOH   G .   ? 0.1903 0.1180 0.1015 0.0163  -0.0117 -0.0067 439 HOH   A O   
6604 O  O   . HOH   G .   ? 0.6051 0.7972 0.4730 0.0852  0.2742  -0.1098 440 HOH   A O   
6605 O  O   A HOH   G .   ? 0.3867 0.3681 0.5826 0.0136  -0.1140 0.0672  441 HOH   A O   
6606 O  O   . HOH   G .   ? 0.7021 0.8017 0.4563 0.2143  -0.1089 0.1986  442 HOH   A O   
6607 O  O   A HOH   G .   ? 0.3013 0.2611 0.3114 0.0338  0.0760  0.0739  443 HOH   A O   
6608 O  O   . HOH   G .   ? 0.3737 0.2628 0.1916 -0.0862 0.0277  0.0402  444 HOH   A O   
6609 O  O   . HOH   G .   ? 0.2924 0.3162 0.4882 0.0073  0.1010  -0.0930 445 HOH   A O   
6610 O  O   . HOH   G .   ? 0.4876 0.6143 0.5275 -0.0388 0.0959  0.2719  446 HOH   A O   
6611 O  O   . HOH   G .   ? 0.2615 0.1651 0.2852 0.0080  -0.0026 0.0152  447 HOH   A O   
6612 O  O   A HOH   G .   ? 0.1885 0.1516 0.2201 0.0293  -0.0707 -0.0316 448 HOH   A O   
6613 O  O   A HOH   G .   ? 0.6294 0.7047 0.3929 -0.0443 -0.1124 0.0821  449 HOH   A O   
6614 O  O   . HOH   G .   ? 0.3808 0.3609 0.3087 0.2192  -0.0152 -0.0077 450 HOH   A O   
6615 O  O   B HOH   G .   ? 0.3283 0.1679 0.4008 -0.0994 -0.0820 0.0420  451 HOH   A O   
6616 O  O   A HOH   G .   ? 0.3204 0.3794 0.3989 -0.0508 -0.0647 -0.1116 452 HOH   A O   
6617 O  O   . HOH   G .   ? 0.5588 0.4340 0.6878 0.0909  0.0248  -0.1185 453 HOH   A O   
6618 O  O   B HOH   G .   ? 0.3031 0.2857 0.3429 0.0673  -0.0429 -0.0165 454 HOH   A O   
6619 O  O   B HOH   G .   ? 0.2799 0.1615 0.2385 -0.0589 -0.0338 0.0028  455 HOH   A O   
6620 O  O   . HOH   G .   ? 0.2123 0.2551 0.2582 0.0016  -0.0159 -0.0497 456 HOH   A O   
6621 O  O   . HOH   G .   ? 0.2286 0.2019 0.2889 0.0104  0.0206  0.0231  457 HOH   A O   
6622 O  O   . HOH   G .   ? 0.6195 0.7353 0.4817 -0.0333 0.1720  0.1546  458 HOH   A O   
6623 O  O   . HOH   G .   ? 0.5100 0.3684 0.3837 -0.0118 0.0352  0.1067  459 HOH   A O   
6624 O  O   A HOH   G .   ? 0.3610 0.1694 0.2870 0.0422  0.0256  0.0707  460 HOH   A O   
6625 O  O   . HOH   G .   ? 0.5019 0.4455 0.4730 0.0696  0.0018  0.1008  461 HOH   A O   
6626 O  O   . HOH   G .   ? 0.4470 0.3283 0.4333 0.0313  0.0722  0.0370  462 HOH   A O   
6627 O  O   . HOH   G .   ? 0.2582 0.2730 0.3609 0.0493  -0.0361 0.0328  463 HOH   A O   
6628 O  O   . HOH   G .   ? 0.7073 0.5865 0.4820 -0.0832 0.1305  0.0940  464 HOH   A O   
6629 O  O   . HOH   G .   ? 0.3219 0.2716 0.3303 -0.0692 0.0175  -0.0548 465 HOH   A O   
6630 O  O   . HOH   G .   ? 0.7612 0.7834 0.5079 0.0107  -0.1182 0.0487  466 HOH   A O   
6631 O  O   . HOH   G .   ? 0.3205 0.4704 0.5318 -0.1613 0.0961  -0.1525 467 HOH   A O   
6632 O  O   . HOH   G .   ? 0.6613 0.7900 0.6255 0.1003  -0.1135 0.0398  468 HOH   A O   
6633 O  O   . HOH   G .   ? 0.2747 0.2418 0.5900 0.0427  -0.1080 -0.0199 469 HOH   A O   
6634 O  O   . HOH   G .   ? 0.6551 0.5523 0.6249 0.1319  0.2409  0.2592  470 HOH   A O   
6635 O  O   . HOH   G .   ? 0.3593 0.4893 0.5114 0.0912  0.0040  0.1440  471 HOH   A O   
6636 O  O   . HOH   G .   ? 0.2971 0.4083 0.4305 -0.0522 -0.0207 0.0107  472 HOH   A O   
6637 O  O   . HOH   G .   ? 0.6273 0.3369 0.8342 0.0284  0.0297  0.2462  473 HOH   A O   
6638 O  O   . HOH   G .   ? 0.2705 0.1752 0.2549 0.0324  -0.0828 -0.0202 474 HOH   A O   
