data_7HFA
# 
_entry.id   7HFA 
# 
_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   7HFA         pdb_00007hfa 10.2210/pdb7hfa/pdb 
WWPDB D_1001407400 ?            ?                   
# 
_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                        7HFA 
_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 '4-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}thian-4-ol' 278.373   1   ?                      ? ? 
?                                                                                    
3 non-polymer syn 'CHLORIDE ION'                                                          35.453    1   ?                      ? ? 
?                                                                                    
4 water       nat water                                                                   18.015    422 ?                      ? ? 
?                                                                                    
# 
_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 '4-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}thian-4-ol' A1BAW 
3 'CHLORIDE ION'                                                          CL    
4 water                                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   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 
A1BAW non-polymer         . '4-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}thian-4-ol' ? 'C13 H18 N4 O S' 278.373 
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 A1BAW 1   201 201  A1BAW LA1 A . 
D 3 CL    1   202 1    CL    CL  A . 
E 4 HOH   1   301 292  HOH   HOH A . 
E 4 HOH   2   302 1289 HOH   HOH A . 
E 4 HOH   3   303 196  HOH   HOH A . 
E 4 HOH   4   304 625  HOH   HOH A . 
E 4 HOH   5   305 148  HOH   HOH A . 
E 4 HOH   6   306 662  HOH   HOH A . 
E 4 HOH   7   307 86   HOH   HOH A . 
E 4 HOH   8   308 70   HOH   HOH A . 
E 4 HOH   9   309 209  HOH   HOH A . 
E 4 HOH   10  310 109  HOH   HOH A . 
E 4 HOH   11  311 153  HOH   HOH A . 
E 4 HOH   12  312 18   HOH   HOH A . 
E 4 HOH   13  313 229  HOH   HOH A . 
E 4 HOH   14  314 76   HOH   HOH A . 
E 4 HOH   15  315 124  HOH   HOH A . 
E 4 HOH   16  316 36   HOH   HOH A . 
E 4 HOH   17  317 1295 HOH   HOH A . 
E 4 HOH   18  318 236  HOH   HOH A . 
E 4 HOH   19  319 247  HOH   HOH A . 
E 4 HOH   20  320 225  HOH   HOH A . 
E 4 HOH   21  321 192  HOH   HOH A . 
E 4 HOH   22  322 1310 HOH   HOH A . 
E 4 HOH   23  323 15   HOH   HOH A . 
E 4 HOH   24  324 136  HOH   HOH A . 
E 4 HOH   25  325 151  HOH   HOH A . 
E 4 HOH   26  326 337  HOH   HOH A . 
E 4 HOH   27  327 11   HOH   HOH A . 
E 4 HOH   28  328 964  HOH   HOH A . 
E 4 HOH   29  329 140  HOH   HOH A . 
E 4 HOH   30  330 164  HOH   HOH A . 
E 4 HOH   31  331 1283 HOH   HOH A . 
E 4 HOH   32  332 469  HOH   HOH A . 
E 4 HOH   33  333 405  HOH   HOH A . 
E 4 HOH   34  334 57   HOH   HOH A . 
E 4 HOH   35  335 195  HOH   HOH A . 
E 4 HOH   36  336 16   HOH   HOH A . 
E 4 HOH   37  337 139  HOH   HOH A . 
E 4 HOH   38  338 630  HOH   HOH A . 
E 4 HOH   39  339 42   HOH   HOH A . 
E 4 HOH   40  340 105  HOH   HOH A . 
E 4 HOH   41  341 9    HOH   HOH A . 
E 4 HOH   42  342 241  HOH   HOH A . 
E 4 HOH   43  343 49   HOH   HOH A . 
E 4 HOH   44  344 93   HOH   HOH A . 
E 4 HOH   45  345 320  HOH   HOH A . 
E 4 HOH   46  346 3    HOH   HOH A . 
E 4 HOH   47  347 354  HOH   HOH A . 
E 4 HOH   48  348 1    HOH   HOH A . 
E 4 HOH   49  349 17   HOH   HOH A . 
E 4 HOH   50  350 939  HOH   HOH A . 
E 4 HOH   51  351 162  HOH   HOH A . 
E 4 HOH   52  352 393  HOH   HOH A . 
E 4 HOH   53  353 102  HOH   HOH A . 
E 4 HOH   54  354 396  HOH   HOH A . 
E 4 HOH   55  355 66   HOH   HOH A . 
E 4 HOH   56  356 92   HOH   HOH A . 
E 4 HOH   57  357 138  HOH   HOH A . 
E 4 HOH   58  358 26   HOH   HOH A . 
E 4 HOH   59  359 1290 HOH   HOH A . 
E 4 HOH   60  360 56   HOH   HOH A . 
E 4 HOH   61  361 409  HOH   HOH A . 
E 4 HOH   62  362 186  HOH   HOH A . 
E 4 HOH   63  363 45   HOH   HOH A . 
E 4 HOH   64  364 165  HOH   HOH A . 
E 4 HOH   65  365 169  HOH   HOH A . 
E 4 HOH   66  366 155  HOH   HOH A . 
E 4 HOH   67  367 33   HOH   HOH A . 
E 4 HOH   68  368 21   HOH   HOH A . 
E 4 HOH   69  369 2    HOH   HOH A . 
E 4 HOH   70  370 19   HOH   HOH A . 
E 4 HOH   71  371 81   HOH   HOH A . 
E 4 HOH   72  372 5    HOH   HOH A . 
E 4 HOH   73  373 159  HOH   HOH A . 
E 4 HOH   74  374 1300 HOH   HOH A . 
E 4 HOH   75  375 199  HOH   HOH A . 
E 4 HOH   76  376 85   HOH   HOH A . 
E 4 HOH   77  377 5    HOH   HOH A . 
E 4 HOH   78  378 1301 HOH   HOH A . 
E 4 HOH   79  379 1275 HOH   HOH A . 
E 4 HOH   80  380 154  HOH   HOH A . 
E 4 HOH   81  381 661  HOH   HOH A . 
E 4 HOH   82  382 46   HOH   HOH A . 
E 4 HOH   83  383 134  HOH   HOH A . 
E 4 HOH   84  384 4    HOH   HOH A . 
E 4 HOH   85  385 132  HOH   HOH A . 
E 4 HOH   86  386 35   HOH   HOH A . 
E 4 HOH   87  387 27   HOH   HOH A . 
E 4 HOH   88  388 296  HOH   HOH A . 
E 4 HOH   89  389 1315 HOH   HOH A . 
E 4 HOH   90  390 39   HOH   HOH A . 
E 4 HOH   91  391 333  HOH   HOH A . 
E 4 HOH   92  392 218  HOH   HOH A . 
E 4 HOH   93  393 303  HOH   HOH A . 
E 4 HOH   94  394 461  HOH   HOH A . 
E 4 HOH   95  395 366  HOH   HOH A . 
E 4 HOH   96  396 12   HOH   HOH A . 
E 4 HOH   97  397 58   HOH   HOH A . 
E 4 HOH   98  398 24   HOH   HOH A . 
E 4 HOH   99  399 116  HOH   HOH A . 
E 4 HOH   100 400 96   HOH   HOH A . 
E 4 HOH   101 401 67   HOH   HOH A . 
E 4 HOH   102 402 83   HOH   HOH A . 
E 4 HOH   103 403 74   HOH   HOH A . 
E 4 HOH   104 404 78   HOH   HOH A . 
E 4 HOH   105 405 10   HOH   HOH A . 
E 4 HOH   106 406 397  HOH   HOH A . 
E 4 HOH   107 407 381  HOH   HOH A . 
E 4 HOH   108 408 1309 HOH   HOH A . 
E 4 HOH   109 409 1308 HOH   HOH A . 
E 4 HOH   110 410 493  HOH   HOH A . 
E 4 HOH   111 411 121  HOH   HOH A . 
E 4 HOH   112 412 51   HOH   HOH A . 
E 4 HOH   113 413 3    HOH   HOH A . 
E 4 HOH   114 414 1279 HOH   HOH A . 
E 4 HOH   115 415 25   HOH   HOH A . 
E 4 HOH   116 416 34   HOH   HOH A . 
E 4 HOH   117 417 68   HOH   HOH A . 
E 4 HOH   118 418 122  HOH   HOH A . 
E 4 HOH   119 419 6    HOH   HOH A . 
E 4 HOH   120 420 212  HOH   HOH A . 
E 4 HOH   121 421 1068 HOH   HOH A . 
E 4 HOH   122 422 582  HOH   HOH A . 
E 4 HOH   123 423 123  HOH   HOH A . 
E 4 HOH   124 424 351  HOH   HOH A . 
E 4 HOH   125 425 125  HOH   HOH A . 
E 4 HOH   126 426 8    HOH   HOH A . 
E 4 HOH   127 427 1313 HOH   HOH A . 
E 4 HOH   128 428 278  HOH   HOH A . 
E 4 HOH   129 429 53   HOH   HOH A . 
E 4 HOH   130 430 156  HOH   HOH A . 
E 4 HOH   131 431 281  HOH   HOH A . 
E 4 HOH   132 432 95   HOH   HOH A . 
E 4 HOH   133 433 115  HOH   HOH A . 
E 4 HOH   134 434 1222 HOH   HOH A . 
E 4 HOH   135 435 7    HOH   HOH A . 
E 4 HOH   136 436 7    HOH   HOH A . 
E 4 HOH   137 437 1286 HOH   HOH A . 
E 4 HOH   138 438 71   HOH   HOH A . 
E 4 HOH   139 439 16   HOH   HOH A . 
E 4 HOH   140 440 73   HOH   HOH A . 
E 4 HOH   141 441 188  HOH   HOH A . 
E 4 HOH   142 442 1189 HOH   HOH A . 
E 4 HOH   143 443 952  HOH   HOH A . 
E 4 HOH   144 444 40   HOH   HOH A . 
E 4 HOH   145 445 1238 HOH   HOH A . 
E 4 HOH   146 446 80   HOH   HOH A . 
E 4 HOH   147 447 94   HOH   HOH A . 
E 4 HOH   148 448 97   HOH   HOH A . 
E 4 HOH   149 449 104  HOH   HOH A . 
E 4 HOH   150 450 944  HOH   HOH A . 
E 4 HOH   151 451 576  HOH   HOH A . 
E 4 HOH   152 452 14   HOH   HOH A . 
E 4 HOH   153 453 1094 HOH   HOH A . 
E 4 HOH   154 454 1296 HOH   HOH A . 
E 4 HOH   155 455 79   HOH   HOH A . 
E 4 HOH   156 456 330  HOH   HOH A . 
E 4 HOH   157 457 1119 HOH   HOH A . 
E 4 HOH   158 458 1276 HOH   HOH A . 
E 4 HOH   159 459 15   HOH   HOH A . 
E 4 HOH   160 460 509  HOH   HOH A . 
E 4 HOH   161 461 107  HOH   HOH A . 
E 4 HOH   162 462 1134 HOH   HOH A . 
E 4 HOH   163 463 163  HOH   HOH A . 
E 4 HOH   164 464 726  HOH   HOH A . 
E 4 HOH   165 465 408  HOH   HOH A . 
E 4 HOH   166 466 756  HOH   HOH A . 
E 4 HOH   167 467 361  HOH   HOH A . 
E 4 HOH   168 468 63   HOH   HOH A . 
E 4 HOH   169 469 126  HOH   HOH A . 
E 4 HOH   170 470 280  HOH   HOH A . 
E 4 HOH   171 471 801  HOH   HOH A . 
E 4 HOH   172 472 319  HOH   HOH A . 
E 4 HOH   173 473 556  HOH   HOH A . 
E 4 HOH   174 474 6    HOH   HOH A . 
E 4 HOH   175 475 250  HOH   HOH A . 
E 4 HOH   176 476 1307 HOH   HOH A . 
E 4 HOH   177 477 342  HOH   HOH A . 
E 4 HOH   178 478 267  HOH   HOH A . 
E 4 HOH   179 479 326  HOH   HOH A . 
E 4 HOH   180 480 370  HOH   HOH A . 
E 4 HOH   181 481 695  HOH   HOH A . 
E 4 HOH   182 482 1287 HOH   HOH A . 
E 4 HOH   183 483 1306 HOH   HOH A . 
E 4 HOH   184 484 224  HOH   HOH A . 
E 4 HOH   185 485 202  HOH   HOH A . 
E 4 HOH   186 486 13   HOH   HOH A . 
E 4 HOH   187 487 919  HOH   HOH A . 
E 4 HOH   188 488 674  HOH   HOH A . 
E 4 HOH   189 489 2    HOH   HOH A . 
E 4 HOH   190 490 135  HOH   HOH A . 
E 4 HOH   191 491 309  HOH   HOH A . 
E 4 HOH   192 492 318  HOH   HOH A . 
E 4 HOH   193 493 1299 HOH   HOH A . 
E 4 HOH   194 494 521  HOH   HOH A . 
E 4 HOH   195 495 711  HOH   HOH A . 
E 4 HOH   196 496 805  HOH   HOH A . 
E 4 HOH   197 497 315  HOH   HOH A . 
E 4 HOH   198 498 152  HOH   HOH A . 
E 4 HOH   199 499 263  HOH   HOH A . 
E 4 HOH   200 500 331  HOH   HOH A . 
E 4 HOH   201 501 941  HOH   HOH A . 
E 4 HOH   202 502 1314 HOH   HOH A . 
E 4 HOH   203 503 208  HOH   HOH A . 
E 4 HOH   204 504 1071 HOH   HOH A . 
E 4 HOH   205 505 1284 HOH   HOH A . 
E 4 HOH   206 506 180  HOH   HOH A . 
E 4 HOH   207 507 356  HOH   HOH A . 
E 4 HOH   208 508 350  HOH   HOH A . 
E 4 HOH   209 509 371  HOH   HOH A . 
E 4 HOH   210 510 363  HOH   HOH A . 
E 4 HOH   211 511 8    HOH   HOH A . 
E 4 HOH   212 512 313  HOH   HOH A . 
E 4 HOH   213 513 12   HOH   HOH A . 
E 4 HOH   214 514 429  HOH   HOH A . 
E 4 HOH   215 515 185  HOH   HOH A . 
E 4 HOH   216 516 772  HOH   HOH A . 
E 4 HOH   217 517 376  HOH   HOH A . 
E 4 HOH   218 518 1074 HOH   HOH A . 
E 4 HOH   219 519 346  HOH   HOH A . 
E 4 HOH   220 520 1292 HOH   HOH A . 
E 4 HOH   221 521 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 358  HOH   HOH B . 
F 4 HOH   3   203 364  HOH   HOH B . 
F 4 HOH   4   204 398  HOH   HOH B . 
F 4 HOH   5   205 240  HOH   HOH B . 
F 4 HOH   6   206 654  HOH   HOH B . 
F 4 HOH   7   207 549  HOH   HOH B . 
F 4 HOH   8   208 900  HOH   HOH B . 
F 4 HOH   9   209 1249 HOH   HOH B . 
F 4 HOH   10  210 531  HOH   HOH B . 
F 4 HOH   11  211 743  HOH   HOH B . 
F 4 HOH   12  212 758  HOH   HOH B . 
F 4 HOH   13  213 353  HOH   HOH B . 
F 4 HOH   14  214 343  HOH   HOH B . 
F 4 HOH   15  215 120  HOH   HOH B . 
F 4 HOH   16  216 50   HOH   HOH B . 
F 4 HOH   17  217 264  HOH   HOH B . 
F 4 HOH   18  218 131  HOH   HOH B . 
F 4 HOH   19  219 1140 HOH   HOH B . 
F 4 HOH   20  220 282  HOH   HOH B . 
F 4 HOH   21  221 444  HOH   HOH B . 
F 4 HOH   22  222 54   HOH   HOH B . 
F 4 HOH   23  223 276  HOH   HOH B . 
F 4 HOH   24  224 723  HOH   HOH B . 
F 4 HOH   25  225 128  HOH   HOH B . 
F 4 HOH   26  226 1312 HOH   HOH B . 
F 4 HOH   27  227 232  HOH   HOH B . 
F 4 HOH   28  228 332  HOH   HOH B . 
F 4 HOH   29  229 75   HOH   HOH B . 
F 4 HOH   30  230 1278 HOH   HOH B . 
F 4 HOH   31  231 452  HOH   HOH B . 
F 4 HOH   32  232 82   HOH   HOH B . 
F 4 HOH   33  233 60   HOH   HOH B . 
F 4 HOH   34  234 272  HOH   HOH B . 
F 4 HOH   35  235 69   HOH   HOH B . 
F 4 HOH   36  236 205  HOH   HOH B . 
F 4 HOH   37  237 110  HOH   HOH B . 
F 4 HOH   38  238 127  HOH   HOH B . 
F 4 HOH   39  239 181  HOH   HOH B . 
F 4 HOH   40  240 166  HOH   HOH B . 
F 4 HOH   41  241 1    HOH   HOH B . 
F 4 HOH   42  242 14   HOH   HOH B . 
F 4 HOH   43  243 300  HOH   HOH B . 
F 4 HOH   44  244 231  HOH   HOH B . 
F 4 HOH   45  245 129  HOH   HOH B . 
F 4 HOH   46  246 9    HOH   HOH B . 
F 4 HOH   47  247 133  HOH   HOH B . 
F 4 HOH   48  248 72   HOH   HOH B . 
F 4 HOH   49  249 172  HOH   HOH B . 
F 4 HOH   50  250 144  HOH   HOH B . 
F 4 HOH   51  251 325  HOH   HOH B . 
F 4 HOH   52  252 52   HOH   HOH B . 
F 4 HOH   53  253 30   HOH   HOH B . 
F 4 HOH   54  254 31   HOH   HOH B . 
F 4 HOH   55  255 143  HOH   HOH B . 
F 4 HOH   56  256 47   HOH   HOH B . 
F 4 HOH   57  257 347  HOH   HOH B . 
F 4 HOH   58  258 10   HOH   HOH B . 
F 4 HOH   59  259 150  HOH   HOH B . 
F 4 HOH   60  260 103  HOH   HOH B . 
F 4 HOH   61  261 271  HOH   HOH B . 
F 4 HOH   62  262 84   HOH   HOH B . 
F 4 HOH   63  263 59   HOH   HOH B . 
F 4 HOH   64  264 1277 HOH   HOH B . 
F 4 HOH   65  265 20   HOH   HOH B . 
F 4 HOH   66  266 77   HOH   HOH B . 
F 4 HOH   67  267 61   HOH   HOH B . 
F 4 HOH   68  268 243  HOH   HOH B . 
F 4 HOH   69  269 41   HOH   HOH B . 
F 4 HOH   70  270 62   HOH   HOH B . 
F 4 HOH   71  271 11   HOH   HOH B . 
F 4 HOH   72  272 117  HOH   HOH B . 
F 4 HOH   73  273 391  HOH   HOH B . 
F 4 HOH   74  274 175  HOH   HOH B . 
F 4 HOH   75  275 242  HOH   HOH B . 
F 4 HOH   76  276 114  HOH   HOH B . 
F 4 HOH   77  277 341  HOH   HOH B . 
F 4 HOH   78  278 302  HOH   HOH B . 
F 4 HOH   79  279 1305 HOH   HOH B . 
F 4 HOH   80  280 43   HOH   HOH B . 
F 4 HOH   81  281 635  HOH   HOH B . 
F 4 HOH   82  282 221  HOH   HOH B . 
F 4 HOH   83  283 252  HOH   HOH B . 
F 4 HOH   84  284 1106 HOH   HOH B . 
F 4 HOH   85  285 387  HOH   HOH B . 
F 4 HOH   86  286 287  HOH   HOH B . 
F 4 HOH   87  287 13   HOH   HOH B . 
F 4 HOH   88  288 22   HOH   HOH B . 
F 4 HOH   89  289 106  HOH   HOH B . 
F 4 HOH   90  290 235  HOH   HOH B . 
F 4 HOH   91  291 416  HOH   HOH B . 
F 4 HOH   92  292 88   HOH   HOH B . 
F 4 HOH   93  293 147  HOH   HOH B . 
F 4 HOH   94  294 704  HOH   HOH B . 
F 4 HOH   95  295 141  HOH   HOH B . 
F 4 HOH   96  296 99   HOH   HOH B . 
F 4 HOH   97  297 32   HOH   HOH B . 
F 4 HOH   98  298 89   HOH   HOH B . 
F 4 HOH   99  299 1066 HOH   HOH B . 
F 4 HOH   100 300 137  HOH   HOH B . 
F 4 HOH   101 301 299  HOH   HOH B . 
F 4 HOH   102 302 112  HOH   HOH B . 
F 4 HOH   103 303 216  HOH   HOH B . 
F 4 HOH   104 304 297  HOH   HOH B . 
F 4 HOH   105 305 316  HOH   HOH B . 
F 4 HOH   106 306 38   HOH   HOH B . 
F 4 HOH   107 307 160  HOH   HOH B . 
F 4 HOH   108 308 48   HOH   HOH B . 
F 4 HOH   109 309 311  HOH   HOH B . 
F 4 HOH   110 310 215  HOH   HOH B . 
F 4 HOH   111 311 220  HOH   HOH B . 
F 4 HOH   112 312 1126 HOH   HOH B . 
F 4 HOH   113 313 101  HOH   HOH B . 
F 4 HOH   114 314 1291 HOH   HOH B . 
F 4 HOH   115 315 142  HOH   HOH B . 
F 4 HOH   116 316 91   HOH   HOH B . 
F 4 HOH   117 317 37   HOH   HOH B . 
F 4 HOH   118 318 118  HOH   HOH B . 
F 4 HOH   119 319 28   HOH   HOH B . 
F 4 HOH   120 320 23   HOH   HOH B . 
F 4 HOH   121 321 170  HOH   HOH B . 
F 4 HOH   122 322 44   HOH   HOH B . 
F 4 HOH   123 323 339  HOH   HOH B . 
F 4 HOH   124 324 1285 HOH   HOH B . 
F 4 HOH   125 325 182  HOH   HOH B . 
F 4 HOH   126 326 177  HOH   HOH B . 
F 4 HOH   127 327 100  HOH   HOH B . 
F 4 HOH   128 328 29   HOH   HOH B . 
F 4 HOH   129 329 161  HOH   HOH B . 
F 4 HOH   130 330 717  HOH   HOH B . 
F 4 HOH   131 331 445  HOH   HOH B . 
F 4 HOH   132 332 55   HOH   HOH B . 
F 4 HOH   133 333 1274 HOH   HOH B . 
F 4 HOH   134 334 234  HOH   HOH B . 
F 4 HOH   135 335 197  HOH   HOH B . 
F 4 HOH   136 336 334  HOH   HOH B . 
F 4 HOH   137 337 1294 HOH   HOH B . 
F 4 HOH   138 338 98   HOH   HOH B . 
F 4 HOH   139 339 207  HOH   HOH B . 
F 4 HOH   140 340 65   HOH   HOH B . 
F 4 HOH   141 341 619  HOH   HOH B . 
F 4 HOH   142 342 178  HOH   HOH B . 
F 4 HOH   143 343 1293 HOH   HOH B . 
F 4 HOH   144 344 90   HOH   HOH B . 
F 4 HOH   145 345 362  HOH   HOH B . 
F 4 HOH   146 346 463  HOH   HOH B . 
F 4 HOH   147 347 960  HOH   HOH B . 
F 4 HOH   148 348 191  HOH   HOH B . 
F 4 HOH   149 349 304  HOH   HOH B . 
F 4 HOH   150 350 335  HOH   HOH B . 
F 4 HOH   151 351 623  HOH   HOH B . 
F 4 HOH   152 352 1046 HOH   HOH B . 
F 4 HOH   153 353 1304 HOH   HOH B . 
F 4 HOH   154 354 541  HOH   HOH B . 
F 4 HOH   155 355 1280 HOH   HOH B . 
F 4 HOH   156 356 203  HOH   HOH B . 
F 4 HOH   157 357 290  HOH   HOH B . 
F 4 HOH   158 358 87   HOH   HOH B . 
F 4 HOH   159 359 479  HOH   HOH B . 
F 4 HOH   160 360 389  HOH   HOH B . 
F 4 HOH   161 361 1077 HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 1072 HOH   HOH B . 
F 4 HOH   164 364 718  HOH   HOH B . 
F 4 HOH   165 365 1316 HOH   HOH B . 
F 4 HOH   166 366 373  HOH   HOH B . 
F 4 HOH   167 367 898  HOH   HOH B . 
F 4 HOH   168 368 340  HOH   HOH B . 
F 4 HOH   169 369 667  HOH   HOH B . 
F 4 HOH   170 370 291  HOH   HOH B . 
F 4 HOH   171 371 1303 HOH   HOH B . 
F 4 HOH   172 372 615  HOH   HOH B . 
F 4 HOH   173 373 310  HOH   HOH B . 
F 4 HOH   174 374 190  HOH   HOH B . 
F 4 HOH   175 375 149  HOH   HOH B . 
F 4 HOH   176 376 1163 HOH   HOH B . 
F 4 HOH   177 377 1173 HOH   HOH B . 
F 4 HOH   178 378 431  HOH   HOH B . 
F 4 HOH   179 379 183  HOH   HOH B . 
F 4 HOH   180 380 1000 HOH   HOH B . 
F 4 HOH   181 381 176  HOH   HOH B . 
F 4 HOH   182 382 418  HOH   HOH B . 
F 4 HOH   183 383 1311 HOH   HOH B . 
F 4 HOH   184 384 424  HOH   HOH B . 
F 4 HOH   185 385 470  HOH   HOH B . 
F 4 HOH   186 386 1298 HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 265  HOH   HOH B . 
F 4 HOH   189 389 491  HOH   HOH B . 
F 4 HOH   190 390 981  HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 360  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 355  HOH   HOH B . 
F 4 HOH   195 395 274  HOH   HOH B . 
F 4 HOH   196 396 314  HOH   HOH B . 
F 4 HOH   197 397 566  HOH   HOH B . 
F 4 HOH   198 398 157  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 HOH   201 401 558  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           7HFA 
_cell.length_a           88.655 
_cell.length_b           88.655 
_cell.length_c           39.521 
_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                         7HFA 
_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          7HFA 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.51 
_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   2023-08-11 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HFA 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.330 
_reflns.d_resolution_high            0.990 
_reflns.number_obs                   169620 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.040 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.000 
_reflns.B_iso_Wilson_estimate        11.580 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.044 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1097353 
_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 0.990 1.010  ? 38646 7725 ? 1.753 ? ? ? 5.000 ? 0.700  ? ? ? ? ? ? 91.900 1.959 0.854 0.511 
1 2 5.420 44.330 ? 7948  1133 ? 0.023 ? ? ? 7.000 ? 77.700 ? ? ? ? ? ? 99.800 0.025 0.010 0.999 
# 
_refine.entry_id                                 7HFA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9900 
_refine.ls_d_res_low                             44.3300 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.2600 
_refine.ls_number_reflns_obs                     169499 
_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                          0.1487 
_refine.ls_R_factor_R_work                       0.1480 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1614 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8170 
_refine.ls_number_reflns_R_work                  161329 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.5421 
_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                            0.1200 
_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                                64.080 
_refine.B_iso_min                                8.430 
_refine.pdbx_overall_phase_error                 18.8300 
_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                       0.9900 
_refine_hist.d_res_low                        44.3300 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.number_atoms_solvent             422 
_refine_hist.number_atoms_total               3002 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           12.78 
_refine_hist.pdbx_B_iso_mean_solvent          29.14 
_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 
0.9900 1.0000  30 89.0000  4810 . 0.4107 0.4197 . 236 0.0000 5046 . 'X-RAY DIFFRACTION' 
1.0000 1.0100  30 97.0000  5210 . 0.3542 0.3620 . 272 0.0000 5482 . 'X-RAY DIFFRACTION' 
1.0100 1.0300  30 100.0000 5360 . 0.3024 0.3041 . 242 0.0000 5602 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5410 . 0.2828 0.2724 . 281 0.0000 5691 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5396 . 0.2626 0.2773 . 283 0.0000 5679 . 'X-RAY DIFFRACTION' 
1.0500 1.0700  30 100.0000 5332 . 0.2485 0.2595 . 322 0.0000 5654 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 5376 . 0.2365 0.2532 . 268 0.0000 5644 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 5411 . 0.2212 0.2453 . 251 0.0000 5662 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 98.0000  5254 . 0.2027 0.2106 . 285 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5443 . 0.1706 0.1874 . 239 0.0000 5682 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5396 . 0.1595 0.1688 . 257 0.0000 5653 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5380 . 0.1459 0.1750 . 284 0.0000 5664 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5410 . 0.1442 0.1745 . 266 0.0000 5676 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5295 . 0.1304 0.1688 . 296 0.0000 5591 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5452 . 0.1316 0.1447 . 259 0.0000 5711 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 98.0000  5354 . 0.1359 0.1500 . 259 0.0000 5613 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 5353 . 0.1317 0.1552 . 275 0.0000 5628 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 5348 . 0.1358 0.1568 . 284 0.0000 5632 . 'X-RAY DIFFRACTION' 
1.3400 1.3800  30 100.0000 5427 . 0.1328 0.1592 . 281 0.0000 5708 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 5439 . 0.1258 0.1484 . 257 0.0000 5696 . 'X-RAY DIFFRACTION' 
1.4300 1.4800  30 100.0000 5406 . 0.1237 0.1348 . 272 0.0000 5678 . 'X-RAY DIFFRACTION' 
1.4800 1.5400  30 100.0000 5407 . 0.1194 0.1318 . 284 0.0000 5691 . 'X-RAY DIFFRACTION' 
1.5400 1.6100  30 99.0000  5340 . 0.1174 0.1339 . 274 0.0000 5614 . 'X-RAY DIFFRACTION' 
1.6100 1.6900  30 100.0000 5452 . 0.1228 0.1404 . 263 0.0000 5715 . 'X-RAY DIFFRACTION' 
1.6900 1.8000  30 100.0000 5473 . 0.1322 0.1371 . 268 0.0000 5741 . 'X-RAY DIFFRACTION' 
1.8000 1.9400  30 100.0000 5397 . 0.1312 0.1297 . 292 0.0000 5689 . 'X-RAY DIFFRACTION' 
1.9400 2.1300  30 100.0000 5435 . 0.1371 0.1474 . 273 0.0000 5708 . 'X-RAY DIFFRACTION' 
2.1300 2.4400  30 100.0000 5438 . 0.1369 0.1386 . 295 0.0000 5733 . 'X-RAY DIFFRACTION' 
2.4400 3.0800  30 100.0000 5501 . 0.1494 0.1647 . 283 0.0000 5784 . 'X-RAY DIFFRACTION' 
3.0800 44.3300 30 100.0000 5624 . 0.1515 0.1724 . 269 0.0000 5893 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFA 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004195' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFA 
_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 4 ? 
F N N 4 ? 
# 
_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 7HFA A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFA 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 7HFA SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFA MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFA SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFA 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 
2 1 B,F     
# 
_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 LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
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 ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 HIS A 86  ? ? 55.59   -133.29 
2 1 SER A 128 ? B 70.53   -13.02  
3 1 PHE A 156 ? B -99.06  42.85   
4 1 ASP A 157 ? B -170.33 110.94  
5 1 HIS B 86  ? ? 56.78   -127.67 
# 
_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 ? A HOH 519 ? 5.87 . 
2 1 O ? A HOH 520 ? 6.07 . 
3 1 O ? A HOH 521 ? 7.57 . 
4 1 O ? B HOH 401 ? 6.23 . 
# 
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 
A1BAW N2   N  Y N 1   
A1BAW C3   C  Y N 2   
A1BAW C6   C  Y N 3   
A1BAW C9   C  N N 4   
A1BAW C12  C  N N 5   
A1BAW C1   C  N N 6   
A1BAW C10  C  N N 7   
A1BAW C11  C  N N 8   
A1BAW C13  C  Y N 9   
A1BAW C2   C  Y N 10  
A1BAW C4   C  Y N 11  
A1BAW C5   C  Y N 12  
A1BAW C7   C  N N 13  
A1BAW C8   C  N N 14  
A1BAW N1   N  Y N 15  
A1BAW N3   N  Y N 16  
A1BAW N4   N  N N 17  
A1BAW O1   O  N N 18  
A1BAW S1   S  N N 19  
A1BAW H4   H  N N 20  
A1BAW H12  H  N N 21  
A1BAW H11  H  N N 22  
A1BAW H17  H  N N 23  
A1BAW H18  H  N N 24  
A1BAW H3   H  N N 25  
A1BAW H1   H  N N 26  
A1BAW H2   H  N N 27  
A1BAW H14  H  N N 28  
A1BAW H13  H  N N 29  
A1BAW H16  H  N N 30  
A1BAW H15  H  N N 31  
A1BAW H6   H  N N 32  
A1BAW H9   H  N N 33  
A1BAW H8   H  N N 34  
A1BAW H5   H  N N 35  
A1BAW H7   H  N N 36  
A1BAW H10  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CL    CL   CL N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
PHE   N    N  N N 288 
PHE   CA   C  N S 289 
PHE   C    C  N N 290 
PHE   O    O  N N 291 
PHE   CB   C  N N 292 
PHE   CG   C  Y N 293 
PHE   CD1  C  Y N 294 
PHE   CD2  C  Y N 295 
PHE   CE1  C  Y N 296 
PHE   CE2  C  Y N 297 
PHE   CZ   C  Y N 298 
PHE   OXT  O  N N 299 
PHE   H    H  N N 300 
PHE   H2   H  N N 301 
PHE   HA   H  N N 302 
PHE   HB2  H  N N 303 
PHE   HB3  H  N N 304 
PHE   HD1  H  N N 305 
PHE   HD2  H  N N 306 
PHE   HE1  H  N N 307 
PHE   HE2  H  N N 308 
PHE   HZ   H  N N 309 
PHE   HXT  H  N N 310 
PRO   N    N  N N 311 
PRO   CA   C  N S 312 
PRO   C    C  N N 313 
PRO   O    O  N N 314 
PRO   CB   C  N N 315 
PRO   CG   C  N N 316 
PRO   CD   C  N N 317 
PRO   OXT  O  N N 318 
PRO   H    H  N N 319 
PRO   HA   H  N N 320 
PRO   HB2  H  N N 321 
PRO   HB3  H  N N 322 
PRO   HG2  H  N N 323 
PRO   HG3  H  N N 324 
PRO   HD2  H  N N 325 
PRO   HD3  H  N N 326 
PRO   HXT  H  N N 327 
SER   N    N  N N 328 
SER   CA   C  N S 329 
SER   C    C  N N 330 
SER   O    O  N N 331 
SER   CB   C  N N 332 
SER   OG   O  N N 333 
SER   OXT  O  N N 334 
SER   H    H  N N 335 
SER   H2   H  N N 336 
SER   HA   H  N N 337 
SER   HB2  H  N N 338 
SER   HB3  H  N N 339 
SER   HG   H  N N 340 
SER   HXT  H  N N 341 
THR   N    N  N N 342 
THR   CA   C  N S 343 
THR   C    C  N N 344 
THR   O    O  N N 345 
THR   CB   C  N R 346 
THR   OG1  O  N N 347 
THR   CG2  C  N N 348 
THR   OXT  O  N N 349 
THR   H    H  N N 350 
THR   H2   H  N N 351 
THR   HA   H  N N 352 
THR   HB   H  N N 353 
THR   HG1  H  N N 354 
THR   HG21 H  N N 355 
THR   HG22 H  N N 356 
THR   HG23 H  N N 357 
THR   HXT  H  N N 358 
TYR   N    N  N N 359 
TYR   CA   C  N S 360 
TYR   C    C  N N 361 
TYR   O    O  N N 362 
TYR   CB   C  N N 363 
TYR   CG   C  Y N 364 
TYR   CD1  C  Y N 365 
TYR   CD2  C  Y N 366 
TYR   CE1  C  Y N 367 
TYR   CE2  C  Y N 368 
TYR   CZ   C  Y N 369 
TYR   OH   O  N N 370 
TYR   OXT  O  N N 371 
TYR   H    H  N N 372 
TYR   H2   H  N N 373 
TYR   HA   H  N N 374 
TYR   HB2  H  N N 375 
TYR   HB3  H  N N 376 
TYR   HD1  H  N N 377 
TYR   HD2  H  N N 378 
TYR   HE1  H  N N 379 
TYR   HE2  H  N N 380 
TYR   HH   H  N N 381 
TYR   HXT  H  N N 382 
VAL   N    N  N N 383 
VAL   CA   C  N S 384 
VAL   C    C  N N 385 
VAL   O    O  N N 386 
VAL   CB   C  N N 387 
VAL   CG1  C  N N 388 
VAL   CG2  C  N N 389 
VAL   OXT  O  N N 390 
VAL   H    H  N N 391 
VAL   H2   H  N N 392 
VAL   HA   H  N N 393 
VAL   HB   H  N N 394 
VAL   HG11 H  N N 395 
VAL   HG12 H  N N 396 
VAL   HG13 H  N N 397 
VAL   HG21 H  N N 398 
VAL   HG22 H  N N 399 
VAL   HG23 H  N N 400 
VAL   HXT  H  N N 401 
# 
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 
A1BAW S1  C10  sing N N 1   
A1BAW S1  C11  sing N N 2   
A1BAW C9  C10  sing N N 3   
A1BAW C9  C8   sing N N 4   
A1BAW C12 C11  sing N N 5   
A1BAW C12 C8   sing N N 6   
A1BAW C8  C7   sing N N 7   
A1BAW C8  O1   sing N N 8   
A1BAW C7  N4   sing N N 9   
A1BAW N4  C6   sing N N 10  
A1BAW C1  C2   sing N N 11  
A1BAW C6  C13  doub Y N 12  
A1BAW C6  N3   sing Y N 13  
A1BAW C2  C13  sing Y N 14  
A1BAW C2  C3   doub Y N 15  
A1BAW C13 C4   sing Y N 16  
A1BAW N3  C5   doub Y N 17  
A1BAW C3  N1   sing Y N 18  
A1BAW C4  N1   sing Y N 19  
A1BAW C4  N2   doub Y N 20  
A1BAW C5  N2   sing Y N 21  
A1BAW C3  H4   sing N N 22  
A1BAW C9  H12  sing N N 23  
A1BAW C9  H11  sing N N 24  
A1BAW C12 H17  sing N N 25  
A1BAW C12 H18  sing N N 26  
A1BAW C1  H3   sing N N 27  
A1BAW C1  H1   sing N N 28  
A1BAW C1  H2   sing N N 29  
A1BAW C10 H14  sing N N 30  
A1BAW C10 H13  sing N N 31  
A1BAW C11 H16  sing N N 32  
A1BAW C11 H15  sing N N 33  
A1BAW C5  H6   sing N N 34  
A1BAW C7  H9   sing N N 35  
A1BAW C7  H8   sing N N 36  
A1BAW N1  H5   sing N N 37  
A1BAW N4  H7   sing N N 38  
A1BAW O1  H10  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_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                    7HFA 
_atom_sites.fract_transf_matrix[1][1]   0.011280 
_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]   0.011280 
_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]   0.025303 
_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    . VAL   A 1 3   ? 19.589 -16.332 22.313  1.00 49.54 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.655 -15.225 22.487  1.00 49.08 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.335 -13.903 22.152  1.00 47.24 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.467 -13.656 22.566  1.00 47.66 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 18.059 -15.212 23.912  1.00 50.02 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 17.049 -14.080 24.063  1.00 50.40 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.411 -16.553 24.225  1.00 50.37 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.919 -15.333 21.871  1.00 58.89 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.769 -15.066 24.556  1.00 60.03 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.566 -14.196 24.898  1.00 60.48 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.520 -13.232 24.072  1.00 60.48 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.429 -14.108 23.318  1.00 60.48 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.972 -16.499 25.089  1.00 60.45 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.760 -16.757 23.535  1.00 60.45 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.097 -17.238 24.245  1.00 60.45 ?  3   VAL   A HG23 1 
ATOM   16   N  N    . ASN   A 1 4   ? 18.642 -13.063 21.385  1.00 44.50 ?  4   ASN   A N    1 
ATOM   17   C  CA   . ASN   A 1 4   ? 19.103 -11.716 21.073  1.00 41.29 ?  4   ASN   A CA   1 
ATOM   18   C  C    . ASN   A 1 4   ? 17.961 -10.732 21.312  1.00 38.31 ?  4   ASN   A C    1 
ATOM   19   O  O    . ASN   A 1 4   ? 16.840 -11.119 21.658  1.00 38.33 ?  4   ASN   A O    1 
ATOM   20   C  CB   . ASN   A 1 4   ? 19.670 -11.622 19.649  1.00 40.98 ?  4   ASN   A CB   1 
ATOM   21   C  CG   . ASN   A 1 4   ? 18.657 -11.990 18.588  1.00 40.53 ?  4   ASN   A CG   1 
ATOM   22   O  OD1  . ASN   A 1 4   ? 17.545 -11.463 18.565  1.00 40.24 ?  4   ASN   A OD1  1 
ATOM   23   N  ND2  . ASN   A 1 4   ? 19.038 -12.902 17.698  1.00 40.25 ?  4   ASN   A ND2  1 
ATOM   24   H  H    . ASN   A 1 4   ? 17.884 -13.258 21.025  1.00 53.40 ?  4   ASN   A H    1 
ATOM   25   H  HA   . ASN   A 1 4   ? 19.819 -11.490 21.681  1.00 49.55 ?  4   ASN   A HA   1 
ATOM   26   H  HB2  . ASN   A 1 4   ? 19.960 -10.710 19.484  1.00 49.17 ?  4   ASN   A HB2  1 
ATOM   27   H  HB3  . ASN   A 1 4   ? 20.422 -12.228 19.569  1.00 49.17 ?  4   ASN   A HB3  1 
ATOM   28   H  HD21 . ASN   A 1 4   ? 18.501 -13.145 17.072  1.00 48.30 ?  4   ASN   A HD21 1 
ATOM   29   H  HD22 . ASN   A 1 4   ? 19.824 -13.250 17.748  1.00 48.30 ?  4   ASN   A HD22 1 
ATOM   30   N  N    . SER   A 1 5   ? 18.250 -9.446  21.118  1.00 34.91 ?  5   SER   A N    1 
ATOM   31   C  CA   . SER   A 1 5   ? 17.352 -8.372  21.523  1.00 31.74 ?  5   SER   A CA   1 
ATOM   32   C  C    . SER   A 1 5   ? 16.457 -7.866  20.395  1.00 27.38 ?  5   SER   A C    1 
ATOM   33   O  O    . SER   A 1 5   ? 15.733 -6.885  20.589  1.00 28.14 ?  5   SER   A O    1 
ATOM   34   C  CB   . SER   A 1 5   ? 18.151 -7.215  22.128  1.00 32.66 ?  5   SER   A CB   1 
ATOM   35   O  OG   . SER   A 1 5   ? 19.067 -6.682  21.189  1.00 33.27 ?  5   SER   A OG   1 
ATOM   36   H  H    . SER   A 1 5   ? 18.972 -9.169  20.741  1.00 41.90 ?  5   SER   A H    1 
ATOM   37   H  HA   . SER   A 1 5   ? 16.771 -8.706  22.220  1.00 38.09 ?  5   SER   A HA   1 
ATOM   38   H  HB2  . SER   A 1 5   ? 17.538 -6.514  22.403  1.00 39.19 ?  5   SER   A HB2  1 
ATOM   39   H  HB3  . SER   A 1 5   ? 18.645 -7.539  22.900  1.00 39.19 ?  5   SER   A HB3  1 
ATOM   40   H  HG   . SER   A 1 5   ? 19.500 -6.047  21.535  1.00 39.92 ?  5   SER   A HG   1 
ATOM   41   N  N    A PHE   A 1 6   ? 16.491 -8.508  19.229  0.72 24.06 ?  6   PHE   A N    1 
ATOM   42   N  N    B PHE   A 1 6   ? 16.476 -8.505  19.231  0.28 25.49 ?  6   PHE   A N    1 
ATOM   43   C  CA   A PHE   A 1 6   ? 15.589 -8.141  18.145  0.72 21.18 ?  6   PHE   A CA   1 
ATOM   44   C  CA   B PHE   A 1 6   ? 15.625 -8.057  18.135  0.28 23.63 ?  6   PHE   A CA   1 
ATOM   45   C  C    A PHE   A 1 6   ? 14.161 -8.532  18.509  0.72 21.17 ?  6   PHE   A C    1 
ATOM   46   C  C    B PHE   A 1 6   ? 14.158 -8.236  18.512  0.28 23.30 ?  6   PHE   A C    1 
ATOM   47   O  O    A PHE   A 1 6   ? 13.914 -9.626  19.023  0.72 22.51 ?  6   PHE   A O    1 
ATOM   48   O  O    B PHE   A 1 6   ? 13.709 -9.352  18.792  0.28 23.49 ?  6   PHE   A O    1 
ATOM   49   C  CB   A PHE   A 1 6   ? 16.003 -8.845  16.854  0.72 18.91 ?  6   PHE   A CB   1 
ATOM   50   C  CB   B PHE   A 1 6   ? 15.967 -8.827  16.862  0.28 22.18 ?  6   PHE   A CB   1 
ATOM   51   C  CG   A PHE   A 1 6   ? 17.265 -8.298  16.236  0.72 17.39 ?  6   PHE   A CG   1 
ATOM   52   C  CG   B PHE   A 1 6   ? 17.304 -8.456  16.274  0.28 20.96 ?  6   PHE   A CG   1 
ATOM   53   C  CD1  A PHE   A 1 6   ? 17.256 -7.084  15.565  0.72 16.80 ?  6   PHE   A CD1  1 
ATOM   54   C  CD1  B PHE   A 1 6   ? 17.432 -7.348  15.451  0.28 20.40 ?  6   PHE   A CD1  1 
ATOM   55   C  CD2  A PHE   A 1 6   ? 18.454 -9.004  16.317  0.72 17.72 ?  6   PHE   A CD2  1 
ATOM   56   C  CD2  B PHE   A 1 6   ? 18.432 -9.212  16.549  0.28 20.60 ?  6   PHE   A CD2  1 
ATOM   57   C  CE1  A PHE   A 1 6   ? 18.412 -6.583  14.998  0.72 16.88 ?  6   PHE   A CE1  1 
ATOM   58   C  CE1  B PHE   A 1 6   ? 18.659 -7.003  14.913  0.28 20.15 ?  6   PHE   A CE1  1 
ATOM   59   C  CE2  A PHE   A 1 6   ? 19.610 -8.511  15.750  0.72 17.86 ?  6   PHE   A CE2  1 
ATOM   60   C  CE2  B PHE   A 1 6   ? 19.661 -8.872  16.014  0.28 20.16 ?  6   PHE   A CE2  1 
ATOM   61   C  CZ   A PHE   A 1 6   ? 19.591 -7.299  15.089  0.72 17.10 ?  6   PHE   A CZ   1 
ATOM   62   C  CZ   B PHE   A 1 6   ? 19.775 -7.766  15.194  0.28 19.97 ?  6   PHE   A CZ   1 
ATOM   63   H  H    A PHE   A 1 6   ? 17.017 -9.161  19.048  0.72 28.88 ?  6   PHE   A H    1 
ATOM   64   H  H    B PHE   A 1 6   ? 16.959 -9.192  19.055  0.28 30.59 ?  6   PHE   A H    1 
ATOM   65   H  HA   A PHE   A 1 6   ? 15.621 -7.184  18.005  0.72 25.42 ?  6   PHE   A HA   1 
ATOM   66   H  HA   B PHE   A 1 6   ? 15.783 -7.117  17.970  0.28 28.36 ?  6   PHE   A HA   1 
ATOM   67   H  HB2  A PHE   A 1 6   ? 16.149 -9.787  17.046  0.72 22.69 ?  6   PHE   A HB2  1 
ATOM   68   H  HB2  B PHE   A 1 6   ? 15.984 -9.776  17.062  0.28 26.62 ?  6   PHE   A HB2  1 
ATOM   69   H  HB3  A PHE   A 1 6   ? 15.287 -8.752  16.206  0.72 22.69 ?  6   PHE   A HB3  1 
ATOM   70   H  HB3  B PHE   A 1 6   ? 15.290 -8.645  16.193  0.28 26.62 ?  6   PHE   A HB3  1 
ATOM   71   H  HD1  A PHE   A 1 6   ? 16.460 -6.599  15.504  0.72 20.16 ?  6   PHE   A HD1  1 
ATOM   72   H  HD1  B PHE   A 1 6   ? 16.684 -6.831  15.259  0.28 24.49 ?  6   PHE   A HD1  1 
ATOM   73   H  HD2  A PHE   A 1 6   ? 18.472 -9.820  16.763  0.72 21.27 ?  6   PHE   A HD2  1 
ATOM   74   H  HD2  B PHE   A 1 6   ? 18.362 -9.956  17.100  0.28 24.72 ?  6   PHE   A HD2  1 
ATOM   75   H  HE1  A PHE   A 1 6   ? 18.393 -5.764  14.552  0.72 20.26 ?  6   PHE   A HE1  1 
ATOM   76   H  HE1  B PHE   A 1 6   ? 18.733 -6.258  14.361  0.28 24.19 ?  6   PHE   A HE1  1 
ATOM   77   H  HE2  A PHE   A 1 6   ? 20.403 -8.989  15.813  0.72 21.43 ?  6   PHE   A HE2  1 
ATOM   78   H  HE2  B PHE   A 1 6   ? 20.412 -9.388  16.205  0.28 24.19 ?  6   PHE   A HE2  1 
ATOM   79   H  HZ   A PHE   A 1 6   ? 20.366 -6.957  14.705  0.72 20.52 ?  6   PHE   A HZ   1 
ATOM   80   H  HZ   B PHE   A 1 6   ? 20.602 -7.536  14.833  0.28 23.97 ?  6   PHE   A HZ   1 
ATOM   81   N  N    A SER   A 1 7   ? 13.216 -7.633  18.234  0.72 20.32 ?  7   SER   A N    1 
ATOM   82   N  N    B SER   A 1 7   ? 13.414 -7.131  18.522  0.28 22.85 ?  7   SER   A N    1 
ATOM   83   C  CA   A SER   A 1 7   ? 11.847 -7.780  18.713  0.72 20.81 ?  7   SER   A CA   1 
ATOM   84   C  CA   B SER   A 1 7   ? 12.068 -7.084  19.079  0.28 22.42 ?  7   SER   A CA   1 
ATOM   85   C  C    A SER   A 1 7   ? 10.855 -7.459  17.602  0.72 19.86 ?  7   SER   A C    1 
ATOM   86   C  C    B SER   A 1 7   ? 11.023 -7.285  17.989  0.28 21.36 ?  7   SER   A C    1 
ATOM   87   O  O    A SER   A 1 7   ? 11.093 -6.567  16.785  0.72 20.56 ?  7   SER   A O    1 
ATOM   88   O  O    B SER   A 1 7   ? 11.014 -6.562  16.987  0.28 21.37 ?  7   SER   A O    1 
ATOM   89   C  CB   A SER   A 1 7   ? 11.604 -6.848  19.909  0.72 22.66 ?  7   SER   A CB   1 
ATOM   90   C  CB   B SER   A 1 7   ? 11.825 -5.740  19.769  0.28 22.91 ?  7   SER   A CB   1 
ATOM   91   O  OG   A SER   A 1 7   ? 10.256 -6.896  20.333  0.72 24.15 ?  7   SER   A OG   1 
ATOM   92   O  OG   B SER   A 1 7   ? 10.469 -5.601  20.158  0.28 23.38 ?  7   SER   A OG   1 
ATOM   93   H  H    A SER   A 1 7   ? 13.349 -6.925  17.764  0.72 24.39 ?  7   SER   A H    1 
ATOM   94   H  H    B SER   A 1 7   ? 13.675 -6.375  18.204  0.28 27.42 ?  7   SER   A H    1 
ATOM   95   H  HA   A SER   A 1 7   ? 11.700 -8.693  19.000  0.72 24.98 ?  7   SER   A HA   1 
ATOM   96   H  HA   B SER   A 1 7   ? 11.963 -7.786  19.738  0.28 26.91 ?  7   SER   A HA   1 
ATOM   97   H  HB2  A SER   A 1 7   ? 12.180 -7.122  20.644  0.72 27.19 ?  7   SER   A HB2  1 
ATOM   98   H  HB2  B SER   A 1 7   ? 12.377 -5.686  20.563  0.28 27.50 ?  7   SER   A HB2  1 
ATOM   99   H  HB3  A SER   A 1 7   ? 11.815 -5.938  19.651  0.72 27.19 ?  7   SER   A HB3  1 
ATOM   100  H  HB3  B SER   A 1 7   ? 12.057 -5.023  19.155  0.28 27.50 ?  7   SER   A HB3  1 
ATOM   101  H  HG   A SER   A 1 7   ? 10.142 -6.392  20.995  0.72 28.98 ?  7   SER   A HG   1 
ATOM   102  H  HG   B SER   A 1 7   ? 10.348 -4.851  20.520  0.28 28.06 ?  7   SER   A HG   1 
ATOM   103  N  N    A GLY   A 1 8   ? 9.739  -8.189  17.579  0.72 18.49 ?  8   GLY   A N    1 
ATOM   104  N  N    B GLY   A 1 8   ? 10.147 -8.266  18.192  0.28 20.29 ?  8   GLY   A N    1 
ATOM   105  C  CA   A GLY   A 1 8   ? 8.676  -7.911  16.634  0.72 17.76 ?  8   GLY   A CA   1 
ATOM   106  C  CA   B GLY   A 1 8   ? 8.943  -8.378  17.392  0.28 19.07 ?  8   GLY   A CA   1 
ATOM   107  C  C    A GLY   A 1 8   ? 8.880  -8.453  15.237  0.72 16.87 ?  8   GLY   A C    1 
ATOM   108  C  C    B GLY   A 1 8   ? 9.162  -8.714  15.938  0.28 17.95 ?  8   GLY   A C    1 
ATOM   109  O  O    A GLY   A 1 8   ? 8.146  -8.055  14.324  0.72 16.94 ?  8   GLY   A O    1 
ATOM   110  O  O    B GLY   A 1 8   ? 8.386  -8.267  15.086  0.28 17.97 ?  8   GLY   A O    1 
ATOM   111  H  H    A GLY   A 1 8   ? 9.584  -8.849  18.104  0.72 22.19 ?  8   GLY   A H    1 
ATOM   112  H  H    B GLY   A 1 8   ? 10.237 -8.885  18.779  0.28 24.35 ?  8   GLY   A H    1 
ATOM   113  H  HA2  A GLY   A 1 8   ? 7.851  -8.279  16.980  0.72 21.32 ?  8   GLY   A HA2  1 
ATOM   114  H  HA2  B GLY   A 1 8   ? 8.377  -9.070  17.764  0.28 22.88 ?  8   GLY   A HA2  1 
ATOM   115  H  HA3  A GLY   A 1 8   ? 8.566  -6.947  16.566  0.72 21.32 ?  8   GLY   A HA3  1 
ATOM   116  H  HA3  B GLY   A 1 8   ? 8.459  -7.539  17.429  0.28 22.88 ?  8   GLY   A HA3  1 
ATOM   117  N  N    A TYR   A 1 9   ? 9.853  -9.336  15.031  0.72 15.30 ?  9   TYR   A N    1 
ATOM   118  N  N    B TYR   A 1 9   ? 10.188 -9.496  15.624  0.28 17.06 ?  9   TYR   A N    1 
ATOM   119  C  CA   A TYR   A 1 9   ? 10.115 -9.903  13.716  0.72 14.45 ?  9   TYR   A CA   1 
ATOM   120  C  CA   B TYR   A 1 9   ? 10.439 -9.899  14.250  0.28 16.17 ?  9   TYR   A CA   1 
ATOM   121  C  C    A TYR   A 1 9   ? 9.229  -11.113 13.453  0.72 14.10 ?  9   TYR   A C    1 
ATOM   122  C  C    B TYR   A 1 9   ? 9.635  -11.145 13.895  0.28 15.59 ?  9   TYR   A C    1 
ATOM   123  O  O    A TYR   A 1 9   ? 8.896  -11.883 14.361  0.72 15.57 ?  9   TYR   A O    1 
ATOM   124  O  O    B TYR   A 1 9   ? 9.478  -12.057 14.712  0.28 16.17 ?  9   TYR   A O    1 
ATOM   125  C  CB   A TYR   A 1 9   ? 11.585 -10.323 13.578  0.72 14.71 ?  9   TYR   A CB   1 
ATOM   126  C  CB   B TYR   A 1 9   ? 11.932 -10.144 14.026  0.28 15.92 ?  9   TYR   A CB   1 
ATOM   127  C  CG   A TYR   A 1 9   ? 12.518 -9.152  13.425  0.72 15.04 ?  9   TYR   A CG   1 
ATOM   128  C  CG   B TYR   A 1 9   ? 12.714 -8.875  13.761  0.28 15.49 ?  9   TYR   A CG   1 
ATOM   129  C  CD1  A TYR   A 1 9   ? 12.853 -8.368  14.516  0.72 15.79 ?  9   TYR   A CD1  1 
ATOM   130  C  CD1  B TYR   A 1 9   ? 13.040 -8.007  14.795  0.28 15.54 ?  9   TYR   A CD1  1 
ATOM   131  C  CD2  A TYR   A 1 9   ? 13.040 -8.815  12.185  0.72 14.94 ?  9   TYR   A CD2  1 
ATOM   132  C  CD2  B TYR   A 1 9   ? 13.113 -8.539  12.473  0.28 15.14 ?  9   TYR   A CD2  1 
ATOM   133  C  CE1  A TYR   A 1 9   ? 13.689 -7.279  14.385  0.72 15.96 ?  9   TYR   A CE1  1 
ATOM   134  C  CE1  B TYR   A 1 9   ? 13.747 -6.843  14.554  0.28 15.48 ?  9   TYR   A CE1  1 
ATOM   135  C  CE2  A TYR   A 1 9   ? 13.875 -7.728  12.040  0.72 15.01 ?  9   TYR   A CE2  1 
ATOM   136  C  CE2  B TYR   A 1 9   ? 13.822 -7.376  12.223  0.28 15.09 ?  9   TYR   A CE2  1 
ATOM   137  C  CZ   A TYR   A 1 9   ? 14.193 -6.962  13.144  0.72 15.63 ?  9   TYR   A CZ   1 
ATOM   138  C  CZ   B TYR   A 1 9   ? 14.135 -6.534  13.267  0.28 15.15 ?  9   TYR   A CZ   1 
ATOM   139  O  OH   A TYR   A 1 9   ? 15.019 -5.879  13.007  0.72 16.60 ?  9   TYR   A OH   1 
ATOM   140  O  OH   B TYR   A 1 9   ? 14.833 -5.376  13.020  0.28 15.32 ?  9   TYR   A OH   1 
ATOM   141  H  H    A TYR   A 1 9   ? 10.381 -9.621  15.646  0.72 18.36 ?  9   TYR   A H    1 
ATOM   142  H  H    B TYR   A 1 9   ? 10.764 -9.802  16.192  0.28 20.47 ?  9   TYR   A H    1 
ATOM   143  H  HA   A TYR   A 1 9   ? 9.929  -9.232  13.040  0.72 17.34 ?  9   TYR   A HA   1 
ATOM   144  H  HA   B TYR   A 1 9   ? 10.167 -9.187  13.654  0.28 19.41 ?  9   TYR   A HA   1 
ATOM   145  H  HB2  A TYR   A 1 9   ? 11.847 -10.820 14.368  0.72 17.66 ?  9   TYR   A HB2  1 
ATOM   146  H  HB2  B TYR   A 1 9   ? 12.315 -10.588 14.800  0.28 19.11 ?  9   TYR   A HB2  1 
ATOM   147  H  HB3  A TYR   A 1 9   ? 11.671 -10.884 12.790  0.72 17.66 ?  9   TYR   A HB3  1 
ATOM   148  H  HB3  B TYR   A 1 9   ? 12.013 -10.706 13.249  0.28 19.11 ?  9   TYR   A HB3  1 
ATOM   149  H  HD1  A TYR   A 1 9   ? 12.501 -8.580  15.353  0.72 18.95 ?  9   TYR   A HD1  1 
ATOM   150  H  HD1  B TYR   A 1 9   ? 12.781 -8.215  15.664  0.28 18.65 ?  9   TYR   A HD1  1 
ATOM   151  H  HD2  A TYR   A 1 9   ? 12.821 -9.329  11.439  0.72 17.93 ?  9   TYR   A HD2  1 
ATOM   152  H  HD2  B TYR   A 1 9   ? 12.904 -9.105  11.766  0.28 18.18 ?  9   TYR   A HD2  1 
ATOM   153  H  HE1  A TYR   A 1 9   ? 13.904 -6.763  15.127  0.72 19.16 ?  9   TYR   A HE1  1 
ATOM   154  H  HE1  B TYR   A 1 9   ? 13.960 -6.271  15.256  0.28 18.58 ?  9   TYR   A HE1  1 
ATOM   155  H  HE2  A TYR   A 1 9   ? 14.225 -7.513  11.205  0.72 18.02 ?  9   TYR   A HE2  1 
ATOM   156  H  HE2  B TYR   A 1 9   ? 14.084 -7.161  11.355  0.28 18.11 ?  9   TYR   A HE2  1 
ATOM   157  H  HH   A TYR   A 1 9   ? 15.139 -5.514  13.754  0.72 19.92 ?  9   TYR   A HH   1 
ATOM   158  H  HH   B TYR   A 1 9   ? 14.979 -4.966  13.739  0.28 18.38 ?  9   TYR   A HH   1 
ATOM   159  N  N    A LEU   A 1 10  ? 8.843  -11.264 12.189  0.72 13.64 ?  10  LEU   A N    1 
ATOM   160  N  N    B LEU   A 1 10  ? 9.121  -11.167 12.667  0.28 14.55 ?  10  LEU   A N    1 
ATOM   161  C  CA   A LEU   A 1 10  ? 8.238  -12.493 11.696  0.72 13.70 ?  10  LEU   A CA   1 
ATOM   162  C  CA   B LEU   A 1 10  ? 8.355  -12.294 12.148  0.28 14.00 ?  10  LEU   A CA   1 
ATOM   163  C  C    A LEU   A 1 10  ? 9.363  -13.426 11.256  0.72 13.37 ?  10  LEU   A C    1 
ATOM   164  C  C    B LEU   A 1 10  ? 9.320  -13.286 11.508  0.28 13.54 ?  10  LEU   A C    1 
ATOM   165  O  O    A LEU   A 1 10  ? 10.336 -12.992 10.630  0.72 13.85 ?  10  LEU   A O    1 
ATOM   166  O  O    B LEU   A 1 10  ? 10.096 -12.921 10.617  0.28 13.74 ?  10  LEU   A O    1 
ATOM   167  C  CB   A LEU   A 1 10  ? 7.331  -12.178 10.505  0.72 15.18 ?  10  LEU   A CB   1 
ATOM   168  C  CB   B LEU   A 1 10  ? 7.332  -11.798 11.125  0.28 13.82 ?  10  LEU   A CB   1 
ATOM   169  C  CG   A LEU   A 1 10  ? 6.594  -13.371 9.892   0.72 17.67 ?  10  LEU   A CG   1 
ATOM   170  C  CG   B LEU   A 1 10  ? 6.365  -12.821 10.520  0.28 13.94 ?  10  LEU   A CG   1 
ATOM   171  C  CD1  A LEU   A 1 10  ? 5.488  -13.876 10.811  0.72 18.92 ?  10  LEU   A CD1  1 
ATOM   172  C  CD1  B LEU   A 1 10  ? 5.026  -12.155 10.227  0.28 14.32 ?  10  LEU   A CD1  1 
ATOM   173  C  CD2  A LEU   A 1 10  ? 6.047  -13.016 8.516   0.72 18.97 ?  10  LEU   A CD2  1 
ATOM   174  C  CD2  B LEU   A 1 10  ? 6.926  -13.457 9.251   0.28 13.63 ?  10  LEU   A CD2  1 
ATOM   175  H  H    A LEU   A 1 10  ? 8.925  -10.653 11.584  0.72 16.38 ?  10  LEU   A H    1 
ATOM   176  H  H    B LEU   A 1 10  ? 9.205  -10.523 12.105  0.28 17.46 ?  10  LEU   A H    1 
ATOM   177  H  HA   A LEU   A 1 10  ? 7.716  -12.915 12.399  0.72 16.45 ?  10  LEU   A HA   1 
ATOM   178  H  HA   B LEU   A 1 10  ? 7.887  -12.736 12.875  0.28 16.81 ?  10  LEU   A HA   1 
ATOM   179  H  HB2  A LEU   A 1 10  ? 6.660  -11.539 10.792  0.72 18.21 ?  10  LEU   A HB2  1 
ATOM   180  H  HB2  B LEU   A 1 10  ? 6.792  -11.115 11.554  0.28 16.59 ?  10  LEU   A HB2  1 
ATOM   181  H  HB3  A LEU   A 1 10  ? 7.874  -11.785 9.807   0.72 18.21 ?  10  LEU   A HB3  1 
ATOM   182  H  HB3  B LEU   A 1 10  ? 7.819  -11.401 10.389  0.28 16.59 ?  10  LEU   A HB3  1 
ATOM   183  H  HG   A LEU   A 1 10  ? 7.224  -14.097 9.776   0.72 21.21 ?  10  LEU   A HG   1 
ATOM   184  H  HG   B LEU   A 1 10  ? 6.223  -13.527 11.163  0.28 16.73 ?  10  LEU   A HG   1 
ATOM   185  H  HD11 A LEU   A 1 10  ? 5.037  -14.619 10.382  0.72 22.71 ?  10  LEU   A HD11 1 
ATOM   186  H  HD11 B LEU   A 1 10  ? 4.431  -12.804 9.825   0.28 17.19 ?  10  LEU   A HD11 1 
ATOM   187  H  HD12 A LEU   A 1 10  ? 5.881  -14.167 11.649  0.72 22.71 ?  10  LEU   A HD12 1 
ATOM   188  H  HD12 B LEU   A 1 10  ? 4.646  -11.826 11.058  0.28 17.19 ?  10  LEU   A HD12 1 
ATOM   189  H  HD13 A LEU   A 1 10  ? 4.859  -13.156 10.974  0.72 22.71 ?  10  LEU   A HD13 1 
ATOM   190  H  HD13 B LEU   A 1 10  ? 5.171  -11.414 9.616   0.28 17.19 ?  10  LEU   A HD13 1 
ATOM   191  H  HD21 A LEU   A 1 10  ? 5.582  -13.788 8.158   0.72 22.77 ?  10  LEU   A HD21 1 
ATOM   192  H  HD21 B LEU   A 1 10  ? 6.235  -14.007 8.845   0.28 16.36 ?  10  LEU   A HD21 1 
ATOM   193  H  HD22 A LEU   A 1 10  ? 5.436  -12.271 8.604   0.72 22.77 ?  10  LEU   A HD22 1 
ATOM   194  H  HD22 B LEU   A 1 10  ? 7.191  -12.756 8.638   0.28 16.36 ?  10  LEU   A HD22 1 
ATOM   195  H  HD23 A LEU   A 1 10  ? 6.787  -12.776 7.939   0.72 22.77 ?  10  LEU   A HD23 1 
ATOM   196  H  HD23 B LEU   A 1 10  ? 7.689  -14.006 9.483   0.28 16.36 ?  10  LEU   A HD23 1 
ATOM   197  N  N    A LYS   A 1 11  ? 9.241  -14.704 11.602  0.72 12.98 ?  11  LYS   A N    1 
ATOM   198  N  N    B LYS   A 1 11  ? 9.271  -14.535 11.961  0.28 12.95 ?  11  LYS   A N    1 
ATOM   199  C  CA   A LYS   A 1 11  ? 10.261 -15.696 11.284  0.72 13.24 ?  11  LYS   A CA   1 
ATOM   200  C  CA   B LYS   A 1 11  ? 10.190 -15.562 11.489  0.28 12.66 ?  11  LYS   A CA   1 
ATOM   201  C  C    A LYS   A 1 11  ? 9.924  -16.324 9.940   0.72 13.06 ?  11  LYS   A C    1 
ATOM   202  C  C    B LYS   A 1 11  ? 9.758  -16.033 10.106  0.28 11.94 ?  11  LYS   A C    1 
ATOM   203  O  O    A LYS   A 1 11  ? 8.882  -16.965 9.806   0.72 14.68 ?  11  LYS   A O    1 
ATOM   204  O  O    B LYS   A 1 11  ? 8.624  -16.488 9.928   0.28 11.39 ?  11  LYS   A O    1 
ATOM   205  C  CB   A LYS   A 1 11  ? 10.297 -16.749 12.390  0.72 13.11 ?  11  LYS   A CB   1 
ATOM   206  C  CB   B LYS   A 1 11  ? 10.209 -16.726 12.477  0.28 12.73 ?  11  LYS   A CB   1 
ATOM   207  C  CG   A LYS   A 1 11  ? 11.306 -17.860 12.208  0.72 13.50 ?  11  LYS   A CG   1 
ATOM   208  C  CG   B LYS   A 1 11  ? 11.272 -17.784 12.209  0.28 12.93 ?  11  LYS   A CG   1 
ATOM   209  C  CD   A LYS   A 1 11  ? 11.367 -18.712 13.474  0.72 13.78 ?  11  LYS   A CD   1 
ATOM   210  C  CD   B LYS   A 1 11  ? 11.380 -18.751 13.389  0.28 13.24 ?  11  LYS   A CD   1 
ATOM   211  C  CE   A LYS   A 1 11  ? 12.336 -19.875 13.347  0.72 13.75 ?  11  LYS   A CE   1 
ATOM   212  C  CE   B LYS   A 1 11  ? 12.415 -19.846 13.154  0.28 13.39 ?  11  LYS   A CE   1 
ATOM   213  N  NZ   A LYS   A 1 11  ? 13.703 -19.410 13.026  0.72 13.87 ?  11  LYS   A NZ   1 
ATOM   214  N  NZ   B LYS   A 1 11  ? 13.801 -19.314 13.055  0.28 13.52 ?  11  LYS   A NZ   1 
ATOM   215  H  H    A LYS   A 1 11  ? 8.554  -15.030 12.012  0.72 15.57 ?  11  LYS   A H    1 
ATOM   216  H  H    B LYS   A 1 11  ? 8.704  -14.807 12.545  0.28 15.54 ?  11  LYS   A H    1 
ATOM   217  H  HA   A LYS   A 1 11  ? 11.126 -15.269 11.223  0.72 15.89 ?  11  LYS   A HA   1 
ATOM   218  H  HA   B LYS   A 1 11  ? 11.079 -15.189 11.419  0.28 15.20 ?  11  LYS   A HA   1 
ATOM   219  H  HB2  A LYS   A 1 11  ? 10.503 -16.302 13.227  0.72 15.73 ?  11  LYS   A HB2  1 
ATOM   220  H  HB2  B LYS   A 1 11  ? 10.365 -16.368 13.364  0.28 15.28 ?  11  LYS   A HB2  1 
ATOM   221  H  HB3  A LYS   A 1 11  ? 9.419  -17.158 12.453  0.72 15.73 ?  11  LYS   A HB3  1 
ATOM   222  H  HB3  B LYS   A 1 11  ? 9.343  -17.163 12.451  0.28 15.28 ?  11  LYS   A HB3  1 
ATOM   223  H  HG2  A LYS   A 1 11  ? 11.036 -18.423 11.466  0.72 16.21 ?  11  LYS   A HG2  1 
ATOM   224  H  HG2  B LYS   A 1 11  ? 11.029 -18.290 11.417  0.28 15.51 ?  11  LYS   A HG2  1 
ATOM   225  H  HG3  A LYS   A 1 11  ? 12.181 -17.477 12.047  0.72 16.21 ?  11  LYS   A HG3  1 
ATOM   226  H  HG3  B LYS   A 1 11  ? 12.132 -17.353 12.084  0.28 15.51 ?  11  LYS   A HG3  1 
ATOM   227  H  HD2  A LYS   A 1 11  ? 11.653 -18.156 14.214  0.72 16.54 ?  11  LYS   A HD2  1 
ATOM   228  H  HD2  B LYS   A 1 11  ? 11.639 -18.255 14.182  0.28 15.89 ?  11  LYS   A HD2  1 
ATOM   229  H  HD3  A LYS   A 1 11  ? 10.482 -19.072 13.653  0.72 16.54 ?  11  LYS   A HD3  1 
ATOM   230  H  HD3  B LYS   A 1 11  ? 10.519 -19.175 13.530  0.28 15.89 ?  11  LYS   A HD3  1 
ATOM   231  H  HE2  A LYS   A 1 11  ? 12.368 -20.355 14.188  0.72 16.51 ?  11  LYS   A HE2  1 
ATOM   232  H  HE2  B LYS   A 1 11  ? 12.386 -20.472 13.894  0.28 16.07 ?  11  LYS   A HE2  1 
ATOM   233  H  HE3  A LYS   A 1 11  ? 12.039 -20.461 12.635  0.72 16.51 ?  11  LYS   A HE3  1 
ATOM   234  H  HE3  B LYS   A 1 11  ? 12.209 -20.303 12.324  0.28 16.07 ?  11  LYS   A HE3  1 
ATOM   235  H  HZ1  A LYS   A 1 11  ? 14.257 -20.101 12.981  0.72 16.65 ?  11  LYS   A HZ1  1 
ATOM   236  H  HZ1  B LYS   A 1 11  ? 14.371 -19.978 12.892  0.28 16.23 ?  11  LYS   A HZ1  1 
ATOM   237  H  HZ2  A LYS   A 1 11  ? 13.704 -18.986 12.241  0.72 16.65 ?  11  LYS   A HZ2  1 
ATOM   238  H  HZ2  B LYS   A 1 11  ? 13.853 -18.720 12.394  0.28 16.23 ?  11  LYS   A HZ2  1 
ATOM   239  H  HZ3  A LYS   A 1 11  ? 13.988 -18.848 13.655  0.72 16.65 ?  11  LYS   A HZ3  1 
ATOM   240  H  HZ3  B LYS   A 1 11  ? 14.031 -18.918 13.818  0.28 16.23 ?  11  LYS   A HZ3  1 
ATOM   241  N  N    A LEU   A 1 12  ? 10.792 -16.147 8.944   0.72 12.00 ?  12  LEU   A N    1 
ATOM   242  N  N    B LEU   A 1 12  ? 10.649 -15.907 9.126   0.28 12.05 ?  12  LEU   A N    1 
ATOM   243  C  CA   A LEU   A 1 12  ? 10.529 -16.739 7.635   0.72 12.28 ?  12  LEU   A CA   1 
ATOM   244  C  CA   B LEU   A 1 12  ? 10.367 -16.409 7.787   0.28 12.37 ?  12  LEU   A CA   1 
ATOM   245  C  C    A LEU   A 1 12  ? 11.125 -18.131 7.496   0.72 12.30 ?  12  LEU   A C    1 
ATOM   246  C  C    B LEU   A 1 12  ? 10.921 -17.815 7.590   0.28 12.40 ?  12  LEU   A C    1 
ATOM   247  O  O    A LEU   A 1 12  ? 10.510 -19.004 6.877   0.72 12.88 ?  12  LEU   A O    1 
ATOM   248  O  O    B LEU   A 1 12  ? 10.226 -18.696 7.074   0.28 12.35 ?  12  LEU   A O    1 
ATOM   249  C  CB   A LEU   A 1 12  ? 11.075 -15.849 6.516   0.72 13.01 ?  12  LEU   A CB   1 
ATOM   250  C  CB   B LEU   A 1 12  ? 10.947 -15.465 6.729   0.28 12.66 ?  12  LEU   A CB   1 
ATOM   251  C  CG   A LEU   A 1 12  ? 10.442 -14.467 6.362   0.72 14.39 ?  12  LEU   A CG   1 
ATOM   252  C  CG   B LEU   A 1 12  ? 10.207 -14.150 6.487   0.28 13.05 ?  12  LEU   A CG   1 
ATOM   253  C  CD1  A LEU   A 1 12  ? 11.146 -13.711 5.248   0.72 15.39 ?  12  LEU   A CD1  1 
ATOM   254  C  CD1  B LEU   A 1 12  ? 10.974 -13.285 5.503   0.28 13.14 ?  12  LEU   A CD1  1 
ATOM   255  C  CD2  A LEU   A 1 12  ? 8.951  -14.576 6.087   0.72 15.16 ?  12  LEU   A CD2  1 
ATOM   256  C  CD2  B LEU   A 1 12  ? 8.803  -14.416 5.972   0.28 13.37 ?  12  LEU   A CD2  1 
ATOM   257  H  H    A LEU   A 1 12  ? 11.522 -15.690 8.993   0.72 14.40 ?  12  LEU   A H    1 
ATOM   258  H  H    B LEU   A 1 12  ? 11.418 -15.527 9.212   0.28 14.46 ?  12  LEU   A H    1 
ATOM   259  H  HA   A LEU   A 1 12  ? 9.570  -16.815 7.513   0.72 14.74 ?  12  LEU   A HA   1 
ATOM   260  H  HA   B LEU   A 1 12  ? 9.404  -16.446 7.666   0.28 14.85 ?  12  LEU   A HA   1 
ATOM   261  H  HB2  A LEU   A 1 12  ? 12.021 -15.712 6.671   0.72 15.61 ?  12  LEU   A HB2  1 
ATOM   262  H  HB2  B LEU   A 1 12  ? 11.851 -15.236 6.991   0.28 15.19 ?  12  LEU   A HB2  1 
ATOM   263  H  HB3  A LEU   A 1 12  ? 10.953 -16.315 5.672   0.72 15.61 ?  12  LEU   A HB3  1 
ATOM   264  H  HB3  B LEU   A 1 12  ? 10.968 -15.938 5.884   0.28 15.19 ?  12  LEU   A HB3  1 
ATOM   265  H  HG   A LEU   A 1 12  ? 10.558 -13.974 7.186   0.72 17.27 ?  12  LEU   A HG   1 
ATOM   266  H  HG   B LEU   A 1 12  ? 10.132 -13.661 7.322   0.28 15.66 ?  12  LEU   A HG   1 
ATOM   267  H  HD11 A LEU   A 1 12  ? 10.739 -12.838 5.155   0.72 18.47 ?  12  LEU   A HD11 1 
ATOM   268  H  HD11 B LEU   A 1 12  ? 10.479 -12.466 5.347   0.28 15.77 ?  12  LEU   A HD11 1 
ATOM   269  H  HD12 A LEU   A 1 12  ? 12.084 -13.619 5.477   0.72 18.47 ?  12  LEU   A HD12 1 
ATOM   270  H  HD12 B LEU   A 1 12  ? 11.844 -13.082 5.876   0.28 15.77 ?  12  LEU   A HD12 1 
ATOM   271  H  HD13 A LEU   A 1 12  ? 11.055 -14.211 4.420   0.72 18.47 ?  12  LEU   A HD13 1 
ATOM   272  H  HD13 B LEU   A 1 12  ? 11.076 -13.773 4.670   0.28 15.77 ?  12  LEU   A HD13 1 
ATOM   273  H  HD21 A LEU   A 1 12  ? 8.604  -13.699 5.863   0.72 18.20 ?  12  LEU   A HD21 1 
ATOM   274  H  HD21 B LEU   A 1 12  ? 8.416  -13.586 5.655   0.28 16.05 ?  12  LEU   A HD21 1 
ATOM   275  H  HD22 A LEU   A 1 12  ? 8.806  -15.187 5.345   0.72 18.20 ?  12  LEU   A HD22 1 
ATOM   276  H  HD22 B LEU   A 1 12  ? 8.851  -15.058 5.245   0.28 16.05 ?  12  LEU   A HD22 1 
ATOM   277  H  HD23 A LEU   A 1 12  ? 8.503  -14.914 6.881   0.72 18.20 ?  12  LEU   A HD23 1 
ATOM   278  H  HD23 B LEU   A 1 12  ? 8.264  -14.778 6.694   0.28 16.05 ?  12  LEU   A HD23 1 
ATOM   279  N  N    A THR   A 1 13  ? 12.327 -18.336 8.028   0.72 12.33 ?  13  THR   A N    1 
ATOM   280  N  N    B THR   A 1 13  ? 12.171 -18.033 7.988   0.28 12.44 ?  13  THR   A N    1 
ATOM   281  C  CA   A THR   A 1 13  ? 13.030 -19.609 7.936   0.72 12.41 ?  13  THR   A CA   1 
ATOM   282  C  CA   B THR   A 1 13  ? 12.815 -19.332 7.875   0.28 12.59 ?  13  THR   A CA   1 
ATOM   283  C  C    A THR   A 1 13  ? 13.810 -19.821 9.229   0.72 12.29 ?  13  THR   A C    1 
ATOM   284  C  C    B THR   A 1 13  ? 13.594 -19.598 9.158   0.28 12.91 ?  13  THR   A C    1 
ATOM   285  O  O    A THR   A 1 13  ? 13.724 -19.034 10.175  0.72 12.74 ?  13  THR   A O    1 
ATOM   286  O  O    B THR   A 1 13  ? 13.484 -18.867 10.147  0.28 13.48 ?  13  THR   A O    1 
ATOM   287  C  CB   A THR   A 1 13  ? 14.004 -19.632 6.753   0.72 12.74 ?  13  THR   A CB   1 
ATOM   288  C  CB   B THR   A 1 13  ? 13.752 -19.375 6.662   0.28 12.72 ?  13  THR   A CB   1 
ATOM   289  O  OG1  A THR   A 1 13  ? 15.064 -18.715 7.024   0.72 12.80 ?  13  THR   A OG1  1 
ATOM   290  O  OG1  B THR   A 1 13  ? 14.807 -18.428 6.853   0.28 13.35 ?  13  THR   A OG1  1 
ATOM   291  C  CG2  A THR   A 1 13  ? 13.328 -19.259 5.443   0.72 14.04 ?  13  THR   A CG2  1 
ATOM   292  C  CG2  B THR   A 1 13  ? 13.002 -19.060 5.374   0.28 13.05 ?  13  THR   A CG2  1 
ATOM   293  H  H    A THR   A 1 13  ? 12.769 -17.735 8.447   0.72 14.79 ?  13  THR   A H    1 
ATOM   294  H  H    B THR   A 1 13  ? 12.673 -17.423 8.324   0.28 14.93 ?  13  THR   A H    1 
ATOM   295  H  HA   A THR   A 1 13  ? 12.396 -20.335 7.825   0.72 14.89 ?  13  THR   A HA   1 
ATOM   296  H  HA   B THR   A 1 13  ? 12.138 -20.020 7.764   0.28 15.12 ?  13  THR   A HA   1 
ATOM   297  H  HB   A THR   A 1 13  ? 14.376 -20.523 6.653   0.72 15.29 ?  13  THR   A HB   1 
ATOM   298  H  HB   B THR   A 1 13  ? 14.135 -20.261 6.583   0.28 15.26 ?  13  THR   A HB   1 
ATOM   299  H  HG1  A THR   A 1 13  ? 15.726 -19.119 7.344   0.72 15.37 ?  13  THR   A HG1  1 
ATOM   300  H  HG1  B THR   A 1 13  ? 15.327 -18.434 6.195   0.28 16.02 ?  13  THR   A HG1  1 
ATOM   301  H  HG21 A THR   A 1 13  ? 13.936 -19.416 4.699   0.72 16.85 ?  13  THR   A HG21 1 
ATOM   302  H  HG21 B THR   A 1 13  ? 13.584 -19.207 4.611   0.28 15.67 ?  13  THR   A HG21 1 
ATOM   303  H  HG22 A THR   A 1 13  ? 12.535 -19.802 5.317   0.72 16.85 ?  13  THR   A HG22 1 
ATOM   304  H  HG22 B THR   A 1 13  ? 12.227 -19.638 5.293   0.28 15.67 ?  13  THR   A HG22 1 
ATOM   305  H  HG23 A THR   A 1 13  ? 13.077 -18.325 5.452   0.72 16.85 ?  13  THR   A HG23 1 
ATOM   306  H  HG23 B THR   A 1 13  ? 12.709 -18.137 5.375   0.28 15.67 ?  13  THR   A HG23 1 
ATOM   307  N  N    A ASP   A 1 14  ? 14.615 -20.883 9.249   0.72 13.03 ?  14  ASP   A N    1 
ATOM   308  N  N    B ASP   A 1 14  ? 14.403 -20.657 9.123   0.28 13.05 ?  14  ASP   A N    1 
ATOM   309  C  CA   A ASP   A 1 14  ? 15.469 -21.145 10.401  0.72 13.95 ?  14  ASP   A CA   1 
ATOM   310  C  CA   B ASP   A 1 14  ? 15.244 -21.008 10.261  0.28 13.28 ?  14  ASP   A CA   1 
ATOM   311  C  C    A ASP   A 1 14  ? 16.272 -19.908 10.796  0.72 13.79 ?  14  ASP   A C    1 
ATOM   312  C  C    B ASP   A 1 14  ? 16.181 -19.874 10.656  0.28 12.63 ?  14  ASP   A C    1 
ATOM   313  O  O    A ASP   A 1 14  ? 16.438 -19.622 11.989  0.72 15.05 ?  14  ASP   A O    1 
ATOM   314  O  O    B ASP   A 1 14  ? 16.576 -19.780 11.825  0.28 13.12 ?  14  ASP   A O    1 
ATOM   315  C  CB   A ASP   A 1 14  ? 16.414 -22.305 10.088  0.72 16.28 ?  14  ASP   A CB   1 
ATOM   316  C  CB   B ASP   A 1 14  ? 16.078 -22.240 9.919   0.28 14.52 ?  14  ASP   A CB   1 
ATOM   317  C  CG   A ASP   A 1 14  ? 17.248 -22.714 11.286  0.72 19.80 ?  14  ASP   A CG   1 
ATOM   318  C  CG   B ASP   A 1 14  ? 17.160 -22.509 10.946  0.28 15.89 ?  14  ASP   A CG   1 
ATOM   319  O  OD1  A ASP   A 1 14  ? 16.648 -23.150 12.295  0.72 21.28 ?  14  ASP   A OD1  1 
ATOM   320  O  OD1  B ASP   A 1 14  ? 16.822 -22.933 12.070  0.28 16.31 ?  14  ASP   A OD1  1 
ATOM   321  O  OD2  A ASP   A 1 14  ? 18.489 -22.611 11.214  0.72 22.09 -1 14  ASP   A OD2  1 
ATOM   322  O  OD2  B ASP   A 1 14  ? 18.348 -22.279 10.632  0.28 16.41 -1 14  ASP   A OD2  1 
ATOM   323  H  H    A ASP   A 1 14  ? 14.697 -21.454 8.609   0.72 15.64 ?  14  ASP   A H    1 
ATOM   324  H  H    B ASP   A 1 14  ? 14.470 -21.185 8.453   0.28 15.66 ?  14  ASP   A H    1 
ATOM   325  H  HA   A ASP   A 1 14  ? 14.915 -21.402 11.154  0.72 16.75 ?  14  ASP   A HA   1 
ATOM   326  H  HA   B ASP   A 1 14  ? 14.679 -21.219 11.023  0.28 15.94 ?  14  ASP   A HA   1 
ATOM   327  H  HB2  A ASP   A 1 14  ? 15.882 -23.076 9.808   0.72 19.54 ?  14  ASP   A HB2  1 
ATOM   328  H  HB2  B ASP   A 1 14  ? 15.489 -23.010 9.863   0.28 17.43 ?  14  ASP   A HB2  1 
ATOM   329  H  HB3  A ASP   A 1 14  ? 17.012 -22.046 9.373   0.72 19.54 ?  14  ASP   A HB3  1 
ATOM   330  H  HB3  B ASP   A 1 14  ? 16.512 -22.094 9.064   0.28 17.43 ?  14  ASP   A HB3  1 
ATOM   331  N  N    A ASN   A 1 15  ? 16.766 -19.149 9.810   0.72 12.97 ?  15  ASN   A N    1 
ATOM   332  N  N    B ASN   A 1 15  ? 16.564 -19.013 9.705   0.28 11.82 ?  15  ASN   A N    1 
ATOM   333  C  CA   A ASN   A 1 15  ? 17.743 -18.098 10.071  0.72 13.26 ?  15  ASN   A CA   1 
ATOM   334  C  CA   B ASN   A 1 15  ? 17.592 -18.020 9.997   0.28 11.76 ?  15  ASN   A CA   1 
ATOM   335  C  C    A ASN   A 1 15  ? 17.343 -16.703 9.603   0.72 13.43 ?  15  ASN   A C    1 
ATOM   336  C  C    B ASN   A 1 15  ? 17.296 -16.637 9.424   0.28 12.05 ?  15  ASN   A C    1 
ATOM   337  O  O    A ASN   A 1 15  ? 18.057 -15.744 9.930   0.72 13.26 ?  15  ASN   A O    1 
ATOM   338  O  O    B ASN   A 1 15  ? 18.216 -15.814 9.330   0.28 12.19 ?  15  ASN   A O    1 
ATOM   339  C  CB   A ASN   A 1 15  ? 19.108 -18.464 9.455   0.72 13.50 ?  15  ASN   A CB   1 
ATOM   340  C  CB   B ASN   A 1 15  ? 18.957 -18.479 9.474   0.28 11.80 ?  15  ASN   A CB   1 
ATOM   341  C  CG   A ASN   A 1 15  ? 19.065 -18.560 7.944   0.72 13.92 ?  15  ASN   A CG   1 
ATOM   342  C  CG   B ASN   A 1 15  ? 18.993 -18.582 7.966   0.28 12.22 ?  15  ASN   A CG   1 
ATOM   343  O  OD1  A ASN   A 1 15  ? 18.371 -19.417 7.385   0.72 14.23 ?  15  ASN   A OD1  1 
ATOM   344  O  OD1  B ASN   A 1 15  ? 18.163 -19.264 7.358   0.28 12.63 ?  15  ASN   A OD1  1 
ATOM   345  N  ND2  A ASN   A 1 15  ? 19.812 -17.682 7.268   0.72 13.90 ?  15  ASN   A ND2  1 
ATOM   346  N  ND2  B ASN   A 1 15  ? 19.938 -17.885 7.348   0.28 12.15 ?  15  ASN   A ND2  1 
ATOM   347  H  H    A ASN   A 1 15  ? 16.553 -19.232 8.987   0.72 15.56 ?  15  ASN   A H    1 
ATOM   348  H  H    B ASN   A 1 15  ? 16.249 -18.987 8.906   0.28 14.19 ?  15  ASN   A H    1 
ATOM   349  H  HA   A ASN   A 1 15  ? 17.883 -18.049 11.032  0.72 15.91 ?  15  ASN   A HA   1 
ATOM   350  H  HA   B ASN   A 1 15  ? 17.664 -17.921 10.957  0.28 14.11 ?  15  ASN   A HA   1 
ATOM   351  H  HB2  A ASN   A 1 15  ? 19.759 -17.781 9.695   0.72 16.20 ?  15  ASN   A HB2  1 
ATOM   352  H  HB2  B ASN   A 1 15  ? 19.631 -17.836 9.752   0.28 14.17 ?  15  ASN   A HB2  1 
ATOM   353  H  HB3  A ASN   A 1 15  ? 19.396 -19.324 9.800   0.72 16.20 ?  15  ASN   A HB3  1 
ATOM   354  H  HB3  B ASN   A 1 15  ? 19.158 -19.352 9.841   0.28 14.17 ?  15  ASN   A HB3  1 
ATOM   355  H  HD21 A ASN   A 1 15  ? 19.824 -17.696 6.408   0.72 16.68 ?  15  ASN   A HD21 1 
ATOM   356  H  HD21 B ASN   A 1 15  ? 19.993 -17.905 6.492   0.28 14.58 ?  15  ASN   A HD21 1 
ATOM   357  H  HD22 A ASN   A 1 15  ? 20.290 -17.102 7.692   0.72 16.68 ?  15  ASN   A HD22 1 
ATOM   358  H  HD22 B ASN   A 1 15  ? 20.500 -17.420 7.806   0.28 14.58 ?  15  ASN   A HD22 1 
ATOM   359  N  N    A VAL   A 1 16  ? 16.252 -16.556 8.846   0.72 12.73 ?  16  VAL   A N    1 
ATOM   360  N  N    B VAL   A 1 16  ? 16.054 -16.343 9.050   0.28 11.69 ?  16  VAL   A N    1 
ATOM   361  C  CA   A VAL   A 1 16  ? 15.843 -15.277 8.268   0.72 12.91 ?  16  VAL   A CA   1 
ATOM   362  C  CA   B VAL   A 1 16  ? 15.705 -15.049 8.477   0.28 11.29 ?  16  VAL   A CA   1 
ATOM   363  C  C    A VAL   A 1 16  ? 14.568 -14.785 8.945   0.72 12.60 ?  16  VAL   A C    1 
ATOM   364  C  C    B VAL   A 1 16  ? 14.437 -14.541 9.147   0.28 11.46 ?  16  VAL   A C    1 
ATOM   365  O  O    A VAL   A 1 16  ? 13.558 -15.502 9.010   0.72 12.62 ?  16  VAL   A O    1 
ATOM   366  O  O    B VAL   A 1 16  ? 13.445 -15.272 9.256   0.28 11.62 ?  16  VAL   A O    1 
ATOM   367  C  CB   A VAL   A 1 16  ? 15.662 -15.362 6.741   0.72 13.50 ?  16  VAL   A CB   1 
ATOM   368  C  CB   B VAL   A 1 16  ? 15.530 -15.115 6.947   0.28 11.14 ?  16  VAL   A CB   1 
ATOM   369  C  CG1  A VAL   A 1 16  ? 15.230 -14.008 6.179   0.72 14.11 ?  16  VAL   A CG1  1 
ATOM   370  C  CG1  B VAL   A 1 16  ? 15.160 -13.743 6.394   0.28 11.18 ?  16  VAL   A CG1  1 
ATOM   371  C  CG2  A VAL   A 1 16  ? 16.942 -15.836 6.060   0.72 14.64 ?  16  VAL   A CG2  1 
ATOM   372  C  CG2  B VAL   A 1 16  ? 16.794 -15.640 6.273   0.28 12.09 ?  16  VAL   A CG2  1 
ATOM   373  H  H    A VAL   A 1 16  ? 15.734 -17.207 8.643   0.72 15.28 ?  16  VAL   A H    1 
ATOM   374  H  H    B VAL   A 1 16  ? 15.381 -16.872 9.131   0.28 14.03 ?  16  VAL   A H    1 
ATOM   375  H  HA   A VAL   A 1 16  ? 16.545 -14.626 8.436   0.72 15.49 ?  16  VAL   A HA   1 
ATOM   376  H  HA   B VAL   A 1 16  ? 16.410 -14.410 8.669   0.28 13.55 ?  16  VAL   A HA   1 
ATOM   377  H  HB   A VAL   A 1 16  ? 14.965 -16.007 6.543   0.72 16.20 ?  16  VAL   A HB   1 
ATOM   378  H  HB   B VAL   A 1 16  ? 14.806 -15.722 6.740   0.28 13.37 ?  16  VAL   A HB   1 
ATOM   379  H  HG11 A VAL   A 1 16  ? 15.312 -14.030 5.212   0.72 16.94 ?  16  VAL   A HG11 1 
ATOM   380  H  HG11 B VAL   A 1 16  ? 15.251 -13.759 5.428   0.28 13.42 ?  16  VAL   A HG11 1 
ATOM   381  H  HG12 A VAL   A 1 16  ? 14.307 -13.843 6.426   0.72 16.94 ?  16  VAL   A HG12 1 
ATOM   382  H  HG12 B VAL   A 1 16  ? 14.241 -13.541 6.633   0.28 13.42 ?  16  VAL   A HG12 1 
ATOM   383  H  HG13 A VAL   A 1 16  ? 15.804 -13.318 6.543   0.72 16.94 ?  16  VAL   A HG13 1 
ATOM   384  H  HG13 B VAL   A 1 16  ? 15.756 -13.078 6.769   0.28 13.42 ?  16  VAL   A HG13 1 
ATOM   385  H  HG21 A VAL   A 1 16  ? 16.814 -15.807 5.098   0.72 17.57 ?  16  VAL   A HG21 1 
ATOM   386  H  HG21 B VAL   A 1 16  ? 16.704 -15.542 5.310   0.28 14.51 ?  16  VAL   A HG21 1 
ATOM   387  H  HG22 A VAL   A 1 16  ? 17.670 -15.248 6.314   0.72 17.57 ?  16  VAL   A HG22 1 
ATOM   388  H  HG22 B VAL   A 1 16  ? 17.557 -15.133 6.586   0.28 14.51 ?  16  VAL   A HG22 1 
ATOM   389  H  HG23 A VAL   A 1 16  ? 17.133 -16.743 6.341   0.72 17.57 ?  16  VAL   A HG23 1 
ATOM   390  H  HG23 B VAL   A 1 16  ? 16.904 -16.576 6.500   0.28 14.51 ?  16  VAL   A HG23 1 
ATOM   391  N  N    A TYR   A 1 17  ? 14.611 -13.523 9.377   0.72 12.53 ?  17  TYR   A N    1 
ATOM   392  N  N    B TYR   A 1 17  ? 14.476 -13.283 9.583   0.28 11.70 ?  17  TYR   A N    1 
ATOM   393  C  CA   A TYR   A 1 17  ? 13.551 -12.846 10.107  0.72 12.47 ?  17  TYR   A CA   1 
ATOM   394  C  CA   B TYR   A 1 17  ? 13.374 -12.615 10.253  0.28 11.81 ?  17  TYR   A CA   1 
ATOM   395  C  C    A TYR   A 1 17  ? 13.274 -11.509 9.430   0.72 12.61 ?  17  TYR   A C    1 
ATOM   396  C  C    B TYR   A 1 17  ? 13.127 -11.283 9.563   0.28 12.26 ?  17  TYR   A C    1 
ATOM   397  O  O    A TYR   A 1 17  ? 14.144 -10.961 8.749   0.72 11.80 ?  17  TYR   A O    1 
ATOM   398  O  O    B TYR   A 1 17  ? 14.078 -10.581 9.213   0.28 12.02 ?  17  TYR   A O    1 
ATOM   399  C  CB   A TYR   A 1 17  ? 13.993 -12.600 11.554  0.72 12.68 ?  17  TYR   A CB   1 
ATOM   400  C  CB   B TYR   A 1 17  ? 13.731 -12.383 11.721  0.28 11.85 ?  17  TYR   A CB   1 
ATOM   401  C  CG   A TYR   A 1 17  ? 14.207 -13.866 12.357  0.72 13.36 ?  17  TYR   A CG   1 
ATOM   402  C  CG   B TYR   A 1 17  ? 13.865 -13.665 12.508  0.28 11.64 ?  17  TYR   A CG   1 
ATOM   403  C  CD1  A TYR   A 1 17  ? 15.378 -14.613 12.243  0.72 14.09 ?  17  TYR   A CD1  1 
ATOM   404  C  CD1  B TYR   A 1 17  ? 15.007 -14.452 12.413  0.28 11.61 ?  17  TYR   A CD1  1 
ATOM   405  C  CD2  A TYR   A 1 17  ? 13.230 -14.324 13.232  0.72 13.57 ?  17  TYR   A CD2  1 
ATOM   406  C  CD2  B TYR   A 1 17  ? 12.838 -14.100 13.335  0.28 11.61 ?  17  TYR   A CD2  1 
ATOM   407  C  CE1  A TYR   A 1 17  ? 15.561 -15.784 12.976  0.72 14.53 ?  17  TYR   A CE1  1 
ATOM   408  C  CE1  B TYR   A 1 17  ? 15.127 -15.635 13.126  0.28 11.39 ?  17  TYR   A CE1  1 
ATOM   409  C  CE2  A TYR   A 1 17  ? 13.404 -15.490 13.967  0.72 14.12 ?  17  TYR   A CE2  1 
ATOM   410  C  CE2  B TYR   A 1 17  ? 12.947 -15.282 14.052  0.28 11.39 ?  17  TYR   A CE2  1 
ATOM   411  C  CZ   A TYR   A 1 17  ? 14.569 -16.216 13.837  0.72 14.39 ?  17  TYR   A CZ   1 
ATOM   412  C  CZ   B TYR   A 1 17  ? 14.093 -16.045 13.945  0.28 11.36 ?  17  TYR   A CZ   1 
ATOM   413  O  OH   A TYR   A 1 17  ? 14.738 -17.366 14.580  0.72 14.91 ?  17  TYR   A OH   1 
ATOM   414  O  OH   B TYR   A 1 17  ? 14.195 -17.217 14.662  0.28 11.53 ?  17  TYR   A OH   1 
ATOM   415  H  H    A TYR   A 1 17  ? 15.294 -13.011 9.233   0.72 15.04 ?  17  TYR   A H    1 
ATOM   416  H  H    B TYR   A 1 17  ? 15.165 -12.771 9.498   0.28 14.05 ?  17  TYR   A H    1 
ATOM   417  H  HA   A TYR   A 1 17  ? 12.748 -13.387 10.095  0.72 14.97 ?  17  TYR   A HA   1 
ATOM   418  H  HA   B TYR   A 1 17  ? 12.569 -13.153 10.204  0.28 14.17 ?  17  TYR   A HA   1 
ATOM   419  H  HB2  A TYR   A 1 17  ? 14.827 -12.111 11.547  0.72 15.22 ?  17  TYR   A HB2  1 
ATOM   420  H  HB2  B TYR   A 1 17  ? 14.570 -11.899 11.779  0.28 14.23 ?  17  TYR   A HB2  1 
ATOM   421  H  HB3  A TYR   A 1 17  ? 13.307 -12.082 11.998  0.72 15.22 ?  17  TYR   A HB3  1 
ATOM   422  H  HB3  B TYR   A 1 17  ? 13.024 -11.865 12.122  0.28 14.23 ?  17  TYR   A HB3  1 
ATOM   423  H  HD1  A TYR   A 1 17  ? 16.043 -14.332 11.660  0.72 16.91 ?  17  TYR   A HD1  1 
ATOM   424  H  HD1  B TYR   A 1 17  ? 15.704 -14.177 11.860  0.28 13.94 ?  17  TYR   A HD1  1 
ATOM   425  H  HD2  A TYR   A 1 17  ? 12.437 -13.851 13.326  0.72 16.28 ?  17  TYR   A HD2  1 
ATOM   426  H  HD2  B TYR   A 1 17  ? 12.063 -13.588 13.410  0.28 13.94 ?  17  TYR   A HD2  1 
ATOM   427  H  HE1  A TYR   A 1 17  ? 16.349 -16.275 12.889  0.72 17.44 ?  17  TYR   A HE1  1 
ATOM   428  H  HE1  B TYR   A 1 17  ? 15.897 -16.150 13.049  0.28 13.67 ?  17  TYR   A HE1  1 
ATOM   429  H  HE2  A TYR   A 1 17  ? 12.740 -15.785 14.550  0.72 16.95 ?  17  TYR   A HE2  1 
ATOM   430  H  HE2  B TYR   A 1 17  ? 12.250 -15.559 14.602  0.28 13.67 ?  17  TYR   A HE2  1 
ATOM   431  H  HH   A TYR   A 1 17  ? 15.488 -17.712 14.421  0.72 17.89 ?  17  TYR   A HH   1 
ATOM   432  H  HH   B TYR   A 1 17  ? 13.445 -17.427 14.974  0.28 13.84 ?  17  TYR   A HH   1 
ATOM   433  N  N    A ILE   A 1 18  ? 12.072 -10.956 9.627   0.72 13.00 ?  18  ILE   A N    1 
ATOM   434  N  N    B ILE   A 1 18  ? 11.855 -10.934 9.363   0.28 12.59 ?  18  ILE   A N    1 
ATOM   435  C  CA   A ILE   A 1 18  ? 11.676 -9.752  8.895   0.72 13.48 ?  18  ILE   A CA   1 
ATOM   436  C  CA   B ILE   A 1 18  ? 11.476 -9.738  8.614   0.28 13.06 ?  18  ILE   A CA   1 
ATOM   437  C  C    A ILE   A 1 18  ? 10.720 -8.900  9.721   0.72 14.32 ?  18  ILE   A C    1 
ATOM   438  C  C    B ILE   A 1 18  ? 10.519 -8.900  9.452   0.28 14.28 ?  18  ILE   A C    1 
ATOM   439  O  O    A ILE   A 1 18  ? 9.910  -9.411  10.502  0.72 14.76 ?  18  ILE   A O    1 
ATOM   440  O  O    B ILE   A 1 18  ? 9.656  -9.441  10.151  0.28 14.26 ?  18  ILE   A O    1 
ATOM   441  C  CB   A ILE   A 1 18  ? 11.090 -10.124 7.513   0.72 13.78 ?  18  ILE   A CB   1 
ATOM   442  C  CB   B ILE   A 1 18  ? 10.854 -10.110 7.249   0.28 13.08 ?  18  ILE   A CB   1 
ATOM   443  C  CG1  A ILE   A 1 18  ? 10.969 -8.893  6.616   0.72 14.85 ?  18  ILE   A CG1  1 
ATOM   444  C  CG1  B ILE   A 1 18  ? 10.939 -8.934  6.273   0.28 13.42 ?  18  ILE   A CG1  1 
ATOM   445  C  CG2  A ILE   A 1 18  ? 9.768  -10.880 7.667   0.72 13.68 ?  18  ILE   A CG2  1 
ATOM   446  C  CG2  B ILE   A 1 18  ? 9.416  -10.608 7.411   0.28 13.12 ?  18  ILE   A CG2  1 
ATOM   447  C  CD1  A ILE   A 1 18  ? 10.641 -9.249  5.189   0.72 16.46 ?  18  ILE   A CD1  1 
ATOM   448  C  CD1  B ILE   A 1 18  ? 10.874 -9.360  4.822   0.28 14.06 ?  18  ILE   A CD1  1 
ATOM   449  H  H    A ILE   A 1 18  ? 11.484 -11.269 10.166  0.72 15.61 ?  18  ILE   A H    1 
ATOM   450  H  H    B ILE   A 1 18  ? 11.182 -11.388 9.650   0.28 15.11 ?  18  ILE   A H    1 
ATOM   451  H  HA   A ILE   A 1 18  ? 12.483 -9.228  8.739   0.72 16.18 ?  18  ILE   A HA   1 
ATOM   452  H  HA   B ILE   A 1 18  ? 12.269 -9.209  8.446   0.28 15.68 ?  18  ILE   A HA   1 
ATOM   453  H  HB   A ILE   A 1 18  ? 11.722 -10.723 7.091   0.72 16.54 ?  18  ILE   A HB   1 
ATOM   454  H  HB   B ILE   A 1 18  ? 11.373 -10.834 6.878   0.28 15.70 ?  18  ILE   A HB   1 
ATOM   455  H  HG12 A ILE   A 1 18  ? 10.266 -8.320  6.952   0.72 17.83 ?  18  ILE   A HG12 1 
ATOM   456  H  HG12 B ILE   A 1 18  ? 10.201 -8.328  6.439   0.28 16.10 ?  18  ILE   A HG12 1 
ATOM   457  H  HG13 A ILE   A 1 18  ? 11.817 -8.413  6.615   0.72 17.83 ?  18  ILE   A HG13 1 
ATOM   458  H  HG13 B ILE   A 1 18  ? 11.782 -8.472  6.407   0.28 16.10 ?  18  ILE   A HG13 1 
ATOM   459  H  HG21 A ILE   A 1 18  ? 9.508  -11.222 6.799   0.72 16.42 ?  18  ILE   A HG21 1 
ATOM   460  H  HG21 B ILE   A 1 18  ? 9.139  -11.039 6.585   0.28 15.75 ?  18  ILE   A HG21 1 
ATOM   461  H  HG22 A ILE   A 1 18  ? 9.900  -11.612 8.288   0.72 16.42 ?  18  ILE   A HG22 1 
ATOM   462  H  HG22 B ILE   A 1 18  ? 9.385  -11.245 8.141   0.28 15.75 ?  18  ILE   A HG22 1 
ATOM   463  H  HG23 A ILE   A 1 18  ? 9.097  -10.271 8.004   0.72 16.42 ?  18  ILE   A HG23 1 
ATOM   464  H  HG23 B ILE   A 1 18  ? 8.834  -9.857  7.600   0.28 15.75 ?  18  ILE   A HG23 1 
ATOM   465  H  HD11 A ILE   A 1 18  ? 10.670 -8.444  4.646   0.72 19.75 ?  18  ILE   A HD11 1 
ATOM   466  H  HD11 B ILE   A 1 18  ? 10.936 -8.573  4.259   0.28 16.88 ?  18  ILE   A HD11 1 
ATOM   467  H  HD12 A ILE   A 1 18  ? 11.295 -9.889  4.863   0.72 19.75 ?  18  ILE   A HD12 1 
ATOM   468  H  HD12 B ILE   A 1 18  ? 11.613 -9.960  4.636   0.28 16.88 ?  18  ILE   A HD12 1 
ATOM   469  H  HD13 A ILE   A 1 18  ? 9.754  -9.638  5.156   0.72 19.75 ?  18  ILE   A HD13 1 
ATOM   470  H  HD13 B ILE   A 1 18  ? 10.031 -9.814  4.665   0.28 16.88 ?  18  ILE   A HD13 1 
ATOM   471  N  N    A LYS   A 1 19  ? 10.800 -7.583  9.508   0.72 14.65 ?  19  LYS   A N    1 
ATOM   472  N  N    B LYS   A 1 19  ? 10.668 -7.575  9.376   0.28 15.45 ?  19  LYS   A N    1 
ATOM   473  C  CA   A LYS   A 1 19  ? 9.994  -6.616  10.243  0.72 15.70 ?  19  LYS   A CA   1 
ATOM   474  C  CA   B LYS   A 1 19  ? 9.858  -6.667  10.180  0.28 16.57 ?  19  LYS   A CA   1 
ATOM   475  C  C    A LYS   A 1 19  ? 9.766  -5.386  9.375   0.72 16.06 ?  19  LYS   A C    1 
ATOM   476  C  C    B LYS   A 1 19  ? 9.776  -5.319  9.479   0.28 17.06 ?  19  LYS   A C    1 
ATOM   477  O  O    A LYS   A 1 19  ? 10.622 -5.009  8.573   0.72 15.74 ?  19  LYS   A O    1 
ATOM   478  O  O    B LYS   A 1 19  ? 10.793 -4.807  9.003   0.28 17.10 ?  19  LYS   A O    1 
ATOM   479  C  CB   A LYS   A 1 19  ? 10.726 -6.210  11.526  0.72 16.63 ?  19  LYS   A CB   1 
ATOM   480  C  CB   B LYS   A 1 19  ? 10.465 -6.495  11.581  0.28 17.14 ?  19  LYS   A CB   1 
ATOM   481  C  CG   A LYS   A 1 19  ? 9.981  -5.309  12.490  0.72 18.39 ?  19  LYS   A CG   1 
ATOM   482  C  CG   B LYS   A 1 19  ? 9.839  -5.383  12.416  0.28 17.98 ?  19  LYS   A CG   1 
ATOM   483  C  CD   A LYS   A 1 19  ? 10.902 -4.996  13.667  0.72 19.52 ?  19  LYS   A CD   1 
ATOM   484  C  CD   B LYS   A 1 19  ? 10.619 -5.152  13.698  0.28 18.65 ?  19  LYS   A CD   1 
ATOM   485  C  CE   A LYS   A 1 19  ? 10.249 -4.129  14.727  0.72 20.34 ?  19  LYS   A CE   1 
ATOM   486  C  CE   B LYS   A 1 19  ? 9.999  -4.048  14.540  0.28 18.95 ?  19  LYS   A CE   1 
ATOM   487  N  NZ   A LYS   A 1 19  ? 11.164 -3.946  15.891  0.72 20.54 ?  19  LYS   A NZ   1 
ATOM   488  N  NZ   B LYS   A 1 19  ? 10.777 -3.792  15.783  0.28 19.00 ?  19  LYS   A NZ   1 
ATOM   489  H  H    A LYS   A 1 19  ? 11.329 -7.227  8.927   0.72 17.58 ?  19  LYS   A H    1 
ATOM   490  H  H    B LYS   A 1 19  ? 11.230 -7.172  8.856   0.28 18.54 ?  19  LYS   A H    1 
ATOM   491  H  HA   A LYS   A 1 19  ? 9.142  -7.014  10.470  0.72 18.84 ?  19  LYS   A HA   1 
ATOM   492  H  HA   B LYS   A 1 19  ? 8.963  -7.022  10.277  0.28 19.88 ?  19  LYS   A HA   1 
ATOM   493  H  HB2  A LYS   A 1 19  ? 10.957 -7.016  12.006  0.72 19.96 ?  19  LYS   A HB2  1 
ATOM   494  H  HB2  B LYS   A 1 19  ? 10.354 -7.328  12.075  0.28 20.57 ?  19  LYS   A HB2  1 
ATOM   495  H  HB3  A LYS   A 1 19  ? 11.541 -5.745  11.269  0.72 19.96 ?  19  LYS   A HB3  1 
ATOM   496  H  HB3  B LYS   A 1 19  ? 11.408 -6.297  11.491  0.28 20.57 ?  19  LYS   A HB3  1 
ATOM   497  H  HG2  A LYS   A 1 19  ? 9.742  -4.478  12.048  0.72 22.07 ?  19  LYS   A HG2  1 
ATOM   498  H  HG2  B LYS   A 1 19  ? 9.844  -4.551  11.918  0.28 21.57 ?  19  LYS   A HG2  1 
ATOM   499  H  HG3  A LYS   A 1 19  ? 9.191  -5.764  12.819  0.72 22.07 ?  19  LYS   A HG3  1 
ATOM   500  H  HG3  B LYS   A 1 19  ? 8.931  -5.629  12.650  0.28 21.57 ?  19  LYS   A HG3  1 
ATOM   501  H  HD2  A LYS   A 1 19  ? 11.168 -5.830  14.087  0.72 23.43 ?  19  LYS   A HD2  1 
ATOM   502  H  HD2  B LYS   A 1 19  ? 10.624 -5.967  14.222  0.28 22.39 ?  19  LYS   A HD2  1 
ATOM   503  H  HD3  A LYS   A 1 19  ? 11.685 -4.529  13.338  0.72 23.43 ?  19  LYS   A HD3  1 
ATOM   504  H  HD3  B LYS   A 1 19  ? 11.528 -4.890  13.477  0.28 22.39 ?  19  LYS   A HD3  1 
ATOM   505  H  HE2  A LYS   A 1 19  ? 10.051 -3.254  14.354  0.72 24.40 ?  19  LYS   A HE2  1 
ATOM   506  H  HE2  B LYS   A 1 19  ? 9.976  -3.226  14.025  0.28 22.75 ?  19  LYS   A HE2  1 
ATOM   507  H  HE3  A LYS   A 1 19  ? 9.436  -4.554  15.041  0.72 24.40 ?  19  LYS   A HE3  1 
ATOM   508  H  HE3  B LYS   A 1 19  ? 9.100  -4.308  14.795  0.28 22.75 ?  19  LYS   A HE3  1 
ATOM   509  H  HZ1  A LYS   A 1 19  ? 10.760 -3.472  16.526  0.72 24.65 ?  19  LYS   A HZ1  1 
ATOM   510  H  HZ1  B LYS   A 1 19  ? 10.393 -3.143  16.256  0.28 22.80 ?  19  LYS   A HZ1  1 
ATOM   511  H  HZ2  A LYS   A 1 19  ? 11.394 -4.739  16.224  0.72 24.65 ?  19  LYS   A HZ2  1 
ATOM   512  H  HZ2  B LYS   A 1 19  ? 10.810 -4.531  16.279  0.28 22.80 ?  19  LYS   A HZ2  1 
ATOM   513  H  HZ3  A LYS   A 1 19  ? 11.900 -3.517  15.635  0.72 24.65 ?  19  LYS   A HZ3  1 
ATOM   514  H  HZ3  B LYS   A 1 19  ? 11.608 -3.546  15.577  0.28 22.80 ?  19  LYS   A HZ3  1 
ATOM   515  N  N    A ASN   A 1 20  ? 8.598  -4.766  9.534   0.72 17.19 ?  20  ASN   A N    1 
ATOM   516  N  N    B ASN   A 1 20  ? 8.572  -4.749  9.418   0.28 17.55 ?  20  ASN   A N    1 
ATOM   517  C  CA   A ASN   A 1 20  ? 8.346  -3.448  8.962   0.72 18.54 ?  20  ASN   A CA   1 
ATOM   518  C  CA   B ASN   A 1 20  ? 8.395  -3.402  8.881   0.28 17.91 ?  20  ASN   A CA   1 
ATOM   519  C  C    A ASN   A 1 20  ? 8.975  -2.435  9.906   0.72 19.17 ?  20  ASN   A C    1 
ATOM   520  C  C    B ASN   A 1 20  ? 9.007  -2.398  9.849   0.28 17.93 ?  20  ASN   A C    1 
ATOM   521  O  O    A ASN   A 1 20  ? 8.464  -2.198  11.004  0.72 20.48 ?  20  ASN   A O    1 
ATOM   522  O  O    B ASN   A 1 20  ? 8.439  -2.121  10.910  0.28 18.43 ?  20  ASN   A O    1 
ATOM   523  C  CB   A ASN   A 1 20  ? 6.843  -3.226  8.807   0.72 20.07 ?  20  ASN   A CB   1 
ATOM   524  C  CB   B ASN   A 1 20  ? 6.912  -3.115  8.655   0.28 18.38 ?  20  ASN   A CB   1 
ATOM   525  C  CG   A ASN   A 1 20  ? 6.481  -1.797  8.416   0.72 21.81 ?  20  ASN   A CG   1 
ATOM   526  C  CG   B ASN   A 1 20  ? 6.641  -1.657  8.304   0.28 19.16 ?  20  ASN   A CG   1 
ATOM   527  O  OD1  A ASN   A 1 20  ? 5.506  -1.237  8.931   0.72 23.86 ?  20  ASN   A OD1  1 
ATOM   528  O  OD1  B ASN   A 1 20  ? 5.727  -1.037  8.846   0.28 20.24 ?  20  ASN   A OD1  1 
ATOM   529  N  ND2  A ASN   A 1 20  ? 7.245  -1.210  7.497   0.72 22.09 ?  20  ASN   A ND2  1 
ATOM   530  N  ND2  B ASN   A 1 20  ? 7.441  -1.103  7.401   0.28 19.18 ?  20  ASN   A ND2  1 
ATOM   531  H  H    A ASN   A 1 20  ? 7.939  -5.091  9.973   0.72 20.63 ?  20  ASN   A H    1 
ATOM   532  H  H    B ASN   A 1 20  ? 7.842  -5.126  9.676   0.28 21.07 ?  20  ASN   A H    1 
ATOM   533  H  HA   A ASN   A 1 20  ? 8.771  -3.378  8.092   0.72 22.25 ?  20  ASN   A HA   1 
ATOM   534  H  HA   B ASN   A 1 20  ? 8.851  -3.329  8.031   0.28 21.49 ?  20  ASN   A HA   1 
ATOM   535  H  HB2  A ASN   A 1 20  ? 6.510  -3.813  8.115   0.72 24.09 ?  20  ASN   A HB2  1 
ATOM   536  H  HB2  B ASN   A 1 20  ? 6.589  -3.666  7.920   0.28 22.06 ?  20  ASN   A HB2  1 
ATOM   537  H  HB3  A ASN   A 1 20  ? 6.412  -3.425  9.651   0.72 24.09 ?  20  ASN   A HB3  1 
ATOM   538  H  HB3  B ASN   A 1 20  ? 6.416  -3.325  9.462   0.28 22.06 ?  20  ASN   A HB3  1 
ATOM   539  H  HD21 A ASN   A 1 20  ? 7.081  -0.404  7.252   0.72 26.51 ?  20  ASN   A HD21 1 
ATOM   540  H  HD21 B ASN   A 1 20  ? 7.322  -0.284  7.168   0.28 23.01 ?  20  ASN   A HD21 1 
ATOM   541  H  HD22 A ASN   A 1 20  ? 7.910  -1.637  7.152   0.72 26.51 ?  20  ASN   A HD22 1 
ATOM   542  H  HD22 B ASN   A 1 20  ? 8.075  -1.563  7.050   0.28 23.01 ?  20  ASN   A HD22 1 
ATOM   543  N  N    A ALA   A 1 21  ? 10.112 -1.872  9.510   0.72 18.77 ?  21  ALA   A N    1 
ATOM   544  N  N    B ALA   A 1 21  ? 10.171 -1.859  9.494   0.28 17.43 ?  21  ALA   A N    1 
ATOM   545  C  CA   A ALA   A 1 21  ? 10.821 -0.976  10.408  0.72 18.49 ?  21  ALA   A CA   1 
ATOM   546  C  CA   B ALA   A 1 21  ? 10.849 -0.895  10.349  0.28 16.90 ?  21  ALA   A CA   1 
ATOM   547  C  C    A ALA   A 1 21  ? 11.759 -0.094  9.610   0.72 17.97 ?  21  ALA   A C    1 
ATOM   548  C  C    B ALA   A 1 21  ? 11.927 -0.180  9.550   0.28 15.98 ?  21  ALA   A C    1 
ATOM   549  O  O    A ALA   A 1 21  ? 12.172 -0.436  8.498   0.72 18.06 ?  21  ALA   A O    1 
ATOM   550  O  O    B ALA   A 1 21  ? 12.424 -0.691  8.543   0.28 15.88 ?  21  ALA   A O    1 
ATOM   551  C  CB   A ALA   A 1 21  ? 11.599 -1.753  11.471  0.72 19.63 ?  21  ALA   A CB   1 
ATOM   552  C  CB   B ALA   A 1 21  ? 11.467 -1.571  11.579  0.28 17.67 ?  21  ALA   A CB   1 
ATOM   553  H  H    A ALA   A 1 21  ? 10.487 -1.992  8.742   0.72 22.53 ?  21  ALA   A H    1 
ATOM   554  H  H    B ALA   A 1 21  ? 10.587 -2.040  8.764   0.28 20.92 ?  21  ALA   A H    1 
ATOM   555  H  HA   A ALA   A 1 21  ? 10.175 -0.403  10.855  0.72 22.20 ?  21  ALA   A HA   1 
ATOM   556  H  HA   B ALA   A 1 21  ? 10.211 -0.234  10.656  0.28 20.28 ?  21  ALA   A HA   1 
ATOM   557  H  HB1  A ALA   A 1 21  ? 12.005 -1.120  12.079  0.72 23.56 ?  21  ALA   A HB1  1 
ATOM   558  H  HB1  B ALA   A 1 21  ? 11.909 -0.898  12.120  0.28 21.21 ?  21  ALA   A HB1  1 
ATOM   559  H  HB2  A ALA   A 1 21  ? 10.977 -2.324  11.954  0.72 23.56 ?  21  ALA   A HB2  1 
ATOM   560  H  HB2  B ALA   A 1 21  ? 10.762 -1.997  12.092  0.28 21.21 ?  21  ALA   A HB2  1 
ATOM   561  H  HB3  A ALA   A 1 21  ? 12.273 -2.290  11.036  0.72 23.56 ?  21  ALA   A HB3  1 
ATOM   562  H  HB3  B ALA   A 1 21  ? 12.110 -2.235  11.285  0.28 21.21 ?  21  ALA   A HB3  1 
ATOM   563  N  N    A ASP   A 1 22  ? 12.063 1.061   10.198  0.72 17.77 ?  22  ASP   A N    1 
ATOM   564  N  N    B ASP   A 1 22  ? 12.268 1.021   10.015  0.28 15.28 ?  22  ASP   A N    1 
ATOM   565  C  CA   A ASP   A 1 22  ? 13.094 1.957   9.702   0.72 17.38 ?  22  ASP   A CA   1 
ATOM   566  C  CA   B ASP   A 1 22  ? 13.419 1.754   9.506   0.28 15.03 ?  22  ASP   A CA   1 
ATOM   567  C  C    A ASP   A 1 22  ? 14.428 1.467   10.248  0.72 16.11 ?  22  ASP   A C    1 
ATOM   568  C  C    B ASP   A 1 22  ? 14.679 1.138   10.101  0.28 13.68 ?  22  ASP   A C    1 
ATOM   569  O  O    A ASP   A 1 22  ? 14.637 1.460   11.465  0.72 16.38 ?  22  ASP   A O    1 
ATOM   570  O  O    B ASP   A 1 22  ? 14.791 1.002   11.323  0.28 13.45 ?  22  ASP   A O    1 
ATOM   571  C  CB   A ASP   A 1 22  ? 12.796 3.370   10.201  0.72 18.58 ?  22  ASP   A CB   1 
ATOM   572  C  CB   B ASP   A 1 22  ? 13.311 3.221   9.932   0.28 15.76 ?  22  ASP   A CB   1 
ATOM   573  C  CG   A ASP   A 1 22  ? 13.809 4.398   9.726   0.72 19.58 ?  22  ASP   A CG   1 
ATOM   574  C  CG   B ASP   A 1 22  ? 14.309 4.121   9.225   0.28 16.07 ?  22  ASP   A CG   1 
ATOM   575  O  OD1  A ASP   A 1 22  ? 14.883 4.026   9.213   0.72 19.42 ?  22  ASP   A OD1  1 
ATOM   576  O  OD1  B ASP   A 1 22  ? 15.359 3.617   8.781   0.28 15.54 ?  22  ASP   A OD1  1 
ATOM   577  O  OD2  A ASP   A 1 22  ? 13.527 5.604   9.883   0.72 21.04 -1 22  ASP   A OD2  1 
ATOM   578  O  OD2  B ASP   A 1 22  ? 14.048 5.339   9.120   0.28 16.79 -1 22  ASP   A OD2  1 
ATOM   579  H  H    A ASP   A 1 22  ? 11.664 1.356   10.904  0.72 21.32 ?  22  ASP   A H    1 
ATOM   580  H  H    B ASP   A 1 22  ? 11.835 1.440   10.630  0.28 18.34 ?  22  ASP   A H    1 
ATOM   581  H  HA   A ASP   A 1 22  ? 13.113 1.951   8.731   0.72 20.85 ?  22  ASP   A HA   1 
ATOM   582  H  HA   B ASP   A 1 22  ? 13.455 1.699   8.537   0.28 18.04 ?  22  ASP   A HA   1 
ATOM   583  H  HB2  A ASP   A 1 22  ? 11.912 3.635   9.896   0.72 22.30 ?  22  ASP   A HB2  1 
ATOM   584  H  HB2  B ASP   A 1 22  ? 12.420 3.543   9.732   0.28 18.91 ?  22  ASP   A HB2  1 
ATOM   585  H  HB3  A ASP   A 1 22  ? 12.821 3.374   11.172  0.72 22.30 ?  22  ASP   A HB3  1 
ATOM   586  H  HB3  B ASP   A 1 22  ? 13.482 3.283   10.885  0.28 18.91 ?  22  ASP   A HB3  1 
ATOM   587  N  N    A ILE   A 1 23  ? 15.319 1.035   9.352   0.72 15.30 ?  23  ILE   A N    1 
ATOM   588  N  N    B ILE   A 1 23  ? 15.624 0.754   9.238   0.28 12.77 ?  23  ILE   A N    1 
ATOM   589  C  CA   A ILE   A 1 23  ? 16.585 0.444   9.780   0.72 14.27 ?  23  ILE   A CA   1 
ATOM   590  C  CA   B ILE   A 1 23  ? 16.852 0.119   9.710   0.28 12.70 ?  23  ILE   A CA   1 
ATOM   591  C  C    A ILE   A 1 23  ? 17.380 1.406   10.652  0.72 14.02 ?  23  ILE   A C    1 
ATOM   592  C  C    B ILE   A 1 23  ? 17.613 1.045   10.650  0.28 13.03 ?  23  ILE   A C    1 
ATOM   593  O  O    A ILE   A 1 23  ? 18.114 0.976   11.549  0.72 14.62 ?  23  ILE   A O    1 
ATOM   594  O  O    B ILE   A 1 23  ? 18.294 0.585   11.574  0.28 12.90 ?  23  ILE   A O    1 
ATOM   595  C  CB   A ILE   A 1 23  ? 17.385 -0.054  8.558   0.72 14.02 ?  23  ILE   A CB   1 
ATOM   596  C  CB   B ILE   A 1 23  ? 17.717 -0.367  8.523   0.28 11.98 ?  23  ILE   A CB   1 
ATOM   597  C  CG1  A ILE   A 1 23  ? 18.554 -0.934  9.004   0.72 13.95 ?  23  ILE   A CG1  1 
ATOM   598  C  CG1  B ILE   A 1 23  ? 18.773 -1.366  9.009   0.28 11.85 ?  23  ILE   A CG1  1 
ATOM   599  C  CG2  A ILE   A 1 23  ? 17.842 1.117   7.690   0.72 14.13 ?  23  ILE   A CG2  1 
ATOM   600  C  CG2  B ILE   A 1 23  ? 18.375 0.807   7.794   0.28 11.86 ?  23  ILE   A CG2  1 
ATOM   601  C  CD1  A ILE   A 1 23  ? 19.259 -1.634  7.859   0.72 13.90 ?  23  ILE   A CD1  1 
ATOM   602  C  CD1  B ILE   A 1 23  ? 19.580 -2.015  7.893   0.28 11.58 ?  23  ILE   A CD1  1 
ATOM   603  H  H    A ILE   A 1 23  ? 15.209 1.071   8.503   0.72 18.36 ?  23  ILE   A H    1 
ATOM   604  H  H    B ILE   A 1 23  ? 15.579 0.848   8.392   0.28 15.33 ?  23  ILE   A H    1 
ATOM   605  H  HA   A ILE   A 1 23  ? 16.387 -0.331  10.324  0.72 17.13 ?  23  ILE   A HA   1 
ATOM   606  H  HA   B ILE   A 1 23  ? 16.606 -0.668  10.215  0.28 15.24 ?  23  ILE   A HA   1 
ATOM   607  H  HB   A ILE   A 1 23  ? 16.793 -0.601  8.021   0.72 16.83 ?  23  ILE   A HB   1 
ATOM   608  H  HB   B ILE   A 1 23  ? 17.141 -0.828  7.892   0.28 14.38 ?  23  ILE   A HB   1 
ATOM   609  H  HG12 A ILE   A 1 23  ? 19.209 -0.384  9.461   0.72 16.74 ?  23  ILE   A HG12 1 
ATOM   610  H  HG12 B ILE   A 1 23  ? 19.397 -0.905  9.591   0.28 14.22 ?  23  ILE   A HG12 1 
ATOM   611  H  HG13 A ILE   A 1 23  ? 18.219 -1.618  9.607   0.72 16.74 ?  23  ILE   A HG13 1 
ATOM   612  H  HG13 B ILE   A 1 23  ? 18.330 -2.076  9.500   0.28 14.22 ?  23  ILE   A HG13 1 
ATOM   613  H  HG21 A ILE   A 1 23  ? 18.205 0.773   6.857   0.72 16.95 ?  23  ILE   A HG21 1 
ATOM   614  H  HG21 B ILE   A 1 23  ? 18.743 0.490   6.951   0.28 14.24 ?  23  ILE   A HG21 1 
ATOM   615  H  HG22 A ILE   A 1 23  ? 17.078 1.688   7.501   0.72 16.95 ?  23  ILE   A HG22 1 
ATOM   616  H  HG22 B ILE   A 1 23  ? 17.707 1.486   7.626   0.28 14.24 ?  23  ILE   A HG22 1 
ATOM   617  H  HG23 A ILE   A 1 23  ? 18.520 1.622   8.162   0.72 16.95 ?  23  ILE   A HG23 1 
ATOM   618  H  HG23 B ILE   A 1 23  ? 19.086 1.167   8.347   0.28 14.24 ?  23  ILE   A HG23 1 
ATOM   619  H  HD11 A ILE   A 1 23  ? 19.937 -2.225  8.221   0.72 16.68 ?  23  ILE   A HD11 1 
ATOM   620  H  HD11 B ILE   A 1 23  ? 20.166 -2.688  8.277   0.28 13.90 ?  23  ILE   A HD11 1 
ATOM   621  H  HD12 A ILE   A 1 23  ? 18.606 -2.147  7.357   0.72 16.68 ?  23  ILE   A HD12 1 
ATOM   622  H  HD12 B ILE   A 1 23  ? 18.971 -2.430  7.263   0.28 13.90 ?  23  ILE   A HD12 1 
ATOM   623  H  HD13 A ILE   A 1 23  ? 19.668 -0.968  7.287   0.72 16.68 ?  23  ILE   A HD13 1 
ATOM   624  H  HD13 B ILE   A 1 23  ? 20.107 -1.335  7.446   0.28 13.90 ?  23  ILE   A HD13 1 
ATOM   625  N  N    A VAL   A 1 24  ? 17.239 2.713   10.419  0.72 14.48 ?  24  VAL   A N    1 
ATOM   626  N  N    B VAL   A 1 24  ? 17.498 2.359   10.444  0.28 14.24 ?  24  VAL   A N    1 
ATOM   627  C  CA   A VAL   A 1 24  ? 17.924 3.697   11.255  0.72 15.88 ?  24  VAL   A CA   1 
ATOM   628  C  CA   B VAL   A 1 24  ? 18.148 3.321   11.330  0.28 15.20 ?  24  VAL   A CA   1 
ATOM   629  C  C    A VAL   A 1 24  ? 17.427 3.607   12.691  0.72 16.84 ?  24  VAL   A C    1 
ATOM   630  C  C    B VAL   A 1 24  ? 17.566 3.230   12.735  0.28 15.98 ?  24  VAL   A C    1 
ATOM   631  O  O    A VAL   A 1 24  ? 18.217 3.538   13.640  0.72 16.93 ?  24  VAL   A O    1 
ATOM   632  O  O    B VAL   A 1 24  ? 18.299 3.266   13.732  0.28 16.38 ?  24  VAL   A O    1 
ATOM   633  C  CB   A VAL   A 1 24  ? 17.733 5.112   10.680  0.72 16.75 ?  24  VAL   A CB   1 
ATOM   634  C  CB   B VAL   A 1 24  ? 18.018 4.740   10.747  0.28 15.85 ?  24  VAL   A CB   1 
ATOM   635  C  CG1  A VAL   A 1 24  ? 18.267 6.168   11.650  0.72 17.30 ?  24  VAL   A CG1  1 
ATOM   636  C  CG1  B VAL   A 1 24  ? 18.546 5.774   11.730  0.28 16.35 ?  24  VAL   A CG1  1 
ATOM   637  C  CG2  A VAL   A 1 24  ? 18.413 5.229   9.326   0.72 17.28 ?  24  VAL   A CG2  1 
ATOM   638  C  CG2  B VAL   A 1 24  ? 18.748 4.833   9.415   0.28 16.00 ?  24  VAL   A CG2  1 
ATOM   639  H  H    A VAL   A 1 24  ? 16.761 3.052   9.792   0.72 17.38 ?  24  VAL   A H    1 
ATOM   640  H  H    B VAL   A 1 24  ? 17.055 2.713   9.803   0.28 17.09 ?  24  VAL   A H    1 
ATOM   641  H  HA   A VAL   A 1 24  ? 18.872 3.506   11.258  0.72 19.06 ?  24  VAL   A HA   1 
ATOM   642  H  HA   B VAL   A 1 24  ? 19.093 3.107   11.387  0.28 18.24 ?  24  VAL   A HA   1 
ATOM   643  H  HB   A VAL   A 1 24  ? 16.785 5.279   10.552  0.72 20.10 ?  24  VAL   A HB   1 
ATOM   644  H  HB   B VAL   A 1 24  ? 17.081 4.929   10.587  0.28 19.02 ?  24  VAL   A HB   1 
ATOM   645  H  HG11 A VAL   A 1 24  ? 18.379 7.005   11.172  0.72 20.77 ?  24  VAL   A HG11 1 
ATOM   646  H  HG11 B VAL   A 1 24  ? 18.672 6.613   11.261  0.28 19.62 ?  24  VAL   A HG11 1 
ATOM   647  H  HG12 A VAL   A 1 24  ? 17.633 6.285   12.373  0.72 20.77 ?  24  VAL   A HG12 1 
ATOM   648  H  HG12 B VAL   A 1 24  ? 17.901 5.890   12.444  0.28 19.62 ?  24  VAL   A HG12 1 
ATOM   649  H  HG13 A VAL   A 1 24  ? 19.122 5.871   11.998  0.72 20.77 ?  24  VAL   A HG13 1 
ATOM   650  H  HG13 B VAL   A 1 24  ? 19.391 5.465   12.089  0.28 19.62 ?  24  VAL   A HG13 1 
ATOM   651  H  HG21 A VAL   A 1 24  ? 18.192 6.090   8.936   0.72 20.74 ?  24  VAL   A HG21 1 
ATOM   652  H  HG21 B VAL   A 1 24  ? 18.608 5.715   9.039   0.28 19.20 ?  24  VAL   A HG21 1 
ATOM   653  H  HG22 A VAL   A 1 24  ? 19.372 5.160   9.449   0.72 20.74 ?  24  VAL   A HG22 1 
ATOM   654  H  HG22 B VAL   A 1 24  ? 19.695 4.684   9.563   0.28 19.20 ?  24  VAL   A HG22 1 
ATOM   655  H  HG23 A VAL   A 1 24  ? 18.098 4.516   8.750   0.72 20.74 ?  24  VAL   A HG23 1 
ATOM   656  H  HG23 B VAL   A 1 24  ? 18.398 4.158   8.812   0.28 19.20 ?  24  VAL   A HG23 1 
ATOM   657  N  N    A GLU   A 1 25  ? 16.106 3.615   12.870  0.72 18.03 ?  25  GLU   A N    1 
ATOM   658  N  N    B GLU   A 1 25  ? 16.241 3.112   12.837  0.28 16.34 ?  25  GLU   A N    1 
ATOM   659  C  CA   A GLU   A 1 25  ? 15.541 3.542   14.213  0.72 19.64 ?  25  GLU   A CA   1 
ATOM   660  C  CA   B GLU   A 1 25  ? 15.605 3.018   14.147  0.28 17.24 ?  25  GLU   A CA   1 
ATOM   661  C  C    A GLU   A 1 25  ? 15.783 2.177   14.846  0.72 18.55 ?  25  GLU   A C    1 
ATOM   662  C  C    B GLU   A 1 25  ? 15.885 1.669   14.799  0.28 16.88 ?  25  GLU   A C    1 
ATOM   663  O  O    A GLU   A 1 25  ? 16.006 2.080   16.057  0.72 19.38 ?  25  GLU   A O    1 
ATOM   664  O  O    B GLU   A 1 25  ? 16.144 1.601   16.006  0.28 16.88 ?  25  GLU   A O    1 
ATOM   665  C  CB   A GLU   A 1 25  ? 14.049 3.876   14.170  0.72 22.25 ?  25  GLU   A CB   1 
ATOM   666  C  CB   B GLU   A 1 25  ? 14.103 3.283   14.020  0.28 18.29 ?  25  GLU   A CB   1 
ATOM   667  C  CG   A GLU   A 1 25  ? 13.769 5.318   13.773  0.72 24.73 ?  25  GLU   A CG   1 
ATOM   668  C  CG   B GLU   A 1 25  ? 13.774 4.679   13.508  0.28 19.66 ?  25  GLU   A CG   1 
ATOM   669  C  CD   A GLU   A 1 25  ? 14.541 6.318   14.621  0.72 26.73 ?  25  GLU   A CD   1 
ATOM   670  C  CD   B GLU   A 1 25  ? 14.228 5.763   14.462  0.28 20.94 ?  25  GLU   A CD   1 
ATOM   671  O  OE1  A GLU   A 1 25  ? 14.581 6.150   15.859  0.72 27.43 ?  25  GLU   A OE1  1 
ATOM   672  O  OE1  B GLU   A 1 25  ? 14.207 5.520   15.688  0.28 21.34 ?  25  GLU   A OE1  1 
ATOM   673  O  OE2  A GLU   A 1 25  ? 15.132 7.257   14.046  0.72 27.76 -1 25  GLU   A OE2  1 
ATOM   674  O  OE2  B GLU   A 1 25  ? 14.611 6.852   13.988  0.28 21.84 -1 25  GLU   A OE2  1 
ATOM   675  H  H    A GLU   A 1 25  ? 15.522 3.672   12.239  0.72 21.64 ?  25  GLU   A H    1 
ATOM   676  H  H    B GLU   A 1 25  ? 15.699 3.080   12.174  0.28 19.61 ?  25  GLU   A H    1 
ATOM   677  H  HA   A GLU   A 1 25  ? 15.976 4.201   14.773  0.72 23.57 ?  25  GLU   A HA   1 
ATOM   678  H  HA   B GLU   A 1 25  ? 15.976 3.699   14.725  0.28 20.69 ?  25  GLU   A HA   1 
ATOM   679  H  HB2  A GLU   A 1 25  ? 13.611 3.301   13.521  0.72 26.71 ?  25  GLU   A HB2  1 
ATOM   680  H  HB2  B GLU   A 1 25  ? 13.720 2.647   13.401  0.28 21.96 ?  25  GLU   A HB2  1 
ATOM   681  H  HB3  A GLU   A 1 25  ? 13.662 3.731   15.049  0.72 26.71 ?  25  GLU   A HB3  1 
ATOM   682  H  HB3  B GLU   A 1 25  ? 13.690 3.188   14.893  0.28 21.96 ?  25  GLU   A HB3  1 
ATOM   683  H  HG2  A GLU   A 1 25  ? 14.042 5.450   12.854  0.72 29.68 ?  25  GLU   A HG2  1 
ATOM   684  H  HG2  B GLU   A 1 25  ? 14.217 4.821   12.655  0.28 23.59 ?  25  GLU   A HG2  1 
ATOM   685  H  HG3  A GLU   A 1 25  ? 12.816 5.491   13.866  0.72 29.68 ?  25  GLU   A HG3  1 
ATOM   686  H  HG3  B GLU   A 1 25  ? 12.813 4.763   13.398  0.28 23.59 ?  25  GLU   A HG3  1 
ATOM   687  N  N    A GLU   A 1 26  ? 15.754 1.111   14.042  0.72 18.02 ?  26  GLU   A N    1 
ATOM   688  N  N    B GLU   A 1 26  ? 15.859 0.587   14.017  0.28 16.86 ?  26  GLU   A N    1 
ATOM   689  C  CA   A GLU   A 1 26  ? 16.051 -0.221  14.565  0.72 18.28 ?  26  GLU   A CA   1 
ATOM   690  C  CA   B GLU   A 1 26  ? 16.265 -0.709  14.554  0.28 16.92 ?  26  GLU   A CA   1 
ATOM   691  C  C    A GLU   A 1 26  ? 17.481 -0.298  15.092  0.72 17.13 ?  26  GLU   A C    1 
ATOM   692  C  C    B GLU   A 1 26  ? 17.702 -0.659  15.053  0.28 16.66 ?  26  GLU   A C    1 
ATOM   693  O  O    A GLU   A 1 26  ? 17.725 -0.806  16.193  0.72 16.79 ?  26  GLU   A O    1 
ATOM   694  O  O    B GLU   A 1 26  ? 18.029 -1.246  16.092  0.28 16.64 ?  26  GLU   A O    1 
ATOM   695  C  CB   A GLU   A 1 26  ? 15.847 -1.268  13.470  0.72 19.74 ?  26  GLU   A CB   1 
ATOM   696  C  CB   B GLU   A 1 26  ? 16.108 -1.795  13.488  0.28 17.80 ?  26  GLU   A CB   1 
ATOM   697  C  CG   A GLU   A 1 26  ? 14.452 -1.835  13.364  0.72 21.89 ?  26  GLU   A CG   1 
ATOM   698  C  CG   B GLU   A 1 26  ? 14.671 -2.104  13.135  0.28 18.23 ?  26  GLU   A CG   1 
ATOM   699  C  CD   A GLU   A 1 26  ? 14.067 -2.680  14.570  0.72 23.10 ?  26  GLU   A CD   1 
ATOM   700  C  CD   B GLU   A 1 26  ? 13.887 -2.627  14.316  0.28 18.64 ?  26  GLU   A CD   1 
ATOM   701  O  OE1  A GLU   A 1 26  ? 14.516 -3.848  14.697  0.72 23.34 ?  26  GLU   A OE1  1 
ATOM   702  O  OE1  B GLU   A 1 26  ? 14.405 -3.506  15.039  0.28 19.39 ?  26  GLU   A OE1  1 
ATOM   703  O  OE2  A GLU   A 1 26  ? 13.308 -2.162  15.401  0.72 23.44 -1 26  GLU   A OE2  1 
ATOM   704  O  OE2  B GLU   A 1 26  ? 12.759 -2.142  14.527  0.28 17.75 -1 26  GLU   A OE2  1 
ATOM   705  H  H    A GLU   A 1 26  ? 15.570 1.138   13.202  0.72 21.63 ?  26  GLU   A H    1 
ATOM   706  H  H    B GLU   A 1 26  ? 15.626 0.576   13.190  0.28 20.23 ?  26  GLU   A H    1 
ATOM   707  H  HA   A GLU   A 1 26  ? 15.442 -0.414  15.294  0.72 21.94 ?  26  GLU   A HA   1 
ATOM   708  H  HA   B GLU   A 1 26  ? 15.699 -0.938  15.305  0.28 20.31 ?  26  GLU   A HA   1 
ATOM   709  H  HB2  A GLU   A 1 26  ? 16.066 -0.862  12.615  0.72 23.69 ?  26  GLU   A HB2  1 
ATOM   710  H  HB2  B GLU   A 1 26  ? 16.554 -1.508  12.676  0.28 21.37 ?  26  GLU   A HB2  1 
ATOM   711  H  HB3  A GLU   A 1 26  ? 16.450 -2.005  13.643  0.72 23.69 ?  26  GLU   A HB3  1 
ATOM   712  H  HB3  B GLU   A 1 26  ? 16.515 -2.616  13.811  0.28 21.37 ?  26  GLU   A HB3  1 
ATOM   713  H  HG2  A GLU   A 1 26  ? 13.826 -1.095  13.278  0.72 26.27 ?  26  GLU   A HG2  1 
ATOM   714  H  HG2  B GLU   A 1 26  ? 14.237 -1.293  12.831  0.28 21.88 ?  26  GLU   A HG2  1 
ATOM   715  H  HG3  A GLU   A 1 26  ? 14.400 -2.401  12.581  0.72 26.27 ?  26  GLU   A HG3  1 
ATOM   716  H  HG3  B GLU   A 1 26  ? 14.648 -2.778  12.440  0.28 21.88 ?  26  GLU   A HG3  1 
ATOM   717  N  N    A ALA   A 1 27  ? 18.445 0.187   14.309  0.72 15.80 ?  27  ALA   A N    1 
ATOM   718  N  N    B ALA   A 1 27  ? 18.572 0.050   14.334  0.28 16.67 ?  27  ALA   A N    1 
ATOM   719  C  CA   A ALA   A 1 27  ? 19.837 0.128   14.745  0.72 15.73 ?  27  ALA   A CA   1 
ATOM   720  C  CA   B ALA   A 1 27  ? 19.966 0.148   14.750  0.28 17.00 ?  27  ALA   A CA   1 
ATOM   721  C  C    A ALA   A 1 27  ? 20.043 0.926   16.026  0.72 16.97 ?  27  ALA   A C    1 
ATOM   722  C  C    B ALA   A 1 27  ? 20.097 0.951   16.037  0.28 17.79 ?  27  ALA   A C    1 
ATOM   723  O  O    A ALA   A 1 27  ? 20.718 0.467   16.954  0.72 17.24 ?  27  ALA   A O    1 
ATOM   724  O  O    B ALA   A 1 27  ? 20.772 0.523   16.981  0.28 17.88 ?  27  ALA   A O    1 
ATOM   725  C  CB   A ALA   A 1 27  ? 20.757 0.633   13.632  0.72 15.63 ?  27  ALA   A CB   1 
ATOM   726  C  CB   B ALA   A 1 27  ? 20.805 0.771   13.634  0.28 16.92 ?  27  ALA   A CB   1 
ATOM   727  H  H    A ALA   A 1 27  ? 18.319 0.546   13.537  0.72 18.97 ?  27  ALA   A H    1 
ATOM   728  H  H    B ALA   A 1 27  ? 18.382 0.476   13.612  0.28 20.01 ?  27  ALA   A H    1 
ATOM   729  H  HA   A ALA   A 1 27  ? 20.066 -0.794  14.929  0.72 18.88 ?  27  ALA   A HA   1 
ATOM   730  H  HA   B ALA   A 1 27  ? 20.308 -0.743  14.919  0.28 20.40 ?  27  ALA   A HA   1 
ATOM   731  H  HB1  A ALA   A 1 27  ? 21.677 0.583   13.939  0.72 18.76 ?  27  ALA   A HB1  1 
ATOM   732  H  HB1  B ALA   A 1 27  ? 21.730 0.815   13.924  0.28 20.31 ?  27  ALA   A HB1  1 
ATOM   733  H  HB2  A ALA   A 1 27  ? 20.641 0.071   12.849  0.72 18.76 ?  27  ALA   A HB2  1 
ATOM   734  H  HB2  B ALA   A 1 27  ? 20.734 0.217   12.841  0.28 20.31 ?  27  ALA   A HB2  1 
ATOM   735  H  HB3  A ALA   A 1 27  ? 20.527 1.549   13.420  0.72 18.76 ?  27  ALA   A HB3  1 
ATOM   736  H  HB3  B ALA   A 1 27  ? 20.473 1.662   13.447  0.28 20.31 ?  27  ALA   A HB3  1 
ATOM   737  N  N    . LYS   A 1 28  ? 19.452 2.120   16.101  1.00 18.76 ?  28  LYS   A N    1 
ATOM   738  C  CA   . LYS   A 1 28  ? 19.575 2.944   17.299  1.00 22.44 ?  28  LYS   A CA   1 
ATOM   739  C  C    . LYS   A 1 28  ? 19.034 2.232   18.531  1.00 23.56 ?  28  LYS   A C    1 
ATOM   740  O  O    . LYS   A 1 28  ? 19.567 2.412   19.632  1.00 25.17 ?  28  LYS   A O    1 
ATOM   741  C  CB   . LYS   A 1 28  ? 18.883 4.294   17.091  1.00 24.63 ?  28  LYS   A CB   1 
ATOM   742  C  CG   . LYS   A 1 28  ? 19.679 5.242   16.208  1.00 26.74 ?  28  LYS   A CG   1 
ATOM   743  C  CD   . LYS   A 1 28  ? 19.184 6.674   16.304  1.00 29.29 ?  28  LYS   A CD   1 
ATOM   744  C  CE   . LYS   A 1 28  ? 17.871 6.854   15.573  1.00 30.89 ?  28  LYS   A CE   1 
ATOM   745  N  NZ   . LYS   A 1 28  ? 17.448 8.283   15.548  1.00 31.87 ?  28  LYS   A NZ   1 
ATOM   746  H  H    A LYS   A 1 28  ? 18.977 2.469   15.477  0.72 22.52 ?  28  LYS   A H    1 
ATOM   747  H  H    B LYS   A 1 28  ? 18.953 2.446   15.484  0.28 22.52 ?  28  LYS   A H    1 
ATOM   748  H  HA   . LYS   A 1 28  ? 20.511 3.119   17.464  1.00 26.94 ?  28  LYS   A HA   1 
ATOM   749  H  HB2  . LYS   A 1 28  ? 18.023 4.149   16.669  1.00 29.56 ?  28  LYS   A HB2  1 
ATOM   750  H  HB3  . LYS   A 1 28  ? 18.761 4.725   17.952  1.00 29.56 ?  28  LYS   A HB3  1 
ATOM   751  H  HG2  . LYS   A 1 28  ? 20.610 5.227   16.481  1.00 32.09 ?  28  LYS   A HG2  1 
ATOM   752  H  HG3  . LYS   A 1 28  ? 19.600 4.959   15.283  1.00 32.09 ?  28  LYS   A HG3  1 
ATOM   753  H  HD2  . LYS   A 1 28  ? 19.048 6.904   17.237  1.00 35.15 ?  28  LYS   A HD2  1 
ATOM   754  H  HD3  . LYS   A 1 28  ? 19.840 7.268   15.905  1.00 35.15 ?  28  LYS   A HD3  1 
ATOM   755  H  HE2  . LYS   A 1 28  ? 17.973 6.551   14.657  1.00 37.07 ?  28  LYS   A HE2  1 
ATOM   756  H  HE3  . LYS   A 1 28  ? 17.182 6.341   16.022  1.00 37.07 ?  28  LYS   A HE3  1 
ATOM   757  H  HZ1  . LYS   A 1 28  ? 16.677 8.364   15.113  1.00 38.25 ?  28  LYS   A HZ1  1 
ATOM   758  H  HZ2  . LYS   A 1 28  ? 17.346 8.584   16.379  1.00 38.25 ?  28  LYS   A HZ2  1 
ATOM   759  H  HZ3  . LYS   A 1 28  ? 18.065 8.775   15.136  1.00 38.25 ?  28  LYS   A HZ3  1 
ATOM   760  N  N    . LYS   A 1 29  ? 18.000 1.406   18.366  1.00 24.12 ?  29  LYS   A N    1 
ATOM   761  C  CA   . LYS   A 1 29  ? 17.409 0.697   19.498  1.00 25.88 ?  29  LYS   A CA   1 
ATOM   762  C  C    . LYS   A 1 29  ? 18.239 -0.520  19.894  1.00 24.70 ?  29  LYS   A C    1 
ATOM   763  O  O    . LYS   A 1 29  ? 18.520 -0.732  21.080  1.00 25.60 ?  29  LYS   A O    1 
ATOM   764  C  CB   . LYS   A 1 29  ? 15.986 0.261   19.142  1.00 29.06 ?  29  LYS   A CB   1 
ATOM   765  C  CG   . LYS   A 1 29  ? 15.230 -0.403  20.282  1.00 32.14 ?  29  LYS   A CG   1 
ATOM   766  C  CD   . LYS   A 1 29  ? 14.852 0.606   21.353  1.00 34.99 ?  29  LYS   A CD   1 
ATOM   767  C  CE   . LYS   A 1 29  ? 13.983 -0.023  22.430  1.00 37.11 ?  29  LYS   A CE   1 
ATOM   768  N  NZ   . LYS   A 1 29  ? 13.519 0.984   23.424  1.00 38.23 ?  29  LYS   A NZ   1 
ATOM   769  H  H    . LYS   A 1 29  ? 17.622 1.238   17.610  1.00 28.95 ?  29  LYS   A H    1 
ATOM   770  H  HA   . LYS   A 1 29  ? 17.360 1.292   20.261  1.00 31.06 ?  29  LYS   A HA   1 
ATOM   771  H  HB2  . LYS   A 1 29  ? 15.477 1.041   18.872  1.00 34.88 ?  29  LYS   A HB2  1 
ATOM   772  H  HB3  . LYS   A 1 29  ? 16.026 -0.374  18.410  1.00 34.88 ?  29  LYS   A HB3  1 
ATOM   773  H  HG2  . LYS   A 1 29  ? 14.413 -0.799  19.938  1.00 38.57 ?  29  LYS   A HG2  1 
ATOM   774  H  HG3  . LYS   A 1 29  ? 15.785 -1.088  20.690  1.00 38.57 ?  29  LYS   A HG3  1 
ATOM   775  H  HD2  . LYS   A 1 29  ? 15.659 0.946   21.772  1.00 41.99 ?  29  LYS   A HD2  1 
ATOM   776  H  HD3  . LYS   A 1 29  ? 14.355 1.333   20.945  1.00 41.99 ?  29  LYS   A HD3  1 
ATOM   777  H  HE2  . LYS   A 1 29  ? 13.202 -0.423  22.017  1.00 44.53 ?  29  LYS   A HE2  1 
ATOM   778  H  HE3  . LYS   A 1 29  ? 14.496 -0.699  22.900  1.00 44.53 ?  29  LYS   A HE3  1 
ATOM   779  H  HZ1  . LYS   A 1 29  ? 13.013 0.591   24.042  1.00 45.88 ?  29  LYS   A HZ1  1 
ATOM   780  H  HZ2  . LYS   A 1 29  ? 14.219 1.363   23.822  1.00 45.88 ?  29  LYS   A HZ2  1 
ATOM   781  H  HZ3  . LYS   A 1 29  ? 13.040 1.615   23.017  1.00 45.88 ?  29  LYS   A HZ3  1 
ATOM   782  N  N    . VAL   A 1 30  ? 18.614 -1.342  18.914  1.00 23.30 ?  30  VAL   A N    1 
ATOM   783  C  CA   . VAL   A 1 30  ? 19.259 -2.618  19.204  1.00 22.50 ?  30  VAL   A CA   1 
ATOM   784  C  C    . VAL   A 1 30  ? 20.764 -2.467  19.407  1.00 21.29 ?  30  VAL   A C    1 
ATOM   785  O  O    . VAL   A 1 30  ? 21.365 -3.215  20.186  1.00 21.69 ?  30  VAL   A O    1 
ATOM   786  C  CB   . VAL   A 1 30  ? 18.938 -3.611  18.073  1.00 23.54 ?  30  VAL   A CB   1 
ATOM   787  C  CG1  . VAL   A 1 30  ? 19.700 -4.918  18.259  1.00 24.36 ?  30  VAL   A CG1  1 
ATOM   788  C  CG2  . VAL   A 1 30  ? 17.438 -3.866  18.001  1.00 24.25 ?  30  VAL   A CG2  1 
ATOM   789  H  H    . VAL   A 1 30  ? 18.485 -1.197  18.075  1.00 27.96 ?  30  VAL   A H    1 
ATOM   790  H  HA   . VAL   A 1 30  ? 18.880 -2.979  20.021  1.00 27.01 ?  30  VAL   A HA   1 
ATOM   791  H  HB   . VAL   A 1 30  ? 19.215 -3.228  17.228  1.00 28.25 ?  30  VAL   A HB   1 
ATOM   792  H  HG11 . VAL   A 1 30  ? 19.319 -5.591  17.672  1.00 29.23 ?  30  VAL   A HG11 1 
ATOM   793  H  HG12 . VAL   A 1 30  ? 20.632 -4.778  18.036  1.00 29.23 ?  30  VAL   A HG12 1 
ATOM   794  H  HG13 . VAL   A 1 30  ? 19.616 -5.203  19.183  1.00 29.23 ?  30  VAL   A HG13 1 
ATOM   795  H  HG21 . VAL   A 1 30  ? 17.263 -4.538  17.323  1.00 29.10 ?  30  VAL   A HG21 1 
ATOM   796  H  HG22 . VAL   A 1 30  ? 17.130 -4.181  18.865  1.00 29.10 ?  30  VAL   A HG22 1 
ATOM   797  H  HG23 . VAL   A 1 30  ? 16.988 -3.039  17.770  1.00 29.10 ?  30  VAL   A HG23 1 
ATOM   798  N  N    . LYS   A 1 31  ? 21.394 -1.514  18.728  1.00 20.22 ?  31  LYS   A N    1 
ATOM   799  C  CA   . LYS   A 1 31  ? 22.847 -1.412  18.664  1.00 20.81 ?  31  LYS   A CA   1 
ATOM   800  C  C    . LYS   A 1 31  ? 23.449 -2.767  18.281  1.00 18.94 ?  31  LYS   A C    1 
ATOM   801  O  O    . LYS   A 1 31  ? 24.246 -3.337  19.033  1.00 19.95 ?  31  LYS   A O    1 
ATOM   802  C  CB   . LYS   A 1 31  ? 23.445 -0.894  19.965  1.00 25.20 ?  31  LYS   A CB   1 
ATOM   803  C  CG   . LYS   A 1 31  ? 22.759 0.356   20.494  1.00 30.57 ?  31  LYS   A CG   1 
ATOM   804  C  CD   . LYS   A 1 31  ? 23.761 1.431   20.885  1.00 34.81 ?  31  LYS   A CD   1 
ATOM   805  C  CE   . LYS   A 1 31  ? 23.117 2.498   21.762  1.00 37.42 ?  31  LYS   A CE   1 
ATOM   806  N  NZ   . LYS   A 1 31  ? 21.939 3.143   21.119  1.00 38.64 ?  31  LYS   A NZ   1 
ATOM   807  H  H    . LYS   A 1 31  ? 20.989 -0.900  18.284  1.00 24.27 ?  31  LYS   A H    1 
ATOM   808  H  HA   . LYS   A 1 31  ? 23.082 -0.780  17.976  1.00 24.97 ?  31  LYS   A HA   1 
ATOM   809  H  HB2  . LYS   A 1 31  ? 23.376 -1.586  20.637  1.00 30.24 ?  31  LYS   A HB2  1 
ATOM   810  H  HB3  . LYS   A 1 31  ? 24.380 -0.680  19.807  1.00 30.24 ?  31  LYS   A HB3  1 
ATOM   811  H  HG2  . LYS   A 1 31  ? 22.180 0.720   19.806  1.00 36.69 ?  31  LYS   A HG2  1 
ATOM   812  H  HG3  . LYS   A 1 31  ? 22.241 0.125   21.280  1.00 36.69 ?  31  LYS   A HG3  1 
ATOM   813  H  HD2  . LYS   A 1 31  ? 24.489 1.027   21.382  1.00 41.77 ?  31  LYS   A HD2  1 
ATOM   814  H  HD3  . LYS   A 1 31  ? 24.099 1.861   20.083  1.00 41.77 ?  31  LYS   A HD3  1 
ATOM   815  H  HE2  . LYS   A 1 31  ? 22.820 2.088   22.589  1.00 44.91 ?  31  LYS   A HE2  1 
ATOM   816  H  HE3  . LYS   A 1 31  ? 23.771 3.189   21.950  1.00 44.91 ?  31  LYS   A HE3  1 
ATOM   817  H  HZ1  . LYS   A 1 31  ? 21.600 3.765   21.659  1.00 46.37 ?  31  LYS   A HZ1  1 
ATOM   818  H  HZ2  . LYS   A 1 31  ? 22.181 3.526   20.353  1.00 46.37 ?  31  LYS   A HZ2  1 
ATOM   819  H  HZ3  . LYS   A 1 31  ? 21.311 2.534   20.952  1.00 46.37 ?  31  LYS   A HZ3  1 
ATOM   820  N  N    . PRO   A 1 32  ? 23.083 -3.303  17.124  1.00 16.69 ?  32  PRO   A N    1 
ATOM   821  C  CA   . PRO   A 1 32  ? 23.558 -4.631  16.742  1.00 16.78 ?  32  PRO   A CA   1 
ATOM   822  C  C    . PRO   A 1 32  ? 25.058 -4.636  16.523  1.00 16.78 ?  32  PRO   A C    1 
ATOM   823  O  O    . PRO   A 1 32  ? 25.693 -3.601  16.305  1.00 16.42 ?  32  PRO   A O    1 
ATOM   824  C  CB   . PRO   A 1 32  ? 22.815 -4.899  15.429  1.00 17.00 ?  32  PRO   A CB   1 
ATOM   825  C  CG   . PRO   A 1 32  ? 22.620 -3.526  14.848  1.00 15.95 ?  32  PRO   A CG   1 
ATOM   826  C  CD   . PRO   A 1 32  ? 22.337 -2.654  16.034  1.00 16.27 ?  32  PRO   A CD   1 
ATOM   827  H  HA   . PRO   A 1 32  ? 23.319 -5.297  17.401  1.00 20.14 ?  32  PRO   A HA   1 
ATOM   828  H  HB2  . PRO   A 1 32  ? 23.355 -5.454  14.841  1.00 20.40 ?  32  PRO   A HB2  1 
ATOM   829  H  HB3  . PRO   A 1 32  ? 21.960 -5.325  15.612  1.00 20.40 ?  32  PRO   A HB3  1 
ATOM   830  H  HG2  . PRO   A 1 32  ? 23.428 -3.252  14.390  1.00 19.14 ?  32  PRO   A HG2  1 
ATOM   831  H  HG3  . PRO   A 1 32  ? 21.865 -3.539  14.235  1.00 19.14 ?  32  PRO   A HG3  1 
ATOM   832  H  HD2  . PRO   A 1 32  ? 22.676 -1.759  15.869  1.00 19.53 ?  32  PRO   A HD2  1 
ATOM   833  H  HD3  . PRO   A 1 32  ? 21.391 -2.649  16.228  1.00 19.53 ?  32  PRO   A HD3  1 
ATOM   834  N  N    . THR   A 1 33  ? 25.626 -5.838  16.575  1.00 16.64 ?  33  THR   A N    1 
ATOM   835  C  CA   . THR   A 1 33  ? 27.031 -5.996  16.233  1.00 16.92 ?  33  THR   A CA   1 
ATOM   836  C  C    . THR   A 1 33  ? 27.300 -5.531  14.809  1.00 15.18 ?  33  THR   A C    1 
ATOM   837  O  O    . THR   A 1 33  ? 28.321 -4.879  14.547  1.00 15.25 ?  33  THR   A O    1 
ATOM   838  C  CB   . THR   A 1 33  ? 27.445 -7.453  16.428  1.00 18.50 ?  33  THR   A CB   1 
ATOM   839  O  OG1  . THR   A 1 33  ? 27.154 -7.842  17.773  1.00 19.98 ?  33  THR   A OG1  1 
ATOM   840  C  CG2  . THR   A 1 33  ? 28.935 -7.638  16.165  1.00 19.79 ?  33  THR   A CG2  1 
ATOM   841  H  H    . THR   A 1 33  ? 25.228 -6.570  16.796  1.00 19.97 ?  33  THR   A H    1 
ATOM   842  H  HA   . THR   A 1 33  ? 27.567 -5.456  16.829  1.00 20.31 ?  33  THR   A HA   1 
ATOM   843  H  HB   . THR   A 1 33  ? 26.954 -8.025  15.814  1.00 22.20 ?  33  THR   A HB   1 
ATOM   844  H  HG1  . THR   A 1 33  ? 27.584 -7.359  18.313  1.00 23.98 ?  33  THR   A HG1  1 
ATOM   845  H  HG21 . THR   A 1 33  ? 29.213 -8.529  16.436  1.00 23.75 ?  33  THR   A HG21 1 
ATOM   846  H  HG22 . THR   A 1 33  ? 29.125 -7.525  15.222  1.00 23.75 ?  33  THR   A HG22 1 
ATOM   847  H  HG23 . THR   A 1 33  ? 29.443 -6.986  16.672  1.00 23.75 ?  33  THR   A HG23 1 
ATOM   848  N  N    . VAL   A 1 34  ? 26.399 -5.848  13.879  1.00 13.86 ?  34  VAL   A N    1 
ATOM   849  C  CA   . VAL   A 1 34  ? 26.566 -5.501  12.473  1.00 12.90 ?  34  VAL   A CA   1 
ATOM   850  C  C    . VAL   A 1 34  ? 25.258 -4.937  11.932  1.00 12.07 ?  34  VAL   A C    1 
ATOM   851  O  O    . VAL   A 1 34  ? 24.217 -5.606  11.987  1.00 12.86 ?  34  VAL   A O    1 
ATOM   852  C  CB   . VAL   A 1 34  ? 27.008 -6.701  11.617  1.00 13.39 ?  34  VAL   A CB   1 
ATOM   853  C  CG1  . VAL   A 1 34  ? 27.161 -6.273  10.160  1.00 13.46 ?  34  VAL   A CG1  1 
ATOM   854  C  CG2  . VAL   A 1 34  ? 28.304 -7.308  12.141  1.00 14.41 ?  34  VAL   A CG2  1 
ATOM   855  H  H    . VAL   A 1 34  ? 25.673 -6.281  14.041  1.00 16.63 ?  34  VAL   A H    1 
ATOM   856  H  HA   . VAL   A 1 34  ? 27.247 -4.813  12.391  1.00 15.48 ?  34  VAL   A HA   1 
ATOM   857  H  HB   . VAL   A 1 34  ? 26.321 -7.384  11.653  1.00 16.07 ?  34  VAL   A HB   1 
ATOM   858  H  HG11 . VAL   A 1 34  ? 27.659 -6.955  9.681   1.00 16.16 ?  34  VAL   A HG11 1 
ATOM   859  H  HG12 . VAL   A 1 34  ? 26.284 -6.166  9.761   1.00 16.16 ?  34  VAL   A HG12 1 
ATOM   860  H  HG13 . VAL   A 1 34  ? 27.646 -5.432  10.127  1.00 16.16 ?  34  VAL   A HG13 1 
ATOM   861  H  HG21 . VAL   A 1 34  ? 28.571 -8.040  11.560  1.00 17.29 ?  34  VAL   A HG21 1 
ATOM   862  H  HG22 . VAL   A 1 34  ? 28.995 -6.625  12.147  1.00 17.29 ?  34  VAL   A HG22 1 
ATOM   863  H  HG23 . VAL   A 1 34  ? 28.159 -7.638  13.041  1.00 17.29 ?  34  VAL   A HG23 1 
ATOM   864  N  N    . VAL   A 1 35  ? 25.317 -3.724  11.384  1.00 11.46 ?  35  VAL   A N    1 
ATOM   865  C  CA   . VAL   A 1 35  ? 24.273 -3.204  10.510  1.00 11.07 ?  35  VAL   A CA   1 
ATOM   866  C  C    . VAL   A 1 35  ? 24.814 -3.198  9.090   1.00 10.43 ?  35  VAL   A C    1 
ATOM   867  O  O    . VAL   A 1 35  ? 25.960 -2.795  8.851   1.00 10.73 ?  35  VAL   A O    1 
ATOM   868  C  CB   . VAL   A 1 35  ? 23.752 -1.815  10.936  1.00 11.87 ?  35  VAL   A CB   1 
ATOM   869  C  CG1  . VAL   A 1 35  ? 24.831 -0.720  10.816  1.00 12.28 ?  35  VAL   A CG1  1 
ATOM   870  C  CG2  . VAL   A 1 35  ? 22.504 -1.451  10.128  1.00 12.32 ?  35  VAL   A CG2  1 
ATOM   871  H  H    . VAL   A 1 35  ? 25.967 -3.173  11.497  1.00 13.75 ?  35  VAL   A H    1 
ATOM   872  H  HA   . VAL   A 1 35  ? 23.517 -3.817  10.535  1.00 13.29 ?  35  VAL   A HA   1 
ATOM   873  H  HB   . VAL   A 1 35  ? 23.484 -1.859  11.864  1.00 14.24 ?  35  VAL   A HB   1 
ATOM   874  H  HG11 . VAL   A 1 35  ? 24.485 0.115   11.183  1.00 14.74 ?  35  VAL   A HG11 1 
ATOM   875  H  HG12 . VAL   A 1 35  ? 25.619 -0.990  11.317  1.00 14.74 ?  35  VAL   A HG12 1 
ATOM   876  H  HG13 . VAL   A 1 35  ? 25.065 -0.591  9.883   1.00 14.74 ?  35  VAL   A HG13 1 
ATOM   877  H  HG21 . VAL   A 1 35  ? 22.154 -0.605  10.446  1.00 14.79 ?  35  VAL   A HG21 1 
ATOM   878  H  HG22 . VAL   A 1 35  ? 22.744 -1.374  9.188   1.00 14.79 ?  35  VAL   A HG22 1 
ATOM   879  H  HG23 . VAL   A 1 35  ? 21.839 -2.149  10.239  1.00 14.79 ?  35  VAL   A HG23 1 
ATOM   880  N  N    . VAL   A 1 36  ? 23.992 -3.651  8.148   1.00 9.82  ?  36  VAL   A N    1 
ATOM   881  C  CA   . VAL   A 1 36  ? 24.358 -3.661  6.740   1.00 9.76  ?  36  VAL   A CA   1 
ATOM   882  C  C    . VAL   A 1 36  ? 23.892 -2.373  6.084   1.00 10.01 ?  36  VAL   A C    1 
ATOM   883  O  O    . VAL   A 1 36  ? 22.733 -1.967  6.232   1.00 10.52 ?  36  VAL   A O    1 
ATOM   884  C  CB   . VAL   A 1 36  ? 23.754 -4.877  6.022   1.00 9.88  ?  36  VAL   A CB   1 
ATOM   885  C  CG1  . VAL   A 1 36  ? 24.005 -4.800  4.533   1.00 10.58 ?  36  VAL   A CG1  1 
ATOM   886  C  CG2  . VAL   A 1 36  ? 24.296 -6.162  6.595   1.00 10.99 ?  36  VAL   A CG2  1 
ATOM   887  H  H    . VAL   A 1 36  ? 23.201 -3.969  8.299   1.00 11.79 ?  36  VAL   A H    1 
ATOM   888  H  HA   . VAL   A 1 36  ? 25.329 -3.715  6.662   1.00 11.71 ?  36  VAL   A HA   1 
ATOM   889  H  HB   . VAL   A 1 36  ? 22.798 -4.869  6.154   1.00 11.86 ?  36  VAL   A HB   1 
ATOM   890  H  HG11 . VAL   A 1 36  ? 23.863 -5.676  4.142   1.00 12.69 ?  36  VAL   A HG11 1 
ATOM   891  H  HG12 . VAL   A 1 36  ? 23.393 -4.160  4.135   1.00 12.69 ?  36  VAL   A HG12 1 
ATOM   892  H  HG13 . VAL   A 1 36  ? 24.923 -4.519  4.378   1.00 12.69 ?  36  VAL   A HG13 1 
ATOM   893  H  HG21 . VAL   A 1 36  ? 23.909 -6.913  6.114   1.00 13.19 ?  36  VAL   A HG21 1 
ATOM   894  H  HG22 . VAL   A 1 36  ? 25.261 -6.175  6.501   1.00 13.19 ?  36  VAL   A HG22 1 
ATOM   895  H  HG23 . VAL   A 1 36  ? 24.055 -6.217  7.534   1.00 13.19 ?  36  VAL   A HG23 1 
ATOM   896  N  N    . ASN   A 1 37  ? 24.792 -1.748  5.331   1.00 9.29  ?  37  ASN   A N    1 
ATOM   897  C  CA   . ASN   A 1 37  ? 24.455 -0.626  4.473   1.00 9.19  ?  37  ASN   A CA   1 
ATOM   898  C  C    . ASN   A 1 37  ? 24.308 -1.093  3.034   1.00 9.27  ?  37  ASN   A C    1 
ATOM   899  O  O    . ASN   A 1 37  ? 25.092 -1.918  2.546   1.00 9.51  ?  37  ASN   A O    1 
ATOM   900  C  CB   . ASN   A 1 37  ? 25.536 0.450   4.546   1.00 9.55  ?  37  ASN   A CB   1 
ATOM   901  C  CG   . ASN   A 1 37  ? 25.209 1.649   3.694   1.00 10.14 ?  37  ASN   A CG   1 
ATOM   902  O  OD1  . ASN   A 1 37  ? 24.034 1.988   3.522   1.00 10.18 ?  37  ASN   A OD1  1 
ATOM   903  N  ND2  . ASN   A 1 37  ? 26.235 2.305   3.171   1.00 10.13 ?  37  ASN   A ND2  1 
ATOM   904  H  H    . ASN   A 1 37  ? 25.632 -1.955  5.314   1.00 11.15 ?  37  ASN   A H    1 
ATOM   905  H  HA   . ASN   A 1 37  ? 23.621 -0.236  4.765   1.00 11.03 ?  37  ASN   A HA   1 
ATOM   906  H  HB2  . ASN   A 1 37  ? 25.627 0.750   5.468   1.00 11.46 ?  37  ASN   A HB2  1 
ATOM   907  H  HB3  . ASN   A 1 37  ? 26.381 0.079   4.239   1.00 11.46 ?  37  ASN   A HB3  1 
ATOM   908  H  HD21 . ASN   A 1 37  ? 26.097 2.994   2.678   1.00 12.16 ?  37  ASN   A HD21 1 
ATOM   909  H  HD22 . ASN   A 1 37  ? 27.036 2.039   3.315   1.00 12.16 ?  37  ASN   A HD22 1 
ATOM   910  N  N    . ALA   A 1 38  ? 23.294 -0.550  2.359   1.00 9.87  ?  38  ALA   A N    1 
ATOM   911  C  CA   . ALA   A 1 38  ? 23.096 -0.715  0.921   1.00 9.82  ?  38  ALA   A CA   1 
ATOM   912  C  C    . ALA   A 1 38  ? 23.999 0.285   0.199   1.00 9.96  ?  38  ALA   A C    1 
ATOM   913  O  O    . ALA   A 1 38  ? 23.580 1.367   -0.221  1.00 10.03 ?  38  ALA   A O    1 
ATOM   914  C  CB   . ALA   A 1 38  ? 21.629 -0.508  0.568   1.00 11.93 ?  38  ALA   A CB   1 
ATOM   915  H  H    . ALA   A 1 38  ? 22.697 -0.058  2.733   1.00 11.85 ?  38  ALA   A H    1 
ATOM   916  H  HA   . ALA   A 1 38  ? 23.354 -1.611  0.661   1.00 11.78 ?  38  ALA   A HA   1 
ATOM   917  H  HB1  . ALA   A 1 38  ? 21.499 -0.701  -0.371  1.00 14.31 ?  38  ALA   A HB1  1 
ATOM   918  H  HB2  . ALA   A 1 38  ? 21.085 -1.109  1.108   1.00 14.31 ?  38  ALA   A HB2  1 
ATOM   919  H  HB3  . ALA   A 1 38  ? 21.385 0.410   0.756   1.00 14.31 ?  38  ALA   A HB3  1 
ATOM   920  N  N    . ALA   A 1 39  ? 25.270 -0.088  0.066   1.00 10.22 ?  39  ALA   A N    1 
ATOM   921  C  CA   . ALA   A 1 39  ? 26.313 0.795   -0.420  1.00 10.24 ?  39  ALA   A CA   1 
ATOM   922  C  C    . ALA   A 1 39  ? 26.423 0.741   -1.938  1.00 10.13 ?  39  ALA   A C    1 
ATOM   923  O  O    . ALA   A 1 39  ? 25.940 -0.181  -2.594  1.00 10.40 ?  39  ALA   A O    1 
ATOM   924  C  CB   . ALA   A 1 39  ? 27.647 0.402   0.219   1.00 10.51 ?  39  ALA   A CB   1 
ATOM   925  H  H    . ALA   A 1 39  ? 25.551 -0.883  0.260   1.00 12.26 ?  39  ALA   A H    1 
ATOM   926  H  HA   . ALA   A 1 39  ? 26.099 1.703   -0.157  1.00 12.29 ?  39  ALA   A HA   1 
ATOM   927  H  HB1  . ALA   A 1 39  ? 28.332 1.000   -0.107  1.00 12.62 ?  39  ALA   A HB1  1 
ATOM   928  H  HB2  . ALA   A 1 39  ? 27.565 0.486   1.186   1.00 12.62 ?  39  ALA   A HB2  1 
ATOM   929  H  HB3  . ALA   A 1 39  ? 27.851 -0.511  -0.018  1.00 12.62 ?  39  ALA   A HB3  1 
ATOM   930  N  N    . ASN   A 1 40  ? 27.091 1.750   -2.495  1.00 10.76 ?  40  ASN   A N    1 
ATOM   931  C  CA   . ASN   A 1 40  ? 27.604 1.702   -3.856  1.00 10.67 ?  40  ASN   A CA   1 
ATOM   932  C  C    . ASN   A 1 40  ? 29.129 1.609   -3.822  1.00 10.02 ?  40  ASN   A C    1 
ATOM   933  O  O    . ASN   A 1 40  ? 29.752 1.718   -2.764  1.00 10.16 ?  40  ASN   A O    1 
ATOM   934  C  CB   . ASN   A 1 40  ? 27.098 2.886   -4.695  1.00 11.61 ?  40  ASN   A CB   1 
ATOM   935  C  CG   . ASN   A 1 40  ? 27.469 4.230   -4.105  1.00 12.78 ?  40  ASN   A CG   1 
ATOM   936  O  OD1  . ASN   A 1 40  ? 28.647 4.516   -3.867  1.00 14.05 ?  40  ASN   A OD1  1 
ATOM   937  N  ND2  . ASN   A 1 40  ? 26.468 5.082   -3.906  1.00 13.88 ?  40  ASN   A ND2  1 
ATOM   938  H  H    . ASN   A 1 40  ? 27.272 2.482   -2.088  1.00 12.91 ?  40  ASN   A H    1 
ATOM   939  H  HA   . ASN   A 1 40  ? 27.277 0.889   -4.279  1.00 12.81 ?  40  ASN   A HA   1 
ATOM   940  H  HB2  . ASN   A 1 40  ? 27.482 2.822   -5.587  1.00 13.93 ?  40  ASN   A HB2  1 
ATOM   941  H  HB3  . ASN   A 1 40  ? 26.131 2.836   -4.752  1.00 13.93 ?  40  ASN   A HB3  1 
ATOM   942  H  HD21 . ASN   A 1 40  ? 26.627 5.866   -3.584  1.00 16.66 ?  40  ASN   A HD21 1 
ATOM   943  H  HD22 . ASN   A 1 40  ? 25.662 4.851   -4.092  1.00 16.66 ?  40  ASN   A HD22 1 
ATOM   944  N  N    . VAL   A 1 41  ? 29.725 1.371   -4.993  1.00 10.61 ?  41  VAL   A N    1 
ATOM   945  C  CA   . VAL   A 1 41  ? 31.155 1.067   -5.041  1.00 11.70 ?  41  VAL   A CA   1 
ATOM   946  C  C    . VAL   A 1 41  ? 32.015 2.220   -4.564  1.00 11.50 ?  41  VAL   A C    1 
ATOM   947  O  O    . VAL   A 1 41  ? 33.165 2.001   -4.161  1.00 12.26 ?  41  VAL   A O    1 
ATOM   948  C  CB   . VAL   A 1 41  ? 31.618 0.602   -6.441  1.00 12.77 ?  41  VAL   A CB   1 
ATOM   949  C  CG1  . VAL   A 1 41  ? 30.934 -0.706  -6.813  1.00 13.80 ?  41  VAL   A CG1  1 
ATOM   950  C  CG2  . VAL   A 1 41  ? 31.387 1.669   -7.507  1.00 13.65 ?  41  VAL   A CG2  1 
ATOM   951  H  H    . VAL   A 1 41  ? 29.328 1.364   -5.760  1.00 12.74 ?  41  VAL   A H    1 
ATOM   952  H  HA   . VAL   A 1 41  ? 31.321 0.327   -4.436  1.00 14.05 ?  41  VAL   A HA   1 
ATOM   953  H  HB   . VAL   A 1 41  ? 32.570 0.419   -6.407  1.00 15.33 ?  41  VAL   A HB   1 
ATOM   954  H  HG11 . VAL   A 1 41  ? 31.263 -1.005  -7.675  1.00 16.56 ?  41  VAL   A HG11 1 
ATOM   955  H  HG12 . VAL   A 1 41  ? 31.134 -1.375  -6.135  1.00 16.56 ?  41  VAL   A HG12 1 
ATOM   956  H  HG13 . VAL   A 1 41  ? 29.975 -0.562  -6.857  1.00 16.56 ?  41  VAL   A HG13 1 
ATOM   957  H  HG21 . VAL   A 1 41  ? 31.636 1.308   -8.373  1.00 16.38 ?  41  VAL   A HG21 1 
ATOM   958  H  HG22 . VAL   A 1 41  ? 30.449 1.914   -7.509  1.00 16.38 ?  41  VAL   A HG22 1 
ATOM   959  H  HG23 . VAL   A 1 41  ? 31.934 2.440   -7.300  1.00 16.38 ?  41  VAL   A HG23 1 
ATOM   960  N  N    . TYR   A 1 42  ? 31.505 3.449   -4.635  1.00 11.25 ?  42  TYR   A N    1 
ATOM   961  C  CA   . TYR   A 1 42  ? 32.247 4.633   -4.221  1.00 11.30 ?  42  TYR   A CA   1 
ATOM   962  C  C    . TYR   A 1 42  ? 31.992 5.005   -2.771  1.00 11.19 ?  42  TYR   A C    1 
ATOM   963  O  O    . TYR   A 1 42  ? 32.565 5.991   -2.286  1.00 11.75 ?  42  TYR   A O    1 
ATOM   964  C  CB   . TYR   A 1 42  ? 31.911 5.823   -5.134  1.00 12.38 ?  42  TYR   A CB   1 
ATOM   965  C  CG   . TYR   A 1 42  ? 32.096 5.514   -6.604  1.00 13.14 ?  42  TYR   A CG   1 
ATOM   966  C  CD1  . TYR   A 1 42  ? 33.358 5.314   -7.139  1.00 13.76 ?  42  TYR   A CD1  1 
ATOM   967  C  CD2  . TYR   A 1 42  ? 31.008 5.395   -7.451  1.00 14.63 ?  42  TYR   A CD2  1 
ATOM   968  C  CE1  . TYR   A 1 42  ? 33.530 5.014   -8.482  1.00 14.48 ?  42  TYR   A CE1  1 
ATOM   969  C  CE2  . TYR   A 1 42  ? 31.171 5.104   -8.795  1.00 15.59 ?  42  TYR   A CE2  1 
ATOM   970  C  CZ   . TYR   A 1 42  ? 32.435 4.911   -9.305  1.00 15.22 ?  42  TYR   A CZ   1 
ATOM   971  O  OH   . TYR   A 1 42  ? 32.591 4.615   -10.640 1.00 16.87 ?  42  TYR   A OH   1 
ATOM   972  H  H    . TYR   A 1 42  ? 30.715 3.624   -4.935  1.00 13.51 ?  42  TYR   A H    1 
ATOM   973  H  HA   . TYR   A 1 42  ? 33.192 4.457   -4.320  1.00 13.56 ?  42  TYR   A HA   1 
ATOM   974  H  HB2  . TYR   A 1 42  ? 30.985 6.083   -4.999  1.00 14.86 ?  42  TYR   A HB2  1 
ATOM   975  H  HB3  . TYR   A 1 42  ? 32.495 6.570   -4.913  1.00 14.86 ?  42  TYR   A HB3  1 
ATOM   976  H  HD1  . TYR   A 1 42  ? 34.105 5.379   -6.588  1.00 16.52 ?  42  TYR   A HD1  1 
ATOM   977  H  HD2  . TYR   A 1 42  ? 30.153 5.530   -7.114  1.00 17.56 ?  42  TYR   A HD2  1 
ATOM   978  H  HE1  . TYR   A 1 42  ? 34.385 4.882   -8.828  1.00 17.37 ?  42  TYR   A HE1  1 
ATOM   979  H  HE2  . TYR   A 1 42  ? 30.427 5.033   -9.353  1.00 18.71 ?  42  TYR   A HE2  1 
ATOM   980  H  HH   . TYR   A 1 42  ? 33.408 4.519   -10.822 1.00 20.24 ?  42  TYR   A HH   1 
ATOM   981  N  N    . LEU   A 1 43  ? 31.147 4.244   -2.076  1.00 10.87 ?  43  LEU   A N    1 
ATOM   982  C  CA   . LEU   A 1 43  ? 30.715 4.578   -0.720  1.00 10.42 ?  43  LEU   A CA   1 
ATOM   983  C  C    . LEU   A 1 43  ? 30.234 6.024   -0.619  1.00 10.65 ?  43  LEU   A C    1 
ATOM   984  O  O    . LEU   A 1 43  ? 30.504 6.722   0.360   1.00 11.30 ?  43  LEU   A O    1 
ATOM   985  C  CB   . LEU   A 1 43  ? 31.777 4.268   0.330   1.00 10.73 ?  43  LEU   A CB   1 
ATOM   986  C  CG   . LEU   A 1 43  ? 32.263 2.816   0.406   1.00 11.09 ?  43  LEU   A CG   1 
ATOM   987  C  CD1  . LEU   A 1 43  ? 33.327 2.696   1.484   1.00 11.79 ?  43  LEU   A CD1  1 
ATOM   988  C  CD2  . LEU   A 1 43  ? 31.118 1.857   0.682   1.00 11.74 ?  43  LEU   A CD2  1 
ATOM   989  H  H    . LEU   A 1 43  ? 30.801 3.511   -2.373  1.00 13.05 ?  43  LEU   A H    1 
ATOM   990  H  HA   . LEU   A 1 43  ? 29.951 4.018   -0.513  1.00 12.50 ?  43  LEU   A HA   1 
ATOM   991  H  HB2  . LEU   A 1 43  ? 32.553 4.822   0.158   1.00 12.88 ?  43  LEU   A HB2  1 
ATOM   992  H  HB3  . LEU   A 1 43  ? 31.412 4.487   1.203   1.00 12.88 ?  43  LEU   A HB3  1 
ATOM   993  H  HG   . LEU   A 1 43  ? 32.667 2.572   -0.443  1.00 13.31 ?  43  LEU   A HG   1 
ATOM   994  H  HD11 . LEU   A 1 43  ? 33.635 1.776   1.527   1.00 14.16 ?  43  LEU   A HD11 1 
ATOM   995  H  HD12 . LEU   A 1 43  ? 34.070 3.282   1.266   1.00 14.16 ?  43  LEU   A HD12 1 
ATOM   996  H  HD13 . LEU   A 1 43  ? 32.944 2.955   2.338   1.00 14.16 ?  43  LEU   A HD13 1 
ATOM   997  H  HD21 . LEU   A 1 43  ? 31.482 0.971   0.836   1.00 14.09 ?  43  LEU   A HD21 1 
