data_7HDV
# 
_entry.id   7HDV 
# 
_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   7HDV         pdb_00007hdv 10.2210/pdb7hdv/pdb 
WWPDB D_1001407349 ?            ?                   
# 
_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                        7HDV 
_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 'trifluoroacetic acid'                                          114.023   1   ?                      ? ? ? 
3 non-polymer syn '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pent-4-yn-1-ol' 216.239   1   ?                      ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                  35.453    1   ?                      ? ? ? 
5 water       nat water                                                           18.015    417 ?                      ? ? ? 
# 
_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 'trifluoroacetic acid'                                          TFA   
3 '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pent-4-yn-1-ol' A1A84 
4 'CHLORIDE ION'                                                  CL    
5 water                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1A84 non-polymer         . '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]pent-4-yn-1-ol' ? 'C11 H12 N4 O'   216.239 
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                          ? 'C2 H F3 O2'     114.023 
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 TFA   1   201 201  TFA   TFA A . 
D 3 A1A84 1   202 201  A1A84 LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 292  HOH   HOH A . 
F 5 HOH   2   302 196  HOH   HOH A . 
F 5 HOH   3   303 229  HOH   HOH A . 
F 5 HOH   4   304 625  HOH   HOH A . 
F 5 HOH   5   305 86   HOH   HOH A . 
F 5 HOH   6   306 9    HOH   HOH A . 
F 5 HOH   7   307 1301 HOH   HOH A . 
F 5 HOH   8   308 409  HOH   HOH A . 
F 5 HOH   9   309 405  HOH   HOH A . 
F 5 HOH   10  310 209  HOH   HOH A . 
F 5 HOH   11  311 493  HOH   HOH A . 
F 5 HOH   12  312 124  HOH   HOH A . 
F 5 HOH   13  313 661  HOH   HOH A . 
F 5 HOH   14  314 18   HOH   HOH A . 
F 5 HOH   15  315 247  HOH   HOH A . 
F 5 HOH   16  316 136  HOH   HOH A . 
F 5 HOH   17  317 76   HOH   HOH A . 
F 5 HOH   18  318 192  HOH   HOH A . 
F 5 HOH   19  319 109  HOH   HOH A . 
F 5 HOH   20  320 1295 HOH   HOH A . 
F 5 HOH   21  321 105  HOH   HOH A . 
F 5 HOH   22  322 337  HOH   HOH A . 
F 5 HOH   23  323 1283 HOH   HOH A . 
F 5 HOH   24  324 1290 HOH   HOH A . 
F 5 HOH   25  325 469  HOH   HOH A . 
F 5 HOH   26  326 2    HOH   HOH A . 
F 5 HOH   27  327 281  HOH   HOH A . 
F 5 HOH   28  328 236  HOH   HOH A . 
F 5 HOH   29  329 15   HOH   HOH A . 
F 5 HOH   30  330 151  HOH   HOH A . 
F 5 HOH   31  331 1300 HOH   HOH A . 
F 5 HOH   32  332 153  HOH   HOH A . 
F 5 HOH   33  333 1310 HOH   HOH A . 
F 5 HOH   34  334 165  HOH   HOH A . 
F 5 HOH   35  335 225  HOH   HOH A . 
F 5 HOH   36  336 241  HOH   HOH A . 
F 5 HOH   37  337 140  HOH   HOH A . 
F 5 HOH   38  338 393  HOH   HOH A . 
F 5 HOH   39  339 6    HOH   HOH A . 
F 5 HOH   40  340 164  HOH   HOH A . 
F 5 HOH   41  341 57   HOH   HOH A . 
F 5 HOH   42  342 630  HOH   HOH A . 
F 5 HOH   43  343 964  HOH   HOH A . 
F 5 HOH   44  344 92   HOH   HOH A . 
F 5 HOH   45  345 42   HOH   HOH A . 
F 5 HOH   46  346 169  HOH   HOH A . 
F 5 HOH   47  347 39   HOH   HOH A . 
F 5 HOH   48  348 24   HOH   HOH A . 
F 5 HOH   49  349 320  HOH   HOH A . 
F 5 HOH   50  350 2    HOH   HOH A . 
F 5 HOH   51  351 1308 HOH   HOH A . 
F 5 HOH   52  352 93   HOH   HOH A . 
F 5 HOH   53  353 33   HOH   HOH A . 
F 5 HOH   54  354 195  HOH   HOH A . 
F 5 HOH   55  355 155  HOH   HOH A . 
F 5 HOH   56  356 8    HOH   HOH A . 
F 5 HOH   57  357 81   HOH   HOH A . 
F 5 HOH   58  358 102  HOH   HOH A . 
F 5 HOH   59  359 19   HOH   HOH A . 
F 5 HOH   60  360 66   HOH   HOH A . 
F 5 HOH   61  361 939  HOH   HOH A . 
F 5 HOH   62  362 56   HOH   HOH A . 
F 5 HOH   63  363 354  HOH   HOH A . 
F 5 HOH   64  364 218  HOH   HOH A . 
F 5 HOH   65  365 139  HOH   HOH A . 
F 5 HOH   66  366 21   HOH   HOH A . 
F 5 HOH   67  367 296  HOH   HOH A . 
F 5 HOH   68  368 5    HOH   HOH A . 
F 5 HOH   69  369 17   HOH   HOH A . 
F 5 HOH   70  370 26   HOH   HOH A . 
F 5 HOH   71  371 159  HOH   HOH A . 
F 5 HOH   72  372 162  HOH   HOH A . 
F 5 HOH   73  373 45   HOH   HOH A . 
F 5 HOH   74  374 27   HOH   HOH A . 
F 5 HOH   75  375 366  HOH   HOH A . 
F 5 HOH   76  376 140  HOH   HOH A . 
F 5 HOH   77  377 396  HOH   HOH A . 
F 5 HOH   78  378 138  HOH   HOH A . 
F 5 HOH   79  379 49   HOH   HOH A . 
F 5 HOH   80  380 132  HOH   HOH A . 
F 5 HOH   81  381 36   HOH   HOH A . 
F 5 HOH   82  382 134  HOH   HOH A . 
F 5 HOH   83  383 461  HOH   HOH A . 
F 5 HOH   84  384 186  HOH   HOH A . 
F 5 HOH   85  385 122  HOH   HOH A . 
F 5 HOH   86  386 62   HOH   HOH A . 
F 5 HOH   87  387 35   HOH   HOH A . 
F 5 HOH   88  388 74   HOH   HOH A . 
F 5 HOH   89  389 46   HOH   HOH A . 
F 5 HOH   90  390 6    HOH   HOH A . 
F 5 HOH   91  391 154  HOH   HOH A . 
F 5 HOH   92  392 58   HOH   HOH A . 
F 5 HOH   93  393 85   HOH   HOH A . 
F 5 HOH   94  394 70   HOH   HOH A . 
F 5 HOH   95  395 303  HOH   HOH A . 
F 5 HOH   96  396 3    HOH   HOH A . 
F 5 HOH   97  397 116  HOH   HOH A . 
F 5 HOH   98  398 333  HOH   HOH A . 
F 5 HOH   99  399 662  HOH   HOH A . 
F 5 HOH   100 400 34   HOH   HOH A . 
F 5 HOH   101 401 12   HOH   HOH A . 
F 5 HOH   102 402 115  HOH   HOH A . 
F 5 HOH   103 403 381  HOH   HOH A . 
F 5 HOH   104 404 4    HOH   HOH A . 
F 5 HOH   105 405 148  HOH   HOH A . 
F 5 HOH   106 406 1313 HOH   HOH A . 
F 5 HOH   107 407 199  HOH   HOH A . 
F 5 HOH   108 408 1275 HOH   HOH A . 
F 5 HOH   109 409 25   HOH   HOH A . 
F 5 HOH   110 410 1315 HOH   HOH A . 
F 5 HOH   111 411 96   HOH   HOH A . 
F 5 HOH   112 412 351  HOH   HOH A . 
F 5 HOH   113 413 83   HOH   HOH A . 
F 5 HOH   114 414 78   HOH   HOH A . 
F 5 HOH   115 415 121  HOH   HOH A . 
F 5 HOH   116 416 3    HOH   HOH A . 
F 5 HOH   117 417 67   HOH   HOH A . 
F 5 HOH   118 418 123  HOH   HOH A . 
F 5 HOH   119 419 68   HOH   HOH A . 
F 5 HOH   120 420 278  HOH   HOH A . 
F 5 HOH   121 421 125  HOH   HOH A . 
F 5 HOH   122 422 53   HOH   HOH A . 
F 5 HOH   123 423 1068 HOH   HOH A . 
F 5 HOH   124 424 51   HOH   HOH A . 
F 5 HOH   125 425 95   HOH   HOH A . 
F 5 HOH   126 426 1279 HOH   HOH A . 
F 5 HOH   127 427 7    HOH   HOH A . 
F 5 HOH   128 428 156  HOH   HOH A . 
F 5 HOH   129 429 397  HOH   HOH A . 
F 5 HOH   130 430 1222 HOH   HOH A . 
F 5 HOH   131 431 582  HOH   HOH A . 
F 5 HOH   132 432 1296 HOH   HOH A . 
F 5 HOH   133 433 71   HOH   HOH A . 
F 5 HOH   134 434 188  HOH   HOH A . 
F 5 HOH   135 435 212  HOH   HOH A . 
F 5 HOH   136 436 1289 HOH   HOH A . 
F 5 HOH   137 437 1238 HOH   HOH A . 
F 5 HOH   138 438 80   HOH   HOH A . 
F 5 HOH   139 439 73   HOH   HOH A . 
F 5 HOH   140 440 16   HOH   HOH A . 
F 5 HOH   141 441 1094 HOH   HOH A . 
F 5 HOH   142 442 1286 HOH   HOH A . 
F 5 HOH   143 443 94   HOH   HOH A . 
F 5 HOH   144 444 1309 HOH   HOH A . 
F 5 HOH   145 445 8    HOH   HOH A . 
F 5 HOH   146 446 79   HOH   HOH A . 
F 5 HOH   147 447 40   HOH   HOH A . 
F 5 HOH   148 448 944  HOH   HOH A . 
F 5 HOH   149 449 104  HOH   HOH A . 
F 5 HOH   150 450 97   HOH   HOH A . 
F 5 HOH   151 451 952  HOH   HOH A . 
F 5 HOH   152 452 1189 HOH   HOH A . 
F 5 HOH   153 453 576  HOH   HOH A . 
F 5 HOH   154 454 1134 HOH   HOH A . 
F 5 HOH   155 455 330  HOH   HOH A . 
F 5 HOH   156 456 1119 HOH   HOH A . 
F 5 HOH   157 457 509  HOH   HOH A . 
F 5 HOH   158 458 107  HOH   HOH A . 
F 5 HOH   159 459 726  HOH   HOH A . 
F 5 HOH   160 460 163  HOH   HOH A . 
F 5 HOH   161 461 408  HOH   HOH A . 
F 5 HOH   162 462 1    HOH   HOH A . 
F 5 HOH   163 463 756  HOH   HOH A . 
F 5 HOH   164 464 319  HOH   HOH A . 
F 5 HOH   165 465 126  HOH   HOH A . 
F 5 HOH   166 466 556  HOH   HOH A . 
F 5 HOH   167 467 63   HOH   HOH A . 
F 5 HOH   168 468 280  HOH   HOH A . 
F 5 HOH   169 469 801  HOH   HOH A . 
F 5 HOH   170 470 361  HOH   HOH A . 
F 5 HOH   171 471 342  HOH   HOH A . 
F 5 HOH   172 472 1307 HOH   HOH A . 
F 5 HOH   173 473 1276 HOH   HOH A . 
F 5 HOH   174 474 250  HOH   HOH A . 
F 5 HOH   175 475 370  HOH   HOH A . 
F 5 HOH   176 476 1287 HOH   HOH A . 
F 5 HOH   177 477 224  HOH   HOH A . 
F 5 HOH   178 478 674  HOH   HOH A . 
F 5 HOH   179 479 1306 HOH   HOH A . 
F 5 HOH   180 480 695  HOH   HOH A . 
F 5 HOH   181 481 267  HOH   HOH A . 
F 5 HOH   182 482 919  HOH   HOH A . 
F 5 HOH   183 483 135  HOH   HOH A . 
F 5 HOH   184 484 318  HOH   HOH A . 
F 5 HOH   185 485 202  HOH   HOH A . 
F 5 HOH   186 486 521  HOH   HOH A . 
F 5 HOH   187 487 1299 HOH   HOH A . 
F 5 HOH   188 488 309  HOH   HOH A . 
F 5 HOH   189 489 1314 HOH   HOH A . 
F 5 HOH   190 490 331  HOH   HOH A . 
F 5 HOH   191 491 941  HOH   HOH A . 
F 5 HOH   192 492 805  HOH   HOH A . 
F 5 HOH   193 493 315  HOH   HOH A . 
F 5 HOH   194 494 711  HOH   HOH A . 
F 5 HOH   195 495 263  HOH   HOH A . 
F 5 HOH   196 496 152  HOH   HOH A . 
F 5 HOH   197 497 208  HOH   HOH A . 
F 5 HOH   198 498 1284 HOH   HOH A . 
F 5 HOH   199 499 356  HOH   HOH A . 
F 5 HOH   200 500 4    HOH   HOH A . 
F 5 HOH   201 501 326  HOH   HOH A . 
F 5 HOH   202 502 7    HOH   HOH A . 
F 5 HOH   203 503 180  HOH   HOH A . 
F 5 HOH   204 504 1071 HOH   HOH A . 
F 5 HOH   205 505 363  HOH   HOH A . 
F 5 HOH   206 506 371  HOH   HOH A . 
F 5 HOH   207 507 313  HOH   HOH A . 
F 5 HOH   208 508 429  HOH   HOH A . 
F 5 HOH   209 509 185  HOH   HOH A . 
F 5 HOH   210 510 70   HOH   HOH A . 
F 5 HOH   211 511 376  HOH   HOH A . 
F 5 HOH   212 512 772  HOH   HOH A . 
F 5 HOH   213 513 1074 HOH   HOH A . 
F 5 HOH   214 514 1292 HOH   HOH A . 
F 5 HOH   215 515 346  HOH   HOH A . 
F 5 HOH   216 516 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 240  HOH   HOH B . 
G 5 HOH   4   204 364  HOH   HOH B . 
G 5 HOH   5   205 1249 HOH   HOH B . 
G 5 HOH   6   206 758  HOH   HOH B . 
G 5 HOH   7   207 205  HOH   HOH B . 
G 5 HOH   8   208 531  HOH   HOH B . 
G 5 HOH   9   209 398  HOH   HOH B . 
G 5 HOH   10  210 358  HOH   HOH B . 
G 5 HOH   11  211 120  HOH   HOH B . 
G 5 HOH   12  212 50   HOH   HOH B . 
G 5 HOH   13  213 264  HOH   HOH B . 
G 5 HOH   14  214 743  HOH   HOH B . 
G 5 HOH   15  215 353  HOH   HOH B . 
G 5 HOH   16  216 232  HOH   HOH B . 
G 5 HOH   17  217 900  HOH   HOH B . 
G 5 HOH   18  218 1278 HOH   HOH B . 
G 5 HOH   19  219 452  HOH   HOH B . 
G 5 HOH   20  220 172  HOH   HOH B . 
G 5 HOH   21  221 1140 HOH   HOH B . 
G 5 HOH   22  222 332  HOH   HOH B . 
G 5 HOH   23  223 82   HOH   HOH B . 
G 5 HOH   24  224 444  HOH   HOH B . 
G 5 HOH   25  225 343  HOH   HOH B . 
G 5 HOH   26  226 75   HOH   HOH B . 
G 5 HOH   27  227 654  HOH   HOH B . 
G 5 HOH   28  228 131  HOH   HOH B . 
G 5 HOH   29  229 54   HOH   HOH B . 
G 5 HOH   30  230 60   HOH   HOH B . 
G 5 HOH   31  231 166  HOH   HOH B . 
G 5 HOH   32  232 723  HOH   HOH B . 
G 5 HOH   33  233 325  HOH   HOH B . 
G 5 HOH   34  234 69   HOH   HOH B . 
G 5 HOH   35  235 1    HOH   HOH B . 
G 5 HOH   36  236 127  HOH   HOH B . 
G 5 HOH   37  237 282  HOH   HOH B . 
G 5 HOH   38  238 133  HOH   HOH B . 
G 5 HOH   39  239 128  HOH   HOH B . 
G 5 HOH   40  240 110  HOH   HOH B . 
G 5 HOH   41  241 276  HOH   HOH B . 
G 5 HOH   42  242 1312 HOH   HOH B . 
G 5 HOH   43  243 14   HOH   HOH B . 
G 5 HOH   44  244 30   HOH   HOH B . 
G 5 HOH   45  245 300  HOH   HOH B . 
G 5 HOH   46  246 143  HOH   HOH B . 
G 5 HOH   47  247 129  HOH   HOH B . 
G 5 HOH   48  248 231  HOH   HOH B . 
G 5 HOH   49  249 9    HOH   HOH B . 
G 5 HOH   50  250 41   HOH   HOH B . 
G 5 HOH   51  251 181  HOH   HOH B . 
G 5 HOH   52  252 272  HOH   HOH B . 
G 5 HOH   53  253 52   HOH   HOH B . 
G 5 HOH   54  254 144  HOH   HOH B . 
G 5 HOH   55  255 72   HOH   HOH B . 
G 5 HOH   56  256 221  HOH   HOH B . 
G 5 HOH   57  257 391  HOH   HOH B . 
G 5 HOH   58  258 31   HOH   HOH B . 
G 5 HOH   59  259 150  HOH   HOH B . 
G 5 HOH   60  260 10   HOH   HOH B . 
G 5 HOH   61  261 47   HOH   HOH B . 
G 5 HOH   62  262 347  HOH   HOH B . 
G 5 HOH   63  263 271  HOH   HOH B . 
G 5 HOH   64  264 103  HOH   HOH B . 
G 5 HOH   65  265 302  HOH   HOH B . 
G 5 HOH   66  266 117  HOH   HOH B . 
G 5 HOH   67  267 11   HOH   HOH B . 
G 5 HOH   68  268 59   HOH   HOH B . 
G 5 HOH   69  269 252  HOH   HOH B . 
G 5 HOH   70  270 242  HOH   HOH B . 
G 5 HOH   71  271 243  HOH   HOH B . 
G 5 HOH   72  272 287  HOH   HOH B . 
G 5 HOH   73  273 77   HOH   HOH B . 
G 5 HOH   74  274 20   HOH   HOH B . 
G 5 HOH   75  275 61   HOH   HOH B . 
G 5 HOH   76  276 147  HOH   HOH B . 
G 5 HOH   77  277 114  HOH   HOH B . 
G 5 HOH   78  278 84   HOH   HOH B . 
G 5 HOH   79  279 216  HOH   HOH B . 
G 5 HOH   80  280 416  HOH   HOH B . 
G 5 HOH   81  281 1305 HOH   HOH B . 
G 5 HOH   82  282 89   HOH   HOH B . 
G 5 HOH   83  283 1277 HOH   HOH B . 
G 5 HOH   84  284 235  HOH   HOH B . 
G 5 HOH   85  285 22   HOH   HOH B . 
G 5 HOH   86  286 175  HOH   HOH B . 
G 5 HOH   87  287 43   HOH   HOH B . 
G 5 HOH   88  288 106  HOH   HOH B . 
G 5 HOH   89  289 88   HOH   HOH B . 
G 5 HOH   90  290 13   HOH   HOH B . 
G 5 HOH   91  291 1106 HOH   HOH B . 
G 5 HOH   92  292 1066 HOH   HOH B . 
G 5 HOH   93  293 137  HOH   HOH B . 
G 5 HOH   94  294 99   HOH   HOH B . 
G 5 HOH   95  295 1285 HOH   HOH B . 
G 5 HOH   96  296 220  HOH   HOH B . 
G 5 HOH   97  297 160  HOH   HOH B . 
G 5 HOH   98  298 311  HOH   HOH B . 
G 5 HOH   99  299 297  HOH   HOH B . 
G 5 HOH   100 300 387  HOH   HOH B . 
G 5 HOH   101 301 38   HOH   HOH B . 
G 5 HOH   102 302 112  HOH   HOH B . 
G 5 HOH   103 303 142  HOH   HOH B . 
G 5 HOH   104 304 299  HOH   HOH B . 
G 5 HOH   105 305 101  HOH   HOH B . 
G 5 HOH   106 306 215  HOH   HOH B . 
G 5 HOH   107 307 32   HOH   HOH B . 
G 5 HOH   108 308 316  HOH   HOH B . 
G 5 HOH   109 309 23   HOH   HOH B . 
G 5 HOH   110 310 118  HOH   HOH B . 
G 5 HOH   111 311 37   HOH   HOH B . 
G 5 HOH   112 312 48   HOH   HOH B . 
G 5 HOH   113 313 28   HOH   HOH B . 
G 5 HOH   114 314 182  HOH   HOH B . 
G 5 HOH   115 315 91   HOH   HOH B . 
G 5 HOH   116 316 170  HOH   HOH B . 
G 5 HOH   117 317 44   HOH   HOH B . 
G 5 HOH   118 318 197  HOH   HOH B . 
G 5 HOH   119 319 207  HOH   HOH B . 
G 5 HOH   120 320 177  HOH   HOH B . 
G 5 HOH   121 321 341  HOH   HOH B . 
G 5 HOH   122 322 704  HOH   HOH B . 
G 5 HOH   123 323 161  HOH   HOH B . 
G 5 HOH   124 324 635  HOH   HOH B . 
G 5 HOH   125 325 100  HOH   HOH B . 
G 5 HOH   126 326 29   HOH   HOH B . 
G 5 HOH   127 327 1274 HOH   HOH B . 
G 5 HOH   128 328 98   HOH   HOH B . 
G 5 HOH   129 329 55   HOH   HOH B . 
G 5 HOH   130 330 1294 HOH   HOH B . 
G 5 HOH   131 331 141  HOH   HOH B . 
G 5 HOH   132 332 1291 HOH   HOH B . 
G 5 HOH   133 333 334  HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 1126 HOH   HOH B . 
G 5 HOH   136 336 65   HOH   HOH B . 
G 5 HOH   137 337 234  HOH   HOH B . 
G 5 HOH   138 338 445  HOH   HOH B . 
G 5 HOH   139 339 619  HOH   HOH B . 
G 5 HOH   140 340 960  HOH   HOH B . 
G 5 HOH   141 341 1293 HOH   HOH B . 
G 5 HOH   142 342 362  HOH   HOH B . 
G 5 HOH   143 343 87   HOH   HOH B . 
G 5 HOH   144 344 178  HOH   HOH B . 
G 5 HOH   145 345 90   HOH   HOH B . 
G 5 HOH   146 346 339  HOH   HOH B . 
G 5 HOH   147 347 1304 HOH   HOH B . 
G 5 HOH   148 348 463  HOH   HOH B . 
G 5 HOH   149 349 623  HOH   HOH B . 
G 5 HOH   150 350 191  HOH   HOH B . 
G 5 HOH   151 351 1046 HOH   HOH B . 
G 5 HOH   152 352 335  HOH   HOH B . 
G 5 HOH   153 353 1280 HOH   HOH B . 
G 5 HOH   154 354 304  HOH   HOH B . 
G 5 HOH   155 355 290  HOH   HOH B . 
G 5 HOH   156 356 541  HOH   HOH B . 
G 5 HOH   157 357 203  HOH   HOH B . 
G 5 HOH   158 358 1077 HOH   HOH B . 
G 5 HOH   159 359 389  HOH   HOH B . 
G 5 HOH   160 360 718  HOH   HOH B . 
G 5 HOH   161 361 283  HOH   HOH B . 
G 5 HOH   162 362 1072 HOH   HOH B . 
G 5 HOH   163 363 479  HOH   HOH B . 
G 5 HOH   164 364 291  HOH   HOH B . 
G 5 HOH   165 365 615  HOH   HOH B . 
G 5 HOH   166 366 1316 HOH   HOH B . 
G 5 HOH   167 367 898  HOH   HOH B . 
G 5 HOH   168 368 340  HOH   HOH B . 
G 5 HOH   169 369 373  HOH   HOH B . 
G 5 HOH   170 370 667  HOH   HOH B . 
G 5 HOH   171 371 190  HOH   HOH B . 
G 5 HOH   172 372 1303 HOH   HOH B . 
G 5 HOH   173 373 310  HOH   HOH B . 
G 5 HOH   174 374 431  HOH   HOH B . 
G 5 HOH   175 375 1173 HOH   HOH B . 
G 5 HOH   176 376 1000 HOH   HOH B . 
G 5 HOH   177 377 149  HOH   HOH B . 
G 5 HOH   178 378 418  HOH   HOH B . 
G 5 HOH   179 379 183  HOH   HOH B . 
G 5 HOH   180 380 1163 HOH   HOH B . 
G 5 HOH   181 381 1311 HOH   HOH B . 
G 5 HOH   182 382 176  HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 491  HOH   HOH B . 
G 5 HOH   185 385 981  HOH   HOH B . 
G 5 HOH   186 386 1298 HOH   HOH B . 
G 5 HOH   187 387 248  HOH   HOH B . 
G 5 HOH   188 388 470  HOH   HOH B . 
G 5 HOH   189 389 265  HOH   HOH B . 
G 5 HOH   190 390 350  HOH   HOH B . 
G 5 HOH   191 391 184  HOH   HOH B . 
G 5 HOH   192 392 360  HOH   HOH B . 
G 5 HOH   193 393 355  HOH   HOH B . 
G 5 HOH   194 394 410  HOH   HOH B . 
G 5 HOH   195 395 274  HOH   HOH B . 
G 5 HOH   196 396 314  HOH   HOH B . 
G 5 HOH   197 397 157  HOH   HOH B . 
G 5 HOH   198 398 566  HOH   HOH B . 
G 5 HOH   199 399 321  HOH   HOH B . 
G 5 HOH   200 400 792  HOH   HOH B . 
G 5 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           7HDV 
_cell.length_a           88.737 
_cell.length_b           88.737 
_cell.length_c           39.425 
_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                         7HDV 
_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          7HDV 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.48 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HDV 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.370 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   175524 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.037 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.900 
_reflns.B_iso_Wilson_estimate        12.410 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.040 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1082428 
_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 0.980 1.000  ? 27445 8372 ? 1.233 ? ? ? 3.300 ? 0.600  ? ? ? ? ? ? 96.500 1.463 0.759 0.428 
1 2 5.370 44.370 ? 8020  1165 ? 0.024 ? ? ? 6.900 ? 62.700 ? ? ? ? ? ? 99.900 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HDV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             44.3700 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7400 
_refine.ls_number_reflns_obs                     175371 
_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                          0.1464 
_refine.ls_R_factor_R_work                       0.1458 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1583 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8454 
_refine.ls_number_reflns_R_work                  166917 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.5809 
_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                                72.450 
_refine.B_iso_min                                9.530 
_refine.pdbx_overall_phase_error                 17.9200 
_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                       0.9800 
_refine_hist.d_res_low                        44.3700 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             417 
_refine_hist.number_atoms_total               2995 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           18.14 
_refine_hist.pdbx_B_iso_mean_solvent          30.98 
_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 
0.9800 0.9900  30 94.0000  5218 . 0.4447 0.4293 . 275 0.0000 5493 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 99.0000  5479 . 0.3851 0.3718 . 272 0.0000 5751 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 100.0000 5552 . 0.3434 0.2971 . 274 0.0000 5826 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5585 . 0.2824 0.2788 . 247 0.0000 5832 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5522 . 0.2567 0.2603 . 313 0.0000 5835 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5534 . 0.2316 0.2481 . 297 0.0000 5831 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5533 . 0.2076 0.2245 . 310 0.0000 5843 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5521 . 0.1850 0.2050 . 253 0.0000 5774 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5597 . 0.1706 0.1875 . 282 0.0000 5879 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5534 . 0.1598 0.1660 . 286 0.0000 5820 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5588 . 0.1532 0.1885 . 254 0.0000 5842 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5561 . 0.1459 0.1613 . 269 0.0000 5830 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5587 . 0.1358 0.1634 . 291 0.0000 5878 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5439 . 0.1291 0.1543 . 308 0.0000 5747 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5666 . 0.1246 0.1564 . 243 0.0000 5909 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5566 . 0.1276 0.1445 . 281 0.0000 5847 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5534 . 0.1278 0.1326 . 282 0.0000 5816 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5558 . 0.1276 0.1455 . 309 0.0000 5867 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5555 . 0.1358 0.1579 . 290 0.0000 5845 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5628 . 0.1354 0.1654 . 243 0.0000 5871 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5542 . 0.1328 0.1446 . 306 0.0000 5848 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5589 . 0.1203 0.1223 . 263 0.0000 5852 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5573 . 0.1211 0.1382 . 305 0.0000 5878 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5591 . 0.1225 0.1348 . 275 0.0000 5866 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5612 . 0.1329 0.1510 . 270 0.0000 5882 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5570 . 0.1327 0.1412 . 293 0.0000 5863 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5630 . 0.1362 0.1380 . 290 0.0000 5920 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5588 . 0.1359 0.1318 . 300 0.0000 5888 . 'X-RAY DIFFRACTION' 
2.4200 3.0500  30 100.0000 5679 . 0.1461 0.1643 . 292 0.0000 5971 . 'X-RAY DIFFRACTION' 
3.0500 44.3700 30 100.0000 5786 . 0.1489 0.1684 . 281 0.0000 6067 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDV 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003644' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDV 
_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 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HDV A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDV 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 7HDV SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDV MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDV SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDV MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_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 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
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 LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HDV 
_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  ? ? 55.74 -132.85 
2 1 SER A 128 ? B 71.55 -9.85   
3 1 HIS B 86  ? ? 57.14 -127.57 
# 
_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 514 ? 5.93 . 
2 1 O ? A HOH 515 ? 6.03 . 
3 1 O ? A HOH 516 ? 7.64 . 
4 1 O ? B HOH 401 ? 6.48 . 
# 
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 
A1A84 N2   N  Y N 1   
A1A84 C3   C  N N 2   
A1A84 C6   C  Y N 3   
A1A84 C9   C  Y N 4   
A1A84 C1   C  N N 5   
A1A84 C10  C  Y N 6   
A1A84 C11  C  Y N 7   
A1A84 C2   C  N N 8   
A1A84 C4   C  N S 9   
A1A84 C5   C  N N 10  
A1A84 C7   C  Y N 11  
A1A84 C8   C  Y N 12  
A1A84 N1   N  N N 13  
A1A84 N3   N  Y N 14  
A1A84 N4   N  Y N 15  
A1A84 O1   O  N N 16  
A1A84 H4   H  N N 17  
A1A84 H3   H  N N 18  
A1A84 H2   H  N N 19  
A1A84 H10  H  N N 20  
A1A84 H11  H  N N 21  
A1A84 H1   H  N N 22  
A1A84 H5   H  N N 23  
A1A84 H6   H  N N 24  
A1A84 H9   H  N N 25  
A1A84 H8   H  N N 26  
A1A84 H12  H  N N 27  
A1A84 H7   H  N N 28  
ALA   N    N  N N 29  
ALA   CA   C  N S 30  
ALA   C    C  N N 31  
ALA   O    O  N N 32  
ALA   CB   C  N N 33  
ALA   OXT  O  N N 34  
ALA   H    H  N N 35  
ALA   H2   H  N N 36  
ALA   HA   H  N N 37  
ALA   HB1  H  N N 38  
ALA   HB2  H  N N 39  
ALA   HB3  H  N N 40  
ALA   HXT  H  N N 41  
ARG   N    N  N N 42  
ARG   CA   C  N S 43  
ARG   C    C  N N 44  
ARG   O    O  N N 45  
ARG   CB   C  N N 46  
ARG   CG   C  N N 47  
ARG   CD   C  N N 48  
ARG   NE   N  N N 49  
ARG   CZ   C  N N 50  
ARG   NH1  N  N N 51  
ARG   NH2  N  N N 52  
ARG   OXT  O  N N 53  
ARG   H    H  N N 54  
ARG   H2   H  N N 55  
ARG   HA   H  N N 56  
ARG   HB2  H  N N 57  
ARG   HB3  H  N N 58  
ARG   HG2  H  N N 59  
ARG   HG3  H  N N 60  
ARG   HD2  H  N N 61  
ARG   HD3  H  N N 62  
ARG   HE   H  N N 63  
ARG   HH11 H  N N 64  
ARG   HH12 H  N N 65  
ARG   HH21 H  N N 66  
ARG   HH22 H  N N 67  
ARG   HXT  H  N N 68  
ASN   N    N  N N 69  
ASN   CA   C  N S 70  
ASN   C    C  N N 71  
ASN   O    O  N N 72  
ASN   CB   C  N N 73  
ASN   CG   C  N N 74  
ASN   OD1  O  N N 75  
ASN   ND2  N  N N 76  
ASN   OXT  O  N N 77  
ASN   H    H  N N 78  
ASN   H2   H  N N 79  
ASN   HA   H  N N 80  
ASN   HB2  H  N N 81  
ASN   HB3  H  N N 82  
ASN   HD21 H  N N 83  
ASN   HD22 H  N N 84  
ASN   HXT  H  N N 85  
ASP   N    N  N N 86  
ASP   CA   C  N S 87  
ASP   C    C  N N 88  
ASP   O    O  N N 89  
ASP   CB   C  N N 90  
ASP   CG   C  N N 91  
ASP   OD1  O  N N 92  
ASP   OD2  O  N N 93  
ASP   OXT  O  N N 94  
ASP   H    H  N N 95  
ASP   H2   H  N N 96  
ASP   HA   H  N N 97  
ASP   HB2  H  N N 98  
ASP   HB3  H  N N 99  
ASP   HD2  H  N N 100 
ASP   HXT  H  N N 101 
CL    CL   CL N N 102 
CYS   N    N  N N 103 
CYS   CA   C  N R 104 
CYS   C    C  N N 105 
CYS   O    O  N N 106 
CYS   CB   C  N N 107 
CYS   SG   S  N N 108 
CYS   OXT  O  N N 109 
CYS   H    H  N N 110 
CYS   H2   H  N N 111 
CYS   HA   H  N N 112 
CYS   HB2  H  N N 113 
CYS   HB3  H  N N 114 
CYS   HG   H  N N 115 
CYS   HXT  H  N N 116 
GLN   N    N  N N 117 
GLN   CA   C  N S 118 
GLN   C    C  N N 119 
GLN   O    O  N N 120 
GLN   CB   C  N N 121 
GLN   CG   C  N N 122 
GLN   CD   C  N N 123 
GLN   OE1  O  N N 124 
GLN   NE2  N  N N 125 
GLN   OXT  O  N N 126 
GLN   H    H  N N 127 
GLN   H2   H  N N 128 
GLN   HA   H  N N 129 
GLN   HB2  H  N N 130 
GLN   HB3  H  N N 131 
GLN   HG2  H  N N 132 
GLN   HG3  H  N N 133 
GLN   HE21 H  N N 134 
GLN   HE22 H  N N 135 
GLN   HXT  H  N N 136 
GLU   N    N  N N 137 
GLU   CA   C  N S 138 
GLU   C    C  N N 139 
GLU   O    O  N N 140 
GLU   CB   C  N N 141 
GLU   CG   C  N N 142 
GLU   CD   C  N N 143 
GLU   OE1  O  N N 144 
GLU   OE2  O  N N 145 
GLU   OXT  O  N N 146 
GLU   H    H  N N 147 
GLU   H2   H  N N 148 
GLU   HA   H  N N 149 
GLU   HB2  H  N N 150 
GLU   HB3  H  N N 151 
GLU   HG2  H  N N 152 
GLU   HG3  H  N N 153 
GLU   HE2  H  N N 154 
GLU   HXT  H  N N 155 
GLY   N    N  N N 156 
GLY   CA   C  N N 157 
GLY   C    C  N N 158 
GLY   O    O  N N 159 
GLY   OXT  O  N N 160 
GLY   H    H  N N 161 
GLY   H2   H  N N 162 
GLY   HA2  H  N N 163 
GLY   HA3  H  N N 164 
GLY   HXT  H  N N 165 
HIS   N    N  N N 166 
HIS   CA   C  N S 167 
HIS   C    C  N N 168 
HIS   O    O  N N 169 
HIS   CB   C  N N 170 
HIS   CG   C  Y N 171 
HIS   ND1  N  Y N 172 
HIS   CD2  C  Y N 173 
HIS   CE1  C  Y N 174 
HIS   NE2  N  Y N 175 
HIS   OXT  O  N N 176 
HIS   H    H  N N 177 
HIS   H2   H  N N 178 
HIS   HA   H  N N 179 
HIS   HB2  H  N N 180 
HIS   HB3  H  N N 181 
HIS   HD1  H  N N 182 
HIS   HD2  H  N N 183 
HIS   HE1  H  N N 184 
HIS   HE2  H  N N 185 
HIS   HXT  H  N N 186 
HOH   O    O  N N 187 
HOH   H1   H  N N 188 
HOH   H2   H  N N 189 
ILE   N    N  N N 190 
ILE   CA   C  N S 191 
ILE   C    C  N N 192 
ILE   O    O  N N 193 
ILE   CB   C  N S 194 
ILE   CG1  C  N N 195 
ILE   CG2  C  N N 196 
ILE   CD1  C  N N 197 
ILE   OXT  O  N N 198 
ILE   H    H  N N 199 
ILE   H2   H  N N 200 
ILE   HA   H  N N 201 
ILE   HB   H  N N 202 
ILE   HG12 H  N N 203 
ILE   HG13 H  N N 204 
ILE   HG21 H  N N 205 
ILE   HG22 H  N N 206 
ILE   HG23 H  N N 207 
ILE   HD11 H  N N 208 
ILE   HD12 H  N N 209 
ILE   HD13 H  N N 210 
ILE   HXT  H  N N 211 
LEU   N    N  N N 212 
LEU   CA   C  N S 213 
LEU   C    C  N N 214 
LEU   O    O  N N 215 
LEU   CB   C  N N 216 
LEU   CG   C  N N 217 
LEU   CD1  C  N N 218 
LEU   CD2  C  N N 219 
LEU   OXT  O  N N 220 
LEU   H    H  N N 221 
LEU   H2   H  N N 222 
LEU   HA   H  N N 223 
LEU   HB2  H  N N 224 
LEU   HB3  H  N N 225 
LEU   HG   H  N N 226 
LEU   HD11 H  N N 227 
LEU   HD12 H  N N 228 
LEU   HD13 H  N N 229 
LEU   HD21 H  N N 230 
LEU   HD22 H  N N 231 
LEU   HD23 H  N N 232 
LEU   HXT  H  N N 233 
LYS   N    N  N N 234 
LYS   CA   C  N S 235 
LYS   C    C  N N 236 
LYS   O    O  N N 237 
LYS   CB   C  N N 238 
LYS   CG   C  N N 239 
LYS   CD   C  N N 240 
LYS   CE   C  N N 241 
LYS   NZ   N  N N 242 
LYS   OXT  O  N N 243 
LYS   H    H  N N 244 
LYS   H2   H  N N 245 
LYS   HA   H  N N 246 
LYS   HB2  H  N N 247 
LYS   HB3  H  N N 248 
LYS   HG2  H  N N 249 
LYS   HG3  H  N N 250 
LYS   HD2  H  N N 251 
LYS   HD3  H  N N 252 
LYS   HE2  H  N N 253 
LYS   HE3  H  N N 254 
LYS   HZ1  H  N N 255 
LYS   HZ2  H  N N 256 
LYS   HZ3  H  N N 257 
LYS   HXT  H  N N 258 
MET   N    N  N N 259 
MET   CA   C  N S 260 
MET   C    C  N N 261 
MET   O    O  N N 262 
MET   CB   C  N N 263 
MET   CG   C  N N 264 
MET   SD   S  N N 265 
MET   CE   C  N N 266 
MET   OXT  O  N N 267 
MET   H    H  N N 268 
MET   H2   H  N N 269 
MET   HA   H  N N 270 
MET   HB2  H  N N 271 
MET   HB3  H  N N 272 
MET   HG2  H  N N 273 
MET   HG3  H  N N 274 
MET   HE1  H  N N 275 
MET   HE2  H  N N 276 
MET   HE3  H  N N 277 
MET   HXT  H  N N 278 
PHE   N    N  N N 279 
PHE   CA   C  N S 280 
PHE   C    C  N N 281 
PHE   O    O  N N 282 
PHE   CB   C  N N 283 
PHE   CG   C  Y N 284 
PHE   CD1  C  Y N 285 
PHE   CD2  C  Y N 286 
PHE   CE1  C  Y N 287 
PHE   CE2  C  Y N 288 
PHE   CZ   C  Y N 289 
PHE   OXT  O  N N 290 
PHE   H    H  N N 291 
PHE   H2   H  N N 292 
PHE   HA   H  N N 293 
PHE   HB2  H  N N 294 
PHE   HB3  H  N N 295 
PHE   HD1  H  N N 296 
PHE   HD2  H  N N 297 
PHE   HE1  H  N N 298 
PHE   HE2  H  N N 299 
PHE   HZ   H  N N 300 
PHE   HXT  H  N N 301 
PRO   N    N  N N 302 
PRO   CA   C  N S 303 
PRO   C    C  N N 304 
PRO   O    O  N N 305 
PRO   CB   C  N N 306 
PRO   CG   C  N N 307 
PRO   CD   C  N N 308 
PRO   OXT  O  N N 309 
PRO   H    H  N N 310 
PRO   HA   H  N N 311 
PRO   HB2  H  N N 312 
PRO   HB3  H  N N 313 
PRO   HG2  H  N N 314 
PRO   HG3  H  N N 315 
PRO   HD2  H  N N 316 
PRO   HD3  H  N N 317 
PRO   HXT  H  N N 318 
SER   N    N  N N 319 
SER   CA   C  N S 320 
SER   C    C  N N 321 
SER   O    O  N N 322 
SER   CB   C  N N 323 
SER   OG   O  N N 324 
SER   OXT  O  N N 325 
SER   H    H  N N 326 
SER   H2   H  N N 327 
SER   HA   H  N N 328 
SER   HB2  H  N N 329 
SER   HB3  H  N N 330 
SER   HG   H  N N 331 
SER   HXT  H  N N 332 
TFA   C1   C  N N 333 
TFA   C2   C  N N 334 
TFA   O    O  N N 335 
TFA   F1   F  N N 336 
TFA   F2   F  N N 337 
TFA   F3   F  N N 338 
TFA   OXT  O  N N 339 
TFA   HXT  H  N N 340 
THR   N    N  N N 341 
THR   CA   C  N S 342 
THR   C    C  N N 343 
THR   O    O  N N 344 
THR   CB   C  N R 345 
THR   OG1  O  N N 346 
THR   CG2  C  N N 347 
THR   OXT  O  N N 348 
THR   H    H  N N 349 
THR   H2   H  N N 350 
THR   HA   H  N N 351 
THR   HB   H  N N 352 
THR   HG1  H  N N 353 
THR   HG21 H  N N 354 
THR   HG22 H  N N 355 
THR   HG23 H  N N 356 
THR   HXT  H  N N 357 
TYR   N    N  N N 358 
TYR   CA   C  N S 359 
TYR   C    C  N N 360 
TYR   O    O  N N 361 
TYR   CB   C  N N 362 
TYR   CG   C  Y N 363 
TYR   CD1  C  Y N 364 
TYR   CD2  C  Y N 365 
TYR   CE1  C  Y N 366 
TYR   CE2  C  Y N 367 
TYR   CZ   C  Y N 368 
TYR   OH   O  N N 369 
TYR   OXT  O  N N 370 
TYR   H    H  N N 371 
TYR   H2   H  N N 372 
TYR   HA   H  N N 373 
TYR   HB2  H  N N 374 
TYR   HB3  H  N N 375 
TYR   HD1  H  N N 376 
TYR   HD2  H  N N 377 
TYR   HE1  H  N N 378 
TYR   HE2  H  N N 379 
TYR   HH   H  N N 380 
TYR   HXT  H  N N 381 
VAL   N    N  N N 382 
VAL   CA   C  N S 383 
VAL   C    C  N N 384 
VAL   O    O  N N 385 
VAL   CB   C  N N 386 
VAL   CG1  C  N N 387 
VAL   CG2  C  N N 388 
VAL   OXT  O  N N 389 
VAL   H    H  N N 390 
VAL   H2   H  N N 391 
VAL   HA   H  N N 392 
VAL   HB   H  N N 393 
VAL   HG11 H  N N 394 
VAL   HG12 H  N N 395 
VAL   HG13 H  N N 396 
VAL   HG21 H  N N 397 
VAL   HG22 H  N N 398 
VAL   HG23 H  N N 399 
VAL   HXT  H  N N 400 
# 
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 
A1A84 O1  C5   sing N N 1   
A1A84 C3  C2   sing N N 2   
A1A84 C3  C4   sing N N 3   
A1A84 C2  C1   trip N N 4   
A1A84 C5  C4   sing N N 5   
A1A84 C4  N1   sing N N 6   
A1A84 N1  C6   sing N N 7   
A1A84 C6  N2   doub Y N 8   
A1A84 C6  C9   sing Y N 9   
A1A84 C10 C9   sing Y N 10  
A1A84 C10 C11  doub Y N 11  
A1A84 N2  C7   sing Y N 12  
A1A84 C9  C8   doub Y N 13  
A1A84 C11 N4   sing Y N 14  
A1A84 C7  N3   doub Y N 15  
A1A84 C8  N4   sing Y N 16  
A1A84 C8  N3   sing Y N 17  
A1A84 C3  H4   sing N N 18  
A1A84 C3  H3   sing N N 19  
A1A84 C1  H2   sing N N 20  
A1A84 C10 H10  sing N N 21  
A1A84 C11 H11  sing N N 22  
A1A84 C4  H1   sing N N 23  
A1A84 C5  H5   sing N N 24  
A1A84 C5  H6   sing N N 25  
A1A84 C7  H9   sing N N 26  
A1A84 N1  H8   sing N N 27  
A1A84 N4  H12  sing N N 28  
A1A84 O1  H7   sing N N 29  
ALA   N   CA   sing N N 30  
ALA   N   H    sing N N 31  
ALA   N   H2   sing N N 32  
ALA   CA  C    sing N N 33  
ALA   CA  CB   sing N N 34  
ALA   CA  HA   sing N N 35  
ALA   C   O    doub N N 36  
ALA   C   OXT  sing N N 37  
ALA   CB  HB1  sing N N 38  
ALA   CB  HB2  sing N N 39  
ALA   CB  HB3  sing N N 40  
ALA   OXT HXT  sing N N 41  
ARG   N   CA   sing N N 42  
ARG   N   H    sing N N 43  
ARG   N   H2   sing N N 44  
ARG   CA  C    sing N N 45  
ARG   CA  CB   sing N N 46  
ARG   CA  HA   sing N N 47  
ARG   C   O    doub N N 48  
ARG   C   OXT  sing N N 49  
ARG   CB  CG   sing N N 50  
ARG   CB  HB2  sing N N 51  
ARG   CB  HB3  sing N N 52  
ARG   CG  CD   sing N N 53  
ARG   CG  HG2  sing N N 54  
ARG   CG  HG3  sing N N 55  
ARG   CD  NE   sing N N 56  
ARG   CD  HD2  sing N N 57  
ARG   CD  HD3  sing N N 58  
ARG   NE  CZ   sing N N 59  
ARG   NE  HE   sing N N 60  
ARG   CZ  NH1  sing N N 61  
ARG   CZ  NH2  doub N N 62  
ARG   NH1 HH11 sing N N 63  
ARG   NH1 HH12 sing N N 64  
ARG   NH2 HH21 sing N N 65  
ARG   NH2 HH22 sing N N 66  
ARG   OXT HXT  sing N N 67  
ASN   N   CA   sing N N 68  
ASN   N   H    sing N N 69  
ASN   N   H2   sing N N 70  
ASN   CA  C    sing N N 71  
ASN   CA  CB   sing N N 72  
ASN   CA  HA   sing N N 73  
ASN   C   O    doub N N 74  
ASN   C   OXT  sing N N 75  
ASN   CB  CG   sing N N 76  
ASN   CB  HB2  sing N N 77  
ASN   CB  HB3  sing N N 78  
ASN   CG  OD1  doub N N 79  
ASN   CG  ND2  sing N N 80  
ASN   ND2 HD21 sing N N 81  
ASN   ND2 HD22 sing N N 82  
ASN   OXT HXT  sing N N 83  
ASP   N   CA   sing N N 84  
ASP   N   H    sing N N 85  
ASP   N   H2   sing N N 86  
ASP   CA  C    sing N N 87  
ASP   CA  CB   sing N N 88  
ASP   CA  HA   sing N N 89  
ASP   C   O    doub N N 90  
ASP   C   OXT  sing N N 91  
ASP   CB  CG   sing N N 92  
ASP   CB  HB2  sing N N 93  
ASP   CB  HB3  sing N N 94  
ASP   CG  OD1  doub N N 95  
ASP   CG  OD2  sing N N 96  
ASP   OD2 HD2  sing N N 97  
ASP   OXT HXT  sing N N 98  
CYS   N   CA   sing N N 99  
CYS   N   H    sing N N 100 
CYS   N   H2   sing N N 101 
CYS   CA  C    sing N N 102 
CYS   CA  CB   sing N N 103 
CYS   CA  HA   sing N N 104 
CYS   C   O    doub N N 105 
CYS   C   OXT  sing N N 106 
CYS   CB  SG   sing N N 107 
CYS   CB  HB2  sing N N 108 
CYS   CB  HB3  sing N N 109 
CYS   SG  HG   sing N N 110 
CYS   OXT HXT  sing N N 111 
GLN   N   CA   sing N N 112 
GLN   N   H    sing N N 113 
GLN   N   H2   sing N N 114 
GLN   CA  C    sing N N 115 
GLN   CA  CB   sing N N 116 
GLN   CA  HA   sing N N 117 
GLN   C   O    doub N N 118 
GLN   C   OXT  sing N N 119 
GLN   CB  CG   sing N N 120 
GLN   CB  HB2  sing N N 121 
GLN   CB  HB3  sing N N 122 
GLN   CG  CD   sing N N 123 
GLN   CG  HG2  sing N N 124 
GLN   CG  HG3  sing N N 125 
GLN   CD  OE1  doub N N 126 
GLN   CD  NE2  sing N N 127 
GLN   NE2 HE21 sing N N 128 
GLN   NE2 HE22 sing N N 129 
GLN   OXT HXT  sing N N 130 
GLU   N   CA   sing N N 131 
GLU   N   H    sing N N 132 
GLU   N   H2   sing N N 133 
GLU   CA  C    sing N N 134 
GLU   CA  CB   sing N N 135 
GLU   CA  HA   sing N N 136 
GLU   C   O    doub N N 137 
GLU   C   OXT  sing N N 138 
GLU   CB  CG   sing N N 139 
GLU   CB  HB2  sing N N 140 
GLU   CB  HB3  sing N N 141 
GLU   CG  CD   sing N N 142 
GLU   CG  HG2  sing N N 143 
GLU   CG  HG3  sing N N 144 
GLU   CD  OE1  doub N N 145 
GLU   CD  OE2  sing N N 146 
GLU   OE2 HE2  sing N N 147 
GLU   OXT HXT  sing N N 148 
GLY   N   CA   sing N N 149 
GLY   N   H    sing N N 150 
GLY   N   H2   sing N N 151 
GLY   CA  C    sing N N 152 
GLY   CA  HA2  sing N N 153 
GLY   CA  HA3  sing N N 154 
GLY   C   O    doub N N 155 
GLY   C   OXT  sing N N 156 
GLY   OXT HXT  sing N N 157 
HIS   N   CA   sing N N 158 
HIS   N   H    sing N N 159 
HIS   N   H2   sing N N 160 
HIS   CA  C    sing N N 161 
HIS   CA  CB   sing N N 162 
HIS   CA  HA   sing N N 163 
HIS   C   O    doub N N 164 
HIS   C   OXT  sing N N 165 
HIS   CB  CG   sing N N 166 
HIS   CB  HB2  sing N N 167 
HIS   CB  HB3  sing N N 168 
HIS   CG  ND1  sing Y N 169 
HIS   CG  CD2  doub Y N 170 
HIS   ND1 CE1  doub Y N 171 
HIS   ND1 HD1  sing N N 172 
HIS   CD2 NE2  sing Y N 173 
HIS   CD2 HD2  sing N N 174 
HIS   CE1 NE2  sing Y N 175 
HIS   CE1 HE1  sing N N 176 
HIS   NE2 HE2  sing N N 177 
HIS   OXT HXT  sing N N 178 
HOH   O   H1   sing N N 179 
HOH   O   H2   sing N N 180 
ILE   N   CA   sing N N 181 
ILE   N   H    sing N N 182 
ILE   N   H2   sing N N 183 
ILE   CA  C    sing N N 184 
ILE   CA  CB   sing N N 185 
ILE   CA  HA   sing N N 186 
ILE   C   O    doub N N 187 
ILE   C   OXT  sing N N 188 
ILE   CB  CG1  sing N N 189 
ILE   CB  CG2  sing N N 190 
ILE   CB  HB   sing N N 191 
ILE   CG1 CD1  sing N N 192 
ILE   CG1 HG12 sing N N 193 
ILE   CG1 HG13 sing N N 194 
ILE   CG2 HG21 sing N N 195 
ILE   CG2 HG22 sing N N 196 
ILE   CG2 HG23 sing N N 197 
ILE   CD1 HD11 sing N N 198 
ILE   CD1 HD12 sing N N 199 
ILE   CD1 HD13 sing N N 200 
ILE   OXT HXT  sing N N 201 
LEU   N   CA   sing N N 202 
LEU   N   H    sing N N 203 
LEU   N   H2   sing N N 204 
LEU   CA  C    sing N N 205 
LEU   CA  CB   sing N N 206 
LEU   CA  HA   sing N N 207 
LEU   C   O    doub N N 208 
LEU   C   OXT  sing N N 209 
LEU   CB  CG   sing N N 210 
LEU   CB  HB2  sing N N 211 
LEU   CB  HB3  sing N N 212 
LEU   CG  CD1  sing N N 213 
LEU   CG  CD2  sing N N 214 
LEU   CG  HG   sing N N 215 
LEU   CD1 HD11 sing N N 216 
LEU   CD1 HD12 sing N N 217 
LEU   CD1 HD13 sing N N 218 
LEU   CD2 HD21 sing N N 219 
LEU   CD2 HD22 sing N N 220 
LEU   CD2 HD23 sing N N 221 
LEU   OXT HXT  sing N N 222 
LYS   N   CA   sing N N 223 
LYS   N   H    sing N N 224 
LYS   N   H2   sing N N 225 
LYS   CA  C    sing N N 226 
LYS   CA  CB   sing N N 227 
LYS   CA  HA   sing N N 228 
LYS   C   O    doub N N 229 
LYS   C   OXT  sing N N 230 
LYS   CB  CG   sing N N 231 
LYS   CB  HB2  sing N N 232 
LYS   CB  HB3  sing N N 233 
LYS   CG  CD   sing N N 234 
LYS   CG  HG2  sing N N 235 
LYS   CG  HG3  sing N N 236 
LYS   CD  CE   sing N N 237 
LYS   CD  HD2  sing N N 238 
LYS   CD  HD3  sing N N 239 
LYS   CE  NZ   sing N N 240 
LYS   CE  HE2  sing N N 241 
LYS   CE  HE3  sing N N 242 
LYS   NZ  HZ1  sing N N 243 
LYS   NZ  HZ2  sing N N 244 
LYS   NZ  HZ3  sing N N 245 
LYS   OXT HXT  sing N N 246 
MET   N   CA   sing N N 247 
MET   N   H    sing N N 248 
MET   N   H2   sing N N 249 
MET   CA  C    sing N N 250 
MET   CA  CB   sing N N 251 
MET   CA  HA   sing N N 252 
MET   C   O    doub N N 253 
MET   C   OXT  sing N N 254 
MET   CB  CG   sing N N 255 
MET   CB  HB2  sing N N 256 
MET   CB  HB3  sing N N 257 
MET   CG  SD   sing N N 258 
MET   CG  HG2  sing N N 259 
MET   CG  HG3  sing N N 260 
MET   SD  CE   sing N N 261 
MET   CE  HE1  sing N N 262 
MET   CE  HE2  sing N N 263 
MET   CE  HE3  sing N N 264 
MET   OXT HXT  sing N N 265 
PHE   N   CA   sing N N 266 
PHE   N   H    sing N N 267 
PHE   N   H2   sing N N 268 
PHE   CA  C    sing N N 269 
PHE   CA  CB   sing N N 270 
PHE   CA  HA   sing N N 271 
PHE   C   O    doub N N 272 
PHE   C   OXT  sing N N 273 
PHE   CB  CG   sing N N 274 
PHE   CB  HB2  sing N N 275 
PHE   CB  HB3  sing N N 276 
PHE   CG  CD1  doub Y N 277 
PHE   CG  CD2  sing Y N 278 
PHE   CD1 CE1  sing Y N 279 
PHE   CD1 HD1  sing N N 280 
PHE   CD2 CE2  doub Y N 281 
PHE   CD2 HD2  sing N N 282 
PHE   CE1 CZ   doub Y N 283 
PHE   CE1 HE1  sing N N 284 
PHE   CE2 CZ   sing Y N 285 
PHE   CE2 HE2  sing N N 286 
PHE   CZ  HZ   sing N N 287 
PHE   OXT HXT  sing N N 288 
PRO   N   CA   sing N N 289 
PRO   N   CD   sing N N 290 
PRO   N   H    sing N N 291 
PRO   CA  C    sing N N 292 
PRO   CA  CB   sing N N 293 
PRO   CA  HA   sing N N 294 
PRO   C   O    doub N N 295 
PRO   C   OXT  sing N N 296 
PRO   CB  CG   sing N N 297 
PRO   CB  HB2  sing N N 298 
PRO   CB  HB3  sing N N 299 
PRO   CG  CD   sing N N 300 
PRO   CG  HG2  sing N N 301 
PRO   CG  HG3  sing N N 302 
PRO   CD  HD2  sing N N 303 
PRO   CD  HD3  sing N N 304 
PRO   OXT HXT  sing N N 305 
SER   N   CA   sing N N 306 
SER   N   H    sing N N 307 
SER   N   H2   sing N N 308 
SER   CA  C    sing N N 309 
SER   CA  CB   sing N N 310 
SER   CA  HA   sing N N 311 
SER   C   O    doub N N 312 
SER   C   OXT  sing N N 313 
SER   CB  OG   sing N N 314 
SER   CB  HB2  sing N N 315 
SER   CB  HB3  sing N N 316 
SER   OG  HG   sing N N 317 
SER   OXT HXT  sing N N 318 
TFA   C1  C2   sing N N 319 
TFA   C1  O    doub N N 320 
TFA   C1  OXT  sing N N 321 
TFA   C2  F1   sing N N 322 
TFA   C2  F2   sing N N 323 
TFA   C2  F3   sing N N 324 
TFA   OXT HXT  sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_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                    7HDV 
_atom_sites.fract_transf_matrix[1][1]   0.011269 
_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]   0.011269 
_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]   0.025365 
_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 
F  
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   ? 19.558 -16.115 22.265  1.00 59.06 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.610 -15.020 22.434  1.00 58.50 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.277 -13.689 22.100  1.00 55.93 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.408 -13.433 22.514  1.00 56.74 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 18.009 -15.014 23.858  1.00 59.93 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 16.978 -13.902 24.002  1.00 60.29 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.386 -16.366 24.178  1.00 60.37 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.879 -15.144 21.816  1.00 70.21 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.713 -14.851 24.504  1.00 71.92 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.500 -14.019 24.839  1.00 72.35 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.432 -13.045 23.999  1.00 72.35 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.356 -13.951 23.259  1.00 72.35 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.938 -16.314 25.037  1.00 72.45 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.745 -16.589 23.484  1.00 72.45 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.085 -17.037 24.210  1.00 72.45 ?  3   VAL   A HG23 1 
ATOM   16   N  N    . ASN   A 1 4   ? 18.577 -12.851 21.335  1.00 51.88 ?  4   ASN   A N    1 
ATOM   17   C  CA   . ASN   A 1 4   ? 19.032 -11.501 21.021  1.00 47.34 ?  4   ASN   A CA   1 
ATOM   18   C  C    . ASN   A 1 4   ? 17.904 -10.510 21.301  1.00 42.64 ?  4   ASN   A C    1 
ATOM   19   O  O    . ASN   A 1 4   ? 16.802 -10.889 21.710  1.00 42.73 ?  4   ASN   A O    1 
ATOM   20   C  CB   . ASN   A 1 4   ? 19.576 -11.396 19.589  1.00 46.93 ?  4   ASN   A CB   1 
ATOM   21   C  CG   . ASN   A 1 4   ? 18.558 -11.790 18.543  1.00 46.28 ?  4   ASN   A CG   1 
ATOM   22   O  OD1  . ASN   A 1 4   ? 17.436 -11.283 18.526  1.00 46.13 ?  4   ASN   A OD1  1 
ATOM   23   N  ND2  . ASN   A 1 4   ? 18.946 -12.704 17.658  1.00 46.15 ?  4   ASN   A ND2  1 
ATOM   24   H  H    . ASN   A 1 4   ? 17.819 -13.052 20.979  1.00 62.26 ?  4   ASN   A H    1 
ATOM   25   H  HA   . ASN   A 1 4   ? 19.762 -11.284 21.614  1.00 56.81 ?  4   ASN   A HA   1 
ATOM   26   H  HB2  . ASN   A 1 4   ? 19.843 -10.478 19.419  1.00 56.33 ?  4   ASN   A HB2  1 
ATOM   27   H  HB3  . ASN   A 1 4   ? 20.342 -11.984 19.499  1.00 56.33 ?  4   ASN   A HB3  1 
ATOM   28   H  HD21 . ASN   A 1 4   ? 18.407 -12.961 17.040  1.00 55.39 ?  4   ASN   A HD21 1 
ATOM   29   H  HD22 . ASN   A 1 4   ? 19.738 -13.038 17.704  1.00 55.39 ?  4   ASN   A HD22 1 
ATOM   30   N  N    A SER   A 1 5   ? 18.176 -9.227  21.066  0.64 39.95 ?  5   SER   A N    1 
ATOM   31   N  N    B SER   A 1 5   ? 18.196 -9.228  21.082  0.36 40.18 ?  5   SER   A N    1 
ATOM   32   C  CA   A SER   A 1 5   ? 17.260 -8.155  21.437  0.64 37.05 ?  5   SER   A CA   1 
ATOM   33   C  CA   B SER   A 1 5   ? 17.292 -8.141  21.430  0.36 37.53 ?  5   SER   A CA   1 
ATOM   34   C  C    A SER   A 1 5   ? 16.399 -7.665  20.276  0.64 33.48 ?  5   SER   A C    1 
ATOM   35   C  C    B SER   A 1 5   ? 16.438 -7.667  20.260  0.36 34.26 ?  5   SER   A C    1 
ATOM   36   O  O    A SER   A 1 5   ? 15.770 -6.608  20.392  0.64 33.70 ?  5   SER   A O    1 
ATOM   37   O  O    B SER   A 1 5   ? 15.685 -6.701  20.415  0.36 34.41 ?  5   SER   A O    1 
ATOM   38   C  CB   A SER   A 1 5   ? 18.030 -6.981  22.043  0.64 37.92 ?  5   SER   A CB   1 
ATOM   39   C  CB   B SER   A 1 5   ? 18.079 -6.960  22.011  0.36 38.21 ?  5   SER   A CB   1 
ATOM   40   O  OG   A SER   A 1 5   ? 19.003 -6.489  21.139  0.64 38.32 ?  5   SER   A OG   1 
ATOM   41   O  OG   B SER   A 1 5   ? 18.973 -6.418  21.055  0.36 38.50 ?  5   SER   A OG   1 
ATOM   42   H  H    A SER   A 1 5   ? 18.893 -8.953  20.680  0.64 47.94 ?  5   SER   A H    1 
ATOM   43   H  H    B SER   A 1 5   ? 18.930 -8.963  20.722  0.36 48.23 ?  5   SER   A H    1 
ATOM   44   H  HA   A SER   A 1 5   ? 16.668 -8.490  22.128  0.64 44.47 ?  5   SER   A HA   1 
ATOM   45   H  HA   B SER   A 1 5   ? 16.690 -8.452  22.121  0.36 45.04 ?  5   SER   A HA   1 
ATOM   46   H  HB2  A SER   A 1 5   ? 17.404 -6.266  22.248  0.64 45.51 ?  5   SER   A HB2  1 
ATOM   47   H  HB2  B SER   A 1 5   ? 17.454 -6.269  22.285  0.36 45.86 ?  5   SER   A HB2  1 
ATOM   48   H  HB3  A SER   A 1 5   ? 18.469 -7.277  22.856  0.64 45.51 ?  5   SER   A HB3  1 
ATOM   49   H  HB3  B SER   A 1 5   ? 18.587 -7.267  22.780  0.36 45.86 ?  5   SER   A HB3  1 
ATOM   50   H  HG   A SER   A 1 5   ? 19.420 -5.848  21.489  0.64 45.99 ?  5   SER   A HG   1 
ATOM   51   H  HG   B SER   A 1 5   ? 19.395 -5.773  21.391  0.36 46.21 ?  5   SER   A HG   1 
ATOM   52   N  N    A PHE   A 1 6   ? 16.357 -8.392  19.163  0.64 29.18 ?  6   PHE   A N    1 
ATOM   53   N  N    B PHE   A 1 6   ? 16.539 -8.309  19.099  0.36 30.57 ?  6   PHE   A N    1 
ATOM   54   C  CA   A PHE   A 1 6   ? 15.456 -8.026  18.079  0.64 25.16 ?  6   PHE   A CA   1 
ATOM   55   C  CA   B PHE   A 1 6   ? 15.624 -8.008  18.005  0.36 26.91 ?  6   PHE   A CA   1 
ATOM   56   C  C    A PHE   A 1 6   ? 14.023 -8.384  18.459  0.64 24.34 ?  6   PHE   A C    1 
ATOM   57   C  C    B PHE   A 1 6   ? 14.210 -8.395  18.415  0.36 25.79 ?  6   PHE   A C    1 
ATOM   58   O  O    A PHE   A 1 6   ? 13.773 -9.424  19.071  0.64 25.35 ?  6   PHE   A O    1 
ATOM   59   O  O    B PHE   A 1 6   ? 13.925 -9.573  18.649  0.36 25.46 ?  6   PHE   A O    1 
ATOM   60   C  CB   A PHE   A 1 6   ? 15.863 -8.735  16.790  0.64 22.65 ?  6   PHE   A CB   1 
ATOM   61   C  CB   B PHE   A 1 6   ? 16.037 -8.785  16.757  0.36 24.85 ?  6   PHE   A CB   1 
ATOM   62   C  CG   A PHE   A 1 6   ? 17.140 -8.206  16.189  0.64 20.64 ?  6   PHE   A CG   1 
ATOM   63   C  CG   B PHE   A 1 6   ? 17.313 -8.297  16.128  0.36 23.10 ?  6   PHE   A CG   1 
ATOM   64   C  CD1  A PHE   A 1 6   ? 17.137 -7.039  15.444  0.64 19.92 ?  6   PHE   A CD1  1 
ATOM   65   C  CD1  B PHE   A 1 6   ? 17.347 -7.093  15.447  0.36 22.29 ?  6   PHE   A CD1  1 
ATOM   66   C  CD2  A PHE   A 1 6   ? 18.335 -8.877  16.370  0.64 20.98 ?  6   PHE   A CD2  1 
ATOM   67   C  CD2  B PHE   A 1 6   ? 18.473 -9.051  16.204  0.36 22.74 ?  6   PHE   A CD2  1 
ATOM   68   C  CE1  A PHE   A 1 6   ? 18.306 -6.548  14.890  0.64 19.59 ?  6   PHE   A CE1  1 
ATOM   69   C  CE1  B PHE   A 1 6   ? 18.516 -6.642  14.862  0.36 21.99 ?  6   PHE   A CE1  1 
ATOM   70   C  CE2  A PHE   A 1 6   ? 19.503 -8.395  15.818  0.64 20.91 ?  6   PHE   A CE2  1 
ATOM   71   C  CE2  B PHE   A 1 6   ? 19.645 -8.606  15.620  0.36 22.46 ?  6   PHE   A CE2  1 
ATOM   72   C  CZ   A PHE   A 1 6   ? 19.488 -7.226  15.078  0.64 20.18 ?  6   PHE   A CZ   1 
ATOM   73   C  CZ   B PHE   A 1 6   ? 19.666 -7.399  14.949  0.36 22.13 ?  6   PHE   A CZ   1 
ATOM   74   H  H    A PHE   A 1 6   ? 16.834 -9.093  19.015  0.64 35.03 ?  6   PHE   A H    1 
ATOM   75   H  H    B PHE   A 1 6   ? 17.124 -8.913  18.921  0.36 36.69 ?  6   PHE   A H    1 
ATOM   76   H  HA   A PHE   A 1 6   ? 15.493 -7.076  17.935  0.64 30.20 ?  6   PHE   A HA   1 
ATOM   77   H  HA   B PHE   A 1 6   ? 15.646 -7.059  17.808  0.36 32.30 ?  6   PHE   A HA   1 
ATOM   78   H  HB2  A PHE   A 1 6   ? 15.990 -9.681  16.977  0.64 27.19 ?  6   PHE   A HB2  1 
ATOM   79   H  HB2  B PHE   A 1 6   ? 16.160 -9.717  16.997  0.36 29.83 ?  6   PHE   A HB2  1 
ATOM   80   H  HB3  A PHE   A 1 6   ? 15.156 -8.626  16.135  0.64 27.19 ?  6   PHE   A HB3  1 
ATOM   81   H  HB3  B PHE   A 1 6   ? 15.332 -8.707  16.096  0.36 29.83 ?  6   PHE   A HB3  1 
ATOM   82   H  HD1  A PHE   A 1 6   ? 16.335 -6.582  15.317  0.64 23.91 ?  6   PHE   A HD1  1 
ATOM   83   H  HD1  B PHE   A 1 6   ? 16.575 -6.579  15.387  0.36 26.75 ?  6   PHE   A HD1  1 
ATOM   84   H  HD2  A PHE   A 1 6   ? 18.350 -9.664  16.870  0.64 25.19 ?  6   PHE   A HD2  1 
ATOM   85   H  HD2  B PHE   A 1 6   ? 18.464 -9.864  16.656  0.36 27.29 ?  6   PHE   A HD2  1 
ATOM   86   H  HE1  A PHE   A 1 6   ? 18.286 -5.764  14.392  0.64 23.52 ?  6   PHE   A HE1  1 
ATOM   87   H  HE1  B PHE   A 1 6   ? 18.528 -5.830  14.409  0.36 26.39 ?  6   PHE   A HE1  1 
ATOM   88   H  HE2  A PHE   A 1 6   ? 20.303 -8.851  15.947  0.64 25.10 ?  6   PHE   A HE2  1 
ATOM   89   H  HE2  B PHE   A 1 6   ? 20.420 -9.118  15.680  0.36 26.96 ?  6   PHE   A HE2  1 
ATOM   90   H  HZ   A PHE   A 1 6   ? 20.272 -6.898  14.707  0.64 24.22 ?  6   PHE   A HZ   1 
ATOM   91   H  HZ   B PHE   A 1 6   ? 20.453 -7.098  14.555  0.36 26.57 ?  6   PHE   A HZ   1 
ATOM   92   N  N    A SER   A 1 7   ? 13.080 -7.509  18.107  0.64 22.39 ?  7   SER   A N    1 
ATOM   93   N  N    B SER   A 1 7   ? 13.324 -7.406  18.500  0.36 25.11 ?  7   SER   A N    1 
ATOM   94   C  CA   A SER   A 1 7   ? 11.704 -7.619  18.577  0.64 21.83 ?  7   SER   A CA   1 
ATOM   95   C  CA   B SER   A 1 7   ? 11.981 -7.602  19.025  0.36 24.81 ?  7   SER   A CA   1 
ATOM   96   C  C    A SER   A 1 7   ? 10.718 -7.388  17.439  0.64 19.10 ?  7   SER   A C    1 
ATOM   97   C  C    B SER   A 1 7   ? 10.949 -7.243  17.965  0.36 23.16 ?  7   SER   A C    1 
ATOM   98   O  O    A SER   A 1 7   ? 10.918 -6.508  16.599  0.64 18.94 ?  7   SER   A O    1 
ATOM   99   O  O    B SER   A 1 7   ? 11.137 -6.297  17.194  0.36 23.24 ?  7   SER   A O    1 
ATOM   100  C  CB   A SER   A 1 7   ? 11.441 -6.586  19.682  0.64 23.57 ?  7   SER   A CB   1 
ATOM   101  C  CB   B SER   A 1 7   ? 11.764 -6.743  20.276  0.36 25.81 ?  7   SER   A CB   1 
ATOM   102  O  OG   A SER   A 1 7   ? 10.096 -6.628  20.119  0.64 24.78 ?  7   SER   A OG   1 
ATOM   103  O  OG   B SER   A 1 7   ? 10.573 -7.111  20.948  0.36 26.63 ?  7   SER   A OG   1 
ATOM   104  H  H    A SER   A 1 7   ? 13.220 -6.837  17.596  0.64 26.88 ?  7   SER   A H    1 
ATOM   105  H  H    B SER   A 1 7   ? 13.482 -6.596  18.250  0.36 30.15 ?  7   SER   A H    1 
ATOM   106  H  HA   A SER   A 1 7   ? 11.551 -8.505  18.940  0.64 26.21 ?  7   SER   A HA   1 
ATOM   107  H  HA   B SER   A 1 7   ? 11.859 -8.532  19.268  0.36 29.78 ?  7   SER   A HA   1 
ATOM   108  H  HB2  A SER   A 1 7   ? 12.032 -6.774  20.429  0.64 28.30 ?  7   SER   A HB2  1 
ATOM   109  H  HB2  B SER   A 1 7   ? 12.519 -6.863  20.876  0.36 30.99 ?  7   SER   A HB2  1 
ATOM   110  H  HB3  A SER   A 1 7   ? 11.623 -5.701  19.332  0.64 28.30 ?  7   SER   A HB3  1 
ATOM   111  H  HB3  B SER   A 1 7   ? 11.698 -5.812  20.013  0.36 30.99 ?  7   SER   A HB3  1 
ATOM   112  H  HG   A SER   A 1 7   ? 9.978  -6.069  20.735  0.64 29.74 ?  7   SER   A HG   1 
ATOM   113  H  HG   B SER   A 1 7   ? 10.473 -6.638  21.635  0.36 31.96 ?  7   SER   A HG   1 
ATOM   114  N  N    A GLY   A 1 8   ? 9.643  -8.179  17.429  0.64 17.51 ?  8   GLY   A N    1 
ATOM   115  N  N    B GLY   A 1 8   ? 9.860  -8.011  17.928  0.36 21.64 ?  8   GLY   A N    1 
ATOM   116  C  CA   A GLY   A 1 8   ? 8.550  -7.964  16.498  0.64 16.52 ?  8   GLY   A CA   1 
ATOM   117  C  CA   B GLY   A 1 8   ? 8.760  -7.730  17.030  0.36 20.20 ?  8   GLY   A CA   1 
ATOM   118  C  C    A GLY   A 1 8   ? 8.774  -8.458  15.088  0.64 15.00 ?  8   GLY   A C    1 
ATOM   119  C  C    B GLY   A 1 8   ? 8.915  -8.254  15.621  0.36 18.57 ?  8   GLY   A C    1 
ATOM   120  O  O    A GLY   A 1 8   ? 8.057  -8.030  14.175  0.64 15.62 ?  8   GLY   A O    1 
ATOM   121  O  O    B GLY   A 1 8   ? 8.093  -7.916  14.762  0.36 18.64 ?  8   GLY   A O    1 
ATOM   122  H  H    A GLY   A 1 8   ? 9.524  -8.847  17.960  0.64 21.03 ?  8   GLY   A H    1 
ATOM   123  H  H    B GLY   A 1 8   ? 9.740  -8.706  18.422  0.36 25.98 ?  8   GLY   A H    1 
ATOM   124  H  HA2  A GLY   A 1 8   ? 7.755  -8.399  16.848  0.64 19.84 ?  8   GLY   A HA2  1 
ATOM   125  H  HA2  B GLY   A 1 8   ? 7.951  -8.114  17.397  0.36 24.25 ?  8   GLY   A HA2  1 
ATOM   126  H  HA3  A GLY   A 1 8   ? 8.369  -7.015  16.446  0.64 19.84 ?  8   GLY   A HA3  1 
ATOM   127  H  HA3  B GLY   A 1 8   ? 8.639  -6.769  16.977  0.36 24.25 ?  8   GLY   A HA3  1 
ATOM   128  N  N    A TYR   A 1 9   ? 9.738  -9.353  14.876  0.64 13.97 ?  9   TYR   A N    1 
ATOM   129  N  N    B TYR   A 1 9   ? 9.933  -9.065  15.351  0.36 16.96 ?  9   TYR   A N    1 
ATOM   130  C  CA   A TYR   A 1 9   ? 10.027 -9.885  13.552  0.64 12.94 ?  9   TYR   A CA   1 
ATOM   131  C  CA   B TYR   A 1 9   ? 10.140 -9.586  14.009  0.36 15.54 ?  9   TYR   A CA   1 
ATOM   132  C  C    A TYR   A 1 9   ? 9.189  -11.123 13.270  0.64 12.01 ?  9   TYR   A C    1 
ATOM   133  C  C    B TYR   A 1 9   ? 9.254  -10.801 13.749  0.36 14.44 ?  9   TYR   A C    1 
ATOM   134  O  O    A TYR   A 1 9   ? 8.955  -11.953 14.152  0.64 12.93 ?  9   TYR   A O    1 
ATOM   135  O  O    B TYR   A 1 9   ? 8.943  -11.581 14.654  0.36 15.17 ?  9   TYR   A O    1 
ATOM   136  C  CB   A TYR   A 1 9   ? 11.508 -10.256 13.415  0.64 13.53 ?  9   TYR   A CB   1 
ATOM   137  C  CB   B TYR   A 1 9   ? 11.609 -9.965  13.801  0.36 15.85 ?  9   TYR   A CB   1 
ATOM   138  C  CG   A TYR   A 1 9   ? 12.417 -9.061  13.257  0.64 14.39 ?  9   TYR   A CG   1 
ATOM   139  C  CG   B TYR   A 1 9   ? 12.516 -8.772  13.582  0.36 15.82 ?  9   TYR   A CG   1 
ATOM   140  C  CD1  A TYR   A 1 9   ? 12.742 -8.273  14.349  0.64 15.33 ?  9   TYR   A CD1  1 
ATOM   141  C  CD1  B TYR   A 1 9   ? 12.861 -7.939  14.635  0.36 16.31 ?  9   TYR   A CD1  1 
ATOM   142  C  CD2  A TYR   A 1 9   ? 12.929 -8.711  12.014  0.64 14.71 ?  9   TYR   A CD2  1 
ATOM   143  C  CD2  B TYR   A 1 9   ? 13.018 -8.478  12.320  0.36 15.59 ?  9   TYR   A CD2  1 
ATOM   144  C  CE1  A TYR   A 1 9   ? 13.554 -7.169  14.213  0.64 16.16 ?  9   TYR   A CE1  1 
ATOM   145  C  CE1  B TYR   A 1 9   ? 13.680 -6.844  14.441  0.36 16.60 ?  9   TYR   A CE1  1 
ATOM   146  C  CE2  A TYR   A 1 9   ? 13.741 -7.610  11.867  0.64 15.18 ?  9   TYR   A CE2  1 
ATOM   147  C  CE2  B TYR   A 1 9   ? 13.835 -7.383  12.114  0.36 15.78 ?  9   TYR   A CE2  1 
ATOM   148  C  CZ   A TYR   A 1 9   ? 14.047 -6.841  12.968  0.64 16.19 ?  9   TYR   A CZ   1 
ATOM   149  C  CZ   B TYR   A 1 9   ? 14.163 -6.571  13.178  0.36 16.68 ?  9   TYR   A CZ   1 
ATOM   150  O  OH   A TYR   A 1 9   ? 14.853 -5.743  12.815  0.64 17.51 ?  9   TYR   A OH   1 
ATOM   151  O  OH   B TYR   A 1 9   ? 14.977 -5.481  12.981  0.36 17.95 ?  9   TYR   A OH   1 
ATOM   152  H  H    A TYR   A 1 9   ? 10.233 -9.682  15.494  0.64 16.78 ?  9   TYR   A H    1 
ATOM   153  H  H    B TYR   A 1 9   ? 10.521 -9.324  15.927  0.36 20.36 ?  9   TYR   A H    1 
ATOM   154  H  HA   A TYR   A 1 9   ? 9.813  -9.222  12.881  0.64 15.53 ?  9   TYR   A HA   1 
ATOM   155  H  HA   B TYR   A 1 9   ? 9.917  -8.896  13.364  0.36 18.66 ?  9   TYR   A HA   1 
ATOM   156  H  HB2  A TYR   A 1 9   ? 11.785 -10.746 14.205  0.64 16.25 ?  9   TYR   A HB2  1 
ATOM   157  H  HB2  B TYR   A 1 9   ? 11.930 -10.448 14.580  0.36 19.03 ?  9   TYR   A HB2  1 
ATOM   158  H  HB3  A TYR   A 1 9   ? 11.609 -10.815 12.629  0.64 16.25 ?  9   TYR   A HB3  1 
ATOM   159  H  HB3  B TYR   A 1 9   ? 11.671 -10.531 13.016  0.36 19.03 ?  9   TYR   A HB3  1 
ATOM   160  H  HD1  A TYR   A 1 9   ? 12.397 -8.491  15.189  0.64 18.40 ?  9   TYR   A HD1  1 
ATOM   161  H  HD1  B TYR   A 1 9   ? 12.536 -8.122  15.488  0.36 19.58 ?  9   TYR   A HD1  1 
ATOM   162  H  HD2  A TYR   A 1 9   ? 12.713 -9.231  11.271  0.64 17.66 ?  9   TYR   A HD2  1 
ATOM   163  H  HD2  B TYR   A 1 9   ? 12.795 -9.025  11.601  0.36 18.71 ?  9   TYR   A HD2  1 
ATOM   164  H  HE1  A TYR   A 1 9   ? 13.765 -6.648  14.953  0.64 19.40 ?  9   TYR   A HE1  1 
ATOM   165  H  HE1  B TYR   A 1 9   ? 13.905 -6.294  15.156  0.36 19.92 ?  9   TYR   A HE1  1 
ATOM   166  H  HE2  A TYR   A 1 9   ? 14.081 -7.391  11.029  0.64 18.23 ?  9   TYR   A HE2  1 
ATOM   167  H  HE2  B TYR   A 1 9   ? 14.166 -7.197  11.264  0.36 18.95 ?  9   TYR   A HE2  1 
ATOM   168  H  HH   A TYR   A 1 9   ? 14.985 -5.374  13.559  0.64 21.02 ?  9   TYR   A HH   1 
ATOM   169  H  HH   B TYR   A 1 9   ? 15.097 -5.077  13.708  0.36 21.55 ?  9   TYR   A HH   1 
ATOM   170  N  N    A LEU   A 1 10  ? 8.761  -11.248 12.021  0.64 11.69 ?  10  LEU   A N    1 
ATOM   171  N  N    B LEU   A 1 10  ? 8.831  -10.934 12.494  0.36 13.61 ?  10  LEU   A N    1 
ATOM   172  C  CA   A LEU   A 1 10  ? 8.178  -12.484 11.523  0.64 11.61 ?  10  LEU   A CA   1 
ATOM   173  C  CA   B LEU   A 1 10  ? 8.147  -12.124 12.010  0.36 13.37 ?  10  LEU   A CA   1 
ATOM   174  C  C    A LEU   A 1 10  ? 9.304  -13.423 11.096  0.64 11.92 ?  10  LEU   A C    1 
ATOM   175  C  C    B LEU   A 1 10  ? 9.198  -13.097 11.491  0.36 12.57 ?  10  LEU   A C    1 
ATOM   176  O  O    A LEU   A 1 10  ? 10.255 -13.001 10.431  0.64 12.65 ?  10  LEU   A O    1 
ATOM   177  O  O    B LEU   A 1 10  ? 10.103 -12.707 10.748  0.36 12.32 ?  10  LEU   A O    1 
ATOM   178  C  CB   A LEU   A 1 10  ? 7.287  -12.165 10.327  0.64 12.39 ?  10  LEU   A CB   1 
ATOM   179  C  CB   B LEU   A 1 10  ? 7.183  -11.745 10.886  0.36 14.18 ?  10  LEU   A CB   1 
ATOM   180  C  CG   A LEU   A 1 10  ? 6.571  -13.331 9.660   0.64 14.39 ?  10  LEU   A CG   1 
ATOM   181  C  CG   B LEU   A 1 10  ? 6.382  -12.884 10.267  0.36 15.36 ?  10  LEU   A CG   1 
ATOM   182  C  CD1  A LEU   A 1 10  ? 5.538  -13.910 10.599  0.64 15.64 ?  10  LEU   A CD1  1 
ATOM   183  C  CD1  B LEU   A 1 10  ? 5.430  -13.468 11.295  0.36 16.36 ?  10  LEU   A CD1  1 
ATOM   184  C  CD2  A LEU   A 1 10  ? 5.935  -12.885 8.353   0.64 15.72 ?  10  LEU   A CD2  1 
ATOM   185  C  CD2  B LEU   A 1 10  ? 5.624  -12.346 9.076   0.36 16.20 ?  10  LEU   A CD2  1 
ATOM   186  H  H    A LEU   A 1 10  ? 8.803  -10.630 11.424  0.64 14.04 ?  10  LEU   A H    1 
ATOM   187  H  H    B LEU   A 1 10  ? 8.928  -10.328 11.891  0.36 16.34 ?  10  LEU   A H    1 
ATOM   188  H  HA   A LEU   A 1 10  ? 7.653  -12.916 12.218  0.64 13.94 ?  10  LEU   A HA   1 
ATOM   189  H  HA   B LEU   A 1 10  ? 7.643  -12.541 12.729  0.36 16.06 ?  10  LEU   A HA   1 
ATOM   190  H  HB2  A LEU   A 1 10  ? 6.607  -11.550 10.617  0.64 14.88 ?  10  LEU   A HB2  1 
ATOM   191  H  HB2  B LEU   A 1 10  ? 6.536  -11.101 11.231  0.36 17.03 ?  10  LEU   A HB2  1 
ATOM   192  H  HB3  A LEU   A 1 10  ? 7.838  -11.752 9.647   0.64 14.88 ?  10  LEU   A HB3  1 
ATOM   193  H  HB3  B LEU   A 1 10  ? 7.689  -11.330 10.171  0.36 17.03 ?  10  LEU   A HB3  1 
ATOM   194  H  HG   A LEU   A 1 10  ? 7.213  -14.035 9.453   0.64 17.28 ?  10  LEU   A HG   1 
ATOM   195  H  HG   B LEU   A 1 10  ? 6.983  -13.583 9.963   0.36 18.44 ?  10  LEU   A HG   1 
ATOM   196  H  HD11 A LEU   A 1 10  ? 5.104  -14.667 10.173  0.64 18.77 ?  10  LEU   A HD11 1 
ATOM   197  H  HD11 B LEU   A 1 10  ? 4.898  -14.162 10.876  0.36 19.64 ?  10  LEU   A HD11 1 
ATOM   198  H  HD12 A LEU   A 1 10  ? 5.973  -14.198 11.416  0.64 18.77 ?  10  LEU   A HD12 1 
ATOM   199  H  HD12 B LEU   A 1 10  ? 5.942  -13.840 12.029  0.36 19.64 ?  10  LEU   A HD12 1 
ATOM   200  H  HD13 A LEU   A 1 10  ? 4.879  -13.226 10.802  0.64 18.77 ?  10  LEU   A HD13 1 
ATOM   201  H  HD13 B LEU   A 1 10  ? 4.850  -12.761 11.623  0.36 19.64 ?  10  LEU   A HD13 1 
ATOM   202  H  HD21 A LEU   A 1 10  ? 5.480  -13.642 7.948   0.64 18.87 ?  10  LEU   A HD21 1 
ATOM   203  H  HD21 B LEU   A 1 10  ? 5.105  -13.063 8.685   0.36 19.45 ?  10  LEU   A HD21 1 
ATOM   204  H  HD22 A LEU   A 1 10  ? 5.297  -12.180 8.542   0.64 18.87 ?  10  LEU   A HD22 1 
ATOM   205  H  HD22 B LEU   A 1 10  ? 5.036  -11.635 9.377   0.36 19.45 ?  10  LEU   A HD22 1 
ATOM   206  H  HD23 A LEU   A 1 10  ? 6.628  -12.559 7.761   0.64 18.87 ?  10  LEU   A HD23 1 
ATOM   207  H  HD23 B LEU   A 1 10  ? 6.259  -12.001 8.431   0.36 19.45 ?  10  LEU   A HD23 1 
ATOM   208  N  N    A LYS   A 1 11  ? 9.201  -14.695 11.480  0.64 12.43 ?  11  LYS   A N    1 
ATOM   209  N  N    B LYS   A 1 11  ? 9.089  -14.355 11.898  0.36 12.76 ?  11  LYS   A N    1 
ATOM   210  C  CA   A LYS   A 1 11  ? 10.213 -15.694 11.157  0.64 12.77 ?  11  LYS   A CA   1 
ATOM   211  C  CA   B LYS   A 1 11  ? 10.048 -15.373 11.490  0.36 12.73 ?  11  LYS   A CA   1 
ATOM   212  C  C    A LYS   A 1 11  ? 9.870  -16.302 9.804   0.64 12.71 ?  11  LYS   A C    1 
ATOM   213  C  C    B LYS   A 1 11  ? 9.669  -15.902 10.111  0.36 12.09 ?  11  LYS   A C    1 
ATOM   214  O  O    A LYS   A 1 11  ? 8.805  -16.905 9.648   0.64 14.25 ?  11  LYS   A O    1 
ATOM   215  O  O    B LYS   A 1 11  ? 8.549  -16.383 9.914   0.36 11.74 ?  11  LYS   A O    1 
ATOM   216  C  CB   A LYS   A 1 11  ? 10.257 -16.767 12.248  0.64 12.84 ?  11  LYS   A CB   1 
ATOM   217  C  CB   B LYS   A 1 11  ? 10.053 -16.507 12.512  0.36 12.77 ?  11  LYS   A CB   1 
ATOM   218  C  CG   A LYS   A 1 11  ? 11.314 -17.859 12.084  0.64 13.11 ?  11  LYS   A CG   1 
ATOM   219  C  CG   B LYS   A 1 11  ? 11.024 -17.626 12.195  0.36 13.07 ?  11  LYS   A CG   1 
ATOM   220  C  CD   A LYS   A 1 11  ? 11.419 -18.671 13.380  0.64 13.42 ?  11  LYS   A CD   1 
ATOM   221  C  CD   B LYS   A 1 11  ? 11.012 -18.680 13.289  0.36 13.68 ?  11  LYS   A CD   1 
ATOM   222  C  CE   A LYS   A 1 11  ? 12.411 -19.822 13.289  0.64 13.73 ?  11  LYS   A CE   1 
ATOM   223  C  CE   B LYS   A 1 11  ? 12.032 -19.778 13.025  0.36 13.88 ?  11  LYS   A CE   1 
ATOM   224  N  NZ   A LYS   A 1 11  ? 13.783 -19.351 12.970  0.64 14.13 ?  11  LYS   A NZ   1 
ATOM   225  N  NZ   B LYS   A 1 11  ? 13.432 -19.260 12.988  0.36 14.20 ?  11  LYS   A NZ   1 
ATOM   226  H  H    A LYS   A 1 11  ? 8.539  -15.015 11.928  0.64 14.92 ?  11  LYS   A H    1 
ATOM   227  H  H    B LYS   A 1 11  ? 8.468  -14.642 12.416  0.36 15.33 ?  11  LYS   A H    1 
ATOM   228  H  HA   A LYS   A 1 11  ? 11.085 -15.277 11.096  0.64 15.33 ?  11  LYS   A HA   1 
ATOM   229  H  HA   B LYS   A 1 11  ? 10.936 -14.983 11.442  0.36 15.29 ?  11  LYS   A HA   1 
ATOM   230  H  HB2  A LYS   A 1 11  ? 10.434 -16.331 13.096  0.64 15.42 ?  11  LYS   A HB2  1 
ATOM   231  H  HB2  B LYS   A 1 11  ? 10.298 -16.140 13.377  0.36 15.33 ?  11  LYS   A HB2  1 
ATOM   232  H  HB3  A LYS   A 1 11  ? 9.398  -17.209 12.284  0.64 15.42 ?  11  LYS   A HB3  1 
ATOM   233  H  HB3  B LYS   A 1 11  ? 9.164  -16.888 12.557  0.36 15.33 ?  11  LYS   A HB3  1 
ATOM   234  H  HG2  A LYS   A 1 11  ? 11.061 -18.461 11.365  0.64 15.74 ?  11  LYS   A HG2  1 
ATOM   235  H  HG2  B LYS   A 1 11  ? 10.767 -18.051 11.362  0.36 15.70 ?  11  LYS   A HG2  1 
ATOM   236  H  HG3  A LYS   A 1 11  ? 12.181 -17.460 11.904  0.64 15.74 ?  11  LYS   A HG3  1 
ATOM   237  H  HG3  B LYS   A 1 11  ? 11.920 -17.264 12.127  0.36 15.70 ?  11  LYS   A HG3  1 
ATOM   238  H  HD2  A LYS   A 1 11  ? 11.704 -18.088 14.099  0.64 16.11 ?  11  LYS   A HD2  1 
ATOM   239  H  HD2  B LYS   A 1 11  ? 11.226 -18.264 14.138  0.36 16.42 ?  11  LYS   A HD2  1 
ATOM   240  H  HD3  A LYS   A 1 11  ? 10.547 -19.049 13.588  0.64 16.11 ?  11  LYS   A HD3  1 
ATOM   241  H  HD3  B LYS   A 1 11  ? 10.131 -19.088 13.329  0.36 16.42 ?  11  LYS   A HD3  1 
ATOM   242  H  HE2  A LYS   A 1 11  ? 12.444 -20.287 14.142  0.64 16.49 ?  11  LYS   A HE2  1 
ATOM   243  H  HE2  B LYS   A 1 11  ? 11.975 -20.441 13.730  0.36 16.67 ?  11  LYS   A HE2  1 
ATOM   244  H  HE3  A LYS   A 1 11  ? 12.132 -20.433 12.589  0.64 16.49 ?  11  LYS   A HE3  1 
ATOM   245  H  HE3  B LYS   A 1 11  ? 11.841 -20.188 12.166  0.36 16.67 ?  11  LYS   A HE3  1 
ATOM   246  H  HZ1  A LYS   A 1 11  ? 14.333 -20.047 12.890  0.64 16.96 ?  11  LYS   A HZ1  1 
ATOM   247  H  HZ1  B LYS   A 1 11  ? 13.990 -19.909 12.745  0.36 17.05 ?  11  LYS   A HZ1  1 
ATOM   248  H  HZ2  A LYS   A 1 11  ? 13.777 -18.898 12.204  0.64 16.96 ?  11  LYS   A HZ2  1 
ATOM   249  H  HZ2  B LYS   A 1 11  ? 13.496 -18.591 12.404  0.36 17.05 ?  11  LYS   A HZ2  1 
ATOM   250  H  HZ3  A LYS   A 1 11  ? 14.082 -18.821 13.618  0.64 16.96 ?  11  LYS   A HZ3  1 
ATOM   251  H  HZ3  B LYS   A 1 11  ? 13.667 -18.963 13.793  0.36 17.05 ?  11  LYS   A HZ3  1 
ATOM   252  N  N    A LEU   A 1 12  ? 10.760 -16.144 8.825   0.64 11.56 ?  12  LEU   A N    1 
ATOM   253  N  N    B LEU   A 1 12  ? 10.591 -15.806 9.153   0.36 12.21 ?  12  LEU   A N    1 
ATOM   254  C  CA   A LEU   A 1 12  ? 10.506 -16.726 7.513   0.64 11.79 ?  12  LEU   A CA   1 
ATOM   255  C  CA   B LEU   A 1 12  ? 10.357 -16.311 7.803   0.36 12.36 ?  12  LEU   A CA   1 
ATOM   256  C  C    A LEU   A 1 12  ? 11.107 -18.119 7.374   0.64 11.80 ?  12  LEU   A C    1 
ATOM   257  C  C    B LEU   A 1 12  ? 10.906 -17.717 7.597   0.36 12.46 ?  12  LEU   A C    1 
ATOM   258  O  O    A LEU   A 1 12  ? 10.498 -18.992 6.749   0.64 12.10 ?  12  LEU   A O    1 
ATOM   259  O  O    B LEU   A 1 12  ? 10.223 -18.579 7.035   0.36 12.47 ?  12  LEU   A O    1 
ATOM   260  C  CB   A LEU   A 1 12  ? 11.055 -15.825 6.402   0.64 11.96 ?  12  LEU   A CB   1 
ATOM   261  C  CB   B LEU   A 1 12  ? 10.957 -15.361 6.757   0.36 13.49 ?  12  LEU   A CB   1 
ATOM   262  C  CG   A LEU   A 1 12  ? 10.399 -14.452 6.229   0.64 12.68 ?  12  LEU   A CG   1 
ATOM   263  C  CG   B LEU   A 1 12  ? 10.309 -13.979 6.677   0.36 14.51 ?  12  LEU   A CG   1 
ATOM   264  C  CD1  A LEU   A 1 12  ? 11.134 -13.664 5.169   0.64 12.77 ?  12  LEU   A CD1  1 
ATOM   265  C  CD1  B LEU   A 1 12  ? 10.841 -13.196 5.481   0.36 14.84 ?  12  LEU   A CD1  1 
ATOM   266  C  CD2  A LEU   A 1 12  ? 8.924  -14.594 5.869   0.64 13.74 ?  12  LEU   A CD2  1 
ATOM   267  C  CD2  B LEU   A 1 12  ? 8.797  -14.106 6.610   0.36 15.23 ?  12  LEU   A CD2  1 
ATOM   268  H  H    A LEU   A 1 12  ? 11.510 -15.715 8.892   0.64 13.89 ?  12  LEU   A H    1 
ATOM   269  H  H    B LEU   A 1 12  ? 11.363 -15.429 9.257   0.36 14.67 ?  12  LEU   A H    1 
ATOM   270  H  HA   A LEU   A 1 12  ? 9.553  -16.807 7.387   0.64 14.16 ?  12  LEU   A HA   1 
ATOM   271  H  HA   B LEU   A 1 12  ? 9.403  -16.351 7.653   0.36 14.85 ?  12  LEU   A HA   1 
ATOM   272  H  HB2  A LEU   A 1 12  ? 11.995 -15.673 6.573   0.64 14.37 ?  12  LEU   A HB2  1 
ATOM   273  H  HB2  B LEU   A 1 12  ? 11.898 -15.227 6.959   0.36 16.20 ?  12  LEU   A HB2  1 
ATOM   274  H  HB3  A LEU   A 1 12  ? 10.956 -16.298 5.559   0.64 14.37 ?  12  LEU   A HB3  1 
ATOM   275  H  HB3  B LEU   A 1 12  ? 10.872 -15.770 5.881   0.36 16.20 ?  12  LEU   A HB3  1 
ATOM   276  H  HG   A LEU   A 1 12  ? 10.457 -13.968 7.065   0.64 15.23 ?  12  LEU   A HG   1 
ATOM   277  H  HG   B LEU   A 1 12  ? 10.533 -13.481 7.479   0.36 17.43 ?  12  LEU   A HG   1 
ATOM   278  H  HD11 A LEU   A 1 12  ? 10.711 -12.801 5.067   0.64 15.33 ?  12  LEU   A HD11 1 
ATOM   279  H  HD11 B LEU   A 1 12  ? 10.417 -12.322 5.463   0.36 17.82 ?  12  LEU   A HD11 1 
ATOM   280  H  HD12 A LEU   A 1 12  ? 12.059 -13.553 5.446   0.64 15.33 ?  12  LEU   A HD12 1 
ATOM   281  H  HD12 B LEU   A 1 12  ? 11.801 -13.095 5.570   0.36 17.82 ?  12  LEU   A HD12 1 
ATOM   282  H  HD13 A LEU   A 1 12  ? 11.100 -14.154 4.331   0.64 15.33 ?  12  LEU   A HD13 1 
ATOM   283  H  HD13 B LEU   A 1 12  ? 10.632 -13.681 4.668   0.36 17.82 ?  12  LEU   A HD13 1 
ATOM   284  H  HD21 A LEU   A 1 12  ? 8.561  -13.721 5.665   0.64 16.49 ?  12  LEU   A HD21 1 
ATOM   285  H  HD21 B LEU   A 1 12  ? 8.423  -13.271 6.294   0.36 18.29 ?  12  LEU   A HD21 1 
ATOM   286  H  HD22 A LEU   A 1 12  ? 8.841  -15.176 5.094   0.64 16.49 ?  12  LEU   A HD22 1 
ATOM   287  H  HD22 B LEU   A 1 12  ? 8.568  -14.826 6.004   0.36 18.29 ?  12  LEU   A HD22 1 
ATOM   288  H  HD23 A LEU   A 1 12  ? 8.447  -14.985 6.620   0.64 16.49 ?  12  LEU   A HD23 1 
ATOM   289  H  HD23 B LEU   A 1 12  ? 8.459  -14.304 7.500   0.36 18.29 ?  12  LEU   A HD23 1 
ATOM   290  N  N    A THR   A 1 13  ? 12.304 -18.328 7.917   0.64 12.43 ?  13  THR   A N    1 
ATOM   291  N  N    B THR   A 1 13  ? 12.140 -17.958 8.021   0.36 12.88 ?  13  THR   A N    1 
ATOM   292  C  CA   A THR   A 1 13  ? 13.015 -19.600 7.844   0.64 12.56 ?  13  THR   A CA   1 
ATOM   293  C  CA   B THR   A 1 13  ? 12.770 -19.261 7.891   0.36 13.28 ?  13  THR   A CA   1 
ATOM   294  C  C    A THR   A 1 13  ? 13.776 -19.794 9.149   0.64 12.86 ?  13  THR   A C    1 
ATOM   295  C  C    B THR   A 1 13  ? 13.543 -19.542 9.172   0.36 13.95 ?  13  THR   A C    1 
ATOM   296  O  O    A THR   A 1 13  ? 13.681 -18.986 10.078  0.64 13.09 ?  13  THR   A O    1 
ATOM   297  O  O    B THR   A 1 13  ? 13.430 -18.824 10.171  0.36 14.44 ?  13  THR   A O    1 
ATOM   298  C  CB   A THR   A 1 13  ? 14.004 -19.651 6.671   0.64 13.27 ?  13  THR   A CB   1 
ATOM   299  C  CB   B THR   A 1 13  ? 13.722 -19.306 6.688   0.36 13.44 ?  13  THR   A CB   1 
ATOM   300  O  OG1  A THR   A 1 13  ? 15.068 -18.727 6.915   0.64 13.54 ?  13  THR   A OG1  1 
ATOM   301  O  OG1  B THR   A 1 13  ? 14.804 -18.398 6.917   0.36 13.36 ?  13  THR   A OG1  1 
ATOM   302  C  CG2  A THR   A 1 13  ? 13.339 -19.321 5.345   0.64 13.98 ?  13  THR   A CG2  1 
ATOM   303  C  CG2  B THR   A 1 13  ? 13.010 -18.943 5.385   0.36 13.93 ?  13  THR   A CG2  1 
ATOM   304  H  H    A THR   A 1 13  ? 12.743 -17.729 8.342   0.64 14.92 ?  13  THR   A H    1 
ATOM   305  H  H    B THR   A 1 13  ? 12.641 -17.365 8.387   0.36 15.47 ?  13  THR   A H    1 
ATOM   306  H  HA   A THR   A 1 13  ? 12.382 -20.329 7.740   0.64 15.08 ?  13  THR   A HA   1 
ATOM   307  H  HA   B THR   A 1 13  ? 12.084 -19.942 7.771   0.36 15.95 ?  13  THR   A HA   1 
ATOM   308  H  HB   A THR   A 1 13  ? 14.378 -20.546 6.602   0.64 15.93 ?  13  THR   A HB   1 
ATOM   309  H  HB   B THR   A 1 13  ? 14.076 -20.203 6.592   0.36 16.14 ?  13  THR   A HB   1 
ATOM   310  H  HG1  A THR   A 1 13  ? 15.616 -18.741 6.269   0.64 16.26 ?  13  THR   A HG1  1 
ATOM   311  H  HG1  B THR   A 1 13  ? 15.334 -18.409 6.265   0.36 16.05 ?  13  THR   A HG1  1 
ATOM   312  H  HG21 A THR   A 1 13  ? 13.960 -19.480 4.614   0.64 16.79 ?  13  THR   A HG21 1 
ATOM   313  H  HG21 B THR   A 1 13  ? 13.622 -19.040 4.635   0.36 16.72 ?  13  THR   A HG21 1 
ATOM   314  H  HG22 A THR   A 1 13  ? 12.560 -19.885 5.218   0.64 16.79 ?  13  THR   A HG22 1 
ATOM   315  H  HG22 B THR   A 1 13  ? 12.252 -19.533 5.245   0.36 16.72 ?  13  THR   A HG22 1 
ATOM   316  H  HG23 A THR   A 1 13  ? 13.066 -18.394 5.331   0.64 16.79 ?  13  THR   A HG23 1 
ATOM   317  H  HG23 B THR   A 1 13  ? 12.697 -18.028 5.418   0.36 16.72 ?  13  THR   A HG23 1 
ATOM   318  N  N    A ASP   A 1 14  ? 14.584 -20.854 9.199   0.64 13.61 ?  14  ASP   A N    1 
ATOM   319  N  N    B ASP   A 1 14  ? 14.356 -20.595 9.117   0.36 14.47 ?  14  ASP   A N    1 
ATOM   320  C  CA   A ASP   A 1 14  ? 15.413 -21.096 10.373  0.64 15.18 ?  14  ASP   A CA   1 
ATOM   321  C  CA   B ASP   A 1 14  ? 15.220 -20.944 10.235  0.36 15.09 ?  14  ASP   A CA   1 
ATOM   322  C  C    A ASP   A 1 14  ? 16.231 -19.868 10.759  0.64 15.01 ?  14  ASP   A C    1 
ATOM   323  C  C    B ASP   A 1 14  ? 16.095 -19.771 10.665  0.36 14.29 ?  14  ASP   A C    1 
ATOM   324  O  O    A ASP   A 1 14  ? 16.439 -19.602 11.948  0.64 16.23 ?  14  ASP   A O    1 
ATOM   325  O  O    B ASP   A 1 14  ? 16.373 -19.605 11.859  0.36 15.01 ?  14  ASP   A O    1 
ATOM   326  C  CB   A ASP   A 1 14  ? 16.353 -22.269 10.111  0.64 17.68 ?  14  ASP   A CB   1 
ATOM   327  C  CB   B ASP   A 1 14  ? 16.088 -22.138 9.839   0.36 16.75 ?  14  ASP   A CB   1 
ATOM   328  C  CG   A ASP   A 1 14  ? 17.271 -22.528 11.275  0.64 21.28 ?  14  ASP   A CG   1 
ATOM   329  C  CG   B ASP   A 1 14  ? 17.078 -22.526 10.919  0.36 18.79 ?  14  ASP   A CG   1 
ATOM   330  O  OD1  A ASP   A 1 14  ? 16.779 -23.042 12.305  0.64 22.51 ?  14  ASP   A OD1  1 
ATOM   331  O  OD1  B ASP   A 1 14  ? 16.664 -22.655 12.090  0.36 19.36 ?  14  ASP   A OD1  1 
ATOM   332  O  OD2  A ASP   A 1 14  ? 18.470 -22.199 11.164  0.64 23.36 -1 14  ASP   A OD2  1 
ATOM   333  O  OD2  B ASP   A 1 14  ? 18.268 -22.722 10.595  0.36 20.16 -1 14  ASP   A OD2  1 
ATOM   334  H  H    A ASP   A 1 14  ? 14.680 -21.438 8.570   0.64 16.34 ?  14  ASP   A H    1 
ATOM   335  H  H    B ASP   A 1 14  ? 14.408 -21.122 8.444   0.36 17.37 ?  14  ASP   A H    1 
ATOM   336  H  HA   A ASP   A 1 14  ? 14.850 -21.332 11.123  0.64 18.23 ?  14  ASP   A HA   1 
ATOM   337  H  HA   B ASP   A 1 14  ? 14.668 -21.203 10.989  0.36 18.11 ?  14  ASP   A HA   1 
ATOM   338  H  HB2  A ASP   A 1 14  ? 15.824 -23.076 9.952   0.64 21.22 ?  14  ASP   A HB2  1 
ATOM   339  H  HB2  B ASP   A 1 14  ? 15.507 -22.897 9.661   0.36 20.11 ?  14  ASP   A HB2  1 
ATOM   340  H  HB3  A ASP   A 1 14  ? 16.901 -22.083 9.334   0.64 21.22 ?  14  ASP   A HB3  1 
ATOM   341  H  HB3  B ASP   A 1 14  ? 16.584 -21.909 9.038   0.36 20.11 ?  14  ASP   A HB3  1 
ATOM   342  N  N    A ASN   A 1 15  ? 16.713 -19.110 9.770   0.64 14.28 ?  15  ASN   A N    1 
ATOM   343  N  N    B ASN   A 1 15  ? 16.535 -18.937 9.715   0.36 13.22 ?  15  ASN   A N    1 
ATOM   344  C  CA   A ASN   A 1 15  ? 17.693 -18.060 10.024  0.64 14.54 ?  15  ASN   A CA   1 
ATOM   345  C  CA   B ASN   A 1 15  ? 17.523 -17.909 10.025  0.36 13.28 ?  15  ASN   A CA   1 
ATOM   346  C  C    A ASN   A 1 15  ? 17.312 -16.683 9.497   0.64 14.78 ?  15  ASN   A C    1 
ATOM   347  C  C    B ASN   A 1 15  ? 17.177 -16.505 9.547   0.36 13.58 ?  15  ASN   A C    1 
ATOM   348  O  O    A ASN   A 1 15  ? 18.059 -15.734 9.758   0.64 16.11 ?  15  ASN   A O    1 
ATOM   349  O  O    B ASN   A 1 15  ? 17.989 -15.596 9.747   0.36 14.92 ?  15  ASN   A O    1 
ATOM   350  C  CB   A ASN   A 1 15  ? 19.063 -18.451 9.440   0.64 14.62 ?  15  ASN   A CB   1 
ATOM   351  C  CB   B ASN   A 1 15  ? 18.906 -18.295 9.474   0.36 13.19 ?  15  ASN   A CB   1 
ATOM   352  C  CG   A ASN   A 1 15  ? 19.042 -18.539 7.932   0.64 15.08 ?  15  ASN   A CG   1 
ATOM   353  C  CG   B ASN   A 1 15  ? 18.921 -18.421 7.966   0.36 13.51 ?  15  ASN   A CG   1 
ATOM   354  O  OD1  A ASN   A 1 15  ? 18.350 -19.384 7.354   0.64 15.71 ?  15  ASN   A OD1  1 
ATOM   355  O  OD1  B ASN   A 1 15  ? 18.148 -19.192 7.387   0.36 14.07 ?  15  ASN   A OD1  1 
ATOM   356  N  ND2  A ASN   A 1 15  ? 19.808 -17.667 7.279   0.64 15.64 ?  15  ASN   A ND2  1 
ATOM   357  N  ND2  B ASN   A 1 15  ? 19.797 -17.651 7.317   0.36 13.65 ?  15  ASN   A ND2  1 
ATOM   358  H  H    A ASN   A 1 15  ? 16.490 -19.191 8.949   0.64 17.14 ?  15  ASN   A H    1 
ATOM   359  H  H    B ASN   A 1 15  ? 16.271 -18.941 8.894   0.36 15.88 ?  15  ASN   A H    1 
ATOM   360  H  HA   A ASN   A 1 15  ? 17.816 -17.979 10.981  0.64 17.46 ?  15  ASN   A HA   1 
ATOM   361  H  HA   B ASN   A 1 15  ? 17.609 -17.854 10.984  0.36 15.95 ?  15  ASN   A HA   1 
ATOM   362  H  HB2  A ASN   A 1 15  ? 19.725 -17.781 9.698   0.64 17.56 ?  15  ASN   A HB2  1 
ATOM   363  H  HB2  B ASN   A 1 15  ? 19.549 -17.612 9.729   0.36 15.84 ?  15  ASN   A HB2  1 
ATOM   364  H  HB3  A ASN   A 1 15  ? 19.331 -19.319 9.787   0.64 17.56 ?  15  ASN   A HB3  1 
ATOM   365  H  HB3  B ASN   A 1 15  ? 19.164 -19.149 9.846   0.36 15.84 ?  15  ASN   A HB3  1 
ATOM   366  H  HD21 A ASN   A 1 15  ? 19.831 -17.671 6.420   0.64 18.77 ?  15  ASN   A HD21 1 
ATOM   367  H  HD21 B ASN   A 1 15  ? 19.851 -17.676 6.458   0.36 16.39 ?  15  ASN   A HD21 1 
ATOM   368  H  HD22 A ASN   A 1 15  ? 20.284 -17.090 7.715   0.64 18.77 ?  15  ASN   A HD22 1 
ATOM   369  H  HD22 B ASN   A 1 15  ? 20.319 -17.118 7.757   0.36 16.39 ?  15  ASN   A HD22 1 
ATOM   370  N  N    A VAL   A 1 16  ? 16.203 -16.535 8.769   0.64 14.12 ?  16  VAL   A N    1 
ATOM   371  N  N    B VAL   A 1 16  ? 16.005 -16.287 8.955   0.36 12.87 ?  16  VAL   A N    1 
ATOM   372  C  CA   A VAL   A 1 16  ? 15.797 -15.256 8.190   0.64 13.63 ?  16  VAL   A CA   1 
ATOM   373  C  CA   B VAL   A 1 16  ? 15.639 -15.001 8.372   0.36 12.68 ?  16  VAL   A CA   1 
ATOM   374  C  C    A VAL   A 1 16  ? 14.517 -14.762 8.855   0.64 12.82 ?  16  VAL   A C    1 
ATOM   375  C  C    B VAL   A 1 16  ? 14.383 -14.482 9.061   0.36 12.34 ?  16  VAL   A C    1 
ATOM   376  O  O    A VAL   A 1 16  ? 13.527 -15.498 8.955   0.64 12.91 ?  16  VAL   A O    1 
ATOM   377  O  O    B VAL   A 1 16  ? 13.381 -15.201 9.167   0.36 12.14 ?  16  VAL   A O    1 
ATOM   378  C  CB   A VAL   A 1 16  ? 15.630 -15.335 6.663   0.64 14.13 ?  16  VAL   A CB   1 
ATOM   379  C  CB   B VAL   A 1 16  ? 15.449 -15.103 6.847   0.36 13.01 ?  16  VAL   A CB   1 
ATOM   380  C  CG1  A VAL   A 1 16  ? 15.202 -13.975 6.112   0.64 15.14 ?  16  VAL   A CG1  1 
ATOM   381  C  CG1  B VAL   A 1 16  ? 15.091 -13.739 6.248   0.36 13.18 ?  16  VAL   A CG1  1 
ATOM   382  C  CG2  A VAL   A 1 16  ? 16.924 -15.788 6.001   0.64 14.66 ?  16  VAL   A CG2  1 
ATOM   383  C  CG2  B VAL   A 1 16  ? 16.708 -15.667 6.192   0.36 13.83 ?  16  VAL   A CG2  1 
ATOM   384  H  H    A VAL   A 1 16  ? 15.676 -17.190 8.581   0.64 16.95 ?  16  VAL   A H    1 
ATOM   385  H  H    B VAL   A 1 16  ? 15.386 -16.879 8.883   0.36 15.45 ?  16  VAL   A H    1 
ATOM   386  H  HA   A VAL   A 1 16  ? 16.494 -14.610 8.372   0.64 16.36 ?  16  VAL   A HA   1 
ATOM   387  H  HA   B VAL   A 1 16  ? 16.344 -14.358 8.539   0.36 15.23 ?  16  VAL   A HA   1 
ATOM   388  H  HB   A VAL   A 1 16  ? 14.940 -15.980 6.449   0.64 16.97 ?  16  VAL   A HB   1 
ATOM   389  H  HB   B VAL   A 1 16  ? 14.720 -15.709 6.660   0.36 15.62 ?  16  VAL   A HB   1 
ATOM   390  H  HG11 A VAL   A 1 16  ? 15.291 -13.984 5.146   0.64 18.18 ?  16  VAL   A HG11 1 
ATOM   391  H  HG11 B VAL   A 1 16  ? 15.137 -13.800 5.278   0.36 15.83 ?  16  VAL   A HG11 1 
ATOM   392  H  HG12 A VAL   A 1 16  ? 14.278 -13.809 6.355   0.64 18.18 ?  16  VAL   A HG12 1 
ATOM   393  H  HG12 B VAL   A 1 16  ? 14.192 -13.499 6.518   0.36 15.83 ?  16  VAL   A HG12 1 
ATOM   394  H  HG13 A VAL   A 1 16  ? 15.773 -13.287 6.489   0.64 18.18 ?  16  VAL   A HG13 1 
ATOM   395  H  HG13 B VAL   A 1 16  ? 15.723 -13.076 6.564   0.36 15.83 ?  16  VAL   A HG13 1 
ATOM   396  H  HG21 A VAL   A 1 16  ? 16.819 -15.731 5.038   0.64 17.60 ?  16  VAL   A HG21 1 
ATOM   397  H  HG21 B VAL   A 1 16  ? 16.607 -15.633 5.228   0.36 16.60 ?  16  VAL   A HG21 1 
ATOM   398  H  HG22 A VAL   A 1 16  ? 17.645 -15.212 6.290   0.64 17.60 ?  16  VAL   A HG22 1 
ATOM   399  H  HG22 B VAL   A 1 16  ? 17.473 -15.137 6.463   0.36 16.60 ?  16  VAL   A HG22 1 
ATOM   400  H  HG23 A VAL   A 1 16  ? 17.105 -16.704 6.260   0.64 17.60 ?  16  VAL   A HG23 1 
ATOM   401  H  HG23 B VAL   A 1 16  ? 16.826 -16.587 6.479   0.36 16.60 ?  16  VAL   A HG23 1 
ATOM   402  N  N    A TYR   A 1 17  ? 14.537 -13.494 9.261   0.64 12.71 ?  17  TYR   A N    1 
ATOM   403  N  N    B TYR   A 1 17  ? 14.445 -13.229 9.516   0.36 12.29 ?  17  TYR   A N    1 
ATOM   404  C  CA   A TYR   A 1 17  ? 13.444 -12.810 9.935   0.64 12.30 ?  17  TYR   A CA   1 
ATOM   405  C  CA   B TYR   A 1 17  ? 13.379 -12.562 10.248  0.36 12.27 ?  17  TYR   A CA   1 
ATOM   406  C  C    A TYR   A 1 17  ? 13.171 -11.496 9.208   0.64 11.92 ?  17  TYR   A C    1 
ATOM   407  C  C    B TYR   A 1 17  ? 13.131 -11.206 9.608   0.36 12.02 ?  17  TYR   A C    1 
ATOM   408  O  O    A TYR   A 1 17  ? 14.065 -10.938 8.571   0.64 11.60 ?  17  TYR   A O    1 
ATOM   409  O  O    B TYR   A 1 17  ? 14.052 -10.599 9.060   0.36 11.73 ?  17  TYR   A O    1 
ATOM   410  C  CB   A TYR   A 1 17  ? 13.843 -12.514 11.385  0.64 13.56 ?  17  TYR   A CB   1 
ATOM   411  C  CB   B TYR   A 1 17  ? 13.795 -12.365 11.706  0.36 12.98 ?  17  TYR   A CB   1 
ATOM   412  C  CG   A TYR   A 1 17  ? 14.042 -13.755 12.231  0.64 15.30 ?  17  TYR   A CG   1 
ATOM   413  C  CG   B TYR   A 1 17  ? 14.003 -13.668 12.440  0.36 13.81 ?  17  TYR   A CG   1 
ATOM   414  C  CD1  A TYR   A 1 17  ? 15.228 -14.483 12.186  0.64 16.55 ?  17  TYR   A CD1  1 
ATOM   415  C  CD1  B TYR   A 1 17  ? 15.169 -14.413 12.277  0.36 14.61 ?  17  TYR   A CD1  1 
ATOM   416  C  CD2  A TYR   A 1 17  ? 13.033 -14.206 13.072  0.64 15.96 ?  17  TYR   A CD2  1 
ATOM   417  C  CD2  B TYR   A 1 17  ? 13.024 -14.164 13.284  0.36 13.92 ?  17  TYR   A CD2  1 
ATOM   418  C  CE1  A TYR   A 1 17  ? 15.398 -15.627 12.956  0.64 17.51 ?  17  TYR   A CE1  1 
ATOM   419  C  CE1  B TYR   A 1 17  ? 15.348 -15.617 12.943  0.36 15.16 ?  17  TYR   A CE1  1 
ATOM   420  C  CE2  A TYR   A 1 17  ? 13.194 -15.351 13.845  0.64 17.07 ?  17  TYR   A CE2  1 
ATOM   421  C  CE2  B TYR   A 1 17  ? 13.193 -15.365 13.953  0.36 14.62 ?  17  TYR   A CE2  1 
ATOM   422  C  CZ   A TYR   A 1 17  ? 14.379 -16.055 13.785  0.64 17.61 ?  17  TYR   A CZ   1 
ATOM   423  C  CZ   B TYR   A 1 17  ? 14.357 -16.085 13.783  0.36 15.02 ?  17  TYR   A CZ   1 
ATOM   424  O  OH   A TYR   A 1 17  ? 14.541 -17.186 14.554  0.64 18.58 ?  17  TYR   A OH   1 
ATOM   425  O  OH   B TYR   A 1 17  ? 14.524 -17.278 14.450  0.36 15.58 ?  17  TYR   A OH   1 
ATOM   426  H  H    A TYR   A 1 17  ? 15.222 -12.993 9.145   0.64 15.26 ?  17  TYR   A H    1 
ATOM   427  H  H    B TYR   A 1 17  ? 15.132 -12.719 9.401   0.36 14.75 ?  17  TYR   A H    1 
ATOM   428  H  HA   A TYR   A 1 17  ? 12.648 -13.374 9.924   0.64 14.77 ?  17  TYR   A HA   1 
ATOM   429  H  HA   B TYR   A 1 17  ? 12.562 -13.078 10.209  0.36 14.73 ?  17  TYR   A HA   1 
ATOM   430  H  HB2  A TYR   A 1 17  ? 14.677 -12.024 11.385  0.64 16.28 ?  17  TYR   A HB2  1 
ATOM   431  H  HB2  B TYR   A 1 17  ? 14.629 -11.870 11.725  0.36 15.58 ?  17  TYR   A HB2  1 
ATOM   432  H  HB3  A TYR   A 1 17  ? 13.145 -11.989 11.794  0.64 16.28 ?  17  TYR   A HB3  1 
ATOM   433  H  HB3  B TYR   A 1 17  ? 13.104 -11.865 12.167  0.36 15.58 ?  17  TYR   A HB3  1 
ATOM   434  H  HD1  A TYR   A 1 17  ? 15.918 -14.204 11.628  0.64 19.87 ?  17  TYR   A HD1  1 
ATOM   435  H  HD1  B TYR   A 1 17  ? 15.839 -14.100 11.709  0.36 17.54 ?  17  TYR   A HD1  1 
ATOM   436  H  HD2  A TYR   A 1 17  ? 12.231 -13.742 13.119  0.64 19.16 ?  17  TYR   A HD2  1 
ATOM   437  H  HD2  B TYR   A 1 17  ? 12.237 -13.683 13.401  0.36 16.72 ?  17  TYR   A HD2  1 
ATOM   438  H  HE1  A TYR   A 1 17  ? 16.199 -16.104 12.915  0.64 21.02 ?  17  TYR   A HE1  1 
ATOM   439  H  HE1  B TYR   A 1 17  ? 16.134 -16.105 12.829  0.36 18.20 ?  17  TYR   A HE1  1 
ATOM   440  H  HE2  A TYR   A 1 17  ? 12.507 -15.639 14.406  0.64 20.50 ?  17  TYR   A HE2  1 
ATOM   441  H  HE2  B TYR   A 1 17  ? 12.527 -15.679 14.518  0.36 17.55 ?  17  TYR   A HE2  1 
ATOM   442  H  HH   A TYR   A 1 17  ? 13.804 -17.415 14.883  0.64 22.30 ?  17  TYR   A HH   1 
ATOM   443  H  HH   B TYR   A 1 17  ? 13.830 -17.457 14.885  0.36 18.71 ?  17  TYR   A HH   1 
ATOM   444  N  N    A ILE   A 1 18  ? 11.945 -10.972 9.315   0.64 12.10 ?  18  ILE   A N    1 
ATOM   445  N  N    B ILE   A 1 18  ? 11.892 -10.715 9.683   0.36 11.69 ?  18  ILE   A N    1 
ATOM   446  C  CA   A ILE   A 1 18  ? 11.561 -9.782  8.551   0.64 12.08 ?  18  ILE   A CA   1 
ATOM   447  C  CA   B ILE   A 1 18  ? 11.512 -9.514  8.944   0.36 11.13 ?  18  ILE   A CA   1 
ATOM   448  C  C    A ILE   A 1 18  ? 10.583 -8.921  9.346   0.64 12.52 ?  18  ILE   A C    1 
ATOM   449  C  C    B ILE   A 1 18  ? 10.589 -8.643  9.787   0.36 11.39 ?  18  ILE   A C    1 
ATOM   450  O  O    A ILE   A 1 18  ? 9.762  -9.429  10.113  0.64 12.94 ?  18  ILE   A O    1 
ATOM   451  O  O    B ILE   A 1 18  ? 9.742  -9.147  10.534  0.36 11.81 ?  18  ILE   A O    1 
ATOM   452  C  CB   A ILE   A 1 18  ? 11.012 -10.192 7.164   0.64 11.81 ?  18  ILE   A CB   1 
ATOM   453  C  CB   B ILE   A 1 18  ? 10.889 -9.869  7.578   0.36 10.86 ?  18  ILE   A CB   1 
ATOM   454  C  CG1  A ILE   A 1 18  ? 10.968 -8.996  6.220   0.64 12.00 ?  18  ILE   A CG1  1 
ATOM   455  C  CG1  B ILE   A 1 18  ? 10.853 -8.643  6.665   0.36 11.82 ?  18  ILE   A CG1  1 
ATOM   456  C  CG2  A ILE   A 1 18  ? 9.656  -10.894 7.296   0.64 11.62 ?  18  ILE   A CG2  1 
ATOM   457  C  CG2  B ILE   A 1 18  ? 9.501  -10.474 7.758   0.36 11.73 ?  18  ILE   A CG2  1 
ATOM   458  C  CD1  A ILE   A 1 18  ? 10.700 -9.397  4.796   0.64 13.34 ?  18  ILE   A CD1  1 
ATOM   459  C  CD1  B ILE   A 1 18  ? 10.541 -8.983  5.227   0.36 13.13 ?  18  ILE   A CD1  1 
ATOM   460  H  H    A ILE   A 1 18  ? 11.334 -11.297 9.825   0.64 14.53 ?  18  ILE   A H    1 
ATOM   461  H  H    B ILE   A 1 18  ? 11.256 -11.056 10.154  0.36 14.04 ?  18  ILE   A H    1 
ATOM   462  H  HA   A ILE   A 1 18  ? 12.362 -9.263  8.399   0.64 14.50 ?  18  ILE   A HA   1 
ATOM   463  H  HA   B ILE   A 1 18  ? 12.311 -8.996  8.773   0.36 13.36 ?  18  ILE   A HA   1 
ATOM   464  H  HB   A ILE   A 1 18  ? 11.630 -10.842 6.785   0.64 14.18 ?  18  ILE   A HB   1 
ATOM   465  H  HB   B ILE   A 1 18  ? 11.453 -10.531 7.162   0.36 13.05 ?  18  ILE   A HB   1 
ATOM   466  H  HG12 A ILE   A 1 18  ? 10.268 -8.396  6.506   0.64 14.41 ?  18  ILE   A HG12 1 
ATOM   467  H  HG12 B ILE   A 1 18  ? 10.171 -8.028  6.980   0.36 14.20 ?  18  ILE   A HG12 1 
ATOM   468  H  HG13 A ILE   A 1 18  ? 11.829 -8.546  6.248   0.64 14.41 ?  18  ILE   A HG13 1 
ATOM   469  H  HG13 B ILE   A 1 18  ? 11.722 -8.207  6.684   0.36 14.20 ?  18  ILE   A HG13 1 
ATOM   470  H  HG21 A ILE   A 1 18  ? 9.417  -11.289 6.439   0.64 13.96 ?  18  ILE   A HG21 1 
ATOM   471  H  HG21 B ILE   A 1 18  ? 9.218  -10.866 6.916   0.36 14.08 ?  18  ILE   A HG21 1 
ATOM   472  H  HG22 A ILE   A 1 18  ? 9.716  -11.589 7.970   0.64 13.96 ?  18  ILE   A HG22 1 
ATOM   473  H  HG22 B ILE   A 1 18  ? 9.543  -11.159 8.443   0.36 14.08 ?  18  ILE   A HG22 1 
ATOM   474  H  HG23 A ILE   A 1 18  ? 8.984  -10.243 7.553   0.64 13.96 ?  18  ILE   A HG23 1 
ATOM   475  H  HG23 B ILE   A 1 18  ? 8.878  -9.778  8.023   0.36 14.08 ?  18  ILE   A HG23 1 
ATOM   476  H  HD11 A ILE   A 1 18  ? 10.757 -8.604  4.233   0.64 16.01 ?  18  ILE   A HD11 1 
ATOM   477  H  HD11 B ILE   A 1 18  ? 10.543 -8.169  4.699   0.36 15.76 ?  18  ILE   A HD11 1 
ATOM   478  H  HD12 A ILE   A 1 18  ? 11.358 -10.047 4.516   0.64 16.01 ?  18  ILE   A HD12 1 
ATOM   479  H  HD12 B ILE   A 1 18  ? 11.217 -9.593  4.892   0.36 15.76 ?  18  ILE   A HD12 1 
ATOM   480  H  HD13 A ILE   A 1 18  ? 9.808  -9.775  4.736   0.64 16.01 ?  18  ILE   A HD13 1 
ATOM   481  H  HD13 B ILE   A 1 18  ? 9.667  -9.400  5.183   0.36 15.76 ?  18  ILE   A HD13 1 
ATOM   482  N  N    A LYS   A 1 19  ? 10.665 -7.601  9.138   0.64 11.96 ?  19  LYS   A N    1 
ATOM   483  N  N    B LYS   A 1 19  ? 10.757 -7.326  9.653   0.36 11.90 ?  19  LYS   A N    1 
ATOM   484  C  CA   A LYS   A 1 19  ? 9.846  -6.633  9.861   0.64 12.63 ?  19  LYS   A CA   1 
ATOM   485  C  CA   B LYS   A 1 19  ? 9.993  -6.356  10.423  0.36 13.24 ?  19  LYS   A CA   1 
ATOM   486  C  C    A LYS   A 1 19  ? 9.678  -5.366  9.027   0.64 12.47 ?  19  LYS   A C    1 
ATOM   487  C  C    B LYS   A 1 19  ? 9.759  -5.137  9.548   0.36 13.77 ?  19  LYS   A C    1 
ATOM   488  O  O    A LYS   A 1 19  ? 10.578 -4.982  8.278   0.64 12.17 ?  19  LYS   A O    1 
ATOM   489  O  O    B LYS   A 1 19  ? 10.654 -4.719  8.811   0.36 13.43 ?  19  LYS   A O    1 
ATOM   490  C  CB   A LYS   A 1 19  ? 10.525 -6.275  11.192  0.64 14.05 ?  19  LYS   A CB   1 
ATOM   491  C  CB   B LYS   A 1 19  ? 10.775 -5.946  11.678  0.36 14.10 ?  19  LYS   A CB   1 
ATOM   492  C  CG   A LYS   A 1 19  ? 9.775  -5.296  12.087  0.64 15.30 ?  19  LYS   A CG   1 
ATOM   493  C  CG   B LYS   A 1 19  ? 10.049 -5.060  12.671  0.36 15.25 ?  19  LYS   A CG   1 
ATOM   494  C  CD   A LYS   A 1 19  ? 10.619 -4.994  13.324  0.64 16.96 ?  19  LYS   A CD   1 
ATOM   495  C  CD   B LYS   A 1 19  ? 10.955 -4.810  13.873  0.36 16.28 ?  19  LYS   A CD   1 
ATOM   496  C  CE   A LYS   A 1 19  ? 9.929  -4.060  14.304  0.64 18.25 ?  19  LYS   A CE   1 
ATOM   497  C  CE   B LYS   A 1 19  ? 10.326 -3.900  14.908  0.36 17.03 ?  19  LYS   A CE   1 
ATOM   498  N  NZ   A LYS   A 1 19  ? 10.816 -3.753  15.465  0.64 18.65 ?  19  LYS   A NZ   1 
ATOM   499  N  NZ   B LYS   A 1 19  ? 11.223 -3.753  16.088  0.36 17.62 ?  19  LYS   A NZ   1 
ATOM   500  H  H    A LYS   A 1 19  ? 11.207 -7.250  8.573   0.64 14.36 ?  19  LYS   A H    1 
ATOM   501  H  H    B LYS   A 1 19  ? 11.328 -6.958  9.112   0.36 14.29 ?  19  LYS   A H    1 
ATOM   502  H  HA   A LYS   A 1 19  ? 8.974  -7.023  10.043  0.64 15.16 ?  19  LYS   A HA   1 
ATOM   503  H  HA   B LYS   A 1 19  ? 9.141  -6.727  10.687  0.36 15.90 ?  19  LYS   A HA   1 
ATOM   504  H  HB2  A LYS   A 1 19  ? 10.648 -7.095  11.702  0.64 16.86 ?  19  LYS   A HB2  1 
ATOM   505  H  HB2  B LYS   A 1 19  ? 11.023 -6.748  12.157  0.36 16.93 ?  19  LYS   A HB2  1 
ATOM   506  H  HB3  A LYS   A 1 19  ? 11.390 -5.889  10.995  0.64 16.86 ?  19  LYS   A HB3  1 
ATOM   507  H  HB3  B LYS   A 1 19  ? 11.577 -5.470  11.405  0.36 16.93 ?  19  LYS   A HB3  1 
ATOM   508  H  HG2  A LYS   A 1 19  ? 9.620  -4.468  11.607  0.64 18.37 ?  19  LYS   A HG2  1 
ATOM   509  H  HG2  B LYS   A 1 19  ? 9.837  -4.206  12.264  0.36 18.31 ?  19  LYS   A HG2  1 
ATOM   510  H  HG3  A LYS   A 1 19  ? 8.934  -5.690  12.372  0.64 18.37 ?  19  LYS   A HG3  1 
ATOM   511  H  HG3  B LYS   A 1 19  ? 9.243  -5.502  12.981  0.36 18.31 ?  19  LYS   A HG3  1 
ATOM   512  H  HD2  A LYS   A 1 19  ? 10.809 -5.826  13.786  0.64 20.36 ?  19  LYS   A HD2  1 
ATOM   513  H  HD2  B LYS   A 1 19  ? 11.149 -5.659  14.303  0.36 19.54 ?  19  LYS   A HD2  1 
ATOM   514  H  HD3  A LYS   A 1 19  ? 11.449 -4.576  13.044  0.64 20.36 ?  19  LYS   A HD3  1 
ATOM   515  H  HD3  B LYS   A 1 19  ? 11.778 -4.397  13.570  0.36 19.54 ?  19  LYS   A HD3  1 
ATOM   516  H  HE2  A LYS   A 1 19  ? 9.715  -3.227  13.858  0.64 21.91 ?  19  LYS   A HE2  1 
ATOM   517  H  HE2  B LYS   A 1 19  ? 10.182 -3.023  14.520  0.36 20.45 ?  19  LYS   A HE2  1 
ATOM   518  H  HE3  A LYS   A 1 19  ? 9.124  -4.482  14.640  0.64 21.91 ?  19  LYS   A HE3  1 
ATOM   519  H  HE3  B LYS   A 1 19  ? 9.486  -4.282  15.206  0.36 20.45 ?  19  LYS   A HE3  1 
ATOM   520  H  HZ1  A LYS   A 1 19  ? 10.393 -3.225  16.042  0.64 22.39 ?  19  LYS   A HZ1  1 
ATOM   521  H  HZ1  B LYS   A 1 19  ? 10.847 -3.217  16.691  0.36 21.16 ?  19  LYS   A HZ1  1 
ATOM   522  H  HZ2  A LYS   A 1 19  ? 11.047 -4.508  15.880  0.64 22.39 ?  19  LYS   A HZ2  1 
ATOM   523  H  HZ2  B LYS   A 1 19  ? 11.369 -4.548  16.460  0.36 21.16 ?  19  LYS   A HZ2  1 
ATOM   524  H  HZ3  A LYS   A 1 19  ? 11.555 -3.343  15.185  0.64 22.39 ?  19  LYS   A HZ3  1 
ATOM   525  H  HZ3  B LYS   A 1 19  ? 12.002 -3.404  15.837  0.36 21.16 ?  19  LYS   A HZ3  1 
ATOM   526  N  N    A ASN   A 1 20  ? 8.517  -4.715  9.158   0.64 13.52 ?  20  ASN   A N    1 
ATOM   527  N  N    B ASN   A 1 20  ? 8.555  -4.577  9.618   0.36 15.03 ?  20  ASN   A N    1 
ATOM   528  C  CA   A ASN   A 1 20  ? 8.312  -3.375  8.605   0.64 14.81 ?  20  ASN   A CA   1 
ATOM   529  C  CA   B ASN   A 1 20  ? 8.256  -3.323  8.931   0.36 16.72 ?  20  ASN   A CA   1 
ATOM   530  C  C    A ASN   A 1 20  ? 8.931  -2.377  9.579   0.64 16.25 ?  20  ASN   A C    1 
ATOM   531  C  C    B ASN   A 1 20  ? 8.846  -2.187  9.753   0.36 16.99 ?  20  ASN   A C    1 
ATOM   532  O  O    A ASN   A 1 20  ? 8.415  -2.168  10.681  0.64 17.41 ?  20  ASN   A O    1 
ATOM   533  O  O    B ASN   A 1 20  ? 8.232  -1.713  10.712  0.36 17.45 ?  20  ASN   A O    1 
ATOM   534  C  CB   A ASN   A 1 20  ? 6.817  -3.125  8.387   0.64 15.33 ?  20  ASN   A CB   1 
ATOM   535  C  CB   B ASN   A 1 20  ? 6.753  -3.145  8.774   0.36 18.30 ?  20  ASN   A CB   1 
ATOM   536  C  CG   A ASN   A 1 20  ? 6.493  -1.694  7.951   0.64 16.45 ?  20  ASN   A CG   1 
ATOM   537  C  CG   B ASN   A 1 20  ? 6.374  -1.726  8.412   0.36 19.86 ?  20  ASN   A CG   1 
ATOM   538  O  OD1  A ASN   A 1 20  ? 5.430  -1.165  8.285   0.64 18.20 ?  20  ASN   A OD1  1 
ATOM   539  O  OD1  B ASN   A 1 20  ? 5.683  -1.043  9.169   0.36 20.91 ?  20  ASN   A OD1  1 
ATOM   540  N  ND2  A ASN   A 1 20  ? 7.393  -1.075  7.192   0.64 16.57 ?  20  ASN   A ND2  1 
ATOM   541  N  ND2  B ASN   A 1 20  ? 6.842  -1.266  7.259   0.36 20.25 ?  20  ASN   A ND2  1 
ATOM   542  H  H    A ASN   A 1 20  ? 7.832  -5.048  9.559   0.64 16.23 ?  20  ASN   A H    1 
ATOM   543  H  H    B ASN   A 1 20  ? 7.892  -4.913  10.045  0.36 18.04 ?  20  ASN   A H    1 
ATOM   544  H  HA   A ASN   A 1 20  ? 8.768  -3.316  7.754   0.64 17.78 ?  20  ASN   A HA   1 
ATOM   545  H  HA   B ASN   A 1 20  ? 8.673  -3.319  8.054   0.36 20.08 ?  20  ASN   A HA   1 
ATOM   546  H  HB2  A ASN   A 1 20  ? 6.498  -3.722  7.695   0.64 18.41 ?  20  ASN   A HB2  1 
ATOM   547  H  HB2  B ASN   A 1 20  ? 6.440  -3.732  8.070   0.36 21.97 ?  20  ASN   A HB2  1 
ATOM   548  H  HB3  A ASN   A 1 20  ? 6.351  -3.309  9.219   0.64 18.41 ?  20  ASN   A HB3  1 
ATOM   549  H  HB3  B ASN   A 1 20  ? 6.323  -3.370  9.613   0.36 21.97 ?  20  ASN   A HB3  1 
ATOM   550  H  HD21 A ASN   A 1 20  ? 7.251  -0.270  6.939   0.64 19.89 ?  20  ASN   A HD21 1 
ATOM   551  H  HD21 B ASN   A 1 20  ? 6.654  -0.467  7.009   0.36 24.31 ?  20  ASN   A HD21 1 
ATOM   552  H  HD22 A ASN   A 1 20  ? 8.120  -1.478  6.963   0.64 19.89 ?  20  ASN   A HD22 1 
ATOM   553  H  HD22 B ASN   A 1 20  ? 7.330  -1.771  6.760   0.36 24.31 ?  20  ASN   A HD22 1 
ATOM   554  N  N    A ALA   A 1 21  ? 10.062 -1.788  9.202   0.64 16.38 ?  21  ALA   A N    1 
ATOM   555  N  N    B ALA   A 1 21  ? 10.039 -1.739  9.373   0.36 16.97 ?  21  ALA   A N    1 
ATOM   556  C  CA   A ALA   A 1 21  ? 10.765 -0.919  10.134  0.64 16.49 ?  21  ALA   A CA   1 
ATOM   557  C  CA   B ALA   A 1 21  ? 10.709 -0.706  10.144  0.36 16.85 ?  21  ALA   A CA   1 
ATOM   558  C  C    A ALA   A 1 21  ? 11.713 -0.005  9.380   0.64 15.99 ?  21  ALA   A C    1 
ATOM   559  C  C    B ALA   A 1 21  ? 11.777 -0.049  9.290   0.36 16.06 ?  21  ALA   A C    1 
ATOM   560  O  O    A ALA   A 1 21  ? 12.172 -0.329  8.280   0.64 15.91 ?  21  ALA   A O    1 
ATOM   561  O  O    B ALA   A 1 21  ? 12.318 -0.660  8.364   0.36 15.88 ?  21  ALA   A O    1 
ATOM   562  C  CB   A ALA   A 1 21  ? 11.548 -1.727  11.172  0.64 17.02 ?  21  ALA   A CB   1 
ATOM   563  C  CB   B ALA   A 1 21  ? 11.345 -1.283  11.412  0.36 17.46 ?  21  ALA   A CB   1 
ATOM   564  H  H    A ALA   A 1 21  ? 10.430 -1.876  8.433   0.64 19.67 ?  21  ALA   A H    1 
ATOM   565  H  H    B ALA   A 1 21  ? 10.472 -2.008  8.677   0.36 20.38 ?  21  ALA   A H    1 
ATOM   566  H  HA   A ALA   A 1 21  ? 10.114 -0.369  10.602  0.64 19.79 ?  21  ALA   A HA   1 
ATOM   567  H  HA   B ALA   A 1 21  ? 10.062 -0.033  10.405  0.36 20.22 ?  21  ALA   A HA   1 
ATOM   568  H  HB1  A ALA   A 1 21  ? 11.977 -1.112  11.785  0.64 20.43 ?  21  ALA   A HB1  1 
ATOM   569  H  HB1  B ALA   A 1 21  ? 11.775 -0.565  11.901  0.36 20.96 ?  21  ALA   A HB1  1 
ATOM   570  H  HB2  A ALA   A 1 21  ? 10.928 -2.298  11.658  0.64 20.43 ?  21  ALA   A HB2  1 
ATOM   571  H  HB2  B ALA   A 1 21  ? 10.651 -1.687  11.956  0.36 20.96 ?  21  ALA   A HB2  1 
ATOM   572  H  HB3  A ALA   A 1 21  ? 12.209 -2.267  10.718  0.64 20.43 ?  21  ALA   A HB3  1 
ATOM   573  H  HB3  B ALA   A 1 21  ? 11.999 -1.952  11.159  0.36 20.96 ?  21  ALA   A HB3  1 
ATOM   574  N  N    A ASP   A 1 22  ? 11.991 1.143   9.998   0.64 15.94 ?  22  ASP   A N    1 
ATOM   575  N  N    B ASP   A 1 22  ? 12.055 1.211   9.606   0.36 15.77 ?  22  ASP   A N    1 
ATOM   576  C  CA   A ASP   A 1 22  ? 13.023 2.070   9.547   0.64 15.86 ?  22  ASP   A CA   1 
ATOM   577  C  CA   B ASP   A 1 22  ? 13.222 1.898   9.072   0.36 15.65 ?  22  ASP   A CA   1 
ATOM   578  C  C    A ASP   A 1 22  ? 14.355 1.604   10.123  0.64 14.61 ?  22  ASP   A C    1 
ATOM   579  C  C    B ASP   A 1 22  ? 14.471 1.295   9.708   0.36 14.28 ?  22  ASP   A C    1 
ATOM   580  O  O    A ASP   A 1 22  ? 14.547 1.614   11.342  0.64 15.45 ?  22  ASP   A O    1 
ATOM   581  O  O    B ASP   A 1 22  ? 14.582 1.241   10.937  0.36 14.26 ?  22  ASP   A O    1 
ATOM   582  C  CB   A ASP   A 1 22  ? 12.672 3.473   10.035  0.64 17.26 ?  22  ASP   A CB   1 
ATOM   583  C  CB   B ASP   A 1 22  ? 13.107 3.383   9.418   0.36 16.96 ?  22  ASP   A CB   1 
ATOM   584  C  CG   A ASP   A 1 22  ? 13.687 4.521   9.613   0.64 19.33 ?  22  ASP   A CG   1 
ATOM   585  C  CG   B ASP   A 1 22  ? 14.198 4.229   8.798   0.36 17.55 ?  22  ASP   A CG   1 
ATOM   586  O  OD1  A ASP   A 1 22  ? 14.825 4.171   9.250   0.64 19.91 ?  22  ASP   A OD1  1 
ATOM   587  O  OD1  B ASP   A 1 22  ? 15.187 3.667   8.285   0.36 17.29 ?  22  ASP   A OD1  1 
ATOM   588  O  OD2  A ASP   A 1 22  ? 13.340 5.717   9.656   0.64 20.91 -1 22  ASP   A OD2  1 
ATOM   589  O  OD2  B ASP   A 1 22  ? 14.061 5.471   8.833   0.36 18.58 -1 22  ASP   A OD2  1 
ATOM   590  H  H    A ASP   A 1 22  ? 11.563 1.422   10.696  0.64 19.13 ?  22  ASP   A H    1 
ATOM   591  H  H    B ASP   A 1 22  ? 11.565 1.696   10.126  0.36 18.93 ?  22  ASP   A H    1 
ATOM   592  H  HA   A ASP   A 1 22  ? 13.073 2.068   8.579   0.64 19.05 ?  22  ASP   A HA   1 
ATOM   593  H  HA   B ASP   A 1 22  ? 13.259 1.787   8.105   0.36 18.79 ?  22  ASP   A HA   1 
ATOM   594  H  HB2  A ASP   A 1 22  ? 11.806 3.729   9.677   0.64 20.72 ?  22  ASP   A HB2  1 
ATOM   595  H  HB2  B ASP   A 1 22  ? 12.253 3.716   9.106   0.36 20.36 ?  22  ASP   A HB2  1 
ATOM   596  H  HB3  A ASP   A 1 22  ? 12.638 3.472   11.005  0.64 20.72 ?  22  ASP   A HB3  1 
ATOM   597  H  HB3  B ASP   A 1 22  ? 13.179 3.485   10.376  0.36 20.36 ?  22  ASP   A HB3  1 
ATOM   598  N  N    A ILE   A 1 23  ? 15.276 1.198   9.244   0.64 13.91 ?  23  ILE   A N    1 
ATOM   599  N  N    B ILE   A 1 23  ? 15.402 0.822   8.874   0.36 13.74 ?  23  ILE   A N    1 
ATOM   600  C  CA   A ILE   A 1 23  ? 16.528 0.586   9.685   0.64 13.66 ?  23  ILE   A CA   1 
ATOM   601  C  CA   B ILE   A 1 23  ? 16.620 0.194   9.388   0.36 13.29 ?  23  ILE   A CA   1 
ATOM   602  C  C    A ILE   A 1 23  ? 17.330 1.532   10.568  0.64 13.67 ?  23  ILE   A C    1 
ATOM   603  C  C    B ILE   A 1 23  ? 17.378 1.150   10.295  0.36 13.95 ?  23  ILE   A C    1 
ATOM   604  O  O    A ILE   A 1 23  ? 18.060 1.088   11.462  0.64 14.35 ?  23  ILE   A O    1 
ATOM   605  O  O    B ILE   A 1 23  ? 18.038 0.721   11.251  0.36 13.92 ?  23  ILE   A O    1 
ATOM   606  C  CB   A ILE   A 1 23  ? 17.332 0.082   8.467   0.64 13.43 ?  23  ILE   A CB   1 
ATOM   607  C  CB   B ILE   A 1 23  ? 17.504 -0.353  8.243   0.36 12.67 ?  23  ILE   A CB   1 
ATOM   608  C  CG1  A ILE   A 1 23  ? 18.466 -0.845  8.913   0.64 13.53 ?  23  ILE   A CG1  1 
ATOM   609  C  CG1  B ILE   A 1 23  ? 18.597 -1.269  8.809   0.36 12.45 ?  23  ILE   A CG1  1 
ATOM   610  C  CG2  A ILE   A 1 23  ? 17.851 1.248   7.634   0.64 13.72 ?  23  ILE   A CG2  1 
ATOM   611  C  CG2  B ILE   A 1 23  ? 18.128 0.781   7.440   0.36 12.51 ?  23  ILE   A CG2  1 
ATOM   612  C  CD1  A ILE   A 1 23  ? 19.126 -1.579  7.767   0.64 13.76 ?  23  ILE   A CD1  1 
ATOM   613  C  CD1  B ILE   A 1 23  ? 19.490 -1.912  7.752   0.36 12.28 ?  23  ILE   A CD1  1 
ATOM   614  H  H    A ILE   A 1 23  ? 15.191 1.263   8.397   0.64 16.70 ?  23  ILE   A H    1 
ATOM   615  H  H    B ILE   A 1 23  ? 15.350 0.848   8.027   0.36 16.50 ?  23  ILE   A H    1 
ATOM   616  H  HA   A ILE   A 1 23  ? 16.312 -0.189  10.226  0.64 16.40 ?  23  ILE   A HA   1 
ATOM   617  H  HA   B ILE   A 1 23  ? 16.357 -0.566  9.929   0.36 15.95 ?  23  ILE   A HA   1 
ATOM   618  H  HB   A ILE   A 1 23  ? 16.729 -0.435  7.912   0.64 16.12 ?  23  ILE   A HB   1 
ATOM   619  H  HB   B ILE   A 1 23  ? 16.947 -0.880  7.650   0.36 15.21 ?  23  ILE   A HB   1 
ATOM   620  H  HG12 A ILE   A 1 23  ? 19.147 -0.320  9.360   0.64 16.25 ?  23  ILE   A HG12 1 
ATOM   621  H  HG12 B ILE   A 1 23  ? 19.169 -0.750  9.397   0.36 14.95 ?  23  ILE   A HG12 1 
ATOM   622  H  HG13 A ILE   A 1 23  ? 18.108 -1.510  9.524   0.64 16.25 ?  23  ILE   A HG13 1 
ATOM   623  H  HG13 B ILE   A 1 23  ? 18.177 -1.985  9.313   0.36 14.95 ?  23  ILE   A HG13 1 
ATOM   624  H  HG21 A ILE   A 1 23  ? 18.200 0.906   6.796   0.64 16.47 ?  23  ILE   A HG21 1 
ATOM   625  H  HG21 B ILE   A 1 23  ? 18.498 0.417   6.617   0.36 15.02 ?  23  ILE   A HG21 1 
ATOM   626  H  HG22 A ILE   A 1 23  ? 17.115 1.859   7.456   0.64 16.47 ?  23  ILE   A HG22 1 
ATOM   627  H  HG22 B ILE   A 1 23  ? 17.444 1.433   7.235   0.36 15.02 ?  23  ILE   A HG22 1 
ATOM   628  H  HG23 A ILE   A 1 23  ? 18.548 1.706   8.123   0.64 16.47 ?  23  ILE   A HG23 1 
ATOM   629  H  HG23 B ILE   A 1 23  ? 18.834 1.190   7.964   0.36 15.02 ?  23  ILE   A HG23 1 
ATOM   630  H  HD11 A ILE   A 1 23  ? 19.786 -2.192  8.124   0.64 16.52 ?  23  ILE   A HD11 1 
ATOM   631  H  HD11 B ILE   A 1 23  ? 20.078 -2.554  8.183   0.36 14.74 ?  23  ILE   A HD11 1 
ATOM   632  H  HD12 A ILE   A 1 23  ? 18.447 -2.073  7.278   0.64 16.52 ?  23  ILE   A HD12 1 
ATOM   633  H  HD12 B ILE   A 1 23  ? 18.931 -2.363  7.101   0.36 14.74 ?  23  ILE   A HD12 1 
ATOM   634  H  HD13 A ILE   A 1 23  ? 19.551 -0.935  7.182   0.64 16.52 ?  23  ILE   A HD13 1 
ATOM   635  H  HD13 B ILE   A 1 23  ? 20.015 -1.223  7.319   0.36 14.74 ?  23  ILE   A HD13 1 
ATOM   636  N  N    A VAL   A 1 24  ? 17.210 2.842   10.344  0.64 14.45 ?  24  VAL   A N    1 
ATOM   637  N  N    B VAL   A 1 24  ? 17.296 2.453   10.021  0.36 14.98 ?  24  VAL   A N    1 
ATOM   638  C  CA   A VAL   A 1 24  ? 17.886 3.808   11.207  0.64 15.59 ?  24  VAL   A CA   1 
ATOM   639  C  CA   B VAL   A 1 24  ? 17.966 3.434   10.867  0.36 16.23 ?  24  VAL   A CA   1 
ATOM   640  C  C    A VAL   A 1 24  ? 17.353 3.710   12.630  0.64 16.15 ?  24  VAL   A C    1 
ATOM   641  C  C    B VAL   A 1 24  ? 17.357 3.434   12.262  0.36 17.22 ?  24  VAL   A C    1 
ATOM   642  O  O    A VAL   A 1 24  ? 18.119 3.629   13.599  0.64 16.49 ?  24  VAL   A O    1 
ATOM   643  O  O    B VAL   A 1 24  ? 18.074 3.447   13.269  0.36 17.96 ?  24  VAL   A O    1 
ATOM   644  C  CB   A VAL   A 1 24  ? 17.728 5.231   10.642  0.64 16.33 ?  24  VAL   A CB   1 
ATOM   645  C  CB   B VAL   A 1 24  ? 17.917 4.823   10.203  0.36 16.68 ?  24  VAL   A CB   1 
ATOM   646  C  CG1  A VAL   A 1 24  ? 18.227 6.263   11.646  0.64 16.78 ?  24  VAL   A CG1  1 
ATOM   647  C  CG1  B VAL   A 1 24  ? 18.607 5.856   11.070  0.36 17.53 ?  24  VAL   A CG1  1 
ATOM   648  C  CG2  A VAL   A 1 24  ? 18.465 5.360   9.318   0.64 17.38 ?  24  VAL   A CG2  1 
ATOM   649  C  CG2  B VAL   A 1 24  ? 18.555 4.763   8.824   0.36 16.55 ?  24  VAL   A CG2  1 
ATOM   650  H  H    A VAL   A 1 24  ? 16.748 3.190   9.708   0.64 17.35 ?  24  VAL   A H    1 
ATOM   651  H  H    B VAL   A 1 24  ? 16.854 2.791   9.369   0.36 17.99 ?  24  VAL   A H    1 
ATOM   652  H  HA   A VAL   A 1 24  ? 18.832 3.603   11.227  0.64 18.71 ?  24  VAL   A HA   1 
ATOM   653  H  HA   B VAL   A 1 24  ? 18.897 3.186   10.957  0.36 19.48 ?  24  VAL   A HA   1 
ATOM   654  H  HB   A VAL   A 1 24  ? 16.790 5.406   10.474  0.64 19.61 ?  24  VAL   A HB   1 
ATOM   655  H  HB   B VAL   A 1 24  ? 16.992 5.092   10.093  0.36 20.03 ?  24  VAL   A HB   1 
ATOM   656  H  HG11 A VAL   A 1 24  ? 18.386 7.100   11.182  0.64 20.14 ?  24  VAL   A HG11 1 
ATOM   657  H  HG11 B VAL   A 1 24  ? 18.748 6.662   10.549  0.36 21.05 ?  24  VAL   A HG11 1 
ATOM   658  H  HG12 A VAL   A 1 24  ? 17.555 6.387   12.331  0.64 20.14 ?  24  VAL   A HG12 1 
ATOM   659  H  HG12 B VAL   A 1 24  ? 18.040 6.051   11.831  0.36 21.05 ?  24  VAL   A HG12 1 