6639 O  O   . HOH   G .   ? 0.2619 0.3994 0.6117 0.0602  0.0108  -0.1732 475 HOH   A O   
6640 O  O   . HOH   G .   ? 0.2385 0.2495 0.3561 -0.0697 0.0368  -0.0147 476 HOH   A O   
6641 O  O   . HOH   G .   ? 0.4287 0.5656 0.3725 0.0496  -0.0653 -0.0715 477 HOH   A O   
6642 O  O   . HOH   G .   ? 0.3852 0.6096 0.4001 -0.0954 -0.0928 0.2288  478 HOH   A O   
6643 O  O   . HOH   G .   ? 0.5837 0.4690 0.4689 0.0255  0.1340  0.0557  479 HOH   A O   
6644 O  O   . HOH   G .   ? 0.3194 0.2375 0.3856 0.0080  0.0928  0.0220  480 HOH   A O   
6645 O  O   . HOH   G .   ? 0.2451 0.2302 0.2653 0.0296  0.0018  0.0165  481 HOH   A O   
6646 O  O   . HOH   G .   ? 0.5453 0.5797 0.5748 -0.1582 -0.1343 0.0472  482 HOH   A O   
6647 O  O   . HOH   G .   ? 0.4430 0.5565 0.5095 0.0830  -0.0445 -0.0524 483 HOH   A O   
6648 O  O   . HOH   G .   ? 0.4465 0.4791 0.4886 -0.1919 -0.0397 -0.0255 484 HOH   A O   
6649 O  O   . HOH   G .   ? 0.6468 0.5557 0.5053 -0.0781 -0.1194 -0.0956 485 HOH   A O   
6650 O  O   . HOH   G .   ? 0.6869 0.5244 0.6494 -0.1239 0.0624  -0.1052 486 HOH   A O   
6651 O  O   . HOH   G .   ? 0.6272 0.4093 0.4151 0.0065  -0.0280 -0.1210 487 HOH   A O   
6652 O  O   . HOH   G .   ? 0.4531 0.4680 0.3463 -0.0468 -0.0564 -0.0208 488 HOH   A O   
6653 O  O   . HOH   G .   ? 0.7888 0.3905 0.3411 -0.0580 -0.1273 0.0001  489 HOH   A O   
6654 O  O   . HOH   G .   ? 0.4733 0.2672 0.3239 -0.0596 -0.1110 0.0737  490 HOH   A O   
6655 O  O   . HOH   G .   ? 0.3989 0.5228 0.2836 -0.0272 -0.0327 -0.0057 491 HOH   A O   
6656 O  O   . HOH   G .   ? 0.6761 0.4018 0.4231 -0.0401 0.1597  -0.0229 492 HOH   A O   
6657 O  O   . HOH   G .   ? 0.4553 0.3673 0.2726 -0.1137 0.1239  -0.0627 493 HOH   A O   
6658 O  O   . HOH   G .   ? 0.6337 0.6213 0.7428 0.1289  0.2584  -0.1007 494 HOH   A O   
6659 O  O   . HOH   G .   ? 0.2716 0.5711 0.4178 0.1486  0.1127  0.2739  495 HOH   A O   
6660 O  O   . HOH   G .   ? 0.2753 0.2250 0.6026 0.0247  0.0632  0.0993  496 HOH   A O   
6661 O  O   . HOH   G .   ? 0.2956 0.3899 0.5200 0.0255  0.1515  0.0979  497 HOH   A O   
6662 O  O   . HOH   G .   ? 0.5127 0.5090 0.5365 0.0092  -0.1243 0.0617  498 HOH   A O   
6663 O  O   . HOH   G .   ? 0.2635 0.2385 0.6943 -0.0080 -0.1047 0.0240  499 HOH   A O   
6664 O  O   . HOH   G .   ? 0.5480 0.4951 0.4423 -0.0258 -0.0745 -0.0221 500 HOH   A O   
6665 O  O   . HOH   G .   ? 0.5148 0.3191 0.4266 -0.0021 0.2164  0.0344  501 HOH   A O   
6666 O  O   . HOH   G .   ? 0.3893 0.3292 0.4807 -0.0994 0.0638  0.0773  502 HOH   A O   
6667 O  O   . HOH   G .   ? 0.6620 0.7089 0.4972 0.2049  -0.1473 0.0023  503 HOH   A O   
6668 O  O   . HOH   G .   ? 0.2377 0.2873 0.5192 -0.0001 0.0964  -0.0396 504 HOH   A O   
6669 O  O   . HOH   G .   ? 0.3985 0.8632 0.6161 -0.1154 -0.0880 0.2273  505 HOH   A O   
6670 O  O   B HOH   G .   ? 0.3857 0.4353 0.4041 -0.1368 0.0885  -0.0004 506 HOH   A O   
6671 O  O   B HOH   G .   ? 0.2587 0.3574 0.2810 0.0545  0.0285  0.0361  507 HOH   A O   
6672 O  O   . HOH   G .   ? 0.2671 0.3347 0.3453 0.0806  -0.0694 0.0275  508 HOH   A O   
6673 O  O   . HOH   G .   ? 0.4694 0.2670 0.4049 -0.1438 -0.0160 0.0457  509 HOH   A O   
6674 O  O   . HOH   G .   ? 0.3137 0.4767 0.3118 -0.0388 -0.0234 -0.0673 510 HOH   A O   