ATOM   998  H  HD22 . LEU   A 1 43  ? 30.640 2.160   1.468   1.00 14.09 ?  43  LEU   A HD22 1 
ATOM   999  H  HD23 . LEU   A 1 43  ? 30.527 1.845   -0.085  1.00 14.09 ?  43  LEU   A HD23 1 
ATOM   1000 N  N    . LYS   A 1 44  ? 29.507 6.471   -1.643  1.00 10.53 ?  44  LYS   A N    1 
ATOM   1001 C  CA   . LYS   A 1 44  ? 28.856 7.780   -1.632  1.00 11.11 ?  44  LYS   A CA   1 
ATOM   1002 C  C    . LYS   A 1 44  ? 27.435 7.584   -1.121  1.00 10.38 ?  44  LYS   A C    1 
ATOM   1003 O  O    . LYS   A 1 44  ? 26.563 7.086   -1.836  1.00 11.54 ?  44  LYS   A O    1 
ATOM   1004 C  CB   . LYS   A 1 44  ? 28.881 8.411   -3.017  1.00 13.43 ?  44  LYS   A CB   1 
ATOM   1005 C  CG   . LYS   A 1 44  ? 30.248 8.891   -3.447  1.00 16.57 ?  44  LYS   A CG   1 
ATOM   1006 C  CD   . LYS   A 1 44  ? 30.909 9.782   -2.398  1.00 22.20 ?  44  LYS   A CD   1 
ATOM   1007 C  CE   . LYS   A 1 44  ? 32.210 10.366  -2.916  1.00 25.53 ?  44  LYS   A CE   1 
ATOM   1008 N  NZ   . LYS   A 1 44  ? 33.119 10.802  -1.818  1.00 26.55 ?  44  LYS   A NZ   1 
ATOM   1009 H  H    . LYS   A 1 44  ? 29.366 6.021   -2.363  1.00 12.64 ?  44  LYS   A H    1 
ATOM   1010 H  HA   . LYS   A 1 44  ? 29.309 8.357   -1.001  1.00 13.34 ?  44  LYS   A HA   1 
ATOM   1011 H  HB2  . LYS   A 1 44  ? 28.583 7.757   -3.666  1.00 16.12 ?  44  LYS   A HB2  1 
ATOM   1012 H  HB3  . LYS   A 1 44  ? 28.286 9.177   -3.023  1.00 16.12 ?  44  LYS   A HB3  1 
ATOM   1013 H  HG2  . LYS   A 1 44  ? 30.825 8.128   -3.602  1.00 19.89 ?  44  LYS   A HG2  1 
ATOM   1014 H  HG3  . LYS   A 1 44  ? 30.162 9.413   -4.265  1.00 19.89 ?  44  LYS   A HG3  1 
ATOM   1015 H  HD2  . LYS   A 1 44  ? 30.306 10.505  -2.167  1.00 26.64 ?  44  LYS   A HD2  1 
ATOM   1016 H  HD3  . LYS   A 1 44  ? 31.115 9.248   -1.614  1.00 26.64 ?  44  LYS   A HD3  1 
ATOM   1017 H  HE2  . LYS   A 1 44  ? 32.673 9.692   -3.437  1.00 30.64 ?  44  LYS   A HE2  1 
ATOM   1018 H  HE3  . LYS   A 1 44  ? 32.011 11.136  -3.467  1.00 30.64 ?  44  LYS   A HE3  1 
ATOM   1019 H  HZ1  . LYS   A 1 44  ? 33.867 11.140  -2.161  1.00 31.87 ?  44  LYS   A HZ1  1 
ATOM   1020 H  HZ2  . LYS   A 1 44  ? 32.720 11.429  -1.325  1.00 31.87 ?  44  LYS   A HZ2  1 
ATOM   1021 H  HZ3  . LYS   A 1 44  ? 33.323 10.112  -1.297  1.00 31.87 ?  44  LYS   A HZ3  1 
ATOM   1022 N  N    . HIS   A 1 45  ? 27.214 7.960   0.132   1.00 10.10 ?  45  HIS   A N    1 
ATOM   1023 C  CA   . HIS   A 1 45  ? 25.980 7.620   0.834   1.00 10.34 ?  45  HIS   A CA   1 
ATOM   1024 C  C    . HIS   A 1 45  ? 24.962 8.753   0.692   1.00 10.88 ?  45  HIS   A C    1 
ATOM   1025 O  O    . HIS   A 1 45  ? 24.655 9.476   1.635   1.00 12.31 ?  45  HIS   A O    1 
ATOM   1026 C  CB   . HIS   A 1 45  ? 26.283 7.357   2.297   1.00 10.16 ?  45  HIS   A CB   1 
ATOM   1027 C  CG   . HIS   A 1 45  ? 27.399 6.388   2.519   1.00 9.80  ?  45  HIS   A CG   1 
ATOM   1028 N  ND1  . HIS   A 1 45  ? 27.387 5.100   2.019   1.00 10.28 ?  45  HIS   A ND1  1 
ATOM   1029 C  CD2  . HIS   A 1 45  ? 28.572 6.537   3.182   1.00 10.16 ?  45  HIS   A CD2  1 
ATOM   1030 C  CE1  . HIS   A 1 45  ? 28.510 4.500   2.383   1.00 9.96  ?  45  HIS   A CE1  1 
ATOM   1031 N  NE2  . HIS   A 1 45  ? 29.247 5.348   3.082   1.00 10.08 ?  45  HIS   A NE2  1 
ATOM   1032 H  H    . HIS   A 1 45  ? 27.769 8.419   0.607   1.00 12.12 ?  45  HIS   A H    1 
ATOM   1033 H  HA   . HIS   A 1 45  ? 25.600 6.817   0.449   1.00 12.41 ?  45  HIS   A HA   1 
ATOM   1034 H  HB2  . HIS   A 1 45  ? 26.523 8.195   2.724   1.00 12.19 ?  45  HIS   A HB2  1 
ATOM   1035 H  HB3  . HIS   A 1 45  ? 25.486 6.993   2.720   1.00 12.19 ?  45  HIS   A HB3  1 
ATOM   1036 H  HD2  . HIS   A 1 45  ? 28.869 7.305   3.619   1.00 12.20 ?  45  HIS   A HD2  1 
ATOM   1037 H  HE1  . HIS   A 1 45  ? 28.739 3.622   2.185   1.00 11.95 ?  45  HIS   A HE1  1 
ATOM   1038 H  HE2  . HIS   A 1 45  ? 30.017 5.178   3.424   1.00 12.09 ?  45  HIS   A HE2  1 
ATOM   1039 N  N    A GLY   A 1 46  ? 24.411 8.866   -0.511  0.72 12.06 ?  46  GLY   A N    1 
ATOM   1040 N  N    B GLY   A 1 46  ? 24.440 8.897   -0.522  0.28 11.32 ?  46  GLY   A N    1 
ATOM   1041 C  CA   A GLY   A 1 46  ? 23.605 10.024  -0.843  0.72 12.60 ?  46  GLY   A CA   1 
ATOM   1042 C  CA   B GLY   A 1 46  ? 23.632 10.059  -0.851  0.28 11.52 ?  46  GLY   A CA   1 
ATOM   1043 C  C    A GLY   A 1 46  ? 22.120 9.881   -0.591  0.72 12.56 ?  46  GLY   A C    1 
ATOM   1044 C  C    B GLY   A 1 46  ? 22.176 9.974   -0.436  0.28 11.33 ?  46  GLY   A C    1 
ATOM   1045 O  O    A GLY   A 1 46  ? 21.442 10.872  -0.293  0.72 13.25 ?  46  GLY   A O    1 
ATOM   1046 O  O    B GLY   A 1 46  ? 21.583 10.976  -0.023  0.28 11.58 ?  46  GLY   A O    1 
ATOM   1047 H  H    A GLY   A 1 46  ? 24.479 8.288   -1.142  0.72 14.47 ?  46  GLY   A H    1 
ATOM   1048 H  H    B GLY   A 1 46  ? 24.534 8.337   -1.166  0.28 13.58 ?  46  GLY   A H    1 
ATOM   1049 H  HA2  A GLY   A 1 46  ? 23.915 10.786  -0.329  0.72 15.12 ?  46  GLY   A HA2  1 
ATOM   1050 H  HA2  B GLY   A 1 46  ? 24.016 10.840  -0.420  0.28 13.83 ?  46  GLY   A HA2  1 
ATOM   1051 H  HA3  A GLY   A 1 46  ? 23.713 10.228  -1.781  0.72 15.12 ?  46  GLY   A HA3  1 
ATOM   1052 H  HA3  B GLY   A 1 46  ? 23.667 10.203  -1.810  0.28 13.83 ?  46  GLY   A HA3  1 
ATOM   1053 N  N    A GLY   A 1 47  ? 21.592 8.669   -0.734  0.72 12.27 ?  47  GLY   A N    1 
ATOM   1054 N  N    B GLY   A 1 47  ? 21.588 8.791   -0.551  0.28 11.46 ?  47  GLY   A N    1 
ATOM   1055 C  CA   A GLY   A 1 47  ? 20.158 8.473   -0.665  0.72 12.21 ?  47  GLY   A CA   1 
ATOM   1056 C  CA   B GLY   A 1 47  ? 20.182 8.605   -0.270  0.28 11.52 ?  47  GLY   A CA   1 
ATOM   1057 C  C    A GLY   A 1 47  ? 19.834 7.032   -0.346  0.72 11.76 ?  47  GLY   A C    1 
ATOM   1058 C  C    B GLY   A 1 47  ? 19.881 7.144   -0.009  0.28 11.20 ?  47  GLY   A C    1 
ATOM   1059 O  O    A GLY   A 1 47  ? 20.721 6.196   -0.146  0.72 12.14 ?  47  GLY   A O    1 
ATOM   1060 O  O    B GLY   A 1 47  ? 20.786 6.313   0.104   0.28 11.42 ?  47  GLY   A O    1 
ATOM   1061 H  H    A GLY   A 1 47  ? 22.042 7.947   -0.856  0.72 14.73 ?  47  GLY   A H    1 
ATOM   1062 H  H    B GLY   A 1 47  ? 21.993 8.077   -0.784  0.28 13.76 ?  47  GLY   A H    1 
ATOM   1063 H  HA2  A GLY   A 1 47  ? 19.770 9.042   0.020   0.72 14.65 ?  47  GLY   A HA2  1 
ATOM   1064 H  HA2  B GLY   A 1 47  ? 19.928 9.120   0.513   0.28 13.82 ?  47  GLY   A HA2  1 
ATOM   1065 H  HA3  A GLY   A 1 47  ? 19.756 8.694   -1.520  0.72 14.65 ?  47  GLY   A HA3  1 
ATOM   1066 H  HA3  B GLY   A 1 47  ? 19.651 8.910   -1.026  0.28 13.82 ?  47  GLY   A HA3  1 
ATOM   1067 N  N    A GLY   A 1 48  ? 18.541 6.736   -0.328  0.72 11.96 ?  48  GLY   A N    1 
ATOM   1068 N  N    B GLY   A 1 48  ? 18.591 6.838   0.092   0.28 11.60 ?  48  GLY   A N    1 
ATOM   1069 C  CA   A GLY   A 1 48  ? 18.130 5.409   0.067   0.72 12.34 ?  48  GLY   A CA   1 
ATOM   1070 C  CA   B GLY   A 1 48  ? 18.191 5.474   0.376   0.28 11.33 ?  48  GLY   A CA   1 
ATOM   1071 C  C    A GLY   A 1 48  ? 18.585 5.098   1.480   0.72 11.50 ?  48  GLY   A C    1 
ATOM   1072 C  C    B GLY   A 1 48  ? 18.657 5.043   1.755   0.28 10.82 ?  48  GLY   A C    1 
ATOM   1073 O  O    A GLY   A 1 48  ? 18.777 5.988   2.318   0.72 11.75 ?  48  GLY   A O    1 
ATOM   1074 O  O    B GLY   A 1 48  ? 18.738 5.840   2.699   0.28 10.70 ?  48  GLY   A O    1 
ATOM   1075 H  H    A GLY   A 1 48  ? 17.898 7.273   -0.531  0.72 14.36 ?  48  GLY   A H    1 
ATOM   1076 H  H    B GLY   A 1 48  ? 17.939 7.396   0.005   0.28 13.92 ?  48  GLY   A H    1 
ATOM   1077 H  HA2  A GLY   A 1 48  ? 17.165 5.331   0.031   0.72 14.81 ?  48  GLY   A HA2  1 
ATOM   1078 H  HA2  B GLY   A 1 48  ? 17.223 5.397   0.315   0.28 13.60 ?  48  GLY   A HA2  1 
ATOM   1079 H  HA3  A GLY   A 1 48  ? 18.519 4.751   -0.531  0.72 14.81 ?  48  GLY   A HA3  1 
ATOM   1080 H  HA3  B GLY   A 1 48  ? 18.586 4.873   -0.277  0.28 13.60 ?  48  GLY   A HA3  1 
ATOM   1081 N  N    A VAL   A 1 49  ? 18.771 3.805   1.746   0.72 11.20 ?  49  VAL   A N    1 
ATOM   1082 N  N    B VAL   A 1 49  ? 18.959 3.748   1.878   0.28 10.27 ?  49  VAL   A N    1 
ATOM   1083 C  CA   A VAL   A 1 49  ? 19.241 3.368   3.057   0.72 11.17 ?  49  VAL   A CA   1 
ATOM   1084 C  CA   B VAL   A 1 49  ? 19.516 3.226   3.124   0.28 9.77  ?  49  VAL   A CA   1 
ATOM   1085 C  C    A VAL   A 1 49  ? 20.557 4.051   3.416   0.72 10.24 ?  49  VAL   A C    1 
ATOM   1086 C  C    B VAL   A 1 49  ? 20.802 3.962   3.475   0.28 9.28  ?  49  VAL   A C    1 
ATOM   1087 O  O    A VAL   A 1 49  ? 20.752 4.487   4.554   0.72 10.33 ?  49  VAL   A O    1 
ATOM   1088 O  O    B VAL   A 1 49  ? 21.030 4.337   4.631   0.28 9.08  ?  49  VAL   A O    1 
ATOM   1089 C  CB   A VAL   A 1 49  ? 19.358 1.832   3.095   0.72 12.25 ?  49  VAL   A CB   1 
ATOM   1090 C  CB   B VAL   A 1 49  ? 19.755 1.709   3.014   0.28 9.63  ?  49  VAL   A CB   1 
ATOM   1091 C  CG1  A VAL   A 1 49  ? 20.126 1.379   4.333   0.72 12.54 ?  49  VAL   A CG1  1 
ATOM   1092 C  CG1  B VAL   A 1 49  ? 20.633 1.229   4.164   0.28 9.17  ?  49  VAL   A CG1  1 
ATOM   1093 C  CG2  A VAL   A 1 49  ? 17.972 1.198   3.055   0.72 14.32 ?  49  VAL   A CG2  1 
ATOM   1094 C  CG2  B VAL   A 1 49  ? 18.438 0.947   2.989   0.28 9.94  ?  49  VAL   A CG2  1 
ATOM   1095 H  H    A VAL   A 1 49  ? 18.628 3.160   1.193   0.72 13.45 ?  49  VAL   A H    1 
ATOM   1096 H  H    B VAL   A 1 49  ? 18.858 3.159   1.259   0.28 12.33 ?  49  VAL   A H    1 
ATOM   1097 H  HA   A VAL   A 1 49  ? 18.590 3.620   3.727   0.72 13.41 ?  49  VAL   A HA   1 
ATOM   1098 H  HA   B VAL   A 1 49  ? 18.884 3.375   3.842   0.28 11.73 ?  49  VAL   A HA   1 
ATOM   1099 H  HB   A VAL   A 1 49  ? 19.848 1.523   2.316   0.72 14.71 ?  49  VAL   A HB   1 
ATOM   1100 H  HB   B VAL   A 1 49  ? 20.219 1.523   2.186   0.28 11.55 ?  49  VAL   A HB   1 
ATOM   1101 H  HG11 A VAL   A 1 49  ? 19.946 0.437   4.490   0.72 15.06 ?  49  VAL   A HG11 1 
ATOM   1102 H  HG11 B VAL   A 1 49  ? 20.533 0.268   4.260   0.28 11.00 ?  49  VAL   A HG11 1 
ATOM   1103 H  HG12 A VAL   A 1 49  ? 21.072 1.514   4.188   0.72 15.06 ?  49  VAL   A HG12 1 
ATOM   1104 H  HG12 B VAL   A 1 49  ? 21.562 1.441   3.968   0.28 11.00 ?  49  VAL   A HG12 1 
ATOM   1105 H  HG13 A VAL   A 1 49  ? 19.824 1.899   5.095   0.72 15.06 ?  49  VAL   A HG13 1 
ATOM   1106 H  HG13 B VAL   A 1 49  ? 20.358 1.671   4.982   0.28 11.00 ?  49  VAL   A HG13 1 
ATOM   1107 H  HG21 A VAL   A 1 49  ? 18.063 0.231   3.079   0.72 17.19 ?  49  VAL   A HG21 1 
ATOM   1108 H  HG21 B VAL   A 1 49  ? 18.619 -0.002  2.900   0.28 11.93 ?  49  VAL   A HG21 1 
ATOM   1109 H  HG22 A VAL   A 1 49  ? 17.466 1.501   3.825   0.72 17.19 ?  49  VAL   A HG22 1 
ATOM   1110 H  HG22 B VAL   A 1 49  ? 17.959 1.114   3.818   0.28 11.93 ?  49  VAL   A HG22 1 
ATOM   1111 H  HG23 A VAL   A 1 49  ? 17.528 1.468   2.238   0.72 17.19 ?  49  VAL   A HG23 1 
ATOM   1112 H  HG23 B VAL   A 1 49  ? 17.908 1.254   2.237   0.28 11.93 ?  49  VAL   A HG23 1 
ATOM   1113 N  N    A ALA   A 1 50  ? 21.495 4.106   2.467   0.72 10.02 ?  50  ALA   A N    1 
ATOM   1114 N  N    B ALA   A 1 50  ? 21.676 4.151   2.484   0.28 9.10  ?  50  ALA   A N    1 
ATOM   1115 C  CA   A ALA   A 1 50  ? 22.815 4.654   2.766   0.72 9.96  ?  50  ALA   A CA   1 
ATOM   1116 C  CA   B ALA   A 1 50  ? 22.984 4.739   2.754   0.28 9.41  ?  50  ALA   A CA   1 
ATOM   1117 C  C    A ALA   A 1 50  ? 22.732 6.114   3.178   0.72 10.03 ?  50  ALA   A C    1 
ATOM   1118 C  C    B ALA   A 1 50  ? 22.850 6.172   3.252   0.28 8.93  ?  50  ALA   A C    1 
ATOM   1119 O  O    A ALA   A 1 50  ? 23.385 6.536   4.141   0.72 10.86 ?  50  ALA   A O    1 
ATOM   1120 O  O    B ALA   A 1 50  ? 23.442 6.549   4.272   0.28 8.43  ?  50  ALA   A O    1 
ATOM   1121 C  CB   A ALA   A 1 50  ? 23.715 4.509   1.545   0.72 9.88  ?  50  ALA   A CB   1 
ATOM   1122 C  CB   B ALA   A 1 50  ? 23.856 4.663   1.499   0.28 9.76  ?  50  ALA   A CB   1 
ATOM   1123 H  H    A ALA   A 1 50  ? 21.395 3.839   1.656   0.72 12.03 ?  50  ALA   A H    1 
ATOM   1124 H  H    B ALA   A 1 50  ? 21.536 3.951   1.657   0.28 10.92 ?  50  ALA   A H    1 
ATOM   1125 H  HA   A ALA   A 1 50  ? 23.212 4.161   3.499   0.72 11.95 ?  50  ALA   A HA   1 
ATOM   1126 H  HA   B ALA   A 1 50  ? 23.421 4.231   3.447   0.28 11.29 ?  50  ALA   A HA   1 
ATOM   1127 H  HB1  A ALA   A 1 50  ? 24.588 4.879   1.751   0.72 11.86 ?  50  ALA   A HB1  1 
ATOM   1128 H  HB1  B ALA   A 1 50  ? 24.727 5.044   1.693   0.28 11.71 ?  50  ALA   A HB1  1 
ATOM   1129 H  HB2  A ALA   A 1 50  ? 23.796 3.570   1.323   0.72 11.86 ?  50  ALA   A HB2  1 
ATOM   1130 H  HB2  B ALA   A 1 50  ? 23.958 3.730   1.240   0.28 11.71 ?  50  ALA   A HB2  1 
ATOM   1131 H  HB3  A ALA   A 1 50  ? 23.318 4.993   0.803   0.72 11.86 ?  50  ALA   A HB3  1 
ATOM   1132 H  HB3  B ALA   A 1 50  ? 23.430 5.156   0.781   0.28 11.71 ?  50  ALA   A HB3  1 
ATOM   1133 N  N    A GLY   A 1 51  ? 21.948 6.908   2.454   0.72 10.14 ?  51  GLY   A N    1 
ATOM   1134 N  N    B GLY   A 1 51  ? 22.066 6.990   2.549   0.28 9.50  ?  51  GLY   A N    1 
ATOM   1135 C  CA   A GLY   A 1 51  ? 21.813 8.302   2.825   0.72 10.49 ?  51  GLY   A CA   1 
ATOM   1136 C  CA   B GLY   A 1 51  ? 21.866 8.354   3.004   0.28 9.55  ?  51  GLY   A CA   1 
ATOM   1137 C  C    A GLY   A 1 51  ? 21.213 8.467   4.205   0.72 10.24 ?  51  GLY   A C    1 
ATOM   1138 C  C    B GLY   A 1 51  ? 21.223 8.411   4.376   0.28 10.06 ?  51  GLY   A C    1 
ATOM   1139 O  O    A GLY   A 1 51  ? 21.609 9.357   4.960   0.72 10.76 ?  51  GLY   A O    1 
ATOM   1140 O  O    B GLY   A 1 51  ? 21.552 9.275   5.193   0.28 10.61 ?  51  GLY   A O    1 
ATOM   1141 H  H    A GLY   A 1 51  ? 21.503 6.669   1.759   0.72 12.17 ?  51  GLY   A H    1 
ATOM   1142 H  H    B GLY   A 1 51  ? 21.647 6.781   1.824   0.28 11.41 ?  51  GLY   A H    1 
ATOM   1143 H  HA2  A GLY   A 1 51  ? 22.683 8.727   2.819   0.72 12.59 ?  51  GLY   A HA2  1 
ATOM   1144 H  HA2  B GLY   A 1 51  ? 22.722 8.810   3.044   0.28 11.47 ?  51  GLY   A HA2  1 
ATOM   1145 H  HA3  A GLY   A 1 51  ? 21.241 8.755   2.188   0.72 12.59 ?  51  GLY   A HA3  1 
ATOM   1146 H  HA3  B GLY   A 1 51  ? 21.298 8.825   2.373   0.28 11.47 ?  51  GLY   A HA3  1 
ATOM   1147 N  N    A ALA   A 1 52  ? 20.244 7.613   4.550   0.72 10.22 ?  52  ALA   A N    1 
ATOM   1148 N  N    B ALA   A 1 52  ? 20.300 7.485   4.648   0.28 10.16 ?  52  ALA   A N    1 
ATOM   1149 C  CA   A ALA   A 1 52  ? 19.607 7.696   5.860   0.72 10.60 ?  52  ALA   A CA   1 
ATOM   1150 C  CA   B ALA   A 1 52  ? 19.644 7.444   5.949   0.28 10.21 ?  52  ALA   A CA   1 
ATOM   1151 C  C    A ALA   A 1 52  ? 20.560 7.269   6.972   0.72 9.94  ?  52  ALA   A C    1 
ATOM   1152 C  C    B ALA   A 1 52  ? 20.631 7.079   7.052   0.28 10.13 ?  52  ALA   A C    1 
ATOM   1153 O  O    A ALA   A 1 52  ? 20.645 7.928   8.015   0.72 11.09 ?  52  ALA   A O    1 
ATOM   1154 O  O    B ALA   A 1 52  ? 20.686 7.742   8.095   0.28 10.58 ?  52  ALA   A O    1 
ATOM   1155 C  CB   A ALA   A 1 52  ? 18.326 6.861   5.878   0.72 11.18 ?  52  ALA   A CB   1 
ATOM   1156 C  CB   B ALA   A 1 52  ? 18.477 6.454   5.910   0.28 10.22 ?  52  ALA   A CB   1 
ATOM   1157 H  H    A ALA   A 1 52  ? 19.949 6.977   4.052   0.72 12.27 ?  52  ALA   A H    1 
ATOM   1158 H  H    B ALA   A 1 52  ? 20.047 6.871   4.101   0.28 12.20 ?  52  ALA   A H    1 
ATOM   1159 H  HA   A ALA   A 1 52  ? 19.361 8.615   6.028   0.72 12.72 ?  52  ALA   A HA   1 
ATOM   1160 H  HA   B ALA   A 1 52  ? 19.287 8.319   6.150   0.28 12.25 ?  52  ALA   A HA   1 
ATOM   1161 H  HB1  A ALA   A 1 52  ? 17.913 6.933   6.756   0.72 13.42 ?  52  ALA   A HB1  1 
ATOM   1162 H  HB1  B ALA   A 1 52  ? 18.050 6.437   6.781   0.28 12.26 ?  52  ALA   A HB1  1 
ATOM   1163 H  HB2  A ALA   A 1 52  ? 17.718 7.202   5.202   0.72 13.42 ?  52  ALA   A HB2  1 
ATOM   1164 H  HB2  B ALA   A 1 52  ? 17.843 6.745   5.236   0.28 12.26 ?  52  ALA   A HB2  1 
ATOM   1165 H  HB3  A ALA   A 1 52  ? 18.543 5.935   5.692   0.72 13.42 ?  52  ALA   A HB3  1 
ATOM   1166 H  HB3  B ALA   A 1 52  ? 18.815 5.573   5.689   0.28 12.26 ?  52  ALA   A HB3  1 
ATOM   1167 N  N    A LEU   A 1 53  ? 21.273 6.152   6.787   0.72 10.06 ?  53  LEU   A N    1 
ATOM   1168 N  N    B LEU   A 1 53  ? 21.416 6.016   6.847   0.28 9.69  ?  53  LEU   A N    1 
ATOM   1169 C  CA   A LEU   A 1 53  ? 22.235 5.730   7.803   0.72 10.41 ?  53  LEU   A CA   1 
ATOM   1170 C  CA   B LEU   A 1 53  ? 22.420 5.649   7.842   0.28 9.29  ?  53  LEU   A CA   1 
ATOM   1171 C  C    A LEU   A 1 53  ? 23.295 6.800   8.000   0.72 9.81  ?  53  LEU   A C    1 
ATOM   1172 C  C    B LEU   A 1 53  ? 23.432 6.770   8.027   0.28 9.43  ?  53  LEU   A C    1 
ATOM   1173 O  O    A LEU   A 1 53  ? 23.623 7.170   9.132   0.72 10.79 ?  53  LEU   A O    1 
ATOM   1174 O  O    B LEU   A 1 53  ? 23.786 7.118   9.158   0.28 9.95  ?  53  LEU   A O    1 
ATOM   1175 C  CB   A LEU   A 1 53  ? 22.886 4.400   7.417   0.72 11.05 ?  53  LEU   A CB   1 
ATOM   1176 C  CB   B LEU   A 1 53  ? 23.138 4.363   7.428   0.28 8.86  ?  53  LEU   A CB   1 
ATOM   1177 C  CG   A LEU   A 1 53  ? 21.986 3.157   7.447   0.72 11.39 ?  53  LEU   A CG   1 
ATOM   1178 C  CG   B LEU   A 1 53  ? 22.378 3.039   7.524   0.28 8.96  ?  53  LEU   A CG   1 
ATOM   1179 C  CD1  A LEU   A 1 53  ? 22.719 1.959   6.866   0.72 11.61 ?  53  LEU   A CD1  1 
ATOM   1180 C  CD1  B LEU   A 1 53  ? 23.200 1.929   6.885   0.28 9.27  ?  53  LEU   A CD1  1 
ATOM   1181 C  CD2  A LEU   A 1 53  ? 21.501 2.851   8.855   0.72 12.18 ?  53  LEU   A CD2  1 
ATOM   1182 C  CD2  B LEU   A 1 53  ? 22.065 2.693   8.967   0.28 8.72  ?  53  LEU   A CD2  1 
ATOM   1183 H  H    A LEU   A 1 53  ? 21.219 5.630   6.102   0.72 12.08 ?  53  LEU   A H    1 
ATOM   1184 H  H    B LEU   A 1 53  ? 21.390 5.502   6.156   0.28 11.63 ?  53  LEU   A H    1 
ATOM   1185 H  HA   A LEU   A 1 53  ? 21.777 5.606   8.649   0.72 12.49 ?  53  LEU   A HA   1 
ATOM   1186 H  HA   B LEU   A 1 53  ? 21.984 5.489   8.693   0.28 11.15 ?  53  LEU   A HA   1 
ATOM   1187 H  HB2  A LEU   A 1 53  ? 23.235 4.481   6.516   0.72 13.26 ?  53  LEU   A HB2  1 
ATOM   1188 H  HB2  B LEU   A 1 53  ? 23.415 4.460   6.505   0.28 10.63 ?  53  LEU   A HB2  1 
ATOM   1189 H  HB3  A LEU   A 1 53  ? 23.624 4.232   8.029   0.72 13.26 ?  53  LEU   A HB3  1 
ATOM   1190 H  HB3  B LEU   A 1 53  ? 23.927 4.270   7.986   0.28 10.63 ?  53  LEU   A HB3  1 
ATOM   1191 H  HG   A LEU   A 1 53  ? 21.209 3.326   6.892   0.72 13.67 ?  53  LEU   A HG   1 
ATOM   1192 H  HG   B LEU   A 1 53  ? 21.542 3.111   7.038   0.28 10.76 ?  53  LEU   A HG   1 
ATOM   1193 H  HD11 A LEU   A 1 53  ? 22.132 1.187   6.893   0.72 13.94 ?  53  LEU   A HD11 1 
ATOM   1194 H  HD11 B LEU   A 1 53  ? 22.712 1.094   6.952   0.28 11.13 ?  53  LEU   A HD11 1 
ATOM   1195 H  HD12 A LEU   A 1 53  ? 22.968 2.153   5.949   0.72 13.94 ?  53  LEU   A HD12 1 
ATOM   1196 H  HD12 B LEU   A 1 53  ? 23.356 2.148   5.953   0.28 11.13 ?  53  LEU   A HD12 1 
ATOM   1197 H  HD13 A LEU   A 1 53  ? 23.515 1.788   7.395   0.72 13.94 ?  53  LEU   A HD13 1 
ATOM   1198 H  HD13 B LEU   A 1 53  ? 24.047 1.855   7.353   0.28 11.13 ?  53  LEU   A HD13 1 
ATOM   1199 H  HD21 A LEU   A 1 53  ? 20.999 2.021   8.841   0.72 14.61 ?  53  LEU   A HD21 1 
ATOM   1200 H  HD21 B LEU   A 1 53  ? 21.602 1.841   8.995   0.28 10.46 ?  53  LEU   A HD21 1 
ATOM   1201 H  HD22 A LEU   A 1 53  ? 22.266 2.767   9.443   0.72 14.61 ?  53  LEU   A HD22 1 
ATOM   1202 H  HD22 B LEU   A 1 53  ? 22.896 2.634   9.464   0.28 10.46 ?  53  LEU   A HD22 1 
ATOM   1203 H  HD23 A LEU   A 1 53  ? 20.929 3.576   9.157   0.72 14.61 ?  53  LEU   A HD23 1 
ATOM   1204 H  HD23 B LEU   A 1 53  ? 21.503 3.387   9.343   0.28 10.46 ?  53  LEU   A HD23 1 
ATOM   1205 N  N    A ASN   A 1 54  ? 23.826 7.330   6.902   0.72 9.79  ?  54  ASN   A N    1 
ATOM   1206 N  N    B ASN   A 1 54  ? 23.903 7.352   6.924   0.28 9.86  ?  54  ASN   A N    1 
ATOM   1207 C  CA   A ASN   A 1 54  ? 24.888 8.317   7.038   0.72 9.60  ?  54  ASN   A CA   1 
ATOM   1208 C  CA   B ASN   A 1 54  ? 24.941 8.372   7.028   0.28 10.03 ?  54  ASN   A CA   1 
ATOM   1209 C  C    A ASN   A 1 54  ? 24.388 9.558   7.773   0.72 10.20 ?  54  ASN   A C    1 
ATOM   1210 C  C    B ASN   A 1 54  ? 24.421 9.623   7.725   0.28 10.30 ?  54  ASN   A C    1 
ATOM   1211 O  O    A ASN   A 1 54  ? 25.074 10.088  8.659   0.72 10.38 ?  54  ASN   A O    1 
ATOM   1212 O  O    B ASN   A 1 54  ? 25.133 10.229  8.535   0.28 10.47 ?  54  ASN   A O    1 
ATOM   1213 C  CB   A ASN   A 1 54  ? 25.447 8.694   5.675   0.72 9.85  ?  54  ASN   A CB   1 
ATOM   1214 C  CB   B ASN   A 1 54  ? 25.495 8.716   5.648   0.28 10.57 ?  54  ASN   A CB   1 
ATOM   1215 C  CG   A ASN   A 1 54  ? 26.477 9.786   5.790   0.72 9.57  ?  54  ASN   A CG   1 
ATOM   1216 C  CG   B ASN   A 1 54  ? 26.470 9.867   5.699   0.28 10.91 ?  54  ASN   A CG   1 
ATOM   1217 O  OD1  A ASN   A 1 54  ? 27.459 9.647   6.527   0.72 9.45  ?  54  ASN   A OD1  1 
ATOM   1218 O  OD1  B ASN   A 1 54  ? 27.571 9.731   6.230   0.28 11.67 ?  54  ASN   A OD1  1 
ATOM   1219 N  ND2  A ASN   A 1 54  ? 26.249 10.897  5.108   0.72 10.32 ?  54  ASN   A ND2  1 
ATOM   1220 N  ND2  B ASN   A 1 54  ? 26.072 11.014  5.161   0.28 10.96 ?  54  ASN   A ND2  1 
ATOM   1221 H  H    A ASN   A 1 54  ? 23.593 7.140   6.093   0.72 11.75 ?  54  ASN   A H    1 
ATOM   1222 H  H    B ASN   A 1 54  ? 23.641 7.177   6.126   0.28 11.83 ?  54  ASN   A H    1 
ATOM   1223 H  HA   A ASN   A 1 54  ? 25.605 7.929   7.554   0.72 11.52 ?  54  ASN   A HA   1 
ATOM   1224 H  HA   B ASN   A 1 54  ? 25.668 8.022   7.561   0.28 12.03 ?  54  ASN   A HA   1 
ATOM   1225 H  HB2  A ASN   A 1 54  ? 25.866 7.908   5.275   0.72 11.82 ?  54  ASN   A HB2  1 
ATOM   1226 H  HB2  B ASN   A 1 54  ? 25.962 7.941   5.295   0.28 12.69 ?  54  ASN   A HB2  1 
ATOM   1227 H  HB3  A ASN   A 1 54  ? 24.726 9.006   5.105   0.72 11.82 ?  54  ASN   A HB3  1 
ATOM   1228 H  HB3  B ASN   A 1 54  ? 24.764 8.963   5.063   0.28 12.69 ?  54  ASN   A HB3  1 
ATOM   1229 H  HD21 A ASN   A 1 54  ? 26.812 11.544  5.152   0.72 12.39 ?  54  ASN   A HD21 1 
ATOM   1230 H  HD21 B ASN   A 1 54  ? 26.591 11.701  5.176   0.28 13.16 ?  54  ASN   A HD21 1 
ATOM   1231 H  HD22 A ASN   A 1 54  ? 25.548 10.963  4.620   0.72 12.39 ?  54  ASN   A HD22 1 
ATOM   1232 H  HD22 B ASN   A 1 54  ? 25.296 11.071  4.796   0.28 13.16 ?  54  ASN   A HD22 1 
ATOM   1233 N  N    . LYS   A 1 55  ? 23.183 10.026  7.429   1.00 10.55 ?  55  LYS   A N    1 
ATOM   1234 C  CA   . LYS   A 1 55  ? 22.607 11.184  8.103   1.00 11.14 ?  55  LYS   A CA   1 
ATOM   1235 C  C    . LYS   A 1 55  ? 22.517 10.941  9.602   1.00 11.35 ?  55  LYS   A C    1 
ATOM   1236 O  O    . LYS   A 1 55  ? 22.795 11.837  10.405  1.00 11.99 ?  55  LYS   A O    1 
ATOM   1237 C  CB   . LYS   A 1 55  ? 21.230 11.482  7.505   1.00 11.76 ?  55  LYS   A CB   1 
ATOM   1238 C  CG   . LYS   A 1 55  ? 20.482 12.637  8.153   1.00 13.00 ?  55  LYS   A CG   1 
ATOM   1239 C  CD   . LYS   A 1 55  ? 19.147 12.873  7.443   1.00 14.61 ?  55  LYS   A CD   1 
ATOM   1240 C  CE   . LYS   A 1 55  ? 18.344 14.000  8.063   1.00 16.16 ?  55  LYS   A CE   1 
ATOM   1241 N  NZ   . LYS   A 1 55  ? 17.003 14.140  7.418   1.00 17.21 ?  55  LYS   A NZ   1 
ATOM   1242 H  H    A LYS   A 1 55  ? 22.678 9.685   6.819   0.72 12.66 ?  55  LYS   A H    1 
ATOM   1243 H  H    B LYS   A 1 55  ? 22.658 9.642   6.862   0.28 12.66 ?  55  LYS   A H    1 
ATOM   1244 H  HA   . LYS   A 1 55  ? 23.177 11.952  7.956   1.00 13.37 ?  55  LYS   A HA   1 
ATOM   1245 H  HB2  . LYS   A 1 55  ? 21.343 11.702  6.568   1.00 14.11 ?  55  LYS   A HB2  1 
ATOM   1246 H  HB3  . LYS   A 1 55  ? 20.676 10.691  7.590   1.00 14.11 ?  55  LYS   A HB3  1 
ATOM   1247 H  HG2  . LYS   A 1 55  ? 20.297 12.421  9.083   1.00 15.61 ?  55  LYS   A HG2  1 
ATOM   1248 H  HG3  . LYS   A 1 55  ? 21.011 13.443  8.091   1.00 15.61 ?  55  LYS   A HG3  1 
ATOM   1249 H  HD2  . LYS   A 1 55  ? 19.321 13.098  6.517   1.00 17.54 ?  55  LYS   A HD2  1 
ATOM   1250 H  HD3  . LYS   A 1 55  ? 18.616 12.061  7.493   1.00 17.54 ?  55  LYS   A HD3  1 
ATOM   1251 H  HE2  . LYS   A 1 55  ? 18.210 13.816  9.006   1.00 19.40 ?  55  LYS   A HE2  1 
ATOM   1252 H  HE3  . LYS   A 1 55  ? 18.824 14.834  7.948   1.00 19.40 ?  55  LYS   A HE3  1 
ATOM   1253 H  HZ1  . LYS   A 1 55  ? 16.473 14.645  7.924   1.00 20.66 ?  55  LYS   A HZ1  1 
ATOM   1254 H  HZ2  . LYS   A 1 55  ? 17.085 14.518  6.618   1.00 20.66 ?  55  LYS   A HZ2  1 
ATOM   1255 H  HZ3  . LYS   A 1 55  ? 16.625 13.337  7.322   1.00 20.66 ?  55  LYS   A HZ3  1 
ATOM   1256 N  N    . ALA   A 1 56  ? 22.132 9.728   9.999   1.00 11.68 ?  56  ALA   A N    1 
ATOM   1257 C  CA   . ALA   A 1 56  ? 22.019 9.400   11.413  1.00 12.42 ?  56  ALA   A CA   1 
ATOM   1258 C  C    . ALA   A 1 56  ? 23.363 9.443   12.129  1.00 11.91 ?  56  ALA   A C    1 
ATOM   1259 O  O    . ALA   A 1 56  ? 23.390 9.635   13.344  1.00 13.49 ?  56  ALA   A O    1 
ATOM   1260 C  CB   . ALA   A 1 56  ? 21.357 8.030   11.585  1.00 13.18 ?  56  ALA   A CB   1 
ATOM   1261 H  H    . ALA   A 1 56  ? 21.931 9.083   9.468   1.00 14.02 ?  56  ALA   A H    1 
ATOM   1262 H  HA   . ALA   A 1 56  ? 21.449 10.051  11.840  1.00 14.91 ?  56  ALA   A HA   1 
ATOM   1263 H  HB1  . ALA   A 1 56  ? 21.287 7.827   12.534  1.00 15.82 ?  56  ALA   A HB1  1 
ATOM   1264 H  HB2  . ALA   A 1 56  ? 20.469 8.058   11.191  1.00 15.82 ?  56  ALA   A HB2  1 
ATOM   1265 H  HB3  . ALA   A 1 56  ? 21.893 7.355   11.143  1.00 15.82 ?  56  ALA   A HB3  1 
ATOM   1266 N  N    . THR   A 1 57  ? 24.474 9.266   11.407  1.00 11.29 ?  57  THR   A N    1 
ATOM   1267 C  CA   . THR   A 1 57  ? 25.818 9.390   11.978  1.00 11.42 ?  57  THR   A CA   1 
ATOM   1268 C  C    . THR   A 1 57  ? 26.365 10.807  11.894  1.00 11.87 ?  57  THR   A C    1 
ATOM   1269 O  O    . THR   A 1 57  ? 27.550 11.019  12.184  1.00 12.38 ?  57  THR   A O    1 
ATOM   1270 C  CB   . THR   A 1 57  ? 26.827 8.440   11.302  1.00 11.51 ?  57  THR   A CB   1 
ATOM   1271 O  OG1  . THR   A 1 57  ? 27.205 8.937   10.007  1.00 11.14 ?  57  THR   A OG1  1 
ATOM   1272 C  CG2  . THR   A 1 57  ? 26.305 7.016   11.212  1.00 11.42 ?  57  THR   A CG2  1 
ATOM   1273 H  H    . THR   A 1 57  ? 24.475 9.059   10.568  1.00 13.55 ?  57  THR   A H    1 
ATOM   1274 H  HA   . THR   A 1 57  ? 25.770 9.136   12.918  1.00 13.70 ?  57  THR   A HA   1 
ATOM   1275 H  HB   . THR   A 1 57  ? 27.622 8.402   11.862  1.00 13.81 ?  57  THR   A HB   1 
ATOM   1276 H  HG1  . THR   A 1 57  ? 26.524 8.990   9.522   1.00 13.37 ?  57  THR   A HG1  1 
ATOM   1277 H  HG21 . THR   A 1 57  ? 26.922 6.463   10.706  1.00 13.70 ?  57  THR   A HG21 1 
ATOM   1278 H  HG22 . THR   A 1 57  ? 26.205 6.633   12.102  1.00 13.70 ?  57  THR   A HG22 1 
ATOM   1279 H  HG23 . THR   A 1 57  ? 25.441 6.999   10.772  1.00 13.70 ?  57  THR   A HG23 1 
ATOM   1280 N  N    . ASN   A 1 58  ? 25.547 11.776  11.492  1.00 12.08 ?  58  ASN   A N    1 
ATOM   1281 C  CA   . ASN   A 1 58  ? 26.004 13.156  11.396  1.00 13.07 ?  58  ASN   A CA   1 
ATOM   1282 C  C    . ASN   A 1 58  ? 27.146 13.287  10.385  1.00 11.90 ?  58  ASN   A C    1 
ATOM   1283 O  O    . ASN   A 1 58  ? 28.044 14.118  10.542  1.00 12.70 ?  58  ASN   A O    1 
ATOM   1284 C  CB   . ASN   A 1 58  ? 26.384 13.684  12.794  1.00 15.61 ?  58  ASN   A CB   1 
ATOM   1285 C  CG   . ASN   A 1 58  ? 26.818 15.133  12.796  1.00 18.96 ?  58  ASN   A CG   1 
ATOM   1286 O  OD1  . ASN   A 1 58  ? 26.189 15.969  12.161  1.00 20.50 ?  58  ASN   A OD1  1 
ATOM   1287 N  ND2  . ASN   A 1 58  ? 27.893 15.440  13.531  1.00 20.00 ?  58  ASN   A ND2  1 
ATOM   1288 H  H    . ASN   A 1 58  ? 24.728 11.647  11.257  1.00 14.50 ?  58  ASN   A H    1 
ATOM   1289 H  HA   . ASN   A 1 58  ? 25.266 13.689  11.072  1.00 15.69 ?  58  ASN   A HA   1 
ATOM   1290 H  HB2  . ASN   A 1 58  ? 25.608 13.600  13.379  1.00 18.73 ?  58  ASN   A HB2  1 
ATOM   1291 H  HB3  . ASN   A 1 58  ? 27.113 13.156  13.148  1.00 18.73 ?  58  ASN   A HB3  1 
ATOM   1292 H  HD21 . ASN   A 1 58  ? 28.174 16.252  13.566  1.00 24.00 ?  58  ASN   A HD21 1 
ATOM   1293 H  HD22 . ASN   A 1 58  ? 28.302 14.824  13.967  1.00 24.00 ?  58  ASN   A HD22 1 
ATOM   1294 N  N    . ASN   A 1 59  ? 27.126 12.467  9.333   1.00 10.98 ?  59  ASN   A N    1 
ATOM   1295 C  CA   . ASN   A 1 59  ? 28.097 12.452  8.235   1.00 11.01 ?  59  ASN   A CA   1 
ATOM   1296 C  C    . ASN   A 1 59  ? 29.414 11.775  8.617   1.00 10.93 ?  59  ASN   A C    1 
ATOM   1297 O  O    . ASN   A 1 59  ? 30.329 11.735  7.789   1.00 11.16 ?  59  ASN   A O    1 
ATOM   1298 C  CB   . ASN   A 1 59  ? 28.374 13.840  7.629   1.00 10.77 ?  59  ASN   A CB   1 
ATOM   1299 C  CG   . ASN   A 1 59  ? 28.722 13.771  6.161   1.00 11.17 ?  59  ASN   A CG   1 
ATOM   1300 O  OD1  . ASN   A 1 59  ? 28.016 13.143  5.376   1.00 11.60 ?  59  ASN   A OD1  1 
ATOM   1301 N  ND2  . ASN   A 1 59  ? 29.802 14.439  5.774   1.00 11.73 ?  59  ASN   A ND2  1 
ATOM   1302 H  H    . ASN   A 1 59  ? 26.516 11.871  9.221   1.00 13.18 ?  59  ASN   A H    1 
ATOM   1303 H  HA   . ASN   A 1 59  ? 27.716 11.924  7.522   1.00 13.22 ?  59  ASN   A HA   1 
ATOM   1304 H  HB2  . ASN   A 1 59  ? 27.585 14.397  7.717   1.00 12.93 ?  59  ASN   A HB2  1 
ATOM   1305 H  HB3  . ASN   A 1 59  ? 29.123 14.253  8.091   1.00 12.93 ?  59  ASN   A HB3  1 
ATOM   1306 H  HD21 . ASN   A 1 59  ? 30.044 14.435  4.948   1.00 14.08 ?  59  ASN   A HD21 1 
ATOM   1307 H  HD22 . ASN   A 1 59  ? 30.275 14.877  6.352   1.00 14.08 ?  59  ASN   A HD22 1 
ATOM   1308 N  N    . ALA   A 1 60  ? 29.542 11.229  9.823   1.00 10.73 ?  60  ALA   A N    1 
ATOM   1309 C  CA   . ALA   A 1 60  ? 30.783 10.550  10.178  1.00 10.95 ?  60  ALA   A CA   1 
ATOM   1310 C  C    . ALA   A 1 60  ? 31.011 9.321   9.305   1.00 10.95 ?  60  ALA   A C    1 
ATOM   1311 O  O    . ALA   A 1 60  ? 32.154 9.004   8.959   1.00 11.19 ?  60  ALA   A O    1 
ATOM   1312 C  CB   . ALA   A 1 60  ? 30.783 10.175  11.658  1.00 11.56 ?  60  ALA   A CB   1 
ATOM   1313 H  H    . ALA   A 1 60  ? 28.946 11.238  10.439  1.00 12.88 ?  60  ALA   A H    1 
ATOM   1314 H  HA   . ALA   A 1 60  ? 31.527 11.158  10.028  1.00 13.14 ?  60  ALA   A HA   1 
ATOM   1315 H  HB1  . ALA   A 1 60  ? 31.614 9.727   11.873  1.00 13.87 ?  60  ALA   A HB1  1 
ATOM   1316 H  HB2  . ALA   A 1 60  ? 30.697 10.986  12.188  1.00 13.87 ?  60  ALA   A HB2  1 
ATOM   1317 H  HB3  . ALA   A 1 60  ? 30.032 9.587   11.833  1.00 13.87 ?  60  ALA   A HB3  1 
ATOM   1318 N  N    . MET   A 1 61  ? 29.941 8.613   8.941   1.00 10.31 ?  61  MET   A N    1 
ATOM   1319 C  CA   . MET   A 1 61  ? 30.081 7.481   8.033   1.00 10.03 ?  61  MET   A CA   1 
ATOM   1320 C  C    . MET   A 1 61  ? 30.701 7.913   6.707   1.00 10.30 ?  61  MET   A C    1 
ATOM   1321 O  O    . MET   A 1 61  ? 31.590 7.237   6.180   1.00 10.16 ?  61  MET   A O    1 
ATOM   1322 C  CB   . MET   A 1 61  ? 28.718 6.814   7.833   1.00 10.03 ?  61  MET   A CB   1 
ATOM   1323 C  CG   . MET   A 1 61  ? 28.716 5.665   6.842   1.00 10.75 ?  61  MET   A CG   1 
ATOM   1324 S  SD   . MET   A 1 61  ? 27.102 4.910   6.645   1.00 11.82 ?  61  MET   A SD   1 
ATOM   1325 C  CE   . MET   A 1 61  ? 26.960 4.032   8.197   1.00 13.14 ?  61  MET   A CE   1 
ATOM   1326 H  H    . MET   A 1 61  ? 29.137 8.770   9.203   1.00 12.37 ?  61  MET   A H    1 
ATOM   1327 H  HA   . MET   A 1 61  ? 30.667 6.830   8.446   1.00 12.04 ?  61  MET   A HA   1 
ATOM   1328 H  HB2  . MET   A 1 61  ? 28.421 6.464   8.686   1.00 12.04 ?  61  MET   A HB2  1 
ATOM   1329 H  HB3  . MET   A 1 61  ? 28.091 7.481   7.517   1.00 12.04 ?  61  MET   A HB3  1 
ATOM   1330 H  HG2  . MET   A 1 61  ? 28.986 5.996   5.968   1.00 12.90 ?  61  MET   A HG2  1 
ATOM   1331 H  HG3  . MET   A 1 61  ? 29.325 4.980   7.141   1.00 12.90 ?  61  MET   A HG3  1 
ATOM   1332 H  HE1  . MET   A 1 61  ? 26.133 3.527   8.201   1.00 15.77 ?  61  MET   A HE1  1 
ATOM   1333 H  HE2  . MET   A 1 61  ? 27.716 3.432   8.286   1.00 15.77 ?  61  MET   A HE2  1 
ATOM   1334 H  HE3  . MET   A 1 61  ? 26.960 4.675   8.925   1.00 15.77 ?  61  MET   A HE3  1 
ATOM   1335 N  N    . GLN   A 1 62  ? 30.247 9.039   6.151   1.00 10.16 ?  62  GLN   A N    1 
ATOM   1336 C  CA   . GLN   A 1 62  ? 30.805 9.517   4.888   1.00 10.54 ?  62  GLN   A CA   1 
ATOM   1337 C  C    . GLN   A 1 62  ? 32.273 9.898   5.025   1.00 10.61 ?  62  GLN   A C    1 
ATOM   1338 O  O    . GLN   A 1 62  ? 33.080 9.584   4.146   1.00 10.85 ?  62  GLN   A O    1 
ATOM   1339 C  CB   . GLN   A 1 62  ? 29.993 10.696  4.354   1.00 10.40 ?  62  GLN   A CB   1 
ATOM   1340 C  CG   . GLN   A 1 62  ? 30.368 11.065  2.933   1.00 10.57 ?  62  GLN   A CG   1 
ATOM   1341 C  CD   . GLN   A 1 62  ? 30.034 9.938   1.987   1.00 10.90 ?  62  GLN   A CD   1 
ATOM   1342 O  OE1  . GLN   A 1 62  ? 28.852 9.624   1.791   1.00 11.31 ?  62  GLN   A OE1  1 
ATOM   1343 N  NE2  . GLN   A 1 62  ? 31.053 9.268   1.449   1.00 11.34 ?  62  GLN   A NE2  1 
ATOM   1344 H  H    . GLN   A 1 62  ? 29.627 9.534   6.480   1.00 12.20 ?  62  GLN   A H    1 
ATOM   1345 H  HA   . GLN   A 1 62  ? 30.752 8.799   4.238   1.00 12.65 ?  62  GLN   A HA   1 
ATOM   1346 H  HB2  . GLN   A 1 62  ? 29.051 10.464  4.363   1.00 12.49 ?  62  GLN   A HB2  1 
ATOM   1347 H  HB3  . GLN   A 1 62  ? 30.151 11.471  4.915   1.00 12.49 ?  62  GLN   A HB3  1 
ATOM   1348 H  HG2  . GLN   A 1 62  ? 29.865 11.846  2.661   1.00 12.69 ?  62  GLN   A HG2  1 
ATOM   1349 H  HG3  . GLN   A 1 62  ? 31.320 11.238  2.882   1.00 12.69 ?  62  GLN   A HG3  1 
ATOM   1350 H  HE21 . GLN   A 1 62  ? 31.862 9.505   1.624   1.00 13.61 ?  62  GLN   A HE21 1 
ATOM   1351 H  HE22 . GLN   A 1 62  ? 30.903 8.612   0.916   1.00 13.61 ?  62  GLN   A HE22 1 
ATOM   1352 N  N    . VAL   A 1 63  ? 32.638 10.590  6.109   1.00 10.94 ?  63  VAL   A N    1 
ATOM   1353 C  CA   . VAL   A 1 63  ? 34.032 10.984  6.313   1.00 11.73 ?  63  VAL   A CA   1 
ATOM   1354 C  C    . VAL   A 1 63  ? 34.928 9.750   6.368   1.00 11.14 ?  63  VAL   A C    1 
ATOM   1355 O  O    . VAL   A 1 63  ? 35.976 9.684   5.710   1.00 11.55 ?  63  VAL   A O    1 
ATOM   1356 C  CB   . VAL   A 1 63  ? 34.151 11.859  7.574   1.00 13.25 ?  63  VAL   A CB   1 
ATOM   1357 C  CG1  . VAL   A 1 63  ? 35.597 12.111  7.918   1.00 15.11 ?  63  VAL   A CG1  1 
ATOM   1358 C  CG2  . VAL   A 1 63  ? 33.406 13.178  7.367   1.00 13.85 ?  63  VAL   A CG2  1 
ATOM   1359 H  H    . VAL   A 1 63  ? 32.097 10.837  6.734   1.00 13.13 ?  63  VAL   A H    1 
ATOM   1360 H  HA   . VAL   A 1 63  ? 34.311 11.517  5.557   1.00 14.08 ?  63  VAL   A HA   1 
ATOM   1361 H  HB   . VAL   A 1 63  ? 33.741 11.395  8.324   1.00 15.90 ?  63  VAL   A HB   1 
ATOM   1362 H  HG11 . VAL   A 1 63  ? 35.647 12.846  8.549   1.00 18.14 ?  63  VAL   A HG11 1 
ATOM   1363 H  HG12 . VAL   A 1 63  ? 35.978 11.311  8.310   1.00 18.14 ?  63  VAL   A HG12 1 
ATOM   1364 H  HG13 . VAL   A 1 63  ? 36.076 12.344  7.105   1.00 18.14 ?  63  VAL   A HG13 1 
ATOM   1365 H  HG21 . VAL   A 1 63  ? 33.506 13.727  8.162   1.00 16.63 ?  63  VAL   A HG21 1 
ATOM   1366 H  HG22 . VAL   A 1 63  ? 33.781 13.638  6.600   1.00 16.63 ?  63  VAL   A HG22 1 
ATOM   1367 H  HG23 . VAL   A 1 63  ? 32.465 12.992  7.214   1.00 16.63 ?  63  VAL   A HG23 1 
ATOM   1368 N  N    . GLU   A 1 64  ? 34.510 8.741   7.137   1.00 11.10 ?  64  GLU   A N    1 
ATOM   1369 C  CA   . GLU   A 1 64  ? 35.274 7.504   7.232   1.00 10.78 ?  64  GLU   A CA   1 
ATOM   1370 C  C    . GLU   A 1 64  ? 35.359 6.816   5.879   1.00 10.85 ?  64  GLU   A C    1 
ATOM   1371 O  O    . GLU   A 1 64  ? 36.410 6.276   5.499   1.00 11.19 ?  64  GLU   A O    1 
ATOM   1372 C  CB   . GLU   A 1 64  ? 34.593 6.597   8.255   1.00 11.44 ?  64  GLU   A CB   1 
ATOM   1373 C  CG   . GLU   A 1 64  ? 35.254 5.248   8.407   1.00 11.95 ?  64  GLU   A CG   1 
ATOM   1374 C  CD   . GLU   A 1 64  ? 34.375 4.252   9.137   1.00 12.58 ?  64  GLU   A CD   1 
ATOM   1375 O  OE1  . GLU   A 1 64  ? 33.135 4.334   9.006   1.00 13.13 ?  64  GLU   A OE1  1 
ATOM   1376 O  OE2  . GLU   A 1 64  ? 34.919 3.362   9.828   1.00 13.00 -1 64  GLU   A OE2  1 
ATOM   1377 H  H    . GLU   A 1 64  ? 33.781 8.742   7.597   1.00 13.32 ?  64  GLU   A H    1 
ATOM   1378 H  HA   . GLU   A 1 64  ? 36.173 7.706   7.542   1.00 12.94 ?  64  GLU   A HA   1 
ATOM   1379 H  HB2  . GLU   A 1 64  ? 34.617 7.038   9.124   1.00 13.74 ?  64  GLU   A HB2  1 
ATOM   1380 H  HB3  . GLU   A 1 64  ? 33.676 6.460   7.984   1.00 13.74 ?  64  GLU   A HB3  1 
ATOM   1381 H  HG2  . GLU   A 1 64  ? 35.454 4.878   7.531   1.00 14.34 ?  64  GLU   A HG2  1 
ATOM   1382 H  HG3  . GLU   A 1 64  ? 36.070 5.349   8.917   1.00 14.34 ?  64  GLU   A HG3  1 
ATOM   1383 N  N    . SER   A 1 65  ? 34.242 6.804   5.150   1.00 10.41 ?  65  SER   A N    1 
ATOM   1384 C  CA   . SER   A 1 65  ? 34.192 6.142   3.855   1.00 10.19 ?  65  SER   A CA   1 
ATOM   1385 C  C    . SER   A 1 65  ? 35.106 6.814   2.846   1.00 10.72 ?  65  SER   A C    1 
ATOM   1386 O  O    . SER   A 1 65  ? 35.730 6.142   2.020   1.00 11.34 ?  65  SER   A O    1 
ATOM   1387 C  CB   . SER   A 1 65  ? 32.757 6.150   3.331   1.00 10.49 ?  65  SER   A CB   1 
ATOM   1388 O  OG   . SER   A 1 65  ? 31.906 5.344   4.138   1.00 10.80 ?  65  SER   A OG   1 
ATOM   1389 H  H    . SER   A 1 65  ? 33.510 7.175   5.387   1.00 12.50 ?  65  SER   A H    1 
ATOM   1390 H  HA   . SER   A 1 65  ? 34.479 5.221   3.949   1.00 12.23 ?  65  SER   A HA   1 
ATOM   1391 H  HB2  . SER   A 1 65  ? 32.426 7.061   3.333   1.00 12.59 ?  65  SER   A HB2  1 
ATOM   1392 H  HB3  . SER   A 1 65  ? 32.753 5.800   2.426   1.00 12.59 ?  65  SER   A HB3  1 
ATOM   1393 H  HG   . SER   A 1 65  ? 31.904 5.640   4.929   1.00 12.96 ?  65  SER   A HG   1 
ATOM   1394 N  N    . ASP   A 1 66  ? 35.167 8.147   2.864   1.00 10.62 ?  66  ASP   A N    1 
ATOM   1395 C  CA   . ASP   A 1 66  ? 36.021 8.846   1.909   1.00 11.41 ?  66  ASP   A CA   1 
ATOM   1396 C  C    . ASP   A 1 66  ? 37.486 8.492   2.128   1.00 11.69 ?  66  ASP   A C    1 
ATOM   1397 O  O    . ASP   A 1 66  ? 38.248 8.320   1.166   1.00 12.69 ?  66  ASP   A O    1 
ATOM   1398 C  CB   . ASP   A 1 66  ? 35.812 10.353  2.021   1.00 13.23 ?  66  ASP   A CB   1 
ATOM   1399 C  CG   . ASP   A 1 66  ? 34.473 10.819  1.443   1.00 14.65 ?  66  ASP   A CG   1 
ATOM   1400 O  OD1  . ASP   A 1 66  ? 33.743 10.026  0.807   1.00 14.42 ?  66  ASP   A OD1  1 
ATOM   1401 O  OD2  . ASP   A 1 66  ? 34.170 12.018  1.613   1.00 17.41 -1 66  ASP   A OD2  1 
ATOM   1402 H  H    . ASP   A 1 66  ? 34.725 8.660   3.400   1.00 12.74 ?  66  ASP   A H    1 
ATOM   1403 H  HA   . ASP   A 1 66  ? 35.774 8.577   1.009   1.00 13.69 ?  66  ASP   A HA   1 
ATOM   1404 H  HB2  . ASP   A 1 66  ? 35.830 10.606  2.958   1.00 15.88 ?  66  ASP   A HB2  1 
ATOM   1405 H  HB3  . ASP   A 1 66  ? 36.526 10.806  1.543   1.00 15.88 ?  66  ASP   A HB3  1 
ATOM   1406 N  N    . ASP   A 1 67  ? 37.896 8.366   3.389   1.00 11.90 ?  67  ASP   A N    1 
ATOM   1407 C  CA   . ASP   A 1 67  ? 39.250 7.913   3.677   1.00 12.80 ?  67  ASP   A CA   1 
ATOM   1408 C  C    . ASP   A 1 67  ? 39.461 6.478   3.210   1.00 12.79 ?  67  ASP   A C    1 
ATOM   1409 O  O    . ASP   A 1 67  ? 40.516 6.151   2.657   1.00 13.50 ?  67  ASP   A O    1 
ATOM   1410 C  CB   . ASP   A 1 67  ? 39.527 8.039   5.171   1.00 13.88 ?  67  ASP   A CB   1 
ATOM   1411 C  CG   . ASP   A 1 67  ? 40.821 7.375   5.580   1.00 14.96 ?  67  ASP   A CG   1 
ATOM   1412 O  OD1  . ASP   A 1 67  ? 41.888 8.002   5.405   1.00 17.91 ?  67  ASP   A OD1  1 
ATOM   1413 O  OD2  . ASP   A 1 67  ? 40.774 6.220   6.065   1.00 14.80 -1 67  ASP   A OD2  1 
ATOM   1414 H  H    . ASP   A 1 67  ? 37.421 8.542   4.079   1.00 14.29 ?  67  ASP   A H    1 
ATOM   1415 H  HA   . ASP   A 1 67  ? 39.881 8.473   3.199   1.00 15.37 ?  67  ASP   A HA   1 
ATOM   1416 H  HB2  . ASP   A 1 67  ? 39.584 8.976   5.397   1.00 16.66 ?  67  ASP   A HB2  1 
ATOM   1417 H  HB3  . ASP   A 1 67  ? 38.805 7.615   5.658   1.00 16.66 ?  67  ASP   A HB3  1 
ATOM   1418 N  N    . TYR   A 1 68  ? 38.467 5.605   3.414   1.00 11.67 ?  68  TYR   A N    1 
ATOM   1419 C  CA   . TYR   A 1 68  ? 38.584 4.226   2.939   1.00 12.12 ?  68  TYR   A CA   1 
ATOM   1420 C  C    . TYR   A 1 68  ? 38.813 4.183   1.428   1.00 11.81 ?  68  TYR   A C    1 
ATOM   1421 O  O    . TYR   A 1 68  ? 39.684 3.445   0.941   1.00 12.59 ?  68  TYR   A O    1 
ATOM   1422 C  CB   . TYR   A 1 68  ? 37.341 3.405   3.334   1.00 12.70 ?  68  TYR   A CB   1 
ATOM   1423 C  CG   . TYR   A 1 68  ? 37.363 2.023   2.705   1.00 13.78 ?  68  TYR   A CG   1 
ATOM   1424 C  CD1  . TYR   A 1 68  ? 36.897 1.833   1.407   1.00 15.11 ?  68  TYR   A CD1  1 
ATOM   1425 C  CD2  . TYR   A 1 68  ? 37.913 0.936   3.366   1.00 15.22 ?  68  TYR   A CD2  1 
ATOM   1426 C  CE1  . TYR   A 1 68  ? 36.963 0.620   0.787   1.00 16.55 ?  68  TYR   A CE1  1 
ATOM   1427 C  CE2  . TYR   A 1 68  ? 37.971 -0.320  2.745   1.00 15.76 ?  68  TYR   A CE2  1 
ATOM   1428 C  CZ   . TYR   A 1 68  ? 37.502 -0.448  1.455   1.00 16.26 ?  68  TYR   A CZ   1 
ATOM   1429 O  OH   . TYR   A 1 68  ? 37.580 -1.656  0.825   1.00 17.40 ?  68  TYR   A OH   1 
ATOM   1430 H  H    . TYR   A 1 68  ? 37.730 5.781   3.824   1.00 14.01 ?  68  TYR   A H    1 
ATOM   1431 H  HA   . TYR   A 1 68  ? 39.350 3.817   3.362   1.00 14.55 ?  68  TYR   A HA   1 
ATOM   1432 H  HB2  . TYR   A 1 68  ? 37.322 3.298   4.298   1.00 15.25 ?  68  TYR   A HB2  1 
ATOM   1433 H  HB3  . TYR   A 1 68  ? 36.542 3.864   3.031   1.00 15.25 ?  68  TYR   A HB3  1 
ATOM   1434 H  HD1  . TYR   A 1 68  ? 36.544 2.563   0.945   1.00 18.13 ?  68  TYR   A HD1  1 
ATOM   1435 H  HD2  . TYR   A 1 68  ? 38.251 1.039   4.226   1.00 18.27 ?  68  TYR   A HD2  1 
ATOM   1436 H  HE1  . TYR   A 1 68  ? 36.637 0.522   -0.078  1.00 19.86 ?  68  TYR   A HE1  1 
ATOM   1437 H  HE2  . TYR   A 1 68  ? 38.345 -1.050  3.181   1.00 18.91 ?  68  TYR   A HE2  1 
ATOM   1438 H  HH   . TYR   A 1 68  ? 37.915 -2.229  1.344   1.00 20.89 ?  68  TYR   A HH   1 
ATOM   1439 N  N    . ILE   A 1 69  ? 38.025 4.948   0.665   1.00 11.68 ?  69  ILE   A N    1 
ATOM   1440 C  CA   . ILE   A 1 69  ? 38.153 4.927   -0.788  1.00 11.93 ?  69  ILE   A CA   1 
ATOM   1441 C  C    . ILE   A 1 69  ? 39.482 5.531   -1.227  1.00 11.74 ?  69  ILE   A C    1 
ATOM   1442 O  O    . ILE   A 1 69  ? 40.119 5.045   -2.169  1.00 12.12 ?  69  ILE   A O    1 
ATOM   1443 C  CB   . ILE   A 1 69  ? 36.956 5.643   -1.443  1.00 13.02 ?  69  ILE   A CB   1 
ATOM   1444 C  CG1  . ILE   A 1 69  ? 35.644 4.908   -1.167  1.00 13.31 ?  69  ILE   A CG1  1 
ATOM   1445 C  CG2  . ILE   A 1 69  ? 37.193 5.848   -2.945  1.00 14.33 ?  69  ILE   A CG2  1 
ATOM   1446 C  CD1  . ILE   A 1 69  ? 35.489 3.599   -1.916  1.00 13.85 ?  69  ILE   A CD1  1 
ATOM   1447 H  H    . ILE   A 1 69  ? 37.425 5.484   0.962   1.00 14.02 ?  69  ILE   A H    1 
ATOM   1448 H  HA   . ILE   A 1 69  ? 38.142 4.003   -1.087  1.00 14.31 ?  69  ILE   A HA   1 
ATOM   1449 H  HB   . ILE   A 1 69  ? 36.886 6.518   -1.040  1.00 15.63 ?  69  ILE   A HB   1 
ATOM   1450 H  HG12 . ILE   A 1 69  ? 35.593 4.712   -0.216  1.00 15.97 ?  69  ILE   A HG12 1 
ATOM   1451 H  HG13 . ILE   A 1 69  ? 34.905 5.482   -1.421  1.00 15.97 ?  69  ILE   A HG13 1 
ATOM   1452 H  HG21 . ILE   A 1 69  ? 36.345 6.051   -3.373  1.00 17.19 ?  69  ILE   A HG21 1 
ATOM   1453 H  HG22 . ILE   A 1 69  ? 37.806 6.593   -3.070  1.00 17.19 ?  69  ILE   A HG22 1 
ATOM   1454 H  HG23 . ILE   A 1 69  ? 37.569 5.041   -3.323  1.00 17.19 ?  69  ILE   A HG23 1 
ATOM   1455 H  HD11 . ILE   A 1 69  ? 34.667 3.173   -1.634  1.00 16.62 ?  69  ILE   A HD11 1 
ATOM   1456 H  HD12 . ILE   A 1 69  ? 35.459 3.781   -2.867  1.00 16.62 ?  69  ILE   A HD12 1 
ATOM   1457 H  HD13 . ILE   A 1 69  ? 36.245 3.026   -1.711  1.00 16.62 ?  69  ILE   A HD13 1 
ATOM   1458 N  N    . ALA   A 1 70  ? 39.907 6.612   -0.576  1.00 12.18 ?  70  ALA   A N    1 
ATOM   1459 C  CA   . ALA   A 1 70  ? 41.182 7.219   -0.939  1.00 13.12 ?  70  ALA   A CA   1 
ATOM   1460 C  C    . ALA   A 1 70  ? 42.328 6.231   -0.763  1.00 13.06 ?  70  ALA   A C    1 
ATOM   1461 O  O    . ALA   A 1 70  ? 43.293 6.255   -1.531  1.00 14.80 ?  70  ALA   A O    1 
ATOM   1462 C  CB   . ALA   A 1 70  ? 41.414 8.480   -0.104  1.00 13.53 ?  70  ALA   A CB   1 
ATOM   1463 H  H    . ALA   A 1 70  ? 39.483 7.005   0.058   1.00 14.62 ?  70  ALA   A H    1 
ATOM   1464 H  HA   . ALA   A 1 70  ? 41.152 7.484   -1.872  1.00 15.75 ?  70  ALA   A HA   1 
ATOM   1465 H  HB1  . ALA   A 1 70  ? 42.268 8.870   -0.356  1.00 16.24 ?  70  ALA   A HB1  1 
ATOM   1466 H  HB2  . ALA   A 1 70  ? 40.700 9.111   -0.274  1.00 16.24 ?  70  ALA   A HB2  1 
ATOM   1467 H  HB3  . ALA   A 1 70  ? 41.429 8.237   0.835   1.00 16.24 ?  70  ALA   A HB3  1 
ATOM   1468 N  N    . THR   A 1 71  ? 42.229 5.346   0.226   1.00 12.68 ?  71  THR   A N    1 
ATOM   1469 C  CA   . THR   A 1 71  ? 43.279 4.364   0.470   1.00 14.13 ?  71  THR   A CA   1 
ATOM   1470 C  C    . THR   A 1 71  ? 43.157 3.144   -0.431  1.00 14.20 ?  71  THR   A C    1 
ATOM   1471 O  O    . THR   A 1 71  ? 44.169 2.648   -0.942  1.00 16.29 ?  71  THR   A O    1 
ATOM   1472 C  CB   . THR   A 1 71  ? 43.221 3.914   1.924   1.00 15.86 ?  71  THR   A CB   1 
ATOM   1473 O  OG1  . THR   A 1 71  ? 43.493 5.036   2.769   1.00 17.00 ?  71  THR   A OG1  1 
ATOM   1474 C  CG2  . THR   A 1 71  ? 44.224 2.792   2.195   1.00 17.20 ?  71  THR   A CG2  1 
ATOM   1475 H  H    . THR   A 1 71  ? 41.564 5.291   0.768   1.00 15.22 ?  71  THR   A H    1 
ATOM   1476 H  HA   . THR   A 1 71  ? 44.145 4.771   0.308   1.00 16.96 ?  71  THR   A HA   1 
ATOM   1477 H  HB   . THR   A 1 71  ? 42.332 3.570   2.115   1.00 19.03 ?  71  THR   A HB   1 
ATOM   1478 H  HG1  . THR   A 1 71  ? 43.465 4.790   3.575   1.00 20.40 ?  71  THR   A HG1  1 
ATOM   1479 H  HG21 . THR   A 1 71  ? 44.377 2.712   3.150   1.00 20.64 ?  71  THR   A HG21 1 
ATOM   1480 H  HG22 . THR   A 1 71  ? 43.889 1.947   1.859   1.00 20.64 ?  71  THR   A HG22 1 
ATOM   1481 H  HG23 . THR   A 1 71  ? 45.070 2.992   1.760   1.00 20.64 ?  71  THR   A HG23 1 
ATOM   1482 N  N    . ASN   A 1 72  ? 41.938 2.636   -0.621  1.00 13.34 ?  72  ASN   A N    1 
ATOM   1483 C  CA   . ASN   A 1 72  ? 41.721 1.313   -1.185  1.00 13.70 ?  72  ASN   A CA   1 
ATOM   1484 C  C    . ASN   A 1 72  ? 41.090 1.308   -2.565  1.00 13.65 ?  72  ASN   A C    1 
ATOM   1485 O  O    . ASN   A 1 72  ? 41.096 0.257   -3.218  1.00 14.80 ?  72  ASN   A O    1 
ATOM   1486 C  CB   . ASN   A 1 72  ? 40.835 0.495   -0.240  1.00 14.53 ?  72  ASN   A CB   1 
ATOM   1487 C  CG   . ASN   A 1 72  ? 41.455 0.338   1.124   1.00 15.53 ?  72  ASN   A CG   1 
ATOM   1488 O  OD1  . ASN   A 1 72  ? 41.001 0.931   2.102   1.00 17.20 ?  72  ASN   A OD1  1 
ATOM   1489 N  ND2  . ASN   A 1 72  ? 42.509 -0.441  1.196   1.00 15.86 ?  72  ASN   A ND2  1 
ATOM   1490 H  H    . ASN   A 1 72  ? 41.204 3.054   -0.431  1.00 16.01 ?  72  ASN   A H    1 
ATOM   1491 H  HA   . ASN   A 1 72  ? 42.573 0.863   -1.256  1.00 16.44 ?  72  ASN   A HA   1 
ATOM   1492 H  HB2  . ASN   A 1 72  ? 39.980 0.937   -0.136  1.00 17.44 ?  72  ASN   A HB2  1 
ATOM   1493 H  HB3  . ASN   A 1 72  ? 40.709 -0.394  -0.612  1.00 17.44 ?  72  ASN   A HB3  1 
ATOM   1494 H  HD21 . ASN   A 1 72  ? 42.905 -0.553  1.952   1.00 19.03 ?  72  ASN   A HD21 1 
ATOM   1495 H  HD22 . ASN   A 1 72  ? 42.806 -0.827  0.491   1.00 19.03 ?  72  ASN   A HD22 1 
ATOM   1496 N  N    . GLY   A 1 73  ? 40.531 2.424   -3.016  1.00 13.37 ?  73  GLY   A N    1 
ATOM   1497 C  CA   . GLY   A 1 73  ? 39.792 2.441   -4.252  1.00 12.88 ?  73  GLY   A CA   1 
ATOM   1498 C  C    . GLY   A 1 73  ? 38.402 1.861   -4.081  1.00 12.33 ?  73  GLY   A C    1 
ATOM   1499 O  O    . GLY   A 1 73  ? 38.020 1.399   -2.999  1.00 13.02 ?  73  GLY   A O    1 
ATOM   1500 H  H    . GLY   A 1 73  ? 40.569 3.192   -2.624  1.00 16.04 ?  73  GLY   A H    1 
ATOM   1501 H  HA2  . GLY   A 1 73  ? 39.709 3.355   -4.570  1.00 15.46 ?  73  GLY   A HA2  1 
ATOM   1502 H  HA3  . GLY   A 1 73  ? 40.263 1.923   -4.924  1.00 15.46 ?  73  GLY   A HA3  1 
ATOM   1503 N  N    . PRO   A 1 74  ? 37.621 1.879   -5.160  1.00 12.71 ?  74  PRO   A N    1 
ATOM   1504 C  CA   . PRO   A 1 74  ? 36.225 1.446   -5.074  1.00 12.51 ?  74  PRO   A CA   1 
ATOM   1505 C  C    . PRO   A 1 74  ? 36.080 -0.036  -4.755  1.00 12.34 ?  74  PRO   A C    1 
ATOM   1506 O  O    . PRO   A 1 74  ? 36.949 -0.868  -5.037  1.00 13.37 ?  74  PRO   A O    1 
ATOM   1507 C  CB   . PRO   A 1 74  ? 35.669 1.756   -6.471  1.00 14.31 ?  74  PRO   A CB   1 
ATOM   1508 C  CG   . PRO   A 1 74  ? 36.623 2.740   -7.074  1.00 17.02 ?  74  PRO   A CG   1 
ATOM   1509 C  CD   . PRO   A 1 74  ? 37.961 2.390   -6.497  1.00 14.70 ?  74  PRO   A CD   1 
ATOM   1510 H  HA   . PRO   A 1 74  ? 35.739 1.970   -4.411  1.00 15.02 ?  74  PRO   A HA   1 
ATOM   1511 H  HB2  . PRO   A 1 74  ? 35.632 0.940   -6.994  1.00 17.18 ?  74  PRO   A HB2  1 
ATOM   1512 H  HB3  . PRO   A 1 74  ? 34.779 2.146   -6.389  1.00 17.18 ?  74  PRO   A HB3  1 
ATOM   1513 H  HG2  . PRO   A 1 74  ? 36.632 2.638   -8.039  1.00 20.43 ?  74  PRO   A HG2  1 
ATOM   1514 H  HG3  . PRO   A 1 74  ? 36.368 3.640   -6.825  1.00 20.43 ?  74  PRO   A HG3  1 
ATOM   1515 H  HD2  . PRO   A 1 74  ? 38.391 1.697   -7.022  1.00 17.64 ?  74  PRO   A HD2  1 
ATOM   1516 H  HD3  . PRO   A 1 74  ? 38.515 3.186   -6.436  1.00 17.64 ?  74  PRO   A HD3  1 
ATOM   1517 N  N    . LEU   A 1 75  ? 34.937 -0.357  -4.164  1.00 11.69 ?  75  LEU   A N    1 
ATOM   1518 C  CA   . LEU   A 1 75  ? 34.543 -1.746  -4.007  1.00 11.28 ?  75  LEU   A CA   1 
ATOM   1519 C  C    . LEU   A 1 75  ? 34.140 -2.325  -5.360  1.00 12.04 ?  75  LEU   A C    1 
ATOM   1520 O  O    . LEU   A 1 75  ? 34.005 -1.612  -6.358  1.00 13.38 ?  75  LEU   A O    1 
ATOM   1521 C  CB   . LEU   A 1 75  ? 33.367 -1.875  -3.042  1.00 11.58 ?  75  LEU   A CB   1 
ATOM   1522 C  CG   . LEU   A 1 75  ? 33.595 -1.457  -1.594  1.00 13.21 ?  75  LEU   A CG   1 
ATOM   1523 C  CD1  . LEU   A 1 75  ? 32.321 -1.646  -0.783  1.00 15.11 ?  75  LEU   A CD1  1 
ATOM   1524 C  CD2  . LEU   A 1 75  ? 34.745 -2.195  -0.966  1.00 16.66 ?  75  LEU   A CD2  1 
ATOM   1525 H  H    . LEU   A 1 75  ? 34.368 0.208   -3.852  1.00 14.03 ?  75  LEU   A H    1 
ATOM   1526 H  HA   . LEU   A 1 75  ? 35.291 -2.258  -3.670  1.00 13.54 ?  75  LEU   A HA   1 
ATOM   1527 H  HB2  . LEU   A 1 75  ? 32.640 -1.338  -3.383  1.00 13.90 ?  75  LEU   A HB2  1 
ATOM   1528 H  HB3  . LEU   A 1 75  ? 33.098 -2.808  -3.029  1.00 13.90 ?  75  LEU   A HB3  1 
ATOM   1529 H  HG   . LEU   A 1 75  ? 33.817 -0.513  -1.581  1.00 15.85 ?  75  LEU   A HG   1 
ATOM   1530 H  HD11 . LEU   A 1 75  ? 32.487 -1.371  0.133   1.00 18.13 ?  75  LEU   A HD11 1 
ATOM   1531 H  HD12 . LEU   A 1 75  ? 31.619 -1.098  -1.170  1.00 18.13 ?  75  LEU   A HD12 1 
ATOM   1532 H  HD13 . LEU   A 1 75  ? 32.065 -2.579  -0.808  1.00 18.13 ?  75  LEU   A HD13 1 
ATOM   1533 H  HD21 . LEU   A 1 75  ? 34.804 -1.952  -0.029  1.00 20.00 ?  75  LEU   A HD21 1 
ATOM   1534 H  HD22 . LEU   A 1 75  ? 34.598 -3.148  -1.055  1.00 20.00 ?  75  LEU   A HD22 1 
ATOM   1535 H  HD23 . LEU   A 1 75  ? 35.570 -1.946  -1.421  1.00 20.00 ?  75  LEU   A HD23 1 
ATOM   1536 N  N    . LYS   A 1 76  ? 33.968 -3.644  -5.384  1.00 12.23 ?  76  LYS   A N    1 
ATOM   1537 C  CA   . LYS   A 1 76  ? 33.371 -4.355  -6.507  1.00 12.83 ?  76  LYS   A CA   1 
ATOM   1538 C  C    . LYS   A 1 76  ? 31.865 -4.450  -6.296  1.00 11.58 ?  76  LYS   A C    1 
ATOM   1539 O  O    . LYS   A 1 76  ? 31.400 -4.577  -5.165  1.00 11.24 ?  76  LYS   A O    1 
ATOM   1540 C  CB   . LYS   A 1 76  ? 33.919 -5.790  -6.579  1.00 14.63 ?  76  LYS   A CB   1 
ATOM   1541 C  CG   . LYS   A 1 76  ? 35.432 -5.893  -6.746  1.00 15.93 ?  76  LYS   A CG   1 
ATOM   1542 C  CD   . LYS   A 1 76  ? 35.944 -7.302  -6.564  1.00 16.93 ?  76  LYS   A CD   1 
ATOM   1543 C  CE   . LYS   A 1 76  ? 37.446 -7.356  -6.723  1.00 19.53 ?  76  LYS   A CE   1 
ATOM   1544 N  NZ   . LYS   A 1 76  ? 37.973 -8.725  -6.577  1.00 20.81 ?  76  LYS   A NZ   1 
ATOM   1545 H  H    . LYS   A 1 76  ? 34.194 -4.167  -4.739  1.00 14.67 ?  76  LYS   A H    1 
ATOM   1546 H  HA   . LYS   A 1 76  ? 33.557 -3.897  -7.345  1.00 15.40 ?  76  LYS   A HA   1 
ATOM   1547 H  HB2  . LYS   A 1 76  ? 33.683 -6.250  -5.758  1.00 17.56 ?  76  LYS   A HB2  1 
ATOM   1548 H  HB3  . LYS   A 1 76  ? 33.509 -6.241  -7.334  1.00 17.56 ?  76  LYS   A HB3  1 
ATOM   1549 H  HG2  . LYS   A 1 76  ? 35.670 -5.595  -7.639  1.00 19.12 ?  76  LYS   A HG2  1 
ATOM   1550 H  HG3  . LYS   A 1 76  ? 35.860 -5.326  -6.083  1.00 19.12 ?  76  LYS   A HG3  1 
ATOM   1551 H  HD2  . LYS   A 1 76  ? 35.717 -7.614  -5.674  1.00 20.32 ?  76  LYS   A HD2  1 
ATOM   1552 H  HD3  . LYS   A 1 76  ? 35.543 -7.878  -7.235  1.00 20.32 ?  76  LYS   A HD3  1 
ATOM   1553 H  HE2  . LYS   A 1 76  ? 37.681 -7.032  -7.605  1.00 23.44 ?  76  LYS   A HE2  1 
ATOM   1554 H  HE3  . LYS   A 1 76  ? 37.854 -6.800  -6.041  1.00 23.44 ?  76  LYS   A HE3  1 
ATOM   1555 H  HZ1  . LYS   A 1 76  ? 38.856 -8.728  -6.675  1.00 24.97 ?  76  LYS   A HZ1  1 
ATOM   1556 H  HZ2  . LYS   A 1 76  ? 37.770 -9.049  -5.771  1.00 24.97 ?  76  LYS   A HZ2  1 
ATOM   1557 H  HZ3  . LYS   A 1 76  ? 37.613 -9.260  -7.196  1.00 24.97 ?  76  LYS   A HZ3  1 
ATOM   1558 N  N    . VAL   A 1 77  ? 31.101 -4.418  -7.392  1.00 12.03 ?  77  VAL   A N    1 
ATOM   1559 C  CA   . VAL   A 1 77  ? 29.697 -4.809  -7.295  1.00 11.68 ?  77  VAL   A CA   1 
ATOM   1560 C  C    . VAL   A 1 77  ? 29.640 -6.264  -6.853  1.00 11.38 ?  77  VAL   A C    1 
ATOM   1561 O  O    . VAL   A 1 77  ? 30.298 -7.130  -7.441  1.00 11.47 ?  77  VAL   A O    1 
ATOM   1562 C  CB   . VAL   A 1 77  ? 28.964 -4.596  -8.627  1.00 13.22 ?  77  VAL   A CB   1 
ATOM   1563 C  CG1  . VAL   A 1 77  ? 27.515 -5.055  -8.506  1.00 13.98 ?  77  VAL   A CG1  1 
ATOM   1564 C  CG2  . VAL   A 1 77  ? 29.031 -3.133  -9.042  1.00 14.61 ?  77  VAL   A CG2  1 
ATOM   1565 H  H    . VAL   A 1 77  ? 31.367 -4.179  -8.175  1.00 14.44 ?  77  VAL   A H    1 
ATOM   1566 H  HA   . VAL   A 1 77  ? 29.265 -4.269  -6.618  1.00 14.02 ?  77  VAL   A HA   1 
ATOM   1567 H  HB   . VAL   A 1 77  ? 29.397 -5.125  -9.316  1.00 15.87 ?  77  VAL   A HB   1 
ATOM   1568 H  HG11 . VAL   A 1 77  ? 27.027 -4.744  -9.283  1.00 16.78 ?  77  VAL   A HG11 1 
ATOM   1569 H  HG12 . VAL   A 1 77  ? 27.493 -6.022  -8.463  1.00 16.78 ?  77  VAL   A HG12 1 
ATOM   1570 H  HG13 . VAL   A 1 77  ? 27.134 -4.674  -7.700  1.00 16.78 ?  77  VAL   A HG13 1 
ATOM   1571 H  HG21 . VAL   A 1 77  ? 28.520 -3.014  -9.856  1.00 17.54 ?  77  VAL   A HG21 1 
ATOM   1572 H  HG22 . VAL   A 1 77  ? 28.655 -2.588  -8.331  1.00 17.54 ?  77  VAL   A HG22 1 
ATOM   1573 H  HG23 . VAL   A 1 77  ? 29.957 -2.886  -9.191  1.00 17.54 ?  77  VAL   A HG23 1 
ATOM   1574 N  N    . GLY   A 1 78  ? 28.864 -6.538  -5.801  1.00 11.13 ?  78  GLY   A N    1 
ATOM   1575 C  CA   . GLY   A 1 78  ? 28.856 -7.827  -5.144  1.00 11.14 ?  78  GLY   A CA   1 
ATOM   1576 C  C    . GLY   A 1 78  ? 29.780 -7.917  -3.950  1.00 10.67 ?  78  GLY   A C    1 
ATOM   1577 O  O    . GLY   A 1 78  ? 29.730 -8.916  -3.218  1.00 11.31 ?  78  GLY   A O    1 
ATOM   1578 H  H    . GLY   A 1 78  ? 28.312 -5.969  -5.458  1.00 13.35 ?  78  GLY   A H    1 
ATOM   1579 H  HA2  . GLY   A 1 78  ? 27.957 -8.024  -4.847  1.00 13.37 ?  78  GLY   A HA2  1 
ATOM   1580 H  HA3  . GLY   A 1 78  ? 29.119 -8.507  -5.786  1.00 13.37 ?  78  GLY   A HA3  1 
ATOM   1581 N  N    . GLY   A 1 79  ? 30.636 -6.912  -3.740  1.00 10.68 ?  79  GLY   A N    1 
ATOM   1582 C  CA   . GLY   A 1 79  ? 31.606 -6.923  -2.671  1.00 11.12 ?  79  GLY   A CA   1 
ATOM   1583 C  C    . GLY   A 1 79  ? 31.156 -6.127  -1.453  1.00 10.67 ?  79  GLY   A C    1 
ATOM   1584 O  O    . GLY   A 1 79  ? 30.039 -5.615  -1.374  1.00 11.00 ?  79  GLY   A O    1 
ATOM   1585 H  H    . GLY   A 1 79  ? 30.671 -6.199  -4.224  1.00 12.82 ?  79  GLY   A H    1 
ATOM   1586 H  HA2  . GLY   A 1 79  ? 31.767 -7.846  -2.398  1.00 13.35 ?  79  GLY   A HA2  1 
ATOM   1587 H  HA3  . GLY   A 1 79  ? 32.441 -6.555  -2.989  1.00 13.35 ?  79  GLY   A HA3  1 
ATOM   1588 N  N    . SER   A 1 80  ? 32.065 -6.037  -0.484  1.00 11.22 ?  80  SER   A N    1 
ATOM   1589 C  CA   . SER   A 1 80  ? 31.756 -5.401  0.786   1.00 10.96 ?  80  SER   A CA   1 
ATOM   1590 C  C    . SER   A 1 80  ? 33.033 -4.948  1.469   1.00 10.59 ?  80  SER   A C    1 
ATOM   1591 O  O    . SER   A 1 80  ? 34.143 -5.375  1.126   1.00 11.94 ?  80  SER   A O    1 
ATOM   1592 C  CB   . SER   A 1 80  ? 31.004 -6.363  1.718   1.00 11.64 ?  80  SER   A CB   1 
ATOM   1593 O  OG   . SER   A 1 80  ? 31.841 -7.417  2.174   1.00 13.41 ?  80  SER   A OG   1 
ATOM   1594 H  H    . SER   A 1 80  ? 32.877 -6.320  -0.550  1.00 13.47 ?  80  SER   A H    1 
ATOM   1595 H  HA   . SER   A 1 80  ? 31.203 -4.625  0.612   1.00 13.15 ?  80  SER   A HA   1 
ATOM   1596 H  HB2  . SER   A 1 80  ? 30.680 -5.865  2.481   1.00 13.97 ?  80  SER   A HB2  1 
ATOM   1597 H  HB3  . SER   A 1 80  ? 30.255 -6.743  1.229   1.00 13.97 ?  80  SER   A HB3  1 
ATOM   1598 H  HG   . SER   A 1 80  ? 32.127 -7.856  1.514   1.00 16.10 ?  80  SER   A HG   1 
ATOM   1599 N  N    . CYS   A 1 81  ? 32.847 -4.106  2.481   1.00 10.11 ?  81  CYS   A N    1 
ATOM   1600 C  CA   . CYS   A 1 81  ? 33.903 -3.828  3.438   1.00 10.63 ?  81  CYS   A CA   1 
ATOM   1601 C  C    . CYS   A 1 81  ? 33.268 -3.590  4.798   1.00 10.54 ?  81  CYS   A C    1 
ATOM   1602 O  O    . CYS   A 1 81  ? 32.102 -3.195  4.895   1.00 11.66 ?  81  CYS   A O    1 
ATOM   1603 C  CB   . CYS   A 1 81  ? 34.773 -2.636  3.015   1.00 11.55 ?  81  CYS   A CB   1 
ATOM   1604 S  SG   . CYS   A 1 81  ? 33.873 -1.062  3.032   1.00 11.68 ?  81  CYS   A SG   1 
ATOM   1605 H  H    . CYS   A 1 81  ? 32.112 -3.678  2.637   1.00 12.14 ?  81  CYS   A H    1 
ATOM   1606 H  HA   . CYS   A 1 81  ? 34.478 -4.604  3.505   1.00 12.76 ?  81  CYS   A HA   1 
ATOM   1607 H  HB2  . CYS   A 1 81  ? 35.528 -2.565  3.622   1.00 13.86 ?  81  CYS   A HB2  1 
ATOM   1608 H  HB3  . CYS   A 1 81  ? 35.099 -2.792  2.108   1.00 13.86 ?  81  CYS   A HB3  1 
ATOM   1609 H  HG   . CYS   A 1 81  ? 34.620 -0.183  2.688   1.00 14.01 ?  81  CYS   A HG   1 
ATOM   1610 N  N    . VAL   A 1 82  ? 34.044 -3.845  5.845   1.00 10.76 ?  82  VAL   A N    1 
ATOM   1611 C  CA   . VAL   A 1 82  ? 33.626 -3.608  7.219   1.00 11.24 ?  82  VAL   A CA   1 
ATOM   1612 C  C    . VAL   A 1 82  ? 34.230 -2.298  7.688   1.00 11.37 ?  82  VAL   A C    1 
ATOM   1613 O  O    . VAL   A 1 82  ? 35.455 -2.125  7.670   1.00 12.08 ?  82  VAL   A O    1 
ATOM   1614 C  CB   . VAL   A 1 82  ? 34.058 -4.749  8.150   1.00 12.87 ?  82  VAL   A CB   1 
ATOM   1615 C  CG1  . VAL   A 1 82  ? 33.602 -4.455  9.572   1.00 14.64 ?  82  VAL   A CG1  1 
ATOM   1616 C  CG2  . VAL   A 1 82  ? 33.507 -6.077  7.673   1.00 13.82 ?  82  VAL   A CG2  1 
ATOM   1617 H  H    . VAL   A 1 82  ? 34.843 -4.173  5.781   1.00 12.92 ?  82  VAL   A H    1 
ATOM   1618 H  HA   . VAL   A 1 82  ? 32.660 -3.534  7.250   1.00 13.49 ?  82  VAL   A HA   1 
ATOM   1619 H  HB   . VAL   A 1 82  ? 35.026 -4.803  8.155   1.00 15.45 ?  82  VAL   A HB   1 
ATOM   1620 H  HG11 . VAL   A 1 82  ? 33.686 -5.262  10.104  1.00 17.57 ?  82  VAL   A HG11 1 
ATOM   1621 H  HG12 . VAL   A 1 82  ? 34.152 -3.752  9.951   1.00 17.57 ?  82  VAL   A HG12 1 
ATOM   1622 H  HG13 . VAL   A 1 82  ? 32.671 -4.172  9.554   1.00 17.57 ?  82  VAL   A HG13 1 
ATOM   1623 H  HG21 . VAL   A 1 82  ? 33.759 -6.766  8.307   1.00 16.58 ?  82  VAL   A HG21 1 
ATOM   1624 H  HG22 . VAL   A 1 82  ? 32.542 -6.014  7.616   1.00 16.58 ?  82  VAL   A HG22 1 
ATOM   1625 H  HG23 . VAL   A 1 82  ? 33.880 -6.275  6.801   1.00 16.58 ?  82  VAL   A HG23 1 
ATOM   1626 N  N    . LEU   A 1 83  ? 33.375 -1.376  8.112   1.00 11.09 ?  83  LEU   A N    1 
ATOM   1627 C  CA   . LEU   A 1 83  ? 33.795 -0.108  8.682   1.00 11.01 ?  83  LEU   A CA   1 
ATOM   1628 C  C    . LEU   A 1 83  ? 33.089 0.066   10.020  1.00 11.35 ?  83  LEU   A C    1 
ATOM   1629 O  O    . LEU   A 1 83  ? 32.370 -0.823  10.484  1.00 11.70 ?  83  LEU   A O    1 
ATOM   1630 C  CB   . LEU   A 1 83  ? 33.528 1.048   7.707   1.00 11.18 ?  83  LEU   A CB   1 
ATOM   1631 C  CG   . LEU   A 1 83  ? 34.422 1.044   6.461   1.00 12.39 ?  83  LEU   A CG   1 
ATOM   1632 C  CD1  . LEU   A 1 83  ? 33.972 2.081   5.448   1.00 12.84 ?  83  LEU   A CD1  1 
ATOM   1633 C  CD2  . LEU   A 1 83  ? 35.891 1.258   6.838   1.00 12.86 ?  83  LEU   A CD2  1 
ATOM   1634 H  H    . LEU   A 1 83  ? 32.519 -1.465  8.067   1.00 13.31 ?  83  LEU   A H    1 
ATOM   1635 H  HA   . LEU   A 1 83  ? 34.748 -0.137  8.848   1.00 13.21 ?  83  LEU   A HA   1 
ATOM   1636 H  HB2  . LEU   A 1 83  ? 32.607 1.000   7.404   1.00 13.41 ?  83  LEU   A HB2  1 
ATOM   1637 H  HB3  . LEU   A 1 83  ? 33.673 1.889   8.169   1.00 13.41 ?  83  LEU   A HB3  1 
ATOM   1638 H  HG   . LEU   A 1 83  ? 34.359 0.174   6.041   1.00 14.88 ?  83  LEU   A HG   1 
ATOM   1639 H  HD11 . LEU   A 1 83  ? 34.561 2.038   4.675   1.00 15.42 ?  83  LEU   A HD11 1 
ATOM   1640 H  HD12 . LEU   A 1 83  ? 33.063 1.879   5.181   1.00 15.42 ?  83  LEU   A HD12 1 
ATOM   1641 H  HD13 . LEU   A 1 83  ? 34.017 2.958   5.852   1.00 15.42 ?  83  LEU   A HD13 1 
ATOM   1642 H  HD21 . LEU   A 1 83  ? 36.401 1.434   6.031   1.00 15.44 ?  83  LEU   A HD21 1 
ATOM   1643 H  HD22 . LEU   A 1 83  ? 35.955 2.019   7.439   1.00 15.44 ?  83  LEU   A HD22 1 
ATOM   1644 H  HD23 . LEU   A 1 83  ? 36.228 0.462   7.276   1.00 15.44 ?  83  LEU   A HD23 1 
ATOM   1645 N  N    . SER   A 1 84  ? 33.302 1.214   10.654  1.00 11.68 ?  84  SER   A N    1 
ATOM   1646 C  CA   . SER   A 1 84  ? 32.663 1.467   11.934  1.00 11.70 ?  84  SER   A CA   1 
ATOM   1647 C  C    . SER   A 1 84  ? 31.145 1.546   11.793  1.00 11.60 ?  84  SER   A C    1 
ATOM   1648 O  O    . SER   A 1 84  ? 30.618 2.018   10.787  1.00 11.70 ?  84  SER   A O    1 
ATOM   1649 C  CB   . SER   A 1 84  ? 33.156 2.791   12.507  1.00 12.35 ?  84  SER   A CB   1 
ATOM   1650 O  OG   . SER   A 1 84  ? 32.533 3.063   13.746  1.00 13.46 ?  84  SER   A OG   1 
ATOM   1651 H  H    . SER   A 1 84  ? 33.800 1.859   10.356  1.00 14.02 ?  84  SER   A H    1 
ATOM   1652 H  HA   . SER   A 1 84  ? 32.886 0.757   12.547  1.00 14.05 ?  84  SER   A HA   1 
ATOM   1653 H  HB2  . SER   A 1 84  ? 34.117 2.743   12.635  1.00 14.83 ?  84  SER   A HB2  1 
ATOM   1654 H  HB3  . SER   A 1 84  ? 32.944 3.507   11.882  1.00 14.83 ?  84  SER   A HB3  1 
ATOM   1655 H  HG   . SER   A 1 84  ? 32.815 3.796   14.054  1.00 16.15 ?  84  SER   A HG   1 
ATOM   1656 N  N    . GLY   A 1 85  ? 30.444 1.118   12.838  1.00 12.42 ?  85  GLY   A N    1 
ATOM   1657 C  CA   . GLY   A 1 85  ? 29.023 1.357   12.938  1.00 13.32 ?  85  GLY   A CA   1 
ATOM   1658 C  C    . GLY   A 1 85  ? 28.663 2.667   13.595  1.00 12.63 ?  85  GLY   A C    1 
ATOM   1659 O  O    . GLY   A 1 85  ? 27.474 2.980   13.723  1.00 13.17 ?  85  GLY   A O    1 
ATOM   1660 H  H    . GLY   A 1 85  ? 30.782 0.680   13.497  1.00 14.91 ?  85  GLY   A H    1 
ATOM   1661 H  HA2  . GLY   A 1 85  ? 28.641 1.346   12.047  1.00 15.99 ?  85  GLY   A HA2  1 
ATOM   1662 H  HA3  . GLY   A 1 85  ? 28.622 0.643   13.449  1.00 15.99 ?  85  GLY   A HA3  1 
ATOM   1663 N  N    . HIS   A 1 86  ? 29.654 3.442   14.027  1.00 12.43 ?  86  HIS   A N    1 
ATOM   1664 C  CA   . HIS   A 1 86  ? 29.427 4.775   14.596  1.00 12.89 ?  86  HIS   A CA   1 
ATOM   1665 C  C    . HIS   A 1 86  ? 28.451 4.648   15.758  1.00 13.60 ?  86  HIS   A C    1 
ATOM   1666 O  O    . HIS   A 1 86  ? 28.644 3.775   16.619  1.00 14.65 ?  86  HIS   A O    1 
ATOM   1667 C  CB   . HIS   A 1 86  ? 29.035 5.751   13.496  1.00 12.89 ?  86  HIS   A CB   1 
ATOM   1668 C  CG   . HIS   A 1 86  ? 30.081 5.862   12.451  1.00 12.84 ?  86  HIS   A CG   1 
ATOM   1669 N  ND1  . HIS   A 1 86  ? 31.160 6.710   12.574  1.00 13.76 ?  86  HIS   A ND1  1 
ATOM   1670 C  CD2  . HIS   A 1 86  ? 30.263 5.172   11.305  1.00 12.45 ?  86  HIS   A CD2  1 
ATOM   1671 C  CE1  . HIS   A 1 86  ? 31.951 6.548   11.529  1.00 13.27 ?  86  HIS   A CE1  1 
ATOM   1672 N  NE2  . HIS   A 1 86  ? 31.434 5.618   10.749  1.00 12.70 ?  86  HIS   A NE2  1 
ATOM   1673 H  H    . HIS   A 1 86  ? 30.483 3.219   14.008  1.00 14.92 ?  86  HIS   A H    1 
ATOM   1674 H  HA   . HIS   A 1 86  ? 30.268 5.093   14.966  1.00 15.47 ?  86  HIS   A HA   1 
ATOM   1675 H  HB2  . HIS   A 1 86  ? 28.214 5.451   13.076  1.00 15.48 ?  86  HIS   A HB2  1 
ATOM   1676 H  HB3  . HIS   A 1 86  ? 28.903 6.637   13.882  1.00 15.48 ?  86  HIS   A HB3  1 
ATOM   1677 H  HD2  . HIS   A 1 86  ? 29.706 4.505   10.961  1.00 14.94 ?  86  HIS   A HD2  1 
ATOM   1678 H  HE1  . HIS   A 1 86  ? 32.735 7.018   11.353  1.00 15.92 ?  86  HIS   A HE1  1 
ATOM   1679 H  HE2  . HIS   A 1 86  ? 31.767 5.345   9.997   1.00 15.25 ?  86  HIS   A HE2  1 
ATOM   1680 N  N    . ASN   A 1 87  ? 27.437 5.495   15.837  1.00 14.63 ?  87  ASN   A N    1 
ATOM   1681 C  CA   . ASN   A 1 87  ? 26.457 5.478   16.906  1.00 15.80 ?  87  ASN   A CA   1 
ATOM   1682 C  C    . ASN   A 1 87  ? 25.339 4.475   16.667  1.00 16.69 ?  87  ASN   A C    1 
ATOM   1683 O  O    . ASN   A 1 87  ? 24.422 4.396   17.488  1.00 19.07 ?  87  ASN   A O    1 
ATOM   1684 C  CB   . ASN   A 1 87  ? 25.858 6.881   17.070  1.00 16.60 ?  87  ASN   A CB   1 
ATOM   1685 C  CG   . ASN   A 1 87  ? 25.327 7.455   15.761  1.00 16.89 ?  87  ASN   A CG   1 
ATOM   1686 O  OD1  . ASN   A 1 87  ? 25.956 7.343   14.708  1.00 17.30 ?  87  ASN   A OD1  1 
ATOM   1687 N  ND2  . ASN   A 1 87  ? 24.165 8.080   15.828  1.00 17.75 ?  87  ASN   A ND2  1 
ATOM   1688 H  H    . ASN   A 1 87  ? 27.293 6.112   15.263  1.00 17.55 ?  87  ASN   A H    1 
ATOM   1689 H  HA   . ASN   A 1 87  ? 26.896 5.236   17.741  1.00 18.97 ?  87  ASN   A HA   1 
ATOM   1690 H  HB2  . ASN   A 1 87  ? 25.122 6.833   17.708  1.00 19.92 ?  87  ASN   A HB2  1 
ATOM   1691 H  HB3  . ASN   A 1 87  ? 26.545 7.474   17.408  1.00 19.92 ?  87  ASN   A HB3  1 
ATOM   1692 H  HD21 . ASN   A 1 87  ? 23.820 8.418   15.121  1.00 21.30 ?  87  ASN   A HD21 1 
ATOM   1693 H  HD22 . ASN   A 1 87  ? 23.752 8.144   16.584  1.00 21.30 ?  87  ASN   A HD22 1 
ATOM   1694 N  N    . LEU   A 1 88  ? 25.399 3.695   15.589  1.00 15.84 ?  88  LEU   A N    1 
ATOM   1695 C  CA   . LEU   A 1 88  ? 24.292 2.829   15.200  1.00 15.86 ?  88  LEU   A CA   1 
ATOM   1696 C  C    . LEU   A 1 88  ? 24.518 1.356   15.503  1.00 15.43 ?  88  LEU   A C    1 
ATOM   1697 O  O    . LEU   A 1 88  ? 23.546 0.620   15.690  1.00 16.57 ?  88  LEU   A O    1 
ATOM   1698 C  CB   . LEU   A 1 88  ? 24.033 2.980   13.700  1.00 16.68 ?  88  LEU   A CB   1 
ATOM   1699 C  CG   . LEU   A 1 88  ? 23.729 4.403   13.234  1.00 18.56 ?  88  LEU   A CG   1 
ATOM   1700 C  CD1  . LEU   A 1 88  ? 23.544 4.421   11.733  1.00 19.09 ?  88  LEU   A CD1  1 
ATOM   1701 C  CD2  . LEU   A 1 88  ? 22.502 4.970   13.942  1.00 20.17 ?  88  LEU   A CD2  1 
ATOM   1702 H  H    . LEU   A 1 88  ? 26.081 3.646   15.066  1.00 19.01 ?  88  LEU   A H    1 
ATOM   1703 H  HA   . LEU   A 1 88  ? 23.495 3.109   15.674  1.00 19.04 ?  88  LEU   A HA   1 
ATOM   1704 H  HB2  . LEU   A 1 88  ? 24.816 2.680   13.217  1.00 20.02 ?  88  LEU   A HB2  1 
ATOM   1705 H  HB3  . LEU   A 1 88  ? 23.271 2.431   13.461  1.00 20.02 ?  88  LEU   A HB3  1 
ATOM   1706 H  HG   . LEU   A 1 88  ? 24.485 4.972   13.446  1.00 22.28 ?  88  LEU   A HG   1 
ATOM   1707 H  HD11 . LEU   A 1 88  ? 23.361 5.332   11.449  1.00 22.91 ?  88  LEU   A HD11 1 
ATOM   1708 H  HD12 . LEU   A 1 88  ? 24.358 4.102   11.312  1.00 22.91 ?  88  LEU   A HD12 1 
ATOM   1709 H  HD13 . LEU   A 1 88  ? 22.801 3.846   11.499  1.00 22.91 ?  88  LEU   A HD13 1 
ATOM   1710 H  HD21 . LEU   A 1 88  ? 22.264 5.816   13.530  1.00 24.21 ?  88  LEU   A HD21 1 
ATOM   1711 H  HD22 . LEU   A 1 88  ? 21.771 4.341   13.857  1.00 24.21 ?  88  LEU   A HD22 1 
ATOM   1712 H  HD23 . LEU   A 1 88  ? 22.716 5.108   14.878  1.00 24.21 ?  88  LEU   A HD23 1 
ATOM   1713 N  N    . ALA   A 1 89  ? 25.768 0.911   15.540  1.00 14.49 ?  89  ALA   A N    1 
ATOM   1714 C  CA   . ALA   A 1 89  ? 26.114 -0.501  15.624  1.00 14.59 ?  89  ALA   A CA   1 
ATOM   1715 C  C    . ALA   A 1 89  ? 27.599 -0.558  15.933  1.00 14.85 ?  89  ALA   A C    1 
ATOM   1716 O  O    . ALA   A 1 89  ? 28.304 0.444   15.816  1.00 15.20 ?  89  ALA   A O    1 
ATOM   1717 C  CB   . ALA   A 1 89  ? 25.828 -1.202  14.297  1.00 14.26 ?  89  ALA   A CB   1 
ATOM   1718 H  H    . ALA   A 1 89  ? 26.455 1.426   15.510  1.00 17.39 ?  89  ALA   A H    1 
ATOM   1719 H  HA   . ALA   A 1 89  ? 25.616 -0.932  16.337  1.00 17.52 ?  89  ALA   A HA   1 
ATOM   1720 H  HB1  . ALA   A 1 89  ? 26.086 -2.138  14.369  1.00 17.12 ?  89  ALA   A HB1  1 
ATOM   1721 H  HB2  . ALA   A 1 89  ? 24.878 -1.142  14.101  1.00 17.12 ?  89  ALA   A HB2  1 
ATOM   1722 H  HB3  . ALA   A 1 89  ? 26.339 -0.776  13.593  1.00 17.12 ?  89  ALA   A HB3  1 
ATOM   1723 N  N    . LYS   A 1 90  ? 28.086 -1.735  16.315  1.00 15.08 ?  90  LYS   A N    1 
ATOM   1724 C  CA   . LYS   A 1 90  ? 29.530 -1.880  16.453  1.00 15.76 ?  90  LYS   A CA   1 
ATOM   1725 C  C    . LYS   A 1 90  ? 30.215 -1.683  15.104  1.00 14.28 ?  90  LYS   A C    1 
ATOM   1726 O  O    . LYS   A 1 90  ? 31.144 -0.869  14.973  1.00 15.52 ?  90  LYS   A O    1 
ATOM   1727 C  CB   . LYS   A 1 90  ? 29.881 -3.239  17.059  1.00 18.35 ?  90  LYS   A CB   1 
ATOM   1728 C  CG   . LYS   A 1 90  ? 31.357 -3.369  17.405  1.00 22.36 ?  90  LYS   A CG   1 
ATOM   1729 C  CD   . LYS   A 1 90  ? 31.627 -4.629  18.210  1.00 26.49 ?  90  LYS   A CD   1 
ATOM   1730 C  CE   . LYS   A 1 90  ? 33.032 -4.640  18.791  1.00 29.05 ?  90  LYS   A CE   1 
ATOM   1731 N  NZ   . LYS   A 1 90  ? 34.073 -4.921  17.765  1.00 30.53 ?  90  LYS   A NZ   1 
ATOM   1732 H  H    . LYS   A 1 90  ? 27.622 -2.436  16.490  1.00 18.10 ?  90  LYS   A H    1 
ATOM   1733 H  HA   . LYS   A 1 90  ? 29.858 -1.193  17.055  1.00 18.91 ?  90  LYS   A HA   1 
ATOM   1734 H  HB2  . LYS   A 1 90  ? 29.368 -3.363  17.875  1.00 22.02 ?  90  LYS   A HB2  1 
ATOM   1735 H  HB3  . LYS   A 1 90  ? 29.659 -3.936  16.422  1.00 22.02 ?  90  LYS   A HB3  1 
ATOM   1736 H  HG2  . LYS   A 1 90  ? 31.876 -3.413  16.588  1.00 26.83 ?  90  LYS   A HG2  1 
ATOM   1737 H  HG3  . LYS   A 1 90  ? 31.630 -2.605  17.937  1.00 26.83 ?  90  LYS   A HG3  1 
ATOM   1738 H  HD2  . LYS   A 1 90  ? 30.994 -4.683  18.944  1.00 31.79 ?  90  LYS   A HD2  1 
ATOM   1739 H  HD3  . LYS   A 1 90  ? 31.532 -5.404  17.632  1.00 31.79 ?  90  LYS   A HD3  1 
ATOM   1740 H  HE2  . LYS   A 1 90  ? 33.220 -3.770  19.178  1.00 34.87 ?  90  LYS   A HE2  1 
ATOM   1741 H  HE3  . LYS   A 1 90  ? 33.088 -5.326  19.474  1.00 34.87 ?  90  LYS   A HE3  1 
ATOM   1742 H  HZ1  . LYS   A 1 90  ? 34.878 -4.931  18.145  1.00 36.63 ?  90  LYS   A HZ1  1 
ATOM   1743 H  HZ2  . LYS   A 1 90  ? 33.922 -5.714  17.390  1.00 36.63 ?  90  LYS   A HZ2  1 
ATOM   1744 H  HZ3  . LYS   A 1 90  ? 34.057 -4.294  17.135  1.00 36.63 ?  90  LYS   A HZ3  1 
ATOM   1745 N  N    . HIS   A 1 91  ? 29.748 -2.404  14.087  1.00 12.82 ?  91  HIS   A N    1 
ATOM   1746 C  CA   . HIS   A 1 91  ? 30.309 -2.371  12.752  1.00 12.60 ?  91  HIS   A CA   1 
ATOM   1747 C  C    . HIS   A 1 91  ? 29.207 -2.094  11.749  1.00 11.38 ?  91  HIS   A C    1 
ATOM   1748 O  O    . HIS   A 1 91  ? 28.044 -2.465  11.953  1.00 12.12 ?  91  HIS   A O    1 
ATOM   1749 C  CB   . HIS   A 1 91  ? 30.916 -3.730  12.372  1.00 15.07 ?  91  HIS   A CB   1 
ATOM   1750 C  CG   . HIS   A 1 91  ? 31.899 -4.259  13.366  1.00 19.25 ?  91  HIS   A CG   1 
ATOM   1751 N  ND1  . HIS   A 1 91  ? 33.171 -3.749  13.499  1.00 21.38 ?  91  HIS   A ND1  1 
ATOM   1752 C  CD2  . HIS   A 1 91  ? 31.802 -5.265  14.267  1.00 21.19 ?  91  HIS   A CD2  1 
ATOM   1753 C  CE1  . HIS   A 1 91  ? 33.815 -4.415  14.441  1.00 22.34 ?  91  HIS   A CE1  1 
ATOM   1754 N  NE2  . HIS   A 1 91  ? 33.005 -5.339  14.925  1.00 22.62 ?  91  HIS   A NE2  1 
ATOM   1755 H  H    . HIS   A 1 91  ? 29.087 -2.955  14.164  1.00 15.38 ?  91  HIS   A H    1 
ATOM   1756 H  HA   . HIS   A 1 91  ? 30.992 -1.690  12.688  1.00 15.13 ?  91  HIS   A HA   1 
ATOM   1757 H  HB2  . HIS   A 1 91  ? 30.201 -4.382  12.293  1.00 18.08 ?  91  HIS   A HB2  1 
ATOM   1758 H  HB3  . HIS   A 1 91  ? 31.374 -3.642  11.522  1.00 18.08 ?  91  HIS   A HB3  1 
ATOM   1759 H  HD1  . HIS   A 1 91  ? 33.498 -3.100  13.037  1.00 25.66 ?  91  HIS   A HD1  1 
ATOM   1760 H  HD2  . HIS   A 1 91  ? 31.062 -5.805  14.416  1.00 25.43 ?  91  HIS   A HD2  1 
ATOM   1761 H  HE1  . HIS   A 1 91  ? 34.691 -4.255  14.718  1.00 26.81 ?  91  HIS   A HE1  1 
ATOM   1762 N  N    . CYS   A 1 92  ? 29.598 -1.488  10.634  1.00 10.90 ?  92  CYS   A N    1 
ATOM   1763 C  CA   . CYS   A 1 92  ? 28.754 -1.415  9.451   1.00 10.80 ?  92  CYS   A CA   1 
ATOM   1764 C  C    . CYS   A 1 92  ? 29.395 -2.231  8.339   1.00 10.34 ?  92  CYS   A C    1 
ATOM   1765 O  O    . CYS   A 1 92  ? 30.551 -1.979  7.964   1.00 11.00 ?  92  CYS   A O    1 
ATOM   1766 C  CB   . CYS   A 1 92  ? 28.532 0.026   8.990   1.00 11.29 ?  92  CYS   A CB   1 
ATOM   1767 S  SG   . CYS   A 1 92  ? 27.513 0.130   7.493   1.00 10.62 ?  92  CYS   A SG   1 
ATOM   1768 H  H    . CYS   A 1 92  ? 30.365 -1.100  10.538  1.00 13.09 ?  92  CYS   A H    1 
ATOM   1769 H  HA   . CYS   A 1 92  ? 27.893 -1.803  9.653   1.00 12.96 ?  92  CYS   A HA   1 
ATOM   1770 H  HB2  . CYS   A 1 92  ? 28.081 0.517   9.694   1.00 13.56 ?  92  CYS   A HB2  1 
ATOM   1771 H  HB3  . CYS   A 1 92  ? 29.389 0.434   8.795   1.00 13.56 ?  92  CYS   A HB3  1 
ATOM   1772 H  HG   . CYS   A 1 92  ? 27.366 1.280   7.201   1.00 12.75 ?  92  CYS   A HG   1 
ATOM   1773 N  N    . LEU   A 1 93  ? 28.654 -3.220  7.841   1.00 10.31 ?  93  LEU   A N    1 
ATOM   1774 C  CA   . LEU   A 1 93  ? 29.046 -3.984  6.665   1.00 9.99  ?  93  LEU   A CA   1 
ATOM   1775 C  C    . LEU   A 1 93  ? 28.445 -3.287  5.451   1.00 9.59  ?  93  LEU   A C    1 
ATOM   1776 O  O    . LEU   A 1 93  ? 27.227 -3.341  5.234   1.00 9.58  ?  93  LEU   A O    1 
ATOM   1777 C  CB   . LEU   A 1 93  ? 28.565 -5.431  6.776   1.00 10.58 ?  93  LEU   A CB   1 
ATOM   1778 C  CG   . LEU   A 1 93  ? 28.947 -6.319  5.598   1.00 10.44 ?  93  LEU   A CG   1 
ATOM   1779 C  CD1  . LEU   A 1 93  ? 30.448 -6.560  5.569   1.00 11.51 ?  93  LEU   A CD1  1 
ATOM   1780 C  CD2  . LEU   A 1 93  ? 28.179 -7.640  5.642   1.00 11.55 ?  93  LEU   A CD2  1 
ATOM   1781 H  H    . LEU   A 1 93  ? 27.901 -3.465  8.182   1.00 12.37 ?  93  LEU   A H    1 
ATOM   1782 H  HA   . LEU   A 1 93  ? 30.007 -3.978  6.585   1.00 11.99 ?  93  LEU   A HA   1 
ATOM   1783 H  HB2  . LEU   A 1 93  ? 28.945 -5.821  7.581   1.00 12.70 ?  93  LEU   A HB2  1 
ATOM   1784 H  HB3  . LEU   A 1 93  ? 27.596 -5.433  6.844   1.00 12.70 ?  93  LEU   A HB3  1 
ATOM   1785 H  HG   . LEU   A 1 93  ? 28.712 -5.871  4.779   1.00 12.53 ?  93  LEU   A HG   1 
ATOM   1786 H  HD11 . LEU   A 1 93  ? 30.662 -7.186  4.861   1.00 13.81 ?  93  LEU   A HD11 1 
ATOM   1787 H  HD12 . LEU   A 1 93  ? 30.908 -5.718  5.415   1.00 13.81 ?  93  LEU   A HD12 1 
ATOM   1788 H  HD13 . LEU   A 1 93  ? 30.733 -6.930  6.427   1.00 13.81 ?  93  LEU   A HD13 1 
ATOM   1789 H  HD21 . LEU   A 1 93  ? 28.448 -8.187  4.883   1.00 13.86 ?  93  LEU   A HD21 1 
ATOM   1790 H  HD22 . LEU   A 1 93  ? 28.384 -8.106  6.468   1.00 13.86 ?  93  LEU   A HD22 1 
ATOM   1791 H  HD23 . LEU   A 1 93  ? 27.229 -7.456  5.592   1.00 13.86 ?  93  LEU   A HD23 1 
ATOM   1792 N  N    . HIS   A 1 94  ? 29.293 -2.593  4.690   1.00 9.54  ?  94  HIS   A N    1 
ATOM   1793 C  CA   . HIS   A 1 94  ? 28.864 -1.920  3.470   1.00 9.36  ?  94  HIS   A CA   1 
ATOM   1794 C  C    . HIS   A 1 94  ? 28.865 -2.944  2.354   1.00 9.59  ?  94  HIS   A C    1 
ATOM   1795 O  O    . HIS   A 1 94  ? 29.926 -3.452  1.989   1.00 10.91 ?  94  HIS   A O    1 
ATOM   1796 C  CB   . HIS   A 1 94  ? 29.816 -0.775  3.133   1.00 9.88  ?  94  HIS   A CB   1 
ATOM   1797 C  CG   . HIS   A 1 94  ? 29.807 0.318   4.144   1.00 9.56  ?  94  HIS   A CG   1 
ATOM   1798 N  ND1  . HIS   A 1 94  ? 28.931 1.383   4.089   1.00 9.58  ?  94  HIS   A ND1  1 
ATOM   1799 C  CD2  . HIS   A 1 94  ? 30.547 0.483   5.262   1.00 10.04 ?  94  HIS   A CD2  1 
ATOM   1800 C  CE1  . HIS   A 1 94  ? 29.149 2.161   5.133   1.00 10.02 ?  94  HIS   A CE1  1 
ATOM   1801 N  NE2  . HIS   A 1 94  ? 30.126 1.641   5.857   1.00 10.27 ?  94  HIS   A NE2  1 
ATOM   1802 H  H    . HIS   A 1 94  ? 30.132 -2.496  4.864   1.00 11.45 ?  94  HIS   A H    1 
ATOM   1803 H  HA   . HIS   A 1 94  ? 27.962 -1.574  3.580   1.00 11.24 ?  94  HIS   A HA   1 
ATOM   1804 H  HB2  . HIS   A 1 94  ? 30.712 -1.123  3.076   1.00 11.85 ?  94  HIS   A HB2  1 
ATOM   1805 H  HB3  . HIS   A 1 94  ? 29.546 -0.393  2.281   1.00 11.85 ?  94  HIS   A HB3  1 
ATOM   1806 H  HD2  . HIS   A 1 94  ? 31.218 -0.079  5.569   1.00 12.05 ?  94  HIS   A HD2  1 
ATOM   1807 H  HE1  . HIS   A 1 94  ? 28.690 2.949   5.326   1.00 12.03 ?  94  HIS   A HE1  1 
ATOM   1808 H  HE2  . HIS   A 1 94  ? 30.440 1.980   6.584   1.00 12.32 ?  94  HIS   A HE2  1 
ATOM   1809 N  N    . VAL   A 1 95  ? 27.693 -3.267  1.818   1.00 8.75  ?  95  VAL   A N    1 
ATOM   1810 C  CA   . VAL   A 1 95  ? 27.557 -4.302  0.797   1.00 9.17  ?  95  VAL   A CA   1 
ATOM   1811 C  C    . VAL   A 1 95  ? 26.998 -3.669  -0.464  1.00 9.34  ?  95  VAL   A C    1 
ATOM   1812 O  O    . VAL   A 1 95  ? 25.992 -2.953  -0.405  1.00 9.75  ?  95  VAL   A O    1 
ATOM   1813 C  CB   . VAL   A 1 95  ? 26.641 -5.456  1.246   1.00 10.09 ?  95  VAL   A CB   1 
ATOM   1814 C  CG1  . VAL   A 1 95  ? 26.558 -6.498  0.147   1.00 10.89 ?  95  VAL   A CG1  1 
ATOM   1815 C  CG2  . VAL   A 1 95  ? 27.145 -6.073  2.533   1.00 10.35 ?  95  VAL   A CG2  1 
ATOM   1816 H  H    . VAL   A 1 95  ? 26.944 -2.895  2.031   1.00 10.50 ?  95  VAL   A H    1 
ATOM   1817 H  HA   . VAL   A 1 95  ? 28.428 -4.670  0.590   1.00 11.01 ?  95  VAL   A HA   1 
ATOM   1818 H  HB   . VAL   A 1 95  ? 25.751 -5.116  1.405   1.00 12.11 ?  95  VAL   A HB   1 
ATOM   1819 H  HG11 . VAL   A 1 95  ? 26.182 -7.317  0.511   1.00 13.07 ?  95  VAL   A HG11 1 
ATOM   1820 H  HG12 . VAL   A 1 95  ? 25.993 -6.168  -0.569  1.00 13.07 ?  95  VAL   A HG12 1 
ATOM   1821 H  HG13 . VAL   A 1 95  ? 27.452 -6.676  -0.194  1.00 13.07 ?  95  VAL   A HG13 1 
ATOM   1822 H  HG21 . VAL   A 1 95  ? 26.591 -6.839  2.752   1.00 12.42 ?  95  VAL   A HG21 1 
ATOM   1823 H  HG22 . VAL   A 1 95  ? 28.065 -6.353  2.411   1.00 12.42 ?  95  VAL   A HG22 1 
ATOM   1824 H  HG23 . VAL   A 1 95  ? 27.089 -5.411  3.239   1.00 12.42 ?  95  VAL   A HG23 1 
ATOM   1825 N  N    . VAL   A 1 96  ? 27.623 -3.952  -1.603  1.00 9.07  ?  96  VAL   A N    1 
ATOM   1826 C  CA   . VAL   A 1 96  ? 27.206 -3.394  -2.883  1.00 9.78  ?  96  VAL   A CA   1 
ATOM   1827 C  C    . VAL   A 1 96  ? 26.398 -4.447  -3.631  1.00 10.55 ?  96  VAL   A C    1 
ATOM   1828 O  O    . VAL   A 1 96  ? 26.956 -5.388  -4.202  1.00 11.04 ?  96  VAL   A O    1 
ATOM   1829 C  CB   . VAL   A 1 96  ? 28.391 -2.920  -3.722  1.00 10.52 ?  96  VAL   A CB   1 
ATOM   1830 C  CG1  . VAL   A 1 96  ? 27.882 -2.285  -5.002  1.00 10.60 ?  96  VAL   A CG1  1 
ATOM   1831 C  CG2  . VAL   A 1 96  ? 29.254 -1.944  -2.937  1.00 11.07 ?  96  VAL   A CG2  1 
ATOM   1832 H  H    . VAL   A 1 96  ? 28.313 -4.470  -1.663  1.00 10.89 ?  96  VAL   A H    1 
ATOM   1833 H  HA   . VAL   A 1 96  ? 26.633 -2.632  -2.727  1.00 11.74 ?  96  VAL   A HA   1 
ATOM   1834 H  HB   . VAL   A 1 96  ? 28.941 -3.681  -3.966  1.00 12.63 ?  96  VAL   A HB   1 
ATOM   1835 H  HG11 . VAL   A 1 96  ? 28.619 -1.821  -5.435  1.00 12.72 ?  96  VAL   A HG11 1 
ATOM   1836 H  HG12 . VAL   A 1 96  ? 27.540 -2.975  -5.587  1.00 12.72 ?  96  VAL   A HG12 1 
ATOM   1837 H  HG13 . VAL   A 1 96  ? 27.182 -1.652  -4.781  1.00 12.72 ?  96  VAL   A HG13 1 
ATOM   1838 H  HG21 . VAL   A 1 96  ? 29.954 -1.599  -3.511  1.00 13.29 ?  96  VAL   A HG21 1 
ATOM   1839 H  HG22 . VAL   A 1 96  ? 28.697 -1.212  -2.620  1.00 13.29 ?  96  VAL   A HG22 1 
ATOM   1840 H  HG23 . VAL   A 1 96  ? 29.646 -2.407  -2.179  1.00 13.29 ?  96  VAL   A HG23 1 
ATOM   1841 N  N    . GLY   A 1 97  ? 25.080 -4.287  -3.650  1.00 10.21 ?  97  GLY   A N    1 
ATOM   1842 C  CA   . GLY   A 1 97  ? 24.254 -5.051  -4.549  1.00 10.88 ?  97  GLY   A CA   1 
ATOM   1843 C  C    . GLY   A 1 97  ? 24.246 -4.406  -5.921  1.00 10.59 ?  97  GLY   A C    1 
ATOM   1844 O  O    . GLY   A 1 97  ? 24.525 -3.211  -6.067  1.00 11.45 ?  97  GLY   A O    1 
ATOM   1845 H  H    . GLY   A 1 97  ? 24.640 -3.737  -3.145  1.00 12.25 ?  97  GLY   A H    1 
ATOM   1846 H  HA2  . GLY   A 1 97  ? 24.605 -5.953  -4.607  1.00 13.06 ?  97  GLY   A HA2  1 
ATOM   1847 H  HA3  . GLY   A 1 97  ? 23.342 -5.091  -4.213  1.00 13.06 ?  97  GLY   A HA3  1 
ATOM   1848 N  N    A PRO   A 1 98  ? 23.892 -5.159  -6.957  0.72 10.64 ?  98  PRO   A N    1 
ATOM   1849 N  N    B PRO   A 1 98  ? 23.964 -5.200  -6.952  0.28 11.33 ?  98  PRO   A N    1 
ATOM   1850 C  CA   A PRO   A 1 98  ? 23.768 -4.550  -8.285  0.72 11.65 ?  98  PRO   A CA   1 
ATOM   1851 C  CA   B PRO   A 1 98  ? 23.909 -4.656  -8.311  0.28 12.08 ?  98  PRO   A CA   1 
ATOM   1852 C  C    A PRO   A 1 98  ? 22.667 -3.497  -8.307  0.72 11.55 ?  98  PRO   A C    1 
ATOM   1853 C  C    B PRO   A 1 98  ? 22.755 -3.680  -8.468  0.28 12.66 ?  98  PRO   A C    1 
ATOM   1854 O  O    A PRO   A 1 98  ? 21.600 -3.665  -7.708  0.72 11.75 ?  98  PRO   A O    1 
ATOM   1855 O  O    B PRO   A 1 98  ? 21.680 -3.853  -7.889  0.28 12.98 ?  98  PRO   A O    1 
ATOM   1856 C  CB   A PRO   A 1 98  ? 23.430 -5.742  -9.189  0.72 12.01 ?  98  PRO   A CB   1 
ATOM   1857 C  CB   B PRO   A 1 98  ? 23.705 -5.903  -9.182  0.28 11.97 ?  98  PRO   A CB   1 
ATOM   1858 C  CG   A PRO   A 1 98  ? 22.804 -6.750  -8.272  0.72 11.78 ?  98  PRO   A CG   1 
ATOM   1859 C  CG   B PRO   A 1 98  ? 23.096 -6.915  -8.260  0.28 12.20 ?  98  PRO   A CG   1 
ATOM   1860 C  CD   A PRO   A 1 98  ? 23.558 -6.595  -6.974  0.72 11.01 ?  98  PRO   A CD   1 
ATOM   1861 C  CD   B PRO   A 1 98  ? 23.747 -6.658  -6.934  0.28 11.66 ?  98  PRO   A CD   1 
ATOM   1862 H  HA   A PRO   A 1 98  ? 24.611 -4.159  -8.559  0.72 13.98 ?  98  PRO   A HA   1 
ATOM   1863 H  HA   B PRO   A 1 98  ? 24.746 -4.225  -8.542  0.28 14.50 ?  98  PRO   A HA   1 
ATOM   1864 H  HB2  A PRO   A 1 98  ? 22.799 -5.464  -9.872  0.72 14.41 ?  98  PRO   A HB2  1 
ATOM   1865 H  HB2  B PRO   A 1 98  ? 23.101 -5.696  -9.912  0.28 14.37 ?  98  PRO   A HB2  1 
ATOM   1866 H  HB3  A PRO   A 1 98  ? 24.239 -6.095  -9.587  0.72 14.41 ?  98  PRO   A HB3  1 
ATOM   1867 H  HB3  B PRO   A 1 98  ? 24.559 -6.214  -9.517  0.28 14.37 ?  98  PRO   A HB3  1 
ATOM   1868 H  HG2  A PRO   A 1 98  ? 21.865 -6.546  -8.151  0.72 14.14 ?  98  PRO   A HG2  1 
ATOM   1869 H  HG2  B PRO   A 1 98  ? 22.137 -6.774  -8.204  0.28 14.64 ?  98  PRO   A HG2  1 
ATOM   1870 H  HG3  A PRO   A 1 98  ? 22.923 -7.641  -8.636  0.72 14.14 ?  98  PRO   A HG3  1 
ATOM   1871 H  HG3  B PRO   A 1 98  ? 23.295 -7.810  -8.575  0.28 14.64 ?  98  PRO   A HG3  1 
ATOM   1872 H  HD2  A PRO   A 1 98  ? 22.987 -6.826  -6.220  0.72 13.22 ?  98  PRO   A HD2  1 
ATOM   1873 H  HD2  B PRO   A 1 98  ? 23.154 -6.910  -6.208  0.28 13.99 ?  98  PRO   A HD2  1 
ATOM   1874 H  HD3  A PRO   A 1 98  ? 24.367 -7.134  -6.980  0.72 13.22 ?  98  PRO   A HD3  1 
ATOM   1875 H  HD3  B PRO   A 1 98  ? 24.597 -7.127  -6.876  0.28 13.99 ?  98  PRO   A HD3  1 
ATOM   1876 N  N    A ASN   A 1 99  ? 22.939 -2.396  -8.999  0.72 12.44 ?  99  ASN   A N    1 
ATOM   1877 N  N    B ASN   A 1 99  ? 22.990 -2.643  -9.261  0.28 12.99 ?  99  ASN   A N    1 
ATOM   1878 C  CA   A ASN   A 1 99  ? 21.962 -1.335  -9.213  0.72 13.41 ?  99  ASN   A CA   1 
ATOM   1879 C  CA   B ASN   A 1 99  ? 21.996 -1.611  -9.519  0.28 13.89 ?  99  ASN   A CA   1 
ATOM   1880 C  C    A ASN   A 1 99  ? 21.405 -1.500  -10.623 0.72 14.58 ?  99  ASN   A C    1 
ATOM   1881 C  C    B ASN   A 1 99  ? 21.291 -1.948  -10.827 0.28 14.79 ?  99  ASN   A C    1 
ATOM   1882 O  O    A ASN   A 1 99  ? 22.109 -1.265  -11.611 0.72 15.52 ?  99  ASN   A O    1 
ATOM   1883 O  O    B ASN   A 1 99  ? 21.903 -1.910  -11.900 0.28 14.70 ?  99  ASN   A O    1 
ATOM   1884 C  CB   A ASN   A 1 99  ? 22.611 0.035   -9.023  0.72 13.61 ?  99  ASN   A CB   1 
ATOM   1885 C  CB   B ASN   A 1 99  ? 22.668 -0.244  -9.589  0.28 14.39 ?  99  ASN   A CB   1 
ATOM   1886 C  CG   A ASN   A 1 99  ? 21.597 1.176   -8.999  0.72 14.10 ?  99  ASN   A CG   1 
ATOM   1887 C  CG   B ASN   A 1 99  ? 21.675 0.887   -9.723  0.28 14.93 ?  99  ASN   A CG   1 
ATOM   1888 O  OD1  A ASN   A 1 99  ? 20.572 1.126   -9.676  0.72 14.88 ?  99  ASN   A OD1  1 
ATOM   1889 O  OD1  B ASN   A 1 99  ? 20.680 0.769   -10.434 0.28 14.92 ?  99  ASN   A OD1  1 
ATOM   1890 N  ND2  A ASN   A 1 99  ? 21.891 2.214   -8.223  0.72 14.67 ?  99  ASN   A ND2  1 
ATOM   1891 N  ND2  B ASN   A 1 99  ? 21.938 1.990   -9.027  0.28 15.49 ?  99  ASN   A ND2  1 
ATOM   1892 H  H    A ASN   A 1 99  ? 23.706 -2.235  -9.349  0.72 14.93 ?  99  ASN   A H    1 
ATOM   1893 H  H    B ASN   A 1 99  ? 23.741 -2.511  -9.660  0.28 15.59 ?  99  ASN   A H    1 
ATOM   1894 H  HA   A ASN   A 1 99  ? 21.237 -1.427  -8.570  0.72 16.10 ?  99  ASN   A HA   1 
ATOM   1895 H  HA   B ASN   A 1 99  ? 21.341 -1.607  -8.800  0.28 16.68 ?  99  ASN   A HA   1 
ATOM   1896 H  HB2  A ASN   A 1 99  ? 23.095 0.045   -8.183  0.72 16.34 ?  99  ASN   A HB2  1 
ATOM   1897 H  HB2  B ASN   A 1 99  ? 23.180 -0.106  -8.778  0.28 17.27 ?  99  ASN   A HB2  1 
ATOM   1898 H  HB3  A ASN   A 1 99  ? 23.228 0.191   -9.760  0.72 16.34 ?  99  ASN   A HB3  1 
ATOM   1899 H  HB3  B ASN   A 1 99  ? 23.250 -0.223  -10.359 0.28 17.27 ?  99  ASN   A HB3  1 
ATOM   1900 H  HD21 A ASN   A 1 99  ? 21.353 2.883   -8.183  0.72 17.61 ?  99  ASN   A HD21 1 
ATOM   1901 H  HD21 B ASN   A 1 99  ? 21.403 2.661   -9.059  0.28 18.59 ?  99  ASN   A HD21 1 
ATOM   1902 H  HD22 A ASN   A 1 99  ? 22.618 2.216   -7.767  0.72 17.61 ?  99  ASN   A HD22 1 
ATOM   1903 H  HD22 B ASN   A 1 99  ? 22.648 2.030   -8.538  0.28 18.59 ?  99  ASN   A HD22 1 
ATOM   1904 N  N    A VAL   A 1 100 ? 20.143 -1.927  -10.708 0.72 15.50 ?  100 VAL   A N    1 
ATOM   1905 N  N    B VAL   A 1 100 ? 20.000 -2.272  -10.732 0.28 16.26 ?  100 VAL   A N    1 
ATOM   1906 C  CA   A VAL   A 1 100 ? 19.506 -2.143  -12.003 0.72 17.10 ?  100 VAL   A CA   1 
ATOM   1907 C  CA   B VAL   A 1 100 ? 19.244 -2.682  -11.910 0.28 17.59 ?  100 VAL   A CA   1 
ATOM   1908 C  C    A VAL   A 1 100 ? 19.429 -0.842  -12.784 0.72 18.09 ?  100 VAL   A C    1 
ATOM   1909 C  C    B VAL   A 1 100 ? 19.093 -1.519  -12.880 0.28 18.09 ?  100 VAL   A C    1 
ATOM   1910 O  O    A VAL   A 1 100 ? 19.498 -0.845  -14.018 0.72 19.15 ?  100 VAL   A O    1 
ATOM   1911 O  O    B VAL   A 1 100 ? 19.099 -1.707  -14.103 0.28 17.94 ?  100 VAL   A O    1 
ATOM   1912 C  CB   A VAL   A 1 100 ? 18.125 -2.800  -11.804 0.72 18.96 ?  100 VAL   A CB   1 
ATOM   1913 C  CB   B VAL   A 1 100 ? 17.883 -3.266  -11.490 0.28 18.52 ?  100 VAL   A CB   1 
ATOM   1914 C  CG1  A VAL   A 1 100 ? 17.391 -2.941  -13.129 0.72 19.71 ?  100 VAL   A CG1  1 
ATOM   1915 C  CG1  B VAL   A 1 100 ? 17.151 -3.824  -12.700 0.28 18.70 ?  100 VAL   A CG1  1 
ATOM   1916 C  CG2  A VAL   A 1 100 ? 18.287 -4.155  -11.140 0.72 19.46 ?  100 VAL   A CG2  1 
ATOM   1917 C  CG2  B VAL   A 1 100 ? 18.080 -4.340  -10.432 0.28 19.07 ?  100 VAL   A CG2  1 
ATOM   1918 H  H    A VAL   A 1 100 ? 19.638 -2.105  -10.028 0.72 18.60 ?  100 VAL   A H    1 
ATOM   1919 H  H    B VAL   A 1 100 ? 19.544 -2.256  -10.002 0.28 19.51 ?  100 VAL   A H    1 
ATOM   1920 H  HA   A VAL   A 1 100 ? 20.049 -2.758  -12.516 0.72 20.52 ?  100 VAL   A HA   1 
ATOM   1921 H  HA   B VAL   A 1 100 ? 19.733 -3.381  -12.367 0.28 21.11 ?  100 VAL   A HA   1 
ATOM   1922 H  HB   A VAL   A 1 100 ? 17.588 -2.243  -11.222 0.72 22.75 ?  100 VAL   A HB   1 
ATOM   1923 H  HB   B VAL   A 1 100 ? 17.338 -2.561  -11.105 0.28 22.22 ?  100 VAL   A HB   1 
ATOM   1924 H  HG11 A VAL   A 1 100 ? 16.622 -3.521  -13.003 0.72 23.65 ?  100 VAL   A HG11 1 
ATOM   1925 H  HG11 B VAL   A 1 100 ? 16.386 -4.337  -12.397 0.28 22.45 ?  100 VAL   A HG11 1 
ATOM   1926 H  HG12 A VAL   A 1 100 ? 17.097 -2.066  -13.426 0.72 23.65 ?  100 VAL   A HG12 1 
ATOM   1927 H  HG12 B VAL   A 1 100 ? 16.856 -3.090  -13.260 0.28 22.45 ?  100 VAL   A HG12 1 
ATOM   1928 H  HG13 A VAL   A 1 100 ? 17.991 -3.331  -13.784 0.72 23.65 ?  100 VAL   A HG13 1 
ATOM   1929 H  HG13 B VAL   A 1 100 ? 17.756 -4.399  -13.196 0.28 22.45 ?  100 VAL   A HG13 1 
ATOM   1930 H  HG21 A VAL   A 1 100 ? 17.420 -4.584  -11.081 0.72 23.36 ?  100 VAL   A HG21 1 
ATOM   1931 H  HG21 B VAL   A 1 100 ? 17.248 -4.822  -10.313 0.28 22.88 ?  100 VAL   A HG21 1 
ATOM   1932 H  HG22 A VAL   A 1 100 ? 18.890 -4.698  -11.673 0.72 23.36 ?  100 VAL   A HG22 1 
ATOM   1933 H  HG22 B VAL   A 1 100 ? 18.776 -4.947  -10.728 0.28 22.88 ?  100 VAL   A HG22 1 
ATOM   1934 H  HG23 A VAL   A 1 100 ? 18.656 -4.029  -10.251 0.72 23.36 ?  100 VAL   A HG23 1 
ATOM   1935 H  HG23 B VAL   A 1 100 ? 18.342 -3.919  -9.597  0.28 22.88 ?  100 VAL   A HG23 1 
ATOM   1936 N  N    A ASN   A 1 101 ? 19.293 0.287   -12.092 0.72 18.89 ?  101 ASN   A N    1 
ATOM   1937 N  N    B ASN   A 1 101 ? 18.954 -0.299  -12.354 0.28 18.77 ?  101 ASN   A N    1 
ATOM   1938 C  CA   A ASN   A 1 101 ? 19.251 1.573   -12.777 0.72 20.73 ?  101 ASN   A CA   1 
ATOM   1939 C  CA   B ASN   A 1 101 ? 18.859 0.874   -13.215 0.28 19.33 ?  101 ASN   A CA   1 
ATOM   1940 C  C    A ASN   A 1 101 ? 20.612 1.993   -13.333 0.72 22.33 ?  101 ASN   A C    1 
ATOM   1941 C  C    B ASN   A 1 101 ? 20.147 1.095   -13.996 0.28 20.12 ?  101 ASN   A C    1 
ATOM   1942 O  O    A ASN   A 1 101 ? 20.693 3.032   -14.001 0.72 23.98 ?  101 ASN   A O    1 
ATOM   1943 O  O    B ASN   A 1 101 ? 20.113 1.608   -15.122 0.28 20.24 ?  101 ASN   A O    1 
ATOM   1944 C  CB   A ASN   A 1 101 ? 18.641 2.624   -11.847 0.72 21.01 ?  101 ASN   A CB   1 
ATOM   1945 C  CB   B ASN   A 1 101 ? 18.537 2.109   -12.372 0.28 18.98 ?  101 ASN   A CB   1 
ATOM   1946 C  CG   A ASN   A 1 101 ? 17.255 2.220   -11.358 0.72 21.13 ?  101 ASN   A CG   1 
ATOM   1947 C  CG   B ASN   A 1 101 ? 17.382 1.878   -11.414 0.28 18.49 ?  101 ASN   A CG   1 
ATOM   1948 O  OD1  A ASN   A 1 101 ? 16.422 1.757   -12.141 0.72 21.80 ?  101 ASN   A OD1  1 
ATOM   1949 O  OD1  B ASN   A 1 101 ? 16.335 1.351   -11.795 0.28 18.38 ?  101 ASN   A OD1  1 
ATOM   1950 N  ND2  A ASN   A 1 101 ? 17.010 2.372   -10.060 0.72 20.55 ?  101 ASN   A ND2  1 
ATOM   1951 N  ND2  B ASN   A 1 101 ? 17.575 2.260   -10.156 0.28 18.11 ?  101 ASN   A ND2  1 
ATOM   1952 H  H    A ASN   A 1 101 ? 19.211 0.332   -11.238 0.72 22.67 ?  101 ASN   A H    1 
ATOM   1953 H  H    B ASN   A 1 101 ? 18.914 -0.129  -11.512 0.28 22.53 ?  101 ASN   A H    1 
ATOM   1954 H  HA   A ASN   A 1 101 ? 18.656 1.489   -13.534 0.72 24.88 ?  101 ASN   A HA   1 
ATOM   1955 H  HA   B ASN   A 1 101 ? 18.137 0.750   -13.850 0.28 23.20 ?  101 ASN   A HA   1 
ATOM   1956 H  HB2  A ASN   A 1 101 ? 19.211 2.742   -11.074 0.72 25.21 ?  101 ASN   A HB2  1 
ATOM   1957 H  HB2  B ASN   A 1 101 ? 19.318 2.351   -11.849 0.28 22.78 ?  101 ASN   A HB2  1 
ATOM   1958 H  HB3  A ASN   A 1 101 ? 18.552 3.462   -12.330 0.72 25.21 ?  101 ASN   A HB3  1 
ATOM   1959 H  HB3  B ASN   A 1 101 ? 18.295 2.843   -12.961 0.28 22.78 ?  101 ASN   A HB3  1 
ATOM   1960 H  HD21 A ASN   A 1 101 ? 16.241 2.151   -9.738  0.72 24.67 ?  101 ASN   A HD21 1 
ATOM   1961 H  HD21 B ASN   A 1 101 ? 16.953 2.151   -9.574  0.28 21.73 ?  101 ASN   A HD21 1 
ATOM   1962 H  HD22 A ASN   A 1 101 ? 17.612 2.700   -9.543  0.72 24.67 ?  101 ASN   A HD22 1 
ATOM   1963 H  HD22 B ASN   A 1 101 ? 18.322 2.620   -9.924  0.28 21.73 ?  101 ASN   A HD22 1 
ATOM   1964 N  N    A LYS   A 1 102 ? 21.663 1.201   -13.092 0.72 23.49 ?  102 LYS   A N    1 
ATOM   1965 N  N    B LYS   A 1 102 ? 21.289 0.730   -13.413 0.28 21.41 ?  102 LYS   A N    1 
ATOM   1966 C  CA   A LYS   A 1 102 ? 22.953 1.359   -13.753 0.72 24.31 ?  102 LYS   A CA   1 
ATOM   1967 C  CA   B LYS   A 1 102 ? 22.573 0.805   -14.097 0.28 22.23 ?  102 LYS   A CA   1 
ATOM   1968 C  C    A LYS   A 1 102 ? 23.244 0.237   -14.742 0.72 24.47 ?  102 LYS   A C    1 
ATOM   1969 C  C    B LYS   A 1 102 ? 22.804 -0.366  -15.042 0.28 21.57 ?  102 LYS   A C    1 
ATOM   1970 O  O    A LYS   A 1 102 ? 24.326 0.223   -15.337 0.72 25.25 ?  102 LYS   A O    1 
ATOM   1971 O  O    B LYS   A 1 102 ? 23.881 -0.454  -15.642 0.28 21.22 ?  102 LYS   A O    1 
ATOM   1972 C  CB   A LYS   A 1 102 ? 24.085 1.420   -12.718 0.72 25.42 ?  102 LYS   A CB   1 
ATOM   1973 C  CB   B LYS   A 1 102 ? 23.715 0.845   -13.076 0.28 23.65 ?  102 LYS   A CB   1 
ATOM   1974 C  CG   A LYS   A 1 102 ? 23.980 2.569   -11.732 0.72 26.51 ?  102 LYS   A CG   1 
ATOM   1975 C  CG   B LYS   A 1 102 ? 23.812 2.128   -12.264 0.28 24.81 ?  102 LYS   A CG   1 
ATOM   1976 C  CD   A LYS   A 1 102 ? 25.116 2.527   -10.717 0.72 27.78 ?  102 LYS   A CD   1 
ATOM   1977 C  CD   B LYS   A 1 102 ? 25.008 2.079   -11.322 0.28 25.85 ?  102 LYS   A CD   1 
ATOM   1978 C  CE   A LYS   A 1 102 ? 25.033 3.689   -9.740  0.72 28.71 ?  102 LYS   A CE   1 
ATOM   1979 C  CE   B LYS   A 1 102 ? 25.230 3.407   -10.618 0.28 26.62 ?  102 LYS   A CE   1 
ATOM   1980 N  NZ   A LYS   A 1 102 ? 26.085 3.607   -8.685  0.72 29.27 ?  102 LYS   A NZ   1 
ATOM   1981 N  NZ   B LYS   A 1 102 ? 26.473 3.392   -9.796  0.28 27.12 ?  102 LYS   A NZ   1 
ATOM   1982 H  H    A LYS   A 1 102 ? 21.649 0.542   -12.538 0.72 28.19 ?  102 LYS   A H    1 
ATOM   1983 H  H    B LYS   A 1 102 ? 21.340 0.432   -12.608 0.28 25.70 ?  102 LYS   A H    1 
ATOM   1984 H  HA   A LYS   A 1 102 ? 22.954 2.192   -14.244 0.72 29.17 ?  102 LYS   A HA   1 
ATOM   1985 H  HA   B LYS   A 1 102 ? 22.605 1.628   -14.609 0.28 26.68 ?  102 LYS   A HA   1 
ATOM   1986 H  HB2  A LYS   A 1 102 ? 24.085 0.595   -12.209 0.72 30.51 ?  102 LYS   A HB2  1 
ATOM   1987 H  HB2  B LYS   A 1 102 ? 23.599 0.111   -12.454 0.28 28.39 ?  102 LYS   A HB2  1 
ATOM   1988 H  HB3  A LYS   A 1 102 ? 24.929 1.513   -13.188 0.72 30.51 ?  102 LYS   A HB3  1 
ATOM   1989 H  HB3  B LYS   A 1 102 ? 24.554 0.739   -13.548 0.28 28.39 ?  102 LYS   A HB3  1 
ATOM   1990 H  HG2  A LYS   A 1 102 ? 24.030 3.410   -12.213 0.72 31.81 ?  102 LYS   A HG2  1 
ATOM   1991 H  HG2  B LYS   A 1 102 ? 23.928 2.882   -12.864 0.28 29.78 ?  102 LYS   A HG2  1 
ATOM   1992 H  HG3  A LYS   A 1 102 ? 23.139 2.505   -11.253 0.72 31.81 ?  102 LYS   A HG3  1 
ATOM   1993 H  HG3  B LYS   A 1 102 ? 23.008 2.239   -11.733 0.28 29.78 ?  102 LYS   A HG3  1 
ATOM   1994 H  HD2  A LYS   A 1 102 ? 25.063 1.700   -10.212 0.72 33.34 ?  102 LYS   A HD2  1 
ATOM   1995 H  HD2  B LYS   A 1 102 ? 24.854 1.400   -10.645 0.28 31.02 ?  102 LYS   A HD2  1 
ATOM   1996 H  HD3  A LYS   A 1 102 ? 25.965 2.581   -11.185 0.72 33.34 ?  102 LYS   A HD3  1 
ATOM   1997 H  HD3  B LYS   A 1 102 ? 25.807 1.868   -11.830 0.28 31.02 ?  102 LYS   A HD3  1 
ATOM   1998 H  HE2  A LYS   A 1 102 ? 25.153 4.522   -10.225 0.72 34.45 ?  102 LYS   A HE2  1 
ATOM   1999 H  HE2  B LYS   A 1 102 ? 25.312 4.110   -11.281 0.28 31.94 ?  102 LYS   A HE2  1 
ATOM   2000 H  HE3  A LYS   A 1 102 ? 24.165 3.679   -9.306  0.72 34.45 ?  102 LYS   A HE3  1 
ATOM   2001 H  HE3  B LYS   A 1 102 ? 24.479 3.587   -10.030 0.28 31.94 ?  102 LYS   A HE3  1 
ATOM   2002 H  HZ1  A LYS   A 1 102 ? 26.012 4.298   -8.130  0.72 35.12 ?  102 LYS   A HZ1  1 
ATOM   2003 H  HZ1  B LYS   A 1 102 ? 26.582 4.178   -9.394  0.28 32.54 ?  102 LYS   A HZ1  1 
ATOM   2004 H  HZ2  A LYS   A 1 102 ? 25.992 2.852   -8.223  0.72 35.12 ?  102 LYS   A HZ2  1 
ATOM   2005 H  HZ2  B LYS   A 1 102 ? 26.420 2.755   -9.176  0.28 32.54 ?  102 LYS   A HZ2  1 
ATOM   2006 H  HZ3  A LYS   A 1 102 ? 26.891 3.620   -9.060  0.72 35.12 ?  102 LYS   A HZ3  1 
ATOM   2007 H  HZ3  B LYS   A 1 102 ? 27.178 3.231   -10.315 0.28 32.54 ?  102 LYS   A HZ3  1 
ATOM   2008 N  N    A GLY   A 1 103 ? 22.323 -0.708  -14.922 0.72 24.30 ?  103 GLY   A N    1 
ATOM   2009 N  N    B GLY   A 1 103 ? 21.836 -1.269  -15.178 0.28 21.31 ?  103 GLY   A N    1 
ATOM   2010 C  CA   A GLY   A 1 103 ? 22.536 -1.808  -15.842 0.72 23.73 ?  103 GLY   A CA   1 
ATOM   2011 C  CA   B GLY   A 1 103 ? 22.011 -2.427  -16.032 0.28 20.90 ?  103 GLY   A CA   1 
ATOM   2012 C  C    A GLY   A 1 103 ? 23.372 -2.948  -15.307 0.72 23.86 ?  103 GLY   A C    1 
ATOM   2013 C  C    B GLY   A 1 103 ? 22.950 -3.477  -15.485 0.28 20.59 ?  103 GLY   A C    1 
ATOM   2014 O  O    A GLY   A 1 103 ? 23.935 -3.710  -16.099 0.72 24.91 ?  103 GLY   A O    1 
ATOM   2015 O  O    B GLY   A 1 103 ? 23.406 -4.341  -16.239 0.28 20.72 ?  103 GLY   A O    1 
ATOM   2016 H  H    A GLY   A 1 103 ? 21.568 -0.738  -14.515 0.72 29.17 ?  103 GLY   A H    1 
ATOM   2017 H  H    B GLY   A 1 103 ? 21.070 -1.226  -14.789 0.28 25.57 ?  103 GLY   A H    1 
ATOM   2018 H  HA2  A GLY   A 1 103 ? 21.673 -2.164  -16.112 0.72 28.48 ?  103 GLY   A HA2  1 
ATOM   2019 H  HA2  B GLY   A 1 103 ? 21.151 -2.848  -16.166 0.28 25.08 ?  103 GLY   A HA2  1 
ATOM   2020 H  HA3  A GLY   A 1 103 ? 22.979 -1.473  -16.637 0.72 28.48 ?  103 GLY   A HA3  1 
ATOM   2021 H  HA3  B GLY   A 1 103 ? 22.340 -2.130  -16.897 0.28 25.08 ?  103 GLY   A HA3  1 
ATOM   2022 N  N    A GLU   A 1 104 ? 23.471 -3.100  -13.991 0.72 22.05 ?  104 GLU   A N    1 
ATOM   2023 N  N    B GLU   A 1 104 ? 23.242 -3.442  -14.189 0.28 20.36 ?  104 GLU   A N    1 
ATOM   2024 C  CA   A GLU   A 1 104 ? 24.344 -4.106  -13.405 0.72 20.56 ?  104 GLU   A CA   1 
ATOM   2025 C  CA   B GLU   A 1 104 ? 24.206 -4.363  -13.608 0.28 20.08 ?  104 GLU   A CA   1 
ATOM   2026 C  C    A GLU   A 1 104 ? 23.647 -5.460  -13.294 0.72 21.50 ?  104 GLU   A C    1 
ATOM   2027 C  C    B GLU   A 1 104 ? 23.594 -5.749  -13.432 0.28 19.92 ?  104 GLU   A C    1 
ATOM   2028 O  O    A GLU   A 1 104 ? 22.428 -5.548  -13.122 0.72 22.42 ?  104 GLU   A O    1 
ATOM   2029 O  O    B GLU   A 1 104 ? 22.380 -5.903  -13.268 0.28 20.09 ?  104 GLU   A O    1 
ATOM   2030 C  CB   A GLU   A 1 104 ? 24.873 -3.621  -12.052 0.72 18.68 ?  104 GLU   A CB   1 
ATOM   2031 C  CB   B GLU   A 1 104 ? 24.723 -3.820  -12.274 0.28 20.04 ?  104 GLU   A CB   1 
ATOM   2032 C  CG   A GLU   A 1 104 ? 25.828 -2.441  -12.225 0.72 18.15 ?  104 GLU   A CG   1 
ATOM   2033 C  CG   B GLU   A 1 104 ? 25.526 -2.533  -12.430 0.28 20.45 ?  104 GLU   A CG   1 
ATOM   2034 C  CD   A GLU   A 1 104 ? 26.139 -1.661  -10.965 0.72 17.19 ?  104 GLU   A CD   1 
ATOM   2035 C  CD   B GLU   A 1 104 ? 25.875 -1.874  -11.109 0.28 20.81 ?  104 GLU   A CD   1 
ATOM   2036 O  OE1  A GLU   A 1 104 ? 25.532 -1.907  -9.905  0.72 15.32 ?  104 GLU   A OE1  1 
ATOM   2037 O  OE1  B GLU   A 1 104 ? 25.437 -2.369  -10.050 0.28 21.01 ?  104 GLU   A OE1  1 
ATOM   2038 O  OE2  A GLU   A 1 104 ? 27.007 -0.763  -11.066 0.72 18.07 -1 104 GLU   A OE2  1 
ATOM   2039 O  OE2  B GLU   A 1 104 ? 26.582 -0.845  -11.134 0.28 21.12 -1 104 GLU   A OE2  1 
ATOM   2040 H  H    A GLU   A 1 104 ? 23.046 -2.621  -13.414 0.72 26.46 ?  104 GLU   A H    1 
ATOM   2041 H  H    B GLU   A 1 104 ? 22.890 -2.896  -13.628 0.28 24.43 ?  104 GLU   A H    1 
ATOM   2042 H  HA   A GLU   A 1 104 ? 25.108 -4.221  -13.989 0.72 24.68 ?  104 GLU   A HA   1 
ATOM   2043 H  HA   B GLU   A 1 104 ? 24.963 -4.446  -14.208 0.28 24.09 ?  104 GLU   A HA   1 
ATOM   2044 H  HB2  A GLU   A 1 104 ? 24.131 -3.336  -11.499 0.72 22.42 ?  104 GLU   A HB2  1 
ATOM   2045 H  HB2  B GLU   A 1 104 ? 23.969 -3.633  -11.694 0.28 24.05 ?  104 GLU   A HB2  1 
ATOM   2046 H  HB3  A GLU   A 1 104 ? 25.358 -4.343  -11.621 0.72 22.42 ?  104 GLU   A HB3  1 
ATOM   2047 H  HB3  B GLU   A 1 104 ? 25.299 -4.486  -11.865 0.28 24.05 ?  104 GLU   A HB3  1 
ATOM   2048 H  HG2  A GLU   A 1 104 ? 26.674 -2.769  -12.565 0.72 21.78 ?  104 GLU   A HG2  1 
ATOM   2049 H  HG2  B GLU   A 1 104 ? 26.352 -2.733  -12.902 0.28 24.54 ?  104 GLU   A HG2  1 
ATOM   2050 H  HG3  A GLU   A 1 104 ? 25.443 -1.816  -12.858 0.72 21.78 ?  104 GLU   A HG3  1 
ATOM   2051 H  HG3  B GLU   A 1 104 ? 25.005 -1.894  -12.937 0.28 24.54 ?  104 GLU   A HG3  1 
ATOM   2052 N  N    A ASP   A 1 105 ? 24.451 -6.518  -13.386 0.72 22.29 ?  105 ASP   A N    1 
ATOM   2053 N  N    B ASP   A 1 105 ? 24.459 -6.762  -13.465 0.28 20.07 ?  105 ASP   A N    1 
ATOM   2054 C  CA   A ASP   A 1 105 ? 23.949 -7.880  -13.528 0.72 23.68 ?  105 ASP   A CA   1 
ATOM   2055 C  CA   B ASP   A 1 105 ? 24.051 -8.163  -13.469 0.28 20.56 ?  105 ASP   A CA   1 
ATOM   2056 C  C    A ASP   A 1 105 ? 23.277 -8.341  -12.238 0.72 21.86 ?  105 ASP   A C    1 
ATOM   2057 C  C    B ASP   A 1 105 ? 23.329 -8.528  -12.179 0.28 20.33 ?  105 ASP   A C    1 
ATOM   2058 O  O    A ASP   A 1 105 ? 23.921 -8.419  -11.189 0.72 19.72 ?  105 ASP   A O    1 
ATOM   2059 O  O    B ASP   A 1 105 ? 23.945 -8.581  -11.111 0.28 19.72 ?  105 ASP   A O    1 
ATOM   2060 C  CB   A ASP   A 1 105 ? 25.119 -8.799  -13.872 0.72 26.93 ?  105 ASP   A CB   1 
ATOM   2061 C  CB   B ASP   A 1 105 ? 25.295 -9.037  -13.642 0.28 21.44 ?  105 ASP   A CB   1 
ATOM   2062 C  CG   A ASP   A 1 105 ? 24.681 -10.219 -14.144 0.72 29.76 ?  105 ASP   A CG   1 
ATOM   2063 C  CG   B ASP   A 1 105 ? 24.977 -10.518 -13.731 0.28 22.01 ?  105 ASP   A CG   1 
ATOM   2064 O  OD1  A ASP   A 1 105 ? 23.460 -10.443 -14.268 0.72 30.41 ?  105 ASP   A OD1  1 
ATOM   2065 O  OD1  B ASP   A 1 105 ? 23.784 -10.877 -13.814 0.28 21.97 ?  105 ASP   A OD1  1 
ATOM   2066 O  OD2  A ASP   A 1 105 ? 25.557 -11.108 -14.236 0.72 31.45 -1 105 ASP   A OD2  1 
ATOM   2067 O  OD2  B ASP   A 1 105 ? 25.934 -11.325 -13.712 0.28 22.75 -1 105 ASP   A OD2  1 
ATOM   2068 H  H    A ASP   A 1 105 ? 25.309 -6.471  -13.362 0.72 26.75 ?  105 ASP   A H    1 
ATOM   2069 H  H    B ASP   A 1 105 ? 25.314 -6.655  -13.472 0.28 24.09 ?  105 ASP   A H    1 
ATOM   2070 H  HA   A ASP   A 1 105 ? 23.302 -7.922  -14.248 0.72 28.42 ?  105 ASP   A HA   1 
ATOM   2071 H  HA   B ASP   A 1 105 ? 23.447 -8.324  -14.215 0.28 24.67 ?  105 ASP   A HA   1 
ATOM   2072 H  HB2  A ASP   A 1 105 ? 25.563 -8.461  -14.670 0.72 32.32 ?  105 ASP   A HB2  1 
ATOM   2073 H  HB2  B ASP   A 1 105 ? 25.753 -8.765  -14.453 0.28 25.73 ?  105 ASP   A HB2  1 
ATOM   2074 H  HB3  A ASP   A 1 105 ? 25.747 -8.806  -13.129 0.72 32.32 ?  105 ASP   A HB3  1 
ATOM   2075 H  HB3  B ASP   A 1 105 ? 25.871 -8.909  -12.875 0.28 25.73 ?  105 ASP   A HB3  1 
ATOM   2076 N  N    A ILE   A 1 106 ? 21.986 -8.673  -12.319 0.72 21.91 ?  106 ILE   A N    1 
ATOM   2077 N  N    B ILE   A 1 106 ? 22.022 -8.791  -12.266 0.28 20.82 ?  106 ILE   A N    1 
ATOM   2078 C  CA   A ILE   A 1 106 ? 21.241 -9.076  -11.132 0.72 21.53 ?  106 ILE   A CA   1 
ATOM   2079 C  CA   B ILE   A 1 106 ? 21.258 -9.143  -11.076 0.28 21.21 ?  106 ILE   A CA   1 
ATOM   2080 C  C    A ILE   A 1 106 ? 21.793 -10.355 -10.522 0.72 20.38 ?  106 ILE   A C    1 
ATOM   2081 C  C    B ILE   A 1 106 ? 21.775 -10.427 -10.448 0.28 20.82 ?  106 ILE   A C    1 
ATOM   2082 O  O    A ILE   A 1 106 ? 21.587 -10.602 -9.330  0.72 19.56 ?  106 ILE   A O    1 
ATOM   2083 O  O    B ILE   A 1 106 ? 21.571 -10.654 -9.250  0.28 20.60 ?  106 ILE   A O    1 
ATOM   2084 C  CB   A ILE   A 1 106 ? 19.731 -9.185  -11.448 0.72 23.11 ?  106 ILE   A CB   1 
ATOM   2085 C  CB   B ILE   A 1 106 ? 19.743 -9.207  -11.384 0.28 22.18 ?  106 ILE   A CB   1 
ATOM   2086 C  CG1  A ILE   A 1 106 ? 18.909 -9.276  -10.159 0.72 23.82 ?  106 ILE   A CG1  1 
ATOM   2087 C  CG1  B ILE   A 1 106 ? 18.927 -9.207  -10.087 0.28 22.73 ?  106 ILE   A CG1  1 
ATOM   2088 C  CG2  A ILE   A 1 106 ? 19.456 -10.391 -12.330 0.72 23.62 ?  106 ILE   A CG2  1 
ATOM   2089 C  CG2  B ILE   A 1 106 ? 19.412 -10.440 -12.209 0.28 22.40 ?  106 ILE   A CG2  1 
ATOM   2090 C  CD1  A ILE   A 1 106 ? 19.013 -8.049  -9.275  0.72 24.15 ?  106 ILE   A CD1  1 
ATOM   2091 C  CD1  B ILE   A 1 106 ? 19.178 -7.999  -9.202  0.28 22.98 ?  106 ILE   A CD1  1 
ATOM   2092 H  H    A ILE   A 1 106 ? 21.528 -8.667  -13.042 0.72 26.29 ?  106 ILE   A H    1 
ATOM   2093 H  H    B ILE   A 1 106 ? 21.568 -8.766  -12.992 0.28 24.98 ?  106 ILE   A H    1 
ATOM   2094 H  HA   A ILE   A 1 106 ? 21.348 -8.387  -10.466 0.72 25.84 ?  106 ILE   A HA   1 
ATOM   2095 H  HA   B ILE   A 1 106 ? 21.392 -8.445  -10.423 0.28 25.45 ?  106 ILE   A HA   1 
ATOM   2096 H  HB   A ILE   A 1 106 ? 19.460 -8.387  -11.928 0.72 27.74 ?  106 ILE   A HB   1 
ATOM   2097 H  HB   B ILE   A 1 106 ? 19.498 -8.420  -11.897 0.28 26.62 ?  106 ILE   A HB   1 
ATOM   2098 H  HG12 A ILE   A 1 106 ? 17.974 -9.389  -10.392 0.72 28.59 ?  106 ILE   A HG12 1 
ATOM   2099 H  HG12 B ILE   A 1 106 ? 17.982 -9.215  -10.310 0.28 27.28 ?  106 ILE   A HG12 1 
ATOM   2100 H  HG13 A ILE   A 1 106 ? 19.211 -10.039 -9.643  0.72 28.59 ?  106 ILE   A HG13 1 
ATOM   2101 H  HG13 B ILE   A 1 106 ? 19.150 -10.000 -9.575  0.28 27.28 ?  106 ILE   A HG13 1 
ATOM   2102 H  HG21 A ILE   A 1 106 ? 18.556 -10.323 -12.685 0.72 28.35 ?  106 ILE   A HG21 1 
ATOM   2103 H  HG21 B ILE   A 1 106 ? 18.514 -10.349 -12.566 0.28 26.88 ?  106 ILE   A HG21 1 
ATOM   2104 H  HG22 A ILE   A 1 106 ? 20.099 -10.402 -13.055 0.72 28.35 ?  106 ILE   A HG22 1 
ATOM   2105 H  HG22 B ILE   A 1 106 ? 20.050 -10.511 -12.935 0.28 26.88 ?  106 ILE   A HG22 1 
ATOM   2106 H  HG23 A ILE   A 1 106 ? 19.542 -11.198 -11.799 0.72 28.35 ?  106 ILE   A HG23 1 
ATOM   2107 H  HG23 B ILE   A 1 106 ? 19.464 -11.225 -11.643 0.28 26.88 ?  106 ILE   A HG23 1 
ATOM   2108 H  HD11 A ILE   A 1 106 ? 18.300 -8.071  -8.620  0.72 28.98 ?  106 ILE   A HD11 1 
ATOM   2109 H  HD11 B ILE   A 1 106 ? 18.439 -7.903  -8.584  0.28 27.57 ?  106 ILE   A HD11 1 
ATOM   2110 H  HD12 A ILE   A 1 106 ? 19.874 -8.055  -8.825  0.72 28.98 ?  106 ILE   A HD12 1 
ATOM   2111 H  HD12 B ILE   A 1 106 ? 20.005 -8.134  -8.711  0.28 27.57 ?  106 ILE   A HD12 1 
ATOM   2112 H  HD13 A ILE   A 1 106 ? 18.933 -7.255  -9.826  0.72 28.98 ?  106 ILE   A HD13 1 
ATOM   2113 H  HD13 B ILE   A 1 106 ? 19.249 -7.209  -9.761  0.28 27.57 ?  106 ILE   A HD13 1 
ATOM   2114 N  N    A GLN   A 1 107 ? 22.502 -11.174 -11.310 0.72 21.08 ?  107 GLN   A N    1 
ATOM   2115 N  N    B GLN   A 1 107 ? 22.455 -11.275 -11.226 0.28 20.75 ?  107 GLN   A N    1 
ATOM   2116 C  CA   A GLN   A 1 107 ? 23.113 -12.383 -10.763 0.72 22.86 ?  107 GLN   A CA   1 
ATOM   2117 C  CA   B GLN   A 1 107 ? 23.092 -12.452 -10.649 0.28 20.88 ?  107 GLN   A CA   1 
ATOM   2118 C  C    A GLN   A 1 107 ? 24.078 -12.048 -9.633  0.72 20.48 ?  107 GLN   A C    1 
ATOM   2119 C  C    B GLN   A 1 107 ? 24.154 -12.081 -9.625  0.28 19.34 ?  107 GLN   A C    1 
ATOM   2120 O  O    A GLN   A 1 107 ? 24.276 -12.856 -8.718  0.72 21.34 ?  107 GLN   A O    1 
ATOM   2121 O  O    B GLN   A 1 107 ? 24.511 -12.917 -8.788  0.28 19.97 ?  107 GLN   A O    1 
ATOM   2122 C  CB   A GLN   A 1 107 ? 23.835 -13.154 -11.874 0.72 26.95 ?  107 GLN   A CB   1 
ATOM   2123 C  CB   B GLN   A 1 107 ? 23.693 -13.330 -11.750 0.28 22.57 ?  107 GLN   A CB   1 
ATOM   2124 C  CG   A GLN   A 1 107 ? 23.004 -13.342 -13.138 0.72 31.04 ?  107 GLN   A CG   1 
ATOM   2125 C  CG   B GLN   A 1 107 ? 22.648 -14.014 -12.615 0.28 24.16 ?  107 GLN   A CG   1 
ATOM   2126 C  CD   A GLN   A 1 107 ? 21.719 -14.106 -12.890 0.72 34.18 ?  107 GLN   A CD   1 
ATOM   2127 C  CD   B GLN   A 1 107 ? 21.595 -14.729 -11.793 0.28 25.69 ?  107 GLN   A CD   1 
ATOM   2128 O  OE1  A GLN   A 1 107 ? 21.725 -15.172 -12.275 0.72 35.36 ?  107 GLN   A OE1  1 
ATOM   2129 O  OE1  B GLN   A 1 107 ? 21.899 -15.666 -11.054 0.28 26.26 ?  107 GLN   A OE1  1 
ATOM   2130 N  NE2  A GLN   A 1 107 ? 20.605 -13.560 -13.367 0.72 35.35 ?  107 GLN   A NE2  1 
ATOM   2131 N  NE2  B GLN   A 1 107 ? 20.352 -14.273 -11.898 0.28 26.17 ?  107 GLN   A NE2  1 
ATOM   2132 H  H    A GLN   A 1 107 ? 22.648 -11.046 -12.148 0.72 25.29 ?  107 GLN   A H    1 
ATOM   2133 H  H    B GLN   A 1 107 ? 22.554 -11.192 -12.077 0.28 24.91 ?  107 GLN   A H    1 
ATOM   2134 H  HA   A GLN   A 1 107 ? 22.424 -12.958 -10.403 0.72 27.43 ?  107 GLN   A HA   1 
ATOM   2135 H  HA   B GLN   A 1 107 ? 22.419 -12.967 -10.184 0.28 25.06 ?  107 GLN   A HA   1 
ATOM   2136 H  HB2  A GLN   A 1 107 ? 24.643 -12.677 -12.123 0.72 32.34 ?  107 GLN   A HB2  1 
ATOM   2137 H  HB2  B GLN   A 1 107 ? 24.243 -12.779 -12.331 0.28 27.09 ?  107 GLN   A HB2  1 
ATOM   2138 H  HB3  A GLN   A 1 107 ? 24.068 -14.040 -11.549 0.72 32.34 ?  107 GLN   A HB3  1 
ATOM   2139 H  HB3  B GLN   A 1 107 ? 24.238 -14.021 -11.342 0.28 27.09 ?  107 GLN   A HB3  1 
ATOM   2140 H  HG2  A GLN   A 1 107 ? 22.770 -12.474 -13.501 0.72 37.25 ?  107 GLN   A HG2  1 
ATOM   2141 H  HG2  B GLN   A 1 107 ? 22.204 -13.347 -13.160 0.28 28.99 ?  107 GLN   A HG2  1 
ATOM   2142 H  HG3  A GLN   A 1 107 ? 23.527 -13.836 -13.785 0.72 37.25 ?  107 GLN   A HG3  1 
ATOM   2143 H  HG3  B GLN   A 1 107 ? 23.083 -14.673 -13.177 0.28 28.99 ?  107 GLN   A HG3  1 
ATOM   2144 H  HE21 A GLN   A 1 107 ? 20.638 -12.813 -13.791 0.72 42.42 ?  107 GLN   A HE21 1 
ATOM   2145 H  HE21 B GLN   A 1 107 ? 20.179 -13.613 -12.422 0.28 31.41 ?  107 GLN   A HE21 1 
ATOM   2146 H  HE22 A GLN   A 1 107 ? 19.850 -13.957 -13.252 0.72 42.42 ?  107 GLN   A HE22 1 
ATOM   2147 H  HE22 B GLN   A 1 107 ? 19.720 -14.638 -11.444 0.28 31.41 ?  107 GLN   A HE22 1 
ATOM   2148 N  N    . LEU   A 1 108 ? 24.662 -10.848 -9.661  1.00 17.27 ?  108 LEU   A N    1 
ATOM   2149 C  CA   . LEU   A 1 108 ? 25.585 -10.415 -8.625  1.00 14.85 ?  108 LEU   A CA   1 
ATOM   2150 C  C    . LEU   A 1 108 ? 24.897 -10.230 -7.284  1.00 12.95 ?  108 LEU   A C    1 
ATOM   2151 O  O    . LEU   A 1 108 ? 25.588 -10.083 -6.275  1.00 13.68 ?  108 LEU   A O    1 
ATOM   2152 C  CB   . LEU   A 1 108 ? 26.304 -9.128  -9.044  1.00 14.76 ?  108 LEU   A CB   1 
ATOM   2153 C  CG   . LEU   A 1 108 ? 27.289 -9.329  -10.198 1.00 16.31 ?  108 LEU   A CG   1 
ATOM   2154 C  CD1  . LEU   A 1 108 ? 27.769 -7.995  -10.753 1.00 17.40 ?  108 LEU   A CD1  1 
ATOM   2155 C  CD2  . LEU   A 1 108 ? 28.480 -10.173 -9.753  1.00 18.02 ?  108 LEU   A CD2  1 
ATOM   2156 H  H    A LEU   A 1 108 ? 24.538 -10.268 -10.280 0.72 20.73 ?  108 LEU   A H    1 
ATOM   2157 H  H    B LEU   A 1 108 ? 24.501 -10.265 -10.268 0.28 20.73 ?  108 LEU   A H    1 
ATOM   2158 H  HA   . LEU   A 1 108 ? 26.260 -11.101 -8.504  1.00 17.82 ?  108 LEU   A HA   1 
ATOM   2159 H  HB2  . LEU   A 1 108 ? 25.647 -8.476  -9.327  1.00 17.71 ?  108 LEU   A HB2  1 
ATOM   2160 H  HB3  . LEU   A 1 108 ? 26.805 -8.785  -8.288  1.00 17.71 ?  108 LEU   A HB3  1 
ATOM   2161 H  HG   . LEU   A 1 108 ? 26.842 -9.804  -10.917 1.00 19.58 ?  108 LEU   A HG   1 
ATOM   2162 H  HD11 . LEU   A 1 108 ? 28.355 -8.158  -11.511 1.00 20.88 ?  108 LEU   A HD11 1 
ATOM   2163 H  HD12 . LEU   A 1 108 ? 27.002 -7.475  -11.036 1.00 20.88 ?  108 LEU   A HD12 1 
ATOM   2164 H  HD13 . LEU   A 1 108 ? 28.254 -7.520  -10.059 1.00 20.88 ?  108 LEU   A HD13 1 
ATOM   2165 H  HD21 . LEU   A 1 108 ? 29.168 -10.130 -10.433 1.00 21.63 ?  108 LEU   A HD21 1 
ATOM   2166 H  HD22 . LEU   A 1 108 ? 28.817 -9.819  -8.916  1.00 21.63 ?  108 LEU   A HD22 1 
ATOM   2167 H  HD23 . LEU   A 1 108 ? 28.188 -11.090 -9.632  1.00 21.63 ?  108 LEU   A HD23 1 
ATOM   2168 N  N    . LEU   A 1 109 ? 23.563 -10.277 -7.238  1.00 12.88 ?  109 LEU   A N    1 
ATOM   2169 C  CA   . LEU   A 1 109 ? 22.874 -10.161 -5.959  1.00 12.41 ?  109 LEU   A CA   1 
ATOM   2170 C  C    . LEU   A 1 109 ? 23.227 -11.320 -5.037  1.00 11.21 ?  109 LEU   A C    1 
ATOM   2171 O  O    . LEU   A 1 109 ? 23.364 -11.137 -3.822  1.00 11.80 ?  109 LEU   A O    1 
ATOM   2172 C  CB   . LEU   A 1 109 ? 21.367 -10.071 -6.190  1.00 13.00 ?  109 LEU   A CB   1 
ATOM   2173 C  CG   . LEU   A 1 109 ? 20.495 -9.802  -4.965  1.00 13.39 ?  109 LEU   A CG   1 
ATOM   2174 C  CD1  . LEU   A 1 109 ? 20.972 -8.556  -4.226  1.00 14.05 ?  109 LEU   A CD1  1 
ATOM   2175 C  CD2  . LEU   A 1 109 ? 19.042 -9.645  -5.385  1.00 14.51 ?  109 LEU   A CD2  1 
ATOM   2176 H  H    . LEU   A 1 109 ? 23.048 -10.374 -7.918  1.00 15.46 ?  109 LEU   A H    1 
ATOM   2177 H  HA   . LEU   A 1 109 ? 23.163 -9.343  -5.528  1.00 14.90 ?  109 LEU   A HA   1 
ATOM   2178 H  HB2  . LEU   A 1 109 ? 21.202 -9.349  -6.820  1.00 15.61 ?  109 LEU   A HB2  1 
ATOM   2179 H  HB3  . LEU   A 1 109 ? 21.067 -10.905 -6.575  1.00 15.61 ?  109 LEU   A HB3  1 
ATOM   2180 H  HG   . LEU   A 1 109 ? 20.555 -10.555 -4.361  1.00 16.07 ?  109 LEU   A HG   1 
ATOM   2181 H  HD11 . LEU   A 1 109 ? 20.295 -8.278  -3.595  1.00 16.87 ?  109 LEU   A HD11 1 
ATOM   2182 H  HD12 . LEU   A 1 109 ? 21.799 -8.764  -3.756  1.00 16.87 ?  109 LEU   A HD12 1 
ATOM   2183 H  HD13 . LEU   A 1 109 ? 21.135 -7.848  -4.872  1.00 16.87 ?  109 LEU   A HD13 1 
ATOM   2184 H  HD21 . LEU   A 1 109 ? 18.521 -9.352  -4.619  1.00 17.42 ?  109 LEU   A HD21 1 
ATOM   2185 H  HD22 . LEU   A 1 109 ? 18.982 -8.987  -6.094  1.00 17.42 ?  109 LEU   A HD22 1 
ATOM   2186 H  HD23 . LEU   A 1 109 ? 18.708 -10.502 -5.700  1.00 17.42 ?  109 LEU   A HD23 1 
ATOM   2187 N  N    . LYS   A 1 110 ? 23.379 -12.527 -5.589  1.00 11.30 ?  110 LYS   A N    1 
ATOM   2188 C  CA   . LYS   A 1 110 ? 23.759 -13.656 -4.745  1.00 11.30 ?  110 LYS   A CA   1 
ATOM   2189 C  C    . LYS   A 1 110 ? 25.144 -13.437 -4.144  1.00 10.92 ?  110 LYS   A C    1 
ATOM   2190 O  O    . LYS   A 1 110 ? 25.349 -13.634 -2.944  1.00 11.15 ?  110 LYS   A O    1 
ATOM   2191 C  CB   . LYS   A 1 110 ? 23.681 -14.976 -5.519  1.00 12.43 ?  110 LYS   A CB   1 
ATOM   2192 C  CG   . LYS   A 1 110 ? 23.896 -16.193 -4.617  1.00 12.42 ?  110 LYS   A CG   1 
ATOM   2193 C  CD   . LYS   A 1 110 ? 23.665 -17.510 -5.335  1.00 12.96 ?  110 LYS   A CD   1 
ATOM   2194 C  CE   . LYS   A 1 110 ? 23.747 -18.687 -4.385  1.00 13.92 ?  110 LYS   A CE   1 
ATOM   2195 N  NZ   . LYS   A 1 110 ? 22.572 -18.796 -3.480  1.00 14.03 ?  110 LYS   A NZ   1 
ATOM   2196 H  H    . LYS   A 1 110 ? 23.266 -12.715 -6.422  1.00 13.56 ?  110 LYS   A H    1 
ATOM   2197 H  HA   . LYS   A 1 110 ? 23.122 -13.717 -4.011  1.00 13.57 ?  110 LYS   A HA   1 
ATOM   2198 H  HB2  . LYS   A 1 110 ? 22.804 -15.055 -5.927  1.00 14.91 ?  110 LYS   A HB2  1 
ATOM   2199 H  HB3  . LYS   A 1 110 ? 24.369 -14.980 -6.201  1.00 14.91 ?  110 LYS   A HB3  1 
ATOM   2200 H  HG2  . LYS   A 1 110 ? 24.809 -16.188 -4.288  1.00 14.90 ?  110 LYS   A HG2  1 
ATOM   2201 H  HG3  . LYS   A 1 110 ? 23.277 -16.148 -3.870  1.00 14.90 ?  110 LYS   A HG3  1 
ATOM   2202 H  HD2  . LYS   A 1 110 ? 22.785 -17.505 -5.738  1.00 15.56 ?  110 LYS   A HD2  1 
ATOM   2203 H  HD3  . LYS   A 1 110 ? 24.347 -17.625 -6.016  1.00 15.56 ?  110 LYS   A HD3  1 
ATOM   2204 H  HE2  . LYS   A 1 110 ? 23.801 -19.505 -4.900  1.00 16.71 ?  110 LYS   A HE2  1 
ATOM   2205 H  HE3  . LYS   A 1 110 ? 24.537 -18.591 -3.830  1.00 16.71 ?  110 LYS   A HE3  1 
ATOM   2206 H  HZ1  . LYS   A 1 110 ? 22.659 -19.495 -2.943  1.00 16.84 ?  110 LYS   A HZ1  1 
ATOM   2207 H  HZ2  . LYS   A 1 110 ? 22.497 -18.056 -2.986  1.00 16.84 ?  110 LYS   A HZ2  1 
ATOM   2208 H  HZ3  . LYS   A 1 110 ? 21.825 -18.890 -3.961  1.00 16.84 ?  110 LYS   A HZ3  1 
ATOM   2209 N  N    . SER   A 1 111 ? 26.098 -12.997 -4.966  1.00 11.08 ?  111 SER   A N    1 
ATOM   2210 C  CA   . SER   A 1 111 ? 27.431 -12.690 -4.460  1.00 11.08 ?  111 SER   A CA   1 
ATOM   2211 C  C    . SER   A 1 111 ? 27.370 -11.644 -3.350  1.00 11.06 ?  111 SER   A C    1 
ATOM   2212 O  O    . SER   A 1 111 ? 28.068 -11.752 -2.337  1.00 11.38 ?  111 SER   A O    1 
ATOM   2213 C  CB   . SER   A 1 111 ? 28.312 -12.193 -5.605  1.00 12.48 ?  111 SER   A CB   1 
ATOM   2214 O  OG   . SER   A 1 111 ? 28.418 -13.179 -6.620  1.00 14.71 ?  111 SER   A OG   1 
ATOM   2215 H  H    . SER   A 1 111 ? 25.993 -12.870 -5.810  1.00 13.30 ?  111 SER   A H    1 
ATOM   2216 H  HA   . SER   A 1 111 ? 27.827 -13.497 -4.099  1.00 13.29 ?  111 SER   A HA   1 
ATOM   2217 H  HB2  . SER   A 1 111 ? 27.910 -11.396 -5.989  1.00 14.97 ?  111 SER   A HB2  1 
ATOM   2218 H  HB3  . SER   A 1 111 ? 29.192 -11.981 -5.253  1.00 14.97 ?  111 SER   A HB3  1 
ATOM   2219 H  HG   . SER   A 1 111 ? 28.931 -12.889 -7.236  1.00 17.66 ?  111 SER   A HG   1 
ATOM   2220 N  N    . ALA   A 1 112 ? 26.524 -10.626 -3.521  1.00 10.94 ?  112 ALA   A N    1 
ATOM   2221 C  CA   . ALA   A 1 112 ? 26.378 -9.591  -2.499  1.00 10.56 ?  112 ALA   A CA   1 
ATOM   2222 C  C    . ALA   A 1 112 ? 25.911 -10.192 -1.175  1.00 10.68 ?  112 ALA   A C    1 
ATOM   2223 O  O    . ALA   A 1 112 ? 26.467 -9.902  -0.109  1.00 10.90 ?  112 ALA   A O    1 
ATOM   2224 C  CB   . ALA   A 1 112 ? 25.420 -8.500  -2.985  1.00 11.25 ?  112 ALA   A CB   1 
ATOM   2225 H  H    . ALA   A 1 112 ? 26.031 -10.509 -4.213  1.00 13.13 ?  112 ALA   A H    1 
ATOM   2226 H  HA   . ALA   A 1 112 ? 27.241 -9.174  -2.345  1.00 12.67 ?  112 ALA   A HA   1 
ATOM   2227 H  HB1  . ALA   A 1 112 ? 25.348 -7.811  -2.300  1.00 13.51 ?  112 ALA   A HB1  1 
ATOM   2228 H  HB2  . ALA   A 1 112 ? 25.767 -8.112  -3.802  1.00 13.51 ?  112 ALA   A HB2  1 
ATOM   2229 H  HB3  . ALA   A 1 112 ? 24.548 -8.891  -3.148  1.00 13.51 ?  112 ALA   A HB3  1 
ATOM   2230 N  N    . TYR   A 1 113 ? 24.884 -11.041 -1.220  1.00 10.68 ?  113 TYR   A N    1 
ATOM   2231 C  CA   . TYR   A 1 113 ? 24.375 -11.640 0.010   1.00 10.55 ?  113 TYR   A CA   1 
ATOM   2232 C  C    . TYR   A 1 113 ? 25.380 -12.594 0.649   1.00 10.41 ?  113 TYR   A C    1 
ATOM   2233 O  O    . TYR   A 1 113 ? 25.345 -12.784 1.867   1.00 10.84 ?  113 TYR   A O    1 
ATOM   2234 C  CB   . TYR   A 1 113 ? 23.065 -12.373 -0.263  1.00 10.95 ?  113 TYR   A CB   1 
ATOM   2235 C  CG   . TYR   A 1 113 ? 21.846 -11.484 -0.155  1.00 10.82 ?  113 TYR   A CG   1 
ATOM   2236 C  CD1  . TYR   A 1 113 ? 21.500 -10.886 1.054   1.00 10.73 ?  113 TYR   A CD1  1 
ATOM   2237 C  CD2  . TYR   A 1 113 ? 21.026 -11.262 -1.251  1.00 11.24 ?  113 TYR   A CD2  1 
ATOM   2238 C  CE1  . TYR   A 1 113 ? 20.379 -10.089 1.166   1.00 10.99 ?  113 TYR   A CE1  1 
ATOM   2239 C  CE2  . TYR   A 1 113 ? 19.882 -10.461 -1.147  1.00 11.19 ?  113 TYR   A CE2  1 
ATOM   2240 C  CZ   . TYR   A 1 113 ? 19.573 -9.885  0.063   1.00 10.84 ?  113 TYR   A CZ   1 
ATOM   2241 O  OH   . TYR   A 1 113 ? 18.452 -9.096  0.204   1.00 11.79 ?  113 TYR   A OH   1 
ATOM   2242 H  H    . TYR   A 1 113 ? 24.467 -11.272 -1.938  1.00 12.81 ?  113 TYR   A H    1 
ATOM   2243 H  HA   . TYR   A 1 113 ? 24.196 -10.936 0.647   1.00 12.66 ?  113 TYR   A HA   1 
ATOM   2244 H  HB2  . TYR   A 1 113 ? 23.088 -12.731 -1.165  1.00 13.15 ?  113 TYR   A HB2  1 
ATOM   2245 H  HB3  . TYR   A 1 113 ? 22.968 -13.091 0.377   1.00 13.15 ?  113 TYR   A HB3  1 
ATOM   2246 H  HD1  . TYR   A 1 113 ? 22.045 -11.024 1.800   1.00 12.88 ?  113 TYR   A HD1  1 
ATOM   2247 H  HD2  . TYR   A 1 113 ? 21.229 -11.662 -2.063  1.00 13.49 ?  113 TYR   A HD2  1 
ATOM   2248 H  HE1  . TYR   A 1 113 ? 20.166 -9.696  1.982   1.00 13.19 ?  113 TYR   A HE1  1 
ATOM   2249 H  HE2  . TYR   A 1 113 ? 19.331 -10.323 -1.885  1.00 13.43 ?  113 TYR   A HE2  1 
ATOM   2250 H  HH   . TYR   A 1 113 ? 18.043 -9.053  -0.536  1.00 14.15 ?  113 TYR   A HH   1 
ATOM   2251 N  N    . GLU   A 1 114 ? 26.275 -13.205 -0.144  1.00 10.55 ?  114 GLU   A N    1 
ATOM   2252 C  CA   . GLU   A 1 114 ? 27.272 -14.102 0.438   1.00 10.35 ?  114 GLU   A CA   1 
ATOM   2253 C  C    . GLU   A 1 114 ? 28.129 -13.397 1.483   1.00 10.71 ?  114 GLU   A C    1 
ATOM   2254 O  O    . GLU   A 1 114 ? 28.610 -14.032 2.427   1.00 10.87 ?  114 GLU   A O    1 
ATOM   2255 C  CB   . GLU   A 1 114 ? 28.138 -14.734 -0.661  1.00 10.53 ?  114 GLU   A CB   1 
ATOM   2256 C  CG   . GLU   A 1 114 ? 27.369 -15.785 -1.431  1.00 11.05 ?  114 GLU   A CG   1 
ATOM   2257 C  CD   . GLU   A 1 114 ? 28.064 -16.308 -2.681  1.00 11.52 ?  114 GLU   A CD   1 
ATOM   2258 O  OE1  . GLU   A 1 114 ? 29.016 -15.682 -3.185  1.00 11.84 ?  114 GLU   A OE1  1 
ATOM   2259 O  OE2  . GLU   A 1 114 ? 27.617 -17.370 -3.172  1.00 12.74 -1 114 GLU   A OE2  1 
ATOM   2260 H  H    . GLU   A 1 114 ? 26.324 -13.113 -1.004  1.00 12.66 ?  114 GLU   A H    1 
ATOM   2261 H  HA   . GLU   A 1 114 ? 26.808 -14.823 0.880   1.00 12.42 ?  114 GLU   A HA   1 
ATOM   2262 H  HB2  . GLU   A 1 114 ? 28.420 -14.049 -1.291  1.00 12.64 ?  114 GLU   A HB2  1 
ATOM   2263 H  HB3  . GLU   A 1 114 ? 28.912 -15.159 -0.262  1.00 12.64 ?  114 GLU   A HB3  1 
ATOM   2264 H  HG2  . GLU   A 1 114 ? 27.216 -16.547 -0.849  1.00 13.26 ?  114 GLU   A HG2  1 
ATOM   2265 H  HG3  . GLU   A 1 114 ? 26.518 -15.412 -1.708  1.00 13.26 ?  114 GLU   A HG3  1 
ATOM   2266 N  N    . ASN   A 1 115 ? 28.308 -12.080 1.355   1.00 10.35 ?  115 ASN   A N    1 
ATOM   2267 C  CA   . ASN   A 1 115 ? 29.072 -11.350 2.361   1.00 10.98 ?  115 ASN   A CA   1 
ATOM   2268 C  C    . ASN   A 1 115 ? 28.461 -11.489 3.748   1.00 10.64 ?  115 ASN   A C    1 
ATOM   2269 O  O    . ASN   A 1 115 ? 29.176 -11.419 4.753   1.00 10.85 ?  115 ASN   A O    1 
ATOM   2270 C  CB   . ASN   A 1 115 ? 29.166 -9.875  1.983   1.00 11.08 ?  115 ASN   A CB   1 
ATOM   2271 C  CG   . ASN   A 1 115 ? 29.966 -9.652  0.720   1.00 12.06 ?  115 ASN   A CG   1 
ATOM   2272 O  OD1  . ASN   A 1 115 ? 31.184 -9.756  0.731   1.00 15.21 ?  115 ASN   A OD1  1 
ATOM   2273 N  ND2  . ASN   A 1 115 ? 29.290 -9.342  -0.371  1.00 11.38 ?  115 ASN   A ND2  1 
ATOM   2274 H  H    . ASN   A 1 115 ? 28.003 -11.593 0.712   1.00 12.42 ?  115 ASN   A H    1 
ATOM   2275 H  HA   . ASN   A 1 115 ? 29.971 -11.710 2.399   1.00 13.18 ?  115 ASN   A HA   1 
ATOM   2276 H  HB2  . ASN   A 1 115 ? 28.268 -9.527  1.849   1.00 13.30 ?  115 ASN   A HB2  1 
ATOM   2277 H  HB3  . ASN   A 1 115 ? 29.598 -9.392  2.709   1.00 13.30 ?  115 ASN   A HB3  1 
ATOM   2278 H  HD21 . ASN   A 1 115 ? 29.704 -9.205  -1.107  1.00 13.66 ?  115 ASN   A HD21 1 
ATOM   2279 H  HD22 . ASN   A 1 115 ? 28.428 -9.292  -0.343  1.00 13.66 ?  115 ASN   A HD22 1 
ATOM   2280 N  N    . PHE   A 1 116 ? 27.136 -11.653 3.828   1.00 10.57 ?  116 PHE   A N    1 
ATOM   2281 C  CA   . PHE   A 1 116 ? 26.491 -11.757 5.132   1.00 10.51 ?  116 PHE   A CA   1 
ATOM   2282 C  C    . PHE   A 1 116 ? 26.974 -12.988 5.894   1.00 10.89 ?  116 PHE   A C    1 
ATOM   2283 O  O    . PHE   A 1 116 ? 26.899 -13.014 7.122   1.00 11.51 ?  116 PHE   A O    1 
ATOM   2284 C  CB   . PHE   A 1 116 ? 24.964 -11.890 4.998   1.00 10.64 ?  116 PHE   A CB   1 
ATOM   2285 C  CG   . PHE   A 1 116 ? 24.210 -10.644 4.548   1.00 10.85 ?  116 PHE   A CG   1 
ATOM   2286 C  CD1  . PHE   A 1 116 ? 24.783 -9.620  3.807   1.00 11.01 ?  116 PHE   A CD1  1 
ATOM   2287 C  CD2  . PHE   A 1 116 ? 22.860 -10.542 4.872   1.00 11.40 ?  116 PHE   A CD2  1 
ATOM   2288 C  CE1  . PHE   A 1 116 ? 24.016 -8.530  3.406   1.00 11.13 ?  116 PHE   A CE1  1 
ATOM   2289 C  CE2  . PHE   A 1 116 ? 22.097 -9.460  4.482   1.00 11.32 ?  116 PHE   A CE2  1 
ATOM   2290 C  CZ   . PHE   A 1 116 ? 22.665 -8.451  3.743   1.00 10.99 ?  116 PHE   A CZ   1 
ATOM   2291 H  H    . PHE   A 1 116 ? 26.597 -11.700 3.154   1.00 12.68 ?  116 PHE   A H    1 
ATOM   2292 H  HA   . PHE   A 1 116 ? 26.682 -10.964 5.659   1.00 12.62 ?  116 PHE   A HA   1 
ATOM   2293 H  HB2  . PHE   A 1 116 ? 24.778 -12.590 4.349   1.00 12.77 ?  116 PHE   A HB2  1 
ATOM   2294 H  HB3  . PHE   A 1 116 ? 24.604 -12.150 5.859   1.00 12.77 ?  116 PHE   A HB3  1 
ATOM   2295 H  HD1  . PHE   A 1 116 ? 25.677 -9.673  3.568   1.00 13.21 ?  116 PHE   A HD1  1 
ATOM   2296 H  HD2  . PHE   A 1 116 ? 22.458 -11.231 5.363   1.00 13.68 ?  116 PHE   A HD2  1 
ATOM   2297 H  HE1  . PHE   A 1 116 ? 24.412 -7.849  2.913   1.00 13.36 ?  116 PHE   A HE1  1 
ATOM   2298 H  HE2  . PHE   A 1 116 ? 21.197 -9.427  4.717   1.00 13.59 ?  116 PHE   A HE2  1 
ATOM   2299 H  HZ   . PHE   A 1 116 ? 22.158 -7.717  3.487   1.00 13.20 ?  116 PHE   A HZ   1 