ATOM   660  H  HG13 A VAL   A 1 24  ? 19.054 5.943   12.040  0.64 20.14 ?  24  VAL   A HG13 1 
ATOM   661  H  HG13 B VAL   A 1 24  ? 19.458 5.501   11.369  0.36 21.05 ?  24  VAL   A HG13 1 
ATOM   662  H  HG21 A VAL   A 1 24  ? 18.257 6.222   8.920   0.64 20.86 ?  24  VAL   A HG21 1 
ATOM   663  H  HG21 B VAL   A 1 24  ? 18.631 5.663   8.471   0.36 19.87 ?  24  VAL   A HG21 1 
ATOM   664  H  HG22 A VAL   A 1 24  ? 19.421 5.296   9.477   0.64 20.86 ?  24  VAL   A HG22 1 
ATOM   665  H  HG22 B VAL   A 1 24  ? 19.437 4.365   8.903   0.36 19.87 ?  24  VAL   A HG22 1 
ATOM   666  H  HG23 A VAL   A 1 24  ? 18.181 4.648   8.722   0.64 20.86 ?  24  VAL   A HG23 1 
ATOM   667  H  HG23 B VAL   A 1 24  ? 18.001 4.223   8.241   0.36 19.87 ?  24  VAL   A HG23 1 
ATOM   668  N  N    A GLU   A 1 25  ? 16.027 3.735   12.777  0.64 16.76 ?  25  GLU   A N    1 
ATOM   669  N  N    B GLU   A 1 25  ? 16.025 3.396   12.346  0.36 17.69 ?  25  GLU   A N    1 
ATOM   670  C  CA   A GLU   A 1 25  ? 15.440 3.666   14.109  0.64 18.16 ?  25  GLU   A CA   1 
ATOM   671  C  CA   B GLU   A 1 25  ? 15.370 3.357   13.650  0.36 18.72 ?  25  GLU   A CA   1 
ATOM   672  C  C    A GLU   A 1 25  ? 15.676 2.302   14.744  0.64 17.13 ?  25  GLU   A C    1 
ATOM   673  C  C    B GLU   A 1 25  ? 15.616 2.026   14.353  0.36 18.64 ?  25  GLU   A C    1 
ATOM   674  O  O    A GLU   A 1 25  ? 15.909 2.209   15.955  0.64 17.27 ?  25  GLU   A O    1 
ATOM   675  O  O    B GLU   A 1 25  ? 15.796 1.990   15.575  0.36 19.11 ?  25  GLU   A O    1 
ATOM   676  C  CB   A GLU   A 1 25  ? 13.951 4.013   14.043  0.64 20.89 ?  25  GLU   A CB   1 
ATOM   677  C  CB   B GLU   A 1 25  ? 13.873 3.640   13.501  0.36 20.19 ?  25  GLU   A CB   1 
ATOM   678  C  CG   A GLU   A 1 25  ? 13.693 5.472   13.679  0.64 24.06 ?  25  GLU   A CG   1 
ATOM   679  C  CG   B GLU   A 1 25  ? 13.569 5.031   12.956  0.36 22.56 ?  25  GLU   A CG   1 
ATOM   680  C  CD   A GLU   A 1 25  ? 14.507 6.444   14.526  0.64 26.88 ?  25  GLU   A CD   1 
ATOM   681  C  CD   B GLU   A 1 25  ? 14.187 6.133   13.786  0.36 24.78 ?  25  GLU   A CD   1 
ATOM   682  O  OE1  A GLU   A 1 25  ? 14.572 6.258   15.762  0.64 27.70 ?  25  GLU   A OE1  1 
ATOM   683  O  OE1  B GLU   A 1 25  ? 14.227 5.990   15.026  0.36 26.05 ?  25  GLU   A OE1  1 
ATOM   684  O  OE2  A GLU   A 1 25  ? 15.102 7.380   13.953  0.64 28.07 -1 25  GLU   A OE2  1 
ATOM   685  O  OE2  B GLU   A 1 25  ? 14.640 7.137   13.197  0.36 25.60 -1 25  GLU   A OE2  1 
ATOM   686  H  H    A GLU   A 1 25  ? 15.459 3.803   12.132  0.64 20.12 ?  25  GLU   A H    1 
ATOM   687  H  H    B GLU   A 1 25  ? 15.491 3.390   11.675  0.36 21.24 ?  25  GLU   A H    1 
ATOM   688  H  HA   A GLU   A 1 25  ? 15.877 4.317   14.676  0.64 21.81 ?  25  GLU   A HA   1 
ATOM   689  H  HA   B GLU   A 1 25  ? 15.749 4.050   14.209  0.36 22.47 ?  25  GLU   A HA   1 
ATOM   690  H  HB2  A GLU   A 1 25  ? 13.521 3.460   13.368  0.64 25.07 ?  25  GLU   A HB2  1 
ATOM   691  H  HB2  B GLU   A 1 25  ? 13.489 2.995   12.887  0.36 24.23 ?  25  GLU   A HB2  1 
ATOM   692  H  HB3  A GLU   A 1 25  ? 13.543 3.850   14.908  0.64 25.07 ?  25  GLU   A HB3  1 
ATOM   693  H  HB3  B GLU   A 1 25  ? 13.449 3.563   14.370  0.36 24.23 ?  25  GLU   A HB3  1 
ATOM   694  H  HG2  A GLU   A 1 25  ? 13.941 5.612   12.752  0.64 28.88 ?  25  GLU   A HG2  1 
ATOM   695  H  HG2  B GLU   A 1 25  ? 13.926 5.108   12.059  0.36 27.08 ?  25  GLU   A HG2  1 
ATOM   696  H  HG3  A GLU   A 1 25  ? 12.749 5.666   13.804  0.64 28.88 ?  25  GLU   A HG3  1 
ATOM   697  H  HG3  B GLU   A 1 25  ? 12.610 5.170   12.949  0.36 27.08 ?  25  GLU   A HG3  1 
ATOM   698  N  N    A GLU   A 1 26  ? 15.638 1.236   13.942  0.64 17.09 ?  26  GLU   A N    1 
ATOM   699  N  N    B GLU   A 1 26  ? 15.630 0.922   13.602  0.36 18.32 ?  26  GLU   A N    1 
ATOM   700  C  CA   A GLU   A 1 26  ? 15.932 -0.092  14.469  0.64 16.85 ?  26  GLU   A CA   1 
ATOM   701  C  CA   B GLU   A 1 26  ? 15.983 -0.363  14.197  0.36 18.32 ?  26  GLU   A CA   1 
ATOM   702  C  C    A GLU   A 1 26  ? 17.354 -0.159  15.013  0.64 15.94 ?  26  GLU   A C    1 
ATOM   703  C  C    B GLU   A 1 26  ? 17.402 -0.340  14.748  0.36 17.47 ?  26  GLU   A C    1 
ATOM   704  O  O    A GLU   A 1 26  ? 17.583 -0.632  16.131  0.64 16.33 ?  26  GLU   A O    1 
ATOM   705  O  O    B GLU   A 1 26  ? 17.683 -0.943  15.789  0.36 17.30 ?  26  GLU   A O    1 
ATOM   706  C  CB   A GLU   A 1 26  ? 15.734 -1.148  13.380  0.64 18.48 ?  26  GLU   A CB   1 
ATOM   707  C  CB   B GLU   A 1 26  ? 15.837 -1.483  13.167  0.36 19.24 ?  26  GLU   A CB   1 
ATOM   708  C  CG   A GLU   A 1 26  ? 14.322 -1.662  13.227  0.64 21.83 ?  26  GLU   A CG   1 
ATOM   709  C  CG   B GLU   A 1 26  ? 14.411 -1.935  12.941  0.36 20.07 ?  26  GLU   A CG   1 
ATOM   710  C  CD   A GLU   A 1 26  ? 13.883 -2.529  14.398  0.64 23.61 ?  26  GLU   A CD   1 
ATOM   711  C  CD   B GLU   A 1 26  ? 13.738 -2.420  14.205  0.36 20.18 ?  26  GLU   A CD   1 
ATOM   712  O  OE1  A GLU   A 1 26  ? 14.341 -3.690  14.519  0.64 23.51 ?  26  GLU   A OE1  1 
ATOM   713  O  OE1  B GLU   A 1 26  ? 14.335 -3.253  14.917  0.36 20.41 ?  26  GLU   A OE1  1 
ATOM   714  O  OE2  A GLU   A 1 26  ? 13.082 -2.032  15.208  0.64 24.92 -1 26  GLU   A OE2  1 
ATOM   715  O  OE2  B GLU   A 1 26  ? 12.619 -1.947  14.490  0.36 19.12 -1 26  GLU   A OE2  1 
ATOM   716  H  H    A GLU   A 1 26  ? 15.454 1.263   13.101  0.64 20.52 ?  26  GLU   A H    1 
ATOM   717  H  H    B GLU   A 1 26  ? 15.439 0.891   12.765  0.36 21.99 ?  26  GLU   A H    1 
ATOM   718  H  HA   A GLU   A 1 26  ? 15.321 -0.281  15.194  0.64 20.23 ?  26  GLU   A HA   1 
ATOM   719  H  HA   B GLU   A 1 26  ? 15.384 -0.545  14.935  0.36 21.99 ?  26  GLU   A HA   1 
ATOM   720  H  HB2  A GLU   A 1 26  ? 16.000 -0.765  12.528  0.64 22.18 ?  26  GLU   A HB2  1 
ATOM   721  H  HB2  B GLU   A 1 26  ? 16.182 -1.170  12.313  0.36 23.09 ?  26  GLU   A HB2  1 
ATOM   722  H  HB3  A GLU   A 1 26  ? 16.302 -1.905  13.586  0.64 22.18 ?  26  GLU   A HB3  1 
ATOM   723  H  HB3  B GLU   A 1 26  ? 16.351 -2.252  13.462  0.36 23.09 ?  26  GLU   A HB3  1 
ATOM   724  H  HG2  A GLU   A 1 26  ? 13.718 -0.905  13.169  0.64 26.21 ?  26  GLU   A HG2  1 
ATOM   725  H  HG2  B GLU   A 1 26  ? 13.892 -1.191  12.613  0.36 24.09 ?  26  GLU   A HG2  1 
ATOM   726  H  HG3  A GLU   A 1 26  ? 14.266 -2.191  12.415  0.64 26.21 ?  26  GLU   A HG3  1 
ATOM   727  H  HG3  B GLU   A 1 26  ? 14.407 -2.663  12.303  0.36 24.09 ?  26  GLU   A HG3  1 
ATOM   728  N  N    A ALA   A 1 27  ? 18.328 0.314   14.230  0.64 15.50 ?  27  ALA   A N    1 
ATOM   729  N  N    B ALA   A 1 27  ? 18.313 0.346   14.059  0.36 16.80 ?  27  ALA   A N    1 
ATOM   730  C  CA   A ALA   A 1 27  ? 19.719 0.249   14.668  0.64 16.03 ?  27  ALA   A CA   1 
ATOM   731  C  CA   B ALA   A 1 27  ? 19.690 0.414   14.534  0.36 16.81 ?  27  ALA   A CA   1 
ATOM   732  C  C    A ALA   A 1 27  ? 19.932 1.042   15.952  0.64 17.42 ?  27  ALA   A C    1 
ATOM   733  C  C    B ALA   A 1 27  ? 19.788 1.235   15.815  0.36 17.69 ?  27  ALA   A C    1 
ATOM   734  O  O    A ALA   A 1 27  ? 20.618 0.579   16.871  0.64 17.74 ?  27  ALA   A O    1 
ATOM   735  O  O    B ALA   A 1 27  ? 20.443 0.823   16.780  0.36 17.62 ?  27  ALA   A O    1 
ATOM   736  C  CB   A ALA   A 1 27  ? 20.647 0.750   13.558  0.64 15.52 ?  27  ALA   A CB   1 
ATOM   737  C  CB   B ALA   A 1 27  ? 20.590 0.988   13.441  0.36 16.35 ?  27  ALA   A CB   1 
ATOM   738  H  H    A ALA   A 1 27  ? 18.210 0.668   13.455  0.64 18.61 ?  27  ALA   A H    1 
ATOM   739  H  H    B ALA   A 1 27  ? 18.159 0.769   13.326  0.36 20.17 ?  27  ALA   A H    1 
ATOM   740  H  HA   A ALA   A 1 27  ? 19.945 -0.676  14.849  0.64 19.24 ?  27  ALA   A HA   1 
ATOM   741  H  HA   B ALA   A 1 27  ? 19.997 -0.484  14.728  0.36 20.18 ?  27  ALA   A HA   1 
ATOM   742  H  HB1  A ALA   A 1 27  ? 21.568 0.696   13.866  0.64 18.64 ?  27  ALA   A HB1  1 
ATOM   743  H  HB1  B ALA   A 1 27  ? 21.502 1.013   13.768  0.36 19.63 ?  27  ALA   A HB1  1 
ATOM   744  H  HB2  A ALA   A 1 27  ? 20.533 0.188   12.773  0.64 18.64 ?  27  ALA   A HB2  1 
ATOM   745  H  HB2  B ALA   A 1 27  ? 20.536 0.419   12.656  0.36 19.63 ?  27  ALA   A HB2  1 
ATOM   746  H  HB3  A ALA   A 1 27  ? 20.424 1.667   13.343  0.64 18.64 ?  27  ALA   A HB3  1 
ATOM   747  H  HB3  B ALA   A 1 27  ? 20.290 1.883   13.221  0.36 19.63 ?  27  ALA   A HB3  1 
ATOM   748  N  N    A LYS   A 1 28  ? 19.353 2.241   16.039  0.64 19.62 ?  28  LYS   A N    1 
ATOM   749  N  N    B LYS   A 1 28  ? 19.130 2.397   15.850  0.36 19.16 ?  28  LYS   A N    1 
ATOM   750  C  CA   A LYS   A 1 28  ? 19.515 3.045   17.247  0.64 22.04 ?  28  LYS   A CA   1 
ATOM   751  C  CA   B LYS   A 1 28  ? 19.215 3.254   17.029  0.36 20.83 ?  28  LYS   A CA   1 
ATOM   752  C  C    A LYS   A 1 28  ? 18.956 2.326   18.468  0.64 23.18 ?  28  LYS   A C    1 
ATOM   753  C  C    B LYS   A 1 28  ? 18.681 2.566   18.275  0.36 22.00 ?  28  LYS   A C    1 
ATOM   754  O  O    A LYS   A 1 28  ? 19.525 2.417   19.562  0.64 24.42 ?  28  LYS   A O    1 
ATOM   755  O  O    B LYS   A 1 28  ? 19.122 2.875   19.388  0.36 22.21 ?  28  LYS   A O    1 
ATOM   756  C  CB   A LYS   A 1 28  ? 18.873 4.423   17.064  0.64 23.91 ?  28  LYS   A CB   1 
ATOM   757  C  CB   B LYS   A 1 28  ? 18.446 4.554   16.805  0.36 21.81 ?  28  LYS   A CB   1 
ATOM   758  C  CG   A LYS   A 1 28  ? 19.672 5.350   16.158  0.64 25.52 ?  28  LYS   A CG   1 
ATOM   759  C  CG   B LYS   A 1 28  ? 18.983 5.411   15.678  0.36 22.89 ?  28  LYS   A CG   1 
ATOM   760  C  CD   A LYS   A 1 28  ? 19.193 6.792   16.235  0.64 27.67 ?  28  LYS   A CD   1 
ATOM   761  C  CD   B LYS   A 1 28  ? 18.336 6.785   15.679  0.36 24.31 ?  28  LYS   A CD   1 
ATOM   762  C  CE   A LYS   A 1 28  ? 17.883 6.988   15.497  0.64 29.27 ?  28  LYS   A CE   1 
ATOM   763  C  CE   B LYS   A 1 28  ? 18.362 7.417   14.298  0.36 25.32 ?  28  LYS   A CE   1 
ATOM   764  N  NZ   A LYS   A 1 28  ? 17.490 8.423   15.458  0.64 30.15 ?  28  LYS   A NZ   1 
ATOM   765  N  NZ   B LYS   A 1 28  ? 18.002 8.862   14.335  0.36 25.79 ?  28  LYS   A NZ   1 
ATOM   766  H  H    A LYS   A 1 28  ? 18.878 2.603   15.427  0.64 23.55 ?  28  LYS   A H    1 
ATOM   767  H  H    B LYS   A 1 28  ? 18.642 2.707   15.216  0.36 23.01 ?  28  LYS   A H    1 
ATOM   768  H  HA   A LYS   A 1 28  ? 20.459 3.182   17.411  0.64 26.45 ?  28  LYS   A HA   1 
ATOM   769  H  HA   B LYS   A 1 28  ? 20.142 3.476   17.191  0.36 25.01 ?  28  LYS   A HA   1 
ATOM   770  H  HB2  A LYS   A 1 28  ? 17.995 4.314   16.670  0.64 28.71 ?  28  LYS   A HB2  1 
ATOM   771  H  HB2  B LYS   A 1 28  ? 17.523 4.334   16.603  0.36 26.19 ?  28  LYS   A HB2  1 
ATOM   772  H  HB3  A LYS   A 1 28  ? 18.796 4.855   17.929  0.64 28.71 ?  28  LYS   A HB3  1 
ATOM   773  H  HB3  B LYS   A 1 28  ? 18.485 5.076   17.623  0.36 26.19 ?  28  LYS   A HB3  1 
ATOM   774  H  HG2  A LYS   A 1 28  ? 20.605 5.330   16.423  0.64 30.64 ?  28  LYS   A HG2  1 
ATOM   775  H  HG2  B LYS   A 1 28  ? 19.940 5.522   15.789  0.36 27.48 ?  28  LYS   A HG2  1 
ATOM   776  H  HG3  A LYS   A 1 28  ? 19.581 5.053   15.239  0.64 30.64 ?  28  LYS   A HG3  1 
ATOM   777  H  HG3  B LYS   A 1 28  ? 18.793 4.985   14.830  0.36 27.48 ?  28  LYS   A HG3  1 
ATOM   778  H  HD2  A LYS   A 1 28  ? 19.057 7.035   17.164  0.64 33.21 ?  28  LYS   A HD2  1 
ATOM   779  H  HD2  B LYS   A 1 28  ? 17.410 6.702   15.959  0.36 29.18 ?  28  LYS   A HD2  1 
ATOM   780  H  HD3  A LYS   A 1 28  ? 19.858 7.373   15.832  0.64 33.21 ?  28  LYS   A HD3  1 
ATOM   781  H  HD3  B LYS   A 1 28  ? 18.819 7.365   16.288  0.36 29.18 ?  28  LYS   A HD3  1 
ATOM   782  H  HE2  A LYS   A 1 28  ? 17.981 6.674   14.585  0.64 35.13 ?  28  LYS   A HE2  1 
ATOM   783  H  HE2  B LYS   A 1 28  ? 19.251 7.330   13.920  0.36 30.39 ?  28  LYS   A HE2  1 
ATOM   784  H  HE3  A LYS   A 1 28  ? 17.184 6.493   15.950  0.64 35.13 ?  28  LYS   A HE3  1 
ATOM   785  H  HE3  B LYS   A 1 28  ? 17.712 6.964   13.737  0.36 30.39 ?  28  LYS   A HE3  1 
ATOM   786  H  HZ1  A LYS   A 1 28  ? 16.721 8.517   15.021  0.64 36.19 ?  28  LYS   A HZ1  1 
ATOM   787  H  HZ1  B LYS   A 1 28  ? 18.026 9.203   13.513  0.36 30.96 ?  28  LYS   A HZ1  1 
ATOM   788  H  HZ2  A LYS   A 1 28  ? 17.393 8.735   16.286  0.64 36.19 ?  28  LYS   A HZ2  1 
ATOM   789  H  HZ2  B LYS   A 1 28  ? 17.182 8.963   14.666  0.36 30.96 ?  28  LYS   A HZ2  1 
ATOM   790  H  HZ3  A LYS   A 1 28  ? 18.118 8.900   15.043  0.64 36.19 ?  28  LYS   A HZ3  1 
ATOM   791  H  HZ3  B LYS   A 1 28  ? 18.578 9.305   14.849  0.36 30.96 ?  28  LYS   A HZ3  1 
ATOM   792  N  N    A LYS   A 1 29  ? 17.855 1.591   18.299  0.64 23.84 ?  29  LYS   A N    1 
ATOM   793  N  N    B LYS   A 1 29  ? 17.727 1.649   18.120  0.36 23.27 ?  29  LYS   A N    1 
ATOM   794  C  CA   A LYS   A 1 29  ? 17.254 0.877   19.422  0.64 25.50 ?  29  LYS   A CA   1 
ATOM   795  C  CA   B LYS   A 1 29  ? 17.126 0.999   19.277  0.36 25.03 ?  29  LYS   A CA   1 
ATOM   796  C  C    A LYS   A 1 29  ? 18.077 -0.351  19.797  0.64 25.17 ?  29  LYS   A C    1 
ATOM   797  C  C    B LYS   A 1 29  ? 17.888 -0.250  19.694  0.36 24.83 ?  29  LYS   A C    1 
ATOM   798  O  O    A LYS   A 1 29  ? 18.433 -0.541  20.967  0.64 26.08 ?  29  LYS   A O    1 
ATOM   799  O  O    B LYS   A 1 29  ? 18.092 -0.479  20.891  0.36 25.34 ?  29  LYS   A O    1 
ATOM   800  C  CB   A LYS   A 1 29  ? 15.822 0.470   19.066  0.64 28.03 ?  29  LYS   A CB   1 
ATOM   801  C  CB   B LYS   A 1 29  ? 15.677 0.625   18.965  0.36 27.06 ?  29  LYS   A CB   1 
ATOM   802  C  CG   A LYS   A 1 29  ? 15.071 -0.233  20.188  0.64 31.04 ?  29  LYS   A CG   1 
ATOM   803  C  CG   B LYS   A 1 29  ? 14.919 -0.007  20.121  0.36 29.15 ?  29  LYS   A CG   1 
ATOM   804  C  CD   A LYS   A 1 29  ? 14.743 0.726   21.321  0.64 33.94 ?  29  LYS   A CD   1 
ATOM   805  C  CD   B LYS   A 1 29  ? 14.606 1.011   21.203  0.36 31.06 ?  29  LYS   A CD   1 
ATOM   806  C  CE   A LYS   A 1 29  ? 13.853 0.069   22.363  0.64 35.82 ?  29  LYS   A CE   1 
ATOM   807  C  CE   B LYS   A 1 29  ? 13.703 0.425   22.276  0.36 32.36 ?  29  LYS   A CE   1 
ATOM   808  N  NZ   A LYS   A 1 29  ? 13.422 1.035   23.409  0.64 37.04 ?  29  LYS   A NZ   1 
ATOM   809  N  NZ   B LYS   A 1 29  ? 13.390 1.427   23.331  0.36 33.17 ?  29  LYS   A NZ   1 
ATOM   810  H  H    A LYS   A 1 29  ? 17.442 1.486   17.554  0.64 28.61 ?  29  LYS   A H    1 
ATOM   811  H  H    B LYS   A 1 29  ? 17.412 1.379   17.362  0.36 27.93 ?  29  LYS   A H    1 
ATOM   812  H  HA   A LYS   A 1 29  ? 17.216 1.462   20.194  0.64 30.61 ?  29  LYS   A HA   1 
ATOM   813  H  HA   B LYS   A 1 29  ? 17.126 1.617   20.023  0.36 30.05 ?  29  LYS   A HA   1 
ATOM   814  H  HB2  A LYS   A 1 29  ? 15.317 1.266   18.835  0.64 33.64 ?  29  LYS   A HB2  1 
ATOM   815  H  HB2  B LYS   A 1 29  ? 15.205 1.430   18.712  0.36 32.49 ?  29  LYS   A HB2  1 
ATOM   816  H  HB3  A LYS   A 1 29  ? 15.845 -0.134  18.309  0.64 33.64 ?  29  LYS   A HB3  1 
ATOM   817  H  HB3  B LYS   A 1 29  ? 15.674 -0.006  18.232  0.36 32.49 ?  29  LYS   A HB3  1 
ATOM   818  H  HG2  A LYS   A 1 29  ? 14.236 -0.586  19.842  0.64 37.25 ?  29  LYS   A HG2  1 
ATOM   819  H  HG2  B LYS   A 1 29  ? 14.082 -0.364  19.789  0.36 34.99 ?  29  LYS   A HG2  1 
ATOM   820  H  HG3  A LYS   A 1 29  ? 15.614 -0.954  20.546  0.64 37.25 ?  29  LYS   A HG3  1 
ATOM   821  H  HG3  B LYS   A 1 29  ? 15.453 -0.716  20.514  0.36 34.99 ?  29  LYS   A HG3  1 
ATOM   822  H  HD2  A LYS   A 1 29  ? 15.566 1.003   21.755  0.64 40.74 ?  29  LYS   A HD2  1 
ATOM   823  H  HD2  B LYS   A 1 29  ? 15.432 1.297   21.623  0.36 37.28 ?  29  LYS   A HD2  1 
ATOM   824  H  HD3  A LYS   A 1 29  ? 14.276 1.497   20.963  0.64 40.74 ?  29  LYS   A HD3  1 
ATOM   825  H  HD3  B LYS   A 1 29  ? 14.152 1.770   20.805  0.36 37.28 ?  29  LYS   A HD3  1 
ATOM   826  H  HE2  A LYS   A 1 29  ? 13.060 -0.283  21.929  0.64 42.99 ?  29  LYS   A HE2  1 
ATOM   827  H  HE2  B LYS   A 1 29  ? 12.869 0.138   21.871  0.36 38.84 ?  29  LYS   A HE2  1 
ATOM   828  H  HE3  A LYS   A 1 29  ? 14.343 -0.648  22.796  0.64 42.99 ?  29  LYS   A HE3  1 
ATOM   829  H  HE3  B LYS   A 1 29  ? 14.150 -0.329  22.693  0.36 38.84 ?  29  LYS   A HE3  1 
ATOM   830  H  HZ1  A LYS   A 1 29  ? 12.903 0.626   24.005  0.64 44.45 ?  29  LYS   A HZ1  1 
ATOM   831  H  HZ1  B LYS   A 1 29  ? 12.861 1.064   23.948  0.36 39.82 ?  29  LYS   A HZ1  1 
ATOM   832  H  HZ2  A LYS   A 1 29  ? 14.134 1.369   23.826  0.64 44.45 ?  29  LYS   A HZ2  1 
ATOM   833  H  HZ2  B LYS   A 1 29  ? 14.141 1.703   23.720  0.36 39.82 ?  29  LYS   A HZ2  1 
ATOM   834  H  HZ3  A LYS   A 1 29  ? 12.965 1.702   23.037  0.64 44.45 ?  29  LYS   A HZ3  1 
ATOM   835  H  HZ3  B LYS   A 1 29  ? 12.976 2.128   22.971  0.36 39.82 ?  29  LYS   A HZ3  1 
ATOM   836  N  N    A VAL   A 1 30  ? 18.373 -1.204  18.817  0.64 23.77 ?  30  VAL   A N    1 
ATOM   837  N  N    B VAL   A 1 30  ? 18.303 -1.066  18.729  0.36 24.28 ?  30  VAL   A N    1 
ATOM   838  C  CA   A VAL   A 1 30  ? 19.041 -2.471  19.098  0.64 22.93 ?  30  VAL   A CA   1 
ATOM   839  C  CA   B VAL   A 1 30  ? 18.929 -2.346  19.041  0.36 23.80 ?  30  VAL   A CA   1 
ATOM   840  C  C    A VAL   A 1 30  ? 20.537 -2.284  19.319  0.64 21.81 ?  30  VAL   A C    1 
ATOM   841  C  C    B VAL   A 1 30  ? 20.425 -2.197  19.295  0.36 23.22 ?  30  VAL   A C    1 
ATOM   842  O  O    A VAL   A 1 30  ? 21.141 -3.006  20.121  0.64 22.20 ?  30  VAL   A O    1 
ATOM   843  O  O    B VAL   A 1 30  ? 20.985 -2.889  20.149  0.36 23.31 ?  30  VAL   A O    1 
ATOM   844  C  CB   A VAL   A 1 30  ? 18.760 -3.470  17.961  0.64 23.67 ?  30  VAL   A CB   1 
ATOM   845  C  CB   B VAL   A 1 30  ? 18.639 -3.358  17.915  0.36 23.99 ?  30  VAL   A CB   1 
ATOM   846  C  CG1  A VAL   A 1 30  ? 19.553 -4.758  18.158  0.64 24.20 ?  30  VAL   A CG1  1 
ATOM   847  C  CG1  B VAL   A 1 30  ? 19.378 -4.660  18.169  0.36 24.28 ?  30  VAL   A CG1  1 
ATOM   848  C  CG2  A VAL   A 1 30  ? 17.270 -3.767  17.869  0.64 24.12 ?  30  VAL   A CG2  1 
ATOM   849  C  CG2  B VAL   A 1 30  ? 17.140 -3.605  17.794  0.36 24.14 ?  30  VAL   A CG2  1 
ATOM   850  H  H    A VAL   A 1 30  ? 18.184 -1.082  17.987  0.64 28.53 ?  30  VAL   A H    1 
ATOM   851  H  H    B VAL   A 1 30  ? 18.222 -0.905  17.885  0.36 29.15 ?  30  VAL   A H    1 
ATOM   852  H  HA   A VAL   A 1 30  ? 18.664 -2.845  19.909  0.64 27.53 ?  30  VAL   A HA   1 
ATOM   853  H  HA   B VAL   A 1 30  ? 18.523 -2.690  19.848  0.36 28.57 ?  30  VAL   A HA   1 
ATOM   854  H  HB   A VAL   A 1 30  ? 19.038 -3.079  17.119  0.64 28.41 ?  30  VAL   A HB   1 
ATOM   855  H  HB   B VAL   A 1 30  ? 18.952 -2.997  17.071  0.36 28.79 ?  30  VAL   A HB   1 
ATOM   856  H  HG11 A VAL   A 1 30  ? 19.194 -5.443  17.571  0.64 29.05 ?  30  VAL   A HG11 1 
ATOM   857  H  HG11 B VAL   A 1 30  ? 19.000 -5.350  17.603  0.36 29.14 ?  30  VAL   A HG11 1 
ATOM   858  H  HG12 A VAL   A 1 30  ? 20.484 -4.595  17.942  0.64 29.05 ?  30  VAL   A HG12 1 
ATOM   859  H  HG12 B VAL   A 1 30  ? 20.317 -4.538  17.960  0.36 29.14 ?  30  VAL   A HG12 1 
ATOM   860  H  HG13 A VAL   A 1 30  ? 19.470 -5.042  19.082  0.64 29.05 ?  30  VAL   A HG13 1 
ATOM   861  H  HG13 B VAL   A 1 30  ? 19.272 -4.903  19.102  0.36 29.14 ?  30  VAL   A HG13 1 
ATOM   862  H  HG21 A VAL   A 1 30  ? 17.123 -4.431  17.177  0.64 28.95 ?  30  VAL   A HG21 1 
ATOM   863  H  HG21 B VAL   A 1 30  ? 16.984 -4.271  17.106  0.36 28.98 ?  30  VAL   A HG21 1 
ATOM   864  H  HG22 A VAL   A 1 30  ? 16.963 -4.107  18.724  0.64 28.95 ?  30  VAL   A HG22 1 
ATOM   865  H  HG22 B VAL   A 1 30  ? 16.804 -3.926  18.646  0.36 28.98 ?  30  VAL   A HG22 1 
ATOM   866  H  HG23 A VAL   A 1 30  ? 16.800 -2.949  17.649  0.64 28.95 ?  30  VAL   A HG23 1 
ATOM   867  H  HG23 B VAL   A 1 30  ? 16.701 -2.774  17.556  0.36 28.98 ?  30  VAL   A HG23 1 
ATOM   868  N  N    A LYS   A 1 31  ? 21.155 -1.331  18.630  0.64 20.93 ?  31  LYS   A N    1 
ATOM   869  N  N    B LYS   A 1 31  ? 21.085 -1.296  18.577  0.36 22.82 ?  31  LYS   A N    1 
ATOM   870  C  CA   A LYS   A 1 31  ? 22.607 -1.208  18.574  0.64 21.65 ?  31  LYS   A CA   1 
ATOM   871  C  CA   B LYS   A 1 31  ? 22.541 -1.208  18.556  0.36 23.13 ?  31  LYS   A CA   1 
ATOM   872  C  C    A LYS   A 1 31  ? 23.224 -2.566  18.231  0.64 20.24 ?  31  LYS   A C    1 
ATOM   873  C  C    B LYS   A 1 31  ? 23.155 -2.578  18.254  0.36 21.07 ?  31  LYS   A C    1 
ATOM   874  O  O    A LYS   A 1 31  ? 24.013 -3.113  19.010  0.64 21.10 ?  31  LYS   A O    1 
ATOM   875  O  O    B LYS   A 1 31  ? 23.879 -3.140  19.083  0.36 21.56 ?  31  LYS   A O    1 
ATOM   876  C  CB   A LYS   A 1 31  ? 23.184 -0.659  19.871  0.64 26.00 ?  31  LYS   A CB   1 
ATOM   877  C  CB   B LYS   A 1 31  ? 23.096 -0.632  19.851  0.36 26.21 ?  31  LYS   A CB   1 
ATOM   878  C  CG   A LYS   A 1 31  ? 22.514 0.612   20.364  0.64 30.82 ?  31  LYS   A CG   1 
ATOM   879  C  CG   B LYS   A 1 31  ? 22.413 0.648   20.304  0.36 29.53 ?  31  LYS   A CG   1 
ATOM   880  C  CD   A LYS   A 1 31  ? 23.540 1.645   20.801  0.64 34.49 ?  31  LYS   A CD   1 
ATOM   881  C  CD   B LYS   A 1 31  ? 23.421 1.674   20.793  0.36 32.14 ?  31  LYS   A CD   1 
ATOM   882  C  CE   A LYS   A 1 31  ? 22.924 2.685   21.721  0.64 36.87 ?  31  LYS   A CE   1 
ATOM   883  C  CE   B LYS   A 1 31  ? 22.772 2.707   21.700  0.36 33.87 ?  31  LYS   A CE   1 
ATOM   884  N  NZ   A LYS   A 1 31  ? 21.726 3.338   21.125  0.64 38.11 ?  31  LYS   A NZ   1 
ATOM   885  N  NZ   B LYS   A 1 31  ? 21.555 3.317   21.099  0.36 34.84 ?  31  LYS   A NZ   1 
ATOM   886  H  H    A LYS   A 1 31  ? 20.743 -0.733  18.172  0.64 25.12 ?  31  LYS   A H    1 
ATOM   887  H  H    B LYS   A 1 31  ? 20.700 -0.708  18.085  0.36 27.39 ?  31  LYS   A H    1 
ATOM   888  H  HA   A LYS   A 1 31  ? 22.834 -0.587  17.866  0.64 25.99 ?  31  LYS   A HA   1 
ATOM   889  H  HA   B LYS   A 1 31  ? 22.792 -0.606  17.844  0.36 27.76 ?  31  LYS   A HA   1 
ATOM   890  H  HB2  A LYS   A 1 31  ? 23.091 -1.331  20.560  0.64 31.20 ?  31  LYS   A HB2  1 
ATOM   891  H  HB2  B LYS   A 1 31  ? 22.981 -1.288  20.549  0.36 31.46 ?  31  LYS   A HB2  1 
ATOM   892  H  HB3  A LYS   A 1 31  ? 24.125 -0.460  19.731  0.64 31.20 ?  31  LYS   A HB3  1 
ATOM   893  H  HB3  B LYS   A 1 31  ? 24.041 -0.440  19.730  0.36 31.46 ?  31  LYS   A HB3  1 
ATOM   894  H  HG2  A LYS   A 1 31  ? 21.983 0.994   19.648  0.64 37.00 ?  31  LYS   A HG2  1 
ATOM   895  H  HG2  B LYS   A 1 31  ? 21.924 1.032   19.560  0.36 35.45 ?  31  LYS   A HG2  1 
ATOM   896  H  HG3  A LYS   A 1 31  ? 21.951 0.402   21.125  0.64 37.00 ?  31  LYS   A HG3  1 
ATOM   897  H  HG3  B LYS   A 1 31  ? 21.807 0.446   21.035  0.36 35.45 ?  31  LYS   A HG3  1 
ATOM   898  H  HD2  A LYS   A 1 31  ? 24.258 1.202   21.280  0.64 41.40 ?  31  LYS   A HD2  1 
ATOM   899  H  HD2  B LYS   A 1 31  ? 24.119 1.225   21.295  0.36 38.58 ?  31  LYS   A HD2  1 
ATOM   900  H  HD3  A LYS   A 1 31  ? 23.890 2.100   20.018  0.64 41.40 ?  31  LYS   A HD3  1 
ATOM   901  H  HD3  B LYS   A 1 31  ? 23.803 2.136   20.029  0.36 38.58 ?  31  LYS   A HD3  1 
ATOM   902  H  HE2  A LYS   A 1 31  ? 22.652 2.255   22.547  0.64 44.26 ?  31  LYS   A HE2  1 
ATOM   903  H  HE2  B LYS   A 1 31  ? 22.516 2.279   22.531  0.36 40.65 ?  31  LYS   A HE2  1 
ATOM   904  H  HE3  A LYS   A 1 31  ? 23.581 3.374   21.906  0.64 44.26 ?  31  LYS   A HE3  1 
ATOM   905  H  HE3  B LYS   A 1 31  ? 23.408 3.418   21.875  0.36 40.65 ?  31  LYS   A HE3  1 
ATOM   906  H  HZ1  A LYS   A 1 31  ? 21.410 3.958   21.680  0.64 45.74 ?  31  LYS   A HZ1  1 
ATOM   907  H  HZ1  B LYS   A 1 31  ? 21.229 3.943   21.642  0.36 41.82 ?  31  LYS   A HZ1  1 
ATOM   908  H  HZ2  A LYS   A 1 31  ? 21.943 3.725   20.353  0.64 45.74 ?  31  LYS   A HZ2  1 
ATOM   909  H  HZ2  B LYS   A 1 31  ? 21.757 3.689   20.316  0.36 41.82 ?  31  LYS   A HZ2  1 
ATOM   910  H  HZ3  A LYS   A 1 31  ? 21.091 2.732   20.976  0.64 45.74 ?  31  LYS   A HZ3  1 
ATOM   911  H  HZ3  B LYS   A 1 31  ? 20.933 2.693   20.971  0.36 41.82 ?  31  LYS   A HZ3  1 
ATOM   912  N  N    . PRO   A 1 32  ? 22.884 -3.135  17.077  1.00 18.80 ?  32  PRO   A N    1 
ATOM   913  C  CA   . PRO   A 1 32  ? 23.358 -4.480  16.759  1.00 18.16 ?  32  PRO   A CA   1 
ATOM   914  C  C    . PRO   A 1 32  ? 24.858 -4.494  16.550  1.00 17.80 ?  32  PRO   A C    1 
ATOM   915  O  O    . PRO   A 1 32  ? 25.499 -3.463  16.337  1.00 17.75 ?  32  PRO   A O    1 
ATOM   916  C  CB   . PRO   A 1 32  ? 22.637 -4.794  15.444  1.00 18.31 ?  32  PRO   A CB   1 
ATOM   917  C  CG   . PRO   A 1 32  ? 22.497 -3.454  14.796  1.00 17.38 ?  32  PRO   A CG   1 
ATOM   918  C  CD   . PRO   A 1 32  ? 22.180 -2.524  15.939  1.00 17.55 ?  32  PRO   A CD   1 
ATOM   919  H  HA   . PRO   A 1 32  ? 23.103 -5.116  17.446  1.00 21.80 ?  32  PRO   A HA   1 
ATOM   920  H  HB2  . PRO   A 1 32  ? 23.180 -5.394  14.905  1.00 21.98 ?  32  PRO   A HB2  1 
ATOM   921  H  HB3  . PRO   A 1 32  ? 21.768 -5.189  15.629  1.00 21.98 ?  32  PRO   A HB3  1 
ATOM   922  H  HG2  . PRO   A 1 32  ? 23.333 -3.217  14.367  1.00 20.86 ?  32  PRO   A HG2  1 
ATOM   923  H  HG3  . PRO   A 1 32  ? 21.772 -3.484  14.152  1.00 20.86 ?  32  PRO   A HG3  1 
ATOM   924  H  HD2  . PRO   A 1 32  ? 22.534 -1.643  15.743  1.00 21.07 ?  32  PRO   A HD2  1 
ATOM   925  H  HD3  . PRO   A 1 32  ? 21.226 -2.505  16.090  1.00 21.07 ?  32  PRO   A HD3  1 
ATOM   926  N  N    . THR   A 1 33  ? 25.411 -5.703  16.579  1.00 17.69 ?  33  THR   A N    1 
ATOM   927  C  CA   . THR   A 1 33  ? 26.825 -5.860  16.270  1.00 17.82 ?  33  THR   A CA   1 
ATOM   928  C  C    . THR   A 1 33  ? 27.131 -5.406  14.848  1.00 16.33 ?  33  THR   A C    1 
ATOM   929  O  O    . THR   A 1 33  ? 28.161 -4.761  14.603  1.00 16.48 ?  33  THR   A O    1 
ATOM   930  C  CB   . THR   A 1 33  ? 27.234 -7.316  16.473  1.00 19.45 ?  33  THR   A CB   1 
ATOM   931  O  OG1  . THR   A 1 33  ? 26.906 -7.713  17.807  1.00 21.24 ?  33  THR   A OG1  1 
ATOM   932  C  CG2  . THR   A 1 33  ? 28.725 -7.494  16.248  1.00 20.66 ?  33  THR   A CG2  1 
ATOM   933  H  H    . THR   A 1 33  ? 24.993 -6.433  16.765  1.00 21.23 ?  33  THR   A H    1 
ATOM   934  H  HA   . THR   A 1 33  ? 27.343 -5.317  16.884  1.00 21.39 ?  33  THR   A HA   1 
ATOM   935  H  HB   . THR   A 1 33  ? 26.755 -7.883  15.845  1.00 23.35 ?  33  THR   A HB   1 
ATOM   936  H  HG1  . THR   A 1 33  ? 27.323 -7.239  18.364  1.00 25.49 ?  33  THR   A HG1  1 
ATOM   937  H  HG21 . THR   A 1 33  ? 29.000 -8.378  16.535  1.00 24.80 ?  33  THR   A HG21 1 
ATOM   938  H  HG22 . THR   A 1 33  ? 28.932 -7.390  15.307  1.00 24.80 ?  33  THR   A HG22 1 
ATOM   939  H  HG23 . THR   A 1 33  ? 29.215 -6.831  16.757  1.00 24.80 ?  33  THR   A HG23 1 
ATOM   940  N  N    . VAL   A 1 34  ? 26.245 -5.726  13.902  1.00 14.91 ?  34  VAL   A N    1 
ATOM   941  C  CA   . VAL   A 1 34  ? 26.447 -5.404  12.494  1.00 13.73 ?  34  VAL   A CA   1 
ATOM   942  C  C    . VAL   A 1 34  ? 25.149 -4.850  11.921  1.00 12.87 ?  34  VAL   A C    1 
ATOM   943  O  O    . VAL   A 1 34  ? 24.109 -5.521  11.963  1.00 13.75 ?  34  VAL   A O    1 
ATOM   944  C  CB   . VAL   A 1 34  ? 26.896 -6.621  11.667  1.00 14.13 ?  34  VAL   A CB   1 
ATOM   945  C  CG1  . VAL   A 1 34  ? 27.082 -6.226  10.207  1.00 14.41 ?  34  VAL   A CG1  1 
ATOM   946  C  CG2  . VAL   A 1 34  ? 28.174 -7.227  12.239  1.00 15.58 ?  34  VAL   A CG2  1 
ATOM   947  H  H    . VAL   A 1 34  ? 25.503 -6.133  14.060  1.00 17.90 ?  34  VAL   A H    1 
ATOM   948  H  HA   . VAL   A 1 34  ? 27.127 -4.713  12.417  1.00 16.48 ?  34  VAL   A HA   1 
ATOM   949  H  HB   . VAL   A 1 34  ? 26.200 -7.296  11.713  1.00 16.96 ?  34  VAL   A HB   1 
ATOM   950  H  HG11 . VAL   A 1 34  ? 27.575 -6.929  9.758   1.00 17.30 ?  34  VAL   A HG11 1 
ATOM   951  H  HG12 . VAL   A 1 34  ? 26.211 -6.118  9.795   1.00 17.30 ?  34  VAL   A HG12 1 
ATOM   952  H  HG13 . VAL   A 1 34  ? 27.577 -5.395  10.168  1.00 17.30 ?  34  VAL   A HG13 1 
ATOM   953  H  HG21 . VAL   A 1 34  ? 28.447 -7.969  11.679  1.00 18.70 ?  34  VAL   A HG21 1 
ATOM   954  H  HG22 . VAL   A 1 34  ? 28.867 -6.548  12.253  1.00 18.70 ?  34  VAL   A HG22 1 
ATOM   955  H  HG23 . VAL   A 1 34  ? 28.002 -7.540  13.143  1.00 18.70 ?  34  VAL   A HG23 1 
ATOM   956  N  N    . VAL   A 1 35  ? 25.214 -3.639  11.368  1.00 12.06 ?  35  VAL   A N    1 
ATOM   957  C  CA   . VAL   A 1 35  ? 24.185 -3.123  10.474  1.00 11.87 ?  35  VAL   A CA   1 
ATOM   958  C  C    . VAL   A 1 35  ? 24.743 -3.130  9.058   1.00 11.36 ?  35  VAL   A C    1 
ATOM   959  O  O    . VAL   A 1 35  ? 25.893 -2.736  8.829   1.00 11.83 ?  35  VAL   A O    1 
ATOM   960  C  CB   . VAL   A 1 35  ? 23.651 -1.730  10.882  1.00 12.28 ?  35  VAL   A CB   1 
ATOM   961  C  CG1  . VAL   A 1 35  ? 24.719 -0.643  10.769  1.00 12.87 ?  35  VAL   A CG1  1 
ATOM   962  C  CG2  . VAL   A 1 35  ? 22.423 -1.378  10.041  1.00 12.85 ?  35  VAL   A CG2  1 
ATOM   963  H  H    . VAL   A 1 35  ? 25.857 -3.079  11.499  1.00 14.49 ?  35  VAL   A H    1 
ATOM   964  H  HA   . VAL   A 1 35  ? 23.430 -3.735  10.491  1.00 14.26 ?  35  VAL   A HA   1 
ATOM   965  H  HB   . VAL   A 1 35  ? 23.358 -1.767  11.804  1.00 14.75 ?  35  VAL   A HB   1 
ATOM   966  H  HG11 . VAL   A 1 35  ? 24.362 0.186   11.128  1.00 15.45 ?  35  VAL   A HG11 1 
ATOM   967  H  HG12 . VAL   A 1 35  ? 25.496 -0.917  11.275  1.00 15.45 ?  35  VAL   A HG12 1 
ATOM   968  H  HG13 . VAL   A 1 35  ? 24.953 -0.522  9.835   1.00 15.45 ?  35  VAL   A HG13 1 
ATOM   969  H  HG21 . VAL   A 1 35  ? 22.057 -0.536  10.348  1.00 15.43 ?  35  VAL   A HG21 1 
ATOM   970  H  HG22 . VAL   A 1 35  ? 22.689 -1.300  9.107   1.00 15.43 ?  35  VAL   A HG22 1 
ATOM   971  H  HG23 . VAL   A 1 35  ? 21.760 -2.082  10.132  1.00 15.43 ?  35  VAL   A HG23 1 
ATOM   972  N  N    . VAL   A 1 36  ? 23.933 -3.595  8.109   1.00 10.67 ?  36  VAL   A N    1 
ATOM   973  C  CA   . VAL   A 1 36  ? 24.312 -3.615  6.704   1.00 10.16 ?  36  VAL   A CA   1 
ATOM   974  C  C    . VAL   A 1 36  ? 23.853 -2.328  6.036   1.00 10.37 ?  36  VAL   A C    1 
ATOM   975  O  O    . VAL   A 1 36  ? 22.692 -1.920  6.174   1.00 11.11 ?  36  VAL   A O    1 
ATOM   976  C  CB   . VAL   A 1 36  ? 23.710 -4.832  5.988   1.00 10.55 ?  36  VAL   A CB   1 
ATOM   977  C  CG1  . VAL   A 1 36  ? 23.981 -4.761  4.501   1.00 11.16 ?  36  VAL   A CG1  1 
ATOM   978  C  CG2  . VAL   A 1 36  ? 24.252 -6.119  6.575   1.00 11.44 ?  36  VAL   A CG2  1 
ATOM   979  H  H    . VAL   A 1 36  ? 23.142 -3.908  8.258   1.00 12.81 ?  36  VAL   A H    1 
ATOM   980  H  HA   . VAL   A 1 36  ? 25.279 -3.673  6.635   1.00 12.20 ?  36  VAL   A HA   1 
ATOM   981  H  HB   . VAL   A 1 36  ? 22.747 -4.823  6.112   1.00 12.67 ?  36  VAL   A HB   1 
ATOM   982  H  HG11 . VAL   A 1 36  ? 23.841 -5.639  4.112   1.00 13.40 ?  36  VAL   A HG11 1 
ATOM   983  H  HG12 . VAL   A 1 36  ? 23.375 -4.121  4.091   1.00 13.40 ?  36  VAL   A HG12 1 
ATOM   984  H  HG13 . VAL   A 1 36  ? 24.900 -4.483  4.359   1.00 13.40 ?  36  VAL   A HG13 1 
ATOM   985  H  HG21 . VAL   A 1 36  ? 23.864 -6.874  6.096   1.00 13.73 ?  36  VAL   A HG21 1 
ATOM   986  H  HG22 . VAL   A 1 36  ? 25.215 -6.131  6.479   1.00 13.73 ?  36  VAL   A HG22 1 
ATOM   987  H  HG23 . VAL   A 1 36  ? 24.009 -6.169  7.512   1.00 13.73 ?  36  VAL   A HG23 1 
ATOM   988  N  N    . ASN   A 1 37  ? 24.772 -1.695  5.309   1.00 10.02 ?  37  ASN   A N    1 
ATOM   989  C  CA   . ASN   A 1 37  ? 24.454 -0.574  4.444   1.00 9.53  ?  37  ASN   A CA   1 
ATOM   990  C  C    . ASN   A 1 37  ? 24.323 -1.053  3.008   1.00 9.78  ?  37  ASN   A C    1 
ATOM   991  O  O    . ASN   A 1 37  ? 25.114 -1.882  2.536   1.00 10.34 ?  37  ASN   A O    1 
ATOM   992  C  CB   . ASN   A 1 37  ? 25.533 0.505   4.523   1.00 10.22 ?  37  ASN   A CB   1 
ATOM   993  C  CG   . ASN   A 1 37  ? 25.211 1.702   3.667   1.00 10.38 ?  37  ASN   A CG   1 
ATOM   994  O  OD1  . ASN   A 1 37  ? 24.040 2.038   3.478   1.00 10.92 ?  37  ASN   A OD1  1 
ATOM   995  N  ND2  . ASN   A 1 37  ? 26.245 2.357   3.148   1.00 10.63 ?  37  ASN   A ND2  1 
ATOM   996  H  H    . ASN   A 1 37  ? 25.610 -1.900  5.309   1.00 12.04 ?  37  ASN   A H    1 
ATOM   997  H  HA   . ASN   A 1 37  ? 23.614 -0.178  4.721   1.00 11.45 ?  37  ASN   A HA   1 
ATOM   998  H  HB2  . ASN   A 1 37  ? 25.620 0.806   5.443   1.00 12.27 ?  37  ASN   A HB2  1 
ATOM   999  H  HB3  . ASN   A 1 37  ? 26.380 0.134   4.218   1.00 12.27 ?  37  ASN   A HB3  1 
ATOM   1000 H  HD21 . ASN   A 1 37  ? 26.106 3.044   2.650   1.00 12.77 ?  37  ASN   A HD21 1 
ATOM   1001 H  HD22 . ASN   A 1 37  ? 27.042 2.096   3.302   1.00 12.77 ?  37  ASN   A HD22 1 
ATOM   1002 N  N    A ALA   A 1 38  ? 23.309 -0.514  2.325   0.64 9.94  ?  38  ALA   A N    1 
ATOM   1003 N  N    B ALA   A 1 38  ? 23.315 -0.533  2.306   0.36 10.39 ?  38  ALA   A N    1 
ATOM   1004 C  CA   A ALA   A 1 38  ? 23.120 -0.655  0.882   0.64 9.93  ?  38  ALA   A CA   1 
ATOM   1005 C  CA   B ALA   A 1 38  ? 23.160 -0.796  0.874   0.36 11.04 ?  38  ALA   A CA   1 
ATOM   1006 C  C    A ALA   A 1 38  ? 24.044 0.341   0.186   0.64 9.71  ?  38  ALA   A C    1 
ATOM   1007 C  C    B ALA   A 1 38  ? 23.978 0.243   0.108   0.36 10.96 ?  38  ALA   A C    1 
ATOM   1008 O  O    A ALA   A 1 38  ? 23.646 1.441   -0.209  0.64 9.76  ?  38  ALA   A O    1 
ATOM   1009 O  O    B ALA   A 1 38  ? 23.472 1.251   -0.392  0.36 11.04 ?  38  ALA   A O    1 
ATOM   1010 C  CB   A ALA   A 1 38  ? 21.660 -0.401  0.519   0.64 10.46 ?  38  ALA   A CB   1 
ATOM   1011 C  CB   B ALA   A 1 38  ? 21.688 -0.783  0.481   0.36 11.88 ?  38  ALA   A CB   1 
ATOM   1012 H  H    A ALA   A 1 38  ? 22.700 -0.032  2.695   0.64 11.94 ?  38  ALA   A H    1 
ATOM   1013 H  H    B ALA   A 1 38  ? 22.705 -0.024  2.640   0.36 12.47 ?  38  ALA   A H    1 
ATOM   1014 H  HA   A ALA   A 1 38  ? 23.361 -1.549  0.604   0.64 11.92 ?  38  ALA   A HA   1 
ATOM   1015 H  HA   B ALA   A 1 38  ? 23.519 -1.677  0.674   0.36 13.26 ?  38  ALA   A HA   1 
ATOM   1016 H  HB1  A ALA   A 1 38  ? 21.548 -0.500  -0.440  0.64 12.57 ?  38  ALA   A HB1  1 
ATOM   1017 H  HB1  B ALA   A 1 38  ? 21.620 -0.919  -0.476  0.36 14.27 ?  38  ALA   A HB1  1 
ATOM   1018 H  HB2  A ALA   A 1 38  ? 21.103 -1.049  0.983   0.64 12.57 ?  38  ALA   A HB2  1 
ATOM   1019 H  HB2  B ALA   A 1 38  ? 21.226 -1.498  0.950   0.36 14.27 ?  38  ALA   A HB2  1 
ATOM   1020 H  HB3  A ALA   A 1 38  ? 21.414 0.497   0.789   0.64 12.57 ?  38  ALA   A HB3  1 
ATOM   1021 H  HB3  B ALA   A 1 38  ? 21.305 0.073   0.721   0.36 14.27 ?  38  ALA   A HB3  1 
ATOM   1022 N  N    A ALA   A 1 39  ? 25.304 -0.059  0.042   0.64 10.12 ?  39  ALA   A N    1 
ATOM   1023 N  N    B ALA   A 1 39  ? 25.274 -0.025  0.012   0.36 11.11 ?  39  ALA   A N    1 
ATOM   1024 C  CA   A ALA   A 1 39  ? 26.362 0.813   -0.437  0.64 9.72  ?  39  ALA   A CA   1 
ATOM   1025 C  CA   B ALA   A 1 39  ? 26.229 0.944   -0.496  0.36 11.13 ?  39  ALA   A CA   1 
ATOM   1026 C  C    A ALA   A 1 39  ? 26.475 0.775   -1.958  0.64 9.91  ?  39  ALA   A C    1 
ATOM   1027 C  C    B ALA   A 1 39  ? 26.418 0.805   -2.002  0.36 10.67 ?  39  ALA   A C    1 
ATOM   1028 O  O    A ALA   A 1 39  ? 25.945 -0.112  -2.635  0.64 10.66 ?  39  ALA   A O    1 
ATOM   1029 O  O    B ALA   A 1 39  ? 26.055 -0.204  -2.613  0.36 10.95 ?  39  ALA   A O    1 
ATOM   1030 C  CB   A ALA   A 1 39  ? 27.694 0.407   0.199   0.64 10.29 ?  39  ALA   A CB   1 
ATOM   1031 C  CB   B ALA   A 1 39  ? 27.575 0.757   0.201   0.36 12.03 ?  39  ALA   A CB   1 
ATOM   1032 H  H    A ALA   A 1 39  ? 25.570 -0.860  0.221   0.64 12.15 ?  39  ALA   A H    1 
ATOM   1033 H  H    B ALA   A 1 39  ? 25.626 -0.780  0.239   0.36 13.34 ?  39  ALA   A H    1 
ATOM   1034 H  HA   A ALA   A 1 39  ? 26.164 1.724   -0.169  0.64 11.67 ?  39  ALA   A HA   1 
ATOM   1035 H  HA   B ALA   A 1 39  ? 25.903 1.837   -0.302  0.36 13.37 ?  39  ALA   A HA   1 
ATOM   1036 H  HB1  A ALA   A 1 39  ? 28.388 1.004   -0.124  0.64 12.36 ?  39  ALA   A HB1  1 
ATOM   1037 H  HB1  B ALA   A 1 39  ? 28.200 1.411   -0.147  0.36 14.44 ?  39  ALA   A HB1  1 
ATOM   1038 H  HB2  A ALA   A 1 39  ? 27.619 0.489   1.167   0.64 12.36 ?  39  ALA   A HB2  1 
ATOM   1039 H  HB2  B ALA   A 1 39  ? 27.458 0.886   1.156   0.36 14.44 ?  39  ALA   A HB2  1 
ATOM   1040 H  HB3  A ALA   A 1 39  ? 27.896 -0.504  -0.041  0.64 12.36 ?  39  ALA   A HB3  1 
ATOM   1041 H  HB3  B ALA   A 1 39  ? 27.899 -0.140  0.026   0.36 14.44 ?  39  ALA   A HB3  1 
ATOM   1042 N  N    A ASN   A 1 40  ? 27.195 1.762   -2.491  0.64 10.29 ?  40  ASN   A N    1 
ATOM   1043 N  N    B ASN   A 1 40  ? 27.003 1.843   -2.594  0.36 10.46 ?  40  ASN   A N    1 
ATOM   1044 C  CA   A ASN   A 1 40  ? 27.739 1.713   -3.842  0.64 10.58 ?  40  ASN   A CA   1 
ATOM   1045 C  CA   B ASN   A 1 40  ? 27.526 1.783   -3.951  0.36 10.70 ?  40  ASN   A CA   1 
ATOM   1046 C  C    A ASN   A 1 40  ? 29.262 1.618   -3.767  0.64 10.13 ?  40  ASN   A C    1 
ATOM   1047 C  C    B ASN   A 1 40  ? 29.046 1.633   -3.905  0.36 10.48 ?  40  ASN   A C    1 
ATOM   1048 O  O    A ASN   A 1 40  ? 29.857 1.737   -2.694  0.64 10.38 ?  40  ASN   A O    1 
ATOM   1049 O  O    B ASN   A 1 40  ? 29.670 1.690   -2.844  0.36 10.52 ?  40  ASN   A O    1 
ATOM   1050 C  CB   A ASN   A 1 40  ? 27.245 2.883   -4.712  0.64 11.31 ?  40  ASN   A CB   1 
ATOM   1051 C  CB   B ASN   A 1 40  ? 27.120 3.020   -4.759  0.36 11.30 ?  40  ASN   A CB   1 
ATOM   1052 C  CG   A ASN   A 1 40  ? 27.598 4.247   -4.148  0.64 12.16 ?  40  ASN   A CG   1 
ATOM   1053 C  CG   B ASN   A 1 40  ? 27.528 4.317   -4.092  0.36 12.21 ?  40  ASN   A CG   1 
ATOM   1054 O  OD1  A ASN   A 1 40  ? 28.750 4.507   -3.800  0.64 13.06 ?  40  ASN   A OD1  1 
ATOM   1055 O  OD1  B ASN   A 1 40  ? 28.718 4.596   -3.927  0.36 12.52 ?  40  ASN   A OD1  1 
ATOM   1056 N  ND2  A ASN   A 1 40  ? 26.600 5.131   -4.067  0.64 12.54 ?  40  ASN   A ND2  1 
ATOM   1057 N  ND2  B ASN   A 1 40  ? 26.539 5.126   -3.717  0.36 13.16 ?  40  ASN   A ND2  1 
ATOM   1058 H  H    A ASN   A 1 40  ? 27.395 2.481   -2.071  0.64 12.35 ?  40  ASN   A H    1 
ATOM   1059 H  H    B ASN   A 1 40  ? 27.110 2.608   -2.215  0.36 12.56 ?  40  ASN   A H    1 
ATOM   1060 H  HA   A ASN   A 1 40  ? 27.434 0.899   -4.264  0.64 12.70 ?  40  ASN   A HA   1 
ATOM   1061 H  HA   B ASN   A 1 40  ? 27.155 1.001   -4.396  0.36 12.85 ?  40  ASN   A HA   1 
ATOM   1062 H  HB2  A ASN   A 1 40  ? 27.647 2.809   -5.595  0.64 13.58 ?  40  ASN   A HB2  1 
ATOM   1063 H  HB2  B ASN   A 1 40  ? 27.553 2.983   -5.622  0.36 13.57 ?  40  ASN   A HB2  1 
ATOM   1064 H  HB3  A ASN   A 1 40  ? 26.283 2.830   -4.785  0.64 13.58 ?  40  ASN   A HB3  1 
ATOM   1065 H  HB3  B ASN   A 1 40  ? 26.159 3.020   -4.870  0.36 13.57 ?  40  ASN   A HB3  1 
ATOM   1066 H  HD21 A ASN   A 1 40  ? 26.747 5.921   -3.757  0.64 15.05 ?  40  ASN   A HD21 1 
ATOM   1067 H  HD21 B ASN   A 1 40  ? 26.718 5.873   -3.333  0.36 15.80 ?  40  ASN   A HD21 1 
ATOM   1068 H  HD22 A ASN   A 1 40  ? 25.807 4.906   -4.309  0.64 15.05 ?  40  ASN   A HD22 1 
ATOM   1069 H  HD22 B ASN   A 1 40  ? 25.721 4.900   -3.859  0.36 15.80 ?  40  ASN   A HD22 1 
ATOM   1070 N  N    A VAL   A 1 41  ? 29.891 1.338   -4.914  0.64 10.12 ?  41  VAL   A N    1 
ATOM   1071 N  N    B VAL   A 1 41  ? 29.644 1.432   -5.082  0.36 10.72 ?  41  VAL   A N    1 
ATOM   1072 C  CA   A VAL   A 1 41  ? 31.322 1.038   -4.925  0.64 10.83 ?  41  VAL   A CA   1 
ATOM   1073 C  CA   B VAL   A 1 41  ? 31.064 1.094   -5.138  0.36 10.98 ?  41  VAL   A CA   1 
ATOM   1074 C  C    A VAL   A 1 41  ? 32.162 2.206   -4.450  0.64 10.74 ?  41  VAL   A C    1 
ATOM   1075 C  C    B VAL   A 1 41  ? 31.960 2.217   -4.632  0.36 10.99 ?  41  VAL   A C    1 
ATOM   1076 O  O    A VAL   A 1 41  ? 33.295 2.003   -4.000  0.64 11.31 ?  41  VAL   A O    1 
ATOM   1077 O  O    B VAL   A 1 41  ? 33.113 1.962   -4.264  0.36 10.95 ?  41  VAL   A O    1 
ATOM   1078 C  CB   A VAL   A 1 41  ? 31.832 0.536   -6.300  0.64 11.20 ?  41  VAL   A CB   1 
ATOM   1079 C  CB   B VAL   A 1 41  ? 31.484 0.650   -6.556  0.36 11.59 ?  41  VAL   A CB   1 
ATOM   1080 C  CG1  A VAL   A 1 41  ? 31.124 -0.750  -6.711  0.64 11.43 ?  41  VAL   A CG1  1 
ATOM   1081 C  CG1  B VAL   A 1 41  ? 30.769 -0.637  -6.946  0.36 12.58 ?  41  VAL   A CG1  1 
ATOM   1082 C  CG2  A VAL   A 1 41  ? 31.713 1.608   -7.382  0.64 11.64 ?  41  VAL   A CG2  1 
ATOM   1083 C  CG2  B VAL   A 1 41  ? 31.226 1.754   -7.572  0.36 11.60 ?  41  VAL   A CG2  1 
ATOM   1084 H  H    A VAL   A 1 41  ? 29.521 1.311   -5.682  0.64 12.16 ?  41  VAL   A H    1 
ATOM   1085 H  H    B VAL   A 1 41  ? 29.248 1.482   -5.843  0.36 12.88 ?  41  VAL   A H    1 
ATOM   1086 H  HA   A VAL   A 1 41  ? 31.489 0.321   -4.298  0.64 13.00 ?  41  VAL   A HA   1 
ATOM   1087 H  HA   B VAL   A 1 41  ? 31.204 0.332   -4.554  0.36 13.19 ?  41  VAL   A HA   1 
ATOM   1088 H  HB   A VAL   A 1 41  ? 32.776 0.320   -6.219  0.64 13.45 ?  41  VAL   A HB   1 
ATOM   1089 H  HB   B VAL   A 1 41  ? 32.436 0.465   -6.550  0.36 13.92 ?  41  VAL   A HB   1 
ATOM   1090 H  HG11 A VAL   A 1 41  ? 31.468 -1.049  -7.569  0.64 13.72 ?  41  VAL   A HG11 1 
ATOM   1091 H  HG11 B VAL   A 1 41  ? 30.995 -0.856  -7.863  0.36 15.11 ?  41  VAL   A HG11 1 
ATOM   1092 H  HG12 A VAL   A 1 41  ? 31.280 -1.431  -6.038  0.64 13.72 ?  41  VAL   A HG12 1 
ATOM   1093 H  HG12 B VAL   A 1 41  ? 31.056 -1.352  -6.355  0.36 15.11 ?  41  VAL   A HG12 1 
ATOM   1094 H  HG13 A VAL   A 1 41  ? 30.169 -0.576  -6.785  0.64 13.72 ?  41  VAL   A HG13 1 
ATOM   1095 H  HG13 B VAL   A 1 41  ? 29.812 -0.508  -6.864  0.36 15.11 ?  41  VAL   A HG13 1 
ATOM   1096 H  HG21 A VAL   A 1 41  ? 31.929 1.212   -8.246  0.64 13.98 ?  41  VAL   A HG21 1 
ATOM   1097 H  HG21 B VAL   A 1 41  ? 31.523 1.449   -8.444  0.36 13.93 ?  41  VAL   A HG21 1 
ATOM   1098 H  HG22 A VAL   A 1 41  ? 30.809 1.948   -7.392  0.64 13.98 ?  41  VAL   A HG22 1 
ATOM   1099 H  HG22 B VAL   A 1 41  ? 30.278 1.949   -7.595  0.36 13.93 ?  41  VAL   A HG22 1 
ATOM   1100 H  HG23 A VAL   A 1 41  ? 32.339 2.323   -7.188  0.64 13.98 ?  41  VAL   A HG23 1 
ATOM   1101 H  HG23 B VAL   A 1 41  ? 31.723 2.544   -7.311  0.36 13.93 ?  41  VAL   A HG23 1 
ATOM   1102 N  N    A TYR   A 1 42  ? 31.647 3.429   -4.562  0.64 11.18 ?  42  TYR   A N    1 
ATOM   1103 N  N    B TYR   A 1 42  ? 31.473 3.461   -4.625  0.36 11.24 ?  42  TYR   A N    1 
ATOM   1104 C  CA   A TYR   A 1 42  ? 32.358 4.632   -4.148  0.64 11.37 ?  42  TYR   A CA   1 
ATOM   1105 C  CA   B TYR   A 1 42  ? 32.267 4.611   -4.201  0.36 11.48 ?  42  TYR   A CA   1 
ATOM   1106 C  C    A TYR   A 1 42  ? 32.068 5.013   -2.707  0.64 11.07 ?  42  TYR   A C    1 
ATOM   1107 C  C    B TYR   A 1 42  ? 32.051 4.991   -2.743  0.36 11.15 ?  42  TYR   A C    1 
ATOM   1108 O  O    A TYR   A 1 42  ? 32.626 6.006   -2.215  0.64 11.74 ?  42  TYR   A O    1 
ATOM   1109 O  O    B TYR   A 1 42  ? 32.654 5.961   -2.270  0.36 11.62 ?  42  TYR   A O    1 
ATOM   1110 C  CB   A TYR   A 1 42  ? 31.997 5.802   -5.079  0.64 12.27 ?  42  TYR   A CB   1 
ATOM   1111 C  CB   B TYR   A 1 42  ? 31.952 5.823   -5.085  0.36 12.26 ?  42  TYR   A CB   1 
ATOM   1112 C  CG   A TYR   A 1 42  ? 32.216 5.477   -6.544  0.64 12.90 ?  42  TYR   A CG   1 
ATOM   1113 C  CG   B TYR   A 1 42  ? 32.078 5.536   -6.563  0.36 12.62 ?  42  TYR   A CG   1 
ATOM   1114 C  CD1  A TYR   A 1 42  ? 33.491 5.280   -7.043  0.64 13.58 ?  42  TYR   A CD1  1 
ATOM   1115 C  CD1  B TYR   A 1 42  ? 33.318 5.324   -7.143  0.36 12.76 ?  42  TYR   A CD1  1 
ATOM   1116 C  CD2  A TYR   A 1 42  ? 31.145 5.331   -7.416  0.64 14.00 ?  42  TYR   A CD2  1 
ATOM   1117 C  CD2  B TYR   A 1 42  ? 30.955 5.472   -7.375  0.36 13.54 ?  42  TYR   A CD2  1 
ATOM   1118 C  CE1  A TYR   A 1 42  ? 33.699 4.958   -8.372  0.64 13.62 ?  42  TYR   A CE1  1 
ATOM   1119 C  CE1  B TYR   A 1 42  ? 33.440 5.052   -8.491  0.36 12.93 ?  42  TYR   A CE1  1 
ATOM   1120 C  CE2  A TYR   A 1 42  ? 31.346 5.017   -8.752  0.64 14.68 ?  42  TYR   A CE2  1 
ATOM   1121 C  CE2  B TYR   A 1 42  ? 31.066 5.208   -8.727  0.36 13.95 ?  42  TYR   A CE2  1 
ATOM   1122 C  CZ   A TYR   A 1 42  ? 32.628 4.834   -9.224  0.64 14.26 ?  42  TYR   A CZ   1 
ATOM   1123 C  CZ   B TYR   A 1 42  ? 32.312 4.999   -9.280  0.36 13.53 ?  42  TYR   A CZ   1 
ATOM   1124 O  OH   A TYR   A 1 42  ? 32.838 4.512   -10.546 0.64 15.58 ?  42  TYR   A OH   1 
ATOM   1125 O  OH   B TYR   A 1 42  ? 32.431 4.734   -10.625 0.36 13.89 ?  42  TYR   A OH   1 
ATOM   1126 H  H    A TYR   A 1 42  ? 30.867 3.590   -4.885  0.64 13.43 ?  42  TYR   A H    1 
ATOM   1127 H  H    B TYR   A 1 42  ? 30.672 3.667   -4.884  0.36 13.50 ?  42  TYR   A H    1 
ATOM   1128 H  HA   A TYR   A 1 42  ? 33.311 4.482   -4.226  0.64 13.66 ?  42  TYR   A HA   1 
ATOM   1129 H  HA   B TYR   A 1 42  ? 33.202 4.397   -4.321  0.36 13.78 ?  42  TYR   A HA   1 
ATOM   1130 H  HB2  A TYR   A 1 42  ? 31.060 6.030   -4.958  0.64 14.73 ?  42  TYR   A HB2  1 
ATOM   1131 H  HB2  B TYR   A 1 42  ? 31.042 6.114   -4.912  0.36 14.72 ?  42  TYR   A HB2  1 
ATOM   1132 H  HB3  A TYR   A 1 42  ? 32.552 6.569   -4.857  0.64 14.73 ?  42  TYR   A HB3  1 
ATOM   1133 H  HB3  B TYR   A 1 42  ? 32.572 6.538   -4.866  0.36 14.72 ?  42  TYR   A HB3  1 
ATOM   1134 H  HD1  A TYR   A 1 42  ? 34.223 5.364   -6.474  0.64 16.30 ?  42  TYR   A HD1  1 
ATOM   1135 H  HD1  B TYR   A 1 42  ? 34.082 5.358   -6.613  0.36 15.32 ?  42  TYR   A HD1  1 
ATOM   1136 H  HD2  A TYR   A 1 42  ? 30.278 5.459   -7.101  0.64 16.81 ?  42  TYR   A HD2  1 
ATOM   1137 H  HD2  B TYR   A 1 42  ? 30.114 5.615   -7.004  0.36 16.25 ?  42  TYR   A HD2  1 
ATOM   1138 H  HE1  A TYR   A 1 42  ? 34.565 4.839   -8.693  0.64 16.35 ?  42  TYR   A HE1  1 
ATOM   1139 H  HE1  B TYR   A 1 42  ? 34.280 4.911   -8.865  0.36 15.52 ?  42  TYR   A HE1  1 
ATOM   1140 H  HE2  A TYR   A 1 42  ? 30.618 4.932   -9.327  0.64 17.63 ?  42  TYR   A HE2  1 
ATOM   1141 H  HE2  B TYR   A 1 42  ? 30.305 5.168   -9.260  0.36 16.75 ?  42  TYR   A HE2  1 
ATOM   1142 H  HH   A TYR   A 1 42  ? 33.658 4.389   -10.682 0.64 18.71 ?  42  TYR   A HH   1 
ATOM   1143 H  HH   B TYR   A 1 42  ? 31.676 4.727   -10.986 0.36 16.67 ?  42  TYR   A HH   1 
ATOM   1144 N  N    . LEU   A 1 43  ? 31.205 4.250   -2.031  1.00 10.72 ?  43  LEU   A N    1 
ATOM   1145 C  CA   . LEU   A 1 43  ? 30.774 4.588   -0.679  1.00 10.34 ?  43  LEU   A CA   1 
ATOM   1146 C  C    . LEU   A 1 43  ? 30.291 6.033   -0.591  1.00 10.91 ?  43  LEU   A C    1 
ATOM   1147 O  O    . LEU   A 1 43  ? 30.553 6.738   0.385   1.00 12.07 ?  43  LEU   A O    1 
ATOM   1148 C  CB   . LEU   A 1 43  ? 31.821 4.284   0.385   1.00 10.86 ?  43  LEU   A CB   1 
ATOM   1149 C  CG   . LEU   A 1 43  ? 32.306 2.834   0.474   1.00 11.43 ?  43  LEU   A CG   1 
ATOM   1150 C  CD1  . LEU   A 1 43  ? 33.331 2.725   1.584   1.00 12.03 ?  43  LEU   A CD1  1 
ATOM   1151 C  CD2  . LEU   A 1 43  ? 31.172 1.859   0.711   1.00 11.74 ?  43  LEU   A CD2  1 
ATOM   1152 H  H    A LEU   A 1 43  ? 30.862 3.514   -2.329  0.64 12.87 ?  43  LEU   A H    1 
ATOM   1153 H  H    B LEU   A 1 43  ? 30.855 3.513   -2.317  0.36 12.87 ?  43  LEU   A H    1 
ATOM   1154 H  HA   . LEU   A 1 43  ? 30.009 4.027   -0.470  1.00 12.42 ?  43  LEU   A HA   1 
ATOM   1155 H  HB2  . LEU   A 1 43  ? 32.595 4.842   0.221   1.00 13.04 ?  43  LEU   A HB2  1 
ATOM   1156 H  HB3  . LEU   A 1 43  ? 31.440 4.511   1.253   1.00 13.04 ?  43  LEU   A HB3  1 
ATOM   1157 H  HG   . LEU   A 1 43  ? 32.742 2.594   -0.357  1.00 13.73 ?  43  LEU   A HG   1 
ATOM   1158 H  HD11 . LEU   A 1 43  ? 33.644 1.809   1.641   1.00 14.45 ?  43  LEU   A HD11 1 
ATOM   1159 H  HD12 . LEU   A 1 43  ? 34.076 3.316   1.386   1.00 14.45 ?  43  LEU   A HD12 1 
ATOM   1160 H  HD13 . LEU   A 1 43  ? 32.919 2.986   2.424   1.00 14.45 ?  43  LEU   A HD13 1 
ATOM   1161 H  HD21 . LEU   A 1 43  ? 31.546 0.974   0.862   1.00 14.10 ?  43  LEU   A HD21 1 
ATOM   1162 H  HD22 . LEU   A 1 43  ? 30.671 2.142   1.490   1.00 14.10 ?  43  LEU   A HD22 1 
ATOM   1163 H  HD23 . LEU   A 1 43  ? 30.600 1.847   -0.069  1.00 14.10 ?  43  LEU   A HD23 1 
ATOM   1164 N  N    A LYS   A 1 44  ? 29.564 6.470   -1.621  0.64 10.95 ?  44  LYS   A N    1 
ATOM   1165 N  N    B LYS   A 1 44  ? 29.569 6.469   -1.625  0.36 11.34 ?  44  LYS   A N    1 
ATOM   1166 C  CA   A LYS   A 1 44  ? 28.925 7.785   -1.629  0.64 11.29 ?  44  LYS   A CA   1 
ATOM   1167 C  CA   B LYS   A 1 44  ? 28.919 7.779   -1.634  0.36 11.96 ?  44  LYS   A CA   1 
ATOM   1168 C  C    A LYS   A 1 44  ? 27.496 7.600   -1.140  0.64 10.54 ?  44  LYS   A C    1 
ATOM   1169 C  C    B LYS   A 1 44  ? 27.494 7.589   -1.138  0.36 11.05 ?  44  LYS   A C    1 
ATOM   1170 O  O    A LYS   A 1 44  ? 26.636 7.084   -1.858  0.64 11.49 ?  44  LYS   A O    1 
ATOM   1171 O  O    B LYS   A 1 44  ? 26.632 7.073   -1.854  0.36 11.58 ?  44  LYS   A O    1 
ATOM   1172 C  CB   A LYS   A 1 44  ? 28.977 8.407   -3.017  0.64 13.38 ?  44  LYS   A CB   1 
ATOM   1173 C  CB   B LYS   A 1 44  ? 28.965 8.393   -3.029  0.36 14.07 ?  44  LYS   A CB   1 
ATOM   1174 C  CG   A LYS   A 1 44  ? 30.366 8.855   -3.448  0.64 16.48 ?  44  LYS   A CG   1 
ATOM   1175 C  CG   B LYS   A 1 44  ? 30.334 8.927   -3.421  0.36 16.68 ?  44  LYS   A CG   1 
ATOM   1176 C  CD   A LYS   A 1 44  ? 31.023 9.784   -2.434  0.64 21.24 ?  44  LYS   A CD   1 
ATOM   1177 C  CD   B LYS   A 1 44  ? 30.921 9.816   -2.331  0.36 19.93 ?  44  LYS   A CD   1 
ATOM   1178 C  CE   A LYS   A 1 44  ? 32.349 10.309  -2.949  0.64 24.18 ?  44  LYS   A CE   1 
ATOM   1179 C  CE   B LYS   A 1 44  ? 32.247 10.404  -2.751  0.36 21.99 ?  44  LYS   A CE   1 
ATOM   1180 N  NZ   A LYS   A 1 44  ? 33.163 10.898  -1.855  0.64 25.59 ?  44  LYS   A NZ   1 
ATOM   1181 N  NZ   B LYS   A 1 44  ? 33.021 10.902  -1.585  0.36 23.03 ?  44  LYS   A NZ   1 
ATOM   1182 H  H    A LYS   A 1 44  ? 29.424 6.014   -2.339  0.64 13.14 ?  44  LYS   A H    1 
ATOM   1183 H  H    B LYS   A 1 44  ? 29.444 6.015   -2.349  0.36 13.62 ?  44  LYS   A H    1 
ATOM   1184 H  HA   A LYS   A 1 44  ? 29.377 8.362   -0.998  0.64 13.55 ?  44  LYS   A HA   1 
ATOM   1185 H  HA   B LYS   A 1 44  ? 29.359 8.363   -0.998  0.36 14.36 ?  44  LYS   A HA   1 
ATOM   1186 H  HB2  A LYS   A 1 44  ? 28.665 7.758   -3.663  0.64 16.07 ?  44  LYS   A HB2  1 
ATOM   1187 H  HB2  B LYS   A 1 44  ? 28.717 7.717   -3.680  0.36 16.89 ?  44  LYS   A HB2  1 
ATOM   1188 H  HB3  A LYS   A 1 44  ? 28.402 9.187   -3.027  0.64 16.07 ?  44  LYS   A HB3  1 
ATOM   1189 H  HB3  B LYS   A 1 44  ? 28.340 9.133   -3.070  0.36 16.89 ?  44  LYS   A HB3  1 
ATOM   1190 H  HG2  A LYS   A 1 44  ? 30.935 8.076   -3.553  0.64 19.79 ?  44  LYS   A HG2  1 
ATOM   1191 H  HG2  B LYS   A 1 44  ? 30.940 8.183   -3.568  0.36 20.03 ?  44  LYS   A HG2  1 
ATOM   1192 H  HG3  A LYS   A 1 44  ? 30.300 9.334   -4.291  0.64 19.79 ?  44  LYS   A HG3  1 
ATOM   1193 H  HG3  B LYS   A 1 44  ? 30.253 9.457   -4.233  0.36 20.03 ?  44  LYS   A HG3  1 
ATOM   1194 H  HD2  A LYS   A 1 44  ? 30.434 10.536  -2.260  0.64 25.50 ?  44  LYS   A HD2  1 
ATOM   1195 H  HD2  B LYS   A 1 44  ? 30.296 10.535  -2.135  0.36 23.92 ?  44  LYS   A HD2  1 
ATOM   1196 H  HD3  A LYS   A 1 44  ? 31.194 9.294   -1.613  0.64 25.50 ?  44  LYS   A HD3  1 
ATOM   1197 H  HD3  B LYS   A 1 44  ? 31.084 9.286   -1.534  0.36 23.92 ?  44  LYS   A HD3  1 
ATOM   1198 H  HE2  A LYS   A 1 44  ? 32.850 9.576   -3.340  0.64 29.03 ?  44  LYS   A HE2  1 
ATOM   1199 H  HE2  B LYS   A 1 44  ? 32.770 9.716   -3.192  0.36 26.39 ?  44  LYS   A HE2  1 
ATOM   1200 H  HE3  A LYS   A 1 44  ? 32.183 10.995  -3.612  0.64 29.03 ?  44  LYS   A HE3  1 
ATOM   1201 H  HE3  B LYS   A 1 44  ? 32.088 11.144  -3.353  0.36 26.39 ?  44  LYS   A HE3  1 
ATOM   1202 H  HZ1  A LYS   A 1 44  ? 33.933 11.200  -2.180  0.64 30.72 ?  44  LYS   A HZ1  1 
ATOM   1203 H  HZ1  B LYS   A 1 44  ? 33.796 11.241  -1.860  0.36 27.65 ?  44  LYS   A HZ1  1 
ATOM   1204 H  HZ2  A LYS   A 1 44  ? 32.721 11.576  -1.481  0.64 30.72 ?  44  LYS   A HZ2  1 
ATOM   1205 H  HZ2  B LYS   A 1 44  ? 32.561 11.536  -1.163  0.36 27.65 ?  44  LYS   A HZ2  1 
ATOM   1206 H  HZ3  A LYS   A 1 44  ? 33.328 10.284  -1.234  0.64 30.72 ?  44  LYS   A HZ3  1 
ATOM   1207 H  HZ3  B LYS   A 1 44  ? 33.182 10.236  -1.017  0.36 27.65 ?  44  LYS   A HZ3  1 
ATOM   1208 N  N    . HIS   A 1 45  ? 27.254 7.992   0.106   1.00 10.50 ?  45  HIS   A N    1 
ATOM   1209 C  CA   . HIS   A 1 45  ? 26.018 7.652   0.802   1.00 10.71 ?  45  HIS   A CA   1 
ATOM   1210 C  C    . HIS   A 1 45  ? 25.001 8.778   0.633   1.00 11.47 ?  45  HIS   A C    1 
ATOM   1211 O  O    . HIS   A 1 45  ? 24.729 9.553   1.545   1.00 13.33 ?  45  HIS   A O    1 
ATOM   1212 C  CB   . HIS   A 1 45  ? 26.315 7.407   2.271   1.00 10.64 ?  45  HIS   A CB   1 
ATOM   1213 C  CG   . HIS   A 1 45  ? 27.426 6.441   2.507   1.00 10.14 ?  45  HIS   A CG   1 
ATOM   1214 N  ND1  . HIS   A 1 45  ? 27.419 5.153   2.008   1.00 10.64 ?  45  HIS   A ND1  1 
ATOM   1215 C  CD2  . HIS   A 1 45  ? 28.592 6.593   3.179   1.00 10.60 ?  45  HIS   A CD2  1 
ATOM   1216 C  CE1  . HIS   A 1 45  ? 28.535 4.552   2.384   1.00 10.54 ?  45  HIS   A CE1  1 
ATOM   1217 N  NE2  . HIS   A 1 45  ? 29.263 5.401   3.094   1.00 10.67 ?  45  HIS   A NE2  1 
ATOM   1218 H  H    A HIS   A 1 45  ? 27.798 8.463   0.574   0.64 12.61 ?  45  HIS   A H    1 
ATOM   1219 H  H    B HIS   A 1 45  ? 27.801 8.458   0.576   0.36 12.61 ?  45  HIS   A H    1 
ATOM   1220 H  HA   . HIS   A 1 45  ? 25.640 6.843   0.421   1.00 12.86 ?  45  HIS   A HA   1 
ATOM   1221 H  HB2  . HIS   A 1 45  ? 26.548 8.250   2.688   1.00 12.78 ?  45  HIS   A HB2  1 
ATOM   1222 H  HB3  . HIS   A 1 45  ? 25.509 7.051   2.693   1.00 12.78 ?  45  HIS   A HB3  1 
ATOM   1223 H  HD2  . HIS   A 1 45  ? 28.883 7.362   3.616   1.00 12.73 ?  45  HIS   A HD2  1 
ATOM   1224 H  HE1  . HIS   A 1 45  ? 28.767 3.671   2.194   1.00 12.65 ?  45  HIS   A HE1  1 
ATOM   1225 H  HE2  . HIS   A 1 45  ? 30.033 5.234   3.438   1.00 12.81 ?  45  HIS   A HE2  1 
ATOM   1226 N  N    A GLY   A 1 46  ? 24.405 8.827   -0.554  0.64 12.37 ?  46  GLY   A N    1 
ATOM   1227 N  N    B GLY   A 1 46  ? 24.435 8.862   -0.567  0.36 12.06 ?  46  GLY   A N    1 
ATOM   1228 C  CA   A GLY   A 1 46  ? 23.575 9.958   -0.920  0.64 13.39 ?  46  GLY   A CA   1 
ATOM   1229 C  CA   B GLY   A 1 46  ? 23.624 10.018  -0.913  0.36 12.58 ?  46  GLY   A CA   1 
ATOM   1230 C  C    A GLY   A 1 46  ? 22.090 9.797   -0.675  0.64 13.57 ?  46  GLY   A C    1 
ATOM   1231 C  C    B GLY   A 1 46  ? 22.160 9.930   -0.522  0.36 12.36 ?  46  GLY   A C    1 
ATOM   1232 O  O    A GLY   A 1 46  ? 21.412 10.773  -0.328  0.64 14.87 ?  46  GLY   A O    1 
ATOM   1233 O  O    B GLY   A 1 46  ? 21.552 10.938  -0.143  0.36 12.91 ?  46  GLY   A O    1 
ATOM   1234 H  H    A GLY   A 1 46  ? 24.460 8.220   -1.160  0.64 14.86 ?  46  GLY   A H    1 
ATOM   1235 H  H    B GLY   A 1 46  ? 24.498 8.270   -1.188  0.36 14.48 ?  46  GLY   A H    1 
ATOM   1236 H  HA2  A GLY   A 1 46  ? 23.865 10.737  -0.422  0.64 16.08 ?  46  GLY   A HA2  1 
ATOM   1237 H  HA2  B GLY   A 1 46  ? 24.003 10.806  -0.481  0.36 15.10 ?  46  GLY   A HA2  1 
ATOM   1238 H  HA3  A GLY   A 1 46  ? 23.690 10.143  -1.861  0.64 16.08 ?  46  GLY   A HA3  1 
ATOM   1239 H  HA3  B GLY   A 1 46  ? 23.668 10.160  -1.870  0.36 15.10 ?  46  GLY   A HA3  1 
ATOM   1240 N  N    A GLY   A 1 47  ? 21.564 8.591   -0.871  0.64 12.62 ?  47  GLY   A N    1 
ATOM   1241 N  N    B GLY   A 1 47  ? 21.575 8.744   -0.634  0.36 11.78 ?  47  GLY   A N    1 
ATOM   1242 C  CA   A GLY   A 1 47  ? 20.132 8.386   -0.830  0.64 12.00 ?  47  GLY   A CA   1 
ATOM   1243 C  CA   B GLY   A 1 47  ? 20.164 8.569   -0.368  0.36 11.72 ?  47  GLY   A CA   1 
ATOM   1244 C  C    A GLY   A 1 47  ? 19.807 6.965   -0.430  0.64 11.72 ?  47  GLY   A C    1 
ATOM   1245 C  C    B GLY   A 1 47  ? 19.843 7.126   -0.039  0.36 11.28 ?  47  GLY   A C    1 
ATOM   1246 O  O    A GLY   A 1 47  ? 20.697 6.140   -0.211  0.64 12.11 ?  47  GLY   A O    1 
ATOM   1247 O  O    B GLY   A 1 47  ? 20.737 6.292   0.123   0.36 11.00 ?  47  GLY   A O    1 
ATOM   1248 H  H    A GLY   A 1 47  ? 22.017 7.871   -1.021  0.64 15.15 ?  47  GLY   A H    1 
ATOM   1249 H  H    B GLY   A 1 47  ? 21.981 8.032   -0.869  0.36 14.14 ?  47  GLY   A H    1 
ATOM   1250 H  HA2  A GLY   A 1 47  ? 19.724 8.994   -0.194  0.64 14.41 ?  47  GLY   A HA2  1 
ATOM   1251 H  HA2  B GLY   A 1 47  ? 19.899 9.126   0.381   0.36 14.07 ?  47  GLY   A HA2  1 
ATOM   1252 H  HA3  A GLY   A 1 47  ? 19.750 8.545   -1.706  0.64 14.41 ?  47  GLY   A HA3  1 
ATOM   1253 H  HA3  B GLY   A 1 47  ? 19.651 8.839   -1.148  0.36 14.07 ?  47  GLY   A HA3  1 
ATOM   1254 N  N    A GLY   A 1 48  ? 18.512 6.676   -0.349  0.64 11.80 ?  48  GLY   A N    1 
ATOM   1255 N  N    B GLY   A 1 48  ? 18.546 6.839   0.064   0.36 11.82 ?  48  GLY   A N    1 
ATOM   1256 C  CA   A GLY   A 1 48  ? 18.101 5.363   0.086   0.64 12.35 ?  48  GLY   A CA   1 
ATOM   1257 C  CA   B GLY   A 1 48  ? 18.120 5.496   0.407   0.36 11.86 ?  48  GLY   A CA   1 
ATOM   1258 C  C    A GLY   A 1 48  ? 18.594 5.079   1.489   0.64 11.60 ?  48  GLY   A C    1 
ATOM   1259 C  C    B GLY   A 1 48  ? 18.632 5.087   1.776   0.36 11.56 ?  48  GLY   A C    1 
ATOM   1260 O  O    A GLY   A 1 48  ? 18.780 5.984   2.312   0.64 11.89 ?  48  GLY   A O    1 
ATOM   1261 O  O    B GLY   A 1 48  ? 18.766 5.901   2.699   0.36 11.84 ?  48  GLY   A O    1 
ATOM   1262 H  H    A GLY   A 1 48  ? 17.868 7.216   -0.529  0.64 14.17 ?  48  GLY   A H    1 
ATOM   1263 H  H    B GLY   A 1 48  ? 17.901 7.398   -0.055  0.36 14.19 ?  48  GLY   A H    1 
ATOM   1264 H  HA2  A GLY   A 1 48  ? 17.135 5.295   0.076   0.64 14.83 ?  48  GLY   A HA2  1 
ATOM   1265 H  HA2  B GLY   A 1 48  ? 17.150 5.444   0.404   0.36 14.24 ?  48  GLY   A HA2  1 
ATOM   1266 H  HA3  A GLY   A 1 48  ? 18.471 4.691   -0.506  0.64 14.83 ?  48  GLY   A HA3  1 
ATOM   1267 H  HA3  B GLY   A 1 48  ? 18.462 4.864   -0.249  0.36 14.24 ?  48  GLY   A HA3  1 
ATOM   1268 N  N    A VAL   A 1 49  ? 18.814 3.794   1.765   0.64 11.30 ?  49  VAL   A N    1 
ATOM   1269 N  N    B VAL   A 1 49  ? 18.911 3.789   1.910   0.36 11.25 ?  49  VAL   A N    1 
ATOM   1270 C  CA   A VAL   A 1 49  ? 19.306 3.384   3.076   0.64 11.47 ?  49  VAL   A CA   1 
ATOM   1271 C  CA   B VAL   A 1 49  ? 19.497 3.266   3.143   0.36 11.11 ?  49  VAL   A CA   1 
ATOM   1272 C  C    A VAL   A 1 49  ? 20.626 4.074   3.405   0.64 10.55 ?  49  VAL   A C    1 
ATOM   1273 C  C    B VAL   A 1 49  ? 20.779 4.015   3.485   0.36 10.45 ?  49  VAL   A C    1 
ATOM   1274 O  O    A VAL   A 1 49  ? 20.845 4.499   4.543   0.64 10.97 ?  49  VAL   A O    1 
ATOM   1275 O  O    B VAL   A 1 49  ? 20.986 4.435   4.629   0.36 10.77 ?  49  VAL   A O    1 
ATOM   1276 C  CB   A VAL   A 1 49  ? 19.431 1.849   3.134   0.64 12.15 ?  49  VAL   A CB   1 
ATOM   1277 C  CB   B VAL   A 1 49  ? 19.749 1.753   3.013   0.36 11.23 ?  49  VAL   A CB   1 
ATOM   1278 C  CG1  A VAL   A 1 49  ? 20.226 1.422   4.364   0.64 12.46 ?  49  VAL   A CG1  1 
ATOM   1279 C  CG1  B VAL   A 1 49  ? 20.610 1.261   4.172   0.36 10.83 ?  49  VAL   A CG1  1 
ATOM   1280 C  CG2  A VAL   A 1 49  ? 18.048 1.206   3.132   0.64 13.75 ?  49  VAL   A CG2  1 
ATOM   1281 C  CG2  B VAL   A 1 49  ? 18.432 0.984   2.934   0.36 11.75 ?  49  VAL   A CG2  1 
ATOM   1282 H  H    A VAL   A 1 49  ? 18.694 3.145   1.216   0.64 13.57 ?  49  VAL   A H    1 
ATOM   1283 H  H    B VAL   A 1 49  ? 18.771 3.192   1.309   0.36 13.50 ?  49  VAL   A H    1 
ATOM   1284 H  HA   A VAL   A 1 49  ? 18.662 3.647   3.751   0.64 13.78 ?  49  VAL   A HA   1 
ATOM   1285 H  HA   B VAL   A 1 49  ? 18.875 3.400   3.875   0.36 13.34 ?  49  VAL   A HA   1 
ATOM   1286 H  HB   A VAL   A 1 49  ? 19.915 1.539   2.351   0.64 14.59 ?  49  VAL   A HB   1 
ATOM   1287 H  HB   B VAL   A 1 49  ? 20.237 1.584   2.193   0.36 13.48 ?  49  VAL   A HB   1 
ATOM   1288 H  HG11 A VAL   A 1 49  ? 20.057 0.484   4.535   0.64 14.96 ?  49  VAL   A HG11 1 
ATOM   1289 H  HG11 B VAL   A 1 49  ? 20.515 0.299   4.252   0.36 13.01 ?  49  VAL   A HG11 1 
ATOM   1290 H  HG12 A VAL   A 1 49  ? 21.171 1.564   4.201   0.64 14.96 ?  49  VAL   A HG12 1 
ATOM   1291 H  HG12 B VAL   A 1 49  ? 21.540 1.483   3.994   0.36 13.01 ?  49  VAL   A HG12 1 
ATOM   1292 H  HG13 A VAL   A 1 49  ? 19.935 1.953   5.124   0.64 14.96 ?  49  VAL   A HG13 1 
ATOM   1293 H  HG13 B VAL   A 1 49  ? 20.318 1.691   4.990   0.36 13.01 ?  49  VAL   A HG13 1 
ATOM   1294 H  HG21 A VAL   A 1 49  ? 18.151 0.245   3.166   0.64 16.51 ?  49  VAL   A HG21 1 
ATOM   1295 H  HG21 B VAL   A 1 49  ? 18.623 0.040   2.819   0.36 14.10 ?  49  VAL   A HG21 1 
ATOM   1296 H  HG22 A VAL   A 1 49  ? 17.560 1.520   3.907   0.64 16.51 ?  49  VAL   A HG22 1 
ATOM   1297 H  HG22 B VAL   A 1 49  ? 17.936 1.124   3.755   0.36 14.10 ?  49  VAL   A HG22 1 
ATOM   1298 H  HG23 A VAL   A 1 49  ? 17.590 1.466   2.320   0.64 16.51 ?  49  VAL   A HG23 1 
ATOM   1299 H  HG23 B VAL   A 1 49  ? 17.922 1.313   2.178   0.36 14.10 ?  49  VAL   A HG23 1 
ATOM   1300 N  N    A ALA   A 1 50  ? 21.534 4.160   2.431   0.64 10.04 ?  50  ALA   A N    1 
ATOM   1301 N  N    B ALA   A 1 50  ? 21.670 4.165   2.502   0.36 10.12 ?  50  ALA   A N    1 
ATOM   1302 C  CA   A ALA   A 1 50  ? 22.860 4.711   2.699   0.64 10.12 ?  50  ALA   A CA   1 
ATOM   1303 C  CA   B ALA   A 1 50  ? 22.974 4.764   2.773   0.36 9.87  ?  50  ALA   A CA   1 
ATOM   1304 C  C    A ALA   A 1 50  ? 22.779 6.170   3.121   0.64 10.13 ?  50  ALA   A C    1 
ATOM   1305 C  C    B ALA   A 1 50  ? 22.836 6.221   3.189   0.36 9.82  ?  50  ALA   A C    1 
ATOM   1306 O  O    A ALA   A 1 50  ? 23.434 6.589   4.079   0.64 10.66 ?  50  ALA   A O    1 
ATOM   1307 O  O    B ALA   A 1 50  ? 23.431 6.652   4.184   0.36 10.21 ?  50  ALA   A O    1 
ATOM   1308 C  CB   A ALA   A 1 50  ? 23.740 4.568   1.462   0.64 10.05 ?  50  ALA   A CB   1 
ATOM   1309 C  CB   B ALA   A 1 50  ? 23.878 4.630   1.548   0.36 9.96  ?  50  ALA   A CB   1 
ATOM   1310 H  H    A ALA   A 1 50  ? 21.408 3.907   1.620   0.64 12.06 ?  50  ALA   A H    1 
ATOM   1311 H  H    B ALA   A 1 50  ? 21.546 3.930   1.681   0.36 12.16 ?  50  ALA   A H    1 
ATOM   1312 H  HA   A ALA   A 1 50  ? 23.272 4.215   3.425   0.64 12.16 ?  50  ALA   A HA   1 
ATOM   1313 H  HA   B ALA   A 1 50  ? 23.393 4.291   3.505   0.36 11.85 ?  50  ALA   A HA   1 
ATOM   1314 H  HB1  A ALA   A 1 50  ? 24.617 4.940   1.656   0.64 12.07 ?  50  ALA   A HB1  1 
ATOM   1315 H  HB1  B ALA   A 1 50  ? 24.740 5.033   1.743   0.36 11.96 ?  50  ALA   A HB1  1 
ATOM   1316 H  HB2  A ALA   A 1 50  ? 23.820 3.631   1.236   0.64 12.07 ?  50  ALA   A HB2  1 
ATOM   1317 H  HB2  B ALA   A 1 50  ? 23.996 3.688   1.342   0.36 11.96 ?  50  ALA   A HB2  1 
ATOM   1318 H  HB3  A ALA   A 1 50  ? 23.331 5.055   0.729   0.64 12.07 ?  50  ALA   A HB3  1 
ATOM   1319 H  HB3  B ALA   A 1 50  ? 23.467 5.082   0.795   0.36 11.96 ?  50  ALA   A HB3  1 
ATOM   1320 N  N    A GLY   A 1 51  ? 21.993 6.966   2.404   0.64 10.47 ?  51  GLY   A N    1 
ATOM   1321 N  N    B GLY   A 1 51  ? 22.057 6.998   2.439   0.36 10.27 ?  51  GLY   A N    1 
ATOM   1322 C  CA   A GLY   A 1 51  ? 21.842 8.357   2.788   0.64 10.83 ?  51  GLY   A CA   1 
ATOM   1323 C  CA   B GLY   A 1 51  ? 21.855 8.386   2.811   0.36 10.59 ?  51  GLY   A CA   1 
ATOM   1324 C  C    A GLY   A 1 51  ? 21.247 8.504   4.174   0.64 10.66 ?  51  GLY   A C    1 
ATOM   1325 C  C    B GLY   A 1 51  ? 21.232 8.524   4.184   0.36 10.62 ?  51  GLY   A C    1 
ATOM   1326 O  O    A GLY   A 1 51  ? 21.643 9.384   4.942   0.64 11.38 ?  51  GLY   A O    1 
ATOM   1327 O  O    B GLY   A 1 51  ? 21.598 9.414   4.957   0.36 11.01 ?  51  GLY   A O    1 
ATOM   1328 H  H    A GLY   A 1 51  ? 21.557 6.727   1.703   0.64 12.57 ?  51  GLY   A H    1 
ATOM   1329 H  H    B GLY   A 1 51  ? 21.647 6.748   1.724   0.36 12.33 ?  51  GLY   A H    1 
ATOM   1330 H  HA2  A GLY   A 1 51  ? 22.709 8.791   2.777   0.64 13.00 ?  51  GLY   A HA2  1 
ATOM   1331 H  HA2  B GLY   A 1 51  ? 22.708 8.848   2.810   0.36 12.72 ?  51  GLY   A HA2  1 
ATOM   1332 H  HA3  A GLY   A 1 51  ? 21.264 8.803   2.150   0.64 13.00 ?  51  GLY   A HA3  1 
ATOM   1333 H  HA3  B GLY   A 1 51  ? 21.274 8.814   2.162   0.36 12.72 ?  51  GLY   A HA3  1 
ATOM   1334 N  N    . ALA   A 1 52  ? 20.284 7.641   4.511   1.00 10.81 ?  52  ALA   A N    1 
ATOM   1335 C  CA   . ALA   A 1 52  ? 19.633 7.708   5.814   1.00 11.81 ?  52  ALA   A CA   1 
ATOM   1336 C  C    . ALA   A 1 52  ? 20.582 7.301   6.941   1.00 11.03 ?  52  ALA   A C    1 
ATOM   1337 O  O    . ALA   A 1 52  ? 20.654 7.968   7.979   1.00 11.90 ?  52  ALA   A O    1 
ATOM   1338 C  CB   . ALA   A 1 52  ? 18.372 6.842   5.806   1.00 13.15 ?  52  ALA   A CB   1 
ATOM   1339 H  H    A ALA   A 1 52  ? 19.999 7.003   4.000   0.64 12.98 ?  52  ALA   A H    1 
ATOM   1340 H  H    B ALA   A 1 52  ? 20.011 6.998   4.000   0.36 12.98 ?  52  ALA   A H    1 
ATOM   1341 H  HA   . ALA   A 1 52  ? 19.359 8.617   5.974   1.00 14.18 ?  52  ALA   A HA   1 
ATOM   1342 H  HB1  . ALA   A 1 52  ? 17.935 6.912   6.671   1.00 15.78 ?  52  ALA   A HB1  1 
ATOM   1343 H  HB2  . ALA   A 1 52  ? 17.774 7.160   5.110   1.00 15.78 ?  52  ALA   A HB2  1 
ATOM   1344 H  HB3  . ALA   A 1 52  ? 18.616 5.919   5.633   1.00 15.78 ?  52  ALA   A HB3  1 
ATOM   1345 N  N    A LEU   A 1 53  ? 21.316 6.198   6.766   0.64 10.84 ?  53  LEU   A N    1 
ATOM   1346 N  N    B LEU   A 1 53  ? 21.313 6.195   6.759   0.36 10.83 ?  53  LEU   A N    1 
ATOM   1347 C  CA   A LEU   A 1 53  ? 22.281 5.803   7.791   0.64 11.09 ?  53  LEU   A CA   1 
ATOM   1348 C  CA   B LEU   A 1 53  ? 22.293 5.787   7.762   0.36 10.88 ?  53  LEU   A CA   1 
ATOM   1349 C  C    A LEU   A 1 53  ? 23.340 6.877   7.976   0.64 10.39 ?  53  LEU   A C    1 
ATOM   1350 C  C    B LEU   A 1 53  ? 23.320 6.888   7.983   0.36 10.60 ?  53  LEU   A C    1 
ATOM   1351 O  O    A LEU   A 1 53  ? 23.692 7.227   9.106   0.64 11.61 ?  53  LEU   A O    1 
ATOM   1352 O  O    B LEU   A 1 53  ? 23.598 7.278   9.121   0.36 11.26 ?  53  LEU   A O    1 
ATOM   1353 C  CB   A LEU   A 1 53  ? 22.941 4.468   7.432   0.64 11.29 ?  53  LEU   A CB   1 
ATOM   1354 C  CB   B LEU   A 1 53  ? 22.994 4.487   7.340   0.36 10.67 ?  53  LEU   A CB   1 
ATOM   1355 C  CG   A LEU   A 1 53  ? 22.020 3.245   7.456   0.64 11.96 ?  53  LEU   A CG   1 
ATOM   1356 C  CG   B LEU   A 1 53  ? 22.279 3.135   7.463   0.36 10.53 ?  53  LEU   A CG   1 
ATOM   1357 C  CD1  A LEU   A 1 53  ? 22.742 2.042   6.889   0.64 12.32 ?  53  LEU   A CD1  1 
ATOM   1358 C  CD1  B LEU   A 1 53  ? 23.145 2.047   6.839   0.36 10.80 ?  53  LEU   A CD1  1 
ATOM   1359 C  CD2  A LEU   A 1 53  ? 21.520 2.955   8.864   0.64 12.94 ?  53  LEU   A CD2  1 
ATOM   1360 C  CD2  B LEU   A 1 53  ? 21.955 2.782   8.909   0.36 10.54 ?  53  LEU   A CD2  1 
ATOM   1361 H  H    A LEU   A 1 53  ? 21.280 5.673   6.082   0.64 13.01 ?  53  LEU   A H    1 
ATOM   1362 H  H    B LEU   A 1 53  ? 21.269 5.677   6.072   0.36 13.01 ?  53  LEU   A H    1 
ATOM   1363 H  HA   A LEU   A 1 53  ? 21.817 5.687   8.634   0.64 13.32 ?  53  LEU   A HA   1 
ATOM   1364 H  HA   B LEU   A 1 53  ? 21.840 5.625   8.602   0.36 13.07 ?  53  LEU   A HA   1 
ATOM   1365 H  HB2  A LEU   A 1 53  ? 23.311 4.538   6.536   0.64 13.56 ?  53  LEU   A HB2  1 
ATOM   1366 H  HB2  B LEU   A 1 53  ? 23.235 4.577   6.407   0.36 12.81 ?  53  LEU   A HB2  1 
ATOM   1367 H  HB3  A LEU   A 1 53  ? 23.661 4.299   8.063   0.64 13.56 ?  53  LEU   A HB3  1 
ATOM   1368 H  HB3  B LEU   A 1 53  ? 23.803 4.409   7.866   0.36 12.81 ?  53  LEU   A HB3  1 
ATOM   1369 H  HG   A LEU   A 1 53  ? 21.249 3.422   6.891   0.64 14.36 ?  53  LEU   A HG   1 
ATOM   1370 H  HG   B LEU   A 1 53  ? 21.445 3.165   6.968   0.36 12.65 ?  53  LEU   A HG   1 
ATOM   1371 H  HD11 A LEU   A 1 53  ? 22.145 1.278   6.910   0.64 14.79 ?  53  LEU   A HD11 1 
ATOM   1372 H  HD11 B LEU   A 1 53  ? 22.691 1.192   6.923   0.36 12.97 ?  53  LEU   A HD11 1 
ATOM   1373 H  HD12 A LEU   A 1 53  ? 23.005 2.233   5.975   0.64 14.79 ?  53  LEU   A HD12 1 
ATOM   1374 H  HD12 B LEU   A 1 53  ? 23.287 2.254   5.903   0.36 12.97 ?  53  LEU   A HD12 1 
ATOM   1375 H  HD13 A LEU   A 1 53  ? 23.527 1.865   7.430   0.64 14.79 ?  53  LEU   A HD13 1 
ATOM   1376 H  HD13 B LEU   A 1 53  ? 23.996 2.015   7.304   0.36 12.97 ?  53  LEU   A HD13 1 
ATOM   1377 H  HD21 A LEU   A 1 53  ? 21.016 2.128   8.856   0.64 15.53 ?  53  LEU   A HD21 1 
ATOM   1378 H  HD21 B LEU   A 1 53  ? 21.415 1.975   8.927   0.36 12.66 ?  53  LEU   A HD21 1 
ATOM   1379 H  HD22 A LEU   A 1 53  ? 22.283 2.875   9.457   0.64 15.53 ?  53  LEU   A HD22 1 
ATOM   1380 H  HD22 B LEU   A 1 53  ? 22.782 2.638   9.393   0.36 12.66 ?  53  LEU   A HD22 1 
ATOM   1381 H  HD23 A LEU   A 1 53  ? 20.952 3.686   9.155   0.64 15.53 ?  53  LEU   A HD23 1 
ATOM   1382 H  HD23 B LEU   A 1 53  ? 21.461 3.515   9.309   0.36 12.66 ?  53  LEU   A HD23 1 
ATOM   1383 N  N    A ASN   A 1 54  ? 23.859 7.411   6.878   0.64 10.32 ?  54  ASN   A N    1 
ATOM   1384 N  N    B ASN   A 1 54  ? 23.883 7.415   6.897   0.36 10.64 ?  54  ASN   A N    1 
ATOM   1385 C  CA   A ASN   A 1 54  ? 24.910 8.407   7.005   0.64 10.46 ?  54  ASN   A CA   1 
ATOM   1386 C  CA   B ASN   A 1 54  ? 24.925 8.421   7.043   0.36 10.62 ?  54  ASN   A CA   1 
ATOM   1387 C  C    A ASN   A 1 54  ? 24.398 9.656   7.723   0.64 10.82 ?  54  ASN   A C    1 
ATOM   1388 C  C    B ASN   A 1 54  ? 24.395 9.667   7.743   0.36 10.73 ?  54  ASN   A C    1 
ATOM   1389 O  O    A ASN   A 1 54  ? 25.089 10.215  8.586   0.64 11.58 ?  54  ASN   A O    1 
ATOM   1390 O  O    B ASN   A 1 54  ? 25.073 10.240  8.607   0.36 10.97 ?  54  ASN   A O    1 
ATOM   1391 C  CB   A ASN   A 1 54  ? 25.466 8.755   5.634   0.64 10.58 ?  54  ASN   A CB   1 
ATOM   1392 C  CB   B ASN   A 1 54  ? 25.511 8.782   5.685   0.36 10.63 ?  54  ASN   A CB   1 
ATOM   1393 C  CG   A ASN   A 1 54  ? 26.504 9.830   5.721   0.64 11.19 ?  54  ASN   A CG   1 
ATOM   1394 C  CG   B ASN   A 1 54  ? 26.475 9.937   5.783   0.36 10.33 ?  54  ASN   A CG   1 
ATOM   1395 O  OD1  A ASN   A 1 54  ? 27.498 9.675   6.436   0.64 11.71 ?  54  ASN   A OD1  1 
ATOM   1396 O  OD1  B ASN   A 1 54  ? 27.513 9.831   6.440   0.36 10.14 ?  54  ASN   A OD1  1 
ATOM   1397 N  ND2  A ASN   A 1 54  ? 26.283 10.937  5.031   0.64 11.95 ?  54  ASN   A ND2  1 
ATOM   1398 N  ND2  B ASN   A 1 54  ? 26.131 11.059  5.167   0.36 10.88 ?  54  ASN   A ND2  1 
ATOM   1399 H  H    A ASN   A 1 54  ? 23.619 7.222   6.074   0.64 12.39 ?  54  ASN   A H    1 
ATOM   1400 H  H    B ASN   A 1 54  ? 23.673 7.217   6.086   0.36 12.77 ?  54  ASN   A H    1 
ATOM   1401 H  HA   A ASN   A 1 54  ? 25.624 8.035   7.536   0.64 12.56 ?  54  ASN   A HA   1 
ATOM   1402 H  HA   B ASN   A 1 54  ? 25.635 8.057   7.586   0.36 12.76 ?  54  ASN   A HA   1 
ATOM   1403 H  HB2  A ASN   A 1 54  ? 25.881 7.961   5.253   0.64 12.70 ?  54  ASN   A HB2  1 
ATOM   1404 H  HB2  B ASN   A 1 54  ? 25.990 8.010   5.330   0.36 12.77 ?  54  ASN   A HB2  1 
ATOM   1405 H  HB3  A ASN   A 1 54  ? 24.750 9.066   5.064   0.64 12.70 ?  54  ASN   A HB3  1 
ATOM   1406 H  HB3  B ASN   A 1 54  ? 24.796 9.032   5.079   0.36 12.77 ?  54  ASN   A HB3  1 
ATOM   1407 H  HD21 A ASN   A 1 54  ? 26.847 11.582  5.063   0.64 14.35 ?  54  ASN   A HD21 1 
ATOM   1408 H  HD21 B ASN   A 1 54  ? 26.651 11.742  5.200   0.36 13.07 ?  54  ASN   A HD21 1 
ATOM   1409 H  HD22 A ASN   A 1 54  ? 25.573 11.007  4.551   0.64 14.35 ?  54  ASN   A HD22 1 
ATOM   1410 H  HD22 B ASN   A 1 54  ? 25.392 11.098  4.730   0.36 13.07 ?  54  ASN   A HD22 1 
ATOM   1411 N  N    . LYS   A 1 55  ? 23.188 10.109  7.379   1.00 11.08 ?  55  LYS   A N    1 
ATOM   1412 C  CA   . LYS   A 1 55  ? 22.605 11.269  8.042   1.00 11.93 ?  55  LYS   A CA   1 
ATOM   1413 C  C    . LYS   A 1 55  ? 22.513 11.039  9.544   1.00 11.86 ?  55  LYS   A C    1 
ATOM   1414 O  O    . LYS   A 1 55  ? 22.797 11.943  10.340  1.00 12.69 ?  55  LYS   A O    1 
ATOM   1415 C  CB   . LYS   A 1 55  ? 21.229 11.558  7.435   1.00 12.88 ?  55  LYS   A CB   1 
ATOM   1416 C  CG   . LYS   A 1 55  ? 20.485 12.733  8.046   1.00 14.43 ?  55  LYS   A CG   1 
ATOM   1417 C  CD   . LYS   A 1 55  ? 19.149 12.942  7.339   1.00 16.14 ?  55  LYS   A CD   1 
ATOM   1418 C  CE   . LYS   A 1 55  ? 18.320 14.037  7.984   1.00 18.41 ?  55  LYS   A CE   1 
ATOM   1419 N  NZ   . LYS   A 1 55  ? 16.968 14.136  7.359   1.00 19.40 ?  55  LYS   A NZ   1 
ATOM   1420 H  H    A LYS   A 1 55  ? 22.682 9.756   6.775   0.64 13.31 ?  55  LYS   A H    1 
ATOM   1421 H  H    B LYS   A 1 55  ? 22.687 9.752   6.773   0.36 13.31 ?  55  LYS   A H    1 
ATOM   1422 H  HA   . LYS   A 1 55  ? 23.168 12.040  7.888   1.00 14.32 ?  55  LYS   A HA   1 
ATOM   1423 H  HB2  . LYS   A 1 55  ? 21.338 11.748  6.490   1.00 15.47 ?  55  LYS   A HB2  1 
ATOM   1424 H  HB3  . LYS   A 1 55  ? 20.667 10.774  7.545   1.00 15.47 ?  55  LYS   A HB3  1 
ATOM   1425 H  HG2  . LYS   A 1 55  ? 20.306 12.554  8.983   1.00 17.32 ?  55  LYS   A HG2  1 
ATOM   1426 H  HG3  . LYS   A 1 55  ? 21.013 13.538  7.947   1.00 17.32 ?  55  LYS   A HG3  1 
ATOM   1427 H  HD2  . LYS   A 1 55  ? 19.319 13.187  6.414   1.00 19.37 ?  55  LYS   A HD2  1 
ATOM   1428 H  HD3  . LYS   A 1 55  ? 18.642 12.113  7.372   1.00 19.37 ?  55  LYS   A HD3  1 
ATOM   1429 H  HE2  . LYS   A 1 55  ? 18.208 13.839  8.926   1.00 22.10 ?  55  LYS   A HE2  1 
ATOM   1430 H  HE3  . LYS   A 1 55  ? 18.773 14.887  7.869   1.00 22.10 ?  55  LYS   A HE3  1 
ATOM   1431 H  HZ1  . LYS   A 1 55  ? 16.379 14.431  7.957   1.00 23.29 ?  55  LYS   A HZ1  1 
ATOM   1432 H  HZ2  . LYS   A 1 55  ? 16.989 14.703  6.673   1.00 23.29 ?  55  LYS   A HZ2  1 
ATOM   1433 H  HZ3  . LYS   A 1 55  ? 16.705 13.336  7.068   1.00 23.29 ?  55  LYS   A HZ3  1 
ATOM   1434 N  N    . ALA   A 1 56  ? 22.125 9.827   9.952   1.00 12.23 ?  56  ALA   A N    1 
ATOM   1435 C  CA   . ALA   A 1 56  ? 21.997 9.517   11.369  1.00 12.96 ?  56  ALA   A CA   1 
ATOM   1436 C  C    . ALA   A 1 56  ? 23.335 9.546   12.098  1.00 12.71 ?  56  ALA   A C    1 
ATOM   1437 O  O    . ALA   A 1 56  ? 23.356 9.734   13.316  1.00 13.96 ?  56  ALA   A O    1 
ATOM   1438 C  CB   . ALA   A 1 56  ? 21.301 8.167   11.558  1.00 14.14 ?  56  ALA   A CB   1 
ATOM   1439 H  H    . ALA   A 1 56  ? 21.934 9.177   9.427   1.00 14.68 ?  56  ALA   A H    1 
ATOM   1440 H  HA   . ALA   A 1 56  ? 21.443 10.184  11.784  1.00 15.56 ?  56  ALA   A HA   1 
ATOM   1441 H  HB1  . ALA   A 1 56  ? 21.228 7.976   12.508  1.00 16.98 ?  56  ALA   A HB1  1 
ATOM   1442 H  HB2  . ALA   A 1 56  ? 20.415 8.215   11.164  1.00 16.98 ?  56  ALA   A HB2  1 
ATOM   1443 H  HB3  . ALA   A 1 56  ? 21.819 7.473   11.121  1.00 16.98 ?  56  ALA   A HB3  1 
ATOM   1444 N  N    . THR   A 1 57  ? 24.447 9.353   11.385  1.00 11.97 ?  57  THR   A N    1 
ATOM   1445 C  CA   . THR   A 1 57  ? 25.789 9.480   11.960  1.00 12.19 ?  57  THR   A CA   1 
ATOM   1446 C  C    . THR   A 1 57  ? 26.341 10.899  11.876  1.00 12.31 ?  57  THR   A C    1 
ATOM   1447 O  O    . THR   A 1 57  ? 27.527 11.108  12.160  1.00 12.78 ?  57  THR   A O    1 
ATOM   1448 C  CB   . THR   A 1 57  ? 26.803 8.532   11.290  1.00 11.98 ?  57  THR   A CB   1 
ATOM   1449 O  OG1  . THR   A 1 57  ? 27.179 9.026   9.992   1.00 11.37 ?  57  THR   A OG1  1 
ATOM   1450 C  CG2  . THR   A 1 57  ? 26.281 7.108   11.190  1.00 12.01 ?  57  THR   A CG2  1 
ATOM   1451 H  H    . THR   A 1 57  ? 24.455 9.123   10.555  1.00 14.38 ?  57  THR   A H    1 
ATOM   1452 H  HA   . THR   A 1 57  ? 25.746 9.227   12.902  1.00 14.64 ?  57  THR   A HA   1 
ATOM   1453 H  HB   . THR   A 1 57  ? 27.605 8.502   11.845  1.00 14.39 ?  57  THR   A HB   1 
ATOM   1454 H  HG1  . THR   A 1 57  ? 26.499 9.094   9.505   1.00 13.65 ?  57  THR   A HG1  1 
ATOM   1455 H  HG21 . THR   A 1 57  ? 26.962 6.526   10.811  1.00 14.42 ?  57  THR   A HG21 1 
ATOM   1456 H  HG22 . THR   A 1 57  ? 26.042 6.775   12.070  1.00 14.42 ?  57  THR   A HG22 1 
ATOM   1457 H  HG23 . THR   A 1 57  ? 25.498 7.079   10.621  1.00 14.42 ?  57  THR   A HG23 1 
ATOM   1458 N  N    . ASN   A 1 58  ? 25.529 11.871  11.469  1.00 12.71 ?  58  ASN   A N    1 
ATOM   1459 C  CA   . ASN   A 1 58  ? 25.997 13.250  11.371  1.00 13.70 ?  58  ASN   A CA   1 
ATOM   1460 C  C    . ASN   A 1 58  ? 27.147 13.371  10.364  1.00 12.69 ?  58  ASN   A C    1 
ATOM   1461 O  O    . ASN   A 1 58  ? 28.039 14.209  10.517  1.00 13.25 ?  58  ASN   A O    1 
ATOM   1462 C  CB   . ASN   A 1 58  ? 26.364 13.787  12.769  1.00 16.33 ?  58  ASN   A CB   1 
ATOM   1463 C  CG   . ASN   A 1 58  ? 26.802 15.235  12.767  1.00 20.24 ?  58  ASN   A CG   1 
ATOM   1464 O  OD1  . ASN   A 1 58  ? 26.181 16.076  12.131  1.00 21.96 ?  58  ASN   A OD1  1 
ATOM   1465 N  ND2  . ASN   A 1 58  ? 27.872 15.538  13.507  1.00 21.17 ?  58  ASN   A ND2  1 
ATOM   1466 H  H    . ASN   A 1 58  ? 24.708 11.748  11.234  1.00 15.26 ?  58  ASN   A H    1 
ATOM   1467 H  HA   . ASN   A 1 58  ? 25.264 13.782  11.038  1.00 16.44 ?  58  ASN   A HA   1 
ATOM   1468 H  HB2  . ASN   A 1 58  ? 25.581 13.711  13.348  1.00 19.60 ?  58  ASN   A HB2  1 
ATOM   1469 H  HB3  . ASN   A 1 58  ? 27.088 13.263  13.136  1.00 19.60 ?  58  ASN   A HB3  1 
ATOM   1470 H  HD21 . ASN   A 1 58  ? 28.155 16.352  13.540  1.00 25.41 ?  58  ASN   A HD21 1 
ATOM   1471 H  HD22 . ASN   A 1 58  ? 28.275 14.923  13.943  1.00 25.41 ?  58  ASN   A HD22 1 
ATOM   1472 N  N    . ASN   A 1 59  ? 27.126 12.546  9.313   1.00 11.55 ?  59  ASN   A N    1 
ATOM   1473 C  CA   . ASN   A 1 59  ? 28.107 12.513  8.219   1.00 11.39 ?  59  ASN   A CA   1 
ATOM   1474 C  C    . ASN   A 1 59  ? 29.424 11.836  8.615   1.00 11.18 ?  59  ASN   A C    1 
ATOM   1475 O  O    . ASN   A 1 59  ? 30.347 11.788  7.793   1.00 11.39 ?  59  ASN   A O    1 
ATOM   1476 C  CB   . ASN   A 1 59  ? 28.389 13.900  7.605   1.00 11.45 ?  59  ASN   A CB   1 
ATOM   1477 C  CG   . ASN   A 1 59  ? 28.758 13.828  6.139   1.00 11.77 ?  59  ASN   A CG   1 
ATOM   1478 O  OD1  . ASN   A 1 59  ? 28.054 13.208  5.341   1.00 12.19 ?  59  ASN   A OD1  1 
ATOM   1479 N  ND2  . ASN   A 1 59  ? 29.853 14.484  5.767   1.00 12.45 ?  59  ASN   A ND2  1 
ATOM   1480 H  H    . ASN   A 1 59  ? 26.509 11.956  9.204   1.00 13.87 ?  59  ASN   A H    1 
ATOM   1481 H  HA   . ASN   A 1 59  ? 27.725 11.979  7.511   1.00 13.67 ?  59  ASN   A HA   1 
ATOM   1482 H  HB2  . ASN   A 1 59  ? 27.595 14.453  7.684   1.00 13.75 ?  59  ASN   A HB2  1 
ATOM   1483 H  HB3  . ASN   A 1 59  ? 29.128 14.315  8.075   1.00 13.75 ?  59  ASN   A HB3  1 
ATOM   1484 H  HD21 . ASN   A 1 59  ? 30.105 14.476  4.945   1.00 14.95 ?  59  ASN   A HD21 1 
ATOM   1485 H  HD22 . ASN   A 1 59  ? 30.323 14.909  6.353   1.00 14.95 ?  59  ASN   A HD22 1 
ATOM   1486 N  N    . ALA   A 1 60  ? 29.542 11.299  9.829   1.00 11.32 ?  60  ALA   A N    1 
ATOM   1487 C  CA   . ALA   A 1 60  ? 30.775 10.611  10.196  1.00 11.58 ?  60  ALA   A CA   1 
ATOM   1488 C  C    . ALA   A 1 60  ? 31.003 9.376   9.329   1.00 11.19 ?  60  ALA   A C    1 
ATOM   1489 O  O    . ALA   A 1 60  ? 32.149 9.044   9.007   1.00 11.51 ?  60  ALA   A O    1 
ATOM   1490 C  CB   . ALA   A 1 60  ? 30.756 10.250  11.679  1.00 12.02 ?  60  ALA   A CB   1 
ATOM   1491 H  H    . ALA   A 1 60  ? 28.940 11.318  10.441  1.00 13.60 ?  60  ALA   A H    1 
ATOM   1492 H  HA   . ALA   A 1 60  ? 31.521 11.211  10.050  1.00 13.91 ?  60  ALA   A HA   1 
ATOM   1493 H  HB1  . ALA   A 1 60  ? 31.578 9.794   11.905  1.00 14.44 ?  60  ALA   A HB1  1 
ATOM   1494 H  HB2  . ALA   A 1 60  ? 30.672 11.066  12.199  1.00 14.44 ?  60  ALA   A HB2  1 
ATOM   1495 H  HB3  . ALA   A 1 60  ? 29.995 9.671   11.852  1.00 14.44 ?  60  ALA   A HB3  1 
ATOM   1496 N  N    . MET   A 1 61  ? 29.930 8.681   8.943   1.00 10.75 ?  61  MET   A N    1 
ATOM   1497 C  CA   . MET   A 1 61  ? 30.073 7.540   8.043   1.00 10.71 ?  61  MET   A CA   1 
ATOM   1498 C  C    . MET   A 1 61  ? 30.709 7.962   6.720   1.00 10.58 ?  61  MET   A C    1 
ATOM   1499 O  O    . MET   A 1 61  ? 31.600 7.276   6.205   1.00 11.13 ?  61  MET   A O    1 
ATOM   1500 C  CB   . MET   A 1 61  ? 28.714 6.880   7.826   1.00 10.60 ?  61  MET   A CB   1 
ATOM   1501 C  CG   . MET   A 1 61  ? 28.731 5.711   6.858   1.00 11.37 ?  61  MET   A CG   1 
ATOM   1502 S  SD   . MET   A 1 61  ? 27.098 4.965   6.655   1.00 12.13 ?  61  MET   A SD   1 
ATOM   1503 C  CE   . MET   A 1 61  ? 26.971 4.084   8.222   1.00 13.64 ?  61  MET   A CE   1 
ATOM   1504 H  H    . MET   A 1 61  ? 29.121 8.848   9.181   1.00 12.91 ?  61  MET   A H    1 
ATOM   1505 H  HA   . MET   A 1 61  ? 30.650 6.884   8.464   1.00 12.87 ?  61  MET   A HA   1 
ATOM   1506 H  HB2  . MET   A 1 61  ? 28.388 6.552   8.677   1.00 12.73 ?  61  MET   A HB2  1 
ATOM   1507 H  HB3  . MET   A 1 61  ? 28.098 7.541   7.473   1.00 12.73 ?  61  MET   A HB3  1 
ATOM   1508 H  HG2  . MET   A 1 61  ? 29.017 6.011   5.983   1.00 13.65 ?  61  MET   A HG2  1 
ATOM   1509 H  HG3  . MET   A 1 61  ? 29.329 5.023   7.190   1.00 13.65 ?  61  MET   A HG3  1 
ATOM   1510 H  HE1  . MET   A 1 61  ? 26.131 3.599   8.244   1.00 16.37 ?  61  MET   A HE1  1 
ATOM   1511 H  HE2  . MET   A 1 61  ? 27.713 3.467   8.299   1.00 16.37 ?  61  MET   A HE2  1 
ATOM   1512 H  HE3  . MET   A 1 61  ? 26.998 4.726   8.953   1.00 16.37 ?  61  MET   A HE3  1 
ATOM   1513 N  N    . GLN   A 1 62  ? 30.271 9.093   6.161   1.00 10.56 ?  62  GLN   A N    1 
ATOM   1514 C  CA   . GLN   A 1 62  ? 30.835 9.558   4.899   1.00 10.56 ?  62  GLN   A CA   1 
ATOM   1515 C  C    . GLN   A 1 62  ? 32.302 9.931   5.049   1.00 10.75 ?  62  GLN   A C    1 
ATOM   1516 O  O    . GLN   A 1 62  ? 33.112 9.615   4.174   1.00 11.21 ?  62  GLN   A O    1 
ATOM   1517 C  CB   . GLN   A 1 62  ? 30.035 10.746  4.362   1.00 10.93 ?  62  GLN   A CB   1 
ATOM   1518 C  CG   . GLN   A 1 62  ? 30.418 11.101  2.934   1.00 10.88 ?  62  GLN   A CG   1 
ATOM   1519 C  CD   . GLN   A 1 62  ? 30.088 9.969   1.991   1.00 10.84 ?  62  GLN   A CD   1 
ATOM   1520 O  OE1  . GLN   A 1 62  ? 28.910 9.666   1.785   1.00 11.77 ?  62  GLN   A OE1  1 
ATOM   1521 N  NE2  . GLN   A 1 62  ? 31.106 9.292   1.468   1.00 11.39 ?  62  GLN   A NE2  1 
ATOM   1522 H  H    . GLN   A 1 62  ? 29.652 9.590   6.486   1.00 12.68 ?  62  GLN   A H    1 
ATOM   1523 H  HA   . GLN   A 1 62  ? 30.779 8.836   4.253   1.00 12.68 ?  62  GLN   A HA   1 
ATOM   1524 H  HB2  . GLN   A 1 62  ? 29.090 10.527  4.377   1.00 13.13 ?  62  GLN   A HB2  1 
ATOM   1525 H  HB3  . GLN   A 1 62  ? 30.206 11.521  4.918   1.00 13.13 ?  62  GLN   A HB3  1 
ATOM   1526 H  HG2  . GLN   A 1 62  ? 29.911 11.878  2.650   1.00 13.07 ?  62  GLN   A HG2  1 
ATOM   1527 H  HG3  . GLN   A 1 62  ? 31.366 11.274  2.882   1.00 13.07 ?  62  GLN   A HG3  1 
ATOM   1528 H  HE21 . GLN   A 1 62  ? 31.914 9.522   1.655   1.00 13.68 ?  62  GLN   A HE21 1 
ATOM   1529 H  HE22 . GLN   A 1 62  ? 30.960 8.632   0.937   1.00 13.68 ?  62  GLN   A HE22 1 
ATOM   1530 N  N    . VAL   A 1 63  ? 32.658 10.621  6.134   1.00 11.36 ?  63  VAL   A N    1 
ATOM   1531 C  CA   . VAL   A 1 63  ? 34.051 11.010  6.349   1.00 12.27 ?  63  VAL   A CA   1 
ATOM   1532 C  C    . VAL   A 1 63  ? 34.943 9.773   6.417   1.00 11.59 ?  63  VAL   A C    1 
ATOM   1533 O  O    . VAL   A 1 63  ? 35.999 9.698   5.769   1.00 12.22 ?  63  VAL   A O    1 
ATOM   1534 C  CB   . VAL   A 1 63  ? 34.166 11.883  7.612   1.00 13.98 ?  63  VAL   A CB   1 
ATOM   1535 C  CG1  . VAL   A 1 63  ? 35.621 12.114  7.972   1.00 15.78 ?  63  VAL   A CG1  1 
ATOM   1536 C  CG2  . VAL   A 1 63  ? 33.449 13.219  7.401   1.00 14.30 ?  63  VAL   A CG2  1 
ATOM   1537 H  H    . VAL   A 1 63  ? 32.118 10.873  6.755   1.00 13.64 ?  63  VAL   A H    1 
ATOM   1538 H  HA   . VAL   A 1 63  ? 34.343 11.542  5.596   1.00 14.73 ?  63  VAL   A HA   1 
ATOM   1539 H  HB   . VAL   A 1 63  ? 33.747 11.426  8.357   1.00 16.79 ?  63  VAL   A HB   1 
ATOM   1540 H  HG11 . VAL   A 1 63  ? 35.676 12.853  8.596   1.00 18.94 ?  63  VAL   A HG11 1 
ATOM   1541 H  HG12 . VAL   A 1 63  ? 35.982 11.311  8.377   1.00 18.94 ?  63  VAL   A HG12 1 
ATOM   1542 H  HG13 . VAL   A 1 63  ? 36.114 12.329  7.163   1.00 18.94 ?  63  VAL   A HG13 1 
ATOM   1543 H  HG21 . VAL   A 1 63  ? 33.544 13.759  8.202   1.00 17.17 ?  63  VAL   A HG21 1 
ATOM   1544 H  HG22 . VAL   A 1 63  ? 33.850 13.678  6.645   1.00 17.17 ?  63  VAL   A HG22 1 
ATOM   1545 H  HG23 . VAL   A 1 63  ? 32.512 13.049  7.225   1.00 17.17 ?  63  VAL   A HG23 1 
ATOM   1546 N  N    . GLU   A 1 64  ? 34.522 8.773   7.195   1.00 11.66 ?  64  GLU   A N    1 
ATOM   1547 C  CA   . GLU   A 1 64  ? 35.274 7.529   7.296   1.00 11.54 ?  64  GLU   A CA   1 
ATOM   1548 C  C    . GLU   A 1 64  ? 35.368 6.840   5.941   1.00 11.30 ?  64  GLU   A C    1 
ATOM   1549 O  O    . GLU   A 1 64  ? 36.422 6.300   5.566   1.00 11.69 ?  64  GLU   A O    1 
ATOM   1550 C  CB   . GLU   A 1 64  ? 34.579 6.622   8.309   1.00 11.97 ?  64  GLU   A CB   1 
ATOM   1551 C  CG   . GLU   A 1 64  ? 35.226 5.269   8.458   1.00 12.51 ?  64  GLU   A CG   1 
ATOM   1552 C  CD   . GLU   A 1 64  ? 34.346 4.279   9.187   1.00 13.27 ?  64  GLU   A CD   1 
ATOM   1553 O  OE1  . GLU   A 1 64  ? 33.107 4.371   9.050   1.00 13.96 ?  64  GLU   A OE1  1 
ATOM   1554 O  OE2  . GLU   A 1 64  ? 34.891 3.397   9.884   1.00 13.46 -1 64  GLU   A OE2  1 
ATOM   1555 H  H    . GLU   A 1 64  ? 33.801 8.791   7.664   1.00 14.00 ?  64  GLU   A H    1 
ATOM   1556 H  HA   . GLU   A 1 64  ? 36.172 7.721   7.613   1.00 13.86 ?  64  GLU   A HA   1 
ATOM   1557 H  HB2  . GLU   A 1 64  ? 34.601 7.057   9.182   1.00 14.37 ?  64  GLU   A HB2  1 
ATOM   1558 H  HB3  . GLU   A 1 64  ? 33.661 6.495   8.032   1.00 14.37 ?  64  GLU   A HB3  1 
ATOM   1559 H  HG2  . GLU   A 1 64  ? 35.413 4.897   7.576   1.00 15.02 ?  64  GLU   A HG2  1 
ATOM   1560 H  HG3  . GLU   A 1 64  ? 36.050 5.363   8.953   1.00 15.02 ?  64  GLU   A HG3  1 
ATOM   1561 N  N    . SER   A 1 65  ? 34.253 6.829   5.208   1.00 10.81 ?  65  SER   A N    1 
ATOM   1562 C  CA   . SER   A 1 65  ? 34.198 6.169   3.910   1.00 10.83 ?  65  SER   A CA   1 
ATOM   1563 C  C    . SER   A 1 65  ? 35.122 6.829   2.896   1.00 11.02 ?  65  SER   A C    1 
ATOM   1564 O  O    . SER   A 1 65  ? 35.766 6.143   2.097   1.00 11.84 ?  65  SER   A O    1 
ATOM   1565 C  CB   . SER   A 1 65  ? 32.764 6.184   3.383   1.00 11.01 ?  65  SER   A CB   1 
ATOM   1566 O  OG   . SER   A 1 65  ? 31.911 5.371   4.181   1.00 11.41 ?  65  SER   A OG   1 
ATOM   1567 H  H    . SER   A 1 65  ? 33.518 7.212   5.437   1.00 12.98 ?  65  SER   A H    1 
ATOM   1568 H  HA   . SER   A 1 65  ? 34.475 5.246   4.011   1.00 13.00 ?  65  SER   A HA   1 
ATOM   1569 H  HB2  . SER   A 1 65  ? 32.428 7.092   3.393   1.00 13.23 ?  65  SER   A HB2  1 
ATOM   1570 H  HB3  . SER   A 1 65  ? 32.757 5.840   2.474   1.00 13.23 ?  65  SER   A HB3  1 
ATOM   1571 H  HG   . SER   A 1 65  ? 31.912 5.657   4.976   1.00 13.70 ?  65  SER   A HG   1 
ATOM   1572 N  N    . ASP   A 1 66  ? 35.203 8.160   2.909   1.00 11.01 ?  66  ASP   A N    1 
ATOM   1573 C  CA   . ASP   A 1 66  ? 36.071 8.850   1.963   1.00 11.97 ?  66  ASP   A CA   1 
ATOM   1574 C  C    . ASP   A 1 66  ? 37.531 8.501   2.211   1.00 11.96 ?  66  ASP   A C    1 
ATOM   1575 O  O    . ASP   A 1 66  ? 38.305 8.324   1.263   1.00 13.02 ?  66  ASP   A O    1 
ATOM   1576 C  CB   . ASP   A 1 66  ? 35.850 10.359  2.048   1.00 13.27 ?  66  ASP   A CB   1 
ATOM   1577 C  CG   . ASP   A 1 66  ? 34.514 10.811  1.440   1.00 15.04 ?  66  ASP   A CG   1 
ATOM   1578 O  OD1  . ASP   A 1 66  ? 33.806 10.006  0.796   1.00 15.21 ?  66  ASP   A OD1  1 
ATOM   1579 O  OD2  . ASP   A 1 66  ? 34.202 12.013  1.585   1.00 17.71 -1 66  ASP   A OD2  1 
ATOM   1580 H  H    . ASP   A 1 66  ? 34.765 8.675   3.445   1.00 13.22 ?  66  ASP   A H    1 
ATOM   1581 H  HA   . ASP   A 1 66  ? 35.839 8.565   1.065   1.00 14.37 ?  66  ASP   A HA   1 
ATOM   1582 H  HB2  . ASP   A 1 66  ? 35.848 10.628  2.979   1.00 15.94 ?  66  ASP   A HB2  1 
ATOM   1583 H  HB3  . ASP   A 1 66  ? 36.568 10.808  1.575   1.00 15.94 ?  66  ASP   A HB3  1 
ATOM   1584 N  N    . ASP   A 1 67  ? 37.924 8.379   3.479   1.00 12.18 ?  67  ASP   A N    1 
ATOM   1585 C  CA   . ASP   A 1 67  ? 39.276 7.936   3.785   1.00 12.86 ?  67  ASP   A CA   1 
ATOM   1586 C  C    . ASP   A 1 67  ? 39.497 6.500   3.321   1.00 12.73 ?  67  ASP   A C    1 
ATOM   1587 O  O    . ASP   A 1 67  ? 40.561 6.174   2.778   1.00 13.52 ?  67  ASP   A O    1 
ATOM   1588 C  CB   . ASP   A 1 67  ? 39.541 8.085   5.282   1.00 14.46 ?  67  ASP   A CB   1 
ATOM   1589 C  CG   . ASP   A 1 67  ? 40.831 7.423   5.708   1.00 15.75 ?  67  ASP   A CG   1 
ATOM   1590 O  OD1  . ASP   A 1 67  ? 41.908 8.052   5.567   1.00 18.37 ?  67  ASP   A OD1  1 
ATOM   1591 O  OD2  . ASP   A 1 67  ? 40.774 6.266   6.174   1.00 15.58 -1 67  ASP   A OD2  1 
ATOM   1592 H  H    . ASP   A 1 67  ? 37.436 8.547   4.164   1.00 14.62 ?  67  ASP   A H    1 
ATOM   1593 H  HA   . ASP   A 1 67  ? 39.909 8.499   3.312   1.00 15.44 ?  67  ASP   A HA   1 
ATOM   1594 H  HB2  . ASP   A 1 67  ? 39.597 9.025   5.499   1.00 17.36 ?  67  ASP   A HB2  1 
ATOM   1595 H  HB3  . ASP   A 1 67  ? 38.814 7.669   5.774   1.00 17.36 ?  67  ASP   A HB3  1 
ATOM   1596 N  N    . TYR   A 1 68  ? 38.501 5.626   3.513   1.00 12.51 ?  68  TYR   A N    1 
ATOM   1597 C  CA   . TYR   A 1 68  ? 38.624 4.246   3.042   1.00 12.66 ?  68  TYR   A CA   1 
ATOM   1598 C  C    . TYR   A 1 68  ? 38.869 4.193   1.535   1.00 12.24 ?  68  TYR   A C    1 
ATOM   1599 O  O    . TYR   A 1 68  ? 39.747 3.461   1.062   1.00 13.08 ?  68  TYR   A O    1 
ATOM   1600 C  CB   . TYR   A 1 68  ? 37.372 3.425   3.416   1.00 13.09 ?  68  TYR   A CB   1 
ATOM   1601 C  CG   . TYR   A 1 68  ? 37.394 2.036   2.789   1.00 14.92 ?  68  TYR   A CG   1 
ATOM   1602 C  CD1  . TYR   A 1 68  ? 36.929 1.838   1.491   1.00 16.43 ?  68  TYR   A CD1  1 
ATOM   1603 C  CD2  . TYR   A 1 68  ? 37.931 0.950   3.460   1.00 16.77 ?  68  TYR   A CD2  1 
ATOM   1604 C  CE1  . TYR   A 1 68  ? 36.989 0.616   0.883   1.00 17.81 ?  68  TYR   A CE1  1 
ATOM   1605 C  CE2  . TYR   A 1 68  ? 37.992 -0.308  2.849   1.00 17.49 ?  68  TYR   A CE2  1 
ATOM   1606 C  CZ   . TYR   A 1 68  ? 37.531 -0.448  1.562   1.00 17.98 ?  68  TYR   A CZ   1 
ATOM   1607 O  OH   . TYR   A 1 68  ? 37.605 -1.666  0.945   1.00 19.37 ?  68  TYR   A OH   1 
ATOM   1608 H  H    . TYR   A 1 68  ? 37.754 5.804   3.904   1.00 15.02 ?  68  TYR   A H    1 
ATOM   1609 H  HA   . TYR   A 1 68  ? 39.383 3.833   3.480   1.00 15.21 ?  68  TYR   A HA   1 
ATOM   1610 H  HB2  . TYR   A 1 68  ? 37.334 3.318   4.379   1.00 15.72 ?  68  TYR   A HB2  1 
ATOM   1611 H  HB3  . TYR   A 1 68  ? 36.579 3.889   3.100   1.00 15.72 ?  68  TYR   A HB3  1 
ATOM   1612 H  HD1  . TYR   A 1 68  ? 36.573 2.562   1.022   1.00 19.73 ?  68  TYR   A HD1  1 
ATOM   1613 H  HD2  . TYR   A 1 68  ? 38.269 1.059   4.315   1.00 20.13 ?  68  TYR   A HD2  1 
ATOM   1614 H  HE1  . TYR   A 1 68  ? 36.663 0.507   0.016   1.00 21.38 ?  68  TYR   A HE1  1 
ATOM   1615 H  HE2  . TYR   A 1 68  ? 38.359 -1.036  3.290   1.00 21.00 ?  68  TYR   A HE2  1 
ATOM   1616 H  HH   . TYR   A 1 68  ? 37.938 -2.237  1.465   1.00 23.26 ?  68  TYR   A HH   1 
ATOM   1617 N  N    . ILE   A 1 69  ? 38.079 4.943   0.760   1.00 12.01 ?  69  ILE   A N    1 
ATOM   1618 C  CA   . ILE   A 1 69  ? 38.221 4.928   -0.694  1.00 11.91 ?  69  ILE   A CA   1 
ATOM   1619 C  C    . ILE   A 1 69  ? 39.553 5.538   -1.118  1.00 12.10 ?  69  ILE   A C    1 
ATOM   1620 O  O    . ILE   A 1 69  ? 40.201 5.054   -2.055  1.00 12.57 ?  69  ILE   A O    1 
ATOM   1621 C  CB   . ILE   A 1 69  ? 37.029 5.644   -1.359  1.00 12.92 ?  69  ILE   A CB   1 
ATOM   1622 C  CG1  . ILE   A 1 69  ? 35.711 4.914   -1.085  1.00 13.42 ?  69  ILE   A CG1  1 
ATOM   1623 C  CG2  . ILE   A 1 69  ? 37.271 5.831   -2.863  1.00 14.38 ?  69  ILE   A CG2  1 
ATOM   1624 C  CD1  . ILE   A 1 69  ? 35.553 3.621   -1.841  1.00 14.15 ?  69  ILE   A CD1  1 
ATOM   1625 H  H    . ILE   A 1 69  ? 37.464 5.466   1.054   1.00 14.42 ?  69  ILE   A H    1 
ATOM   1626 H  HA   . ILE   A 1 69  ? 38.215 4.010   -0.993  1.00 14.30 ?  69  ILE   A HA   1 
ATOM   1627 H  HB   . ILE   A 1 69  ? 36.956 6.526   -0.967  1.00 15.51 ?  69  ILE   A HB   1 
ATOM   1628 H  HG12 . ILE   A 1 69  ? 35.661 4.708   -0.136  1.00 16.11 ?  69  ILE   A HG12 1 
ATOM   1629 H  HG13 . ILE   A 1 69  ? 34.974 5.493   -1.331  1.00 16.11 ?  69  ILE   A HG13 1 
ATOM   1630 H  HG21 . ILE   A 1 69  ? 36.429 6.037   -3.298  1.00 17.26 ?  69  ILE   A HG21 1 
ATOM   1631 H  HG22 . ILE   A 1 69  ? 37.893 6.569   -2.995  1.00 17.26 ?  69  ILE   A HG22 1 
ATOM   1632 H  HG23 . ILE   A 1 69  ? 37.644 5.017   -3.231  1.00 17.26 ?  69  ILE   A HG23 1 
ATOM   1633 H  HD11 . ILE   A 1 69  ? 34.748 3.178   -1.535  1.00 16.99 ?  69  ILE   A HD11 1 
ATOM   1634 H  HD12 . ILE   A 1 69  ? 35.481 3.818   -2.788  1.00 16.99 ?  69  ILE   A HD12 1 
ATOM   1635 H  HD13 . ILE   A 1 69  ? 36.324 3.060   -1.675  1.00 16.99 ?  69  ILE   A HD13 1 
ATOM   1636 N  N    . ALA   A 1 70  ? 39.969 6.623   -0.465  1.00 12.64 ?  70  ALA   A N    1 
ATOM   1637 C  CA   . ALA   A 1 70  ? 41.249 7.230   -0.814  1.00 13.58 ?  70  ALA   A CA   1 
ATOM   1638 C  C    . ALA   A 1 70  ? 42.398 6.247   -0.643  1.00 13.83 ?  70  ALA   A C    1 
ATOM   1639 O  O    . ALA   A 1 70  ? 43.372 6.292   -1.400  1.00 15.97 ?  70  ALA   A O    1 
ATOM   1640 C  CB   . ALA   A 1 70  ? 41.489 8.485   0.027   1.00 14.22 ?  70  ALA   A CB   1 
ATOM   1641 H  H    . ALA   A 1 70  ? 39.543 7.021   0.162   1.00 15.17 ?  70  ALA   A H    1 
ATOM   1642 H  HA   . ALA   A 1 70  ? 41.226 7.505   -1.747  1.00 16.30 ?  70  ALA   A HA   1 
ATOM   1643 H  HB1  . ALA   A 1 70  ? 42.351 8.872   -0.221  1.00 17.08 ?  70  ALA   A HB1  1 
ATOM   1644 H  HB2  . ALA   A 1 70  ? 40.784 9.125   -0.141  1.00 17.08 ?  70  ALA   A HB2  1 
ATOM   1645 H  HB3  . ALA   A 1 70  ? 41.504 8.239   0.965   1.00 17.08 ?  70  ALA   A HB3  1 
ATOM   1646 N  N    . THR   A 1 71  ? 42.293 5.345   0.330   1.00 13.39 ?  71  THR   A N    1 
ATOM   1647 C  CA   . THR   A 1 71  ? 43.347 4.370   0.586   1.00 14.87 ?  71  THR   A CA   1 
ATOM   1648 C  C    . THR   A 1 71  ? 43.226 3.141   -0.306  1.00 15.16 ?  71  THR   A C    1 
ATOM   1649 O  O    . THR   A 1 71  ? 44.240 2.618   -0.788  1.00 16.87 ?  71  THR   A O    1 
ATOM   1650 C  CB   . THR   A 1 71  ? 43.266 3.928   2.044   1.00 17.16 ?  71  THR   A CB   1 
ATOM   1651 O  OG1  . THR   A 1 71  ? 43.494 5.059   2.890   1.00 18.67 ?  71  THR   A OG1  1 
ATOM   1652 C  CG2  . THR   A 1 71  ? 44.283 2.830   2.347   1.00 18.95 ?  71  THR   A CG2  1 
ATOM   1653 H  H    . THR   A 1 71  ? 41.614 5.275   0.849   1.00 16.08 ?  71  THR   A H    1 
ATOM   1654 H  HA   . THR   A 1 71  ? 44.211 4.777   0.429   1.00 17.85 ?  71  THR   A HA   1 
ATOM   1655 H  HB   . THR   A 1 71  ? 42.379 3.567   2.213   1.00 20.60 ?  71  THR   A HB   1 
ATOM   1656 H  HG1  . THR   A 1 71  ? 42.901 5.636   2.749   1.00 22.41 ?  71  THR   A HG1  1 
ATOM   1657 H  HG21 . THR   A 1 71  ? 44.405 2.748   3.305   1.00 22.75 ?  71  THR   A HG21 1 
ATOM   1658 H  HG22 . THR   A 1 71  ? 43.979 1.977   1.997   1.00 22.75 ?  71  THR   A HG22 1 
ATOM   1659 H  HG23 . THR   A 1 71  ? 45.140 3.048   1.942   1.00 22.75 ?  71  THR   A HG23 1 
ATOM   1660 N  N    . ASN   A 1 72  ? 42.001 2.641   -0.505  1.00 14.08 ?  72  ASN   A N    1 
ATOM   1661 C  CA   . ASN   A 1 72  ? 41.777 1.313   -1.063  1.00 14.36 ?  72  ASN   A CA   1 
ATOM   1662 C  C    . ASN   A 1 72  ? 41.161 1.299   -2.450  1.00 14.27 ?  72  ASN   A C    1 
ATOM   1663 O  O    . ASN   A 1 72  ? 41.162 0.237   -3.090  1.00 15.35 ?  72  ASN   A O    1 
ATOM   1664 C  CB   . ASN   A 1 72  ? 40.874 0.504   -0.124  1.00 15.20 ?  72  ASN   A CB   1 
ATOM   1665 C  CG   . ASN   A 1 72  ? 41.487 0.329   1.238   1.00 16.45 ?  72  ASN   A CG   1 
ATOM   1666 O  OD1  . ASN   A 1 72  ? 41.047 0.930   2.216   1.00 18.15 ?  72  ASN   A OD1  1 
ATOM   1667 N  ND2  . ASN   A 1 72  ? 42.530 -0.470  1.307   1.00 16.96 ?  72  ASN   A ND2  1 
ATOM   1668 H  H    . ASN   A 1 72  ? 41.273 3.066   -0.322  1.00 16.90 ?  72  ASN   A H    1 
ATOM   1669 H  HA   . ASN   A 1 72  ? 42.626 0.858   -1.121  1.00 17.24 ?  72  ASN   A HA   1 
ATOM   1670 H  HB2  . ASN   A 1 72  ? 40.027 0.964   -0.020  1.00 18.25 ?  72  ASN   A HB2  1 
ATOM   1671 H  HB3  . ASN   A 1 72  ? 40.732 -0.377  -0.506  1.00 18.25 ?  72  ASN   A HB3  1 
ATOM   1672 H  HD21 . ASN   A 1 72  ? 42.919 -0.602  2.063   1.00 20.36 ?  72  ASN   A HD21 1 
ATOM   1673 H  HD22 . ASN   A 1 72  ? 42.816 -0.868  0.602   1.00 20.36 ?  72  ASN   A HD22 1 
ATOM   1674 N  N    . GLY   A 1 73  ? 40.613 2.413   -2.919  1.00 13.78 ?  73  GLY   A N    1 
ATOM   1675 C  CA   . GLY   A 1 73  ? 39.881 2.425   -4.160  1.00 13.67 ?  73  GLY   A CA   1 
ATOM   1676 C  C    . GLY   A 1 73  ? 38.490 1.848   -3.991  1.00 12.70 ?  73  GLY   A C    1 
ATOM   1677 O  O    . GLY   A 1 73  ? 38.103 1.401   -2.906  1.00 13.42 ?  73  GLY   A O    1 
ATOM   1678 H  H    . GLY   A 1 73  ? 40.657 3.188   -2.534  1.00 16.54 ?  73  GLY   A H    1 
ATOM   1679 H  HA2  . GLY   A 1 73  ? 39.805 3.337   -4.485  1.00 16.41 ?  73  GLY   A HA2  1 
ATOM   1680 H  HA3  . GLY   A 1 73  ? 40.360 1.902   -4.824  1.00 16.41 ?  73  GLY   A HA3  1 
ATOM   1681 N  N    . PRO   A 1 74  ? 37.716 1.855   -5.073  1.00 13.57 ?  74  PRO   A N    1 
ATOM   1682 C  CA   . PRO   A 1 74  ? 36.317 1.433   -4.990  1.00 13.33 ?  74  PRO   A CA   1 
ATOM   1683 C  C    . PRO   A 1 74  ? 36.169 -0.050  -4.671  1.00 13.03 ?  74  PRO   A C    1 
ATOM   1684 O  O    . PRO   A 1 74  ? 37.037 -0.881  -4.949  1.00 13.83 ?  74  PRO   A O    1 
ATOM   1685 C  CB   . PRO   A 1 74  ? 35.774 1.734   -6.392  1.00 15.11 ?  74  PRO   A CB   1 
ATOM   1686 C  CG   . PRO   A 1 74  ? 36.724 2.705   -6.991  1.00 17.90 ?  74  PRO   A CG   1 
ATOM   1687 C  CD   . PRO   A 1 74  ? 38.058 2.359   -6.412  1.00 15.66 ?  74  PRO   A CD   1 
ATOM   1688 H  HA   . PRO   A 1 74  ? 35.840 1.960   -4.329  1.00 16.01 ?  74  PRO   A HA   1 
ATOM   1689 H  HB2  . PRO   A 1 74  ? 35.744 0.914   -6.908  1.00 18.14 ?  74  PRO   A HB2  1 
ATOM   1690 H  HB3  . PRO   A 1 74  ? 34.887 2.123   -6.316  1.00 18.14 ?  74  PRO   A HB3  1 
ATOM   1691 H  HG2  . PRO   A 1 74  ? 36.734 2.599   -7.953  1.00 21.49 ?  74  PRO   A HG2  1 
ATOM   1692 H  HG3  . PRO   A 1 74  ? 36.471 3.605   -6.743  1.00 21.49 ?  74  PRO   A HG3  1 
ATOM   1693 H  HD2  . PRO   A 1 74  ? 38.493 1.663   -6.937  1.00 18.80 ?  74  PRO   A HD2  1 
ATOM   1694 H  HD3  . PRO   A 1 74  ? 38.616 3.153   -6.353  1.00 18.80 ?  74  PRO   A HD3  1 
ATOM   1695 N  N    . LEU   A 1 75  ? 35.019 -0.371  -4.085  1.00 12.29 ?  75  LEU   A N    1 
ATOM   1696 C  CA   . LEU   A 1 75  ? 34.625 -1.761  -3.931  1.00 11.70 ?  75  LEU   A CA   1 
ATOM   1697 C  C    . LEU   A 1 75  ? 34.239 -2.338  -5.290  1.00 12.15 ?  75  LEU   A C    1 
ATOM   1698 O  O    . LEU   A 1 75  ? 34.112 -1.624  -6.288  1.00 13.65 ?  75  LEU   A O    1 
ATOM   1699 C  CB   . LEU   A 1 75  ? 33.439 -1.883  -2.977  1.00 11.89 ?  75  LEU   A CB   1 
ATOM   1700 C  CG   . LEU   A 1 75  ? 33.639 -1.465  -1.524  1.00 13.77 ?  75  LEU   A CG   1 
ATOM   1701 C  CD1  . LEU   A 1 75  ? 32.354 -1.683  -0.734  1.00 15.57 ?  75  LEU   A CD1  1 
ATOM   1702 C  CD2  . LEU   A 1 75  ? 34.783 -2.179  -0.868  1.00 16.87 ?  75  LEU   A CD2  1 
ATOM   1703 H  H    . LEU   A 1 75  ? 34.455 0.198   -3.774  1.00 14.76 ?  75  LEU   A H    1 
ATOM   1704 H  HA   . LEU   A 1 75  ? 35.367 -2.270  -3.582  1.00 14.06 ?  75  LEU   A HA   1 
ATOM   1705 H  HB2  . LEU   A 1 75  ? 32.716 -1.348  -3.330  1.00 14.27 ?  75  LEU   A HB2  1 
ATOM   1706 H  HB3  . LEU   A 1 75  ? 33.169 -2.816  -2.967  1.00 14.27 ?  75  LEU   A HB3  1 
ATOM   1707 H  HG   . LEU   A 1 75  ? 33.842 -0.517  -1.504  1.00 16.54 ?  75  LEU   A HG   1 
ATOM   1708 H  HD11 . LEU   A 1 75  ? 32.502 -1.406  0.184   1.00 18.70 ?  75  LEU   A HD11 1 
ATOM   1709 H  HD12 . LEU   A 1 75  ? 31.651 -1.146  -1.132  1.00 18.70 ?  75  LEU   A HD12 1 
ATOM   1710 H  HD13 . LEU   A 1 75  ? 32.120 -2.620  -0.767  1.00 18.70 ?  75  LEU   A HD13 1 
ATOM   1711 H  HD21 . LEU   A 1 75  ? 34.832 -1.911  0.064   1.00 20.26 ?  75  LEU   A HD21 1 
ATOM   1712 H  HD22 . LEU   A 1 75  ? 34.640 -3.136  -0.930  1.00 20.26 ?  75  LEU   A HD22 1 
ATOM   1713 H  HD23 . LEU   A 1 75  ? 35.611 -1.940  -1.320  1.00 20.26 ?  75  LEU   A HD23 1 
ATOM   1714 N  N    . LYS   A 1 76  ? 34.062 -3.657  -5.315  1.00 12.53 ?  76  LYS   A N    1 
ATOM   1715 C  CA   . LYS   A 1 76  ? 33.463 -4.369  -6.437  1.00 13.09 ?  76  LYS   A CA   1 
ATOM   1716 C  C    . LYS   A 1 76  ? 31.953 -4.450  -6.245  1.00 12.02 ?  76  LYS   A C    1 
ATOM   1717 O  O    . LYS   A 1 76  ? 31.467 -4.567  -5.121  1.00 11.91 ?  76  LYS   A O    1 
ATOM   1718 C  CB   . LYS   A 1 76  ? 34.006 -5.808  -6.494  1.00 14.73 ?  76  LYS   A CB   1 
ATOM   1719 C  CG   . LYS   A 1 76  ? 35.514 -5.915  -6.684  1.00 16.06 ?  76  LYS   A CG   1 
ATOM   1720 C  CD   . LYS   A 1 76  ? 36.027 -7.322  -6.469  1.00 17.45 ?  76  LYS   A CD   1 
ATOM   1721 C  CE   . LYS   A 1 76  ? 37.528 -7.390  -6.667  1.00 19.92 ?  76  LYS   A CE   1 
ATOM   1722 N  NZ   . LYS   A 1 76  ? 38.057 -8.753  -6.452  1.00 20.80 ?  76  LYS   A NZ   1 
ATOM   1723 H  H    . LYS   A 1 76  ? 34.292 -4.178  -4.667  1.00 15.05 ?  76  LYS   A H    1 
ATOM   1724 H  HA   . LYS   A 1 76  ? 33.663 -3.913  -7.271  1.00 15.72 ?  76  LYS   A HA   1 
ATOM   1725 H  HB2  . LYS   A 1 76  ? 33.783 -6.252  -5.663  1.00 17.68 ?  76  LYS   A HB2  1 
ATOM   1726 H  HB3  . LYS   A 1 76  ? 33.583 -6.265  -7.236  1.00 17.68 ?  76  LYS   A HB3  1 
ATOM   1727 H  HG2  . LYS   A 1 76  ? 35.739 -5.647  -7.590  1.00 19.28 ?  76  LYS   A HG2  1 
ATOM   1728 H  HG3  . LYS   A 1 76  ? 35.958 -5.332  -6.047  1.00 19.28 ?  76  LYS   A HG3  1 
ATOM   1729 H  HD2  . LYS   A 1 76  ? 35.821 -7.605  -5.563  1.00 20.94 ?  76  LYS   A HD2  1 
ATOM   1730 H  HD3  . LYS   A 1 76  ? 35.605 -7.920  -7.109  1.00 20.94 ?  76  LYS   A HD3  1 
ATOM   1731 H  HE2  . LYS   A 1 76  ? 37.740 -7.121  -7.573  1.00 23.92 ?  76  LYS   A HE2  1 
ATOM   1732 H  HE3  . LYS   A 1 76  ? 37.957 -6.797  -6.031  1.00 23.92 ?  76  LYS   A HE3  1 
ATOM   1733 H  HZ1  . LYS   A 1 76  ? 38.937 -8.767  -6.575  1.00 24.97 ?  76  LYS   A HZ1  1 
ATOM   1734 H  HZ2  . LYS   A 1 76  ? 37.875 -9.029  -5.624  1.00 24.97 ?  76  LYS   A HZ2  1 
ATOM   1735 H  HZ3  . LYS   A 1 76  ? 37.678 -9.323  -7.029  1.00 24.97 ?  76  LYS   A HZ3  1 
ATOM   1736 N  N    . VAL   A 1 77  ? 31.206 -4.425  -7.352  1.00 12.44 ?  77  VAL   A N    1 
ATOM   1737 C  CA   . VAL   A 1 77  ? 29.798 -4.805  -7.265  1.00 12.39 ?  77  VAL   A CA   1 
ATOM   1738 C  C    . VAL   A 1 77  ? 29.730 -6.258  -6.824  1.00 12.23 ?  77  VAL   A C    1 
ATOM   1739 O  O    . VAL   A 1 77  ? 30.384 -7.129  -7.408  1.00 12.43 ?  77  VAL   A O    1 
ATOM   1740 C  CB   . VAL   A 1 77  ? 29.075 -4.586  -8.601  1.00 13.46 ?  77  VAL   A CB   1 
ATOM   1741 C  CG1  . VAL   A 1 77  ? 27.615 -5.017  -8.488  1.00 14.38 ?  77  VAL   A CG1  1 
ATOM   1742 C  CG2  . VAL   A 1 77  ? 29.174 -3.133  -9.027  1.00 15.15 ?  77  VAL   A CG2  1 
ATOM   1743 H  H    . VAL   A 1 77  ? 31.484 -4.193  -8.132  1.00 14.94 ?  77  VAL   A H    1 
ATOM   1744 H  HA   . VAL   A 1 77  ? 29.363 -4.262  -6.591  1.00 14.87 ?  77  VAL   A HA   1 
ATOM   1745 H  HB   . VAL   A 1 77  ? 29.502 -5.128  -9.285  1.00 16.16 ?  77  VAL   A HB   1 
ATOM   1746 H  HG11 . VAL   A 1 77  ? 27.138 -4.705  -9.270  1.00 17.26 ?  77  VAL   A HG11 1 
ATOM   1747 H  HG12 . VAL   A 1 77  ? 27.576 -5.984  -8.436  1.00 17.26 ?  77  VAL   A HG12 1 
ATOM   1748 H  HG13 . VAL   A 1 77  ? 27.237 -4.623  -7.687  1.00 17.26 ?  77  VAL   A HG13 1 
ATOM   1749 H  HG21 . VAL   A 1 77  ? 28.660 -3.008  -9.838  1.00 18.19 ?  77  VAL   A HG21 1 
ATOM   1750 H  HG22 . VAL   A 1 77  ? 28.821 -2.574  -8.318  1.00 18.19 ?  77  VAL   A HG22 1 
ATOM   1751 H  HG23 . VAL   A 1 77  ? 30.106 -2.913  -9.187  1.00 18.19 ?  77  VAL   A HG23 1 
ATOM   1752 N  N    . GLY   A 1 78  ? 28.954 -6.524  -5.778  1.00 11.64 ?  78  GLY   A N    1 
ATOM   1753 C  CA   . GLY   A 1 78  ? 28.924 -7.816  -5.127  1.00 12.03 ?  78  GLY   A CA   1 
ATOM   1754 C  C    . GLY   A 1 78  ? 29.829 -7.909  -3.919  1.00 11.49 ?  78  GLY   A C    1 
ATOM   1755 O  O    . GLY   A 1 78  ? 29.767 -8.910  -3.193  1.00 12.26 ?  78  GLY   A O    1 
ATOM   1756 H  H    . GLY   A 1 78  ? 28.418 -5.944  -5.425  1.00 13.98 ?  78  GLY   A H    1 
ATOM   1757 H  HA2  . GLY   A 1 78  ? 28.018 -8.005  -4.849  1.00 14.44 ?  78  GLY   A HA2  1 
ATOM   1758 H  HA3  . GLY   A 1 78  ? 29.195 -8.492  -5.769  1.00 14.44 ?  78  GLY   A HA3  1 
ATOM   1759 N  N    . GLY   A 1 79  ? 30.682 -6.903  -3.699  1.00 11.43 ?  79  GLY   A N    1 
ATOM   1760 C  CA   . GLY   A 1 79  ? 31.643 -6.916  -2.620  1.00 11.73 ?  79  GLY   A CA   1 
ATOM   1761 C  C    . GLY   A 1 79  ? 31.190 -6.116  -1.408  1.00 11.02 ?  79  GLY   A C    1 
ATOM   1762 O  O    . GLY   A 1 79  ? 30.074 -5.604  -1.338  1.00 11.84 ?  79  GLY   A O    1 
ATOM   1763 H  H    . GLY   A 1 79  ? 30.720 -6.187  -4.177  1.00 13.72 ?  79  GLY   A H    1 
ATOM   1764 H  HA2  . GLY   A 1 79  ? 31.799 -7.839  -2.344  1.00 14.08 ?  79  GLY   A HA2  1 
ATOM   1765 H  HA3  . GLY   A 1 79  ? 32.484 -6.551  -2.932  1.00 14.08 ?  79  GLY   A HA3  1 
ATOM   1766 N  N    . SER   A 1 80  ? 32.091 -6.026  -0.430  1.00 11.87 ?  80  SER   A N    1 