6675 O  O   B HOH   G .   ? 0.3404 0.4557 0.3032 -0.0136 -0.0317 0.0174  511 HOH   A O   
6676 O  O   . HOH   G .   ? 0.2882 0.3866 0.4551 0.0210  -0.0632 0.0371  512 HOH   A O   
6677 O  O   . HOH   G .   ? 0.6745 0.2482 0.4598 -0.0386 0.0691  0.0523  513 HOH   A O   
6678 O  O   . HOH   G .   ? 0.5882 0.7683 0.5243 0.1503  -0.1164 0.0801  514 HOH   A O   
6679 O  O   . HOH   G .   ? 0.7783 0.4654 0.5754 -0.0848 -0.0180 0.0903  515 HOH   A O   
6680 O  O   . HOH   G .   ? 0.4728 0.6962 0.4955 0.3018  -0.0187 0.1270  516 HOH   A O   
6681 O  O   . HOH   G .   ? 0.2788 0.2245 0.4223 0.0057  0.0268  0.0323  517 HOH   A O   
6682 O  O   . HOH   G .   ? 0.5088 0.6125 0.4667 -0.0029 -0.1098 -0.1116 518 HOH   A O   
6683 O  O   A HOH   G .   ? 0.4208 0.6179 0.2140 0.0588  0.0755  0.0556  519 HOH   A O   
6684 O  O   . HOH   G .   ? 0.2905 0.7121 0.3842 0.0478  0.0141  -0.0497 520 HOH   A O   
6685 O  O   B HOH   G .   ? 0.3224 0.2721 0.3217 0.0093  0.0717  0.0866  521 HOH   A O   
6686 O  O   . HOH   G .   ? 0.4562 0.7170 0.5677 -0.0723 -0.0845 0.0355  522 HOH   A O   
6687 O  O   . HOH   G .   ? 0.4994 0.5301 0.4395 0.2262  0.0152  0.1096  523 HOH   A O   
6688 O  O   . HOH   G .   ? 0.3369 0.4537 0.5655 -0.0196 -0.1121 0.2748  524 HOH   A O   
6689 O  O   . HOH   H .   ? 0.2337 0.2183 0.3211 0.0189  0.0872  0.0467  201 HOH   B O   
6690 O  O   . HOH   H .   ? 0.3639 0.4319 0.5229 -0.1040 0.0776  -0.1388 202 HOH   B O   
6691 O  O   . HOH   H .   ? 0.4630 0.3613 0.3522 -0.0510 0.0269  -0.1288 203 HOH   B O   
6692 O  O   . HOH   H .   ? 0.3304 0.5315 0.5033 -0.0071 0.1848  -0.1775 204 HOH   B O   
6693 O  O   . HOH   H .   ? 0.3157 0.3884 0.6520 -0.0473 0.0307  -0.0559 205 HOH   B O   
6694 O  O   . HOH   H .   ? 0.5179 0.5101 0.2907 0.0440  -0.0607 -0.1506 206 HOH   B O   
6695 O  O   . HOH   H .   ? 0.6869 0.3386 0.4830 0.0724  0.1092  0.0343  207 HOH   B O   
6696 O  O   . HOH   H .   ? 0.2993 0.7204 0.4349 0.1268  0.0331  0.2715  208 HOH   B O   
6697 O  O   . HOH   H .   ? 0.5051 0.5875 0.3851 0.2889  -0.1305 -0.0353 209 HOH   B O   
6698 O  O   . HOH   H .   ? 0.4782 0.4120 0.6524 0.0128  -0.1192 0.2708  210 HOH   B O   
6699 O  O   . HOH   H .   ? 0.2202 0.2317 0.2864 0.0188  -0.0054 -0.0516 211 HOH   B O   
6700 O  O   . HOH   H .   ? 0.4211 0.5203 0.4276 0.2427  -0.0417 0.0247  212 HOH   B O   
6701 O  O   . HOH   H .   ? 0.3719 0.5143 0.4893 0.2211  0.0289  -0.0699 213 HOH   B O   
6702 O  O   . HOH   H .   ? 0.6725 0.6856 0.5867 0.2354  0.0640  0.0249  214 HOH   B O   
6703 O  O   . HOH   H .   ? 0.4402 0.3673 0.3709 0.0172  -0.1156 0.0570  215 HOH   B O   
6704 O  O   . HOH   H .   ? 0.2818 0.2880 0.6381 0.0671  -0.1144 0.0348  216 HOH   B O   
6705 O  O   . HOH   H .   ? 0.3155 0.2037 0.5717 0.0197  0.2054  0.0794  217 HOH   B O   
6706 O  O   . HOH   H .   ? 0.1546 0.1960 0.2903 -0.0127 -0.0074 0.0076  218 HOH   B O   
6707 O  O   . HOH   H .   ? 0.4287 0.4326 0.6969 -0.0689 -0.1525 -0.1201 219 HOH   B O   
6708 O  O   . HOH   H .   ? 0.1824 0.2055 0.2995 -0.0247 0.0037  -0.0119 220 HOH   B O   
6709 O  O   . HOH   H .   ? 0.3876 0.3315 0.6611 0.0469  0.0511  -0.0301 221 HOH   B O   