ATOM   2300 N  N    . ASN   A 1 117 ? 27.415 -14.036 5.187   1.00 10.92 ?  117 ASN   A N    1 
ATOM   2301 C  CA   . ASN   A 1 117 ? 27.780 -15.286 5.849   1.00 11.10 ?  117 ASN   A CA   1 
ATOM   2302 C  C    . ASN   A 1 117 ? 29.044 -15.170 6.678   1.00 11.79 ?  117 ASN   A C    1 
ATOM   2303 O  O    . ASN   A 1 117 ? 29.349 -16.085 7.449   1.00 12.58 ?  117 ASN   A O    1 
ATOM   2304 C  CB   . ASN   A 1 117 ? 27.889 -16.404 4.818   1.00 11.42 ?  117 ASN   A CB   1 
ATOM   2305 C  CG   . ASN   A 1 117 ? 26.533 -16.786 4.286   1.00 11.55 ?  117 ASN   A CG   1 
ATOM   2306 O  OD1  . ASN   A 1 117 ? 25.564 -16.829 5.045   1.00 12.25 ?  117 ASN   A OD1  1 
ATOM   2307 N  ND2  . ASN   A 1 117 ? 26.440 -17.032 2.991   1.00 11.48 ?  117 ASN   A ND2  1 
ATOM   2308 H  H    . ASN   A 1 117 ? 27.492 -14.045 4.327   1.00 13.11 ?  117 ASN   A H    1 
ATOM   2309 H  HA   . ASN   A 1 117 ? 27.059 -15.520 6.452   1.00 13.32 ?  117 ASN   A HA   1 
ATOM   2310 H  HB2  . ASN   A 1 117 ? 28.438 -16.107 4.076   1.00 13.71 ?  117 ASN   A HB2  1 
ATOM   2311 H  HB3  . ASN   A 1 117 ? 28.278 -17.184 5.236   1.00 13.71 ?  117 ASN   A HB3  1 
ATOM   2312 H  HD21 . ASN   A 1 117 ? 25.684 -17.243 2.646   1.00 13.77 ?  117 ASN   A HD21 1 
ATOM   2313 H  HD22 . ASN   A 1 117 ? 27.140 -16.975 2.489   1.00 13.77 ?  117 ASN   A HD22 1 
ATOM   2314 N  N    . GLN   A 1 118 ? 29.771 -14.065 6.550   1.00 11.80 ?  118 GLN   A N    1 
ATOM   2315 C  CA   . GLN   A 1 118 ? 30.952 -13.823 7.363   1.00 12.29 ?  118 GLN   A CA   1 
ATOM   2316 C  C    . GLN   A 1 118 ? 30.617 -13.249 8.734   1.00 12.27 ?  118 GLN   A C    1 
ATOM   2317 O  O    . GLN   A 1 118 ? 31.536 -12.961 9.509   1.00 14.05 ?  118 GLN   A O    1 
ATOM   2318 C  CB   . GLN   A 1 118 ? 31.930 -12.912 6.617   1.00 12.39 ?  118 GLN   A CB   1 
ATOM   2319 C  CG   . GLN   A 1 118 ? 32.396 -13.496 5.296   1.00 12.51 ?  118 GLN   A CG   1 
ATOM   2320 C  CD   . GLN   A 1 118 ? 33.225 -14.758 5.479   1.00 12.44 ?  118 GLN   A CD   1 
ATOM   2321 O  OE1  . GLN   A 1 118 ? 34.088 -14.820 6.362   1.00 13.50 ?  118 GLN   A OE1  1 
ATOM   2322 N  NE2  . GLN   A 1 118 ? 32.973 -15.764 4.642   1.00 12.66 ?  118 GLN   A NE2  1 
ATOM   2323 H  H    . GLN   A 1 118 ? 29.592 -13.422 5.997   1.00 14.16 ?  118 GLN   A H    1 
ATOM   2324 H  HA   . GLN   A 1 118 ? 31.393 -14.674 7.505   1.00 14.75 ?  118 GLN   A HA   1 
ATOM   2325 H  HB2  . GLN   A 1 118 ? 31.498 -12.065 6.438   1.00 14.87 ?  118 GLN   A HB2  1 
ATOM   2326 H  HB3  . GLN   A 1 118 ? 32.713 -12.774 7.175   1.00 14.87 ?  118 GLN   A HB3  1 
ATOM   2327 H  HG2  . GLN   A 1 118 ? 31.623 -13.715 4.750   1.00 15.01 ?  118 GLN   A HG2  1 
ATOM   2328 H  HG3  . GLN   A 1 118 ? 32.947 -12.841 4.834   1.00 15.01 ?  118 GLN   A HG3  1 
ATOM   2329 H  HE21 . GLN   A 1 118 ? 32.360 -15.681 4.034   1.00 15.19 ?  118 GLN   A HE21 1 
ATOM   2330 H  HE22 . GLN   A 1 118 ? 33.412 -16.498 4.701   1.00 15.19 ?  118 GLN   A HE22 1 
ATOM   2331 N  N    . HIS   A 1 119 ? 29.331 -13.101 9.055   1.00 11.82 ?  119 HIS   A N    1 
ATOM   2332 C  CA   . HIS   A 1 119 ? 28.882 -12.490 10.301  1.00 12.41 ?  119 HIS   A CA   1 
ATOM   2333 C  C    . HIS   A 1 119 ? 27.745 -13.312 10.881  1.00 12.46 ?  119 HIS   A C    1 
ATOM   2334 O  O    . HIS   A 1 119 ? 26.791 -13.641 10.171  1.00 13.09 ?  119 HIS   A O    1 
ATOM   2335 C  CB   . HIS   A 1 119 ? 28.421 -11.060 10.025  1.00 13.04 ?  119 HIS   A CB   1 
ATOM   2336 C  CG   . HIS   A 1 119 ? 29.497 -10.247 9.406   1.00 14.26 ?  119 HIS   A CG   1 
ATOM   2337 N  ND1  . HIS   A 1 119 ? 30.477 -9.641  10.156  1.00 16.30 ?  119 HIS   A ND1  1 
ATOM   2338 C  CD2  . HIS   A 1 119 ? 29.824 -10.047 8.110   1.00 15.14 ?  119 HIS   A CD2  1 
ATOM   2339 C  CE1  . HIS   A 1 119 ? 31.335 -9.052  9.343   1.00 16.65 ?  119 HIS   A CE1  1 
ATOM   2340 N  NE2  . HIS   A 1 119 ? 30.970 -9.293  8.098   1.00 16.55 ?  119 HIS   A NE2  1 
ATOM   2341 H  H    . HIS   A 1 119 ? 28.680 -13.361 8.552   1.00 14.19 ?  119 HIS   A H    1 
ATOM   2342 H  HA   . HIS   A 1 119 ? 29.617 -12.473 10.938  1.00 14.89 ?  119 HIS   A HA   1 
ATOM   2343 H  HB2  . HIS   A 1 119 ? 27.665 -11.090 9.418   1.00 15.65 ?  119 HIS   A HB2  1 
ATOM   2344 H  HB3  . HIS   A 1 119 ? 28.167 -10.649 10.863  1.00 15.65 ?  119 HIS   A HB3  1 
ATOM   2345 H  HD2  . HIS   A 1 119 ? 29.359 -10.361 7.364   1.00 18.17 ?  119 HIS   A HD2  1 
ATOM   2346 H  HE1  . HIS   A 1 119 ? 32.071 -8.549  9.601   1.00 19.99 ?  119 HIS   A HE1  1 
ATOM   2347 H  HE2  . HIS   A 1 119 ? 31.367 -8.998  7.391   1.00 19.86 ?  119 HIS   A HE2  1 
ATOM   2348 N  N    . GLU   A 1 120 ? 27.845 -13.629 12.173  1.00 13.38 ?  120 GLU   A N    1 
ATOM   2349 C  CA   . GLU   A 1 120 ? 26.898 -14.565 12.776  1.00 15.23 ?  120 GLU   A CA   1 
ATOM   2350 C  C    . GLU   A 1 120 ? 25.483 -13.999 12.838  1.00 14.14 ?  120 GLU   A C    1 
ATOM   2351 O  O    . GLU   A 1 120 ? 24.505 -14.756 12.726  1.00 14.44 ?  120 GLU   A O    1 
ATOM   2352 C  CB   . GLU   A 1 120 ? 27.380 -14.966 14.171  1.00 19.78 ?  120 GLU   A CB   1 
ATOM   2353 C  CG   . GLU   A 1 120 ? 28.556 -15.927 14.162  1.00 25.87 ?  120 GLU   A CG   1 
ATOM   2354 C  CD   . GLU   A 1 120 ? 28.723 -16.645 15.486  1.00 31.45 ?  120 GLU   A CD   1 
ATOM   2355 O  OE1  . GLU   A 1 120 ? 28.266 -16.108 16.518  1.00 33.48 ?  120 GLU   A OE1  1 
ATOM   2356 O  OE2  . GLU   A 1 120 ? 29.304 -17.751 15.493  1.00 35.83 -1 120 GLU   A OE2  1 
ATOM   2357 H  H    . GLU   A 1 120 ? 28.451 -13.329 12.712  1.00 16.06 ?  120 GLU   A H    1 
ATOM   2358 H  HA   . GLU   A 1 120 ? 26.870 -15.368 12.240  1.00 18.28 ?  120 GLU   A HA   1 
ATOM   2359 H  HB2  . GLU   A 1 120 ? 27.658 -14.174 14.657  1.00 23.73 ?  120 GLU   A HB2  1 
ATOM   2360 H  HB3  . GLU   A 1 120 ? 26.653 -15.402 14.646  1.00 23.73 ?  120 GLU   A HB3  1 
ATOM   2361 H  HG2  . GLU   A 1 120 ? 28.422 -16.595 13.470  1.00 31.05 ?  120 GLU   A HG2  1 
ATOM   2362 H  HG3  . GLU   A 1 120 ? 29.375 -15.436 13.997  1.00 31.05 ?  120 GLU   A HG3  1 
ATOM   2363 N  N    . VAL   A 1 121 ? 25.354 -12.691 13.064  1.00 13.58 ?  121 VAL   A N    1 
ATOM   2364 C  CA   . VAL   A 1 121 ? 24.061 -12.025 13.187  1.00 13.70 ?  121 VAL   A CA   1 
ATOM   2365 C  C    . VAL   A 1 121 ? 24.166 -10.642 12.555  1.00 12.32 ?  121 VAL   A C    1 
ATOM   2366 O  O    . VAL   A 1 121 ? 25.140 -9.917  12.789  1.00 13.37 ?  121 VAL   A O    1 
ATOM   2367 C  CB   . VAL   A 1 121 ? 23.621 -11.891 14.662  1.00 16.75 ?  121 VAL   A CB   1 
ATOM   2368 C  CG1  . VAL   A 1 121 ? 22.226 -11.286 14.749  1.00 17.44 ?  121 VAL   A CG1  1 
ATOM   2369 C  CG2  . VAL   A 1 121 ? 23.654 -13.225 15.384  1.00 18.98 ?  121 VAL   A CG2  1 
ATOM   2370 H  H    . VAL   A 1 121 ? 26.021 -12.151 13.160  1.00 16.30 ?  121 VAL   A H    1 
ATOM   2371 H  HA   . VAL   A 1 121 ? 23.389 -12.538 12.715  1.00 16.44 ?  121 VAL   A HA   1 
ATOM   2372 H  HB   . VAL   A 1 121 ? 24.227 -11.293 15.121  1.00 20.10 ?  121 VAL   A HB   1 
ATOM   2373 H  HG11 . VAL   A 1 121 ? 21.910 -11.346 15.665  1.00 20.94 ?  121 VAL   A HG11 1 
ATOM   2374 H  HG12 . VAL   A 1 121 ? 22.264 -10.357 14.475  1.00 20.94 ?  121 VAL   A HG12 1 
ATOM   2375 H  HG13 . VAL   A 1 121 ? 21.629 -11.780 14.163  1.00 20.94 ?  121 VAL   A HG13 1 
ATOM   2376 H  HG21 . VAL   A 1 121 ? 23.291 -13.111 16.282  1.00 22.78 ?  121 VAL   A HG21 1 
ATOM   2377 H  HG22 . VAL   A 1 121 ? 23.110 -13.866 14.896  1.00 22.78 ?  121 VAL   A HG22 1 
ATOM   2378 H  HG23 . VAL   A 1 121 ? 24.567 -13.537 15.437  1.00 22.78 ?  121 VAL   A HG23 1 
ATOM   2379 N  N    . LEU   A 1 122 ? 23.147 -10.250 11.783  1.00 11.94 ?  122 LEU   A N    1 
ATOM   2380 C  CA   . LEU   A 1 122 ? 23.150 -8.950  11.118  1.00 11.89 ?  122 LEU   A CA   1 
ATOM   2381 C  C    . LEU   A 1 122 ? 21.754 -8.357  11.077  1.00 11.64 ?  122 LEU   A C    1 
ATOM   2382 O  O    . LEU   A 1 122 ? 20.759 -9.074  10.957  1.00 12.90 ?  122 LEU   A O    1 
ATOM   2383 C  CB   . LEU   A 1 122 ? 23.568 -9.033  9.647   1.00 13.28 ?  122 LEU   A CB   1 
ATOM   2384 C  CG   . LEU   A 1 122 ? 24.774 -9.881  9.270   1.00 13.46 ?  122 LEU   A CG   1 
ATOM   2385 C  CD1  . LEU   A 1 122 ? 24.377 -11.334 9.062   1.00 14.48 ?  122 LEU   A CD1  1 
ATOM   2386 C  CD2  . LEU   A 1 122 ? 25.431 -9.313  8.014   1.00 12.89 ?  122 LEU   A CD2  1 
ATOM   2387 H  H    . LEU   A 1 122 ? 22.436 -10.719 11.632  1.00 14.34 ?  122 LEU   A H    1 
ATOM   2388 H  HA   . LEU   A 1 122 ? 23.742 -8.338  11.585  1.00 14.27 ?  122 LEU   A HA   1 
ATOM   2389 H  HB2  . LEU   A 1 122 ? 22.823 -9.383  9.145   1.00 15.94 ?  122 LEU   A HB2  1 
ATOM   2390 H  HB3  . LEU   A 1 122 ? 23.760 -8.131  9.344   1.00 15.94 ?  122 LEU   A HB3  1 
ATOM   2391 H  HG   . LEU   A 1 122 ? 25.437 -9.843  9.980   1.00 16.16 ?  122 LEU   A HG   1 
ATOM   2392 H  HD11 . LEU   A 1 122 ? 25.147 -11.837 8.755   1.00 17.38 ?  122 LEU   A HD11 1 
ATOM   2393 H  HD12 . LEU   A 1 122 ? 24.061 -11.695 9.905   1.00 17.38 ?  122 LEU   A HD12 1 
ATOM   2394 H  HD13 . LEU   A 1 122 ? 23.670 -11.376 8.398   1.00 17.38 ?  122 LEU   A HD13 1 
ATOM   2395 H  HD21 . LEU   A 1 122 ? 26.176 -9.881  7.755   1.00 15.47 ?  122 LEU   A HD21 1 
ATOM   2396 H  HD22 . LEU   A 1 122 ? 24.775 -9.288  7.298   1.00 15.47 ?  122 LEU   A HD22 1 
ATOM   2397 H  HD23 . LEU   A 1 122 ? 25.752 -8.415  8.197   1.00 15.47 ?  122 LEU   A HD23 1 
ATOM   2398 N  N    A LEU   A 1 123 ? 21.700 -7.032  11.185  0.72 11.19 ?  123 LEU   A N    1 
ATOM   2399 N  N    B LEU   A 1 123 ? 21.704 -7.027  11.146  0.28 11.58 ?  123 LEU   A N    1 
ATOM   2400 C  CA   A LEU   A 1 123 ? 20.533 -6.233  10.838  0.72 11.14 ?  123 LEU   A CA   1 
ATOM   2401 C  CA   B LEU   A 1 123 ? 20.514 -6.240  10.847  0.28 11.78 ?  123 LEU   A CA   1 
ATOM   2402 C  C    A LEU   A 1 123 ? 20.760 -5.705  9.432   0.72 10.61 ?  123 LEU   A C    1 
ATOM   2403 C  C    B LEU   A 1 123 ? 20.722 -5.632  9.465   0.28 11.61 ?  123 LEU   A C    1 
ATOM   2404 O  O    A LEU   A 1 123 ? 21.834 -5.170  9.147   0.72 10.21 ?  123 LEU   A O    1 
ATOM   2405 O  O    B LEU   A 1 123 ? 21.648 -4.836  9.277   0.28 11.47 ?  123 LEU   A O    1 
ATOM   2406 C  CB   A LEU   A 1 123 ? 20.411 -5.048  11.796  0.72 11.83 ?  123 LEU   A CB   1 
ATOM   2407 C  CB   B LEU   A 1 123 ? 20.360 -5.132  11.890  0.28 12.16 ?  123 LEU   A CB   1 
ATOM   2408 C  CG   A LEU   A 1 123 ? 19.342 -4.008  11.456  0.72 12.64 ?  123 LEU   A CG   1 
ATOM   2409 C  CG   B LEU   A 1 123 ? 19.392 -3.992  11.563  0.28 12.19 ?  123 LEU   A CG   1 
ATOM   2410 C  CD1  A LEU   A 1 123 ? 17.965 -4.645  11.464  0.72 13.42 ?  123 LEU   A CD1  1 
ATOM   2411 C  CD1  B LEU   A 1 123 ? 17.956 -4.487  11.549  0.28 12.59 ?  123 LEU   A CD1  1 
ATOM   2412 C  CD2  A LEU   A 1 123 ? 19.405 -2.826  12.425  0.72 13.31 ?  123 LEU   A CD2  1 
ATOM   2413 C  CD2  B LEU   A 1 123 ? 19.567 -2.848  12.550  0.28 12.40 ?  123 LEU   A CD2  1 
ATOM   2414 H  H    A LEU   A 1 123 ? 22.359 -6.551  11.467  0.72 13.43 ?  123 LEU   A H    1 
ATOM   2415 H  H    B LEU   A 1 123 ? 22.377 -6.536  11.367  0.28 13.90 ?  123 LEU   A H    1 
ATOM   2416 H  HA   A LEU   A 1 123 ? 19.724 -6.767  10.862  0.72 13.37 ?  123 LEU   A HA   1 
ATOM   2417 H  HA   B LEU   A 1 123 ? 19.720 -6.796  10.845  0.28 14.14 ?  123 LEU   A HA   1 
ATOM   2418 H  HB2  A LEU   A 1 123 ? 20.197 -5.390  12.678  0.72 14.20 ?  123 LEU   A HB2  1 
ATOM   2419 H  HB2  B LEU   A 1 123 ? 20.050 -5.536  12.717  0.28 14.60 ?  123 LEU   A HB2  1 
ATOM   2420 H  HB3  A LEU   A 1 123 ? 21.259 -4.585  11.824  0.72 14.20 ?  123 LEU   A HB3  1 
ATOM   2421 H  HB3  B LEU   A 1 123 ? 21.230 -4.731  12.039  0.28 14.60 ?  123 LEU   A HB3  1 
ATOM   2422 H  HG   A LEU   A 1 123 ? 19.501 -3.657  10.562  0.72 15.17 ?  123 LEU   A HG   1 
ATOM   2423 H  HG   B LEU   A 1 123 ? 19.592 -3.641  10.682  0.28 14.63 ?  123 LEU   A HG   1 
ATOM   2424 H  HD11 A LEU   A 1 123 ? 17.294 -3.957  11.340  0.72 16.11 ?  123 LEU   A HD11 1 
ATOM   2425 H  HD11 B LEU   A 1 123 ? 17.368 -3.744  11.344  0.28 15.11 ?  123 LEU   A HD11 1 
ATOM   2426 H  HD12 A LEU   A 1 123 ? 17.913 -5.293  10.744  0.72 16.11 ?  123 LEU   A HD12 1 
ATOM   2427 H  HD12 B LEU   A 1 123 ? 17.867 -5.177  10.873  0.28 15.11 ?  123 LEU   A HD12 1 
ATOM   2428 H  HD13 A LEU   A 1 123 ? 17.830 -5.088  12.318  0.72 16.11 ?  123 LEU   A HD13 1 
ATOM   2429 H  HD13 B LEU   A 1 123 ? 17.739 -4.850  12.422  0.28 15.11 ?  123 LEU   A HD13 1 
ATOM   2430 H  HD21 A LEU   A 1 123 ? 18.721 -2.181  12.188  0.72 15.98 ?  123 LEU   A HD21 1 
ATOM   2431 H  HD21 B LEU   A 1 123 ? 18.944 -2.141  12.325  0.28 14.88 ?  123 LEU   A HD21 1 
ATOM   2432 H  HD22 A LEU   A 1 123 ? 19.253 -3.152  13.327  0.72 15.98 ?  123 LEU   A HD22 1 
ATOM   2433 H  HD22 B LEU   A 1 123 ? 19.389 -3.176  13.445  0.28 14.88 ?  123 LEU   A HD22 1 
ATOM   2434 H  HD23 A LEU   A 1 123 ? 20.282 -2.416  12.366  0.72 15.98 ?  123 LEU   A HD23 1 
ATOM   2435 H  HD23 B LEU   A 1 123 ? 20.477 -2.519  12.492  0.28 14.88 ?  123 LEU   A HD23 1 
ATOM   2436 N  N    A ALA   A 1 124 ? 19.767 -5.842  8.553   0.72 10.09 ?  124 ALA   A N    1 
ATOM   2437 N  N    B ALA   A 1 124 ? 19.881 -5.999  8.505   0.28 11.47 ?  124 ALA   A N    1 
ATOM   2438 C  CA   A ALA   A 1 124 ? 20.025 -5.540  7.154   0.72 9.96  ?  124 ALA   A CA   1 
ATOM   2439 C  CA   B ALA   A 1 124 ? 20.177 -5.734  7.106   0.28 11.63 ?  124 ALA   A CA   1 
ATOM   2440 C  C    A ALA   A 1 124 ? 18.779 -5.072  6.422   0.72 10.14 ?  124 ALA   A C    1 
ATOM   2441 C  C    B ALA   A 1 124 ? 18.937 -5.312  6.333   0.28 11.16 ?  124 ALA   A C    1 
ATOM   2442 O  O    A ALA   A 1 124 ? 17.653 -5.435  6.795   0.72 10.87 ?  124 ALA   A O    1 
ATOM   2443 O  O    B ALA   A 1 124 ? 17.807 -5.620  6.732   0.28 11.27 ?  124 ALA   A O    1 
ATOM   2444 C  CB   A ALA   A 1 124 ? 20.594 -6.764  6.426   0.72 10.37 ?  124 ALA   A CB   1 
ATOM   2445 C  CB   B ALA   A 1 124 ? 20.783 -6.975  6.437   0.28 12.29 ?  124 ALA   A CB   1 
ATOM   2446 H  H    A ALA   A 1 124 ? 18.964 -6.094  8.732   0.72 12.11 ?  124 ALA   A H    1 
ATOM   2447 H  H    B ALA   A 1 124 ? 19.133 -6.405  8.638   0.28 13.77 ?  124 ALA   A H    1 
ATOM   2448 H  HA   A ALA   A 1 124 ? 20.693 -4.836  7.111   0.72 11.96 ?  124 ALA   A HA   1 
ATOM   2449 H  HA   B ALA   A 1 124 ? 20.826 -5.017  7.060   0.28 13.95 ?  124 ALA   A HA   1 
ATOM   2450 H  HB1  A ALA   A 1 124 ? 20.766 -6.534  5.498   0.72 12.44 ?  124 ALA   A HB1  1 
ATOM   2451 H  HB1  B ALA   A 1 124 ? 20.973 -6.772  5.508   0.28 14.76 ?  124 ALA   A HB1  1 
ATOM   2452 H  HB2  A ALA   A 1 124 ? 21.431 -7.027  6.855   0.72 12.44 ?  124 ALA   A HB2  1 
ATOM   2453 H  HB2  B ALA   A 1 124 ? 21.604 -7.213  6.898   0.28 14.76 ?  124 ALA   A HB2  1 
ATOM   2454 H  HB3  A ALA   A 1 124 ? 19.958 -7.490  6.478   0.72 12.44 ?  124 ALA   A HB3  1 
ATOM   2455 H  HB3  B ALA   A 1 124 ? 20.148 -7.706  6.493   0.28 14.76 ?  124 ALA   A HB3  1 
ATOM   2456 N  N    A PRO   A 1 125 ? 18.957 -4.306  5.352   0.72 10.23 ?  125 PRO   A N    1 
ATOM   2457 N  N    B PRO   A 1 125 ? 19.122 -4.604  5.206   0.28 10.21 ?  125 PRO   A N    1 
ATOM   2458 C  CA   A PRO   A 1 125 ? 17.886 -4.064  4.390   0.72 10.81 ?  125 PRO   A CA   1 
ATOM   2459 C  CA   B PRO   A 1 125 ? 18.012 -4.345  4.284   0.28 10.16 ?  125 PRO   A CA   1 
ATOM   2460 C  C    A PRO   A 1 125 ? 17.943 -5.141  3.314   0.72 10.70 ?  125 PRO   A C    1 
ATOM   2461 C  C    B PRO   A 1 125 ? 18.028 -5.334  3.130   0.28 10.32 ?  125 PRO   A C    1 
ATOM   2462 O  O    A PRO   A 1 125 ? 18.902 -5.912  3.219   0.72 11.14 ?  125 PRO   A O    1 
ATOM   2463 O  O    B PRO   A 1 125 ? 19.027 -6.030  2.926   0.28 10.39 ?  125 PRO   A O    1 
ATOM   2464 C  CB   A PRO   A 1 125 ? 18.310 -2.721  3.785   0.72 11.24 ?  125 PRO   A CB   1 
ATOM   2465 C  CB   B PRO   A 1 125 ? 18.330 -2.935  3.780   0.28 10.11 ?  125 PRO   A CB   1 
ATOM   2466 C  CG   A PRO   A 1 125 ? 19.818 -2.886  3.671   0.72 11.86 ?  125 PRO   A CG   1 
ATOM   2467 C  CG   B PRO   A 1 125 ? 19.849 -2.942  3.697   0.28 10.13 ?  125 PRO   A CG   1 
ATOM   2468 C  CD   A PRO   A 1 125 ? 20.209 -3.637  4.940   0.72 11.04 ?  125 PRO   A CD   1 
ATOM   2469 C  CD   B PRO   A 1 125 ? 20.343 -3.887  4.790   0.28 9.68  ?  125 PRO   A CD   1 
ATOM   2470 H  HA   A PRO   A 1 125 ? 17.007 -4.018  4.807   0.72 12.97 ?  125 PRO   A HA   1 
ATOM   2471 H  HA   B PRO   A 1 125 ? 17.155 -4.364  4.736   0.28 12.19 ?  125 PRO   A HA   1 
ATOM   2472 H  HB2  A PRO   A 1 125 ? 17.891 -2.600  2.915   0.72 13.49 ?  125 PRO   A HB2  1 
ATOM   2473 H  HB2  B PRO   A 1 125 ? 17.929 -2.795  2.906   0.28 12.14 ?  125 PRO   A HB2  1 
ATOM   2474 H  HB3  A PRO   A 1 125 ? 18.072 -1.997  4.389   0.72 13.49 ?  125 PRO   A HB3  1 
ATOM   2475 H  HB3  B PRO   A 1 125 ? 18.014 -2.277  4.418   0.28 12.14 ?  125 PRO   A HB3  1 
ATOM   2476 H  HG2  A PRO   A 1 125 ? 20.031 -3.406  2.878   0.72 14.24 ?  125 PRO   A HG2  1 
ATOM   2477 H  HG2  B PRO   A 1 125 ? 20.121 -3.262  2.822   0.28 12.16 ?  125 PRO   A HG2  1 
ATOM   2478 H  HG3  A PRO   A 1 125 ? 20.238 -2.013  3.633   0.72 14.24 ?  125 PRO   A HG3  1 
ATOM   2479 H  HG3  B PRO   A 1 125 ? 20.181 -2.044  3.847   0.28 12.16 ?  125 PRO   A HG3  1 
ATOM   2480 H  HD2  A PRO   A 1 125 ? 20.902 -4.282  4.746   0.72 13.25 ?  125 PRO   A HD2  1 
ATOM   2481 H  HD2  B PRO   A 1 125 ? 20.998 -4.507  4.430   0.28 11.61 ?  125 PRO   A HD2  1 
ATOM   2482 H  HD3  A PRO   A 1 125 ? 20.491 -3.004  5.623   0.72 13.25 ?  125 PRO   A HD3  1 
ATOM   2483 H  HD3  B PRO   A 1 125 ? 20.706 -3.379  5.533   0.28 11.61 ?  125 PRO   A HD3  1 
ATOM   2484 N  N    A LEU   A 1 126 ? 16.912 -5.156  2.480   0.72 10.93 ?  126 LEU   A N    1 
ATOM   2485 N  N    B LEU   A 1 126 ? 16.950 -5.396  2.355   0.28 10.48 ?  126 LEU   A N    1 
ATOM   2486 C  CA   A LEU   A 1 126 ? 16.929 -5.997  1.291   0.72 11.09 ?  126 LEU   A CA   1 
ATOM   2487 C  CA   B LEU   A 1 126 ? 16.931 -6.214  1.147   0.28 10.85 ?  126 LEU   A CA   1 
ATOM   2488 C  C    A LEU   A 1 126 ? 17.875 -5.404  0.253   0.72 11.15 ?  126 LEU   A C    1 
ATOM   2489 C  C    B LEU   A 1 126 ? 17.759 -5.524  0.072   0.28 10.79 ?  126 LEU   A C    1 
ATOM   2490 O  O    A LEU   A 1 126 ? 17.682 -4.274  -0.207  0.72 11.67 ?  126 LEU   A O    1 
ATOM   2491 O  O    B LEU   A 1 126 ? 17.350 -4.502  -0.490  0.28 11.38 ?  126 LEU   A O    1 
ATOM   2492 C  CB   A LEU   A 1 126 ? 15.523 -6.133  0.716   0.72 12.18 ?  126 LEU   A CB   1 
ATOM   2493 C  CB   B LEU   A 1 126 ? 15.495 -6.444  0.688   0.28 11.14 ?  126 LEU   A CB   1 
ATOM   2494 C  CG   A LEU   A 1 126 ? 14.589 -7.061  1.488   0.72 13.30 ?  126 LEU   A CG   1 
ATOM   2495 C  CG   B LEU   A 1 126 ? 14.730 -7.429  1.574   0.28 11.63 ?  126 LEU   A CG   1 
ATOM   2496 C  CD1  A LEU   A 1 126 ? 13.170 -6.899  0.970   0.72 13.98 ?  126 LEU   A CD1  1 
ATOM   2497 C  CD1  B LEU   A 1 126 ? 13.257 -7.444  1.218   0.28 12.04 ?  126 LEU   A CD1  1 
ATOM   2498 C  CD2  A LEU   A 1 126 ? 15.040 -8.513  1.366   0.72 13.50 ?  126 LEU   A CD2  1 
ATOM   2499 C  CD2  B LEU   A 1 126 ? 15.333 -8.825  1.450   0.28 11.63 ?  126 LEU   A CD2  1 
ATOM   2500 H  H    A LEU   A 1 126 ? 16.191 -4.691  2.576   0.72 13.11 ?  126 LEU   A H    1 
ATOM   2501 H  H    B LEU   A 1 126 ? 16.222 -4.968  2.498   0.28 12.57 ?  126 LEU   A H    1 
ATOM   2502 H  HA   A LEU   A 1 126 ? 17.251 -6.877  1.526   0.72 13.31 ?  126 LEU   A HA   1 
ATOM   2503 H  HA   B LEU   A 1 126 ? 17.333 -7.077  1.332   0.28 13.02 ?  126 LEU   A HA   1 
ATOM   2504 H  HB2  A LEU   A 1 126 ? 15.109 -5.257  0.698   0.72 14.62 ?  126 LEU   A HB2  1 
ATOM   2505 H  HB2  B LEU   A 1 126 ? 15.016 -5.602  0.704   0.28 13.37 ?  126 LEU   A HB2  1 
ATOM   2506 H  HB3  A LEU   A 1 126 ? 15.590 -6.479  -0.187  0.72 14.62 ?  126 LEU   A HB3  1 
ATOM   2507 H  HB3  B LEU   A 1 126 ? 15.499 -6.804  -0.215  0.28 13.37 ?  126 LEU   A HB3  1 
ATOM   2508 H  HG   A LEU   A 1 126 ? 14.595 -6.819  2.428   0.72 15.96 ?  126 LEU   A HG   1 
ATOM   2509 H  HG   B LEU   A 1 126 ? 14.811 -7.151  2.500   0.28 13.96 ?  126 LEU   A HG   1 
ATOM   2510 H  HD11 A LEU   A 1 126 ? 12.583 -7.496  1.458   0.72 16.78 ?  126 LEU   A HD11 1 
ATOM   2511 H  HD11 B LEU   A 1 126 ? 12.799 -8.070  1.800   0.28 14.45 ?  126 LEU   A HD11 1 
ATOM   2512 H  HD12 A LEU   A 1 126 ? 12.891 -5.979  1.098   0.72 16.78 ?  126 LEU   A HD12 1 
ATOM   2513 H  HD12 B LEU   A 1 126 ? 12.898 -6.552  1.341   0.28 14.45 ?  126 LEU   A HD12 1 
ATOM   2514 H  HD13 A LEU   A 1 126 ? 13.154 -7.120  0.024   0.72 16.78 ?  126 LEU   A HD13 1 
ATOM   2515 H  HD13 B LEU   A 1 126 ? 13.161 -7.717  0.293   0.28 14.45 ?  126 LEU   A HD13 1 
ATOM   2516 H  HD21 A LEU   A 1 126 ? 14.362 -9.090  1.746   0.72 16.20 ?  126 LEU   A HD21 1 
ATOM   2517 H  HD21 B LEU   A 1 126 ? 14.706 -9.473  1.803   0.28 13.96 ?  126 LEU   A HD21 1 
ATOM   2518 H  HD22 A LEU   A 1 126 ? 15.169 -8.725  0.428   0.72 16.20 ?  126 LEU   A HD22 1 
ATOM   2519 H  HD22 B LEU   A 1 126 ? 15.509 -9.009  0.514   0.28 13.96 ?  126 LEU   A HD22 1 
ATOM   2520 H  HD23 A LEU   A 1 126 ? 15.877 -8.625  1.847   0.72 16.20 ?  126 LEU   A HD23 1 
ATOM   2521 H  HD23 B LEU   A 1 126 ? 16.162 -8.857  1.954   0.28 13.96 ?  126 LEU   A HD23 1 
ATOM   2522 N  N    A LEU   A 1 127 ? 18.900 -6.165  -0.114  0.72 11.34 ?  127 LEU   A N    1 
ATOM   2523 N  N    B LEU   A 1 127 ? 18.932 -6.080  -0.205  0.28 10.31 ?  127 LEU   A N    1 
ATOM   2524 C  CA   A LEU   A 1 127 ? 19.884 -5.687  -1.072  0.72 11.21 ?  127 LEU   A CA   1 
ATOM   2525 C  CA   B LEU   A 1 127 ? 19.867 -5.460  -1.128  0.28 10.29 ?  127 LEU   A CA   1 
ATOM   2526 C  C    A LEU   A 1 127 ? 19.252 -5.482  -2.439  0.72 10.40 ?  127 LEU   A C    1 
ATOM   2527 C  C    B LEU   A 1 127 ? 19.317 -5.446  -2.552  0.28 10.48 ?  127 LEU   A C    1 
ATOM   2528 O  O    A LEU   A 1 127 ? 18.411 -6.265  -2.891  0.72 11.57 ?  127 LEU   A O    1 
ATOM   2529 O  O    B LEU   A 1 127 ? 18.505 -6.288  -2.949  0.28 10.55 ?  127 LEU   A O    1 
ATOM   2530 C  CB   A LEU   A 1 127 ? 21.046 -6.673  -1.189  0.72 11.35 ?  127 LEU   A CB   1 
ATOM   2531 C  CB   B LEU   A 1 127 ? 21.198 -6.208  -1.087  0.28 10.56 ?  127 LEU   A CB   1 
ATOM   2532 C  CG   A LEU   A 1 127 ? 21.869 -6.895  0.076   0.72 11.37 ?  127 LEU   A CG   1 
ATOM   2533 C  CG   B LEU   A 1 127 ? 21.915 -6.202  0.267   0.28 10.61 ?  127 LEU   A CG   1 
ATOM   2534 C  CD1  A LEU   A 1 127 ? 22.975 -7.879  -0.208  0.72 11.80 ?  127 LEU   A CD1  1 
ATOM   2535 C  CD1  B LEU   A 1 127 ? 23.093 -7.159  0.242   0.28 11.01 ?  127 LEU   A CD1  1 
ATOM   2536 C  CD2  A LEU   A 1 127 ? 22.456 -5.601  0.586   0.72 12.29 ?  127 LEU   A CD2  1 
ATOM   2537 C  CD2  B LEU   A 1 127 ? 22.374 -4.790  0.635   0.28 11.02 ?  127 LEU   A CD2  1 
ATOM   2538 H  H    A LEU   A 1 127 ? 19.054 -6.957  0.184   0.72 13.61 ?  127 LEU   A H    1 
ATOM   2539 H  H    B LEU   A 1 127 ? 19.217 -6.814  0.149   0.28 12.38 ?  127 LEU   A H    1 
ATOM   2540 H  HA   A LEU   A 1 127 ? 20.235 -4.835  -0.774  0.72 13.46 ?  127 LEU   A HA   1 
ATOM   2541 H  HA   B LEU   A 1 127 ? 20.027 -4.541  -0.849  0.28 12.35 ?  127 LEU   A HA   1 
ATOM   2542 H  HB2  A LEU   A 1 127 ? 20.692 -7.534  -1.457  0.72 13.62 ?  127 LEU   A HB2  1 
ATOM   2543 H  HB2  B LEU   A 1 127 ? 21.036 -7.134  -1.325  0.28 12.67 ?  127 LEU   A HB2  1 
ATOM   2544 H  HB3  A LEU   A 1 127 ? 21.655 -6.348  -1.874  0.72 13.62 ?  127 LEU   A HB3  1 
ATOM   2545 H  HB3  B LEU   A 1 127 ? 21.796 -5.805  -1.733  0.28 12.67 ?  127 LEU   A HB3  1 
ATOM   2546 H  HG   A LEU   A 1 127 ? 21.297 -7.264  0.769   0.72 13.65 ?  127 LEU   A HG   1 
ATOM   2547 H  HG   B LEU   A 1 127 ? 21.301 -6.506  0.954   0.28 12.73 ?  127 LEU   A HG   1 
ATOM   2548 H  HD11 A LEU   A 1 127 ? 23.477 -8.034  0.610   0.72 14.16 ?  127 LEU   A HD11 1 
ATOM   2549 H  HD11 B LEU   A 1 127 ? 23.597 -7.058  1.063   0.28 13.22 ?  127 LEU   A HD11 1 
ATOM   2550 H  HD12 A LEU   A 1 127 ? 22.586 -8.712  -0.518  0.72 14.16 ?  127 LEU   A HD12 1 
ATOM   2551 H  HD12 B LEU   A 1 127 ? 22.758 -8.067  0.167   0.28 13.22 ?  127 LEU   A HD12 1 
ATOM   2552 H  HD13 A LEU   A 1 127 ? 23.559 -7.511  -0.888  0.72 14.16 ?  127 LEU   A HD13 1 
ATOM   2553 H  HD13 B LEU   A 1 127 ? 23.653 -6.947  -0.520  0.28 13.22 ?  127 LEU   A HD13 1 
ATOM   2554 H  HD21 A LEU   A 1 127 ? 23.084 -5.796  1.298   0.72 14.75 ?  127 LEU   A HD21 1 
ATOM   2555 H  HD21 B LEU   A 1 127 ? 22.902 -4.832  1.448   0.28 13.23 ?  127 LEU   A HD21 1 
ATOM   2556 H  HD22 A LEU   A 1 127 ? 22.916 -5.155  -0.146  0.72 14.75 ?  127 LEU   A HD22 1 
ATOM   2557 H  HD22 B LEU   A 1 127 ? 22.910 -4.435  -0.091  0.28 13.23 ?  127 LEU   A HD22 1 
ATOM   2558 H  HD23 A LEU   A 1 127 ? 21.742 -5.035  0.918   0.72 14.75 ?  127 LEU   A HD23 1 
ATOM   2559 H  HD23 B LEU   A 1 127 ? 21.594 -4.232  0.775   0.28 13.23 ?  127 LEU   A HD23 1 
ATOM   2560 N  N    A SER   A 1 128 ? 19.689 -4.419  -3.102  0.72 10.38 ?  128 SER   A N    1 
ATOM   2561 N  N    B SER   A 1 128 ? 19.785 -4.464  -3.321  0.28 10.69 ?  128 SER   A N    1 
ATOM   2562 C  CA   A SER   A 1 128 ? 19.273 -4.019  -4.438  0.72 10.34 ?  128 SER   A CA   1 
ATOM   2563 C  CA   B SER   A 1 128 ? 19.397 -4.227  -4.708  0.28 10.57 ?  128 SER   A CA   1 
ATOM   2564 C  C    A SER   A 1 128 ? 17.818 -3.572  -4.516  0.72 10.98 ?  128 SER   A C    1 
ATOM   2565 C  C    B SER   A 1 128 ? 17.969 -3.709  -4.864  0.28 10.40 ?  128 SER   A C    1 
ATOM   2566 O  O    A SER   A 1 128 ? 17.340 -3.288  -5.613  0.72 12.35 ?  128 SER   A O    1 
ATOM   2567 O  O    B SER   A 1 128 ? 17.610 -3.227  -5.942  0.28 10.37 ?  128 SER   A O    1 
ATOM   2568 C  CB   A SER   A 1 128 ? 19.606 -5.054  -5.521  0.72 10.47 ?  128 SER   A CB   1 
ATOM   2569 C  CB   B SER   A 1 128 ? 19.661 -5.450  -5.596  0.28 10.95 ?  128 SER   A CB   1 
ATOM   2570 O  OG   A SER   A 1 128 ? 21.015 -5.256  -5.592  0.72 11.09 ?  128 SER   A OG   1 
ATOM   2571 O  OG   B SER   A 1 128 ? 21.055 -5.635  -5.791  0.28 11.04 ?  128 SER   A OG   1 
ATOM   2572 H  H    A SER   A 1 128 ? 20.280 -3.877  -2.777  0.72 12.45 ?  128 SER   A H    1 
ATOM   2573 H  H    B SER   A 1 128 ? 20.371 -3.903  -3.044  0.28 12.83 ?  128 SER   A H    1 
ATOM   2574 H  HA   A SER   A 1 128 ? 19.798 -3.238  -4.664  0.72 12.41 ?  128 SER   A HA   1 
ATOM   2575 H  HA   B SER   A 1 128 ? 19.968 -3.528  -5.042  0.28 12.68 ?  128 SER   A HA   1 
ATOM   2576 H  HB2  A SER   A 1 128 ? 19.170 -5.891  -5.307  0.72 12.57 ?  128 SER   A HB2  1 
ATOM   2577 H  HB2  B SER   A 1 128 ? 19.292 -6.244  -5.185  0.28 13.15 ?  128 SER   A HB2  1 
ATOM   2578 H  HB3  A SER   A 1 128 ? 19.285 -4.725  -6.382  0.72 12.57 ?  128 SER   A HB3  1 
ATOM   2579 H  HB3  B SER   A 1 128 ? 19.247 -5.304  -6.465  0.28 13.15 ?  128 SER   A HB3  1 
ATOM   2580 H  HG   A SER   A 1 128 ? 21.399 -4.536  -5.786  0.72 13.31 ?  128 SER   A HG   1 
ATOM   2581 H  HG   B SER   A 1 128 ? 21.390 -4.952  -6.149  0.28 13.25 ?  128 SER   A HG   1 
ATOM   2582 N  N    A ALA   A 1 129 ? 17.118 -3.468  -3.387  0.72 11.31 ?  129 ALA   A N    1 
ATOM   2583 N  N    B ALA   A 1 129 ? 17.161 -3.780  -3.807  0.28 10.67 ?  129 ALA   A N    1 
ATOM   2584 C  CA   A ALA   A 1 129 ? 15.752 -2.968  -3.373  0.72 11.86 ?  129 ALA   A CA   1 
ATOM   2585 C  CA   B ALA   A 1 129 ? 15.804 -3.249  -3.839  0.28 11.10 ?  129 ALA   A CA   1 
ATOM   2586 C  C    A ALA   A 1 129 ? 15.756 -1.439  -3.375  0.72 11.40 ?  129 ALA   A C    1 
ATOM   2587 C  C    B ALA   A 1 129 ? 15.837 -1.743  -3.563  0.28 11.76 ?  129 ALA   A C    1 
ATOM   2588 O  O    A ALA   A 1 129 ? 16.804 -0.791  -3.458  0.72 11.69 ?  129 ALA   A O    1 
ATOM   2589 O  O    B ALA   A 1 129 ? 16.893 -1.103  -3.584  0.28 12.09 ?  129 ALA   A O    1 
ATOM   2590 C  CB   A ALA   A 1 129 ? 14.986 -3.543  -2.179  0.72 13.04 ?  129 ALA   A CB   1 
ATOM   2591 C  CB   B ALA   A 1 129 ? 14.909 -4.022  -2.870  0.28 10.20 ?  129 ALA   A CB   1 
ATOM   2592 H  H    A ALA   A 1 129 ? 17.421 -3.685  -2.609  0.72 13.57 ?  129 ALA   A H    1 
ATOM   2593 H  H    B ALA   A 1 129 ? 17.370 -4.147  -3.056  0.28 12.81 ?  129 ALA   A H    1 
ATOM   2594 H  HA   A ALA   A 1 129 ? 15.307 -3.267  -4.178  0.72 14.23 ?  129 ALA   A HA   1 
ATOM   2595 H  HA   B ALA   A 1 129 ? 15.444 -3.381  -4.727  0.28 13.33 ?  129 ALA   A HA   1 
ATOM   2596 H  HB1  A ALA   A 1 129 ? 14.076 -3.205  -2.197  0.72 15.65 ?  129 ALA   A HB1  1 
ATOM   2597 H  HB1  B ALA   A 1 129 ? 14.007 -3.668  -2.920  0.28 12.24 ?  129 ALA   A HB1  1 
ATOM   2598 H  HB2  A ALA   A 1 129 ? 14.978 -4.512  -2.244  0.72 15.65 ?  129 ALA   A HB2  1 
ATOM   2599 H  HB2  B ALA   A 1 129 ? 14.908 -4.961  -3.117  0.28 12.24 ?  129 ALA   A HB2  1 
ATOM   2600 H  HB3  A ALA   A 1 129 ? 15.424 -3.271  -1.359  0.72 15.65 ?  129 ALA   A HB3  1 
ATOM   2601 H  HB3  B ALA   A 1 129 ? 15.254 -3.922  -1.968  0.28 12.24 ?  129 ALA   A HB3  1 
ATOM   2602 N  N    A GLY   A 1 130 ? 14.567 -0.850  -3.302  0.72 12.48 ?  130 GLY   A N    1 
ATOM   2603 N  N    B GLY   A 1 130 ? 14.670 -1.157  -3.313  0.28 12.53 ?  130 GLY   A N    1 
ATOM   2604 C  CA   A GLY   A 1 130 ? 14.488 0.601   -3.293  0.72 13.04 ?  130 GLY   A CA   1 
ATOM   2605 C  CA   B GLY   A 1 130 ? 14.613 0.269   -3.049  0.28 12.71 ?  130 GLY   A CA   1 
ATOM   2606 C  C    A GLY   A 1 130 ? 15.114 1.194   -4.539  0.72 12.64 ?  130 GLY   A C    1 
ATOM   2607 C  C    B GLY   A 1 130 ? 15.063 1.065   -4.257  0.28 12.57 ?  130 GLY   A C    1 
ATOM   2608 O  O    A GLY   A 1 130 ? 14.898 0.721   -5.660  0.72 12.66 ?  130 GLY   A O    1 
ATOM   2609 O  O    B GLY   A 1 130 ? 14.698 0.770   -5.400  0.28 12.15 ?  130 GLY   A O    1 
ATOM   2610 H  H    A GLY   A 1 130 ? 13.810 -1.264  -3.261  0.72 14.97 ?  130 GLY   A H    1 
ATOM   2611 H  H    B GLY   A 1 130 ? 13.912 -1.560  -3.296  0.28 15.04 ?  130 GLY   A H    1 
ATOM   2612 H  HA2  A GLY   A 1 130 ? 13.556 0.873   -3.246  0.72 15.65 ?  130 GLY   A HA2  1 
ATOM   2613 H  HA2  B GLY   A 1 130 ? 13.704 0.521   -2.814  0.28 15.26 ?  130 GLY   A HA2  1 
ATOM   2614 H  HA3  A GLY   A 1 130 ? 14.951 0.944   -2.514  0.72 15.65 ?  130 GLY   A HA3  1 
ATOM   2615 H  HA3  B GLY   A 1 130 ? 15.195 0.488   -2.306  0.28 15.26 ?  130 GLY   A HA3  1 
ATOM   2616 N  N    A ILE   A 1 131 ? 15.914 2.248   -4.345  0.72 12.38 ?  131 ILE   A N    1 
ATOM   2617 N  N    B ILE   A 1 131 ? 15.881 2.091   -4.007  0.28 12.97 ?  131 ILE   A N    1 
ATOM   2618 C  CA   A ILE   A 1 131 ? 16.482 2.986   -5.471  0.72 12.02 ?  131 ILE   A CA   1 
ATOM   2619 C  CA   B ILE   A 1 131 ? 16.377 2.941   -5.084  0.28 12.89 ?  131 ILE   A CA   1 
ATOM   2620 C  C    A ILE   A 1 131 ? 17.497 2.188   -6.279  0.72 11.68 ?  131 ILE   A C    1 
ATOM   2621 C  C    B ILE   A 1 131 ? 17.357 2.227   -6.005  0.28 12.48 ?  131 ILE   A C    1 
ATOM   2622 O  O    A ILE   A 1 131 ? 17.910 2.658   -7.347  0.72 12.64 ?  131 ILE   A O    1 
ATOM   2623 O  O    B ILE   A 1 131 ? 17.736 2.791   -7.038  0.28 12.68 ?  131 ILE   A O    1 
ATOM   2624 C  CB   A ILE   A 1 131 ? 17.045 4.361   -5.049  0.72 12.66 ?  131 ILE   A CB   1 
ATOM   2625 C  CB   B ILE   A 1 131 ? 16.992 4.246   -4.531  0.28 13.42 ?  131 ILE   A CB   1 
ATOM   2626 C  CG1  A ILE   A 1 131 ? 18.280 4.205   -4.155  0.72 14.17 ?  131 ILE   A CG1  1 
ATOM   2627 C  CG1  B ILE   A 1 131 ? 18.237 3.946   -3.693  0.28 13.99 ?  131 ILE   A CG1  1 
ATOM   2628 C  CG2  A ILE   A 1 131 ? 15.960 5.183   -4.361  0.72 12.97 ?  131 ILE   A CG2  1 
ATOM   2629 C  CG2  B ILE   A 1 131 ? 15.966 5.011   -3.700  0.28 13.45 ?  131 ILE   A CG2  1 
ATOM   2630 C  CD1  A ILE   A 1 131 ? 18.950 5.527   -3.804  0.72 15.21 ?  131 ILE   A CD1  1 
ATOM   2631 C  CD1  B ILE   A 1 131 ? 18.936 5.189   -3.181  0.28 14.37 ?  131 ILE   A CD1  1 
ATOM   2632 H  H    A ILE   A 1 131 ? 16.126 2.554   -3.571  0.72 14.85 ?  131 ILE   A H    1 
ATOM   2633 H  H    B ILE   A 1 131 ? 16.156 2.312   -3.226  0.28 15.57 ?  131 ILE   A H    1 
ATOM   2634 H  HA   A ILE   A 1 131 ? 15.756 3.170   -6.077  0.72 14.43 ?  131 ILE   A HA   1 
ATOM   2635 H  HA   B ILE   A 1 131 ? 15.619 3.203   -5.627  0.28 15.47 ?  131 ILE   A HA   1 
ATOM   2636 H  HB   A ILE   A 1 131 ? 17.313 4.830   -5.852  0.72 15.20 ?  131 ILE   A HB   1 
ATOM   2637 H  HB   B ILE   A 1 131 ? 17.252 4.804   -5.281  0.28 16.11 ?  131 ILE   A HB   1 
ATOM   2638 H  HG12 A ILE   A 1 131 ? 18.017 3.774   -3.327  0.72 17.01 ?  131 ILE   A HG12 1 
ATOM   2639 H  HG12 B ILE   A 1 131 ? 17.976 3.415   -2.926  0.28 16.79 ?  131 ILE   A HG12 1 
ATOM   2640 H  HG13 A ILE   A 1 131 ? 18.938 3.656   -4.614  0.72 17.01 ?  131 ILE   A HG13 1 
ATOM   2641 H  HG13 B ILE   A 1 131 ? 18.872 3.455   -4.235  0.28 16.79 ?  131 ILE   A HG13 1 
ATOM   2642 H  HG21 A ILE   A 1 131 ? 16.279 6.089   -4.238  0.72 15.57 ?  131 ILE   A HG21 1 
ATOM   2643 H  HG21 B ILE   A 1 131 ? 16.313 5.895   -3.502  0.28 16.15 ?  131 ILE   A HG21 1 
ATOM   2644 H  HG22 A ILE   A 1 131 ? 15.167 5.186   -4.921  0.72 15.57 ?  131 ILE   A HG22 1 
ATOM   2645 H  HG22 B ILE   A 1 131 ? 15.143 5.085   -4.206  0.28 16.15 ?  131 ILE   A HG22 1 
ATOM   2646 H  HG23 A ILE   A 1 131 ? 15.755 4.781   -3.503  0.72 15.57 ?  131 ILE   A HG23 1 
ATOM   2647 H  HG23 B ILE   A 1 131 ? 15.805 4.526   -2.875  0.28 16.15 ?  131 ILE   A HG23 1 
ATOM   2648 H  HD11 A ILE   A 1 131 ? 19.778 5.345   -3.331  0.72 18.26 ?  131 ILE   A HD11 1 
ATOM   2649 H  HD11 B ILE   A 1 131 ? 19.783 4.933   -2.785  0.28 17.24 ?  131 ILE   A HD11 1 
ATOM   2650 H  HD12 A ILE   A 1 131 ? 19.137 6.013   -4.622  0.72 18.26 ?  131 ILE   A HD12 1 
ATOM   2651 H  HD12 B ILE   A 1 131 ? 19.088 5.795   -3.924  0.28 17.24 ?  131 ILE   A HD12 1 
ATOM   2652 H  HD13 A ILE   A 1 131 ? 18.354 6.044   -3.240  0.72 18.26 ?  131 ILE   A HD13 1 
ATOM   2653 H  HD13 B ILE   A 1 131 ? 18.376 5.618   -2.515  0.28 17.24 ?  131 ILE   A HD13 1 
ATOM   2654 N  N    A PHE   A 1 132 ? 17.908 0.999   -5.818  0.72 11.05 ?  132 PHE   A N    1 
ATOM   2655 N  N    B PHE   A 1 132 ? 17.780 1.003   -5.666  0.28 12.17 ?  132 PHE   A N    1 
ATOM   2656 C  CA   A PHE   A 1 132 ? 18.741 0.135   -6.650  0.72 11.42 ?  132 PHE   A CA   1 
ATOM   2657 C  CA   B PHE   A 1 132 ? 18.688 0.249   -6.524  0.28 12.16 ?  132 PHE   A CA   1 
ATOM   2658 C  C    A PHE   A 1 132 ? 17.935 -0.629  -7.702  0.72 12.40 ?  132 PHE   A C    1 
ATOM   2659 C  C    B PHE   A 1 132 ? 17.980 -0.471  -7.671  0.28 12.59 ?  132 PHE   A C    1 
ATOM   2660 O  O    A PHE   A 1 132 ? 18.532 -1.306  -8.546  0.72 12.72 ?  132 PHE   A O    1 
ATOM   2661 O  O    B PHE   A 1 132 ? 18.656 -0.929  -8.598  0.28 12.90 ?  132 PHE   A O    1 
ATOM   2662 C  CB   A PHE   A 1 132 ? 19.561 -0.843  -5.798  0.72 11.59 ?  132 PHE   A CB   1 
ATOM   2663 C  CB   B PHE   A 1 132 ? 19.531 -0.738  -5.703  0.28 12.04 ?  132 PHE   A CB   1 
ATOM   2664 C  CG   A PHE   A 1 132 ? 20.774 -0.232  -5.128  0.72 11.35 ?  132 PHE   A CG   1 
ATOM   2665 C  CG   B PHE   A 1 132 ? 20.777 -0.132  -5.100  0.28 12.11 ?  132 PHE   A CG   1 
ATOM   2666 C  CD1  A PHE   A 1 132 ? 20.645 0.798   -4.215  0.72 12.59 ?  132 PHE   A CD1  1 
ATOM   2667 C  CD1  B PHE   A 1 132 ? 20.688 0.838   -4.116  0.28 12.69 ?  132 PHE   A CD1  1 
ATOM   2668 C  CD2  A PHE   A 1 132 ? 22.044 -0.733  -5.381  0.72 11.95 ?  132 PHE   A CD2  1 
ATOM   2669 C  CD2  B PHE   A 1 132 ? 22.037 -0.548  -5.506  0.28 12.25 ?  132 PHE   A CD2  1 
ATOM   2670 C  CE1  A PHE   A 1 132 ? 21.760 1.334   -3.588  0.72 12.71 ?  132 PHE   A CE1  1 
ATOM   2671 C  CE1  B PHE   A 1 132 ? 21.829 1.389   -3.556  0.28 12.80 ?  132 PHE   A CE1  1 
ATOM   2672 C  CE2  A PHE   A 1 132 ? 23.158 -0.205  -4.757  0.72 12.33 ?  132 PHE   A CE2  1 
ATOM   2673 C  CE2  B PHE   A 1 132 ? 23.183 -0.000  -4.948  0.28 12.75 ?  132 PHE   A CE2  1 
ATOM   2674 C  CZ   A PHE   A 1 132 ? 23.015 0.832   -3.860  0.72 12.41 ?  132 PHE   A CZ   1 
ATOM   2675 C  CZ   B PHE   A 1 132 ? 23.076 0.969   -3.972  0.28 12.86 ?  132 PHE   A CZ   1 
ATOM   2676 H  H    A PHE   A 1 132 ? 17.725 0.677   -5.036  0.72 13.26 ?  132 PHE   A H    1 
ATOM   2677 H  H    B PHE   A 1 132 ? 17.557 0.595   -4.944  0.28 14.61 ?  132 PHE   A H    1 
ATOM   2678 H  HA   A PHE   A 1 132 ? 19.374 0.694   -7.120  0.72 13.71 ?  132 PHE   A HA   1 
ATOM   2679 H  HA   B PHE   A 1 132 ? 19.304 0.876   -6.928  0.28 14.59 ?  132 PHE   A HA   1 
ATOM   2680 H  HB2  A PHE   A 1 132 ? 18.991 -1.199  -5.097  0.72 13.92 ?  132 PHE   A HB2  1 
ATOM   2681 H  HB2  B PHE   A 1 132 ? 18.991 -1.083  -4.976  0.28 14.46 ?  132 PHE   A HB2  1 
ATOM   2682 H  HB3  A PHE   A 1 132 ? 19.870 -1.572  -6.365  0.72 13.92 ?  132 PHE   A HB3  1 
ATOM   2683 H  HB3  B PHE   A 1 132 ? 19.808 -1.468  -6.280  0.28 14.46 ?  132 PHE   A HB3  1 
ATOM   2684 H  HD1  A PHE   A 1 132 ? 19.803 1.140   -4.024  0.72 15.11 ?  132 PHE   A HD1  1 
ATOM   2685 H  HD1  B PHE   A 1 132 ? 19.852 1.126   -3.831  0.28 15.24 ?  132 PHE   A HD1  1 
ATOM   2686 H  HD2  A PHE   A 1 132 ? 22.148 -1.438  -5.986  0.72 14.34 ?  132 PHE   A HD2  1 
ATOM   2687 H  HD2  B PHE   A 1 132 ? 22.118 -1.203  -6.163  0.28 14.70 ?  132 PHE   A HD2  1 
ATOM   2688 H  HE1  A PHE   A 1 132 ? 21.664 2.035   -2.983  0.72 15.26 ?  132 PHE   A HE1  1 
ATOM   2689 H  HE1  B PHE   A 1 132 ? 21.757 2.042   -2.899  0.28 15.36 ?  132 PHE   A HE1  1 
ATOM   2690 H  HE2  A PHE   A 1 132 ? 24.002 -0.547  -4.949  0.72 14.80 ?  132 PHE   A HE2  1 
ATOM   2691 H  HE2  B PHE   A 1 132 ? 24.024 -0.287  -5.231  0.28 15.31 ?  132 PHE   A HE2  1 
ATOM   2692 H  HZ   A PHE   A 1 132 ? 23.765 1.192   -3.447  0.72 14.89 ?  132 PHE   A HZ   1 
ATOM   2693 H  HZ   B PHE   A 1 132 ? 23.845 1.338   -3.598  0.28 15.43 ?  132 PHE   A HZ   1 
ATOM   2694 N  N    A GLY   A 1 133 ? 16.603 -0.558  -7.663  0.72 12.65 ?  133 GLY   A N    1 
ATOM   2695 N  N    B GLY   A 1 133 ? 16.651 -0.591  -7.640  0.28 12.57 ?  133 GLY   A N    1 
ATOM   2696 C  CA   A GLY   A 1 133 ? 15.780 -0.921  -8.801  0.72 13.52 ?  133 GLY   A CA   1 
ATOM   2697 C  CA   B GLY   A 1 133 ? 15.875 -0.957  -8.810  0.28 12.63 ?  133 GLY   A CA   1 
ATOM   2698 C  C    A GLY   A 1 133 ? 15.463 -2.387  -9.003  0.72 13.44 ?  133 GLY   A C    1 
ATOM   2699 C  C    B GLY   A 1 133 ? 15.269 -2.346  -8.802  0.28 12.23 ?  133 GLY   A C    1 
ATOM   2700 O  O    A GLY   A 1 133 ? 14.814 -2.714  -10.005 0.72 14.29 ?  133 GLY   A O    1 
ATOM   2701 O  O    B GLY   A 1 133 ? 14.365 -2.606  -9.608  0.28 12.37 ?  133 GLY   A O    1 
ATOM   2702 H  H    A GLY   A 1 133 ? 16.150 -0.302  -6.975  0.72 15.18 ?  133 GLY   A H    1 
ATOM   2703 H  H    B GLY   A 1 133 ? 16.172 -0.461  -6.937  0.28 15.09 ?  133 GLY   A H    1 
ATOM   2704 H  HA2  A GLY   A 1 133 ? 14.933 -0.460  -8.727  0.72 16.23 ?  133 GLY   A HA2  1 
ATOM   2705 H  HA2  B GLY   A 1 133 ? 15.148 -0.327  -8.909  0.28 15.16 ?  133 GLY   A HA2  1 
ATOM   2706 H  HA3  A GLY   A 1 133 ? 16.218 -0.612  -9.608  0.72 16.23 ?  133 GLY   A HA3  1 
ATOM   2707 H  HA3  B GLY   A 1 133 ? 16.440 -0.886  -9.597  0.28 15.16 ?  133 GLY   A HA3  1 
ATOM   2708 N  N    A ALA   A 1 134 ? 15.893 -3.283  -8.119  0.72 13.08 ?  134 ALA   A N    1 
ATOM   2709 N  N    B ALA   A 1 134 ? 15.723 -3.246  -7.936  0.28 12.39 ?  134 ALA   A N    1 
ATOM   2710 C  CA   A ALA   A 1 134 ? 15.543 -4.686  -8.278  0.72 13.65 ?  134 ALA   A CA   1 
ATOM   2711 C  CA   B ALA   A 1 134 ? 15.266 -4.627  -7.997  0.28 12.78 ?  134 ALA   A CA   1 
ATOM   2712 C  C    A ALA   A 1 134 ? 14.184 -4.976  -7.639  0.72 13.72 ?  134 ALA   A C    1 
ATOM   2713 C  C    B ALA   A 1 134 ? 13.966 -4.820  -7.225  0.28 12.55 ?  134 ALA   A C    1 
ATOM   2714 O  O    A ALA   A 1 134 ? 13.660 -4.192  -6.845  0.72 14.73 ?  134 ALA   A O    1 
ATOM   2715 O  O    B ALA   A 1 134 ? 13.614 -4.043  -6.335  0.28 12.60 ?  134 ALA   A O    1 
ATOM   2716 C  CB   A ALA   A 1 134 ? 16.623 -5.595  -7.686  0.72 14.32 ?  134 ALA   A CB   1 
ATOM   2717 C  CB   B ALA   A 1 134 ? 16.324 -5.584  -7.450  0.28 13.27 ?  134 ALA   A CB   1 
ATOM   2718 H  H    A ALA   A 1 134 ? 16.391 -3.106  -7.431  0.72 15.70 ?  134 ALA   A H    1 
ATOM   2719 H  H    B ALA   A 1 134 ? 16.290 -3.080  -7.310  0.28 14.87 ?  134 ALA   A H    1 
ATOM   2720 H  HA   A ALA   A 1 134 ? 15.478 -4.886  -9.222  0.72 16.38 ?  134 ALA   A HA   1 
ATOM   2721 H  HA   B ALA   A 1 134 ? 15.099 -4.856  -8.923  0.28 15.34 ?  134 ALA   A HA   1 
ATOM   2722 H  HB1  A ALA   A 1 134 ? 16.365 -6.521  -7.821  0.72 17.19 ?  134 ALA   A HB1  1 
ATOM   2723 H  HB1  B ALA   A 1 134 ? 15.994 -6.493  -7.538  0.28 15.93 ?  134 ALA   A HB1  1 
ATOM   2724 H  HB2  A ALA   A 1 134 ? 17.467 -5.421  -8.137  0.72 17.19 ?  134 ALA   A HB2  1 
ATOM   2725 H  HB2  B ALA   A 1 134 ? 17.138 -5.474  -7.961  0.28 15.93 ?  134 ALA   A HB2  1 
ATOM   2726 H  HB3  A ALA   A 1 134 ? 16.713 -5.410  -6.739  0.72 17.19 ?  134 ALA   A HB3  1 
ATOM   2727 H  HB3  B ALA   A 1 134 ? 16.482 -5.377  -6.517  0.28 15.93 ?  134 ALA   A HB3  1 
ATOM   2728 N  N    A ASP   A 1 135 ? 13.618 -6.122  -8.004  0.72 14.37 ?  135 ASP   A N    1 
ATOM   2729 N  N    B ASP   A 1 135 ? 13.258 -5.885  -7.582  0.28 12.38 ?  135 ASP   A N    1 
ATOM   2730 C  CA   A ASP   A 1 135 ? 12.358 -6.581  -7.420  0.72 15.29 ?  135 ASP   A CA   1 
ATOM   2731 C  CA   B ASP   A 1 135 ? 12.041 -6.277  -6.890  0.28 12.12 ?  135 ASP   A CA   1 
ATOM   2732 C  C    A ASP   A 1 135 ? 12.619 -7.041  -5.992  0.72 14.59 ?  135 ASP   A C    1 
ATOM   2733 C  C    B ASP   A 1 135 ? 12.402 -6.787  -5.500  0.28 11.39 ?  135 ASP   A C    1 
ATOM   2734 O  O    A ASP   A 1 135 ? 13.398 -7.984  -5.792  0.72 14.58 ?  135 ASP   A O    1 
ATOM   2735 O  O    B ASP   A 1 135 ? 13.154 -7.766  -5.386  0.28 11.33 ?  135 ASP   A O    1 
ATOM   2736 C  CB   A ASP   A 1 135 ? 11.827 -7.748  -8.250  0.72 17.84 ?  135 ASP   A CB   1 
ATOM   2737 C  CB   B ASP   A 1 135 ? 11.373 -7.390  -7.688  0.28 12.74 ?  135 ASP   A CB   1 
ATOM   2738 C  CG   A ASP   A 1 135 ? 10.528 -8.345  -7.698  0.72 19.84 ?  135 ASP   A CG   1 
ATOM   2739 C  CG   B ASP   A 1 135 ? 9.983  -7.727  -7.184  0.28 13.92 ?  135 ASP   A CG   1 
ATOM   2740 O  OD1  A ASP   A 1 135 ? 10.039 -7.900  -6.641  0.72 20.29 ?  135 ASP   A OD1  1 
ATOM   2741 O  OD1  B ASP   A 1 135 ? 9.668  -7.392  -6.022  0.28 13.71 ?  135 ASP   A OD1  1 
ATOM   2742 O  OD2  A ASP   A 1 135 ? 9.987  -9.268  -8.344  0.72 22.36 -1 135 ASP   A OD2  1 
ATOM   2743 O  OD2  B ASP   A 1 135 ? 9.211  -8.338  -7.955  0.28 14.85 -1 135 ASP   A OD2  1 
ATOM   2744 H  H    A ASP   A 1 135 ? 13.938 -6.653  -8.598  0.72 17.25 ?  135 ASP   A H    1 
ATOM   2745 H  H    B ASP   A 1 135 ? 13.459 -6.402  -8.234  0.28 14.86 ?  135 ASP   A H    1 
ATOM   2746 H  HA   A ASP   A 1 135 ? 11.705 -5.863  -7.431  0.72 18.35 ?  135 ASP   A HA   1 
ATOM   2747 H  HA   B ASP   A 1 135 ? 11.428 -5.521  -6.832  0.28 14.55 ?  135 ASP   A HA   1 
ATOM   2748 H  HB2  A ASP   A 1 135 ? 11.648 -7.435  -9.149  0.72 21.42 ?  135 ASP   A HB2  1 
ATOM   2749 H  HB2  B ASP   A 1 135 ? 11.302 -7.113  -8.613  0.28 15.29 ?  135 ASP   A HB2  1 
ATOM   2750 H  HB3  A ASP   A 1 135 ? 12.500 -8.447  -8.269  0.72 21.42 ?  135 ASP   A HB3  1 
ATOM   2751 H  HB3  B ASP   A 1 135 ? 11.915 -8.190  -7.619  0.28 15.29 ?  135 ASP   A HB3  1 
ATOM   2752 N  N    A PRO   A 1 136 ? 12.015 -6.418  -4.978  0.72 14.51 ?  136 PRO   A N    1 
ATOM   2753 N  N    B PRO   A 1 136 ? 11.908 -6.167  -4.426  0.28 10.84 ?  136 PRO   A N    1 
ATOM   2754 C  CA   A PRO   A 1 136 ? 12.273 -6.859  -3.597  0.72 14.73 ?  136 PRO   A CA   1 
ATOM   2755 C  CA   B PRO   A 1 136 ? 12.233 -6.672  -3.080  0.28 11.09 ?  136 PRO   A CA   1 
ATOM   2756 C  C    A PRO   A 1 136 ? 11.844 -8.287  -3.314  0.72 14.00 ?  136 PRO   A C    1 
ATOM   2757 C  C    B PRO   A 1 136 ? 11.834 -8.122  -2.857  0.28 11.14 ?  136 PRO   A C    1 
ATOM   2758 O  O    A PRO   A 1 136 ? 12.446 -8.940  -2.455  0.72 13.73 ?  136 PRO   A O    1 
ATOM   2759 O  O    B PRO   A 1 136 ? 12.451 -8.803  -2.029  0.28 10.54 ?  136 PRO   A O    1 
ATOM   2760 C  CB   A PRO   A 1 136 ? 11.486 -5.846  -2.753  0.72 15.44 ?  136 PRO   A CB   1 
ATOM   2761 C  CB   B PRO   A 1 136 ? 11.483 -5.703  -2.151  0.28 11.24 ?  136 PRO   A CB   1 
ATOM   2762 C  CG   A PRO   A 1 136 ? 10.419 -5.338  -3.675  0.72 16.25 ?  136 PRO   A CG   1 
ATOM   2763 C  CG   B PRO   A 1 136 ? 10.425 -5.077  -3.009  0.28 11.48 ?  136 PRO   A CG   1 
ATOM   2764 C  CD   A PRO   A 1 136 ? 11.036 -5.318  -5.037  0.72 15.45 ?  136 PRO   A CD   1 
ATOM   2765 C  CD   B PRO   A 1 136 ? 11.030 -4.986  -4.376  0.28 10.62 ?  136 PRO   A CD   1 
ATOM   2766 H  HA   A PRO   A 1 136 ? 13.219 -6.768  -3.391  0.72 17.68 ?  136 PRO   A HA   1 
ATOM   2767 H  HA   B PRO   A 1 136 ? 13.183 -6.579  -2.912  0.28 13.32 ?  136 PRO   A HA   1 
ATOM   2768 H  HB2  A PRO   A 1 136 ? 11.095 -6.294  -1.985  0.72 18.53 ?  136 PRO   A HB2  1 
ATOM   2769 H  HB2  B PRO   A 1 136 ? 11.085 -6.183  -1.408  0.28 13.49 ?  136 PRO   A HB2  1 
ATOM   2770 H  HB3  A PRO   A 1 136 ? 12.073 -5.128  -2.471  0.72 18.53 ?  136 PRO   A HB3  1 
ATOM   2771 H  HB3  B PRO   A 1 136 ? 12.094 -5.021  -1.831  0.28 13.49 ?  136 PRO   A HB3  1 
ATOM   2772 H  HG2  A PRO   A 1 136 ? 9.660  -5.938  -3.653  0.72 19.51 ?  136 PRO   A HG2  1 
ATOM   2773 H  HG2  B PRO   A 1 136 ? 9.637  -5.641  -3.022  0.28 13.78 ?  136 PRO   A HG2  1 
ATOM   2774 H  HG3  A PRO   A 1 136 ? 10.160 -4.444  -3.407  0.72 19.51 ?  136 PRO   A HG3  1 
ATOM   2775 H  HG3  B PRO   A 1 136 ? 10.207 -4.192  -2.676  0.28 13.78 ?  136 PRO   A HG3  1 
ATOM   2776 H  HD2  A PRO   A 1 136 ? 10.362 -5.504  -5.714  0.72 18.54 ?  136 PRO   A HD2  1 
ATOM   2777 H  HD2  B PRO   A 1 136 ? 10.334 -5.049  -5.052  0.28 12.75 ?  136 PRO   A HD2  1 
ATOM   2778 H  HD3  A PRO   A 1 136 ? 11.481 -4.473  -5.202  0.72 18.54 ?  136 PRO   A HD3  1 
ATOM   2779 H  HD3  B PRO   A 1 136 ? 11.546 -4.169  -4.473  0.28 12.75 ?  136 PRO   A HD3  1 
ATOM   2780 N  N    A ILE   A 1 137 ? 10.798 -8.785  -3.978  0.72 14.30 ?  137 ILE   A N    1 
ATOM   2781 N  N    B ILE   A 1 137 ? 10.818 -8.616  -3.568  0.28 11.80 ?  137 ILE   A N    1 
ATOM   2782 C  CA   A ILE   A 1 137 ? 10.427 -10.187 -3.809  0.72 15.09 ?  137 ILE   A CA   1 
ATOM   2783 C  CA   B ILE   A 1 137 ? 10.424 -10.017 -3.426  0.28 12.43 ?  137 ILE   A CA   1 
ATOM   2784 C  C    A ILE   A 1 137 ? 11.586 -11.080 -4.216  0.72 14.72 ?  137 ILE   A C    1 
ATOM   2785 C  C    B ILE   A 1 137 ? 11.551 -10.932 -3.890  0.28 12.29 ?  137 ILE   A C    1 
ATOM   2786 O  O    A ILE   A 1 137 ? 11.884 -12.084 -3.557  0.72 14.90 ?  137 ILE   A O    1 
ATOM   2787 O  O    B ILE   A 1 137 ? 11.894 -11.916 -3.222  0.28 12.19 ?  137 ILE   A O    1 
ATOM   2788 C  CB   A ILE   A 1 137 ? 9.147  -10.504 -4.605  0.72 16.52 ?  137 ILE   A CB   1 
ATOM   2789 C  CB   B ILE   A 1 137 ? 9.119  -10.290 -4.196  0.28 13.10 ?  137 ILE   A CB   1 
ATOM   2790 C  CG1  A ILE   A 1 137 ? 7.954  -9.729  -4.034  0.72 18.33 ?  137 ILE   A CG1  1 
ATOM   2791 C  CG1  B ILE   A 1 137 ? 8.011  -9.323  -3.763  0.28 14.07 ?  137 ILE   A CG1  1 
ATOM   2792 C  CG2  A ILE   A 1 137 ? 8.872  -12.010 -4.598  0.72 16.78 ?  137 ILE   A CG2  1 
ATOM   2793 C  CG2  B ILE   A 1 137 ? 8.679  -11.733 -3.986  0.28 13.26 ?  137 ILE   A CG2  1 
ATOM   2794 C  CD1  A ILE   A 1 137 ? 6.665  -9.935  -4.796  0.72 19.82 ?  137 ILE   A CD1  1 
ATOM   2795 C  CD1  B ILE   A 1 137 ? 6.796  -9.372  -4.656  0.28 14.67 ?  137 ILE   A CD1  1 
ATOM   2796 H  H    A ILE   A 1 137 ? 10.307 -8.342  -4.521  0.72 17.16 ?  137 ILE   A H    1 
ATOM   2797 H  H    B ILE   A 1 137 ? 10.348 -8.159  -4.126  0.28 14.16 ?  137 ILE   A H    1 
ATOM   2798 H  HA   A ILE   A 1 137 ? 10.248 -10.355 -2.874  0.72 18.11 ?  137 ILE   A HA   1 
ATOM   2799 H  HA   B ILE   A 1 137 ? 10.257 -10.200 -2.489  0.28 14.91 ?  137 ILE   A HA   1 
ATOM   2800 H  HB   A ILE   A 1 137 ? 9.278  -10.220 -5.521  0.72 19.83 ?  137 ILE   A HB   1 
ATOM   2801 H  HB   B ILE   A 1 137 ? 9.288  -10.154 -5.139  0.28 15.73 ?  137 ILE   A HB   1 
ATOM   2802 H  HG12 A ILE   A 1 137 ? 7.808  -10.008 -3.115  0.72 22.00 ?  137 ILE   A HG12 1 
ATOM   2803 H  HG12 B ILE   A 1 137 ? 7.731  -9.550  -2.863  0.28 16.89 ?  137 ILE   A HG12 1 
ATOM   2804 H  HG13 A ILE   A 1 137 ? 8.163  -8.776  -4.053  0.72 22.00 ?  137 ILE   A HG13 1 
ATOM   2805 H  HG13 B ILE   A 1 137 ? 8.349  -8.413  -3.783  0.28 16.89 ?  137 ILE   A HG13 1 
ATOM   2806 H  HG21 A ILE   A 1 137 ? 8.109  -12.200 -5.162  0.72 20.14 ?  137 ILE   A HG21 1 
ATOM   2807 H  HG21 B ILE   A 1 137 ? 7.799  -11.855 -4.372  0.28 15.92 ?  137 ILE   A HG21 1 
ATOM   2808 H  HG22 A ILE   A 1 137 ? 9.639  -12.482 -4.946  0.72 20.14 ?  137 ILE   A HG22 1 
ATOM   2809 H  HG22 B ILE   A 1 137 ? 9.315  -12.322 -4.419  0.28 15.92 ?  137 ILE   A HG22 1 
ATOM   2810 H  HG23 A ILE   A 1 137 ? 8.691  -12.289 -3.689  0.72 20.14 ?  137 ILE   A HG23 1 
ATOM   2811 H  HG23 B ILE   A 1 137 ? 8.651  -11.917 -3.034  0.28 15.92 ?  137 ILE   A HG23 1 
ATOM   2812 H  HD11 A ILE   A 1 137 ? 5.939  -9.686  -4.214  0.72 23.78 ?  137 ILE   A HD11 1 
ATOM   2813 H  HD11 B ILE   A 1 137 ? 6.553  -8.470  -4.907  0.28 17.60 ?  137 ILE   A HD11 1 
ATOM   2814 H  HD12 A ILE   A 1 137 ? 6.676  -9.372  -5.586  0.72 23.78 ?  137 ILE   A HD12 1 
ATOM   2815 H  HD12 B ILE   A 1 137 ? 7.010  -9.891  -5.450  0.28 17.60 ?  137 ILE   A HD12 1 
ATOM   2816 H  HD13 A ILE   A 1 137 ? 6.569  -10.862 -5.050  0.72 23.78 ?  137 ILE   A HD13 1 
ATOM   2817 H  HD13 B ILE   A 1 137 ? 6.068  -9.796  -4.175  0.28 17.60 ?  137 ILE   A HD13 1 
ATOM   2818 N  N    A HIS   A 1 138 ? 12.250 -10.729 -5.316  0.72 14.95 ?  138 HIS   A N    1 
ATOM   2819 N  N    B HIS   A 1 138 ? 12.138 -10.622 -5.049  0.28 12.82 ?  138 HIS   A N    1 
ATOM   2820 C  CA   A HIS   A 1 138 ? 13.426 -11.474 -5.734  0.72 14.28 ?  138 HIS   A CA   1 
ATOM   2821 C  CA   B HIS   A 1 138 ? 13.245 -11.422 -5.564  0.28 13.05 ?  138 HIS   A CA   1 
ATOM   2822 C  C    A HIS   A 1 138 ? 14.557 -11.337 -4.722  0.72 13.63 ?  138 HIS   A C    1 
ATOM   2823 C  C    B HIS   A 1 138 ? 14.446 -11.341 -4.634  0.28 12.89 ?  138 HIS   A C    1 
ATOM   2824 O  O    A HIS   A 1 138 ? 15.225 -12.326 -4.399  0.72 14.14 ?  138 HIS   A O    1 
ATOM   2825 O  O    B HIS   A 1 138 ? 15.068 -12.358 -4.309  0.28 13.10 ?  138 HIS   A O    1 
ATOM   2826 C  CB   A HIS   A 1 138 ? 13.859 -11.031 -7.128  0.72 15.30 ?  138 HIS   A CB   1 
ATOM   2827 C  CB   B HIS   A 1 138 ? 13.620 -10.947 -6.969  0.28 13.32 ?  138 HIS   A CB   1 
ATOM   2828 C  CG   A HIS   A 1 138 ? 15.090 -11.724 -7.611  0.72 16.09 ?  138 HIS   A CG   1 
ATOM   2829 C  CG   B HIS   A 1 138 ? 14.916 -11.507 -7.469  0.28 13.74 ?  138 HIS   A CG   1 
ATOM   2830 N  ND1  A HIS   A 1 138 ? 15.155 -13.090 -7.788  0.72 17.58 ?  138 HIS   A ND1  1 
ATOM   2831 N  ND1  B HIS   A 1 138 ? 15.045 -12.805 -7.912  0.28 14.67 ?  138 HIS   A ND1  1 
ATOM   2832 C  CD2  A HIS   A 1 138 ? 16.314 -11.243 -7.926  0.72 16.42 ?  138 HIS   A CD2  1 
ATOM   2833 C  CD2  B HIS   A 1 138 ? 16.142 -10.944 -7.590  0.28 13.73 ?  138 HIS   A CD2  1 
ATOM   2834 C  CE1  A HIS   A 1 138 ? 16.363 -13.418 -8.209  0.72 17.48 ?  138 HIS   A CE1  1 
ATOM   2835 C  CE1  B HIS   A 1 138 ? 16.294 -13.018 -8.287  0.28 14.58 ?  138 HIS   A CE1  1 
ATOM   2836 N  NE2  A HIS   A 1 138 ? 17.087 -12.317 -8.298  0.72 16.56 ?  138 HIS   A NE2  1 
ATOM   2837 N  NE2  B HIS   A 1 138 ? 16.981 -11.905 -8.101  0.28 14.07 ?  138 HIS   A NE2  1 
ATOM   2838 H  H    A HIS   A 1 138 ? 12.038 -10.069 -5.834  0.72 17.94 ?  138 HIS   A H    1 
ATOM   2839 H  H    B HIS   A 1 138 ? 11.919 -9.953  -5.545  0.28 15.39 ?  138 HIS   A H    1 
ATOM   2840 H  HA   A HIS   A 1 138 ? 13.191 -12.411 -5.790  0.72 17.14 ?  138 HIS   A HA   1 
ATOM   2841 H  HA   B HIS   A 1 138 ? 12.968 -12.347 -5.619  0.28 15.66 ?  138 HIS   A HA   1 
ATOM   2842 H  HB2  A HIS   A 1 138 ? 13.140 -11.224 -7.757  0.72 18.36 ?  138 HIS   A HB2  1 
ATOM   2843 H  HB2  B HIS   A 1 138 ? 12.921 -11.219 -7.587  0.28 15.99 ?  138 HIS   A HB2  1 
ATOM   2844 H  HB3  A HIS   A 1 138 ? 14.034 -10.078 -7.118  0.72 18.36 ?  138 HIS   A HB3  1 
ATOM   2845 H  HB3  B HIS   A 1 138 ? 13.695 -9.980  -6.965  0.28 15.99 ?  138 HIS   A HB3  1 
ATOM   2846 H  HD1  A HIS   A 1 138 ? 14.505 -13.638 -7.657  0.72 21.10 ?  138 HIS   A HD1  1 
ATOM   2847 H  HD2  A HIS   A 1 138 ? 16.577 -10.352 -7.901  0.72 19.71 ?  138 HIS   A HD2  1 
ATOM   2848 H  HD2  B HIS   A 1 138 ? 16.372 -10.070 -7.369  0.28 16.48 ?  138 HIS   A HD2  1 
ATOM   2849 H  HE1  A HIS   A 1 138 ? 16.654 -14.278 -8.404  0.72 20.98 ?  138 HIS   A HE1  1 
ATOM   2850 H  HE1  B HIS   A 1 138 ? 16.634 -13.816 -8.624  0.28 17.49 ?  138 HIS   A HE1  1 
ATOM   2851 H  HE2  B HIS   A 1 138 ? 17.817 -11.797 -8.273  0.28 16.89 ?  138 HIS   A HE2  1 
ATOM   2852 N  N    . SER   A 1 139 ? 14.785 -10.129 -4.199  1.00 13.07 ?  139 SER   A N    1 
ATOM   2853 C  CA   . SER   A 1 139 ? 15.864 -9.956  -3.242  1.00 12.67 ?  139 SER   A CA   1 
ATOM   2854 C  C    . SER   A 1 139 ? 15.654 -10.813 -2.001  1.00 12.25 ?  139 SER   A C    1 
ATOM   2855 O  O    . SER   A 1 139 ? 16.606 -11.406 -1.484  1.00 12.25 ?  139 SER   A O    1 
ATOM   2856 C  CB   . SER   A 1 139 ? 15.987 -8.486  -2.863  1.00 12.81 ?  139 SER   A CB   1 
ATOM   2857 O  OG   . SER   A 1 139 ? 17.087 -8.326  -1.988  1.00 12.86 ?  139 SER   A OG   1 
ATOM   2858 H  H    A SER   A 1 139 ? 14.339 -9.416  -4.379  0.72 15.68 ?  139 SER   A H    1 
ATOM   2859 H  H    B SER   A 1 139 ? 14.399 -9.398  -4.437  0.28 15.68 ?  139 SER   A H    1 
ATOM   2860 H  HA   . SER   A 1 139 ? 16.700 -10.224 -3.652  1.00 15.20 ?  139 SER   A HA   1 
ATOM   2861 H  HB2  . SER   A 1 139 ? 16.132 -7.951  -3.662  1.00 15.37 ?  139 SER   A HB2  1 
ATOM   2862 H  HB3  . SER   A 1 139 ? 15.177 -8.195  -2.410  1.00 15.37 ?  139 SER   A HB3  1 
ATOM   2863 H  HG   . SER   A 1 139 ? 17.173 -7.516  -1.769  1.00 15.44 ?  139 SER   A HG   1 
ATOM   2864 N  N    . LEU   A 1 140 ? 14.422 -10.875 -1.495  1.00 12.56 ?  140 LEU   A N    1 
ATOM   2865 C  CA   . LEU   A 1 140 ? 14.152 -11.708 -0.325  1.00 12.35 ?  140 LEU   A CA   1 
ATOM   2866 C  C    . LEU   A 1 140 ? 14.412 -13.181 -0.627  1.00 12.07 ?  140 LEU   A C    1 
ATOM   2867 O  O    . LEU   A 1 140 ? 14.965 -13.907 0.208   1.00 12.66 ?  140 LEU   A O    1 
ATOM   2868 C  CB   . LEU   A 1 140 ? 12.714 -11.491 0.141   1.00 12.92 ?  140 LEU   A CB   1 
ATOM   2869 C  CG   . LEU   A 1 140 ? 12.255 -12.361 1.309   1.00 13.56 ?  140 LEU   A CG   1 
ATOM   2870 C  CD1  . LEU   A 1 140 ? 13.157 -12.198 2.525   1.00 13.54 ?  140 LEU   A CD1  1 
ATOM   2871 C  CD2  . LEU   A 1 140 ? 10.798 -12.049 1.668   1.00 14.17 ?  140 LEU   A CD2  1 
ATOM   2872 H  H    . LEU   A 1 140 ? 13.739 -10.445 -1.797  1.00 15.08 ?  140 LEU   A H    1 
ATOM   2873 H  HA   . LEU   A 1 140 ? 14.743 -11.441 0.396   1.00 14.82 ?  140 LEU   A HA   1 
ATOM   2874 H  HB2  . LEU   A 1 140 ? 12.616 -10.569 0.416   1.00 15.51 ?  140 LEU   A HB2  1 
ATOM   2875 H  HB3  . LEU   A 1 140 ? 12.122 -11.674 -0.603  1.00 15.51 ?  140 LEU   A HB3  1 
ATOM   2876 H  HG   . LEU   A 1 140 ? 12.282 -13.293 1.040   1.00 16.27 ?  140 LEU   A HG   1 
ATOM   2877 H  HD11 . LEU   A 1 140 ? 12.780 -12.697 3.267   1.00 16.25 ?  140 LEU   A HD11 1 
ATOM   2878 H  HD12 . LEU   A 1 140 ? 14.036 -12.547 2.308   1.00 16.25 ?  140 LEU   A HD12 1 
ATOM   2879 H  HD13 . LEU   A 1 140 ? 13.215 -11.260 2.751   1.00 16.25 ?  140 LEU   A HD13 1 
ATOM   2880 H  HD21 . LEU   A 1 140 ? 10.526 -12.614 2.413   1.00 17.01 ?  140 LEU   A HD21 1 
ATOM   2881 H  HD22 . LEU   A 1 140 ? 10.727 -11.116 1.923   1.00 17.01 ?  140 LEU   A HD22 1 
ATOM   2882 H  HD23 . LEU   A 1 140 ? 10.234 -12.227 0.900   1.00 17.01 ?  140 LEU   A HD23 1 
ATOM   2883 N  N    . ARG   A 1 141 ? 14.010 -13.639 -1.816  1.00 12.66 ?  141 ARG   A N    1 
ATOM   2884 C  CA   . ARG   A 1 141 ? 14.250 -15.023 -2.207  1.00 13.86 ?  141 ARG   A CA   1 
ATOM   2885 C  C    . ARG   A 1 141 ? 15.745 -15.330 -2.225  1.00 13.00 ?  141 ARG   A C    1 
ATOM   2886 O  O    . ARG   A 1 141 ? 16.194 -16.338 -1.665  1.00 13.02 ?  141 ARG   A O    1 
ATOM   2887 C  CB   . ARG   A 1 141 ? 13.623 -15.258 -3.584  1.00 16.10 ?  141 ARG   A CB   1 
ATOM   2888 C  CG   . ARG   A 1 141 ? 13.607 -16.693 -4.048  1.00 19.47 ?  141 ARG   A CG   1 
ATOM   2889 C  CD   . ARG   A 1 141 ? 12.567 -17.465 -3.300  1.00 21.87 ?  141 ARG   A CD   1 
ATOM   2890 N  NE   . ARG   A 1 141 ? 13.180 -18.266 -2.256  1.00 22.34 ?  141 ARG   A NE   1 
ATOM   2891 C  CZ   . ARG   A 1 141 ? 12.509 -18.856 -1.277  1.00 23.16 ?  141 ARG   A CZ   1 
ATOM   2892 N  NH1  . ARG   A 1 141 ? 11.217 -18.637 -1.094  1.00 22.79 ?  141 ARG   A NH1  1 
ATOM   2893 N  NH2  . ARG   A 1 141 ? 13.153 -19.677 -0.454  1.00 24.19 ?  141 ARG   A NH2  1 
ATOM   2894 H  H    . ARG   A 1 141 ? 13.600 -13.166 -2.408  1.00 15.20 ?  141 ARG   A H    1 
ATOM   2895 H  HA   . ARG   A 1 141 ? 13.828 -15.615 -1.569  1.00 16.64 ?  141 ARG   A HA   1 
ATOM   2896 H  HB2  . ARG   A 1 141 ? 12.708 -14.939 -3.563  1.00 19.33 ?  141 ARG   A HB2  1 
ATOM   2897 H  HB3  . ARG   A 1 141 ? 14.126 -14.746 -4.237  1.00 19.33 ?  141 ARG   A HB3  1 
ATOM   2898 H  HG2  . ARG   A 1 141 ? 13.396 -16.724 -4.995  1.00 23.36 ?  141 ARG   A HG2  1 
ATOM   2899 H  HG3  . ARG   A 1 141 ? 14.475 -17.100 -3.883  1.00 23.36 ?  141 ARG   A HG3  1 
ATOM   2900 H  HD2  . ARG   A 1 141 ? 11.942 -16.851 -2.881  1.00 26.25 ?  141 ARG   A HD2  1 
ATOM   2901 H  HD3  . ARG   A 1 141 ? 12.098 -18.053 -3.914  1.00 26.25 ?  141 ARG   A HD3  1 
ATOM   2902 H  HE   . ARG   A 1 141 ? 14.016 -18.448 -2.331  1.00 26.81 ?  141 ARG   A HE   1 
ATOM   2903 H  HH11 . ARG   A 1 141 ? 10.782 -18.122 -1.630  1.00 27.35 ?  141 ARG   A HH11 1 
ATOM   2904 H  HH12 . ARG   A 1 141 ? 10.799 -19.033 -0.453  1.00 27.35 ?  141 ARG   A HH12 1 
ATOM   2905 H  HH21 . ARG   A 1 141 ? 13.996 -19.817 -0.560  1.00 29.04 ?  141 ARG   A HH21 1 
ATOM   2906 H  HH22 . ARG   A 1 141 ? 12.733 -20.055 0.194   1.00 29.04 ?  141 ARG   A HH22 1 
ATOM   2907 N  N    . VAL   A 1 142 ? 16.536 -14.459 -2.857  1.00 12.58 ?  142 VAL   A N    1 
ATOM   2908 C  CA   . VAL   A 1 142 ? 17.979 -14.668 -2.892  1.00 12.46 ?  142 VAL   A CA   1 
ATOM   2909 C  C    . VAL   A 1 142 ? 18.550 -14.659 -1.484  1.00 11.68 ?  142 VAL   A C    1 
ATOM   2910 O  O    . VAL   A 1 142 ? 19.423 -15.469 -1.150  1.00 12.17 ?  142 VAL   A O    1 
ATOM   2911 C  CB   . VAL   A 1 142 ? 18.668 -13.637 -3.803  1.00 12.82 ?  142 VAL   A CB   1 
ATOM   2912 C  CG1  . VAL   A 1 142 ? 20.179 -13.865 -3.794  1.00 12.66 ?  142 VAL   A CG1  1 
ATOM   2913 C  CG2  . VAL   A 1 142 ? 18.140 -13.741 -5.221  1.00 14.26 ?  142 VAL   A CG2  1 
ATOM   2914 H  H    . VAL   A 1 142 ? 16.267 -13.740 -3.262  1.00 15.10 ?  142 VAL   A H    1 
ATOM   2915 H  HA   . VAL   A 1 142 ? 18.151 -15.537 -3.271  1.00 14.95 ?  142 VAL   A HA   1 
ATOM   2916 H  HB   . VAL   A 1 142 ? 18.497 -12.735 -3.475  1.00 15.39 ?  142 VAL   A HB   1 
ATOM   2917 H  HG11 . VAL   A 1 142 ? 20.582 -13.363 -4.520  1.00 15.20 ?  142 VAL   A HG11 1 
ATOM   2918 H  HG12 . VAL   A 1 142 ? 20.545 -13.562 -2.945  1.00 15.20 ?  142 VAL   A HG12 1 
ATOM   2919 H  HG13 . VAL   A 1 142 ? 20.354 -14.811 -3.910  1.00 15.20 ?  142 VAL   A HG13 1 
ATOM   2920 H  HG21 . VAL   A 1 142 ? 18.612 -13.104 -5.782  1.00 17.11 ?  142 VAL   A HG21 1 
ATOM   2921 H  HG22 . VAL   A 1 142 ? 18.293 -14.642 -5.542  1.00 17.11 ?  142 VAL   A HG22 1 
ATOM   2922 H  HG23 . VAL   A 1 142 ? 17.194 -13.543 -5.218  1.00 17.11 ?  142 VAL   A HG23 1 
ATOM   2923 N  N    . CYS   A 1 143 ? 18.088 -13.737 -0.644  1.00 11.97 ?  143 CYS   A N    1 
ATOM   2924 C  CA   . CYS   A 1 143 ? 18.552 -13.695 0.737   1.00 12.00 ?  143 CYS   A CA   1 
ATOM   2925 C  C    . CYS   A 1 143 ? 18.331 -15.038 1.427   1.00 11.73 ?  143 CYS   A C    1 
ATOM   2926 O  O    . CYS   A 1 143 ? 19.257 -15.624 1.994   1.00 11.85 ?  143 CYS   A O    1 
ATOM   2927 C  CB   . CYS   A 1 143 ? 17.819 -12.582 1.484   1.00 12.37 ?  143 CYS   A CB   1 
ATOM   2928 S  SG   . CYS   A 1 143 ? 18.315 -12.416 3.200   1.00 12.81 ?  143 CYS   A SG   1 
ATOM   2929 H  H    . CYS   A 1 143 ? 17.509 -13.135 -0.845  1.00 14.36 ?  143 CYS   A H    1 
ATOM   2930 H  HA   . CYS   A 1 143 ? 19.499 -13.503 0.752   1.00 14.40 ?  143 CYS   A HA   1 
ATOM   2931 H  HB2  . CYS   A 1 143 ? 17.991 -11.739 1.040   1.00 14.85 ?  143 CYS   A HB2  1 
ATOM   2932 H  HB3  . CYS   A 1 143 ? 16.869 -12.770 1.468   1.00 14.85 ?  143 CYS   A HB3  1 
ATOM   2933 H  HG   . CYS   A 1 143 ? 17.742 -11.481 3.677   1.00 15.37 ?  143 CYS   A HG   1 
ATOM   2934 N  N    . VAL   A 1 144 ? 17.104 -15.551 1.376   1.00 12.20 ?  144 VAL   A N    1 
ATOM   2935 C  CA   . VAL   A 1 144 ? 16.779 -16.787 2.079   1.00 13.34 ?  144 VAL   A CA   1 
ATOM   2936 C  C    . VAL   A 1 144 ? 17.584 -17.956 1.535   1.00 13.25 ?  144 VAL   A C    1 
ATOM   2937 O  O    . VAL   A 1 144 ? 17.955 -18.870 2.281   1.00 13.57 ?  144 VAL   A O    1 
ATOM   2938 C  CB   . VAL   A 1 144 ? 15.263 -17.034 1.977   1.00 16.46 ?  144 VAL   A CB   1 
ATOM   2939 C  CG1  . VAL   A 1 144 ? 14.915 -18.467 2.304   1.00 18.16 ?  144 VAL   A CG1  1 
ATOM   2940 C  CG2  . VAL   A 1 144 ? 14.523 -16.043 2.871   1.00 16.16 ?  144 VAL   A CG2  1 
ATOM   2941 H  H    . VAL   A 1 144 ? 16.442 -15.200 0.947   1.00 14.64 ?  144 VAL   A H    1 
ATOM   2942 H  HA   . VAL   A 1 144 ? 16.995 -16.682 3.015   1.00 16.02 ?  144 VAL   A HA   1 
ATOM   2943 H  HB   . VAL   A 1 144 ? 14.976 -16.862 1.064   1.00 19.75 ?  144 VAL   A HB   1 
ATOM   2944 H  HG11 . VAL   A 1 144 ? 13.960 -18.526 2.486   1.00 21.80 ?  144 VAL   A HG11 1 
ATOM   2945 H  HG12 . VAL   A 1 144 ? 15.136 -19.030 1.548   1.00 21.80 ?  144 VAL   A HG12 1 
ATOM   2946 H  HG13 . VAL   A 1 144 ? 15.413 -18.743 3.087   1.00 21.80 ?  144 VAL   A HG13 1 
ATOM   2947 H  HG21 . VAL   A 1 144 ? 13.565 -16.207 2.807   1.00 19.40 ?  144 VAL   A HG21 1 
ATOM   2948 H  HG22 . VAL   A 1 144 ? 14.814 -16.161 3.788   1.00 19.40 ?  144 VAL   A HG22 1 
ATOM   2949 H  HG23 . VAL   A 1 144 ? 14.717 -15.138 2.576   1.00 19.40 ?  144 VAL   A HG23 1 
ATOM   2950 N  N    . ASP   A 1 145 ? 17.843 -17.964 0.232   1.00 13.21 ?  145 ASP   A N    1 
ATOM   2951 C  CA   . ASP   A 1 145 ? 18.548 -19.062 -0.413  1.00 13.73 ?  145 ASP   A CA   1 
ATOM   2952 C  C    . ASP   A 1 145 ? 20.067 -18.907 -0.385  1.00 13.80 ?  145 ASP   A C    1 
ATOM   2953 O  O    . ASP   A 1 145 ? 20.771 -19.794 -0.884  1.00 15.23 ?  145 ASP   A O    1 
ATOM   2954 C  CB   . ASP   A 1 145 ? 18.093 -19.192 -1.866  1.00 15.35 ?  145 ASP   A CB   1 
ATOM   2955 C  CG   . ASP   A 1 145 ? 16.648 -19.625 -1.991  1.00 17.15 ?  145 ASP   A CG   1 
ATOM   2956 O  OD1  . ASP   A 1 145 ? 16.097 -20.178 -1.015  1.00 17.77 ?  145 ASP   A OD1  1 
ATOM   2957 O  OD2  . ASP   A 1 145 ? 16.072 -19.411 -3.074  1.00 18.49 -1 145 ASP   A OD2  1 
ATOM   2958 H  H    . ASP   A 1 145 ? 17.599 -17.342 -0.312  1.00 15.86 ?  145 ASP   A H    1 
ATOM   2959 H  HA   . ASP   A 1 145 ? 18.322 -19.888 0.042   1.00 16.48 ?  145 ASP   A HA   1 
ATOM   2960 H  HB2  . ASP   A 1 145 ? 18.195 -18.335 -2.308  1.00 18.43 ?  145 ASP   A HB2  1 
ATOM   2961 H  HB3  . ASP   A 1 145 ? 18.637 -19.862 -2.308  1.00 18.43 ?  145 ASP   A HB3  1 
ATOM   2962 N  N    . THR   A 1 146 ? 20.590 -17.821 0.174   1.00 12.27 ?  146 THR   A N    1 
ATOM   2963 C  CA   . THR   A 1 146 ? 22.027 -17.573 0.181   1.00 11.86 ?  146 THR   A CA   1 
ATOM   2964 C  C    . THR   A 1 146 ? 22.595 -17.390 1.575   1.00 11.48 ?  146 THR   A C    1 
ATOM   2965 O  O    . THR   A 1 146 ? 23.674 -17.915 1.876   1.00 12.59 ?  146 THR   A O    1 
ATOM   2966 C  CB   . THR   A 1 146 ? 22.350 -16.324 -0.659  1.00 11.73 ?  146 THR   A CB   1 
ATOM   2967 O  OG1  . THR   A 1 146 ? 21.823 -16.480 -1.977  1.00 12.39 ?  146 THR   A OG1  1 
ATOM   2968 C  CG2  . THR   A 1 146 ? 23.853 -16.101 -0.750  1.00 12.21 ?  146 THR   A CG2  1 
ATOM   2969 H  H    . THR   A 1 146 ? 20.127 -17.199 0.554   1.00 14.73 ?  146 THR   A H    1 
ATOM   2970 H  HA   . THR   A 1 146 ? 22.480 -18.322 -0.223  1.00 14.23 ?  146 THR   A HA   1 
ATOM   2971 H  HB   . THR   A 1 146 ? 21.954 -15.541 -0.248  1.00 14.07 ?  146 THR   A HB   1 
ATOM   2972 H  HG1  . THR   A 1 146 ? 20.987 -16.562 -1.944  1.00 14.87 ?  146 THR   A HG1  1 
ATOM   2973 H  HG21 . THR   A 1 146 ? 24.049 -15.447 -1.439  1.00 14.65 ?  146 THR   A HG21 1 
ATOM   2974 H  HG22 . THR   A 1 146 ? 24.193 -15.776 0.098   1.00 14.65 ?  146 THR   A HG22 1 
ATOM   2975 H  HG23 . THR   A 1 146 ? 24.297 -16.934 -0.972  1.00 14.65 ?  146 THR   A HG23 1 
ATOM   2976 N  N    . VAL   A 1 147 ? 21.922 -16.611 2.412   1.00 11.48 ?  147 VAL   A N    1 
ATOM   2977 C  CA   . VAL   A 1 147 ? 22.413 -16.318 3.749   1.00 11.50 ?  147 VAL   A CA   1 
ATOM   2978 C  C    . VAL   A 1 147 ? 22.099 -17.490 4.664   1.00 11.95 ?  147 VAL   A C    1 
ATOM   2979 O  O    . VAL   A 1 147 ? 20.954 -17.958 4.729   1.00 12.81 ?  147 VAL   A O    1 
ATOM   2980 C  CB   . VAL   A 1 147 ? 21.793 -15.016 4.279   1.00 12.27 ?  147 VAL   A CB   1 
ATOM   2981 C  CG1  . VAL   A 1 147 ? 22.361 -14.711 5.651   1.00 13.04 ?  147 VAL   A CG1  1 
ATOM   2982 C  CG2  . VAL   A 1 147 ? 22.036 -13.863 3.313   1.00 12.36 ?  147 VAL   A CG2  1 
ATOM   2983 H  H    . VAL   A 1 147 ? 21.163 -16.242 2.231   1.00 13.78 ?  147 VAL   A H    1 
ATOM   2984 H  HA   . VAL   A 1 147 ? 23.374 -16.201 3.715   1.00 13.81 ?  147 VAL   A HA   1 
ATOM   2985 H  HB   . VAL   A 1 147 ? 20.833 -15.135 4.373   1.00 14.73 ?  147 VAL   A HB   1 
ATOM   2986 H  HG11 . VAL   A 1 147 ? 22.124 -13.806 5.898   1.00 15.65 ?  147 VAL   A HG11 1 
ATOM   2987 H  HG12 . VAL   A 1 147 ? 21.989 -15.337 6.296   1.00 15.65 ?  147 VAL   A HG12 1 
ATOM   2988 H  HG13 . VAL   A 1 147 ? 23.326 -14.805 5.619   1.00 15.65 ?  147 VAL   A HG13 1 
ATOM   2989 H  HG21 . VAL   A 1 147 ? 21.701 -13.042 3.716   1.00 14.83 ?  147 VAL   A HG21 1 
ATOM   2990 H  HG22 . VAL   A 1 147 ? 22.983 -13.787 3.145   1.00 14.83 ?  147 VAL   A HG22 1 
ATOM   2991 H  HG23 . VAL   A 1 147 ? 21.559 -14.039 2.487   1.00 14.83 ?  147 VAL   A HG23 1 
ATOM   2992 N  N    . ARG   A 1 148 ? 23.124 -17.964 5.371   1.00 12.04 ?  148 ARG   A N    1 
ATOM   2993 C  CA   . ARG   A 1 148 ? 22.991 -19.044 6.337   1.00 12.30 ?  148 ARG   A CA   1 
ATOM   2994 C  C    . ARG   A 1 148 ? 23.126 -18.575 7.773   1.00 12.93 ?  148 ARG   A C    1 
ATOM   2995 O  O    . ARG   A 1 148 ? 22.732 -19.306 8.690   1.00 14.52 ?  148 ARG   A O    1 
ATOM   2996 C  CB   . ARG   A 1 148 ? 24.018 -20.149 6.056   1.00 12.96 ?  148 ARG   A CB   1 
ATOM   2997 C  CG   . ARG   A 1 148 ? 23.850 -20.773 4.686   1.00 14.15 ?  148 ARG   A CG   1 
ATOM   2998 C  CD   . ARG   A 1 148 ? 24.929 -21.803 4.380   1.00 15.10 ?  148 ARG   A CD   1 
ATOM   2999 N  NE   . ARG   A 1 148 ? 26.265 -21.220 4.403   1.00 14.91 ?  148 ARG   A NE   1 
ATOM   3000 C  CZ   . ARG   A 1 148 ? 26.777 -20.484 3.426   1.00 14.22 ?  148 ARG   A CZ   1 
ATOM   3001 N  NH1  . ARG   A 1 148 ? 26.097 -20.239 2.318   1.00 14.64 ?  148 ARG   A NH1  1 
ATOM   3002 N  NH2  . ARG   A 1 148 ? 28.004 -19.977 3.566   1.00 14.55 ?  148 ARG   A NH2  1 
ATOM   3003 H  H    . ARG   A 1 148 ? 23.931 -17.664 5.298   1.00 14.46 ?  148 ARG   A H    1 
ATOM   3004 H  HA   . ARG   A 1 148 ? 22.109 -19.431 6.239   1.00 14.76 ?  148 ARG   A HA   1 
ATOM   3005 H  HB2  . ARG   A 1 148 ? 24.906 -19.781 6.110   1.00 15.55 ?  148 ARG   A HB2  1 
ATOM   3006 H  HB3  . ARG   A 1 148 ? 23.903 -20.855 6.715   1.00 15.55 ?  148 ARG   A HB3  1 
ATOM   3007 H  HG2  . ARG   A 1 148 ? 22.985 -21.212 4.643   1.00 16.98 ?  148 ARG   A HG2  1 
ATOM   3008 H  HG3  . ARG   A 1 148 ? 23.898 -20.071 4.017   1.00 16.98 ?  148 ARG   A HG3  1 
ATOM   3009 H  HD2  . ARG   A 1 148 ? 24.897 -22.506 5.048   1.00 18.13 ?  148 ARG   A HD2  1 
ATOM   3010 H  HD3  . ARG   A 1 148 ? 24.773 -22.175 3.498   1.00 18.13 ?  148 ARG   A HD3  1 
ATOM   3011 H  HE   . ARG   A 1 148 ? 26.756 -21.366 5.092   1.00 17.90 ?  148 ARG   A HE   1 
ATOM   3012 H  HH11 . ARG   A 1 148 ? 25.308 -20.557 2.215   1.00 17.58 ?  148 ARG   A HH11 1 
ATOM   3013 H  HH12 . ARG   A 1 148 ? 26.449 -19.755 1.697   1.00 17.58 ?  148 ARG   A HH12 1 
ATOM   3014 H  HH21 . ARG   A 1 148 ? 28.450 -20.123 4.284   1.00 17.46 ?  148 ARG   A HH21 1 
ATOM   3015 H  HH22 . ARG   A 1 148 ? 28.344 -19.490 2.940   1.00 17.46 ?  148 ARG   A HH22 1 
ATOM   3016 N  N    . THR   A 1 149 ? 23.677 -17.386 7.986   1.00 12.94 ?  149 THR   A N    1 
ATOM   3017 C  CA   . THR   A 1 149 ? 23.762 -16.791 9.304   1.00 13.22 ?  149 THR   A CA   1 
ATOM   3018 C  C    . THR   A 1 149 ? 22.439 -16.094 9.618   1.00 12.83 ?  149 THR   A C    1 
ATOM   3019 O  O    . THR   A 1 149 ? 21.499 -16.092 8.814   1.00 13.25 ?  149 THR   A O    1 
ATOM   3020 C  CB   . THR   A 1 149 ? 24.962 -15.853 9.363   1.00 13.59 ?  149 THR   A CB   1 
ATOM   3021 O  OG1  . THR   A 1 149 ? 24.831 -14.909 8.300   1.00 13.52 ?  149 THR   A OG1  1 
ATOM   3022 C  CG2  . THR   A 1 149 ? 26.268 -16.645 9.214   1.00 14.11 ?  149 THR   A CG2  1 
ATOM   3023 H  H    . THR   A 1 149 ? 24.013 -16.892 7.363   1.00 15.54 ?  149 THR   A H    1 
ATOM   3024 H  HA   . THR   A 1 149 ? 23.888 -17.496 9.957   1.00 15.87 ?  149 THR   A HA   1 
ATOM   3025 H  HB   . THR   A 1 149 ? 24.963 -15.396 10.216  1.00 16.31 ?  149 THR   A HB   1 
ATOM   3026 H  HG1  . THR   A 1 149 ? 25.481 -14.376 8.313   1.00 16.23 ?  149 THR   A HG1  1 
ATOM   3027 H  HG21 . THR   A 1 149 ? 27.026 -16.043 9.274   1.00 16.93 ?  149 THR   A HG21 1 
ATOM   3028 H  HG22 . THR   A 1 149 ? 26.339 -17.311 9.918   1.00 16.93 ?  149 THR   A HG22 1 
ATOM   3029 H  HG23 . THR   A 1 149 ? 26.291 -17.096 8.354   1.00 16.93 ?  149 THR   A HG23 1 
ATOM   3030 N  N    . ASN   A 1 150 ? 22.330 -15.544 10.821  1.00 12.99 ?  150 ASN   A N    1 
ATOM   3031 C  CA   . ASN   A 1 150 ? 21.053 -15.033 11.318  1.00 13.35 ?  150 ASN   A CA   1 
ATOM   3032 C  C    . ASN   A 1 150 ? 20.866 -13.596 10.861  1.00 12.79 ?  150 ASN   A C    1 
ATOM   3033 O  O    . ASN   A 1 150 ? 21.610 -12.701 11.280  1.00 14.35 ?  150 ASN   A O    1 
ATOM   3034 C  CB   . ASN   A 1 150 ? 21.009 -15.144 12.837  1.00 15.80 ?  150 ASN   A CB   1 
ATOM   3035 C  CG   . ASN   A 1 150 ? 20.870 -16.571 13.300  1.00 20.24 ?  150 ASN   A CG   1 
ATOM   3036 O  OD1  . ASN   A 1 150 ? 20.251 -17.389 12.621  1.00 21.38 ?  150 ASN   A OD1  1 
ATOM   3037 N  ND2  . ASN   A 1 150 ? 21.457 -16.887 14.449  1.00 22.55 ?  150 ASN   A ND2  1 
ATOM   3038 H  H    . ASN   A 1 150 ? 22.983 -15.456 11.371  1.00 15.60 ?  150 ASN   A H    1 
ATOM   3039 H  HA   . ASN   A 1 150 ? 20.329 -15.573 10.956  1.00 16.03 ?  150 ASN   A HA   1 
ATOM   3040 H  HB2  . ASN   A 1 150 ? 21.830 -14.789 13.209  1.00 18.96 ?  150 ASN   A HB2  1 
ATOM   3041 H  HB3  . ASN   A 1 150 ? 20.247 -14.647 13.174  1.00 18.96 ?  150 ASN   A HB3  1 
ATOM   3042 H  HD21 . ASN   A 1 150 ? 21.408 -17.693 14.758  1.00 27.07 ?  150 ASN   A HD21 1 
ATOM   3043 H  HD22 . ASN   A 1 150 ? 21.884 -16.288 14.898  1.00 27.07 ?  150 ASN   A HD22 1 
ATOM   3044 N  N    . VAL   A 1 151 ? 19.871 -13.364 10.012  1.00 12.39 ?  151 VAL   A N    1 
ATOM   3045 C  CA   . VAL   A 1 151 ? 19.653 -12.052 9.429   1.00 12.64 ?  151 VAL   A CA   1 
ATOM   3046 C  C    . VAL   A 1 151 ? 18.270 -11.536 9.808   1.00 12.51 ?  151 VAL   A C    1 
ATOM   3047 O  O    . VAL   A 1 151 ? 17.259 -12.248 9.681   1.00 14.09 ?  151 VAL   A O    1 
ATOM   3048 C  CB   . VAL   A 1 151 ? 19.928 -12.032 7.910   1.00 13.78 ?  151 VAL   A CB   1 
ATOM   3049 C  CG1  . VAL   A 1 151 ? 19.094 -13.050 7.169   1.00 14.63 ?  151 VAL   A CG1  1 
ATOM   3050 C  CG2  . VAL   A 1 151 ? 19.726 -10.625 7.347   1.00 14.46 ?  151 VAL   A CG2  1 
ATOM   3051 H  H    . VAL   A 1 151 ? 19.305 -13.960 9.759   1.00 14.87 ?  151 VAL   A H    1 
ATOM   3052 H  HA   . VAL   A 1 151 ? 20.297 -11.443 9.823   1.00 15.17 ?  151 VAL   A HA   1 
ATOM   3053 H  HB   . VAL   A 1 151 ? 20.863 -12.265 7.763   1.00 16.53 ?  151 VAL   A HB   1 
ATOM   3054 H  HG11 . VAL   A 1 151 ? 19.279 -12.985 6.217   1.00 17.56 ?  151 VAL   A HG11 1 
ATOM   3055 H  HG12 . VAL   A 1 151 ? 19.324 -13.941 7.486   1.00 17.56 ?  151 VAL   A HG12 1 
ATOM   3056 H  HG13 . VAL   A 1 151 ? 18.156 -12.874 7.335   1.00 17.56 ?  151 VAL   A HG13 1 
ATOM   3057 H  HG21 . VAL   A 1 151 ? 20.048 -10.601 6.430   1.00 17.36 ?  151 VAL   A HG21 1 
ATOM   3058 H  HG22 . VAL   A 1 151 ? 18.784 -10.404 7.372   1.00 17.36 ?  151 VAL   A HG22 1 
ATOM   3059 H  HG23 . VAL   A 1 151 ? 20.231 -9.993  7.886   1.00 17.36 ?  151 VAL   A HG23 1 
ATOM   3060 N  N    . TYR   A 1 152 ? 18.259 -10.292 10.286  1.00 12.41 ?  152 TYR   A N    1 
ATOM   3061 C  CA   . TYR   A 1 152 ? 17.067 -9.563  10.684  1.00 12.17 ?  152 TYR   A CA   1 
ATOM   3062 C  C    . TYR   A 1 152 ? 16.872 -8.459  9.657   1.00 11.83 ?  152 TYR   A C    1 
ATOM   3063 O  O    . TYR   A 1 152 ? 17.657 -7.505  9.604   1.00 12.36 ?  152 TYR   A O    1 
ATOM   3064 C  CB   . TYR   A 1 152 ? 17.258 -9.019  12.096  1.00 12.79 ?  152 TYR   A CB   1 
ATOM   3065 C  CG   . TYR   A 1 152 ? 17.228 -10.152 13.086  1.00 13.58 ?  152 TYR   A CG   1 
ATOM   3066 C  CD1  . TYR   A 1 152 ? 18.359 -10.914 13.347  1.00 14.74 ?  152 TYR   A CD1  1 
ATOM   3067 C  CD2  . TYR   A 1 152 ? 16.045 -10.510 13.712  1.00 13.85 ?  152 TYR   A CD2  1 
ATOM   3068 C  CE1  . TYR   A 1 152 ? 18.322 -11.976 14.223  1.00 16.19 ?  152 TYR   A CE1  1 
ATOM   3069 C  CE2  . TYR   A 1 152 ? 15.995 -11.581 14.595  1.00 15.13 ?  152 TYR   A CE2  1 
ATOM   3070 C  CZ   . TYR   A 1 152 ? 17.138 -12.310 14.844  1.00 16.05 ?  152 TYR   A CZ   1 
ATOM   3071 O  OH   . TYR   A 1 152 ? 17.103 -13.382 15.717  1.00 18.10 ?  152 TYR   A OH   1 
ATOM   3072 H  H    . TYR   A 1 152 ? 18.978 -9.818  10.377  1.00 14.90 ?  152 TYR   A H    1 
ATOM   3073 H  HA   . TYR   A 1 152 ? 16.299 -10.154 10.667  1.00 14.61 ?  152 TYR   A HA   1 
ATOM   3074 H  HB2  . TYR   A 1 152 ? 18.117 -8.580  12.162  1.00 15.36 ?  152 TYR   A HB2  1 
ATOM   3075 H  HB3  . TYR   A 1 152 ? 16.540 -8.404  12.307  1.00 15.36 ?  152 TYR   A HB3  1 
ATOM   3076 H  HD1  . TYR   A 1 152 ? 19.156 -10.697 12.926  1.00 17.69 ?  152 TYR   A HD1  1 
ATOM   3077 H  HD2  . TYR   A 1 152 ? 15.266 -10.024 13.545  1.00 16.62 ?  152 TYR   A HD2  1 
ATOM   3078 H  HE1  . TYR   A 1 152 ? 19.090 -12.470 14.396  1.00 19.43 ?  152 TYR   A HE1  1 
ATOM   3079 H  HE2  . TYR   A 1 152 ? 15.194 -11.801 15.020  1.00 18.16 ?  152 TYR   A HE2  1 
ATOM   3080 H  HH   . TYR   A 1 152 ? 16.322 -13.462 16.034  1.00 21.72 ?  152 TYR   A HH   1 
ATOM   3081 N  N    A LEU   A 1 153 ? 15.855 -8.622  8.810   0.72 12.16 ?  153 LEU   A N    1 
ATOM   3082 N  N    B LEU   A 1 153 ? 15.816 -8.571  8.862   0.28 11.85 ?  153 LEU   A N    1 
ATOM   3083 C  CA   A LEU   A 1 153 ? 15.596 -7.735  7.683   0.72 12.29 ?  153 LEU   A CA   1 
ATOM   3084 C  CA   B LEU   A 1 153 ? 15.538 -7.599  7.818   0.28 11.69 ?  153 LEU   A CA   1 
ATOM   3085 C  C    A LEU   A 1 153 ? 14.592 -6.659  8.069   0.72 12.33 ?  153 LEU   A C    1 
ATOM   3086 C  C    B LEU   A 1 153 ? 14.590 -6.524  8.332   0.28 11.94 ?  153 LEU   A C    1 
ATOM   3087 O  O    A LEU   A 1 153 ? 13.480 -6.965  8.515   0.72 13.46 ?  153 LEU   A O    1 
ATOM   3088 O  O    B LEU   A 1 153 ? 13.559 -6.830  8.941   0.28 12.10 ?  153 LEU   A O    1 
ATOM   3089 C  CB   A LEU   A 1 153 ? 15.034 -8.534  6.504   0.72 12.36 ?  153 LEU   A CB   1 
ATOM   3090 C  CB   B LEU   A 1 153 ? 14.920 -8.293  6.608   0.28 11.77 ?  153 LEU   A CB   1 
ATOM   3091 C  CG   A LEU   A 1 153 ? 15.976 -9.545  5.845   0.72 12.32 ?  153 LEU   A CG   1 
ATOM   3092 C  CG   B LEU   A 1 153 ? 15.823 -9.325  5.938   0.28 11.55 ?  153 LEU   A CG   1 
ATOM   3093 C  CD1  A LEU   A 1 153 ? 15.203 -10.454 4.898   0.72 12.66 ?  153 LEU   A CD1  1 
ATOM   3094 C  CD1  B LEU   A 1 153 ? 15.015 -10.146 4.952   0.28 11.65 ?  153 LEU   A CD1  1 
ATOM   3095 C  CD2  A LEU   A 1 153 ? 17.095 -8.829  5.101   0.72 13.10 ?  153 LEU   A CD2  1 
ATOM   3096 C  CD2  B LEU   A 1 153 ? 16.996 -8.643  5.248   0.28 11.87 ?  153 LEU   A CD2  1 
ATOM   3097 H  H    A LEU   A 1 153 ? 15.277 -9.262  8.881   0.72 14.60 ?  153 LEU   A H    1 
ATOM   3098 H  H    B LEU   A 1 153 ? 15.238 -9.209  8.910   0.28 14.22 ?  153 LEU   A H    1 
ATOM   3099 H  HA   A LEU   A 1 153 ? 16.422 -7.313  7.410   0.72 14.75 ?  153 LEU   A HA   1 
ATOM   3100 H  HA   B LEU   A 1 153 ? 16.366 -7.179  7.550   0.28 14.03 ?  153 LEU   A HA   1 
ATOM   3101 H  HB2  A LEU   A 1 153 ? 14.259 -9.028  6.814   0.72 14.84 ?  153 LEU   A HB2  1 
ATOM   3102 H  HB2  B LEU   A 1 153 ? 14.113 -8.745  6.895   0.28 14.13 ?  153 LEU   A HB2  1 
ATOM   3103 H  HB3  A LEU   A 1 153 ? 14.762 -7.907  5.817   0.72 14.84 ?  153 LEU   A HB3  1 
ATOM   3104 H  HB3  B LEU   A 1 153 ? 14.701 -7.615  5.950   0.28 14.13 ?  153 LEU   A HB3  1 
ATOM   3105 H  HG   A LEU   A 1 153 ? 16.381 -10.096 6.533   0.72 14.79 ?  153 LEU   A HG   1 
ATOM   3106 H  HG   B LEU   A 1 153 ? 16.178 -9.921  6.615   0.28 13.86 ?  153 LEU   A HG   1 
ATOM   3107 H  HD11 A LEU   A 1 153 ? 15.774 -11.195 4.639   0.72 15.19 ?  153 LEU   A HD11 1 
ATOM   3108 H  HD11 B LEU   A 1 153 ? 15.599 -10.792 4.530   0.28 13.98 ?  153 LEU   A HD11 1 
ATOM   3109 H  HD12 A LEU   A 1 153 ? 14.418 -10.786 5.354   0.72 15.19 ?  153 LEU   A HD12 1 
ATOM   3110 H  HD12 B LEU   A 1 153 ? 14.306 -10.601 5.432   0.28 13.98 ?  153 LEU   A HD12 1 
ATOM   3111 H  HD13 A LEU   A 1 153 ? 14.945 -9.944  4.115   0.72 15.19 ?  153 LEU   A HD13 1 
ATOM   3112 H  HD13 B LEU   A 1 153 ? 14.636 -9.552  4.286   0.28 13.98 ?  153 LEU   A HD13 1 
ATOM   3113 H  HD21 A LEU   A 1 153 ? 17.680 -9.491  4.700   0.72 15.73 ?  153 LEU   A HD21 1 
ATOM   3114 H  HD21 B LEU   A 1 153 ? 17.502 -9.310  4.759   0.28 14.25 ?  153 LEU   A HD21 1 
ATOM   3115 H  HD22 A LEU   A 1 153 ? 16.707 -8.269  4.413   0.72 15.73 ?  153 LEU   A HD22 1 
ATOM   3116 H  HD22 B LEU   A 1 153 ? 16.656 -7.971  4.638   0.28 14.25 ?  153 LEU   A HD22 1 
ATOM   3117 H  HD23 A LEU   A 1 153 ? 17.595 -8.285  5.729   0.72 15.73 ?  153 LEU   A HD23 1 
ATOM   3118 H  HD23 B LEU   A 1 153 ? 17.560 -8.226  5.919   0.28 14.25 ?  153 LEU   A HD23 1 
ATOM   3119 N  N    A ALA   A 1 154 ? 14.976 -5.404  7.864   0.72 12.49 ?  154 ALA   A N    1 
ATOM   3120 N  N    B ALA   A 1 154 ? 14.951 -5.267  8.087   0.28 12.24 ?  154 ALA   A N    1 
ATOM   3121 C  CA   A ALA   A 1 154 ? 14.111 -4.255  8.096   0.72 13.00 ?  154 ALA   A CA   1 
ATOM   3122 C  CA   B ALA   A 1 154 ? 14.105 -4.115  8.367   0.28 12.99 ?  154 ALA   A CA   1 
ATOM   3123 C  C    A ALA   A 1 154 ? 13.602 -3.742  6.756   0.72 12.94 ?  154 ALA   A C    1 
ATOM   3124 C  C    B ALA   A 1 154 ? 13.614 -3.555  7.039   0.28 13.40 ?  154 ALA   A C    1 
ATOM   3125 O  O    A ALA   A 1 154 ? 14.398 -3.365  5.889   0.72 13.10 ?  154 ALA   A O    1 
ATOM   3126 O  O    B ALA   A 1 154 ? 14.420 -3.104  6.218   0.28 13.12 ?  154 ALA   A O    1 
ATOM   3127 C  CB   A ALA   A 1 154 ? 14.878 -3.147  8.811   0.72 13.31 ?  154 ALA   A CB   1 
ATOM   3128 C  CB   B ALA   A 1 154 ? 14.886 -3.048  9.133   0.28 13.23 ?  154 ALA   A CB   1 
ATOM   3129 H  H    A ALA   A 1 154 ? 15.761 -5.189  7.584   0.72 14.99 ?  154 ALA   A H    1 
ATOM   3130 H  H    B ALA   A 1 154 ? 15.714 -5.051  7.751   0.28 14.69 ?  154 ALA   A H    1 
ATOM   3131 H  HA   A ALA   A 1 154 ? 13.353 -4.517  8.641   0.72 15.60 ?  154 ALA   A HA   1 
ATOM   3132 H  HA   B ALA   A 1 154 ? 13.341 -4.386  8.900   0.28 15.59 ?  154 ALA   A HA   1 
ATOM   3133 H  HB1  A ALA   A 1 154 ? 14.284 -2.393  8.952   0.72 15.98 ?  154 ALA   A HB1  1 
ATOM   3134 H  HB1  B ALA   A 1 154 ? 14.302 -2.292  9.305   0.28 15.88 ?  154 ALA   A HB1  1 
ATOM   3135 H  HB2  A ALA   A 1 154 ? 15.200 -3.482  9.660   0.72 15.98 ?  154 ALA   A HB2  1 
ATOM   3136 H  HB2  B ALA   A 1 154 ? 15.199 -3.421  9.971   0.28 15.88 ?  154 ALA   A HB2  1 
ATOM   3137 H  HB3  A ALA   A 1 154 ? 15.628 -2.875  8.255   0.72 15.98 ?  154 ALA   A HB3  1 
ATOM   3138 H  HB3  B ALA   A 1 154 ? 15.643 -2.763  8.595   0.28 15.88 ?  154 ALA   A HB3  1 
ATOM   3139 N  N    A VAL   A 1 155 ? 12.284 -3.718  6.596   0.72 13.78 ?  155 VAL   A N    1 
ATOM   3140 N  N    B VAL   A 1 155 ? 12.300 -3.581  6.830   0.28 14.33 ?  155 VAL   A N    1 
ATOM   3141 C  CA   A VAL   A 1 155 ? 11.632 -3.236  5.383   0.72 14.93 ?  155 VAL   A CA   1 
ATOM   3142 C  CA   B VAL   A 1 155 ? 11.681 -3.156  5.578   0.28 15.29 ?  155 VAL   A CA   1 
ATOM   3143 C  C    A VAL   A 1 155 ? 10.891 -1.956  5.748   0.72 16.29 ?  155 VAL   A C    1 
ATOM   3144 C  C    B VAL   A 1 155 ? 11.023 -1.799  5.795   0.28 16.65 ?  155 VAL   A C    1 
ATOM   3145 O  O    A VAL   A 1 155 ? 9.947  -1.983  6.546   0.72 16.18 ?  155 VAL   A O    1 
ATOM   3146 O  O    B VAL   A 1 155 ? 10.265 -1.615  6.756   0.28 16.49 ?  155 VAL   A O    1 
ATOM   3147 C  CB   A VAL   A 1 155 ? 10.693 -4.296  4.787   0.72 14.91 ?  155 VAL   A CB   1 
ATOM   3148 C  CB   B VAL   A 1 155 ? 10.665 -4.198  5.076   0.28 15.31 ?  155 VAL   A CB   1 
ATOM   3149 C  CG1  A VAL   A 1 155 ? 9.950  -3.740  3.584   0.72 16.06 ?  155 VAL   A CG1  1 
ATOM   3150 C  CG1  B VAL   A 1 155 ? 9.971  -3.702  3.816   0.28 15.72 ?  155 VAL   A CG1  1 
ATOM   3151 C  CG2  A VAL   A 1 155 ? 11.492 -5.530  4.385   0.72 15.29 ?  155 VAL   A CG2  1 
ATOM   3152 C  CG2  B VAL   A 1 155 ? 11.358 -5.532  4.821   0.28 15.10 ?  155 VAL   A CG2  1 
ATOM   3153 H  H    A VAL   A 1 155 ? 11.729 -3.995  7.195   0.72 16.54 ?  155 VAL   A H    1 
ATOM   3154 H  H    B VAL   A 1 155 ? 11.736 -3.854  7.417   0.28 17.20 ?  155 VAL   A H    1 
ATOM   3155 H  HA   A VAL   A 1 155 ? 12.302 -3.028  4.720   0.72 17.92 ?  155 VAL   A HA   1 
ATOM   3156 H  HA   B VAL   A 1 155 ? 12.369 -3.058  4.900   0.28 18.35 ?  155 VAL   A HA   1 
ATOM   3157 H  HB   A VAL   A 1 155 ? 10.038 -4.567  5.455   0.72 17.90 ?  155 VAL   A HB   1 
ATOM   3158 H  HB   B VAL   A 1 155 ? 9.991  -4.338  5.759   0.28 18.37 ?  155 VAL   A HB   1 
ATOM   3159 H  HG11 A VAL   A 1 155 ? 9.516  -4.468  3.112   0.72 19.27 ?  155 VAL   A HG11 1 
ATOM   3160 H  HG11 B VAL   A 1 155 ? 9.502  -4.444  3.403   0.28 18.87 ?  155 VAL   A HG11 1 
ATOM   3161 H  HG12 A VAL   A 1 155 ? 9.282  -3.104  3.889   0.72 19.27 ?  155 VAL   A HG12 1 
ATOM   3162 H  HG12 B VAL   A 1 155 ? 9.340  -3.005  4.054   0.28 18.87 ?  155 VAL   A HG12 1 
ATOM   3163 H  HG13 A VAL   A 1 155 ? 10.584 -3.299  2.999   0.72 19.27 ?  155 VAL   A HG13 1 
ATOM   3164 H  HG13 B VAL   A 1 155 ? 10.638 -3.352  3.205   0.28 18.87 ?  155 VAL   A HG13 1 
ATOM   3165 H  HG21 A VAL   A 1 155 ? 10.897 -6.177  3.975   0.72 18.35 ?  155 VAL   A HG21 1 
ATOM   3166 H  HG21 B VAL   A 1 155 ? 10.709 -6.162  4.471   0.28 18.12 ?  155 VAL   A HG21 1 
ATOM   3167 H  HG22 A VAL   A 1 155 ? 12.179 -5.266  3.751   0.72 18.35 ?  155 VAL   A HG22 1 
ATOM   3168 H  HG22 B VAL   A 1 155 ? 12.071 -5.399  4.177   0.28 18.12 ?  155 VAL   A HG22 1 
ATOM   3169 H  HG23 A VAL   A 1 155 ? 11.905 -5.914  5.175   0.72 18.35 ?  155 VAL   A HG23 1 
ATOM   3170 H  HG23 B VAL   A 1 155 ? 11.724 -5.864  5.656   0.28 18.12 ?  155 VAL   A HG23 1 
ATOM   3171 N  N    A PHE   A 1 156 ? 11.330 -0.830  5.172   0.72 17.41 ?  156 PHE   A N    1 
ATOM   3172 N  N    B PHE   A 1 156 ? 11.298 -0.859  4.890   0.28 17.99 ?  156 PHE   A N    1 
ATOM   3173 C  CA   A PHE   A 1 156 ? 10.813 0.478   5.571   0.72 19.03 ?  156 PHE   A CA   1 
ATOM   3174 C  CA   B PHE   A 1 156 ? 10.880 0.541   5.007   0.28 19.15 ?  156 PHE   A CA   1 
ATOM   3175 C  C    A PHE   A 1 156 ? 9.348  0.656   5.193   0.72 19.24 ?  156 PHE   A C    1 
ATOM   3176 C  C    B PHE   A 1 156 ? 9.629  0.844   4.191   0.28 20.33 ?  156 PHE   A C    1 
ATOM   3177 O  O    A PHE   A 1 156 ? 8.577  1.252   5.953   0.72 20.59 ?  156 PHE   A O    1 
ATOM   3178 O  O    B PHE   A 1 156 ? 9.547  1.883   3.528   0.28 21.01 ?  156 PHE   A O    1 
ATOM   3179 C  CB   A PHE   A 1 156 ? 11.652 1.577   4.922   0.72 20.07 ?  156 PHE   A CB   1 
ATOM   3180 C  CB   B PHE   A 1 156 ? 12.032 1.453   4.588   0.28 19.12 ?  156 PHE   A CB   1 
ATOM   3181 C  CG   A PHE   A 1 156 ? 11.168 2.967   5.226   0.72 21.82 ?  156 PHE   A CG   1 
ATOM   3182 C  CG   B PHE   A 1 156 ? 11.836 2.910   4.941   0.28 19.37 ?  156 PHE   A CG   1 
ATOM   3183 C  CD1  A PHE   A 1 156 ? 11.108 3.410   6.536   0.72 22.84 ?  156 PHE   A CD1  1 
ATOM   3184 C  CD1  B PHE   A 1 156 ? 11.877 3.327   6.261   0.28 19.52 ?  156 PHE   A CD1  1 
ATOM   3185 C  CD2  A PHE   A 1 156 ? 10.774 3.824   4.209   0.72 22.39 ?  156 PHE   A CD2  1 
ATOM   3186 C  CD2  B PHE   A 1 156 ? 11.652 3.863   3.950   0.28 19.74 ?  156 PHE   A CD2  1 
ATOM   3187 C  CE1  A PHE   A 1 156 ? 10.668 4.683   6.830   0.72 23.81 ?  156 PHE   A CE1  1 
ATOM   3188 C  CE1  B PHE   A 1 156 ? 11.710 4.660   6.590   0.28 19.56 ?  156 PHE   A CE1  1 
ATOM   3189 C  CE2  A PHE   A 1 156 ? 10.334 5.103   4.496   0.72 23.53 ?  156 PHE   A CE2  1 
ATOM   3190 C  CE2  B PHE   A 1 156 ? 11.484 5.202   4.275   0.28 19.85 ?  156 PHE   A CE2  1 
ATOM   3191 C  CZ   A PHE   A 1 156 ? 10.284 5.534   5.810   0.72 24.15 ?  156 PHE   A CZ   1 
ATOM   3192 C  CZ   B PHE   A 1 156 ? 11.514 5.597   5.597   0.28 19.67 ?  156 PHE   A CZ   1 
ATOM   3193 H  H    A PHE   A 1 156 ? 11.935 -0.805  4.562   0.72 20.89 ?  156 PHE   A H    1 
ATOM   3194 H  H    B PHE   A 1 156 ? 11.746 -1.018  4.176   0.28 21.59 ?  156 PHE   A H    1 
ATOM   3195 H  HA   A PHE   A 1 156 ? 10.892 0.566   6.535   0.72 22.84 ?  156 PHE   A HA   1 
ATOM   3196 H  HA   B PHE   A 1 156 ? 10.678 0.726   5.936   0.28 22.98 ?  156 PHE   A HA   1 
ATOM   3197 H  HB2  A PHE   A 1 156 ? 12.565 1.504   5.242   0.72 24.09 ?  156 PHE   A HB2  1 
ATOM   3198 H  HB2  B PHE   A 1 156 ? 12.830 1.152   5.040   0.28 22.94 ?  156 PHE   A HB2  1 
ATOM   3199 H  HB3  A PHE   A 1 156 ? 11.630 1.458   3.960   0.72 24.09 ?  156 PHE   A HB3  1 
ATOM   3200 H  HB3  B PHE   A 1 156 ? 12.151 1.389   3.627   0.28 22.94 ?  156 PHE   A HB3  1 
ATOM   3201 H  HD1  A PHE   A 1 156 ? 11.369 2.840   7.226   0.72 27.41 ?  156 PHE   A HD1  1 
ATOM   3202 H  HD1  B PHE   A 1 156 ? 12.005 2.699   6.935   0.28 23.42 ?  156 PHE   A HD1  1 
ATOM   3203 H  HD2  A PHE   A 1 156 ? 10.810 3.533   3.326   0.72 26.87 ?  156 PHE   A HD2  1 
ATOM   3204 H  HD2  B PHE   A 1 156 ? 11.630 3.602   3.057   0.28 23.69 ?  156 PHE   A HD2  1 
ATOM   3205 H  HE1  A PHE   A 1 156 ? 10.634 4.969   7.715   0.72 28.57 ?  156 PHE   A HE1  1 
ATOM   3206 H  HE1  B PHE   A 1 156 ? 11.732 4.922   7.482   0.28 23.47 ?  156 PHE   A HE1  1 
ATOM   3207 H  HE2  A PHE   A 1 156 ? 10.072 5.668   3.809   0.72 28.24 ?  156 PHE   A HE2  1 
ATOM   3208 H  HE2  B PHE   A 1 156 ? 11.355 5.835   3.604   0.28 23.83 ?  156 PHE   A HE2  1 
ATOM   3209 H  HZ   A PHE   A 1 156 ? 9.983  6.390   6.007   0.72 28.98 ?  156 PHE   A HZ   1 
ATOM   3210 H  HZ   B PHE   A 1 156 ? 11.405 6.494   5.820   0.28 23.61 ?  156 PHE   A HZ   1 
ATOM   3211 N  N    A ASP   A 1 157 ? 8.955  0.179   4.017   0.72 18.61 ?  157 ASP   A N    1 
ATOM   3212 N  N    B ASP   A 1 157 ? 8.634  -0.041  4.221   0.28 20.68 ?  157 ASP   A N    1 
ATOM   3213 C  CA   A ASP   A 1 157 ? 7.634  0.447   3.462   0.72 19.41 ?  157 ASP   A CA   1 
ATOM   3214 C  CA   B ASP   A 1 157 ? 7.395  0.180   3.484   0.28 21.08 ?  157 ASP   A CA   1 
ATOM   3215 C  C    A ASP   A 1 157 ? 6.640  -0.599  3.960   0.72 19.11 ?  157 ASP   A C    1 
ATOM   3216 C  C    B ASP   A 1 157 ? 6.365  -0.864  3.893   0.28 20.79 ?  157 ASP   A C    1 
ATOM   3217 O  O    A ASP   A 1 157 ? 6.827  -1.799  3.726   0.72 17.91 ?  157 ASP   A O    1 
ATOM   3218 O  O    B ASP   A 1 157 ? 6.517  -2.048  3.577   0.28 20.65 ?  157 ASP   A O    1 
ATOM   3219 C  CB   A ASP   A 1 157 ? 7.723  0.407   1.940   0.72 20.46 ?  157 ASP   A CB   1 
ATOM   3220 C  CB   B ASP   A 1 157 ? 7.644  0.104   1.976   0.28 21.83 ?  157 ASP   A CB   1 
ATOM   3221 C  CG   A ASP   A 1 157 ? 6.489  0.932   1.272   0.72 22.40 ?  157 ASP   A CG   1 
ATOM   3222 C  CG   B ASP   A 1 157 ? 6.491  0.665   1.170   0.28 22.63 ?  157 ASP   A CG   1 
ATOM   3223 O  OD1  A ASP   A 1 157 ? 6.416  2.155   1.059   0.72 24.55 ?  157 ASP   A OD1  1 
ATOM   3224 O  OD1  B ASP   A 1 157 ? 6.219  1.877   1.290   0.28 23.13 ?  157 ASP   A OD1  1 
ATOM   3225 O  OD2  A ASP   A 1 157 ? 5.592  0.125   0.959   0.72 22.26 -1 157 ASP   A OD2  1 
ATOM   3226 O  OD2  B ASP   A 1 157 ? 5.853  -0.103  0.420   0.28 22.78 -1 157 ASP   A OD2  1 
ATOM   3227 H  H    A ASP   A 1 157 ? 9.458  -0.298  3.503   0.72 22.33 ?  157 ASP   A H    1 
ATOM   3228 H  H    B ASP   A 1 157 ? 8.650  -0.782  4.662   0.28 24.82 ?  157 ASP   A H    1 
ATOM   3229 H  HA   A ASP   A 1 157 ? 7.339  1.332   3.739   0.72 23.30 ?  157 ASP   A HA   1 
ATOM   3230 H  HA   B ASP   A 1 157 ? 7.044  1.061   3.693   0.28 25.30 ?  157 ASP   A HA   1 
ATOM   3231 H  HB2  A ASP   A 1 157 ? 8.473  0.949   1.650   0.72 24.56 ?  157 ASP   A HB2  1 
ATOM   3232 H  HB2  B ASP   A 1 157 ? 8.449  0.598   1.754   0.28 26.20 ?  157 ASP   A HB2  1 
ATOM   3233 H  HB3  A ASP   A 1 157 ? 7.848  -0.509  1.658   0.72 24.56 ?  157 ASP   A HB3  1 
ATOM   3234 H  HB3  B ASP   A 1 157 ? 7.745  -0.825  1.717   0.28 26.20 ?  157 ASP   A HB3  1 
ATOM   3235 N  N    A LYS   A 1 158 ? 5.582  -0.145  4.641   0.72 20.50 ?  158 LYS   A N    1 
ATOM   3236 N  N    B LYS   A 1 158 ? 5.313  -0.436  4.595   0.28 20.81 ?  158 LYS   A N    1 
ATOM   3237 C  CA   A LYS   A 1 158 ? 4.619  -1.081  5.217   0.72 21.77 ?  158 LYS   A CA   1 
ATOM   3238 C  CA   B LYS   A 1 158 ? 4.342  -1.391  5.119   0.28 20.97 ?  158 LYS   A CA   1 
ATOM   3239 C  C    A LYS   A 1 158 ? 3.906  -1.877  4.130   0.72 21.59 ?  158 LYS   A C    1 
ATOM   3240 C  C    B LYS   A 1 158 ? 3.675  -2.176  3.995   0.28 20.40 ?  158 LYS   A C    1 
ATOM   3241 O  O    A LYS   A 1 158 ? 3.736  -3.097  4.248   0.72 21.51 ?  158 LYS   A O    1 
ATOM   3242 O  O    B LYS   A 1 158 ? 3.447  -3.385  4.121   0.28 20.11 ?  158 LYS   A O    1 
ATOM   3243 C  CB   A LYS   A 1 158 ? 3.618  -0.327  6.097   0.72 23.37 ?  158 LYS   A CB   1 
ATOM   3244 C  CB   B LYS   A 1 158 ? 3.307  -0.665  5.984   0.28 21.76 ?  158 LYS   A CB   1 
ATOM   3245 C  CG   A LYS   A 1 158 ? 2.397  -1.149  6.518   0.72 25.03 ?  158 LYS   A CG   1 
ATOM   3246 C  CG   B LYS   A 1 158 ? 2.353  -1.584  6.745   0.28 22.54 ?  158 LYS   A CG   1 
ATOM   3247 C  CD   A LYS   A 1 158 ? 2.773  -2.400  7.313   0.72 26.25 ?  158 LYS   A CD   1 
ATOM   3248 C  CD   B LYS   A 1 158 ? 3.106  -2.545  7.656   0.28 23.23 ?  158 LYS   A CD   1 
ATOM   3249 C  CE   A LYS   A 1 158 ? 1.528  -3.149  7.779   0.72 27.18 ?  158 LYS   A CE   1 
ATOM   3250 C  CE   B LYS   A 1 158 ? 2.186  -3.211  8.667   0.28 23.84 ?  158 LYS   A CE   1 
ATOM   3251 N  NZ   A LYS   A 1 158 ? 1.846  -4.452  8.436   0.72 27.68 ?  158 LYS   A NZ   1 
ATOM   3252 N  NZ   B LYS   A 1 158 ? 1.296  -4.241  8.069   0.28 24.08 ?  158 LYS   A NZ   1 
ATOM   3253 H  H    A LYS   A 1 158 ? 5.413  0.688   4.781   0.72 24.60 ?  158 LYS   A H    1 
ATOM   3254 H  H    B LYS   A 1 158 ? 5.143  0.387   4.776   0.28 24.98 ?  158 LYS   A H    1 
ATOM   3255 H  HA   A LYS   A 1 158 ? 5.096  -1.704  5.788   0.72 26.13 ?  158 LYS   A HA   1 
ATOM   3256 H  HA   B LYS   A 1 158 ? 4.809  -2.024  5.682   0.28 25.16 ?  158 LYS   A HA   1 
ATOM   3257 H  HB2  A LYS   A 1 158 ? 4.070  -0.037  6.909   0.72 28.04 ?  158 LYS   A HB2  1 
ATOM   3258 H  HB2  B LYS   A 1 158 ? 3.777  -0.123  6.641   0.28 26.11 ?  158 LYS   A HB2  1 
ATOM   3259 H  HB3  A LYS   A 1 158 ? 3.298  0.450   5.612   0.72 28.04 ?  158 LYS   A HB3  1 
ATOM   3260 H  HB3  B LYS   A 1 158 ? 2.771  -0.091  5.416   0.28 26.11 ?  158 LYS   A HB3  1 
ATOM   3261 H  HG2  A LYS   A 1 158 ? 1.832  -0.600  7.082   0.72 30.04 ?  158 LYS   A HG2  1 
ATOM   3262 H  HG2  B LYS   A 1 158 ? 1.761  -1.046  7.296   0.28 27.05 ?  158 LYS   A HG2  1 
ATOM   3263 H  HG3  A LYS   A 1 158 ? 1.903  -1.425  5.730   0.72 30.04 ?  158 LYS   A HG3  1 
ATOM   3264 H  HG3  B LYS   A 1 158 ? 1.839  -2.106  6.111   0.28 27.05 ?  158 LYS   A HG3  1 
ATOM   3265 H  HD2  A LYS   A 1 158 ? 3.296  -2.994  6.752   0.72 31.50 ?  158 LYS   A HD2  1 
ATOM   3266 H  HD2  B LYS   A 1 158 ? 3.518  -3.239  7.118   0.28 27.88 ?  158 LYS   A HD2  1 
ATOM   3267 H  HD3  A LYS   A 1 158 ? 3.285  -2.140  8.096   0.72 31.50 ?  158 LYS   A HD3  1 
ATOM   3268 H  HD3  B LYS   A 1 158 ? 3.784  -2.053  8.142   0.28 27.88 ?  158 LYS   A HD3  1 
ATOM   3269 H  HE2  A LYS   A 1 158 ? 1.051  -2.599  8.420   0.72 32.62 ?  158 LYS   A HE2  1 
ATOM   3270 H  HE2  B LYS   A 1 158 ? 2.725  -3.636  9.343   0.28 28.61 ?  158 LYS   A HE2  1 
ATOM   3271 H  HE3  A LYS   A 1 158 ? 0.963  -3.330  7.012   0.72 32.62 ?  158 LYS   A HE3  1 
ATOM   3272 H  HE3  B LYS   A 1 158 ? 1.628  -2.540  9.081   0.28 28.61 ?  158 LYS   A HE3  1 
ATOM   3273 H  HZ1  A LYS   A 1 158 ? 1.095  -4.855  8.691   0.72 33.22 ?  158 LYS   A HZ1  1 
ATOM   3274 H  HZ1  B LYS   A 1 158 ? 0.777  -4.596  8.699   0.28 28.90 ?  158 LYS   A HZ1  1 
ATOM   3275 H  HZ2  A LYS   A 1 158 ? 2.279  -4.982  7.867   0.72 33.22 ?  158 LYS   A HZ2  1 
ATOM   3276 H  HZ2  B LYS   A 1 158 ? 0.783  -3.873  7.443   0.28 28.90 ?  158 LYS   A HZ2  1 
ATOM   3277 H  HZ3  A LYS   A 1 158 ? 2.358  -4.315  9.151   0.72 33.22 ?  158 LYS   A HZ3  1 
ATOM   3278 H  HZ3  B LYS   A 1 158 ? 1.787  -4.885  7.701   0.28 28.90 ?  158 LYS   A HZ3  1 
ATOM   3279 N  N    A ASN   A 1 159 ? 3.473  -1.204  3.063   0.72 22.27 ?  159 ASN   A N    1 
ATOM   3280 N  N    B ASN   A 1 159 ? 3.372  -1.510  2.879   0.28 20.39 ?  159 ASN   A N    1 
ATOM   3281 C  CA   A ASN   A 1 159 ? 2.809  -1.918  1.980   0.72 22.42 ?  159 ASN   A CA   1 
ATOM   3282 C  CA   B ASN   A 1 159 ? 2.723  -2.190  1.761   0.28 20.06 ?  159 ASN   A CA   1 
ATOM   3283 C  C    A ASN   A 1 159 ? 3.720  -2.987  1.390   0.72 21.34 ?  159 ASN   A C    1 
ATOM   3284 C  C    B ASN   A 1 159 ? 3.624  -3.276  1.178   0.28 18.42 ?  159 ASN   A C    1 
ATOM   3285 O  O    A ASN   A 1 159 ? 3.280  -4.108  1.111   0.72 21.13 ?  159 ASN   A O    1 
ATOM   3286 O  O    B ASN   A 1 159 ? 3.220  -4.440  1.062   0.28 18.29 ?  159 ASN   A O    1 
ATOM   3287 C  CB   A ASN   A 1 159 ? 2.337  -0.928  0.914   0.72 24.53 ?  159 ASN   A CB   1 
ATOM   3288 C  CB   B ASN   A 1 159 ? 2.322  -1.167  0.696   0.28 21.38 ?  159 ASN   A CB   1 
ATOM   3289 C  CG   A ASN   A 1 159 ? 1.126  -0.130  1.359   0.72 26.93 ?  159 ASN   A CG   1 
ATOM   3290 C  CG   B ASN   A 1 159 ? 1.115  -0.342  1.107   0.28 22.57 ?  159 ASN   A CG   1 
ATOM   3291 O  OD1  A ASN   A 1 159 ? 0.221  -0.668  1.994   0.72 27.99 ?  159 ASN   A OD1  1 
ATOM   3292 O  OD1  B ASN   A 1 159 ? 0.611  -0.476  2.222   0.28 22.81 ?  159 ASN   A OD1  1 
ATOM   3293 N  ND2  A ASN   A 1 159 ? 1.103  1.157   1.030   0.72 27.64 ?  159 ASN   A ND2  1 
ATOM   3294 N  ND2  B ASN   A 1 159 ? 0.646  0.518   0.206   0.28 23.12 ?  159 ASN   A ND2  1 
ATOM   3295 H  H    A ASN   A 1 159 ? 3.556  -0.356  2.947   0.72 26.72 ?  159 ASN   A H    1 
ATOM   3296 H  H    B ASN   A 1 159 ? 3.531  -0.677  2.748   0.28 24.47 ?  159 ASN   A H    1 
ATOM   3297 H  HA   A ASN   A 1 159 ? 2.028  -2.364  2.338   0.72 26.91 ?  159 ASN   A HA   1 
ATOM   3298 H  HA   B ASN   A 1 159 ? 1.911  -2.614  2.081   0.28 24.08 ?  159 ASN   A HA   1 
ATOM   3299 H  HB2  A ASN   A 1 159 ? 3.052  -0.303  0.720   0.72 29.43 ?  159 ASN   A HB2  1 
ATOM   3300 H  HB2  B ASN   A 1 159 ? 3.059  -0.554  0.548   0.28 25.66 ?  159 ASN   A HB2  1 
ATOM   3301 H  HB3  A ASN   A 1 159 ? 2.096  -1.419  0.114   0.72 29.43 ?  159 ASN   A HB3  1 
ATOM   3302 H  HB3  B ASN   A 1 159 ? 2.103  -1.630  -0.126  0.28 25.66 ?  159 ASN   A HB3  1 
ATOM   3303 H  HD21 A ASN   A 1 159 ? 0.437  1.649   1.263   0.72 33.17 ?  159 ASN   A HD21 1 
ATOM   3304 H  HD21 B ASN   A 1 159 ? -0.035 1.011   0.388   0.28 27.74 ?  159 ASN   A HD21 1 
ATOM   3305 H  HD22 A ASN   A 1 159 ? 1.756  1.498   0.588   0.72 33.17 ?  159 ASN   A HD22 1 
ATOM   3306 H  HD22 B ASN   A 1 159 ? 1.029  0.591   -0.561  0.28 27.74 ?  159 ASN   A HD22 1 
ATOM   3307 N  N    A LEU   A 1 160 ? 5.004  -2.669  1.221   0.72 20.06 ?  160 LEU   A N    1 
ATOM   3308 N  N    B LEU   A 1 160 ? 4.857  -2.916  0.811   0.28 17.03 ?  160 LEU   A N    1 
ATOM   3309 C  CA   A LEU   A 1 160 ? 5.936  -3.663  0.699   0.72 19.37 ?  160 LEU   A CA   1 
ATOM   3310 C  CA   B LEU   A 1 160 ? 5.780  -3.904  0.258   0.28 16.18 ?  160 LEU   A CA   1 
ATOM   3311 C  C    A LEU   A 1 160 ? 6.148  -4.798  1.691   0.72 18.40 ?  160 LEU   A C    1 
ATOM   3312 C  C    B LEU   A 1 160 ? 6.098  -4.994  1.276   0.28 15.90 ?  160 LEU   A C    1 
ATOM   3313 O  O    A LEU   A 1 160 ? 6.205  -5.969  1.298   0.72 19.23 ?  160 LEU   A O    1 
ATOM   3314 O  O    B LEU   A 1 160 ? 6.201  -6.174  0.920   0.28 16.10 ?  160 LEU   A O    1 
ATOM   3315 C  CB   A LEU   A 1 160 ? 7.265  -3.008  0.334   0.72 19.67 ?  160 LEU   A CB   1 
ATOM   3316 C  CB   B LEU   A 1 160 ? 7.059  -3.218  -0.223  0.28 15.78 ?  160 LEU   A CB   1 
ATOM   3317 C  CG   A LEU   A 1 160 ? 8.331  -4.020  -0.093  0.72 20.37 ?  160 LEU   A CG   1 
ATOM   3318 C  CG   B LEU   A 1 160 ? 6.920  -2.319  -1.455  0.28 15.70 ?  160 LEU   A CG   1 
ATOM   3319 C  CD1  A LEU   A 1 160 ? 7.871  -4.795  -1.315  0.72 20.96 ?  160 LEU   A CD1  1 
ATOM   3320 C  CD1  B LEU   A 1 160 ? 8.197  -1.534  -1.706  0.28 15.48 ?  160 LEU   A CD1  1 
ATOM   3321 C  CD2  A LEU   A 1 160 ? 9.658  -3.334  -0.355  0.72 20.75 ?  160 LEU   A CD2  1 
ATOM   3322 C  CD2  B LEU   A 1 160 ? 6.559  -3.154  -2.676  0.28 16.00 ?  160 LEU   A CD2  1 
ATOM   3323 H  H    A LEU   A 1 160 ? 5.355  -1.903  1.406   0.72 24.07 ?  160 LEU   A H    1 
ATOM   3324 H  H    B LEU   A 1 160 ? 5.174  -2.120  0.871   0.28 20.44 ?  160 LEU   A H    1 
ATOM   3325 H  HA   A LEU   A 1 160 ? 5.561  -4.040  -0.105  0.72 23.24 ?  160 LEU   A HA   1 
ATOM   3326 H  HA   B LEU   A 1 160 ? 5.360  -4.326  -0.506  0.28 19.42 ?  160 LEU   A HA   1 
ATOM   3327 H  HB2  A LEU   A 1 160 ? 7.125  -2.385  -0.401  0.72 23.61 ?  160 LEU   A HB2  1 
ATOM   3328 H  HB2  B LEU   A 1 160 ? 7.400  -2.668  0.497   0.28 18.93 ?  160 LEU   A HB2  1 
ATOM   3329 H  HB3  A LEU   A 1 160 ? 7.606  -2.534  1.107   0.72 23.61 ?  160 LEU   A HB3  1 
ATOM   3330 H  HB3  B LEU   A 1 160 ? 7.708  -3.905  -0.440  0.28 18.93 ?  160 LEU   A HB3  1 
ATOM   3331 H  HG   A LEU   A 1 160 ? 8.476  -4.655  0.624   0.72 24.44 ?  160 LEU   A HG   1 
ATOM   3332 H  HG   B LEU   A 1 160 ? 6.201  -1.686  -1.304  0.28 18.84 ?  160 LEU   A HG   1 
ATOM   3333 H  HD11 A LEU   A 1 160 ? 8.606  -5.338  -1.635  0.72 25.15 ?  160 LEU   A HD11 1 
ATOM   3334 H  HD11 B LEU   A 1 160 ? 8.075  -0.974  -2.490  0.28 18.57 ?  160 LEU   A HD11 1 
ATOM   3335 H  HD12 A LEU   A 1 160 ? 7.124  -5.363  -1.068  0.72 25.15 ?  160 LEU   A HD12 1 
ATOM   3336 H  HD12 B LEU   A 1 160 ? 8.383  -0.980  -0.931  0.28 18.57 ?  160 LEU   A HD12 1 
ATOM   3337 H  HD13 A LEU   A 1 160 ? 7.597  -4.167  -2.002  0.72 25.15 ?  160 LEU   A HD13 1 
ATOM   3338 H  HD13 B LEU   A 1 160 ? 8.927  -2.155  -1.853  0.28 18.57 ?  160 LEU   A HD13 1 
ATOM   3339 H  HD21 A LEU   A 1 160 ? 10.311 -4.003  -0.620  0.72 24.90 ?  160 LEU   A HD21 1 
ATOM   3340 H  HD21 B LEU   A 1 160 ? 6.618  -2.597  -3.467  0.28 19.20 ?  160 LEU   A HD21 1 
ATOM   3341 H  HD22 A LEU   A 1 160 ? 9.544  -2.684  -1.065  0.72 24.90 ?  160 LEU   A HD22 1 
ATOM   3342 H  HD22 B LEU   A 1 160 ? 7.180  -3.896  -2.746  0.28 19.20 ?  160 LEU   A HD22 1 
ATOM   3343 H  HD23 A LEU   A 1 160 ? 9.951  -2.891  0.457   0.72 24.90 ?  160 LEU   A HD23 1 
ATOM   3344 H  HD23 B LEU   A 1 160 ? 5.654  -3.490  -2.575  0.28 19.20 ?  160 LEU   A HD23 1 
ATOM   3345 N  N    A TYR   A 1 161 ? 6.271  -4.475  2.979   0.72 17.50 ?  161 TYR   A N    1 
ATOM   3346 N  N    B TYR   A 1 161 ? 6.260  -4.617  2.548   0.28 15.83 ?  161 TYR   A N    1 
ATOM   3347 C  CA   A TYR   A 1 161 ? 6.416  -5.522  3.984   0.72 17.30 ?  161 TYR   A CA   1 
ATOM   3348 C  CA   B TYR   A 1 161 ? 6.443  -5.608  3.606   0.28 16.22 ?  161 TYR   A CA   1 
ATOM   3349 C  C    A TYR   A 1 161 ? 5.285  -6.544  3.894   0.72 17.72 ?  161 TYR   A C    1 
ATOM   3350 C  C    B TYR   A 1 161 ? 5.280  -6.586  3.635   0.28 16.68 ?  161 TYR   A C    1 
ATOM   3351 O  O    A TYR   A 1 161 ? 5.518  -7.755  3.958   0.72 18.06 ?  161 TYR   A O    1 
ATOM   3352 O  O    B TYR   A 1 161 ? 5.477  -7.804  3.565   0.28 15.98 ?  161 TYR   A O    1 
ATOM   3353 C  CB   A TYR   A 1 161 ? 6.483  -4.905  5.381   0.72 17.62 ?  161 TYR   A CB   1 
ATOM   3354 C  CB   B TYR   A 1 161 ? 6.592  -4.904  4.956   0.28 16.21 ?  161 TYR   A CB   1 
ATOM   3355 C  CG   A TYR   A 1 161 ? 6.407  -5.946  6.452   0.72 17.65 ?  161 TYR   A CG   1 
ATOM   3356 C  CG   B TYR   A 1 161 ? 6.468  -5.797  6.178   0.28 16.27 ?  161 TYR   A CG   1 
ATOM   3357 C  CD1  A TYR   A 1 161 ? 7.538  -6.646  6.838   0.72 17.75 ?  161 TYR   A CD1  1 
ATOM   3358 C  CD1  B TYR   A 1 161 ? 7.559  -6.512  6.657   0.28 16.39 ?  161 TYR   A CD1  1 
ATOM   3359 C  CD2  A TYR   A 1 161 ? 5.198  -6.259  7.054   0.72 17.59 ?  161 TYR   A CD2  1 
ATOM   3360 C  CD2  B TYR   A 1 161 ? 5.265  -5.902  6.870   0.28 16.23 ?  161 TYR   A CD2  1 
ATOM   3361 C  CE1  A TYR   A 1 161 ? 7.471  -7.617  7.798   0.72 17.94 ?  161 TYR   A CE1  1 
ATOM   3362 C  CE1  B TYR   A 1 161 ? 7.452  -7.320  7.779   0.28 16.46 ?  161 TYR   A CE1  1 
ATOM   3363 C  CE2  A TYR   A 1 161 ? 5.119  -7.226  8.017   0.72 17.86 ?  161 TYR   A CE2  1 
ATOM   3364 C  CE2  B TYR   A 1 161 ? 5.149  -6.709  7.993   0.28 16.34 ?  161 TYR   A CE2  1 
ATOM   3365 C  CZ   A TYR   A 1 161 ? 6.262  -7.902  8.384   0.72 18.30 ?  161 TYR   A CZ   1 
ATOM   3366 C  CZ   B TYR   A 1 161 ? 6.245  -7.413  8.442   0.28 16.81 ?  161 TYR   A CZ   1 
ATOM   3367 O  OH   A TYR   A 1 161 ? 6.200  -8.869  9.348   0.72 19.27 ?  161 TYR   A OH   1 
ATOM   3368 O  OH   B TYR   A 1 161 ? 6.131  -8.214  9.557   0.28 17.59 ?  161 TYR   A OH   1 
ATOM   3369 H  H    A TYR   A 1 161 ? 6.268  -3.671  3.293   0.72 21.00 ?  161 TYR   A H    1 
ATOM   3370 H  H    B TYR   A 1 161 ? 6.262  -3.807  2.818   0.28 19.00 ?  161 TYR   A H    1 
ATOM   3371 H  HA   A TYR   A 1 161 ? 7.250  -5.986  3.833   0.72 20.77 ?  161 TYR   A HA   1 
ATOM   3372 H  HA   B TYR   A 1 161 ? 7.253  -6.113  3.436   0.28 19.47 ?  161 TYR   A HA   1 
ATOM   3373 H  HB2  A TYR   A 1 161 ? 7.324  -4.428  5.482   0.72 21.14 ?  161 TYR   A HB2  1 
ATOM   3374 H  HB2  B TYR   A 1 161 ? 7.468  -4.491  4.988   0.28 19.46 ?  161 TYR   A HB2  1 
ATOM   3375 H  HB3  A TYR   A 1 161 ? 5.739  -4.292  5.501   0.72 21.14 ?  161 TYR   A HB3  1 
ATOM   3376 H  HB3  B TYR   A 1 161 ? 5.907  -4.224  5.023   0.28 19.46 ?  161 TYR   A HB3  1 
ATOM   3377 H  HD1  A TYR   A 1 161 ? 8.354  -6.453  6.439   0.72 21.30 ?  161 TYR   A HD1  1 
ATOM   3378 H  HD1  B TYR   A 1 161 ? 8.373  -6.455  6.214   0.28 19.67 ?  161 TYR   A HD1  1 
ATOM   3379 H  HD2  A TYR   A 1 161 ? 4.426  -5.803  6.802   0.72 21.11 ?  161 TYR   A HD2  1 
ATOM   3380 H  HD2  B TYR   A 1 161 ? 4.521  -5.430  6.573   0.28 19.48 ?  161 TYR   A HD2  1 
ATOM   3381 H  HE1  A TYR   A 1 161 ? 8.235  -8.083  8.053   0.72 21.53 ?  161 TYR   A HE1  1 
ATOM   3382 H  HE1  B TYR   A 1 161 ? 8.190  -7.796  8.087   0.28 19.76 ?  161 TYR   A HE1  1 
ATOM   3383 H  HE2  A TYR   A 1 161 ? 4.297  -7.431  8.418   0.72 21.44 ?  161 TYR   A HE2  1 
ATOM   3384 H  HE2  B TYR   A 1 161 ? 4.335  -6.770  8.446   0.28 19.62 ?  161 TYR   A HE2  1 
ATOM   3385 H  HH   A TYR   A 1 161 ? 6.951  -9.215  9.477   0.72 23.13 ?  161 TYR   A HH   1 
ATOM   3386 H  HH   B TYR   A 1 161 ? 6.863  -8.583  9.732   0.28 21.11 ?  161 TYR   A HH   1 
ATOM   3387 N  N    . ASP   A 1 162 ? 4.051  -6.073  3.732   1.00 18.05 ?  162 ASP   A N    1 
ATOM   3388 C  CA   . ASP   A 1 162 ? 2.903  -6.973  3.700   1.00 19.02 ?  162 ASP   A CA   1 
ATOM   3389 C  C    . ASP   A 1 162 ? 2.941  -7.852  2.453   1.00 19.26 ?  162 ASP   A C    1 
ATOM   3390 O  O    . ASP   A 1 162 ? 2.598  -9.040  2.509   1.00 19.70 ?  162 ASP   A O    1 
ATOM   3391 C  CB   . ASP   A 1 162 ? 1.599  -6.172  3.753   1.00 20.34 ?  162 ASP   A CB   1 
ATOM   3392 C  CG   . ASP   A 1 162 ? 1.289  -5.612  5.131   1.00 21.87 ?  162 ASP   A CG   1 
ATOM   3393 O  OD1  . ASP   A 1 162 ? 1.932  -6.011  6.119   1.00 22.67 ?  162 ASP   A OD1  1 
ATOM   3394 O  OD2  . ASP   A 1 162 ? 0.361  -4.775  5.217   1.00 23.36 -1 162 ASP   A OD2  1 
ATOM   3395 H  H    A ASP   A 1 162 ? 3.852  -5.247  3.635   0.72 21.66 ?  162 ASP   A H    1 
ATOM   3396 H  H    B ASP   A 1 162 ? 3.862  -5.242  3.814   0.28 21.66 ?  162 ASP   A H    1 
ATOM   3397 H  HA   . ASP   A 1 162 ? 2.927  -7.559  4.471   1.00 22.83 ?  162 ASP   A HA   1 
ATOM   3398 H  HB2  . ASP   A 1 162 ? 1.658  -5.421  3.152   1.00 24.41 ?  162 ASP   A HB2  1 
ATOM   3399 H  HB3  . ASP   A 1 162 ? 0.858  -6.747  3.508   1.00 24.41 ?  162 ASP   A HB3  1 
ATOM   3400 N  N    A LYS   A 1 163 ? 3.359  -7.287  1.318   0.72 20.18 ?  163 LYS   A N    1 
ATOM   3401 N  N    B LYS   A 1 163 ? 3.365  -7.289  1.320   0.28 19.79 ?  163 LYS   A N    1 
ATOM   3402 C  CA   A LYS   A 1 163 ? 3.454  -8.077  0.095   0.72 20.72 ?  163 LYS   A CA   1 
ATOM   3403 C  CA   B LYS   A 1 163 ? 3.452  -8.073  0.092   0.28 20.31 ?  163 LYS   A CA   1 
ATOM   3404 C  C    A LYS   A 1 163 ? 4.549  -9.128  0.203   0.72 20.12 ?  163 LYS   A C    1 
ATOM   3405 C  C    B LYS   A 1 163 ? 4.559  -9.117  0.180   0.28 19.53 ?  163 LYS   A C    1 
ATOM   3406 O  O    A LYS   A 1 163 ? 4.388  -10.254 -0.280  0.72 21.20 ?  163 LYS   A O    1 
ATOM   3407 O  O    B LYS   A 1 163 ? 4.413  -10.230 -0.337  0.28 19.83 ?  163 LYS   A O    1 
ATOM   3408 C  CB   A LYS   A 1 163 ? 3.699  -7.158  -1.102  0.72 22.94 ?  163 LYS   A CB   1 
ATOM   3409 C  CB   B LYS   A 1 163 ? 3.680  -7.139  -1.096  0.28 22.12 ?  163 LYS   A CB   1 
ATOM   3410 C  CG   A LYS   A 1 163 ? 3.755  -7.876  -2.438  0.72 25.69 ?  163 LYS   A CG   1 
ATOM   3411 C  CG   B LYS   A 1 163 ? 3.654  -7.816  -2.454  0.28 24.07 ?  163 LYS   A CG   1 
ATOM   3412 C  CD   A LYS   A 1 163 ? 4.124  -6.916  -3.555  0.72 28.12 ?  163 LYS   A CD   1 
ATOM   3413 C  CD   B LYS   A 1 163 ? 3.929  -6.806  -3.555  0.28 25.81 ?  163 LYS   A CD   1 
ATOM   3414 C  CE   A LYS   A 1 163 ? 3.999  -7.573  -4.919  0.72 29.68 ?  163 LYS   A CE   1 
ATOM   3415 C  CE   B LYS   A 1 163 ? 3.875  -7.441  -4.932  0.28 26.95 ?  163 LYS   A CE   1 
ATOM   3416 N  NZ   A LYS   A 1 163 ? 4.617  -6.747  -5.992  0.72 30.51 ?  163 LYS   A NZ   1 
ATOM   3417 N  NZ   B LYS   A 1 163 ? 4.538  -6.582  -5.953  0.28 27.59 ?  163 LYS   A NZ   1 
ATOM   3418 H  H    A LYS   A 1 163 ? 3.585  -6.462  1.233   0.72 24.21 ?  163 LYS   A H    1 
ATOM   3419 H  H    B LYS   A 1 163 ? 3.599  -6.466  1.238   0.28 23.75 ?  163 LYS   A H    1 
ATOM   3420 H  HA   A LYS   A 1 163 ? 2.611  -8.536  -0.051  0.72 24.86 ?  163 LYS   A HA   1 
ATOM   3421 H  HA   B LYS   A 1 163 ? 2.612  -8.536  -0.049  0.28 24.38 ?  163 LYS   A HA   1 
ATOM   3422 H  HB2  A LYS   A 1 163 ? 2.978  -6.508  -1.149  0.72 27.53 ?  163 LYS   A HB2  1 
ATOM   3423 H  HB2  B LYS   A 1 163 ? 2.985  -6.462  -1.095  0.28 26.55 ?  163 LYS   A HB2  1 
ATOM   3424 H  HB3  A LYS   A 1 163 ? 4.543  -6.702  -0.977  0.72 27.53 ?  163 LYS   A HB3  1 
ATOM   3425 H  HB3  B LYS   A 1 163 ? 4.547  -6.718  -0.997  0.28 26.55 ?  163 LYS   A HB3  1 
ATOM   3426 H  HG2  A LYS   A 1 163 ? 4.426  -8.574  -2.404  0.72 30.83 ?  163 LYS   A HG2  1 
ATOM   3427 H  HG2  B LYS   A 1 163 ? 4.341  -8.501  -2.489  0.28 28.89 ?  163 LYS   A HG2  1 
ATOM   3428 H  HG3  A LYS   A 1 163 ? 2.883  -8.255  -2.636  0.72 30.83 ?  163 LYS   A HG3  1 
ATOM   3429 H  HG3  B LYS   A 1 163 ? 2.779  -8.207  -2.605  0.28 28.89 ?  163 LYS   A HG3  1 
ATOM   3430 H  HD2  A LYS   A 1 163 ? 3.526  -6.151  -3.531  0.72 33.74 ?  163 LYS   A HD2  1 
ATOM   3431 H  HD2  B LYS   A 1 163 ? 3.258  -6.105  -3.518  0.28 30.98 ?  163 LYS   A HD2  1 
ATOM   3432 H  HD3  A LYS   A 1 163 ? 5.042  -6.627  -3.438  0.72 33.74 ?  163 LYS   A HD3  1 
ATOM   3433 H  HD3  B LYS   A 1 163 ? 4.813  -6.428  -3.428  0.28 30.98 ?  163 LYS   A HD3  1 
ATOM   3434 H  HE2  A LYS   A 1 163 ? 4.436  -8.436  -4.907  0.72 35.62 ?  163 LYS   A HE2  1 
ATOM   3435 H  HE2  B LYS   A 1 163 ? 4.326  -8.298  -4.910  0.28 32.34 ?  163 LYS   A HE2  1 
ATOM   3436 H  HE3  A LYS   A 1 163 ? 3.060  -7.684  -5.129  0.72 35.62 ?  163 LYS   A HE3  1 
ATOM   3437 H  HE3  B LYS   A 1 163 ? 2.948  -7.558  -5.192  0.28 32.34 ?  163 LYS   A HE3  1 
ATOM   3438 H  HZ1  A LYS   A 1 163 ? 4.530  -7.155  -6.778  0.72 36.61 ?  163 LYS   A HZ1  1 
ATOM   3439 H  HZ1  B LYS   A 1 163 ? 4.496  -6.972  -6.752  0.28 33.11 ?  163 LYS   A HZ1  1 
ATOM   3440 H  HZ2  A LYS   A 1 163 ? 4.214  -5.953  -6.033  0.72 36.61 ?  163 LYS   A HZ2  1 
ATOM   3441 H  HZ2  B LYS   A 1 163 ? 4.132  -5.791  -5.995  0.28 33.11 ?  163 LYS   A HZ2  1 
ATOM   3442 H  HZ3  A LYS   A 1 163 ? 5.481  -6.623  -5.823  0.72 36.61 ?  163 LYS   A HZ3  1 
ATOM   3443 H  HZ3  B LYS   A 1 163 ? 5.392  -6.457  -5.737  0.28 33.11 ?  163 LYS   A HZ3  1 
ATOM   3444 N  N    . LEU   A 1 164 ? 5.675  -8.772  0.827   1.00 18.67 ?  164 LEU   A N    1 
ATOM   3445 C  CA   . LEU   A 1 164 ? 6.778  -9.721  0.981   1.00 17.77 ?  164 LEU   A CA   1 
ATOM   3446 C  C    . LEU   A 1 164 ? 6.368  -10.904 1.845   1.00 17.94 ?  164 LEU   A C    1 
ATOM   3447 O  O    . LEU   A 1 164 ? 6.683  -12.059 1.533   1.00 18.66 ?  164 LEU   A O    1 
ATOM   3448 C  CB   . LEU   A 1 164 ? 7.960  -9.003  1.623   1.00 17.24 ?  164 LEU   A CB   1 
ATOM   3449 C  CG   . LEU   A 1 164 ? 8.723  -8.032  0.724   1.00 17.81 ?  164 LEU   A CG   1 
ATOM   3450 C  CD1  . LEU   A 1 164 ? 9.603  -7.098  1.541   1.00 17.85 ?  164 LEU   A CD1  1 
ATOM   3451 C  CD2  . LEU   A 1 164 ? 9.559  -8.787  -0.277  1.00 18.31 ?  164 LEU   A CD2  1 
ATOM   3452 H  H    A LEU   A 1 164 ? 5.822  -7.995  1.171   0.72 22.40 ?  164 LEU   A H    1 
ATOM   3453 H  H    B LEU   A 1 164 ? 5.818  -7.999  1.181   0.28 22.40 ?  164 LEU   A H    1 
ATOM   3454 H  HA   . LEU   A 1 164 ? 7.050  -10.047 0.111   1.00 21.33 ?  164 LEU   A HA   1 
ATOM   3455 H  HB2  . LEU   A 1 164 ? 7.637  -8.490  2.382   1.00 20.69 ?  164 LEU   A HB2  1 
ATOM   3456 H  HB3  . LEU   A 1 164 ? 8.597  -9.665  1.929   1.00 20.69 ?  164 LEU   A HB3  1 
ATOM   3457 H  HG   . LEU   A 1 164 ? 8.093  -7.485  0.231   1.00 21.37 ?  164 LEU   A HG   1 
ATOM   3458 H  HD11 . LEU   A 1 164 ? 10.099 -6.518  0.941   1.00 21.42 ?  164 LEU   A HD11 1 
ATOM   3459 H  HD12 . LEU   A 1 164 ? 9.041  -6.561  2.124   1.00 21.42 ?  164 LEU   A HD12 1 
ATOM   3460 H  HD13 . LEU   A 1 164 ? 10.219 -7.625  2.074   1.00 21.42 ?  164 LEU   A HD13 1 
ATOM   3461 H  HD21 . LEU   A 1 164 ? 10.056 -8.150  -0.814  1.00 21.97 ?  164 LEU   A HD21 1 
ATOM   3462 H  HD22 . LEU   A 1 164 ? 10.173 -9.366  0.201   1.00 21.97 ?  164 LEU   A HD22 1 
ATOM   3463 H  HD23 . LEU   A 1 164 ? 8.973  -9.312  -0.839  1.00 21.97 ?  164 LEU   A HD23 1 
ATOM   3464 N  N    . VAL   A 1 165 ? 5.670  -10.627 2.944   1.00 18.03 ?  165 VAL   A N    1 
ATOM   3465 C  CA   . VAL   A 1 165 ? 5.182  -11.692 3.810   1.00 17.91 ?  165 VAL   A CA   1 
ATOM   3466 C  C    . VAL   A 1 165 ? 4.152  -12.542 3.076   1.00 18.03 ?  165 VAL   A C    1 
ATOM   3467 O  O    . VAL   A 1 165 ? 4.251  -13.775 3.032   1.00 17.60 ?  165 VAL   A O    1 
ATOM   3468 C  CB   . VAL   A 1 165 ? 4.598  -11.084 5.097   1.00 18.59 ?  165 VAL   A CB   1 
ATOM   3469 C  CG1  . VAL   A 1 165 ? 3.836  -12.137 5.888   1.00 18.88 ?  165 VAL   A CG1  1 
ATOM   3470 C  CG2  . VAL   A 1 165 ? 5.698  -10.447 5.933   1.00 19.54 ?  165 VAL   A CG2  1 
ATOM   3471 H  H    . VAL   A 1 165 ? 5.469  -9.836  3.210   1.00 21.64 ?  165 VAL   A H    1 
ATOM   3472 H  HA   . VAL   A 1 165 ? 5.920  -12.269 4.061   1.00 21.50 ?  165 VAL   A HA   1 
ATOM   3473 H  HB   . VAL   A 1 165 ? 3.969  -10.386 4.854   1.00 22.31 ?  165 VAL   A HB   1 
ATOM   3474 H  HG11 . VAL   A 1 165 ? 3.723  -11.822 6.798   1.00 22.65 ?  165 VAL   A HG11 1 
ATOM   3475 H  HG12 . VAL   A 1 165 ? 2.963  -12.270 5.478   1.00 22.65 ?  165 VAL   A HG12 1 
ATOM   3476 H  HG13 . VAL   A 1 165 ? 4.338  -12.962 5.880   1.00 22.65 ?  165 VAL   A HG13 1 
ATOM   3477 H  HG21 . VAL   A 1 165 ? 5.307  -10.071 6.737   1.00 23.45 ?  165 VAL   A HG21 1 
ATOM   3478 H  HG22 . VAL   A 1 165 ? 6.350  -11.125 6.166   1.00 23.45 ?  165 VAL   A HG22 1 
ATOM   3479 H  HG23 . VAL   A 1 165 ? 6.122  -9.745  5.412   1.00 23.45 ?  165 VAL   A HG23 1 
ATOM   3480 N  N    . SER   A 1 166 ? 3.150  -11.892 2.481   1.00 18.71 ?  166 SER   A N    1 
ATOM   3481 C  CA   . SER   A 1 166 ? 2.022  -12.628 1.922   1.00 19.98 ?  166 SER   A CA   1 
ATOM   3482 C  C    . SER   A 1 166 ? 2.431  -13.508 0.753   1.00 20.72 ?  166 SER   A C    1 
ATOM   3483 O  O    . SER   A 1 166 ? 1.792  -14.540 0.509   1.00 23.07 ?  166 SER   A O    1 
ATOM   3484 C  CB   . SER   A 1 166 ? 0.924  -11.658 1.484   1.00 21.69 ?  166 SER   A CB   1 
ATOM   3485 O  OG   . SER   A 1 166 ? 0.263  -11.093 2.601   1.00 23.86 ?  166 SER   A OG   1 
ATOM   3486 H  H    . SER   A 1 166 ? 3.096  -11.042 2.395   1.00 22.46 ?  166 SER   A H    1 
ATOM   3487 H  HA   . SER   A 1 166 ? 1.645  -13.207 2.600   1.00 23.98 ?  166 SER   A HA   1 
ATOM   3488 H  HB2  . SER   A 1 166 ? 1.314  -10.950 0.951   1.00 26.04 ?  166 SER   A HB2  1 
ATOM   3489 H  HB3  . SER   A 1 166 ? 0.260  -12.138 0.959   1.00 26.04 ?  166 SER   A HB3  1 
ATOM   3490 H  HG   . SER   A 1 166 ? -0.325 -10.549 2.349   1.00 28.64 ?  166 SER   A HG   1 
ATOM   3491 N  N    . SER   A 1 167 ? 3.481  -13.129 0.026   1.00 20.09 ?  167 SER   A N    1 
ATOM   3492 C  CA   . SER   A 1 167 ? 3.910  -13.863 -1.155  1.00 20.80 ?  167 SER   A CA   1 
ATOM   3493 C  C    . SER   A 1 167 ? 5.062  -14.816 -0.871  1.00 20.74 ?  167 SER   A C    1 
ATOM   3494 O  O    . SER   A 1 167 ? 5.585  -15.430 -1.806  1.00 21.65 ?  167 SER   A O    1 
ATOM   3495 C  CB   . SER   A 1 167 ? 4.303  -12.891 -2.273  1.00 21.96 ?  167 SER   A CB   1 
ATOM   3496 O  OG   . SER   A 1 167 ? 5.419  -12.105 -1.891  1.00 22.11 ?  167 SER   A OG   1 
ATOM   3497 H  H    . SER   A 1 167 ? 3.972  -12.438 0.205   1.00 24.11 ?  167 SER   A H    1 
ATOM   3498 H  HA   . SER   A 1 167 ? 3.161  -14.385 -1.477  1.00 24.96 ?  167 SER   A HA   1 
ATOM   3499 H  HB2  . SER   A 1 167 ? 4.534  -13.401 -3.067  1.00 26.35 ?  167 SER   A HB2  1 
ATOM   3500 H  HB3  . SER   A 1 167 ? 3.549  -12.308 -2.467  1.00 26.35 ?  167 SER   A HB3  1 
ATOM   3501 H  HG   . SER   A 1 167 ? 5.225  -11.646 -1.212  1.00 26.53 ?  167 SER   A HG   1 
ATOM   3502 N  N    . PHE   A 1 168 ? 5.474  -14.952 0.385   1.00 19.87 ?  168 PHE   A N    1 
ATOM   3503 C  CA   . PHE   A 1 168 ? 6.668  -15.728 0.692   1.00 20.07 ?  168 PHE   A CA   1 
ATOM   3504 C  C    . PHE   A 1 168 ? 6.382  -17.218 0.601   1.00 22.24 ?  168 PHE   A C    1 
ATOM   3505 O  O    . PHE   A 1 168 ? 5.435  -17.722 1.217   1.00 23.24 ?  168 PHE   A O    1 
ATOM   3506 C  CB   . PHE   A 1 168 ? 7.191  -15.414 2.089   1.00 18.88 ?  168 PHE   A CB   1 
ATOM   3507 C  CG   . PHE   A 1 168 ? 8.467  -16.136 2.405   1.00 17.79 ?  168 PHE   A CG   1 
ATOM   3508 C  CD1  . PHE   A 1 168 ? 9.643  -15.753 1.796   1.00 18.22 ?  168 PHE   A CD1  1 
ATOM   3509 C  CD2  . PHE   A 1 168 ? 8.492  -17.220 3.269   1.00 17.24 ?  168 PHE   A CD2  1 
ATOM   3510 C  CE1  . PHE   A 1 168 ? 10.821 -16.412 2.057   1.00 17.79 ?  168 PHE   A CE1  1 
ATOM   3511 C  CE2  . PHE   A 1 168 ? 9.678  -17.879 3.534   1.00 17.20 ?  168 PHE   A CE2  1 
ATOM   3512 C  CZ   . PHE   A 1 168 ? 10.838 -17.475 2.923   1.00 17.32 ?  168 PHE   A CZ   1 
ATOM   3513 H  H    . PHE   A 1 168 ? 5.092  -14.599 1.068   1.00 23.84 ?  168 PHE   A H    1 
ATOM   3514 H  HA   . PHE   A 1 168 ? 7.365  -15.509 0.050   1.00 24.08 ?  168 PHE   A HA   1 
ATOM   3515 H  HB2  . PHE   A 1 168 ? 7.361  -14.461 2.154   1.00 22.66 ?  168 PHE   A HB2  1 
ATOM   3516 H  HB3  . PHE   A 1 168 ? 6.523  -15.678 2.740   1.00 22.66 ?  168 PHE   A HB3  1 
ATOM   3517 H  HD1  . PHE   A 1 168 ? 9.640  -15.031 1.209   1.00 21.86 ?  168 PHE   A HD1  1 
ATOM   3518 H  HD2  . PHE   A 1 168 ? 7.703  -17.497 3.682   1.00 20.69 ?  168 PHE   A HD2  1 
ATOM   3519 H  HE1  . PHE   A 1 168 ? 11.612 -16.136 1.648   1.00 21.35 ?  168 PHE   A HE1  1 
ATOM   3520 H  HE2  . PHE   A 1 168 ? 9.685  -18.603 4.120   1.00 20.64 ?  168 PHE   A HE2  1 
ATOM   3521 H  HZ   . PHE   A 1 168 ? 11.639 -17.918 3.102   1.00 20.78 ?  168 PHE   A HZ   1 
ATOM   3522 N  N    . LEU   A 1 169 ? 7.236  -17.928 -0.133  1.00 26.29 ?  169 LEU   A N    1 
ATOM   3523 C  CA   . LEU   A 1 169 ? 7.059  -19.355 -0.307  1.00 32.62 ?  169 LEU   A CA   1 
ATOM   3524 C  C    . LEU   A 1 169 ? 7.952  -20.080 0.687   1.00 34.71 ?  169 LEU   A C    1 
ATOM   3525 O  O    . LEU   A 1 169 ? 7.497  -20.474 1.761   1.00 35.98 ?  169 LEU   A O    1 
ATOM   3526 C  CB   . LEU   A 1 169 ? 7.395  -19.769 -1.742  1.00 36.26 ?  169 LEU   A CB   1 
ATOM   3527 C  CG   . LEU   A 1 169 ? 7.055  -21.210 -2.132  1.00 38.57 ?  169 LEU   A CG   1 
ATOM   3528 C  CD1  . LEU   A 1 169 ? 5.646  -21.572 -1.692  1.00 39.62 ?  169 LEU   A CD1  1 
ATOM   3529 C  CD2  . LEU   A 1 169 ? 7.210  -21.403 -3.634  1.00 39.24 ?  169 LEU   A CD2  1 
ATOM   3530 O  OXT  . LEU   A 1 169 ? 9.146  -20.263 0.450   1.00 34.95 -1 169 LEU   A OXT  1 
ATOM   3531 H  H    . LEU   A 1 169 ? 7.930  -17.608 -0.533  1.00 31.55 ?  169 LEU   A H    1 
ATOM   3532 H  HA   . LEU   A 1 169 ? 6.133  -19.578 -0.128  1.00 39.15 ?  169 LEU   A HA   1 
ATOM   3533 H  HB2  . LEU   A 1 169 ? 6.911  -19.187 -2.345  1.00 43.52 ?  169 LEU   A HB2  1 
ATOM   3534 H  HB3  . LEU   A 1 169 ? 8.348  -19.654 -1.876  1.00 43.52 ?  169 LEU   A HB3  1 
ATOM   3535 H  HG   . LEU   A 1 169 ? 7.673  -21.814 -1.690  1.00 46.29 ?  169 LEU   A HG   1 
ATOM   3536 H  HD11 . LEU   A 1 169 ? 5.374  -22.385 -2.142  1.00 47.55 ?  169 LEU   A HD11 1 
ATOM   3537 H  HD12 . LEU   A 1 169 ? 5.640  -21.708 -0.731  1.00 47.55 ?  169 LEU   A HD12 1 
ATOM   3538 H  HD13 . LEU   A 1 169 ? 5.046  -20.847 -1.928  1.00 47.55 ?  169 LEU   A HD13 1 
ATOM   3539 H  HD21 . LEU   A 1 169 ? 6.998  -22.323 -3.858  1.00 47.09 ?  169 LEU   A HD21 1 
ATOM   3540 H  HD22 . LEU   A 1 169 ? 6.600  -20.803 -4.093  1.00 47.09 ?  169 LEU   A HD22 1 
ATOM   3541 H  HD23 . LEU   A 1 169 ? 8.124  -21.203 -3.887  1.00 47.09 ?  169 LEU   A HD23 1 
ATOM   3542 N  N    A SER   B 1 1   ? 50.702 -9.195  -23.752 0.72 28.72 ?  1   SER   B N    1 
ATOM   3543 N  N    B SER   B 1 1   ? 50.700 -9.183  -23.745 0.28 26.86 ?  1   SER   B N    1 
ATOM   3544 C  CA   A SER   B 1 1   ? 51.192 -10.257 -22.851 0.72 28.07 ?  1   SER   B CA   1 
ATOM   3545 C  CA   B SER   B 1 1   ? 51.175 -10.189 -22.772 0.28 26.55 ?  1   SER   B CA   1 
ATOM   3546 C  C    A SER   B 1 1   ? 50.112 -11.292 -22.586 0.72 26.46 ?  1   SER   B C    1 
ATOM   3547 C  C    B SER   B 1 1   ? 50.100 -11.238 -22.528 0.28 26.01 ?  1   SER   B C    1 
ATOM   3548 O  O    A SER   B 1 1   ? 48.920 -11.078 -22.854 0.72 25.94 ?  1   SER   B O    1 
ATOM   3549 O  O    B SER   B 1 1   ? 48.951 -11.087 -22.950 0.28 25.80 ?  1   SER   B O    1 
ATOM   3550 C  CB   A SER   B 1 1   ? 51.663 -9.670  -21.525 0.72 29.07 ?  1   SER   B CB   1 
ATOM   3551 C  CB   B SER   B 1 1   ? 51.557 -9.527  -21.453 0.28 26.84 ?  1   SER   B CB   1 
ATOM   3552 O  OG   A SER   B 1 1   ? 50.558 -9.323  -20.712 0.72 30.59 ?  1   SER   B OG   1 
ATOM   3553 O  OG   B SER   B 1 1   ? 50.474 -9.568  -20.540 0.28 27.24 ?  1   SER   B OG   1 
ATOM   3554 H  H1   A SER   B 1 1   ? 50.531 -9.547  -24.549 0.72 34.46 ?  1   SER   B H1   1 
ATOM   3555 H  H1   B SER   B 1 1   ? 51.392 -8.694  -24.012 0.28 32.24 ?  1   SER   B H1   1 
ATOM   3556 H  H2   A SER   B 1 1   ? 49.964 -8.844  -23.410 0.72 34.46 ?  1   SER   B H2   1 
ATOM   3557 H  H2   B SER   B 1 1   ? 50.339 -9.600  -24.440 0.28 32.24 ?  1   SER   B H2   1 
ATOM   3558 H  H3   A SER   B 1 1   ? 51.330 -8.571  -23.827 0.72 34.46 ?  1   SER   B H3   1 
ATOM   3559 H  H3   B SER   B 1 1   ? 50.096 -8.666  -23.354 0.28 32.24 ?  1   SER   B H3   1 
ATOM   3560 H  HA   A SER   B 1 1   ? 51.942 -10.693 -23.279 0.72 33.69 ?  1   SER   B HA   1 
ATOM   3561 H  HA   B SER   B 1 1   ? 51.956 -10.624 -23.139 0.28 31.86 ?  1   SER   B HA   1 
ATOM   3562 H  HB2  A SER   B 1 1   ? 52.199 -10.336 -21.068 0.72 34.89 ?  1   SER   B HB2  1 
ATOM   3563 H  HB2  B SER   B 1 1   ? 52.309 -10.004 -21.075 0.28 32.22 ?  1   SER   B HB2  1 
ATOM   3564 H  HB3  A SER   B 1 1   ? 52.189 -8.877  -21.698 0.72 34.89 ?  1   SER   B HB3  1 
ATOM   3565 H  HB3  B SER   B 1 1   ? 51.799 -8.602  -21.622 0.28 32.22 ?  1   SER   B HB3  1 
ATOM   3566 H  HG   A SER   B 1 1   ? 50.807 -8.792  -20.111 0.72 36.71 ?  1   SER   B HG   1 
ATOM   3567 H  HG   B SER   B 1 1   ? 50.760 -9.734  -19.769 0.28 32.69 ?  1   SER   B HG   1 
ATOM   3568 N  N    A MET   B 1 2   ? 50.553 -12.412 -22.031 0.72 25.74 ?  2   MET   B N    1 
ATOM   3569 N  N    B MET   B 1 2   ? 50.487 -12.295 -21.822 0.28 25.76 ?  2   MET   B N    1 
ATOM   3570 C  CA   A MET   B 1 2   ? 49.730 -13.598 -21.850 0.72 25.74 ?  2   MET   B CA   1 
ATOM   3571 C  CA   B MET   B 1 2   ? 49.671 -13.492 -21.662 0.28 25.47 ?  2   MET   B CA   1 
ATOM   3572 C  C    A MET   B 1 2   ? 49.497 -13.787 -20.357 0.72 23.36 ?  2   MET   B C    1 
ATOM   3573 C  C    B MET   B 1 2   ? 49.399 -13.696 -20.178 0.28 23.48 ?  2   MET   B C    1 
ATOM   3574 O  O    A MET   B 1 2   ? 50.438 -14.061 -19.607 0.72 23.47 ?  2   MET   B O    1 
ATOM   3575 O  O    B MET   B 1 2   ? 50.294 -14.104 -19.429 0.28 23.68 ?  2   MET   B O    1 
ATOM   3576 C  CB   A MET   B 1 2   ? 50.451 -14.800 -22.448 0.72 29.37 ?  2   MET   B CB   1 
ATOM   3577 C  CB   B MET   B 1 2   ? 50.415 -14.685 -22.252 0.28 27.45 ?  2   MET   B CB   1 
ATOM   3578 C  CG   A MET   B 1 2   ? 49.588 -16.028 -22.662 0.72 32.90 ?  2   MET   B CG   1 
ATOM   3579 C  CG   B MET   B 1 2   ? 49.540 -15.848 -22.681 0.28 29.23 ?  2   MET   B CG   1 
ATOM   3580 S  SD   A MET   B 1 2   ? 50.442 -17.269 -23.652 0.72 36.13 ?  2   MET   B SD   1 
ATOM   3581 S  SD   B MET   B 1 2   ? 50.449 -16.990 -23.733 0.28 30.83 ?  2   MET   B SD   1 
ATOM   3582 C  CE   A MET   B 1 2   ? 51.038 -16.236 -24.984 0.72 36.22 ?  2   MET   B CE   1 
ATOM   3583 C  CE   B MET   B 1 2   ? 51.259 -15.840 -24.834 0.28 30.91 ?  2   MET   B CE   1 
ATOM   3584 H  H    A MET   B 1 2   ? 51.355 -12.516 -21.741 0.72 30.89 ?  2   MET   B H    1 
ATOM   3585 H  H    B MET   B 1 2   ? 51.247 -12.346 -21.422 0.28 30.92 ?  2   MET   B H    1 
ATOM   3586 H  HA   A MET   B 1 2   ? 48.882 -13.494 -22.307 0.72 30.89 ?  2   MET   B HA   1 
ATOM   3587 H  HA   B MET   B 1 2   ? 48.837 -13.392 -22.144 0.28 30.56 ?  2   MET   B HA   1 
ATOM   3588 H  HB2  A MET   B 1 2   ? 50.809 -14.516 -23.299 0.72 35.25 ?  2   MET   B HB2  1 
ATOM   3589 H  HB2  B MET   B 1 2   ? 50.905 -14.351 -23.017 0.28 32.94 ?  2   MET   B HB2  1 
ATOM   3590 H  HB3  A MET   B 1 2   ? 51.176 -15.065 -21.864 0.72 35.25 ?  2   MET   B HB3  1 
ATOM   3591 H  HB3  B MET   B 1 2   ? 51.038 -15.034 -21.602 0.28 32.94 ?  2   MET   B HB3  1 
ATOM   3592 H  HG2  A MET   B 1 2   ? 49.371 -16.417 -21.798 0.72 39.49 ?  2   MET   B HG2  1 
ATOM   3593 H  HG2  B MET   B 1 2   ? 49.240 -16.330 -21.893 0.28 35.08 ?  2   MET   B HG2  1 
ATOM   3594 H  HG3  A MET   B 1 2   ? 48.778 -15.781 -23.132 0.72 39.49 ?  2   MET   B HG3  1 
ATOM   3595 H  HG3  B MET   B 1 2   ? 48.780 -15.524 -23.182 0.28 35.08 ?  2   MET   B HG3  1 
ATOM   3596 H  HE1  A MET   B 1 2   ? 51.203 -16.791 -25.751 0.72 43.47 ?  2   MET   B HE1  1 
ATOM   3597 H  HE1  B MET   B 1 2   ? 51.465 -16.300 -25.649 0.28 37.10 ?  2   MET   B HE1  1 
ATOM   3598 H  HE2  A MET   B 1 2   ? 50.356 -15.573 -25.188 0.72 43.47 ?  2   MET   B HE2  1 
ATOM   3599 H  HE2  B MET   B 1 2   ? 50.658 -15.096 -25.014 0.28 37.10 ?  2   MET   B HE2  1 
ATOM   3600 H  HE3  A MET   B 1 2   ? 51.858 -15.789 -24.709 0.72 43.47 ?  2   MET   B HE3  1 
ATOM   3601 H  HE3  B MET   B 1 2   ? 52.074 -15.514 -24.411 0.28 37.10 ?  2   MET   B HE3  1 