ATOM   1767 C  CA   . SER   A 1 80  ? 31.767 -5.391  0.838   1.00 11.47 ?  80  SER   A CA   1 
ATOM   1768 C  C    . SER   A 1 80  ? 33.041 -4.940  1.536   1.00 11.25 ?  80  SER   A C    1 
ATOM   1769 O  O    . SER   A 1 80  ? 34.153 -5.381  1.217   1.00 12.87 ?  80  SER   A O    1 
ATOM   1770 C  CB   . SER   A 1 80  ? 31.004 -6.346  1.757   1.00 12.41 ?  80  SER   A CB   1 
ATOM   1771 O  OG   . SER   A 1 80  ? 31.839 -7.397  2.229   1.00 13.88 ?  80  SER   A OG   1 
ATOM   1772 H  H    . SER   A 1 80  ? 32.901 -6.316  -0.482  1.00 14.25 ?  80  SER   A H    1 
ATOM   1773 H  HA   . SER   A 1 80  ? 31.214 -4.614  0.656   1.00 13.77 ?  80  SER   A HA   1 
ATOM   1774 H  HB2  . SER   A 1 80  ? 30.669 -5.844  2.515   1.00 14.90 ?  80  SER   A HB2  1 
ATOM   1775 H  HB3  . SER   A 1 80  ? 30.261 -6.728  1.261   1.00 14.90 ?  80  SER   A HB3  1 
ATOM   1776 H  HG   . SER   A 1 80  ? 32.133 -7.835  1.573   1.00 16.66 ?  80  SER   A HG   1 
ATOM   1777 N  N    . CYS   A 1 81  ? 32.849 -4.089  2.542   1.00 11.19 ?  81  CYS   A N    1 
ATOM   1778 C  CA   . CYS   A 1 81  ? 33.898 -3.802  3.504   1.00 11.40 ?  81  CYS   A CA   1 
ATOM   1779 C  C    . CYS   A 1 81  ? 33.249 -3.563  4.859   1.00 11.24 ?  81  CYS   A C    1 
ATOM   1780 O  O    . CYS   A 1 81  ? 32.084 -3.155  4.944   1.00 12.22 ?  81  CYS   A O    1 
ATOM   1781 C  CB   . CYS   A 1 81  ? 34.771 -2.613  3.084   1.00 11.89 ?  81  CYS   A CB   1 
ATOM   1782 S  SG   . CYS   A 1 81  ? 33.875 -1.042  3.090   1.00 12.04 ?  81  CYS   A SG   1 
ATOM   1783 H  H    . CYS   A 1 81  ? 32.112 -3.670  2.689   1.00 13.43 ?  81  CYS   A H    1 
ATOM   1784 H  HA   . CYS   A 1 81  ? 34.473 -4.580  3.582   1.00 13.68 ?  81  CYS   A HA   1 
ATOM   1785 H  HB2  . CYS   A 1 81  ? 35.519 -2.540  3.704   1.00 14.27 ?  81  CYS   A HB2  1 
ATOM   1786 H  HB3  . CYS   A 1 81  ? 35.108 -2.773  2.187   1.00 14.27 ?  81  CYS   A HB3  1 
ATOM   1787 H  HG   . CYS   A 1 81  ? 34.625 -0.167  2.751   1.00 14.46 ?  81  CYS   A HG   1 
ATOM   1788 N  N    . VAL   A 1 82  ? 34.010 -3.833  5.916   1.00 11.49 ?  82  VAL   A N    1 
ATOM   1789 C  CA   . VAL   A 1 82  ? 33.586 -3.585  7.288   1.00 11.84 ?  82  VAL   A CA   1 
ATOM   1790 C  C    . VAL   A 1 82  ? 34.187 -2.271  7.754   1.00 12.23 ?  82  VAL   A C    1 
ATOM   1791 O  O    . VAL   A 1 82  ? 35.413 -2.104  7.745   1.00 12.85 ?  82  VAL   A O    1 
ATOM   1792 C  CB   . VAL   A 1 82  ? 34.013 -4.724  8.225   1.00 13.31 ?  82  VAL   A CB   1 
ATOM   1793 C  CG1  . VAL   A 1 82  ? 33.571 -4.431  9.653   1.00 14.78 ?  82  VAL   A CG1  1 
ATOM   1794 C  CG2  . VAL   A 1 82  ? 33.456 -6.054  7.751   1.00 14.35 ?  82  VAL   A CG2  1 
ATOM   1795 H  H    . VAL   A 1 82  ? 34.805 -4.174  5.859   1.00 13.79 ?  82  VAL   A H    1 
ATOM   1796 H  HA   . VAL   A 1 82  ? 32.620 -3.507  7.313   1.00 14.22 ?  82  VAL   A HA   1 
ATOM   1797 H  HB   . VAL   A 1 82  ? 34.980 -4.783  8.221   1.00 15.98 ?  82  VAL   A HB   1 
ATOM   1798 H  HG11 . VAL   A 1 82  ? 33.669 -5.236  10.184  1.00 17.74 ?  82  VAL   A HG11 1 
ATOM   1799 H  HG12 . VAL   A 1 82  ? 34.126 -3.724  10.023  1.00 17.74 ?  82  VAL   A HG12 1 
ATOM   1800 H  HG13 . VAL   A 1 82  ? 32.642 -4.151  9.648   1.00 17.74 ?  82  VAL   A HG13 1 
ATOM   1801 H  HG21 . VAL   A 1 82  ? 33.700 -6.743  8.388   1.00 17.24 ?  82  VAL   A HG21 1 
ATOM   1802 H  HG22 . VAL   A 1 82  ? 32.488 -5.988  7.691   1.00 17.24 ?  82  VAL   A HG22 1 
ATOM   1803 H  HG23 . VAL   A 1 82  ? 33.826 -6.260  6.879   1.00 17.24 ?  82  VAL   A HG23 1 
ATOM   1804 N  N    . LEU   A 1 83  ? 33.330 -1.344  8.170   1.00 11.81 ?  83  LEU   A N    1 
ATOM   1805 C  CA   . LEU   A 1 83  ? 33.750 -0.075  8.745   1.00 11.59 ?  83  LEU   A CA   1 
ATOM   1806 C  C    . LEU   A 1 83  ? 33.028 0.109   10.078  1.00 11.69 ?  83  LEU   A C    1 
ATOM   1807 O  O    . LEU   A 1 83  ? 32.306 -0.782  10.547  1.00 12.44 ?  83  LEU   A O    1 
ATOM   1808 C  CB   . LEU   A 1 83  ? 33.500 1.079   7.760   1.00 12.20 ?  83  LEU   A CB   1 
ATOM   1809 C  CG   . LEU   A 1 83  ? 34.400 1.071   6.519   1.00 12.80 ?  83  LEU   A CG   1 
ATOM   1810 C  CD1  . LEU   A 1 83  ? 33.962 2.140   5.534   1.00 13.54 ?  83  LEU   A CD1  1 
ATOM   1811 C  CD2  . LEU   A 1 83  ? 35.871 1.291   6.905   1.00 13.59 ?  83  LEU   A CD2  1 
ATOM   1812 H  H    . LEU   A 1 83  ? 32.476 -1.429  8.122   1.00 14.18 ?  83  LEU   A H    1 
ATOM   1813 H  HA   . LEU   A 1 83  ? 34.701 -0.105  8.926   1.00 13.92 ?  83  LEU   A HA   1 
ATOM   1814 H  HB2  . LEU   A 1 83  ? 32.583 1.032   7.446   1.00 14.65 ?  83  LEU   A HB2  1 
ATOM   1815 H  HB3  . LEU   A 1 83  ? 33.645 1.921   8.215   1.00 14.65 ?  83  LEU   A HB3  1 
ATOM   1816 H  HG   . LEU   A 1 83  ? 34.335 0.212   6.078   1.00 15.37 ?  83  LEU   A HG   1 
ATOM   1817 H  HD11 . LEU   A 1 83  ? 34.547 2.113   4.759   1.00 16.25 ?  83  LEU   A HD11 1 
ATOM   1818 H  HD12 . LEU   A 1 83  ? 33.049 1.962   5.266   1.00 16.25 ?  83  LEU   A HD12 1 
ATOM   1819 H  HD13 . LEU   A 1 83  ? 34.021 3.007   5.963   1.00 16.25 ?  83  LEU   A HD13 1 
ATOM   1820 H  HD21 . LEU   A 1 83  ? 36.394 1.442   6.098   1.00 16.32 ?  83  LEU   A HD21 1 
ATOM   1821 H  HD22 . LEU   A 1 83  ? 35.935 2.071   7.483   1.00 16.32 ?  83  LEU   A HD22 1 
ATOM   1822 H  HD23 . LEU   A 1 83  ? 36.202 0.509   7.369   1.00 16.32 ?  83  LEU   A HD23 1 
ATOM   1823 N  N    . SER   A 1 84  ? 33.244 1.260   10.708  1.00 12.32 ?  84  SER   A N    1 
ATOM   1824 C  CA   . SER   A 1 84  ? 32.600 1.521   11.986  1.00 12.65 ?  84  SER   A CA   1 
ATOM   1825 C  C    . SER   A 1 84  ? 31.083 1.606   11.834  1.00 12.32 ?  84  SER   A C    1 
ATOM   1826 O  O    . SER   A 1 84  ? 30.560 2.064   10.817  1.00 12.53 ?  84  SER   A O    1 
ATOM   1827 C  CB   . SER   A 1 84  ? 33.101 2.844   12.555  1.00 13.36 ?  84  SER   A CB   1 
ATOM   1828 O  OG   . SER   A 1 84  ? 32.457 3.126   13.780  1.00 14.41 ?  84  SER   A OG   1 
ATOM   1829 H  H    . SER   A 1 84  ? 33.750 1.898   10.412  1.00 14.79 ?  84  SER   A H    1 
ATOM   1830 H  HA   . SER   A 1 84  ? 32.820 0.812   12.604  1.00 15.19 ?  84  SER   A HA   1 
ATOM   1831 H  HB2  . SER   A 1 84  ? 34.060 2.789   12.697  1.00 16.04 ?  84  SER   A HB2  1 
ATOM   1832 H  HB3  . SER   A 1 84  ? 32.901 3.557   11.926  1.00 16.04 ?  84  SER   A HB3  1 
ATOM   1833 H  HG   . SER   A 1 84  ? 32.743 3.851   14.096  1.00 17.31 ?  84  SER   A HG   1 
ATOM   1834 N  N    . GLY   A 1 85  ? 30.372 1.193   12.881  1.00 13.35 ?  85  GLY   A N    1 
ATOM   1835 C  CA   . GLY   A 1 85  ? 28.949 1.426   12.970  1.00 13.88 ?  85  GLY   A CA   1 
ATOM   1836 C  C    . GLY   A 1 85  ? 28.579 2.748   13.605  1.00 13.82 ?  85  GLY   A C    1 
ATOM   1837 O  O    . GLY   A 1 85  ? 27.389 3.068   13.707  1.00 14.27 ?  85  GLY   A O    1 
ATOM   1838 H  H    . GLY   A 1 85  ? 30.709 0.769   13.555  1.00 16.02 ?  85  GLY   A H    1 
ATOM   1839 H  HA2  . GLY   A 1 85  ? 28.574 1.399   12.078  1.00 16.66 ?  85  GLY   A HA2  1 
ATOM   1840 H  HA3  . GLY   A 1 85  ? 28.548 0.715   13.489  1.00 16.66 ?  85  GLY   A HA3  1 
ATOM   1841 N  N    . HIS   A 1 86  ? 29.565 3.524   14.043  1.00 13.57 ?  86  HIS   A N    1 
ATOM   1842 C  CA   . HIS   A 1 86  ? 29.346 4.865   14.601  1.00 14.05 ?  86  HIS   A CA   1 
ATOM   1843 C  C    . HIS   A 1 86  ? 28.361 4.753   15.757  1.00 14.70 ?  86  HIS   A C    1 
ATOM   1844 O  O    . HIS   A 1 86  ? 28.546 3.883   16.624  1.00 15.81 ?  86  HIS   A O    1 
ATOM   1845 C  CB   . HIS   A 1 86  ? 28.978 5.844   13.494  1.00 13.99 ?  86  HIS   A CB   1 
ATOM   1846 C  CG   . HIS   A 1 86  ? 30.034 5.934   12.453  1.00 13.73 ?  86  HIS   A CG   1 
ATOM   1847 N  ND1  . HIS   A 1 86  ? 31.124 6.770   12.576  1.00 14.66 ?  86  HIS   A ND1  1 
ATOM   1848 C  CD2  . HIS   A 1 86  ? 30.216 5.234   11.311  1.00 13.38 ?  86  HIS   A CD2  1 
ATOM   1849 C  CE1  . HIS   A 1 86  ? 31.917 6.597   11.533  1.00 14.47 ?  86  HIS   A CE1  1 
ATOM   1850 N  NE2  . HIS   A 1 86  ? 31.395 5.664   10.758  1.00 13.67 ?  86  HIS   A NE2  1 
ATOM   1851 H  H    . HIS   A 1 86  ? 30.390 3.299   14.034  1.00 16.29 ?  86  HIS   A H    1 
ATOM   1852 H  HA   . HIS   A 1 86  ? 30.182 5.174   14.974  1.00 16.87 ?  86  HIS   A HA   1 
ATOM   1853 H  HB2  . HIS   A 1 86  ? 28.155 5.559   13.066  1.00 16.80 ?  86  HIS   A HB2  1 
ATOM   1854 H  HB3  . HIS   A 1 86  ? 28.860 6.734   13.873  1.00 16.80 ?  86  HIS   A HB3  1 
ATOM   1855 H  HD2  . HIS   A 1 86  ? 29.653 4.572   10.966  1.00 16.07 ?  86  HIS   A HD2  1 
ATOM   1856 H  HE1  . HIS   A 1 86  ? 32.711 7.052   11.363  1.00 17.37 ?  86  HIS   A HE1  1 
ATOM   1857 H  HE2  . HIS   A 1 86  ? 31.731 5.381   10.009  1.00 16.41 ?  86  HIS   A HE2  1 
ATOM   1858 N  N    . ASN   A 1 87  ? 27.346 5.604   15.820  1.00 15.58 ?  87  ASN   A N    1 
ATOM   1859 C  CA   . ASN   A 1 87  ? 26.364 5.597   16.888  1.00 16.66 ?  87  ASN   A CA   1 
ATOM   1860 C  C    . ASN   A 1 87  ? 25.234 4.607   16.649  1.00 17.60 ?  87  ASN   A C    1 
ATOM   1861 O  O    . ASN   A 1 87  ? 24.316 4.541   17.469  1.00 19.64 ?  87  ASN   A O    1 
ATOM   1862 C  CB   . ASN   A 1 87  ? 25.778 7.008   17.045  1.00 17.22 ?  87  ASN   A CB   1 
ATOM   1863 C  CG   . ASN   A 1 87  ? 25.264 7.579   15.731  1.00 18.37 ?  87  ASN   A CG   1 
ATOM   1864 O  OD1  . ASN   A 1 87  ? 25.901 7.447   14.688  1.00 18.82 ?  87  ASN   A OD1  1 
ATOM   1865 N  ND2  . ASN   A 1 87  ? 24.107 8.217   15.778  1.00 19.26 ?  87  ASN   A ND2  1 
ATOM   1866 H  H    . ASN   A 1 87  ? 27.195 6.209   15.234  1.00 18.70 ?  87  ASN   A H    1 
ATOM   1867 H  HA   . ASN   A 1 87  ? 26.795 5.357   17.728  1.00 20.00 ?  87  ASN   A HA   1 
ATOM   1868 H  HB2  . ASN   A 1 87  ? 25.034 6.974   17.675  1.00 20.68 ?  87  ASN   A HB2  1 
ATOM   1869 H  HB3  . ASN   A 1 87  ? 26.467 7.599   17.384  1.00 20.68 ?  87  ASN   A HB3  1 
ATOM   1870 H  HD21 . ASN   A 1 87  ? 23.777 8.550   15.060  1.00 23.12 ?  87  ASN   A HD21 1 
ATOM   1871 H  HD22 . ASN   A 1 87  ? 23.691 8.302   16.526  1.00 23.12 ?  87  ASN   A HD22 1 
ATOM   1872 N  N    . LEU   A 1 88  ? 25.283 3.832   15.570  1.00 16.12 ?  88  LEU   A N    1 
ATOM   1873 C  CA   . LEU   A 1 88  ? 24.174 2.964   15.183  1.00 16.01 ?  88  LEU   A CA   1 
ATOM   1874 C  C    . LEU   A 1 88  ? 24.394 1.488   15.488  1.00 15.71 ?  88  LEU   A C    1 
ATOM   1875 O  O    . LEU   A 1 88  ? 23.417 0.753   15.656  1.00 17.00 ?  88  LEU   A O    1 
ATOM   1876 C  CB   . LEU   A 1 88  ? 23.914 3.113   13.682  1.00 16.08 ?  88  LEU   A CB   1 
ATOM   1877 C  CG   . LEU   A 1 88  ? 23.630 4.536   13.201  1.00 17.89 ?  88  LEU   A CG   1 
ATOM   1878 C  CD1  . LEU   A 1 88  ? 23.490 4.546   11.692  1.00 18.12 ?  88  LEU   A CD1  1 
ATOM   1879 C  CD2  . LEU   A 1 88  ? 22.378 5.098   13.864  1.00 19.57 ?  88  LEU   A CD2  1 
ATOM   1880 H  H    . LEU   A 1 88  ? 25.957 3.794   15.047  1.00 19.35 ?  88  LEU   A H    1 
ATOM   1881 H  HA   . LEU   A 1 88  ? 23.375 3.246   15.655  1.00 19.22 ?  88  LEU   A HA   1 
ATOM   1882 H  HB2  . LEU   A 1 88  ? 24.690 2.799   13.199  1.00 19.31 ?  88  LEU   A HB2  1 
ATOM   1883 H  HB3  . LEU   A 1 88  ? 23.142 2.574   13.449  1.00 19.31 ?  88  LEU   A HB3  1 
ATOM   1884 H  HG   . LEU   A 1 88  ? 24.375 5.110   13.436  1.00 21.48 ?  88  LEU   A HG   1 
ATOM   1885 H  HD11 . LEU   A 1 88  ? 23.326 5.455   11.393  1.00 21.76 ?  88  LEU   A HD11 1 
ATOM   1886 H  HD12 . LEU   A 1 88  ? 24.310 4.211   11.298  1.00 21.76 ?  88  LEU   A HD12 1 
ATOM   1887 H  HD13 . LEU   A 1 88  ? 22.745 3.977   11.440  1.00 21.76 ?  88  LEU   A HD13 1 
ATOM   1888 H  HD21 . LEU   A 1 88  ? 22.165 5.955   13.461  1.00 23.49 ?  88  LEU   A HD21 1 
ATOM   1889 H  HD22 . LEU   A 1 88  ? 21.645 4.478   13.729  1.00 23.49 ?  88  LEU   A HD22 1 
ATOM   1890 H  HD23 . LEU   A 1 88  ? 22.546 5.212   14.811  1.00 23.49 ?  88  LEU   A HD23 1 
ATOM   1891 N  N    . ALA   A 1 89  ? 25.642 1.039   15.537  1.00 15.29 ?  89  ALA   A N    1 
ATOM   1892 C  CA   . ALA   A 1 89  ? 25.978 -0.374  15.635  1.00 14.93 ?  89  ALA   A CA   1 
ATOM   1893 C  C    . ALA   A 1 89  ? 27.461 -0.448  15.954  1.00 15.33 ?  89  ALA   A C    1 
ATOM   1894 O  O    . ALA   A 1 89  ? 28.180 0.544   15.839  1.00 16.06 ?  89  ALA   A O    1 
ATOM   1895 C  CB   . ALA   A 1 89  ? 25.693 -1.085  14.314  1.00 14.47 ?  89  ALA   A CB   1 
ATOM   1896 H  H    . ALA   A 1 89  ? 26.331 1.551   15.503  1.00 18.36 ?  89  ALA   A H    1 
ATOM   1897 H  HA   . ALA   A 1 89  ? 25.470 -0.791  16.350  1.00 17.93 ?  89  ALA   A HA   1 
ATOM   1898 H  HB1  . ALA   A 1 89  ? 25.934 -2.022  14.402  1.00 17.38 ?  89  ALA   A HB1  1 
ATOM   1899 H  HB2  . ALA   A 1 89  ? 24.745 -1.009  14.110  1.00 17.38 ?  89  ALA   A HB2  1 
ATOM   1900 H  HB3  . ALA   A 1 89  ? 26.216 -0.673  13.612  1.00 17.38 ?  89  ALA   A HB3  1 
ATOM   1901 N  N    . LYS   A 1 90  ? 27.930 -1.628  16.351  1.00 15.88 ?  90  LYS   A N    1 
ATOM   1902 C  CA   . LYS   A 1 90  ? 29.373 -1.786  16.497  1.00 16.71 ?  90  LYS   A CA   1 
ATOM   1903 C  C    . LYS   A 1 90  ? 30.073 -1.595  15.154  1.00 15.67 ?  90  LYS   A C    1 
ATOM   1904 O  O    . LYS   A 1 90  ? 31.010 -0.788  15.026  1.00 16.71 ?  90  LYS   A O    1 
ATOM   1905 C  CB   . LYS   A 1 90  ? 29.707 -3.148  17.107  1.00 19.25 ?  90  LYS   A CB   1 
ATOM   1906 C  CG   . LYS   A 1 90  ? 31.191 -3.312  17.419  1.00 24.64 ?  90  LYS   A CG   1 
ATOM   1907 C  CD   . LYS   A 1 90  ? 31.435 -4.517  18.311  1.00 30.75 ?  90  LYS   A CD   1 
ATOM   1908 C  CE   . LYS   A 1 90  ? 32.847 -4.524  18.886  1.00 35.50 ?  90  LYS   A CE   1 
ATOM   1909 N  NZ   . LYS   A 1 90  ? 33.867 -4.966  17.898  1.00 38.59 ?  90  LYS   A NZ   1 
ATOM   1910 H  H    . LYS   A 1 90  ? 27.453 -2.317  16.539  1.00 19.06 ?  90  LYS   A H    1 
ATOM   1911 H  HA   . LYS   A 1 90  ? 29.702 -1.104  17.099  1.00 20.06 ?  90  LYS   A HA   1 
ATOM   1912 H  HB2  . LYS   A 1 90  ? 29.214 -3.253  17.938  1.00 23.10 ?  90  LYS   A HB2  1 
ATOM   1913 H  HB3  . LYS   A 1 90  ? 29.453 -3.848  16.485  1.00 23.10 ?  90  LYS   A HB3  1 
ATOM   1914 H  HG2  . LYS   A 1 90  ? 31.682 -3.439  16.592  1.00 29.58 ?  90  LYS   A HG2  1 
ATOM   1915 H  HG3  . LYS   A 1 90  ? 31.511 -2.521  17.881  1.00 29.58 ?  90  LYS   A HG3  1 
ATOM   1916 H  HD2  . LYS   A 1 90  ? 30.809 -4.500  19.052  1.00 36.91 ?  90  LYS   A HD2  1 
ATOM   1917 H  HD3  . LYS   A 1 90  ? 31.318 -5.329  17.792  1.00 36.91 ?  90  LYS   A HD3  1 
ATOM   1918 H  HE2  . LYS   A 1 90  ? 33.077 -3.625  19.172  1.00 42.61 ?  90  LYS   A HE2  1 
ATOM   1919 H  HE3  . LYS   A 1 90  ? 32.879 -5.130  19.643  1.00 42.61 ?  90  LYS   A HE3  1 
ATOM   1920 H  HZ1  . LYS   A 1 90  ? 33.680 -5.790  17.617  1.00 46.31 ?  90  LYS   A HZ1  1 
ATOM   1921 H  HZ2  . LYS   A 1 90  ? 33.874 -4.416  17.200  1.00 46.31 ?  90  LYS   A HZ2  1 
ATOM   1922 H  HZ3  . LYS   A 1 90  ? 34.675 -4.967  18.274  1.00 46.31 ?  90  LYS   A HZ3  1 
ATOM   1923 N  N    . HIS   A 1 91  ? 29.605 -2.312  14.133  1.00 14.06 ?  91  HIS   A N    1 
ATOM   1924 C  CA   . HIS   A 1 91  ? 30.189 -2.308  12.807  1.00 13.32 ?  91  HIS   A CA   1 
ATOM   1925 C  C    . HIS   A 1 91  ? 29.113 -2.021  11.780  1.00 12.05 ?  91  HIS   A C    1 
ATOM   1926 O  O    . HIS   A 1 91  ? 27.944 -2.367  11.969  1.00 12.87 ?  91  HIS   A O    1 
ATOM   1927 C  CB   . HIS   A 1 91  ? 30.771 -3.680  12.453  1.00 15.86 ?  91  HIS   A CB   1 
ATOM   1928 C  CG   . HIS   A 1 91  ? 31.770 -4.188  13.439  1.00 19.90 ?  91  HIS   A CG   1 
ATOM   1929 N  ND1  . HIS   A 1 91  ? 33.053 -3.691  13.520  1.00 21.84 ?  91  HIS   A ND1  1 
ATOM   1930 C  CD2  . HIS   A 1 91  ? 31.682 -5.157  14.380  1.00 21.74 ?  91  HIS   A CD2  1 
ATOM   1931 C  CE1  . HIS   A 1 91  ? 33.712 -4.330  14.470  1.00 22.79 ?  91  HIS   A CE1  1 
ATOM   1932 N  NE2  . HIS   A 1 91  ? 32.902 -5.226  15.008  1.00 22.89 ?  91  HIS   A NE2  1 
ATOM   1933 H  H    . HIS   A 1 91  ? 28.918 -2.840  14.196  1.00 16.88 ?  91  HIS   A H    1 
ATOM   1934 H  HA   . HIS   A 1 91  ? 30.887 -1.639  12.746  1.00 16.00 ?  91  HIS   A HA   1 
ATOM   1935 H  HB2  . HIS   A 1 91  ? 30.047 -4.326  12.410  1.00 19.04 ?  91  HIS   A HB2  1 
ATOM   1936 H  HB3  . HIS   A 1 91  ? 31.208 -3.621  11.589  1.00 19.04 ?  91  HIS   A HB3  1 
ATOM   1937 H  HD1  . HIS   A 1 91  ? 33.376 -3.063  13.024  1.00 26.21 ?  91  HIS   A HD1  1 
ATOM   1938 H  HD2  . HIS   A 1 91  ? 30.941 -5.680  14.569  1.00 26.10 ?  91  HIS   A HD2  1 
ATOM   1939 H  HE1  . HIS   A 1 91  ? 34.599 -4.171  14.717  1.00 27.36 ?  91  HIS   A HE1  1 
ATOM   1940 N  N    . CYS   A 1 92  ? 29.523 -1.426  10.667  1.00 11.96 ?  92  CYS   A N    1 
ATOM   1941 C  CA   . CYS   A 1 92  ? 28.690 -1.352  9.474   1.00 11.64 ?  92  CYS   A CA   1 
ATOM   1942 C  C    . CYS   A 1 92  ? 29.341 -2.174  8.370   1.00 11.26 ?  92  CYS   A C    1 
ATOM   1943 O  O    . CYS   A 1 92  ? 30.502 -1.932  8.012   1.00 11.83 ?  92  CYS   A O    1 
ATOM   1944 C  CB   . CYS   A 1 92  ? 28.477 0.089   9.010   1.00 11.77 ?  92  CYS   A CB   1 
ATOM   1945 S  SG   . CYS   A 1 92  ? 27.477 0.187   7.491   1.00 11.31 ?  92  CYS   A SG   1 
ATOM   1946 H  H    . CYS   A 1 92  ? 30.294 -1.049  10.577  1.00 14.36 ?  92  CYS   A H    1 
ATOM   1947 H  HA   . CYS   A 1 92  ? 27.824 -1.737  9.668   1.00 13.98 ?  92  CYS   A HA   1 
ATOM   1948 H  HB2  . CYS   A 1 92  ? 28.017 0.584   9.708   1.00 14.13 ?  92  CYS   A HB2  1 
ATOM   1949 H  HB3  . CYS   A 1 92  ? 29.338 0.497   8.827   1.00 14.13 ?  92  CYS   A HB3  1 
ATOM   1950 H  HG   . CYS   A 1 92  ? 27.336 1.343   7.202   1.00 13.58 ?  92  CYS   A HG   1 
ATOM   1951 N  N    . LEU   A 1 93  ? 28.609 -3.168  7.868   1.00 11.05 ?  93  LEU   A N    1 
ATOM   1952 C  CA   . LEU   A 1 93  ? 29.019 -3.928  6.694   1.00 10.55 ?  93  LEU   A CA   1 
ATOM   1953 C  C    . LEU   A 1 93  ? 28.428 -3.240  5.469   1.00 10.11 ?  93  LEU   A C    1 
ATOM   1954 O  O    . LEU   A 1 93  ? 27.217 -3.295  5.237   1.00 10.30 ?  93  LEU   A O    1 
ATOM   1955 C  CB   . LEU   A 1 93  ? 28.534 -5.372  6.803   1.00 11.18 ?  93  LEU   A CB   1 
ATOM   1956 C  CG   . LEU   A 1 93  ? 28.924 -6.272  5.632   1.00 11.42 ?  93  LEU   A CG   1 
ATOM   1957 C  CD1  . LEU   A 1 93  ? 30.426 -6.542  5.626   1.00 12.47 ?  93  LEU   A CD1  1 
ATOM   1958 C  CD2  . LEU   A 1 93  ? 28.148 -7.596  5.675   1.00 12.12 ?  93  LEU   A CD2  1 
ATOM   1959 H  H    . LEU   A 1 93  ? 27.857 -3.422  8.204   1.00 13.27 ?  93  LEU   A H    1 
ATOM   1960 H  HA   . LEU   A 1 93  ? 29.982 -3.920  6.624   1.00 12.67 ?  93  LEU   A HA   1 
ATOM   1961 H  HB2  . LEU   A 1 93  ? 28.913 -5.759  7.611   1.00 13.43 ?  93  LEU   A HB2  1 
ATOM   1962 H  HB3  . LEU   A 1 93  ? 27.570 -5.372  6.864   1.00 13.43 ?  93  LEU   A HB3  1 
ATOM   1963 H  HG   . LEU   A 1 93  ? 28.707 -5.828  4.804   1.00 13.72 ?  93  LEU   A HG   1 
ATOM   1964 H  HD11 . LEU   A 1 93  ? 30.639 -7.155  4.905   1.00 14.98 ?  93  LEU   A HD11 1 
ATOM   1965 H  HD12 . LEU   A 1 93  ? 30.902 -5.707  5.502   1.00 14.98 ?  93  LEU   A HD12 1 
ATOM   1966 H  HD13 . LEU   A 1 93  ? 30.683 -6.941  6.479   1.00 14.98 ?  93  LEU   A HD13 1 
ATOM   1967 H  HD21 . LEU   A 1 93  ? 28.421 -8.145  4.922   1.00 14.55 ?  93  LEU   A HD21 1 
ATOM   1968 H  HD22 . LEU   A 1 93  ? 28.346 -8.054  6.506   1.00 14.55 ?  93  LEU   A HD22 1 
ATOM   1969 H  HD23 . LEU   A 1 93  ? 27.200 -7.404  5.618   1.00 14.55 ?  93  LEU   A HD23 1 
ATOM   1970 N  N    . HIS   A 1 94  ? 29.280 -2.549  4.710   1.00 10.11 ?  94  HIS   A N    1 
ATOM   1971 C  CA   . HIS   A 1 94  ? 28.861 -1.874  3.484   1.00 10.06 ?  94  HIS   A CA   1 
ATOM   1972 C  C    . HIS   A 1 94  ? 28.875 -2.907  2.371   1.00 9.95  ?  94  HIS   A C    1 
ATOM   1973 O  O    . HIS   A 1 94  ? 29.939 -3.423  2.027   1.00 11.76 ?  94  HIS   A O    1 
ATOM   1974 C  CB   . HIS   A 1 94  ? 29.823 -0.734  3.157   1.00 10.14 ?  94  HIS   A CB   1 
ATOM   1975 C  CG   . HIS   A 1 94  ? 29.809 0.361   4.168   1.00 10.19 ?  94  HIS   A CG   1 
ATOM   1976 N  ND1  . HIS   A 1 94  ? 28.931 1.424   4.107   1.00 10.46 ?  94  HIS   A ND1  1 
ATOM   1977 C  CD2  . HIS   A 1 94  ? 30.549 0.535   5.287   1.00 10.92 ?  94  HIS   A CD2  1 
ATOM   1978 C  CE1  . HIS   A 1 94  ? 29.145 2.210   5.148   1.00 10.58 ?  94  HIS   A CE1  1 
ATOM   1979 N  NE2  . HIS   A 1 94  ? 30.117 1.690   5.879   1.00 11.08 ?  94  HIS   A NE2  1 
ATOM   1980 H  H    . HIS   A 1 94  ? 30.115 -2.448  4.890   1.00 12.14 ?  94  HIS   A H    1 
ATOM   1981 H  HA   . HIS   A 1 94  ? 27.957 -1.522  3.584   1.00 12.08 ?  94  HIS   A HA   1 
ATOM   1982 H  HB2  . HIS   A 1 94  ? 30.717 -1.085  3.113   1.00 12.17 ?  94  HIS   A HB2  1 
ATOM   1983 H  HB3  . HIS   A 1 94  ? 29.566 -0.348  2.304   1.00 12.17 ?  94  HIS   A HB3  1 
ATOM   1984 H  HD2  . HIS   A 1 94  ? 31.220 -0.019  5.599   1.00 13.12 ?  94  HIS   A HD2  1 
ATOM   1985 H  HE1  . HIS   A 1 94  ? 28.675 2.996   5.336   1.00 12.70 ?  94  HIS   A HE1  1 
ATOM   1986 H  HE2  . HIS   A 1 94  ? 30.427 2.040   6.602   1.00 13.31 ?  94  HIS   A HE2  1 
ATOM   1987 N  N    . VAL   A 1 95  ? 27.702 -3.234  1.827   1.00 9.82  ?  95  VAL   A N    1 
ATOM   1988 C  CA   . VAL   A 1 95  ? 27.562 -4.272  0.809   1.00 9.94  ?  95  VAL   A CA   1 
ATOM   1989 C  C    . VAL   A 1 95  ? 27.024 -3.639  -0.461  1.00 9.92  ?  95  VAL   A C    1 
ATOM   1990 O  O    . VAL   A 1 95  ? 26.016 -2.921  -0.415  1.00 10.52 ?  95  VAL   A O    1 
ATOM   1991 C  CB   . VAL   A 1 95  ? 26.632 -5.414  1.261   1.00 10.60 ?  95  VAL   A CB   1 
ATOM   1992 C  CG1  . VAL   A 1 95  ? 26.526 -6.449  0.157   1.00 11.44 ?  95  VAL   A CG1  1 
ATOM   1993 C  CG2  . VAL   A 1 95  ? 27.130 -6.037  2.552   1.00 11.02 ?  95  VAL   A CG2  1 
ATOM   1994 H  H    . VAL   A 1 95  ? 26.952 -2.866  2.042   1.00 11.79 ?  95  VAL   A H    1 
ATOM   1995 H  HA   . VAL   A 1 95  ? 28.431 -4.650  0.614   1.00 11.94 ?  95  VAL   A HA   1 
ATOM   1996 H  HB   . VAL   A 1 95  ? 25.747 -5.060  1.421   1.00 12.73 ?  95  VAL   A HB   1 
ATOM   1997 H  HG11 . VAL   A 1 95  ? 26.150 -7.268  0.523   1.00 13.74 ?  95  VAL   A HG11 1 
ATOM   1998 H  HG12 . VAL   A 1 95  ? 25.949 -6.112  -0.547  1.00 13.74 ?  95  VAL   A HG12 1 
ATOM   1999 H  HG13 . VAL   A 1 95  ? 27.412 -6.630  -0.200  1.00 13.74 ?  95  VAL   A HG13 1 
ATOM   2000 H  HG21 . VAL   A 1 95  ? 26.566 -6.796  2.773   1.00 13.24 ?  95  VAL   A HG21 1 
ATOM   2001 H  HG22 . VAL   A 1 95  ? 28.045 -6.328  2.430   1.00 13.24 ?  95  VAL   A HG22 1 
ATOM   2002 H  HG23 . VAL   A 1 95  ? 27.081 -5.373  3.257   1.00 13.24 ?  95  VAL   A HG23 1 
ATOM   2003 N  N    . VAL   A 1 96  ? 27.658 -3.933  -1.593  1.00 9.86  ?  96  VAL   A N    1 
ATOM   2004 C  CA   . VAL   A 1 96  ? 27.251 -3.380  -2.879  1.00 10.50 ?  96  VAL   A CA   1 
ATOM   2005 C  C    . VAL   A 1 96  ? 26.448 -4.432  -3.635  1.00 10.76 ?  96  VAL   A C    1 
ATOM   2006 O  O    . VAL   A 1 96  ? 27.011 -5.380  -4.194  1.00 11.84 ?  96  VAL   A O    1 
ATOM   2007 C  CB   . VAL   A 1 96  ? 28.444 -2.907  -3.704  1.00 10.67 ?  96  VAL   A CB   1 
ATOM   2008 C  CG1  . VAL   A 1 96  ? 27.941 -2.269  -4.972  1.00 11.04 ?  96  VAL   A CG1  1 
ATOM   2009 C  CG2  . VAL   A 1 96  ? 29.308 -1.940  -2.905  1.00 11.25 ?  96  VAL   A CG2  1 
ATOM   2010 H  H    . VAL   A 1 96  ? 28.348 -4.450  -1.636  1.00 11.84 ?  96  VAL   A H    1 
ATOM   2011 H  HA   . VAL   A 1 96  ? 26.677 -2.617  -2.722  1.00 12.61 ?  96  VAL   A HA   1 
ATOM   2012 H  HB   . VAL   A 1 96  ? 28.992 -3.665  -3.943  1.00 12.82 ?  96  VAL   A HB   1 
ATOM   2013 H  HG11 . VAL   A 1 96  ? 28.673 -1.790  -5.391  1.00 13.25 ?  96  VAL   A HG11 1 
ATOM   2014 H  HG12 . VAL   A 1 96  ? 27.613 -2.958  -5.564  1.00 13.25 ?  96  VAL   A HG12 1 
ATOM   2015 H  HG13 . VAL   A 1 96  ? 27.228 -1.647  -4.751  1.00 13.25 ?  96  VAL   A HG13 1 
ATOM   2016 H  HG21 . VAL   A 1 96  ? 30.008 -1.589  -3.472  1.00 13.51 ?  96  VAL   A HG21 1 
ATOM   2017 H  HG22 . VAL   A 1 96  ? 28.751 -1.210  -2.577  1.00 13.51 ?  96  VAL   A HG22 1 
ATOM   2018 H  HG23 . VAL   A 1 96  ? 29.698 -2.411  -2.149  1.00 13.51 ?  96  VAL   A HG23 1 
ATOM   2019 N  N    . GLY   A 1 97  ? 25.131 -4.270  -3.669  1.00 10.78 ?  97  GLY   A N    1 
ATOM   2020 C  CA   . GLY   A 1 97  ? 24.322 -5.039  -4.576  1.00 11.29 ?  97  GLY   A CA   1 
ATOM   2021 C  C    . GLY   A 1 97  ? 24.328 -4.389  -5.946  1.00 11.50 ?  97  GLY   A C    1 
ATOM   2022 O  O    . GLY   A 1 97  ? 24.609 -3.191  -6.086  1.00 12.30 ?  97  GLY   A O    1 
ATOM   2023 H  H    . GLY   A 1 97  ? 24.692 -3.714  -3.175  1.00 12.95 ?  97  GLY   A H    1 
ATOM   2024 H  HA2  . GLY   A 1 97  ? 24.682 -5.936  -4.631  1.00 13.56 ?  97  GLY   A HA2  1 
ATOM   2025 H  HA3  . GLY   A 1 97  ? 23.410 -5.085  -4.244  1.00 13.56 ?  97  GLY   A HA3  1 
ATOM   2026 N  N    A PRO   A 1 98  ? 23.973 -5.129  -6.990  0.64 11.73 ?  98  PRO   A N    1 
ATOM   2027 N  N    B PRO   A 1 98  ? 24.074 -5.197  -6.976  0.36 11.77 ?  98  PRO   A N    1 
ATOM   2028 C  CA   A PRO   A 1 98  ? 23.839 -4.494  -8.308  0.64 12.52 ?  98  PRO   A CA   1 
ATOM   2029 C  CA   B PRO   A 1 98  ? 24.054 -4.675  -8.345  0.36 12.46 ?  98  PRO   A CA   1 
ATOM   2030 C  C    A PRO   A 1 98  ? 22.727 -3.451  -8.320  0.64 12.22 ?  98  PRO   A C    1 
ATOM   2031 C  C    B PRO   A 1 98  ? 22.915 -3.693  -8.549  0.36 12.51 ?  98  PRO   A C    1 
ATOM   2032 O  O    A PRO   A 1 98  ? 21.662 -3.641  -7.729  0.64 12.24 ?  98  PRO   A O    1 
ATOM   2033 O  O    B PRO   A 1 98  ? 21.816 -3.854  -8.014  0.36 13.05 ?  98  PRO   A O    1 
ATOM   2034 C  CB   A PRO   A 1 98  ? 23.520 -5.671  -9.237  0.64 12.22 ?  98  PRO   A CB   1 
ATOM   2035 C  CB   B PRO   A 1 98  ? 23.855 -5.933  -9.201  0.36 12.52 ?  98  PRO   A CB   1 
ATOM   2036 C  CG   A PRO   A 1 98  ? 22.910 -6.700  -8.347  0.64 12.32 ?  98  PRO   A CG   1 
ATOM   2037 C  CG   B PRO   A 1 98  ? 23.226 -6.930  -8.276  0.36 12.81 ?  98  PRO   A CG   1 
ATOM   2038 C  CD   A PRO   A 1 98  ? 23.631 -6.562  -7.027  0.64 11.98 ?  98  PRO   A CD   1 
ATOM   2039 C  CD   B PRO   A 1 98  ? 23.841 -6.652  -6.937  0.36 11.98 ?  98  PRO   A CD   1 
ATOM   2040 H  HA   A PRO   A 1 98  ? 24.675 -4.087  -8.570  0.64 15.03 ?  98  PRO   A HA   1 
ATOM   2041 H  HA   B PRO   A 1 98  ? 24.901 -4.258  -8.565  0.36 14.97 ?  98  PRO   A HA   1 
ATOM   2042 H  HB2  A PRO   A 1 98  ? 22.888 -5.388  -9.917  0.64 14.67 ?  98  PRO   A HB2  1 
ATOM   2043 H  HB2  B PRO   A 1 98  ? 23.263 -5.734  -9.944  0.36 15.03 ?  98  PRO   A HB2  1 
ATOM   2044 H  HB3  A PRO   A 1 98  ? 24.337 -6.001  -9.640  0.64 14.67 ?  98  PRO   A HB3  1 
ATOM   2045 H  HB3  B PRO   A 1 98  ? 24.712 -6.256  -9.520  0.36 15.03 ?  98  PRO   A HB3  1 
ATOM   2046 H  HG2  A PRO   A 1 98  ? 21.964 -6.523  -8.240  0.64 14.79 ?  98  PRO   A HG2  1 
ATOM   2047 H  HG2  B PRO   A 1 98  ? 22.266 -6.789  -8.249  0.36 15.39 ?  98  PRO   A HG2  1 
ATOM   2048 H  HG3  A PRO   A 1 98  ? 23.055 -7.583  -8.724  0.64 14.79 ?  98  PRO   A HG3  1 
ATOM   2049 H  HG3  B PRO   A 1 98  ? 23.433 -7.829  -8.574  0.36 15.39 ?  98  PRO   A HG3  1 
ATOM   2050 H  HD2  A PRO   A 1 98  ? 23.038 -6.800  -6.293  0.64 14.39 ?  98  PRO   A HD2  1 
ATOM   2051 H  HD2  B PRO   A 1 98  ? 23.221 -6.887  -6.227  0.36 14.38 ?  98  PRO   A HD2  1 
ATOM   2052 H  HD3  A PRO   A 1 98  ? 24.436 -7.104  -7.021  0.64 14.39 ?  98  PRO   A HD3  1 
ATOM   2053 H  HD3  B PRO   A 1 98  ? 24.682 -7.131  -6.845  0.36 14.38 ?  98  PRO   A HD3  1 
ATOM   2054 N  N    A ASN   A 1 99  ? 22.993 -2.330  -8.991  0.64 12.77 ?  99  ASN   A N    1 
ATOM   2055 N  N    B ASN   A 1 99  ? 23.194 -2.669  -9.339  0.36 12.68 ?  99  ASN   A N    1 
ATOM   2056 C  CA   A ASN   A 1 99  ? 22.009 -1.269  -9.187  0.64 13.36 ?  99  ASN   A CA   1 
ATOM   2057 C  CA   B ASN   A 1 99  ? 22.218 -1.648  -9.689  0.36 13.26 ?  99  ASN   A CA   1 
ATOM   2058 C  C    A ASN   A 1 99  ? 21.447 -1.405  -10.598 0.64 14.32 ?  99  ASN   A C    1 
ATOM   2059 C  C    B ASN   A 1 99  ? 21.683 -1.971  -11.079 0.36 13.82 ?  99  ASN   A C    1 
ATOM   2060 O  O    A ASN   A 1 99  ? 22.126 -1.088  -11.582 0.64 15.57 ?  99  ASN   A O    1 
ATOM   2061 O  O    B ASN   A 1 99  ? 22.389 -1.805  -12.080 0.36 13.57 ?  99  ASN   A O    1 
ATOM   2062 C  CB   A ASN   A 1 99  ? 22.644 0.105   -8.976  0.64 13.30 ?  99  ASN   A CB   1 
ATOM   2063 C  CB   B ASN   A 1 99  ? 22.878 -0.274  -9.663  0.36 14.19 ?  99  ASN   A CB   1 
ATOM   2064 C  CG   A ASN   A 1 99  ? 21.621 1.239   -8.985  0.64 13.83 ?  99  ASN   A CG   1 
ATOM   2065 C  CG   B ASN   A 1 99  ? 21.895 0.846   -9.897  0.36 15.25 ?  99  ASN   A CG   1 
ATOM   2066 O  OD1  A ASN   A 1 99  ? 20.633 1.195   -9.719  0.64 14.42 ?  99  ASN   A OD1  1 
ATOM   2067 O  OD1  B ASN   A 1 99  ? 20.922 0.685   -10.627 0.36 15.19 ?  99  ASN   A OD1  1 
ATOM   2068 N  ND2  A ASN   A 1 99  ? 21.866 2.262   -8.173  0.64 14.17 ?  99  ASN   A ND2  1 
ATOM   2069 N  ND2  B ASN   A 1 99  ? 22.139 1.989   -9.271  0.36 16.61 ?  99  ASN   A ND2  1 
ATOM   2070 H  H    A ASN   A 1 99  ? 23.758 -2.156  -9.337  0.64 15.33 ?  99  ASN   A H    1 
ATOM   2071 H  H    B ASN   A 1 99  ? 23.969 -2.536  -9.685  0.36 15.22 ?  99  ASN   A H    1 
ATOM   2072 H  HA   A ASN   A 1 99  ? 21.282 -1.377  -8.546  0.64 16.04 ?  99  ASN   A HA   1 
ATOM   2073 H  HA   B ASN   A 1 99  ? 21.483 -1.664  -9.053  0.36 15.92 ?  99  ASN   A HA   1 
ATOM   2074 H  HB2  A ASN   A 1 99  ? 23.101 0.117   -8.124  0.64 15.97 ?  99  ASN   A HB2  1 
ATOM   2075 H  HB2  B ASN   A 1 99  ? 23.290 -0.138  -8.797  0.36 17.04 ?  99  ASN   A HB2  1 
ATOM   2076 H  HB3  A ASN   A 1 99  ? 23.275 0.267   -9.696  0.64 15.97 ?  99  ASN   A HB3  1 
ATOM   2077 H  HB3  B ASN   A 1 99  ? 23.546 -0.240  -10.362 0.36 17.04 ?  99  ASN   A HB3  1 
ATOM   2078 H  HD21 A ASN   A 1 99  ? 21.320 2.924   -8.139  0.64 17.02 ?  99  ASN   A HD21 1 
ATOM   2079 H  HD21 B ASN   A 1 99  ? 21.607 2.656   -9.372  0.36 19.94 ?  99  ASN   A HD21 1 
ATOM   2080 H  HD22 A ASN   A 1 99  ? 22.569 2.256   -7.677  0.64 17.02 ?  99  ASN   A HD22 1 
ATOM   2081 H  HD22 B ASN   A 1 99  ? 22.830 2.060   -8.766  0.36 19.94 ?  99  ASN   A HD22 1 
ATOM   2082 N  N    A VAL   A 1 100 ? 20.202 -1.888  -10.687 0.64 15.31 ?  100 VAL   A N    1 
ATOM   2083 N  N    B VAL   A 1 100 ? 20.434 -2.439  -11.135 0.36 15.53 ?  100 VAL   A N    1 
ATOM   2084 C  CA   A VAL   A 1 100 ? 19.568 -2.121  -11.981 0.64 16.59 ?  100 VAL   A CA   1 
ATOM   2085 C  CA   B VAL   A 1 100 ? 19.829 -2.830  -12.405 0.36 17.72 ?  100 VAL   A CA   1 
ATOM   2086 C  C    A VAL   A 1 100 ? 19.469 -0.827  -12.773 0.64 16.94 ?  100 VAL   A C    1 
ATOM   2087 C  C    B VAL   A 1 100 ? 19.697 -1.639  -13.341 0.36 17.98 ?  100 VAL   A C    1 
ATOM   2088 O  O    A VAL   A 1 100 ? 19.557 -0.834  -14.005 0.64 17.87 ?  100 VAL   A O    1 
ATOM   2089 O  O    B VAL   A 1 100 ? 19.737 -1.799  -14.568 0.36 17.99 ?  100 VAL   A O    1 
ATOM   2090 C  CB   A VAL   A 1 100 ? 18.193 -2.797  -11.786 0.64 18.14 ?  100 VAL   A CB   1 
ATOM   2091 C  CB   B VAL   A 1 100 ? 18.478 -3.527  -12.148 0.36 20.15 ?  100 VAL   A CB   1 
ATOM   2092 C  CG1  A VAL   A 1 100 ? 17.480 -2.976  -13.120 0.64 19.41 ?  100 VAL   A CG1  1 
ATOM   2093 C  CG1  B VAL   A 1 100 ? 17.541 -3.374  -13.343 0.36 21.03 ?  100 VAL   A CG1  1 
ATOM   2094 C  CG2  A VAL   A 1 100 ? 18.360 -4.143  -11.090 0.64 18.39 ?  100 VAL   A CG2  1 
ATOM   2095 C  CG2  B VAL   A 1 100 ? 18.706 -4.991  -11.829 0.36 21.10 ?  100 VAL   A CG2  1 
ATOM   2096 H  H    A VAL   A 1 100 ? 19.701 -2.085  -10.009 0.64 18.38 ?  100 VAL   A H    1 
ATOM   2097 H  H    B VAL   A 1 100 ? 19.921 -2.545  -10.451 0.36 18.64 ?  100 VAL   A H    1 
ATOM   2098 H  HA   A VAL   A 1 100 ? 20.116 -2.738  -12.488 0.64 19.92 ?  100 VAL   A HA   1 
ATOM   2099 H  HA   B VAL   A 1 100 ? 20.412 -3.473  -12.836 0.36 21.28 ?  100 VAL   A HA   1 
ATOM   2100 H  HB   A VAL   A 1 100 ? 17.635 -2.240  -11.223 0.64 21.78 ?  100 VAL   A HB   1 
ATOM   2101 H  HB   B VAL   A 1 100 ? 18.052 -3.113  -11.382 0.36 24.19 ?  100 VAL   A HB   1 
ATOM   2102 H  HG11 A VAL   A 1 100 ? 16.722 -3.574  -12.998 0.64 23.30 ?  100 VAL   A HG11 1 
ATOM   2103 H  HG11 B VAL   A 1 100 ? 16.803 -3.994  -13.240 0.36 25.25 ?  100 VAL   A HG11 1 
ATOM   2104 H  HG12 A VAL   A 1 100 ? 17.169 -2.114  -13.434 0.64 23.30 ?  100 VAL   A HG12 1 
ATOM   2105 H  HG12 B VAL   A 1 100 ? 17.200 -2.464  -13.371 0.36 25.25 ?  100 VAL   A HG12 1 
ATOM   2106 H  HG13 A VAL   A 1 100 ? 18.098 -3.362  -13.761 0.64 23.30 ?  100 VAL   A HG13 1 
ATOM   2107 H  HG13 B VAL   A 1 100 ? 18.026 -3.573  -14.158 0.36 25.25 ?  100 VAL   A HG13 1 
ATOM   2108 H  HG21 A VAL   A 1 100 ? 17.496 -4.582  -11.031 0.64 22.08 ?  100 VAL   A HG21 1 
ATOM   2109 H  HG21 B VAL   A 1 100 ? 17.889 -5.362  -11.465 0.36 25.33 ?  100 VAL   A HG21 1 
ATOM   2110 H  HG22 A VAL   A 1 100 ? 18.974 -4.692  -11.604 0.64 22.08 ?  100 VAL   A HG22 1 
ATOM   2111 H  HG22 B VAL   A 1 100 ? 18.949 -5.458  -12.645 0.36 25.33 ?  100 VAL   A HG22 1 
ATOM   2112 H  HG23 A VAL   A 1 100 ? 18.716 -3.997  -10.199 0.64 22.08 ?  100 VAL   A HG23 1 
ATOM   2113 H  HG23 B VAL   A 1 100 ? 19.421 -5.062  -11.179 0.36 25.33 ?  100 VAL   A HG23 1 
ATOM   2114 N  N    A ASN   A 1 101 ? 19.280 0.298   -12.092 0.64 17.88 ?  101 ASN   A N    1 
ATOM   2115 N  N    B ASN   A 1 101 ? 19.519 -0.434  -12.792 0.36 18.32 ?  101 ASN   A N    1 
ATOM   2116 C  CA   A ASN   A 1 101 ? 19.209 1.574   -12.789 0.64 19.16 ?  101 ASN   A CA   1 
ATOM   2117 C  CA   B ASN   A 1 101 ? 19.439 0.755   -13.636 0.36 19.24 ?  101 ASN   A CA   1 
ATOM   2118 C  C    A ASN   A 1 101 ? 20.562 2.028   -13.338 0.64 21.51 ?  101 ASN   A C    1 
ATOM   2119 C  C    B ASN   A 1 101 ? 20.773 1.065   -14.303 0.36 20.34 ?  101 ASN   A C    1 
ATOM   2120 O  O    A ASN   A 1 101 ? 20.623 3.084   -13.980 0.64 23.45 ?  101 ASN   A O    1 
ATOM   2121 O  O    B ASN   A 1 101 ? 20.798 1.710   -15.357 0.36 20.58 ?  101 ASN   A O    1 
ATOM   2122 C  CB   A ASN   A 1 101 ? 18.581 2.621   -11.871 0.64 18.36 ?  101 ASN   A CB   1 
ATOM   2123 C  CB   B ASN   A 1 101 ? 18.957 1.955   -12.818 0.36 19.07 ?  101 ASN   A CB   1 
ATOM   2124 C  CG   A ASN   A 1 101 ? 17.203 2.197   -11.375 0.64 17.93 ?  101 ASN   A CG   1 
ATOM   2125 C  CG   B ASN   A 1 101 ? 17.716 1.645   -12.004 0.36 19.62 ?  101 ASN   A CG   1 
ATOM   2126 O  OD1  A ASN   A 1 101 ? 16.390 1.670   -12.139 0.64 17.33 ?  101 ASN   A OD1  1 
ATOM   2127 O  OD1  B ASN   A 1 101 ? 16.805 0.962   -12.473 0.36 20.67 ?  101 ASN   A OD1  1 
ATOM   2128 N  ND2  A ASN   A 1 101 ? 16.945 2.398   -10.089 0.64 18.22 ?  101 ASN   A ND2  1 
ATOM   2129 N  ND2  B ASN   A 1 101 ? 17.678 2.140   -10.773 0.36 19.62 ?  101 ASN   A ND2  1 
ATOM   2130 H  H    A ASN   A 1 101 ? 19.185 0.346   -11.245 0.64 21.47 ?  101 ASN   A H    1 
ATOM   2131 H  H    B ASN   A 1 101 ? 19.422 -0.281  -11.950 0.36 21.99 ?  101 ASN   A H    1 
ATOM   2132 H  HA   A ASN   A 1 101 ? 18.618 1.466   -13.551 0.64 23.00 ?  101 ASN   A HA   1 
ATOM   2133 H  HA   B ASN   A 1 101 ? 18.798 0.598   -14.341 0.36 23.10 ?  101 ASN   A HA   1 
ATOM   2134 H  HB2  A ASN   A 1 101 ? 19.156 2.755   -11.104 0.64 22.05 ?  101 ASN   A HB2  1 
ATOM   2135 H  HB2  B ASN   A 1 101 ? 19.658 2.222   -12.208 0.36 22.90 ?  101 ASN   A HB2  1 
ATOM   2136 H  HB3  A ASN   A 1 101 ? 18.486 3.454   -12.365 0.64 22.05 ?  101 ASN   A HB3  1 
ATOM   2137 H  HB3  B ASN   A 1 101 ? 18.743 2.687   -13.422 0.36 22.90 ?  101 ASN   A HB3  1 
ATOM   2138 H  HD21 A ASN   A 1 101 ? 16.182 2.174   -9.765  0.64 21.87 ?  101 ASN   A HD21 1 
ATOM   2139 H  HD21 B ASN   A 1 101 ? 16.996 1.992   -10.270 0.36 23.55 ?  101 ASN   A HD21 1 
ATOM   2140 H  HD22 A ASN   A 1 101 ? 17.539 2.761   -9.584  0.64 21.87 ?  101 ASN   A HD22 1 
ATOM   2141 H  HD22 B ASN   A 1 101 ? 18.334 2.613   -10.481 0.36 23.55 ?  101 ASN   A HD22 1 
ATOM   2142 N  N    A LYS   A 1 102 ? 21.629 1.249   -13.117 0.64 23.49 ?  102 LYS   A N    1 
ATOM   2143 N  N    B LYS   A 1 102 ? 21.883 0.627   -13.711 0.36 21.85 ?  102 LYS   A N    1 
ATOM   2144 C  CA   A LYS   A 1 102 ? 22.918 1.444   -13.771 0.64 25.28 ?  102 LYS   A CA   1 
ATOM   2145 C  CA   B LYS   A 1 102 ? 23.206 0.776   -14.304 0.36 22.73 ?  102 LYS   A CA   1 
ATOM   2146 C  C    A LYS   A 1 102 ? 23.242 0.350   -14.780 0.64 26.08 ?  102 LYS   A C    1 
ATOM   2147 C  C    B LYS   A 1 102 ? 23.566 -0.395  -15.213 0.36 22.47 ?  102 LYS   A C    1 
ATOM   2148 O  O    A LYS   A 1 102 ? 24.321 0.385   -15.379 0.64 26.68 ?  102 LYS   A O    1 
ATOM   2149 O  O    B LYS   A 1 102 ? 24.717 -0.497  -15.649 0.36 22.45 ?  102 LYS   A O    1 
ATOM   2150 C  CB   A LYS   A 1 102 ? 24.048 1.497   -12.734 0.64 27.02 ?  102 LYS   A CB   1 
ATOM   2151 C  CB   B LYS   A 1 102 ? 24.271 0.891   -13.209 0.36 24.13 ?  102 LYS   A CB   1 
ATOM   2152 C  CG   A LYS   A 1 102 ? 23.937 2.620   -11.727 0.64 28.40 ?  102 LYS   A CG   1 
ATOM   2153 C  CG   B LYS   A 1 102 ? 24.216 2.158   -12.373 0.36 25.30 ?  102 LYS   A CG   1 
ATOM   2154 C  CD   A LYS   A 1 102 ? 25.110 2.582   -10.759 0.64 29.94 ?  102 LYS   A CD   1 
ATOM   2155 C  CD   B LYS   A 1 102 ? 25.251 2.095   -11.254 0.36 26.69 ?  102 LYS   A CD   1 
ATOM   2156 C  CE   A LYS   A 1 102 ? 25.043 3.712   -9.748  0.64 31.17 ?  102 LYS   A CE   1 
ATOM   2157 C  CE   B LYS   A 1 102 ? 25.062 3.209   -10.239 0.36 27.77 ?  102 LYS   A CE   1 
ATOM   2158 N  NZ   A LYS   A 1 102 ? 26.146 3.618   -8.749  0.64 31.63 ?  102 LYS   A NZ   1 
ATOM   2159 N  NZ   B LYS   A 1 102 ? 25.306 2.731   -8.846  0.36 28.55 ?  102 LYS   A NZ   1 
ATOM   2160 H  H    A LYS   A 1 102 ? 21.629 0.576   -12.581 0.64 28.19 ?  102 LYS   A H    1 
ATOM   2161 H  H    B LYS   A 1 102 ? 21.894 0.227   -12.951 0.36 26.23 ?  102 LYS   A H    1 
ATOM   2162 H  HA   A LYS   A 1 102 ? 22.913 2.281   -14.250 0.64 30.34 ?  102 LYS   A HA   1 
ATOM   2163 H  HA   B LYS   A 1 102 ? 23.228 1.600   -14.820 0.36 27.29 ?  102 LYS   A HA   1 
ATOM   2164 H  HB2  A LYS   A 1 102 ? 24.057 0.660   -12.243 0.64 32.43 ?  102 LYS   A HB2  1 
ATOM   2165 H  HB2  B LYS   A 1 102 ? 24.160 0.148   -12.598 0.36 28.97 ?  102 LYS   A HB2  1 
ATOM   2166 H  HB3  A LYS   A 1 102 ? 24.893 1.604   -13.202 0.64 32.43 ?  102 LYS   A HB3  1 
ATOM   2167 H  HB3  B LYS   A 1 102 ? 25.151 0.847   -13.620 0.36 28.97 ?  102 LYS   A HB3  1 
ATOM   2168 H  HG2  A LYS   A 1 102 ? 23.947 3.471   -12.192 0.64 34.09 ?  102 LYS   A HG2  1 
ATOM   2169 H  HG2  B LYS   A 1 102 ? 24.414 2.928   -12.930 0.36 30.37 ?  102 LYS   A HG2  1 
ATOM   2170 H  HG3  A LYS   A 1 102 ? 23.115 2.518   -11.222 0.64 34.09 ?  102 LYS   A HG3  1 
ATOM   2171 H  HG3  B LYS   A 1 102 ? 23.337 2.246   -11.973 0.36 30.37 ?  102 LYS   A HG3  1 
ATOM   2172 H  HD2  A LYS   A 1 102 ? 25.097 1.739   -10.277 0.64 35.93 ?  102 LYS   A HD2  1 
ATOM   2173 H  HD2  B LYS   A 1 102 ? 25.171 1.246   -10.792 0.36 32.04 ?  102 LYS   A HD2  1 
ATOM   2174 H  HD3  A LYS   A 1 102 ? 25.938 2.668   -11.259 0.64 35.93 ?  102 LYS   A HD3  1 
ATOM   2175 H  HD3  B LYS   A 1 102 ? 26.139 2.181   -11.638 0.36 32.04 ?  102 LYS   A HD3  1 
ATOM   2176 H  HE2  A LYS   A 1 102 ? 25.122 4.560   -10.213 0.64 37.42 ?  102 LYS   A HE2  1 
ATOM   2177 H  HE2  B LYS   A 1 102 ? 25.693 3.922   -10.429 0.36 33.33 ?  102 LYS   A HE2  1 
ATOM   2178 H  HE3  A LYS   A 1 102 ? 24.197 3.666   -9.275  0.64 37.42 ?  102 LYS   A HE3  1 
ATOM   2179 H  HE3  B LYS   A 1 102 ? 24.154 3.542   -10.293 0.36 33.33 ?  102 LYS   A HE3  1 
ATOM   2180 H  HZ1  A LYS   A 1 102 ? 26.087 4.289   -8.169  0.64 37.97 ?  102 LYS   A HZ1  1 
ATOM   2181 H  HZ1  B LYS   A 1 102 ? 25.133 3.382   -8.266  0.36 34.27 ?  102 LYS   A HZ1  1 
ATOM   2182 H  HZ2  A LYS   A 1 102 ? 26.092 2.847   -8.308  0.64 37.97 ?  102 LYS   A HZ2  1 
ATOM   2183 H  HZ2  B LYS   A 1 102 ? 24.779 2.036   -8.667  0.36 34.27 ?  102 LYS   A HZ2  1 
ATOM   2184 H  HZ3  A LYS   A 1 102 ? 26.934 3.661   -9.162  0.64 37.97 ?  102 LYS   A HZ3  1 
ATOM   2185 H  HZ3  B LYS   A 1 102 ? 26.155 2.479   -8.754  0.36 34.27 ?  102 LYS   A HZ3  1 
ATOM   2186 N  N    A GLY   A 1 103 ? 22.352 -0.623  -14.975 0.64 26.94 ?  103 GLY   A N    1 
ATOM   2187 N  N    B GLY   A 1 103 ? 22.620 -1.290  -15.486 0.36 22.33 ?  103 GLY   A N    1 
ATOM   2188 C  CA   A GLY   A 1 103 ? 22.599 -1.704  -15.910 0.64 27.29 ?  103 GLY   A CA   1 
ATOM   2189 C  CA   B GLY   A 1 103 ? 22.915 -2.455  -16.295 0.36 22.28 ?  103 GLY   A CA   1 
ATOM   2190 C  C    A GLY   A 1 103 ? 23.455 -2.828  -15.375 0.64 27.62 ?  103 GLY   A C    1 
ATOM   2191 C  C    B GLY   A 1 103 ? 23.738 -3.514  -15.598 0.36 21.56 ?  103 GLY   A C    1 
ATOM   2192 O  O    A GLY   A 1 103 ? 24.026 -3.584  -16.168 0.64 28.64 ?  103 GLY   A O    1 
ATOM   2193 O  O    B GLY   A 1 103 ? 24.269 -4.410  -16.260 0.36 21.78 ?  103 GLY   A O    1 
ATOM   2194 H  H    A GLY   A 1 103 ? 21.599 -0.683  -14.575 0.64 32.33 ?  103 GLY   A H    1 
ATOM   2195 H  H    B GLY   A 1 103 ? 21.806 -1.236  -15.213 0.36 26.80 ?  103 GLY   A H    1 
ATOM   2196 H  HA2  A GLY   A 1 103 ? 21.747 -2.075  -16.204 0.64 32.76 ?  103 GLY   A HA2  1 
ATOM   2197 H  HA2  B GLY   A 1 103 ? 22.082 -2.859  -16.579 0.36 26.74 ?  103 GLY   A HA2  1 
ATOM   2198 H  HA3  A GLY   A 1 103 ? 23.052 -1.353  -16.691 0.64 32.76 ?  103 GLY   A HA3  1 
ATOM   2199 H  HA3  B GLY   A 1 103 ? 23.398 -2.165  -17.085 0.36 26.74 ?  103 GLY   A HA3  1 
ATOM   2200 N  N    A GLU   A 1 104 ? 23.566 -2.966  -14.057 0.64 26.14 ?  104 GLU   A N    1 
ATOM   2201 N  N    B GLU   A 1 104 ? 23.853 -3.444  -14.276 0.36 20.24 ?  104 GLU   A N    1 
ATOM   2202 C  CA   A GLU   A 1 104 ? 24.436 -3.971  -13.462 0.64 24.88 ?  104 GLU   A CA   1 
ATOM   2203 C  CA   B GLU   A 1 104 ? 24.716 -4.360  -13.546 0.36 18.94 ?  104 GLU   A CA   1 
ATOM   2204 C  C    A GLU   A 1 104 ? 23.741 -5.330  -13.376 0.64 25.17 ?  104 GLU   A C    1 
ATOM   2205 C  C    B GLU   A 1 104 ? 24.037 -5.719  -13.388 0.36 19.10 ?  104 GLU   A C    1 
ATOM   2206 O  O    A GLU   A 1 104 ? 22.513 -5.425  -13.284 0.64 25.34 ?  104 GLU   A O    1 
ATOM   2207 O  O    B GLU   A 1 104 ? 22.835 -5.809  -13.117 0.36 19.47 ?  104 GLU   A O    1 
ATOM   2208 C  CB   A GLU   A 1 104 ? 24.927 -3.493  -12.092 0.64 23.41 ?  104 GLU   A CB   1 
ATOM   2209 C  CB   B GLU   A 1 104 ? 25.093 -3.750  -12.194 0.36 18.44 ?  104 GLU   A CB   1 
ATOM   2210 C  CG   A GLU   A 1 104 ? 25.938 -2.345  -12.229 0.64 22.56 ?  104 GLU   A CG   1 
ATOM   2211 C  CG   B GLU   A 1 104 ? 25.725 -2.363  -12.343 0.36 18.73 ?  104 GLU   A CG   1 
ATOM   2212 C  CD   A GLU   A 1 104 ? 26.184 -1.528  -10.969 0.64 21.76 ?  104 GLU   A CD   1 
ATOM   2213 C  CD   B GLU   A 1 104 ? 26.226 -1.762  -11.041 0.36 18.69 ?  104 GLU   A CD   1 
ATOM   2214 O  OE1  A GLU   A 1 104 ? 25.577 -1.810  -9.917  0.64 20.30 ?  104 GLU   A OE1  1 
ATOM   2215 O  OE1  B GLU   A 1 104 ? 25.750 -2.158  -9.958  0.36 18.32 ?  104 GLU   A OE1  1 
ATOM   2216 O  OE2  A GLU   A 1 104 ? 26.997 -0.575  -11.052 0.64 22.73 -1 104 GLU   A OE2  1 
ATOM   2217 O  OE2  B GLU   A 1 104 ? 27.104 -0.875  -11.110 0.36 19.60 -1 104 GLU   A OE2  1 
ATOM   2218 H  H    A GLU   A 1 104 ? 23.152 -2.479  -13.486 0.64 31.38 ?  104 GLU   A H    1 
ATOM   2219 H  H    B GLU   A 1 104 ? 23.436 -2.871  -13.783 0.36 24.29 ?  104 GLU   A H    1 
ATOM   2220 H  HA   A GLU   A 1 104 ? 25.212 -4.080  -14.031 0.64 29.86 ?  104 GLU   A HA   1 
ATOM   2221 H  HA   B GLU   A 1 104 ? 25.537 -4.480  -14.050 0.36 22.73 ?  104 GLU   A HA   1 
ATOM   2222 H  HB2  A GLU   A 1 104 ? 24.169 -3.178  -11.576 0.64 28.10 ?  104 GLU   A HB2  1 
ATOM   2223 H  HB2  B GLU   A 1 104 ? 24.298 -3.656  -11.649 0.36 22.14 ?  104 GLU   A HB2  1 
ATOM   2224 H  HB3  A GLU   A 1 104 ? 25.361 -4.232  -11.636 0.64 28.10 ?  104 GLU   A HB3  1 
ATOM   2225 H  HB3  B GLU   A 1 104 ? 25.739 -4.322  -11.754 0.36 22.14 ?  104 GLU   A HB3  1 
ATOM   2226 H  HG2  A GLU   A 1 104 ? 26.783 -2.718  -12.512 0.64 27.08 ?  104 GLU   A HG2  1 
ATOM   2227 H  HG2  B GLU   A 1 104 ? 26.480 -2.423  -12.948 0.36 22.48 ?  104 GLU   A HG2  1 
ATOM   2228 H  HG3  A GLU   A 1 104 ? 25.606 -1.728  -12.895 0.64 27.08 ?  104 GLU   A HG3  1 
ATOM   2229 H  HG3  B GLU   A 1 104 ? 25.063 -1.756  -12.709 0.36 22.48 ?  104 GLU   A HG3  1 
ATOM   2230 N  N    A ASP   A 1 105 ? 24.554 -6.387  -13.409 0.64 25.48 ?  105 ASP   A N    1 
ATOM   2231 N  N    B ASP   A 1 105 ? 24.826 -6.775  -13.580 0.36 20.20 ?  105 ASP   A N    1 
ATOM   2232 C  CA   A ASP   A 1 105 ? 24.060 -7.753  -13.552 0.64 26.66 ?  105 ASP   A CA   1 
ATOM   2233 C  CA   B ASP   A 1 105 ? 24.322 -8.145  -13.623 0.36 21.55 ?  105 ASP   A CA   1 
ATOM   2234 C  C    A ASP   A 1 105 ? 23.386 -8.220  -12.265 0.64 24.33 ?  105 ASP   A C    1 
ATOM   2235 C  C    B ASP   A 1 105 ? 23.586 -8.499  -12.338 0.36 21.25 ?  105 ASP   A C    1 
ATOM   2236 O  O    A ASP   A 1 105 ? 24.021 -8.278  -11.209 0.64 22.80 ?  105 ASP   A O    1 
ATOM   2237 O  O    B ASP   A 1 105 ? 24.182 -8.525  -11.257 0.36 19.71 ?  105 ASP   A O    1 
ATOM   2238 C  CB   A ASP   A 1 105 ? 25.234 -8.667  -13.898 0.64 29.83 ?  105 ASP   A CB   1 
ATOM   2239 C  CB   B ASP   A 1 105 ? 25.517 -9.078  -13.822 0.36 23.22 ?  105 ASP   A CB   1 
ATOM   2240 C  CG   A ASP   A 1 105 ? 24.809 -10.094 -14.144 0.64 32.56 ?  105 ASP   A CG   1 
ATOM   2241 C  CG   B ASP   A 1 105 ? 25.125 -10.539 -13.932 0.36 24.70 ?  105 ASP   A CG   1 
ATOM   2242 O  OD1  A ASP   A 1 105 ? 23.591 -10.337 -14.267 0.64 33.25 ?  105 ASP   A OD1  1 
ATOM   2243 O  OD1  B ASP   A 1 105 ? 23.917 -10.842 -13.993 0.36 24.86 ?  105 ASP   A OD1  1 
ATOM   2244 O  OD2  A ASP   A 1 105 ? 25.697 -10.970 -14.215 0.64 34.08 -1 105 ASP   A OD2  1 
ATOM   2245 O  OD2  B ASP   A 1 105 ? 26.044 -11.390 -13.951 0.36 25.62 -1 105 ASP   A OD2  1 
ATOM   2246 H  H    A ASP   A 1 105 ? 25.413 -6.338  -13.356 0.64 30.58 ?  105 ASP   A H    1 
ATOM   2247 H  H    B ASP   A 1 105 ? 25.671 -6.716  -13.703 0.36 24.25 ?  105 ASP   A H    1 
ATOM   2248 H  HA   A ASP   A 1 105 ? 23.416 -7.799  -14.275 0.64 32.00 ?  105 ASP   A HA   1 
ATOM   2249 H  HA   B ASP   A 1 105 ? 23.708 -8.242  -14.369 0.36 25.87 ?  105 ASP   A HA   1 
ATOM   2250 H  HB2  A ASP   A 1 105 ? 25.666 -8.345  -14.707 0.64 35.80 ?  105 ASP   A HB2  1 
ATOM   2251 H  HB2  B ASP   A 1 105 ? 25.985 -8.812  -14.630 0.36 27.87 ?  105 ASP   A HB2  1 
ATOM   2252 H  HB3  A ASP   A 1 105 ? 25.870 -8.666  -13.164 0.64 35.80 ?  105 ASP   A HB3  1 
ATOM   2253 H  HB3  B ASP   A 1 105 ? 26.103 -8.999  -13.056 0.36 27.87 ?  105 ASP   A HB3  1 
ATOM   2254 N  N    A ILE   A 1 106 ? 22.104 -8.584  -12.359 0.64 23.71 ?  106 ILE   A N    1 
ATOM   2255 N  N    B ILE   A 1 106 ? 22.290 -8.795  -12.458 0.36 22.32 ?  106 ILE   A N    1 
ATOM   2256 C  CA   A ILE   A 1 106 ? 21.352 -9.010  -11.183 0.64 22.73 ?  106 ILE   A CA   1 
ATOM   2257 C  CA   B ILE   A 1 106 ? 21.502 -9.130  -11.278 0.36 23.33 ?  106 ILE   A CA   1 
ATOM   2258 C  C    A ILE   A 1 106 ? 21.904 -10.298 -10.590 0.64 21.82 ?  106 ILE   A C    1 
ATOM   2259 C  C    B ILE   A 1 106 ? 21.972 -10.428 -10.638 0.36 23.32 ?  106 ILE   A C    1 
ATOM   2260 O  O    A ILE   A 1 106 ? 21.698 -10.562 -9.401  0.64 20.87 ?  106 ILE   A O    1 
ATOM   2261 O  O    B ILE   A 1 106 ? 21.715 -10.654 -9.450  0.36 23.00 ?  106 ILE   A O    1 
ATOM   2262 C  CB   A ILE   A 1 106 ? 19.845 -9.118  -11.517 0.64 23.90 ?  106 ILE   A CB   1 
ATOM   2263 C  CB   B ILE   A 1 106 ? 19.992 -9.146  -11.593 0.36 24.76 ?  106 ILE   A CB   1 
ATOM   2264 C  CG1  A ILE   A 1 106 ? 19.006 -9.221  -10.240 0.64 24.15 ?  106 ILE   A CG1  1 
ATOM   2265 C  CG1  B ILE   A 1 106 ? 19.174 -8.992  -10.307 0.36 25.49 ?  106 ILE   A CG1  1 
ATOM   2266 C  CG2  A ILE   A 1 106 ? 19.575 -10.318 -12.402 0.64 24.73 ?  106 ILE   A CG2  1 
ATOM   2267 C  CG2  B ILE   A 1 106 ? 19.603 -10.432 -12.301 0.36 25.19 ?  106 ILE   A CG2  1 
ATOM   2268 C  CD1  A ILE   A 1 106 ? 19.061 -7.987  -9.367  0.64 24.26 ?  106 ILE   A CD1  1 
ATOM   2269 C  CD1  B ILE   A 1 106 ? 19.565 -7.789  -9.473  0.36 25.79 ?  106 ILE   A CD1  1 
ATOM   2270 H  H    A ILE   A 1 106 ? 21.655 -8.587  -13.089 0.64 28.46 ?  106 ILE   A H    1 
ATOM   2271 H  H    B ILE   A 1 106 ? 21.853 -8.800  -13.196 0.36 26.79 ?  106 ILE   A H    1 
ATOM   2272 H  HA   A ILE   A 1 106 ? 21.453 -8.332  -10.506 0.64 27.29 ?  106 ILE   A HA   1 
ATOM   2273 H  HA   B ILE   A 1 106 ? 21.664 -8.435  -10.630 0.36 28.01 ?  106 ILE   A HA   1 
ATOM   2274 H  HB   A ILE   A 1 106 ? 19.581 -8.316  -11.995 0.64 28.69 ?  106 ILE   A HB   1 
ATOM   2275 H  HB   B ILE   A 1 106 ? 19.789 -8.399  -12.178 0.36 29.72 ?  106 ILE   A HB   1 
ATOM   2276 H  HG12 A ILE   A 1 106 ? 18.079 -9.362  -10.487 0.64 28.99 ?  106 ILE   A HG12 1 
ATOM   2277 H  HG12 B ILE   A 1 106 ? 18.236 -8.895  -10.539 0.36 30.60 ?  106 ILE   A HG12 1 
ATOM   2278 H  HG13 A ILE   A 1 106 ? 19.323 -9.969  -9.712  0.64 28.99 ?  106 ILE   A HG13 1 
ATOM   2279 H  HG13 B ILE   A 1 106 ? 19.297 -9.783  -9.760  0.36 30.60 ?  106 ILE   A HG13 1 
ATOM   2280 H  HG21 A ILE   A 1 106 ? 18.679 -10.241 -12.765 0.64 29.69 ?  106 ILE   A HG21 1 
ATOM   2281 H  HG21 B ILE   A 1 106 ? 18.731 -10.314 -12.709 0.36 30.23 ?  106 ILE   A HG21 1 
ATOM   2282 H  HG22 A ILE   A 1 106 ? 20.225 -10.328 -13.119 0.64 29.69 ?  106 ILE   A HG22 1 
ATOM   2283 H  HG22 B ILE   A 1 106 ? 20.265 -10.625 -12.982 0.36 30.23 ?  106 ILE   A HG22 1 
ATOM   2284 H  HG23 A ILE   A 1 106 ? 19.651 -11.124 -11.871 0.64 29.69 ?  106 ILE   A HG23 1 
ATOM   2285 H  HG23 B ILE   A 1 106 ? 19.572 -11.152 -11.653 0.36 30.23 ?  106 ILE   A HG23 1 
ATOM   2286 H  HD11 A ILE   A 1 106 ? 18.353 -8.036  -8.707  0.64 29.12 ?  106 ILE   A HD11 1 
ATOM   2287 H  HD11 B ILE   A 1 106 ? 18.812 -7.525  -8.929  0.36 30.96 ?  106 ILE   A HD11 1 
ATOM   2288 H  HD12 A ILE   A 1 106 ? 19.924 -7.948  -8.925  0.64 29.12 ?  106 ILE   A HD12 1 
ATOM   2289 H  HD12 B ILE   A 1 106 ? 20.317 -8.029  -8.907  0.36 30.96 ?  106 ILE   A HD12 1 
ATOM   2290 H  HD13 A ILE   A 1 106 ? 18.939 -7.201  -9.924  0.64 29.12 ?  106 ILE   A HD13 1 
ATOM   2291 H  HD13 B ILE   A 1 106 ? 19.817 -7.064  -10.068 0.36 30.96 ?  106 ILE   A HD13 1 
ATOM   2292 N  N    A GLN   A 1 107 ? 22.614 -11.106 -11.388 0.64 22.89 ?  107 GLN   A N    1 
ATOM   2293 N  N    B GLN   A 1 107 ? 22.665 -11.286 -11.391 0.36 23.69 ?  107 GLN   A N    1 
ATOM   2294 C  CA   A GLN   A 1 107 ? 23.220 -12.330 -10.870 0.64 25.23 ?  107 GLN   A CA   1 
ATOM   2295 C  CA   B GLN   A 1 107 ? 23.283 -12.462 -10.793 0.36 24.75 ?  107 GLN   A CA   1 
ATOM   2296 C  C    A GLN   A 1 107 ? 24.192 -12.039 -9.732  0.64 22.81 ?  107 GLN   A C    1 
ATOM   2297 C  C    B GLN   A 1 107 ? 24.281 -12.081 -9.709  0.36 22.39 ?  107 GLN   A C    1 
ATOM   2298 O  O    A GLN   A 1 107 ? 24.407 -12.891 -8.862  0.64 24.15 ?  107 GLN   A O    1 
ATOM   2299 O  O    B GLN   A 1 107 ? 24.607 -12.917 -8.858  0.36 23.22 ?  107 GLN   A O    1 
ATOM   2300 C  CB   A GLN   A 1 107 ? 23.924 -13.080 -12.007 0.64 29.78 ?  107 GLN   A CB   1 
ATOM   2301 C  CB   B GLN   A 1 107 ? 23.971 -13.305 -11.871 0.36 28.00 ?  107 GLN   A CB   1 
ATOM   2302 C  CG   A GLN   A 1 107 ? 23.044 -13.314 -13.231 0.64 34.41 ?  107 GLN   A CG   1 
ATOM   2303 C  CG   B GLN   A 1 107 ? 23.053 -13.728 -13.010 0.36 31.15 ?  107 GLN   A CG   1 
ATOM   2304 C  CD   A GLN   A 1 107 ? 21.771 -14.067 -12.897 0.64 38.26 ?  107 GLN   A CD   1 
ATOM   2305 C  CD   B GLN   A 1 107 ? 21.925 -14.629 -12.551 0.36 33.88 ?  107 GLN   A CD   1 
ATOM   2306 O  OE1  A GLN   A 1 107 ? 21.807 -15.114 -12.252 0.64 39.72 ?  107 GLN   A OE1  1 
ATOM   2307 O  OE1  B GLN   A 1 107 ? 22.104 -15.467 -11.665 0.36 34.81 ?  107 GLN   A OE1  1 
ATOM   2308 N  NE2  A GLN   A 1 107 ? 20.636 -13.531 -13.330 0.64 39.40 ?  107 GLN   A NE2  1 
ATOM   2309 N  NE2  B GLN   A 1 107 ? 20.751 -14.459 -13.150 0.36 34.71 ?  107 GLN   A NE2  1 
ATOM   2310 H  H    A GLN   A 1 107 ? 22.756 -10.966 -12.224 0.64 27.48 ?  107 GLN   A H    1 
ATOM   2311 H  H    B GLN   A 1 107 ? 22.791 -11.208 -12.237 0.36 28.43 ?  107 GLN   A H    1 
ATOM   2312 H  HA   A GLN   A 1 107 ? 22.529 -12.908 -10.522 0.64 30.29 ?  107 GLN   A HA   1 
ATOM   2313 H  HA   B GLN   A 1 107 ? 22.595 -13.007 -10.386 0.36 29.71 ?  107 GLN   A HA   1 
ATOM   2314 H  HB2  A GLN   A 1 107 ? 24.697 -12.568 -12.296 0.64 35.75 ?  107 GLN   A HB2  1 
ATOM   2315 H  HB2  B GLN   A 1 107 ? 24.699 -12.792 -12.256 0.36 33.61 ?  107 GLN   A HB2  1 
ATOM   2316 H  HB3  A GLN   A 1 107 ? 24.210 -13.950 -11.685 0.64 35.75 ?  107 GLN   A HB3  1 
ATOM   2317 H  HB3  B GLN   A 1 107 ? 24.321 -14.113 -11.462 0.36 33.61 ?  107 GLN   A HB3  1 
ATOM   2318 H  HG2  A GLN   A 1 107 ? 22.793 -12.459 -13.616 0.64 41.30 ?  107 GLN   A HG2  1 
ATOM   2319 H  HG2  B GLN   A 1 107 ? 22.661 -12.938 -13.414 0.36 37.38 ?  107 GLN   A HG2  1 
ATOM   2320 H  HG3  A GLN   A 1 107 ? 23.540 -13.834 -13.884 0.64 41.30 ?  107 GLN   A HG3  1 
ATOM   2321 H  HG3  B GLN   A 1 107 ? 23.572 -14.213 -13.671 0.36 37.38 ?  107 GLN   A HG3  1 
ATOM   2322 H  HE21 A GLN   A 1 107 ? 20.649 -12.797 -13.777 0.64 47.29 ?  107 GLN   A HE21 1 
ATOM   2323 H  HE21 B GLN   A 1 107 ? 20.663 -13.861 -13.764 0.36 41.66 ?  107 GLN   A HE21 1 
ATOM   2324 H  HE22 A GLN   A 1 107 ? 19.887 -13.921 -13.165 0.64 47.29 ?  107 GLN   A HE22 1 
ATOM   2325 H  HE22 B GLN   A 1 107 ? 20.078 -14.945 -12.926 0.36 41.66 ?  107 GLN   A HE22 1 
ATOM   2326 N  N    . LEU   A 1 108 ? 24.769 -10.836 -9.709  1.00 19.51 ?  108 LEU   A N    1 
ATOM   2327 C  CA   . LEU   A 1 108 ? 25.679 -10.417 -8.653  1.00 16.49 ?  108 LEU   A CA   1 
ATOM   2328 C  C    . LEU   A 1 108 ? 24.975 -10.240 -7.317  1.00 14.38 ?  108 LEU   A C    1 
ATOM   2329 O  O    . LEU   A 1 108 ? 25.652 -10.074 -6.301  1.00 14.59 ?  108 LEU   A O    1 
ATOM   2330 C  CB   . LEU   A 1 108 ? 26.401 -9.125  -9.056  1.00 16.50 ?  108 LEU   A CB   1 
ATOM   2331 C  CG   . LEU   A 1 108 ? 27.402 -9.324  -10.195 1.00 18.21 ?  108 LEU   A CG   1 
ATOM   2332 C  CD1  . LEU   A 1 108 ? 27.865 -7.989  -10.752 1.00 18.65 ?  108 LEU   A CD1  1 
ATOM   2333 C  CD2  . LEU   A 1 108 ? 28.596 -10.146 -9.727  1.00 20.26 ?  108 LEU   A CD2  1 
ATOM   2334 H  H    A LEU   A 1 108 ? 24.641 -10.237 -10.304 0.64 23.42 ?  108 LEU   A H    1 
ATOM   2335 H  H    B LEU   A 1 108 ? 24.600 -10.241 -10.298 0.36 23.42 ?  108 LEU   A H    1 
ATOM   2336 H  HA   . LEU   A 1 108 ? 26.351 -11.103 -8.529  1.00 19.80 ?  108 LEU   A HA   1 
ATOM   2337 H  HB2  . LEU   A 1 108 ? 25.744 -8.474  -9.348  1.00 19.81 ?  108 LEU   A HB2  1 
ATOM   2338 H  HB3  . LEU   A 1 108 ? 26.886 -8.783  -8.290  1.00 19.81 ?  108 LEU   A HB3  1 
ATOM   2339 H  HG   . LEU   A 1 108 ? 26.970 -9.813  -10.912 1.00 21.86 ?  108 LEU   A HG   1 
ATOM   2340 H  HD11 . LEU   A 1 108 ? 28.478 -8.150  -11.491 1.00 22.39 ?  108 LEU   A HD11 1 
ATOM   2341 H  HD12 . LEU   A 1 108 ? 27.096 -7.492  -11.066 1.00 22.39 ?  108 LEU   A HD12 1 
ATOM   2342 H  HD13 . LEU   A 1 108 ? 28.319 -7.494  -10.053 1.00 22.39 ?  108 LEU   A HD13 1 
ATOM   2343 H  HD21 . LEU   A 1 108 ? 29.289 -10.106 -10.402 1.00 24.32 ?  108 LEU   A HD21 1 
ATOM   2344 H  HD22 . LEU   A 1 108 ? 28.923 -9.775  -8.892  1.00 24.32 ?  108 LEU   A HD22 1 
ATOM   2345 H  HD23 . LEU   A 1 108 ? 28.314 -11.064 -9.593  1.00 24.32 ?  108 LEU   A HD23 1 
ATOM   2346 N  N    . LEU   A 1 109 ? 23.641 -10.294 -7.282  1.00 13.74 ?  109 LEU   A N    1 
ATOM   2347 C  CA   . LEU   A 1 109 ? 22.945 -10.164 -6.009  1.00 12.93 ?  109 LEU   A CA   1 
ATOM   2348 C  C    . LEU   A 1 109 ? 23.285 -11.317 -5.069  1.00 12.53 ?  109 LEU   A C    1 
ATOM   2349 O  O    . LEU   A 1 109 ? 23.426 -11.118 -3.859  1.00 12.94 ?  109 LEU   A O    1 
ATOM   2350 C  CB   . LEU   A 1 109 ? 21.440 -10.084 -6.257  1.00 13.95 ?  109 LEU   A CB   1 
ATOM   2351 C  CG   . LEU   A 1 109 ? 20.548 -9.799  -5.053  1.00 14.08 ?  109 LEU   A CG   1 
ATOM   2352 C  CD1  . LEU   A 1 109 ? 21.005 -8.537  -4.337  1.00 14.24 ?  109 LEU   A CD1  1 
ATOM   2353 C  CD2  . LEU   A 1 109 ? 19.094 -9.663  -5.496  1.00 15.05 ?  109 LEU   A CD2  1 
ATOM   2354 H  H    . LEU   A 1 109 ? 23.129 -10.402 -7.963  1.00 16.50 ?  109 LEU   A H    1 
ATOM   2355 H  HA   . LEU   A 1 109 ? 23.225 -9.337  -5.582  1.00 15.52 ?  109 LEU   A HA   1 
ATOM   2356 H  HB2  . LEU   A 1 109 ? 21.278 -9.379  -6.901  1.00 16.75 ?  109 LEU   A HB2  1 
ATOM   2357 H  HB3  . LEU   A 1 109 ? 21.150 -10.930 -6.626  1.00 16.75 ?  109 LEU   A HB3  1 
ATOM   2358 H  HG   . LEU   A 1 109 ? 20.602 -10.534 -4.426  1.00 16.90 ?  109 LEU   A HG   1 
ATOM   2359 H  HD11 . LEU   A 1 109 ? 20.317 -8.254  -3.712  1.00 17.10 ?  109 LEU   A HD11 1 
ATOM   2360 H  HD12 . LEU   A 1 109 ? 21.829 -8.718  -3.863  1.00 17.10 ?  109 LEU   A HD12 1 
ATOM   2361 H  HD13 . LEU   A 1 109 ? 21.150 -7.835  -4.997  1.00 17.10 ?  109 LEU   A HD13 1 
ATOM   2362 H  HD21 . LEU   A 1 109 ? 18.554 -9.371  -4.741  1.00 18.07 ?  109 LEU   A HD21 1 
ATOM   2363 H  HD22 . LEU   A 1 109 ? 19.035 -9.012  -6.211  1.00 18.07 ?  109 LEU   A HD22 1 
ATOM   2364 H  HD23 . LEU   A 1 109 ? 18.775 -10.527 -5.809  1.00 18.07 ?  109 LEU   A HD23 1 
ATOM   2365 N  N    . LYS   A 1 110 ? 23.418 -12.533 -5.601  1.00 12.23 ?  110 LYS   A N    1 
ATOM   2366 C  CA   . LYS   A 1 110 ? 23.792 -13.646 -4.737  1.00 12.42 ?  110 LYS   A CA   1 
ATOM   2367 C  C    . LYS   A 1 110 ? 25.173 -13.421 -4.133  1.00 12.20 ?  110 LYS   A C    1 
ATOM   2368 O  O    . LYS   A 1 110 ? 25.369 -13.621 -2.932  1.00 12.29 ?  110 LYS   A O    1 
ATOM   2369 C  CB   . LYS   A 1 110 ? 23.717 -14.973 -5.494  1.00 13.49 ?  110 LYS   A CB   1 
ATOM   2370 C  CG   . LYS   A 1 110 ? 23.910 -16.184 -4.581  1.00 13.54 ?  110 LYS   A CG   1 
ATOM   2371 C  CD   . LYS   A 1 110 ? 23.674 -17.504 -5.295  1.00 14.23 ?  110 LYS   A CD   1 
ATOM   2372 C  CE   . LYS   A 1 110 ? 23.791 -18.684 -4.341  1.00 14.85 ?  110 LYS   A CE   1 
ATOM   2373 N  NZ   . LYS   A 1 110 ? 22.617 -18.801 -3.433  1.00 15.37 ?  110 LYS   A NZ   1 
ATOM   2374 H  H    . LYS   A 1 110 ? 23.303 -12.731 -6.425  1.00 14.68 ?  110 LYS   A H    1 
ATOM   2375 H  HA   . LYS   A 1 110 ? 23.153 -13.693 -4.003  1.00 14.92 ?  110 LYS   A HA   1 
ATOM   2376 H  HB2  . LYS   A 1 110 ? 22.844 -15.051 -5.912  1.00 16.20 ?  110 LYS   A HB2  1 
ATOM   2377 H  HB3  . LYS   A 1 110 ? 24.412 -14.992 -6.165  1.00 16.20 ?  110 LYS   A HB3  1 
ATOM   2378 H  HG2  . LYS   A 1 110 ? 24.815 -16.182 -4.238  1.00 16.26 ?  110 LYS   A HG2  1 
ATOM   2379 H  HG3  . LYS   A 1 110 ? 23.277 -16.127 -3.845  1.00 16.26 ?  110 LYS   A HG3  1 
ATOM   2380 H  HD2  . LYS   A 1 110 ? 22.787 -17.511 -5.678  1.00 17.09 ?  110 LYS   A HD2  1 
ATOM   2381 H  HD3  . LYS   A 1 110 ? 24.345 -17.612 -5.990  1.00 17.09 ?  110 LYS   A HD3  1 
ATOM   2382 H  HE2  . LYS   A 1 110 ? 23.856 -19.507 -4.851  1.00 17.83 ?  110 LYS   A HE2  1 
ATOM   2383 H  HE3  . LYS   A 1 110 ? 24.585 -18.576 -3.788  1.00 17.83 ?  110 LYS   A HE3  1 
ATOM   2384 H  HZ1  . LYS   A 1 110 ? 22.711 -19.493 -2.888  1.00 18.45 ?  110 LYS   A HZ1  1 
ATOM   2385 H  HZ2  . LYS   A 1 110 ? 22.536 -18.056 -2.943  1.00 18.45 ?  110 LYS   A HZ2  1 
ATOM   2386 H  HZ3  . LYS   A 1 110 ? 21.871 -18.905 -3.912  1.00 18.45 ?  110 LYS   A HZ3  1 
ATOM   2387 N  N    . SER   A 1 111 ? 26.134 -12.986 -4.949  1.00 12.23 ?  111 SER   A N    1 
ATOM   2388 C  CA   . SER   A 1 111 ? 27.464 -12.677 -4.432  1.00 12.15 ?  111 SER   A CA   1 
ATOM   2389 C  C    . SER   A 1 111 ? 27.400 -11.625 -3.329  1.00 11.72 ?  111 SER   A C    1 
ATOM   2390 O  O    . SER   A 1 111 ? 28.098 -11.726 -2.315  1.00 12.41 ?  111 SER   A O    1 
ATOM   2391 C  CB   . SER   A 1 111 ? 28.352 -12.190 -5.577  1.00 13.73 ?  111 SER   A CB   1 
ATOM   2392 O  OG   . SER   A 1 111 ? 28.452 -13.187 -6.583  1.00 15.42 ?  111 SER   A OG   1 
ATOM   2393 H  H    . SER   A 1 111 ? 26.036 -12.862 -5.792  1.00 14.68 ?  111 SER   A H    1 
ATOM   2394 H  HA   . SER   A 1 111 ? 27.859 -13.486 -4.068  1.00 14.59 ?  111 SER   A HA   1 
ATOM   2395 H  HB2  . SER   A 1 111 ? 27.955 -11.395 -5.970  1.00 16.48 ?  111 SER   A HB2  1 
ATOM   2396 H  HB3  . SER   A 1 111 ? 29.233 -11.990 -5.235  1.00 16.48 ?  111 SER   A HB3  1 
ATOM   2397 H  HG   . SER   A 1 111 ? 28.951 -12.913 -7.211  1.00 18.52 ?  111 SER   A HG   1 
ATOM   2398 N  N    . ALA   A 1 112 ? 26.560 -10.604 -3.511  1.00 11.89 ?  112 ALA   A N    1 
ATOM   2399 C  CA   . ALA   A 1 112 ? 26.417 -9.567  -2.492  1.00 11.58 ?  112 ALA   A CA   1 
ATOM   2400 C  C    . ALA   A 1 112 ? 25.930 -10.162 -1.172  1.00 11.72 ?  112 ALA   A C    1 
ATOM   2401 O  O    . ALA   A 1 112 ? 26.469 -9.865  -0.101  1.00 11.96 ?  112 ALA   A O    1 
ATOM   2402 C  CB   . ALA   A 1 112 ? 25.448 -8.491  -2.984  1.00 12.15 ?  112 ALA   A CB   1 
ATOM   2403 H  H    . ALA   A 1 112 ? 26.070 -10.493 -4.205  1.00 14.28 ?  112 ALA   A H    1 
ATOM   2404 H  HA   . ALA   A 1 112 ? 27.278 -9.148  -2.339  1.00 13.90 ?  112 ALA   A HA   1 
ATOM   2405 H  HB1  . ALA   A 1 112 ? 25.374 -7.796  -2.305  1.00 14.59 ?  112 ALA   A HB1  1 
ATOM   2406 H  HB2  . ALA   A 1 112 ? 25.784 -8.108  -3.808  1.00 14.59 ?  112 ALA   A HB2  1 
ATOM   2407 H  HB3  . ALA   A 1 112 ? 24.576 -8.891  -3.136  1.00 14.59 ?  112 ALA   A HB3  1 
ATOM   2408 N  N    . TYR   A 1 113 ? 24.891 -11.001 -1.224  1.00 11.79 ?  113 TYR   A N    1 
ATOM   2409 C  CA   . TYR   A 1 113 ? 24.378 -11.605 0.004   1.00 11.48 ?  113 TYR   A CA   1 
ATOM   2410 C  C    . TYR   A 1 113 ? 25.380 -12.557 0.652   1.00 11.23 ?  113 TYR   A C    1 
ATOM   2411 O  O    . TYR   A 1 113 ? 25.332 -12.748 1.869   1.00 11.85 ?  113 TYR   A O    1 
ATOM   2412 C  CB   . TYR   A 1 113 ? 23.061 -12.337 -0.266  1.00 11.73 ?  113 TYR   A CB   1 
ATOM   2413 C  CG   . TYR   A 1 113 ? 21.845 -11.438 -0.198  1.00 11.50 ?  113 TYR   A CG   1 
ATOM   2414 C  CD1  . TYR   A 1 113 ? 21.475 -10.835 0.999   1.00 11.86 ?  113 TYR   A CD1  1 
ATOM   2415 C  CD2  . TYR   A 1 113 ? 21.047 -11.224 -1.314  1.00 11.74 ?  113 TYR   A CD2  1 
ATOM   2416 C  CE1  . TYR   A 1 113 ? 20.351 -10.036 1.083   1.00 12.29 ?  113 TYR   A CE1  1 
ATOM   2417 C  CE2  . TYR   A 1 113 ? 19.900 -10.419 -1.237  1.00 11.98 ?  113 TYR   A CE2  1 
ATOM   2418 C  CZ   . TYR   A 1 113 ? 19.567 -9.833  -0.030  1.00 12.18 ?  113 TYR   A CZ   1 
ATOM   2419 O  OH   . TYR   A 1 113 ? 18.444 -9.035  0.096   1.00 12.95 ?  113 TYR   A OH   1 
ATOM   2420 H  H    . TYR   A 1 113 ? 24.476 -11.223 -1.942  1.00 14.16 ?  113 TYR   A H    1 
ATOM   2421 H  HA   . TYR   A 1 113 ? 24.199 -10.901 0.642   1.00 13.79 ?  113 TYR   A HA   1 
ATOM   2422 H  HB2  . TYR   A 1 113 ? 23.093 -12.719 -1.157  1.00 14.08 ?  113 TYR   A HB2  1 
ATOM   2423 H  HB3  . TYR   A 1 113 ? 22.953 -13.038 0.392   1.00 14.08 ?  113 TYR   A HB3  1 
ATOM   2424 H  HD1  . TYR   A 1 113 ? 21.995 -10.978 1.758   1.00 14.24 ?  113 TYR   A HD1  1 
ATOM   2425 H  HD2  . TYR   A 1 113 ? 21.269 -11.628 -2.122  1.00 14.10 ?  113 TYR   A HD2  1 
ATOM   2426 H  HE1  . TYR   A 1 113 ? 20.123 -9.644  1.893   1.00 14.75 ?  113 TYR   A HE1  1 
ATOM   2427 H  HE2  . TYR   A 1 113 ? 19.370 -10.276 -1.987  1.00 14.38 ?  113 TYR   A HE2  1 
ATOM   2428 H  HH   . TYR   A 1 113 ? 18.030 -9.026  -0.636  1.00 15.55 ?  113 TYR   A HH   1 
ATOM   2429 N  N    . GLU   A 1 114 ? 26.283 -13.171 -0.127  1.00 11.54 ?  114 GLU   A N    1 
ATOM   2430 C  CA   . GLU   A 1 114 ? 27.270 -14.071 0.474   1.00 11.82 ?  114 GLU   A CA   1 
ATOM   2431 C  C    . GLU   A 1 114 ? 28.114 -13.359 1.523   1.00 11.76 ?  114 GLU   A C    1 
ATOM   2432 O  O    . GLU   A 1 114 ? 28.593 -13.992 2.471   1.00 11.88 ?  114 GLU   A O    1 
ATOM   2433 C  CB   . GLU   A 1 114 ? 28.144 -14.717 -0.609  1.00 11.88 ?  114 GLU   A CB   1 
ATOM   2434 C  CG   . GLU   A 1 114 ? 27.376 -15.764 -1.396  1.00 12.27 ?  114 GLU   A CG   1 
ATOM   2435 C  CD   . GLU   A 1 114 ? 28.094 -16.299 -2.623  1.00 12.61 ?  114 GLU   A CD   1 
ATOM   2436 O  OE1  . GLU   A 1 114 ? 29.050 -15.669 -3.116  1.00 12.96 ?  114 GLU   A OE1  1 
ATOM   2437 O  OE2  . GLU   A 1 114 ? 27.656 -17.364 -3.111  1.00 13.90 -1 114 GLU   A OE2  1 
ATOM   2438 H  H    . GLU   A 1 114 ? 26.349 -13.076 -0.984  1.00 13.86 ?  114 GLU   A H    1 
ATOM   2439 H  HA   . GLU   A 1 114 ? 26.794 -14.780 0.922   1.00 14.19 ?  114 GLU   A HA   1 
ATOM   2440 H  HB2  . GLU   A 1 114 ? 28.443 -14.035 -1.233  1.00 14.26 ?  114 GLU   A HB2  1 
ATOM   2441 H  HB3  . GLU   A 1 114 ? 28.900 -15.151 -0.195  1.00 14.26 ?  114 GLU   A HB3  1 
ATOM   2442 H  HG2  . GLU   A 1 114 ? 27.193 -16.517 -0.815  1.00 14.73 ?  114 GLU   A HG2  1 
ATOM   2443 H  HG3  . GLU   A 1 114 ? 26.535 -15.375 -1.695  1.00 14.73 ?  114 GLU   A HG3  1 
ATOM   2444 N  N    . ASN   A 1 115 ? 28.301 -12.043 1.384   1.00 11.60 ?  115 ASN   A N    1 
ATOM   2445 C  CA   . ASN   A 1 115 ? 29.066 -11.311 2.389   1.00 11.79 ?  115 ASN   A CA   1 
ATOM   2446 C  C    . ASN   A 1 115 ? 28.446 -11.439 3.773   1.00 11.83 ?  115 ASN   A C    1 
ATOM   2447 O  O    . ASN   A 1 115 ? 29.152 -11.364 4.784   1.00 12.20 ?  115 ASN   A O    1 
ATOM   2448 C  CB   . ASN   A 1 115 ? 29.170 -9.836  2.004   1.00 12.11 ?  115 ASN   A CB   1 
ATOM   2449 C  CG   . ASN   A 1 115 ? 29.972 -9.622  0.741   1.00 12.56 ?  115 ASN   A CG   1 
ATOM   2450 O  OD1  . ASN   A 1 115 ? 31.193 -9.711  0.757   1.00 15.94 ?  115 ASN   A OD1  1 
ATOM   2451 N  ND2  . ASN   A 1 115 ? 29.297 -9.322  -0.351  1.00 11.99 ?  115 ASN   A ND2  1 
ATOM   2452 H  H    . ASN   A 1 115 ? 28.002 -11.559 0.738   1.00 13.93 ?  115 ASN   A H    1 
ATOM   2453 H  HA   . ASN   A 1 115 ? 29.962 -11.675 2.432   1.00 14.16 ?  115 ASN   A HA   1 
ATOM   2454 H  HB2  . ASN   A 1 115 ? 28.276 -9.483  1.868   1.00 14.54 ?  115 ASN   A HB2  1 
ATOM   2455 H  HB3  . ASN   A 1 115 ? 29.605 -9.354  2.730   1.00 14.54 ?  115 ASN   A HB3  1 
ATOM   2456 H  HD21 . ASN   A 1 115 ? 29.714 -9.188  -1.090  1.00 14.40 ?  115 ASN   A HD21 1 
ATOM   2457 H  HD22 . ASN   A 1 115 ? 28.437 -9.283  -0.328  1.00 14.40 ?  115 ASN   A HD22 1 
ATOM   2458 N  N    . PHE   A 1 116 ? 27.121 -11.606 3.844   1.00 11.67 ?  116 PHE   A N    1 
ATOM   2459 C  CA   . PHE   A 1 116 ? 26.467 -11.702 5.145   1.00 11.61 ?  116 PHE   A CA   1 
ATOM   2460 C  C    . PHE   A 1 116 ? 26.941 -12.933 5.917   1.00 11.91 ?  116 PHE   A C    1 
ATOM   2461 O  O    . PHE   A 1 116 ? 26.861 -12.958 7.146   1.00 12.43 ?  116 PHE   A O    1 
ATOM   2462 C  CB   . PHE   A 1 116 ? 24.940 -11.834 4.993   1.00 11.95 ?  116 PHE   A CB   1 
ATOM   2463 C  CG   . PHE   A 1 116 ? 24.188 -10.582 4.534   1.00 11.48 ?  116 PHE   A CG   1 
ATOM   2464 C  CD1  . PHE   A 1 116 ? 24.767 -9.557  3.799   1.00 11.40 ?  116 PHE   A CD1  1 
ATOM   2465 C  CD2  . PHE   A 1 116 ? 22.830 -10.480 4.838   1.00 12.33 ?  116 PHE   A CD2  1 
ATOM   2466 C  CE1  . PHE   A 1 116 ? 23.998 -8.481  3.379   1.00 11.98 ?  116 PHE   A CE1  1 
ATOM   2467 C  CE2  . PHE   A 1 116 ? 22.069 -9.406  4.432   1.00 12.35 ?  116 PHE   A CE2  1 
ATOM   2468 C  CZ   . PHE   A 1 116 ? 22.646 -8.405  3.703   1.00 11.73 ?  116 PHE   A CZ   1 
ATOM   2469 H  H    . PHE   A 1 116 ? 26.588 -11.653 3.167   1.00 14.01 ?  116 PHE   A H    1 
ATOM   2470 H  HA   . PHE   A 1 116 ? 26.653 -10.909 5.670   1.00 13.94 ?  116 PHE   A HA   1 
ATOM   2471 H  HB2  . PHE   A 1 116 ? 24.759 -12.535 4.342   1.00 14.35 ?  116 PHE   A HB2  1 
ATOM   2472 H  HB3  . PHE   A 1 116 ? 24.570 -12.097 5.851   1.00 14.35 ?  116 PHE   A HB3  1 
ATOM   2473 H  HD1  . PHE   A 1 116 ? 25.662 -9.613  3.571   1.00 13.68 ?  116 PHE   A HD1  1 
ATOM   2474 H  HD2  . PHE   A 1 116 ? 22.422 -11.171 5.324   1.00 14.81 ?  116 PHE   A HD2  1 
ATOM   2475 H  HE1  . PHE   A 1 116 ? 24.396 -7.796  2.895   1.00 14.39 ?  116 PHE   A HE1  1 
ATOM   2476 H  HE2  . PHE   A 1 116 ? 21.164 -9.367  4.654   1.00 14.83 ?  116 PHE   A HE2  1 
ATOM   2477 H  HZ   . PHE   A 1 116 ? 22.140 -7.670  3.438   1.00 14.08 ?  116 PHE   A HZ   1 
ATOM   2478 N  N    . ASN   A 1 117 ? 27.387 -13.978 5.214   1.00 12.29 ?  117 ASN   A N    1 
ATOM   2479 C  CA   . ASN   A 1 117 ? 27.752 -15.221 5.884   1.00 12.54 ?  117 ASN   A CA   1 
ATOM   2480 C  C    . ASN   A 1 117 ? 29.006 -15.102 6.728   1.00 13.15 ?  117 ASN   A C    1 
ATOM   2481 O  O    . ASN   A 1 117 ? 29.297 -16.024 7.500   1.00 13.90 ?  117 ASN   A O    1 
ATOM   2482 C  CB   . ASN   A 1 117 ? 27.868 -16.351 4.870   1.00 12.49 ?  117 ASN   A CB   1 
ATOM   2483 C  CG   . ASN   A 1 117 ? 26.522 -16.734 4.333   1.00 12.67 ?  117 ASN   A CG   1 
ATOM   2484 O  OD1  . ASN   A 1 117 ? 25.545 -16.756 5.081   1.00 13.46 ?  117 ASN   A OD1  1 
ATOM   2485 N  ND2  . ASN   A 1 117 ? 26.442 -17.001 3.045   1.00 12.45 ?  117 ASN   A ND2  1 
ATOM   2486 H  H    . ASN   A 1 117 ? 27.472 -13.990 4.354   1.00 14.75 ?  117 ASN   A H    1 
ATOM   2487 H  HA   . ASN   A 1 117 ? 27.025 -15.451 6.485   1.00 15.05 ?  117 ASN   A HA   1 
ATOM   2488 H  HB2  . ASN   A 1 117 ? 28.419 -16.060 4.128   1.00 15.00 ?  117 ASN   A HB2  1 
ATOM   2489 H  HB3  . ASN   A 1 117 ? 28.256 -17.124 5.302   1.00 15.00 ?  117 ASN   A HB3  1 
ATOM   2490 H  HD21 . ASN   A 1 117 ? 25.689 -17.220 2.703   1.00 14.95 ?  117 ASN   A HD21 1 
ATOM   2491 H  HD22 . ASN   A 1 117 ? 27.150 -16.965 2.561   1.00 14.95 ?  117 ASN   A HD22 1 
ATOM   2492 N  N    . GLN   A 1 118 ? 29.731 -13.993 6.615   1.00 12.85 ?  118 GLN   A N    1 
ATOM   2493 C  CA   . GLN   A 1 118 ? 30.908 -13.760 7.441   1.00 13.65 ?  118 GLN   A CA   1 
ATOM   2494 C  C    . GLN   A 1 118 ? 30.561 -13.185 8.809   1.00 13.41 ?  118 GLN   A C    1 
ATOM   2495 O  O    . GLN   A 1 118 ? 31.475 -12.895 9.591   1.00 14.72 ?  118 GLN   A O    1 
ATOM   2496 C  CB   . GLN   A 1 118 ? 31.909 -12.858 6.706   1.00 13.78 ?  118 GLN   A CB   1 
ATOM   2497 C  CG   . GLN   A 1 118 ? 32.379 -13.440 5.384   1.00 13.72 ?  118 GLN   A CG   1 
ATOM   2498 C  CD   . GLN   A 1 118 ? 33.212 -14.697 5.565   1.00 14.09 ?  118 GLN   A CD   1 
ATOM   2499 O  OE1  . GLN   A 1 118 ? 34.078 -14.758 6.446   1.00 15.02 ?  118 GLN   A OE1  1 
ATOM   2500 N  NE2  . GLN   A 1 118 ? 32.966 -15.700 4.722   1.00 14.11 ?  118 GLN   A NE2  1 
ATOM   2501 H  H    . GLN   A 1 118 ? 29.559 -13.345 6.065   1.00 15.43 ?  118 GLN   A H    1 
ATOM   2502 H  HA   . GLN   A 1 118 ? 31.339 -14.616 7.590   1.00 16.39 ?  118 GLN   A HA   1 
ATOM   2503 H  HB2  . GLN   A 1 118 ? 31.489 -12.005 6.529   1.00 16.55 ?  118 GLN   A HB2  1 
ATOM   2504 H  HB3  . GLN   A 1 118 ? 32.687 -12.735 7.273   1.00 16.55 ?  118 GLN   A HB3  1 
ATOM   2505 H  HG2  . GLN   A 1 118 ? 31.607 -13.663 4.838   1.00 16.47 ?  118 GLN   A HG2  1 
ATOM   2506 H  HG3  . GLN   A 1 118 ? 32.926 -12.780 4.924   1.00 16.47 ?  118 GLN   A HG3  1 
ATOM   2507 H  HE21 . GLN   A 1 118 ? 32.345 -15.617 4.121   1.00 16.94 ?  118 GLN   A HE21 1 
ATOM   2508 H  HE22 . GLN   A 1 118 ? 33.403 -16.434 4.780   1.00 16.94 ?  118 GLN   A HE22 1 
ATOM   2509 N  N    . HIS   A 1 119 ? 29.272 -13.022 9.113   1.00 13.33 ?  119 HIS   A N    1 
ATOM   2510 C  CA   . HIS   A 1 119 ? 28.819 -12.412 10.356  1.00 13.65 ?  119 HIS   A CA   1 
ATOM   2511 C  C    . HIS   A 1 119 ? 27.680 -13.233 10.931  1.00 13.94 ?  119 HIS   A C    1 
ATOM   2512 O  O    . HIS   A 1 119 ? 26.737 -13.572 10.212  1.00 14.09 ?  119 HIS   A O    1 
ATOM   2513 C  CB   . HIS   A 1 119 ? 28.362 -10.983 10.077  1.00 14.16 ?  119 HIS   A CB   1 
ATOM   2514 C  CG   . HIS   A 1 119 ? 29.440 -10.175 9.456   1.00 14.99 ?  119 HIS   A CG   1 
ATOM   2515 N  ND1  . HIS   A 1 119 ? 30.414 -9.558  10.204  1.00 17.37 ?  119 HIS   A ND1  1 
ATOM   2516 C  CD2  . HIS   A 1 119 ? 29.775 -9.991  8.159   1.00 16.01 ?  119 HIS   A CD2  1 
ATOM   2517 C  CE1  . HIS   A 1 119 ? 31.277 -8.976  9.390   1.00 17.56 ?  119 HIS   A CE1  1 
ATOM   2518 N  NE2  . HIS   A 1 119 ? 30.919 -9.233  8.144   1.00 17.47 ?  119 HIS   A NE2  1 
ATOM   2519 H  H    . HIS   A 1 119 ? 28.622 -13.283 8.605   1.00 16.00 ?  119 HIS   A H    1 
ATOM   2520 H  HA   . HIS   A 1 119 ? 29.547 -12.396 10.996  1.00 16.39 ?  119 HIS   A HA   1 
ATOM   2521 H  HB2  . HIS   A 1 119 ? 27.605 -11.007 9.471   1.00 17.00 ?  119 HIS   A HB2  1 
ATOM   2522 H  HB3  . HIS   A 1 119 ? 28.111 -10.566 10.914  1.00 17.00 ?  119 HIS   A HB3  1 
ATOM   2523 H  HD2  . HIS   A 1 119 ? 29.313 -10.311 7.414   1.00 19.22 ?  119 HIS   A HD2  1 
ATOM   2524 H  HE1  . HIS   A 1 119 ? 32.014 -8.470  9.644   1.00 21.08 ?  119 HIS   A HE1  1 
ATOM   2525 H  HE2  . HIS   A 1 119 ? 31.319 -8.946  7.435   1.00 20.98 ?  119 HIS   A HE2  1 
ATOM   2526 N  N    . GLU   A 1 120 ? 27.759 -13.529 12.230  1.00 14.96 ?  120 GLU   A N    1 
ATOM   2527 C  CA   . GLU   A 1 120 ? 26.801 -14.455 12.833  1.00 17.23 ?  120 GLU   A CA   1 
ATOM   2528 C  C    . GLU   A 1 120 ? 25.385 -13.892 12.879  1.00 15.53 ?  120 GLU   A C    1 
ATOM   2529 O  O    . GLU   A 1 120 ? 24.413 -14.656 12.767  1.00 15.74 ?  120 GLU   A O    1 
ATOM   2530 C  CB   . GLU   A 1 120 ? 27.262 -14.843 14.240  1.00 22.01 ?  120 GLU   A CB   1 
ATOM   2531 C  CG   . GLU   A 1 120 ? 28.468 -15.768 14.262  1.00 29.22 ?  120 GLU   A CG   1 
ATOM   2532 C  CD   . GLU   A 1 120 ? 28.610 -16.512 15.574  1.00 36.34 ?  120 GLU   A CD   1 
ATOM   2533 O  OE1  . GLU   A 1 120 ? 28.214 -15.957 16.621  1.00 37.93 ?  120 GLU   A OE1  1 
ATOM   2534 O  OE2  . GLU   A 1 120 ? 29.115 -17.655 15.557  1.00 39.58 -1 120 GLU   A OE2  1 
ATOM   2535 H  H    . GLU   A 1 120 ? 28.360 -13.222 12.775  1.00 17.96 ?  120 GLU   A H    1 
ATOM   2536 H  HA   . GLU   A 1 120 ? 26.785 -15.267 12.308  1.00 20.69 ?  120 GLU   A HA   1 
ATOM   2537 H  HB2  . GLU   A 1 120 ? 27.503 -14.044 14.734  1.00 26.42 ?  120 GLU   A HB2  1 
ATOM   2538 H  HB3  . GLU   A 1 120 ? 26.538 -15.303 14.697  1.00 26.42 ?  120 GLU   A HB3  1 
ATOM   2539 H  HG2  . GLU   A 1 120 ? 28.385 -16.419 13.549  1.00 35.07 ?  120 GLU   A HG2  1 
ATOM   2540 H  HG3  . GLU   A 1 120 ? 29.275 -15.245 14.147  1.00 35.07 ?  120 GLU   A HG3  1 
ATOM   2541 N  N    . VAL   A 1 121 ? 25.249 -12.581 13.085  1.00 14.97 ?  121 VAL   A N    1 
ATOM   2542 C  CA   . VAL   A 1 121 ? 23.951 -11.918 13.195  1.00 14.92 ?  121 VAL   A CA   1 
ATOM   2543 C  C    . VAL   A 1 121 ? 24.059 -10.541 12.551  1.00 13.69 ?  121 VAL   A C    1 
ATOM   2544 O  O    . VAL   A 1 121 ? 25.026 -9.812  12.799  1.00 14.10 ?  121 VAL   A O    1 
ATOM   2545 C  CB   . VAL   A 1 121 ? 23.510 -11.763 14.669  1.00 17.94 ?  121 VAL   A CB   1 
ATOM   2546 C  CG1  . VAL   A 1 121 ? 22.120 -11.148 14.747  1.00 18.44 ?  121 VAL   A CG1  1 
ATOM   2547 C  CG2  . VAL   A 1 121 ? 23.535 -13.090 15.410  1.00 19.69 ?  121 VAL   A CG2  1 
ATOM   2548 H  H    . VAL   A 1 121 ? 25.916 -12.039 13.169  1.00 17.97 ?  121 VAL   A H    1 
ATOM   2549 H  HA   . VAL   A 1 121 ? 23.283 -12.439 12.724  1.00 17.91 ?  121 VAL   A HA   1 
ATOM   2550 H  HB   . VAL   A 1 121 ? 24.122 -11.164 15.120  1.00 21.53 ?  121 VAL   A HB   1 
ATOM   2551 H  HG11 . VAL   A 1 121 ? 21.801 -11.202 15.663  1.00 22.13 ?  121 VAL   A HG11 1 
ATOM   2552 H  HG12 . VAL   A 1 121 ? 22.165 -10.221 14.469  1.00 22.13 ?  121 VAL   A HG12 1 
ATOM   2553 H  HG13 . VAL   A 1 121 ? 21.522 -11.642 14.163  1.00 22.13 ?  121 VAL   A HG13 1 
ATOM   2554 H  HG21 . VAL   A 1 121 ? 23.184 -12.959 16.312  1.00 23.63 ?  121 VAL   A HG21 1 
ATOM   2555 H  HG22 . VAL   A 1 121 ? 22.978 -13.732 14.939  1.00 23.63 ?  121 VAL   A HG22 1 
ATOM   2556 H  HG23 . VAL   A 1 121 ? 24.445 -13.414 15.460  1.00 23.63 ?  121 VAL   A HG23 1 
ATOM   2557 N  N    . LEU   A 1 122 ? 23.051 -10.162 11.759  1.00 12.91 ?  122 LEU   A N    1 
ATOM   2558 C  CA   . LEU   A 1 122 ? 23.053 -8.869  11.083  1.00 12.50 ?  122 LEU   A CA   1 
ATOM   2559 C  C    . LEU   A 1 122 ? 21.654 -8.274  11.055  1.00 12.51 ?  122 LEU   A C    1 
ATOM   2560 O  O    . LEU   A 1 122 ? 20.661 -8.990  10.913  1.00 13.48 ?  122 LEU   A O    1 
ATOM   2561 C  CB   . LEU   A 1 122 ? 23.484 -8.979  9.615   1.00 13.78 ?  122 LEU   A CB   1 
ATOM   2562 C  CG   . LEU   A 1 122 ? 24.705 -9.820  9.266   1.00 13.86 ?  122 LEU   A CG   1 
ATOM   2563 C  CD1  . LEU   A 1 122 ? 24.316 -11.273 9.037   1.00 14.81 ?  122 LEU   A CD1  1 
ATOM   2564 C  CD2  . LEU   A 1 122 ? 25.402 -9.262  8.039   1.00 13.49 ?  122 LEU   A CD2  1 
ATOM   2565 H  H    . LEU   A 1 122 ? 22.348 -10.639 11.602  1.00 15.50 ?  122 LEU   A H    1 
ATOM   2566 H  HA   . LEU   A 1 122 ? 23.650 -8.257  11.541  1.00 15.00 ?  122 LEU   A HA   1 
ATOM   2567 H  HB2  . LEU   A 1 122 ? 22.749 -9.351  9.114   1.00 16.54 ?  122 LEU   A HB2  1 
ATOM   2568 H  HB3  . LEU   A 1 122 ? 23.676 -8.088  9.293   1.00 16.54 ?  122 LEU   A HB3  1 
ATOM   2569 H  HG   . LEU   A 1 122 ? 25.344 -9.805  9.998   1.00 16.64 ?  122 LEU   A HG   1 
ATOM   2570 H  HD11 . LEU   A 1 122 ? 25.101 -11.788 8.785   1.00 17.78 ?  122 LEU   A HD11 1 
ATOM   2571 H  HD12 . LEU   A 1 122 ? 23.937 -11.635 9.855   1.00 17.78 ?  122 LEU   A HD12 1 
ATOM   2572 H  HD13 . LEU   A 1 122 ? 23.656 -11.318 8.324   1.00 17.78 ?  122 LEU   A HD13 1 
ATOM   2573 H  HD21 . LEU   A 1 122 ? 26.159 -9.836  7.805   1.00 16.20 ?  122 LEU   A HD21 1 
ATOM   2574 H  HD22 . LEU   A 1 122 ? 24.777 -9.237  7.300   1.00 16.20 ?  122 LEU   A HD22 1 
ATOM   2575 H  HD23 . LEU   A 1 122 ? 25.723 -8.370  8.236   1.00 16.20 ?  122 LEU   A HD23 1 
ATOM   2576 N  N    . LEU   A 1 123 ? 21.597 -6.945  11.156  1.00 12.00 ?  123 LEU   A N    1 
ATOM   2577 C  CA   . LEU   A 1 123 ? 20.429 -6.147  10.785  1.00 11.82 ?  123 LEU   A CA   1 
ATOM   2578 C  C    . LEU   A 1 123 ? 20.680 -5.627  9.378   1.00 11.33 ?  123 LEU   A C    1 
ATOM   2579 O  O    . LEU   A 1 123 ? 21.730 -5.029  9.132   1.00 12.11 ?  123 LEU   A O    1 
ATOM   2580 C  CB   . LEU   A 1 123 ? 20.295 -4.963  11.743  1.00 12.36 ?  123 LEU   A CB   1 
ATOM   2581 C  CG   . LEU   A 1 123 ? 19.247 -3.901  11.404  1.00 13.13 ?  123 LEU   A CG   1 
ATOM   2582 C  CD1  . LEU   A 1 123 ? 17.849 -4.507  11.382  1.00 13.74 ?  123 LEU   A CD1  1 
ATOM   2583 C  CD2  . LEU   A 1 123 ? 19.321 -2.733  12.382  1.00 14.10 ?  123 LEU   A CD2  1 
ATOM   2584 H  H    . LEU   A 1 123 ? 22.256 -6.465  11.438  1.00 14.41 ?  123 LEU   A H    1 
ATOM   2585 H  HA   . LEU   A 1 123 ? 19.623 -6.688  10.801  1.00 14.19 ?  123 LEU   A HA   1 
ATOM   2586 H  HB2  . LEU   A 1 123 ? 20.067 -5.310  12.622  1.00 14.84 ?  123 LEU   A HB2  1 
ATOM   2587 H  HB3  . LEU   A 1 123 ? 21.148 -4.511  11.791  1.00 14.84 ?  123 LEU   A HB3  1 
ATOM   2588 H  HG   . LEU   A 1 123 ? 19.423 -3.548  10.517  1.00 15.76 ?  123 LEU   A HG   1 
ATOM   2589 H  HD11 . LEU   A 1 123 ? 17.200 -3.810  11.210  1.00 16.50 ?  123 LEU   A HD11 1 
ATOM   2590 H  HD12 . LEU   A 1 123 ? 17.807 -5.180  10.683  1.00 16.50 ?  123 LEU   A HD12 1 
ATOM   2591 H  HD13 . LEU   A 1 123 ? 17.673 -4.919  12.244  1.00 16.50 ?  123 LEU   A HD13 1 
ATOM   2592 H  HD21 . LEU   A 1 123 ? 18.645 -2.077  12.148  1.00 16.93 ?  123 LEU   A HD21 1 
ATOM   2593 H  HD22 . LEU   A 1 123 ? 19.153 -3.068  13.281  1.00 16.93 ?  123 LEU   A HD22 1 
ATOM   2594 H  HD23 . LEU   A 1 123 ? 20.201 -2.338  12.336  1.00 16.93 ?  123 LEU   A HD23 1 
ATOM   2595 N  N    A ALA   A 1 124 ? 19.711 -5.797  8.473   0.64 10.80 ?  124 ALA   A N    1 
ATOM   2596 N  N    B ALA   A 1 124 ? 19.761 -5.878  8.455   0.36 11.36 ?  124 ALA   A N    1 
ATOM   2597 C  CA   A ALA   A 1 124 ? 19.987 -5.500  7.074   0.64 10.36 ?  124 ALA   A CA   1 
ATOM   2598 C  CA   B ALA   A 1 124 ? 20.065 -5.650  7.053   0.36 11.63 ?  124 ALA   A CA   1 
ATOM   2599 C  C    A ALA   A 1 124 ? 18.747 -5.060  6.309   0.64 10.36 ?  124 ALA   A C    1 
ATOM   2600 C  C    B ALA   A 1 124 ? 18.836 -5.159  6.306   0.36 11.28 ?  124 ALA   A C    1 
ATOM   2601 O  O    A ALA   A 1 124 ? 17.621 -5.445  6.656   0.64 11.42 ?  124 ALA   A O    1 
ATOM   2602 O  O    B ALA   A 1 124 ? 17.700 -5.431  6.711   0.36 11.68 ?  124 ALA   A O    1 
ATOM   2603 C  CB   A ALA   A 1 124 ? 20.588 -6.718  6.363   0.64 11.01 ?  124 ALA   A CB   1 
ATOM   2604 C  CB   B ALA   A 1 124 ? 20.589 -6.932  6.390   0.36 12.46 ?  124 ALA   A CB   1 
ATOM   2605 H  H    A ALA   A 1 124 ? 18.907 -6.063  8.642   0.64 12.97 ?  124 ALA   A H    1 
ATOM   2606 H  H    B ALA   A 1 124 ? 18.961 -6.172  8.605   0.36 13.64 ?  124 ALA   A H    1 
ATOM   2607 H  HA   A ALA   A 1 124 ? 20.638 -4.784  7.042   0.64 12.44 ?  124 ALA   A HA   1 
ATOM   2608 H  HA   B ALA   A 1 124 ? 20.768 -4.985  6.993   0.36 13.96 ?  124 ALA   A HA   1 
ATOM   2609 H  HB1  A ALA   A 1 124 ? 20.763 -6.488  5.436   0.64 13.22 ?  124 ALA   A HB1  1 
ATOM   2610 H  HB1  B ALA   A 1 124 ? 20.797 -6.749  5.460   0.36 14.96 ?  124 ALA   A HB1  1 
ATOM   2611 H  HB2  A ALA   A 1 124 ? 21.419 -6.960  6.804   0.64 13.22 ?  124 ALA   A HB2  1 
ATOM   2612 H  HB2  B ALA   A 1 124 ? 21.395 -7.228  6.852   0.36 14.96 ?  124 ALA   A HB2  1 
ATOM   2613 H  HB3  A ALA   A 1 124 ? 19.961 -7.454  6.410   0.64 13.22 ?  124 ALA   A HB3  1 
ATOM   2614 H  HB3  B ALA   A 1 124 ? 19.910 -7.621  6.449   0.36 14.96 ?  124 ALA   A HB3  1 
ATOM   2615 N  N    A PRO   A 1 125 ? 18.937 -4.297  5.235   0.64 10.82 ?  125 PRO   A N    1 
ATOM   2616 N  N    B PRO   A 1 125 ? 19.038 -4.440  5.195   0.36 10.63 ?  125 PRO   A N    1 
ATOM   2617 C  CA   A PRO   A 1 125 ? 17.894 -4.087  4.232   0.64 11.20 ?  125 PRO   A CA   1 
ATOM   2618 C  CA   B PRO   A 1 125 ? 17.925 -4.087  4.310   0.36 11.08 ?  125 PRO   A CA   1 
ATOM   2619 C  C    A PRO   A 1 125 ? 17.958 -5.181  3.171   0.64 10.83 ?  125 PRO   A C    1 
ATOM   2620 C  C    B PRO   A 1 125 ? 17.870 -5.066  3.150   0.36 11.53 ?  125 PRO   A C    1 
ATOM   2621 O  O    A PRO   A 1 125 ? 18.930 -5.935  3.076   0.64 11.27 ?  125 PRO   A O    1 
ATOM   2622 O  O    B PRO   A 1 125 ? 18.775 -5.897  3.006   0.36 12.01 ?  125 PRO   A O    1 
ATOM   2623 C  CB   A PRO   A 1 125 ? 18.332 -2.753  3.612   0.64 11.54 ?  125 PRO   A CB   1 
ATOM   2624 C  CB   B PRO   A 1 125 ? 18.342 -2.702  3.810   0.36 10.65 ?  125 PRO   A CB   1 
ATOM   2625 C  CG   A PRO   A 1 125 ? 19.841 -2.895  3.571   0.64 11.55 ?  125 PRO   A CG   1 
ATOM   2626 C  CG   B PRO   A 1 125 ? 19.856 -2.853  3.646   0.36 10.57 ?  125 PRO   A CG   1 
ATOM   2627 C  CD   A PRO   A 1 125 ? 20.180 -3.577  4.887   0.64 11.54 ?  125 PRO   A CD   1 
ATOM   2628 C  CD   B PRO   A 1 125 ? 20.305 -3.854  4.714   0.36 10.07 ?  125 PRO   A CD   1 
ATOM   2629 H  HA   A PRO   A 1 125 ? 17.008 -4.026  4.622   0.64 13.45 ?  125 PRO   A HA   1 
ATOM   2630 H  HA   B PRO   A 1 125 ? 17.076 -4.043  4.792   0.36 13.30 ?  125 PRO   A HA   1 
ATOM   2631 H  HB2  A PRO   A 1 125 ? 17.956 -2.660  2.720   0.64 13.86 ?  125 PRO   A HB2  1 
ATOM   2632 H  HB2  B PRO   A 1 125 ? 17.910 -2.512  2.959   0.36 12.79 ?  125 PRO   A HB2  1 
ATOM   2633 H  HB3  A PRO   A 1 125 ? 18.058 -2.015  4.184   0.64 13.86 ?  125 PRO   A HB3  1 
ATOM   2634 H  HB3  B PRO   A 1 125 ? 18.121 -2.024  4.469   0.36 12.79 ?  125 PRO   A HB3  1 
ATOM   2635 H  HG2  A PRO   A 1 125 ? 20.100 -3.449  2.817   0.64 13.87 ?  125 PRO   A HG2  1 
ATOM   2636 H  HG2  B PRO   A 1 125 ? 20.053 -3.192  2.759   0.36 12.70 ?  125 PRO   A HG2  1 
ATOM   2637 H  HG3  A PRO   A 1 125 ? 20.252 -2.018  3.513   0.64 13.87 ?  125 PRO   A HG3  1 
ATOM   2638 H  HG3  B PRO   A 1 125 ? 20.284 -1.993  3.784   0.36 12.70 ?  125 PRO   A HG3  1 
ATOM   2639 H  HD2  A PRO   A 1 125 ? 20.911 -4.195  4.771   0.64 13.86 ?  125 PRO   A HD2  1 
ATOM   2640 H  HD2  B PRO   A 1 125 ? 20.869 -4.537  4.319   0.36 12.09 ?  125 PRO   A HD2  1 
ATOM   2641 H  HD3  A PRO   A 1 125 ? 20.382 -2.908  5.567   0.64 13.86 ?  125 PRO   A HD3  1 
ATOM   2642 H  HD3  B PRO   A 1 125 ? 20.761 -3.389  5.434   0.36 12.09 ?  125 PRO   A HD3  1 
ATOM   2643 N  N    A LEU   A 1 126 ? 16.914 -5.230  2.350   0.64 10.99 ?  126 LEU   A N    1 
ATOM   2644 N  N    B LEU   A 1 126 ? 16.854 -4.970  2.298   0.36 11.96 ?  126 LEU   A N    1 
ATOM   2645 C  CA   A LEU   A 1 126 ? 16.941 -6.062  1.156   0.64 11.16 ?  126 LEU   A CA   1 
ATOM   2646 C  CA   B LEU   A 1 126 ? 16.828 -5.772  1.081   0.36 11.75 ?  126 LEU   A CA   1 
ATOM   2647 C  C    A LEU   A 1 126 ? 17.867 -5.450  0.113   0.64 11.45 ?  126 LEU   A C    1 
ATOM   2648 C  C    B LEU   A 1 126 ? 17.783 -5.168  0.057   0.36 11.60 ?  126 LEU   A C    1 
ATOM   2649 O  O    A LEU   A 1 126 ? 17.620 -4.350  -0.391  0.64 12.43 ?  126 LEU   A O    1 
ATOM   2650 O  O    B LEU   A 1 126 ? 17.578 -4.040  -0.402  0.36 12.36 ?  126 LEU   A O    1 
ATOM   2651 C  CB   A LEU   A 1 126 ? 15.536 -6.218  0.593   0.64 11.72 ?  126 LEU   A CB   1 
ATOM   2652 C  CB   B LEU   A 1 126 ? 15.417 -5.820  0.503   0.36 12.55 ?  126 LEU   A CB   1 
ATOM   2653 C  CG   A LEU   A 1 126 ? 14.646 -7.154  1.401   0.64 12.03 ?  126 LEU   A CG   1 
ATOM   2654 C  CG   B LEU   A 1 126 ? 14.404 -6.745  1.174   0.36 13.08 ?  126 LEU   A CG   1 
ATOM   2655 C  CD1  A LEU   A 1 126 ? 13.207 -6.997  0.957   0.64 13.17 ?  126 LEU   A CD1  1 
ATOM   2656 C  CD1  B LEU   A 1 126 ? 13.085 -6.669  0.428   0.36 13.61 ?  126 LEU   A CD1  1 
ATOM   2657 C  CD2  A LEU   A 1 126 ? 15.109 -8.607  1.255   0.64 11.85 ?  126 LEU   A CD2  1 
ATOM   2658 C  CD2  B LEU   A 1 126 ? 14.901 -8.178  1.219   0.36 13.53 ?  126 LEU   A CD2  1 
ATOM   2659 H  H    A LEU   A 1 126 ? 16.189 -4.784  2.455   0.64 13.20 ?  126 LEU   A H    1 
ATOM   2660 H  H    B LEU   A 1 126 ? 16.173 -4.447  2.405   0.36 14.36 ?  126 LEU   A H    1 
ATOM   2661 H  HA   A LEU   A 1 126 ? 17.282 -6.938  1.381   0.64 13.40 ?  126 LEU   A HA   1 
ATOM   2662 H  HA   B LEU   A 1 126 ? 17.117 -6.674  1.289   0.36 14.11 ?  126 LEU   A HA   1 
ATOM   2663 H  HB2  A LEU   A 1 126 ? 15.106 -5.349  0.576   0.64 14.07 ?  126 LEU   A HB2  1 
ATOM   2664 H  HB2  B LEU   A 1 126 ? 15.049 -4.924  0.537   0.36 15.07 ?  126 LEU   A HB2  1 
ATOM   2665 H  HB3  A LEU   A 1 126 ? 15.595 -6.572  -0.309  0.64 14.07 ?  126 LEU   A HB3  1 
ATOM   2666 H  HB3  B LEU   A 1 126 ? 15.489 -6.101  -0.421  0.36 15.07 ?  126 LEU   A HB3  1 
ATOM   2667 H  HG   A LEU   A 1 126 ? 14.699 -6.919  2.339   0.64 14.44 ?  126 LEU   A HG   1 
ATOM   2668 H  HG   B LEU   A 1 126 ? 14.250 -6.448  2.084   0.36 15.71 ?  126 LEU   A HG   1 
ATOM   2669 H  HD11 A LEU   A 1 126 ? 12.650 -7.606  1.467   0.64 15.81 ?  126 LEU   A HD11 1 
ATOM   2670 H  HD11 B LEU   A 1 126 ? 12.443 -7.255  0.859   0.36 16.34 ?  126 LEU   A HD11 1 
ATOM   2671 H  HD12 A LEU   A 1 126 ? 12.930 -6.083  1.112   0.64 15.81 ?  126 LEU   A HD12 1 
ATOM   2672 H  HD12 B LEU   A 1 126 ? 12.764 -5.756  0.443   0.36 16.34 ?  126 LEU   A HD12 1 
ATOM   2673 H  HD13 A LEU   A 1 126 ? 13.145 -7.208  0.011   0.64 15.81 ?  126 LEU   A HD13 1 
ATOM   2674 H  HD13 B LEU   A 1 126 ? 13.226 -6.956  -0.490  0.36 16.34 ?  126 LEU   A HD13 1 
ATOM   2675 H  HD21 A LEU   A 1 126 ? 14.448 -9.194  1.650   0.64 14.23 ?  126 LEU   A HD21 1 
ATOM   2676 H  HD21 B LEU   A 1 126 ? 14.168 -8.758  1.472   0.36 16.24 ?  126 LEU   A HD21 1 
ATOM   2677 H  HD22 A LEU   A 1 126 ? 15.213 -8.812  0.311   0.64 14.23 ?  126 LEU   A HD22 1 
ATOM   2678 H  HD22 B LEU   A 1 126 ? 15.230 -8.422  0.340   0.36 16.24 ?  126 LEU   A HD22 1 
ATOM   2679 H  HD23 A LEU   A 1 126 ? 15.962 -8.716  1.709   0.64 14.23 ?  126 LEU   A HD23 1 
ATOM   2680 H  HD23 B LEU   A 1 126 ? 15.616 -8.242  1.870   0.36 16.24 ?  126 LEU   A HD23 1 
ATOM   2681 N  N    A LEU   A 1 127 ? 18.929 -6.175  -0.218  0.64 11.72 ?  127 LEU   A N    1 
ATOM   2682 N  N    B LEU   A 1 127 ? 18.819 -5.915  -0.314  0.36 11.00 ?  127 LEU   A N    1 
ATOM   2683 C  CA   A LEU   A 1 127 ? 19.912 -5.678  -1.168  0.64 11.24 ?  127 LEU   A CA   1 
ATOM   2684 C  CA   B LEU   A 1 127 ? 19.812 -5.385  -1.238  0.36 11.39 ?  127 LEU   A CA   1 
ATOM   2685 C  C    A LEU   A 1 127 ? 19.280 -5.474  -2.534  0.64 10.52 ?  127 LEU   A C    1 
ATOM   2686 C  C    B LEU   A 1 127 ? 19.274 -5.337  -2.668  0.36 11.76 ?  127 LEU   A C    1 
ATOM   2687 O  O    A LEU   A 1 127 ? 18.446 -6.267  -2.986  0.64 11.18 ?  127 LEU   A O    1 
ATOM   2688 O  O    B LEU   A 1 127 ? 18.451 -6.160  -3.085  0.36 11.97 ?  127 LEU   A O    1 
ATOM   2689 C  CB   A LEU   A 1 127 ? 21.073 -6.663  -1.279  0.64 11.66 ?  127 LEU   A CB   1 
ATOM   2690 C  CB   B LEU   A 1 127 ? 21.093 -6.221  -1.190  0.36 11.84 ?  127 LEU   A CB   1 
ATOM   2691 C  CG   A LEU   A 1 127 ? 21.869 -6.882  0.006   0.64 11.86 ?  127 LEU   A CG   1 
ATOM   2692 C  CG   B LEU   A 1 127 ? 21.877 -6.208  0.128   0.36 12.73 ?  127 LEU   A CG   1 
ATOM   2693 C  CD1  A LEU   A 1 127 ? 22.955 -7.892  -0.256  0.64 12.28 ?  127 LEU   A CD1  1 
ATOM   2694 C  CD1  B LEU   A 1 127 ? 23.044 -7.183  0.066   0.36 13.18 ?  127 LEU   A CD1  1 
ATOM   2695 C  CD2  A LEU   A 1 127 ? 22.471 -5.587  0.504   0.64 12.80 ?  127 LEU   A CD2  1 
ATOM   2696 C  CD2  B LEU   A 1 127 ? 22.367 -4.799  0.462   0.36 13.35 ?  127 LEU   A CD2  1 
ATOM   2697 H  H    A LEU   A 1 127 ? 19.103 -6.955  0.095   0.64 14.08 ?  127 LEU   A H    1 
ATOM   2698 H  H    B LEU   A 1 127 ? 18.970 -6.719  -0.037  0.36 13.21 ?  127 LEU   A H    1 
ATOM   2699 H  HA   A LEU   A 1 127 ? 20.258 -4.830  -0.865  0.64 13.49 ?  127 LEU   A HA   1 
ATOM   2700 H  HA   B LEU   A 1 127 ? 20.032 -4.479  -0.966  0.36 13.68 ?  127 LEU   A HA   1 
ATOM   2701 H  HB2  A LEU   A 1 127 ? 20.720 -7.527  -1.554  0.64 14.00 ?  127 LEU   A HB2  1 
ATOM   2702 H  HB2  B LEU   A 1 127 ? 20.862 -7.143  -1.376  0.36 14.21 ?  127 LEU   A HB2  1 
ATOM   2703 H  HB3  A LEU   A 1 127 ? 21.690 -6.340  -1.953  0.64 14.00 ?  127 LEU   A HB3  1 
ATOM   2704 H  HB3  B LEU   A 1 127 ? 21.690 -5.893  -1.881  0.36 14.21 ?  127 LEU   A HB3  1 
ATOM   2705 H  HG   A LEU   A 1 127 ? 21.279 -7.235  0.693   0.64 14.25 ?  127 LEU   A HG   1 
ATOM   2706 H  HG   B LEU   A 1 127 ? 21.290 -6.494  0.844   0.36 15.29 ?  127 LEU   A HG   1 
ATOM   2707 H  HD11 A LEU   A 1 127 ? 23.425 -8.072  0.575   0.64 14.75 ?  127 LEU   A HD11 1 
ATOM   2708 H  HD11 B LEU   A 1 127 ? 23.535 -7.139  0.902   0.36 15.83 ?  127 LEU   A HD11 1 
ATOM   2709 H  HD12 A LEU   A 1 127 ? 22.554 -8.711  -0.591  0.64 14.75 ?  127 LEU   A HD12 1 
ATOM   2710 H  HD12 B LEU   A 1 127 ? 22.697 -8.079  -0.067  0.36 15.83 ?  127 LEU   A HD12 1 
ATOM   2711 H  HD13 A LEU   A 1 127 ? 23.569 -7.532  -0.913  0.64 14.75 ?  127 LEU   A HD13 1 
ATOM   2712 H  HD13 B LEU   A 1 127 ? 23.621 -6.937  -0.672  0.36 15.83 ?  127 LEU   A HD13 1 
ATOM   2713 H  HD21 A LEU   A 1 127 ? 23.092 -5.783  1.219   0.64 15.37 ?  127 LEU   A HD21 1 
ATOM   2714 H  HD21 B LEU   A 1 127 ? 22.952 -4.843  1.234   0.36 16.02 ?  127 LEU   A HD21 1 
ATOM   2715 H  HD22 A LEU   A 1 127 ? 22.937 -5.156  -0.232  0.64 15.37 ?  127 LEU   A HD22 1 
ATOM   2716 H  HD22 B LEU   A 1 127 ? 22.851 -4.445  -0.300  0.36 16.02 ?  127 LEU   A HD22 1 
ATOM   2717 H  HD23 A LEU   A 1 127 ? 21.760 -5.011  0.826   0.64 15.37 ?  127 LEU   A HD23 1 
ATOM   2718 H  HD23 B LEU   A 1 127 ? 21.602 -4.237  0.658   0.36 16.02 ?  127 LEU   A HD23 1 
ATOM   2719 N  N    A SER   A 1 128 ? 19.703 -4.402  -3.197  0.64 10.59 ?  128 SER   A N    1 
ATOM   2720 N  N    B SER   A 1 128 ? 19.758 -4.346  -3.416  0.36 12.31 ?  128 SER   A N    1 
ATOM   2721 C  CA   A SER   A 1 128 ? 19.297 -4.011  -4.540  0.64 10.49 ?  128 SER   A CA   1 
ATOM   2722 C  CA   B SER   A 1 128 ? 19.456 -4.134  -4.831  0.36 12.62 ?  128 SER   A CA   1 
ATOM   2723 C  C    A SER   A 1 128 ? 17.842 -3.573  -4.635  0.64 10.00 ?  128 SER   A C    1 
ATOM   2724 C  C    B SER   A 1 128 ? 18.039 -3.644  -5.115  0.36 12.85 ?  128 SER   A C    1 
ATOM   2725 O  O    A SER   A 1 128 ? 17.384 -3.271  -5.738  0.64 10.84 ?  128 SER   A O    1 
ATOM   2726 O  O    B SER   A 1 128 ? 17.739 -3.254  -6.248  0.36 12.89 ?  128 SER   A O    1 
ATOM   2727 C  CB   A SER   A 1 128 ? 19.633 -5.062  -5.608  0.64 10.70 ?  128 SER   A CB   1 
ATOM   2728 C  CB   B SER   A 1 128 ? 19.786 -5.369  -5.674  0.36 12.43 ?  128 SER   A CB   1 
ATOM   2729 O  OG   A SER   A 1 128 ? 21.043 -5.256  -5.671  0.64 11.13 ?  128 SER   A OG   1 
ATOM   2730 O  OG   B SER   A 1 128 ? 21.189 -5.551  -5.760  0.36 12.47 ?  128 SER   A OG   1 
ATOM   2731 H  H    A SER   A 1 128 ? 20.275 -3.847  -2.863  0.64 12.72 ?  128 SER   A H    1 
ATOM   2732 H  H    B SER   A 1 128 ? 20.304 -3.762  -3.103  0.36 14.79 ?  128 SER   A H    1 
ATOM   2733 H  HA   A SER   A 1 128 ? 19.819 -3.232  -4.769  0.64 12.60 ?  128 SER   A HA   1 
ATOM   2734 H  HA   B SER   A 1 128 ? 20.047 -3.435  -5.132  0.36 15.15 ?  128 SER   A HA   1 
ATOM   2735 H  HB2  A SER   A 1 128 ? 19.200 -5.897  -5.377  0.64 12.85 ?  128 SER   A HB2  1 
ATOM   2736 H  HB2  B SER   A 1 128 ? 19.387 -6.153  -5.274  0.36 14.92 ?  128 SER   A HB2  1 
ATOM   2737 H  HB3  A SER   A 1 128 ? 19.308 -4.746  -6.470  0.64 12.85 ?  128 SER   A HB3  1 
ATOM   2738 H  HB3  B SER   A 1 128 ? 19.436 -5.235  -6.570  0.36 14.92 ?  128 SER   A HB3  1 
ATOM   2739 H  HG   A SER   A 1 128 ? 21.418 -4.528  -5.870  0.64 13.37 ?  128 SER   A HG   1 
ATOM   2740 H  HG   B SER   A 1 128 ? 21.545 -4.867  -6.097  0.36 14.97 ?  128 SER   A HG   1 
ATOM   2741 N  N    A ALA   A 1 129 ? 17.116 -3.503  -3.522  0.64 10.24 ?  129 ALA   A N    1 
ATOM   2742 N  N    B ALA   A 1 129 ? 17.165 -3.646  -4.118  0.36 13.23 ?  129 ALA   A N    1 
ATOM   2743 C  CA   A ALA   A 1 129 ? 15.745 -3.024  -3.533  0.64 10.53 ?  129 ALA   A CA   1 
ATOM   2744 C  CA   B ALA   A 1 129 ? 15.824 -3.111  -4.304  0.36 13.77 ?  129 ALA   A CA   1 
ATOM   2745 C  C    A ALA   A 1 129 ? 15.722 -1.493  -3.496  0.64 10.82 ?  129 ALA   A C    1 
ATOM   2746 C  C    B ALA   A 1 129 ? 15.833 -1.621  -3.946  0.36 14.01 ?  129 ALA   A C    1 
ATOM   2747 O  O    A ALA   A 1 129 ? 16.760 -0.821  -3.553  0.64 11.45 ?  129 ALA   A O    1 
ATOM   2748 O  O    B ALA   A 1 129 ? 16.893 -0.989  -3.913  0.36 13.69 ?  129 ALA   A O    1 
ATOM   2749 C  CB   A ALA   A 1 129 ? 14.958 -3.651  -2.381  0.64 11.74 ?  129 ALA   A CB   1 
ATOM   2750 C  CB   B ALA   A 1 129 ? 14.808 -3.973  -3.549  0.36 15.18 ?  129 ALA   A CB   1 
ATOM   2751 H  H    A ALA   A 1 129 ? 17.400 -3.724  -2.739  0.64 12.30 ?  129 ALA   A H    1 
ATOM   2752 H  H    B ALA   A 1 129 ? 17.316 -3.954  -3.328  0.36 15.89 ?  129 ALA   A H    1 
ATOM   2753 H  HA   A ALA   A 1 129 ? 15.322 -3.299  -4.353  0.64 12.65 ?  129 ALA   A HA   1 
ATOM   2754 H  HA   B ALA   A 1 129 ? 15.601 -3.169  -5.244  0.36 16.54 ?  129 ALA   A HA   1 
ATOM   2755 H  HB1  A ALA   A 1 129 ? 14.043 -3.327  -2.404  0.64 14.10 ?  129 ALA   A HB1  1 
ATOM   2756 H  HB1  B ALA   A 1 129 ? 13.922 -3.604  -3.687  0.36 18.23 ?  129 ALA   A HB1  1 
ATOM   2757 H  HB2  A ALA   A 1 129 ? 14.970 -4.615  -2.477  0.64 14.10 ?  129 ALA   A HB2  1 
ATOM   2758 H  HB2  B ALA   A 1 129 ? 14.846 -4.878  -3.903  0.36 18.23 ?  129 ALA   A HB2  1 
ATOM   2759 H  HB3  A ALA   A 1 129 ? 15.372 -3.400  -1.536  0.64 14.10 ?  129 ALA   A HB3  1 
ATOM   2760 H  HB3  B ALA   A 1 129 ? 15.030 -3.974  -2.610  0.36 18.23 ?  129 ALA   A HB3  1 
ATOM   2761 N  N    A GLY   A 1 130 ? 14.514 -0.935  -3.423  0.64 11.75 ?  130 GLY   A N    1 
ATOM   2762 N  N    B GLY   A 1 130 ? 14.664 -1.036  -3.702  0.36 14.36 ?  130 GLY   A N    1 
ATOM   2763 C  CA   A GLY   A 1 130 ? 14.367 0.512   -3.429  0.64 12.50 ?  130 GLY   A CA   1 
ATOM   2764 C  CA   B GLY   A 1 130 ? 14.631 0.387   -3.414  0.36 14.70 ?  130 GLY   A CA   1 
ATOM   2765 C  C    A GLY   A 1 130 ? 15.012 1.121   -4.658  0.64 12.18 ?  130 GLY   A C    1 
ATOM   2766 C  C    B GLY   A 1 130 ? 15.146 1.176   -4.598  0.36 14.76 ?  130 GLY   A C    1 
ATOM   2767 O  O    A GLY   A 1 130 ? 14.816 0.651   -5.784  0.64 12.30 ?  130 GLY   A O    1 
ATOM   2768 O  O    B GLY   A 1 130 ? 14.855 0.862   -5.757  0.36 14.97 ?  130 GLY   A O    1 
ATOM   2769 H  H    A GLY   A 1 130 ? 13.767 -1.371  -3.375  0.64 14.11 ?  130 GLY   A H    1 
ATOM   2770 H  H    B GLY   A 1 130 ? 13.896 -1.429  -3.709  0.36 17.24 ?  130 GLY   A H    1 
ATOM   2771 H  HA2  A GLY   A 1 130 ? 13.419 0.743   -3.426  0.64 15.01 ?  130 GLY   A HA2  1 
ATOM   2772 H  HA2  B GLY   A 1 130 ? 13.718 0.665   -3.182  0.36 17.65 ?  130 GLY   A HA2  1 
ATOM   2773 H  HA3  A GLY   A 1 130 ? 14.780 0.886   -2.644  0.64 15.01 ?  130 GLY   A HA3  1 
ATOM   2774 H  HA3  B GLY   A 1 130 ? 15.217 0.575   -2.662  0.36 17.65 ?  130 GLY   A HA3  1 
ATOM   2775 N  N    A ILE   A 1 131 ? 15.792 2.189   -4.447  0.64 12.45 ?  131 ILE   A N    1 
ATOM   2776 N  N    B ILE   A 1 131 ? 15.945 2.209   -4.312  0.36 14.87 ?  131 ILE   A N    1 
ATOM   2777 C  CA   A ILE   A 1 131 ? 16.373 2.949   -5.553  0.64 12.62 ?  131 ILE   A CA   1 
ATOM   2778 C  CA   B ILE   A 1 131 ? 16.512 3.032   -5.374  0.36 14.69 ?  131 ILE   A CA   1 
ATOM   2779 C  C    A ILE   A 1 131 ? 17.442 2.187   -6.327  0.64 12.54 ?  131 ILE   A C    1 
ATOM   2780 C  C    B ILE   A 1 131 ? 17.460 2.259   -6.287  0.36 14.55 ?  131 ILE   A C    1 
ATOM   2781 O  O    A ILE   A 1 131 ? 17.910 2.693   -7.354  0.64 13.34 ?  131 ILE   A O    1 
ATOM   2782 O  O    B ILE   A 1 131 ? 17.798 2.752   -7.368  0.36 14.88 ?  131 ILE   A O    1 
ATOM   2783 C  CB   A ILE   A 1 131 ? 16.885 4.338   -5.108  0.64 13.51 ?  131 ILE   A CB   1 
ATOM   2784 C  CB   B ILE   A 1 131 ? 17.189 4.314   -4.828  0.36 15.01 ?  131 ILE   A CB   1 
ATOM   2785 C  CG1  A ILE   A 1 131 ? 18.093 4.214   -4.173  0.64 14.88 ?  131 ILE   A CG1  1 
ATOM   2786 C  CG1  B ILE   A 1 131 ? 18.436 3.992   -3.999  0.36 15.59 ?  131 ILE   A CG1  1 
ATOM   2787 C  CG2  A ILE   A 1 131 ? 15.760 5.137   -4.451  0.64 13.58 ?  131 ILE   A CG2  1 
ATOM   2788 C  CG2  B ILE   A 1 131 ? 16.212 5.128   -4.002  0.36 15.23 ?  131 ILE   A CG2  1 
ATOM   2789 C  CD1  A ILE   A 1 131 ? 18.731 5.554   -3.821  0.64 16.02 ?  131 ILE   A CD1  1 
ATOM   2790 C  CD1  B ILE   A 1 131 ? 19.134 5.239   -3.436  0.36 16.20 ?  131 ILE   A CD1  1 
ATOM   2791 H  H    A ILE   A 1 131 ? 15.979 2.497   -3.669  0.64 14.95 ?  131 ILE   A H    1 
ATOM   2792 H  H    B ILE   A 1 131 ? 16.152 2.453   -3.510  0.36 17.85 ?  131 ILE   A H    1 
ATOM   2793 H  HA   A ILE   A 1 131 ? 15.663 3.112   -6.188  0.64 15.16 ?  131 ILE   A HA   1 
ATOM   2794 H  HA   B ILE   A 1 131 ? 15.774 3.333   -5.927  0.36 17.63 ?  131 ILE   A HA   1 
ATOM   2795 H  HB   A ILE   A 1 131 ? 17.166 4.814   -5.902  0.64 16.22 ?  131 ILE   A HB   1 
ATOM   2796 H  HB   B ILE   A 1 131 ? 17.458 4.851   -5.588  0.36 18.02 ?  131 ILE   A HB   1 
ATOM   2797 H  HG12 A ILE   A 1 131 ? 17.808 3.792   -3.348  0.64 17.87 ?  131 ILE   A HG12 1 
ATOM   2798 H  HG12 B ILE   A 1 131 ? 18.179 3.436   -3.251  0.36 18.72 ?  131 ILE   A HG12 1 
ATOM   2799 H  HG13 A ILE   A 1 131 ? 18.772 3.669   -4.603  0.64 17.87 ?  131 ILE   A HG13 1 
ATOM   2800 H  HG13 B ILE   A 1 131 ? 19.072 3.524   -4.557  0.36 18.72 ?  131 ILE   A HG13 1 
ATOM   2801 H  HG21 A ILE   A 1 131 ? 16.057 6.049   -4.315  0.64 16.30 ?  131 ILE   A HG21 1 
ATOM   2802 H  HG21 B ILE   A 1 131 ? 16.566 6.024   -3.890  0.36 18.28 ?  131 ILE   A HG21 1 
ATOM   2803 H  HG22 A ILE   A 1 131 ? 14.983 5.126   -5.034  0.64 16.30 ?  131 ILE   A HG22 1 
ATOM   2804 H  HG22 B ILE   A 1 131 ? 15.362 5.163   -4.465  0.36 18.28 ?  131 ILE   A HG22 1 
ATOM   2805 H  HG23 A ILE   A 1 131 ? 15.536 4.729   -3.599  0.64 16.30 ?  131 ILE   A HG23 1 
ATOM   2806 H  HG23 B ILE   A 1 131 ? 16.101 4.704   -3.137  0.36 18.28 ?  131 ILE   A HG23 1 
ATOM   2807 H  HD11 A ILE   A 1 131 ? 19.547 5.394   -3.322  0.64 19.23 ?  131 ILE   A HD11 1 
ATOM   2808 H  HD11 B ILE   A 1 131 ? 19.993 4.983   -3.066  0.36 19.44 ?  131 ILE   A HD11 1 
ATOM   2809 H  HD12 A ILE   A 1 131 ? 18.934 6.032   -4.642  0.64 19.23 ?  131 ILE   A HD12 1 
ATOM   2810 H  HD12 B ILE   A 1 131 ? 19.262 5.885   -4.151  0.36 19.44 ?  131 ILE   A HD12 1 
ATOM   2811 H  HD13 A ILE   A 1 131 ? 18.109 6.070   -3.284  0.64 19.23 ?  131 ILE   A HD13 1 
ATOM   2812 H  HD13 B ILE   A 1 131 ? 18.579 5.630   -2.740  0.36 19.44 ?  131 ILE   A HD13 1 
ATOM   2813 N  N    A PHE   A 1 132 ? 17.844 0.987   -5.879  0.64 12.21 ?  132 PHE   A N    1 
ATOM   2814 N  N    B PHE   A 1 132 ? 17.895 1.057   -5.888  0.36 14.45 ?  132 PHE   A N    1 
ATOM   2815 C  CA   A PHE   A 1 132 ? 18.709 0.144   -6.702  0.64 12.18 ?  132 PHE   A CA   1 
ATOM   2816 C  CA   B PHE   A 1 132 ? 18.841 0.297   -6.703  0.36 14.53 ?  132 PHE   A CA   1 
ATOM   2817 C  C    A PHE   A 1 132 ? 17.940 -0.611  -7.786  0.64 12.60 ?  132 PHE   A C    1 
ATOM   2818 C  C    B PHE   A 1 132 ? 18.195 -0.418  -7.893  0.36 15.21 ?  132 PHE   A C    1 
ATOM   2819 O  O    A PHE   A 1 132 ? 18.566 -1.256  -8.633  0.64 12.87 ?  132 PHE   A O    1 
ATOM   2820 O  O    B PHE   A 1 132 ? 18.917 -0.852  -8.798  0.36 15.69 ?  132 PHE   A O    1 
ATOM   2821 C  CB   A PHE   A 1 132 ? 19.521 -0.837  -5.845  0.64 12.09 ?  132 PHE   A CB   1 
ATOM   2822 C  CB   B PHE   A 1 132 ? 19.632 -0.693  -5.840  0.36 13.73 ?  132 PHE   A CB   1 
ATOM   2823 C  CG   A PHE   A 1 132 ? 20.747 -0.233  -5.183  0.64 11.98 ?  132 PHE   A CG   1 
ATOM   2824 C  CG   B PHE   A 1 132 ? 20.844 -0.088  -5.168  0.36 13.15 ?  132 PHE   A CG   1 
ATOM   2825 C  CD1  A PHE   A 1 132 ? 20.638 0.834   -4.306  0.64 12.74 ?  132 PHE   A CD1  1 
ATOM   2826 C  CD1  B PHE   A 1 132 ? 20.705 0.823   -4.131  0.36 13.66 ?  132 PHE   A CD1  1 
ATOM   2827 C  CD2  A PHE   A 1 132 ? 22.004 -0.788  -5.393  0.64 12.24 ?  132 PHE   A CD2  1 
ATOM   2828 C  CD2  B PHE   A 1 132 ? 22.124 -0.450  -5.562  0.36 13.13 ?  132 PHE   A CD2  1 
ATOM   2829 C  CE1  A PHE   A 1 132 ? 21.770 1.360   -3.684  0.64 12.96 ?  132 PHE   A CE1  1 
ATOM   2830 C  CE1  B PHE   A 1 132 ? 21.821 1.370   -3.511  0.36 13.76 ?  132 PHE   A CE1  1 
ATOM   2831 C  CE2  A PHE   A 1 132 ? 23.133 -0.272  -4.771  0.64 12.26 ?  132 PHE   A CE2  1 
ATOM   2832 C  CE2  B PHE   A 1 132 ? 23.242 0.092   -4.944  0.36 13.60 ?  132 PHE   A CE2  1 
ATOM   2833 C  CZ   A PHE   A 1 132 ? 23.011 0.805   -3.916  0.64 12.62 ?  132 PHE   A CZ   1 
ATOM   2834 C  CZ   B PHE   A 1 132 ? 23.087 1.003   -3.918  0.36 13.87 ?  132 PHE   A CZ   1 
ATOM   2835 H  H    A PHE   A 1 132 ? 17.630 0.640   -5.115  0.64 14.66 ?  132 PHE   A H    1 
ATOM   2836 H  H    B PHE   A 1 132 ? 17.670 0.675   -5.149  0.36 17.35 ?  132 PHE   A H    1 
ATOM   2837 H  HA   A PHE   A 1 132 ? 19.348 0.717   -7.145  0.64 14.63 ?  132 PHE   A HA   1 
ATOM   2838 H  HA   B PHE   A 1 132 ? 19.484 0.929   -7.056  0.36 17.45 ?  132 PHE   A HA   1 
ATOM   2839 H  HB2  A PHE   A 1 132 ? 18.950 -1.182  -5.138  0.64 14.52 ?  132 PHE   A HB2  1 
ATOM   2840 H  HB2  B PHE   A 1 132 ? 19.052 -1.039  -5.144  0.36 16.49 ?  132 PHE   A HB2  1 
ATOM   2841 H  HB3  A PHE   A 1 132 ? 19.822 -1.575  -6.405  0.64 14.52 ?  132 PHE   A HB3  1 
ATOM   2842 H  HB3  B PHE   A 1 132 ? 19.939 -1.420  -6.404  0.36 16.49 ?  132 PHE   A HB3  1 
ATOM   2843 H  HD1  A PHE   A 1 132 ? 19.808 1.209   -4.138  0.64 15.30 ?  132 PHE   A HD1  1 
ATOM   2844 H  HD1  B PHE   A 1 132 ? 19.856 1.075   -3.850  0.36 16.40 ?  132 PHE   A HD1  1 
ATOM   2845 H  HD2  A PHE   A 1 132 ? 22.097 -1.518  -5.968  0.64 14.70 ?  132 PHE   A HD2  1 
ATOM   2846 H  HD2  B PHE   A 1 132 ? 22.236 -1.063  -6.254  0.36 15.77 ?  132 PHE   A HD2  1 
ATOM   2847 H  HE1  A PHE   A 1 132 ? 21.687 2.083   -3.103  0.64 15.56 ?  132 PHE   A HE1  1 
ATOM   2848 H  HE1  B PHE   A 1 132 ? 21.717 1.983   -2.819  0.36 16.52 ?  132 PHE   A HE1  1 
ATOM   2849 H  HE2  A PHE   A 1 132 ? 23.971 -0.647  -4.935  0.64 14.72 ?  132 PHE   A HE2  1 
ATOM   2850 H  HE2  B PHE   A 1 132 ? 24.095 -0.156  -5.224  0.36 16.33 ?  132 PHE   A HE2  1 
ATOM   2851 H  HZ   A PHE   A 1 132 ? 23.765 1.160   -3.500  0.64 15.15 ?  132 PHE   A HZ   1 
ATOM   2852 H  HZ   B PHE   A 1 132 ? 23.837 1.370   -3.504  0.36 16.65 ?  132 PHE   A HZ   1 
ATOM   2853 N  N    A GLY   A 1 133 ? 16.608 -0.563  -7.770  0.64 12.94 ?  133 GLY   A N    1 
ATOM   2854 N  N    B GLY   A 1 133 ? 16.869 -0.575  -7.916  0.36 15.03 ?  133 GLY   A N    1 
ATOM   2855 C  CA   A GLY   A 1 133 ? 15.810 -0.928  -8.926  0.64 13.53 ?  133 GLY   A CA   1 
ATOM   2856 C  CA   B GLY   A 1 133 ? 16.147 -0.923  -9.126  0.36 14.94 ?  133 GLY   A CA   1 
ATOM   2857 C  C    A GLY   A 1 133 ? 15.524 -2.400  -9.138  0.64 14.24 ?  133 GLY   A C    1 
ATOM   2858 C  C    B GLY   A 1 133 ? 15.549 -2.315  -9.170  0.36 14.86 ?  133 GLY   A C    1 
ATOM   2859 O  O    A GLY   A 1 133 ? 14.955 -2.748  -10.179 0.64 15.15 ?  133 GLY   A O    1 
ATOM   2860 O  O    B GLY   A 1 133 ? 14.625 -2.545  -9.963  0.36 14.83 ?  133 GLY   A O    1 
ATOM   2861 H  H    A GLY   A 1 133 ? 16.142 -0.325  -7.089  0.64 15.53 ?  133 GLY   A H    1 
ATOM   2862 H  H    B GLY   A 1 133 ? 16.369 -0.497  -7.223  0.36 18.04 ?  133 GLY   A H    1 
ATOM   2863 H  HA2  A GLY   A 1 133 ? 14.953 -0.478  -8.864  0.64 16.24 ?  133 GLY   A HA2  1 
ATOM   2864 H  HA2  B GLY   A 1 133 ? 15.421 -0.304  -9.251  0.36 17.94 ?  133 GLY   A HA2  1 
ATOM   2865 H  HA3  A GLY   A 1 133 ? 16.254 -0.611  -9.724  0.64 16.24 ?  133 GLY   A HA3  1 
ATOM   2866 H  HA3  B GLY   A 1 133 ? 16.742 -0.834  -9.886  0.36 17.94 ?  133 GLY   A HA3  1 
ATOM   2867 N  N    A ALA   A 1 134 ? 15.890 -3.278  -8.208  0.64 13.85 ?  134 ALA   A N    1 
ATOM   2868 N  N    B ALA   A 1 134 ? 16.038 -3.250  -8.363  0.36 14.55 ?  134 ALA   A N    1 
ATOM   2869 C  CA   A ALA   A 1 134 ? 15.580 -4.689  -8.377  0.64 14.65 ?  134 ALA   A CA   1 
ATOM   2870 C  CA   B ALA   A 1 134 ? 15.600 -4.629  -8.511  0.36 14.70 ?  134 ALA   A CA   1 
ATOM   2871 C  C    A ALA   A 1 134 ? 14.207 -5.014  -7.789  0.64 14.78 ?  134 ALA   A C    1 
ATOM   2872 C  C    B ALA   A 1 134 ? 14.293 -4.882  -7.757  0.36 14.34 ?  134 ALA   A C    1 
ATOM   2873 O  O    A ALA   A 1 134 ? 13.614 -4.228  -7.047  0.64 15.78 ?  134 ALA   A O    1 