6710 O  O   . HOH   H .   ? 0.4842 0.1950 0.2930 -0.0252 -0.0827 0.0085  222 HOH   B O   
6711 O  O   . HOH   H .   ? 0.7355 0.4982 0.4683 0.1780  -0.0161 -0.1254 223 HOH   B O   
6712 O  O   . HOH   H .   ? 0.3880 0.3767 0.4088 0.0385  -0.0753 -0.0043 224 HOH   B O   
6713 O  O   . HOH   H .   ? 0.2086 0.2119 0.4086 -0.0350 -0.0003 -0.0632 225 HOH   B O   
6714 O  O   . HOH   H .   ? 0.4167 0.4536 0.4122 0.0266  0.0702  -0.1486 226 HOH   B O   
6715 O  O   . HOH   H .   ? 0.2394 0.1767 0.2910 -0.0275 0.0946  0.0049  227 HOH   B O   
6716 O  O   . HOH   H .   ? 0.3133 0.2167 0.4693 0.0084  0.1614  0.0341  228 HOH   B O   
6717 O  O   . HOH   H .   ? 0.5977 0.2938 0.3935 -0.1943 0.0176  -0.0063 229 HOH   B O   
6718 O  O   . HOH   H .   ? 0.4569 0.7233 0.3578 0.2715  0.0227  0.0245  230 HOH   B O   
6719 O  O   . HOH   H .   ? 0.3932 0.4125 0.5690 -0.1596 0.0143  0.1079  231 HOH   B O   
6720 O  O   . HOH   H .   ? 0.3610 0.3238 0.2107 0.0328  0.0690  0.0459  232 HOH   B O   
6721 O  O   . HOH   H .   ? 0.2683 0.3512 0.3264 -0.0802 0.0435  -0.0072 233 HOH   B O   
6722 O  O   . HOH   H .   ? 0.2720 0.2522 0.2964 0.0364  0.0171  -0.0733 234 HOH   B O   
6723 O  O   . HOH   H .   ? 0.6300 0.5951 0.3148 0.0229  -0.0234 0.0482  235 HOH   B O   
6724 O  O   . HOH   H .   ? 0.2069 0.1285 0.3567 0.0073  -0.0546 -0.0209 236 HOH   B O   
6725 O  O   . HOH   H .   ? 0.3487 0.2618 0.3159 -0.0531 0.0156  -0.0651 237 HOH   B O   
6726 O  O   . HOH   H .   ? 0.2197 0.3760 0.3230 -0.0614 -0.0611 -0.0349 238 HOH   B O   
6727 O  O   . HOH   H .   ? 0.2127 0.2552 0.3167 -0.0542 0.0038  -0.0287 239 HOH   B O   
6728 O  O   . HOH   H .   ? 0.3363 0.1754 0.2276 0.0191  -0.0721 -0.0104 240 HOH   B O   
6729 O  O   . HOH   H .   ? 0.3701 0.2678 0.4074 0.0704  -0.1116 -0.1349 241 HOH   B O   
6730 O  O   . HOH   H .   ? 0.1475 0.1406 0.1589 -0.0102 -0.0025 -0.0024 242 HOH   B O   
6731 O  O   . HOH   H .   ? 0.1443 0.1350 0.1741 -0.0044 -0.0086 0.0082  243 HOH   B O   
6732 O  O   . HOH   H .   ? 0.2997 0.1806 0.6507 -0.0047 -0.1139 -0.0513 244 HOH   B O   
6733 O  O   . HOH   H .   ? 0.5202 0.3216 0.3878 -0.2302 0.0118  0.0187  245 HOH   B O   
6734 O  O   . HOH   H .   ? 0.1523 0.1447 0.2810 -0.0048 0.0105  -0.0135 246 HOH   B O   
6735 O  O   . HOH   H .   ? 0.3823 0.2691 0.3964 0.0913  -0.0368 -0.0639 247 HOH   B O   
6736 O  O   . HOH   H .   ? 0.1944 0.3972 0.2490 -0.0339 -0.0060 0.0542  248 HOH   B O   
6737 O  O   . HOH   H .   ? 0.3292 0.3804 0.2096 0.0343  0.0689  0.0154  249 HOH   B O   
6738 O  O   . HOH   H .   ? 0.2915 0.2250 0.3039 0.0844  0.0909  0.0079  250 HOH   B O   
6739 O  O   . HOH   H .   ? 0.6010 0.3251 0.2783 -0.0233 0.1107  -0.0300 251 HOH   B O   
6740 O  O   . HOH   H .   ? 0.2108 0.1988 0.2261 -0.0338 -0.0425 0.0219  252 HOH   B O   
6741 O  O   . HOH   H .   ? 0.2234 0.1870 0.4034 -0.0008 -0.0453 -0.0276 253 HOH   B O   
6742 O  O   . HOH   H .   ? 0.1635 0.1662 0.3105 -0.0243 -0.0283 0.0170  254 HOH   B O   
6743 O  O   . HOH   H .   ? 0.2243 0.3106 0.2210 -0.0414 0.0142  0.0395  255 HOH   B O   
6744 O  O   . HOH   H .   ? 0.2582 0.2211 0.1976 0.0197  -0.0123 -0.0000 256 HOH   B O   
6745 O  O   . HOH   H .   ? 0.3349 0.4508 0.3973 -0.0257 -0.1114 0.1421  257 HOH   B O   