ATOM   3602 N  N    A VAL   B 1 3   ? 48.249 -13.615 -19.929 0.72 21.07 ?  3   VAL   B N    1 
ATOM   3603 N  N    B VAL   B 1 3   ? 48.172 -13.406 -19.753 0.28 21.34 ?  3   VAL   B N    1 
ATOM   3604 C  CA   A VAL   B 1 3   ? 47.837 -13.873 -18.557 0.72 19.90 ?  3   VAL   B CA   1 
ATOM   3605 C  CA   B VAL   B 1 3   ? 47.727 -13.675 -18.391 0.28 19.50 ?  3   VAL   B CA   1 
ATOM   3606 C  C    A VAL   B 1 3   ? 46.603 -14.764 -18.590 0.72 18.05 ?  3   VAL   B C    1 
ATOM   3607 C  C    B VAL   B 1 3   ? 46.475 -14.536 -18.442 0.28 17.67 ?  3   VAL   B C    1 
ATOM   3608 O  O    A VAL   B 1 3   ? 45.891 -14.850 -19.594 0.72 18.69 ?  3   VAL   B O    1 
ATOM   3609 O  O    B VAL   B 1 3   ? 45.637 -14.385 -19.337 0.28 17.43 ?  3   VAL   B O    1 
ATOM   3610 C  CB   A VAL   B 1 3   ? 47.549 -12.573 -17.769 0.72 21.37 ?  3   VAL   B CB   1 
ATOM   3611 C  CB   B VAL   B 1 3   ? 47.478 -12.390 -17.571 0.28 19.70 ?  3   VAL   B CB   1 
ATOM   3612 C  CG1  A VAL   B 1 3   ? 48.812 -11.721 -17.657 0.72 21.75 ?  3   VAL   B CG1  1 
ATOM   3613 C  CG1  B VAL   B 1 3   ? 48.757 -11.576 -17.450 0.28 19.82 ?  3   VAL   B CG1  1 
ATOM   3614 C  CG2  A VAL   B 1 3   ? 46.415 -11.792 -18.420 0.72 22.27 ?  3   VAL   B CG2  1 
ATOM   3615 C  CG2  B VAL   B 1 3   ? 46.356 -11.564 -18.182 0.28 19.76 ?  3   VAL   B CG2  1 
ATOM   3616 H  H    A VAL   B 1 3   ? 47.608 -13.346 -20.432 0.72 25.29 ?  3   VAL   B H    1 
ATOM   3617 H  H    B VAL   B 1 3   ? 47.570 -13.047 -20.254 0.28 25.61 ?  3   VAL   B H    1 
ATOM   3618 H  HA   A VAL   B 1 3   ? 48.547 -14.352 -18.095 0.72 23.88 ?  3   VAL   B HA   1 
ATOM   3619 H  HA   B VAL   B 1 3   ? 48.411 -14.185 -17.938 0.28 23.41 ?  3   VAL   B HA   1 
ATOM   3620 H  HB   A VAL   B 1 3   ? 47.272 -12.811 -16.869 0.72 25.64 ?  3   VAL   B HB   1 
ATOM   3621 H  HB   B VAL   B 1 3   ? 47.204 -12.645 -16.675 0.28 23.65 ?  3   VAL   B HB   1 
ATOM   3622 H  HG11 A VAL   B 1 3   ? 48.607 -10.920 -17.151 0.72 26.10 ?  3   VAL   B HG11 1 
ATOM   3623 H  HG11 B VAL   B 1 3   ? 48.580 -10.789 -16.911 0.28 23.79 ?  3   VAL   B HG11 1 
ATOM   3624 H  HG12 A VAL   B 1 3   ? 49.500 -12.233 -17.203 0.72 26.10 ?  3   VAL   B HG12 1 
ATOM   3625 H  HG12 B VAL   B 1 3   ? 49.439 -12.121 -17.027 0.28 23.79 ?  3   VAL   B HG12 1 
ATOM   3626 H  HG13 A VAL   B 1 3   ? 49.111 -11.484 -18.548 0.72 26.10 ?  3   VAL   B HG13 1 
ATOM   3627 H  HG13 B VAL   B 1 3   ? 49.047 -11.312 -18.337 0.28 23.79 ?  3   VAL   B HG13 1 
ATOM   3628 H  HG21 A VAL   B 1 3   ? 46.350 -10.924 -17.997 0.72 26.72 ?  3   VAL   B HG21 1 
ATOM   3629 H  HG21 B VAL   B 1 3   ? 46.324 -10.703 -17.739 0.28 23.71 ?  3   VAL   B HG21 1 
ATOM   3630 H  HG22 A VAL   B 1 3   ? 46.604 -11.690 -19.364 0.72 26.72 ?  3   VAL   B HG22 1 
ATOM   3631 H  HG22 B VAL   B 1 3   ? 46.533 -11.445 -19.127 0.28 23.71 ?  3   VAL   B HG22 1 
ATOM   3632 H  HG23 A VAL   B 1 3   ? 45.585 -12.282 -18.300 0.72 26.72 ?  3   VAL   B HG23 1 
ATOM   3633 H  HG23 B VAL   B 1 3   ? 45.515 -12.032 -18.058 0.28 23.71 ?  3   VAL   B HG23 1 
ATOM   3634 N  N    . ASN   B 1 4   ? 46.355 -15.438 -17.471 1.00 16.53 ?  4   ASN   B N    1 
ATOM   3635 C  CA   . ASN   B 1 4   ? 45.223 -16.360 -17.372 1.00 15.70 ?  4   ASN   B CA   1 
ATOM   3636 C  C    . ASN   B 1 4   ? 45.175 -17.320 -18.561 1.00 16.12 ?  4   ASN   B C    1 
ATOM   3637 O  O    . ASN   B 1 4   ? 44.116 -17.581 -19.127 1.00 16.97 ?  4   ASN   B O    1 
ATOM   3638 C  CB   . ASN   B 1 4   ? 43.895 -15.616 -17.206 1.00 15.09 ?  4   ASN   B CB   1 
ATOM   3639 C  CG   . ASN   B 1 4   ? 43.843 -14.804 -15.930 1.00 14.37 ?  4   ASN   B CG   1 
ATOM   3640 O  OD1  . ASN   B 1 4   ? 44.135 -15.315 -14.854 1.00 13.72 ?  4   ASN   B OD1  1 
ATOM   3641 N  ND2  . ASN   B 1 4   ? 43.493 -13.528 -16.047 1.00 15.22 ?  4   ASN   B ND2  1 
ATOM   3642 H  H    A ASN   B 1 4   ? 46.825 -15.378 -16.756 0.72 19.83 ?  4   ASN   B H    1 
ATOM   3643 H  H    B ASN   B 1 4   ? 46.933 -15.535 -16.844 0.28 19.83 ?  4   ASN   B H    1 
ATOM   3644 H  HA   . ASN   B 1 4   ? 45.350 -16.899 -16.575 1.00 18.84 ?  4   ASN   B HA   1 
ATOM   3645 H  HB2  . ASN   B 1 4   ? 43.768 -15.014 -17.953 1.00 18.11 ?  4   ASN   B HB2  1 
ATOM   3646 H  HB3  . ASN   B 1 4   ? 43.172 -16.267 -17.179 1.00 18.11 ?  4   ASN   B HB3  1 
ATOM   3647 H  HD21 . ASN   B 1 4   ? 43.455 -13.028 -15.347 1.00 18.27 ?  4   ASN   B HD21 1 
ATOM   3648 H  HD22 . ASN   B 1 4   ? 43.300 -13.202 -16.818 1.00 18.27 ?  4   ASN   B HD22 1 
ATOM   3649 N  N    . SER   B 1 5   ? 46.336 -17.845 -18.947 1.00 17.27 ?  5   SER   B N    1 
ATOM   3650 C  CA   . SER   B 1 5   ? 46.427 -18.761 -20.085 1.00 19.43 ?  5   SER   B CA   1 
ATOM   3651 C  C    . SER   B 1 5   ? 46.417 -20.198 -19.573 1.00 20.81 ?  5   SER   B C    1 
ATOM   3652 O  O    . SER   B 1 5   ? 47.423 -20.903 -19.571 1.00 22.93 ?  5   SER   B O    1 
ATOM   3653 C  CB   . SER   B 1 5   ? 47.675 -18.466 -20.910 1.00 21.13 ?  5   SER   B CB   1 
ATOM   3654 O  OG   . SER   B 1 5   ? 48.855 -18.680 -20.152 1.00 23.64 ?  5   SER   B OG   1 
ATOM   3655 H  H    . SER   B 1 5   ? 47.094 -17.683 -18.569 1.00 20.72 ?  5   SER   B H    1 
ATOM   3656 H  HA   . SER   B 1 5   ? 45.654 -18.639 -20.655 1.00 23.32 ?  5   SER   B HA   1 
ATOM   3657 H  HB2  . SER   B 1 5   ? 47.684 -19.047 -21.689 1.00 25.35 ?  5   SER   B HB2  1 
ATOM   3658 H  HB3  . SER   B 1 5   ? 47.635 -17.540 -21.193 1.00 25.35 ?  5   SER   B HB3  1 
ATOM   3659 H  HG   . SER   B 1 5   ? 48.909 -19.489 -19.932 1.00 28.37 ?  5   SER   B HG   1 
ATOM   3660 N  N    . PHE   B 1 6   ? 45.240 -20.616 -19.121 1.00 20.74 ?  6   PHE   B N    1 
ATOM   3661 C  CA   . PHE   B 1 6   ? 45.056 -21.965 -18.611 1.00 20.16 ?  6   PHE   B CA   1 
ATOM   3662 C  C    . PHE   B 1 6   ? 44.984 -22.947 -19.770 1.00 23.06 ?  6   PHE   B C    1 
ATOM   3663 O  O    . PHE   B 1 6   ? 44.326 -22.683 -20.780 1.00 25.36 ?  6   PHE   B O    1 
ATOM   3664 C  CB   . PHE   B 1 6   ? 43.769 -22.041 -17.789 1.00 18.60 ?  6   PHE   B CB   1 
ATOM   3665 C  CG   . PHE   B 1 6   ? 43.778 -21.169 -16.563 1.00 16.44 ?  6   PHE   B CG   1 
ATOM   3666 C  CD1  . PHE   B 1 6   ? 44.278 -21.647 -15.370 1.00 15.37 ?  6   PHE   B CD1  1 
ATOM   3667 C  CD2  . PHE   B 1 6   ? 43.289 -19.871 -16.607 1.00 15.87 ?  6   PHE   B CD2  1 
ATOM   3668 C  CE1  . PHE   B 1 6   ? 44.278 -20.856 -14.233 1.00 14.99 ?  6   PHE   B CE1  1 
ATOM   3669 C  CE2  . PHE   B 1 6   ? 43.293 -19.069 -15.477 1.00 16.38 ?  6   PHE   B CE2  1 
ATOM   3670 C  CZ   . PHE   B 1 6   ? 43.796 -19.555 -14.292 1.00 15.30 ?  6   PHE   B CZ   1 
ATOM   3671 H  H    . PHE   B 1 6   ? 44.527 -20.137 -19.107 1.00 24.89 ?  6   PHE   B H    1 
ATOM   3672 H  HA   . PHE   B 1 6   ? 45.802 -22.210 -18.044 1.00 24.19 ?  6   PHE   B HA   1 
ATOM   3673 H  HB2  . PHE   B 1 6   ? 43.025 -21.763 -18.346 1.00 22.33 ?  6   PHE   B HB2  1 
ATOM   3674 H  HB3  . PHE   B 1 6   ? 43.635 -22.958 -17.499 1.00 22.33 ?  6   PHE   B HB3  1 
ATOM   3675 H  HD1  . PHE   B 1 6   ? 44.611 -22.515 -15.322 1.00 18.44 ?  6   PHE   B HD1  1 
ATOM   3676 H  HD2  . PHE   B 1 6   ? 42.947 -19.538 -17.406 1.00 19.04 ?  6   PHE   B HD2  1 
ATOM   3677 H  HE1  . PHE   B 1 6   ? 44.627 -21.185 -13.434 1.00 17.99 ?  6   PHE   B HE1  1 
ATOM   3678 H  HE2  . PHE   B 1 6   ? 42.961 -18.198 -15.519 1.00 19.66 ?  6   PHE   B HE2  1 
ATOM   3679 H  HZ   . PHE   B 1 6   ? 43.802 -19.023 -13.529 1.00 18.36 ?  6   PHE   B HZ   1 
ATOM   3680 N  N    . SER   B 1 7   ? 45.674 -24.079 -19.624 1.00 23.81 ?  7   SER   B N    1 
ATOM   3681 C  CA   . SER   B 1 7   ? 45.766 -25.069 -20.688 1.00 26.22 ?  7   SER   B CA   1 
ATOM   3682 C  C    . SER   B 1 7   ? 45.721 -26.472 -20.101 1.00 25.92 ?  7   SER   B C    1 
ATOM   3683 O  O    . SER   B 1 7   ? 46.305 -26.736 -19.046 1.00 26.70 ?  7   SER   B O    1 
ATOM   3684 C  CB   . SER   B 1 7   ? 47.062 -24.888 -21.492 1.00 28.44 ?  7   SER   B CB   1 
ATOM   3685 O  OG   . SER   B 1 7   ? 47.090 -25.752 -22.612 1.00 30.36 ?  7   SER   B OG   1 
ATOM   3686 H  H    . SER   B 1 7   ? 46.103 -24.297 -18.907 1.00 28.57 ?  7   SER   B H    1 
ATOM   3687 H  HA   . SER   B 1 7   ? 45.015 -24.970 -21.288 1.00 31.46 ?  7   SER   B HA   1 
ATOM   3688 H  HB2  . SER   B 1 7   ? 47.113 -23.969 -21.800 1.00 34.14 ?  7   SER   B HB2  1 
ATOM   3689 H  HB3  . SER   B 1 7   ? 47.820 -25.087 -20.920 1.00 34.14 ?  7   SER   B HB3  1 
ATOM   3690 H  HG   . SER   B 1 7   ? 47.802 -25.641 -23.044 1.00 36.43 ?  7   SER   B HG   1 
ATOM   3691 N  N    . GLY   B 1 8   ? 45.023 -27.370 -20.794 1.00 25.56 ?  8   GLY   B N    1 
ATOM   3692 C  CA   . GLY   B 1 8   ? 44.993 -28.762 -20.405 1.00 24.91 ?  8   GLY   B CA   1 
ATOM   3693 C  C    . GLY   B 1 8   ? 44.038 -29.090 -19.286 1.00 23.34 ?  8   GLY   B C    1 
ATOM   3694 O  O    . GLY   B 1 8   ? 44.170 -30.155 -18.669 1.00 24.50 ?  8   GLY   B O    1 
ATOM   3695 H  H    . GLY   B 1 8   ? 44.558 -27.188 -21.493 1.00 30.68 ?  8   GLY   B H    1 
ATOM   3696 H  HA2  . GLY   B 1 8   ? 44.745 -29.298 -21.175 1.00 29.90 ?  8   GLY   B HA2  1 
ATOM   3697 H  HA3  . GLY   B 1 8   ? 45.879 -29.032 -20.123 1.00 29.90 ?  8   GLY   B HA3  1 
ATOM   3698 N  N    . TYR   B 1 9   ? 43.068 -28.223 -19.009 1.00 21.62 ?  9   TYR   B N    1 
ATOM   3699 C  CA   . TYR   B 1 9   ? 42.099 -28.491 -17.960 1.00 19.41 ?  9   TYR   B CA   1 
ATOM   3700 C  C    . TYR   B 1 9   ? 40.919 -29.282 -18.492 1.00 18.68 ?  9   TYR   B C    1 
ATOM   3701 O  O    . TYR   B 1 9   ? 40.505 -29.138 -19.646 1.00 20.74 ?  9   TYR   B O    1 
ATOM   3702 C  CB   . TYR   B 1 9   ? 41.580 -27.201 -17.329 1.00 18.82 ?  9   TYR   B CB   1 
ATOM   3703 C  CG   . TYR   B 1 9   ? 42.596 -26.574 -16.411 1.00 18.13 ?  9   TYR   B CG   1 
ATOM   3704 C  CD1  . TYR   B 1 9   ? 43.700 -25.913 -16.927 1.00 18.45 ?  9   TYR   B CD1  1 
ATOM   3705 C  CD2  . TYR   B 1 9   ? 42.473 -26.669 -15.034 1.00 17.08 ?  9   TYR   B CD2  1 
ATOM   3706 C  CE1  . TYR   B 1 9   ? 44.648 -25.355 -16.098 1.00 18.64 ?  9   TYR   B CE1  1 
ATOM   3707 C  CE2  . TYR   B 1 9   ? 43.417 -26.110 -14.194 1.00 17.65 ?  9   TYR   B CE2  1 
ATOM   3708 C  CZ   . TYR   B 1 9   ? 44.505 -25.455 -14.735 1.00 18.50 ?  9   TYR   B CZ   1 
ATOM   3709 O  OH   . TYR   B 1 9   ? 45.454 -24.906 -13.910 1.00 19.12 ?  9   TYR   B OH   1 
ATOM   3710 H  H    . TYR   B 1 9   ? 42.938 -27.483 -19.423 1.00 25.95 ?  9   TYR   B H    1 
ATOM   3711 H  HA   . TYR   B 1 9   ? 42.517 -29.016 -17.261 1.00 23.29 ?  9   TYR   B HA   1 
ATOM   3712 H  HB2  . TYR   B 1 9   ? 41.360 -26.562 -18.026 1.00 22.58 ?  9   TYR   B HB2  1 
ATOM   3713 H  HB3  . TYR   B 1 9   ? 40.794 -27.411 -16.806 1.00 22.58 ?  9   TYR   B HB3  1 
ATOM   3714 H  HD1  . TYR   B 1 9   ? 43.799 -25.850 -17.850 1.00 22.14 ?  9   TYR   B HD1  1 
ATOM   3715 H  HD2  . TYR   B 1 9   ? 41.737 -27.116 -14.669 1.00 20.50 ?  9   TYR   B HD2  1 
ATOM   3716 H  HE1  . TYR   B 1 9   ? 45.377 -24.918 -16.461 1.00 22.37 ?  9   TYR   B HE1  1 
ATOM   3717 H  HE2  . TYR   B 1 9   ? 43.315 -26.184 -13.271 1.00 21.19 ?  9   TYR   B HE2  1 
ATOM   3718 H  HH   . TYR   B 1 9   ? 46.050 -24.542 -14.369 1.00 22.95 ?  9   TYR   B HH   1 
ATOM   3719 N  N    . LEU   B 1 10  ? 40.385 -30.129 -17.623 1.00 17.06 ?  10  LEU   B N    1 
ATOM   3720 C  CA   . LEU   B 1 10  ? 39.183 -30.892 -17.900 1.00 16.92 ?  10  LEU   B CA   1 
ATOM   3721 C  C    . LEU   B 1 10  ? 37.992 -30.128 -17.342 1.00 16.18 ?  10  LEU   B C    1 
ATOM   3722 O  O    . LEU   B 1 10  ? 38.005 -29.705 -16.183 1.00 15.77 ?  10  LEU   B O    1 
ATOM   3723 C  CB   . LEU   B 1 10  ? 39.290 -32.258 -17.225 1.00 17.69 ?  10  LEU   B CB   1 
ATOM   3724 C  CG   . LEU   B 1 10  ? 38.154 -33.214 -17.557 1.00 19.29 ?  10  LEU   B CG   1 
ATOM   3725 C  CD1  . LEU   B 1 10  ? 38.291 -33.716 -18.988 1.00 20.28 ?  10  LEU   B CD1  1 
ATOM   3726 C  CD2  . LEU   B 1 10  ? 38.110 -34.362 -16.568 1.00 20.55 ?  10  LEU   B CD2  1 
ATOM   3727 H  H    . LEU   B 1 10  ? 40.708 -30.281 -16.838 1.00 20.48 ?  10  LEU   B H    1 
ATOM   3728 H  HA   . LEU   B 1 10  ? 39.068 -31.015 -18.853 1.00 20.31 ?  10  LEU   B HA   1 
ATOM   3729 H  HB2  . LEU   B 1 10  ? 40.119 -32.681 -17.501 1.00 21.23 ?  10  LEU   B HB2  1 
ATOM   3730 H  HB3  . LEU   B 1 10  ? 39.295 -32.133 -16.261 1.00 21.23 ?  10  LEU   B HB3  1 
ATOM   3731 H  HG   . LEU   B 1 10  ? 37.310 -32.737 -17.491 1.00 23.15 ?  10  LEU   B HG   1 
ATOM   3732 H  HD11 . LEU   B 1 10  ? 37.603 -34.379 -19.155 1.00 24.34 ?  10  LEU   B HD11 1 
ATOM   3733 H  HD12 . LEU   B 1 10  ? 38.184 -32.968 -19.596 1.00 24.34 ?  10  LEU   B HD12 1 
ATOM   3734 H  HD13 . LEU   B 1 10  ? 39.168 -34.112 -19.099 1.00 24.34 ?  10  LEU   B HD13 1 
ATOM   3735 H  HD21 . LEU   B 1 10  ? 37.381 -34.953 -16.808 1.00 24.66 ?  10  LEU   B HD21 1 
ATOM   3736 H  HD22 . LEU   B 1 10  ? 38.952 -34.836 -16.602 1.00 24.66 ?  10  LEU   B HD22 1 
ATOM   3737 H  HD23 . LEU   B 1 10  ? 37.964 -34.001 -15.679 1.00 24.66 ?  10  LEU   B HD23 1 
ATOM   3738 N  N    . LYS   B 1 11  ? 36.967 -29.952 -18.165 1.00 17.22 ?  11  LYS   B N    1 
ATOM   3739 C  CA   . LYS   B 1 11  ? 35.771 -29.237 -17.749 1.00 19.22 ?  11  LYS   B CA   1 
ATOM   3740 C  C    . LYS   B 1 11  ? 34.895 -30.163 -16.912 1.00 18.43 ?  11  LYS   B C    1 
ATOM   3741 O  O    . LYS   B 1 11  ? 34.527 -31.253 -17.362 1.00 19.99 ?  11  LYS   B O    1 
ATOM   3742 C  CB   . LYS   B 1 11  ? 35.021 -28.756 -18.989 1.00 22.52 ?  11  LYS   B CB   1 
ATOM   3743 C  CG   . LYS   B 1 11  ? 33.860 -27.819 -18.717 1.00 25.91 ?  11  LYS   B CG   1 
ATOM   3744 C  CD   . LYS   B 1 11  ? 33.097 -27.531 -20.003 1.00 28.75 ?  11  LYS   B CD   1 
ATOM   3745 C  CE   . LYS   B 1 11  ? 32.072 -26.431 -19.812 1.00 30.75 ?  11  LYS   B CE   1 
ATOM   3746 N  NZ   . LYS   B 1 11  ? 32.725 -25.113 -19.600 1.00 32.01 ?  11  LYS   B NZ   1 
ATOM   3747 H  H    . LYS   B 1 11  ? 36.938 -30.245 -18.972 1.00 20.67 ?  11  LYS   B H    1 
ATOM   3748 H  HA   . LYS   B 1 11  ? 36.015 -28.468 -17.212 1.00 23.07 ?  11  LYS   B HA   1 
ATOM   3749 H  HB2  . LYS   B 1 11  ? 35.647 -28.284 -19.563 1.00 27.03 ?  11  LYS   B HB2  1 
ATOM   3750 H  HB3  . LYS   B 1 11  ? 34.670 -29.527 -19.458 1.00 27.03 ?  11  LYS   B HB3  1 
ATOM   3751 H  HG2  . LYS   B 1 11  ? 33.250 -28.231 -18.086 1.00 31.10 ?  11  LYS   B HG2  1 
ATOM   3752 H  HG3  . LYS   B 1 11  ? 34.195 -26.979 -18.366 1.00 31.10 ?  11  LYS   B HG3  1 
ATOM   3753 H  HD2  . LYS   B 1 11  ? 33.722 -27.249 -20.690 1.00 34.50 ?  11  LYS   B HD2  1 
ATOM   3754 H  HD3  . LYS   B 1 11  ? 32.632 -28.335 -20.285 1.00 34.50 ?  11  LYS   B HD3  1 
ATOM   3755 H  HE2  . LYS   B 1 11  ? 31.515 -26.372 -20.604 1.00 36.90 ?  11  LYS   B HE2  1 
ATOM   3756 H  HE3  . LYS   B 1 11  ? 31.530 -26.635 -19.034 1.00 36.90 ?  11  LYS   B HE3  1 
ATOM   3757 H  HZ1  . LYS   B 1 11  ? 32.107 -24.477 -19.524 1.00 38.42 ?  11  LYS   B HZ1  1 
ATOM   3758 H  HZ2  . LYS   B 1 11  ? 33.214 -25.131 -18.857 1.00 38.42 ?  11  LYS   B HZ2  1 
ATOM   3759 H  HZ3  . LYS   B 1 11  ? 33.254 -24.921 -20.290 1.00 38.42 ?  11  LYS   B HZ3  1 
ATOM   3760 N  N    . LEU   B 1 12  ? 34.560 -29.733 -15.697 1.00 16.69 ?  12  LEU   B N    1 
ATOM   3761 C  CA   . LEU   B 1 12  ? 33.608 -30.442 -14.848 1.00 16.39 ?  12  LEU   B CA   1 
ATOM   3762 C  C    . LEU   B 1 12  ? 32.213 -29.841 -14.930 1.00 16.60 ?  12  LEU   B C    1 
ATOM   3763 O  O    . LEU   B 1 12  ? 31.231 -30.564 -15.104 1.00 17.23 ?  12  LEU   B O    1 
ATOM   3764 C  CB   . LEU   B 1 12  ? 34.078 -30.452 -13.392 1.00 15.80 ?  12  LEU   B CB   1 
ATOM   3765 C  CG   . LEU   B 1 12  ? 35.405 -31.150 -13.104 1.00 16.26 ?  12  LEU   B CG   1 
ATOM   3766 C  CD1  . LEU   B 1 12  ? 35.714 -31.098 -11.618 1.00 16.62 ?  12  LEU   B CD1  1 
ATOM   3767 C  CD2  . LEU   B 1 12  ? 35.411 -32.585 -13.611 1.00 17.24 ?  12  LEU   B CD2  1 
ATOM   3768 H  H    . LEU   B 1 12  ? 34.877 -29.020 -15.339 1.00 20.03 ?  12  LEU   B H    1 
ATOM   3769 H  HA   . LEU   B 1 12  ? 33.544 -31.360 -15.151 1.00 19.67 ?  12  LEU   B HA   1 
ATOM   3770 H  HB2  . LEU   B 1 12  ? 34.166 -29.533 -13.098 1.00 18.96 ?  12  LEU   B HB2  1 
ATOM   3771 H  HB3  . LEU   B 1 12  ? 33.399 -30.895 -12.861 1.00 18.96 ?  12  LEU   B HB3  1 
ATOM   3772 H  HG   . LEU   B 1 12  ? 36.112 -30.672 -13.564 1.00 19.52 ?  12  LEU   B HG   1 
ATOM   3773 H  HD11 . LEU   B 1 12  ? 36.562 -31.545 -11.456 1.00 19.95 ?  12  LEU   B HD11 1 
ATOM   3774 H  HD12 . LEU   B 1 12  ? 35.772 -30.172 -11.337 1.00 19.95 ?  12  LEU   B HD12 1 
ATOM   3775 H  HD13 . LEU   B 1 12  ? 35.007 -31.549 -11.130 1.00 19.95 ?  12  LEU   B HD13 1 
ATOM   3776 H  HD21 . LEU   B 1 12  ? 36.215 -33.027 -13.299 1.00 20.69 ?  12  LEU   B HD21 1 
ATOM   3777 H  HD22 . LEU   B 1 12  ? 34.626 -33.042 -13.274 1.00 20.69 ?  12  LEU   B HD22 1 
ATOM   3778 H  HD23 . LEU   B 1 12  ? 35.396 -32.575 -14.583 1.00 20.69 ?  12  LEU   B HD23 1 
ATOM   3779 N  N    . THR   B 1 13  ? 32.115 -28.525 -14.800 1.00 16.75 ?  13  THR   B N    1 
ATOM   3780 C  CA   . THR   B 1 13  ? 30.886 -27.777 -15.001 1.00 16.60 ?  13  THR   B CA   1 
ATOM   3781 C  C    . THR   B 1 13  ? 31.216 -26.573 -15.876 1.00 18.44 ?  13  THR   B C    1 
ATOM   3782 O  O    . THR   B 1 13  ? 32.361 -26.377 -16.298 1.00 19.49 ?  13  THR   B O    1 
ATOM   3783 C  CB   . THR   B 1 13  ? 30.292 -27.310 -13.670 1.00 16.50 ?  13  THR   B CB   1 
ATOM   3784 O  OG1  . THR   B 1 13  ? 31.145 -26.299 -13.120 1.00 16.05 ?  13  THR   B OG1  1 
ATOM   3785 C  CG2  . THR   B 1 13  ? 30.179 -28.469 -12.687 1.00 17.22 ?  13  THR   B CG2  1 
ATOM   3786 H  H    . THR   B 1 13  ? 32.780 -28.020 -14.585 1.00 20.11 ?  13  THR   B H    1 
ATOM   3787 H  HA   . THR   B 1 13  ? 30.233 -28.332 -15.453 1.00 19.92 ?  13  THR   B HA   1 
ATOM   3788 H  HB   . THR   B 1 13  ? 29.402 -26.943 -13.815 1.00 19.80 ?  13  THR   B HB   1 
ATOM   3789 H  HG1  . THR   B 1 13  ? 30.848 -25.536 -13.304 1.00 19.27 ?  13  THR   B HG1  1 
ATOM   3790 H  HG21 . THR   B 1 13  ? 29.664 -28.201 -11.910 1.00 20.67 ?  13  THR   B HG21 1 
ATOM   3791 H  HG22 . THR   B 1 13  ? 29.734 -29.221 -13.113 1.00 20.67 ?  13  THR   B HG22 1 
ATOM   3792 H  HG23 . THR   B 1 13  ? 31.062 -28.750 -12.401 1.00 20.67 ?  13  THR   B HG23 1 
ATOM   3793 N  N    A ASP   B 1 14  ? 30.201 -25.751 -16.142 0.72 19.37 ?  14  ASP   B N    1 
ATOM   3794 N  N    B ASP   B 1 14  ? 30.203 -25.743 -16.135 0.28 19.22 ?  14  ASP   B N    1 
ATOM   3795 C  CA   A ASP   B 1 14  ? 30.412 -24.587 -16.994 0.72 21.07 ?  14  ASP   B CA   1 
ATOM   3796 C  CA   B ASP   B 1 14  ? 30.401 -24.581 -16.996 0.28 20.15 ?  14  ASP   B CA   1 
ATOM   3797 C  C    A ASP   B 1 14  ? 31.505 -23.674 -16.454 0.72 19.23 ?  14  ASP   B C    1 
ATOM   3798 C  C    B ASP   B 1 14  ? 31.410 -23.591 -16.431 0.28 18.61 ?  14  ASP   B C    1 
ATOM   3799 O  O    A ASP   B 1 14  ? 32.157 -22.967 -17.234 0.72 20.54 ?  14  ASP   B O    1 
ATOM   3800 O  O    B ASP   B 1 14  ? 31.882 -22.723 -17.174 0.28 19.03 ?  14  ASP   B O    1 
ATOM   3801 C  CB   A ASP   B 1 14  ? 29.104 -23.815 -17.164 0.72 24.67 ?  14  ASP   B CB   1 
ATOM   3802 C  CB   B ASP   B 1 14  ? 29.075 -23.860 -17.238 0.28 22.49 ?  14  ASP   B CB   1 
ATOM   3803 C  CG   A ASP   B 1 14  ? 28.145 -24.495 -18.115 0.72 28.12 ?  14  ASP   B CG   1 
ATOM   3804 C  CG   B ASP   B 1 14  ? 28.187 -24.589 -18.228 0.28 24.51 ?  14  ASP   B CG   1 
ATOM   3805 O  OD1  A ASP   B 1 14  ? 28.539 -25.483 -18.773 0.72 29.34 ?  14  ASP   B OD1  1 
ATOM   3806 O  OD1  B ASP   B 1 14  ? 28.730 -25.239 -19.146 0.28 25.15 ?  14  ASP   B OD1  1 
ATOM   3807 O  OD2  A ASP   B 1 14  ? 26.988 -24.037 -18.199 0.72 29.53 -1 14  ASP   B OD2  1 
ATOM   3808 O  OD2  B ASP   B 1 14  ? 26.949 -24.518 -18.088 0.28 25.35 -1 14  ASP   B OD2  1 
ATOM   3809 H  H    A ASP   B 1 14  ? 29.401 -25.838 -15.839 0.72 23.25 ?  14  ASP   B H    1 
ATOM   3810 H  H    B ASP   B 1 14  ? 29.405 -25.829 -15.827 0.28 23.07 ?  14  ASP   B H    1 
ATOM   3811 H  HA   A ASP   B 1 14  ? 30.694 -24.884 -17.869 0.72 25.29 ?  14  ASP   B HA   1 
ATOM   3812 H  HA   B ASP   B 1 14  ? 30.732 -24.885 -17.854 0.28 24.18 ?  14  ASP   B HA   1 
ATOM   3813 H  HB2  A ASP   B 1 14  ? 28.653 -23.747 -16.310 0.72 29.61 ?  14  ASP   B HB2  1 
ATOM   3814 H  HB2  B ASP   B 1 14  ? 28.595 -23.792 -16.398 0.28 26.99 ?  14  ASP   B HB2  1 
ATOM   3815 H  HB3  A ASP   B 1 14  ? 29.292 -22.932 -17.516 0.72 29.61 ?  14  ASP   B HB3  1 
ATOM   3816 H  HB3  B ASP   B 1 14  ? 29.262 -22.969 -17.584 0.28 26.99 ?  14  ASP   B HB3  1 
ATOM   3817 N  N    . ASN   B 1 15  ? 31.733 -23.678 -15.138 1.00 17.00 ?  15  ASN   B N    1 
ATOM   3818 C  CA   . ASN   B 1 15  ? 32.695 -22.759 -14.531 1.00 14.93 ?  15  ASN   B CA   1 
ATOM   3819 C  C    . ASN   B 1 15  ? 33.786 -23.414 -13.693 1.00 13.73 ?  15  ASN   B C    1 
ATOM   3820 O  O    . ASN   B 1 15  ? 34.627 -22.684 -13.155 1.00 14.32 ?  15  ASN   B O    1 
ATOM   3821 C  CB   . ASN   B 1 15  ? 31.981 -21.707 -13.667 1.00 14.91 ?  15  ASN   B CB   1 
ATOM   3822 C  CG   . ASN   B 1 15  ? 31.360 -22.308 -12.431 1.00 14.62 ?  15  ASN   B CG   1 
ATOM   3823 O  OD1  . ASN   B 1 15  ? 30.427 -23.111 -12.523 1.00 16.48 ?  15  ASN   B OD1  1 
ATOM   3824 N  ND2  . ASN   B 1 15  ? 31.875 -21.947 -11.268 1.00 13.98 ?  15  ASN   B ND2  1 
ATOM   3825 H  H    A ASN   B 1 15  ? 31.346 -24.206 -14.577 0.72 20.40 ?  15  ASN   B H    1 
ATOM   3826 H  H    B ASN   B 1 15  ? 31.386 -24.241 -14.586 0.28 20.40 ?  15  ASN   B H    1 
ATOM   3827 H  HA   . ASN   B 1 15  ? 33.145 -22.279 -15.236 1.00 17.92 ?  15  ASN   B HA   1 
ATOM   3828 H  HB2  . ASN   B 1 15  ? 32.631 -21.033 -13.389 1.00 17.89 ?  15  ASN   B HB2  1 
ATOM   3829 H  HB3  . ASN   B 1 15  ? 31.279 -21.286 -14.187 1.00 17.89 ?  15  ASN   B HB3  1 
ATOM   3830 H  HD21 . ASN   B 1 15  ? 31.554 -22.264 -10.535 1.00 16.78 ?  15  ASN   B HD21 1 
ATOM   3831 H  HD22 . ASN   B 1 15  ? 32.532 -21.386 -11.235 1.00 16.78 ?  15  ASN   B HD22 1 
ATOM   3832 N  N    . VAL   B 1 16  ? 33.803 -24.738 -13.554 1.00 13.55 ?  16  VAL   B N    1 
ATOM   3833 C  CA   . VAL   B 1 16  ? 34.803 -25.430 -12.745 1.00 13.40 ?  16  VAL   B CA   1 
ATOM   3834 C  C    . VAL   B 1 16  ? 35.594 -26.361 -13.649 1.00 13.50 ?  16  VAL   B C    1 
ATOM   3835 O  O    . VAL   B 1 16  ? 35.015 -27.230 -14.320 1.00 14.37 ?  16  VAL   B O    1 
ATOM   3836 C  CB   . VAL   B 1 16  ? 34.178 -26.196 -11.569 1.00 13.61 ?  16  VAL   B CB   1 
ATOM   3837 C  CG1  . VAL   B 1 16  ? 35.264 -26.912 -10.771 1.00 14.07 ?  16  VAL   B CG1  1 
ATOM   3838 C  CG2  . VAL   B 1 16  ? 33.382 -25.250 -10.676 1.00 14.31 ?  16  VAL   B CG2  1 
ATOM   3839 H  H    . VAL   B 1 16  ? 33.230 -25.270 -13.921 1.00 16.26 ?  16  VAL   B H    1 
ATOM   3840 H  HA   . VAL   B 1 16  ? 35.416 -24.777 -12.375 1.00 16.08 ?  16  VAL   B HA   1 
ATOM   3841 H  HB   . VAL   B 1 16  ? 33.569 -26.871 -11.913 1.00 16.34 ?  16  VAL   B HB   1 
ATOM   3842 H  HG11 . VAL   B 1 16  ? 34.888 -27.214 -9.929  1.00 16.89 ?  16  VAL   B HG11 1 
ATOM   3843 H  HG12 . VAL   B 1 16  ? 35.590 -27.667 -11.279 1.00 16.89 ?  16  VAL   B HG12 1 
ATOM   3844 H  HG13 . VAL   B 1 16  ? 35.988 -26.286 -10.599 1.00 16.89 ?  16  VAL   B HG13 1 
ATOM   3845 H  HG21 . VAL   B 1 16  ? 33.044 -25.748 -9.913  1.00 17.17 ?  16  VAL   B HG21 1 
ATOM   3846 H  HG22 . VAL   B 1 16  ? 33.963 -24.537 -10.376 1.00 17.17 ?  16  VAL   B HG22 1 
ATOM   3847 H  HG23 . VAL   B 1 16  ? 32.641 -24.887 -11.185 1.00 17.17 ?  16  VAL   B HG23 1 
ATOM   3848 N  N    . TYR   B 1 17  ? 36.916 -26.193 -13.634 1.00 13.74 ?  17  TYR   B N    1 
ATOM   3849 C  CA   . TYR   B 1 17  ? 37.860 -26.941 -14.450 1.00 14.41 ?  17  TYR   B CA   1 
ATOM   3850 C  C    . TYR   B 1 17  ? 38.917 -27.544 -13.539 1.00 13.39 ?  17  TYR   B C    1 
ATOM   3851 O  O    . TYR   B 1 17  ? 39.192 -27.012 -12.459 1.00 13.99 ?  17  TYR   B O    1 
ATOM   3852 C  CB   . TYR   B 1 17  ? 38.567 -26.017 -15.442 1.00 16.43 ?  17  TYR   B CB   1 
ATOM   3853 C  CG   . TYR   B 1 17  ? 37.643 -25.246 -16.346 1.00 18.95 ?  17  TYR   B CG   1 
ATOM   3854 C  CD1  . TYR   B 1 17  ? 37.064 -24.052 -15.932 1.00 19.97 ?  17  TYR   B CD1  1 
ATOM   3855 C  CD2  . TYR   B 1 17  ? 37.351 -25.709 -17.620 1.00 21.10 ?  17  TYR   B CD2  1 
ATOM   3856 C  CE1  . TYR   B 1 17  ? 36.214 -23.344 -16.762 1.00 21.55 ?  17  TYR   B CE1  1 
ATOM   3857 C  CE2  . TYR   B 1 17  ? 36.508 -25.009 -18.458 1.00 22.49 ?  17  TYR   B CE2  1 
ATOM   3858 C  CZ   . TYR   B 1 17  ? 35.940 -23.831 -18.023 1.00 22.70 ?  17  TYR   B CZ   1 
ATOM   3859 O  OH   . TYR   B 1 17  ? 35.102 -23.132 -18.858 1.00 24.22 ?  17  TYR   B OH   1 
ATOM   3860 H  H    . TYR   B 1 17  ? 37.313 -25.610 -13.131 1.00 16.48 ?  17  TYR   B H    1 
ATOM   3861 H  HA   . TYR   B 1 17  ? 37.403 -27.650 -14.931 1.00 17.29 ?  17  TYR   B HA   1 
ATOM   3862 H  HB2  . TYR   B 1 17  ? 39.104 -25.379 -14.950 1.00 19.72 ?  17  TYR   B HB2  1 
ATOM   3863 H  HB3  . TYR   B 1 17  ? 39.132 -26.556 -16.009 1.00 19.72 ?  17  TYR   B HB3  1 
ATOM   3864 H  HD1  . TYR   B 1 17  ? 37.248 -23.726 -15.083 1.00 23.97 ?  17  TYR   B HD1  1 
ATOM   3865 H  HD2  . TYR   B 1 17  ? 37.724 -26.506 -17.916 1.00 25.32 ?  17  TYR   B HD2  1 
ATOM   3866 H  HE1  . TYR   B 1 17  ? 35.832 -22.542 -16.474 1.00 25.86 ?  17  TYR   B HE1  1 
ATOM   3867 H  HE2  . TYR   B 1 17  ? 36.312 -25.332 -19.311 1.00 26.99 ?  17  TYR   B HE2  1 
ATOM   3868 H  HH   . TYR   B 1 17  ? 35.014 -23.530 -19.592 1.00 29.06 ?  17  TYR   B HH   1 
ATOM   3869 N  N    . ILE   B 1 18  ? 39.533 -28.643 -13.978 1.00 13.10 ?  18  ILE   B N    1 
ATOM   3870 C  CA   . ILE   B 1 18  ? 40.463 -29.366 -13.117 1.00 13.30 ?  18  ILE   B CA   1 
ATOM   3871 C  C    . ILE   B 1 18  ? 41.626 -29.912 -13.936 1.00 13.57 ?  18  ILE   B C    1 
ATOM   3872 O  O    . ILE   B 1 18  ? 41.468 -30.309 -15.095 1.00 14.65 ?  18  ILE   B O    1 
ATOM   3873 C  CB   . ILE   B 1 18  ? 39.715 -30.465 -12.321 1.00 13.76 ?  18  ILE   B CB   1 
ATOM   3874 C  CG1  . ILE   B 1 18  ? 40.567 -30.997 -11.170 1.00 14.11 ?  18  ILE   B CG1  1 
ATOM   3875 C  CG2  . ILE   B 1 18  ? 39.226 -31.587 -13.244 1.00 14.39 ?  18  ILE   B CG2  1 
ATOM   3876 C  CD1  . ILE   B 1 18  ? 39.755 -31.812 -10.171 1.00 15.84 ?  18  ILE   B CD1  1 
ATOM   3877 H  H    . ILE   B 1 18  ? 39.436 -28.984 -14.763 1.00 15.73 ?  18  ILE   B H    1 
ATOM   3878 H  HA   . ILE   B 1 18  ? 40.828 -28.749 -12.470 1.00 15.96 ?  18  ILE   B HA   1 
ATOM   3879 H  HB   . ILE   B 1 18  ? 38.926 -30.060 -11.927 1.00 16.51 ?  18  ILE   B HB   1 
ATOM   3880 H  HG12 . ILE   B 1 18  ? 41.263 -31.565 -11.525 1.00 16.94 ?  18  ILE   B HG12 1 
ATOM   3881 H  HG13 . ILE   B 1 18  ? 40.955 -30.246 -10.694 1.00 16.94 ?  18  ILE   B HG13 1 
ATOM   3882 H  HG21 . ILE   B 1 18  ? 38.630 -32.172 -12.745 1.00 17.27 ?  18  ILE   B HG21 1 
ATOM   3883 H  HG22 . ILE   B 1 18  ? 38.752 -31.194 -13.991 1.00 17.27 ?  18  ILE   B HG22 1 
ATOM   3884 H  HG23 . ILE   B 1 18  ? 39.990 -32.092 -13.562 1.00 17.27 ?  18  ILE   B HG23 1 
ATOM   3885 H  HD11 . ILE   B 1 18  ? 40.326 -32.074 -9.433  1.00 19.01 ?  18  ILE   B HD11 1 
ATOM   3886 H  HD12 . ILE   B 1 18  ? 39.017 -31.272 -9.842  1.00 19.01 ?  18  ILE   B HD12 1 
ATOM   3887 H  HD13 . ILE   B 1 18  ? 39.406 -32.604 -10.615 1.00 19.01 ?  18  ILE   B HD13 1 
ATOM   3888 N  N    . LYS   B 1 19  ? 42.805 -29.943 -13.315 1.00 13.93 ?  19  LYS   B N    1 
ATOM   3889 C  CA   . LYS   B 1 19  ? 44.015 -30.414 -13.973 1.00 14.78 ?  19  LYS   B CA   1 
ATOM   3890 C  C    . LYS   B 1 19  ? 44.907 -31.095 -12.949 1.00 14.49 ?  19  LYS   B C    1 
ATOM   3891 O  O    . LYS   B 1 19  ? 44.990 -30.661 -11.799 1.00 14.43 ?  19  LYS   B O    1 
ATOM   3892 C  CB   . LYS   B 1 19  ? 44.787 -29.248 -14.607 1.00 16.27 ?  19  LYS   B CB   1 
ATOM   3893 C  CG   . LYS   B 1 19  ? 46.001 -29.652 -15.424 1.00 17.90 ?  19  LYS   B CG   1 
ATOM   3894 C  CD   . LYS   B 1 19  ? 46.718 -28.416 -15.953 1.00 19.59 ?  19  LYS   B CD   1 
ATOM   3895 C  CE   . LYS   B 1 19  ? 47.906 -28.790 -16.817 1.00 21.43 ?  19  LYS   B CE   1 
ATOM   3896 N  NZ   . LYS   B 1 19  ? 48.643 -27.598 -17.306 1.00 22.80 ?  19  LYS   B NZ   1 
ATOM   3897 H  H    . LYS   B 1 19  ? 42.920 -29.692 -12.498 1.00 16.71 ?  19  LYS   B H    1 
ATOM   3898 H  HA   . LYS   B 1 19  ? 43.781 -31.052 -14.663 1.00 17.74 ?  19  LYS   B HA   1 
ATOM   3899 H  HB2  . LYS   B 1 19  ? 44.182 -28.767 -15.195 1.00 19.52 ?  19  LYS   B HB2  1 
ATOM   3900 H  HB3  . LYS   B 1 19  ? 45.086 -28.655 -13.897 1.00 19.52 ?  19  LYS   B HB3  1 
ATOM   3901 H  HG2  . LYS   B 1 19  ? 46.613 -30.151 -14.864 1.00 21.48 ?  19  LYS   B HG2  1 
ATOM   3902 H  HG3  . LYS   B 1 19  ? 45.712 -30.191 -16.178 1.00 21.48 ?  19  LYS   B HG3  1 
ATOM   3903 H  HD2  . LYS   B 1 19  ? 46.100 -27.894 -16.490 1.00 23.51 ?  19  LYS   B HD2  1 
ATOM   3904 H  HD3  . LYS   B 1 19  ? 47.038 -27.889 -15.203 1.00 23.51 ?  19  LYS   B HD3  1 
ATOM   3905 H  HE2  . LYS   B 1 19  ? 48.517 -29.335 -16.295 1.00 25.72 ?  19  LYS   B HE2  1 
ATOM   3906 H  HE3  . LYS   B 1 19  ? 47.591 -29.292 -17.587 1.00 25.72 ?  19  LYS   B HE3  1 
ATOM   3907 H  HZ1  . LYS   B 1 19  ? 49.247 -27.842 -17.914 1.00 27.36 ?  19  LYS   B HZ1  1 
ATOM   3908 H  HZ2  . LYS   B 1 19  ? 48.077 -27.021 -17.678 1.00 27.36 ?  19  LYS   B HZ2  1 
ATOM   3909 H  HZ3  . LYS   B 1 19  ? 49.061 -27.199 -16.630 1.00 27.36 ?  19  LYS   B HZ3  1 
ATOM   3910 N  N    . ASN   B 1 20  ? 45.593 -32.148 -13.382 1.00 15.48 ?  20  ASN   B N    1 
ATOM   3911 C  CA   . ASN   B 1 20  ? 46.629 -32.773 -12.570 1.00 16.64 ?  20  ASN   B CA   1 
ATOM   3912 C  C    . ASN   B 1 20  ? 47.899 -31.950 -12.750 1.00 17.16 ?  20  ASN   B C    1 
ATOM   3913 O  O    . ASN   B 1 20  ? 48.540 -32.017 -13.806 1.00 19.18 ?  20  ASN   B O    1 
ATOM   3914 C  CB   . ASN   B 1 20  ? 46.814 -34.220 -13.023 1.00 18.09 ?  20  ASN   B CB   1 
ATOM   3915 C  CG   . ASN   B 1 20  ? 47.973 -34.925 -12.338 1.00 19.55 ?  20  ASN   B CG   1 
ATOM   3916 O  OD1  . ASN   B 1 20  ? 48.649 -35.751 -12.952 1.00 21.70 ?  20  ASN   B OD1  1 
ATOM   3917 N  ND2  . ASN   B 1 20  ? 48.200 -34.622 -11.070 1.00 19.07 ?  20  ASN   B ND2  1 
ATOM   3918 H  H    . ASN   B 1 20  ? 45.476 -32.518 -14.148 1.00 18.58 ?  20  ASN   B H    1 
ATOM   3919 H  HA   . ASN   B 1 20  ? 46.363 -32.761 -11.637 1.00 19.97 ?  20  ASN   B HA   1 
ATOM   3920 H  HB2  . ASN   B 1 20  ? 46.004 -34.716 -12.822 1.00 21.71 ?  20  ASN   B HB2  1 
ATOM   3921 H  HB3  . ASN   B 1 20  ? 46.976 -34.227 -13.979 1.00 21.71 ?  20  ASN   B HB3  1 
ATOM   3922 H  HD21 . ASN   B 1 20  ? 48.852 -34.994 -10.652 1.00 22.89 ?  20  ASN   B HD21 1 
ATOM   3923 H  HD22 . ASN   B 1 20  ? 47.705 -34.046 -10.666 1.00 22.89 ?  20  ASN   B HD22 1 
ATOM   3924 N  N    . ALA   B 1 21  ? 48.255 -31.158 -11.736 1.00 16.76 ?  21  ALA   B N    1 
ATOM   3925 C  CA   . ALA   B 1 21  ? 49.355 -30.220 -11.886 1.00 17.47 ?  21  ALA   B CA   1 
ATOM   3926 C  C    . ALA   B 1 21  ? 49.813 -29.731 -10.522 1.00 16.76 ?  21  ALA   B C    1 
ATOM   3927 O  O    . ALA   B 1 21  ? 49.070 -29.768 -9.537  1.00 16.71 ?  21  ALA   B O    1 
ATOM   3928 C  CB   . ALA   B 1 21  ? 48.941 -29.045 -12.768 1.00 18.75 ?  21  ALA   B CB   1 
ATOM   3929 H  H    . ALA   B 1 21  ? 47.878 -31.156 -10.958 1.00 20.11 ?  21  ALA   B H    1 
ATOM   3930 H  HA   . ALA   B 1 21  ? 50.100 -30.679 -12.306 1.00 20.97 ?  21  ALA   B HA   1 
ATOM   3931 H  HB1  . ALA   B 1 21  ? 49.728 -28.531 -12.968 1.00 22.51 ?  21  ALA   B HB1  1 
ATOM   3932 H  HB2  . ALA   B 1 21  ? 48.553 -29.401 -13.584 1.00 22.51 ?  21  ALA   B HB2  1 
ATOM   3933 H  HB3  . ALA   B 1 21  ? 48.286 -28.516 -12.293 1.00 22.51 ?  21  ALA   B HB3  1 
ATOM   3934 N  N    . ASP   B 1 22  ? 51.071 -29.293 -10.495 1.00 15.79 ?  22  ASP   B N    1 
ATOM   3935 C  CA   . ASP   B 1 22  ? 51.682 -28.596 -9.368  1.00 14.94 ?  22  ASP   B CA   1 
ATOM   3936 C  C    . ASP   B 1 22  ? 51.271 -27.128 -9.453  1.00 13.59 ?  22  ASP   B C    1 
ATOM   3937 O  O    . ASP   B 1 22  ? 51.572 -26.460 -10.445 1.00 13.80 ?  22  ASP   B O    1 
ATOM   3938 C  CB   . ASP   B 1 22  ? 53.198 -28.772 -9.520  1.00 16.54 ?  22  ASP   B CB   1 
ATOM   3939 C  CG   . ASP   B 1 22  ? 54.025 -28.002 -8.498  1.00 18.08 ?  22  ASP   B CG   1 
ATOM   3940 O  OD1  . ASP   B 1 22  ? 53.657 -26.885 -8.100  1.00 18.38 ?  22  ASP   B OD1  1 
ATOM   3941 O  OD2  . ASP   B 1 22  ? 55.101 -28.520 -8.119  1.00 20.45 -1 22  ASP   B OD2  1 
ATOM   3942 H  H    . ASP   B 1 22  ? 51.621 -29.400 -11.155 1.00 18.96 ?  22  ASP   B H    1 
ATOM   3943 H  HA   . ASP   B 1 22  ? 51.388 -28.982 -8.525  1.00 17.93 ?  22  ASP   B HA   1 
ATOM   3944 H  HB2  . ASP   B 1 22  ? 53.423 -29.707 -9.427  1.00 19.85 ?  22  ASP   B HB2  1 
ATOM   3945 H  HB3  . ASP   B 1 22  ? 53.464 -28.451 -10.396 1.00 19.85 ?  22  ASP   B HB3  1 
ATOM   3946 N  N    . ILE   B 1 23  ? 50.560 -26.637 -8.432  1.00 13.40 ?  23  ILE   B N    1 
ATOM   3947 C  CA   . ILE   B 1 23  ? 49.965 -25.302 -8.502  1.00 12.92 ?  23  ILE   B CA   1 
ATOM   3948 C  C    . ILE   B 1 23  ? 51.019 -24.211 -8.640  1.00 12.33 ?  23  ILE   B C    1 
ATOM   3949 O  O    . ILE   B 1 23  ? 50.752 -23.166 -9.239  1.00 12.24 ?  23  ILE   B O    1 
ATOM   3950 C  CB   . ILE   B 1 23  ? 49.027 -25.069 -7.304  1.00 13.28 ?  23  ILE   B CB   1 
ATOM   3951 C  CG1  . ILE   B 1 23  ? 48.191 -23.807 -7.512  1.00 14.00 ?  23  ILE   B CG1  1 
ATOM   3952 C  CG2  . ILE   B 1 23  ? 49.796 -25.025 -6.000  1.00 14.17 ?  23  ILE   B CG2  1 
ATOM   3953 C  CD1  . ILE   B 1 23  ? 47.068 -23.648 -6.507  1.00 14.57 ?  23  ILE   B CD1  1 
ATOM   3954 H  H    . ILE   B 1 23  ? 50.413 -27.059 -7.696  1.00 16.08 ?  23  ILE   B H    1 
ATOM   3955 H  HA   . ILE   B 1 23  ? 49.417 -25.267 -9.298  1.00 15.51 ?  23  ILE   B HA   1 
ATOM   3956 H  HB   . ILE   B 1 23  ? 48.414 -25.822 -7.260  1.00 15.94 ?  23  ILE   B HB   1 
ATOM   3957 H  HG12 . ILE   B 1 23  ? 48.772 -23.033 -7.436  1.00 16.81 ?  23  ILE   B HG12 1 
ATOM   3958 H  HG13 . ILE   B 1 23  ? 47.799 -23.834 -8.401  1.00 16.81 ?  23  ILE   B HG13 1 
ATOM   3959 H  HG21 . ILE   B 1 23  ? 49.166 -25.025 -5.262  1.00 17.01 ?  23  ILE   B HG21 1 
ATOM   3960 H  HG22 . ILE   B 1 23  ? 50.369 -25.805 -5.944  1.00 17.01 ?  23  ILE   B HG22 1 
ATOM   3961 H  HG23 . ILE   B 1 23  ? 50.332 -24.218 -5.977  1.00 17.01 ?  23  ILE   B HG23 1 
ATOM   3962 H  HD11 . ILE   B 1 23  ? 46.538 -22.874 -6.748  1.00 17.49 ?  23  ILE   B HD11 1 
ATOM   3963 H  HD12 . ILE   B 1 23  ? 46.515 -24.448 -6.530  1.00 17.49 ?  23  ILE   B HD12 1 
ATOM   3964 H  HD13 . ILE   B 1 23  ? 47.448 -23.534 -5.625  1.00 17.49 ?  23  ILE   B HD13 1 
ATOM   3965 N  N    . VAL   B 1 24  ? 52.213 -24.416 -8.084  1.00 12.73 ?  24  VAL   B N    1 
ATOM   3966 C  CA   . VAL   B 1 24  ? 53.286 -23.435 -8.253  1.00 13.04 ?  24  VAL   B CA   1 
ATOM   3967 C  C    . VAL   B 1 24  ? 53.738 -23.389 -9.706  1.00 13.37 ?  24  VAL   B C    1 
ATOM   3968 O  O    . VAL   B 1 24  ? 53.873 -22.313 -10.304 1.00 13.83 ?  24  VAL   B O    1 
ATOM   3969 C  CB   . VAL   B 1 24  ? 54.466 -23.750 -7.310  1.00 14.20 ?  24  VAL   B CB   1 
ATOM   3970 C  CG1  . VAL   B 1 24  ? 55.674 -22.875 -7.643  1.00 15.07 ?  24  VAL   B CG1  1 
ATOM   3971 C  CG2  . VAL   B 1 24  ? 54.054 -23.562 -5.870  1.00 15.25 ?  24  VAL   B CG2  1 
ATOM   3972 H  H    . VAL   B 1 24  ? 52.427 -25.103 -7.613  1.00 15.28 ?  24  VAL   B H    1 
ATOM   3973 H  HA   . VAL   B 1 24  ? 52.949 -22.559 -8.017  1.00 15.65 ?  24  VAL   B HA   1 
ATOM   3974 H  HB   . VAL   B 1 24  ? 54.729 -24.678 -7.426  1.00 17.04 ?  24  VAL   B HB   1 
ATOM   3975 H  HG11 . VAL   B 1 24  ? 56.273 -22.861 -6.880  1.00 18.09 ?  24  VAL   B HG11 1 
ATOM   3976 H  HG12 . VAL   B 1 24  ? 56.132 -23.248 -8.412  1.00 18.09 ?  24  VAL   B HG12 1 
ATOM   3977 H  HG13 . VAL   B 1 24  ? 55.369 -21.976 -7.839  1.00 18.09 ?  24  VAL   B HG13 1 
ATOM   3978 H  HG21 . VAL   B 1 24  ? 54.770 -23.868 -5.293  1.00 18.30 ?  24  VAL   B HG21 1 
ATOM   3979 H  HG22 . VAL   B 1 24  ? 53.881 -22.622 -5.714  1.00 18.30 ?  24  VAL   B HG22 1 
ATOM   3980 H  HG23 . VAL   B 1 24  ? 53.250 -24.080 -5.701  1.00 18.30 ?  24  VAL   B HG23 1 
ATOM   3981 N  N    . GLU   B 1 25  ? 54.003 -24.560 -10.290 1.00 14.78 ?  25  GLU   B N    1 
ATOM   3982 C  CA   . GLU   B 1 25  ? 54.392 -24.597 -11.693 1.00 15.98 ?  25  GLU   B CA   1 
ATOM   3983 C  C    . GLU   B 1 25  ? 53.284 -24.048 -12.576 1.00 14.69 ?  25  GLU   B C    1 
ATOM   3984 O  O    . GLU   B 1 25  ? 53.550 -23.338 -13.554 1.00 15.75 ?  25  GLU   B O    1 
ATOM   3985 C  CB   . GLU   B 1 25  ? 54.777 -26.020 -12.089 1.00 19.33 ?  25  GLU   B CB   1 
ATOM   3986 C  CG   . GLU   B 1 25  ? 56.067 -26.477 -11.427 1.00 24.08 ?  25  GLU   B CG   1 
ATOM   3987 C  CD   . GLU   B 1 25  ? 57.185 -25.447 -11.529 1.00 28.44 ?  25  GLU   B CD   1 
ATOM   3988 O  OE1  . GLU   B 1 25  ? 57.552 -25.071 -12.664 1.00 30.02 ?  25  GLU   B OE1  1 
ATOM   3989 O  OE2  . GLU   B 1 25  ? 57.687 -24.992 -10.474 1.00 30.02 -1 25  GLU   B OE2  1 
ATOM   3990 H  H    . GLU   B 1 25  ? 53.961 -25.327 -9.901  1.00 17.74 ?  25  GLU   B H    1 
ATOM   3991 H  HA   . GLU   B 1 25  ? 55.152 -24.017 -11.819 1.00 19.18 ?  25  GLU   B HA   1 
ATOM   3992 H  HB2  . GLU   B 1 25  ? 54.072 -26.632 -11.817 1.00 23.20 ?  25  GLU   B HB2  1 
ATOM   3993 H  HB3  . GLU   B 1 25  ? 54.899 -26.063 -13.051 1.00 23.20 ?  25  GLU   B HB3  1 
ATOM   3994 H  HG2  . GLU   B 1 25  ? 55.906 -26.630 -10.488 1.00 28.89 ?  25  GLU   B HG2  1 
ATOM   3995 H  HG3  . GLU   B 1 25  ? 56.373 -27.291 -11.858 1.00 28.89 ?  25  GLU   B HG3  1 
ATOM   3996 N  N    A GLU   B 1 26  ? 52.032 -24.357 -12.239 0.72 13.89 ?  26  GLU   B N    1 
ATOM   3997 N  N    B GLU   B 1 26  ? 52.030 -24.362 -12.243 0.28 14.44 ?  26  GLU   B N    1 
ATOM   3998 C  CA   A GLU   B 1 26  ? 50.908 -23.833 -13.004 0.72 14.72 ?  26  GLU   B CA   1 
ATOM   3999 C  CA   B GLU   B 1 26  ? 50.906 -23.832 -13.007 0.28 14.82 ?  26  GLU   B CA   1 
ATOM   4000 C  C    A GLU   B 1 26  ? 50.855 -22.317 -12.925 0.72 14.08 ?  26  GLU   B C    1 
ATOM   4001 C  C    B GLU   B 1 26  ? 50.860 -22.315 -12.927 0.28 13.97 ?  26  GLU   B C    1 
ATOM   4002 O  O    A GLU   B 1 26  ? 50.656 -21.640 -13.938 0.72 15.09 ?  26  GLU   B O    1 
ATOM   4003 O  O    B GLU   B 1 26  ? 50.686 -21.633 -13.942 0.28 14.34 ?  26  GLU   B O    1 
ATOM   4004 C  CB   A GLU   B 1 26  ? 49.598 -24.424 -12.480 0.72 16.87 ?  26  GLU   B CB   1 
ATOM   4005 C  CB   B GLU   B 1 26  ? 49.595 -24.425 -12.490 0.28 16.34 ?  26  GLU   B CB   1 
ATOM   4006 C  CG   A GLU   B 1 26  ? 49.186 -25.713 -13.142 0.72 19.90 ?  26  GLU   B CG   1 
ATOM   4007 C  CG   B GLU   B 1 26  ? 49.192 -25.718 -13.162 0.28 18.14 ?  26  GLU   B CG   1 
ATOM   4008 C  CD   A GLU   B 1 26  ? 48.923 -25.545 -14.636 0.72 21.48 ?  26  GLU   B CD   1 
ATOM   4009 C  CD   B GLU   B 1 26  ? 48.947 -25.576 -14.652 0.28 19.34 ?  26  GLU   B CD   1 
ATOM   4010 O  OE1  A GLU   B 1 26  ? 47.920 -24.907 -15.025 0.72 21.78 ?  26  GLU   B OE1  1 
ATOM   4011 O  OE1  B GLU   B 1 26  ? 48.059 -24.794 -15.050 0.28 19.29 ?  26  GLU   B OE1  1 
ATOM   4012 O  OE2  A GLU   B 1 26  ? 49.731 -26.054 -15.424 0.72 23.12 -1 26  GLU   B OE2  1 
ATOM   4013 O  OE2  B GLU   B 1 26  ? 49.640 -26.263 -15.426 0.28 20.33 -1 26  GLU   B OE2  1 
ATOM   4014 H  H    A GLU   B 1 26  ? 51.808 -24.870 -11.581 0.72 16.67 ?  26  GLU   B H    1 
ATOM   4015 H  H    B GLU   B 1 26  ? 51.807 -24.876 -11.589 0.28 17.33 ?  26  GLU   B H    1 
ATOM   4016 H  HA   A GLU   B 1 26  ? 51.010 -24.085 -13.933 0.72 17.66 ?  26  GLU   B HA   1 
ATOM   4017 H  HA   B GLU   B 1 26  ? 51.010 -24.081 -13.936 0.28 17.79 ?  26  GLU   B HA   1 
ATOM   4018 H  HB2  A GLU   B 1 26  ? 49.687 -24.596 -11.531 0.72 20.24 ?  26  GLU   B HB2  1 
ATOM   4019 H  HB2  B GLU   B 1 26  ? 49.686 -24.607 -11.539 0.28 19.61 ?  26  GLU   B HB2  1 
ATOM   4020 H  HB3  A GLU   B 1 26  ? 48.885 -23.781 -12.630 0.72 20.24 ?  26  GLU   B HB3  1 
ATOM   4021 H  HB3  B GLU   B 1 26  ? 48.883 -23.783 -12.632 0.28 19.61 ?  26  GLU   B HB3  1 
ATOM   4022 H  HG2  A GLU   B 1 26  ? 49.896 -26.363 -13.013 0.72 23.89 ?  26  GLU   B HG2  1 
ATOM   4023 H  HG2  B GLU   B 1 26  ? 49.902 -26.359 -13.037 0.28 21.77 ?  26  GLU   B HG2  1 
ATOM   4024 H  HG3  A GLU   B 1 26  ? 48.367 -26.033 -12.731 0.72 23.89 ?  26  GLU   B HG3  1 
ATOM   4025 H  HG3  B GLU   B 1 26  ? 48.370 -26.034 -12.763 0.28 21.77 ?  26  GLU   B HG3  1 
ATOM   4026 N  N    . ALA   B 1 27  ? 51.001 -21.767 -11.719 1.00 13.03 ?  27  ALA   B N    1 
ATOM   4027 C  CA   . ALA   B 1 27  ? 50.961 -20.320 -11.564 1.00 13.67 ?  27  ALA   B CA   1 
ATOM   4028 C  C    . ALA   B 1 27  ? 52.033 -19.653 -12.412 1.00 14.59 ?  27  ALA   B C    1 
ATOM   4029 O  O    . ALA   B 1 27  ? 51.780 -18.638 -13.076 1.00 15.01 ?  27  ALA   B O    1 
ATOM   4030 C  CB   . ALA   B 1 27  ? 51.116 -19.949 -10.091 1.00 13.65 ?  27  ALA   B CB   1 
ATOM   4031 H  H    A ALA   B 1 27  ? 51.116 -22.204 -10.986 0.72 15.64 ?  27  ALA   B H    1 
ATOM   4032 H  H    B ALA   B 1 27  ? 51.118 -22.205 -10.986 0.28 15.64 ?  27  ALA   B H    1 
ATOM   4033 H  HA   . ALA   B 1 27  ? 50.103 -19.990 -11.864 1.00 16.41 ?  27  ALA   B HA   1 
ATOM   4034 H  HB1  . ALA   B 1 27  ? 51.083 -18.984 -10.002 1.00 16.39 ?  27  ALA   B HB1  1 
ATOM   4035 H  HB2  . ALA   B 1 27  ? 50.387 -20.350 -9.589  1.00 16.39 ?  27  ALA   B HB2  1 
ATOM   4036 H  HB3  . ALA   B 1 27  ? 51.964 -20.285 -9.766  1.00 16.39 ?  27  ALA   B HB3  1 
ATOM   4037 N  N    . LYS   B 1 28  ? 53.242 -20.211 -12.410 1.00 15.80 ?  28  LYS   B N    1 
ATOM   4038 C  CA   . LYS   B 1 28  ? 54.321 -19.587 -13.164 1.00 17.69 ?  28  LYS   B CA   1 
ATOM   4039 C  C    . LYS   B 1 28  ? 54.071 -19.652 -14.666 1.00 18.45 ?  28  LYS   B C    1 
ATOM   4040 O  O    . LYS   B 1 28  ? 54.472 -18.739 -15.398 1.00 19.74 ?  28  LYS   B O    1 
ATOM   4041 C  CB   . LYS   B 1 28  ? 55.673 -20.194 -12.772 1.00 19.92 ?  28  LYS   B CB   1 
ATOM   4042 C  CG   . LYS   B 1 28  ? 56.075 -19.866 -11.334 1.00 22.88 ?  28  LYS   B CG   1 
ATOM   4043 C  CD   . LYS   B 1 28  ? 57.508 -20.259 -11.009 1.00 26.48 ?  28  LYS   B CD   1 
ATOM   4044 C  CE   . LYS   B 1 28  ? 57.626 -21.735 -10.716 1.00 28.65 ?  28  LYS   B CE   1 
ATOM   4045 N  NZ   . LYS   B 1 28  ? 58.979 -22.083 -10.199 1.00 30.01 ?  28  LYS   B NZ   1 
ATOM   4046 H  H    . LYS   B 1 28  ? 53.463 -20.930 -11.988 1.00 18.96 ?  28  LYS   B H    1 
ATOM   4047 H  HA   . LYS   B 1 28  ? 54.357 -18.648 -12.926 1.00 21.23 ?  28  LYS   B HA   1 
ATOM   4048 H  HB2  . LYS   B 1 28  ? 55.628 -21.157 -12.853 1.00 23.91 ?  28  LYS   B HB2  1 
ATOM   4049 H  HB3  . LYS   B 1 28  ? 56.364 -19.842 -13.358 1.00 23.91 ?  28  LYS   B HB3  1 
ATOM   4050 H  HG2  . LYS   B 1 28  ? 55.986 -18.907 -11.196 1.00 27.46 ?  28  LYS   B HG2  1 
ATOM   4051 H  HG3  . LYS   B 1 28  ? 55.486 -20.341 -10.728 1.00 27.46 ?  28  LYS   B HG3  1 
ATOM   4052 H  HD2  . LYS   B 1 28  ? 58.074 -20.050 -11.769 1.00 31.77 ?  28  LYS   B HD2  1 
ATOM   4053 H  HD3  . LYS   B 1 28  ? 57.802 -19.765 -10.227 1.00 31.77 ?  28  LYS   B HD3  1 
ATOM   4054 H  HE2  . LYS   B 1 28  ? 56.970 -21.981 -10.043 1.00 34.38 ?  28  LYS   B HE2  1 
ATOM   4055 H  HE3  . LYS   B 1 28  ? 57.472 -22.238 -11.531 1.00 34.38 ?  28  LYS   B HE3  1 
ATOM   4056 H  HZ1  . LYS   B 1 28  ? 59.026 -22.956 -10.032 1.00 36.01 ?  28  LYS   B HZ1  1 
ATOM   4057 H  HZ2  . LYS   B 1 28  ? 59.598 -21.869 -10.801 1.00 36.01 ?  28  LYS   B HZ2  1 
ATOM   4058 H  HZ3  . LYS   B 1 28  ? 59.141 -21.636 -9.446  1.00 36.01 ?  28  LYS   B HZ3  1 
ATOM   4059 N  N    . LYS   B 1 29  ? 53.377 -20.691 -15.135 1.00 19.41 ?  29  LYS   B N    1 
ATOM   4060 C  CA   . LYS   B 1 29  ? 53.082 -20.822 -16.560 1.00 21.86 ?  29  LYS   B CA   1 
ATOM   4061 C  C    . LYS   B 1 29  ? 51.845 -20.027 -16.971 1.00 21.12 ?  29  LYS   B C    1 
ATOM   4062 O  O    . LYS   B 1 29  ? 51.856 -19.356 -18.009 1.00 22.60 ?  29  LYS   B O    1 
ATOM   4063 C  CB   . LYS   B 1 29  ? 52.894 -22.296 -16.915 1.00 26.11 ?  29  LYS   B CB   1 
ATOM   4064 C  CG   . LYS   B 1 29  ? 52.786 -22.563 -18.407 1.00 29.82 ?  29  LYS   B CG   1 
ATOM   4065 C  CD   . LYS   B 1 29  ? 53.078 -24.022 -18.741 1.00 32.79 ?  29  LYS   B CD   1 
ATOM   4066 C  CE   . LYS   B 1 29  ? 52.027 -24.956 -18.165 1.00 34.56 ?  29  LYS   B CE   1 
ATOM   4067 N  NZ   . LYS   B 1 29  ? 52.300 -26.380 -18.519 1.00 35.39 ?  29  LYS   B NZ   1 
ATOM   4068 H  H    . LYS   B 1 29  ? 53.074 -21.332 -14.647 1.00 23.29 ?  29  LYS   B H    1 
ATOM   4069 H  HA   . LYS   B 1 29  ? 53.834 -20.486 -17.066 1.00 26.24 ?  29  LYS   B HA   1 
ATOM   4070 H  HB2  . LYS   B 1 29  ? 53.655 -22.797 -16.581 1.00 31.34 ?  29  LYS   B HB2  1 
ATOM   4071 H  HB3  . LYS   B 1 29  ? 52.081 -22.619 -16.498 1.00 31.34 ?  29  LYS   B HB3  1 
ATOM   4072 H  HG2  . LYS   B 1 29  ? 51.885 -22.358 -18.703 1.00 35.78 ?  29  LYS   B HG2  1 
ATOM   4073 H  HG3  . LYS   B 1 29  ? 53.428 -22.009 -18.878 1.00 35.78 ?  29  LYS   B HG3  1 
ATOM   4074 H  HD2  . LYS   B 1 29  ? 53.086 -24.134 -19.705 1.00 39.35 ?  29  LYS   B HD2  1 
ATOM   4075 H  HD3  . LYS   B 1 29  ? 53.939 -24.270 -18.369 1.00 39.35 ?  29  LYS   B HD3  1 
ATOM   4076 H  HE2  . LYS   B 1 29  ? 52.026 -24.880 -17.198 1.00 41.47 ?  29  LYS   B HE2  1 
ATOM   4077 H  HE3  . LYS   B 1 29  ? 51.157 -24.716 -18.521 1.00 41.47 ?  29  LYS   B HE3  1 
ATOM   4078 H  HZ1  . LYS   B 1 29  ? 51.672 -26.906 -18.171 1.00 42.46 ?  29  LYS   B HZ1  1 
ATOM   4079 H  HZ2  . LYS   B 1 29  ? 52.302 -26.479 -19.404 1.00 42.46 ?  29  LYS   B HZ2  1 
ATOM   4080 H  HZ3  . LYS   B 1 29  ? 53.093 -26.627 -18.199 1.00 42.46 ?  29  LYS   B HZ3  1 
ATOM   4081 N  N    . VAL   B 1 30  ? 50.772 -20.109 -16.180 1.00 19.49 ?  30  VAL   B N    1 
ATOM   4082 C  CA   . VAL   B 1 30  ? 49.481 -19.517 -16.544 1.00 19.77 ?  30  VAL   B CA   1 
ATOM   4083 C  C    . VAL   B 1 30  ? 49.483 -18.005 -16.374 1.00 18.59 ?  30  VAL   B C    1 
ATOM   4084 O  O    . VAL   B 1 30  ? 48.749 -17.291 -17.073 1.00 19.68 ?  30  VAL   B O    1 
ATOM   4085 C  CB   . VAL   B 1 30  ? 48.376 -20.149 -15.675 1.00 21.07 ?  30  VAL   B CB   1 
ATOM   4086 C  CG1  . VAL   B 1 30  ? 47.087 -19.335 -15.746 1.00 21.31 ?  30  VAL   B CG1  1 
ATOM   4087 C  CG2  . VAL   B 1 30  ? 48.132 -21.598 -16.082 1.00 21.76 ?  30  VAL   B CG2  1 
ATOM   4088 H  H    . VAL   B 1 30  ? 50.760 -20.524 -15.417 1.00 23.39 ?  30  VAL   B H    1 
ATOM   4089 H  HA   . VAL   B 1 30  ? 49.285 -19.738 -17.470 1.00 23.72 ?  30  VAL   B HA   1 
ATOM   4090 H  HB   . VAL   B 1 30  ? 48.665 -20.160 -14.748 1.00 25.28 ?  30  VAL   B HB   1 
ATOM   4091 H  HG11 . VAL   B 1 30  ? 46.342 -19.912 -15.507 1.00 25.57 ?  30  VAL   B HG11 1 
ATOM   4092 H  HG12 . VAL   B 1 30  ? 47.140 -18.598 -15.120 1.00 25.57 ?  30  VAL   B HG12 1 
ATOM   4093 H  HG13 . VAL   B 1 30  ? 46.964 -19.010 -16.647 1.00 25.57 ?  30  VAL   B HG13 1 
ATOM   4094 H  HG21 . VAL   B 1 30  ? 47.435 -21.977 -15.518 1.00 26.12 ?  30  VAL   B HG21 1 
ATOM   4095 H  HG22 . VAL   B 1 30  ? 47.848 -21.621 -17.010 1.00 26.12 ?  30  VAL   B HG22 1 
ATOM   4096 H  HG23 . VAL   B 1 30  ? 48.952 -22.101 -15.973 1.00 26.12 ?  30  VAL   B HG23 1 
ATOM   4097 N  N    . LYS   B 1 31  ? 50.262 -17.509 -15.428 1.00 18.50 ?  31  LYS   B N    1 
ATOM   4098 C  CA   . LYS   B 1 31  ? 50.290 -16.102 -15.060 1.00 18.77 ?  31  LYS   B CA   1 
ATOM   4099 C  C    . LYS   B 1 31  ? 48.885 -15.635 -14.679 1.00 16.58 ?  31  LYS   B C    1 
ATOM   4100 O  O    . LYS   B 1 31  ? 48.341 -14.716 -15.303 1.00 17.95 ?  31  LYS   B O    1 
ATOM   4101 C  CB   . LYS   B 1 31  ? 50.924 -15.276 -16.186 1.00 22.01 ?  31  LYS   B CB   1 
ATOM   4102 C  CG   . LYS   B 1 31  ? 52.345 -15.735 -16.534 1.00 25.11 ?  31  LYS   B CG   1 
ATOM   4103 C  CD   . LYS   B 1 31  ? 52.920 -14.964 -17.706 1.00 27.39 ?  31  LYS   B CD   1 
ATOM   4104 C  CE   . LYS   B 1 31  ? 54.399 -15.236 -17.873 1.00 28.81 ?  31  LYS   B CE   1 
ATOM   4105 N  NZ   . LYS   B 1 31  ? 55.147 -14.854 -16.646 1.00 29.72 ?  31  LYS   B NZ   1 
ATOM   4106 H  H    . LYS   B 1 31  ? 50.807 -17.998 -14.978 1.00 22.20 ?  31  LYS   B H    1 
ATOM   4107 H  HA   . LYS   B 1 31  ? 50.845 -16.018 -14.283 1.00 22.52 ?  31  LYS   B HA   1 
ATOM   4108 H  HB2  . LYS   B 1 31  ? 50.381 -15.353 -16.986 1.00 26.41 ?  31  LYS   B HB2  1 
ATOM   4109 H  HB3  . LYS   B 1 31  ? 50.970 -14.353 -15.901 1.00 26.41 ?  31  LYS   B HB3  1 
ATOM   4110 H  HG2  . LYS   B 1 31  ? 52.915 -15.599 -15.762 1.00 30.13 ?  31  LYS   B HG2  1 
ATOM   4111 H  HG3  . LYS   B 1 31  ? 52.327 -16.678 -16.771 1.00 30.13 ?  31  LYS   B HG3  1 
ATOM   4112 H  HD2  . LYS   B 1 31  ? 52.463 -15.236 -18.517 1.00 32.87 ?  31  LYS   B HD2  1 
ATOM   4113 H  HD3  . LYS   B 1 31  ? 52.797 -14.017 -17.550 1.00 32.87 ?  31  LYS   B HD3  1 
ATOM   4114 H  HE2  . LYS   B 1 31  ? 54.539 -16.184 -18.035 1.00 34.57 ?  31  LYS   B HE2  1 
ATOM   4115 H  HE3  . LYS   B 1 31  ? 54.741 -14.714 -18.616 1.00 34.57 ?  31  LYS   B HE3  1 
ATOM   4116 H  HZ1  . LYS   B 1 31  ? 56.022 -14.865 -16.807 1.00 35.66 ?  31  LYS   B HZ1  1 
ATOM   4117 H  HZ2  . LYS   B 1 31  ? 54.910 -14.036 -16.389 1.00 35.66 ?  31  LYS   B HZ2  1 
ATOM   4118 H  HZ3  . LYS   B 1 31  ? 54.968 -15.427 -15.989 1.00 35.66 ?  31  LYS   B HZ3  1 
ATOM   4119 N  N    . PRO   B 1 32  ? 48.272 -16.243 -13.657 1.00 14.42 ?  32  PRO   B N    1 
ATOM   4120 C  CA   . PRO   B 1 32  ? 46.887 -15.899 -13.308 1.00 13.47 ?  32  PRO   B CA   1 
ATOM   4121 C  C    . PRO   B 1 32  ? 46.798 -14.557 -12.605 1.00 13.70 ?  32  PRO   B C    1 
ATOM   4122 O  O    . PRO   B 1 32  ? 47.719 -14.134 -11.902 1.00 14.82 ?  32  PRO   B O    1 
ATOM   4123 C  CB   . PRO   B 1 32  ? 46.490 -17.019 -12.343 1.00 13.72 ?  32  PRO   B CB   1 
ATOM   4124 C  CG   . PRO   B 1 32  ? 47.785 -17.356 -11.661 1.00 14.23 ?  32  PRO   B CG   1 
ATOM   4125 C  CD   . PRO   B 1 32  ? 48.841 -17.238 -12.728 1.00 14.63 ?  32  PRO   B CD   1 
ATOM   4126 H  HA   . PRO   B 1 32  ? 46.312 -15.910 -14.090 1.00 16.16 ?  32  PRO   B HA   1 
ATOM   4127 H  HB2  . PRO   B 1 32  ? 45.835 -16.693 -11.703 1.00 16.47 ?  32  PRO   B HB2  1 
ATOM   4128 H  HB3  . PRO   B 1 32  ? 46.149 -17.780 -12.835 1.00 16.47 ?  32  PRO   B HB3  1 
ATOM   4129 H  HG2  . PRO   B 1 32  ? 47.955 -16.722 -10.941 1.00 17.08 ?  32  PRO   B HG2  1 
ATOM   4130 H  HG3  . PRO   B 1 32  ? 47.751 -18.262 -11.311 1.00 17.08 ?  32  PRO   B HG3  1 
ATOM   4131 H  HD2  . PRO   B 1 32  ? 49.669 -16.910 -12.348 1.00 17.56 ?  32  PRO   B HD2  1 
ATOM   4132 H  HD3  . PRO   B 1 32  ? 48.961 -18.089 -13.173 1.00 17.56 ?  32  PRO   B HD3  1 
ATOM   4133 N  N    . THR   B 1 33  ? 45.645 -13.903 -12.772 1.00 12.94 ?  33  THR   B N    1 
ATOM   4134 C  CA   . THR   B 1 33  ? 45.344 -12.725 -11.968 1.00 13.20 ?  33  THR   B CA   1 
ATOM   4135 C  C    . THR   B 1 33  ? 45.298 -13.077 -10.488 1.00 12.75 ?  33  THR   B C    1 
ATOM   4136 O  O    . THR   B 1 33  ? 45.760 -12.298 -9.644  1.00 13.60 ?  33  THR   B O    1 
ATOM   4137 C  CB   . THR   B 1 33  ? 44.025 -12.096 -12.417 1.00 13.89 ?  33  THR   B CB   1 
ATOM   4138 O  OG1  . THR   B 1 33  ? 44.082 -11.830 -13.820 1.00 13.92 ?  33  THR   B OG1  1 
ATOM   4139 C  CG2  . THR   B 1 33  ? 43.763 -10.802 -11.662 1.00 15.33 ?  33  THR   B CG2  1 
ATOM   4140 H  H    . THR   B 1 33  ? 45.024 -14.126 -13.329 1.00 15.53 ?  33  THR   B H    1 
ATOM   4141 H  HA   . THR   B 1 33  ? 46.040 -12.070 -12.095 1.00 15.84 ?  33  THR   B HA   1 
ATOM   4142 H  HB   . THR   B 1 33  ? 43.289 -12.710 -12.236 1.00 16.67 ?  33  THR   B HB   1 
ATOM   4143 H  HG1  . THR   B 1 33  ? 43.354 -11.471 -14.077 1.00 16.70 ?  33  THR   B HG1  1 
ATOM   4144 H  HG21 . THR   B 1 33  ? 43.018 -10.330 -12.062 1.00 18.40 ?  33  THR   B HG21 1 
ATOM   4145 H  HG22 . THR   B 1 33  ? 43.554 -10.995 -10.735 1.00 18.40 ?  33  THR   B HG22 1 
ATOM   4146 H  HG23 . THR   B 1 33  ? 44.551 -10.238 -11.700 1.00 18.40 ?  33  THR   B HG23 1 
ATOM   4147 N  N    . VAL   B 1 34  ? 44.757 -14.252 -10.152 1.00 11.99 ?  34  VAL   B N    1 
ATOM   4148 C  CA   . VAL   B 1 34  ? 44.564 -14.651 -8.762  1.00 11.44 ?  34  VAL   B CA   1 
ATOM   4149 C  C    . VAL   B 1 34  ? 45.003 -16.096 -8.605  1.00 10.83 ?  34  VAL   B C    1 
ATOM   4150 O  O    . VAL   B 1 34  ? 44.480 -16.982 -9.288  1.00 11.32 ?  34  VAL   B O    1 
ATOM   4151 C  CB   . VAL   B 1 34  ? 43.099 -14.514 -8.310  1.00 12.54 ?  34  VAL   B CB   1 
ATOM   4152 C  CG1  . VAL   B 1 34  ? 42.947 -14.973 -6.869  1.00 12.83 ?  34  VAL   B CG1  1 
ATOM   4153 C  CG2  . VAL   B 1 34  ? 42.598 -13.092 -8.487  1.00 13.71 ?  34  VAL   B CG2  1 
ATOM   4154 H  H    . VAL   B 1 34  ? 44.498 -14.844 -10.720 1.00 14.39 ?  34  VAL   B H    1 
ATOM   4155 H  HA   . VAL   B 1 34  ? 45.113 -14.100 -8.185  1.00 13.73 ?  34  VAL   B HA   1 
ATOM   4156 H  HB   . VAL   B 1 34  ? 42.547 -15.091 -8.861  1.00 15.05 ?  34  VAL   B HB   1 
ATOM   4157 H  HG11 . VAL   B 1 34  ? 42.096 -14.658 -6.523  1.00 15.40 ?  34  VAL   B HG11 1 
ATOM   4158 H  HG12 . VAL   B 1 34  ? 42.972 -15.944 -6.836  1.00 15.40 ?  34  VAL   B HG12 1 
ATOM   4159 H  HG13 . VAL   B 1 34  ? 43.672 -14.606 -6.339  1.00 15.40 ?  34  VAL   B HG13 1 
ATOM   4160 H  HG21 . VAL   B 1 34  ? 41.682 -13.035 -8.169  1.00 16.45 ?  34  VAL   B HG21 1 
ATOM   4161 H  HG22 . VAL   B 1 34  ? 43.162 -12.490 -7.977  1.00 16.45 ?  34  VAL   B HG22 1 
ATOM   4162 H  HG23 . VAL   B 1 34  ? 42.633 -12.858 -9.429  1.00 16.45 ?  34  VAL   B HG23 1 
ATOM   4163 N  N    . VAL   B 1 35  ? 45.917 -16.344 -7.672  1.00 10.39 ?  35  VAL   B N    1 
ATOM   4164 C  CA   . VAL   B 1 35  ? 46.157 -17.686 -7.156  1.00 10.36 ?  35  VAL   B CA   1 
ATOM   4165 C  C    . VAL   B 1 35  ? 45.619 -17.744 -5.738  1.00 9.90  ?  35  VAL   B C    1 
ATOM   4166 O  O    . VAL   B 1 35  ? 45.841 -16.820 -4.948  1.00 10.02 ?  35  VAL   B O    1 
ATOM   4167 C  CB   . VAL   B 1 35  ? 47.641 -18.104 -7.238  1.00 11.12 ?  35  VAL   B CB   1 
ATOM   4168 C  CG1  . VAL   B 1 35  ? 48.536 -17.272 -6.316  1.00 11.49 ?  35  VAL   B CG1  1 
ATOM   4169 C  CG2  . VAL   B 1 35  ? 47.783 -19.599 -6.922  1.00 11.69 ?  35  VAL   B CG2  1 
ATOM   4170 H  H    . VAL   B 1 35  ? 46.423 -15.742 -7.319  1.00 12.47 ?  35  VAL   B H    1 
ATOM   4171 H  HA   . VAL   B 1 35  ? 45.646 -18.319 -7.684  1.00 12.44 ?  35  VAL   B HA   1 
ATOM   4172 H  HB   . VAL   B 1 35  ? 47.949 -17.974 -8.149  1.00 13.35 ?  35  VAL   B HB   1 
ATOM   4173 H  HG11 . VAL   B 1 35  ? 49.461 -17.490 -6.498  1.00 13.79 ?  35  VAL   B HG11 1 
ATOM   4174 H  HG12 . VAL   B 1 35  ? 48.371 -16.335 -6.484  1.00 13.79 ?  35  VAL   B HG12 1 
ATOM   4175 H  HG13 . VAL   B 1 35  ? 48.321 -17.488 -5.393  1.00 13.79 ?  35  VAL   B HG13 1 
ATOM   4176 H  HG21 . VAL   B 1 35  ? 48.709 -19.863 -7.031  1.00 14.03 ?  35  VAL   B HG21 1 
ATOM   4177 H  HG22 . VAL   B 1 35  ? 47.501 -19.760 -6.004  1.00 14.03 ?  35  VAL   B HG22 1 
ATOM   4178 H  HG23 . VAL   B 1 35  ? 47.222 -20.111 -7.529  1.00 14.03 ?  35  VAL   B HG23 1 
ATOM   4179 N  N    . VAL   B 1 36  ? 44.895 -18.814 -5.421  1.00 9.91  ?  36  VAL   B N    1 
ATOM   4180 C  CA   . VAL   B 1 36  ? 44.356 -19.020 -4.087  1.00 9.74  ?  36  VAL   B CA   1 
ATOM   4181 C  C    . VAL   B 1 36  ? 45.367 -19.784 -3.243  1.00 9.65  ?  36  VAL   B C    1 
ATOM   4182 O  O    . VAL   B 1 36  ? 45.903 -20.817 -3.669  1.00 10.44 ?  36  VAL   B O    1 
ATOM   4183 C  CB   . VAL   B 1 36  ? 43.025 -19.784 -4.161  1.00 10.29 ?  36  VAL   B CB   1 
ATOM   4184 C  CG1  . VAL   B 1 36  ? 42.525 -20.151 -2.771  1.00 10.92 ?  36  VAL   B CG1  1 
ATOM   4185 C  CG2  . VAL   B 1 36  ? 42.000 -18.955 -4.908  1.00 11.13 ?  36  VAL   B CG2  1 
ATOM   4186 H  H    . VAL   B 1 36  ? 44.708 -19.446 -5.970  1.00 11.90 ?  36  VAL   B H    1 
ATOM   4187 H  HA   . VAL   B 1 36  ? 44.191 -18.160 -3.667  1.00 11.70 ?  36  VAL   B HA   1 
ATOM   4188 H  HB   . VAL   B 1 36  ? 43.164 -20.610 -4.653  1.00 12.35 ?  36  VAL   B HB   1 
ATOM   4189 H  HG11 . VAL   B 1 36  ? 41.589 -20.395 -2.828  1.00 13.10 ?  36  VAL   B HG11 1 
ATOM   4190 H  HG12 . VAL   B 1 36  ? 43.041 -20.895 -2.428  1.00 13.10 ?  36  VAL   B HG12 1 
ATOM   4191 H  HG13 . VAL   B 1 36  ? 42.627 -19.379 -2.187  1.00 13.10 ?  36  VAL   B HG13 1 
ATOM   4192 H  HG21 . VAL   B 1 36  ? 41.156 -19.428 -4.918  1.00 13.36 ?  36  VAL   B HG21 1 
ATOM   4193 H  HG22 . VAL   B 1 36  ? 41.899 -18.101 -4.460  1.00 13.36 ?  36  VAL   B HG22 1 
ATOM   4194 H  HG23 . VAL   B 1 36  ? 42.312 -18.814 -5.818  1.00 13.36 ?  36  VAL   B HG23 1 
ATOM   4195 N  N    . ASN   B 1 37  ? 45.594 -19.296 -2.025  1.00 9.71  ?  37  ASN   B N    1 
ATOM   4196 C  CA   . ASN   B 1 37  ? 46.356 -20.020 -1.022  1.00 10.25 ?  37  ASN   B CA   1 
ATOM   4197 C  C    . ASN   B 1 37  ? 45.413 -20.695 -0.034  1.00 10.36 ?  37  ASN   B C    1 
ATOM   4198 O  O    . ASN   B 1 37  ? 44.402 -20.118 0.380   1.00 10.46 ?  37  ASN   B O    1 
ATOM   4199 C  CB   . ASN   B 1 37  ? 47.287 -19.074 -0.266  1.00 10.15 ?  37  ASN   B CB   1 
ATOM   4200 C  CG   . ASN   B 1 37  ? 48.142 -19.790 0.745   1.00 10.47 ?  37  ASN   B CG   1 
ATOM   4201 O  OD1  . ASN   B 1 37  ? 48.485 -20.966 0.564   1.00 11.02 ?  37  ASN   B OD1  1 
ATOM   4202 N  ND2  . ASN   B 1 37  ? 48.486 -19.097 1.823   1.00 10.65 ?  37  ASN   B ND2  1 
ATOM   4203 H  H    . ASN   B 1 37  ? 45.308 -18.529 -1.746  1.00 11.66 ?  37  ASN   B H    1 
ATOM   4204 H  HA   . ASN   B 1 37  ? 46.887 -20.711 -1.450  1.00 12.30 ?  37  ASN   B HA   1 
ATOM   4205 H  HB2  . ASN   B 1 37  ? 47.875 -18.645 -0.905  1.00 12.19 ?  37  ASN   B HB2  1 
ATOM   4206 H  HB3  . ASN   B 1 37  ? 46.757 -18.416 0.202   1.00 12.19 ?  37  ASN   B HB3  1 
ATOM   4207 H  HD21 . ASN   B 1 37  ? 48.971 -19.467 2.434   1.00 12.78 ?  37  ASN   B HD21 1 
ATOM   4208 H  HD22 . ASN   B 1 37  ? 48.223 -18.293 1.920   1.00 12.78 ?  37  ASN   B HD22 1 
ATOM   4209 N  N    . ALA   B 1 38  ? 45.767 -21.926 0.343   1.00 10.14 ?  38  ALA   B N    1 
ATOM   4210 C  CA   . ALA   B 1 38  ? 45.107 -22.673 1.413   1.00 10.41 ?  38  ALA   B CA   1 
ATOM   4211 C  C    . ALA   B 1 38  ? 45.695 -22.195 2.737   1.00 10.86 ?  38  ALA   B C    1 
ATOM   4212 O  O    . ALA   B 1 38  ? 46.601 -22.800 3.319   1.00 11.48 ?  38  ALA   B O    1 
ATOM   4213 C  CB   . ALA   B 1 38  ? 45.329 -24.164 1.213   1.00 11.48 ?  38  ALA   B CB   1 
ATOM   4214 H  H    . ALA   B 1 38  ? 46.424 -22.356 -0.006  1.00 12.17 ?  38  ALA   B H    1 
ATOM   4215 H  HA   . ALA   B 1 38  ? 44.153 -22.489 1.408   1.00 12.49 ?  38  ALA   B HA   1 
ATOM   4216 H  HB1  . ALA   B 1 38  ? 44.877 -24.650 1.931   1.00 13.78 ?  38  ALA   B HB1  1 
ATOM   4217 H  HB2  . ALA   B 1 38  ? 44.950 -24.429 0.359   1.00 13.78 ?  38  ALA   B HB2  1 
ATOM   4218 H  HB3  . ALA   B 1 38  ? 46.274 -24.354 1.234   1.00 13.78 ?  38  ALA   B HB3  1 
ATOM   4219 N  N    . ALA   B 1 39  ? 45.185 -21.051 3.193   1.00 10.35 ?  39  ALA   B N    1 
ATOM   4220 C  CA   . ALA   B 1 39  ? 45.734 -20.317 4.321   1.00 10.65 ?  39  ALA   B CA   1 
ATOM   4221 C  C    . ALA   B 1 39  ? 45.115 -20.764 5.642   1.00 10.76 ?  39  ALA   B C    1 
ATOM   4222 O  O    . ALA   B 1 39  ? 44.092 -21.450 5.690   1.00 11.70 ?  39  ALA   B O    1 
ATOM   4223 C  CB   . ALA   B 1 39  ? 45.495 -18.817 4.134   1.00 11.39 ?  39  ALA   B CB   1 
ATOM   4224 H  H    . ALA   B 1 39  ? 44.494 -20.672 2.847   1.00 12.42 ?  39  ALA   B H    1 
ATOM   4225 H  HA   . ALA   B 1 39  ? 46.685 -20.468 4.367   1.00 12.78 ?  39  ALA   B HA   1 
ATOM   4226 H  HB1  . ALA   B 1 39  ? 45.868 -18.342 4.895   1.00 13.67 ?  39  ALA   B HB1  1 
ATOM   4227 H  HB2  . ALA   B 1 39  ? 45.936 -18.527 3.318   1.00 13.67 ?  39  ALA   B HB2  1 
ATOM   4228 H  HB3  . ALA   B 1 39  ? 44.543 -18.649 4.073   1.00 13.67 ?  39  ALA   B HB3  1 
ATOM   4229 N  N    . ASN   B 1 40  ? 45.751 -20.335 6.729   1.00 11.63 ?  40  ASN   B N    1 
ATOM   4230 C  CA   . ASN   B 1 40  ? 45.197 -20.391 8.073   1.00 12.18 ?  40  ASN   B CA   1 
ATOM   4231 C  C    . ASN   B 1 40  ? 45.022 -18.965 8.601   1.00 11.65 ?  40  ASN   B C    1 
ATOM   4232 O  O    . ASN   B 1 40  ? 45.429 -17.984 7.969   1.00 11.87 ?  40  ASN   B O    1 
ATOM   4233 C  CB   . ASN   B 1 40  ? 46.054 -21.268 9.006   1.00 13.37 ?  40  ASN   B CB   1 
ATOM   4234 C  CG   . ASN   B 1 40  ? 47.509 -20.866 9.022   1.00 14.09 ?  40  ASN   B CG   1 
ATOM   4235 O  OD1  . ASN   B 1 40  ? 47.829 -19.686 9.069   1.00 15.62 ?  40  ASN   B OD1  1 
ATOM   4236 N  ND2  . ASN   B 1 40  ? 48.402 -21.845 8.996   1.00 14.54 ?  40  ASN   B ND2  1 
ATOM   4237 H  H    . ASN   B 1 40  ? 46.541 -19.995 6.705   1.00 13.96 ?  40  ASN   B H    1 
ATOM   4238 H  HA   . ASN   B 1 40  ? 44.316 -20.792 8.030   1.00 14.62 ?  40  ASN   B HA   1 
ATOM   4239 H  HB2  . ASN   B 1 40  ? 45.712 -21.195 9.912   1.00 16.05 ?  40  ASN   B HB2  1 
ATOM   4240 H  HB3  . ASN   B 1 40  ? 46.004 -22.189 8.708   1.00 16.05 ?  40  ASN   B HB3  1 
ATOM   4241 H  HD21 . ASN   B 1 40  ? 49.244 -21.662 9.007   1.00 17.45 ?  40  ASN   B HD21 1 
ATOM   4242 H  HD22 . ASN   B 1 40  ? 48.143 -22.664 8.963   1.00 17.45 ?  40  ASN   B HD22 1 
ATOM   4243 N  N    . VAL   B 1 41  ? 44.374 -18.842 9.761   1.00 12.08 ?  41  VAL   B N    1 
ATOM   4244 C  CA   . VAL   B 1 41  ? 43.918 -17.523 10.206  1.00 12.98 ?  41  VAL   B CA   1 
ATOM   4245 C  C    . VAL   B 1 41  ? 45.075 -16.577 10.505  1.00 12.77 ?  41  VAL   B C    1 
ATOM   4246 O  O    . VAL   B 1 41  ? 44.901 -15.355 10.437  1.00 12.99 ?  41  VAL   B O    1 
ATOM   4247 C  CB   . VAL   B 1 41  ? 42.937 -17.602 11.393  1.00 14.45 ?  41  VAL   B CB   1 
ATOM   4248 C  CG1  . VAL   B 1 41  ? 41.640 -18.290 10.984  1.00 14.70 ?  41  VAL   B CG1  1 
ATOM   4249 C  CG2  . VAL   B 1 41  ? 43.586 -18.286 12.585  1.00 15.75 ?  41  VAL   B CG2  1 
ATOM   4250 H  H    . VAL   B 1 41  ? 44.192 -19.484 10.292  1.00 14.50 ?  41  VAL   B H    1 
ATOM   4251 H  HA   . VAL   B 1 41  ? 43.423 -17.122 9.474   1.00 15.57 ?  41  VAL   B HA   1 
ATOM   4252 H  HB   . VAL   B 1 41  ? 42.712 -16.699 11.667  1.00 17.34 ?  41  VAL   B HB   1 
ATOM   4253 H  HG11 . VAL   B 1 41  ? 41.030 -18.291 11.739  1.00 17.64 ?  41  VAL   B HG11 1 
ATOM   4254 H  HG12 . VAL   B 1 41  ? 41.245 -17.805 10.242  1.00 17.64 ?  41  VAL   B HG12 1 
ATOM   4255 H  HG13 . VAL   B 1 41  ? 41.837 -19.201 10.716  1.00 17.64 ?  41  VAL   B HG13 1 
ATOM   4256 H  HG21 . VAL   B 1 41  ? 42.949 -18.322 13.313  1.00 18.90 ?  41  VAL   B HG21 1 
ATOM   4257 H  HG22 . VAL   B 1 41  ? 43.847 -19.186 12.330  1.00 18.90 ?  41  VAL   B HG22 1 
ATOM   4258 H  HG23 . VAL   B 1 41  ? 44.368 -17.780 12.854  1.00 18.90 ?  41  VAL   B HG23 1 
ATOM   4259 N  N    . TYR   B 1 42  ? 46.248 -17.095 10.872  1.00 13.35 ?  42  TYR   B N    1 
ATOM   4260 C  CA   . TYR   B 1 42  ? 47.400 -16.242 11.139  1.00 13.86 ?  42  TYR   B CA   1 
ATOM   4261 C  C    . TYR   B 1 42  ? 48.358 -16.166 9.957   1.00 12.96 ?  42  TYR   B C    1 
ATOM   4262 O  O    . TYR   B 1 42  ? 49.447 -15.595 10.091  1.00 14.01 ?  42  TYR   B O    1 
ATOM   4263 C  CB   . TYR   B 1 42  ? 48.107 -16.642 12.440  1.00 15.87 ?  42  TYR   B CB   1 
ATOM   4264 C  CG   . TYR   B 1 42  ? 47.492 -15.975 13.663  1.00 16.37 ?  42  TYR   B CG   1 
ATOM   4265 C  CD1  . TYR   B 1 42  ? 47.700 -14.622 13.912  1.00 15.83 ?  42  TYR   B CD1  1 
ATOM   4266 C  CD2  . TYR   B 1 42  ? 46.700 -16.684 14.552  1.00 18.37 ?  42  TYR   B CD2  1 
ATOM   4267 C  CE1  . TYR   B 1 42  ? 47.142 -13.999 15.015  1.00 16.69 ?  42  TYR   B CE1  1 
ATOM   4268 C  CE2  . TYR   B 1 42  ? 46.135 -16.068 15.658  1.00 18.55 ?  42  TYR   B CE2  1 
ATOM   4269 C  CZ   . TYR   B 1 42  ? 46.357 -14.723 15.884  1.00 18.45 ?  42  TYR   B CZ   1 
ATOM   4270 O  OH   . TYR   B 1 42  ? 45.804 -14.104 16.986  1.00 21.37 ?  42  TYR   B OH   1 
ATOM   4271 H  H    . TYR   B 1 42  ? 46.396 -17.938 10.965  1.00 16.03 ?  42  TYR   B H    1 
ATOM   4272 H  HA   . TYR   B 1 42  ? 47.070 -15.344 11.275  1.00 16.64 ?  42  TYR   B HA   1 
ATOM   4273 H  HB2  . TYR   B 1 42  ? 48.043 -17.601 12.557  1.00 19.05 ?  42  TYR   B HB2  1 
ATOM   4274 H  HB3  . TYR   B 1 42  ? 49.039 -16.374 12.387  1.00 19.05 ?  42  TYR   B HB3  1 
ATOM   4275 H  HD1  . TYR   B 1 42  ? 48.230 -14.126 13.324  1.00 19.00 ?  42  TYR   B HD1  1 
ATOM   4276 H  HD2  . TYR   B 1 42  ? 46.545 -17.590 14.399  1.00 22.04 ?  42  TYR   B HD2  1 
ATOM   4277 H  HE1  . TYR   B 1 42  ? 47.295 -13.094 15.165  1.00 20.03 ?  42  TYR   B HE1  1 
ATOM   4278 H  HE2  . TYR   B 1 42  ? 45.607 -16.559 16.243  1.00 22.26 ?  42  TYR   B HE2  1 
ATOM   4279 H  HH   . TYR   B 1 42  ? 46.025 -13.296 16.994  1.00 25.65 ?  42  TYR   B HH   1 
ATOM   4280 N  N    . LEU   B 1 43  ? 47.951 -16.677 8.797   1.00 12.00 ?  43  LEU   B N    1 
ATOM   4281 C  CA   . LEU   B 1 43  ? 48.762 -16.614 7.589   1.00 11.82 ?  43  LEU   B CA   1 
ATOM   4282 C  C    . LEU   B 1 43  ? 50.175 -17.118 7.854   1.00 12.25 ?  43  LEU   B C    1 
ATOM   4283 O  O    . LEU   B 1 43  ? 51.156 -16.516 7.421   1.00 12.72 ?  43  LEU   B O    1 
ATOM   4284 C  CB   . LEU   B 1 43  ? 48.781 -15.208 6.984   1.00 12.04 ?  43  LEU   B CB   1 
ATOM   4285 C  CG   . LEU   B 1 43  ? 47.424 -14.591 6.624   1.00 12.09 ?  43  LEU   B CG   1 
ATOM   4286 C  CD1  . LEU   B 1 43  ? 47.633 -13.196 6.051   1.00 13.55 ?  43  LEU   B CD1  1 
ATOM   4287 C  CD2  . LEU   B 1 43  ? 46.653 -15.482 5.651   1.00 12.37 ?  43  LEU   B CD2  1 
ATOM   4288 H  H    . LEU   B 1 43  ? 47.202 -17.085 8.686   1.00 14.41 ?  43  LEU   B H    1 
ATOM   4289 H  HA   . LEU   B 1 43  ? 48.366 -17.205 6.926   1.00 14.18 ?  43  LEU   B HA   1 
ATOM   4290 H  HB2  . LEU   B 1 43  ? 49.210 -14.613 7.617   1.00 14.46 ?  43  LEU   B HB2  1 
ATOM   4291 H  HB3  . LEU   B 1 43  ? 49.306 -15.240 6.168   1.00 14.46 ?  43  LEU   B HB3  1 
ATOM   4292 H  HG   . LEU   B 1 43  ? 46.898 -14.504 7.429   1.00 14.51 ?  43  LEU   B HG   1 
ATOM   4293 H  HD11 . LEU   B 1 43  ? 46.770 -12.813 5.826   1.00 16.27 ?  43  LEU   B HD11 1 
ATOM   4294 H  HD12 . LEU   B 1 43  ? 48.075 -12.642 6.716   1.00 16.27 ?  43  LEU   B HD12 1 
ATOM   4295 H  HD13 . LEU   B 1 43  ? 48.185 -13.256 5.254   1.00 16.27 ?  43  LEU   B HD13 1 
ATOM   4296 H  HD21 . LEU   B 1 43  ? 45.851 -15.019 5.364   1.00 14.84 ?  43  LEU   B HD21 1 
ATOM   4297 H  HD22 . LEU   B 1 43  ? 47.215 -15.677 4.883   1.00 14.84 ?  43  LEU   B HD22 1 
ATOM   4298 H  HD23 . LEU   B 1 43  ? 46.414 -16.309 6.101   1.00 14.84 ?  43  LEU   B HD23 1 
ATOM   4299 N  N    . LYS   B 1 44  ? 50.273 -18.240 8.569   1.00 12.11 ?  44  LYS   B N    1 
ATOM   4300 C  CA   . LYS   B 1 44  ? 51.541 -18.918 8.804   1.00 12.78 ?  44  LYS   B CA   1 
ATOM   4301 C  C    . LYS   B 1 44  ? 51.656 -20.030 7.773   1.00 12.22 ?  44  LYS   B C    1 
ATOM   4302 O  O    . LYS   B 1 44  ? 50.956 -21.045 7.855   1.00 13.70 ?  44  LYS   B O    1 
ATOM   4303 C  CB   . LYS   B 1 44  ? 51.600 -19.444 10.236  1.00 14.44 ?  44  LYS   B CB   1 
ATOM   4304 C  CG   . LYS   B 1 44  ? 51.775 -18.336 11.268  1.00 17.26 ?  44  LYS   B CG   1 
ATOM   4305 C  CD   . LYS   B 1 44  ? 52.984 -17.472 10.904  1.00 20.02 ?  44  LYS   B CD   1 
ATOM   4306 C  CE   . LYS   B 1 44  ? 53.452 -16.592 12.035  1.00 22.70 ?  44  LYS   B CE   1 
ATOM   4307 N  NZ   . LYS   B 1 44  ? 54.626 -15.769 11.643  1.00 23.98 ?  44  LYS   B NZ   1 
ATOM   4308 H  H    . LYS   B 1 44  ? 49.602 -18.626 8.941   1.00 14.54 ?  44  LYS   B H    1 
ATOM   4309 H  HA   . LYS   B 1 44  ? 52.272 -18.302 8.647   1.00 15.33 ?  44  LYS   B HA   1 
ATOM   4310 H  HB2  . LYS   B 1 44  ? 50.768 -19.908 10.435  1.00 17.33 ?  44  LYS   B HB2  1 
ATOM   4311 H  HB3  . LYS   B 1 44  ? 52.346 -20.053 10.319  1.00 17.33 ?  44  LYS   B HB3  1 
ATOM   4312 H  HG2  . LYS   B 1 44  ? 50.984 -17.777 11.283  1.00 20.72 ?  44  LYS   B HG2  1 
ATOM   4313 H  HG3  . LYS   B 1 44  ? 51.929 -18.733 12.142  1.00 20.72 ?  44  LYS   B HG3  1 
ATOM   4314 H  HD2  . LYS   B 1 44  ? 53.715 -18.059 10.638  1.00 24.02 ?  44  LYS   B HD2  1 
ATOM   4315 H  HD3  . LYS   B 1 44  ? 52.740 -16.896 10.163  1.00 24.02 ?  44  LYS   B HD3  1 
ATOM   4316 H  HE2  . LYS   B 1 44  ? 52.737 -15.988 12.267  1.00 27.24 ?  44  LYS   B HE2  1 
ATOM   4317 H  HE3  . LYS   B 1 44  ? 53.697 -17.146 12.793  1.00 27.24 ?  44  LYS   B HE3  1 
ATOM   4318 H  HZ1  . LYS   B 1 44  ? 54.879 -15.259 12.326  1.00 28.78 ?  44  LYS   B HZ1  1 
ATOM   4319 H  HZ2  . LYS   B 1 44  ? 55.303 -16.293 11.404  1.00 28.78 ?  44  LYS   B HZ2  1 
ATOM   4320 H  HZ3  . LYS   B 1 44  ? 54.411 -15.243 10.955  1.00 28.78 ?  44  LYS   B HZ3  1 
ATOM   4321 N  N    . HIS   B 1 45  ? 52.500 -19.808 6.770   1.00 11.95 ?  45  HIS   B N    1 
ATOM   4322 C  CA   . HIS   B 1 45  ? 52.509 -20.638 5.569   1.00 12.45 ?  45  HIS   B CA   1 
ATOM   4323 C  C    . HIS   B 1 45  ? 53.520 -21.768 5.725   1.00 14.23 ?  45  HIS   B C    1 
ATOM   4324 O  O    . HIS   B 1 45  ? 54.578 -21.785 5.106   1.00 16.63 ?  45  HIS   B O    1 
ATOM   4325 C  CB   . HIS   B 1 45  ? 52.825 -19.790 4.352   1.00 11.97 ?  45  HIS   B CB   1 
ATOM   4326 C  CG   . HIS   B 1 45  ? 51.956 -18.586 4.242   1.00 11.81 ?  45  HIS   B CG   1 
ATOM   4327 N  ND1  . HIS   B 1 45  ? 50.578 -18.664 4.208   1.00 12.05 ?  45  HIS   B ND1  1 
ATOM   4328 C  CD2  . HIS   B 1 45  ? 52.273 -17.272 4.178   1.00 12.75 ?  45  HIS   B CD2  1 
ATOM   4329 C  CE1  . HIS   B 1 45  ? 50.090 -17.441 4.112   1.00 11.77 ?  45  HIS   B CE1  1 
ATOM   4330 N  NE2  . HIS   B 1 45  ? 51.094 -16.580 4.092   1.00 12.72 ?  45  HIS   B NE2  1 
ATOM   4331 H  H    . HIS   B 1 45  ? 53.073 -19.170 6.754   1.00 14.34 ?  45  HIS   B H    1 
ATOM   4332 H  HA   . HIS   B 1 45  ? 51.628 -21.030 5.441   1.00 14.94 ?  45  HIS   B HA   1 
ATOM   4333 H  HB2  . HIS   B 1 45  ? 53.745 -19.496 4.400   1.00 14.37 ?  45  HIS   B HB2  1 
ATOM   4334 H  HB3  . HIS   B 1 45  ? 52.694 -20.330 3.549   1.00 14.37 ?  45  HIS   B HB3  1 
ATOM   4335 H  HD2  . HIS   B 1 45  ? 53.128 -16.907 4.184   1.00 15.30 ?  45  HIS   B HD2  1 
ATOM   4336 H  HE1  . HIS   B 1 45  ? 49.186 -17.223 4.057   1.00 14.13 ?  45  HIS   B HE1  1 
ATOM   4337 H  HE2  . HIS   B 1 45  ? 51.015 -15.724 4.037   1.00 15.27 ?  45  HIS   B HE2  1 
ATOM   4338 N  N    . GLY   B 1 46  ? 53.161 -22.731 6.565   1.00 15.01 ?  46  GLY   B N    1 
ATOM   4339 C  CA   . GLY   B 1 46  ? 54.089 -23.790 6.912   1.00 16.39 ?  46  GLY   B CA   1 
ATOM   4340 C  C    . GLY   B 1 46  ? 54.131 -24.977 5.969   1.00 18.15 ?  46  GLY   B C    1 
ATOM   4341 O  O    . GLY   B 1 46  ? 55.195 -25.363 5.476   1.00 21.30 ?  46  GLY   B O    1 
ATOM   4342 H  H    . GLY   B 1 46  ? 52.394 -22.780 6.963   1.00 18.02 ?  46  GLY   B H    1 
ATOM   4343 H  HA2  . GLY   B 1 46  ? 54.982 -23.414 6.962   1.00 19.67 ?  46  GLY   B HA2  1 
ATOM   4344 H  HA3  . GLY   B 1 46  ? 53.861 -24.127 7.795   1.00 19.67 ?  46  GLY   B HA3  1 
ATOM   4345 N  N    . GLY   B 1 47  ? 52.975 -25.575 5.705   1.00 17.51 ?  47  GLY   B N    1 
ATOM   4346 C  CA   . GLY   B 1 47  ? 52.915 -26.862 5.044   1.00 15.28 ?  47  GLY   B CA   1 
ATOM   4347 C  C    . GLY   B 1 47  ? 52.003 -26.836 3.833   1.00 13.43 ?  47  GLY   B C    1 
ATOM   4348 O  O    . GLY   B 1 47  ? 51.354 -25.831 3.543   1.00 13.80 ?  47  GLY   B O    1 
ATOM   4349 H  H    . GLY   B 1 47  ? 52.204 -25.255 5.921   1.00 21.01 ?  47  GLY   B H    1 
ATOM   4350 H  HA2  . GLY   B 1 47  ? 53.803 -27.121 4.755   1.00 18.33 ?  47  GLY   B HA2  1 
ATOM   4351 H  HA3  . GLY   B 1 47  ? 52.589 -27.529 5.670   1.00 18.33 ?  47  GLY   B HA3  1 
ATOM   4352 N  N    . GLY   B 1 48  ? 51.963 -27.973 3.143   1.00 12.77 ?  48  GLY   B N    1 
ATOM   4353 C  CA   . GLY   B 1 48  ? 51.038 -28.122 2.039   1.00 12.60 ?  48  GLY   B CA   1 
ATOM   4354 C  C    . GLY   B 1 48  ? 51.173 -27.008 1.023   1.00 12.21 ?  48  GLY   B C    1 
ATOM   4355 O  O    . GLY   B 1 48  ? 52.277 -26.541 0.708   1.00 12.74 ?  48  GLY   B O    1 
ATOM   4356 H  H    . GLY   B 1 48  ? 52.465 -28.652 3.290   1.00 15.32 ?  48  GLY   B H    1 
ATOM   4357 H  HA2  . GLY   B 1 48  ? 51.198 -28.967 1.596   1.00 15.12 ?  48  GLY   B HA2  1 
ATOM   4358 H  HA3  . GLY   B 1 48  ? 50.128 -28.118 2.379   1.00 15.12 ?  48  GLY   B HA3  1 
ATOM   4359 N  N    . VAL   B 1 49  ? 50.025 -26.583 0.492   1.00 11.79 ?  49  VAL   B N    1 
ATOM   4360 C  CA   . VAL   B 1 49  ? 50.005 -25.557 -0.546  1.00 12.03 ?  49  VAL   B CA   1 
ATOM   4361 C  C    . VAL   B 1 49  ? 50.664 -24.270 -0.056  1.00 11.08 ?  49  VAL   B C    1 
ATOM   4362 O  O    . VAL   B 1 49  ? 51.454 -23.648 -0.779  1.00 11.85 ?  49  VAL   B O    1 
ATOM   4363 C  CB   . VAL   B 1 49  ? 48.562 -25.309 -1.026  1.00 13.64 ?  49  VAL   B CB   1 
ATOM   4364 C  CG1  . VAL   B 1 49  ? 48.491 -24.056 -1.885  1.00 13.26 ?  49  VAL   B CG1  1 
ATOM   4365 C  CG2  . VAL   B 1 49  ? 48.033 -26.523 -1.784  1.00 14.70 ?  49  VAL   B CG2  1 
ATOM   4366 H  H    . VAL   B 1 49  ? 49.241 -26.877 0.709   1.00 14.15 ?  49  VAL   B H    1 
ATOM   4367 H  HA   . VAL   B 1 49  ? 50.511 -25.875 -1.310  1.00 14.44 ?  49  VAL   B HA   1 
ATOM   4368 H  HB   . VAL   B 1 49  ? 47.991 -25.171 -0.257  1.00 16.38 ?  49  VAL   B HB   1 
ATOM   4369 H  HG11 . VAL   B 1 49  ? 47.665 -24.071 -2.397  1.00 15.92 ?  49  VAL   B HG11 1 
ATOM   4370 H  HG12 . VAL   B 1 49  ? 48.504 -23.274 -1.310  1.00 15.92 ?  49  VAL   B HG12 1 
ATOM   4371 H  HG13 . VAL   B 1 49  ? 49.249 -24.040 -2.488  1.00 15.92 ?  49  VAL   B HG13 1 
ATOM   4372 H  HG21 . VAL   B 1 49  ? 47.126 -26.346 -2.079  1.00 17.65 ?  49  VAL   B HG21 1 
ATOM   4373 H  HG22 . VAL   B 1 49  ? 48.603 -26.688 -2.556  1.00 17.65 ?  49  VAL   B HG22 1 
ATOM   4374 H  HG23 . VAL   B 1 49  ? 48.047 -27.293 -1.196  1.00 17.65 ?  49  VAL   B HG23 1 
ATOM   4375 N  N    . ALA   B 1 50  ? 50.325 -23.831 1.159   1.00 11.04 ?  50  ALA   B N    1 
ATOM   4376 C  CA   . ALA   B 1 50  ? 50.844 -22.553 1.637   1.00 10.84 ?  50  ALA   B CA   1 
ATOM   4377 C  C    . ALA   B 1 50  ? 52.362 -22.578 1.742   1.00 11.43 ?  50  ALA   B C    1 
ATOM   4378 O  O    . ALA   B 1 50  ? 53.039 -21.607 1.378   1.00 11.37 ?  50  ALA   B O    1 
ATOM   4379 C  CB   . ALA   B 1 50  ? 50.212 -22.190 2.982   1.00 11.50 ?  50  ALA   B CB   1 
ATOM   4380 H  H    . ALA   B 1 50  ? 49.815 -24.248 1.712   1.00 13.25 ?  50  ALA   B H    1 
ATOM   4381 H  HA   . ALA   B 1 50  ? 50.614 -21.864 1.004   1.00 13.01 ?  50  ALA   B HA   1 
ATOM   4382 H  HB1  . ALA   B 1 50  ? 50.569 -21.337 3.280   1.00 13.80 ?  50  ALA   B HB1  1 
ATOM   4383 H  HB2  . ALA   B 1 50  ? 49.250 -22.121 2.868   1.00 13.80 ?  50  ALA   B HB2  1 
ATOM   4384 H  HB3  . ALA   B 1 50  ? 50.420 -22.879 3.631   1.00 13.80 ?  50  ALA   B HB3  1 
ATOM   4385 N  N    . GLY   B 1 51  ? 52.919 -23.671 2.254   1.00 11.80 ?  51  GLY   B N    1 
ATOM   4386 C  CA   . GLY   B 1 51  ? 54.364 -23.765 2.328   1.00 12.37 ?  51  GLY   B CA   1 
ATOM   4387 C  C    . GLY   B 1 51  ? 55.009 -23.717 0.959   1.00 12.22 ?  51  GLY   B C    1 
ATOM   4388 O  O    . GLY   B 1 51  ? 56.048 -23.079 0.773   1.00 12.99 ?  51  GLY   B O    1 
ATOM   4389 H  H    . GLY   B 1 51  ? 52.497 -24.360 2.552   1.00 14.16 ?  51  GLY   B H    1 
ATOM   4390 H  HA2  . GLY   B 1 51  ? 54.714 -23.029 2.856   1.00 14.84 ?  51  GLY   B HA2  1 
ATOM   4391 H  HA3  . GLY   B 1 51  ? 54.620 -24.598 2.759   1.00 14.84 ?  51  GLY   B HA3  1 
ATOM   4392 N  N    . ALA   B 1 52  ? 54.399 -24.379 -0.022  1.00 12.01 ?  52  ALA   B N    1 
ATOM   4393 C  CA   . ALA   B 1 52  ? 54.955 -24.387 -1.367  1.00 12.17 ?  52  ALA   B CA   1 
ATOM   4394 C  C    . ALA   B 1 52  ? 54.871 -23.011 -2.013  1.00 11.70 ?  52  ALA   B C    1 
ATOM   4395 O  O    . ALA   B 1 52  ? 55.837 -22.558 -2.644  1.00 12.51 ?  52  ALA   B O    1 
ATOM   4396 C  CB   . ALA   B 1 52  ? 54.240 -25.429 -2.222  1.00 12.98 ?  52  ALA   B CB   1 
ATOM   4397 H  H    . ALA   B 1 52  ? 53.666 -24.820 0.067   1.00 14.42 ?  52  ALA   B H    1 
ATOM   4398 H  HA   . ALA   B 1 52  ? 55.890 -24.634 -1.316  1.00 14.61 ?  52  ALA   B HA   1 
ATOM   4399 H  HB1  . ALA   B 1 52  ? 54.625 -25.420 -3.113  1.00 15.58 ?  52  ALA   B HB1  1 
ATOM   4400 H  HB2  . ALA   B 1 52  ? 54.362 -26.303 -1.818  1.00 15.58 ?  52  ALA   B HB2  1 
ATOM   4401 H  HB3  . ALA   B 1 52  ? 53.298 -25.211 -2.265  1.00 15.58 ?  52  ALA   B HB3  1 
ATOM   4402 N  N    . LEU   B 1 53  ? 53.724 -22.337 -1.893  1.00 11.08 ?  53  LEU   B N    1 
ATOM   4403 C  CA   . LEU   B 1 53  ? 53.610 -21.001 -2.467  1.00 11.45 ?  53  LEU   B CA   1 
ATOM   4404 C  C    . LEU   B 1 53  ? 54.618 -20.060 -1.824  1.00 11.52 ?  53  LEU   B C    1 
ATOM   4405 O  O    . LEU   B 1 53  ? 55.322 -19.314 -2.513  1.00 12.55 ?  53  LEU   B O    1 
ATOM   4406 C  CB   . LEU   B 1 53  ? 52.186 -20.463 -2.292  1.00 12.21 ?  53  LEU   B CB   1 
ATOM   4407 C  CG   . LEU   B 1 53  ? 51.065 -21.196 -3.025  1.00 12.74 ?  53  LEU   B CG   1 
ATOM   4408 C  CD1  . LEU   B 1 53  ? 49.722 -20.574 -2.696  1.00 14.06 ?  53  LEU   B CD1  1 
ATOM   4409 C  CD2  . LEU   B 1 53  ? 51.289 -21.194 -4.525  1.00 14.66 ?  53  LEU   B CD2  1 
ATOM   4410 H  H    . LEU   B 1 53  ? 53.020 -22.624 -1.490  1.00 13.30 ?  53  LEU   B H    1 
ATOM   4411 H  HA   . LEU   B 1 53  ? 53.806 -21.047 -3.418  1.00 13.74 ?  53  LEU   B HA   1 
ATOM   4412 H  HB2  . LEU   B 1 53  ? 51.971 -20.488 -1.350  1.00 14.66 ?  53  LEU   B HB2  1 
ATOM   4413 H  HB3  . LEU   B 1 53  ? 52.172 -19.547 -2.604  1.00 14.66 ?  53  LEU   B HB3  1 
ATOM   4414 H  HG   . LEU   B 1 53  ? 51.040 -22.119 -2.727  1.00 15.30 ?  53  LEU   B HG   1 
ATOM   4415 H  HD11 . LEU   B 1 53  ? 49.023 -21.056 -3.167  1.00 16.88 ?  53  LEU   B HD11 1 
ATOM   4416 H  HD12 . LEU   B 1 53  ? 49.572 -20.633 -1.737  1.00 16.88 ?  53  LEU   B HD12 1 
ATOM   4417 H  HD13 . LEU   B 1 53  ? 49.727 -19.645 -2.972  1.00 16.88 ?  53  LEU   B HD13 1 
ATOM   4418 H  HD21 . LEU   B 1 53  ? 50.527 -21.605 -4.963  1.00 17.60 ?  53  LEU   B HD21 1 
ATOM   4419 H  HD22 . LEU   B 1 53  ? 51.389 -20.278 -4.829  1.00 17.60 ?  53  LEU   B HD22 1 
ATOM   4420 H  HD23 . LEU   B 1 53  ? 52.094 -21.698 -4.725  1.00 17.60 ?  53  LEU   B HD23 1 
ATOM   4421 N  N    . ASN   B 1 54  ? 54.709 -20.090 -0.498  1.00 11.29 ?  54  ASN   B N    1 
ATOM   4422 C  CA   . ASN   B 1 54  ? 55.624 -19.179 0.173   1.00 12.14 ?  54  ASN   B CA   1 
ATOM   4423 C  C    . ASN   B 1 54  ? 57.066 -19.454 -0.222  1.00 12.42 ?  54  ASN   B C    1 
ATOM   4424 O  O    . ASN   B 1 54  ? 57.841 -18.517 -0.449  1.00 12.61 ?  54  ASN   B O    1 
ATOM   4425 C  CB   . ASN   B 1 54  ? 55.462 -19.256 1.681   1.00 12.69 ?  54  ASN   B CB   1 
ATOM   4426 C  CG   . ASN   B 1 54  ? 56.447 -18.352 2.396   1.00 12.76 ?  54  ASN   B CG   1 
ATOM   4427 O  OD1  . ASN   B 1 54  ? 56.467 -17.142 2.160   1.00 12.87 ?  54  ASN   B OD1  1 
ATOM   4428 N  ND2  . ASN   B 1 54  ? 57.295 -18.934 3.240   1.00 14.17 ?  54  ASN   B ND2  1 
ATOM   4429 H  H    . ASN   B 1 54  ? 54.262 -20.609 0.023   1.00 13.55 ?  54  ASN   B H    1 
ATOM   4430 H  HA   . ASN   B 1 54  ? 55.412 -18.270 -0.101  1.00 14.57 ?  54  ASN   B HA   1 
ATOM   4431 H  HB2  . ASN   B 1 54  ? 54.563 -18.970 1.919   1.00 15.23 ?  54  ASN   B HB2  1 
ATOM   4432 H  HB3  . ASN   B 1 54  ? 55.615 -20.163 1.973   1.00 15.23 ?  54  ASN   B HB3  1 
ATOM   4433 H  HD21 . ASN   B 1 54  ? 57.875 -18.459 3.663   1.00 17.00 ?  54  ASN   B HD21 1 
ATOM   4434 H  HD22 . ASN   B 1 54  ? 57.260 -19.783 3.369   1.00 17.00 ?  54  ASN   B HD22 1 
ATOM   4435 N  N    . LYS   B 1 55  ? 57.450 -20.730 -0.291  1.00 12.93 ?  55  LYS   B N    1 
ATOM   4436 C  CA   . LYS   B 1 55  ? 58.803 -21.073 -0.713  1.00 13.92 ?  55  LYS   B CA   1 
ATOM   4437 C  C    . LYS   B 1 55  ? 59.096 -20.532 -2.106  1.00 13.35 ?  55  LYS   B C    1 
ATOM   4438 O  O    . LYS   B 1 55  ? 60.198 -20.033 -2.364  1.00 13.99 ?  55  LYS   B O    1 
ATOM   4439 C  CB   . LYS   B 1 55  ? 58.996 -22.590 -0.659  1.00 15.02 ?  55  LYS   B CB   1 
ATOM   4440 C  CG   . LYS   B 1 55  ? 60.390 -23.045 -1.052  1.00 18.94 ?  55  LYS   B CG   1 
ATOM   4441 C  CD   . LYS   B 1 55  ? 60.555 -24.544 -0.897  1.00 22.31 ?  55  LYS   B CD   1 
ATOM   4442 C  CE   . LYS   B 1 55  ? 60.515 -24.968 0.569   1.00 24.88 ?  55  LYS   B CE   1 
ATOM   4443 N  NZ   . LYS   B 1 55  ? 60.911 -26.384 0.754   1.00 26.30 ?  55  LYS   B NZ   1 
ATOM   4444 H  H    . LYS   B 1 55  ? 56.948 -21.400 -0.104  1.00 15.52 ?  55  LYS   B H    1 
ATOM   4445 H  HA   . LYS   B 1 55  ? 59.435 -20.669 -0.102  1.00 16.70 ?  55  LYS   B HA   1 
ATOM   4446 H  HB2  . LYS   B 1 55  ? 58.830 -22.887 0.248   1.00 18.03 ?  55  LYS   B HB2  1 
ATOM   4447 H  HB3  . LYS   B 1 55  ? 58.368 -23.009 -1.265  1.00 18.03 ?  55  LYS   B HB3  1 
ATOM   4448 H  HG2  . LYS   B 1 55  ? 60.553 -22.819 -1.981  1.00 22.73 ?  55  LYS   B HG2  1 
ATOM   4449 H  HG3  . LYS   B 1 55  ? 61.043 -22.606 -0.482  1.00 22.73 ?  55  LYS   B HG3  1 
ATOM   4450 H  HD2  . LYS   B 1 55  ? 59.834 -25.000 -1.361  1.00 26.78 ?  55  LYS   B HD2  1 
ATOM   4451 H  HD3  . LYS   B 1 55  ? 61.413 -24.816 -1.264  1.00 26.78 ?  55  LYS   B HD3  1 
ATOM   4452 H  HE2  . LYS   B 1 55  ? 61.128 -24.406 1.074   1.00 29.86 ?  55  LYS   B HE2  1 
ATOM   4453 H  HE3  . LYS   B 1 55  ? 59.611 -24.855 0.905   1.00 29.86 ?  55  LYS   B HE3  1 
ATOM   4454 H  HZ1  . LYS   B 1 55  ? 60.841 -26.606 1.613   1.00 31.56 ?  55  LYS   B HZ1  1 
ATOM   4455 H  HZ2  . LYS   B 1 55  ? 60.377 -26.909 0.274   1.00 31.56 ?  55  LYS   B HZ2  1 
ATOM   4456 H  HZ3  . LYS   B 1 55  ? 61.750 -26.500 0.489   1.00 31.56 ?  55  LYS   B HZ3  1 
ATOM   4457 N  N    . ALA   B 1 56  ? 58.123 -20.610 -3.018  1.00 13.13 ?  56  ALA   B N    1 
ATOM   4458 C  CA   . ALA   B 1 56  ? 58.340 -20.105 -4.368  1.00 13.64 ?  56  ALA   B CA   1 
ATOM   4459 C  C    . ALA   B 1 56  ? 58.616 -18.609 -4.365  1.00 13.52 ?  56  ALA   B C    1 
ATOM   4460 O  O    . ALA   B 1 56  ? 59.343 -18.109 -5.234  1.00 14.77 ?  56  ALA   B O    1 
ATOM   4461 C  CB   . ALA   B 1 56  ? 57.141 -20.431 -5.260  1.00 14.47 ?  56  ALA   B CB   1 
ATOM   4462 H  H    . ALA   B 1 56  ? 57.338 -20.941 -2.881  1.00 15.76 ?  56  ALA   B H    1 
ATOM   4463 H  HA   . ALA   B 1 56  ? 59.116 -20.541 -4.745  1.00 16.37 ?  56  ALA   B HA   1 
ATOM   4464 H  HB1  . ALA   B 1 56  ? 57.313 -20.094 -6.157  1.00 17.37 ?  56  ALA   B HB1  1 
ATOM   4465 H  HB2  . ALA   B 1 56  ? 57.025 -21.393 -5.290  1.00 17.37 ?  56  ALA   B HB2  1 
ATOM   4466 H  HB3  . ALA   B 1 56  ? 56.348 -20.011 -4.897  1.00 17.37 ?  56  ALA   B HB3  1 
ATOM   4467 N  N    . THR   B 1 57  ? 58.049 -17.878 -3.402  1.00 13.28 ?  57  THR   B N    1 
ATOM   4468 C  CA   . THR   B 1 57  ? 58.290 -16.446 -3.266  1.00 13.29 ?  57  THR   B CA   1 
ATOM   4469 C  C    . THR   B 1 57  ? 59.538 -16.130 -2.455  1.00 14.45 ?  57  THR   B C    1 
ATOM   4470 O  O    . THR   B 1 57  ? 59.776 -14.956 -2.145  1.00 14.67 ?  57  THR   B O    1 
ATOM   4471 C  CB   . THR   B 1 57  ? 57.093 -15.725 -2.620  1.00 12.45 ?  57  THR   B CB   1 
ATOM   4472 O  OG1  . THR   B 1 57  ? 57.085 -15.943 -1.203  1.00 12.77 ?  57  THR   B OG1  1 
ATOM   4473 C  CG2  . THR   B 1 57  ? 55.774 -16.148 -3.244  1.00 12.37 ?  57  THR   B CG2  1 
ATOM   4474 H  H    . THR   B 1 57  ? 57.507 -18.193 -2.811  1.00 15.94 ?  57  THR   B H    1 
ATOM   4475 H  HA   . THR   B 1 57  ? 58.409 -16.068 -4.153  1.00 15.95 ?  57  THR   B HA   1 
ATOM   4476 H  HB   . THR   B 1 57  ? 57.191 -14.773 -2.781  1.00 14.94 ?  57  THR   B HB   1 
ATOM   4477 H  HG1  . THR   B 1 57  ? 57.024 -16.766 -1.040  1.00 15.32 ?  57  THR   B HG1  1 
ATOM   4478 H  HG21 . THR   B 1 57  ? 55.053 -15.594 -2.911  1.00 14.84 ?  57  THR   B HG21 1 
ATOM   4479 H  HG22 . THR   B 1 57  ? 55.819 -16.060 -4.211  1.00 14.84 ?  57  THR   B HG22 1 
ATOM   4480 H  HG23 . THR   B 1 57  ? 55.584 -17.074 -3.026  1.00 14.84 ?  57  THR   B HG23 1 
ATOM   4481 N  N    . ASN   B 1 58  ? 60.332 -17.137 -2.099  1.00 15.09 ?  58  ASN   B N    1 
ATOM   4482 C  CA   . ASN   B 1 58  ? 61.535 -16.923 -1.299  1.00 17.60 ?  58  ASN   B CA   1 
ATOM   4483 C  C    . ASN   B 1 58  ? 61.201 -16.214 0.014   1.00 15.62 ?  58  ASN   B C    1 
ATOM   4484 O  O    . ASN   B 1 58  ? 61.932 -15.334 0.478   1.00 16.09 ?  58  ASN   B O    1 
ATOM   4485 C  CB   . ASN   B 1 58  ? 62.612 -16.172 -2.089  1.00 23.88 ?  58  ASN   B CB   1 
ATOM   4486 C  CG   . ASN   B 1 58  ? 63.981 -16.271 -1.447  1.00 31.13 ?  58  ASN   B CG   1 
ATOM   4487 O  OD1  . ASN   B 1 58  ? 64.283 -17.238 -0.748  1.00 35.40 ?  58  ASN   B OD1  1 
ATOM   4488 N  ND2  . ASN   B 1 58  ? 64.818 -15.266 -1.680  1.00 35.73 ?  58  ASN   B ND2  1 
ATOM   4489 H  H    . ASN   B 1 58  ? 60.191 -17.964 -2.302  1.00 18.11 ?  58  ASN   B H    1 
ATOM   4490 H  HA   . ASN   B 1 58  ? 61.904 -17.794 -1.076  1.00 21.12 ?  58  ASN   B HA   1 
ATOM   4491 H  HB2  . ASN   B 1 58  ? 62.671 -16.549 -2.984  1.00 28.66 ?  58  ASN   B HB2  1 
ATOM   4492 H  HB3  . ASN   B 1 58  ? 62.373 -15.236 -2.140  1.00 28.66 ?  58  ASN   B HB3  1 
ATOM   4493 H  HD21 . ASN   B 1 58  ? 65.608 -15.275 -1.340  1.00 42.88 ?  58  ASN   B HD21 1 
ATOM   4494 H  HD22 . ASN   B 1 58  ? 64.571 -14.606 -2.173  1.00 42.88 ?  58  ASN   B HD22 1 
ATOM   4495 N  N    . ASN   B 1 59  ? 60.078 -16.599 0.615   1.00 14.40 ?  59  ASN   B N    1 
ATOM   4496 C  CA   . ASN   B 1 59  ? 59.604 -16.127 1.915   1.00 14.34 ?  59  ASN   B CA   1 
ATOM   4497 C  C    . ASN   B 1 59  ? 59.013 -14.719 1.862   1.00 13.95 ?  59  ASN   B C    1 
ATOM   4498 O  O    . ASN   B 1 59  ? 58.588 -14.213 2.908   1.00 14.13 ?  59  ASN   B O    1 
ATOM   4499 C  CB   . ASN   B 1 59  ? 60.680 -16.188 3.015   1.00 15.67 ?  59  ASN   B CB   1 
ATOM   4500 C  CG   . ASN   B 1 59  ? 60.096 -16.376 4.396   1.00 16.72 ?  59  ASN   B CG   1 
ATOM   4501 O  OD1  . ASN   B 1 59  ? 59.266 -17.258 4.612   1.00 17.00 ?  59  ASN   B OD1  1 
ATOM   4502 N  ND2  . ASN   B 1 59  ? 60.519 -15.545 5.342   1.00 17.52 ?  59  ASN   B ND2  1 
ATOM   4503 H  H    . ASN   B 1 59  ? 59.541 -17.173 0.264   1.00 17.29 ?  59  ASN   B H    1 
ATOM   4504 H  HA   . ASN   B 1 59  ? 58.894 -16.723 2.195   1.00 17.21 ?  59  ASN   B HA   1 
ATOM   4505 H  HB2  . ASN   B 1 59  ? 61.272 -16.938 2.846   1.00 18.81 ?  59  ASN   B HB2  1 
ATOM   4506 H  HB3  . ASN   B 1 59  ? 61.180 -15.361 3.021   1.00 18.81 ?  59  ASN   B HB3  1 
ATOM   4507 H  HD21 . ASN   B 1 59  ? 60.213 -15.612 6.145   1.00 21.03 ?  59  ASN   B HD21 1 
ATOM   4508 H  HD22 . ASN   B 1 59  ? 61.098 -14.943 5.152   1.00 21.03 ?  59  ASN   B HD22 1 
ATOM   4509 N  N    . ALA   B 1 60  ? 58.953 -14.072 0.695   1.00 13.64 ?  60  ALA   B N    1 
ATOM   4510 C  CA   . ALA   B 1 60  ? 58.363 -12.740 0.631   1.00 13.70 ?  60  ALA   B CA   1 
ATOM   4511 C  C    . ALA   B 1 60  ? 56.894 -12.766 1.033   1.00 13.02 ?  60  ALA   B C    1 
ATOM   4512 O  O    . ALA   B 1 60  ? 56.391 -11.815 1.647   1.00 13.36 ?  60  ALA   B O    1 
ATOM   4513 C  CB   . ALA   B 1 60  ? 58.525 -12.154 -0.772  1.00 14.28 ?  60  ALA   B CB   1 
ATOM   4514 H  H    . ALA   B 1 60  ? 59.245 -14.378 -0.052  1.00 16.38 ?  60  ALA   B H    1 
ATOM   4515 H  HA   . ALA   B 1 60  ? 58.825 -12.160 1.253   1.00 16.45 ?  60  ALA   B HA   1 
ATOM   4516 H  HB1  . ALA   B 1 60  ? 58.128 -11.270 -0.793  1.00 17.14 ?  60  ALA   B HB1  1 
ATOM   4517 H  HB2  . ALA   B 1 60  ? 59.473 -12.095 -0.980  1.00 17.14 ?  60  ALA   B HB2  1 
ATOM   4518 H  HB3  . ALA   B 1 60  ? 58.083 -12.733 -1.411  1.00 17.14 ?  60  ALA   B HB3  1 
ATOM   4519 N  N    . MET   B 1 61  ? 56.185 -13.838 0.681   1.00 12.38 ?  61  MET   B N    1 
ATOM   4520 C  CA   . MET   B 1 61  ? 54.790 -13.960 1.077   1.00 12.03 ?  61  MET   B CA   1 
ATOM   4521 C  C    . MET   B 1 61  ? 54.657 -13.976 2.598   1.00 12.63 ?  61  MET   B C    1 
ATOM   4522 O  O    . MET   B 1 61  ? 53.756 -13.336 3.155   1.00 12.19 ?  61  MET   B O    1 
ATOM   4523 C  CB   . MET   B 1 61  ? 54.211 -15.224 0.447   1.00 12.10 ?  61  MET   B CB   1 
ATOM   4524 C  CG   . MET   B 1 61  ? 52.773 -15.514 0.863   1.00 11.97 ?  61  MET   B CG   1 
ATOM   4525 S  SD   . MET   B 1 61  ? 52.128 -17.021 0.101   1.00 12.34 ?  61  MET   B SD   1 
ATOM   4526 C  CE   . MET   B 1 61  ? 51.880 -16.429 -1.568  1.00 13.58 ?  61  MET   B CE   1 
ATOM   4527 H  H    . MET   B 1 61  ? 56.484 -14.502 0.218   1.00 14.86 ?  61  MET   B H    1 
ATOM   4528 H  HA   . MET   B 1 61  ? 54.293 -13.204 0.721   1.00 14.44 ?  61  MET   B HA   1 
ATOM   4529 H  HB2  . MET   B 1 61  ? 54.225 -15.131 -0.521  1.00 14.52 ?  61  MET   B HB2  1 
ATOM   4530 H  HB3  . MET   B 1 61  ? 54.754 -15.984 0.709   1.00 14.52 ?  61  MET   B HB3  1 
ATOM   4531 H  HG2  . MET   B 1 61  ? 52.731 -15.629 1.826   1.00 14.37 ?  61  MET   B HG2  1 
ATOM   4532 H  HG3  . MET   B 1 61  ? 52.206 -14.773 0.593   1.00 14.37 ?  61  MET   B HG3  1 
ATOM   4533 H  HE1  . MET   B 1 61  ? 51.487 -17.137 -2.099  1.00 16.29 ?  61  MET   B HE1  1 
ATOM   4534 H  HE2  . MET   B 1 61  ? 51.290 -15.660 -1.548  1.00 16.29 ?  61  MET   B HE2  1 
ATOM   4535 H  HE3  . MET   B 1 61  ? 52.741 -16.175 -1.941  1.00 16.29 ?  61  MET   B HE3  1 
ATOM   4536 N  N    . GLN   B 1 62  ? 55.544 -14.692 3.293   1.00 12.12 ?  62  GLN   B N    1 
ATOM   4537 C  CA   . GLN   B 1 62  ? 55.441 -14.756 4.747   1.00 12.44 ?  62  GLN   B CA   1 
ATOM   4538 C  C    . GLN   B 1 62  ? 55.725 -13.403 5.386   1.00 12.47 ?  62  GLN   B C    1 
ATOM   4539 O  O    . GLN   B 1 62  ? 55.043 -13.003 6.335   1.00 13.05 ?  62  GLN   B O    1 
ATOM   4540 C  CB   . GLN   B 1 62  ? 56.391 -15.813 5.301   1.00 12.54 ?  62  GLN   B CB   1 
ATOM   4541 C  CG   . GLN   B 1 62  ? 56.177 -16.082 6.780   1.00 12.83 ?  62  GLN   B CG   1 
ATOM   4542 C  CD   . GLN   B 1 62  ? 54.810 -16.675 7.031   1.00 12.63 ?  62  GLN   B CD   1 
ATOM   4543 O  OE1  . GLN   B 1 62  ? 54.552 -17.819 6.663   1.00 12.91 ?  62  GLN   B OE1  1 
ATOM   4544 N  NE2  . GLN   B 1 62  ? 53.908 -15.889 7.616   1.00 13.08 ?  62  GLN   B NE2  1 
ATOM   4545 H  H    . GLN   B 1 62  ? 56.191 -15.143 2.948   1.00 14.55 ?  62  GLN   B H    1 
ATOM   4546 H  HA   . GLN   B 1 62  ? 54.536 -15.016 4.981   1.00 14.92 ?  62  GLN   B HA   1 
ATOM   4547 H  HB2  . GLN   B 1 62  ? 56.261 -16.646 4.820   1.00 15.05 ?  62  GLN   B HB2  1 
ATOM   4548 H  HB3  . GLN   B 1 62  ? 57.308 -15.507 5.182   1.00 15.05 ?  62  GLN   B HB3  1 
ATOM   4549 H  HG2  . GLN   B 1 62  ? 56.842 -16.719 7.087   1.00 15.40 ?  62  GLN   B HG2  1 
ATOM   4550 H  HG3  . GLN   B 1 62  ? 56.250 -15.254 7.274   1.00 15.40 ?  62  GLN   B HG3  1 
ATOM   4551 H  HE21 . GLN   B 1 62  ? 54.120 -15.090 7.853   1.00 15.70 ?  62  GLN   B HE21 1 
ATOM   4552 H  HE22 . GLN   B 1 62  ? 53.115 -16.187 7.772   1.00 15.70 ?  62  GLN   B HE22 1 
ATOM   4553 N  N    . VAL   B 1 63  ? 56.741 -12.693 4.896   1.00 13.16 ?  63  VAL   B N    1 
ATOM   4554 C  CA   . VAL   B 1 63  ? 57.054 -11.379 5.451   1.00 13.88 ?  63  VAL   B CA   1 
ATOM   4555 C  C    . VAL   B 1 63  ? 55.867 -10.439 5.274   1.00 13.25 ?  63  VAL   B C    1 
ATOM   4556 O  O    . VAL   B 1 63  ? 55.457 -9.738  6.208   1.00 14.03 ?  63  VAL   B O    1 
ATOM   4557 C  CB   . VAL   B 1 63  ? 58.340 -10.825 4.820   1.00 15.54 ?  63  VAL   B CB   1 
ATOM   4558 C  CG1  . VAL   B 1 63  ? 58.571 -9.385  5.268   1.00 16.02 ?  63  VAL   B CG1  1 
ATOM   4559 C  CG2  . VAL   B 1 63  ? 59.522 -11.704 5.203   1.00 16.13 ?  63  VAL   B CG2  1 
ATOM   4560 H  H    . VAL   B 1 63  ? 57.250 -12.947 4.248   1.00 15.80 ?  63  VAL   B H    1 
ATOM   4561 H  HA   . VAL   B 1 63  ? 57.213 -11.481 6.400   1.00 16.66 ?  63  VAL   B HA   1 
ATOM   4562 H  HB   . VAL   B 1 63  ? 58.261 -10.835 3.855   1.00 18.65 ?  63  VAL   B HB   1 
ATOM   4563 H  HG11 . VAL   B 1 63  ? 59.488 -9.137  5.079   1.00 19.23 ?  63  VAL   B HG11 1 
ATOM   4564 H  HG12 . VAL   B 1 63  ? 57.963 -8.803  4.789   1.00 19.23 ?  63  VAL   B HG12 1 
ATOM   4565 H  HG13 . VAL   B 1 63  ? 58.404 -9.324  6.225   1.00 19.23 ?  63  VAL   B HG13 1 
ATOM   4566 H  HG21 . VAL   B 1 63  ? 60.334 -11.329 4.824   1.00 19.36 ?  63  VAL   B HG21 1 
ATOM   4567 H  HG22 . VAL   B 1 63  ? 59.596 -11.730 6.173   1.00 19.36 ?  63  VAL   B HG22 1 
ATOM   4568 H  HG23 . VAL   B 1 63  ? 59.380 -12.599 4.861   1.00 19.36 ?  63  VAL   B HG23 1 
ATOM   4569 N  N    . GLU   B 1 64  ? 55.290 -10.424 4.071   1.00 12.88 ?  64  GLU   B N    1 
ATOM   4570 C  CA   . GLU   B 1 64  ? 54.121 -9.590  3.805   1.00 12.48 ?  64  GLU   B CA   1 
ATOM   4571 C  C    . GLU   B 1 64  ? 52.947 -9.995  4.687   1.00 12.10 ?  64  GLU   B C    1 
ATOM   4572 O  O    . GLU   B 1 64  ? 52.205 -9.135  5.194   1.00 12.98 ?  64  GLU   B O    1 
ATOM   4573 C  CB   . GLU   B 1 64  ? 53.749 -9.735  2.330   1.00 12.94 ?  64  GLU   B CB   1 
ATOM   4574 C  CG   . GLU   B 1 64  ? 52.481 -9.006  1.909   1.00 12.88 ?  64  GLU   B CG   1 
ATOM   4575 C  CD   . GLU   B 1 64  ? 51.932 -9.507  0.579   1.00 13.50 ?  64  GLU   B CD   1 
ATOM   4576 O  OE1  . GLU   B 1 64  ? 52.112 -10.712 0.257   1.00 14.31 ?  64  GLU   B OE1  1 
ATOM   4577 O  OE2  . GLU   B 1 64  ? 51.306 -8.693  -0.142  1.00 14.21 -1 64  GLU   B OE2  1 
ATOM   4578 H  H    . GLU   B 1 64  ? 55.567 -10.879 3.389   1.00 15.46 ?  64  GLU   B H    1 
ATOM   4579 H  HA   . GLU   B 1 64  ? 54.339 -8.662  3.980   1.00 14.97 ?  64  GLU   B HA   1 
ATOM   4580 H  HB2  . GLU   B 1 64  ? 54.474 -9.376  1.788   1.00 15.53 ?  64  GLU   B HB2  1 
ATOM   4581 H  HB3  . GLU   B 1 64  ? 53.629 -10.672 2.130   1.00 15.53 ?  64  GLU   B HB3  1 
ATOM   4582 H  HG2  . GLU   B 1 64  ? 51.789 -9.136  2.581   1.00 15.46 ?  64  GLU   B HG2  1 
ATOM   4583 H  HG3  . GLU   B 1 64  ? 52.672 -8.060  1.817   1.00 15.46 ?  64  GLU   B HG3  1 
ATOM   4584 N  N    . SER   B 1 65  ? 52.761 -11.305 4.870   1.00 11.90 ?  65  SER   B N    1 
ATOM   4585 C  CA   . SER   B 1 65  ? 51.653 -11.807 5.670   1.00 12.18 ?  65  SER   B CA   1 
ATOM   4586 C  C    . SER   B 1 65  ? 51.791 -11.412 7.134   1.00 12.35 ?  65  SER   B C    1 
ATOM   4587 O  O    . SER   B 1 65  ? 50.796 -11.046 7.777   1.00 12.51 ?  65  SER   B O    1 
ATOM   4588 C  CB   . SER   B 1 65  ? 51.566 -13.326 5.538   1.00 12.33 ?  65  SER   B CB   1 
ATOM   4589 O  OG   . SER   B 1 65  ? 51.220 -13.720 4.219   1.00 12.34 ?  65  SER   B OG   1 
ATOM   4590 H  H    . SER   B 1 65  ? 53.268 -11.923 4.543   1.00 14.28 ?  65  SER   B H    1 
ATOM   4591 H  HA   . SER   B 1 65  ? 50.825 -11.430 5.336   1.00 14.62 ?  65  SER   B HA   1 
ATOM   4592 H  HB2  . SER   B 1 65  ? 52.426 -13.712 5.761   1.00 14.80 ?  65  SER   B HB2  1 
ATOM   4593 H  HB3  . SER   B 1 65  ? 50.888 -13.655 6.149   1.00 14.80 ?  65  SER   B HB3  1 
ATOM   4594 H  HG   . SER   B 1 65  ? 51.799 -13.437 3.673   1.00 14.81 ?  65  SER   B HG   1 
ATOM   4595 N  N    . ASP   B 1 66  ? 53.002 -11.511 7.692   1.00 13.02 ?  66  ASP   B N    1 
ATOM   4596 C  CA   . ASP   B 1 66  ? 53.197 -11.126 9.087   1.00 13.10 ?  66  ASP   B CA   1 
ATOM   4597 C  C    . ASP   B 1 66  ? 52.884 -9.651  9.295   1.00 13.39 ?  66  ASP   B C    1 
ATOM   4598 O  O    . ASP   B 1 66  ? 52.309 -9.264  10.320  1.00 13.51 ?  66  ASP   B O    1 
ATOM   4599 C  CB   . ASP   B 1 66  ? 54.633 -11.429 9.520   1.00 14.46 ?  66  ASP   B CB   1 
ATOM   4600 C  CG   . ASP   B 1 66  ? 54.907 -12.915 9.674   1.00 16.29 ?  66  ASP   B CG   1 
ATOM   4601 O  OD1  . ASP   B 1 66  ? 53.954 -13.723 9.594   1.00 16.74 ?  66  ASP   B OD1  1 
ATOM   4602 O  OD2  . ASP   B 1 66  ? 56.085 -13.286 9.889   1.00 18.92 -1 66  ASP   B OD2  1 
ATOM   4603 H  H    . ASP   B 1 66  ? 53.706 -11.804 7.293   1.00 15.62 ?  66  ASP   B H    1 
ATOM   4604 H  HA   . ASP   B 1 66  ? 52.598 -11.641 9.647   1.00 15.72 ?  66  ASP   B HA   1 
ATOM   4605 H  HB2  . ASP   B 1 66  ? 55.244 -11.078 8.855   1.00 17.35 ?  66  ASP   B HB2  1 
ATOM   4606 H  HB3  . ASP   B 1 66  ? 54.797 -11.004 10.378  1.00 17.35 ?  66  ASP   B HB3  1 
ATOM   4607 N  N    . ASP   B 1 67  ? 53.250 -8.808  8.331   1.00 13.00 ?  67  ASP   B N    1 
ATOM   4608 C  CA   . ASP   B 1 67  ? 52.907 -7.397  8.425   1.00 13.73 ?  67  ASP   B CA   1 
ATOM   4609 C  C    . ASP   B 1 67  ? 51.396 -7.192  8.344   1.00 13.82 ?  67  ASP   B C    1 
ATOM   4610 O  O    . ASP   B 1 67  ? 50.829 -6.397  9.104   1.00 13.93 ?  67  ASP   B O    1 
ATOM   4611 C  CB   . ASP   B 1 67  ? 53.623 -6.628  7.322   1.00 15.23 ?  67  ASP   B CB   1 
ATOM   4612 C  CG   . ASP   B 1 67  ? 53.212 -5.185  7.285   1.00 16.22 ?  67  ASP   B CG   1 
ATOM   4613 O  OD1  . ASP   B 1 67  ? 53.717 -4.391  8.114   1.00 17.13 ?  67  ASP   B OD1  1 
ATOM   4614 O  OD2  . ASP   B 1 67  ? 52.356 -4.861  6.445   1.00 17.37 -1 67  ASP   B OD2  1 
ATOM   4615 H  H    . ASP   B 1 67  ? 53.696 -9.025  7.627   1.00 15.61 ?  67  ASP   B H    1 
ATOM   4616 H  HA   . ASP   B 1 67  ? 53.215 -7.051  9.276   1.00 16.48 ?  67  ASP   B HA   1 
ATOM   4617 H  HB2  . ASP   B 1 67  ? 54.581 -6.663  7.478   1.00 18.28 ?  67  ASP   B HB2  1 
ATOM   4618 H  HB3  . ASP   B 1 67  ? 53.415 -7.035  6.463   1.00 18.28 ?  67  ASP   B HB3  1 
ATOM   4619 N  N    . TYR   B 1 68  ? 50.721 -7.921  7.449   1.00 13.12 ?  68  TYR   B N    1 
ATOM   4620 C  CA   . TYR   B 1 68  ? 49.263 -7.842  7.377   1.00 13.97 ?  68  TYR   B CA   1 
ATOM   4621 C  C    . TYR   B 1 68  ? 48.629 -8.192  8.719   1.00 13.34 ?  68  TYR   B C    1 
ATOM   4622 O  O    . TYR   B 1 68  ? 47.696 -7.517  9.175   1.00 14.00 ?  68  TYR   B O    1 
ATOM   4623 C  CB   . TYR   B 1 68  ? 48.731 -8.772  6.277   1.00 14.60 ?  68  TYR   B CB   1 
ATOM   4624 C  CG   . TYR   B 1 68  ? 47.225 -8.925  6.334   1.00 15.35 ?  68  TYR   B CG   1 
ATOM   4625 C  CD1  . TYR   B 1 68  ? 46.635 -9.881  7.154   1.00 15.92 ?  68  TYR   B CD1  1 
ATOM   4626 C  CD2  . TYR   B 1 68  ? 46.396 -8.086  5.611   1.00 16.23 ?  68  TYR   B CD2  1 
ATOM   4627 C  CE1  . TYR   B 1 68  ? 45.274 -10.006 7.241   1.00 16.93 ?  68  TYR   B CE1  1 
ATOM   4628 C  CE2  . TYR   B 1 68  ? 45.016 -8.211  5.687   1.00 16.94 ?  68  TYR   B CE2  1 
ATOM   4629 C  CZ   . TYR   B 1 68  ? 44.475 -9.170  6.505   1.00 17.04 ?  68  TYR   B CZ   1 
ATOM   4630 O  OH   . TYR   B 1 68  ? 43.110 -9.289  6.599   1.00 18.15 ?  68  TYR   B OH   1 
ATOM   4631 H  H    . TYR   B 1 68  ? 51.081 -8.465  6.885   1.00 15.74 ?  68  TYR   B H    1 
ATOM   4632 H  HA   . TYR   B 1 68  ? 49.012 -6.936  7.155   1.00 16.76 ?  68  TYR   B HA   1 
ATOM   4633 H  HB2  . TYR   B 1 68  ? 48.962 -8.401  5.413   1.00 17.52 ?  68  TYR   B HB2  1 
ATOM   4634 H  HB3  . TYR   B 1 68  ? 49.128 -9.650  6.384   1.00 17.52 ?  68  TYR   B HB3  1 
ATOM   4635 H  HD1  . TYR   B 1 68  ? 47.176 -10.451 7.655   1.00 19.11 ?  68  TYR   B HD1  1 
ATOM   4636 H  HD2  . TYR   B 1 68  ? 46.772 -7.433  5.070   1.00 19.48 ?  68  TYR   B HD2  1 
ATOM   4637 H  HE1  . TYR   B 1 68  ? 44.892 -10.664 7.784   1.00 20.32 ?  68  TYR   B HE1  1 
ATOM   4638 H  HE2  . TYR   B 1 68  ? 44.463 -7.647  5.198   1.00 20.33 ?  68  TYR   B HE2  1 
ATOM   4639 H  HH   . TYR   B 1 68  ? 42.721 -8.735  6.089   1.00 21.78 ?  68  TYR   B HH   1 
ATOM   4640 N  N    . ILE   B 1 69  ? 49.116 -9.256  9.362   1.00 13.45 ?  69  ILE   B N    1 
ATOM   4641 C  CA   . ILE   B 1 69  ? 48.555 -9.683  10.640  1.00 13.82 ?  69  ILE   B CA   1 
ATOM   4642 C  C    . ILE   B 1 69  ? 48.809 -8.639  11.718  1.00 13.59 ?  69  ILE   B C    1 
ATOM   4643 O  O    . ILE   B 1 69  ? 47.936 -8.357  12.546  1.00 14.03 ?  69  ILE   B O    1 
ATOM   4644 C  CB   . ILE   B 1 69  ? 49.127 -11.059 11.030  1.00 15.07 ?  69  ILE   B CB   1 
ATOM   4645 C  CG1  . ILE   B 1 69  ? 48.589 -12.158 10.102  1.00 15.42 ?  69  ILE   B CG1  1 
ATOM   4646 C  CG2  . ILE   B 1 69  ? 48.854 -11.372 12.496  1.00 15.86 ?  69  ILE   B CG2  1 
ATOM   4647 C  CD1  . ILE   B 1 69  ? 47.116 -12.468 10.267  1.00 15.26 ?  69  ILE   B CD1  1 
ATOM   4648 H  H    . ILE   B 1 69  ? 49.770 -9.742  9.085   1.00 16.15 ?  69  ILE   B H    1 
ATOM   4649 H  HA   . ILE   B 1 69  ? 47.597 -9.775  10.546  1.00 16.59 ?  69  ILE   B HA   1 
ATOM   4650 H  HB   . ILE   B 1 69  ? 50.089 -11.023 10.913  1.00 18.08 ?  69  ILE   B HB   1 
ATOM   4651 H  HG12 . ILE   B 1 69  ? 48.729 -11.879 9.183   1.00 18.51 ?  69  ILE   B HG12 1 
ATOM   4652 H  HG13 . ILE   B 1 69  ? 49.083 -12.975 10.272  1.00 18.51 ?  69  ILE   B HG13 1 
ATOM   4653 H  HG21 . ILE   B 1 69  ? 48.992 -12.323 12.642  1.00 19.03 ?  69  ILE   B HG21 1 
ATOM   4654 H  HG22 . ILE   B 1 69  ? 49.471 -10.866 13.050  1.00 19.03 ?  69  ILE   B HG22 1 
ATOM   4655 H  HG23 . ILE   B 1 69  ? 47.941 -11.135 12.707  1.00 19.03 ?  69  ILE   B HG23 1 
ATOM   4656 H  HD11 . ILE   B 1 69  ? 46.877 -13.184 9.658   1.00 18.32 ?  69  ILE   B HD11 1 
ATOM   4657 H  HD12 . ILE   B 1 69  ? 46.950 -12.748 11.182  1.00 18.32 ?  69  ILE   B HD12 1 
ATOM   4658 H  HD13 . ILE   B 1 69  ? 46.597 -11.676 10.064  1.00 18.32 ?  69  ILE   B HD13 1 
ATOM   4659 N  N    . ALA   B 1 70  ? 50.007 -8.055  11.742  1.00 13.84 ?  70  ALA   B N    1 
ATOM   4660 C  CA   . ALA   B 1 70  ? 50.289 -7.019  12.730  1.00 13.52 ?  70  ALA   B CA   1 
ATOM   4661 C  C    . ALA   B 1 70  ? 49.296 -5.870  12.618  1.00 13.61 ?  70  ALA   B C    1 
ATOM   4662 O  O    . ALA   B 1 70  ? 48.858 -5.318  13.632  1.00 14.05 ?  70  ALA   B O    1 
ATOM   4663 C  CB   . ALA   B 1 70  ? 51.721 -6.516  12.556  1.00 14.65 ?  70  ALA   B CB   1 
ATOM   4664 H  H    . ALA   B 1 70  ? 50.653 -8.235  11.211  1.00 16.61 ?  70  ALA   B H    1 
ATOM   4665 H  HA   . ALA   B 1 70  ? 50.214 -7.399  13.622  1.00 16.22 ?  70  ALA   B HA   1 
ATOM   4666 H  HB1  . ALA   B 1 70  ? 51.911 -5.853  13.240  1.00 17.58 ?  70  ALA   B HB1  1 
ATOM   4667 H  HB2  . ALA   B 1 70  ? 52.335 -7.264  12.647  1.00 17.58 ?  70  ALA   B HB2  1 
ATOM   4668 H  HB3  . ALA   B 1 70  ? 51.813 -6.120  11.676  1.00 17.58 ?  70  ALA   B HB3  1 
ATOM   4669 N  N    . THR   B 1 71  ? 48.922 -5.507  11.394  1.00 14.33 ?  71  THR   B N    1 
ATOM   4670 C  CA   . THR   B 1 71  ? 48.028 -4.375  11.187  1.00 15.08 ?  71  THR   B CA   1 
ATOM   4671 C  C    . THR   B 1 71  ? 46.564 -4.746  11.392  1.00 15.87 ?  71  THR   B C    1 
ATOM   4672 O  O    . THR   B 1 71  ? 45.786 -3.931  11.902  1.00 17.55 ?  71  THR   B O    1 
ATOM   4673 C  CB   . THR   B 1 71  ? 48.242 -3.816  9.782   1.00 16.77 ?  71  THR   B CB   1 
ATOM   4674 O  OG1  . THR   B 1 71  ? 49.567 -3.281  9.684   1.00 19.09 ?  71  THR   B OG1  1 
ATOM   4675 C  CG2  . THR   B 1 71  ? 47.216 -2.730  9.452   1.00 17.78 ?  71  THR   B CG2  1 
ATOM   4676 H  H    . THR   B 1 71  ? 49.174 -5.897  10.674  1.00 17.20 ?  71  THR   B H    1 
ATOM   4677 H  HA   . THR   B 1 71  ? 48.251 -3.674  11.821  1.00 18.10 ?  71  THR   B HA   1 
ATOM   4678 H  HB   . THR   B 1 71  ? 48.145 -4.530  9.133   1.00 20.12 ?  71  THR   B HB   1 
ATOM   4679 H  HG1  . THR   B 1 71  ? 49.695 -2.961  8.914   1.00 22.91 ?  71  THR   B HG1  1 
ATOM   4680 H  HG21 . THR   B 1 71  ? 47.517 -2.212  8.688   1.00 21.34 ?  71  THR   B HG21 1 
ATOM   4681 H  HG22 . THR   B 1 71  ? 46.360 -3.132  9.240   1.00 21.34 ?  71  THR   B HG22 1 
ATOM   4682 H  HG23 . THR   B 1 71  ? 47.109 -2.134  10.211  1.00 21.34 ?  71  THR   B HG23 1 
ATOM   4683 N  N    . ASN   B 1 72  ? 46.168 -5.958  10.997  1.00 15.36 ?  72  ASN   B N    1 
ATOM   4684 C  CA   . ASN   B 1 72  ? 44.764 -6.311  10.869  1.00 15.69 ?  72  ASN   B CA   1 
ATOM   4685 C  C    . ASN   B 1 72  ? 44.292 -7.407  11.808  1.00 16.20 ?  72  ASN   B C    1 
ATOM   4686 O  O    . ASN   B 1 72  ? 43.076 -7.560  11.976  1.00 17.32 ?  72  ASN   B O    1 
ATOM   4687 C  CB   . ASN   B 1 72  ? 44.459 -6.735  9.426   1.00 16.79 ?  72  ASN   B CB   1 
ATOM   4688 C  CG   . ASN   B 1 72  ? 44.722 -5.626  8.442   1.00 17.78 ?  72  ASN   B CG   1 
ATOM   4689 O  OD1  . ASN   B 1 72  ? 45.733 -5.626  7.733   1.00 18.74 ?  72  ASN   B OD1  1 
ATOM   4690 N  ND2  . ASN   B 1 72  ? 43.840 -4.648  8.422   1.00 19.38 ?  72  ASN   B ND2  1 
ATOM   4691 H  H    . ASN   B 1 72  ? 46.708 -6.601  10.795  1.00 18.44 ?  72  ASN   B H    1 
ATOM   4692 H  HA   . ASN   B 1 72  ? 44.234 -5.523  11.056  1.00 18.83 ?  72  ASN   B HA   1 
ATOM   4693 H  HB2  . ASN   B 1 72  ? 45.026 -7.491  9.193   1.00 20.15 ?  72  ASN   B HB2  1 
ATOM   4694 H  HB3  . ASN   B 1 72  ? 43.528 -6.985  9.360   1.00 20.15 ?  72  ASN   B HB3  1 
ATOM   4695 H  HD21 . ASN   B 1 72  ? 43.943 -3.989  7.880   1.00 23.26 ?  72  ASN   B HD21 1 
ATOM   4696 H  HD22 . ASN   B 1 72  ? 43.150 -4.679  8.935   1.00 23.26 ?  72  ASN   B HD22 1 
ATOM   4697 N  N    . GLY   B 1 73  ? 45.192 -8.162  12.424  1.00 15.81 ?  73  GLY   B N    1 
ATOM   4698 C  CA   . GLY   B 1 73  ? 44.797 -9.299  13.216  1.00 15.18 ?  73  GLY   B CA   1 
ATOM   4699 C  C    . GLY   B 1 73  ? 44.433 -10.479 12.345  1.00 14.10 ?  73  GLY   B C    1 
ATOM   4700 O  O    . GLY   B 1 73  ? 44.421 -10.400 11.115  1.00 14.04 ?  73  GLY   B O    1 
ATOM   4701 H  H    . GLY   B 1 73  ? 46.044 -8.032  12.394  1.00 18.98 ?  73  GLY   B H    1 
ATOM   4702 H  HA2  . GLY   B 1 73  ? 45.527 -9.556  13.803  1.00 18.22 ?  73  GLY   B HA2  1 
ATOM   4703 H  HA3  . GLY   B 1 73  ? 44.030 -9.067  13.762  1.00 18.22 ?  73  GLY   B HA3  1 
ATOM   4704 N  N    . PRO   B 1 74  ? 44.128 -11.602 12.984  1.00 14.16 ?  74  PRO   B N    1 
ATOM   4705 C  CA   . PRO   B 1 74  ? 43.880 -12.836 12.238  1.00 14.03 ?  74  PRO   B CA   1 
ATOM   4706 C  C    . PRO   B 1 74  ? 42.576 -12.787 11.453  1.00 13.17 ?  74  PRO   B C    1 
ATOM   4707 O  O    . PRO   B 1 74  ? 41.633 -12.051 11.769  1.00 14.64 ?  74  PRO   B O    1 
ATOM   4708 C  CB   . PRO   B 1 74  ? 43.813 -13.897 13.343  1.00 15.08 ?  74  PRO   B CB   1 
ATOM   4709 C  CG   . PRO   B 1 74  ? 43.354 -13.153 14.544  1.00 16.55 ?  74  PRO   B CG   1 
ATOM   4710 C  CD   . PRO   B 1 74  ? 44.009 -11.804 14.436  1.00 15.57 ?  74  PRO   B CD   1 
ATOM   4711 H  HA   . PRO   B 1 74  ? 44.628 -13.030 11.639  1.00 16.83 ?  74  PRO   B HA   1 
ATOM   4712 H  HB2  . PRO   B 1 74  ? 43.178 -14.585 13.094  1.00 18.10 ?  74  PRO   B HB2  1 
ATOM   4713 H  HB3  . PRO   B 1 74  ? 44.696 -14.278 13.487  1.00 18.10 ?  74  PRO   B HB3  1 
ATOM   4714 H  HG2  . PRO   B 1 74  ? 42.388 -13.069 14.525  1.00 19.86 ?  74  PRO   B HG2  1 
ATOM   4715 H  HG3  . PRO   B 1 74  ? 43.645 -13.613 15.345  1.00 19.86 ?  74  PRO   B HG3  1 
ATOM   4716 H  HD2  . PRO   B 1 74  ? 43.440 -11.118 14.830  1.00 18.69 ?  74  PRO   B HD2  1 
ATOM   4717 H  HD3  . PRO   B 1 74  ? 44.886 -11.815 14.850  1.00 18.69 ?  74  PRO   B HD3  1 
ATOM   4718 N  N    . LEU   B 1 75  ? 42.547 -13.598 10.399  1.00 12.43 ?  75  LEU   B N    1 
ATOM   4719 C  CA   . LEU   B 1 75  ? 41.332 -13.818 9.638   1.00 12.71 ?  75  LEU   B CA   1 
ATOM   4720 C  C    . LEU   B 1 75  ? 40.364 -14.681 10.446  1.00 12.96 ?  75  LEU   B C    1 
ATOM   4721 O  O    . LEU   B 1 75  ? 40.709 -15.236 11.491  1.00 14.15 ?  75  LEU   B O    1 
ATOM   4722 C  CB   . LEU   B 1 75  ? 41.659 -14.535 8.328   1.00 13.05 ?  75  LEU   B CB   1 
ATOM   4723 C  CG   . LEU   B 1 75  ? 42.500 -13.788 7.287   1.00 14.86 ?  75  LEU   B CG   1 
ATOM   4724 C  CD1  . LEU   B 1 75  ? 42.644 -14.613 6.014   1.00 15.86 ?  75  LEU   B CD1  1 
ATOM   4725 C  CD2  . LEU   B 1 75  ? 41.929 -12.434 6.966   1.00 17.34 ?  75  LEU   B CD2  1 
ATOM   4726 H  H    . LEU   B 1 75  ? 43.226 -14.042 10.101  1.00 14.92 ?  75  LEU   B H    1 
ATOM   4727 H  HA   . LEU   B 1 75  ? 40.908 -12.970 9.437   1.00 15.25 ?  75  LEU   B HA   1 
ATOM   4728 H  HB2  . LEU   B 1 75  ? 42.138 -15.350 8.538   1.00 15.67 ?  75  LEU   B HB2  1 
ATOM   4729 H  HB3  . LEU   B 1 75  ? 40.822 -14.764 7.891   1.00 15.67 ?  75  LEU   B HB3  1 
ATOM   4730 H  HG   . LEU   B 1 75  ? 43.392 -13.653 7.643   1.00 17.83 ?  75  LEU   B HG   1 
ATOM   4731 H  HD11 . LEU   B 1 75  ? 43.187 -14.120 5.371   1.00 19.03 ?  75  LEU   B HD11 1 
ATOM   4732 H  HD12 . LEU   B 1 75  ? 43.078 -15.455 6.225   1.00 19.03 ?  75  LEU   B HD12 1 
ATOM   4733 H  HD13 . LEU   B 1 75  ? 41.766 -14.779 5.638   1.00 19.03 ?  75  LEU   B HD13 1 
ATOM   4734 H  HD21 . LEU   B 1 75  ? 42.432 -12.038 6.239   1.00 20.81 ?  75  LEU   B HD21 1 
ATOM   4735 H  HD22 . LEU   B 1 75  ? 40.999 -12.538 6.708   1.00 20.81 ?  75  LEU   B HD22 1 
ATOM   4736 H  HD23 . LEU   B 1 75  ? 41.991 -11.872 7.756   1.00 20.81 ?  75  LEU   B HD23 1 
ATOM   4737 N  N    . LYS   B 1 76  ? 39.134 -14.790 9.938   1.00 14.03 ?  76  LYS   B N    1 
ATOM   4738 C  CA   . LYS   B 1 76  ? 38.154 -15.756 10.417  1.00 15.53 ?  76  LYS   B CA   1 
ATOM   4739 C  C    . LYS   B 1 76  ? 38.246 -17.024 9.573   1.00 13.96 ?  76  LYS   B C    1 
ATOM   4740 O  O    . LYS   B 1 76  ? 38.512 -16.959 8.372   1.00 13.80 ?  76  LYS   B O    1 
ATOM   4741 C  CB   . LYS   B 1 76  ? 36.733 -15.191 10.254  1.00 18.28 ?  76  LYS   B CB   1 
ATOM   4742 C  CG   . LYS   B 1 76  ? 36.474 -13.787 10.830  1.00 20.31 ?  76  LYS   B CG   1 
ATOM   4743 C  CD   . LYS   B 1 76  ? 35.056 -13.273 10.505  1.00 22.04 ?  76  LYS   B CD   1 
ATOM   4744 C  CE   . LYS   B 1 76  ? 34.794 -11.902 11.118  1.00 23.85 ?  76  LYS   B CE   1 
ATOM   4745 N  NZ   . LYS   B 1 76  ? 33.491 -11.313 10.687  1.00 24.77 ?  76  LYS   B NZ   1 
ATOM   4746 H  H    . LYS   B 1 76  ? 38.841 -14.303 9.295   1.00 16.84 ?  76  LYS   B H    1 
ATOM   4747 H  HA   . LYS   B 1 76  ? 38.314 -15.978 11.348  1.00 18.64 ?  76  LYS   B HA   1 
ATOM   4748 H  HB2  . LYS   B 1 76  ? 36.528 -15.154 9.306   1.00 21.94 ?  76  LYS   B HB2  1 
ATOM   4749 H  HB3  . LYS   B 1 76  ? 36.113 -15.796 10.691  1.00 21.94 ?  76  LYS   B HB3  1 
ATOM   4750 H  HG2  . LYS   B 1 76  ? 36.574 -13.816 11.794  1.00 24.38 ?  76  LYS   B HG2  1 
ATOM   4751 H  HG3  . LYS   B 1 76  ? 37.117 -13.166 10.448  1.00 24.38 ?  76  LYS   B HG3  1 
ATOM   4752 H  HD2  . LYS   B 1 76  ? 34.958 -13.200 9.542   1.00 26.45 ?  76  LYS   B HD2  1 
ATOM   4753 H  HD3  . LYS   B 1 76  ? 34.405 -13.896 10.861  1.00 26.45 ?  76  LYS   B HD3  1 
ATOM   4754 H  HE2  . LYS   B 1 76  ? 34.782 -11.985 12.084  1.00 28.63 ?  76  LYS   B HE2  1 
ATOM   4755 H  HE3  . LYS   B 1 76  ? 35.501 -11.294 10.848  1.00 28.63 ?  76  LYS   B HE3  1 
ATOM   4756 H  HZ1  . LYS   B 1 76  ? 33.375 -10.515 11.066  1.00 29.72 ?  76  LYS   B HZ1  1 
ATOM   4757 H  HZ2  . LYS   B 1 76  ? 33.476 -11.216 9.802   1.00 29.72 ?  76  LYS   B HZ2  1 
ATOM   4758 H  HZ3  . LYS   B 1 76  ? 32.820 -11.846 10.930  1.00 29.72 ?  76  LYS   B HZ3  1 
ATOM   4759 N  N    . VAL   B 1 77  ? 38.004 -18.184 10.197  1.00 14.27 ?  77  VAL   B N    1 
ATOM   4760 C  CA   . VAL   B 1 77  ? 37.789 -19.390 9.404   1.00 14.28 ?  77  VAL   B CA   1 
ATOM   4761 C  C    . VAL   B 1 77  ? 36.592 -19.149 8.496   1.00 13.37 ?  77  VAL   B C    1 
ATOM   4762 O  O    . VAL   B 1 77  ? 35.527 -18.706 8.950   1.00 13.51 ?  77  VAL   B O    1 
ATOM   4763 C  CB   . VAL   B 1 77  ? 37.589 -20.619 10.303  1.00 15.67 ?  77  VAL   B CB   1 
ATOM   4764 C  CG1  . VAL   B 1 77  ? 37.287 -21.843 9.448   1.00 16.74 ?  77  VAL   B CG1  1 
ATOM   4765 C  CG2  . VAL   B 1 77  ? 38.824 -20.862 11.169  1.00 17.37 ?  77  VAL   B CG2  1 
ATOM   4766 H  H    . VAL   B 1 77  ? 37.967 -18.290 11.046  1.00 17.13 ?  77  VAL   B H    1 
ATOM   4767 H  HA   . VAL   B 1 77  ? 38.562 -19.546 8.844   1.00 17.14 ?  77  VAL   B HA   1 
ATOM   4768 H  HB   . VAL   B 1 77  ? 36.832 -20.462 10.892  1.00 18.81 ?  77  VAL   B HB   1 
ATOM   4769 H  HG11 . VAL   B 1 77  ? 37.352 -22.636 10.005  1.00 20.10 ?  77  VAL   B HG11 1 
ATOM   4770 H  HG12 . VAL   B 1 77  ? 36.387 -21.768 9.090   1.00 20.10 ?  77  VAL   B HG12 1 
ATOM   4771 H  HG13 . VAL   B 1 77  ? 37.930 -21.891 8.727   1.00 20.10 ?  77  VAL   B HG13 1 
ATOM   4772 H  HG21 . VAL   B 1 77  ? 38.680 -21.660 11.700  1.00 20.85 ?  77  VAL   B HG21 1 
ATOM   4773 H  HG22 . VAL   B 1 77  ? 39.592 -20.980 10.591  1.00 20.85 ?  77  VAL   B HG22 1 
ATOM   4774 H  HG23 . VAL   B 1 77  ? 38.957 -20.096 11.749  1.00 20.85 ?  77  VAL   B HG23 1 
ATOM   4775 N  N    . GLY   B 1 78  ? 36.770 -19.419 7.207   1.00 12.98 ?  78  GLY   B N    1 
ATOM   4776 C  CA   . GLY   B 1 78  ? 35.792 -19.095 6.196   1.00 12.66 ?  78  GLY   B CA   1 
ATOM   4777 C  C    . GLY   B 1 78  ? 36.034 -17.776 5.501   1.00 12.33 ?  78  GLY   B C    1 
ATOM   4778 O  O    . GLY   B 1 78  ? 35.360 -17.492 4.507   1.00 12.47 ?  78  GLY   B O    1 
ATOM   4779 H  H    . GLY   B 1 78  ? 37.473 -19.804 6.891   1.00 15.58 ?  78  GLY   B H    1 
ATOM   4780 H  HA2  . GLY   B 1 78  ? 35.787 -19.789 5.524   1.00 15.20 ?  78  GLY   B HA2  1 
ATOM   4781 H  HA3  . GLY   B 1 78  ? 34.913 -19.058 6.605   1.00 15.20 ?  78  GLY   B HA3  1 
ATOM   4782 N  N    . GLY   B 1 79  ? 36.982 -16.971 5.990   1.00 12.21 ?  79  GLY   B N    1 
ATOM   4783 C  CA   . GLY   B 1 79  ? 37.281 -15.677 5.419   1.00 11.88 ?  79  GLY   B CA   1 
ATOM   4784 C  C    . GLY   B 1 79  ? 38.511 -15.695 4.525   1.00 11.48 ?  79  GLY   B C    1 
ATOM   4785 O  O    . GLY   B 1 79  ? 39.126 -16.730 4.267   1.00 12.13 ?  79  GLY   B O    1 
ATOM   4786 H  H    . GLY   B 1 79  ? 37.479 -17.164 6.664   1.00 14.65 ?  79  GLY   B H    1 
ATOM   4787 H  HA2  . GLY   B 1 79  ? 36.526 -15.370 4.890   1.00 14.26 ?  79  GLY   B HA2  1 
ATOM   4788 H  HA3  . GLY   B 1 79  ? 37.432 -15.034 6.131   1.00 14.26 ?  79  GLY   B HA3  1 
ATOM   4789 N  N    . SER   B 1 80  ? 38.873 -14.499 4.058   1.00 11.60 ?  80  SER   B N    1 
ATOM   4790 C  CA   . SER   B 1 80  ? 39.976 -14.366 3.119   1.00 11.51 ?  80  SER   B CA   1 
ATOM   4791 C  C    . SER   B 1 80  ? 40.554 -12.957 3.175   1.00 11.27 ?  80  SER   B C    1 
ATOM   4792 O  O    . SER   B 1 80  ? 39.939 -12.023 3.699   1.00 12.61 ?  80  SER   B O    1 
ATOM   4793 C  CB   . SER   B 1 80  ? 39.526 -14.659 1.685   1.00 11.56 ?  80  SER   B CB   1 
ATOM   4794 O  OG   . SER   B 1 80  ? 38.688 -13.631 1.182   1.00 12.53 ?  80  SER   B OG   1 
ATOM   4795 H  H    . SER   B 1 80  ? 38.503 -13.754 4.273   1.00 13.92 ?  80  SER   B H    1 
ATOM   4796 H  HA   . SER   B 1 80  ? 40.670 -14.995 3.360   1.00 13.82 ?  80  SER   B HA   1 
ATOM   4797 H  HB2  . SER   B 1 80  ? 40.304 -14.730 1.112   1.00 13.88 ?  80  SER   B HB2  1 
ATOM   4798 H  HB3  . SER   B 1 80  ? 39.031 -15.496 1.674   1.00 13.88 ?  80  SER   B HB3  1 
ATOM   4799 H  HG   . SER   B 1 80  ? 38.001 -13.560 1.667   1.00 15.04 ?  80  SER   B HG   1 
ATOM   4800 N  N    . CYS   B 1 81  ? 41.739 -12.809 2.586   1.00 11.12 ?  81  CYS   B N    1 
ATOM   4801 C  CA   . CYS   B 1 81  ? 42.278 -11.493 2.285   1.00 11.20 ?  81  CYS   B CA   1 
ATOM   4802 C  C    . CYS   B 1 81  ? 43.044 -11.570 0.976   1.00 10.47 ?  81  CYS   B C    1 
ATOM   4803 O  O    . CYS   B 1 81  ? 43.559 -12.630 0.598   1.00 11.57 ?  81  CYS   B O    1 
ATOM   4804 C  CB   . CYS   B 1 81  ? 43.163 -10.945 3.409   1.00 11.92 ?  81  CYS   B CB   1 
ATOM   4805 S  SG   . CYS   B 1 81  ? 44.690 -11.875 3.650   1.00 12.37 ?  81  CYS   B SG   1 
ATOM   4806 H  H    . CYS   B 1 81  ? 42.250 -13.462 2.342   1.00 13.35 ?  81  CYS   B H    1 
ATOM   4807 H  HA   . CYS   B 1 81  ? 41.540 -10.874 2.160   1.00 13.44 ?  81  CYS   B HA   1 
ATOM   4808 H  HB2  . CYS   B 1 81  ? 43.406 -10.028 3.201   1.00 14.30 ?  81  CYS   B HB2  1 
ATOM   4809 H  HB3  . CYS   B 1 81  ? 42.662 -10.967 4.243   1.00 14.30 ?  81  CYS   B HB3  1 
ATOM   4810 H  HG   . CYS   B 1 81  ? 45.314 -11.383 4.550   1.00 14.85 ?  81  CYS   B HG   1 
ATOM   4811 N  N    . VAL   B 1 82  ? 43.134 -10.428 0.302   1.00 10.91 ?  82  VAL   B N    1 
ATOM   4812 C  CA   . VAL   B 1 82  ? 43.903 -10.305 -0.934  1.00 11.27 ?  82  VAL   B CA   1 
ATOM   4813 C  C    . VAL   B 1 82  ? 45.244 -9.666  -0.613  1.00 11.40 ?  82  VAL   B C    1 
ATOM   4814 O  O    . VAL   B 1 82  ? 45.297 -8.550  -0.081  1.00 12.43 ?  82  VAL   B O    1 
ATOM   4815 C  CB   . VAL   B 1 82  ? 43.158 -9.464  -1.981  1.00 12.29 ?  82  VAL   B CB   1 
ATOM   4816 C  CG1  . VAL   B 1 82  ? 44.011 -9.315  -3.238  1.00 13.61 ?  82  VAL   B CG1  1 
ATOM   4817 C  CG2  . VAL   B 1 82  ? 41.806 -10.072 -2.299  1.00 13.28 ?  82  VAL   B CG2  1 
ATOM   4818 H  H    . VAL   B 1 82  ? 42.746 -9.695  0.540   1.00 13.09 ?  82  VAL   B H    1 
ATOM   4819 H  HA   . VAL   B 1 82  ? 44.059 -11.185 -1.306  1.00 13.52 ?  82  VAL   B HA   1 
ATOM   4820 H  HB   . VAL   B 1 82  ? 43.004 -8.578  -1.622  1.00 14.75 ?  82  VAL   B HB   1 
ATOM   4821 H  HG11 . VAL   B 1 82  ? 43.452 -9.007  -3.968  1.00 16.33 ?  82  VAL   B HG11 1 
ATOM   4822 H  HG12 . VAL   B 1 82  ? 44.716 -8.665  -3.070  1.00 16.33 ?  82  VAL   B HG12 1 
ATOM   4823 H  HG13 . VAL   B 1 82  ? 44.402 -10.174 -3.461  1.00 16.33 ?  82  VAL   B HG13 1 
ATOM   4824 H  HG21 . VAL   B 1 82  ? 41.373 -9.548  -2.995  1.00 15.93 ?  82  VAL   B HG21 1 
ATOM   4825 H  HG22 . VAL   B 1 82  ? 41.929 -10.985 -2.608  1.00 15.93 ?  82  VAL   B HG22 1 
ATOM   4826 H  HG23 . VAL   B 1 82  ? 41.256 -10.068 -1.498  1.00 15.93 ?  82  VAL   B HG23 1 
ATOM   4827 N  N    . LEU   B 1 83  ? 46.324 -10.348 -0.981  1.00 10.98 ?  83  LEU   B N    1 
ATOM   4828 C  CA   . LEU   B 1 83  ? 47.676 -9.829  -0.857  1.00 10.76 ?  83  LEU   B CA   1 
ATOM   4829 C  C    . LEU   B 1 83  ? 48.373 -9.967  -2.207  1.00 11.05 ?  83  LEU   B C    1 
ATOM   4830 O  O    . LEU   B 1 83  ? 47.769 -10.376 -3.203  1.00 10.70 ?  83  LEU   B O    1 
ATOM   4831 C  CB   . LEU   B 1 83  ? 48.431 -10.509 0.291   1.00 11.53 ?  83  LEU   B CB   1 
ATOM   4832 C  CG   . LEU   B 1 83  ? 47.927 -10.147 1.690   1.00 12.77 ?  83  LEU   B CG   1 
ATOM   4833 C  CD1  . LEU   B 1 83  ? 48.549 -11.017 2.760   1.00 13.37 ?  83  LEU   B CD1  1 
ATOM   4834 C  CD2  . LEU   B 1 83  ? 48.155 -8.669  2.005   1.00 13.50 ?  83  LEU   B CD2  1 
ATOM   4835 H  H    . LEU   B 1 83  ? 46.290 -11.140 -1.321  1.00 13.18 ?  83  LEU   B H    1 
ATOM   4836 H  HA   . LEU   B 1 83  ? 47.621 -8.884  -0.658  1.00 12.91 ?  83  LEU   B HA   1 
ATOM   4837 H  HB2  . LEU   B 1 83  ? 48.356 -11.468 0.191   1.00 13.84 ?  83  LEU   B HB2  1 
ATOM   4838 H  HB3  . LEU   B 1 83  ? 49.366 -10.248 0.240   1.00 13.84 ?  83  LEU   B HB3  1 
ATOM   4839 H  HG   . LEU   B 1 83  ? 46.972 -10.299 1.713   1.00 15.33 ?  83  LEU   B HG   1 
ATOM   4840 H  HD11 . LEU   B 1 83  ? 48.192 -10.761 3.626   1.00 16.04 ?  83  LEU   B HD11 1 
ATOM   4841 H  HD12 . LEU   B 1 83  ? 48.328 -11.948 2.578   1.00 16.04 ?  83  LEU   B HD12 1 
ATOM   4842 H  HD13 . LEU   B 1 83  ? 49.510 -10.901 2.751   1.00 16.04 ?  83  LEU   B HD13 1 
ATOM   4843 H  HD21 . LEU   B 1 83  ? 47.968 -8.515  2.945   1.00 16.20 ?  83  LEU   B HD21 1 
ATOM   4844 H  HD22 . LEU   B 1 83  ? 49.077 -8.441  1.809   1.00 16.20 ?  83  LEU   B HD22 1 
ATOM   4845 H  HD23 . LEU   B 1 83  ? 47.559 -8.132  1.458   1.00 16.20 ?  83  LEU   B HD23 1 
ATOM   4846 N  N    . SER   B 1 84  ? 49.649 -9.595  -2.260  1.00 12.04 ?  84  SER   B N    1 
ATOM   4847 C  CA   . SER   B 1 84  ? 50.381 -9.704  -3.513  1.00 12.36 ?  84  SER   B CA   1 
ATOM   4848 C  C    . SER   B 1 84  ? 50.531 -11.160 -3.941  1.00 11.88 ?  84  SER   B C    1 
ATOM   4849 O  O    . SER   B 1 84  ? 50.650 -12.066 -3.117  1.00 11.41 ?  84  SER   B O    1 
ATOM   4850 C  CB   . SER   B 1 84  ? 51.776 -9.103  -3.367  1.00 14.29 ?  84  SER   B CB   1 
ATOM   4851 O  OG   . SER   B 1 84  ? 52.516 -9.313  -4.554  1.00 15.71 ?  84  SER   B OG   1 
ATOM   4852 H  H    . SER   B 1 84  ? 50.101 -9.273  -1.600  1.00 14.45 ?  84  SER   B H    1 
ATOM   4853 H  HA   . SER   B 1 84  ? 49.909 -9.228  -4.211  1.00 14.83 ?  84  SER   B HA   1 
ATOM   4854 H  HB2  . SER   B 1 84  ? 51.694 -8.146  -3.204  1.00 17.15 ?  84  SER   B HB2  1 
ATOM   4855 H  HB3  . SER   B 1 84  ? 52.236 -9.527  -2.631  1.00 17.15 ?  84  SER   B HB3  1 
ATOM   4856 H  HG   . SER   B 1 84  ? 53.284 -8.968  -4.483  1.00 18.85 ?  84  SER   B HG   1 
ATOM   4857 N  N    . GLY   B 1 85  ? 50.592 -11.369 -5.248  1.00 12.89 ?  85  GLY   B N    1 
ATOM   4858 C  CA   . GLY   B 1 85  ? 50.938 -12.659 -5.793  1.00 13.44 ?  85  GLY   B CA   1 
ATOM   4859 C  C    . GLY   B 1 85  ? 52.406 -12.851 -6.093  1.00 12.44 ?  85  GLY   B C    1 
ATOM   4860 O  O    . GLY   B 1 85  ? 52.782 -13.923 -6.565  1.00 12.89 ?  85  GLY   B O    1 
ATOM   4861 H  H    . GLY   B 1 85  ? 50.443 -10.772 -5.840  1.00 15.47 ?  85  GLY   B H    1 
ATOM   4862 H  HA2  . GLY   B 1 85  ? 50.671 -13.352 -5.164  1.00 16.13 ?  85  GLY   B HA2  1 
ATOM   4863 H  HA3  . GLY   B 1 85  ? 50.447 -12.799 -6.613  1.00 16.13 ?  85  GLY   B HA3  1 
ATOM   4864 N  N    . HIS   B 1 86  ? 53.259 -11.855 -5.853  1.00 12.42 ?  86  HIS   B N    1 
ATOM   4865 C  CA   . HIS   B 1 86  ? 54.719 -12.024 -5.940  1.00 12.39 ?  86  HIS   B CA   1 
ATOM   4866 C  C    . HIS   B 1 86  ? 55.085 -12.530 -7.333  1.00 12.43 ?  86  HIS   B C    1 
ATOM   4867 O  O    . HIS   B 1 86  ? 54.693 -11.913 -8.336  1.00 13.52 ?  86  HIS   B O    1 
ATOM   4868 C  CB   . HIS   B 1 86  ? 55.209 -12.874 -4.772  1.00 12.33 ?  86  HIS   B CB   1 
ATOM   4869 C  CG   . HIS   B 1 86  ? 54.903 -12.273 -3.444  1.00 12.59 ?  86  HIS   B CG   1 
ATOM   4870 N  ND1  . HIS   B 1 86  ? 55.735 -11.363 -2.827  1.00 14.08 ?  86  HIS   B ND1  1 
ATOM   4871 C  CD2  . HIS   B 1 86  ? 53.830 -12.422 -2.632  1.00 12.87 ?  86  HIS   B CD2  1 
ATOM   4872 C  CE1  . HIS   B 1 86  ? 55.182 -10.978 -1.690  1.00 13.83 ?  86  HIS   B CE1  1 
ATOM   4873 N  NE2  . HIS   B 1 86  ? 54.025 -11.603 -1.550  1.00 13.31 ?  86  HIS   B NE2  1 
ATOM   4874 H  H    . HIS   B 1 86  ? 53.019 -11.061 -5.635  1.00 14.90 ?  86  HIS   B H    1 
ATOM   4875 H  HA   . HIS   B 1 86  ? 55.130 -11.152 -5.840  1.00 14.87 ?  86  HIS   B HA   1 
ATOM   4876 H  HB2  . HIS   B 1 86  ? 54.788 -13.747 -4.816  1.00 14.80 ?  86  HIS   B HB2  1 
ATOM   4877 H  HB3  . HIS   B 1 86  ? 56.176 -12.975 -4.838  1.00 14.80 ?  86  HIS   B HB3  1 
ATOM   4878 H  HD2  . HIS   B 1 86  ? 53.089 -12.967 -2.788  1.00 15.44 ?  86  HIS   B HD2  1 
ATOM   4879 H  HE1  . HIS   B 1 86  ? 55.554 -10.385 -1.080  1.00 16.60 ?  86  HIS   B HE1  1 
ATOM   4880 H  HE2  . HIS   B 1 86  ? 53.491 -11.527 -0.879  1.00 15.97 ?  86  HIS   B HE2  1 
ATOM   4881 N  N    . ASN   B 1 87  ? 55.844 -13.617 -7.449  1.00 12.92 ?  87  ASN   B N    1 
ATOM   4882 C  CA   . ASN   B 1 87  ? 56.239 -14.181 -8.730  1.00 13.72 ?  87  ASN   B CA   1 
ATOM   4883 C  C    . ASN   B 1 87  ? 55.259 -15.223 -9.234  1.00 13.41 ?  87  ASN   B C    1 
ATOM   4884 O  O    . ASN   B 1 87  ? 55.581 -15.938 -10.188 1.00 14.92 ?  87  ASN   B O    1 
ATOM   4885 C  CB   . ASN   B 1 87  ? 57.636 -14.805 -8.621  1.00 15.35 ?  87  ASN   B CB   1 
ATOM   4886 C  CG   . ASN   B 1 87  ? 57.700 -15.927 -7.591  1.00 16.36 ?  87  ASN   B CG   1 
ATOM   4887 O  OD1  . ASN   B 1 87  ? 57.064 -15.859 -6.535  1.00 15.66 ?  87  ASN   B OD1  1 
ATOM   4888 N  ND2  . ASN   B 1 87  ? 58.448 -16.985 -7.914  1.00 18.68 ?  87  ASN   B ND2  1 
ATOM   4889 H  H    . ASN   B 1 87  ? 56.152 -14.059 -6.777  1.00 15.51 ?  87  ASN   B H    1 
ATOM   4890 H  HA   . ASN   B 1 87  ? 56.280 -13.470 -9.385  1.00 16.47 ?  87  ASN   B HA   1 
ATOM   4891 H  HB2  . ASN   B 1 87  ? 57.884 -15.172 -9.486  1.00 18.43 ?  87  ASN   B HB2  1 
ATOM   4892 H  HB3  . ASN   B 1 87  ? 58.267 -14.120 -8.358  1.00 18.43 ?  87  ASN   B HB3  1 
ATOM   4893 H  HD21 . ASN   B 1 87  ? 58.518 -17.644 -7.370  1.00 22.42 ?  87  ASN   B HD21 1 
ATOM   4894 H  HD22 . ASN   B 1 87  ? 58.872 -17.000 -8.665  1.00 22.42 ?  87  ASN   B HD22 1 
ATOM   4895 N  N    . LEU   B 1 88  ? 54.083 -15.325 -8.615  1.00 12.49 ?  88  LEU   B N    1 
ATOM   4896 C  CA   . LEU   B 1 88  ? 53.108 -16.356 -8.939  1.00 12.51 ?  88  LEU   B CA   1 
ATOM   4897 C  C    . LEU   B 1 88  ? 51.875 -15.839 -9.661  1.00 12.18 ?  88  LEU   B C    1 
ATOM   4898 O  O    . LEU   B 1 88  ? 51.277 -16.583 -10.447 1.00 13.92 ?  88  LEU   B O    1 
ATOM   4899 C  CB   . LEU   B 1 88  ? 52.646 -17.039 -7.650  1.00 13.31 ?  88  LEU   B CB   1 
ATOM   4900 C  CG   . LEU   B 1 88  ? 53.756 -17.696 -6.842  1.00 15.46 ?  88  LEU   B CG   1 
ATOM   4901 C  CD1  . LEU   B 1 88  ? 53.250 -17.999 -5.443  1.00 16.96 ?  88  LEU   B CD1  1 
ATOM   4902 C  CD2  . LEU   B 1 88  ? 54.216 -18.956 -7.542  1.00 18.58 ?  88  LEU   B CD2  1 
ATOM   4903 H  H    . LEU   B 1 88  ? 53.825 -14.799 -7.980  1.00 14.99 ?  88  LEU   B H    1 
ATOM   4904 H  HA   . LEU   B 1 88  ? 53.524 -17.022 -9.500  1.00 15.02 ?  88  LEU   B HA   1 