ATOM   2874 O  O    B ALA   A 1 134 ? 13.873 -4.101  -6.898  0.36 14.82 ?  134 ALA   A O    1 
ATOM   2875 C  CB   A ALA   A 1 134 ? 16.660 -5.568  -7.746  0.64 15.28 ?  134 ALA   A CB   1 
ATOM   2876 C  CB   B ALA   A 1 134 ? 16.688 -5.591  -8.037  0.36 15.24 ?  134 ALA   A CB   1 
ATOM   2877 H  H    A ALA   A 1 134 ? 16.317 -3.085  -7.482  0.64 16.63 ?  134 ALA   A H    1 
ATOM   2878 H  H    B ALA   A 1 134 ? 16.614 -3.113  -7.738  0.36 17.47 ?  134 ALA   A H    1 
ATOM   2879 H  HA   A ALA   A 1 134 ? 15.553 -4.893  -9.325  0.64 17.59 ?  134 ALA   A HA   1 
ATOM   2880 H  HA   B ALA   A 1 134 ? 15.444 -4.802  -9.452  0.36 17.65 ?  134 ALA   A HA   1 
ATOM   2881 H  HB1  A ALA   A 1 134 ? 16.439 -6.500  -7.901  0.64 18.34 ?  134 ALA   A HB1  1 
ATOM   2882 H  HB1  B ALA   A 1 134 ? 16.376 -6.500  -8.154  0.36 18.29 ?  134 ALA   A HB1  1 
ATOM   2883 H  HB2  A ALA   A 1 134 ? 17.516 -5.360  -8.158  0.64 18.34 ?  134 ALA   A HB2  1 
ATOM   2884 H  HB2  B ALA   A 1 134 ? 17.489 -5.444  -8.568  0.36 18.29 ?  134 ALA   A HB2  1 
ATOM   2885 H  HB3  A ALA   A 1 134 ? 16.700 -5.389  -6.796  0.64 18.34 ?  134 ALA   A HB3  1 
ATOM   2886 H  HB3  B ALA   A 1 134 ? 16.876 -5.419  -7.103  0.36 18.29 ?  134 ALA   A HB3  1 
ATOM   2887 N  N    A ASP   A 1 135 ? 13.704 -6.194  -8.144  0.64 15.32 ?  135 ASP   A N    1 
ATOM   2888 N  N    B ASP   A 1 135 ? 13.653 -6.000  -8.097  0.36 14.72 ?  135 ASP   A N    1 
ATOM   2889 C  CA   A ASP   A 1 135 ? 12.451 -6.695  -7.593  0.64 16.16 ?  135 ASP   A CA   1 
ATOM   2890 C  CA   B ASP   A 1 135 ? 12.384 -6.385  -7.485  0.36 15.23 ?  135 ASP   A CA   1 
ATOM   2891 C  C    A ASP   A 1 135 ? 12.681 -7.127  -6.151  0.64 15.42 ?  135 ASP   A C    1 
ATOM   2892 C  C    B ASP   A 1 135 ? 12.633 -6.867  -6.062  0.36 14.68 ?  135 ASP   A C    1 
ATOM   2893 O  O    A ASP   A 1 135 ? 13.489 -8.032  -5.910  0.64 15.33 ?  135 ASP   A O    1 
ATOM   2894 O  O    B ASP   A 1 135 ? 13.361 -7.850  -5.870  0.36 14.33 ?  135 ASP   A O    1 
ATOM   2895 C  CB   A ASP   A 1 135 ? 11.989 -7.886  -8.428  0.64 18.09 ?  135 ASP   A CB   1 
ATOM   2896 C  CB   B ASP   A 1 135 ? 11.746 -7.498  -8.312  0.36 16.35 ?  135 ASP   A CB   1 
ATOM   2897 C  CG   A ASP   A 1 135 ? 10.730 -8.552  -7.885  0.64 19.73 ?  135 ASP   A CG   1 
ATOM   2898 C  CG   B ASP   A 1 135 ? 10.344 -7.862  -7.836  0.36 17.71 ?  135 ASP   A CG   1 
ATOM   2899 O  OD1  A ASP   A 1 135 ? 10.141 -8.057  -6.902  0.64 19.45 ?  135 ASP   A OD1  1 
ATOM   2900 O  OD1  B ASP   A 1 135 ? 9.942  -7.421  -6.738  0.36 18.26 ?  135 ASP   A OD1  1 
ATOM   2901 O  OD2  A ASP   A 1 135 ? 10.334 -9.588  -8.457  0.64 21.97 -1 135 ASP   A OD2  1 
ATOM   2902 O  OD2  B ASP   A 1 135 ? 9.643  -8.597  -8.566  0.36 18.74 -1 135 ASP   A OD2  1 
ATOM   2903 H  H    A ASP   A 1 135 ? 14.076 -6.729  -8.709  0.64 18.40 ?  135 ASP   A H    1 
ATOM   2904 H  H    B ASP   A 1 135 ? 13.933 -6.558  -8.687  0.36 17.68 ?  135 ASP   A H    1 
ATOM   2905 H  HA   A ASP   A 1 135 ? 11.779 -6.000  -7.632  0.64 19.40 ?  135 ASP   A HA   1 
ATOM   2906 H  HA   B ASP   A 1 135 ? 11.783 -5.624  -7.482  0.36 18.28 ?  135 ASP   A HA   1 
ATOM   2907 H  HB2  A ASP   A 1 135 ? 11.811 -7.585  -9.332  0.64 21.72 ?  135 ASP   A HB2  1 
ATOM   2908 H  HB2  B ASP   A 1 135 ? 11.699 -7.211  -9.238  0.36 19.63 ?  135 ASP   A HB2  1 
ATOM   2909 H  HB3  A ASP   A 1 135 ? 12.682 -8.559  -8.429  0.64 21.72 ?  135 ASP   A HB3  1 
ATOM   2910 H  HB3  B ASP   A 1 135 ? 12.292 -8.295  -8.239  0.36 19.63 ?  135 ASP   A HB3  1 
ATOM   2911 N  N    A PRO   A 1 136 ? 12.016 -6.515  -5.169  0.64 15.15 ?  136 PRO   A N    1 
ATOM   2912 N  N    B PRO   A 1 136 ? 12.067 -6.216  -5.043  0.36 14.40 ?  136 PRO   A N    1 
ATOM   2913 C  CA   A PRO   A 1 136 ? 12.255 -6.916  -3.772  0.64 15.07 ?  136 PRO   A CA   1 
ATOM   2914 C  CA   B PRO   A 1 136 ? 12.318 -6.655  -3.659  0.36 14.34 ?  136 PRO   A CA   1 
ATOM   2915 C  C    A PRO   A 1 136 ? 11.849 -8.346  -3.462  0.64 14.22 ?  136 PRO   A C    1 
ATOM   2916 C  C    B PRO   A 1 136 ? 11.851 -8.070  -3.359  0.36 13.88 ?  136 PRO   A C    1 
ATOM   2917 O  O    A PRO   A 1 136 ? 12.475 -8.977  -2.605  0.64 13.78 ?  136 PRO   A O    1 
ATOM   2918 O  O    B PRO   A 1 136 ? 12.394 -8.709  -2.449  0.36 13.03 ?  136 PRO   A O    1 
ATOM   2919 C  CB   A PRO   A 1 136 ? 11.444 -5.890  -2.967  0.64 15.90 ?  136 PRO   A CB   1 
ATOM   2920 C  CB   B PRO   A 1 136 ? 11.582 -5.602  -2.818  0.36 14.64 ?  136 PRO   A CB   1 
ATOM   2921 C  CG   A PRO   A 1 136 ? 10.398 -5.398  -3.922  0.64 16.59 ?  136 PRO   A CG   1 
ATOM   2922 C  CG   B PRO   A 1 136 ? 10.606 -4.971  -3.762  0.36 15.28 ?  136 PRO   A CG   1 
ATOM   2923 C  CD   A PRO   A 1 136 ? 11.036 -5.421  -5.276  0.64 16.01 ?  136 PRO   A CD   1 
ATOM   2924 C  CD   B PRO   A 1 136 ? 11.249 -4.995  -5.096  0.36 14.84 ?  136 PRO   A CD   1 
ATOM   2925 H  HA   A PRO   A 1 136 ? 13.197 -6.811  -3.553  0.64 18.09 ?  136 PRO   A HA   1 
ATOM   2926 H  HA   B PRO   A 1 136 ? 13.265 -6.599  -3.462  0.36 17.21 ?  136 PRO   A HA   1 
ATOM   2927 H  HB2  A PRO   A 1 136 ? 11.037 -6.328  -2.202  0.64 19.09 ?  136 PRO   A HB2  1 
ATOM   2928 H  HB2  B PRO   A 1 136 ? 11.118 -6.028  -2.081  0.36 17.58 ?  136 PRO   A HB2  1 
ATOM   2929 H  HB3  A PRO   A 1 136 ? 12.026 -5.169  -2.682  0.64 19.09 ?  136 PRO   A HB3  1 
ATOM   2930 H  HB3  B PRO   A 1 136 ? 12.215 -4.942  -2.489  0.36 17.58 ?  136 PRO   A HB3  1 
ATOM   2931 H  HG2  A PRO   A 1 136 ? 9.633  -5.988  -3.896  0.64 19.92 ?  136 PRO   A HG2  1 
ATOM   2932 H  HG2  B PRO   A 1 136 ? 9.792  -5.494  -3.785  0.36 18.34 ?  136 PRO   A HG2  1 
ATOM   2933 H  HG3  A PRO   A 1 136 ? 10.148 -4.493  -3.683  0.64 19.92 ?  136 PRO   A HG3  1 
ATOM   2934 H  HG3  B PRO   A 1 136 ? 10.427 -4.061  -3.492  0.36 18.34 ?  136 PRO   A HG3  1 
ATOM   2935 H  HD2  A PRO   A 1 136 ? 10.377 -5.633  -5.957  0.64 19.23 ?  136 PRO   A HD2  1 
ATOM   2936 H  HD2  B PRO   A 1 136 ? 10.575 -5.066  -5.792  0.36 17.81 ?  136 PRO   A HD2  1 
ATOM   2937 H  HD3  A PRO   A 1 136 ? 11.484 -4.581  -5.464  0.64 19.23 ?  136 PRO   A HD3  1 
ATOM   2938 H  HD3  B PRO   A 1 136 ? 11.814 -4.217  -5.222  0.36 17.81 ?  136 PRO   A HD3  1 
ATOM   2939 N  N    A ILE   A 1 137 ? 10.803 -8.869  -4.106  0.64 14.29 ?  137 ILE   A N    1 
ATOM   2940 N  N    B ILE   A 1 137 ? 10.850 -8.578  -4.079  0.36 14.21 ?  137 ILE   A N    1 
ATOM   2941 C  CA   A ILE   A 1 137 ? 10.446 -10.273 -3.915  0.64 14.43 ?  137 ILE   A CA   1 
ATOM   2942 C  CA   B ILE   A 1 137 ? 10.432 -9.966  -3.888  0.36 14.51 ?  137 ILE   A CA   1 
ATOM   2943 C  C    A ILE   A 1 137 ? 11.614 -11.164 -4.310  0.64 13.86 ?  137 ILE   A C    1 
ATOM   2944 C  C    B ILE   A 1 137 ? 11.578 -10.908 -4.239  0.36 14.38 ?  137 ILE   A C    1 
ATOM   2945 O  O    A ILE   A 1 137 ? 11.938 -12.141 -3.621  0.64 13.81 ?  137 ILE   A O    1 
ATOM   2946 O  O    B ILE   A 1 137 ? 11.870 -11.865 -3.512  0.36 14.44 ?  137 ILE   A O    1 
ATOM   2947 C  CB   A ILE   A 1 137 ? 9.164  -10.612 -4.699  0.64 15.48 ?  137 ILE   A CB   1 
ATOM   2948 C  CB   B ILE   A 1 137 ? 9.174  -10.269 -4.724  0.36 15.31 ?  137 ILE   A CB   1 
ATOM   2949 C  CG1  A ILE   A 1 137 ? 7.974  -9.805  -4.158  0.64 16.83 ?  137 ILE   A CG1  1 
ATOM   2950 C  CG1  B ILE   A 1 137 ? 8.064  -9.251  -4.439  0.36 16.10 ?  137 ILE   A CG1  1 
ATOM   2951 C  CG2  A ILE   A 1 137 ? 8.884  -12.114 -4.643  0.64 15.88 ?  137 ILE   A CG2  1 
ATOM   2952 C  CG2  B ILE   A 1 137 ? 8.691  -11.692 -4.461  0.36 15.64 ?  137 ILE   A CG2  1 
ATOM   2953 C  CD1  A ILE   A 1 137 ? 6.697  -9.964  -4.962  0.64 17.90 ?  137 ILE   A CD1  1 
ATOM   2954 C  CD1  B ILE   A 1 137 ? 6.849  -9.423  -5.323  0.36 16.73 ?  137 ILE   A CD1  1 
ATOM   2955 H  H    A ILE   A 1 137 ? 10.291 -8.441  -4.645  0.64 17.16 ?  137 ILE   A H    1 
ATOM   2956 H  H    B ILE   A 1 137 ? 10.404 -8.143  -4.673  0.36 17.06 ?  137 ILE   A H    1 
ATOM   2957 H  HA   A ILE   A 1 137 ? 10.271 -10.434 -2.980  0.64 17.32 ?  137 ILE   A HA   1 
ATOM   2958 H  HA   B ILE   A 1 137 ? 10.206 -10.103 -2.955  0.36 17.42 ?  137 ILE   A HA   1 
ATOM   2959 H  HB   A ILE   A 1 137 ? 9.296  -10.368 -5.627  0.64 18.58 ?  137 ILE   A HB   1 
ATOM   2960 H  HB   B ILE   A 1 137 ? 9.407  -10.198 -5.660  0.36 18.38 ?  137 ILE   A HB   1 
ATOM   2961 H  HG12 A ILE   A 1 137 ? 7.792  -10.090 -3.250  0.64 20.21 ?  137 ILE   A HG12 1 
ATOM   2962 H  HG12 B ILE   A 1 137 ? 7.777  -9.343  -3.518  0.36 19.33 ?  137 ILE   A HG12 1 
ATOM   2963 H  HG13 A ILE   A 1 137 ? 8.213  -8.863  -4.164  0.64 20.21 ?  137 ILE   A HG13 1 
ATOM   2964 H  HG13 B ILE   A 1 137 ? 8.402  -8.353  -4.589  0.36 19.33 ?  137 ILE   A HG13 1 
ATOM   2965 H  HG21 A ILE   A 1 137 ? 7.974  -12.292 -4.934  0.64 19.06 ?  137 ILE   A HG21 1 
ATOM   2966 H  HG21 B ILE   A 1 137 ? 7.872  -11.849 -4.955  0.36 18.78 ?  137 ILE   A HG21 1 
ATOM   2967 H  HG22 A ILE   A 1 137 ? 9.504  -12.572 -5.230  0.64 19.06 ?  137 ILE   A HG22 1 
ATOM   2968 H  HG22 B ILE   A 1 137 ? 9.373  -12.315 -4.754  0.36 18.78 ?  137 ILE   A HG22 1 
ATOM   2969 H  HG23 A ILE   A 1 137 ? 8.999  -12.421 -3.732  0.64 19.06 ?  137 ILE   A HG23 1 
ATOM   2970 H  HG23 B ILE   A 1 137 ? 8.530  -11.799 -3.511  0.36 18.78 ?  137 ILE   A HG23 1 
ATOM   2971 H  HD11 A ILE   A 1 137 ? 5.979  -10.222 -4.365  0.64 21.49 ?  137 ILE   A HD11 1 
ATOM   2972 H  HD11 B ILE   A 1 137 ? 6.413  -8.565  -5.431  0.36 20.09 ?  137 ILE   A HD11 1 
ATOM   2973 H  HD12 A ILE   A 1 137 ? 6.494  -9.116  -5.383  0.64 21.49 ?  137 ILE   A HD12 1 
ATOM   2974 H  HD12 B ILE   A 1 137 ? 7.135  -9.760  -6.187  0.36 20.09 ?  137 ILE   A HD12 1 
ATOM   2975 H  HD13 A ILE   A 1 137 ? 6.825  -10.641 -5.643  0.64 21.49 ?  137 ILE   A HD13 1 
ATOM   2976 H  HD13 B ILE   A 1 137 ? 6.243  -10.057 -4.906  0.36 20.09 ?  137 ILE   A HD13 1 
ATOM   2977 N  N    A HIS   A 1 138 ? 12.268 -10.833 -5.426  0.64 14.26 ?  138 HIS   A N    1 
ATOM   2978 N  N    B HIS   A 1 138 ? 12.241 -10.646 -5.368  0.36 14.72 ?  138 HIS   A N    1 
ATOM   2979 C  CA   A HIS   A 1 138 ? 13.469 -11.554 -5.826  0.64 14.46 ?  138 HIS   A CA   1 
ATOM   2980 C  CA   B HIS   A 1 138 ? 13.370 -11.470 -5.791  0.36 14.57 ?  138 HIS   A CA   1 
ATOM   2981 C  C    A HIS   A 1 138 ? 14.591 -11.379 -4.807  0.64 13.87 ?  138 HIS   A C    1 
ATOM   2982 C  C    B HIS   A 1 138 ? 14.535 -11.362 -4.812  0.36 14.07 ?  138 HIS   A C    1 
ATOM   2983 O  O    A HIS   A 1 138 ? 15.262 -12.354 -4.440  0.64 14.05 ?  138 HIS   A O    1 
ATOM   2984 O  O    B HIS   A 1 138 ? 15.183 -12.366 -4.488  0.36 14.25 ?  138 HIS   A O    1 
ATOM   2985 C  CB   A HIS   A 1 138 ? 13.908 -11.102 -7.217  0.64 15.52 ?  138 HIS   A CB   1 
ATOM   2986 C  CB   B HIS   A 1 138 ? 13.793 -11.051 -7.200  0.36 14.93 ?  138 HIS   A CB   1 
ATOM   2987 C  CG   A HIS   A 1 138 ? 15.162 -11.767 -7.688  0.64 16.72 ?  138 HIS   A CG   1 
ATOM   2988 C  CG   B HIS   A 1 138 ? 15.081 -11.662 -7.652  0.36 15.55 ?  138 HIS   A CG   1 
ATOM   2989 N  ND1  A HIS   A 1 138 ? 15.252 -13.128 -7.893  0.64 17.83 ?  138 HIS   A ND1  1 
ATOM   2990 N  ND1  B HIS   A 1 138 ? 15.203 -12.999 -7.964  0.36 16.30 ?  138 HIS   A ND1  1 
ATOM   2991 C  CD2  A HIS   A 1 138 ? 16.385 -11.262 -7.971  0.64 17.12 ?  138 HIS   A CD2  1 
ATOM   2992 C  CD2  B HIS   A 1 138 ? 16.305 -11.117 -7.845  0.36 15.68 ?  138 HIS   A CD2  1 
ATOM   2993 C  CE1  A HIS   A 1 138 ? 16.474 -13.429 -8.296  0.64 18.47 ?  138 HIS   A CE1  1 
ATOM   2994 C  CE1  B HIS   A 1 138 ? 16.448 -13.251 -8.331  0.36 16.60 ?  138 HIS   A CE1  1 
ATOM   2995 N  NE2  A HIS   A 1 138 ? 17.181 -12.315 -8.350  0.64 17.71 ?  138 HIS   A NE2  1 
ATOM   2996 N  NE2  B HIS   A 1 138 ? 17.137 -12.125 -8.267  0.36 16.12 ?  138 HIS   A NE2  1 
ATOM   2997 H  H    A HIS   A 1 138 ? 12.033 -10.198 -5.969  0.64 17.12 ?  138 HIS   A H    1 
ATOM   2998 H  H    B HIS   A 1 138 ? 12.052 -10.000 -5.907  0.36 17.67 ?  138 HIS   A H    1 
ATOM   2999 H  HA   A HIS   A 1 138 ? 13.258 -12.494 -5.883  0.64 17.36 ?  138 HIS   A HA   1 
ATOM   3000 H  HA   B HIS   A 1 138 ? 13.089 -12.394 -5.826  0.36 17.49 ?  138 HIS   A HA   1 
ATOM   3001 H  HB2  A HIS   A 1 138 ? 13.203 -11.312 -7.857  0.64 18.63 ?  138 HIS   A HB2  1 
ATOM   3002 H  HB2  B HIS   A 1 138 ? 13.101 -11.320 -7.829  0.36 17.93 ?  138 HIS   A HB2  1 
ATOM   3003 H  HB3  A HIS   A 1 138 ? 14.064 -10.145 -7.210  0.64 18.63 ?  138 HIS   A HB3  1 
ATOM   3004 H  HB3  B HIS   A 1 138 ? 13.898 -10.087 -7.226  0.36 17.93 ?  138 HIS   A HB3  1 
ATOM   3005 H  HD1  A HIS   A 1 138 ? 14.610 -13.692 -7.787  0.64 21.40 ?  138 HIS   A HD1  1 
ATOM   3006 H  HD1  B HIS   A 1 138 ? 14.569 -13.579 -7.929  0.36 19.57 ?  138 HIS   A HD1  1 
ATOM   3007 H  HD2  A HIS   A 1 138 ? 16.634 -10.368 -7.923  0.64 20.56 ?  138 HIS   A HD2  1 
ATOM   3008 H  HD2  B HIS   A 1 138 ? 16.538 -10.227 -7.717  0.36 18.83 ?  138 HIS   A HD2  1 
ATOM   3009 H  HE1  A HIS   A 1 138 ? 16.784 -14.280 -8.502  0.64 22.17 ?  138 HIS   A HE1  1 
ATOM   3010 H  HE1  B HIS   A 1 138 ? 16.781 -14.081 -8.589  0.36 19.93 ?  138 HIS   A HE1  1 
ATOM   3011 N  N    . SER   A 1 139 ? 14.814 -10.150 -4.333  1.00 13.49 ?  139 SER   A N    1 
ATOM   3012 C  CA   . SER   A 1 139 ? 15.882 -9.952  -3.364  1.00 13.28 ?  139 SER   A CA   1 
ATOM   3013 C  C    . SER   A 1 139 ? 15.659 -10.793 -2.113  1.00 12.72 ?  139 SER   A C    1 
ATOM   3014 O  O    . SER   A 1 139 ? 16.605 -11.386 -1.583  1.00 12.91 ?  139 SER   A O    1 
ATOM   3015 C  CB   . SER   A 1 139 ? 16.007 -8.471  -3.011  1.00 13.13 ?  139 SER   A CB   1 
ATOM   3016 O  OG   . SER   A 1 139 ? 17.082 -8.290  -2.109  1.00 13.56 ?  139 SER   A OG   1 
ATOM   3017 H  H    A SER   A 1 139 ? 14.376 -9.440  -4.549  0.64 16.19 ?  139 SER   A H    1 
ATOM   3018 H  H    B SER   A 1 139 ? 14.395 -9.430  -4.551  0.36 16.19 ?  139 SER   A H    1 
ATOM   3019 H  HA   . SER   A 1 139 ? 16.721 -10.227 -3.760  1.00 15.94 ?  139 SER   A HA   1 
ATOM   3020 H  HB2  . SER   A 1 139 ? 16.178 -7.955  -3.816  1.00 15.76 ?  139 SER   A HB2  1 
ATOM   3021 H  HB3  . SER   A 1 139 ? 15.184 -8.165  -2.590  1.00 15.76 ?  139 SER   A HB3  1 
ATOM   3022 H  HG   . SER   A 1 139 ? 17.810 -8.485  -2.477  1.00 16.28 ?  139 SER   A HG   1 
ATOM   3023 N  N    . LEU   A 1 140 ? 14.417 -10.856 -1.626  1.00 12.57 ?  140 LEU   A N    1 
ATOM   3024 C  CA   . LEU   A 1 140 ? 14.137 -11.668 -0.447  1.00 12.39 ?  140 LEU   A CA   1 
ATOM   3025 C  C    . LEU   A 1 140 ? 14.411 -13.141 -0.721  1.00 12.89 ?  140 LEU   A C    1 
ATOM   3026 O  O    . LEU   A 1 140 ? 14.963 -13.850 0.131   1.00 13.39 ?  140 LEU   A O    1 
ATOM   3027 C  CB   . LEU   A 1 140 ? 12.692 -11.451 -0.008  1.00 12.91 ?  140 LEU   A CB   1 
ATOM   3028 C  CG   . LEU   A 1 140 ? 12.227 -12.292 1.179   1.00 13.68 ?  140 LEU   A CG   1 
ATOM   3029 C  CD1  . LEU   A 1 140 ? 13.125 -12.104 2.397   1.00 14.31 ?  140 LEU   A CD1  1 
ATOM   3030 C  CD2  . LEU   A 1 140 ? 10.771 -11.959 1.516   1.00 14.30 ?  140 LEU   A CD2  1 
ATOM   3031 H  H    . LEU   A 1 140 ? 13.739 -10.440 -1.953  1.00 15.10 ?  140 LEU   A H    1 
ATOM   3032 H  HA   . LEU   A 1 140 ? 14.715 -11.388 0.275   1.00 14.88 ?  140 LEU   A HA   1 
ATOM   3033 H  HB2  . LEU   A 1 140 ? 12.579 -10.525 0.234   1.00 15.50 ?  140 LEU   A HB2  1 
ATOM   3034 H  HB3  . LEU   A 1 140 ? 12.110 -11.667 -0.757  1.00 15.50 ?  140 LEU   A HB3  1 
ATOM   3035 H  HG   . LEU   A 1 140 ? 12.251 -13.231 0.930   1.00 16.42 ?  140 LEU   A HG   1 
ATOM   3036 H  HD11 . LEU   A 1 140 ? 12.736 -12.575 3.151   1.00 17.18 ?  140 LEU   A HD11 1 
ATOM   3037 H  HD12 . LEU   A 1 140 ? 14.002 -12.476 2.196   1.00 17.18 ?  140 LEU   A HD12 1 
ATOM   3038 H  HD13 . LEU   A 1 140 ? 13.200 -11.162 2.592   1.00 17.18 ?  140 LEU   A HD13 1 
ATOM   3039 H  HD21 . LEU   A 1 140 ? 10.481 -12.517 2.260   1.00 17.17 ?  140 LEU   A HD21 1 
ATOM   3040 H  HD22 . LEU   A 1 140 ? 10.706 -11.025 1.764   1.00 17.17 ?  140 LEU   A HD22 1 
ATOM   3041 H  HD23 . LEU   A 1 140 ? 10.212 -12.136 0.741   1.00 17.17 ?  140 LEU   A HD23 1 
ATOM   3042 N  N    . ARG   A 1 141 ? 14.023 -13.621 -1.905  1.00 13.38 ?  141 ARG   A N    1 
ATOM   3043 C  CA   . ARG   A 1 141 ? 14.269 -15.015 -2.259  1.00 14.30 ?  141 ARG   A CA   1 
ATOM   3044 C  C    . ARG   A 1 141 ? 15.765 -15.318 -2.277  1.00 13.66 ?  141 ARG   A C    1 
ATOM   3045 O  O    . ARG   A 1 141 ? 16.217 -16.332 -1.729  1.00 14.06 ?  141 ARG   A O    1 
ATOM   3046 C  CB   . ARG   A 1 141 ? 13.642 -15.298 -3.624  1.00 16.06 ?  141 ARG   A CB   1 
ATOM   3047 C  CG   . ARG   A 1 141 ? 13.640 -16.754 -4.037  1.00 18.82 ?  141 ARG   A CG   1 
ATOM   3048 C  CD   . ARG   A 1 141 ? 12.601 -17.510 -3.269  1.00 21.43 ?  141 ARG   A CD   1 
ATOM   3049 N  NE   . ARG   A 1 141 ? 13.208 -18.313 -2.222  1.00 22.81 ?  141 ARG   A NE   1 
ATOM   3050 C  CZ   . ARG   A 1 141 ? 12.530 -18.882 -1.234  1.00 23.72 ?  141 ARG   A CZ   1 
ATOM   3051 N  NH1  . ARG   A 1 141 ? 11.243 -18.636 -1.046  1.00 23.00 ?  141 ARG   A NH1  1 
ATOM   3052 N  NH2  . ARG   A 1 141 ? 13.160 -19.713 -0.409  1.00 25.09 ?  141 ARG   A NH2  1 
ATOM   3053 H  H    . ARG   A 1 141 ? 13.623 -13.164 -2.516  1.00 16.07 ?  141 ARG   A H    1 
ATOM   3054 H  HA   . ARG   A 1 141 ? 13.850 -15.592 -1.607  1.00 17.17 ?  141 ARG   A HA   1 
ATOM   3055 H  HB2  . ARG   A 1 141 ? 12.721 -14.991 -3.615  1.00 19.28 ?  141 ARG   A HB2  1 
ATOM   3056 H  HB3  . ARG   A 1 141 ? 14.137 -14.807 -4.299  1.00 19.28 ?  141 ARG   A HB3  1 
ATOM   3057 H  HG2  . ARG   A 1 141 ? 13.439 -16.825 -4.985  1.00 22.60 ?  141 ARG   A HG2  1 
ATOM   3058 H  HG3  . ARG   A 1 141 ? 14.509 -17.150 -3.850  1.00 22.60 ?  141 ARG   A HG3  1 
ATOM   3059 H  HD2  . ARG   A 1 141 ? 11.989 -16.887 -2.844  1.00 25.73 ?  141 ARG   A HD2  1 
ATOM   3060 H  HD3  . ARG   A 1 141 ? 12.108 -18.092 -3.877  1.00 25.73 ?  141 ARG   A HD3  1 
ATOM   3061 H  HE   . ARG   A 1 141 ? 14.029 -18.542 -2.319  1.00 27.38 ?  141 ARG   A HE   1 
ATOM   3062 H  HH11 . ARG   A 1 141 ? 10.816 -18.116 -1.580  1.00 27.60 ?  141 ARG   A HH11 1 
ATOM   3063 H  HH12 . ARG   A 1 141 ? 10.821 -19.013 -0.393  1.00 27.60 ?  141 ARG   A HH12 1 
ATOM   3064 H  HH21 . ARG   A 1 141 ? 13.993 -19.884 -0.525  1.00 30.12 ?  141 ARG   A HH21 1 
ATOM   3065 H  HH22 . ARG   A 1 141 ? 12.733 -20.080 0.244   1.00 30.12 ?  141 ARG   A HH22 1 
ATOM   3066 N  N    . VAL   A 1 142 ? 16.554 -14.452 -2.915  1.00 13.02 ?  142 VAL   A N    1 
ATOM   3067 C  CA   . VAL   A 1 142 ? 17.997 -14.665 -2.944  1.00 13.04 ?  142 VAL   A CA   1 
ATOM   3068 C  C    . VAL   A 1 142 ? 18.565 -14.640 -1.534  1.00 12.71 ?  142 VAL   A C    1 
ATOM   3069 O  O    . VAL   A 1 142 ? 19.424 -15.458 -1.182  1.00 13.03 ?  142 VAL   A O    1 
ATOM   3070 C  CB   . VAL   A 1 142 ? 18.693 -13.649 -3.868  1.00 13.23 ?  142 VAL   A CB   1 
ATOM   3071 C  CG1  . VAL   A 1 142 ? 20.205 -13.858 -3.834  1.00 13.21 ?  142 VAL   A CG1  1 
ATOM   3072 C  CG2  . VAL   A 1 142 ? 18.198 -13.787 -5.293  1.00 14.70 ?  142 VAL   A CG2  1 
ATOM   3073 H  H    . VAL   A 1 142 ? 16.286 -13.738 -3.325  1.00 15.63 ?  142 VAL   A H    1 
ATOM   3074 H  HA   . VAL   A 1 142 ? 18.169 -15.539 -3.310  1.00 15.65 ?  142 VAL   A HA   1 
ATOM   3075 H  HB   . VAL   A 1 142 ? 18.512 -12.742 -3.567  1.00 15.89 ?  142 VAL   A HB   1 
ATOM   3076 H  HG11 . VAL   A 1 142 ? 20.611 -13.374 -4.570  1.00 15.86 ?  142 VAL   A HG11 1 
ATOM   3077 H  HG12 . VAL   A 1 142 ? 20.556 -13.528 -2.991  1.00 15.86 ?  142 VAL   A HG12 1 
ATOM   3078 H  HG13 . VAL   A 1 142 ? 20.392 -14.807 -3.921  1.00 15.86 ?  142 VAL   A HG13 1 
ATOM   3079 H  HG21 . VAL   A 1 142 ? 18.671 -13.149 -5.854  1.00 17.65 ?  142 VAL   A HG21 1 
ATOM   3080 H  HG22 . VAL   A 1 142 ? 18.382 -14.690 -5.597  1.00 17.65 ?  142 VAL   A HG22 1 
ATOM   3081 H  HG23 . VAL   A 1 142 ? 17.251 -13.611 -5.312  1.00 17.65 ?  142 VAL   A HG23 1 
ATOM   3082 N  N    . CYS   A 1 143 ? 18.090 -13.716 -0.699  1.00 12.71 ?  143 CYS   A N    1 
ATOM   3083 C  CA   . CYS   A 1 143 ? 18.552 -13.658 0.683   1.00 12.95 ?  143 CYS   A CA   1 
ATOM   3084 C  C    . CYS   A 1 143 ? 18.324 -14.993 1.383   1.00 13.17 ?  143 CYS   A C    1 
ATOM   3085 O  O    . CYS   A 1 143 ? 19.241 -15.578 1.968   1.00 12.87 ?  143 CYS   A O    1 
ATOM   3086 C  CB   . CYS   A 1 143 ? 17.819 -12.538 1.418   1.00 13.09 ?  143 CYS   A CB   1 
ATOM   3087 S  SG   . CYS   A 1 143 ? 18.317 -12.358 3.143   1.00 13.55 ?  143 CYS   A SG   1 
ATOM   3088 H  H    . CYS   A 1 143 ? 17.509 -13.119 -0.907  1.00 15.27 ?  143 CYS   A H    1 
ATOM   3089 H  HA   . CYS   A 1 143 ? 19.500 -13.469 0.699   1.00 15.55 ?  143 CYS   A HA   1 
ATOM   3090 H  HB2  . CYS   A 1 143 ? 17.992 -11.699 0.966   1.00 15.72 ?  143 CYS   A HB2  1 
ATOM   3091 H  HB3  . CYS   A 1 143 ? 16.868 -12.726 1.404   1.00 15.72 ?  143 CYS   A HB3  1 
ATOM   3092 H  HG   . CYS   A 1 143 ? 17.731 -11.433 3.621   1.00 16.27 ?  143 CYS   A HG   1 
ATOM   3093 N  N    . VAL   A 1 144 ? 17.095 -15.498 1.321   1.00 13.65 ?  144 VAL   A N    1 
ATOM   3094 C  CA   . VAL   A 1 144 ? 16.752 -16.733 2.018   1.00 14.92 ?  144 VAL   A CA   1 
ATOM   3095 C  C    . VAL   A 1 144 ? 17.572 -17.903 1.495   1.00 14.46 ?  144 VAL   A C    1 
ATOM   3096 O  O    . VAL   A 1 144 ? 17.939 -18.810 2.254   1.00 15.19 ?  144 VAL   A O    1 
ATOM   3097 C  CB   . VAL   A 1 144 ? 15.236 -16.975 1.889   1.00 17.90 ?  144 VAL   A CB   1 
ATOM   3098 C  CG1  . VAL   A 1 144 ? 14.870 -18.410 2.218   1.00 19.71 ?  144 VAL   A CG1  1 
ATOM   3099 C  CG2  . VAL   A 1 144 ? 14.483 -15.972 2.769   1.00 17.67 ?  144 VAL   A CG2  1 
ATOM   3100 H  H    . VAL   A 1 144 ? 16.440 -15.145 0.880   1.00 16.38 ?  144 VAL   A H    1 
ATOM   3101 H  HA   . VAL   A 1 144 ? 16.950 -16.628 2.955   1.00 17.91 ?  144 VAL   A HA   1 
ATOM   3102 H  HB   . VAL   A 1 144 ? 14.966 -16.807 0.968   1.00 21.49 ?  144 VAL   A HB   1 
ATOM   3103 H  HG11 . VAL   A 1 144 ? 13.916 -18.460 2.397   1.00 23.66 ?  144 VAL   A HG11 1 
ATOM   3104 H  HG12 . VAL   A 1 144 ? 15.091 -18.975 1.461   1.00 23.66 ?  144 VAL   A HG12 1 
ATOM   3105 H  HG13 . VAL   A 1 144 ? 15.367 -18.687 3.001   1.00 23.66 ?  144 VAL   A HG13 1 
ATOM   3106 H  HG21 . VAL   A 1 144 ? 13.523 -16.117 2.674   1.00 21.21 ?  144 VAL   A HG21 1 
ATOM   3107 H  HG22 . VAL   A 1 144 ? 14.740 -16.100 3.694   1.00 21.21 ?  144 VAL   A HG22 1 
ATOM   3108 H  HG23 . VAL   A 1 144 ? 14.700 -15.068 2.487   1.00 21.21 ?  144 VAL   A HG23 1 
ATOM   3109 N  N    . ASP   A 1 145 ? 17.842 -17.925 0.192   1.00 14.93 ?  145 ASP   A N    1 
ATOM   3110 C  CA   . ASP   A 1 145 ? 18.552 -19.036 -0.431  1.00 15.42 ?  145 ASP   A CA   1 
ATOM   3111 C  C    . ASP   A 1 145 ? 20.072 -18.889 -0.382  1.00 14.99 ?  145 ASP   A C    1 
ATOM   3112 O  O    . ASP   A 1 145 ? 20.777 -19.783 -0.860  1.00 16.93 ?  145 ASP   A O    1 
ATOM   3113 C  CB   . ASP   A 1 145 ? 18.110 -19.186 -1.889  1.00 16.83 ?  145 ASP   A CB   1 
ATOM   3114 C  CG   . ASP   A 1 145 ? 16.664 -19.629 -2.022  1.00 19.15 ?  145 ASP   A CG   1 
ATOM   3115 O  OD1  . ASP   A 1 145 ? 16.095 -20.164 -1.043  1.00 19.77 ?  145 ASP   A OD1  1 
ATOM   3116 O  OD2  . ASP   A 1 145 ? 16.099 -19.433 -3.117  1.00 20.34 -1 145 ASP   A OD2  1 
ATOM   3117 H  H    . ASP   A 1 145 ? 17.606 -17.308 -0.363  1.00 17.93 ?  145 ASP   A H    1 
ATOM   3118 H  HA   . ASP   A 1 145 ? 18.316 -19.854 0.031   1.00 18.52 ?  145 ASP   A HA   1 
ATOM   3119 H  HB2  . ASP   A 1 145 ? 18.215 -18.335 -2.343  1.00 20.21 ?  145 ASP   A HB2  1 
ATOM   3120 H  HB3  . ASP   A 1 145 ? 18.662 -19.860 -2.319  1.00 20.21 ?  145 ASP   A HB3  1 
ATOM   3121 N  N    . THR   A 1 146 ? 20.595 -17.797 0.175   1.00 13.46 ?  146 THR   A N    1 
ATOM   3122 C  CA   . THR   A 1 146 ? 22.034 -17.546 0.193   1.00 13.25 ?  146 THR   A CA   1 
ATOM   3123 C  C    . THR   A 1 146 ? 22.587 -17.360 1.593   1.00 12.95 ?  146 THR   A C    1 
ATOM   3124 O  O    . THR   A 1 146 ? 23.666 -17.886 1.906   1.00 13.89 ?  146 THR   A O    1 
ATOM   3125 C  CB   . THR   A 1 146 ? 22.356 -16.297 -0.648  1.00 13.29 ?  146 THR   A CB   1 
ATOM   3126 O  OG1  . THR   A 1 146 ? 21.839 -16.467 -1.967  1.00 13.62 ?  146 THR   A OG1  1 
ATOM   3127 C  CG2  . THR   A 1 146 ? 23.859 -16.071 -0.739  1.00 13.61 ?  146 THR   A CG2  1 
ATOM   3128 H  H    . THR   A 1 146 ? 20.128 -17.178 0.547   1.00 16.16 ?  146 THR   A H    1 
ATOM   3129 H  HA   . THR   A 1 146 ? 22.495 -18.295 -0.204  1.00 15.91 ?  146 THR   A HA   1 
ATOM   3130 H  HB   . THR   A 1 146 ? 21.957 -15.513 -0.233  1.00 15.96 ?  146 THR   A HB   1 
ATOM   3131 H  HG1  . THR   A 1 146 ? 21.002 -16.541 -1.933  1.00 16.35 ?  146 THR   A HG1  1 
ATOM   3132 H  HG21 . THR   A 1 146 ? 24.049 -15.406 -1.419  1.00 16.35 ?  146 THR   A HG21 1 
ATOM   3133 H  HG22 . THR   A 1 146 ? 24.203 -15.759 0.112   1.00 16.35 ?  146 THR   A HG22 1 
ATOM   3134 H  HG23 . THR   A 1 146 ? 24.301 -16.900 -0.976  1.00 16.35 ?  146 THR   A HG23 1 
ATOM   3135 N  N    . VAL   A 1 147 ? 21.909 -16.576 2.427   1.00 12.83 ?  147 VAL   A N    1 
ATOM   3136 C  CA   . VAL   A 1 147 ? 22.403 -16.273 3.760   1.00 13.07 ?  147 VAL   A CA   1 
ATOM   3137 C  C    . VAL   A 1 147 ? 22.079 -17.439 4.680   1.00 13.37 ?  147 VAL   A C    1 
ATOM   3138 O  O    . VAL   A 1 147 ? 20.935 -17.912 4.732   1.00 13.97 ?  147 VAL   A O    1 
ATOM   3139 C  CB   . VAL   A 1 147 ? 21.780 -14.968 4.276   1.00 12.99 ?  147 VAL   A CB   1 
ATOM   3140 C  CG1  . VAL   A 1 147 ? 22.316 -14.645 5.648   1.00 13.92 ?  147 VAL   A CG1  1 
ATOM   3141 C  CG2  . VAL   A 1 147 ? 22.044 -13.832 3.299   1.00 13.02 ?  147 VAL   A CG2  1 
ATOM   3142 H  H    . VAL   A 1 147 ? 21.148 -16.212 2.246   1.00 15.41 ?  147 VAL   A H    1 
ATOM   3143 H  HA   . VAL   A 1 147 ? 23.366 -16.163 3.728   1.00 15.69 ?  147 VAL   A HA   1 
ATOM   3144 H  HB   . VAL   A 1 147 ? 20.825 -15.082 4.352   1.00 15.59 ?  147 VAL   A HB   1 
ATOM   3145 H  HG11 . VAL   A 1 147 ? 22.069 -13.739 5.879   1.00 16.71 ?  147 VAL   A HG11 1 
ATOM   3146 H  HG12 . VAL   A 1 147 ? 21.939 -15.267 6.290   1.00 16.71 ?  147 VAL   A HG12 1 
ATOM   3147 H  HG13 . VAL   A 1 147 ? 23.285 -14.730 5.637   1.00 16.71 ?  147 VAL   A HG13 1 
ATOM   3148 H  HG21 . VAL   A 1 147 ? 21.728 -13.003 3.691   1.00 15.64 ?  147 VAL   A HG21 1 
ATOM   3149 H  HG22 . VAL   A 1 147 ? 22.993 -13.779 3.124   1.00 15.64 ?  147 VAL   A HG22 1 
ATOM   3150 H  HG23 . VAL   A 1 147 ? 21.562 -14.012 2.476   1.00 15.64 ?  147 VAL   A HG23 1 
ATOM   3151 N  N    . ARG   A 1 148 ? 23.097 -17.908 5.400   1.00 13.74 ?  148 ARG   A N    1 
ATOM   3152 C  CA   . ARG   A 1 148 ? 22.958 -18.983 6.366   1.00 14.01 ?  148 ARG   A CA   1 
ATOM   3153 C  C    . ARG   A 1 148 ? 23.079 -18.507 7.799   1.00 14.26 ?  148 ARG   A C    1 
ATOM   3154 O  O    . ARG   A 1 148 ? 22.672 -19.232 8.715   1.00 15.66 ?  148 ARG   A O    1 
ATOM   3155 C  CB   . ARG   A 1 148 ? 24.005 -20.074 6.097   1.00 14.61 ?  148 ARG   A CB   1 
ATOM   3156 C  CG   . ARG   A 1 148 ? 23.860 -20.717 4.730   1.00 15.99 ?  148 ARG   A CG   1 
ATOM   3157 C  CD   . ARG   A 1 148 ? 24.954 -21.743 4.461   1.00 16.67 ?  148 ARG   A CD   1 
ATOM   3158 N  NE   . ARG   A 1 148 ? 26.291 -21.158 4.496   1.00 16.56 ?  148 ARG   A NE   1 
ATOM   3159 C  CZ   . ARG   A 1 148 ? 26.809 -20.428 3.518   1.00 16.00 ?  148 ARG   A CZ   1 
ATOM   3160 N  NH1  . ARG   A 1 148 ? 26.140 -20.200 2.399   1.00 16.16 ?  148 ARG   A NH1  1 
ATOM   3161 N  NH2  . ARG   A 1 148 ? 28.026 -19.900 3.670   1.00 16.32 ?  148 ARG   A NH2  1 
ATOM   3162 H  H    . ARG   A 1 148 ? 23.902 -17.603 5.336   1.00 16.50 ?  148 ARG   A H    1 
ATOM   3163 H  HA   . ARG   A 1 148 ? 22.085 -19.381 6.262   1.00 16.82 ?  148 ARG   A HA   1 
ATOM   3164 H  HB2  . ARG   A 1 148 ? 24.892 -19.690 6.151   1.00 17.54 ?  148 ARG   A HB2  1 
ATOM   3165 H  HB3  . ARG   A 1 148 ? 23.906 -20.777 6.759   1.00 17.54 ?  148 ARG   A HB3  1 
ATOM   3166 H  HG2  . ARG   A 1 148 ? 22.999 -21.157 4.678   1.00 19.20 ?  148 ARG   A HG2  1 
ATOM   3167 H  HG3  . ARG   A 1 148 ? 23.918 -20.019 4.051   1.00 19.20 ?  148 ARG   A HG3  1 
ATOM   3168 H  HD2  . ARG   A 1 148 ? 24.907 -22.430 5.139   1.00 20.01 ?  148 ARG   A HD2  1 
ATOM   3169 H  HD3  . ARG   A 1 148 ? 24.813 -22.125 3.582   1.00 20.01 ?  148 ARG   A HD3  1 
ATOM   3170 H  HE   . ARG   A 1 148 ? 26.763 -21.282 5.199   1.00 19.88 ?  148 ARG   A HE   1 
ATOM   3171 H  HH11 . ARG   A 1 148 ? 25.353 -20.522 2.289   1.00 19.40 ?  148 ARG   A HH11 1 
ATOM   3172 H  HH12 . ARG   A 1 148 ? 26.496 -19.717 1.778   1.00 19.40 ?  148 ARG   A HH12 1 
ATOM   3173 H  HH21 . ARG   A 1 148 ? 28.460 -20.033 4.397   1.00 19.59 ?  148 ARG   A HH21 1 
ATOM   3174 H  HH22 . ARG   A 1 148 ? 28.368 -19.420 3.043   1.00 19.59 ?  148 ARG   A HH22 1 
ATOM   3175 N  N    . THR   A 1 149 ? 23.627 -17.313 8.009   1.00 14.39 ?  149 THR   A N    1 
ATOM   3176 C  CA   . THR   A 1 149 ? 23.692 -16.708 9.324   1.00 14.49 ?  149 THR   A CA   1 
ATOM   3177 C  C    . THR   A 1 149 ? 22.364 -16.013 9.620   1.00 13.94 ?  149 THR   A C    1 
ATOM   3178 O  O    . THR   A 1 149 ? 21.434 -16.013 8.804   1.00 14.61 ?  149 THR   A O    1 
ATOM   3179 C  CB   . THR   A 1 149 ? 24.891 -15.768 9.390   1.00 14.85 ?  149 THR   A CB   1 
ATOM   3180 O  OG1  . THR   A 1 149 ? 24.773 -14.835 8.314   1.00 14.80 ?  149 THR   A OG1  1 
ATOM   3181 C  CG2  . THR   A 1 149 ? 26.204 -16.562 9.278   1.00 15.10 ?  149 THR   A CG2  1 
ATOM   3182 H  H    . THR   A 1 149 ? 23.985 -16.830 7.389   1.00 17.28 ?  149 THR   A H    1 
ATOM   3183 H  HA   . THR   A 1 149 ? 23.820 -17.410 9.983   1.00 17.39 ?  149 THR   A HA   1 
ATOM   3184 H  HB   . THR   A 1 149 ? 24.876 -15.298 10.235  1.00 17.83 ?  149 THR   A HB   1 
ATOM   3185 H  HG1  . THR   A 1 149 ? 25.422 -14.305 8.324   1.00 17.76 ?  149 THR   A HG1  1 
ATOM   3186 H  HG21 . THR   A 1 149 ? 26.961 -15.961 9.340   1.00 18.13 ?  149 THR   A HG21 1 
ATOM   3187 H  HG22 . THR   A 1 149 ? 26.264 -17.217 9.995   1.00 18.13 ?  149 THR   A HG22 1 
ATOM   3188 H  HG23 . THR   A 1 149 ? 26.243 -17.030 8.427   1.00 18.13 ?  149 THR   A HG23 1 
ATOM   3189 N  N    . ASN   A 1 150 ? 22.237 -15.471 10.826  1.00 14.14 ?  150 ASN   A N    1 
ATOM   3190 C  CA   . ASN   A 1 150 ? 20.957 -14.952 11.305  1.00 14.57 ?  150 ASN   A CA   1 
ATOM   3191 C  C    . ASN   A 1 150 ? 20.780 -13.514 10.834  1.00 13.61 ?  150 ASN   A C    1 
ATOM   3192 O  O    . ASN   A 1 150 ? 21.534 -12.619 11.236  1.00 14.85 ?  150 ASN   A O    1 
ATOM   3193 C  CB   . ASN   A 1 150 ? 20.892 -15.057 12.822  1.00 17.11 ?  150 ASN   A CB   1 
ATOM   3194 C  CG   . ASN   A 1 150 ? 20.785 -16.489 13.288  1.00 21.29 ?  150 ASN   A CG   1 
ATOM   3195 O  OD1  . ASN   A 1 150 ? 20.187 -17.324 12.607  1.00 22.44 ?  150 ASN   A OD1  1 
ATOM   3196 N  ND2  . ASN   A 1 150 ? 21.372 -16.790 14.444  1.00 23.80 ?  150 ASN   A ND2  1 
ATOM   3197 H  H    . ASN   A 1 150 ? 22.878 -15.397 11.391  1.00 16.98 ?  150 ASN   A H    1 
ATOM   3198 H  HA   . ASN   A 1 150 ? 20.235 -15.489 10.934  1.00 17.49 ?  150 ASN   A HA   1 
ATOM   3199 H  HB2  . ASN   A 1 150 ? 21.695 -14.679 13.205  1.00 20.54 ?  150 ASN   A HB2  1 
ATOM   3200 H  HB3  . ASN   A 1 150 ? 20.108 -14.586 13.144  1.00 20.54 ?  150 ASN   A HB3  1 
ATOM   3201 H  HD21 . ASN   A 1 150 ? 21.344 -17.597 14.756  1.00 28.57 ?  150 ASN   A HD21 1 
ATOM   3202 H  HD22 . ASN   A 1 150 ? 21.781 -16.179 14.892  1.00 28.57 ?  150 ASN   A HD22 1 
ATOM   3203 N  N    . VAL   A 1 151 ? 19.790 -13.289 9.978   1.00 13.34 ?  151 VAL   A N    1 
ATOM   3204 C  CA   . VAL   A 1 151 ? 19.583 -11.987 9.365   1.00 13.31 ?  151 VAL   A CA   1 
ATOM   3205 C  C    . VAL   A 1 151 ? 18.195 -11.472 9.724   1.00 13.16 ?  151 VAL   A C    1 
ATOM   3206 O  O    . VAL   A 1 151 ? 17.186 -12.182 9.584   1.00 14.79 ?  151 VAL   A O    1 
ATOM   3207 C  CB   . VAL   A 1 151 ? 19.876 -11.994 7.849   1.00 14.75 ?  151 VAL   A CB   1 
ATOM   3208 C  CG1  . VAL   A 1 151 ? 19.055 -13.031 7.114   1.00 15.76 ?  151 VAL   A CG1  1 
ATOM   3209 C  CG2  . VAL   A 1 151 ? 19.680 -10.599 7.255   1.00 14.76 ?  151 VAL   A CG2  1 
ATOM   3210 H  H    . VAL   A 1 151 ? 19.212 -13.882 9.736   1.00 16.02 ?  151 VAL   A H    1 
ATOM   3211 H  HA   . VAL   A 1 151 ? 20.225 -11.371 9.755   1.00 15.99 ?  151 VAL   A HA   1 
ATOM   3212 H  HB   . VAL   A 1 151 ? 20.811 -12.230 7.717   1.00 17.71 ?  151 VAL   A HB   1 
ATOM   3213 H  HG11 . VAL   A 1 151 ? 19.255 -12.990 6.164   1.00 18.92 ?  151 VAL   A HG11 1 
ATOM   3214 H  HG12 . VAL   A 1 151 ? 19.278 -13.917 7.454   1.00 18.92 ?  151 VAL   A HG12 1 
ATOM   3215 H  HG13 . VAL   A 1 151 ? 18.112 -12.856 7.260   1.00 18.92 ?  151 VAL   A HG13 1 
ATOM   3216 H  HG21 . VAL   A 1 151 ? 20.001 -10.598 6.336   1.00 17.72 ?  151 VAL   A HG21 1 
ATOM   3217 H  HG22 . VAL   A 1 151 ? 18.735 -10.378 7.269   1.00 17.72 ?  151 VAL   A HG22 1 
ATOM   3218 H  HG23 . VAL   A 1 151 ? 20.181 -9.958  7.778   1.00 17.72 ?  151 VAL   A HG23 1 
ATOM   3219 N  N    . TYR   A 1 152 ? 18.176 -10.227 10.201  1.00 13.20 ?  152 TYR   A N    1 
ATOM   3220 C  CA   . TYR   A 1 152 ? 16.980 -9.496  10.585  1.00 13.16 ?  152 TYR   A CA   1 
ATOM   3221 C  C    . TYR   A 1 152 ? 16.785 -8.392  9.558   1.00 12.49 ?  152 TYR   A C    1 
ATOM   3222 O  O    . TYR   A 1 152 ? 17.563 -7.431  9.508   1.00 12.65 ?  152 TYR   A O    1 
ATOM   3223 C  CB   . TYR   A 1 152 ? 17.156 -8.945  11.996  1.00 14.21 ?  152 TYR   A CB   1 
ATOM   3224 C  CG   . TYR   A 1 152 ? 17.113 -10.062 12.999  1.00 14.92 ?  152 TYR   A CG   1 
ATOM   3225 C  CD1  . TYR   A 1 152 ? 18.246 -10.815 13.285  1.00 16.28 ?  152 TYR   A CD1  1 
ATOM   3226 C  CD2  . TYR   A 1 152 ? 15.925 -10.409 13.622  1.00 15.30 ?  152 TYR   A CD2  1 
ATOM   3227 C  CE1  . TYR   A 1 152 ? 18.203 -11.864 14.179  1.00 17.90 ?  152 TYR   A CE1  1 
ATOM   3228 C  CE2  . TYR   A 1 152 ? 15.868 -11.465 14.520  1.00 17.02 ?  152 TYR   A CE2  1 
ATOM   3229 C  CZ   . TYR   A 1 152 ? 17.012 -12.187 14.794  1.00 17.96 ?  152 TYR   A CZ   1 
ATOM   3230 O  OH   . TYR   A 1 152 ? 16.972 -13.241 15.684  1.00 20.59 ?  152 TYR   A OH   1 
ATOM   3231 H  H    . TYR   A 1 152 ? 18.898 -9.750  10.293  1.00 15.84 ?  152 TYR   A H    1 
ATOM   3232 H  HA   . TYR   A 1 152 ? 16.217 -10.089 10.565  1.00 15.80 ?  152 TYR   A HA   1 
ATOM   3233 H  HB2  . TYR   A 1 152 ? 18.020 -8.508  12.064  1.00 17.07 ?  152 TYR   A HB2  1 
ATOM   3234 H  HB3  . TYR   A 1 152 ? 16.443 -8.326  12.193  1.00 17.07 ?  152 TYR   A HB3  1 
ATOM   3235 H  HD1  . TYR   A 1 152 ? 19.051 -10.605 12.866  1.00 19.54 ?  152 TYR   A HD1  1 
ATOM   3236 H  HD2  . TYR   A 1 152 ? 15.151 -9.923  13.433  1.00 18.37 ?  152 TYR   A HD2  1 
ATOM   3237 H  HE1  . TYR   A 1 152 ? 18.971 -12.354 14.364  1.00 21.49 ?  152 TYR   A HE1  1 
ATOM   3238 H  HE2  . TYR   A 1 152 ? 15.064 -11.677 14.938  1.00 20.43 ?  152 TYR   A HE2  1 
ATOM   3239 H  HH   . TYR   A 1 152 ? 16.196 -13.324 15.993  1.00 24.71 ?  152 TYR   A HH   1 
ATOM   3240 N  N    . LEU   A 1 153 ? 15.775 -8.558  8.712   1.00 12.62 ?  153 LEU   A N    1 
ATOM   3241 C  CA   . LEU   A 1 153 ? 15.530 -7.662  7.593   1.00 12.62 ?  153 LEU   A CA   1 
ATOM   3242 C  C    . LEU   A 1 153 ? 14.536 -6.582  7.990   1.00 12.81 ?  153 LEU   A C    1 
ATOM   3243 O  O    . LEU   A 1 153 ? 13.433 -6.883  8.458   1.00 14.10 ?  153 LEU   A O    1 
ATOM   3244 C  CB   . LEU   A 1 153 ? 14.965 -8.447  6.411   1.00 12.70 ?  153 LEU   A CB   1 
ATOM   3245 C  CG   . LEU   A 1 153 ? 15.902 -9.460  5.753   1.00 12.75 ?  153 LEU   A CG   1 
ATOM   3246 C  CD1  . LEU   A 1 153 ? 15.127 -10.349 4.800   1.00 13.47 ?  153 LEU   A CD1  1 
ATOM   3247 C  CD2  . LEU   A 1 153 ? 17.025 -8.750  5.019   1.00 13.42 ?  153 LEU   A CD2  1 
ATOM   3248 H  H    . LEU   A 1 153 ? 15.194 -9.196  8.775   1.00 15.15 ?  153 LEU   A H    1 
ATOM   3249 H  HA   . LEU   A 1 153 ? 16.361 -7.250  7.332   1.00 15.16 ?  153 LEU   A HA   1 
ATOM   3250 H  HB2  . LEU   A 1 153 ? 14.182 -8.932  6.722   1.00 15.25 ?  153 LEU   A HB2  1 
ATOM   3251 H  HB3  . LEU   A 1 153 ? 14.698 -7.810  5.732   1.00 15.25 ?  153 LEU   A HB3  1 
ATOM   3252 H  HG   . LEU   A 1 153 ? 16.299 -10.019 6.443   1.00 15.31 ?  153 LEU   A HG   1 
ATOM   3253 H  HD11 . LEU   A 1 153 ? 15.711 -11.047 4.476   1.00 16.18 ?  153 LEU   A HD11 1 
ATOM   3254 H  HD12 . LEU   A 1 153 ? 14.373 -10.732 5.271   1.00 16.18 ?  153 LEU   A HD12 1 
ATOM   3255 H  HD13 . LEU   A 1 153 ? 14.811 -9.806  4.058   1.00 16.18 ?  153 LEU   A HD13 1 
ATOM   3256 H  HD21 . LEU   A 1 153 ? 17.585 -9.412  4.597   1.00 16.11 ?  153 LEU   A HD21 1 
ATOM   3257 H  HD22 . LEU   A 1 153 ? 16.633 -8.164  4.353   1.00 16.11 ?  153 LEU   A HD22 1 
ATOM   3258 H  HD23 . LEU   A 1 153 ? 17.538 -8.231  5.657   1.00 16.11 ?  153 LEU   A HD23 1 
ATOM   3259 N  N    . ALA   A 1 154 ? 14.925 -5.328  7.790   1.00 12.76 ?  154 ALA   A N    1 
ATOM   3260 C  CA   . ALA   A 1 154 ? 14.067 -4.177  8.022   1.00 13.12 ?  154 ALA   A CA   1 
ATOM   3261 C  C    . ALA   A 1 154 ? 13.576 -3.677  6.673   1.00 12.88 ?  154 ALA   A C    1 
ATOM   3262 O  O    . ALA   A 1 154 ? 14.374 -3.296  5.809   1.00 13.84 ?  154 ALA   A O    1 
ATOM   3263 C  CB   . ALA   A 1 154 ? 14.833 -3.070  8.745   1.00 13.96 ?  154 ALA   A CB   1 
ATOM   3264 H  H    . ALA   A 1 154 ? 15.713 -5.112  7.511   1.00 15.32 ?  154 ALA   A H    1 
ATOM   3265 H  HA   . ALA   A 1 154 ? 13.306 -4.437  8.572   1.00 15.75 ?  154 ALA   A HA   1 
ATOM   3266 H  HB1  . ALA   A 1 154 ? 14.239 -2.316  8.892   1.00 16.76 ?  154 ALA   A HB1  1 
ATOM   3267 H  HB2  . ALA   A 1 154 ? 15.156 -3.404  9.600   1.00 16.76 ?  154 ALA   A HB2  1 
ATOM   3268 H  HB3  . ALA   A 1 154 ? 15.585 -2.796  8.196   1.00 16.76 ?  154 ALA   A HB3  1 
ATOM   3269 N  N    A VAL   A 1 155 ? 12.264 -3.678  6.496   0.34 11.72 ?  155 VAL   A N    1 
ATOM   3270 N  N    B VAL   A 1 155 ? 12.261 -3.681  6.498   0.36 11.49 ?  155 VAL   A N    1 
ATOM   3271 C  CA   A VAL   A 1 155 ? 11.627 -3.180  5.289   0.34 12.14 ?  155 VAL   A CA   1 
ATOM   3272 C  CA   B VAL   A 1 155 ? 11.620 -3.227  5.275   0.36 11.79 ?  155 VAL   A CA   1 
ATOM   3273 C  CA   T VAL   A 1 155 ? 11.358 -3.312  4.610   0.30 16.04 ?  155 VAL   A CA   1 
ATOM   3274 C  C    A VAL   A 1 155 ? 10.939 -1.872  5.654   0.34 13.05 ?  155 VAL   A C    1 
ATOM   3275 C  C    B VAL   A 1 155 ? 10.913 -1.914  5.583   0.36 12.95 ?  155 VAL   A C    1 
ATOM   3276 C  C    T VAL   A 1 155 ? 10.796 -1.984  5.121   0.30 15.25 ?  155 VAL   A C    1 
ATOM   3277 O  O    A VAL   A 1 155 ? 10.000 -1.860  6.459   0.34 13.39 ?  155 VAL   A O    1 
ATOM   3278 O  O    B VAL   A 1 155 ? 10.098 -1.842  6.513   0.36 12.92 ?  155 VAL   A O    1 
ATOM   3279 O  O    T VAL   A 1 155 ? 9.804  -1.950  5.849   0.30 14.94 ?  155 VAL   A O    1 
ATOM   3280 C  CB   A VAL   A 1 155 ? 10.638 -4.202  4.716   0.34 12.30 ?  155 VAL   A CB   1 
ATOM   3281 C  CB   B VAL   A 1 155 ? 10.651 -4.283  4.726   0.36 11.85 ?  155 VAL   A CB   1 
ATOM   3282 C  CB   T VAL   A 1 155 ? 10.268 -4.374  4.395   0.30 16.63 ?  155 VAL   A CB   1 
ATOM   3283 C  CG1  A VAL   A 1 155 ? 9.987  -3.659  3.454   0.34 12.44 ?  155 VAL   A CG1  1 
ATOM   3284 C  CG1  B VAL   A 1 155 ? 9.913  -3.741  3.511   0.36 12.10 ?  155 VAL   A CG1  1 
ATOM   3285 C  CG1  T VAL   A 1 155 ? 9.535  -4.135  3.086   0.30 16.84 ?  155 VAL   A CG1  1 
ATOM   3286 C  CG2  A VAL   A 1 155 ? 11.350 -5.524  4.438   0.34 13.25 ?  155 VAL   A CG2  1 
ATOM   3287 C  CG2  B VAL   A 1 155 ? 11.410 -5.560  4.380   0.36 12.92 ?  155 VAL   A CG2  1 
ATOM   3288 C  CG2  T VAL   A 1 155 ? 10.883 -5.766  4.407   0.30 16.76 ?  155 VAL   A CG2  1 
ATOM   3289 H  H    A VAL   A 1 155 ? 11.704 -3.977  7.083   0.34 14.07 ?  155 VAL   A H    1 
ATOM   3290 H  H    B VAL   A 1 155 ? 11.704 -3.959  7.099   0.36 13.79 ?  155 VAL   A H    1 
ATOM   3291 H  HA   A VAL   A 1 155 ? 12.302 -2.989  4.624   0.34 14.58 ?  155 VAL   A HA   1 
ATOM   3292 H  HA   B VAL   A 1 155 ? 12.301 -3.055  4.607   0.36 14.15 ?  155 VAL   A HA   1 
ATOM   3293 H  HB   A VAL   A 1 155 ? 9.938  -4.364  5.370   0.34 14.77 ?  155 VAL   A HB   1 
ATOM   3294 H  HB   B VAL   A 1 155 ? 9.995  -4.493  5.411   0.36 14.23 ?  155 VAL   A HB   1 
ATOM   3295 H  HB   T VAL   A 1 155 ? 9.621  -4.312  5.115   0.30 19.97 ?  155 VAL   A HB   1 
ATOM   3296 H  HG11 A VAL   A 1 155 ? 9.475  -4.369  3.037   0.34 14.94 ?  155 VAL   A HG11 1 
ATOM   3297 H  HG11 B VAL   A 1 155 ? 9.461  -4.474  3.068   0.36 14.52 ?  155 VAL   A HG11 1 
ATOM   3298 H  HG11 T VAL   A 1 155 ? 8.847  -4.814  2.980   0.30 20.22 ?  155 VAL   A HG11 1 
ATOM   3299 H  HG12 A VAL   A 1 155 ? 9.399  -2.922  3.689   0.34 14.94 ?  155 VAL   A HG12 1 
ATOM   3300 H  HG12 B VAL   A 1 155 ? 9.265  -3.079  3.800   0.36 14.52 ?  155 VAL   A HG12 1 
ATOM   3301 H  HG12 T VAL   A 1 155 ? 9.130  -3.255  3.106   0.30 20.22 ?  155 VAL   A HG12 1 
ATOM   3302 H  HG13 A VAL   A 1 155 ? 10.679 -3.351  2.850   0.34 14.94 ?  155 VAL   A HG13 1 
ATOM   3303 H  HG13 B VAL   A 1 155 ? 10.555 -3.335  2.908   0.36 14.52 ?  155 VAL   A HG13 1 
ATOM   3304 H  HG13 T VAL   A 1 155 ? 10.170 -4.193  2.356   0.30 20.22 ?  155 VAL   A HG13 1 
ATOM   3305 H  HG21 A VAL   A 1 155 ? 10.730 -6.131  4.009   0.34 15.91 ?  155 VAL   A HG21 1 
ATOM   3306 H  HG21 B VAL   A 1 155 ? 10.829 -6.139  3.867   0.36 15.51 ?  155 VAL   A HG21 1 
ATOM   3307 H  HG21 T VAL   A 1 155 ? 10.182 -6.427  4.292   0.30 20.12 ?  155 VAL   A HG21 1 
ATOM   3308 H  HG22 A VAL   A 1 155 ? 12.108 -5.354  3.854   0.34 15.91 ?  155 VAL   A HG22 1 
ATOM   3309 H  HG22 B VAL   A 1 155 ? 12.194 -5.328  3.857   0.36 15.51 ?  155 VAL   A HG22 1 
ATOM   3310 H  HG22 T VAL   A 1 155 ? 11.523 -5.834  3.679   0.30 20.12 ?  155 VAL   A HG22 1 
ATOM   3311 H  HG23 A VAL   A 1 155 ? 11.660 -5.900  5.277   0.34 15.91 ?  155 VAL   A HG23 1 
ATOM   3312 H  HG23 B VAL   A 1 155 ? 11.682 -6.000  5.202   0.36 15.51 ?  155 VAL   A HG23 1 
ATOM   3313 H  HG23 T VAL   A 1 155 ? 11.331 -5.901  5.255   0.30 20.12 ?  155 VAL   A HG23 1 
ATOM   3314 N  N    A PHE   A 1 156 ? 11.406 -0.764  5.070   0.34 14.18 ?  156 PHE   A N    1 
ATOM   3315 N  N    B PHE   A 1 156 ? 11.238 -0.873  4.810   0.36 14.87 ?  156 PHE   A N    1 
ATOM   3316 N  N    T PHE   A 1 156 ? 11.459 -0.898  4.712   0.30 15.28 ?  156 PHE   A N    1 
ATOM   3317 C  CA   A PHE   A 1 156 ? 10.879 0.549   5.442   0.34 16.02 ?  156 PHE   A CA   1 
ATOM   3318 C  CA   B PHE   A 1 156 ? 10.698 0.462   5.064   0.36 16.05 ?  156 PHE   A CA   1 
ATOM   3319 C  CA   T PHE   A 1 156 ? 11.070 0.452   5.124   0.30 15.06 ?  156 PHE   A CA   1 
ATOM   3320 C  C    A PHE   A 1 156 ? 9.408  0.692   5.066   0.34 16.36 ?  156 PHE   A C    1 
ATOM   3321 C  C    B PHE   A 1 156 ? 9.236  0.581   4.625   0.36 16.20 ?  156 PHE   A C    1 
ATOM   3322 C  C    T PHE   A 1 156 ? 9.613  0.734   4.792   0.30 15.09 ?  156 PHE   A C    1 
ATOM   3323 O  O    A PHE   A 1 156 ? 8.593  1.165   5.867   0.34 16.65 ?  156 PHE   A O    1 
ATOM   3324 O  O    B PHE   A 1 156 ? 8.422  1.190   5.331   0.36 16.42 ?  156 PHE   A O    1 
ATOM   3325 O  O    T PHE   A 1 156 ? 8.908  1.406   5.555   0.30 15.58 ?  156 PHE   A O    1 
ATOM   3326 C  CB   A PHE   A 1 156 ? 11.710 1.660   4.794   0.34 17.33 ?  156 PHE   A CB   1 
ATOM   3327 C  CB   B PHE   A 1 156 ? 11.577 1.499   4.351   0.36 17.40 ?  156 PHE   A CB   1 
ATOM   3328 C  CB   T PHE   A 1 156 ? 11.973 1.453   4.397   0.30 14.61 ?  156 PHE   A CB   1 
ATOM   3329 C  CG   A PHE   A 1 156 ? 11.198 3.043   5.094   0.34 18.46 ?  156 PHE   A CG   1 
ATOM   3330 C  CG   B PHE   A 1 156 ? 11.295 2.933   4.742   0.36 19.33 ?  156 PHE   A CG   1 
ATOM   3331 C  CG   T PHE   A 1 156 ? 11.571 2.903   4.568   0.30 14.72 ?  156 PHE   A CG   1 
ATOM   3332 C  CD1  A PHE   A 1 156 ? 11.054 3.461   6.405   0.34 18.81 ?  156 PHE   A CD1  1 
ATOM   3333 C  CD1  B PHE   A 1 156 ? 10.299 3.659   4.110   0.36 20.44 ?  156 PHE   A CD1  1 
ATOM   3334 C  CD1  T PHE   A 1 156 ? 11.879 3.582   5.738   0.30 16.02 ?  156 PHE   A CD1  1 
ATOM   3335 C  CD2  A PHE   A 1 156 ? 10.865 3.923   4.073   0.34 18.88 ?  156 PHE   A CD2  1 
ATOM   3336 C  CD2  B PHE   A 1 156 ? 12.052 3.563   5.723   0.36 20.29 ?  156 PHE   A CD2  1 
ATOM   3337 C  CD2  T PHE   A 1 156 ? 10.920 3.591   3.550   0.30 14.81 ?  156 PHE   A CD2  1 
ATOM   3338 C  CE1  A PHE   A 1 156 ? 10.586 4.725   6.697   0.34 19.23 ?  156 PHE   A CE1  1 
ATOM   3339 C  CE1  B PHE   A 1 156 ? 10.044 4.978   4.462   0.36 20.89 ?  156 PHE   A CE1  1 
ATOM   3340 C  CE1  T PHE   A 1 156 ? 11.527 4.909   5.901   0.30 16.53 ?  156 PHE   A CE1  1 
ATOM   3341 C  CE2  A PHE   A 1 156 ? 10.393 5.194   4.359   0.34 19.58 ?  156 PHE   A CE2  1 
ATOM   3342 C  CE2  B PHE   A 1 156 ? 11.806 4.882   6.079   0.36 20.98 ?  156 PHE   A CE2  1 
ATOM   3343 C  CE2  T PHE   A 1 156 ? 10.570 4.923   3.707   0.30 15.69 ?  156 PHE   A CE2  1 
ATOM   3344 C  CZ   A PHE   A 1 156 ? 10.254 5.594   5.674   0.34 19.71 ?  156 PHE   A CZ   1 
ATOM   3345 C  CZ   B PHE   A 1 156 ? 10.804 5.591   5.447   0.36 21.09 ?  156 PHE   A CZ   1 
ATOM   3346 C  CZ   T PHE   A 1 156 ? 10.876 5.581   4.885   0.30 16.16 ?  156 PHE   A CZ   1 
ATOM   3347 H  H    A PHE   A 1 156 ? 12.015 -0.744  4.458   0.34 17.02 ?  156 PHE   A H    1 
ATOM   3348 H  H    B PHE   A 1 156 ? 11.783 -0.912  4.148   0.36 17.86 ?  156 PHE   A H    1 
ATOM   3349 H  H    T PHE   A 1 156 ? 12.130 -0.922  4.182   0.30 18.35 ?  156 PHE   A H    1 
ATOM   3350 H  HA   A PHE   A 1 156 ? 10.949 0.656   6.399   0.34 19.23 ?  156 PHE   A HA   1 
ATOM   3351 H  HA   B PHE   A 1 156 ? 10.745 0.646   6.019   0.36 19.27 ?  156 PHE   A HA   1 
ATOM   3352 H  HA   T PHE   A 1 156 ? 11.197 0.547   6.083   0.30 18.08 ?  156 PHE   A HA   1 
ATOM   3353 H  HB2  A PHE   A 1 156 ? 12.623 1.606   5.124   0.34 20.81 ?  156 PHE   A HB2  1 
ATOM   3354 H  HB2  B PHE   A 1 156 ? 12.512 1.321   4.559   0.36 20.89 ?  156 PHE   A HB2  1 
ATOM   3355 H  HB2  T PHE   A 1 156 ? 12.876 1.350   4.737   0.30 17.54 ?  156 PHE   A HB2  1 
ATOM   3356 H  HB3  A PHE   A 1 156 ? 11.703 1.545   3.831   0.34 20.81 ?  156 PHE   A HB3  1 
ATOM   3357 H  HB3  B PHE   A 1 156 ? 11.439 1.425   3.396   0.36 20.89 ?  156 PHE   A HB3  1 
ATOM   3358 H  HB3  T PHE   A 1 156 ? 11.954 1.248   3.451   0.30 17.54 ?  156 PHE   A HB3  1 
ATOM   3359 H  HD1  A PHE   A 1 156 ? 11.277 2.881   7.098   0.34 22.58 ?  156 PHE   A HD1  1 
ATOM   3360 H  HD1  B PHE   A 1 156 ? 9.787  3.256   3.448   0.36 24.54 ?  156 PHE   A HD1  1 
ATOM   3361 H  HD1  T PHE   A 1 156 ? 12.316 3.128   6.429   0.30 19.23 ?  156 PHE   A HD1  1 
ATOM   3362 H  HD2  A PHE   A 1 156 ? 10.959 3.656   3.187   0.34 22.67 ?  156 PHE   A HD2  1 
ATOM   3363 H  HD2  B PHE   A 1 156 ? 12.728 3.093   6.154   0.36 24.36 ?  156 PHE   A HD2  1 
ATOM   3364 H  HD2  T PHE   A 1 156 ? 10.714 3.146   2.761   0.30 17.78 ?  156 PHE   A HD2  1 
ATOM   3365 H  HE1  A PHE   A 1 156 ? 10.494 4.992   7.584   0.34 23.08 ?  156 PHE   A HE1  1 
ATOM   3366 H  HE1  B PHE   A 1 156 ? 9.369  5.454   4.033   0.36 25.07 ?  156 PHE   A HE1  1 
ATOM   3367 H  HE1  T PHE   A 1 156 ? 11.733 5.345   6.698   0.30 19.85 ?  156 PHE   A HE1  1 
ATOM   3368 H  HE2  A PHE   A 1 156 ? 10.173 5.775   3.669   0.34 23.51 ?  156 PHE   A HE2  1 
ATOM   3369 H  HE2  B PHE   A 1 156 ? 12.316 5.289   6.744   0.36 25.19 ?  156 PHE   A HE2  1 
ATOM   3370 H  HE2  T PHE   A 1 156 ? 10.129 5.368   3.027   0.30 18.84 ?  156 PHE   A HE2  1 
ATOM   3371 H  HZ   A PHE   A 1 156 ? 9.939  6.445   5.873   0.34 23.66 ?  156 PHE   A HZ   1 
ATOM   3372 H  HZ   B PHE   A 1 156 ? 10.634 6.475   5.686   0.36 25.32 ?  156 PHE   A HZ   1 
ATOM   3373 H  HZ   T PHE   A 1 156 ? 10.638 6.470   4.999   0.30 19.40 ?  156 PHE   A HZ   1 
ATOM   3374 N  N    A ASP   A 1 157 ? 9.052  0.294   3.848   0.34 16.60 ?  157 ASP   A N    1 
ATOM   3375 N  N    B ASP   A 1 157 ? 8.878  0.004   3.477   0.36 16.85 ?  157 ASP   A N    1 
ATOM   3376 N  N    T ASP   A 1 157 ? 9.152  0.233   3.655   0.30 14.96 ?  157 ASP   A N    1 
ATOM   3377 C  CA   A ASP   A 1 157 ? 7.727  0.557   3.301   0.34 17.51 ?  157 ASP   A CA   1 
ATOM   3378 C  CA   B ASP   A 1 157 ? 7.568  0.231   2.867   0.36 17.24 ?  157 ASP   A CA   1 
ATOM   3379 C  CA   T ASP   A 1 157 ? 7.856  0.580   3.096   0.30 15.06 ?  157 ASP   A CA   1 
ATOM   3380 C  C    A ASP   A 1 157 ? 6.737  -0.484  3.819   0.34 17.94 ?  157 ASP   A C    1 
ATOM   3381 C  C    B ASP   A 1 157 ? 6.558  -0.825  3.310   0.36 16.62 ?  157 ASP   A C    1 
ATOM   3382 C  C    T ASP   A 1 157 ? 6.805  -0.403  3.602   0.30 15.46 ?  157 ASP   A C    1 
ATOM   3383 O  O    A ASP   A 1 157 ? 6.915  -1.685  3.589   0.34 17.66 ?  157 ASP   A O    1 
ATOM   3384 O  O    B ASP   A 1 157 ? 6.792  -2.026  3.147   0.36 16.10 ?  157 ASP   A O    1 
ATOM   3385 O  O    T ASP   A 1 157 ? 6.900  -1.608  3.343   0.30 15.32 ?  157 ASP   A O    1 
ATOM   3386 C  CB   A ASP   A 1 157 ? 7.813  0.505   1.779   0.34 18.05 ?  157 ASP   A CB   1 
ATOM   3387 C  CB   B ASP   A 1 157 ? 7.689  0.210   1.345   0.36 18.14 ?  157 ASP   A CB   1 
ATOM   3388 C  CB   T ASP   A 1 157 ? 7.983  0.507   1.578   0.30 14.69 ?  157 ASP   A CB   1 
ATOM   3389 C  CG   A ASP   A 1 157 ? 6.572  1.039   1.108   0.34 19.00 ?  157 ASP   A CG   1 
ATOM   3390 C  CG   B ASP   A 1 157 ? 6.422  0.685   0.651   0.36 19.13 ?  157 ASP   A CG   1 
ATOM   3391 C  CG   T ASP   A 1 157 ? 6.788  1.052   0.869   0.30 14.41 ?  157 ASP   A CG   1 
ATOM   3392 O  OD1  A ASP   A 1 157 ? 6.426  2.277   1.032   0.34 20.40 ?  157 ASP   A OD1  1 
ATOM   3393 O  OD1  B ASP   A 1 157 ? 6.141  1.900   0.684   0.36 20.48 ?  157 ASP   A OD1  1 
ATOM   3394 O  OD1  T ASP   A 1 157 ? 5.698  0.472   1.036   0.30 15.08 ?  157 ASP   A OD1  1 
ATOM   3395 O  OD2  A ASP   A 1 157 ? 5.740  0.222   0.662   0.34 18.67 -1 157 ASP   A OD2  1 
ATOM   3396 O  OD2  B ASP   A 1 157 ? 5.701  -0.161  0.079   0.36 18.78 -1 157 ASP   A OD2  1 
ATOM   3397 O  OD2  T ASP   A 1 157 ? 6.938  2.055   0.146   0.30 13.62 -1 157 ASP   A OD2  1 
ATOM   3398 H  H    A ASP   A 1 157 ? 9.566  -0.142  3.314   0.34 19.93 ?  157 ASP   A H    1 
ATOM   3399 H  H    B ASP   A 1 157 ? 9.385  -0.533  3.033   0.36 20.23 ?  157 ASP   A H    1 
ATOM   3400 H  H    T ASP   A 1 157 ? 9.592  -0.324  3.173   0.30 17.96 ?  157 ASP   A H    1 
ATOM   3401 H  HA   A ASP   A 1 157 ? 7.426  1.440   3.565   0.34 21.02 ?  157 ASP   A HA   1 
ATOM   3402 H  HA   B ASP   A 1 157 ? 7.242  1.100   3.143   0.36 20.70 ?  157 ASP   A HA   1 
ATOM   3403 H  HA   T ASP   A 1 157 ? 7.608  1.483   3.357   0.30 18.08 ?  157 ASP   A HA   1 
ATOM   3404 H  HB2  A ASP   A 1 157 ? 8.570  1.039   1.485   0.34 21.67 ?  157 ASP   A HB2  1 
ATOM   3405 H  HB2  B ASP   A 1 157 ? 8.445  0.767   1.089   0.36 21.77 ?  157 ASP   A HB2  1 
ATOM   3406 H  HB2  T ASP   A 1 157 ? 8.759  1.016   1.301   0.30 17.64 ?  157 ASP   A HB2  1 
ATOM   3407 H  HB3  A ASP   A 1 157 ? 7.943  -0.416  1.500   0.34 21.67 ?  157 ASP   A HB3  1 
ATOM   3408 H  HB3  B ASP   A 1 157 ? 7.841  -0.701  1.056   0.36 21.77 ?  157 ASP   A HB3  1 
ATOM   3409 H  HB3  T ASP   A 1 157 ? 8.088  -0.421  1.317   0.30 17.64 ?  157 ASP   A HB3  1 
ATOM   3410 N  N    A LYS   A 1 158 ? 5.688  -0.028  4.513   0.34 18.74 ?  158 LYS   A N    1 
ATOM   3411 N  N    B LYS   A 1 158 ? 5.410  -0.366  3.819   0.36 17.16 ?  158 LYS   A N    1 
ATOM   3412 N  N    T LYS   A 1 158 ? 5.799  0.108   4.318   0.30 16.48 ?  158 LYS   A N    1 
ATOM   3413 C  CA   A LYS   A 1 158 ? 4.713  -0.965  5.069   0.34 19.62 ?  158 LYS   A CA   1 
ATOM   3414 C  CA   B LYS   A 1 158 ? 4.430  -1.271  4.419   0.36 17.84 ?  158 LYS   A CA   1 
ATOM   3415 C  CA   T LYS   A 1 158 ? 4.819  -0.782  4.936   0.30 17.80 ?  158 LYS   A CA   1 
ATOM   3416 C  C    A LYS   A 1 158 ? 3.978  -1.715  3.968   0.34 18.67 ?  158 LYS   A C    1 
ATOM   3417 C  C    B LYS   A 1 158 ? 3.751  -2.143  3.364   0.36 16.49 ?  158 LYS   A C    1 
ATOM   3418 C  C    T LYS   A 1 158 ? 4.052  -1.577  3.889   0.30 17.22 ?  158 LYS   A C    1 
ATOM   3419 O  O    A LYS   A 1 158 ? 3.777  -2.930  4.065   0.34 18.68 ?  158 LYS   A O    1 
ATOM   3420 O  O    B LYS   A 1 158 ? 3.646  -3.365  3.529   0.36 16.11 ?  158 LYS   A O    1 
ATOM   3421 O  O    T LYS   A 1 158 ? 3.812  -2.776  4.067   0.30 16.88 ?  158 LYS   A O    1 
ATOM   3422 C  CB   A LYS   A 1 158 ? 3.715  -0.237  5.971   0.34 21.46 ?  158 LYS   A CB   1 
ATOM   3423 C  CB   B LYS   A 1 158 ? 3.406  -0.456  5.217   0.36 20.05 ?  158 LYS   A CB   1 
ATOM   3424 C  CB   T LYS   A 1 158 ? 3.855  0.001   5.828   0.30 19.95 ?  158 LYS   A CB   1 
ATOM   3425 C  CG   A LYS   A 1 158 ? 2.485  -1.070  6.379   0.34 23.26 ?  158 LYS   A CG   1 
ATOM   3426 C  CG   B LYS   A 1 158 ? 2.204  -1.240  5.736   0.36 22.45 ?  158 LYS   A CG   1 
ATOM   3427 C  CG   T LYS   A 1 158 ? 2.630  -0.802  6.285   0.30 22.14 ?  158 LYS   A CG   1 
ATOM   3428 C  CD   A LYS   A 1 158 ? 2.844  -2.359  7.132   0.34 24.63 ?  158 LYS   A CD   1 
ATOM   3429 C  CD   B LYS   A 1 158 ? 2.596  -2.300  6.755   0.36 24.49 ?  158 LYS   A CD   1 
ATOM   3430 C  CD   T LYS   A 1 158 ? 3.010  -2.027  7.119   0.30 24.14 ?  158 LYS   A CD   1 
ATOM   3431 C  CE   A LYS   A 1 158 ? 1.598  -3.040  7.702   0.34 25.43 ?  158 LYS   A CE   1 
ATOM   3432 C  CE   B LYS   A 1 158 ? 1.361  -2.871  7.441   0.36 25.79 ?  158 LYS   A CE   1 
ATOM   3433 C  CE   T LYS   A 1 158 ? 1.774  -2.834  7.518   0.30 25.52 ?  158 LYS   A CE   1 
ATOM   3434 N  NZ   A LYS   A 1 158 ? 1.878  -4.394  8.269   0.34 25.77 ?  158 LYS   A NZ   1 
ATOM   3435 N  NZ   B LYS   A 1 158 ? 1.679  -4.034  8.315   0.36 26.49 ?  158 LYS   A NZ   1 
ATOM   3436 N  NZ   T LYS   A 1 158 ? 2.111  -4.070  8.288   0.30 26.23 ?  158 LYS   A NZ   1 
ATOM   3437 H  H    A LYS   A 1 158 ? 5.525  0.799   4.669   0.34 22.50 ?  158 LYS   A H    1 
ATOM   3438 H  H    B LYS   A 1 158 ? 5.175  0.460   3.822   0.36 20.61 ?  158 LYS   A H    1 
ATOM   3439 H  H    T LYS   A 1 158 ? 5.662  0.945   4.449   0.30 19.79 ?  158 LYS   A H    1 
ATOM   3440 H  HA   A LYS   A 1 158 ? 5.181  -1.619  5.608   0.34 23.55 ?  158 LYS   A HA   1 
ATOM   3441 H  HA   B LYS   A 1 158 ? 4.883  -1.858  5.044   0.36 21.42 ?  158 LYS   A HA   1 
ATOM   3442 H  HA   T LYS   A 1 158 ? 5.289  -1.417  5.498   0.30 21.37 ?  158 LYS   A HA   1 
ATOM   3443 H  HB2  A LYS   A 1 158 ? 4.169  0.038   6.781   0.34 25.76 ?  158 LYS   A HB2  1 
ATOM   3444 H  HB2  B LYS   A 1 158 ? 3.851  -0.068  5.991   0.36 24.07 ?  158 LYS   A HB2  1 
ATOM   3445 H  HB2  T LYS   A 1 158 ? 4.331  0.285   6.625   0.30 23.94 ?  158 LYS   A HB2  1 
ATOM   3446 H  HB3  A LYS   A 1 158 ? 3.392  0.546   5.499   0.34 25.76 ?  158 LYS   A HB3  1 
ATOM   3447 H  HB3  B LYS   A 1 158 ? 3.066  0.256   4.654   0.36 24.07 ?  158 LYS   A HB3  1 
ATOM   3448 H  HB3  T LYS   A 1 158 ? 3.536  0.774   5.342   0.30 23.94 ?  158 LYS   A HB3  1 
ATOM   3449 H  HG2  A LYS   A 1 158 ? 1.930  -0.534  6.964   0.34 27.92 ?  158 LYS   A HG2  1 
ATOM   3450 H  HG2  B LYS   A 1 158 ? 1.593  -0.625  6.170   0.36 26.95 ?  158 LYS   A HG2  1 
ATOM   3451 H  HG2  T LYS   A 1 158 ? 2.073  -0.234  6.835   0.30 26.57 ?  158 LYS   A HG2  1 
ATOM   3452 H  HG3  A LYS   A 1 158 ? 1.979  -1.314  5.586   0.34 27.92 ?  158 LYS   A HG3  1 
ATOM   3453 H  HG3  B LYS   A 1 158 ? 1.758  -1.680  4.997   0.36 26.95 ?  158 LYS   A HG3  1 
ATOM   3454 H  HG3  T LYS   A 1 158 ? 2.124  -1.104  5.512   0.30 26.57 ?  158 LYS   A HG3  1 
ATOM   3455 H  HD2  A LYS   A 1 158 ? 3.278  -2.978  6.525   0.34 29.56 ?  158 LYS   A HD2  1 
ATOM   3456 H  HD2  B LYS   A 1 158 ? 3.062  -3.022  6.306   0.36 29.40 ?  158 LYS   A HD2  1 
ATOM   3457 H  HD2  T LYS   A 1 158 ? 3.591  -2.606  6.603   0.30 28.97 ?  158 LYS   A HD2  1 
ATOM   3458 H  HD3  A LYS   A 1 158 ? 3.429  -2.145  7.872   0.34 29.56 ?  158 LYS   A HD3  1 
ATOM   3459 H  HD3  B LYS   A 1 158 ? 3.166  -1.899  7.432   0.36 29.40 ?  158 LYS   A HD3  1 
ATOM   3460 H  HD3  T LYS   A 1 158 ? 3.456  -1.739  7.931   0.30 28.97 ?  158 LYS   A HD3  1 
ATOM   3461 H  HE2  A LYS   A 1 158 ? 1.230  -2.488  8.412   0.34 30.52 ?  158 LYS   A HE2  1 
ATOM   3462 H  HE2  B LYS   A 1 158 ? 0.962  -2.180  7.993   0.36 30.95 ?  158 LYS   A HE2  1 
ATOM   3463 H  HE2  T LYS   A 1 158 ? 1.197  -2.284  8.072   0.30 30.63 ?  158 LYS   A HE2  1 
ATOM   3464 H  HE3  A LYS   A 1 158 ? 0.944  -3.142  6.996   0.34 30.52 ?  158 LYS   A HE3  1 
ATOM   3465 H  HE3  B LYS   A 1 158 ? 0.728  -3.159  6.766   0.36 30.95 ?  158 LYS   A HE3  1 
ATOM   3466 H  HE3  T LYS   A 1 158 ? 1.300  -3.105  6.717   0.30 30.63 ?  158 LYS   A HE3  1 
ATOM   3467 H  HZ1  A LYS   A 1 158 ? 1.128  -4.752  8.590   0.34 30.93 ?  158 LYS   A HZ1  1 
ATOM   3468 H  HZ1  B LYS   A 1 158 ? 0.935  -4.339  8.696   0.36 31.79 ?  158 LYS   A HZ1  1 
ATOM   3469 H  HZ1  T LYS   A 1 158 ? 1.366  -4.510  8.500   0.30 31.49 ?  158 LYS   A HZ1  1 
ATOM   3470 H  HZ2  A LYS   A 1 158 ? 2.203  -4.927  7.634   0.34 30.93 ?  158 LYS   A HZ2  1 
ATOM   3471 H  HZ2  B LYS   A 1 158 ? 2.046  -4.685  7.833   0.36 31.79 ?  158 LYS   A HZ2  1 
ATOM   3472 H  HZ2  T LYS   A 1 158 ? 2.629  -4.602  7.797   0.30 31.49 ?  158 LYS   A HZ2  1 
ATOM   3473 H  HZ3  A LYS   A 1 158 ? 2.474  -4.333  8.927   0.34 30.93 ?  158 LYS   A HZ3  1 
ATOM   3474 H  HZ3  B LYS   A 1 158 ? 2.250  -3.787  8.952   0.36 31.79 ?  158 LYS   A HZ3  1 
ATOM   3475 H  HZ3  T LYS   A 1 158 ? 2.542  -3.855  9.036   0.30 31.49 ?  158 LYS   A HZ3  1 
ATOM   3476 N  N    A ASN   A 1 159 ? 3.554  -1.009  2.920   0.34 17.98 ?  159 ASN   A N    1 
ATOM   3477 N  N    B ASN   A 1 159 ? 3.270  -1.533  2.277   0.36 16.28 ?  159 ASN   A N    1 
ATOM   3478 N  N    T ASN   A 1 159 ? 3.645  -0.934  2.801   0.30 17.32 ?  159 ASN   A N    1 
ATOM   3479 C  CA   A ASN   A 1 159 ? 2.876  -1.689  1.824   0.34 17.24 ?  159 ASN   A CA   1 
ATOM   3480 C  CA   B ASN   A 1 159 ? 2.656  -2.316  1.209   0.36 16.29 ?  159 ASN   A CA   1 
ATOM   3481 C  CA   T ASN   A 1 159 ? 2.905  -1.638  1.761   0.30 17.64 ?  159 ASN   A CA   1 
ATOM   3482 C  C    A ASN   A 1 159 ? 3.780  -2.740  1.195   0.34 16.07 ?  159 ASN   A C    1 
ATOM   3483 C  C    B ASN   A 1 159 ? 3.610  -3.394  0.712   0.36 15.43 ?  159 ASN   A C    1 
ATOM   3484 C  C    T ASN   A 1 159 ? 3.753  -2.736  1.134   0.30 17.80 ?  159 ASN   A C    1 
ATOM   3485 O  O    A ASN   A 1 159 ? 3.334  -3.853  0.898   0.34 15.39 ?  159 ASN   A O    1 
ATOM   3486 O  O    B ASN   A 1 159 ? 3.209  -4.543  0.486   0.36 15.76 ?  159 ASN   A O    1 
ATOM   3487 O  O    T ASN   A 1 159 ? 3.237  -3.791  0.774   0.30 17.60 ?  159 ASN   A O    1 
ATOM   3488 C  CB   A ASN   A 1 159 ? 2.389  -0.677  0.786   0.34 18.13 ?  159 ASN   A CB   1 
ATOM   3489 C  CB   B ASN   A 1 159 ? 2.224  -1.395  0.065   0.36 17.84 ?  159 ASN   A CB   1 
ATOM   3490 C  CB   T ASN   A 1 159 ? 2.395  -0.668  0.693   0.30 18.26 ?  159 ASN   A CB   1 
ATOM   3491 C  CG   A ASN   A 1 159 ? 1.156  0.084   1.246   0.34 19.53 ?  159 ASN   A CG   1 
ATOM   3492 C  CG   B ASN   A 1 159 ? 0.819  -0.856  0.248   0.36 19.74 ?  159 ASN   A CG   1 
ATOM   3493 C  CG   T ASN   A 1 159 ? 1.182  0.123   1.157   0.30 19.19 ?  159 ASN   A CG   1 
ATOM   3494 O  OD1  A ASN   A 1 159 ? 0.326  -0.445  1.985   0.34 20.75 ?  159 ASN   A OD1  1 
ATOM   3495 O  OD1  B ASN   A 1 159 ? 0.312  -0.780  1.366   0.36 20.83 ?  159 ASN   A OD1  1 
ATOM   3496 O  OD1  T ASN   A 1 159 ? 0.385  -0.356  1.962   0.30 20.20 ?  159 ASN   A OD1  1 
ATOM   3497 N  ND2  A ASN   A 1 159 ? 1.029  1.328   0.808   0.34 19.90 ?  159 ASN   A ND2  1 
ATOM   3498 N  ND2  B ASN   A 1 159 ? 0.180  -0.481  -0.855  0.36 20.23 ?  159 ASN   A ND2  1 
ATOM   3499 N  ND2  T ASN   A 1 159 ? 1.037  1.337   0.650   0.30 19.41 ?  159 ASN   A ND2  1 
ATOM   3500 H  H    A ASN   A 1 159 ? 3.646  -0.164  2.821   0.34 21.59 ?  159 ASN   A H    1 
ATOM   3501 H  H    B ASN   A 1 159 ? 3.296  -0.686  2.140   0.36 19.54 ?  159 ASN   A H    1 
ATOM   3502 H  H    T ASN   A 1 159 ? 3.778  -0.103  2.644   0.30 20.80 ?  159 ASN   A H    1 
ATOM   3503 H  HA   A ASN   A 1 159 ? 2.095  -2.148  2.174   0.34 20.70 ?  159 ASN   A HA   1 
ATOM   3504 H  HA   B ASN   A 1 159 ? 1.861  -2.749  1.550   0.36 19.55 ?  159 ASN   A HA   1 
ATOM   3505 H  HA   T ASN   A 1 159 ? 2.135  -2.068  2.161   0.30 21.18 ?  159 ASN   A HA   1 
ATOM   3506 H  HB2  A ASN   A 1 159 ? 3.089  -0.033  0.618   0.34 21.77 ?  159 ASN   A HB2  1 
ATOM   3507 H  HB2  B ASN   A 1 159 ? 2.834  -0.633  0.018   0.36 21.42 ?  159 ASN   A HB2  1 
ATOM   3508 H  HB2  T ASN   A 1 159 ? 3.096  -0.039  0.474   0.30 21.92 ?  159 ASN   A HB2  1 
ATOM   3509 H  HB3  A ASN   A 1 159 ? 2.166  -1.149  -0.036  0.34 21.77 ?  159 ASN   A HB3  1 
ATOM   3510 H  HB3  B ASN   A 1 159 ? 2.243  -1.882  -0.768  0.36 21.42 ?  159 ASN   A HB3  1 
ATOM   3511 H  HB3  T ASN   A 1 159 ? 2.146  -1.176  -0.101  0.30 21.92 ?  159 ASN   A HB3  1 
ATOM   3512 H  HD21 A ASN   A 1 159 ? 0.345  1.792   1.038   0.34 23.89 ?  159 ASN   A HD21 1 
ATOM   3513 H  HD21 B ASN   A 1 159 ? -0.619 -0.158  -0.807  0.36 24.29 ?  159 ASN   A HD21 1 
ATOM   3514 H  HD21 T ASN   A 1 159 ? 0.362  1.814   0.880   0.30 23.30 ?  159 ASN   A HD21 1 
ATOM   3515 H  HD22 A ASN   A 1 159 ? 1.630  1.665   0.298   0.34 23.89 ?  159 ASN   A HD22 1 
ATOM   3516 H  HD22 B ASN   A 1 159 ? 0.563  -0.556  -1.621  0.36 24.29 ?  159 ASN   A HD22 1 
ATOM   3517 H  HD22 T ASN   A 1 159 ? 1.615  1.640   0.096   0.30 23.30 ?  159 ASN   A HD22 1 
ATOM   3518 N  N    A LEU   A 1 160 ? 5.061  -2.422  1.008   0.34 15.54 ?  160 LEU   A N    1 
ATOM   3519 N  N    B LEU   A 1 160 ? 4.886  -3.045  0.560   0.36 14.84 ?  160 LEU   A N    1 
ATOM   3520 N  N    T LEU   A 1 160 ? 5.053  -2.503  1.014   0.30 18.13 ?  160 LEU   A N    1 
ATOM   3521 C  CA   A LEU   A 1 160 ? 5.974  -3.423  0.468   0.34 15.52 ?  160 LEU   A CA   1 
ATOM   3522 C  CA   B LEU   A 1 160 ? 5.875  -4.032  0.156   0.36 14.34 ?  160 LEU   A CA   1 
ATOM   3523 C  CA   T LEU   A 1 160 ? 5.940  -3.524  0.475   0.30 18.58 ?  160 LEU   A CA   1 
ATOM   3524 C  C    A LEU   A 1 160 ? 6.133  -4.597  1.425   0.34 14.71 ?  160 LEU   A C    1 
ATOM   3525 C  C    B LEU   A 1 160 ? 6.065  -5.085  1.243   0.36 14.01 ?  160 LEU   A C    1 
ATOM   3526 O  O    A LEU   A 1 160 ? 6.184  -5.755  0.994   0.34 14.18 ?  160 LEU   A O    1 
ATOM   3527 O  O    B LEU   A 1 160 ? 6.040  -6.289  0.965   0.36 14.20 ?  160 LEU   A O    1 
ATOM   3528 C  CB   A LEU   A 1 160 ? 7.332  -2.803  0.159   0.34 16.15 ?  160 LEU   A CB   1 
ATOM   3529 C  CB   B LEU   A 1 160 ? 7.194  -3.331  -0.153  0.36 14.41 ?  160 LEU   A CB   1 
ATOM   3530 C  CB   T LEU   A 1 160 ? 7.298  -2.932  0.115   0.30 18.97 ?  160 LEU   A CB   1 
ATOM   3531 C  CG   A LEU   A 1 160 ? 8.362  -3.841  -0.288  0.34 17.40 ?  160 LEU   A CG   1 
ATOM   3532 C  CG   B LEU   A 1 160 ? 8.318  -4.298  -0.487  0.36 15.30 ?  160 LEU   A CG   1 
ATOM   3533 C  CG   T LEU   A 1 160 ? 8.315  -3.976  -0.339  0.30 19.60 ?  160 LEU   A CG   1 
ATOM   3534 C  CD1  A LEU   A 1 160 ? 7.870  -4.614  -1.505  0.34 18.00 ?  160 LEU   A CD1  1 
ATOM   3535 C  CD1  B LEU   A 1 160 ? 7.918  -5.107  -1.705  0.36 16.26 ?  160 LEU   A CD1  1 
ATOM   3536 C  CD1  T LEU   A 1 160 ? 7.824  -4.716  -1.572  0.30 19.99 ?  160 LEU   A CD1  1 
ATOM   3537 C  CD2  A LEU   A 1 160 ? 9.690  -3.181  -0.572  0.34 17.76 ?  160 LEU   A CD2  1 
ATOM   3538 C  CD2  B LEU   A 1 160 ? 9.605  -3.531  -0.713  0.36 15.64 ?  160 LEU   A CD2  1 
ATOM   3539 C  CD2  T LEU   A 1 160 ? 9.650  -3.320  -0.606  0.30 19.73 ?  160 LEU   A CD2  1 
ATOM   3540 H  H    A LEU   A 1 160 ? 5.410  -1.657  1.180   0.34 18.66 ?  160 LEU   A H    1 
ATOM   3541 H  H    B LEU   A 1 160 ? 5.201  -2.259  0.695   0.36 17.82 ?  160 LEU   A H    1 
ATOM   3542 H  H    T LEU   A 1 160 ? 5.444  -1.770  1.238   0.30 21.76 ?  160 LEU   A H    1 
ATOM   3543 H  HA   A LEU   A 1 160 ? 5.602  -3.760  -0.358  0.34 18.63 ?  160 LEU   A HA   1 
ATOM   3544 H  HA   B LEU   A 1 160 ? 5.565  -4.473  -0.652  0.36 17.22 ?  160 LEU   A HA   1 
ATOM   3545 H  HB2  A LEU   A 1 160 ? 7.231  -2.140  -0.546  0.34 19.39 ?  160 LEU   A HB2  1 
ATOM   3546 H  HB2  B LEU   A 1 160 ? 7.071  -2.739  -0.916  0.36 17.30 ?  160 LEU   A HB2  1 
ATOM   3547 H  HB2  T LEU   A 1 160 ? 7.183  -2.289  -0.605  0.30 22.77 ?  160 LEU   A HB2  1 
ATOM   3548 H  HB3  A LEU   A 1 160 ? 7.670  -2.387  0.965   0.34 19.39 ?  160 LEU   A HB3  1 
ATOM   3549 H  HB3  B LEU   A 1 160 ? 7.464  -2.816  0.623   0.36 17.30 ?  160 LEU   A HB3  1 
ATOM   3550 H  HB3  T LEU   A 1 160 ? 7.660  -2.490  0.898   0.30 22.77 ?  160 LEU   A HB3  1 
ATOM   3551 H  HG   A LEU   A 1 160 ? 8.502  -4.477  0.430   0.34 20.89 ?  160 LEU   A HG   1 
ATOM   3552 H  HG   B LEU   A 1 160 ? 8.463  -4.905  0.255   0.36 18.37 ?  160 LEU   A HG   1 
ATOM   3553 H  HG   T LEU   A 1 160 ? 8.436  -4.625  0.371   0.30 23.53 ?  160 LEU   A HG   1 
ATOM   3554 H  HD11 A LEU   A 1 160 ? 8.602  -5.147  -1.853  0.34 21.61 ?  160 LEU   A HD11 1 
ATOM   3555 H  HD11 B LEU   A 1 160 ? 8.665  -5.649  -1.971  0.36 19.52 ?  160 LEU   A HD11 1 
ATOM   3556 H  HD11 T LEU   A 1 160 ? 8.536  -5.289  -1.897  0.30 24.00 ?  160 LEU   A HD11 1 
ATOM   3557 H  HD12 A LEU   A 1 160 ? 7.139  -5.197  -1.242  0.34 21.61 ?  160 LEU   A HD12 1 
ATOM   3558 H  HD12 B LEU   A 1 160 ? 7.165  -5.676  -1.477  0.36 19.52 ?  160 LEU   A HD12 1 
ATOM   3559 H  HD12 T LEU   A 1 160 ? 7.052  -5.253  -1.333  0.30 24.00 ?  160 LEU   A HD12 1 
ATOM   3560 H  HD13 A LEU   A 1 160 ? 7.567  -3.987  -2.179  0.34 21.61 ?  160 LEU   A HD13 1 
ATOM   3561 H  HD13 B LEU   A 1 160 ? 7.668  -4.496  -2.419  0.36 19.52 ?  160 LEU   A HD13 1 
ATOM   3562 H  HD13 T LEU   A 1 160 ? 7.582  -4.070  -2.252  0.30 24.00 ?  160 LEU   A HD13 1 
ATOM   3563 H  HD21 A LEU   A 1 160 ? 10.323 -3.862  -0.846  0.34 21.32 ?  160 LEU   A HD21 1 
ATOM   3564 H  HD21 B LEU   A 1 160 ? 10.333 -4.161  -0.827  0.36 18.78 ?  160 LEU   A HD21 1 
ATOM   3565 H  HD21 T LEU   A 1 160 ? 10.281 -3.999  -0.889  0.30 23.69 ?  160 LEU   A HD21 1 
ATOM   3566 H  HD22 A LEU   A 1 160 ? 9.573  -2.531  -1.280  0.34 21.32 ?  160 LEU   A HD22 1 
ATOM   3567 H  HD22 B LEU   A 1 160 ? 9.513  -2.983  -1.508  0.36 18.78 ?  160 LEU   A HD22 1 
ATOM   3568 H  HD22 T LEU   A 1 160 ? 9.539  -2.656  -1.303  0.30 23.69 ?  160 LEU   A HD22 1 
ATOM   3569 H  HD23 A LEU   A 1 160 ? 10.001 -2.744  0.235   0.34 21.32 ?  160 LEU   A HD23 1 
ATOM   3570 H  HD23 B LEU   A 1 160 ? 9.779  -2.966  0.059   0.36 18.78 ?  160 LEU   A HD23 1 
ATOM   3571 H  HD23 T LEU   A 1 160 ? 9.960  -2.898  0.210   0.30 23.69 ?  160 LEU   A HD23 1 
ATOM   3572 N  N    A TYR   A 1 161 ? 6.228  -4.320  2.726   0.64 16.03 ?  161 TYR   A N    1 
ATOM   3573 N  N    B TYR   A 1 161 ? 6.263  -4.647  2.492   0.36 14.60 ?  161 TYR   A N    1 
ATOM   3574 C  CA   A TYR   A 1 161 ? 6.357  -5.398  3.702   0.64 16.28 ?  161 TYR   A CA   1 
ATOM   3575 C  CA   B TYR   A 1 161 ? 6.380  -5.586  3.606   0.36 15.25 ?  161 TYR   A CA   1 
ATOM   3576 C  C    A TYR   A 1 161 ? 5.205  -6.391  3.588   0.64 17.31 ?  161 TYR   A C    1 
ATOM   3577 C  C    B TYR   A 1 161 ? 5.195  -6.541  3.629   0.36 16.44 ?  161 TYR   A C    1 
ATOM   3578 O  O    A TYR   A 1 161 ? 5.417  -7.610  3.570   0.64 16.89 ?  161 TYR   A O    1 
ATOM   3579 O  O    B TYR   A 1 161 ? 5.363  -7.765  3.661   0.36 15.97 ?  161 TYR   A O    1 
ATOM   3580 C  CB   A TYR   A 1 161 ? 6.432  -4.822  5.114   0.64 16.34 ?  161 TYR   A CB   1 
ATOM   3581 C  CB   B TYR   A 1 161 ? 6.476  -4.830  4.939   0.36 15.25 ?  161 TYR   A CB   1 
ATOM   3582 C  CG   A TYR   A 1 161 ? 6.344  -5.887  6.169   0.64 15.66 ?  161 TYR   A CG   1 
ATOM   3583 C  CG   B TYR   A 1 161 ? 6.369  -5.738  6.155   0.36 14.98 ?  161 TYR   A CG   1 
ATOM   3584 C  CD1  A TYR   A 1 161 ? 7.457  -6.636  6.516   0.64 15.40 ?  161 TYR   A CD1  1 
ATOM   3585 C  CD1  B TYR   A 1 161 ? 7.485  -6.400  6.657   0.36 14.96 ?  161 TYR   A CD1  1 
ATOM   3586 C  CD2  A TYR   A 1 161 ? 5.141  -6.153  6.813   0.64 15.28 ?  161 TYR   A CD2  1 
ATOM   3587 C  CD2  B TYR   A 1 161 ? 5.149  -5.940  6.796   0.36 15.03 ?  161 TYR   A CD2  1 
ATOM   3588 C  CE1  A TYR   A 1 161 ? 7.375  -7.619  7.469   0.64 14.51 ?  161 TYR   A CE1  1 
ATOM   3589 C  CE1  B TYR   A 1 161 ? 7.389  -7.240  7.758   0.36 15.24 ?  161 TYR   A CE1  1 
ATOM   3590 C  CE2  A TYR   A 1 161 ? 5.053  -7.132  7.770   0.64 14.78 ?  161 TYR   A CE2  1 
ATOM   3591 C  CE2  B TYR   A 1 161 ? 5.045  -6.778  7.900   0.36 15.25 ?  161 TYR   A CE2  1 
ATOM   3592 C  CZ   A TYR   A 1 161 ? 6.173  -7.861  8.094   0.64 14.37 ?  161 TYR   A CZ   1 
ATOM   3593 C  CZ   B TYR   A 1 161 ? 6.169  -7.424  8.375   0.36 15.69 ?  161 TYR   A CZ   1 
ATOM   3594 O  OH   A TYR   A 1 161 ? 6.107  -8.839  9.053   0.64 14.18 ?  161 TYR   A OH   1 
ATOM   3595 O  OH   B TYR   A 1 161 ? 6.072  -8.260  9.470   0.36 16.79 ?  161 TYR   A OH   1 
ATOM   3596 H  H    A TYR   A 1 161 ? 6.223  -3.526  3.065   0.64 19.25 ?  161 TYR   A H    1 
ATOM   3597 H  H    B TYR   A 1 161 ? 6.324  -3.822  2.710   0.36 17.53 ?  161 TYR   A H    1 
ATOM   3598 H  HA   A TYR   A 1 161 ? 7.176  -5.877  3.534   0.64 19.55 ?  161 TYR   A HA   1 
ATOM   3599 H  HA   B TYR   A 1 161 ? 7.188  -6.109  3.498   0.36 18.31 ?  161 TYR   A HA   1 
ATOM   3600 H  HB2  A TYR   A 1 161 ? 7.284  -4.361  5.223   0.64 19.62 ?  161 TYR   A HB2  1 
ATOM   3601 H  HB2  B TYR   A 1 161 ? 7.334  -4.374  4.980   0.36 18.31 ?  161 TYR   A HB2  1 
ATOM   3602 H  HB3  A TYR   A 1 161 ? 5.702  -4.200  5.250   0.64 19.62 ?  161 TYR   A HB3  1 
ATOM   3603 H  HB3  B TYR   A 1 161 ? 5.758  -4.178  4.985   0.36 18.31 ?  161 TYR   A HB3  1 
ATOM   3604 H  HD1  A TYR   A 1 161 ? 8.269  -6.480  6.093   0.64 18.49 ?  161 TYR   A HD1  1 
ATOM   3605 H  HD1  B TYR   A 1 161 ? 8.309  -6.281  6.248   0.36 17.96 ?  161 TYR   A HD1  1 
ATOM   3606 H  HD2  A TYR   A 1 161 ? 4.383  -5.664  6.593   0.64 18.34 ?  161 TYR   A HD2  1 
ATOM   3607 H  HD2  B TYR   A 1 161 ? 4.387  -5.509  6.482   0.36 18.04 ?  161 TYR   A HD2  1 
ATOM   3608 H  HE1  A TYR   A 1 161 ? 8.127  -8.122  7.693   0.64 17.42 ?  161 TYR   A HE1  1 
ATOM   3609 H  HE1  B TYR   A 1 161 ? 8.144  -7.675  8.086   0.36 18.29 ?  161 TYR   A HE1  1 
ATOM   3610 H  HE2  A TYR   A 1 161 ? 4.237  -7.306  8.193   0.64 17.74 ?  161 TYR   A HE2  1 
ATOM   3611 H  HE2  B TYR   A 1 161 ? 4.219  -6.903  8.319   0.36 18.31 ?  161 TYR   A HE2  1 
ATOM   3612 H  HH   A TYR   A 1 161 ? 5.318  -8.902  9.354   0.64 17.03 ?  161 TYR   A HH   1 
ATOM   3613 H  HH   B TYR   A 1 161 ? 6.819  -8.588  9.657   0.36 20.16 ?  161 TYR   A HH   1 
ATOM   3614 N  N    A ASP   A 1 162 ? 3.970  -5.891  3.529   0.64 18.22 ?  162 ASP   A N    1 
ATOM   3615 N  N    B ASP   A 1 162 ? 3.980  -5.990  3.620   0.36 17.78 ?  162 ASP   A N    1 
ATOM   3616 C  CA   A ASP   A 1 162 ? 2.826  -6.798  3.464   0.64 19.41 ?  162 ASP   A CA   1 
ATOM   3617 C  CA   B ASP   A 1 162 ? 2.789  -6.832  3.583   0.36 19.10 ?  162 ASP   A CA   1 
ATOM   3618 C  C    A ASP   A 1 162 ? 2.871  -7.642  2.199   0.64 19.07 ?  162 ASP   A C    1 
ATOM   3619 C  C    B ASP   A 1 162 ? 2.816  -7.758  2.374   0.36 19.21 ?  162 ASP   A C    1 
ATOM   3620 O  O    A ASP   A 1 162 ? 2.529  -8.831  2.220   0.64 19.41 ?  162 ASP   A O    1 
ATOM   3621 O  O    B ASP   A 1 162 ? 2.448  -8.936  2.474   0.36 19.28 ?  162 ASP   A O    1 
ATOM   3622 C  CB   A ASP   A 1 162 ? 1.512  -6.017  3.536   0.64 21.30 ?  162 ASP   A CB   1 
ATOM   3623 C  CB   B ASP   A 1 162 ? 1.532  -5.960  3.560   0.36 20.37 ?  162 ASP   A CB   1 
ATOM   3624 C  CG   A ASP   A 1 162 ? 1.209  -5.491  4.923   0.64 23.07 ?  162 ASP   A CG   1 
ATOM   3625 C  CG   B ASP   A 1 162 ? 1.298  -5.217  4.860   0.36 21.63 ?  162 ASP   A CG   1 
ATOM   3626 O  OD1  A ASP   A 1 162 ? 1.824  -5.961  5.899   0.64 23.51 ?  162 ASP   A OD1  1 
ATOM   3627 O  OD1  B ASP   A 1 162 ? 1.978  -5.512  5.862   0.36 21.96 ?  162 ASP   A OD1  1 
ATOM   3628 O  OD2  A ASP   A 1 162 ? 0.319  -4.621  5.036   0.64 24.32 -1 162 ASP   A OD2  1 
ATOM   3629 O  OD2  B ASP   A 1 162 ? 0.420  -4.327  4.869   0.36 22.51 -1 162 ASP   A OD2  1 
ATOM   3630 H  H    A ASP   A 1 162 ? 3.767  -5.050  3.525   0.64 21.87 ?  162 ASP   A H    1 
ATOM   3631 H  H    B ASP   A 1 162 ? 3.823  -5.145  3.636   0.36 21.35 ?  162 ASP   A H    1 
ATOM   3632 H  HA   A ASP   A 1 162 ? 2.854  -7.399  4.222   0.64 23.30 ?  162 ASP   A HA   1 
ATOM   3633 H  HA   B ASP   A 1 162 ? 2.764  -7.382  4.378   0.36 22.93 ?  162 ASP   A HA   1 
ATOM   3634 H  HB2  A ASP   A 1 162 ? 1.555  -5.258  2.939   0.64 25.57 ?  162 ASP   A HB2  1 
ATOM   3635 H  HB2  B ASP   A 1 162 ? 1.621  -5.285  2.876   0.36 24.46 ?  162 ASP   A HB2  1 
ATOM   3636 H  HB3  A ASP   A 1 162 ? 0.779  -6.601  3.285   0.64 25.57 ?  162 ASP   A HB3  1 
ATOM   3637 H  HB3  B ASP   A 1 162 ? 0.761  -6.520  3.387   0.36 24.46 ?  162 ASP   A HB3  1 
ATOM   3638 N  N    A LYS   A 1 163 ? 3.296  -7.047  1.084   0.64 19.65 ?  163 LYS   A N    1 
ATOM   3639 N  N    B LYS   A 1 163 ? 3.255  -7.245  1.223   0.36 19.87 ?  163 LYS   A N    1 
ATOM   3640 C  CA   A LYS   A 1 163 ? 3.383  -7.812  -0.154  0.64 20.47 ?  163 LYS   A CA   1 
ATOM   3641 C  CA   B LYS   A 1 163 ? 3.375  -8.082  0.034   0.36 20.66 ?  163 LYS   A CA   1 
ATOM   3642 C  C    A LYS   A 1 163 ? 4.448  -8.901  -0.064  0.64 19.23 ?  163 LYS   A C    1 
ATOM   3643 C  C    B LYS   A 1 163 ? 4.489  -9.109  0.201   0.36 19.76 ?  163 LYS   A C    1 
ATOM   3644 O  O    A LYS   A 1 163 ? 4.269  -9.995  -0.609  0.64 18.89 ?  163 LYS   A O    1 
ATOM   3645 O  O    B LYS   A 1 163 ? 4.323  -10.279 -0.164  0.36 19.62 ?  163 LYS   A O    1 
ATOM   3646 C  CB   A LYS   A 1 163 ? 3.655  -6.883  -1.337  0.64 23.08 ?  163 LYS   A CB   1 
ATOM   3647 C  CB   B LYS   A 1 163 ? 3.627  -7.193  -1.184  0.36 22.88 ?  163 LYS   A CB   1 
ATOM   3648 C  CG   A LYS   A 1 163 ? 3.660  -7.605  -2.672  0.64 26.04 ?  163 LYS   A CG   1 
ATOM   3649 C  CG   B LYS   A 1 163 ? 3.838  -7.928  -2.494  0.36 25.25 ?  163 LYS   A CG   1 
ATOM   3650 C  CD   A LYS   A 1 163 ? 4.075  -6.690  -3.804  0.64 29.09 ?  163 LYS   A CD   1 
ATOM   3651 C  CD   B LYS   A 1 163 ? 4.514  -7.007  -3.493  0.36 27.50 ?  163 LYS   A CD   1 
ATOM   3652 C  CE   A LYS   A 1 163 ? 4.067  -7.431  -5.131  0.64 31.65 ?  163 LYS   A CE   1 
ATOM   3653 C  CE   B LYS   A 1 163 ? 4.052  -7.271  -4.911  0.36 29.27 ?  163 LYS   A CE   1 
ATOM   3654 N  NZ   A LYS   A 1 163 ? 4.713  -6.641  -6.213  0.64 32.92 ?  163 LYS   A NZ   1 
ATOM   3655 N  NZ   B LYS   A 1 163 ? 4.750  -6.381  -5.879  0.36 30.19 ?  163 LYS   A NZ   1 
ATOM   3656 H  H    A LYS   A 1 163 ? 3.529  -6.215  1.021   0.64 23.59 ?  163 LYS   A H    1 
ATOM   3657 H  H    B LYS   A 1 163 ? 3.493  -6.424  1.106   0.36 23.85 ?  163 LYS   A H    1 
ATOM   3658 H  HA   A LYS   A 1 163 ? 2.525  -8.238  -0.308  0.64 24.58 ?  163 LYS   A HA   1 
ATOM   3659 H  HA   B LYS   A 1 163 ? 2.541  -8.555  -0.109  0.36 24.81 ?  163 LYS   A HA   1 
ATOM   3660 H  HB2  A LYS   A 1 163 ? 2.961  -6.199  -1.372  0.64 27.70 ?  163 LYS   A HB2  1 
ATOM   3661 H  HB2  B LYS   A 1 163 ? 2.859  -6.607  -1.306  0.36 27.47 ?  163 LYS   A HB2  1 
ATOM   3662 H  HB3  A LYS   A 1 163 ? 4.519  -6.465  -1.218  0.64 27.70 ?  163 LYS   A HB3  1 
ATOM   3663 H  HB3  B LYS   A 1 163 ? 4.417  -6.657  -1.021  0.36 27.47 ?  163 LYS   A HB3  1 
ATOM   3664 H  HG2  A LYS   A 1 163 ? 4.288  -8.343  -2.636  0.64 31.26 ?  163 LYS   A HG2  1 
ATOM   3665 H  HG2  B LYS   A 1 163 ? 4.410  -8.700  -2.357  0.36 30.31 ?  163 LYS   A HG2  1 
ATOM   3666 H  HG3  A LYS   A 1 163 ? 2.767  -7.936  -2.859  0.64 31.26 ?  163 LYS   A HG3  1 
ATOM   3667 H  HG3  B LYS   A 1 163 ? 2.981  -8.201  -2.855  0.36 30.31 ?  163 LYS   A HG3  1 
ATOM   3668 H  HD2  A LYS   A 1 163 ? 3.452  -5.950  -3.863  0.64 34.92 ?  163 LYS   A HD2  1 
ATOM   3669 H  HD2  B LYS   A 1 163 ? 4.302  -6.087  -3.271  0.36 33.01 ?  163 LYS   A HD2  1 
ATOM   3670 H  HD3  A LYS   A 1 163 ? 4.974  -6.365  -3.640  0.64 34.92 ?  163 LYS   A HD3  1 
ATOM   3671 H  HD3  B LYS   A 1 163 ? 5.474  -7.147  -3.454  0.36 33.01 ?  163 LYS   A HD3  1 
ATOM   3672 H  HE2  A LYS   A 1 163 ? 4.546  -8.268  -5.032  0.64 37.99 ?  163 LYS   A HE2  1 
ATOM   3673 H  HE2  B LYS   A 1 163 ? 4.243  -8.192  -5.146  0.36 35.13 ?  163 LYS   A HE2  1 
ATOM   3674 H  HE3  A LYS   A 1 163 ? 3.150  -7.604  -5.391  0.64 37.99 ?  163 LYS   A HE3  1 
ATOM   3675 H  HE3  B LYS   A 1 163 ? 3.100  -7.099  -4.973  0.36 35.13 ?  163 LYS   A HE3  1 
ATOM   3676 H  HZ1  A LYS   A 1 163 ? 4.694  -7.099  -6.976  0.64 39.51 ?  163 LYS   A HZ1  1 
ATOM   3677 H  HZ1  B LYS   A 1 163 ? 4.468  -6.550  -6.705  0.36 36.24 ?  163 LYS   A HZ1  1 
ATOM   3678 H  HZ2  A LYS   A 1 163 ? 4.280  -5.872  -6.326  0.64 39.51 ?  163 LYS   A HZ2  1 
ATOM   3679 H  HZ2  B LYS   A 1 163 ? 4.583  -5.529  -5.683  0.36 36.24 ?  163 LYS   A HZ2  1 
ATOM   3680 H  HZ3  A LYS   A 1 163 ? 5.560  -6.468  -6.000  0.64 39.51 ?  163 LYS   A HZ3  1 
ATOM   3681 H  HZ3  B LYS   A 1 163 ? 5.629  -6.519  -5.839  0.36 36.24 ?  163 LYS   A HZ3  1 
ATOM   3682 N  N    A LEU   A 1 164 ? 5.567  -8.622  0.610   0.64 17.68 ?  164 LEU   A N    1 
ATOM   3683 N  N    B LEU   A 1 164 ? 5.628  -8.691  0.755   0.36 18.65 ?  164 LEU   A N    1 
ATOM   3684 C  CA   A LEU   A 1 164 ? 6.626  -9.624  0.715   0.64 17.01 ?  164 LEU   A CA   1 
ATOM   3685 C  CA   B LEU   A 1 164 ? 6.735  -9.617  0.977   0.36 17.65 ?  164 LEU   A CA   1 
ATOM   3686 C  C    A LEU   A 1 164 ? 6.184  -10.810 1.562   0.64 16.98 ?  164 LEU   A C    1 
ATOM   3687 C  C    B LEU   A 1 164 ? 6.307  -10.764 1.880   0.36 17.70 ?  164 LEU   A C    1 
ATOM   3688 O  O    A LEU   A 1 164 ? 6.468  -11.964 1.221   0.64 17.29 ?  164 LEU   A O    1 
ATOM   3689 O  O    B LEU   A 1 164 ? 6.610  -11.932 1.610   0.36 17.56 ?  164 LEU   A O    1 
ATOM   3690 C  CB   A LEU   A 1 164 ? 7.881  -8.997  1.311   0.64 16.45 ?  164 LEU   A CB   1 
ATOM   3691 C  CB   B LEU   A 1 164 ? 7.912  -8.872  1.606   0.36 16.87 ?  164 LEU   A CB   1 
ATOM   3692 C  CG   A LEU   A 1 164 ? 8.624  -8.021  0.402   0.64 16.48 ?  164 LEU   A CG   1 
ATOM   3693 C  CG   B LEU   A 1 164 ? 8.740  -7.951  0.711   0.36 16.68 ?  164 LEU   A CG   1 
ATOM   3694 C  CD1  A LEU   A 1 164 ? 9.583  -7.180  1.220   0.64 15.78 ?  164 LEU   A CD1  1 
ATOM   3695 C  CD1  B LEU   A 1 164 ? 9.637  -7.080  1.573   0.36 16.59 ?  164 LEU   A CD1  1 
ATOM   3696 C  CD2  A LEU   A 1 164 ? 9.372  -8.766  -0.690  0.64 17.04 ?  164 LEU   A CD2  1 
ATOM   3697 C  CD2  B LEU   A 1 164 ? 9.567  -8.752  -0.283  0.36 16.46 ?  164 LEU   A CD2  1 
ATOM   3698 H  H    A LEU   A 1 164 ? 5.733  -7.869  1.008   0.64 21.23 ?  164 LEU   A H    1 
ATOM   3699 H  H    B LEU   A 1 164 ? 5.777  -7.885  1.016   0.36 22.39 ?  164 LEU   A H    1 
ATOM   3700 H  HA   A LEU   A 1 164 ? 6.836  -9.944  -0.174  0.64 20.42 ?  164 LEU   A HA   1 
ATOM   3701 H  HA   B LEU   A 1 164 ? 7.021  -9.983  0.127   0.36 21.19 ?  164 LEU   A HA   1 
ATOM   3702 H  HB2  A LEU   A 1 164 ? 7.635  -8.513  2.112   0.64 19.74 ?  164 LEU   A HB2  1 
ATOM   3703 H  HB2  B LEU   A 1 164 ? 7.569  -8.325  2.328   0.36 20.25 ?  164 LEU   A HB2  1 
ATOM   3704 H  HB3  A LEU   A 1 164 ? 8.499  -9.709  1.534   0.64 19.74 ?  164 LEU   A HB3  1 
ATOM   3705 H  HB3  B LEU   A 1 164 ? 8.522  -9.532  1.967   0.36 20.25 ?  164 LEU   A HB3  1 
ATOM   3706 H  HG   A LEU   A 1 164 ? 7.987  -7.424  -0.021  0.64 19.78 ?  164 LEU   A HG   1 
ATOM   3707 H  HG   B LEU   A 1 164 ? 8.148  -7.369  0.210   0.36 20.03 ?  164 LEU   A HG   1 
ATOM   3708 H  HD11 A LEU   A 1 164 ? 10.059 -6.576  0.631   0.64 18.95 ?  164 LEU   A HD11 1 
ATOM   3709 H  HD11 B LEU   A 1 164 ? 10.153 -6.491  1.001   0.36 19.92 ?  164 LEU   A HD11 1 
ATOM   3710 H  HD12 A LEU   A 1 164 ? 9.079  -6.675  1.877   0.64 18.95 ?  164 LEU   A HD12 1 
ATOM   3711 H  HD12 B LEU   A 1 164 ? 9.084  -6.557  2.175   0.36 19.92 ?  164 LEU   A HD12 1 
ATOM   3712 H  HD13 A LEU   A 1 164 ? 10.213 -7.769  1.670   0.64 18.95 ?  164 LEU   A HD13 1 
ATOM   3713 H  HD13 B LEU   A 1 164 ? 10.233 -7.650  2.085   0.36 19.92 ?  164 LEU   A HD13 1 
ATOM   3714 H  HD21 A LEU   A 1 164 ? 9.867  -8.126  -1.227  0.64 20.45 ?  164 LEU   A HD21 1 
ATOM   3715 H  HD21 B LEU   A 1 164 ? 10.104 -8.140  -0.812  0.36 19.76 ?  164 LEU   A HD21 1 
ATOM   3716 H  HD22 A LEU   A 1 164 ? 9.983  -9.396  -0.279  0.64 20.45 ?  164 LEU   A HD22 1 
ATOM   3717 H  HD22 B LEU   A 1 164 ? 10.142 -9.361  0.204   0.36 19.76 ?  164 LEU   A HD22 1 
ATOM   3718 H  HD23 A LEU   A 1 164 ? 8.732  -9.238  -1.245  0.64 20.45 ?  164 LEU   A HD23 1 
ATOM   3719 H  HD23 B LEU   A 1 164 ? 8.969  -9.250  -0.860  0.36 19.76 ?  164 LEU   A HD23 1 
ATOM   3720 N  N    A VAL   A 1 165 ? 5.506  -10.541 2.677   0.64 16.14 ?  165 VAL   A N    1 
ATOM   3721 N  N    B VAL   A 1 165 ? 5.613  -10.445 2.972   0.36 17.58 ?  165 VAL   A N    1 
ATOM   3722 C  CA   A VAL   A 1 165 ? 5.031  -11.617 3.544   0.64 15.89 ?  165 VAL   A CA   1 
ATOM   3723 C  CA   B VAL   A 1 165 ? 5.146  -11.484 3.882   0.36 17.69 ?  165 VAL   A CA   1 
ATOM   3724 C  C    A VAL   A 1 165 ? 4.006  -12.469 2.811   0.64 16.31 ?  165 VAL   A C    1 
ATOM   3725 C  C    B VAL   A 1 165 ? 4.101  -12.357 3.202   0.36 17.44 ?  165 VAL   A C    1 
ATOM   3726 O  O    A VAL   A 1 165 ? 4.117  -13.700 2.755   0.64 15.99 ?  165 VAL   A O    1 
ATOM   3727 O  O    B VAL   A 1 165 ? 4.168  -13.591 3.257   0.36 16.86 ?  165 VAL   A O    1 
ATOM   3728 C  CB   A VAL   A 1 165 ? 4.450  -11.028 4.843   0.64 16.31 ?  165 VAL   A CB   1 
ATOM   3729 C  CB   B VAL   A 1 165 ? 4.609  -10.857 5.181   0.36 18.20 ?  165 VAL   A CB   1 
ATOM   3730 C  CG1  A VAL   A 1 165 ? 3.698  -12.097 5.634   0.64 16.31 ?  165 VAL   A CG1  1 
ATOM   3731 C  CG1  B VAL   A 1 165 ? 3.898  -11.910 6.023   0.36 18.41 ?  165 VAL   A CG1  1 
ATOM   3732 C  CG2  A VAL   A 1 165 ? 5.553  -10.391 5.680   0.64 16.74 ?  165 VAL   A CG2  1 
ATOM   3733 C  CG2  B VAL   A 1 165 ? 5.741  -10.205 5.962   0.36 18.52 ?  165 VAL   A CG2  1 
ATOM   3734 H  H    A VAL   A 1 165 ? 5.304  -9.752  2.951   0.64 19.38 ?  165 VAL   A H    1 
ATOM   3735 H  H    B VAL   A 1 165 ? 5.408  -9.642  3.206   0.36 21.10 ?  165 VAL   A H    1 
ATOM   3736 H  HA   A VAL   A 1 165 ? 5.779  -12.186 3.781   0.64 19.08 ?  165 VAL   A HA   1 
ATOM   3737 H  HA   B VAL   A 1 165 ? 5.894  -12.049 4.116   0.36 21.24 ?  165 VAL   A HA   1 
ATOM   3738 H  HB   A VAL   A 1 165 ? 3.817  -10.333 4.615   0.64 19.58 ?  165 VAL   A HB   1 
ATOM   3739 H  HB   B VAL   A 1 165 ? 3.965  -10.166 4.959   0.36 21.84 ?  165 VAL   A HB   1 
ATOM   3740 H  HG11 A VAL   A 1 165 ? 3.591  -11.793 6.549   0.64 19.58 ?  165 VAL   A HG11 1 
ATOM   3741 H  HG11 B VAL   A 1 165 ? 3.820  -11.584 6.933   0.36 22.10 ?  165 VAL   A HG11 1 
ATOM   3742 H  HG12 A VAL   A 1 165 ? 2.826  -12.235 5.231   0.64 19.58 ?  165 VAL   A HG12 1 
ATOM   3743 H  HG12 B VAL   A 1 165 ? 3.014  -12.068 5.654   0.36 22.10 ?  165 VAL   A HG12 1 
ATOM   3744 H  HG13 A VAL   A 1 165 ? 4.207  -12.921 5.618   0.64 19.58 ?  165 VAL   A HG13 1 
ATOM   3745 H  HG13 B VAL   A 1 165 ? 4.417  -12.728 6.009   0.36 22.10 ?  165 VAL   A HG13 1 
ATOM   3746 H  HG21 A VAL   A 1 165 ? 5.167  -10.038 6.498   0.64 20.09 ?  165 VAL   A HG21 1 
ATOM   3747 H  HG21 B VAL   A 1 165 ? 5.383  -9.822  6.778   0.36 22.23 ?  165 VAL   A HG21 1 
ATOM   3748 H  HG22 A VAL   A 1 165 ? 6.220  -11.063 5.893   0.64 20.09 ?  165 VAL   A HG22 1 
ATOM   3749 H  HG22 B VAL   A 1 165 ? 6.405  -10.879 6.176   0.36 22.23 ?  165 VAL   A HG22 1 
ATOM   3750 H  HG23 A VAL   A 1 165 ? 5.960  -9.672  5.171   0.64 20.09 ?  165 VAL   A HG23 1 
ATOM   3751 H  HG23 B VAL   A 1 165 ? 6.139  -9.508  5.417   0.36 22.23 ?  165 VAL   A HG23 1 
ATOM   3752 N  N    A SER   A 1 166 ? 2.991  -11.822 2.238   0.64 17.00 ?  166 SER   A N    1 
ATOM   3753 N  N    B SER   A 1 166 ? 3.126  -11.731 2.540   0.36 17.81 ?  166 SER   A N    1 
ATOM   3754 C  CA   A SER   A 1 166 ? 1.891  -12.557 1.625   0.64 17.99 ?  166 SER   A CA   1 
ATOM   3755 C  CA   B SER   A 1 166 ? 1.971  -12.481 2.064   0.36 18.24 ?  166 SER   A CA   1 
ATOM   3756 C  C    A SER   A 1 166 ? 2.355  -13.360 0.422   0.64 18.65 ?  166 SER   A C    1 
ATOM   3757 C  C    B SER   A 1 166 ? 2.314  -13.469 0.956   0.36 18.53 ?  166 SER   A C    1 
ATOM   3758 O  O    A SER   A 1 166 ? 1.739  -14.379 0.086   0.64 20.02 ?  166 SER   A O    1 
ATOM   3759 O  O    B SER   A 1 166 ? 1.554  -14.415 0.742   0.36 19.01 ?  166 SER   A O    1 
ATOM   3760 C  CB   A SER   A 1 166 ? 0.776  -11.591 1.210   0.64 18.70 ?  166 SER   A CB   1 
ATOM   3761 C  CB   B SER   A 1 166 ? 0.853  -11.531 1.616   0.36 18.59 ?  166 SER   A CB   1 
ATOM   3762 O  OG   A SER   A 1 166 ? 0.180  -10.964 2.335   0.64 19.39 ?  166 SER   A OG   1 
ATOM   3763 O  OG   B SER   A 1 166 ? 1.181  -10.863 0.411   0.36 18.98 ?  166 SER   A OG   1 
ATOM   3764 H  H    A SER   A 1 166 ? 2.910  -10.971 2.203   0.64 20.41 ?  166 SER   A H    1 
ATOM   3765 H  H    B SER   A 1 166 ? 3.104  -10.886 2.367   0.36 21.38 ?  166 SER   A H    1 
ATOM   3766 H  HA   A SER   A 1 166 ? 1.516  -13.179 2.271   0.64 21.60 ?  166 SER   A HA   1 
ATOM   3767 H  HA   B SER   A 1 166 ? 1.619  -12.995 2.804   0.36 21.90 ?  166 SER   A HA   1 
ATOM   3768 H  HB2  A SER   A 1 166 ? 1.147  -10.917 0.622   0.64 22.45 ?  166 SER   A HB2  1 
ATOM   3769 H  HB2  B SER   A 1 166 ? 0.044  -12.045 1.463   0.36 22.31 ?  166 SER   A HB2  1 
ATOM   3770 H  HB3  A SER   A 1 166 ? 0.082  -12.087 0.748   0.64 22.45 ?  166 SER   A HB3  1 
ATOM   3771 H  HB3  B SER   A 1 166 ? 0.693  -10.876 2.319   0.36 22.31 ?  166 SER   A HB3  1 
ATOM   3772 H  HG   A SER   A 1 166 ? -0.407 -10.420 2.089   0.64 23.27 ?  166 SER   A HG   1 
ATOM   3773 H  HG   B SER   A 1 166 ? 0.567  -10.331 0.200   0.36 22.79 ?  166 SER   A HG   1 
ATOM   3774 N  N    A SER   A 1 167 ? 3.420  -12.921 -0.242  0.64 17.42 ?  167 SER   A N    1 
ATOM   3775 N  N    B SER   A 1 167 ? 3.443  -13.306 0.266   0.36 18.98 ?  167 SER   A N    1 
ATOM   3776 C  CA   A SER   A 1 167 ? 3.918  -13.623 -1.413  0.64 17.99 ?  167 SER   A CA   1 
ATOM   3777 C  CA   B SER   A 1 167 ? 3.737  -14.120 -0.909  0.36 19.55 ?  167 SER   A CA   1 
ATOM   3778 C  C    A SER   A 1 167 ? 5.045  -14.591 -1.087  0.64 18.49 ?  167 SER   A C    1 
ATOM   3779 C  C    B SER   A 1 167 ? 4.983  -14.982 -0.724  0.36 19.58 ?  167 SER   A C    1 
ATOM   3780 O  O    A SER   A 1 167 ? 5.490  -15.320 -1.981  0.64 19.66 ?  167 SER   A O    1 
ATOM   3781 O  O    B SER   A 1 167 ? 5.654  -15.326 -1.699  0.36 20.35 ?  167 SER   A O    1 
ATOM   3782 C  CB   A SER   A 1 167 ? 4.372  -12.621 -2.486  0.64 17.92 ?  167 SER   A CB   1 
ATOM   3783 C  CB   B SER   A 1 167 ? 3.883  -13.244 -2.152  0.36 20.41 ?  167 SER   A CB   1 
ATOM   3784 O  OG   A SER   A 1 167 ? 5.420  -11.793 -1.996  0.64 18.34 ?  167 SER   A OG   1 
ATOM   3785 O  OG   B SER   A 1 167 ? 5.016  -12.400 -2.048  0.36 21.22 ?  167 SER   A OG   1 
ATOM   3786 H  H    A SER   A 1 167 ? 3.856  -12.206 -0.043  0.64 20.92 ?  167 SER   A H    1 
ATOM   3787 H  H    B SER   A 1 167 ? 4.057  -12.738 0.470   0.36 22.78 ?  167 SER   A H    1 
ATOM   3788 H  HA   A SER   A 1 167 ? 3.196  -14.138 -1.797  0.64 21.59 ?  167 SER   A HA   1 
ATOM   3789 H  HA   B SER   A 1 167 ? 2.984  -14.718 -1.058  0.36 23.46 ?  167 SER   A HA   1 
ATOM   3790 H  HB2  A SER   A 1 167 ? 4.694  -13.108 -3.261  0.64 21.51 ?  167 SER   A HB2  1 
ATOM   3791 H  HB2  B SER   A 1 167 ? 3.981  -13.819 -2.925  0.36 24.50 ?  167 SER   A HB2  1 
ATOM   3792 H  HB3  A SER   A 1 167 ? 3.607  -12.069 -2.749  0.64 21.51 ?  167 SER   A HB3  1 
ATOM   3793 H  HB3  B SER   A 1 167 ? 3.085  -12.699 -2.242  0.36 24.50 ?  167 SER   A HB3  1 
ATOM   3794 H  HG   A SER   A 1 167 ? 5.130  -11.337 -1.345  0.64 22.02 ?  167 SER   A HG   1 
ATOM   3795 H  HG   B SER   A 1 167 ? 4.935  -11.907 -1.371  0.36 25.47 ?  167 SER   A HG   1 
ATOM   3796 N  N    A PHE   A 1 168 ? 5.503  -14.638 0.164   0.64 17.70 ?  168 PHE   A N    1 
ATOM   3797 N  N    B PHE   A 1 168 ? 5.298  -15.358 0.515   0.36 19.04 ?  168 PHE   A N    1 
ATOM   3798 C  CA   A PHE   A 1 168 ? 6.668  -15.453 0.479   0.64 18.37 ?  168 PHE   A CA   1 
ATOM   3799 C  CA   B PHE   A 1 168 ? 6.573  -16.008 0.790   0.36 18.75 ?  168 PHE   A CA   1 
ATOM   3800 C  C    A PHE   A 1 168 ? 6.331  -16.932 0.381   0.64 20.07 ?  168 PHE   A C    1 
ATOM   3801 C  C    B PHE   A 1 168 ? 6.542  -17.521 0.592   0.36 19.46 ?  168 PHE   A C    1 
ATOM   3802 O  O    A PHE   A 1 168 ? 5.338  -17.398 0.951   0.64 21.55 ?  168 PHE   A O    1 
ATOM   3803 O  O    B PHE   A 1 168 ? 7.478  -18.086 0.021   0.36 18.55 ?  168 PHE   A O    1 
ATOM   3804 C  CB   A PHE   A 1 168 ? 7.208  -15.160 1.875   0.64 17.62 ?  168 PHE   A CB   1 
ATOM   3805 C  CB   B PHE   A 1 168 ? 7.032  -15.676 2.212   0.36 18.44 ?  168 PHE   A CB   1 
ATOM   3806 C  CG   A PHE   A 1 168 ? 8.440  -15.962 2.200   0.64 17.05 ?  168 PHE   A CG   1 
ATOM   3807 C  CG   B PHE   A 1 168 ? 8.400  -16.182 2.528   0.36 18.29 ?  168 PHE   A CG   1 
ATOM   3808 C  CD1  A PHE   A 1 168 ? 9.644  -15.665 1.588   0.64 17.31 ?  168 PHE   A CD1  1 
ATOM   3809 C  CD1  B PHE   A 1 168 ? 9.510  -15.620 1.923   0.36 18.49 ?  168 PHE   A CD1  1 
ATOM   3810 C  CD2  A PHE   A 1 168 ? 8.389  -17.036 3.076   0.64 16.89 ?  168 PHE   A CD2  1 
ATOM   3811 C  CD2  B PHE   A 1 168 ? 8.582  -17.223 3.420   0.36 18.05 ?  168 PHE   A CD2  1 
ATOM   3812 C  CE1  A PHE   A 1 168 ? 10.779 -16.406 1.858   0.64 16.92 ?  168 PHE   A CE1  1 
ATOM   3813 C  CE1  B PHE   A 1 168 ? 10.775 -16.084 2.205   0.36 18.28 ?  168 PHE   A CE1  1 
ATOM   3814 C  CE2  A PHE   A 1 168 ? 9.530  -17.777 3.353   0.64 17.01 ?  168 PHE   A CE2  1 
ATOM   3815 C  CE2  B PHE   A 1 168 ? 9.845  -17.689 3.707   0.36 17.74 ?  168 PHE   A CE2  1 
ATOM   3816 C  CZ   A PHE   A 1 168 ? 10.723 -17.457 2.742   0.64 16.93 ?  168 PHE   A CZ   1 
ATOM   3817 C  CZ   B PHE   A 1 168 ? 10.942 -17.120 3.098   0.36 18.00 ?  168 PHE   A CZ   1 
ATOM   3818 H  H    A PHE   A 1 168 ? 5.161  -14.210 0.830   0.64 21.24 ?  168 PHE   A H    1 
ATOM   3819 H  H    B PHE   A 1 168 ? 4.803  -15.248 1.212   0.36 22.85 ?  168 PHE   A H    1 
ATOM   3820 H  HA   A PHE   A 1 168 ? 7.368  -15.255 -0.163  0.64 22.05 ?  168 PHE   A HA   1 
ATOM   3821 H  HA   B PHE   A 1 168 ? 7.236  -15.655 0.180   0.36 22.52 ?  168 PHE   A HA   1 
ATOM   3822 H  HB2  A PHE   A 1 168 ? 7.434  -14.219 1.936   0.64 21.15 ?  168 PHE   A HB2  1 
ATOM   3823 H  HB2  B PHE   A 1 168 ? 7.042  -14.712 2.324   0.36 22.14 ?  168 PHE   A HB2  1 
ATOM   3824 H  HB3  A PHE   A 1 168 ? 6.522  -15.378 2.528   0.64 21.15 ?  168 PHE   A HB3  1 
ATOM   3825 H  HB3  B PHE   A 1 168 ? 6.416  -16.074 2.849   0.36 22.14 ?  168 PHE   A HB3  1 
ATOM   3826 H  HD1  A PHE   A 1 168 ? 9.691  -14.955 0.990   0.64 20.78 ?  168 PHE   A HD1  1 
ATOM   3827 H  HD1  B PHE   A 1 168 ? 9.402  -14.922 1.319   0.36 22.20 ?  168 PHE   A HD1  1 
ATOM   3828 H  HD2  A PHE   A 1 168 ? 7.586  -17.255 3.492   0.64 20.28 ?  168 PHE   A HD2  1 
ATOM   3829 H  HD2  B PHE   A 1 168 ? 7.846  -17.610 3.834   0.36 21.66 ?  168 PHE   A HD2  1 
ATOM   3830 H  HE1  A PHE   A 1 168 ? 11.586 -16.192 1.447   0.64 20.31 ?  168 PHE   A HE1  1 
ATOM   3831 H  HE1  B PHE   A 1 168 ? 11.516 -15.698 1.793   0.36 21.95 ?  168 PHE   A HE1  1 
ATOM   3832 H  HE2  A PHE   A 1 168 ? 9.489  -18.493 3.947   0.64 20.42 ?  168 PHE   A HE2  1 
ATOM   3833 H  HE2  B PHE   A 1 168 ? 9.958  -18.387 4.309   0.36 21.30 ?  168 PHE   A HE2  1 
ATOM   3834 H  HZ   A PHE   A 1 168 ? 11.489 -17.957 2.923   0.64 20.32 ?  168 PHE   A HZ   1 
ATOM   3835 H  HZ   B PHE   A 1 168 ? 11.797 -17.432 3.289   0.36 21.62 ?  168 PHE   A HZ   1 
ATOM   3836 N  N    A LEU   A 1 169 ? 7.183  -17.675 -0.317  0.64 21.52 ?  169 LEU   A N    1 
ATOM   3837 N  N    B LEU   A 1 169 ? 5.501  -18.196 1.056   0.36 21.30 ?  169 LEU   A N    1 
ATOM   3838 C  CA   A LEU   A 1 169 ? 6.999  -19.110 -0.457  0.64 23.15 ?  169 LEU   A CA   1 
ATOM   3839 C  CA   B LEU   A 1 169 ? 5.474  -19.654 1.027   0.36 23.26 ?  169 LEU   A CA   1 
ATOM   3840 C  C    A LEU   A 1 169 ? 7.838  -19.861 0.572   0.64 22.95 ?  169 LEU   A C    1 
ATOM   3841 C  C    B LEU   A 1 169 ? 4.932  -20.188 -0.292  0.36 24.49 ?  169 LEU   A C    1 
ATOM   3842 O  O    A LEU   A 1 169 ? 7.292  -20.365 1.559   0.64 23.10 ?  169 LEU   A O    1 
ATOM   3843 O  O    B LEU   A 1 169 ? 4.036  -19.598 -0.891  0.36 24.93 ?  169 LEU   A O    1 
ATOM   3844 C  CB   A LEU   A 1 169 ? 7.344  -19.560 -1.880  0.64 24.40 ?  169 LEU   A CB   1 
ATOM   3845 C  CB   B LEU   A 1 169 ? 4.596  -20.151 2.160   0.36 23.83 ?  169 LEU   A CB   1 
ATOM   3846 C  CG   A LEU   A 1 169 ? 7.062  -21.028 -2.220  0.64 25.71 ?  169 LEU   A CG   1 
ATOM   3847 C  CG   B LEU   A 1 169 ? 5.003  -21.397 2.927   0.36 24.14 ?  169 LEU   A CG   1 
ATOM   3848 C  CD1  A LEU   A 1 169 ? 5.646  -21.422 -1.830  0.64 26.15 ?  169 LEU   A CD1  1 
ATOM   3849 C  CD1  B LEU   A 1 169 ? 3.990  -21.522 4.023   0.36 24.34 ?  169 LEU   A CD1  1 
ATOM   3850 C  CD2  A LEU   A 1 169 ? 7.292  -21.295 -3.703  0.64 26.06 ?  169 LEU   A CD2  1 
ATOM   3851 C  CD2  B LEU   A 1 169 ? 5.022  -22.637 2.046   0.36 24.33 ?  169 LEU   A CD2  1 
ATOM   3852 O  OXT  A LEU   A 1 169 ? 9.062  -19.973 0.454   0.64 22.43 -1 169 LEU   A OXT  1 
ATOM   3853 O  OXT  B LEU   A 1 169 ? 5.367  -21.232 -0.779  0.36 25.19 -1 169 LEU   A OXT  1 
ATOM   3854 H  H    A LEU   A 1 169 ? 7.882  -17.365 -0.720  0.64 25.83 ?  169 LEU   A H    1 
ATOM   3855 H  H    B LEU   A 1 169 ? 4.801  -17.833 1.396   0.36 25.57 ?  169 LEU   A H    1 
ATOM   3856 H  HA   A LEU   A 1 169 ? 6.073  -19.322 -0.288  0.64 27.79 ?  169 LEU   A HA   1 
ATOM   3857 H  HA   B LEU   A 1 169 ? 6.372  -20.002 1.152   0.36 27.92 ?  169 LEU   A HA   1 
ATOM   3858 H  HB2  A LEU   A 1 169 ? 6.829  -19.022 -2.502  0.64 29.29 ?  169 LEU   A HB2  1 
ATOM   3859 H  HB2  B LEU   A 1 169 ? 4.535  -19.438 2.808   0.36 28.61 ?  169 LEU   A HB2  1 
ATOM   3860 H  HB3  A LEU   A 1 169 ? 8.288  -19.410 -2.031  0.64 29.29 ?  169 LEU   A HB3  1 
ATOM   3861 H  HB3  B LEU   A 1 169 ? 3.718  -20.332 1.795   0.36 28.61 ?  169 LEU   A HB3  1 
ATOM   3862 H  HG   A LEU   A 1 169 ? 7.674  -21.592 -1.722  0.64 30.86 ?  169 LEU   A HG   1 
ATOM   3863 H  HG   B LEU   A 1 169 ? 5.884  -21.276 3.321   0.36 28.98 ?  169 LEU   A HG   1 
ATOM   3864 H  HD11 A LEU   A 1 169 ? 5.440  -22.289 -2.216  0.64 31.39 ?  169 LEU   A HD11 1 
ATOM   3865 H  HD11 B LEU   A 1 169 ? 4.448  -21.551 4.873   0.36 29.21 ?  169 LEU   A HD11 1 
ATOM   3866 H  HD12 A LEU   A 1 169 ? 5.586  -21.470 -0.863  0.64 31.39 ?  169 LEU   A HD12 1 
ATOM   3867 H  HD12 B LEU   A 1 169 ? 3.396  -20.754 3.987   0.36 29.21 ?  169 LEU   A HD12 1 
ATOM   3868 H  HD13 A LEU   A 1 169 ? 5.027  -20.756 -2.169  0.64 31.39 ?  169 LEU   A HD13 1 
ATOM   3869 H  HD13 B LEU   A 1 169 ? 3.482  -22.325 3.876   0.36 29.21 ?  169 LEU   A HD13 1 
ATOM   3870 H  HD21 A LEU   A 1 169 ? 7.113  -22.231 -3.888  0.64 31.28 ?  169 LEU   A HD21 1 
ATOM   3871 H  HD21 B LEU   A 1 169 ? 5.368  -23.386 2.558   0.36 29.21 ?  169 LEU   A HD21 1 
ATOM   3872 H  HD22 A LEU   A 1 169 ? 6.691  -20.736 -4.221  0.64 31.28 ?  169 LEU   A HD22 1 
ATOM   3873 H  HD22 B LEU   A 1 169 ? 4.117  -22.829 1.755   0.36 29.21 ?  169 LEU   A HD22 1 
ATOM   3874 H  HD23 A LEU   A 1 169 ? 8.212  -21.085 -3.923  0.64 31.28 ?  169 LEU   A HD23 1 
ATOM   3875 H  HD23 B LEU   A 1 169 ? 5.589  -22.472 1.277   0.36 29.21 ?  169 LEU   A HD23 1 
ATOM   3876 N  N    A SER   B 1 1   ? 50.789 -9.265  -23.702 0.64 27.49 ?  1   SER   B N    1 
ATOM   3877 N  N    B SER   B 1 1   ? 50.721 -9.257  -23.680 0.36 26.24 ?  1   SER   B N    1 
ATOM   3878 C  CA   A SER   B 1 1   ? 51.285 -10.312 -22.784 0.64 27.93 ?  1   SER   B CA   1 
ATOM   3879 C  CA   B SER   B 1 1   ? 51.228 -10.253 -22.712 0.36 26.31 ?  1   SER   B CA   1 
ATOM   3880 C  C    A SER   B 1 1   ? 50.202 -11.345 -22.497 0.64 27.12 ?  1   SER   B C    1 
ATOM   3881 C  C    B SER   B 1 1   ? 50.183 -11.327 -22.461 0.36 25.53 ?  1   SER   B C    1 
ATOM   3882 O  O    A SER   B 1 1   ? 49.007 -11.120 -22.734 0.64 26.95 ?  1   SER   B O    1 
ATOM   3883 O  O    B SER   B 1 1   ? 48.986 -11.134 -22.704 0.36 25.44 ?  1   SER   B O    1 
ATOM   3884 C  CB   A SER   B 1 1   ? 51.760 -9.700  -21.470 0.64 28.66 ?  1   SER   B CB   1 
ATOM   3885 C  CB   B SER   B 1 1   ? 51.595 -9.586  -21.392 0.36 26.75 ?  1   SER   B CB   1 
ATOM   3886 O  OG   A SER   B 1 1   ? 50.662 -9.410  -20.626 0.64 30.40 ?  1   SER   B OG   1 
ATOM   3887 O  OG   B SER   B 1 1   ? 50.450 -9.436  -20.572 0.36 27.84 ?  1   SER   B OG   1 
ATOM   3888 H  H1   A SER   B 1 1   ? 50.627 -9.628  -24.497 0.64 33.00 ?  1   SER   B H1   1 
ATOM   3889 H  H1   B SER   B 1 1   ? 50.561 -9.661  -24.455 0.36 31.50 ?  1   SER   B H1   1 
ATOM   3890 H  H2   A SER   B 1 1   ? 50.046 -8.918  -23.369 0.64 33.00 ?  1   SER   B H2   1 
ATOM   3891 H  H2   B SER   B 1 1   ? 49.974 -8.901  -23.364 0.36 31.50 ?  1   SER   B H2   1 
ATOM   3892 H  H3   A SER   B 1 1   ? 51.411 -8.635  -23.782 0.64 33.00 ?  1   SER   B H3   1 
ATOM   3893 H  H3   B SER   B 1 1   ? 51.336 -8.626  -23.791 0.36 31.50 ?  1   SER   B H3   1 
ATOM   3894 H  HA   A SER   B 1 1   ? 52.039 -10.748 -23.210 0.64 33.53 ?  1   SER   B HA   1 
ATOM   3895 H  HA   B SER   B 1 1   ? 52.021 -10.663 -23.085 0.36 31.59 ?  1   SER   B HA   1 
ATOM   3896 H  HB2  A SER   B 1 1   ? 52.337 -10.339 -21.027 0.64 34.40 ?  1   SER   B HB2  1 
ATOM   3897 H  HB2  B SER   B 1 1   ? 52.247 -10.142 -20.938 0.36 32.11 ?  1   SER   B HB2  1 
ATOM   3898 H  HB3  A SER   B 1 1   ? 52.245 -8.883  -21.656 0.64 34.40 ?  1   SER   B HB3  1 
ATOM   3899 H  HB3  B SER   B 1 1   ? 51.969 -8.711  -21.571 0.36 32.11 ?  1   SER   B HB3  1 
ATOM   3900 H  HG   A SER   B 1 1   ? 50.929 -8.981  -19.955 0.64 36.49 ?  1   SER   B HG   1 
ATOM   3901 H  HG   B SER   B 1 1   ? 50.626 -8.920  -19.934 0.36 33.42 ?  1   SER   B HG   1 
ATOM   3902 N  N    A MET   B 1 2   ? 50.641 -12.475 -21.958 0.64 26.51 ?  2   MET   B N    1 
ATOM   3903 N  N    B MET   B 1 2   ? 50.649 -12.460 -21.955 0.36 24.77 ?  2   MET   B N    1 
ATOM   3904 C  CA   A MET   B 1 2   ? 49.813 -13.664 -21.804 0.64 26.72 ?  2   MET   B CA   1 
ATOM   3905 C  CA   B MET   B 1 2   ? 49.827 -13.648 -21.777 0.36 24.46 ?  2   MET   B CA   1 
ATOM   3906 C  C    A MET   B 1 2   ? 49.557 -13.895 -20.321 0.64 24.45 ?  2   MET   B C    1 
ATOM   3907 C  C    B MET   B 1 2   ? 49.570 -13.834 -20.293 0.36 23.18 ?  2   MET   B C    1 
ATOM   3908 O  O    A MET   B 1 2   ? 50.474 -14.254 -19.577 0.64 25.03 ?  2   MET   B O    1 
ATOM   3909 O  O    B MET   B 1 2   ? 50.500 -14.090 -19.522 0.36 23.22 ?  2   MET   B O    1 
ATOM   3910 C  CB   A MET   B 1 2   ? 50.534 -14.857 -22.421 0.64 30.55 ?  2   MET   B CB   1 
ATOM   3911 C  CB   B MET   B 1 2   ? 50.555 -14.848 -22.352 0.36 26.32 ?  2   MET   B CB   1 
ATOM   3912 C  CG   A MET   B 1 2   ? 49.689 -16.111 -22.559 0.64 33.99 ?  2   MET   B CG   1 
ATOM   3913 C  CG   B MET   B 1 2   ? 49.661 -16.014 -22.750 0.36 27.75 ?  2   MET   B CG   1 
ATOM   3914 S  SD   A MET   B 1 2   ? 50.541 -17.362 -23.537 0.64 37.40 ?  2   MET   B SD   1 
ATOM   3915 S  SD   B MET   B 1 2   ? 50.532 -17.144 -23.844 0.36 29.11 ?  2   MET   B SD   1 
ATOM   3916 C  CE   A MET   B 1 2   ? 51.076 -16.354 -24.916 0.64 37.80 ?  2   MET   B CE   1 
ATOM   3917 C  CE   B MET   B 1 2   ? 51.644 -16.005 -24.643 0.36 29.50 ?  2   MET   B CE   1 
ATOM   3918 H  H    A MET   B 1 2   ? 51.444 -12.581 -21.666 0.64 31.82 ?  2   MET   B H    1 
ATOM   3919 H  H    B MET   B 1 2   ? 51.467 -12.574 -21.703 0.36 29.74 ?  2   MET   B H    1 
ATOM   3920 H  HA   A MET   B 1 2   ? 48.974 -13.545 -22.271 0.64 32.07 ?  2   MET   B HA   1 
ATOM   3921 H  HA   B MET   B 1 2   ? 48.994 -13.555 -22.262 0.36 29.36 ?  2   MET   B HA   1 
ATOM   3922 H  HB2  A MET   B 1 2   ? 50.831 -14.581 -23.298 0.64 36.67 ?  2   MET   B HB2  1 
ATOM   3923 H  HB2  B MET   B 1 2   ? 50.989 -14.474 -23.123 0.36 31.59 ?  2   MET   B HB2  1 
ATOM   3924 H  HB3  A MET   B 1 2   ? 51.299 -15.092 -21.877 0.64 36.67 ?  2   MET   B HB3  1 
ATOM   3925 H  HB3  B MET   B 1 2   ? 51.216 -15.195 -21.734 0.36 31.59 ?  2   MET   B HB3  1 
ATOM   3926 H  HG2  A MET   B 1 2   ? 49.512 -16.479 -21.676 0.64 40.80 ?  2   MET   B HG2  1 
ATOM   3927 H  HG2  B MET   B 1 2   ? 49.384 -16.504 -21.952 0.36 33.31 ?  2   MET   B HG2  1 
ATOM   3928 H  HG3  A MET   B 1 2   ? 48.855 -15.894 -23.005 0.64 40.80 ?  2   MET   B HG3  1 
ATOM   3929 H  HG3  B MET   B 1 2   ? 48.885 -15.691 -23.228 0.36 33.31 ?  2   MET   B HG3  1 
ATOM   3930 H  HE1  A MET   B 1 2   ? 51.245 -16.925 -25.670 0.64 45.36 ?  2   MET   B HE1  1 
ATOM   3931 H  HE1  B MET   B 1 2   ? 52.040 -16.469 -25.359 0.36 35.41 ?  2   MET   B HE1  1 
ATOM   3932 H  HE2  A MET   B 1 2   ? 50.372 -15.716 -25.127 0.64 45.36 ?  2   MET   B HE2  1 
ATOM   3933 H  HE2  B MET   B 1 2   ? 51.132 -15.244 -24.977 0.36 35.41 ?  2   MET   B HE2  1 
ATOM   3934 H  HE3  A MET   B 1 2   ? 51.887 -15.876 -24.668 0.64 45.36 ?  2   MET   B HE3  1 
ATOM   3935 H  HE3  B MET   B 1 2   ? 52.338 -15.709 -24.019 0.36 35.41 ?  2   MET   B HE3  1 
ATOM   3936 N  N    . VAL   B 1 3   ? 48.310 -13.691 -19.897 1.00 22.24 ?  3   VAL   B N    1 
ATOM   3937 C  CA   . VAL   B 1 3   ? 47.894 -13.927 -18.524 1.00 20.86 ?  3   VAL   B CA   1 
ATOM   3938 C  C    . VAL   B 1 3   ? 46.656 -14.813 -18.548 1.00 19.13 ?  3   VAL   B C    1 
ATOM   3939 O  O    . VAL   B 1 3   ? 45.924 -14.879 -19.537 1.00 19.72 ?  3   VAL   B O    1 
ATOM   3940 C  CB   . VAL   B 1 3   ? 47.614 -12.618 -17.754 1.00 22.50 ?  3   VAL   B CB   1 
ATOM   3941 C  CG1  . VAL   B 1 3   ? 48.889 -11.779 -17.624 1.00 23.04 ?  3   VAL   B CG1  1 
ATOM   3942 C  CG2  . VAL   B 1 3   ? 46.508 -11.831 -18.436 1.00 23.04 ?  3   VAL   B CG2  1 
ATOM   3943 H  H    A VAL   B 1 3   ? 47.673 -13.427 -20.412 0.64 26.69 ?  3   VAL   B H    1 
ATOM   3944 H  H    B VAL   B 1 3   ? 47.670 -13.452 -20.421 0.36 26.69 ?  3   VAL   B H    1 
ATOM   3945 H  HA   . VAL   B 1 3   ? 48.599 -14.406 -18.057 1.00 25.04 ?  3   VAL   B HA   1 
ATOM   3946 H  HB   . VAL   B 1 3   ? 47.314 -12.847 -16.860 1.00 27.00 ?  3   VAL   B HB   1 
ATOM   3947 H  HG11 . VAL   B 1 3   ? 48.679 -10.971 -17.131 1.00 27.66 ?  3   VAL   B HG11 1 
ATOM   3948 H  HG12 . VAL   B 1 3   ? 49.557 -12.295 -17.149 1.00 27.66 ?  3   VAL   B HG12 1 
ATOM   3949 H  HG13 . VAL   B 1 3   ? 49.207 -11.556 -18.511 1.00 27.66 ?  3   VAL   B HG13 1 
ATOM   3950 H  HG21 . VAL   B 1 3   ? 46.434 -10.966 -18.011 1.00 27.66 ?  3   VAL   B HG21 1 
ATOM   3951 H  HG22 . VAL   B 1 3   ? 46.726 -11.727 -19.374 1.00 27.66 ?  3   VAL   B HG22 1 
ATOM   3952 H  HG23 . VAL   B 1 3   ? 45.671 -12.317 -18.344 1.00 27.66 ?  3   VAL   B HG23 1 
ATOM   3953 N  N    . ASN   B 1 4   ? 46.433 -15.509 -17.437 1.00 17.18 ?  4   ASN   B N    1 
ATOM   3954 C  CA   . ASN   B 1 4   ? 45.298 -16.423 -17.313 1.00 16.01 ?  4   ASN   B CA   1 
ATOM   3955 C  C    . ASN   B 1 4   ? 45.235 -17.384 -18.497 1.00 16.25 ?  4   ASN   B C    1 
ATOM   3956 O  O    . ASN   B 1 4   ? 44.172 -17.629 -19.062 1.00 16.86 ?  4   ASN   B O    1 
ATOM   3957 C  CB   . ASN   B 1 4   ? 43.981 -15.656 -17.152 1.00 15.77 ?  4   ASN   B CB   1 
ATOM   3958 C  CG   . ASN   B 1 4   ? 43.941 -14.838 -15.876 1.00 15.09 ?  4   ASN   B CG   1 
ATOM   3959 O  OD1  . ASN   B 1 4   ? 44.222 -15.346 -14.793 1.00 14.85 ?  4   ASN   B OD1  1 
ATOM   3960 N  ND2  . ASN   B 1 4   ? 43.606 -13.560 -16.001 1.00 15.95 ?  4   ASN   B ND2  1 
ATOM   3961 H  H    . ASN   B 1 4   ? 46.933 -15.474 -16.742 1.00 20.63 ?  4   ASN   B H    1 
ATOM   3962 H  HA   . ASN   B 1 4   ? 45.425 -16.956 -16.514 1.00 19.22 ?  4   ASN   B HA   1 
ATOM   3963 H  HB2  . ASN   B 1 4   ? 43.874 -15.049 -17.902 1.00 18.94 ?  4   ASN   B HB2  1 
ATOM   3964 H  HB3  . ASN   B 1 4   ? 43.247 -16.289 -17.128 1.00 18.94 ?  4   ASN   B HB3  1 
ATOM   3965 H  HD21 . ASN   B 1 4   ? 43.580 -13.050 -15.304 1.00 19.15 ?  4   ASN   B HD21 1 
ATOM   3966 H  HD22 . ASN   B 1 4   ? 43.424 -13.230 -16.774 1.00 19.15 ?  4   ASN   B HD22 1 
ATOM   3967 N  N    . SER   B 1 5   ? 46.391 -17.927 -18.882 1.00 17.38 ?  5   SER   B N    1 
ATOM   3968 C  CA   . SER   B 1 5   ? 46.481 -18.848 -20.016 1.00 19.45 ?  5   SER   B CA   1 
ATOM   3969 C  C    . SER   B 1 5   ? 46.456 -20.267 -19.463 1.00 21.30 ?  5   SER   B C    1 
ATOM   3970 O  O    . SER   B 1 5   ? 47.475 -20.944 -19.357 1.00 23.49 ?  5   SER   B O    1 
ATOM   3971 C  CB   . SER   B 1 5   ? 47.743 -18.576 -20.833 1.00 21.06 ?  5   SER   B CB   1 
ATOM   3972 O  OG   . SER   B 1 5   ? 48.904 -18.688 -20.028 1.00 23.56 ?  5   SER   B OG   1 
ATOM   3973 H  H    . SER   B 1 5   ? 47.147 -17.775 -18.503 1.00 20.86 ?  5   SER   B H    1 
ATOM   3974 H  HA   . SER   B 1 5   ? 45.714 -18.732 -20.594 1.00 23.35 ?  5   SER   B HA   1 
ATOM   3975 H  HB2  . SER   B 1 5   ? 47.792 -19.220 -21.562 1.00 25.28 ?  5   SER   B HB2  1 
ATOM   3976 H  HB3  . SER   B 1 5   ? 47.687 -17.678 -21.195 1.00 25.28 ?  5   SER   B HB3  1 
ATOM   3977 H  HG   . SER   B 1 5   ? 48.970 -19.469 -19.730 1.00 28.28 ?  5   SER   B HG   1 
ATOM   3978 N  N    . PHE   B 1 6   ? 45.260 -20.701 -19.080 1.00 21.95 ?  6   PHE   B N    1 
ATOM   3979 C  CA   . PHE   B 1 6   ? 45.064 -22.041 -18.548 1.00 21.99 ?  6   PHE   B CA   1 