6746 O  O   . HOH   H .   ? 0.2225 0.1519 0.2121 -0.0338 -0.0462 0.0318  258 HOH   B O   
6747 O  O   . HOH   H .   ? 0.2151 0.4055 0.5316 -0.0480 -0.0375 -0.1464 259 HOH   B O   
6748 O  O   . HOH   H .   ? 0.2640 0.5644 0.5598 0.1552  -0.0863 -0.0855 260 HOH   B O   
6749 O  O   . HOH   H .   ? 0.1337 0.1646 0.2082 -0.0060 0.0091  0.0172  261 HOH   B O   
6750 O  O   . HOH   H .   ? 0.2303 0.2228 0.2629 0.0765  -0.0770 -0.0636 262 HOH   B O   
6751 O  O   . HOH   H .   ? 0.2483 0.4337 0.6213 -0.0072 -0.0338 -0.1423 263 HOH   B O   
6752 O  O   . HOH   H .   ? 0.4117 0.3111 0.4724 -0.0210 -0.1148 -0.0646 264 HOH   B O   
6753 O  O   . HOH   H .   ? 0.2279 0.1999 0.2314 0.0109  -0.0131 0.0001  265 HOH   B O   
6754 O  O   . HOH   H .   ? 0.2912 0.4625 0.3399 -0.1022 -0.0440 -0.0825 266 HOH   B O   
6755 O  O   . HOH   H .   ? 0.2024 0.1554 0.2258 -0.0297 -0.0199 0.0142  267 HOH   B O   
6756 O  O   . HOH   H .   ? 0.4376 0.3529 0.3987 -0.0973 0.0823  -0.0859 268 HOH   B O   
6757 O  O   . HOH   H .   ? 0.2419 0.1972 0.2834 -0.0646 0.0170  -0.0121 269 HOH   B O   
6758 O  O   . HOH   H .   ? 0.2460 0.2508 0.2381 -0.0454 -0.0716 -0.0273 270 HOH   B O   
6759 O  O   . HOH   H .   ? 0.1836 0.2673 0.2756 0.0501  0.0514  0.0919  271 HOH   B O   
6760 O  O   . HOH   H .   ? 0.2539 0.2675 0.2600 -0.0411 -0.0819 0.0233  272 HOH   B O   
6761 O  O   . HOH   H .   ? 0.2704 0.2136 0.5025 0.0178  0.0396  0.0674  273 HOH   B O   
6762 O  O   . HOH   H .   ? 0.2279 0.3016 0.2308 0.0727  -0.0209 -0.0102 274 HOH   B O   
6763 O  O   . HOH   H .   ? 0.1880 0.1811 0.1732 -0.0445 -0.0416 0.0110  275 HOH   B O   
6764 O  O   . HOH   H .   ? 0.3447 0.3592 0.4948 0.1232  -0.0687 -0.0875 276 HOH   B O   
6765 O  O   . HOH   H .   ? 0.2452 0.4141 0.3725 0.0139  0.1029  0.0030  277 HOH   B O   
6766 O  O   . HOH   H .   ? 0.2389 0.4242 0.2890 -0.0581 0.0458  -0.1464 278 HOH   B O   
6767 O  O   . HOH   H .   ? 0.1825 0.1403 0.4225 -0.0105 -0.0367 -0.0070 279 HOH   B O   
6768 O  O   . HOH   H .   ? 0.4371 0.3894 0.4975 -0.0214 0.0167  0.0589  280 HOH   B O   
6769 O  O   . HOH   H .   ? 0.4318 0.4602 0.4569 -0.0081 -0.1389 0.0093  281 HOH   B O   
6770 O  O   . HOH   H .   ? 0.2722 0.4625 0.4651 -0.0963 -0.1262 0.0875  282 HOH   B O   
6771 O  O   . HOH   H .   ? 0.1611 0.1577 0.3481 -0.0121 0.0066  -0.0086 283 HOH   B O   
6772 O  O   . HOH   H .   ? 0.4591 0.3743 0.2943 0.0297  0.0098  -0.1025 284 HOH   B O   
6773 O  O   . HOH   H .   ? 0.1664 0.1513 0.1936 -0.0038 0.0110  0.0001  285 HOH   B O   
6774 O  O   . HOH   H .   ? 0.1560 0.2049 0.1630 -0.0122 -0.0202 0.0114  286 HOH   B O   
6775 O  O   . HOH   H .   ? 0.3016 0.7633 0.7537 0.1234  -0.1063 -0.0924 287 HOH   B O   
6776 O  O   . HOH   H .   ? 0.3852 0.2270 0.4010 -0.1037 -0.2186 0.0835  288 HOH   B O   
6777 O  O   . HOH   H .   ? 0.1711 0.3167 0.5020 0.0250  0.0016  -0.1417 289 HOH   B O   
6778 O  O   . HOH   H .   ? 0.1670 0.2040 0.3006 0.0202  -0.0207 0.0117  290 HOH   B O   
6779 O  O   . HOH   H .   ? 0.2414 0.2684 0.2904 0.0054  -0.0769 0.0280  291 HOH   B O   
6780 O  O   . HOH   H .   ? 0.5174 0.6696 0.2480 -0.0593 -0.1116 0.1257  292 HOH   B O   
6781 O  O   . HOH   H .   ? 0.4232 0.5084 0.2303 0.0074  0.0712  0.0811  293 HOH   B O   