ATOM   4905 H  HB2  . LEU   B 1 88  ? 52.222 -16.380 -7.079  1.00 15.97 ?  88  LEU   B HB2  1 
ATOM   4906 H  HB3  . LEU   B 1 88  ? 52.005 -17.731 -7.879  1.00 15.97 ?  88  LEU   B HB3  1 
ATOM   4907 H  HG   . LEU   B 1 88  ? 54.512 -17.089 -6.772  1.00 18.56 ?  88  LEU   B HG   1 
ATOM   4908 H  HD11 . LEU   B 1 88  ? 53.873 -18.596 -5.003  1.00 20.35 ?  88  LEU   B HD11 1 
ATOM   4909 H  HD12 . LEU   B 1 88  ? 53.178 -17.168 -4.947  1.00 20.35 ?  88  LEU   B HD12 1 
ATOM   4910 H  HD13 . LEU   B 1 88  ? 52.379 -18.419 -5.512  1.00 20.35 ?  88  LEU   B HD13 1 
ATOM   4911 H  HD21 . LEU   B 1 88  ? 54.891 -19.390 -6.998  1.00 22.30 ?  88  LEU   B HD21 1 
ATOM   4912 H  HD22 . LEU   B 1 88  ? 53.455 -19.546 -7.659  1.00 22.30 ?  88  LEU   B HD22 1 
ATOM   4913 H  HD23 . LEU   B 1 88  ? 54.588 -18.721 -8.406  1.00 22.30 ?  88  LEU   B HD23 1 
ATOM   4914 N  N    . ALA   B 1 89  ? 51.477 -14.599 -9.403  1.00 11.72 ?  89  ALA   B N    1 
ATOM   4915 C  CA   . ALA   B 1 89  ? 50.176 -14.111 -9.837  1.00 11.03 ?  89  ALA   B CA   1 
ATOM   4916 C  C    . ALA   B 1 89  ? 50.143 -12.619 -9.558  1.00 11.81 ?  89  ALA   B C    1 
ATOM   4917 O  O    . ALA   B 1 89  ? 50.984 -12.099 -8.825  1.00 12.61 ?  89  ALA   B O    1 
ATOM   4918 C  CB   . ALA   B 1 89  ? 49.057 -14.793 -9.054  1.00 11.10 ?  89  ALA   B CB   1 
ATOM   4919 H  H    . ALA   B 1 89  ? 51.931 -14.016 -8.959  1.00 14.06 ?  89  ALA   B H    1 
ATOM   4920 H  HA   . ALA   B 1 89  ? 50.050 -14.265 -10.784 1.00 13.23 ?  89  ALA   B HA   1 
ATOM   4921 H  HB1  . ALA   B 1 89  ? 48.199 -14.464 -9.374  1.00 13.32 ?  89  ALA   B HB1  1 
ATOM   4922 H  HB2  . ALA   B 1 89  ? 49.112 -15.753 -9.200  1.00 13.32 ?  89  ALA   B HB2  1 
ATOM   4923 H  HB3  . ALA   B 1 89  ? 49.158 -14.594 -8.114  1.00 13.32 ?  89  ALA   B HB3  1 
ATOM   4924 N  N    . LYS   B 1 90  ? 49.145 -11.933 -10.111 1.00 12.53 ?  90  LYS   B N    1 
ATOM   4925 C  CA   . LYS   B 1 90  ? 48.951 -10.546 -9.708  1.00 12.68 ?  90  LYS   B CA   1 
ATOM   4926 C  C    . LYS   B 1 90  ? 48.637 -10.475 -8.221  1.00 12.82 ?  90  LYS   B C    1 
ATOM   4927 O  O    . LYS   B 1 90  ? 49.271 -9.715  -7.472  1.00 13.95 ?  90  LYS   B O    1 
ATOM   4928 C  CB   . LYS   B 1 90  ? 47.859 -9.892  -10.554 1.00 14.51 ?  90  LYS   B CB   1 
ATOM   4929 C  CG   . LYS   B 1 90  ? 47.574 -8.448  -10.183 1.00 15.28 ?  90  LYS   B CG   1 
ATOM   4930 C  CD   . LYS   B 1 90  ? 48.787 -7.558  -10.292 1.00 18.25 ?  90  LYS   B CD   1 
ATOM   4931 C  CE   . LYS   B 1 90  ? 48.366 -6.129  -10.051 1.00 20.25 ?  90  LYS   B CE   1 
ATOM   4932 N  NZ   . LYS   B 1 90  ? 49.526 -5.210  -9.939  1.00 19.95 ?  90  LYS   B NZ   1 
ATOM   4933 H  H    . LYS   B 1 90  ? 48.591 -12.235 -10.697 1.00 15.04 ?  90  LYS   B H    1 
ATOM   4934 H  HA   . LYS   B 1 90  ? 49.774 -10.064 -9.861  1.00 15.22 ?  90  LYS   B HA   1 
ATOM   4935 H  HB2  . LYS   B 1 90  ? 48.135 -9.909  -11.486 1.00 17.41 ?  90  LYS   B HB2  1 
ATOM   4936 H  HB3  . LYS   B 1 90  ? 47.036 -10.397 -10.450 1.00 17.41 ?  90  LYS   B HB3  1 
ATOM   4937 H  HG2  . LYS   B 1 90  ? 46.891 -8.102  -10.779 1.00 18.34 ?  90  LYS   B HG2  1 
ATOM   4938 H  HG3  . LYS   B 1 90  ? 47.253 -8.415  -9.265  1.00 18.34 ?  90  LYS   B HG3  1 
ATOM   4939 H  HD2  . LYS   B 1 90  ? 49.438 -7.809  -9.618  1.00 21.90 ?  90  LYS   B HD2  1 
ATOM   4940 H  HD3  . LYS   B 1 90  ? 49.166 -7.631  -11.181 1.00 21.90 ?  90  LYS   B HD3  1 
ATOM   4941 H  HE2  . LYS   B 1 90  ? 47.820 -5.823  -10.795 1.00 24.30 ?  90  LYS   B HE2  1 
ATOM   4942 H  HE3  . LYS   B 1 90  ? 47.864 -6.071  -9.225  1.00 24.30 ?  90  LYS   B HE3  1 
ATOM   4943 H  HZ1  . LYS   B 1 90  ? 49.247 -4.372  -9.801  1.00 23.94 ?  90  LYS   B HZ1  1 
ATOM   4944 H  HZ2  . LYS   B 1 90  ? 50.047 -5.453  -9.260  1.00 23.94 ?  90  LYS   B HZ2  1 
ATOM   4945 H  HZ3  . LYS   B 1 90  ? 50.007 -5.227  -10.691 1.00 23.94 ?  90  LYS   B HZ3  1 
ATOM   4946 N  N    . HIS   B 1 91  ? 47.692 -11.304 -7.771  1.00 11.17 ?  91  HIS   B N    1 
ATOM   4947 C  CA   . HIS   B 1 91  ? 47.237 -11.323 -6.397  1.00 11.51 ?  91  HIS   B CA   1 
ATOM   4948 C  C    . HIS   B 1 91  ? 47.241 -12.750 -5.880  1.00 10.55 ?  91  HIS   B C    1 
ATOM   4949 O  O    . HIS   B 1 91  ? 47.000 -13.705 -6.625  1.00 11.10 ?  91  HIS   B O    1 
ATOM   4950 C  CB   . HIS   B 1 91  ? 45.787 -10.853 -6.274  1.00 12.78 ?  91  HIS   B CB   1 
ATOM   4951 C  CG   . HIS   B 1 91  ? 45.563 -9.452  -6.719  1.00 16.10 ?  91  HIS   B CG   1 
ATOM   4952 N  ND1  . HIS   B 1 91  ? 46.162 -8.372  -6.108  1.00 18.59 ?  91  HIS   B ND1  1 
ATOM   4953 C  CD2  . HIS   B 1 91  ? 44.789 -8.948  -7.704  1.00 18.42 ?  91  HIS   B CD2  1 
ATOM   4954 C  CE1  . HIS   B 1 91  ? 45.774 -7.259  -6.705  1.00 19.62 ?  91  HIS   B CE1  1 
ATOM   4955 N  NE2  . HIS   B 1 91  ? 44.934 -7.582  -7.674  1.00 19.71 ?  91  HIS   B NE2  1 
ATOM   4956 H  H    . HIS   B 1 91  ? 47.291 -11.883 -8.264  1.00 13.41 ?  91  HIS   B H    1 
ATOM   4957 H  HA   . HIS   B 1 91  ? 47.811 -10.770 -5.835  1.00 13.81 ?  91  HIS   B HA   1 
ATOM   4958 H  HB2  . HIS   B 1 91  ? 45.228 -11.427 -6.814  1.00 15.34 ?  91  HIS   B HB2  1 
ATOM   4959 H  HB3  . HIS   B 1 91  ? 45.518 -10.913 -5.342  1.00 15.34 ?  91  HIS   B HB3  1 
ATOM   4960 H  HD1  . HIS   B 1 91  ? 46.705 -8.413  -5.439  1.00 22.31 ?  91  HIS   B HD1  1 
ATOM   4961 H  HD2  . HIS   B 1 91  ? 44.261 -9.424  -8.296  1.00 22.11 ?  91  HIS   B HD2  1 
ATOM   4962 H  HE1  . HIS   B 1 91  ? 46.043 -6.393  -6.475  1.00 23.55 ?  91  HIS   B HE1  1 
ATOM   4963 N  N    . CYS   B 1 92  ? 47.442 -12.882 -4.579  1.00 10.44 ?  92  CYS   B N    1 
ATOM   4964 C  CA   . CYS   B 1 92  ? 47.143 -14.117 -3.871  1.00 10.20 ?  92  CYS   B CA   1 
ATOM   4965 C  C    . CYS   B 1 92  ? 45.928 -13.882 -2.983  1.00 10.11 ?  92  CYS   B C    1 
ATOM   4966 O  O    . CYS   B 1 92  ? 45.930 -12.980 -2.135  1.00 10.89 ?  92  CYS   B O    1 
ATOM   4967 C  CB   . CYS   B 1 92  ? 48.325 -14.577 -3.026  1.00 11.06 ?  92  CYS   B CB   1 
ATOM   4968 S  SG   . CYS   B 1 92  ? 47.968 -16.110 -2.128  1.00 10.73 ?  92  CYS   B SG   1 
ATOM   4969 H  H    . CYS   B 1 92  ? 47.771 -12.266 -4.072  1.00 12.53 ?  92  CYS   B H    1 
ATOM   4970 H  HA   . CYS   B 1 92  ? 46.939 -14.815 -4.514  1.00 12.25 ?  92  CYS   B HA   1 
ATOM   4971 H  HB2  . CYS   B 1 92  ? 49.087 -14.728 -3.599  1.00 13.28 ?  92  CYS   B HB2  1 
ATOM   4972 H  HB3  . CYS   B 1 92  ? 48.526 -13.888 -2.371  1.00 13.28 ?  92  CYS   B HB3  1 
ATOM   4973 H  HG   . CYS   B 1 92  ? 48.943 -16.429 -1.509  1.00 12.87 ?  92  CYS   B HG   1 
ATOM   4974 N  N    . LEU   B 1 93  ? 44.888 -14.686 -3.199  1.00 9.71  ?  93  LEU   B N    1 
ATOM   4975 C  CA   . LEU   B 1 93  ? 43.718 -14.710 -2.334  1.00 10.25 ?  93  LEU   B CA   1 
ATOM   4976 C  C    . LEU   B 1 93  ? 43.952 -15.777 -1.272  1.00 9.79  ?  93  LEU   B C    1 
ATOM   4977 O  O    . LEU   B 1 93  ? 43.904 -16.979 -1.566  1.00 10.01 ?  93  LEU   B O    1 
ATOM   4978 C  CB   . LEU   B 1 93  ? 42.455 -14.993 -3.145  1.00 10.62 ?  93  LEU   B CB   1 
ATOM   4979 C  CG   . LEU   B 1 93  ? 41.162 -15.030 -2.330  1.00 11.29 ?  93  LEU   B CG   1 
ATOM   4980 C  CD1  . LEU   B 1 93  ? 40.800 -13.649 -1.811  1.00 11.61 ?  93  LEU   B CD1  1 
ATOM   4981 C  CD2  . LEU   B 1 93  ? 40.037 -15.611 -3.164  1.00 11.43 ?  93  LEU   B CD2  1 
ATOM   4982 H  H    . LEU   B 1 93  ? 44.841 -15.254 -3.859  1.00 11.65 ?  93  LEU   B H    1 
ATOM   4983 H  HA   . LEU   B 1 93  ? 43.626 -13.853 -1.900  1.00 12.30 ?  93  LEU   B HA   1 
ATOM   4984 H  HB2  . LEU   B 1 93  ? 42.357 -14.292 -3.812  1.00 12.75 ?  93  LEU   B HB2  1 
ATOM   4985 H  HB3  . LEU   B 1 93  ? 42.549 -15.848 -3.583  1.00 12.75 ?  93  LEU   B HB3  1 
ATOM   4986 H  HG   . LEU   B 1 93  ? 41.292 -15.606 -1.563  1.00 13.55 ?  93  LEU   B HG   1 
ATOM   4987 H  HD11 . LEU   B 1 93  ? 39.952 -13.701 -1.345  1.00 13.93 ?  93  LEU   B HD11 1 
ATOM   4988 H  HD12 . LEU   B 1 93  ? 41.494 -13.346 -1.203  1.00 13.93 ?  93  LEU   B HD12 1 
ATOM   4989 H  HD13 . LEU   B 1 93  ? 40.729 -13.038 -2.561  1.00 13.93 ?  93  LEU   B HD13 1 
ATOM   4990 H  HD21 . LEU   B 1 93  ? 39.224 -15.621 -2.636  1.00 13.72 ?  93  LEU   B HD21 1 
ATOM   4991 H  HD22 . LEU   B 1 93  ? 39.910 -15.060 -3.954  1.00 13.72 ?  93  LEU   B HD22 1 
ATOM   4992 H  HD23 . LEU   B 1 93  ? 40.272 -16.515 -3.428  1.00 13.72 ?  93  LEU   B HD23 1 
ATOM   4993 N  N    . HIS   B 1 94  ? 44.230 -15.342 -0.050  1.00 9.61  ?  94  HIS   B N    1 
ATOM   4994 C  CA   . HIS   B 1 94  ? 44.449 -16.248 1.070   1.00 9.88  ?  94  HIS   B CA   1 
ATOM   4995 C  C    . HIS   B 1 94  ? 43.091 -16.606 1.654   1.00 10.15 ?  94  HIS   B C    1 
ATOM   4996 O  O    . HIS   B 1 94  ? 42.422 -15.735 2.216   1.00 11.53 ?  94  HIS   B O    1 
ATOM   4997 C  CB   . HIS   B 1 94  ? 45.323 -15.573 2.123   1.00 10.23 ?  94  HIS   B CB   1 
ATOM   4998 C  CG   . HIS   B 1 94  ? 46.701 -15.267 1.645   1.00 10.44 ?  94  HIS   B CG   1 
ATOM   4999 N  ND1  . HIS   B 1 94  ? 47.727 -16.184 1.720   1.00 10.44 ?  94  HIS   B ND1  1 
ATOM   5000 C  CD2  . HIS   B 1 94  ? 47.207 -14.158 1.052   1.00 10.07 ?  94  HIS   B CD2  1 
ATOM   5001 C  CE1  . HIS   B 1 94  ? 48.815 -15.635 1.207   1.00 10.56 ?  94  HIS   B CE1  1 
ATOM   5002 N  NE2  . HIS   B 1 94  ? 48.531 -14.408 0.797   1.00 10.62 ?  94  HIS   B NE2  1 
ATOM   5003 H  H    . HIS   B 1 94  ? 44.303 -14.508 0.157   1.00 11.54 ?  94  HIS   B H    1 
ATOM   5004 H  HA   . HIS   B 1 94  ? 44.890 -17.057 0.763   1.00 11.86 ?  94  HIS   B HA   1 
ATOM   5005 H  HB2  . HIS   B 1 94  ? 44.908 -14.736 2.383   1.00 12.28 ?  94  HIS   B HB2  1 
ATOM   5006 H  HB3  . HIS   B 1 94  ? 45.398 -16.160 2.890   1.00 12.28 ?  94  HIS   B HB3  1 
ATOM   5007 H  HD2  . HIS   B 1 94  ? 46.751 -13.373 0.862   1.00 12.09 ?  94  HIS   B HD2  1 
ATOM   5008 H  HE1  . HIS   B 1 94  ? 49.649 -16.050 1.148   1.00 12.67 ?  94  HIS   B HE1  1 
ATOM   5009 H  HE2  . HIS   B 1 94  ? 49.088 -13.868 0.429   1.00 12.74 ?  94  HIS   B HE2  1 
ATOM   5010 N  N    . VAL   B 1 95  ? 42.662 -17.861 1.496   1.00 10.21 ?  95  VAL   B N    1 
ATOM   5011 C  CA   . VAL   B 1 95  ? 41.338 -18.301 1.931   1.00 10.09 ?  95  VAL   B CA   1 
ATOM   5012 C  C    . VAL   B 1 95  ? 41.508 -19.341 3.024   1.00 10.36 ?  95  VAL   B C    1 
ATOM   5013 O  O    . VAL   B 1 95  ? 42.284 -20.290 2.862   1.00 10.76 ?  95  VAL   B O    1 
ATOM   5014 C  CB   . VAL   B 1 95  ? 40.515 -18.893 0.772   1.00 10.67 ?  95  VAL   B CB   1 
ATOM   5015 C  CG1  . VAL   B 1 95  ? 39.145 -19.349 1.262   1.00 11.58 ?  95  VAL   B CG1  1 
ATOM   5016 C  CG2  . VAL   B 1 95  ? 40.386 -17.908 -0.362  1.00 10.88 ?  95  VAL   B CG2  1 
ATOM   5017 H  H    . VAL   B 1 95  ? 43.125 -18.486 1.128   1.00 12.25 ?  95  VAL   B H    1 
ATOM   5018 H  HA   . VAL   B 1 95  ? 40.847 -17.549 2.300   1.00 12.11 ?  95  VAL   B HA   1 
ATOM   5019 H  HB   . VAL   B 1 95  ? 40.973 -19.673 0.429   1.00 12.81 ?  95  VAL   B HB   1 
ATOM   5020 H  HG11 . VAL   B 1 95  ? 38.577 -19.533 0.492   1.00 13.90 ?  95  VAL   B HG11 1 
ATOM   5021 H  HG12 . VAL   B 1 95  ? 39.244 -20.156 1.790   1.00 13.90 ?  95  VAL   B HG12 1 
ATOM   5022 H  HG13 . VAL   B 1 95  ? 38.746 -18.647 1.798   1.00 13.90 ?  95  VAL   B HG13 1 
ATOM   5023 H  HG21 . VAL   B 1 95  ? 39.802 -18.284 -1.038  1.00 13.06 ?  95  VAL   B HG21 1 
ATOM   5024 H  HG22 . VAL   B 1 95  ? 40.008 -17.085 -0.017  1.00 13.06 ?  95  VAL   B HG22 1 
ATOM   5025 H  HG23 . VAL   B 1 95  ? 41.264 -17.745 -0.730  1.00 13.06 ?  95  VAL   B HG23 1 
ATOM   5026 N  N    . VAL   B 1 96  ? 40.780 -19.175 4.123   1.00 10.89 ?  96  VAL   B N    1 
ATOM   5027 C  CA   . VAL   B 1 96  ? 40.875 -20.090 5.257   1.00 11.25 ?  96  VAL   B CA   1 
ATOM   5028 C  C    . VAL   B 1 96  ? 39.686 -21.046 5.207   1.00 11.67 ?  96  VAL   B C    1 
ATOM   5029 O  O    . VAL   B 1 96  ? 38.564 -20.686 5.575   1.00 12.30 ?  96  VAL   B O    1 
ATOM   5030 C  CB   . VAL   B 1 96  ? 40.929 -19.342 6.591   1.00 12.06 ?  96  VAL   B CB   1 
ATOM   5031 C  CG1  . VAL   B 1 96  ? 41.106 -20.329 7.731   1.00 12.65 ?  96  VAL   B CG1  1 
ATOM   5032 C  CG2  . VAL   B 1 96  ? 42.044 -18.304 6.598   1.00 12.99 ?  96  VAL   B CG2  1 
ATOM   5033 H  H    . VAL   B 1 96  ? 40.213 -18.541 4.235   1.00 13.07 ?  96  VAL   B H    1 
ATOM   5034 H  HA   . VAL   B 1 96  ? 41.689 -20.616 5.177   1.00 13.50 ?  96  VAL   B HA   1 
ATOM   5035 H  HB   . VAL   B 1 96  ? 40.089 -18.878 6.727   1.00 14.47 ?  96  VAL   B HB   1 
ATOM   5036 H  HG11 . VAL   B 1 96  ? 41.296 -19.840 8.549   1.00 15.18 ?  96  VAL   B HG11 1 
ATOM   5037 H  HG12 . VAL   B 1 96  ? 40.294 -20.846 7.839   1.00 15.18 ?  96  VAL   B HG12 1 
ATOM   5038 H  HG13 . VAL   B 1 96  ? 41.850 -20.921 7.527   1.00 15.18 ?  96  VAL   B HG13 1 
ATOM   5039 H  HG21 . VAL   B 1 96  ? 42.089 -17.889 7.477   1.00 15.59 ?  96  VAL   B HG21 1 
ATOM   5040 H  HG22 . VAL   B 1 96  ? 42.888 -18.737 6.397   1.00 15.59 ?  96  VAL   B HG22 1 
ATOM   5041 H  HG23 . VAL   B 1 96  ? 41.854 -17.625 5.928   1.00 15.59 ?  96  VAL   B HG23 1 
ATOM   5042 N  N    . GLY   B 1 97  ? 39.922 -22.278 4.775   1.00 11.83 ?  97  GLY   B N    1 
ATOM   5043 C  CA   . GLY   B 1 97  ? 38.942 -23.326 4.929   1.00 12.11 ?  97  GLY   B CA   1 
ATOM   5044 C  C    . GLY   B 1 97  ? 39.065 -23.938 6.307   1.00 12.94 ?  97  GLY   B C    1 
ATOM   5045 O  O    . GLY   B 1 97  ? 40.105 -23.818 6.966   1.00 13.44 ?  97  GLY   B O    1 
ATOM   5046 H  H    . GLY   B 1 97  ? 40.654 -22.527 4.390   1.00 14.19 ?  97  GLY   B H    1 
ATOM   5047 H  HA2  . GLY   B 1 97  ? 38.053 -22.955 4.816   1.00 14.53 ?  97  GLY   B HA2  1 
ATOM   5048 H  HA3  . GLY   B 1 97  ? 39.084 -24.011 4.255   1.00 14.53 ?  97  GLY   B HA3  1 
ATOM   5049 N  N    . PRO   B 1 98  ? 38.020 -24.626 6.762   1.00 13.35 ?  98  PRO   B N    1 
ATOM   5050 C  CA   . PRO   B 1 98  ? 38.105 -25.320 8.049   1.00 14.13 ?  98  PRO   B CA   1 
ATOM   5051 C  C    . PRO   B 1 98  ? 39.133 -26.437 8.003   1.00 14.21 ?  98  PRO   B C    1 
ATOM   5052 O  O    . PRO   B 1 98  ? 39.237 -27.173 7.020   1.00 14.48 ?  98  PRO   B O    1 
ATOM   5053 C  CB   . PRO   B 1 98  ? 36.687 -25.869 8.245   1.00 14.45 ?  98  PRO   B CB   1 
ATOM   5054 C  CG   . PRO   B 1 98  ? 36.137 -26.000 6.863   1.00 14.23 ?  98  PRO   B CG   1 
ATOM   5055 C  CD   . PRO   B 1 98  ? 36.708 -24.817 6.118   1.00 13.50 ?  98  PRO   B CD   1 
ATOM   5056 H  HA   . PRO   B 1 98  ? 38.320 -24.701 8.758   1.00 16.96 ?  98  PRO   B HA   1 
ATOM   5057 H  HB2  . PRO   B 1 98  ? 36.726 -26.737 8.679   1.00 17.34 ?  98  PRO   B HB2  1 
ATOM   5058 H  HB3  . PRO   B 1 98  ? 36.161 -25.245 8.764   1.00 17.34 ?  98  PRO   B HB3  1 
ATOM   5059 H  HG2  . PRO   B 1 98  ? 36.435 -26.836 6.467   1.00 17.08 ?  98  PRO   B HG2  1 
ATOM   5060 H  HG3  . PRO   B 1 98  ? 35.168 -25.958 6.888   1.00 17.08 ?  98  PRO   B HG3  1 
ATOM   5061 H  HD2  . PRO   B 1 98  ? 36.814 -25.031 5.173   1.00 16.21 ?  98  PRO   B HD2  1 
ATOM   5062 H  HD3  . PRO   B 1 98  ? 36.154 -24.033 6.243   1.00 16.21 ?  98  PRO   B HD3  1 
ATOM   5063 N  N    . ASN   B 1 99  ? 39.891 -26.557 9.085   1.00 15.31 ?  99  ASN   B N    1 
ATOM   5064 C  CA   . ASN   B 1 99  ? 40.865 -27.631 9.249   1.00 16.01 ?  99  ASN   B CA   1 
ATOM   5065 C  C    . ASN   B 1 99  ? 40.229 -28.717 10.116  1.00 17.88 ?  99  ASN   B C    1 
ATOM   5066 O  O    . ASN   B 1 99  ? 40.148 -28.582 11.339  1.00 18.33 ?  99  ASN   B O    1 
ATOM   5067 C  CB   . ASN   B 1 99  ? 42.137 -27.083 9.879   1.00 16.35 ?  99  ASN   B CB   1 
ATOM   5068 C  CG   . ASN   B 1 99  ? 43.265 -28.091 9.878   1.00 17.22 ?  99  ASN   B CG   1 
ATOM   5069 O  OD1  . ASN   B 1 99  ? 43.040 -29.285 10.033  1.00 17.89 ?  99  ASN   B OD1  1 
ATOM   5070 N  ND2  . ASN   B 1 99  ? 44.482 -27.615 9.688   1.00 17.60 ?  99  ASN   B ND2  1 
ATOM   5071 H  H    . ASN   B 1 99  ? 39.860 -26.016 9.751   1.00 18.37 ?  99  ASN   B H    1 
ATOM   5072 H  HA   . ASN   B 1 99  ? 41.082 -28.015 8.386   1.00 19.22 ?  99  ASN   B HA   1 
ATOM   5073 H  HB2  . ASN   B 1 99  ? 42.426 -26.308 9.384   1.00 19.62 ?  99  ASN   B HB2  1 
ATOM   5074 H  HB3  . ASN   B 1 99  ? 41.946 -26.839 10.803  1.00 19.62 ?  99  ASN   B HB3  1 
ATOM   5075 H  HD21 . ASN   B 1 99  ? 45.155 -28.150 9.682   1.00 21.12 ?  99  ASN   B HD21 1 
ATOM   5076 H  HD22 . ASN   B 1 99  ? 44.597 -26.773 9.575   1.00 21.12 ?  99  ASN   B HD22 1 
ATOM   5077 N  N    A VAL   B 1 100 ? 39.769 -29.795 9.473   0.72 19.43 ?  100 VAL   B N    1 
ATOM   5078 N  N    B VAL   B 1 100 ? 39.774 -29.796 9.472   0.28 19.53 ?  100 VAL   B N    1 
ATOM   5079 C  CA   A VAL   B 1 100 ? 39.153 -30.897 10.208  0.72 21.88 ?  100 VAL   B CA   1 
ATOM   5080 C  CA   B VAL   B 1 100 ? 39.157 -30.902 10.201  0.28 21.55 ?  100 VAL   B CA   1 
ATOM   5081 C  C    A VAL   B 1 100 ? 40.156 -31.558 11.144  0.72 22.40 ?  100 VAL   B C    1 
ATOM   5082 C  C    B VAL   B 1 100 ? 40.157 -31.555 11.144  0.28 22.23 ?  100 VAL   B C    1 
ATOM   5083 O  O    A VAL   B 1 100 ? 39.781 -32.064 12.209  0.72 23.11 ?  100 VAL   B O    1 
ATOM   5084 O  O    B VAL   B 1 100 ? 39.782 -32.044 12.216  0.28 22.62 ?  100 VAL   B O    1 
ATOM   5085 C  CB   A VAL   B 1 100 ? 38.521 -31.908 9.229   0.72 24.33 ?  100 VAL   B CB   1 
ATOM   5086 C  CB   B VAL   B 1 100 ? 38.543 -31.916 9.213   0.28 23.00 ?  100 VAL   B CB   1 
ATOM   5087 C  CG1  A VAL   B 1 100 ? 38.030 -33.143 9.972   0.72 25.23 ?  100 VAL   B CG1  1 
ATOM   5088 C  CG1  B VAL   B 1 100 ? 37.993 -33.129 9.955   0.28 23.54 ?  100 VAL   B CG1  1 
ATOM   5089 C  CG2  A VAL   B 1 100 ? 37.378 -31.263 8.461   0.72 24.95 ?  100 VAL   B CG2  1 
ATOM   5090 C  CG2  B VAL   B 1 100 ? 37.451 -31.254 8.391   0.28 23.37 ?  100 VAL   B CG2  1 
ATOM   5091 H  H    A VAL   B 1 100 ? 39.796 -29.904 8.620   0.72 23.32 ?  100 VAL   B H    1 
ATOM   5092 H  H    B VAL   B 1 100 ? 39.807 -29.908 8.620   0.28 23.44 ?  100 VAL   B H    1 
ATOM   5093 H  HA   A VAL   B 1 100 ? 38.437 -30.540 10.753  0.72 26.26 ?  100 VAL   B HA   1 
ATOM   5094 H  HA   B VAL   B 1 100 ? 38.434 -30.552 10.742  0.28 25.86 ?  100 VAL   B HA   1 
ATOM   5095 H  HB   A VAL   B 1 100 ? 39.191 -32.195 8.592   0.72 29.20 ?  100 VAL   B HB   1 
ATOM   5096 H  HB   B VAL   B 1 100 ? 39.233 -32.225 8.606   0.28 27.60 ?  100 VAL   B HB   1 
ATOM   5097 H  HG11 A VAL   B 1 100 ? 37.448 -33.653 9.384   0.72 30.28 ?  100 VAL   B HG11 1 
ATOM   5098 H  HG11 B VAL   B 1 100 ? 37.438 -33.645 9.347   0.28 28.25 ?  100 VAL   B HG11 1 
ATOM   5099 H  HG12 A VAL   B 1 100 ? 38.791 -33.688 10.229  0.72 30.28 ?  100 VAL   B HG12 1 
ATOM   5100 H  HG12 B VAL   B 1 100 ? 38.732 -33.676 10.267  0.28 28.25 ?  100 VAL   B HG12 1 
ATOM   5101 H  HG13 A VAL   B 1 100 ? 37.537 -32.867 10.760  0.72 30.28 ?  100 VAL   B HG13 1 
ATOM   5102 H  HG13 B VAL   B 1 100 ? 37.462 -32.827 10.708  0.28 28.25 ?  100 VAL   B HG13 1 
ATOM   5103 H  HG21 A VAL   B 1 100 ? 37.001 -31.917 7.850   0.72 29.95 ?  100 VAL   B HG21 1 
ATOM   5104 H  HG21 B VAL   B 1 100 ? 37.056 -31.916 7.802   0.28 28.05 ?  100 VAL   B HG21 1 
ATOM   5105 H  HG22 A VAL   B 1 100 ? 36.699 -30.971 9.091   0.72 29.95 ?  100 VAL   B HG22 1 
ATOM   5106 H  HG22 B VAL   B 1 100 ? 36.776 -30.900 8.991   0.28 28.05 ?  100 VAL   B HG22 1 
ATOM   5107 H  HG23 A VAL   B 1 100 ? 37.720 -30.505 7.966   0.72 29.95 ?  100 VAL   B HG23 1 
ATOM   5108 H  HG23 B VAL   B 1 100 ? 37.840 -30.536 7.870   0.28 28.05 ?  100 VAL   B HG23 1 
ATOM   5109 N  N    . ASN   B 1 101 ? 41.437 -31.585 10.765  1.00 22.62 ?  101 ASN   B N    1 
ATOM   5110 C  CA   . ASN   B 1 101 ? 42.469 -32.122 11.649  1.00 24.90 ?  101 ASN   B CA   1 
ATOM   5111 C  C    . ASN   B 1 101 ? 42.657 -31.286 12.909  1.00 26.54 ?  101 ASN   B C    1 
ATOM   5112 O  O    . ASN   B 1 101 ? 43.297 -31.759 13.856  1.00 27.78 ?  101 ASN   B O    1 
ATOM   5113 C  CB   . ASN   B 1 101 ? 43.798 -32.256 10.899  1.00 25.01 ?  101 ASN   B CB   1 
ATOM   5114 C  CG   . ASN   B 1 101 ? 43.778 -33.381 9.883   1.00 24.80 ?  101 ASN   B CG   1 
ATOM   5115 O  OD1  . ASN   B 1 101 ? 43.098 -34.386 10.073  1.00 25.85 ?  101 ASN   B OD1  1 
ATOM   5116 N  ND2  . ASN   B 1 101 ? 44.520 -33.214 8.796   1.00 24.77 ?  101 ASN   B ND2  1 
ATOM   5117 H  H    A ASN   B 1 101 ? 41.726 -31.313 10.002  0.72 27.15 ?  101 ASN   B H    1 
ATOM   5118 H  H    B ASN   B 1 101 ? 41.727 -31.307 10.004  0.28 27.15 ?  101 ASN   B H    1 
ATOM   5119 H  HA   . ASN   B 1 101 ? 42.204 -33.007 11.931  1.00 29.89 ?  101 ASN   B HA   1 
ATOM   5120 H  HB2  . ASN   B 1 101 ? 43.989 -31.432 10.426  1.00 30.01 ?  101 ASN   B HB2  1 
ATOM   5121 H  HB3  . ASN   B 1 101 ? 44.505 -32.443 11.537  1.00 30.01 ?  101 ASN   B HB3  1 
ATOM   5122 H  HD21 . ASN   B 1 101 ? 44.541 -33.825 8.190   1.00 29.73 ?  101 ASN   B HD21 1 
ATOM   5123 H  HD22 . ASN   B 1 101 ? 44.981 -32.495 8.696   1.00 29.73 ?  101 ASN   B HD22 1 
ATOM   5124 N  N    . LYS   B 1 102 ? 42.121 -30.064 12.937  1.00 28.01 ?  102 LYS   B N    1 
ATOM   5125 C  CA   . LYS   B 1 102 ? 42.101 -29.223 14.126  1.00 30.51 ?  102 LYS   B CA   1 
ATOM   5126 C  C    . LYS   B 1 102 ? 40.724 -29.176 14.777  1.00 29.96 ?  102 LYS   B C    1 
ATOM   5127 O  O    . LYS   B 1 102 ? 40.511 -28.377 15.695  1.00 30.56 ?  102 LYS   B O    1 
ATOM   5128 C  CB   . LYS   B 1 102 ? 42.533 -27.797 13.778  1.00 33.62 ?  102 LYS   B CB   1 
ATOM   5129 C  CG   . LYS   B 1 102 ? 43.997 -27.638 13.412  1.00 36.91 ?  102 LYS   B CG   1 
ATOM   5130 C  CD   . LYS   B 1 102 ? 44.275 -26.208 12.969  1.00 39.63 ?  102 LYS   B CD   1 
ATOM   5131 C  CE   . LYS   B 1 102 ? 45.751 -25.966 12.710  1.00 41.72 ?  102 LYS   B CE   1 
ATOM   5132 N  NZ   . LYS   B 1 102 ? 46.001 -24.573 12.236  1.00 42.90 ?  102 LYS   B NZ   1 
ATOM   5133 H  H    . LYS   B 1 102 ? 41.743 -29.692 12.258  1.00 33.61 ?  102 LYS   B H    1 
ATOM   5134 H  HA   . LYS   B 1 102 ? 42.735 -29.575 14.769  1.00 36.62 ?  102 LYS   B HA   1 
ATOM   5135 H  HB2  . LYS   B 1 102 ? 42.006 -27.491 13.024  1.00 40.34 ?  102 LYS   B HB2  1 
ATOM   5136 H  HB3  . LYS   B 1 102 ? 42.360 -27.228 14.546  1.00 40.34 ?  102 LYS   B HB3  1 
ATOM   5137 H  HG2  . LYS   B 1 102 ? 44.548 -27.833 14.186  1.00 44.30 ?  102 LYS   B HG2  1 
ATOM   5138 H  HG3  . LYS   B 1 102 ? 44.215 -28.235 12.679  1.00 44.30 ?  102 LYS   B HG3  1 
ATOM   5139 H  HD2  . LYS   B 1 102 ? 43.790 -26.030 12.147  1.00 47.56 ?  102 LYS   B HD2  1 
ATOM   5140 H  HD3  . LYS   B 1 102 ? 43.985 -25.598 13.665  1.00 47.56 ?  102 LYS   B HD3  1 
ATOM   5141 H  HE2  . LYS   B 1 102 ? 46.247 -26.101 13.533  1.00 50.07 ?  102 LYS   B HE2  1 
ATOM   5142 H  HE3  . LYS   B 1 102 ? 46.061 -26.580 12.026  1.00 50.07 ?  102 LYS   B HE3  1 
ATOM   5143 H  HZ1  . LYS   B 1 102 ? 46.871 -24.453 12.091  1.00 51.48 ?  102 LYS   B HZ1  1 
ATOM   5144 H  HZ2  . LYS   B 1 102 ? 45.558 -24.426 11.478  1.00 51.48 ?  102 LYS   B HZ2  1 
ATOM   5145 H  HZ3  . LYS   B 1 102 ? 45.727 -23.989 12.850  1.00 51.48 ?  102 LYS   B HZ3  1 
ATOM   5146 N  N    A GLY   B 1 103 ? 39.787 -30.004 14.322  0.72 29.17 ?  103 GLY   B N    1 
ATOM   5147 N  N    B GLY   B 1 103 ? 39.782 -29.994 14.314  0.28 29.65 ?  103 GLY   B N    1 
ATOM   5148 C  CA   A GLY   B 1 103 ? 38.456 -30.041 14.891  0.72 28.86 ?  103 GLY   B CA   1 
ATOM   5149 C  CA   B GLY   B 1 103 ? 38.463 -30.033 14.911  0.28 29.42 ?  103 GLY   B CA   1 
ATOM   5150 C  C    A GLY   B 1 103 ? 37.522 -28.955 14.409  0.72 28.07 ?  103 GLY   B C    1 
ATOM   5151 C  C    B GLY   B 1 103 ? 37.529 -28.931 14.470  0.28 28.82 ?  103 GLY   B C    1 
ATOM   5152 O  O    A GLY   B 1 103 ? 36.401 -28.853 14.921  0.72 28.82 ?  103 GLY   B O    1 
ATOM   5153 O  O    B GLY   B 1 103 ? 36.512 -28.697 15.130  0.28 29.11 ?  103 GLY   B O    1 
ATOM   5154 H  H    A GLY   B 1 103 ? 39.903 -30.557 13.677  0.72 35.00 ?  103 GLY   B H    1 
ATOM   5155 H  H    B GLY   B 1 103 ? 39.885 -30.531 13.652  0.28 35.59 ?  103 GLY   B H    1 
ATOM   5156 H  HA2  A GLY   B 1 103 ? 38.047 -30.893 14.674  0.72 34.63 ?  103 GLY   B HA2  1 
ATOM   5157 H  HA2  B GLY   B 1 103 ? 38.049 -30.885 14.700  0.28 35.30 ?  103 GLY   B HA2  1 
ATOM   5158 H  HA3  A GLY   B 1 103 ? 38.526 -29.982 15.859  0.72 34.63 ?  103 GLY   B HA3  1 
ATOM   5159 H  HA3  B GLY   B 1 103 ? 38.551 -29.974 15.875  0.28 35.30 ?  103 GLY   B HA3  1 
ATOM   5160 N  N    A GLU   B 1 104 ? 37.937 -28.148 13.438  0.72 26.45 ?  104 GLU   B N    1 
ATOM   5161 N  N    B GLU   B 1 104 ? 37.839 -28.245 13.374  0.28 27.76 ?  104 GLU   B N    1 
ATOM   5162 C  CA   A GLU   B 1 104 ? 37.100 -27.057 12.967  0.72 24.48 ?  104 GLU   B CA   1 
ATOM   5163 C  CA   B GLU   B 1 104 ? 37.010 -27.142 12.915  0.28 26.56 ?  104 GLU   B CA   1 
ATOM   5164 C  C    A GLU   B 1 104 ? 35.929 -27.594 12.148  0.72 25.12 ?  104 GLU   B C    1 
ATOM   5165 C  C    B GLU   B 1 104 ? 35.848 -27.654 12.069  0.28 26.42 ?  104 GLU   B C    1 
ATOM   5166 O  O    A GLU   B 1 104 ? 35.986 -28.688 11.578  0.72 26.14 ?  104 GLU   B O    1 
ATOM   5167 O  O    B GLU   B 1 104 ? 35.937 -28.696 11.413  0.28 26.59 ?  104 GLU   B O    1 
ATOM   5168 C  CB   A GLU   B 1 104 ? 37.938 -26.064 12.163  0.72 23.00 ?  104 GLU   B CB   1 
ATOM   5169 C  CB   B GLU   B 1 104 ? 37.856 -26.138 12.132  0.28 25.64 ?  104 GLU   B CB   1 
ATOM   5170 C  CG   A GLU   B 1 104 ? 39.057 -25.463 13.000  0.72 21.79 ?  104 GLU   B CG   1 
ATOM   5171 C  CG   B GLU   B 1 104 ? 38.956 -25.518 12.983  0.28 24.81 ?  104 GLU   B CG   1 
ATOM   5172 C  CD   A GLU   B 1 104 ? 39.992 -24.569 12.220  0.72 20.51 ?  104 GLU   B CD   1 
ATOM   5173 C  CD   B GLU   B 1 104 ? 39.887 -24.617 12.198  0.28 24.21 ?  104 GLU   B CD   1 
ATOM   5174 O  OE1  A GLU   B 1 104 ? 39.979 -24.599 10.971  0.72 18.15 ?  104 GLU   B OE1  1 
ATOM   5175 O  OE1  B GLU   B 1 104 ? 39.816 -24.609 10.951  0.28 23.72 ?  104 GLU   B OE1  1 
ATOM   5176 O  OE2  A GLU   B 1 104 ? 40.750 -23.827 12.875  0.72 21.84 -1 104 GLU   B OE2  1 
ATOM   5177 O  OE2  B GLU   B 1 104 ? 40.695 -23.912 12.837  0.28 24.31 -1 104 GLU   B OE2  1 
ATOM   5178 H  H    A GLU   B 1 104 ? 38.697 -28.209 13.043  0.72 31.75 ?  104 GLU   B H    1 
ATOM   5179 H  H    B GLU   B 1 104 ? 38.528 -28.397 12.884  0.28 33.31 ?  104 GLU   B H    1 
ATOM   5180 H  HA   A GLU   B 1 104 ? 36.740 -26.585 13.734  0.72 29.38 ?  104 GLU   B HA   1 
ATOM   5181 H  HA   B GLU   B 1 104 ? 36.640 -26.685 13.684  0.28 31.88 ?  104 GLU   B HA   1 
ATOM   5182 H  HB2  A GLU   B 1 104 ? 38.338 -26.518 11.407  0.72 27.60 ?  104 GLU   B HB2  1 
ATOM   5183 H  HB2  B GLU   B 1 104 ? 38.274 -26.589 11.382  0.28 30.77 ?  104 GLU   B HB2  1 
ATOM   5184 H  HB3  A GLU   B 1 104 ? 37.370 -25.339 11.857  0.72 27.60 ?  104 GLU   B HB3  1 
ATOM   5185 H  HB3  B GLU   B 1 104 ? 37.284 -25.421 11.813  0.28 30.77 ?  104 GLU   B HB3  1 
ATOM   5186 H  HG2  A GLU   B 1 104 ? 38.671 -24.928 13.713  0.72 26.16 ?  104 GLU   B HG2  1 
ATOM   5187 H  HG2  B GLU   B 1 104 ? 38.549 -24.987 13.687  0.28 29.78 ?  104 GLU   B HG2  1 
ATOM   5188 H  HG3  A GLU   B 1 104 ? 39.591 -26.177 13.381  0.72 26.16 ?  104 GLU   B HG3  1 
ATOM   5189 H  HG3  B GLU   B 1 104 ? 39.489 -26.228 13.376  0.28 29.78 ?  104 GLU   B HG3  1 
ATOM   5190 N  N    A ASP   B 1 105 ? 34.855 -26.810 12.108  0.72 25.15 ?  105 ASP   B N    1 
ATOM   5191 N  N    B ASP   B 1 105 ? 34.749 -26.903 12.096  0.28 26.26 ?  105 ASP   B N    1 
ATOM   5192 C  CA   A ASP   B 1 105 ? 33.578 -27.275 11.583  0.72 25.80 ?  105 ASP   B CA   1 
ATOM   5193 C  CA   B ASP   B 1 105 ? 33.494 -27.369 11.520  0.28 26.27 ?  105 ASP   B CA   1 
ATOM   5194 C  C    A ASP   B 1 105 ? 33.618 -27.321 10.059  0.72 24.16 ?  105 ASP   B C    1 
ATOM   5195 C  C    B ASP   B 1 105 ? 33.579 -27.383 9.998   0.28 25.38 ?  105 ASP   B C    1 
ATOM   5196 O  O    A ASP   B 1 105 ? 33.759 -26.285 9.400   0.72 23.53 ?  105 ASP   B O    1 
ATOM   5197 O  O    B ASP   B 1 105 ? 33.782 -26.340 9.367   0.28 25.08 ?  105 ASP   B O    1 
ATOM   5198 C  CB   A ASP   B 1 105 ? 32.458 -26.353 12.061  0.72 28.61 ?  105 ASP   B CB   1 
ATOM   5199 C  CB   B ASP   B 1 105 ? 32.349 -26.472 11.985  0.28 27.14 ?  105 ASP   B CB   1 
ATOM   5200 C  CG   A ASP   B 1 105 ? 31.081 -26.850 11.662  0.72 30.47 ?  105 ASP   B CG   1 
ATOM   5201 C  CG   B ASP   B 1 105 ? 30.985 -27.069 11.686  0.28 27.79 ?  105 ASP   B CG   1 
ATOM   5202 O  OD1  A ASP   B 1 105 ? 30.991 -27.909 11.005  0.72 30.71 ?  105 ASP   B OD1  1 
ATOM   5203 O  OD1  B ASP   B 1 105 ? 30.920 -28.046 10.911  0.28 27.92 ?  105 ASP   B OD1  1 
ATOM   5204 O  OD2  A ASP   B 1 105 ? 30.085 -26.181 12.009  0.72 31.90 -1 105 ASP   B OD2  1 
ATOM   5205 O  OD2  B ASP   B 1 105 ? 29.980 -26.570 12.234  0.28 28.05 -1 105 ASP   B OD2  1 
ATOM   5206 H  H    A ASP   B 1 105 ? 34.845 -25.995 12.381  0.72 30.18 ?  105 ASP   B H    1 
ATOM   5207 H  H    B ASP   B 1 105 ? 34.706 -26.118 12.442  0.28 31.51 ?  105 ASP   B H    1 
ATOM   5208 H  HA   A ASP   B 1 105 ? 33.399 -28.170 11.914  0.72 30.96 ?  105 ASP   B HA   1 
ATOM   5209 H  HA   B ASP   B 1 105 ? 33.313 -28.273 11.823  0.28 31.52 ?  105 ASP   B HA   1 
ATOM   5210 H  HB2  A ASP   B 1 105 ? 32.499 -26.283 13.031  0.72 34.33 ?  105 ASP   B HB2  1 
ATOM   5211 H  HB2  B ASP   B 1 105 ? 32.419 -26.340 12.945  0.28 32.57 ?  105 ASP   B HB2  1 
ATOM   5212 H  HB3  A ASP   B 1 105 ? 32.580 -25.477 11.663  0.72 34.33 ?  105 ASP   B HB3  1 
ATOM   5213 H  HB3  B ASP   B 1 105 ? 32.411 -25.616 11.530  0.28 32.57 ?  105 ASP   B HB3  1 
ATOM   5214 N  N    A ILE   B 1 106 ? 33.474 -28.527 9.503   0.72 23.74 ?  106 ILE   B N    1 
ATOM   5215 N  N    B ILE   B 1 106 ? 33.411 -28.571 9.411   0.28 24.92 ?  106 ILE   B N    1 
ATOM   5216 C  CA   A ILE   B 1 106 ? 33.466 -28.706 8.056   0.72 23.05 ?  106 ILE   B CA   1 
ATOM   5217 C  CA   B ILE   B 1 106 ? 33.425 -28.718 7.961   0.28 24.55 ?  106 ILE   B CA   1 
ATOM   5218 C  C    A ILE   B 1 106 ? 32.363 -27.888 7.390   0.72 21.84 ?  106 ILE   B C    1 
ATOM   5219 C  C    B ILE   B 1 106 ? 32.324 -27.899 7.300   0.28 23.96 ?  106 ILE   B C    1 
ATOM   5220 O  O    A ILE   B 1 106 ? 32.458 -27.569 6.201   0.72 20.63 ?  106 ILE   B O    1 
ATOM   5221 O  O    B ILE   B 1 106 ? 32.406 -27.603 6.103   0.28 23.63 ?  106 ILE   B O    1 
ATOM   5222 C  CB   A ILE   B 1 106 ? 33.371 -30.215 7.727   0.72 23.90 ?  106 ILE   B CB   1 
ATOM   5223 C  CB   B ILE   B 1 106 ? 33.335 -30.218 7.594   0.28 24.81 ?  106 ILE   B CB   1 
ATOM   5224 C  CG1  A ILE   B 1 106 ? 33.602 -30.469 6.237   0.72 24.36 ?  106 ILE   B CG1  1 
ATOM   5225 C  CG1  B ILE   B 1 106 ? 33.597 -30.436 6.101   0.28 25.00 ?  106 ILE   B CG1  1 
ATOM   5226 C  CG2  A ILE   B 1 106 ? 32.025 -30.779 8.170   0.72 24.56 ?  106 ILE   B CG2  1 
ATOM   5227 C  CG2  B ILE   B 1 106 ? 31.978 -30.788 7.986   0.28 24.99 ?  106 ILE   B CG2  1 
ATOM   5228 C  CD1  A ILE   B 1 106 ? 34.948 -29.992 5.750   0.72 24.27 ?  106 ILE   B CD1  1 
ATOM   5229 C  CD1  B ILE   B 1 106 ? 34.953 -29.948 5.649   0.28 25.09 ?  106 ILE   B CD1  1 
ATOM   5230 H  H    A ILE   B 1 106 ? 33.387 -29.255 9.949   0.72 28.49 ?  106 ILE   B H    1 
ATOM   5231 H  H    B ILE   B 1 106 ? 33.297 -29.307 9.836   0.28 29.91 ?  106 ILE   B H    1 
ATOM   5232 H  HA   A ILE   B 1 106 ? 34.309 -28.385 7.712   0.72 27.67 ?  106 ILE   B HA   1 
ATOM   5233 H  HA   B ILE   B 1 106 ? 34.270 -28.383 7.633   0.28 29.47 ?  106 ILE   B HA   1 
ATOM   5234 H  HB   A ILE   B 1 106 ? 34.066 -30.679 8.223   0.72 28.68 ?  106 ILE   B HB   1 
ATOM   5235 H  HB   B ILE   B 1 106 ? 34.017 -30.694 8.092   0.28 29.78 ?  106 ILE   B HB   1 
ATOM   5236 H  HG12 A ILE   B 1 106 ? 33.551 -31.426 6.071   0.72 29.23 ?  106 ILE   B HG12 1 
ATOM   5237 H  HG12 B ILE   B 1 106 ? 33.549 -31.388 5.911   0.28 30.00 ?  106 ILE   B HG12 1 
ATOM   5238 H  HG13 A ILE   B 1 106 ? 32.919 -30.011 5.728   0.72 29.23 ?  106 ILE   B HG13 1 
ATOM   5239 H  HG13 B ILE   B 1 106 ? 32.924 -29.966 5.588   0.28 30.00 ?  106 ILE   B HG13 1 
ATOM   5240 H  HG21 A ILE   B 1 106 ? 32.036 -31.744 8.064   0.72 29.47 ?  106 ILE   B HG21 1 
ATOM   5241 H  HG21 B ILE   B 1 106 ? 31.996 -31.751 7.875   0.28 29.99 ?  106 ILE   B HG21 1 
ATOM   5242 H  HG22 A ILE   B 1 106 ? 31.878 -30.553 9.102   0.72 29.47 ?  106 ILE   B HG22 1 
ATOM   5243 H  HG22 B ILE   B 1 106 ? 31.800 -30.567 8.914   0.28 29.99 ?  106 ILE   B HG22 1 
ATOM   5244 H  HG23 A ILE   B 1 106 ? 31.324 -30.395 7.622   0.72 29.47 ?  106 ILE   B HG23 1 
ATOM   5245 H  HG23 B ILE   B 1 106 ? 31.294 -30.402 7.418   0.28 29.99 ?  106 ILE   B HG23 1 
ATOM   5246 H  HD11 A ILE   B 1 106 ? 35.137 -30.400 4.893   0.72 29.13 ?  106 ILE   B HD11 1 
ATOM   5247 H  HD11 B ILE   B 1 106 ? 35.155 -30.335 4.784   0.28 30.11 ?  106 ILE   B HD11 1 
ATOM   5248 H  HD12 A ILE   B 1 106 ? 34.927 -29.026 5.659   0.72 29.13 ?  106 ILE   B HD12 1 
ATOM   5249 H  HD12 B ILE   B 1 106 ? 34.934 -28.980 5.582   0.28 30.11 ?  106 ILE   B HD12 1 
ATOM   5250 H  HD13 A ILE   B 1 106 ? 35.627 -30.249 6.395   0.72 29.13 ?  106 ILE   B HD13 1 
ATOM   5251 H  HD13 B ILE   B 1 106 ? 35.620 -30.223 6.298   0.28 30.11 ?  106 ILE   B HD13 1 
ATOM   5252 N  N    A GLN   B 1 107 ? 31.319 -27.523 8.136   0.72 22.54 ?  107 GLN   B N    1 
ATOM   5253 N  N    B GLN   B 1 107 ? 31.289 -27.520 8.053   0.28 23.94 ?  107 GLN   B N    1 
ATOM   5254 C  CA   A GLN   B 1 107 ? 30.234 -26.731 7.563   0.72 22.99 ?  107 GLN   B CA   1 
ATOM   5255 C  CA   B GLN   B 1 107 ? 30.212 -26.711 7.495   0.28 23.87 ?  107 GLN   B CA   1 
ATOM   5256 C  C    A GLN   B 1 107 ? 30.711 -25.378 7.043   0.72 21.18 ?  107 GLN   B C    1 
ATOM   5257 C  C    B GLN   B 1 107 ? 30.698 -25.342 7.032   0.28 21.65 ?  107 GLN   B C    1 
ATOM   5258 O  O    A GLN   B 1 107 ? 30.063 -24.805 6.163   0.72 21.93 ?  107 GLN   B O    1 
ATOM   5259 O  O    B GLN   B 1 107 ? 30.041 -24.717 6.194   0.28 22.00 ?  107 GLN   B O    1 
ATOM   5260 C  CB   A GLN   B 1 107 ? 29.128 -26.542 8.606   0.72 26.18 ?  107 GLN   B CB   1 
ATOM   5261 C  CB   B GLN   B 1 107 ? 29.093 -26.557 8.531   0.28 26.06 ?  107 GLN   B CB   1 
ATOM   5262 C  CG   A GLN   B 1 107 ? 27.798 -26.050 8.045   0.72 29.70 ?  107 GLN   B CG   1 
ATOM   5263 C  CG   B GLN   B 1 107 ? 27.764 -26.066 7.967   0.28 28.19 ?  107 GLN   B CG   1 
ATOM   5264 C  CD   A GLN   B 1 107 ? 27.725 -24.537 7.935   0.72 32.21 ?  107 GLN   B CD   1 
ATOM   5265 C  CD   B GLN   B 1 107 ? 27.651 -24.553 7.949   0.28 29.83 ?  107 GLN   B CD   1 
ATOM   5266 O  OE1  A GLN   B 1 107 ? 28.563 -23.819 8.486   0.72 33.18 ?  107 GLN   B OE1  1 
ATOM   5267 O  OE1  B GLN   B 1 107 ? 28.486 -23.847 8.516   0.28 30.51 ?  107 GLN   B OE1  1 
ATOM   5268 N  NE2  A GLN   B 1 107 ? 26.715 -24.043 7.223   0.72 33.19 ?  107 GLN   B NE2  1 
ATOM   5269 N  NE2  B GLN   B 1 107 ? 26.609 -24.046 7.297   0.28 30.42 ?  107 GLN   B NE2  1 
ATOM   5270 H  H    A GLN   B 1 107 ? 31.218 -27.712 8.966   0.72 27.05 ?  107 GLN   B H    1 
ATOM   5271 H  H    B GLN   B 1 107 ? 31.186 -27.720 8.882   0.28 28.73 ?  107 GLN   B H    1 
ATOM   5272 H  HA   A GLN   B 1 107 ? 29.854 -27.222 6.816   0.72 27.59 ?  107 GLN   B HA   1 
ATOM   5273 H  HA   B GLN   B 1 107 ? 29.840 -27.173 6.726   0.28 28.64 ?  107 GLN   B HA   1 
ATOM   5274 H  HB2  A GLN   B 1 107 ? 28.964 -27.393 9.038   0.72 31.41 ?  107 GLN   B HB2  1 
ATOM   5275 H  HB2  B GLN   B 1 107 ? 28.931 -27.419 8.941   0.28 31.27 ?  107 GLN   B HB2  1 
ATOM   5276 H  HB3  A GLN   B 1 107 ? 29.430 -25.896 9.264   0.72 31.41 ?  107 GLN   B HB3  1 
ATOM   5277 H  HB3  B GLN   B 1 107 ? 29.379 -25.924 9.208   0.28 31.27 ?  107 GLN   B HB3  1 
ATOM   5278 H  HG2  A GLN   B 1 107 ? 27.671 -26.417 7.157   0.72 35.65 ?  107 GLN   B HG2  1 
ATOM   5279 H  HG2  B GLN   B 1 107 ? 27.669 -26.383 7.056   0.28 33.83 ?  107 GLN   B HG2  1 
ATOM   5280 H  HG3  A GLN   B 1 107 ? 27.080 -26.346 8.630   0.72 35.65 ?  107 GLN   B HG3  1 
ATOM   5281 H  HG3  B GLN   B 1 107 ? 27.040 -26.417 8.514   0.28 33.83 ?  107 GLN   B HG3  1 
ATOM   5282 H  HE21 A GLN   B 1 107 ? 26.149 -24.575 6.850   0.72 39.84 ?  107 GLN   B HE21 1 
ATOM   5283 H  HE21 B GLN   B 1 107 ? 26.046 -24.570 6.911   0.28 36.51 ?  107 GLN   B HE21 1 
ATOM   5284 H  HE22 A GLN   B 1 107 ? 26.625 -23.192 7.135   0.72 39.84 ?  107 GLN   B HE22 1 
ATOM   5285 H  HE22 B GLN   B 1 107 ? 26.498 -23.195 7.261   0.28 36.51 ?  107 GLN   B HE22 1 
ATOM   5286 N  N    . LEU   B 1 108 ? 31.834 -24.865 7.551   1.00 19.31 ?  108 LEU   B N    1 
ATOM   5287 C  CA   . LEU   B 1 108 ? 32.377 -23.569 7.140   1.00 17.41 ?  108 LEU   B CA   1 
ATOM   5288 C  C    . LEU   B 1 108 ? 33.017 -23.592 5.760   1.00 15.38 ?  108 LEU   B C    1 
ATOM   5289 O  O    . LEU   B 1 108 ? 33.447 -22.536 5.269   1.00 15.10 ?  108 LEU   B O    1 
ATOM   5290 C  CB   . LEU   B 1 108 ? 33.388 -23.088 8.178   1.00 17.96 ?  108 LEU   B CB   1 
ATOM   5291 C  CG   . LEU   B 1 108 ? 32.768 -22.635 9.499   1.00 19.52 ?  108 LEU   B CG   1 
ATOM   5292 C  CD1  . LEU   B 1 108 ? 33.808 -22.543 10.602  1.00 19.76 ?  108 LEU   B CD1  1 
ATOM   5293 C  CD2  . LEU   B 1 108 ? 32.084 -21.296 9.307   1.00 21.30 ?  108 LEU   B CD2  1 
ATOM   5294 H  H    A LEU   B 1 108 ? 32.297 -25.256 8.156   0.72 23.17 ?  108 LEU   B H    1 
ATOM   5295 H  H    B LEU   B 1 108 ? 32.296 -25.270 8.148   0.28 23.17 ?  108 LEU   B H    1 
ATOM   5296 H  HA   . LEU   B 1 108 ? 31.651 -22.930 7.113   1.00 20.89 ?  108 LEU   B HA   1 
ATOM   5297 H  HB2  . LEU   B 1 108 ? 34.000 -23.812 8.376   1.00 21.56 ?  108 LEU   B HB2  1 
ATOM   5298 H  HB3  . LEU   B 1 108 ? 33.874 -22.336 7.810   1.00 21.56 ?  108 LEU   B HB3  1 
ATOM   5299 H  HG   . LEU   B 1 108 ? 32.095 -23.279 9.775   1.00 23.42 ?  108 LEU   B HG   1 
ATOM   5300 H  HD11 . LEU   B 1 108 ? 33.367 -22.294 11.432  1.00 23.71 ?  108 LEU   B HD11 1 
ATOM   5301 H  HD12 . LEU   B 1 108 ? 34.239 -23.405 10.704  1.00 23.71 ?  108 LEU   B HD12 1 
ATOM   5302 H  HD13 . LEU   B 1 108 ? 34.463 -21.869 10.363  1.00 23.71 ?  108 LEU   B HD13 1 
ATOM   5303 H  HD21 . LEU   B 1 108 ? 31.790 -20.965 10.170  1.00 25.56 ?  108 LEU   B HD21 1 
ATOM   5304 H  HD22 . LEU   B 1 108 ? 32.715 -20.674 8.912   1.00 25.56 ?  108 LEU   B HD22 1 
ATOM   5305 H  HD23 . LEU   B 1 108 ? 31.321 -21.411 8.720   1.00 25.56 ?  108 LEU   B HD23 1 
ATOM   5306 N  N    . LEU   B 1 109 ? 33.080 -24.759 5.126   1.00 14.46 ?  109 LEU   B N    1 
ATOM   5307 C  CA   . LEU   B 1 109 ? 33.713 -24.868 3.821   1.00 13.60 ?  109 LEU   B CA   1 
ATOM   5308 C  C    . LEU   B 1 109 ? 32.949 -24.085 2.760   1.00 12.98 ?  109 LEU   B C    1 
ATOM   5309 O  O    . LEU   B 1 109 ? 33.563 -23.487 1.871   1.00 12.76 ?  109 LEU   B O    1 
ATOM   5310 C  CB   . LEU   B 1 109 ? 33.835 -26.344 3.443   1.00 13.57 ?  109 LEU   B CB   1 
ATOM   5311 C  CG   . LEU   B 1 109 ? 34.613 -26.674 2.172   1.00 13.44 ?  109 LEU   B CG   1 
ATOM   5312 C  CD1  . LEU   B 1 109 ? 35.990 -26.024 2.194   1.00 13.60 ?  109 LEU   B CD1  1 
ATOM   5313 C  CD2  . LEU   B 1 109 ? 34.726 -28.182 2.002   1.00 14.47 ?  109 LEU   B CD2  1 
ATOM   5314 H  H    . LEU   B 1 109 ? 32.771 -25.502 5.426   1.00 17.36 ?  109 LEU   B H    1 
ATOM   5315 H  HA   . LEU   B 1 109 ? 34.606 -24.500 3.872   1.00 16.33 ?  109 LEU   B HA   1 
ATOM   5316 H  HB2  . LEU   B 1 109 ? 34.274 -26.808 4.171   1.00 16.28 ?  109 LEU   B HB2  1 
ATOM   5317 H  HB3  . LEU   B 1 109 ? 32.940 -26.704 3.329   1.00 16.28 ?  109 LEU   B HB3  1 
ATOM   5318 H  HG   . LEU   B 1 109 ? 34.128 -26.330 1.403   1.00 16.13 ?  109 LEU   B HG   1 
ATOM   5319 H  HD11 . LEU   B 1 109 ? 36.524 -26.387 1.470   1.00 16.33 ?  109 LEU   B HD11 1 
ATOM   5320 H  HD12 . LEU   B 1 109 ? 35.888 -25.067 2.082   1.00 16.33 ?  109 LEU   B HD12 1 
ATOM   5321 H  HD13 . LEU   B 1 109 ? 36.415 -26.217 3.045   1.00 16.33 ?  109 LEU   B HD13 1 
ATOM   5322 H  HD21 . LEU   B 1 109 ? 35.310 -28.374 1.248   1.00 17.37 ?  109 LEU   B HD21 1 
ATOM   5323 H  HD22 . LEU   B 1 109 ? 35.095 -28.568 2.809   1.00 17.37 ?  109 LEU   B HD22 1 
ATOM   5324 H  HD23 . LEU   B 1 109 ? 33.842 -28.553 1.832   1.00 17.37 ?  109 LEU   B HD23 1 
ATOM   5325 N  N    . LYS   B 1 110 ? 31.616 -24.047 2.844   1.00 12.88 ?  110 LYS   B N    1 
ATOM   5326 C  CA   . LYS   B 1 110 ? 30.860 -23.289 1.852   1.00 12.62 ?  110 LYS   B CA   1 
ATOM   5327 C  C    . LYS   B 1 110 ? 31.194 -21.803 1.942   1.00 12.26 ?  110 LYS   B C    1 
ATOM   5328 O  O    . LYS   B 1 110 ? 31.453 -21.153 0.927   1.00 11.90 ?  110 LYS   B O    1 
ATOM   5329 C  CB   . LYS   B 1 110 ? 29.359 -23.534 2.009   1.00 13.36 ?  110 LYS   B CB   1 
ATOM   5330 C  CG   . LYS   B 1 110 ? 28.545 -22.890 0.895   1.00 13.63 ?  110 LYS   B CG   1 
ATOM   5331 C  CD   . LYS   B 1 110 ? 27.094 -23.343 0.899   1.00 13.73 ?  110 LYS   B CD   1 
ATOM   5332 C  CE   . LYS   B 1 110 ? 26.333 -22.802 -0.311  1.00 14.64 ?  110 LYS   B CE   1 
ATOM   5333 N  NZ   . LYS   B 1 110 ? 26.657 -23.512 -1.578  1.00 14.51 ?  110 LYS   B NZ   1 
ATOM   5334 H  H    . LYS   B 1 110 ? 31.146 -24.443 3.441   1.00 15.45 ?  110 LYS   B H    1 
ATOM   5335 H  HA   . LYS   B 1 110 ? 31.120 -23.595 0.965   1.00 15.14 ?  110 LYS   B HA   1 
ATOM   5336 H  HB2  . LYS   B 1 110 ? 29.193 -24.493 1.986   1.00 16.04 ?  110 LYS   B HB2  1 
ATOM   5337 H  HB3  . LYS   B 1 110 ? 29.066 -23.167 2.853   1.00 16.04 ?  110 LYS   B HB3  1 
ATOM   5338 H  HG2  . LYS   B 1 110 ? 28.555 -21.927 1.011   1.00 16.36 ?  110 LYS   B HG2  1 
ATOM   5339 H  HG3  . LYS   B 1 110 ? 28.928 -23.127 0.038   1.00 16.36 ?  110 LYS   B HG3  1 
ATOM   5340 H  HD2  . LYS   B 1 110 ? 27.057 -24.316 0.873   1.00 16.47 ?  110 LYS   B HD2  1 
ATOM   5341 H  HD3  . LYS   B 1 110 ? 26.653 -23.020 1.704   1.00 16.47 ?  110 LYS   B HD3  1 
ATOM   5342 H  HE2  . LYS   B 1 110 ? 25.380 -22.896 -0.154  1.00 17.57 ?  110 LYS   B HE2  1 
ATOM   5343 H  HE3  . LYS   B 1 110 ? 26.559 -21.868 -0.429  1.00 17.57 ?  110 LYS   B HE3  1 
ATOM   5344 H  HZ1  . LYS   B 1 110 ? 26.193 -23.162 -2.249  1.00 17.41 ?  110 LYS   B HZ1  1 
ATOM   5345 H  HZ2  . LYS   B 1 110 ? 27.526 -23.439 -1.753  1.00 17.41 ?  110 LYS   B HZ2  1 
ATOM   5346 H  HZ3  . LYS   B 1 110 ? 26.450 -24.376 -1.502  1.00 17.41 ?  110 LYS   B HZ3  1 
ATOM   5347 N  N    . SER   B 1 111 ? 31.217 -21.253 3.159   1.00 12.70 ?  111 SER   B N    1 
ATOM   5348 C  CA   . SER   B 1 111 ? 31.602 -19.854 3.337   1.00 12.38 ?  111 SER   B CA   1 
ATOM   5349 C  C    . SER   B 1 111 ? 32.984 -19.590 2.756   1.00 12.06 ?  111 SER   B C    1 
ATOM   5350 O  O    . SER   B 1 111 ? 33.212 -18.555 2.116   1.00 12.38 ?  111 SER   B O    1 
ATOM   5351 C  CB   . SER   B 1 111 ? 31.596 -19.504 4.822   1.00 13.78 ?  111 SER   B CB   1 
ATOM   5352 O  OG   . SER   B 1 111 ? 30.289 -19.492 5.342   1.00 15.48 ?  111 SER   B OG   1 
ATOM   5353 H  H    . SER   B 1 111 ? 31.015 -21.669 3.886   1.00 15.25 ?  111 SER   B H    1 
ATOM   5354 H  HA   . SER   B 1 111 ? 30.966 -19.286 2.882   1.00 14.86 ?  111 SER   B HA   1 
ATOM   5355 H  HB2  . SER   B 1 111 ? 32.115 -20.166 5.305   1.00 16.53 ?  111 SER   B HB2  1 
ATOM   5356 H  HB3  . SER   B 1 111 ? 31.984 -18.626 4.939   1.00 16.53 ?  111 SER   B HB3  1 
ATOM   5357 H  HG   . SER   B 1 111 ? 30.301 -19.297 6.164   1.00 18.58 ?  111 SER   B HG   1 
ATOM   5358 N  N    . ALA   B 1 112 ? 33.923 -20.512 2.976   1.00 12.24 ?  112 ALA   B N    1 
ATOM   5359 C  CA   . ALA   B 1 112 ? 35.267 -20.338 2.436   1.00 11.99 ?  112 ALA   B CA   1 
ATOM   5360 C  C    . ALA   B 1 112 ? 35.234 -20.238 0.914   1.00 11.31 ?  112 ALA   B C    1 
ATOM   5361 O  O    . ALA   B 1 112 ? 35.864 -19.357 0.321   1.00 11.58 ?  112 ALA   B O    1 
ATOM   5362 C  CB   . ALA   B 1 112 ? 36.174 -21.480 2.903   1.00 12.41 ?  112 ALA   B CB   1 
ATOM   5363 H  H    . ALA   B 1 112 ? 33.809 -21.236 3.436   1.00 14.69 ?  112 ALA   B H    1 
ATOM   5364 H  HA   . ALA   B 1 112 ? 35.634 -19.510 2.784   1.00 14.39 ?  112 ALA   B HA   1 
ATOM   5365 H  HB1  . ALA   B 1 112 ? 37.065 -21.340 2.542   1.00 14.90 ?  112 ALA   B HB1  1 
ATOM   5366 H  HB2  . ALA   B 1 112 ? 36.213 -21.479 3.875   1.00 14.90 ?  112 ALA   B HB2  1 
ATOM   5367 H  HB3  . ALA   B 1 112 ? 35.816 -22.321 2.588   1.00 14.90 ?  112 ALA   B HB3  1 
ATOM   5368 N  N    . TYR   B 1 113 ? 34.498 -21.137 0.259   1.00 11.54 ?  113 TYR   B N    1 
ATOM   5369 C  CA   . TYR   B 1 113 ? 34.426 -21.087 -1.195  1.00 11.10 ?  113 TYR   B CA   1 
ATOM   5370 C  C    . TYR   B 1 113 ? 33.714 -19.841 -1.712  1.00 10.74 ?  113 TYR   B C    1 
ATOM   5371 O  O    . TYR   B 1 113 ? 33.987 -19.407 -2.838  1.00 10.77 ?  113 TYR   B O    1 
ATOM   5372 C  CB   . TYR   B 1 113 ? 33.757 -22.343 -1.746  1.00 11.56 ?  113 TYR   B CB   1 
ATOM   5373 C  CG   . TYR   B 1 113 ? 34.714 -23.488 -2.019  1.00 11.84 ?  113 TYR   B CG   1 
ATOM   5374 C  CD1  . TYR   B 1 113 ? 35.701 -23.378 -2.989  1.00 12.29 ?  113 TYR   B CD1  1 
ATOM   5375 C  CD2  . TYR   B 1 113 ? 34.614 -24.686 -1.323  1.00 12.40 ?  113 TYR   B CD2  1 
ATOM   5376 C  CE1  . TYR   B 1 113 ? 36.575 -24.411 -3.243  1.00 12.32 ?  113 TYR   B CE1  1 
ATOM   5377 C  CE2  . TYR   B 1 113 ? 35.483 -25.738 -1.576  1.00 12.38 ?  113 TYR   B CE2  1 
ATOM   5378 C  CZ   . TYR   B 1 113 ? 36.457 -25.593 -2.543  1.00 12.32 ?  113 TYR   B CZ   1 
ATOM   5379 O  OH   . TYR   B 1 113 ? 37.334 -26.606 -2.829  1.00 12.96 ?  113 TYR   B OH   1 
ATOM   5380 H  H    . TYR   B 1 113 ? 34.036 -21.767 0.631   1.00 13.85 ?  113 TYR   B H    1 
ATOM   5381 H  HA   . TYR   B 1 113 ? 35.328 -21.065 -1.534  1.00 13.32 ?  113 TYR   B HA   1 
ATOM   5382 H  HB2  . TYR   B 1 113 ? 33.100 -22.662 -1.105  1.00 13.87 ?  113 TYR   B HB2  1 
ATOM   5383 H  HB3  . TYR   B 1 113 ? 33.316 -22.122 -2.581  1.00 13.87 ?  113 TYR   B HB3  1 
ATOM   5384 H  HD1  . TYR   B 1 113 ? 35.786 -22.582 -3.470  1.00 14.75 ?  113 TYR   B HD1  1 
ATOM   5385 H  HD2  . TYR   B 1 113 ? 33.954 -24.781 -0.680  1.00 14.89 ?  113 TYR   B HD2  1 
ATOM   5386 H  HE1  . TYR   B 1 113 ? 37.230 -24.316 -3.905  1.00 14.78 ?  113 TYR   B HE1  1 
ATOM   5387 H  HE2  . TYR   B 1 113 ? 35.401 -26.531 -1.110  1.00 14.86 ?  113 TYR   B HE2  1 
ATOM   5388 H  HH   . TYR   B 1 113 ? 37.158 -27.276 -2.350  1.00 15.55 ?  113 TYR   B HH   1 
ATOM   5389 N  N    . GLU   B 1 114 ? 32.791 -19.266 -0.933  1.00 10.86 ?  114 GLU   B N    1 
ATOM   5390 C  CA   . GLU   B 1 114 ? 32.110 -18.057 -1.386  1.00 10.95 ?  114 GLU   B CA   1 
ATOM   5391 C  C    . GLU   B 1 114 ? 33.094 -16.936 -1.682  1.00 10.80 ?  114 GLU   B C    1 
ATOM   5392 O  O    . GLU   B 1 114 ? 32.813 -16.076 -2.522  1.00 10.86 ?  114 GLU   B O    1 
ATOM   5393 C  CB   . GLU   B 1 114 ? 31.048 -17.630 -0.369  1.00 11.28 ?  114 GLU   B CB   1 
ATOM   5394 C  CG   . GLU   B 1 114 ? 29.844 -18.555 -0.428  1.00 11.51 ?  114 GLU   B CG   1 
ATOM   5395 C  CD   . GLU   B 1 114 ? 28.829 -18.378 0.682   1.00 11.45 ?  114 GLU   B CD   1 
ATOM   5396 O  OE1  . GLU   B 1 114 ? 29.116 -17.758 1.727   1.00 11.84 ?  114 GLU   B OE1  1 
ATOM   5397 O  OE2  . GLU   B 1 114 ? 27.705 -18.911 0.513   1.00 12.33 -1 114 GLU   B OE2  1 
ATOM   5398 H  H    . GLU   B 1 114 ? 32.535 -19.560 -0.160  1.00 13.03 ?  114 GLU   B H    1 
ATOM   5399 H  HA   . GLU   B 1 114 ? 31.650 -18.257 -2.210  1.00 13.14 ?  114 GLU   B HA   1 
ATOM   5400 H  HB2  . GLU   B 1 114 ? 31.422 -17.672 0.528   1.00 13.54 ?  114 GLU   B HB2  1 
ATOM   5401 H  HB3  . GLU   B 1 114 ? 30.752 -16.731 -0.569  1.00 13.54 ?  114 GLU   B HB3  1 
ATOM   5402 H  HG2  . GLU   B 1 114 ? 29.391 -18.411 -1.268  1.00 13.81 ?  114 GLU   B HG2  1 
ATOM   5403 H  HG3  . GLU   B 1 114 ? 30.164 -19.473 -0.384  1.00 13.81 ?  114 GLU   B HG3  1 
ATOM   5404 N  N    . ASN   B 1 115 ? 34.255 -16.932 -1.027  1.00 10.67 ?  115 ASN   B N    1 
ATOM   5405 C  CA   . ASN   B 1 115 ? 35.244 -15.903 -1.325  1.00 10.68 ?  115 ASN   B CA   1 
ATOM   5406 C  C    . ASN   B 1 115 ? 35.650 -15.921 -2.790  1.00 10.58 ?  115 ASN   B C    1 
ATOM   5407 O  O    . ASN   B 1 115 ? 36.034 -14.880 -3.341  1.00 11.06 ?  115 ASN   B O    1 
ATOM   5408 C  CB   . ASN   B 1 115 ? 36.485 -16.088 -0.454  1.00 11.24 ?  115 ASN   B CB   1 
ATOM   5409 C  CG   . ASN   B 1 115 ? 36.226 -15.824 1.008   1.00 11.67 ?  115 ASN   B CG   1 
ATOM   5410 O  OD1  . ASN   B 1 115 ? 36.236 -14.680 1.448   1.00 13.29 ?  115 ASN   B OD1  1 
ATOM   5411 N  ND2  . ASN   B 1 115 ? 36.063 -16.888 1.787   1.00 12.08 ?  115 ASN   B ND2  1 
ATOM   5412 H  H    . ASN   B 1 115 ? 34.489 -17.494 -0.411  1.00 12.80 ?  115 ASN   B H    1 
ATOM   5413 H  HA   . ASN   B 1 115 ? 34.871 -15.030 -1.125  1.00 12.82 ?  115 ASN   B HA   1 
ATOM   5414 H  HB2  . ASN   B 1 115 ? 36.801 -17.000 -0.542  1.00 13.50 ?  115 ASN   B HB2  1 
ATOM   5415 H  HB3  . ASN   B 1 115 ? 37.174 -15.470 -0.748  1.00 13.50 ?  115 ASN   B HB3  1 
ATOM   5416 H  HD21 . ASN   B 1 115 ? 35.927 -16.785 2.632   1.00 14.50 ?  115 ASN   B HD21 1 
ATOM   5417 H  HD22 . ASN   B 1 115 ? 36.079 -17.676 1.449   1.00 14.50 ?  115 ASN   B HD22 1 
ATOM   5418 N  N    . PHE   B 1 116 ? 35.625 -17.096 -3.429  1.00 10.40 ?  116 PHE   B N    1 
ATOM   5419 C  CA   . PHE   B 1 116 ? 36.055 -17.181 -4.820  1.00 10.70 ?  116 PHE   B CA   1 
ATOM   5420 C  C    . PHE   B 1 116 ? 35.150 -16.354 -5.725  1.00 10.69 ?  116 PHE   B C    1 
ATOM   5421 O  O    . PHE   B 1 116 ? 35.578 -15.927 -6.798  1.00 10.96 ?  116 PHE   B O    1 
ATOM   5422 C  CB   . PHE   B 1 116 ? 36.021 -18.624 -5.351  1.00 10.62 ?  116 PHE   B CB   1 
ATOM   5423 C  CG   . PHE   B 1 116 ? 37.090 -19.577 -4.810  1.00 10.34 ?  116 PHE   B CG   1 
ATOM   5424 C  CD1  . PHE   B 1 116 ? 37.743 -19.386 -3.606  1.00 11.12 ?  116 PHE   B CD1  1 
ATOM   5425 C  CD2  . PHE   B 1 116 ? 37.390 -20.714 -5.547  1.00 10.76 ?  116 PHE   B CD2  1 
ATOM   5426 C  CE1  . PHE   B 1 116 ? 38.674 -20.322 -3.152  1.00 11.37 ?  116 PHE   B CE1  1 
ATOM   5427 C  CE2  . PHE   B 1 116 ? 38.322 -21.645 -5.099  1.00 10.96 ?  116 PHE   B CE2  1 
ATOM   5428 C  CZ   . PHE   B 1 116 ? 38.959 -21.445 -3.909  1.00 11.06 ?  116 PHE   B CZ   1 
ATOM   5429 H  H    . PHE   B 1 116 ? 35.359 -17.843 -3.085  1.00 12.49 ?  116 PHE   B H    1 
ATOM   5430 H  HA   . PHE   B 1 116 ? 36.959 -16.850 -4.902  1.00 12.85 ?  116 PHE   B HA   1 
ATOM   5431 H  HB2  . PHE   B 1 116 ? 35.152 -19.009 -5.136  1.00 12.75 ?  116 PHE   B HB2  1 
ATOM   5432 H  HB3  . PHE   B 1 116 ? 36.119 -18.597 -6.318  1.00 12.75 ?  116 PHE   B HB3  1 
ATOM   5433 H  HD1  . PHE   B 1 116 ? 37.549 -18.637 -3.091  1.00 13.35 ?  116 PHE   B HD1  1 
ATOM   5434 H  HD2  . PHE   B 1 116 ? 36.948 -20.866 -6.353  1.00 12.91 ?  116 PHE   B HD2  1 
ATOM   5435 H  HE1  . PHE   B 1 116 ? 39.121 -20.181 -2.347  1.00 13.64 ?  116 PHE   B HE1  1 
ATOM   5436 H  HE2  . PHE   B 1 116 ? 38.511 -22.396 -5.610  1.00 13.16 ?  116 PHE   B HE2  1 
ATOM   5437 H  HZ   . PHE   B 1 116 ? 39.595 -22.054 -3.611  1.00 13.27 ?  116 PHE   B HZ   1 
ATOM   5438 N  N    . ASN   B 1 117 ? 33.884 -16.163 -5.336  1.00 11.00 ?  117 ASN   B N    1 
ATOM   5439 C  CA   . ASN   B 1 117 ? 32.935 -15.456 -6.198  1.00 11.25 ?  117 ASN   B CA   1 
ATOM   5440 C  C    . ASN   B 1 117 ? 33.246 -13.978 -6.348  1.00 11.30 ?  117 ASN   B C    1 
ATOM   5441 O  O    . ASN   B 1 117 ? 32.643 -13.324 -7.204  1.00 12.27 ?  117 ASN   B O    1 
ATOM   5442 C  CB   . ASN   B 1 117 ? 31.508 -15.674 -5.716  1.00 11.64 ?  117 ASN   B CB   1 
ATOM   5443 C  CG   . ASN   B 1 117 ? 31.065 -17.088 -5.962  1.00 11.70 ?  117 ASN   B CG   1 
ATOM   5444 O  OD1  . ASN   B 1 117 ? 31.419 -17.682 -6.985  1.00 12.31 ?  117 ASN   B OD1  1 
ATOM   5445 N  ND2  . ASN   B 1 117 ? 30.336 -17.657 -5.019  1.00 11.34 ?  117 ASN   B ND2  1 
ATOM   5446 H  H    . ASN   B 1 117 ? 33.558 -16.426 -4.580  1.00 13.20 ?  117 ASN   B H    1 
ATOM   5447 H  HA   . ASN   B 1 117 ? 32.998 -15.848 -7.076  1.00 13.50 ?  117 ASN   B HA   1 
ATOM   5448 H  HB2  . ASN   B 1 117 ? 31.456 -15.504 -4.758  1.00 13.97 ?  117 ASN   B HB2  1 
ATOM   5449 H  HB3  . ASN   B 1 117 ? 30.912 -15.075 -6.192  1.00 13.97 ?  117 ASN   B HB3  1 
ATOM   5450 H  HD21 . ASN   B 1 117 ? 30.063 -18.465 -5.115  1.00 13.61 ?  117 ASN   B HD21 1 
ATOM   5451 H  HD22 . ASN   B 1 117 ? 30.117 -17.211 -4.313  1.00 13.61 ?  117 ASN   B HD22 1 
ATOM   5452 N  N    . GLN   B 1 118 ? 34.179 -13.451 -5.566  1.00 11.01 ?  118 GLN   B N    1 
ATOM   5453 C  CA   . GLN   B 1 118 ? 34.605 -12.065 -5.709  1.00 11.34 ?  118 GLN   B CA   1 
ATOM   5454 C  C    . GLN   B 1 118 ? 35.672 -11.873 -6.782  1.00 11.44 ?  118 GLN   B C    1 
ATOM   5455 O  O    . GLN   B 1 118 ? 36.143 -10.745 -6.964  1.00 12.84 ?  118 GLN   B O    1 
ATOM   5456 C  CB   . GLN   B 1 118 ? 35.090 -11.531 -4.360  1.00 11.97 ?  118 GLN   B CB   1 
ATOM   5457 C  CG   . GLN   B 1 118 ? 34.013 -11.561 -3.290  1.00 12.26 ?  118 GLN   B CG   1 
ATOM   5458 C  CD   . GLN   B 1 118 ? 32.840 -10.666 -3.631  1.00 12.06 ?  118 GLN   B CD   1 
ATOM   5459 O  OE1  . GLN   B 1 118 ? 33.018 -9.525  -4.070  1.00 12.85 ?  118 GLN   B OE1  1 
ATOM   5460 N  NE2  . GLN   B 1 118 ? 31.629 -11.165 -3.423  1.00 12.66 ?  118 GLN   B NE2  1 
ATOM   5461 H  H    . GLN   B 1 118 ? 34.595 -13.875 -4.935  1.00 13.22 ?  118 GLN   B H    1 
ATOM   5462 H  HA   . GLN   B 1 118 ? 33.837 -11.537 -5.973  1.00 13.61 ?  118 GLN   B HA   1 
ATOM   5463 H  HB2  . GLN   B 1 118 ? 35.832 -12.067 -4.050  1.00 14.37 ?  118 GLN   B HB2  1 
ATOM   5464 H  HB3  . GLN   B 1 118 ? 35.371 -10.605 -4.466  1.00 14.37 ?  118 GLN   B HB3  1 
ATOM   5465 H  HG2  . GLN   B 1 118 ? 33.683 -12.468 -3.197  1.00 14.72 ?  118 GLN   B HG2  1 
ATOM   5466 H  HG3  . GLN   B 1 118 ? 34.390 -11.257 -2.449  1.00 14.72 ?  118 GLN   B HG3  1 
ATOM   5467 H  HE21 . GLN   B 1 118 ? 31.544 -11.962 -3.109  1.00 15.19 ?  118 GLN   B HE21 1 
ATOM   5468 H  HE22 . GLN   B 1 118 ? 30.938 -10.693 -3.601  1.00 15.19 ?  118 GLN   B HE22 1 
ATOM   5469 N  N    . HIS   B 1 119 ? 36.028 -12.926 -7.514  1.00 11.21 ?  119 HIS   B N    1 
ATOM   5470 C  CA   . HIS   B 1 119 ? 37.061 -12.875 -8.540  1.00 11.53 ?  119 HIS   B CA   1 
ATOM   5471 C  C    . HIS   B 1 119 ? 36.580 -13.612 -9.776  1.00 11.68 ?  119 HIS   B C    1 
ATOM   5472 O  O    . HIS   B 1 119 ? 36.079 -14.732 -9.669  1.00 12.42 ?  119 HIS   B O    1 
ATOM   5473 C  CB   . HIS   B 1 119 ? 38.341 -13.502 -7.998  1.00 12.25 ?  119 HIS   B CB   1 
ATOM   5474 C  CG   . HIS   B 1 119 ? 38.835 -12.793 -6.785  1.00 13.55 ?  119 HIS   B CG   1 
ATOM   5475 N  ND1  . HIS   B 1 119 ? 39.625 -11.665 -6.857  1.00 15.16 ?  119 HIS   B ND1  1 
ATOM   5476 C  CD2  . HIS   B 1 119 ? 38.559 -12.979 -5.474  1.00 14.50 ?  119 HIS   B CD2  1 
ATOM   5477 C  CE1  . HIS   B 1 119 ? 39.849 -11.215 -5.637  1.00 16.14 ?  119 HIS   B CE1  1 
ATOM   5478 N  NE2  . HIS   B 1 119 ? 39.205 -11.987 -4.781  1.00 15.99 ?  119 HIS   B NE2  1 
ATOM   5479 H  H    . HIS   B 1 119 ? 35.663 -13.706 -7.440  1.00 13.45 ?  119 HIS   B H    1 
ATOM   5480 H  HA   . HIS   B 1 119 ? 37.236 -11.951 -8.780  1.00 13.84 ?  119 HIS   B HA   1 
ATOM   5481 H  HB2  . HIS   B 1 119 ? 38.167 -14.425 -7.763  1.00 14.70 ?  119 HIS   B HB2  1 
ATOM   5482 H  HB3  . HIS   B 1 119 ? 39.029 -13.452 -8.680  1.00 14.70 ?  119 HIS   B HB3  1 
ATOM   5483 H  HD2  . HIS   B 1 119 ? 38.032 -13.657 -5.112  1.00 17.40 ?  119 HIS   B HD2  1 
ATOM   5484 H  HE1  . HIS   B 1 119 ? 40.376 -10.482 -5.416  1.00 19.37 ?  119 HIS   B HE1  1 
ATOM   5485 H  HE2  . HIS   B 1 119 ? 39.219 -11.905 -3.925  1.00 19.19 ?  119 HIS   B HE2  1 
ATOM   5486 N  N    . GLU   B 1 120 ? 36.733 -12.997 -10.947 1.00 12.10 ?  120 GLU   B N    1 
ATOM   5487 C  CA   . GLU   B 1 120 ? 36.139 -13.576 -12.145 1.00 13.42 ?  120 GLU   B CA   1 
ATOM   5488 C  C    . GLU   B 1 120 ? 36.816 -14.874 -12.558 1.00 12.26 ?  120 GLU   B C    1 
ATOM   5489 O  O    . GLU   B 1 120 ? 36.154 -15.744 -13.132 1.00 12.66 ?  120 GLU   B O    1 
ATOM   5490 C  CB   . GLU   B 1 120 ? 36.148 -12.570 -13.294 1.00 17.46 ?  120 GLU   B CB   1 
ATOM   5491 C  CG   . GLU   B 1 120 ? 35.208 -11.403 -13.062 1.00 22.86 ?  120 GLU   B CG   1 
ATOM   5492 C  CD   . GLU   B 1 120 ? 35.026 -10.536 -14.286 1.00 27.57 ?  120 GLU   B CD   1 
ATOM   5493 O  OE1  . GLU   B 1 120 ? 36.022 -10.307 -15.006 1.00 29.54 ?  120 GLU   B OE1  1 
ATOM   5494 O  OE2  . GLU   B 1 120 ? 33.887 -10.084 -14.523 1.00 30.36 -1 120 GLU   B OE2  1 
ATOM   5495 H  H    . GLU   B 1 120 ? 37.163 -12.261 -11.076 1.00 14.53 ?  120 GLU   B H    1 
ATOM   5496 H  HA   . GLU   B 1 120 ? 35.217 -13.791 -11.958 1.00 16.11 ?  120 GLU   B HA   1 
ATOM   5497 H  HB2  . GLU   B 1 120 ? 37.043 -12.216 -13.402 1.00 20.96 ?  120 GLU   B HB2  1 
ATOM   5498 H  HB3  . GLU   B 1 120 ? 35.870 -13.019 -14.111 1.00 20.96 ?  120 GLU   B HB3  1 
ATOM   5499 H  HG2  . GLU   B 1 120 ? 34.336 -11.746 -12.807 1.00 27.44 ?  120 GLU   B HG2  1 
ATOM   5500 H  HG3  . GLU   B 1 120 ? 35.566 -10.846 -12.357 1.00 27.44 ?  120 GLU   B HG3  1 
ATOM   5501 N  N    . VAL   B 1 121 ? 38.117 -15.013 -12.301 1.00 11.81 ?  121 VAL   B N    1 
ATOM   5502 C  CA   . VAL   B 1 121 ? 38.861 -16.222 -12.649 1.00 12.05 ?  121 VAL   B CA   1 
ATOM   5503 C  C    . VAL   B 1 121 ? 39.978 -16.423 -11.632 1.00 11.51 ?  121 VAL   B C    1 
ATOM   5504 O  O    . VAL   B 1 121 ? 40.654 -15.465 -11.237 1.00 12.06 ?  121 VAL   B O    1 
ATOM   5505 C  CB   . VAL   B 1 121 ? 39.371 -16.185 -14.110 1.00 13.71 ?  121 VAL   B CB   1 
ATOM   5506 C  CG1  . VAL   B 1 121 ? 40.232 -14.956 -14.380 1.00 14.77 ?  121 VAL   B CG1  1 
ATOM   5507 C  CG2  . VAL   B 1 121 ? 40.109 -17.470 -14.455 1.00 15.07 ?  121 VAL   B CG2  1 
ATOM   5508 H  H    . VAL   B 1 121 ? 38.602 -14.410 -11.920 1.00 14.17 ?  121 VAL   B H    1 
ATOM   5509 H  HA   . VAL   B 1 121 ? 38.257 -16.975 -12.574 1.00 14.46 ?  121 VAL   B HA   1 
ATOM   5510 H  HB   . VAL   B 1 121 ? 38.600 -16.134 -14.699 1.00 16.46 ?  121 VAL   B HB   1 
ATOM   5511 H  HG11 . VAL   B 1 121 ? 40.535 -14.981 -15.303 1.00 17.72 ?  121 VAL   B HG11 1 
ATOM   5512 H  HG12 . VAL   B 1 121 ? 39.699 -14.160 -14.230 1.00 17.72 ?  121 VAL   B HG12 1 
ATOM   5513 H  HG13 . VAL   B 1 121 ? 40.993 -14.966 -13.782 1.00 17.72 ?  121 VAL   B HG13 1 
ATOM   5514 H  HG21 . VAL   B 1 121 ? 40.303 -17.476 -15.407 1.00 18.09 ?  121 VAL   B HG21 1 
ATOM   5515 H  HG22 . VAL   B 1 121 ? 40.936 -17.507 -13.952 1.00 18.09 ?  121 VAL   B HG22 1 
ATOM   5516 H  HG23 . VAL   B 1 121 ? 39.548 -18.229 -14.230 1.00 18.09 ?  121 VAL   B HG23 1 
ATOM   5517 N  N    . LEU   B 1 122 ? 40.166 -17.675 -11.200 1.00 11.30 ?  122 LEU   B N    1 
ATOM   5518 C  CA   . LEU   B 1 122 ? 41.149 -18.021 -10.175 1.00 10.87 ?  122 LEU   B CA   1 
ATOM   5519 C  C    . LEU   B 1 122 ? 41.805 -19.351 -10.503 1.00 10.88 ?  122 LEU   B C    1 
ATOM   5520 O  O    . LEU   B 1 122 ? 41.147 -20.270 -11.006 1.00 11.90 ?  122 LEU   B O    1 
ATOM   5521 C  CB   . LEU   B 1 122 ? 40.507 -18.252 -8.799  1.00 12.28 ?  122 LEU   B CB   1 
ATOM   5522 C  CG   . LEU   B 1 122 ? 39.472 -17.235 -8.314  1.00 12.49 ?  122 LEU   B CG   1 
ATOM   5523 C  CD1  . LEU   B 1 122 ? 38.069 -17.591 -8.791  1.00 13.44 ?  122 LEU   B CD1  1 
ATOM   5524 C  CD2  . LEU   B 1 122 ? 39.520 -17.126 -6.807  1.00 12.14 ?  122 LEU   B CD2  1 
ATOM   5525 H  H    . LEU   B 1 122 ? 39.733 -18.355 -11.495 1.00 13.57 ?  122 LEU   B H    1 
ATOM   5526 H  HA   . LEU   B 1 122 ? 41.831 -17.330 -10.103 1.00 13.05 ?  122 LEU   B HA   1 
ATOM   5527 H  HB2  . LEU   B 1 122 ? 40.068 -19.113 -8.817  1.00 14.74 ?  122 LEU   B HB2  1 
ATOM   5528 H  HB3  . LEU   B 1 122 ? 41.216 -18.268 -8.137  1.00 14.74 ?  122 LEU   B HB3  1 
ATOM   5529 H  HG   . LEU   B 1 122 ? 39.695 -16.363 -8.677  1.00 14.99 ?  122 LEU   B HG   1 
ATOM   5530 H  HD11 . LEU   B 1 122 ? 37.439 -16.954 -8.424  1.00 16.14 ?  122 LEU   B HD11 1 
ATOM   5531 H  HD12 . LEU   B 1 122 ? 38.047 -17.555 -9.762  1.00 16.14 ?  122 LEU   B HD12 1 
ATOM   5532 H  HD13 . LEU   B 1 122 ? 37.851 -18.486 -8.489  1.00 16.14 ?  122 LEU   B HD13 1 
ATOM   5533 H  HD21 . LEU   B 1 122 ? 38.838 -16.507 -6.507  1.00 14.57 ?  122 LEU   B HD21 1 
ATOM   5534 H  HD22 . LEU   B 1 122 ? 39.368 -18.002 -6.419  1.00 14.57 ?  122 LEU   B HD22 1 
ATOM   5535 H  HD23 . LEU   B 1 122 ? 40.399 -16.799 -6.540  1.00 14.57 ?  122 LEU   B HD23 1 
ATOM   5536 N  N    . LEU   B 1 123 ? 43.092 -19.454 -10.153 1.00 10.75 ?  123 LEU   B N    1 
ATOM   5537 C  CA   . LEU   B 1 123 ? 43.803 -20.724 -10.035 1.00 10.80 ?  123 LEU   B CA   1 
ATOM   5538 C  C    . LEU   B 1 123 ? 43.775 -21.120 -8.565  1.00 10.57 ?  123 LEU   B C    1 
ATOM   5539 O  O    . LEU   B 1 123 ? 44.119 -20.294 -7.709  1.00 10.74 ?  123 LEU   B O    1 
ATOM   5540 C  CB   . LEU   B 1 123 ? 45.249 -20.537 -10.495 1.00 11.09 ?  123 LEU   B CB   1 
ATOM   5541 C  CG   . LEU   B 1 123 ? 46.189 -21.723 -10.266 1.00 11.58 ?  123 LEU   B CG   1 
ATOM   5542 C  CD1  . LEU   B 1 123 ? 45.762 -22.950 -11.063 1.00 12.15 ?  123 LEU   B CD1  1 
ATOM   5543 C  CD2  . LEU   B 1 123 ? 47.613 -21.331 -10.618 1.00 12.41 ?  123 LEU   B CD2  1 
ATOM   5544 H  H    . LEU   B 1 123 ? 43.590 -18.775 -9.961  1.00 12.90 ?  123 LEU   B H    1 
ATOM   5545 H  HA   . LEU   B 1 123 ? 43.370 -21.409 -10.569 1.00 12.97 ?  123 LEU   B HA   1 
ATOM   5546 H  HB2  . LEU   B 1 123 ? 45.243 -20.355 -11.448 1.00 13.32 ?  123 LEU   B HB2  1 
ATOM   5547 H  HB3  . LEU   B 1 123 ? 45.624 -19.779 -10.024 1.00 13.32 ?  123 LEU   B HB3  1 
ATOM   5548 H  HG   . LEU   B 1 123 ? 46.176 -21.965 -9.327  1.00 13.89 ?  123 LEU   B HG   1 
ATOM   5549 H  HD11 . LEU   B 1 123 ? 46.398 -23.664 -10.907 1.00 14.58 ?  123 LEU   B HD11 1 
ATOM   5550 H  HD12 . LEU   B 1 123 ? 44.878 -23.223 -10.772 1.00 14.58 ?  123 LEU   B HD12 1 
ATOM   5551 H  HD13 . LEU   B 1 123 ? 45.745 -22.721 -12.006 1.00 14.58 ?  123 LEU   B HD13 1 
ATOM   5552 H  HD21 . LEU   B 1 123 ? 48.197 -22.091 -10.468 1.00 14.89 ?  123 LEU   B HD21 1 
ATOM   5553 H  HD22 . LEU   B 1 123 ? 47.646 -21.065 -11.549 1.00 14.89 ?  123 LEU   B HD22 1 
ATOM   5554 H  HD23 . LEU   B 1 123 ? 47.883 -20.591 -10.051 1.00 14.89 ?  123 LEU   B HD23 1 
ATOM   5555 N  N    . ALA   B 1 124 ? 43.351 -22.351 -8.257  1.00 10.46 ?  124 ALA   B N    1 
ATOM   5556 C  CA   . ALA   B 1 124 ? 43.087 -22.666 -6.860  1.00 10.73 ?  124 ALA   B CA   1 
ATOM   5557 C  C    . ALA   B 1 124 ? 43.366 -24.125 -6.537  1.00 10.59 ?  124 ALA   B C    1 
ATOM   5558 O  O    . ALA   B 1 124 ? 43.231 -25.003 -7.401  1.00 11.02 ?  124 ALA   B O    1 
ATOM   5559 C  CB   . ALA   B 1 124 ? 41.634 -22.359 -6.490  1.00 11.14 ?  124 ALA   B CB   1 
ATOM   5560 H  H    . ALA   B 1 124 ? 43.194 -22.986 -8.820  1.00 12.55 ?  124 ALA   B H    1 
ATOM   5561 H  HA   . ALA   B 1 124 ? 43.662 -22.116 -6.315  1.00 12.88 ?  124 ALA   B HA   1 
ATOM   5562 H  HB1  . ALA   B 1 124 ? 41.487 -22.580 -5.559  1.00 13.37 ?  124 ALA   B HB1  1 
ATOM   5563 H  HB2  . ALA   B 1 124 ? 41.466 -21.412 -6.636  1.00 13.37 ?  124 ALA   B HB2  1 
ATOM   5564 H  HB3  . ALA   B 1 124 ? 41.042 -22.886 -7.053  1.00 13.37 ?  124 ALA   B HB3  1 
ATOM   5565 N  N    . PRO   B 1 125 ? 43.653 -24.419 -5.272  1.00 10.48 ?  125 PRO   B N    1 
ATOM   5566 C  CA   . PRO   B 1 125 ? 43.601 -25.786 -4.756  1.00 11.54 ?  125 PRO   B CA   1 
ATOM   5567 C  C    . PRO   B 1 125 ? 42.202 -26.062 -4.211  1.00 11.45 ?  125 PRO   B C    1 
ATOM   5568 O  O    . PRO   B 1 125 ? 41.405 -25.145 -4.006  1.00 11.85 ?  125 PRO   B O    1 
ATOM   5569 C  CB   . PRO   B 1 125 ? 44.591 -25.708 -3.587  1.00 12.54 ?  125 PRO   B CB   1 
ATOM   5570 C  CG   . PRO   B 1 125 ? 44.328 -24.324 -3.009  1.00 12.13 ?  125 PRO   B CG   1 
ATOM   5571 C  CD   . PRO   B 1 125 ? 43.988 -23.452 -4.208  1.00 11.21 ?  125 PRO   B CD   1 
ATOM   5572 H  HA   . PRO   B 1 125 ? 43.874 -26.448 -5.408  1.00 13.85 ?  125 PRO   B HA   1 
ATOM   5573 H  HB2  . PRO   B 1 125 ? 44.392 -26.399 -2.931  1.00 15.05 ?  125 PRO   B HB2  1 
ATOM   5574 H  HB3  . PRO   B 1 125 ? 45.500 -25.785 -3.909  1.00 15.05 ?  125 PRO   B HB3  1 
ATOM   5575 H  HG2  . PRO   B 1 125 ? 43.582 -24.358 -2.388  1.00 14.56 ?  125 PRO   B HG2  1 
ATOM   5576 H  HG3  . PRO   B 1 125 ? 45.128 -23.998 -2.558  1.00 14.56 ?  125 PRO   B HG3  1 
ATOM   5577 H  HD2  . PRO   B 1 125 ? 43.231 -22.880 -4.012  1.00 13.45 ?  125 PRO   B HD2  1 
ATOM   5578 H  HD3  . PRO   B 1 125 ? 44.767 -22.922 -4.470  1.00 13.45 ?  125 PRO   B HD3  1 
ATOM   5579 N  N    . LEU   B 1 126 ? 41.935 -27.340 -3.936  1.00 11.95 ?  126 LEU   B N    1 
ATOM   5580 C  CA   . LEU   B 1 126 ? 40.714 -27.713 -3.230  1.00 12.45 ?  126 LEU   B CA   1 
ATOM   5581 C  C    . LEU   B 1 126 ? 40.829 -27.313 -1.768  1.00 12.66 ?  126 LEU   B C    1 
ATOM   5582 O  O    . LEU   B 1 126 ? 41.728 -27.765 -1.052  1.00 14.05 ?  126 LEU   B O    1 
ATOM   5583 C  CB   . LEU   B 1 126 ? 40.469 -29.211 -3.352  1.00 13.83 ?  126 LEU   B CB   1 
ATOM   5584 C  CG   . LEU   B 1 126 ? 39.929 -29.679 -4.705  1.00 14.58 ?  126 LEU   B CG   1 
ATOM   5585 C  CD1  . LEU   B 1 126 ? 39.987 -31.189 -4.811  1.00 16.09 ?  126 LEU   B CD1  1 
ATOM   5586 C  CD2  . LEU   B 1 126 ? 38.506 -29.183 -4.917  1.00 15.10 ?  126 LEU   B CD2  1 
ATOM   5587 H  H    . LEU   B 1 126 ? 42.445 -28.006 -4.134  1.00 14.34 ?  126 LEU   B H    1 
ATOM   5588 H  HA   . LEU   B 1 126 ? 39.961 -27.241 -3.621  1.00 14.94 ?  126 LEU   B HA   1 
ATOM   5589 H  HB2  . LEU   B 1 126 ? 41.306 -29.672 -3.199  1.00 16.60 ?  126 LEU   B HB2  1 
ATOM   5590 H  HB3  . LEU   B 1 126 ? 39.823 -29.473 -2.678  1.00 16.60 ?  126 LEU   B HB3  1 
ATOM   5591 H  HG   . LEU   B 1 126 ? 40.484 -29.307 -5.410  1.00 17.50 ?  126 LEU   B HG   1 
ATOM   5592 H  HD11 . LEU   B 1 126 ? 39.641 -31.460 -5.676  1.00 19.31 ?  126 LEU   B HD11 1 
ATOM   5593 H  HD12 . LEU   B 1 126 ? 40.907 -31.480 -4.717  1.00 19.31 ?  126 LEU   B HD12 1 
ATOM   5594 H  HD13 . LEU   B 1 126 ? 39.445 -31.576 -4.103  1.00 19.31 ?  126 LEU   B HD13 1 
ATOM   5595 H  HD21 . LEU   B 1 126 ? 38.139 -29.606 -5.707  1.00 18.12 ?  126 LEU   B HD21 1 
ATOM   5596 H  HD22 . LEU   B 1 126 ? 37.973 -29.412 -4.139  1.00 18.12 ?  126 LEU   B HD22 1 
ATOM   5597 H  HD23 . LEU   B 1 126 ? 38.519 -28.218 -5.033  1.00 18.12 ?  126 LEU   B HD23 1 
ATOM   5598 N  N    . LEU   B 1 127 ? 39.902 -26.479 -1.313  1.00 12.14 ?  127 LEU   B N    1 
ATOM   5599 C  CA   . LEU   B 1 127 ? 39.965 -25.986 0.051   1.00 12.33 ?  127 LEU   B CA   1 
ATOM   5600 C  C    . LEU   B 1 127 ? 39.690 -27.108 1.045   1.00 12.32 ?  127 LEU   B C    1 
ATOM   5601 O  O    . LEU   B 1 127 ? 38.871 -28.006 0.814   1.00 12.69 ?  127 LEU   B O    1 
ATOM   5602 C  CB   . LEU   B 1 127 ? 38.950 -24.864 0.266   1.00 13.16 ?  127 LEU   B CB   1 
ATOM   5603 C  CG   . LEU   B 1 127 ? 39.125 -23.601 -0.569  1.00 13.77 ?  127 LEU   B CG   1 
ATOM   5604 C  CD1  . LEU   B 1 127 ? 38.002 -22.636 -0.230  1.00 13.93 ?  127 LEU   B CD1  1 
ATOM   5605 C  CD2  . LEU   B 1 127 ? 40.476 -22.954 -0.322  1.00 14.47 ?  127 LEU   B CD2  1 
ATOM   5606 H  H    . LEU   B 1 127 ? 39.229 -26.180 -1.769  1.00 14.57 ?  127 LEU   B H    1 
ATOM   5607 H  HA   . LEU   B 1 127 ? 40.854 -25.630 0.220   1.00 14.80 ?  127 LEU   B HA   1 
ATOM   5608 H  HB2  . LEU   B 1 127 ? 38.067 -25.215 0.075   1.00 15.80 ?  127 LEU   B HB2  1 
ATOM   5609 H  HB3  . LEU   B 1 127 ? 38.991 -24.594 1.198   1.00 15.80 ?  127 LEU   B HB3  1 
ATOM   5610 H  HG   . LEU   B 1 127 ? 39.048 -23.819 -1.510  1.00 16.53 ?  127 LEU   B HG   1 
ATOM   5611 H  HD11 . LEU   B 1 127 ? 38.106 -21.826 -0.757  1.00 16.72 ?  127 LEU   B HD11 1 
ATOM   5612 H  HD12 . LEU   B 1 127 ? 37.148 -23.051 -0.430  1.00 16.72 ?  127 LEU   B HD12 1 
ATOM   5613 H  HD13 . LEU   B 1 127 ? 38.046 -22.417 0.717   1.00 16.72 ?  127 LEU   B HD13 1 
ATOM   5614 H  HD21 . LEU   B 1 127 ? 40.509 -22.099 -0.782  1.00 17.37 ?  127 LEU   B HD21 1 
ATOM   5615 H  HD22 . LEU   B 1 127 ? 40.591 -22.817 0.633   1.00 17.37 ?  127 LEU   B HD22 1 
ATOM   5616 H  HD23 . LEU   B 1 127 ? 41.169 -23.539 -0.659  1.00 17.37 ?  127 LEU   B HD23 1 
ATOM   5617 N  N    . SER   B 1 128 ? 40.376 -27.023 2.175   1.00 12.53 ?  128 SER   B N    1 
ATOM   5618 C  CA   . SER   B 1 128 ? 40.272 -27.942 3.298   1.00 12.94 ?  128 SER   B CA   1 
ATOM   5619 C  C    . SER   B 1 128 ? 40.768 -29.346 2.973   1.00 13.87 ?  128 SER   B C    1 
ATOM   5620 O  O    . SER   B 1 128 ? 40.680 -30.229 3.828   1.00 15.20 ?  128 SER   B O    1 
ATOM   5621 C  CB   . SER   B 1 128 ? 38.872 -27.960 3.930   1.00 13.15 ?  128 SER   B CB   1 
ATOM   5622 O  OG   . SER   B 1 128 ? 38.556 -26.687 4.482   1.00 13.76 ?  128 SER   B OG   1 
ATOM   5623 H  H    . SER   B 1 128 ? 40.944 -26.392 2.324   1.00 15.03 ?  128 SER   B H    1 
ATOM   5624 H  HA   . SER   B 1 128 ? 40.860 -27.603 3.984   1.00 15.53 ?  128 SER   B HA   1 
ATOM   5625 H  HB2  . SER   B 1 128 ? 38.213 -28.194 3.257   1.00 15.78 ?  128 SER   B HB2  1 
ATOM   5626 H  HB3  . SER   B 1 128 ? 38.858 -28.635 4.643   1.00 15.78 ?  128 SER   B HB3  1 
ATOM   5627 H  HG   . SER   B 1 128 ? 39.127 -26.491 5.071   1.00 16.52 ?  128 SER   B HG   1 
ATOM   5628 N  N    . ALA   B 1 129 ? 41.336 -29.563 1.787   1.00 14.79 ?  129 ALA   B N    1 
ATOM   5629 C  CA   . ALA   B 1 129 ? 41.877 -30.860 1.426   1.00 15.79 ?  129 ALA   B CA   1 
ATOM   5630 C  C    . ALA   B 1 129 ? 43.268 -31.038 2.021   1.00 14.99 ?  129 ALA   B C    1 
ATOM   5631 O  O    . ALA   B 1 129 ? 43.828 -30.143 2.669   1.00 14.99 ?  129 ALA   B O    1 
ATOM   5632 C  CB   . ALA   B 1 129 ? 41.918 -31.017 -0.092  1.00 17.87 ?  129 ALA   B CB   1 
ATOM   5633 H  H    . ALA   B 1 129 ? 41.422 -28.968 1.169   1.00 17.75 ?  129 ALA   B H    1 
ATOM   5634 H  HA   . ALA   B 1 129 ? 41.306 -31.554 1.786   1.00 18.95 ?  129 ALA   B HA   1 
ATOM   5635 H  HB1  . ALA   B 1 129 ? 42.273 -31.896 -0.307  1.00 21.45 ?  129 ALA   B HB1  1 
ATOM   5636 H  HB2  . ALA   B 1 129 ? 41.018 -30.930 -0.439  1.00 21.45 ?  129 ALA   B HB2  1 
ATOM   5637 H  HB3  . ALA   B 1 129 ? 42.489 -30.329 -0.465  1.00 21.45 ?  129 ALA   B HB3  1 
ATOM   5638 N  N    . GLY   B 1 130 ? 43.829 -32.223 1.789   1.00 15.01 ?  130 GLY   B N    1 
ATOM   5639 C  CA   . GLY   B 1 130 ? 45.214 -32.468 2.143   1.00 15.99 ?  130 GLY   B CA   1 
ATOM   5640 C  C    . GLY   B 1 130 ? 45.426 -32.373 3.635   1.00 15.60 ?  130 GLY   B C    1 
ATOM   5641 O  O    . GLY   B 1 130 ? 44.724 -33.011 4.435   1.00 16.32 ?  130 GLY   B O    1 
ATOM   5642 H  H    . GLY   B 1 130 ? 43.434 -32.893 1.420   1.00 18.01 ?  130 GLY   B H    1 
ATOM   5643 H  HA2  . GLY   B 1 130 ? 45.476 -33.357 1.845   1.00 19.19 ?  130 GLY   B HA2  1 
ATOM   5644 H  HA3  . GLY   B 1 130 ? 45.786 -31.818 1.703   1.00 19.19 ?  130 GLY   B HA3  1 
ATOM   5645 N  N    . ILE   B 1 131 ? 46.399 -31.543 4.023   1.00 15.91 ?  131 ILE   B N    1 
ATOM   5646 C  CA   . ILE   B 1 131 ? 46.758 -31.412 5.426   1.00 16.59 ?  131 ILE   B CA   1 
ATOM   5647 C  C    . ILE   B 1 131 ? 45.646 -30.808 6.263   1.00 15.81 ?  131 ILE   B C    1 
ATOM   5648 O  O    . ILE   B 1 131 ? 45.729 -30.861 7.494   1.00 16.92 ?  131 ILE   B O    1 
ATOM   5649 C  CB   . ILE   B 1 131 ? 48.077 -30.633 5.619   1.00 18.04 ?  131 ILE   B CB   1 
ATOM   5650 C  CG1  . ILE   B 1 131 ? 47.906 -29.155 5.243   1.00 18.65 ?  131 ILE   B CG1  1 
ATOM   5651 C  CG2  . ILE   B 1 131 ? 49.194 -31.273 4.803   1.00 19.22 ?  131 ILE   B CG2  1 
ATOM   5652 C  CD1  . ILE   B 1 131 ? 49.118 -28.299 5.564   1.00 19.52 ?  131 ILE   B CD1  1 
ATOM   5653 H  H    . ILE   B 1 131 ? 46.858 -31.048 3.492   1.00 19.10 ?  131 ILE   B H    1 
ATOM   5654 H  HA   . ILE   B 1 131 ? 46.901 -32.302 5.775   1.00 19.92 ?  131 ILE   B HA   1 
ATOM   5655 H  HB   . ILE   B 1 131 ? 48.316 -30.683 6.557   1.00 21.65 ?  131 ILE   B HB   1 
ATOM   5656 H  HG12 . ILE   B 1 131 ? 47.740 -29.096 4.290   1.00 22.39 ?  131 ILE   B HG12 1 
ATOM   5657 H  HG13 . ILE   B 1 131 ? 47.152 -28.785 5.730   1.00 22.39 ?  131 ILE   B HG13 1 
ATOM   5658 H  HG21 . ILE   B 1 131 ? 50.038 -30.876 5.065   1.00 23.07 ?  131 ILE   B HG21 1 
ATOM   5659 H  HG22 . ILE   B 1 131 ? 49.204 -32.225 4.979   1.00 23.07 ?  131 ILE   B HG22 1 
ATOM   5660 H  HG23 . ILE   B 1 131 ? 49.025 -31.110 3.862   1.00 23.07 ?  131 ILE   B HG23 1 
ATOM   5661 H  HD11 . ILE   B 1 131 ? 48.900 -27.370 5.389   1.00 23.43 ?  131 ILE   B HD11 1 
ATOM   5662 H  HD12 . ILE   B 1 131 ? 49.347 -28.415 6.499   1.00 23.43 ?  131 ILE   B HD12 1 
ATOM   5663 H  HD13 . ILE   B 1 131 ? 49.858 -28.577 5.004   1.00 23.43 ?  131 ILE   B HD13 1 
ATOM   5664 N  N    . PHE   B 1 132 ? 44.611 -30.236 5.634   1.00 14.62 ?  132 PHE   B N    1 
ATOM   5665 C  CA   . PHE   B 1 132 ? 43.455 -29.727 6.367   1.00 15.02 ?  132 PHE   B CA   1 
ATOM   5666 C  C    . PHE   B 1 132 ? 42.434 -30.816 6.694   1.00 16.33 ?  132 PHE   B C    1 
ATOM   5667 O  O    . PHE   B 1 132 ? 41.526 -30.563 7.491   1.00 17.99 ?  132 PHE   B O    1 
ATOM   5668 C  CB   . PHE   B 1 132 ? 42.779 -28.587 5.590   1.00 13.95 ?  132 PHE   B CB   1 
ATOM   5669 C  CG   . PHE   B 1 132 ? 43.477 -27.246 5.708   1.00 14.10 ?  132 PHE   B CG   1 
ATOM   5670 C  CD1  . PHE   B 1 132 ? 44.778 -27.065 5.253   1.00 15.08 ?  132 PHE   B CD1  1 
ATOM   5671 C  CD2  . PHE   B 1 132 ? 42.799 -26.150 6.224   1.00 13.40 ?  132 PHE   B CD2  1 
ATOM   5672 C  CE1  . PHE   B 1 132 ? 45.398 -25.829 5.348   1.00 15.33 ?  132 PHE   B CE1  1 
ATOM   5673 C  CE2  . PHE   B 1 132 ? 43.414 -24.910 6.317   1.00 13.76 ?  132 PHE   B CE2  1 
ATOM   5674 C  CZ   . PHE   B 1 132 ? 44.713 -24.753 5.877   1.00 15.10 ?  132 PHE   B CZ   1 
ATOM   5675 H  H    . PHE   B 1 132 ? 44.552 -30.129 4.780   1.00 17.55 ?  132 PHE   B H    1 
ATOM   5676 H  HA   . PHE   B 1 132 ? 43.763 -29.356 7.206   1.00 18.02 ?  132 PHE   B HA   1 
ATOM   5677 H  HB2  . PHE   B 1 132 ? 42.762 -28.820 4.651   1.00 16.75 ?  132 PHE   B HB2  1 
ATOM   5678 H  HB3  . PHE   B 1 132 ? 41.873 -28.475 5.920   1.00 16.75 ?  132 PHE   B HB3  1 
ATOM   5679 H  HD1  . PHE   B 1 132 ? 45.245 -27.789 4.901   1.00 18.10 ?  132 PHE   B HD1  1 
ATOM   5680 H  HD2  . PHE   B 1 132 ? 41.922 -26.250 6.520   1.00 16.08 ?  132 PHE   B HD2  1 
ATOM   5681 H  HE1  . PHE   B 1 132 ? 46.276 -25.724 5.054   1.00 18.40 ?  132 PHE   B HE1  1 
ATOM   5682 H  HE2  . PHE   B 1 132 ? 42.951 -24.182 6.673   1.00 16.52 ?  132 PHE   B HE2  1 
ATOM   5683 H  HZ   . PHE   B 1 132 ? 45.128 -23.918 5.942   1.00 18.12 ?  132 PHE   B HZ   1 
ATOM   5684 N  N    . GLY   B 1 133 ? 42.542 -32.008 6.097   1.00 15.70 ?  133 GLY   B N    1 
ATOM   5685 C  CA   . GLY   B 1 133 ? 41.834 -33.176 6.588   1.00 16.43 ?  133 GLY   B CA   1 
ATOM   5686 C  C    . GLY   B 1 133 ? 40.441 -33.441 6.049   1.00 16.84 ?  133 GLY   B C    1 
ATOM   5687 O  O    . GLY   B 1 133 ? 39.849 -34.460 6.419   1.00 19.00 ?  133 GLY   B O    1 
ATOM   5688 H  H    . GLY   B 1 133 ? 43.028 -32.155 5.402   1.00 18.84 ?  133 GLY   B H    1 
ATOM   5689 H  HA2  . GLY   B 1 133 ? 42.369 -33.957 6.393   1.00 19.72 ?  133 GLY   B HA2  1 
ATOM   5690 H  HA3  . GLY   B 1 133 ? 41.762 -33.100 7.552   1.00 19.72 ?  133 GLY   B HA3  1 
ATOM   5691 N  N    . ALA   B 1 134 ? 39.883 -32.578 5.209   1.00 15.89 ?  134 ALA   B N    1 
ATOM   5692 C  CA   . ALA   B 1 134 ? 38.555 -32.855 4.682   1.00 16.27 ?  134 ALA   B CA   1 
ATOM   5693 C  C    . ALA   B 1 134 ? 38.636 -33.842 3.522   1.00 16.22 ?  134 ALA   B C    1 
ATOM   5694 O  O    . ALA   B 1 134 ? 39.687 -34.034 2.905   1.00 17.49 ?  134 ALA   B O    1 
ATOM   5695 C  CB   . ALA   B 1 134 ? 37.870 -31.567 4.226   1.00 16.68 ?  134 ALA   B CB   1 
ATOM   5696 H  H    . ALA   B 1 134 ? 40.239 -31.840 4.939   1.00 19.07 ?  134 ALA   B H    1 
ATOM   5697 H  HA   . ALA   B 1 134 ? 38.012 -33.251 5.384   1.00 19.53 ?  134 ALA   B HA   1 
ATOM   5698 H  HB1  . ALA   B 1 134 ? 36.984 -31.784 3.896   1.00 20.02 ?  134 ALA   B HB1  1 
ATOM   5699 H  HB2  . ALA   B 1 134 ? 37.803 -30.961 4.981   1.00 20.02 ?  134 ALA   B HB2  1 
ATOM   5700 H  HB3  . ALA   B 1 134 ? 38.398 -31.163 3.521   1.00 20.02 ?  134 ALA   B HB3  1 
ATOM   5701 N  N    . ASP   B 1 135 ? 37.504 -34.469 3.233   1.00 16.19 ?  135 ASP   B N    1 
ATOM   5702 C  CA   . ASP   B 1 135 ? 37.409 -35.367 2.091   1.00 17.26 ?  135 ASP   B CA   1 
ATOM   5703 C  C    . ASP   B 1 135 ? 37.507 -34.528 0.823   1.00 16.08 ?  135 ASP   B C    1 
ATOM   5704 O  O    . ASP   B 1 135 ? 36.660 -33.649 0.608   1.00 16.08 ?  135 ASP   B O    1 
ATOM   5705 C  CB   . ASP   B 1 135 ? 36.065 -36.094 2.151   1.00 18.84 ?  135 ASP   B CB   1 
ATOM   5706 C  CG   . ASP   B 1 135 ? 35.866 -37.071 1.003   1.00 20.27 ?  135 ASP   B CG   1 
ATOM   5707 O  OD1  . ASP   B 1 135 ? 36.735 -37.133 0.106   1.00 20.37 ?  135 ASP   B OD1  1 
ATOM   5708 O  OD2  . ASP   B 1 135 ? 34.844 -37.801 1.016   1.00 23.18 -1 135 ASP   B OD2  1 
ATOM   5709 H  H    . ASP   B 1 135 ? 36.776 -34.391 3.682   1.00 19.43 ?  135 ASP   B H    1 
ATOM   5710 H  HA   . ASP   B 1 135 ? 38.127 -36.021 2.123   1.00 20.71 ?  135 ASP   B HA   1 
ATOM   5711 H  HB2  . ASP   B 1 135 ? 36.018 -36.595 2.979   1.00 22.61 ?  135 ASP   B HB2  1 
ATOM   5712 H  HB3  . ASP   B 1 135 ? 35.355 -35.435 2.120   1.00 22.61 ?  135 ASP   B HB3  1 
ATOM   5713 N  N    . PRO   B 1 136 ? 38.514 -34.736 -0.028  1.00 16.17 ?  136 PRO   B N    1 
ATOM   5714 C  CA   . PRO   B 1 136 ? 38.616 -33.906 -1.238  1.00 15.34 ?  136 PRO   B CA   1 
ATOM   5715 C  C    . PRO   B 1 136 ? 37.429 -34.060 -2.166  1.00 14.79 ?  136 PRO   B C    1 
ATOM   5716 O  O    . PRO   B 1 136 ? 37.098 -33.113 -2.885  1.00 14.30 ?  136 PRO   B O    1 
ATOM   5717 C  CB   . PRO   B 1 136 ? 39.927 -34.377 -1.884  1.00 16.59 ?  136 PRO   B CB   1 
ATOM   5718 C  CG   . PRO   B 1 136 ? 40.115 -35.774 -1.371  1.00 17.74 ?  136 PRO   B CG   1 
ATOM   5719 C  CD   . PRO   B 1 136 ? 39.567 -35.762 0.029   1.00 17.35 ?  136 PRO   B CD   1 
ATOM   5720 H  HA   . PRO   B 1 136 ? 38.704 -32.971 -0.997  1.00 18.41 ?  136 PRO   B HA   1 
ATOM   5721 H  HB2  . PRO   B 1 136 ? 39.839 -34.374 -2.852  1.00 19.91 ?  136 PRO   B HB2  1 
ATOM   5722 H  HB3  . PRO   B 1 136 ? 40.657 -33.804 -1.603  1.00 19.91 ?  136 PRO   B HB3  1 
ATOM   5723 H  HG2  . PRO   B 1 136 ? 39.619 -36.398 -1.925  1.00 21.29 ?  136 PRO   B HG2  1 
ATOM   5724 H  HG3  . PRO   B 1 136 ? 41.059 -35.998 -1.365  1.00 21.29 ?  136 PRO   B HG3  1 
ATOM   5725 H  HD2  . PRO   B 1 136 ? 39.182 -36.625 0.253   1.00 20.82 ?  136 PRO   B HD2  1 
ATOM   5726 H  HD3  . PRO   B 1 136 ? 40.255 -35.506 0.666   1.00 20.82 ?  136 PRO   B HD3  1 
ATOM   5727 N  N    . ILE   B 1 137 ? 36.773 -35.225 -2.170  1.00 15.08 ?  137 ILE   B N    1 
ATOM   5728 C  CA   . ILE   B 1 137 ? 35.560 -35.388 -2.968  1.00 15.51 ?  137 ILE   B CA   1 
ATOM   5729 C  C    . ILE   B 1 137 ? 34.483 -34.424 -2.487  1.00 15.19 ?  137 ILE   B C    1 
ATOM   5730 O  O    . ILE   B 1 137 ? 33.765 -33.810 -3.286  1.00 14.84 ?  137 ILE   B O    1 
ATOM   5731 C  CB   . ILE   B 1 137 ? 35.088 -36.857 -2.924  1.00 17.48 ?  137 ILE   B CB   1 
ATOM   5732 C  CG1  . ILE   B 1 137 ? 36.093 -37.757 -3.647  1.00 19.67 ?  137 ILE   B CG1  1 
ATOM   5733 C  CG2  . ILE   B 1 137 ? 33.702 -37.008 -3.543  1.00 18.09 ?  137 ILE   B CG2  1 
ATOM   5734 C  CD1  . ILE   B 1 137 ? 35.796 -39.240 -3.530  1.00 21.62 ?  137 ILE   B CD1  1 
ATOM   5735 H  H    . ILE   B 1 137 ? 37.007 -35.925 -1.729  1.00 18.10 ?  137 ILE   B H    1 
ATOM   5736 H  HA   . ILE   B 1 137 ? 35.759 -35.174 -3.893  1.00 18.62 ?  137 ILE   B HA   1 
ATOM   5737 H  HB   . ILE   B 1 137 ? 35.038 -37.138 -2.000  1.00 20.98 ?  137 ILE   B HB   1 
ATOM   5738 H  HG12 . ILE   B 1 137 ? 36.093 -37.532 -4.591  1.00 23.60 ?  137 ILE   B HG12 1 
ATOM   5739 H  HG13 . ILE   B 1 137 ? 36.973 -37.604 -3.273  1.00 23.60 ?  137 ILE   B HG13 1 
ATOM   5740 H  HG21 . ILE   B 1 137 ? 33.492 -37.951 -3.639  1.00 21.71 ?  137 ILE   B HG21 1 
ATOM   5741 H  HG22 . ILE   B 1 137 ? 33.047 -36.591 -2.964  1.00 21.71 ?  137 ILE   B HG22 1 
ATOM   5742 H  HG23 . ILE   B 1 137 ? 33.697 -36.582 -4.414  1.00 21.71 ?  137 ILE   B HG23 1 
ATOM   5743 H  HD11 . ILE   B 1 137 ? 36.585 -39.742 -3.786  1.00 25.95 ?  137 ILE   B HD11 1 
ATOM   5744 H  HD12 . ILE   B 1 137 ? 35.559 -39.443 -2.611  1.00 25.95 ?  137 ILE   B HD12 1 
ATOM   5745 H  HD13 . ILE   B 1 137 ? 35.057 -39.465 -4.117  1.00 25.95 ?  137 ILE   B HD13 1 
ATOM   5746 N  N    . HIS   B 1 138 ? 34.352 -34.280 -1.172  1.00 15.06 ?  138 HIS   B N    1 
ATOM   5747 C  CA   . HIS   B 1 138 ? 33.402 -33.319 -0.633  1.00 15.41 ?  138 HIS   B CA   1 
ATOM   5748 C  C    . HIS   B 1 138 ? 33.822 -31.890 -0.947  1.00 14.69 ?  138 HIS   B C    1 
ATOM   5749 O  O    . HIS   B 1 138 ? 32.977 -31.046 -1.251  1.00 15.21 ?  138 HIS   B O    1 
ATOM   5750 C  CB   . HIS   B 1 138 ? 33.279 -33.501 0.870   1.00 16.74 ?  138 HIS   B CB   1 
ATOM   5751 C  CG   . HIS   B 1 138 ? 32.345 -32.523 1.501   1.00 17.72 ?  138 HIS   B CG   1 
ATOM   5752 N  ND1  . HIS   B 1 138 ? 31.008 -32.459 1.172   1.00 19.10 ?  138 HIS   B ND1  1 
ATOM   5753 C  CD2  . HIS   B 1 138 ? 32.555 -31.546 2.413   1.00 18.11 ?  138 HIS   B CD2  1 
ATOM   5754 C  CE1  . HIS   B 1 138 ? 30.431 -31.496 1.866   1.00 19.15 ?  138 HIS   B CE1  1 
ATOM   5755 N  NE2  . HIS   B 1 138 ? 31.348 -30.926 2.628   1.00 18.61 ?  138 HIS   B NE2  1 
ATOM   5756 H  H    . HIS   B 1 138 ? 34.800 -34.716 -0.583  1.00 18.08 ?  138 HIS   B H    1 
ATOM   5757 H  HA   . HIS   B 1 138 ? 32.531 -33.477 -1.033  1.00 18.50 ?  138 HIS   B HA   1 
ATOM   5758 H  HB2  . HIS   B 1 138 ? 32.942 -34.392 1.053   1.00 20.09 ?  138 HIS   B HB2  1 
ATOM   5759 H  HB3  . HIS   B 1 138 ? 34.150 -33.384 1.274   1.00 20.09 ?  138 HIS   B HB3  1 
ATOM   5760 H  HD1  . HIS   B 1 138 ? 30.610 -32.974 0.605   1.00 22.92 ?  138 HIS   B HD1  1 
ATOM   5761 H  HD2  . HIS   B 1 138 ? 33.358 -31.337 2.826   1.00 21.73 ?  138 HIS   B HD2  1 
ATOM   5762 H  HE1  . HIS   B 1 138 ? 29.528 -31.265 1.825   1.00 22.99 ?  138 HIS   B HE1  1 
ATOM   5763 N  N    . SER   B 1 139 ? 35.116 -31.590 -0.869  1.00 14.51 ?  139 SER   B N    1 
ATOM   5764 C  CA   . SER   B 1 139 ? 35.553 -30.241 -1.190  1.00 13.85 ?  139 SER   B CA   1 
ATOM   5765 C  C    . SER   B 1 139 ? 35.214 -29.888 -2.629  1.00 12.78 ?  139 SER   B C    1 
ATOM   5766 O  O    . SER   B 1 139 ? 34.770 -28.773 -2.909  1.00 13.12 ?  139 SER   B O    1 
ATOM   5767 C  CB   . SER   B 1 139 ? 37.048 -30.104 -0.932  1.00 13.74 ?  139 SER   B CB   1 
ATOM   5768 O  OG   . SER   B 1 139 ? 37.466 -28.775 -1.195  1.00 14.09 ?  139 SER   B OG   1 
ATOM   5769 H  H    . SER   B 1 139 ? 35.737 -32.136 -0.647  1.00 17.41 ?  139 SER   B H    1 
ATOM   5770 H  HA   . SER   B 1 139 ? 35.089 -29.618 -0.616  1.00 16.62 ?  139 SER   B HA   1 
ATOM   5771 H  HB2  . SER   B 1 139 ? 37.231 -30.315 -0.004  1.00 16.50 ?  139 SER   B HB2  1 
ATOM   5772 H  HB3  . SER   B 1 139 ? 37.531 -30.715 -1.514  1.00 16.50 ?  139 SER   B HB3  1 
ATOM   5773 H  HG   . SER   B 1 139 ? 38.294 -28.702 -1.057  1.00 16.91 ?  139 SER   B HG   1 
ATOM   5774 N  N    . LEU   B 1 140 ? 35.404 -30.828 -3.553  1.00 12.84 ?  140 LEU   B N    1 
ATOM   5775 C  CA   . LEU   B 1 140 ? 35.039 -30.575 -4.940  1.00 12.74 ?  140 LEU   B CA   1 
ATOM   5776 C  C    . LEU   B 1 140 ? 33.535 -30.357 -5.071  1.00 13.09 ?  140 LEU   B C    1 
ATOM   5777 O  O    . LEU   B 1 140 ? 33.092 -29.470 -5.806  1.00 13.38 ?  140 LEU   B O    1 
ATOM   5778 C  CB   . LEU   B 1 140 ? 35.510 -31.733 -5.820  1.00 13.15 ?  140 LEU   B CB   1 
ATOM   5779 C  CG   . LEU   B 1 140 ? 35.135 -31.634 -7.291  1.00 13.40 ?  140 LEU   B CG   1 
ATOM   5780 C  CD1  . LEU   B 1 140 ? 35.694 -30.358 -7.895  1.00 14.12 ?  140 LEU   B CD1  1 
ATOM   5781 C  CD2  . LEU   B 1 140 ? 35.620 -32.856 -8.038  1.00 14.15 ?  140 LEU   B CD2  1 
ATOM   5782 H  H    . LEU   B 1 140 ? 35.740 -31.603 -3.409  1.00 15.42 ?  140 LEU   B H    1 
ATOM   5783 H  HA   . LEU   B 1 140 ? 35.487 -29.769 -5.244  1.00 15.29 ?  140 LEU   B HA   1 
ATOM   5784 H  HB2  . LEU   B 1 140 ? 36.481 -31.780 -5.774  1.00 15.78 ?  140 LEU   B HB2  1 
ATOM   5785 H  HB3  . LEU   B 1 140 ? 35.129 -32.555 -5.483  1.00 15.78 ?  140 LEU   B HB3  1 
ATOM   5786 H  HG   . LEU   B 1 140 ? 34.170 -31.595 -7.369  1.00 16.09 ?  140 LEU   B HG   1 
ATOM   5787 H  HD11 . LEU   B 1 140 ? 35.568 -30.383 -8.856  1.00 16.94 ?  140 LEU   B HD11 1 
ATOM   5788 H  HD12 . LEU   B 1 140 ? 35.224 -29.594 -7.522  1.00 16.94 ?  140 LEU   B HD12 1 
ATOM   5789 H  HD13 . LEU   B 1 140 ? 36.640 -30.297 -7.688  1.00 16.94 ?  140 LEU   B HD13 1 
ATOM   5790 H  HD21 . LEU   B 1 140 ? 35.367 -32.770 -8.972  1.00 16.98 ?  140 LEU   B HD21 1 
ATOM   5791 H  HD22 . LEU   B 1 140 ? 36.581 -32.913 -7.957  1.00 16.98 ?  140 LEU   B HD22 1 
ATOM   5792 H  HD23 . LEU   B 1 140 ? 35.201 -33.639 -7.652  1.00 16.98 ?  140 LEU   B HD23 1 
ATOM   5793 N  N    . ARG   B 1 141 ? 32.736 -31.143 -4.348  1.00 13.15 ?  141 ARG   B N    1 
ATOM   5794 C  CA   . ARG   B 1 141 ? 31.286 -30.970 -4.336  1.00 14.11 ?  141 ARG   B CA   1 
ATOM   5795 C  C    . ARG   B 1 141 ? 30.907 -29.559 -3.901  1.00 13.68 ?  141 ARG   B C    1 
ATOM   5796 O  O    . ARG   B 1 141 ? 30.104 -28.878 -4.558  1.00 13.94 ?  141 ARG   B O    1 
ATOM   5797 C  CB   . ARG   B 1 141 ? 30.703 -32.001 -3.361  1.00 15.67 ?  141 ARG   B CB   1 
ATOM   5798 C  CG   . ARG   B 1 141 ? 29.239 -31.893 -3.028  1.00 17.94 ?  141 ARG   B CG   1 
ATOM   5799 C  CD   . ARG   B 1 141 ? 28.427 -32.521 -4.094  1.00 19.80 ?  141 ARG   B CD   1 
ATOM   5800 N  NE   . ARG   B 1 141 ? 28.178 -31.608 -5.198  1.00 20.19 ?  141 ARG   B NE   1 
ATOM   5801 C  CZ   . ARG   B 1 141 ? 28.186 -31.954 -6.478  1.00 19.80 ?  141 ARG   B CZ   1 
ATOM   5802 N  NH1  . ARG   B 1 141 ? 28.630 -33.137 -6.873  1.00 19.78 ?  141 ARG   B NH1  1 
ATOM   5803 N  NH2  . ARG   B 1 141 ? 27.732 -31.093 -7.384  1.00 20.74 ?  141 ARG   B NH2  1 
ATOM   5804 H  H    . ARG   B 1 141 ? 33.017 -31.784 -3.853  1.00 15.79 ?  141 ARG   B H    1 
ATOM   5805 H  HA   . ARG   B 1 141 ? 30.926 -31.133 -5.219  1.00 16.93 ?  141 ARG   B HA   1 
ATOM   5806 H  HB2  . ARG   B 1 141 ? 30.859 -32.886 -3.734  1.00 18.81 ?  141 ARG   B HB2  1 
ATOM   5807 H  HB3  . ARG   B 1 141 ? 31.192 -31.931 -2.525  1.00 18.81 ?  141 ARG   B HB3  1 
ATOM   5808 H  HG2  . ARG   B 1 141 ? 29.071 -32.353 -2.193  1.00 21.53 ?  141 ARG   B HG2  1 
ATOM   5809 H  HG3  . ARG   B 1 141 ? 28.986 -30.958 -2.952  1.00 21.53 ?  141 ARG   B HG3  1 
ATOM   5810 H  HD2  . ARG   B 1 141 ? 28.898 -33.304 -4.431  1.00 23.76 ?  141 ARG   B HD2  1 
ATOM   5811 H  HD3  . ARG   B 1 141 ? 27.578 -32.792 -3.722  1.00 23.76 ?  141 ARG   B HD3  1 
ATOM   5812 H  HE   . ARG   B 1 141 ? 27.993 -30.790 -5.005  1.00 24.23 ?  141 ARG   B HE   1 
ATOM   5813 H  HH11 . ARG   B 1 141 ? 28.915 -33.711 -6.299  1.00 23.74 ?  141 ARG   B HH11 1 
ATOM   5814 H  HH12 . ARG   B 1 141 ? 28.636 -33.333 -7.707  1.00 23.74 ?  141 ARG   B HH12 1 
ATOM   5815 H  HH21 . ARG   B 1 141 ? 27.449 -30.317 -7.140  1.00 24.89 ?  141 ARG   B HH21 1 
ATOM   5816 H  HH22 . ARG   B 1 141 ? 27.755 -31.295 -8.221  1.00 24.89 ?  141 ARG   B HH22 1 
ATOM   5817 N  N    . VAL   B 1 142 ? 31.451 -29.118 -2.769  1.00 13.11 ?  142 VAL   B N    1 
ATOM   5818 C  CA   . VAL   B 1 142 ? 31.123 -27.785 -2.279  1.00 13.19 ?  142 VAL   B CA   1 
ATOM   5819 C  C    . VAL   B 1 142 ? 31.591 -26.725 -3.270  1.00 13.27 ?  142 VAL   B C    1 
ATOM   5820 O  O    . VAL   B 1 142 ? 30.886 -25.739 -3.527  1.00 13.42 ?  142 VAL   B O    1 
ATOM   5821 C  CB   . VAL   B 1 142 ? 31.678 -27.559 -0.861  1.00 13.78 ?  142 VAL   B CB   1 
ATOM   5822 C  CG1  . VAL   B 1 142 ? 31.358 -26.142 -0.385  1.00 13.72 ?  142 VAL   B CG1  1 
ATOM   5823 C  CG2  . VAL   B 1 142 ? 31.100 -28.584 0.104   1.00 14.94 ?  142 VAL   B CG2  1 
ATOM   5824 H  H    . VAL   B 1 142 ? 32.003 -29.564 -2.274  1.00 15.74 ?  142 VAL   B H    1 
ATOM   5825 H  HA   . VAL   B 1 142 ? 30.164 -27.715 -2.216  1.00 15.83 ?  142 VAL   B HA   1 
ATOM   5826 H  HB   . VAL   B 1 142 ? 32.647 -27.666 -0.869  1.00 16.54 ?  142 VAL   B HB   1 
ATOM   5827 H  HG11 . VAL   B 1 142 ? 31.548 -26.078 0.563   1.00 16.47 ?  142 VAL   B HG11 1 
ATOM   5828 H  HG12 . VAL   B 1 142 ? 31.910 -25.511 -0.875  1.00 16.47 ?  142 VAL   B HG12 1 
ATOM   5829 H  HG13 . VAL   B 1 142 ? 30.421 -25.963 -0.549  1.00 16.47 ?  142 VAL   B HG13 1 
ATOM   5830 H  HG21 . VAL   B 1 142 ? 31.429 -28.396 0.997   1.00 17.93 ?  142 VAL   B HG21 1 
ATOM   5831 H  HG22 . VAL   B 1 142 ? 30.134 -28.519 0.084   1.00 17.93 ?  142 VAL   B HG22 1 
ATOM   5832 H  HG23 . VAL   B 1 142 ? 31.380 -29.470 -0.172  1.00 17.93 ?  142 VAL   B HG23 1 
ATOM   5833 N  N    . CYS   B 1 143 ? 32.769 -26.924 -3.861  1.00 12.66 ?  143 CYS   B N    1 
ATOM   5834 C  CA   . CYS   B 1 143 ? 33.261 -25.984 -4.862  1.00 12.33 ?  143 CYS   B CA   1 
ATOM   5835 C  C    . CYS   B 1 143 ? 32.261 -25.838 -6.002  1.00 12.25 ?  143 CYS   B C    1 
ATOM   5836 O  O    . CYS   B 1 143 ? 31.852 -24.729 -6.354  1.00 12.82 ?  143 CYS   B O    1 
ATOM   5837 C  CB   . CYS   B 1 143 ? 34.618 -26.464 -5.390  1.00 12.71 ?  143 CYS   B CB   1 
ATOM   5838 S  SG   . CYS   B 1 143 ? 35.359 -25.364 -6.608  1.00 13.33 ?  143 CYS   B SG   1 
ATOM   5839 H  H    . CYS   B 1 143 ? 33.297 -27.587 -3.702  1.00 15.20 ?  143 CYS   B H    1 
ATOM   5840 H  HA   . CYS   B 1 143 ? 33.388 -25.115 -4.450  1.00 14.80 ?  143 CYS   B HA   1 
ATOM   5841 H  HB2  . CYS   B 1 143 ? 35.239 -26.545 -4.650  1.00 15.25 ?  143 CYS   B HB2  1 
ATOM   5842 H  HB3  . CYS   B 1 143 ? 34.500 -27.330 -5.806  1.00 15.25 ?  143 CYS   B HB3  1 
ATOM   5843 H  HG   . CYS   B 1 143 ? 36.431 -25.796 -6.934  1.00 15.99 ?  143 CYS   B HG   1 
ATOM   5844 N  N    . VAL   B 1 144 ? 31.855 -26.956 -6.595  1.00 12.72 ?  144 VAL   B N    1 
ATOM   5845 C  CA   . VAL   B 1 144 ? 30.948 -26.890 -7.735  1.00 13.59 ?  144 VAL   B CA   1 
ATOM   5846 C  C    . VAL   B 1 144 ? 29.610 -26.274 -7.354  1.00 13.77 ?  144 VAL   B C    1 
ATOM   5847 O  O    . VAL   B 1 144 ? 28.990 -25.571 -8.162  1.00 15.12 ?  144 VAL   B O    1 
ATOM   5848 C  CB   . VAL   B 1 144 ? 30.790 -28.301 -8.318  1.00 16.57 ?  144 VAL   B CB   1 
ATOM   5849 C  CG1  . VAL   B 1 144 ? 29.527 -28.415 -9.162  1.00 19.17 ?  144 VAL   B CG1  1 
ATOM   5850 C  CG2  . VAL   B 1 144 ? 32.042 -28.691 -9.100  1.00 16.43 ?  144 VAL   B CG2  1 
ATOM   5851 H  H    . VAL   B 1 144 ? 32.092 -27.750 -6.364  1.00 15.26 ?  144 VAL   B H    1 
ATOM   5852 H  HA   . VAL   B 1 144 ? 31.344 -26.334 -8.420  1.00 16.31 ?  144 VAL   B HA   1 
ATOM   5853 H  HB   . VAL   B 1 144 ? 30.706 -28.933 -7.584  1.00 19.89 ?  144 VAL   B HB   1 
ATOM   5854 H  HG11 . VAL   B 1 144 ? 29.605 -29.194 -9.738  1.00 23.01 ?  144 VAL   B HG11 1 
ATOM   5855 H  HG12 . VAL   B 1 144 ? 28.765 -28.519 -8.574  1.00 23.01 ?  144 VAL   B HG12 1 
ATOM   5856 H  HG13 . VAL   B 1 144 ? 29.434 -27.616 -9.701  1.00 23.01 ?  144 VAL   B HG13 1 
ATOM   5857 H  HG21 . VAL   B 1 144 ? 31.929 -29.587 -9.456  1.00 19.71 ?  144 VAL   B HG21 1 
ATOM   5858 H  HG22 . VAL   B 1 144 ? 32.168 -28.061 -9.827  1.00 19.71 ?  144 VAL   B HG22 1 
ATOM   5859 H  HG23 . VAL   B 1 144 ? 32.808 -28.667 -8.505  1.00 19.71 ?  144 VAL   B HG23 1 
ATOM   5860 N  N    . ASP   B 1 145 ? 29.147 -26.523 -6.135  1.00 13.76 ?  145 ASP   B N    1 
ATOM   5861 C  CA   . ASP   B 1 145 ? 27.841 -26.060 -5.699  1.00 14.49 ?  145 ASP   B CA   1 
ATOM   5862 C  C    . ASP   B 1 145 ? 27.870 -24.639 -5.152  1.00 14.05 ?  145 ASP   B C    1 
ATOM   5863 O  O    . ASP   B 1 145 ? 26.809 -24.096 -4.824  1.00 16.04 ?  145 ASP   B O    1 
ATOM   5864 C  CB   . ASP   B 1 145 ? 27.268 -26.986 -4.619  1.00 16.18 ?  145 ASP   B CB   1 
ATOM   5865 C  CG   . ASP   B 1 145 ? 26.895 -28.360 -5.133  1.00 17.85 ?  145 ASP   B CG   1 
ATOM   5866 O  OD1  . ASP   B 1 145 ? 26.770 -28.546 -6.360  1.00 18.25 ?  145 ASP   B OD1  1 
ATOM   5867 O  OD2  . ASP   B 1 145 ? 26.727 -29.251 -4.280  1.00 20.25 -1 145 ASP   B OD2  1 
ATOM   5868 H  H    . ASP   B 1 145 ? 29.589 -26.949 -5.531  1.00 16.52 ?  145 ASP   B H    1 
ATOM   5869 H  HA   . ASP   B 1 145 ? 27.245 -26.056 -6.459  1.00 17.39 ?  145 ASP   B HA   1 
ATOM   5870 H  HB2  . ASP   B 1 145 ? 27.924 -27.104 -3.927  1.00 19.42 ?  145 ASP   B HB2  1 
ATOM   5871 H  HB3  . ASP   B 1 145 ? 26.465 -26.574 -4.261  1.00 19.42 ?  145 ASP   B HB3  1 
ATOM   5872 N  N    . THR   B 1 146 ? 29.047 -24.029 -5.031  1.00 12.68 ?  146 THR   B N    1 
ATOM   5873 C  CA   . THR   B 1 146 ? 29.177 -22.713 -4.421  1.00 12.31 ?  146 THR   B CA   1 
ATOM   5874 C  C    . THR   B 1 146 ? 29.804 -21.682 -5.340  1.00 12.36 ?  146 THR   B C    1 
ATOM   5875 O  O    . THR   B 1 146 ? 29.346 -20.527 -5.385  1.00 12.69 ?  146 THR   B O    1 
ATOM   5876 C  CB   . THR   B 1 146 ? 30.006 -22.822 -3.134  1.00 12.70 ?  146 THR   B CB   1 
ATOM   5877 O  OG1  . THR   B 1 146 ? 29.434 -23.812 -2.272  1.00 12.96 ?  146 THR   B OG1  1 
ATOM   5878 C  CG2  . THR   B 1 146 ? 30.083 -21.484 -2.416  1.00 12.96 ?  146 THR   B CG2  1 
ATOM   5879 H  H    . THR   B 1 146 ? 29.801 -24.361 -5.292  1.00 15.22 ?  146 THR   B H    1 
ATOM   5880 H  HA   . THR   B 1 146 ? 28.303 -22.388 -4.175  1.00 14.78 ?  146 THR   B HA   1 
ATOM   5881 H  HB   . THR   B 1 146 ? 30.914 -23.086 -3.360  1.00 15.24 ?  146 THR   B HB   1 
ATOM   5882 H  HG1  . THR   B 1 146 ? 29.460 -24.569 -2.652  1.00 15.55 ?  146 THR   B HG1  1 
ATOM   5883 H  HG21 . THR   B 1 146 ? 30.428 -21.610 -1.521  1.00 15.55 ?  146 THR   B HG21 1 
ATOM   5884 H  HG22 . THR   B 1 146 ? 30.675 -20.884 -2.900  1.00 15.55 ?  146 THR   B HG22 1 
ATOM   5885 H  HG23 . THR   B 1 146 ? 29.202 -21.089 -2.366  1.00 15.55 ?  146 THR   B HG23 1 
ATOM   5886 N  N    . VAL   B 1 147 ? 30.867 -22.052 -6.044  1.00 12.15 ?  147 VAL   B N    1 
ATOM   5887 C  CA   . VAL   B 1 147 ? 31.589 -21.105 -6.877  1.00 11.78 ?  147 VAL   B CA   1 
ATOM   5888 C  C    . VAL   B 1 147 ? 30.856 -20.972 -8.198  1.00 12.29 ?  147 VAL   B C    1 
ATOM   5889 O  O    . VAL   B 1 147 ? 30.486 -21.973 -8.827  1.00 13.17 ?  147 VAL   B O    1 
ATOM   5890 C  CB   . VAL   B 1 147 ? 33.040 -21.565 -7.090  1.00 11.98 ?  147 VAL   B CB   1 
ATOM   5891 C  CG1  . VAL   B 1 147 ? 33.797 -20.531 -7.898  1.00 12.01 ?  147 VAL   B CG1  1 
ATOM   5892 C  CG2  . VAL   B 1 147 ? 33.726 -21.786 -5.752  1.00 12.26 ?  147 VAL   B CG2  1 
ATOM   5893 H  H    . VAL   B 1 147 ? 31.193 -22.853 -6.060  1.00 14.58 ?  147 VAL   B H    1 
ATOM   5894 H  HA   . VAL   B 1 147 ? 31.608 -20.241 -6.442  1.00 14.14 ?  147 VAL   B HA   1 
ATOM   5895 H  HB   . VAL   B 1 147 ? 33.050 -22.404 -7.583  1.00 14.38 ?  147 VAL   B HB   1 
ATOM   5896 H  HG11 . VAL   B 1 147 ? 34.743 -20.752 -7.891  1.00 14.41 ?  147 VAL   B HG11 1 
ATOM   5897 H  HG12 . VAL   B 1 147 ? 33.467 -20.530 -8.809  1.00 14.41 ?  147 VAL   B HG12 1 
ATOM   5898 H  HG13 . VAL   B 1 147 ? 33.663 -19.657 -7.496  1.00 14.41 ?  147 VAL   B HG13 1 
ATOM   5899 H  HG21 . VAL   B 1 147 ? 34.666 -21.984 -5.906  1.00 14.71 ?  147 VAL   B HG21 1 
ATOM   5900 H  HG22 . VAL   B 1 147 ? 33.644 -20.980 -5.219  1.00 14.71 ?  147 VAL   B HG22 1 
ATOM   5901 H  HG23 . VAL   B 1 147 ? 33.305 -22.530 -5.296  1.00 14.71 ?  147 VAL   B HG23 1 
ATOM   5902 N  N    . ARG   B 1 148 ? 30.647 -19.725 -8.616  1.00 12.06 ?  148 ARG   B N    1 
ATOM   5903 C  CA   . ARG   B 1 148 ? 30.011 -19.407 -9.884  1.00 12.40 ?  148 ARG   B CA   1 
ATOM   5904 C  C    . ARG   B 1 148 ? 30.959 -18.732 -10.861 1.00 12.41 ?  148 ARG   B C    1 
ATOM   5905 O  O    . ARG   B 1 148 ? 30.672 -18.715 -12.060 1.00 13.68 ?  148 ARG   B O    1 
ATOM   5906 C  CB   . ARG   B 1 148 ? 28.772 -18.527 -9.656  1.00 12.97 ?  148 ARG   B CB   1 
ATOM   5907 C  CG   . ARG   B 1 148 ? 27.708 -19.241 -8.837  1.00 13.91 ?  148 ARG   B CG   1 
ATOM   5908 C  CD   . ARG   B 1 148 ? 26.500 -18.361 -8.542  1.00 14.59 ?  148 ARG   B CD   1 
ATOM   5909 N  NE   . ARG   B 1 148 ? 26.875 -17.158 -7.812  1.00 14.58 ?  148 ARG   B NE   1 
ATOM   5910 C  CZ   . ARG   B 1 148 ? 27.177 -17.125 -6.520  1.00 13.42 ?  148 ARG   B CZ   1 
ATOM   5911 N  NH1  . ARG   B 1 148 ? 27.114 -18.211 -5.765  1.00 13.40 ?  148 ARG   B NH1  1 
ATOM   5912 N  NH2  . ARG   B 1 148 ? 27.567 -15.977 -5.972  1.00 13.63 ?  148 ARG   B NH2  1 
ATOM   5913 H  H    . ARG   B 1 148 ? 30.875 -19.022 -8.161  1.00 14.47 ?  148 ARG   B H    1 
ATOM   5914 H  HA   . ARG   B 1 148 ? 29.713 -20.230 -10.288 1.00 14.88 ?  148 ARG   B HA   1 
ATOM   5915 H  HB2  . ARG   B 1 148 ? 29.031 -17.724 -9.176  1.00 15.57 ?  148 ARG   B HB2  1 
ATOM   5916 H  HB3  . ARG   B 1 148 ? 28.385 -18.294 -10.514 1.00 15.57 ?  148 ARG   B HB3  1 
ATOM   5917 H  HG2  . ARG   B 1 148 ? 27.396 -20.017 -9.331  1.00 16.70 ?  148 ARG   B HG2  1 
ATOM   5918 H  HG3  . ARG   B 1 148 ? 28.090 -19.519 -7.991  1.00 16.70 ?  148 ARG   B HG3  1 
ATOM   5919 H  HD2  . ARG   B 1 148 ? 26.090 -18.090 -9.376  1.00 17.51 ?  148 ARG   B HD2  1 
ATOM   5920 H  HD3  . ARG   B 1 148 ? 25.866 -18.858 -8.001  1.00 17.51 ?  148 ARG   B HD3  1 
ATOM   5921 H  HE   . ARG   B 1 148 ? 26.914 -16.418 -8.246  1.00 17.50 ?  148 ARG   B HE   1 
ATOM   5922 H  HH11 . ARG   B 1 148 ? 26.857 -18.960 -6.101  1.00 16.08 ?  148 ARG   B HH11 1 
ATOM   5923 H  HH12 . ARG   B 1 148 ? 27.303 -18.165 -4.924  1.00 16.08 ?  148 ARG   B HH12 1 
ATOM   5924 H  HH21 . ARG   B 1 148 ? 27.615 -15.266 -6.452  1.00 16.36 ?  148 ARG   B HH21 1 
ATOM   5925 H  HH22 . ARG   B 1 148 ? 27.760 -15.941 -5.134  1.00 16.36 ?  148 ARG   B HH22 1 
ATOM   5926 N  N    . THR   B 1 149 ? 32.064 -18.173 -10.379 1.00 12.46 ?  149 THR   B N    1 
ATOM   5927 C  CA   . THR   B 1 149 ? 33.099 -17.614 -11.233 1.00 12.34 ?  149 THR   B CA   1 
ATOM   5928 C  C    . THR   B 1 149 ? 33.990 -18.751 -11.735 1.00 12.20 ?  149 THR   B C    1 
ATOM   5929 O  O    . THR   B 1 149 ? 33.798 -19.923 -11.395 1.00 12.70 ?  149 THR   B O    1 
ATOM   5930 C  CB   . THR   B 1 149 ? 33.878 -16.565 -10.454 1.00 12.50 ?  149 THR   B CB   1 
ATOM   5931 O  OG1  . THR   B 1 149 ? 34.321 -17.161 -9.234  1.00 12.51 ?  149 THR   B OG1  1 
ATOM   5932 C  CG2  . THR   B 1 149 ? 32.995 -15.355 -10.167 1.00 13.11 ?  149 THR   B CG2  1 
ATOM   5933 H  H    . THR   B 1 149 ? 32.232 -18.095 -9.541  1.00 14.95 ?  149 THR   B H    1 
ATOM   5934 H  HA   . THR   B 1 149 ? 32.687 -17.182 -11.999 1.00 14.81 ?  149 THR   B HA   1 
ATOM   5935 H  HB   . THR   B 1 149 ? 34.645 -16.283 -10.968 1.00 15.00 ?  149 THR   B HB   1 
ATOM   5936 H  HG1  . THR   B 1 149 ? 34.741 -16.592 -8.772  1.00 15.02 ?  149 THR   B HG1  1 
ATOM   5937 H  HG21 . THR   B 1 149 ? 33.502 -14.684 -9.685  1.00 15.74 ?  149 THR   B HG21 1 
ATOM   5938 H  HG22 . THR   B 1 149 ? 32.680 -14.972 -11.001 1.00 15.74 ?  149 THR   B HG22 1 
ATOM   5939 H  HG23 . THR   B 1 149 ? 32.230 -15.618 -9.633  1.00 15.74 ?  149 THR   B HG23 1 
ATOM   5940 N  N    . ASN   B 1 150 ? 34.955 -18.426 -12.586 1.00 12.49 ?  150 ASN   B N    1 
ATOM   5941 C  CA   . ASN   B 1 150 ? 35.718 -19.452 -13.287 1.00 12.70 ?  150 ASN   B CA   1 
ATOM   5942 C  C    . ASN   B 1 150 ? 36.884 -19.902 -12.418 1.00 12.58 ?  150 ASN   B C    1 
ATOM   5943 O  O    . ASN   B 1 150 ? 37.815 -19.133 -12.160 1.00 13.31 ?  150 ASN   B O    1 
ATOM   5944 C  CB   . ASN   B 1 150 ? 36.188 -18.924 -14.635 1.00 14.32 ?  150 ASN   B CB   1 
ATOM   5945 C  CG   . ASN   B 1 150 ? 35.046 -18.721 -15.585 1.00 17.12 ?  150 ASN   B CG   1 
ATOM   5946 O  OD1  . ASN   B 1 150 ? 34.154 -19.554 -15.668 1.00 18.61 ?  150 ASN   B OD1  1 
ATOM   5947 N  ND2  . ASN   B 1 150 ? 35.043 -17.603 -16.286 1.00 18.81 ?  150 ASN   B ND2  1 
ATOM   5948 H  H    . ASN   B 1 150 ? 35.189 -17.618 -12.775 1.00 14.99 ?  150 ASN   B H    1 
ATOM   5949 H  HA   . ASN   B 1 150 ? 35.139 -20.219 -13.450 1.00 15.24 ?  150 ASN   B HA   1 
ATOM   5950 H  HB2  . ASN   B 1 150 ? 36.626 -18.069 -14.504 1.00 17.19 ?  150 ASN   B HB2  1 
ATOM   5951 H  HB3  . ASN   B 1 150 ? 36.801 -19.560 -15.029 1.00 17.19 ?  150 ASN   B HB3  1 
ATOM   5952 H  HD21 . ASN   B 1 150 ? 34.407 -17.443 -16.845 1.00 22.57 ?  150 ASN   B HD21 1 
ATOM   5953 H  HD22 . ASN   B 1 150 ? 35.684 -17.035 -16.195 1.00 22.57 ?  150 ASN   B HD22 1 
ATOM   5954 N  N    . VAL   B 1 151 ? 36.840 -21.149 -11.969 1.00 12.00 ?  151 VAL   B N    1 
ATOM   5955 C  CA   . VAL   B 1 151 ? 37.866 -21.679 -11.089 1.00 12.11 ?  151 VAL   B CA   1 
ATOM   5956 C  C    . VAL   B 1 151 ? 38.572 -22.842 -11.770 1.00 12.18 ?  151 VAL   B C    1 
ATOM   5957 O  O    . VAL   B 1 151 ? 37.930 -23.772 -12.283 1.00 13.00 ?  151 VAL   B O    1 
ATOM   5958 C  CB   . VAL   B 1 151 ? 37.319 -22.020 -9.689  1.00 13.30 ?  151 VAL   B CB   1 
ATOM   5959 C  CG1  . VAL   B 1 151 ? 36.152 -23.012 -9.759  1.00 14.28 ?  151 VAL   B CG1  1 
ATOM   5960 C  CG2  . VAL   B 1 151 ? 38.440 -22.515 -8.786  1.00 13.74 ?  151 VAL   B CG2  1 
ATOM   5961 H  H    . VAL   B 1 151 ? 36.217 -21.714 -12.167 1.00 14.40 ?  151 VAL   B H    1 
ATOM   5962 H  HA   . VAL   B 1 151 ? 38.532 -20.983 -10.964 1.00 14.53 ?  151 VAL   B HA   1 
ATOM   5963 H  HB   . VAL   B 1 151 ? 36.978 -21.200 -9.292  1.00 15.96 ?  151 VAL   B HB   1 
ATOM   5964 H  HG11 . VAL   B 1 151 ? 35.849 -23.208 -8.858  1.00 17.14 ?  151 VAL   B HG11 1 
ATOM   5965 H  HG12 . VAL   B 1 151 ? 35.429 -22.617 -10.272 1.00 17.14 ?  151 VAL   B HG12 1 
ATOM   5966 H  HG13 . VAL   B 1 151 ? 36.456 -23.827 -10.189 1.00 17.14 ?  151 VAL   B HG13 1 
ATOM   5967 H  HG21 . VAL   B 1 151 ? 38.103 -22.590 -7.878  1.00 16.49 ?  151 VAL   B HG21 1 
ATOM   5968 H  HG22 . VAL   B 1 151 ? 38.739 -23.383 -9.098  1.00 16.49 ?  151 VAL   B HG22 1 
ATOM   5969 H  HG23 . VAL   B 1 151 ? 39.175 -21.881 -8.811  1.00 16.49 ?  151 VAL   B HG23 1 
ATOM   5970 N  N    . TYR   B 1 152 ? 39.900 -22.752 -11.786 1.00 11.61 ?  152 TYR   B N    1 
ATOM   5971 C  CA   . TYR   B 1 152 ? 40.805 -23.731 -12.367 1.00 11.63 ?  152 TYR   B CA   1 
ATOM   5972 C  C    . TYR   B 1 152 ? 41.526 -24.406 -11.206 1.00 11.20 ?  152 TYR   B C    1 
ATOM   5973 O  O    . TYR   B 1 152 ? 42.368 -23.787 -10.546 1.00 11.79 ?  152 TYR   B O    1 
ATOM   5974 C  CB   . TYR   B 1 152 ? 41.773 -23.014 -13.307 1.00 12.38 ?  152 TYR   B CB   1 
ATOM   5975 C  CG   . TYR   B 1 152 ? 41.090 -22.558 -14.575 1.00 12.84 ?  152 TYR   B CG   1 
ATOM   5976 C  CD1  . TYR   B 1 152 ? 40.418 -21.339 -14.644 1.00 13.51 ?  152 TYR   B CD1  1 
ATOM   5977 C  CD2  . TYR   B 1 152 ? 41.097 -23.365 -15.698 1.00 13.87 ?  152 TYR   B CD2  1 
ATOM   5978 C  CE1  . TYR   B 1 152 ? 39.781 -20.945 -15.804 1.00 14.47 ?  152 TYR   B CE1  1 
ATOM   5979 C  CE2  . TYR   B 1 152 ? 40.473 -22.981 -16.859 1.00 14.65 ?  152 TYR   B CE2  1 
ATOM   5980 C  CZ   . TYR   B 1 152 ? 39.813 -21.772 -16.911 1.00 15.21 ?  152 TYR   B CZ   1 
ATOM   5981 O  OH   . TYR   B 1 152 ? 39.187 -21.407 -18.077 1.00 17.64 ?  152 TYR   B OH   1 
ATOM   5982 H  H    . TYR   B 1 152 ? 40.329 -22.096 -11.425 1.00 13.94 ?  152 TYR   B H    1 
ATOM   5983 H  HA   . TYR   B 1 152 ? 40.302 -24.397 -12.868 1.00 13.96 ?  152 TYR   B HA   1 
ATOM   5984 H  HB2  . TYR   B 1 152 ? 42.128 -22.232 -12.851 1.00 14.86 ?  152 TYR   B HB2  1 
ATOM   5985 H  HB3  . TYR   B 1 152 ? 42.493 -23.616 -13.544 1.00 14.86 ?  152 TYR   B HB3  1 
ATOM   5986 H  HD1  . TYR   B 1 152 ? 40.394 -20.786 -13.893 1.00 16.22 ?  152 TYR   B HD1  1 
ATOM   5987 H  HD2  . TYR   B 1 152 ? 41.540 -24.184 -15.668 1.00 16.64 ?  152 TYR   B HD2  1 
ATOM   5988 H  HE1  . TYR   B 1 152 ? 39.335 -20.131 -15.842 1.00 17.37 ?  152 TYR   B HE1  1 
ATOM   5989 H  HE2  . TYR   B 1 152 ? 40.491 -23.538 -17.605 1.00 17.59 ?  152 TYR   B HE2  1 
ATOM   5990 H  HH   . TYR   B 1 152 ? 38.823 -20.659 -17.984 1.00 21.17 ?  152 TYR   B HH   1 
ATOM   5991 N  N    . LEU   B 1 153 ? 41.168 -25.666 -10.946 1.00 11.50 ?  153 LEU   B N    1 
ATOM   5992 C  CA   . LEU   B 1 153 ? 41.675 -26.416 -9.808  1.00 11.53 ?  153 LEU   B CA   1 
ATOM   5993 C  C    . LEU   B 1 153 ? 42.908 -27.211 -10.203 1.00 11.83 ?  153 LEU   B C    1 
ATOM   5994 O  O    . LEU   B 1 153 ? 42.893 -27.943 -11.197 1.00 12.96 ?  153 LEU   B O    1 
ATOM   5995 C  CB   . LEU   B 1 153 ? 40.601 -27.375 -9.294  1.00 11.84 ?  153 LEU   B CB   1 
ATOM   5996 C  CG   . LEU   B 1 153 ? 39.345 -26.722 -8.719  1.00 12.66 ?  153 LEU   B CG   1 
ATOM   5997 C  CD1  . LEU   B 1 153 ? 38.249 -27.764 -8.564  1.00 12.97 ?  153 LEU   B CD1  1 
ATOM   5998 C  CD2  . LEU   B 1 153 ? 39.644 -26.071 -7.382  1.00 13.10 ?  153 LEU   B CD2  1 
ATOM   5999 H  H    . LEU   B 1 153 ? 40.605 -26.113 -11.428 1.00 13.81 ?  153 LEU   B H    1 
ATOM   6000 H  HA   . LEU   B 1 153 ? 41.901 -25.800 -9.097  1.00 13.83 ?  153 LEU   B HA   1 
ATOM   6001 H  HB2  . LEU   B 1 153 ? 40.318 -27.947 -10.026 1.00 14.21 ?  153 LEU   B HB2  1 
ATOM   6002 H  HB3  . LEU   B 1 153 ? 40.988 -27.923 -8.591  1.00 14.21 ?  153 LEU   B HB3  1 
ATOM   6003 H  HG   . LEU   B 1 153 ? 39.030 -26.033 -9.327  1.00 15.20 ?  153 LEU   B HG   1 
ATOM   6004 H  HD11 . LEU   B 1 153 ? 37.446 -27.326 -8.236  1.00 15.56 ?  153 LEU   B HD11 1 
ATOM   6005 H  HD12 . LEU   B 1 153 ? 38.079 -28.167 -9.425  1.00 15.56 ?  153 LEU   B HD12 1 
ATOM   6006 H  HD13 . LEU   B 1 153 ? 38.544 -28.433 -7.929  1.00 15.56 ?  153 LEU   B HD13 1 
ATOM   6007 H  HD21 . LEU   B 1 153 ? 38.830 -25.701 -7.014  1.00 15.72 ?  153 LEU   B HD21 1 
ATOM   6008 H  HD22 . LEU   B 1 153 ? 40.009 -26.739 -6.779  1.00 15.72 ?  153 LEU   B HD22 1 
ATOM   6009 H  HD23 . LEU   B 1 153 ? 40.299 -25.361 -7.514  1.00 15.72 ?  153 LEU   B HD23 1 
ATOM   6010 N  N    . ALA   B 1 154 ? 43.957 -27.099 -9.398  1.00 11.78 ?  154 ALA   B N    1 
ATOM   6011 C  CA   . ALA   B 1 154 ? 45.184 -27.861 -9.588  1.00 12.56 ?  154 ALA   B CA   1 
ATOM   6012 C  C    . ALA   B 1 154 ? 45.248 -28.935 -8.514  1.00 13.24 ?  154 ALA   B C    1 
ATOM   6013 O  O    . ALA   B 1 154 ? 45.169 -28.630 -7.317  1.00 14.43 ?  154 ALA   B O    1 
ATOM   6014 C  CB   . ALA   B 1 154 ? 46.413 -26.959 -9.520  1.00 13.71 ?  154 ALA   B CB   1 
ATOM   6015 H  H    . ALA   B 1 154 ? 43.977 -26.572 -8.714  1.00 14.14 ?  154 ALA   B H    1 
ATOM   6016 H  HA   . ALA   B 1 154 ? 45.167 -28.291 -10.452 1.00 15.07 ?  154 ALA   B HA   1 
ATOM   6017 H  HB1  . ALA   B 1 154 ? 47.209 -27.499 -9.647  1.00 16.46 ?  154 ALA   B HB1  1 
ATOM   6018 H  HB2  . ALA   B 1 154 ? 46.354 -26.288 -10.219 1.00 16.46 ?  154 ALA   B HB2  1 
ATOM   6019 H  HB3  . ALA   B 1 154 ? 46.445 -26.526 -8.651  1.00 16.46 ?  154 ALA   B HB3  1 
ATOM   6020 N  N    . VAL   B 1 155 ? 45.372 -30.183 -8.945  1.00 12.33 ?  155 VAL   B N    1 
ATOM   6021 C  CA   . VAL   B 1 155 ? 45.481 -31.328 -8.053  1.00 12.68 ?  155 VAL   B CA   1 
ATOM   6022 C  C    . VAL   B 1 155 ? 46.821 -31.995 -8.333  1.00 12.65 ?  155 VAL   B C    1 
ATOM   6023 O  O    . VAL   B 1 155 ? 47.057 -32.490 -9.444  1.00 14.47 ?  155 VAL   B O    1 
ATOM   6024 C  CB   . VAL   B 1 155 ? 44.326 -32.326 -8.252  1.00 14.02 ?  155 VAL   B CB   1 
ATOM   6025 C  CG1  . VAL   B 1 155 ? 44.503 -33.527 -7.335  1.00 14.07 ?  155 VAL   B CG1  1 
ATOM   6026 C  CG2  . VAL   B 1 155 ? 42.987 -31.644 -7.997  1.00 14.88 ?  155 VAL   B CG2  1 
ATOM   6027 H  H    . VAL   B 1 155 ? 45.405 -30.399 -9.778  1.00 14.80 ?  155 VAL   B H    1 
ATOM   6028 H  HA   . VAL   B 1 155 ? 45.471 -31.032 -7.131  1.00 15.22 ?  155 VAL   B HA   1 
ATOM   6029 H  HB   . VAL   B 1 155 ? 44.331 -32.643 -9.169  1.00 16.83 ?  155 VAL   B HB   1 
ATOM   6030 H  HG11 . VAL   B 1 155 ? 43.678 -34.037 -7.314  1.00 16.89 ?  155 VAL   B HG11 1 
ATOM   6031 H  HG12 . VAL   B 1 155 ? 45.223 -34.087 -7.675  1.00 16.89 ?  155 VAL   B HG12 1 
ATOM   6032 H  HG13 . VAL   B 1 155 ? 44.722 -33.218 -6.442  1.00 16.89 ?  155 VAL   B HG13 1 
ATOM   6033 H  HG21 . VAL   B 1 155 ? 42.276 -32.298 -8.088  1.00 17.86 ?  155 VAL   B HG21 1 
ATOM   6034 H  HG22 . VAL   B 1 155 ? 42.985 -31.279 -7.097  1.00 17.86 ?  155 VAL   B HG22 1 
ATOM   6035 H  HG23 . VAL   B 1 155 ? 42.866 -30.931 -8.643  1.00 17.86 ?  155 VAL   B HG23 1 
ATOM   6036 N  N    . PHE   B 1 156 ? 47.685 -32.041 -7.318  1.00 13.13 ?  156 PHE   B N    1 
ATOM   6037 C  CA   . PHE   B 1 156 ? 49.061 -32.497 -7.520  1.00 14.26 ?  156 PHE   B CA   1 
ATOM   6038 C  C    . PHE   B 1 156 ? 49.160 -33.996 -7.802  1.00 14.86 ?  156 PHE   B C    1 
ATOM   6039 O  O    . PHE   B 1 156 ? 49.895 -34.425 -8.705  1.00 16.81 ?  156 PHE   B O    1 
ATOM   6040 C  CB   . PHE   B 1 156 ? 49.883 -32.128 -6.288  1.00 14.37 ?  156 PHE   B CB   1 
ATOM   6041 C  CG   . PHE   B 1 156 ? 51.307 -32.580 -6.351  1.00 15.28 ?  156 PHE   B CG   1 
ATOM   6042 C  CD1  . PHE   B 1 156 ? 52.185 -32.033 -7.266  1.00 16.81 ?  156 PHE   B CD1  1 
ATOM   6043 C  CD2  . PHE   B 1 156 ? 51.772 -33.544 -5.482  1.00 15.47 ?  156 PHE   B CD2  1 
ATOM   6044 C  CE1  . PHE   B 1 156 ? 53.509 -32.441 -7.317  1.00 17.46 ?  156 PHE   B CE1  1 
ATOM   6045 C  CE2  . PHE   B 1 156 ? 53.092 -33.964 -5.530  1.00 16.69 ?  156 PHE   B CE2  1 
ATOM   6046 C  CZ   . PHE   B 1 156 ? 53.958 -33.409 -6.451  1.00 17.22 ?  156 PHE   B CZ   1 
ATOM   6047 H  H    . PHE   B 1 156 ? 47.499 -31.817 -6.504  1.00 15.76 ?  156 PHE   B H    1 
ATOM   6048 H  HA   . PHE   B 1 156 ? 49.435 -32.026 -8.274  1.00 17.11 ?  156 PHE   B HA   1 
ATOM   6049 H  HB2  . PHE   B 1 156 ? 49.889 -31.162 -6.193  1.00 17.25 ?  156 PHE   B HB2  1 
ATOM   6050 H  HB3  . PHE   B 1 156 ? 49.482 -32.532 -5.503  1.00 17.25 ?  156 PHE   B HB3  1 
ATOM   6051 H  HD1  . PHE   B 1 156 ? 51.890 -31.374 -7.853  1.00 20.18 ?  156 PHE   B HD1  1 
ATOM   6052 H  HD2  . PHE   B 1 156 ? 51.189 -33.924 -4.862  1.00 18.57 ?  156 PHE   B HD2  1 
ATOM   6053 H  HE1  . PHE   B 1 156 ? 54.092 -32.065 -7.941  1.00 20.95 ?  156 PHE   B HE1  1 
ATOM   6054 H  HE2  . PHE   B 1 156 ? 53.392 -34.623 -4.944  1.00 20.03 ?  156 PHE   B HE2  1 
ATOM   6055 H  HZ   . PHE   B 1 156 ? 54.843 -33.693 -6.484  1.00 20.67 ?  156 PHE   B HZ   1 
ATOM   6056 N  N    . ASP   B 1 157 ? 48.494 -34.813 -7.001  1.00 15.43 ?  157 ASP   B N    1 
ATOM   6057 C  CA   . ASP   B 1 157 ? 48.650 -36.258 -7.100  1.00 16.64 ?  157 ASP   B CA   1 
ATOM   6058 C  C    . ASP   B 1 157 ? 47.735 -36.798 -8.193  1.00 16.58 ?  157 ASP   B C    1 
ATOM   6059 O  O    . ASP   B 1 157 ? 46.509 -36.684 -8.088  1.00 16.06 ?  157 ASP   B O    1 
ATOM   6060 C  CB   . ASP   B 1 157 ? 48.291 -36.874 -5.757  1.00 17.92 ?  157 ASP   B CB   1 
ATOM   6061 C  CG   . ASP   B 1 157 ? 48.424 -38.379 -5.748  1.00 19.73 ?  157 ASP   B CG   1 
ATOM   6062 O  OD1  . ASP   B 1 157 ? 48.760 -38.979 -6.797  1.00 20.17 ?  157 ASP   B OD1  1 
ATOM   6063 O  OD2  . ASP   B 1 157 ? 48.203 -38.962 -4.670  1.00 22.05 -1 157 ASP   B OD2  1 
ATOM   6064 H  H    . ASP   B 1 157 ? 47.948 -34.563 -6.388  1.00 18.52 ?  157 ASP   B H    1 
ATOM   6065 H  HA   . ASP   B 1 157 ? 49.573 -36.485 -7.317  1.00 19.97 ?  157 ASP   B HA   1 
ATOM   6066 H  HB2  . ASP   B 1 157 ? 48.874 -36.508 -5.077  1.00 21.51 ?  157 ASP   B HB2  1 
ATOM   6067 H  HB3  . ASP   B 1 157 ? 47.367 -36.656 -5.552  1.00 21.51 ?  157 ASP   B HB3  1 
ATOM   6068 N  N    . LYS   B 1 158 ? 48.330 -37.410 -9.224  1.00 17.66 ?  158 LYS   B N    1 
ATOM   6069 C  CA   . LYS   B 1 158 ? 47.554 -38.018 -10.307 1.00 18.64 ?  158 LYS   B CA   1 
ATOM   6070 C  C    . LYS   B 1 158 ? 46.500 -38.987 -9.777  1.00 18.40 ?  158 LYS   B C    1 
ATOM   6071 O  O    . LYS   B 1 158 ? 45.396 -39.078 -10.326 1.00 18.44 ?  158 LYS   B O    1 
ATOM   6072 C  CB   . LYS   B 1 158 ? 48.500 -38.733 -11.279 1.00 20.35 ?  158 LYS   B CB   1 
ATOM   6073 C  CG   . LYS   B 1 158 ? 47.817 -39.625 -12.306 1.00 22.37 ?  158 LYS   B CG   1 
ATOM   6074 C  CD   . LYS   B 1 158 ? 46.975 -38.839 -13.286 1.00 24.29 ?  158 LYS   B CD   1 
ATOM   6075 C  CE   . LYS   B 1 158 ? 46.381 -39.753 -14.344 1.00 25.85 ?  158 LYS   B CE   1 
ATOM   6076 N  NZ   . LYS   B 1 158 ? 45.314 -39.072 -15.136 1.00 25.56 ?  158 LYS   B NZ   1 
ATOM   6077 H  H    . LYS   B 1 158 ? 49.185 -37.489 -9.321  1.00 21.20 ?  158 LYS   B H    1 
ATOM   6078 H  HA   . LYS   B 1 158 ? 47.100 -37.320 -10.803 1.00 22.37 ?  158 LYS   B HA   1 
ATOM   6079 H  HB2  . LYS   B 1 158 ? 49.008 -38.065 -11.773 1.00 24.42 ?  158 LYS   B HB2  1 
ATOM   6080 H  HB3  . LYS   B 1 158 ? 49.113 -39.288 -10.771 1.00 24.42 ?  158 LYS   B HB3  1 
ATOM   6081 H  HG2  . LYS   B 1 158 ? 48.499 -40.095 -12.814 1.00 26.85 ?  158 LYS   B HG2  1 
ATOM   6082 H  HG3  . LYS   B 1 158 ? 47.247 -40.274 -11.860 1.00 26.85 ?  158 LYS   B HG3  1 
ATOM   6083 H  HD2  . LYS   B 1 158 ? 46.248 -38.405 -12.812 1.00 29.15 ?  158 LYS   B HD2  1 
ATOM   6084 H  HD3  . LYS   B 1 158 ? 47.530 -38.179 -13.731 1.00 29.15 ?  158 LYS   B HD3  1 
ATOM   6085 H  HE2  . LYS   B 1 158 ? 47.077 -40.032 -14.956 1.00 31.03 ?  158 LYS   B HE2  1 
ATOM   6086 H  HE3  . LYS   B 1 158 ? 45.984 -40.528 -13.913 1.00 31.03 ?  158 LYS   B HE3  1 
ATOM   6087 H  HZ1  . LYS   B 1 158 ? 44.982 -39.627 -15.747 1.00 30.68 ?  158 LYS   B HZ1  1 
ATOM   6088 H  HZ2  . LYS   B 1 158 ? 44.655 -38.807 -14.599 1.00 30.68 ?  158 LYS   B HZ2  1 
ATOM   6089 H  HZ3  . LYS   B 1 158 ? 45.652 -38.358 -15.549 1.00 30.68 ?  158 LYS   B HZ3  1 
ATOM   6090 N  N    . ASN   B 1 159 ? 46.828 -39.745 -8.730  1.00 18.63 ?  159 ASN   B N    1 
ATOM   6091 C  CA   . ASN   B 1 159 ? 45.872 -40.725 -8.225  1.00 19.27 ?  159 ASN   B CA   1 
ATOM   6092 C  C    . ASN   B 1 159 ? 44.677 -40.055 -7.549  1.00 18.22 ?  159 ASN   B C    1 
ATOM   6093 O  O    . ASN   B 1 159 ? 43.549 -40.552 -7.658  1.00 18.42 ?  159 ASN   B O    1 
ATOM   6094 C  CB   . ASN   B 1 159 ? 46.575 -41.710 -7.298  1.00 20.72 ?  159 ASN   B CB   1 
ATOM   6095 C  CG   . ASN   B 1 159 ? 47.611 -42.542 -8.027  1.00 22.44 ?  159 ASN   B CG   1 
ATOM   6096 O  OD1  . ASN   B 1 159 ? 47.356 -43.048 -9.125  1.00 23.42 ?  159 ASN   B OD1  1 
ATOM   6097 N  ND2  . ASN   B 1 159 ? 48.788 -42.685 -7.428  1.00 23.14 ?  159 ASN   B ND2  1 
ATOM   6098 H  H    . ASN   B 1 159 ? 47.570 -39.699 -8.304  1.00 22.36 ?  159 ASN   B H    1 
ATOM   6099 H  HA   . ASN   B 1 159 ? 45.534 -41.231 -8.981  1.00 23.12 ?  159 ASN   B HA   1 
ATOM   6100 H  HB2  . ASN   B 1 159 ? 47.025 -41.223 -6.594  1.00 24.87 ?  159 ASN   B HB2  1 
ATOM   6101 H  HB3  . ASN   B 1 159 ? 45.918 -42.316 -6.923  1.00 24.87 ?  159 ASN   B HB3  1 
ATOM   6102 H  HD21 . ASN   B 1 159 ? 49.412 -43.149 -7.805  1.00 27.77 ?  159 ASN   B HD21 1 
ATOM   6103 H  HD22 . ASN   B 1 159 ? 48.928 -42.328 -6.660  1.00 27.77 ?  159 ASN   B HD22 1 
ATOM   6104 N  N    . LEU   B 1 160 ? 44.887 -38.921 -6.874  1.00 17.25 ?  160 LEU   B N    1 
ATOM   6105 C  CA   . LEU   B 1 160 ? 43.751 -38.190 -6.328  1.00 16.40 ?  160 LEU   B CA   1 
ATOM   6106 C  C    . LEU   B 1 160 ? 42.962 -37.524 -7.442  1.00 15.73 ?  160 LEU   B C    1 
ATOM   6107 O  O    . LEU   B 1 160 ? 41.726 -37.525 -7.422  1.00 15.38 ?  160 LEU   B O    1 
ATOM   6108 C  CB   . LEU   B 1 160 ? 44.212 -37.163 -5.297  1.00 16.13 ?  160 LEU   B CB   1 
ATOM   6109 C  CG   . LEU   B 1 160 ? 43.091 -36.270 -4.753  1.00 15.68 ?  160 LEU   B CG   1 
ATOM   6110 C  CD1  . LEU   B 1 160 ? 41.971 -37.095 -4.131  1.00 16.71 ?  160 LEU   B CD1  1 
ATOM   6111 C  CD2  . LEU   B 1 160 ? 43.652 -35.275 -3.747  1.00 15.82 ?  160 LEU   B CD2  1 
ATOM   6112 H  H    . LEU   B 1 160 ? 45.660 -38.566 -6.730  1.00 20.71 ?  160 LEU   B H    1 
ATOM   6113 H  HA   . LEU   B 1 160 ? 43.165 -38.819 -5.889  1.00 19.68 ?  160 LEU   B HA   1 
ATOM   6114 H  HB2  . LEU   B 1 160 ? 44.610 -37.640 -4.547  1.00 19.36 ?  160 LEU   B HB2  1 
ATOM   6115 H  HB3  . LEU   B 1 160 ? 44.883 -36.590 -5.706  1.00 19.36 ?  160 LEU   B HB3  1 
ATOM   6116 H  HG   . LEU   B 1 160 ? 42.716 -35.764 -5.486  1.00 18.82 ?  160 LEU   B HG   1 
ATOM   6117 H  HD11 . LEU   B 1 160 ? 41.335 -36.494 -3.718  1.00 20.06 ?  160 LEU   B HD11 1 
ATOM   6118 H  HD12 . LEU   B 1 160 ? 41.534 -37.614 -4.825  1.00 20.06 ?  160 LEU   B HD12 1 
ATOM   6119 H  HD13 . LEU   B 1 160 ? 42.348 -37.690 -3.462  1.00 20.06 ?  160 LEU   B HD13 1 
ATOM   6120 H  HD21 . LEU   B 1 160 ? 42.933 -34.697 -3.447  1.00 18.99 ?  160 LEU   B HD21 1 
ATOM   6121 H  HD22 . LEU   B 1 160 ? 44.023 -35.760 -2.993  1.00 18.99 ?  160 LEU   B HD22 1 
ATOM   6122 H  HD23 . LEU   B 1 160 ? 44.344 -34.747 -4.176  1.00 18.99 ?  160 LEU   B HD23 1 
ATOM   6123 N  N    . TYR   B 1 161 ? 43.660 -36.950 -8.424  1.00 15.83 ?  161 TYR   B N    1 
ATOM   6124 C  CA   . TYR   B 1 161 ? 42.988 -36.383 -9.587  1.00 15.57 ?  161 TYR   B CA   1 
ATOM   6125 C  C    . TYR   B 1 161 ? 42.045 -37.405 -10.209 1.00 15.34 ?  161 TYR   B C    1 
ATOM   6126 O  O    . TYR   B 1 161 ? 40.873 -37.111 -10.468 1.00 15.32 ?  161 TYR   B O    1 
ATOM   6127 C  CB   . TYR   B 1 161 ? 44.032 -35.901 -10.602 1.00 16.03 ?  161 TYR   B CB   1 
ATOM   6128 C  CG   . TYR   B 1 161 ? 43.457 -35.432 -11.915 1.00 16.48 ?  161 TYR   B CG   1 
ATOM   6129 C  CD1  . TYR   B 1 161 ? 43.057 -34.113 -12.078 1.00 16.47 ?  161 TYR   B CD1  1 
ATOM   6130 C  CD2  . TYR   B 1 161 ? 43.292 -36.306 -12.986 1.00 17.04 ?  161 TYR   B CD2  1 
ATOM   6131 C  CE1  . TYR   B 1 161 ? 42.524 -33.675 -13.261 1.00 17.55 ?  161 TYR   B CE1  1 
ATOM   6132 C  CE2  . TYR   B 1 161 ? 42.753 -35.874 -14.175 1.00 18.01 ?  161 TYR   B CE2  1 
ATOM   6133 C  CZ   . TYR   B 1 161 ? 42.370 -34.559 -14.308 1.00 18.04 ?  161 TYR   B CZ   1 
ATOM   6134 O  OH   . TYR   B 1 161 ? 41.833 -34.121 -15.491 1.00 20.23 ?  161 TYR   B OH   1 
ATOM   6135 H  H    . TYR   B 1 161 ? 44.517 -36.877 -8.443  1.00 19.00 ?  161 TYR   B H    1 
ATOM   6136 H  HA   . TYR   B 1 161 ? 42.462 -35.616 -9.315  1.00 18.68 ?  161 TYR   B HA   1 
ATOM   6137 H  HB2  . TYR   B 1 161 ? 44.522 -35.155 -10.218 1.00 19.24 ?  161 TYR   B HB2  1 
ATOM   6138 H  HB3  . TYR   B 1 161 ? 44.642 -36.626 -10.798 1.00 19.24 ?  161 TYR   B HB3  1 
ATOM   6139 H  HD1  . TYR   B 1 161 ? 43.160 -33.506 -11.378 1.00 19.77 ?  161 TYR   B HD1  1 
ATOM   6140 H  HD2  . TYR   B 1 161 ? 43.543 -37.194 -12.898 1.00 20.45 ?  161 TYR   B HD2  1 
ATOM   6141 H  HE1  . TYR   B 1 161 ? 42.266 -32.782 -13.355 1.00 21.06 ?  161 TYR   B HE1  1 
ATOM   6142 H  HE2  . TYR   B 1 161 ? 42.643 -36.463 -14.886 1.00 21.61 ?  161 TYR   B HE2  1 
ATOM   6143 H  HH   . TYR   B 1 161 ? 41.792 -34.756 -16.042 1.00 24.28 ?  161 TYR   B HH   1 
ATOM   6144 N  N    . ASP   B 1 162 ? 42.543 -38.624 -10.431 1.00 15.84 ?  162 ASP   B N    1 
ATOM   6145 C  CA   . ASP   B 1 162 ? 41.717 -39.657 -11.043 1.00 16.43 ?  162 ASP   B CA   1 
ATOM   6146 C  C    . ASP   B 1 162 ? 40.513 -39.999 -10.173 1.00 15.91 ?  162 ASP   B C    1 
ATOM   6147 O  O    . ASP   B 1 162 ? 39.410 -40.219 -10.687 1.00 16.25 ?  162 ASP   B O    1 
ATOM   6148 C  CB   . ASP   B 1 162 ? 42.553 -40.914 -11.296 1.00 18.04 ?  162 ASP   B CB   1 
ATOM   6149 C  CG   . ASP   B 1 162 ? 43.545 -40.753 -12.440 1.00 19.09 ?  162 ASP   B CG   1 
ATOM   6150 O  OD1  . ASP   B 1 162 ? 43.418 -39.789 -13.219 1.00 19.39 ?  162 ASP   B OD1  1 
ATOM   6151 O  OD2  . ASP   B 1 162 ? 44.442 -41.616 -12.568 1.00 20.72 -1 162 ASP   B OD2  1 
ATOM   6152 H  H    . ASP   B 1 162 ? 43.343 -38.869 -10.236 1.00 19.01 ?  162 ASP   B H    1 
ATOM   6153 H  HA   . ASP   B 1 162 ? 41.387 -39.335 -11.895 1.00 19.72 ?  162 ASP   B HA   1 
ATOM   6154 H  HB2  . ASP   B 1 162 ? 43.052 -41.126 -10.494 1.00 21.65 ?  162 ASP   B HB2  1 
ATOM   6155 H  HB3  . ASP   B 1 162 ? 41.957 -41.645 -11.520 1.00 21.65 ?  162 ASP   B HB3  1 
ATOM   6156 N  N    . LYS   B 1 163 ? 40.703 -40.066 -8.854  1.00 15.61 ?  163 LYS   B N    1 
ATOM   6157 C  CA   . LYS   B 1 163 ? 39.581 -40.350 -7.965  1.00 16.29 ?  163 LYS   B CA   1 
ATOM   6158 C  C    . LYS   B 1 163 ? 38.537 -39.243 -8.027  1.00 15.07 ?  163 LYS   B C    1 
ATOM   6159 O  O    . LYS   B 1 163 ? 37.329 -39.514 -8.033  1.00 15.88 ?  163 LYS   B O    1 
ATOM   6160 C  CB   . LYS   B 1 163 ? 40.068 -40.535 -6.531  1.00 19.38 ?  163 LYS   B CB   1 
ATOM   6161 C  CG   . LYS   B 1 163 ? 38.970 -40.999 -5.592  1.00 24.72 ?  163 LYS   B CG   1 
ATOM   6162 C  CD   . LYS   B 1 163 ? 39.478 -41.296 -4.195  1.00 29.25 ?  163 LYS   B CD   1 
ATOM   6163 C  CE   . LYS   B 1 163 ? 38.412 -42.022 -3.385  1.00 32.46 ?  163 LYS   B CE   1 
ATOM   6164 N  NZ   . LYS   B 1 163 ? 38.306 -41.504 -1.994  1.00 36.03 ?  163 LYS   B NZ   1 
ATOM   6165 H  H    . LYS   B 1 163 ? 41.462 -39.951 -8.457  1.00 18.73 ?  163 LYS   B H    1 
ATOM   6166 H  HA   . LYS   B 1 163 ? 39.163 -41.175 -8.248  1.00 19.55 ?  163 LYS   B HA   1 
ATOM   6167 H  HB2  . LYS   B 1 163 ? 40.772 -41.205 -6.520  1.00 23.26 ?  163 LYS   B HB2  1 
ATOM   6168 H  HB3  . LYS   B 1 163 ? 40.410 -39.691 -6.199  1.00 23.26 ?  163 LYS   B HB3  1 
ATOM   6169 H  HG2  . LYS   B 1 163 ? 38.296 -40.304 -5.523  1.00 29.66 ?  163 LYS   B HG2  1 
ATOM   6170 H  HG3  . LYS   B 1 163 ? 38.571 -41.811 -5.946  1.00 29.66 ?  163 LYS   B HG3  1 
ATOM   6171 H  HD2  . LYS   B 1 163 ? 40.262 -41.865 -4.250  1.00 35.10 ?  163 LYS   B HD2  1 
ATOM   6172 H  HD3  . LYS   B 1 163 ? 39.691 -40.465 -3.745  1.00 35.10 ?  163 LYS   B HD3  1 
ATOM   6173 H  HE2  . LYS   B 1 163 ? 37.551 -41.907 -3.818  1.00 38.96 ?  163 LYS   B HE2  1 
ATOM   6174 H  HE3  . LYS   B 1 163 ? 38.637 -42.965 -3.339  1.00 38.96 ?  163 LYS   B HE3  1 
ATOM   6175 H  HZ1  . LYS   B 1 163 ? 37.675 -41.950 -1.552  1.00 43.24 ?  163 LYS   B HZ1  1 
ATOM   6176 H  HZ2  . LYS   B 1 163 ? 39.082 -41.605 -1.572  1.00 43.24 ?  163 LYS   B HZ2  1 
ATOM   6177 H  HZ3  . LYS   B 1 163 ? 38.093 -40.640 -2.009  1.00 43.24 ?  163 LYS   B HZ3  1 
ATOM   6178 N  N    . LEU   B 1 164 ? 38.987 -37.988 -8.081  1.00 14.28 ?  164 LEU   B N    1 
ATOM   6179 C  CA   . LEU   B 1 164 ? 38.070 -36.855 -8.136  1.00 13.94 ?  164 LEU   B CA   1 
ATOM   6180 C  C    . LEU   B 1 164 ? 37.289 -36.839 -9.445  1.00 13.89 ?  164 LEU   B C    1 
ATOM   6181 O  O    . LEU   B 1 164 ? 36.066 -36.640 -9.452  1.00 14.96 ?  164 LEU   B O    1 
ATOM   6182 C  CB   . LEU   B 1 164 ? 38.866 -35.560 -7.974  1.00 13.54 ?  164 LEU   B CB   1 
ATOM   6183 C  CG   . LEU   B 1 164 ? 39.407 -35.292 -6.575  1.00 14.63 ?  164 LEU   B CG   1 
ATOM   6184 C  CD1  . LEU   B 1 164 ? 40.494 -34.229 -6.630  1.00 14.32 ?  164 LEU   B CD1  1 
ATOM   6185 C  CD2  . LEU   B 1 164 ? 38.299 -34.862 -5.636  1.00 16.27 ?  164 LEU   B CD2  1 
ATOM   6186 H  H    . LEU   B 1 164 ? 39.820 -37.768 -8.091  1.00 17.14 ?  164 LEU   B H    1 
ATOM   6187 H  HA   . LEU   B 1 164 ? 37.440 -36.916 -7.409  1.00 16.73 ?  164 LEU   B HA   1 
ATOM   6188 H  HB2  . LEU   B 1 164 ? 39.630 -35.587 -8.577  1.00 16.25 ?  164 LEU   B HB2  1 
ATOM   6189 H  HB3  . LEU   B 1 164 ? 38.298 -34.813 -8.213  1.00 16.25 ?  164 LEU   B HB3  1 
ATOM   6190 H  HG   . LEU   B 1 164 ? 39.805 -36.102 -6.226  1.00 17.56 ?  164 LEU   B HG   1 
ATOM   6191 H  HD11 . LEU   B 1 164 ? 40.820 -34.059 -5.731  1.00 17.19 ?  164 LEU   B HD11 1 
ATOM   6192 H  HD12 . LEU   B 1 164 ? 41.223 -34.546 -7.188  1.00 17.19 ?  164 LEU   B HD12 1 
ATOM   6193 H  HD13 . LEU   B 1 164 ? 40.125 -33.412 -7.004  1.00 17.19 ?  164 LEU   B HD13 1 
ATOM   6194 H  HD21 . LEU   B 1 164 ? 38.680 -34.649 -4.771  1.00 19.53 ?  164 LEU   B HD21 1 
ATOM   6195 H  HD22 . LEU   B 1 164 ? 37.856 -34.081 -6.004  1.00 19.53 ?  164 LEU   B HD22 1 
ATOM   6196 H  HD23 . LEU   B 1 164 ? 37.664 -35.590 -5.547  1.00 19.53 ?  164 LEU   B HD23 1 
ATOM   6197 N  N    . VAL   B 1 165 ? 37.983 -37.008 -10.571 1.00 15.13 ?  165 VAL   B N    1 
ATOM   6198 C  CA   . VAL   B 1 165 ? 37.327 -36.942 -11.872 1.00 16.38 ?  165 VAL   B CA   1 
ATOM   6199 C  C    . VAL   B 1 165 ? 36.410 -38.141 -12.059 1.00 18.01 ?  165 VAL   B C    1 
ATOM   6200 O  O    . VAL   B 1 165 ? 35.253 -38.007 -12.476 1.00 18.73 ?  165 VAL   B O    1 
ATOM   6201 C  CB   . VAL   B 1 165 ? 38.375 -36.853 -12.997 1.00 17.56 ?  165 VAL   B CB   1 
ATOM   6202 C  CG1  . VAL   B 1 165 ? 37.715 -36.968 -14.352 1.00 18.83 ?  165 VAL   B CG1  1 
ATOM   6203 C  CG2  . VAL   B 1 165 ? 39.165 -35.563 -12.891 1.00 17.41 ?  165 VAL   B CG2  1 
ATOM   6204 H  H    . VAL   B 1 165 ? 38.831 -37.153 -10.606 1.00 18.16 ?  165 VAL   B H    1 
ATOM   6205 H  HA   . VAL   B 1 165 ? 36.782 -36.141 -11.912 1.00 19.66 ?  165 VAL   B HA   1 
ATOM   6206 H  HB   . VAL   B 1 165 ? 39.002 -37.585 -12.902 1.00 21.07 ?  165 VAL   B HB   1 