ATOM   3980 C  C    . PHE   B 1 6   ? 44.964 -23.028 -19.701 1.00 25.88 ?  6   PHE   B C    1 
ATOM   3981 O  O    . PHE   B 1 6   ? 44.253 -22.778 -20.679 1.00 27.92 ?  6   PHE   B O    1 
ATOM   3982 C  CB   . PHE   B 1 6   ? 43.783 -22.087 -17.718 1.00 19.79 ?  6   PHE   B CB   1 
ATOM   3983 C  CG   . PHE   B 1 6   ? 43.818 -21.221 -16.488 1.00 17.91 ?  6   PHE   B CG   1 
ATOM   3984 C  CD1  . PHE   B 1 6   ? 44.328 -21.710 -15.299 1.00 16.89 ?  6   PHE   B CD1  1 
ATOM   3985 C  CD2  . PHE   B 1 6   ? 43.338 -19.920 -16.524 1.00 17.29 ?  6   PHE   B CD2  1 
ATOM   3986 C  CE1  . PHE   B 1 6   ? 44.347 -20.920 -14.161 1.00 16.65 ?  6   PHE   B CE1  1 
ATOM   3987 C  CE2  . PHE   B 1 6   ? 43.367 -19.120 -15.396 1.00 17.79 ?  6   PHE   B CE2  1 
ATOM   3988 C  CZ   . PHE   B 1 6   ? 43.873 -19.617 -14.215 1.00 16.93 ?  6   PHE   B CZ   1 
ATOM   3989 H  H    . PHE   B 1 6   ? 44.538 -20.236 -19.125 1.00 26.35 ?  6   PHE   B H    1 
ATOM   3990 H  HA   . PHE   B 1 6   ? 45.811 -22.289 -17.987 1.00 26.40 ?  6   PHE   B HA   1 
ATOM   3991 H  HB2  . PHE   B 1 6   ? 43.041 -21.789 -18.270 1.00 23.75 ?  6   PHE   B HB2  1 
ATOM   3992 H  HB3  . PHE   B 1 6   ? 43.627 -23.002 -17.432 1.00 23.75 ?  6   PHE   B HB3  1 
ATOM   3993 H  HD1  . PHE   B 1 6   ? 44.655 -22.581 -15.261 1.00 20.28 ?  6   PHE   B HD1  1 
ATOM   3994 H  HD2  . PHE   B 1 6   ? 42.988 -19.585 -17.317 1.00 20.76 ?  6   PHE   B HD2  1 
ATOM   3995 H  HE1  . PHE   B 1 6   ? 44.703 -21.251 -13.367 1.00 19.99 ?  6   PHE   B HE1  1 
ATOM   3996 H  HE2  . PHE   B 1 6   ? 43.034 -18.253 -15.433 1.00 21.35 ?  6   PHE   B HE2  1 
ATOM   3997 H  HZ   . PHE   B 1 6   ? 43.892 -19.085 -13.452 1.00 20.32 ?  6   PHE   B HZ   1 
ATOM   3998 N  N    . SER   B 1 7   ? 45.688 -24.141 -19.593 1.00 27.58 ?  7   SER   B N    1 
ATOM   3999 C  CA   . SER   B 1 7   ? 45.759 -25.121 -20.667 1.00 30.96 ?  7   SER   B CA   1 
ATOM   4000 C  C    . SER   B 1 7   ? 45.689 -26.527 -20.093 1.00 29.50 ?  7   SER   B C    1 
ATOM   4001 O  O    . SER   B 1 7   ? 46.299 -26.821 -19.062 1.00 29.90 ?  7   SER   B O    1 
ATOM   4002 C  CB   . SER   B 1 7   ? 47.055 -24.957 -21.473 1.00 35.08 ?  7   SER   B CB   1 
ATOM   4003 O  OG   . SER   B 1 7   ? 47.012 -25.719 -22.667 1.00 37.48 ?  7   SER   B OG   1 
ATOM   4004 H  H    . SER   B 1 7   ? 46.157 -24.348 -18.899 1.00 33.11 ?  7   SER   B H    1 
ATOM   4005 H  HA   . SER   B 1 7   ? 45.010 -25.001 -21.265 1.00 37.16 ?  7   SER   B HA   1 
ATOM   4006 H  HB2  . SER   B 1 7   ? 47.170 -24.019 -21.697 1.00 42.10 ?  7   SER   B HB2  1 
ATOM   4007 H  HB3  . SER   B 1 7   ? 47.804 -25.261 -20.936 1.00 42.10 ?  7   SER   B HB3  1 
ATOM   4008 H  HG   . SER   B 1 7   ? 47.724 -25.612 -23.100 1.00 44.98 ?  7   SER   B HG   1 
ATOM   4009 N  N    . GLY   B 1 8   ? 44.948 -27.396 -20.777 1.00 28.87 ?  8   GLY   B N    1 
ATOM   4010 C  CA   . GLY   B 1 8   ? 44.894 -28.788 -20.399 1.00 27.82 ?  8   GLY   B CA   1 
ATOM   4011 C  C    . GLY   B 1 8   ? 43.979 -29.102 -19.244 1.00 25.96 ?  8   GLY   B C    1 
ATOM   4012 O  O    . GLY   B 1 8   ? 44.145 -30.151 -18.609 1.00 27.44 ?  8   GLY   B O    1 
ATOM   4013 H  H    . GLY   B 1 8   ? 44.478 -27.193 -21.465 1.00 34.65 ?  8   GLY   B H    1 
ATOM   4014 H  HA2  . GLY   B 1 8   ? 44.599 -29.309 -21.160 1.00 33.39 ?  8   GLY   B HA2  1 
ATOM   4015 H  HA3  . GLY   B 1 8   ? 45.780 -29.086 -20.152 1.00 33.39 ?  8   GLY   B HA3  1 
ATOM   4016 N  N    . TYR   B 1 9   ? 43.001 -28.245 -18.957 1.00 23.95 ?  9   TYR   B N    1 
ATOM   4017 C  CA   . TYR   B 1 9   ? 42.060 -28.525 -17.885 1.00 21.76 ?  9   TYR   B CA   1 
ATOM   4018 C  C    . TYR   B 1 9   ? 40.875 -29.326 -18.392 1.00 21.38 ?  9   TYR   B C    1 
ATOM   4019 O  O    . TYR   B 1 9   ? 40.450 -29.199 -19.544 1.00 23.17 ?  9   TYR   B O    1 
ATOM   4020 C  CB   . TYR   B 1 9   ? 41.555 -27.243 -17.232 1.00 21.14 ?  9   TYR   B CB   1 
ATOM   4021 C  CG   . TYR   B 1 9   ? 42.586 -26.616 -16.324 1.00 20.35 ?  9   TYR   B CG   1 
ATOM   4022 C  CD1  . TYR   B 1 9   ? 43.671 -25.931 -16.848 1.00 20.80 ?  9   TYR   B CD1  1 
ATOM   4023 C  CD2  . TYR   B 1 9   ? 42.487 -26.727 -14.945 1.00 19.72 ?  9   TYR   B CD2  1 
ATOM   4024 C  CE1  . TYR   B 1 9   ? 44.629 -25.373 -16.027 1.00 20.89 ?  9   TYR   B CE1  1 
ATOM   4025 C  CE2  . TYR   B 1 9   ? 43.441 -26.170 -14.112 1.00 19.85 ?  9   TYR   B CE2  1 
ATOM   4026 C  CZ   . TYR   B 1 9   ? 44.512 -25.488 -14.661 1.00 20.44 ?  9   TYR   B CZ   1 
ATOM   4027 O  OH   . TYR   B 1 9   ? 45.469 -24.933 -13.847 1.00 21.04 ?  9   TYR   B OH   1 
ATOM   4028 H  H    . TYR   B 1 9   ? 42.845 -27.511 -19.380 1.00 28.75 ?  9   TYR   B H    1 
ATOM   4029 H  HA   . TYR   B 1 9   ? 42.496 -29.053 -17.206 1.00 26.12 ?  9   TYR   B HA   1 
ATOM   4030 H  HB2  . TYR   B 1 9   ? 41.317 -26.597 -17.917 1.00 25.38 ?  9   TYR   B HB2  1 
ATOM   4031 H  HB3  . TYR   B 1 9   ? 40.780 -27.462 -16.695 1.00 25.38 ?  9   TYR   B HB3  1 
ATOM   4032 H  HD1  . TYR   B 1 9   ? 43.753 -25.855 -17.772 1.00 24.97 ?  9   TYR   B HD1  1 
ATOM   4033 H  HD2  . TYR   B 1 9   ? 41.761 -27.195 -14.577 1.00 23.67 ?  9   TYR   B HD2  1 
ATOM   4034 H  HE1  . TYR   B 1 9   ? 45.341 -24.919 -16.396 1.00 25.08 ?  9   TYR   B HE1  1 
ATOM   4035 H  HE2  . TYR   B 1 9   ? 43.349 -26.260 -13.191 1.00 23.83 ?  9   TYR   B HE2  1 
ATOM   4036 H  HH   . TYR   B 1 9   ? 46.042 -24.554 -14.315 1.00 25.26 ?  9   TYR   B HH   1 
ATOM   4037 N  N    . LEU   B 1 10  ? 40.359 -30.176 -17.511 1.00 20.08 ?  10  LEU   B N    1 
ATOM   4038 C  CA   . LEU   B 1 10  ? 39.152 -30.940 -17.765 1.00 19.76 ?  10  LEU   B CA   1 
ATOM   4039 C  C    . LEU   B 1 10  ? 37.970 -30.165 -17.201 1.00 19.50 ?  10  LEU   B C    1 
ATOM   4040 O  O    . LEU   B 1 10  ? 37.992 -29.742 -16.041 1.00 19.37 ?  10  LEU   B O    1 
ATOM   4041 C  CB   . LEU   B 1 10  ? 39.257 -32.302 -17.081 1.00 20.76 ?  10  LEU   B CB   1 
ATOM   4042 C  CG   . LEU   B 1 10  ? 38.117 -33.265 -17.396 1.00 22.49 ?  10  LEU   B CG   1 
ATOM   4043 C  CD1  . LEU   B 1 10  ? 38.237 -33.770 -18.826 1.00 23.62 ?  10  LEU   B CD1  1 
ATOM   4044 C  CD2  . LEU   B 1 10  ? 38.096 -34.421 -16.411 1.00 23.74 ?  10  LEU   B CD2  1 
ATOM   4045 H  H    . LEU   B 1 10  ? 40.697 -30.332 -16.733 1.00 24.11 ?  10  LEU   B H    1 
ATOM   4046 H  HA   . LEU   B 1 10  ? 39.024 -31.072 -18.716 1.00 23.73 ?  10  LEU   B HA   1 
ATOM   4047 H  HB2  . LEU   B 1 10  ? 40.083 -32.729 -17.360 1.00 24.93 ?  10  LEU   B HB2  1 
ATOM   4048 H  HB3  . LEU   B 1 10  ? 39.268 -32.172 -16.119 1.00 24.93 ?  10  LEU   B HB3  1 
ATOM   4049 H  HG   . LEU   B 1 10  ? 37.271 -32.795 -17.317 1.00 27.00 ?  10  LEU   B HG   1 
ATOM   4050 H  HD11 . LEU   B 1 10  ? 37.553 -34.437 -18.984 1.00 28.35 ?  10  LEU   B HD11 1 
ATOM   4051 H  HD12 . LEU   B 1 10  ? 38.117 -33.022 -19.434 1.00 28.35 ?  10  LEU   B HD12 1 
ATOM   4052 H  HD13 . LEU   B 1 10  ? 39.116 -34.159 -18.950 1.00 28.35 ?  10  LEU   B HD13 1 
ATOM   4053 H  HD21 . LEU   B 1 10  ? 37.364 -35.014 -16.640 1.00 28.50 ?  10  LEU   B HD21 1 
ATOM   4054 H  HD22 . LEU   B 1 10  ? 38.939 -34.893 -16.466 1.00 28.50 ?  10  LEU   B HD22 1 
ATOM   4055 H  HD23 . LEU   B 1 10  ? 37.969 -34.066 -15.518 1.00 28.50 ?  10  LEU   B HD23 1 
ATOM   4056 N  N    . LYS   B 1 11  ? 36.945 -29.984 -18.025 1.00 20.71 ?  11  LYS   B N    1 
ATOM   4057 C  CA   . LYS   B 1 11  ? 35.744 -29.274 -17.611 1.00 22.83 ?  11  LYS   B CA   1 
ATOM   4058 C  C    . LYS   B 1 11  ? 34.886 -30.200 -16.753 1.00 21.61 ?  11  LYS   B C    1 
ATOM   4059 O  O    . LYS   B 1 11  ? 34.529 -31.303 -17.186 1.00 23.39 ?  11  LYS   B O    1 
ATOM   4060 C  CB   . LYS   B 1 11  ? 34.984 -28.831 -18.861 1.00 27.12 ?  11  LYS   B CB   1 
ATOM   4061 C  CG   . LYS   B 1 11  ? 33.858 -27.844 -18.625 1.00 30.82 ?  11  LYS   B CG   1 
ATOM   4062 C  CD   . LYS   B 1 11  ? 33.137 -27.539 -19.934 1.00 33.68 ?  11  LYS   B CD   1 
ATOM   4063 C  CE   . LYS   B 1 11  ? 32.102 -26.439 -19.769 1.00 35.76 ?  11  LYS   B CE   1 
ATOM   4064 N  NZ   . LYS   B 1 11  ? 32.731 -25.109 -19.550 1.00 36.83 ?  11  LYS   B NZ   1 
ATOM   4065 H  H    . LYS   B 1 11  ? 36.916 -30.268 -18.839 1.00 24.87 ?  11  LYS   B H    1 
ATOM   4066 H  HA   . LYS   B 1 11  ? 35.984 -28.488 -17.095 1.00 27.40 ?  11  LYS   B HA   1 
ATOM   4067 H  HB2  . LYS   B 1 11  ? 35.612 -28.408 -19.471 1.00 32.55 ?  11  LYS   B HB2  1 
ATOM   4068 H  HB3  . LYS   B 1 11  ? 34.600 -29.612 -19.284 1.00 32.55 ?  11  LYS   B HB3  1 
ATOM   4069 H  HG2  . LYS   B 1 11  ? 33.219 -28.226 -18.006 1.00 36.99 ?  11  LYS   B HG2  1 
ATOM   4070 H  HG3  . LYS   B 1 11  ? 34.220 -27.016 -18.275 1.00 36.99 ?  11  LYS   B HG3  1 
ATOM   4071 H  HD2  . LYS   B 1 11  ? 33.786 -27.249 -20.595 1.00 40.43 ?  11  LYS   B HD2  1 
ATOM   4072 H  HD3  . LYS   B 1 11  ? 32.684 -28.340 -20.242 1.00 40.43 ?  11  LYS   B HD3  1 
ATOM   4073 H  HE2  . LYS   B 1 11  ? 31.560 -26.390 -20.572 1.00 42.92 ?  11  LYS   B HE2  1 
ATOM   4074 H  HE3  . LYS   B 1 11  ? 31.545 -26.645 -19.002 1.00 42.92 ?  11  LYS   B HE3  1 
ATOM   4075 H  HZ1  . LYS   B 1 11  ? 32.102 -24.484 -19.474 1.00 44.20 ?  11  LYS   B HZ1  1 
ATOM   4076 H  HZ2  . LYS   B 1 11  ? 33.219 -25.122 -18.807 1.00 44.20 ?  11  LYS   B HZ2  1 
ATOM   4077 H  HZ3  . LYS   B 1 11  ? 33.257 -24.905 -20.239 1.00 44.20 ?  11  LYS   B HZ3  1 
ATOM   4078 N  N    . LEU   B 1 12  ? 34.561 -29.761 -15.536 1.00 19.96 ?  12  LEU   B N    1 
ATOM   4079 C  CA   . LEU   B 1 12  ? 33.607 -30.468 -14.689 1.00 19.15 ?  12  LEU   B CA   1 
ATOM   4080 C  C    . LEU   B 1 12  ? 32.218 -29.859 -14.776 1.00 18.93 ?  12  LEU   B C    1 
ATOM   4081 O  O    . LEU   B 1 12  ? 31.235 -30.576 -14.956 1.00 19.42 ?  12  LEU   B O    1 
ATOM   4082 C  CB   . LEU   B 1 12  ? 34.068 -30.486 -13.225 1.00 18.45 ?  12  LEU   B CB   1 
ATOM   4083 C  CG   . LEU   B 1 12  ? 35.409 -31.167 -12.956 1.00 18.03 ?  12  LEU   B CG   1 
ATOM   4084 C  CD1  . LEU   B 1 12  ? 35.788 -31.110 -11.482 1.00 18.27 ?  12  LEU   B CD1  1 
ATOM   4085 C  CD2  . LEU   B 1 12  ? 35.395 -32.601 -13.451 1.00 18.72 ?  12  LEU   B CD2  1 
ATOM   4086 H  H    . LEU   B 1 12  ? 34.876 -29.041 -15.178 1.00 23.97 ?  12  LEU   B H    1 
ATOM   4087 H  HA   . LEU   B 1 12  ? 33.536 -31.381 -14.994 1.00 22.99 ?  12  LEU   B HA   1 
ATOM   4088 H  HB2  . LEU   B 1 12  ? 34.132 -29.571 -12.914 1.00 22.15 ?  12  LEU   B HB2  1 
ATOM   4089 H  HB3  . LEU   B 1 12  ? 33.394 -30.955 -12.703 1.00 22.15 ?  12  LEU   B HB3  1 
ATOM   4090 H  HG   . LEU   B 1 12  ? 36.094 -30.689 -13.449 1.00 21.64 ?  12  LEU   B HG   1 
ATOM   4091 H  HD11 . LEU   B 1 12  ? 36.650 -31.544 -11.361 1.00 21.93 ?  12  LEU   B HD11 1 
ATOM   4092 H  HD12 . LEU   B 1 12  ? 35.849 -30.181 -11.201 1.00 21.93 ?  12  LEU   B HD12 1 
ATOM   4093 H  HD13 . LEU   B 1 12  ? 35.113 -31.568 -10.960 1.00 21.93 ?  12  LEU   B HD13 1 
ATOM   4094 H  HD21 . LEU   B 1 12  ? 36.192 -33.051 -13.135 1.00 22.47 ?  12  LEU   B HD21 1 
ATOM   4095 H  HD22 . LEU   B 1 12  ? 34.604 -33.045 -13.105 1.00 22.47 ?  12  LEU   B HD22 1 
ATOM   4096 H  HD23 . LEU   B 1 12  ? 35.375 -32.599 -14.421 1.00 22.47 ?  12  LEU   B HD23 1 
ATOM   4097 N  N    . THR   B 1 13  ? 32.128 -28.543 -14.639 1.00 18.95 ?  13  THR   B N    1 
ATOM   4098 C  CA   . THR   B 1 13  ? 30.907 -27.790 -14.857 1.00 18.85 ?  13  THR   B CA   1 
ATOM   4099 C  C    . THR   B 1 13  ? 31.250 -26.608 -15.754 1.00 21.11 ?  13  THR   B C    1 
ATOM   4100 O  O    . THR   B 1 13  ? 32.401 -26.428 -16.174 1.00 22.04 ?  13  THR   B O    1 
ATOM   4101 C  CB   . THR   B 1 13  ? 30.302 -27.303 -13.534 1.00 17.89 ?  13  THR   B CB   1 
ATOM   4102 O  OG1  . THR   B 1 13  ? 31.150 -26.289 -12.982 1.00 17.89 ?  13  THR   B OG1  1 
ATOM   4103 C  CG2  . THR   B 1 13  ? 30.169 -28.453 -12.538 1.00 18.21 ?  13  THR   B CG2  1 
ATOM   4104 H  H    . THR   B 1 13  ? 32.786 -28.045 -14.408 1.00 22.75 ?  13  THR   B H    1 
ATOM   4105 H  HA   . THR   B 1 13  ? 30.248 -28.346 -15.304 1.00 22.63 ?  13  THR   B HA   1 
ATOM   4106 H  HB   . THR   B 1 13  ? 29.411 -26.933 -13.694 1.00 21.48 ?  13  THR   B HB   1 
ATOM   4107 H  HG1  . THR   B 1 13  ? 30.867 -25.524 -13.211 1.00 21.48 ?  13  THR   B HG1  1 
ATOM   4108 H  HG21 . THR   B 1 13  ? 29.665 -28.167 -11.759 1.00 21.87 ?  13  THR   B HG21 1 
ATOM   4109 H  HG22 . THR   B 1 13  ? 29.705 -29.199 -12.953 1.00 21.87 ?  13  THR   B HG22 1 
ATOM   4110 H  HG23 . THR   B 1 13  ? 31.047 -28.748 -12.254 1.00 21.87 ?  13  THR   B HG23 1 
ATOM   4111 N  N    A ASP   B 1 14  ? 30.244 -25.781 -16.038 0.64 21.79 ?  14  ASP   B N    1 
ATOM   4112 N  N    B ASP   B 1 14  ? 30.248 -25.772 -16.036 0.36 21.83 ?  14  ASP   B N    1 
ATOM   4113 C  CA   A ASP   B 1 14  ? 30.472 -24.631 -16.904 0.64 23.37 ?  14  ASP   B CA   1 
ATOM   4114 C  CA   B ASP   B 1 14  ? 30.471 -24.628 -16.912 0.36 22.87 ?  14  ASP   B CA   1 
ATOM   4115 C  C    A ASP   B 1 14  ? 31.577 -23.731 -16.369 0.64 21.46 ?  14  ASP   B C    1 
ATOM   4116 C  C    B ASP   B 1 14  ? 31.495 -23.652 -16.354 0.36 21.08 ?  14  ASP   B C    1 
ATOM   4117 O  O    A ASP   B 1 14  ? 32.274 -23.080 -17.156 0.64 22.44 ?  14  ASP   B O    1 
ATOM   4118 O  O    B ASP   B 1 14  ? 32.028 -22.839 -17.117 0.36 21.64 ?  14  ASP   B O    1 
ATOM   4119 C  CB   A ASP   B 1 14  ? 29.176 -23.840 -17.089 0.64 27.01 ?  14  ASP   B CB   1 
ATOM   4120 C  CB   B ASP   B 1 14  ? 29.160 -23.885 -17.179 0.36 25.65 ?  14  ASP   B CB   1 
ATOM   4121 C  CG   A ASP   B 1 14  ? 28.197 -24.526 -18.018 0.64 30.52 ?  14  ASP   B CG   1 
ATOM   4122 C  CG   B ASP   B 1 14  ? 28.286 -24.593 -18.196 0.36 28.24 ?  14  ASP   B CG   1 
ATOM   4123 O  OD1  A ASP   B 1 14  ? 28.572 -25.522 -18.677 0.64 31.55 ?  14  ASP   B OD1  1 
ATOM   4124 O  OD1  B ASP   B 1 14  ? 28.833 -25.324 -19.049 0.36 29.11 ?  14  ASP   B OD1  1 
ATOM   4125 O  OD2  A ASP   B 1 14  ? 27.039 -24.068 -18.083 0.64 31.94 -1 14  ASP   B OD2  1 
ATOM   4126 O  OD2  B ASP   B 1 14  ? 27.050 -24.419 -18.146 0.36 29.10 -1 14  ASP   B OD2  1 
ATOM   4127 H  H    A ASP   B 1 14  ? 29.443 -25.848 -15.736 0.64 26.15 ?  14  ASP   B H    1 
ATOM   4128 H  H    B ASP   B 1 14  ? 29.447 -25.840 -15.735 0.36 26.20 ?  14  ASP   B H    1 
ATOM   4129 H  HA   A ASP   B 1 14  ? 30.758 -24.938 -17.772 0.64 28.05 ?  14  ASP   B HA   1 
ATOM   4130 H  HA   B ASP   B 1 14  ? 30.809 -24.944 -17.760 0.36 27.45 ?  14  ASP   B HA   1 
ATOM   4131 H  HB2  A ASP   B 1 14  ? 28.730 -23.744 -16.236 0.64 32.42 ?  14  ASP   B HB2  1 
ATOM   4132 H  HB2  B ASP   B 1 14  ? 28.661 -23.815 -16.351 0.36 30.79 ?  14  ASP   B HB2  1 
ATOM   4133 H  HB3  A ASP   B 1 14  ? 29.379 -22.968 -17.463 0.64 32.42 ?  14  ASP   B HB3  1 
ATOM   4134 H  HB3  B ASP   B 1 14  ? 29.363 -22.996 -17.517 0.36 30.79 ?  14  ASP   B HB3  1 
ATOM   4135 N  N    . ASN   B 1 15  ? 31.772 -23.695 -15.047 1.00 19.16 ?  15  ASN   B N    1 
ATOM   4136 C  CA   . ASN   B 1 15  ? 32.734 -22.778 -14.440 1.00 16.77 ?  15  ASN   B CA   1 
ATOM   4137 C  C    . ASN   B 1 15  ? 33.824 -23.435 -13.602 1.00 15.41 ?  15  ASN   B C    1 
ATOM   4138 O  O    . ASN   B 1 15  ? 34.677 -22.712 -13.077 1.00 15.40 ?  15  ASN   B O    1 
ATOM   4139 C  CB   . ASN   B 1 15  ? 32.019 -21.724 -13.577 1.00 16.90 ?  15  ASN   B CB   1 
ATOM   4140 C  CG   . ASN   B 1 15  ? 31.401 -22.321 -12.332 1.00 16.40 ?  15  ASN   B CG   1 
ATOM   4141 O  OD1  . ASN   B 1 15  ? 30.455 -23.112 -12.419 1.00 18.02 ?  15  ASN   B OD1  1 
ATOM   4142 N  ND2  . ASN   B 1 15  ? 31.930 -21.967 -11.171 1.00 15.52 ?  15  ASN   B ND2  1 
ATOM   4143 H  H    A ASN   B 1 15  ? 31.356 -24.191 -14.480 0.64 23.00 ?  15  ASN   B H    1 
ATOM   4144 H  H    B ASN   B 1 15  ? 31.394 -24.227 -14.486 0.36 23.00 ?  15  ASN   B H    1 
ATOM   4145 H  HA   . ASN   B 1 15  ? 33.182 -22.291 -15.140 1.00 20.13 ?  15  ASN   B HA   1 
ATOM   4146 H  HB2  . ASN   B 1 15  ? 32.663 -21.043 -13.299 1.00 20.29 ?  15  ASN   B HB2  1 
ATOM   4147 H  HB3  . ASN   B 1 15  ? 31.311 -21.303 -14.093 1.00 20.29 ?  15  ASN   B HB3  1 
ATOM   4148 H  HD21 . ASN   B 1 15  ? 31.613 -22.276 -10.432 1.00 18.63 ?  15  ASN   B HD21 1 
ATOM   4149 H  HD22 . ASN   B 1 15  ? 32.600 -21.417 -11.144 1.00 18.63 ?  15  ASN   B HD22 1 
ATOM   4150 N  N    . VAL   B 1 16  ? 33.824 -24.757 -13.443 1.00 15.20 ?  16  VAL   B N    1 
ATOM   4151 C  CA   . VAL   B 1 16  ? 34.825 -25.445 -12.633 1.00 14.67 ?  16  VAL   B CA   1 
ATOM   4152 C  C    . VAL   B 1 16  ? 35.617 -26.381 -13.529 1.00 15.15 ?  16  VAL   B C    1 
ATOM   4153 O  O    . VAL   B 1 16  ? 35.041 -27.268 -14.180 1.00 16.15 ?  16  VAL   B O    1 
ATOM   4154 C  CB   . VAL   B 1 16  ? 34.203 -26.209 -11.455 1.00 14.98 ?  16  VAL   B CB   1 
ATOM   4155 C  CG1  . VAL   B 1 16  ? 35.291 -26.938 -10.668 1.00 14.79 ?  16  VAL   B CG1  1 
ATOM   4156 C  CG2  . VAL   B 1 16  ? 33.405 -25.261 -10.560 1.00 15.88 ?  16  VAL   B CG2  1 
ATOM   4157 H  H    . VAL   B 1 16  ? 33.235 -25.282 -13.794 1.00 18.25 ?  16  VAL   B H    1 
ATOM   4158 H  HA   . VAL   B 1 16  ? 35.435 -24.789 -12.266 1.00 17.61 ?  16  VAL   B HA   1 
ATOM   4159 H  HB   . VAL   B 1 16  ? 33.588 -26.878 -11.802 1.00 17.99 ?  16  VAL   B HB   1 
ATOM   4160 H  HG11 . VAL   B 1 16  ? 34.921 -27.232 -9.821  1.00 17.76 ?  16  VAL   B HG11 1 
ATOM   4161 H  HG12 . VAL   B 1 16  ? 35.597 -27.701 -11.179 1.00 17.76 ?  16  VAL   B HG12 1 
ATOM   4162 H  HG13 . VAL   B 1 16  ? 36.026 -26.324 -10.511 1.00 17.76 ?  16  VAL   B HG13 1 
ATOM   4163 H  HG21 . VAL   B 1 16  ? 33.069 -25.758 -9.797  1.00 19.06 ?  16  VAL   B HG21 1 
ATOM   4164 H  HG22 . VAL   B 1 16  ? 33.984 -24.546 -10.263 1.00 19.06 ?  16  VAL   B HG22 1 
ATOM   4165 H  HG23 . VAL   B 1 16  ? 32.662 -24.898 -11.069 1.00 19.06 ?  16  VAL   B HG23 1 
ATOM   4166 N  N    . TYR   B 1 17  ? 36.938 -26.208 -13.517 1.00 15.35 ?  17  TYR   B N    1 
ATOM   4167 C  CA   . TYR   B 1 17  ? 37.882 -26.959 -14.329 1.00 15.91 ?  17  TYR   B CA   1 
ATOM   4168 C  C    . TYR   B 1 17  ? 38.938 -27.570 -13.418 1.00 14.95 ?  17  TYR   B C    1 
ATOM   4169 O  O    . TYR   B 1 17  ? 39.227 -27.043 -12.343 1.00 14.94 ?  17  TYR   B O    1 
ATOM   4170 C  CB   . TYR   B 1 17  ? 38.588 -26.036 -15.330 1.00 19.04 ?  17  TYR   B CB   1 
ATOM   4171 C  CG   . TYR   B 1 17  ? 37.662 -25.270 -16.246 1.00 22.81 ?  17  TYR   B CG   1 
ATOM   4172 C  CD1  . TYR   B 1 17  ? 37.092 -24.067 -15.850 1.00 24.89 ?  17  TYR   B CD1  1 
ATOM   4173 C  CD2  . TYR   B 1 17  ? 37.358 -25.753 -17.513 1.00 24.87 ?  17  TYR   B CD2  1 
ATOM   4174 C  CE1  . TYR   B 1 17  ? 36.245 -23.365 -16.689 1.00 26.60 ?  17  TYR   B CE1  1 
ATOM   4175 C  CE2  . TYR   B 1 17  ? 36.515 -25.058 -18.360 1.00 26.58 ?  17  TYR   B CE2  1 
ATOM   4176 C  CZ   . TYR   B 1 17  ? 35.960 -23.867 -17.941 1.00 27.73 ?  17  TYR   B CZ   1 
ATOM   4177 O  OH   . TYR   B 1 17  ? 35.121 -23.173 -18.780 1.00 28.95 ?  17  TYR   B OH   1 
ATOM   4178 H  H    . TYR   B 1 17  ? 37.329 -25.621 -13.020 1.00 18.43 ?  17  TYR   B H    1 
ATOM   4179 H  HA   . TYR   B 1 17  ? 37.416 -27.664 -14.813 1.00 19.10 ?  17  TYR   B HA   1 
ATOM   4180 H  HB2  . TYR   B 1 17  ? 39.121 -25.392 -14.841 1.00 22.86 ?  17  TYR   B HB2  1 
ATOM   4181 H  HB3  . TYR   B 1 17  ? 39.156 -26.577 -15.892 1.00 22.86 ?  17  TYR   B HB3  1 
ATOM   4182 H  HD1  . TYR   B 1 17  ? 37.281 -23.726 -15.008 1.00 29.88 ?  17  TYR   B HD1  1 
ATOM   4183 H  HD2  . TYR   B 1 17  ? 37.727 -26.555 -17.800 1.00 29.86 ?  17  TYR   B HD2  1 
ATOM   4184 H  HE1  . TYR   B 1 17  ? 35.868 -22.559 -16.412 1.00 31.94 ?  17  TYR   B HE1  1 
ATOM   4185 H  HE2  . TYR   B 1 17  ? 36.316 -25.393 -19.207 1.00 31.91 ?  17  TYR   B HE2  1 
ATOM   4186 H  HH   . TYR   B 1 17  ? 35.028 -23.584 -19.508 1.00 34.75 ?  17  TYR   B HH   1 
ATOM   4187 N  N    . ILE   B 1 18  ? 39.532 -28.683 -13.844 1.00 15.15 ?  18  ILE   B N    1 
ATOM   4188 C  CA   . ILE   B 1 18  ? 40.461 -29.404 -12.981 1.00 15.24 ?  18  ILE   B CA   1 
ATOM   4189 C  C    . ILE   B 1 18  ? 41.618 -29.958 -13.803 1.00 15.58 ?  18  ILE   B C    1 
ATOM   4190 O  O    . ILE   B 1 18  ? 41.457 -30.341 -14.966 1.00 16.85 ?  18  ILE   B O    1 
ATOM   4191 C  CB   . ILE   B 1 18  ? 39.714 -30.503 -12.179 1.00 15.48 ?  18  ILE   B CB   1 
ATOM   4192 C  CG1  . ILE   B 1 18  ? 40.581 -31.045 -11.040 1.00 15.92 ?  18  ILE   B CG1  1 
ATOM   4193 C  CG2  . ILE   B 1 18  ? 39.230 -31.629 -13.106 1.00 16.02 ?  18  ILE   B CG2  1 
ATOM   4194 C  CD1  . ILE   B 1 18  ? 39.799 -31.880 -10.037 1.00 17.36 ?  18  ILE   B CD1  1 
ATOM   4195 H  H    . ILE   B 1 18  ? 39.407 -29.039 -14.613 1.00 18.19 ?  18  ILE   B H    1 
ATOM   4196 H  HA   . ILE   B 1 18  ? 40.818 -28.789 -12.329 1.00 18.30 ?  18  ILE   B HA   1 
ATOM   4197 H  HB   . ILE   B 1 18  ? 38.923 -30.108 -11.775 1.00 18.58 ?  18  ILE   B HB   1 
ATOM   4198 H  HG12 . ILE   B 1 18  ? 41.278 -31.603 -11.411 1.00 19.11 ?  18  ILE   B HG12 1 
ATOM   4199 H  HG13 . ILE   B 1 18  ? 40.968 -30.297 -10.562 1.00 19.11 ?  18  ILE   B HG13 1 
ATOM   4200 H  HG21 . ILE   B 1 18  ? 38.628 -32.211 -12.612 1.00 19.23 ?  18  ILE   B HG21 1 
ATOM   4201 H  HG22 . ILE   B 1 18  ? 38.759 -31.232 -13.855 1.00 19.23 ?  18  ILE   B HG22 1 
ATOM   4202 H  HG23 . ILE   B 1 18  ? 39.994 -32.131 -13.420 1.00 19.23 ?  18  ILE   B HG23 1 
ATOM   4203 H  HD11 . ILE   B 1 18  ? 40.395 -32.154 -9.320  1.00 20.84 ?  18  ILE   B HD11 1 
ATOM   4204 H  HD12 . ILE   B 1 18  ? 39.073 -31.348 -9.676  1.00 20.84 ?  18  ILE   B HD12 1 
ATOM   4205 H  HD13 . ILE   B 1 18  ? 39.442 -32.664 -10.484 1.00 20.84 ?  18  ILE   B HD13 1 
ATOM   4206 N  N    . LYS   B 1 19  ? 42.795 -30.000 -13.179 1.00 15.71 ?  19  LYS   B N    1 
ATOM   4207 C  CA   . LYS   B 1 19  ? 44.006 -30.466 -13.836 1.00 16.95 ?  19  LYS   B CA   1 
ATOM   4208 C  C    . LYS   B 1 19  ? 44.914 -31.143 -12.819 1.00 16.76 ?  19  LYS   B C    1 
ATOM   4209 O  O    . LYS   B 1 19  ? 45.001 -30.715 -11.667 1.00 15.88 ?  19  LYS   B O    1 
ATOM   4210 C  CB   . LYS   B 1 19  ? 44.760 -29.297 -14.479 1.00 18.68 ?  19  LYS   B CB   1 
ATOM   4211 C  CG   . LYS   B 1 19  ? 45.956 -29.701 -15.319 1.00 20.84 ?  19  LYS   B CG   1 
ATOM   4212 C  CD   . LYS   B 1 19  ? 46.665 -28.470 -15.872 1.00 22.49 ?  19  LYS   B CD   1 
ATOM   4213 C  CE   . LYS   B 1 19  ? 47.843 -28.843 -16.749 1.00 24.44 ?  19  LYS   B CE   1 
ATOM   4214 N  NZ   . LYS   B 1 19  ? 48.563 -27.641 -17.247 1.00 25.15 ?  19  LYS   B NZ   1 
ATOM   4215 H  H    . LYS   B 1 19  ? 42.900 -29.758 -12.358 1.00 18.86 ?  19  LYS   B H    1 
ATOM   4216 H  HA   . LYS   B 1 19  ? 43.764 -31.107 -14.523 1.00 20.34 ?  19  LYS   B HA   1 
ATOM   4217 H  HB2  . LYS   B 1 19  ? 44.142 -28.820 -15.053 1.00 22.42 ?  19  LYS   B HB2  1 
ATOM   4218 H  HB3  . LYS   B 1 19  ? 45.068 -28.708 -13.770 1.00 22.42 ?  19  LYS   B HB3  1 
ATOM   4219 H  HG2  . LYS   B 1 19  ? 46.576 -30.200 -14.768 1.00 25.02 ?  19  LYS   B HG2  1 
ATOM   4220 H  HG3  . LYS   B 1 19  ? 45.647 -30.245 -16.062 1.00 25.02 ?  19  LYS   B HG3  1 
ATOM   4221 H  HD2  . LYS   B 1 19  ? 46.035 -27.955 -16.402 1.00 26.99 ?  19  LYS   B HD2  1 
ATOM   4222 H  HD3  . LYS   B 1 19  ? 46.989 -27.936 -15.130 1.00 26.99 ?  19  LYS   B HD3  1 
ATOM   4223 H  HE2  . LYS   B 1 19  ? 48.464 -29.381 -16.234 1.00 29.34 ?  19  LYS   B HE2  1 
ATOM   4224 H  HE3  . LYS   B 1 19  ? 47.521 -29.346 -17.515 1.00 29.34 ?  19  LYS   B HE3  1 
ATOM   4225 H  HZ1  . LYS   B 1 19  ? 49.211 -27.884 -17.806 1.00 30.19 ?  19  LYS   B HZ1  1 
ATOM   4226 H  HZ2  . LYS   B 1 19  ? 47.998 -27.102 -17.676 1.00 30.19 ?  19  LYS   B HZ2  1 
ATOM   4227 H  HZ3  . LYS   B 1 19  ? 48.922 -27.197 -16.564 1.00 30.19 ?  19  LYS   B HZ3  1 
ATOM   4228 N  N    . ASN   B 1 20  ? 45.601 -32.193 -13.259 1.00 17.99 ?  20  ASN   B N    1 
ATOM   4229 C  CA   . ASN   B 1 20  ? 46.625 -32.837 -12.442 1.00 19.18 ?  20  ASN   B CA   1 
ATOM   4230 C  C    . ASN   B 1 20  ? 47.907 -32.028 -12.621 1.00 19.70 ?  20  ASN   B C    1 
ATOM   4231 O  O    . ASN   B 1 20  ? 48.563 -32.110 -13.664 1.00 21.58 ?  20  ASN   B O    1 
ATOM   4232 C  CB   . ASN   B 1 20  ? 46.784 -34.291 -12.879 1.00 20.90 ?  20  ASN   B CB   1 
ATOM   4233 C  CG   . ASN   B 1 20  ? 47.926 -35.011 -12.182 1.00 22.49 ?  20  ASN   B CG   1 
ATOM   4234 O  OD1  . ASN   B 1 20  ? 48.567 -35.881 -12.776 1.00 24.71 ?  20  ASN   B OD1  1 
ATOM   4235 N  ND2  . ASN   B 1 20  ? 48.178 -34.674 -10.923 1.00 22.08 ?  20  ASN   B ND2  1 
ATOM   4236 H  H    . ASN   B 1 20  ? 45.492 -32.549 -14.033 1.00 21.60 ?  20  ASN   B H    1 
ATOM   4237 H  HA   . ASN   B 1 20  ? 46.352 -32.817 -11.510 1.00 23.03 ?  20  ASN   B HA   1 
ATOM   4238 H  HB2  . ASN   B 1 20  ? 45.962 -34.772 -12.680 1.00 25.09 ?  20  ASN   B HB2  1 
ATOM   4239 H  HB3  . ASN   B 1 20  ? 46.953 -34.314 -13.832 1.00 25.09 ?  20  ASN   B HB3  1 
ATOM   4240 H  HD21 . ASN   B 1 20  ? 48.817 -35.055 -10.495 1.00 26.51 ?  20  ASN   B HD21 1 
ATOM   4241 H  HD22 . ASN   B 1 20  ? 47.709 -34.063 -10.532 1.00 26.51 ?  20  ASN   B HD22 1 
ATOM   4242 N  N    . ALA   B 1 21  ? 48.260 -31.224 -11.617 1.00 18.97 ?  21  ALA   B N    1 
ATOM   4243 C  CA   . ALA   B 1 21  ? 49.380 -30.309 -11.770 1.00 19.50 ?  21  ALA   B CA   1 
ATOM   4244 C  C    . ALA   B 1 21  ? 49.845 -29.810 -10.411 1.00 18.40 ?  21  ALA   B C    1 
ATOM   4245 O  O    . ALA   B 1 21  ? 49.107 -29.837 -9.422  1.00 18.19 ?  21  ALA   B O    1 
ATOM   4246 C  CB   . ALA   B 1 21  ? 49.003 -29.129 -12.667 1.00 20.81 ?  21  ALA   B CB   1 
ATOM   4247 H  H    . ALA   B 1 21  ? 47.866 -31.194 -10.846 1.00 22.78 ?  21  ALA   B H    1 
ATOM   4248 H  HA   . ALA   B 1 21  ? 50.115 -30.787 -12.185 1.00 23.40 ?  21  ALA   B HA   1 
ATOM   4249 H  HB1  . ALA   B 1 21  ? 49.794 -28.593 -12.812 1.00 24.98 ?  21  ALA   B HB1  1 
ATOM   4250 H  HB2  . ALA   B 1 21  ? 48.674 -29.475 -13.510 1.00 24.98 ?  21  ALA   B HB2  1 
ATOM   4251 H  HB3  . ALA   B 1 21  ? 48.315 -28.609 -12.228 1.00 24.98 ?  21  ALA   B HB3  1 
ATOM   4252 N  N    . ASP   B 1 22  ? 51.103 -29.364 -10.398 1.00 17.31 ?  22  ASP   B N    1 
ATOM   4253 C  CA   . ASP   B 1 22  ? 51.717 -28.662 -9.277  1.00 16.61 ?  22  ASP   B CA   1 
ATOM   4254 C  C    . ASP   B 1 22  ? 51.304 -27.193 -9.360  1.00 15.08 ?  22  ASP   B C    1 
ATOM   4255 O  O    . ASP   B 1 22  ? 51.601 -26.522 -10.352 1.00 15.53 ?  22  ASP   B O    1 
ATOM   4256 C  CB   . ASP   B 1 22  ? 53.233 -28.831 -9.439  1.00 17.98 ?  22  ASP   B CB   1 
ATOM   4257 C  CG   . ASP   B 1 22  ? 54.058 -28.077 -8.405  1.00 19.73 ?  22  ASP   B CG   1 
ATOM   4258 O  OD1  . ASP   B 1 22  ? 53.688 -26.961 -8.003  1.00 19.42 ?  22  ASP   B OD1  1 
ATOM   4259 O  OD2  . ASP   B 1 22  ? 55.131 -28.595 -8.023  1.00 22.29 -1 22  ASP   B OD2  1 
ATOM   4260 H  H    . ASP   B 1 22  ? 51.645 -29.464 -11.064 1.00 20.78 ?  22  ASP   B H    1 
ATOM   4261 H  HA   . ASP   B 1 22  ? 51.435 -29.045 -8.431  1.00 19.94 ?  22  ASP   B HA   1 
ATOM   4262 H  HB2  . ASP   B 1 22  ? 53.462 -29.769 -9.370  1.00 21.59 ?  22  ASP   B HB2  1 
ATOM   4263 H  HB3  . ASP   B 1 22  ? 53.498 -28.489 -10.309 1.00 21.59 ?  22  ASP   B HB3  1 
ATOM   4264 N  N    . ILE   B 1 23  ? 50.604 -26.698 -8.333  1.00 14.30 ?  23  ILE   B N    1 
ATOM   4265 C  CA   . ILE   B 1 23  ? 50.010 -25.359 -8.406  1.00 13.52 ?  23  ILE   B CA   1 
ATOM   4266 C  C    . ILE   B 1 23  ? 51.067 -24.274 -8.543  1.00 13.17 ?  23  ILE   B C    1 
ATOM   4267 O  O    . ILE   B 1 23  ? 50.806 -23.231 -9.147  1.00 12.87 ?  23  ILE   B O    1 
ATOM   4268 C  CB   . ILE   B 1 23  ? 49.071 -25.109 -7.212  1.00 13.94 ?  23  ILE   B CB   1 
ATOM   4269 C  CG1  . ILE   B 1 23  ? 48.242 -23.839 -7.428  1.00 14.24 ?  23  ILE   B CG1  1 
ATOM   4270 C  CG2  . ILE   B 1 23  ? 49.836 -25.067 -5.902  1.00 14.58 ?  23  ILE   B CG2  1 
ATOM   4271 C  CD1  . ILE   B 1 23  ? 47.144 -23.658 -6.393  1.00 15.30 ?  23  ILE   B CD1  1 
ATOM   4272 H  H    . ILE   B 1 23  ? 50.461 -27.114 -7.596  1.00 17.17 ?  23  ILE   B H    1 
ATOM   4273 H  HA   . ILE   B 1 23  ? 49.467 -25.320 -9.207  1.00 16.23 ?  23  ILE   B HA   1 
ATOM   4274 H  HB   . ILE   B 1 23  ? 48.449 -25.855 -7.170  1.00 16.74 ?  23  ILE   B HB   1 
ATOM   4275 H  HG12 . ILE   B 1 23  ? 48.833 -23.067 -7.379  1.00 17.09 ?  23  ILE   B HG12 1 
ATOM   4276 H  HG13 . ILE   B 1 23  ? 47.828 -23.876 -8.307  1.00 17.09 ?  23  ILE   B HG13 1 
ATOM   4277 H  HG21 . ILE   B 1 23  ? 49.203 -25.073 -5.168  1.00 17.51 ?  23  ILE   B HG21 1 
ATOM   4278 H  HG22 . ILE   B 1 23  ? 50.412 -25.845 -5.850  1.00 17.51 ?  23  ILE   B HG22 1 
ATOM   4279 H  HG23 . ILE   B 1 23  ? 50.369 -24.258 -5.876  1.00 17.51 ?  23  ILE   B HG23 1 
ATOM   4280 H  HD11 . ILE   B 1 23  ? 46.604 -22.895 -6.643  1.00 18.37 ?  23  ILE   B HD11 1 
ATOM   4281 H  HD12 . ILE   B 1 23  ? 46.602 -24.461 -6.375  1.00 18.37 ?  23  ILE   B HD12 1 
ATOM   4282 H  HD13 . ILE   B 1 23  ? 47.553 -23.511 -5.528  1.00 18.37 ?  23  ILE   B HD13 1 
ATOM   4283 N  N    . VAL   B 1 24  ? 52.259 -24.480 -7.981  1.00 13.71 ?  24  VAL   B N    1 
ATOM   4284 C  CA   . VAL   B 1 24  ? 53.336 -23.503 -8.147  1.00 14.39 ?  24  VAL   B CA   1 
ATOM   4285 C  C    . VAL   B 1 24  ? 53.791 -23.456 -9.600  1.00 14.57 ?  24  VAL   B C    1 
ATOM   4286 O  O    . VAL   B 1 24  ? 53.932 -22.378 -10.193 1.00 14.61 ?  24  VAL   B O    1 
ATOM   4287 C  CB   . VAL   B 1 24  ? 54.509 -23.822 -7.201  1.00 15.15 ?  24  VAL   B CB   1 
ATOM   4288 C  CG1  . VAL   B 1 24  ? 55.719 -22.949 -7.529  1.00 15.74 ?  24  VAL   B CG1  1 
ATOM   4289 C  CG2  . VAL   B 1 24  ? 54.095 -23.628 -5.761  1.00 16.36 ?  24  VAL   B CG2  1 
ATOM   4290 H  H    . VAL   B 1 24  ? 52.470 -25.162 -7.505  1.00 16.47 ?  24  VAL   B H    1 
ATOM   4291 H  HA   . VAL   B 1 24  ? 53.005 -22.623 -7.911  1.00 17.27 ?  24  VAL   B HA   1 
ATOM   4292 H  HB   . VAL   B 1 24  ? 54.770 -24.750 -7.312  1.00 18.19 ?  24  VAL   B HB   1 
ATOM   4293 H  HG11 . VAL   B 1 24  ? 56.322 -22.951 -6.768  1.00 18.90 ?  24  VAL   B HG11 1 
ATOM   4294 H  HG12 . VAL   B 1 24  ? 56.168 -23.314 -8.305  1.00 18.90 ?  24  VAL   B HG12 1 
ATOM   4295 H  HG13 . VAL   B 1 24  ? 55.415 -22.047 -7.707  1.00 18.90 ?  24  VAL   B HG13 1 
ATOM   4296 H  HG21 . VAL   B 1 24  ? 54.823 -23.898 -5.180  1.00 19.64 ?  24  VAL   B HG21 1 
ATOM   4297 H  HG22 . VAL   B 1 24  ? 53.889 -22.690 -5.617  1.00 19.64 ?  24  VAL   B HG22 1 
ATOM   4298 H  HG23 . VAL   B 1 24  ? 53.310 -24.170 -5.582  1.00 19.64 ?  24  VAL   B HG23 1 
ATOM   4299 N  N    . GLU   B 1 25  ? 54.060 -24.626 -10.187 1.00 15.70 ?  25  GLU   B N    1 
ATOM   4300 C  CA   . GLU   B 1 25  ? 54.448 -24.664 -11.592 1.00 17.23 ?  25  GLU   B CA   1 
ATOM   4301 C  C    . GLU   B 1 25  ? 53.336 -24.127 -12.478 1.00 15.75 ?  25  GLU   B C    1 
ATOM   4302 O  O    . GLU   B 1 25  ? 53.597 -23.410 -13.451 1.00 16.38 ?  25  GLU   B O    1 
ATOM   4303 C  CB   . GLU   B 1 25  ? 54.843 -26.085 -11.989 1.00 21.26 ?  25  GLU   B CB   1 
ATOM   4304 C  CG   . GLU   B 1 25  ? 56.146 -26.529 -11.341 1.00 26.91 ?  25  GLU   B CG   1 
ATOM   4305 C  CD   . GLU   B 1 25  ? 57.248 -25.478 -11.430 1.00 31.93 ?  25  GLU   B CD   1 
ATOM   4306 O  OE1  . GLU   B 1 25  ? 57.656 -25.129 -12.559 1.00 33.87 ?  25  GLU   B OE1  1 
ATOM   4307 O  OE2  . GLU   B 1 25  ? 57.693 -24.980 -10.369 1.00 33.56 -1 25  GLU   B OE2  1 
ATOM   4308 H  H    . GLU   B 1 25  ? 54.027 -25.392 -9.798  1.00 18.84 ?  25  GLU   B H    1 
ATOM   4309 H  HA   . GLU   B 1 25  ? 55.203 -24.076 -11.721 1.00 20.68 ?  25  GLU   B HA   1 
ATOM   4310 H  HB2  . GLU   B 1 25  ? 54.142 -26.698 -11.710 1.00 25.52 ?  25  GLU   B HB2  1 
ATOM   4311 H  HB3  . GLU   B 1 25  ? 54.951 -26.124 -12.953 1.00 25.52 ?  25  GLU   B HB3  1 
ATOM   4312 H  HG2  . GLU   B 1 25  ? 55.991 -26.693 -10.403 1.00 32.30 ?  25  GLU   B HG2  1 
ATOM   4313 H  HG3  . GLU   B 1 25  ? 56.454 -27.336 -11.781 1.00 32.30 ?  25  GLU   B HG3  1 
ATOM   4314 N  N    . GLU   B 1 26  ? 52.084 -24.448 -12.144 1.00 15.10 ?  26  GLU   B N    1 
ATOM   4315 C  CA   . GLU   B 1 26  ? 50.956 -23.920 -12.905 1.00 15.58 ?  26  GLU   B CA   1 
ATOM   4316 C  C    . GLU   B 1 26  ? 50.910 -22.402 -12.831 1.00 14.86 ?  26  GLU   B C    1 
ATOM   4317 O  O    . GLU   B 1 26  ? 50.714 -21.729 -13.847 1.00 15.63 ?  26  GLU   B O    1 
ATOM   4318 C  CB   . GLU   B 1 26  ? 49.640 -24.500 -12.383 1.00 17.44 ?  26  GLU   B CB   1 
ATOM   4319 C  CG   . GLU   B 1 26  ? 49.199 -25.777 -13.065 1.00 21.25 ?  26  GLU   B CG   1 
ATOM   4320 C  CD   . GLU   B 1 26  ? 48.941 -25.601 -14.562 1.00 22.78 ?  26  GLU   B CD   1 
ATOM   4321 O  OE1  . GLU   B 1 26  ? 47.972 -24.920 -14.967 1.00 23.37 ?  26  GLU   B OE1  1 
ATOM   4322 O  OE2  . GLU   B 1 26  ? 49.716 -26.169 -15.338 1.00 25.13 -1 26  GLU   B OE2  1 
ATOM   4323 H  H    . GLU   B 1 26  ? 51.860 -24.968 -11.490 1.00 18.13 ?  26  GLU   B H    1 
ATOM   4324 H  HA   . GLU   B 1 26  ? 51.054 -24.173 -13.832 1.00 18.70 ?  26  GLU   B HA   1 
ATOM   4325 H  HB2  . GLU   B 1 26  ? 49.732 -24.691 -11.435 1.00 20.94 ?  26  GLU   B HB2  1 
ATOM   4326 H  HB3  . GLU   B 1 26  ? 48.934 -23.843 -12.512 1.00 20.94 ?  26  GLU   B HB3  1 
ATOM   4327 H  HG2  . GLU   B 1 26  ? 49.896 -26.439 -12.946 1.00 25.51 ?  26  GLU   B HG2  1 
ATOM   4328 H  HG3  . GLU   B 1 26  ? 48.373 -26.083 -12.660 1.00 25.51 ?  26  GLU   B HG3  1 
ATOM   4329 N  N    . ALA   B 1 27  ? 51.055 -21.848 -11.628 1.00 13.78 ?  27  ALA   B N    1 
ATOM   4330 C  CA   . ALA   B 1 27  ? 51.021 -20.399 -11.483 1.00 13.88 ?  27  ALA   B CA   1 
ATOM   4331 C  C    . ALA   B 1 27  ? 52.091 -19.741 -12.346 1.00 14.85 ?  27  ALA   B C    1 
ATOM   4332 O  O    . ALA   B 1 27  ? 51.828 -18.744 -13.034 1.00 15.54 ?  27  ALA   B O    1 
ATOM   4333 C  CB   . ALA   B 1 27  ? 51.185 -20.018 -10.011 1.00 13.72 ?  27  ALA   B CB   1 
ATOM   4334 H  H    . ALA   B 1 27  ? 51.166 -22.284 -10.891 1.00 16.54 ?  27  ALA   B H    1 
ATOM   4335 H  HA   . ALA   B 1 27  ? 50.159 -20.072 -11.775 1.00 16.67 ?  27  ALA   B HA   1 
ATOM   4336 H  HB1  . ALA   B 1 27  ? 51.153 -19.051 -9.928  1.00 16.48 ?  27  ALA   B HB1  1 
ATOM   4337 H  HB2  . ALA   B 1 27  ? 50.458 -20.413 -9.499  1.00 16.48 ?  27  ALA   B HB2  1 
ATOM   4338 H  HB3  . ALA   B 1 27  ? 52.034 -20.351 -9.686  1.00 16.48 ?  27  ALA   B HB3  1 
ATOM   4339 N  N    . LYS   B 1 28  ? 53.303 -20.295 -12.341 1.00 16.50 ?  28  LYS   B N    1 
ATOM   4340 C  CA   . LYS   B 1 28  ? 54.375 -19.681 -13.113 1.00 18.91 ?  28  LYS   B CA   1 
ATOM   4341 C  C    . LYS   B 1 28  ? 54.121 -19.768 -14.611 1.00 19.53 ?  28  LYS   B C    1 
ATOM   4342 O  O    . LYS   B 1 28  ? 54.541 -18.876 -15.358 1.00 20.33 ?  28  LYS   B O    1 
ATOM   4343 C  CB   . LYS   B 1 28  ? 55.731 -20.274 -12.721 1.00 22.02 ?  28  LYS   B CB   1 
ATOM   4344 C  CG   . LYS   B 1 28  ? 56.131 -19.911 -11.294 1.00 25.38 ?  28  LYS   B CG   1 
ATOM   4345 C  CD   . LYS   B 1 28  ? 57.558 -20.308 -10.948 1.00 30.21 ?  28  LYS   B CD   1 
ATOM   4346 C  CE   . LYS   B 1 28  ? 57.675 -21.790 -10.685 1.00 34.34 ?  28  LYS   B CE   1 
ATOM   4347 N  NZ   . LYS   B 1 28  ? 59.032 -22.149 -10.187 1.00 36.29 ?  28  LYS   B NZ   1 
ATOM   4348 H  H    . LYS   B 1 28  ? 53.525 -21.006 -11.909 1.00 19.81 ?  28  LYS   B H    1 
ATOM   4349 H  HA   . LYS   B 1 28  ? 54.404 -18.740 -12.896 1.00 22.71 ?  28  LYS   B HA   1 
ATOM   4350 H  HB2  . LYS   B 1 28  ? 55.689 -21.238 -12.789 1.00 26.43 ?  28  LYS   B HB2  1 
ATOM   4351 H  HB3  . LYS   B 1 28  ? 56.412 -19.927 -13.323 1.00 26.43 ?  28  LYS   B HB3  1 
ATOM   4352 H  HG2  . LYS   B 1 28  ? 56.050 -18.949 -11.183 1.00 30.46 ?  28  LYS   B HG2  1 
ATOM   4353 H  HG3  . LYS   B 1 28  ? 55.535 -20.364 -10.680 1.00 30.46 ?  28  LYS   B HG3  1 
ATOM   4354 H  HD2  . LYS   B 1 28  ? 58.140 -20.080 -11.691 1.00 36.26 ?  28  LYS   B HD2  1 
ATOM   4355 H  HD3  . LYS   B 1 28  ? 57.833 -19.830 -10.149 1.00 36.26 ?  28  LYS   B HD3  1 
ATOM   4356 H  HE2  . LYS   B 1 28  ? 57.025 -22.047 -10.012 1.00 41.22 ?  28  LYS   B HE2  1 
ATOM   4357 H  HE3  . LYS   B 1 28  ? 57.514 -22.274 -11.509 1.00 41.22 ?  28  LYS   B HE3  1 
ATOM   4358 H  HZ1  . LYS   B 1 28  ? 59.079 -23.025 -10.039 1.00 43.56 ?  28  LYS   B HZ1  1 
ATOM   4359 H  HZ2  . LYS   B 1 28  ? 59.646 -21.924 -10.790 1.00 43.56 ?  28  LYS   B HZ2  1 
ATOM   4360 H  HZ3  . LYS   B 1 28  ? 59.201 -21.717 -9.427  1.00 43.56 ?  28  LYS   B HZ3  1 
ATOM   4361 N  N    . LYS   B 1 29  ? 53.399 -20.795 -15.063 1.00 20.56 ?  29  LYS   B N    1 
ATOM   4362 C  CA   . LYS   B 1 29  ? 53.125 -20.950 -16.487 1.00 23.49 ?  29  LYS   B CA   1 
ATOM   4363 C  C    . LYS   B 1 29  ? 51.872 -20.199 -16.928 1.00 22.34 ?  29  LYS   B C    1 
ATOM   4364 O  O    . LYS   B 1 29  ? 51.867 -19.583 -18.001 1.00 23.45 ?  29  LYS   B O    1 
ATOM   4365 C  CB   . LYS   B 1 29  ? 52.993 -22.434 -16.838 1.00 28.42 ?  29  LYS   B CB   1 
ATOM   4366 C  CG   . LYS   B 1 29  ? 52.895 -22.721 -18.328 1.00 33.13 ?  29  LYS   B CG   1 
ATOM   4367 C  CD   . LYS   B 1 29  ? 53.089 -24.206 -18.626 1.00 36.86 ?  29  LYS   B CD   1 
ATOM   4368 C  CE   . LYS   B 1 29  ? 51.908 -25.040 -18.160 1.00 39.60 ?  29  LYS   B CE   1 
ATOM   4369 N  NZ   . LYS   B 1 29  ? 52.126 -26.494 -18.411 1.00 41.07 ?  29  LYS   B NZ   1 
ATOM   4370 H  H    . LYS   B 1 29  ? 53.047 -21.411 -14.563 1.00 24.68 ?  29  LYS   B H    1 
ATOM   4371 H  HA   . LYS   B 1 29  ? 53.874 -20.598 -16.982 1.00 28.20 ?  29  LYS   B HA   1 
ATOM   4372 H  HB2  . LYS   B 1 29  ? 53.775 -22.897 -16.500 1.00 34.11 ?  29  LYS   B HB2  1 
ATOM   4373 H  HB3  . LYS   B 1 29  ? 52.196 -22.782 -16.417 1.00 34.11 ?  29  LYS   B HB3  1 
ATOM   4374 H  HG2  . LYS   B 1 29  ? 52.017 -22.459 -18.646 1.00 39.76 ?  29  LYS   B HG2  1 
ATOM   4375 H  HG3  . LYS   B 1 29  ? 53.583 -22.223 -18.797 1.00 39.76 ?  29  LYS   B HG3  1 
ATOM   4376 H  HD2  . LYS   B 1 29  ? 53.188 -24.331 -19.583 1.00 44.24 ?  29  LYS   B HD2  1 
ATOM   4377 H  HD3  . LYS   B 1 29  ? 53.883 -24.524 -18.166 1.00 44.24 ?  29  LYS   B HD3  1 
ATOM   4378 H  HE2  . LYS   B 1 29  ? 51.781 -24.914 -17.207 1.00 47.53 ?  29  LYS   B HE2  1 
ATOM   4379 H  HE3  . LYS   B 1 29  ? 51.112 -24.766 -18.643 1.00 47.53 ?  29  LYS   B HE3  1 
ATOM   4380 H  HZ1  . LYS   B 1 29  ? 51.422 -26.961 -18.131 1.00 49.29 ?  29  LYS   B HZ1  1 
ATOM   4381 H  HZ2  . LYS   B 1 29  ? 52.240 -26.639 -19.282 1.00 49.29 ?  29  LYS   B HZ2  1 
ATOM   4382 H  HZ3  . LYS   B 1 29  ? 52.850 -26.773 -17.974 1.00 49.29 ?  29  LYS   B HZ3  1 
ATOM   4383 N  N    . VAL   B 1 30  ? 50.811 -20.242 -16.116 1.00 20.39 ?  30  VAL   B N    1 
ATOM   4384 C  CA   . VAL   B 1 30  ? 49.522 -19.647 -16.478 1.00 20.10 ?  30  VAL   B CA   1 
ATOM   4385 C  C    . VAL   B 1 30  ? 49.538 -18.132 -16.340 1.00 19.11 ?  30  VAL   B C    1 
ATOM   4386 O  O    . VAL   B 1 30  ? 48.801 -17.425 -17.050 1.00 19.73 ?  30  VAL   B O    1 
ATOM   4387 C  CB   . VAL   B 1 30  ? 48.427 -20.252 -15.579 1.00 21.19 ?  30  VAL   B CB   1 
ATOM   4388 C  CG1  . VAL   B 1 30  ? 47.144 -19.446 -15.661 1.00 21.55 ?  30  VAL   B CG1  1 
ATOM   4389 C  CG2  . VAL   B 1 30  ? 48.177 -21.710 -15.945 1.00 22.11 ?  30  VAL   B CG2  1 
ATOM   4390 H  H    . VAL   B 1 30  ? 50.804 -20.639 -15.342 1.00 24.48 ?  30  VAL   B H    1 
ATOM   4391 H  HA   . VAL   B 1 30  ? 49.311 -19.885 -17.395 1.00 24.13 ?  30  VAL   B HA   1 
ATOM   4392 H  HB   . VAL   B 1 30  ? 48.727 -20.237 -14.656 1.00 25.44 ?  30  VAL   B HB   1 
ATOM   4393 H  HG11 . VAL   B 1 30  ? 46.403 -20.025 -15.426 1.00 25.87 ?  30  VAL   B HG11 1 
ATOM   4394 H  HG12 . VAL   B 1 30  ? 47.192 -18.707 -15.039 1.00 25.87 ?  30  VAL   B HG12 1 
ATOM   4395 H  HG13 . VAL   B 1 30  ? 47.028 -19.127 -16.565 1.00 25.87 ?  30  VAL   B HG13 1 
ATOM   4396 H  HG21 . VAL   B 1 30  ? 47.494 -22.078 -15.354 1.00 26.54 ?  30  VAL   B HG21 1 
ATOM   4397 H  HG22 . VAL   B 1 30  ? 47.868 -21.758 -16.865 1.00 26.54 ?  30  VAL   B HG22 1 
ATOM   4398 H  HG23 . VAL   B 1 30  ? 48.999 -22.211 -15.845 1.00 26.54 ?  30  VAL   B HG23 1 
ATOM   4399 N  N    . LYS   B 1 31  ? 50.332 -17.624 -15.405 1.00 18.78 ?  31  LYS   B N    1 
ATOM   4400 C  CA   . LYS   B 1 31  ? 50.358 -16.212 -15.043 1.00 19.11 ?  31  LYS   B CA   1 
ATOM   4401 C  C    . LYS   B 1 31  ? 48.961 -15.726 -14.657 1.00 16.90 ?  31  LYS   B C    1 
ATOM   4402 O  O    . LYS   B 1 31  ? 48.421 -14.808 -15.287 1.00 17.56 ?  31  LYS   B O    1 
ATOM   4403 C  CB   . LYS   B 1 31  ? 50.986 -15.392 -16.172 1.00 22.21 ?  31  LYS   B CB   1 
ATOM   4404 C  CG   . LYS   B 1 31  ? 52.411 -15.846 -16.495 1.00 25.54 ?  31  LYS   B CG   1 
ATOM   4405 C  CD   . LYS   B 1 31  ? 52.994 -15.100 -17.673 1.00 29.53 ?  31  LYS   B CD   1 
ATOM   4406 C  CE   . LYS   B 1 31  ? 54.477 -15.360 -17.797 1.00 32.58 ?  31  LYS   B CE   1 
ATOM   4407 N  NZ   . LYS   B 1 31  ? 55.186 -14.925 -16.563 1.00 34.21 ?  31  LYS   B NZ   1 
ATOM   4408 H  H    . LYS   B 1 31  ? 50.892 -18.116 -14.955 1.00 22.55 ?  31  LYS   B H    1 
ATOM   4409 H  HA   . LYS   B 1 31  ? 50.918 -16.130 -14.273 1.00 22.94 ?  31  LYS   B HA   1 
ATOM   4410 H  HB2  . LYS   B 1 31  ? 50.443 -15.484 -16.968 1.00 26.66 ?  31  LYS   B HB2  1 
ATOM   4411 H  HB3  . LYS   B 1 31  ? 51.013 -14.470 -15.883 1.00 26.66 ?  31  LYS   B HB3  1 
ATOM   4412 H  HG2  . LYS   B 1 31  ? 52.965 -15.692 -15.715 1.00 30.66 ?  31  LYS   B HG2  1 
ATOM   4413 H  HG3  . LYS   B 1 31  ? 52.398 -16.795 -16.708 1.00 30.66 ?  31  LYS   B HG3  1 
ATOM   4414 H  HD2  . LYS   B 1 31  ? 52.554 -15.402 -18.481 1.00 35.44 ?  31  LYS   B HD2  1 
ATOM   4415 H  HD3  . LYS   B 1 31  ? 52.853 -14.153 -17.541 1.00 35.44 ?  31  LYS   B HD3  1 
ATOM   4416 H  HE2  . LYS   B 1 31  ? 54.630 -16.311 -17.923 1.00 39.10 ?  31  LYS   B HE2  1 
ATOM   4417 H  HE3  . LYS   B 1 31  ? 54.826 -14.858 -18.549 1.00 39.10 ?  31  LYS   B HE3  1 
ATOM   4418 H  HZ1  . LYS   B 1 31  ? 56.062 -14.905 -16.707 1.00 41.07 ?  31  LYS   B HZ1  1 
ATOM   4419 H  HZ2  . LYS   B 1 31  ? 54.911 -14.111 -16.327 1.00 41.07 ?  31  LYS   B HZ2  1 
ATOM   4420 H  HZ3  . LYS   B 1 31  ? 55.014 -15.490 -15.896 1.00 41.07 ?  31  LYS   B HZ3  1 
ATOM   4421 N  N    . PRO   B 1 32  ? 48.352 -16.314 -13.624 1.00 14.64 ?  32  PRO   B N    1 
ATOM   4422 C  CA   . PRO   B 1 32  ? 46.978 -15.945 -13.264 1.00 13.96 ?  32  PRO   B CA   1 
ATOM   4423 C  C    . PRO   B 1 32  ? 46.909 -14.600 -12.561 1.00 13.99 ?  32  PRO   B C    1 
ATOM   4424 O  O    . PRO   B 1 32  ? 47.838 -14.177 -11.865 1.00 15.17 ?  32  PRO   B O    1 
ATOM   4425 C  CB   . PRO   B 1 32  ? 46.572 -17.056 -12.291 1.00 14.10 ?  32  PRO   B CB   1 
ATOM   4426 C  CG   . PRO   B 1 32  ? 47.863 -17.409 -11.614 1.00 14.24 ?  32  PRO   B CG   1 
ATOM   4427 C  CD   . PRO   B 1 32  ? 48.926 -17.291 -12.677 1.00 14.67 ?  32  PRO   B CD   1 
ATOM   4428 H  HA   . PRO   B 1 32  ? 46.399 -15.954 -14.048 1.00 16.76 ?  32  PRO   B HA   1 
ATOM   4429 H  HB2  . PRO   B 1 32  ? 45.923 -16.716 -11.654 1.00 16.93 ?  32  PRO   B HB2  1 
ATOM   4430 H  HB3  . PRO   B 1 32  ? 46.213 -17.815 -12.780 1.00 16.93 ?  32  PRO   B HB3  1 
ATOM   4431 H  HG2  . PRO   B 1 32  ? 48.036 -16.787 -10.888 1.00 17.10 ?  32  PRO   B HG2  1 
ATOM   4432 H  HG3  . PRO   B 1 32  ? 47.822 -18.319 -11.278 1.00 17.10 ?  32  PRO   B HG3  1 
ATOM   4433 H  HD2  . PRO   B 1 32  ? 49.746 -16.942 -12.296 1.00 17.61 ?  32  PRO   B HD2  1 
ATOM   4434 H  HD3  . PRO   B 1 32  ? 49.064 -18.142 -13.112 1.00 17.61 ?  32  PRO   B HD3  1 
ATOM   4435 N  N    . THR   B 1 33  ? 45.759 -13.939 -12.726 1.00 13.64 ?  33  THR   B N    1 
ATOM   4436 C  CA   . THR   B 1 33  ? 45.474 -12.760 -11.915 1.00 13.78 ?  33  THR   B CA   1 
ATOM   4437 C  C    . THR   B 1 33  ? 45.423 -13.115 -10.433 1.00 13.45 ?  33  THR   B C    1 
ATOM   4438 O  O    . THR   B 1 33  ? 45.902 -12.342 -9.589  1.00 14.40 ?  33  THR   B O    1 
ATOM   4439 C  CB   . THR   B 1 33  ? 44.156 -12.121 -12.360 1.00 14.32 ?  33  THR   B CB   1 
ATOM   4440 O  OG1  . THR   B 1 33  ? 44.188 -11.872 -13.769 1.00 14.51 ?  33  THR   B OG1  1 
ATOM   4441 C  CG2  . THR   B 1 33  ? 43.906 -10.824 -11.606 1.00 15.46 ?  33  THR   B CG2  1 
ATOM   4442 H  H    . THR   B 1 33  ? 45.138 -14.152 -13.290 1.00 16.38 ?  33  THR   B H    1 
ATOM   4443 H  HA   . THR   B 1 33  ? 46.177 -12.109 -12.048 1.00 16.54 ?  33  THR   B HA   1 
ATOM   4444 H  HB   . THR   B 1 33  ? 43.423 -12.733 -12.165 1.00 17.19 ?  33  THR   B HB   1 
ATOM   4445 H  HG1  . THR   B 1 33  ? 43.468 -11.503 -14.011 1.00 17.42 ?  33  THR   B HG1  1 
ATOM   4446 H  HG21 . THR   B 1 33  ? 43.151 -10.358 -11.992 1.00 18.56 ?  33  THR   B HG21 1 
ATOM   4447 H  HG22 . THR   B 1 33  ? 43.717 -11.012 -10.672 1.00 18.56 ?  33  THR   B HG22 1 
ATOM   4448 H  HG23 . THR   B 1 33  ? 44.691 -10.257 -11.661 1.00 18.56 ?  33  THR   B HG23 1 
ATOM   4449 N  N    . VAL   B 1 34  ? 44.866 -14.285 -10.096 1.00 12.68 ?  34  VAL   B N    1 
ATOM   4450 C  CA   . VAL   B 1 34  ? 44.663 -14.676 -8.704  1.00 12.06 ?  34  VAL   B CA   1 
ATOM   4451 C  C    . VAL   B 1 34  ? 45.082 -16.126 -8.533  1.00 11.36 ?  34  VAL   B C    1 
ATOM   4452 O  O    . VAL   B 1 34  ? 44.549 -17.011 -9.213  1.00 12.04 ?  34  VAL   B O    1 
ATOM   4453 C  CB   . VAL   B 1 34  ? 43.194 -14.530 -8.266  1.00 13.05 ?  34  VAL   B CB   1 
ATOM   4454 C  CG1  . VAL   B 1 34  ? 43.028 -14.984 -6.823  1.00 13.41 ?  34  VAL   B CG1  1 
ATOM   4455 C  CG2  . VAL   B 1 34  ? 42.705 -13.106 -8.453  1.00 14.17 ?  34  VAL   B CG2  1 
ATOM   4456 H  H    . VAL   B 1 34  ? 44.603 -14.875 -10.665 1.00 15.23 ?  34  VAL   B H    1 
ATOM   4457 H  HA   . VAL   B 1 34  ? 45.216 -14.123 -8.128  1.00 14.48 ?  34  VAL   B HA   1 
ATOM   4458 H  HB   . VAL   B 1 34  ? 42.648 -15.105 -8.825  1.00 15.67 ?  34  VAL   B HB   1 
ATOM   4459 H  HG11 . VAL   B 1 34  ? 42.179 -14.657 -6.485  1.00 16.10 ?  34  VAL   B HG11 1 
ATOM   4460 H  HG12 . VAL   B 1 34  ? 43.042 -15.955 -6.788  1.00 16.10 ?  34  VAL   B HG12 1 
ATOM   4461 H  HG13 . VAL   B 1 34  ? 43.755 -14.624 -6.290  1.00 16.10 ?  34  VAL   B HG13 1 
ATOM   4462 H  HG21 . VAL   B 1 34  ? 41.787 -13.045 -8.148  1.00 17.01 ?  34  VAL   B HG21 1 
ATOM   4463 H  HG22 . VAL   B 1 34  ? 43.268 -12.507 -7.939  1.00 17.01 ?  34  VAL   B HG22 1 
ATOM   4464 H  HG23 . VAL   B 1 34  ? 42.754 -12.875 -9.397  1.00 17.01 ?  34  VAL   B HG23 1 
ATOM   4465 N  N    . VAL   B 1 35  ? 45.990 -16.377 -7.598  1.00 10.84 ?  35  VAL   B N    1 
ATOM   4466 C  CA   . VAL   B 1 35  ? 46.218 -17.717 -7.074  1.00 10.63 ?  35  VAL   B CA   1 
ATOM   4467 C  C    . VAL   B 1 35  ? 45.684 -17.766 -5.652  1.00 10.42 ?  35  VAL   B C    1 
ATOM   4468 O  O    . VAL   B 1 35  ? 45.908 -16.843 -4.860  1.00 10.77 ?  35  VAL   B O    1 
ATOM   4469 C  CB   . VAL   B 1 35  ? 47.700 -18.147 -7.157  1.00 11.30 ?  35  VAL   B CB   1 
ATOM   4470 C  CG1  . VAL   B 1 35  ? 48.596 -17.315 -6.245  1.00 12.10 ?  35  VAL   B CG1  1 
ATOM   4471 C  CG2  . VAL   B 1 35  ? 47.826 -19.643 -6.828  1.00 12.29 ?  35  VAL   B CG2  1 
ATOM   4472 H  H    . VAL   B 1 35  ? 46.499 -15.777 -7.242  1.00 13.01 ?  35  VAL   B H    1 
ATOM   4473 H  HA   . VAL   B 1 35  ? 45.700 -18.347 -7.600  1.00 12.77 ?  35  VAL   B HA   1 
ATOM   4474 H  HB   . VAL   B 1 35  ? 48.006 -18.033 -8.069  1.00 13.56 ?  35  VAL   B HB   1 
ATOM   4475 H  HG11 . VAL   B 1 35  ? 49.516 -17.540 -6.431  1.00 14.53 ?  35  VAL   B HG11 1 
ATOM   4476 H  HG12 . VAL   B 1 35  ? 48.425 -16.385 -6.420  1.00 14.53 ?  35  VAL   B HG12 1 
ATOM   4477 H  HG13 . VAL   B 1 35  ? 48.379 -17.532 -5.322  1.00 14.53 ?  35  VAL   B HG13 1 
ATOM   4478 H  HG21 . VAL   B 1 35  ? 48.744 -19.926 -6.943  1.00 14.76 ?  35  VAL   B HG21 1 
ATOM   4479 H  HG22 . VAL   B 1 35  ? 47.546 -19.797 -5.908  1.00 14.76 ?  35  VAL   B HG22 1 
ATOM   4480 H  HG23 . VAL   B 1 35  ? 47.249 -20.158 -7.427  1.00 14.76 ?  35  VAL   B HG23 1 
ATOM   4481 N  N    . VAL   B 1 36  ? 44.958 -18.841 -5.336  1.00 10.51 ?  36  VAL   B N    1 
ATOM   4482 C  CA   . VAL   B 1 36  ? 44.412 -19.041 -4.006  1.00 10.05 ?  36  VAL   B CA   1 
ATOM   4483 C  C    . VAL   B 1 36  ? 45.420 -19.804 -3.153  1.00 10.03 ?  36  VAL   B C    1 
ATOM   4484 O  O    . VAL   B 1 36  ? 45.966 -20.836 -3.572  1.00 11.05 ?  36  VAL   B O    1 
ATOM   4485 C  CB   . VAL   B 1 36  ? 43.077 -19.798 -4.083  1.00 10.45 ?  36  VAL   B CB   1 
ATOM   4486 C  CG1  . VAL   B 1 36  ? 42.577 -20.174 -2.695  1.00 11.03 ?  36  VAL   B CG1  1 
ATOM   4487 C  CG2  . VAL   B 1 36  ? 42.040 -18.968 -4.819  1.00 10.98 ?  36  VAL   B CG2  1 
ATOM   4488 H  H    . VAL   B 1 36  ? 44.771 -19.477 -5.885  1.00 12.62 ?  36  VAL   B H    1 
ATOM   4489 H  HA   . VAL   B 1 36  ? 44.246 -18.180 -3.590  1.00 12.07 ?  36  VAL   B HA   1 
ATOM   4490 H  HB   . VAL   B 1 36  ? 43.206 -20.620 -4.579  1.00 12.55 ?  36  VAL   B HB   1 
ATOM   4491 H  HG11 . VAL   B 1 36  ? 41.636 -20.403 -2.748  1.00 13.25 ?  36  VAL   B HG11 1 
ATOM   4492 H  HG12 . VAL   B 1 36  ? 43.084 -20.927 -2.364  1.00 13.25 ?  36  VAL   B HG12 1 
ATOM   4493 H  HG13 . VAL   B 1 36  ? 42.692 -19.408 -2.103  1.00 13.25 ?  36  VAL   B HG13 1 
ATOM   4494 H  HG21 . VAL   B 1 36  ? 41.200 -19.454 -4.842  1.00 13.18 ?  36  VAL   B HG21 1 
ATOM   4495 H  HG22 . VAL   B 1 36  ? 41.920 -18.124 -4.354  1.00 13.18 ?  36  VAL   B HG22 1 
ATOM   4496 H  HG23 . VAL   B 1 36  ? 42.351 -18.805 -5.724  1.00 13.18 ?  36  VAL   B HG23 1 
ATOM   4497 N  N    . ASN   B 1 37  ? 45.640 -19.312 -1.938  1.00 10.12 ?  37  ASN   B N    1 
ATOM   4498 C  CA   . ASN   B 1 37  ? 46.394 -20.032 -0.926  1.00 10.38 ?  37  ASN   B CA   1 
ATOM   4499 C  C    . ASN   B 1 37  ? 45.446 -20.704 0.056   1.00 10.55 ?  37  ASN   B C    1 
ATOM   4500 O  O    . ASN   B 1 37  ? 44.430 -20.128 0.464   1.00 11.18 ?  37  ASN   B O    1 
ATOM   4501 C  CB   . ASN   B 1 37  ? 47.319 -19.087 -0.162  1.00 10.25 ?  37  ASN   B CB   1 
ATOM   4502 C  CG   . ASN   B 1 37  ? 48.164 -19.805 0.853   1.00 10.97 ?  37  ASN   B CG   1 
ATOM   4503 O  OD1  . ASN   B 1 37  ? 48.502 -20.980 0.670   1.00 11.71 ?  37  ASN   B OD1  1 
ATOM   4504 N  ND2  . ASN   B 1 37  ? 48.530 -19.105 1.922   1.00 11.00 ?  37  ASN   B ND2  1 
ATOM   4505 H  H    . ASN   B 1 37  ? 45.347 -18.544 -1.662  1.00 12.15 ?  37  ASN   B H    1 
ATOM   4506 H  HA   . ASN   B 1 37  ? 46.927 -20.719 -1.345  1.00 12.46 ?  37  ASN   B HA   1 
ATOM   4507 H  HB2  . ASN   B 1 37  ? 47.914 -18.658 -0.795  1.00 12.31 ?  37  ASN   B HB2  1 
ATOM   4508 H  HB3  . ASN   B 1 37  ? 46.789 -18.424 0.303   1.00 12.31 ?  37  ASN   B HB3  1 
ATOM   4509 H  HD21 . ASN   B 1 37  ? 49.023 -19.466 2.522   1.00 13.21 ?  37  ASN   B HD21 1 
ATOM   4510 H  HD22 . ASN   B 1 37  ? 48.284 -18.289 2.004   1.00 13.21 ?  37  ASN   B HD22 1 
ATOM   4511 N  N    . ALA   B 1 38  ? 45.794 -21.938 0.426   1.00 10.85 ?  38  ALA   B N    1 
ATOM   4512 C  CA   . ALA   B 1 38  ? 45.140 -22.682 1.507   1.00 11.41 ?  38  ALA   B CA   1 
ATOM   4513 C  C    . ALA   B 1 38  ? 45.721 -22.188 2.831   1.00 10.95 ?  38  ALA   B C    1 
ATOM   4514 O  O    . ALA   B 1 38  ? 46.622 -22.793 3.421   1.00 11.94 ?  38  ALA   B O    1 
ATOM   4515 C  CB   . ALA   B 1 38  ? 45.368 -24.176 1.322   1.00 12.43 ?  38  ALA   B CB   1 
ATOM   4516 H  H    . ALA   B 1 38  ? 46.438 -22.378 0.066   1.00 13.03 ?  38  ALA   B H    1 
ATOM   4517 H  HA   . ALA   B 1 38  ? 44.186 -22.505 1.499   1.00 13.70 ?  38  ALA   B HA   1 
ATOM   4518 H  HB1  . ALA   B 1 38  ? 44.924 -24.654 2.045   1.00 14.92 ?  38  ALA   B HB1  1 
ATOM   4519 H  HB2  . ALA   B 1 38  ? 44.993 -24.449 0.471   1.00 14.92 ?  38  ALA   B HB2  1 
ATOM   4520 H  HB3  . ALA   B 1 38  ? 46.318 -24.356 1.344   1.00 14.92 ?  38  ALA   B HB3  1 
ATOM   4521 N  N    . ALA   B 1 39  ? 45.201 -21.048 3.291   1.00 11.06 ?  39  ALA   B N    1 
ATOM   4522 C  CA   . ALA   B 1 39  ? 45.754 -20.313 4.418   1.00 11.30 ?  39  ALA   B CA   1 
ATOM   4523 C  C    . ALA   B 1 39  ? 45.143 -20.754 5.745   1.00 11.38 ?  39  ALA   B C    1 
ATOM   4524 O  O    . ALA   B 1 39  ? 44.114 -21.426 5.801   1.00 12.54 ?  39  ALA   B O    1 
ATOM   4525 C  CB   . ALA   B 1 39  ? 45.514 -18.813 4.226   1.00 12.05 ?  39  ALA   B CB   1 
ATOM   4526 H  H    . ALA   B 1 39  ? 44.503 -20.680 2.950   1.00 13.28 ?  39  ALA   B H    1 
ATOM   4527 H  HA   . ALA   B 1 39  ? 46.708 -20.463 4.456   1.00 13.57 ?  39  ALA   B HA   1 
ATOM   4528 H  HB1  . ALA   B 1 39  ? 45.888 -18.336 4.984   1.00 14.47 ?  39  ALA   B HB1  1 
ATOM   4529 H  HB2  . ALA   B 1 39  ? 45.948 -18.525 3.408   1.00 14.47 ?  39  ALA   B HB2  1 
ATOM   4530 H  HB3  . ALA   B 1 39  ? 44.560 -18.648 4.170   1.00 14.47 ?  39  ALA   B HB3  1 
ATOM   4531 N  N    . ASN   B 1 40  ? 45.792 -20.335 6.828   1.00 12.21 ?  40  ASN   B N    1 
ATOM   4532 C  CA   . ASN   B 1 40  ? 45.223 -20.374 8.165   1.00 12.75 ?  40  ASN   B CA   1 
ATOM   4533 C  C    . ASN   B 1 40  ? 45.039 -18.947 8.683   1.00 12.44 ?  40  ASN   B C    1 
ATOM   4534 O  O    . ASN   B 1 40  ? 45.455 -17.971 8.054   1.00 12.30 ?  40  ASN   B O    1 
ATOM   4535 C  CB   . ASN   B 1 40  ? 46.069 -21.241 9.111   1.00 13.45 ?  40  ASN   B CB   1 
ATOM   4536 C  CG   . ASN   B 1 40  ? 47.524 -20.841 9.131   1.00 14.51 ?  40  ASN   B CG   1 
ATOM   4537 O  OD1  . ASN   B 1 40  ? 47.843 -19.660 9.197   1.00 16.69 ?  40  ASN   B OD1  1 
ATOM   4538 N  ND2  . ASN   B 1 40  ? 48.416 -21.818 9.078   1.00 14.65 ?  40  ASN   B ND2  1 
ATOM   4539 H  H    . ASN   B 1 40  ? 46.592 -20.018 6.809   1.00 14.67 ?  40  ASN   B H    1 
ATOM   4540 H  HA   . ASN   B 1 40  ? 44.342 -20.775 8.116   1.00 15.31 ?  40  ASN   B HA   1 
ATOM   4541 H  HB2  . ASN   B 1 40  ? 45.722 -21.156 10.012  1.00 16.15 ?  40  ASN   B HB2  1 
ATOM   4542 H  HB3  . ASN   B 1 40  ? 46.017 -22.164 8.820   1.00 16.15 ?  40  ASN   B HB3  1 
ATOM   4543 H  HD21 . ASN   B 1 40  ? 49.256 -21.641 9.086   1.00 17.59 ?  40  ASN   B HD21 1 
ATOM   4544 H  HD22 . ASN   B 1 40  ? 48.150 -22.637 9.027   1.00 17.59 ?  40  ASN   B HD22 1 
ATOM   4545 N  N    . VAL   B 1 41  ? 44.387 -18.824 9.840   1.00 13.00 ?  41  VAL   B N    1 
ATOM   4546 C  CA   . VAL   B 1 41  ? 43.928 -17.506 10.287  1.00 13.61 ?  41  VAL   B CA   1 
ATOM   4547 C  C    . VAL   B 1 41  ? 45.078 -16.549 10.571  1.00 13.21 ?  41  VAL   B C    1 
ATOM   4548 O  O    . VAL   B 1 41  ? 44.896 -15.330 10.482  1.00 13.47 ?  41  VAL   B O    1 
ATOM   4549 C  CB   . VAL   B 1 41  ? 42.961 -17.588 11.486  1.00 15.32 ?  41  VAL   B CB   1 
ATOM   4550 C  CG1  . VAL   B 1 41  ? 41.655 -18.257 11.085  1.00 15.77 ?  41  VAL   B CG1  1 
ATOM   4551 C  CG2  . VAL   B 1 41  ? 43.616 -18.286 12.672  1.00 16.55 ?  41  VAL   B CG2  1 
ATOM   4552 H  H    . VAL   B 1 41  ? 44.203 -19.469 10.371  1.00 15.61 ?  41  VAL   B H    1 
ATOM   4553 H  HA   . VAL   B 1 41  ? 43.424 -17.112 9.560   1.00 16.34 ?  41  VAL   B HA   1 
ATOM   4554 H  HB   . VAL   B 1 41  ? 42.743 -16.685 11.768  1.00 18.39 ?  41  VAL   B HB   1 
ATOM   4555 H  HG11 . VAL   B 1 41  ? 41.055 -18.266 11.847  1.00 18.93 ?  41  VAL   B HG11 1 
ATOM   4556 H  HG12 . VAL   B 1 41  ? 41.256 -17.761 10.354  1.00 18.93 ?  41  VAL   B HG12 1 
ATOM   4557 H  HG13 . VAL   B 1 41  ? 41.843 -19.168 10.803  1.00 18.93 ?  41  VAL   B HG13 1 
ATOM   4558 H  HG21 . VAL   B 1 41  ? 42.990 -18.306 13.413  1.00 19.87 ?  41  VAL   B HG21 1 
ATOM   4559 H  HG22 . VAL   B 1 41  ? 43.850 -19.194 12.416  1.00 19.87 ?  41  VAL   B HG22 1 
ATOM   4560 H  HG23 . VAL   B 1 41  ? 44.414 -17.799 12.926  1.00 19.87 ?  41  VAL   B HG23 1 
ATOM   4561 N  N    . TYR   B 1 42  ? 46.248 -17.061 10.953  1.00 13.44 ?  42  TYR   B N    1 
ATOM   4562 C  CA   . TYR   B 1 42  ? 47.400 -16.210 11.221  1.00 13.81 ?  42  TYR   B CA   1 
ATOM   4563 C  C    . TYR   B 1 42  ? 48.365 -16.140 10.039  1.00 13.21 ?  42  TYR   B C    1 
ATOM   4564 O  O    . TYR   B 1 42  ? 49.456 -15.568 10.168  1.00 14.20 ?  42  TYR   B O    1 
ATOM   4565 C  CB   . TYR   B 1 42  ? 48.093 -16.619 12.526  1.00 15.65 ?  42  TYR   B CB   1 
ATOM   4566 C  CG   . TYR   B 1 42  ? 47.498 -15.931 13.752  1.00 15.65 ?  42  TYR   B CG   1 
ATOM   4567 C  CD1  . TYR   B 1 42  ? 47.705 -14.574 13.970  1.00 14.80 ?  42  TYR   B CD1  1 
ATOM   4568 C  CD2  . TYR   B 1 42  ? 46.733 -16.629 14.678  1.00 17.12 ?  42  TYR   B CD2  1 
ATOM   4569 C  CE1  . TYR   B 1 42  ? 47.175 -13.932 15.066  1.00 15.75 ?  42  TYR   B CE1  1 
ATOM   4570 C  CE2  . TYR   B 1 42  ? 46.199 -15.989 15.789  1.00 17.47 ?  42  TYR   B CE2  1 
ATOM   4571 C  CZ   . TYR   B 1 42  ? 46.423 -14.635 15.977  1.00 17.53 ?  42  TYR   B CZ   1 
ATOM   4572 O  OH   . TYR   B 1 42  ? 45.910 -13.973 17.075  1.00 19.76 ?  42  TYR   B OH   1 
ATOM   4573 H  H    . TYR   B 1 42  ? 46.400 -17.908 11.055  1.00 16.14 ?  42  TYR   B H    1 
ATOM   4574 H  HA   . TYR   B 1 42  ? 47.071 -15.313 11.355  1.00 16.58 ?  42  TYR   B HA   1 
ATOM   4575 H  HB2  . TYR   B 1 42  ? 48.004 -17.577 12.644  1.00 18.78 ?  42  TYR   B HB2  1 
ATOM   4576 H  HB3  . TYR   B 1 42  ? 49.032 -16.378 12.469  1.00 18.78 ?  42  TYR   B HB3  1 
ATOM   4577 H  HD1  . TYR   B 1 42  ? 48.216 -14.089 13.351  1.00 17.77 ?  42  TYR   B HD1  1 
ATOM   4578 H  HD2  . TYR   B 1 42  ? 46.583 -17.540 14.547  1.00 20.55 ?  42  TYR   B HD2  1 
ATOM   4579 H  HE1  . TYR   B 1 42  ? 47.332 -13.024 15.188  1.00 18.91 ?  42  TYR   B HE1  1 
ATOM   4580 H  HE2  . TYR   B 1 42  ? 45.691 -16.471 16.398  1.00 20.97 ?  42  TYR   B HE2  1 
ATOM   4581 H  HH   . TYR   B 1 42  ? 46.134 -13.167 17.043  1.00 23.72 ?  42  TYR   B HH   1 
ATOM   4582 N  N    . LEU   B 1 43  ? 47.966 -16.664 8.883   1.00 12.16 ?  43  LEU   B N    1 
ATOM   4583 C  CA   . LEU   B 1 43  ? 48.775 -16.599 7.671   1.00 11.99 ?  43  LEU   B CA   1 
ATOM   4584 C  C    . LEU   B 1 43  ? 50.188 -17.107 7.930   1.00 12.21 ?  43  LEU   B C    1 
ATOM   4585 O  O    . LEU   B 1 43  ? 51.171 -16.514 7.482   1.00 13.07 ?  43  LEU   B O    1 
ATOM   4586 C  CB   . LEU   B 1 43  ? 48.798 -15.195 7.060   1.00 12.31 ?  43  LEU   B CB   1 
ATOM   4587 C  CG   . LEU   B 1 43  ? 47.445 -14.577 6.684   1.00 12.63 ?  43  LEU   B CG   1 
ATOM   4588 C  CD1  . LEU   B 1 43  ? 47.668 -13.187 6.089   1.00 13.68 ?  43  LEU   B CD1  1 
ATOM   4589 C  CD2  . LEU   B 1 43  ? 46.688 -15.472 5.720   1.00 12.87 ?  43  LEU   B CD2  1 
ATOM   4590 H  H    . LEU   B 1 43  ? 47.221 -17.075 8.772   1.00 14.60 ?  43  LEU   B H    1 
ATOM   4591 H  HA   . LEU   B 1 43  ? 48.378 -17.189 7.010   1.00 14.40 ?  43  LEU   B HA   1 
ATOM   4592 H  HB2  . LEU   B 1 43  ? 49.223 -14.598 7.695   1.00 14.78 ?  43  LEU   B HB2  1 
ATOM   4593 H  HB3  . LEU   B 1 43  ? 49.330 -15.230 6.249   1.00 14.78 ?  43  LEU   B HB3  1 
ATOM   4594 H  HG   . LEU   B 1 43  ? 46.911 -14.472 7.486   1.00 15.16 ?  43  LEU   B HG   1 
ATOM   4595 H  HD11 . LEU   B 1 43  ? 46.810 -12.802 5.857   1.00 16.42 ?  43  LEU   B HD11 1 
ATOM   4596 H  HD12 . LEU   B 1 43  ? 48.114 -12.629 6.748   1.00 16.42 ?  43  LEU   B HD12 1 
ATOM   4597 H  HD13 . LEU   B 1 43  ? 48.222 -13.268 5.297   1.00 16.42 ?  43  LEU   B HD13 1 
ATOM   4598 H  HD21 . LEU   B 1 43  ? 45.896 -15.005 5.412   1.00 15.45 ?  43  LEU   B HD21 1 
ATOM   4599 H  HD22 . LEU   B 1 43  ? 47.263 -15.681 4.967   1.00 15.45 ?  43  LEU   B HD22 1 
ATOM   4600 H  HD23 . LEU   B 1 43  ? 46.435 -16.286 6.180   1.00 15.45 ?  43  LEU   B HD23 1 
ATOM   4601 N  N    . LYS   B 1 44  ? 50.285 -18.229 8.644   1.00 12.57 ?  44  LYS   B N    1 
ATOM   4602 C  CA   . LYS   B 1 44  ? 51.553 -18.900 8.894   1.00 13.03 ?  44  LYS   B CA   1 
ATOM   4603 C  C    . LYS   B 1 44  ? 51.676 -20.024 7.875   1.00 12.50 ?  44  LYS   B C    1 
ATOM   4604 O  O    . LYS   B 1 44  ? 50.979 -21.039 7.968   1.00 13.80 ?  44  LYS   B O    1 
ATOM   4605 C  CB   . LYS   B 1 44  ? 51.604 -19.403 10.336  1.00 14.89 ?  44  LYS   B CB   1 
ATOM   4606 C  CG   . LYS   B 1 44  ? 51.807 -18.282 11.347  1.00 17.59 ?  44  LYS   B CG   1 
ATOM   4607 C  CD   . LYS   B 1 44  ? 53.025 -17.447 10.939  1.00 21.17 ?  44  LYS   B CD   1 
ATOM   4608 C  CE   . LYS   B 1 44  ? 53.506 -16.520 12.018  1.00 24.27 ?  44  LYS   B CE   1 
ATOM   4609 N  NZ   . LYS   B 1 44  ? 54.729 -15.784 11.617  1.00 25.47 ?  44  LYS   B NZ   1 
ATOM   4610 H  H    . LYS   B 1 44  ? 49.611 -18.625 9.002   1.00 15.09 ?  44  LYS   B H    1 
ATOM   4611 H  HA   . LYS   B 1 44  ? 52.285 -18.288 8.727   1.00 15.65 ?  44  LYS   B HA   1 
ATOM   4612 H  HB2  . LYS   B 1 44  ? 50.757 -19.839 10.548  1.00 17.88 ?  44  LYS   B HB2  1 
ATOM   4613 H  HB3  . LYS   B 1 44  ? 52.331 -20.030 10.434  1.00 17.88 ?  44  LYS   B HB3  1 
ATOM   4614 H  HG2  . LYS   B 1 44  ? 51.026 -17.712 11.367  1.00 21.11 ?  44  LYS   B HG2  1 
ATOM   4615 H  HG3  . LYS   B 1 44  ? 51.974 -18.666 12.226  1.00 21.11 ?  44  LYS   B HG3  1 
ATOM   4616 H  HD2  . LYS   B 1 44  ? 53.749 -18.053 10.692  1.00 25.42 ?  44  LYS   B HD2  1 
ATOM   4617 H  HD3  . LYS   B 1 44  ? 52.782 -16.900 10.175  1.00 25.42 ?  44  LYS   B HD3  1 
ATOM   4618 H  HE2  . LYS   B 1 44  ? 52.811 -15.872 12.194  1.00 29.13 ?  44  LYS   B HE2  1 
ATOM   4619 H  HE3  . LYS   B 1 44  ? 53.708 -17.040 12.809  1.00 29.13 ?  44  LYS   B HE3  1 
ATOM   4620 H  HZ1  . LYS   B 1 44  ? 54.979 -15.240 12.273  1.00 30.57 ?  44  LYS   B HZ1  1 
ATOM   4621 H  HZ2  . LYS   B 1 44  ? 55.387 -16.357 11.446  1.00 30.57 ?  44  LYS   B HZ2  1 
ATOM   4622 H  HZ3  . LYS   B 1 44  ? 54.567 -15.303 10.885  1.00 30.57 ?  44  LYS   B HZ3  1 
ATOM   4623 N  N    . HIS   B 1 45  ? 52.525 -19.809 6.874   1.00 12.42 ?  45  HIS   B N    1 
ATOM   4624 C  CA   . HIS   B 1 45  ? 52.545 -20.643 5.672   1.00 12.56 ?  45  HIS   B CA   1 
ATOM   4625 C  C    . HIS   B 1 45  ? 53.561 -21.768 5.837   1.00 14.67 ?  45  HIS   B C    1 
ATOM   4626 O  O    . HIS   B 1 45  ? 54.624 -21.787 5.224   1.00 16.73 ?  45  HIS   B O    1 
ATOM   4627 C  CB   . HIS   B 1 45  ? 52.860 -19.790 4.455   1.00 12.74 ?  45  HIS   B CB   1 
ATOM   4628 C  CG   . HIS   B 1 45  ? 51.991 -18.586 4.340   1.00 12.27 ?  45  HIS   B CG   1 
ATOM   4629 N  ND1  . HIS   B 1 45  ? 50.613 -18.659 4.312   1.00 12.32 ?  45  HIS   B ND1  1 
ATOM   4630 C  CD2  . HIS   B 1 45  ? 52.311 -17.273 4.258   1.00 13.00 ?  45  HIS   B CD2  1 
ATOM   4631 C  CE1  . HIS   B 1 45  ? 50.128 -17.437 4.201   1.00 12.20 ?  45  HIS   B CE1  1 
ATOM   4632 N  NE2  . HIS   B 1 45  ? 51.134 -16.578 4.168   1.00 12.71 ?  45  HIS   B NE2  1 
ATOM   4633 H  H    . HIS   B 1 45  ? 53.093 -19.162 6.859   1.00 14.91 ?  45  HIS   B H    1 
ATOM   4634 H  HA   . HIS   B 1 45  ? 51.663 -21.039 5.543   1.00 15.08 ?  45  HIS   B HA   1 
ATOM   4635 H  HB2  . HIS   B 1 45  ? 53.780 -19.495 4.509   1.00 15.30 ?  45  HIS   B HB2  1 
ATOM   4636 H  HB3  . HIS   B 1 45  ? 52.734 -20.330 3.654   1.00 15.30 ?  45  HIS   B HB3  1 
ATOM   4637 H  HD2  . HIS   B 1 45  ? 53.169 -16.911 4.260   1.00 15.61 ?  45  HIS   B HD2  1 
ATOM   4638 H  HE1  . HIS   B 1 45  ? 49.226 -17.214 4.152   1.00 14.65 ?  45  HIS   B HE1  1 
ATOM   4639 H  HE2  . HIS   B 1 45  ? 51.060 -15.722 4.109   1.00 15.26 ?  45  HIS   B HE2  1 
ATOM   4640 N  N    A GLY   B 1 46  ? 53.185 -22.739 6.666   0.64 15.72 ?  46  GLY   B N    1 
ATOM   4641 N  N    B GLY   B 1 46  ? 53.198 -22.724 6.685   0.36 15.58 ?  46  GLY   B N    1 
ATOM   4642 C  CA   A GLY   B 1 46  ? 54.104 -23.783 7.076   0.64 17.72 ?  46  GLY   B CA   1 
ATOM   4643 C  CA   B GLY   B 1 46  ? 54.117 -23.784 7.045   0.36 16.97 ?  46  GLY   B CA   1 
ATOM   4644 C  C    A GLY   B 1 46  ? 54.174 -25.014 6.192   0.64 19.26 ?  46  GLY   B C    1 
ATOM   4645 C  C    B GLY   B 1 46  ? 54.166 -24.939 6.066   0.36 18.25 ?  46  GLY   B C    1 
ATOM   4646 O  O    A GLY   B 1 46  ? 55.266 -25.471 5.843   0.64 22.02 ?  46  GLY   B O    1 
ATOM   4647 O  O    B GLY   B 1 46  ? 55.221 -25.244 5.499   0.36 19.51 ?  46  GLY   B O    1 
ATOM   4648 H  H    A GLY   B 1 46  ? 52.397 -22.799 7.019   0.64 18.87 ?  46  GLY   B H    1 
ATOM   4649 H  H    B GLY   B 1 46  ? 52.424 -22.770 7.071   0.36 18.71 ?  46  GLY   B H    1 
ATOM   4650 H  HA2  A GLY   B 1 46  ? 54.994 -23.403 7.132   0.64 21.27 ?  46  GLY   B HA2  1 
ATOM   4651 H  HA2  B GLY   B 1 46  ? 55.008 -23.409 7.118   0.36 20.38 ?  46  GLY   B HA2  1 
ATOM   4652 H  HA3  A GLY   B 1 46  ? 53.853 -24.084 7.962   0.64 21.27 ?  46  GLY   B HA3  1 
ATOM   4653 H  HA3  B GLY   B 1 46  ? 53.866 -24.131 7.916   0.36 20.38 ?  46  GLY   B HA3  1 
ATOM   4654 N  N    . GLY   B 1 47  ? 53.023 -25.586 5.843   1.00 18.40 ?  47  GLY   B N    1 
ATOM   4655 C  CA   . GLY   B 1 47  ? 52.983 -26.857 5.146   1.00 16.71 ?  47  GLY   B CA   1 
ATOM   4656 C  C    . GLY   B 1 47  ? 52.051 -26.842 3.950   1.00 14.50 ?  47  GLY   B C    1 
ATOM   4657 O  O    . GLY   B 1 47  ? 51.396 -25.841 3.660   1.00 14.45 ?  47  GLY   B O    1 
ATOM   4658 H  H    A GLY   B 1 47  ? 52.246 -25.263 6.024   0.64 22.08 ?  47  GLY   B H    1 
ATOM   4659 H  H    B GLY   B 1 47  ? 52.250 -25.303 6.095   0.36 22.08 ?  47  GLY   B H    1 
ATOM   4660 H  HA2  . GLY   B 1 47  ? 53.873 -27.089 4.836   1.00 20.06 ?  47  GLY   B HA2  1 
ATOM   4661 H  HA3  . GLY   B 1 47  ? 52.686 -27.547 5.759   1.00 20.06 ?  47  GLY   B HA3  1 
ATOM   4662 N  N    . GLY   B 1 48  ? 52.002 -27.985 3.268   1.00 13.59 ?  48  GLY   B N    1 
ATOM   4663 C  CA   . GLY   B 1 48  ? 51.080 -28.137 2.158   1.00 13.36 ?  48  GLY   B CA   1 
ATOM   4664 C  C    . GLY   B 1 48  ? 51.218 -27.026 1.146   1.00 12.82 ?  48  GLY   B C    1 
ATOM   4665 O  O    . GLY   B 1 48  ? 52.318 -26.554 0.842   1.00 13.31 ?  48  GLY   B O    1 
ATOM   4666 H  H    . GLY   B 1 48  ? 52.495 -28.667 3.421   1.00 16.32 ?  48  GLY   B H    1 
ATOM   4667 H  HA2  . GLY   B 1 48  ? 51.247 -28.984 1.713   1.00 16.04 ?  48  GLY   B HA2  1 
ATOM   4668 H  HA3  . GLY   B 1 48  ? 50.171 -28.137 2.489   1.00 16.04 ?  48  GLY   B HA3  1 
ATOM   4669 N  N    . VAL   B 1 49  ? 50.073 -26.596 0.616   1.00 12.78 ?  49  VAL   B N    1 
ATOM   4670 C  CA   . VAL   B 1 49  ? 50.057 -25.573 -0.427  1.00 12.64 ?  49  VAL   B CA   1 
ATOM   4671 C  C    . VAL   B 1 49  ? 50.714 -24.287 0.059   1.00 11.71 ?  49  VAL   B C    1 
ATOM   4672 O  O    . VAL   B 1 49  ? 51.499 -23.666 -0.664  1.00 12.41 ?  49  VAL   B O    1 
ATOM   4673 C  CB   . VAL   B 1 49  ? 48.613 -25.320 -0.906  1.00 13.79 ?  49  VAL   B CB   1 
ATOM   4674 C  CG1  . VAL   B 1 49  ? 48.534 -24.081 -1.789  1.00 14.02 ?  49  VAL   B CG1  1 
ATOM   4675 C  CG2  . VAL   B 1 49  ? 48.065 -26.541 -1.647  1.00 15.13 ?  49  VAL   B CG2  1 
ATOM   4676 H  H    . VAL   B 1 49  ? 49.287 -26.874 0.843   1.00 15.35 ?  49  VAL   B H    1 
ATOM   4677 H  HA   . VAL   B 1 49  ? 50.556 -25.894 -1.192  1.00 15.18 ?  49  VAL   B HA   1 
ATOM   4678 H  HB   . VAL   B 1 49  ? 48.041 -25.168 -0.139  1.00 16.55 ?  49  VAL   B HB   1 
ATOM   4679 H  HG11 . VAL   B 1 49  ? 47.698 -24.100 -2.290  1.00 16.83 ?  49  VAL   B HG11 1 
ATOM   4680 H  HG12 . VAL   B 1 49  ? 48.559 -23.290 -1.230  1.00 16.83 ?  49  VAL   B HG12 1 
ATOM   4681 H  HG13 . VAL   B 1 49  ? 49.281 -24.083 -2.404  1.00 16.83 ?  49  VAL   B HG13 1 
ATOM   4682 H  HG21 . VAL   B 1 49  ? 47.154 -26.361 -1.937  1.00 18.16 ?  49  VAL   B HG21 1 
ATOM   4683 H  HG22 . VAL   B 1 49  ? 48.625 -26.721 -2.421  1.00 18.16 ?  49  VAL   B HG22 1 
ATOM   4684 H  HG23 . VAL   B 1 49  ? 48.074 -27.304 -1.049  1.00 18.16 ?  49  VAL   B HG23 1 
ATOM   4685 N  N    . ALA   B 1 50  ? 50.364 -23.835 1.263   1.00 11.64 ?  50  ALA   B N    1 
ATOM   4686 C  CA   . ALA   B 1 50  ? 50.885 -22.557 1.735   1.00 11.40 ?  50  ALA   B CA   1 
ATOM   4687 C  C    . ALA   B 1 50  ? 52.403 -22.590 1.846   1.00 11.67 ?  50  ALA   B C    1 
ATOM   4688 O  O    . ALA   B 1 50  ? 53.087 -21.624 1.482   1.00 11.64 ?  50  ALA   B O    1 
ATOM   4689 C  CB   . ALA   B 1 50  ? 50.257 -22.203 3.078   1.00 11.61 ?  50  ALA   B CB   1 
ATOM   4690 H  H    . ALA   B 1 50  ? 49.839 -24.238 1.807   1.00 13.97 ?  50  ALA   B H    1 
ATOM   4691 H  HA   . ALA   B 1 50  ? 50.655 -21.864 1.101   1.00 13.69 ?  50  ALA   B HA   1 
ATOM   4692 H  HB1  . ALA   B 1 50  ? 50.614 -21.351 3.379   1.00 13.94 ?  50  ALA   B HB1  1 
ATOM   4693 H  HB2  . ALA   B 1 50  ? 49.295 -22.134 2.966   1.00 13.94 ?  50  ALA   B HB2  1 
ATOM   4694 H  HB3  . ALA   B 1 50  ? 50.467 -22.896 3.721   1.00 13.94 ?  50  ALA   B HB3  1 
ATOM   4695 N  N    . GLY   B 1 51  ? 52.950 -23.685 2.366   1.00 12.18 ?  51  GLY   B N    1 
ATOM   4696 C  CA   . GLY   B 1 51  ? 54.393 -23.794 2.440   1.00 12.75 ?  51  GLY   B CA   1 
ATOM   4697 C  C    . GLY   B 1 51  ? 55.044 -23.748 1.073   1.00 12.56 ?  51  GLY   B C    1 
ATOM   4698 O  O    . GLY   B 1 51  ? 56.088 -23.114 0.894   1.00 13.65 ?  51  GLY   B O    1 
ATOM   4699 H  H    . GLY   B 1 51  ? 52.520 -24.366 2.668   1.00 14.62 ?  51  GLY   B H    1 
ATOM   4700 H  HA2  . GLY   B 1 51  ? 54.749 -23.064 2.971   1.00 15.31 ?  51  GLY   B HA2  1 
ATOM   4701 H  HA3  . GLY   B 1 51  ? 54.638 -24.632 2.867   1.00 15.31 ?  51  GLY   B HA3  1 
ATOM   4702 N  N    . ALA   B 1 52  ? 54.435 -24.409 0.088   1.00 12.30 ?  52  ALA   B N    1 
ATOM   4703 C  CA   . ALA   B 1 52  ? 54.998 -24.419 -1.256  1.00 12.89 ?  52  ALA   B CA   1 
ATOM   4704 C  C    . ALA   B 1 52  ? 54.922 -23.042 -1.906  1.00 12.17 ?  52  ALA   B C    1 
ATOM   4705 O  O    . ALA   B 1 52  ? 55.894 -22.591 -2.532  1.00 12.77 ?  52  ALA   B O    1 
ATOM   4706 C  CB   . ALA   B 1 52  ? 54.286 -25.457 -2.116  1.00 13.47 ?  52  ALA   B CB   1 
ATOM   4707 H  H    . ALA   B 1 52  ? 53.696 -24.844 0.172   1.00 14.76 ?  52  ALA   B H    1 
ATOM   4708 H  HA   . ALA   B 1 52  ? 55.929 -24.666 -1.201  1.00 15.48 ?  52  ALA   B HA   1 
ATOM   4709 H  HB1  . ALA   B 1 52  ? 54.678 -25.450 -3.006  1.00 16.18 ?  52  ALA   B HB1  1 
ATOM   4710 H  HB2  . ALA   B 1 52  ? 54.406 -26.333 -1.714  1.00 16.18 ?  52  ALA   B HB2  1 
ATOM   4711 H  HB3  . ALA   B 1 52  ? 53.345 -25.241 -2.168  1.00 16.18 ?  52  ALA   B HB3  1 
ATOM   4712 N  N    . LEU   B 1 53  ? 53.777 -22.361 -1.788  1.00 11.86 ?  53  LEU   B N    1 
ATOM   4713 C  CA   . LEU   B 1 53  ? 53.672 -21.021 -2.358  1.00 12.02 ?  53  LEU   B CA   1 
ATOM   4714 C  C    . LEU   B 1 53  ? 54.681 -20.083 -1.709  1.00 11.84 ?  53  LEU   B C    1 
ATOM   4715 O  O    . LEU   B 1 53  ? 55.385 -19.335 -2.395  1.00 12.53 ?  53  LEU   B O    1 
ATOM   4716 C  CB   . LEU   B 1 53  ? 52.249 -20.474 -2.196  1.00 12.71 ?  53  LEU   B CB   1 
ATOM   4717 C  CG   . LEU   B 1 53  ? 51.115 -21.214 -2.918  1.00 12.55 ?  53  LEU   B CG   1 
ATOM   4718 C  CD1  . LEU   B 1 53  ? 49.780 -20.593 -2.569  1.00 13.89 ?  53  LEU   B CD1  1 
ATOM   4719 C  CD2  . LEU   B 1 53  ? 51.308 -21.220 -4.428  1.00 14.46 ?  53  LEU   B CD2  1 
ATOM   4720 H  H    . LEU   B 1 53  ? 53.068 -22.638 -1.392  1.00 14.25 ?  53  LEU   B H    1 
ATOM   4721 H  HA   . LEU   B 1 53  ? 53.874 -21.063 -3.309  1.00 14.43 ?  53  LEU   B HA   1 
ATOM   4722 H  HB2  . LEU   B 1 53  ? 52.037 -20.481 -1.252  1.00 15.26 ?  53  LEU   B HB2  1 
ATOM   4723 H  HB3  . LEU   B 1 53  ? 52.242 -19.561 -2.520  1.00 15.26 ?  53  LEU   B HB3  1 
ATOM   4724 H  HG   . LEU   B 1 53  ? 51.098 -22.134 -2.616  1.00 15.06 ?  53  LEU   B HG   1 
ATOM   4725 H  HD11 . LEU   B 1 53  ? 49.075 -21.079 -3.031  1.00 16.67 ?  53  LEU   B HD11 1 
ATOM   4726 H  HD12 . LEU   B 1 53  ? 49.642 -20.658 -1.607  1.00 16.67 ?  53  LEU   B HD12 1 
ATOM   4727 H  HD13 . LEU   B 1 53  ? 49.776 -19.666 -2.841  1.00 16.67 ?  53  LEU   B HD13 1 
ATOM   4728 H  HD21 . LEU   B 1 53  ? 50.628 -21.784 -4.830  1.00 17.37 ?  53  LEU   B HD21 1 
ATOM   4729 H  HD22 . LEU   B 1 53  ? 51.221 -20.314 -4.762  1.00 17.37 ?  53  LEU   B HD22 1 
ATOM   4730 H  HD23 . LEU   B 1 53  ? 52.188 -21.569 -4.636  1.00 17.37 ?  53  LEU   B HD23 1 
ATOM   4731 N  N    . ASN   B 1 54  ? 54.768 -20.103 -0.382  1.00 11.58 ?  54  ASN   B N    1 
ATOM   4732 C  CA   . ASN   B 1 54  ? 55.687 -19.193 0.286   1.00 12.19 ?  54  ASN   B CA   1 
ATOM   4733 C  C    . ASN   B 1 54  ? 57.130 -19.481 -0.108  1.00 12.68 ?  54  ASN   B C    1 
ATOM   4734 O  O    . ASN   B 1 54  ? 57.916 -18.551 -0.338  1.00 12.84 ?  54  ASN   B O    1 
ATOM   4735 C  CB   . ASN   B 1 54  ? 55.531 -19.274 1.796   1.00 13.09 ?  54  ASN   B CB   1 
ATOM   4736 C  CG   . ASN   B 1 54  ? 56.507 -18.362 2.503   1.00 13.31 ?  54  ASN   B CG   1 
ATOM   4737 O  OD1  . ASN   B 1 54  ? 56.518 -17.151 2.265   1.00 13.47 ?  54  ASN   B OD1  1 
ATOM   4738 N  ND2  . ASN   B 1 54  ? 57.351 -18.931 3.354   1.00 14.84 ?  54  ASN   B ND2  1 
ATOM   4739 H  H    . ASN   B 1 54  ? 54.321 -20.623 0.135   1.00 13.90 ?  54  ASN   B H    1 
ATOM   4740 H  HA   . ASN   B 1 54  ? 55.478 -18.288 0.013   1.00 14.63 ?  54  ASN   B HA   1 
ATOM   4741 H  HB2  . ASN   B 1 54  ? 54.633 -19.003 2.043   1.00 15.72 ?  54  ASN   B HB2  1 
ATOM   4742 H  HB3  . ASN   B 1 54  ? 55.701 -20.182 2.091   1.00 15.72 ?  54  ASN   B HB3  1 
ATOM   4743 H  HD21 . ASN   B 1 54  ? 57.934 -18.451 3.771   1.00 17.82 ?  54  ASN   B HD21 1 
ATOM   4744 H  HD22 . ASN   B 1 54  ? 57.327 -19.781 3.484   1.00 17.82 ?  54  ASN   B HD22 1 
ATOM   4745 N  N    . LYS   B 1 55  ? 57.506 -20.761 -0.172  1.00 13.39 ?  55  LYS   B N    1 
ATOM   4746 C  CA   . LYS   B 1 55  ? 58.859 -21.111 -0.592  1.00 14.38 ?  55  LYS   B CA   1 
ATOM   4747 C  C    . LYS   B 1 55  ? 59.159 -20.570 -1.983  1.00 14.21 ?  55  LYS   B C    1 
ATOM   4748 O  O    . LYS   B 1 55  ? 60.259 -20.064 -2.234  1.00 14.76 ?  55  LYS   B O    1 
ATOM   4749 C  CB   . LYS   B 1 55  ? 59.045 -22.628 -0.540  1.00 16.49 ?  55  LYS   B CB   1 
ATOM   4750 C  CG   . LYS   B 1 55  ? 60.411 -23.096 -0.996  1.00 20.45 ?  55  LYS   B CG   1 
ATOM   4751 C  CD   . LYS   B 1 55  ? 60.582 -24.591 -0.809  1.00 23.93 ?  55  LYS   B CD   1 
ATOM   4752 C  CE   . LYS   B 1 55  ? 60.689 -24.966 0.665   1.00 26.95 ?  55  LYS   B CE   1 
ATOM   4753 N  NZ   . LYS   B 1 55  ? 61.062 -26.387 0.847   1.00 28.41 ?  55  LYS   B NZ   1 
ATOM   4754 H  H    . LYS   B 1 55  ? 56.999 -21.430 0.014   1.00 16.07 ?  55  LYS   B H    1 
ATOM   4755 H  HA   . LYS   B 1 55  ? 59.490 -20.711 0.020   1.00 17.26 ?  55  LYS   B HA   1 
ATOM   4756 H  HB2  . LYS   B 1 55  ? 58.915 -22.918 0.378   1.00 19.80 ?  55  LYS   B HB2  1 
ATOM   4757 H  HB3  . LYS   B 1 55  ? 58.379 -23.045 -1.110  1.00 19.80 ?  55  LYS   B HB3  1 
ATOM   4758 H  HG2  . LYS   B 1 55  ? 60.519 -22.896 -1.938  1.00 24.55 ?  55  LYS   B HG2  1 
ATOM   4759 H  HG3  . LYS   B 1 55  ? 61.092 -22.643 -0.475  1.00 24.55 ?  55  LYS   B HG3  1 
ATOM   4760 H  HD2  . LYS   B 1 55  ? 59.816 -25.055 -1.184  1.00 28.73 ?  55  LYS   B HD2  1 
ATOM   4761 H  HD3  . LYS   B 1 55  ? 61.397 -24.880 -1.252  1.00 28.73 ?  55  LYS   B HD3  1 
ATOM   4762 H  HE2  . LYS   B 1 55  ? 61.368 -24.410 1.083   1.00 32.35 ?  55  LYS   B HE2  1 
ATOM   4763 H  HE3  . LYS   B 1 55  ? 59.829 -24.816 1.093   1.00 32.35 ?  55  LYS   B HE3  1 
ATOM   4764 H  HZ1  . LYS   B 1 55  ? 61.096 -26.581 1.714   1.00 34.10 ?  55  LYS   B HZ1  1 
ATOM   4765 H  HZ2  . LYS   B 1 55  ? 60.458 -26.909 0.455   1.00 34.10 ?  55  LYS   B HZ2  1 
ATOM   4766 H  HZ3  . LYS   B 1 55  ? 61.858 -26.539 0.483   1.00 34.10 ?  55  LYS   B HZ3  1 
ATOM   4767 N  N    . ALA   B 1 56  ? 58.188 -20.655 -2.900  1.00 13.80 ?  56  ALA   B N    1 
ATOM   4768 C  CA   . ALA   B 1 56  ? 58.407 -20.155 -4.251  1.00 14.48 ?  56  ALA   B CA   1 
ATOM   4769 C  C    . ALA   B 1 56  ? 58.689 -18.661 -4.251  1.00 14.16 ?  56  ALA   B C    1 
ATOM   4770 O  O    . ALA   B 1 56  ? 59.412 -18.167 -5.124  1.00 15.07 ?  56  ALA   B O    1 
ATOM   4771 C  CB   . ALA   B 1 56  ? 57.206 -20.478 -5.141  1.00 15.24 ?  56  ALA   B CB   1 
ATOM   4772 H  H    . ALA   B 1 56  ? 57.400 -20.982 -2.763  1.00 16.57 ?  56  ALA   B H    1 
ATOM   4773 H  HA   . ALA   B 1 56  ? 59.179 -20.597 -4.627  1.00 17.39 ?  56  ALA   B HA   1 
ATOM   4774 H  HB1  . ALA   B 1 56  ? 57.375 -20.142 -6.038  1.00 18.29 ?  56  ALA   B HB1  1 
ATOM   4775 H  HB2  . ALA   B 1 56  ? 57.083 -21.441 -5.171  1.00 18.29 ?  56  ALA   B HB2  1 
ATOM   4776 H  HB3  . ALA   B 1 56  ? 56.413 -20.056 -4.777  1.00 18.29 ?  56  ALA   B HB3  1 
ATOM   4777 N  N    . THR   B 1 57  ? 58.129 -17.926 -3.288  1.00 13.94 ?  57  THR   B N    1 
ATOM   4778 C  CA   . THR   B 1 57  ? 58.365 -16.492 -3.170  1.00 13.98 ?  57  THR   B CA   1 
ATOM   4779 C  C    . THR   B 1 57  ? 59.613 -16.161 -2.361  1.00 14.86 ?  57  THR   B C    1 
ATOM   4780 O  O    . THR   B 1 57  ? 59.854 -14.985 -2.065  1.00 15.35 ?  57  THR   B O    1 
ATOM   4781 C  CB   . THR   B 1 57  ? 57.162 -15.767 -2.537  1.00 13.17 ?  57  THR   B CB   1 
ATOM   4782 O  OG1  . THR   B 1 57  ? 57.143 -15.976 -1.116  1.00 13.52 ?  57  THR   B OG1  1 
ATOM   4783 C  CG2  . THR   B 1 57  ? 55.845 -16.196 -3.171  1.00 13.24 ?  57  THR   B CG2  1 
ATOM   4784 H  H    . THR   B 1 57  ? 57.592 -18.240 -2.687  1.00 16.74 ?  57  THR   B H    1 
ATOM   4785 H  HA   . THR   B 1 57  ? 58.483 -16.128 -4.060  1.00 16.78 ?  57  THR   B HA   1 
ATOM   4786 H  HB   . THR   B 1 57  ? 57.259 -14.815 -2.705  1.00 15.81 ?  57  THR   B HB   1 
ATOM   4787 H  HG1  . THR   B 1 57  ? 57.071 -16.799 -0.953  1.00 16.23 ?  57  THR   B HG1  1 
ATOM   4788 H  HG21 . THR   B 1 57  ? 55.120 -15.644 -2.849  1.00 15.90 ?  57  THR   B HG21 1 
ATOM   4789 H  HG22 . THR   B 1 57  ? 55.898 -16.120 -4.138  1.00 15.90 ?  57  THR   B HG22 1 
ATOM   4790 H  HG23 . THR   B 1 57  ? 55.655 -17.123 -2.947  1.00 15.90 ?  57  THR   B HG23 1 
ATOM   4791 N  N    . ASN   B 1 58  ? 60.404 -17.165 -1.993  1.00 15.51 ?  58  ASN   B N    1 
ATOM   4792 C  CA   . ASN   B 1 58  ? 61.603 -16.950 -1.191  1.00 18.33 ?  58  ASN   B CA   1 
ATOM   4793 C  C    . ASN   B 1 58  ? 61.270 -16.233 0.118   1.00 16.24 ?  58  ASN   B C    1 
ATOM   4794 O  O    . ASN   B 1 58  ? 62.014 -15.363 0.582   1.00 16.93 ?  58  ASN   B O    1 
ATOM   4795 C  CB   . ASN   B 1 58  ? 62.689 -16.209 -1.979  1.00 26.26 ?  58  ASN   B CB   1 
ATOM   4796 C  CG   . ASN   B 1 58  ? 64.062 -16.356 -1.354  1.00 35.50 ?  58  ASN   B CG   1 
ATOM   4797 O  OD1  . ASN   B 1 58  ? 64.364 -17.370 -0.725  1.00 38.02 ?  58  ASN   B OD1  1 
ATOM   4798 N  ND2  . ASN   B 1 58  ? 64.901 -15.341 -1.520  1.00 40.07 ?  58  ASN   B ND2  1 
ATOM   4799 H  H    . ASN   B 1 58  ? 60.260 -17.992 -2.191  1.00 18.62 ?  58  ASN   B H    1 
ATOM   4800 H  HA   . ASN   B 1 58  ? 61.966 -17.822 -0.964  1.00 22.00 ?  58  ASN   B HA   1 
ATOM   4801 H  HB2  . ASN   B 1 58  ? 62.729 -16.569 -2.883  1.00 31.52 ?  58  ASN   B HB2  1 
ATOM   4802 H  HB3  . ASN   B 1 58  ? 62.472 -15.266 -2.009  1.00 31.52 ?  58  ASN   B HB3  1 
ATOM   4803 H  HD21 . ASN   B 1 58  ? 65.692 -15.377 -1.184  1.00 48.10 ?  58  ASN   B HD21 1 
ATOM   4804 H  HD22 . ASN   B 1 58  ? 64.654 -14.647 -1.964  1.00 48.10 ?  58  ASN   B HD22 1 
ATOM   4805 N  N    . ASN   B 1 59  ? 60.140 -16.607 0.721   1.00 15.23 ?  59  ASN   B N    1 
ATOM   4806 C  CA   . ASN   B 1 59  ? 59.665 -16.137 2.021   1.00 15.13 ?  59  ASN   B CA   1 
ATOM   4807 C  C    . ASN   B 1 59  ? 59.068 -14.734 1.965   1.00 14.37 ?  59  ASN   B C    1 
ATOM   4808 O  O    . ASN   B 1 59  ? 58.636 -14.225 3.007   1.00 14.36 ?  59  ASN   B O    1 
ATOM   4809 C  CB   . ASN   B 1 59  ? 60.738 -16.191 3.124   1.00 16.30 ?  59  ASN   B CB   1 
ATOM   4810 C  CG   . ASN   B 1 59  ? 60.149 -16.371 4.507   1.00 17.18 ?  59  ASN   B CG   1 
ATOM   4811 O  OD1  . ASN   B 1 59  ? 59.324 -17.259 4.737   1.00 17.28 ?  59  ASN   B OD1  1 
ATOM   4812 N  ND2  . ASN   B 1 59  ? 60.567 -15.527 5.440   1.00 17.79 ?  59  ASN   B ND2  1 
ATOM   4813 H  H    . ASN   B 1 59  ? 59.600 -17.179 0.370   1.00 18.29 ?  59  ASN   B H    1 
ATOM   4814 H  HA   . ASN   B 1 59  ? 58.960 -16.735 2.303   1.00 18.16 ?  59  ASN   B HA   1 
ATOM   4815 H  HB2  . ASN   B 1 59  ? 61.336 -16.940 2.961   1.00 19.57 ?  59  ASN   B HB2  1 
ATOM   4816 H  HB3  . ASN   B 1 59  ? 61.242 -15.362 3.125   1.00 19.57 ?  59  ASN   B HB3  1 
ATOM   4817 H  HD21 . ASN   B 1 59  ? 60.262 -15.587 6.243   1.00 21.35 ?  59  ASN   B HD21 1 
ATOM   4818 H  HD22 . ASN   B 1 59  ? 61.143 -14.918 5.246   1.00 21.35 ?  59  ASN   B HD22 1 
ATOM   4819 N  N    . ALA   B 1 60  ? 59.011 -14.094 0.794   1.00 14.28 ?  60  ALA   B N    1 
ATOM   4820 C  CA   . ALA   B 1 60  ? 58.416 -12.763 0.719   1.00 14.22 ?  60  ALA   B CA   1 
ATOM   4821 C  C    . ALA   B 1 60  ? 56.947 -12.789 1.115   1.00 13.25 ?  60  ALA   B C    1 
ATOM   4822 O  O    . ALA   B 1 60  ? 56.443 -11.842 1.732   1.00 13.63 ?  60  ALA   B O    1 
ATOM   4823 C  CB   . ALA   B 1 60  ? 58.585 -12.185 -0.685  1.00 15.24 ?  60  ALA   B CB   1 
ATOM   4824 H  H    . ALA   B 1 60  ? 59.306 -14.408 0.049   1.00 17.14 ?  60  ALA   B H    1 
ATOM   4825 H  HA   . ALA   B 1 60  ? 58.880 -12.182 1.341   1.00 17.08 ?  60  ALA   B HA   1 
ATOM   4826 H  HB1  . ALA   B 1 60  ? 58.187 -11.305 -0.712  1.00 18.30 ?  60  ALA   B HB1  1 
ATOM   4827 H  HB2  . ALA   B 1 60  ? 59.534 -12.128 -0.890  1.00 18.30 ?  60  ALA   B HB2  1 
ATOM   4828 H  HB3  . ALA   B 1 60  ? 58.147 -12.772 -1.322  1.00 18.30 ?  60  ALA   B HB3  1 
ATOM   4829 N  N    . MET   B 1 61  ? 56.241 -13.862 0.762   1.00 12.60 ?  61  MET   B N    1 
ATOM   4830 C  CA   . MET   B 1 61  ? 54.845 -13.984 1.158   1.00 12.28 ?  61  MET   B CA   1 
ATOM   4831 C  C    . MET   B 1 61  ? 54.706 -13.991 2.680   1.00 12.22 ?  61  MET   B C    1 
ATOM   4832 O  O    . MET   B 1 61  ? 53.809 -13.338 3.231   1.00 12.12 ?  61  MET   B O    1 
ATOM   4833 C  CB   . MET   B 1 61  ? 54.261 -15.247 0.519   1.00 12.07 ?  61  MET   B CB   1 
ATOM   4834 C  CG   . MET   B 1 61  ? 52.822 -15.537 0.927   1.00 11.84 ?  61  MET   B CG   1 
ATOM   4835 S  SD   . MET   B 1 61  ? 52.181 -17.046 0.182   1.00 12.51 ?  61  MET   B SD   1 
ATOM   4836 C  CE   . MET   B 1 61  ? 51.903 -16.471 -1.492  1.00 13.82 ?  61  MET   B CE   1 
ATOM   4837 H  H    . MET   B 1 61  ? 56.545 -14.531 0.300   1.00 15.13 ?  61  MET   B H    1 
ATOM   4838 H  HA   . MET   B 1 61  ? 54.356 -13.230 0.798   1.00 14.74 ?  61  MET   B HA   1 
ATOM   4839 H  HB2  . MET   B 1 61  ? 54.275 -15.148 -0.451  1.00 14.50 ?  61  MET   B HB2  1 
ATOM   4840 H  HB3  . MET   B 1 61  ? 54.800 -16.011 0.774   1.00 14.50 ?  61  MET   B HB3  1 
ATOM   4841 H  HG2  . MET   B 1 61  ? 52.781 -15.645 1.891   1.00 14.21 ?  61  MET   B HG2  1 
ATOM   4842 H  HG3  . MET   B 1 61  ? 52.259 -14.796 0.652   1.00 14.21 ?  61  MET   B HG3  1 
ATOM   4843 H  HE1  . MET   B 1 61  ? 51.523 -17.195 -2.014  1.00 16.59 ?  61  MET   B HE1  1 
ATOM   4844 H  HE2  . MET   B 1 61  ? 51.283 -15.721 -1.473  1.00 16.59 ?  61  MET   B HE2  1 
ATOM   4845 H  HE3  . MET   B 1 61  ? 52.746 -16.190 -1.877  1.00 16.59 ?  61  MET   B HE3  1 
ATOM   4846 N  N    . GLN   B 1 62  ? 55.585 -14.709 3.383   1.00 12.48 ?  62  GLN   B N    1 
ATOM   4847 C  CA   . GLN   B 1 62  ? 55.479 -14.760 4.838   1.00 12.78 ?  62  GLN   B CA   1 
ATOM   4848 C  C    . GLN   B 1 62  ? 55.760 -13.402 5.466   1.00 12.85 ?  62  GLN   B C    1 
ATOM   4849 O  O    . GLN   B 1 62  ? 55.075 -12.997 6.413   1.00 13.34 ?  62  GLN   B O    1 
ATOM   4850 C  CB   . GLN   B 1 62  ? 56.427 -15.813 5.410   1.00 13.09 ?  62  GLN   B CB   1 
ATOM   4851 C  CG   . GLN   B 1 62  ? 56.201 -16.075 6.890   1.00 13.27 ?  62  GLN   B CG   1 
ATOM   4852 C  CD   . GLN   B 1 62  ? 54.828 -16.668 7.132   1.00 13.00 ?  62  GLN   B CD   1 
ATOM   4853 O  OE1  . GLN   B 1 62  ? 54.570 -17.813 6.765   1.00 13.39 ?  62  GLN   B OE1  1 
ATOM   4854 N  NE2  . GLN   B 1 62  ? 53.918 -15.876 7.689   1.00 13.07 ?  62  GLN   B NE2  1 
ATOM   4855 H  H    . GLN   B 1 62  ? 56.234 -15.164 3.045   1.00 14.99 ?  62  GLN   B H    1 
ATOM   4856 H  HA   . GLN   B 1 62  ? 54.571 -15.013 5.071   1.00 15.34 ?  62  GLN   B HA   1 
ATOM   4857 H  HB2  . GLN   B 1 62  ? 56.294 -16.652 4.937   1.00 15.72 ?  62  GLN   B HB2  1 
ATOM   4858 H  HB3  . GLN   B 1 62  ? 57.341 -15.512 5.295   1.00 15.72 ?  62  GLN   B HB3  1 
ATOM   4859 H  HG2  . GLN   B 1 62  ? 56.866 -16.705 7.206   1.00 15.93 ?  62  GLN   B HG2  1 
ATOM   4860 H  HG3  . GLN   B 1 62  ? 56.266 -15.240 7.377   1.00 15.93 ?  62  GLN   B HG3  1 
ATOM   4861 H  HE21 . GLN   B 1 62  ? 54.128 -15.075 7.914   1.00 15.69 ?  62  GLN   B HE21 1 
ATOM   4862 H  HE22 . GLN   B 1 62  ? 53.126 -16.174 7.831   1.00 15.69 ?  62  GLN   B HE22 1 
ATOM   4863 N  N    . VAL   B 1 63  ? 56.778 -12.695 4.976   1.00 13.56 ?  63  VAL   B N    1 
ATOM   4864 C  CA   . VAL   B 1 63  ? 57.086 -11.377 5.527   1.00 14.71 ?  63  VAL   B CA   1 
ATOM   4865 C  C    . VAL   B 1 63  ? 55.895 -10.443 5.342   1.00 13.82 ?  63  VAL   B C    1 
ATOM   4866 O  O    . VAL   B 1 63  ? 55.478 -9.738  6.272   1.00 14.35 ?  63  VAL   B O    1 
ATOM   4867 C  CB   . VAL   B 1 63  ? 58.377 -10.824 4.898   1.00 15.92 ?  63  VAL   B CB   1 
ATOM   4868 C  CG1  . VAL   B 1 63  ? 58.617 -9.384  5.337   1.00 16.41 ?  63  VAL   B CG1  1 
ATOM   4869 C  CG2  . VAL   B 1 63  ? 59.557 -11.705 5.286   1.00 16.42 ?  63  VAL   B CG2  1 
ATOM   4870 H  H    . VAL   B 1 63  ? 57.291 -12.949 4.327   1.00 16.29 ?  63  VAL   B H    1 
ATOM   4871 H  HA   . VAL   B 1 63  ? 57.244 -11.474 6.475   1.00 17.66 ?  63  VAL   B HA   1 
ATOM   4872 H  HB   . VAL   B 1 63  ? 58.303 -10.843 3.931   1.00 19.12 ?  63  VAL   B HB   1 
ATOM   4873 H  HG11 . VAL   B 1 63  ? 59.534 -9.143  5.135   1.00 19.70 ?  63  VAL   B HG11 1 
ATOM   4874 H  HG12 . VAL   B 1 63  ? 58.007 -8.806  4.857   1.00 19.70 ?  63  VAL   B HG12 1 
ATOM   4875 H  HG13 . VAL   B 1 63  ? 58.461 -9.320  6.292   1.00 19.70 ?  63  VAL   B HG13 1 
ATOM   4876 H  HG21 . VAL   B 1 63  ? 60.372 -11.333 4.907   1.00 19.71 ?  63  VAL   B HG21 1 
ATOM   4877 H  HG22 . VAL   B 1 63  ? 59.631 -11.727 6.256   1.00 19.71 ?  63  VAL   B HG22 1 
ATOM   4878 H  HG23 . VAL   B 1 63  ? 59.417 -12.601 4.947   1.00 19.71 ?  63  VAL   B HG23 1 
ATOM   4879 N  N    . GLU   B 1 64  ? 55.327 -10.433 4.136   1.00 13.32 ?  64  GLU   B N    1 
ATOM   4880 C  CA   . GLU   B 1 64  ? 54.166 -9.592  3.860   1.00 13.22 ?  64  GLU   B CA   1 
ATOM   4881 C  C    . GLU   B 1 64  ? 52.983 -9.991  4.736   1.00 12.47 ?  64  GLU   B C    1 
ATOM   4882 O  O    . GLU   B 1 64  ? 52.238 -9.132  5.235   1.00 12.95 ?  64  GLU   B O    1 
ATOM   4883 C  CB   . GLU   B 1 64  ? 53.804 -9.751  2.383   1.00 13.22 ?  64  GLU   B CB   1 
ATOM   4884 C  CG   . GLU   B 1 64  ? 52.546 -9.008  1.943   1.00 13.17 ?  64  GLU   B CG   1 
ATOM   4885 C  CD   . GLU   B 1 64  ? 52.007 -9.512  0.617   1.00 13.88 ?  64  GLU   B CD   1 
ATOM   4886 O  OE1  . GLU   B 1 64  ? 52.184 -10.719 0.305   1.00 14.55 ?  64  GLU   B OE1  1 
ATOM   4887 O  OE2  . GLU   B 1 64  ? 51.386 -8.701  -0.105  1.00 14.47 -1 64  GLU   B OE2  1 
ATOM   4888 H  H    . GLU   B 1 64  ? 55.594 -10.904 3.464   1.00 15.99 ?  64  GLU   B H    1 
ATOM   4889 H  HA   . GLU   B 1 64  ? 54.382 -8.665  4.030   1.00 15.88 ?  64  GLU   B HA   1 
ATOM   4890 H  HB2  . GLU   B 1 64  ? 54.539 -9.411  1.845   1.00 15.88 ?  64  GLU   B HB2  1 
ATOM   4891 H  HB3  . GLU   B 1 64  ? 53.669 -10.689 2.194   1.00 15.88 ?  64  GLU   B HB3  1 
ATOM   4892 H  HG2  . GLU   B 1 64  ? 51.846 -9.125  2.607   1.00 15.81 ?  64  GLU   B HG2  1 
ATOM   4893 H  HG3  . GLU   B 1 64  ? 52.753 -8.063  1.852   1.00 15.81 ?  64  GLU   B HG3  1 
ATOM   4894 N  N    . SER   B 1 65  ? 52.795 -11.295 4.923   1.00 12.33 ?  65  SER   B N    1 
ATOM   4895 C  CA   . SER   B 1 65  ? 51.684 -11.796 5.720   1.00 12.29 ?  65  SER   B CA   1 
ATOM   4896 C  C    . SER   B 1 65  ? 51.816 -11.400 7.183   1.00 12.40 ?  65  SER   B C    1 
ATOM   4897 O  O    . SER   B 1 65  ? 50.821 -11.029 7.819   1.00 12.82 ?  65  SER   B O    1 
ATOM   4898 C  CB   . SER   B 1 65  ? 51.606 -13.314 5.594   1.00 12.31 ?  65  SER   B CB   1 
ATOM   4899 O  OG   . SER   B 1 65  ? 51.249 -13.719 4.283   1.00 12.62 ?  65  SER   B OG   1 
ATOM   4900 H  H    . SER   B 1 65  ? 53.301 -11.918 4.600   1.00 14.81 ?  65  SER   B H    1 
ATOM   4901 H  HA   . SER   B 1 65  ? 50.854 -11.424 5.380   1.00 14.76 ?  65  SER   B HA   1 
ATOM   4902 H  HB2  . SER   B 1 65  ? 52.464 -13.695 5.809   1.00 14.78 ?  65  SER   B HB2  1 
ATOM   4903 H  HB3  . SER   B 1 65  ? 50.930 -13.644 6.214   1.00 14.78 ?  65  SER   B HB3  1 
ATOM   4904 H  HG   . SER   B 1 65  ? 51.810 -13.434 3.724   1.00 15.15 ?  65  SER   B HG   1 
ATOM   4905 N  N    . ASP   B 1 66  ? 53.023 -11.502 7.748   1.00 12.96 ?  66  ASP   B N    1 
ATOM   4906 C  CA   . ASP   B 1 66  ? 53.208 -11.109 9.142   1.00 13.33 ?  66  ASP   B CA   1 
ATOM   4907 C  C    . ASP   B 1 66  ? 52.897 -9.630  9.339   1.00 13.49 ?  66  ASP   B C    1 
ATOM   4908 O  O    . ASP   B 1 66  ? 52.324 -9.236  10.362  1.00 13.94 ?  66  ASP   B O    1 
ATOM   4909 C  CB   . ASP   B 1 66  ? 54.635 -11.421 9.596   1.00 14.62 ?  66  ASP   B CB   1 
ATOM   4910 C  CG   . ASP   B 1 66  ? 54.897 -12.915 9.753   1.00 16.44 ?  66  ASP   B CG   1 
ATOM   4911 O  OD1  . ASP   B 1 66  ? 53.942 -13.721 9.691   1.00 16.70 ?  66  ASP   B OD1  1 
ATOM   4912 O  OD2  . ASP   B 1 66  ? 56.076 -13.287 9.954   1.00 19.02 -1 66  ASP   B OD2  1 
ATOM   4913 H  H    . ASP   B 1 66  ? 53.729 -11.796 7.358   1.00 15.56 ?  66  ASP   B H    1 
ATOM   4914 H  HA   . ASP   B 1 66  ? 52.602 -11.615 9.703   1.00 16.00 ?  66  ASP   B HA   1 
ATOM   4915 H  HB2  . ASP   B 1 66  ? 55.263 -11.082 8.940   1.00 17.55 ?  66  ASP   B HB2  1 
ATOM   4916 H  HB3  . ASP   B 1 66  ? 54.798 -10.994 10.457  1.00 17.55 ?  66  ASP   B HB3  1 
ATOM   4917 N  N    . ASP   B 1 67  ? 53.274 -8.791  8.374   1.00 12.92 ?  67  ASP   B N    1 
ATOM   4918 C  CA   . ASP   B 1 67  ? 52.928 -7.379  8.453   1.00 13.53 ?  67  ASP   B CA   1 
ATOM   4919 C  C    . ASP   B 1 67  ? 51.418 -7.171  8.369   1.00 13.75 ?  67  ASP   B C    1 
ATOM   4920 O  O    . ASP   B 1 67  ? 50.855 -6.365  9.117   1.00 14.28 ?  67  ASP   B O    1 
ATOM   4921 C  CB   . ASP   B 1 67  ? 53.645 -6.615  7.348   1.00 14.73 ?  67  ASP   B CB   1 
ATOM   4922 C  CG   . ASP   B 1 67  ? 53.226 -5.173  7.300   1.00 16.33 ?  67  ASP   B CG   1 
ATOM   4923 O  OD1  . ASP   B 1 67  ? 53.719 -4.356  8.112   1.00 17.45 ?  67  ASP   B OD1  1 
ATOM   4924 O  OD2  . ASP   B 1 67  ? 52.365 -4.873  6.460   1.00 17.31 -1 67  ASP   B OD2  1 
ATOM   4925 H  H    . ASP   B 1 67  ? 53.729 -9.015  7.678   1.00 15.51 ?  67  ASP   B H    1 
ATOM   4926 H  HA   . ASP   B 1 67  ? 53.230 -7.026  9.301   1.00 16.25 ?  67  ASP   B HA   1 
ATOM   4927 H  HB2  . ASP   B 1 67  ? 54.601 -6.643  7.504   1.00 17.69 ?  67  ASP   B HB2  1 
ATOM   4928 H  HB3  . ASP   B 1 67  ? 53.440 -7.026  6.487   1.00 17.69 ?  67  ASP   B HB3  1 
ATOM   4929 N  N    . TYR   B 1 68  ? 50.740 -7.903  7.478   1.00 13.26 ?  68  TYR   B N    1 
ATOM   4930 C  CA   . TYR   B 1 68  ? 49.284 -7.822  7.407   1.00 14.11 ?  68  TYR   B CA   1 
ATOM   4931 C  C    . TYR   B 1 68  ? 48.650 -8.162  8.752   1.00 13.73 ?  68  TYR   B C    1 
ATOM   4932 O  O    . TYR   B 1 68  ? 47.722 -7.478  9.203   1.00 14.55 ?  68  TYR   B O    1 
ATOM   4933 C  CB   . TYR   B 1 68  ? 48.751 -8.758  6.313   1.00 14.83 ?  68  TYR   B CB   1 
ATOM   4934 C  CG   . TYR   B 1 68  ? 47.246 -8.908  6.369   1.00 15.93 ?  68  TYR   B CG   1 
ATOM   4935 C  CD1  . TYR   B 1 68  ? 46.658 -9.859  7.196   1.00 17.04 ?  68  TYR   B CD1  1 
ATOM   4936 C  CD2  . TYR   B 1 68  ? 46.415 -8.075  5.635   1.00 17.13 ?  68  TYR   B CD2  1 
ATOM   4937 C  CE1  . TYR   B 1 68  ? 45.292 -9.980  7.286   1.00 18.14 ?  68  TYR   B CE1  1 
ATOM   4938 C  CE2  . TYR   B 1 68  ? 45.033 -8.199  5.713   1.00 17.58 ?  68  TYR   B CE2  1 
ATOM   4939 C  CZ   . TYR   B 1 68  ? 44.490 -9.151  6.543   1.00 18.15 ?  68  TYR   B CZ   1 
ATOM   4940 O  OH   . TYR   B 1 68  ? 43.122 -9.269  6.638   1.00 19.11 ?  68  TYR   B OH   1 
ATOM   4941 H  H    . TYR   B 1 68  ? 51.096 -8.458  6.917   1.00 15.92 ?  68  TYR   B H    1 
ATOM   4942 H  HA   . TYR   B 1 68  ? 49.033 -6.918  7.175   1.00 16.94 ?  68  TYR   B HA   1 
ATOM   4943 H  HB2  . TYR   B 1 68  ? 48.980 -8.398  5.445   1.00 17.81 ?  68  TYR   B HB2  1 
ATOM   4944 H  HB3  . TYR   B 1 68  ? 49.142 -9.639  6.425   1.00 17.81 ?  68  TYR   B HB3  1 
ATOM   4945 H  HD1  . TYR   B 1 68  ? 47.194 -10.427 7.701   1.00 20.46 ?  68  TYR   B HD1  1 
ATOM   4946 H  HD2  . TYR   B 1 68  ? 46.786 -7.424  5.090   1.00 20.57 ?  68  TYR   B HD2  1 
ATOM   4947 H  HE1  . TYR   B 1 68  ? 44.906 -10.634 7.832   1.00 21.77 ?  68  TYR   B HE1  1 
ATOM   4948 H  HE2  . TYR   B 1 68  ? 44.476 -7.634  5.222   1.00 21.11 ?  68  TYR   B HE2  1 
ATOM   4949 H  HH   . TYR   B 1 68  ? 42.733 -8.718  6.128   1.00 22.94 ?  68  TYR   B HH   1 
ATOM   4950 N  N    . ILE   B 1 69  ? 49.126 -9.231  9.399   1.00 13.40 ?  69  ILE   B N    1 
ATOM   4951 C  CA   . ILE   B 1 69  ? 48.567 -9.652  10.682  1.00 14.13 ?  69  ILE   B CA   1 
ATOM   4952 C  C    . ILE   B 1 69  ? 48.824 -8.603  11.758  1.00 13.97 ?  69  ILE   B C    1 
ATOM   4953 O  O    . ILE   B 1 69  ? 47.955 -8.320  12.590  1.00 14.09 ?  69  ILE   B O    1 
ATOM   4954 C  CB   . ILE   B 1 69  ? 49.142 -11.026 11.078  1.00 14.81 ?  69  ILE   B CB   1 
ATOM   4955 C  CG1  . ILE   B 1 69  ? 48.612 -12.131 10.156  1.00 15.12 ?  69  ILE   B CG1  1 
ATOM   4956 C  CG2  . ILE   B 1 69  ? 48.858 -11.335 12.545  1.00 15.72 ?  69  ILE   B CG2  1 
ATOM   4957 C  CD1  . ILE   B 1 69  ? 47.132 -12.432 10.300  1.00 15.56 ?  69  ILE   B CD1  1 
ATOM   4958 H  H    . ILE   B 1 69  ? 49.770 -9.722  9.118   1.00 16.09 ?  69  ILE   B H    1 
ATOM   4959 H  HA   . ILE   B 1 69  ? 47.608 -9.746  10.588  1.00 16.96 ?  69  ILE   B HA   1 
ATOM   4960 H  HB   . ILE   B 1 69  ? 50.105 -10.986 10.968  1.00 17.78 ?  69  ILE   B HB   1 
ATOM   4961 H  HG12 . ILE   B 1 69  ? 48.769 -11.865 9.235   1.00 18.15 ?  69  ILE   B HG12 1 
ATOM   4962 H  HG13 . ILE   B 1 69  ? 49.098 -12.949 10.344  1.00 18.15 ?  69  ILE   B HG13 1 
ATOM   4963 H  HG21 . ILE   B 1 69  ? 48.998 -12.283 12.697  1.00 18.87 ?  69  ILE   B HG21 1 
ATOM   4964 H  HG22 . ILE   B 1 69  ? 49.464 -10.823 13.104  1.00 18.87 ?  69  ILE   B HG22 1 
ATOM   4965 H  HG23 . ILE   B 1 69  ? 47.939 -11.102 12.747  1.00 18.87 ?  69  ILE   B HG23 1 
ATOM   4966 H  HD11 . ILE   B 1 69  ? 46.904 -13.163 9.705   1.00 18.68 ?  69  ILE   B HD11 1 
ATOM   4967 H  HD12 . ILE   B 1 69  ? 46.946 -12.682 11.217  1.00 18.68 ?  69  ILE   B HD12 1 
ATOM   4968 H  HD13 . ILE   B 1 69  ? 46.622 -11.642 10.060  1.00 18.68 ?  69  ILE   B HD13 1 
ATOM   4969 N  N    . ALA   B 1 70  ? 50.020 -8.018  11.779  1.00 13.86 ?  70  ALA   B N    1 
ATOM   4970 C  CA   . ALA   B 1 70  ? 50.304 -6.979  12.763  1.00 13.55 ?  70  ALA   B CA   1 
ATOM   4971 C  C    . ALA   B 1 70  ? 49.304 -5.840  12.650  1.00 14.09 ?  70  ALA   B C    1 
ATOM   4972 O  O    . ALA   B 1 70  ? 48.864 -5.288  13.663  1.00 14.43 ?  70  ALA   B O    1 
ATOM   4973 C  CB   . ALA   B 1 70  ? 51.731 -6.468  12.584  1.00 14.16 ?  70  ALA   B CB   1 
ATOM   4974 H  H    . ALA   B 1 70  ? 50.663 -8.205  11.250  1.00 16.64 ?  70  ALA   B H    1 
ATOM   4975 H  HA   . ALA   B 1 70  ? 50.231 -7.356  13.655  1.00 16.26 ?  70  ALA   B HA   1 
ATOM   4976 H  HB1  . ALA   B 1 70  ? 51.920 -5.810  13.270  1.00 17.00 ?  70  ALA   B HB1  1 
ATOM   4977 H  HB2  . ALA   B 1 70  ? 52.347 -7.215  12.666  1.00 17.00 ?  70  ALA   B HB2  1 
ATOM   4978 H  HB3  . ALA   B 1 70  ? 51.817 -6.068  11.705  1.00 17.00 ?  70  ALA   B HB3  1 
ATOM   4979 N  N    . THR   B 1 71  ? 48.930 -5.476  11.425  1.00 14.55 ?  71  THR   B N    1 
ATOM   4980 C  CA   . THR   B 1 71  ? 48.038 -4.343  11.211  1.00 15.54 ?  71  THR   B CA   1 
ATOM   4981 C  C    . THR   B 1 71  ? 46.571 -4.710  11.415  1.00 16.21 ?  71  THR   B C    1 
ATOM   4982 O  O    . THR   B 1 71  ? 45.789 -3.893  11.924  1.00 17.62 ?  71  THR   B O    1 
ATOM   4983 C  CB   . THR   B 1 71  ? 48.260 -3.778  9.805   1.00 17.68 ?  71  THR   B CB   1 
ATOM   4984 O  OG1  . THR   B 1 71  ? 49.584 -3.240  9.716   1.00 19.68 ?  71  THR   B OG1  1 
ATOM   4985 C  CG2  . THR   B 1 71  ? 47.245 -2.689  9.474   1.00 18.73 ?  71  THR   B CG2  1 
ATOM   4986 H  H    . THR   B 1 71  ? 49.187 -5.868  10.704  1.00 17.47 ?  71  THR   B H    1 
ATOM   4987 H  HA   . THR   B 1 71  ? 48.256 -3.646  11.846  1.00 18.66 ?  71  THR   B HA   1 
ATOM   4988 H  HB   . THR   B 1 71  ? 48.173 -4.486  9.150   1.00 21.23 ?  71  THR   B HB   1 
ATOM   4989 H  HG1  . THR   B 1 71  ? 49.713 -2.903  8.952   1.00 23.63 ?  71  THR   B HG1  1 
ATOM   4990 H  HG21 . THR   B 1 71  ? 47.545 -2.178  8.703   1.00 22.49 ?  71  THR   B HG21 1 
ATOM   4991 H  HG22 . THR   B 1 71  ? 46.385 -3.085  9.267   1.00 22.49 ?  71  THR   B HG22 1 
ATOM   4992 H  HG23 . THR   B 1 71  ? 47.145 -2.086  10.227  1.00 22.49 ?  71  THR   B HG23 1 
ATOM   4993 N  N    . ASN   B 1 72  ? 46.178 -5.928  11.031  1.00 15.90 ?  72  ASN   B N    1 
ATOM   4994 C  CA   . ASN   B 1 72  ? 44.773 -6.286  10.907  1.00 16.40 ?  72  ASN   B CA   1 
ATOM   4995 C  C    . ASN   B 1 72  ? 44.302 -7.378  11.855  1.00 16.90 ?  72  ASN   B C    1 
ATOM   4996 O  O    . ASN   B 1 72  ? 43.087 -7.538  12.022  1.00 17.98 ?  72  ASN   B O    1 
ATOM   4997 C  CB   . ASN   B 1 72  ? 44.463 -6.720  9.466   1.00 16.90 ?  72  ASN   B CB   1 
ATOM   4998 C  CG   . ASN   B 1 72  ? 44.736 -5.622  8.465   1.00 18.03 ?  72  ASN   B CG   1 
ATOM   4999 O  OD1  . ASN   B 1 72  ? 45.753 -5.629  7.765   1.00 18.87 ?  72  ASN   B OD1  1 
ATOM   5000 N  ND2  . ASN   B 1 72  ? 43.848 -4.648  8.416   1.00 19.64 ?  72  ASN   B ND2  1 
ATOM   5001 H  H    . ASN   B 1 72  ? 46.717 -6.578  10.834  1.00 19.09 ?  72  ASN   B H    1 
ATOM   5002 H  HA   . ASN   B 1 72  ? 44.243 -5.500  11.089  1.00 19.69 ?  72  ASN   B HA   1 
ATOM   5003 H  HB2  . ASN   B 1 72  ? 45.019 -7.483  9.236   1.00 20.29 ?  72  ASN   B HB2  1 
ATOM   5004 H  HB3  . ASN   B 1 72  ? 43.526 -6.961  9.402   1.00 20.29 ?  72  ASN   B HB3  1 
ATOM   5005 H  HD21 . ASN   B 1 72  ? 43.950 -3.995  7.863   1.00 23.57 ?  72  ASN   B HD21 1 
ATOM   5006 H  HD22 . ASN   B 1 72  ? 43.149 -4.672  8.921   1.00 23.57 ?  72  ASN   B HD22 1 
ATOM   5007 N  N    . GLY   B 1 73  ? 45.206 -8.122  12.483  1.00 16.33 ?  73  GLY   B N    1 
ATOM   5008 C  CA   . GLY   B 1 73  ? 44.814 -9.264  13.273  1.00 15.90 ?  73  GLY   B CA   1 
ATOM   5009 C  C    . GLY   B 1 73  ? 44.453 -10.450 12.404  1.00 14.66 ?  73  GLY   B C    1 
ATOM   5010 O  O    . GLY   B 1 73  ? 44.444 -10.371 11.173  1.00 14.35 ?  73  GLY   B O    1 
ATOM   5011 H  H    . GLY   B 1 73  ? 46.055 -7.985  12.464  1.00 19.61 ?  73  GLY   B H    1 
ATOM   5012 H  HA2  . GLY   B 1 73  ? 45.544 -9.519  13.863  1.00 19.09 ?  73  GLY   B HA2  1 
ATOM   5013 H  HA3  . GLY   B 1 73  ? 44.045 -9.035  13.820  1.00 19.09 ?  73  GLY   B HA3  1 
ATOM   5014 N  N    . PRO   B 1 74  ? 44.146 -11.575 13.042  1.00 14.68 ?  74  PRO   B N    1 
ATOM   5015 C  CA   . PRO   B 1 74  ? 43.892 -12.807 12.295  1.00 14.09 ?  74  PRO   B CA   1 
ATOM   5016 C  C    . PRO   B 1 74  ? 42.591 -12.748 11.509  1.00 13.34 ?  74  PRO   B C    1 
ATOM   5017 O  O    . PRO   B 1 74  ? 41.653 -12.011 11.831  1.00 14.73 ?  74  PRO   B O    1 
ATOM   5018 C  CB   . PRO   B 1 74  ? 43.822 -13.871 13.395  1.00 15.29 ?  74  PRO   B CB   1 
ATOM   5019 C  CG   . PRO   B 1 74  ? 43.375 -13.122 14.608  1.00 16.74 ?  74  PRO   B CG   1 
ATOM   5020 C  CD   . PRO   B 1 74  ? 44.029 -11.776 14.497  1.00 16.21 ?  74  PRO   B CD   1 
ATOM   5021 H  HA   . PRO   B 1 74  ? 44.636 -12.998 11.696  1.00 16.92 ?  74  PRO   B HA   1 
ATOM   5022 H  HB2  . PRO   B 1 74  ? 43.177 -14.551 13.146  1.00 18.35 ?  74  PRO   B HB2  1 
ATOM   5023 H  HB3  . PRO   B 1 74  ? 44.700 -14.261 13.531  1.00 18.35 ?  74  PRO   B HB3  1 
ATOM   5024 H  HG2  . PRO   B 1 74  ? 42.408 -13.038 14.598  1.00 20.09 ?  74  PRO   B HG2  1 
ATOM   5025 H  HG3  . PRO   B 1 74  ? 43.672 -13.587 15.403  1.00 20.09 ?  74  PRO   B HG3  1 
ATOM   5026 H  HD2  . PRO   B 1 74  ? 43.462 -11.092 14.895  1.00 19.46 ?  74  PRO   B HD2  1 
ATOM   5027 H  HD3  . PRO   B 1 74  ? 44.907 -11.790 14.908  1.00 19.46 ?  74  PRO   B HD3  1 
ATOM   5028 N  N    . LEU   B 1 75  ? 42.556 -13.557 10.455  1.00 12.77 ?  75  LEU   B N    1 
ATOM   5029 C  CA   . LEU   B 1 75  ? 41.347 -13.771 9.682   1.00 13.08 ?  75  LEU   B CA   1 
ATOM   5030 C  C    . LEU   B 1 75  ? 40.368 -14.625 10.481  1.00 13.67 ?  75  LEU   B C    1 
ATOM   5031 O  O    . LEU   B 1 75  ? 40.707 -15.198 11.516  1.00 14.60 ?  75  LEU   B O    1 
ATOM   5032 C  CB   . LEU   B 1 75  ? 41.677 -14.487 8.371   1.00 13.13 ?  75  LEU   B CB   1 
ATOM   5033 C  CG   . LEU   B 1 75  ? 42.522 -13.737 7.336   1.00 15.03 ?  75  LEU   B CG   1 
ATOM   5034 C  CD1  . LEU   B 1 75  ? 42.736 -14.568 6.075   1.00 16.27 ?  75  LEU   B CD1  1 
ATOM   5035 C  CD2  . LEU   B 1 75  ? 41.905 -12.406 6.991   1.00 18.16 ?  75  LEU   B CD2  1 
ATOM   5036 H  H    . LEU   B 1 75  ? 43.233 -14.005 10.163  1.00 15.33 ?  75  LEU   B H    1 
ATOM   5037 H  HA   . LEU   B 1 75  ? 40.929 -12.922 9.480   1.00 15.71 ?  75  LEU   B HA   1 
ATOM   5038 H  HB2  . LEU   B 1 75  ? 42.157 -15.305 8.588   1.00 15.77 ?  75  LEU   B HB2  1 
ATOM   5039 H  HB3  . LEU   B 1 75  ? 40.842 -14.721 7.936   1.00 15.77 ?  75  LEU   B HB3  1 
ATOM   5040 H  HG   . LEU   B 1 75  ? 43.397 -13.566 7.719   1.00 18.04 ?  75  LEU   B HG   1 
ATOM   5041 H  HD11 . LEU   B 1 75  ? 43.282 -14.057 5.449   1.00 19.54 ?  75  LEU   B HD11 1 
ATOM   5042 H  HD12 . LEU   B 1 75  ? 43.194 -15.391 6.306   1.00 19.54 ?  75  LEU   B HD12 1 
ATOM   5043 H  HD13 . LEU   B 1 75  ? 41.878 -14.765 5.672   1.00 19.54 ?  75  LEU   B HD13 1 
ATOM   5044 H  HD21 . LEU   B 1 75  ? 42.396 -12.011 6.255   1.00 21.80 ?  75  LEU   B HD21 1 
ATOM   5045 H  HD22 . LEU   B 1 75  ? 40.980 -12.545 6.737   1.00 21.80 ?  75  LEU   B HD22 1 
ATOM   5046 H  HD23 . LEU   B 1 75  ? 41.951 -11.827 7.769   1.00 21.80 ?  75  LEU   B HD23 1 
ATOM   5047 N  N    . LYS   B 1 76  ? 39.136 -14.698 9.982   1.00 14.59 ?  76  LYS   B N    1 
ATOM   5048 C  CA   . LYS   B 1 76  ? 38.150 -15.653 10.464  1.00 15.85 ?  76  LYS   B CA   1 
ATOM   5049 C  C    . LYS   B 1 76  ? 38.246 -16.930 9.635   1.00 14.77 ?  76  LYS   B C    1 
ATOM   5050 O  O    . LYS   B 1 76  ? 38.526 -16.883 8.439   1.00 14.19 ?  76  LYS   B O    1 
ATOM   5051 C  CB   . LYS   B 1 76  ? 36.733 -15.089 10.280  1.00 17.81 ?  76  LYS   B CB   1 
ATOM   5052 C  CG   . LYS   B 1 76  ? 36.446 -13.717 10.906  1.00 19.70 ?  76  LYS   B CG   1 
ATOM   5053 C  CD   . LYS   B 1 76  ? 35.053 -13.191 10.517  1.00 20.69 ?  76  LYS   B CD   1 
ATOM   5054 C  CE   . LYS   B 1 76  ? 34.761 -11.833 11.145  1.00 22.42 ?  76  LYS   B CE   1 
ATOM   5055 N  NZ   . LYS   B 1 76  ? 33.483 -11.224 10.675  1.00 22.97 ?  76  LYS   B NZ   1 
ATOM   5056 H  H    . LYS   B 1 76  ? 38.848 -14.204 9.341   1.00 17.52 ?  76  LYS   B H    1 
ATOM   5057 H  HA   . LYS   B 1 76  ? 38.303 -15.866 11.398  1.00 19.02 ?  76  LYS   B HA   1 
ATOM   5058 H  HB2  . LYS   B 1 76  ? 36.561 -15.012 9.329   1.00 21.38 ?  76  LYS   B HB2  1 
ATOM   5059 H  HB3  . LYS   B 1 76  ? 36.105 -15.717 10.669  1.00 21.38 ?  76  LYS   B HB3  1 
ATOM   5060 H  HG2  . LYS   B 1 76  ? 36.487 -13.793 11.872  1.00 23.65 ?  76  LYS   B HG2  1 
ATOM   5061 H  HG3  . LYS   B 1 76  ? 37.112 -13.080 10.594  1.00 23.65 ?  76  LYS   B HG3  1 
ATOM   5062 H  HD2  . LYS   B 1 76  ? 35.007 -13.095 9.552   1.00 24.84 ?  76  LYS   B HD2  1 
ATOM   5063 H  HD3  . LYS   B 1 76  ? 34.380 -13.818 10.823  1.00 24.84 ?  76  LYS   B HD3  1 
ATOM   5064 H  HE2  . LYS   B 1 76  ? 34.706 -11.938 12.106  1.00 26.91 ?  76  LYS   B HE2  1 
ATOM   5065 H  HE3  . LYS   B 1 76  ? 35.481 -11.223 10.919  1.00 26.91 ?  76  LYS   B HE3  1 
ATOM   5066 H  HZ1  . LYS   B 1 76  ? 33.358 -10.433 11.070  1.00 27.58 ?  76  LYS   B HZ1  1 
ATOM   5067 H  HZ2  . LYS   B 1 76  ? 33.504 -11.102 9.793   1.00 27.58 ?  76  LYS   B HZ2  1 
ATOM   5068 H  HZ3  . LYS   B 1 76  ? 32.797 -11.755 10.876  1.00 27.58 ?  76  LYS   B HZ3  1 
ATOM   5069 N  N    . VAL   B 1 77  ? 38.004 -18.079 10.272  1.00 15.55 ?  77  VAL   B N    1 
ATOM   5070 C  CA   . VAL   B 1 77  ? 37.802 -19.299 9.498   1.00 15.69 ?  77  VAL   B CA   1 
ATOM   5071 C  C    . VAL   B 1 77  ? 36.611 -19.074 8.579   1.00 14.51 ?  77  VAL   B C    1 
ATOM   5072 O  O    . VAL   B 1 77  ? 35.549 -18.622 9.022   1.00 14.55 ?  77  VAL   B O    1 
ATOM   5073 C  CB   . VAL   B 1 77  ? 37.591 -20.508 10.422  1.00 17.25 ?  77  VAL   B CB   1 
ATOM   5074 C  CG1  . VAL   B 1 77  ? 37.292 -21.747 9.591   1.00 17.73 ?  77  VAL   B CG1  1 
ATOM   5075 C  CG2  . VAL   B 1 77  ? 38.816 -20.728 11.306  1.00 18.60 ?  77  VAL   B CG2  1 
ATOM   5076 H  H    . VAL   B 1 77  ? 37.950 -18.176 11.120  1.00 18.67 ?  77  VAL   B H    1 
ATOM   5077 H  HA   . VAL   B 1 77  ? 38.576 -19.466 8.945   1.00 18.84 ?  77  VAL   B HA   1 
ATOM   5078 H  HB   . VAL   B 1 77  ? 36.823 -20.338 10.994  1.00 20.71 ?  77  VAL   B HB   1 
ATOM   5079 H  HG11 . VAL   B 1 77  ? 37.335 -22.527 10.166  1.00 21.29 ?  77  VAL   B HG11 1 
ATOM   5080 H  HG12 . VAL   B 1 77  ? 36.398 -21.672 9.211   1.00 21.29 ?  77  VAL   B HG12 1 
ATOM   5081 H  HG13 . VAL   B 1 77  ? 37.946 -21.819 8.883   1.00 21.29 ?  77  VAL   B HG13 1 
ATOM   5082 H  HG21 . VAL   B 1 77  ? 38.671 -21.519 11.845  1.00 22.33 ?  77  VAL   B HG21 1 
ATOM   5083 H  HG22 . VAL   B 1 77  ? 39.591 -20.843 10.739  1.00 22.33 ?  77  VAL   B HG22 1 
ATOM   5084 H  HG23 . VAL   B 1 77  ? 38.930 -19.952 11.876  1.00 22.33 ?  77  VAL   B HG23 1 
ATOM   5085 N  N    . GLY   B 1 78  ? 36.789 -19.360 7.290   1.00 13.83 ?  78  GLY   B N    1 
ATOM   5086 C  CA   . GLY   B 1 78  ? 35.810 -19.037 6.278   1.00 13.74 ?  78  GLY   B CA   1 