6782 O  O   . HOH   H .   ? 0.1766 0.1646 0.2494 0.0119  0.0112  0.0143  294 HOH   B O   
6783 O  O   . HOH   H .   ? 0.3399 0.2865 0.2898 -0.0315 0.0222  -0.1227 295 HOH   B O   
6784 O  O   . HOH   H .   ? 0.3759 0.7218 0.3369 0.1629  -0.0942 0.0664  296 HOH   B O   
6785 O  O   . HOH   H .   ? 0.2084 0.2726 0.6006 0.0429  -0.0596 -0.1396 297 HOH   B O   
6786 O  O   . HOH   H .   ? 0.3173 0.2801 0.5152 -0.0088 -0.0758 0.1132  298 HOH   B O   
6787 O  O   . HOH   H .   ? 0.3373 0.3849 0.3883 -0.1630 0.1031  -0.0492 299 HOH   B O   
6788 O  O   . HOH   H .   ? 0.4359 0.3805 0.2437 0.1210  -0.0748 0.0491  300 HOH   B O   
6789 O  O   . HOH   H .   ? 0.3436 0.2720 0.2174 0.0212  -0.0776 -0.0066 301 HOH   B O   
6790 O  O   . HOH   H .   ? 0.2480 0.7006 0.2499 0.0806  -0.0386 -0.0438 302 HOH   B O   
6791 O  O   . HOH   H .   ? 0.2103 0.1561 0.3482 0.0289  -0.1006 0.0036  303 HOH   B O   
6792 O  O   . HOH   H .   ? 0.2556 0.3790 0.4472 -0.0567 -0.1409 0.1334  304 HOH   B O   
6793 O  O   . HOH   H .   ? 0.1577 0.1481 0.3263 0.0036  -0.0021 0.0017  305 HOH   B O   
6794 O  O   . HOH   H .   ? 0.2310 0.3247 0.5046 -0.0139 -0.0855 -0.0421 306 HOH   B O   
6795 O  O   . HOH   H .   ? 0.5923 0.3932 0.3172 0.2707  0.1085  0.0786  307 HOH   B O   
6796 O  O   . HOH   H .   ? 0.4403 0.3365 0.5309 -0.0884 0.0232  0.1434  308 HOH   B O   
6797 O  O   . HOH   H .   ? 0.1590 0.1881 0.3088 -0.0245 -0.0025 0.0067  309 HOH   B O   
6798 O  O   . HOH   H .   ? 0.2052 0.1647 0.2843 -0.0280 -0.0305 -0.0002 310 HOH   B O   
6799 O  O   . HOH   H .   ? 0.5002 0.3016 0.2400 -0.1667 0.0835  -0.0303 311 HOH   B O   
6800 O  O   . HOH   H .   ? 0.2760 0.2890 0.3438 -0.0384 0.0908  -0.0867 312 HOH   B O   
6801 O  O   . HOH   H .   ? 0.3081 0.3656 0.8083 -0.0338 -0.0889 0.1773  313 HOH   B O   
6802 O  O   . HOH   H .   ? 0.3442 0.1905 0.3448 0.0700  0.1022  0.0415  314 HOH   B O   
6803 O  O   . HOH   H .   ? 0.2441 0.1503 0.2618 -0.0197 -0.0214 0.0269  315 HOH   B O   
6804 O  O   . HOH   H .   ? 0.5792 0.5842 0.5660 -0.1120 -0.0141 0.1887  316 HOH   B O   
6805 O  O   . HOH   H .   ? 0.4171 0.2206 0.2655 0.1450  0.0917  0.0330  317 HOH   B O   
6806 O  O   . HOH   H .   ? 0.2170 0.6317 0.5306 -0.0524 0.0210  -0.0019 318 HOH   B O   
6807 O  O   . HOH   H .   ? 0.6435 0.6213 0.4701 0.3074  0.0045  -0.0077 319 HOH   B O   
6808 O  O   . HOH   H .   ? 0.2177 0.1912 0.2041 -0.0031 0.0235  0.0242  320 HOH   B O   
6809 O  O   . HOH   H .   ? 0.4902 0.4067 0.2697 0.0054  -0.0528 -0.0680 321 HOH   B O   
6810 O  O   . HOH   H .   ? 0.1637 0.2928 0.2455 -0.0170 -0.0193 0.0904  322 HOH   B O   
6811 O  O   . HOH   H .   ? 0.1557 0.1670 0.2983 -0.0136 -0.0126 -0.0182 323 HOH   B O   
6812 O  O   . HOH   H .   ? 0.6085 0.4396 0.5990 0.0850  0.1781  0.0230  324 HOH   B O   
6813 O  O   . HOH   H .   ? 0.4956 0.4222 0.2450 0.1667  -0.1176 -0.0482 325 HOH   B O   
6814 O  O   . HOH   H .   ? 0.4049 0.4285 0.6226 0.0473  -0.0138 0.0886  326 HOH   B O   
6815 O  O   . HOH   H .   ? 0.3220 0.2176 0.2492 0.0257  -0.0372 0.0250  327 HOH   B O   
6816 O  O   . HOH   H .   ? 0.4720 0.2613 0.2885 0.0389  0.0596  0.0936  328 HOH   B O   
6817 O  O   . HOH   H .   ? 0.7811 0.2083 0.3105 0.0339  -0.0909 -0.0067 329 HOH   B O   