ATOM   6207 H  HG11 . VAL   B 1 165 ? 38.334 -36.663 -15.031 1.00 22.60 ?  165 VAL   B HG11 1 
ATOM   6208 H  HG12 . VAL   B 1 165 ? 37.490 -37.899 -14.509 1.00 22.60 ?  165 VAL   B HG12 1 
ATOM   6209 H  HG13 . VAL   B 1 165 ? 36.914 -36.426 -14.360 1.00 22.60 ?  165 VAL   B HG13 1 
ATOM   6210 H  HG21 . VAL   B 1 165 ? 39.801 -35.517 -13.624 1.00 20.89 ?  165 VAL   B HG21 1 
ATOM   6211 H  HG22 . VAL   B 1 165 ? 38.553 -34.810 -12.940 1.00 20.89 ?  165 VAL   B HG22 1 
ATOM   6212 H  HG23 . VAL   B 1 165 ? 39.639 -35.545 -12.044 1.00 20.89 ?  165 VAL   B HG23 1 
ATOM   6213 N  N    . SER   B 1 166 ? 36.919 -39.334 -11.750 1.00 18.58 ?  166 SER   B N    1 
ATOM   6214 C  CA   . SER   B 1 166 ? 36.168 -40.550 -12.027 1.00 19.74 ?  166 SER   B CA   1 
ATOM   6215 C  C    . SER   B 1 166 ? 34.910 -40.640 -11.178 1.00 20.02 ?  166 SER   B C    1 
ATOM   6216 O  O    . SER   B 1 166 ? 33.941 -41.266 -11.604 1.00 21.58 ?  166 SER   B O    1 
ATOM   6217 C  CB   . SER   B 1 166 ? 37.044 -41.796 -11.853 1.00 20.87 ?  166 SER   B CB   1 
ATOM   6218 O  OG   . SER   B 1 166 ? 37.399 -42.006 -10.496 1.00 20.98 ?  166 SER   B OG   1 
ATOM   6219 H  H    . SER   B 1 166 ? 37.693 -39.464 -11.390 1.00 22.30 ?  166 SER   B H    1 
ATOM   6220 H  HA   . SER   B 1 166 ? 35.889 -40.531 -12.953 1.00 23.70 ?  166 SER   B HA   1 
ATOM   6221 H  HB2  . SER   B 1 166 ? 36.553 -42.572 -12.172 1.00 25.05 ?  166 SER   B HB2  1 
ATOM   6222 H  HB3  . SER   B 1 166 ? 37.853 -41.687 -12.381 1.00 25.05 ?  166 SER   B HB3  1 
ATOM   6223 H  HG   . SER   B 1 166 ? 37.841 -41.354 -10.215 1.00 25.17 ?  166 SER   B HG   1 
ATOM   6224 N  N    . SER   B 1 167 ? 34.890 -40.030 -9.993  1.00 18.90 ?  167 SER   B N    1 
ATOM   6225 C  CA   . SER   B 1 167 ? 33.734 -40.095 -9.107  1.00 18.54 ?  167 SER   B CA   1 
ATOM   6226 C  C    . SER   B 1 167 ? 32.815 -38.879 -9.208  1.00 18.13 ?  167 SER   B C    1 
ATOM   6227 O  O    . SER   B 1 167 ? 31.740 -38.881 -8.598  1.00 18.41 ?  167 SER   B O    1 
ATOM   6228 C  CB   . SER   B 1 167 ? 34.180 -40.269 -7.649  1.00 18.40 ?  167 SER   B CB   1 
ATOM   6229 O  OG   . SER   B 1 167 ? 34.859 -39.111 -7.185  1.00 17.98 ?  167 SER   B OG   1 
ATOM   6230 H  H    . SER   B 1 167 ? 35.543 -39.574 -9.677  1.00 22.68 ?  167 SER   B H    1 
ATOM   6231 H  HA   . SER   B 1 167 ? 33.207 -40.876 -9.344  1.00 22.25 ?  167 SER   B HA   1 
ATOM   6232 H  HB2  . SER   B 1 167 ? 33.396 -40.421 -7.097  1.00 22.08 ?  167 SER   B HB2  1 
ATOM   6233 H  HB3  . SER   B 1 167 ? 34.775 -41.036 -7.593  1.00 22.08 ?  167 SER   B HB3  1 
ATOM   6234 H  HG   . SER   B 1 167 ? 35.539 -38.977 -7.662  1.00 21.58 ?  167 SER   B HG   1 
ATOM   6235 N  N    . PHE   B 1 168 ? 33.194 -37.843 -9.958  1.00 18.07 ?  168 PHE   B N    1 
ATOM   6236 C  CA   . PHE   B 1 168 ? 32.356 -36.646 -10.026 1.00 17.28 ?  168 PHE   B CA   1 
ATOM   6237 C  C    . PHE   B 1 168 ? 31.045 -36.914 -10.759 1.00 15.31 ?  168 PHE   B C    1 
ATOM   6238 O  O    . PHE   B 1 168 ? 30.001 -36.318 -10.428 1.00 16.03 ?  168 PHE   B O    1 
ATOM   6239 C  CB   . PHE   B 1 168 ? 33.112 -35.512 -10.709 1.00 17.98 ?  168 PHE   B CB   1 
ATOM   6240 C  CG   . PHE   B 1 168 ? 32.311 -34.262 -10.825 1.00 18.18 ?  168 PHE   B CG   1 
ATOM   6241 C  CD1  . PHE   B 1 168 ? 32.007 -33.521 -9.692  1.00 19.23 ?  168 PHE   B CD1  1 
ATOM   6242 C  CD2  . PHE   B 1 168 ? 31.842 -33.830 -12.048 1.00 17.75 ?  168 PHE   B CD2  1 
ATOM   6243 C  CE1  . PHE   B 1 168 ? 31.246 -32.373 -9.774  1.00 19.73 ?  168 PHE   B CE1  1 
ATOM   6244 C  CE2  . PHE   B 1 168 ? 31.090 -32.662 -12.146 1.00 18.87 ?  168 PHE   B CE2  1 
ATOM   6245 C  CZ   . PHE   B 1 168 ? 30.790 -31.934 -11.003 1.00 19.13 ?  168 PHE   B CZ   1 
ATOM   6246 H  H    . PHE   B 1 168 ? 33.916 -37.805 -10.423 1.00 21.68 ?  168 PHE   B H    1 
ATOM   6247 H  HA   . PHE   B 1 168 ? 32.136 -36.362 -9.128  1.00 20.74 ?  168 PHE   B HA   1 
ATOM   6248 H  HB2  . PHE   B 1 168 ? 33.905 -35.306 -10.190 1.00 21.58 ?  168 PHE   B HB2  1 
ATOM   6249 H  HB3  . PHE   B 1 168 ? 33.360 -35.785 -11.603 1.00 21.58 ?  168 PHE   B HB3  1 
ATOM   6250 H  HD1  . PHE   B 1 168 ? 32.306 -33.816 -8.861  1.00 23.08 ?  168 PHE   B HD1  1 
ATOM   6251 H  HD2  . PHE   B 1 168 ? 32.042 -34.311 -12.815 1.00 21.30 ?  168 PHE   B HD2  1 
ATOM   6252 H  HE1  . PHE   B 1 168 ? 31.049 -31.888 -9.003  1.00 23.67 ?  168 PHE   B HE1  1 
ATOM   6253 H  HE2  . PHE   B 1 168 ? 30.779 -32.373 -12.975 1.00 22.65 ?  168 PHE   B HE2  1 
ATOM   6254 H  HZ   . PHE   B 1 168 ? 30.280 -31.157 -11.065 1.00 22.95 ?  168 PHE   B HZ   1 
ATOM   6255 N  N    . LEU   B 1 169 ? 31.079 -37.800 -11.750 1.00 15.67 ?  169 LEU   B N    1 
ATOM   6256 C  CA   . LEU   B 1 169 ? 29.904 -38.107 -12.555 1.00 17.63 ?  169 LEU   B CA   1 
ATOM   6257 C  C    . LEU   B 1 169 ? 29.897 -39.538 -13.064 1.00 20.20 ?  169 LEU   B C    1 
ATOM   6258 O  O    . LEU   B 1 169 ? 28.991 -39.944 -13.792 1.00 22.68 ?  169 LEU   B O    1 
ATOM   6259 C  CB   . LEU   B 1 169 ? 29.828 -37.158 -13.747 1.00 19.22 ?  169 LEU   B CB   1 
ATOM   6260 C  CG   . LEU   B 1 169 ? 28.577 -36.285 -13.831 1.00 22.68 ?  169 LEU   B CG   1 
ATOM   6261 C  CD1  . LEU   B 1 169 ? 28.546 -35.559 -15.162 1.00 23.60 ?  169 LEU   B CD1  1 
ATOM   6262 C  CD2  . LEU   B 1 169 ? 27.310 -37.103 -13.631 1.00 23.25 ?  169 LEU   B CD2  1 
ATOM   6263 O  OXT  . LEU   B 1 169 ? 30.807 -40.300 -12.769 1.00 20.70 -1 169 LEU   B OXT  1 
ATOM   6264 H  H    . LEU   B 1 169 ? 31.784 -38.244 -11.982 1.00 18.81 ?  169 LEU   B H    1 
ATOM   6265 H  HA   . LEU   B 1 169 ? 29.119 -37.980 -12.009 1.00 21.16 ?  169 LEU   B HA   1 
ATOM   6266 H  HB2  . LEU   B 1 169 ? 30.593 -36.562 -13.715 1.00 23.07 ?  169 LEU   B HB2  1 
ATOM   6267 H  HB3  . LEU   B 1 169 ? 29.864 -37.682 -14.562 1.00 23.07 ?  169 LEU   B HB3  1 
ATOM   6268 H  HG   . LEU   B 1 169 ? 28.614 -35.615 -13.130 1.00 27.22 ?  169 LEU   B HG   1 
ATOM   6269 H  HD11 . LEU   B 1 169 ? 27.759 -34.992 -15.194 1.00 28.32 ?  169 LEU   B HD11 1 
ATOM   6270 H  HD12 . LEU   B 1 169 ? 29.347 -35.018 -15.244 1.00 28.32 ?  169 LEU   B HD12 1 
ATOM   6271 H  HD13 . LEU   B 1 169 ? 28.513 -36.214 -15.876 1.00 28.32 ?  169 LEU   B HD13 1 
ATOM   6272 H  HD21 . LEU   B 1 169 ? 26.564 -36.639 -14.037 1.00 27.90 ?  169 LEU   B HD21 1 
ATOM   6273 H  HD22 . LEU   B 1 169 ? 27.428 -37.972 -14.048 1.00 27.90 ?  169 LEU   B HD22 1 
ATOM   6274 H  HD23 . LEU   B 1 169 ? 27.156 -37.213 -12.680 1.00 27.90 ?  169 LEU   B HD23 1 
HETATM 6275 N  N2   B A1BAW C 2 .   ? 15.297 1.132   6.355   0.28 11.26 ?  201 A1BAW A N2   1 
HETATM 6276 C  C3   B A1BAW C 2 .   ? 15.587 4.441   5.041   0.28 10.19 ?  201 A1BAW A C3   1 
HETATM 6277 C  C6   B A1BAW C 2 .   ? 15.095 1.094   3.521   0.28 10.95 ?  201 A1BAW A C6   1 
HETATM 6278 C  C9   B A1BAW C 2 .   ? 13.955 -2.348  0.519   0.28 11.86 ?  201 A1BAW A C9   1 
HETATM 6279 C  C12  B A1BAW C 2 .   ? 12.561 -0.283  0.797   0.28 12.54 ?  201 A1BAW A C12  1 
HETATM 6280 C  C1   B A1BAW C 2 .   ? 15.397 4.364   2.555   0.28 11.18 ?  201 A1BAW A C1   1 
HETATM 6281 C  C10  B A1BAW C 2 .   ? 12.803 -3.317  0.535   0.28 12.51 ?  201 A1BAW A C10  1 
HETATM 6282 C  C11  B A1BAW C 2 .   ? 11.225 -0.999  0.843   0.28 13.23 ?  201 A1BAW A C11  1 
HETATM 6283 C  C13  B A1BAW C 2 .   ? 15.287 2.345   4.182   0.28 10.48 ?  201 A1BAW A C13  1 
HETATM 6284 C  C2   B A1BAW C 2 .   ? 15.425 3.712   3.861   0.28 10.95 ?  201 A1BAW A C2   1 
HETATM 6285 C  C4   B A1BAW C 2 .   ? 15.376 2.275   5.601   0.28 10.66 ?  201 A1BAW A C4   1 
HETATM 6286 C  C5   B A1BAW C 2 .   ? 15.127 0.034   5.610   0.28 11.54 ?  201 A1BAW A C5   1 
HETATM 6287 C  C7   B A1BAW C 2 .   ? 15.075 -0.293  1.425   0.28 10.90 ?  201 A1BAW A C7   1 
HETATM 6288 C  C8   B A1BAW C 2 .   ? 13.742 -1.104  1.382   0.28 11.65 ?  201 A1BAW A C8   1 
HETATM 6289 N  N1   B A1BAW C 2 .   ? 15.557 3.547   6.126   0.28 10.76 ?  201 A1BAW A N1   1 
HETATM 6290 N  N3   B A1BAW C 2 .   ? 15.026 -0.071  4.246   0.28 11.56 ?  201 A1BAW A N3   1 
HETATM 6291 N  N4   B A1BAW C 2 .   ? 14.993 0.992   2.145   0.28 11.20 ?  201 A1BAW A N4   1 
HETATM 6292 O  O1   B A1BAW C 2 .   ? 13.403 -1.580  2.652   0.28 12.02 ?  201 A1BAW A O1   1 
HETATM 6293 S  S1   B A1BAW C 2 .   ? 11.229 -2.605  0.031   0.28 13.83 ?  201 A1BAW A S1   1 
HETATM 6294 H  H4   B A1BAW C 2 .   ? 15.707 5.515   5.165   0.28 12.24 ?  201 A1BAW A H4   1 
HETATM 6295 H  H12  B A1BAW C 2 .   ? 14.139 -2.026  -0.531  0.28 14.24 ?  201 A1BAW A H12  1 
HETATM 6296 H  H11  B A1BAW C 2 .   ? 14.868 -2.875  0.840   0.28 14.24 ?  201 A1BAW A H11  1 
HETATM 6297 H  H17  B A1BAW C 2 .   ? 12.463 0.676   1.347   0.28 15.05 ?  201 A1BAW A H17  1 
HETATM 6298 H  H18  B A1BAW C 2 .   ? 12.769 0.032   -0.251  0.28 15.05 ?  201 A1BAW A H18  1 
HETATM 6299 H  H3   B A1BAW C 2 .   ? 15.376 3.643   1.728   0.28 13.41 ?  201 A1BAW A H3   1 
HETATM 6300 H  H1   B A1BAW C 2 .   ? 16.200 5.038   2.371   0.28 13.41 ?  201 A1BAW A H1   1 
HETATM 6301 H  H2   B A1BAW C 2 .   ? 14.480 4.926   2.451   0.28 13.41 ?  201 A1BAW A H2   1 
HETATM 6302 H  H14  B A1BAW C 2 .   ? 12.975 -4.127  -0.191  0.28 15.01 ?  201 A1BAW A H14  1 
HETATM 6303 H  H13  B A1BAW C 2 .   ? 12.671 -3.820  1.501   0.28 15.01 ?  201 A1BAW A H13  1 
HETATM 6304 H  H16  B A1BAW C 2 .   ? 10.931 -1.236  1.876   0.28 15.88 ?  201 A1BAW A H16  1 
HETATM 6305 H  H15  B A1BAW C 2 .   ? 10.393 -0.386  0.441   0.28 15.88 ?  201 A1BAW A H15  1 
HETATM 6306 H  H6   B A1BAW C 2 .   ? 15.056 -0.898  6.210   0.28 13.86 ?  201 A1BAW A H6   1 
HETATM 6307 H  H9   B A1BAW C 2 .   ? 15.443 -0.121  0.389   0.28 13.08 ?  201 A1BAW A H9   1 
HETATM 6308 H  H8   B A1BAW C 2 .   ? 15.856 -0.934  1.882   0.28 13.08 ?  201 A1BAW A H8   1 
HETATM 6309 H  H5   B A1BAW C 2 .   ? 15.642 3.782   7.103   0.28 12.91 ?  201 A1BAW A H5   1 
HETATM 6310 H  H7   B A1BAW C 2 .   ? 14.856 1.833   1.634   0.28 13.44 ?  201 A1BAW A H7   1 
HETATM 6311 H  H10  B A1BAW C 2 .   ? 14.136 -2.083  2.981   0.28 14.43 ?  201 A1BAW A H10  1 
HETATM 6312 CL CL   B CL    D 3 .   ? 15.902 2.650   -0.712  0.28 12.75 ?  202 CL    A CL   1 
HETATM 6313 O  O    . HOH   E 4 .   ? 14.838 -4.688  20.576  1.00 43.60 ?  301 HOH   A O    1 
HETATM 6314 O  O    . HOH   E 4 .   ? 18.542 -2.471  -16.334 1.00 40.75 ?  302 HOH   A O    1 
HETATM 6315 O  O    . HOH   E 4 .   ? 4.752  3.945   0.903   1.00 26.22 ?  303 HOH   A O    1 
HETATM 6316 O  O    . HOH   E 4 .   ? 34.364 -1.876  12.454  1.00 37.30 ?  304 HOH   A O    1 
HETATM 6317 O  O    . HOH   E 4 .   ? 14.011 -4.967  17.506  1.00 25.56 ?  305 HOH   A O    1 
HETATM 6318 O  O    . HOH   E 4 .   ? 8.015  -21.498 3.984   1.00 44.16 ?  306 HOH   A O    1 
HETATM 6319 O  O    . HOH   E 4 .   ? 6.970  -8.174  11.917  1.00 23.92 ?  307 HOH   A O    1 
HETATM 6320 O  O    . HOH   E 4 .   ? 11.768 -10.768 17.119  1.00 27.48 ?  308 HOH   A O    1 
HETATM 6321 O  O    . HOH   E 4 .   ? 15.148 -12.238 18.682  1.00 35.70 ?  309 HOH   A O    1 
HETATM 6322 O  O    . HOH   E 4 .   ? 28.791 0.417   -9.723  1.00 20.47 ?  310 HOH   A O    1 
HETATM 6323 O  O    . HOH   E 4 .   ? 17.124 -18.066 15.120  1.00 24.13 ?  311 HOH   A O    1 
HETATM 6324 O  O    . HOH   E 4 .   ? 22.729 12.500  1.684   1.00 14.40 ?  312 HOH   A O    1 
HETATM 6325 O  O    . HOH   E 4 .   ? 12.120 0.334   14.908  1.00 36.83 ?  313 HOH   A O    1 
HETATM 6326 O  O    . HOH   E 4 .   ? 42.415 10.531  5.198   1.00 19.64 ?  314 HOH   A O    1 
HETATM 6327 O  O    . HOH   E 4 .   ? 30.169 -13.316 -8.531  1.00 19.43 ?  315 HOH   A O    1 
HETATM 6328 O  O    . HOH   E 4 .   ? 17.593 -1.779  0.523   1.00 19.48 ?  316 HOH   A O    1 
HETATM 6329 O  O    . HOH   E 4 .   ? 28.267 -6.325  19.595  1.00 41.28 ?  317 HOH   A O    1 
HETATM 6330 O  O    . HOH   E 4 .   ? 36.093 -5.058  -0.595  1.00 28.01 ?  318 HOH   A O    1 
HETATM 6331 O  O    . HOH   E 4 .   ? 0.706  -4.674  0.311   1.00 31.36 ?  319 HOH   A O    1 
HETATM 6332 O  O    . HOH   E 4 .   ? 33.903 -1.026  -8.930  1.00 27.07 ?  320 HOH   A O    1 
HETATM 6333 O  O    . HOH   E 4 .   ? 14.048 -4.507  -11.796 1.00 32.62 ?  321 HOH   A O    1 
HETATM 6334 O  O    . HOH   E 4 .   ? 28.471 -10.613 -14.031 1.00 40.07 ?  322 HOH   A O    1 
HETATM 6335 O  O    . HOH   E 4 .   ? 26.446 -19.321 -1.805  1.00 13.60 ?  323 HOH   A O    1 
HETATM 6336 O  O    . HOH   E 4 .   ? 14.702 -13.969 16.693  1.00 22.86 ?  324 HOH   A O    1 
HETATM 6337 O  O    . HOH   E 4 .   ? 19.806 -12.570 -8.721  1.00 27.18 ?  325 HOH   A O    1 
HETATM 6338 O  O    . HOH   E 4 .   ? 18.796 -21.985 6.842   1.00 30.39 ?  326 HOH   A O    1 
HETATM 6339 O  O    B HOH   E 4 .   ? 7.489  -5.957  -5.491  0.28 23.56 ?  327 HOH   A O    1 
HETATM 6340 O  O    . HOH   E 4 .   ? 28.188 -0.173  -13.383 1.00 33.91 ?  328 HOH   A O    1 
HETATM 6341 O  O    . HOH   E 4 .   ? 30.998 -18.160 7.772   1.00 19.41 ?  329 HOH   A O    1 
HETATM 6342 O  O    . HOH   E 4 .   ? 37.500 2.763   10.165  1.00 26.39 ?  330 HOH   A O    1 
HETATM 6343 O  O    . HOH   E 4 .   ? 15.157 3.914   17.805  1.00 38.31 ?  331 HOH   A O    1 
HETATM 6344 O  O    . HOH   E 4 .   ? 38.213 10.100  7.111   1.00 26.78 ?  332 HOH   A O    1 
HETATM 6345 O  O    . HOH   E 4 .   ? 8.813  -12.005 17.306  1.00 41.45 ?  333 HOH   A O    1 
HETATM 6346 O  O    . HOH   E 4 .   ? 9.847  -21.351 5.769   1.00 17.70 ?  334 HOH   A O    1 
HETATM 6347 O  O    . HOH   E 4 .   ? 14.423 -0.520  -11.947 1.00 27.88 ?  335 HOH   A O    1 
HETATM 6348 O  O    B HOH   E 4 .   ? 21.292 2.746   0.002   0.28 14.49 ?  336 HOH   A O    1 
HETATM 6349 O  O    . HOH   E 4 .   ? 17.099 -17.820 -4.977  1.00 26.16 ?  337 HOH   A O    1 
HETATM 6350 O  O    . HOH   E 4 .   ? 18.705 -19.374 13.589  1.00 32.11 ?  338 HOH   A O    1 
HETATM 6351 O  O    . HOH   E 4 .   ? 38.538 4.978   6.917   1.00 15.86 ?  339 HOH   A O    1 
HETATM 6352 O  O    . HOH   E 4 .   ? 7.965  -12.680 -0.759  1.00 21.15 ?  340 HOH   A O    1 
HETATM 6353 O  O    B HOH   E 4 .   ? 15.102 7.187   7.459   0.28 19.36 ?  341 HOH   A O    1 
HETATM 6354 O  O    . HOH   E 4 .   ? 27.215 13.708  2.861   1.00 27.99 ?  342 HOH   A O    1 
HETATM 6355 O  O    . HOH   E 4 .   ? 17.003 -19.271 4.919   1.00 14.83 ?  343 HOH   A O    1 
HETATM 6356 O  O    . HOH   E 4 .   ? 26.783 11.358  1.680   1.00 15.58 ?  344 HOH   A O    1 
HETATM 6357 O  O    . HOH   E 4 .   ? 20.554 -19.670 -5.062  1.00 25.25 ?  345 HOH   A O    1 
HETATM 6358 O  O    B HOH   E 4 .   ? 13.320 -1.307  -6.471  0.28 17.53 ?  346 HOH   A O    1 
HETATM 6359 O  O    . HOH   E 4 .   ? 42.476 4.261   5.267   1.00 29.62 ?  347 HOH   A O    1 
HETATM 6360 O  O    B HOH   E 4 .   ? 12.112 -2.067  -3.282  0.28 13.47 ?  348 HOH   A O    1 
HETATM 6361 O  O    . HOH   E 4 .   ? 21.231 -2.386  -2.149  1.00 16.25 ?  349 HOH   A O    1 
HETATM 6362 O  O    . HOH   E 4 .   ? 37.232 -2.806  9.620   1.00 40.15 ?  350 HOH   A O    1 
HETATM 6363 O  O    . HOH   E 4 .   ? 37.334 11.911  4.916   1.00 33.15 ?  351 HOH   A O    1 
HETATM 6364 O  O    A HOH   E 4 .   ? 3.583  -9.495  9.818   0.72 32.29 ?  352 HOH   A O    1 
HETATM 6365 O  O    . HOH   E 4 .   ? 31.677 8.226   14.789  1.00 22.39 ?  353 HOH   A O    1 
HETATM 6366 O  O    . HOH   E 4 .   ? 22.261 -19.239 11.383  1.00 32.95 ?  354 HOH   A O    1 
HETATM 6367 O  O    . HOH   E 4 .   ? 35.749 -12.689 6.787   1.00 15.27 ?  355 HOH   A O    1 
HETATM 6368 O  O    . HOH   E 4 .   ? 39.672 -1.028  -5.241  1.00 19.57 ?  356 HOH   A O    1 
HETATM 6369 O  O    . HOH   E 4 .   ? 21.870 -21.887 8.403   1.00 27.02 ?  357 HOH   A O    1 
HETATM 6370 O  O    . HOH   E 4 .   ? 25.627 -0.845  -7.381  1.00 14.64 ?  358 HOH   A O    1 
HETATM 6371 O  O    A HOH   E 4 .   ? -0.674 -8.520  2.505   0.72 37.65 ?  359 HOH   A O    1 
HETATM 6372 O  O    . HOH   E 4 .   ? 18.570 9.420   9.005   1.00 20.68 ?  360 HOH   A O    1 
HETATM 6373 O  O    . HOH   E 4 .   ? -0.446 -3.049  3.178   1.00 40.28 ?  361 HOH   A O    1 
HETATM 6374 O  O    . HOH   E 4 .   ? 16.478 -22.012 0.987   1.00 26.78 ?  362 HOH   A O    1 
HETATM 6375 O  O    . HOH   E 4 .   ? 33.619 -7.169  4.250   1.00 16.36 ?  363 HOH   A O    1 
HETATM 6376 O  O    . HOH   E 4 .   ? 44.254 7.039   6.409   1.00 25.50 ?  364 HOH   A O    1 
HETATM 6377 O  O    . HOH   E 4 .   ? 14.303 -21.194 -4.183  1.00 29.75 ?  365 HOH   A O    1 
HETATM 6378 O  O    . HOH   E 4 .   ? 13.457 -15.201 -7.333  1.00 27.41 ?  366 HOH   A O    1 
HETATM 6379 O  O    A HOH   E 4 .   ? 14.241 0.555   6.869   0.72 26.01 ?  367 HOH   A O    1 
HETATM 6380 O  O    A HOH   E 4 .   ? 14.593 -3.667  3.159   0.72 15.49 ?  368 HOH   A O    1 
HETATM 6381 O  O    . HOH   E 4 .   ? 23.974 -2.113  -2.080  1.00 10.64 ?  369 HOH   A O    1 
HETATM 6382 O  O    . HOH   E 4 .   ? 31.032 -13.935 -2.492  1.00 13.19 ?  370 HOH   A O    1 
HETATM 6383 O  O    . HOH   E 4 .   ? 31.751 -9.342  -6.664  1.00 21.65 ?  371 HOH   A O    1 
HETATM 6384 O  O    . HOH   E 4 .   ? 30.786 3.076   8.243   1.00 11.72 ?  372 HOH   A O    1 
HETATM 6385 O  O    . HOH   E 4 .   ? 43.812 8.426   -3.157  1.00 24.73 ?  373 HOH   A O    1 
HETATM 6386 O  O    . HOH   E 4 .   ? 22.365 5.337   19.073  1.00 44.60 ?  374 HOH   A O    1 
HETATM 6387 O  O    . HOH   E 4 .   ? 23.871 -15.719 -9.120  1.00 34.40 ?  375 HOH   A O    1 
HETATM 6388 O  O    . HOH   E 4 .   ? 24.550 1.958   -7.082  1.00 19.31 ?  376 HOH   A O    1 
HETATM 6389 O  O    B HOH   E 4 .   ? 6.868  1.594   7.136   0.28 29.37 ?  377 HOH   A O    1 
HETATM 6390 O  O    . HOH   E 4 .   ? 11.552 -10.791 -10.049 1.00 39.72 ?  378 HOH   A O    1 
HETATM 6391 O  O    . HOH   E 4 .   ? 14.445 -24.685 11.607  1.00 31.33 ?  379 HOH   A O    1 
HETATM 6392 O  O    . HOH   E 4 .   ? 24.741 -17.522 12.760  1.00 24.08 ?  380 HOH   A O    1 
HETATM 6393 O  O    . HOH   E 4 .   ? 9.375  -10.478 19.693  1.00 46.42 ?  381 HOH   A O    1 
HETATM 6394 O  O    . HOH   E 4 .   ? 27.531 -10.650 14.011  1.00 16.83 ?  382 HOH   A O    1 
HETATM 6395 O  O    . HOH   E 4 .   ? 31.652 -7.281  -9.869  1.00 21.11 ?  383 HOH   A O    1 
HETATM 6396 O  O    . HOH   E 4 .   ? 18.923 -0.689  -1.640  1.00 13.43 ?  384 HOH   A O    1 
HETATM 6397 O  O    . HOH   E 4 .   ? 11.098 1.597   12.765  1.00 24.06 ?  385 HOH   A O    1 
HETATM 6398 O  O    . HOH   E 4 .   ? 24.315 -7.812  14.432  1.00 17.32 ?  386 HOH   A O    1 
HETATM 6399 O  O    . HOH   E 4 .   ? 24.364 3.536   -1.801  1.00 14.06 ?  387 HOH   A O    1 
HETATM 6400 O  O    . HOH   E 4 .   ? 15.504 11.848  7.980   1.00 26.82 ?  388 HOH   A O    1 
HETATM 6401 O  O    . HOH   E 4 .   ? 27.466 2.316   18.703  1.00 30.10 ?  389 HOH   A O    1 
HETATM 6402 O  O    A HOH   E 4 .   ? 13.235 -1.436  -6.455  0.72 15.00 ?  390 HOH   A O    1 
HETATM 6403 O  O    . HOH   E 4 .   ? 21.711 -13.817 -8.062  1.00 37.91 ?  391 HOH   A O    1 
HETATM 6404 O  O    . HOH   E 4 .   ? 43.300 7.841   2.588   1.00 24.04 ?  392 HOH   A O    1 
HETATM 6405 O  O    A HOH   E 4 .   ? 15.762 -0.960  5.332   0.72 25.12 ?  393 HOH   A O    1 
HETATM 6406 O  O    . HOH   E 4 .   ? 22.623 -11.986 21.842  1.00 44.15 ?  394 HOH   A O    1 
HETATM 6407 O  O    . HOH   E 4 .   ? 21.233 10.307  15.036  1.00 32.77 ?  395 HOH   A O    1 
HETATM 6408 O  O    . HOH   E 4 .   ? 23.430 11.350  4.126   1.00 12.25 ?  396 HOH   A O    1 
HETATM 6409 O  O    . HOH   E 4 .   ? 32.761 -9.257  5.912   1.00 19.45 ?  397 HOH   A O    1 
HETATM 6410 O  O    . HOH   E 4 .   ? 6.491  -5.600  11.229  1.00 22.19 ?  398 HOH   A O    1 
HETATM 6411 O  O    . HOH   E 4 .   ? 37.497 -2.018  5.703   1.00 25.38 ?  399 HOH   A O    1 
HETATM 6412 O  O    . HOH   E 4 .   ? 15.014 -8.066  -9.537  1.00 23.57 ?  400 HOH   A O    1 
HETATM 6413 O  O    . HOH   E 4 .   ? 20.552 -20.011 2.800   1.00 16.75 ?  401 HOH   A O    1 
HETATM 6414 O  O    . HOH   E 4 .   ? 30.737 1.847   16.671  1.00 20.64 ?  402 HOH   A O    1 
HETATM 6415 O  O    . HOH   E 4 .   ? 15.217 -21.590 14.200  1.00 17.36 ?  403 HOH   A O    1 
HETATM 6416 O  O    . HOH   E 4 .   ? 20.081 4.499   -7.455  1.00 20.12 ?  404 HOH   A O    1 
HETATM 6417 O  O    B HOH   E 4 .   ? 14.709 -4.118  3.570   0.28 14.55 ?  405 HOH   A O    1 
HETATM 6418 O  O    . HOH   E 4 .   ? 41.504 1.541   4.841   1.00 36.18 ?  406 HOH   A O    1 
HETATM 6419 O  O    . HOH   E 4 .   ? 5.162  2.609   5.257   1.00 32.29 ?  407 HOH   A O    1 
HETATM 6420 O  O    . HOH   E 4 .   ? 10.391 -22.186 -1.258  1.00 48.49 ?  408 HOH   A O    1 
HETATM 6421 O  O    . HOH   E 4 .   ? 27.199 -6.020  -14.024 1.00 33.87 ?  409 HOH   A O    1 
HETATM 6422 O  O    A HOH   E 4 .   ? 7.643  -6.335  -6.431  0.72 36.46 ?  410 HOH   A O    1 
HETATM 6423 O  O    . HOH   E 4 .   ? 30.089 -10.119 12.959  1.00 20.95 ?  411 HOH   A O    1 
HETATM 6424 O  O    . HOH   E 4 .   ? 10.375 -13.730 -1.591  1.00 16.88 ?  412 HOH   A O    1 
HETATM 6425 O  O    . HOH   E 4 .   ? 26.894 4.127   -0.645  1.00 12.47 ?  413 HOH   A O    1 
HETATM 6426 O  O    . HOH   E 4 .   ? 44.807 -0.635  2.925   1.00 42.57 ?  414 HOH   A O    1 
HETATM 6427 O  O    . HOH   E 4 .   ? 23.887 -20.259 -1.373  1.00 14.99 ?  415 HOH   A O    1 
HETATM 6428 O  O    . HOH   E 4 .   ? 14.056 -23.060 7.438   1.00 18.03 ?  416 HOH   A O    1 
HETATM 6429 O  O    . HOH   E 4 .   ? 38.011 -1.326  -2.013  1.00 19.24 ?  417 HOH   A O    1 
HETATM 6430 O  O    . HOH   E 4 .   ? 24.008 3.944   -4.910  1.00 23.97 ?  418 HOH   A O    1 
HETATM 6431 O  O    A HOH   E 4 .   ? 21.290 3.153   -0.298  0.72 11.53 ?  419 HOH   A O    1 
HETATM 6432 O  O    . HOH   E 4 .   ? 27.145 -3.249  19.275  1.00 32.90 ?  420 HOH   A O    1 
HETATM 6433 O  O    . HOH   E 4 .   ? 40.835 -8.222  -6.740  1.00 35.21 ?  421 HOH   A O    1 
HETATM 6434 O  O    . HOH   E 4 .   ? 16.179 -14.226 20.356  1.00 46.94 ?  422 HOH   A O    1 
HETATM 6435 O  O    . HOH   E 4 .   ? 30.358 -12.954 13.485  1.00 19.41 ?  423 HOH   A O    1 
HETATM 6436 O  O    . HOH   E 4 .   ? 6.762  -3.443  13.016  1.00 31.33 ?  424 HOH   A O    1 
HETATM 6437 O  O    . HOH   E 4 .   ? 32.572 -4.315  -9.913  1.00 28.11 ?  425 HOH   A O    1 
HETATM 6438 O  O    . HOH   E 4 .   ? 27.826 0.828   -7.145  1.00 13.73 ?  426 HOH   A O    1 
HETATM 6439 O  O    . HOH   E 4 .   ? 15.815 2.087   24.857  1.00 50.18 ?  427 HOH   A O    1 
HETATM 6440 O  O    . HOH   E 4 .   ? 16.220 16.615  8.761   1.00 28.06 ?  428 HOH   A O    1 
HETATM 6441 O  O    . HOH   E 4 .   ? 35.018 -5.220  -3.152  1.00 17.70 ?  429 HOH   A O    1 
HETATM 6442 O  O    . HOH   E 4 .   ? 32.505 -10.661 3.186   1.00 29.19 ?  430 HOH   A O    1 
HETATM 6443 O  O    . HOH   E 4 .   ? 30.830 6.234   -12.334 1.00 28.95 ?  431 HOH   A O    1 
HETATM 6444 O  O    . HOH   E 4 .   ? 36.714 -4.944  5.336   1.00 23.11 ?  432 HOH   A O    1 
HETATM 6445 O  O    A HOH   E 4 .   ? 11.019 -0.394  2.011   0.72 27.29 ?  433 HOH   A O    1 
HETATM 6446 O  O    . HOH   E 4 .   ? 22.690 8.073   18.370  1.00 41.61 ?  434 HOH   A O    1 
HETATM 6447 O  O    . HOH   E 4 .   ? 16.051 7.102   3.073   1.00 17.30 ?  435 HOH   A O    1 
HETATM 6448 O  O    B HOH   E 4 .   ? 8.468  3.959   1.646   0.28 18.37 ?  436 HOH   A O    1 
HETATM 6449 O  O    . HOH   E 4 .   ? 21.246 -9.267  21.364  1.00 43.83 ?  437 HOH   A O    1 
HETATM 6450 O  O    . HOH   E 4 .   ? 23.634 -8.042  17.068  1.00 21.12 ?  438 HOH   A O    1 
HETATM 6451 O  O    A HOH   E 4 .   ? 18.804 2.029   -0.694  0.72 12.27 ?  439 HOH   A O    1 
HETATM 6452 O  O    . HOH   E 4 .   ? 37.661 -8.810  -3.564  1.00 24.81 ?  440 HOH   A O    1 
HETATM 6453 O  O    . HOH   E 4 .   ? 23.184 7.687   -3.121  1.00 20.17 ?  441 HOH   A O    1 
HETATM 6454 O  O    . HOH   E 4 .   ? 20.566 -17.792 24.785  1.00 52.49 ?  442 HOH   A O    1 
HETATM 6455 O  O    . HOH   E 4 .   ? 9.393  -16.351 -1.987  1.00 44.81 ?  443 HOH   A O    1 
HETATM 6456 O  O    A HOH   E 4 .   ? 16.196 2.943   -1.374  0.72 15.20 ?  444 HOH   A O    1 
HETATM 6457 O  O    . HOH   E 4 .   ? 18.452 4.841   -15.075 1.00 46.79 ?  445 HOH   A O    1 
HETATM 6458 O  O    . HOH   E 4 .   ? 23.280 -20.947 1.307   1.00 17.23 ?  446 HOH   A O    1 
HETATM 6459 O  O    . HOH   E 4 .   ? 34.378 -8.080  -0.592  1.00 25.55 ?  447 HOH   A O    1 
HETATM 6460 O  O    . HOH   E 4 .   ? 30.573 14.755  2.797   1.00 17.97 ?  448 HOH   A O    1 
HETATM 6461 O  O    . HOH   E 4 .   ? 31.307 -12.777 0.005   1.00 18.33 ?  449 HOH   A O    1 
HETATM 6462 O  O    . HOH   E 4 .   ? 18.433 -16.100 16.445  1.00 35.79 ?  450 HOH   A O    1 
HETATM 6463 O  O    . HOH   E 4 .   ? 21.567 -14.696 17.991  1.00 49.62 ?  451 HOH   A O    1 
HETATM 6464 O  O    B HOH   E 4 .   ? -0.241 -8.357  1.177   0.28 21.47 ?  452 HOH   A O    1 
HETATM 6465 O  O    A HOH   E 4 .   ? -1.456 -4.976  7.755   0.72 36.25 ?  453 HOH   A O    1 
HETATM 6466 O  O    . HOH   E 4 .   ? 19.518 -11.085 24.118  1.00 64.08 ?  454 HOH   A O    1 
HETATM 6467 O  O    A HOH   E 4 .   ? 13.984 -0.352  3.530   0.72 29.90 ?  455 HOH   A O    1 
HETATM 6468 O  O    . HOH   E 4 .   ? 29.755 -16.050 10.613  1.00 33.23 ?  456 HOH   A O    1 
HETATM 6469 O  O    . HOH   E 4 .   ? 27.647 6.986   -6.264  1.00 32.03 ?  457 HOH   A O    1 
HETATM 6470 O  O    . HOH   E 4 .   ? 11.918 -13.423 16.415  1.00 42.51 ?  458 HOH   A O    1 
HETATM 6471 O  O    B HOH   E 4 .   ? 18.761 1.393   -0.491  0.28 14.66 ?  459 HOH   A O    1 
HETATM 6472 O  O    . HOH   E 4 .   ? 32.446 -15.946 10.777  1.00 35.91 ?  460 HOH   A O    1 
HETATM 6473 O  O    . HOH   E 4 .   ? 25.374 8.230   -4.790  1.00 20.60 ?  461 HOH   A O    1 
HETATM 6474 O  O    . HOH   E 4 .   ? 29.718 -2.011  -12.792 1.00 45.28 ?  462 HOH   A O    1 
HETATM 6475 O  O    . HOH   E 4 .   ? 19.876 -17.304 -5.062  1.00 25.12 ?  463 HOH   A O    1 
HETATM 6476 O  O    . HOH   E 4 .   ? 24.944 5.663   20.752  1.00 47.41 ?  464 HOH   A O    1 
HETATM 6477 O  O    . HOH   E 4 .   ? 23.170 -22.295 -3.395  1.00 33.99 ?  465 HOH   A O    1 
HETATM 6478 O  O    . HOH   E 4 .   ? 24.576 14.499  7.898   1.00 31.84 ?  466 HOH   A O    1 
HETATM 6479 O  O    . HOH   E 4 .   ? 26.874 11.626  -1.234  1.00 26.91 ?  467 HOH   A O    1 
HETATM 6480 O  O    . HOH   E 4 .   ? 23.493 13.687  5.524   1.00 18.69 ?  468 HOH   A O    1 
HETATM 6481 O  O    . HOH   E 4 .   ? 15.677 -21.461 3.709   1.00 21.60 ?  469 HOH   A O    1 
HETATM 6482 O  O    . HOH   E 4 .   ? 21.898 5.202   -5.940  1.00 28.77 ?  470 HOH   A O    1 
HETATM 6483 O  O    . HOH   E 4 .   ? 27.544 -11.370 16.520  1.00 35.04 ?  471 HOH   A O    1 
HETATM 6484 O  O    . HOH   E 4 .   ? 18.768 10.743  11.404  1.00 31.41 ?  472 HOH   A O    1 
HETATM 6485 O  O    . HOH   E 4 .   ? 39.571 -7.027  -3.553  1.00 42.72 ?  473 HOH   A O    1 
HETATM 6486 O  O    B HOH   E 4 .   ? 10.010 1.953   -0.289  0.28 24.37 ?  474 HOH   A O    1 
HETATM 6487 O  O    . HOH   E 4 .   ? 25.798 10.786  -3.666  1.00 23.08 ?  475 HOH   A O    1 
HETATM 6488 O  O    . HOH   E 4 .   ? 12.323 1.590   17.405  1.00 39.57 ?  476 HOH   A O    1 
HETATM 6489 O  O    . HOH   E 4 .   ? 10.901 -15.025 -6.016  1.00 34.69 ?  477 HOH   A O    1 
HETATM 6490 O  O    . HOH   E 4 .   ? 13.916 -10.279 -10.783 1.00 33.69 ?  478 HOH   A O    1 
HETATM 6491 O  O    . HOH   E 4 .   ? 20.466 -15.985 -7.335  1.00 29.77 ?  479 HOH   A O    1 
HETATM 6492 O  O    . HOH   E 4 .   ? 18.067 -16.262 -8.710  1.00 39.99 ?  480 HOH   A O    1 
HETATM 6493 O  O    . HOH   E 4 .   ? 17.394 -18.712 19.804  1.00 49.59 ?  481 HOH   A O    1 
HETATM 6494 O  O    . HOH   E 4 .   ? 28.816 8.989   17.485  1.00 36.96 ?  482 HOH   A O    1 
HETATM 6495 O  O    . HOH   E 4 .   ? 35.185 7.408   12.182  1.00 38.88 ?  483 HOH   A O    1 
HETATM 6496 O  O    . HOH   E 4 .   ? 15.601 -17.118 -6.940  1.00 30.85 ?  484 HOH   A O    1 
HETATM 6497 O  O    . HOH   E 4 .   ? 16.793 -20.585 16.200  1.00 26.89 ?  485 HOH   A O    1 
HETATM 6498 O  O    B HOH   E 4 .   ? 3.171  -0.982  -2.730  0.28 26.62 ?  486 HOH   A O    1 
HETATM 6499 O  O    . HOH   E 4 .   ? 30.795 0.637   19.164  1.00 37.67 ?  487 HOH   A O    1 
HETATM 6500 O  O    . HOH   E 4 .   ? 40.853 -3.994  -0.374  1.00 38.46 ?  488 HOH   A O    1 
HETATM 6501 O  O    B HOH   E 4 .   ? 10.472 -1.479  -5.237  0.28 15.56 ?  489 HOH   A O    1 
HETATM 6502 O  O    . HOH   E 4 .   ? 23.124 11.825  -4.037  1.00 18.63 ?  490 HOH   A O    1 
HETATM 6503 O  O    . HOH   E 4 .   ? 41.615 9.204   -4.175  1.00 30.33 ?  491 HOH   A O    1 
HETATM 6504 O  O    . HOH   E 4 .   ? 44.415 10.425  -1.639  1.00 30.22 ?  492 HOH   A O    1 
HETATM 6505 O  O    . HOH   E 4 .   ? 23.280 -12.927 19.346  1.00 45.06 ?  493 HOH   A O    1 
HETATM 6506 O  O    . HOH   E 4 .   ? 28.494 -4.702  -12.314 1.00 34.25 ?  494 HOH   A O    1 
HETATM 6507 O  O    . HOH   E 4 .   ? 15.880 -6.865  -11.696 1.00 42.70 ?  495 HOH   A O    1 
HETATM 6508 O  O    . HOH   E 4 .   ? 18.488 -23.223 1.938   1.00 39.04 ?  496 HOH   A O    1 
HETATM 6509 O  O    . HOH   E 4 .   ? 31.381 -0.631  -10.593 1.00 26.06 ?  497 HOH   A O    1 
HETATM 6510 O  O    . HOH   E 4 .   ? 19.989 -22.301 4.178   1.00 27.57 ?  498 HOH   A O    1 
HETATM 6511 O  O    . HOH   E 4 .   ? 40.407 -0.284  -7.842  1.00 33.20 ?  499 HOH   A O    1 
HETATM 6512 O  O    . HOH   E 4 .   ? 39.126 2.387   7.574   1.00 31.23 ?  500 HOH   A O    1 
HETATM 6513 O  O    . HOH   E 4 .   ? 14.101 -25.367 8.896   1.00 28.66 ?  501 HOH   A O    1 
HETATM 6514 O  O    . HOH   E 4 .   ? 28.581 -7.896  -15.254 1.00 41.92 ?  502 HOH   A O    1 
HETATM 6515 O  O    . HOH   E 4 .   ? 16.135 -23.322 5.697   1.00 27.93 ?  503 HOH   A O    1 
HETATM 6516 O  O    . HOH   E 4 .   ? 30.665 -5.852  -11.838 1.00 43.69 ?  504 HOH   A O    1 
HETATM 6517 O  O    . HOH   E 4 .   ? 8.118  -3.058  -5.649  1.00 50.50 ?  505 HOH   A O    1 
HETATM 6518 O  O    . HOH   E 4 .   ? 37.377 -6.692  7.425   1.00 22.84 ?  506 HOH   A O    1 
HETATM 6519 O  O    . HOH   E 4 .   ? 30.620 5.852   -14.684 1.00 36.61 ?  507 HOH   A O    1 
HETATM 6520 O  O    . HOH   E 4 .   ? 23.076 -23.737 1.657   1.00 29.68 ?  508 HOH   A O    1 
HETATM 6521 O  O    . HOH   E 4 .   ? 28.922 14.422  0.946   1.00 45.90 ?  509 HOH   A O    1 
HETATM 6522 O  O    . HOH   E 4 .   ? 39.500 -0.016  6.524   1.00 27.31 ?  510 HOH   A O    1 
HETATM 6523 O  O    B HOH   E 4 .   ? 14.747 8.029   4.897   0.28 22.02 ?  511 HOH   A O    1 
HETATM 6524 O  O    . HOH   E 4 .   ? 38.027 13.859  6.720   1.00 48.22 ?  512 HOH   A O    1 
HETATM 6525 O  O    B HOH   E 4 .   ? 5.804  -1.960  -5.969  0.28 21.73 ?  513 HOH   A O    1 
HETATM 6526 O  O    . HOH   E 4 .   ? 36.437 -6.506  10.132  1.00 43.04 ?  514 HOH   A O    1 
HETATM 6527 O  O    . HOH   E 4 .   ? 21.996 -24.050 4.456   1.00 25.15 ?  515 HOH   A O    1 
HETATM 6528 O  O    . HOH   E 4 .   ? 17.274 -6.799  -14.082 1.00 38.88 ?  516 HOH   A O    1 
HETATM 6529 O  O    A HOH   E 4 .   ? 14.804 8.635   4.968   0.72 38.57 ?  517 HOH   A O    1 
HETATM 6530 O  O    . HOH   E 4 .   ? 24.019 9.002   -7.245  1.00 31.15 ?  518 HOH   A O    1 
HETATM 6531 O  O    . HOH   E 4 .   ? 16.355 -21.124 18.786  1.00 32.27 ?  519 HOH   A O    1 
HETATM 6532 O  O    . HOH   E 4 .   ? 15.857 -12.294 27.530  1.00 42.95 ?  520 HOH   A O    1 
HETATM 6533 O  O    . HOH   E 4 .   ? 14.635 -22.785 19.869  1.00 33.20 ?  521 HOH   A O    1 
HETATM 6534 O  O    . HOH   F 4 .   ? 29.802 -22.408 5.452   1.00 19.31 ?  201 HOH   B O    1 
HETATM 6535 O  O    . HOH   F 4 .   ? 48.088 -6.879  15.484  1.00 34.44 ?  202 HOH   B O    1 
HETATM 6536 O  O    . HOH   F 4 .   ? 59.108 -18.694 6.726   1.00 36.78 ?  203 HOH   B O    1 
HETATM 6537 O  O    . HOH   F 4 .   ? 27.822 -41.806 -15.117 1.00 34.15 ?  204 HOH   B O    1 
HETATM 6538 O  O    . HOH   F 4 .   ? 27.694 -29.185 -1.898  1.00 33.39 ?  205 HOH   B O    1 
HETATM 6539 O  O    . HOH   F 4 .   ? 47.355 -7.426  -4.023  1.00 38.98 ?  206 HOH   B O    1 
HETATM 6540 O  O    . HOH   F 4 .   ? 41.809 -35.850 -17.409 1.00 27.43 ?  207 HOH   B O    1 
HETATM 6541 O  O    . HOH   F 4 .   ? 49.287 -22.682 -19.799 1.00 48.45 ?  208 HOH   B O    1 
HETATM 6542 O  O    . HOH   F 4 .   ? 37.895 -39.435 -0.300  1.00 37.43 ?  209 HOH   B O    1 
HETATM 6543 O  O    . HOH   F 4 .   ? 52.850 -13.406 -20.369 1.00 33.92 ?  210 HOH   B O    1 
HETATM 6544 O  O    . HOH   F 4 .   ? 56.282 -19.718 7.152   1.00 31.50 ?  211 HOH   B O    1 
HETATM 6545 O  O    . HOH   F 4 .   ? 41.361 -7.730  5.431   1.00 37.22 ?  212 HOH   B O    1 
HETATM 6546 O  O    . HOH   F 4 .   ? 50.252 -3.348  7.149   1.00 32.06 ?  213 HOH   B O    1 
HETATM 6547 O  O    . HOH   F 4 .   ? 55.323 -16.466 -14.378 1.00 35.01 ?  214 HOH   B O    1 
HETATM 6548 O  O    . HOH   F 4 .   ? 54.373 -9.346  -8.850  1.00 19.05 ?  215 HOH   B O    1 
HETATM 6549 O  O    . HOH   F 4 .   ? 30.179 -40.976 -8.213  1.00 15.97 ?  216 HOH   B O    1 
HETATM 6550 O  O    . HOH   F 4 .   ? 58.204 -12.922 8.353   1.00 32.23 ?  217 HOH   B O    1 
HETATM 6551 O  O    . HOH   F 4 .   ? 50.687 -6.119  0.124   1.00 26.13 ?  218 HOH   B O    1 
HETATM 6552 O  O    . HOH   F 4 .   ? 57.082 -26.800 -7.672  1.00 38.78 ?  219 HOH   B O    1 
HETATM 6553 O  O    . HOH   F 4 .   ? 35.882 -43.183 -8.645  1.00 27.94 ?  220 HOH   B O    1 
HETATM 6554 O  O    . HOH   F 4 .   ? 44.358 -7.253  2.064   1.00 34.24 ?  221 HOH   B O    1 
HETATM 6555 O  O    . HOH   F 4 .   ? 57.334 -16.219 -12.204 1.00 18.91 ?  222 HOH   B O    1 
HETATM 6556 O  O    . HOH   F 4 .   ? 29.728 -34.187 -0.438  1.00 33.92 ?  223 HOH   B O    1 
HETATM 6557 O  O    . HOH   F 4 .   ? 45.113 -34.924 6.809   1.00 40.35 ?  224 HOH   B O    1 
HETATM 6558 O  O    . HOH   F 4 .   ? 40.578 -16.041 14.061  1.00 25.24 ?  225 HOH   B O    1 
HETATM 6559 O  O    . HOH   F 4 .   ? 48.482 -36.430 -15.562 1.00 40.84 ?  226 HOH   B O    1 
HETATM 6560 O  O    . HOH   F 4 .   ? 29.870 -26.328 3.937   1.00 26.73 ?  227 HOH   B O    1 
HETATM 6561 O  O    . HOH   F 4 .   ? 56.635 -30.724 -7.795  1.00 27.82 ?  228 HOH   B O    1 
HETATM 6562 O  O    . HOH   F 4 .   ? 34.496 -36.329 -7.271  1.00 17.47 ?  229 HOH   B O    1 
HETATM 6563 O  O    . HOH   F 4 .   ? 37.051 -19.744 -18.080 1.00 38.91 ?  230 HOH   B O    1 
HETATM 6564 O  O    . HOH   F 4 .   ? 57.677 -24.381 4.977   1.00 33.54 ?  231 HOH   B O    1 
HETATM 6565 O  O    . HOH   F 4 .   ? 41.475 -39.097 -14.986 1.00 21.22 ?  232 HOH   B O    1 
HETATM 6566 O  O    . HOH   F 4 .   ? 51.632 -6.491  4.391   1.00 19.67 ?  233 HOH   B O    1 
HETATM 6567 O  O    . HOH   F 4 .   ? 39.273 -10.904 6.089   1.00 25.75 ?  234 HOH   B O    1 
HETATM 6568 O  O    . HOH   F 4 .   ? 32.802 -43.731 -11.402 1.00 19.37 ?  235 HOH   B O    1 
HETATM 6569 O  O    . HOH   F 4 .   ? 30.808 -28.762 4.199   1.00 24.21 ?  236 HOH   B O    1 
HETATM 6570 O  O    . HOH   F 4 .   ? 35.051 -7.989  -3.083  1.00 18.21 ?  237 HOH   B O    1 
HETATM 6571 O  O    . HOH   F 4 .   ? 41.362 -9.627  13.003  1.00 22.12 ?  238 HOH   B O    1 
HETATM 6572 O  O    . HOH   F 4 .   ? 28.324 -19.661 -13.101 1.00 23.37 ?  239 HOH   B O    1 
HETATM 6573 O  O    . HOH   F 4 .   ? 44.942 -43.455 -10.600 1.00 26.56 ?  240 HOH   B O    1 
HETATM 6574 O  O    . HOH   F 4 .   ? 50.661 -12.959 -0.525  1.00 11.70 ?  241 HOH   B O    1 
HETATM 6575 O  O    . HOH   F 4 .   ? 42.513 -25.347 2.562   1.00 14.76 ?  242 HOH   B O    1 
HETATM 6576 O  O    . HOH   F 4 .   ? 25.415 -25.955 -1.388  1.00 31.24 ?  243 HOH   B O    1 
HETATM 6577 O  O    . HOH   F 4 .   ? 51.540 -13.869 10.902  1.00 28.04 ?  244 HOH   B O    1 
HETATM 6578 O  O    . HOH   F 4 .   ? 43.050 -43.174 -8.321  1.00 27.27 ?  245 HOH   B O    1 
HETATM 6579 O  O    . HOH   F 4 .   ? 42.603 -22.857 3.798   1.00 11.52 ?  246 HOH   B O    1 
HETATM 6580 O  O    . HOH   F 4 .   ? 44.465 -27.723 -0.760  1.00 21.96 ?  247 HOH   B O    1 
HETATM 6581 O  O    . HOH   F 4 .   ? 41.833 -23.522 9.229   1.00 16.39 ?  248 HOH   B O    1 
HETATM 6582 O  O    . HOH   F 4 .   ? 34.868 -24.630 13.810  1.00 28.56 ?  249 HOH   B O    1 
HETATM 6583 O  O    . HOH   F 4 .   ? 34.178 -18.533 11.363  1.00 22.77 ?  250 HOH   B O    1 
HETATM 6584 O  O    . HOH   F 4 .   ? 46.352 -1.561  13.220  1.00 29.26 ?  251 HOH   B O    1 
HETATM 6585 O  O    . HOH   F 4 .   ? 57.530 -24.373 -3.876  1.00 21.23 ?  252 HOH   B O    1 
HETATM 6586 O  O    . HOH   F 4 .   ? 39.450 -11.117 0.286   1.00 16.88 ?  253 HOH   B O    1 
HETATM 6587 O  O    . HOH   F 4 .   ? 40.244 -12.736 -11.539 1.00 15.11 ?  254 HOH   B O    1 
HETATM 6588 O  O    . HOH   F 4 .   ? 43.144 -32.310 -17.139 1.00 22.82 ?  255 HOH   B O    1 
HETATM 6589 O  O    . HOH   F 4 .   ? 29.680 -25.202 -10.842 1.00 15.71 ?  256 HOH   B O    1 
HETATM 6590 O  O    . HOH   F 4 .   ? 38.901 -12.044 12.310  1.00 31.42 ?  257 HOH   B O    1 
HETATM 6591 O  O    . HOH   F 4 .   ? 30.833 -15.759 2.637   1.00 13.46 ?  258 HOH   B O    1 
HETATM 6592 O  O    . HOH   F 4 .   ? 58.096 -10.611 -4.106  1.00 19.50 ?  259 HOH   B O    1 
HETATM 6593 O  O    . HOH   F 4 .   ? 27.113 -31.809 -10.013 1.00 20.62 ?  260 HOH   B O    1 
HETATM 6594 O  O    . HOH   F 4 .   ? 31.753 -17.942 -14.519 1.00 29.94 ?  261 HOH   B O    1 
HETATM 6595 O  O    . HOH   F 4 .   ? 56.919 -8.656  8.332   1.00 20.38 ?  262 HOH   B O    1 
HETATM 6596 O  O    . HOH   F 4 .   ? 47.950 -22.748 5.770   1.00 16.88 ?  263 HOH   B O    1 
HETATM 6597 O  O    . HOH   F 4 .   ? 34.869 -33.300 -19.241 1.00 28.74 ?  264 HOH   B O    1 
HETATM 6598 O  O    . HOH   F 4 .   ? 49.268 -28.657 -6.972  1.00 15.30 ?  265 HOH   B O    1 
HETATM 6599 O  O    . HOH   F 4 .   ? 28.250 -34.323 -9.513  1.00 17.80 ?  266 HOH   B O    1 
HETATM 6600 O  O    . HOH   F 4 .   ? 57.429 -9.220  1.342   1.00 19.95 ?  267 HOH   B O    1 
HETATM 6601 O  O    . HOH   F 4 .   ? 28.448 -30.804 -14.782 1.00 28.21 ?  268 HOH   B O    1 
HETATM 6602 O  O    . HOH   F 4 .   ? 38.400 -11.041 -2.258  1.00 18.78 ?  269 HOH   B O    1 
HETATM 6603 O  O    . HOH   F 4 .   ? 33.476 -17.026 8.012   1.00 18.91 ?  270 HOH   B O    1 
HETATM 6604 O  O    . HOH   F 4 .   ? 43.284 -15.764 -12.200 1.00 13.89 ?  271 HOH   B O    1 
HETATM 6605 O  O    . HOH   F 4 .   ? 42.317 -9.900  9.293   1.00 20.87 ?  272 HOH   B O    1 
HETATM 6606 O  O    . HOH   F 4 .   ? 50.944 -39.892 -8.346  1.00 27.78 ?  273 HOH   B O    1 
HETATM 6607 O  O    . HOH   F 4 .   ? 34.432 -12.811 2.569   1.00 21.75 ?  274 HOH   B O    1 
HETATM 6608 O  O    . HOH   F 4 .   ? 56.104 -23.439 -14.771 1.00 26.33 ?  275 HOH   B O    1 
HETATM 6609 O  O    . HOH   F 4 .   ? 46.559 -31.230 -4.846  1.00 18.74 ?  276 HOH   B O    1 
HETATM 6610 O  O    . HOH   F 4 .   ? 43.543 -15.336 18.174  1.00 28.97 ?  277 HOH   B O    1 
HETATM 6611 O  O    . HOH   F 4 .   ? 49.738 -0.497  10.220  1.00 31.34 ?  278 HOH   B O    1 
HETATM 6612 O  O    . HOH   F 4 .   ? 41.148 -5.527  11.504  1.00 43.48 ?  279 HOH   B O    1 
HETATM 6613 O  O    . HOH   F 4 .   ? 27.918 -22.884 -8.013  1.00 16.54 ?  280 HOH   B O    1 
HETATM 6614 O  O    . HOH   F 4 .   ? 37.350 -35.626 7.125   1.00 31.32 ?  281 HOH   B O    1 
HETATM 6615 O  O    . HOH   F 4 .   ? 30.584 -42.180 -10.642 1.00 26.99 ?  282 HOH   B O    1 
HETATM 6616 O  O    . HOH   F 4 .   ? 47.896 -24.374 -17.862 1.00 31.51 ?  283 HOH   B O    1 
HETATM 6617 O  O    . HOH   F 4 .   ? 57.070 -12.041 12.256  1.00 36.01 ?  284 HOH   B O    1 
HETATM 6618 O  O    . HOH   F 4 .   ? 42.172 -10.063 -14.984 1.00 33.71 ?  285 HOH   B O    1 
HETATM 6619 O  O    . HOH   F 4 .   ? 46.826 -29.495 9.743   1.00 30.67 ?  286 HOH   B O    1 
HETATM 6620 O  O    . HOH   F 4 .   ? 48.673 -20.012 5.847   1.00 13.65 ?  287 HOH   B O    1 
HETATM 6621 O  O    . HOH   F 4 .   ? 48.367 -25.025 3.041   1.00 12.99 ?  288 HOH   B O    1 
HETATM 6622 O  O    . HOH   F 4 .   ? 33.453 -15.304 -13.972 1.00 20.52 ?  289 HOH   B O    1 
HETATM 6623 O  O    . HOH   F 4 .   ? 27.551 -26.755 -15.723 1.00 32.47 ?  290 HOH   B O    1 
HETATM 6624 O  O    . HOH   F 4 .   ? 42.763 -20.282 -20.809 1.00 37.13 ?  291 HOH   B O    1 
HETATM 6625 O  O    . HOH   F 4 .   ? 52.492 -10.456 12.919  1.00 22.94 ?  292 HOH   B O    1 
HETATM 6626 O  O    . HOH   F 4 .   ? 42.365 -34.648 3.755   1.00 24.05 ?  293 HOH   B O    1 
HETATM 6627 O  O    . HOH   F 4 .   ? 62.717 -20.178 -0.980  1.00 38.55 ?  294 HOH   B O    1 
HETATM 6628 O  O    . HOH   F 4 .   ? 57.580 -22.084 2.998   1.00 25.27 ?  295 HOH   B O    1 
HETATM 6629 O  O    . HOH   F 4 .   ? 45.336 -33.320 -16.001 1.00 22.66 ?  296 HOH   B O    1 
HETATM 6630 O  O    . HOH   F 4 .   ? 40.170 -10.820 -9.557  1.00 16.17 ?  297 HOH   B O    1 
HETATM 6631 O  O    . HOH   F 4 .   ? 47.034 -33.944 -4.674  1.00 16.50 ?  298 HOH   B O    1 
HETATM 6632 O  O    . HOH   F 4 .   ? 36.737 -12.761 -1.518  1.00 26.09 ?  299 HOH   B O    1 
HETATM 6633 O  O    . HOH   F 4 .   ? 51.180 -37.551 -9.666  1.00 23.93 ?  300 HOH   B O    1 
HETATM 6634 O  O    . HOH   F 4 .   ? 45.882 -40.365 -3.674  1.00 27.34 ?  301 HOH   B O    1 
HETATM 6635 O  O    . HOH   F 4 .   ? 44.566 -27.438 1.925   1.00 14.72 ?  302 HOH   B O    1 
HETATM 6636 O  O    . HOH   F 4 .   ? 59.730 -15.338 8.127   1.00 32.09 ?  303 HOH   B O    1 
HETATM 6637 O  O    . HOH   F 4 .   ? 35.026 -33.540 4.425   1.00 25.99 ?  304 HOH   B O    1 
HETATM 6638 O  O    . HOH   F 4 .   ? 52.559 -35.577 -8.663  1.00 28.44 ?  305 HOH   B O    1 
HETATM 6639 O  O    . HOH   F 4 .   ? 25.915 -21.476 -3.529  1.00 15.28 ?  306 HOH   B O    1 
HETATM 6640 O  O    . HOH   F 4 .   ? 42.636 -12.236 -18.526 1.00 30.30 ?  307 HOH   B O    1 
HETATM 6641 O  O    . HOH   F 4 .   ? 32.766 -34.559 -5.930  1.00 16.68 ?  308 HOH   B O    1 
HETATM 6642 O  O    . HOH   F 4 .   ? 37.512 -18.240 13.079  1.00 26.98 ?  309 HOH   B O    1 
HETATM 6643 O  O    . HOH   F 4 .   ? 53.133 -16.061 -12.780 1.00 28.83 ?  310 HOH   B O    1 
HETATM 6644 O  O    . HOH   F 4 .   ? 49.970 -24.590 5.803   1.00 33.57 ?  311 HOH   B O    1 
HETATM 6645 O  O    . HOH   F 4 .   ? 41.172 -24.423 15.711  1.00 40.55 ?  312 HOH   B O    1 
HETATM 6646 O  O    . HOH   F 4 .   ? 53.396 -30.165 4.464   1.00 18.12 ?  313 HOH   B O    1 
HETATM 6647 O  O    . HOH   F 4 .   ? 48.021 -32.590 -16.636 1.00 42.07 ?  314 HOH   B O    1 
HETATM 6648 O  O    . HOH   F 4 .   ? 43.991 -29.308 -4.712  1.00 23.15 ?  315 HOH   B O    1 
HETATM 6649 O  O    . HOH   F 4 .   ? 41.673 -8.098  1.362   1.00 24.01 ?  316 HOH   B O    1 
HETATM 6650 O  O    . HOH   F 4 .   ? 37.774 -10.245 -10.754 1.00 16.38 ?  317 HOH   B O    1 
HETATM 6651 O  O    . HOH   F 4 .   ? 52.496 -29.195 -13.080 1.00 23.36 ?  318 HOH   B O    1 
HETATM 6652 O  O    . HOH   F 4 .   ? 26.308 -21.018 -6.259  1.00 15.87 ?  319 HOH   B O    1 
HETATM 6653 O  O    . HOH   F 4 .   ? 43.173 -21.426 10.605  1.00 15.62 ?  320 HOH   B O    1 
HETATM 6654 O  O    . HOH   F 4 .   ? 62.648 -13.563 4.669   1.00 26.47 ?  321 HOH   B O    1 
HETATM 6655 O  O    . HOH   F 4 .   ? 38.306 -12.779 7.886   1.00 18.70 ?  322 HOH   B O    1 
HETATM 6656 O  O    . HOH   F 4 .   ? 39.403 -23.408 -20.293 1.00 35.96 ?  323 HOH   B O    1 
HETATM 6657 O  O    . HOH   F 4 .   ? 51.668 -5.940  -7.967  1.00 47.39 ?  324 HOH   B O    1 
HETATM 6658 O  O    . HOH   F 4 .   ? 38.280 -9.348  -13.273 1.00 26.99 ?  325 HOH   B O    1 
HETATM 6659 O  O    . HOH   F 4 .   ? 37.191 -30.521 -21.114 1.00 29.75 ?  326 HOH   B O    1 
HETATM 6660 O  O    . HOH   F 4 .   ? 44.536 -24.602 9.513   1.00 18.71 ?  327 HOH   B O    1 
HETATM 6661 O  O    . HOH   F 4 .   ? 36.678 -12.422 4.265   1.00 18.01 ?  328 HOH   B O    1 
HETATM 6662 O  O    . HOH   F 4 .   ? 59.860 -17.225 -10.588 1.00 34.12 ?  329 HOH   B O    1 
HETATM 6663 O  O    . HOH   F 4 .   ? 33.660 -31.136 11.040  1.00 34.11 ?  330 HOH   B O    1 
HETATM 6664 O  O    . HOH   F 4 .   ? 45.695 -36.234 -16.152 1.00 33.03 ?  331 HOH   B O    1 
HETATM 6665 O  O    . HOH   F 4 .   ? 43.077 -34.572 0.011   1.00 20.05 ?  332 HOH   B O    1 
HETATM 6666 O  O    . HOH   F 4 .   ? 51.372 -32.880 -10.879 1.00 37.41 ?  333 HOH   B O    1 
HETATM 6667 O  O    . HOH   F 4 .   ? 42.847 -43.443 -14.428 1.00 42.30 ?  334 HOH   B O    1 
HETATM 6668 O  O    . HOH   F 4 .   ? 53.610 -12.549 -22.310 1.00 31.21 ?  335 HOH   B O    1 
HETATM 6669 O  O    . HOH   F 4 .   ? 27.871 -14.773 -9.485  1.00 33.89 ?  336 HOH   B O    1 
HETATM 6670 O  O    . HOH   F 4 .   ? 44.144 -1.699  7.571   1.00 42.95 ?  337 HOH   B O    1 
HETATM 6671 O  O    . HOH   F 4 .   ? 47.109 -24.498 8.097   1.00 25.93 ?  338 HOH   B O    1 
HETATM 6672 O  O    . HOH   F 4 .   ? 48.515 -11.846 -13.815 1.00 25.59 ?  339 HOH   B O    1 
HETATM 6673 O  O    . HOH   F 4 .   ? 47.423 -27.403 1.968   1.00 14.88 ?  340 HOH   B O    1 
HETATM 6674 O  O    . HOH   F 4 .   ? 46.836 -19.880 12.204  1.00 30.28 ?  341 HOH   B O    1 
HETATM 6675 O  O    . HOH   F 4 .   ? 37.009 -45.124 -9.833  1.00 36.10 ?  342 HOH   B O    1 
HETATM 6676 O  O    . HOH   F 4 .   ? 36.963 -15.032 -16.538 1.00 39.34 ?  343 HOH   B O    1 
HETATM 6677 O  O    . HOH   F 4 .   ? 32.973 -14.701 1.008   1.00 17.55 ?  344 HOH   B O    1 
HETATM 6678 O  O    . HOH   F 4 .   ? 28.841 -42.920 -12.384 1.00 34.63 ?  345 HOH   B O    1 
HETATM 6679 O  O    . HOH   F 4 .   ? 39.712 -44.257 -11.220 1.00 37.05 ?  346 HOH   B O    1 
HETATM 6680 O  O    . HOH   F 4 .   ? 38.368 -12.265 -16.282 1.00 38.46 ?  347 HOH   B O    1 
HETATM 6681 O  O    . HOH   F 4 .   ? 40.349 -43.399 -9.183  1.00 25.97 ?  348 HOH   B O    1 
HETATM 6682 O  O    . HOH   F 4 .   ? 55.569 -8.260  10.743  1.00 24.83 ?  349 HOH   B O    1 
HETATM 6683 O  O    . HOH   F 4 .   ? 27.747 -26.593 -0.645  1.00 28.64 ?  350 HOH   B O    1 
HETATM 6684 O  O    . HOH   F 4 .   ? 33.689 -9.223  -8.808  1.00 31.83 ?  351 HOH   B O    1 
HETATM 6685 O  O    . HOH   F 4 .   ? 62.460 -20.074 -4.945  1.00 46.05 ?  352 HOH   B O    1 
HETATM 6686 O  O    . HOH   F 4 .   ? 38.533 -22.306 15.032  1.00 40.13 ?  353 HOH   B O    1 
HETATM 6687 O  O    . HOH   F 4 .   ? 36.044 -8.570  -9.682  1.00 34.85 ?  354 HOH   B O    1 
HETATM 6688 O  O    . HOH   F 4 .   ? 44.113 -37.301 -17.885 1.00 32.21 ?  355 HOH   B O    1 
HETATM 6689 O  O    . HOH   F 4 .   ? 23.174 -23.662 6.751   1.00 33.81 ?  356 HOH   B O    1 
HETATM 6690 O  O    . HOH   F 4 .   ? 56.554 -7.312  3.028   1.00 28.53 ?  357 HOH   B O    1 
HETATM 6691 O  O    . HOH   F 4 .   ? 34.602 -10.324 7.476   1.00 24.15 ?  358 HOH   B O    1 
HETATM 6692 O  O    . HOH   F 4 .   ? 43.087 -12.715 -21.244 1.00 40.94 ?  359 HOH   B O    1 
HETATM 6693 O  O    . HOH   F 4 .   ? 61.468 -19.888 1.499   1.00 30.89 ?  360 HOH   B O    1 
HETATM 6694 O  O    . HOH   F 4 .   ? 34.114 -7.744  11.420  1.00 41.88 ?  361 HOH   B O    1 
HETATM 6695 O  O    . HOH   F 4 .   ? 40.213 -8.785  9.885   1.00 37.48 ?  362 HOH   B O    1 
HETATM 6696 O  O    . HOH   F 4 .   ? 27.116 -25.942 -11.463 1.00 32.27 ?  363 HOH   B O    1 
HETATM 6697 O  O    . HOH   F 4 .   ? 56.888 -21.505 -16.470 1.00 39.47 ?  364 HOH   B O    1 
HETATM 6698 O  O    . HOH   F 4 .   ? 54.129 -5.703  2.956   1.00 36.14 ?  365 HOH   B O    1 
HETATM 6699 O  O    . HOH   F 4 .   ? 58.907 -10.514 9.101   1.00 37.62 ?  366 HOH   B O    1 
HETATM 6700 O  O    . HOH   F 4 .   ? 32.477 -23.569 14.045  1.00 37.46 ?  367 HOH   B O    1 
HETATM 6701 O  O    . HOH   F 4 .   ? 36.205 -8.735  8.931   1.00 36.75 ?  368 HOH   B O    1 
HETATM 6702 O  O    . HOH   F 4 .   ? 39.837 -7.058  7.801   1.00 42.24 ?  369 HOH   B O    1 
HETATM 6703 O  O    . HOH   F 4 .   ? 39.902 -11.374 -14.002 1.00 30.70 ?  370 HOH   B O    1 
HETATM 6704 O  O    . HOH   F 4 .   ? 41.779 -10.025 -17.478 1.00 54.27 ?  371 HOH   B O    1 
HETATM 6705 O  O    . HOH   F 4 .   ? 48.402 -26.491 8.715   1.00 37.26 ?  372 HOH   B O    1 
HETATM 6706 O  O    . HOH   F 4 .   ? 51.996 -12.917 13.279  1.00 32.39 ?  373 HOH   B O    1 
HETATM 6707 O  O    . HOH   F 4 .   ? 55.966 -7.812  -0.567  1.00 34.59 ?  374 HOH   B O    1 
HETATM 6708 O  O    . HOH   F 4 .   ? 38.014 -10.600 10.034  1.00 29.31 ?  375 HOH   B O    1 
HETATM 6709 O  O    . HOH   F 4 .   ? 44.030 -5.638  -3.557  1.00 43.80 ?  376 HOH   B O    1 
HETATM 6710 O  O    . HOH   F 4 .   ? 41.756 -6.782  -4.872  1.00 46.62 ?  377 HOH   B O    1 
HETATM 6711 O  O    . HOH   F 4 .   ? 63.016 -12.346 6.826   1.00 38.58 ?  378 HOH   B O    1 
HETATM 6712 O  O    . HOH   F 4 .   ? 36.503 -22.806 13.252  1.00 24.09 ?  379 HOH   B O    1 
HETATM 6713 O  O    . HOH   F 4 .   ? 42.554 -17.042 -23.240 1.00 43.14 ?  380 HOH   B O    1 
HETATM 6714 O  O    . HOH   F 4 .   ? 52.772 -29.879 7.100   1.00 23.71 ?  381 HOH   B O    1 
HETATM 6715 O  O    . HOH   F 4 .   ? 40.103 -7.589  3.174   1.00 33.18 ?  382 HOH   B O    1 
HETATM 6716 O  O    . HOH   F 4 .   ? 39.704 -14.055 15.700  1.00 48.52 ?  383 HOH   B O    1 
HETATM 6717 O  O    . HOH   F 4 .   ? 60.420 -22.282 2.730   1.00 46.73 ?  384 HOH   B O    1 
HETATM 6718 O  O    . HOH   F 4 .   ? 35.393 -33.702 7.224   1.00 41.46 ?  385 HOH   B O    1 
HETATM 6719 O  O    . HOH   F 4 .   ? 40.968 -9.748  15.752  1.00 49.84 ?  386 HOH   B O    1 
HETATM 6720 O  O    . HOH   F 4 .   ? 23.908 -20.867 -7.716  1.00 26.84 ?  387 HOH   B O    1 
HETATM 6721 O  O    . HOH   F 4 .   ? 35.330 -20.308 13.300  1.00 30.07 ?  388 HOH   B O    1 
HETATM 6722 O  O    . HOH   F 4 .   ? 46.765 -5.349  2.908   1.00 42.71 ?  389 HOH   B O    1 
HETATM 6723 O  O    . HOH   F 4 .   ? 25.719 -18.899 -11.994 1.00 37.11 ?  390 HOH   B O    1 
HETATM 6724 O  O    . HOH   F 4 .   ? 40.657 -6.626  -0.895  1.00 25.39 ?  391 HOH   B O    1 
HETATM 6725 O  O    . HOH   F 4 .   ? 44.014 -31.665 -3.894  1.00 32.76 ?  392 HOH   B O    1 
HETATM 6726 O  O    . HOH   F 4 .   ? 27.882 -27.078 2.247   1.00 31.43 ?  393 HOH   B O    1 
HETATM 6727 O  O    . HOH   F 4 .   ? 26.572 -27.949 -13.524 1.00 33.30 ?  394 HOH   B O    1 
HETATM 6728 O  O    . HOH   F 4 .   ? 24.566 -20.695 -10.441 1.00 33.97 ?  395 HOH   B O    1 
HETATM 6729 O  O    . HOH   F 4 .   ? 50.576 -30.765 8.651   1.00 27.37 ?  396 HOH   B O    1 
HETATM 6730 O  O    . HOH   F 4 .   ? 34.375 -33.461 9.533   1.00 31.73 ?  397 HOH   B O    1 
HETATM 6731 O  O    . HOH   F 4 .   ? 26.832 -30.627 -12.675 1.00 25.89 ?  398 HOH   B O    1 
HETATM 6732 O  O    . HOH   F 4 .   ? 45.754 -20.231 15.143  1.00 49.57 ?  399 HOH   B O    1 
HETATM 6733 O  O    . HOH   F 4 .   ? 57.546 -6.428  -2.355  1.00 33.79 ?  400 HOH   B O    1 
HETATM 6734 O  O    . HOH   F 4 .   ? 40.861 -11.786 -22.370 1.00 41.49 ?  401 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   . VAL   A 3   ? 0.6160 0.5957 0.6707 0.0104  -0.0278 0.1017  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.6120 0.5919 0.6608 0.0097  -0.0288 0.1009  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.5935 0.5769 0.6244 0.0042  -0.0320 0.1027  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.5968 0.5790 0.6350 0.0071  -0.0321 0.1051  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.6233 0.6006 0.6767 0.0131  -0.0239 0.0987  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.6272 0.6040 0.6836 0.0141  -0.0220 0.0980  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.6271 0.6031 0.6836 0.0143  -0.0212 0.0986  3   VAL   A CG2 
16   N  N   . ASN   A 4   ? 0.5682 0.5574 0.5651 -0.0045 -0.0326 0.1002  4   ASN   A N   
17   C  CA  . ASN   A 4   ? 0.5409 0.5341 0.4938 -0.0144 -0.0300 0.0961  4   ASN   A CA  
18   C  C   . ASN   A 4   ? 0.5003 0.5008 0.4543 -0.0259 -0.0152 0.0752  4   ASN   A C   
19   O  O   . ASN   A 4   ? 0.5041 0.5039 0.4484 -0.0263 -0.0177 0.0812  4   ASN   A O   
20   C  CB  . ASN   A 4   ? 0.5517 0.5423 0.4630 -0.0128 -0.0424 0.1098  4   ASN   A CB  
21   C  CG  . ASN   A 4   ? 0.5602 0.5467 0.4330 -0.0123 -0.0524 0.1230  4   ASN   A CG  
22   O  OD1 . ASN   A 4   ? 0.5636 0.5461 0.4191 -0.0121 -0.0530 0.1259  4   ASN   A OD1 
23   N  ND2 . ASN   A 4   ? 0.5628 0.5486 0.4179 -0.0113 -0.0577 0.1319  4   ASN   A ND2 
30   N  N   . SER   A 5   ? 0.4530 0.4609 0.4126 -0.0385 0.0012  0.0484  5   SER   A N   
31   C  CA  . SER   A 5   ? 0.4055 0.4243 0.3760 -0.0464 0.0173  0.0192  5   SER   A CA  
32   C  C   . SER   A 5   ? 0.3501 0.3762 0.3140 -0.0500 0.0335  -0.0048 5   SER   A C   
33   O  O   . SER   A 5   ? 0.3561 0.3903 0.3226 -0.0373 0.0374  -0.0180 5   SER   A O   
34   C  CB  . SER   A 5   ? 0.4139 0.4342 0.3927 -0.0488 0.0186  0.0148  5   SER   A CB  
35   O  OG  . SER   A 5   ? 0.4183 0.4391 0.4066 -0.0494 0.0248  0.0142  5   SER   A OG  
41   N  N   A PHE   A 6   ? 0.3036 0.3381 0.2726 -0.0657 0.0530  -0.0032 6   PHE   A N   
42   N  N   B PHE   A 6   ? 0.3280 0.3496 0.2909 -0.0487 0.0351  -0.0100 6   PHE   A N   
43   C  CA  A PHE   A 6   ? 0.2624 0.3021 0.2402 -0.0762 0.0661  0.0123  6   PHE   A CA  
44   C  CA  B PHE   A 6   ? 0.3066 0.3229 0.2683 -0.0461 0.0362  -0.0090 6   PHE   A CA  
45   C  C   A PHE   A 6   ? 0.2538 0.3001 0.2505 -0.0899 0.0793  0.0168  6   PHE   A C   
46   C  C   B PHE   A 6   ? 0.3022 0.3130 0.2702 -0.0464 0.0396  -0.0049 6   PHE   A C   
47   O  O   A PHE   A 6   ? 0.2625 0.3113 0.2814 -0.0923 0.0757  0.0237  6   PHE   A O   
48   O  O   B PHE   A 6   ? 0.3037 0.3138 0.2751 -0.0480 0.0338  -0.0014 6   PHE   A O   
49   C  CB  A PHE   A 6   ? 0.2370 0.2734 0.2079 -0.0640 0.0599  0.0202  6   PHE   A CB  
50   C  CB  B PHE   A 6   ? 0.2909 0.3069 0.2450 -0.0413 0.0336  -0.0129 6   PHE   A CB  
51   C  CG  A PHE   A 6   ? 0.2211 0.2554 0.1843 -0.0515 0.0515  0.0306  6   PHE   A CG  
52   C  CG  B PHE   A 6   ? 0.2764 0.2925 0.2275 -0.0384 0.0309  -0.0152 6   PHE   A CG  
53   C  CD1 A PHE   A 6   ? 0.2123 0.2460 0.1800 -0.0449 0.0434  0.0329  6   PHE   A CD1 
54   C  CD1 B PHE   A 6   ? 0.2692 0.2854 0.2205 -0.0365 0.0306  -0.0164 6   PHE   A CD1 
55   C  CD2 A PHE   A 6   ? 0.2254 0.2554 0.1925 -0.0351 0.0459  0.0306  6   PHE   A CD2 
56   C  CD2 B PHE   A 6   ? 0.2724 0.2868 0.2234 -0.0358 0.0307  -0.0154 6   PHE   A CD2 
57   C  CE1 A PHE   A 6   ? 0.2116 0.2413 0.1886 -0.0401 0.0386  0.0319  6   PHE   A CE1 
58   C  CE1 B PHE   A 6   ? 0.2653 0.2809 0.2195 -0.0366 0.0312  -0.0150 6   PHE   A CE1 
59   C  CE2 A PHE   A 6   ? 0.2235 0.2522 0.2027 -0.0301 0.0384  0.0245  6   PHE   A CE2 
60   C  CE2 B PHE   A 6   ? 0.2675 0.2813 0.2172 -0.0362 0.0312  -0.0160 6   PHE   A CE2 
61   C  CZ  A PHE   A 6   ? 0.2172 0.2444 0.1881 -0.0379 0.0345  0.0222  6   PHE   A CZ  
62   C  CZ  B PHE   A 6   ? 0.2646 0.2795 0.2147 -0.0365 0.0309  -0.0155 6   PHE   A CZ  
81   N  N   A SER   A 7   ? 0.2379 0.2869 0.2473 -0.0917 0.0823  0.0033  7   SER   A N   
82   N  N   B SER   A 7   ? 0.2953 0.3014 0.2714 -0.0437 0.0455  -0.0076 7   SER   A N   
83   C  CA  A SER   A 7   ? 0.2376 0.2856 0.2676 -0.0799 0.0816  -0.0157 7   SER   A CA  
84   C  CA  B SER   A 7   ? 0.2897 0.2913 0.2709 -0.0402 0.0451  -0.0122 7   SER   A CA  
85   C  C   A SER   A 7   ? 0.2215 0.2590 0.2741 -0.0759 0.0855  -0.0166 7   SER   A C   
86   C  C   B SER   A 7   ? 0.2756 0.2776 0.2583 -0.0372 0.0529  -0.0119 7   SER   A C   
87   O  O   A SER   A 7   ? 0.2361 0.2504 0.2949 -0.0785 0.0880  -0.0138 7   SER   A O   
88   O  O   B SER   A 7   ? 0.2774 0.2754 0.2592 -0.0396 0.0578  -0.0125 7   SER   A O   
89   C  CB  A SER   A 7   ? 0.2572 0.3110 0.2926 -0.0668 0.0809  -0.0164 7   SER   A CB  
90   C  CB  B SER   A 7   ? 0.2957 0.2942 0.2807 -0.0413 0.0380  -0.0167 7   SER   A CB  
91   O  OG  A SER   A 7   ? 0.2718 0.3277 0.3179 -0.0561 0.0767  -0.0131 7   SER   A OG  
92   O  OG  B SER   A 7   ? 0.3007 0.2975 0.2901 -0.0416 0.0312  -0.0159 7   SER   A OG  
103  N  N   A GLY   A 8   ? 0.1981 0.2439 0.2606 -0.0734 0.0707  -0.0182 8   GLY   A N   
104  N  N   B GLY   A 8   ? 0.2602 0.2686 0.2421 -0.0330 0.0564  -0.0076 8   GLY   A N   
105  C  CA  A GLY   A 8   ? 0.1887 0.2300 0.2562 -0.0501 0.0619  -0.0082 8   GLY   A CA  
106  C  CA  B GLY   A 8   ? 0.2433 0.2572 0.2240 -0.0284 0.0568  -0.0020 8   GLY   A CA  
107  C  C   A GLY   A 8   ? 0.1748 0.2202 0.2460 -0.0315 0.0420  -0.0072 8   GLY   A C   
108  C  C   B GLY   A 8   ? 0.2248 0.2469 0.2105 -0.0253 0.0558  0.0041  8   GLY   A C   
109  O  O   A GLY   A 8   ? 0.1772 0.2194 0.2471 -0.0146 0.0274  -0.0257 8   GLY   A O   
110  O  O   B GLY   A 8   ? 0.2231 0.2457 0.2141 -0.0224 0.0597  0.0052  8   GLY   A O   
117  N  N   A TYR   A 9   ? 0.1513 0.2037 0.2262 -0.0297 0.0317  0.0038  9   TYR   A N   
118  N  N   B TYR   A 9   ? 0.2057 0.2361 0.2063 -0.0259 0.0499  0.0095  9   TYR   A N   
119  C  CA  A TYR   A 9   ? 0.1436 0.1875 0.2179 -0.0313 0.0261  0.0067  9   TYR   A CA  
120  C  CA  B TYR   A 9   ? 0.1866 0.2215 0.2063 -0.0244 0.0393  0.0139  9   TYR   A CA  
121  C  C   A TYR   A 9   ? 0.1446 0.1752 0.2160 -0.0262 0.0301  0.0297  9   TYR   A C   
122  C  C   B TYR   A 9   ? 0.1768 0.2106 0.2049 -0.0223 0.0314  0.0268  9   TYR   A C   
123  O  O   A TYR   A 9   ? 0.1602 0.1958 0.2358 -0.0253 0.0245  0.0381  9   TYR   A O   
124  O  O   B TYR   A 9   ? 0.1786 0.2176 0.2182 -0.0192 0.0165  0.0359  9   TYR   A O   
125  C  CB  A TYR   A 9   ? 0.1399 0.1925 0.2266 -0.0241 0.0293  -0.0098 9   TYR   A CB  
126  C  CB  B TYR   A 9   ? 0.1771 0.2188 0.2091 -0.0228 0.0356  0.0075  9   TYR   A CB  
127  C  CG  A TYR   A 9   ? 0.1454 0.1915 0.2345 -0.0183 0.0444  -0.0195 9   TYR   A CG  
128  C  CG  B TYR   A 9   ? 0.1682 0.2172 0.2031 -0.0208 0.0372  0.0062  9   TYR   A CG  
129  C  CD1 A TYR   A 9   ? 0.1532 0.1996 0.2473 -0.0243 0.0526  -0.0253 9   TYR   A CD1 
130  C  CD1 B TYR   A 9   ? 0.1665 0.2179 0.2060 -0.0234 0.0394  0.0064  9   TYR   A CD1 
131  C  CD2 A TYR   A 9   ? 0.1488 0.1827 0.2362 -0.0134 0.0421  -0.0079 9   TYR   A CD2 
132  C  CD2 B TYR   A 9   ? 0.1664 0.2153 0.1937 -0.0168 0.0327  0.0083  9   TYR   A CD2 
133  C  CE1 A TYR   A 9   ? 0.1582 0.1947 0.2537 -0.0237 0.0531  -0.0301 9   TYR   A CE1 
134  C  CE1 B TYR   A 9   ? 0.1654 0.2148 0.2081 -0.0221 0.0390  0.0033  9   TYR   A CE1 
135  C  CE2 A TYR   A 9   ? 0.1463 0.1828 0.2413 -0.0088 0.0500  -0.0229 9   TYR   A CE2 
136  C  CE2 B TYR   A 9   ? 0.1621 0.2150 0.1961 -0.0144 0.0372  0.0089  9   TYR   A CE2 
137  C  CZ  A TYR   A 9   ? 0.1521 0.1862 0.2556 -0.0253 0.0576  -0.0198 9   TYR   A CZ  
138  C  CZ  B TYR   A 9   ? 0.1589 0.2116 0.2053 -0.0152 0.0472  0.0076  9   TYR   A CZ  
139  O  OH  A TYR   A 9   ? 0.1624 0.1918 0.2765 -0.0325 0.0606  -0.0171 9   TYR   A OH  
140  O  OH  B TYR   A 9   ? 0.1528 0.2091 0.2201 -0.0136 0.0580  0.0104  9   TYR   A OH  
159  N  N   A LEU   A 10  ? 0.1454 0.1602 0.2129 -0.0260 0.0194  0.0270  10  LEU   A N   
160  N  N   B LEU   A 10  ? 0.1684 0.1941 0.1902 -0.0224 0.0307  0.0331  10  LEU   A N   
161  C  CA  A LEU   A 10  ? 0.1490 0.1632 0.2085 -0.0249 0.0139  0.0367  10  LEU   A CA  
162  C  CA  B LEU   A 10  ? 0.1622 0.1853 0.1846 -0.0262 0.0278  0.0320  10  LEU   A CA  
163  C  C   A LEU   A 10  ? 0.1493 0.1536 0.2050 -0.0176 0.0209  0.0382  10  LEU   A C   
164  C  C   B LEU   A 10  ? 0.1600 0.1718 0.1826 -0.0264 0.0185  0.0267  10  LEU   A C   
165  O  O   A LEU   A 10  ? 0.1544 0.1449 0.2269 -0.0222 0.0470  0.0429  10  LEU   A O   
166  O  O   B LEU   A 10  ? 0.1619 0.1676 0.1927 -0.0307 0.0242  0.0276  10  LEU   A O   
167  C  CB  A LEU   A 10  ? 0.1617 0.1786 0.2363 -0.0262 0.0046  0.0470  10  LEU   A CB  
168  C  CB  B LEU   A 10  ? 0.1571 0.1839 0.1841 -0.0308 0.0151  0.0456  10  LEU   A CB  
169  C  CG  A LEU   A 10  ? 0.1927 0.1984 0.2803 -0.0217 -0.0202 0.0477  10  LEU   A CG  
170  C  CG  B LEU   A 10  ? 0.1559 0.1871 0.1867 -0.0338 -0.0055 0.0606  10  LEU   A CG  
171  C  CD1 A LEU   A 10  ? 0.2059 0.2036 0.3095 -0.0257 -0.0184 0.0496  10  LEU   A CD1 
172  C  CD1 B LEU   A 10  ? 0.1541 0.2001 0.1899 -0.0371 -0.0061 0.0606  10  LEU   A CD1 
173  C  CD2 A LEU   A 10  ? 0.2113 0.2141 0.2955 -0.0204 -0.0215 0.0349  10  LEU   A CD2 
174  C  CD2 B LEU   A 10  ? 0.1589 0.1819 0.1772 -0.0326 -0.0224 0.0723  10  LEU   A CD2 
197  N  N   A LYS   A 11  ? 0.1509 0.1510 0.1912 -0.0231 0.0192  0.0340  11  LYS   A N   
198  N  N   B LYS   A 11  ? 0.1599 0.1610 0.1710 -0.0294 0.0109  0.0261  11  LYS   A N   
199  C  CA  A LYS   A 11  ? 0.1517 0.1499 0.2015 -0.0300 0.0182  0.0355  11  LYS   A CA  
200  C  CA  B LYS   A 11  ? 0.1592 0.1499 0.1720 -0.0285 0.0113  0.0261  11  LYS   A CA  
201  C  C   A LYS   A 11  ? 0.1457 0.1487 0.2020 -0.0275 0.0263  0.0262  11  LYS   A C   
202  C  C   B LYS   A 11  ? 0.1471 0.1373 0.1692 -0.0270 0.0220  0.0145  11  LYS   A C   
203  O  O   A LYS   A 11  ? 0.1535 0.1706 0.2337 -0.0473 0.0320  0.0064  11  LYS   A O   
204  O  O   B LYS   A 11  ? 0.1384 0.1256 0.1688 -0.0244 0.0335  -0.0020 11  LYS   A O   
205  C  CB  A LYS   A 11  ? 0.1611 0.1479 0.1890 -0.0289 0.0123  0.0261  11  LYS   A CB  
206  C  CB  B LYS   A 11  ? 0.1697 0.1476 0.1663 -0.0267 0.0025  0.0235  11  LYS   A CB  
207  C  CG  A LYS   A 11  ? 0.1770 0.1478 0.1883 -0.0265 0.0187  0.0252  11  LYS   A CG  
208  C  CG  B LYS   A 11  ? 0.1783 0.1489 0.1640 -0.0218 0.0024  0.0207  11  LYS   A CG  
209  C  CD  A LYS   A 11  ? 0.1901 0.1504 0.1832 -0.0272 0.0202  0.0278  11  LYS   A CD  
210  C  CD  B LYS   A 11  ? 0.1848 0.1528 0.1655 -0.0185 0.0012  0.0191  11  LYS   A CD  
211  C  CE  A LYS   A 11  ? 0.1956 0.1432 0.1838 -0.0237 0.0213  0.0330  11  LYS   A CE  
212  C  CE  B LYS   A 11  ? 0.1887 0.1536 0.1664 -0.0138 0.0027  0.0186  11  LYS   A CE  
213  N  NZ  A LYS   A 11  ? 0.1954 0.1417 0.1900 -0.0112 0.0091  0.0363  11  LYS   A NZ  
214  N  NZ  B LYS   A 11  ? 0.1895 0.1550 0.1693 -0.0065 -0.0004 0.0203  11  LYS   A NZ  
241  N  N   A LEU   A 12  ? 0.1355 0.1359 0.1844 -0.0230 0.0181  0.0300  12  LEU   A N   
242  N  N   B LEU   A 12  ? 0.1414 0.1474 0.1691 -0.0210 0.0171  0.0113  12  LEU   A N   
243  C  CA  A LEU   A 12  ? 0.1347 0.1415 0.1902 -0.0210 0.0107  0.0368  12  LEU   A CA  
244  C  CA  B LEU   A 12  ? 0.1368 0.1575 0.1757 -0.0137 0.0179  0.0107  12  LEU   A CA  
245  C  C   A LEU   A 12  ? 0.1352 0.1378 0.1944 -0.0235 0.0146  0.0381  12  LEU   A C   
246  C  C   B LEU   A 12  ? 0.1342 0.1555 0.1813 -0.0095 0.0187  0.0098  12  LEU   A C   
247  O  O   A LEU   A 12  ? 0.1373 0.1413 0.2109 -0.0216 0.0206  0.0267  12  LEU   A O   
248  O  O   B LEU   A 12  ? 0.1376 0.1493 0.1824 -0.0029 0.0098  0.0047  12  LEU   A O   
249  C  CB  A LEU   A 12  ? 0.1466 0.1409 0.2067 -0.0184 -0.0040 0.0432  12  LEU   A CB  
250  C  CB  B LEU   A 12  ? 0.1378 0.1628 0.1805 -0.0081 0.0245  0.0074  12  LEU   A CB  
251  C  CG  A LEU   A 12  ? 0.1544 0.1519 0.2403 -0.0086 -0.0002 0.0504  12  LEU   A CG  
252  C  CG  B LEU   A 12  ? 0.1366 0.1663 0.1929 -0.0036 0.0338  0.0116  12  LEU   A CG  
253  C  CD1 A LEU   A 12  ? 0.1784 0.1576 0.2489 0.0031  0.0081  0.0650  12  LEU   A CD1 
254  C  CD1 B LEU   A 12  ? 0.1396 0.1678 0.1920 0.0055  0.0383  0.0120  12  LEU   A CD1 
255  C  CD2 A LEU   A 12  ? 0.1559 0.1669 0.2532 -0.0072 -0.0120 0.0454  12  LEU   A CD2 
256  C  CD2 B LEU   A 12  ? 0.1363 0.1729 0.1988 -0.0096 0.0354  0.0187  12  LEU   A CD2 
279  N  N   A THR   A 13  ? 0.1304 0.1378 0.2001 -0.0185 0.0067  0.0334  13  THR   A N   
280  N  N   B THR   A 13  ? 0.1318 0.1547 0.1862 -0.0093 0.0180  0.0095  13  THR   A N   
281  C  CA  A THR   A 13  ? 0.1299 0.1387 0.2027 -0.0195 0.0098  0.0282  13  THR   A CA  
282  C  CA  B THR   A 13  ? 0.1352 0.1588 0.1845 -0.0108 0.0206  0.0168  13  THR   A CA  
283  C  C   A THR   A 13  ? 0.1321 0.1332 0.2018 -0.0270 0.0121  0.0405  13  THR   A C   
284  C  C   B THR   A 13  ? 0.1451 0.1622 0.1834 -0.0154 0.0152  0.0143  13  THR   A C   
285  O  O   A THR   A 13  ? 0.1390 0.1326 0.2125 -0.0140 0.0178  0.0348  13  THR   A O   
286  O  O   B THR   A 13  ? 0.1538 0.1666 0.1916 -0.0186 0.0136  0.0189  13  THR   A O   
287  C  CB  A THR   A 13  ? 0.1316 0.1484 0.2041 -0.0174 0.0029  0.0403  13  THR   A CB  
288  C  CB  B THR   A 13  ? 0.1292 0.1668 0.1872 -0.0035 0.0229  0.0226  13  THR   A CB  
289  O  OG1 A THR   A 13  ? 0.1328 0.1456 0.2080 -0.0169 -0.0074 0.0491  13  THR   A OG1 
290  O  OG1 B THR   A 13  ? 0.1251 0.1734 0.2087 -0.0051 0.0296  0.0294  13  THR   A OG1 
291  C  CG2 A THR   A 13  ? 0.1406 0.1695 0.2233 -0.0126 0.0011  0.0334  13  THR   A CG2 
292  C  CG2 B THR   A 13  ? 0.1310 0.1741 0.1908 0.0040  0.0191  0.0233  13  THR   A CG2 
307  N  N   A ASP   A 14  ? 0.1398 0.1400 0.2153 -0.0321 0.0088  0.0563  14  ASP   A N   
308  N  N   B ASP   A 14  ? 0.1493 0.1604 0.1861 -0.0120 0.0029  0.0123  14  ASP   A N   
309  C  CA  A ASP   A 14  ? 0.1424 0.1597 0.2281 -0.0270 -0.0015 0.0687  14  ASP   A CA  
310  C  CA  B ASP   A 14  ? 0.1567 0.1612 0.1867 -0.0074 -0.0024 0.0136  14  ASP   A CA  
311  C  C   A ASP   A 14  ? 0.1483 0.1665 0.2092 -0.0288 -0.0064 0.0584  14  ASP   A C   
312  C  C   B ASP   A 14  ? 0.1493 0.1574 0.1732 -0.0081 0.0008  0.0174  14  ASP   A C   
313  O  O   A ASP   A 14  ? 0.1701 0.1789 0.2228 -0.0460 -0.0077 0.0592  14  ASP   A O   
314  O  O   B ASP   A 14  ? 0.1570 0.1611 0.1803 -0.0073 0.0029  0.0128  14  ASP   A O   
315  C  CB  A ASP   A 14  ? 0.1553 0.1882 0.2751 -0.0317 -0.0013 0.0859  14  ASP   A CB  
316  C  CB  B ASP   A 14  ? 0.1735 0.1680 0.2102 -0.0003 -0.0080 0.0230  14  ASP   A CB  
317  C  CG  A ASP   A 14  ? 0.1847 0.2327 0.3350 -0.0349 0.0035  0.0938  14  ASP   A CG  
318  C  CG  B ASP   A 14  ? 0.1889 0.1845 0.2306 0.0064  -0.0141 0.0355  14  ASP   A CG  
319  O  OD1 A ASP   A 14  ? 0.2013 0.2463 0.3610 -0.0339 0.0028  0.0946  14  ASP   A OD1 
320  O  OD1 B ASP   A 14  ? 0.1982 0.1894 0.2321 0.0157  -0.0255 0.0429  14  ASP   A OD1 
321  O  OD2 A ASP   A 14  ? 0.2044 0.2730 0.3617 -0.0209 -0.0029 0.0854  14  ASP   A OD2 
322  O  OD2 B ASP   A 14  ? 0.1943 0.1955 0.2337 0.0086  -0.0175 0.0461  14  ASP   A OD2 
331  N  N   A ASN   A 15  ? 0.1373 0.1497 0.2056 -0.0257 0.0120  0.0570  15  ASN   A N   
332  N  N   B ASN   A 15  ? 0.1350 0.1472 0.1670 -0.0127 0.0033  0.0296  15  ASN   A N   
333  C  CA  A ASN   A 15  ? 0.1376 0.1527 0.2134 -0.0253 0.0017  0.0383  15  ASN   A CA  
334  C  CA  B ASN   A 15  ? 0.1281 0.1472 0.1715 -0.0154 0.0011  0.0201  15  ASN   A CA  
335  C  C   A ASN   A 15  ? 0.1382 0.1505 0.2217 -0.0252 0.0049  0.0365  15  ASN   A C   
336  C  C   B ASN   A 15  ? 0.1289 0.1474 0.1816 -0.0113 0.0147  0.0204  15  ASN   A C   
337  O  O   A ASN   A 15  ? 0.1340 0.1537 0.2162 -0.0292 0.0003  0.0369  15  ASN   A O   
338  O  O   B ASN   A 15  ? 0.1267 0.1523 0.1843 -0.0067 0.0263  0.0129  15  ASN   A O   
339  C  CB  A ASN   A 15  ? 0.1341 0.1548 0.2239 -0.0179 0.0031  0.0399  15  ASN   A CB  
340  C  CB  B ASN   A 15  ? 0.1270 0.1465 0.1750 -0.0191 -0.0016 0.0226  15  ASN   A CB  
341  C  CG  A ASN   A 15  ? 0.1327 0.1588 0.2374 -0.0140 0.0014  0.0340  15  ASN   A CG  
342  C  CG  B ASN   A 15  ? 0.1315 0.1492 0.1835 -0.0190 0.0012  0.0200  15  ASN   A CG  
343  O  OD1 A ASN   A 15  ? 0.1380 0.1602 0.2425 -0.0194 0.0067  0.0279  15  ASN   A OD1 
344  O  OD1 B ASN   A 15  ? 0.1378 0.1486 0.1936 -0.0215 0.0036  0.0190  15  ASN   A OD1 
345  N  ND2 A ASN   A 15  ? 0.1346 0.1637 0.2298 -0.0144 0.0070  0.0335  15  ASN   A ND2 
346  N  ND2 B ASN   A 15  ? 0.1316 0.1531 0.1769 -0.0194 0.0077  0.0193  15  ASN   A ND2 
359  N  N   A VAL   A 16  ? 0.1407 0.1371 0.2060 -0.0157 0.0185  0.0336  16  VAL   A N   
360  N  N   B VAL   A 16  ? 0.1291 0.1406 0.1745 -0.0091 0.0170  0.0331  16  VAL   A N   
361  C  CA  A VAL   A 16  ? 0.1403 0.1352 0.2148 -0.0111 0.0147  0.0329  16  VAL   A CA  
362  C  CA  B VAL   A 16  ? 0.1279 0.1377 0.1634 -0.0052 0.0262  0.0420  16  VAL   A CA  
363  C  C   A VAL   A 16  ? 0.1339 0.1322 0.2125 -0.0176 0.0106  0.0243  16  VAL   A C   
364  C  C   B VAL   A 16  ? 0.1233 0.1440 0.1681 -0.0037 0.0271  0.0406  16  VAL   A C   
365  O  O   A VAL   A 16  ? 0.1270 0.1321 0.2203 -0.0234 0.0153  0.0108  16  VAL   A O   
366  O  O   B VAL   A 16  ? 0.1190 0.1427 0.1797 0.0019  0.0375  0.0412  16  VAL   A O   
367  C  CB  A VAL   A 16  ? 0.1456 0.1518 0.2153 0.0033  0.0218  0.0377  16  VAL   A CB  
368  C  CB  B VAL   A 16  ? 0.1380 0.1361 0.1492 -0.0021 0.0333  0.0461  16  VAL   A CB  
369  C  CG1 A VAL   A 16  ? 0.1591 0.1600 0.2171 0.0073  0.0226  0.0353  16  VAL   A CG1 
370  C  CG1 B VAL   A 16  ? 0.1469 0.1329 0.1451 -0.0018 0.0323  0.0449  16  VAL   A CG1 
371  C  CG2 A VAL   A 16  ? 0.1557 0.1696 0.2308 0.0046  0.0300  0.0261  16  VAL   A CG2 
372  C  CG2 B VAL   A 16  ? 0.1432 0.1484 0.1679 0.0015  0.0401  0.0459  16  VAL   A CG2 
391  N  N   A TYR   A 17  ? 0.1338 0.1296 0.2129 -0.0200 0.0222  0.0256  17  TYR   A N   
392  N  N   B TYR   A 17  ? 0.1267 0.1440 0.1740 -0.0096 0.0206  0.0347  17  TYR   A N   
393  C  CA  A TYR   A 17  ? 0.1355 0.1355 0.2029 -0.0147 0.0273  0.0268  17  TYR   A CA  
394  C  CA  B TYR   A 17  ? 0.1316 0.1428 0.1742 -0.0095 0.0128  0.0268  17  TYR   A CA  
395  C  C   A TYR   A 17  ? 0.1395 0.1295 0.2100 -0.0122 0.0277  0.0216  17  TYR   A C   
396  C  C   B TYR   A 17  ? 0.1375 0.1473 0.1809 -0.0091 0.0115  0.0223  17  TYR   A C   
397  O  O   A TYR   A 17  ? 0.1324 0.1125 0.2033 -0.0117 0.0312  0.0246  17  TYR   A O   
398  O  O   B TYR   A 17  ? 0.1351 0.1499 0.1718 -0.0211 0.0115  0.0089  17  TYR   A O   
399  C  CB  A TYR   A 17  ? 0.1374 0.1413 0.2032 -0.0112 0.0206  0.0234  17  TYR   A CB  
400  C  CB  B TYR   A 17  ? 0.1384 0.1368 0.1751 -0.0158 0.0062  0.0197  17  TYR   A CB  
401  C  CG  A TYR   A 17  ? 0.1499 0.1517 0.2060 -0.0116 0.0147  0.0181  17  TYR   A CG  
402  C  CG  B TYR   A 17  ? 0.1416 0.1328 0.1679 -0.0167 -0.0010 0.0094  17  TYR   A CG  
403  C  CD1 A TYR   A 17  ? 0.1654 0.1616 0.2083 -0.0009 0.0126  0.0131  17  TYR   A CD1 
404  C  CD1 B TYR   A 17  ? 0.1409 0.1352 0.1652 -0.0184 0.0016  0.0133  17  TYR   A CD1 
405  C  CD2 A TYR   A 17  ? 0.1577 0.1533 0.2046 -0.0134 0.0171  0.0215  17  TYR   A CD2 
406  C  CD2 B TYR   A 17  ? 0.1417 0.1330 0.1666 -0.0221 -0.0043 0.0038  17  TYR   A CD2 
407  C  CE1 A TYR   A 17  ? 0.1717 0.1615 0.2188 -0.0023 0.0116  0.0146  17  TYR   A CE1 
408  C  CE1 B TYR   A 17  ? 0.1327 0.1324 0.1677 -0.0221 -0.0066 0.0189  17  TYR   A CE1 
409  C  CE2 A TYR   A 17  ? 0.1679 0.1513 0.2174 -0.0083 0.0124  0.0157  17  TYR   A CE2 
410  C  CE2 B TYR   A 17  ? 0.1364 0.1304 0.1660 -0.0245 -0.0110 0.0105  17  TYR   A CE2 
411  C  CZ  A TYR   A 17  ? 0.1688 0.1566 0.2215 -0.0059 0.0093  0.0250  17  TYR   A CZ  
412  C  CZ  B TYR   A 17  ? 0.1343 0.1300 0.1675 -0.0242 -0.0114 0.0153  17  TYR   A CZ  
413  O  OH  A TYR   A 17  ? 0.1733 0.1609 0.2322 -0.0052 0.0185  0.0345  17  TYR   A OH  
414  O  OH  B TYR   A 17  ? 0.1400 0.1266 0.1715 -0.0190 -0.0157 0.0135  17  TYR   A OH  
433  N  N   A ILE   A 18  ? 0.1344 0.1414 0.2183 -0.0213 0.0246  0.0434  18  ILE   A N   
434  N  N   B ILE   A 18  ? 0.1416 0.1496 0.1872 0.0024  0.0094  0.0376  18  ILE   A N   
435  C  CA  A ILE   A 18  ? 0.1317 0.1487 0.2319 -0.0195 0.0188  0.0461  18  ILE   A CA  
436  C  CA  B ILE   A 18  ? 0.1519 0.1530 0.1914 0.0075  0.0163  0.0384  18  ILE   A CA  
437  C  C   A ILE   A 18  ? 0.1258 0.1585 0.2598 -0.0193 0.0234  0.0421  18  ILE   A C   
438  C  C   B ILE   A 18  ? 0.1680 0.1642 0.2105 0.0061  0.0234  0.0301  18  ILE   A C   
439  O  O   A ILE   A 18  ? 0.1265 0.1763 0.2581 -0.0280 0.0381  0.0474  18  ILE   A O   
440  O  O   B ILE   A 18  ? 0.1647 0.1693 0.2079 0.0024  0.0217  0.0332  18  ILE   A O   
441  C  CB  A ILE   A 18  ? 0.1470 0.1530 0.2237 -0.0115 0.0052  0.0677  18  ILE   A CB  
442  C  CB  B ILE   A 18  ? 0.1551 0.1542 0.1875 0.0094  0.0109  0.0464  18  ILE   A CB  
443  C  CG1 A ILE   A 18  ? 0.1651 0.1676 0.2317 -0.0120 -0.0017 0.0807  18  ILE   A CG1 
444  C  CG1 B ILE   A 18  ? 0.1636 0.1594 0.1868 0.0105  0.0042  0.0396  18  ILE   A CG1 
445  C  CG2 A ILE   A 18  ? 0.1422 0.1485 0.2291 -0.0116 0.0025  0.0615  18  ILE   A CG2 
446  C  CG2 B ILE   A 18  ? 0.1538 0.1553 0.1895 0.0029  0.0065  0.0545  18  ILE   A CG2 
447  C  CD1 A ILE   A 18  ? 0.1892 0.1893 0.2468 -0.0141 -0.0049 0.0777  18  ILE   A CD1 
448  C  CD1 B ILE   A 18  ? 0.1714 0.1660 0.1969 0.0149  0.0070  0.0334  18  ILE   A CD1 
471  N  N   A LYS   A 19  ? 0.1279 0.1532 0.2754 -0.0155 0.0440  0.0422  19  LYS   A N   
472  N  N   B LYS   A 19  ? 0.1841 0.1714 0.2316 0.0067  0.0337  0.0208  19  LYS   A N   
473  C  CA  A LYS   A 19  ? 0.1339 0.1618 0.3009 -0.0062 0.0551  0.0457  19  LYS   A CA  
474  C  CA  B LYS   A 19  ? 0.1975 0.1835 0.2485 0.0081  0.0382  0.0172  19  LYS   A CA  
475  C  C   A LYS   A 19  ? 0.1225 0.1535 0.3342 0.0019  0.0449  0.0408  19  LYS   A C   
476  C  C   B LYS   A 19  ? 0.2010 0.1829 0.2644 0.0068  0.0362  0.0201  19  LYS   A C   
477  O  O   A LYS   A 19  ? 0.1169 0.1505 0.3306 -0.0028 0.0285  0.0457  19  LYS   A O   
478  O  O   B LYS   A 19  ? 0.2033 0.1802 0.2662 0.0105  0.0285  0.0205  19  LYS   A O   
479  C  CB  A LYS   A 19  ? 0.1460 0.1806 0.3053 -0.0106 0.0682  0.0364  19  LYS   A CB  
480  C  CB  B LYS   A 19  ? 0.2061 0.1959 0.2491 0.0084  0.0424  0.0081  19  LYS   A CB  
481  C  CG  A LYS   A 19  ? 0.1805 0.2052 0.3129 -0.0060 0.0705  0.0205  19  LYS   A CG  
482  C  CG  B LYS   A 19  ? 0.2178 0.2086 0.2566 0.0092  0.0380  -0.0018 19  LYS   A CG  
483  C  CD  A LYS   A 19  ? 0.2091 0.2217 0.3109 -0.0099 0.0817  0.0220  19  LYS   A CD  
484  C  CD  B LYS   A 19  ? 0.2285 0.2198 0.2604 0.0100  0.0339  -0.0066 19  LYS   A CD  
485  C  CE  A LYS   A 19  ? 0.2297 0.2298 0.3131 -0.0066 0.0794  0.0124  19  LYS   A CE  
486  C  CE  B LYS   A 19  ? 0.2347 0.2261 0.2593 0.0076  0.0317  -0.0083 19  LYS   A CE  
487  N  NZ  A LYS   A 19  ? 0.2387 0.2323 0.3092 -0.0122 0.0911  0.0030  19  LYS   A NZ  
488  N  NZ  B LYS   A 19  ? 0.2346 0.2294 0.2577 0.0066  0.0318  -0.0124 19  LYS   A NZ  
515  N  N   A ASN   A 20  ? 0.1305 0.1564 0.3664 0.0011  0.0476  0.0479  20  ASN   A N   
516  N  N   B ASN   A 20  ? 0.2049 0.1863 0.2757 -0.0019 0.0412  0.0273  20  ASN   A N   
517  C  CA  A ASN   A 20  ? 0.1430 0.1765 0.3849 0.0174  0.0529  0.0371  20  ASN   A CA  
518  C  CA  B ASN   A 20  ? 0.2090 0.1920 0.2795 -0.0054 0.0473  0.0276  20  ASN   A CA  
519  C  C   A ASN   A 20  ? 0.1686 0.1806 0.3793 0.0107  0.0611  0.0239  20  ASN   A C   
520  C  C   B ASN   A 20  ? 0.2126 0.1938 0.2750 -0.0063 0.0511  0.0182  20  ASN   A C   
521  O  O   A ASN   A 20  ? 0.1924 0.1979 0.3877 -0.0095 0.0625  0.0153  20  ASN   A O   
522  O  O   B ASN   A 20  ? 0.2201 0.2001 0.2799 -0.0139 0.0542  0.0144  20  ASN   A O   
523  C  CB  A ASN   A 20  ? 0.1530 0.1955 0.4140 0.0309  0.0557  0.0400  20  ASN   A CB  
524  C  CB  B ASN   A 20  ? 0.2138 0.1955 0.2891 -0.0104 0.0519  0.0397  20  ASN   A CB  
525  C  CG  A ASN   A 20  ? 0.1687 0.2103 0.4497 0.0463  0.0562  0.0452  20  ASN   A CG  
526  C  CG  B ASN   A 20  ? 0.2202 0.1996 0.3081 -0.0131 0.0556  0.0479  20  ASN   A CG  
527  O  OD1 A ASN   A 20  ? 0.1917 0.2228 0.4919 0.0485  0.0744  0.0342  20  ASN   A OD1 
528  O  OD1 B ASN   A 20  ? 0.2308 0.2090 0.3291 -0.0112 0.0564  0.0416  20  ASN   A OD1 
529  N  ND2 A ASN   A 20  ? 0.1775 0.2090 0.4528 0.0501  0.0414  0.0504  20  ASN   A ND2 
530  N  ND2 B ASN   A 20  ? 0.2226 0.1969 0.3091 -0.0168 0.0534  0.0549  20  ASN   A ND2 
543  N  N   A ALA   A 21  ? 0.1691 0.1727 0.3716 0.0083  0.0483  0.0176  21  ALA   A N   
544  N  N   B ALA   A 21  ? 0.2077 0.1888 0.2656 -0.0034 0.0452  0.0133  21  ALA   A N   
545  C  CA  A ALA   A 21  ? 0.1762 0.1693 0.3571 0.0076  0.0495  0.0237  21  ALA   A CA  
546  C  CA  B ALA   A 21  ? 0.2054 0.1842 0.2523 -0.0009 0.0462  0.0139  21  ALA   A CA  
547  C  C   A ALA   A 21  ? 0.1708 0.1703 0.3417 0.0020  0.0404  0.0213  21  ALA   A C   
548  C  C   B ALA   A 21  ? 0.1957 0.1787 0.2326 0.0059  0.0512  0.0128  21  ALA   A C   
549  O  O   A ALA   A 21  ? 0.1630 0.1774 0.3459 0.0004  0.0341  0.0199  21  ALA   A O   
550  O  O   B ALA   A 21  ? 0.1953 0.1759 0.2323 0.0118  0.0501  0.0101  21  ALA   A O   
551  C  CB  A ALA   A 21  ? 0.1974 0.1819 0.3667 0.0005  0.0446  0.0290  21  ALA   A CB  
552  C  CB  B ALA   A 21  ? 0.2158 0.1903 0.2653 -0.0071 0.0359  0.0143  21  ALA   A CB  
563  N  N   A ASP   A 22  ? 0.1755 0.1694 0.3301 -0.0102 0.0384  0.0212  22  ASP   A N   
564  N  N   B ASP   A 22  ? 0.1874 0.1758 0.2174 0.0050  0.0600  0.0123  22  ASP   A N   
565  C  CA  A ASP   A 22  ? 0.1788 0.1727 0.3087 -0.0086 0.0267  0.0247  22  ASP   A CA  
566  C  CA  B ASP   A 22  ? 0.1842 0.1765 0.2105 0.0043  0.0568  0.0101  22  ASP   A CA  
567  C  C   A ASP   A 22  ? 0.1682 0.1775 0.2664 -0.0111 0.0308  0.0294  22  ASP   A C   
568  C  C   B ASP   A 22  ? 0.1693 0.1712 0.1793 -0.0058 0.0518  0.0135  22  ASP   A C   
569  O  O   A ASP   A 22  ? 0.1711 0.1841 0.2674 -0.0075 0.0452  0.0373  22  ASP   A O   
570  O  O   B ASP   A 22  ? 0.1673 0.1681 0.1758 -0.0078 0.0554  0.0110  22  ASP   A O   
571  C  CB  A ASP   A 22  ? 0.1977 0.1750 0.3333 -0.0052 0.0265  0.0125  22  ASP   A CB  
572  C  CB  B ASP   A 22  ? 0.1915 0.1813 0.2258 0.0137  0.0642  0.0066  22  ASP   A CB  
573  C  CG  A ASP   A 22  ? 0.2124 0.1768 0.3548 -0.0063 0.0168  0.0078  22  ASP   A CG  
574  C  CG  B ASP   A 22  ? 0.1983 0.1824 0.2298 0.0208  0.0736  0.0174  22  ASP   A CG  
575  O  OD1 A ASP   A 22  ? 0.2037 0.1756 0.3586 -0.0225 0.0024  0.0248  22  ASP   A OD1 
576  O  OD1 B ASP   A 22  ? 0.1960 0.1787 0.2158 0.0274  0.0744  0.0275  22  ASP   A OD1 
577  O  OD2 A ASP   A 22  ? 0.2359 0.1865 0.3769 0.0067  0.0210  -0.0153 22  ASP   A OD2 
578  O  OD2 B ASP   A 22  ? 0.2034 0.1909 0.2436 0.0177  0.0796  0.0225  22  ASP   A OD2 
587  N  N   A ILE   A 23  ? 0.1684 0.1812 0.2318 -0.0102 0.0311  0.0253  23  ILE   A N   
588  N  N   B ILE   A 23  ? 0.1595 0.1698 0.1560 -0.0047 0.0386  0.0174  23  ILE   A N   
589  C  CA  A ILE   A 23  ? 0.1667 0.1742 0.2012 -0.0097 0.0325  0.0263  23  ILE   A CA  
590  C  CA  B ILE   A 23  ? 0.1539 0.1728 0.1556 -0.0081 0.0161  0.0202  23  ILE   A CA  
591  C  C   A ILE   A 23  ? 0.1628 0.1832 0.1868 -0.0108 0.0499  0.0173  23  ILE   A C   
592  C  C   B ILE   A 23  ? 0.1620 0.1795 0.1536 -0.0155 0.0139  0.0141  23  ILE   A C   
593  O  O   A ILE   A 23  ? 0.1674 0.1888 0.1993 0.0001  0.0504  0.0066  23  ILE   A O   
594  O  O   B ILE   A 23  ? 0.1644 0.1750 0.1508 -0.0157 0.0064  0.0117  23  ILE   A O   
595  C  CB  A ILE   A 23  ? 0.1800 0.1716 0.1810 -0.0015 0.0200  0.0262  23  ILE   A CB  
596  C  CB  B ILE   A 23  ? 0.1428 0.1670 0.1454 -0.0077 0.0050  0.0306  23  ILE   A CB  
597  C  CG1 A ILE   A 23  ? 0.1803 0.1741 0.1756 0.0043  0.0172  0.0137  23  ILE   A CG1 
598  C  CG1 B ILE   A 23  ? 0.1420 0.1638 0.1446 -0.0071 -0.0078 0.0236  23  ILE   A CG1 
599  C  CG2 A ILE   A 23  ? 0.1882 0.1724 0.1761 -0.0050 0.0146  0.0273  23  ILE   A CG2 
600  C  CG2 B ILE   A 23  ? 0.1401 0.1636 0.1469 -0.0022 -0.0003 0.0297  23  ILE   A CG2 
601  C  CD1 A ILE   A 23  ? 0.1785 0.1737 0.1758 0.0019  0.0048  0.0089  23  ILE   A CD1 
602  C  CD1 B ILE   A 23  ? 0.1373 0.1590 0.1436 -0.0091 -0.0197 0.0196  23  ILE   A CD1 
625  N  N   A VAL   A 24  ? 0.1717 0.1883 0.1901 -0.0139 0.0526  0.0052  24  VAL   A N   
626  N  N   B VAL   A 24  ? 0.1732 0.1919 0.1761 -0.0205 0.0154  0.0114  24  VAL   A N   
627  C  CA  A VAL   A 24  ? 0.1885 0.1976 0.2173 -0.0238 0.0487  0.0055  24  VAL   A CA  
628  C  CA  B VAL   A 24  ? 0.1832 0.2017 0.1925 -0.0192 0.0220  0.0068  24  VAL   A CA  
629  C  C   A VAL   A 24  ? 0.2047 0.2122 0.2231 -0.0295 0.0555  0.0066  24  VAL   A C   
630  C  C   B VAL   A 24  ? 0.1919 0.2145 0.2005 -0.0208 0.0375  -0.0075 24  VAL   A C   
631  O  O   A VAL   A 24  ? 0.2195 0.2117 0.2121 -0.0251 0.0557  0.0113  24  VAL   A O   
632  O  O   B VAL   A 24  ? 0.1982 0.2165 0.2076 -0.0160 0.0390  -0.0089 24  VAL   A O   
633  C  CB  A VAL   A 24  ? 0.1921 0.2013 0.2430 -0.0217 0.0457  0.0091  24  VAL   A CB  
634  C  CB  B VAL   A 24  ? 0.1843 0.2050 0.2129 -0.0164 0.0177  0.0180  24  VAL   A CB  
635  C  CG1 A VAL   A 24  ? 0.2016 0.2074 0.2484 -0.0183 0.0475  -0.0020 24  VAL   A CG1 
636  C  CG1 B VAL   A 24  ? 0.1915 0.2078 0.2218 -0.0139 0.0115  0.0179  24  VAL   A CG1 
637  C  CG2 A VAL   A 24  ? 0.2021 0.2059 0.2486 -0.0134 0.0508  0.0277  24  VAL   A CG2 
638  C  CG2 B VAL   A 24  ? 0.1840 0.2082 0.2156 -0.0142 0.0228  0.0245  24  VAL   A CG2 
657  N  N   A GLU   A 25  ? 0.2144 0.2387 0.2321 -0.0301 0.0691  -0.0047 25  GLU   A N   
658  N  N   B GLU   A 25  ? 0.1960 0.2250 0.2000 -0.0241 0.0554  -0.0132 25  GLU   A N   
659  C  CA  A GLU   A 25  ? 0.2376 0.2640 0.2447 -0.0248 0.0781  -0.0102 25  GLU   A CA  
660  C  CA  B GLU   A 25  ? 0.2050 0.2368 0.2132 -0.0294 0.0649  -0.0146 25  GLU   A CA  
661  C  C   A GLU   A 25  ? 0.2242 0.2608 0.2200 -0.0365 0.0857  -0.0143 25  GLU   A C   
662  C  C   B GLU   A 25  ? 0.2004 0.2413 0.1997 -0.0310 0.0719  -0.0150 25  GLU   A C   
663  O  O   A GLU   A 25  ? 0.2344 0.2690 0.2330 -0.0334 0.0846  -0.0164 25  GLU   A O   
664  O  O   B GLU   A 25  ? 0.2019 0.2429 0.1966 -0.0288 0.0785  -0.0187 25  GLU   A O   
665  C  CB  A GLU   A 25  ? 0.2664 0.2914 0.2877 -0.0184 0.0784  -0.0088 25  GLU   A CB  
666  C  CB  B GLU   A 25  ? 0.2181 0.2415 0.2355 -0.0319 0.0686  -0.0086 25  GLU   A CB  
667  C  CG  A GLU   A 25  ? 0.2926 0.3130 0.3342 -0.0191 0.0661  -0.0099 25  GLU   A CG  
668  C  CG  B GLU   A 25  ? 0.2338 0.2486 0.2645 -0.0364 0.0609  -0.0025 25  GLU   A CG  
669  C  CD  A GLU   A 25  ? 0.3123 0.3303 0.3731 -0.0245 0.0618  -0.0062 25  GLU   A CD  
670  C  CD  B GLU   A 25  ? 0.2470 0.2560 0.2927 -0.0416 0.0525  0.0011  25  GLU   A CD  
671  O  OE1 A GLU   A 25  ? 0.3226 0.3363 0.3834 -0.0228 0.0504  -0.0164 25  GLU   A OE1 
672  O  OE1 B GLU   A 25  ? 0.2513 0.2569 0.3027 -0.0426 0.0493  0.0032  25  GLU   A OE1 
673  O  OE2 A GLU   A 25  ? 0.3162 0.3393 0.3994 -0.0281 0.0608  -0.0095 25  GLU   A OE2 
674  O  OE2 B GLU   A 25  ? 0.2568 0.2607 0.3123 -0.0435 0.0486  0.0042  25  GLU   A OE2 
687  N  N   A GLU   A 26  ? 0.2129 0.2503 0.2215 -0.0538 0.0864  -0.0180 26  GLU   A N   
688  N  N   B GLU   A 26  ? 0.2012 0.2413 0.1979 -0.0343 0.0659  -0.0149 26  GLU   A N   
689  C  CA  A GLU   A 26  ? 0.2212 0.2472 0.2261 -0.0692 0.0811  -0.0035 26  GLU   A CA  
690  C  CA  B GLU   A 26  ? 0.2070 0.2439 0.1921 -0.0348 0.0640  -0.0187 26  GLU   A CA  
691  C  C   A GLU   A 26  ? 0.2126 0.2420 0.1963 -0.0682 0.0683  -0.0064 26  GLU   A C   
692  C  C   B GLU   A 26  ? 0.2122 0.2424 0.1782 -0.0321 0.0641  -0.0253 26  GLU   A C   
693  O  O   A GLU   A 26  ? 0.2170 0.2428 0.1782 -0.0667 0.0646  -0.0078 26  GLU   A O   
694  O  O   B GLU   A 26  ? 0.2123 0.2392 0.1807 -0.0285 0.0679  -0.0271 26  GLU   A O   
695  C  CB  A GLU   A 26  ? 0.2450 0.2415 0.2633 -0.0775 0.0689  0.0008  26  GLU   A CB  
696  C  CB  B GLU   A 26  ? 0.2127 0.2526 0.2111 -0.0381 0.0471  -0.0198 26  GLU   A CB  
697  C  CG  A GLU   A 26  ? 0.2687 0.2496 0.3135 -0.0770 0.0721  -0.0098 26  GLU   A CG  
698  C  CG  B GLU   A 26  ? 0.2151 0.2581 0.2195 -0.0442 0.0467  -0.0174 26  GLU   A CG  
699  C  CD  A GLU   A 26  ? 0.2819 0.2531 0.3425 -0.0824 0.0936  -0.0188 26  GLU   A CD  
700  C  CD  B GLU   A 26  ? 0.2175 0.2629 0.2278 -0.0543 0.0476  -0.0150 26  GLU   A CD  
701  O  OE1 A GLU   A 26  ? 0.2751 0.2751 0.3367 -0.0653 0.1320  -0.0683 26  GLU   A OE1 
702  O  OE1 B GLU   A 26  ? 0.2249 0.2781 0.2337 -0.0454 0.0528  -0.0206 26  GLU   A OE1 
703  O  OE2 A GLU   A 26  ? 0.2994 0.2529 0.3382 -0.0829 0.0866  -0.0028 26  GLU   A OE2 
704  O  OE2 B GLU   A 26  ? 0.2094 0.2559 0.2091 -0.0689 0.0570  -0.0136 26  GLU   A OE2 
717  N  N   A ALA   A 27  ? 0.1933 0.2304 0.1767 -0.0719 0.0629  -0.0065 27  ALA   A N   
718  N  N   B ALA   A 27  ? 0.2182 0.2445 0.1708 -0.0369 0.0566  -0.0248 27  ALA   A N   
719  C  CA  A ALA   A 27  ? 0.2011 0.2343 0.1623 -0.0685 0.0526  0.0017  27  ALA   A CA  
720  C  CA  B ALA   A 27  ? 0.2297 0.2514 0.1646 -0.0399 0.0498  -0.0248 27  ALA   A CA  
721  C  C   A ALA   A 27  ? 0.2299 0.2490 0.1659 -0.0685 0.0507  -0.0103 27  ALA   A C   
722  C  C   B ALA   A 27  ? 0.2455 0.2615 0.1690 -0.0475 0.0483  -0.0296 27  ALA   A C   
723  O  O   A ALA   A 27  ? 0.2365 0.2497 0.1687 -0.0743 0.0370  -0.0123 27  ALA   A O   
724  O  O   B ALA   A 27  ? 0.2487 0.2619 0.1687 -0.0479 0.0409  -0.0306 27  ALA   A O   
725  C  CB  A ALA   A 27  ? 0.1892 0.2267 0.1781 -0.0701 0.0472  0.0080  27  ALA   A CB  
726  C  CB  B ALA   A 27  ? 0.2280 0.2494 0.1654 -0.0388 0.0477  -0.0217 27  ALA   A CB  
737  N  N   . LYS   A 28  ? 0.2604 0.2725 0.1800 -0.0547 0.0517  -0.0405 28  LYS   A N   
738  C  CA  . LYS   A 28  ? 0.3069 0.3155 0.2304 -0.0541 0.0458  -0.0565 28  LYS   A CA  
739  C  C   . LYS   A 28  ? 0.3287 0.3481 0.2185 -0.0577 0.0654  -0.0463 28  LYS   A C   
740  O  O   . LYS   A 28  ? 0.3347 0.3589 0.2627 -0.0563 0.0427  -0.0364 28  LYS   A O   
741  C  CB  . LYS   A 28  ? 0.3296 0.3294 0.2767 -0.0442 0.0389  -0.0766 28  LYS   A CB  
742  C  CG  . LYS   A 28  ? 0.3478 0.3404 0.3277 -0.0351 0.0392  -0.0871 28  LYS   A CG  
743  C  CD  . LYS   A 28  ? 0.3626 0.3571 0.3931 -0.0251 0.0384  -0.0880 28  LYS   A CD  
744  C  CE  . LYS   A 28  ? 0.3709 0.3657 0.4370 -0.0208 0.0336  -0.0889 28  LYS   A CE  
745  N  NZ  . LYS   A 28  ? 0.3764 0.3703 0.4643 -0.0157 0.0319  -0.0828 28  LYS   A NZ  
760  N  N   . LYS   A 29  ? 0.3394 0.3724 0.2048 -0.0670 0.0983  -0.0252 29  LYS   A N   
761  C  CA  . LYS   A 29  ? 0.3599 0.3993 0.2243 -0.0729 0.1039  -0.0071 29  LYS   A CA  
762  C  C   . LYS   A 29  ? 0.3583 0.3925 0.1877 -0.0814 0.0922  -0.0053 29  LYS   A C   
763  O  O   . LYS   A 29  ? 0.3716 0.4000 0.2011 -0.0724 0.0853  -0.0029 29  LYS   A O   
764  C  CB  . LYS   A 29  ? 0.3782 0.4289 0.2971 -0.0669 0.1174  0.0055  29  LYS   A CB  
765  C  CG  . LYS   A 29  ? 0.3964 0.4512 0.3738 -0.0610 0.1241  0.0105  29  LYS   A CG  
766  C  CD  . LYS   A 29  ? 0.4127 0.4703 0.4465 -0.0557 0.1256  0.0106  29  LYS   A CD  
767  C  CE  . LYS   A 29  ? 0.4247 0.4828 0.5026 -0.0507 0.1258  0.0130  29  LYS   A CE  
768  N  NZ  . LYS   A 29  ? 0.4304 0.4898 0.5323 -0.0469 0.1230  0.0141  29  LYS   A NZ  
782  N  N   . VAL   A 30  ? 0.3389 0.3739 0.1726 -0.1005 0.0943  -0.0013 30  VAL   A N   
783  C  CA  . VAL   A 30  ? 0.3316 0.3586 0.1648 -0.1120 0.0671  0.0155  30  VAL   A CA  
784  C  C   . VAL   A 30  ? 0.3312 0.3409 0.1367 -0.1089 0.0485  0.0265  30  VAL   A C   
785  O  O   . VAL   A 30  ? 0.3404 0.3458 0.1377 -0.1108 0.0445  0.0307  30  VAL   A O   
786  C  CB  . VAL   A 30  ? 0.3275 0.3552 0.2115 -0.1260 0.0401  0.0159  30  VAL   A CB  
787  C  CG1 . VAL   A 30  ? 0.3327 0.3584 0.2344 -0.1236 0.0271  0.0191  30  VAL   A CG1 
788  C  CG2 . VAL   A 30  ? 0.3240 0.3532 0.2442 -0.1318 0.0441  0.0184  30  VAL   A CG2 
798  N  N   . LYS   A 31  ? 0.3210 0.3212 0.1261 -0.1124 0.0376  0.0170  31  LYS   A N   
799  C  CA  . LYS   A 31  ? 0.3338 0.3135 0.1434 -0.1012 0.0111  0.0046  31  LYS   A CA  
800  C  C   . LYS   A 31  ? 0.3080 0.2876 0.1240 -0.0817 0.0105  0.0379  31  LYS   A C   
801  O  O   . LYS   A 31  ? 0.3138 0.2970 0.1472 -0.0768 -0.0091 0.0590  31  LYS   A O   
802  C  CB  . LYS   A 31  ? 0.3756 0.3371 0.2448 -0.0972 -0.0083 -0.0204 31  LYS   A CB  
803  C  CG  . LYS   A 31  ? 0.4167 0.3713 0.3737 -0.0820 -0.0241 -0.0299 31  LYS   A CG  
804  C  CD  . LYS   A 31  ? 0.4472 0.3995 0.4758 -0.0721 -0.0426 -0.0398 31  LYS   A CD  
805  C  CE  . LYS   A 31  ? 0.4699 0.4127 0.5392 -0.0653 -0.0586 -0.0500 31  LYS   A CE  
806  N  NZ  . LYS   A 31  ? 0.4835 0.4156 0.5691 -0.0635 -0.0667 -0.0552 31  LYS   A NZ  
820  N  N   . PRO   A 32  ? 0.2687 0.2558 0.1094 -0.0696 0.0089  0.0333  32  PRO   A N   
821  C  CA  . PRO   A 32  ? 0.2596 0.2344 0.1437 -0.0682 0.0031  0.0457  32  PRO   A CA  
822  C  C   . PRO   A 32  ? 0.2548 0.2288 0.1540 -0.0542 -0.0122 0.0456  32  PRO   A C   
823  O  O   . PRO   A 32  ? 0.2465 0.2231 0.1545 -0.0576 -0.0255 0.0437  32  PRO   A O   
824  C  CB  . PRO   A 32  ? 0.2560 0.2416 0.1482 -0.0651 -0.0104 0.0344  32  PRO   A CB  
825  C  CG  . PRO   A 32  ? 0.2493 0.2449 0.1118 -0.0626 -0.0204 0.0179  32  PRO   A CG  
826  C  CD  . PRO   A 32  ? 0.2553 0.2456 0.1174 -0.0603 -0.0060 0.0258  32  PRO   A CD  
834  N  N   . THR   A 33  ? 0.2618 0.2233 0.1473 -0.0480 -0.0129 0.0578  33  THR   A N   
835  C  CA  . THR   A 33  ? 0.2606 0.2224 0.1600 -0.0343 -0.0218 0.0553  33  THR   A CA  
836  C  C   . THR   A 33  ? 0.2279 0.2031 0.1458 -0.0362 -0.0279 0.0417  33  THR   A C   
837  O  O   . THR   A 33  ? 0.2213 0.2102 0.1481 -0.0350 -0.0423 0.0484  33  THR   A O   
838  C  CB  . THR   A 33  ? 0.2839 0.2402 0.1787 -0.0230 -0.0316 0.0690  33  THR   A CB  
839  O  OG1 . THR   A 33  ? 0.3018 0.2486 0.2089 -0.0110 -0.0272 0.0815  33  THR   A OG1 
840  C  CG2 . THR   A 33  ? 0.2872 0.2565 0.2083 -0.0139 -0.0425 0.0662  33  THR   A CG2 
848  N  N   . VAL   A 34  ? 0.2023 0.1893 0.1349 -0.0374 -0.0222 0.0411  34  VAL   A N   
849  C  CA  . VAL   A 34  ? 0.1838 0.1744 0.1319 -0.0311 -0.0132 0.0360  34  VAL   A CA  
850  C  C   . VAL   A 34  ? 0.1671 0.1712 0.1201 -0.0245 -0.0058 0.0311  34  VAL   A C   
851  O  O   . VAL   A 34  ? 0.1658 0.1757 0.1470 -0.0364 -0.0057 0.0401  34  VAL   A O   
852  C  CB  . VAL   A 34  ? 0.1882 0.1706 0.1500 -0.0264 -0.0150 0.0200  34  VAL   A CB  
853  C  CG1 . VAL   A 34  ? 0.1881 0.1690 0.1544 -0.0254 -0.0010 0.0115  34  VAL   A CG1 
854  C  CG2 . VAL   A 34  ? 0.1881 0.1837 0.1757 -0.0208 -0.0328 0.0224  34  VAL   A CG2 
864  N  N   . VAL   A 35  ? 0.1585 0.1596 0.1171 -0.0257 -0.0104 0.0233  35  VAL   A N   
865  C  CA  . VAL   A 35  ? 0.1480 0.1536 0.1192 -0.0254 0.0025  0.0194  35  VAL   A CA  
866  C  C   . VAL   A 35  ? 0.1360 0.1425 0.1177 -0.0173 0.0037  0.0241  35  VAL   A C   
867  O  O   . VAL   A 35  ? 0.1361 0.1550 0.1167 -0.0253 0.0078  0.0132  35  VAL   A O   
868  C  CB  . VAL   A 35  ? 0.1547 0.1598 0.1364 -0.0159 0.0154  0.0071  35  VAL   A CB  
869  C  CG1 . VAL   A 35  ? 0.1720 0.1559 0.1388 -0.0058 0.0082  -0.0021 35  VAL   A CG1 
870  C  CG2 . VAL   A 35  ? 0.1505 0.1601 0.1577 -0.0116 0.0161  -0.0033 35  VAL   A CG2 
880  N  N   . VAL   A 36  ? 0.1254 0.1394 0.1085 -0.0214 0.0101  0.0204  36  VAL   A N   
881  C  CA  . VAL   A 36  ? 0.1196 0.1286 0.1226 -0.0099 0.0014  0.0135  36  VAL   A CA  
882  C  C   . VAL   A 36  ? 0.1161 0.1299 0.1346 -0.0137 0.0120  0.0103  36  VAL   A C   
883  O  O   . VAL   A 36  ? 0.1300 0.1313 0.1384 -0.0050 0.0214  0.0098  36  VAL   A O   
884  C  CB  . VAL   A 36  ? 0.1228 0.1223 0.1303 -0.0098 0.0014  0.0128  36  VAL   A CB  
885  C  CG1 . VAL   A 36  ? 0.1331 0.1265 0.1423 -0.0185 -0.0027 0.0054  36  VAL   A CG1 
886  C  CG2 . VAL   A 36  ? 0.1291 0.1254 0.1632 -0.0071 -0.0030 0.0182  36  VAL   A CG2 
896  N  N   . ASN   A 37  ? 0.1124 0.1206 0.1201 -0.0045 0.0032  0.0075  37  ASN   A N   
897  C  CA  . ASN   A 37  ? 0.1118 0.1190 0.1185 0.0043  0.0041  0.0185  37  ASN   A CA  
898  C  C   . ASN   A 37  ? 0.1161 0.1156 0.1206 -0.0017 0.0093  0.0187  37  ASN   A C   
899  O  O   . ASN   A 37  ? 0.1270 0.1259 0.1087 0.0038  0.0057  0.0073  37  ASN   A O   
900  C  CB  . ASN   A 37  ? 0.1119 0.1171 0.1338 0.0023  0.0086  0.0058  37  ASN   A CB  
901  C  CG  . ASN   A 37  ? 0.1155 0.1200 0.1499 0.0033  0.0077  0.0097  37  ASN   A CG  
902  O  OD1 . ASN   A 37  ? 0.1220 0.1230 0.1415 -0.0008 0.0010  0.0105  37  ASN   A OD1 
903  N  ND2 . ASN   A 37  ? 0.1172 0.1245 0.1432 0.0001  0.0013  0.0237  37  ASN   A ND2 
910  N  N   . ALA   A 38  ? 0.1174 0.1303 0.1273 0.0046  0.0079  0.0126  38  ALA   A N   
911  C  CA  . ALA   A 38  ? 0.1237 0.1350 0.1143 0.0003  -0.0004 0.0065  38  ALA   A CA  
912  C  C   . ALA   A 38  ? 0.1226 0.1307 0.1250 0.0078  -0.0056 0.0031  38  ALA   A C   
913  O  O   . ALA   A 38  ? 0.1234 0.1280 0.1298 0.0084  -0.0019 0.0086  38  ALA   A O   
914  C  CB  . ALA   A 38  ? 0.1274 0.1713 0.1545 -0.0196 -0.0067 0.0101  38  ALA   A CB  
920  N  N   . ALA   A 39  ? 0.1234 0.1290 0.1359 0.0084  0.0034  0.0111  39  ALA   A N   
921  C  CA  . ALA   A 39  ? 0.1267 0.1232 0.1391 0.0041  0.0098  0.0121  39  ALA   A CA  
922  C  C   . ALA   A 39  ? 0.1318 0.1218 0.1313 0.0049  0.0094  0.0037  39  ALA   A C   
923  O  O   . ALA   A 39  ? 0.1414 0.1235 0.1300 -0.0044 0.0013  0.0011  39  ALA   A O   
924  C  CB  . ALA   A 39  ? 0.1236 0.1393 0.1367 0.0005  -0.0102 0.0010  39  ALA   A CB  
930  N  N   . ASN   A 40  ? 0.1411 0.1239 0.1437 -0.0001 0.0192  0.0037  40  ASN   A N   
931  C  CA  . ASN   A 40  ? 0.1505 0.1178 0.1372 -0.0028 0.0068  0.0040  40  ASN   A CA  
932  C  C   . ASN   A 40  ? 0.1526 0.1150 0.1131 -0.0052 0.0201  0.0102  40  ASN   A C   
933  O  O   . ASN   A 40  ? 0.1488 0.1150 0.1221 -0.0060 0.0170  0.0119  40  ASN   A O   
934  C  CB  . ASN   A 40  ? 0.1635 0.1216 0.1560 0.0056  0.0003  0.0041  40  ASN   A CB  
935  C  CG  . ASN   A 40  ? 0.1696 0.1310 0.1851 0.0053  -0.0046 0.0074  40  ASN   A CG  
936  O  OD1 . ASN   A 40  ? 0.1825 0.1352 0.2161 -0.0003 0.0096  -0.0033 40  ASN   A OD1 
937  N  ND2 . ASN   A 40  ? 0.1733 0.1474 0.2067 0.0057  -0.0005 -0.0078 40  ASN   A ND2 
944  N  N   . VAL   A 41  ? 0.1652 0.1182 0.1198 -0.0057 0.0232  0.0118  41  VAL   A N   
945  C  CA  . VAL   A 41  ? 0.1713 0.1275 0.1460 -0.0054 0.0339  0.0117  41  VAL   A CA  
946  C  C   . VAL   A 41  ? 0.1607 0.1236 0.1525 -0.0045 0.0457  0.0050  41  VAL   A C   
947  O  O   . VAL   A 41  ? 0.1642 0.1183 0.1834 0.0024  0.0384  0.0046  41  VAL   A O   
948  C  CB  . VAL   A 41  ? 0.1945 0.1355 0.1553 -0.0149 0.0530  0.0011  41  VAL   A CB  
949  C  CG1 . VAL   A 41  ? 0.2097 0.1499 0.1647 -0.0070 0.0555  -0.0056 41  VAL   A CG1 
950  C  CG2 . VAL   A 41  ? 0.2158 0.1483 0.1545 -0.0225 0.0495  -0.0011 41  VAL   A CG2 
960  N  N   . TYR   A 42  ? 0.1497 0.1173 0.1605 -0.0004 0.0418  0.0167  42  TYR   A N   
961  C  CA  . TYR   A 42  ? 0.1515 0.1154 0.1624 -0.0026 0.0403  0.0199  42  TYR   A CA  
962  C  C   . TYR   A 42  ? 0.1411 0.1202 0.1640 0.0020  0.0352  0.0211  42  TYR   A C   
963  O  O   . TYR   A 42  ? 0.1429 0.1238 0.1796 -0.0101 0.0285  0.0019  42  TYR   A O   
964  C  CB  . TYR   A 42  ? 0.1734 0.1305 0.1665 -0.0043 0.0333  0.0271  42  TYR   A CB  
965  C  CG  . TYR   A 42  ? 0.1908 0.1397 0.1689 -0.0069 0.0330  0.0302  42  TYR   A CG  
966  C  CD1 . TYR   A 42  ? 0.1958 0.1532 0.1738 -0.0097 0.0292  0.0286  42  TYR   A CD1 
967  C  CD2 . TYR   A 42  ? 0.2008 0.1612 0.1940 -0.0029 0.0226  0.0217  42  TYR   A CD2 
968  C  CE1 . TYR   A 42  ? 0.2025 0.1639 0.1836 -0.0159 0.0378  0.0250  42  TYR   A CE1 
969  C  CE2 . TYR   A 42  ? 0.2118 0.1777 0.2029 -0.0205 0.0221  0.0214  42  TYR   A CE2 
970  C  CZ  . TYR   A 42  ? 0.2173 0.1777 0.1834 -0.0241 0.0340  0.0192  42  TYR   A CZ  
971  O  OH  . TYR   A 42  ? 0.2322 0.2059 0.2027 -0.0354 0.0360  0.0117  42  TYR   A OH  
981  N  N   . LEU   A 43  ? 0.1374 0.1194 0.1563 -0.0018 0.0215  0.0098  43  LEU   A N   
982  C  CA  . LEU   A 43  ? 0.1240 0.1197 0.1521 -0.0056 0.0138  0.0076  43  LEU   A CA  
983  C  C   . LEU   A 43  ? 0.1285 0.1215 0.1548 -0.0017 0.0104  0.0063  43  LEU   A C   
984  O  O   . LEU   A 43  ? 0.1437 0.1252 0.1606 0.0051  0.0010  -0.0044 43  LEU   A O   
985  C  CB  . LEU   A 43  ? 0.1323 0.1187 0.1568 -0.0066 0.0095  0.0116  43  LEU   A CB  
986  C  CG  . LEU   A 43  ? 0.1359 0.1199 0.1655 -0.0036 0.0090  0.0036  43  LEU   A CG  
987  C  CD1 . LEU   A 43  ? 0.1417 0.1243 0.1821 0.0018  0.0044  0.0155  43  LEU   A CD1 
988  C  CD2 . LEU   A 43  ? 0.1521 0.1250 0.1689 -0.0070 0.0057  0.0180  43  LEU   A CD2 
1000 N  N   . LYS   A 44  ? 0.1350 0.1230 0.1420 0.0006  0.0096  0.0098  44  LYS   A N   
1001 C  CA  . LYS   A 44  ? 0.1483 0.1200 0.1540 -0.0054 0.0142  0.0199  44  LYS   A CA  
1002 C  C   . LYS   A 44  ? 0.1367 0.1212 0.1367 0.0037  0.0105  0.0084  44  LYS   A C   
1003 O  O   . LYS   A 44  ? 0.1425 0.1367 0.1593 0.0000  0.0003  -0.0020 44  LYS   A O   
1004 C  CB  . LYS   A 44  ? 0.1754 0.1385 0.1965 0.0036  0.0273  0.0262  44  LYS   A CB  
1005 C  CG  . LYS   A 44  ? 0.2050 0.1684 0.2562 -0.0051 0.0527  0.0385  44  LYS   A CG  
1006 C  CD  . LYS   A 44  ? 0.2454 0.2241 0.3739 -0.0133 0.0358  0.0241  44  LYS   A CD  
1007 C  CE  . LYS   A 44  ? 0.2654 0.2542 0.4504 -0.0154 0.0277  0.0185  44  LYS   A CE  
1008 N  NZ  . LYS   A 44  ? 0.2637 0.2629 0.4823 -0.0167 0.0271  0.0197  44  LYS   A NZ  
1022 N  N   . HIS   A 45  ? 0.1312 0.1181 0.1344 0.0058  -0.0004 0.0149  45  HIS   A N   
1023 C  CA  . HIS   A 45  ? 0.1280 0.1242 0.1408 0.0045  -0.0007 0.0062  45  HIS   A CA  
1024 C  C   . HIS   A 45  ? 0.1312 0.1359 0.1461 0.0058  -0.0017 0.0093  45  HIS   A C   
1025 O  O   . HIS   A 45  ? 0.1480 0.1454 0.1742 0.0205  -0.0006 -0.0065 45  HIS   A O   
1026 C  CB  . HIS   A 45  ? 0.1261 0.1239 0.1360 0.0055  0.0017  0.0030  45  HIS   A CB  
1027 C  CG  . HIS   A 45  ? 0.1213 0.1230 0.1280 -0.0027 0.0055  0.0049  45  HIS   A CG  
1028 N  ND1 . HIS   A 45  ? 0.1166 0.1260 0.1479 -0.0005 0.0006  0.0127  45  HIS   A ND1 
1029 C  CD2 . HIS   A 45  ? 0.1211 0.1254 0.1396 -0.0115 -0.0030 0.0170  45  HIS   A CD2 
1030 C  CE1 . HIS   A 45  ? 0.1193 0.1254 0.1338 -0.0062 -0.0023 0.0172  45  HIS   A CE1 
1031 N  NE2 . HIS   A 45  ? 0.1221 0.1285 0.1323 -0.0011 -0.0050 0.0144  45  HIS   A NE2 
1039 N  N   A GLY   A 46  ? 0.1413 0.1423 0.1745 0.0101  -0.0173 0.0192  46  GLY   A N   
1040 N  N   B GLY   A 46  ? 0.1378 0.1399 0.1524 0.0136  -0.0091 0.0101  46  GLY   A N   
1041 C  CA  A GLY   A 46  ? 0.1470 0.1457 0.1860 0.0090  -0.0245 0.0285  46  GLY   A CA  
1042 C  CA  B GLY   A 46  ? 0.1437 0.1417 0.1522 0.0167  -0.0160 0.0092  46  GLY   A CA  
1043 C  C   A GLY   A 46  ? 0.1481 0.1413 0.1879 0.0167  -0.0330 0.0345  46  GLY   A C   
1044 C  C   B GLY   A 46  ? 0.1472 0.1381 0.1452 0.0242  -0.0206 0.0042  46  GLY   A C   
1045 O  O   A GLY   A 46  ? 0.1495 0.1469 0.2070 0.0128  -0.0421 0.0206  46  GLY   A O   
1046 O  O   B GLY   A 46  ? 0.1463 0.1404 0.1533 0.0286  -0.0173 -0.0056 46  GLY   A O   
1053 N  N   A GLY   A 47  ? 0.1506 0.1398 0.1759 0.0223  -0.0251 0.0216  47  GLY   A N   
1054 N  N   B GLY   A 47  ? 0.1524 0.1380 0.1451 0.0259  -0.0199 0.0016  47  GLY   A N   
1055 C  CA  A GLY   A 47  ? 0.1522 0.1445 0.1671 0.0176  -0.0435 0.0082  47  GLY   A CA  
1056 C  CA  B GLY   A 47  ? 0.1570 0.1397 0.1409 0.0253  -0.0222 0.0015  47  GLY   A CA  
1057 C  C   A GLY   A 47  ? 0.1522 0.1340 0.1606 0.0212  -0.0525 0.0011  47  GLY   A C   
1058 C  C   B GLY   A 47  ? 0.1614 0.1366 0.1276 0.0239  -0.0213 -0.0044 47  GLY   A C   
1059 O  O   A GLY   A 47  ? 0.1539 0.1313 0.1760 0.0266  -0.0470 0.0063  47  GLY   A O   
1060 O  O   B GLY   A 47  ? 0.1647 0.1381 0.1311 0.0256  -0.0095 0.0012  47  GLY   A O   
1067 N  N   A GLY   A 48  ? 0.1467 0.1425 0.1653 0.0183  -0.0559 -0.0068 48  GLY   A N   
1068 N  N   B GLY   A 48  ? 0.1600 0.1359 0.1448 0.0177  -0.0227 -0.0052 48  GLY   A N   
1069 C  CA  A GLY   A 48  ? 0.1488 0.1421 0.1779 0.0042  -0.0430 -0.0116 48  GLY   A CA  
1070 C  CA  B GLY   A 48  ? 0.1538 0.1316 0.1451 0.0134  -0.0167 -0.0136 48  GLY   A CA  
1071 C  C   A GLY   A 48  ? 0.1365 0.1365 0.1640 -0.0024 -0.0239 -0.0074 48  GLY   A C   
1072 C  C   B GLY   A 48  ? 0.1439 0.1274 0.1397 0.0116  -0.0067 -0.0057 48  GLY   A C   
1073 O  O   A GLY   A 48  ? 0.1500 0.1365 0.1599 -0.0049 -0.0172 -0.0117 48  GLY   A O   
1074 O  O   B GLY   A 48  ? 0.1487 0.1278 0.1300 0.0089  -0.0035 -0.0006 48  GLY   A O   
1081 N  N   A VAL   A 49  ? 0.1200 0.1288 0.1769 -0.0055 -0.0177 -0.0013 49  VAL   A N   
1082 N  N   B VAL   A 49  ? 0.1297 0.1220 0.1385 0.0058  -0.0052 -0.0138 49  VAL   A N   
1083 C  CA  A VAL   A 49  ? 0.1280 0.1271 0.1694 -0.0071 0.0090  -0.0016 49  VAL   A CA  
1084 C  CA  B VAL   A 49  ? 0.1171 0.1227 0.1314 0.0059  0.0040  -0.0091 49  VAL   A CA  
1085 C  C   A VAL   A 49  ? 0.1263 0.1178 0.1450 -0.0014 0.0013  0.0073  49  VAL   A C   
1086 C  C   B VAL   A 49  ? 0.1164 0.1193 0.1168 0.0093  0.0045  -0.0094 49  VAL   A C   
1087 O  O   A VAL   A 49  ? 0.1294 0.1225 0.1405 -0.0057 0.0108  0.0034  49  VAL   A O   
1088 O  O   B VAL   A 49  ? 0.1163 0.1153 0.1132 0.0150  0.0026  -0.0019 49  VAL   A O   
1089 C  CB  A VAL   A 49  ? 0.1521 0.1302 0.1833 -0.0084 0.0091  -0.0085 49  VAL   A CB  
1090 C  CB  B VAL   A 49  ? 0.1057 0.1195 0.1405 0.0125  0.0034  0.0028  49  VAL   A CB  
1091 C  CG1 A VAL   A 49  ? 0.1626 0.1220 0.1920 -0.0033 0.0153  -0.0035 49  VAL   A CG1 
1092 C  CG1 B VAL   A 49  ? 0.0932 0.1188 0.1363 0.0192  0.0019  0.0108  49  VAL   A CG1 
1093 C  CG2 A VAL   A 49  ? 0.1684 0.1470 0.2289 -0.0240 0.0013  -0.0096 49  VAL   A CG2 
1094 C  CG2 B VAL   A 49  ? 0.1037 0.1221 0.1519 0.0104  0.0129  0.0104  49  VAL   A CG2 
1113 N  N   A ALA   A 50  ? 0.1234 0.1128 0.1445 -0.0043 -0.0131 0.0152  50  ALA   A N   
1114 N  N   B ALA   A 50  ? 0.1202 0.1163 0.1091 0.0136  0.0031  -0.0165 50  ALA   A N   
1115 C  CA  A ALA   A 50  ? 0.1136 0.1152 0.1496 -0.0045 -0.0042 0.0204  50  ALA   A CA  
1116 C  CA  B ALA   A 50  ? 0.1261 0.1183 0.1131 0.0082  -0.0043 -0.0176 50  ALA   A CA  
1117 C  C   A ALA   A 50  ? 0.1100 0.1214 0.1496 -0.0088 -0.0030 0.0173  50  ALA   A C   
1118 C  C   B ALA   A 50  ? 0.1245 0.1207 0.0941 0.0083  -0.0124 -0.0246 50  ALA   A C   
1119 O  O   A ALA   A 50  ? 0.1193 0.1233 0.1699 -0.0034 -0.0130 0.0220  50  ALA   A O   
1120 O  O   B ALA   A 50  ? 0.1223 0.1215 0.0764 0.0153  -0.0034 -0.0362 50  ALA   A O   
1121 C  CB  A ALA   A 50  ? 0.1084 0.1164 0.1506 -0.0107 -0.0077 0.0071  50  ALA   A CB  
1122 C  CB  B ALA   A 50  ? 0.1340 0.1157 0.1209 0.0070  0.0058  -0.0272 50  ALA   A CB  
1133 N  N   A GLY   A 51  ? 0.1205 0.1106 0.1540 0.0017  -0.0080 0.0118  51  GLY   A N   
1134 N  N   B GLY   A 51  ? 0.1285 0.1172 0.1153 0.0088  -0.0261 -0.0247 51  GLY   A N   
1135 C  CA  A GLY   A 51  ? 0.1320 0.1132 0.1533 0.0081  -0.0095 0.0079  51  GLY   A CA  
1136 C  CA  B GLY   A 51  ? 0.1302 0.1187 0.1140 0.0112  -0.0307 -0.0250 51  GLY   A CA  
1137 C  C   A GLY   A 51  ? 0.1245 0.1203 0.1442 0.0095  0.0038  -0.0025 51  GLY   A C   
1138 C  C   B GLY   A 51  ? 0.1281 0.1228 0.1312 0.0144  -0.0218 -0.0182 51  GLY   A C   
1139 O  O   A GLY   A 51  ? 0.1276 0.1283 0.1531 -0.0015 0.0032  -0.0047 51  GLY   A O   
1140 O  O   B GLY   A 51  ? 0.1350 0.1233 0.1451 0.0134  -0.0134 -0.0184 51  GLY   A O   
1147 N  N   A ALA   A 52  ? 0.1228 0.1255 0.1401 0.0001  0.0028  -0.0121 52  ALA   A N   
1148 N  N   B ALA   A 52  ? 0.1260 0.1264 0.1338 0.0098  -0.0124 -0.0163 52  ALA   A N   
1149 C  CA  A ALA   A 52  ? 0.1225 0.1299 0.1503 -0.0005 0.0010  -0.0060 52  ALA   A CA  
1150 C  CA  B ALA   A 52  ? 0.1170 0.1276 0.1433 0.0087  -0.0066 -0.0169 52  ALA   A CA  
1151 C  C   A ALA   A 52  ? 0.1203 0.1267 0.1304 -0.0077 0.0021  -0.0093 52  ALA   A C   
1152 C  C   B ALA   A 52  ? 0.1170 0.1300 0.1378 -0.0004 0.0057  -0.0095 52  ALA   A C   
1153 O  O   A ALA   A 52  ? 0.1314 0.1383 0.1517 0.0014  -0.0001 -0.0182 52  ALA   A O   
1154 O  O   B ALA   A 52  ? 0.1258 0.1259 0.1503 -0.0022 0.0163  -0.0125 52  ALA   A O   
1155 C  CB  A ALA   A 52  ? 0.1260 0.1392 0.1597 0.0018  -0.0026 0.0005  52  ALA   A CB  
1156 C  CB  B ALA   A 52  ? 0.1068 0.1322 0.1492 0.0091  -0.0226 -0.0182 52  ALA   A CB  
1167 N  N   A LEU   A 53  ? 0.1201 0.1277 0.1345 -0.0065 -0.0019 -0.0016 53  LEU   A N   
1168 N  N   B LEU   A 53  ? 0.1093 0.1308 0.1278 0.0003  0.0030  0.0003  53  LEU   A N   
1169 C  CA  A LEU   A 53  ? 0.1292 0.1389 0.1272 -0.0024 0.0020  0.0007  53  LEU   A CA  
1170 C  CA  B LEU   A 53  ? 0.1093 0.1334 0.1104 0.0012  0.0043  0.0006  53  LEU   A CA  
1171 C  C   A LEU   A 53  ? 0.1282 0.1382 0.1065 0.0002  -0.0047 -0.0069 53  LEU   A C   
1172 C  C   B LEU   A 53  ? 0.1115 0.1386 0.1084 -0.0025 0.0087  -0.0025 53  LEU   A C   
1173 O  O   A LEU   A 53  ? 0.1415 0.1461 0.1224 -0.0095 -0.0044 -0.0038 53  LEU   A O   
1174 O  O   B LEU   A 53  ? 0.1141 0.1437 0.1203 -0.0106 0.0201  -0.0004 53  LEU   A O   
1175 C  CB  A LEU   A 53  ? 0.1318 0.1407 0.1474 -0.0021 0.0096  0.0082  53  LEU   A CB  
1176 C  CB  B LEU   A 53  ? 0.1036 0.1278 0.1051 -0.0020 0.0009  -0.0018 53  LEU   A CB  
1177 C  CG  A LEU   A 53  ? 0.1380 0.1407 0.1540 -0.0008 0.0090  0.0093  53  LEU   A CG  
1178 C  CG  B LEU   A 53  ? 0.1033 0.1235 0.1137 -0.0033 -0.0109 -0.0062 53  LEU   A CG  
1179 C  CD1 A LEU   A 53  ? 0.1388 0.1474 0.1551 0.0021  0.0024  0.0145  53  LEU   A CD1 
1180 C  CD1 B LEU   A 53  ? 0.1069 0.1301 0.1152 -0.0055 -0.0032 -0.0141 53  LEU   A CD1 
1181 C  CD2 A LEU   A 53  ? 0.1493 0.1501 0.1633 -0.0108 0.0040  0.0182  53  LEU   A CD2 
1182 C  CD2 B LEU   A 53  ? 0.0960 0.1125 0.1227 -0.0038 -0.0003 0.0005  53  LEU   A CD2 
1205 N  N   A ASN   A 54  ? 0.1219 0.1314 0.1186 0.0022  -0.0014 0.0043  54  ASN   A N   
1206 N  N   B ASN   A 54  ? 0.1137 0.1400 0.1207 -0.0015 0.0096  0.0024  54  ASN   A N   
1207 C  CA  A ASN   A 54  ? 0.1139 0.1184 0.1324 0.0013  -0.0100 -0.0014 54  ASN   A CA  
1208 C  CA  B ASN   A 54  ? 0.1136 0.1368 0.1306 -0.0023 0.0035  0.0013  54  ASN   A CA  
1209 C  C   A ASN   A 54  ? 0.1229 0.1288 0.1357 -0.0083 -0.0011 -0.0023 54  ASN   A C   
1210 C  C   B ASN   A 54  ? 0.1206 0.1353 0.1355 -0.0053 -0.0005 0.0008  54  ASN   A C   
1211 O  O   A ASN   A 54  ? 0.1228 0.1379 0.1338 -0.0089 -0.0008 -0.0138 54  ASN   A O   
1212 O  O   B ASN   A 54  ? 0.1212 0.1374 0.1391 -0.0050 -0.0071 0.0037  54  ASN   A O   
1213 C  CB  A ASN   A 54  ? 0.1117 0.1166 0.1459 -0.0035 -0.0129 -0.0043 54  ASN   A CB  
1214 C  CB  B ASN   A 54  ? 0.1171 0.1420 0.1425 0.0015  0.0049  0.0060  54  ASN   A CB  
1215 C  CG  A ASN   A 54  ? 0.1124 0.1206 0.1305 -0.0033 -0.0050 -0.0054 54  ASN   A CG  
1216 C  CG  B ASN   A 54  ? 0.1195 0.1480 0.1472 0.0053  0.0091  0.0092  54  ASN   A CG  
1217 O  OD1 A ASN   A 54  ? 0.1128 0.1241 0.1222 -0.0025 -0.0041 0.0002  54  ASN   A OD1 
1218 O  OD1 B ASN   A 54  ? 0.1203 0.1589 0.1642 0.0008  0.0072  0.0158  54  ASN   A OD1 
1219 N  ND2 A ASN   A 54  ? 0.1176 0.1278 0.1468 -0.0060 -0.0205 0.0050  54  ASN   A ND2 
1220 N  ND2 B ASN   A 54  ? 0.1250 0.1467 0.1448 0.0127  0.0050  0.0088  54  ASN   A ND2 
1233 N  N   . LYS   A 55  ? 0.1244 0.1330 0.1434 -0.0021 -0.0051 -0.0114 55  LYS   A N   
1234 C  CA  . LYS   A 55  ? 0.1303 0.1419 0.1510 -0.0001 -0.0052 -0.0153 55  LYS   A CA  
1235 C  C   . LYS   A 55  ? 0.1296 0.1533 0.1484 -0.0034 -0.0014 -0.0189 55  LYS   A C   
1236 O  O   . LYS   A 55  ? 0.1383 0.1631 0.1543 0.0004  -0.0034 -0.0267 55  LYS   A O   
1237 C  CB  . LYS   A 55  ? 0.1368 0.1511 0.1588 0.0077  -0.0018 -0.0226 55  LYS   A CB  
1238 C  CG  . LYS   A 55  ? 0.1469 0.1760 0.1711 0.0176  -0.0127 -0.0263 55  LYS   A CG  
1239 C  CD  . LYS   A 55  ? 0.1596 0.2013 0.1944 0.0318  -0.0065 -0.0221 55  LYS   A CD  
1240 C  CE  . LYS   A 55  ? 0.1755 0.2265 0.2121 0.0406  -0.0246 -0.0247 55  LYS   A CE  
1241 N  NZ  . LYS   A 55  ? 0.1825 0.2417 0.2298 0.0439  -0.0246 -0.0165 55  LYS   A NZ  
1256 N  N   . ALA   A 56  ? 0.1314 0.1582 0.1543 -0.0085 0.0098  -0.0173 56  ALA   A N   
1257 C  CA  . ALA   A 56  ? 0.1484 0.1708 0.1527 -0.0096 0.0125  -0.0208 56  ALA   A CA  
1258 C  C   . ALA   A 56  ? 0.1514 0.1780 0.1233 -0.0081 0.0114  -0.0345 56  ALA   A C   
1259 O  O   . ALA   A 56  ? 0.1565 0.2131 0.1429 0.0057  0.0059  -0.0257 56  ALA   A O   
1260 C  CB  . ALA   A 56  ? 0.1579 0.1843 0.1587 -0.0148 0.0158  0.0013  56  ALA   A CB  
1266 N  N   . THR   A 57  ? 0.1404 0.1562 0.1325 -0.0050 0.0086  -0.0210 57  THR   A N   
1267 C  CA  . THR   A 57  ? 0.1408 0.1513 0.1417 -0.0094 -0.0025 -0.0134 57  THR   A CA  
1268 C  C   . THR   A 57  ? 0.1390 0.1597 0.1524 -0.0010 -0.0070 -0.0260 57  THR   A C   
1269 O  O   . THR   A 57  ? 0.1383 0.1656 0.1666 -0.0057 -0.0113 -0.0305 57  THR   A O   
1270 C  CB  . THR   A 57  ? 0.1411 0.1549 0.1412 -0.0075 -0.0017 -0.0218 57  THR   A CB  
1271 O  OG1 . THR   A 57  ? 0.1293 0.1557 0.1383 -0.0054 0.0026  -0.0108 57  THR   A OG1 
1272 C  CG2 . THR   A 57  ? 0.1462 0.1582 0.1294 -0.0092 -0.0037 -0.0059 57  THR   A CG2 
1280 N  N   . ASN   A 58  ? 0.1366 0.1598 0.1627 -0.0039 0.0081  -0.0318 58  ASN   A N   
1281 C  CA  . ASN   A 58  ? 0.1597 0.1529 0.1840 -0.0112 0.0056  -0.0380 58  ASN   A CA  
1282 C  C   . ASN   A 58  ? 0.1429 0.1383 0.1709 0.0009  -0.0024 -0.0220 58  ASN   A C   
1283 O  O   . ASN   A 58  ? 0.1441 0.1507 0.1876 -0.0117 0.0035  -0.0229 58  ASN   A O   
1284 C  CB  . ASN   A 58  ? 0.2005 0.1739 0.2187 -0.0207 0.0257  -0.0461 58  ASN   A CB  
1285 C  CG  . ASN   A 58  ? 0.2405 0.2003 0.2796 -0.0111 0.0358  -0.0361 58  ASN   A CG  
1286 O  OD1 . ASN   A 58  ? 0.2665 0.1969 0.3156 0.0213  0.0565  -0.0431 58  ASN   A OD1 
1287 N  ND2 . ASN   A 58  ? 0.2524 0.2079 0.2996 -0.0123 0.0269  -0.0376 58  ASN   A ND2 
1294 N  N   . ASN   A 59  ? 0.1236 0.1319 0.1616 -0.0064 -0.0093 -0.0130 59  ASN   A N   
1295 C  CA  . ASN   A 59  ? 0.1292 0.1259 0.1633 -0.0031 -0.0052 -0.0022 59  ASN   A CA  
1296 C  C   . ASN   A 59  ? 0.1285 0.1226 0.1643 -0.0038 -0.0088 0.0010  59  ASN   A C   
1297 O  O   . ASN   A 59  ? 0.1298 0.1319 0.1624 -0.0045 -0.0018 0.0029  59  ASN   A O   
1298 C  CB  . ASN   A 59  ? 0.1288 0.1236 0.1569 0.0027  -0.0098 -0.0134 59  ASN   A CB  
1299 C  CG  . ASN   A 59  ? 0.1343 0.1327 0.1575 0.0018  -0.0256 -0.0015 59  ASN   A CG  
1300 O  OD1 . ASN   A 59  ? 0.1465 0.1361 0.1583 -0.0105 -0.0302 0.0012  59  ASN   A OD1 
1301 N  ND2 . ASN   A 59  ? 0.1414 0.1343 0.1702 -0.0103 -0.0193 0.0074  59  ASN   A ND2 
1308 N  N   . ALA   A 60  ? 0.1206 0.1327 0.1544 0.0010  -0.0099 -0.0024 60  ALA   A N   
1309 C  CA  . ALA   A 60  ? 0.1239 0.1352 0.1569 0.0010  -0.0141 -0.0071 60  ALA   A CA  
1310 C  C   . ALA   A 60  ? 0.1231 0.1297 0.1633 -0.0015 -0.0031 -0.0043 60  ALA   A C   
1311 O  O   . ALA   A 60  ? 0.1211 0.1309 0.1732 -0.0005 -0.0099 -0.0065 60  ALA   A O   
1312 C  CB  . ALA   A 60  ? 0.1391 0.1464 0.1537 -0.0041 -0.0210 -0.0204 60  ALA   A CB  
1318 N  N   . MET   A 61  ? 0.1202 0.1296 0.1418 -0.0031 0.0034  -0.0041 61  MET   A N   
1319 C  CA  . MET   A 61  ? 0.1251 0.1201 0.1359 -0.0024 0.0021  0.0012  61  MET   A CA  
1320 C  C   . MET   A 61  ? 0.1240 0.1194 0.1478 -0.0039 -0.0026 -0.0108 61  MET   A C   
1321 O  O   . MET   A 61  ? 0.1260 0.1202 0.1399 -0.0028 0.0055  0.0001  61  MET   A O   
1322 C  CB  . MET   A 61  ? 0.1281 0.1220 0.1310 -0.0045 0.0040  0.0026  61  MET   A CB  
1323 C  CG  . MET   A 61  ? 0.1272 0.1318 0.1494 0.0031  0.0032  0.0016  61  MET   A CG  
1324 S  SD  . MET   A 61  ? 0.1281 0.1312 0.1899 -0.0085 0.0005  -0.0185 61  MET   A SD  
1325 C  CE  . MET   A 61  ? 0.1493 0.1479 0.2021 -0.0145 0.0162  -0.0205 61  MET   A CE  
1335 N  N   . GLN   A 62  ? 0.1239 0.1224 0.1398 -0.0053 0.0022  -0.0032 62  GLN   A N   
1336 C  CA  . GLN   A 62  ? 0.1290 0.1153 0.1562 -0.0046 0.0035  -0.0021 62  GLN   A CA  
1337 C  C   . GLN   A 62  ? 0.1231 0.1091 0.1708 -0.0023 0.0043  0.0058  62  GLN   A C   
1338 O  O   . GLN   A 62  ? 0.1240 0.1251 0.1631 -0.0010 0.0110  0.0026  62  GLN   A O   
1339 C  CB  . GLN   A 62  ? 0.1223 0.1140 0.1590 -0.0026 0.0020  -0.0038 62  GLN   A CB  
1340 C  CG  . GLN   A 62  ? 0.1295 0.1128 0.1594 -0.0010 0.0012  0.0141  62  GLN   A CG  
1341 C  CD  . GLN   A 62  ? 0.1384 0.1168 0.1589 0.0001  0.0089  0.0075  62  GLN   A CD  
1342 O  OE1 . GLN   A 62  ? 0.1381 0.1318 0.1597 -0.0025 0.0035  0.0037  62  GLN   A OE1 
1343 N  NE2 . GLN   A 62  ? 0.1423 0.1255 0.1630 0.0003  0.0044  -0.0058 62  GLN   A NE2 
1352 N  N   . VAL   A 63  ? 0.1231 0.1188 0.1737 -0.0042 0.0105  -0.0163 63  VAL   A N   
1353 C  CA  . VAL   A 63  ? 0.1244 0.1280 0.1934 -0.0154 -0.0009 -0.0148 63  VAL   A CA  
1354 C  C   . VAL   A 63  ? 0.1129 0.1225 0.1877 -0.0132 -0.0104 -0.0153 63  VAL   A C   
1355 O  O   . VAL   A 63  ? 0.1146 0.1287 0.1955 -0.0159 0.0012  -0.0065 63  VAL   A O   
1356 C  CB  . VAL   A 63  ? 0.1367 0.1475 0.2193 -0.0114 -0.0035 -0.0380 63  VAL   A CB  
1357 C  CG1 . VAL   A 63  ? 0.1521 0.1698 0.2522 -0.0110 -0.0103 -0.0545 63  VAL   A CG1 
1358 C  CG2 . VAL   A 63  ? 0.1534 0.1350 0.2379 -0.0149 0.0161  -0.0392 63  VAL   A CG2 
1368 N  N   . GLU   A 64  ? 0.1190 0.1298 0.1728 -0.0042 -0.0033 -0.0101 64  GLU   A N   
1369 C  CA  . GLU   A 64  ? 0.1186 0.1241 0.1668 -0.0078 -0.0064 -0.0030 64  GLU   A CA  
1370 C  C   . GLU   A 64  ? 0.1162 0.1264 0.1697 -0.0090 0.0014  -0.0015 64  GLU   A C   
1371 O  O   . GLU   A 64  ? 0.1256 0.1339 0.1656 -0.0034 0.0007  -0.0059 64  GLU   A O   
1372 C  CB  . GLU   A 64  ? 0.1273 0.1383 0.1692 -0.0044 0.0002  -0.0104 64  GLU   A CB  
1373 C  CG  . GLU   A 64  ? 0.1377 0.1415 0.1749 -0.0151 0.0027  0.0015  64  GLU   A CG  
1374 C  CD  . GLU   A 64  ? 0.1468 0.1486 0.1826 -0.0190 0.0100  0.0011  64  GLU   A CD  
1375 O  OE1 . GLU   A 64  ? 0.1439 0.1589 0.1961 -0.0240 0.0181  -0.0018 64  GLU   A OE1 
1376 O  OE2 . GLU   A 64  ? 0.1621 0.1477 0.1842 -0.0221 -0.0016 0.0066  64  GLU   A OE2 
1383 N  N   . SER   A 65  ? 0.1150 0.1297 0.1511 0.0005  0.0024  0.0004  65  SER   A N   
1384 C  CA  . SER   A 65  ? 0.1200 0.1217 0.1455 -0.0009 0.0032  -0.0083 65  SER   A CA  
1385 C  C   . SER   A 65  ? 0.1206 0.1312 0.1555 0.0005  0.0029  -0.0061 65  SER   A C   
1386 O  O   . SER   A 65  ? 0.1317 0.1333 0.1660 0.0028  0.0136  -0.0025 65  SER   A O   
1387 C  CB  . SER   A 65  ? 0.1204 0.1181 0.1602 -0.0074 0.0111  0.0040  65  SER   A CB  
1388 O  OG  . SER   A 65  ? 0.1203 0.1325 0.1576 -0.0076 -0.0046 0.0059  65  SER   A OG  
1394 N  N   . ASP   A 66  ? 0.1187 0.1218 0.1629 -0.0041 0.0123  0.0031  66  ASP   A N   
1395 C  CA  . ASP   A 66  ? 0.1343 0.1279 0.1714 0.0001  0.0047  0.0094  66  ASP   A CA  
1396 C  C   . ASP   A 66  ? 0.1264 0.1295 0.1883 -0.0037 0.0099  0.0181  66  ASP   A C   
1397 O  O   . ASP   A 66  ? 0.1341 0.1417 0.2064 0.0005  0.0287  0.0250  66  ASP   A O   
1398 C  CB  . ASP   A 66  ? 0.1407 0.1478 0.2140 -0.0004 0.0092  0.0233  66  ASP   A CB  
1399 C  CG  . ASP   A 66  ? 0.1638 0.1536 0.2392 0.0048  -0.0020 0.0444  66  ASP   A CG  
1400 O  OD1 . ASP   A 66  ? 0.1580 0.1810 0.2087 -0.0010 0.0016  0.0462  66  ASP   A OD1 
1401 O  OD2 . ASP   A 66  ? 0.1789 0.1670 0.3157 0.0200  -0.0182 0.0241  66  ASP   A OD2 
1406 N  N   . ASP   A 67  ? 0.1223 0.1334 0.1966 0.0011  0.0048  0.0193  67  ASP   A N   
1407 C  CA  . ASP   A 67  ? 0.1263 0.1503 0.2098 0.0026  0.0005  0.0247  67  ASP   A CA  
1408 C  C   . ASP   A 67  ? 0.1257 0.1510 0.2094 0.0052  0.0095  0.0285  67  ASP   A C   
1409 O  O   . ASP   A 67  ? 0.1270 0.1601 0.2257 0.0060  0.0274  0.0358  67  ASP   A O   
1410 C  CB  . ASP   A 67  ? 0.1316 0.1574 0.2386 0.0005  -0.0222 0.0249  67  ASP   A CB  
1411 C  CG  . ASP   A 67  ? 0.1268 0.1687 0.2729 0.0005  -0.0325 0.0198  67  ASP   A CG  
1412 O  OD1 . ASP   A 67  ? 0.1323 0.1918 0.3562 -0.0077 -0.0352 0.0342  67  ASP   A OD1 
1413 O  OD2 . ASP   A 67  ? 0.1283 0.1735 0.2608 0.0081  -0.0171 0.0200  67  ASP   A OD2 
1418 N  N   . TYR   A 68  ? 0.1255 0.1351 0.1829 0.0018  0.0164  0.0249  68  TYR   A N   
1419 C  CA  . TYR   A 68  ? 0.1413 0.1348 0.1844 -0.0007 0.0196  0.0222  68  TYR   A CA  
1420 C  C   . TYR   A 68  ? 0.1305 0.1359 0.1821 -0.0032 0.0236  0.0198  68  TYR   A C   
1421 O  O   . TYR   A 68  ? 0.1403 0.1398 0.1982 0.0112  0.0312  0.0200  68  TYR   A O   
1422 C  CB  . TYR   A 68  ? 0.1454 0.1286 0.2086 0.0045  0.0369  0.0265  68  TYR   A CB  
1423 C  CG  . TYR   A 68  ? 0.1477 0.1494 0.2264 0.0062  0.0506  0.0331  68  TYR   A CG  
1424 C  CD1 . TYR   A 68  ? 0.1579 0.1593 0.2569 -0.0123 0.0420  0.0034  68  TYR   A CD1 
1425 C  CD2 . TYR   A 68  ? 0.1673 0.1528 0.2583 0.0119  0.0536  0.0328  68  TYR   A CD2 
1426 C  CE1 . TYR   A 68  ? 0.1695 0.1667 0.2926 -0.0098 0.0466  -0.0041 68  TYR   A CE1 
1427 C  CE2 . TYR   A 68  ? 0.1661 0.1562 0.2763 0.0082  0.0677  0.0135  68  TYR   A CE2 
1428 C  CZ  . TYR   A 68  ? 0.1700 0.1574 0.2905 -0.0121 0.0628  -0.0045 68  TYR   A CZ  
1429 O  OH  . TYR   A 68  ? 0.1987 0.1530 0.3097 -0.0036 0.0276  -0.0268 68  TYR   A OH  
1439 N  N   . ILE   A 69  ? 0.1258 0.1294 0.1885 0.0027  0.0272  0.0253  69  ILE   A N   
1440 C  CA  . ILE   A 69  ? 0.1342 0.1311 0.1878 0.0051  0.0241  0.0132  69  ILE   A CA  
1441 C  C   . ILE   A 69  ? 0.1410 0.1351 0.1702 0.0029  0.0267  0.0223  69  ILE   A C   
1442 O  O   . ILE   A 69  ? 0.1447 0.1471 0.1688 -0.0023 0.0248  0.0216  69  ILE   A O   
1443 C  CB  . ILE   A 69  ? 0.1438 0.1568 0.1941 0.0045  0.0143  -0.0017 69  ILE   A CB  
1444 C  CG1 . ILE   A 69  ? 0.1369 0.1659 0.2027 0.0054  0.0164  -0.0121 69  ILE   A CG1 
1445 C  CG2 . ILE   A 69  ? 0.1605 0.1769 0.2070 0.0088  0.0032  -0.0058 69  ILE   A CG2 
1446 C  CD1 . ILE   A 69  ? 0.1412 0.1788 0.2060 -0.0028 0.0120  -0.0236 69  ILE   A CD1 
1458 N  N   . ALA   A 70  ? 0.1462 0.1402 0.1765 -0.0038 0.0289  0.0200  70  ALA   A N   
1459 C  CA  . ALA   A 70  ? 0.1480 0.1503 0.2001 -0.0116 0.0297  0.0276  70  ALA   A CA  
1460 C  C   . ALA   A 70  ? 0.1473 0.1633 0.1855 -0.0068 0.0306  0.0267  70  ALA   A C   
1461 O  O   . ALA   A 70  ? 0.1621 0.1898 0.2105 0.0078  0.0476  0.0397  70  ALA   A O   
1462 C  CB  . ALA   A 70  ? 0.1447 0.1431 0.2262 -0.0147 0.0228  0.0247  70  ALA   A CB  
1468 N  N   . THR   A 71  ? 0.1416 0.1593 0.1808 -0.0004 0.0233  0.0223  71  THR   A N   
1469 C  CA  . THR   A 71  ? 0.1485 0.1760 0.2124 0.0142  0.0314  0.0177  71  THR   A CA  
1470 C  C   . THR   A 71  ? 0.1388 0.1698 0.2309 0.0185  0.0377  0.0194  71  THR   A C   
1471 O  O   . THR   A 71  ? 0.1494 0.1940 0.2756 0.0158  0.0487  -0.0041 71  THR   A O   
1472 C  CB  . THR   A 71  ? 0.1731 0.1976 0.2318 0.0188  -0.0039 0.0247  71  THR   A CB  
1473 O  OG1 . THR   A 71  ? 0.1949 0.2181 0.2329 0.0107  -0.0263 0.0184  71  THR   A OG1 
1474 C  CG2 . THR   A 71  ? 0.1857 0.2126 0.2552 0.0266  -0.0134 0.0427  71  THR   A CG2 
1482 N  N   . ASN   A 72  ? 0.1414 0.1522 0.2133 0.0140  0.0311  0.0215  72  ASN   A N   
1483 C  CA  . ASN   A 72  ? 0.1493 0.1525 0.2185 0.0184  0.0427  0.0175  72  ASN   A CA  
1484 C  C   . ASN   A 72  ? 0.1598 0.1535 0.2053 0.0133  0.0501  0.0110  72  ASN   A C   
1485 O  O   . ASN   A 72  ? 0.1758 0.1536 0.2327 0.0172  0.0471  -0.0017 72  ASN   A O   
1486 C  CB  . ASN   A 72  ? 0.1691 0.1594 0.2236 0.0183  0.0420  0.0217  72  ASN   A CB  
1487 C  CG  . ASN   A 72  ? 0.1933 0.1744 0.2224 0.0280  0.0349  0.0257  72  ASN   A CG  
1488 O  OD1 . ASN   A 72  ? 0.2104 0.2053 0.2378 0.0288  0.0402  0.0250  72  ASN   A OD1 
1489 N  ND2 . ASN   A 72  ? 0.2046 0.1761 0.2218 0.0516  0.0140  0.0107  72  ASN   A ND2 
1496 N  N   . GLY   A 73  ? 0.1620 0.1490 0.1968 0.0054  0.0481  0.0024  73  GLY   A N   
1497 C  CA  . GLY   A 73  ? 0.1671 0.1443 0.1779 -0.0073 0.0436  0.0047  73  GLY   A CA  
1498 C  C   . GLY   A 73  ? 0.1641 0.1359 0.1685 -0.0021 0.0473  0.0172  73  GLY   A C   
1499 O  O   . GLY   A 73  ? 0.1595 0.1448 0.1904 0.0089  0.0386  0.0210  73  GLY   A O   
1503 N  N   . PRO   A 74  ? 0.1725 0.1368 0.1736 -0.0102 0.0448  0.0093  74  PRO   A N   
1504 C  CA  . PRO   A 74  ? 0.1703 0.1353 0.1699 -0.0016 0.0436  0.0109  74  PRO   A CA  
1505 C  C   . PRO   A 74  ? 0.1681 0.1271 0.1737 -0.0026 0.0294  0.0022  74  PRO   A C   
1506 O  O   . PRO   A 74  ? 0.1772 0.1303 0.2004 0.0025  0.0328  -0.0059 74  PRO   A O   
1507 C  CB  . PRO   A 74  ? 0.1845 0.1613 0.1980 0.0034  0.0435  0.0223  74  PRO   A CB  
1508 C  CG  . PRO   A 74  ? 0.2087 0.1951 0.2430 -0.0141 0.0332  0.0140  74  PRO   A CG  
1509 C  CD  . PRO   A 74  ? 0.1915 0.1735 0.1935 -0.0141 0.0397  0.0116  74  PRO   A CD  
1517 N  N   . LEU   A 75  ? 0.1609 0.1194 0.1637 0.0024  0.0276  0.0034  75  LEU   A N   
1518 C  CA  . LEU   A 75  ? 0.1661 0.1228 0.1398 -0.0020 0.0117  0.0064  75  LEU   A CA  
1519 C  C   . LEU   A 75  ? 0.1787 0.1324 0.1465 0.0031  0.0136  0.0132  75  LEU   A C   
1520 O  O   . LEU   A 75  ? 0.2175 0.1487 0.1420 0.0121  0.0123  0.0058  75  LEU   A O   
1521 C  CB  . LEU   A 75  ? 0.1679 0.1299 0.1421 -0.0109 0.0015  0.0206  75  LEU   A CB  
1522 C  CG  . LEU   A 75  ? 0.1867 0.1609 0.1543 -0.0412 0.0018  0.0228  75  LEU   A CG  
1523 C  CD1 . LEU   A 75  ? 0.1990 0.2035 0.1714 -0.0370 -0.0057 0.0106  75  LEU   A CD1 
1524 C  CD2 . LEU   A 75  ? 0.2204 0.2032 0.2095 -0.0156 -0.0002 0.0263  75  LEU   A CD2 
1536 N  N   . LYS   A 76  ? 0.1710 0.1299 0.1636 -0.0096 0.0140  -0.0015 76  LYS   A N   
1537 C  CA  . LYS   A 76  ? 0.1656 0.1499 0.1719 -0.0076 0.0146  -0.0150 76  LYS   A CA  
1538 C  C   . LYS   A 76  ? 0.1575 0.1350 0.1476 -0.0029 0.0151  -0.0043 76  LYS   A C   
1539 O  O   . LYS   A 76  ? 0.1543 0.1299 0.1428 0.0003  0.0122  0.0057  76  LYS   A O   
1540 C  CB  . LYS   A 76  ? 0.1704 0.1761 0.2094 0.0032  0.0158  -0.0386 76  LYS   A CB  
1541 C  CG  . LYS   A 76  ? 0.1787 0.1671 0.2593 0.0075  0.0210  -0.0313 76  LYS   A CG  
1542 C  CD  . LYS   A 76  ? 0.1819 0.1632 0.2982 0.0074  0.0178  -0.0358 76  LYS   A CD  
1543 C  CE  . LYS   A 76  ? 0.1995 0.1869 0.3558 -0.0014 0.0242  -0.0379 76  LYS   A CE  
1544 N  NZ  . LYS   A 76  ? 0.2014 0.1868 0.4025 -0.0206 0.0163  -0.0480 76  LYS   A NZ  
1558 N  N   . VAL   A 77  ? 0.1688 0.1405 0.1477 -0.0014 0.0195  0.0122  77  VAL   A N   
1559 C  CA  . VAL   A 77  ? 0.1675 0.1384 0.1380 0.0125  0.0144  0.0171  77  VAL   A CA  
1560 C  C   . VAL   A 77  ? 0.1604 0.1389 0.1332 0.0158  0.0123  0.0056  77  VAL   A C   
1561 O  O   . VAL   A 77  ? 0.1649 0.1391 0.1320 0.0145  0.0194  -0.0025 77  VAL   A O   
1562 C  CB  . VAL   A 77  ? 0.1908 0.1583 0.1533 0.0085  0.0146  0.0223  77  VAL   A CB  
1563 C  CG1 . VAL   A 77  ? 0.1864 0.1737 0.1711 0.0182  0.0024  0.0084  77  VAL   A CG1 
1564 C  CG2 . VAL   A 77  ? 0.2201 0.1616 0.1734 0.0060  0.0070  0.0295  77  VAL   A CG2 
1574 N  N   . GLY   A 78  ? 0.1602 0.1333 0.1292 0.0113  0.0184  0.0042  78  GLY   A N   
1575 C  CA  . GLY   A 78  ? 0.1502 0.1269 0.1460 0.0082  0.0226  0.0119  78  GLY   A CA  
1576 C  C   . GLY   A 78  ? 0.1423 0.1229 0.1402 0.0091  0.0186  0.0044  78  GLY   A C   
1577 O  O   . GLY   A 78  ? 0.1481 0.1280 0.1535 0.0075  0.0168  0.0244  78  GLY   A O   
1581 N  N   . GLY   A 79  ? 0.1492 0.1227 0.1341 0.0065  0.0156  0.0088  79  GLY   A N   
1582 C  CA  . GLY   A 79  ? 0.1426 0.1263 0.1538 -0.0004 0.0189  0.0074  79  GLY   A CA  
1583 C  C   . GLY   A 79  ? 0.1291 0.1235 0.1529 -0.0032 0.0119  0.0031  79  GLY   A C   
1584 O  O   . GLY   A 79  ? 0.1377 0.1286 0.1517 0.0223  0.0087  0.0073  79  GLY   A O   
1588 N  N   . SER   A 80  ? 0.1227 0.1302 0.1736 -0.0032 0.0159  0.0020  80  SER   A N   
1589 C  CA  . SER   A 80  ? 0.1268 0.1263 0.1633 0.0015  0.0078  -0.0033 80  SER   A CA  
1590 C  C   . SER   A 80  ? 0.1209 0.1291 0.1524 -0.0050 0.0090  0.0111  80  SER   A C   
1591 O  O   . SER   A 80  ? 0.1240 0.1472 0.1826 0.0076  0.0131  -0.0013 80  SER   A O   
1592 C  CB  . SER   A 80  ? 0.1348 0.1323 0.1752 -0.0073 0.0067  0.0125  80  SER   A CB  
1593 O  OG  . SER   A 80  ? 0.1546 0.1334 0.2216 0.0032  -0.0082 0.0198  80  SER   A OG  
1599 N  N   . CYS   A 81  ? 0.1142 0.1236 0.1464 -0.0014 -0.0006 0.0084  81  CYS   A N   
1600 C  CA  . CYS   A 81  ? 0.1164 0.1350 0.1525 -0.0049 -0.0090 0.0199  81  CYS   A CA  
1601 C  C   . CYS   A 81  ? 0.1165 0.1296 0.1544 -0.0090 -0.0007 0.0239  81  CYS   A C   
1602 O  O   . CYS   A 81  ? 0.1228 0.1590 0.1610 -0.0007 0.0027  0.0321  81  CYS   A O   
1603 C  CB  . CYS   A 81  ? 0.1250 0.1401 0.1736 -0.0097 -0.0052 0.0276  81  CYS   A CB  
1604 S  SG  . CYS   A 81  ? 0.1410 0.1276 0.1751 -0.0123 0.0026  0.0107  81  CYS   A SG  
1610 N  N   . VAL   A 82  ? 0.1179 0.1389 0.1520 -0.0007 -0.0114 0.0143  82  VAL   A N   
1611 C  CA  . VAL   A 82  ? 0.1328 0.1395 0.1549 0.0007  -0.0038 0.0208  82  VAL   A CA  
1612 C  C   . VAL   A 82  ? 0.1305 0.1412 0.1602 -0.0013 -0.0052 0.0232  82  VAL   A C   
1613 O  O   . VAL   A 82  ? 0.1235 0.1537 0.1818 -0.0012 -0.0052 -0.0004 82  VAL   A O   
1614 C  CB  . VAL   A 82  ? 0.1656 0.1531 0.1702 0.0061  0.0022  0.0273  82  VAL   A CB  
1615 C  CG1 . VAL   A 82  ? 0.1876 0.1664 0.2024 0.0129  0.0066  0.0218  82  VAL   A CG1 
1616 C  CG2 . VAL   A 82  ? 0.1826 0.1531 0.1892 0.0026  -0.0005 0.0227  82  VAL   A CG2 
1626 N  N   . LEU   A 83  ? 0.1277 0.1383 0.1554 -0.0094 -0.0059 0.0079  83  LEU   A N   
1627 C  CA  . LEU   A 83  ? 0.1250 0.1448 0.1485 -0.0105 -0.0067 0.0072  83  LEU   A CA  
1628 C  C   . LEU   A 83  ? 0.1348 0.1458 0.1507 -0.0121 -0.0120 0.0134  83  LEU   A C   
1629 O  O   . LEU   A 83  ? 0.1451 0.1488 0.1505 -0.0107 -0.0051 0.0157  83  LEU   A O   
1630 C  CB  . LEU   A 83  ? 0.1362 0.1486 0.1399 -0.0122 -0.0120 0.0175  83  LEU   A CB  
1631 C  CG  . LEU   A 83  ? 0.1516 0.1609 0.1585 -0.0108 0.0084  0.0140  83  LEU   A CG  