ATOM   5087 C  C    . GLY   B 1 78  ? 36.046 -17.720 5.576   1.00 13.15 ?  78  GLY   B C    1 
ATOM   5088 O  O    . GLY   B 1 78  ? 35.362 -17.438 4.584   1.00 13.44 ?  78  GLY   B O    1 
ATOM   5089 H  H    . GLY   B 1 78  ? 37.484 -19.758 6.977   1.00 16.60 ?  78  GLY   B H    1 
ATOM   5090 H  HA2  . GLY   B 1 78  ? 35.804 -19.734 5.607   1.00 16.49 ?  78  GLY   B HA2  1 
ATOM   5091 H  HA3  . GLY   B 1 78  ? 34.931 -19.000 6.685   1.00 16.49 ?  78  GLY   B HA3  1 
ATOM   5092 N  N    . GLY   B 1 79  ? 36.999 -16.915 6.054   1.00 12.93 ?  79  GLY   B N    1 
ATOM   5093 C  CA   . GLY   B 1 79  ? 37.298 -15.625 5.472   1.00 12.58 ?  79  GLY   B CA   1 
ATOM   5094 C  C    . GLY   B 1 79  ? 38.538 -15.648 4.589   1.00 12.10 ?  79  GLY   B C    1 
ATOM   5095 O  O    . GLY   B 1 79  ? 39.158 -16.681 4.348   1.00 12.49 ?  79  GLY   B O    1 
ATOM   5096 H  H    . GLY   B 1 79  ? 37.501 -17.103 6.728   1.00 15.53 ?  79  GLY   B H    1 
ATOM   5097 H  HA2  . GLY   B 1 79  ? 36.545 -15.327 4.934   1.00 15.11 ?  79  GLY   B HA2  1 
ATOM   5098 H  HA3  . GLY   B 1 79  ? 37.443 -14.974 6.177   1.00 15.11 ?  79  GLY   B HA3  1 
ATOM   5099 N  N    . SER   B 1 80  ? 38.905 -14.457 4.111   1.00 12.13 ?  80  SER   B N    1 
ATOM   5100 C  CA   . SER   B 1 80  ? 40.017 -14.325 3.179   1.00 11.98 ?  80  SER   B CA   1 
ATOM   5101 C  C    . SER   B 1 80  ? 40.600 -12.920 3.232   1.00 11.67 ?  80  SER   B C    1 
ATOM   5102 O  O    . SER   B 1 80  ? 39.981 -11.981 3.739   1.00 12.62 ?  80  SER   B O    1 
ATOM   5103 C  CB   . SER   B 1 80  ? 39.580 -14.619 1.740   1.00 12.04 ?  80  SER   B CB   1 
ATOM   5104 O  OG   . SER   B 1 80  ? 38.731 -13.600 1.234   1.00 13.15 ?  80  SER   B OG   1 
ATOM   5105 H  H    . SER   B 1 80  ? 38.529 -13.712 4.309   1.00 14.56 ?  80  SER   B H    1 
ATOM   5106 H  HA   . SER   B 1 80  ? 40.707 -14.958 3.424   1.00 14.39 ?  80  SER   B HA   1 
ATOM   5107 H  HB2  . SER   B 1 80  ? 40.364 -14.675 1.171   1.00 14.46 ?  80  SER   B HB2  1 
ATOM   5108 H  HB3  . SER   B 1 80  ? 39.099 -15.464 1.718   1.00 14.46 ?  80  SER   B HB3  1 
ATOM   5109 H  HG   . SER   B 1 80  ? 38.037 -13.541 1.715   1.00 15.79 ?  80  SER   B HG   1 
ATOM   5110 N  N    . CYS   B 1 81  ? 41.786 -12.783 2.642   1.00 11.51 ?  81  CYS   B N    1 
ATOM   5111 C  CA   . CYS   B 1 81  ? 42.336 -11.476 2.321   1.00 11.58 ?  81  CYS   B CA   1 
ATOM   5112 C  C    . CYS   B 1 81  ? 43.103 -11.564 1.010   1.00 10.99 ?  81  CYS   B C    1 
ATOM   5113 O  O    . CYS   B 1 81  ? 43.611 -12.627 0.636   1.00 11.86 ?  81  CYS   B O    1 
ATOM   5114 C  CB   . CYS   B 1 81  ? 43.231 -10.919 3.436   1.00 12.33 ?  81  CYS   B CB   1 
ATOM   5115 S  SG   . CYS   B 1 81  ? 44.741 -11.862 3.694   1.00 12.66 ?  81  CYS   B SG   1 
ATOM   5116 H  H    . CYS   B 1 81  ? 42.295 -13.441 2.412   1.00 13.82 ?  81  CYS   B H    1 
ATOM   5117 H  HA   . CYS   B 1 81  ? 41.603 -10.852 2.190   1.00 13.91 ?  81  CYS   B HA   1 
ATOM   5118 H  HB2  . CYS   B 1 81  ? 43.484 -10.008 3.212   1.00 14.81 ?  81  CYS   B HB2  1 
ATOM   5119 H  HB3  . CYS   B 1 81  ? 42.727 -10.919 4.269   1.00 14.81 ?  81  CYS   B HB3  1 
ATOM   5120 H  HG   . CYS   B 1 81  ? 45.366 -11.358 4.588   1.00 15.21 ?  81  CYS   B HG   1 
ATOM   5121 N  N    . VAL   B 1 82  ? 43.208 -10.422 0.335   1.00 11.56 ?  82  VAL   B N    1 
ATOM   5122 C  CA   . VAL   B 1 82  ? 43.971 -10.298 -0.903  1.00 11.48 ?  82  VAL   B CA   1 
ATOM   5123 C  C    . VAL   B 1 82  ? 45.312 -9.658  -0.584  1.00 11.68 ?  82  VAL   B C    1 
ATOM   5124 O  O    . VAL   B 1 82  ? 45.367 -8.541  -0.056  1.00 12.88 ?  82  VAL   B O    1 
ATOM   5125 C  CB   . VAL   B 1 82  ? 43.224 -9.458  -1.950  1.00 12.65 ?  82  VAL   B CB   1 
ATOM   5126 C  CG1  . VAL   B 1 82  ? 44.063 -9.334  -3.217  1.00 14.13 ?  82  VAL   B CG1  1 
ATOM   5127 C  CG2  . VAL   B 1 82  ? 41.856 -10.049 -2.250  1.00 13.56 ?  82  VAL   B CG2  1 
ATOM   5128 H  H    . VAL   B 1 82  ? 42.835 -9.680  0.577   1.00 13.88 ?  82  VAL   B H    1 
ATOM   5129 H  HA   . VAL   B 1 82  ? 44.131 -11.179 -1.275  1.00 13.79 ?  82  VAL   B HA   1 
ATOM   5130 H  HB   . VAL   B 1 82  ? 43.091 -8.567  -1.601  1.00 15.19 ?  82  VAL   B HB   1 
ATOM   5131 H  HG11 . VAL   B 1 82  ? 43.505 -9.011  -3.941  1.00 16.97 ?  82  VAL   B HG11 1 
ATOM   5132 H  HG12 . VAL   B 1 82  ? 44.790 -8.705  -3.061  1.00 16.97 ?  82  VAL   B HG12 1 
ATOM   5133 H  HG13 . VAL   B 1 82  ? 44.428 -10.205 -3.447  1.00 16.97 ?  82  VAL   B HG13 1 
ATOM   5134 H  HG21 . VAL   B 1 82  ? 41.426 -9.525  -2.946  1.00 16.29 ?  82  VAL   B HG21 1 
ATOM   5135 H  HG22 . VAL   B 1 82  ? 41.963 -10.968 -2.552  1.00 16.29 ?  82  VAL   B HG22 1 
ATOM   5136 H  HG23 . VAL   B 1 82  ? 41.318 -10.031 -1.443  1.00 16.29 ?  82  VAL   B HG23 1 
ATOM   5137 N  N    . LEU   B 1 83  ? 46.391 -10.350 -0.936  1.00 11.28 ?  83  LEU   B N    1 
ATOM   5138 C  CA   . LEU   B 1 83  ? 47.750 -9.836  -0.819  1.00 11.45 ?  83  LEU   B CA   1 
ATOM   5139 C  C    . LEU   B 1 83  ? 48.444 -9.984  -2.173  1.00 11.49 ?  83  LEU   B C    1 
ATOM   5140 O  O    . LEU   B 1 83  ? 47.839 -10.409 -3.162  1.00 11.48 ?  83  LEU   B O    1 
ATOM   5141 C  CB   . LEU   B 1 83  ? 48.499 -10.511 0.340   1.00 11.73 ?  83  LEU   B CB   1 
ATOM   5142 C  CG   . LEU   B 1 83  ? 47.992 -10.146 1.742   1.00 12.97 ?  83  LEU   B CG   1 
ATOM   5143 C  CD1  . LEU   B 1 83  ? 48.628 -11.012 2.808   1.00 13.57 ?  83  LEU   B CD1  1 
ATOM   5144 C  CD2  . LEU   B 1 83  ? 48.210 -8.665  2.062   1.00 13.72 ?  83  LEU   B CD2  1 
ATOM   5145 H  H    . LEU   B 1 83  ? 46.352 -11.149 -1.258  1.00 13.55 ?  83  LEU   B H    1 
ATOM   5146 H  HA   . LEU   B 1 83  ? 47.701 -8.891  -0.629  1.00 13.75 ?  83  LEU   B HA   1 
ATOM   5147 H  HB2  . LEU   B 1 83  ? 48.424 -11.469 0.240   1.00 14.09 ?  83  LEU   B HB2  1 
ATOM   5148 H  HB3  . LEU   B 1 83  ? 49.433 -10.249 0.288   1.00 14.09 ?  83  LEU   B HB3  1 
ATOM   5149 H  HG   . LEU   B 1 83  ? 47.039 -10.307 1.768   1.00 15.57 ?  83  LEU   B HG   1 
ATOM   5150 H  HD11 . LEU   B 1 83  ? 48.275 -10.756 3.675   1.00 16.29 ?  83  LEU   B HD11 1 
ATOM   5151 H  HD12 . LEU   B 1 83  ? 48.410 -11.943 2.627   1.00 16.29 ?  83  LEU   B HD12 1 
ATOM   5152 H  HD13 . LEU   B 1 83  ? 49.588 -10.889 2.791   1.00 16.29 ?  83  LEU   B HD13 1 
ATOM   5153 H  HD21 . LEU   B 1 83  ? 47.990 -8.509  2.995   1.00 16.48 ?  83  LEU   B HD21 1 
ATOM   5154 H  HD22 . LEU   B 1 83  ? 49.136 -8.435  1.898   1.00 16.48 ?  83  LEU   B HD22 1 
ATOM   5155 H  HD23 . LEU   B 1 83  ? 47.631 -8.129  1.496   1.00 16.48 ?  83  LEU   B HD23 1 
ATOM   5156 N  N    . SER   B 1 84  ? 49.721 -9.616  -2.233  1.00 12.34 ?  84  SER   B N    1 
ATOM   5157 C  CA   . SER   B 1 84  ? 50.453 -9.740  -3.484  1.00 12.64 ?  84  SER   B CA   1 
ATOM   5158 C  C    . SER   B 1 84  ? 50.614 -11.204 -3.881  1.00 11.77 ?  84  SER   B C    1 
ATOM   5159 O  O    . SER   B 1 84  ? 50.724 -12.093 -3.036  1.00 11.87 ?  84  SER   B O    1 
ATOM   5160 C  CB   . SER   B 1 84  ? 51.846 -9.136  -3.343  1.00 14.24 ?  84  SER   B CB   1 
ATOM   5161 O  OG   . SER   B 1 84  ? 52.590 -9.356  -4.523  1.00 15.39 ?  84  SER   B OG   1 
ATOM   5162 H  H    . SER   B 1 84  ? 50.171 -9.284  -1.581  1.00 14.82 ?  84  SER   B H    1 
ATOM   5163 H  HA   . SER   B 1 84  ? 49.979 -9.276  -4.193  1.00 15.17 ?  84  SER   B HA   1 
ATOM   5164 H  HB2  . SER   B 1 84  ? 51.763 -8.181  -3.185  1.00 17.10 ?  84  SER   B HB2  1 
ATOM   5165 H  HB3  . SER   B 1 84  ? 52.301 -9.558  -2.599  1.00 17.10 ?  84  SER   B HB3  1 
ATOM   5166 H  HG   . SER   B 1 84  ? 53.359 -9.013  -4.447  1.00 18.48 ?  84  SER   B HG   1 
ATOM   5167 N  N    . GLY   B 1 85  ? 50.679 -11.440 -5.185  1.00 12.79 ?  85  GLY   B N    1 
ATOM   5168 C  CA   . GLY   B 1 85  ? 51.030 -12.740 -5.705  1.00 13.43 ?  85  GLY   B CA   1 
ATOM   5169 C  C    . GLY   B 1 85  ? 52.500 -12.930 -6.016  1.00 12.80 ?  85  GLY   B C    1 
ATOM   5170 O  O    . GLY   B 1 85  ? 52.880 -14.007 -6.481  1.00 13.32 ?  85  GLY   B O    1 
ATOM   5171 H  H    . GLY   B 1 85  ? 50.525 -10.857 -5.795  1.00 15.36 ?  85  GLY   B H    1 
ATOM   5172 H  HA2  . GLY   B 1 85  ? 50.776 -13.421 -5.060  1.00 16.12 ?  85  GLY   B HA2  1 
ATOM   5173 H  HA3  . GLY   B 1 85  ? 50.539 -12.904 -6.520  1.00 16.12 ?  85  GLY   B HA3  1 
ATOM   5174 N  N    . HIS   B 1 86  ? 53.347 -11.927 -5.792  1.00 12.73 ?  86  HIS   B N    1 
ATOM   5175 C  CA   . HIS   B 1 86  ? 54.812 -12.085 -5.879  1.00 12.83 ?  86  HIS   B CA   1 
ATOM   5176 C  C    . HIS   B 1 86  ? 55.186 -12.599 -7.268  1.00 13.06 ?  86  HIS   B C    1 
ATOM   5177 O  O    . HIS   B 1 86  ? 54.788 -11.985 -8.270  1.00 13.90 ?  86  HIS   B O    1 
ATOM   5178 C  CB   . HIS   B 1 86  ? 55.314 -12.916 -4.701  1.00 13.42 ?  86  HIS   B CB   1 
ATOM   5179 C  CG   . HIS   B 1 86  ? 54.995 -12.307 -3.377  1.00 13.53 ?  86  HIS   B CG   1 
ATOM   5180 N  ND1  . HIS   B 1 86  ? 55.827 -11.403 -2.754  1.00 14.70 ?  86  HIS   B ND1  1 
ATOM   5181 C  CD2  . HIS   B 1 86  ? 53.909 -12.438 -2.578  1.00 13.55 ?  86  HIS   B CD2  1 
ATOM   5182 C  CE1  . HIS   B 1 86  ? 55.267 -11.009 -1.623  1.00 14.67 ?  86  HIS   B CE1  1 
ATOM   5183 N  NE2  . HIS   B 1 86  ? 54.102 -11.619 -1.495  1.00 13.77 ?  86  HIS   B NE2  1 
ATOM   5184 H  H    . HIS   B 1 86  ? 53.103 -11.131 -5.583  1.00 15.28 ?  86  HIS   B H    1 
ATOM   5185 H  HA   . HIS   B 1 86  ? 55.215 -11.208 -5.790  1.00 15.40 ?  86  HIS   B HA   1 
ATOM   5186 H  HB2  . HIS   B 1 86  ? 54.906 -13.794 -4.734  1.00 16.11 ?  86  HIS   B HB2  1 
ATOM   5187 H  HB3  . HIS   B 1 86  ? 56.281 -13.000 -4.761  1.00 16.11 ?  86  HIS   B HB3  1 
ATOM   5188 H  HD2  . HIS   B 1 86  ? 53.160 -12.967 -2.743  1.00 16.26 ?  86  HIS   B HD2  1 
ATOM   5189 H  HE1  . HIS   B 1 86  ? 55.638 -10.416 -1.009  1.00 17.61 ?  86  HIS   B HE1  1 
ATOM   5190 H  HE2  . HIS   B 1 86  ? 53.556 -11.526 -0.833  1.00 16.53 ?  86  HIS   B HE2  1 
ATOM   5191 N  N    . ASN   B 1 87  ? 55.955 -13.683 -7.377  1.00 13.27 ?  87  ASN   B N    1 
ATOM   5192 C  CA   . ASN   B 1 87  ? 56.349 -14.259 -8.654  1.00 14.10 ?  87  ASN   B CA   1 
ATOM   5193 C  C    . ASN   B 1 87  ? 55.362 -15.298 -9.158  1.00 13.79 ?  87  ASN   B C    1 
ATOM   5194 O  O    . ASN   B 1 87  ? 55.670 -16.007 -10.123 1.00 15.79 ?  87  ASN   B O    1 
ATOM   5195 C  CB   . ASN   B 1 87  ? 57.737 -14.895 -8.530  1.00 16.17 ?  87  ASN   B CB   1 
ATOM   5196 C  CG   . ASN   B 1 87  ? 57.784 -16.009 -7.489  1.00 16.89 ?  87  ASN   B CG   1 
ATOM   5197 O  OD1  . ASN   B 1 87  ? 57.156 -15.918 -6.431  1.00 16.08 ?  87  ASN   B OD1  1 
ATOM   5198 N  ND2  . ASN   B 1 87  ? 58.521 -17.080 -7.800  1.00 19.00 ?  87  ASN   B ND2  1 
ATOM   5199 H  H    . ASN   B 1 87  ? 56.259 -14.119 -6.702  1.00 15.93 ?  87  ASN   B H    1 
ATOM   5200 H  HA   . ASN   B 1 87  ? 56.399 -13.556 -9.314  1.00 16.93 ?  87  ASN   B HA   1 
ATOM   5201 H  HB2  . ASN   B 1 87  ? 57.990 -15.274 -9.388  1.00 19.41 ?  87  ASN   B HB2  1 
ATOM   5202 H  HB3  . ASN   B 1 87  ? 58.374 -14.212 -8.270  1.00 19.41 ?  87  ASN   B HB3  1 
ATOM   5203 H  HD21 . ASN   B 1 87  ? 58.587 -17.734 -7.248  1.00 22.81 ?  87  ASN   B HD21 1 
ATOM   5204 H  HD22 . ASN   B 1 87  ? 58.942 -17.110 -8.553  1.00 22.81 ?  87  ASN   B HD22 1 
ATOM   5205 N  N    . LEU   B 1 88  ? 54.185 -15.399 -8.535  1.00 12.72 ?  88  LEU   B N    1 
ATOM   5206 C  CA   . LEU   B 1 88  ? 53.202 -16.429 -8.858  1.00 13.25 ?  88  LEU   B CA   1 
ATOM   5207 C  C    . LEU   B 1 88  ? 51.974 -15.911 -9.584  1.00 12.93 ?  88  LEU   B C    1 
ATOM   5208 O  O    . LEU   B 1 88  ? 51.374 -16.655 -10.369 1.00 14.59 ?  88  LEU   B O    1 
ATOM   5209 C  CB   . LEU   B 1 88  ? 52.729 -17.112 -7.571  1.00 14.32 ?  88  LEU   B CB   1 
ATOM   5210 C  CG   . LEU   B 1 88  ? 53.854 -17.764 -6.775  1.00 16.73 ?  88  LEU   B CG   1 
ATOM   5211 C  CD1  . LEU   B 1 88  ? 53.356 -18.206 -5.411  1.00 18.19 ?  88  LEU   B CD1  1 
ATOM   5212 C  CD2  . LEU   B 1 88  ? 54.429 -18.931 -7.555  1.00 20.10 ?  88  LEU   B CD2  1 
ATOM   5213 H  H    . LEU   B 1 88  ? 53.926 -14.869 -7.901  1.00 15.28 ?  88  LEU   B H    1 
ATOM   5214 H  HA   . LEU   B 1 88  ? 53.617 -17.095 -9.418  1.00 15.91 ?  88  LEU   B HA   1 
ATOM   5215 H  HB2  . LEU   B 1 88  ? 52.305 -16.454 -6.998  1.00 17.19 ?  88  LEU   B HB2  1 
ATOM   5216 H  HB3  . LEU   B 1 88  ? 52.089 -17.806 -7.802  1.00 17.19 ?  88  LEU   B HB3  1 
ATOM   5217 H  HG   . LEU   B 1 88  ? 54.560 -17.116 -6.639  1.00 20.08 ?  88  LEU   B HG   1 
ATOM   5218 H  HD11 . LEU   B 1 88  ? 54.067 -18.680 -4.954  1.00 21.83 ?  88  LEU   B HD11 1 
ATOM   5219 H  HD12 . LEU   B 1 88  ? 53.095 -17.424 -4.901  1.00 21.83 ?  88  LEU   B HD12 1 
ATOM   5220 H  HD13 . LEU   B 1 88  ? 52.592 -18.792 -5.533  1.00 21.83 ?  88  LEU   B HD13 1 
ATOM   5221 H  HD21 . LEU   B 1 88  ? 55.035 -19.424 -6.981  1.00 24.13 ?  88  LEU   B HD21 1 
ATOM   5222 H  HD22 . LEU   B 1 88  ? 53.704 -19.507 -7.843  1.00 24.13 ?  88  LEU   B HD22 1 
ATOM   5223 H  HD23 . LEU   B 1 88  ? 54.908 -18.591 -8.327  1.00 24.13 ?  88  LEU   B HD23 1 
ATOM   5224 N  N    . ALA   B 1 89  ? 51.569 -14.677 -9.313  1.00 12.37 ?  89  ALA   B N    1 
ATOM   5225 C  CA   . ALA   B 1 89  ? 50.277 -14.179 -9.758  1.00 11.76 ?  89  ALA   B CA   1 
ATOM   5226 C  C    . ALA   B 1 89  ? 50.257 -12.691 -9.466  1.00 12.31 ?  89  ALA   B C    1 
ATOM   5227 O  O    . ALA   B 1 89  ? 51.094 -12.183 -8.717  1.00 13.09 ?  89  ALA   B O    1 
ATOM   5228 C  CB   . ALA   B 1 89  ? 49.140 -14.851 -9.000  1.00 11.94 ?  89  ALA   B CB   1 
ATOM   5229 H  H    . ALA   B 1 89  ? 52.021 -14.099 -8.860  1.00 14.86 ?  89  ALA   B H    1 
ATOM   5230 H  HA   . ALA   B 1 89  ? 50.165 -14.321 -10.714 1.00 14.13 ?  89  ALA   B HA   1 
ATOM   5231 H  HB1  . ALA   B 1 89  ? 48.294 -14.511 -9.337  1.00 14.33 ?  89  ALA   B HB1  1 
ATOM   5232 H  HB2  . ALA   B 1 89  ? 49.192 -15.809 -9.152  1.00 14.33 ?  89  ALA   B HB2  1 
ATOM   5233 H  HB3  . ALA   B 1 89  ? 49.230 -14.655 -8.061  1.00 14.33 ?  89  ALA   B HB3  1 
ATOM   5234 N  N    . LYS   B 1 90  ? 49.281 -11.989 -10.039 1.00 13.02 ?  90  LYS   B N    1 
ATOM   5235 C  CA   . LYS   B 1 90  ? 49.096 -10.602 -9.631  1.00 13.11 ?  90  LYS   B CA   1 
ATOM   5236 C  C    . LYS   B 1 90  ? 48.773 -10.528 -8.144  1.00 12.82 ?  90  LYS   B C    1 
ATOM   5237 O  O    . LYS   B 1 90  ? 49.414 -9.776  -7.391  1.00 13.77 ?  90  LYS   B O    1 
ATOM   5238 C  CB   . LYS   B 1 90  ? 48.020 -9.939  -10.491 1.00 14.57 ?  90  LYS   B CB   1 
ATOM   5239 C  CG   . LYS   B 1 90  ? 47.711 -8.504  -10.110 1.00 15.23 ?  90  LYS   B CG   1 
ATOM   5240 C  CD   . LYS   B 1 90  ? 48.923 -7.610  -10.150 1.00 17.53 ?  90  LYS   B CD   1 
ATOM   5241 C  CE   . LYS   B 1 90  ? 48.475 -6.188  -9.906  1.00 19.50 ?  90  LYS   B CE   1 
ATOM   5242 N  NZ   . LYS   B 1 90  ? 49.624 -5.262  -9.791  1.00 19.41 ?  90  LYS   B NZ   1 
ATOM   5243 H  H    . LYS   B 1 90  ? 48.735 -12.282 -10.638 1.00 15.64 ?  90  LYS   B H    1 
ATOM   5244 H  HA   . LYS   B 1 90  ? 49.920 -10.124 -9.775  1.00 15.74 ?  90  LYS   B HA   1 
ATOM   5245 H  HB2  . LYS   B 1 90  ? 48.319 -9.933  -11.419 1.00 17.49 ?  90  LYS   B HB2  1 
ATOM   5246 H  HB3  . LYS   B 1 90  ? 47.196 -10.446 -10.423 1.00 17.49 ?  90  LYS   B HB3  1 
ATOM   5247 H  HG2  . LYS   B 1 90  ? 47.054 -8.143  -10.730 1.00 18.28 ?  90  LYS   B HG2  1 
ATOM   5248 H  HG3  . LYS   B 1 90  ? 47.349 -8.485  -9.208  1.00 18.28 ?  90  LYS   B HG3  1 
ATOM   5249 H  HD2  . LYS   B 1 90  ? 49.545 -7.863  -9.448  1.00 21.04 ?  90  LYS   B HD2  1 
ATOM   5250 H  HD3  . LYS   B 1 90  ? 49.345 -7.661  -11.020 1.00 21.04 ?  90  LYS   B HD3  1 
ATOM   5251 H  HE2  . LYS   B 1 90  ? 47.926 -5.886  -10.650 1.00 23.41 ?  90  LYS   B HE2  1 
ATOM   5252 H  HE3  . LYS   B 1 90  ? 47.971 -6.138  -9.079  1.00 23.41 ?  90  LYS   B HE3  1 
ATOM   5253 H  HZ1  . LYS   B 1 90  ? 49.339 -4.429  -9.650  1.00 23.30 ?  90  LYS   B HZ1  1 
ATOM   5254 H  HZ2  . LYS   B 1 90  ? 50.146 -5.505  -9.111  1.00 23.30 ?  90  LYS   B HZ2  1 
ATOM   5255 H  HZ3  . LYS   B 1 90  ? 50.106 -5.276  -10.541 1.00 23.30 ?  90  LYS   B HZ3  1 
ATOM   5256 N  N    . HIS   B 1 91  ? 47.803 -11.337 -7.702  1.00 11.61 ?  91  HIS   B N    1 
ATOM   5257 C  CA   . HIS   B 1 91  ? 47.333 -11.360 -6.332  1.00 11.46 ?  91  HIS   B CA   1 
ATOM   5258 C  C    . HIS   B 1 91  ? 47.328 -12.785 -5.811  1.00 11.00 ?  91  HIS   B C    1 
ATOM   5259 O  O    . HIS   B 1 91  ? 47.108 -13.740 -6.563  1.00 11.62 ?  91  HIS   B O    1 
ATOM   5260 C  CB   . HIS   B 1 91  ? 45.886 -10.874 -6.228  1.00 13.11 ?  91  HIS   B CB   1 
ATOM   5261 C  CG   . HIS   B 1 91  ? 45.684 -9.461  -6.655  1.00 16.34 ?  91  HIS   B CG   1 
ATOM   5262 N  ND1  . HIS   B 1 91  ? 46.301 -8.395  -6.035  1.00 18.85 ?  91  HIS   B ND1  1 
ATOM   5263 C  CD2  . HIS   B 1 91  ? 44.897 -8.933  -7.618  1.00 18.71 ?  91  HIS   B CD2  1 
ATOM   5264 C  CE1  . HIS   B 1 91  ? 45.923 -7.270  -6.617  1.00 19.82 ?  91  HIS   B CE1  1 
ATOM   5265 N  NE2  . HIS   B 1 91  ? 45.068 -7.570  -7.578  1.00 20.09 ?  91  HIS   B NE2  1 
ATOM   5266 H  H    . HIS   B 1 91  ? 47.383 -11.898 -8.204  1.00 13.94 ?  91  HIS   B H    1 
ATOM   5267 H  HA   . HIS   B 1 91  ? 47.902 -10.798 -5.767  1.00 13.76 ?  91  HIS   B HA   1 
ATOM   5268 H  HB2  . HIS   B 1 91  ? 45.327 -11.430 -6.790  1.00 15.75 ?  91  HIS   B HB2  1 
ATOM   5269 H  HB3  . HIS   B 1 91  ? 45.592 -10.944 -5.303  1.00 15.75 ?  91  HIS   B HB3  1 
ATOM   5270 H  HD1  . HIS   B 1 91  ? 46.853 -8.453  -5.376  1.00 22.63 ?  91  HIS   B HD1  1 
ATOM   5271 H  HD2  . HIS   B 1 91  ? 44.353 -9.392  -8.212  1.00 22.46 ?  91  HIS   B HD2  1 
ATOM   5272 H  HE1  . HIS   B 1 91  ? 46.208 -6.412  -6.381  1.00 23.79 ?  91  HIS   B HE1  1 
ATOM   5273 N  N    . CYS   B 1 92  ? 47.517 -12.913 -4.506  1.00 10.91 ?  92  CYS   B N    1 
ATOM   5274 C  CA   . CYS   B 1 92  ? 47.214 -14.145 -3.793  1.00 10.60 ?  92  CYS   B CA   1 
ATOM   5275 C  C    . CYS   B 1 92  ? 45.990 -13.903 -2.920  1.00 10.32 ?  92  CYS   B C    1 
ATOM   5276 O  O    . CYS   B 1 92  ? 45.990 -13.000 -2.075  1.00 11.21 ?  92  CYS   B O    1 
ATOM   5277 C  CB   . CYS   B 1 92  ? 48.388 -14.606 -2.937  1.00 11.10 ?  92  CYS   B CB   1 
ATOM   5278 S  SG   . CYS   B 1 92  ? 48.024 -16.141 -2.040  1.00 11.10 ?  92  CYS   B SG   1 
ATOM   5279 H  H    . CYS   B 1 92  ? 47.841 -12.288 -3.998  1.00 13.10 ?  92  CYS   B H    1 
ATOM   5280 H  HA   . CYS   B 1 92  ? 47.014 -14.841 -4.438  1.00 12.73 ?  92  CYS   B HA   1 
ATOM   5281 H  HB2  . CYS   B 1 92  ? 49.157 -14.755 -3.501  1.00 13.32 ?  92  CYS   B HB2  1 
ATOM   5282 H  HB3  . CYS   B 1 92  ? 48.583 -13.917 -2.279  1.00 13.32 ?  92  CYS   B HB3  1 
ATOM   5283 H  HG   . CYS   B 1 92  ? 49.003 -16.460 -1.410  1.00 13.32 ?  92  CYS   B HG   1 
ATOM   5284 N  N    . LEU   B 1 93  ? 44.954 -14.711 -3.129  1.00 10.30 ?  93  LEU   B N    1 
ATOM   5285 C  CA   . LEU   B 1 93  ? 43.778 -14.716 -2.270  1.00 10.30 ?  93  LEU   B CA   1 
ATOM   5286 C  C    . LEU   B 1 93  ? 43.998 -15.779 -1.201  1.00 9.98  ?  93  LEU   B C    1 
ATOM   5287 O  O    . LEU   B 1 93  ? 43.953 -16.982 -1.494  1.00 10.71 ?  93  LEU   B O    1 
ATOM   5288 C  CB   . LEU   B 1 93  ? 42.520 -15.012 -3.081  1.00 10.83 ?  93  LEU   B CB   1 
ATOM   5289 C  CG   . LEU   B 1 93  ? 41.220 -15.026 -2.272  1.00 11.62 ?  93  LEU   B CG   1 
ATOM   5290 C  CD1  . LEU   B 1 93  ? 40.875 -13.632 -1.780  1.00 11.95 ?  93  LEU   B CD1  1 
ATOM   5291 C  CD2  . LEU   B 1 93  ? 40.084 -15.622 -3.091  1.00 11.82 ?  93  LEU   B CD2  1 
ATOM   5292 H  H    . LEU   B 1 93  ? 44.914 -15.284 -3.781  1.00 12.37 ?  93  LEU   B H    1 
ATOM   5293 H  HA   . LEU   B 1 93  ? 43.685 -13.854 -1.846  1.00 12.36 ?  93  LEU   B HA   1 
ATOM   5294 H  HB2  . LEU   B 1 93  ? 42.429 -14.327 -3.767  1.00 13.00 ?  93  LEU   B HB2  1 
ATOM   5295 H  HB3  . LEU   B 1 93  ? 42.615 -15.878 -3.499  1.00 13.00 ?  93  LEU   B HB3  1 
ATOM   5296 H  HG   . LEU   B 1 93  ? 41.347 -15.586 -1.495  1.00 13.96 ?  93  LEU   B HG   1 
ATOM   5297 H  HD11 . LEU   B 1 93  ? 40.019 -13.659 -1.330  1.00 14.35 ?  93  LEU   B HD11 1 
ATOM   5298 H  HD12 . LEU   B 1 93  ? 41.564 -13.329 -1.169  1.00 14.35 ?  93  LEU   B HD12 1 
ATOM   5299 H  HD13 . LEU   B 1 93  ? 40.827 -13.030 -2.544  1.00 14.35 ?  93  LEU   B HD13 1 
ATOM   5300 H  HD21 . LEU   B 1 93  ? 39.274 -15.612 -2.559  1.00 14.20 ?  93  LEU   B HD21 1 
ATOM   5301 H  HD22 . LEU   B 1 93  ? 39.961 -15.094 -3.895  1.00 14.20 ?  93  LEU   B HD22 1 
ATOM   5302 H  HD23 . LEU   B 1 93  ? 40.313 -16.536 -3.329  1.00 14.20 ?  93  LEU   B HD23 1 
ATOM   5303 N  N    . HIS   B 1 94  ? 44.273 -15.341 0.023   1.00 10.11 ?  94  HIS   B N    1 
ATOM   5304 C  CA   . HIS   B 1 94  ? 44.497 -16.247 1.141   1.00 10.25 ?  94  HIS   B CA   1 
ATOM   5305 C  C    . HIS   B 1 94  ? 43.134 -16.596 1.722   1.00 10.50 ?  94  HIS   B C    1 
ATOM   5306 O  O    . HIS   B 1 94  ? 42.467 -15.723 2.275   1.00 11.91 ?  94  HIS   B O    1 
ATOM   5307 C  CB   . HIS   B 1 94  ? 45.365 -15.568 2.197   1.00 10.52 ?  94  HIS   B CB   1 
ATOM   5308 C  CG   . HIS   B 1 94  ? 46.748 -15.269 1.730   1.00 10.67 ?  94  HIS   B CG   1 
ATOM   5309 N  ND1  . HIS   B 1 94  ? 47.772 -16.189 1.815   1.00 10.91 ?  94  HIS   B ND1  1 
ATOM   5310 C  CD2  . HIS   B 1 94  ? 47.259 -14.166 1.129   1.00 10.86 ?  94  HIS   B CD2  1 
ATOM   5311 C  CE1  . HIS   B 1 94  ? 48.862 -15.642 1.305   1.00 11.15 ?  94  HIS   B CE1  1 
ATOM   5312 N  NE2  . HIS   B 1 94  ? 48.580 -14.420 0.880   1.00 11.26 ?  94  HIS   B NE2  1 
ATOM   5313 H  H    . HIS   B 1 94  ? 44.345 -14.506 0.226   1.00 12.14 ?  94  HIS   B H    1 
ATOM   5314 H  HA   . HIS   B 1 94  ? 44.931 -17.057 0.830   1.00 12.31 ?  94  HIS   B HA   1 
ATOM   5315 H  HB2  . HIS   B 1 94  ? 44.949 -14.733 2.448   1.00 12.63 ?  94  HIS   B HB2  1 
ATOM   5316 H  HB3  . HIS   B 1 94  ? 45.432 -16.156 2.961   1.00 12.63 ?  94  HIS   B HB3  1 
ATOM   5317 H  HD2  . HIS   B 1 94  ? 46.802 -13.383 0.927   1.00 13.04 ?  94  HIS   B HD2  1 
ATOM   5318 H  HE1  . HIS   B 1 94  ? 49.691 -16.061 1.244   1.00 13.38 ?  94  HIS   B HE1  1 
ATOM   5319 H  HE2  . HIS   B 1 94  ? 49.138 -13.882 0.509   1.00 13.52 ?  94  HIS   B HE2  1 
ATOM   5320 N  N    . VAL   B 1 95  ? 42.701 -17.849 1.571   1.00 10.57 ?  95  VAL   B N    1 
ATOM   5321 C  CA   . VAL   B 1 95  ? 41.374 -18.287 2.003   1.00 10.74 ?  95  VAL   B CA   1 
ATOM   5322 C  C    . VAL   B 1 95  ? 41.541 -19.322 3.099   1.00 11.07 ?  95  VAL   B C    1 
ATOM   5323 O  O    . VAL   B 1 95  ? 42.316 -20.275 2.944   1.00 11.66 ?  95  VAL   B O    1 
ATOM   5324 C  CB   . VAL   B 1 95  ? 40.557 -18.893 0.846   1.00 11.06 ?  95  VAL   B CB   1 
ATOM   5325 C  CG1  . VAL   B 1 95  ? 39.178 -19.331 1.336   1.00 12.40 ?  95  VAL   B CG1  1 
ATOM   5326 C  CG2  . VAL   B 1 95  ? 40.437 -17.911 -0.296  1.00 11.11 ?  95  VAL   B CG2  1 
ATOM   5327 H  H    . VAL   B 1 95  ? 43.165 -18.478 1.206   1.00 12.70 ?  95  VAL   B H    1 
ATOM   5328 H  HA   . VAL   B 1 95  ? 40.883 -17.532 2.363   1.00 12.90 ?  95  VAL   B HA   1 
ATOM   5329 H  HB   . VAL   B 1 95  ? 41.011 -19.674 0.513   1.00 13.28 ?  95  VAL   B HB   1 
ATOM   5330 H  HG11 . VAL   B 1 95  ? 38.611 -19.519 0.566   1.00 14.89 ?  95  VAL   B HG11 1 
ATOM   5331 H  HG12 . VAL   B 1 95  ? 39.268 -20.130 1.876   1.00 14.89 ?  95  VAL   B HG12 1 
ATOM   5332 H  HG13 . VAL   B 1 95  ? 38.780 -18.617 1.862   1.00 14.89 ?  95  VAL   B HG13 1 
ATOM   5333 H  HG21 . VAL   B 1 95  ? 39.858 -18.290 -0.974  1.00 13.35 ?  95  VAL   B HG21 1 
ATOM   5334 H  HG22 . VAL   B 1 95  ? 40.056 -17.084 0.041   1.00 13.35 ?  95  VAL   B HG22 1 
ATOM   5335 H  HG23 . VAL   B 1 95  ? 41.318 -17.750 -0.659  1.00 13.35 ?  95  VAL   B HG23 1 
ATOM   5336 N  N    . VAL   B 1 96  ? 40.807 -19.148 4.193   1.00 11.54 ?  96  VAL   B N    1 
ATOM   5337 C  CA   . VAL   B 1 96  ? 40.889 -20.053 5.336   1.00 11.76 ?  96  VAL   B CA   1 
ATOM   5338 C  C    . VAL   B 1 96  ? 39.702 -21.011 5.290   1.00 12.24 ?  96  VAL   B C    1 
ATOM   5339 O  O    . VAL   B 1 96  ? 38.583 -20.652 5.668   1.00 13.13 ?  96  VAL   B O    1 
ATOM   5340 C  CB   . VAL   B 1 96  ? 40.938 -19.299 6.668   1.00 12.42 ?  96  VAL   B CB   1 
ATOM   5341 C  CG1  . VAL   B 1 96  ? 41.119 -20.295 7.811   1.00 13.31 ?  96  VAL   B CG1  1 
ATOM   5342 C  CG2  . VAL   B 1 96  ? 42.052 -18.262 6.674   1.00 12.98 ?  96  VAL   B CG2  1 
ATOM   5343 H  H    . VAL   B 1 96  ? 40.246 -18.506 4.304   1.00 13.86 ?  96  VAL   B H    1 
ATOM   5344 H  HA   . VAL   B 1 96  ? 41.702 -20.582 5.266   1.00 14.12 ?  96  VAL   B HA   1 
ATOM   5345 H  HB   . VAL   B 1 96  ? 40.094 -18.843 6.806   1.00 14.91 ?  96  VAL   B HB   1 
ATOM   5346 H  HG11 . VAL   B 1 96  ? 41.309 -19.807 8.630   1.00 15.99 ?  96  VAL   B HG11 1 
ATOM   5347 H  HG12 . VAL   B 1 96  ? 40.305 -20.812 7.922   1.00 15.99 ?  96  VAL   B HG12 1 
ATOM   5348 H  HG13 . VAL   B 1 96  ? 41.861 -20.886 7.605   1.00 15.99 ?  96  VAL   B HG13 1 
ATOM   5349 H  HG21 . VAL   B 1 96  ? 42.095 -17.850 7.554   1.00 15.59 ?  96  VAL   B HG21 1 
ATOM   5350 H  HG22 . VAL   B 1 96  ? 42.892 -18.695 6.470   1.00 15.59 ?  96  VAL   B HG22 1 
ATOM   5351 H  HG23 . VAL   B 1 96  ? 41.854 -17.585 6.007   1.00 15.59 ?  96  VAL   B HG23 1 
ATOM   5352 N  N    . GLY   B 1 97  ? 39.938 -22.240 4.841   1.00 12.42 ?  97  GLY   B N    1 
ATOM   5353 C  CA   . GLY   B 1 97  ? 38.972 -23.301 5.004   1.00 13.32 ?  97  GLY   B CA   1 
ATOM   5354 C  C    . GLY   B 1 97  ? 39.102 -23.912 6.382   1.00 14.57 ?  97  GLY   B C    1 
ATOM   5355 O  O    . GLY   B 1 97  ? 40.144 -23.786 7.038   1.00 14.92 ?  97  GLY   B O    1 
ATOM   5356 H  H    . GLY   B 1 97  ? 40.661 -22.479 4.434   1.00 14.91 ?  97  GLY   B H    1 
ATOM   5357 H  HA2  . GLY   B 1 97  ? 38.076 -22.939 4.889   1.00 16.00 ?  97  GLY   B HA2  1 
ATOM   5358 H  HA3  . GLY   B 1 97  ? 39.117 -23.986 4.331   1.00 16.00 ?  97  GLY   B HA3  1 
ATOM   5359 N  N    . PRO   B 1 98  ? 38.051 -24.589 6.851   1.00 15.87 ?  98  PRO   B N    1 
ATOM   5360 C  CA   . PRO   B 1 98  ? 38.146 -25.283 8.139   1.00 17.05 ?  98  PRO   B CA   1 
ATOM   5361 C  C    . PRO   B 1 98  ? 39.175 -26.404 8.094   1.00 16.67 ?  98  PRO   B C    1 
ATOM   5362 O  O    . PRO   B 1 98  ? 39.279 -27.143 7.115   1.00 16.63 ?  98  PRO   B O    1 
ATOM   5363 C  CB   . PRO   B 1 98  ? 36.728 -25.830 8.349   1.00 17.37 ?  98  PRO   B CB   1 
ATOM   5364 C  CG   . PRO   B 1 98  ? 36.159 -25.955 6.986   1.00 16.86 ?  98  PRO   B CG   1 
ATOM   5365 C  CD   . PRO   B 1 98  ? 36.730 -24.782 6.223   1.00 16.28 ?  98  PRO   B CD   1 
ATOM   5366 H  HA   . PRO   B 1 98  ? 38.369 -24.658 8.841   1.00 20.47 ?  98  PRO   B HA   1 
ATOM   5367 H  HB2  . PRO   B 1 98  ? 36.774 -26.696 8.781   1.00 20.85 ?  98  PRO   B HB2  1 
ATOM   5368 H  HB3  . PRO   B 1 98  ? 36.213 -25.204 8.879   1.00 20.85 ?  98  PRO   B HB3  1 
ATOM   5369 H  HG2  . PRO   B 1 98  ? 36.442 -26.794 6.587   1.00 20.24 ?  98  PRO   B HG2  1 
ATOM   5370 H  HG3  . PRO   B 1 98  ? 35.192 -25.902 7.027   1.00 20.24 ?  98  PRO   B HG3  1 
ATOM   5371 H  HD2  . PRO   B 1 98  ? 36.820 -25.004 5.278   1.00 19.54 ?  98  PRO   B HD2  1 
ATOM   5372 H  HD3  . PRO   B 1 98  ? 36.178 -23.993 6.348   1.00 19.54 ?  98  PRO   B HD3  1 
ATOM   5373 N  N    . ASN   B 1 99  ? 39.937 -26.525 9.174   1.00 17.70 ?  99  ASN   B N    1 
ATOM   5374 C  CA   . ASN   B 1 99  ? 40.921 -27.593 9.337   1.00 19.01 ?  99  ASN   B CA   1 
ATOM   5375 C  C    . ASN   B 1 99  ? 40.301 -28.665 10.229  1.00 21.97 ?  99  ASN   B C    1 
ATOM   5376 O  O    . ASN   B 1 99  ? 40.249 -28.518 11.453  1.00 22.70 ?  99  ASN   B O    1 
ATOM   5377 C  CB   . ASN   B 1 99  ? 42.201 -27.031 9.942   1.00 19.14 ?  99  ASN   B CB   1 
ATOM   5378 C  CG   . ASN   B 1 99  ? 43.331 -28.039 9.957   1.00 19.90 ?  99  ASN   B CG   1 
ATOM   5379 O  OD1  . ASN   B 1 99  ? 43.108 -29.227 10.145  1.00 20.55 ?  99  ASN   B OD1  1 
ATOM   5380 N  ND2  . ASN   B 1 99  ? 44.546 -27.567 9.758   1.00 20.14 ?  99  ASN   B ND2  1 
ATOM   5381 H  H    . ASN   B 1 99  ? 39.898 -25.985 9.840   1.00 21.25 ?  99  ASN   B H    1 
ATOM   5382 H  HA   . ASN   B 1 99  ? 41.120 -27.989 8.473   1.00 22.82 ?  99  ASN   B HA   1 
ATOM   5383 H  HB2  . ASN   B 1 99  ? 42.480 -26.268 9.426   1.00 22.98 ?  99  ASN   B HB2  1 
ATOM   5384 H  HB3  . ASN   B 1 99  ? 42.017 -26.773 10.860  1.00 22.98 ?  99  ASN   B HB3  1 
ATOM   5385 H  HD21 . ASN   B 1 99  ? 45.218 -28.100 9.754   1.00 24.17 ?  99  ASN   B HD21 1 
ATOM   5386 H  HD22 . ASN   B 1 99  ? 44.658 -26.724 9.637   1.00 24.17 ?  99  ASN   B HD22 1 
ATOM   5387 N  N    A VAL   B 1 100 ? 39.814 -29.743 9.607   0.64 23.96 ?  100 VAL   B N    1 
ATOM   5388 N  N    B VAL   B 1 100 ? 39.822 -29.744 9.601   0.36 24.10 ?  100 VAL   B N    1 
ATOM   5389 C  CA   A VAL   B 1 100 ? 39.202 -30.825 10.373  0.64 26.65 ?  100 VAL   B CA   1 
ATOM   5390 C  CA   B VAL   B 1 100 ? 39.203 -30.838 10.344  0.36 26.44 ?  100 VAL   B CA   1 
ATOM   5391 C  C    A VAL   B 1 100 ? 40.221 -31.473 11.299  0.64 27.17 ?  100 VAL   B C    1 
ATOM   5392 C  C    B VAL   B 1 100 ? 40.211 -31.507 11.270  0.36 27.10 ?  100 VAL   B C    1 
ATOM   5393 O  O    A VAL   B 1 100 ? 39.875 -31.921 12.399  0.64 27.95 ?  100 VAL   B O    1 
ATOM   5394 O  O    B VAL   B 1 100 ? 39.844 -32.008 12.341  0.36 27.51 ?  100 VAL   B O    1 
ATOM   5395 C  CB   A VAL   B 1 100 ? 38.536 -31.844 9.426   0.64 28.83 ?  100 VAL   B CB   1 
ATOM   5396 C  CB   B VAL   B 1 100 ? 38.553 -31.835 9.362   0.36 28.02 ?  100 VAL   B CB   1 
ATOM   5397 C  CG1  A VAL   B 1 100 ? 38.050 -33.060 10.201  0.64 29.83 ?  100 VAL   B CG1  1 
ATOM   5398 C  CG1  B VAL   B 1 100 ? 38.055 -33.072 10.093  0.36 28.66 ?  100 VAL   B CG1  1 
ATOM   5399 C  CG2  A VAL   B 1 100 ? 37.380 -31.192 8.682   0.64 29.34 ?  100 VAL   B CG2  1 
ATOM   5400 C  CG2  B VAL   B 1 100 ? 37.411 -31.164 8.610   0.36 28.52 ?  100 VAL   B CG2  1 
ATOM   5401 H  H    A VAL   B 1 100 ? 39.826 -29.868 8.755   0.64 28.76 ?  100 VAL   B H    1 
ATOM   5402 H  H    B VAL   B 1 100 ? 39.838 -29.862 8.748   0.36 28.93 ?  100 VAL   B H    1 
ATOM   5403 H  HA   A VAL   B 1 100 ? 38.497 -30.450 10.925  0.64 31.99 ?  100 VAL   B HA   1 
ATOM   5404 H  HA   B VAL   B 1 100 ? 38.492 -30.475 10.895  0.36 31.73 ?  100 VAL   B HA   1 
ATOM   5405 H  HB   A VAL   B 1 100 ? 39.186 -32.145 8.772   0.64 34.60 ?  100 VAL   B HB   1 
ATOM   5406 H  HB   B VAL   B 1 100 ? 39.215 -32.119 8.712   0.36 33.63 ?  100 VAL   B HB   1 
ATOM   5407 H  HG11 A VAL   B 1 100 ? 37.445 -33.571 9.639   0.64 35.81 ?  100 VAL   B HG11 1 
ATOM   5408 H  HG11 B VAL   B 1 100 ? 37.470 -33.573 9.500   0.36 34.40 ?  100 VAL   B HG11 1 
ATOM   5409 H  HG12 A VAL   B 1 100 ? 38.811 -33.608 10.446  0.64 35.81 ?  100 VAL   B HG12 1 
ATOM   5410 H  HG12 B VAL   B 1 100 ? 38.813 -33.621 10.346  0.36 34.40 ?  100 VAL   B HG12 1 
ATOM   5411 H  HG13 A VAL   B 1 100 ? 37.584 -32.762 10.998  0.64 35.81 ?  100 VAL   B HG13 1 
ATOM   5412 H  HG13 B VAL   B 1 100 ? 37.564 -32.797 10.882  0.36 34.40 ?  100 VAL   B HG13 1 
ATOM   5413 H  HG21 A VAL   B 1 100 ? 36.965 -31.851 8.104   0.64 35.22 ?  100 VAL   B HG21 1 
ATOM   5414 H  HG21 B VAL   B 1 100 ? 36.997 -31.812 8.019   0.36 34.23 ?  100 VAL   B HG21 1 
ATOM   5415 H  HG22 A VAL   B 1 100 ? 36.734 -30.866 9.329   0.64 35.22 ?  100 VAL   B HG22 1 
ATOM   5416 H  HG22 B VAL   B 1 100 ? 36.760 -30.838 9.251   0.36 34.23 ?  100 VAL   B HG22 1 
ATOM   5417 H  HG23 A VAL   B 1 100 ? 37.722 -30.456 8.153   0.64 35.22 ?  100 VAL   B HG23 1 
ATOM   5418 H  HG23 B VAL   B 1 100 ? 37.766 -30.424 8.093   0.36 34.23 ?  100 VAL   B HG23 1 
ATOM   5419 N  N    . ASN   B 1 101 ? 41.488 -31.532 10.882  1.00 27.63 ?  101 ASN   B N    1 
ATOM   5420 C  CA   . ASN   B 1 101 ? 42.528 -32.087 11.747  1.00 29.19 ?  101 ASN   B CA   1 
ATOM   5421 C  C    . ASN   B 1 101 ? 42.751 -31.250 12.999  1.00 31.61 ?  101 ASN   B C    1 
ATOM   5422 O  O    . ASN   B 1 101 ? 43.402 -31.727 13.937  1.00 32.55 ?  101 ASN   B O    1 
ATOM   5423 C  CB   . ASN   B 1 101 ? 43.842 -32.239 10.980  1.00 29.06 ?  101 ASN   B CB   1 
ATOM   5424 C  CG   . ASN   B 1 101 ? 43.816 -33.398 10.005  1.00 28.56 ?  101 ASN   B CG   1 
ATOM   5425 O  OD1  . ASN   B 1 101 ? 43.141 -34.394 10.233  1.00 29.06 ?  101 ASN   B OD1  1 
ATOM   5426 N  ND2  . ASN   B 1 101 ? 44.544 -33.266 8.904   1.00 28.09 ?  101 ASN   B ND2  1 
ATOM   5427 H  H    A ASN   B 1 101 ? 41.764 -31.261 10.112  0.64 33.16 ?  101 ASN   B H    1 
ATOM   5428 H  H    B ASN   B 1 101 ? 41.773 -31.237 10.124  0.36 33.16 ?  101 ASN   B H    1 
ATOM   5429 H  HA   . ASN   B 1 101 ? 42.248 -32.968 12.032  1.00 35.04 ?  101 ASN   B HA   1 
ATOM   5430 H  HB2  . ASN   B 1 101 ? 44.016 -31.431 10.477  1.00 34.89 ?  101 ASN   B HB2  1 
ATOM   5431 H  HB3  . ASN   B 1 101 ? 44.559 -32.397 11.615  1.00 34.89 ?  101 ASN   B HB3  1 
ATOM   5432 H  HD21 . ASN   B 1 101 ? 44.561 -33.898 8.322   1.00 33.72 ?  101 ASN   B HD21 1 
ATOM   5433 H  HD22 . ASN   B 1 101 ? 44.997 -32.548 8.776   1.00 33.72 ?  101 ASN   B HD22 1 
ATOM   5434 N  N    . LYS   B 1 102 ? 42.241 -30.018 13.025  1.00 34.27 ?  102 LYS   B N    1 
ATOM   5435 C  CA   . LYS   B 1 102 ? 42.208 -29.187 14.220  1.00 37.12 ?  102 LYS   B CA   1 
ATOM   5436 C  C    . LYS   B 1 102 ? 40.819 -29.133 14.846  1.00 36.68 ?  102 LYS   B C    1 
ATOM   5437 O  O    . LYS   B 1 102 ? 40.584 -28.313 15.737  1.00 37.43 ?  102 LYS   B O    1 
ATOM   5438 C  CB   . LYS   B 1 102 ? 42.658 -27.764 13.890  1.00 40.64 ?  102 LYS   B CB   1 
ATOM   5439 C  CG   . LYS   B 1 102 ? 44.121 -27.615 13.516  1.00 43.86 ?  102 LYS   B CG   1 
ATOM   5440 C  CD   . LYS   B 1 102 ? 44.384 -26.198 13.032  1.00 46.89 ?  102 LYS   B CD   1 
ATOM   5441 C  CE   . LYS   B 1 102 ? 45.861 -25.916 12.834  1.00 49.14 ?  102 LYS   B CE   1 
ATOM   5442 N  NZ   . LYS   B 1 102 ? 46.077 -24.518 12.358  1.00 50.38 ?  102 LYS   B NZ   1 
ATOM   5443 H  H    . LYS   B 1 102 ? 41.896 -29.630 12.337  1.00 41.14 ?  102 LYS   B H    1 
ATOM   5444 H  HA   . LYS   B 1 102 ? 42.827 -29.551 14.871  1.00 44.55 ?  102 LYS   B HA   1 
ATOM   5445 H  HB2  . LYS   B 1 102 ? 42.132 -27.440 13.143  1.00 48.78 ?  102 LYS   B HB2  1 
ATOM   5446 H  HB3  . LYS   B 1 102 ? 42.498 -27.204 14.666  1.00 48.78 ?  102 LYS   B HB3  1 
ATOM   5447 H  HG2  . LYS   B 1 102 ? 44.677 -27.784 14.294  1.00 52.64 ?  102 LYS   B HG2  1 
ATOM   5448 H  HG3  . LYS   B 1 102 ? 44.340 -28.232 12.800  1.00 52.64 ?  102 LYS   B HG3  1 
ATOM   5449 H  HD2  . LYS   B 1 102 ? 43.935 -26.066 12.182  1.00 56.28 ?  102 LYS   B HD2  1 
ATOM   5450 H  HD3  . LYS   B 1 102 ? 44.042 -25.571 13.689  1.00 56.28 ?  102 LYS   B HD3  1 
ATOM   5451 H  HE2  . LYS   B 1 102 ? 46.325 -26.026 13.679  1.00 58.98 ?  102 LYS   B HE2  1 
ATOM   5452 H  HE3  . LYS   B 1 102 ? 46.219 -26.525 12.170  1.00 58.98 ?  102 LYS   B HE3  1 
ATOM   5453 H  HZ1  . LYS   B 1 102 ? 46.946 -24.365 12.246  1.00 60.47 ?  102 LYS   B HZ1  1 
ATOM   5454 H  HZ2  . LYS   B 1 102 ? 45.659 -24.394 11.582  1.00 60.47 ?  102 LYS   B HZ2  1 
ATOM   5455 H  HZ3  . LYS   B 1 102 ? 45.755 -23.941 12.954  1.00 60.47 ?  102 LYS   B HZ3  1 
ATOM   5456 N  N    . GLY   B 1 103 ? 39.889 -29.965 14.381  1.00 36.18 ?  103 GLY   B N    1 
ATOM   5457 C  CA   . GLY   B 1 103 ? 38.561 -30.026 14.957  1.00 35.74 ?  103 GLY   B CA   1 
ATOM   5458 C  C    . GLY   B 1 103 ? 37.606 -28.945 14.504  1.00 34.85 ?  103 GLY   B C    1 
ATOM   5459 O  O    . GLY   B 1 103 ? 36.515 -28.830 15.073  1.00 35.12 ?  103 GLY   B O    1 
ATOM   5460 H  H    . GLY   B 1 103 ? 40.007 -30.502 13.722  1.00 43.43 ?  103 GLY   B H    1 
ATOM   5461 H  HA2  . GLY   B 1 103 ? 38.163 -30.883 14.739  1.00 42.89 ?  103 GLY   B HA2  1 
ATOM   5462 H  HA3  . GLY   B 1 103 ? 38.634 -29.968 15.924  1.00 42.89 ?  103 GLY   B HA3  1 
ATOM   5463 N  N    A GLU   B 1 104 ? 37.981 -28.146 13.508  0.64 33.95 ?  104 GLU   B N    1 
ATOM   5464 N  N    B GLU   B 1 104 ? 37.965 -28.164 13.491  0.36 34.11 ?  104 GLU   B N    1 
ATOM   5465 C  CA   A GLU   B 1 104 ? 37.136 -27.048 13.069  0.64 32.86 ?  104 GLU   B CA   1 
ATOM   5466 C  CA   B GLU   B 1 104 ? 37.102 -27.087 13.034  0.36 33.15 ?  104 GLU   B CA   1 
ATOM   5467 C  C    A GLU   B 1 104 ? 35.944 -27.573 12.268  0.64 32.91 ?  104 GLU   B C    1 
ATOM   5468 C  C    B GLU   B 1 104 ? 35.934 -27.639 12.217  0.36 33.19 ?  104 GLU   B C    1 
ATOM   5469 O  O    A GLU   B 1 104 ? 35.973 -28.667 11.697  0.64 33.44 ?  104 GLU   B O    1 
ATOM   5470 O  O    B GLU   B 1 104 ? 35.998 -28.731 11.644  0.36 33.43 ?  104 GLU   B O    1 
ATOM   5471 C  CB   A GLU   B 1 104 ? 37.956 -26.043 12.256  0.64 31.93 ?  104 GLU   B CB   1 
ATOM   5472 C  CB   B GLU   B 1 104 ? 37.910 -26.067 12.232  0.36 32.22 ?  104 GLU   B CB   1 
ATOM   5473 C  CG   A GLU   B 1 104 ? 39.062 -25.389 13.079  0.64 30.82 ?  104 GLU   B CG   1 
ATOM   5474 C  CG   B GLU   B 1 104 ? 39.012 -25.417 13.060  0.36 31.33 ?  104 GLU   B CG   1 
ATOM   5475 C  CD   A GLU   B 1 104 ? 39.985 -24.501 12.271  0.64 29.57 ?  104 GLU   B CD   1 
ATOM   5476 C  CD   B GLU   B 1 104 ? 39.943 -24.543 12.245  0.36 30.51 ?  104 GLU   B CD   1 
ATOM   5477 O  OE1  A GLU   B 1 104 ? 39.966 -24.571 11.024  0.64 27.83 ?  104 GLU   B OE1  1 
ATOM   5478 O  OE1  B GLU   B 1 104 ? 39.870 -24.580 10.999  0.36 29.72 ?  104 GLU   B OE1  1 
ATOM   5479 O  OE2  A GLU   B 1 104 ? 40.742 -23.731 12.896  0.64 29.28 -1 104 GLU   B OE2  1 
ATOM   5480 O  OE2  B GLU   B 1 104 ? 40.752 -23.817 12.859  0.36 30.26 -1 104 GLU   B OE2  1 
ATOM   5481 H  H    A GLU   B 1 104 ? 38.720 -28.218 13.075  0.64 40.75 ?  104 GLU   B H    1 
ATOM   5482 H  H    B GLU   B 1 104 ? 38.704 -28.235 13.056  0.36 40.94 ?  104 GLU   B H    1 
ATOM   5483 H  HA   A GLU   B 1 104 ? 36.792 -26.586 13.849  0.64 39.44 ?  104 GLU   B HA   1 
ATOM   5484 H  HA   B GLU   B 1 104 ? 36.735 -26.632 13.806  0.36 39.78 ?  104 GLU   B HA   1 
ATOM   5485 H  HB2  A GLU   B 1 104 ? 38.368 -26.500 11.508  0.64 38.32 ?  104 GLU   B HB2  1 
ATOM   5486 H  HB2  B GLU   B 1 104 ? 38.324 -26.511 11.476  0.36 38.68 ?  104 GLU   B HB2  1 
ATOM   5487 H  HB3  A GLU   B 1 104 ? 37.368 -25.341 11.933  0.64 38.32 ?  104 GLU   B HB3  1 
ATOM   5488 H  HB3  B GLU   B 1 104 ? 37.316 -25.365 11.921  0.36 38.68 ?  104 GLU   B HB3  1 
ATOM   5489 H  HG2  A GLU   B 1 104 ? 38.659 -24.842 13.771  0.64 37.00 ?  104 GLU   B HG2  1 
ATOM   5490 H  HG2  B GLU   B 1 104 ? 38.605 -24.863 13.745  0.36 37.61 ?  104 GLU   B HG2  1 
ATOM   5491 H  HG3  A GLU   B 1 104 ? 39.608 -26.080 13.482  0.64 37.00 ?  104 GLU   B HG3  1 
ATOM   5492 H  HG3  B GLU   B 1 104 ? 39.546 -26.113 13.475  0.36 37.61 ?  104 GLU   B HG3  1 
ATOM   5493 N  N    A ASP   B 1 105 ? 34.882 -26.771 12.240  0.64 32.00 ?  105 ASP   B N    1 
ATOM   5494 N  N    B ASP   B 1 105 ? 34.853 -26.862 12.175  0.36 32.58 ?  105 ASP   B N    1 
ATOM   5495 C  CA   A ASP   B 1 105 ? 33.606 -27.216 11.693  0.64 32.09 ?  105 ASP   B CA   1 
ATOM   5496 C  CA   B ASP   B 1 105 ? 33.589 -27.322 11.612  0.36 32.52 ?  105 ASP   B CA   1 
ATOM   5497 C  C    A ASP   B 1 105 ? 33.670 -27.270 10.170  0.64 29.81 ?  105 ASP   B C    1 
ATOM   5498 C  C    B ASP   B 1 105 ? 33.670 -27.339 10.089  0.36 31.17 ?  105 ASP   B C    1 
ATOM   5499 O  O    A ASP   B 1 105 ? 33.856 -26.242 9.511   0.64 28.95 ?  105 ASP   B O    1 
ATOM   5500 O  O    B ASP   B 1 105 ? 33.872 -26.296 9.458   0.36 30.74 ?  105 ASP   B O    1 
ATOM   5501 C  CB   A ASP   B 1 105 ? 32.497 -26.268 12.143  0.64 35.00 ?  105 ASP   B CB   1 
ATOM   5502 C  CB   B ASP   B 1 105 ? 32.453 -26.413 12.077  0.36 33.81 ?  105 ASP   B CB   1 
ATOM   5503 C  CG   A ASP   B 1 105 ? 31.121 -26.731 11.712  0.64 37.63 ?  105 ASP   B CG   1 
ATOM   5504 C  CG   B ASP   B 1 105 ? 31.084 -26.964 11.725  0.36 35.08 ?  105 ASP   B CG   1 
ATOM   5505 O  OD1  A ASP   B 1 105 ? 31.009 -27.846 11.161  0.64 38.03 ?  105 ASP   B OD1  1 
ATOM   5506 O  OD1  B ASP   B 1 105 ? 31.017 -28.004 11.037  0.36 35.37 ?  105 ASP   B OD1  1 
ATOM   5507 O  OD2  A ASP   B 1 105 ? 30.149 -25.973 11.918  0.64 38.96 -1 105 ASP   B OD2  1 
ATOM   5508 O  OD2  B ASP   B 1 105 ? 30.072 -26.361 12.142  0.36 35.52 -1 105 ASP   B OD2  1 
ATOM   5509 H  H    A ASP   B 1 105 ? 34.876 -25.962 12.534  0.64 38.41 ?  105 ASP   B H    1 
ATOM   5510 H  H    B ASP   B 1 105 ? 34.828 -26.055 12.467  0.36 39.11 ?  105 ASP   B H    1 
ATOM   5511 H  HA   A ASP   B 1 105 ? 33.405 -28.105 12.025  0.64 38.52 ?  105 ASP   B HA   1 
ATOM   5512 H  HA   B ASP   B 1 105 ? 33.403 -28.223 11.918  0.36 39.03 ?  105 ASP   B HA   1 
ATOM   5513 H  HB2  A ASP   B 1 105 ? 32.517 -26.195 13.112  0.64 42.01 ?  105 ASP   B HB2  1 
ATOM   5514 H  HB2  B ASP   B 1 105 ? 32.500 -26.315 13.042  0.36 40.58 ?  105 ASP   B HB2  1 
ATOM   5515 H  HB3  A ASP   B 1 105 ? 32.641 -25.399 11.742  0.64 42.01 ?  105 ASP   B HB3  1 
ATOM   5516 H  HB3  B ASP   B 1 105 ? 32.545 -25.545 11.652  0.36 40.58 ?  105 ASP   B HB3  1 
ATOM   5517 N  N    A ILE   B 1 106 ? 33.484 -28.471 9.615   0.64 29.03 ?  106 ILE   B N    1 
ATOM   5518 N  N    B ILE   B 1 106 ? 33.497 -28.527 9.503   0.36 30.27 ?  106 ILE   B N    1 
ATOM   5519 C  CA   A ILE   B 1 106 ? 33.479 -28.654 8.169   0.64 28.34 ?  106 ILE   B CA   1 
ATOM   5520 C  CA   B ILE   B 1 106 ? 33.502 -28.676 8.053   0.36 29.53 ?  106 ILE   B CA   1 
ATOM   5521 C  C    A ILE   B 1 106 ? 32.390 -27.830 7.495   0.64 27.12 ?  106 ILE   B C    1 
ATOM   5522 C  C    B ILE   B 1 106 ? 32.401 -27.853 7.397   0.36 28.48 ?  106 ILE   B C    1 
ATOM   5523 O  O    A ILE   B 1 106 ? 32.490 -27.530 6.300   0.64 26.31 ?  106 ILE   B O    1 
ATOM   5524 O  O    B ILE   B 1 106 ? 32.486 -27.545 6.203   0.36 28.09 ?  106 ILE   B O    1 
ATOM   5525 C  CB   A ILE   B 1 106 ? 33.360 -30.160 7.837   0.64 29.18 ?  106 ILE   B CB   1 
ATOM   5526 C  CB   B ILE   B 1 106 ? 33.403 -30.177 7.689   0.36 29.92 ?  106 ILE   B CB   1 
ATOM   5527 C  CG1  A ILE   B 1 106 ? 33.611 -30.420 6.351   0.64 29.50 ?  106 ILE   B CG1  1 
ATOM   5528 C  CG1  B ILE   B 1 106 ? 33.670 -30.400 6.198   0.36 30.03 ?  106 ILE   B CG1  1 
ATOM   5529 C  CG2  A ILE   B 1 106 ? 31.993 -30.695 8.250   0.64 29.70 ?  106 ILE   B CG2  1 
ATOM   5530 C  CG2  B ILE   B 1 106 ? 32.038 -30.733 8.072   0.36 30.25 ?  106 ILE   B CG2  1 
ATOM   5531 C  CD1  A ILE   B 1 106 ? 34.977 -29.986 5.883   0.64 29.42 ?  106 ILE   B CD1  1 
ATOM   5532 C  CD1  B ILE   B 1 106 ? 35.026 -29.916 5.747   0.36 30.06 ?  106 ILE   B CD1  1 
ATOM   5533 H  H    A ILE   B 1 106 ? 33.358 -29.194 10.061  0.64 34.85 ?  106 ILE   B H    1 
ATOM   5534 H  H    B ILE   B 1 106 ? 33.381 -29.262 9.930   0.36 36.33 ?  106 ILE   B H    1 
ATOM   5535 H  HA   A ILE   B 1 106 ? 34.326 -28.342 7.827   0.64 34.02 ?  106 ILE   B HA   1 
ATOM   5536 H  HA   B ILE   B 1 106 ? 34.344 -28.344 7.717   0.36 35.45 ?  106 ILE   B HA   1 
ATOM   5537 H  HB   A ILE   B 1 106 ? 34.032 -30.634 8.346   0.64 35.03 ?  106 ILE   B HB   1 
ATOM   5538 H  HB   B ILE   B 1 106 ? 34.077 -30.657 8.193   0.36 35.92 ?  106 ILE   B HB   1 
ATOM   5539 H  HG12 A ILE   B 1 106 ? 33.534 -31.374 6.185   0.64 35.40 ?  106 ILE   B HG12 1 
ATOM   5540 H  HG12 B ILE   B 1 106 ? 33.620 -31.353 6.011   0.36 36.05 ?  106 ILE   B HG12 1 
ATOM   5541 H  HG13 A ILE   B 1 106 ? 32.951 -29.943 5.828   0.64 35.40 ?  106 ILE   B HG13 1 
ATOM   5542 H  HG13 B ILE   B 1 106 ? 32.998 -29.931 5.682   0.36 36.05 ?  106 ILE   B HG13 1 
ATOM   5543 H  HG21 A ILE   B 1 106 ? 31.995 -31.661 8.163   0.64 35.64 ?  106 ILE   B HG21 1 
ATOM   5544 H  HG21 B ILE   B 1 106 ? 32.058 -31.700 7.991   0.36 36.31 ?  106 ILE   B HG21 1 
ATOM   5545 H  HG22 A ILE   B 1 106 ? 31.823 -30.448 9.173   0.64 35.64 ?  106 ILE   B HG22 1 
ATOM   5546 H  HG22 B ILE   B 1 106 ? 31.841 -30.483 8.988   0.36 36.31 ?  106 ILE   B HG22 1 
ATOM   5547 H  HG23 A ILE   B 1 106 ? 31.313 -30.312 7.675   0.64 35.64 ?  106 ILE   B HG23 1 
ATOM   5548 H  HG23 B ILE   B 1 106 ? 31.366 -30.367 7.477   0.36 36.31 ?  106 ILE   B HG23 1 
ATOM   5549 H  HD11 A ILE   B 1 106 ? 35.160 -30.393 5.023   0.64 35.31 ?  106 ILE   B HD11 1 
ATOM   5550 H  HD11 B ILE   B 1 106 ? 35.231 -30.313 4.888   0.36 36.08 ?  106 ILE   B HD11 1 
ATOM   5551 H  HD12 A ILE   B 1 106 ? 34.991 -29.019 5.801   0.64 35.31 ?  106 ILE   B HD12 1 
ATOM   5552 H  HD12 B ILE   B 1 106 ? 35.005 -28.949 5.668   0.36 36.08 ?  106 ILE   B HD12 1 
ATOM   5553 H  HD13 A ILE   B 1 106 ? 35.640 -30.273 6.532   0.64 35.31 ?  106 ILE   B HD13 1 
ATOM   5554 H  HD13 B ILE   B 1 106 ? 35.690 -30.182 6.402   0.36 36.08 ?  106 ILE   B HD13 1 
ATOM   5555 N  N    A GLN   B 1 107 ? 31.353 -27.432 8.238   0.64 27.23 ?  107 GLN   B N    1 
ATOM   5556 N  N    B GLN   B 1 107 ? 31.364 -27.482 8.152   0.36 28.14 ?  107 GLN   B N    1 
ATOM   5557 C  CA   A GLN   B 1 107 ? 30.270 -26.656 7.646   0.64 27.44 ?  107 GLN   B CA   1 
ATOM   5558 C  CA   B GLN   B 1 107 ? 30.280 -26.679 7.597   0.36 27.86 ?  107 GLN   B CA   1 
ATOM   5559 C  C    A GLN   B 1 107 ? 30.752 -25.308 7.133   0.64 24.90 ?  107 GLN   B C    1 
ATOM   5560 C  C    B GLN   B 1 107 ? 30.752 -25.308 7.124   0.36 25.32 ?  107 GLN   B C    1 
ATOM   5561 O  O    A GLN   B 1 107 ? 30.100 -24.722 6.264   0.64 25.33 ?  107 GLN   B O    1 
ATOM   5562 O  O    B GLN   B 1 107 ? 30.087 -24.697 6.281   0.36 25.57 ?  107 GLN   B O    1 
ATOM   5563 C  CB   A GLN   B 1 107 ? 29.149 -26.457 8.669   0.64 31.12 ?  107 GLN   B CB   1 
ATOM   5564 C  CB   B GLN   B 1 107 ? 29.163 -26.532 8.635   0.36 30.52 ?  107 GLN   B CB   1 
ATOM   5565 C  CG   A GLN   B 1 107 ? 27.824 -25.957 8.095   0.64 34.51 ?  107 GLN   B CG   1 
ATOM   5566 C  CG   B GLN   B 1 107 ? 27.834 -26.030 8.078   0.36 32.92 ?  107 GLN   B CG   1 
ATOM   5567 C  CD   A GLN   B 1 107 ? 27.758 -24.444 7.980   0.64 37.12 ?  107 GLN   B CD   1 
ATOM   5568 C  CD   B GLN   B 1 107 ? 27.727 -24.516 8.078   0.36 34.80 ?  107 GLN   B CD   1 
ATOM   5569 O  OE1  A GLN   B 1 107 ? 28.588 -23.728 8.542   0.64 38.11 ?  107 GLN   B OE1  1 
ATOM   5570 O  OE1  B GLN   B 1 107 ? 28.549 -23.821 8.678   0.36 35.44 ?  107 GLN   B OE1  1 
ATOM   5571 N  NE2  A GLN   B 1 107 ? 26.761 -23.950 7.250   0.64 37.97 ?  107 GLN   B NE2  1 
ATOM   5572 N  NE2  B GLN   B 1 107 ? 26.705 -23.996 7.405   0.36 35.45 ?  107 GLN   B NE2  1 
ATOM   5573 H  H    A GLN   B 1 107 ? 31.267 -27.570 9.078   0.64 32.68 ?  107 GLN   B H    1 
ATOM   5574 H  H    B GLN   B 1 107 ? 31.263 -27.691 8.978   0.36 33.77 ?  107 GLN   B H    1 
ATOM   5575 H  HA   A GLN   B 1 107 ? 29.905 -27.147 6.894   0.64 32.94 ?  107 GLN   B HA   1 
ATOM   5576 H  HA   B GLN   B 1 107 ? 29.908 -27.144 6.832   0.36 33.45 ?  107 GLN   B HA   1 
ATOM   5577 H  HB2  A GLN   B 1 107 ? 28.976 -27.306 9.095   0.64 37.35 ?  107 GLN   B HB2  1 
ATOM   5578 H  HB2  B GLN   B 1 107 ? 28.999 -27.398 9.035   0.36 36.63 ?  107 GLN   B HB2  1 
ATOM   5579 H  HB3  A GLN   B 1 107 ? 29.443 -25.811 9.329   0.64 37.35 ?  107 GLN   B HB3  1 
ATOM   5580 H  HB3  B GLN   B 1 107 ? 29.453 -25.908 9.318   0.36 36.63 ?  107 GLN   B HB3  1 
ATOM   5581 H  HG2  A GLN   B 1 107 ? 27.700 -26.326 7.208   0.64 41.43 ?  107 GLN   B HG2  1 
ATOM   5582 H  HG2  B GLN   B 1 107 ? 27.737 -26.335 7.163   0.36 39.51 ?  107 GLN   B HG2  1 
ATOM   5583 H  HG3  A GLN   B 1 107 ? 27.100 -26.247 8.676   0.64 41.43 ?  107 GLN   B HG3  1 
ATOM   5584 H  HG3  B GLN   B 1 107 ? 27.110 -26.384 8.622   0.36 39.51 ?  107 GLN   B HG3  1 
ATOM   5585 H  HE21 A GLN   B 1 107 ? 26.200 -24.482 6.871   0.64 45.57 ?  107 GLN   B HE21 1 
ATOM   5586 H  HE21 B GLN   B 1 107 ? 26.151 -24.512 6.997   0.36 42.55 ?  107 GLN   B HE21 1 
ATOM   5587 H  HE22 A GLN   B 1 107 ? 26.676 -23.099 7.157   0.64 45.57 ?  107 GLN   B HE22 1 
ATOM   5588 H  HE22 B GLN   B 1 107 ? 26.598 -23.143 7.377   0.36 42.55 ?  107 GLN   B HE22 1 
ATOM   5589 N  N    . LEU   B 1 108 ? 31.882 -24.811 7.637   1.00 22.95 ?  108 LEU   B N    1 
ATOM   5590 C  CA   . LEU   B 1 108 ? 32.414 -23.513 7.225   1.00 20.00 ?  108 LEU   B CA   1 
ATOM   5591 C  C    . LEU   B 1 108 ? 33.062 -23.539 5.852   1.00 17.35 ?  108 LEU   B C    1 
ATOM   5592 O  O    . LEU   B 1 108 ? 33.492 -22.483 5.364   1.00 16.27 ?  108 LEU   B O    1 
ATOM   5593 C  CB   . LEU   B 1 108 ? 33.407 -23.007 8.269   1.00 20.56 ?  108 LEU   B CB   1 
ATOM   5594 C  CG   . LEU   B 1 108 ? 32.771 -22.516 9.568   1.00 21.89 ?  108 LEU   B CG   1 
ATOM   5595 C  CD1  . LEU   B 1 108 ? 33.792 -22.501 10.687  1.00 22.23 ?  108 LEU   B CD1  1 
ATOM   5596 C  CD2  . LEU   B 1 108 ? 32.183 -21.125 9.372   1.00 22.72 ?  108 LEU   B CD2  1 
ATOM   5597 H  H    A LEU   B 1 108 ? 32.351 -25.208 8.234   0.64 27.55 ?  108 LEU   B H    1 
ATOM   5598 H  H    B LEU   B 1 108 ? 32.353 -25.208 8.233   0.36 27.55 ?  108 LEU   B H    1 
ATOM   5599 H  HA   . LEU   B 1 108 ? 31.681 -22.881 7.188   1.00 24.01 ?  108 LEU   B HA   1 
ATOM   5600 H  HB2  . LEU   B 1 108 ? 34.009 -23.729 8.499   1.00 24.68 ?  108 LEU   B HB2  1 
ATOM   5601 H  HB3  . LEU   B 1 108 ? 33.903 -22.268 7.892   1.00 24.68 ?  108 LEU   B HB3  1 
ATOM   5602 H  HG   . LEU   B 1 108 ? 32.047 -23.113 9.825   1.00 26.28 ?  108 LEU   B HG   1 
ATOM   5603 H  HD11 . LEU   B 1 108 ? 33.358 -22.224 11.510  1.00 26.69 ?  108 LEU   B HD11 1 
ATOM   5604 H  HD12 . LEU   B 1 108 ? 34.158 -23.392 10.790  1.00 26.69 ?  108 LEU   B HD12 1 
ATOM   5605 H  HD13 . LEU   B 1 108 ? 34.497 -21.876 10.459  1.00 26.69 ?  108 LEU   B HD13 1 
ATOM   5606 H  HD21 . LEU   B 1 108 ? 31.805 -20.817 10.213  1.00 27.27 ?  108 LEU   B HD21 1 
ATOM   5607 H  HD22 . LEU   B 1 108 ? 32.887 -20.522 9.088   1.00 27.27 ?  108 LEU   B HD22 1 
ATOM   5608 H  HD23 . LEU   B 1 108 ? 31.488 -21.165 8.696   1.00 27.27 ?  108 LEU   B HD23 1 
ATOM   5609 N  N    . LEU   B 1 109 ? 33.126 -24.709 5.223   1.00 16.18 ?  109 LEU   B N    1 
ATOM   5610 C  CA   . LEU   B 1 109 ? 33.749 -24.823 3.912   1.00 14.88 ?  109 LEU   B CA   1 
ATOM   5611 C  C    . LEU   B 1 109 ? 32.981 -24.043 2.853   1.00 14.19 ?  109 LEU   B C    1 
ATOM   5612 O  O    . LEU   B 1 109 ? 33.593 -23.452 1.955   1.00 14.04 ?  109 LEU   B O    1 
ATOM   5613 C  CB   . LEU   B 1 109 ? 33.857 -26.301 3.536   1.00 14.99 ?  109 LEU   B CB   1 
ATOM   5614 C  CG   . LEU   B 1 109 ? 34.638 -26.648 2.274   1.00 14.94 ?  109 LEU   B CG   1 
ATOM   5615 C  CD1  . LEU   B 1 109 ? 36.012 -25.988 2.275   1.00 14.77 ?  109 LEU   B CD1  1 
ATOM   5616 C  CD2  . LEU   B 1 109 ? 34.775 -28.160 2.163   1.00 15.82 ?  109 LEU   B CD2  1 
ATOM   5617 H  H    . LEU   B 1 109 ? 32.836 -25.451 5.536   1.00 19.42 ?  109 LEU   B H    1 
ATOM   5618 H  HA   . LEU   B 1 109 ? 34.649 -24.460 3.952   1.00 17.86 ?  109 LEU   B HA   1 
ATOM   5619 H  HB2  . LEU   B 1 109 ? 34.287 -26.770 4.265   1.00 18.00 ?  109 LEU   B HB2  1 
ATOM   5620 H  HB3  . LEU   B 1 109 ? 32.961 -26.650 3.415   1.00 18.00 ?  109 LEU   B HB3  1 
ATOM   5621 H  HG   . LEU   B 1 109 ? 34.149 -26.345 1.489   1.00 17.94 ?  109 LEU   B HG   1 
ATOM   5622 H  HD11 . LEU   B 1 109 ? 36.546 -26.367 1.557   1.00 17.73 ?  109 LEU   B HD11 1 
ATOM   5623 H  HD12 . LEU   B 1 109 ? 35.901 -25.039 2.141   1.00 17.73 ?  109 LEU   B HD12 1 
ATOM   5624 H  HD13 . LEU   B 1 109 ? 36.439 -26.162 3.128   1.00 17.73 ?  109 LEU   B HD13 1 
ATOM   5625 H  HD21 . LEU   B 1 109 ? 35.338 -28.376 1.400   1.00 19.00 ?  109 LEU   B HD21 1 
ATOM   5626 H  HD22 . LEU   B 1 109 ? 35.181 -28.501 2.975   1.00 19.00 ?  109 LEU   B HD22 1 
ATOM   5627 H  HD23 . LEU   B 1 109 ? 33.896 -28.555 2.043   1.00 19.00 ?  109 LEU   B HD23 1 
ATOM   5628 N  N    . LYS   B 1 110 ? 31.648 -24.006 2.938   1.00 14.06 ?  110 LYS   B N    1 
ATOM   5629 C  CA   . LYS   B 1 110 ? 30.895 -23.248 1.945   1.00 14.06 ?  110 LYS   B CA   1 
ATOM   5630 C  C    . LYS   B 1 110 ? 31.228 -21.758 2.033   1.00 13.43 ?  110 LYS   B C    1 
ATOM   5631 O  O    . LYS   B 1 110 ? 31.485 -21.107 1.013   1.00 13.35 ?  110 LYS   B O    1 
ATOM   5632 C  CB   . LYS   B 1 110 ? 29.391 -23.501 2.092   1.00 14.59 ?  110 LYS   B CB   1 
ATOM   5633 C  CG   . LYS   B 1 110 ? 28.578 -22.889 0.952   1.00 15.05 ?  110 LYS   B CG   1 
ATOM   5634 C  CD   . LYS   B 1 110 ? 27.111 -23.308 0.998   1.00 15.52 ?  110 LYS   B CD   1 
ATOM   5635 C  CE   . LYS   B 1 110 ? 26.343 -22.767 -0.202  1.00 16.13 ?  110 LYS   B CE   1 
ATOM   5636 N  NZ   . LYS   B 1 110 ? 26.674 -23.473 -1.470  1.00 16.50 ?  110 LYS   B NZ   1 
ATOM   5637 H  H    . LYS   B 1 110 ? 31.179 -24.400 3.535   1.00 16.88 ?  110 LYS   B H    1 
ATOM   5638 H  HA   . LYS   B 1 110 ? 31.155 -23.550 1.060   1.00 16.88 ?  110 LYS   B HA   1 
ATOM   5639 H  HB2  . LYS   B 1 110 ? 29.231 -24.461 2.093   1.00 17.52 ?  110 LYS   B HB2  1 
ATOM   5640 H  HB3  . LYS   B 1 110 ? 29.082 -23.114 2.924   1.00 17.52 ?  110 LYS   B HB3  1 
ATOM   5641 H  HG2  . LYS   B 1 110 ? 28.612 -21.924 1.018   1.00 18.07 ?  110 LYS   B HG2  1 
ATOM   5642 H  HG3  . LYS   B 1 110 ? 28.944 -23.182 0.104   1.00 18.07 ?  110 LYS   B HG3  1 
ATOM   5643 H  HD2  . LYS   B 1 110 ? 27.052 -24.280 0.984   1.00 18.63 ?  110 LYS   B HD2  1 
ATOM   5644 H  HD3  . LYS   B 1 110 ? 26.700 -22.963 1.807   1.00 18.63 ?  110 LYS   B HD3  1 
ATOM   5645 H  HE2  . LYS   B 1 110 ? 25.391 -22.867 -0.043  1.00 19.37 ?  110 LYS   B HE2  1 
ATOM   5646 H  HE3  . LYS   B 1 110 ? 26.562 -21.827 -0.316  1.00 19.37 ?  110 LYS   B HE3  1 
ATOM   5647 H  HZ1  . LYS   B 1 110 ? 26.211 -23.126 -2.142  1.00 19.81 ?  110 LYS   B HZ1  1 
ATOM   5648 H  HZ2  . LYS   B 1 110 ? 27.546 -23.389 -1.642  1.00 19.81 ?  110 LYS   B HZ2  1 
ATOM   5649 H  HZ3  . LYS   B 1 110 ? 26.479 -24.337 -1.393  1.00 19.81 ?  110 LYS   B HZ3  1 
ATOM   5650 N  N    . SER   B 1 111 ? 31.245 -21.208 3.252   1.00 14.00 ?  111 SER   B N    1 
ATOM   5651 C  CA   . SER   B 1 111 ? 31.641 -19.814 3.432   1.00 13.94 ?  111 SER   B CA   1 
ATOM   5652 C  C    . SER   B 1 111 ? 33.018 -19.557 2.834   1.00 13.27 ?  111 SER   B C    1 
ATOM   5653 O  O    . SER   B 1 111 ? 33.244 -18.523 2.187   1.00 13.38 ?  111 SER   B O    1 
ATOM   5654 C  CB   . SER   B 1 111 ? 31.652 -19.463 4.917   1.00 15.03 ?  111 SER   B CB   1 
ATOM   5655 O  OG   . SER   B 1 111 ? 30.349 -19.445 5.458   1.00 16.36 ?  111 SER   B OG   1 
ATOM   5656 H  H    . SER   B 1 111 ? 31.043 -21.624 3.978   1.00 16.81 ?  111 SER   B H    1 
ATOM   5657 H  HA   . SER   B 1 111 ? 31.004 -19.241 2.987   1.00 16.74 ?  111 SER   B HA   1 
ATOM   5658 H  HB2  . SER   B 1 111 ? 32.168 -20.130 5.397   1.00 18.04 ?  111 SER   B HB2  1 
ATOM   5659 H  HB3  . SER   B 1 111 ? 32.051 -18.590 5.033   1.00 18.04 ?  111 SER   B HB3  1 
ATOM   5660 H  HG   . SER   B 1 111 ? 30.375 -19.240 6.280   1.00 19.65 ?  111 SER   B HG   1 
ATOM   5661 N  N    . ALA   B 1 112 ? 33.957 -20.477 3.055   1.00 13.38 ?  112 ALA   B N    1 
ATOM   5662 C  CA   . ALA   B 1 112 ? 35.302 -20.305 2.516   1.00 12.96 ?  112 ALA   B CA   1 
ATOM   5663 C  C    . ALA   B 1 112 ? 35.274 -20.214 0.993   1.00 12.47 ?  112 ALA   B C    1 
ATOM   5664 O  O    . ALA   B 1 112 ? 35.895 -19.324 0.398   1.00 12.89 ?  112 ALA   B O    1 
ATOM   5665 C  CB   . ALA   B 1 112 ? 36.205 -21.446 2.995   1.00 13.17 ?  112 ALA   B CB   1 
ATOM   5666 H  H    . ALA   B 1 112 ? 33.842 -21.201 3.515   1.00 16.07 ?  112 ALA   B H    1 
ATOM   5667 H  HA   . ALA   B 1 112 ? 35.666 -19.474 2.857   1.00 15.56 ?  112 ALA   B HA   1 
ATOM   5668 H  HB1  . ALA   B 1 112 ? 37.095 -21.310 2.631   1.00 15.82 ?  112 ALA   B HB1  1 
ATOM   5669 H  HB2  . ALA   B 1 112 ? 36.242 -21.430 3.966   1.00 15.82 ?  112 ALA   B HB2  1 
ATOM   5670 H  HB3  . ALA   B 1 112 ? 35.842 -22.286 2.689   1.00 15.82 ?  112 ALA   B HB3  1 
ATOM   5671 N  N    . TYR   B 1 113 ? 34.541 -21.121 0.340   1.00 12.56 ?  113 TYR   B N    1 
ATOM   5672 C  CA   . TYR   B 1 113 ? 34.465 -21.077 -1.115  1.00 12.12 ?  113 TYR   B CA   1 
ATOM   5673 C  C    . TYR   B 1 113 ? 33.757 -19.825 -1.631  1.00 11.82 ?  113 TYR   B C    1 
ATOM   5674 O  O    . TYR   B 1 113 ? 34.023 -19.396 -2.758  1.00 11.91 ?  113 TYR   B O    1 
ATOM   5675 C  CB   . TYR   B 1 113 ? 33.792 -22.335 -1.657  1.00 12.44 ?  113 TYR   B CB   1 
ATOM   5676 C  CG   . TYR   B 1 113 ? 34.756 -23.486 -1.908  1.00 12.71 ?  113 TYR   B CG   1 
ATOM   5677 C  CD1  . TYR   B 1 113 ? 35.758 -23.384 -2.865  1.00 13.21 ?  113 TYR   B CD1  1 
ATOM   5678 C  CD2  . TYR   B 1 113 ? 34.651 -24.675 -1.205  1.00 12.85 ?  113 TYR   B CD2  1 
ATOM   5679 C  CE1  . TYR   B 1 113 ? 36.633 -24.413 -3.104  1.00 13.33 ?  113 TYR   B CE1  1 
ATOM   5680 C  CE2  . TYR   B 1 113 ? 35.526 -25.725 -1.441  1.00 13.19 ?  113 TYR   B CE2  1 
ATOM   5681 C  CZ   . TYR   B 1 113 ? 36.509 -25.592 -2.398  1.00 13.34 ?  113 TYR   B CZ   1 
ATOM   5682 O  OH   . TYR   B 1 113 ? 37.392 -26.614 -2.663  1.00 14.13 ?  113 TYR   B OH   1 
ATOM   5683 H  H    . TYR   B 1 113 ? 34.079 -21.750 0.715   1.00 15.08 ?  113 TYR   B H    1 
ATOM   5684 H  HA   . TYR   B 1 113 ? 35.366 -21.066 -1.454  1.00 14.55 ?  113 TYR   B HA   1 
ATOM   5685 H  HB2  . TYR   B 1 113 ? 33.127 -22.648 -1.015  1.00 14.94 ?  113 TYR   B HB2  1 
ATOM   5686 H  HB3  . TYR   B 1 113 ? 33.355 -22.125 -2.496  1.00 14.94 ?  113 TYR   B HB3  1 
ATOM   5687 H  HD1  . TYR   B 1 113 ? 35.846 -22.591 -3.348  1.00 15.86 ?  113 TYR   B HD1  1 
ATOM   5688 H  HD2  . TYR   B 1 113 ? 33.977 -24.772 -0.570  1.00 15.42 ?  113 TYR   B HD2  1 
ATOM   5689 H  HE1  . TYR   B 1 113 ? 37.299 -24.325 -3.751  1.00 16.00 ?  113 TYR   B HE1  1 
ATOM   5690 H  HE2  . TYR   B 1 113 ? 35.434 -26.521 -0.969  1.00 15.84 ?  113 TYR   B HE2  1 
ATOM   5691 H  HH   . TYR   B 1 113 ? 37.210 -27.279 -2.183  1.00 16.96 ?  113 TYR   B HH   1 
ATOM   5692 N  N    . GLU   B 1 114 ? 32.835 -19.247 -0.853  1.00 12.05 ?  114 GLU   B N    1 
ATOM   5693 C  CA   . GLU   B 1 114 ? 32.148 -18.042 -1.313  1.00 12.03 ?  114 GLU   B CA   1 
ATOM   5694 C  C    . GLU   B 1 114 ? 33.131 -16.921 -1.616  1.00 11.85 ?  114 GLU   B C    1 
ATOM   5695 O  O    . GLU   B 1 114 ? 32.852 -16.062 -2.457  1.00 12.05 ?  114 GLU   B O    1 
ATOM   5696 C  CB   . GLU   B 1 114 ? 31.092 -17.606 -0.291  1.00 12.36 ?  114 GLU   B CB   1 
ATOM   5697 C  CG   . GLU   B 1 114 ? 29.870 -18.522 -0.357  1.00 12.53 ?  114 GLU   B CG   1 
ATOM   5698 C  CD   . GLU   B 1 114 ? 28.854 -18.337 0.754   1.00 12.69 ?  114 GLU   B CD   1 
ATOM   5699 O  OE1  . GLU   B 1 114 ? 29.143 -17.717 1.794   1.00 13.15 ?  114 GLU   B OE1  1 
ATOM   5700 O  OE2  . GLU   B 1 114 ? 27.735 -18.887 0.592   1.00 14.00 -1 114 GLU   B OE2  1 
ATOM   5701 H  H    . GLU   B 1 114 ? 32.587 -19.535 -0.078  1.00 14.47 ?  114 GLU   B H    1 
ATOM   5702 H  HA   . GLU   B 1 114 ? 31.687 -18.247 -2.136  1.00 14.45 ?  114 GLU   B HA   1 
ATOM   5703 H  HB2  . GLU   B 1 114 ? 31.468 -17.658 0.605   1.00 14.84 ?  114 GLU   B HB2  1 
ATOM   5704 H  HB3  . GLU   B 1 114 ? 30.810 -16.701 -0.486  1.00 14.84 ?  114 GLU   B HB3  1 
ATOM   5705 H  HG2  . GLU   B 1 114 ? 29.416 -18.361 -1.195  1.00 15.04 ?  114 GLU   B HG2  1 
ATOM   5706 H  HG3  . GLU   B 1 114 ? 30.176 -19.441 -0.320  1.00 15.04 ?  114 GLU   B HG3  1 
ATOM   5707 N  N    . ASN   B 1 115 ? 34.299 -16.920 -0.971  1.00 11.69 ?  115 ASN   B N    1 
ATOM   5708 C  CA   . ASN   B 1 115 ? 35.286 -15.887 -1.271  1.00 11.53 ?  115 ASN   B CA   1 
ATOM   5709 C  C    . ASN   B 1 115 ? 35.696 -15.913 -2.735  1.00 11.52 ?  115 ASN   B C    1 
ATOM   5710 O  O    . ASN   B 1 115 ? 36.088 -14.875 -3.292  1.00 12.11 ?  115 ASN   B O    1 
ATOM   5711 C  CB   . ASN   B 1 115 ? 36.524 -16.061 -0.387  1.00 12.21 ?  115 ASN   B CB   1 
ATOM   5712 C  CG   . ASN   B 1 115 ? 36.251 -15.792 1.071   1.00 12.43 ?  115 ASN   B CG   1 
ATOM   5713 O  OD1  . ASN   B 1 115 ? 36.254 -14.644 1.516   1.00 14.40 ?  115 ASN   B OD1  1 
ATOM   5714 N  ND2  . ASN   B 1 115 ? 36.076 -16.858 1.844   1.00 12.53 ?  115 ASN   B ND2  1 
ATOM   5715 H  H    . ASN   B 1 115 ? 34.541 -17.483 -0.362  1.00 14.04 ?  115 ASN   B H    1 
ATOM   5716 H  HA   . ASN   B 1 115 ? 34.910 -15.013 -1.081  1.00 13.85 ?  115 ASN   B HA   1 
ATOM   5717 H  HB2  . ASN   B 1 115 ? 36.850 -16.971 -0.469  1.00 14.66 ?  115 ASN   B HB2  1 
ATOM   5718 H  HB3  . ASN   B 1 115 ? 37.214 -15.439 -0.675  1.00 14.66 ?  115 ASN   B HB3  1 
ATOM   5719 H  HD21 . ASN   B 1 115 ? 35.923 -16.760 2.687   1.00 15.05 ?  115 ASN   B HD21 1 
ATOM   5720 H  HD22 . ASN   B 1 115 ? 36.094 -17.648 1.504   1.00 15.05 ?  115 ASN   B HD22 1 
ATOM   5721 N  N    . PHE   B 1 116 ? 35.666 -17.094 -3.363  1.00 11.36 ?  116 PHE   B N    1 
ATOM   5722 C  CA   . PHE   B 1 116 ? 36.101 -17.190 -4.751  1.00 11.66 ?  116 PHE   B CA   1 
ATOM   5723 C  C    . PHE   B 1 116 ? 35.197 -16.367 -5.667  1.00 11.24 ?  116 PHE   B C    1 
ATOM   5724 O  O    . PHE   B 1 116 ? 35.631 -15.935 -6.742  1.00 11.88 ?  116 PHE   B O    1 
ATOM   5725 C  CB   . PHE   B 1 116 ? 36.068 -18.636 -5.262  1.00 11.31 ?  116 PHE   B CB   1 
ATOM   5726 C  CG   . PHE   B 1 116 ? 37.137 -19.586 -4.711  1.00 11.16 ?  116 PHE   B CG   1 
ATOM   5727 C  CD1  . PHE   B 1 116 ? 37.782 -19.399 -3.498  1.00 12.08 ?  116 PHE   B CD1  1 
ATOM   5728 C  CD2  . PHE   B 1 116 ? 37.443 -20.724 -5.445  1.00 11.45 ?  116 PHE   B CD2  1 
ATOM   5729 C  CE1  . PHE   B 1 116 ? 38.717 -20.332 -3.043  1.00 11.98 ?  116 PHE   B CE1  1 
ATOM   5730 C  CE2  . PHE   B 1 116 ? 38.370 -21.656 -4.999  1.00 11.61 ?  116 PHE   B CE2  1 
ATOM   5731 C  CZ   . PHE   B 1 116 ? 39.003 -21.465 -3.801  1.00 11.67 ?  116 PHE   B CZ   1 
ATOM   5732 H  H    . PHE   B 1 116 ? 35.403 -17.837 -3.012  1.00 13.64 ?  116 PHE   B H    1 
ATOM   5733 H  HA   . PHE   B 1 116 ? 37.010 -16.859 -4.829  1.00 14.01 ?  116 PHE   B HA   1 
ATOM   5734 H  HB2  . PHE   B 1 116 ? 35.199 -19.014 -5.038  1.00 13.58 ?  116 PHE   B HB2  1 
ATOM   5735 H  HB3  . PHE   B 1 116 ? 36.164 -18.616 -6.227  1.00 13.58 ?  116 PHE   B HB3  1 
ATOM   5736 H  HD1  . PHE   B 1 116 ? 37.578 -18.649 -2.981  1.00 14.51 ?  116 PHE   B HD1  1 
ATOM   5737 H  HD2  . PHE   B 1 116 ? 37.008 -20.869 -6.257  1.00 13.75 ?  116 PHE   B HD2  1 
ATOM   5738 H  HE1  . PHE   B 1 116 ? 39.148 -20.196 -2.229  1.00 14.39 ?  116 PHE   B HE1  1 
ATOM   5739 H  HE2  . PHE   B 1 116 ? 38.563 -22.403 -5.515  1.00 13.94 ?  116 PHE   B HE2  1 
ATOM   5740 H  HZ   . PHE   B 1 116 ? 39.637 -22.076 -3.504  1.00 14.01 ?  116 PHE   B HZ   1 
ATOM   5741 N  N    . ASN   B 1 117 ? 33.931 -16.161 -5.278  1.00 11.67 ?  117 ASN   B N    1 
ATOM   5742 C  CA   . ASN   B 1 117 ? 32.983 -15.460 -6.141  1.00 12.03 ?  117 ASN   B CA   1 
ATOM   5743 C  C    . ASN   B 1 117 ? 33.298 -13.981 -6.292  1.00 12.32 ?  117 ASN   B C    1 
ATOM   5744 O  O    . ASN   B 1 117 ? 32.693 -13.324 -7.141  1.00 13.55 ?  117 ASN   B O    1 
ATOM   5745 C  CB   . ASN   B 1 117 ? 31.565 -15.680 -5.641  1.00 12.18 ?  117 ASN   B CB   1 
ATOM   5746 C  CG   . ASN   B 1 117 ? 31.114 -17.085 -5.892  1.00 12.55 ?  117 ASN   B CG   1 
ATOM   5747 O  OD1  . ASN   B 1 117 ? 31.463 -17.673 -6.917  1.00 13.53 ?  117 ASN   B OD1  1 
ATOM   5748 N  ND2  . ASN   B 1 117 ? 30.384 -17.658 -4.948  1.00 12.51 ?  117 ASN   B ND2  1 
ATOM   5749 H  H    . ASN   B 1 117 ? 33.607 -16.419 -4.519  1.00 14.01 ?  117 ASN   B H    1 
ATOM   5750 H  HA   . ASN   B 1 117 ? 33.041 -15.858 -7.018  1.00 14.44 ?  117 ASN   B HA   1 
ATOM   5751 H  HB2  . ASN   B 1 117 ? 31.531 -15.512 -4.681  1.00 14.63 ?  117 ASN   B HB2  1 
ATOM   5752 H  HB3  . ASN   B 1 117 ? 30.968 -15.069 -6.103  1.00 14.63 ?  117 ASN   B HB3  1 
ATOM   5753 H  HD21 . ASN   B 1 117 ? 30.096 -18.461 -5.051  1.00 15.03 ?  117 ASN   B HD21 1 
ATOM   5754 H  HD22 . ASN   B 1 117 ? 30.166 -17.214 -4.239  1.00 15.03 ?  117 ASN   B HD22 1 
ATOM   5755 N  N    . GLN   B 1 118 ? 34.239 -13.456 -5.521  1.00 11.99 ?  118 GLN   B N    1 
ATOM   5756 C  CA   . GLN   B 1 118 ? 34.670 -12.071 -5.659  1.00 12.97 ?  118 GLN   B CA   1 
ATOM   5757 C  C    . GLN   B 1 118 ? 35.737 -11.879 -6.732  1.00 12.88 ?  118 GLN   B C    1 
ATOM   5758 O  O    . GLN   B 1 118 ? 36.209 -10.754 -6.914  1.00 14.23 ?  118 GLN   B O    1 
ATOM   5759 C  CB   . GLN   B 1 118 ? 35.149 -11.542 -4.304  1.00 13.18 ?  118 GLN   B CB   1 
ATOM   5760 C  CG   . GLN   B 1 118 ? 34.066 -11.573 -3.236  1.00 13.47 ?  118 GLN   B CG   1 
ATOM   5761 C  CD   . GLN   B 1 118 ? 32.889 -10.673 -3.571  1.00 13.28 ?  118 GLN   B CD   1 
ATOM   5762 O  OE1  . GLN   B 1 118 ? 33.073 -9.537  -4.019  1.00 13.95 ?  118 GLN   B OE1  1 
ATOM   5763 N  NE2  . GLN   B 1 118 ? 31.680 -11.166 -3.353  1.00 13.76 ?  118 GLN   B NE2  1 
ATOM   5764 H  H    . GLN   B 1 118 ? 34.665 -13.880 -4.905  1.00 14.39 ?  118 GLN   B H    1 
ATOM   5765 H  HA   . GLN   B 1 118 ? 33.907 -11.537 -5.933  1.00 15.57 ?  118 GLN   B HA   1 
ATOM   5766 H  HB2  . GLN   B 1 118 ? 35.893 -12.079 -3.999  1.00 15.83 ?  118 GLN   B HB2  1 
ATOM   5767 H  HB3  . GLN   B 1 118 ? 35.434 -10.614 -4.410  1.00 15.83 ?  118 GLN   B HB3  1 
ATOM   5768 H  HG2  . GLN   B 1 118 ? 33.738 -12.483 -3.150  1.00 16.17 ?  118 GLN   B HG2  1 
ATOM   5769 H  HG3  . GLN   B 1 118 ? 34.446 -11.277 -2.394  1.00 16.17 ?  118 GLN   B HG3  1 
ATOM   5770 H  HE21 . GLN   B 1 118 ? 31.595 -11.965 -3.037  1.00 16.52 ?  118 GLN   B HE21 1 
ATOM   5771 H  HE22 . GLN   B 1 118 ? 30.989 -10.696 -3.528  1.00 16.52 ?  118 GLN   B HE22 1 
ATOM   5772 N  N    . HIS   B 1 119 ? 36.087 -12.937 -7.466  1.00 12.22 ?  119 HIS   B N    1 
ATOM   5773 C  CA   . HIS   B 1 119 ? 37.133 -12.893 -8.479  1.00 12.42 ?  119 HIS   B CA   1 
ATOM   5774 C  C    . HIS   B 1 119 ? 36.651 -13.623 -9.719  1.00 12.32 ?  119 HIS   B C    1 
ATOM   5775 O  O    . HIS   B 1 119 ? 36.138 -14.739 -9.619  1.00 13.14 ?  119 HIS   B O    1 
ATOM   5776 C  CB   . HIS   B 1 119 ? 38.409 -13.530 -7.929  1.00 12.73 ?  119 HIS   B CB   1 
ATOM   5777 C  CG   . HIS   B 1 119 ? 38.889 -12.840 -6.700  1.00 13.93 ?  119 HIS   B CG   1 
ATOM   5778 N  ND1  . HIS   B 1 119 ? 39.685 -11.715 -6.747  1.00 15.61 ?  119 HIS   B ND1  1 
ATOM   5779 C  CD2  . HIS   B 1 119 ? 38.592 -13.041 -5.396  1.00 15.00 ?  119 HIS   B CD2  1 
ATOM   5780 C  CE1  . HIS   B 1 119 ? 39.892 -11.281 -5.518  1.00 16.55 ?  119 HIS   B CE1  1 
ATOM   5781 N  NE2  . HIS   B 1 119 ? 39.233 -12.061 -4.680  1.00 16.57 ?  119 HIS   B NE2  1 
ATOM   5782 H  H    . HIS   B 1 119 ? 35.713 -13.715 -7.403  1.00 14.67 ?  119 HIS   B H    1 
ATOM   5783 H  HA   . HIS   B 1 119 ? 37.317 -11.971 -8.718  1.00 14.91 ?  119 HIS   B HA   1 
ATOM   5784 H  HB2  . HIS   B 1 119 ? 38.238 -14.457 -7.713  1.00 15.28 ?  119 HIS   B HB2  1 
ATOM   5785 H  HB3  . HIS   B 1 119 ? 39.110 -13.469 -8.603  1.00 15.28 ?  119 HIS   B HB3  1 
ATOM   5786 H  HD2  . HIS   B 1 119 ? 38.058 -13.721 -5.051  1.00 18.01 ?  119 HIS   B HD2  1 
ATOM   5787 H  HE1  . HIS   B 1 119 ? 40.426 -10.559 -5.274  1.00 19.87 ?  119 HIS   B HE1  1 
ATOM   5788 H  HE2  . HIS   B 1 119 ? 39.236 -11.993 -3.820  1.00 19.90 ?  119 HIS   B HE2  1 
ATOM   5789 N  N    . GLU   B 1 120 ? 36.812 -13.003 -10.888 1.00 13.15 ?  120 GLU   B N    1 
ATOM   5790 C  CA   . GLU   B 1 120 ? 36.228 -13.582 -12.095 1.00 14.54 ?  120 GLU   B CA   1 
ATOM   5791 C  C    . GLU   B 1 120 ? 36.899 -14.888 -12.504 1.00 13.47 ?  120 GLU   B C    1 
ATOM   5792 O  O    . GLU   B 1 120 ? 36.231 -15.766 -13.063 1.00 13.73 ?  120 GLU   B O    1 
ATOM   5793 C  CB   . GLU   B 1 120 ? 36.258 -12.573 -13.240 1.00 19.28 ?  120 GLU   B CB   1 
ATOM   5794 C  CG   . GLU   B 1 120 ? 35.305 -11.406 -13.036 1.00 25.89 ?  120 GLU   B CG   1 
ATOM   5795 C  CD   . GLU   B 1 120 ? 35.181 -10.523 -14.262 1.00 32.10 ?  120 GLU   B CD   1 
ATOM   5796 O  OE1  . GLU   B 1 120 ? 36.185 -10.364 -14.990 1.00 34.31 ?  120 GLU   B OE1  1 
ATOM   5797 O  OE2  . GLU   B 1 120 ? 34.076 -9.991  -14.498 1.00 34.92 -1 120 GLU   B OE2  1 
ATOM   5798 H  H    . GLU   B 1 120 ? 37.236 -12.259 -11.008 1.00 15.78 ?  120 GLU   B H    1 
ATOM   5799 H  HA   . GLU   B 1 120 ? 35.299 -13.779 -11.915 1.00 17.45 ?  120 GLU   B HA   1 
ATOM   5800 H  HB2  . GLU   B 1 120 ? 37.151 -12.209 -13.325 1.00 23.15 ?  120 GLU   B HB2  1 
ATOM   5801 H  HB3  . GLU   B 1 120 ? 36.002 -13.018 -14.063 1.00 23.15 ?  120 GLU   B HB3  1 
ATOM   5802 H  HG2  . GLU   B 1 120 ? 34.418 -11.746 -12.834 1.00 31.08 ?  120 GLU   B HG2  1 
ATOM   5803 H  HG3  . GLU   B 1 120 ? 35.622 -10.856 -12.303 1.00 31.08 ?  120 GLU   B HG3  1 
ATOM   5804 N  N    . VAL   B 1 121 ? 38.196 -15.037 -12.240 1.00 13.26 ?  121 VAL   B N    1 
ATOM   5805 C  CA   . VAL   B 1 121 ? 38.936 -16.248 -12.587 1.00 12.79 ?  121 VAL   B CA   1 
ATOM   5806 C  C    . VAL   B 1 121 ? 40.048 -16.453 -11.566 1.00 12.39 ?  121 VAL   B C    1 
ATOM   5807 O  O    . VAL   B 1 121 ? 40.730 -15.498 -11.176 1.00 13.08 ?  121 VAL   B O    1 
ATOM   5808 C  CB   . VAL   B 1 121 ? 39.454 -16.201 -14.044 1.00 14.53 ?  121 VAL   B CB   1 
ATOM   5809 C  CG1  . VAL   B 1 121 ? 40.304 -14.958 -14.293 1.00 15.56 ?  121 VAL   B CG1  1 
ATOM   5810 C  CG2  . VAL   B 1 121 ? 40.216 -17.473 -14.397 1.00 15.95 ?  121 VAL   B CG2  1 
ATOM   5811 H  H    . VAL   B 1 121 ? 38.682 -14.435 -11.861 1.00 15.92 ?  121 VAL   B H    1 
ATOM   5812 H  HA   . VAL   B 1 121 ? 38.326 -17.001 -12.521 1.00 15.36 ?  121 VAL   B HA   1 
ATOM   5813 H  HB   . VAL   B 1 121 ? 38.685 -16.152 -14.640 1.00 17.44 ?  121 VAL   B HB   1 
ATOM   5814 H  HG11 . VAL   B 1 121 ? 40.626 -14.972 -15.207 1.00 18.69 ?  121 VAL   B HG11 1 
ATOM   5815 H  HG12 . VAL   B 1 121 ? 39.759 -14.167 -14.147 1.00 18.69 ?  121 VAL   B HG12 1 
ATOM   5816 H  HG13 . VAL   B 1 121 ? 41.053 -14.960 -13.677 1.00 18.69 ?  121 VAL   B HG13 1 
ATOM   5817 H  HG21 . VAL   B 1 121 ? 40.414 -17.471 -15.348 1.00 19.15 ?  121 VAL   B HG21 1 
ATOM   5818 H  HG22 . VAL   B 1 121 ? 41.044 -17.498 -13.891 1.00 19.15 ?  121 VAL   B HG22 1 
ATOM   5819 H  HG23 . VAL   B 1 121 ? 39.671 -18.245 -14.177 1.00 19.15 ?  121 VAL   B HG23 1 
ATOM   5820 N  N    . LEU   B 1 122 ? 40.224 -17.705 -11.125 1.00 11.83 ?  122 LEU   B N    1 
ATOM   5821 C  CA   . LEU   B 1 122 ? 41.207 -18.056 -10.104 1.00 11.68 ?  122 LEU   B CA   1 
ATOM   5822 C  C    . LEU   B 1 122 ? 41.862 -19.386 -10.430 1.00 11.42 ?  122 LEU   B C    1 
ATOM   5823 O  O    . LEU   B 1 122 ? 41.202 -20.303 -10.928 1.00 12.58 ?  122 LEU   B O    1 
ATOM   5824 C  CB   . LEU   B 1 122 ? 40.553 -18.287 -8.729  1.00 13.16 ?  122 LEU   B CB   1 
ATOM   5825 C  CG   . LEU   B 1 122 ? 39.522 -17.263 -8.250  1.00 13.34 ?  122 LEU   B CG   1 
ATOM   5826 C  CD1  . LEU   B 1 122 ? 38.127 -17.635 -8.724  1.00 14.23 ?  122 LEU   B CD1  1 
ATOM   5827 C  CD2  . LEU   B 1 122 ? 39.554 -17.140 -6.742  1.00 12.80 ?  122 LEU   B CD2  1 
ATOM   5828 H  H    . LEU   B 1 122 ? 39.773 -18.383 -11.408 1.00 14.20 ?  122 LEU   B H    1 
ATOM   5829 H  HA   . LEU   B 1 122 ? 41.880 -17.363 -10.023 1.00 14.03 ?  122 LEU   B HA   1 
ATOM   5830 H  HB2  . LEU   B 1 122 ? 40.107 -19.147 -8.746  1.00 15.80 ?  122 LEU   B HB2  1 
ATOM   5831 H  HB3  . LEU   B 1 122 ? 41.254 -18.305 -8.059  1.00 15.80 ?  122 LEU   B HB3  1 
ATOM   5832 H  HG   . LEU   B 1 122 ? 39.736 -16.396 -8.624  1.00 16.02 ?  122 LEU   B HG   1 
ATOM   5833 H  HD11 . LEU   B 1 122 ? 37.489 -16.992 -8.371  1.00 17.09 ?  122 LEU   B HD11 1 
ATOM   5834 H  HD12 . LEU   B 1 122 ? 38.104 -17.616 -9.695  1.00 17.09 ?  122 LEU   B HD12 1 
ATOM   5835 H  HD13 . LEU   B 1 122 ? 37.908 -18.524 -8.406  1.00 17.09 ?  122 LEU   B HD13 1 
ATOM   5836 H  HD21 . LEU   B 1 122 ? 38.872 -16.512 -6.457  1.00 15.37 ?  122 LEU   B HD21 1 
ATOM   5837 H  HD22 . LEU   B 1 122 ? 39.388 -18.010 -6.348  1.00 15.37 ?  122 LEU   B HD22 1 
ATOM   5838 H  HD23 . LEU   B 1 122 ? 40.430 -16.818 -6.473  1.00 15.37 ?  122 LEU   B HD23 1 
ATOM   5839 N  N    . LEU   B 1 123 ? 43.149 -19.494 -10.079 1.00 11.07 ?  123 LEU   B N    1 
ATOM   5840 C  CA   . LEU   B 1 123 ? 43.858 -20.763 -9.953  1.00 11.26 ?  123 LEU   B CA   1 
ATOM   5841 C  C    . LEU   B 1 123 ? 43.832 -21.150 -8.481  1.00 10.73 ?  123 LEU   B C    1 
ATOM   5842 O  O    . LEU   B 1 123 ? 44.186 -20.326 -7.629  1.00 11.29 ?  123 LEU   B O    1 
ATOM   5843 C  CB   . LEU   B 1 123 ? 45.306 -20.589 -10.413 1.00 11.88 ?  123 LEU   B CB   1 
ATOM   5844 C  CG   . LEU   B 1 123 ? 46.248 -21.773 -10.173 1.00 12.22 ?  123 LEU   B CG   1 
ATOM   5845 C  CD1  . LEU   B 1 123 ? 45.820 -23.022 -10.937 1.00 12.85 ?  123 LEU   B CD1  1 
ATOM   5846 C  CD2  . LEU   B 1 123 ? 47.666 -21.380 -10.555 1.00 13.01 ?  123 LEU   B CD2  1 
ATOM   5847 H  H    . LEU   B 1 123 ? 43.643 -18.816 -9.884  1.00 13.29 ?  123 LEU   B H    1 
ATOM   5848 H  HA   . LEU   B 1 123 ? 43.417 -21.454 -10.477 1.00 13.53 ?  123 LEU   B HA   1 
ATOM   5849 H  HB2  . LEU   B 1 123 ? 45.294 -20.418 -11.366 1.00 14.26 ?  123 LEU   B HB2  1 
ATOM   5850 H  HB3  . LEU   B 1 123 ? 45.676 -19.826 -9.950  1.00 14.26 ?  123 LEU   B HB3  1 
ATOM   5851 H  HG   . LEU   B 1 123 ? 46.251 -21.992 -9.228  1.00 14.68 ?  123 LEU   B HG   1 
ATOM   5852 H  HD11 . LEU   B 1 123 ? 46.460 -23.729 -10.763 1.00 15.43 ?  123 LEU   B HD11 1 
ATOM   5853 H  HD12 . LEU   B 1 123 ? 44.939 -23.287 -10.636 1.00 15.43 ?  123 LEU   B HD12 1 
ATOM   5854 H  HD13 . LEU   B 1 123 ? 45.802 -22.816 -11.884 1.00 15.43 ?  123 LEU   B HD13 1 
ATOM   5855 H  HD21 . LEU   B 1 123 ? 48.253 -22.136 -10.401 1.00 15.62 ?  123 LEU   B HD21 1 
ATOM   5856 H  HD22 . LEU   B 1 123 ? 47.681 -21.134 -11.493 1.00 15.62 ?  123 LEU   B HD22 1 
ATOM   5857 H  HD23 . LEU   B 1 123 ? 47.940 -20.628 -10.009 1.00 15.62 ?  123 LEU   B HD23 1 
ATOM   5858 N  N    . ALA   B 1 124 ? 43.404 -22.379 -8.168  1.00 10.93 ?  124 ALA   B N    1 
ATOM   5859 C  CA   . ALA   B 1 124 ? 43.145 -22.696 -6.773  1.00 11.09 ?  124 ALA   B CA   1 
ATOM   5860 C  C    . ALA   B 1 124 ? 43.415 -24.153 -6.436  1.00 10.91 ?  124 ALA   B C    1 
ATOM   5861 O  O    . ALA   B 1 124 ? 43.273 -25.032 -7.297  1.00 11.52 ?  124 ALA   B O    1 
ATOM   5862 C  CB   . ALA   B 1 124 ? 41.684 -22.388 -6.416  1.00 11.90 ?  124 ALA   B CB   1 
ATOM   5863 H  H    . ALA   B 1 124 ? 43.251 -23.024 -8.725  1.00 13.13 ?  124 ALA   B H    1 
ATOM   5864 H  HA   . ALA   B 1 124 ? 43.709 -22.139 -6.221  1.00 13.32 ?  124 ALA   B HA   1 
ATOM   5865 H  HB1  . ALA   B 1 124 ? 41.526 -22.597 -5.483  1.00 14.29 ?  124 ALA   B HB1  1 
ATOM   5866 H  HB2  . ALA   B 1 124 ? 41.512 -21.440 -6.572  1.00 14.29 ?  124 ALA   B HB2  1 
ATOM   5867 H  HB3  . ALA   B 1 124 ? 41.096 -22.919 -6.979  1.00 14.29 ?  124 ALA   B HB3  1 
ATOM   5868 N  N    . PRO   B 1 125 ? 43.713 -24.441 -5.173  1.00 11.12 ?  125 PRO   B N    1 
ATOM   5869 C  CA   . PRO   B 1 125 ? 43.647 -25.806 -4.651  1.00 11.92 ?  125 PRO   B CA   1 
ATOM   5870 C  C    . PRO   B 1 125 ? 42.245 -26.077 -4.109  1.00 11.95 ?  125 PRO   B C    1 
ATOM   5871 O  O    . PRO   B 1 125 ? 41.450 -25.160 -3.902  1.00 12.41 ?  125 PRO   B O    1 
ATOM   5872 C  CB   . PRO   B 1 125 ? 44.630 -25.740 -3.476  1.00 12.82 ?  125 PRO   B CB   1 
ATOM   5873 C  CG   . PRO   B 1 125 ? 44.381 -24.349 -2.905  1.00 12.58 ?  125 PRO   B CG   1 
ATOM   5874 C  CD   . PRO   B 1 125 ? 44.037 -23.475 -4.108  1.00 11.67 ?  125 PRO   B CD   1 
ATOM   5875 H  HA   . PRO   B 1 125 ? 43.924 -26.474 -5.298  1.00 14.31 ?  125 PRO   B HA   1 
ATOM   5876 H  HB2  . PRO   B 1 125 ? 44.419 -26.422 -2.817  1.00 15.39 ?  125 PRO   B HB2  1 
ATOM   5877 H  HB3  . PRO   B 1 125 ? 45.542 -25.823 -3.787  1.00 15.39 ?  125 PRO   B HB3  1 
ATOM   5878 H  HG2  . PRO   B 1 125 ? 43.637 -24.376 -2.277  1.00 15.10 ?  125 PRO   B HG2  1 
ATOM   5879 H  HG3  . PRO   B 1 125 ? 45.183 -24.025 -2.459  1.00 15.10 ?  125 PRO   B HG3  1 
ATOM   5880 H  HD2  . PRO   B 1 125 ? 43.271 -22.915 -3.913  1.00 14.01 ?  125 PRO   B HD2  1 
ATOM   5881 H  HD3  . PRO   B 1 125 ? 44.810 -22.938 -4.362  1.00 14.01 ?  125 PRO   B HD3  1 
ATOM   5882 N  N    . LEU   B 1 126 ? 41.980 -27.356 -3.817  1.00 12.63 ?  126 LEU   B N    1 
ATOM   5883 C  CA   . LEU   B 1 126 ? 40.761 -27.722 -3.103  1.00 13.12 ?  126 LEU   B CA   1 
ATOM   5884 C  C    . LEU   B 1 126 ? 40.882 -27.322 -1.639  1.00 13.46 ?  126 LEU   B C    1 
ATOM   5885 O  O    . LEU   B 1 126 ? 41.777 -27.785 -0.925  1.00 15.18 ?  126 LEU   B O    1 
ATOM   5886 C  CB   . LEU   B 1 126 ? 40.508 -29.218 -3.218  1.00 14.22 ?  126 LEU   B CB   1 
ATOM   5887 C  CG   . LEU   B 1 126 ? 39.987 -29.704 -4.570  1.00 15.41 ?  126 LEU   B CG   1 
ATOM   5888 C  CD1  . LEU   B 1 126 ? 40.014 -31.213 -4.628  1.00 17.29 ?  126 LEU   B CD1  1 
ATOM   5889 C  CD2  . LEU   B 1 126 ? 38.572 -29.210 -4.833  1.00 15.73 ?  126 LEU   B CD2  1 
ATOM   5890 H  H    . LEU   B 1 126 ? 42.494 -28.021 -4.006  1.00 15.16 ?  126 LEU   B H    1 
ATOM   5891 H  HA   . LEU   B 1 126 ? 40.012 -27.244 -3.488  1.00 15.76 ?  126 LEU   B HA   1 
ATOM   5892 H  HB2  . LEU   B 1 126 ? 41.342 -29.679 -3.045  1.00 17.08 ?  126 LEU   B HB2  1 
ATOM   5893 H  HB3  . LEU   B 1 126 ? 39.854 -29.464 -2.549  1.00 17.08 ?  126 LEU   B HB3  1 
ATOM   5894 H  HG   . LEU   B 1 126 ? 40.563 -29.365 -5.273  1.00 18.50 ?  126 LEU   B HG   1 
ATOM   5895 H  HD11 . LEU   B 1 126 ? 39.679 -31.502 -5.492  1.00 20.76 ?  126 LEU   B HD11 1 
ATOM   5896 H  HD12 . LEU   B 1 126 ? 40.923 -31.520 -4.504  1.00 20.76 ?  126 LEU   B HD12 1 
ATOM   5897 H  HD13 . LEU   B 1 126 ? 39.446 -31.565 -3.921  1.00 20.76 ?  126 LEU   B HD13 1 
ATOM   5898 H  HD21 . LEU   B 1 126 ? 38.241 -29.619 -5.648  1.00 18.89 ?  126 LEU   B HD21 1 
ATOM   5899 H  HD22 . LEU   B 1 126 ? 38.006 -29.456 -4.086  1.00 18.89 ?  126 LEU   B HD22 1 
ATOM   5900 H  HD23 . LEU   B 1 126 ? 38.586 -28.243 -4.932  1.00 18.89 ?  126 LEU   B HD23 1 
ATOM   5901 N  N    . LEU   B 1 127 ? 39.959 -26.486 -1.183  1.00 13.34 ?  127 LEU   B N    1 
ATOM   5902 C  CA   . LEU   B 1 127 ? 40.011 -25.988 0.180   1.00 13.77 ?  127 LEU   B CA   1 
ATOM   5903 C  C    . LEU   B 1 127 ? 39.739 -27.108 1.179   1.00 13.56 ?  127 LEU   B C    1 
ATOM   5904 O  O    . LEU   B 1 127 ? 38.915 -28.003 0.953   1.00 14.09 ?  127 LEU   B O    1 
ATOM   5905 C  CB   . LEU   B 1 127 ? 38.984 -24.874 0.381   1.00 14.30 ?  127 LEU   B CB   1 
ATOM   5906 C  CG   . LEU   B 1 127 ? 39.173 -23.610 -0.461  1.00 14.81 ?  127 LEU   B CG   1 
ATOM   5907 C  CD1  . LEU   B 1 127 ? 38.054 -22.636 -0.163  1.00 15.07 ?  127 LEU   B CD1  1 
ATOM   5908 C  CD2  . LEU   B 1 127 ? 40.532 -22.965 -0.214  1.00 15.65 ?  127 LEU   B CD2  1 
ATOM   5909 H  H    . LEU   B 1 127 ? 39.295 -26.186 -1.647  1.00 16.01 ?  127 LEU   B H    1 
ATOM   5910 H  HA   . LEU   B 1 127 ? 40.894 -25.623 0.357   1.00 16.53 ?  127 LEU   B HA   1 
ATOM   5911 H  HB2  . LEU   B 1 127 ? 38.106 -25.229 0.169   1.00 17.16 ?  127 LEU   B HB2  1 
ATOM   5912 H  HB3  . LEU   B 1 127 ? 39.005 -24.603 1.311   1.00 17.16 ?  127 LEU   B HB3  1 
ATOM   5913 H  HG   . LEU   B 1 127 ? 39.114 -23.839 -1.400  1.00 17.78 ?  127 LEU   B HG   1 
ATOM   5914 H  HD11 . LEU   B 1 127 ? 38.186 -21.827 -0.693  1.00 18.09 ?  127 LEU   B HD11 1 
ATOM   5915 H  HD12 . LEU   B 1 127 ? 37.204 -23.039 -0.390  1.00 18.09 ?  127 LEU   B HD12 1 
ATOM   5916 H  HD13 . LEU   B 1 127 ? 38.071 -22.407 0.781   1.00 18.09 ?  127 LEU   B HD13 1 
ATOM   5917 H  HD21 . LEU   B 1 127 ? 40.570 -22.110 -0.674  1.00 18.79 ?  127 LEU   B HD21 1 
ATOM   5918 H  HD22 . LEU   B 1 127 ? 40.652 -22.830 0.741   1.00 18.79 ?  127 LEU   B HD22 1 
ATOM   5919 H  HD23 . LEU   B 1 127 ? 41.226 -23.552 -0.553  1.00 18.79 ?  127 LEU   B HD23 1 
ATOM   5920 N  N    . SER   B 1 128 ? 40.418 -27.020 2.314   1.00 13.65 ?  128 SER   B N    1 
ATOM   5921 C  CA   . SER   B 1 128 ? 40.300 -27.932 3.440   1.00 14.09 ?  128 SER   B CA   1 
ATOM   5922 C  C    . SER   B 1 128 ? 40.787 -29.343 3.124   1.00 15.51 ?  128 SER   B C    1 
ATOM   5923 O  O    . SER   B 1 128 ? 40.679 -30.220 3.979   1.00 16.75 ?  128 SER   B O    1 
ATOM   5924 C  CB   . SER   B 1 128 ? 38.899 -27.935 4.071   1.00 14.53 ?  128 SER   B CB   1 
ATOM   5925 O  OG   . SER   B 1 128 ? 38.590 -26.653 4.611   1.00 15.00 ?  128 SER   B OG   1 
ATOM   5926 H  H    . SER   B 1 128 ? 40.983 -26.393 2.466   1.00 16.39 ?  128 SER   B H    1 
ATOM   5927 H  HA   . SER   B 1 128 ? 40.892 -27.598 4.123   1.00 16.92 ?  128 SER   B HA   1 
ATOM   5928 H  HB2  . SER   B 1 128 ? 38.238 -28.173 3.401   1.00 17.44 ?  128 SER   B HB2  1 
ATOM   5929 H  HB3  . SER   B 1 128 ? 38.879 -28.597 4.794   1.00 17.44 ?  128 SER   B HB3  1 
ATOM   5930 H  HG   . SER   B 1 128 ? 39.161 -26.447 5.190   1.00 18.01 ?  128 SER   B HG   1 
ATOM   5931 N  N    . ALA   B 1 129 ? 41.365 -29.569 1.942   1.00 16.72 ?  129 ALA   B N    1 
ATOM   5932 C  CA   . ALA   B 1 129 ? 41.907 -30.868 1.582   1.00 17.52 ?  129 ALA   B CA   1 
ATOM   5933 C  C    . ALA   B 1 129 ? 43.304 -31.049 2.165   1.00 16.48 ?  129 ALA   B C    1 
ATOM   5934 O  O    . ALA   B 1 129 ? 43.864 -30.157 2.815   1.00 16.14 ?  129 ALA   B O    1 
ATOM   5935 C  CB   . ALA   B 1 129 ? 41.956 -31.025 0.063   1.00 19.84 ?  129 ALA   B CB   1 
ATOM   5936 H  H    . ALA   B 1 129 ? 41.464 -28.976 1.323   1.00 20.07 ?  129 ALA   B H    1 
ATOM   5937 H  HA   . ALA   B 1 129 ? 41.339 -31.562 1.941   1.00 21.03 ?  129 ALA   B HA   1 
ATOM   5938 H  HB1  . ALA   B 1 129 ? 42.305 -31.905 -0.155  1.00 23.82 ?  129 ALA   B HB1  1 
ATOM   5939 H  HB2  . ALA   B 1 129 ? 41.060 -30.928 -0.291  1.00 23.82 ?  129 ALA   B HB2  1 
ATOM   5940 H  HB3  . ALA   B 1 129 ? 42.536 -30.341 -0.309  1.00 23.82 ?  129 ALA   B HB3  1 
ATOM   5941 N  N    . GLY   B 1 130 ? 43.874 -32.229 1.912   1.00 16.34 ?  130 GLY   B N    1 
ATOM   5942 C  CA   . GLY   B 1 130 ? 45.261 -32.472 2.266   1.00 16.76 ?  130 GLY   B CA   1 
ATOM   5943 C  C    . GLY   B 1 130 ? 45.471 -32.374 3.758   1.00 16.81 ?  130 GLY   B C    1 
ATOM   5944 O  O    . GLY   B 1 130 ? 44.769 -33.013 4.555   1.00 17.79 ?  130 GLY   B O    1 
ATOM   5945 H  H    . GLY   B 1 130 ? 43.485 -32.892 1.523   1.00 19.62 ?  130 GLY   B H    1 
ATOM   5946 H  HA2  . GLY   B 1 130 ? 45.526 -33.361 1.976   1.00 20.12 ?  130 GLY   B HA2  1 
ATOM   5947 H  HA3  . GLY   B 1 130 ? 45.835 -31.823 1.826   1.00 20.12 ?  130 GLY   B HA3  1 
ATOM   5948 N  N    . ILE   B 1 131 ? 46.452 -31.551 4.146   1.00 17.20 ?  131 ILE   B N    1 
ATOM   5949 C  CA   . ILE   B 1 131 ? 46.814 -31.419 5.550   1.00 18.34 ?  131 ILE   B CA   1 
ATOM   5950 C  C    . ILE   B 1 131 ? 45.702 -30.812 6.387   1.00 17.29 ?  131 ILE   B C    1 
ATOM   5951 O  O    . ILE   B 1 131 ? 45.782 -30.866 7.618   1.00 18.78 ?  131 ILE   B O    1 
ATOM   5952 C  CB   . ILE   B 1 131 ? 48.138 -30.645 5.752   1.00 20.08 ?  131 ILE   B CB   1 
ATOM   5953 C  CG1  . ILE   B 1 131 ? 47.974 -29.165 5.378   1.00 21.20 ?  131 ILE   B CG1  1 
ATOM   5954 C  CG2  . ILE   B 1 131 ? 49.263 -31.287 4.942   1.00 21.07 ?  131 ILE   B CG2  1 
ATOM   5955 C  CD1  . ILE   B 1 131 ? 49.184 -28.312 5.699   1.00 22.42 ?  131 ILE   B CD1  1 
ATOM   5956 H  H    . ILE   B 1 131 ? 46.915 -31.050 3.615   1.00 20.64 ?  131 ILE   B H    1 
ATOM   5957 H  HA   . ILE   B 1 131 ? 46.956 -32.306 5.895   1.00 22.02 ?  131 ILE   B HA   1 
ATOM   5958 H  HB   . ILE   B 1 131 ? 48.372 -30.693 6.692   1.00 24.11 ?  131 ILE   B HB   1 
ATOM   5959 H  HG12 . ILE   B 1 131 ? 47.808 -29.102 4.425   1.00 25.46 ?  131 ILE   B HG12 1 
ATOM   5960 H  HG13 . ILE   B 1 131 ? 47.221 -28.791 5.865   1.00 25.46 ?  131 ILE   B HG13 1 
ATOM   5961 H  HG21 . ILE   B 1 131 ? 50.103 -30.884 5.201   1.00 25.30 ?  131 ILE   B HG21 1 
ATOM   5962 H  HG22 . ILE   B 1 131 ? 49.274 -32.236 5.126   1.00 25.30 ?  131 ILE   B HG22 1 
ATOM   5963 H  HG23 . ILE   B 1 131 ? 49.093 -31.132 3.999   1.00 25.30 ?  131 ILE   B HG23 1 
ATOM   5964 H  HD11 . ILE   B 1 131 ? 48.966 -27.383 5.529   1.00 26.92 ?  131 ILE   B HD11 1 
ATOM   5965 H  HD12 . ILE   B 1 131 ? 49.414 -28.434 6.633   1.00 26.92 ?  131 ILE   B HD12 1 
ATOM   5966 H  HD13 . ILE   B 1 131 ? 49.922 -28.589 5.136   1.00 26.92 ?  131 ILE   B HD13 1 
ATOM   5967 N  N    . PHE   B 1 132 ? 44.669 -30.235 5.759   1.00 16.21 ?  132 PHE   B N    1 
ATOM   5968 C  CA   . PHE   B 1 132 ? 43.518 -29.722 6.492   1.00 16.74 ?  132 PHE   B CA   1 
ATOM   5969 C  C    . PHE   B 1 132 ? 42.497 -30.807 6.834   1.00 18.31 ?  132 PHE   B C    1 
ATOM   5970 O  O    . PHE   B 1 132 ? 41.603 -30.554 7.647   1.00 19.89 ?  132 PHE   B O    1 
ATOM   5971 C  CB   . PHE   B 1 132 ? 42.839 -28.594 5.707   1.00 15.61 ?  132 PHE   B CB   1 
ATOM   5972 C  CG   . PHE   B 1 132 ? 43.539 -27.256 5.808   1.00 15.19 ?  132 PHE   B CG   1 
ATOM   5973 C  CD1  . PHE   B 1 132 ? 44.827 -27.080 5.332   1.00 16.15 ?  132 PHE   B CD1  1 
ATOM   5974 C  CD2  . PHE   B 1 132 ? 42.873 -26.157 6.333   1.00 14.65 ?  132 PHE   B CD2  1 
ATOM   5975 C  CE1  . PHE   B 1 132 ? 45.449 -25.844 5.417   1.00 16.71 ?  132 PHE   B CE1  1 
ATOM   5976 C  CE2  . PHE   B 1 132 ? 43.485 -24.917 6.408   1.00 15.22 ?  132 PHE   B CE2  1 
ATOM   5977 C  CZ   . PHE   B 1 132 ? 44.772 -24.765 5.954   1.00 16.19 ?  132 PHE   B CZ   1 
ATOM   5978 H  H    . PHE   B 1 132 ? 44.609 -30.135 4.906   1.00 19.46 ?  132 PHE   B H    1 
ATOM   5979 H  HA   . PHE   B 1 132 ? 43.830 -29.348 7.327   1.00 20.10 ?  132 PHE   B HA   1 
ATOM   5980 H  HB2  . PHE   B 1 132 ? 42.817 -28.840 4.773   1.00 18.74 ?  132 PHE   B HB2  1 
ATOM   5981 H  HB3  . PHE   B 1 132 ? 41.934 -28.484 6.042   1.00 18.74 ?  132 PHE   B HB3  1 
ATOM   5982 H  HD1  . PHE   B 1 132 ? 45.286 -27.808 4.976   1.00 19.38 ?  132 PHE   B HD1  1 
ATOM   5983 H  HD2  . PHE   B 1 132 ? 42.002 -26.255 6.648   1.00 17.59 ?  132 PHE   B HD2  1 
ATOM   5984 H  HE1  . PHE   B 1 132 ? 46.320 -25.742 5.106   1.00 20.06 ?  132 PHE   B HE1  1 
ATOM   5985 H  HE2  . PHE   B 1 132 ? 43.030 -24.190 6.780   1.00 18.27 ?  132 PHE   B HE2  1 
ATOM   5986 H  HZ   . PHE   B 1 132 ? 45.189 -23.931 6.012   1.00 19.44 ?  132 PHE   B HZ   1 
ATOM   5987 N  N    . GLY   B 1 133 ? 42.586 -31.997 6.229   1.00 18.22 ?  133 GLY   B N    1 
ATOM   5988 C  CA   . GLY   B 1 133 ? 41.873 -33.157 6.733   1.00 19.22 ?  133 GLY   B CA   1 
ATOM   5989 C  C    . GLY   B 1 133 ? 40.478 -33.420 6.199   1.00 19.52 ?  133 GLY   B C    1 
ATOM   5990 O  O    . GLY   B 1 133 ? 39.895 -34.443 6.566   1.00 21.13 ?  133 GLY   B O    1 
ATOM   5991 H  H    . GLY   B 1 133 ? 43.055 -32.151 5.523   1.00 21.88 ?  133 GLY   B H    1 
ATOM   5992 H  HA2  . GLY   B 1 133 ? 42.411 -33.943 6.556   1.00 23.07 ?  133 GLY   B HA2  1 
ATOM   5993 H  HA3  . GLY   B 1 133 ? 41.789 -33.067 7.692   1.00 23.07 ?  133 GLY   B HA3  1 
ATOM   5994 N  N    . ALA   B 1 134 ? 39.912 -32.553 5.368   1.00 18.71 ?  134 ALA   B N    1 
ATOM   5995 C  CA   . ALA   B 1 134 ? 38.590 -32.841 4.833   1.00 18.60 ?  134 ALA   B CA   1 
ATOM   5996 C  C    . ALA   B 1 134 ? 38.680 -33.837 3.683   1.00 18.62 ?  134 ALA   B C    1 
ATOM   5997 O  O    . ALA   B 1 134 ? 39.735 -34.035 3.074   1.00 19.50 ?  134 ALA   B O    1 
ATOM   5998 C  CB   . ALA   B 1 134 ? 37.909 -31.561 4.351   1.00 18.85 ?  134 ALA   B CB   1 
ATOM   5999 H  H    . ALA   B 1 134 ? 40.256 -31.805 5.116   1.00 22.46 ?  134 ALA   B H    1 
ATOM   6000 H  HA   . ALA   B 1 134 ? 38.040 -33.228 5.534   1.00 22.32 ?  134 ALA   B HA   1 
ATOM   6001 H  HB1  . ALA   B 1 134 ? 37.022 -31.782 4.023   1.00 22.63 ?  134 ALA   B HB1  1 
ATOM   6002 H  HB2  . ALA   B 1 134 ? 37.842 -30.940 5.092   1.00 22.63 ?  134 ALA   B HB2  1 
ATOM   6003 H  HB3  . ALA   B 1 134 ? 38.438 -31.173 3.638   1.00 22.63 ?  134 ALA   B HB3  1 
ATOM   6004 N  N    . ASP   B 1 135 ? 37.546 -34.460 3.388   1.00 18.71 ?  135 ASP   B N    1 
ATOM   6005 C  CA   . ASP   B 1 135 ? 37.454 -35.351 2.243   1.00 19.37 ?  135 ASP   B CA   1 
ATOM   6006 C  C    . ASP   B 1 135 ? 37.548 -34.514 0.975   1.00 18.15 ?  135 ASP   B C    1 
ATOM   6007 O  O    . ASP   B 1 135 ? 36.689 -33.645 0.753   1.00 17.88 ?  135 ASP   B O    1 
ATOM   6008 C  CB   . ASP   B 1 135 ? 36.118 -36.090 2.293   1.00 21.51 ?  135 ASP   B CB   1 
ATOM   6009 C  CG   . ASP   B 1 135 ? 35.946 -37.083 1.160   1.00 23.40 ?  135 ASP   B CG   1 
ATOM   6010 O  OD1  . ASP   B 1 135 ? 36.820 -37.138 0.268   1.00 23.12 ?  135 ASP   B OD1  1 
ATOM   6011 O  OD2  . ASP   B 1 135 ? 34.934 -37.824 1.167   1.00 26.20 -1 135 ASP   B OD2  1 
ATOM   6012 H  H    . ASP   B 1 135 ? 36.814 -34.381 3.832   1.00 22.47 ?  135 ASP   B H    1 
ATOM   6013 H  HA   . ASP   B 1 135 ? 38.175 -36.003 2.276   1.00 23.26 ?  135 ASP   B HA   1 
ATOM   6014 H  HB2  . ASP   B 1 135 ? 36.058 -36.573 3.131   1.00 25.83 ?  135 ASP   B HB2  1 
ATOM   6015 H  HB3  . ASP   B 1 135 ? 35.402 -35.445 2.225   1.00 25.83 ?  135 ASP   B HB3  1 
ATOM   6016 N  N    . PRO   B 1 136 ? 38.555 -34.724 0.126   1.00 18.04 ?  136 PRO   B N    1 
ATOM   6017 C  CA   . PRO   B 1 136 ? 38.646 -33.906 -1.093  1.00 17.15 ?  136 PRO   B CA   1 
ATOM   6018 C  C    . PRO   B 1 136 ? 37.453 -34.065 -2.013  1.00 16.72 ?  136 PRO   B C    1 
ATOM   6019 O  O    . PRO   B 1 136 ? 37.128 -33.125 -2.744  1.00 15.82 ?  136 PRO   B O    1 
ATOM   6020 C  CB   . PRO   B 1 136 ? 39.955 -34.379 -1.742  1.00 18.48 ?  136 PRO   B CB   1 
ATOM   6021 C  CG   . PRO   B 1 136 ? 40.166 -35.764 -1.198  1.00 19.73 ?  136 PRO   B CG   1 
ATOM   6022 C  CD   . PRO   B 1 136 ? 39.635 -35.724 0.203   1.00 19.14 ?  136 PRO   B CD   1 
ATOM   6023 H  HA   . PRO   B 1 136 ? 38.736 -32.972 -0.860  1.00 20.59 ?  136 PRO   B HA   1 
ATOM   6024 H  HB2  . PRO   B 1 136 ? 39.859 -34.402 -2.708  1.00 22.19 ?  136 PRO   B HB2  1 
ATOM   6025 H  HB3  . PRO   B 1 136 ? 40.682 -33.793 -1.483  1.00 22.19 ?  136 PRO   B HB3  1 
ATOM   6026 H  HG2  . PRO   B 1 136 ? 39.672 -36.408 -1.731  1.00 23.68 ?  136 PRO   B HG2  1 
ATOM   6027 H  HG3  . PRO   B 1 136 ? 41.114 -35.978 -1.198  1.00 23.68 ?  136 PRO   B HG3  1 
ATOM   6028 H  HD2  . PRO   B 1 136 ? 39.280 -36.590 0.457   1.00 22.97 ?  136 PRO   B HD2  1 
ATOM   6029 H  HD3  . PRO   B 1 136 ? 40.324 -35.428 0.822   1.00 22.97 ?  136 PRO   B HD3  1 
ATOM   6030 N  N    . ILE   B 1 137 ? 36.795 -35.229 -2.011  1.00 17.22 ?  137 ILE   B N    1 
ATOM   6031 C  CA   . ILE   B 1 137 ? 35.574 -35.395 -2.797  1.00 17.33 ?  137 ILE   B CA   1 
ATOM   6032 C  C    . ILE   B 1 137 ? 34.502 -34.424 -2.318  1.00 16.97 ?  137 ILE   B C    1 
ATOM   6033 O  O    . ILE   B 1 137 ? 33.789 -33.806 -3.120  1.00 16.49 ?  137 ILE   B O    1 
ATOM   6034 C  CB   . ILE   B 1 137 ? 35.096 -36.861 -2.730  1.00 19.38 ?  137 ILE   B CB   1 
ATOM   6035 C  CG1  . ILE   B 1 137 ? 36.118 -37.777 -3.409  1.00 21.76 ?  137 ILE   B CG1  1 
ATOM   6036 C  CG2  . ILE   B 1 137 ? 33.706 -37.003 -3.355  1.00 19.65 ?  137 ILE   B CG2  1 
ATOM   6037 C  CD1  . ILE   B 1 137 ? 35.799 -39.256 -3.297  1.00 23.88 ?  137 ILE   B CD1  1 
ATOM   6038 H  H    . ILE   B 1 137 ? 37.035 -35.931 -1.575  1.00 20.67 ?  137 ILE   B H    1 
ATOM   6039 H  HA   . ILE   B 1 137 ? 35.768 -35.193 -3.729  1.00 20.81 ?  137 ILE   B HA   1 
ATOM   6040 H  HB   . ILE   B 1 137 ? 35.032 -37.117 -1.802  1.00 23.26 ?  137 ILE   B HB   1 
ATOM   6041 H  HG12 . ILE   B 1 137 ? 36.162 -37.561 -4.353  1.00 26.13 ?  137 ILE   B HG12 1 
ATOM   6042 H  HG13 . ILE   B 1 137 ? 36.986 -37.637 -3.000  1.00 26.13 ?  137 ILE   B HG13 1 
ATOM   6043 H  HG21 . ILE   B 1 137 ? 33.474 -37.945 -3.427  1.00 23.59 ?  137 ILE   B HG21 1 
ATOM   6044 H  HG22 . ILE   B 1 137 ? 33.051 -36.559 -2.792  1.00 23.59 ?  137 ILE   B HG22 1 
ATOM   6045 H  HG23 . ILE   B 1 137 ? 33.707 -36.602 -4.239  1.00 23.59 ?  137 ILE   B HG23 1 
ATOM   6046 H  HD11 . ILE   B 1 137 ? 36.537 -39.761 -3.672  1.00 28.67 ?  137 ILE   B HD11 1 
ATOM   6047 H  HD12 . ILE   B 1 137 ? 35.681 -39.489 -2.362  1.00 28.67 ?  137 ILE   B HD12 1 
ATOM   6048 H  HD13 . ILE   B 1 137 ? 34.988 -39.452 -3.792  1.00 28.67 ?  137 ILE   B HD13 1 
ATOM   6049 N  N    . HIS   B 1 138 ? 34.371 -34.276 -1.003  1.00 17.33 ?  138 HIS   B N    1 
ATOM   6050 C  CA   . HIS   B 1 138 ? 33.426 -33.306 -0.467  1.00 17.77 ?  138 HIS   B CA   1 
ATOM   6051 C  C    . HIS   B 1 138 ? 33.843 -31.877 -0.799  1.00 16.85 ?  138 HIS   B C    1 
ATOM   6052 O  O    . HIS   B 1 138 ? 32.996 -31.034 -1.113  1.00 17.18 ?  138 HIS   B O    1 
ATOM   6053 C  CB   . HIS   B 1 138 ? 33.319 -33.474 1.041   1.00 19.09 ?  138 HIS   B CB   1 
ATOM   6054 C  CG   . HIS   B 1 138 ? 32.394 -32.489 1.677   1.00 20.47 ?  138 HIS   B CG   1 
ATOM   6055 N  ND1  . HIS   B 1 138 ? 31.055 -32.415 1.356   1.00 21.64 ?  138 HIS   B ND1  1 
ATOM   6056 C  CD2  . HIS   B 1 138 ? 32.620 -31.509 2.582   1.00 21.22 ?  138 HIS   B CD2  1 
ATOM   6057 C  CE1  . HIS   B 1 138 ? 30.491 -31.448 2.055   1.00 21.83 ?  138 HIS   B CE1  1 
ATOM   6058 N  NE2  . HIS   B 1 138 ? 31.418 -30.885 2.810   1.00 21.29 ?  138 HIS   B NE2  1 
ATOM   6059 H  H    . HIS   B 1 138 ? 34.816 -34.718 -0.415  1.00 20.80 ?  138 HIS   B H    1 
ATOM   6060 H  HA   . HIS   B 1 138 ? 32.553 -33.472 -0.856  1.00 21.34 ?  138 HIS   B HA   1 
ATOM   6061 H  HB2  . HIS   B 1 138 ? 32.984 -34.364 1.236   1.00 22.91 ?  138 HIS   B HB2  1 
ATOM   6062 H  HB3  . HIS   B 1 138 ? 34.195 -33.356 1.435   1.00 22.91 ?  138 HIS   B HB3  1 
ATOM   6063 H  HD1  . HIS   B 1 138 ? 30.648 -32.929 0.795   1.00 25.98 ?  138 HIS   B HD1  1 
ATOM   6064 H  HD2  . HIS   B 1 138 ? 33.423 -31.311 2.995   1.00 25.48 ?  138 HIS   B HD2  1 
ATOM   6065 H  HE1  . HIS   B 1 138 ? 29.587 -31.214 2.027   1.00 26.20 ?  138 HIS   B HE1  1 
ATOM   6066 N  N    . SER   B 1 139 ? 35.137 -31.576 -0.719  1.00 16.33 ?  139 SER   B N    1 
ATOM   6067 C  CA   . SER   B 1 139 ? 35.579 -30.229 -1.047  1.00 15.41 ?  139 SER   B CA   1 
ATOM   6068 C  C    . SER   B 1 139 ? 35.242 -29.885 -2.487  1.00 14.55 ?  139 SER   B C    1 
ATOM   6069 O  O    . SER   B 1 139 ? 34.788 -28.772 -2.770  1.00 14.38 ?  139 SER   B O    1 
ATOM   6070 C  CB   . SER   B 1 139 ? 37.073 -30.089 -0.782  1.00 15.67 ?  139 SER   B CB   1 
ATOM   6071 O  OG   . SER   B 1 139 ? 37.479 -28.759 -1.042  1.00 15.68 ?  139 SER   B OG   1 
ATOM   6072 H  H    . SER   B 1 139 ? 35.758 -32.120 -0.494  1.00 19.61 ?  139 SER   B H    1 
ATOM   6073 H  HA   . SER   B 1 139 ? 35.106 -29.601 -0.486  1.00 18.50 ?  139 SER   B HA   1 
ATOM   6074 H  HB2  . SER   B 1 139 ? 37.245 -30.298 0.148   1.00 18.81 ?  139 SER   B HB2  1 
ATOM   6075 H  HB3  . SER   B 1 139 ? 37.560 -30.692 -1.361  1.00 18.81 ?  139 SER   B HB3  1 
ATOM   6076 H  HG   . SER   B 1 139 ? 38.303 -28.676 -0.894  1.00 18.83 ?  139 SER   B HG   1 
ATOM   6077 N  N    . LEU   B 1 140 ? 35.432 -30.834 -3.408  1.00 14.03 ?  140 LEU   B N    1 
ATOM   6078 C  CA   . LEU   B 1 140 ? 35.065 -30.589 -4.794  1.00 14.22 ?  140 LEU   B CA   1 
ATOM   6079 C  C    . LEU   B 1 140 ? 33.564 -30.360 -4.925  1.00 14.47 ?  140 LEU   B C    1 
ATOM   6080 O  O    . LEU   B 1 140 ? 33.130 -29.473 -5.665  1.00 14.31 ?  140 LEU   B O    1 
ATOM   6081 C  CB   . LEU   B 1 140 ? 35.529 -31.756 -5.667  1.00 14.46 ?  140 LEU   B CB   1 
ATOM   6082 C  CG   . LEU   B 1 140 ? 35.166 -31.650 -7.143  1.00 14.83 ?  140 LEU   B CG   1 
ATOM   6083 C  CD1  . LEU   B 1 140 ? 35.734 -30.378 -7.744  1.00 15.61 ?  140 LEU   B CD1  1 
ATOM   6084 C  CD2  . LEU   B 1 140 ? 35.657 -32.884 -7.875  1.00 16.08 ?  140 LEU   B CD2  1 
ATOM   6085 H  H    . LEU   B 1 140 ? 35.763 -31.613 -3.260  1.00 16.85 ?  140 LEU   B H    1 
ATOM   6086 H  HA   . LEU   B 1 140 ? 35.519 -29.792 -5.108  1.00 17.07 ?  140 LEU   B HA   1 
ATOM   6087 H  HB2  . LEU   B 1 140 ? 36.495 -31.825 -5.614  1.00 17.36 ?  140 LEU   B HB2  1 
ATOM   6088 H  HB3  . LEU   B 1 140 ? 35.127 -32.576 -5.335  1.00 17.36 ?  140 LEU   B HB3  1 
ATOM   6089 H  HG   . LEU   B 1 140 ? 34.201 -31.611 -7.231  1.00 17.81 ?  140 LEU   B HG   1 
ATOM   6090 H  HD11 . LEU   B 1 140 ? 35.625 -30.409 -8.705  1.00 18.75 ?  140 LEU   B HD11 1 
ATOM   6091 H  HD12 . LEU   B 1 140 ? 35.257 -29.614 -7.381  1.00 18.75 ?  140 LEU   B HD12 1 
ATOM   6092 H  HD13 . LEU   B 1 140 ? 36.676 -30.317 -7.518  1.00 18.75 ?  140 LEU   B HD13 1 
ATOM   6093 H  HD21 . LEU   B 1 140 ? 35.419 -32.805 -8.812  1.00 19.30 ?  140 LEU   B HD21 1 
ATOM   6094 H  HD22 . LEU   B 1 140 ? 36.616 -32.946 -7.776  1.00 19.30 ?  140 LEU   B HD22 1 
ATOM   6095 H  HD23 . LEU   B 1 140 ? 35.227 -33.663 -7.489  1.00 19.30 ?  140 LEU   B HD23 1 
ATOM   6096 N  N    . ARG   B 1 141 ? 32.760 -31.148 -4.206  1.00 14.90 ?  141 ARG   B N    1 
ATOM   6097 C  CA   . ARG   B 1 141 ? 31.310 -30.972 -4.191  1.00 15.72 ?  141 ARG   B CA   1 
ATOM   6098 C  C    . ARG   B 1 141 ? 30.931 -29.562 -3.768  1.00 15.26 ?  141 ARG   B C    1 
ATOM   6099 O  O    . ARG   B 1 141 ? 30.128 -28.890 -4.430  1.00 15.35 ?  141 ARG   B O    1 
ATOM   6100 C  CB   . ARG   B 1 141 ? 30.723 -31.995 -3.212  1.00 17.11 ?  141 ARG   B CB   1 
ATOM   6101 C  CG   . ARG   B 1 141 ? 29.255 -31.876 -2.897  1.00 18.48 ?  141 ARG   B CG   1 
ATOM   6102 C  CD   . ARG   B 1 141 ? 28.463 -32.517 -3.964  1.00 19.93 ?  141 ARG   B CD   1 
ATOM   6103 N  NE   . ARG   B 1 141 ? 28.207 -31.609 -5.071  1.00 20.40 ?  141 ARG   B NE   1 
ATOM   6104 C  CZ   . ARG   B 1 141 ? 28.203 -31.963 -6.348  1.00 19.93 ?  141 ARG   B CZ   1 
ATOM   6105 N  NH1  . ARG   B 1 141 ? 28.614 -33.161 -6.736  1.00 19.73 ?  141 ARG   B NH1  1 
ATOM   6106 N  NH2  . ARG   B 1 141 ? 27.766 -31.099 -7.258  1.00 20.89 ?  141 ARG   B NH2  1 
ATOM   6107 H  H    . ARG   B 1 141 ? 33.040 -31.789 -3.713  1.00 17.89 ?  141 ARG   B H    1 
ATOM   6108 H  HA   . ARG   B 1 141 ? 30.950 -31.135 -5.074  1.00 18.87 ?  141 ARG   B HA   1 
ATOM   6109 H  HB2  . ARG   B 1 141 ? 30.880 -32.880 -3.576  1.00 20.54 ?  141 ARG   B HB2  1 
ATOM   6110 H  HB3  . ARG   B 1 141 ? 31.201 -31.913 -2.374  1.00 20.54 ?  141 ARG   B HB3  1 
ATOM   6111 H  HG2  . ARG   B 1 141 ? 29.074 -32.320 -2.058  1.00 22.19 ?  141 ARG   B HG2  1 
ATOM   6112 H  HG3  . ARG   B 1 141 ? 28.999 -30.936 -2.839  1.00 22.19 ?  141 ARG   B HG3  1 
ATOM   6113 H  HD2  . ARG   B 1 141 ? 28.947 -33.293 -4.295  1.00 23.92 ?  141 ARG   B HD2  1 
ATOM   6114 H  HD3  . ARG   B 1 141 ? 27.617 -32.800 -3.593  1.00 23.92 ?  141 ARG   B HD3  1 
ATOM   6115 H  HE   . ARG   B 1 141 ? 28.027 -30.790 -4.881  1.00 24.49 ?  141 ARG   B HE   1 
ATOM   6116 H  HH11 . ARG   B 1 141 ? 28.887 -33.740 -6.160  1.00 23.69 ?  141 ARG   B HH11 1 
ATOM   6117 H  HH12 . ARG   B 1 141 ? 28.614 -33.364 -7.570  1.00 23.69 ?  141 ARG   B HH12 1 
ATOM   6118 H  HH21 . ARG   B 1 141 ? 27.508 -30.314 -7.017  1.00 25.08 ?  141 ARG   B HH21 1 
ATOM   6119 H  HH22 . ARG   B 1 141 ? 27.784 -31.307 -8.092  1.00 25.08 ?  141 ARG   B HH22 1 
ATOM   6120 N  N    . VAL   B 1 142 ? 31.475 -29.110 -2.642  1.00 14.92 ?  142 VAL   B N    1 
ATOM   6121 C  CA   . VAL   B 1 142 ? 31.142 -27.777 -2.163  1.00 14.80 ?  142 VAL   B CA   1 
ATOM   6122 C  C    . VAL   B 1 142 ? 31.620 -26.725 -3.155  1.00 14.56 ?  142 VAL   B C    1 
ATOM   6123 O  O    . VAL   B 1 142 ? 30.921 -25.741 -3.418  1.00 14.93 ?  142 VAL   B O    1 
ATOM   6124 C  CB   . VAL   B 1 142 ? 31.694 -27.549 -0.744  1.00 15.72 ?  142 VAL   B CB   1 
ATOM   6125 C  CG1  . VAL   B 1 142 ? 31.381 -26.130 -0.271  1.00 15.51 ?  142 VAL   B CG1  1 
ATOM   6126 C  CG2  . VAL   B 1 142 ? 31.109 -28.570 0.214   1.00 16.55 ?  142 VAL   B CG2  1 
ATOM   6127 H  H    . VAL   B 1 142 ? 32.034 -29.542 -2.149  1.00 17.91 ?  142 VAL   B H    1 
ATOM   6128 H  HA   . VAL   B 1 142 ? 30.183 -27.700 -2.110  1.00 17.77 ?  142 VAL   B HA   1 
ATOM   6129 H  HB   . VAL   B 1 142 ? 32.660 -27.658 -0.750  1.00 18.87 ?  142 VAL   B HB   1 
ATOM   6130 H  HG11 . VAL   B 1 142 ? 31.571 -26.063 0.677   1.00 18.62 ?  142 VAL   B HG11 1 
ATOM   6131 H  HG12 . VAL   B 1 142 ? 31.937 -25.500 -0.761  1.00 18.62 ?  142 VAL   B HG12 1 
ATOM   6132 H  HG13 . VAL   B 1 142 ? 30.445 -25.941 -0.436  1.00 18.62 ?  142 VAL   B HG13 1 
ATOM   6133 H  HG21 . VAL   B 1 142 ? 31.420 -28.378 1.110   1.00 19.87 ?  142 VAL   B HG21 1 
ATOM   6134 H  HG22 . VAL   B 1 142 ? 30.141 -28.514 0.178   1.00 19.87 ?  142 VAL   B HG22 1 
ATOM   6135 H  HG23 . VAL   B 1 142 ? 31.398 -29.456 -0.056  1.00 19.87 ?  142 VAL   B HG23 1 
ATOM   6136 N  N    . CYS   B 1 143 ? 32.804 -26.921 -3.733  1.00 14.01 ?  143 CYS   B N    1 
ATOM   6137 C  CA   . CYS   B 1 143 ? 33.300 -25.985 -4.738  1.00 13.81 ?  143 CYS   B CA   1 
ATOM   6138 C  C    . CYS   B 1 143 ? 32.299 -25.842 -5.878  1.00 13.77 ?  143 CYS   B C    1 
ATOM   6139 O  O    . CYS   B 1 143 ? 31.893 -24.731 -6.240  1.00 14.05 ?  143 CYS   B O    1 
ATOM   6140 C  CB   . CYS   B 1 143 ? 34.657 -26.470 -5.259  1.00 14.20 ?  143 CYS   B CB   1 
ATOM   6141 S  SG   . CYS   B 1 143 ? 35.403 -25.377 -6.487  1.00 14.47 ?  143 CYS   B SG   1 
ATOM   6142 H  H    . CYS   B 1 143 ? 33.340 -27.565 -3.555  1.00 16.82 ?  143 CYS   B H    1 
ATOM   6143 H  HA   . CYS   B 1 143 ? 33.432 -25.109 -4.339  1.00 16.58 ?  143 CYS   B HA   1 
ATOM   6144 H  HB2  . CYS   B 1 143 ? 35.283 -26.539 -4.518  1.00 17.05 ?  143 CYS   B HB2  1 
ATOM   6145 H  HB3  . CYS   B 1 143 ? 34.548 -27.338 -5.669  1.00 17.05 ?  143 CYS   B HB3  1 
ATOM   6146 H  HG   . CYS   B 1 143 ? 36.484 -25.808 -6.801  1.00 17.37 ?  143 CYS   B HG   1 
ATOM   6147 N  N    . VAL   B 1 144 ? 31.890 -26.965 -6.458  1.00 14.65 ?  144 VAL   B N    1 
ATOM   6148 C  CA   . VAL   B 1 144 ? 30.984 -26.919 -7.599  1.00 15.73 ?  144 VAL   B CA   1 
ATOM   6149 C  C    . VAL   B 1 144 ? 29.647 -26.292 -7.223  1.00 15.80 ?  144 VAL   B C    1 
ATOM   6150 O  O    . VAL   B 1 144 ? 29.032 -25.584 -8.030  1.00 16.91 ?  144 VAL   B O    1 
ATOM   6151 C  CB   . VAL   B 1 144 ? 30.817 -28.337 -8.158  1.00 17.85 ?  144 VAL   B CB   1 
ATOM   6152 C  CG1  . VAL   B 1 144 ? 29.537 -28.474 -8.972  1.00 20.13 ?  144 VAL   B CG1  1 
ATOM   6153 C  CG2  . VAL   B 1 144 ? 32.051 -28.733 -8.963  1.00 18.03 ?  144 VAL   B CG2  1 
ATOM   6154 H  H    . VAL   B 1 144 ? 32.127 -27.757 -6.224  1.00 17.59 ?  144 VAL   B H    1 
ATOM   6155 H  HA   . VAL   B 1 144 ? 31.371 -26.371 -8.298  1.00 18.89 ?  144 VAL   B HA   1 
ATOM   6156 H  HB   . VAL   B 1 144 ? 30.752 -28.957 -7.411  1.00 21.43 ?  144 VAL   B HB   1 
ATOM   6157 H  HG11 . VAL   B 1 144 ? 29.603 -29.272 -9.524  1.00 24.17 ?  144 VAL   B HG11 1 
ATOM   6158 H  HG12 . VAL   B 1 144 ? 28.784 -28.560 -8.367  1.00 24.17 ?  144 VAL   B HG12 1 
ATOM   6159 H  HG13 . VAL   B 1 144 ? 29.433 -27.695 -9.533  1.00 24.17 ?  144 VAL   B HG13 1 
ATOM   6160 H  HG21 . VAL   B 1 144 ? 31.934 -29.635 -9.300  1.00 21.64 ?  144 VAL   B HG21 1 
ATOM   6161 H  HG22 . VAL   B 1 144 ? 32.151 -28.114 -9.706  1.00 21.64 ?  144 VAL   B HG22 1 
ATOM   6162 H  HG23 . VAL   B 1 144 ? 32.830 -28.690 -8.390  1.00 21.64 ?  144 VAL   B HG23 1 
ATOM   6163 N  N    . ASP   B 1 145 ? 29.174 -26.540 -6.008  1.00 15.77 ?  145 ASP   B N    1 
ATOM   6164 C  CA   . ASP   B 1 145 ? 27.867 -26.062 -5.580  1.00 16.63 ?  145 ASP   B CA   1 
ATOM   6165 C  C    . ASP   B 1 145 ? 27.899 -24.637 -5.042  1.00 16.22 ?  145 ASP   B C    1 
ATOM   6166 O  O    . ASP   B 1 145 ? 26.842 -24.099 -4.697  1.00 18.02 ?  145 ASP   B O    1 
ATOM   6167 C  CB   . ASP   B 1 145 ? 27.278 -26.982 -4.499  1.00 18.62 ?  145 ASP   B CB   1 
ATOM   6168 C  CG   . ASP   B 1 145 ? 26.922 -28.363 -5.012  1.00 20.35 ?  145 ASP   B CG   1 
ATOM   6169 O  OD1  . ASP   B 1 145 ? 26.818 -28.549 -6.238  1.00 20.44 ?  145 ASP   B OD1  1 
ATOM   6170 O  OD2  . ASP   B 1 145 ? 26.746 -29.256 -4.162  1.00 22.17 -1 145 ASP   B OD2  1 
ATOM   6171 H  H    . ASP   B 1 145 ? 29.603 -26.967 -5.402  1.00 18.94 ?  145 ASP   B H    1 
ATOM   6172 H  HA   . ASP   B 1 145 ? 27.270 -26.057 -6.339  1.00 19.97 ?  145 ASP   B HA   1 
ATOM   6173 H  HB2  . ASP   B 1 145 ? 27.924 -27.090 -3.793  1.00 22.35 ?  145 ASP   B HB2  1 
ATOM   6174 H  HB3  . ASP   B 1 145 ? 26.466 -26.575 -4.156  1.00 22.35 ?  145 ASP   B HB3  1 
ATOM   6175 N  N    . THR   B 1 146 ? 29.077 -24.022 -4.945  1.00 14.25 ?  146 THR   B N    1 
ATOM   6176 C  CA   . THR   B 1 146 ? 29.214 -22.701 -4.340  1.00 13.82 ?  146 THR   B CA   1 
ATOM   6177 C  C    . THR   B 1 146 ? 29.844 -21.675 -5.263  1.00 13.99 ?  146 THR   B C    1 
ATOM   6178 O  O    . THR   B 1 146 ? 29.388 -20.519 -5.315  1.00 13.94 ?  146 THR   B O    1 
ATOM   6179 C  CB   . THR   B 1 146 ? 30.048 -22.803 -3.056  1.00 14.17 ?  146 THR   B CB   1 
ATOM   6180 O  OG1  . THR   B 1 146 ? 29.464 -23.786 -2.195  1.00 14.29 ?  146 THR   B OG1  1 
ATOM   6181 C  CG2  . THR   B 1 146 ? 30.115 -21.461 -2.339  1.00 14.48 ?  146 THR   B CG2  1 
ATOM   6182 H  H    . THR   B 1 146 ? 29.825 -24.344 -5.230  1.00 17.11 ?  146 THR   B H    1 
ATOM   6183 H  HA   . THR   B 1 146 ? 28.341 -22.367 -4.095  1.00 16.60 ?  146 THR   B HA   1 
ATOM   6184 H  HB   . THR   B 1 146 ? 30.955 -23.061 -3.281  1.00 17.02 ?  146 THR   B HB   1 
ATOM   6185 H  HG1  . THR   B 1 146 ? 29.501 -24.546 -2.567  1.00 17.15 ?  146 THR   B HG1  1 
ATOM   6186 H  HG21 . THR   B 1 146 ? 30.466 -21.578 -1.444  1.00 17.39 ?  146 THR   B HG21 1 
ATOM   6187 H  HG22 . THR   B 1 146 ? 30.701 -20.852 -2.824  1.00 17.39 ?  146 THR   B HG22 1 
ATOM   6188 H  HG23 . THR   B 1 146 ? 29.232 -21.068 -2.284  1.00 17.39 ?  146 THR   B HG23 1 
ATOM   6189 N  N    . VAL   B 1 147 ? 30.906 -22.053 -5.965  1.00 13.77 ?  147 VAL   B N    1 
ATOM   6190 C  CA   . VAL   B 1 147 ? 31.632 -21.114 -6.805  1.00 13.35 ?  147 VAL   B CA   1 
ATOM   6191 C  C    . VAL   B 1 147 ? 30.897 -20.980 -8.125  1.00 13.47 ?  147 VAL   B C    1 
ATOM   6192 O  O    . VAL   B 1 147 ? 30.519 -21.981 -8.748  1.00 14.20 ?  147 VAL   B O    1 