6818 O  O   . HOH   H .   ? 0.1945 0.2804 0.3242 0.0383  -0.0091 -0.0739 330 HOH   B O   
6819 O  O   . HOH   H .   ? 0.1906 0.1967 0.2782 0.0285  0.0479  0.0243  331 HOH   B O   
6820 O  O   . HOH   H .   ? 0.5777 0.3552 0.3572 0.0304  0.1053  0.1084  332 HOH   B O   
6821 O  O   . HOH   H .   ? 0.4540 0.3117 0.5496 0.1092  0.2275  0.1675  333 HOH   B O   
6822 O  O   . HOH   H .   ? 0.2636 0.2081 0.5110 -0.0004 0.0184  0.0252  334 HOH   B O   
6823 O  O   . HOH   H .   ? 0.4910 0.5215 0.3270 0.0132  -0.1066 0.0103  335 HOH   B O   
6824 O  O   . HOH   H .   ? 0.5554 0.4895 0.6940 0.1208  -0.0611 0.2346  336 HOH   B O   
6825 O  O   . HOH   H .   ? 0.1677 0.1477 0.2485 0.0029  -0.0174 0.0054  337 HOH   B O   
6826 O  O   . HOH   H .   ? 0.2218 0.2537 0.5607 -0.0509 0.0014  0.1524  338 HOH   B O   
6827 O  O   . HOH   H .   ? 0.5668 0.4649 0.6253 -0.0781 -0.0756 -0.1280 339 HOH   B O   
6828 O  O   . HOH   H .   ? 0.5118 0.3859 0.3134 0.0823  -0.1380 -0.0887 340 HOH   B O   
6829 O  O   . HOH   H .   ? 0.4186 0.6402 0.3951 -0.0149 -0.0590 0.1701  341 HOH   B O   
6830 O  O   . HOH   H .   ? 0.5361 0.3499 0.4041 -0.0123 0.0832  -0.1595 342 HOH   B O   
6831 O  O   . HOH   H .   ? 0.4085 0.6217 0.3742 -0.1067 -0.0654 -0.0616 343 HOH   B O   
6832 O  O   . HOH   H .   ? 0.7104 0.7175 0.2855 0.0512  -0.0242 0.1724  344 HOH   B O   
6833 O  O   . HOH   H .   ? 0.2456 0.5892 0.6477 -0.0154 0.0016  0.0370  345 HOH   B O   
6834 O  O   . HOH   H .   ? 0.2065 0.2006 0.3139 -0.0005 0.0643  0.0135  346 HOH   B O   
6835 O  O   . HOH   H .   ? 0.4304 0.5731 0.5175 0.0035  -0.1017 0.0361  347 HOH   B O   
6836 O  O   . HOH   H .   ? 0.4915 0.5554 0.4699 -0.1141 0.0101  0.1021  348 HOH   B O   
6837 O  O   . HOH   H .   ? 0.2779 0.2204 0.4968 -0.0381 -0.0724 -0.0413 349 HOH   B O   
6838 O  O   . HOH   H .   ? 0.4069 0.2160 0.3147 -0.0734 0.0257  -0.0675 350 HOH   B O   
6839 O  O   . HOH   H .   ? 0.3017 0.1881 0.3863 0.0247  -0.1201 -0.0442 351 HOH   B O   
6840 O  O   . HOH   H .   ? 0.2164 0.4228 0.5043 0.0560  0.0289  0.0291  352 HOH   B O   
6841 O  O   . HOH   H .   ? 0.2334 0.6088 0.4308 0.1429  -0.0480 -0.1536 353 HOH   B O   
6842 O  O   . HOH   H .   ? 0.4592 0.6704 0.6884 0.0811  0.0040  -0.0294 354 HOH   B O   
6843 O  O   . HOH   H .   ? 0.4655 0.2934 0.5455 -0.1053 0.1381  0.0553  355 HOH   B O   
6844 O  O   . HOH   H .   ? 0.3493 0.4455 0.5050 -0.1547 0.0057  -0.0522 356 HOH   B O   
6845 O  O   . HOH   H .   ? 0.3888 0.2915 0.3765 -0.0949 -0.0158 -0.0924 357 HOH   B O   
6846 O  O   . HOH   H .   ? 0.4889 0.5362 0.4599 0.2116  -0.1227 0.1186  358 HOH   B O   
6847 O  O   . HOH   H .   ? 0.5098 0.3493 0.4111 0.0556  0.1172  -0.0412 359 HOH   B O   
6848 O  O   . HOH   H .   ? 0.5744 0.4633 0.5035 -0.0741 0.0157  0.0095  360 HOH   B O   
6849 O  O   . HOH   H .   ? 0.5470 0.3484 0.4676 -0.0221 -0.1507 -0.0423 361 HOH   B O   
6850 O  O   . HOH   H .   ? 0.5133 0.4112 0.6240 0.0470  0.0841  0.1136  362 HOH   B O   
6851 O  O   . HOH   H .   ? 0.4487 0.6799 0.2869 0.2337  -0.0463 0.0180  363 HOH   B O   
6852 O  O   . HOH   H .   ? 0.2177 0.3941 0.6670 -0.0851 -0.0463 -0.0795 364 HOH   B O   