1632 C  CD1 . LEU   A 83  ? 0.1612 0.1605 0.1662 -0.0227 0.0010  0.0240  83  LEU   A CD1 
1633 C  CD2 . LEU   A 83  ? 0.1490 0.1707 0.1691 -0.0053 0.0145  0.0161  83  LEU   A CD2 
1645 N  N   . SER   A 84  ? 0.1480 0.1492 0.1468 -0.0137 -0.0135 0.0156  84  SER   A N   
1646 C  CA  . SER   A 84  ? 0.1591 0.1508 0.1348 -0.0101 -0.0106 0.0104  84  SER   A CA  
1647 C  C   . SER   A 84  ? 0.1617 0.1464 0.1327 -0.0117 -0.0044 0.0150  84  SER   A C   
1648 O  O   . SER   A 84  ? 0.1553 0.1622 0.1271 -0.0087 -0.0054 0.0077  84  SER   A O   
1649 C  CB  . SER   A 84  ? 0.1647 0.1684 0.1363 -0.0072 -0.0137 0.0004  84  SER   A CB  
1650 O  OG  . SER   A 84  ? 0.1724 0.1955 0.1434 -0.0085 -0.0194 -0.0126 84  SER   A OG  
1656 N  N   . GLY   A 85  ? 0.1752 0.1630 0.1339 -0.0189 0.0029  0.0109  85  GLY   A N   
1657 C  CA  . GLY   A 85  ? 0.1797 0.1704 0.1560 -0.0263 0.0126  -0.0036 85  GLY   A CA  
1658 C  C   . GLY   A 85  ? 0.1713 0.1808 0.1276 -0.0159 -0.0032 -0.0014 85  GLY   A C   
1659 O  O   . GLY   A 85  ? 0.1678 0.1943 0.1384 -0.0269 0.0105  -0.0086 85  GLY   A O   
1663 N  N   . HIS   A 86  ? 0.1703 0.1712 0.1307 -0.0178 -0.0047 0.0011  86  HIS   A N   
1664 C  CA  . HIS   A 86  ? 0.1863 0.1778 0.1255 -0.0195 -0.0041 -0.0015 86  HIS   A CA  
1665 C  C   . HIS   A 86  ? 0.2043 0.1839 0.1286 -0.0228 -0.0047 -0.0001 86  HIS   A C   
1666 O  O   . HIS   A 86  ? 0.2130 0.2051 0.1385 -0.0179 0.0059  0.0099  86  HIS   A O   
1667 C  CB  . HIS   A 86  ? 0.1839 0.1663 0.1396 -0.0151 0.0081  0.0011  86  HIS   A CB  
1668 C  CG  . HIS   A 86  ? 0.1764 0.1657 0.1456 -0.0068 0.0015  0.0026  86  HIS   A CG  
1669 N  ND1 . HIS   A 86  ? 0.1781 0.1653 0.1793 -0.0156 0.0013  0.0055  86  HIS   A ND1 
1670 C  CD2 . HIS   A 86  ? 0.1792 0.1558 0.1379 0.0053  -0.0019 0.0090  86  HIS   A CD2 
1671 C  CE1 . HIS   A 86  ? 0.1705 0.1680 0.1656 -0.0131 0.0183  0.0079  86  HIS   A CE1 
1672 N  NE2 . HIS   A 86  ? 0.1715 0.1574 0.1537 0.0032  0.0071  0.0211  86  HIS   A NE2 
1680 N  N   . ASN   A 87  ? 0.2119 0.1954 0.1484 -0.0178 0.0186  -0.0102 87  ASN   A N   
1681 C  CA  . ASN   A 87  ? 0.2280 0.2076 0.1648 -0.0108 0.0502  -0.0084 87  ASN   A CA  
1682 C  C   . ASN   A 87  ? 0.2307 0.2234 0.1802 -0.0164 0.0699  0.0026  87  ASN   A C   
1683 O  O   . ASN   A 87  ? 0.2555 0.2426 0.2263 -0.0296 0.0941  -0.0051 87  ASN   A O   
1684 C  CB  . ASN   A 87  ? 0.2437 0.2146 0.1724 0.0023  0.0442  -0.0124 87  ASN   A CB  
1685 C  CG  . ASN   A 87  ? 0.2501 0.2211 0.1707 0.0117  0.0507  -0.0007 87  ASN   A CG  
1686 O  OD1 . ASN   A 87  ? 0.2633 0.2206 0.1735 0.0287  0.0434  0.0078  87  ASN   A OD1 
1687 N  ND2 . ASN   A 87  ? 0.2558 0.2439 0.1746 0.0128  0.0488  0.0072  87  ASN   A ND2 
1694 N  N   . LEU   A 88  ? 0.2051 0.2187 0.1778 -0.0230 0.0386  0.0097  88  LEU   A N   
1695 C  CA  . LEU   A 88  ? 0.1888 0.2203 0.1936 -0.0263 0.0271  0.0223  88  LEU   A CA  
1696 C  C   . LEU   A 88  ? 0.1851 0.2164 0.1850 -0.0334 0.0209  0.0308  88  LEU   A C   
1697 O  O   . LEU   A 88  ? 0.1895 0.2255 0.2146 -0.0340 0.0223  0.0480  88  LEU   A O   
1698 C  CB  . LEU   A 88  ? 0.1940 0.2308 0.2091 -0.0318 0.0012  0.0349  88  LEU   A CB  
1699 C  CG  . LEU   A 88  ? 0.2149 0.2436 0.2467 -0.0344 -0.0142 0.0323  88  LEU   A CG  
1700 C  CD1 . LEU   A 88  ? 0.2282 0.2500 0.2470 -0.0327 -0.0142 0.0215  88  LEU   A CD1 
1701 C  CD2 . LEU   A 88  ? 0.2278 0.2533 0.2853 -0.0314 -0.0160 0.0186  88  LEU   A CD2 
1713 N  N   . ALA   A 89  ? 0.1891 0.2038 0.1575 -0.0320 0.0170  0.0108  89  ALA   A N   
1714 C  CA  . ALA   A 89  ? 0.2078 0.1999 0.1468 -0.0268 0.0063  0.0193  89  ALA   A CA  
1715 C  C   . ALA   A 89  ? 0.2120 0.2014 0.1508 -0.0174 -0.0056 0.0118  89  ALA   A C   
1716 O  O   . ALA   A 89  ? 0.2083 0.1985 0.1705 -0.0227 -0.0107 -0.0095 89  ALA   A O   
1717 C  CB  . ALA   A 89  ? 0.2021 0.1987 0.1412 -0.0287 0.0027  0.0199  89  ALA   A CB  
1723 N  N   . LYS   A 90  ? 0.2172 0.2117 0.1441 -0.0283 -0.0216 0.0172  90  LYS   A N   
1724 C  CA  . LYS   A 90  ? 0.2197 0.2275 0.1517 -0.0255 -0.0303 0.0199  90  LYS   A CA  
1725 C  C   . LYS   A 90  ? 0.1964 0.2108 0.1355 -0.0177 -0.0246 0.0066  90  LYS   A C   
1726 O  O   . LYS   A 90  ? 0.1990 0.2259 0.1646 -0.0227 -0.0268 -0.0020 90  LYS   A O   
1727 C  CB  . LYS   A 90  ? 0.2478 0.2590 0.1904 -0.0195 -0.0367 0.0323  90  LYS   A CB  
1728 C  CG  . LYS   A 90  ? 0.2830 0.2928 0.2736 -0.0174 -0.0381 0.0412  90  LYS   A CG  
1729 C  CD  . LYS   A 90  ? 0.3184 0.3227 0.3655 -0.0170 -0.0284 0.0556  90  LYS   A CD  
1730 C  CE  . LYS   A 90  ? 0.3340 0.3357 0.4342 -0.0166 -0.0175 0.0553  90  LYS   A CE  
1731 N  NZ  . LYS   A 90  ? 0.3413 0.3420 0.4766 -0.0149 -0.0076 0.0471  90  LYS   A NZ  
1745 N  N   . HIS   A 91  ? 0.1887 0.1854 0.1128 -0.0130 -0.0264 0.0080  91  HIS   A N   
1746 C  CA  . HIS   A 91  ? 0.1744 0.1731 0.1314 -0.0144 -0.0333 0.0201  91  HIS   A CA  
1747 C  C   . HIS   A 91  ? 0.1538 0.1612 0.1175 -0.0161 -0.0190 0.0209  91  HIS   A C   
1748 O  O   . HIS   A 91  ? 0.1501 0.1759 0.1344 -0.0201 -0.0107 0.0233  91  HIS   A O   
1749 C  CB  . HIS   A 91  ? 0.1889 0.2029 0.1806 0.0057  -0.0508 0.0201  91  HIS   A CB  
1750 C  CG  . HIS   A 91  ? 0.2282 0.2505 0.2526 0.0165  -0.0783 0.0102  91  HIS   A CG  
1751 N  ND1 . HIS   A 91  ? 0.2353 0.2789 0.2982 0.0208  -0.0839 -0.0085 91  HIS   A ND1 
1752 C  CD2 . HIS   A 91  ? 0.2512 0.2700 0.2840 0.0248  -0.0843 0.0193  91  HIS   A CD2 
1753 C  CE1 . HIS   A 91  ? 0.2463 0.2883 0.3141 0.0252  -0.0858 0.0003  91  HIS   A CE1 
1754 N  NE2 . HIS   A 91  ? 0.2600 0.2861 0.3134 0.0300  -0.0839 0.0079  91  HIS   A NE2 
1762 N  N   . CYS   A 92  ? 0.1441 0.1543 0.1159 -0.0153 -0.0150 0.0159  92  CYS   A N   
1763 C  CA  . CYS   A 92  ? 0.1319 0.1455 0.1330 -0.0118 -0.0022 0.0128  92  CYS   A CA  
1764 C  C   . CYS   A 92  ? 0.1273 0.1401 0.1255 -0.0140 -0.0030 0.0130  92  CYS   A C   
1765 O  O   . CYS   A 92  ? 0.1333 0.1451 0.1396 -0.0187 -0.0028 0.0093  92  CYS   A O   
1766 C  CB  . CYS   A 92  ? 0.1354 0.1451 0.1486 -0.0066 0.0004  0.0122  92  CYS   A CB  
1767 S  SG  . CYS   A 92  ? 0.1380 0.1368 0.1288 -0.0118 -0.0055 0.0084  92  CYS   A SG  
1773 N  N   . LEU   A 93  ? 0.1312 0.1332 0.1273 -0.0096 0.0038  0.0173  93  LEU   A N   
1774 C  CA  . LEU   A 93  ? 0.1201 0.1280 0.1314 -0.0063 -0.0012 0.0148  93  LEU   A CA  
1775 C  C   . LEU   A 93  ? 0.1176 0.1146 0.1321 -0.0017 0.0040  0.0016  93  LEU   A C   
1776 O  O   . LEU   A 93  ? 0.1136 0.1284 0.1219 -0.0027 0.0006  0.0139  93  LEU   A O   
1777 C  CB  . LEU   A 93  ? 0.1281 0.1297 0.1442 -0.0015 -0.0047 0.0248  93  LEU   A CB  
1778 C  CG  . LEU   A 93  ? 0.1329 0.1276 0.1362 -0.0048 -0.0006 0.0228  93  LEU   A CG  
1779 C  CD1 . LEU   A 93  ? 0.1392 0.1298 0.1682 -0.0008 0.0047  0.0166  93  LEU   A CD1 
1780 C  CD2 . LEU   A 93  ? 0.1458 0.1297 0.1633 -0.0073 0.0043  0.0151  93  LEU   A CD2 
1792 N  N   . HIS   A 94  ? 0.1133 0.1123 0.1369 -0.0018 0.0015  0.0148  94  HIS   A N   
1793 C  CA  . HIS   A 94  ? 0.1070 0.1161 0.1326 -0.0041 -0.0021 0.0160  94  HIS   A CA  
1794 C  C   . HIS   A 94  ? 0.1108 0.1162 0.1373 -0.0035 -0.0029 0.0065  94  HIS   A C   
1795 O  O   . HIS   A 94  ? 0.1146 0.1327 0.1673 0.0028  -0.0013 -0.0055 94  HIS   A O   
1796 C  CB  . HIS   A 94  ? 0.1133 0.1176 0.1443 -0.0016 0.0025  0.0106  94  HIS   A CB  
1797 C  CG  . HIS   A 94  ? 0.1165 0.1177 0.1291 0.0014  -0.0035 0.0145  94  HIS   A CG  
1798 N  ND1 . HIS   A 94  ? 0.1185 0.1169 0.1287 -0.0034 0.0012  0.0104  94  HIS   A ND1 
1799 C  CD2 . HIS   A 94  ? 0.1202 0.1268 0.1345 -0.0041 -0.0036 0.0121  94  HIS   A CD2 
1800 C  CE1 . HIS   A 94  ? 0.1205 0.1262 0.1341 -0.0082 -0.0062 0.0019  94  HIS   A CE1 
1801 N  NE2 . HIS   A 94  ? 0.1236 0.1246 0.1419 -0.0118 -0.0111 0.0052  94  HIS   A NE2 
1809 N  N   . VAL   A 95  ? 0.1109 0.1112 0.1103 0.0013  0.0062  0.0045  95  VAL   A N   
1810 C  CA  . VAL   A 95  ? 0.1141 0.1182 0.1161 -0.0028 0.0100  0.0119  95  VAL   A CA  
1811 C  C   . VAL   A 95  ? 0.1180 0.1210 0.1159 -0.0145 0.0070  0.0049  95  VAL   A C   
1812 O  O   . VAL   A 95  ? 0.1265 0.1290 0.1150 0.0069  0.0066  0.0017  95  VAL   A O   
1813 C  CB  . VAL   A 95  ? 0.1161 0.1209 0.1463 -0.0140 0.0020  0.0034  95  VAL   A CB  
1814 C  CG1 . VAL   A 95  ? 0.1347 0.1227 0.1565 -0.0222 0.0009  -0.0029 95  VAL   A CG1 
1815 C  CG2 . VAL   A 95  ? 0.1205 0.1254 0.1474 -0.0132 0.0011  0.0218  95  VAL   A CG2 
1825 N  N   . VAL   A 96  ? 0.1264 0.1163 0.1021 -0.0017 0.0059  0.0108  96  VAL   A N   
1826 C  CA  . VAL   A 96  ? 0.1324 0.1139 0.1253 0.0021  0.0119  0.0155  96  VAL   A CA  
1827 C  C   . VAL   A 96  ? 0.1336 0.1236 0.1436 -0.0018 0.0052  0.0186  96  VAL   A C   
1828 O  O   . VAL   A 96  ? 0.1411 0.1287 0.1498 -0.0018 0.0092  0.0002  96  VAL   A O   
1829 C  CB  . VAL   A 96  ? 0.1403 0.1234 0.1361 0.0002  0.0232  0.0176  96  VAL   A CB  
1830 C  CG1 . VAL   A 96  ? 0.1409 0.1289 0.1329 0.0042  0.0126  0.0138  96  VAL   A CG1 
1831 C  CG2 . VAL   A 96  ? 0.1375 0.1288 0.1545 -0.0109 0.0158  0.0180  96  VAL   A CG2 
1841 N  N   . GLY   A 97  ? 0.1309 0.1244 0.1325 -0.0035 0.0086  0.0132  97  GLY   A N   
1842 C  CA  . GLY   A 97  ? 0.1443 0.1339 0.1354 0.0016  0.0015  0.0160  97  GLY   A CA  
1843 C  C   . GLY   A 97  ? 0.1455 0.1462 0.1108 0.0012  0.0063  0.0103  97  GLY   A C   
1844 O  O   . GLY   A 97  ? 0.1550 0.1494 0.1307 0.0020  0.0037  0.0130  97  GLY   A O   
1848 N  N   A PRO   A 98  ? 0.1482 0.1524 0.1035 0.0052  -0.0022 0.0132  98  PRO   A N   
1849 N  N   B PRO   A 98  ? 0.1562 0.1492 0.1250 0.0019  0.0025  0.0163  98  PRO   A N   
1850 C  CA  A PRO   A 98  ? 0.1584 0.1691 0.1149 0.0051  0.0015  0.0026  98  PRO   A CA  
1851 C  CA  B PRO   A 98  ? 0.1677 0.1535 0.1379 0.0015  -0.0022 0.0132  98  PRO   A CA  
1852 C  C   A PRO   A 98  ? 0.1602 0.1773 0.1013 -0.0057 0.0082  0.0178  98  PRO   A C   
1853 C  C   B PRO   A 98  ? 0.1858 0.1547 0.1405 -0.0039 -0.0051 0.0248  98  PRO   A C   
1854 O  O   A PRO   A 98  ? 0.1549 0.1629 0.1285 -0.0032 0.0062  0.0197  98  PRO   A O   
1855 O  O   B PRO   A 98  ? 0.1838 0.1572 0.1523 -0.0040 -0.0045 0.0203  98  PRO   A O   
1856 C  CB  A PRO   A 98  ? 0.1588 0.1758 0.1217 0.0109  -0.0017 -0.0133 98  PRO   A CB  
1857 C  CB  B PRO   A 98  ? 0.1650 0.1547 0.1351 0.0059  -0.0018 0.0086  98  PRO   A CB  
1858 C  CG  A PRO   A 98  ? 0.1572 0.1651 0.1252 0.0121  -0.0047 -0.0150 98  PRO   A CG  
1859 C  CG  B PRO   A 98  ? 0.1674 0.1552 0.1407 0.0046  -0.0023 0.0120  98  PRO   A CG  
1860 C  CD  A PRO   A 98  ? 0.1540 0.1536 0.1109 0.0099  -0.0016 0.0026  98  PRO   A CD  
1861 C  CD  B PRO   A 98  ? 0.1594 0.1510 0.1325 0.0044  -0.0018 0.0170  98  PRO   A CD  
1876 N  N   A ASN   A 99  ? 0.1609 0.1972 0.1145 0.0014  0.0087  0.0317  99  ASN   A N   
1877 N  N   B ASN   A 99  ? 0.2052 0.1532 0.1351 -0.0025 -0.0092 0.0381  99  ASN   A N   
1878 C  CA  A ASN   A 99  ? 0.1778 0.2122 0.1197 -0.0032 0.0034  0.0401  99  ASN   A CA  
1879 C  CA  B ASN   A 99  ? 0.2275 0.1548 0.1456 0.0019  -0.0156 0.0448  99  ASN   A CA  
1880 C  C   A ASN   A 99  ? 0.1928 0.2425 0.1184 -0.0195 0.0004  0.0465  99  ASN   A C   
1881 C  C   B ASN   A 99  ? 0.2417 0.1585 0.1616 0.0043  -0.0223 0.0356  99  ASN   A C   
1882 O  O   A ASN   A 99  ? 0.2018 0.2610 0.1268 -0.0158 -0.0008 0.0426  99  ASN   A O   
1883 O  O   B ASN   A 99  ? 0.2403 0.1462 0.1719 0.0016  -0.0228 0.0149  99  ASN   A O   
1884 C  CB  A ASN   A 99  ? 0.1778 0.2076 0.1319 -0.0018 -0.0034 0.0432  99  ASN   A CB  
1885 C  CB  B ASN   A 99  ? 0.2357 0.1592 0.1519 0.0039  -0.0173 0.0504  99  ASN   A CB  
1886 C  CG  A ASN   A 99  ? 0.1793 0.2068 0.1498 -0.0028 -0.0050 0.0277  99  ASN   A CG  
1887 C  CG  B ASN   A 99  ? 0.2403 0.1671 0.1599 0.0076  -0.0195 0.0549  99  ASN   A CG  
1888 O  OD1 A ASN   A 99  ? 0.1936 0.2174 0.1544 0.0083  -0.0141 0.0180  99  ASN   A OD1 
1889 O  OD1 B ASN   A 99  ? 0.2466 0.1711 0.1490 0.0051  -0.0217 0.0622  99  ASN   A OD1 
1890 N  ND2 A ASN   A 99  ? 0.1802 0.2097 0.1676 -0.0066 -0.0042 0.0394  99  ASN   A ND2 
1891 N  ND2 B ASN   A 99  ? 0.2395 0.1735 0.1756 0.0160  -0.0200 0.0375  99  ASN   A ND2 
1904 N  N   A VAL   A 100 ? 0.2083 0.2592 0.1215 -0.0378 -0.0241 0.0402  100 VAL   A N   
1905 N  N   B VAL   A 100 ? 0.2566 0.1806 0.1805 0.0050  -0.0342 0.0322  100 VAL   A N   
1906 C  CA  A VAL   A 100 ? 0.2326 0.2782 0.1389 -0.0462 -0.0328 0.0456  100 VAL   A CA  
1907 C  CA  B VAL   A 100 ? 0.2708 0.1983 0.1991 0.0005  -0.0357 0.0360  100 VAL   A CA  
1908 C  C   A VAL   A 100 ? 0.2409 0.2908 0.1556 -0.0534 -0.0368 0.0652  100 VAL   A C   
1909 C  C   B VAL   A 100 ? 0.2853 0.2048 0.1973 -0.0025 -0.0373 0.0414  100 VAL   A C   
1910 O  O   A VAL   A 100 ? 0.2503 0.3031 0.1741 -0.0536 -0.0220 0.0679  100 VAL   A O   
1911 O  O   B VAL   A 100 ? 0.2912 0.2013 0.1890 -0.0100 -0.0304 0.0351  100 VAL   A O   
1912 C  CB  A VAL   A 100 ? 0.2527 0.2862 0.1814 -0.0558 -0.0368 0.0361  100 VAL   A CB  
1913 C  CB  B VAL   A 100 ? 0.2724 0.2104 0.2206 -0.0002 -0.0370 0.0333  100 VAL   A CB  
1914 C  CG1 A VAL   A 100 ? 0.2564 0.2928 0.1997 -0.0599 -0.0343 0.0398  100 VAL   A CG1 
1915 C  CG1 B VAL   A 100 ? 0.2738 0.2107 0.2261 -0.0002 -0.0398 0.0325  100 VAL   A CG1 
1916 C  CG2 A VAL   A 100 ? 0.2660 0.2898 0.1836 -0.0603 -0.0326 0.0278  100 VAL   A CG2 
1917 C  CG2 B VAL   A 100 ? 0.2750 0.2175 0.2318 -0.0017 -0.0353 0.0307  100 VAL   A CG2 
1936 N  N   A ASN   A 101 ? 0.2440 0.2944 0.1794 -0.0556 -0.0458 0.0896  101 ASN   A N   
1937 N  N   B ASN   A 101 ? 0.2919 0.2132 0.2082 0.0019  -0.0433 0.0478  101 ASN   A N   
1938 C  CA  A ASN   A 101 ? 0.2678 0.3083 0.2116 -0.0538 -0.0497 0.1032  101 ASN   A CA  
1939 C  CA  B ASN   A 101 ? 0.2979 0.2178 0.2188 0.0018  -0.0438 0.0489  101 ASN   A CA  
1940 C  C   A ASN   A 101 ? 0.2897 0.3348 0.2239 -0.0601 -0.0243 0.1273  101 ASN   A C   
1941 C  C   B ASN   A 101 ? 0.3082 0.2320 0.2241 -0.0012 -0.0254 0.0530  101 ASN   A C   
1942 O  O   A ASN   A 101 ? 0.3062 0.3399 0.2649 -0.0534 -0.0234 0.1246  101 ASN   A O   
1943 O  O   B ASN   A 101 ? 0.3120 0.2367 0.2203 -0.0009 -0.0170 0.0509  101 ASN   A O   
1944 C  CB  A ASN   A 101 ? 0.2754 0.3028 0.2200 -0.0421 -0.0767 0.0859  101 ASN   A CB  
1945 C  CB  B ASN   A 101 ? 0.2937 0.2065 0.2208 0.0019  -0.0525 0.0474  101 ASN   A CB  
1946 C  CG  A ASN   A 101 ? 0.2784 0.2974 0.2270 -0.0341 -0.0883 0.0620  101 ASN   A CG  
1947 C  CG  B ASN   A 101 ? 0.2881 0.1951 0.2193 0.0003  -0.0540 0.0438  101 ASN   A CG  
1948 O  OD1 A ASN   A 101 ? 0.2810 0.3086 0.2386 -0.0209 -0.0900 0.0361  101 ASN   A OD1 
1949 O  OD1 B ASN   A 101 ? 0.2892 0.1913 0.2177 -0.0057 -0.0453 0.0474  101 ASN   A OD1 
1950 N  ND2 A ASN   A 101 ? 0.2755 0.2823 0.2230 -0.0408 -0.0876 0.0722  101 ASN   A ND2 
1951 N  ND2 B ASN   A 101 ? 0.2835 0.1872 0.2173 0.0013  -0.0547 0.0347  101 ASN   A ND2 
1964 N  N   A LYS   A 102 ? 0.2939 0.3595 0.2389 -0.0730 -0.0047 0.1204  102 LYS   A N   
1965 N  N   B LYS   A 102 ? 0.3153 0.2482 0.2500 -0.0075 -0.0123 0.0448  102 LYS   A N   
1966 C  CA  A LYS   A 102 ? 0.3042 0.3817 0.2376 -0.0796 0.0012  0.1109  102 LYS   A CA  
1967 C  CA  B LYS   A 102 ? 0.3214 0.2615 0.2616 -0.0151 0.0017  0.0428  102 LYS   A CA  
1968 C  C   A LYS   A 102 ? 0.3147 0.3969 0.2182 -0.0707 -0.0044 0.1015  102 LYS   A C   
1969 C  C   B LYS   A 102 ? 0.3187 0.2631 0.2376 -0.0219 0.0058  0.0514  102 LYS   A C   
1970 O  O   A LYS   A 102 ? 0.3209 0.4102 0.2282 -0.0678 -0.0024 0.0927  102 LYS   A O   
1971 O  O   B LYS   A 102 ? 0.3199 0.2593 0.2272 -0.0296 0.0080  0.0631  102 LYS   A O   
1972 C  CB  A LYS   A 102 ? 0.3093 0.3888 0.2678 -0.0887 0.0008  0.0984  102 LYS   A CB  
1973 C  CB  B LYS   A 102 ? 0.3286 0.2735 0.2967 -0.0184 0.0072  0.0266  102 LYS   A CB  
1974 C  CG  A LYS   A 102 ? 0.3157 0.3933 0.2982 -0.0936 -0.0067 0.0782  102 LYS   A CG  
1975 C  CG  B LYS   A 102 ? 0.3331 0.2834 0.3263 -0.0207 0.0103  0.0152  102 LYS   A CG  
1976 C  CD  A LYS   A 102 ? 0.3265 0.3987 0.3303 -0.0949 -0.0134 0.0532  102 LYS   A CD  
1977 C  CD  B LYS   A 102 ? 0.3362 0.2916 0.3543 -0.0222 0.0113  0.0046  102 LYS   A CD  
1978 C  CE  A LYS   A 102 ? 0.3369 0.4029 0.3511 -0.0944 -0.0170 0.0387  102 LYS   A CE  
1979 C  CE  B LYS   A 102 ? 0.3377 0.2977 0.3759 -0.0233 0.0094  -0.0019 102 LYS   A CE  
1980 N  NZ  A LYS   A 102 ? 0.3448 0.4039 0.3633 -0.0970 -0.0137 0.0321  102 LYS   A NZ  
1981 N  NZ  B LYS   A 102 ? 0.3395 0.3018 0.3889 -0.0238 0.0100  -0.0052 102 LYS   A NZ  
2008 N  N   A GLY   A 103 ? 0.3171 0.4015 0.2047 -0.0588 -0.0190 0.0785  103 GLY   A N   
2009 N  N   B GLY   A 103 ? 0.3141 0.2681 0.2273 -0.0216 0.0038  0.0441  103 GLY   A N   
2010 C  CA  A GLY   A 103 ? 0.3223 0.4016 0.1779 -0.0458 -0.0212 0.0654  103 GLY   A CA  
2011 C  CA  B GLY   A 103 ? 0.3089 0.2698 0.2154 -0.0235 0.0056  0.0393  103 GLY   A CA  
2012 C  C   A GLY   A 103 ? 0.3236 0.4012 0.1817 -0.0394 -0.0121 0.0405  103 GLY   A C   
2013 C  C   B GLY   A 103 ? 0.3053 0.2701 0.2069 -0.0238 0.0060  0.0305  103 GLY   A C   
2014 O  O   A GLY   A 103 ? 0.3330 0.4095 0.2041 -0.0369 -0.0106 0.0201  103 GLY   A O   
2015 O  O   B GLY   A 103 ? 0.3037 0.2724 0.2112 -0.0259 0.0075  0.0289  103 GLY   A O   
2022 N  N   A GLU   A 104 ? 0.3104 0.3867 0.1405 -0.0396 -0.0104 0.0329  104 GLU   A N   
2023 N  N   B GLU   A 104 ? 0.3042 0.2676 0.2017 -0.0194 0.0023  0.0217  104 GLU   A N   
2024 C  CA  A GLU   A 104 ? 0.2897 0.3672 0.1245 -0.0463 -0.0053 0.0224  104 GLU   A CA  
2025 C  CA  B GLU   A 104 ? 0.3001 0.2621 0.2006 -0.0160 -0.0003 0.0159  104 GLU   A CA  
2026 C  C   A GLU   A 104 ? 0.2916 0.3760 0.1493 -0.0469 0.0020  0.0009  104 GLU   A C   
2027 C  C   B GLU   A 104 ? 0.2946 0.2575 0.2048 -0.0132 -0.0008 0.0097  104 GLU   A C   
2028 O  O   A GLU   A 104 ? 0.2862 0.3726 0.1931 -0.0492 -0.0015 -0.0095 104 GLU   A O   
2029 O  O   B GLU   A 104 ? 0.2922 0.2511 0.2199 -0.0119 -0.0015 0.0139  104 GLU   A O   
2030 C  CB  A GLU   A 104 ? 0.2641 0.3397 0.1060 -0.0526 0.0096  0.0416  104 GLU   A CB  
2031 C  CB  B GLU   A 104 ? 0.2994 0.2620 0.2001 -0.0143 -0.0003 0.0202  104 GLU   A CB  
2032 C  CG  A GLU   A 104 ? 0.2473 0.3174 0.1248 -0.0490 0.0076  0.0504  104 GLU   A CG  
2033 C  CG  B GLU   A 104 ? 0.2997 0.2638 0.2134 -0.0118 -0.0021 0.0219  104 GLU   A CG  
2034 C  CD  A GLU   A 104 ? 0.2251 0.2934 0.1345 -0.0452 0.0095  0.0579  104 GLU   A CD  
2035 C  CD  B GLU   A 104 ? 0.2993 0.2667 0.2247 -0.0086 -0.0019 0.0208  104 GLU   A CD  
2036 O  OE1 A GLU   A 104 ? 0.2030 0.2784 0.1009 -0.0351 -0.0006 0.0557  104 GLU   A OE1 
2037 O  OE1 B GLU   A 104 ? 0.2996 0.2705 0.2281 -0.0056 -0.0017 0.0205  104 GLU   A OE1 
2038 O  OE2 A GLU   A 104 ? 0.2348 0.2913 0.1604 -0.0497 0.0092  0.0717  104 GLU   A OE2 
2039 O  OE2 B GLU   A 104 ? 0.3002 0.2672 0.2350 -0.0102 -0.0036 0.0209  104 GLU   A OE2 
2052 N  N   A ASP   A 105 ? 0.2983 0.3877 0.1609 -0.0446 0.0177  -0.0149 105 ASP   A N   
2053 N  N   B ASP   A 105 ? 0.2917 0.2606 0.2104 -0.0130 0.0002  -0.0031 105 ASP   A N   
2054 C  CA  A ASP   A 105 ? 0.3045 0.3979 0.1973 -0.0426 0.0226  -0.0365 105 ASP   A CA  
2055 C  CA  B ASP   A 105 ? 0.2886 0.2652 0.2274 -0.0095 0.0023  -0.0172 105 ASP   A CA  
2056 C  C   A ASP   A 105 ? 0.2731 0.3855 0.1721 -0.0505 0.0151  -0.0486 105 ASP   A C   
2057 C  C   B ASP   A 105 ? 0.2805 0.2645 0.2274 -0.0163 0.0040  -0.0139 105 ASP   A C   
2058 O  O   A ASP   A 105 ? 0.2503 0.3774 0.1217 -0.0513 0.0149  -0.0709 105 ASP   A O   
2059 O  O   B ASP   A 105 ? 0.2726 0.2584 0.2181 -0.0167 0.0026  -0.0140 105 ASP   A O   
2060 C  CB  A ASP   A 105 ? 0.3371 0.4177 0.2683 -0.0339 0.0314  -0.0482 105 ASP   A CB  
2061 C  CB  B ASP   A 105 ? 0.2938 0.2708 0.2500 -0.0003 0.0023  -0.0320 105 ASP   A CB  
2062 C  CG  A ASP   A 105 ? 0.3657 0.4338 0.3312 -0.0258 0.0339  -0.0568 105 ASP   A CG  
2063 C  CG  B ASP   A 105 ? 0.2982 0.2739 0.2641 0.0084  0.0012  -0.0452 105 ASP   A CG  
2064 O  OD1 A ASP   A 105 ? 0.3731 0.4415 0.3407 -0.0253 0.0324  -0.0672 105 ASP   A OD1 
2065 O  OD1 B ASP   A 105 ? 0.3012 0.2715 0.2620 0.0112  -0.0026 -0.0520 105 ASP   A OD1 
2066 O  OD2 A ASP   A 105 ? 0.3811 0.4397 0.3743 -0.0231 0.0353  -0.0470 105 ASP   A OD2 
2067 O  OD2 B ASP   A 105 ? 0.2993 0.2794 0.2856 0.0082  -0.0022 -0.0427 105 ASP   A OD2 
2076 N  N   A ILE   A 106 ? 0.2621 0.3754 0.1949 -0.0537 -0.0174 -0.0468 106 ILE   A N   
2077 N  N   B ILE   A 106 ? 0.2800 0.2719 0.2390 -0.0190 -0.0030 -0.0118 106 ILE   A N   
2078 C  CA  A ILE   A 106 ? 0.2380 0.3630 0.2171 -0.0616 -0.0381 -0.0570 106 ILE   A CA  
2079 C  CA  B ILE   A 106 ? 0.2754 0.2782 0.2522 -0.0241 -0.0063 -0.0129 106 ILE   A CA  
2080 C  C   A ILE   A 106 ? 0.2152 0.3382 0.2209 -0.0776 -0.0344 -0.0715 106 ILE   A C   
2081 C  C   B ILE   A 106 ? 0.2684 0.2709 0.2517 -0.0296 -0.0004 -0.0132 106 ILE   A C   
2082 O  O   A ILE   A 106 ? 0.1887 0.3291 0.2254 -0.0836 -0.0142 -0.0706 106 ILE   A O   
2083 O  O   B ILE   A 106 ? 0.2643 0.2694 0.2490 -0.0279 0.0041  -0.0160 106 ILE   A O   
2084 C  CB  A ILE   A 106 ? 0.2395 0.3772 0.2615 -0.0493 -0.0509 -0.0334 106 ILE   A CB  
2085 C  CB  B ILE   A 106 ? 0.2782 0.2907 0.2737 -0.0227 -0.0133 -0.0079 106 ILE   A CB  
2086 C  CG1 A ILE   A 106 ? 0.2327 0.3838 0.2887 -0.0332 -0.0593 -0.0116 106 ILE   A CG1 
2087 C  CG1 B ILE   A 106 ? 0.2789 0.2980 0.2869 -0.0181 -0.0183 -0.0014 106 ILE   A CG1 
2088 C  CG2 A ILE   A 106 ? 0.2420 0.3797 0.2758 -0.0523 -0.0535 -0.0334 106 ILE   A CG2 
2089 C  CG2 B ILE   A 106 ? 0.2785 0.2929 0.2795 -0.0244 -0.0158 -0.0086 106 ILE   A CG2 
2090 C  CD1 A ILE   A 106 ? 0.2324 0.3843 0.3008 -0.0216 -0.0521 -0.0033 106 ILE   A CD1 
2091 C  CD1 B ILE   A 106 ? 0.2806 0.3002 0.2923 -0.0139 -0.0179 0.0015  106 ILE   A CD1 
2114 N  N   A GLN   A 107 ? 0.2351 0.3205 0.2452 -0.0749 -0.0252 -0.0824 107 GLN   A N   
2115 N  N   B GLN   A 107 ? 0.2674 0.2622 0.2589 -0.0348 0.0040  -0.0125 107 GLN   A N   
2116 C  CA  A GLN   A 107 ? 0.2586 0.3022 0.3078 -0.0581 0.0072  -0.0749 107 GLN   A CA  
2117 C  CA  B GLN   A 107 ? 0.2653 0.2539 0.2741 -0.0374 0.0131  -0.0180 107 GLN   A CA  
2118 C  C   A GLN   A 107 ? 0.2343 0.2535 0.2904 -0.0504 0.0281  -0.0449 107 GLN   A C   
2119 C  C   B GLN   A 107 ? 0.2413 0.2331 0.2605 -0.0414 0.0219  -0.0218 107 GLN   A C   
2120 O  O   A GLN   A 107 ? 0.2354 0.2466 0.3288 -0.0418 0.0410  -0.0364 107 GLN   A O   
2121 O  O   B GLN   A 107 ? 0.2467 0.2327 0.2796 -0.0396 0.0179  -0.0136 107 GLN   A O   
2122 C  CB  A GLN   A 107 ? 0.2987 0.3302 0.3951 -0.0586 0.0038  -0.0814 107 GLN   A CB  
2123 C  CB  B GLN   A 107 ? 0.2836 0.2661 0.3080 -0.0385 0.0073  -0.0132 107 GLN   A CB  
2124 C  CG  A GLN   A 107 ? 0.3347 0.3597 0.4851 -0.0546 0.0006  -0.0763 107 GLN   A CG  
2125 C  CG  B GLN   A 107 ? 0.2993 0.2782 0.3405 -0.0394 0.0027  -0.0061 107 GLN   A CG  
2126 C  CD  A GLN   A 107 ? 0.3581 0.3823 0.5585 -0.0531 0.0009  -0.0680 107 GLN   A CD  
2127 C  CD  B GLN   A 107 ? 0.3153 0.2910 0.3699 -0.0381 0.0000  0.0014  107 GLN   A CD  
2128 O  OE1 A GLN   A 107 ? 0.3655 0.3888 0.5891 -0.0521 0.0009  -0.0676 107 GLN   A OE1 
2129 O  OE1 B GLN   A 107 ? 0.3206 0.2977 0.3797 -0.0367 0.0002  0.0076  107 GLN   A OE1 
2130 N  NE2 A GLN   A 107 ? 0.3697 0.3914 0.5818 -0.0559 0.0009  -0.0667 107 GLN   A NE2 
2131 N  NE2 B GLN   A 107 ? 0.3207 0.2941 0.3795 -0.0383 -0.0023 0.0048  107 GLN   A NE2 
2148 N  N   . LEU   A 108 ? 0.2107 0.2139 0.2317 -0.0467 0.0312  -0.0388 108 LEU   A N   
2149 C  CA  . LEU   A 108 ? 0.1844 0.1770 0.2029 -0.0149 0.0215  -0.0093 108 LEU   A CA  
2150 C  C   . LEU   A 108 ? 0.1602 0.1420 0.1899 -0.0041 0.0182  0.0082  108 LEU   A C   
2151 O  O   . LEU   A 108 ? 0.1554 0.1472 0.2170 -0.0011 0.0257  0.0166  108 LEU   A O   
2152 C  CB  . LEU   A 108 ? 0.1896 0.1872 0.1840 -0.0181 0.0266  -0.0087 108 LEU   A CB  
2153 C  CG  . LEU   A 108 ? 0.2031 0.2067 0.2100 -0.0165 0.0368  -0.0183 108 LEU   A CG  
2154 C  CD1 . LEU   A 108 ? 0.2260 0.2133 0.2218 -0.0257 0.0463  -0.0181 108 LEU   A CD1 
2155 C  CD2 . LEU   A 108 ? 0.2028 0.2318 0.2502 -0.0090 0.0377  -0.0139 108 LEU   A CD2 
2168 N  N   . LEU   A 109 ? 0.1462 0.1449 0.1984 0.0031  0.0108  0.0225  109 LEU   A N   
2169 C  CA  . LEU   A 109 ? 0.1450 0.1403 0.1863 -0.0020 0.0038  0.0220  109 LEU   A CA  
2170 C  C   . LEU   A 109 ? 0.1329 0.1303 0.1628 -0.0106 0.0060  0.0086  109 LEU   A C   
2171 O  O   . LEU   A 109 ? 0.1469 0.1274 0.1739 -0.0051 -0.0022 0.0043  109 LEU   A O   
2172 C  CB  . LEU   A 109 ? 0.1485 0.1453 0.2003 0.0098  -0.0059 0.0373  109 LEU   A CB  
2173 C  CG  . LEU   A 109 ? 0.1464 0.1496 0.2127 0.0055  0.0107  0.0359  109 LEU   A CG  
2174 C  CD1 . LEU   A 109 ? 0.1564 0.1460 0.2316 -0.0004 0.0249  0.0105  109 LEU   A CD1 
2175 C  CD2 . LEU   A 109 ? 0.1509 0.1640 0.2365 0.0032  0.0099  0.0373  109 LEU   A CD2 
2187 N  N   . LYS   A 110 ? 0.1317 0.1306 0.1670 -0.0071 -0.0014 0.0085  110 LYS   A N   
2188 C  CA  . LYS   A 110 ? 0.1353 0.1262 0.1679 -0.0049 -0.0077 0.0134  110 LYS   A CA  
2189 C  C   . LYS   A 110 ? 0.1370 0.1187 0.1594 -0.0073 0.0008  0.0040  110 LYS   A C   
2190 O  O   . LYS   A 110 ? 0.1298 0.1242 0.1698 -0.0087 0.0058  -0.0005 110 LYS   A O   
2191 C  CB  . LYS   A 110 ? 0.1382 0.1351 0.1989 -0.0090 -0.0164 -0.0052 110 LYS   A CB  
2192 C  CG  . LYS   A 110 ? 0.1393 0.1310 0.2016 -0.0043 -0.0065 -0.0056 110 LYS   A CG  
2193 C  CD  . LYS   A 110 ? 0.1454 0.1335 0.2135 -0.0069 -0.0134 -0.0012 110 LYS   A CD  
2194 C  CE  . LYS   A 110 ? 0.1503 0.1385 0.2401 -0.0111 0.0121  -0.0068 110 LYS   A CE  
2195 N  NZ  . LYS   A 110 ? 0.1512 0.1411 0.2408 -0.0221 0.0068  -0.0009 110 LYS   A NZ  
2209 N  N   . SER   A 111 ? 0.1344 0.1260 0.1606 -0.0029 -0.0031 0.0083  111 SER   A N   
2210 C  CA  . SER   A 111 ? 0.1278 0.1239 0.1691 0.0019  0.0057  0.0036  111 SER   A CA  
2211 C  C   . SER   A 111 ? 0.1225 0.1238 0.1739 -0.0081 0.0079  0.0102  111 SER   A C   
2212 O  O   . SER   A 111 ? 0.1341 0.1169 0.1814 -0.0035 0.0132  0.0106  111 SER   A O   
2213 C  CB  . SER   A 111 ? 0.1445 0.1473 0.1822 -0.0024 0.0180  -0.0070 111 SER   A CB  
2214 O  OG  . SER   A 111 ? 0.1999 0.1657 0.1934 0.0018  0.0184  -0.0138 111 SER   A OG  
2220 N  N   . ALA   A 112 ? 0.1259 0.1164 0.1732 -0.0028 0.0142  0.0062  112 ALA   A N   
2221 C  CA  . ALA   A 112 ? 0.1290 0.1128 0.1593 -0.0036 0.0122  0.0050  112 ALA   A CA  
2222 C  C   . ALA   A 112 ? 0.1248 0.1114 0.1696 -0.0015 0.0069  0.0008  112 ALA   A C   
2223 O  O   . ALA   A 112 ? 0.1308 0.1129 0.1707 -0.0140 0.0151  0.0098  112 ALA   A O   
2224 C  CB  . ALA   A 112 ? 0.1406 0.1134 0.1737 -0.0051 0.0091  0.0040  112 ALA   A CB  
2230 N  N   . TYR   A 113 ? 0.1170 0.1178 0.1708 -0.0028 0.0040  0.0125  113 TYR   A N   
2231 C  CA  . TYR   A 113 ? 0.1147 0.1149 0.1712 -0.0015 0.0092  0.0140  113 TYR   A CA  
2232 C  C   . TYR   A 113 ? 0.1150 0.1168 0.1637 -0.0100 0.0104  0.0063  113 TYR   A C   
2233 O  O   . TYR   A 113 ? 0.1188 0.1239 0.1690 -0.0055 0.0148  0.0059  113 TYR   A O   
2234 C  CB  . TYR   A 113 ? 0.1133 0.1215 0.1814 -0.0010 0.0018  0.0168  113 TYR   A CB  
2235 C  CG  . TYR   A 113 ? 0.1221 0.1244 0.1646 -0.0090 0.0097  0.0156  113 TYR   A CG  
2236 C  CD1 . TYR   A 113 ? 0.1245 0.1292 0.1540 -0.0011 0.0083  0.0209  113 TYR   A CD1 
2237 C  CD2 . TYR   A 113 ? 0.1291 0.1285 0.1694 -0.0088 0.0017  0.0167  113 TYR   A CD2 
2238 C  CE1 . TYR   A 113 ? 0.1304 0.1385 0.1485 0.0003  0.0078  0.0263  113 TYR   A CE1 
2239 C  CE2 . TYR   A 113 ? 0.1234 0.1346 0.1671 -0.0104 0.0005  0.0234  113 TYR   A CE2 
2240 C  CZ  . TYR   A 113 ? 0.1240 0.1338 0.1539 0.0045  0.0124  0.0267  113 TYR   A CZ  
2241 O  OH  . TYR   A 113 ? 0.1267 0.1429 0.1784 0.0098  0.0025  0.0263  113 TYR   A OH  
2251 N  N   . GLU   A 114 ? 0.1166 0.1144 0.1698 -0.0080 0.0083  0.0132  114 GLU   A N   
2252 C  CA  . GLU   A 114 ? 0.1181 0.1081 0.1671 0.0028  0.0067  0.0189  114 GLU   A CA  
2253 C  C   . GLU   A 114 ? 0.1182 0.1152 0.1737 0.0056  0.0134  0.0082  114 GLU   A C   
2254 O  O   . GLU   A 114 ? 0.1267 0.1145 0.1716 -0.0009 0.0030  0.0072  114 GLU   A O   
2255 C  CB  . GLU   A 114 ? 0.1205 0.1094 0.1704 -0.0014 0.0041  0.0106  114 GLU   A CB  
2256 C  CG  . GLU   A 114 ? 0.1275 0.1164 0.1759 0.0027  0.0016  0.0040  114 GLU   A CG  
2257 C  CD  . GLU   A 114 ? 0.1346 0.1158 0.1872 -0.0025 -0.0000 0.0023  114 GLU   A CD  
2258 O  OE1 . GLU   A 114 ? 0.1419 0.1176 0.1905 -0.0136 0.0134  -0.0028 114 GLU   A OE1 
2259 O  OE2 . GLU   A 114 ? 0.1503 0.1188 0.2151 -0.0097 0.0146  -0.0140 114 GLU   A OE2 
2266 N  N   . ASN   A 115 ? 0.1189 0.1160 0.1584 -0.0038 0.0063  0.0021  115 ASN   A N   
2267 C  CA  . ASN   A 115 ? 0.1176 0.1247 0.1748 -0.0103 0.0118  0.0074  115 ASN   A CA  
2268 C  C   . ASN   A 115 ? 0.1184 0.1167 0.1692 -0.0120 0.0050  0.0084  115 ASN   A C   
2269 O  O   . ASN   A 115 ? 0.1228 0.1330 0.1566 -0.0116 0.0084  0.0129  115 ASN   A O   
2270 C  CB  . ASN   A 115 ? 0.1255 0.1313 0.1641 -0.0084 0.0131  0.0055  115 ASN   A CB  
2271 C  CG  . ASN   A 115 ? 0.1263 0.1537 0.1784 -0.0167 0.0174  0.0051  115 ASN   A CG  
2272 O  OD1 . ASN   A 115 ? 0.1346 0.2493 0.1941 -0.0152 0.0232  0.0255  115 ASN   A OD1 
2273 N  ND2 . ASN   A 115 ? 0.1323 0.1320 0.1681 -0.0117 0.0233  0.0071  115 ASN   A ND2 
2280 N  N   . PHE   A 116 ? 0.1189 0.1196 0.1630 -0.0018 0.0052  0.0203  116 PHE   A N   
2281 C  CA  . PHE   A 116 ? 0.1198 0.1273 0.1524 -0.0036 0.0088  0.0169  116 PHE   A CA  
2282 C  C   . PHE   A 116 ? 0.1145 0.1292 0.1701 -0.0078 0.0149  0.0181  116 PHE   A C   
2283 O  O   . PHE   A 116 ? 0.1268 0.1382 0.1723 0.0038  0.0163  0.0284  116 PHE   A O   
2284 C  CB  . PHE   A 116 ? 0.1221 0.1181 0.1639 -0.0076 0.0132  0.0159  116 PHE   A CB  
2285 C  CG  . PHE   A 116 ? 0.1229 0.1223 0.1669 -0.0109 0.0111  0.0109  116 PHE   A CG  
2286 C  CD1 . PHE   A 116 ? 0.1299 0.1193 0.1690 -0.0060 0.0163  0.0113  116 PHE   A CD1 
2287 C  CD2 . PHE   A 116 ? 0.1271 0.1270 0.1791 -0.0061 0.0155  0.0162  116 PHE   A CD2 
2288 C  CE1 . PHE   A 116 ? 0.1269 0.1175 0.1785 -0.0113 0.0073  0.0032  116 PHE   A CE1 
2289 C  CE2 . PHE   A 116 ? 0.1269 0.1263 0.1769 -0.0079 0.0124  0.0120  116 PHE   A CE2 
2290 C  CZ  . PHE   A 116 ? 0.1326 0.1129 0.1722 -0.0039 0.0054  0.0097  116 PHE   A CZ  
2300 N  N   . ASN   A 117 ? 0.1180 0.1248 0.1722 -0.0040 0.0106  0.0171  117 ASN   A N   
2301 C  CA  . ASN   A 117 ? 0.1223 0.1260 0.1733 -0.0033 0.0113  0.0274  117 ASN   A CA  
2302 C  C   . ASN   A 117 ? 0.1254 0.1340 0.1888 -0.0020 0.0134  0.0262  117 ASN   A C   
2303 O  O   . ASN   A 117 ? 0.1343 0.1381 0.2058 -0.0053 -0.0053 0.0424  117 ASN   A O   
2304 C  CB  . ASN   A 117 ? 0.1217 0.1278 0.1844 0.0012  0.0133  0.0263  117 ASN   A CB  
2305 C  CG  . ASN   A 117 ? 0.1185 0.1314 0.1888 0.0002  0.0089  0.0247  117 ASN   A CG  
2306 O  OD1 . ASN   A 117 ? 0.1215 0.1510 0.1927 -0.0115 0.0078  0.0160  117 ASN   A OD1 
2307 N  ND2 . ASN   A 117 ? 0.1221 0.1291 0.1849 -0.0005 0.0118  0.0257  117 ASN   A ND2 
2314 N  N   . GLN   A 118 ? 0.1187 0.1360 0.1935 -0.0036 -0.0008 0.0277  118 GLN   A N   
2315 C  CA  . GLN   A 118 ? 0.1295 0.1401 0.1974 -0.0042 -0.0002 0.0256  118 GLN   A CA  
2316 C  C   . GLN   A 118 ? 0.1261 0.1459 0.1942 -0.0059 -0.0047 0.0254  118 GLN   A C   
2317 O  O   . GLN   A 118 ? 0.1265 0.1796 0.2276 0.0013  -0.0152 0.0083  118 GLN   A O   
2318 C  CB  . GLN   A 118 ? 0.1259 0.1461 0.1987 -0.0004 0.0043  0.0293  118 GLN   A CB  
2319 C  CG  . GLN   A 118 ? 0.1177 0.1490 0.2086 -0.0037 0.0005  0.0247  118 GLN   A CG  
2320 C  CD  . GLN   A 118 ? 0.1181 0.1474 0.2073 0.0006  0.0050  0.0220  118 GLN   A CD  
2321 O  OE1 . GLN   A 118 ? 0.1281 0.1659 0.2190 0.0124  -0.0005 0.0069  118 GLN   A OE1 
2322 N  NE2 . GLN   A 118 ? 0.1307 0.1438 0.2066 0.0030  -0.0008 0.0219  118 GLN   A NE2 
2331 N  N   . HIS   A 119 ? 0.1334 0.1409 0.1750 -0.0036 -0.0062 0.0194  119 HIS   A N   
2332 C  CA  . HIS   A 119 ? 0.1453 0.1514 0.1748 -0.0061 -0.0011 0.0260  119 HIS   A CA  
2333 C  C   . HIS   A 119 ? 0.1564 0.1547 0.1624 -0.0048 0.0066  0.0310  119 HIS   A C   
2334 O  O   . HIS   A 119 ? 0.1549 0.1693 0.1733 -0.0282 0.0024  0.0306  119 HIS   A O   
2335 C  CB  . HIS   A 119 ? 0.1502 0.1522 0.1932 -0.0031 0.0198  0.0264  119 HIS   A CB  
2336 C  CG  . HIS   A 119 ? 0.1467 0.1567 0.2384 0.0018  0.0223  0.0353  119 HIS   A CG  
2337 N  ND1 . HIS   A 119 ? 0.1597 0.1727 0.2870 -0.0104 0.0081  0.0300  119 HIS   A ND1 
2338 C  CD2 . HIS   A 119 ? 0.1587 0.1593 0.2573 0.0147  0.0359  0.0561  119 HIS   A CD2 
2339 C  CE1 . HIS   A 119 ? 0.1561 0.1700 0.3066 -0.0191 0.0233  0.0496  119 HIS   A CE1 
2340 N  NE2 . HIS   A 119 ? 0.1650 0.1660 0.2977 0.0015  0.0488  0.0581  119 HIS   A NE2 
2348 N  N   . GLU   A 120 ? 0.1653 0.1732 0.1699 0.0031  0.0018  0.0470  120 GLU   A N   
2349 C  CA  . GLU   A 120 ? 0.1862 0.2027 0.1898 0.0082  -0.0018 0.0823  120 GLU   A CA  
2350 C  C   . GLU   A 120 ? 0.1640 0.1876 0.1857 -0.0076 -0.0045 0.0701  120 GLU   A C   
2351 O  O   . GLU   A 120 ? 0.1662 0.1896 0.1928 -0.0077 -0.0031 0.0724  120 GLU   A O   
2352 C  CB  . GLU   A 120 ? 0.2406 0.2630 0.2478 0.0247  0.0034  0.1355  120 GLU   A CB  
2353 C  CG  . GLU   A 120 ? 0.3097 0.3256 0.3477 0.0397  0.0013  0.1302  120 GLU   A CG  
2354 C  CD  . GLU   A 120 ? 0.3689 0.3845 0.4415 0.0513  0.0112  0.1213  120 GLU   A CD  
2355 O  OE1 . GLU   A 120 ? 0.3891 0.4096 0.4735 0.0507  0.0151  0.1143  120 GLU   A OE1 
2356 O  OE2 . GLU   A 120 ? 0.4374 0.4374 0.4865 0.0566  0.0147  0.1238  120 GLU   A OE2 
2363 N  N   . VAL   A 121 ? 0.1599 0.1919 0.1644 -0.0093 0.0039  0.0652  121 VAL   A N   
2364 C  CA  . VAL   A 121 ? 0.1673 0.1984 0.1549 -0.0107 0.0150  0.0611  121 VAL   A CA  
2365 C  C   . VAL   A 121 ? 0.1551 0.1819 0.1313 -0.0164 0.0065  0.0468  121 VAL   A C   
2366 O  O   . VAL   A 121 ? 0.1554 0.1898 0.1627 -0.0259 -0.0110 0.0403  121 VAL   A O   
2367 C  CB  . VAL   A 121 ? 0.2087 0.2350 0.1927 0.0089  0.0308  0.0614  121 VAL   A CB  
2368 C  CG1 . VAL   A 121 ? 0.2142 0.2505 0.1982 0.0143  0.0354  0.0578  121 VAL   A CG1 
2369 C  CG2 . VAL   A 121 ? 0.2342 0.2511 0.2358 -0.0015 0.0252  0.0462  121 VAL   A CG2 
2379 N  N   . LEU   A 122 ? 0.1501 0.1599 0.1438 -0.0140 0.0126  0.0394  122 LEU   A N   
2380 C  CA  . LEU   A 122 ? 0.1514 0.1529 0.1473 -0.0197 0.0238  0.0265  122 LEU   A CA  
2381 C  C   . LEU   A 122 ? 0.1476 0.1493 0.1456 -0.0187 0.0120  0.0297  122 LEU   A C   
2382 O  O   . LEU   A 122 ? 0.1415 0.1567 0.1917 -0.0254 0.0106  0.0300  122 LEU   A O   
2383 C  CB  . LEU   A 122 ? 0.1696 0.1570 0.1781 -0.0102 0.0138  0.0316  122 LEU   A CB  
2384 C  CG  . LEU   A 122 ? 0.1713 0.1599 0.1803 -0.0094 0.0184  0.0286  122 LEU   A CG  
2385 C  CD1 . LEU   A 122 ? 0.1866 0.1669 0.1967 -0.0172 0.0230  0.0341  122 LEU   A CD1 
2386 C  CD2 . LEU   A 122 ? 0.1663 0.1598 0.1635 -0.0095 0.0248  0.0214  122 LEU   A CD2 
2398 N  N   A LEU   A 123 ? 0.1420 0.1455 0.1376 -0.0177 0.0098  0.0259  123 LEU   A N   
2399 N  N   B LEU   A 123 ? 0.1449 0.1470 0.1481 -0.0190 0.0057  0.0226  123 LEU   A N   
2400 C  CA  A LEU   A 123 ? 0.1405 0.1480 0.1348 -0.0148 0.0219  0.0320  123 LEU   A CA  
2401 C  CA  B LEU   A 123 ? 0.1446 0.1495 0.1535 -0.0190 0.0039  0.0204  123 LEU   A CA  
2402 C  C   A LEU   A 123 ? 0.1307 0.1357 0.1367 -0.0126 0.0154  0.0261  123 LEU   A C   
2403 C  C   B LEU   A 123 ? 0.1425 0.1416 0.1570 -0.0146 0.0031  0.0137  123 LEU   A C   
2404 O  O   A LEU   A 123 ? 0.1231 0.1368 0.1279 -0.0187 0.0123  0.0246  123 LEU   A O   
2405 O  O   B LEU   A 123 ? 0.1386 0.1357 0.1614 -0.0081 -0.0018 0.0043  123 LEU   A O   
2406 C  CB  A LEU   A 123 ? 0.1524 0.1596 0.1376 -0.0162 0.0323  0.0238  123 LEU   A CB  
2407 C  CB  B LEU   A 123 ? 0.1471 0.1576 0.1575 -0.0248 0.0009  0.0173  123 LEU   A CB  
2408 C  CG  A LEU   A 123 ? 0.1570 0.1735 0.1497 -0.0130 0.0313  0.0203  123 LEU   A CG  
2409 C  CG  B LEU   A 123 ? 0.1445 0.1632 0.1555 -0.0292 -0.0029 0.0176  123 LEU   A CG  
2410 C  CD1 A LEU   A 123 ? 0.1640 0.1848 0.1611 -0.0010 0.0212  0.0137  123 LEU   A CD1 
2411 C  CD1 B LEU   A 123 ? 0.1476 0.1670 0.1638 -0.0271 -0.0038 0.0205  123 LEU   A CD1 
2412 C  CD2 A LEU   A 123 ? 0.1685 0.1817 0.1557 -0.0086 0.0262  0.0120  123 LEU   A CD2 
2413 C  CD2 B LEU   A 123 ? 0.1478 0.1674 0.1560 -0.0281 -0.0059 0.0101  123 LEU   A CD2 
2436 N  N   A ALA   A 124 ? 0.1307 0.1265 0.1261 -0.0065 0.0140  0.0115  124 ALA   A N   
2437 N  N   B ALA   A 124 ? 0.1444 0.1386 0.1529 -0.0164 0.0053  0.0116  124 ALA   A N   
2438 C  CA  A ALA   A 124 ? 0.1191 0.1271 0.1324 -0.0028 0.0038  0.0166  124 ALA   A CA  
2439 C  CA  B ALA   A 124 ? 0.1420 0.1386 0.1611 -0.0199 0.0079  0.0142  124 ALA   A CA  
2440 C  C   A ALA   A 124 ? 0.1157 0.1275 0.1419 -0.0056 0.0138  0.0180  124 ALA   A C   
2441 C  C   B ALA   A 124 ? 0.1351 0.1307 0.1582 -0.0086 0.0080  0.0154  124 ALA   A C   
2442 O  O   A ALA   A 124 ? 0.1171 0.1326 0.1632 -0.0074 0.0187  0.0308  124 ALA   A O   
2443 O  O   B ALA   A 124 ? 0.1324 0.1233 0.1727 0.0065  0.0088  0.0173  124 ALA   A O   
2444 C  CB  A ALA   A 124 ? 0.1194 0.1257 0.1487 0.0024  -0.0012 0.0252  124 ALA   A CB  
2445 C  CB  B ALA   A 124 ? 0.1505 0.1422 0.1744 -0.0287 0.0110  0.0169  124 ALA   A CB  
2456 N  N   A PRO   A 125 ? 0.1182 0.1248 0.1456 -0.0024 0.0134  0.0210  125 PRO   A N   
2457 N  N   B PRO   A 125 ? 0.1259 0.1221 0.1397 -0.0062 0.0068  0.0126  125 PRO   A N   
2458 C  CA  A PRO   A 125 ? 0.1262 0.1330 0.1514 -0.0097 0.0035  0.0208  125 PRO   A CA  
2459 C  CA  B PRO   A 125 ? 0.1246 0.1220 0.1394 0.0003  0.0074  0.0150  125 PRO   A CA  
2460 C  C   A PRO   A 125 ? 0.1221 0.1412 0.1433 -0.0156 0.0066  0.0167  125 PRO   A C   
2461 C  C   B PRO   A 125 ? 0.1217 0.1246 0.1457 0.0021  0.0108  0.0203  125 PRO   A C   
2462 O  O   A PRO   A 125 ? 0.1296 0.1409 0.1526 -0.0054 -0.0023 0.0125  125 PRO   A O   
2463 O  O   B PRO   A 125 ? 0.1217 0.1248 0.1482 0.0081  0.0119  0.0217  125 PRO   A O   
2464 C  CB  A PRO   A 125 ? 0.1441 0.1350 0.1478 -0.0151 0.0031  0.0331  125 PRO   A CB  
2465 C  CB  B PRO   A 125 ? 0.1316 0.1210 0.1316 -0.0014 -0.0018 0.0140  125 PRO   A CB  
2466 C  CG  A PRO   A 125 ? 0.1419 0.1362 0.1728 -0.0189 0.0024  0.0310  125 PRO   A CG  
2467 C  CG  B PRO   A 125 ? 0.1280 0.1180 0.1390 -0.0094 -0.0028 0.0156  125 PRO   A CG  
2468 C  CD  A PRO   A 125 ? 0.1300 0.1336 0.1557 -0.0155 0.0110  0.0223  125 PRO   A CD  
2469 C  CD  B PRO   A 125 ? 0.1225 0.1140 0.1311 -0.0119 0.0028  0.0109  125 PRO   A CD  
2484 N  N   A LEU   A 126 ? 0.1237 0.1500 0.1415 -0.0117 -0.0082 0.0181  126 LEU   A N   
2485 N  N   B LEU   A 126 ? 0.1208 0.1302 0.1470 0.0063  0.0050  0.0221  126 LEU   A N   
2486 C  CA  A LEU   A 126 ? 0.1257 0.1487 0.1470 -0.0167 0.0032  0.0182  126 LEU   A CA  
2487 C  CA  B LEU   A 126 ? 0.1255 0.1380 0.1488 0.0032  0.0012  0.0266  126 LEU   A CA  
2488 C  C   A LEU   A 126 ? 0.1278 0.1371 0.1587 -0.0065 0.0032  0.0181  126 LEU   A C   
2489 C  C   B LEU   A 126 ? 0.1253 0.1406 0.1442 -0.0030 -0.0067 0.0288  126 LEU   A C   
2490 O  O   A LEU   A 126 ? 0.1313 0.1277 0.1843 -0.0044 0.0133  0.0231  126 LEU   A O   
2491 O  O   B LEU   A 126 ? 0.1287 0.1457 0.1581 -0.0089 -0.0140 0.0217  126 LEU   A O   
2492 C  CB  A LEU   A 126 ? 0.1255 0.1601 0.1771 -0.0232 0.0053  0.0144  126 LEU   A CB  
2493 C  CB  B LEU   A 126 ? 0.1298 0.1412 0.1522 0.0086  -0.0027 0.0242  126 LEU   A CB  
2494 C  CG  A LEU   A 126 ? 0.1229 0.1744 0.2080 -0.0222 0.0125  0.0288  126 LEU   A CG  
2495 C  CG  B LEU   A 126 ? 0.1348 0.1466 0.1605 0.0095  0.0048  0.0318  126 LEU   A CG  
2496 C  CD1 A LEU   A 126 ? 0.1214 0.1825 0.2273 -0.0225 0.0094  0.0299  126 LEU   A CD1 
2497 C  CD1 B LEU   A 126 ? 0.1411 0.1471 0.1692 0.0023  0.0172  0.0358  126 LEU   A CD1 
2498 C  CD2 A LEU   A 126 ? 0.1282 0.1732 0.2116 -0.0327 -0.0019 0.0362  126 LEU   A CD2 
2499 C  CD2 B LEU   A 126 ? 0.1383 0.1480 0.1556 0.0119  0.0038  0.0291  126 LEU   A CD2 
2522 N  N   A LEU   A 127 ? 0.1294 0.1384 0.1629 0.0035  0.0095  0.0179  127 LEU   A N   
2523 N  N   B LEU   A 127 ? 0.1212 0.1389 0.1317 -0.0028 -0.0004 0.0385  127 LEU   A N   
2524 C  CA  A LEU   A 127 ? 0.1279 0.1393 0.1588 -0.0036 -0.0021 0.0169  127 LEU   A CA  
2525 C  CA  B LEU   A 127 ? 0.1192 0.1390 0.1328 -0.0073 -0.0055 0.0340  127 LEU   A CA  
2526 C  C   A LEU   A 127 ? 0.1236 0.1277 0.1437 0.0001  0.0018  0.0104  127 LEU   A C   
2527 C  C   B LEU   A 127 ? 0.1221 0.1358 0.1404 -0.0061 -0.0058 0.0193  127 LEU   A C   
2528 O  O   A LEU   A 127 ? 0.1322 0.1360 0.1713 -0.0104 -0.0031 0.0123  127 LEU   A O   
2529 O  O   B LEU   A 127 ? 0.1238 0.1394 0.1377 -0.0110 0.0057  0.0258  127 LEU   A O   
2530 C  CB  A LEU   A 127 ? 0.1255 0.1439 0.1618 0.0022  -0.0008 0.0197  127 LEU   A CB  
2531 C  CB  B LEU   A 127 ? 0.1139 0.1451 0.1422 -0.0112 -0.0085 0.0276  127 LEU   A CB  
2532 C  CG  A LEU   A 127 ? 0.1307 0.1436 0.1578 0.0072  -0.0057 0.0196  127 LEU   A CG  
2533 C  CG  B LEU   A 127 ? 0.1141 0.1522 0.1367 -0.0071 -0.0096 0.0344  127 LEU   A CG  
2534 C  CD1 A LEU   A 127 ? 0.1403 0.1337 0.1742 0.0065  -0.0064 0.0144  127 LEU   A CD1 
2535 C  CD1 B LEU   A 127 ? 0.1135 0.1587 0.1462 -0.0045 0.0006  0.0286  127 LEU   A CD1 
2536 C  CD2 A LEU   A 127 ? 0.1455 0.1461 0.1754 0.0081  -0.0236 0.0163  127 LEU   A CD2 
2537 C  CD2 B LEU   A 127 ? 0.1203 0.1553 0.1432 -0.0033 -0.0258 0.0265  127 LEU   A CD2 
2560 N  N   A SER   A 128 ? 0.1338 0.1271 0.1334 -0.0035 0.0065  0.0218  128 SER   A N   
2561 N  N   B SER   A 128 ? 0.1282 0.1318 0.1463 -0.0095 -0.0104 0.0168  128 SER   A N   
2562 C  CA  A SER   A 128 ? 0.1410 0.1271 0.1246 -0.0038 0.0003  0.0206  128 SER   A CA  
2563 C  CA  B SER   A 128 ? 0.1327 0.1274 0.1415 -0.0069 -0.0095 0.0101  128 SER   A CA  
2564 C  C   A SER   A 128 ? 0.1460 0.1345 0.1368 0.0027  0.0023  0.0226  128 SER   A C   
2565 C  C   B SER   A 128 ? 0.1286 0.1274 0.1392 -0.0084 -0.0208 0.0105  128 SER   A C   
2566 O  O   A SER   A 128 ? 0.1617 0.1553 0.1523 0.0054  -0.0002 0.0218  128 SER   A O   
2567 O  O   B SER   A 128 ? 0.1250 0.1310 0.1380 -0.0099 -0.0289 0.0189  128 SER   A O   
2568 C  CB  A SER   A 128 ? 0.1406 0.1247 0.1326 -0.0063 -0.0030 0.0118  128 SER   A CB  
2569 C  CB  B SER   A 128 ? 0.1423 0.1327 0.1411 -0.0044 -0.0015 0.0081  128 SER   A CB  
2570 O  OG  A SER   A 128 ? 0.1413 0.1364 0.1436 -0.0062 0.0053  0.0061  128 SER   A OG  
2571 O  OG  B SER   A 128 ? 0.1481 0.1372 0.1340 -0.0026 0.0043  0.0219  128 SER   A OG  
2582 N  N   A ALA   A 129 ? 0.1368 0.1410 0.1518 0.0044  -0.0009 0.0303  129 ALA   A N   
2583 N  N   B ALA   A 129 ? 0.1299 0.1278 0.1476 -0.0012 -0.0203 -0.0002 129 ALA   A N   
2584 C  CA  A ALA   A 129 ? 0.1357 0.1451 0.1696 0.0039  -0.0048 0.0194  129 ALA   A CA  
2585 C  CA  B ALA   A 129 ? 0.1315 0.1302 0.1601 0.0008  -0.0113 -0.0059 129 ALA   A CA  
2586 C  C   A ALA   A 129 ? 0.1343 0.1389 0.1600 0.0010  -0.0149 0.0080  129 ALA   A C   
2587 C  C   B ALA   A 129 ? 0.1393 0.1391 0.1684 0.0013  -0.0039 -0.0029 129 ALA   A C   
2588 O  O   A ALA   A 129 ? 0.1367 0.1398 0.1676 -0.0008 -0.0111 0.0154  129 ALA   A O   
2589 O  O   B ALA   A 129 ? 0.1421 0.1409 0.1761 -0.0041 -0.0046 -0.0026 129 ALA   A O   
2590 C  CB  A ALA   A 129 ? 0.1398 0.1635 0.1923 0.0107  0.0131  0.0361  129 ALA   A CB  
2591 C  CB  B ALA   A 129 ? 0.1235 0.1218 0.1421 0.0019  -0.0143 -0.0128 129 ALA   A CB  
2602 N  N   A GLY   A 130 ? 0.1423 0.1419 0.1898 0.0039  -0.0050 -0.0031 130 GLY   A N   
2603 N  N   B GLY   A 130 ? 0.1472 0.1445 0.1843 0.0057  0.0064  0.0047  130 GLY   A N   
2604 C  CA  A GLY   A 130 ? 0.1550 0.1419 0.1985 0.0107  -0.0036 -0.0033 130 GLY   A CA  
2605 C  CA  B GLY   A 130 ? 0.1547 0.1467 0.1816 0.0075  0.0160  0.0113  130 GLY   A CA  
2606 C  C   A GLY   A 130 ? 0.1596 0.1377 0.1831 0.0068  -0.0055 -0.0037 130 GLY   A C   
2607 C  C   B GLY   A 130 ? 0.1612 0.1451 0.1713 0.0064  0.0216  0.0053  130 GLY   A C   
2608 O  O   A GLY   A 130 ? 0.1600 0.1386 0.1823 0.0037  -0.0127 -0.0092 130 GLY   A O   
2609 O  O   B GLY   A 130 ? 0.1603 0.1422 0.1591 0.0032  0.0317  -0.0002 130 GLY   A O   
2616 N  N   A ILE   A 131 ? 0.1683 0.1333 0.1686 0.0003  -0.0068 0.0090  131 ILE   A N   
2617 N  N   B ILE   A 131 ? 0.1713 0.1514 0.1702 0.0052  0.0073  0.0027  131 ILE   A N   
2618 C  CA  A ILE   A 131 ? 0.1786 0.1323 0.1458 -0.0097 -0.0190 0.0051  131 ILE   A CA  
2619 C  CA  B ILE   A 131 ? 0.1751 0.1513 0.1633 0.0024  -0.0020 0.0024  131 ILE   A CA  
2620 C  C   A ILE   A 131 ? 0.1692 0.1360 0.1386 -0.0121 -0.0159 0.0146  131 ILE   A C   
2621 C  C   B ILE   A 131 ? 0.1718 0.1450 0.1573 -0.0010 -0.0077 0.0001  131 ILE   A C   
2622 O  O   A ILE   A 131 ? 0.1765 0.1543 0.1494 -0.0042 -0.0164 0.0225  131 ILE   A O   
2623 O  O   B ILE   A 131 ? 0.1741 0.1453 0.1622 -0.0017 -0.0080 0.0026  131 ILE   A O   
2624 C  CB  A ILE   A 131 ? 0.2021 0.1369 0.1421 -0.0146 -0.0254 0.0022  131 ILE   A CB  
2625 C  CB  B ILE   A 131 ? 0.1830 0.1585 0.1684 -0.0022 -0.0029 0.0113  131 ILE   A CB  
2626 C  CG1 A ILE   A 131 ? 0.2105 0.1693 0.1587 -0.0226 -0.0220 0.0089  131 ILE   A CG1 
2627 C  CG1 B ILE   A 131 ? 0.1861 0.1695 0.1759 -0.0040 -0.0079 0.0186  131 ILE   A CG1 
2628 C  CG2 A ILE   A 131 ? 0.2175 0.1258 0.1496 -0.0036 -0.0208 -0.0120 131 ILE   A CG2 
2629 C  CG2 B ILE   A 131 ? 0.1901 0.1558 0.1652 -0.0022 -0.0000 0.0131  131 ILE   A CG2 
2630 C  CD1 A ILE   A 131 ? 0.2170 0.1795 0.1815 -0.0296 -0.0261 0.0083  131 ILE   A CD1 
2631 C  CD1 B ILE   A 131 ? 0.1902 0.1752 0.1804 -0.0075 -0.0166 0.0275  131 ILE   A CD1 
2654 N  N   A PHE   A 132 ? 0.1534 0.1276 0.1388 -0.0044 -0.0109 0.0193  132 PHE   A N   
2655 N  N   B PHE   A 132 ? 0.1656 0.1419 0.1549 -0.0001 -0.0086 -0.0018 132 PHE   A N   
2656 C  CA  A PHE   A 132 ? 0.1562 0.1344 0.1434 -0.0057 -0.0130 0.0162  132 PHE   A CA  
2657 C  CA  B PHE   A 132 ? 0.1663 0.1458 0.1497 -0.0032 -0.0050 -0.0022 132 PHE   A CA  
2658 C  C   A PHE   A 132 ? 0.1676 0.1495 0.1542 -0.0055 -0.0078 0.0156  132 PHE   A C   
2659 C  C   B PHE   A 132 ? 0.1681 0.1560 0.1544 -0.0082 -0.0052 0.0020  132 PHE   A C   
2660 O  O   A PHE   A 132 ? 0.1772 0.1562 0.1499 -0.0068 -0.0100 0.0071  132 PHE   A O   
2661 O  O   B PHE   A 132 ? 0.1717 0.1627 0.1557 -0.0138 -0.0016 0.0019  132 PHE   A O   
2662 C  CB  A PHE   A 132 ? 0.1546 0.1329 0.1531 -0.0042 -0.0076 0.0196  132 PHE   A CB  
2663 C  CB  B PHE   A 132 ? 0.1674 0.1425 0.1478 0.0007  -0.0026 -0.0101 132 PHE   A CB  
2664 C  CG  A PHE   A 132 ? 0.1584 0.1365 0.1362 -0.0013 -0.0183 0.0220  132 PHE   A CG  
2665 C  CG  B PHE   A 132 ? 0.1689 0.1446 0.1467 0.0034  -0.0080 -0.0130 132 PHE   A CG  
2666 C  CD1 A PHE   A 132 ? 0.1612 0.1546 0.1625 0.0062  -0.0180 0.0013  132 PHE   A CD1 
2667 C  CD1 B PHE   A 132 ? 0.1708 0.1514 0.1601 0.0063  -0.0083 -0.0218 132 PHE   A CD1 
2668 C  CD2 A PHE   A 132 ? 0.1622 0.1507 0.1410 0.0031  -0.0082 0.0171  132 PHE   A CD2 
2669 C  CD2 B PHE   A 132 ? 0.1701 0.1465 0.1487 0.0066  -0.0028 -0.0245 132 PHE   A CD2 
2670 C  CE1 A PHE   A 132 ? 0.1628 0.1543 0.1658 0.0125  -0.0208 -0.0088 132 PHE   A CE1 
2671 C  CE1 B PHE   A 132 ? 0.1720 0.1516 0.1627 0.0091  -0.0113 -0.0283 132 PHE   A CE1 
2672 C  CE2 A PHE   A 132 ? 0.1591 0.1586 0.1508 0.0051  -0.0116 0.0122  132 PHE   A CE2 
2673 C  CE2 B PHE   A 132 ? 0.1701 0.1527 0.1617 0.0107  -0.0084 -0.0240 132 PHE   A CE2 
2674 C  CZ  A PHE   A 132 ? 0.1561 0.1551 0.1602 0.0028  -0.0178 0.0099  132 PHE   A CZ  
2675 C  CZ  B PHE   A 132 ? 0.1702 0.1531 0.1653 0.0072  -0.0111 -0.0236 132 PHE   A CZ  
2694 N  N   A GLY   A 133 ? 0.1709 0.1557 0.1539 -0.0039 -0.0305 0.0250  133 GLY   A N   
2695 N  N   B GLY   A 133 ? 0.1655 0.1569 0.1552 -0.0075 -0.0155 0.0066  133 GLY   A N   
2696 C  CA  A GLY   A 133 ? 0.1795 0.1677 0.1666 0.0015  -0.0427 0.0096  133 GLY   A CA  
2697 C  CA  B GLY   A 133 ? 0.1644 0.1591 0.1563 -0.0056 -0.0177 0.0053  133 GLY   A CA  
2698 C  C   A GLY   A 133 ? 0.1777 0.1773 0.1556 0.0006  -0.0442 -0.0028 133 GLY   A C   
2699 C  C   B GLY   A 133 ? 0.1575 0.1604 0.1468 -0.0080 -0.0110 0.0023  133 GLY   A C   
2700 O  O   A GLY   A 133 ? 0.1924 0.1914 0.1591 -0.0000 -0.0307 -0.0240 133 GLY   A O   
2701 O  O   B GLY   A 133 ? 0.1564 0.1684 0.1453 -0.0025 -0.0123 -0.0002 133 GLY   A O   
2708 N  N   A ALA   A 134 ? 0.1707 0.1703 0.1560 -0.0036 -0.0405 -0.0041 134 ALA   A N   
2709 N  N   B ALA   A 134 ? 0.1600 0.1513 0.1594 -0.0160 -0.0082 -0.0023 134 ALA   A N   
2710 C  CA  A ALA   A 134 ? 0.1679 0.1729 0.1778 0.0017  -0.0317 -0.0094 134 ALA   A CA  
2711 C  CA  B ALA   A 134 ? 0.1656 0.1467 0.1733 -0.0156 -0.0109 -0.0107 134 ALA   A CA  
2712 C  C   A ALA   A 134 ? 0.1690 0.1790 0.1733 0.0009  -0.0309 -0.0029 134 ALA   A C   
2713 C  C   B ALA   A 134 ? 0.1670 0.1469 0.1629 -0.0118 -0.0117 -0.0141 134 ALA   A C   
2714 O  O   A ALA   A 134 ? 0.1812 0.1876 0.1910 0.0007  -0.0029 0.0003  134 ALA   A O   
2715 O  O   B ALA   A 134 ? 0.1707 0.1539 0.1543 -0.0116 0.0031  -0.0171 134 ALA   A O   
2716 C  CB  A ALA   A 134 ? 0.1736 0.1659 0.2047 0.0066  -0.0269 -0.0079 134 ALA   A CB  
2717 C  CB  B ALA   A 134 ? 0.1667 0.1445 0.1932 -0.0196 -0.0097 -0.0072 134 ALA   A CB  
2728 N  N   A ASP   A 135 ? 0.1763 0.1860 0.1837 -0.0098 -0.0295 0.0034  135 ASP   A N   
2729 N  N   B ASP   A 135 ? 0.1664 0.1477 0.1562 -0.0115 -0.0161 -0.0086 135 ASP   A N   
2730 C  CA  A ASP   A 135 ? 0.1744 0.1937 0.2129 -0.0149 -0.0380 0.0146  135 ASP   A CA  
2731 C  CA  B ASP   A 135 ? 0.1616 0.1495 0.1494 -0.0134 -0.0190 -0.0015 135 ASP   A CA  
2732 C  C   A ASP   A 135 ? 0.1641 0.1789 0.2113 -0.0122 -0.0255 0.0239  135 ASP   A C   
2733 C  C   B ASP   A 135 ? 0.1483 0.1442 0.1403 -0.0086 -0.0158 0.0026  135 ASP   A C   
2734 O  O   A ASP   A 135 ? 0.1649 0.1703 0.2190 -0.0068 -0.0215 0.0277  135 ASP   A O   
2735 O  O   B ASP   A 135 ? 0.1483 0.1447 0.1374 -0.0124 -0.0234 -0.0057 135 ASP   A O   
2736 C  CB  A ASP   A 135 ? 0.1989 0.2207 0.2583 -0.0354 -0.0504 0.0019  135 ASP   A CB  
2737 C  CB  B ASP   A 135 ? 0.1686 0.1592 0.1562 -0.0162 -0.0345 -0.0065 135 ASP   A CB  
2738 C  CG  A ASP   A 135 ? 0.2157 0.2476 0.2906 -0.0530 -0.0656 -0.0004 135 ASP   A CG  
2739 C  CG  B ASP   A 135 ? 0.1746 0.1723 0.1821 -0.0146 -0.0478 -0.0076 135 ASP   A CG  
2740 O  OD1 A ASP   A 135 ? 0.2166 0.2599 0.2943 -0.0569 -0.0740 0.0165  135 ASP   A OD1 
2741 O  OD1 B ASP   A 135 ? 0.1736 0.1696 0.1777 -0.0095 -0.0496 -0.0043 135 ASP   A OD1 
2742 O  OD2 A ASP   A 135 ? 0.2419 0.2669 0.3409 -0.0555 -0.0522 -0.0064 135 ASP   A OD2 
2743 O  OD2 B ASP   A 135 ? 0.1802 0.1817 0.2023 -0.0130 -0.0580 -0.0125 135 ASP   A OD2 
2752 N  N   A PRO   A 136 ? 0.1557 0.1811 0.2146 0.0012  -0.0229 0.0275  136 PRO   A N   
2753 N  N   B PRO   A 136 ? 0.1443 0.1400 0.1276 0.0014  -0.0073 0.0077  136 PRO   A N   
2754 C  CA  A PRO   A 136 ? 0.1501 0.1811 0.2285 -0.0022 -0.0130 0.0187  136 PRO   A CA  
2755 C  CA  B PRO   A 136 ? 0.1411 0.1467 0.1337 -0.0027 -0.0007 0.0056  136 PRO   A CA  
2756 C  C   A PRO   A 136 ? 0.1291 0.1777 0.2250 -0.0022 -0.0086 0.0271  136 PRO   A C   
2757 C  C   B PRO   A 136 ? 0.1356 0.1496 0.1382 -0.0077 -0.0073 0.0091  136 PRO   A C   
2758 O  O   A PRO   A 136 ? 0.1229 0.1782 0.2205 -0.0060 0.0004  0.0329  136 PRO   A O   
2759 O  O   B PRO   A 136 ? 0.1289 0.1436 0.1281 -0.0072 -0.0027 0.0008  136 PRO   A O   
2760 C  CB  A PRO   A 136 ? 0.1645 0.1813 0.2409 -0.0008 -0.0021 0.0119  136 PRO   A CB  
2761 C  CB  B PRO   A 136 ? 0.1469 0.1455 0.1347 -0.0025 -0.0010 -0.0019 136 PRO   A CB  
2762 C  CG  A PRO   A 136 ? 0.1758 0.1916 0.2502 0.0064  -0.0044 0.0070  136 PRO   A CG  
2763 C  CG  B PRO   A 136 ? 0.1532 0.1442 0.1390 0.0040  0.0047  -0.0019 136 PRO   A CG  
2764 C  CD  A PRO   A 136 ? 0.1673 0.1894 0.2302 0.0109  -0.0128 0.0256  136 PRO   A CD  
2765 C  CD  B PRO   A 136 ? 0.1474 0.1348 0.1213 0.0080  0.0059  0.0113  136 PRO   A CD  
2780 N  N   A ILE   A 137 ? 0.1272 0.1761 0.2400 -0.0052 -0.0170 0.0305  137 ILE   A N   
2781 N  N   B ILE   A 137 ? 0.1350 0.1515 0.1616 -0.0082 -0.0154 0.0119  137 ILE   A N   
2782 C  CA  A ILE   A 137 ? 0.1322 0.1777 0.2635 -0.0165 -0.0311 0.0271  137 ILE   A CA  
2783 C  CA  B ILE   A 137 ? 0.1379 0.1552 0.1790 -0.0054 -0.0135 0.0093  137 ILE   A CA  
2784 C  C   A ILE   A 137 ? 0.1384 0.1748 0.2462 -0.0211 -0.0328 0.0237  137 ILE   A C   
2785 C  C   B ILE   A 137 ? 0.1358 0.1587 0.1724 -0.0087 -0.0077 0.0193  137 ILE   A C   
2786 O  O   A ILE   A 137 ? 0.1433 0.1756 0.2471 -0.0213 -0.0343 0.0178  137 ILE   A O   
2787 O  O   B ILE   A 137 ? 0.1340 0.1606 0.1684 -0.0066 -0.0019 0.0259  137 ILE   A O   
2788 C  CB  A ILE   A 137 ? 0.1415 0.1942 0.2919 -0.0218 -0.0430 0.0248  137 ILE   A CB  
2789 C  CB  B ILE   A 137 ? 0.1427 0.1568 0.1983 -0.0043 -0.0218 -0.0035 137 ILE   A CB  
2790 C  CG1 A ILE   A 137 ? 0.1542 0.2100 0.3322 -0.0179 -0.0402 0.0221  137 ILE   A CG1 
2791 C  CG1 B ILE   A 137 ? 0.1499 0.1596 0.2252 -0.0051 -0.0294 -0.0109 137 ILE   A CG1 
2792 C  CG2 A ILE   A 137 ? 0.1497 0.1948 0.2931 -0.0238 -0.0342 0.0164  137 ILE   A CG2 
2793 C  CG2 B ILE   A 137 ? 0.1447 0.1586 0.2006 -0.0011 -0.0178 -0.0085 137 ILE   A CG2 
2794 C  CD1 A ILE   A 137 ? 0.1696 0.2244 0.3589 -0.0103 -0.0348 0.0131  137 ILE   A CD1 
2795 C  CD1 B ILE   A 137 ? 0.1529 0.1611 0.2432 -0.0089 -0.0320 -0.0116 137 ILE   A CD1 
2818 N  N   A HIS   A 138 ? 0.1343 0.1907 0.2429 -0.0151 -0.0202 0.0244  138 HIS   A N   
2819 N  N   B HIS   A 138 ? 0.1366 0.1677 0.1828 -0.0113 0.0006  0.0174  138 HIS   A N   
2820 C  CA  A HIS   A 138 ? 0.1378 0.1899 0.2150 -0.0186 -0.0196 0.0223  138 HIS   A CA  
2821 C  CA  B HIS   A 138 ? 0.1404 0.1688 0.1865 -0.0128 -0.0003 0.0144  138 HIS   A CA  
2822 C  C   A HIS   A 138 ? 0.1358 0.1785 0.2036 -0.0107 -0.0169 0.0319  138 HIS   A C   
2823 C  C   B HIS   A 138 ? 0.1365 0.1644 0.1888 -0.0088 -0.0021 0.0278  138 HIS   A C   
2824 O  O   A HIS   A 138 ? 0.1490 0.1776 0.2108 -0.0142 -0.0161 0.0281  138 HIS   A O   
2825 O  O   B HIS   A 138 ? 0.1410 0.1604 0.1965 -0.0100 -0.0016 0.0235  138 HIS   A O   
2826 C  CB  A HIS   A 138 ? 0.1569 0.2008 0.2237 -0.0155 -0.0233 0.0166  138 HIS   A CB  
2827 C  CB  B HIS   A 138 ? 0.1443 0.1733 0.1885 -0.0102 -0.0000 -0.0004 138 HIS   A CB  
2828 C  CG  A HIS   A 138 ? 0.1778 0.2108 0.2227 -0.0116 -0.0271 0.0043  138 HIS   A CG  
2829 C  CG  B HIS   A 138 ? 0.1533 0.1774 0.1913 -0.0062 -0.0086 -0.0140 138 HIS   A CG  
2830 N  ND1 A HIS   A 138 ? 0.1990 0.2221 0.2470 -0.0117 -0.0292 0.0031  138 HIS   A ND1 
2831 N  ND1 B HIS   A 138 ? 0.1649 0.1827 0.2097 -0.0034 -0.0168 -0.0201 138 HIS   A ND1 
2832 C  CD2 A HIS   A 138 ? 0.1812 0.2180 0.2246 -0.0064 -0.0184 0.0033  138 HIS   A CD2 
2833 C  CD2 B HIS   A 138 ? 0.1540 0.1753 0.1925 0.0004  -0.0065 -0.0129 138 HIS   A CD2 
2834 C  CE1 A HIS   A 138 ? 0.2023 0.2241 0.2378 -0.0054 -0.0277 0.0071  138 HIS   A CE1 
2835 C  CE1 B HIS   A 138 ? 0.1669 0.1814 0.2056 0.0000  -0.0151 -0.0155 138 HIS   A CE1 
2836 N  NE2 A HIS   A 138 ? 0.1894 0.2207 0.2190 -0.0028 -0.0106 0.0063  138 HIS   A NE2 
2837 N  NE2 B HIS   A 138 ? 0.1614 0.1777 0.1955 0.0020  -0.0055 -0.0129 138 HIS   A NE2 
2852 N  N   . SER   A 139 ? 0.1337 0.1639 0.1989 -0.0080 -0.0133 0.0394  139 SER   A N   
2853 C  CA  . SER   A 139 ? 0.1281 0.1576 0.1956 -0.0079 -0.0091 0.0384  139 SER   A CA  
2854 C  C   . SER   A 139 ? 0.1243 0.1460 0.1952 -0.0088 -0.0009 0.0276  139 SER   A C   
2855 O  O   . SER   A 139 ? 0.1192 0.1442 0.2022 -0.0096 0.0025  0.0289  139 SER   A O   
2856 C  CB  . SER   A 139 ? 0.1249 0.1551 0.2066 -0.0174 -0.0120 0.0351  139 SER   A CB  
2857 O  OG  . SER   A 139 ? 0.1327 0.1513 0.2047 -0.0173 -0.0172 0.0405  139 SER   A OG  
2864 N  N   . LEU   A 140 ? 0.1203 0.1517 0.2054 -0.0040 0.0034  0.0363  140 LEU   A N   
2865 C  CA  . LEU   A 140 ? 0.1187 0.1470 0.2035 -0.0073 -0.0007 0.0357  140 LEU   A CA  
2866 C  C   . LEU   A 140 ? 0.1149 0.1564 0.1872 -0.0157 -0.0008 0.0344  140 LEU   A C   
2867 O  O   . LEU   A 140 ? 0.1226 0.1576 0.2006 -0.0071 -0.0077 0.0396  140 LEU   A O   
2868 C  CB  . LEU   A 140 ? 0.1203 0.1518 0.2189 -0.0078 0.0040  0.0264  140 LEU   A CB  
2869 C  CG  . LEU   A 140 ? 0.1218 0.1716 0.2216 -0.0209 0.0090  0.0293  140 LEU   A CG  
2870 C  CD1 . LEU   A 140 ? 0.1259 0.1724 0.2163 -0.0097 0.0089  0.0276  140 LEU   A CD1 
2871 C  CD2 . LEU   A 140 ? 0.1272 0.1881 0.2233 -0.0169 0.0165  0.0433  140 LEU   A CD2 
2883 N  N   . ARG   A 141 ? 0.1250 0.1587 0.1974 -0.0111 -0.0053 0.0308  141 ARG   A N   
2884 C  CA  . ARG   A 141 ? 0.1380 0.1703 0.2184 -0.0214 -0.0126 0.0108  141 ARG   A CA  
2885 C  C   . ARG   A 141 ? 0.1380 0.1496 0.2065 -0.0161 -0.0124 0.0168  141 ARG   A C   
2886 O  O   . ARG   A 141 ? 0.1336 0.1467 0.2146 -0.0198 0.0022  0.0121  141 ARG   A O   
2887 C  CB  . ARG   A 141 ? 0.1493 0.1986 0.2640 -0.0264 -0.0294 -0.0175 141 ARG   A CB  
2888 C  CG  . ARG   A 141 ? 0.1867 0.2398 0.3132 -0.0208 -0.0215 -0.0284 141 ARG   A CG  
2889 C  CD  . ARG   A 141 ? 0.2138 0.2679 0.3492 -0.0289 -0.0093 -0.0299 141 ARG   A CD  
2890 N  NE  . ARG   A 141 ? 0.2024 0.2884 0.3580 -0.0370 -0.0185 -0.0307 141 ARG   A NE  
2891 C  CZ  . ARG   A 141 ? 0.2045 0.3090 0.3665 -0.0565 -0.0151 -0.0261 141 ARG   A CZ  
2892 N  NH1 . ARG   A 141 ? 0.1894 0.3120 0.3645 -0.0666 -0.0011 -0.0312 141 ARG   A NH1 
2893 N  NH2 . ARG   A 141 ? 0.2069 0.3247 0.3877 -0.0610 -0.0233 -0.0205 141 ARG   A NH2 
2907 N  N   . VAL   A 142 ? 0.1314 0.1491 0.1974 -0.0079 -0.0078 0.0130  142 VAL   A N   
2908 C  CA  . VAL   A 142 ? 0.1290 0.1434 0.2009 -0.0056 0.0088  0.0066  142 VAL   A CA  
2909 C  C   . VAL   A 142 ? 0.1201 0.1395 0.1840 -0.0145 0.0035  0.0154  142 VAL   A C   
2910 O  O   . VAL   A 142 ? 0.1263 0.1447 0.1914 -0.0044 0.0021  0.0133  142 VAL   A O   
2911 C  CB  . VAL   A 142 ? 0.1402 0.1539 0.1931 -0.0133 0.0057  0.0179  142 VAL   A CB  
2912 C  CG1 . VAL   A 142 ? 0.1357 0.1475 0.1980 -0.0205 0.0119  0.0149  142 VAL   A CG1 
2913 C  CG2 . VAL   A 142 ? 0.1516 0.1718 0.2183 -0.0005 0.0005  0.0203  142 VAL   A CG2 
2923 N  N   . CYS   A 143 ? 0.1220 0.1415 0.1912 -0.0141 -0.0052 0.0199  143 CYS   A N   
2924 C  CA  . CYS   A 143 ? 0.1182 0.1411 0.1965 -0.0113 0.0027  0.0213  143 CYS   A CA  
2925 C  C   . CYS   A 143 ? 0.1221 0.1396 0.1839 -0.0114 0.0014  0.0309  143 CYS   A C   
2926 O  O   . CYS   A 143 ? 0.1197 0.1388 0.1918 -0.0054 0.0024  0.0281  143 CYS   A O   
2927 C  CB  . CYS   A 143 ? 0.1289 0.1409 0.2004 -0.0053 0.0149  0.0245  143 CYS   A CB  
2928 S  SG  . CYS   A 143 ? 0.1476 0.1481 0.1909 0.0014  0.0100  0.0162  143 CYS   A SG  
2934 N  N   . VAL   A 144 ? 0.1208 0.1427 0.1999 -0.0047 0.0092  0.0320  144 VAL   A N   
2935 C  CA  . VAL   A 144 ? 0.1247 0.1463 0.2360 -0.0134 0.0181  0.0264  144 VAL   A CA  
2936 C  C   . VAL   A 144 ? 0.1304 0.1335 0.2395 -0.0205 -0.0043 0.0171  144 VAL   A C   
2937 O  O   . VAL   A 144 ? 0.1404 0.1415 0.2337 -0.0065 -0.0078 0.0308  144 VAL   A O   
2938 C  CB  . VAL   A 144 ? 0.1557 0.1655 0.3041 -0.0023 0.0339  0.0286  144 VAL   A CB  
2939 C  CG1 . VAL   A 144 ? 0.1744 0.1818 0.3338 -0.0095 0.0203  0.0251  144 VAL   A CG1 
2940 C  CG2 . VAL   A 144 ? 0.1366 0.1725 0.3049 -0.0088 0.0482  0.0360  144 VAL   A CG2 
2950 N  N   . ASP   A 145 ? 0.1301 0.1304 0.2414 -0.0122 -0.0007 0.0154  145 ASP   A N   
2951 C  CA  . ASP   A 145 ? 0.1411 0.1362 0.2443 -0.0175 -0.0015 0.0072  145 ASP   A CA  
2952 C  C   . ASP   A 145 ? 0.1482 0.1372 0.2391 -0.0126 0.0006  0.0015  145 ASP   A C   
2953 O  O   . ASP   A 145 ? 0.1534 0.1481 0.2771 -0.0149 -0.0024 -0.0295 145 ASP   A O   
2954 C  CB  . ASP   A 145 ? 0.1563 0.1656 0.2614 -0.0214 -0.0142 -0.0035 145 ASP   A CB  
2955 C  CG  . ASP   A 145 ? 0.1685 0.1970 0.2861 -0.0377 -0.0215 -0.0006 145 ASP   A CG  
2956 O  OD1 . ASP   A 145 ? 0.1630 0.2113 0.3009 -0.0487 -0.0077 0.0059  145 ASP   A OD1 
2957 O  OD2 . ASP   A 145 ? 0.1922 0.2167 0.2936 -0.0409 -0.0372 0.0004  145 ASP   A OD2 
2962 N  N   . THR   A 146 ? 0.1290 0.1271 0.2103 -0.0126 0.0030  0.0148  146 THR   A N   
2963 C  CA  . THR   A 146 ? 0.1263 0.1308 0.1933 -0.0034 -0.0011 0.0122  146 THR   A CA  
2964 C  C   . THR   A 146 ? 0.1248 0.1276 0.1837 0.0026  0.0105  0.0179  146 THR   A C   
2965 O  O   . THR   A 146 ? 0.1387 0.1377 0.2018 0.0072  0.0048  0.0094  146 THR   A O   
2966 C  CB  . THR   A 146 ? 0.1230 0.1373 0.1851 -0.0018 0.0009  0.0159  146 THR   A CB  
2967 O  OG1 . THR   A 146 ? 0.1234 0.1471 0.2002 0.0015  0.0001  0.0054  146 THR   A OG1 
2968 C  CG2 . THR   A 146 ? 0.1266 0.1386 0.1987 -0.0063 0.0033  0.0105  146 THR   A CG2 
2976 N  N   . VAL   A 147 ? 0.1231 0.1334 0.1798 0.0004  0.0080  0.0184  147 VAL   A N   
2977 C  CA  . VAL   A 147 ? 0.1185 0.1373 0.1812 -0.0053 0.0221  0.0232  147 VAL   A CA  
2978 C  C   . VAL   A 147 ? 0.1271 0.1311 0.1957 -0.0093 0.0160  0.0310  147 VAL   A C   
2979 O  O   . VAL   A 147 ? 0.1309 0.1372 0.2187 -0.0162 0.0107  0.0188  147 VAL   A O   
2980 C  CB  . VAL   A 147 ? 0.1334 0.1398 0.1931 -0.0094 0.0186  0.0295  147 VAL   A CB  
2981 C  CG1 . VAL   A 147 ? 0.1627 0.1466 0.1860 -0.0115 0.0080  0.0286  147 VAL   A CG1 
2982 C  CG2 . VAL   A 147 ? 0.1376 0.1371 0.1950 -0.0146 0.0086  0.0285  147 VAL   A CG2 
2992 N  N   . ARG   A 148 ? 0.1226 0.1370 0.1980 -0.0080 0.0162  0.0393  148 ARG   A N   
2993 C  CA  . ARG   A 148 ? 0.1303 0.1335 0.2036 -0.0057 0.0100  0.0384  148 ARG   A CA  
2994 C  C   . ARG   A 148 ? 0.1427 0.1371 0.2114 -0.0135 0.0102  0.0494  148 ARG   A C   
2995 O  O   . ARG   A 148 ? 0.1737 0.1482 0.2298 -0.0201 0.0159  0.0523  148 ARG   A O   
2996 C  CB  . ARG   A 148 ? 0.1354 0.1350 0.2219 -0.0096 0.0167  0.0371  148 ARG   A CB  
2997 C  CG  . ARG   A 148 ? 0.1528 0.1337 0.2512 -0.0084 0.0247  0.0209  148 ARG   A CG  
2998 C  CD  . ARG   A 148 ? 0.1637 0.1369 0.2732 -0.0031 0.0343  0.0375  148 ARG   A CD  
2999 N  NE  . ARG   A 148 ? 0.1543 0.1426 0.2696 0.0036  0.0394  0.0443  148 ARG   A NE  
3000 C  CZ  . ARG   A 148 ? 0.1565 0.1322 0.2516 0.0005  0.0371  0.0360  148 ARG   A CZ  
3001 N  NH1 . ARG   A 148 ? 0.1600 0.1360 0.2605 -0.0114 0.0336  0.0089  148 ARG   A NH1 
3002 N  NH2 . ARG   A 148 ? 0.1505 0.1507 0.2516 0.0135  0.0368  0.0471  148 ARG   A NH2 
3016 N  N   . THR   A 149 ? 0.1447 0.1476 0.1995 -0.0156 -0.0066 0.0446  149 THR   A N   
3017 C  CA  . THR   A 149 ? 0.1485 0.1559 0.1980 -0.0137 0.0019  0.0503  149 THR   A CA  
3018 C  C   . THR   A 149 ? 0.1406 0.1545 0.1925 -0.0215 0.0114  0.0499  149 THR   A C   
3019 O  O   . THR   A 149 ? 0.1387 0.1628 0.2022 -0.0213 0.0124  0.0440  149 THR   A O   
3020 C  CB  . THR   A 149 ? 0.1468 0.1666 0.2030 -0.0126 0.0023  0.0407  149 THR   A CB  
3021 O  OG1 . THR   A 149 ? 0.1460 0.1561 0.2116 -0.0268 0.0018  0.0324  149 THR   A OG1 
3022 C  CG2 . THR   A 149 ? 0.1497 0.1806 0.2057 -0.0087 -0.0008 0.0328  149 THR   A CG2 
3030 N  N   . ASN   A 150 ? 0.1464 0.1552 0.1921 -0.0155 0.0033  0.0482  150 ASN   A N   
3031 C  CA  . ASN   A 150 ? 0.1582 0.1649 0.1842 -0.0104 0.0136  0.0451  150 ASN   A CA  
3032 C  C   . ASN   A 150 ? 0.1420 0.1569 0.1872 -0.0153 0.0076  0.0428  150 ASN   A C   
3033 O  O   . ASN   A 150 ? 0.1514 0.1672 0.2265 -0.0170 -0.0079 0.0294  150 ASN   A O   
3034 C  CB  . ASN   A 150 ? 0.2035 0.1907 0.2060 -0.0137 0.0330  0.0681  150 ASN   A CB  
3035 C  CG  . ASN   A 150 ? 0.2529 0.2303 0.2858 -0.0183 0.0104  0.0716  150 ASN   A CG  
3036 O  OD1 . ASN   A 150 ? 0.2704 0.2409 0.3011 -0.0271 0.0034  0.0883  150 ASN   A OD1 
3037 N  ND2 . ASN   A 150 ? 0.2844 0.2491 0.3234 -0.0131 -0.0003 0.0718  150 ASN   A ND2 
3044 N  N   . VAL   A 151 ? 0.1432 0.1444 0.1830 -0.0149 0.0068  0.0406  151 VAL   A N   
3045 C  CA  . VAL   A 151 ? 0.1540 0.1469 0.1794 -0.0190 0.0157  0.0396  151 VAL   A CA  
3046 C  C   . VAL   A 151 ? 0.1437 0.1418 0.1899 -0.0239 0.0149  0.0407  151 VAL   A C   
3047 O  O   . VAL   A 151 ? 0.1534 0.1486 0.2333 -0.0224 0.0069  0.0390  151 VAL   A O   
3048 C  CB  . VAL   A 151 ? 0.1809 0.1651 0.1775 -0.0052 0.0147  0.0410  151 VAL   A CB  
3049 C  CG1 . VAL   A 151 ? 0.1763 0.1851 0.1945 -0.0085 0.0098  0.0381  151 VAL   A CG1 
3050 C  CG2 . VAL   A 151 ? 0.1958 0.1659 0.1878 -0.0056 0.0207  0.0277  151 VAL   A CG2 
3060 N  N   . TYR   A 152 ? 0.1429 0.1430 0.1856 -0.0221 0.0148  0.0328  152 TYR   A N   
3061 C  CA  . TYR   A 152 ? 0.1409 0.1462 0.1753 -0.0180 0.0127  0.0287  152 TYR   A CA  
3062 C  C   . TYR   A 152 ? 0.1343 0.1445 0.1706 -0.0204 0.0196  0.0350  152 TYR   A C   
3063 O  O   . TYR   A 152 ? 0.1438 0.1430 0.1827 -0.0278 0.0184  0.0282  152 TYR   A O   
3064 C  CB  . TYR   A 152 ? 0.1574 0.1520 0.1767 -0.0087 0.0225  0.0275  152 TYR   A CB  
3065 C  CG  . TYR   A 152 ? 0.1734 0.1671 0.1757 -0.0157 0.0347  0.0362  152 TYR   A CG  
3066 C  CD1 . TYR   A 152 ? 0.1840 0.1873 0.1887 -0.0041 0.0314  0.0461  152 TYR   A CD1 
3067 C  CD2 . TYR   A 152 ? 0.1811 0.1776 0.1675 -0.0287 0.0303  0.0317  152 TYR   A CD2 
3068 C  CE1 . TYR   A 152 ? 0.2103 0.1987 0.2062 -0.0028 0.0153  0.0544  152 TYR   A CE1 
3069 C  CE2 . TYR   A 152 ? 0.2020 0.1913 0.1817 -0.0324 0.0276  0.0420  152 TYR   A CE2 
3070 C  CZ  . TYR   A 152 ? 0.2214 0.1975 0.1909 -0.0172 0.0177  0.0558  152 TYR   A CZ  
3071 O  OH  . TYR   A 152 ? 0.2465 0.2214 0.2198 -0.0104 0.0257  0.0670  152 TYR   A OH  
3081 N  N   A LEU   A 153 ? 0.1309 0.1462 0.1850 -0.0209 0.0223  0.0390  153 LEU   A N   
3082 N  N   B LEU   A 153 ? 0.1366 0.1521 0.1614 -0.0157 0.0176  0.0302  153 LEU   A N   
3083 C  CA  A LEU   A 153 ? 0.1258 0.1365 0.2046 -0.0146 0.0205  0.0354  153 LEU   A CA  
3084 C  CA  B LEU   A 153 ? 0.1362 0.1539 0.1539 -0.0051 0.0183  0.0225  153 LEU   A CA  
3085 C  C   A LEU   A 153 ? 0.1323 0.1363 0.2000 -0.0122 0.0292  0.0252  153 LEU   A C   
3086 C  C   B LEU   A 153 ? 0.1390 0.1628 0.1518 -0.0002 0.0163  0.0247  153 LEU   A C   
3087 O  O   A LEU   A 153 ? 0.1363 0.1477 0.2273 -0.0205 0.0351  0.0188  153 LEU   A O   
3088 O  O   B LEU   A 153 ? 0.1345 0.1686 0.1568 -0.0030 0.0149  0.0298  153 LEU   A O   
3089 C  CB  A LEU   A 153 ? 0.1208 0.1344 0.2146 -0.0128 0.0067  0.0351  153 LEU   A CB  
3090 C  CB  B LEU   A 153 ? 0.1371 0.1503 0.1599 0.0037  0.0118  0.0181  153 LEU   A CB  
3091 C  CG  A LEU   A 153 ? 0.1208 0.1424 0.2049 -0.0160 0.0171  0.0286  153 LEU   A CG  
3092 C  CG  B LEU   A 153 ? 0.1414 0.1491 0.1482 0.0111  0.0109  0.0181  153 LEU   A CG  
3093 C  CD1 A LEU   A 153 ? 0.1281 0.1435 0.2092 -0.0128 -0.0039 0.0212  153 LEU   A CD1 
3094 C  CD1 B LEU   A 153 ? 0.1419 0.1471 0.1536 0.0152  0.0103  0.0172  153 LEU   A CD1 
3095 C  CD2 A LEU   A 153 ? 0.1371 0.1512 0.2096 -0.0157 0.0221  0.0058  153 LEU   A CD2 
3096 C  CD2 B LEU   A 153 ? 0.1457 0.1500 0.1554 0.0151  0.0104  0.0144  153 LEU   A CD2 
3119 N  N   A ALA   A 154 ? 0.1324 0.1340 0.2081 -0.0105 0.0300  0.0344  154 ALA   A N   
3120 N  N   B ALA   A 154 ? 0.1473 0.1674 0.1503 0.0041  0.0159  0.0260  154 ALA   A N   
3121 C  CA  A ALA   A 154 ? 0.1393 0.1346 0.2200 -0.0074 0.0326  0.0241  154 ALA   A CA  
3122 C  CA  B ALA   A 154 ? 0.1600 0.1725 0.1612 0.0093  0.0129  0.0246  154 ALA   A CA  
3123 C  C   A ALA   A 154 ? 0.1385 0.1283 0.2248 0.0017  0.0288  0.0279  154 ALA   A C   
3124 C  C   B ALA   A 154 ? 0.1694 0.1755 0.1643 0.0111  0.0084  0.0307  154 ALA   A C   
3125 O  O   A ALA   A 154 ? 0.1457 0.1457 0.2065 -0.0078 0.0198  0.0236  154 ALA   A O   
3126 O  O   B ALA   A 154 ? 0.1710 0.1732 0.1543 0.0089  0.0081  0.0361  154 ALA   A O   
3127 C  CB  A ALA   A 154 ? 0.1514 0.1379 0.2165 0.0024  0.0285  0.0121  154 ALA   A CB  
3128 C  CB  B ALA   A 154 ? 0.1634 0.1739 0.1653 0.0119  0.0070  0.0210  154 ALA   A CB  
3139 N  N   A VAL   A 155 ? 0.1446 0.1275 0.2516 0.0033  0.0226  0.0491  155 VAL   A N   
3140 N  N   B VAL   A 155 ? 0.1809 0.1830 0.1805 0.0098  0.0010  0.0346  155 VAL   A N   
3141 C  CA  A VAL   A 155 ? 0.1483 0.1374 0.2818 -0.0001 0.0119  0.0569  155 VAL   A CA  
3142 C  CA  B VAL   A 155 ? 0.1925 0.1928 0.1956 0.0071  0.0001  0.0363  155 VAL   A CA  
3143 C  C   A VAL   A 155 ? 0.1590 0.1439 0.3159 0.0122  -0.0045 0.0592  155 VAL   A C   
3144 C  C   B VAL   A 155 ? 0.2085 0.2016 0.2227 0.0098  -0.0008 0.0364  155 VAL   A C   
3145 O  O   A VAL   A 155 ? 0.1492 0.1390 0.3264 0.0141  -0.0013 0.0409  155 VAL   A O   
3146 O  O   B VAL   A 155 ? 0.2076 0.2037 0.2154 0.0085  -0.0038 0.0287  155 VAL   A O   
3147 C  CB  A VAL   A 155 ? 0.1468 0.1435 0.2764 0.0029  0.0108  0.0497  155 VAL   A CB  
3148 C  CB  B VAL   A 155 ? 0.1904 0.1963 0.1949 0.0063  0.0036  0.0312  155 VAL   A CB  
3149 C  CG1 A VAL   A 155 ? 0.1610 0.1594 0.2897 0.0048  -0.0037 0.0547  155 VAL   A CG1 
3150 C  CG1 B VAL   A 155 ? 0.1952 0.2013 0.2008 0.0061  -0.0043 0.0357  155 VAL   A CG1 
3151 C  CG2 A VAL   A 155 ? 0.1570 0.1508 0.2730 0.0133  0.0039  0.0458  155 VAL   A CG2 
3152 C  CG2 B VAL   A 155 ? 0.1895 0.1982 0.1859 0.0068  0.0127  0.0252  155 VAL   A CG2 
3171 N  N   A PHE   A 156 ? 0.1744 0.1581 0.3290 0.0073  -0.0105 0.0774  156 PHE   A N   
3172 N  N   B PHE   A 156 ? 0.2240 0.2084 0.2510 0.0102  0.0014  0.0406  156 PHE   A N   
3173 C  CA  A PHE   A 156 ? 0.2003 0.1684 0.3545 0.0139  -0.0085 0.0806  156 PHE   A CA  
3174 C  CA  B PHE   A 156 ? 0.2421 0.2143 0.2712 0.0113  0.0026  0.0379  156 PHE   A CA  
3175 C  C   A PHE   A 156 ? 0.1984 0.1737 0.3590 0.0241  -0.0042 0.0822  156 PHE   A C   
3176 C  C   B PHE   A 156 ? 0.2534 0.2222 0.2967 0.0078  -0.0038 0.0311  156 PHE   A C   
3177 O  O   A PHE   A 156 ? 0.2073 0.1966 0.3785 0.0371  -0.0039 0.0486  156 PHE   A O   
3178 O  O   B PHE   A 156 ? 0.2596 0.2268 0.3119 0.0058  -0.0033 0.0328  156 PHE   A O   
3179 C  CB  A PHE   A 156 ? 0.2247 0.1765 0.3615 0.0099  -0.0161 0.0907  156 PHE   A CB  
3180 C  CB  B PHE   A 156 ? 0.2473 0.2140 0.2652 0.0123  0.0082  0.0364  156 PHE   A CB  
3181 C  CG  A PHE   A 156 ? 0.2534 0.1887 0.3872 0.0215  -0.0328 0.0855  156 PHE   A CG  
3182 C  CG  B PHE   A 156 ? 0.2522 0.2173 0.2663 0.0154  0.0108  0.0317  156 PHE   A CG  
3183 C  CD1 A PHE   A 156 ? 0.2696 0.1997 0.3984 0.0291  -0.0291 0.0700  156 PHE   A CD1 
3184 C  CD1 B PHE   A 156 ? 0.2518 0.2189 0.2708 0.0178  0.0079  0.0234  156 PHE   A CD1 
3185 C  CD2 A PHE   A 156 ? 0.2623 0.1983 0.3901 0.0298  -0.0346 0.1000  156 PHE   A CD2 
3186 C  CD2 B PHE   A 156 ? 0.2590 0.2202 0.2710 0.0140  0.0097  0.0302  156 PHE   A CD2 
3187 C  CE1 A PHE   A 156 ? 0.2802 0.2096 0.4147 0.0313  -0.0198 0.0628  156 PHE   A CE1 
3188 C  CE1 B PHE   A 156 ? 0.2532 0.2207 0.2691 0.0140  0.0088  0.0177  156 PHE   A CE1 
3189 C  CE2 A PHE   A 156 ? 0.2796 0.2115 0.4029 0.0351  -0.0273 0.0828  156 PHE   A CE2 
3190 C  CE2 B PHE   A 156 ? 0.2598 0.2208 0.2738 0.0105  0.0098  0.0261  156 PHE   A CE2 
3191 C  CZ  A PHE   A 156 ? 0.2839 0.2152 0.4185 0.0394  -0.0231 0.0594  156 PHE   A CZ  
3192 C  CZ  B PHE   A 156 ? 0.2570 0.2203 0.2702 0.0083  0.0136  0.0190  156 PHE   A CZ  
3211 N  N   A ASP   A 157 ? 0.1877 0.1655 0.3537 0.0132  0.0018  0.0970  157 ASP   A N   
3212 N  N   B ASP   A 157 ? 0.2583 0.2264 0.3012 0.0036  -0.0125 0.0283  157 ASP   A N   
3213 C  CA  A ASP   A 157 ? 0.1917 0.1816 0.3643 0.0131  0.0041  0.1039  157 ASP   A CA  
3214 C  CA  B ASP   A 157 ? 0.2629 0.2323 0.3058 0.0017  -0.0169 0.0260  157 ASP   A CA  
3215 C  C   A ASP   A 157 ? 0.1746 0.1904 0.3611 0.0250  0.0185  0.1043  157 ASP   A C   
3216 C  C   B ASP   A 157 ? 0.2511 0.2335 0.3054 0.0005  -0.0134 0.0221  157 ASP   A C   
3217 O  O   A ASP   A 157 ? 0.1602 0.1775 0.3427 0.0226  0.0208  0.1053  157 ASP   A O   
3218 O  O   B ASP   A 157 ? 0.2495 0.2312 0.3040 -0.0010 -0.0162 0.0149  157 ASP   A O   
3219 C  CB  A ASP   A 157 ? 0.2087 0.1913 0.3775 0.0217  -0.0229 0.1186  157 ASP   A CB  
3220 C  CB  B ASP   A 157 ? 0.2756 0.2367 0.3173 0.0015  -0.0207 0.0330  157 ASP   A CB  
3221 C  CG  A ASP   A 157 ? 0.2338 0.2066 0.4108 0.0316  -0.0441 0.1176  157 ASP   A CG  
3222 C  CG  B ASP   A 157 ? 0.2881 0.2390 0.3328 0.0056  -0.0264 0.0380  157 ASP   A CG  
3223 O  OD1 A ASP   A 157 ? 0.2657 0.2217 0.4455 0.0233  -0.0628 0.1188  157 ASP   A OD1 
3224 O  OD1 B ASP   A 157 ? 0.2962 0.2373 0.3453 0.0033  -0.0307 0.0406  157 ASP   A OD1 
3225 O  OD2 A ASP   A 157 ? 0.2191 0.1968 0.4301 0.0306  -0.0395 0.1075  157 ASP   A OD2 
3226 O  OD2 B ASP   A 157 ? 0.2892 0.2407 0.3357 0.0077  -0.0281 0.0417  157 ASP   A OD2 
3235 N  N   A LYS   A 158 ? 0.1841 0.2141 0.3806 0.0310  0.0311  0.0951  158 LYS   A N   
3236 N  N   B LYS   A 158 ? 0.2427 0.2378 0.3103 0.0007  -0.0062 0.0222  158 LYS   A N   
3237 C  CA  A LYS   A 158 ? 0.1876 0.2457 0.3939 0.0395  0.0458  0.0950  158 LYS   A CA  
3238 C  CA  B LYS   A 158 ? 0.2358 0.2451 0.3158 0.0032  0.0000  0.0199  158 LYS   A CA  
3239 C  C   A LYS   A 158 ? 0.1749 0.2577 0.3878 0.0437  0.0398  0.1108  158 LYS   A C   
3240 C  C   B LYS   A 158 ? 0.2209 0.2442 0.3102 0.0012  -0.0036 0.0282  158 LYS   A C   
3241 O  O   A LYS   A 158 ? 0.1666 0.2583 0.3925 0.0383  0.0438  0.1218  158 LYS   A O   
3242 O  O   B LYS   A 158 ? 0.2157 0.2369 0.3114 -0.0087 -0.0118 0.0299  158 LYS   A O   
3243 C  CB  A LYS   A 158 ? 0.2098 0.2643 0.4137 0.0363  0.0669  0.0891  158 LYS   A CB  
3244 C  CB  B LYS   A 158 ? 0.2448 0.2530 0.3289 0.0088  0.0081  0.0109  158 LYS   A CB  
3245 C  CG  A LYS   A 158 ? 0.2313 0.2853 0.4344 0.0307  0.0804  0.0905  158 LYS   A CG  
3246 C  CG  B LYS   A 158 ? 0.2533 0.2609 0.3422 0.0132  0.0148  0.0077  158 LYS   A CG  
3247 C  CD  A LYS   A 158 ? 0.2458 0.3047 0.4468 0.0250  0.0991  0.0994  158 LYS   A CD  
3248 C  CD  B LYS   A 158 ? 0.2603 0.2683 0.3540 0.0147  0.0209  0.0041  158 LYS   A CD  
3249 C  CE  A LYS   A 158 ? 0.2562 0.3156 0.4610 0.0234  0.1043  0.1108  158 LYS   A CE  
3250 C  CE  B LYS   A 158 ? 0.2668 0.2725 0.3666 0.0145  0.0231  0.0014  158 LYS   A CE  
3251 N  NZ  A LYS   A 158 ? 0.2638 0.3215 0.4664 0.0225  0.1054  0.1180  158 LYS   A NZ  
3252 N  NZ  B LYS   A 158 ? 0.2671 0.2742 0.3735 0.0152  0.0236  -0.0000 158 LYS   A NZ  
3279 N  N   A ASN   A 159 ? 0.1771 0.2712 0.3977 0.0490  0.0182  0.1082  159 ASN   A N   
3280 N  N   B ASN   A 159 ? 0.2118 0.2513 0.3116 0.0093  0.0020  0.0375  159 ASN   A N   
3281 C  CA  A ASN   A 159 ? 0.1771 0.2839 0.3908 0.0509  -0.0032 0.1170  159 ASN   A CA  
3282 C  CA  B ASN   A 159 ? 0.2013 0.2551 0.3059 0.0160  0.0021  0.0517  159 ASN   A CA  
3283 C  C   A ASN   A 159 ? 0.1594 0.2812 0.3702 0.0347  -0.0025 0.1073  159 ASN   A C   
3284 C  C   B ASN   A 159 ? 0.1795 0.2425 0.2780 0.0048  -0.0033 0.0555  159 ASN   A C   
3285 O  O   A ASN   A 159 ? 0.1437 0.2909 0.3684 0.0327  -0.0157 0.0990  159 ASN   A O   
3286 O  O   B ASN   A 159 ? 0.1720 0.2462 0.2766 0.0023  -0.0064 0.0619  159 ASN   A O   
3287 C  CB  A ASN   A 159 ? 0.2020 0.3029 0.4270 0.0524  -0.0067 0.1260  159 ASN   A CB  
3288 C  CB  B ASN   A 159 ? 0.2124 0.2690 0.3311 0.0280  0.0060  0.0600  159 ASN   A CB  
3289 C  CG  A ASN   A 159 ? 0.2320 0.3222 0.4691 0.0391  -0.0016 0.1217  159 ASN   A CG  
3290 C  CG  B ASN   A 159 ? 0.2235 0.2806 0.3534 0.0312  0.0077  0.0626  159 ASN   A CG  
3291 O  OD1 A ASN   A 159 ? 0.2371 0.3362 0.4902 0.0298  0.0105  0.1144  159 ASN   A OD1 
3292 O  OD1 B ASN   A 159 ? 0.2224 0.2851 0.3594 0.0274  0.0170  0.0634  159 ASN   A OD1 
3293 N  ND2 A ASN   A 159 ? 0.2411 0.3256 0.4836 0.0355  -0.0042 0.1179  159 ASN   A ND2 
3294 N  ND2 B ASN   A 159 ? 0.2282 0.2846 0.3655 0.0350  0.0006  0.0606  159 ASN   A ND2 
3307 N  N   A LEU   A 160 ? 0.1499 0.2626 0.3496 0.0273  -0.0188 0.1024  160 LEU   A N   
3308 N  N   B LEU   A 160 ? 0.1642 0.2266 0.2562 -0.0027 -0.0116 0.0558  160 LEU   A N   
3309 C  CA  A LEU   A 160 ? 0.1570 0.2462 0.3326 0.0167  -0.0055 0.0940  160 LEU   A CA  
3310 C  CA  B LEU   A 160 ? 0.1606 0.2162 0.2381 -0.0066 -0.0038 0.0572  160 LEU   A CA  
3311 C  C   A LEU   A 160 ? 0.1421 0.2354 0.3218 0.0118  0.0080  0.0851  160 LEU   A C   
3312 C  C   B LEU   A 160 ? 0.1544 0.2131 0.2366 -0.0023 0.0057  0.0648  160 LEU   A C   
3313 O  O   A LEU   A 160 ? 0.1455 0.2399 0.3453 0.0079  0.0044  0.0797  160 LEU   A O   
3314 O  O   B LEU   A 160 ? 0.1547 0.2114 0.2458 -0.0037 0.0114  0.0639  160 LEU   A O   
3315 C  CB  A LEU   A 160 ? 0.1764 0.2501 0.3209 0.0078  0.0051  0.0941  160 LEU   A CB  
3316 C  CB  B LEU   A 160 ? 0.1606 0.2123 0.2265 -0.0115 -0.0028 0.0539  160 LEU   A CB  
3317 C  CG  A LEU   A 160 ? 0.1928 0.2583 0.3228 -0.0040 0.0241  0.0812  160 LEU   A CG  
3318 C  CG  B LEU   A 160 ? 0.1665 0.2130 0.2169 -0.0144 -0.0002 0.0465  160 LEU   A CG  
3319 C  CD1 A LEU   A 160 ? 0.2047 0.2642 0.3275 -0.0062 0.0271  0.0686  160 LEU   A CD1 
3320 C  CD1 B LEU   A 160 ? 0.1677 0.2096 0.2106 -0.0191 0.0050  0.0473  160 LEU   A CD1 
3321 C  CD2 A LEU   A 160 ? 0.1991 0.2591 0.3301 -0.0110 0.0335  0.0771  160 LEU   A CD2 
3322 C  CD2 B LEU   A 160 ? 0.1706 0.2163 0.2210 -0.0143 0.0042  0.0377  160 LEU   A CD2 
3345 N  N   A TYR   A 161 ? 0.1381 0.2196 0.3071 0.0173  0.0112  0.0782  161 TYR   A N   
3346 N  N   B TYR   A 161 ? 0.1514 0.2120 0.2380 0.0020  0.0121  0.0698  161 TYR   A N   
3347 C  CA  A TYR   A 161 ? 0.1417 0.2086 0.3072 0.0129  0.0142  0.0731  161 TYR   A CA  
3348 C  CA  B TYR   A 161 ? 0.1524 0.2138 0.2501 0.0057  0.0151  0.0736  161 TYR   A CA  
3349 C  C   A TYR   A 161 ? 0.1397 0.2158 0.3178 0.0121  0.0175  0.0637  161 TYR   A C   
3350 C  C   B TYR   A 161 ? 0.1440 0.2178 0.2719 0.0081  0.0159  0.0710  161 TYR   A C   
3351 O  O   A TYR   A 161 ? 0.1367 0.2180 0.3313 0.0072  0.0195  0.0589  161 TYR   A O   
3352 O  O   B TYR   A 161 ? 0.1391 0.2153 0.2528 0.0039  0.0154  0.0822  161 TYR   A O   
3353 C  CB  A TYR   A 161 ? 0.1537 0.2001 0.3156 0.0069  0.0183  0.0703  161 TYR   A CB  
3354 C  CB  B TYR   A 161 ? 0.1602 0.2122 0.2437 0.0079  0.0235  0.0746  161 TYR   A CB  
3355 C  CG  A TYR   A 161 ? 0.1548 0.1928 0.3232 0.0014  0.0087  0.0670  161 TYR   A CG  
3356 C  CG  B TYR   A 161 ? 0.1629 0.2096 0.2457 0.0088  0.0226  0.0729  161 TYR   A CG  
3357 C  CD1 A TYR   A 161 ? 0.1542 0.1898 0.3305 -0.0056 0.0036  0.0613  161 TYR   A CD1 
3358 C  CD1 B TYR   A 161 ? 0.1657 0.2102 0.2467 0.0108  0.0187  0.0710  161 TYR   A CD1 
3359 C  CD2 A TYR   A 161 ? 0.1562 0.1944 0.3179 0.0019  -0.0018 0.0688  161 TYR   A CD2 
3360 C  CD2 B TYR   A 161 ? 0.1638 0.2071 0.2458 0.0072  0.0252  0.0747  161 TYR   A CD2 
3361 C  CE1 A TYR   A 161 ? 0.1604 0.1845 0.3366 -0.0055 -0.0005 0.0693  161 TYR   A CE1 
3362 C  CE1 B TYR   A 161 ? 0.1681 0.2109 0.2465 0.0125  0.0161  0.0732  161 TYR   A CE1 
3363 C  CE2 A TYR   A 161 ? 0.1629 0.1873 0.3285 -0.0051 0.0002  0.0741  161 TYR   A CE2 
3364 C  CE2 B TYR   A 161 ? 0.1662 0.2064 0.2484 0.0080  0.0274  0.0774  161 TYR   A CE2 
3365 C  CZ  A TYR   A 161 ? 0.1726 0.1804 0.3422 -0.0129 -0.0032 0.0807  161 TYR   A CZ  
3366 C  CZ  B TYR   A 161 ? 0.1757 0.2098 0.2531 0.0095  0.0225  0.0756  161 TYR   A CZ  
3367 O  OH  A TYR   A 161 ? 0.1878 0.1728 0.3716 -0.0237 -0.0163 0.0902  161 TYR   A OH  
3368 O  OH  B TYR   A 161 ? 0.1898 0.2117 0.2669 0.0093  0.0221  0.0741  161 TYR   A OH  
3387 N  N   . ASP   A 162 ? 0.1407 0.2259 0.3192 0.0116  0.0197  0.0633  162 ASP   A N   
3388 C  CA  . ASP   A 162 ? 0.1369 0.2512 0.3345 0.0070  0.0277  0.0619  162 ASP   A CA  
3389 C  C   . ASP   A 162 ? 0.1361 0.2638 0.3320 0.0028  0.0249  0.0697  162 ASP   A C   
3390 O  O   . ASP   A 162 ? 0.1377 0.2527 0.3583 -0.0018 0.0332  0.0618  162 ASP   A O   
3391 C  CB  . ASP   A 162 ? 0.1487 0.2607 0.3632 0.0090  0.0368  0.0558  162 ASP   A CB  
3392 C  CG  . ASP   A 162 ? 0.1664 0.2776 0.3869 0.0170  0.0434  0.0510  162 ASP   A CG  
3393 O  OD1 . ASP   A 162 ? 0.1778 0.2890 0.3947 0.0071  0.0427  0.0488  162 ASP   A OD1 
3394 O  OD2 . ASP   A 162 ? 0.1892 0.2842 0.4142 0.0343  0.0435  0.0446  162 ASP   A OD2 
3400 N  N   A LYS   A 163 ? 0.1403 0.2844 0.3419 -0.0012 0.0010  0.0703  163 LYS   A N   
3401 N  N   B LYS   A 163 ? 0.1466 0.2778 0.3275 -0.0025 0.0143  0.0666  163 LYS   A N   
3402 C  CA  A LYS   A 163 ? 0.1497 0.2995 0.3379 -0.0040 -0.0024 0.0703  163 LYS   A CA  
3403 C  CA  B LYS   A 163 ? 0.1592 0.2882 0.3245 -0.0079 0.0121  0.0603  163 LYS   A CA  
3404 C  C   A LYS   A 163 ? 0.1426 0.2879 0.3337 -0.0117 0.0198  0.0675  163 LYS   A C   
3405 C  C   B LYS   A 163 ? 0.1468 0.2784 0.3167 -0.0136 0.0190  0.0622  163 LYS   A C   
3406 O  O   A LYS   A 163 ? 0.1446 0.3042 0.3569 -0.0151 0.0111  0.0478  163 LYS   A O   
3407 O  O   B LYS   A 163 ? 0.1484 0.2859 0.3191 -0.0156 0.0130  0.0544  163 LYS   A O   
3408 C  CB  A LYS   A 163 ? 0.1830 0.3260 0.3625 0.0036  -0.0267 0.0675  163 LYS   A CB  
3409 C  CB  B LYS   A 163 ? 0.1887 0.3072 0.3447 -0.0069 0.0008  0.0498  163 LYS   A CB  
3410 C  CG  A LYS   A 163 ? 0.2246 0.3514 0.4001 0.0023  -0.0194 0.0650  163 LYS   A CG  
3411 C  CG  B LYS   A 163 ? 0.2182 0.3244 0.3719 -0.0092 0.0021  0.0410  163 LYS   A CG  
3412 C  CD  A LYS   A 163 ? 0.2582 0.3738 0.4363 0.0002  -0.0164 0.0611  163 LYS   A CD  
3413 C  CD  B LYS   A 163 ? 0.2435 0.3390 0.3983 -0.0111 0.0010  0.0344  163 LYS   A CD  
3414 C  CE  A LYS   A 163 ? 0.2738 0.3885 0.4654 -0.0040 -0.0120 0.0590  163 LYS   A CE  
3415 C  CE  B LYS   A 163 ? 0.2554 0.3490 0.4196 -0.0149 0.0017  0.0297  163 LYS   A CE  
3416 N  NZ  A LYS   A 163 ? 0.2789 0.3986 0.4816 -0.0082 -0.0110 0.0584  163 LYS   A NZ  
3417 N  NZ  B LYS   A 163 ? 0.2614 0.3553 0.4314 -0.0177 0.0005  0.0280  163 LYS   A NZ  
3444 N  N   . LEU   A 164 ? 0.1294 0.2612 0.3186 -0.0180 0.0183  0.0655  164 LEU   A N   
3445 C  CA  . LEU   A 164 ? 0.1317 0.2337 0.3098 -0.0182 0.0274  0.0596  164 LEU   A CA  
3446 C  C   . LEU   A 164 ? 0.1426 0.2270 0.3120 -0.0191 0.0376  0.0630  164 LEU   A C   
3447 O  O   . LEU   A 164 ? 0.1579 0.2369 0.3141 -0.0187 0.0565  0.0422  164 LEU   A O   
3448 C  CB  . LEU   A 164 ? 0.1272 0.2243 0.3036 -0.0232 0.0262  0.0560  164 LEU   A CB  
3449 C  CG  . LEU   A 164 ? 0.1391 0.2241 0.3134 -0.0162 0.0154  0.0531  164 LEU   A CG  
3450 C  CD1 . LEU   A 164 ? 0.1326 0.2296 0.3160 -0.0044 0.0127  0.0353  164 LEU   A CD1 
3451 C  CD2 . LEU   A 164 ? 0.1598 0.2272 0.3086 -0.0211 0.0257  0.0479  164 LEU   A CD2 
3464 N  N   . VAL   A 165 ? 0.1451 0.2289 0.3110 -0.0194 0.0341  0.0623  165 VAL   A N   
3465 C  CA  . VAL   A 165 ? 0.1497 0.2273 0.3037 -0.0201 0.0400  0.0659  165 VAL   A CA  
3466 C  C   . VAL   A 165 ? 0.1425 0.2338 0.3087 -0.0152 0.0380  0.0609  165 VAL   A C   
3467 O  O   . VAL   A 165 ? 0.1454 0.2331 0.2901 -0.0149 0.0358  0.0561  165 VAL   A O   
3468 C  CB  . VAL   A 165 ? 0.1745 0.2259 0.3060 -0.0198 0.0406  0.0523  165 VAL   A CB  
3469 C  CG1 . VAL   A 165 ? 0.1807 0.2280 0.3085 -0.0209 0.0395  0.0443  165 VAL   A CG1 
3470 C  CG2 . VAL   A 165 ? 0.1937 0.2269 0.3217 -0.0194 0.0351  0.0502  165 VAL   A CG2 
3480 N  N   . SER   A 166 ? 0.1295 0.2488 0.3327 -0.0140 0.0423  0.0604  166 SER   A N   
3481 C  CA  . SER   A 166 ? 0.1317 0.2742 0.3534 -0.0144 0.0339  0.0491  166 SER   A CA  
3482 C  C   . SER   A 166 ? 0.1357 0.2980 0.3535 -0.0179 0.0174  0.0342  166 SER   A C   
3483 O  O   . SER   A 166 ? 0.1610 0.3127 0.4026 -0.0336 0.0277  0.0062  166 SER   A O   
3484 C  CB  . SER   A 166 ? 0.1492 0.2875 0.3876 0.0008  0.0205  0.0398  166 SER   A CB  
3485 O  OG  . SER   A 166 ? 0.1929 0.3013 0.4126 -0.0069 0.0318  0.0537  166 SER   A OG  
3491 N  N   . SER   A 167 ? 0.1414 0.3067 0.3153 -0.0018 0.0068  0.0356  167 SER   A N   
3492 C  CA  . SER   A 167 ? 0.1671 0.3224 0.3008 0.0047  -0.0130 0.0268  167 SER   A CA  
3493 C  C   . SER   A 167 ? 0.1677 0.3278 0.2924 0.0156  -0.0092 0.0170  167 SER   A C   
3494 O  O   . SER   A 167 ? 0.1857 0.3348 0.3020 0.0182  -0.0216 0.0162  167 SER   A O   
3495 C  CB  . SER   A 167 ? 0.1830 0.3341 0.3171 0.0044  -0.0067 0.0309  167 SER   A CB  
3496 O  OG  . SER   A 167 ? 0.1831 0.3411 0.3159 0.0003  0.0167  0.0308  167 SER   A OG  
3502 N  N   . PHE   A 168 ? 0.1553 0.3247 0.2748 0.0233  -0.0010 0.0076  168 PHE   A N   
3503 C  CA  . PHE   A 168 ? 0.1606 0.3188 0.2830 0.0107  0.0112  0.0007  168 PHE   A CA  
3504 C  C   . PHE   A 168 ? 0.1756 0.3474 0.3222 -0.0094 0.0600  -0.0320 168 PHE   A C   
3505 O  O   . PHE   A 168 ? 0.1765 0.3510 0.3554 -0.0254 0.0592  -0.0271 168 PHE   A O   
3506 C  CB  . PHE   A 168 ? 0.1632 0.2878 0.2663 0.0064  -0.0087 0.0155  168 PHE   A CB  
3507 C  CG  . PHE   A 168 ? 0.1585 0.2606 0.2569 -0.0047 -0.0171 0.0250  168 PHE   A CG  
3508 C  CD1 . PHE   A 168 ? 0.1608 0.2613 0.2701 -0.0106 -0.0151 0.0423  168 PHE   A CD1 
3509 C  CD2 . PHE   A 168 ? 0.1617 0.2470 0.2463 -0.0004 0.0004  0.0293  168 PHE   A CD2 
3510 C  CE1 . PHE   A 168 ? 0.1525 0.2583 0.2651 -0.0108 -0.0066 0.0500  168 PHE   A CE1 
3511 C  CE2 . PHE   A 168 ? 0.1646 0.2410 0.2477 0.0021  0.0085  0.0460  168 PHE   A CE2 
3512 C  CZ  . PHE   A 168 ? 0.1592 0.2479 0.2508 -0.0047 0.0038  0.0491  168 PHE   A CZ  
3522 N  N   . LEU   A 169 ? 0.2372 0.3800 0.3815 -0.0289 0.0642  -0.0513 169 LEU   A N   
3523 C  CA  . LEU   A 169 ? 0.3331 0.4241 0.4823 -0.0307 0.0146  -0.0642 169 LEU   A CA  
3524 C  C   . LEU   A 169 ? 0.3621 0.4347 0.5220 -0.0309 -0.0012 -0.0621 169 LEU   A C   
3525 O  O   . LEU   A 169 ? 0.3885 0.4374 0.5412 -0.0305 -0.0010 -0.0615 169 LEU   A O   
3526 C  CB  . LEU   A 169 ? 0.3905 0.4524 0.5350 -0.0313 -0.0107 -0.0701 169 LEU   A CB  
3527 C  CG  . LEU   A 169 ? 0.4242 0.4705 0.5707 -0.0338 -0.0285 -0.0763 169 LEU   A CG  
3528 C  CD1 . LEU   A 169 ? 0.4428 0.4767 0.5859 -0.0331 -0.0323 -0.0756 169 LEU   A CD1 
3529 C  CD2 . LEU   A 169 ? 0.4350 0.4760 0.5798 -0.0362 -0.0334 -0.0790 169 LEU   A CD2 
3530 O  OXT . LEU   A 169 ? 0.3584 0.4378 0.5316 -0.0300 -0.0028 -0.0617 169 LEU   A OXT 
3542 N  N   A SER   B 1   ? 0.3511 0.3528 0.3873 -0.1055 -0.0655 0.0650  1   SER   B N   
3543 N  N   B SER   B 1   ? 0.3381 0.3313 0.3512 -0.0529 -0.0343 0.0267  1   SER   B N   
3544 C  CA  A SER   B 1   ? 0.3365 0.3523 0.3776 -0.1107 -0.0754 0.0653  1   SER   B CA  
3545 C  CA  B SER   B 1   ? 0.3330 0.3313 0.3444 -0.0541 -0.0360 0.0271  1   SER   B CA  
3546 C  C   A SER   B 1   ? 0.3059 0.3495 0.3500 -0.1115 -0.0905 0.0802  1   SER   B C   
3547 C  C   B SER   B 1   ? 0.3221 0.3315 0.3345 -0.0518 -0.0406 0.0342  1   SER   B C   
3548 O  O   A SER   B 1   ? 0.3119 0.3478 0.3258 -0.1050 -0.0906 0.0787  1   SER   B O   
3549 O  O   B SER   B 1   ? 0.3247 0.3306 0.3250 -0.0498 -0.0435 0.0332  1   SER   B O   
3550 C  CB  A SER   B 1   ? 0.3485 0.3518 0.4044 -0.1103 -0.0606 0.0500  1   SER   B CB  
3551 C  CB  B SER   B 1   ? 0.3366 0.3295 0.3539 -0.0557 -0.0286 0.0186  1   SER   B CB  
3552 O  OG  A SER   B 1   ? 0.3627 0.3606 0.4390 -0.1064 -0.0468 0.0397  1   SER   B OG  
3553 O  OG  B SER   B 1   ? 0.3409 0.3307 0.3633 -0.0569 -0.0227 0.0135  1   SER   B OG  
3568 N  N   A MET   B 2   ? 0.2804 0.3476 0.3502 -0.1076 -0.0902 0.1132  2   MET   B N   
3569 N  N   B MET   B 2   ? 0.3108 0.3320 0.3361 -0.0489 -0.0377 0.0479  2   MET   B N   
3570 C  CA  A MET   B 2   ? 0.2666 0.3468 0.3645 -0.0841 -0.0859 0.1292  2   MET   B CA  
3571 C  CA  B MET   B 2   ? 0.3003 0.3307 0.3366 -0.0411 -0.0328 0.0570  2   MET   B CA  
3572 C  C   A MET   B 2   ? 0.2307 0.3206 0.3364 -0.0674 -0.0877 0.1506  2   MET   B C   
3573 C  C   B MET   B 2   ? 0.2771 0.3109 0.3041 -0.0364 -0.0271 0.0633  2   MET   B C   
3574 O  O   A MET   B 2   ? 0.2193 0.3316 0.3410 -0.0563 -0.0978 0.1570  2   MET   B O   
3575 O  O   B MET   B 2   ? 0.2777 0.3150 0.3071 -0.0348 -0.0224 0.0621  2   MET   B O   
3576 C  CB  A MET   B 2   ? 0.2986 0.3788 0.4386 -0.0624 -0.0752 0.1053  2   MET   B CB  
3577 C  CB  B MET   B 2   ? 0.3146 0.3491 0.3793 -0.0345 -0.0337 0.0556  2   MET   B CB  
3578 C  CG  A MET   B 2   ? 0.3270 0.4080 0.5151 -0.0425 -0.0632 0.0915  2   MET   B CG  
3579 C  CG  B MET   B 2   ? 0.3265 0.3641 0.4200 -0.0287 -0.0333 0.0575  2   MET   B CG  
3580 S  SD  A MET   B 2   ? 0.3550 0.4350 0.5827 -0.0272 -0.0507 0.0740  2   MET   B SD  
3581 S  SD  B MET   B 2   ? 0.3378 0.3774 0.4560 -0.0230 -0.0327 0.0581  2   MET   B SD  
3582 C  CE  A MET   B 2   ? 0.3547 0.4377 0.5838 -0.0267 -0.0436 0.0726  2   MET   B CE  
3583 C  CE  B MET   B 2   ? 0.3366 0.3775 0.4606 -0.0234 -0.0319 0.0542  2   MET   B CE  
3602 N  N   A VAL   B 3   ? 0.2074 0.2807 0.3126 -0.0715 -0.0753 0.1538  3   VAL   B N   
3603 N  N   B VAL   B 3   ? 0.2527 0.2858 0.2724 -0.0353 -0.0261 0.0681  3   VAL   B N   
3604 C  CA  A VAL   B 3   ? 0.2005 0.2440 0.3114 -0.0660 -0.0643 0.1311  3   VAL   B CA  
3605 C  CA  B VAL   B 3   ? 0.2309 0.2602 0.2501 -0.0319 -0.0290 0.0682  3   VAL   B CA  
3606 C  C   A VAL   B 3   ? 0.1829 0.2329 0.2701 -0.0578 -0.0672 0.1124  3   VAL   B C   
3607 C  C   B VAL   B 3   ? 0.2034 0.2408 0.2272 -0.0329 -0.0402 0.0754  3   VAL   B C   
3608 O  O   A VAL   B 3   ? 0.1815 0.2401 0.2885 -0.0581 -0.0696 0.1163  3   VAL   B O   
3609 O  O   B VAL   B 3   ? 0.2038 0.2460 0.2125 -0.0196 -0.0357 0.0708  3   VAL   B O   
3610 C  CB  A VAL   B 3   ? 0.2240 0.2380 0.3499 -0.0619 -0.0562 0.1160  3   VAL   B CB  
3611 C  CB  B VAL   B 3   ? 0.2393 0.2565 0.2528 -0.0284 -0.0240 0.0636  3   VAL   B CB  
3612 C  CG1 A VAL   B 3   ? 0.2315 0.2320 0.3630 -0.0600 -0.0596 0.1074  3   VAL   B CG1 
3613 C  CG1 B VAL   B 3   ? 0.2422 0.2545 0.2565 -0.0290 -0.0242 0.0603  3   VAL   B CG1 
3614 C  CG2 A VAL   B 3   ? 0.2324 0.2449 0.3686 -0.0565 -0.0532 0.1140  3   VAL   B CG2 
3615 C  CG2 B VAL   B 3   ? 0.2427 0.2561 0.2518 -0.0258 -0.0240 0.0621  3   VAL   B CG2 
3634 N  N   . ASN   B 4   ? 0.1798 0.2170 0.2311 -0.0479 -0.0588 0.0899  4   ASN   B N   
3635 C  CA  . ASN   B 4   ? 0.1802 0.2148 0.2014 -0.0509 -0.0554 0.0503  4   ASN   B CA  
3636 C  C   . ASN   B 4   ? 0.1953 0.2262 0.1912 -0.0487 -0.0431 0.0374  4   ASN   B C   
3637 O  O   . ASN   B 4   ? 0.1945 0.2343 0.2158 -0.0439 -0.0262 0.0138  4   ASN   B O   
3638 C  CB  . ASN   B 4   ? 0.1755 0.2065 0.1915 -0.0442 -0.0628 0.0443  4   ASN   B CB  
3639 C  CG  . ASN   B 4   ? 0.1754 0.1907 0.1797 -0.0476 -0.0513 0.0380  4   ASN   B CG  
3640 O  OD1 . ASN   B 4   ? 0.1795 0.1738 0.1680 -0.0433 -0.0513 0.0285  4   ASN   B OD1 
3641 N  ND2 . ASN   B 4   ? 0.1974 0.1995 0.1814 -0.0236 -0.0348 0.0335  4   ASN   B ND2 
3649 N  N   . SER   B 5   ? 0.2123 0.2414 0.2024 -0.0500 -0.0208 0.0345  5   SER   B N   
3650 C  CA  . SER   B 5   ? 0.2366 0.2752 0.2264 -0.0390 0.0043  0.0364  5   SER   B CA  
3651 C  C   . SER   B 5   ? 0.2482 0.2783 0.2640 -0.0512 0.0251  0.0364  5   SER   B C   
3652 O  O   . SER   B 5   ? 0.2579 0.2790 0.3343 -0.0462 0.0488  0.0386  5   SER   B O   
3653 C  CB  . SER   B 5   ? 0.2505 0.3011 0.2510 -0.0313 0.0104  0.0502  5   SER   B CB  
3654 O  OG  . SER   B 5   ? 0.2741 0.3248 0.2994 -0.0216 0.0152  0.0574  5   SER   B OG  
3660 N  N   . PHE   B 6   ? 0.2631 0.2935 0.2315 -0.0562 0.0385  0.0317  6   PHE   B N   
3661 C  CA  . PHE   B 6   ? 0.2735 0.2926 0.1998 -0.0743 0.0419  0.0132  6   PHE   B CA  
3662 C  C   . PHE   B 6   ? 0.3169 0.3181 0.2411 -0.0786 0.0648  -0.0133 6   PHE   B C   
3663 O  O   . PHE   B 6   ? 0.3315 0.3473 0.2847 -0.0687 0.0470  -0.0295 6   PHE   B O   
3664 C  CB  . PHE   B 6   ? 0.2461 0.2720 0.1887 -0.0722 0.0145  0.0115  6   PHE   B CB  
3665 C  CG  . PHE   B 6   ? 0.2119 0.2425 0.1703 -0.0690 0.0068  0.0101  6   PHE   B CG  
3666 C  CD1 . PHE   B 6   ? 0.2133 0.2161 0.1545 -0.0596 -0.0113 0.0085  6   PHE   B CD1 
3667 C  CD2 . PHE   B 6   ? 0.1893 0.2408 0.1728 -0.0588 0.0135  0.0299  6   PHE   B CD2 
3668 C  CE1 . PHE   B 6   ? 0.2054 0.1970 0.1671 -0.0531 -0.0068 0.0024  6   PHE   B CE1 
3669 C  CE2 . PHE   B 6   ? 0.1937 0.2274 0.2014 -0.0439 0.0116  0.0241  6   PHE   B CE2 
3670 C  CZ  . PHE   B 6   ? 0.1984 0.2042 0.1787 -0.0435 0.0103  0.0075  6   PHE   B CZ  
3680 N  N   . SER   B 7   ? 0.3492 0.3030 0.2523 -0.1014 0.0847  -0.0421 7   SER   B N   
3681 C  CA  . SER   B 7   ? 0.3826 0.3168 0.2967 -0.1001 0.1000  -0.0499 7   SER   B CA  
3682 C  C   . SER   B 7   ? 0.3817 0.3036 0.2996 -0.1042 0.1200  -0.0506 7   SER   B C   
3683 O  O   . SER   B 7   ? 0.3895 0.3066 0.3183 -0.1061 0.1320  -0.0444 7   SER   B O   
3684 C  CB  . SER   B 7   ? 0.4031 0.3302 0.3474 -0.0965 0.1123  -0.0478 7   SER   B CB  
3685 O  OG  . SER   B 7   ? 0.4159 0.3385 0.3991 -0.0959 0.1150  -0.0339 7   SER   B OG  
3691 N  N   . GLY   B 8   ? 0.3764 0.2855 0.3093 -0.0950 0.1196  -0.0531 8   GLY   B N   
3692 C  CA  . GLY   B 8   ? 0.3592 0.2676 0.3199 -0.0900 0.1232  -0.0574 8   GLY   B CA  
3693 C  C   . GLY   B 8   ? 0.3372 0.2451 0.3044 -0.0870 0.1308  -0.0500 8   GLY   B C   
3694 O  O   . GLY   B 8   ? 0.3450 0.2508 0.3352 -0.0749 0.1353  -0.0557 8   GLY   B O   
3698 N  N   . TYR   B 9   ? 0.3170 0.2300 0.2745 -0.0791 0.1057  -0.0560 9   TYR   B N   
3699 C  CA  . TYR   B 9   ? 0.2939 0.2053 0.2382 -0.0631 0.0756  -0.0481 9   TYR   B CA  
3700 C  C   . TYR   B 9   ? 0.2876 0.2077 0.2145 -0.0558 0.0413  -0.0377 9   TYR   B C   
3701 O  O   . TYR   B 9   ? 0.3029 0.2341 0.2509 -0.0597 0.0419  -0.0179 9   TYR   B O   
3702 C  CB  . TYR   B 9   ? 0.2867 0.1878 0.2405 -0.0504 0.0707  -0.0450 9   TYR   B CB  
3703 C  CG  . TYR   B 9   ? 0.2769 0.1728 0.2393 -0.0518 0.0687  -0.0517 9   TYR   B CG  
3704 C  CD1 . TYR   B 9   ? 0.2812 0.1700 0.2498 -0.0673 0.0691  -0.0539 9   TYR   B CD1 
3705 C  CD2 . TYR   B 9   ? 0.2593 0.1660 0.2238 -0.0493 0.0656  -0.0540 9   TYR   B CD2 
3706 C  CE1 . TYR   B 9   ? 0.2725 0.1830 0.2526 -0.0734 0.0730  -0.0589 9   TYR   B CE1 
3707 C  CE2 . TYR   B 9   ? 0.2579 0.1697 0.2431 -0.0483 0.0637  -0.0505 9   TYR   B CE2 
3708 C  CZ  . TYR   B 9   ? 0.2591 0.1844 0.2593 -0.0614 0.0688  -0.0647 9   TYR   B CZ  
3709 O  OH  . TYR   B 9   ? 0.2538 0.1944 0.2784 -0.0719 0.0637  -0.0716 9   TYR   B OH  
3719 N  N   . LEU   B 10  ? 0.2637 0.1834 0.2012 -0.0506 0.0160  -0.0367 10  LEU   B N   
3720 C  CA  . LEU   B 10  ? 0.2571 0.1786 0.2072 -0.0543 -0.0091 -0.0355 10  LEU   B CA  
3721 C  C   . LEU   B 10  ? 0.2391 0.1766 0.1990 -0.0472 -0.0216 -0.0313 10  LEU   B C   
3722 O  O   . LEU   B 10  ? 0.2246 0.1789 0.1959 -0.0328 -0.0169 -0.0250 10  LEU   B O   
3723 C  CB  . LEU   B 10  ? 0.2714 0.1767 0.2242 -0.0588 -0.0211 -0.0219 10  LEU   B CB  
3724 C  CG  . LEU   B 10  ? 0.2917 0.1854 0.2559 -0.0488 -0.0406 -0.0081 10  LEU   B CG  
3725 C  CD1 . LEU   B 10  ? 0.3027 0.1976 0.2701 -0.0441 -0.0388 -0.0094 10  LEU   B CD1 
3726 C  CD2 . LEU   B 10  ? 0.3016 0.1919 0.2873 -0.0475 -0.0328 0.0094  10  LEU   B CD2 
3738 N  N   . LYS   B 11  ? 0.2528 0.1974 0.2042 -0.0420 -0.0200 -0.0238 11  LYS   B N   
3739 C  CA  . LYS   B 11  ? 0.2728 0.2253 0.2323 -0.0283 -0.0270 -0.0230 11  LYS   B CA  
3740 C  C   . LYS   B 11  ? 0.2604 0.2075 0.2325 -0.0440 -0.0349 -0.0368 11  LYS   B C   
3741 O  O   . LYS   B 11  ? 0.2730 0.2265 0.2600 -0.0619 -0.0406 -0.0680 11  LYS   B O   
3742 C  CB  . LYS   B 11  ? 0.3021 0.2766 0.2769 -0.0038 -0.0263 -0.0110 11  LYS   B CB  
3743 C  CG  . LYS   B 11  ? 0.3312 0.3098 0.3436 0.0084  -0.0294 -0.0071 11  LYS   B CG  
3744 C  CD  . LYS   B 11  ? 0.3551 0.3342 0.4031 0.0148  -0.0300 -0.0106 11  LYS   B CD  
3745 C  CE  . LYS   B 11  ? 0.3707 0.3510 0.4466 0.0163  -0.0235 -0.0110 11  LYS   B CE  
3746 N  NZ  . LYS   B 11  ? 0.3795 0.3625 0.4744 0.0168  -0.0186 -0.0098 11  LYS   B NZ  
3760 N  N   . LEU   B 12  ? 0.2262 0.1825 0.2254 -0.0375 -0.0318 -0.0449 12  LEU   B N   
3761 C  CA  . LEU   B 12  ? 0.2144 0.1655 0.2427 -0.0359 -0.0207 -0.0389 12  LEU   B CA  
3762 C  C   . LEU   B 12  ? 0.2020 0.1685 0.2602 -0.0391 -0.0374 -0.0317 12  LEU   B C   
3763 O  O   . LEU   B 12  ? 0.1989 0.1741 0.2814 -0.0517 -0.0513 -0.0260 12  LEU   B O   
3764 C  CB  . LEU   B 12  ? 0.2140 0.1457 0.2406 -0.0251 -0.0048 -0.0431 12  LEU   B CB  
3765 C  CG  . LEU   B 12  ? 0.2151 0.1460 0.2568 -0.0280 -0.0050 -0.0370 12  LEU   B CG  
3766 C  CD1 . LEU   B 12  ? 0.2252 0.1521 0.2542 -0.0177 -0.0024 -0.0227 12  LEU   B CD1 
3767 C  CD2 . LEU   B 12  ? 0.2239 0.1534 0.2776 -0.0331 -0.0124 -0.0409 12  LEU   B CD2 
3779 N  N   . THR   B 13  ? 0.1990 0.1739 0.2636 -0.0346 -0.0432 -0.0373 13  THR   B N   
3780 C  CA  . THR   B 13  ? 0.1990 0.1781 0.2536 -0.0461 -0.0547 -0.0313 13  THR   B CA  
3781 C  C   . THR   B 13  ? 0.2393 0.1941 0.2673 -0.0550 -0.0641 -0.0223 13  THR   B C   
3782 O  O   . THR   B 13  ? 0.2557 0.1997 0.2850 -0.0562 -0.0251 -0.0210 13  THR   B O   
3783 C  CB  . THR   B 13  ? 0.1812 0.1840 0.2618 -0.0469 -0.0490 -0.0205 13  THR   B CB  
3784 O  OG1 . THR   B 13  ? 0.1739 0.1733 0.2627 -0.0392 -0.0342 -0.0203 13  THR   B OG1 
3785 C  CG2 . THR   B 13  ? 0.1946 0.1906 0.2692 -0.0386 -0.0384 -0.0116 13  THR   B CG2 
3793 N  N   A ASP   B 14  ? 0.2566 0.2011 0.2784 -0.0561 -0.0931 -0.0114 14  ASP   B N   
3794 N  N   B ASP   B 14  ? 0.2502 0.2026 0.2777 -0.0536 -0.0711 -0.0137 14  ASP   B N   
3795 C  CA  A ASP   B 14  ? 0.2673 0.2215 0.3119 -0.0561 -0.1006 0.0122  14  ASP   B CA  
3796 C  CA  B ASP   B 14  ? 0.2561 0.2143 0.2951 -0.0511 -0.0729 -0.0005 14  ASP   B CA  
3797 C  C   A ASP   B 14  ? 0.2527 0.2069 0.2711 -0.0601 -0.0818 0.0144  14  ASP   B C   
3798 C  C   B ASP   B 14  ? 0.2415 0.2011 0.2645 -0.0512 -0.0719 0.0022  14  ASP   B C   
3799 O  O   A ASP   B 14  ? 0.2790 0.2223 0.2792 -0.0619 -0.0760 0.0306  14  ASP   B O   
3800 O  O   B ASP   B 14  ? 0.2518 0.2061 0.2651 -0.0506 -0.0740 0.0018  14  ASP   B O   
3801 C  CB  A ASP   B 14  ? 0.2906 0.2563 0.3904 -0.0491 -0.1124 0.0168  14  ASP   B CB  
3802 C  CB  B ASP   B 14  ? 0.2738 0.2370 0.3439 -0.0456 -0.0714 0.0035  14  ASP   B CB  
3803 C  CG  A ASP   B 14  ? 0.3168 0.2874 0.4642 -0.0420 -0.1119 0.0111  14  ASP   B CG  
3804 C  CG  B ASP   B 14  ? 0.2908 0.2556 0.3848 -0.0398 -0.0669 0.0019  14  ASP   B CG  
3805 O  OD1 A ASP   B 14  ? 0.3304 0.3011 0.4834 -0.0446 -0.1113 -0.0008 14  ASP   B OD1 
3806 O  OD1 B ASP   B 14  ? 0.2962 0.2631 0.3961 -0.0399 -0.0629 -0.0023 14  ASP   B OD1 
3807 O  OD2 A ASP   B 14  ? 0.3242 0.2987 0.4989 -0.0386 -0.1107 0.0161  14  ASP   B OD2 
3808 O  OD2 B ASP   B 14  ? 0.2982 0.2627 0.4021 -0.0388 -0.0693 0.0038  14  ASP   B OD2 
3817 N  N   . ASN   B 15  ? 0.2199 0.1844 0.2415 -0.0464 -0.0722 0.0042  15  ASN   B N   
3818 C  CA  . ASN   B 15  ? 0.1814 0.1610 0.2251 -0.0300 -0.0456 -0.0033 15  ASN   B CA  
3819 C  C   . ASN   B 15  ? 0.1611 0.1515 0.2090 -0.0191 -0.0332 -0.0091 15  ASN   B C   
3820 O  O   . ASN   B 15  ? 0.1573 0.1492 0.2376 -0.0222 -0.0431 -0.0184 15  ASN   B O   
3821 C  CB  . ASN   B 15  ? 0.1779 0.1526 0.2361 -0.0112 -0.0390 -0.0058 15  ASN   B CB  
3822 C  CG  . ASN   B 15  ? 0.1572 0.1517 0.2466 -0.0186 -0.0223 -0.0027 15  ASN   B CG  
3823 O  OD1 . ASN   B 15  ? 0.1618 0.1794 0.2850 -0.0393 -0.0314 -0.0017 15  ASN   B OD1 
3824 N  ND2 . ASN   B 15  ? 0.1593 0.1312 0.2407 -0.0133 0.0005  -0.0084 15  ASN   B ND2 
3832 N  N   . VAL   B 16  ? 0.1642 0.1436 0.2071 -0.0238 -0.0385 -0.0024 16  VAL   B N   
3833 C  CA  . VAL   B 16  ? 0.1658 0.1455 0.1978 -0.0201 -0.0353 -0.0243 16  VAL   B CA  
3834 C  C   . VAL   B 16  ? 0.1614 0.1521 0.1994 -0.0285 -0.0345 -0.0192 16  VAL   B C   
3835 O  O   . VAL   B 16  ? 0.1617 0.1639 0.2205 -0.0259 -0.0249 -0.0353 16  VAL   B O   
3836 C  CB  . VAL   B 16  ? 0.1706 0.1417 0.2049 -0.0126 -0.0260 -0.0237 16  VAL   B CB  
3837 C  CG1 . VAL   B 16  ? 0.1830 0.1423 0.2095 0.0035  -0.0263 -0.0095 16  VAL   B CG1 
3838 C  CG2 . VAL   B 16  ? 0.1723 0.1432 0.2281 -0.0090 -0.0111 -0.0191 16  VAL   B CG2 
3848 N  N   . TYR   B 17  ? 0.1618 0.1553 0.2048 -0.0227 -0.0276 -0.0262 17  TYR   B N   
3849 C  CA  . TYR   B 17  ? 0.1729 0.1696 0.2049 -0.0228 -0.0245 -0.0084 17  TYR   B CA  
3850 C  C   . TYR   B 17  ? 0.1667 0.1487 0.1936 -0.0330 -0.0162 -0.0140 17  TYR   B C   
3851 O  O   . TYR   B 17  ? 0.1663 0.1488 0.2162 -0.0285 -0.0245 -0.0351 17  TYR   B O   
3852 C  CB  . TYR   B 17  ? 0.2037 0.2082 0.2124 -0.0120 -0.0238 0.0255  17  TYR   B CB  
3853 C  CG  . TYR   B 17  ? 0.2307 0.2438 0.2456 -0.0061 -0.0291 0.0304  17  TYR   B CG  
3854 C  CD1 . TYR   B 17  ? 0.2468 0.2562 0.2557 -0.0009 -0.0384 0.0378  17  TYR   B CD1 
3855 C  CD2 . TYR   B 17  ? 0.2578 0.2736 0.2703 0.0048  -0.0341 0.0209  17  TYR   B CD2 
3856 C  CE1 . TYR   B 17  ? 0.2666 0.2818 0.2704 0.0100  -0.0503 0.0315  17  TYR   B CE1 
3857 C  CE2 . TYR   B 17  ? 0.2742 0.2936 0.2867 0.0156  -0.0474 0.0231  17  TYR   B CE2 
3858 C  CZ  . TYR   B 17  ? 0.2810 0.2978 0.2839 0.0185  -0.0580 0.0271  17  TYR   B CZ  
3859 O  OH  . TYR   B 17  ? 0.2983 0.3174 0.3044 0.0257  -0.0685 0.0311  17  TYR   B OH  
3869 N  N   . ILE   B 18  ? 0.1762 0.1510 0.1706 -0.0281 -0.0102 -0.0228 18  ILE   B N   
3870 C  CA  . ILE   B 18  ? 0.1795 0.1464 0.1793 -0.0292 -0.0085 -0.0254 18  ILE   B CA  
3871 C  C   . ILE   B 18  ? 0.1851 0.1468 0.1836 -0.0349 -0.0045 -0.0329 18  ILE   B C   
3872 O  O   . ILE   B 18  ? 0.2036 0.1661 0.1868 -0.0282 0.0077  -0.0421 18  ILE   B O   
3873 C  CB  . ILE   B 18  ? 0.1847 0.1473 0.1906 -0.0374 -0.0099 -0.0129 18  ILE   B CB  
3874 C  CG1 . ILE   B 18  ? 0.1861 0.1491 0.2010 -0.0311 0.0000  -0.0046 18  ILE   B CG1 
3875 C  CG2 . ILE   B 18  ? 0.1880 0.1545 0.2042 -0.0400 -0.0158 -0.0027 18  ILE   B CG2 
3876 C  CD1 . ILE   B 18  ? 0.1956 0.1753 0.2308 -0.0301 -0.0135 0.0132  18  ILE   B CD1 
3888 N  N   . LYS   B 19  ? 0.1832 0.1460 0.1999 -0.0213 0.0298  -0.0316 19  LYS   B N   
3889 C  CA  . LYS   B 19  ? 0.1903 0.1588 0.2125 -0.0240 0.0269  -0.0390 19  LYS   B CA  
3890 C  C   . LYS   B 19  ? 0.1764 0.1531 0.2210 -0.0201 0.0314  -0.0513 19  LYS   B C   
3891 O  O   . LYS   B 19  ? 0.1778 0.1567 0.2138 -0.0134 0.0246  -0.0476 19  LYS   B O   
3892 C  CB  . LYS   B 19  ? 0.2091 0.1820 0.2270 -0.0304 0.0391  -0.0301 19  LYS   B CB  
3893 C  CG  . LYS   B 19  ? 0.2348 0.2001 0.2453 -0.0369 0.0492  -0.0288 19  LYS   B CG  
3894 C  CD  . LYS   B 19  ? 0.2613 0.2270 0.2559 -0.0470 0.0522  -0.0188 19  LYS   B CD  
3895 C  CE  . LYS   B 19  ? 0.2869 0.2535 0.2739 -0.0479 0.0438  -0.0200 19  LYS   B CE  
3896 N  NZ  . LYS   B 19  ? 0.3044 0.2713 0.2905 -0.0538 0.0503  -0.0191 19  LYS   B NZ  
3910 N  N   . ASN   B 20  ? 0.1761 0.1565 0.2557 -0.0133 0.0360  -0.0571 20  ASN   B N   
3911 C  CA  . ASN   B 20  ? 0.1759 0.1732 0.2830 -0.0079 0.0392  -0.0669 20  ASN   B CA  
3912 C  C   . ASN   B 20  ? 0.1737 0.1886 0.2895 -0.0115 0.0450  -0.0760 20  ASN   B C   
3913 O  O   . ASN   B 20  ? 0.1969 0.2248 0.3072 -0.0255 0.0506  -0.0703 20  ASN   B O   
3914 C  CB  . ASN   B 20  ? 0.2014 0.1782 0.3076 0.0059  0.0282  -0.0630 20  ASN   B CB  
3915 C  CG  . ASN   B 20  ? 0.2317 0.1820 0.3292 0.0343  0.0211  -0.0712 20  ASN   B CG  
3916 O  OD1 . ASN   B 20  ? 0.2613 0.2085 0.3549 0.0548  0.0218  -0.0698 20  ASN   B OD1 
3917 N  ND2 . ASN   B 20  ? 0.2251 0.1797 0.3200 0.0310  0.0082  -0.0769 20  ASN   B ND2 
3924 N  N   . ALA   B 21  ? 0.1738 0.1703 0.2926 -0.0189 0.0455  -0.0625 21  ALA   B N   
3925 C  CA  . ALA   B 21  ? 0.1853 0.1797 0.2987 -0.0226 0.0342  -0.0436 21  ALA   B CA  
3926 C  C   . ALA   B 21  ? 0.1923 0.1587 0.2860 -0.0185 0.0412  -0.0330 21  ALA   B C   
3927 O  O   . ALA   B 21  ? 0.1901 0.1480 0.2969 -0.0282 0.0369  -0.0316 21  ALA   B O   
3928 C  CB  . ALA   B 21  ? 0.2001 0.2088 0.3037 -0.0349 0.0342  -0.0277 21  ALA   B CB  
3934 N  N   . ASP   B 22  ? 0.1872 0.1508 0.2622 -0.0223 0.0363  -0.0210 22  ASP   B N   
3935 C  CA  . ASP   B 22  ? 0.1834 0.1427 0.2415 -0.0099 0.0196  -0.0178 22  ASP   B CA  
3936 C  C   . ASP   B 22  ? 0.1765 0.1413 0.1985 -0.0113 0.0036  -0.0041 22  ASP   B C   
3937 O  O   . ASP   B 22  ? 0.1772 0.1400 0.2073 -0.0052 0.0040  -0.0022 22  ASP   B O   
3938 C  CB  . ASP   B 22  ? 0.1873 0.1519 0.2893 -0.0113 0.0277  0.0022  22  ASP   B CB  
3939 C  CG  . ASP   B 22  ? 0.1925 0.1661 0.3284 -0.0021 -0.0058 0.0028  22  ASP   B CG  
3940 O  OD1 . ASP   B 22  ? 0.2088 0.1596 0.3298 0.0058  -0.0172 0.0052  22  ASP   B OD1 
3941 O  OD2 . ASP   B 22  ? 0.1983 0.1986 0.3800 0.0070  -0.0290 -0.0121 22  ASP   B OD2 
3946 N  N   . ILE   B 23  ? 0.1749 0.1380 0.1962 -0.0063 -0.0024 0.0145  23  ILE   B N   
3947 C  CA  . ILE   B 23  ? 0.1646 0.1393 0.1870 -0.0070 -0.0042 0.0049  23  ILE   B CA  
3948 C  C   . ILE   B 23  ? 0.1544 0.1379 0.1760 -0.0051 -0.0057 -0.0010 23  ILE   B C   
3949 O  O   . ILE   B 23  ? 0.1551 0.1306 0.1794 -0.0059 -0.0057 0.0077  23  ILE   B O   
3950 C  CB  . ILE   B 23  ? 0.1614 0.1423 0.2010 -0.0151 0.0079  0.0173  23  ILE   B CB  
3951 C  CG1 . ILE   B 23  ? 0.1646 0.1514 0.2161 -0.0114 0.0123  0.0241  23  ILE   B CG1 
3952 C  CG2 . ILE   B 23  ? 0.1670 0.1602 0.2111 -0.0125 0.0044  0.0064  23  ILE   B CG2 
3953 C  CD1 . ILE   B 23  ? 0.1713 0.1675 0.2148 -0.0072 0.0171  0.0120  23  ILE   B CD1 
3965 N  N   . VAL   B 24  ? 0.1507 0.1421 0.1910 -0.0088 -0.0040 0.0018  24  VAL   B N   
3966 C  CA  . VAL   B 24  ? 0.1466 0.1456 0.2032 -0.0057 -0.0127 -0.0011 24  VAL   B CA  
3967 C  C   . VAL   B 24  ? 0.1466 0.1456 0.2158 -0.0105 -0.0096 0.0069  24  VAL   B C   
3968 O  O   . VAL   B 24  ? 0.1494 0.1521 0.2241 -0.0114 -0.0069 0.0118  24  VAL   B O   
3969 C  CB  . VAL   B 24  ? 0.1630 0.1623 0.2141 0.0031  -0.0205 -0.0062 24  VAL   B CB  
3970 C  CG1 . VAL   B 24  ? 0.1626 0.1658 0.2443 -0.0020 -0.0151 -0.0057 24  VAL   B CG1 
3971 C  CG2 . VAL   B 24  ? 0.1775 0.1930 0.2089 0.0104  -0.0231 -0.0129 24  VAL   B CG2 
3981 N  N   . GLU   B 25  ? 0.1752 0.1584 0.2280 -0.0149 -0.0023 0.0005  25  GLU   B N   
3982 C  CA  . GLU   B 25  ? 0.1853 0.1888 0.2333 -0.0003 0.0073  -0.0043 25  GLU   B CA  
3983 C  C   . GLU   B 25  ? 0.1792 0.1765 0.2024 -0.0104 0.0127  0.0018  25  GLU   B C   
3984 O  O   . GLU   B 25  ? 0.1834 0.1923 0.2226 -0.0090 0.0251  0.0063  25  GLU   B O   
3985 C  CB  . GLU   B 25  ? 0.2083 0.2360 0.2903 0.0181  0.0172  -0.0000 25  GLU   B CB  
3986 C  CG  . GLU   B 25  ? 0.2440 0.2920 0.3787 0.0226  0.0143  -0.0084 25  GLU   B CG  
3987 C  CD  . GLU   B 25  ? 0.2911 0.3366 0.4528 0.0146  0.0082  -0.0152 25  GLU   B CD  
3988 O  OE1 . GLU   B 25  ? 0.2995 0.3553 0.4858 0.0197  0.0165  -0.0176 25  GLU   B OE1 
3989 O  OE2 . GLU   B 25  ? 0.2981 0.3514 0.4912 0.0096  -0.0001 -0.0228 25  GLU   B OE2 
3996 N  N   A GLU   B 26  ? 0.1772 0.1688 0.1817 -0.0242 0.0070  0.0029  26  GLU   B N   
3997 N  N   B GLU   B 26  ? 0.1768 0.1775 0.1942 -0.0200 0.0107  0.0053  26  GLU   B N   
3998 C  CA  A GLU   B 26  ? 0.1780 0.1769 0.2043 -0.0339 -0.0127 0.0043  26  GLU   B CA  
3999 C  CA  B GLU   B 26  ? 0.1776 0.1819 0.2037 -0.0267 0.0039  0.0096  26  GLU   B CA  
4000 C  C   A GLU   B 26  ? 0.1650 0.1730 0.1971 -0.0208 0.0006  0.0127  26  GLU   B C   
4001 C  C   B GLU   B 26  ? 0.1642 0.1722 0.1942 -0.0199 0.0066  0.0140  26  GLU   B C   
4002 O  O   A GLU   B 26  ? 0.1822 0.1949 0.1964 -0.0154 0.0007  0.0223  26  GLU   B O   
4003 O  O   B GLU   B 26  ? 0.1726 0.1804 0.1919 -0.0162 0.0047  0.0179  26  GLU   B O   
4004 C  CB  A GLU   B 26  ? 0.2050 0.1985 0.2373 -0.0474 -0.0131 0.0082  26  GLU   B CB  
4005 C  CB  B GLU   B 26  ? 0.1968 0.1976 0.2264 -0.0362 0.0084  0.0152  26  GLU   B CB  
4006 C  CG  A GLU   B 26  ? 0.2453 0.2323 0.2787 -0.0448 0.0007  -0.0143 26  GLU   B CG  
4007 C  CG  B GLU   B 26  ? 0.2184 0.2182 0.2526 -0.0389 0.0216  0.0128  26  GLU   B CG  
4008 C  CD  A GLU   B 26  ? 0.2706 0.2521 0.2933 -0.0578 0.0088  -0.0496 26  GLU   B CD  
4009 C  CD  B GLU   B 26  ? 0.2319 0.2347 0.2682 -0.0495 0.0386  0.0117  26  GLU   B CD  
4010 O  OE1 A GLU   B 26  ? 0.2912 0.2399 0.2964 -0.0661 0.0469  -0.0526 26  GLU   B OE1 
4011 O  OE1 B GLU   B 26  ? 0.2430 0.2303 0.2598 -0.0553 0.0690  0.0300  26  GLU   B OE1 
4012 O  OE2 A GLU   B 26  ? 0.2719 0.2861 0.3204 -0.0497 0.0012  -0.0438 26  GLU   B OE2 
4013 O  OE2 B GLU   B 26  ? 0.2308 0.2530 0.2888 -0.0495 0.0352  0.0117  26  GLU   B OE2 
4026 N  N   . ALA   B 27  ? 0.1471 0.1578 0.1903 -0.0199 0.0089  0.0154  27  ALA   B N   
4027 C  CA  . ALA   B 27  ? 0.1529 0.1529 0.2138 -0.0109 0.0028  0.0238  27  ALA   B CA  
4028 C  C   . ALA   B 27  ? 0.1556 0.1625 0.2363 -0.0105 0.0125  0.0409  27  ALA   B C   
4029 O  O   . ALA   B 27  ? 0.1675 0.1659 0.2367 -0.0004 0.0039  0.0394  27  ALA   B O   
4030 C  CB  . ALA   B 27  ? 0.1675 0.1348 0.2165 -0.0128 -0.0017 0.0166  27  ALA   B CB  
4037 N  N   . LYS   B 28  ? 0.1496 0.1846 0.2660 -0.0156 0.0205  0.0665  28  LYS   B N   
4038 C  CA  . LYS   B 28  ? 0.1667 0.2206 0.2848 -0.0097 0.0396  0.0886  28  LYS   B CA  
4039 C  C   . LYS   B 28  ? 0.1906 0.2432 0.2674 -0.0024 0.0574  0.0754  28  LYS   B C   
4040 O  O   . LYS   B 28  ? 0.2169 0.2501 0.2832 -0.0002 0.0626  0.0744  28  LYS   B O   
4041 C  CB  . LYS   B 28  ? 0.1810 0.2489 0.3269 -0.0032 0.0557  0.1020  28  LYS   B CB  
4042 C  CG  . LYS   B 28  ? 0.2066 0.2953 0.3674 0.0048  0.0583  0.1035  28  LYS   B CG  
4043 C  CD  . LYS   B 28  ? 0.2438 0.3424 0.4197 0.0103  0.0729  0.0984  28  LYS   B CD  
4044 C  CE  . LYS   B 28  ? 0.2643 0.3666 0.4577 0.0206  0.0739  0.0975  28  LYS   B CE  
4045 N  NZ  . LYS   B 28  ? 0.2829 0.3734 0.4839 0.0296  0.0750  0.1055  28  LYS   B NZ  
4059 N  N   . LYS   B 29  ? 0.2102 0.2612 0.2659 0.0171  0.0583  0.0599  29  LYS   B N   
4060 C  CA  . LYS   B 29  ? 0.2510 0.2902 0.2894 0.0201  0.0540  0.0612  29  LYS   B CA  
4061 C  C   . LYS   B 29  ? 0.2467 0.2976 0.2581 0.0203  0.0487  0.0730  29  LYS   B C   
4062 O  O   . LYS   B 29  ? 0.2628 0.3242 0.2716 0.0277  0.0486  0.0744  29  LYS   B O   
4063 C  CB  . LYS   B 29  ? 0.3013 0.3213 0.3696 0.0176  0.0485  0.0501  29  LYS   B CB  
4064 C  CG  . LYS   B 29  ? 0.3471 0.3463 0.4396 0.0133  0.0491  0.0512  29  LYS   B CG  
4065 C  CD  . LYS   B 29  ? 0.3801 0.3617 0.5041 0.0072  0.0572  0.0478  29  LYS   B CD  
4066 C  CE  . LYS   B 29  ? 0.3953 0.3695 0.5483 0.0036  0.0645  0.0447  29  LYS   B CE  
4067 N  NZ  . LYS   B 29  ? 0.3975 0.3757 0.5713 0.0018  0.0645  0.0423  29  LYS   B NZ  
4081 N  N   . VAL   B 30  ? 0.2182 0.2810 0.2412 0.0075  0.0404  0.0769  30  VAL   B N   
4082 C  CA  . VAL   B 30  ? 0.2011 0.2744 0.2756 0.0013  0.0065  0.0799  30  VAL   B CA  
4083 C  C   . VAL   B 30  ? 0.1706 0.2673 0.2686 -0.0033 0.0156  0.1016  30  VAL   B C   
4084 O  O   . VAL   B 30  ? 0.1857 0.2903 0.2716 0.0049  0.0213  0.1166  30  VAL   B O   
4085 C  CB  . VAL   B 30  ? 0.2092 0.2722 0.3191 -0.0112 -0.0177 0.0665  30  VAL   B CB  
4086 C  CG1 . VAL   B 30  ? 0.2109 0.2769 0.3217 -0.0175 -0.0166 0.0646  30  VAL   B CG1 
4087 C  CG2 . VAL   B 30  ? 0.2219 0.2704 0.3346 -0.0155 -0.0284 0.0495  30  VAL   B CG2 
4097 N  N   . LYS   B 31  ? 0.1641 0.2303 0.3086 -0.0184 0.0088  0.1037  31  LYS   B N   
4098 C  CA  . LYS   B 31  ? 0.1563 0.2191 0.3377 -0.0340 0.0044  0.1134  31  LYS   B CA  
4099 C  C   . LYS   B 31  ? 0.1525 0.1858 0.2917 -0.0362 -0.0191 0.0962  31  LYS   B C   
4100 O  O   . LYS   B 31  ? 0.1659 0.2087 0.3076 -0.0281 -0.0141 0.1091  31  LYS   B O   
4101 C  CB  . LYS   B 31  ? 0.1767 0.2608 0.3988 -0.0290 0.0231  0.1218  31  LYS   B CB  
4102 C  CG  . LYS   B 31  ? 0.2069 0.3041 0.4430 -0.0245 0.0411  0.1126  31  LYS   B CG  
4103 C  CD  . LYS   B 31  ? 0.2297 0.3373 0.4736 -0.0138 0.0392  0.0960  31  LYS   B CD  
4104 C  CE  . LYS   B 31  ? 0.2460 0.3544 0.4941 -0.0050 0.0294  0.0846  31  LYS   B CE  
4105 N  NZ  . LYS   B 31  ? 0.2610 0.3602 0.5079 0.0068  0.0132  0.0716  31  LYS   B NZ  
4119 N  N   . PRO   B 32  ? 0.1618 0.1532 0.2328 -0.0335 -0.0416 0.0534  32  PRO   B N   
4120 C  CA  . PRO   B 32  ? 0.1691 0.1486 0.1940 -0.0323 -0.0406 0.0372  32  PRO   B CA  
4121 C  C   . PRO   B 32  ? 0.1781 0.1414 0.2010 -0.0349 -0.0502 0.0338  32  PRO   B C   
4122 O  O   . PRO   B 32  ? 0.1923 0.1428 0.2278 -0.0367 -0.0706 0.0362  32  PRO   B O   
4123 C  CB  . PRO   B 32  ? 0.1838 0.1488 0.1888 -0.0310 -0.0313 0.0233  32  PRO   B CB  
4124 C  CG  . PRO   B 32  ? 0.1971 0.1362 0.2075 -0.0330 -0.0498 0.0240  32  PRO   B CG  
4125 C  CD  . PRO   B 32  ? 0.1868 0.1419 0.2272 -0.0276 -0.0578 0.0321  32  PRO   B CD  
4133 N  N   . THR   B 33  ? 0.1810 0.1346 0.1762 -0.0275 -0.0505 0.0218  33  THR   B N   
4134 C  CA  . THR   B 33  ? 0.1852 0.1424 0.1737 -0.0350 -0.0485 0.0233  33  THR   B CA  
4135 C  C   . THR   B 33  ? 0.1893 0.1335 0.1616 -0.0300 -0.0515 0.0162  33  THR   B C   
4136 O  O   . THR   B 33  ? 0.2153 0.1361 0.1652 -0.0363 -0.0588 0.0170  33  THR   B O   
4137 C  CB  . THR   B 33  ? 0.1959 0.1491 0.1826 -0.0174 -0.0574 0.0316  33  THR   B CB  
4138 O  OG1 . THR   B 33  ? 0.1848 0.1574 0.1866 -0.0195 -0.0494 0.0352  33  THR   B OG1 
4139 C  CG2 . THR   B 33  ? 0.2179 0.1545 0.2102 -0.0052 -0.0580 0.0217  33  THR   B CG2 
4147 N  N   . VAL   B 34  ? 0.1762 0.1296 0.1499 -0.0299 -0.0404 0.0120  34  VAL   B N   
4148 C  CA  . VAL   B 34  ? 0.1615 0.1284 0.1447 -0.0254 -0.0311 0.0079  34  VAL   B CA  
4149 C  C   . VAL   B 34  ? 0.1486 0.1201 0.1428 -0.0230 -0.0149 0.0020  34  VAL   B C   
4150 O  O   . VAL   B 34  ? 0.1671 0.1238 0.1390 -0.0199 -0.0287 0.0034  34  VAL   B O   
4151 C  CB  . VAL   B 34  ? 0.1685 0.1379 0.1699 -0.0092 -0.0287 0.0027  34  VAL   B CB  
4152 C  CG1 . VAL   B 34  ? 0.1657 0.1534 0.1684 0.0007  -0.0126 -0.0015 34  VAL   B CG1 
4153 C  CG2 . VAL   B 34  ? 0.1782 0.1392 0.2034 -0.0055 -0.0286 0.0075  34  VAL   B CG2 
4163 N  N   . VAL   B 35  ? 0.1389 0.1208 0.1351 -0.0219 -0.0087 0.0030  35  VAL   B N   
4164 C  CA  . VAL   B 35  ? 0.1363 0.1189 0.1386 -0.0188 -0.0072 0.0038  35  VAL   B CA  
4165 C  C   . VAL   B 35  ? 0.1308 0.1133 0.1320 -0.0154 -0.0104 -0.0012 35  VAL   B C   
4166 O  O   . VAL   B 35  ? 0.1322 0.1210 0.1274 -0.0186 -0.0002 -0.0045 35  VAL   B O   
4167 C  CB  . VAL   B 35  ? 0.1348 0.1388 0.1489 -0.0144 0.0034  0.0034  35  VAL   B CB  
4168 C  CG1 . VAL   B 35  ? 0.1238 0.1474 0.1654 -0.0164 -0.0051 0.0030  35  VAL   B CG1 
4169 C  CG2 . VAL   B 35  ? 0.1356 0.1359 0.1726 -0.0024 0.0034  0.0054  35  VAL   B CG2 
4179 N  N   . VAL   B 36  ? 0.1322 0.1114 0.1330 -0.0147 -0.0130 0.0130  36  VAL   B N   
4180 C  CA  . VAL   B 36  ? 0.1236 0.1104 0.1362 -0.0103 -0.0122 0.0078  36  VAL   B CA  
4181 C  C   . VAL   B 36  ? 0.1267 0.1107 0.1291 -0.0142 -0.0029 0.0059  36  VAL   B C   
4182 O  O   . VAL   B 36  ? 0.1308 0.1207 0.1453 -0.0107 -0.0014 -0.0044 36  VAL   B O   
4183 C  CB  . VAL   B 36  ? 0.1190 0.1177 0.1543 -0.0097 -0.0059 0.0063  36  VAL   B CB  
4184 C  CG1 . VAL   B 36  ? 0.1214 0.1338 0.1597 -0.0180 -0.0039 0.0065  36  VAL   B CG1 
4185 C  CG2 . VAL   B 36  ? 0.1322 0.1271 0.1638 -0.0145 -0.0195 0.0098  36  VAL   B CG2 
4195 N  N   . ASN   B 37  ? 0.1267 0.1177 0.1245 -0.0038 -0.0046 0.0064  37  ASN   B N   
4196 C  CA  . ASN   B 37  ? 0.1257 0.1195 0.1442 0.0043  -0.0131 0.0119  37  ASN   B CA  
4197 C  C   . ASN   B 37  ? 0.1256 0.1252 0.1428 0.0040  -0.0069 0.0009  37  ASN   B C   
4198 O  O   . ASN   B 37  ? 0.1373 0.1298 0.1302 -0.0023 -0.0026 0.0092  37  ASN   B O   
4199 C  CB  . ASN   B 37  ? 0.1270 0.1236 0.1352 -0.0009 -0.0170 0.0083  37  ASN   B CB  
4200 C  CG  . ASN   B 37  ? 0.1284 0.1227 0.1467 -0.0018 -0.0126 0.0055  37  ASN   B CG  
4201 O  OD1 . ASN   B 37  ? 0.1368 0.1275 0.1543 0.0067  -0.0107 0.0013  37  ASN   B OD1 
4202 N  ND2 . ASN   B 37  ? 0.1341 0.1204 0.1502 -0.0007 -0.0181 0.0096  37  ASN   B ND2 
4209 N  N   . ALA   B 38  ? 0.1291 0.1167 0.1395 0.0059  -0.0011 0.0005  38  ALA   B N   
4210 C  CA  . ALA   B 38  ? 0.1375 0.1181 0.1399 0.0007  0.0074  0.0075  38  ALA   B CA  
4211 C  C   . ALA   B 38  ? 0.1348 0.1186 0.1593 -0.0017 0.0037  0.0077  38  ALA   B C   
4212 O  O   . ALA   B 38  ? 0.1463 0.1320 0.1578 0.0022  -0.0006 0.0117  38  ALA   B O   
4213 C  CB  . ALA   B 38  ? 0.1569 0.1306 0.1488 -0.0093 0.0125  0.0097  38  ALA   B CB  
4219 N  N   . ALA   B 39  ? 0.1370 0.1278 0.1284 0.0064  -0.0038 0.0009  39  ALA   B N   
4220 C  CA  . ALA   B 39  ? 0.1457 0.1299 0.1291 0.0043  -0.0067 0.0124  39  ALA   B CA  
4221 C  C   . ALA   B 39  ? 0.1448 0.1398 0.1244 0.0055  -0.0072 0.0000  39  ALA   B C   
4222 O  O   . ALA   B 39  ? 0.1505 0.1464 0.1477 0.0016  -0.0020 0.0078  39  ALA   B O   
4223 C  CB  . ALA   B 39  ? 0.1521 0.1340 0.1467 -0.0035 -0.0002 0.0053  39  ALA   B CB  
4229 N  N   . ASN   B 40  ? 0.1474 0.1611 0.1334 -0.0077 0.0025  -0.0058 40  ASN   B N   
4230 C  CA  . ASN   B 40  ? 0.1565 0.1666 0.1399 -0.0039 -0.0001 -0.0088 40  ASN   B CA  
4231 C  C   . ASN   B 40  ? 0.1622 0.1620 0.1186 0.0011  -0.0051 -0.0047 40  ASN   B C   
4232 O  O   . ASN   B 40  ? 0.1639 0.1506 0.1364 0.0088  -0.0067 0.0005  40  ASN   B O   
4233 C  CB  . ASN   B 40  ? 0.1714 0.1673 0.1694 0.0054  -0.0169 0.0194  40  ASN   B CB  
4234 C  CG  . ASN   B 40  ? 0.1764 0.1700 0.1890 0.0028  -0.0195 0.0210  40  ASN   B CG  
4235 O  OD1 . ASN   B 40  ? 0.1676 0.1612 0.2648 0.0025  -0.0358 0.0167  40  ASN   B OD1 
4236 N  ND2 . ASN   B 40  ? 0.1829 0.1728 0.1966 0.0048  -0.0125 0.0255  40  ASN   B ND2 
4243 N  N   . VAL   B 41  ? 0.1672 0.1653 0.1265 0.0085  0.0030  0.0015  41  VAL   B N   
4244 C  CA  . VAL   B 41  ? 0.1734 0.1831 0.1364 0.0110  -0.0019 -0.0096 41  VAL   B CA  
4245 C  C   . VAL   B 41  ? 0.1706 0.1822 0.1324 0.0201  -0.0011 -0.0117 41  VAL   B C   
4246 O  O   . VAL   B 41  ? 0.1697 0.1780 0.1457 0.0151  -0.0053 -0.0179 41  VAL   B O   
4247 C  CB  . VAL   B 41  ? 0.1869 0.1981 0.1641 -0.0033 0.0198  -0.0199 41  VAL   B CB  
4248 C  CG1 . VAL   B 41  ? 0.1848 0.2067 0.1670 -0.0067 0.0345  -0.0223 41  VAL   B CG1 
4249 C  CG2 . VAL   B 41  ? 0.1983 0.2161 0.1839 -0.0064 0.0268  -0.0187 41  VAL   B CG2 
4259 N  N   . TYR   B 42  ? 0.1807 0.1814 0.1453 0.0185  -0.0227 -0.0002 42  TYR   B N   
4260 C  CA  . TYR   B 42  ? 0.1875 0.1873 0.1519 0.0183  -0.0276 -0.0148 42  TYR   B CA  
4261 C  C   . TYR   B 42  ? 0.1698 0.1669 0.1556 0.0160  -0.0220 -0.0184 42  TYR   B C   
4262 O  O   . TYR   B 42  ? 0.1722 0.1732 0.1868 0.0150  -0.0283 -0.0250 42  TYR   B O   
4263 C  CB  . TYR   B 42  ? 0.2159 0.2165 0.1706 0.0151  -0.0335 -0.0063 42  TYR   B CB  
4264 C  CG  . TYR   B 42  ? 0.2177 0.2374 0.1668 0.0097  -0.0287 0.0059  42  TYR   B CG  
4265 C  CD1 . TYR   B 42  ? 0.2115 0.2381 0.1521 0.0095  -0.0214 -0.0058 42  TYR   B CD1 
4266 C  CD2 . TYR   B 42  ? 0.2344 0.2529 0.2105 0.0058  -0.0163 0.0106  42  TYR   B CD2 
4267 C  CE1 . TYR   B 42  ? 0.2267 0.2526 0.1546 0.0114  -0.0145 -0.0115 42  TYR   B CE1 
4268 C  CE2 . TYR   B 42  ? 0.2375 0.2609 0.2062 0.0105  -0.0024 0.0161  42  TYR   B CE2 
4269 C  CZ  . TYR   B 42  ? 0.2457 0.2699 0.1851 0.0239  0.0004  0.0003  42  TYR   B CZ  
4270 O  OH  . TYR   B 42  ? 0.2797 0.2953 0.2371 0.0355  0.0128  0.0125  42  TYR   B OH  
4280 N  N   . LEU   B 43  ? 0.1576 0.1493 0.1491 0.0061  -0.0145 -0.0130 43  LEU   B N   
4281 C  CA  . LEU   B 43  ? 0.1554 0.1519 0.1416 0.0039  -0.0149 -0.0003 43  LEU   B CA  
4282 C  C   . LEU   B 43  ? 0.1619 0.1568 0.1468 0.0060  -0.0155 -0.0071 43  LEU   B C   
4283 O  O   . LEU   B 43  ? 0.1555 0.1584 0.1693 0.0052  -0.0199 0.0032  43  LEU   B O   
4284 C  CB  . LEU   B 43  ? 0.1525 0.1485 0.1566 0.0001  -0.0294 -0.0068 43  LEU   B CB  
4285 C  CG  . LEU   B 43  ? 0.1624 0.1443 0.1528 0.0022  -0.0252 -0.0059 43  LEU   B CG  
4286 C  CD1 . LEU   B 43  ? 0.1688 0.1542 0.1920 0.0034  -0.0392 -0.0019 43  LEU   B CD1 
4287 C  CD2 . LEU   B 43  ? 0.1570 0.1425 0.1704 -0.0049 -0.0246 -0.0073 43  LEU   B CD2 
4299 N  N   . LYS   B 44  ? 0.1572 0.1529 0.1502 0.0111  -0.0097 -0.0059 44  LYS   B N   
4300 C  CA  . LYS   B 44  ? 0.1700 0.1612 0.1543 0.0106  -0.0132 0.0107  44  LYS   B CA  
4301 C  C   . LYS   B 44  ? 0.1594 0.1558 0.1493 0.0098  -0.0147 -0.0004 44  LYS   B C   
4302 O  O   . LYS   B 44  ? 0.1813 0.1493 0.1899 0.0065  -0.0093 -0.0016 44  LYS   B O   
4303 C  CB  . LYS   B 44  ? 0.1934 0.1854 0.1699 0.0169  -0.0250 0.0074  44  LYS   B CB  
4304 C  CG  . LYS   B 44  ? 0.2342 0.2172 0.2045 0.0139  -0.0460 0.0044  44  LYS   B CG  
4305 C  CD  . LYS   B 44  ? 0.2692 0.2384 0.2530 -0.0028 -0.0550 0.0074  44  LYS   B CD  
4306 C  CE  . LYS   B 44  ? 0.2993 0.2624 0.3008 -0.0126 -0.0499 0.0121  44  LYS   B CE  
4307 N  NZ  . LYS   B 44  ? 0.3100 0.2737 0.3275 -0.0121 -0.0560 0.0201  44  LYS   B NZ  
4321 N  N   . HIS   B 45  ? 0.1539 0.1584 0.1417 0.0063  -0.0161 0.0047  45  HIS   B N   
4322 C  CA  . HIS   B 45  ? 0.1603 0.1526 0.1600 0.0092  -0.0051 -0.0039 45  HIS   B CA  
4323 C  C   . HIS   B 45  ? 0.1863 0.1718 0.1827 0.0160  -0.0179 -0.0080 45  HIS   B C   
4324 O  O   . HIS   B 45  ? 0.1981 0.2013 0.2325 0.0401  0.0050  -0.0043 45  HIS   B O   
4325 C  CB  . HIS   B 45  ? 0.1490 0.1542 0.1516 0.0008  -0.0046 0.0042  45  HIS   B CB  
4326 C  CG  . HIS   B 45  ? 0.1499 0.1532 0.1455 -0.0120 -0.0004 -0.0016 45  HIS   B CG  
4327 N  ND1 . HIS   B 45  ? 0.1534 0.1471 0.1575 -0.0047 -0.0170 -0.0062 45  HIS   B ND1 
4328 C  CD2 . HIS   B 45  ? 0.1625 0.1563 0.1657 -0.0126 -0.0099 -0.0015 45  HIS   B CD2 
4329 C  CE1 . HIS   B 45  ? 0.1616 0.1385 0.1472 -0.0007 -0.0354 -0.0132 45  HIS   B CE1 
4330 N  NE2 . HIS   B 45  ? 0.1661 0.1537 0.1634 -0.0005 -0.0244 -0.0105 45  HIS   B NE2 
4338 N  N   . GLY   B 46  ? 0.1962 0.1649 0.2093 0.0190  -0.0367 0.0081  46  GLY   B N   
4339 C  CA  . GLY   B 46  ? 0.2064 0.1774 0.2391 0.0130  -0.0440 0.0055  46  GLY   B CA  
4340 C  C   . GLY   B 46  ? 0.2078 0.1978 0.2840 0.0223  -0.0369 0.0025  46  GLY   B C   
4341 O  O   . GLY   B 46  ? 0.2185 0.2263 0.3646 0.0295  -0.0183 -0.0160 46  GLY   B O   
4345 N  N   . GLY   B 47  ? 0.2046 0.2025 0.2580 0.0106  -0.0149 -0.0020 47  GLY   B N   
4346 C  CA  . GLY   B 47  ? 0.1945 0.1718 0.2142 0.0063  -0.0078 -0.0002 47  GLY   B CA  
4347 C  C   . GLY   B 47  ? 0.1705 0.1502 0.1894 0.0052  0.0069  0.0100  47  GLY   B C   
4348 O  O   . GLY   B 47  ? 0.1816 0.1369 0.2060 0.0024  -0.0080 0.0114  47  GLY   B O   
4352 N  N   . GLY   B 48  ? 0.1522 0.1433 0.1895 0.0043  -0.0071 0.0161  48  GLY   B N   
4353 C  CA  . GLY   B 48  ? 0.1521 0.1393 0.1874 -0.0031 -0.0056 0.0153  48  GLY   B CA  
4354 C  C   . GLY   B 48  ? 0.1475 0.1383 0.1779 0.0032  0.0049  0.0026  48  GLY   B C   
4355 O  O   . GLY   B 48  ? 0.1426 0.1462 0.1955 0.0028  -0.0049 0.0059  48  GLY   B O   
4359 N  N   . VAL   B 49  ? 0.1443 0.1408 0.1627 0.0130  0.0024  0.0097  49  VAL   B N   
4360 C  CA  . VAL   B 49  ? 0.1507 0.1489 0.1574 0.0091  -0.0137 -0.0009 49  VAL   B CA  
4361 C  C   . VAL   B 49  ? 0.1437 0.1456 0.1318 0.0155  0.0010  0.0083  49  VAL   B C   
4362 O  O   . VAL   B 49  ? 0.1514 0.1513 0.1473 0.0083  -0.0010 0.0104  49  VAL   B O   
4363 C  CB  . VAL   B 49  ? 0.1534 0.1677 0.1973 0.0044  -0.0274 0.0049  49  VAL   B CB  
4364 C  CG1 . VAL   B 49  ? 0.1487 0.1769 0.1784 0.0047  -0.0338 0.0065  49  VAL   B CG1 
4365 C  CG2 . VAL   B 49  ? 0.1688 0.1765 0.2134 -0.0050 -0.0402 -0.0008 49  VAL   B CG2 
4375 N  N   . ALA   B 50  ? 0.1325 0.1382 0.1488 0.0037  0.0029  0.0055  50  ALA   B N   
4376 C  CA  . ALA   B 50  ? 0.1275 0.1299 0.1544 0.0028  -0.0049 0.0046  50  ALA   B CA  
4377 C  C   . ALA   B 50  ? 0.1428 0.1308 0.1606 0.0061  -0.0053 0.0060  50  ALA   B C   
4378 O  O   . ALA   B 50  ? 0.1452 0.1355 0.1515 0.0059  -0.0063 0.0016  50  ALA   B O   
4379 C  CB  . ALA   B 50  ? 0.1337 0.1314 0.1717 -0.0049 -0.0018 0.0068  50  ALA   B CB  
4385 N  N   . GLY   B 51  ? 0.1399 0.1425 0.1660 0.0091  -0.0077 0.0053  51  GLY   B N   
4386 C  CA  . GLY   B 51  ? 0.1373 0.1512 0.1813 0.0141  -0.0111 0.0117  51  GLY   B CA  
4387 C  C   . GLY   B 51  ? 0.1387 0.1454 0.1801 0.0203  -0.0125 0.0128  51  GLY   B C   
4388 O  O   . GLY   B 51  ? 0.1403 0.1548 0.1984 0.0077  -0.0115 0.0041  51  GLY   B O   
4392 N  N   . ALA   B 52  ? 0.1452 0.1366 0.1748 0.0163  -0.0092 0.0144  52  ALA   B N   
4393 C  CA  . ALA   B 52  ? 0.1429 0.1476 0.1720 0.0188  0.0045  0.0059  52  ALA   B CA  
4394 C  C   . ALA   B 52  ? 0.1351 0.1476 0.1619 0.0120  -0.0008 0.0039  52  ALA   B C   
4395 O  O   . ALA   B 52  ? 0.1423 0.1527 0.1801 0.0163  0.0036  0.0009  52  ALA   B O   
4396 C  CB  . ALA   B 52  ? 0.1640 0.1558 0.1734 0.0057  0.0142  0.0009  52  ALA   B CB  
4402 N  N   . LEU   B 53  ? 0.1307 0.1408 0.1494 0.0118  0.0048  0.0040  53  LEU   B N   
4403 C  CA  . LEU   B 53  ? 0.1339 0.1504 0.1507 0.0139  0.0019  0.0062  53  LEU   B CA  
4404 C  C   . LEU   B 53  ? 0.1354 0.1431 0.1592 0.0136  0.0084  0.0122  53  LEU   B C   
4405 O  O   . LEU   B 53  ? 0.1444 0.1543 0.1782 0.0033  0.0071  0.0191  53  LEU   B O   
4406 C  CB  . LEU   B 53  ? 0.1336 0.1564 0.1740 0.0088  0.0008  0.0170  53  LEU   B CB  