ATOM   6193 C  CB   . VAL   B 1 147 ? 33.083 -21.577 -7.015  1.00 13.52 ?  147 VAL   B CB   1 
ATOM   6194 C  CG1  . VAL   B 1 147 ? 33.844 -20.549 -7.840  1.00 13.47 ?  147 VAL   B CG1  1 
ATOM   6195 C  CG2  . VAL   B 1 147 ? 33.767 -21.791 -5.681  1.00 13.85 ?  147 VAL   B CG2  1 
ATOM   6196 H  H    . VAL   B 1 147 ? 31.226 -22.855 -5.977  1.00 16.53 ?  147 VAL   B H    1 
ATOM   6197 H  HA   . VAL   B 1 147 ? 31.655 -20.248 -6.373  1.00 16.03 ?  147 VAL   B HA   1 
ATOM   6198 H  HB   . VAL   B 1 147 ? 33.090 -22.421 -7.499  1.00 16.23 ?  147 VAL   B HB   1 
ATOM   6199 H  HG11 . VAL   B 1 147 ? 34.787 -20.768 -7.831  1.00 16.17 ?  147 VAL   B HG11 1 
ATOM   6200 H  HG12 . VAL   B 1 147 ? 33.510 -20.559 -8.750  1.00 16.17 ?  147 VAL   B HG12 1 
ATOM   6201 H  HG13 . VAL   B 1 147 ? 33.707 -19.669 -7.447  1.00 16.17 ?  147 VAL   B HG13 1 
ATOM   6202 H  HG21 . VAL   B 1 147 ? 34.707 -21.992 -5.834  1.00 16.63 ?  147 VAL   B HG21 1 
ATOM   6203 H  HG22 . VAL   B 1 147 ? 33.687 -20.983 -5.152  1.00 16.63 ?  147 VAL   B HG22 1 
ATOM   6204 H  HG23 . VAL   B 1 147 ? 33.345 -22.533 -5.220  1.00 16.63 ?  147 VAL   B HG23 1 
ATOM   6205 N  N    . ARG   B 1 148 ? 30.692 -19.734 -8.544  1.00 13.38 ?  148 ARG   B N    1 
ATOM   6206 C  CA   . ARG   B 1 148 ? 30.067 -19.420 -9.816  1.00 13.63 ?  148 ARG   B CA   1 
ATOM   6207 C  C    . ARG   B 1 148 ? 31.020 -18.747 -10.790 1.00 13.78 ?  148 ARG   B C    1 
ATOM   6208 O  O    . ARG   B 1 148 ? 30.729 -18.723 -11.989 1.00 15.38 ?  148 ARG   B O    1 
ATOM   6209 C  CB   . ARG   B 1 148 ? 28.826 -18.538 -9.597  1.00 13.92 ?  148 ARG   B CB   1 
ATOM   6210 C  CG   . ARG   B 1 148 ? 27.750 -19.249 -8.793  1.00 14.64 ?  148 ARG   B CG   1 
ATOM   6211 C  CD   . ARG   B 1 148 ? 26.545 -18.361 -8.491  1.00 15.61 ?  148 ARG   B CD   1 
ATOM   6212 N  NE   . ARG   B 1 148 ? 26.931 -17.161 -7.759  1.00 15.57 ?  148 ARG   B NE   1 
ATOM   6213 C  CZ   . ARG   B 1 148 ? 27.229 -17.126 -6.466  1.00 14.80 ?  148 ARG   B CZ   1 
ATOM   6214 N  NH1  . ARG   B 1 148 ? 27.174 -18.213 -5.711  1.00 15.03 ?  148 ARG   B NH1  1 
ATOM   6215 N  NH2  . ARG   B 1 148 ? 27.619 -15.975 -5.922  1.00 14.65 ?  148 ARG   B NH2  1 
ATOM   6216 H  H    . ARG   B 1 148 ? 30.921 -19.033 -8.093  1.00 16.06 ?  148 ARG   B H    1 
ATOM   6217 H  HA   . ARG   B 1 148 ? 29.771 -20.246 -10.224 1.00 16.36 ?  148 ARG   B HA   1 
ATOM   6218 H  HB2  . ARG   B 1 148 ? 29.087 -17.739 -9.110  1.00 16.72 ?  148 ARG   B HB2  1 
ATOM   6219 H  HB3  . ARG   B 1 148 ? 28.453 -18.298 -10.457 1.00 16.72 ?  148 ARG   B HB3  1 
ATOM   6220 H  HG2  . ARG   B 1 148 ? 27.436 -20.017 -9.299  1.00 17.58 ?  148 ARG   B HG2  1 
ATOM   6221 H  HG3  . ARG   B 1 148 ? 28.125 -19.541 -7.949  1.00 17.58 ?  148 ARG   B HG3  1 
ATOM   6222 H  HD2  . ARG   B 1 148 ? 26.134 -18.090 -9.326  1.00 18.74 ?  148 ARG   B HD2  1 
ATOM   6223 H  HD3  . ARG   B 1 148 ? 25.911 -18.859 -7.951  1.00 18.74 ?  148 ARG   B HD3  1 
ATOM   6224 H  HE   . ARG   B 1 148 ? 26.978 -16.426 -8.198  1.00 18.69 ?  148 ARG   B HE   1 
ATOM   6225 H  HH11 . ARG   B 1 148 ? 26.925 -18.967 -6.048  1.00 18.05 ?  148 ARG   B HH11 1 
ATOM   6226 H  HH12 . ARG   B 1 148 ? 27.371 -18.169 -4.874  1.00 18.05 ?  148 ARG   B HH12 1 
ATOM   6227 H  HH21 . ARG   B 1 148 ? 27.669 -15.267 -6.406  1.00 17.59 ?  148 ARG   B HH21 1 
ATOM   6228 H  HH22 . ARG   B 1 148 ? 27.820 -15.940 -5.087  1.00 17.59 ?  148 ARG   B HH22 1 
ATOM   6229 N  N    . THR   B 1 149 ? 32.127 -18.191 -10.303 1.00 13.27 ?  149 THR   B N    1 
ATOM   6230 C  CA   . THR   B 1 149 ? 33.166 -17.630 -11.149 1.00 13.46 ?  149 THR   B CA   1 
ATOM   6231 C  C    . THR   B 1 149 ? 34.049 -18.771 -11.661 1.00 13.09 ?  149 THR   B C    1 
ATOM   6232 O  O    . THR   B 1 149 ? 33.849 -19.942 -11.327 1.00 13.71 ?  149 THR   B O    1 
ATOM   6233 C  CB   . THR   B 1 149 ? 33.936 -16.576 -10.366 1.00 13.34 ?  149 THR   B CB   1 
ATOM   6234 O  OG1  . THR   B 1 149 ? 34.397 -17.176 -9.154  1.00 13.42 ?  149 THR   B OG1  1 
ATOM   6235 C  CG2  . THR   B 1 149 ? 33.042 -15.370 -10.066 1.00 14.31 ?  149 THR   B CG2  1 
ATOM   6236 H  H    . THR   B 1 149 ? 32.292 -18.122 -9.462  1.00 15.94 ?  149 THR   B H    1 
ATOM   6237 H  HA   . THR   B 1 149 ? 32.753 -17.195 -11.911 1.00 16.17 ?  149 THR   B HA   1 
ATOM   6238 H  HB   . THR   B 1 149 ? 34.694 -16.283 -10.883 1.00 16.02 ?  149 THR   B HB   1 
ATOM   6239 H  HG1  . THR   B 1 149 ? 34.817 -16.605 -8.690  1.00 16.11 ?  149 THR   B HG1  1 
ATOM   6240 H  HG21 . THR   B 1 149 ? 33.547 -14.698 -9.577  1.00 17.18 ?  149 THR   B HG21 1 
ATOM   6241 H  HG22 . THR   B 1 149 ? 32.722 -14.980 -10.894 1.00 17.18 ?  149 THR   B HG22 1 
ATOM   6242 H  HG23 . THR   B 1 149 ? 32.280 -15.640 -9.529  1.00 17.18 ?  149 THR   B HG23 1 
ATOM   6243 N  N    . ASN   B 1 150 ? 35.014 -18.448 -12.508 1.00 13.13 ?  150 ASN   B N    1 
ATOM   6244 C  CA   . ASN   B 1 150 ? 35.778 -19.469 -13.214 1.00 13.58 ?  150 ASN   B CA   1 
ATOM   6245 C  C    . ASN   B 1 150 ? 36.949 -19.923 -12.351 1.00 13.27 ?  150 ASN   B C    1 
ATOM   6246 O  O    . ASN   B 1 150 ? 37.886 -19.158 -12.105 1.00 13.75 ?  150 ASN   B O    1 
ATOM   6247 C  CB   . ASN   B 1 150 ? 36.243 -18.931 -14.560 1.00 15.20 ?  150 ASN   B CB   1 
ATOM   6248 C  CG   . ASN   B 1 150 ? 35.097 -18.721 -15.510 1.00 18.13 ?  150 ASN   B CG   1 
ATOM   6249 O  OD1  . ASN   B 1 150 ? 34.189 -19.542 -15.575 1.00 18.97 ?  150 ASN   B OD1  1 
ATOM   6250 N  ND2  . ASN   B 1 150 ? 35.109 -17.611 -16.231 1.00 20.07 ?  150 ASN   B ND2  1 
ATOM   6251 H  H    . ASN   B 1 150 ? 35.257 -17.638 -12.683 1.00 15.76 ?  150 ASN   B H    1 
ATOM   6252 H  HA   . ASN   B 1 150 ? 35.201 -20.234 -13.378 1.00 16.31 ?  150 ASN   B HA   1 
ATOM   6253 H  HB2  . ASN   B 1 150 ? 36.681 -18.073 -14.423 1.00 18.25 ?  150 ASN   B HB2  1 
ATOM   6254 H  HB3  . ASN   B 1 150 ? 36.856 -19.560 -14.960 1.00 18.25 ?  150 ASN   B HB3  1 
ATOM   6255 H  HD21 . ASN   B 1 150 ? 34.472 -17.447 -16.789 1.00 24.10 ?  150 ASN   B HD21 1 
ATOM   6256 H  HD22 . ASN   B 1 150 ? 35.761 -17.053 -16.155 1.00 24.10 ?  150 ASN   B HD22 1 
ATOM   6257 N  N    . VAL   B 1 151 ? 36.897 -21.167 -11.884 1.00 13.08 ?  151 VAL   B N    1 
ATOM   6258 C  CA   . VAL   B 1 151 ? 37.912 -21.698 -10.990 1.00 12.92 ?  151 VAL   B CA   1 
ATOM   6259 C  C    . VAL   B 1 151 ? 38.616 -22.868 -11.661 1.00 12.84 ?  151 VAL   B C    1 
ATOM   6260 O  O    . VAL   B 1 151 ? 37.973 -23.804 -12.157 1.00 14.00 ?  151 VAL   B O    1 
ATOM   6261 C  CB   . VAL   B 1 151 ? 37.349 -22.040 -9.595  1.00 14.22 ?  151 VAL   B CB   1 
ATOM   6262 C  CG1  . VAL   B 1 151 ? 36.186 -23.034 -9.680  1.00 15.18 ?  151 VAL   B CG1  1 
ATOM   6263 C  CG2  . VAL   B 1 151 ? 38.458 -22.543 -8.679  1.00 14.60 ?  151 VAL   B CG2  1 
ATOM   6264 H  H    . VAL   B 1 151 ? 36.269 -21.730 -12.078 1.00 15.70 ?  151 VAL   B H    1 
ATOM   6265 H  HA   . VAL   B 1 151 ? 38.576 -21.005 -10.853 1.00 15.51 ?  151 VAL   B HA   1 
ATOM   6266 H  HB   . VAL   B 1 151 ? 36.998 -21.226 -9.199  1.00 17.08 ?  151 VAL   B HB   1 
ATOM   6267 H  HG11 . VAL   B 1 151 ? 35.863 -23.222 -8.783  1.00 18.23 ?  151 VAL   B HG11 1 
ATOM   6268 H  HG12 . VAL   B 1 151 ? 35.471 -22.644 -10.210 1.00 18.23 ?  151 VAL   B HG12 1 
ATOM   6269 H  HG13 . VAL   B 1 151 ? 36.496 -23.853 -10.096 1.00 18.23 ?  151 VAL   B HG13 1 
ATOM   6270 H  HG21 . VAL   B 1 151 ? 38.109 -22.617 -7.774  1.00 17.53 ?  151 VAL   B HG21 1 
ATOM   6271 H  HG22 . VAL   B 1 151 ? 38.757 -23.412 -8.988  1.00 17.53 ?  151 VAL   B HG22 1 
ATOM   6272 H  HG23 . VAL   B 1 151 ? 39.193 -21.911 -8.696  1.00 17.53 ?  151 VAL   B HG23 1 
ATOM   6273 N  N    . TYR   B 1 152 ? 39.946 -22.782 -11.683 1.00 12.46 ?  152 TYR   B N    1 
ATOM   6274 C  CA   . TYR   B 1 152 ? 40.847 -23.773 -12.257 1.00 12.64 ?  152 TYR   B CA   1 
ATOM   6275 C  C    . TYR   B 1 152 ? 41.570 -24.449 -11.096 1.00 11.79 ?  152 TYR   B C    1 
ATOM   6276 O  O    . TYR   B 1 152 ? 42.416 -23.833 -10.442 1.00 12.39 ?  152 TYR   B O    1 
ATOM   6277 C  CB   . TYR   B 1 152 ? 41.816 -23.077 -13.215 1.00 13.47 ?  152 TYR   B CB   1 
ATOM   6278 C  CG   . TYR   B 1 152 ? 41.131 -22.605 -14.477 1.00 14.05 ?  152 TYR   B CG   1 
ATOM   6279 C  CD1  . TYR   B 1 152 ? 40.473 -21.381 -14.531 1.00 14.58 ?  152 TYR   B CD1  1 
ATOM   6280 C  CD2  . TYR   B 1 152 ? 41.115 -23.406 -15.608 1.00 15.22 ?  152 TYR   B CD2  1 
ATOM   6281 C  CE1  . TYR   B 1 152 ? 39.833 -20.968 -15.684 1.00 16.04 ?  152 TYR   B CE1  1 
ATOM   6282 C  CE2  . TYR   B 1 152 ? 40.478 -23.006 -16.762 1.00 16.26 ?  152 TYR   B CE2  1 
ATOM   6283 C  CZ   . TYR   B 1 152 ? 39.839 -21.785 -16.797 1.00 16.72 ?  152 TYR   B CZ   1 
ATOM   6284 O  OH   . TYR   B 1 152 ? 39.209 -21.399 -17.953 1.00 19.42 ?  152 TYR   B OH   1 
ATOM   6285 H  H    . TYR   B 1 152 ? 40.378 -22.112 -11.346 1.00 14.97 ?  152 TYR   B H    1 
ATOM   6286 H  HA   . TYR   B 1 152 ? 40.335 -24.441 -12.743 1.00 15.17 ?  152 TYR   B HA   1 
ATOM   6287 H  HB2  . TYR   B 1 152 ? 42.197 -22.307 -12.768 1.00 16.17 ?  152 TYR   B HB2  1 
ATOM   6288 H  HB3  . TYR   B 1 152 ? 42.516 -23.701 -13.462 1.00 16.17 ?  152 TYR   B HB3  1 
ATOM   6289 H  HD1  . TYR   B 1 152 ? 40.463 -20.828 -13.780 1.00 17.51 ?  152 TYR   B HD1  1 
ATOM   6290 H  HD2  . TYR   B 1 152 ? 41.541 -24.234 -15.586 1.00 18.27 ?  152 TYR   B HD2  1 
ATOM   6291 H  HE1  . TYR   B 1 152 ? 39.401 -20.145 -15.713 1.00 19.26 ?  152 TYR   B HE1  1 
ATOM   6292 H  HE2  . TYR   B 1 152 ? 40.484 -23.556 -17.514 1.00 19.52 ?  152 TYR   B HE2  1 
ATOM   6293 H  HH   . TYR   B 1 152 ? 38.863 -20.638 -17.849 1.00 23.31 ?  152 TYR   B HH   1 
ATOM   6294 N  N    . LEU   B 1 153 ? 41.197 -25.699 -10.817 1.00 12.19 ?  153 LEU   B N    1 
ATOM   6295 C  CA   . LEU   B 1 153 ? 41.709 -26.450 -9.679  1.00 11.92 ?  153 LEU   B CA   1 
ATOM   6296 C  C    . LEU   B 1 153 ? 42.938 -27.250 -10.079 1.00 12.33 ?  153 LEU   B C    1 
ATOM   6297 O  O    . LEU   B 1 153 ? 42.913 -27.980 -11.073 1.00 13.48 ?  153 LEU   B O    1 
ATOM   6298 C  CB   . LEU   B 1 153 ? 40.631 -27.409 -9.165  1.00 12.39 ?  153 LEU   B CB   1 
ATOM   6299 C  CG   . LEU   B 1 153 ? 39.371 -26.748 -8.599  1.00 13.42 ?  153 LEU   B CG   1 
ATOM   6300 C  CD1  . LEU   B 1 153 ? 38.267 -27.771 -8.433  1.00 14.03 ?  153 LEU   B CD1  1 
ATOM   6301 C  CD2  . LEU   B 1 153 ? 39.667 -26.069 -7.272  1.00 13.80 ?  153 LEU   B CD2  1 
ATOM   6302 H  H    . LEU   B 1 153 ? 40.617 -26.142 -11.281 1.00 14.63 ?  153 LEU   B H    1 
ATOM   6303 H  HA   . LEU   B 1 153 ? 41.939 -25.835 -8.965  1.00 14.31 ?  153 LEU   B HA   1 
ATOM   6304 H  HB2  . LEU   B 1 153 ? 40.353 -27.984 -9.891  1.00 14.88 ?  153 LEU   B HB2  1 
ATOM   6305 H  HB3  . LEU   B 1 153 ? 41.012 -27.948 -8.451  1.00 14.88 ?  153 LEU   B HB3  1 
ATOM   6306 H  HG   . LEU   B 1 153 ? 39.056 -26.068 -9.219  1.00 16.11 ?  153 LEU   B HG   1 
ATOM   6307 H  HD11 . LEU   B 1 153 ? 37.456 -27.316 -8.144  1.00 16.85 ?  153 LEU   B HD11 1 
ATOM   6308 H  HD12 . LEU   B 1 153 ? 38.114 -28.207 -9.281  1.00 16.85 ?  153 LEU   B HD12 1 
ATOM   6309 H  HD13 . LEU   B 1 153 ? 38.537 -28.416 -7.765  1.00 16.85 ?  153 LEU   B HD13 1 
ATOM   6310 H  HD21 . LEU   B 1 153 ? 38.847 -25.698 -6.909  1.00 16.57 ?  153 LEU   B HD21 1 
ATOM   6311 H  HD22 . LEU   B 1 153 ? 40.033 -26.724 -6.657  1.00 16.57 ?  153 LEU   B HD22 1 
ATOM   6312 H  HD23 . LEU   B 1 153 ? 40.313 -25.358 -7.418  1.00 16.57 ?  153 LEU   B HD23 1 
ATOM   6313 N  N    . ALA   B 1 154 ? 43.994 -27.140 -9.281  1.00 12.41 ?  154 ALA   B N    1 
ATOM   6314 C  CA   . ALA   B 1 154 ? 45.221 -27.903 -9.469  1.00 13.57 ?  154 ALA   B CA   1 
ATOM   6315 C  C    . ALA   B 1 154 ? 45.281 -28.974 -8.391  1.00 14.34 ?  154 ALA   B C    1 
ATOM   6316 O  O    . ALA   B 1 154 ? 45.215 -28.665 -7.194  1.00 15.30 ?  154 ALA   B O    1 
ATOM   6317 C  CB   . ALA   B 1 154 ? 46.446 -26.994 -9.400  1.00 14.49 ?  154 ALA   B CB   1 
ATOM   6318 H  H    . ALA   B 1 154 ? 44.022 -26.607 -8.603  1.00 14.91 ?  154 ALA   B H    1 
ATOM   6319 H  HA   . ALA   B 1 154 ? 45.202 -28.332 -10.338 1.00 16.29 ?  154 ALA   B HA   1 
ATOM   6320 H  HB1  . ALA   B 1 154 ? 47.243 -27.531 -9.529  1.00 17.39 ?  154 ALA   B HB1  1 
ATOM   6321 H  HB2  . ALA   B 1 154 ? 46.384 -26.322 -10.098 1.00 17.39 ?  154 ALA   B HB2  1 
ATOM   6322 H  HB3  . ALA   B 1 154 ? 46.474 -26.565 -8.530  1.00 17.39 ?  154 ALA   B HB3  1 
ATOM   6323 N  N    . VAL   B 1 155 ? 45.393 -30.225 -8.818  1.00 13.80 ?  155 VAL   B N    1 
ATOM   6324 C  CA   . VAL   B 1 155 ? 45.501 -31.371 -7.924  1.00 14.12 ?  155 VAL   B CA   1 
ATOM   6325 C  C    . VAL   B 1 155 ? 46.839 -32.043 -8.209  1.00 13.92 ?  155 VAL   B C    1 
ATOM   6326 O  O    . VAL   B 1 155 ? 47.070 -32.536 -9.320  1.00 16.05 ?  155 VAL   B O    1 
ATOM   6327 C  CB   . VAL   B 1 155 ? 44.339 -32.360 -8.115  1.00 15.40 ?  155 VAL   B CB   1 
ATOM   6328 C  CG1  . VAL   B 1 155 ? 44.513 -33.558 -7.202  1.00 15.59 ?  155 VAL   B CG1  1 
ATOM   6329 C  CG2  . VAL   B 1 155 ? 43.012 -31.666 -7.850  1.00 16.06 ?  155 VAL   B CG2  1 
ATOM   6330 H  H    . VAL   B 1 155 ? 45.415 -30.446 -9.653  1.00 16.57 ?  155 VAL   B H    1 
ATOM   6331 H  HA   . VAL   B 1 155 ? 45.497 -31.068 -7.003  1.00 16.96 ?  155 VAL   B HA   1 
ATOM   6332 H  HB   . VAL   B 1 155 ? 44.336 -32.672 -9.034  1.00 18.49 ?  155 VAL   B HB   1 
ATOM   6333 H  HG11 . VAL   B 1 155 ? 43.684 -34.062 -7.179  1.00 18.72 ?  155 VAL   B HG11 1 
ATOM   6334 H  HG12 . VAL   B 1 155 ? 45.228 -34.120 -7.543  1.00 18.72 ?  155 VAL   B HG12 1 
ATOM   6335 H  HG13 . VAL   B 1 155 ? 44.734 -33.248 -6.309  1.00 18.72 ?  155 VAL   B HG13 1 
ATOM   6336 H  HG21 . VAL   B 1 155 ? 42.295 -32.316 -7.930  1.00 19.29 ?  155 VAL   B HG21 1 
ATOM   6337 H  HG22 . VAL   B 1 155 ? 43.023 -31.297 -6.952  1.00 19.29 ?  155 VAL   B HG22 1 
ATOM   6338 H  HG23 . VAL   B 1 155 ? 42.888 -30.956 -8.498  1.00 19.29 ?  155 VAL   B HG23 1 
ATOM   6339 N  N    . PHE   B 1 156 ? 47.704 -32.087 -7.197  1.00 14.35 ?  156 PHE   B N    1 
ATOM   6340 C  CA   . PHE   B 1 156 ? 49.080 -32.545 -7.402  1.00 15.71 ?  156 PHE   B CA   1 
ATOM   6341 C  C    . PHE   B 1 156 ? 49.170 -34.046 -7.679  1.00 16.81 ?  156 PHE   B C    1 
ATOM   6342 O  O    . PHE   B 1 156 ? 49.877 -34.479 -8.600  1.00 18.93 ?  156 PHE   B O    1 
ATOM   6343 C  CB   . PHE   B 1 156 ? 49.917 -32.175 -6.179  1.00 15.58 ?  156 PHE   B CB   1 
ATOM   6344 C  CG   . PHE   B 1 156 ? 51.339 -32.637 -6.247  1.00 16.24 ?  156 PHE   B CG   1 
ATOM   6345 C  CD1  . PHE   B 1 156 ? 52.210 -32.116 -7.185  1.00 17.60 ?  156 PHE   B CD1  1 
ATOM   6346 C  CD2  . PHE   B 1 156 ? 51.811 -33.576 -5.353  1.00 16.78 ?  156 PHE   B CD2  1 
ATOM   6347 C  CE1  . PHE   B 1 156 ? 53.531 -32.532 -7.240  1.00 18.63 ?  156 PHE   B CE1  1 
ATOM   6348 C  CE2  . PHE   B 1 156 ? 53.129 -33.995 -5.404  1.00 18.22 ?  156 PHE   B CE2  1 
ATOM   6349 C  CZ   . PHE   B 1 156 ? 53.982 -33.474 -6.352  1.00 18.63 ?  156 PHE   B CZ   1 
ATOM   6350 H  H    . PHE   B 1 156 ? 47.524 -31.864 -6.387  1.00 17.23 ?  156 PHE   B H    1 
ATOM   6351 H  HA   . PHE   B 1 156 ? 49.452 -32.082 -8.164  1.00 18.86 ?  156 PHE   B HA   1 
ATOM   6352 H  HB2  . PHE   B 1 156 ? 49.928 -31.210 -6.092  1.00 18.71 ?  156 PHE   B HB2  1 
ATOM   6353 H  HB3  . PHE   B 1 156 ? 49.518 -32.573 -5.391  1.00 18.71 ?  156 PHE   B HB3  1 
ATOM   6354 H  HD1  . PHE   B 1 156 ? 51.909 -31.477 -7.790  1.00 21.13 ?  156 PHE   B HD1  1 
ATOM   6355 H  HD2  . PHE   B 1 156 ? 51.235 -33.936 -4.716  1.00 20.14 ?  156 PHE   B HD2  1 
ATOM   6356 H  HE1  . PHE   B 1 156 ? 54.108 -32.177 -7.880  1.00 22.36 ?  156 PHE   B HE1  1 
ATOM   6357 H  HE2  . PHE   B 1 156 ? 53.434 -34.639 -4.803  1.00 21.87 ?  156 PHE   B HE2  1 
ATOM   6358 H  HZ   . PHE   B 1 156 ? 54.869 -33.759 -6.386  1.00 22.36 ?  156 PHE   B HZ   1 
ATOM   6359 N  N    . ASP   B 1 157 ? 48.514 -34.860 -6.864  1.00 17.41 ?  157 ASP   B N    1 
ATOM   6360 C  CA   . ASP   B 1 157 ? 48.657 -36.308 -6.958  1.00 18.89 ?  157 ASP   B CA   1 
ATOM   6361 C  C    . ASP   B 1 157 ? 47.740 -36.852 -8.050  1.00 19.09 ?  157 ASP   B C    1 
ATOM   6362 O  O    . ASP   B 1 157 ? 46.515 -36.723 -7.952  1.00 18.38 ?  157 ASP   B O    1 
ATOM   6363 C  CB   . ASP   B 1 157 ? 48.296 -36.920 -5.611  1.00 20.30 ?  157 ASP   B CB   1 
ATOM   6364 C  CG   . ASP   B 1 157 ? 48.447 -38.428 -5.591  1.00 22.43 ?  157 ASP   B CG   1 
ATOM   6365 O  OD1  . ASP   B 1 157 ? 48.779 -39.028 -6.643  1.00 23.05 ?  157 ASP   B OD1  1 
ATOM   6366 O  OD2  . ASP   B 1 157 ? 48.238 -39.010 -4.509  1.00 24.42 -1 157 ASP   B OD2  1 
ATOM   6367 H  H    . ASP   B 1 157 ? 47.988 -34.600 -6.241  1.00 20.90 ?  157 ASP   B H    1 
ATOM   6368 H  HA   . ASP   B 1 157 ? 49.575 -36.542 -7.173  1.00 22.68 ?  157 ASP   B HA   1 
ATOM   6369 H  HB2  . ASP   B 1 157 ? 48.869 -36.540 -4.930  1.00 24.37 ?  157 ASP   B HB2  1 
ATOM   6370 H  HB3  . ASP   B 1 157 ? 47.367 -36.706 -5.411  1.00 24.37 ?  157 ASP   B HB3  1 
ATOM   6371 N  N    . LYS   B 1 158 ? 48.332 -37.473 -9.080  1.00 20.05 ?  158 LYS   B N    1 
ATOM   6372 C  CA   . LYS   B 1 158 ? 47.552 -38.080 -10.162 1.00 21.27 ?  158 LYS   B CA   1 
ATOM   6373 C  C    . LYS   B 1 158 ? 46.489 -39.040 -9.631  1.00 21.29 ?  158 LYS   B C    1 
ATOM   6374 O  O    . LYS   B 1 158 ? 45.383 -39.124 -10.178 1.00 21.45 ?  158 LYS   B O    1 
ATOM   6375 C  CB   . LYS   B 1 158 ? 48.494 -38.801 -11.137 1.00 23.18 ?  158 LYS   B CB   1 
ATOM   6376 C  CG   . LYS   B 1 158 ? 47.809 -39.709 -12.151 1.00 25.95 ?  158 LYS   B CG   1 
ATOM   6377 C  CD   . LYS   B 1 158 ? 46.949 -38.933 -13.128 1.00 28.24 ?  158 LYS   B CD   1 
ATOM   6378 C  CE   . LYS   B 1 158 ? 46.354 -39.855 -14.183 1.00 30.10 ?  158 LYS   B CE   1 
ATOM   6379 N  NZ   . LYS   B 1 158 ? 45.287 -39.185 -14.979 1.00 30.79 ?  158 LYS   B NZ   1 
ATOM   6380 H  H    . LYS   B 1 158 ? 49.187 -37.554 -9.177  1.00 24.07 ?  158 LYS   B H    1 
ATOM   6381 H  HA   . LYS   B 1 158 ? 47.102 -37.378 -10.659 1.00 25.53 ?  158 LYS   B HA   1 
ATOM   6382 H  HB2  . LYS   B 1 158 ? 48.993 -38.133 -11.641 1.00 27.83 ?  158 LYS   B HB2  1 
ATOM   6383 H  HB3  . LYS   B 1 158 ? 49.113 -39.345 -10.627 1.00 27.83 ?  158 LYS   B HB3  1 
ATOM   6384 H  HG2  . LYS   B 1 158 ? 48.491 -40.174 -12.661 1.00 31.15 ?  158 LYS   B HG2  1 
ATOM   6385 H  HG3  . LYS   B 1 158 ? 47.251 -40.358 -11.694 1.00 31.15 ?  158 LYS   B HG3  1 
ATOM   6386 H  HD2  . LYS   B 1 158 ? 46.221 -38.506 -12.650 1.00 33.90 ?  158 LYS   B HD2  1 
ATOM   6387 H  HD3  . LYS   B 1 158 ? 47.494 -38.268 -13.578 1.00 33.90 ?  158 LYS   B HD3  1 
ATOM   6388 H  HE2  . LYS   B 1 158 ? 47.054 -40.134 -14.793 1.00 36.13 ?  158 LYS   B HE2  1 
ATOM   6389 H  HE3  . LYS   B 1 158 ? 45.965 -40.630 -13.747 1.00 36.13 ?  158 LYS   B HE3  1 
ATOM   6390 H  HZ1  . LYS   B 1 158 ? 44.958 -39.748 -15.585 1.00 36.96 ?  158 LYS   B HZ1  1 
ATOM   6391 H  HZ2  . LYS   B 1 158 ? 44.627 -38.921 -14.442 1.00 36.96 ?  158 LYS   B HZ2  1 
ATOM   6392 H  HZ3  . LYS   B 1 158 ? 45.621 -38.473 -15.397 1.00 36.96 ?  158 LYS   B HZ3  1 
ATOM   6393 N  N    . ASN   B 1 159 ? 46.811 -39.796 -8.580  1.00 21.46 ?  159 ASN   B N    1 
ATOM   6394 C  CA   . ASN   B 1 159 ? 45.854 -40.776 -8.073  1.00 21.94 ?  159 ASN   B CA   1 
ATOM   6395 C  C    . ASN   B 1 159 ? 44.661 -40.101 -7.390  1.00 20.96 ?  159 ASN   B C    1 
ATOM   6396 O  O    . ASN   B 1 159 ? 43.526 -40.594 -7.479  1.00 21.31 ?  159 ASN   B O    1 
ATOM   6397 C  CB   . ASN   B 1 159 ? 46.566 -41.759 -7.146  1.00 23.46 ?  159 ASN   B CB   1 
ATOM   6398 C  CG   . ASN   B 1 159 ? 47.574 -42.621 -7.880  1.00 25.39 ?  159 ASN   B CG   1 
ATOM   6399 O  OD1  . ASN   B 1 159 ? 47.303 -43.109 -8.982  1.00 25.83 ?  159 ASN   B OD1  1 
ATOM   6400 N  ND2  . ASN   B 1 159 ? 48.746 -42.814 -7.276  1.00 25.88 ?  159 ASN   B ND2  1 
ATOM   6401 H  H    . ASN   B 1 159 ? 47.558 -39.756 -8.160  1.00 25.76 ?  159 ASN   B H    1 
ATOM   6402 H  HA   . ASN   B 1 159 ? 45.520 -41.286 -8.832  1.00 26.34 ?  159 ASN   B HA   1 
ATOM   6403 H  HB2  . ASN   B 1 159 ? 47.039 -41.267 -6.461  1.00 28.16 ?  159 ASN   B HB2  1 
ATOM   6404 H  HB3  . ASN   B 1 159 ? 45.911 -42.349 -6.751  1.00 28.16 ?  159 ASN   B HB3  1 
ATOM   6405 H  HD21 . ASN   B 1 159 ? 49.355 -43.300 -7.652  1.00 31.07 ?  159 ASN   B HD21 1 
ATOM   6406 H  HD22 . ASN   B 1 159 ? 48.896 -42.470 -6.503  1.00 31.07 ?  159 ASN   B HD22 1 
ATOM   6407 N  N    . LEU   B 1 160 ? 44.885 -38.974 -6.708  1.00 19.85 ?  160 LEU   B N    1 
ATOM   6408 C  CA   . LEU   B 1 160 ? 43.758 -38.232 -6.160  1.00 18.66 ?  160 LEU   B CA   1 
ATOM   6409 C  C    . LEU   B 1 160 ? 42.966 -37.566 -7.271  1.00 18.13 ?  160 LEU   B C    1 
ATOM   6410 O  O    . LEU   B 1 160 ? 41.730 -37.569 -7.246  1.00 17.87 ?  160 LEU   B O    1 
ATOM   6411 C  CB   . LEU   B 1 160 ? 44.235 -37.196 -5.147  1.00 18.36 ?  160 LEU   B CB   1 
ATOM   6412 C  CG   . LEU   B 1 160 ? 43.110 -36.298 -4.615  1.00 17.96 ?  160 LEU   B CG   1 
ATOM   6413 C  CD1  . LEU   B 1 160 ? 41.996 -37.138 -4.005  1.00 18.81 ?  160 LEU   B CD1  1 
ATOM   6414 C  CD2  . LEU   B 1 160 ? 43.649 -35.306 -3.606  1.00 17.85 ?  160 LEU   B CD2  1 
ATOM   6415 H  H    . LEU   B 1 160 ? 45.663 -38.640 -6.559  1.00 23.83 ?  160 LEU   B H    1 
ATOM   6416 H  HA   . LEU   B 1 160 ? 43.171 -38.862 -5.713  1.00 22.40 ?  160 LEU   B HA   1 
ATOM   6417 H  HB2  . LEU   B 1 160 ? 44.637 -37.665 -4.400  1.00 22.04 ?  160 LEU   B HB2  1 
ATOM   6418 H  HB3  . LEU   B 1 160 ? 44.899 -36.633 -5.578  1.00 22.04 ?  160 LEU   B HB3  1 
ATOM   6419 H  HG   . LEU   B 1 160 ? 42.735 -35.801 -5.355  1.00 21.56 ?  160 LEU   B HG   1 
ATOM   6420 H  HD11 . LEU   B 1 160 ? 41.382 -36.552 -3.544  1.00 22.58 ?  160 LEU   B HD11 1 
ATOM   6421 H  HD12 . LEU   B 1 160 ? 41.530 -37.618 -4.711  1.00 22.58 ?  160 LEU   B HD12 1 
ATOM   6422 H  HD13 . LEU   B 1 160 ? 42.383 -37.774 -3.378  1.00 22.58 ?  160 LEU   B HD13 1 
ATOM   6423 H  HD21 . LEU   B 1 160 ? 42.920 -34.740 -3.313  1.00 21.43 ?  160 LEU   B HD21 1 
ATOM   6424 H  HD22 . LEU   B 1 160 ? 44.017 -35.792 -2.853  1.00 21.43 ?  160 LEU   B HD22 1 
ATOM   6425 H  HD23 . LEU   B 1 160 ? 44.338 -34.773 -4.028  1.00 21.43 ?  160 LEU   B HD23 1 
ATOM   6426 N  N    . TYR   B 1 161 ? 43.661 -37.003 -8.264  1.00 18.11 ?  161 TYR   B N    1 
ATOM   6427 C  CA   . TYR   B 1 161 ? 42.985 -36.436 -9.426  1.00 18.05 ?  161 TYR   B CA   1 
ATOM   6428 C  C    . TYR   B 1 161 ? 42.037 -37.457 -10.042 1.00 17.98 ?  161 TYR   B C    1 
ATOM   6429 O  O    . TYR   B 1 161 ? 40.867 -37.159 -10.299 1.00 17.71 ?  161 TYR   B O    1 
ATOM   6430 C  CB   . TYR   B 1 161 ? 44.021 -35.965 -10.455 1.00 18.63 ?  161 TYR   B CB   1 
ATOM   6431 C  CG   . TYR   B 1 161 ? 43.439 -35.496 -11.771 1.00 19.26 ?  161 TYR   B CG   1 
ATOM   6432 C  CD1  . TYR   B 1 161 ? 43.055 -34.173 -11.944 1.00 19.39 ?  161 TYR   B CD1  1 
ATOM   6433 C  CD2  . TYR   B 1 161 ? 43.266 -36.373 -12.839 1.00 19.79 ?  161 TYR   B CD2  1 
ATOM   6434 C  CE1  . TYR   B 1 161 ? 42.520 -33.733 -13.133 1.00 20.42 ?  161 TYR   B CE1  1 
ATOM   6435 C  CE2  . TYR   B 1 161 ? 42.726 -35.941 -14.035 1.00 21.02 ?  161 TYR   B CE2  1 
ATOM   6436 C  CZ   . TYR   B 1 161 ? 42.360 -34.618 -14.176 1.00 21.26 ?  161 TYR   B CZ   1 
ATOM   6437 O  OH   . TYR   B 1 161 ? 41.818 -34.180 -15.360 1.00 23.18 ?  161 TYR   B OH   1 
ATOM   6438 H  H    . TYR   B 1 161 ? 44.516 -36.944 -8.295  1.00 21.74 ?  161 TYR   B H    1 
ATOM   6439 H  HA   . TYR   B 1 161 ? 42.461 -35.671 -9.156  1.00 21.67 ?  161 TYR   B HA   1 
ATOM   6440 H  HB2  . TYR   B 1 161 ? 44.517 -35.221 -10.079 1.00 22.37 ?  161 TYR   B HB2  1 
ATOM   6441 H  HB3  . TYR   B 1 161 ? 44.626 -36.695 -10.653 1.00 22.37 ?  161 TYR   B HB3  1 
ATOM   6442 H  HD1  . TYR   B 1 161 ? 43.162 -33.567 -11.247 1.00 23.28 ?  161 TYR   B HD1  1 
ATOM   6443 H  HD2  . TYR   B 1 161 ? 43.510 -37.266 -12.751 1.00 23.76 ?  161 TYR   B HD2  1 
ATOM   6444 H  HE1  . TYR   B 1 161 ? 42.270 -32.840 -13.231 1.00 24.51 ?  161 TYR   B HE1  1 
ATOM   6445 H  HE2  . TYR   B 1 161 ? 42.613 -36.535 -14.743 1.00 25.23 ?  161 TYR   B HE2  1 
ATOM   6446 H  HH   . TYR   B 1 161 ? 41.777 -34.814 -15.909 1.00 27.83 ?  161 TYR   B HH   1 
ATOM   6447 N  N    . ASP   B 1 162 ? 42.529 -38.678 -10.268 1.00 18.52 ?  162 ASP   B N    1 
ATOM   6448 C  CA   . ASP   B 1 162 ? 41.697 -39.710 -10.877 1.00 19.15 ?  162 ASP   B CA   1 
ATOM   6449 C  C    . ASP   B 1 162 ? 40.497 -40.045 -9.999  1.00 18.70 ?  162 ASP   B C    1 
ATOM   6450 O  O    . ASP   B 1 162 ? 39.389 -40.256 -10.506 1.00 18.98 ?  162 ASP   B O    1 
ATOM   6451 C  CB   . ASP   B 1 162 ? 42.523 -40.975 -11.131 1.00 20.47 ?  162 ASP   B CB   1 
ATOM   6452 C  CG   . ASP   B 1 162 ? 43.531 -40.814 -12.249 1.00 22.13 ?  162 ASP   B CG   1 
ATOM   6453 O  OD1  . ASP   B 1 162 ? 43.403 -39.880 -13.061 1.00 22.38 ?  162 ASP   B OD1  1 
ATOM   6454 O  OD2  . ASP   B 1 162 ? 44.445 -41.662 -12.335 1.00 23.65 -1 162 ASP   B OD2  1 
ATOM   6455 H  H    . ASP   B 1 162 ? 43.328 -38.928 -10.081 1.00 22.24 ?  162 ASP   B H    1 
ATOM   6456 H  HA   . ASP   B 1 162 ? 41.363 -39.394 -11.730 1.00 22.99 ?  162 ASP   B HA   1 
ATOM   6457 H  HB2  . ASP   B 1 162 ? 43.022 -41.199 -10.335 1.00 24.58 ?  162 ASP   B HB2  1 
ATOM   6458 H  HB3  . ASP   B 1 162 ? 41.929 -41.703 -11.372 1.00 24.58 ?  162 ASP   B HB3  1 
ATOM   6459 N  N    . LYS   B 1 163 ? 40.700 -40.123 -8.683  1.00 18.00 ?  163 LYS   B N    1 
ATOM   6460 C  CA   . LYS   B 1 163 ? 39.579 -40.396 -7.787  1.00 18.62 ?  163 LYS   B CA   1 
ATOM   6461 C  C    . LYS   B 1 163 ? 38.537 -39.284 -7.846  1.00 17.08 ?  163 LYS   B C    1 
ATOM   6462 O  O    . LYS   B 1 163 ? 37.324 -39.547 -7.830  1.00 17.81 ?  163 LYS   B O    1 
ATOM   6463 C  CB   . LYS   B 1 163 ? 40.079 -40.578 -6.356  1.00 21.33 ?  163 LYS   B CB   1 
ATOM   6464 C  CG   . LYS   B 1 163 ? 38.997 -41.063 -5.416  1.00 26.23 ?  163 LYS   B CG   1 
ATOM   6465 C  CD   . LYS   B 1 163 ? 39.489 -41.236 -3.993  1.00 30.79 ?  163 LYS   B CD   1 
ATOM   6466 C  CE   . LYS   B 1 163 ? 38.411 -41.901 -3.149  1.00 34.63 ?  163 LYS   B CE   1 
ATOM   6467 N  NZ   . LYS   B 1 163 ? 38.527 -41.579 -1.702  1.00 36.71 ?  163 LYS   B NZ   1 
ATOM   6468 H  H    . LYS   B 1 163 ? 41.464 -40.028 -8.296  1.00 21.61 ?  163 LYS   B H    1 
ATOM   6469 H  HA   . LYS   B 1 163 ? 39.153 -41.219 -8.065  1.00 22.36 ?  163 LYS   B HA   1 
ATOM   6470 H  HB2  . LYS   B 1 163 ? 40.795 -41.235 -6.353  1.00 25.60 ?  163 LYS   B HB2  1 
ATOM   6471 H  HB3  . LYS   B 1 163 ? 40.406 -39.730 -6.024  1.00 25.60 ?  163 LYS   B HB3  1 
ATOM   6472 H  HG2  . LYS   B 1 163 ? 38.272 -40.420 -5.404  1.00 31.48 ?  163 LYS   B HG2  1 
ATOM   6473 H  HG3  . LYS   B 1 163 ? 38.670 -41.924 -5.726  1.00 31.48 ?  163 LYS   B HG3  1 
ATOM   6474 H  HD2  . LYS   B 1 163 ? 40.277 -41.803 -3.988  1.00 36.96 ?  163 LYS   B HD2  1 
ATOM   6475 H  HD3  . LYS   B 1 163 ? 39.690 -40.368 -3.611  1.00 36.96 ?  163 LYS   B HD3  1 
ATOM   6476 H  HE2  . LYS   B 1 163 ? 37.539 -41.612 -3.459  1.00 41.56 ?  163 LYS   B HE2  1 
ATOM   6477 H  HE3  . LYS   B 1 163 ? 38.489 -42.862 -3.247  1.00 41.56 ?  163 LYS   B HE3  1 
ATOM   6478 H  HZ1  . LYS   B 1 163 ? 37.878 -41.986 -1.249  1.00 44.06 ?  163 LYS   B HZ1  1 
ATOM   6479 H  HZ2  . LYS   B 1 163 ? 39.313 -41.854 -1.393  1.00 44.06 ?  163 LYS   B HZ2  1 
ATOM   6480 H  HZ3  . LYS   B 1 163 ? 38.458 -40.700 -1.580  1.00 44.06 ?  163 LYS   B HZ3  1 
ATOM   6481 N  N    . LEU   B 1 164 ? 38.997 -38.032 -7.904  1.00 15.79 ?  164 LEU   B N    1 
ATOM   6482 C  CA   . LEU   B 1 164 ? 38.087 -36.893 -7.960  1.00 15.75 ?  164 LEU   B CA   1 
ATOM   6483 C  C    . LEU   B 1 164 ? 37.302 -36.876 -9.265  1.00 15.93 ?  164 LEU   B C    1 
ATOM   6484 O  O    . LEU   B 1 164 ? 36.078 -36.679 -9.263  1.00 17.25 ?  164 LEU   B O    1 
ATOM   6485 C  CB   . LEU   B 1 164 ? 38.884 -35.599 -7.799  1.00 15.22 ?  164 LEU   B CB   1 
ATOM   6486 C  CG   . LEU   B 1 164 ? 39.413 -35.308 -6.396  1.00 16.02 ?  164 LEU   B CG   1 
ATOM   6487 C  CD1  . LEU   B 1 164 ? 40.495 -34.248 -6.466  1.00 16.02 ?  164 LEU   B CD1  1 
ATOM   6488 C  CD2  . LEU   B 1 164 ? 38.304 -34.860 -5.463  1.00 17.73 ?  164 LEU   B CD2  1 
ATOM   6489 H  H    . LEU   B 1 164 ? 39.836 -37.814 -7.913  1.00 18.95 ?  164 LEU   B H    1 
ATOM   6490 H  HA   . LEU   B 1 164 ? 37.457 -36.953 -7.237  1.00 18.91 ?  164 LEU   B HA   1 
ATOM   6491 H  HB2  . LEU   B 1 164 ? 39.655 -35.633 -8.396  1.00 18.27 ?  164 LEU   B HB2  1 
ATOM   6492 H  HB3  . LEU   B 1 164 ? 38.320 -34.854 -8.054  1.00 18.27 ?  164 LEU   B HB3  1 
ATOM   6493 H  HG   . LEU   B 1 164 ? 39.817 -36.109 -6.035  1.00 19.23 ?  164 LEU   B HG   1 
ATOM   6494 H  HD11 . LEU   B 1 164 ? 40.815 -34.056 -5.569  1.00 19.23 ?  164 LEU   B HD11 1 
ATOM   6495 H  HD12 . LEU   B 1 164 ? 41.230 -34.570 -7.014  1.00 19.23 ?  164 LEU   B HD12 1 
ATOM   6496 H  HD13 . LEU   B 1 164 ? 40.126 -33.437 -6.860  1.00 19.23 ?  164 LEU   B HD13 1 
ATOM   6497 H  HD21 . LEU   B 1 164 ? 38.686 -34.644 -4.598  1.00 21.29 ?  164 LEU   B HD21 1 
ATOM   6498 H  HD22 . LEU   B 1 164 ? 37.869 -34.080 -5.838  1.00 21.29 ?  164 LEU   B HD22 1 
ATOM   6499 H  HD23 . LEU   B 1 164 ? 37.666 -35.585 -5.371  1.00 21.29 ?  164 LEU   B HD23 1 
ATOM   6500 N  N    . VAL   B 1 165 ? 37.992 -37.052 -10.394 1.00 17.65 ?  165 VAL   B N    1 
ATOM   6501 C  CA   . VAL   B 1 165 ? 37.331 -36.997 -11.694 1.00 19.27 ?  165 VAL   B CA   1 
ATOM   6502 C  C    . VAL   B 1 165 ? 36.403 -38.192 -11.861 1.00 21.06 ?  165 VAL   B C    1 
ATOM   6503 O  O    . VAL   B 1 165 ? 35.230 -38.047 -12.229 1.00 22.45 ?  165 VAL   B O    1 
ATOM   6504 C  CB   . VAL   B 1 165 ? 38.372 -36.922 -12.828 1.00 20.41 ?  165 VAL   B CB   1 
ATOM   6505 C  CG1  . VAL   B 1 165 ? 37.702 -37.044 -14.178 1.00 21.35 ?  165 VAL   B CG1  1 
ATOM   6506 C  CG2  . VAL   B 1 165 ? 39.160 -35.626 -12.749 1.00 20.16 ?  165 VAL   B CG2  1 
ATOM   6507 H  H    . VAL   B 1 165 ? 38.843 -37.209 -10.439 1.00 21.19 ?  165 VAL   B H    1 
ATOM   6508 H  HA   . VAL   B 1 165 ? 36.793 -36.196 -11.742 1.00 23.13 ?  165 VAL   B HA   1 
ATOM   6509 H  HB   . VAL   B 1 165 ? 39.006 -37.651 -12.738 1.00 24.50 ?  165 VAL   B HB   1 
ATOM   6510 H  HG11 . VAL   B 1 165 ? 38.308 -36.729 -14.865 1.00 25.63 ?  165 VAL   B HG11 1 
ATOM   6511 H  HG12 . VAL   B 1 165 ? 37.487 -37.977 -14.334 1.00 25.63 ?  165 VAL   B HG12 1 
ATOM   6512 H  HG13 . VAL   B 1 165 ? 36.894 -36.512 -14.177 1.00 25.63 ?  165 VAL   B HG13 1 
ATOM   6513 H  HG21 . VAL   B 1 165 ? 39.797 -35.591 -13.484 1.00 24.20 ?  165 VAL   B HG21 1 
ATOM   6514 H  HG22 . VAL   B 1 165 ? 38.546 -34.876 -12.815 1.00 24.20 ?  165 VAL   B HG22 1 
ATOM   6515 H  HG23 . VAL   B 1 165 ? 39.634 -35.590 -11.904 1.00 24.20 ?  165 VAL   B HG23 1 
ATOM   6516 N  N    . SER   B 1 166 ? 36.917 -39.394 -11.578 1.00 21.88 ?  166 SER   B N    1 
ATOM   6517 C  CA   . SER   B 1 166 ? 36.163 -40.604 -11.868 1.00 22.96 ?  166 SER   B CA   1 
ATOM   6518 C  C    . SER   B 1 166 ? 34.899 -40.687 -11.028 1.00 23.50 ?  166 SER   B C    1 
ATOM   6519 O  O    . SER   B 1 166 ? 33.924 -41.307 -11.453 1.00 24.78 ?  166 SER   B O    1 
ATOM   6520 C  CB   . SER   B 1 166 ? 37.030 -41.856 -11.679 1.00 23.78 ?  166 SER   B CB   1 
ATOM   6521 O  OG   . SER   B 1 166 ? 37.385 -42.057 -10.322 1.00 23.61 ?  166 SER   B OG   1 
ATOM   6522 H  H    . SER   B 1 166 ? 37.695 -39.528 -11.224 1.00 26.27 ?  166 SER   B H    1 
ATOM   6523 H  HA   . SER   B 1 166 ? 35.898 -40.585 -12.801 1.00 27.56 ?  166 SER   B HA   1 
ATOM   6524 H  HB2  . SER   B 1 166 ? 36.531 -42.631 -11.988 1.00 28.55 ?  166 SER   B HB2  1 
ATOM   6525 H  HB3  . SER   B 1 166 ? 37.842 -41.762 -12.204 1.00 28.55 ?  166 SER   B HB3  1 
ATOM   6526 H  HG   . SER   B 1 166 ? 37.820 -41.391 -10.043 1.00 28.34 ?  166 SER   B HG   1 
ATOM   6527 N  N    . SER   B 1 167 ? 34.885 -40.072 -9.847  1.00 21.94 ?  167 SER   B N    1 
ATOM   6528 C  CA   . SER   B 1 167 ? 33.731 -40.125 -8.955  1.00 21.43 ?  167 SER   B CA   1 
ATOM   6529 C  C    . SER   B 1 167 ? 32.815 -38.905 -9.049  1.00 20.93 ?  167 SER   B C    1 
ATOM   6530 O  O    . SER   B 1 167 ? 31.737 -38.913 -8.445  1.00 21.27 ?  167 SER   B O    1 
ATOM   6531 C  CB   . SER   B 1 167 ? 34.184 -40.312 -7.499  1.00 21.39 ?  167 SER   B CB   1 
ATOM   6532 O  OG   . SER   B 1 167 ? 34.852 -39.151 -7.015  1.00 21.20 ?  167 SER   B OG   1 
ATOM   6533 H  H    . SER   B 1 167 ? 35.539 -39.619 -9.539  1.00 26.34 ?  167 SER   B H    1 
ATOM   6534 H  HA   . SER   B 1 167 ? 33.198 -40.904 -9.195  1.00 25.73 ?  167 SER   B HA   1 
ATOM   6535 H  HB2  . SER   B 1 167 ? 33.401 -40.491 -6.951  1.00 25.67 ?  167 SER   B HB2  1 
ATOM   6536 H  HB3  . SER   B 1 167 ? 34.787 -41.079 -7.458  1.00 25.67 ?  167 SER   B HB3  1 
ATOM   6537 H  HG   . SER   B 1 167 ? 35.529 -39.009 -7.482  1.00 25.45 ?  167 SER   B HG   1 
ATOM   6538 N  N    . PHE   B 1 168 ? 33.196 -37.861 -9.786  1.00 20.32 ?  168 PHE   B N    1 
ATOM   6539 C  CA   . PHE   B 1 168 ? 32.352 -36.667 -9.852  1.00 19.42 ?  168 PHE   B CA   1 
ATOM   6540 C  C    . PHE   B 1 168 ? 31.054 -36.932 -10.609 1.00 17.29 ?  168 PHE   B C    1 
ATOM   6541 O  O    . PHE   B 1 168 ? 29.998 -36.356 -10.280 1.00 17.51 ?  168 PHE   B O    1 
ATOM   6542 C  CB   . PHE   B 1 168 ? 33.117 -35.520 -10.509 1.00 20.10 ?  168 PHE   B CB   1 
ATOM   6543 C  CG   . PHE   B 1 168 ? 32.299 -34.280 -10.668 1.00 19.72 ?  168 PHE   B CG   1 
ATOM   6544 C  CD1  . PHE   B 1 168 ? 31.943 -33.527 -9.559  1.00 20.75 ?  168 PHE   B CD1  1 
ATOM   6545 C  CD2  . PHE   B 1 168 ? 31.872 -33.865 -11.915 1.00 19.01 ?  168 PHE   B CD2  1 
ATOM   6546 C  CE1  . PHE   B 1 168 ? 31.171 -32.390 -9.688  1.00 20.87 ?  168 PHE   B CE1  1 
ATOM   6547 C  CE2  . PHE   B 1 168 ? 31.111 -32.710 -12.056 1.00 19.99 ?  168 PHE   B CE2  1 
ATOM   6548 C  CZ   . PHE   B 1 168 ? 30.758 -31.970 -10.937 1.00 20.29 ?  168 PHE   B CZ   1 
ATOM   6549 H  H    . PHE   B 1 168 ? 33.921 -37.815 -10.240 1.00 24.40 ?  168 PHE   B H    1 
ATOM   6550 H  HA   . PHE   B 1 168 ? 32.111 -36.398 -8.955  1.00 23.31 ?  168 PHE   B HA   1 
ATOM   6551 H  HB2  . PHE   B 1 168 ? 33.882 -35.300 -9.960  1.00 24.13 ?  168 PHE   B HB2  1 
ATOM   6552 H  HB3  . PHE   B 1 168 ? 33.406 -35.794 -11.392 1.00 24.13 ?  168 PHE   B HB3  1 
ATOM   6553 H  HD1  . PHE   B 1 168 ? 32.213 -33.804 -8.714  1.00 24.91 ?  168 PHE   B HD1  1 
ATOM   6554 H  HD2  . PHE   B 1 168 ? 32.104 -34.349 -12.668 1.00 22.82 ?  168 PHE   B HD2  1 
ATOM   6555 H  HE1  . PHE   B 1 168 ? 30.939 -31.896 -8.935  1.00 25.05 ?  168 PHE   B HE1  1 
ATOM   6556 H  HE2  . PHE   B 1 168 ? 30.826 -32.435 -12.902 1.00 24.00 ?  168 PHE   B HE2  1 
ATOM   6557 H  HZ   . PHE   B 1 168 ? 30.240 -31.202 -11.030 1.00 24.35 ?  168 PHE   B HZ   1 
ATOM   6558 N  N    . LEU   B 1 169 ? 31.113 -37.799 -11.617 1.00 17.61 ?  169 LEU   B N    1 
ATOM   6559 C  CA   . LEU   B 1 169 ? 29.945 -38.128 -12.424 1.00 19.74 ?  169 LEU   B CA   1 
ATOM   6560 C  C    . LEU   B 1 169 ? 29.946 -39.573 -12.898 1.00 22.59 ?  169 LEU   B C    1 
ATOM   6561 O  O    . LEU   B 1 169 ? 29.048 -39.993 -13.632 1.00 24.68 ?  169 LEU   B O    1 
ATOM   6562 C  CB   . LEU   B 1 169 ? 29.870 -37.210 -13.642 1.00 21.34 ?  169 LEU   B CB   1 
ATOM   6563 C  CG   . LEU   B 1 169 ? 28.617 -36.346 -13.754 1.00 23.83 ?  169 LEU   B CG   1 
ATOM   6564 C  CD1  . LEU   B 1 169 ? 28.557 -35.738 -15.135 1.00 24.67 ?  169 LEU   B CD1  1 
ATOM   6565 C  CD2  . LEU   B 1 169 ? 27.357 -37.144 -13.461 1.00 23.78 ?  169 LEU   B CD2  1 
ATOM   6566 O  OXT  . LEU   B 1 169 ? 30.847 -40.340 -12.569 1.00 23.45 -1 169 LEU   B OXT  1 
ATOM   6567 H  H    . LEU   B 1 169 ? 31.830 -38.207 -11.867 1.00 21.14 ?  169 LEU   B H    1 
ATOM   6568 H  HA   . LEU   B 1 169 ? 29.157 -37.987 -11.885 1.00 23.70 ?  169 LEU   B HA   1 
ATOM   6569 H  HB2  . LEU   B 1 169 ? 30.631 -36.609 -13.629 1.00 25.62 ?  169 LEU   B HB2  1 
ATOM   6570 H  HB3  . LEU   B 1 169 ? 29.907 -37.755 -14.446 1.00 25.62 ?  169 LEU   B HB3  1 
ATOM   6571 H  HG   . LEU   B 1 169 ? 28.670 -35.618 -13.111 1.00 28.61 ?  169 LEU   B HG   1 
ATOM   6572 H  HD11 . LEU   B 1 169 ? 27.780 -35.162 -15.193 1.00 29.61 ?  169 LEU   B HD11 1 
ATOM   6573 H  HD12 . LEU   B 1 169 ? 29.365 -35.224 -15.286 1.00 29.61 ?  169 LEU   B HD12 1 
ATOM   6574 H  HD13 . LEU   B 1 169 ? 28.491 -36.452 -15.787 1.00 29.61 ?  169 LEU   B HD13 1 
ATOM   6575 H  HD21 . LEU   B 1 169 ? 26.605 -36.729 -13.907 1.00 28.55 ?  169 LEU   B HD21 1 
ATOM   6576 H  HD22 . LEU   B 1 169 ? 27.479 -38.051 -13.790 1.00 28.55 ?  169 LEU   B HD22 1 
ATOM   6577 H  HD23 . LEU   B 1 169 ? 27.210 -37.158 -12.503 1.00 28.55 ?  169 LEU   B HD23 1 
HETATM 6578 C  C1   T TFA   C 2 .   ? 12.138 -1.261  1.464   0.30 11.24 ?  201 TFA   A C1   1 
HETATM 6579 C  C2   T TFA   C 2 .   ? 12.758 -1.722  0.120   0.30 13.41 ?  201 TFA   A C2   1 
HETATM 6580 O  O    T TFA   C 2 .   ? 12.848 -1.514  2.442   0.30 9.77  ?  201 TFA   A O    1 
HETATM 6581 F  F1   T TFA   C 2 .   ? 12.813 -3.065  0.083   0.30 14.49 ?  201 TFA   A F1   1 
HETATM 6582 F  F2   T TFA   C 2 .   ? 12.056 -1.346  -0.960  0.30 13.65 ?  201 TFA   A F2   1 
HETATM 6583 F  F3   T TFA   C 2 .   ? 13.993 -1.251  -0.065  0.30 14.62 ?  201 TFA   A F3   1 
HETATM 6584 O  OXT  T TFA   C 2 .   ? 11.044 -0.705  1.388   0.30 10.96 ?  201 TFA   A OXT  1 
HETATM 6585 N  N2   B A1A84 D 3 .   ? 14.844 -0.061  3.788   0.36 17.12 ?  202 A1A84 A N2   1 
HETATM 6586 C  C3   B A1A84 D 3 .   ? 13.524 0.175   -0.182  0.36 20.73 ?  202 A1A84 A C3   1 
HETATM 6587 C  C6   B A1A84 D 3 .   ? 15.075 1.106   3.085   0.36 17.15 ?  202 A1A84 A C6   1 
HETATM 6588 C  C9   B A1A84 D 3 .   ? 15.348 2.307   3.823   0.36 15.74 ?  202 A1A84 A C9   1 
HETATM 6589 C  C1   B A1A84 D 3 .   ? 11.789 2.079   0.481   0.36 20.48 ?  202 A1A84 A C1   1 
HETATM 6590 C  C10  B A1A84 D 3 .   ? 15.649 3.707   3.584   0.36 14.98 ?  202 A1A84 A C10  1 
HETATM 6591 C  C11  B A1A84 D 3 .   ? 15.809 4.340   4.802   0.36 14.07 ?  202 A1A84 A C11  1 
HETATM 6592 C  C2   B A1A84 D 3 .   ? 12.565 1.223   0.189   0.36 20.90 ?  202 A1A84 A C2   1 
HETATM 6593 C  C4   B A1A84 D 3 .   ? 14.596 -0.162  0.918   0.36 20.04 ?  202 A1A84 A C4   1 
HETATM 6594 C  C5   B A1A84 D 3 .   ? 15.853 -0.842  0.230   0.36 20.47 ?  202 A1A84 A C5   1 
HETATM 6595 C  C7   B A1A84 D 3 .   ? 14.877 -0.059  5.163   0.36 16.67 ?  202 A1A84 A C7   1 
HETATM 6596 C  C8   B A1A84 D 3 .   ? 15.349 2.146   5.237   0.36 14.93 ?  202 A1A84 A C8   1 
HETATM 6597 N  N1   B A1A84 D 3 .   ? 15.023 1.050   1.690   0.36 18.53 ?  202 A1A84 A N1   1 
HETATM 6598 N  N3   B A1A84 D 3 .   ? 15.117 0.992   5.955   0.36 15.78 ?  202 A1A84 A N3   1 
HETATM 6599 N  N4   B A1A84 D 3 .   ? 15.633 3.377   5.803   0.36 13.67 ?  202 A1A84 A N4   1 
HETATM 6600 O  O1   B A1A84 D 3 .   ? 15.469 -2.066  -0.330  0.36 20.70 ?  202 A1A84 A O1   1 
HETATM 6601 H  H4   B A1A84 D 3 .   ? 14.061 0.480   -1.048  0.36 24.89 ?  202 A1A84 A H4   1 
HETATM 6602 H  H3   B A1A84 D 3 .   ? 13.015 -0.771  -0.513  0.36 24.89 ?  202 A1A84 A H3   1 
HETATM 6603 H  H2   B A1A84 D 3 .   ? 11.089 2.848   0.749   0.36 24.58 ?  202 A1A84 A H2   1 
HETATM 6604 H  H10  B A1A84 D 3 .   ? 15.728 4.227   2.644   0.36 17.98 ?  202 A1A84 A H10  1 
HETATM 6605 H  H11  B A1A84 D 3 .   ? 16.038 5.370   5.099   0.36 16.89 ?  202 A1A84 A H11  1 
HETATM 6606 H  H1   B A1A84 D 3 .   ? 14.121 -0.877  1.619   0.36 24.06 ?  202 A1A84 A H1   1 
HETATM 6607 H  H5   B A1A84 D 3 .   ? 16.274 -0.162  -0.548  0.36 24.58 ?  202 A1A84 A H5   1 
HETATM 6608 H  H6   B A1A84 D 3 .   ? 16.654 -1.024  0.984   0.36 24.58 ?  202 A1A84 A H6   1 
HETATM 6609 H  H9   B A1A84 D 3 .   ? 14.679 -1.035  5.695   0.36 20.01 ?  202 A1A84 A H9   1 
HETATM 6610 H  H8   B A1A84 D 3 .   ? 15.292 1.885   1.151   0.36 22.24 ?  202 A1A84 A H8   1 
HETATM 6611 H  H12  B A1A84 D 3 .   ? 15.699 3.577   6.788   0.36 16.41 ?  202 A1A84 A H12  1 
HETATM 6612 H  H7   B A1A84 D 3 .   ? 16.243 -2.539  -0.668  0.36 24.85 ?  202 A1A84 A H7   1 
HETATM 6613 CL CL   B CL    E 4 .   ? 16.089 2.772   -1.286  0.36 16.87 ?  203 CL    A CL   1 
HETATM 6614 O  O    . HOH   F 5 .   ? 14.707 -4.585  20.470  1.00 43.93 ?  301 HOH   A O    1 
HETATM 6615 O  O    . HOH   F 5 .   ? 4.662  3.749   0.525   1.00 23.01 ?  302 HOH   A O    1 
HETATM 6616 O  O    . HOH   F 5 .   ? 11.973 0.381   14.688  1.00 34.64 ?  303 HOH   A O    1 
HETATM 6617 O  O    . HOH   F 5 .   ? 34.298 -1.832  12.510  1.00 36.92 ?  304 HOH   A O    1 
HETATM 6618 O  O    . HOH   F 5 .   ? 6.824  -7.959  11.788  1.00 19.18 ?  305 HOH   A O    1 
HETATM 6619 O  O    B HOH   F 5 .   ? 11.139 -0.869  2.350   0.36 28.20 ?  306 HOH   A O    1 
HETATM 6620 O  O    . HOH   F 5 .   ? 11.758 -10.806 -10.086 1.00 49.08 ?  307 HOH   A O    1 
HETATM 6621 O  O    . HOH   F 5 .   ? -0.444 -2.904  2.959   1.00 38.31 ?  308 HOH   A O    1 
HETATM 6622 O  O    . HOH   F 5 .   ? 8.902  -12.031 17.150  1.00 48.04 ?  309 HOH   A O    1 
HETATM 6623 O  O    . HOH   F 5 .   ? 15.043 -12.191 18.615  1.00 44.50 ?  310 HOH   A O    1 
HETATM 6624 O  O    . HOH   F 5 .   ? 7.631  -6.303  -6.638  1.00 40.83 ?  311 HOH   A O    1 
HETATM 6625 O  O    . HOH   F 5 .   ? 30.213 -13.324 -8.461  1.00 23.40 ?  312 HOH   A O    1 
HETATM 6626 O  O    . HOH   F 5 .   ? 9.180  -10.070 19.341  1.00 40.50 ?  313 HOH   A O    1 
HETATM 6627 O  O    . HOH   F 5 .   ? 22.693 12.496  1.581   1.00 15.27 ?  314 HOH   A O    1 
HETATM 6628 O  O    . HOH   F 5 .   ? 0.659  -4.398  0.041   1.00 32.84 ?  315 HOH   A O    1 
HETATM 6629 O  O    . HOH   F 5 .   ? 14.653 -13.929 16.619  1.00 26.31 ?  316 HOH   A O    1 
HETATM 6630 O  O    . HOH   F 5 .   ? 42.386 10.567  5.087   1.00 20.17 ?  317 HOH   A O    1 
HETATM 6631 O  O    . HOH   F 5 .   ? 14.148 -4.536  -11.902 1.00 36.17 ?  318 HOH   A O    1 
HETATM 6632 O  O    . HOH   F 5 .   ? 28.953 0.468   -9.670  1.00 21.30 ?  319 HOH   A O    1 
HETATM 6633 O  O    . HOH   F 5 .   ? 28.145 -6.248  19.602  1.00 41.49 ?  320 HOH   A O    1 
HETATM 6634 O  O    . HOH   F 5 .   ? 7.919  -12.532 -0.901  1.00 21.71 ?  321 HOH   A O    1 
HETATM 6635 O  O    . HOH   F 5 .   ? 18.911 -21.931 6.983   1.00 32.37 ?  322 HOH   A O    1 
HETATM 6636 O  O    . HOH   F 5 .   ? 15.030 4.039   17.637  1.00 42.88 ?  323 HOH   A O    1 
HETATM 6637 O  O    . HOH   F 5 .   ? -0.658 -8.471  2.144   1.00 43.28 ?  324 HOH   A O    1 
HETATM 6638 O  O    . HOH   F 5 .   ? 38.224 10.198  7.136   1.00 45.26 ?  325 HOH   A O    1 
HETATM 6639 O  O    B HOH   F 5 .   ? 13.161 -3.050  -1.216  0.36 35.03 ?  326 HOH   A O    1 
HETATM 6640 O  O    . HOH   F 5 .   ? 30.928 6.227   -12.236 1.00 28.23 ?  327 HOH   A O    1 
HETATM 6641 O  O    . HOH   F 5 .   ? 36.139 -5.096  -0.532  1.00 30.77 ?  328 HOH   A O    1 
HETATM 6642 O  O    . HOH   F 5 .   ? 26.471 -19.309 -1.733  1.00 14.76 ?  329 HOH   A O    1 
HETATM 6643 O  O    . HOH   F 5 .   ? 19.907 -12.518 -8.857  1.00 25.09 ?  330 HOH   A O    1 
HETATM 6644 O  O    . HOH   F 5 .   ? 22.274 5.428   18.943  1.00 41.36 ?  331 HOH   A O    1 
HETATM 6645 O  O    . HOH   F 5 .   ? 17.057 -17.964 14.996  1.00 27.25 ?  332 HOH   A O    1 
HETATM 6646 O  O    . HOH   F 5 .   ? 28.587 -10.563 -14.019 1.00 43.66 ?  333 HOH   A O    1 
HETATM 6647 O  O    . HOH   F 5 .   ? 44.286 7.148   6.405   1.00 26.89 ?  334 HOH   A O    1 
HETATM 6648 O  O    . HOH   F 5 .   ? 34.009 -1.045  -8.906  1.00 27.40 ?  335 HOH   A O    1 
HETATM 6649 O  O    . HOH   F 5 .   ? 27.338 13.799  2.823   1.00 31.56 ?  336 HOH   A O    1 
HETATM 6650 O  O    . HOH   F 5 .   ? 30.998 -18.077 7.810   1.00 19.50 ?  337 HOH   A O    1 
HETATM 6651 O  O    A HOH   F 5 .   ? 3.567  -9.409  9.710   0.64 22.90 ?  338 HOH   A O    1 
HETATM 6652 O  O    B HOH   F 5 .   ? 14.867 -2.864  3.205   0.36 18.20 ?  339 HOH   A O    1 
HETATM 6653 O  O    . HOH   F 5 .   ? 37.491 2.809   10.228  1.00 28.09 ?  340 HOH   A O    1 
HETATM 6654 O  O    . HOH   F 5 .   ? 9.866  -21.367 5.655   1.00 19.55 ?  341 HOH   A O    1 
HETATM 6655 O  O    . HOH   F 5 .   ? 18.656 -19.335 13.538  1.00 37.98 ?  342 HOH   A O    1 
HETATM 6656 O  O    . HOH   F 5 .   ? 28.318 -0.097  -13.387 1.00 35.13 ?  343 HOH   A O    1 
HETATM 6657 O  O    . HOH   F 5 .   ? 39.740 -1.037  -5.119  1.00 22.61 ?  344 HOH   A O    1 
HETATM 6658 O  O    . HOH   F 5 .   ? 38.529 4.994   7.020   1.00 15.30 ?  345 HOH   A O    1 
HETATM 6659 O  O    . HOH   F 5 .   ? 14.370 -21.218 -4.217  1.00 30.05 ?  346 HOH   A O    1 
HETATM 6660 O  O    . HOH   F 5 .   ? 13.236 -1.467  -6.668  1.00 17.85 ?  347 HOH   A O    1 
HETATM 6661 O  O    . HOH   F 5 .   ? 6.392  -5.441  11.030  1.00 19.26 ?  348 HOH   A O    1 
HETATM 6662 O  O    . HOH   F 5 .   ? 20.620 -19.758 -5.021  1.00 26.64 ?  349 HOH   A O    1 
HETATM 6663 O  O    . HOH   F 5 .   ? 24.021 -2.091  -2.084  1.00 11.13 ?  350 HOH   A O    1 
HETATM 6664 O  O    . HOH   F 5 .   ? 27.443 -6.094  -13.958 1.00 37.90 ?  351 HOH   A O    1 
HETATM 6665 O  O    . HOH   F 5 .   ? 26.853 11.456  1.633   1.00 17.17 ?  352 HOH   A O    1 
HETATM 6666 O  O    A HOH   F 5 .   ? 14.251 0.617   6.772   0.64 17.23 ?  353 HOH   A O    1 
HETATM 6667 O  O    . HOH   F 5 .   ? 14.532 -0.537  -12.158 1.00 23.66 ?  354 HOH   A O    1 
HETATM 6668 O  O    . HOH   F 5 .   ? 13.560 -15.239 -7.449  1.00 25.53 ?  355 HOH   A O    1 
HETATM 6669 O  O    . HOH   F 5 .   ? 27.916 0.821   -7.128  1.00 14.33 ?  356 HOH   A O    1 
HETATM 6670 O  O    . HOH   F 5 .   ? 31.827 -9.337  -6.641  1.00 23.42 ?  357 HOH   A O    1 
HETATM 6671 O  O    . HOH   F 5 .   ? 31.647 8.240   14.839  1.00 24.74 ?  358 HOH   A O    1 
HETATM 6672 O  O    . HOH   F 5 .   ? 31.067 -13.924 -2.443  1.00 14.28 ?  359 HOH   A O    1 
HETATM 6673 O  O    . HOH   F 5 .   ? 35.747 -12.613 6.877   1.00 16.13 ?  360 HOH   A O    1 
HETATM 6674 O  O    . HOH   F 5 .   ? 37.184 -2.787  9.741   1.00 42.31 ?  361 HOH   A O    1 
HETATM 6675 O  O    . HOH   F 5 .   ? 18.574 9.464   8.991   1.00 22.07 ?  362 HOH   A O    1 
HETATM 6676 O  O    . HOH   F 5 .   ? 42.554 4.300   5.429   1.00 33.64 ?  363 HOH   A O    1 
HETATM 6677 O  O    . HOH   F 5 .   ? 43.344 7.806   2.706   1.00 29.65 ?  364 HOH   A O    1 
HETATM 6678 O  O    . HOH   F 5 .   ? 17.135 -17.742 -5.039  1.00 26.37 ?  365 HOH   A O    1 
HETATM 6679 O  O    A HOH   F 5 .   ? 14.612 -3.616  3.076   0.64 14.00 ?  366 HOH   A O    1 
HETATM 6680 O  O    . HOH   F 5 .   ? 15.494 11.860  7.887   1.00 43.84 ?  367 HOH   A O    1 
HETATM 6681 O  O    . HOH   F 5 .   ? 30.773 3.110   8.268   1.00 12.48 ?  368 HOH   A O    1 
HETATM 6682 O  O    . HOH   F 5 .   ? 21.293 -2.277  -2.415  1.00 16.45 ?  369 HOH   A O    1 
HETATM 6683 O  O    . HOH   F 5 .   ? 25.690 -0.797  -7.347  1.00 15.91 ?  370 HOH   A O    1 
HETATM 6684 O  O    . HOH   F 5 .   ? 43.972 8.463   -3.004  1.00 27.49 ?  371 HOH   A O    1 
HETATM 6685 O  O    . HOH   F 5 .   ? 37.282 11.994  4.914   1.00 28.47 ?  372 HOH   A O    1 
HETATM 6686 O  O    . HOH   F 5 .   ? 33.606 -7.130  4.348   1.00 16.46 ?  373 HOH   A O    1 
HETATM 6687 O  O    . HOH   F 5 .   ? 24.396 3.587   -1.798  1.00 15.23 ?  374 HOH   A O    1 
HETATM 6688 O  O    . HOH   F 5 .   ? 21.192 10.269  14.969  1.00 35.33 ?  375 HOH   A O    1 
HETATM 6689 O  O    T HOH   F 5 .   ? 15.386 -0.385  2.361   0.30 12.73 ?  376 HOH   A O    1 
HETATM 6690 O  O    . HOH   F 5 .   ? 22.098 -19.203 11.436  1.00 35.91 ?  377 HOH   A O    1 
HETATM 6691 O  O    . HOH   F 5 .   ? 21.860 -21.882 8.480   1.00 29.61 ?  378 HOH   A O    1 
HETATM 6692 O  O    . HOH   F 5 .   ? 16.963 -19.214 4.870   1.00 16.18 ?  379 HOH   A O    1 
HETATM 6693 O  O    . HOH   F 5 .   ? 10.934 1.726   12.505  1.00 24.93 ?  380 HOH   A O    1 
HETATM 6694 O  O    A HOH   F 5 .   ? 17.476 -1.681  0.420   0.64 17.54 ?  381 HOH   A O    1 
HETATM 6695 O  O    . HOH   F 5 .   ? 31.807 -7.269  -9.808  1.00 22.22 ?  382 HOH   A O    1 
HETATM 6696 O  O    . HOH   F 5 .   ? 22.627 -11.898 21.784  1.00 48.84 ?  383 HOH   A O    1 
HETATM 6697 O  O    . HOH   F 5 .   ? 16.518 -22.030 0.997   1.00 27.78 ?  384 HOH   A O    1 
HETATM 6698 O  O    . HOH   F 5 .   ? 24.139 3.934   -4.651  1.00 25.99 ?  385 HOH   A O    1 
HETATM 6699 O  O    . HOH   F 5 .   ? 33.502 -16.921 8.128   1.00 19.76 ?  386 HOH   A O    1 
HETATM 6700 O  O    . HOH   F 5 .   ? 24.131 -7.699  14.414  1.00 17.44 ?  387 HOH   A O    1 
HETATM 6701 O  O    . HOH   F 5 .   ? 15.154 -21.465 14.206  1.00 19.09 ?  388 HOH   A O    1 
HETATM 6702 O  O    . HOH   F 5 .   ? 27.416 -10.564 14.065  1.00 18.42 ?  389 HOH   A O    1 
HETATM 6703 O  O    . HOH   F 5 .   ? 21.330 3.070   -0.285  1.00 13.76 ?  390 HOH   A O    1 
HETATM 6704 O  O    . HOH   F 5 .   ? 24.626 -17.460 12.711  1.00 24.58 ?  391 HOH   A O    1 
HETATM 6705 O  O    . HOH   F 5 .   ? 32.742 -9.219  5.994   1.00 20.25 ?  392 HOH   A O    1 
HETATM 6706 O  O    A HOH   F 5 .   ? 24.570 2.057   -7.009  0.64 16.07 ?  393 HOH   A O    1 
HETATM 6707 O  O    . HOH   F 5 .   ? 11.626 -10.685 16.934  1.00 25.90 ?  394 HOH   A O    1 
HETATM 6708 O  O    A HOH   F 5 .   ? 15.776 -0.904  5.246   0.64 17.95 ?  395 HOH   A O    1 
HETATM 6709 O  O    B HOH   F 5 .   ? 11.937 -1.654  -3.226  0.36 20.97 ?  396 HOH   A O    1 
HETATM 6710 O  O    . HOH   F 5 .   ? 37.530 -2.011  5.849   1.00 26.34 ?  397 HOH   A O    1 
HETATM 6711 O  O    . HOH   F 5 .   ? 21.797 -13.784 -8.170  1.00 41.07 ?  398 HOH   A O    1 
HETATM 6712 O  O    . HOH   F 5 .   ? 8.026  -21.472 4.075   1.00 47.48 ?  399 HOH   A O    1 
HETATM 6713 O  O    . HOH   F 5 .   ? 14.024 -23.010 7.424   1.00 19.01 ?  400 HOH   A O    1 
HETATM 6714 O  O    . HOH   F 5 .   ? 23.461 11.394  4.061   1.00 12.48 ?  401 HOH   A O    1 
HETATM 6715 O  O    A HOH   F 5 .   ? 11.046 -0.342  1.905   0.34 17.97 ?  402 HOH   A O    1 
HETATM 6716 O  O    . HOH   F 5 .   ? 5.366  2.867   4.917   1.00 33.46 ?  403 HOH   A O    1 
HETATM 6717 O  O    . HOH   F 5 .   ? 18.889 -0.754  -1.650  1.00 14.96 ?  404 HOH   A O    1 
HETATM 6718 O  O    . HOH   F 5 .   ? 13.863 -4.852  17.337  1.00 28.10 ?  405 HOH   A O    1 
HETATM 6719 O  O    . HOH   F 5 .   ? 15.813 2.147   24.665  1.00 44.68 ?  406 HOH   A O    1 
HETATM 6720 O  O    . HOH   F 5 .   ? 23.927 -15.698 -9.204  1.00 36.61 ?  407 HOH   A O    1 
HETATM 6721 O  O    . HOH   F 5 .   ? 14.493 -24.628 11.599  1.00 40.51 ?  408 HOH   A O    1 
HETATM 6722 O  O    . HOH   F 5 .   ? 23.921 -20.253 -1.328  1.00 17.47 ?  409 HOH   A O    1 
HETATM 6723 O  O    . HOH   F 5 .   ? 27.283 2.340   18.692  1.00 33.01 ?  410 HOH   A O    1 
HETATM 6724 O  O    . HOH   F 5 .   ? 15.166 -8.070  -9.758  1.00 23.39 ?  411 HOH   A O    1 
HETATM 6725 O  O    . HOH   F 5 .   ? 6.698  -3.160  12.762  1.00 30.09 ?  412 HOH   A O    1 
HETATM 6726 O  O    . HOH   F 5 .   ? 30.637 1.909   16.680  1.00 21.66 ?  413 HOH   A O    1 
HETATM 6727 O  O    A HOH   F 5 .   ? 20.088 4.561   -7.575  0.64 18.09 ?  414 HOH   A O    1 
HETATM 6728 O  O    . HOH   F 5 .   ? 29.987 -10.058 13.006  1.00 22.86 ?  415 HOH   A O    1 
HETATM 6729 O  O    . HOH   F 5 .   ? 26.917 4.175   -0.663  1.00 12.92 ?  416 HOH   A O    1 
HETATM 6730 O  O    . HOH   F 5 .   ? 20.536 -19.991 2.766   1.00 19.42 ?  417 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 30.252 -12.864 13.530  1.00 20.84 ?  418 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 5 .   ? 38.068 -1.340  -1.894  1.00 19.43 ?  419 HOH   A O    1 
HETATM 6733 O  O    . HOH   F 5 .   ? 16.139 16.632  8.579   1.00 36.59 ?  420 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 5 .   ? 32.654 -4.294  -9.872  1.00 28.20 ?  421 HOH   A O    1 
HETATM 6735 O  O    . HOH   F 5 .   ? 35.089 -5.221  -3.079  1.00 17.87 ?  422 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 5 .   ? 40.916 -8.241  -6.821  1.00 36.56 ?  423 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 10.362 -13.703 -1.710  1.00 17.15 ?  424 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 36.692 -4.929  5.402   1.00 23.75 ?  425 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 44.933 -0.621  3.024   1.00 39.88 ?  426 HOH   A O    1 
HETATM 6740 O  O    . HOH   F 5 .   ? 15.973 6.855   2.919   1.00 20.00 ?  427 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 32.482 -10.650 3.254   1.00 32.94 ?  428 HOH   A O    1 
HETATM 6742 O  O    . HOH   F 5 .   ? 41.588 1.543   5.073   1.00 39.89 ?  429 HOH   A O    1 
HETATM 6743 O  O    . HOH   F 5 .   ? 22.604 8.221   18.350  1.00 47.38 ?  430 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 16.179 -14.173 20.139  1.00 51.63 ?  431 HOH   A O    1 
HETATM 6745 O  O    . HOH   F 5 .   ? 19.394 -11.054 24.024  1.00 71.80 ?  432 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 23.470 -7.954  17.083  1.00 22.22 ?  433 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 5 .   ? 23.153 7.588   -3.234  1.00 30.93 ?  434 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 27.015 -3.096  19.382  1.00 38.03 ?  435 HOH   A O    1 
HETATM 6749 O  O    A HOH   F 5 .   ? 18.565 -2.457  -16.358 0.64 35.55 ?  436 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 18.462 4.893   -15.122 1.00 50.60 ?  437 HOH   A O    1 
HETATM 6751 O  O    . HOH   F 5 .   ? 23.351 -20.881 1.368   1.00 19.01 ?  438 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 37.723 -8.828  -3.420  1.00 23.89 ?  439 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? 18.823 1.979   -0.691  1.00 13.81 ?  440 HOH   A O    1 
HETATM 6754 O  O    . HOH   F 5 .   ? -1.419 -4.861  7.541   1.00 42.29 ?  441 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 21.247 -9.143  21.320  1.00 53.66 ?  442 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 34.380 -8.076  -0.540  1.00 28.07 ?  443 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? 10.380 -22.207 -1.216  1.00 51.54 ?  444 HOH   A O    1 
HETATM 6758 O  O    B HOH   F 5 .   ? 8.445  3.932   1.063   0.36 25.42 ?  445 HOH   A O    1 
HETATM 6759 O  O    A HOH   F 5 .   ? 14.005 -0.299  3.435   0.34 24.10 ?  446 HOH   A O    1 
HETATM 6760 O  O    A HOH   F 5 .   ? 16.242 2.978   -1.471  0.64 18.87 ?  447 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 18.322 -15.992 16.323  1.00 39.60 ?  448 HOH   A O    1 
HETATM 6762 O  O    . HOH   F 5 .   ? 31.306 -12.752 0.023   1.00 20.12 ?  449 HOH   A O    1 
HETATM 6763 O  O    . HOH   F 5 .   ? 30.576 14.767  2.733   1.00 19.06 ?  450 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 9.418  -16.265 -2.017  1.00 43.84 ?  451 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 20.532 -17.713 24.834  1.00 54.27 ?  452 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? 21.492 -14.648 17.945  1.00 52.67 ?  453 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 29.726 -2.007  -12.789 1.00 46.51 ?  454 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 29.831 -16.037 10.793  1.00 34.77 ?  455 HOH   A O    1 
HETATM 6769 O  O    . HOH   F 5 .   ? 27.761 7.042   -6.569  1.00 38.68 ?  456 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 32.413 -15.855 10.898  1.00 30.19 ?  457 HOH   A O    1 
HETATM 6771 O  O    . HOH   F 5 .   ? 25.384 8.239   -4.827  1.00 33.01 ?  458 HOH   A O    1 
HETATM 6772 O  O    . HOH   F 5 .   ? 24.781 5.728   20.726  1.00 49.86 ?  459 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 19.868 -17.340 -5.037  1.00 24.41 ?  460 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 23.171 -22.311 -3.276  1.00 40.39 ?  461 HOH   A O    1 
HETATM 6775 O  O    B HOH   F 5 .   ? 12.543 -3.148  1.496   0.36 25.76 ?  462 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 24.602 14.641  7.774   1.00 34.82 ?  463 HOH   A O    1 
HETATM 6777 O  O    . HOH   F 5 .   ? 18.754 10.893  11.277  1.00 32.77 ?  464 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 15.715 -21.480 3.691   1.00 24.42 ?  465 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 39.613 -7.016  -3.499  1.00 44.99 ?  466 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 23.454 13.705  5.481   1.00 18.50 ?  467 HOH   A O    1 
HETATM 6781 O  O    A HOH   F 5 .   ? 21.953 5.287   -5.864  0.64 27.02 ?  468 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 27.422 -11.305 16.598  1.00 37.57 ?  469 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 26.919 11.660  -1.370  1.00 34.25 ?  470 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? 11.037 -15.001 -6.092  1.00 34.95 ?  471 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 12.283 1.642   17.262  1.00 41.54 ?  472 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 11.970 -13.374 16.340  1.00 56.11 ?  473 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 25.790 10.797  -3.749  1.00 27.54 ?  474 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 18.064 -16.181 -8.882  1.00 39.49 ?  475 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 28.799 9.065   17.502  1.00 36.56 ?  476 HOH   A O    1 
HETATM 6790 O  O    . HOH   F 5 .   ? 15.676 -17.125 -6.993  1.00 30.86 ?  477 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 41.031 -3.960  -0.347  1.00 37.61 ?  478 HOH   A O    1 
HETATM 6792 O  O    . HOH   F 5 .   ? 35.190 7.522   12.217  1.00 48.79 ?  479 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 17.312 -18.682 19.856  1.00 53.54 ?  480 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 13.950 -10.323 -10.917 1.00 32.79 ?  481 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 30.799 0.725   19.117  1.00 40.04 ?  482 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 23.100 11.839  -4.063  1.00 20.05 ?  483 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 44.496 10.371  -1.647  1.00 32.29 ?  484 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 16.806 -20.482 16.092  1.00 29.39 ?  485 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 28.601 -4.682  -12.296 1.00 36.95 ?  486 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 23.201 -12.847 19.283  1.00 49.37 ?  487 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 41.725 9.408   -3.923  1.00 30.66 ?  488 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 28.660 -7.961  -15.250 1.00 51.48 ?  489 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 39.151 2.427   7.444   1.00 31.30 ?  490 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 13.855 -25.153 8.897   1.00 34.91 ?  491 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 18.335 -23.180 1.900   1.00 45.78 ?  492 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 31.476 -0.570  -10.551 1.00 29.10 ?  493 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 16.024 -6.803  -11.885 1.00 42.98 ?  494 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 40.577 -0.254  -7.805  1.00 33.65 ?  495 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 20.054 -22.310 4.222   1.00 29.81 ?  496 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 16.202 -23.361 5.781   1.00 31.27 ?  497 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 8.047  -3.183  -5.791  1.00 46.06 ?  498 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 30.757 5.814   -14.768 1.00 34.25 ?  499 HOH   A O    1 
HETATM 6813 O  O    B HOH   F 5 .   ? 9.733  0.481   -2.093  0.36 25.36 ?  500 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 20.490 -16.071 -7.373  1.00 28.79 ?  501 HOH   A O    1 
HETATM 6815 O  O    B HOH   F 5 .   ? 14.782 7.835   4.709   0.36 26.53 ?  502 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 37.352 -6.610  7.648   1.00 26.81 ?  503 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 30.735 -5.852  -11.897 1.00 45.87 ?  504 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 39.483 0.017   6.627   1.00 32.53 ?  505 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 29.009 14.470  0.813   1.00 50.14 ?  506 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 37.957 13.994  6.718   1.00 43.56 ?  507 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 36.434 -6.473  10.237  1.00 47.23 ?  508 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 21.995 -23.978 4.473   1.00 26.76 ?  509 HOH   A O    1 
HETATM 6823 O  O    T HOH   F 5 .   ? 11.905 -2.119  -3.680  0.30 12.29 ?  510 HOH   A O    1 
HETATM 6824 O  O    A HOH   F 5 .   ? 14.832 8.692   4.849   0.64 37.57 ?  511 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 17.204 -6.610  -14.224 1.00 42.92 ?  512 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 24.058 9.044   -7.226  1.00 38.34 ?  513 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 15.773 -12.155 27.406  1.00 45.75 ?  514 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 16.342 -21.100 18.773  1.00 39.45 ?  515 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 14.708 -22.715 19.825  1.00 36.50 ?  516 HOH   A O    1 
HETATM 6830 O  O    . HOH   G 5 .   ? 29.827 -22.397 5.547   1.00 21.30 ?  201 HOH   B O    1 
HETATM 6831 O  O    . HOH   G 5 .   ? 41.668 -36.050 -17.063 1.00 34.08 ?  202 HOH   B O    1 
HETATM 6832 O  O    . HOH   G 5 .   ? 27.684 -29.131 -1.790  1.00 36.96 ?  203 HOH   B O    1 
HETATM 6833 O  O    . HOH   G 5 .   ? 59.124 -18.692 6.870   1.00 35.55 ?  204 HOH   B O    1 
HETATM 6834 O  O    . HOH   G 5 .   ? 37.991 -39.418 -0.118  1.00 39.06 ?  205 HOH   B O    1 
HETATM 6835 O  O    . HOH   G 5 .   ? 41.334 -7.789  5.471   1.00 42.62 ?  206 HOH   B O    1 
HETATM 6836 O  O    . HOH   G 5 .   ? 30.975 -28.723 4.448   1.00 29.26 ?  207 HOH   B O    1 
HETATM 6837 O  O    . HOH   G 5 .   ? 52.931 -13.477 -20.238 1.00 33.43 ?  208 HOH   B O    1 
HETATM 6838 O  O    . HOH   G 5 .   ? 27.884 -41.817 -15.091 1.00 37.49 ?  209 HOH   B O    1 
HETATM 6839 O  O    . HOH   G 5 .   ? 48.065 -6.909  15.546  1.00 32.67 ?  210 HOH   B O    1 
HETATM 6840 O  O    . HOH   G 5 .   ? 54.485 -9.422  -8.673  1.00 19.35 ?  211 HOH   B O    1 
HETATM 6841 O  O    . HOH   G 5 .   ? 30.206 -40.990 -8.006  1.00 17.57 ?  212 HOH   B O    1 
HETATM 6842 O  O    . HOH   G 5 .   ? 58.187 -12.895 8.448   1.00 30.80 ?  213 HOH   B O    1 
HETATM 6843 O  O    . HOH   G 5 .   ? 56.334 -19.690 7.273   1.00 32.16 ?  214 HOH   B O    1 
HETATM 6844 O  O    . HOH   G 5 .   ? 50.160 -3.381  7.146   1.00 35.14 ?  215 HOH   B O    1 
HETATM 6845 O  O    . HOH   G 5 .   ? 29.940 -26.253 4.116   1.00 28.87 ?  216 HOH   B O    1 
HETATM 6846 O  O    . HOH   G 5 .   ? 49.384 -22.732 -19.745 1.00 48.72 ?  217 HOH   B O    1 
HETATM 6847 O  O    . HOH   G 5 .   ? 37.091 -19.820 -18.090 1.00 40.98 ?  218 HOH   B O    1 
HETATM 6848 O  O    . HOH   G 5 .   ? 57.721 -24.475 5.055   1.00 39.28 ?  219 HOH   B O    1 
HETATM 6849 O  O    . HOH   G 5 .   ? 34.891 -24.642 13.823  1.00 38.88 ?  220 HOH   B O    1 
HETATM 6850 O  O    . HOH   G 5 .   ? 57.120 -26.889 -7.606  1.00 39.94 ?  221 HOH   B O    1 
HETATM 6851 O  O    . HOH   G 5 .   ? 56.630 -30.773 -7.708  1.00 29.58 ?  222 HOH   B O    1 
HETATM 6852 O  O    . HOH   G 5 .   ? 41.499 -39.194 -14.792 1.00 22.90 ?  223 HOH   B O    1 
HETATM 6853 O  O    . HOH   G 5 .   ? 44.406 -7.179  2.022   1.00 33.92 ?  224 HOH   B O    1 
HETATM 6854 O  O    . HOH   G 5 .   ? 55.396 -16.585 -14.294 1.00 33.63 ?  225 HOH   B O    1 
HETATM 6855 O  O    . HOH   G 5 .   ? 34.520 -36.378 -7.116  1.00 19.68 ?  226 HOH   B O    1 
HETATM 6856 O  O    . HOH   G 5 .   ? 47.414 -7.354  -3.836  1.00 40.49 ?  227 HOH   B O    1 
HETATM 6857 O  O    . HOH   G 5 .   ? 50.761 -6.096  0.154   1.00 27.05 ?  228 HOH   B O    1 
HETATM 6858 O  O    . HOH   G 5 .   ? 57.387 -16.290 -12.187 1.00 18.71 ?  229 HOH   B O    1 
HETATM 6859 O  O    . HOH   G 5 .   ? 51.662 -6.466  4.393   1.00 20.00 ?  230 HOH   B O    1 
HETATM 6860 O  O    . HOH   G 5 .   ? 44.894 -43.579 -10.477 1.00 29.28 ?  231 HOH   B O    1 
HETATM 6861 O  O    . HOH   G 5 .   ? 45.100 -34.960 6.847   1.00 43.37 ?  232 HOH   B O    1 
HETATM 6862 O  O    . HOH   G 5 .   ? 46.395 -1.562  13.197  1.00 27.78 ?  233 HOH   B O    1 
HETATM 6863 O  O    . HOH   G 5 .   ? 32.776 -43.776 -11.260 1.00 21.84 ?  234 HOH   B O    1 
HETATM 6864 O  O    . HOH   G 5 .   ? 50.719 -12.979 -0.453  1.00 12.05 ?  235 HOH   B O    1 
HETATM 6865 O  O    . HOH   G 5 .   ? 41.356 -9.605  13.091  1.00 22.63 ?  236 HOH   B O    1 
HETATM 6866 O  O    . HOH   G 5 .   ? 35.999 -43.331 -8.340  1.00 37.07 ?  237 HOH   B O    1 
HETATM 6867 O  O    . HOH   G 5 .   ? 44.496 -27.704 -0.641  1.00 22.90 ?  238 HOH   B O    1 
HETATM 6868 O  O    . HOH   G 5 .   ? 40.624 -16.051 14.115  1.00 23.47 ?  239 HOH   B O    1 
HETATM 6869 O  O    . HOH   G 5 .   ? 35.082 -7.996  -2.979  1.00 18.29 ?  240 HOH   B O    1 
HETATM 6870 O  O    . HOH   G 5 .   ? 29.811 -34.134 -0.382  1.00 36.12 ?  241 HOH   B O    1 
HETATM 6871 O  O    . HOH   G 5 .   ? 48.552 -36.504 -15.449 1.00 46.93 ?  242 HOH   B O    1 
HETATM 6872 O  O    . HOH   G 5 .   ? 42.562 -25.345 2.703   1.00 15.39 ?  243 HOH   B O    1 
HETATM 6873 O  O    . HOH   G 5 .   ? 39.515 -11.114 0.359   1.00 16.86 ?  244 HOH   B O    1 
HETATM 6874 O  O    . HOH   G 5 .   ? 25.393 -25.892 -1.200  1.00 32.44 ?  245 HOH   B O    1 
HETATM 6875 O  O    . HOH   G 5 .   ? 43.155 -32.417 -16.997 1.00 25.40 ?  246 HOH   B O    1 
HETATM 6876 O  O    . HOH   G 5 .   ? 43.020 -43.229 -8.097  1.00 30.31 ?  247 HOH   B O    1 
HETATM 6877 O  O    . HOH   G 5 .   ? 51.538 -13.831 11.031  1.00 26.93 ?  248 HOH   B O    1 
HETATM 6878 O  O    . HOH   G 5 .   ? 42.622 -22.844 3.893   1.00 12.10 ?  249 HOH   B O    1 
HETATM 6879 O  O    . HOH   G 5 .   ? 38.466 -11.051 -2.232  1.00 19.27 ?  250 HOH   B O    1 
HETATM 6880 O  O    . HOH   G 5 .   ? 28.401 -19.701 -13.101 1.00 24.85 ?  251 HOH   B O    1 
HETATM 6881 O  O    . HOH   G 5 .   ? 39.300 -10.815 6.148   1.00 25.05 ?  252 HOH   B O    1 
HETATM 6882 O  O    . HOH   G 5 .   ? 57.585 -24.381 -3.789  1.00 21.63 ?  253 HOH   B O    1 
HETATM 6883 O  O    . HOH   G 5 .   ? 34.276 -18.366 11.465  1.00 26.00 ?  254 HOH   B O    1 
HETATM 6884 O  O    . HOH   G 5 .   ? 41.858 -23.472 9.321   1.00 19.16 ?  255 HOH   B O    1 
HETATM 6885 O  O    . HOH   G 5 .   ? 30.517 -42.205 -10.535 1.00 31.42 ?  256 HOH   B O    1 
HETATM 6886 O  O    . HOH   G 5 .   ? 50.921 -39.948 -8.157  1.00 37.07 ?  257 HOH   B O    1 
HETATM 6887 O  O    . HOH   G 5 .   ? 40.316 -12.759 -11.478 1.00 15.70 ?  258 HOH   B O    1 
HETATM 6888 O  O    . HOH   G 5 .   ? 58.197 -10.670 -4.024  1.00 20.56 ?  259 HOH   B O    1 
HETATM 6889 O  O    . HOH   G 5 .   ? 30.846 -15.703 2.702   1.00 14.17 ?  260 HOH   B O    1 
HETATM 6890 O  O    . HOH   G 5 .   ? 29.715 -25.205 -10.709 1.00 17.88 ?  261 HOH   B O    1 
HETATM 6891 O  O    . HOH   G 5 .   ? 38.908 -11.916 12.333  1.00 36.90 ?  262 HOH   B O    1 
HETATM 6892 O  O    . HOH   G 5 .   ? 31.762 -17.886 -14.447 1.00 31.49 ?  263 HOH   B O    1 
HETATM 6893 O  O    . HOH   G 5 .   ? 27.113 -31.810 -9.888  1.00 20.45 ?  264 HOH   B O    1 
HETATM 6894 O  O    . HOH   G 5 .   ? 49.711 -0.476  10.164  1.00 30.02 ?  265 HOH   B O    1 
HETATM 6895 O  O    . HOH   G 5 .   ? 42.346 -9.913  9.367   1.00 21.03 ?  266 HOH   B O    1 
HETATM 6896 O  O    . HOH   G 5 .   ? 43.355 -15.798 -12.128 1.00 14.93 ?  267 HOH   B O    1 
HETATM 6897 O  O    . HOH   G 5 .   ? 48.008 -22.766 5.865   1.00 17.81 ?  268 HOH   B O    1 
HETATM 6898 O  O    . HOH   G 5 .   ? 47.986 -24.503 -17.746 1.00 32.86 ?  269 HOH   B O    1 
HETATM 6899 O  O    . HOH   G 5 .   ? 56.129 -23.596 -14.661 1.00 28.52 ?  270 HOH   B O    1 
HETATM 6900 O  O    . HOH   G 5 .   ? 28.460 -30.913 -14.642 1.00 31.49 ?  271 HOH   B O    1 
HETATM 6901 O  O    . HOH   G 5 .   ? 46.860 -29.496 9.831   1.00 32.03 ?  272 HOH   B O    1 
HETATM 6902 O  O    . HOH   G 5 .   ? 28.241 -34.346 -9.341  1.00 18.25 ?  273 HOH   B O    1 
HETATM 6903 O  O    . HOH   G 5 .   ? 49.303 -28.702 -6.813  1.00 16.18 ?  274 HOH   B O    1 
HETATM 6904 O  O    . HOH   G 5 .   ? 57.475 -9.216  1.448   1.00 20.59 ?  275 HOH   B O    1 
HETATM 6905 O  O    . HOH   G 5 .   ? 42.394 -34.676 3.823   1.00 27.58 ?  276 HOH   B O    1 
HETATM 6906 O  O    . HOH   G 5 .   ? 46.586 -31.248 -4.729  1.00 23.48 ?  277 HOH   B O    1 
HETATM 6907 O  O    . HOH   G 5 .   ? 56.931 -8.627  8.440   1.00 19.34 ?  278 HOH   B O    1 
HETATM 6908 O  O    . HOH   G 5 .   ? 59.781 -15.244 8.151   1.00 31.75 ?  279 HOH   B O    1 
HETATM 6909 O  O    . HOH   G 5 .   ? 42.895 -20.273 -20.671 1.00 38.65 ?  280 HOH   B O    1 
HETATM 6910 O  O    . HOH   G 5 .   ? 41.128 -5.522  11.542  1.00 45.82 ?  281 HOH   B O    1 
HETATM 6911 O  O    . HOH   G 5 .   ? 47.049 -33.976 -4.582  1.00 18.38 ?  282 HOH   B O    1 
HETATM 6912 O  O    . HOH   G 5 .   ? 34.941 -33.330 -19.153 1.00 40.16 ?  283 HOH   B O    1 
HETATM 6913 O  O    . HOH   G 5 .   ? 27.573 -26.695 -15.560 1.00 33.33 ?  284 HOH   B O    1 
HETATM 6914 O  O    . HOH   G 5 .   ? 48.395 -25.026 3.153   1.00 14.03 ?  285 HOH   B O    1 
HETATM 6915 O  O    . HOH   G 5 .   ? 34.449 -12.736 2.659   1.00 24.91 ?  286 HOH   B O    1 
HETATM 6916 O  O    . HOH   G 5 .   ? 27.928 -22.880 -7.910  1.00 18.30 ?  287 HOH   B O    1 
HETATM 6917 O  O    . HOH   G 5 .   ? 33.507 -15.284 -13.866 1.00 21.48 ?  288 HOH   B O    1 
HETATM 6918 O  O    . HOH   G 5 .   ? 52.484 -10.386 12.999  1.00 22.57 ?  289 HOH   B O    1 
HETATM 6919 O  O    . HOH   G 5 .   ? 48.678 -20.002 5.978   1.00 14.24 ?  290 HOH   B O    1 
HETATM 6920 O  O    . HOH   G 5 .   ? 57.059 -12.056 12.375  1.00 39.38 ?  291 HOH   B O    1 
HETATM 6921 O  O    . HOH   G 5 .   ? 36.793 -12.759 -1.456  1.00 27.88 ?  292 HOH   B O    1 
HETATM 6922 O  O    . HOH   G 5 .   ? 51.179 -37.578 -9.561  1.00 27.61 ?  293 HOH   B O    1 
HETATM 6923 O  O    . HOH   G 5 .   ? 45.286 -33.402 -15.865 1.00 25.33 ?  294 HOH   B O    1 
HETATM 6924 O  O    . HOH   G 5 .   ? 51.695 -5.986  -7.899  1.00 45.50 ?  295 HOH   B O    1 
HETATM 6925 O  O    . HOH   G 5 .   ? 49.887 -24.694 5.854   1.00 32.44 ?  296 HOH   B O    1 
HETATM 6926 O  O    . HOH   G 5 .   ? 42.702 -12.282 -18.446 1.00 30.10 ?  297 HOH   B O    1 
HETATM 6927 O  O    . HOH   G 5 .   ? 37.441 -17.988 13.127  1.00 32.26 ?  298 HOH   B O    1 
HETATM 6928 O  O    . HOH   G 5 .   ? 35.066 -33.577 4.634   1.00 31.23 ?  299 HOH   B O    1 
HETATM 6929 O  O    . HOH   G 5 .   ? 42.340 -9.886  -14.842 1.00 39.75 ?  300 HOH   B O    1 
HETATM 6930 O  O    . HOH   G 5 .   ? 25.946 -21.462 -3.456  1.00 17.14 ?  301 HOH   B O    1 
HETATM 6931 O  O    . HOH   G 5 .   ? 44.619 -27.436 2.076   1.00 15.77 ?  302 HOH   B O    1 
HETATM 6932 O  O    . HOH   G 5 .   ? 44.012 -29.346 -4.620  1.00 23.41 ?  303 HOH   B O    1 
HETATM 6933 O  O    . HOH   G 5 .   ? 45.879 -40.403 -3.491  1.00 30.46 ?  304 HOH   B O    1 
HETATM 6934 O  O    . HOH   G 5 .   ? 53.456 -30.183 4.563   1.00 19.00 ?  305 HOH   B O    1 
HETATM 6935 O  O    . HOH   G 5 .   ? 53.026 -16.053 -12.721 1.00 27.01 ?  306 HOH   B O    1 
HETATM 6936 O  O    . HOH   G 5 .   ? 40.246 -10.853 -9.498  1.00 17.55 ?  307 HOH   B O    1 
HETATM 6937 O  O    . HOH   G 5 .   ? 52.572 -35.649 -8.673  1.00 29.59 ?  308 HOH   B O    1 
HETATM 6938 O  O    . HOH   G 5 .   ? 43.210 -21.384 10.702  1.00 16.36 ?  309 HOH   B O    1 
HETATM 6939 O  O    . HOH   G 5 .   ? 52.461 -29.247 -13.012 1.00 26.32 ?  310 HOH   B O    1 
HETATM 6940 O  O    . HOH   G 5 .   ? 37.860 -10.246 -10.722 1.00 17.84 ?  311 HOH   B O    1 
HETATM 6941 O  O    . HOH   G 5 .   ? 32.804 -34.561 -5.815  1.00 17.66 ?  312 HOH   B O    1 
HETATM 6942 O  O    . HOH   G 5 .   ? 26.332 -21.021 -6.186  1.00 16.82 ?  313 HOH   B O    1 
HETATM 6943 O  O    . HOH   G 5 .   ? 38.375 -9.367  -13.246 1.00 28.17 ?  314 HOH   B O    1 
HETATM 6944 O  O    . HOH   G 5 .   ? 41.751 -8.048  1.376   1.00 24.75 ?  315 HOH   B O    1 
HETATM 6945 O  O    . HOH   G 5 .   ? 62.708 -13.573 4.768   1.00 27.78 ?  316 HOH   B O    1 
HETATM 6946 O  O    . HOH   G 5 .   ? 38.315 -12.671 7.963   1.00 18.35 ?  317 HOH   B O    1 
HETATM 6947 O  O    . HOH   G 5 .   ? 53.621 -12.575 -22.146 1.00 32.23 ?  318 HOH   B O    1 
HETATM 6948 O  O    . HOH   G 5 .   ? 48.583 -12.054 -14.159 1.00 27.19 ?  319 HOH   B O    1 
HETATM 6949 O  O    . HOH   G 5 .   ? 37.116 -30.550 -20.952 1.00 30.91 ?  320 HOH   B O    1 
HETATM 6950 O  O    . HOH   G 5 .   ? 43.523 -15.409 18.157  1.00 32.53 ?  321 HOH   B O    1 
HETATM 6951 O  O    . HOH   G 5 .   ? 62.867 -20.183 -0.769  1.00 37.40 ?  322 HOH   B O    1 
HETATM 6952 O  O    . HOH   G 5 .   ? 59.937 -17.199 -10.446 1.00 34.35 ?  323 HOH   B O    1 
HETATM 6953 O  O    . HOH   G 5 .   ? 37.240 -35.646 7.299   1.00 33.79 ?  324 HOH   B O    1 
HETATM 6954 O  O    . HOH   G 5 .   ? 44.625 -24.559 9.610   1.00 21.65 ?  325 HOH   B O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 36.723 -12.386 4.298   1.00 18.18 ?  326 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 51.371 -33.030 -10.781 1.00 43.70 ?  327 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 47.209 -24.449 8.234   1.00 24.52 ?  328 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 43.111 -34.573 0.175   1.00 21.53 ?  329 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 44.127 -1.732  7.672   1.00 47.13 ?  330 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 57.543 -21.965 3.397   1.00 30.99 ?  331 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 48.082 -32.669 -16.614 1.00 42.19 ?  332 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 27.824 -14.778 -9.434  1.00 37.50 ?  333 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 33.606 -31.145 11.103  1.00 35.38 ?  334 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 41.248 -24.478 15.876  1.00 45.61 ?  335 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 47.446 -27.424 2.078   1.00 15.30 ?  336 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 42.833 -43.471 -14.299 1.00 43.38 ?  337 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 45.669 -36.271 -16.049 1.00 37.25 ?  338 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 46.819 -19.856 12.278  1.00 28.97 ?  339 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 38.441 -12.210 -16.212 1.00 45.48 ?  340 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 37.038 -15.114 -16.503 1.00 43.33 ?  341 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 28.887 -42.905 -12.275 1.00 37.68 ?  342 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 34.469 -10.326 7.745   1.00 23.21 ?  343 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 37.034 -45.206 -9.644  1.00 36.55 ?  344 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 33.004 -14.670 1.090   1.00 19.30 ?  345 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 39.569 -23.601 -20.388 1.00 37.67 ?  346 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 38.592 -22.356 15.043  1.00 43.01 ?  347 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 39.796 -44.220 -11.136 1.00 42.31 ?  348 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 33.684 -9.616  -8.836  1.00 32.43 ?  349 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 40.397 -43.471 -9.046  1.00 26.87 ?  350 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 62.506 -20.110 -4.798  1.00 43.98 ?  351 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 27.771 -26.566 -0.500  1.00 30.77 ?  352 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 44.149 -37.364 -17.686 1.00 34.18 ?  353 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 55.669 -8.251  10.818  1.00 24.14 ?  354 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 56.554 -7.282  3.093   1.00 25.07 ?  355 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 36.092 -8.543  -9.714  1.00 35.35 ?  356 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 23.180 -23.620 6.849   1.00 35.50 ?  357 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 34.070 -7.748  11.482  1.00 39.96 ?  358 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 61.482 -19.904 1.730   1.00 36.94 ?  359 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 56.863 -21.604 -16.312 1.00 41.21 ?  360 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 40.251 -8.805  9.897   1.00 35.23 ?  361 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 27.139 -25.923 -11.296 1.00 35.18 ?  362 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 43.148 -12.678 -21.154 1.00 43.67 ?  363 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 40.248 -11.326 -13.898 1.00 33.09 ?  364 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 48.274 -26.446 8.884   1.00 40.64 ?  365 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 54.192 -5.742  3.003   1.00 35.55 ?  366 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 32.553 -23.592 14.095  1.00 39.47 ?  367 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 36.113 -8.630  8.992   1.00 36.33 ?  368 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 58.890 -10.433 9.225   1.00 38.71 ?  369 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 39.859 -7.015  7.853   1.00 37.85 ?  370 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 56.024 -7.825  -0.623  1.00 33.99 ?  371 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 41.793 -10.044 -17.446 1.00 55.90 ?  372 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 52.039 -12.916 13.367  1.00 30.07 ?  373 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 62.982 -12.373 6.951   1.00 37.31 ?  374 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 41.831 -6.725  -4.867  1.00 45.99 ?  375 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 42.662 -17.100 -23.065 1.00 45.29 ?  376 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 38.009 -10.533 10.037  1.00 29.24 ?  377 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 40.112 -7.695  3.193   1.00 35.95 ?  378 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 36.507 -22.789 13.307  1.00 30.33 ?  379 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 44.040 -5.599  -3.510  1.00 44.13 ?  380 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 39.632 -14.000 15.690  1.00 47.69 ?  381 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 52.844 -29.851 7.255   1.00 23.11 ?  382 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 60.465 -22.238 2.931   1.00 46.63 ?  383 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 46.824 -5.354  2.875   1.00 40.31 ?  384 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 25.808 -18.865 -11.853 1.00 40.01 ?  385 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 40.967 -9.744  15.833  1.00 48.61 ?  386 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 23.911 -20.879 -7.601  1.00 29.09 ?  387 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 35.392 -33.712 7.424   1.00 43.95 ?  388 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 35.264 -20.339 13.319  1.00 34.09 ?  389 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 23.129 -23.759 1.572   1.00 33.35 ?  390 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 40.702 -6.616  -0.842  1.00 25.37 ?  391 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 44.122 -31.745 -3.737  1.00 40.10 ?  392 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 26.610 -27.950 -13.392 1.00 36.24 ?  393 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 27.929 -27.069 2.272   1.00 30.71 ?  394 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 24.645 -20.599 -10.492 1.00 39.15 ?  395 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 50.641 -30.841 8.760   1.00 30.59 ?  396 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 26.852 -30.678 -12.566 1.00 29.57 ?  397 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 34.361 -33.455 9.698   1.00 37.43 ?  398 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 57.680 -6.582  -2.348  1.00 33.97 ?  399 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 45.717 -20.096 15.245  1.00 50.91 ?  400 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 40.932 -11.765 -22.261 1.00 40.92 ?  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   ? 0.7039 0.7223 0.8178 -0.0123 -0.0410 0.1024  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.7010 0.7194 0.8022 -0.0140 -0.0389 0.1017  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.6740 0.6964 0.7549 -0.0217 -0.0391 0.1019  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.6795 0.7022 0.7741 -0.0195 -0.0428 0.1062  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.7203 0.7357 0.8208 -0.0098 -0.0367 0.0992  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.7264 0.7403 0.8240 -0.0077 -0.0364 0.0985  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.7272 0.7420 0.8243 -0.0089 -0.0358 0.0984  3   VAL   A CG2 
16   N  N   . ASN   A 4   ? 0.6360 0.6628 0.6723 -0.0322 -0.0345 0.0957  4   ASN   A N   
17   C  CA  . ASN   A 4   ? 0.5928 0.6250 0.5808 -0.0434 -0.0279 0.0867  4   ASN   A CA  
18   C  C   . ASN   A 4   ? 0.5287 0.5781 0.5134 -0.0559 -0.0077 0.0523  4   ASN   A C   
19   O  O   . ASN   A 4   ? 0.5304 0.5815 0.5116 -0.0558 -0.0103 0.0556  4   ASN   A O   
20   C  CB  . ASN   A 4   ? 0.6077 0.6300 0.5454 -0.0427 -0.0394 0.1117  4   ASN   A CB  
21   C  CG  . ASN   A 4   ? 0.6181 0.6323 0.5082 -0.0425 -0.0502 0.1336  4   ASN   A CG  
22   O  OD1 . ASN   A 4   ? 0.6227 0.6329 0.4971 -0.0431 -0.0560 0.1418  4   ASN   A OD1 
23   N  ND2 . ASN   A 4   ? 0.6206 0.6328 0.5002 -0.0416 -0.0529 0.1427  4   ASN   A ND2 
30   N  N   A SER   A 5   ? 0.4897 0.5537 0.4744 -0.0684 0.0085  0.0324  5   SER   A N   
31   N  N   B SER   A 5   ? 0.4985 0.5481 0.4803 -0.0580 -0.0000 0.0350  5   SER   A N   
32   C  CA  A SER   A 5   ? 0.4477 0.5268 0.4334 -0.0818 0.0269  0.0121  5   SER   A CA  
33   C  CA  B SER   A 5   ? 0.4655 0.5159 0.4444 -0.0610 0.0090  0.0182  5   SER   A CA  
34   C  C   A SER   A 5   ? 0.3990 0.4872 0.3858 -0.0954 0.0449  0.0034  5   SER   A C   
35   C  C   B SER   A 5   ? 0.4271 0.4758 0.3990 -0.0639 0.0175  0.0097  5   SER   A C   
36   O  O   A SER   A 5   ? 0.4034 0.4923 0.3846 -0.0901 0.0488  -0.0043 5   SER   A O   
37   O  O   B SER   A 5   ? 0.4291 0.4785 0.3997 -0.0623 0.0168  0.0052  5   SER   A O   
38   C  CB  A SER   A 5   ? 0.4540 0.5371 0.4497 -0.0828 0.0277  0.0025  5   SER   A CB  
39   C  CB  B SER   A 5   ? 0.4702 0.5223 0.4592 -0.0619 0.0099  0.0114  5   SER   A CB  
40   O  OG  A SER   A 5   ? 0.4572 0.5423 0.4564 -0.0841 0.0283  -0.0021 5   SER   A OG  
41   O  OG  B SER   A 5   ? 0.4724 0.5255 0.4648 -0.0629 0.0102  0.0080  5   SER   A OG  
52   N  N   A PHE   A 6   ? 0.3427 0.4398 0.3262 -0.1156 0.0589  0.0102  6   PHE   A N   
53   N  N   B PHE   A 6   ? 0.3847 0.4317 0.3450 -0.0686 0.0271  0.0098  6   PHE   A N   
54   C  CA  A PHE   A 6   ? 0.2928 0.3919 0.2713 -0.1273 0.0646  0.0232  6   PHE   A CA  
55   C  CA  B PHE   A 6   ? 0.3430 0.3867 0.2928 -0.0722 0.0357  0.0136  6   PHE   A CA  
56   C  C   A PHE   A 6   ? 0.2821 0.3808 0.2618 -0.1276 0.0699  0.0191  6   PHE   A C   
57   C  C   B PHE   A 6   ? 0.3295 0.3708 0.2796 -0.0715 0.0493  0.0132  6   PHE   A C   
58   O  O   A PHE   A 6   ? 0.2872 0.3858 0.2903 -0.1256 0.0811  0.0309  6   PHE   A O   
59   O  O   B PHE   A 6   ? 0.3293 0.3701 0.2679 -0.0762 0.0579  0.0200  6   PHE   A O   
60   C  CB  A PHE   A 6   ? 0.2661 0.3560 0.2385 -0.1280 0.0485  0.0387  6   PHE   A CB  
61   C  CB  B PHE   A 6   ? 0.3199 0.3594 0.2650 -0.0725 0.0245  0.0157  6   PHE   A CB  
62   C  CG  A PHE   A 6   ? 0.2453 0.3259 0.2129 -0.1218 0.0381  0.0436  6   PHE   A CG  
63   C  CG  B PHE   A 6   ? 0.2990 0.3351 0.2436 -0.0721 0.0157  0.0146  6   PHE   A CG  
64   C  CD1 A PHE   A 6   ? 0.2352 0.3139 0.2076 -0.1137 0.0227  0.0382  6   PHE   A CD1 
65   C  CD1 B PHE   A 6   ? 0.2888 0.3246 0.2334 -0.0711 0.0097  0.0136  6   PHE   A CD1 
66   C  CD2 A PHE   A 6   ? 0.2519 0.3194 0.2258 -0.1030 0.0350  0.0439  6   PHE   A CD2 
67   C  CD2 B PHE   A 6   ? 0.2952 0.3259 0.2427 -0.0671 0.0133  0.0127  6   PHE   A CD2 
68   C  CE1 A PHE   A 6   ? 0.2316 0.3064 0.2065 -0.1095 0.0263  0.0414  6   PHE   A CE1 
69   C  CE1 B PHE   A 6   ? 0.2844 0.3182 0.2328 -0.0707 0.0112  0.0142  6   PHE   A CE1 
70   C  CE2 A PHE   A 6   ? 0.2482 0.3137 0.2324 -0.0951 0.0296  0.0392  6   PHE   A CE2 
71   C  CE2 B PHE   A 6   ? 0.2906 0.3195 0.2431 -0.0661 0.0110  0.0126  6   PHE   A CE2 
72   C  CZ  A PHE   A 6   ? 0.2405 0.3068 0.2194 -0.1005 0.0233  0.0385  6   PHE   A CZ  
73   C  CZ  B PHE   A 6   ? 0.2867 0.3170 0.2371 -0.0676 0.0090  0.0126  6   PHE   A CZ  
92   N  N   A SER   A 7   ? 0.2661 0.3621 0.2225 -0.1273 0.0616  0.0090  7   SER   A N   
93   N  N   B SER   A 7   ? 0.3170 0.3559 0.2814 -0.0643 0.0494  0.0061  7   SER   A N   
94   C  CA  A SER   A 7   ? 0.2618 0.3489 0.2188 -0.1109 0.0510  -0.0045 7   SER   A CA  
95   C  CA  B SER   A 7   ? 0.3081 0.3439 0.2906 -0.0531 0.0449  -0.0030 7   SER   A CA  
96   C  C   A SER   A 7   ? 0.2406 0.3062 0.1789 -0.1082 0.0498  -0.0053 7   SER   A C   
97   C  C   B SER   A 7   ? 0.2906 0.3230 0.2664 -0.0503 0.0470  -0.0046 7   SER   A C   
98   O  O   A SER   A 7   ? 0.2526 0.2952 0.1718 -0.1166 0.0531  -0.0063 7   SER   A O   
99   O  O   B SER   A 7   ? 0.2940 0.3245 0.2644 -0.0466 0.0404  -0.0061 7   SER   A O   
100  C  CB  A SER   A 7   ? 0.2810 0.3721 0.2427 -0.0943 0.0480  -0.0042 7   SER   A CB  
101  C  CB  B SER   A 7   ? 0.3148 0.3506 0.3155 -0.0468 0.0396  -0.0056 7   SER   A CB  
102  O  OG  A SER   A 7   ? 0.2978 0.3855 0.2581 -0.0819 0.0437  -0.0056 7   SER   A OG  
103  O  OG  B SER   A 7   ? 0.3195 0.3541 0.3381 -0.0427 0.0323  -0.0044 7   SER   A OG  
114  N  N   A GLY   A 8   ? 0.2163 0.2768 0.1724 -0.0905 0.0414  -0.0097 8   GLY   A N   
115  N  N   B GLY   A 8   ? 0.2737 0.3028 0.2458 -0.0493 0.0515  -0.0039 8   GLY   A N   
116  C  CA  A GLY   A 8   ? 0.2010 0.2515 0.1754 -0.0639 0.0367  -0.0123 8   GLY   A CA  
117  C  CA  B GLY   A 8   ? 0.2575 0.2797 0.2303 -0.0455 0.0466  -0.0038 8   GLY   A CA  
118  C  C   A GLY   A 8   ? 0.1769 0.2300 0.1632 -0.0424 0.0315  -0.0068 8   GLY   A C   
119  C  C   B GLY   A 8   ? 0.2382 0.2560 0.2114 -0.0412 0.0436  -0.0025 8   GLY   A C   
120  O  O   A GLY   A 8   ? 0.1823 0.2316 0.1796 -0.0251 0.0408  -0.0146 8   GLY   A O   
121  O  O   B GLY   A 8   ? 0.2425 0.2565 0.2092 -0.0368 0.0472  -0.0120 8   GLY   A O   
128  N  N   A TYR   A 9   ? 0.1573 0.2155 0.1581 -0.0334 0.0215  0.0082  9   TYR   A N   
129  N  N   B TYR   A 9   ? 0.2143 0.2331 0.1971 -0.0384 0.0348  0.0055  9   TYR   A N   
130  C  CA  A TYR   A 9   ? 0.1452 0.1987 0.1476 -0.0332 0.0181  0.0105  9   TYR   A CA  
131  C  CA  B TYR   A 9   ? 0.1945 0.2148 0.1812 -0.0321 0.0301  0.0128  9   TYR   A CA  
132  C  C   A TYR   A 9   ? 0.1493 0.1771 0.1298 -0.0236 0.0327  0.0189  9   TYR   A C   
133  C  C   B TYR   A 9   ? 0.1845 0.1914 0.1728 -0.0203 0.0275  0.0069  9   TYR   A C   
134  O  O   A TYR   A 9   ? 0.1770 0.1805 0.1338 -0.0194 0.0226  0.0059  9   TYR   A O   
135  O  O   B TYR   A 9   ? 0.1922 0.1957 0.1884 -0.0195 0.0179  0.0025  9   TYR   A O   
136  C  CB  A TYR   A 9   ? 0.1342 0.2140 0.1659 -0.0288 0.0155  0.0023  9   TYR   A CB  
137  C  CB  B TYR   A 9   ? 0.1879 0.2256 0.1889 -0.0350 0.0242  0.0135  9   TYR   A CB  
138  C  CG  A TYR   A 9   ? 0.1389 0.2254 0.1826 -0.0236 0.0281  -0.0055 9   TYR   A CG  
139  C  CG  B TYR   A 9   ? 0.1844 0.2326 0.1841 -0.0399 0.0225  0.0095  9   TYR   A CG  
140  C  CD1 A TYR   A 9   ? 0.1453 0.2340 0.2030 -0.0347 0.0333  -0.0193 9   TYR   A CD1 
141  C  CD1 B TYR   A 9   ? 0.1885 0.2397 0.1914 -0.0466 0.0217  0.0011  9   TYR   A CD1 
142  C  CD2 A TYR   A 9   ? 0.1427 0.2245 0.1916 -0.0166 0.0228  0.0037  9   TYR   A CD2 
143  C  CD2 B TYR   A 9   ? 0.1834 0.2327 0.1761 -0.0395 0.0214  0.0101  9   TYR   A CD2 
144  C  CE1 A TYR   A 9   ? 0.1548 0.2407 0.2185 -0.0396 0.0373  -0.0264 9   TYR   A CE1 
145  C  CE1 B TYR   A 9   ? 0.1908 0.2432 0.1965 -0.0522 0.0264  -0.0044 9   TYR   A CE1 
146  C  CE2 A TYR   A 9   ? 0.1465 0.2307 0.1997 -0.0225 0.0274  -0.0041 9   TYR   A CE2 
147  C  CE2 B TYR   A 9   ? 0.1865 0.2374 0.1757 -0.0416 0.0285  0.0064  9   TYR   A CE2 
148  C  CZ  A TYR   A 9   ? 0.1496 0.2427 0.2231 -0.0424 0.0445  -0.0186 9   TYR   A CZ  
149  C  CZ  B TYR   A 9   ? 0.1931 0.2438 0.1967 -0.0470 0.0365  -0.0018 9   TYR   A CZ  
150  O  OH  A TYR   A 9   ? 0.1567 0.2548 0.2537 -0.0624 0.0500  -0.0213 9   TYR   A OH  
151  O  OH  B TYR   A 9   ? 0.2037 0.2523 0.2260 -0.0502 0.0443  -0.0014 9   TYR   A OH  
170  N  N   A LEU   A 10  ? 0.1532 0.1569 0.1341 -0.0278 0.0212  0.0204  10  LEU   A N   
171  N  N   B LEU   A 10  ? 0.1789 0.1737 0.1646 -0.0138 0.0262  0.0073  10  LEU   A N   
172  C  CA  A LEU   A 10  ? 0.1422 0.1511 0.1478 -0.0291 0.0255  0.0337  10  LEU   A CA  
173  C  CA  B LEU   A 10  ? 0.1735 0.1650 0.1695 -0.0098 0.0206  0.0069  10  LEU   A CA  
174  C  C   A LEU   A 10  ? 0.1414 0.1453 0.1663 -0.0253 0.0233  0.0322  10  LEU   A C   
175  C  C   B LEU   A 10  ? 0.1670 0.1543 0.1563 -0.0104 0.0119  0.0232  10  LEU   A C   
176  O  O   A LEU   A 10  ? 0.1509 0.1398 0.1901 -0.0161 0.0380  0.0266  10  LEU   A O   
177  O  O   B LEU   A 10  ? 0.1698 0.1522 0.1460 -0.0103 0.0224  0.0249  10  LEU   A O   
178  C  CB  A LEU   A 10  ? 0.1437 0.1574 0.1698 -0.0235 0.0112  0.0321  10  LEU   A CB  
179  C  CB  B LEU   A 10  ? 0.1805 0.1689 0.1894 -0.0125 0.0101  0.0045  10  LEU   A CB  
180  C  CG  A LEU   A 10  ? 0.1650 0.1661 0.2155 -0.0076 -0.0046 0.0293  10  LEU   A CG  
181  C  CG  B LEU   A 10  ? 0.1921 0.1807 0.2107 -0.0103 -0.0097 0.0042  10  LEU   A CG  
182  C  CD1 A LEU   A 10  ? 0.1819 0.1693 0.2430 -0.0153 0.0016  0.0260  10  LEU   A CD1 
183  C  CD1 B LEU   A 10  ? 0.1997 0.1884 0.2334 -0.0215 -0.0097 0.0054  10  LEU   A CD1 
184  C  CD2 A LEU   A 10  ? 0.1821 0.1838 0.2312 0.0045  0.0014  0.0200  10  LEU   A CD2 
185  C  CD2 B LEU   A 10  ? 0.2044 0.1891 0.2220 0.0034  -0.0253 -0.0007 10  LEU   A CD2 
208  N  N   A LYS   A 11  ? 0.1462 0.1494 0.1766 -0.0264 0.0256  0.0392  11  LYS   A N   
209  N  N   B LYS   A 11  ? 0.1687 0.1506 0.1657 -0.0154 0.0080  0.0255  11  LYS   A N   
210  C  CA  A LYS   A 11  ? 0.1493 0.1496 0.1863 -0.0266 0.0204  0.0379  11  LYS   A CA  
211  C  CA  B LYS   A 11  ? 0.1691 0.1470 0.1677 -0.0210 0.0075  0.0263  11  LYS   A CA  
212  C  C   A LYS   A 11  ? 0.1438 0.1511 0.1882 -0.0213 0.0204  0.0219  11  LYS   A C   
213  C  C   B LYS   A 11  ? 0.1584 0.1370 0.1640 -0.0214 0.0069  0.0153  11  LYS   A C   
214  O  O   A LYS   A 11  ? 0.1474 0.1703 0.2236 -0.0422 0.0255  0.0069  11  LYS   A O   
215  O  O   B LYS   A 11  ? 0.1520 0.1266 0.1674 -0.0215 0.0022  -0.0010 11  LYS   A O   
216  C  CB  A LYS   A 11  ? 0.1604 0.1503 0.1772 -0.0282 0.0099  0.0277  11  LYS   A CB  
217  C  CB  B LYS   A 11  ? 0.1772 0.1466 0.1611 -0.0231 0.0093  0.0284  11  LYS   A CB  
218  C  CG  A LYS   A 11  ? 0.1635 0.1528 0.1818 -0.0283 0.0099  0.0365  11  LYS   A CG  
219  C  CG  B LYS   A 11  ? 0.1805 0.1525 0.1637 -0.0245 0.0110  0.0404  11  LYS   A CG  
220  C  CD  A LYS   A 11  ? 0.1720 0.1547 0.1832 -0.0257 -0.0052 0.0315  11  LYS   A CD  
221  C  CD  B LYS   A 11  ? 0.1848 0.1603 0.1745 -0.0232 0.0096  0.0414  11  LYS   A CD  
222  C  CE  A LYS   A 11  ? 0.1821 0.1539 0.1857 -0.0167 -0.0055 0.0391  11  LYS   A CE  
223  C  CE  B LYS   A 11  ? 0.1845 0.1632 0.1798 -0.0221 0.0037  0.0460  11  LYS   A CE  
224  N  NZ  A LYS   A 11  ? 0.1769 0.1585 0.2014 -0.0072 -0.0029 0.0375  11  LYS   A NZ  
225  N  NZ  B LYS   A 11  ? 0.1843 0.1676 0.1875 -0.0204 0.0058  0.0473  11  LYS   A NZ  
252  N  N   A LEU   A 12  ? 0.1348 0.1416 0.1630 -0.0190 0.0174  0.0193  12  LEU   A N   
253  N  N   B LEU   A 12  ? 0.1504 0.1459 0.1679 -0.0070 0.0071  0.0107  12  LEU   A N   
254  C  CA  A LEU   A 12  ? 0.1378 0.1471 0.1632 -0.0133 0.0075  0.0246  12  LEU   A CA  
255  C  CA  B LEU   A 12  ? 0.1492 0.1543 0.1662 0.0018  0.0158  0.0139  12  LEU   A CA  
256  C  C   A LEU   A 12  ? 0.1391 0.1388 0.1704 -0.0192 0.0120  0.0295  12  LEU   A C   
257  C  C   B LEU   A 12  ? 0.1478 0.1573 0.1683 -0.0008 0.0235  0.0169  12  LEU   A C   
258  O  O   A LEU   A 12  ? 0.1413 0.1403 0.1780 -0.0157 0.0170  0.0152  12  LEU   A O   
259  O  O   B LEU   A 12  ? 0.1540 0.1573 0.1623 0.0023  0.0246  0.0127  12  LEU   A O   
260  C  CB  A LEU   A 12  ? 0.1451 0.1421 0.1673 -0.0120 0.0054  0.0243  12  LEU   A CB  
261  C  CB  B LEU   A 12  ? 0.1578 0.1637 0.1912 0.0013  0.0189  0.0128  12  LEU   A CB  
262  C  CG  A LEU   A 12  ? 0.1492 0.1491 0.1836 -0.0020 0.0136  0.0213  12  LEU   A CG  
263  C  CG  B LEU   A 12  ? 0.1627 0.1691 0.2197 0.0011  0.0280  0.0102  12  LEU   A CG  
264  C  CD1 A LEU   A 12  ? 0.1573 0.1482 0.1796 0.0102  0.0296  0.0346  12  LEU   A CD1 
265  C  CD1 B LEU   A 12  ? 0.1619 0.1748 0.2272 0.0045  0.0448  0.0103  12  LEU   A CD1 
266  C  CD2 A LEU   A 12  ? 0.1510 0.1559 0.2150 -0.0053 0.0084  0.0223  12  LEU   A CD2 
267  C  CD2 B LEU   A 12  ? 0.1689 0.1743 0.2356 0.0003  0.0222  0.0017  12  LEU   A CD2 
290  N  N   A THR   A 13  ? 0.1390 0.1358 0.1974 -0.0178 0.0075  0.0309  13  THR   A N   
291  N  N   B THR   A 13  ? 0.1485 0.1585 0.1823 -0.0040 0.0163  0.0203  13  THR   A N   
292  C  CA  A THR   A 13  ? 0.1375 0.1421 0.1976 -0.0170 0.0106  0.0315  13  THR   A CA  
293  C  CA  B THR   A 13  ? 0.1487 0.1622 0.1938 -0.0083 0.0170  0.0276  13  THR   A CA  
294  C  C   A THR   A 13  ? 0.1402 0.1439 0.2046 -0.0212 -0.0024 0.0520  13  THR   A C   
295  C  C   B THR   A 13  ? 0.1568 0.1719 0.2015 -0.0152 0.0118  0.0332  13  THR   A C   
296  O  O   A THR   A 13  ? 0.1392 0.1488 0.2094 -0.0128 -0.0014 0.0429  13  THR   A O   
297  O  O   B THR   A 13  ? 0.1641 0.1789 0.2056 -0.0201 0.0078  0.0376  13  THR   A O   
298  C  CB  A THR   A 13  ? 0.1403 0.1566 0.2072 -0.0096 0.0093  0.0328  13  THR   A CB  
299  C  CB  B THR   A 13  ? 0.1432 0.1670 0.2006 -0.0043 0.0205  0.0323  13  THR   A CB  
300  O  OG1 A THR   A 13  ? 0.1431 0.1597 0.2117 -0.0100 0.0022  0.0428  13  THR   A OG1 
301  O  OG1 B THR   A 13  ? 0.1309 0.1680 0.2088 -0.0092 0.0316  0.0439  13  THR   A OG1 
302  C  CG2 A THR   A 13  ? 0.1504 0.1681 0.2128 -0.0056 0.0153  0.0247  13  THR   A CG2 
303  C  CG2 B THR   A 13  ? 0.1481 0.1727 0.2084 0.0062  0.0224  0.0249  13  THR   A CG2 
318  N  N   A ASP   A 14  ? 0.1423 0.1468 0.2279 -0.0309 -0.0099 0.0698  14  ASP   A N   
319  N  N   B ASP   A 14  ? 0.1597 0.1744 0.2156 -0.0162 0.0025  0.0360  14  ASP   A N   
320  C  CA  A ASP   A 14  ? 0.1542 0.1671 0.2556 -0.0272 -0.0173 0.0876  14  ASP   A CA  
321  C  CA  B ASP   A 14  ? 0.1672 0.1789 0.2271 -0.0127 -0.0052 0.0542  14  ASP   A CA  
322  C  C   A ASP   A 14  ? 0.1559 0.1743 0.2400 -0.0265 -0.0207 0.0754  14  ASP   A C   
323  C  C   B ASP   A 14  ? 0.1595 0.1723 0.2110 -0.0207 -0.0092 0.0669  14  ASP   A C   
324  O  O   A ASP   A 14  ? 0.1784 0.1898 0.2482 -0.0398 -0.0218 0.0731  14  ASP   A O   
325  O  O   B ASP   A 14  ? 0.1705 0.1824 0.2175 -0.0329 -0.0107 0.0650  14  ASP   A O   
326  C  CB  A ASP   A 14  ? 0.1714 0.1923 0.3079 -0.0284 -0.0168 0.1094  14  ASP   A CB  
327  C  CB  B ASP   A 14  ? 0.1810 0.1957 0.2599 -0.0026 -0.0084 0.0564  14  ASP   A CB  
328  C  CG  A ASP   A 14  ? 0.1965 0.2351 0.3769 -0.0266 -0.0090 0.1001  14  ASP   A CG  
329  C  CG  B ASP   A 14  ? 0.1934 0.2235 0.2971 0.0016  -0.0106 0.0510  14  ASP   A CG  
330  O  OD1 A ASP   A 14  ? 0.2085 0.2462 0.4005 -0.0192 -0.0148 0.1096  14  ASP   A OD1 
331  O  OD1 B ASP   A 14  ? 0.2043 0.2285 0.3029 0.0141  -0.0186 0.0672  14  ASP   A OD1 
332  O  OD2 A ASP   A 14  ? 0.2134 0.2588 0.4156 -0.0297 -0.0186 0.0709  14  ASP   A OD2 
333  O  OD2 B ASP   A 14  ? 0.1974 0.2414 0.3272 -0.0060 -0.0124 0.0304  14  ASP   A OD2 
342  N  N   A ASN   A 15  ? 0.1446 0.1587 0.2392 -0.0225 -0.0127 0.0689  15  ASN   A N   
343  N  N   B ASN   A 15  ? 0.1472 0.1542 0.2009 -0.0224 -0.0042 0.0794  15  ASN   A N   
344  C  CA  A ASN   A 15  ? 0.1427 0.1584 0.2515 -0.0120 -0.0145 0.0538  15  ASN   A CA  
345  C  CA  B ASN   A 15  ? 0.1432 0.1519 0.2096 -0.0204 -0.0032 0.0708  15  ASN   A CA  
346  C  C   A ASN   A 15  ? 0.1398 0.1552 0.2665 -0.0128 -0.0101 0.0474  15  ASN   A C   
347  C  C   B ASN   A 15  ? 0.1395 0.1495 0.2271 -0.0234 0.0061  0.0604  15  ASN   A C   
348  O  O   A ASN   A 15  ? 0.1497 0.1560 0.3064 -0.0135 -0.0324 0.0539  15  ASN   A O   
349  O  O   B ASN   A 15  ? 0.1510 0.1567 0.2591 -0.0301 -0.0067 0.0519  15  ASN   A O   
350  C  CB  A ASN   A 15  ? 0.1384 0.1571 0.2602 -0.0050 -0.0038 0.0422  15  ASN   A CB  
351  C  CB  B ASN   A 15  ? 0.1438 0.1532 0.2041 -0.0179 -0.0004 0.0678  15  ASN   A CB  
352  C  CG  A ASN   A 15  ? 0.1421 0.1632 0.2678 -0.0047 0.0030  0.0269  15  ASN   A CG  
353  C  CG  B ASN   A 15  ? 0.1433 0.1610 0.2090 -0.0198 0.0111  0.0520  15  ASN   A CG  
354  O  OD1 A ASN   A 15  ? 0.1555 0.1664 0.2752 -0.0159 -0.0024 0.0287  15  ASN   A OD1 
355  O  OD1 B ASN   A 15  ? 0.1498 0.1602 0.2246 -0.0248 0.0076  0.0599  15  ASN   A OD1 
356  N  ND2 A ASN   A 15  ? 0.1477 0.1775 0.2689 -0.0103 0.0108  0.0265  15  ASN   A ND2 
357  N  ND2 B ASN   A 15  ? 0.1459 0.1703 0.2026 -0.0236 0.0185  0.0468  15  ASN   A ND2 
370  N  N   A VAL   A 16  ? 0.1382 0.1545 0.2438 -0.0079 0.0009  0.0418  16  VAL   A N   
371  N  N   B VAL   A 16  ? 0.1318 0.1448 0.2124 -0.0155 0.0130  0.0611  16  VAL   A N   
372  C  CA  A VAL   A 16  ? 0.1386 0.1527 0.2264 -0.0117 0.0096  0.0404  16  VAL   A CA  
373  C  CA  B VAL   A 16  ? 0.1362 0.1491 0.1966 -0.0104 0.0184  0.0550  16  VAL   A CA  
374  C  C   A VAL   A 16  ? 0.1349 0.1445 0.2076 -0.0162 0.0065  0.0354  16  VAL   A C   
375  C  C   B VAL   A 16  ? 0.1316 0.1539 0.1835 -0.0122 0.0111  0.0495  16  VAL   A C   
376  O  O   A VAL   A 16  ? 0.1283 0.1400 0.2221 -0.0193 0.0152  0.0193  16  VAL   A O   
377  O  O   B VAL   A 16  ? 0.1252 0.1545 0.1813 -0.0054 0.0239  0.0452  16  VAL   A O   
378  C  CB  A VAL   A 16  ? 0.1477 0.1693 0.2201 0.0043  0.0252  0.0500  16  VAL   A CB  
379  C  CB  B VAL   A 16  ? 0.1502 0.1601 0.1841 0.0019  0.0269  0.0514  16  VAL   A CB  
380  C  CG1 A VAL   A 16  ? 0.1634 0.1830 0.2291 0.0061  0.0222  0.0497  16  VAL   A CG1 
381  C  CG1 B VAL   A 16  ? 0.1580 0.1619 0.1811 0.0107  0.0255  0.0544  16  VAL   A CG1 
382  C  CG2 A VAL   A 16  ? 0.1501 0.1804 0.2265 0.0114  0.0396  0.0431  16  VAL   A CG2 
383  C  CG2 B VAL   A 16  ? 0.1576 0.1725 0.1954 0.0055  0.0331  0.0442  16  VAL   A CG2 
402  N  N   A TYR   A 17  ? 0.1360 0.1416 0.2054 -0.0124 0.0191  0.0435  17  TYR   A N   
403  N  N   B TYR   A 17  ? 0.1386 0.1518 0.1765 -0.0200 0.0048  0.0436  17  TYR   A N   
404  C  CA  A TYR   A 17  ? 0.1404 0.1460 0.1809 -0.0187 0.0156  0.0427  17  TYR   A CA  
405  C  CA  B TYR   A 17  ? 0.1461 0.1540 0.1661 -0.0264 -0.0037 0.0352  17  TYR   A CA  
406  C  C   A TYR   A 17  ? 0.1399 0.1380 0.1750 -0.0174 0.0155  0.0242  17  TYR   A C   
407  C  C   B TYR   A 17  ? 0.1443 0.1567 0.1559 -0.0206 0.0079  0.0249  17  TYR   A C   
408  O  O   A TYR   A 17  ? 0.1369 0.1342 0.1695 -0.0171 0.0158  0.0254  17  TYR   A O   
409  O  O   B TYR   A 17  ? 0.1400 0.1529 0.1527 -0.0222 0.0066  0.0231  17  TYR   A O   
410  C  CB  A TYR   A 17  ? 0.1616 0.1589 0.1946 -0.0252 0.0067  0.0488  17  TYR   A CB  
411  C  CB  B TYR   A 17  ? 0.1640 0.1571 0.1719 -0.0390 -0.0189 0.0367  17  TYR   A CB  
412  C  CG  A TYR   A 17  ? 0.1918 0.1811 0.2084 -0.0243 -0.0035 0.0559  17  TYR   A CG  
413  C  CG  B TYR   A 17  ? 0.1854 0.1622 0.1770 -0.0465 -0.0333 0.0313  17  TYR   A CG  
414  C  CD1 A TYR   A 17  ? 0.2105 0.1924 0.2260 -0.0096 -0.0105 0.0553  17  TYR   A CD1 
415  C  CD1 B TYR   A 17  ? 0.1989 0.1668 0.1894 -0.0403 -0.0390 0.0300  17  TYR   A CD1 
416  C  CD2 A TYR   A 17  ? 0.2095 0.1929 0.2039 -0.0356 -0.0079 0.0634  17  TYR   A CD2 
417  C  CD2 B TYR   A 17  ? 0.1963 0.1641 0.1686 -0.0596 -0.0412 0.0266  17  TYR   A CD2 
418  C  CE1 A TYR   A 17  ? 0.2283 0.1991 0.2378 -0.0131 -0.0202 0.0616  17  TYR   A CE1 
419  C  CE1 B TYR   A 17  ? 0.2088 0.1670 0.2003 -0.0469 -0.0464 0.0288  17  TYR   A CE1 
420  C  CE2 A TYR   A 17  ? 0.2297 0.1991 0.2199 -0.0339 -0.0164 0.0587  17  TYR   A CE2 
421  C  CE2 B TYR   A 17  ? 0.2101 0.1633 0.1820 -0.0634 -0.0465 0.0211  17  TYR   A CE2 
422  C  CZ  A TYR   A 17  ? 0.2439 0.1988 0.2265 -0.0225 -0.0257 0.0661  17  TYR   A CZ  
423  C  CZ  B TYR   A 17  ? 0.2195 0.1608 0.1905 -0.0574 -0.0527 0.0263  17  TYR   A CZ  
424  O  OH  A TYR   A 17  ? 0.2678 0.2000 0.2381 -0.0172 -0.0208 0.0668  17  TYR   A OH  
425  O  OH  B TYR   A 17  ? 0.2381 0.1572 0.1967 -0.0552 -0.0529 0.0214  17  TYR   A OH  
444  N  N   A ILE   A 18  ? 0.1436 0.1420 0.1741 -0.0228 0.0167  0.0378  18  ILE   A N   
445  N  N   B ILE   A 18  ? 0.1394 0.1524 0.1524 -0.0214 0.0214  0.0261  18  ILE   A N   
446  C  CA  A ILE   A 18  ? 0.1477 0.1401 0.1712 -0.0117 0.0235  0.0264  18  ILE   A CA  
447  C  CA  B ILE   A 18  ? 0.1381 0.1480 0.1366 -0.0120 0.0274  0.0141  18  ILE   A CA  
448  C  C   A ILE   A 18  ? 0.1493 0.1469 0.1797 -0.0231 0.0252  0.0255  18  ILE   A C   
449  C  C   B ILE   A 18  ? 0.1409 0.1620 0.1298 -0.0170 0.0175  0.0130  18  ILE   A C   
450  O  O   A ILE   A 18  ? 0.1486 0.1605 0.1824 -0.0291 0.0318  0.0222  18  ILE   A O   
451  O  O   B ILE   A 18  ? 0.1376 0.1651 0.1459 -0.0208 0.0195  0.0125  18  ILE   A O   
452  C  CB  A ILE   A 18  ? 0.1552 0.1361 0.1575 0.0020  0.0256  0.0254  18  ILE   A CB  
453  C  CB  B ILE   A 18  ? 0.1441 0.1446 0.1241 -0.0014 0.0405  0.0068  18  ILE   A CB  
454  C  CG1 A ILE   A 18  ? 0.1634 0.1424 0.1502 0.0142  0.0201  0.0296  18  ILE   A CG1 
455  C  CG1 B ILE   A 18  ? 0.1591 0.1512 0.1390 0.0016  0.0434  0.0133  18  ILE   A CG1 
456  C  CG2 A ILE   A 18  ? 0.1569 0.1310 0.1537 0.0068  0.0222  0.0159  18  ILE   A CG2 
457  C  CG2 B ILE   A 18  ? 0.1528 0.1553 0.1375 -0.0020 0.0331  0.0042  18  ILE   A CG2 
458  C  CD1 A ILE   A 18  ? 0.1869 0.1570 0.1629 0.0276  0.0161  0.0349  18  ILE   A CD1 
459  C  CD1 B ILE   A 18  ? 0.1771 0.1632 0.1585 0.0040  0.0417  0.0040  18  ILE   A CD1 
482  N  N   A LYS   A 19  ? 0.1487 0.1485 0.1571 -0.0182 0.0302  0.0178  19  LYS   A N   
483  N  N   B LYS   A 19  ? 0.1497 0.1739 0.1286 -0.0118 0.0262  0.0008  19  LYS   A N   
484  C  CA  A LYS   A 19  ? 0.1554 0.1626 0.1617 -0.0208 0.0300  0.0237  19  LYS   A CA  
485  C  CA  B LYS   A 19  ? 0.1661 0.1922 0.1448 -0.0078 0.0348  -0.0128 19  LYS   A CA  
486  C  C   A LYS   A 19  ? 0.1462 0.1523 0.1754 -0.0097 0.0337  0.0326  19  LYS   A C   
487  C  C   B LYS   A 19  ? 0.1752 0.1974 0.1507 -0.0040 0.0357  -0.0095 19  LYS   A C   
488  O  O   A LYS   A 19  ? 0.1406 0.1461 0.1756 -0.0067 0.0276  0.0379  19  LYS   A O   
489  O  O   B LYS   A 19  ? 0.1731 0.1957 0.1415 -0.0096 0.0286  -0.0035 19  LYS   A O   
490  C  CB  A LYS   A 19  ? 0.1733 0.1908 0.1696 -0.0264 0.0216  0.0212  19  LYS   A CB  
491  C  CB  B LYS   A 19  ? 0.1709 0.2040 0.1609 -0.0087 0.0334  -0.0248 19  LYS   A CB  
492  C  CG  A LYS   A 19  ? 0.1989 0.2105 0.1718 -0.0322 0.0194  0.0191  19  LYS   A CG  
493  C  CG  B LYS   A 19  ? 0.1905 0.2192 0.1697 -0.0075 0.0277  -0.0229 19  LYS   A CG  
494  C  CD  A LYS   A 19  ? 0.2246 0.2343 0.1854 -0.0357 0.0120  0.0144  19  LYS   A CD  
495  C  CD  B LYS   A 19  ? 0.2069 0.2344 0.1772 -0.0123 0.0199  -0.0138 19  LYS   A CD  
496  C  CE  A LYS   A 19  ? 0.2455 0.2474 0.2005 -0.0469 0.0078  0.0119  19  LYS   A CE  
497  C  CE  B LYS   A 19  ? 0.2167 0.2456 0.1848 -0.0199 0.0115  -0.0093 19  LYS   A CE  
498  N  NZ  A LYS   A 19  ? 0.2586 0.2576 0.1923 -0.0554 0.0089  0.0099  19  LYS   A NZ  
499  N  NZ  B LYS   A 19  ? 0.2249 0.2539 0.1908 -0.0278 0.0115  -0.0088 19  LYS   A NZ  
526  N  N   A ASN   A 20  ? 0.1501 0.1611 0.2024 -0.0178 0.0354  0.0492  20  ASN   A N   
527  N  N   B ASN   A 20  ? 0.1888 0.2062 0.1761 0.0037  0.0440  -0.0145 20  ASN   A N   
528  C  CA  A ASN   A 20  ? 0.1602 0.1747 0.2278 0.0039  0.0535  0.0469  20  ASN   A CA  
529  C  CA  B ASN   A 20  ? 0.2038 0.2193 0.2123 0.0110  0.0419  -0.0125 20  ASN   A CA  
530  C  C   A ASN   A 20  ? 0.1811 0.1825 0.2537 -0.0058 0.0694  0.0256  20  ASN   A C   
531  C  C   B ASN   A 20  ? 0.2100 0.2135 0.2222 0.0064  0.0534  -0.0141 20  ASN   A C   
532  O  O   A ASN   A 20  ? 0.2074 0.1884 0.2658 -0.0225 0.0803  0.0018  20  ASN   A O   
533  O  O   B ASN   A 20  ? 0.2193 0.2137 0.2299 0.0057  0.0601  -0.0201 20  ASN   A O   
534  C  CB  A ASN   A 20  ? 0.1630 0.1874 0.2322 0.0190  0.0597  0.0669  20  ASN   A CB  
535  C  CB  B ASN   A 20  ? 0.2162 0.2382 0.2408 0.0209  0.0309  -0.0068 20  ASN   A CB  
536  C  CG  A ASN   A 20  ? 0.1708 0.1991 0.2553 0.0349  0.0682  0.0750  20  ASN   A CG  
537  C  CG  B ASN   A 20  ? 0.2306 0.2536 0.2704 0.0307  0.0203  0.0031  20  ASN   A CG  
538  O  OD1 A ASN   A 20  ? 0.2003 0.2084 0.2827 0.0545  0.0799  0.0601  20  ASN   A OD1 
539  O  OD1 B ASN   A 20  ? 0.2478 0.2628 0.2837 0.0327  0.0163  0.0066  20  ASN   A OD1 
540  N  ND2 A ASN   A 20  ? 0.1604 0.1945 0.2746 0.0331  0.0521  0.0875  20  ASN   A ND2 
541  N  ND2 B ASN   A 20  ? 0.2305 0.2551 0.2840 0.0382  0.0114  0.0079  20  ASN   A ND2 
554  N  N   A ALA   A 21  ? 0.1827 0.1855 0.2542 0.0027  0.0584  0.0231  21  ALA   A N   
555  N  N   B ALA   A 21  ? 0.2099 0.2076 0.2273 0.0056  0.0445  -0.0079 21  ALA   A N   
556  C  CA  A ALA   A 21  ? 0.1936 0.1864 0.2464 -0.0051 0.0550  0.0380  21  ALA   A CA  
557  C  CA  B ALA   A 21  ? 0.2118 0.2004 0.2279 -0.0025 0.0477  0.0053  21  ALA   A CA  
558  C  C   A ALA   A 21  ? 0.1819 0.1862 0.2396 -0.0056 0.0430  0.0439  21  ALA   A C   
559  C  C   B ALA   A 21  ? 0.1999 0.1885 0.2218 -0.0059 0.0570  0.0169  21  ALA   A C   