6853 O  O   . HOH   H .   ? 0.5332 0.3031 0.4971 -0.1276 -0.0592 0.0494  365 HOH   B O   
6854 O  O   . HOH   H .   ? 0.6492 0.4371 0.3954 0.1086  0.0582  0.0424  366 HOH   B O   
6855 O  O   . HOH   H .   ? 0.5659 0.3627 0.5104 0.1202  -0.1608 0.0389  367 HOH   B O   
6856 O  O   . HOH   H .   ? 0.6261 0.2154 0.4248 -0.0084 0.0036  0.0745  368 HOH   B O   
6857 O  O   . HOH   H .   ? 0.5859 0.5993 0.3106 0.1538  -0.1631 0.0733  369 HOH   B O   
6858 O  O   . HOH   H .   ? 0.4177 0.5625 0.5274 0.2532  0.1170  0.1206  370 HOH   B O   
6859 O  O   . HOH   H .   ? 0.7828 0.7245 0.4879 0.2850  -0.1221 0.1135  371 HOH   B O   
6860 O  O   . HOH   H .   ? 0.5703 0.5258 0.4092 -0.0581 -0.0760 -0.1029 372 HOH   B O   
6861 O  O   . HOH   H .   ? 0.4085 0.3160 0.3915 0.0664  -0.1415 -0.0456 373 HOH   B O   
6862 O  O   . HOH   H .   ? 0.6489 0.3991 0.2766 -0.0690 -0.1094 -0.0568 374 HOH   B O   
6863 O  O   . HOH   H .   ? 0.4721 0.4885 0.4337 -0.0754 -0.0776 0.0276  375 HOH   B O   
6864 O  O   . HOH   H .   ? 0.3815 0.4878 0.2337 0.0330  0.0457  0.0285  376 HOH   B O   
6865 O  O   . HOH   H .   ? 0.4890 0.6842 0.6210 0.1724  0.0756  0.2896  377 HOH   B O   
6866 O  O   . HOH   H .   ? 0.6635 0.3692 0.5039 -0.0939 -0.0892 -0.0154 378 HOH   B O   
6867 O  O   . HOH   H .   ? 0.2289 0.3845 0.4793 0.0212  -0.0837 -0.0433 379 HOH   B O   
6868 O  O   . HOH   H .   ? 0.5502 0.6818 0.3797 -0.1338 -0.0099 -0.1476 380 HOH   B O   
6869 O  O   . HOH   H .   ? 0.3330 0.5310 0.5487 0.1008  -0.0220 0.0593  381 HOH   B O   
6870 O  O   . HOH   H .   ? 0.2881 0.2652 0.3213 0.0072  0.0148  0.0192  382 HOH   B O   
6871 O  O   . HOH   H .   ? 0.4527 0.9150 0.5772 0.0810  0.2325  0.1395  383 HOH   B O   
6872 O  O   . HOH   H .   ? 0.5695 0.6922 0.6467 0.0408  0.2673  0.1943  384 HOH   B O   
6873 O  O   . HOH   H .   ? 0.7286 0.5837 0.3814 0.2565  0.0755  0.0095  385 HOH   B O   
6874 O  O   . HOH   H .   ? 0.6777 0.3944 0.4373 0.0602  0.1019  -0.0844 386 HOH   B O   
6875 O  O   . HOH   H .   ? 0.5820 0.4757 0.5104 -0.0877 0.1040  -0.0214 387 HOH   B O   
6876 O  O   . HOH   H .   ? 0.2573 0.4549 0.3567 -0.0916 -0.0964 -0.0371 388 HOH   B O   
6877 O  O   . HOH   H .   ? 0.5034 0.3729 0.3027 0.0301  0.0517  0.0176  389 HOH   B O   
6878 O  O   . HOH   H .   ? 0.3969 0.2258 0.3315 0.0862  -0.0317 0.0207  390 HOH   B O   
6879 O  O   . HOH   H .   ? 0.4932 0.4746 0.4326 0.0737  0.0744  0.0690  391 HOH   B O   
6880 O  O   . HOH   H .   ? 0.4043 0.2254 0.5217 -0.0488 0.0505  0.0509  392 HOH   B O   
6881 O  O   . HOH   H .   ? 0.2506 0.4744 0.6911 -0.1398 -0.0695 0.0079  393 HOH   B O   
6882 O  O   . HOH   H .   ? 0.4255 0.4470 0.4133 0.0176  0.0940  0.0809  394 HOH   B O   
6883 O  O   . HOH   H .   ? 0.5199 0.6378 0.3584 0.2167  -0.0422 -0.0921 395 HOH   B O   
6884 O  O   . HOH   H .   ? 0.3307 0.3977 0.3639 0.0259  0.0146  -0.0745 396 HOH   B O   
6885 O  O   . HOH   H .   ? 0.2240 0.2756 0.6307 -0.0611 -0.1153 0.0181  397 HOH   B O   
6886 O  O   . HOH   H .   ? 0.5569 0.7540 0.6918 0.1795  -0.1154 0.2349  398 HOH   B O   
6887 O  O   . HOH   H .   ? 0.5678 0.4144 0.3064 -0.2277 -0.0341 0.1018  399 HOH   B O   
6888 O  O   . HOH   H .   ? 0.5740 0.6050 0.3745 0.1511  -0.0544 -0.0435 400 HOH   B O   
# 