4407 C  CG  . LEU   B 53  ? 0.1313 0.1715 0.1814 0.0042  0.0006  0.0222  53  LEU   B CG  
4408 C  CD1 . LEU   B 53  ? 0.1373 0.1920 0.2049 0.0111  -0.0051 0.0047  53  LEU   B CD1 
4409 C  CD2 . LEU   B 53  ? 0.1509 0.1960 0.2102 -0.0015 -0.0033 -0.0073 53  LEU   B CD2 
4421 N  N   . ASN   B 54  ? 0.1327 0.1370 0.1592 0.0005  -0.0020 0.0111  54  ASN   B N   
4422 C  CA  . ASN   B 54  ? 0.1377 0.1475 0.1762 0.0027  -0.0048 0.0056  54  ASN   B CA  
4423 C  C   . ASN   B 54  ? 0.1389 0.1498 0.1831 0.0013  0.0067  0.0104  54  ASN   B C   
4424 O  O   . ASN   B 54  ? 0.1390 0.1537 0.1862 -0.0005 0.0076  0.0101  54  ASN   B O   
4425 C  CB  . ASN   B 54  ? 0.1411 0.1579 0.1831 0.0043  -0.0045 0.0016  54  ASN   B CB  
4426 C  CG  . ASN   B 54  ? 0.1376 0.1685 0.1787 0.0052  -0.0075 0.0063  54  ASN   B CG  
4427 O  OD1 . ASN   B 54  ? 0.1423 0.1616 0.1853 0.0011  -0.0146 -0.0065 54  ASN   B OD1 
4428 N  ND2 . ASN   B 54  ? 0.1470 0.1874 0.2038 -0.0016 -0.0256 0.0211  54  ASN   B ND2 
4435 N  N   . LYS   B 55  ? 0.1374 0.1521 0.2020 0.0123  0.0018  0.0026  55  LYS   B N   
4436 C  CA  . LYS   B 55  ? 0.1459 0.1669 0.2160 0.0164  -0.0018 0.0004  55  LYS   B CA  
4437 C  C   . LYS   B 55  ? 0.1373 0.1619 0.2080 0.0121  0.0049  -0.0027 55  LYS   B C   
4438 O  O   . LYS   B 55  ? 0.1337 0.1762 0.2217 0.0110  0.0012  -0.0018 55  LYS   B O   
4439 C  CB  . LYS   B 55  ? 0.1564 0.1704 0.2441 0.0262  0.0093  0.0062  55  LYS   B CB  
4440 C  CG  . LYS   B 55  ? 0.1995 0.1978 0.3224 0.0326  0.0291  0.0140  55  LYS   B CG  
4441 C  CD  . LYS   B 55  ? 0.2408 0.2246 0.3825 0.0422  0.0417  0.0249  55  LYS   B CD  
4442 C  CE  . LYS   B 55  ? 0.2663 0.2466 0.4324 0.0447  0.0550  0.0291  55  LYS   B CE  
4443 N  NZ  . LYS   B 55  ? 0.2761 0.2608 0.4622 0.0431  0.0437  0.0317  55  LYS   B NZ  
4457 N  N   . ALA   B 56  ? 0.1370 0.1670 0.1947 0.0079  0.0007  -0.0099 56  ALA   B N   
4458 C  CA  . ALA   B 56  ? 0.1512 0.1764 0.1904 0.0031  0.0059  -0.0028 56  ALA   B CA  
4459 C  C   . ALA   B 56  ? 0.1497 0.1733 0.1909 0.0030  0.0090  0.0017  56  ALA   B C   
4460 O  O   . ALA   B 56  ? 0.1629 0.1878 0.2104 0.0069  0.0323  0.0088  56  ALA   B O   
4461 C  CB  . ALA   B 56  ? 0.1665 0.1978 0.1854 -0.0128 0.0014  -0.0067 56  ALA   B CB  
4467 N  N   . THR   B 57  ? 0.1419 0.1665 0.1962 0.0049  0.0183  0.0042  57  THR   B N   
4468 C  CA  . THR   B 57  ? 0.1480 0.1676 0.1894 0.0018  0.0224  0.0119  57  THR   B CA  
4469 C  C   . THR   B 57  ? 0.1532 0.1806 0.2151 -0.0024 0.0240  0.0089  57  THR   B C   
4470 O  O   . THR   B 57  ? 0.1581 0.1775 0.2219 -0.0147 0.0207  0.0142  57  THR   B O   
4471 C  CB  . THR   B 57  ? 0.1566 0.1536 0.1627 0.0038  0.0157  0.0156  57  THR   B CB  
4472 O  OG1 . THR   B 57  ? 0.1581 0.1508 0.1762 -0.0007 0.0155  0.0106  57  THR   B OG1 
4473 C  CG2 . THR   B 57  ? 0.1527 0.1591 0.1582 0.0025  0.0083  0.0046  57  THR   B CG2 
4481 N  N   . ASN   B 58  ? 0.1345 0.2017 0.2369 -0.0172 0.0078  -0.0043 58  ASN   B N   
4482 C  CA  . ASN   B 58  ? 0.1576 0.2435 0.2677 -0.0277 0.0257  0.0004  58  ASN   B CA  
4483 C  C   . ASN   B 58  ? 0.1442 0.2199 0.2295 -0.0172 -0.0012 0.0029  58  ASN   B C   
4484 O  O   . ASN   B 58  ? 0.1544 0.2249 0.2319 -0.0182 0.0046  -0.0052 58  ASN   B O   
4485 C  CB  . ASN   B 58  ? 0.2295 0.3065 0.3713 -0.0392 0.0540  0.0008  58  ASN   B CB  
4486 C  CG  . ASN   B 58  ? 0.3272 0.3522 0.5035 -0.0421 0.0613  0.0243  58  ASN   B CG  
4487 O  OD1 . ASN   B 58  ? 0.3969 0.3969 0.5514 -0.0438 0.0617  0.0323  58  ASN   B OD1 
4488 N  ND2 . ASN   B 58  ? 0.4033 0.4033 0.5511 -0.0466 0.0647  0.0327  58  ASN   B ND2 
4495 N  N   . ASN   B 59  ? 0.1380 0.1962 0.2131 -0.0074 0.0018  0.0063  59  ASN   B N   
4496 C  CA  . ASN   B 59  ? 0.1395 0.1952 0.2102 -0.0044 -0.0071 0.0139  59  ASN   B CA  
4497 C  C   . ASN   B 59  ? 0.1375 0.1854 0.2073 -0.0113 -0.0130 0.0019  59  ASN   B C   
4498 O  O   . ASN   B 59  ? 0.1418 0.1884 0.2068 -0.0092 -0.0142 -0.0034 59  ASN   B O   
4499 C  CB  . ASN   B 59  ? 0.1517 0.2143 0.2294 -0.0002 -0.0237 0.0150  59  ASN   B CB  
4500 C  CG  . ASN   B 59  ? 0.1661 0.2357 0.2334 0.0064  -0.0372 0.0112  59  ASN   B CG  
4501 O  OD1 . ASN   B 59  ? 0.1728 0.2415 0.2315 0.0042  -0.0266 0.0231  59  ASN   B OD1 
4502 N  ND2 . ASN   B 59  ? 0.1740 0.2439 0.2479 -0.0033 -0.0356 0.0043  59  ASN   B ND2 
4509 N  N   . ALA   B 60  ? 0.1397 0.1728 0.2059 -0.0084 -0.0017 0.0016  60  ALA   B N   
4510 C  CA  . ALA   B 60  ? 0.1528 0.1653 0.2026 -0.0155 -0.0063 0.0057  60  ALA   B CA  
4511 C  C   . ALA   B 60  ? 0.1524 0.1542 0.1881 -0.0126 -0.0088 0.0052  60  ALA   B C   
4512 O  O   . ALA   B 60  ? 0.1528 0.1517 0.2030 -0.0148 -0.0025 0.0011  60  ALA   B O   
4513 C  CB  . ALA   B 60  ? 0.1602 0.1589 0.2236 -0.0140 -0.0051 0.0129  60  ALA   B CB  
4519 N  N   . MET   B 61  ? 0.1407 0.1509 0.1789 -0.0083 -0.0027 0.0029  61  MET   B N   
4520 C  CA  . MET   B 61  ? 0.1335 0.1466 0.1771 -0.0084 -0.0130 -0.0023 61  MET   B CA  
4521 C  C   . MET   B 61  ? 0.1442 0.1516 0.1842 -0.0090 -0.0135 0.0036  61  MET   B C   
4522 O  O   . MET   B 61  ? 0.1496 0.1420 0.1716 -0.0053 -0.0064 -0.0017 61  MET   B O   
4523 C  CB  . MET   B 61  ? 0.1329 0.1483 0.1786 0.0033  -0.0097 -0.0024 61  MET   B CB  
4524 C  CG  . MET   B 61  ? 0.1378 0.1488 0.1682 -0.0052 -0.0056 0.0018  61  MET   B CG  
4525 S  SD  . MET   B 61  ? 0.1354 0.1462 0.1873 -0.0024 -0.0018 -0.0084 61  MET   B SD  
4526 C  CE  . MET   B 61  ? 0.1453 0.1673 0.2032 0.0032  -0.0020 -0.0218 61  MET   B CE  
4536 N  N   . GLN   B 62  ? 0.1413 0.1554 0.1639 -0.0030 -0.0102 -0.0006 62  GLN   B N   
4537 C  CA  . GLN   B 62  ? 0.1423 0.1525 0.1776 0.0024  -0.0194 -0.0070 62  GLN   B CA  
4538 C  C   . GLN   B 62  ? 0.1454 0.1593 0.1689 0.0009  -0.0201 -0.0041 62  GLN   B C   
4539 O  O   . GLN   B 62  ? 0.1615 0.1640 0.1702 -0.0004 -0.0225 -0.0078 62  GLN   B O   
4540 C  CB  . GLN   B 62  ? 0.1493 0.1524 0.1748 0.0031  -0.0152 -0.0016 62  GLN   B CB  
4541 C  CG  . GLN   B 62  ? 0.1492 0.1643 0.1740 0.0041  -0.0241 -0.0051 62  GLN   B CG  
4542 C  CD  . GLN   B 62  ? 0.1549 0.1604 0.1645 0.0052  -0.0219 0.0085  62  GLN   B CD  
4543 O  OE1 . GLN   B 62  ? 0.1562 0.1597 0.1746 0.0030  -0.0218 -0.0066 62  GLN   B OE1 
4544 N  NE2 . GLN   B 62  ? 0.1568 0.1650 0.1752 0.0002  -0.0227 -0.0063 62  GLN   B NE2 
4553 N  N   . VAL   B 63  ? 0.1439 0.1632 0.1930 -0.0055 -0.0162 -0.0173 63  VAL   B N   
4554 C  CA  . VAL   B 63  ? 0.1563 0.1631 0.2080 -0.0090 -0.0251 -0.0123 63  VAL   B CA  
4555 C  C   . VAL   B 63  ? 0.1564 0.1512 0.1958 -0.0153 -0.0283 -0.0153 63  VAL   B C   
4556 O  O   . VAL   B 63  ? 0.1631 0.1564 0.2137 -0.0092 -0.0426 -0.0167 63  VAL   B O   
4557 C  CB  . VAL   B 63  ? 0.1594 0.1796 0.2513 -0.0178 -0.0274 -0.0162 63  VAL   B CB  
4558 C  CG1 . VAL   B 63  ? 0.1700 0.1865 0.2522 -0.0201 -0.0264 -0.0177 63  VAL   B CG1 
4559 C  CG2 . VAL   B 63  ? 0.1558 0.1964 0.2608 -0.0109 -0.0295 -0.0132 63  VAL   B CG2 
4569 N  N   . GLU   B 64  ? 0.1559 0.1484 0.1853 -0.0119 -0.0213 -0.0096 64  GLU   B N   
4570 C  CA  . GLU   B 64  ? 0.1572 0.1428 0.1741 -0.0128 -0.0316 -0.0050 64  GLU   B CA  
4571 C  C   . GLU   B 64  ? 0.1548 0.1396 0.1652 -0.0043 -0.0260 -0.0201 64  GLU   B C   
4572 O  O   . GLU   B 64  ? 0.1646 0.1483 0.1802 -0.0081 -0.0278 -0.0160 64  GLU   B O   
4573 C  CB  . GLU   B 64  ? 0.1538 0.1534 0.1843 -0.0101 -0.0221 -0.0030 64  GLU   B CB  
4574 C  CG  . GLU   B 64  ? 0.1597 0.1512 0.1784 -0.0207 -0.0301 -0.0143 64  GLU   B CG  
4575 C  CD  . GLU   B 64  ? 0.1612 0.1593 0.1923 -0.0262 -0.0264 -0.0091 64  GLU   B CD  
4576 O  OE1 . GLU   B 64  ? 0.1694 0.1769 0.1974 -0.0333 -0.0199 -0.0263 64  GLU   B OE1 
4577 O  OE2 . GLU   B 64  ? 0.1751 0.1644 0.2006 -0.0273 -0.0372 -0.0092 64  GLU   B OE2 
4584 N  N   . SER   B 65  ? 0.1476 0.1382 0.1663 -0.0094 -0.0117 -0.0181 65  SER   B N   
4585 C  CA  . SER   B 65  ? 0.1491 0.1419 0.1719 -0.0036 -0.0205 -0.0180 65  SER   B CA  
4586 C  C   . SER   B 65  ? 0.1525 0.1432 0.1735 -0.0027 -0.0262 -0.0190 65  SER   B C   
4587 O  O   . SER   B 65  ? 0.1522 0.1540 0.1690 -0.0041 -0.0190 -0.0189 65  SER   B O   
4588 C  CB  . SER   B 65  ? 0.1523 0.1491 0.1673 -0.0071 -0.0185 -0.0128 65  SER   B CB  
4589 O  OG  . SER   B 65  ? 0.1528 0.1432 0.1729 -0.0089 -0.0111 -0.0161 65  SER   B OG  
4595 N  N   . ASP   B 66  ? 0.1663 0.1505 0.1779 -0.0016 -0.0283 -0.0211 66  ASP   B N   
4596 C  CA  . ASP   B 66  ? 0.1736 0.1575 0.1666 0.0036  -0.0266 -0.0137 66  ASP   B CA  
4597 C  C   . ASP   B 66  ? 0.1755 0.1621 0.1710 -0.0046 -0.0171 -0.0187 66  ASP   B C   
4598 O  O   . ASP   B 66  ? 0.1733 0.1716 0.1684 0.0065  -0.0292 -0.0192 66  ASP   B O   
4599 C  CB  . ASP   B 66  ? 0.1874 0.1708 0.1910 0.0124  -0.0407 -0.0230 66  ASP   B CB  
4600 C  CG  . ASP   B 66  ? 0.2164 0.1830 0.2195 0.0200  -0.0513 -0.0076 66  ASP   B CG  
4601 O  OD1 . ASP   B 66  ? 0.2372 0.1770 0.2218 0.0134  -0.0535 -0.0011 66  ASP   B OD1 
4602 O  OD2 . ASP   B 66  ? 0.2348 0.2073 0.2769 0.0392  -0.0522 -0.0080 66  ASP   B OD2 
4607 N  N   . ASP   B 67  ? 0.1772 0.1516 0.1653 -0.0044 -0.0206 -0.0247 67  ASP   B N   
4608 C  CA  . ASP   B 67  ? 0.1916 0.1504 0.1796 -0.0071 -0.0265 -0.0171 67  ASP   B CA  
4609 C  C   . ASP   B 67  ? 0.1858 0.1477 0.1915 0.0015  -0.0264 -0.0202 67  ASP   B C   
4610 O  O   . ASP   B 67  ? 0.1909 0.1501 0.1885 0.0017  -0.0193 -0.0216 67  ASP   B O   
4611 C  CB  . ASP   B 67  ? 0.2133 0.1590 0.2065 -0.0113 -0.0365 -0.0137 67  ASP   B CB  
4612 C  CG  . ASP   B 67  ? 0.2458 0.1644 0.2061 -0.0065 -0.0612 -0.0168 67  ASP   B CG  
4613 O  OD1 . ASP   B 67  ? 0.2668 0.1688 0.2154 -0.0135 -0.0661 -0.0069 67  ASP   B OD1 
4614 O  OD2 . ASP   B 67  ? 0.2603 0.1760 0.2235 0.0069  -0.0697 -0.0134 67  ASP   B OD2 
4619 N  N   . TYR   B 68  ? 0.1741 0.1474 0.1768 0.0007  -0.0371 -0.0306 68  TYR   B N   
4620 C  CA  . TYR   B 68  ? 0.1696 0.1691 0.1920 0.0014  -0.0357 -0.0301 68  TYR   B CA  
4621 C  C   . TYR   B 68  ? 0.1601 0.1673 0.1795 -0.0015 -0.0326 -0.0341 68  TYR   B C   
4622 O  O   . TYR   B 68  ? 0.1680 0.1738 0.1902 0.0045  -0.0271 -0.0507 68  TYR   B O   
4623 C  CB  . TYR   B 68  ? 0.1741 0.1882 0.1923 0.0039  -0.0426 -0.0419 68  TYR   B CB  
4624 C  CG  . TYR   B 68  ? 0.1830 0.1983 0.2019 0.0101  -0.0342 -0.0564 68  TYR   B CG  
4625 C  CD1 . TYR   B 68  ? 0.1814 0.2019 0.2217 0.0003  -0.0265 -0.0663 68  TYR   B CD1 
4626 C  CD2 . TYR   B 68  ? 0.1904 0.2136 0.2126 0.0178  -0.0390 -0.0467 68  TYR   B CD2 
4627 C  CE1 . TYR   B 68  ? 0.1892 0.2158 0.2381 0.0017  -0.0224 -0.0656 68  TYR   B CE1 
4628 C  CE2 . TYR   B 68  ? 0.1928 0.2205 0.2302 0.0163  -0.0269 -0.0604 68  TYR   B CE2 
4629 C  CZ  . TYR   B 68  ? 0.1828 0.2219 0.2426 0.0074  -0.0240 -0.0613 68  TYR   B CZ  
4630 O  OH  . TYR   B 68  ? 0.1766 0.2402 0.2728 0.0042  -0.0199 -0.0419 68  TYR   B OH  
4640 N  N   . ILE   B 69  ? 0.1621 0.1600 0.1892 -0.0021 -0.0294 -0.0318 69  ILE   B N   
4641 C  CA  . ILE   B 69  ? 0.1692 0.1650 0.1910 -0.0025 -0.0257 -0.0410 69  ILE   B CA  
4642 C  C   . ILE   B 69  ? 0.1694 0.1617 0.1853 0.0108  -0.0395 -0.0291 69  ILE   B C   
4643 O  O   . ILE   B 69  ? 0.1763 0.1670 0.1896 0.0072  -0.0238 -0.0348 69  ILE   B O   
4644 C  CB  . ILE   B 69  ? 0.1801 0.1719 0.2204 -0.0039 0.0012  -0.0375 69  ILE   B CB  
4645 C  CG1 . ILE   B 69  ? 0.1795 0.1746 0.2318 -0.0086 0.0013  -0.0439 69  ILE   B CG1 
4646 C  CG2 . ILE   B 69  ? 0.1915 0.1813 0.2297 -0.0016 -0.0014 -0.0296 69  ILE   B CG2 
4647 C  CD1 . ILE   B 69  ? 0.1670 0.1774 0.2355 -0.0188 0.0034  -0.0466 69  ILE   B CD1 
4659 N  N   . ALA   B 70  ? 0.1696 0.1658 0.1904 0.0103  -0.0480 -0.0300 70  ALA   B N   
4660 C  CA  . ALA   B 70  ? 0.1796 0.1675 0.1665 0.0077  -0.0489 -0.0318 70  ALA   B CA  
4661 C  C   . ALA   B 70  ? 0.1805 0.1602 0.1764 0.0026  -0.0506 -0.0363 70  ALA   B C   
4662 O  O   . ALA   B 70  ? 0.1915 0.1628 0.1795 0.0077  -0.0417 -0.0347 70  ALA   B O   
4663 C  CB  . ALA   B 70  ? 0.1890 0.1817 0.1858 0.0067  -0.0515 -0.0301 70  ALA   B CB  
4669 N  N   . THR   B 71  ? 0.1871 0.1596 0.1977 0.0030  -0.0563 -0.0365 71  THR   B N   
4670 C  CA  . THR   B 71  ? 0.2016 0.1656 0.2059 0.0103  -0.0725 -0.0386 71  THR   B CA  
4671 C  C   . THR   B 71  ? 0.1996 0.1698 0.2338 0.0275  -0.0652 -0.0529 71  THR   B C   
4672 O  O   . THR   B 71  ? 0.2133 0.1773 0.2764 0.0306  -0.0640 -0.0667 71  THR   B O   
4673 C  CB  . THR   B 71  ? 0.2232 0.1936 0.2203 0.0011  -0.0811 -0.0159 71  THR   B CB  
4674 O  OG1 . THR   B 71  ? 0.2430 0.2244 0.2579 -0.0171 -0.0752 0.0062  71  THR   B OG1 
4675 C  CG2 . THR   B 71  ? 0.2421 0.1927 0.2409 0.0054  -0.0683 -0.0055 71  THR   B CG2 
4683 N  N   . ASN   B 72  ? 0.1856 0.1740 0.2241 0.0177  -0.0586 -0.0698 72  ASN   B N   
4684 C  CA  . ASN   B 72  ? 0.1837 0.1917 0.2206 0.0221  -0.0494 -0.0682 72  ASN   B CA  
4685 C  C   . ASN   B 72  ? 0.1860 0.2003 0.2293 0.0094  -0.0266 -0.0668 72  ASN   B C   
4686 O  O   . ASN   B 72  ? 0.1869 0.2188 0.2525 0.0084  -0.0048 -0.0700 72  ASN   B O   
4687 C  CB  . ASN   B 72  ? 0.1921 0.2111 0.2348 0.0227  -0.0617 -0.0564 72  ASN   B CB  
4688 C  CG  . ASN   B 72  ? 0.2091 0.2251 0.2416 0.0418  -0.0637 -0.0391 72  ASN   B CG  
4689 O  OD1 . ASN   B 72  ? 0.2270 0.2407 0.2445 0.0277  -0.0492 -0.0513 72  ASN   B OD1 
4690 N  ND2 . ASN   B 72  ? 0.2228 0.2327 0.2811 0.0571  -0.0492 -0.0074 72  ASN   B ND2 
4697 N  N   . GLY   B 73  ? 0.1931 0.1981 0.2097 0.0044  -0.0382 -0.0656 73  GLY   B N   
4698 C  CA  . GLY   B 73  ? 0.1879 0.2065 0.1823 0.0013  -0.0329 -0.0554 73  GLY   B CA  
4699 C  C   . GLY   B 73  ? 0.1779 0.2056 0.1522 0.0056  -0.0201 -0.0513 73  GLY   B C   
4700 O  O   . GLY   B 73  ? 0.1729 0.1870 0.1736 0.0064  -0.0216 -0.0420 73  GLY   B O   
4704 N  N   . PRO   B 74  ? 0.1790 0.2182 0.1407 0.0033  -0.0241 -0.0397 74  PRO   B N   
4705 C  CA  . PRO   B 74  ? 0.1736 0.2186 0.1407 0.0075  -0.0202 -0.0248 74  PRO   B CA  
4706 C  C   . PRO   B 74  ? 0.1574 0.2017 0.1415 0.0070  -0.0153 -0.0230 74  PRO   B C   
4707 O  O   . PRO   B 74  ? 0.1663 0.2043 0.1858 0.0085  -0.0105 -0.0376 74  PRO   B O   
4708 C  CB  . PRO   B 74  ? 0.1864 0.2374 0.1491 0.0020  -0.0202 -0.0177 74  PRO   B CB  
4709 C  CG  . PRO   B 74  ? 0.2084 0.2468 0.1735 0.0059  -0.0147 -0.0187 74  PRO   B CG  
4710 C  CD  . PRO   B 74  ? 0.2030 0.2362 0.1523 0.0073  -0.0145 -0.0360 74  PRO   B CD  
4718 N  N   . LEU   B 75  ? 0.1559 0.1878 0.1285 0.0113  -0.0112 -0.0192 75  LEU   B N   
4719 C  CA  . LEU   B 75  ? 0.1567 0.1840 0.1422 0.0031  -0.0191 -0.0104 75  LEU   B CA  
4720 C  C   . LEU   B 75  ? 0.1621 0.1908 0.1395 0.0104  -0.0099 -0.0085 75  LEU   B C   
4721 O  O   . LEU   B 75  ? 0.1771 0.2048 0.1556 0.0033  -0.0110 -0.0050 75  LEU   B O   
4722 C  CB  . LEU   B 75  ? 0.1655 0.1856 0.1449 -0.0042 -0.0180 0.0066  75  LEU   B CB  
4723 C  CG  . LEU   B 75  ? 0.1981 0.1971 0.1693 -0.0248 -0.0058 -0.0069 75  LEU   B CG  
4724 C  CD1 . LEU   B 75  ? 0.2275 0.2118 0.1631 -0.0402 0.0120  -0.0100 75  LEU   B CD1 
4725 C  CD2 . LEU   B 75  ? 0.2313 0.2095 0.2180 -0.0230 0.0068  -0.0026 75  LEU   B CD2 
4737 N  N   . LYS   B 76  ? 0.1584 0.2101 0.1646 0.0056  0.0069  0.0010  76  LYS   B N   
4738 C  CA  . LYS   B 76  ? 0.1703 0.2206 0.1992 -0.0024 0.0208  -0.0009 76  LYS   B CA  
4739 C  C   . LYS   B 76  ? 0.1620 0.2043 0.1643 0.0069  0.0074  0.0223  76  LYS   B C   
4740 O  O   . LYS   B 76  ? 0.1648 0.1900 0.1696 0.0013  0.0006  0.0229  76  LYS   B O   
4741 C  CB  . LYS   B 76  ? 0.1892 0.2326 0.2728 -0.0063 0.0393  -0.0354 76  LYS   B CB  
4742 C  CG  . LYS   B 76  ? 0.1973 0.2497 0.3248 0.0073  0.0335  -0.0462 76  LYS   B CG  
4743 C  CD  . LYS   B 76  ? 0.1971 0.2611 0.3793 0.0172  0.0193  -0.0601 76  LYS   B CD  
4744 C  CE  . LYS   B 76  ? 0.2062 0.2773 0.4228 0.0207  0.0069  -0.0681 76  LYS   B CE  
4745 N  NZ  . LYS   B 76  ? 0.2067 0.2824 0.4519 0.0141  -0.0146 -0.0825 76  LYS   B NZ  
4759 N  N   . VAL   B 77  ? 0.1698 0.2134 0.1591 0.0167  0.0050  0.0196  77  VAL   B N   
4760 C  CA  . VAL   B 77  ? 0.1733 0.2014 0.1681 0.0186  0.0153  0.0448  77  VAL   B CA  
4761 C  C   . VAL   B 77  ? 0.1597 0.1818 0.1666 0.0163  0.0216  0.0326  77  VAL   B C   
4762 O  O   . VAL   B 77  ? 0.1644 0.1780 0.1709 0.0271  0.0293  0.0230  77  VAL   B O   
4763 C  CB  . VAL   B 77  ? 0.1813 0.2125 0.2016 0.0202  0.0261  0.0559  77  VAL   B CB  
4764 C  CG1 . VAL   B 77  ? 0.1931 0.2011 0.2421 0.0065  0.0338  0.0579  77  VAL   B CG1 
4765 C  CG2 . VAL   B 77  ? 0.1926 0.2328 0.2346 0.0207  0.0178  0.0631  77  VAL   B CG2 
4775 N  N   . GLY   B 78  ? 0.1542 0.1704 0.1685 0.0131  0.0182  0.0263  78  GLY   B N   
4776 C  CA  . GLY   B 78  ? 0.1486 0.1684 0.1642 0.0131  0.0245  0.0158  78  GLY   B CA  
4777 C  C   . GLY   B 78  ? 0.1459 0.1611 0.1614 0.0114  0.0196  0.0200  78  GLY   B C   
4778 O  O   . GLY   B 78  ? 0.1544 0.1572 0.1623 0.0131  0.0140  0.0201  78  GLY   B O   
4782 N  N   . GLY   B 79  ? 0.1405 0.1636 0.1596 0.0119  0.0151  0.0130  79  GLY   B N   
4783 C  CA  . GLY   B 79  ? 0.1394 0.1574 0.1546 0.0118  -0.0016 0.0121  79  GLY   B CA  
4784 C  C   . GLY   B 79  ? 0.1326 0.1447 0.1587 0.0131  0.0072  0.0065  79  GLY   B C   
4785 O  O   . GLY   B 79  ? 0.1406 0.1445 0.1756 0.0106  0.0133  0.0171  79  GLY   B O   
4789 N  N   . SER   B 80  ? 0.1333 0.1393 0.1681 0.0098  0.0166  0.0007  80  SER   B N   
4790 C  CA  . SER   B 80  ? 0.1310 0.1372 0.1692 0.0064  -0.0011 0.0042  80  SER   B CA  
4791 C  C   . SER   B 80  ? 0.1369 0.1341 0.1572 0.0057  -0.0137 -0.0002 80  SER   B C   
4792 O  O   . SER   B 80  ? 0.1519 0.1347 0.1925 0.0077  0.0021  -0.0086 80  SER   B O   
4793 C  CB  . SER   B 80  ? 0.1321 0.1366 0.1707 -0.0003 0.0028  0.0057  80  SER   B CB  
4794 O  OG  . SER   B 80  ? 0.1424 0.1498 0.1838 -0.0040 -0.0164 0.0088  80  SER   B OG  
4800 N  N   . CYS   B 81  ? 0.1365 0.1232 0.1629 0.0041  -0.0100 -0.0068 81  CYS   B N   
4801 C  CA  . CYS   B 81  ? 0.1378 0.1230 0.1647 0.0025  -0.0124 -0.0015 81  CYS   B CA  
4802 C  C   . CYS   B 81  ? 0.1361 0.1165 0.1453 0.0049  -0.0171 -0.0055 81  CYS   B C   
4803 O  O   . CYS   B 81  ? 0.1609 0.1252 0.1535 0.0071  -0.0051 -0.0062 81  CYS   B O   
4804 C  CB  . CYS   B 81  ? 0.1530 0.1336 0.1663 0.0021  -0.0071 -0.0054 81  CYS   B CB  
4805 S  SG  . CYS   B 81  ? 0.1505 0.1528 0.1668 -0.0035 -0.0263 -0.0129 81  CYS   B SG  
4811 N  N   . VAL   B 82  ? 0.1395 0.1179 0.1569 -0.0013 -0.0145 -0.0100 82  VAL   B N   
4812 C  CA  . VAL   B 82  ? 0.1464 0.1221 0.1596 -0.0024 -0.0101 0.0014  82  VAL   B CA  
4813 C  C   . VAL   B 82  ? 0.1506 0.1156 0.1670 0.0002  -0.0063 -0.0018 82  VAL   B C   
4814 O  O   . VAL   B 82  ? 0.1568 0.1203 0.1949 -0.0047 -0.0051 -0.0212 82  VAL   B O   
4815 C  CB  . VAL   B 82  ? 0.1547 0.1441 0.1682 0.0047  -0.0145 0.0021  82  VAL   B CB  
4816 C  CG1 . VAL   B 82  ? 0.1758 0.1682 0.1731 0.0034  -0.0131 0.0211  82  VAL   B CG1 
4817 C  CG2 . VAL   B 82  ? 0.1665 0.1579 0.1800 -0.0012 -0.0310 0.0103  82  VAL   B CG2 
4827 N  N   . LEU   B 83  ? 0.1376 0.1200 0.1596 -0.0104 -0.0126 -0.0124 83  LEU   B N   
4828 C  CA  . LEU   B 83  ? 0.1419 0.1221 0.1447 -0.0081 -0.0111 -0.0096 83  LEU   B CA  
4829 C  C   . LEU   B 83  ? 0.1458 0.1225 0.1518 -0.0111 -0.0164 -0.0033 83  LEU   B C   
4830 O  O   . LEU   B 83  ? 0.1466 0.1326 0.1275 -0.0164 -0.0111 0.0060  83  LEU   B O   
4831 C  CB  . LEU   B 83  ? 0.1476 0.1334 0.1571 -0.0110 -0.0209 -0.0144 83  LEU   B CB  
4832 C  CG  . LEU   B 83  ? 0.1676 0.1559 0.1617 -0.0129 -0.0117 -0.0197 83  LEU   B CG  
4833 C  CD1 . LEU   B 83  ? 0.1794 0.1658 0.1627 -0.0078 -0.0179 -0.0077 83  LEU   B CD1 
4834 C  CD2 . LEU   B 83  ? 0.1810 0.1647 0.1671 -0.0066 -0.0139 -0.0307 83  LEU   B CD2 
4846 N  N   . SER   B 84  ? 0.1463 0.1313 0.1797 -0.0211 -0.0086 0.0039  84  SER   B N   
4847 C  CA  . SER   B 84  ? 0.1489 0.1466 0.1740 -0.0230 -0.0140 0.0143  84  SER   B CA  
4848 C  C   . SER   B 84  ? 0.1422 0.1638 0.1453 -0.0131 -0.0175 0.0134  84  SER   B C   
4849 O  O   . SER   B 84  ? 0.1507 0.1463 0.1367 -0.0142 -0.0114 -0.0021 84  SER   B O   
4850 C  CB  . SER   B 84  ? 0.1632 0.1548 0.2249 -0.0261 0.0152  0.0264  84  SER   B CB  
4851 O  OG  . SER   B 84  ? 0.1629 0.1704 0.2637 -0.0318 0.0185  0.0269  84  SER   B OG  
4857 N  N   . GLY   B 85  ? 0.1432 0.1884 0.1580 -0.0209 -0.0173 0.0199  85  GLY   B N   
4858 C  CA  . GLY   B 85  ? 0.1431 0.1960 0.1717 -0.0286 -0.0034 -0.0015 85  GLY   B CA  
4859 C  C   . GLY   B 85  ? 0.1419 0.1770 0.1537 -0.0362 -0.0006 0.0076  85  GLY   B C   
4860 O  O   . GLY   B 85  ? 0.1523 0.1788 0.1588 -0.0505 0.0128  -0.0083 85  GLY   B O   
4864 N  N   . HIS   B 86  ? 0.1409 0.1610 0.1699 -0.0269 -0.0148 0.0174  86  HIS   B N   
4865 C  CA  . HIS   B 86  ? 0.1438 0.1581 0.1687 -0.0279 -0.0112 0.0184  86  HIS   B CA  
4866 C  C   . HIS   B 86  ? 0.1406 0.1696 0.1622 -0.0413 -0.0130 0.0307  86  HIS   B C   
4867 O  O   . HIS   B 86  ? 0.1544 0.1816 0.1777 -0.0280 0.0011  0.0362  86  HIS   B O   
4868 C  CB  . HIS   B 86  ? 0.1516 0.1542 0.1627 -0.0197 -0.0208 0.0099  86  HIS   B CB  
4869 C  CG  . HIS   B 86  ? 0.1536 0.1634 0.1614 -0.0110 -0.0182 0.0053  86  HIS   B CG  
4870 N  ND1 . HIS   B 86  ? 0.1578 0.1865 0.1907 -0.0238 -0.0211 -0.0081 86  HIS   B ND1 
4871 C  CD2 . HIS   B 86  ? 0.1569 0.1652 0.1668 -0.0091 -0.0193 0.0146  86  HIS   B CD2 
4872 C  CE1 . HIS   B 86  ? 0.1624 0.1826 0.1805 -0.0141 -0.0132 -0.0226 86  HIS   B CE1 
4873 N  NE2 . HIS   B 86  ? 0.1599 0.1752 0.1705 -0.0048 -0.0181 -0.0025 86  HIS   B NE2 
4881 N  N   . ASN   B 87  ? 0.1433 0.1765 0.1711 -0.0310 -0.0094 0.0338  87  ASN   B N   
4882 C  CA  . ASN   B 87  ? 0.1510 0.1910 0.1793 -0.0263 0.0190  0.0227  87  ASN   B CA  
4883 C  C   . ASN   B 87  ? 0.1657 0.1774 0.1664 -0.0248 0.0310  0.0201  87  ASN   B C   
4884 O  O   . ASN   B 87  ? 0.1868 0.1891 0.1911 -0.0206 0.0430  0.0120  87  ASN   B O   
4885 C  CB  . ASN   B 87  ? 0.1559 0.2290 0.1985 -0.0224 0.0194  0.0166  87  ASN   B CB  
4886 C  CG  . ASN   B 87  ? 0.1605 0.2492 0.2118 0.0063  0.0344  0.0327  87  ASN   B CG  
4887 O  OD1 . ASN   B 87  ? 0.1596 0.2333 0.2021 0.0112  0.0427  0.0476  87  ASN   B OD1 
4888 N  ND2 . ASN   B 87  ? 0.1968 0.2612 0.2518 0.0102  0.0398  0.0206  87  ASN   B ND2 
4895 N  N   . LEU   B 88  ? 0.1570 0.1692 0.1483 -0.0297 0.0134  0.0111  88  LEU   B N   
4896 C  CA  . LEU   B 88  ? 0.1649 0.1588 0.1518 -0.0291 0.0016  -0.0018 88  LEU   B CA  
4897 C  C   . LEU   B 88  ? 0.1661 0.1481 0.1486 -0.0352 -0.0048 0.0043  88  LEU   B C   
4898 O  O   . LEU   B 88  ? 0.1884 0.1584 0.1821 -0.0218 -0.0294 -0.0072 88  LEU   B O   
4899 C  CB  . LEU   B 88  ? 0.1719 0.1597 0.1741 -0.0364 -0.0029 0.0168  88  LEU   B CB  
4900 C  CG  . LEU   B 88  ? 0.2088 0.1920 0.1867 -0.0289 -0.0279 0.0407  88  LEU   B CG  
4901 C  CD1 . LEU   B 88  ? 0.2218 0.2246 0.1979 -0.0385 -0.0058 0.0465  88  LEU   B CD1 
4902 C  CD2 . LEU   B 88  ? 0.2421 0.2184 0.2455 0.0029  -0.0535 0.0179  88  LEU   B CD2 
4914 N  N   . ALA   B 89  ? 0.1606 0.1444 0.1402 -0.0364 0.0217  -0.0027 89  ALA   B N   
4915 C  CA  . ALA   B 89  ? 0.1522 0.1446 0.1222 -0.0323 0.0006  0.0078  89  ALA   B CA  
4916 C  C   . ALA   B 89  ? 0.1599 0.1493 0.1396 -0.0337 0.0145  0.0026  89  ALA   B C   
4917 O  O   . ALA   B 89  ? 0.1455 0.1578 0.1759 -0.0338 0.0134  -0.0275 89  ALA   B O   
4918 C  CB  . ALA   B 89  ? 0.1450 0.1421 0.1345 -0.0311 -0.0023 0.0149  89  ALA   B CB  
4924 N  N   . LYS   B 90  ? 0.1913 0.1386 0.1460 -0.0369 -0.0057 0.0144  90  LYS   B N   
4925 C  CA  . LYS   B 90  ? 0.2086 0.1338 0.1394 -0.0398 -0.0124 0.0087  90  LYS   B CA  
4926 C  C   . LYS   B 90  ? 0.1944 0.1292 0.1635 -0.0389 -0.0064 -0.0022 90  LYS   B C   
4927 O  O   . LYS   B 90  ? 0.2099 0.1488 0.1712 -0.0573 0.0038  -0.0008 90  LYS   B O   
4928 C  CB  . LYS   B 90  ? 0.2341 0.1412 0.1759 -0.0327 -0.0021 0.0196  90  LYS   B CB  
4929 C  CG  . LYS   B 90  ? 0.2363 0.1597 0.1847 -0.0187 0.0164  0.0211  90  LYS   B CG  
4930 C  CD  . LYS   B 90  ? 0.2642 0.1900 0.2390 -0.0086 0.0353  0.0052  90  LYS   B CD  
4931 C  CE  . LYS   B 90  ? 0.2771 0.2093 0.2828 -0.0171 0.0412  -0.0112 90  LYS   B CE  
4932 N  NZ  . LYS   B 90  ? 0.2807 0.2035 0.2737 -0.0314 0.0553  -0.0162 90  LYS   B NZ  
4946 N  N   . HIS   B 91  ? 0.1694 0.1223 0.1328 -0.0266 -0.0097 -0.0020 91  HIS   B N   
4947 C  CA  . HIS   B 91  ? 0.1551 0.1285 0.1535 -0.0198 -0.0080 0.0066  91  HIS   B CA  
4948 C  C   . HIS   B 91  ? 0.1458 0.1271 0.1280 -0.0192 -0.0110 0.0077  91  HIS   B C   
4949 O  O   . HIS   B 91  ? 0.1651 0.1289 0.1279 -0.0243 -0.0208 0.0006  91  HIS   B O   
4950 C  CB  . HIS   B 91  ? 0.1684 0.1300 0.1873 -0.0029 -0.0008 0.0191  91  HIS   B CB  
4951 C  CG  . HIS   B 91  ? 0.2117 0.1467 0.2532 0.0067  0.0278  0.0251  91  HIS   B CG  
4952 N  ND1 . HIS   B 91  ? 0.2467 0.1538 0.3059 0.0039  0.0372  0.0155  91  HIS   B ND1 
4953 C  CD2 . HIS   B 91  ? 0.2311 0.1719 0.2969 0.0224  0.0152  0.0570  91  HIS   B CD2 
4954 C  CE1 . HIS   B 91  ? 0.2510 0.1675 0.3271 0.0194  0.0386  0.0230  91  HIS   B CE1 
4955 N  NE2 . HIS   B 91  ? 0.2422 0.1784 0.3282 0.0323  0.0317  0.0616  91  HIS   B NE2 
4963 N  N   . CYS   B 92  ? 0.1414 0.1265 0.1286 -0.0221 -0.0168 0.0029  92  CYS   B N   
4964 C  CA  . CYS   B 92  ? 0.1376 0.1202 0.1299 -0.0174 -0.0124 0.0061  92  CYS   B CA  
4965 C  C   . CYS   B 92  ? 0.1324 0.1122 0.1394 -0.0105 -0.0005 0.0094  92  CYS   B C   
4966 O  O   . CYS   B 92  ? 0.1371 0.1222 0.1544 -0.0123 -0.0001 -0.0017 92  CYS   B O   
4967 C  CB  . CYS   B 92  ? 0.1392 0.1303 0.1507 -0.0101 -0.0066 0.0077  92  CYS   B CB  
4968 S  SG  . CYS   B 92  ? 0.1372 0.1306 0.1397 -0.0095 -0.0084 0.0046  92  CYS   B SG  
4974 N  N   . LEU   B 93  ? 0.1250 0.1186 0.1253 -0.0160 0.0001  -0.0032 93  LEU   B N   
4975 C  CA  . LEU   B 93  ? 0.1299 0.1162 0.1434 -0.0042 -0.0048 0.0004  93  LEU   B CA  
4976 C  C   . LEU   B 93  ? 0.1197 0.1186 0.1338 -0.0022 -0.0086 0.0029  93  LEU   B C   
4977 O  O   . LEU   B 93  ? 0.1287 0.1177 0.1339 -0.0028 0.0004  -0.0007 93  LEU   B O   
4978 C  CB  . LEU   B 93  ? 0.1298 0.1165 0.1572 0.0011  -0.0063 0.0046  93  LEU   B CB  
4979 C  CG  . LEU   B 93  ? 0.1272 0.1326 0.1692 -0.0034 -0.0007 0.0146  93  LEU   B CG  
4980 C  CD1 . LEU   B 93  ? 0.1292 0.1474 0.1646 0.0070  0.0031  0.0040  93  LEU   B CD1 
4981 C  CD2 . LEU   B 93  ? 0.1183 0.1331 0.1828 -0.0076 -0.0096 0.0084  93  LEU   B CD2 
4993 N  N   . HIS   B 94  ? 0.1268 0.1098 0.1287 -0.0048 -0.0109 -0.0011 94  HIS   B N   
4994 C  CA  . HIS   B 94  ? 0.1264 0.1169 0.1321 0.0018  -0.0069 0.0065  94  HIS   B CA  
4995 C  C   . HIS   B 94  ? 0.1209 0.1226 0.1422 -0.0036 -0.0064 0.0055  94  HIS   B C   
4996 O  O   . HIS   B 94  ? 0.1283 0.1302 0.1797 -0.0052 0.0117  -0.0104 94  HIS   B O   
4997 C  CB  . HIS   B 94  ? 0.1235 0.1242 0.1409 0.0028  -0.0021 0.0019  94  HIS   B CB  
4998 C  CG  . HIS   B 94  ? 0.1305 0.1233 0.1429 -0.0038 -0.0235 -0.0005 94  HIS   B CG  
4999 N  ND1 . HIS   B 94  ? 0.1376 0.1288 0.1302 -0.0080 -0.0176 0.0009  94  HIS   B ND1 
5000 C  CD2 . HIS   B 94  ? 0.1356 0.1196 0.1275 0.0004  -0.0165 0.0017  94  HIS   B CD2 
5001 C  CE1 . HIS   B 94  ? 0.1377 0.1272 0.1362 -0.0087 -0.0229 0.0061  94  HIS   B CE1 
5002 N  NE2 . HIS   B 94  ? 0.1333 0.1329 0.1372 -0.0103 -0.0170 0.0075  94  HIS   B NE2 
5010 N  N   . VAL   B 95  ? 0.1207 0.1213 0.1458 -0.0003 0.0005  -0.0006 95  VAL   B N   
5011 C  CA  . VAL   B 95  ? 0.1233 0.1284 0.1314 0.0019  0.0018  0.0105  95  VAL   B CA  
5012 C  C   . VAL   B 95  ? 0.1286 0.1282 0.1368 0.0021  0.0084  0.0047  95  VAL   B C   
5013 O  O   . VAL   B 95  ? 0.1332 0.1269 0.1488 0.0082  0.0040  0.0115  95  VAL   B O   
5014 C  CB  . VAL   B 95  ? 0.1297 0.1230 0.1529 -0.0020 -0.0094 0.0002  95  VAL   B CB  
5015 C  CG1 . VAL   B 95  ? 0.1346 0.1373 0.1680 -0.0076 -0.0026 0.0094  95  VAL   B CG1 
5016 C  CG2 . VAL   B 95  ? 0.1386 0.1190 0.1559 -0.0001 -0.0150 0.0031  95  VAL   B CG2 
5026 N  N   . VAL   B 96  ? 0.1365 0.1300 0.1475 0.0119  0.0081  0.0111  96  VAL   B N   
5027 C  CA  . VAL   B 96  ? 0.1388 0.1378 0.1507 0.0106  -0.0002 0.0133  96  VAL   B CA  
5028 C  C   . VAL   B 96  ? 0.1415 0.1469 0.1548 0.0114  0.0107  0.0143  96  VAL   B C   
5029 O  O   . VAL   B 96  ? 0.1460 0.1521 0.1691 0.0051  0.0160  0.0026  96  VAL   B O   
5030 C  CB  . VAL   B 96  ? 0.1442 0.1625 0.1514 0.0084  0.0081  0.0006  96  VAL   B CB  
5031 C  CG1 . VAL   B 96  ? 0.1484 0.1750 0.1570 0.0119  0.0087  0.0005  96  VAL   B CG1 
5032 C  CG2 . VAL   B 96  ? 0.1573 0.1652 0.1710 0.0066  0.0086  -0.0065 96  VAL   B CG2 
5042 N  N   . GLY   B 97  ? 0.1456 0.1477 0.1560 0.0054  0.0141  0.0180  97  GLY   B N   
5043 C  CA  . GLY   B 97  ? 0.1531 0.1485 0.1585 0.0020  0.0190  0.0155  97  GLY   B CA  
5044 C  C   . GLY   B 97  ? 0.1715 0.1562 0.1641 0.0131  0.0098  0.0136  97  GLY   B C   
5045 O  O   . GLY   B 97  ? 0.1813 0.1649 0.1645 0.0076  0.0038  0.0132  97  GLY   B O   
5049 N  N   . PRO   B 98  ? 0.1859 0.1577 0.1635 0.0127  0.0270  0.0294  98  PRO   B N   
5050 C  CA  . PRO   B 98  ? 0.1958 0.1700 0.1710 0.0212  0.0388  0.0257  98  PRO   B CA  
5051 C  C   . PRO   B 98  ? 0.2082 0.1752 0.1567 0.0334  0.0378  0.0434  98  PRO   B C   
5052 O  O   . PRO   B 98  ? 0.2010 0.1723 0.1768 0.0287  0.0444  0.0368  98  PRO   B O   
5053 C  CB  . PRO   B 98  ? 0.1829 0.1768 0.1893 0.0138  0.0566  0.0321  98  PRO   B CB  
5054 C  CG  . PRO   B 98  ? 0.1817 0.1703 0.1889 0.0137  0.0390  0.0352  98  PRO   B CG  
5055 C  CD  . PRO   B 98  ? 0.1713 0.1602 0.1816 0.0167  0.0299  0.0325  98  PRO   B CD  
5063 N  N   . ASN   B 99  ? 0.2206 0.1896 0.1715 0.0435  0.0382  0.0352  99  ASN   B N   
5064 C  CA  . ASN   B 99  ? 0.2364 0.1903 0.1817 0.0464  0.0315  0.0532  99  ASN   B CA  
5065 C  C   . ASN   B 99  ? 0.2568 0.2213 0.2010 0.0405  0.0460  0.0663  99  ASN   B C   
5066 O  O   . ASN   B 99  ? 0.2677 0.2264 0.2022 0.0360  0.0403  0.0578  99  ASN   B O   
5067 C  CB  . ASN   B 99  ? 0.2447 0.1907 0.1858 0.0459  0.0212  0.0452  99  ASN   B CB  
5068 C  CG  . ASN   B 99  ? 0.2447 0.2017 0.2080 0.0419  0.0116  0.0453  99  ASN   B CG  
5069 O  OD1 . ASN   B 99  ? 0.2475 0.2024 0.2297 0.0454  0.0018  0.0474  99  ASN   B OD1 
5070 N  ND2 . ASN   B 99  ? 0.2427 0.2072 0.2187 0.0466  -0.0172 0.0385  99  ASN   B ND2 
5077 N  N   A VAL   B 100 ? 0.2695 0.2351 0.2338 0.0293  0.0534  0.0849  100 VAL   B N   
5078 N  N   B VAL   B 100 ? 0.2755 0.2353 0.2312 0.0344  0.0425  0.0758  100 VAL   B N   
5079 C  CA  A VAL   B 100 ? 0.2959 0.2532 0.2824 0.0185  0.0625  0.0920  100 VAL   B CA  
5080 C  CA  B VAL   B 100 ? 0.2988 0.2509 0.2691 0.0282  0.0418  0.0808  100 VAL   B CA  
5081 C  C   A VAL   B 100 ? 0.3171 0.2575 0.2767 0.0283  0.0595  0.1039  100 VAL   B C   
5082 C  C   B VAL   B 100 ? 0.3168 0.2565 0.2715 0.0335  0.0438  0.0945  100 VAL   B C   
5083 O  O   A VAL   B 100 ? 0.3266 0.2684 0.2831 0.0260  0.0657  0.0990  100 VAL   B O   
5084 O  O   B VAL   B 100 ? 0.3211 0.2617 0.2767 0.0314  0.0446  0.0920  100 VAL   B O   
5085 C  CB  A VAL   B 100 ? 0.3058 0.2691 0.3497 -0.0076 0.0598  0.0927  100 VAL   B CB  
5086 C  CB  B VAL   B 100 ? 0.3051 0.2613 0.3075 0.0150  0.0368  0.0751  100 VAL   B CB  
5087 C  CG1 A VAL   B 100 ? 0.3106 0.2745 0.3736 -0.0135 0.0593  0.0909  100 VAL   B CG1 
5088 C  CG1 B VAL   B 100 ? 0.3084 0.2652 0.3207 0.0121  0.0358  0.0731  100 VAL   B CG1 
5089 C  CG2 A VAL   B 100 ? 0.3090 0.2736 0.3655 -0.0149 0.0616  0.0974  100 VAL   B CG2 
5090 C  CG2 B VAL   B 100 ? 0.3063 0.2641 0.3176 0.0108  0.0365  0.0745  100 VAL   B CG2 
5109 N  N   . ASN   B 101 ? 0.3307 0.2595 0.2694 0.0422  0.0443  0.1063  101 ASN   B N   
5110 C  CA  . ASN   B 101 ? 0.3699 0.2750 0.3013 0.0515  0.0223  0.1157  101 ASN   B CA  
5111 C  C   . ASN   B 101 ? 0.4075 0.3051 0.2957 0.0546  0.0081  0.1249  101 ASN   B C   
5112 O  O   . ASN   B 101 ? 0.4122 0.3210 0.3225 0.0590  0.0058  0.0989  101 ASN   B O   
5113 C  CB  . ASN   B 101 ? 0.3705 0.2653 0.3144 0.0496  0.0243  0.1079  101 ASN   B CB  
5114 C  CG  . ASN   B 101 ? 0.3692 0.2502 0.3229 0.0476  0.0307  0.1096  101 ASN   B CG  
5115 O  OD1 . ASN   B 101 ? 0.3730 0.2514 0.3577 0.0370  0.0493  0.1004  101 ASN   B OD1 
5116 N  ND2 . ASN   B 101 ? 0.3665 0.2497 0.3251 0.0451  0.0276  0.0996  101 ASN   B ND2 
5124 N  N   . LYS   B 102 ? 0.4375 0.3276 0.2991 0.0460  0.0105  0.1187  102 LYS   B N   
5125 C  CA  . LYS   B 102 ? 0.4651 0.3659 0.3284 0.0323  0.0205  0.0972  102 LYS   B CA  
5126 C  C   . LYS   B 102 ? 0.4588 0.3686 0.3110 0.0320  0.0363  0.0954  102 LYS   B C   
5127 O  O   . LYS   B 102 ? 0.4703 0.3757 0.3152 0.0330  0.0255  0.0853  102 LYS   B O   
5128 C  CB  . LYS   B 102 ? 0.4931 0.3985 0.3856 0.0222  0.0256  0.0667  102 LYS   B CB  
5129 C  CG  . LYS   B 102 ? 0.5158 0.4277 0.4590 0.0161  0.0288  0.0327  102 LYS   B CG  
5130 C  CD  . LYS   B 102 ? 0.5358 0.4513 0.5187 0.0108  0.0326  0.0054  102 LYS   B CD  
5131 C  CE  . LYS   B 102 ? 0.5491 0.4658 0.5703 0.0051  0.0374  -0.0121 102 LYS   B CE  
5132 N  NZ  . LYS   B 102 ? 0.5560 0.4737 0.6002 0.0017  0.0411  -0.0207 102 LYS   B NZ  
5146 N  N   A GLY   B 103 ? 0.4475 0.3651 0.2955 0.0311  0.0639  0.1023  103 GLY   B N   
5147 N  N   B GLY   B 103 ? 0.4474 0.3667 0.3126 0.0268  0.0367  0.0878  103 GLY   B N   
5148 C  CA  A GLY   B 103 ? 0.4357 0.3614 0.2992 0.0299  0.0921  0.0946  103 GLY   B CA  
5149 C  CA  B GLY   B 103 ? 0.4339 0.3623 0.3215 0.0213  0.0393  0.0727  103 GLY   B CA  
5150 C  C   A GLY   B 103 ? 0.4208 0.3509 0.2949 0.0249  0.1134  0.0868  103 GLY   B C   
5151 C  C   B GLY   B 103 ? 0.4180 0.3540 0.3229 0.0143  0.0397  0.0569  103 GLY   B C   
5152 O  O   A GLY   B 103 ? 0.4260 0.3569 0.3123 0.0235  0.1095  0.0849  103 GLY   B O   
5153 O  O   B GLY   B 103 ? 0.4199 0.3558 0.3305 0.0140  0.0395  0.0557  103 GLY   B O   
5160 N  N   A GLU   B 104 ? 0.3987 0.3311 0.2753 0.0226  0.1312  0.0699  104 GLU   B N   
5161 N  N   B GLU   B 104 ? 0.3993 0.3420 0.3134 0.0075  0.0383  0.0389  104 GLU   B N   
5162 C  CA  A GLU   B 104 ? 0.3748 0.3117 0.2437 0.0201  0.1379  0.0565  104 GLU   B CA  
5163 C  CA  B GLU   B 104 ? 0.3799 0.3298 0.2996 0.0008  0.0344  0.0227  104 GLU   B CA  
5164 C  C   A GLU   B 104 ? 0.3791 0.3103 0.2649 0.0117  0.1516  0.0425  104 GLU   B C   
5165 C  C   B GLU   B 104 ? 0.3725 0.3255 0.3059 -0.0042 0.0438  0.0135  104 GLU   B C   
5166 O  O   A GLU   B 104 ? 0.3822 0.3113 0.2997 0.0093  0.1438  0.0310  104 GLU   B O   
5167 O  O   B GLU   B 104 ? 0.3722 0.3250 0.3131 -0.0053 0.0434  0.0081  104 GLU   B O   
5168 C  CB  A GLU   B 104 ? 0.3539 0.2929 0.2269 0.0289  0.1095  0.0378  104 GLU   B CB  
5169 C  CB  B GLU   B 104 ? 0.3697 0.3207 0.2839 -0.0010 0.0207  0.0127  104 GLU   B CB  
5170 C  CG  A GLU   B 104 ? 0.3376 0.2783 0.2122 0.0395  0.0666  0.0072  104 GLU   B CG  
5171 C  CG  B GLU   B 104 ? 0.3612 0.3123 0.2692 -0.0018 0.0055  0.0007  104 GLU   B CG  
5172 C  CD  A GLU   B 104 ? 0.3216 0.2601 0.1976 0.0488  0.0370  0.0003  104 GLU   B CD  
5173 C  CD  B GLU   B 104 ? 0.3543 0.3041 0.2615 -0.0031 -0.0040 -0.0042 104 GLU   B CD  
5174 O  OE1 A GLU   B 104 ? 0.2975 0.2411 0.1511 0.0514  0.0486  0.0108  104 GLU   B OE1 
5175 O  OE1 B GLU   B 104 ? 0.3490 0.2987 0.2538 -0.0058 -0.0029 -0.0038 104 GLU   B OE1 
5176 O  OE2 A GLU   B 104 ? 0.3303 0.2712 0.2282 0.0460  -0.0022 -0.0133 104 GLU   B OE2 
5177 O  OE2 B GLU   B 104 ? 0.3546 0.3045 0.2648 -0.0034 -0.0151 -0.0099 104 GLU   B OE2 
5190 N  N   A ASP   B 105 ? 0.3756 0.3121 0.2677 -0.0000 0.1720  0.0468  105 ASP   B N   
5191 N  N   B ASP   B 105 ? 0.3650 0.3236 0.3091 -0.0095 0.0533  0.0118  105 ASP   B N   
5192 C  CA  A ASP   B 105 ? 0.3749 0.3137 0.2916 -0.0093 0.1868  0.0382  105 ASP   B CA  
5193 C  CA  B ASP   B 105 ? 0.3594 0.3216 0.3171 -0.0133 0.0614  0.0086  105 ASP   B CA  
5194 C  C   A ASP   B 105 ? 0.3577 0.2793 0.2811 -0.0142 0.1827  0.0265  105 ASP   B C   
5195 C  C   B ASP   B 105 ? 0.3501 0.3113 0.3028 -0.0146 0.0625  0.0023  105 ASP   B C   
5196 O  O   A ASP   B 105 ? 0.3448 0.2708 0.2785 -0.0134 0.1800  0.0239  105 ASP   B O   
5197 O  O   B ASP   B 105 ? 0.3477 0.3090 0.2962 -0.0151 0.0640  0.0011  105 ASP   B O   
5198 C  CB  A ASP   B 105 ? 0.3931 0.3439 0.3499 -0.0018 0.1904  0.0240  105 ASP   B CB  
5199 C  CB  B ASP   B 105 ? 0.3620 0.3283 0.3408 -0.0131 0.0677  0.0092  105 ASP   B CB  
5200 C  CG  A ASP   B 105 ? 0.4025 0.3632 0.3920 -0.0004 0.2022  0.0168  105 ASP   B CG  
5201 C  CG  B ASP   B 105 ? 0.3634 0.3317 0.3607 -0.0148 0.0732  0.0118  105 ASP   B CG  
5202 O  OD1 A ASP   B 105 ? 0.4036 0.3701 0.3930 -0.0083 0.2125  0.0265  105 ASP   B OD1 
5203 O  OD1 B ASP   B 105 ? 0.3634 0.3325 0.3651 -0.0175 0.0743  0.0136  105 ASP   B OD1 
5204 O  OD2 A ASP   B 105 ? 0.4073 0.3728 0.4321 0.0059  0.1919  0.0020  105 ASP   B OD2 
5205 O  OD2 B ASP   B 105 ? 0.3626 0.3337 0.3694 -0.0162 0.0759  0.0147  105 ASP   B OD2 
5214 N  N   A ILE   B 106 ? 0.3506 0.2518 0.2995 -0.0128 0.1594  0.0237  106 ILE   B N   
5215 N  N   B ILE   B 106 ? 0.3429 0.3033 0.3007 -0.0132 0.0592  -0.0003 106 ILE   B N   
5216 C  CA  A ILE   B 106 ? 0.3321 0.2261 0.3177 -0.0184 0.1597  0.0227  106 ILE   B CA  
5217 C  CA  B ILE   B 106 ? 0.3330 0.2963 0.3036 -0.0123 0.0597  -0.0026 106 ILE   B CA  
5218 C  C   A ILE   B 106 ? 0.2993 0.2196 0.3109 -0.0179 0.1571  0.0019  106 ILE   B C   
5219 C  C   B ILE   B 106 ? 0.3172 0.2919 0.3013 -0.0114 0.0594  -0.0102 106 ILE   B C   
5220 O  O   A ILE   B 106 ? 0.2854 0.1917 0.3067 -0.0229 0.1449  -0.0075 106 ILE   B O   
5221 O  O   B ILE   B 106 ? 0.3146 0.2877 0.2956 -0.0148 0.0532  -0.0150 106 ILE   B O   
5222 C  CB  A ILE   B 106 ? 0.3504 0.2186 0.3390 -0.0202 0.1482  0.0366  106 ILE   B CB  
5223 C  CB  B ILE   B 106 ? 0.3390 0.2958 0.3079 -0.0117 0.0594  0.0019  106 ILE   B CB  
5224 C  CG1 A ILE   B 106 ? 0.3608 0.2182 0.3463 -0.0111 0.1335  0.0321  106 ILE   B CG1 
5225 C  CG1 B ILE   B 106 ? 0.3427 0.2962 0.3108 -0.0085 0.0559  0.0034  106 ILE   B CG1 
5226 C  CG2 A ILE   B 106 ? 0.3562 0.2206 0.3563 -0.0266 0.1458  0.0432  106 ILE   B CG2 
5227 C  CG2 B ILE   B 106 ? 0.3404 0.2965 0.3125 -0.0131 0.0606  0.0032  106 ILE   B CG2 
5228 C  CD1 A ILE   B 106 ? 0.3639 0.2177 0.3404 -0.0021 0.1328  0.0365  106 ILE   B CD1 
5229 C  CD1 B ILE   B 106 ? 0.3444 0.2964 0.3124 -0.0056 0.0556  0.0062  106 ILE   B CD1 
5252 N  N   A GLN   B 107 ? 0.2861 0.2440 0.3262 -0.0216 0.1506  0.0011  107 GLN   B N   
5253 N  N   B GLN   B 107 ? 0.3045 0.2923 0.3127 -0.0090 0.0621  -0.0122 107 GLN   B N   
5254 C  CA  A GLN   B 107 ? 0.2712 0.2640 0.3384 -0.0234 0.1421  0.0053  107 GLN   B CA  
5255 C  CA  B GLN   B 107 ? 0.2909 0.2900 0.3260 -0.0057 0.0655  -0.0101 107 GLN   B CA  
5256 C  C   A GLN   B 107 ? 0.2473 0.2454 0.3120 -0.0094 0.1036  -0.0064 107 GLN   B C   
5257 C  C   B GLN   B 107 ? 0.2599 0.2643 0.2984 0.0007  0.0696  -0.0136 107 GLN   B C   
5258 O  O   A GLN   B 107 ? 0.2468 0.2419 0.3443 -0.0019 0.0718  -0.0211 107 GLN   B O   
5259 O  O   B GLN   B 107 ? 0.2610 0.2663 0.3085 0.0024  0.0587  -0.0211 107 GLN   B O   
5260 C  CB  A GLN   B 107 ? 0.2968 0.3028 0.3950 -0.0283 0.1387  0.0126  107 GLN   B CB  
5261 C  CB  B GLN   B 107 ? 0.3098 0.3113 0.3690 -0.0062 0.0591  -0.0059 107 GLN   B CB  
5262 C  CG  A GLN   B 107 ? 0.3304 0.3353 0.4629 -0.0203 0.1071  0.0121  107 GLN   B CG  
5263 C  CG  B GLN   B 107 ? 0.3281 0.3291 0.4139 -0.0036 0.0476  -0.0030 107 GLN   B CG  
5264 C  CD  A GLN   B 107 ? 0.3534 0.3563 0.5141 -0.0162 0.0865  0.0147  107 GLN   B CD  
5265 C  CD  B GLN   B 107 ? 0.3417 0.3417 0.4499 -0.0018 0.0391  0.0002  107 GLN   B CD  
5266 O  OE1 A GLN   B 107 ? 0.3607 0.3655 0.5345 -0.0094 0.0847  0.0113  107 GLN   B OE1 
5267 O  OE1 B GLN   B 107 ? 0.3473 0.3477 0.4641 0.0006  0.0385  -0.0005 107 GLN   B OE1 
5268 N  NE2 A GLN   B 107 ? 0.3659 0.3621 0.5332 -0.0152 0.0767  0.0205  107 GLN   B NE2 
5269 N  NE2 B GLN   B 107 ? 0.3477 0.3449 0.4633 -0.0013 0.0358  0.0034  107 GLN   B NE2 
5286 N  N   . LEU   B 108 ? 0.2274 0.2366 0.2696 0.0087  0.0810  -0.0096 108 LEU   B N   
5287 C  CA  . LEU   B 108 ? 0.2087 0.2172 0.2356 0.0257  0.0523  0.0003  108 LEU   B CA  
5288 C  C   . LEU   B 108 ? 0.1785 0.1818 0.2241 0.0217  0.0356  0.0199  108 LEU   B C   
5289 O  O   . LEU   B 108 ? 0.1824 0.1713 0.2200 0.0221  0.0258  0.0243  108 LEU   B O   
5290 C  CB  . LEU   B 108 ? 0.2262 0.2418 0.2146 0.0278  0.0523  -0.0014 108 LEU   B CB  
5291 C  CG  . LEU   B 108 ? 0.2472 0.2722 0.2222 0.0294  0.0462  -0.0167 108 LEU   B CG  
5292 C  CD1 . LEU   B 108 ? 0.2545 0.2886 0.2076 0.0162  0.0512  -0.0155 108 LEU   B CD1 
5293 C  CD2 . LEU   B 108 ? 0.2678 0.2858 0.2556 0.0365  0.0350  -0.0254 108 LEU   B CD2 
5306 N  N   . LEU   B 109 ? 0.1708 0.1630 0.2158 0.0133  0.0353  0.0260  109 LEU   B N   
5307 C  CA  . LEU   B 109 ? 0.1549 0.1400 0.2220 0.0076  0.0269  0.0303  109 LEU   B CA  
5308 C  C   . LEU   B 109 ? 0.1444 0.1288 0.2200 0.0055  0.0321  0.0148  109 LEU   B C   
5309 O  O   . LEU   B 109 ? 0.1430 0.1292 0.2127 0.0049  0.0270  0.0268  109 LEU   B O   
5310 C  CB  . LEU   B 109 ? 0.1608 0.1347 0.2199 0.0140  0.0179  0.0324  109 LEU   B CB  
5311 C  CG  . LEU   B 109 ? 0.1611 0.1326 0.2169 0.0075  0.0122  0.0202  109 LEU   B CG  
5312 C  CD1 . LEU   B 109 ? 0.1575 0.1443 0.2152 0.0117  0.0209  0.0168  109 LEU   B CD1 
5313 C  CD2 . LEU   B 109 ? 0.1782 0.1374 0.2344 0.0118  0.0026  0.0131  109 LEU   B CD2 
5325 N  N   . LYS   B 110 ? 0.1406 0.1274 0.2212 -0.0022 0.0356  0.0235  110 LYS   B N   
5326 C  CA  . LYS   B 110 ? 0.1396 0.1226 0.2171 0.0018  0.0232  0.0143  110 LYS   B CA  
5327 C  C   . LYS   B 110 ? 0.1357 0.1268 0.2035 -0.0014 0.0217  0.0094  110 LYS   B C   
5328 O  O   . LYS   B 110 ? 0.1352 0.1261 0.1908 -0.0049 0.0154  0.0056  110 LYS   B O   
5329 C  CB  . LYS   B 110 ? 0.1453 0.1295 0.2329 -0.0027 0.0233  0.0105  110 LYS   B CB  
5330 C  CG  . LYS   B 110 ? 0.1520 0.1279 0.2378 -0.0044 0.0122  0.0113  110 LYS   B CG  
5331 C  CD  . LYS   B 110 ? 0.1490 0.1292 0.2433 -0.0056 0.0173  0.0152  110 LYS   B CD  
5332 C  CE  . LYS   B 110 ? 0.1452 0.1434 0.2677 -0.0025 0.0187  0.0083  110 LYS   B CE  
5333 N  NZ  . LYS   B 110 ? 0.1420 0.1543 0.2549 0.0020  -0.0001 0.0051  110 LYS   B NZ  
5347 N  N   . SER   B 111 ? 0.1486 0.1292 0.2048 -0.0035 0.0276  0.0139  111 SER   B N   
5348 C  CA  . SER   B 111 ? 0.1470 0.1328 0.1905 0.0026  0.0112  0.0154  111 SER   B CA  
5349 C  C   . SER   B 111 ? 0.1415 0.1325 0.1843 0.0009  0.0056  0.0106  111 SER   B C   
5350 O  O   . SER   B 111 ? 0.1377 0.1352 0.1976 -0.0024 0.0090  0.0129  111 SER   B O   
5351 C  CB  . SER   B 111 ? 0.1620 0.1559 0.2056 0.0021  0.0253  0.0271  111 SER   B CB  
5352 O  OG  . SER   B 111 ? 0.1798 0.1934 0.2149 0.0073  0.0399  0.0363  111 SER   B OG  
5358 N  N   . ALA   B 112 ? 0.1320 0.1326 0.2003 0.0022  0.0122  0.0211  112 ALA   B N   
5359 C  CA  . ALA   B 112 ? 0.1277 0.1371 0.1907 0.0037  0.0072  0.0100  112 ALA   B CA  
5360 C  C   . ALA   B 112 ? 0.1193 0.1283 0.1823 0.0029  0.0068  0.0056  112 ALA   B C   
5361 O  O   . ALA   B 112 ? 0.1214 0.1285 0.1899 -0.0065 0.0099  0.0051  112 ALA   B O   
5362 C  CB  . ALA   B 112 ? 0.1283 0.1435 0.1997 0.0035  0.0130  0.0136  112 ALA   B CB  
5368 N  N   . TYR   B 113 ? 0.1217 0.1231 0.1936 -0.0005 0.0074  0.0081  113 TYR   B N   
5369 C  CA  . TYR   B 113 ? 0.1199 0.1189 0.1829 -0.0023 0.0137  0.0011  113 TYR   B CA  
5370 C  C   . TYR   B 113 ? 0.1168 0.1118 0.1797 -0.0067 0.0073  -0.0015 113 TYR   B C   
5371 O  O   . TYR   B 113 ? 0.1240 0.1166 0.1687 -0.0040 0.0059  0.0000  113 TYR   B O   
5372 C  CB  . TYR   B 113 ? 0.1283 0.1133 0.1975 -0.0010 0.0144  0.0137  113 TYR   B CB  
5373 C  CG  . TYR   B 113 ? 0.1281 0.1131 0.2084 -0.0083 0.0104  0.0139  113 TYR   B CG  
5374 C  CD1 . TYR   B 113 ? 0.1373 0.1122 0.2175 -0.0092 0.0159  0.0169  113 TYR   B CD1 
5375 C  CD2 . TYR   B 113 ? 0.1379 0.1195 0.2139 -0.0040 0.0074  0.0114  113 TYR   B CD2 
5376 C  CE1 . TYR   B 113 ? 0.1391 0.1190 0.2099 -0.0009 0.0148  0.0091  113 TYR   B CE1 
5377 C  CE2 . TYR   B 113 ? 0.1420 0.1096 0.2188 0.0018  0.0058  0.0094  113 TYR   B CE2 
5378 C  CZ  . TYR   B 113 ? 0.1325 0.1139 0.2216 0.0092  0.0097  0.0065  113 TYR   B CZ  
5379 O  OH  . TYR   B 113 ? 0.1410 0.1130 0.2384 0.0105  0.0146  0.0040  113 TYR   B OH  
5389 N  N   . GLU   B 114 ? 0.1178 0.1100 0.1848 0.0002  0.0097  0.0033  114 GLU   B N   
5390 C  CA  . GLU   B 114 ? 0.1201 0.1105 0.1853 0.0018  0.0025  -0.0028 114 GLU   B CA  
5391 C  C   . GLU   B 114 ? 0.1204 0.1127 0.1773 -0.0021 0.0095  -0.0009 114 GLU   B C   
5392 O  O   . GLU   B 114 ? 0.1229 0.1075 0.1823 0.0008  0.0042  0.0100  114 GLU   B O   
5393 C  CB  . GLU   B 114 ? 0.1213 0.1133 0.1941 -0.0021 0.0121  0.0052  114 GLU   B CB  
5394 C  CG  . GLU   B 114 ? 0.1275 0.1184 0.1913 -0.0015 0.0143  0.0082  114 GLU   B CG  
5395 C  CD  . GLU   B 114 ? 0.1221 0.1237 0.1894 -0.0053 0.0098  0.0012  114 GLU   B CD  
5396 O  OE1 . GLU   B 114 ? 0.1248 0.1390 0.1862 -0.0080 0.0170  0.0077  114 GLU   B OE1 
5397 O  OE2 . GLU   B 114 ? 0.1206 0.1423 0.2057 -0.0177 0.0073  0.0039  114 GLU   B OE2 
5404 N  N   . ASN   B 115 ? 0.1177 0.1116 0.1759 -0.0032 0.0007  0.0035  115 ASN   B N   
5405 C  CA  . ASN   B 115 ? 0.1203 0.1174 0.1680 -0.0054 0.0066  0.0052  115 ASN   B CA  
5406 C  C   . ASN   B 115 ? 0.1205 0.1133 0.1679 -0.0098 0.0020  -0.0001 115 ASN   B C   
5407 O  O   . ASN   B 115 ? 0.1277 0.1190 0.1735 -0.0118 0.0043  0.0029  115 ASN   B O   
5408 C  CB  . ASN   B 115 ? 0.1305 0.1296 0.1671 -0.0050 0.0054  0.0045  115 ASN   B CB  
5409 C  CG  . ASN   B 115 ? 0.1378 0.1331 0.1726 0.0044  0.0051  -0.0064 115 ASN   B CG  
5410 O  OD1 . ASN   B 115 ? 0.1792 0.1457 0.1800 0.0041  0.0085  -0.0149 115 ASN   B OD1 
5411 N  ND2 . ASN   B 115 ? 0.1417 0.1416 0.1756 -0.0056 0.0073  0.0098  115 ASN   B ND2 
5418 N  N   . PHE   B 116 ? 0.1217 0.1141 0.1595 -0.0041 0.0063  -0.0009 116 PHE   B N   
5419 C  CA  . PHE   B 116 ? 0.1259 0.1148 0.1660 -0.0038 -0.0036 -0.0010 116 PHE   B CA  
5420 C  C   . PHE   B 116 ? 0.1267 0.1039 0.1757 -0.0105 0.0010  0.0068  116 PHE   B C   
5421 O  O   . PHE   B 116 ? 0.1287 0.1160 0.1717 -0.0038 -0.0025 0.0085  116 PHE   B O   
5422 C  CB  . PHE   B 116 ? 0.1262 0.1138 0.1637 -0.0061 -0.0126 0.0009  116 PHE   B CB  
5423 C  CG  . PHE   B 116 ? 0.1158 0.1153 0.1618 -0.0065 -0.0082 0.0024  116 PHE   B CG  
5424 C  CD1 . PHE   B 116 ? 0.1240 0.1142 0.1844 0.0004  0.0012  0.0041  116 PHE   B CD1 
5425 C  CD2 . PHE   B 116 ? 0.1275 0.1238 0.1575 -0.0077 -0.0018 -0.0011 116 PHE   B CD2 
5426 C  CE1 . PHE   B 116 ? 0.1251 0.1222 0.1846 -0.0051 -0.0157 0.0054  116 PHE   B CE1 
5427 C  CE2 . PHE   B 116 ? 0.1258 0.1264 0.1644 0.0018  0.0008  0.0118  116 PHE   B CE2 
5428 C  CZ  . PHE   B 116 ? 0.1165 0.1263 0.1774 -0.0013 -0.0105 0.0104  116 PHE   B CZ  
5438 N  N   . ASN   B 117 ? 0.1232 0.1112 0.1835 -0.0004 -0.0042 0.0037  117 ASN   B N   
5439 C  CA  . ASN   B 117 ? 0.1327 0.1156 0.1790 -0.0001 -0.0016 -0.0071 117 ASN   B CA  
5440 C  C   . ASN   B 117 ? 0.1366 0.1111 0.1817 0.0001  -0.0095 0.0058  117 ASN   B C   
5441 O  O   . ASN   B 117 ? 0.1408 0.1211 0.2042 -0.0039 -0.0272 0.0116  117 ASN   B O   
5442 C  CB  . ASN   B 117 ? 0.1338 0.1165 0.1919 -0.0028 -0.0034 -0.0037 117 ASN   B CB  
5443 C  CG  . ASN   B 117 ? 0.1319 0.1183 0.1942 0.0012  -0.0105 -0.0038 117 ASN   B CG  
5444 O  OD1 . ASN   B 117 ? 0.1493 0.1191 0.1992 -0.0160 0.0023  -0.0044 117 ASN   B OD1 
5445 N  ND2 . ASN   B 117 ? 0.1325 0.1205 0.1778 -0.0052 0.0002  -0.0003 117 ASN   B ND2 
5452 N  N   . GLN   B 118 ? 0.1365 0.1060 0.1759 -0.0020 -0.0181 0.0014  118 GLN   B N   
5453 C  CA  . GLN   B 118 ? 0.1405 0.1155 0.1748 0.0036  -0.0047 0.0026  118 GLN   B CA  
5454 C  C   . GLN   B 118 ? 0.1418 0.1142 0.1785 -0.0018 -0.0117 0.0008  118 GLN   B C   
5455 O  O   . GLN   B 118 ? 0.1604 0.1127 0.2147 -0.0080 0.0043  0.0029  118 GLN   B O   
5456 C  CB  . GLN   B 118 ? 0.1506 0.1199 0.1844 0.0058  -0.0100 0.0029  118 GLN   B CB  
5457 C  CG  . GLN   B 118 ? 0.1571 0.1234 0.1855 0.0066  -0.0068 -0.0051 118 GLN   B CG  
5458 C  CD  . GLN   B 118 ? 0.1590 0.1183 0.1809 0.0108  -0.0075 -0.0072 118 GLN   B CD  
5459 O  OE1 . GLN   B 118 ? 0.1652 0.1175 0.2054 0.0050  0.0006  0.0069  118 GLN   B OE1 
5460 N  NE2 . GLN   B 118 ? 0.1622 0.1176 0.2010 0.0096  -0.0102 0.0074  118 GLN   B NE2 
5469 N  N   . HIS   B 119 ? 0.1412 0.1183 0.1663 -0.0075 -0.0053 0.0031  119 HIS   B N   
5470 C  CA  . HIS   B 119 ? 0.1494 0.1311 0.1575 -0.0000 -0.0153 0.0079  119 HIS   B CA  
5471 C  C   . HIS   B 119 ? 0.1523 0.1289 0.1628 -0.0010 -0.0266 0.0063  119 HIS   B C   
5472 O  O   . HIS   B 119 ? 0.1577 0.1229 0.1912 -0.0174 -0.0116 0.0064  119 HIS   B O   
5473 C  CB  . HIS   B 119 ? 0.1542 0.1461 0.1651 0.0022  -0.0180 0.0011  119 HIS   B CB  
5474 C  CG  . HIS   B 119 ? 0.1613 0.1642 0.1893 0.0109  -0.0299 -0.0222 119 HIS   B CG  
5475 N  ND1 . HIS   B 119 ? 0.1757 0.1792 0.2209 0.0032  -0.0411 -0.0393 119 HIS   B ND1 
5476 C  CD2 . HIS   B 119 ? 0.1759 0.1772 0.1978 0.0398  -0.0431 -0.0198 119 HIS   B CD2 
5477 C  CE1 . HIS   B 119 ? 0.1957 0.1894 0.2281 0.0200  -0.0485 -0.0490 119 HIS   B CE1 
5478 N  NE2 . HIS   B 119 ? 0.1963 0.1999 0.2113 0.0323  -0.0457 -0.0451 119 HIS   B NE2 
5486 N  N   . GLU   B 120 ? 0.1717 0.1289 0.1593 -0.0112 -0.0312 0.0126  120 GLU   B N   
5487 C  CA  . GLU   B 120 ? 0.1944 0.1441 0.1716 -0.0019 -0.0378 0.0129  120 GLU   B CA  
5488 C  C   . GLU   B 120 ? 0.1763 0.1373 0.1524 -0.0120 -0.0291 0.0228  120 GLU   B C   
5489 O  O   . GLU   B 120 ? 0.1727 0.1467 0.1618 -0.0149 -0.0227 0.0074  120 GLU   B O   
5490 C  CB  . GLU   B 120 ? 0.2520 0.1791 0.2324 0.0189  -0.0646 0.0290  120 GLU   B CB  
5491 C  CG  . GLU   B 120 ? 0.3067 0.2407 0.3212 0.0265  -0.0819 0.0459  120 GLU   B CG  
5492 C  CD  . GLU   B 120 ? 0.3436 0.2915 0.4126 0.0177  -0.0815 0.0579  120 GLU   B CD  
5493 O  OE1 . GLU   B 120 ? 0.3607 0.3177 0.4440 0.0066  -0.0730 0.0712  120 GLU   B OE1 
5494 O  OE2 . GLU   B 120 ? 0.3718 0.3116 0.4699 0.0151  -0.0791 0.0490  120 GLU   B OE2 
5501 N  N   . VAL   B 121 ? 0.1659 0.1274 0.1554 -0.0156 -0.0116 0.0080  121 VAL   B N   
5502 C  CA  . VAL   B 121 ? 0.1648 0.1436 0.1493 -0.0195 -0.0100 0.0126  121 VAL   B CA  
5503 C  C   . VAL   B 121 ? 0.1524 0.1420 0.1430 -0.0223 -0.0184 0.0110  121 VAL   B C   
5504 O  O   . VAL   B 121 ? 0.1570 0.1333 0.1678 -0.0283 -0.0247 0.0040  121 VAL   B O   
5505 C  CB  . VAL   B 121 ? 0.1900 0.1738 0.1572 -0.0093 -0.0152 0.0203  121 VAL   B CB  
5506 C  CG1 . VAL   B 121 ? 0.1954 0.1846 0.1811 -0.0178 -0.0067 0.0203  121 VAL   B CG1 
5507 C  CG2 . VAL   B 121 ? 0.2150 0.1920 0.1658 -0.0029 -0.0102 0.0091  121 VAL   B CG2 
5517 N  N   . LEU   B 122 ? 0.1475 0.1323 0.1497 -0.0150 -0.0177 0.0073  122 LEU   B N   
5518 C  CA  . LEU   B 122 ? 0.1343 0.1359 0.1429 -0.0181 -0.0132 0.0056  122 LEU   B CA  
5519 C  C   . LEU   B 122 ? 0.1341 0.1245 0.1547 -0.0270 -0.0156 0.0095  122 LEU   B C   
5520 O  O   . LEU   B 122 ? 0.1464 0.1275 0.1784 -0.0250 -0.0222 -0.0003 122 LEU   B O   
5521 C  CB  . LEU   B 122 ? 0.1537 0.1498 0.1631 0.0024  -0.0247 0.0147  122 LEU   B CB  
5522 C  CG  . LEU   B 122 ? 0.1487 0.1532 0.1728 -0.0112 -0.0085 0.0060  122 LEU   B CG  
5523 C  CD1 . LEU   B 122 ? 0.1545 0.1781 0.1782 -0.0176 -0.0098 0.0068  122 LEU   B CD1 
5524 C  CD2 . LEU   B 122 ? 0.1504 0.1483 0.1626 -0.0095 -0.0029 -0.0059 122 LEU   B CD2 
5536 N  N   . LEU   B 123 ? 0.1391 0.1167 0.1526 -0.0218 -0.0045 0.0031  123 LEU   B N   
5537 C  CA  . LEU   B 123 ? 0.1430 0.1151 0.1525 -0.0220 -0.0115 -0.0030 123 LEU   B CA  
5538 C  C   . LEU   B 123 ? 0.1391 0.1130 0.1495 -0.0233 -0.0102 0.0020  123 LEU   B C   
5539 O  O   . LEU   B 123 ? 0.1500 0.1168 0.1412 -0.0278 -0.0132 0.0012  123 LEU   B O   
5540 C  CB  . LEU   B 123 ? 0.1475 0.1200 0.1541 -0.0194 -0.0086 -0.0062 123 LEU   B CB  
5541 C  CG  . LEU   B 123 ? 0.1465 0.1283 0.1650 -0.0139 0.0018  0.0033  123 LEU   B CG  
5542 C  CD1 . LEU   B 123 ? 0.1554 0.1371 0.1691 -0.0154 0.0086  -0.0066 123 LEU   B CD1 
5543 C  CD2 . LEU   B 123 ? 0.1582 0.1344 0.1787 -0.0127 0.0055  0.0176  123 LEU   B CD2 
5555 N  N   . ALA   B 124 ? 0.1366 0.1163 0.1443 -0.0177 -0.0060 -0.0028 124 ALA   B N   
5556 C  CA  . ALA   B 124 ? 0.1320 0.1195 0.1563 -0.0153 -0.0037 -0.0071 124 ALA   B CA  
5557 C  C   . ALA   B 124 ? 0.1239 0.1204 0.1582 -0.0172 -0.0011 0.0009  124 ALA   B C   
5558 O  O   . ALA   B 124 ? 0.1383 0.1234 0.1571 -0.0132 -0.0057 -0.0022 124 ALA   B O   
5559 C  CB  . ALA   B 124 ? 0.1328 0.1251 0.1652 -0.0077 -0.0005 0.0119  124 ALA   B CB  
5565 N  N   . PRO   B 125 ? 0.1350 0.1185 0.1446 -0.0156 -0.0045 0.0108  125 PRO   B N   
5566 C  CA  . PRO   B 125 ? 0.1456 0.1216 0.1710 -0.0143 -0.0074 0.0206  125 PRO   B CA  
5567 C  C   . PRO   B 125 ? 0.1392 0.1168 0.1791 -0.0162 -0.0052 0.0072  125 PRO   B C   
5568 O  O   . PRO   B 125 ? 0.1419 0.1124 0.1959 -0.0107 0.0012  0.0127  125 PRO   B O   
5569 C  CB  . PRO   B 125 ? 0.1416 0.1454 0.1896 -0.0174 -0.0206 0.0316  125 PRO   B CB  
5570 C  CG  . PRO   B 125 ? 0.1527 0.1434 0.1647 -0.0248 -0.0183 0.0187  125 PRO   B CG  
5571 C  CD  . PRO   B 125 ? 0.1482 0.1282 0.1495 -0.0236 -0.0002 0.0045  125 PRO   B CD  
5579 N  N   . LEU   B 126 ? 0.1462 0.1134 0.1943 -0.0102 0.0116  0.0140  126 LEU   B N   
5580 C  CA  . LEU   B 126 ? 0.1478 0.1222 0.2031 -0.0087 0.0260  0.0153  126 LEU   B CA  
5581 C  C   . LEU   B 126 ? 0.1471 0.1327 0.2012 0.0026  0.0264  0.0140  126 LEU   B C   
5582 O  O   . LEU   B 126 ? 0.1634 0.1597 0.2109 0.0125  0.0005  -0.0015 126 LEU   B O   
5583 C  CB  . LEU   B 126 ? 0.1698 0.1247 0.2310 -0.0107 0.0302  0.0062  126 LEU   B CB  
5584 C  CG  . LEU   B 126 ? 0.1882 0.1299 0.2360 -0.0204 0.0251  -0.0094 126 LEU   B CG  
5585 C  CD1 . LEU   B 126 ? 0.1958 0.1389 0.2767 -0.0185 0.0209  -0.0164 126 LEU   B CD1 
5586 C  CD2 . LEU   B 126 ? 0.1908 0.1444 0.2383 -0.0249 0.0148  -0.0037 126 LEU   B CD2 
5598 N  N   . LEU   B 127 ? 0.1452 0.1172 0.1990 0.0022  0.0231  0.0130  127 LEU   B N   
5599 C  CA  . LEU   B 127 ? 0.1395 0.1287 0.2003 -0.0042 0.0226  0.0148  127 LEU   B CA  
5600 C  C   . LEU   B 127 ? 0.1355 0.1235 0.2091 -0.0029 0.0168  0.0152  127 LEU   B C   
5601 O  O   . LEU   B 127 ? 0.1407 0.1255 0.2159 -0.0100 0.0063  0.0175  127 LEU   B O   
5602 C  CB  . LEU   B 127 ? 0.1537 0.1258 0.2205 -0.0024 0.0144  0.0297  127 LEU   B CB  
5603 C  CG  . LEU   B 127 ? 0.1676 0.1268 0.2288 0.0061  0.0174  0.0275  127 LEU   B CG  
5604 C  CD1 . LEU   B 127 ? 0.1754 0.1260 0.2280 0.0096  0.0069  0.0114  127 LEU   B CD1 
5605 C  CD2 . LEU   B 127 ? 0.1721 0.1364 0.2414 -0.0058 0.0187  0.0345  127 LEU   B CD2 
5617 N  N   . SER   B 128 ? 0.1426 0.1238 0.2096 0.0011  0.0063  0.0097  128 SER   B N   
5618 C  CA  . SER   B 128 ? 0.1529 0.1334 0.2054 0.0106  -0.0060 0.0242  128 SER   B CA  
5619 C  C   . SER   B 128 ? 0.1639 0.1340 0.2290 0.0071  -0.0218 0.0184  128 SER   B C   
5620 O  O   . SER   B 128 ? 0.1790 0.1343 0.2641 0.0059  -0.0203 0.0313  128 SER   B O   
5621 C  CB  . SER   B 128 ? 0.1643 0.1383 0.1970 0.0112  0.0019  0.0303  128 SER   B CB  
5622 O  OG  . SER   B 128 ? 0.1737 0.1518 0.1975 0.0129  0.0143  0.0334  128 SER   B OG  
5628 N  N   . ALA   B 129 ? 0.1731 0.1396 0.2493 0.0241  -0.0157 0.0077  129 ALA   B N   
5629 C  CA  . ALA   B 129 ? 0.1894 0.1508 0.2599 0.0267  -0.0146 -0.0097 129 ALA   B CA  
5630 C  C   . ALA   B 129 ? 0.1791 0.1446 0.2459 0.0178  0.0079  0.0048  129 ALA   B C   
5631 O  O   . ALA   B 129 ? 0.1635 0.1463 0.2596 0.0125  0.0038  0.0094  129 ALA   B O   
5632 C  CB  . ALA   B 129 ? 0.2115 0.1753 0.2921 0.0317  -0.0068 -0.0197 129 ALA   B CB  
5638 N  N   . GLY   B 130 ? 0.1817 0.1386 0.2500 0.0260  0.0142  0.0008  130 GLY   B N   
5639 C  CA  . GLY   B 130 ? 0.1812 0.1574 0.2689 0.0243  0.0365  0.0027  130 GLY   B CA  
5640 C  C   . GLY   B 130 ? 0.1840 0.1540 0.2548 0.0184  0.0218  0.0135  130 GLY   B C   
5641 O  O   . GLY   B 130 ? 0.2026 0.1617 0.2557 0.0186  0.0196  0.0149  130 GLY   B O   
5645 N  N   . ILE   B 131 ? 0.1776 0.1683 0.2588 0.0350  0.0214  0.0107  131 ILE   B N   
5646 C  CA  . ILE   B 131 ? 0.1951 0.1793 0.2561 0.0279  0.0122  0.0169  131 ILE   B CA  
5647 C  C   . ILE   B 131 ? 0.2053 0.1695 0.2259 0.0191  0.0127  0.0243  131 ILE   B C   
5648 O  O   . ILE   B 131 ? 0.2288 0.1837 0.2304 0.0280  -0.0006 0.0228  131 ILE   B O   
5649 C  CB  . ILE   B 131 ? 0.1905 0.2169 0.2781 0.0237  0.0055  0.0228  131 ILE   B CB  
5650 C  CG1 . ILE   B 131 ? 0.1954 0.2310 0.2824 0.0031  0.0131  0.0290  131 ILE   B CG1 
5651 C  CG2 . ILE   B 131 ? 0.1876 0.2401 0.3026 0.0226  0.0024  0.0136  131 ILE   B CG2 
5652 C  CD1 . ILE   B 131 ? 0.2068 0.2478 0.2870 -0.0139 0.0068  0.0386  131 ILE   B CD1 
5664 N  N   . PHE   B 132 ? 0.1885 0.1521 0.2151 0.0138  0.0190  0.0260  132 PHE   B N   
5665 C  CA  . PHE   B 132 ? 0.1968 0.1554 0.2184 0.0096  0.0268  0.0149  132 PHE   B CA  
5666 C  C   . PHE   B 132 ? 0.2149 0.1720 0.2337 0.0084  0.0410  0.0238  132 PHE   B C   
5667 O  O   . PHE   B 132 ? 0.2353 0.1919 0.2563 0.0122  0.0548  0.0284  132 PHE   B O   
5668 C  CB  . PHE   B 132 ? 0.1758 0.1537 0.2007 0.0103  0.0294  0.0182  132 PHE   B CB  
5669 C  CG  . PHE   B 132 ? 0.1744 0.1614 0.1998 0.0140  0.0175  0.0110  132 PHE   B CG  
5670 C  CD1 . PHE   B 132 ? 0.1806 0.1629 0.2297 0.0074  0.0220  0.0035  132 PHE   B CD1 
5671 C  CD2 . PHE   B 132 ? 0.1750 0.1552 0.1790 0.0215  0.0076  0.0242  132 PHE   B CD2 
5672 C  CE1 . PHE   B 132 ? 0.1846 0.1639 0.2340 0.0045  0.0207  0.0105  132 PHE   B CE1 
5673 C  CE2 . PHE   B 132 ? 0.1836 0.1612 0.1782 0.0164  0.0051  0.0118  132 PHE   B CE2 
5674 C  CZ  . PHE   B 132 ? 0.1885 0.1603 0.2250 0.0065  -0.0002 0.0237  132 PHE   B CZ  
5684 N  N   . GLY   B 133 ? 0.2121 0.1632 0.2212 0.0082  0.0289  0.0427  133 GLY   B N   
5685 C  CA  . GLY   B 133 ? 0.2206 0.1711 0.2327 -0.0082 0.0290  0.0468  133 GLY   B CA  
5686 C  C   . GLY   B 133 ? 0.2246 0.1768 0.2385 -0.0212 0.0385  0.0459  133 GLY   B C   
5687 O  O   . GLY   B 133 ? 0.2436 0.1908 0.2876 -0.0369 0.0374  0.0552  133 GLY   B O   
5691 N  N   . ALA   B 134 ? 0.2052 0.1731 0.2253 -0.0246 0.0299  0.0249  134 ALA   B N   
5692 C  CA  . ALA   B 134 ? 0.2020 0.1701 0.2462 -0.0195 0.0350  0.0044  134 ALA   B CA  
5693 C  C   . ALA   B 134 ? 0.2097 0.1628 0.2436 -0.0119 0.0272  0.0210  134 ALA   B C   
5694 O  O   . ALA   B 134 ? 0.2171 0.1852 0.2624 0.0023  0.0195  0.0190  134 ALA   B O   
5695 C  CB  . ALA   B 134 ? 0.2028 0.1647 0.2664 -0.0074 0.0324  -0.0052 134 ALA   B CB  
5701 N  N   . ASP   B 135 ? 0.2215 0.1553 0.2383 -0.0160 0.0113  0.0252  135 ASP   B N   
5702 C  CA  . ASP   B 135 ? 0.2416 0.1494 0.2646 -0.0132 -0.0047 0.0324  135 ASP   B CA  
5703 C  C   . ASP   B 135 ? 0.2218 0.1417 0.2475 -0.0063 -0.0015 0.0314  135 ASP   B C   
5704 O  O   . ASP   B 135 ? 0.2127 0.1362 0.2621 -0.0110 0.0073  0.0306  135 ASP   B O   
5705 C  CB  . ASP   B 135 ? 0.2732 0.1590 0.2837 -0.0312 -0.0021 0.0374  135 ASP   B CB  
5706 C  CG  . ASP   B 135 ? 0.2987 0.1595 0.3119 -0.0497 0.0025  0.0363  135 ASP   B CG  
5707 O  OD1 . ASP   B 135 ? 0.3088 0.1536 0.3117 -0.0333 -0.0094 0.0317  135 ASP   B OD1 
5708 O  OD2 . ASP   B 135 ? 0.3166 0.1925 0.3716 -0.0618 0.0101  0.0153  135 ASP   B OD2 
5713 N  N   . PRO   B 136 ? 0.2155 0.1460 0.2528 0.0164  -0.0060 0.0237  136 PRO   B N   
5714 C  CA  . PRO   B 136 ? 0.1916 0.1379 0.2533 0.0151  -0.0044 0.0103  136 PRO   B CA  
5715 C  C   . PRO   B 136 ? 0.1724 0.1310 0.2585 0.0126  0.0003  0.0021  136 PRO   B C   
5716 O  O   . PRO   B 136 ? 0.1564 0.1270 0.2598 0.0115  -0.0012 0.0070  136 PRO   B O   
5717 C  CB  . PRO   B 136 ? 0.1970 0.1631 0.2701 0.0313  -0.0097 0.0020  136 PRO   B CB  
5718 C  CG  . PRO   B 136 ? 0.2177 0.1719 0.2843 0.0337  -0.0033 0.0086  136 PRO   B CG  
5719 C  CD  . PRO   B 136 ? 0.2229 0.1623 0.2741 0.0397  -0.0023 0.0198  136 PRO   B CD  
5727 N  N   . ILE   B 137 ? 0.1863 0.1279 0.2587 0.0117  -0.0121 0.0075  137 ILE   B N   
5728 C  CA  . ILE   B 137 ? 0.1951 0.1238 0.2704 -0.0032 -0.0010 0.0014  137 ILE   B CA  
5729 C  C   . ILE   B 137 ? 0.1860 0.1305 0.2607 -0.0049 0.0018  0.0106  137 ILE   B C   
5730 O  O   . ILE   B 137 ? 0.1738 0.1304 0.2598 -0.0087 0.0033  0.0101  137 ILE   B O   
5731 C  CB  . ILE   B 137 ? 0.2225 0.1336 0.3082 -0.0028 -0.0041 0.0031  137 ILE   B CB  
5732 C  CG1 . ILE   B 137 ? 0.2498 0.1453 0.3521 0.0087  0.0019  -0.0103 137 ILE   B CG1 
5733 C  CG2 . ILE   B 137 ? 0.2297 0.1363 0.3215 -0.0229 -0.0074 0.0052  137 ILE   B CG2 
5734 C  CD1 . ILE   B 137 ? 0.2714 0.1690 0.3812 0.0241  -0.0084 -0.0009 137 ILE   B CD1 
5746 N  N   . HIS   B 138 ? 0.1897 0.1255 0.2572 -0.0023 0.0163  0.0124  138 HIS   B N   
5747 C  CA  . HIS   B 138 ? 0.1944 0.1332 0.2580 -0.0067 0.0355  0.0179  138 HIS   B CA  
5748 C  C   . HIS   B 138 ? 0.1790 0.1317 0.2473 -0.0038 0.0302  0.0250  138 HIS   B C   
5749 O  O   . HIS   B 138 ? 0.1666 0.1367 0.2747 0.0058  0.0287  0.0362  138 HIS   B O   
5750 C  CB  . HIS   B 138 ? 0.2171 0.1442 0.2748 -0.0104 0.0485  0.0178  138 HIS   B CB  
5751 C  CG  . HIS   B 138 ? 0.2367 0.1574 0.2792 -0.0101 0.0622  0.0340  138 HIS   B CG  
5752 N  ND1 . HIS   B 138 ? 0.2440 0.1790 0.3026 -0.0065 0.0725  0.0280  138 HIS   B ND1 
5753 C  CD2 . HIS   B 138 ? 0.2545 0.1639 0.2696 -0.0090 0.0662  0.0197  138 HIS   B CD2 
5754 C  CE1 . HIS   B 138 ? 0.2545 0.1810 0.2922 -0.0051 0.0757  0.0241  138 HIS   B CE1 
5755 N  NE2 . HIS   B 138 ? 0.2613 0.1710 0.2749 -0.0012 0.0743  0.0114  138 HIS   B NE2 
5763 N  N   . SER   B 139 ? 0.1765 0.1229 0.2518 0.0025  0.0247  0.0163  139 SER   B N   
5764 C  CA  . SER   B 139 ? 0.1716 0.1183 0.2361 0.0002  0.0175  0.0057  139 SER   B CA  
5765 C  C   . SER   B 139 ? 0.1457 0.1093 0.2305 -0.0030 0.0174  -0.0015 139 SER   B C   
5766 O  O   . SER   B 139 ? 0.1489 0.1147 0.2348 0.0028  -0.0001 0.0019  139 SER   B O   
5767 C  CB  . SER   B 139 ? 0.1795 0.1185 0.2242 0.0047  0.0066  0.0056  139 SER   B CB  
5768 O  OG  . SER   B 139 ? 0.1789 0.1196 0.2368 -0.0018 -0.0065 0.0086  139 SER   B OG  
5774 N  N   . LEU   B 140 ? 0.1504 0.1069 0.2307 -0.0020 0.0163  -0.0040 140 LEU   B N   
5775 C  CA  . LEU   B 140 ? 0.1368 0.1139 0.2334 -0.0029 0.0054  0.0014  140 LEU   B CA  
5776 C  C   . LEU   B 140 ? 0.1388 0.1143 0.2442 -0.0008 0.0065  -0.0060 140 LEU   B C   
5777 O  O   . LEU   B 140 ? 0.1443 0.1169 0.2472 0.0016  0.0050  0.0021  140 LEU   B O   
5778 C  CB  . LEU   B 140 ? 0.1376 0.1158 0.2463 -0.0082 0.0140  -0.0083 140 LEU   B CB  
5779 C  CG  . LEU   B 140 ? 0.1535 0.1171 0.2386 -0.0073 0.0079  0.0028  140 LEU   B CG  
5780 C  CD1 . LEU   B 140 ? 0.1639 0.1251 0.2474 -0.0094 0.0231  -0.0129 140 LEU   B CD1 
5781 C  CD2 . LEU   B 140 ? 0.1711 0.1252 0.2411 -0.0033 0.0071  -0.0134 140 LEU   B CD2 
5793 N  N   . ARG   B 141 ? 0.1344 0.1179 0.2476 -0.0064 0.0142  -0.0018 141 ARG   B N   
5794 C  CA  . ARG   B 141 ? 0.1404 0.1189 0.2767 -0.0128 0.0284  -0.0060 141 ARG   B CA  
5795 C  C   . ARG   B 141 ? 0.1383 0.1199 0.2615 -0.0134 0.0191  -0.0044 141 ARG   B C   
5796 O  O   . ARG   B 141 ? 0.1363 0.1231 0.2704 -0.0135 -0.0004 -0.0114 141 ARG   B O   
5797 C  CB  . ARG   B 141 ? 0.1571 0.1278 0.3106 -0.0217 0.0429  -0.0006 141 ARG   B CB  
5798 C  CG  . ARG   B 141 ? 0.1898 0.1504 0.3415 -0.0241 0.0430  0.0080  141 ARG   B CG  
5799 C  CD  . ARG   B 141 ? 0.2299 0.1743 0.3481 -0.0177 0.0206  -0.0018 141 ARG   B CD  
5800 N  NE  . ARG   B 141 ? 0.2505 0.1739 0.3428 -0.0299 0.0266  -0.0089 141 ARG   B NE  
5801 C  CZ  . ARG   B 141 ? 0.2616 0.1568 0.3340 -0.0259 0.0311  -0.0245 141 ARG   B CZ  
5802 N  NH1 . ARG   B 141 ? 0.2749 0.1463 0.3303 -0.0247 0.0259  -0.0278 141 ARG   B NH1 
5803 N  NH2 . ARG   B 141 ? 0.2689 0.1710 0.3481 -0.0129 0.0226  -0.0164 141 ARG   B NH2 
5817 N  N   . VAL   B 142 ? 0.1415 0.1176 0.2391 -0.0109 0.0241  -0.0102 142 VAL   B N   
5818 C  CA  . VAL   B 142 ? 0.1384 0.1201 0.2426 -0.0086 0.0146  -0.0048 142 VAL   B CA  
5819 C  C   . VAL   B 142 ? 0.1338 0.1212 0.2492 -0.0083 0.0105  -0.0060 142 VAL   B C   
5820 O  O   . VAL   B 142 ? 0.1399 0.1175 0.2524 -0.0026 0.0137  -0.0063 142 VAL   B O   
5821 C  CB  . VAL   B 142 ? 0.1458 0.1257 0.2520 0.0031  0.0294  0.0079  142 VAL   B CB  
5822 C  CG1 . VAL   B 142 ? 0.1471 0.1183 0.2560 0.0104  0.0300  0.0141  142 VAL   B CG1 
5823 C  CG2 . VAL   B 142 ? 0.1675 0.1339 0.2662 0.0053  0.0263  0.0071  142 VAL   B CG2 
5833 N  N   . CYS   B 143 ? 0.1311 0.1157 0.2342 -0.0026 0.0108  0.0066  143 CYS   B N   
5834 C  CA  . CYS   B 143 ? 0.1268 0.1161 0.2255 -0.0079 0.0034  0.0014  143 CYS   B CA  
5835 C  C   . CYS   B 143 ? 0.1221 0.1183 0.2249 -0.0064 0.0052  -0.0012 143 CYS   B C   
5836 O  O   . CYS   B 143 ? 0.1308 0.1236 0.2327 -0.0068 -0.0005 -0.0021 143 CYS   B O   
5837 C  CB  . CYS   B 143 ? 0.1333 0.1223 0.2272 -0.0102 0.0080  -0.0008 143 CYS   B CB  
5838 S  SG  . CYS   B 143 ? 0.1364 0.1416 0.2283 -0.0032 0.0085  0.0018  143 CYS   B SG  
5844 N  N   . VAL   B 144 ? 0.1319 0.1187 0.2326 -0.0079 0.0077  -0.0093 144 VAL   B N   
5845 C  CA  . VAL   B 144 ? 0.1385 0.1256 0.2523 -0.0108 -0.0017 -0.0192 144 VAL   B CA  
5846 C  C   . VAL   B 144 ? 0.1389 0.1281 0.2560 -0.0104 -0.0015 0.0010  144 VAL   B C   
5847 O  O   . VAL   B 144 ? 0.1482 0.1494 0.2767 -0.0003 -0.0035 0.0162  144 VAL   B O   
5848 C  CB  . VAL   B 144 ? 0.1598 0.1471 0.3227 -0.0107 -0.0213 -0.0281 144 VAL   B CB  
5849 C  CG1 . VAL   B 144 ? 0.1882 0.1888 0.3513 -0.0060 -0.0310 -0.0236 144 VAL   B CG1 
5850 C  CG2 . VAL   B 144 ? 0.1700 0.1433 0.3108 -0.0054 -0.0353 -0.0339 144 VAL   B CG2 
5860 N  N   . ASP   B 145 ? 0.1338 0.1214 0.2678 -0.0082 0.0012  -0.0131 145 ASP   B N   
5861 C  CA  . ASP   B 145 ? 0.1322 0.1283 0.2899 -0.0002 0.0039  -0.0113 145 ASP   B CA  
5862 C  C   . ASP   B 145 ? 0.1308 0.1301 0.2729 -0.0020 0.0082  -0.0139 145 ASP   B C   
5863 O  O   . ASP   B 145 ? 0.1321 0.1485 0.3288 -0.0058 0.0177  -0.0317 145 ASP   B O   
5864 C  CB  . ASP   B 145 ? 0.1497 0.1358 0.3294 -0.0133 0.0217  -0.0071 145 ASP   B CB  
5865 C  CG  . ASP   B 145 ? 0.1633 0.1402 0.3749 -0.0242 0.0238  -0.0039 145 ASP   B CG  
5866 O  OD1 . ASP   B 145 ? 0.1648 0.1436 0.3851 -0.0225 -0.0004 -0.0200 145 ASP   B OD1 
5867 O  OD2 . ASP   B 145 ? 0.1935 0.1498 0.4259 -0.0294 0.0550  0.0021  145 ASP   B OD2 
5872 N  N   . THR   B 146 ? 0.1245 0.1216 0.2356 -0.0086 -0.0013 -0.0027 146 THR   B N   
5873 C  CA  . THR   B 146 ? 0.1310 0.1181 0.2188 -0.0029 0.0079  -0.0052 146 THR   B CA  
5874 C  C   . THR   B 146 ? 0.1312 0.1162 0.2222 -0.0049 0.0025  -0.0046 146 THR   B C   
5875 O  O   . THR   B 146 ? 0.1385 0.1163 0.2273 -0.0054 -0.0033 -0.0030 146 THR   B O   
5876 C  CB  . THR   B 146 ? 0.1364 0.1199 0.2262 -0.0022 0.0181  -0.0042 146 THR   B CB  
5877 O  OG1 . THR   B 146 ? 0.1393 0.1224 0.2307 -0.0060 0.0170  0.0098  146 THR   B OG1 
5878 C  CG2 . THR   B 146 ? 0.1471 0.1258 0.2194 -0.0044 0.0186  0.0016  146 THR   B CG2 
5886 N  N   . VAL   B 147 ? 0.1348 0.1183 0.2086 -0.0036 0.0143  -0.0027 147 VAL   B N   
5887 C  CA  . VAL   B 147 ? 0.1365 0.1190 0.1920 -0.0111 0.0042  -0.0032 147 VAL   B CA  
5888 C  C   . VAL   B 147 ? 0.1330 0.1206 0.2135 -0.0137 -0.0088 -0.0085 147 VAL   B C   
5889 O  O   . VAL   B 147 ? 0.1464 0.1288 0.2252 -0.0218 -0.0210 -0.0192 147 VAL   B O   
5890 C  CB  . VAL   B 147 ? 0.1335 0.1377 0.1840 -0.0091 -0.0017 0.0004  147 VAL   B CB  
5891 C  CG1 . VAL   B 147 ? 0.1291 0.1509 0.1763 -0.0139 -0.0042 0.0031  147 VAL   B CG1 
5892 C  CG2 . VAL   B 147 ? 0.1421 0.1317 0.1919 -0.0110 -0.0022 0.0126  147 VAL   B CG2 
5902 N  N   . ARG   B 148 ? 0.1349 0.1206 0.2026 -0.0062 -0.0196 -0.0097 148 ARG   B N   
5903 C  CA  . ARG   B 148 ? 0.1383 0.1309 0.2019 -0.0041 -0.0272 -0.0107 148 ARG   B CA  
5904 C  C   . ARG   B 148 ? 0.1425 0.1415 0.1874 -0.0039 -0.0243 -0.0125 148 ARG   B C   
5905 O  O   . ARG   B 148 ? 0.1587 0.1706 0.1906 -0.0199 -0.0344 -0.0031 148 ARG   B O   
5906 C  CB  . ARG   B 148 ? 0.1418 0.1387 0.2123 -0.0013 -0.0285 -0.0149 148 ARG   B CB  
5907 C  CG  . ARG   B 148 ? 0.1462 0.1586 0.2238 -0.0093 -0.0214 -0.0312 148 ARG   B CG  
5908 C  CD  . ARG   B 148 ? 0.1527 0.1684 0.2334 0.0067  -0.0266 -0.0318 148 ARG   B CD  
5909 N  NE  . ARG   B 148 ? 0.1559 0.1624 0.2359 0.0202  -0.0325 -0.0301 148 ARG   B NE  
5910 C  CZ  . ARG   B 148 ? 0.1465 0.1530 0.2104 0.0150  -0.0196 -0.0244 148 ARG   B CZ  
5911 N  NH1 . ARG   B 148 ? 0.1393 0.1567 0.2130 -0.0026 -0.0066 -0.0185 148 ARG   B NH1 
5912 N  NH2 . ARG   B 148 ? 0.1682 0.1436 0.2060 0.0158  -0.0152 -0.0120 148 ARG   B NH2 
5926 N  N   . THR   B 149 ? 0.1468 0.1377 0.1889 -0.0088 -0.0199 -0.0031 149 THR   B N   
5927 C  CA  . THR   B 149 ? 0.1509 0.1377 0.1802 -0.0122 -0.0223 0.0010  149 THR   B CA  
5928 C  C   . THR   B 149 ? 0.1491 0.1332 0.1812 -0.0158 -0.0254 0.0006  149 THR   B C   
5929 O  O   . THR   B 149 ? 0.1629 0.1306 0.1891 -0.0141 -0.0098 -0.0023 149 THR   B O   
5930 C  CB  . THR   B 149 ? 0.1528 0.1356 0.1864 -0.0163 -0.0210 -0.0026 149 THR   B CB  
5931 O  OG1 . THR   B 149 ? 0.1563 0.1432 0.1760 -0.0235 -0.0231 -0.0015 149 THR   B OG1 
5932 C  CG2 . THR   B 149 ? 0.1540 0.1416 0.2026 -0.0079 -0.0149 0.0047  149 THR   B CG2 
5940 N  N   . ASN   B 150 ? 0.1591 0.1328 0.1826 -0.0130 -0.0253 -0.0004 150 ASN   B N   
5941 C  CA  . ASN   B 150 ? 0.1643 0.1458 0.1725 -0.0169 -0.0257 -0.0147 150 ASN   B CA  
5942 C  C   . ASN   B 150 ? 0.1545 0.1365 0.1872 -0.0094 -0.0191 -0.0067 150 ASN   B C   
5943 O  O   . ASN   B 150 ? 0.1610 0.1325 0.2123 -0.0205 -0.0415 -0.0007 150 ASN   B O   
5944 C  CB  . ASN   B 150 ? 0.1832 0.1801 0.1810 -0.0217 -0.0346 0.0064  150 ASN   B CB  
5945 C  CG  . ASN   B 150 ? 0.2144 0.2211 0.2149 -0.0207 -0.0389 0.0267  150 ASN   B CG  
5946 O  OD1 . ASN   B 150 ? 0.2290 0.2432 0.2349 -0.0308 -0.0527 0.0215  150 ASN   B OD1 
5947 N  ND2 . ASN   B 150 ? 0.2254 0.2377 0.2514 -0.0154 -0.0460 0.0565  150 ASN   B ND2 
5954 N  N   . VAL   B 151 ? 0.1461 0.1362 0.1735 -0.0156 -0.0226 -0.0026 151 VAL   B N   
5955 C  CA  . VAL   B 151 ? 0.1450 0.1389 0.1762 -0.0190 -0.0197 -0.0039 151 VAL   B CA  
5956 C  C   . VAL   B 151 ? 0.1436 0.1332 0.1859 -0.0257 -0.0235 -0.0117 151 VAL   B C   
5957 O  O   . VAL   B 151 ? 0.1509 0.1433 0.1995 -0.0225 -0.0106 -0.0147 151 VAL   B O   
5958 C  CB  . VAL   B 151 ? 0.1662 0.1505 0.1884 -0.0041 -0.0121 0.0010  151 VAL   B CB  
5959 C  CG1 . VAL   B 151 ? 0.1781 0.1527 0.2119 -0.0144 -0.0044 -0.0136 151 VAL   B CG1 
5960 C  CG2 . VAL   B 151 ? 0.1804 0.1671 0.1744 0.0087  -0.0169 0.0131  151 VAL   B CG2 
5970 N  N   . TYR   B 152 ? 0.1419 0.1221 0.1773 -0.0209 -0.0184 -0.0089 152 TYR   B N   
5971 C  CA  . TYR   B 152 ? 0.1441 0.1360 0.1618 -0.0199 -0.0083 -0.0091 152 TYR   B CA  
5972 C  C   . TYR   B 152 ? 0.1394 0.1244 0.1619 -0.0173 -0.0068 -0.0075 152 TYR   B C   
5973 O  O   . TYR   B 152 ? 0.1498 0.1270 0.1712 -0.0208 -0.0076 -0.0022 152 TYR   B O   
5974 C  CB  . TYR   B 152 ? 0.1588 0.1461 0.1655 -0.0210 -0.0086 0.0033  152 TYR   B CB  
5975 C  CG  . TYR   B 152 ? 0.1733 0.1563 0.1582 -0.0331 -0.0110 0.0010  152 TYR   B CG  
5976 C  CD1 . TYR   B 152 ? 0.1777 0.1691 0.1665 -0.0204 -0.0245 0.0062  152 TYR   B CD1 
5977 C  CD2 . TYR   B 152 ? 0.1937 0.1747 0.1584 -0.0287 -0.0096 -0.0097 152 TYR   B CD2 
5978 C  CE1 . TYR   B 152 ? 0.1955 0.1814 0.1728 -0.0149 -0.0247 0.0185  152 TYR   B CE1 
5979 C  CE2 . TYR   B 152 ? 0.1989 0.1926 0.1652 -0.0267 -0.0070 -0.0115 152 TYR   B CE2 
5980 C  CZ  . TYR   B 152 ? 0.2074 0.2038 0.1668 -0.0233 -0.0269 0.0109  152 TYR   B CZ  
5981 O  OH  . TYR   B 152 ? 0.2311 0.2412 0.1979 -0.0109 -0.0340 0.0119  152 TYR   B OH  
5991 N  N   . LEU   B 153 ? 0.1429 0.1224 0.1718 -0.0248 -0.0068 -0.0083 153 LEU   B N   
5992 C  CA  . LEU   B 153 ? 0.1497 0.1214 0.1668 -0.0187 -0.0003 -0.0112 153 LEU   B CA  
5993 C  C   . LEU   B 153 ? 0.1478 0.1205 0.1813 -0.0197 0.0043  -0.0153 153 LEU   B C   
5994 O  O   . LEU   B 153 ? 0.1552 0.1416 0.1956 -0.0106 -0.0070 -0.0330 153 LEU   B O   
5995 C  CB  . LEU   B 153 ? 0.1508 0.1137 0.1853 -0.0182 0.0055  -0.0129 153 LEU   B CB  
5996 C  CG  . LEU   B 153 ? 0.1478 0.1322 0.2012 -0.0205 0.0009  -0.0148 153 LEU   B CG  
5997 C  CD1 . LEU   B 153 ? 0.1472 0.1448 0.2007 -0.0264 0.0064  -0.0036 153 LEU   B CD1 
5998 C  CD2 . LEU   B 153 ? 0.1526 0.1425 0.2026 -0.0280 0.0091  -0.0072 153 LEU   B CD2 
6010 N  N   . ALA   B 154 ? 0.1442 0.1244 0.1790 -0.0031 -0.0068 -0.0068 154 ALA   B N   
6011 C  CA  . ALA   B 154 ? 0.1579 0.1303 0.1889 -0.0024 -0.0122 -0.0236 154 ALA   B CA  
6012 C  C   . ALA   B 154 ? 0.1652 0.1351 0.2029 0.0010  -0.0241 -0.0279 154 ALA   B C   
6013 O  O   . ALA   B 154 ? 0.1923 0.1351 0.2208 0.0100  -0.0135 -0.0080 154 ALA   B O   
6014 C  CB  . ALA   B 154 ? 0.1547 0.1440 0.2222 -0.0055 -0.0134 -0.0268 154 ALA   B CB  
6020 N  N   . VAL   B 155 ? 0.1345 0.1237 0.2102 0.0006  -0.0076 -0.0161 155 VAL   B N   
6021 C  CA  . VAL   B 155 ? 0.1327 0.1248 0.2243 0.0018  -0.0128 -0.0094 155 VAL   B CA  
6022 C  C   . VAL   B 155 ? 0.1332 0.1255 0.2219 -0.0052 -0.0108 -0.0223 155 VAL   B C   
6023 O  O   . VAL   B 155 ? 0.1538 0.1497 0.2462 0.0028  -0.0100 -0.0383 155 VAL   B O   
6024 C  CB  . VAL   B 155 ? 0.1403 0.1414 0.2511 -0.0038 -0.0169 -0.0023 155 VAL   B CB  
6025 C  CG1 . VAL   B 155 ? 0.1459 0.1388 0.2499 -0.0086 -0.0180 -0.0070 155 VAL   B CG1 
6026 C  CG2 . VAL   B 155 ? 0.1331 0.1536 0.2787 -0.0046 -0.0165 0.0233  155 VAL   B CG2 
6036 N  N   . PHE   B 156 ? 0.1260 0.1386 0.2344 0.0046  -0.0056 -0.0142 156 PHE   B N   
6037 C  CA  . PHE   B 156 ? 0.1291 0.1494 0.2633 0.0047  -0.0036 -0.0188 156 PHE   B CA  
6038 C  C   . PHE   B 156 ? 0.1249 0.1556 0.2840 0.0070  -0.0167 -0.0390 156 PHE   B C   
6039 O  O   . PHE   B 156 ? 0.1530 0.1743 0.3113 0.0210  -0.0018 -0.0375 156 PHE   B O   
6040 C  CB  . PHE   B 156 ? 0.1369 0.1417 0.2676 0.0002  -0.0163 -0.0131 156 PHE   B CB  
6041 C  CG  . PHE   B 156 ? 0.1457 0.1459 0.2889 -0.0022 -0.0134 0.0041  156 PHE   B CG  
6042 C  CD1 . PHE   B 156 ? 0.1493 0.1754 0.3141 0.0044  -0.0119 0.0368  156 PHE   B CD1 
6043 C  CD2 . PHE   B 156 ? 0.1479 0.1561 0.2838 0.0090  -0.0261 0.0050  156 PHE   B CD2 
6044 C  CE1 . PHE   B 156 ? 0.1489 0.1860 0.3284 0.0105  -0.0085 0.0470  156 PHE   B CE1 
6045 C  CE2 . PHE   B 156 ? 0.1520 0.1768 0.3052 0.0039  -0.0276 0.0073  156 PHE   B CE2 
6046 C  CZ  . PHE   B 156 ? 0.1454 0.1816 0.3272 0.0158  -0.0189 0.0242  156 PHE   B CZ  
6056 N  N   . ASP   B 157 ? 0.1331 0.1427 0.3104 0.0095  -0.0223 -0.0217 157 ASP   B N   
6057 C  CA  . ASP   B 157 ? 0.1434 0.1435 0.3453 0.0056  -0.0238 -0.0244 157 ASP   B CA  
6058 C  C   . ASP   B 157 ? 0.1428 0.1392 0.3481 0.0060  -0.0230 -0.0412 157 ASP   B C   
6059 O  O   . ASP   B 157 ? 0.1319 0.1402 0.3381 0.0011  -0.0212 -0.0334 157 ASP   B O   
6060 C  CB  . ASP   B 157 ? 0.1630 0.1591 0.3590 -0.0016 -0.0407 -0.0146 157 ASP   B CB  
6061 C  CG  . ASP   B 157 ? 0.1995 0.1692 0.3811 -0.0060 -0.0319 -0.0132 157 ASP   B CG  
6062 O  OD1 . ASP   B 157 ? 0.2072 0.1639 0.3953 0.0034  -0.0358 -0.0106 157 ASP   B OD1 
6063 O  OD2 . ASP   B 157 ? 0.2340 0.1932 0.4106 -0.0065 -0.0087 -0.0065 157 ASP   B OD2 
6068 N  N   . LYS   B 158 ? 0.1422 0.1686 0.3602 0.0053  -0.0108 -0.0665 158 LYS   B N   
6069 C  CA  . LYS   B 158 ? 0.1558 0.1837 0.3685 0.0060  -0.0034 -0.0791 158 LYS   B CA  
6070 C  C   . LYS   B 158 ? 0.1588 0.1688 0.3715 0.0032  -0.0087 -0.0694 158 LYS   B C   
6071 O  O   . LYS   B 158 ? 0.1600 0.1678 0.3730 -0.0014 -0.0141 -0.0844 158 LYS   B O   
6072 C  CB  . LYS   B 158 ? 0.1781 0.2253 0.3696 0.0057  0.0081  -0.0971 158 LYS   B CB  
6073 C  CG  . LYS   B 158 ? 0.2116 0.2621 0.3763 0.0071  0.0186  -0.0970 158 LYS   B CG  
6074 C  CD  . LYS   B 158 ? 0.2366 0.2990 0.3875 0.0068  0.0250  -0.0849 158 LYS   B CD  
6075 C  CE  . LYS   B 158 ? 0.2600 0.3232 0.3990 0.0087  0.0219  -0.0751 158 LYS   B CE  
6076 N  NZ  . LYS   B 158 ? 0.2565 0.3240 0.3908 0.0058  0.0285  -0.0730 158 LYS   B NZ  
6090 N  N   . ASN   B 159 ? 0.1650 0.1574 0.3855 0.0034  -0.0219 -0.0479 159 ASN   B N   
6091 C  CA  . ASN   B 159 ? 0.1800 0.1539 0.3980 0.0177  -0.0361 -0.0397 159 ASN   B CA  
6092 C  C   . ASN   B 159 ? 0.1620 0.1416 0.3887 0.0084  -0.0451 -0.0312 159 ASN   B C   
6093 O  O   . ASN   B 159 ? 0.1678 0.1390 0.3930 -0.0076 -0.0469 -0.0247 159 ASN   B O   
6094 C  CB  . ASN   B 159 ? 0.2017 0.1662 0.4195 0.0251  -0.0382 -0.0364 159 ASN   B CB  
6095 C  CG  . ASN   B 159 ? 0.2243 0.1906 0.4375 0.0272  -0.0426 -0.0555 159 ASN   B CG  
6096 O  OD1 . ASN   B 159 ? 0.2407 0.2028 0.4463 0.0304  -0.0527 -0.0676 159 ASN   B OD1 
6097 N  ND2 . ASN   B 159 ? 0.2264 0.2016 0.4513 0.0286  -0.0372 -0.0491 159 ASN   B ND2 
6104 N  N   . LEU   B 160 ? 0.1503 0.1399 0.3653 0.0055  -0.0451 -0.0259 160 LEU   B N   
6105 C  CA  . LEU   B 160 ? 0.1486 0.1444 0.3301 0.0067  -0.0349 -0.0202 160 LEU   B CA  
6106 C  C   . LEU   B 160 ? 0.1431 0.1364 0.3184 -0.0026 -0.0249 -0.0317 160 LEU   B C   
6107 O  O   . LEU   B 160 ? 0.1340 0.1409 0.3096 -0.0058 -0.0234 -0.0271 160 LEU   B O   
6108 C  CB  . LEU   B 160 ? 0.1474 0.1507 0.3148 0.0037  -0.0347 -0.0138 160 LEU   B CB  
6109 C  CG  . LEU   B 160 ? 0.1486 0.1652 0.2821 0.0105  -0.0286 -0.0079 160 LEU   B CG  
6110 C  CD1 . LEU   B 160 ? 0.1643 0.1884 0.2824 0.0025  -0.0164 -0.0060 160 LEU   B CD1 
6111 C  CD2 . LEU   B 160 ? 0.1535 0.1640 0.2837 0.0232  -0.0264 -0.0178 160 LEU   B CD2 
6123 N  N   . TYR   B 161 ? 0.1428 0.1408 0.3179 -0.0079 -0.0006 -0.0388 161 TYR   B N   
6124 C  CA  . TYR   B 161 ? 0.1436 0.1429 0.3049 -0.0134 0.0064  -0.0417 161 TYR   B CA  
6125 C  C   . TYR   B 161 ? 0.1478 0.1393 0.2959 -0.0119 0.0121  -0.0372 161 TYR   B C   
6126 O  O   . TYR   B 161 ? 0.1530 0.1395 0.2895 -0.0131 0.0047  -0.0366 161 TYR   B O   
6127 C  CB  . TYR   B 161 ? 0.1536 0.1510 0.3044 -0.0159 0.0163  -0.0432 161 TYR   B CB  
6128 C  CG  . TYR   B 161 ? 0.1773 0.1504 0.2983 -0.0197 0.0323  -0.0502 161 TYR   B CG  
6129 C  CD1 . TYR   B 161 ? 0.1839 0.1477 0.2943 -0.0324 0.0297  -0.0514 161 TYR   B CD1 
6130 C  CD2 . TYR   B 161 ? 0.2018 0.1548 0.2909 -0.0189 0.0271  -0.0482 161 TYR   B CD2 
6131 C  CE1 . TYR   B 161 ? 0.2024 0.1707 0.2937 -0.0308 0.0293  -0.0510 161 TYR   B CE1 
6132 C  CE2 . TYR   B 161 ? 0.2206 0.1723 0.2913 -0.0245 0.0360  -0.0397 161 TYR   B CE2 
6133 C  CZ  . TYR   B 161 ? 0.2164 0.1763 0.2929 -0.0363 0.0304  -0.0362 161 TYR   B CZ  
6134 O  OH  . TYR   B 161 ? 0.2454 0.1991 0.3242 -0.0414 0.0285  -0.0330 161 TYR   B OH  
6144 N  N   . ASP   B 162 ? 0.1571 0.1390 0.3056 -0.0059 -0.0042 -0.0502 162 ASP   B N   
6145 C  CA  . ASP   B 162 ? 0.1655 0.1435 0.3153 -0.0046 -0.0080 -0.0512 162 ASP   B CA  
6146 C  C   . ASP   B 162 ? 0.1612 0.1337 0.3095 -0.0088 -0.0110 -0.0466 162 ASP   B C   
6147 O  O   . ASP   B 162 ? 0.1673 0.1401 0.3102 -0.0108 -0.0158 -0.0408 162 ASP   B O   
6148 C  CB  . ASP   B 162 ? 0.1807 0.1620 0.3428 -0.0033 -0.0064 -0.0637 162 ASP   B CB  
6149 C  CG  . ASP   B 162 ? 0.1871 0.1798 0.3586 0.0073  -0.0076 -0.0782 162 ASP   B CG  
6150 O  OD1 . ASP   B 162 ? 0.1837 0.2009 0.3522 0.0066  0.0002  -0.0695 162 ASP   B OD1 
6151 O  OD2 . ASP   B 162 ? 0.2035 0.1969 0.3867 0.0233  -0.0019 -0.0736 162 ASP   B OD2 
6156 N  N   . LYS   B 163 ? 0.1587 0.1295 0.3047 -0.0104 -0.0306 -0.0321 163 LYS   B N   
6157 C  CA  . LYS   B 163 ? 0.1723 0.1376 0.3091 -0.0113 -0.0233 -0.0089 163 LYS   B CA  
6158 C  C   . LYS   B 163 ? 0.1428 0.1329 0.2969 -0.0135 -0.0191 -0.0078 163 LYS   B C   
6159 O  O   . LYS   B 163 ? 0.1457 0.1393 0.3185 -0.0187 -0.0128 -0.0074 163 LYS   B O   
6160 C  CB  . LYS   B 163 ? 0.2152 0.1730 0.3482 0.0030  -0.0282 0.0149  163 LYS   B CB  
6161 C  CG  . LYS   B 163 ? 0.2804 0.2549 0.4038 -0.0006 -0.0127 0.0210  163 LYS   B CG  
6162 C  CD  . LYS   B 163 ? 0.3311 0.3164 0.4637 -0.0073 -0.0102 0.0117  163 LYS   B CD  
6163 C  CE  . LYS   B 163 ? 0.3743 0.3523 0.5068 -0.0159 -0.0088 0.0106  163 LYS   B CE  
6164 N  NZ  . LYS   B 163 ? 0.4180 0.4180 0.5329 -0.0200 -0.0081 0.0092  163 LYS   B NZ  
6178 N  N   . LEU   B 164 ? 0.1316 0.1284 0.2827 -0.0113 -0.0102 -0.0085 164 LEU   B N   
6179 C  CA  . LEU   B 164 ? 0.1337 0.1299 0.2662 -0.0082 -0.0189 -0.0053 164 LEU   B CA  
6180 C  C   . LEU   B 164 ? 0.1408 0.1306 0.2563 -0.0106 -0.0290 -0.0105 164 LEU   B C   
6181 O  O   . LEU   B 164 ? 0.1419 0.1523 0.2742 -0.0142 -0.0254 -0.0095 164 LEU   B O   
6182 C  CB  . LEU   B 164 ? 0.1357 0.1255 0.2533 -0.0120 -0.0115 -0.0061 164 LEU   B CB  
6183 C  CG  . LEU   B 164 ? 0.1453 0.1457 0.2648 -0.0094 -0.0042 -0.0082 164 LEU   B CG  
6184 C  CD1 . LEU   B 164 ? 0.1455 0.1418 0.2570 -0.0168 -0.0181 -0.0058 164 LEU   B CD1 
6185 C  CD2 . LEU   B 164 ? 0.1636 0.1824 0.2724 -0.0062 0.0106  -0.0262 164 LEU   B CD2 
6197 N  N   . VAL   B 165 ? 0.1602 0.1353 0.2794 -0.0137 -0.0275 -0.0216 165 VAL   B N   
6198 C  CA  . VAL   B 165 ? 0.1890 0.1469 0.2864 -0.0253 -0.0426 -0.0179 165 VAL   B CA  
6199 C  C   . VAL   B 165 ? 0.2153 0.1538 0.3152 -0.0299 -0.0702 -0.0159 165 VAL   B C   
6200 O  O   . VAL   B 165 ? 0.2282 0.1634 0.3201 -0.0334 -0.0753 -0.0093 165 VAL   B O   
6201 C  CB  . VAL   B 165 ? 0.2103 0.1683 0.2886 -0.0076 -0.0093 -0.0242 165 VAL   B CB  
6202 C  CG1 . VAL   B 165 ? 0.2274 0.1733 0.3150 -0.0152 -0.0004 -0.0157 165 VAL   B CG1 
6203 C  CG2 . VAL   B 165 ? 0.2009 0.1738 0.2868 -0.0057 0.0024  -0.0207 165 VAL   B CG2 
6213 N  N   . SER   B 166 ? 0.2266 0.1429 0.3366 -0.0256 -0.0744 -0.0280 166 SER   B N   
6214 C  CA  . SER   B 166 ? 0.2245 0.1443 0.3814 -0.0309 -0.0636 -0.0363 166 SER   B CA  
6215 C  C   . SER   B 166 ? 0.2133 0.1516 0.3958 -0.0291 -0.0661 -0.0164 166 SER   B C   
6216 O  O   . SER   B 166 ? 0.2151 0.1748 0.4299 -0.0415 -0.0857 -0.0357 166 SER   B O   
6217 C  CB  . SER   B 166 ? 0.2289 0.1557 0.4083 -0.0230 -0.0540 -0.0345 166 SER   B CB  
6218 O  OG  . SER   B 166 ? 0.2236 0.1530 0.4204 -0.0156 -0.0538 -0.0167 166 SER   B OG  
6224 N  N   . SER   B 167 ? 0.1984 0.1447 0.3749 -0.0291 -0.0648 0.0163  167 SER   B N   
6225 C  CA  . SER   B 167 ? 0.1928 0.1532 0.3583 -0.0293 -0.0433 0.0167  167 SER   B CA  
6226 C  C   . SER   B 167 ? 0.1856 0.1610 0.3424 -0.0452 -0.0427 0.0332  167 SER   B C   
6227 O  O   . SER   B 167 ? 0.1890 0.1791 0.3315 -0.0522 -0.0391 0.0343  167 SER   B O   
6228 C  CB  . SER   B 167 ? 0.1885 0.1647 0.3458 -0.0280 -0.0224 0.0242  167 SER   B CB  
6229 O  OG  . SER   B 167 ? 0.1797 0.1755 0.3282 -0.0198 -0.0176 0.0256  167 SER   B OG  
6235 N  N   . PHE   B 168 ? 0.1873 0.1625 0.3367 -0.0406 -0.0256 0.0349  168 PHE   B N   
6236 C  CA  . PHE   B 168 ? 0.1930 0.1563 0.3071 -0.0455 -0.0232 0.0241  168 PHE   B CA  
6237 C  C   . PHE   B 168 ? 0.1672 0.1533 0.2612 -0.0250 -0.0035 0.0131  168 PHE   B C   
6238 O  O   . PHE   B 168 ? 0.1939 0.1447 0.2705 0.0009  -0.0040 -0.0026 168 PHE   B O   
6239 C  CB  . PHE   B 168 ? 0.2065 0.1631 0.3135 -0.0520 -0.0438 0.0330  168 PHE   B CB  
6240 C  CG  . PHE   B 168 ? 0.2340 0.1508 0.3059 -0.0557 -0.0446 0.0186  168 PHE   B CG  
6241 C  CD1 . PHE   B 168 ? 0.2635 0.1551 0.3119 -0.0526 -0.0543 0.0143  168 PHE   B CD1 
6242 C  CD2 . PHE   B 168 ? 0.2232 0.1524 0.2989 -0.0531 -0.0452 0.0308  168 PHE   B CD2 
6243 C  CE1 . PHE   B 168 ? 0.2751 0.1645 0.3099 -0.0362 -0.0469 0.0223  168 PHE   B CE1 
6244 C  CE2 . PHE   B 168 ? 0.2464 0.1607 0.3100 -0.0390 -0.0507 0.0226  168 PHE   B CE2 
6245 C  CZ  . PHE   B 168 ? 0.2619 0.1549 0.3099 -0.0291 -0.0528 0.0324  168 PHE   B CZ  
6255 N  N   . LEU   B 169 ? 0.1671 0.1712 0.2571 -0.0022 0.0042  0.0038  169 LEU   B N   
6256 C  CA  . LEU   B 169 ? 0.1875 0.1961 0.2864 -0.0063 0.0014  -0.0195 169 LEU   B CA  
6257 C  C   . LEU   B 169 ? 0.2164 0.2198 0.3313 0.0135  -0.0012 -0.0493 169 LEU   B C   
6258 O  O   . LEU   B 169 ? 0.2387 0.2406 0.3823 0.0126  -0.0061 -0.0707 169 LEU   B O   
6259 C  CB  . LEU   B 169 ? 0.2066 0.2343 0.2893 -0.0153 -0.0118 0.0064  169 LEU   B CB  
6260 C  CG  . LEU   B 169 ? 0.2506 0.2736 0.3374 -0.0024 -0.0097 0.0119  169 LEU   B CG  
6261 C  CD1 . LEU   B 169 ? 0.2627 0.2937 0.3403 -0.0028 -0.0107 0.0272  169 LEU   B CD1 
6262 C  CD2 . LEU   B 169 ? 0.2515 0.2833 0.3485 0.0162  0.0055  0.0005  169 LEU   B CD2 
6263 O  OXT . LEU   B 169 ? 0.2307 0.2355 0.3202 0.0408  0.0049  -0.0533 169 LEU   B OXT 
6275 N  N2  B A1BAW C .   ? 0.1155 0.1719 0.1406 -0.0093 0.0064  0.0285  201 A1BAW A N2  
6276 C  C3  B A1BAW C .   ? 0.0925 0.1642 0.1306 -0.0045 -0.0046 0.0297  201 A1BAW A C3  
6277 C  C6  B A1BAW C .   ? 0.1123 0.1653 0.1385 0.0102  -0.0133 0.0114  201 A1BAW A C6  
6278 C  C9  B A1BAW C .   ? 0.1145 0.1777 0.1586 -0.0099 -0.0073 0.0199  201 A1BAW A C9  
6279 C  C12 B A1BAW C .   ? 0.1271 0.1762 0.1732 -0.0043 -0.0206 0.0157  201 A1BAW A C12 
6280 C  C1  B A1BAW C .   ? 0.1284 0.1653 0.1309 0.0188  -0.0037 0.0158  201 A1BAW A C1  
6281 C  C10 B A1BAW C .   ? 0.1191 0.1920 0.1641 -0.0075 -0.0151 0.0238  201 A1BAW A C10 
6282 C  C11 B A1BAW C .   ? 0.1337 0.1910 0.1781 -0.0050 -0.0199 0.0095  201 A1BAW A C11 
6283 C  C13 B A1BAW C .   ? 0.1098 0.1637 0.1246 0.0095  0.0003  0.0207  201 A1BAW A C13 
6284 C  C2  B A1BAW C .   ? 0.1161 0.1669 0.1331 0.0092  -0.0025 0.0213  201 A1BAW A C2  
6285 C  C4  B A1BAW C .   ? 0.1068 0.1696 0.1286 -0.0020 0.0031  0.0271  201 A1BAW A C4  
6286 C  C5  B A1BAW C .   ? 0.1165 0.1746 0.1475 0.0028  -0.0019 0.0102  201 A1BAW A C5  
6287 C  C7  B A1BAW C .   ? 0.1029 0.1526 0.1587 -0.0034 -0.0027 0.0216  201 A1BAW A C7  
6288 C  C8  B A1BAW C .   ? 0.1161 0.1675 0.1591 -0.0146 -0.0129 0.0099  201 A1BAW A C8  
6289 N  N1  B A1BAW C .   ? 0.1036 0.1706 0.1345 0.0024  -0.0128 0.0308  201 A1BAW A N1  
6290 N  N3  B A1BAW C .   ? 0.1135 0.1716 0.1540 0.0087  -0.0144 0.0044  201 A1BAW A N3  
6291 N  N4  B A1BAW C .   ? 0.1131 0.1569 0.1553 0.0063  -0.0120 0.0174  201 A1BAW A N4  
6292 O  O1  B A1BAW C .   ? 0.1388 0.1650 0.1530 -0.0191 -0.0225 -0.0138 201 A1BAW A O1  
6293 S  S1  B A1BAW C .   ? 0.1301 0.2042 0.1912 -0.0035 -0.0191 0.0188  201 A1BAW A S1  
6312 CL CL  B CL    D .   ? 0.1920 0.1372 0.1553 -0.0084 0.0367  0.0007  202 CL    A CL  
6313 O  O   . HOH   E .   ? 0.4319 0.7368 0.4880 -0.1157 0.1054  0.0356  301 HOH   A O   
6314 O  O   . HOH   E .   ? 0.7097 0.5093 0.3292 -0.0508 0.0852  0.1424  302 HOH   A O   
6315 O  O   . HOH   E .   ? 0.3353 0.2257 0.4354 -0.0002 0.0031  0.0521  303 HOH   A O   
6316 O  O   . HOH   E .   ? 0.5982 0.4861 0.3328 0.2125  -0.1120 0.0371  304 HOH   A O   
6317 O  O   . HOH   E .   ? 0.2808 0.2779 0.4126 -0.0785 0.1221  -0.0273 305 HOH   A O   
6318 O  O   . HOH   E .   ? 0.8238 0.3507 0.5036 -0.0479 -0.1200 0.0786  306 HOH   A O   
6319 O  O   . HOH   E .   ? 0.2473 0.2535 0.4082 -0.0172 0.1194  0.0704  307 HOH   A O   
6320 O  O   . HOH   E .   ? 0.4402 0.2796 0.3244 -0.0447 0.0516  0.0029  308 HOH   A O   
6321 O  O   . HOH   E .   ? 0.5543 0.3371 0.4651 -0.0574 0.1548  0.0850  309 HOH   A O   
6322 O  O   . HOH   E .   ? 0.3295 0.2920 0.1564 -0.0396 0.0561  0.0403  310 HOH   A O   
6323 O  O   . HOH   E .   ? 0.2762 0.2313 0.4092 -0.0271 -0.0759 0.0967  311 HOH   A O   
6324 O  O   . HOH   E .   ? 0.1723 0.1660 0.2086 0.0134  -0.0176 0.0303  312 HOH   A O   
6325 O  O   . HOH   E .   ? 0.4545 0.3831 0.5618 -0.0508 0.1626  -0.0726 313 HOH   A O   
6326 O  O   . HOH   E .   ? 0.2011 0.1753 0.3696 -0.0412 -0.0088 -0.0064 314 HOH   A O   
6327 O  O   . HOH   E .   ? 0.1699 0.2679 0.3004 0.0285  -0.0203 -0.0138 315 HOH   A O   
6328 O  O   . HOH   E .   ? 0.3277 0.1874 0.2250 0.0056  0.0276  0.0020  316 HOH   A O   
6329 O  O   . HOH   E .   ? 0.6597 0.5513 0.3573 -0.0159 -0.0770 0.1058  317 HOH   A O   
6330 O  O   . HOH   E .   ? 0.3656 0.3267 0.3719 -0.0553 0.1764  -0.0033 318 HOH   A O   
6331 O  O   . HOH   E .   ? 0.2291 0.5692 0.3931 -0.0336 -0.0448 0.0602  319 HOH   A O   
6332 O  O   . HOH   E .   ? 0.3273 0.4274 0.2740 -0.0123 0.0525  0.0813  320 HOH   A O   
6333 O  O   . HOH   E .   ? 0.4797 0.3674 0.3925 -0.0154 -0.1252 -0.0788 321 HOH   A O   
6334 O  O   . HOH   E .   ? 0.6157 0.5503 0.3565 0.1921  -0.0372 -0.0349 322 HOH   A O   
6335 O  O   . HOH   E .   ? 0.1473 0.1403 0.2291 -0.0145 0.0058  -0.0025 323 HOH   A O   
6336 O  O   . HOH   E .   ? 0.3034 0.2770 0.2881 -0.0911 0.0391  0.0475  324 HOH   A O   
6337 O  O   . HOH   E .   ? 0.1863 0.3188 0.5275 -0.0161 0.0400  -0.0976 325 HOH   A O   
6338 O  O   . HOH   E .   ? 0.4993 0.2054 0.4498 0.0382  0.0530  0.0077  326 HOH   A O   
6339 O  O   B HOH   E .   ? 0.2760 0.3100 0.3093 0.0063  -0.0209 0.0599  327 HOH   A O   
6340 O  O   . HOH   E .   ? 0.4971 0.5172 0.2741 -0.1023 0.1509  0.0887  328 HOH   A O   
6341 O  O   . HOH   E .   ? 0.2502 0.2157 0.2716 0.0358  0.0238  0.0436  329 HOH   A O   
6342 O  O   . HOH   E .   ? 0.2211 0.4111 0.3705 -0.0055 -0.0419 0.1744  330 HOH   A O   
6343 O  O   . HOH   E .   ? 0.4568 0.4857 0.5133 0.1527  0.1491  -0.0772 331 HOH   A O   
6344 O  O   . HOH   E .   ? 0.3481 0.3265 0.3429 -0.0597 -0.1289 -0.0372 332 HOH   A O   
6345 O  O   . HOH   E .   ? 0.4819 0.5205 0.5726 -0.0915 0.0457  0.1706  333 HOH   A O   
6346 O  O   . HOH   E .   ? 0.2493 0.1914 0.2320 -0.0282 0.0236  -0.0010 334 HOH   A O   
6347 O  O   . HOH   E .   ? 0.4229 0.3608 0.2756 0.0814  -0.1449 0.0187  335 HOH   A O   
6348 O  O   B HOH   E .   ? 0.1636 0.1319 0.2549 0.0059  -0.0650 -0.0315 336 HOH   A O   
6349 O  O   . HOH   E .   ? 0.2768 0.4036 0.3137 -0.0327 0.0293  0.0138  337 HOH   A O   
6350 O  O   . HOH   E .   ? 0.4502 0.3676 0.4023 -0.1865 -0.0662 0.1668  338 HOH   A O   
6351 O  O   . HOH   E .   ? 0.1488 0.2226 0.2313 0.0084  -0.0098 0.0640  339 HOH   A O   
6352 O  O   . HOH   E .   ? 0.1415 0.3499 0.3122 -0.0112 0.0219  0.0249  340 HOH   A O   
6353 O  O   B HOH   E .   ? 0.2995 0.2537 0.1824 -0.0224 0.0117  0.0015  341 HOH   A O   
6354 O  O   . HOH   E .   ? 0.3682 0.2222 0.4733 -0.0128 -0.1756 0.0796  342 HOH   A O   
6355 O  O   . HOH   E .   ? 0.1656 0.1663 0.2318 -0.0240 0.0101  0.0317  343 HOH   A O   
6356 O  O   . HOH   E .   ? 0.2028 0.1661 0.2230 0.0253  -0.0267 0.0012  344 HOH   A O   
6357 O  O   . HOH   E .   ? 0.2630 0.3465 0.3497 -0.0629 -0.0514 -0.0618 345 HOH   A O   
6358 O  O   B HOH   E .   ? 0.2568 0.1800 0.2294 0.0479  -0.0089 0.0280  346 HOH   A O   
6359 O  O   . HOH   E .   ? 0.3681 0.4221 0.3354 0.1840  0.0465  0.0650  347 HOH   A O   
6360 O  O   B HOH   E .   ? 0.0855 0.1652 0.2611 -0.0341 -0.0183 0.0560  348 HOH   A O   
6361 O  O   . HOH   E .   ? 0.1452 0.1756 0.2965 0.0042  -0.0358 -0.0619 349 HOH   A O   
6362 O  O   . HOH   E .   ? 0.3736 0.6514 0.5004 -0.0704 -0.1245 0.0429  350 HOH   A O   
6363 O  O   . HOH   E .   ? 0.5169 0.3155 0.4272 -0.1926 0.2096  -0.1129 351 HOH   A O   
6364 O  O   A HOH   E .   ? 0.2544 0.4515 0.5209 -0.0795 0.0525  0.2008  352 HOH   A O   
6365 O  O   . HOH   E .   ? 0.2846 0.3272 0.2390 -0.0613 -0.0216 -0.0650 353 HOH   A O   
6366 O  O   . HOH   E .   ? 0.5466 0.4014 0.3039 -0.0210 0.0340  0.1352  354 HOH   A O   
6367 O  O   . HOH   E .   ? 0.1472 0.1811 0.2521 0.0050  -0.0136 0.0037  355 HOH   A O   
6368 O  O   . HOH   E .   ? 0.1972 0.2073 0.3390 0.0088  0.0904  -0.0192 356 HOH   A O   
6369 O  O   . HOH   E .   ? 0.3743 0.2318 0.4207 -0.1040 0.0760  0.0158  357 HOH   A O   
6370 O  O   . HOH   E .   ? 0.1714 0.2017 0.1831 -0.0004 0.0080  0.0551  358 HOH   A O   
6371 O  O   A HOH   E .   ? 0.5476 0.3935 0.4894 -0.0377 -0.0422 0.0845  359 HOH   A O   
6372 O  O   . HOH   E .   ? 0.1908 0.2532 0.3420 0.0338  0.0867  -0.0534 360 HOH   A O   
6373 O  O   . HOH   E .   ? 0.2939 0.6220 0.6148 0.1568  0.0543  0.1178  361 HOH   A O   
6374 O  O   . HOH   E .   ? 0.3058 0.2159 0.4958 -0.0551 -0.0357 0.0218  362 HOH   A O   
6375 O  O   . HOH   E .   ? 0.1923 0.1897 0.2398 -0.0377 0.0117  0.0308  363 HOH   A O   
6376 O  O   . HOH   E .   ? 0.2373 0.3664 0.3653 0.0834  -0.0502 -0.0056 364 HOH   A O   
6377 O  O   . HOH   E .   ? 0.2902 0.3095 0.5304 -0.0659 -0.1190 -0.0900 365 HOH   A O   
6378 O  O   . HOH   E .   ? 0.3616 0.2949 0.3850 -0.0989 -0.0259 -0.0199 366 HOH   A O   
6379 O  O   A HOH   E .   ? 0.2513 0.4251 0.3117 0.1247  -0.0250 -0.0354 367 HOH   A O   
6380 O  O   A HOH   E .   ? 0.1464 0.2443 0.1978 0.0342  0.0204  0.0630  368 HOH   A O   
6381 O  O   . HOH   E .   ? 0.1307 0.1323 0.1413 -0.0009 0.0091  0.0049  369 HOH   A O   
6382 O  O   . HOH   E .   ? 0.1522 0.1284 0.2204 -0.0060 0.0138  -0.0048 370 HOH   A O   
6383 O  O   . HOH   E .   ? 0.3875 0.2031 0.2318 0.1199  0.0383  0.0169  371 HOH   A O   
6384 O  O   . HOH   E .   ? 0.1420 0.1462 0.1571 -0.0014 -0.0163 -0.0039 372 HOH   A O   
6385 O  O   . HOH   E .   ? 0.2544 0.3827 0.3027 0.0392  0.0590  0.1475  373 HOH   A O   
6386 O  O   . HOH   E .   ? 0.6486 0.4694 0.5765 0.1369  0.1626  -0.1117 374 HOH   A O   
6387 O  O   . HOH   E .   ? 0.5625 0.3430 0.4016 0.1356  -0.0235 -0.0278 375 HOH   A O   
6388 O  O   . HOH   E .   ? 0.2029 0.2059 0.3249 0.0180  -0.0269 0.0195  376 HOH   A O   
6389 O  O   B HOH   E .   ? 0.4204 0.3247 0.3709 -0.0753 0.0117  0.0160  377 HOH   A O   
6390 O  O   . HOH   E .   ? 0.4965 0.5723 0.4405 -0.1340 -0.1009 -0.0495 378 HOH   A O   
6391 O  O   . HOH   E .   ? 0.3609 0.3369 0.4928 0.0905  0.0948  -0.0853 379 HOH   A O   
6392 O  O   . HOH   E .   ? 0.3205 0.2380 0.3565 -0.0062 -0.0366 0.1013  380 HOH   A O   
6393 O  O   . HOH   E .   ? 0.6469 0.6315 0.4853 -0.0953 0.2069  0.1059  381 HOH   A O   
6394 O  O   . HOH   E .   ? 0.2051 0.2226 0.2118 -0.0220 -0.0382 0.0354  382 HOH   A O   
6395 O  O   . HOH   E .   ? 0.3010 0.2792 0.2218 0.0288  0.0713  -0.0037 383 HOH   A O   
6396 O  O   . HOH   E .   ? 0.1588 0.1648 0.1866 0.0037  -0.0225 -0.0005 384 HOH   A O   
6397 O  O   . HOH   E .   ? 0.2596 0.2841 0.3705 -0.0115 0.0956  -0.0318 385 HOH   A O   
6398 O  O   . HOH   E .   ? 0.2723 0.1987 0.1871 -0.0633 0.0204  0.0227  386 HOH   A O   
6399 O  O   . HOH   E .   ? 0.1832 0.1719 0.1792 0.0174  0.0075  0.0154  387 HOH   A O   
6400 O  O   . HOH   E .   ? 0.2382 0.3837 0.3969 0.0554  0.0506  0.0581  388 HOH   A O   
6401 O  O   . HOH   E .   ? 0.5250 0.3921 0.2265 0.0476  0.1070  0.0743  389 HOH   A O   
6402 O  O   A HOH   E .   ? 0.1808 0.1542 0.2350 -0.0233 -0.0399 -0.0066 390 HOH   A O   
6403 O  O   . HOH   E .   ? 0.3309 0.5593 0.5501 0.0825  -0.0357 0.1276  391 HOH   A O   
6404 O  O   . HOH   E .   ? 0.2207 0.3441 0.3487 -0.0141 0.0150  0.0524  392 HOH   A O   
6405 O  O   A HOH   E .   ? 0.2598 0.2918 0.4031 -0.0677 0.0548  -0.0625 393 HOH   A O   
6406 O  O   . HOH   E .   ? 0.5101 0.5716 0.5956 -0.0964 -0.0496 0.1484  394 HOH   A O   
6407 O  O   . HOH   E .   ? 0.2682 0.6228 0.3541 0.0906  0.0419  -0.1396 395 HOH   A O   
6408 O  O   . HOH   E .   ? 0.1372 0.1398 0.1884 0.0021  -0.0179 0.0031  396 HOH   A O   
6409 O  O   . HOH   E .   ? 0.1691 0.1832 0.3867 0.0302  0.0918  0.0838  397 HOH   A O   
6410 O  O   . HOH   E .   ? 0.1617 0.2682 0.4133 -0.0160 0.0630  0.0637  398 HOH   A O   
6411 O  O   . HOH   E .   ? 0.2591 0.4051 0.3001 -0.0284 0.0745  -0.0732 399 HOH   A O   
6412 O  O   . HOH   E .   ? 0.2779 0.2482 0.3694 -0.0066 -0.0575 -0.0403 400 HOH   A O   
6413 O  O   . HOH   E .   ? 0.2109 0.1520 0.2736 0.0018  -0.0255 0.0101  401 HOH   A O   
6414 O  O   . HOH   E .   ? 0.2929 0.2587 0.2327 -0.0535 -0.0837 0.0247  402 HOH   A O   
6415 O  O   . HOH   E .   ? 0.1872 0.2110 0.2616 -0.0194 -0.0032 0.0729  403 HOH   A O   
6416 O  O   . HOH   E .   ? 0.2221 0.2341 0.3082 0.0314  0.0168  0.1034  404 HOH   A O   
6417 O  O   B HOH   E .   ? 0.1507 0.2436 0.1587 0.0321  -0.0140 0.0517  405 HOH   A O   
6418 O  O   . HOH   E .   ? 0.4282 0.6215 0.3250 -0.0707 -0.0304 0.1550  406 HOH   A O   
6419 O  O   . HOH   E .   ? 0.3791 0.2709 0.5768 0.0745  0.0846  0.0091  407 HOH   A O   
6420 O  O   . HOH   E .   ? 0.6705 0.6420 0.5298 -0.0835 0.0553  -0.0143 408 HOH   A O   
6421 O  O   . HOH   E .   ? 0.3731 0.5254 0.3884 -0.0189 0.0960  0.0958  409 HOH   A O   
6422 O  O   A HOH   E .   ? 0.3030 0.6146 0.4677 0.0003  -0.0505 0.1331  410 HOH   A O   
6423 O  O   . HOH   E .   ? 0.2046 0.2512 0.3402 -0.0190 -0.0175 0.0123  411 HOH   A O   
6424 O  O   . HOH   E .   ? 0.1564 0.1997 0.2853 -0.0096 -0.0025 0.0275  412 HOH   A O   
6425 O  O   . HOH   E .   ? 0.1643 0.1416 0.1678 -0.0162 0.0055  0.0016  413 HOH   A O   
6426 O  O   . HOH   E .   ? 0.6745 0.4190 0.5241 0.1518  -0.0984 0.1467  414 HOH   A O   
6427 O  O   . HOH   E .   ? 0.1446 0.1593 0.2658 -0.0026 0.0026  0.0210  415 HOH   A O   
6428 O  O   . HOH   E .   ? 0.2450 0.1725 0.2677 -0.0015 0.0222  0.0167  416 HOH   A O   
6429 O  O   . HOH   E .   ? 0.2603 0.2021 0.2688 -0.0576 -0.0068 0.0510  417 HOH   A O   
6430 O  O   . HOH   E .   ? 0.2377 0.2435 0.4295 0.0143  -0.0490 -0.0771 418 HOH   A O   
6431 O  O   A HOH   E .   ? 0.1216 0.1463 0.1703 0.0137  -0.0191 -0.0133 419 HOH   A O   
6432 O  O   . HOH   E .   ? 0.4543 0.4600 0.3356 0.0026  -0.1406 0.0189  420 HOH   A O   
6433 O  O   . HOH   E .   ? 0.2968 0.3738 0.6672 -0.0127 0.1182  -0.0324 421 HOH   A O   
6434 O  O   . HOH   E .   ? 0.6194 0.5749 0.5893 -0.0929 -0.0851 -0.1353 422 HOH   A O   
6435 O  O   . HOH   E .   ? 0.2180 0.2666 0.2530 -0.0001 -0.0648 0.0519  423 HOH   A O   
6436 O  O   . HOH   E .   ? 0.3008 0.3405 0.5489 -0.0027 0.1263  -0.0243 424 HOH   A O   
6437 O  O   . HOH   E .   ? 0.2797 0.6099 0.1786 -0.0386 0.0506  -0.0257 425 HOH   A O   
6438 O  O   . HOH   E .   ? 0.2085 0.1574 0.1560 -0.0023 0.0184  0.0133  426 HOH   A O   
6439 O  O   . HOH   E .   ? 0.5837 0.7267 0.5965 0.1078  -0.0656 0.0327  427 HOH   A O   
6440 O  O   . HOH   E .   ? 0.3542 0.3899 0.3221 0.1165  -0.0408 -0.1144 428 HOH   A O   
6441 O  O   . HOH   E .   ? 0.3277 0.1279 0.2168 0.0039  -0.0536 0.0133  429 HOH   A O   
6442 O  O   . HOH   E .   ? 0.3856 0.2165 0.5068 -0.0810 -0.2049 0.0986  430 HOH   A O   
6443 O  O   . HOH   E .   ? 0.4896 0.2972 0.3131 -0.1083 0.0524  0.0538  431 HOH   A O   
6444 O  O   . HOH   E .   ? 0.2090 0.4271 0.2419 0.1455  -0.0166 -0.0001 432 HOH   A O   
6445 O  O   A HOH   E .   ? 0.4007 0.2436 0.3926 0.0319  0.0675  0.0896  433 HOH   A O   
6446 O  O   . HOH   E .   ? 0.5195 0.6716 0.3899 0.0763  0.2389  -0.0831 434 HOH   A O   
6447 O  O   . HOH   E .   ? 0.1930 0.2151 0.2490 0.0283  -0.0250 0.0162  435 HOH   A O   
6448 O  O   B HOH   E .   ? 0.2804 0.1524 0.2651 0.0496  -0.0464 0.0316  436 HOH   A O   
6449 O  O   . HOH   E .   ? 0.5947 0.5121 0.5585 -0.1554 0.0744  -0.0778 437 HOH   A O   
6450 O  O   . HOH   E .   ? 0.3754 0.2442 0.1828 -0.0879 0.0412  0.0491  438 HOH   A O   
6451 O  O   A HOH   E .   ? 0.2009 0.1148 0.1505 -0.0008 0.0050  -0.0002 439 HOH   A O   
6452 O  O   . HOH   E .   ? 0.1779 0.2133 0.5514 -0.0225 -0.0736 0.0638  440 HOH   A O   
6453 O  O   . HOH   E .   ? 0.2522 0.2199 0.2944 0.0214  0.0154  0.0168  441 HOH   A O   
6454 O  O   . HOH   E .   ? 0.6628 0.7217 0.6098 0.0239  -0.1050 0.0662  442 HOH   A O   
6455 O  O   . HOH   E .   ? 0.5729 0.4964 0.6334 0.0792  -0.0239 -0.1362 443 HOH   A O   
6456 O  O   A HOH   E .   ? 0.2152 0.1446 0.2176 0.0196  -0.0750 -0.0208 444 HOH   A O   
6457 O  O   . HOH   E .   ? 0.7103 0.6714 0.3959 0.2166  -0.1135 0.1483  445 HOH   A O   
6458 O  O   . HOH   E .   ? 0.2323 0.1607 0.2615 0.0086  0.0102  0.0083  446 HOH   A O   
6459 O  O   . HOH   E .   ? 0.3459 0.3258 0.2989 0.1722  -0.0495 -0.0327 447 HOH   A O   
6460 O  O   . HOH   E .   ? 0.2332 0.2050 0.2446 0.0255  0.0381  0.0249  448 HOH   A O   
6461 O  O   . HOH   E .   ? 0.2106 0.2494 0.2363 0.0024  -0.0122 -0.0341 449 HOH   A O   
6462 O  O   . HOH   E .   ? 0.3868 0.4193 0.5539 -0.1026 -0.0956 -0.1320 450 HOH   A O   
6463 O  O   . HOH   E .   ? 0.5947 0.5433 0.7472 0.0377  -0.1347 0.1826  451 HOH   A O   
6464 O  O   B HOH   E .   ? 0.2108 0.3090 0.2958 0.0436  -0.0666 -0.0007 452 HOH   A O   
6465 O  O   A HOH   E .   ? 0.3758 0.4685 0.5330 -0.0022 0.0656  0.1803  453 HOH   A O   
6466 O  O   . HOH   E .   ? 0.8456 0.9241 0.6650 0.0072  0.0035  -0.0832 454 HOH   A O   
6467 O  O   A HOH   E .   ? 0.4153 0.3414 0.3795 0.1854  0.1715  0.1653  455 HOH   A O   
6468 O  O   . HOH   E .   ? 0.5504 0.3411 0.3710 0.0331  -0.0304 0.1289  456 HOH   A O   
6469 O  O   . HOH   E .   ? 0.4360 0.3669 0.4139 0.0443  -0.0503 0.1010  457 HOH   A O   
6470 O  O   . HOH   E .   ? 0.5930 0.4774 0.5445 0.1267  0.2248  0.1901  458 HOH   A O   
6471 O  O   B HOH   E .   ? 0.1500 0.1789 0.2282 0.0202  -0.0605 0.0337  459 HOH   A O   
6472 O  O   . HOH   E .   ? 0.5206 0.3462 0.4978 0.0593  0.0360  0.0471  460 HOH   A O   
6473 O  O   . HOH   E .   ? 0.2391 0.2349 0.3086 0.0208  -0.0106 0.0164  461 HOH   A O   
6474 O  O   . HOH   E .   ? 0.6473 0.5788 0.4943 -0.0562 0.1583  0.0576  462 HOH   A O   
6475 O  O   . HOH   E .   ? 0.3381 0.2811 0.3351 -0.0636 0.0078  -0.0597 463 HOH   A O   
6476 O  O   . HOH   E .   ? 0.6178 0.7204 0.4632 -0.0023 -0.1079 -0.0102 464 HOH   A O   
6477 O  O   . HOH   E .   ? 0.2898 0.4628 0.5389 -0.1250 0.0673  -0.2150 465 HOH   A O   
6478 O  O   . HOH   E .   ? 0.3426 0.4547 0.4124 0.0794  -0.0840 0.0865  466 HOH   A O   
6479 O  O   . HOH   E .   ? 0.2818 0.3768 0.3637 -0.0473 -0.0396 0.0127  467 HOH   A O   
6480 O  O   . HOH   E .   ? 0.2750 0.1801 0.2549 0.0294  -0.0763 -0.0225 468 HOH   A O   
6481 O  O   . HOH   E .   ? 0.2364 0.2530 0.3313 -0.0730 0.0316  -0.0220 469 HOH   A O   
6482 O  O   . HOH   E .   ? 0.2792 0.2415 0.5725 0.0750  -0.0837 0.0276  470 HOH   A O   
6483 O  O   . HOH   E .   ? 0.4070 0.5589 0.3656 -0.0797 -0.0525 0.1824  471 HOH   A O   
6484 O  O   . HOH   E .   ? 0.2838 0.3927 0.5170 0.0760  0.0297  -0.1628 472 HOH   A O   
6485 O  O   . HOH   E .   ? 0.5463 0.3172 0.7598 0.0573  0.0834  0.1927  473 HOH   A O   
6486 O  O   B HOH   E .   ? 0.3522 0.3191 0.2547 -0.0300 0.1047  0.0037  474 HOH   A O   
6487 O  O   . HOH   E .   ? 0.2561 0.2279 0.3927 0.0227  0.0548  -0.0078 475 HOH   A O   
6488 O  O   . HOH   E .   ? 0.5469 0.5255 0.4310 0.0588  0.0893  0.0713  476 HOH   A O   
6489 O  O   . HOH   E .   ? 0.4080 0.5660 0.3441 0.0647  -0.0627 -0.0537 477 HOH   A O   
6490 O  O   . HOH   E .   ? 0.5236 0.4014 0.3553 -0.0809 -0.0816 -0.0341 478 HOH   A O   
6491 O  O   . HOH   E .   ? 0.3161 0.4913 0.3239 -0.0332 -0.0310 -0.0786 479 HOH   A O   
6492 O  O   . HOH   E .   ? 0.4837 0.5651 0.4705 0.0733  -0.1380 -0.1352 480 HOH   A O   
6493 O  O   . HOH   E .   ? 0.7087 0.5453 0.6302 -0.1000 0.0236  -0.0423 481 HOH   A O   
6494 O  O   . HOH   E .   ? 0.4578 0.4143 0.5323 -0.2147 -0.0031 -0.0203 482 HOH   A O   
6495 O  O   . HOH   E .   ? 0.5061 0.4577 0.5136 -0.1754 -0.1063 0.0648  483 HOH   A O   
6496 O  O   . HOH   E .   ? 0.4342 0.4629 0.2748 -0.0083 -0.0216 0.0084  484 HOH   A O   
6497 O  O   . HOH   E .   ? 0.4003 0.2505 0.3710 -0.0422 -0.1054 0.0588  485 HOH   A O   
6498 O  O   B HOH   E .   ? 0.3245 0.3478 0.3390 0.0030  -0.0024 -0.1084 486 HOH   A O   
6499 O  O   . HOH   E .   ? 0.7377 0.3839 0.3098 -0.0431 -0.0830 -0.0173 487 HOH   A O   
6500 O  O   . HOH   E .   ? 0.6077 0.4545 0.3990 -0.0118 0.0591  -0.1420 488 HOH   A O   
6501 O  O   B HOH   E .   ? 0.2406 0.1316 0.2188 0.0618  -0.0156 0.0666  489 HOH   A O   
6502 O  O   . HOH   E .   ? 0.2325 0.2155 0.2598 0.0154  0.0054  0.0079  490 HOH   A O   
6503 O  O   . HOH   E .   ? 0.2779 0.5403 0.3341 0.1286  0.1096  0.2135  491 HOH   A O   
6504 O  O   . HOH   E .   ? 0.2563 0.4387 0.4533 0.0033  0.0718  0.1333  492 HOH   A O   
6505 O  O   . HOH   E .   ? 0.6329 0.6160 0.4630 0.0269  0.1163  0.0984  493 HOH   A O   
6506 O  O   . HOH   E .   ? 0.5044 0.3833 0.4136 -0.0282 0.1019  -0.0003 494 HOH   A O   
6507 O  O   . HOH   E .   ? 0.6263 0.5295 0.4667 -0.0878 -0.0911 -0.0972 495 HOH   A O   
6508 O  O   . HOH   E .   ? 0.5165 0.4607 0.5060 -0.0493 -0.1331 0.0785  496 HOH   A O   
6509 O  O   . HOH   E .   ? 0.3806 0.3488 0.2609 -0.0678 0.1103  -0.0365 497 HOH   A O   
6510 O  O   . HOH   E .   ? 0.2939 0.2050 0.5486 0.0261  0.0604  0.0945  498 HOH   A O   
6511 O  O   . HOH   E .   ? 0.4808 0.3362 0.4446 -0.0068 0.2446  0.0163  499 HOH   A O   
6512 O  O   . HOH   E .   ? 0.2430 0.2555 0.6881 -0.0103 -0.1152 0.0311  500 HOH   A O   
6513 O  O   . HOH   E .   ? 0.3816 0.2739 0.4335 -0.0691 0.0569  0.0741  501 HOH   A O   
6514 O  O   . HOH   E .   ? 0.4786 0.5227 0.5914 0.0476  0.1365  -0.1253 502 HOH   A O   
6515 O  O   . HOH   E .   ? 0.2322 0.3649 0.4640 0.0124  0.0725  -0.0887 503 HOH   A O   
6516 O  O   . HOH   E .   ? 0.3665 0.7821 0.5112 -0.1056 0.0079  0.2856  504 HOH   A O   
6517 O  O   . HOH   E .   ? 0.7153 0.6469 0.5564 0.1867  -0.1460 0.0787  505 HOH   A O   
6518 O  O   . HOH   E .   ? 0.2259 0.3110 0.3309 0.0354  -0.0375 0.0576  506 HOH   A O   
6519 O  O   . HOH   E .   ? 0.6577 0.2736 0.4598 -0.0626 0.0669  0.0719  507 HOH   A O   
6520 O  O   . HOH   E .   ? 0.4667 0.2346 0.4264 -0.1357 0.0316  0.0187  508 HOH   A O   
6521 O  O   . HOH   E .   ? 0.5387 0.7252 0.4801 0.1068  -0.0427 0.1144  509 HOH   A O   
6522 O  O   . HOH   E .   ? 0.2699 0.3786 0.3890 0.0393  -0.0102 0.0168  510 HOH   A O   
6523 O  O   B HOH   E .   ? 0.2315 0.3134 0.2917 0.0875  0.0544  0.1279  511 HOH   A O   
6524 O  O   . HOH   E .   ? 0.7138 0.5042 0.6140 0.0158  0.0565  0.0813  512 HOH   A O   
6525 O  O   B HOH   E .   ? 0.3394 0.2281 0.2581 -0.0032 -0.0406 0.0086  513 HOH   A O   
6526 O  O   . HOH   E .   ? 0.4358 0.6749 0.5246 0.2811  -0.0291 0.1118  514 HOH   A O   
6527 O  O   . HOH   E .   ? 0.2749 0.2138 0.4669 0.0171  0.0352  0.0399  515 HOH   A O   
6528 O  O   . HOH   E .   ? 0.4345 0.5700 0.4726 -0.0125 -0.0215 -0.1152 516 HOH   A O   
6529 O  O   A HOH   E .   ? 0.4275 0.6490 0.3889 0.0939  0.1602  0.0219  517 HOH   A O   
6530 O  O   . HOH   E .   ? 0.2535 0.6282 0.3017 0.0261  0.0190  0.0358  518 HOH   A O   
6531 O  O   . HOH   E .   ? 0.3912 0.4776 0.3575 0.0789  -0.0607 0.1046  519 HOH   A O   
6532 O  O   . HOH   E .   ? 0.4834 0.6012 0.5474 -0.0637 -0.0587 0.0314  520 HOH   A O   
6533 O  O   . HOH   E .   ? 0.3418 0.3927 0.5269 -0.0299 -0.0762 0.2259  521 HOH   A O   
6534 O  O   . HOH   F .   ? 0.2336 0.2005 0.2996 0.0283  0.0690  0.0308  201 HOH   B O   
6535 O  O   . HOH   F .   ? 0.5593 0.4883 0.2611 0.0895  -0.0840 -0.1317 202 HOH   B O   
6536 O  O   . HOH   F .   ? 0.3523 0.6486 0.3966 0.0822  0.0199  0.2369  203 HOH   B O   
6537 O  O   . HOH   F .   ? 0.2836 0.5438 0.4702 0.0090  0.1475  -0.1725 204 HOH   B O   
6538 O  O   . HOH   F .   ? 0.3547 0.2785 0.6353 -0.0466 0.0731  -0.0214 205 HOH   B O   
6539 O  O   . HOH   F .   ? 0.5045 0.3978 0.5787 0.0547  -0.0977 0.2487  206 HOH   B O   
6540 O  O   . HOH   F .   ? 0.4037 0.2875 0.3510 -0.0651 0.0294  -0.1003 207 HOH   B O   
6541 O  O   . HOH   F .   ? 0.6121 0.6440 0.5849 0.2013  0.0174  0.0120  208 HOH   B O   
6542 O  O   . HOH   F .   ? 0.6762 0.2698 0.4762 0.0691  0.1357  -0.0085 209 HOH   B O   
6543 O  O   . HOH   F .   ? 0.3783 0.4032 0.5074 -0.1288 0.0541  -0.1214 210 HOH   B O   
6544 O  O   . HOH   F .   ? 0.2573 0.3012 0.6385 0.0472  -0.0920 0.0640  211 HOH   B O   
6545 O  O   . HOH   F .   ? 0.4619 0.5549 0.3974 0.2776  -0.1175 -0.0427 212 HOH   B O   
6546 O  O   . HOH   F .   ? 0.3825 0.4469 0.3889 0.1710  -0.0384 0.0315  213 HOH   B O   
6547 O  O   . HOH   F .   ? 0.5814 0.2944 0.4543 -0.1649 0.0529  0.0195  214 HOH   B O   
6548 O  O   . HOH   F .   ? 0.1798 0.2367 0.3073 -0.0008 0.0142  -0.0264 215 HOH   B O   
6549 O  O   . HOH   F .   ? 0.1484 0.1812 0.2771 -0.0201 -0.0062 0.0069  216 HOH   B O   
6550 O  O   . HOH   F .   ? 0.4434 0.4009 0.3801 -0.0508 -0.1075 0.0692  217 HOH   B O   
6551 O  O   . HOH   F .   ? 0.4807 0.2002 0.3118 -0.0056 -0.0691 0.0093  218 HOH   B O   
6552 O  O   . HOH   F .   ? 0.4090 0.3843 0.6801 -0.0226 -0.1716 -0.1000 219 HOH   B O   
6553 O  O   . HOH   F .   ? 0.2647 0.2588 0.5380 0.0056  0.0360  0.0129  220 HOH   B O   
6554 O  O   . HOH   F .   ? 0.4441 0.4355 0.4215 0.0345  0.1345  -0.1078 221 HOH   B O   
6555 O  O   . HOH   F .   ? 0.2556 0.1714 0.2914 -0.0231 0.1196  0.0043  222 HOH   B O   
6556 O  O   . HOH   F .   ? 0.3575 0.4165 0.5149 -0.1546 0.0469  0.0774  223 HOH   B O   
6557 O  O   . HOH   F .   ? 0.5881 0.6211 0.3239 0.0345  -0.0388 -0.0007 224 HOH   B O   
6558 O  O   . HOH   F .   ? 0.3756 0.3525 0.2308 0.0553  0.0737  0.0596  225 HOH   B O   
6559 O  O   . HOH   F .   ? 0.6230 0.3959 0.5330 0.1163  0.0013  -0.0939 226 HOH   B O   
6560 O  O   . HOH   F .   ? 0.3032 0.1937 0.5187 0.0161  0.1885  0.0800  227 HOH   B O   
6561 O  O   . HOH   F .   ? 0.3067 0.2472 0.5032 0.0239  -0.0678 -0.0359 228 HOH   B O   
6562 O  O   . HOH   F .   ? 0.1684 0.2113 0.2840 -0.0098 0.0098  -0.0063 229 HOH   B O   
6563 O  O   . HOH   F .   ? 0.4234 0.6598 0.3950 0.2660  -0.0153 -0.0647 230 HOH   B O   
6564 O  O   . HOH   F .   ? 0.2886 0.4925 0.4934 0.1485  0.0253  -0.0851 231 HOH   B O   
6565 O  O   . HOH   F .   ? 0.2156 0.2113 0.3795 -0.0357 -0.0094 -0.0625 232 HOH   B O   
6566 O  O   . HOH   F .   ? 0.3435 0.1751 0.2286 0.0175  -0.0744 -0.0215 233 HOH   B O   
6567 O  O   . HOH   F .   ? 0.2717 0.3801 0.3264 -0.0743 0.0289  -0.0417 234 HOH   B O   
6568 O  O   . HOH   F .   ? 0.2041 0.2267 0.3051 -0.0542 -0.0001 -0.0320 235 HOH   B O   
6569 O  O   . HOH   F .   ? 0.2998 0.2151 0.4050 -0.0033 0.1264  0.0208  236 HOH   B O   
6570 O  O   . HOH   F .   ? 0.2062 0.1312 0.3544 0.0156  -0.0639 -0.0221 237 HOH   B O   
6571 O  O   . HOH   F .   ? 0.2746 0.2514 0.3145 0.0442  0.0084  -0.0848 238 HOH   B O   
6572 O  O   . HOH   F .   ? 0.2242 0.3646 0.2994 -0.0390 -0.0565 -0.0519 239 HOH   B O   
6573 O  O   . HOH   F .   ? 0.3637 0.2367 0.4087 0.0768  -0.0390 -0.0508 240 HOH   B O   
6574 O  O   . HOH   F .   ? 0.1445 0.1359 0.1643 -0.0117 0.0023  0.0009  241 HOH   B O   
6575 O  O   . HOH   F .   ? 0.1514 0.1424 0.2672 -0.0040 0.0002  -0.0084 242 HOH   B O   
6576 O  O   . HOH   F .   ? 0.4355 0.3345 0.4169 -0.2250 0.0134  0.0022  243 HOH   B O   
6577 O  O   . HOH   F .   ? 0.2772 0.4562 0.3321 -0.0925 -0.0359 -0.0737 244 HOH   B O   
6578 O  O   . HOH   F .   ? 0.3043 0.1699 0.5620 -0.0146 -0.1351 -0.0198 245 HOH   B O   
6579 O  O   . HOH   F .   ? 0.1460 0.1328 0.1590 0.0018  -0.0041 0.0129  246 HOH   B O   
6580 O  O   . HOH   F .   ? 0.2050 0.3908 0.2384 -0.0663 -0.0082 0.0613  247 HOH   B O   
6581 O  O   . HOH   F .   ? 0.2313 0.2005 0.1911 0.0149  0.0004  -0.0022 248 HOH   B O   
6582 O  O   . HOH   F .   ? 0.5284 0.2858 0.2710 0.0246  0.1029  -0.0247 249 HOH   B O   
6583 O  O   . HOH   F .   ? 0.3153 0.3364 0.2134 0.0590  0.0617  0.0174  250 HOH   B O   
6584 O  O   . HOH   F .   ? 0.3567 0.3097 0.4456 0.0688  -0.0830 -0.1580 251 HOH   B O   
6585 O  O   . HOH   F .   ? 0.3065 0.2203 0.2799 0.0904  0.0873  0.0141  252 HOH   B O   
6586 O  O   . HOH   F .   ? 0.2281 0.1932 0.2200 -0.0213 -0.0508 0.0095  253 HOH   B O   
6587 O  O   . HOH   F .   ? 0.2058 0.1512 0.2172 -0.0269 -0.0261 0.0274  254 HOH   B O   
6588 O  O   . HOH   F .   ? 0.3193 0.2345 0.3132 -0.0292 0.0264  -0.0567 255 HOH   B O   
6589 O  O   . HOH   F .   ? 0.1584 0.1597 0.2789 -0.0166 -0.0163 0.0005  256 HOH   B O   
6590 O  O   . HOH   F .   ? 0.2500 0.4656 0.4781 0.0357  0.0323  -0.0966 257 HOH   B O   
6591 O  O   . HOH   F .   ? 0.1369 0.1655 0.2089 -0.0075 0.0111  0.0181  258 HOH   B O   
6592 O  O   . HOH   F .   ? 0.2234 0.2892 0.2284 -0.0492 0.0258  0.0604  259 HOH   B O   
6593 O  O   . HOH   F .   ? 0.2185 0.1997 0.3653 0.0036  -0.0571 -0.0370 260 HOH   B O   
6594 O  O   . HOH   F .   ? 0.2988 0.4586 0.3803 -0.0188 -0.0980 0.1139  261 HOH   B O   
6595 O  O   . HOH   F .   ? 0.2451 0.2600 0.2693 -0.0579 -0.0768 -0.0316 262 HOH   B O   
6596 O  O   . HOH   F .   ? 0.2189 0.2108 0.2118 0.0119  -0.0102 0.0119  263 HOH   B O   
6597 O  O   . HOH   F .   ? 0.2626 0.3403 0.4889 -0.0347 0.0460  -0.1627 264 HOH   B O   
6598 O  O   . HOH   F .   ? 0.1887 0.1486 0.2438 -0.0276 -0.0207 0.0169  265 HOH   B O   
6599 O  O   . HOH   F .   ? 0.1723 0.1396 0.3644 -0.0009 -0.0313 -0.0059 266 HOH   B O   
6600 O  O   . HOH   F .   ? 0.2484 0.2027 0.3068 -0.0625 0.0279  -0.0044 267 HOH   B O   
6601 O  O   . HOH   F .   ? 0.2047 0.4185 0.4485 -0.0356 -0.0045 -0.1779 268 HOH   B O   
6602 O  O   . HOH   F .   ? 0.2456 0.2055 0.2626 0.0757  -0.0819 -0.0594 269 HOH   B O   
6603 O  O   . HOH   F .   ? 0.1868 0.2655 0.2662 0.0498  0.0416  0.0988  270 HOH   B O   
6604 O  O   . HOH   F .   ? 0.1853 0.1784 0.1640 -0.0346 -0.0345 0.0087  271 HOH   B O   
6605 O  O   . HOH   F .   ? 0.2724 0.2848 0.2359 -0.0470 -0.0854 0.0160  272 HOH   B O   
6606 O  O   . HOH   F .   ? 0.2281 0.3379 0.4896 0.0780  -0.0669 -0.0965 273 HOH   B O   
6607 O  O   . HOH   F .   ? 0.2292 0.2854 0.3118 -0.0377 0.0244  -0.0782 274 HOH   B O   
6608 O  O   . HOH   F .   ? 0.2571 0.3885 0.3547 0.0292  0.0925  0.0257  275 HOH   B O   
6609 O  O   . HOH   F .   ? 0.2269 0.2527 0.2323 0.0579  -0.0214 -0.0126 276 HOH   B O   
6610 O  O   . HOH   F .   ? 0.4312 0.4227 0.2469 0.1058  -0.0630 0.0088  277 HOH   B O   
6611 O  O   . HOH   F .   ? 0.4256 0.3070 0.4581 -0.0353 -0.1050 -0.0897 278 HOH   B O   
6612 O  O   . HOH   F .   ? 0.2909 0.6408 0.7202 0.1415  -0.0629 -0.0980 279 HOH   B O   
6613 O  O   . HOH   F .   ? 0.1551 0.1486 0.3246 -0.0102 0.0089  -0.0092 280 HOH   B O   
6614 O  O   . HOH   F .   ? 0.4420 0.3069 0.4413 -0.0960 0.0182  0.0940  281 HOH   B O   
6615 O  O   . HOH   F .   ? 0.4398 0.3113 0.2746 0.0566  -0.0321 -0.0752 282 HOH   B O   
6616 O  O   . HOH   F .   ? 0.4181 0.3741 0.4053 -0.1102 0.1182  -0.1161 283 HOH   B O   
6617 O  O   . HOH   F .   ? 0.3877 0.5104 0.4702 -0.0096 -0.1445 0.0043  284 HOH   B O   
6618 O  O   . HOH   F .   ? 0.3531 0.6112 0.3164 0.1821  -0.0739 -0.0013 285 HOH   B O   
6619 O  O   . HOH   F .   ? 0.3186 0.3736 0.4733 0.1135  -0.0692 -0.0744 286 HOH   B O   
6620 O  O   . HOH   F .   ? 0.1587 0.2011 0.1589 -0.0115 -0.0150 -0.0032 287 HOH   B O   
6621 O  O   . HOH   F .   ? 0.1586 0.1516 0.1832 0.0028  0.0002  0.0012  288 HOH   B O   
6622 O  O   . HOH   F .   ? 0.2444 0.2619 0.2736 0.0149  -0.0703 0.0186  289 HOH   B O   
6623 O  O   . HOH   F .   ? 0.2746 0.4720 0.4869 -0.1134 -0.1001 0.1166  290 HOH   B O   
6624 O  O   . HOH   F .   ? 0.5068 0.6360 0.2678 0.0532  -0.0895 0.0841  291 HOH   B O   
6625 O  O   . HOH   F .   ? 0.3739 0.2811 0.2166 0.0759  -0.0627 -0.0156 292 HOH   B O   
6626 O  O   . HOH   F .   ? 0.2688 0.2082 0.4370 0.0170  0.0463  0.0285  293 HOH   B O   
6627 O  O   . HOH   F .   ? 0.4544 0.3907 0.6198 0.0774  -0.0140 0.0468  294 HOH   B O   
6628 O  O   . HOH   F .   ? 0.2457 0.3127 0.4016 -0.0369 -0.1209 0.0688  295 HOH   B O   
6629 O  O   . HOH   F .   ? 0.2830 0.2896 0.2885 0.0104  -0.0024 -0.1261 296 HOH   B O   
6630 O  O   . HOH   F .   ? 0.2000 0.1603 0.2542 -0.0162 -0.0274 -0.0009 297 HOH   B O   
6631 O  O   . HOH   F .   ? 0.1600 0.1864 0.2806 0.0221  -0.0123 0.0051  298 HOH   B O   
6632 O  O   . HOH   F .   ? 0.3586 0.2167 0.4158 -0.0923 -0.2011 0.0803  299 HOH   B O   
6633 O  O   . HOH   F .   ? 0.1668 0.3029 0.4394 0.0150  -0.0112 -0.0975 300 HOH   B O   
6634 O  O   . HOH   F .   ? 0.2560 0.2757 0.5072 -0.0247 -0.0733 0.1009  301 HOH   B O   
6635 O  O   . HOH   F .   ? 0.1722 0.1483 0.2387 0.0060  -0.0003 0.0181  302 HOH   B O   
6636 O  O   . HOH   F .   ? 0.2532 0.6918 0.2744 0.0350  -0.0294 -0.0547 303 HOH   B O   
6637 O  O   . HOH   F .   ? 0.2748 0.3126 0.4002 -0.0944 0.1006  -0.0527 304 HOH   B O   
6638 O  O   . HOH   F .   ? 0.2079 0.2708 0.6019 0.0466  -0.0396 -0.1176 305 HOH   B O   
6639 O  O   . HOH   F .   ? 0.1530 0.1458 0.2819 0.0039  -0.0033 -0.0014 306 HOH   B O   
6640 O  O   . HOH   F .   ? 0.4671 0.4162 0.2680 0.1404  -0.0799 0.0544  307 HOH   B O   
6641 O  O   . HOH   F .   ? 0.1556 0.1902 0.2879 -0.0260 -0.0095 0.0058  308 HOH   B O   
6642 O  O   . HOH   F .   ? 0.4214 0.4263 0.1773 -0.0469 0.0287  0.0083  309 HOH   B O   
6643 O  O   . HOH   F .   ? 0.5408 0.2936 0.2608 -0.1907 0.0926  -0.0223 310 HOH   B O   
6644 O  O   . HOH   F .   ? 0.5759 0.3817 0.3180 0.2640  0.0980  0.0669  311 HOH   B O   
6645 O  O   . HOH   F .   ? 0.5868 0.4760 0.4780 -0.0976 -0.0138 0.0726  312 HOH   B O   
6646 O  O   . HOH   F .   ? 0.1995 0.1585 0.3305 0.0306  -0.0874 0.0029  313 HOH   B O   
6647 O  O   . HOH   F .   ? 0.6616 0.4451 0.4917 0.1463  0.0601  0.0119  314 HOH   B O   
6648 O  O   . HOH   F .   ? 0.3405 0.1876 0.3516 0.0818  0.1153  0.0515  315 HOH   B O   
6649 O  O   . HOH   F .   ? 0.3866 0.2150 0.3106 0.1342  0.1091  0.0236  316 HOH   B O   
6650 O  O   . HOH   F .   ? 0.2366 0.1476 0.2383 -0.0137 -0.0122 0.0284  317 HOH   B O   
6651 O  O   . HOH   F .   ? 0.2725 0.2733 0.3418 -0.0355 0.1007  -0.0641 318 HOH   B O   
6652 O  O   . HOH   F .   ? 0.1585 0.1583 0.2861 -0.0100 -0.0166 -0.0122 319 HOH   B O   
6653 O  O   . HOH   F .   ? 0.2033 0.1981 0.1919 -0.0026 0.0209  0.0216  320 HOH   B O   
6654 O  O   . HOH   F .   ? 0.2353 0.3014 0.4690 -0.0236 -0.0425 0.0051  321 HOH   B O   
6655 O  O   . HOH   F .   ? 0.1568 0.2980 0.2558 -0.0209 -0.0305 0.0838  322 HOH   B O   
6656 O  O   . HOH   F .   ? 0.4778 0.5840 0.3046 0.0172  -0.0809 0.0433  323 HOH   B O   
6657 O  O   . HOH   F .   ? 0.6789 0.6113 0.5104 0.3084  0.0775  0.0196  324 HOH   B O   
6658 O  O   . HOH   F .   ? 0.4627 0.2434 0.3193 0.0326  0.0179  0.0981  325 HOH   B O   
6659 O  O   . HOH   F .   ? 0.4329 0.4489 0.2486 0.0766  -0.0491 -0.0474 326 HOH   B O   
6660 O  O   . HOH   F .   ? 0.2629 0.2139 0.2341 0.0259  -0.0186 0.0217  327 HOH   B O   
6661 O  O   . HOH   F .   ? 0.1921 0.2007 0.2914 0.0351  0.0404  0.0211  328 HOH   B O   
6662 O  O   . HOH   F .   ? 0.4157 0.3311 0.5495 0.1072  0.2213  0.1825  329 HOH   B O   
6663 O  O   . HOH   F .   ? 0.6276 0.3446 0.3239 -0.0132 0.1169  0.1213  330 HOH   B O   
6664 O  O   . HOH   F .   ? 0.5021 0.3318 0.4210 0.0238  0.0353  -0.1531 331 HOH   B O   
6665 O  O   . HOH   F .   ? 0.1759 0.2907 0.2951 0.0398  -0.0089 -0.0607 332 HOH   B O   
6666 O  O   . HOH   F .   ? 0.2955 0.3901 0.7356 -0.0416 -0.0608 0.2320  333 HOH   B O   
6667 O  O   . HOH   F .   ? 0.5742 0.4239 0.6092 -0.0838 -0.0489 -0.1151 334 HOH   B O   
6668 O  O   . HOH   F .   ? 0.2254 0.4722 0.4882 -0.0201 0.0125  -0.0853 335 HOH   B O   
6669 O  O   . HOH   F .   ? 0.7762 0.2002 0.3113 0.0095  -0.0906 0.0114  336 HOH   B O   
6670 O  O   . HOH   F .   ? 0.5694 0.4615 0.6009 0.0850  -0.0699 0.1895  337 HOH   B O   
6671 O  O   . HOH   F .   ? 0.2681 0.2141 0.5031 -0.0097 0.0032  0.0350  338 HOH   B O   
6672 O  O   . HOH   F .   ? 0.2158 0.2273 0.5292 -0.0451 -0.0063 0.1295  339 HOH   B O   
6673 O  O   . HOH   F .   ? 0.1667 0.1519 0.2466 0.0096  -0.0160 0.0092  340 HOH   B O   
6674 O  O   . HOH   F .   ? 0.5076 0.3204 0.3222 0.0640  -0.1171 -0.0836 341 HOH   B O   
6675 O  O   . HOH   F .   ? 0.3870 0.5989 0.3856 -0.0812 -0.0953 -0.0639 342 HOH   B O   
6676 O  O   . HOH   F .   ? 0.4873 0.6875 0.3199 0.0255  -0.0092 0.1214  343 HOH   B O   
6677 O  O   . HOH   F .   ? 0.2088 0.1874 0.2705 -0.0033 0.0512  -0.0064 344 HOH   B O   
6678 O  O   . HOH   F .   ? 0.1726 0.5705 0.5728 -0.0304 -0.0338 0.0606  345 HOH   B O   
6679 O  O   . HOH   F .   ? 0.4384 0.4733 0.4962 0.0218  -0.1052 0.0821  346 HOH   B O   
6680 O  O   . HOH   F .   ? 0.5592 0.6199 0.2823 -0.0155 -0.0339 0.1025  347 HOH   B O   
6681 O  O   . HOH   F .   ? 0.2590 0.2194 0.5085 -0.0245 -0.0891 -0.0648 348 HOH   B O   
6682 O  O   . HOH   F .   ? 0.3538 0.2146 0.3752 -0.0440 -0.0321 -0.0743 349 HOH   B O   
6683 O  O   . HOH   F .   ? 0.2173 0.3425 0.5283 -0.0002 0.0412  0.0261  350 HOH   B O   
6684 O  O   . HOH   F .   ? 0.2377 0.5981 0.3735 0.1565  -0.0593 -0.1271 351 HOH   B O   
6685 O  O   . HOH   F .   ? 0.4458 0.6376 0.6662 0.0657  -0.0197 -0.0944 352 HOH   B O   
6686 O  O   . HOH   F .   ? 0.5222 0.5484 0.4541 -0.1223 0.0508  0.1131  353 HOH   B O   
6687 O  O   . HOH   F .   ? 0.5337 0.3629 0.4276 0.0668  0.1397  -0.0498 354 HOH   B O   
6688 O  O   . HOH   F .   ? 0.3543 0.4074 0.4623 -0.1534 0.0354  -0.0103 355 HOH   B O   
6689 O  O   . HOH   F .   ? 0.4736 0.2608 0.5502 -0.0748 0.1450  0.0647  356 HOH   B O   
6690 O  O   . HOH   F .   ? 0.3755 0.2899 0.4184 -0.0971 -0.0098 -0.0610 357 HOH   B O   
6691 O  O   . HOH   F .   ? 0.3271 0.1820 0.4087 0.0469  -0.1329 -0.0672 358 HOH   B O   
6692 O  O   . HOH   F .   ? 0.4782 0.5242 0.5533 -0.0586 -0.0247 0.0154  359 HOH   B O   
6693 O  O   . HOH   F .   ? 0.3947 0.3459 0.4329 0.0661  -0.1430 -0.0073 360 HOH   B O   
6694 O  O   . HOH   F .   ? 0.4439 0.5763 0.5710 0.1577  -0.1339 0.2068  361 HOH   B O   
6695 O  O   . HOH   F .   ? 0.4350 0.6666 0.3226 0.2478  -0.0352 0.0113  362 HOH   B O   
6696 O  O   . HOH   F .   ? 0.2069 0.3343 0.6850 -0.0544 -0.0421 -0.0873 363 HOH   B O   
6697 O  O   . HOH   F .   ? 0.4515 0.3989 0.6492 0.0324  0.0738  0.0835  364 HOH   B O   
6698 O  O   . HOH   F .   ? 0.5002 0.3430 0.5299 -0.1482 -0.0467 0.0196  365 HOH   B O   
6699 O  O   . HOH   F .   ? 0.5470 0.5506 0.3317 0.1307  -0.1533 0.0563  366 HOH   B O   
6700 O  O   . HOH   F .   ? 0.5636 0.4255 0.4342 0.0631  0.0903  0.0306  367 HOH   B O   
6701 O  O   . HOH   F .   ? 0.4962 0.3809 0.5192 0.1017  -0.1771 0.0068  368 HOH   B O   
6702 O  O   . HOH   F .   ? 0.4517 0.5413 0.6118 0.2515  0.1079  0.0808  369 HOH   B O   
6703 O  O   . HOH   F .   ? 0.5938 0.2205 0.3522 0.0062  0.0373  0.0431  370 HOH   B O   
6704 O  O   . HOH   F .   ? 0.7770 0.7674 0.5177 0.2962  -0.1388 0.1319  371 HOH   B O   
6705 O  O   . HOH   F .   ? 0.4757 0.5057 0.4342 0.0035  -0.0747 -0.0970 372 HOH   B O   
6706 O  O   . HOH   F .   ? 0.4077 0.3486 0.4744 0.0357  -0.1457 -0.0486 373 HOH   B O   
6707 O  O   . HOH   F .   ? 0.6056 0.4110 0.2977 -0.1314 -0.1023 -0.0358 374 HOH   B O   
6708 O  O   . HOH   F .   ? 0.2382 0.3991 0.4764 0.0370  -0.0802 -0.0427 375 HOH   B O   
6709 O  O   . HOH   F .   ? 0.7965 0.3654 0.5023 -0.0631 -0.0208 -0.0239 376 HOH   B O   
6710 O  O   . HOH   F .   ? 0.4834 0.7016 0.5862 0.1807  0.0957  0.2880  377 HOH   B O   
6711 O  O   . HOH   F .   ? 0.4672 0.4754 0.5231 -0.1040 -0.0883 0.0592  378 HOH   B O   
6712 O  O   . HOH   F .   ? 0.3229 0.3544 0.2379 0.0765  0.0268  0.0185  379 HOH   B O   
6713 O  O   . HOH   F .   ? 0.5613 0.6852 0.3928 -0.1519 0.0702  -0.1626 380 HOH   B O   
6714 O  O   . HOH   F .   ? 0.2887 0.2528 0.3593 0.0071  0.0243  0.0593  381 HOH   B O   
6715 O  O   . HOH   F .   ? 0.3447 0.4128 0.5030 0.1129  -0.0631 0.0274  382 HOH   B O   
6716 O  O   . HOH   F .   ? 0.5730 0.6734 0.5971 0.0328  0.2301  0.1051  383 HOH   B O   
6717 O  O   . HOH   F .   ? 0.4198 0.7436 0.6121 0.0695  0.2323  0.1015  384 HOH   B O   
6718 O  O   . HOH   F .   ? 0.5762 0.4722 0.5270 -0.0658 0.0033  -0.0081 385 HOH   B O   
6719 O  O   . HOH   F .   ? 0.7629 0.6763 0.4547 0.2325  -0.0005 0.0317  386 HOH   B O   
6720 O  O   . HOH   F .   ? 0.2402 0.4171 0.3624 -0.0689 -0.0912 -0.0403 387 HOH   B O   
6721 O  O   . HOH   F .   ? 0.4729 0.3719 0.2978 0.0289  0.0330  0.0032  388 HOH   B O   
6722 O  O   . HOH   F .   ? 0.7234 0.4438 0.4554 0.1145  0.0994  -0.0951 389 HOH   B O   
6723 O  O   . HOH   F .   ? 0.5456 0.4518 0.4127 -0.0115 -0.0626 -0.0389 390 HOH   B O   
6724 O  O   . HOH   F .   ? 0.4080 0.2377 0.3191 0.0986  -0.0060 0.0199  391 HOH   B O   
6725 O  O   . HOH   F .   ? 0.4886 0.4246 0.3316 -0.0058 0.0300  0.0618  392 HOH   B O   
6726 O  O   . HOH   F .   ? 0.4169 0.2252 0.5522 -0.0497 0.0749  0.0248  393 HOH   B O   
6727 O  O   . HOH   F .   ? 0.2441 0.4057 0.6155 -0.1261 -0.0727 0.0611  394 HOH   B O   
6728 O  O   . HOH   F .   ? 0.4027 0.5551 0.3330 0.1155  -0.0514 -0.0863 395 HOH   B O   
6729 O  O   . HOH   F .   ? 0.3014 0.3813 0.3573 0.0519  0.0167  -0.0365 396 HOH   B O   
6730 O  O   . HOH   F .   ? 0.4172 0.3946 0.3940 -0.0020 0.0949  0.0657  397 HOH   B O   
6731 O  O   . HOH   F .   ? 0.2285 0.2866 0.4686 -0.0568 -0.0827 -0.0158 398 HOH   B O   
6732 O  O   . HOH   F .   ? 0.5936 0.6237 0.6662 0.1386  -0.1010 0.1711  399 HOH   B O   
6733 O  O   . HOH   F .   ? 0.5454 0.4259 0.3127 -0.2290 -0.0061 0.1036  400 HOH   B O   
6734 O  O   . HOH   F .   ? 0.5821 0.6251 0.3692 0.1665  -0.0120 0.0159  401 HOH   B O   
# 