560  O  O   A ALA   A 21  ? 0.1751 0.1867 0.2426 0.0003  0.0325  0.0516  21  ALA   A O   
561  O  O   B ALA   A 21  ? 0.1911 0.1773 0.2349 -0.0012 0.0605  0.0116  21  ALA   A O   
562  C  CB  A ALA   A 21  ? 0.2123 0.1888 0.2455 -0.0067 0.0503  0.0321  21  ALA   A CB  
563  C  CB  B ALA   A 21  ? 0.2199 0.2002 0.2431 -0.0032 0.0388  0.0013  21  ALA   A CB  
574  N  N   A ASP   A 22  ? 0.1818 0.1828 0.2410 -0.0117 0.0431  0.0403  22  ASP   A N   
575  N  N   B ASP   A 22  ? 0.1998 0.1850 0.2142 -0.0122 0.0613  0.0307  22  ASP   A N   
576  C  CA  A ASP   A 22  ? 0.1813 0.1858 0.2357 -0.0041 0.0363  0.0278  22  ASP   A CA  
577  C  CA  B ASP   A 22  ? 0.1995 0.1800 0.2151 -0.0130 0.0589  0.0324  22  ASP   A CA  
578  C  C   A ASP   A 22  ? 0.1752 0.1854 0.1943 -0.0009 0.0373  0.0247  22  ASP   A C   
579  C  C   B ASP   A 22  ? 0.1841 0.1745 0.1839 -0.0216 0.0595  0.0239  22  ASP   A C   
580  O  O   A ASP   A 22  ? 0.1853 0.1953 0.2064 -0.0018 0.0313  0.0190  22  ASP   A O   
581  O  O   B ASP   A 22  ? 0.1805 0.1807 0.1805 -0.0303 0.0541  0.0078  22  ASP   A O   
582  C  CB  A ASP   A 22  ? 0.1926 0.1863 0.2769 -0.0087 0.0276  0.0221  22  ASP   A CB  
583  C  CB  B ASP   A 22  ? 0.2156 0.1832 0.2456 -0.0042 0.0584  0.0320  22  ASP   A CB  
584  C  CG  A ASP   A 22  ? 0.2111 0.1936 0.3298 -0.0079 0.0028  0.0319  22  ASP   A CG  
585  C  CG  B ASP   A 22  ? 0.2245 0.1833 0.2591 -0.0025 0.0602  0.0376  22  ASP   A CG  
586  O  OD1 A ASP   A 22  ? 0.2050 0.1926 0.3589 -0.0234 -0.0173 0.0405  22  ASP   A OD1 
587  O  OD1 B ASP   A 22  ? 0.2244 0.1822 0.2503 -0.0077 0.0645  0.0296  22  ASP   A OD1 
588  O  OD2 A ASP   A 22  ? 0.2327 0.2039 0.3580 0.0031  0.0097  0.0250  22  ASP   A OD2 
589  O  OD2 B ASP   A 22  ? 0.2321 0.1893 0.2845 -0.0021 0.0632  0.0460  22  ASP   A OD2 
598  N  N   A ILE   A 23  ? 0.1747 0.1855 0.1684 -0.0007 0.0379  0.0175  23  ILE   A N   
599  N  N   B ILE   A 23  ? 0.1785 0.1653 0.1784 -0.0173 0.0539  0.0228  23  ILE   A N   
600  C  CA  A ILE   A 23  ? 0.1767 0.1748 0.1675 -0.0009 0.0249  0.0158  23  ILE   A CA  
601  C  CA  B ILE   A 23  ? 0.1728 0.1675 0.1645 -0.0162 0.0437  0.0260  23  ILE   A CA  
602  C  C   A ILE   A 23  ? 0.1746 0.1778 0.1669 -0.0040 0.0422  0.0132  23  ILE   A C   
603  C  C   B ILE   A 23  ? 0.1779 0.1769 0.1752 -0.0263 0.0432  0.0208  23  ILE   A C   
604  O  O   A ILE   A 23  ? 0.1819 0.1902 0.1731 -0.0072 0.0325  0.0026  23  ILE   A O   
605  O  O   B ILE   A 23  ? 0.1760 0.1711 0.1818 -0.0274 0.0388  0.0228  23  ILE   A O   
606  C  CB  A ILE   A 23  ? 0.1851 0.1673 0.1578 0.0018  0.0188  0.0127  23  ILE   A CB  
607  C  CB  B ILE   A 23  ? 0.1705 0.1635 0.1474 -0.0021 0.0366  0.0264  23  ILE   A CB  
608  C  CG1 A ILE   A 23  ? 0.1885 0.1658 0.1599 0.0045  0.0205  0.0069  23  ILE   A CG1 
609  C  CG1 B ILE   A 23  ? 0.1719 0.1627 0.1386 -0.0039 0.0270  0.0139  23  ILE   A CG1 
610  C  CG2 A ILE   A 23  ? 0.1871 0.1738 0.1604 0.0019  0.0249  0.0192  23  ILE   A CG2 
611  C  CG2 B ILE   A 23  ? 0.1704 0.1588 0.1461 0.0060  0.0351  0.0276  23  ILE   A CG2 
612  C  CD1 A ILE   A 23  ? 0.1901 0.1665 0.1662 0.0002  0.0171  -0.0076 23  ILE   A CD1 
613  C  CD1 B ILE   A 23  ? 0.1657 0.1622 0.1386 -0.0066 0.0133  0.0084  23  ILE   A CD1 
636  N  N   A VAL   A 24  ? 0.1805 0.1803 0.1882 -0.0100 0.0411  0.0077  24  VAL   A N   
637  N  N   B VAL   A 24  ? 0.1884 0.1907 0.1901 -0.0346 0.0369  0.0127  24  VAL   A N   
638  C  CA  A VAL   A 24  ? 0.1914 0.1931 0.2076 -0.0192 0.0423  -0.0033 24  VAL   A CA  
639  C  CA  B VAL   A 24  ? 0.2041 0.2035 0.2089 -0.0413 0.0366  0.0076  24  VAL   A CA  
640  C  C   A VAL   A 24  ? 0.1943 0.2124 0.2068 -0.0297 0.0381  -0.0020 24  VAL   A C   
641  C  C   B VAL   A 24  ? 0.2127 0.2218 0.2199 -0.0410 0.0371  -0.0032 24  VAL   A C   
642  O  O   A VAL   A 24  ? 0.2040 0.2141 0.2084 -0.0284 0.0372  -0.0055 24  VAL   A O   
643  O  O   B VAL   A 24  ? 0.2213 0.2284 0.2326 -0.0354 0.0368  -0.0019 24  VAL   A O   
644  C  CB  A VAL   A 24  ? 0.1956 0.1925 0.2324 -0.0196 0.0549  -0.0066 24  VAL   A CB  
645  C  CB  B VAL   A 24  ? 0.2104 0.2003 0.2231 -0.0491 0.0333  0.0100  24  VAL   A CB  
646  C  CG1 A VAL   A 24  ? 0.1966 0.1978 0.2431 -0.0153 0.0585  -0.0191 24  VAL   A CG1 
647  C  CG1 B VAL   A 24  ? 0.2174 0.2047 0.2440 -0.0477 0.0285  0.0087  24  VAL   A CG1 
648  C  CG2 A VAL   A 24  ? 0.2091 0.1981 0.2530 -0.0171 0.0678  0.0039  24  VAL   A CG2 
649  C  CG2 B VAL   A 24  ? 0.2150 0.1943 0.2197 -0.0548 0.0365  0.0134  24  VAL   A CG2 
668  N  N   A GLU   A 25  ? 0.1987 0.2354 0.2025 -0.0382 0.0472  -0.0055 25  GLU   A N   
669  N  N   B GLU   A 25  ? 0.2166 0.2377 0.2178 -0.0405 0.0456  -0.0143 25  GLU   A N   
670  C  CA  A GLU   A 25  ? 0.2171 0.2645 0.2085 -0.0287 0.0610  -0.0107 25  GLU   A CA  
671  C  CA  B GLU   A 25  ? 0.2283 0.2571 0.2257 -0.0393 0.0462  -0.0175 25  GLU   A CA  
672  C  C   A GLU   A 25  ? 0.2086 0.2701 0.1721 -0.0393 0.0646  -0.0137 25  GLU   A C   
673  C  C   B GLU   A 25  ? 0.2248 0.2667 0.2169 -0.0378 0.0494  -0.0148 25  GLU   A C   
674  O  O   A GLU   A 25  ? 0.2107 0.2818 0.1636 -0.0399 0.0575  -0.0156 25  GLU   A O   
675  O  O   B GLU   A 25  ? 0.2283 0.2715 0.2263 -0.0379 0.0503  -0.0161 25  GLU   A O   
676  C  CB  A GLU   A 25  ? 0.2445 0.2917 0.2573 -0.0161 0.0670  -0.0074 25  GLU   A CB  
677  C  CB  B GLU   A 25  ? 0.2461 0.2688 0.2521 -0.0378 0.0443  -0.0216 25  GLU   A CB  
678  C  CG  A GLU   A 25  ? 0.2759 0.3166 0.3217 -0.0119 0.0471  -0.0142 25  GLU   A CG  
679  C  CG  B GLU   A 25  ? 0.2692 0.2835 0.3044 -0.0361 0.0357  -0.0248 25  GLU   A CG  
680  C  CD  A GLU   A 25  ? 0.3020 0.3406 0.3787 -0.0039 0.0241  -0.0215 25  GLU   A CD  
681  C  CD  B GLU   A 25  ? 0.2885 0.2993 0.3538 -0.0339 0.0223  -0.0271 25  GLU   A CD  
682  O  OE1 A GLU   A 25  ? 0.3143 0.3520 0.3861 0.0029  0.0112  -0.0314 25  GLU   A OE1 
683  O  OE1 B GLU   A 25  ? 0.2985 0.3097 0.3814 -0.0324 0.0163  -0.0251 25  GLU   A OE1 
684  O  OE2 A GLU   A 25  ? 0.3081 0.3489 0.4095 -0.0034 0.0126  -0.0278 25  GLU   A OE2 
685  O  OE2 B GLU   A 25  ? 0.2957 0.3019 0.3750 -0.0336 0.0164  -0.0293 25  GLU   A OE2 
698  N  N   A GLU   A 26  ? 0.2009 0.2641 0.1844 -0.0545 0.0649  -0.0170 26  GLU   A N   
699  N  N   B GLU   A 26  ? 0.2183 0.2703 0.2073 -0.0392 0.0514  -0.0119 26  GLU   A N   
700  C  CA  A GLU   A 26  ? 0.2088 0.2623 0.1693 -0.0664 0.0603  -0.0102 26  GLU   A CA  
701  C  CA  B GLU   A 26  ? 0.2198 0.2757 0.2004 -0.0366 0.0448  -0.0034 26  GLU   A CA  
702  C  C   A GLU   A 26  ? 0.2079 0.2527 0.1449 -0.0643 0.0523  -0.0059 26  GLU   A C   
703  C  C   B GLU   A 26  ? 0.2127 0.2662 0.1848 -0.0308 0.0462  0.0008  26  GLU   A C   
704  O  O   A GLU   A 26  ? 0.2188 0.2521 0.1497 -0.0670 0.0452  -0.0013 26  GLU   A O   
705  O  O   B GLU   A 26  ? 0.2157 0.2640 0.1777 -0.0369 0.0520  -0.0021 26  GLU   A O   
706  C  CB  A GLU   A 26  ? 0.2294 0.2668 0.2059 -0.0787 0.0637  -0.0023 26  GLU   A CB  
707  C  CB  B GLU   A 26  ? 0.2324 0.2868 0.2116 -0.0427 0.0300  -0.0001 26  GLU   A CB  
708  C  CG  A GLU   A 26  ? 0.2557 0.2848 0.2890 -0.0859 0.0563  -0.0123 26  GLU   A CG  
709  C  CG  B GLU   A 26  ? 0.2420 0.2991 0.2215 -0.0475 0.0298  -0.0017 26  GLU   A CG  
710  C  CD  A GLU   A 26  ? 0.2726 0.2970 0.3275 -0.0931 0.0651  -0.0189 26  GLU   A CD  
711  C  CD  B GLU   A 26  ? 0.2472 0.3074 0.2120 -0.0546 0.0341  0.0016  26  GLU   A CD  
712  O  OE1 A GLU   A 26  ? 0.2672 0.3093 0.3169 -0.0871 0.0894  -0.0567 26  GLU   A OE1 
713  O  OE1 B GLU   A 26  ? 0.2515 0.3168 0.2073 -0.0522 0.0422  0.0026  26  GLU   A OE1 
714  O  OE2 A GLU   A 26  ? 0.2932 0.3022 0.3514 -0.0948 0.0544  -0.0077 26  GLU   A OE2 
715  O  OE2 B GLU   A 26  ? 0.2472 0.3057 0.1735 -0.0598 0.0389  0.0003  26  GLU   A OE2 
728  N  N   A ALA   A 27  ? 0.1965 0.2452 0.1472 -0.0680 0.0506  -0.0012 27  ALA   A N   
729  N  N   B ALA   A 27  ? 0.2040 0.2596 0.1746 -0.0199 0.0386  0.0099  27  ALA   A N   
730  C  CA  A ALA   A 27  ? 0.2036 0.2568 0.1486 -0.0674 0.0460  -0.0019 27  ALA   A CA  
731  C  CA  B ALA   A 27  ? 0.2057 0.2636 0.1693 -0.0114 0.0314  0.0143  27  ALA   A CA  
732  C  C   A ALA   A 27  ? 0.2254 0.2763 0.1603 -0.0784 0.0452  -0.0136 27  ALA   A C   
733  C  C   B ALA   A 27  ? 0.2174 0.2761 0.1787 -0.0066 0.0259  0.0074  27  ALA   A C   
734  O  O   A ALA   A 27  ? 0.2348 0.2721 0.1669 -0.0835 0.0294  -0.0049 27  ALA   A O   
735  O  O   B ALA   A 27  ? 0.2140 0.2740 0.1815 -0.0043 0.0191  0.0094  27  ALA   A O   
736  C  CB  A ALA   A 27  ? 0.1905 0.2491 0.1502 -0.0664 0.0345  -0.0025 27  ALA   A CB  
737  C  CB  B ALA   A 27  ? 0.1988 0.2584 0.1640 -0.0135 0.0311  0.0164  27  ALA   A CB  
748  N  N   A LYS   A 28  ? 0.2552 0.3042 0.1860 -0.0738 0.0394  -0.0405 28  LYS   A N   
749  N  N   B LYS   A 28  ? 0.2405 0.2917 0.1960 -0.0013 0.0215  -0.0021 28  LYS   A N   
750  C  CA  A LYS   A 28  ? 0.2890 0.3352 0.2131 -0.0655 0.0501  -0.0579 28  LYS   A CA  
751  C  CA  B LYS   A 28  ? 0.2655 0.3107 0.2154 0.0046  0.0183  -0.0149 28  LYS   A CA  
752  C  C   A LYS   A 28  ? 0.3111 0.3641 0.2057 -0.0695 0.0707  -0.0444 28  LYS   A C   
753  C  C   B LYS   A 28  ? 0.2903 0.3304 0.2153 -0.0004 0.0151  -0.0108 28  LYS   A C   
754  O  O   A LYS   A 28  ? 0.3190 0.3713 0.2374 -0.0677 0.0546  -0.0464 28  LYS   A O   
755  O  O   B LYS   A 28  ? 0.2961 0.3333 0.2147 0.0028  0.0030  -0.0141 28  LYS   A O   
756  C  CB  A LYS   A 28  ? 0.3026 0.3440 0.2620 -0.0511 0.0428  -0.0664 28  LYS   A CB  
757  C  CB  B LYS   A 28  ? 0.2705 0.3139 0.2444 0.0139  0.0183  -0.0231 28  LYS   A CB  
758  C  CG  A LYS   A 28  ? 0.3175 0.3516 0.3007 -0.0403 0.0402  -0.0681 28  LYS   A CG  
759  C  CG  B LYS   A 28  ? 0.2780 0.3190 0.2728 0.0194  0.0219  -0.0242 28  LYS   A CG  
760  C  CD  A LYS   A 28  ? 0.3324 0.3645 0.3543 -0.0313 0.0361  -0.0594 28  LYS   A CD  
761  C  CD  B LYS   A 28  ? 0.2880 0.3266 0.3089 0.0233  0.0246  -0.0232 28  LYS   A CD  
762  C  CE  A LYS   A 28  ? 0.3462 0.3742 0.3917 -0.0253 0.0363  -0.0570 28  LYS   A CE  
763  C  CE  B LYS   A 28  ? 0.2970 0.3329 0.3322 0.0243  0.0293  -0.0247 28  LYS   A CE  
764  N  NZ  A LYS   A 28  ? 0.3541 0.3785 0.4131 -0.0206 0.0422  -0.0637 28  LYS   A NZ  
765  N  NZ  B LYS   A 28  ? 0.3030 0.3368 0.3402 0.0245  0.0325  -0.0278 28  LYS   A NZ  
792  N  N   A LYS   A 29  ? 0.3238 0.3846 0.1973 -0.0785 0.1010  -0.0217 29  LYS   A N   
793  N  N   B LYS   A 29  ? 0.3074 0.3463 0.2303 -0.0096 0.0266  -0.0017 29  LYS   A N   
794  C  CA  A LYS   A 29  ? 0.3425 0.4088 0.2175 -0.0820 0.1215  -0.0078 29  LYS   A CA  
795  C  CA  B LYS   A 29  ? 0.3264 0.3637 0.2610 -0.0179 0.0372  0.0041  29  LYS   A CA  
796  C  C   A LYS   A 29  ? 0.3481 0.4046 0.2039 -0.0917 0.1070  0.0018  29  LYS   A C   
797  C  C   B LYS   A 29  ? 0.3329 0.3631 0.2475 -0.0304 0.0307  0.0118  29  LYS   A C   
798  O  O   A LYS   A 29  ? 0.3614 0.4195 0.2100 -0.0834 0.1029  0.0002  29  LYS   A O   
799  O  O   B LYS   A 29  ? 0.3391 0.3715 0.2524 -0.0291 0.0324  0.0146  29  LYS   A O   
800  C  CB  A LYS   A 29  ? 0.3558 0.4372 0.2719 -0.0721 0.1428  -0.0024 29  LYS   A CB  
801  C  CB  B LYS   A 29  ? 0.3387 0.3809 0.3087 -0.0120 0.0497  0.0045  29  LYS   A CB  
802  C  CG  A LYS   A 29  ? 0.3736 0.4636 0.3421 -0.0606 0.1439  0.0016  29  LYS   A CG  
803  C  CG  B LYS   A 29  ? 0.3516 0.3966 0.3593 -0.0053 0.0568  0.0055  29  LYS   A CG  
804  C  CD  A LYS   A 29  ? 0.3906 0.4855 0.4135 -0.0506 0.1378  0.0014  29  LYS   A CD  
805  C  CD  B LYS   A 29  ? 0.3624 0.4094 0.4082 0.0008  0.0599  0.0061  29  LYS   A CD  
806  C  CE  A LYS   A 29  ? 0.4019 0.5009 0.4580 -0.0444 0.1357  0.0002  29  LYS   A CE  
807  C  CE  B LYS   A 29  ? 0.3697 0.4188 0.4409 0.0043  0.0626  0.0047  29  LYS   A CE  
808  N  NZ  A LYS   A 29  ? 0.4070 0.5094 0.4908 -0.0400 0.1317  -0.0009 29  LYS   A NZ  
809  N  NZ  B LYS   A 29  ? 0.3734 0.4238 0.4632 0.0062  0.0620  0.0056  29  LYS   A NZ  
836  N  N   A VAL   A 30  ? 0.3366 0.3837 0.1828 -0.1108 0.0968  0.0118  30  VAL   A N   
837  N  N   B VAL   A 30  ? 0.3320 0.3532 0.2375 -0.0441 0.0256  0.0156  30  VAL   A N   
838  C  CA  A VAL   A 30  ? 0.3313 0.3614 0.1787 -0.1243 0.0634  0.0276  30  VAL   A CA  
839  C  CA  B VAL   A 30  ? 0.3322 0.3423 0.2299 -0.0564 0.0127  0.0240  30  VAL   A CA  
840  C  C   A VAL   A 30  ? 0.3311 0.3490 0.1487 -0.1217 0.0432  0.0392  30  VAL   A C   
841  C  C   B VAL   A 30  ? 0.3339 0.3375 0.2109 -0.0615 0.0039  0.0262  30  VAL   A C   
842  O  O   A VAL   A 30  ? 0.3382 0.3512 0.1540 -0.1194 0.0405  0.0504  30  VAL   A O   
843  O  O   B VAL   A 30  ? 0.3377 0.3393 0.2087 -0.0613 0.0012  0.0296  30  VAL   A O   
844  C  CB  A VAL   A 30  ? 0.3289 0.3523 0.2180 -0.1408 0.0424  0.0291  30  VAL   A CB  
845  C  CB  B VAL   A 30  ? 0.3302 0.3353 0.2459 -0.0631 0.0059  0.0269  30  VAL   A CB  
846  C  CG1 A VAL   A 30  ? 0.3326 0.3482 0.2388 -0.1446 0.0353  0.0318  30  VAL   A CG1 
847  C  CG1 B VAL   A 30  ? 0.3320 0.3332 0.2573 -0.0640 0.0033  0.0269  30  VAL   A CG1 
848  C  CG2 A VAL   A 30  ? 0.3267 0.3518 0.2379 -0.1490 0.0404  0.0272  30  VAL   A CG2 
849  C  CG2 B VAL   A 30  ? 0.3291 0.3334 0.2548 -0.0672 0.0048  0.0295  30  VAL   A CG2 
868  N  N   A LYS   A 31  ? 0.3255 0.3367 0.1330 -0.1186 0.0177  0.0344  31  LYS   A N   
869  N  N   B LYS   A 31  ? 0.3313 0.3313 0.2042 -0.0661 -0.0059 0.0261  31  LYS   A N   
870  C  CA  A LYS   A 31  ? 0.3345 0.3349 0.1531 -0.1015 -0.0112 0.0357  31  LYS   A CA  
871  C  CA  B LYS   A 31  ? 0.3336 0.3296 0.2155 -0.0664 -0.0174 0.0300  31  LYS   A CA  
872  C  C   A LYS   A 31  ? 0.3157 0.3174 0.1358 -0.0872 -0.0129 0.0735  31  LYS   A C   
873  C  C   B LYS   A 31  ? 0.3141 0.3133 0.1734 -0.0704 -0.0176 0.0581  31  LYS   A C   
874  O  O   A LYS   A 31  ? 0.3227 0.3298 0.1492 -0.0837 -0.0202 0.0765  31  LYS   A O   
875  O  O   B LYS   A 31  ? 0.3202 0.3201 0.1787 -0.0678 -0.0234 0.0636  31  LYS   A O   
876  C  CB  A LYS   A 31  ? 0.3696 0.3563 0.2618 -0.0913 -0.0319 0.0092  31  LYS   A CB  
877  C  CB  B LYS   A 31  ? 0.3572 0.3456 0.2930 -0.0603 -0.0267 0.0113  31  LYS   A CB  
878  C  CG  A LYS   A 31  ? 0.4079 0.3788 0.3845 -0.0740 -0.0485 -0.0089 31  LYS   A CG  
879  C  CG  B LYS   A 31  ? 0.3815 0.3622 0.3783 -0.0512 -0.0354 -0.0023 31  LYS   A CG  
880  C  CD  A LYS   A 31  ? 0.4384 0.3972 0.4748 -0.0588 -0.0610 -0.0240 31  LYS   A CD  
881  C  CD  B LYS   A 31  ? 0.4004 0.3764 0.4445 -0.0432 -0.0429 -0.0137 31  LYS   A CD  
882  C  CE  A LYS   A 31  ? 0.4582 0.4107 0.5320 -0.0481 -0.0695 -0.0343 31  LYS   A CE  
883  C  CE  B LYS   A 31  ? 0.4130 0.3870 0.4869 -0.0374 -0.0473 -0.0212 31  LYS   A CE  
884  N  NZ  A LYS   A 31  ? 0.4680 0.4165 0.5634 -0.0416 -0.0764 -0.0407 31  LYS   A NZ  
885  N  NZ  B LYS   A 31  ? 0.4196 0.3923 0.5119 -0.0334 -0.0499 -0.0259 31  LYS   A NZ  
912  N  N   . PRO   A 32  ? 0.2854 0.2905 0.1385 -0.0789 -0.0143 0.0636  32  PRO   A N   
913  C  CA  . PRO   A 32  ? 0.2666 0.2710 0.1524 -0.0673 -0.0242 0.0739  32  PRO   A CA  
914  C  C   . PRO   A 32  ? 0.2543 0.2643 0.1579 -0.0568 -0.0335 0.0737  32  PRO   A C   
915  O  O   . PRO   A 32  ? 0.2460 0.2565 0.1717 -0.0571 -0.0378 0.0687  32  PRO   A O   
916  C  CB  . PRO   A 32  ? 0.2579 0.2700 0.1678 -0.0678 -0.0275 0.0541  32  PRO   A CB  
917  C  CG  . PRO   A 32  ? 0.2574 0.2744 0.1284 -0.0646 -0.0368 0.0421  32  PRO   A CG  
918  C  CD  . PRO   A 32  ? 0.2621 0.2793 0.1253 -0.0736 -0.0280 0.0551  32  PRO   A CD  
926  N  N   . THR   A 33  ? 0.2551 0.2623 0.1545 -0.0504 -0.0284 0.0736  33  THR   A N   
927  C  CA  . THR   A 33  ? 0.2531 0.2600 0.1640 -0.0408 -0.0396 0.0690  33  THR   A CA  
928  C  C   . THR   A 33  ? 0.2220 0.2383 0.1600 -0.0454 -0.0350 0.0575  33  THR   A C   
929  O  O   . THR   A 33  ? 0.2192 0.2378 0.1693 -0.0511 -0.0451 0.0551  33  THR   A O   
930  C  CB  . THR   A 33  ? 0.2819 0.2829 0.1741 -0.0309 -0.0481 0.0861  33  THR   A CB  
931  O  OG1 . THR   A 33  ? 0.3049 0.3004 0.2016 -0.0194 -0.0409 0.0943  33  THR   A OG1 
932  C  CG2 . THR   A 33  ? 0.2879 0.2935 0.2036 -0.0259 -0.0548 0.0864  33  THR   A CG2 
940  N  N   . VAL   A 34  ? 0.1975 0.2198 0.1491 -0.0454 -0.0253 0.0539  34  VAL   A N   
941  C  CA  . VAL   A 34  ? 0.1843 0.2018 0.1354 -0.0353 -0.0196 0.0418  34  VAL   A CA  
942  C  C   . VAL   A 34  ? 0.1768 0.1912 0.1209 -0.0344 -0.0087 0.0372  34  VAL   A C   
943  O  O   . VAL   A 34  ? 0.1775 0.1902 0.1546 -0.0424 -0.0119 0.0461  34  VAL   A O   
944  C  CB  . VAL   A 34  ? 0.1862 0.1986 0.1520 -0.0344 -0.0081 0.0353  34  VAL   A CB  
945  C  CG1 . VAL   A 34  ? 0.1912 0.1990 0.1574 -0.0314 0.0006  0.0214  34  VAL   A CG1 
946  C  CG2 . VAL   A 34  ? 0.1904 0.2116 0.1900 -0.0237 -0.0171 0.0344  34  VAL   A CG2 
956  N  N   . VAL   A 35  ? 0.1589 0.1746 0.1250 -0.0351 -0.0099 0.0300  35  VAL   A N   
957  C  CA  . VAL   A 35  ? 0.1498 0.1691 0.1321 -0.0287 0.0002  0.0271  35  VAL   A CA  
958  C  C   . VAL   A 35  ? 0.1432 0.1569 0.1314 -0.0194 0.0002  0.0185  35  VAL   A C   
959  O  O   . VAL   A 35  ? 0.1367 0.1661 0.1468 -0.0247 0.0132  0.0156  35  VAL   A O   
960  C  CB  . VAL   A 35  ? 0.1571 0.1748 0.1347 -0.0187 0.0096  0.0093  35  VAL   A CB  
961  C  CG1 . VAL   A 35  ? 0.1665 0.1806 0.1419 -0.0107 0.0002  0.0097  35  VAL   A CG1 
962  C  CG2 . VAL   A 35  ? 0.1563 0.1765 0.1554 -0.0131 0.0087  -0.0009 35  VAL   A CG2 
972  N  N   . VAL   A 36  ? 0.1284 0.1514 0.1256 -0.0202 0.0046  0.0279  36  VAL   A N   
973  C  CA  . VAL   A 36  ? 0.1286 0.1382 0.1192 -0.0128 0.0051  0.0196  36  VAL   A CA  
974  C  C   . VAL   A 36  ? 0.1247 0.1446 0.1249 -0.0137 0.0062  0.0187  36  VAL   A C   
975  O  O   . VAL   A 36  ? 0.1300 0.1444 0.1476 -0.0156 0.0161  0.0195  36  VAL   A O   
976  C  CB  . VAL   A 36  ? 0.1272 0.1334 0.1401 -0.0103 0.0036  0.0178  36  VAL   A CB  
977  C  CG1 . VAL   A 36  ? 0.1345 0.1403 0.1492 -0.0148 0.0087  0.0055  36  VAL   A CG1 
978  C  CG2 . VAL   A 36  ? 0.1406 0.1390 0.1549 -0.0113 -0.0018 0.0218  36  VAL   A CG2 
988  N  N   . ASN   A 37  ? 0.1215 0.1305 0.1287 -0.0038 0.0085  0.0193  37  ASN   A N   
989  C  CA  . ASN   A 37  ? 0.1195 0.1267 0.1160 0.0008  0.0045  0.0195  37  ASN   A CA  
990  C  C   . ASN   A 37  ? 0.1156 0.1243 0.1318 -0.0092 0.0076  0.0242  37  ASN   A C   
991  O  O   . ASN   A 37  ? 0.1317 0.1348 0.1264 0.0029  0.0152  0.0143  37  ASN   A O   
992  C  CB  . ASN   A 37  ? 0.1226 0.1324 0.1333 -0.0038 0.0036  0.0151  37  ASN   A CB  
993  C  CG  . ASN   A 37  ? 0.1255 0.1297 0.1393 0.0001  0.0061  0.0170  37  ASN   A CG  
994  O  OD1 . ASN   A 37  ? 0.1206 0.1305 0.1640 -0.0016 0.0058  0.0211  37  ASN   A OD1 
995  N  ND2 . ASN   A 37  ? 0.1262 0.1305 0.1473 -0.0020 -0.0000 0.0292  37  ASN   A ND2 
1002 N  N   A ALA   A 38  ? 0.1224 0.1311 0.1242 -0.0035 0.0150  0.0111  38  ALA   A N   
1003 N  N   B ALA   A 38  ? 0.1257 0.1338 0.1352 -0.0075 0.0037  0.0215  38  ALA   A N   
1004 C  CA  A ALA   A 38  ? 0.1287 0.1323 0.1163 -0.0036 0.0084  0.0022  38  ALA   A CA  
1005 C  CA  B ALA   A 38  ? 0.1348 0.1410 0.1439 -0.0069 -0.0076 0.0212  38  ALA   A CA  
1006 C  C   A ALA   A 38  ? 0.1247 0.1342 0.1098 -0.0031 0.0044  0.0027  38  ALA   A C   
1007 C  C   B ALA   A 38  ? 0.1298 0.1424 0.1442 -0.0032 -0.0130 0.0227  38  ALA   A C   
1008 O  O   A ALA   A 38  ? 0.1223 0.1292 0.1195 -0.0073 -0.0044 -0.0021 38  ALA   A O   
1009 O  O   B ALA   A 38  ? 0.1220 0.1362 0.1614 -0.0069 -0.0196 0.0199  38  ALA   A O   
1010 C  CB  A ALA   A 38  ? 0.1271 0.1455 0.1250 -0.0151 0.0059  -0.0026 38  ALA   A CB  
1011 C  CB  B ALA   A 38  ? 0.1428 0.1508 0.1579 -0.0127 -0.0123 0.0152  38  ALA   A CB  
1022 N  N   A ALA   A 39  ? 0.1212 0.1309 0.1324 0.0009  0.0096  0.0103  39  ALA   A N   
1023 N  N   B ALA   A 39  ? 0.1319 0.1463 0.1439 -0.0034 -0.0095 0.0354  39  ALA   A N   
1024 C  CA  A ALA   A 39  ? 0.1224 0.1195 0.1273 0.0032  0.0090  0.0002  39  ALA   A CA  
1025 C  CA  B ALA   A 39  ? 0.1371 0.1477 0.1382 -0.0043 -0.0070 0.0357  39  ALA   A CA  
1026 C  C   A ALA   A 39  ? 0.1221 0.1249 0.1295 0.0002  0.0020  -0.0004 39  ALA   A C   
1027 C  C   B ALA   A 39  ? 0.1297 0.1405 0.1352 -0.0039 -0.0005 0.0300  39  ALA   A C   
1028 O  O   A ALA   A 39  ? 0.1409 0.1296 0.1344 0.0014  0.0058  -0.0036 39  ALA   A O   
1029 O  O   B ALA   A 39  ? 0.1345 0.1416 0.1398 -0.0100 0.0104  0.0340  39  ALA   A O   
1030 C  CB  A ALA   A 39  ? 0.1210 0.1222 0.1479 0.0036  -0.0033 -0.0022 39  ALA   A CB  
1031 C  CB  B ALA   A 39  ? 0.1510 0.1573 0.1488 -0.0045 -0.0139 0.0247  39  ALA   A CB  
1042 N  N   A ASN   A 40  ? 0.1257 0.1298 0.1353 -0.0095 0.0170  0.0055  40  ASN   A N   
1043 N  N   B ASN   A 40  ? 0.1330 0.1347 0.1298 0.0005  0.0113  0.0266  40  ASN   A N   
1044 C  CA  A ASN   A 40  ? 0.1358 0.1305 0.1357 -0.0050 0.0083  0.0032  40  ASN   A CA  
1045 C  CA  B ASN   A 40  ? 0.1377 0.1345 0.1345 0.0046  0.0091  0.0243  40  ASN   A CA  
1046 C  C   A ASN   A 40  ? 0.1397 0.1205 0.1248 -0.0089 0.0172  0.0106  40  ASN   A C   
1047 C  C   B ASN   A 40  ? 0.1370 0.1318 0.1295 0.0024  0.0143  0.0231  40  ASN   A C   
1048 O  O   A ASN   A 40  ? 0.1371 0.1260 0.1312 -0.0112 0.0191  0.0156  40  ASN   A O   
1049 O  O   B ASN   A 40  ? 0.1330 0.1314 0.1353 -0.0013 0.0116  0.0226  40  ASN   A O   
1050 C  CB  A ASN   A 40  ? 0.1478 0.1380 0.1439 0.0031  0.0019  0.0051  40  ASN   A CB  
1051 C  CB  B ASN   A 40  ? 0.1472 0.1364 0.1457 0.0050  0.0141  0.0228  40  ASN   A CB  
1052 C  CG  A ASN   A 40  ? 0.1618 0.1403 0.1599 0.0075  -0.0074 0.0092  40  ASN   A CG  
1053 C  CG  B ASN   A 40  ? 0.1546 0.1396 0.1698 -0.0013 0.0234  0.0182  40  ASN   A CG  
1054 O  OD1 A ASN   A 40  ? 0.1741 0.1342 0.1879 0.0071  -0.0154 0.0082  40  ASN   A OD1 
1055 O  OD1 B ASN   A 40  ? 0.1608 0.1392 0.1758 -0.0098 0.0324  0.0184  40  ASN   A OD1 
1056 N  ND2 A ASN   A 40  ? 0.1650 0.1541 0.1572 0.0092  -0.0065 -0.0082 40  ASN   A ND2 
1057 N  ND2 B ASN   A 40  ? 0.1587 0.1521 0.1893 -0.0041 0.0270  0.0075  40  ASN   A ND2 
1070 N  N   A VAL   A 41  ? 0.1406 0.1225 0.1216 -0.0028 0.0145  0.0165  41  VAL   A N   
1071 N  N   B VAL   A 41  ? 0.1414 0.1358 0.1303 0.0039  0.0144  0.0236  41  VAL   A N   
1072 C  CA  A VAL   A 41  ? 0.1431 0.1304 0.1379 0.0007  0.0205  0.0169  41  VAL   A CA  
1073 C  CA  B VAL   A 41  ? 0.1430 0.1386 0.1356 0.0035  0.0210  0.0271  41  VAL   A CA  
1074 C  C   A VAL   A 41  ? 0.1392 0.1278 0.1409 0.0011  0.0224  0.0167  41  VAL   A C   
1075 C  C   B VAL   A 41  ? 0.1455 0.1341 0.1380 -0.0004 0.0203  0.0261  41  VAL   A C   
1076 O  O   A VAL   A 41  ? 0.1446 0.1303 0.1547 0.0040  0.0145  0.0076  41  VAL   A O   
1077 O  O   B VAL   A 41  ? 0.1462 0.1285 0.1413 -0.0038 0.0131  0.0190  41  VAL   A O   
1078 C  CB  A VAL   A 41  ? 0.1468 0.1382 0.1406 0.0017  0.0273  0.0098  41  VAL   A CB  
1079 C  CB  B VAL   A 41  ? 0.1497 0.1490 0.1418 0.0054  0.0312  0.0261  41  VAL   A CB  
1080 C  CG1 A VAL   A 41  ? 0.1491 0.1372 0.1478 0.0033  0.0191  -0.0008 41  VAL   A CG1 
1081 C  CG1 B VAL   A 41  ? 0.1662 0.1540 0.1579 0.0035  0.0321  0.0173  41  VAL   A CG1 
1082 C  CG2 A VAL   A 41  ? 0.1551 0.1462 0.1411 0.0015  0.0305  0.0063  41  VAL   A CG2 
1083 C  CG2 B VAL   A 41  ? 0.1484 0.1547 0.1378 0.0056  0.0275  0.0209  41  VAL   A CG2 
1102 N  N   A TYR   A 42  ? 0.1355 0.1249 0.1645 -0.0027 0.0315  0.0204  42  TYR   A N   
1103 N  N   B TYR   A 42  ? 0.1462 0.1329 0.1481 0.0020  0.0215  0.0282  42  TYR   A N   
1104 C  CA  A TYR   A 42  ? 0.1409 0.1245 0.1668 -0.0061 0.0345  0.0243  42  TYR   A CA  
1105 C  CA  B TYR   A 42  ? 0.1482 0.1344 0.1535 0.0046  0.0247  0.0275  42  TYR   A CA  
1106 C  C   A TYR   A 42  ? 0.1345 0.1272 0.1591 -0.0082 0.0267  0.0225  42  TYR   A C   
1107 C  C   B TYR   A 42  ? 0.1394 0.1329 0.1513 0.0019  0.0213  0.0250  42  TYR   A C   
1108 O  O   A TYR   A 42  ? 0.1361 0.1295 0.1804 -0.0191 0.0248  0.0069  42  TYR   A O   
1109 O  O   B TYR   A 42  ? 0.1393 0.1372 0.1649 -0.0005 0.0229  0.0197  42  TYR   A O   
1110 C  CB  A TYR   A 42  ? 0.1609 0.1342 0.1711 -0.0095 0.0457  0.0319  42  TYR   A CB  
1111 C  CB  B TYR   A 42  ? 0.1625 0.1422 0.1612 0.0071  0.0236  0.0258  42  TYR   A CB  
1112 C  CG  A TYR   A 42  ? 0.1783 0.1421 0.1696 -0.0072 0.0338  0.0330  42  TYR   A CG  
1113 C  CG  B TYR   A 42  ? 0.1738 0.1481 0.1574 0.0125  0.0101  0.0237  42  TYR   A CG  
1114 C  CD1 A TYR   A 42  ? 0.1870 0.1552 0.1736 -0.0175 0.0309  0.0329  42  TYR   A CD1 
1115 C  CD1 B TYR   A 42  ? 0.1761 0.1526 0.1560 0.0074  0.0110  0.0252  42  TYR   A CD1 
1116 C  CD2 A TYR   A 42  ? 0.1890 0.1622 0.1807 -0.0026 0.0295  0.0258  42  TYR   A CD2 
1117 C  CD2 B TYR   A 42  ? 0.1854 0.1622 0.1667 0.0154  0.0074  0.0174  42  TYR   A CD2 
1118 C  CE1 A TYR   A 42  ? 0.1950 0.1628 0.1597 -0.0149 0.0246  0.0296  42  TYR   A CE1 
1119 C  CE1 B TYR   A 42  ? 0.1809 0.1589 0.1515 0.0066  0.0161  0.0221  42  TYR   A CE1 
1120 C  CE2 A TYR   A 42  ? 0.1968 0.1723 0.1887 -0.0082 0.0234  0.0270  42  TYR   A CE2 
1121 C  CE2 B TYR   A 42  ? 0.1909 0.1701 0.1689 0.0137  0.0161  0.0154  42  TYR   A CE2 
1122 C  CZ  A TYR   A 42  ? 0.2025 0.1735 0.1660 -0.0160 0.0277  0.0271  42  TYR   A CZ  
1123 C  CZ  B TYR   A 42  ? 0.1880 0.1700 0.1560 0.0077  0.0246  0.0172  42  TYR   A CZ  
1124 O  OH  A TYR   A 42  ? 0.2152 0.1871 0.1897 -0.0204 0.0148  0.0088  42  TYR   A OH  
1125 O  OH  B TYR   A 42  ? 0.1857 0.1828 0.1590 -0.0001 0.0354  0.0146  42  TYR   A OH  
1144 N  N   . LEU   A 43  ? 0.1326 0.1263 0.1483 -0.0035 0.0144  0.0081  43  LEU   A N   
1145 C  CA  . LEU   A 43  ? 0.1253 0.1264 0.1413 -0.0067 0.0156  0.0100  43  LEU   A CA  
1146 C  C   . LEU   A 43  ? 0.1322 0.1311 0.1511 -0.0022 0.0111  0.0070  43  LEU   A C   
1147 O  O   . LEU   A 43  ? 0.1513 0.1345 0.1727 0.0015  -0.0051 -0.0003 43  LEU   A O   
1148 C  CB  . LEU   A 43  ? 0.1339 0.1253 0.1534 -0.0076 0.0094  0.0112  43  LEU   A CB  
1149 C  CG  . LEU   A 43  ? 0.1389 0.1289 0.1666 -0.0048 -0.0012 0.0108  43  LEU   A CG  
1150 C  CD1 . LEU   A 43  ? 0.1454 0.1301 0.1816 -0.0051 -0.0082 0.0111  43  LEU   A CD1 
1151 C  CD2 . LEU   A 43  ? 0.1543 0.1325 0.1592 -0.0068 0.0061  0.0165  43  LEU   A CD2 
1164 N  N   A LYS   A 44  ? 0.1435 0.1263 0.1461 0.0003  0.0123  0.0153  44  LYS   A N   
1165 N  N   B LYS   A 44  ? 0.1442 0.1335 0.1533 -0.0016 0.0082  0.0113  44  LYS   A N   
1166 C  CA  A LYS   A 44  ? 0.1493 0.1337 0.1459 -0.0039 0.0192  0.0163  44  LYS   A CA  
1167 C  CA  B LYS   A 44  ? 0.1524 0.1419 0.1603 -0.0042 0.0068  0.0103  44  LYS   A CA  
1168 C  C   A LYS   A 44  ? 0.1369 0.1353 0.1281 0.0027  -0.0003 0.0119  44  LYS   A C   
1169 C  C   B LYS   A 44  ? 0.1400 0.1375 0.1424 -0.0005 -0.0003 0.0107  44  LYS   A C   
1170 O  O   A LYS   A 44  ? 0.1441 0.1524 0.1400 0.0013  0.0046  -0.0006 44  LYS   A O   
1171 O  O   B LYS   A 44  ? 0.1445 0.1475 0.1479 -0.0016 0.0040  0.0034  44  LYS   A O   
1172 C  CB  A LYS   A 44  ? 0.1836 0.1489 0.1760 0.0005  0.0382  0.0311  44  LYS   A CB  
1173 C  CB  B LYS   A 44  ? 0.1809 0.1598 0.1940 -0.0020 0.0103  0.0121  44  LYS   A CB  
1174 C  CG  A LYS   A 44  ? 0.2130 0.1762 0.2371 -0.0056 0.0600  0.0409  44  LYS   A CG  
1175 C  CG  B LYS   A 44  ? 0.2058 0.1837 0.2443 -0.0048 0.0168  0.0154  44  LYS   A CG  
1176 C  CD  A LYS   A 44  ? 0.2465 0.2241 0.3364 -0.0115 0.0528  0.0327  44  LYS   A CD  
1177 C  CD  B LYS   A 44  ? 0.2315 0.2169 0.3087 -0.0115 0.0118  0.0153  44  LYS   A CD  
1178 C  CE  A LYS   A 44  ? 0.2647 0.2543 0.3998 -0.0152 0.0510  0.0301  44  LYS   A CE  
1179 C  CE  B LYS   A 44  ? 0.2460 0.2385 0.3509 -0.0190 0.0100  0.0193  44  LYS   A CE  
1180 N  NZ  A LYS   A 44  ? 0.2720 0.2722 0.4282 -0.0173 0.0453  0.0251  44  LYS   A NZ  
1181 N  NZ  B LYS   A 44  ? 0.2534 0.2524 0.3694 -0.0245 0.0062  0.0231  44  LYS   A NZ  
1208 N  N   . HIS   A 45  ? 0.1298 0.1244 0.1448 -0.0001 0.0010  0.0186  45  HIS   A N   
1209 C  CA  . HIS   A 45  ? 0.1313 0.1300 0.1457 -0.0028 -0.0092 0.0116  45  HIS   A CA  
1210 C  C   . HIS   A 45  ? 0.1369 0.1417 0.1574 0.0009  -0.0003 0.0182  45  HIS   A C   
1211 O  O   . HIS   A 45  ? 0.1588 0.1537 0.1940 0.0223  -0.0032 -0.0003 45  HIS   A O   
1212 C  CB  . HIS   A 45  ? 0.1367 0.1283 0.1393 -0.0025 -0.0021 0.0047  45  HIS   A CB  
1213 C  CG  . HIS   A 45  ? 0.1280 0.1263 0.1309 -0.0050 0.0026  0.0090  45  HIS   A CG  
1214 N  ND1 . HIS   A 45  ? 0.1204 0.1334 0.1503 -0.0007 -0.0022 0.0127  45  HIS   A ND1 
1215 C  CD2 . HIS   A 45  ? 0.1287 0.1306 0.1435 -0.0089 -0.0012 0.0215  45  HIS   A CD2 
1216 C  CE1 . HIS   A 45  ? 0.1283 0.1372 0.1349 -0.0084 -0.0035 0.0187  45  HIS   A CE1 
1217 N  NE2 . HIS   A 45  ? 0.1228 0.1415 0.1411 -0.0048 0.0018  0.0240  45  HIS   A NE2 
1226 N  N   A GLY   A 46  ? 0.1504 0.1505 0.1693 0.0091  -0.0182 0.0225  46  GLY   A N   
1227 N  N   B GLY   A 46  ? 0.1456 0.1499 0.1625 0.0095  -0.0072 0.0200  46  GLY   A N   
1228 C  CA  A GLY   A 46  ? 0.1579 0.1589 0.1920 0.0140  -0.0229 0.0274  46  GLY   A CA  
1229 C  CA  B GLY   A 46  ? 0.1517 0.1554 0.1708 0.0161  -0.0083 0.0218  46  GLY   A CA  
1230 C  C   A GLY   A 46  ? 0.1626 0.1530 0.1999 0.0215  -0.0298 0.0304  46  GLY   A C   
1231 C  C   B GLY   A 46  ? 0.1566 0.1518 0.1614 0.0236  -0.0107 0.0196  46  GLY   A C   
1232 O  O   A GLY   A 46  ? 0.1609 0.1649 0.2390 0.0171  -0.0492 0.0067  46  GLY   A O   
1233 O  O   B GLY   A 46  ? 0.1566 0.1537 0.1801 0.0242  -0.0221 0.0091  46  GLY   A O   
1240 N  N   A GLY   A 47  ? 0.1623 0.1495 0.1678 0.0218  -0.0230 0.0189  47  GLY   A N   
1241 N  N   B GLY   A 47  ? 0.1569 0.1516 0.1391 0.0219  -0.0042 0.0085  47  GLY   A N   
1242 C  CA  A GLY   A 47  ? 0.1613 0.1506 0.1441 0.0237  -0.0320 0.0011  47  GLY   A CA  
1243 C  CA  B GLY   A 47  ? 0.1615 0.1551 0.1287 0.0187  -0.0159 0.0024  47  GLY   A CA  
1244 C  C   A GLY   A 47  ? 0.1504 0.1465 0.1484 0.0204  -0.0405 -0.0077 47  GLY   A C   
1245 C  C   B GLY   A 47  ? 0.1594 0.1551 0.1143 0.0214  -0.0118 -0.0133 47  GLY   A C   
1246 O  O   A GLY   A 47  ? 0.1518 0.1416 0.1668 0.0242  -0.0463 0.0036  47  GLY   A O   
1247 O  O   B GLY   A 47  ? 0.1612 0.1532 0.1036 0.0231  -0.0081 -0.0052 47  GLY   A O   
1254 N  N   A GLY   A 48  ? 0.1438 0.1451 0.1595 0.0217  -0.0415 -0.0067 48  GLY   A N   
1255 N  N   B GLY   A 48  ? 0.1580 0.1569 0.1340 0.0143  -0.0229 -0.0188 48  GLY   A N   
1256 C  CA  A GLY   A 48  ? 0.1449 0.1392 0.1852 0.0089  -0.0371 -0.0103 48  GLY   A CA  
1257 C  CA  B GLY   A 48  ? 0.1547 0.1537 0.1422 0.0128  -0.0169 -0.0180 48  GLY   A CA  
1258 C  C   A GLY   A 48  ? 0.1371 0.1348 0.1690 -0.0009 -0.0160 -0.0005 48  GLY   A C   
1259 C  C   B GLY   A 48  ? 0.1475 0.1530 0.1387 0.0089  -0.0028 -0.0070 48  GLY   A C   
1260 O  O   A GLY   A 48  ? 0.1511 0.1318 0.1691 0.0012  -0.0124 0.0028  48  GLY   A O   
1261 O  O   B GLY   A 48  ? 0.1597 0.1510 0.1393 0.0092  0.0047  -0.0113 48  GLY   A O   
1268 N  N   A VAL   A 49  ? 0.1255 0.1287 0.1751 -0.0056 -0.0133 0.0029  49  VAL   A N   
1269 N  N   B VAL   A 49  ? 0.1337 0.1497 0.1439 0.0058  0.0010  -0.0087 49  VAL   A N   
1270 C  CA  A VAL   A 49  ? 0.1411 0.1275 0.1674 -0.0095 0.0041  0.0085  49  VAL   A CA  
1271 C  CA  B VAL   A 49  ? 0.1259 0.1498 0.1463 0.0031  0.0110  0.0020  49  VAL   A CA  
1272 C  C   A VAL   A 49  ? 0.1389 0.1195 0.1426 -0.0017 0.0058  0.0199  49  VAL   A C   
1273 C  C   B VAL   A 49  ? 0.1275 0.1468 0.1228 0.0027  0.0130  -0.0082 49  VAL   A C   
1274 O  O   A VAL   A 49  ? 0.1410 0.1272 0.1487 -0.0046 0.0106  0.0133  49  VAL   A O   
1275 O  O   B VAL   A 49  ? 0.1275 0.1563 0.1252 0.0057  0.0174  -0.0094 49  VAL   A O   
1276 C  CB  A VAL   A 49  ? 0.1536 0.1306 0.1773 -0.0106 0.0051  -0.0088 49  VAL   A CB  
1277 C  CB  B VAL   A 49  ? 0.1146 0.1464 0.1656 0.0097  0.0148  0.0091  49  VAL   A CB  
1278 C  CG1 A VAL   A 49  ? 0.1550 0.1265 0.1920 -0.0044 0.0119  -0.0057 49  VAL   A CG1 
1279 C  CG1 B VAL   A 49  ? 0.1069 0.1373 0.1674 0.0210  0.0186  0.0194  49  VAL   A CG1 
1280 C  CG2 A VAL   A 49  ? 0.1621 0.1389 0.2215 -0.0252 0.0054  -0.0019 49  VAL   A CG2 
1281 C  CG2 B VAL   A 49  ? 0.1157 0.1503 0.1802 0.0183  0.0126  0.0111  49  VAL   A CG2 
1300 N  N   A ALA   A 50  ? 0.1308 0.1178 0.1329 -0.0030 -0.0129 0.0193  50  ALA   A N   
1301 N  N   B ALA   A 50  ? 0.1295 0.1434 0.1117 -0.0016 0.0076  -0.0128 50  ALA   A N   
1302 C  CA  A ALA   A 50  ? 0.1244 0.1222 0.1380 -0.0060 -0.0086 0.0194  50  ALA   A CA  
1303 C  CA  B ALA   A 50  ? 0.1310 0.1390 0.1049 -0.0105 -0.0008 -0.0152 50  ALA   A CA  
1304 C  C   A ALA   A 50  ? 0.1212 0.1223 0.1415 -0.0052 -0.0051 0.0169  50  ALA   A C   
1305 C  C   B ALA   A 50  ? 0.1329 0.1376 0.1028 -0.0082 -0.0004 -0.0107 50  ALA   A C   
1306 O  O   A ALA   A 50  ? 0.1192 0.1240 0.1619 0.0017  -0.0100 0.0109  50  ALA   A O   
1307 O  O   B ALA   A 50  ? 0.1342 0.1428 0.1110 -0.0084 0.0024  -0.0088 50  ALA   A O   
1308 C  CB  A ALA   A 50  ? 0.1214 0.1269 0.1336 -0.0063 -0.0073 0.0184  50  ALA   A CB  
1309 C  CB  B ALA   A 50  ? 0.1341 0.1385 0.1060 -0.0072 0.0004  -0.0199 50  ALA   A CB  
1320 N  N   A GLY   A 51  ? 0.1283 0.1197 0.1498 0.0051  -0.0081 0.0103  51  GLY   A N   
1321 N  N   B GLY   A 51  ? 0.1362 0.1342 0.1198 -0.0006 -0.0048 -0.0128 51  GLY   A N   
1322 C  CA  A GLY   A 51  ? 0.1418 0.1190 0.1506 0.0058  -0.0143 0.0153  51  GLY   A CA  
1323 C  CA  B GLY   A 51  ? 0.1414 0.1338 0.1272 -0.0000 -0.0108 -0.0089 51  GLY   A CA  
1324 C  C   A GLY   A 51  ? 0.1267 0.1304 0.1481 0.0078  -0.0034 -0.0002 51  GLY   A C   
1325 C  C   B GLY   A 51  ? 0.1301 0.1385 0.1350 0.0032  -0.0047 -0.0093 51  GLY   A C   
1326 O  O   A GLY   A 51  ? 0.1310 0.1389 0.1626 0.0012  -0.0050 -0.0040 51  GLY   A O   
1327 O  O   B GLY   A 51  ? 0.1321 0.1445 0.1419 -0.0007 -0.0094 -0.0101 51  GLY   A O   
1334 N  N   . ALA   A 52  ? 0.1252 0.1413 0.1442 0.0029  -0.0004 -0.0100 52  ALA   A N   
1335 C  CA  . ALA   A 52  ? 0.1264 0.1544 0.1678 -0.0015 0.0059  -0.0096 52  ALA   A CA  
1336 C  C   . ALA   A 52  ? 0.1262 0.1486 0.1442 -0.0080 0.0087  -0.0085 52  ALA   A C   
1337 O  O   . ALA   A 52  ? 0.1390 0.1563 0.1568 -0.0035 0.0071  -0.0124 52  ALA   A O   
1338 C  CB  . ALA   A 52  ? 0.1409 0.1815 0.1771 -0.0106 0.0055  -0.0064 52  ALA   A CB  
1345 N  N   A LEU   A 53  ? 0.1270 0.1456 0.1391 -0.0089 0.0067  0.0011  53  LEU   A N   
1346 N  N   B LEU   A 53  ? 0.1247 0.1485 0.1385 -0.0034 0.0042  -0.0040 53  LEU   A N   
1347 C  CA  A LEU   A 53  ? 0.1403 0.1492 0.1320 -0.0089 0.0100  0.0109  53  LEU   A CA  
1348 C  CA  B LEU   A 53  ? 0.1304 0.1509 0.1322 0.0003  0.0031  -0.0001 53  LEU   A CA  
1349 C  C   A LEU   A 53  ? 0.1347 0.1535 0.1067 -0.0051 0.0059  0.0116  53  LEU   A C   
1350 C  C   B LEU   A 53  ? 0.1316 0.1555 0.1157 0.0037  -0.0052 -0.0037 53  LEU   A C   
1351 O  O   A LEU   A 53  ? 0.1466 0.1658 0.1289 -0.0184 0.0040  0.0094  53  LEU   A O   
1352 O  O   B LEU   A 53  ? 0.1409 0.1633 0.1236 -0.0031 -0.0128 0.0004  53  LEU   A O   
1353 C  CB  A LEU   A 53  ? 0.1481 0.1496 0.1314 -0.0101 0.0100  0.0108  53  LEU   A CB  
1354 C  CB  B LEU   A 53  ? 0.1282 0.1473 0.1298 0.0009  0.0036  0.0000  53  LEU   A CB  
1355 C  CG  A LEU   A 53  ? 0.1538 0.1519 0.1485 -0.0098 0.0046  0.0160  53  LEU   A CG  
1356 C  CG  B LEU   A 53  ? 0.1261 0.1454 0.1286 -0.0013 -0.0044 -0.0011 53  LEU   A CG  
1357 C  CD1 A LEU   A 53  ? 0.1495 0.1625 0.1560 -0.0040 0.0017  0.0263  53  LEU   A CD1 
1358 C  CD1 B LEU   A 53  ? 0.1274 0.1492 0.1339 -0.0056 -0.0001 -0.0077 53  LEU   A CD1 
1359 C  CD2 A LEU   A 53  ? 0.1636 0.1655 0.1624 -0.0180 0.0018  0.0183  53  LEU   A CD2 
1360 C  CD2 B LEU   A 53  ? 0.1277 0.1463 0.1266 0.0025  -0.0013 -0.0101 53  LEU   A CD2 
1383 N  N   A ASN   A 54  ? 0.1281 0.1427 0.1213 -0.0036 0.0040  0.0113  54  ASN   A N   
1384 N  N   B ASN   A 54  ? 0.1310 0.1505 0.1227 0.0062  -0.0041 -0.0115 54  ASN   A N   
1385 C  CA  A ASN   A 54  ? 0.1183 0.1392 0.1401 -0.0058 -0.0059 0.0111  54  ASN   A CA  
1386 C  CA  B ASN   A 54  ? 0.1270 0.1493 0.1273 0.0063  -0.0077 -0.0151 54  ASN   A CA  
1387 C  C   A ASN   A 54  ? 0.1323 0.1410 0.1377 -0.0106 0.0022  0.0083  54  ASN   A C   
1388 C  C   B ASN   A 54  ? 0.1343 0.1467 0.1268 -0.0023 -0.0020 -0.0131 54  ASN   A C   
1389 O  O   A ASN   A 54  ? 0.1320 0.1518 0.1563 -0.0085 -0.0017 0.0003  54  ASN   A O   
1390 O  O   B ASN   A 54  ? 0.1340 0.1512 0.1318 -0.0027 -0.0065 -0.0202 54  ASN   A O   
1391 C  CB  A ASN   A 54  ? 0.1167 0.1382 0.1470 -0.0152 -0.0137 0.0176  54  ASN   A CB  
1392 C  CB  B ASN   A 54  ? 0.1280 0.1528 0.1231 0.0132  -0.0081 -0.0184 54  ASN   A CB  
1393 C  CG  A ASN   A 54  ? 0.1252 0.1368 0.1630 -0.0114 -0.0072 0.0200  54  ASN   A CG  
1394 C  CG  B ASN   A 54  ? 0.1286 0.1510 0.1127 0.0227  -0.0045 -0.0285 54  ASN   A CG  
1395 O  OD1 A ASN   A 54  ? 0.1248 0.1343 0.1859 -0.0151 -0.0079 0.0263  54  ASN   A OD1 
1396 O  OD1 B ASN   A 54  ? 0.1252 0.1547 0.1055 0.0218  -0.0057 -0.0369 54  ASN   A OD1 
1397 N  ND2 A ASN   A 54  ? 0.1337 0.1423 0.1781 -0.0189 -0.0153 0.0241  54  ASN   A ND2 
1398 N  ND2 B ASN   A 54  ? 0.1368 0.1494 0.1272 0.0199  -0.0071 -0.0253 54  ASN   A ND2 
1411 N  N   . LYS   A 55  ? 0.1334 0.1447 0.1431 -0.0033 0.0003  -0.0083 55  LYS   A N   
1412 C  CA  . LYS   A 55  ? 0.1410 0.1564 0.1558 0.0052  -0.0072 -0.0110 55  LYS   A CA  
1413 C  C   . LYS   A 55  ? 0.1394 0.1612 0.1499 -0.0011 0.0007  -0.0209 55  LYS   A C   
1414 O  O   . LYS   A 55  ? 0.1529 0.1708 0.1585 0.0008  -0.0050 -0.0301 55  LYS   A O   
1415 C  CB  . LYS   A 55  ? 0.1494 0.1667 0.1734 0.0153  -0.0071 -0.0191 55  LYS   A CB  
1416 C  CG  . LYS   A 55  ? 0.1691 0.1932 0.1858 0.0358  -0.0199 -0.0282 55  LYS   A CG  
1417 C  CD  . LYS   A 55  ? 0.1851 0.2316 0.1964 0.0501  -0.0198 -0.0328 55  LYS   A CD  
1418 C  CE  . LYS   A 55  ? 0.2077 0.2713 0.2206 0.0700  -0.0271 -0.0382 55  LYS   A CE  
1419 N  NZ  . LYS   A 55  ? 0.2151 0.2920 0.2301 0.0814  -0.0357 -0.0392 55  LYS   A NZ  
1434 N  N   . ALA   A 56  ? 0.1401 0.1688 0.1556 -0.0106 0.0007  -0.0204 56  ALA   A N   
1435 C  CA  . ALA   A 56  ? 0.1528 0.1869 0.1526 -0.0151 0.0108  -0.0209 56  ALA   A CA  
1436 C  C   . ALA   A 56  ? 0.1544 0.1962 0.1324 -0.0100 0.0098  -0.0284 56  ALA   A C   
1437 O  O   . ALA   A 56  ? 0.1618 0.2241 0.1446 -0.0049 0.0140  -0.0162 56  ALA   A O   
1438 C  CB  . ALA   A 56  ? 0.1615 0.2092 0.1668 -0.0259 0.0095  -0.0083 56  ALA   A CB  
1444 N  N   . THR   A 57  ? 0.1439 0.1763 0.1348 -0.0122 0.0085  -0.0177 57  THR   A N   
1445 C  CA  . THR   A 57  ? 0.1535 0.1735 0.1364 -0.0153 0.0027  -0.0156 57  THR   A CA  
1446 C  C   . THR   A 57  ? 0.1509 0.1801 0.1367 -0.0096 0.0021  -0.0168 57  THR   A C   
1447 O  O   . THR   A 57  ? 0.1451 0.1811 0.1592 -0.0140 -0.0055 -0.0240 57  THR   A O   
1448 C  CB  . THR   A 57  ? 0.1471 0.1693 0.1389 -0.0106 0.0040  -0.0109 57  THR   A CB  
1449 O  OG1 . THR   A 57  ? 0.1345 0.1637 0.1337 -0.0058 0.0026  -0.0085 57  THR   A OG1 
1450 C  CG2 . THR   A 57  ? 0.1520 0.1719 0.1323 -0.0088 -0.0051 -0.0064 57  THR   A CG2 
1458 N  N   . ASN   A 58  ? 0.1536 0.1751 0.1543 -0.0085 0.0029  -0.0306 58  ASN   A N   
1459 C  CA  . ASN   A 58  ? 0.1719 0.1714 0.1771 -0.0130 0.0143  -0.0383 58  ASN   A CA  
1460 C  C   . ASN   A 58  ? 0.1506 0.1581 0.1736 -0.0022 -0.0034 -0.0246 58  ASN   A C   
1461 O  O   . ASN   A 58  ? 0.1487 0.1692 0.1856 -0.0151 -0.0000 -0.0296 58  ASN   A O   
1462 C  CB  . ASN   A 58  ? 0.2174 0.1850 0.2180 -0.0168 0.0383  -0.0561 58  ASN   A CB  
1463 C  CG  . ASN   A 58  ? 0.2586 0.2091 0.3012 -0.0152 0.0353  -0.0382 58  ASN   A CG  
1464 O  OD1 . ASN   A 58  ? 0.2862 0.2027 0.3453 0.0184  0.0678  -0.0226 58  ASN   A OD1 
1465 N  ND2 . ASN   A 58  ? 0.2627 0.2201 0.3216 -0.0206 0.0191  -0.0447 58  ASN   A ND2 
1472 N  N   . ASN   A 59  ? 0.1324 0.1464 0.1602 -0.0041 -0.0101 -0.0122 59  ASN   A N   
1473 C  CA  . ASN   A 59  ? 0.1375 0.1384 0.1567 -0.0033 -0.0041 -0.0057 59  ASN   A CA  
1474 C  C   . ASN   A 59  ? 0.1385 0.1415 0.1449 -0.0044 -0.0012 -0.0075 59  ASN   A C   
1475 O  O   . ASN   A 59  ? 0.1377 0.1422 0.1527 -0.0101 -0.0007 0.0012  59  ASN   A O   
1476 C  CB  . ASN   A 59  ? 0.1411 0.1369 0.1571 0.0019  -0.0157 -0.0145 59  ASN   A CB  
1477 C  CG  . ASN   A 59  ? 0.1435 0.1434 0.1603 -0.0004 -0.0252 0.0007  59  ASN   A CG  
1478 O  OD1 . ASN   A 59  ? 0.1554 0.1520 0.1556 -0.0122 -0.0197 0.0036  59  ASN   A OD1 
1479 N  ND2 . ASN   A 59  ? 0.1543 0.1480 0.1708 -0.0170 -0.0117 0.0063  59  ASN   A ND2 
1486 N  N   . ALA   A 60  ? 0.1317 0.1465 0.1520 -0.0026 -0.0063 -0.0069 60  ALA   A N   
1487 C  CA  . ALA   A 60  ? 0.1353 0.1501 0.1548 -0.0029 -0.0123 -0.0003 60  ALA   A CA  
1488 C  C   . ALA   A 60  ? 0.1376 0.1455 0.1422 -0.0055 -0.0026 0.0001  60  ALA   A C   
1489 O  O   . ALA   A 60  ? 0.1269 0.1446 0.1660 -0.0062 -0.0050 -0.0112 60  ALA   A O   
1490 C  CB  . ALA   A 60  ? 0.1440 0.1604 0.1524 -0.0007 -0.0159 -0.0167 60  ALA   A CB  
1496 N  N   . MET   A 61  ? 0.1267 0.1406 0.1413 -0.0080 0.0002  -0.0038 61  MET   A N   
1497 C  CA  . MET   A 61  ? 0.1288 0.1363 0.1420 -0.0052 0.0007  0.0018  61  MET   A CA  
1498 C  C   . MET   A 61  ? 0.1257 0.1314 0.1450 -0.0092 -0.0007 -0.0033 61  MET   A C   
1499 O  O   . MET   A 61  ? 0.1278 0.1367 0.1584 -0.0038 0.0131  0.0068  61  MET   A O   
1500 C  CB  . MET   A 61  ? 0.1308 0.1370 0.1349 -0.0099 0.0025  -0.0043 61  MET   A CB  
1501 C  CG  . MET   A 61  ? 0.1280 0.1457 0.1582 -0.0105 -0.0008 -0.0031 61  MET   A CG  
1502 S  SD  . MET   A 61  ? 0.1363 0.1446 0.1801 -0.0141 0.0018  -0.0125 61  MET   A SD  
1503 C  CE  . MET   A 61  ? 0.1551 0.1599 0.2031 -0.0117 0.0135  -0.0102 61  MET   A CE  
1513 N  N   . GLN   A 62  ? 0.1223 0.1269 0.1521 -0.0124 -0.0013 -0.0071 62  GLN   A N   
1514 C  CA  . GLN   A 62  ? 0.1287 0.1250 0.1473 -0.0097 0.0057  0.0056  62  GLN   A CA  
1515 C  C   . GLN   A 62  ? 0.1325 0.1185 0.1573 -0.0014 0.0073  0.0038  62  GLN   A C   
1516 O  O   . GLN   A 62  ? 0.1361 0.1370 0.1528 -0.0047 0.0116  0.0003  62  GLN   A O   
1517 C  CB  . GLN   A 62  ? 0.1381 0.1232 0.1539 -0.0048 0.0015  0.0000  62  GLN   A CB  
1518 C  CG  . GLN   A 62  ? 0.1385 0.1231 0.1519 -0.0057 0.0007  0.0123  62  GLN   A CG  
1519 C  CD  . GLN   A 62  ? 0.1402 0.1278 0.1440 -0.0024 0.0035  0.0139  62  GLN   A CD  
1520 O  OE1 . GLN   A 62  ? 0.1444 0.1422 0.1607 -0.0032 -0.0008 0.0022  62  GLN   A OE1 
1521 N  NE2 . GLN   A 62  ? 0.1440 0.1300 0.1589 0.0023  0.0047  -0.0021 62  GLN   A NE2 
1530 N  N   . VAL   A 63  ? 0.1259 0.1302 0.1754 -0.0073 0.0078  -0.0146 63  VAL   A N   
1531 C  CA  . VAL   A 63  ? 0.1277 0.1424 0.1960 -0.0129 0.0045  -0.0102 63  VAL   A CA  
1532 C  C   . VAL   A 63  ? 0.1205 0.1393 0.1806 -0.0109 -0.0053 -0.0096 63  VAL   A C   
1533 O  O   . VAL   A 63  ? 0.1242 0.1398 0.2001 -0.0138 -0.0011 -0.0035 63  VAL   A O   
1534 C  CB  . VAL   A 63  ? 0.1422 0.1604 0.2286 -0.0140 -0.0055 -0.0358 63  VAL   A CB  
1535 C  CG1 . VAL   A 63  ? 0.1566 0.1822 0.2607 -0.0133 -0.0155 -0.0616 63  VAL   A CG1 
1536 C  CG2 . VAL   A 63  ? 0.1490 0.1561 0.2383 -0.0111 0.0049  -0.0340 63  VAL   A CG2 
1546 N  N   . GLU   A 64  ? 0.1286 0.1434 0.1710 -0.0061 -0.0007 -0.0017 64  GLU   A N   
1547 C  CA  . GLU   A 64  ? 0.1262 0.1435 0.1688 -0.0070 -0.0062 0.0043  64  GLU   A CA  
1548 C  C   . GLU   A 64  ? 0.1233 0.1378 0.1684 -0.0128 0.0009  0.0047  64  GLU   A C   
1549 O  O   . GLU   A 64  ? 0.1307 0.1380 0.1754 -0.0021 0.0063  -0.0022 64  GLU   A O   
1550 C  CB  . GLU   A 64  ? 0.1312 0.1577 0.1658 -0.0064 -0.0020 -0.0002 64  GLU   A CB  
1551 C  CG  . GLU   A 64  ? 0.1419 0.1557 0.1777 -0.0112 0.0001  0.0033  64  GLU   A CG  
1552 C  CD  . GLU   A 64  ? 0.1557 0.1662 0.1821 -0.0154 0.0021  0.0014  64  GLU   A CD  
1553 O  OE1 . GLU   A 64  ? 0.1511 0.1766 0.2028 -0.0238 0.0106  0.0038  64  GLU   A OE1 
1554 O  OE2 . GLU   A 64  ? 0.1714 0.1637 0.1764 -0.0273 -0.0066 0.0080  64  GLU   A OE2 
1561 N  N   . SER   A 65  ? 0.1201 0.1353 0.1555 -0.0002 0.0019  0.0049  65  SER   A N   
1562 C  CA  . SER   A 65  ? 0.1282 0.1289 0.1543 0.0007  -0.0019 0.0027  65  SER   A CA  
1563 C  C   . SER   A 65  ? 0.1320 0.1379 0.1488 -0.0045 -0.0030 -0.0050 65  SER   A C   
1564 O  O   . SER   A 65  ? 0.1386 0.1394 0.1717 -0.0037 0.0117  -0.0031 65  SER   A O   
1565 C  CB  . SER   A 65  ? 0.1301 0.1311 0.1573 -0.0072 0.0052  0.0054  65  SER   A CB  
1566 O  OG  . SER   A 65  ? 0.1259 0.1434 0.1642 -0.0107 -0.0070 0.0135  65  SER   A OG  
1572 N  N   . ASP   A 66  ? 0.1304 0.1328 0.1549 -0.0034 0.0127  0.0043  66  ASP   A N   
1573 C  CA  . ASP   A 66  ? 0.1377 0.1426 0.1743 -0.0030 0.0108  0.0129  66  ASP   A CA  
1574 C  C   . ASP   A 66  ? 0.1364 0.1387 0.1791 -0.0059 0.0102  0.0168  66  ASP   A C   
1575 O  O   . ASP   A 66  ? 0.1460 0.1530 0.1957 -0.0066 0.0325  0.0232  66  ASP   A O   
1576 C  CB  . ASP   A 66  ? 0.1476 0.1538 0.2030 0.0051  0.0232  0.0301  66  ASP   A CB  
1577 C  CG  . ASP   A 66  ? 0.1704 0.1682 0.2329 -0.0015 0.0051  0.0491  66  ASP   A CG  
1578 O  OD1 . ASP   A 66  ? 0.1731 0.1935 0.2113 -0.0094 -0.0077 0.0511  66  ASP   A OD1 
1579 O  OD2 . ASP   A 66  ? 0.1898 0.1829 0.3004 0.0161  -0.0126 0.0280  66  ASP   A OD2 
1584 N  N   . ASP   A 67  ? 0.1292 0.1446 0.1888 -0.0027 0.0097  0.0199  67  ASP   A N   
1585 C  CA  . ASP   A 67  ? 0.1250 0.1616 0.2020 -0.0038 0.0059  0.0196  67  ASP   A CA  
1586 C  C   . ASP   A 67  ? 0.1331 0.1588 0.1919 0.0008  0.0101  0.0275  67  ASP   A C   
1587 O  O   . ASP   A 67  ? 0.1308 0.1673 0.2156 0.0027  0.0260  0.0317  67  ASP   A O   
1588 C  CB  . ASP   A 67  ? 0.1371 0.1748 0.2375 -0.0085 -0.0108 0.0378  67  ASP   A CB  
1589 C  CG  . ASP   A 67  ? 0.1389 0.1858 0.2736 -0.0114 -0.0238 0.0454  67  ASP   A CG  
1590 O  OD1 . ASP   A 67  ? 0.1431 0.2030 0.3518 -0.0142 -0.0375 0.0595  67  ASP   A OD1 
1591 O  OD2 . ASP   A 67  ? 0.1443 0.1908 0.2570 -0.0015 -0.0142 0.0364  67  ASP   A OD2 
1596 N  N   . TYR   A 68  ? 0.1351 0.1487 0.1916 0.0015  0.0185  0.0330  68  TYR   A N   
1597 C  CA  . TYR   A 68  ? 0.1403 0.1478 0.1931 0.0011  0.0192  0.0256  68  TYR   A CA  
1598 C  C   . TYR   A 68  ? 0.1340 0.1462 0.1848 -0.0025 0.0244  0.0123  68  TYR   A C   
1599 O  O   . TYR   A 68  ? 0.1427 0.1492 0.2050 0.0064  0.0305  0.0153  68  TYR   A O   
1600 C  CB  . TYR   A 68  ? 0.1468 0.1422 0.2085 0.0108  0.0397  0.0262  68  TYR   A CB  
1601 C  CG  . TYR   A 68  ? 0.1597 0.1593 0.2477 0.0048  0.0563  0.0320  68  TYR   A CG  
1602 C  CD1 . TYR   A 68  ? 0.1642 0.1692 0.2910 -0.0210 0.0494  -0.0100 68  TYR   A CD1 
1603 C  CD2 . TYR   A 68  ? 0.1787 0.1646 0.2937 0.0137  0.0651  0.0404  68  TYR   A CD2 
1604 C  CE1 . TYR   A 68  ? 0.1708 0.1783 0.3276 -0.0202 0.0540  -0.0178 68  TYR   A CE1 
1605 C  CE2 . TYR   A 68  ? 0.1757 0.1721 0.3168 0.0080  0.0753  0.0139  68  TYR   A CE2 
1606 C  CZ  . TYR   A 68  ? 0.1743 0.1745 0.3342 -0.0204 0.0598  -0.0177 68  TYR   A CZ  
1607 O  OH  . TYR   A 68  ? 0.1999 0.1746 0.3617 -0.0174 0.0319  -0.0442 68  TYR   A OH  
1617 N  N   . ILE   A 69  ? 0.1294 0.1422 0.1848 -0.0013 0.0193  0.0125  69  ILE   A N   
1618 C  CA  . ILE   A 69  ? 0.1362 0.1417 0.1744 0.0037  0.0161  0.0061  69  ILE   A CA  
1619 C  C   . ILE   A 69  ? 0.1424 0.1462 0.1710 0.0068  0.0227  0.0213  69  ILE   A C   
1620 O  O   . ILE   A 69  ? 0.1478 0.1533 0.1763 0.0009  0.0258  0.0204  69  ILE   A O   
1621 C  CB  . ILE   A 69  ? 0.1449 0.1656 0.1805 0.0053  0.0183  -0.0010 69  ILE   A CB  
1622 C  CG1 . ILE   A 69  ? 0.1486 0.1766 0.1847 0.0055  0.0175  -0.0172 69  ILE   A CG1 
1623 C  CG2 . ILE   A 69  ? 0.1655 0.1866 0.1941 0.0187  0.0009  -0.0156 69  ILE   A CG2 
1624 C  CD1 . ILE   A 69  ? 0.1516 0.1860 0.2000 -0.0023 0.0216  -0.0166 69  ILE   A CD1 
1636 N  N   . ALA   A 70  ? 0.1455 0.1454 0.1892 -0.0063 0.0249  0.0182  70  ALA   A N   
1637 C  CA  . ALA   A 70  ? 0.1534 0.1593 0.2031 -0.0135 0.0300  0.0235  70  ALA   A CA  
1638 C  C   . ALA   A 70  ? 0.1506 0.1727 0.2021 -0.0111 0.0315  0.0218  70  ALA   A C   
1639 O  O   . ALA   A 70  ? 0.1673 0.2097 0.2297 0.0069  0.0478  0.0398  70  ALA   A O   
1640 C  CB  . ALA   A 70  ? 0.1587 0.1543 0.2275 -0.0255 0.0275  0.0226  70  ALA   A CB  
1646 N  N   . THR   A 71  ? 0.1457 0.1682 0.1950 -0.0027 0.0194  0.0221  71  THR   A N   
1647 C  CA  . THR   A 71  ? 0.1574 0.1867 0.2209 0.0126  0.0158  0.0280  71  THR   A CA  
1648 C  C   . THR   A 71  ? 0.1482 0.1814 0.2463 0.0144  0.0344  0.0242  71  THR   A C   
1649 O  O   . THR   A 71  ? 0.1505 0.2009 0.2896 0.0081  0.0466  0.0008  71  THR   A O   
1650 C  CB  . THR   A 71  ? 0.1847 0.2100 0.2572 0.0199  -0.0159 0.0414  71  THR   A CB  
1651 O  OG1 . THR   A 71  ? 0.2095 0.2274 0.2725 0.0086  -0.0351 0.0310  71  THR   A OG1 
1652 C  CG2 . THR   A 71  ? 0.1973 0.2263 0.2964 0.0247  -0.0246 0.0564  71  THR   A CG2 
1660 N  N   . ASN   A 72  ? 0.1535 0.1627 0.2188 0.0134  0.0305  0.0320  72  ASN   A N   
1661 C  CA  . ASN   A 72  ? 0.1579 0.1621 0.2257 0.0170  0.0371  0.0275  72  ASN   A CA  
1662 C  C   . ASN   A 72  ? 0.1672 0.1612 0.2139 0.0085  0.0503  0.0219  72  ASN   A C   
1663 O  O   . ASN   A 72  ? 0.1779 0.1622 0.2433 0.0124  0.0465  0.0115  72  ASN   A O   
1664 C  CB  . ASN   A 72  ? 0.1762 0.1698 0.2315 0.0106  0.0396  0.0385  72  ASN   A CB  
1665 C  CG  . ASN   A 72  ? 0.2013 0.1831 0.2408 0.0210  0.0389  0.0341  72  ASN   A CG  
1666 O  OD1 . ASN   A 72  ? 0.2174 0.2139 0.2584 0.0216  0.0442  0.0368  72  ASN   A OD1 
1667 N  ND2 . ASN   A 72  ? 0.2164 0.1808 0.2473 0.0522  0.0159  0.0282  72  ASN   A ND2 
1674 N  N   . GLY   A 73  ? 0.1687 0.1558 0.1990 0.0012  0.0447  0.0137  73  GLY   A N   
1675 C  CA  . GLY   A 73  ? 0.1726 0.1554 0.1913 -0.0038 0.0462  0.0114  73  GLY   A CA  
1676 C  C   . GLY   A 73  ? 0.1675 0.1451 0.1701 -0.0011 0.0516  0.0232  73  GLY   A C   
1677 O  O   . GLY   A 73  ? 0.1666 0.1545 0.1890 0.0128  0.0386  0.0257  73  GLY   A O   
1681 N  N   . PRO   A 74  ? 0.1770 0.1498 0.1888 -0.0159 0.0485  0.0175  74  PRO   A N   
1682 C  CA  . PRO   A 74  ? 0.1712 0.1436 0.1919 -0.0074 0.0442  0.0115  74  PRO   A CA  
1683 C  C   . PRO   A 74  ? 0.1646 0.1369 0.1937 -0.0015 0.0299  0.0056  74  PRO   A C   
1684 O  O   . PRO   A 74  ? 0.1685 0.1421 0.2149 0.0024  0.0389  0.0017  74  PRO   A O   
1685 C  CB  . PRO   A 74  ? 0.1823 0.1765 0.2152 -0.0026 0.0442  0.0260  74  PRO   A CB  
1686 C  CG  . PRO   A 74  ? 0.2103 0.2112 0.2585 -0.0197 0.0388  0.0183  74  PRO   A CG  
1687 C  CD  . PRO   A 74  ? 0.1947 0.1875 0.2128 -0.0264 0.0407  0.0091  74  PRO   A CD  
1695 N  N   . LEU   A 75  ? 0.1648 0.1298 0.1723 0.0015  0.0232  0.0015  75  LEU   A N   
1696 C  CA  . LEU   A 75  ? 0.1625 0.1266 0.1556 -0.0002 0.0146  0.0113  75  LEU   A CA  
1697 C  C   . LEU   A 75  ? 0.1720 0.1408 0.1487 0.0005  0.0170  0.0143  75  LEU   A C   
1698 O  O   . LEU   A 75  ? 0.2033 0.1548 0.1607 0.0125  0.0105  0.0070  75  LEU   A O   
1699 C  CB  . LEU   A 75  ? 0.1701 0.1372 0.1443 -0.0061 0.0154  0.0186  75  LEU   A CB  
1700 C  CG  . LEU   A 75  ? 0.1874 0.1741 0.1617 -0.0325 0.0132  0.0127  75  LEU   A CG  
1701 C  CD1 . LEU   A 75  ? 0.1940 0.2228 0.1749 -0.0368 0.0139  -0.0039 75  LEU   A CD1 
1702 C  CD2 . LEU   A 75  ? 0.2165 0.2097 0.2149 -0.0114 0.0084  0.0236  75  LEU   A CD2 
1714 N  N   . LYS   A 76  ? 0.1704 0.1400 0.1657 -0.0024 0.0108  0.0005  76  LYS   A N   
1715 C  CA  . LYS   A 76  ? 0.1675 0.1600 0.1699 -0.0076 0.0102  -0.0104 76  LYS   A CA  
1716 C  C   . LYS   A 76  ? 0.1650 0.1469 0.1450 -0.0018 0.0108  0.0098  76  LYS   A C   
1717 O  O   . LYS   A 76  ? 0.1681 0.1373 0.1470 -0.0041 0.0173  0.0167  76  LYS   A O   
1718 C  CB  . LYS   A 76  ? 0.1669 0.1811 0.2115 0.0020  0.0147  -0.0336 76  LYS   A CB  
1719 C  CG  . LYS   A 76  ? 0.1781 0.1767 0.2553 0.0088  0.0104  -0.0314 76  LYS   A CG  
1720 C  CD  . LYS   A 76  ? 0.1868 0.1728 0.3033 0.0134  -0.0040 -0.0339 76  LYS   A CD  
1721 C  CE  . LYS   A 76  ? 0.2050 0.1941 0.3580 0.0072  0.0065  -0.0403 76  LYS   A CE  
1722 N  NZ  . LYS   A 76  ? 0.2071 0.1850 0.3983 -0.0075 0.0030  -0.0482 76  LYS   A NZ  
1736 N  N   . VAL   A 77  ? 0.1774 0.1469 0.1483 -0.0038 0.0222  0.0162  77  VAL   A N   
1737 C  CA  . VAL   A 77  ? 0.1757 0.1491 0.1458 0.0034  0.0129  0.0157  77  VAL   A CA  
1738 C  C   . VAL   A 77  ? 0.1694 0.1472 0.1480 0.0075  0.0151  0.0068  77  VAL   A C   
1739 O  O   . VAL   A 77  ? 0.1761 0.1485 0.1476 0.0096  0.0320  -0.0055 77  VAL   A O   
1740 C  CB  . VAL   A 77  ? 0.1873 0.1666 0.1576 0.0008  0.0133  0.0212  77  VAL   A CB  
1741 C  CG1 . VAL   A 77  ? 0.1836 0.1826 0.1800 0.0116  0.0052  0.0049  77  VAL   A CG1 
1742 C  CG2 . VAL   A 77  ? 0.2136 0.1798 0.1825 -0.0045 -0.0002 0.0253  77  VAL   A CG2 
1752 N  N   . GLY   A 78  ? 0.1612 0.1438 0.1375 0.0046  0.0244  0.0071  78  GLY   A N   
1753 C  CA  . GLY   A 78  ? 0.1631 0.1439 0.1501 -0.0003 0.0233  0.0097  78  GLY   A CA  
1754 C  C   . GLY   A 78  ? 0.1494 0.1311 0.1561 0.0034  0.0193  0.0121  78  GLY   A C   
1755 O  O   . GLY   A 78  ? 0.1449 0.1438 0.1774 0.0024  0.0153  0.0277  78  GLY   A O   
1759 N  N   . GLY   A 79  ? 0.1540 0.1301 0.1502 0.0011  0.0150  0.0089  79  GLY   A N   
1760 C  CA  . GLY   A 79  ? 0.1523 0.1355 0.1577 -0.0026 0.0137  0.0127  79  GLY   A CA  
1761 C  C   . GLY   A 79  ? 0.1389 0.1302 0.1497 -0.0034 0.0101  0.0102  79  GLY   A C   
1762 O  O   . GLY   A 79  ? 0.1416 0.1382 0.1701 0.0156  0.0078  0.0061  79  GLY   A O   
1766 N  N   . SER   A 80  ? 0.1344 0.1426 0.1740 -0.0020 0.0142  0.0018  80  SER   A N   
1767 C  CA  . SER   A 80  ? 0.1345 0.1353 0.1658 0.0004  0.0127  0.0039  80  SER   A CA  
1768 C  C   . SER   A 80  ? 0.1323 0.1385 0.1568 -0.0033 0.0094  0.0194  80  SER   A C   
1769 O  O   . SER   A 80  ? 0.1330 0.1627 0.1934 0.0054  0.0099  0.0049  80  SER   A O   
1770 C  CB  . SER   A 80  ? 0.1494 0.1360 0.1861 -0.0094 0.0154  0.0110  80  SER   A CB  
1771 O  OG  . SER   A 80  ? 0.1730 0.1370 0.2173 0.0057  -0.0002 0.0266  80  SER   A OG  
1777 N  N   . CYS   A 81  ? 0.1341 0.1349 0.1561 -0.0005 -0.0049 0.0200  81  CYS   A N   
1778 C  CA  . CYS   A 81  ? 0.1294 0.1452 0.1584 -0.0053 -0.0103 0.0197  81  CYS   A CA  
1779 C  C   . CYS   A 81  ? 0.1261 0.1410 0.1600 -0.0130 -0.0015 0.0278  81  CYS   A C   
1780 O  O   . CYS   A 81  ? 0.1261 0.1696 0.1686 0.0003  0.0007  0.0366  81  CYS   A O   
1781 C  CB  . CYS   A 81  ? 0.1310 0.1459 0.1747 -0.0114 -0.0047 0.0260  81  CYS   A CB  
1782 S  SG  . CYS   A 81  ? 0.1495 0.1403 0.1677 -0.0146 -0.0010 0.0168  81  CYS   A SG  
1788 N  N   . VAL   A 82  ? 0.1328 0.1437 0.1599 -0.0013 -0.0095 0.0223  82  VAL   A N   
1789 C  CA  . VAL   A 82  ? 0.1450 0.1510 0.1540 0.0011  -0.0068 0.0302  82  VAL   A CA  
1790 C  C   . VAL   A 82  ? 0.1400 0.1603 0.1645 -0.0028 -0.0080 0.0303  82  VAL   A C   
1791 O  O   . VAL   A 82  ? 0.1347 0.1686 0.1850 -0.0082 -0.0071 0.0076  82  VAL   A O   
1792 C  CB  . VAL   A 82  ? 0.1707 0.1678 0.1673 0.0013  -0.0045 0.0271  82  VAL   A CB  
1793 C  CG1 . VAL   A 82  ? 0.1906 0.1757 0.1952 0.0065  0.0016  0.0240  82  VAL   A CG1 
1794 C  CG2 . VAL   A 82  ? 0.1730 0.1739 0.1985 -0.0065 -0.0120 0.0295  82  VAL   A CG2 
1804 N  N   . LEU   A 83  ? 0.1341 0.1583 0.1562 -0.0119 -0.0086 0.0148  83  LEU   A N   
1805 C  CA  . LEU   A 83  ? 0.1385 0.1569 0.1452 -0.0133 -0.0102 0.0140  83  LEU   A CA  
1806 C  C   . LEU   A 83  ? 0.1418 0.1593 0.1432 -0.0102 -0.0183 0.0175  83  LEU   A C   
1807 O  O   . LEU   A 83  ? 0.1487 0.1595 0.1644 -0.0188 -0.0096 0.0258  83  LEU   A O   
1808 C  CB  . LEU   A 83  ? 0.1454 0.1636 0.1544 -0.0127 -0.0125 0.0161  83  LEU   A CB  
1809 C  CG  . LEU   A 83  ? 0.1551 0.1690 0.1622 -0.0149 0.0065  0.0140  83  LEU   A CG  
1810 C  CD1 . LEU   A 83  ? 0.1707 0.1741 0.1695 -0.0215 -0.0072 0.0227  83  LEU   A CD1 
1811 C  CD2 . LEU   A 83  ? 0.1534 0.1806 0.1825 -0.0148 0.0154  0.0203  83  LEU   A CD2 
1823 N  N   . SER   A 84  ? 0.1563 0.1648 0.1470 -0.0145 -0.0147 0.0222  84  SER   A N   
1824 C  CA  . SER   A 84  ? 0.1707 0.1739 0.1362 -0.0147 -0.0126 0.0208  84  SER   A CA  
1825 C  C   . SER   A 84  ? 0.1672 0.1723 0.1286 -0.0220 -0.0033 0.0153  84  SER   A C   
1826 O  O   . SER   A 84  ? 0.1610 0.1833 0.1316 -0.0175 -0.0067 0.0147  84  SER   A O   
1827 C  CB  . SER   A 84  ? 0.1740 0.1919 0.1415 -0.0156 -0.0138 0.0051  84  SER   A CB  
1828 O  OG  . SER   A 84  ? 0.1756 0.2144 0.1577 -0.0146 -0.0206 -0.0021 84  SER   A OG  
1834 N  N   . GLY   A 85  ? 0.1836 0.1882 0.1353 -0.0247 0.0031  0.0147  85  GLY   A N   
1835 C  CA  . GLY   A 85  ? 0.1834 0.1919 0.1519 -0.0271 0.0116  0.0038  85  GLY   A CA  
1836 C  C   . GLY   A 85  ? 0.1829 0.1997 0.1423 -0.0261 -0.0055 0.0050  85  GLY   A C   
1837 O  O   . GLY   A 85  ? 0.1821 0.2121 0.1480 -0.0325 0.0086  -0.0076 85  GLY   A O   
1841 N  N   . HIS   A 86  ? 0.1845 0.1952 0.1358 -0.0237 -0.0114 0.0047  86  HIS   A N   
1842 C  CA  . HIS   A 86  ? 0.2020 0.2045 0.1275 -0.0236 -0.0047 0.0046  86  HIS   A CA  
1843 C  C   . HIS   A 86  ? 0.2230 0.2218 0.1139 -0.0284 -0.0123 -0.0000 86  HIS   A C   
1844 O  O   . HIS   A 86  ? 0.2322 0.2467 0.1217 -0.0253 0.0016  0.0040  86  HIS   A O   
1845 C  CB  . HIS   A 86  ? 0.1993 0.1904 0.1419 -0.0155 -0.0028 0.0064  86  HIS   A CB  
1846 C  CG  . HIS   A 86  ? 0.1900 0.1883 0.1435 -0.0122 -0.0029 0.0113  86  HIS   A CG  
1847 N  ND1 . HIS   A 86  ? 0.2007 0.1853 0.1711 -0.0187 -0.0051 0.0057  86  HIS   A ND1 
1848 C  CD2 . HIS   A 86  ? 0.1860 0.1810 0.1415 -0.0004 0.0053  0.0122  86  HIS   A CD2 
1849 C  CE1 . HIS   A 86  ? 0.1955 0.1839 0.1702 -0.0108 0.0163  0.0112  86  HIS   A CE1 
1850 N  NE2 . HIS   A 86  ? 0.1870 0.1792 0.1531 0.0044  0.0076  0.0193  86  HIS   A NE2 
1858 N  N   . ASN   A 87  ? 0.2329 0.2263 0.1327 -0.0293 0.0093  -0.0125 87  ASN   A N   
1859 C  CA  . ASN   A 87  ? 0.2566 0.2365 0.1400 -0.0249 0.0325  -0.0105 87  ASN   A CA  
1860 C  C   . ASN   A 87  ? 0.2567 0.2481 0.1640 -0.0288 0.0581  -0.0021 87  ASN   A C   
1861 O  O   . ASN   A 87  ? 0.2816 0.2648 0.1998 -0.0372 0.0898  -0.0149 87  ASN   A O   
1862 C  CB  . ASN   A 87  ? 0.2720 0.2419 0.1405 -0.0157 0.0326  -0.0128 87  ASN   A CB  
1863 C  CG  . ASN   A 87  ? 0.2882 0.2546 0.1552 -0.0060 0.0464  -0.0067 87  ASN   A CG  
1864 O  OD1 . ASN   A 87  ? 0.3031 0.2548 0.1573 0.0070  0.0441  -0.0024 87  ASN   A OD1 
1865 N  ND2 . ASN   A 87  ? 0.2912 0.2725 0.1680 -0.0061 0.0483  -0.0058 87  ASN   A ND2 
1872 N  N   . LEU   A 88  ? 0.2256 0.2318 0.1551 -0.0280 0.0344  0.0085  88  LEU   A N   
1873 C  CA  . LEU   A 88  ? 0.2052 0.2304 0.1727 -0.0323 0.0328  0.0223  88  LEU   A CA  
1874 C  C   . LEU   A 88  ? 0.1978 0.2361 0.1629 -0.0312 0.0312  0.0283  88  LEU   A C   
1875 O  O   . LEU   A 88  ? 0.1991 0.2399 0.2070 -0.0264 0.0336  0.0422  88  LEU   A O   
1876 C  CB  . LEU   A 88  ? 0.2019 0.2360 0.1730 -0.0414 0.0003  0.0313  88  LEU   A CB  
1877 C  CG  . LEU   A 88  ? 0.2235 0.2477 0.2086 -0.0378 -0.0099 0.0309  88  LEU   A CG  
1878 C  CD1 . LEU   A 88  ? 0.2331 0.2516 0.2038 -0.0426 -0.0183 0.0192  88  LEU   A CD1 
1879 C  CD2 . LEU   A 88  ? 0.2372 0.2568 0.2496 -0.0266 -0.0017 0.0207  88  LEU   A CD2 
1891 N  N   . ALA   A 89  ? 0.1949 0.2337 0.1525 -0.0329 0.0136  0.0139  89  ALA   A N   
1892 C  CA  . ALA   A 89  ? 0.1994 0.2313 0.1366 -0.0257 0.0004  0.0248  89  ALA   A CA  
1893 C  C   . ALA   A 89  ? 0.2061 0.2321 0.1444 -0.0247 -0.0107 0.0226  89  ALA   A C   
1894 O  O   . ALA   A 89  ? 0.2008 0.2232 0.1861 -0.0326 -0.0075 -0.0025 89  ALA   A O   
1895 C  CB  . ALA   A 89  ? 0.1923 0.2264 0.1312 -0.0235 0.0008  0.0256  89  ALA   A CB  
1901 N  N   . LYS   A 90  ? 0.2146 0.2490 0.1396 -0.0312 -0.0225 0.0315  90  LYS   A N   
1902 C  CA  . LYS   A 90  ? 0.2244 0.2653 0.1453 -0.0260 -0.0408 0.0289  90  LYS   A CA  
1903 C  C   . LYS   A 90  ? 0.2043 0.2419 0.1493 -0.0292 -0.0315 0.0191  90  LYS   A C   
1904 O  O   . LYS   A 90  ? 0.2081 0.2538 0.1730 -0.0328 -0.0343 0.0089  90  LYS   A O   
1905 C  CB  . LYS   A 90  ? 0.2584 0.3089 0.1640 -0.0267 -0.0428 0.0556  90  LYS   A CB  
1906 C  CG  . LYS   A 90  ? 0.3097 0.3516 0.2750 -0.0282 -0.0391 0.0631  90  LYS   A CG  
1907 C  CD  . LYS   A 90  ? 0.3748 0.4007 0.3930 -0.0328 -0.0206 0.0612  90  LYS   A CD  
1908 C  CE  . LYS   A 90  ? 0.4241 0.4420 0.4828 -0.0352 -0.0050 0.0575  90  LYS   A CE  
1909 N  NZ  . LYS   A 90  ? 0.4586 0.4649 0.5426 -0.0369 0.0024  0.0577  90  LYS   A NZ  
1923 N  N   . HIS   A 91  ? 0.1920 0.2108 0.1314 -0.0272 -0.0366 0.0290  91  HIS   A N   
1924 C  CA  . HIS   A 91  ? 0.1783 0.1905 0.1375 -0.0146 -0.0292 0.0192  91  HIS   A CA  
1925 C  C   . HIS   A 91  ? 0.1585 0.1756 0.1238 -0.0170 -0.0201 0.0193  91  HIS   A C   
1926 O  O   . HIS   A 91  ? 0.1560 0.1893 0.1437 -0.0238 -0.0079 0.0267  91  HIS   A O   
1927 C  CB  . HIS   A 91  ? 0.1995 0.2158 0.1872 0.0061  -0.0433 0.0241  91  HIS   A CB  
1928 C  CG  . HIS   A 91  ? 0.2432 0.2680 0.2451 0.0180  -0.0675 0.0085  91  HIS   A CG  
1929 N  ND1 . HIS   A 91  ? 0.2546 0.2960 0.2791 0.0225  -0.0788 -0.0087 91  HIS   A ND1 
1930 C  CD2 . HIS   A 91  ? 0.2690 0.2928 0.2642 0.0213  -0.0869 0.0143  91  HIS   A CD2 
1931 C  CE1 . HIS   A 91  ? 0.2692 0.3086 0.2882 0.0260  -0.0788 0.0048  91  HIS   A CE1 
1932 N  NE2 . HIS   A 91  ? 0.2798 0.3085 0.2813 0.0299  -0.0897 0.0141  91  HIS   A NE2 
1940 N  N   . CYS   A 92  ? 0.1480 0.1724 0.1338 -0.0195 -0.0113 0.0267  92  CYS   A N   
1941 C  CA  . CYS   A 92  ? 0.1442 0.1633 0.1349 -0.0147 -0.0008 0.0217  92  CYS   A CA  
1942 C  C   . CYS   A 92  ? 0.1412 0.1555 0.1312 -0.0171 0.0000  0.0230  92  CYS   A C   
1943 O  O   . CYS   A 92  ? 0.1381 0.1566 0.1549 -0.0196 -0.0046 0.0139  92  CYS   A O   
1944 C  CB  . CYS   A 92  ? 0.1437 0.1625 0.1410 -0.0099 -0.0069 0.0119  92  CYS   A CB  
1945 S  SG  . CYS   A 92  ? 0.1442 0.1471 0.1384 -0.0135 -0.0053 0.0149  92  CYS   A SG  
1951 N  N   . LEU   A 93  ? 0.1409 0.1413 0.1377 -0.0135 0.0049  0.0192  93  LEU   A N   
1952 C  CA  . LEU   A 93  ? 0.1266 0.1400 0.1344 -0.0090 -0.0048 0.0196  93  LEU   A CA  
1953 C  C   . LEU   A 93  ? 0.1253 0.1308 0.1281 -0.0047 0.0027  0.0161  93  LEU   A C   
1954 O  O   . LEU   A 93  ? 0.1216 0.1386 0.1312 -0.0028 0.0005  0.0152  93  LEU   A O   
1955 C  CB  . LEU   A 93  ? 0.1350 0.1410 0.1488 -0.0047 -0.0067 0.0287  93  LEU   A CB  
1956 C  CG  . LEU   A 93  ? 0.1417 0.1426 0.1497 -0.0040 -0.0001 0.0243  93  LEU   A CG  
1957 C  CD1 . LEU   A 93  ? 0.1438 0.1494 0.1808 -0.0044 0.0126  0.0173  93  LEU   A CD1 
1958 C  CD2 . LEU   A 93  ? 0.1544 0.1346 0.1714 -0.0094 0.0018  0.0170  93  LEU   A CD2 
1970 N  N   . HIS   A 94  ? 0.1262 0.1261 0.1318 -0.0063 0.0004  0.0199  94  HIS   A N   
1971 C  CA  . HIS   A 94  ? 0.1228 0.1287 0.1306 -0.0061 -0.0017 0.0229  94  HIS   A CA  
1972 C  C   . HIS   A 94  ? 0.1179 0.1256 0.1346 -0.0060 0.0009  0.0118  94  HIS   A C   
1973 O  O   . HIS   A 94  ? 0.1213 0.1477 0.1780 -0.0012 0.0008  -0.0081 94  HIS   A O   
1974 C  CB  . HIS   A 94  ? 0.1192 0.1251 0.1408 -0.0064 -0.0036 0.0176  94  HIS   A CB  
1975 C  CG  . HIS   A 94  ? 0.1268 0.1228 0.1376 -0.0080 0.0020  0.0172  94  HIS   A CG  
1976 N  ND1 . HIS   A 94  ? 0.1242 0.1229 0.1502 -0.0075 0.0029  0.0212  94  HIS   A ND1 
1977 C  CD2 . HIS   A 94  ? 0.1335 0.1373 0.1442 -0.0128 -0.0049 0.0112  94  HIS   A CD2 
1978 C  CE1 . HIS   A 94  ? 0.1305 0.1270 0.1444 -0.0088 -0.0098 0.0105  94  HIS   A CE1 
1979 N  NE2 . HIS   A 94  ? 0.1383 0.1328 0.1501 -0.0137 -0.0105 0.0062  94  HIS   A NE2 
1987 N  N   . VAL   A 95  ? 0.1196 0.1214 0.1320 -0.0059 0.0093  0.0076  95  VAL   A N   
1988 C  CA  . VAL   A 95  ? 0.1251 0.1236 0.1292 -0.0081 0.0111  0.0108  95  VAL   A CA  
1989 C  C   . VAL   A 95  ? 0.1253 0.1194 0.1324 -0.0115 0.0042  0.0102  95  VAL   A C   
1990 O  O   . VAL   A 95  ? 0.1299 0.1326 0.1374 0.0065  0.0039  0.0087  95  VAL   A O   
1991 C  CB  . VAL   A 95  ? 0.1288 0.1272 0.1468 -0.0108 0.0074  0.0053  95  VAL   A CB  
1992 C  CG1 . VAL   A 95  ? 0.1405 0.1327 0.1615 -0.0187 0.0083  0.0002  95  VAL   A CG1 
1993 C  CG2 . VAL   A 95  ? 0.1326 0.1353 0.1510 -0.0131 0.0048  0.0230  95  VAL   A CG2 
2003 N  N   . VAL   A 96  ? 0.1291 0.1233 0.1223 -0.0042 0.0078  0.0125  96  VAL   A N   
2004 C  CA  . VAL   A 96  ? 0.1380 0.1245 0.1365 -0.0004 0.0094  0.0212  96  VAL   A CA  
2005 C  C   . VAL   A 96  ? 0.1389 0.1329 0.1369 -0.0035 0.0126  0.0214  96  VAL   A C   
2006 O  O   . VAL   A 96  ? 0.1480 0.1407 0.1613 -0.0040 0.0190  -0.0008 96  VAL   A O   
2007 C  CB  . VAL   A 96  ? 0.1375 0.1313 0.1367 -0.0065 0.0133  0.0146  96  VAL   A CB  
2008 C  CG1 . VAL   A 96  ? 0.1458 0.1432 0.1304 -0.0066 0.0132  0.0115  96  VAL   A CG1 
2009 C  CG2 . VAL   A 96  ? 0.1423 0.1405 0.1448 -0.0155 0.0139  0.0069  96  VAL   A CG2 
2019 N  N   . GLY   A 97  ? 0.1371 0.1395 0.1331 -0.0046 0.0085  0.0141  97  GLY   A N   
2020 C  CA  . GLY   A 97  ? 0.1471 0.1506 0.1315 -0.0046 0.0036  0.0142  97  GLY   A CA  
2021 C  C   . GLY   A 97  ? 0.1511 0.1615 0.1244 -0.0070 0.0006  0.0117  97  GLY   A C   
2022 O  O   . GLY   A 97  ? 0.1612 0.1565 0.1497 -0.0120 0.0039  0.0211  97  GLY   A O   
2026 N  N   A PRO   A 98  ? 0.1539 0.1676 0.1243 -0.0008 -0.0033 0.0113  98  PRO   A N   
2027 N  N   B PRO   A 98  ? 0.1580 0.1623 0.1268 -0.0033 0.0054  0.0195  98  PRO   A N   
2028 C  CA  A PRO   A 98  ? 0.1597 0.1877 0.1282 -0.0056 -0.0013 0.0044  98  PRO   A CA  
2029 C  CA  B PRO   A 98  ? 0.1673 0.1695 0.1367 -0.0049 0.0064  0.0144  98  PRO   A CA  
2030 C  C   A PRO   A 98  ? 0.1579 0.1934 0.1131 -0.0132 -0.0011 0.0107  98  PRO   A C   
2031 C  C   B PRO   A 98  ? 0.1845 0.1640 0.1267 -0.0099 0.0050  0.0212  98  PRO   A C   
2032 O  O   A PRO   A 98  ? 0.1517 0.1828 0.1307 -0.0077 0.0032  0.0068  98  PRO   A O   
2033 O  O   B PRO   A 98  ? 0.1807 0.1609 0.1543 -0.0035 0.0120  0.0164  98  PRO   A O   
2034 C  CB  A PRO   A 98  ? 0.1665 0.1942 0.1035 0.0094  -0.0089 -0.0055 98  PRO   A CB  
2035 C  CB  B PRO   A 98  ? 0.1656 0.1717 0.1383 0.0061  0.0059  0.0170  98  PRO   A CB  
2036 C  CG  A PRO   A 98  ? 0.1640 0.1846 0.1195 0.0109  -0.0119 -0.0096 98  PRO   A CG  
2037 C  CG  B PRO   A 98  ? 0.1691 0.1730 0.1449 0.0013  0.0051  0.0138  98  PRO   A CG  
2038 C  CD  A PRO   A 98  ? 0.1610 0.1691 0.1252 0.0039  -0.0036 -0.0029 98  PRO   A CD  
2039 C  CD  B PRO   A 98  ? 0.1613 0.1624 0.1314 -0.0012 0.0050  0.0183  98  PRO   A CD  
2054 N  N   A ASN   A 99  ? 0.1628 0.2110 0.1114 -0.0103 0.0118  0.0123  99  ASN   A N   
2055 N  N   B ASN   A 99  ? 0.2084 0.1616 0.1116 -0.0064 0.0019  0.0311  99  ASN   A N   
2056 C  CA  A ASN   A 99  ? 0.1801 0.2228 0.1046 -0.0120 0.0095  0.0216  99  ASN   A CA  
2057 C  CA  B ASN   A 99  ? 0.2351 0.1594 0.1093 0.0013  -0.0015 0.0415  99  ASN   A CA  
2058 C  C   A ASN   A 99  ? 0.1966 0.2472 0.1002 -0.0156 0.0147  0.0247  99  ASN   A C   
2059 C  C   B ASN   A 99  ? 0.2487 0.1641 0.1125 -0.0002 -0.0159 0.0495  99  ASN   A C   
2060 O  O   A ASN   A 99  ? 0.2054 0.2671 0.1191 -0.0078 0.0059  0.0168  99  ASN   A O   
2061 O  O   B ASN   A 99  ? 0.2479 0.1534 0.1141 0.0045  -0.0211 0.0349  99  ASN   A O   
2062 C  CB  A ASN   A 99  ? 0.1779 0.2165 0.1109 -0.0131 0.0052  0.0293  99  ASN   A CB  
2063 C  CB  B ASN   A 99  ? 0.2474 0.1559 0.1359 0.0071  -0.0021 0.0384  99  ASN   A CB  
2064 C  CG  A ASN   A 99  ? 0.1808 0.2111 0.1334 -0.0025 -0.0028 0.0244  99  ASN   A CG  
2065 C  CG  B ASN   A 99  ? 0.2578 0.1637 0.1581 0.0082  -0.0087 0.0414  99  ASN   A CG  
2066 O  OD1 A ASN   A 99  ? 0.1888 0.2225 0.1365 0.0094  -0.0057 0.0060  99  ASN   A OD1 
2067 O  OD1 B ASN   A 99  ? 0.2601 0.1695 0.1476 0.0093  -0.0221 0.0459  99  ASN   A OD1 
2068 N  ND2 A ASN   A 99  ? 0.1815 0.2060 0.1511 0.0036  -0.0106 0.0382  99  ASN   A ND2 
2069 N  ND2 B ASN   A 99  ? 0.2641 0.1709 0.1962 0.0160  -0.0162 0.0259  99  ASN   A ND2 
2082 N  N   A VAL   A 100 ? 0.2143 0.2521 0.1154 -0.0249 -0.0103 0.0178  100 VAL   A N   
2083 N  N   B VAL   A 100 ? 0.2616 0.1892 0.1392 0.0002  -0.0229 0.0493  100 VAL   A N   
2084 C  CA  A VAL   A 100 ? 0.2363 0.2649 0.1291 -0.0296 -0.0129 0.0233  100 VAL   A CA  
2085 C  CA  B VAL   A 100 ? 0.2773 0.2129 0.1833 0.0025  -0.0262 0.0370  100 VAL   A CA  
2086 C  C   A VAL   A 100 ? 0.2450 0.2819 0.1165 -0.0393 -0.0164 0.0454  100 VAL   A C   
2087 C  C   B VAL   A 100 ? 0.2779 0.2120 0.1933 0.0138  -0.0353 0.0249  100 VAL   A C   
2088 O  O   A VAL   A 100 ? 0.2516 0.2923 0.1348 -0.0357 0.0036  0.0411  100 VAL   A O   
2089 O  O   B VAL   A 100 ? 0.2778 0.2122 0.1936 0.0141  -0.0465 0.0114  100 VAL   A O   
2090 C  CB  A VAL   A 100 ? 0.2550 0.2617 0.1728 -0.0328 -0.0141 0.0111  100 VAL   A CB  
2091 C  CB  B VAL   A 100 ? 0.2909 0.2379 0.2369 -0.0019 -0.0156 0.0306  100 VAL   A CB  
2092 C  CG1 A VAL   A 100 ? 0.2597 0.2698 0.2079 -0.0362 -0.0085 0.0088  100 VAL   A CG1 
2093 C  CG1 B VAL   A 100 ? 0.2931 0.2461 0.2598 -0.0038 -0.0101 0.0258  100 VAL   A CG1 
2094 C  CG2 A VAL   A 100 ? 0.2638 0.2557 0.1792 -0.0406 -0.0153 0.0028  100 VAL   A CG2 
2095 C  CG2 B VAL   A 100 ? 0.2947 0.2458 0.2612 -0.0003 -0.0095 0.0299  100 VAL   A CG2 
2114 N  N   A ASN   A 101 ? 0.2490 0.2921 0.1383 -0.0488 -0.0189 0.0690  101 ASN   A N   
2115 N  N   B ASN   A 101 ? 0.2827 0.2153 0.1979 0.0190  -0.0373 0.0256  101 ASN   A N   
2116 C  CA  A ASN   A 101 ? 0.2697 0.3047 0.1535 -0.0530 -0.0235 0.0940  101 ASN   A CA  
2117 C  CA  B ASN   A 101 ? 0.2919 0.2261 0.2133 0.0261  -0.0325 0.0322  101 ASN   A CA  
2118 C  C   A ASN   A 101 ? 0.3002 0.3407 0.1766 -0.0613 -0.0003 0.1214  101 ASN   A C   
2119 C  C   B ASN   A 101 ? 0.3070 0.2454 0.2206 0.0240  -0.0249 0.0540  101 ASN   A C   
2120 O  O   A ASN   A 101 ? 0.3147 0.3485 0.2279 -0.0621 -0.0014 0.1071  101 ASN   A O   
2121 O  O   B ASN   A 101 ? 0.3138 0.2492 0.2188 0.0229  -0.0323 0.0731  101 ASN   A O   
2122 C  CB  A ASN   A 101 ? 0.2633 0.2808 0.1536 -0.0482 -0.0409 0.0830  101 ASN   A CB  
2123 C  CB  B ASN   A 101 ? 0.2859 0.2201 0.2188 0.0288  -0.0309 0.0259  101 ASN   A CB  
2124 C  CG  A ASN   A 101 ? 0.2582 0.2597 0.1636 -0.0440 -0.0404 0.0466  101 ASN   A CG  
2125 C  CG  B ASN   A 101 ? 0.2843 0.2257 0.2355 0.0263  -0.0312 0.0206  101 ASN   A CG  
2126 O  OD1 A ASN   A 101 ? 0.2474 0.2491 0.1620 -0.0311 -0.0232 0.0168  101 ASN   A OD1 
2127 O  OD1 B ASN   A 101 ? 0.2904 0.2337 0.2612 0.0185  -0.0274 0.0289  101 ASN   A OD1 
2128 N  ND2 A ASN   A 101 ? 0.2618 0.2525 0.1778 -0.0549 -0.0400 0.0382  101 ASN   A ND2 
2129 N  ND2 B ASN   A 101 ? 0.2808 0.2218 0.2428 0.0293  -0.0273 0.0044  101 ASN   A ND2 
2142 N  N   A LYS   A 102 ? 0.3097 0.3674 0.2153 -0.0694 0.0105  0.1209  102 LYS   A N   
2143 N  N   B LYS   A 102 ? 0.3136 0.2644 0.2524 0.0222  -0.0095 0.0513  102 LYS   A N   
2144 C  CA  A LYS   A 102 ? 0.3260 0.3934 0.2411 -0.0726 0.0023  0.1073  102 LYS   A CA  
2145 C  CA  B LYS   A 102 ? 0.3206 0.2849 0.2581 0.0163  0.0009  0.0513  102 LYS   A CA  
2146 C  C   A LYS   A 102 ? 0.3356 0.4158 0.2396 -0.0601 0.0015  0.0955  102 LYS   A C   
2147 C  C   B LYS   A 102 ? 0.3221 0.2902 0.2413 0.0214  -0.0028 0.0688  102 LYS   A C   
2148 O  O   A LYS   A 102 ? 0.3368 0.4252 0.2516 -0.0561 0.0068  0.0918  102 LYS   A O   
2149 O  O   B LYS   A 102 ? 0.3259 0.2883 0.2390 0.0242  0.0025  0.0794  102 LYS   A O   
2150 C  CB  A LYS   A 102 ? 0.3387 0.3985 0.2893 -0.0829 -0.0144 0.0873  102 LYS   A CB  
2151 C  CB  B LYS   A 102 ? 0.3264 0.2992 0.2913 0.0092  0.0047  0.0355  102 LYS   A CB  
2152 C  CG  A LYS   A 102 ? 0.3510 0.4021 0.3260 -0.0919 -0.0301 0.0697  102 LYS   A CG  
2153 C  CG  B LYS   A 102 ? 0.3315 0.3117 0.3180 0.0016  0.0076  0.0209  102 LYS   A CG  
2154 C  CD  A LYS   A 102 ? 0.3652 0.4069 0.3654 -0.0961 -0.0402 0.0481  102 LYS   A CD  
2155 C  CD  B LYS   A 102 ? 0.3383 0.3257 0.3502 -0.0045 0.0091  0.0077  102 LYS   A CD  
2156 C  CE  A LYS   A 102 ? 0.3762 0.4084 0.3999 -0.0986 -0.0479 0.0360  102 LYS   A CE  
2157 C  CE  B LYS   A 102 ? 0.3445 0.3365 0.3742 -0.0089 0.0066  0.0014  102 LYS   A CE  
2158 N  NZ  A LYS   A 102 ? 0.3804 0.4070 0.4146 -0.1036 -0.0531 0.0285  102 LYS   A NZ  
2159 N  NZ  B LYS   A 102 ? 0.3487 0.3438 0.3921 -0.0110 0.0048  -0.0035 102 LYS   A NZ  
2186 N  N   A GLY   A 103 ? 0.3418 0.4280 0.2536 -0.0491 -0.0040 0.0760  103 GLY   A N   
2187 N  N   B GLY   A 103 ? 0.3192 0.3003 0.2289 0.0243  -0.0128 0.0647  103 GLY   A N   
2188 C  CA  A GLY   A 103 ? 0.3470 0.4365 0.2534 -0.0367 0.0001  0.0592  103 GLY   A CA  
2189 C  CA  B GLY   A 103 ? 0.3145 0.3048 0.2271 0.0264  -0.0203 0.0698  103 GLY   A CA  
2190 C  C   A GLY   A 103 ? 0.3458 0.4438 0.2598 -0.0288 0.0091  0.0492  103 GLY   A C   
2191 C  C   B GLY   A 103 ? 0.3042 0.3057 0.2092 0.0266  -0.0249 0.0664  103 GLY   A C   
2192 O  O   A GLY   A 103 ? 0.3558 0.4507 0.2819 -0.0200 0.0065  0.0415  103 GLY   A O   
2193 O  O   B GLY   A 103 ? 0.3132 0.3101 0.2042 0.0283  -0.0295 0.0700  103 GLY   A O   
2200 N  N   A GLU   A 104 ? 0.3295 0.4399 0.2238 -0.0350 0.0260  0.0472  104 GLU   A N   
2201 N  N   B GLU   A 104 ? 0.2821 0.2990 0.1878 0.0231  -0.0323 0.0644  104 GLU   A N   
2202 C  CA  A GLU   A 104 ? 0.3107 0.4326 0.2019 -0.0448 0.0372  0.0431  104 GLU   A CA  
2203 C  CA  B GLU   A 104 ? 0.2639 0.2920 0.1635 0.0163  -0.0379 0.0538  104 GLU   A CA  
2204 C  C   A GLU   A 104 ? 0.3125 0.4406 0.2033 -0.0454 0.0314  0.0166  104 GLU   A C   
2205 C  C   B GLU   A 104 ? 0.2635 0.2887 0.1734 0.0245  -0.0302 0.0371  104 GLU   A C   
2206 O  O   A GLU   A 104 ? 0.3077 0.4438 0.2113 -0.0477 0.0078  0.0130  104 GLU   A O   
2207 O  O   B GLU   A 104 ? 0.2621 0.2816 0.1960 0.0237  -0.0301 0.0380  104 GLU   A O   
2208 C  CB  A GLU   A 104 ? 0.2850 0.4163 0.1882 -0.0555 0.0516  0.0689  104 GLU   A CB  
2209 C  CB  B GLU   A 104 ? 0.2528 0.2901 0.1579 0.0003  -0.0416 0.0601  104 GLU   A CB  
2210 C  CG  A GLU   A 104 ? 0.2662 0.4003 0.1905 -0.0598 0.0506  0.0854  104 GLU   A CG  
2211 C  CG  B GLU   A 104 ? 0.2465 0.2937 0.1714 -0.0115 -0.0498 0.0618  104 GLU   A CG  
2212 C  CD  A GLU   A 104 ? 0.2503 0.3838 0.1928 -0.0610 0.0525  0.0974  104 GLU   A CD  
2213 C  CD  B GLU   A 104 ? 0.2373 0.2936 0.1791 -0.0182 -0.0638 0.0663  104 GLU   A CD  
2214 O  OE1 A GLU   A 104 ? 0.2339 0.3616 0.1759 -0.0583 0.0462  0.0951  104 GLU   A OE1 
2215 O  OE1 B GLU   A 104 ? 0.2303 0.2911 0.1747 -0.0182 -0.0720 0.0686  104 GLU   A OE1 
2216 O  OE2 A GLU   A 104 ? 0.2614 0.3865 0.2158 -0.0641 0.0493  0.1109  104 GLU   A OE2 
2217 O  OE2 B GLU   A 104 ? 0.2433 0.2961 0.2054 -0.0237 -0.0560 0.0653  104 GLU   A OE2 
2230 N  N   A ASP   A 105 ? 0.3197 0.4442 0.2041 -0.0427 0.0447  -0.0153 105 ASP   A N   
2231 N  N   B ASP   A 105 ? 0.2748 0.2959 0.1968 0.0253  -0.0176 0.0164  105 ASP   A N   
2232 C  CA  A ASP   A 105 ? 0.3210 0.4476 0.2445 -0.0379 0.0495  -0.0445 105 ASP   A CA  
2233 C  CA  B ASP   A 105 ? 0.2841 0.3051 0.2296 0.0259  -0.0048 -0.0140 105 ASP   A CA  
2234 C  C   A ASP   A 105 ? 0.2878 0.4322 0.2045 -0.0526 0.0421  -0.0643 105 ASP   A C   
2235 C  C   B ASP   A 105 ? 0.2849 0.3069 0.2155 0.0100  -0.0032 -0.0240 105 ASP   A C   
2236 O  O   A ASP   A 105 ? 0.2748 0.4303 0.1611 -0.0558 0.0419  -0.0881 105 ASP   A O   
2237 O  O   B ASP   A 105 ? 0.2767 0.3011 0.1713 0.0115  -0.0022 -0.0350 105 ASP   A O   
2238 C  CB  A ASP   A 105 ? 0.3503 0.4644 0.3186 -0.0216 0.0545  -0.0512 105 ASP   A CB  
2239 C  CB  B ASP   A 105 ? 0.2908 0.3135 0.2780 0.0396  0.0072  -0.0328 105 ASP   A CB  
2240 C  CG  A ASP   A 105 ? 0.3741 0.4791 0.3840 -0.0102 0.0521  -0.0588 105 ASP   A CG  
2241 C  CG  B ASP   A 105 ? 0.2958 0.3200 0.3228 0.0519  0.0157  -0.0482 105 ASP   A CG  
2242 O  OD1 A ASP   A 105 ? 0.3796 0.4853 0.3987 -0.0066 0.0501  -0.0686 105 ASP   A OD1 
2243 O  OD1 B ASP   A 105 ? 0.2967 0.3209 0.3270 0.0525  0.0139  -0.0553 105 ASP   A OD1 
2244 O  OD2 A ASP   A 105 ? 0.3865 0.4847 0.4239 -0.0075 0.0507  -0.0535 105 ASP   A OD2 
2245 O  OD2 B ASP   A 105 ? 0.2999 0.3245 0.3492 0.0573  0.0212  -0.0485 105 ASP   A OD2 
2254 N  N   A ILE   A 106 ? 0.2682 0.4155 0.2173 -0.0648 0.0180  -0.0607 106 ILE   A N   
2255 N  N   B ILE   A 106 ? 0.2920 0.3146 0.2414 -0.0064 -0.0051 -0.0232 106 ILE   A N   
2256 C  CA  A ILE   A 106 ? 0.2422 0.3924 0.2291 -0.0796 -0.0085 -0.0722 106 ILE   A CA  
2257 C  CA  B ILE   A 106 ? 0.2964 0.3222 0.2678 -0.0263 -0.0093 -0.0278 106 ILE   A CA  
2258 C  C   A ILE   A 106 ? 0.2294 0.3631 0.2366 -0.0982 -0.0069 -0.0940 106 ILE   A C   
2259 C  C   B ILE   A 106 ? 0.2947 0.3168 0.2746 -0.0371 -0.0004 -0.0335 106 ILE   A C   
2260 O  O   A ILE   A 106 ? 0.2101 0.3476 0.2352 -0.1048 0.0167  -0.0989 106 ILE   A O   
2261 O  O   B ILE   A 106 ? 0.2899 0.3145 0.2695 -0.0380 0.0045  -0.0347 106 ILE   A O   
2262 C  CB  A ILE   A 106 ? 0.2399 0.4008 0.2673 -0.0657 -0.0288 -0.0436 106 ILE   A CB  
2263 C  CB  B ILE   A 106 ? 0.3042 0.3360 0.3006 -0.0328 -0.0189 -0.0179 106 ILE   A CB  
2264 C  CG1 A ILE   A 106 ? 0.2256 0.3989 0.2932 -0.0530 -0.0337 -0.0209 106 ILE   A CG1 
2265 C  CG1 B ILE   A 106 ? 0.3049 0.3403 0.3234 -0.0357 -0.0232 -0.0084 106 ILE   A CG1 
2266 C  CG2 A ILE   A 106 ? 0.2504 0.4061 0.2831 -0.0632 -0.0371 -0.0404 106 ILE   A CG2 
2267 C  CG2 B ILE   A 106 ? 0.3091 0.3407 0.3072 -0.0341 -0.0219 -0.0172 106 ILE   A CG2 
2268 C  CD1 A ILE   A 106 ? 0.2206 0.3959 0.3051 -0.0385 -0.0294 -0.0095 106 ILE   A CD1 
2269 C  CD1 B ILE   A 106 ? 0.3061 0.3401 0.3338 -0.0360 -0.0244 -0.0033 106 ILE   A CD1 
2292 N  N   A GLN   A 107 ? 0.2495 0.3495 0.2706 -0.0945 0.0008  -0.1033 107 GLN   A N   
2293 N  N   B GLN   A 107 ? 0.2982 0.3110 0.2908 -0.0437 0.0098  -0.0384 107 GLN   A N   
2294 C  CA  A GLN   A 107 ? 0.2782 0.3356 0.3449 -0.0783 0.0209  -0.0940 107 GLN   A CA  
2295 C  CA  B GLN   A 107 ? 0.3028 0.3068 0.3310 -0.0484 0.0202  -0.0408 107 GLN   A CA  
2296 C  C   A GLN   A 107 ? 0.2553 0.2869 0.3243 -0.0659 0.0496  -0.0728 107 GLN   A C   
2297 C  C   B GLN   A 107 ? 0.2700 0.2741 0.3066 -0.0537 0.0408  -0.0471 107 GLN   A C   
2298 O  O   A GLN   A 107 ? 0.2594 0.2830 0.3753 -0.0600 0.0624  -0.0754 107 GLN   A O   
2299 O  O   B GLN   A 107 ? 0.2758 0.2728 0.3335 -0.0546 0.0428  -0.0500 107 GLN   A O   
2300 C  CB  A GLN   A 107 ? 0.3225 0.3670 0.4421 -0.0780 0.0084  -0.0934 107 GLN   A CB  
2301 C  CB  B GLN   A 107 ? 0.3355 0.3329 0.3955 -0.0506 0.0068  -0.0326 107 GLN   A CB  
2302 C  CG  A GLN   A 107 ? 0.3663 0.3972 0.5439 -0.0729 -0.0028 -0.0831 107 GLN   A CG  
2303 C  CG  B GLN   A 107 ? 0.3644 0.3560 0.4630 -0.0507 -0.0059 -0.0206 107 GLN   A CG  
2304 C  CD  A GLN   A 107 ? 0.4036 0.4193 0.6306 -0.0686 -0.0113 -0.0699 107 GLN   A CD  
2305 C  CD  B GLN   A 107 ? 0.3885 0.3755 0.5233 -0.0493 -0.0164 -0.0088 107 GLN   A CD  
2306 O  OE1 A GLN   A 107 ? 0.4158 0.4278 0.6654 -0.0678 -0.0137 -0.0652 107 GLN   A OE1 
2307 O  OE1 B GLN   A 107 ? 0.3987 0.3834 0.5407 -0.0483 -0.0200 -0.0036 107 GLN   A OE1 
2308 N  NE2 A GLN   A 107 ? 0.4115 0.4265 0.6590 -0.0665 -0.0152 -0.0679 107 GLN   A NE2 
2309 N  NE2 B GLN   A 107 ? 0.3949 0.3811 0.5427 -0.0489 -0.0228 -0.0055 107 GLN   A NE2 
2326 N  N   . LEU   A 108 ? 0.2314 0.2451 0.2647 -0.0578 0.0493  -0.0564 108 LEU   A N   
2327 C  CA  . LEU   A 108 ? 0.1986 0.1988 0.2291 -0.0269 0.0455  -0.0223 108 LEU   A CA  
2328 C  C   . LEU   A 108 ? 0.1750 0.1565 0.2148 -0.0105 0.0373  0.0003  108 LEU   A C   
2329 O  O   . LEU   A 108 ? 0.1683 0.1592 0.2268 0.0005  0.0388  0.0080  108 LEU   A O   
2330 C  CB  . LEU   A 108 ? 0.2000 0.2099 0.2172 -0.0271 0.0443  -0.0240 108 LEU   A CB  
2331 C  CG  . LEU   A 108 ? 0.2134 0.2350 0.2436 -0.0233 0.0532  -0.0264 108 LEU   A CG  
2332 C  CD1 . LEU   A 108 ? 0.2283 0.2378 0.2426 -0.0309 0.0575  -0.0187 108 LEU   A CD1 
2333 C  CD2 . LEU   A 108 ? 0.2185 0.2561 0.2952 -0.0168 0.0495  -0.0221 108 LEU   A CD2 
2346 N  N   . LEU   A 109 ? 0.1604 0.1544 0.2072 -0.0004 0.0320  0.0075  109 LEU   A N   
2347 C  CA  . LEU   A 109 ? 0.1540 0.1481 0.1891 0.0025  0.0158  0.0134  109 LEU   A CA  
2348 C  C   . LEU   A 109 ? 0.1449 0.1412 0.1898 -0.0065 0.0152  0.0098  109 LEU   A C   
2349 O  O   . LEU   A 109 ? 0.1494 0.1331 0.2091 -0.0038 0.0028  0.0064  109 LEU   A O   
2350 C  CB  . LEU   A 109 ? 0.1651 0.1563 0.2088 0.0105  0.0130  0.0315  109 LEU   A CB  
2351 C  CG  . LEU   A 109 ? 0.1554 0.1624 0.2171 0.0072  0.0166  0.0377  109 LEU   A CG  
2352 C  CD1 . LEU   A 109 ? 0.1603 0.1571 0.2237 0.0042  0.0170  0.0194  109 LEU   A CD1 
2353 C  CD2 . LEU   A 109 ? 0.1502 0.1866 0.2351 0.0030  0.0111  0.0377  109 LEU   A CD2 
2365 N  N   . LYS   A 110 ? 0.1463 0.1419 0.1764 -0.0061 0.0013  -0.0002 110 LYS   A N   
2366 C  CA  . LYS   A 110 ? 0.1426 0.1319 0.1975 -0.0065 0.0006  0.0103  110 LYS   A CA  
2367 C  C   . LYS   A 110 ? 0.1456 0.1296 0.1882 -0.0070 0.0098  0.0016  110 LYS   A C   
2368 O  O   . LYS   A 110 ? 0.1393 0.1304 0.1972 -0.0062 0.0103  -0.0012 110 LYS   A O   
2369 C  CB  . LYS   A 110 ? 0.1492 0.1391 0.2244 -0.0061 -0.0052 -0.0010 110 LYS   A CB  
2370 C  CG  . LYS   A 110 ? 0.1461 0.1376 0.2308 -0.0019 -0.0013 -0.0016 110 LYS   A CG  
2371 C  CD  . LYS   A 110 ? 0.1532 0.1436 0.2440 -0.0115 -0.0001 -0.0095 110 LYS   A CD  
2372 C  CE  . LYS   A 110 ? 0.1609 0.1470 0.2563 -0.0092 0.0169  -0.0151 110 LYS   A CE  
2373 N  NZ  . LYS   A 110 ? 0.1642 0.1487 0.2709 -0.0146 0.0182  -0.0080 110 LYS   A NZ  
2387 N  N   . SER   A 111 ? 0.1437 0.1344 0.1866 -0.0016 0.0037  0.0029  111 SER   A N   
2388 C  CA  . SER   A 111 ? 0.1372 0.1419 0.1826 -0.0071 0.0104  -0.0021 111 SER   A CA  
2389 C  C   . SER   A 111 ? 0.1316 0.1306 0.1833 -0.0098 0.0118  0.0059  111 SER   A C   
2390 O  O   . SER   A 111 ? 0.1442 0.1284 0.1989 -0.0048 0.0120  0.0062  111 SER   A O   
2391 C  CB  . SER   A 111 ? 0.1585 0.1610 0.2021 -0.0042 0.0138  -0.0088 111 SER   A CB  
2392 O  OG  . SER   A 111 ? 0.2001 0.1773 0.2086 0.0038  0.0265  -0.0244 111 SER   A OG  
2398 N  N   . ALA   A 112 ? 0.1372 0.1289 0.1857 -0.0032 0.0163  0.0097  112 ALA   A N   
2399 C  CA  . ALA   A 112 ? 0.1408 0.1228 0.1763 -0.0061 0.0256  0.0014  112 ALA   A CA  
2400 C  C   . ALA   A 112 ? 0.1322 0.1234 0.1899 -0.0013 0.0165  0.0006  112 ALA   A C   
2401 O  O   . ALA   A 112 ? 0.1359 0.1210 0.1976 -0.0116 0.0191  0.0108  112 ALA   A O   
2402 C  CB  . ALA   A 112 ? 0.1507 0.1255 0.1853 -0.0054 0.0193  0.0042  112 ALA   A CB  
2408 N  N   . TYR   A 113 ? 0.1252 0.1285 0.1945 -0.0028 0.0128  0.0143  113 TYR   A N   
2409 C  CA  . TYR   A 113 ? 0.1254 0.1243 0.1865 -0.0043 0.0175  0.0135  113 TYR   A CA  
2410 C  C   . TYR   A 113 ? 0.1199 0.1247 0.1821 -0.0142 0.0095  0.0083  113 TYR   A C   
2411 O  O   . TYR   A 113 ? 0.1315 0.1271 0.1914 -0.0068 0.0177  0.0085  113 TYR   A O   
2412 C  CB  . TYR   A 113 ? 0.1258 0.1327 0.1871 -0.0068 0.0063  0.0166  113 TYR   A CB  
2413 C  CG  . TYR   A 113 ? 0.1279 0.1387 0.1704 -0.0104 0.0124  0.0169  113 TYR   A CG  
2414 C  CD1 . TYR   A 113 ? 0.1337 0.1477 0.1692 -0.0028 0.0091  0.0281  113 TYR   A CD1 
2415 C  CD2 . TYR   A 113 ? 0.1345 0.1397 0.1721 -0.0113 0.0100  0.0134  113 TYR   A CD2 
2416 C  CE1 . TYR   A 113 ? 0.1383 0.1553 0.1733 -0.0036 0.0105  0.0260  113 TYR   A CE1 
2417 C  CE2 . TYR   A 113 ? 0.1345 0.1469 0.1736 -0.0110 0.0053  0.0235  113 TYR   A CE2 
2418 C  CZ  . TYR   A 113 ? 0.1373 0.1510 0.1744 0.0041  0.0126  0.0267  113 TYR   A CZ  
2419 O  OH  . TYR   A 113 ? 0.1376 0.1599 0.1945 0.0105  0.0083  0.0228  113 TYR   A OH  
2429 N  N   . GLU   A 114 ? 0.1286 0.1211 0.1887 -0.0094 0.0151  0.0111  114 GLU   A N   
2430 C  CA  . GLU   A 114 ? 0.1340 0.1166 0.1984 0.0013  0.0112  0.0178  114 GLU   A CA  
2431 C  C   . GLU   A 114 ? 0.1265 0.1252 0.1952 -0.0012 0.0150  0.0107  114 GLU   A C   
2432 O  O   . GLU   A 114 ? 0.1357 0.1252 0.1906 -0.0010 0.0071  0.0150  114 GLU   A O   
2433 C  CB  . GLU   A 114 ? 0.1327 0.1191 0.1995 -0.0059 0.0137  0.0143  114 GLU   A CB  
2434 C  CG  . GLU   A 114 ? 0.1376 0.1239 0.2048 0.0011  0.0149  0.0092  114 GLU   A CG  
2435 C  CD  . GLU   A 114 ? 0.1426 0.1247 0.2121 -0.0068 0.0057  0.0019  114 GLU   A CD  
2436 O  OE1 . GLU   A 114 ? 0.1469 0.1302 0.2151 -0.0102 0.0118  -0.0096 114 GLU   A OE1 
2437 O  OE2 . GLU   A 114 ? 0.1615 0.1368 0.2297 -0.0087 0.0118  -0.0136 114 GLU   A OE2 
2444 N  N   . ASN   A 115 ? 0.1298 0.1282 0.1827 -0.0093 0.0158  0.0085  115 ASN   A N   
2445 C  CA  . ASN   A 115 ? 0.1303 0.1307 0.1871 -0.0084 0.0161  0.0108  115 ASN   A CA  
2446 C  C   . ASN   A 115 ? 0.1367 0.1279 0.1849 -0.0128 0.0055  0.0066  115 ASN   A C   
2447 O  O   . ASN   A 115 ? 0.1340 0.1354 0.1943 -0.0101 0.0158  0.0173  115 ASN   A O   
2448 C  CB  . ASN   A 115 ? 0.1419 0.1385 0.1798 -0.0151 0.0090  0.0103  115 ASN   A CB  
2449 C  CG  . ASN   A 115 ? 0.1387 0.1544 0.1843 -0.0198 0.0240  0.0111  115 ASN   A CG  
2450 O  OD1 . ASN   A 115 ? 0.1452 0.2443 0.2163 -0.0183 0.0284  0.0197  115 ASN   A OD1 
2451 N  ND2 . ASN   A 115 ? 0.1400 0.1369 0.1788 -0.0142 0.0297  0.0161  115 ASN   A ND2 
2458 N  N   . PHE   A 116 ? 0.1287 0.1322 0.1825 -0.0048 0.0126  0.0233  116 PHE   A N   
2459 C  CA  . PHE   A 116 ? 0.1289 0.1368 0.1755 -0.0060 0.0185  0.0186  116 PHE   A CA  
2460 C  C   . PHE   A 116 ? 0.1297 0.1424 0.1804 -0.0077 0.0184  0.0266  116 PHE   A C   
2461 O  O   . PHE   A 116 ? 0.1342 0.1476 0.1905 -0.0009 0.0150  0.0373  116 PHE   A O   
2462 C  CB  . PHE   A 116 ? 0.1325 0.1312 0.1904 -0.0050 0.0184  0.0228  116 PHE   A CB  
2463 C  CG  . PHE   A 116 ? 0.1319 0.1312 0.1732 -0.0061 0.0117  0.0195  116 PHE   A CG  
2464 C  CD1 . PHE   A 116 ? 0.1356 0.1298 0.1676 -0.0073 0.0090  0.0146  116 PHE   A CD1 
2465 C  CD2 . PHE   A 116 ? 0.1365 0.1392 0.1929 -0.0055 0.0169  0.0201  116 PHE   A CD2 
2466 C  CE1 . PHE   A 116 ? 0.1400 0.1305 0.1848 -0.0171 0.0035  0.0093  116 PHE   A CE1 
2467 C  CE2 . PHE   A 116 ? 0.1380 0.1349 0.1964 -0.0036 0.0114  0.0131  116 PHE   A CE2 
2468 C  CZ  . PHE   A 116 ? 0.1416 0.1195 0.1846 -0.0041 0.0020  0.0099  116 PHE   A CZ  
2478 N  N   . ASN   A 117 ? 0.1334 0.1333 0.2001 -0.0048 0.0151  0.0285  117 ASN   A N   
2479 C  CA  . ASN   A 117 ? 0.1322 0.1373 0.2068 -0.0058 0.0142  0.0222  117 ASN   A CA  
2480 C  C   . ASN   A 117 ? 0.1358 0.1451 0.2188 -0.0005 0.0164  0.0272  117 ASN   A C   
2481 O  O   . ASN   A 117 ? 0.1432 0.1522 0.2327 -0.0054 -0.0070 0.0403  117 ASN   A O   
2482 C  CB  . ASN   A 117 ? 0.1368 0.1380 0.1999 -0.0009 0.0139  0.0274  117 ASN   A CB  
2483 C  CG  . ASN   A 117 ? 0.1355 0.1410 0.2049 -0.0020 0.0144  0.0337  117 ASN   A CG  
2484 O  OD1 . ASN   A 117 ? 0.1366 0.1602 0.2147 -0.0124 0.0147  0.0280  117 ASN   A OD1 
2485 N  ND2 . ASN   A 117 ? 0.1285 0.1366 0.2079 -0.0019 0.0103  0.0349  117 ASN   A ND2 
2492 N  N   . GLN   A 118 ? 0.1325 0.1429 0.2128 -0.0080 -0.0026 0.0344  118 GLN   A N   
2493 C  CA  . GLN   A 118 ? 0.1409 0.1554 0.2223 -0.0086 0.0014  0.0280  118 GLN   A CA  
2494 C  C   . GLN   A 118 ? 0.1423 0.1632 0.2040 -0.0130 -0.0028 0.0380  118 GLN   A C   
2495 O  O   . GLN   A 118 ? 0.1363 0.1915 0.2314 -0.0047 -0.0081 0.0144  118 GLN   A O   
2496 C  CB  . GLN   A 118 ? 0.1370 0.1554 0.2312 -0.0055 0.0111  0.0283  118 GLN   A CB  
2497 C  CG  . GLN   A 118 ? 0.1371 0.1569 0.2272 -0.0093 0.0092  0.0351  118 GLN   A CG  
2498 C  CD  . GLN   A 118 ? 0.1335 0.1604 0.2415 -0.0035 0.0122  0.0278  118 GLN   A CD  
2499 O  OE1 . GLN   A 118 ? 0.1382 0.1719 0.2606 0.0044  0.0022  0.0210  118 GLN   A OE1 
2500 N  NE2 . GLN   A 118 ? 0.1423 0.1580 0.2358 0.0009  0.0066  0.0277  118 GLN   A NE2 
2509 N  N   . HIS   A 119 ? 0.1458 0.1615 0.1991 -0.0054 0.0012  0.0382  119 HIS   A N   
2510 C  CA  . HIS   A 119 ? 0.1492 0.1675 0.2020 -0.0078 0.0004  0.0397  119 HIS   A CA  
2511 C  C   . HIS   A 119 ? 0.1596 0.1792 0.1908 -0.0090 0.0010  0.0467  119 HIS   A C   
2512 O  O   . HIS   A 119 ? 0.1629 0.1856 0.1869 -0.0262 -0.0066 0.0455  119 HIS   A O   
2513 C  CB  . HIS   A 119 ? 0.1574 0.1609 0.2198 -0.0079 0.0145  0.0414  119 HIS   A CB  
2514 C  CG  . HIS   A 119 ? 0.1588 0.1657 0.2452 -0.0036 0.0084  0.0480  119 HIS   A CG  
2515 N  ND1 . HIS   A 119 ? 0.1700 0.1847 0.3054 -0.0141 0.0116  0.0332  119 HIS   A ND1 
2516 C  CD2 . HIS   A 119 ? 0.1681 0.1761 0.2642 0.0071  0.0267  0.0610  119 HIS   A CD2 
2517 C  CE1 . HIS   A 119 ? 0.1695 0.1823 0.3154 -0.0173 0.0190  0.0529  119 HIS   A CE1 
2518 N  NE2 . HIS   A 119 ? 0.1788 0.1820 0.3031 -0.0002 0.0366  0.0638  119 HIS   A NE2 
2526 N  N   . GLU   A 120 ? 0.1637 0.2028 0.2020 -0.0096 -0.0075 0.0778  120 GLU   A N   
2527 C  CA  . GLU   A 120 ? 0.1876 0.2324 0.2347 -0.0026 -0.0090 0.1130  120 GLU   A CA  
2528 C  C   . GLU   A 120 ? 0.1696 0.2198 0.2008 -0.0155 -0.0061 0.1007  120 GLU   A C   
2529 O  O   . GLU   A 120 ? 0.1699 0.2130 0.2150 -0.0208 -0.0109 0.0940  120 GLU   A O   
2530 C  CB  . GLU   A 120 ? 0.2573 0.2928 0.2862 0.0109  -0.0028 0.1607  120 GLU   A CB  
2531 C  CG  . GLU   A 120 ? 0.3481 0.3670 0.3952 0.0276  -0.0044 0.1627  120 GLU   A CG  
2532 C  CD  . GLU   A 120 ? 0.4355 0.4336 0.5118 0.0390  0.0049  0.1465  120 GLU   A CD  
2533 O  OE1 . GLU   A 120 ? 0.4599 0.4455 0.5359 0.0420  0.0088  0.1421  120 GLU   A OE1 
2534 O  OE2 . GLU   A 120 ? 0.4756 0.4690 0.5592 0.0416  0.0079  0.1377  120 GLU   A OE2 
2541 N  N   . VAL   A 121 ? 0.1663 0.2213 0.1811 -0.0154 0.0007  0.0768  121 VAL   A N   
2542 C  CA  . VAL   A 121 ? 0.1711 0.2275 0.1682 -0.0193 0.0167  0.0808  121 VAL   A CA  
2543 C  C   . VAL   A 121 ? 0.1603 0.2088 0.1512 -0.0246 0.0091  0.0577  121 VAL   A C   
2544 O  O   . VAL   A 121 ? 0.1657 0.2058 0.1644 -0.0307 -0.0116 0.0522  121 VAL   A O   
2545 C  CB  . VAL   A 121 ? 0.2098 0.2654 0.2063 -0.0084 0.0239  0.0859  121 VAL   A CB  
2546 C  CG1 . VAL   A 121 ? 0.2157 0.2789 0.2059 -0.0032 0.0401  0.0878  121 VAL   A CG1 
2547 C  CG2 . VAL   A 121 ? 0.2284 0.2812 0.2384 -0.0166 0.0255  0.0759  121 VAL   A CG2 
2557 N  N   . LEU   A 122 ? 0.1516 0.1818 0.1570 -0.0237 0.0056  0.0471  122 LEU   A N   
2558 C  CA  . LEU   A 122 ? 0.1587 0.1655 0.1506 -0.0210 0.0142  0.0450  122 LEU   A CA  
2559 C  C   . LEU   A 122 ? 0.1540 0.1664 0.1548 -0.0258 0.0001  0.0400  122 LEU   A C   
2560 O  O   . LEU   A 122 ? 0.1522 0.1743 0.1856 -0.0327 0.0022  0.0405  122 LEU   A O   
2561 C  CB  . LEU   A 122 ? 0.1734 0.1707 0.1794 -0.0093 0.0057  0.0458  122 LEU   A CB  
2562 C  CG  . LEU   A 122 ? 0.1708 0.1738 0.1821 -0.0122 0.0120  0.0402  122 LEU   A CG  
2563 C  CD1 . LEU   A 122 ? 0.1889 0.1752 0.1986 -0.0218 0.0210  0.0481  122 LEU   A CD1 
2564 C  CD2 . LEU   A 122 ? 0.1661 0.1712 0.1753 -0.0097 0.0262  0.0354  122 LEU   A CD2 
2576 N  N   . LEU   A 123 ? 0.1464 0.1661 0.1436 -0.0249 0.0020  0.0326  123 LEU   A N   
2577 C  CA  . LEU   A 123 ? 0.1456 0.1646 0.1388 -0.0213 0.0078  0.0311  123 LEU   A CA  
2578 C  C   . LEU   A 123 ? 0.1432 0.1569 0.1302 -0.0185 0.0076  0.0389  123 LEU   A C   
2579 O  O   . LEU   A 123 ? 0.1375 0.1715 0.1513 -0.0277 -0.0015 0.0343  123 LEU   A O   
2580 C  CB  . LEU   A 123 ? 0.1580 0.1776 0.1339 -0.0283 0.0113  0.0320  123 LEU   A CB  
2581 C  CG  . LEU   A 123 ? 0.1634 0.1953 0.1401 -0.0181 0.0099  0.0154  123 LEU   A CG  
2582 C  CD1 . LEU   A 123 ? 0.1632 0.2035 0.1555 -0.0110 0.0142  0.0123  123 LEU   A CD1 
2583 C  CD2 . LEU   A 123 ? 0.1706 0.2013 0.1638 -0.0171 0.0070  0.0067  123 LEU   A CD2 
2595 N  N   A ALA   A 124 ? 0.1393 0.1434 0.1278 -0.0172 0.0082  0.0291  124 ALA   A N   
2596 N  N   B ALA   A 124 ? 0.1473 0.1516 0.1328 -0.0192 0.0056  0.0260  124 ALA   A N   
2597 C  CA  A ALA   A 124 ? 0.1286 0.1361 0.1288 -0.0074 0.0071  0.0243  124 ALA   A CA  
2598 C  CA  B ALA   A 124 ? 0.1489 0.1510 0.1418 -0.0231 0.0012  0.0252  124 ALA   A CA  
2599 C  C   A ALA   A 124 ? 0.1210 0.1382 0.1344 -0.0090 0.0125  0.0269  124 ALA   A C   
2600 C  C   B ALA   A 124 ? 0.1495 0.1509 0.1282 -0.0206 0.0045  0.0307  124 ALA   A C   
2601 O  O   A ALA   A 124 ? 0.1216 0.1489 0.1635 -0.0152 0.0167  0.0337  124 ALA   A O   
2602 O  O   B ALA   A 124 ? 0.1508 0.1568 0.1363 -0.0131 0.0073  0.0361  124 ALA   A O   
2603 C  CB  A ALA   A 124 ? 0.1331 0.1322 0.1531 -0.0024 0.0021  0.0317  124 ALA   A CB  
2604 C  CB  B ALA   A 124 ? 0.1542 0.1498 0.1695 -0.0265 0.0016  0.0235  124 ALA   A CB  
2615 N  N   A PRO   A 125 ? 0.1217 0.1380 0.1514 -0.0051 0.0108  0.0310  125 PRO   A N   
2616 N  N   B PRO   A 125 ? 0.1434 0.1434 0.1173 -0.0161 0.0071  0.0326  125 PRO   A N   
2617 C  CA  A PRO   A 125 ? 0.1255 0.1419 0.1581 -0.0028 0.0055  0.0223  125 PRO   A CA  
2618 C  CA  B PRO   A 125 ? 0.1481 0.1495 0.1233 -0.0111 0.0050  0.0253  125 PRO   A CA  
2619 C  C   A PRO   A 125 ? 0.1185 0.1376 0.1553 -0.0071 0.0054  0.0226  125 PRO   A C   
2620 C  C   B PRO   A 125 ? 0.1496 0.1580 0.1304 -0.0103 0.0052  0.0304  125 PRO   A C   
2621 O  O   A PRO   A 125 ? 0.1271 0.1345 0.1665 -0.0018 0.0002  0.0176  125 PRO   A O   
2622 O  O   B PRO   A 125 ? 0.1542 0.1583 0.1440 -0.0107 0.0107  0.0342  125 PRO   A O   
2623 C  CB  A PRO   A 125 ? 0.1430 0.1403 0.1552 -0.0138 0.0121  0.0235  125 PRO   A CB  
2624 C  CB  B PRO   A 125 ? 0.1514 0.1401 0.1131 -0.0144 0.0076  0.0225  125 PRO   A CB  
2625 C  CG  A PRO   A 125 ? 0.1404 0.1429 0.1558 -0.0109 0.0149  0.0258  125 PRO   A CG  
2626 C  CG  B PRO   A 125 ? 0.1459 0.1360 0.1198 -0.0144 0.0100  0.0233  125 PRO   A CG  
2627 C  CD  A PRO   A 125 ? 0.1285 0.1472 0.1628 -0.0101 0.0152  0.0231  125 PRO   A CD  
2628 C  CD  B PRO   A 125 ? 0.1359 0.1317 0.1149 -0.0166 0.0145  0.0217  125 PRO   A CD  
2643 N  N   A LEU   A 126 ? 0.1164 0.1412 0.1600 -0.0022 0.0087  0.0246  126 LEU   A N   
2644 N  N   B LEU   A 126 ? 0.1535 0.1621 0.1387 -0.0064 0.0010  0.0218  126 LEU   A N   
2645 C  CA  A LEU   A 126 ? 0.1193 0.1407 0.1639 -0.0052 0.0084  0.0277  126 LEU   A CA  
2646 C  CA  B LEU   A 126 ? 0.1539 0.1573 0.1353 -0.0036 0.0042  0.0215  126 LEU   A CA  
2647 C  C   A LEU   A 126 ? 0.1307 0.1365 0.1676 -0.0011 0.0020  0.0226  126 LEU   A C   
2648 C  C   B LEU   A 126 ? 0.1548 0.1489 0.1370 0.0035  0.0153  0.0105  126 LEU   A C   
2649 O  O   A LEU   A 126 ? 0.1398 0.1346 0.1981 0.0062  0.0192  0.0295  126 LEU   A O   
2650 O  O   B LEU   A 126 ? 0.1665 0.1444 0.1586 0.0016  0.0244  0.0130  126 LEU   A O   
2651 C  CB  A LEU   A 126 ? 0.1268 0.1428 0.1756 -0.0011 0.0023  0.0222  126 LEU   A CB  
2652 C  CB  B LEU   A 126 ? 0.1571 0.1628 0.1569 -0.0082 0.0021  0.0199  126 LEU   A CB  
2653 C  CG  A LEU   A 126 ? 0.1251 0.1560 0.1759 -0.0048 0.0033  0.0238  126 LEU   A CG  
2654 C  CG  B LEU   A 126 ? 0.1533 0.1643 0.1795 -0.0025 0.0076  0.0228  126 LEU   A CG  
2655 C  CD1 A LEU   A 126 ? 0.1340 0.1716 0.1948 -0.0070 0.0020  0.0299  126 LEU   A CD1 
2656 C  CD1 B LEU   A 126 ? 0.1544 0.1697 0.1928 -0.0017 -0.0042 0.0251  126 LEU   A CD1 
2657 C  CD2 A LEU   A 126 ? 0.1386 0.1522 0.1594 -0.0075 0.0027  0.0196  126 LEU   A CD2 
2658 C  CD2 B LEU   A 126 ? 0.1500 0.1667 0.1973 -0.0019 0.0057  0.0196  126 LEU   A CD2 
2681 N  N   A LEU   A 127 ? 0.1332 0.1460 0.1662 0.0008  -0.0002 0.0179  127 LEU   A N   
2682 N  N   B LEU   A 127 ? 0.1462 0.1492 0.1225 0.0054  0.0155  0.0202  127 LEU   A N   
2683 C  CA  A LEU   A 127 ? 0.1295 0.1439 0.1535 -0.0036 0.0007  0.0191  127 LEU   A CA  
2684 C  CA  B LEU   A 127 ? 0.1412 0.1553 0.1363 0.0016  0.0193  0.0307  127 LEU   A CA  
2685 C  C   A LEU   A 127 ? 0.1282 0.1352 0.1363 0.0024  0.0061  0.0098  127 LEU   A C   
2686 C  C   B LEU   A 127 ? 0.1400 0.1566 0.1503 0.0000  0.0167  0.0250  127 LEU   A C   
2687 O  O   A LEU   A 127 ? 0.1369 0.1338 0.1543 -0.0101 -0.0033 0.0084  127 LEU   A O   
2688 O  O   B LEU   A 127 ? 0.1424 0.1605 0.1518 -0.0130 0.0242  0.0355  127 LEU   A O   
2689 C  CB  A LEU   A 127 ? 0.1314 0.1499 0.1616 0.0050  0.0064  0.0176  127 LEU   A CB  
2690 C  CB  B LEU   A 127 ? 0.1459 0.1654 0.1384 0.0006  0.0175  0.0296  127 LEU   A CB  
2691 C  CG  A LEU   A 127 ? 0.1363 0.1519 0.1626 0.0074  -0.0027 0.0281  127 LEU   A CG  
2692 C  CG  B LEU   A 127 ? 0.1518 0.1785 0.1535 0.0046  0.0063  0.0286  127 LEU   A CG  
2693 C  CD1 A LEU   A 127 ? 0.1419 0.1474 0.1775 0.0085  0.0021  0.0180  127 LEU   A CD1 
2694 C  CD1 B LEU   A 127 ? 0.1499 0.1831 0.1679 0.0085  0.0058  0.0343  127 LEU   A CD1 
2695 C  CD2 A LEU   A 127 ? 0.1518 0.1552 0.1795 0.0121  -0.0114 0.0248  127 LEU   A CD2 
2696 C  CD2 B LEU   A 127 ? 0.1623 0.1860 0.1588 0.0052  -0.0068 0.0201  127 LEU   A CD2 
2719 N  N   A SER   A 128 ? 0.1358 0.1362 0.1304 -0.0032 -0.0000 0.0130  128 SER   A N   
2720 N  N   B SER   A 128 ? 0.1457 0.1587 0.1635 -0.0036 0.0074  0.0181  128 SER   A N   
2721 C  CA  A SER   A 128 ? 0.1463 0.1341 0.1183 -0.0032 0.0021  0.0103  128 SER   A CA  
2722 C  CA  B SER   A 128 ? 0.1536 0.1603 0.1653 -0.0021 0.0007  0.0111  128 SER   A CA  
2723 C  C   A SER   A 128 ? 0.1423 0.1367 0.1010 -0.0008 0.0044  0.0070  128 SER   A C   
2724 C  C   B SER   A 128 ? 0.1578 0.1657 0.1647 -0.0006 -0.0135 0.0159  128 SER   A C   
2725 O  O   A SER   A 128 ? 0.1485 0.1536 0.1099 -0.0002 0.0183  0.0090  128 SER   A O   
2726 O  O   B SER   A 128 ? 0.1581 0.1709 0.1607 0.0018  -0.0098 0.0153  128 SER   A O   
2727 C  CB  A SER   A 128 ? 0.1438 0.1363 0.1263 -0.0068 -0.0032 0.0102  128 SER   A CB  
2728 C  CB  B SER   A 128 ? 0.1514 0.1564 0.1645 0.0007  0.0019  0.0103  128 SER   A CB  
2729 O  OG  A SER   A 128 ? 0.1462 0.1404 0.1365 -0.0017 0.0067  0.0056  128 SER   A OG  
2730 O  OG  B SER   A 128 ? 0.1476 0.1554 0.1708 0.0039  0.0082  0.0153  128 SER   A OG  
2741 N  N   A ALA   A 129 ? 0.1401 0.1414 0.1077 -0.0013 0.0021  0.0135  129 ALA   A N   
2742 N  N   B ALA   A 129 ? 0.1607 0.1660 0.1760 0.0044  -0.0195 0.0185  129 ALA   A N   
2743 C  CA  A ALA   A 129 ? 0.1319 0.1443 0.1240 0.0033  0.0022  0.0177  129 ALA   A CA  
2744 C  CA  B ALA   A 129 ? 0.1656 0.1700 0.1877 0.0035  -0.0107 0.0191  129 ALA   A CA  
2745 C  C   A ALA   A 129 ? 0.1435 0.1422 0.1254 0.0026  -0.0004 0.0068  129 ALA   A C   
2746 C  C   B ALA   A 129 ? 0.1707 0.1742 0.1873 0.0046  -0.0148 0.0213  129 ALA   A C   
2747 O  O   A ALA   A 129 ? 0.1497 0.1471 0.1382 -0.0033 0.0065  0.0085  129 ALA   A O   
2748 O  O   B ALA   A 129 ? 0.1680 0.1746 0.1775 0.0022  -0.0137 0.0240  129 ALA   A O   
2749 C  CB  A ALA   A 129 ? 0.1321 0.1539 0.1600 0.0024  0.0126  0.0298  129 ALA   A CB  
2750 C  CB  B ALA   A 129 ? 0.1722 0.1794 0.2253 0.0029  0.0002  0.0157  129 ALA   A CB  
2761 N  N   A GLY   A 130 ? 0.1513 0.1356 0.1597 0.0004  0.0014  0.0044  130 GLY   A N   
2762 N  N   B GLY   A 130 ? 0.1763 0.1765 0.1930 0.0040  -0.0212 0.0244  130 GLY   A N   
2763 C  CA  A GLY   A 130 ? 0.1694 0.1410 0.1646 0.0075  -0.0012 0.0101  130 GLY   A CA  
2764 C  CA  B GLY   A 130 ? 0.1863 0.1784 0.1939 0.0068  -0.0229 0.0189  130 GLY   A CA  
2765 C  C   A GLY   A 130 ? 0.1753 0.1367 0.1508 0.0054  -0.0208 0.0052  130 GLY   A C   
2766 C  C   B GLY   A 130 ? 0.1939 0.1764 0.1906 0.0068  -0.0255 0.0099  130 GLY   A C   
2767 O  O   A GLY   A 130 ? 0.1752 0.1290 0.1631 0.0019  -0.0239 0.0065  130 GLY   A O   
2768 O  O   B GLY   A 130 ? 0.1990 0.1758 0.1940 0.0079  -0.0197 0.0075  130 GLY   A O   
2775 N  N   A ILE   A 131 ? 0.1911 0.1359 0.1461 -0.0047 -0.0178 0.0088  131 ILE   A N   
2776 N  N   B ILE   A 131 ? 0.1998 0.1733 0.1919 0.0006  -0.0298 0.0095  131 ILE   A N   
2777 C  CA  A ILE   A 131 ? 0.2048 0.1403 0.1346 -0.0116 -0.0268 0.0109  131 ILE   A CA  
2778 C  CA  B ILE   A 131 ? 0.2041 0.1724 0.1814 -0.0015 -0.0407 0.0102  131 ILE   A CA  
2779 C  C   A ILE   A 131 ? 0.1914 0.1453 0.1396 -0.0132 -0.0139 0.0287  131 ILE   A C   
2780 C  C   B ILE   A 131 ? 0.1996 0.1762 0.1769 -0.0031 -0.0344 0.0196  131 ILE   A C   
2781 O  O   A ILE   A 131 ? 0.1955 0.1514 0.1599 -0.0098 -0.0130 0.0229  131 ILE   A O   
2782 O  O   B ILE   A 131 ? 0.2014 0.1791 0.1848 -0.0015 -0.0338 0.0222  131 ILE   A O   
2783 C  CB  A ILE   A 131 ? 0.2227 0.1521 0.1387 -0.0219 -0.0358 0.0033  131 ILE   A CB  
2784 C  CB  B ILE   A 131 ? 0.2100 0.1773 0.1829 -0.0021 -0.0629 0.0077  131 ILE   A CB  
2785 C  CG1 A ILE   A 131 ? 0.2268 0.1805 0.1581 -0.0298 -0.0454 0.0096  131 ILE   A CG1 
2786 C  CG1 B ILE   A 131 ? 0.2134 0.1897 0.1895 -0.0002 -0.0746 0.0128  131 ILE   A CG1 
2787 C  CG2 A ILE   A 131 ? 0.2326 0.1367 0.1466 -0.0133 -0.0359 -0.0121 131 ILE   A CG2 
2788 C  CG2 B ILE   A 131 ? 0.2104 0.1731 0.1951 -0.0003 -0.0717 0.0033  131 ILE   A CG2 
2789 C  CD1 A ILE   A 131 ? 0.2318 0.1913 0.1856 -0.0295 -0.0573 0.0048  131 ILE   A CD1 
2790 C  CD1 B ILE   A 131 ? 0.2182 0.1962 0.2009 0.0009  -0.0809 0.0164  131 ILE   A CD1 
2813 N  N   A PHE   A 132 ? 0.1780 0.1390 0.1469 -0.0099 -0.0061 0.0258  132 PHE   A N   
2814 N  N   B PHE   A 132 ? 0.1948 0.1754 0.1787 -0.0030 -0.0312 0.0188  132 PHE   A N   
2815 C  CA  A PHE   A 132 ? 0.1739 0.1429 0.1462 -0.0176 -0.0089 0.0168  132 PHE   A CA  
2816 C  CA  B PHE   A 132 ? 0.1946 0.1782 0.1793 -0.0089 -0.0283 0.0133  132 PHE   A CA  
2817 C  C   A PHE   A 132 ? 0.1733 0.1556 0.1499 -0.0219 -0.0067 0.0184  132 PHE   A C   
2818 C  C   B PHE   A 132 ? 0.1961 0.1886 0.1934 -0.0106 -0.0258 0.0177  132 PHE   A C   
2819 O  O   A PHE   A 132 ? 0.1749 0.1604 0.1536 -0.0270 -0.0133 0.0185  132 PHE   A O   
2820 O  O   B PHE   A 132 ? 0.2054 0.1979 0.1929 -0.0202 -0.0191 0.0213  132 PHE   A O   
2821 C  CB  A PHE   A 132 ? 0.1734 0.1384 0.1478 -0.0162 -0.0106 0.0175  132 PHE   A CB  
2822 C  CB  B PHE   A 132 ? 0.1921 0.1689 0.1608 -0.0115 -0.0220 0.0075  132 PHE   A CB  
2823 C  CG  A PHE   A 132 ? 0.1688 0.1404 0.1460 -0.0039 -0.0119 0.0258  132 PHE   A CG  
2824 C  CG  B PHE   A 132 ? 0.1904 0.1647 0.1446 -0.0069 -0.0176 -0.0049 132 PHE   A CG  
2825 C  CD1 A PHE   A 132 ? 0.1679 0.1503 0.1660 0.0033  -0.0142 0.0112  132 PHE   A CD1 
2826 C  CD1 B PHE   A 132 ? 0.1908 0.1715 0.1569 -0.0011 -0.0131 -0.0194 132 PHE   A CD1 
2827 C  CD2 A PHE   A 132 ? 0.1654 0.1454 0.1542 -0.0031 -0.0092 0.0276  132 PHE   A CD2 
2828 C  CD2 B PHE   A 132 ? 0.1921 0.1628 0.1441 -0.0019 -0.0178 -0.0180 132 PHE   A CD2 
2829 C  CE1 A PHE   A 132 ? 0.1672 0.1549 0.1703 0.0016  -0.0189 0.0072  132 PHE   A CE1 
2830 C  CE1 B PHE   A 132 ? 0.1907 0.1753 0.1567 0.0013  -0.0170 -0.0218 132 PHE   A CE1 
2831 C  CE2 A PHE   A 132 ? 0.1598 0.1490 0.1569 0.0007  -0.0146 0.0222  132 PHE   A CE2 
2832 C  CE2 B PHE   A 132 ? 0.1908 0.1711 0.1547 0.0045  -0.0160 -0.0194 132 PHE   A CE2 
2833 C  CZ  A PHE   A 132 ? 0.1605 0.1520 0.1670 -0.0046 -0.0230 0.0166  132 PHE   A CZ  
2834 C  CZ  B PHE   A 132 ? 0.1905 0.1747 0.1618 0.0015  -0.0182 -0.0202 132 PHE   A CZ  
2853 N  N   A GLY   A 133 ? 0.1745 0.1690 0.1480 -0.0143 -0.0191 0.0234  133 GLY   A N   
2854 N  N   B GLY   A 133 ? 0.1923 0.1880 0.1907 -0.0034 -0.0365 0.0182  133 GLY   A N   
2855 C  CA  A GLY   A 133 ? 0.1778 0.1839 0.1522 -0.0159 -0.0202 0.0130  133 GLY   A CA  
2856 C  CA  B GLY   A 133 ? 0.1907 0.1899 0.1872 0.0005  -0.0342 0.0105  133 GLY   A CA  
2857 C  C   A GLY   A 133 ? 0.1863 0.1952 0.1597 -0.0179 -0.0336 0.0065  133 GLY   A C   
2858 C  C   B GLY   A 133 ? 0.1895 0.1934 0.1817 0.0071  -0.0403 -0.0002 133 GLY   A C   
2859 O  O   A GLY   A 133 ? 0.2001 0.2088 0.1669 -0.0143 -0.0273 -0.0122 133 GLY   A O   
2860 O  O   B GLY   A 133 ? 0.1905 0.1990 0.1741 0.0156  -0.0385 -0.0247 133 GLY   A O   
2867 N  N   A ALA   A 134 ? 0.1871 0.1842 0.1551 -0.0217 -0.0259 0.0073  134 ALA   A N   
2868 N  N   B ALA   A 134 ? 0.1897 0.1860 0.1773 0.0054  -0.0373 0.0033  134 ALA   A N   
2869 C  CA  A ALA   A 134 ? 0.1885 0.1834 0.1849 -0.0189 -0.0199 0.0039  134 ALA   A CA  
2870 C  CA  B ALA   A 134 ? 0.1907 0.1814 0.1864 0.0021  -0.0333 0.0001  134 ALA   A CA  
2871 C  C   A ALA   A 134 ? 0.1866 0.1829 0.1922 -0.0225 -0.0219 0.0070  134 ALA   A C   
2872 C  C   B ALA   A 134 ? 0.1884 0.1719 0.1845 -0.0049 -0.0317 -0.0004 134 ALA   A C   
2873 O  O   A ALA   A 134 ? 0.1935 0.1922 0.2138 -0.0249 -0.0114 0.0048  134 ALA   A O   
2874 O  O   B ALA   A 134 ? 0.1876 0.1722 0.2032 -0.0089 -0.0195 0.0023  134 ALA   A O   
2875 C  CB  A ALA   A 134 ? 0.1962 0.1810 0.2032 -0.0120 -0.0212 -0.0050 134 ALA   A CB  
2876 C  CB  B ALA   A 134 ? 0.1960 0.1823 0.2006 0.0049  -0.0361 -0.0036 134 ALA   A CB  
2887 N  N   A ASP   A 135 ? 0.1904 0.1806 0.2111 -0.0217 -0.0257 0.0217  135 ASP   A N   
2888 N  N   B ASP   A 135 ? 0.1937 0.1706 0.1951 -0.0102 -0.0378 0.0049  135 ASP   A N   
2889 C  CA  A ASP   A 135 ? 0.1898 0.1912 0.2329 -0.0273 -0.0348 0.0326  135 ASP   A CA  
2890 C  CA  B ASP   A 135 ? 0.1933 0.1713 0.2139 -0.0168 -0.0371 0.0027  135 ASP   A CA  
2891 C  C   A ASP   A 135 ? 0.1765 0.1805 0.2288 -0.0192 -0.0267 0.0489  135 ASP   A C   
2892 C  C   B ASP   A 135 ? 0.1794 0.1669 0.2115 -0.0124 -0.0262 0.0082  135 ASP   A C   
2893 O  O   A ASP   A 135 ? 0.1734 0.1790 0.2301 -0.0142 -0.0301 0.0539  135 ASP   A O   
2894 O  O   B ASP   A 135 ? 0.1735 0.1633 0.2077 -0.0149 -0.0243 0.0081  135 ASP   A O   
2895 C  CB  A ASP   A 135 ? 0.2105 0.2157 0.2613 -0.0383 -0.0466 0.0265  135 ASP   A CB  
2896 C  CB  B ASP   A 135 ? 0.2069 0.1822 0.2320 -0.0247 -0.0405 0.0007  135 ASP   A CB  
2897 C  CG  A ASP   A 135 ? 0.2241 0.2311 0.2945 -0.0561 -0.0492 0.0201  135 ASP   A CG  
2898 C  CG  B ASP   A 135 ? 0.2146 0.1970 0.2613 -0.0280 -0.0397 0.0026  135 ASP   A CG  
2899 O  OD1 A ASP   A 135 ? 0.2178 0.2345 0.2868 -0.0647 -0.0641 0.0378  135 ASP   A OD1 
2900 O  OD1 B ASP   A 135 ? 0.2158 0.1986 0.2795 -0.0232 -0.0352 0.0046  135 ASP   A OD1 
2901 O  OD2 A ASP   A 135 ? 0.2480 0.2478 0.3391 -0.0584 -0.0217 0.0094  135 ASP   A OD2 
2902 O  OD2 B ASP   A 135 ? 0.2208 0.2070 0.2843 -0.0358 -0.0394 0.0057  135 ASP   A OD2 
2911 N  N   A PRO   A 136 ? 0.1613 0.1729 0.2413 -0.0101 -0.0117 0.0496  136 PRO   A N   
2912 N  N   B PRO   A 136 ? 0.1694 0.1622 0.2156 -0.0037 -0.0152 0.0106  136 PRO   A N   
2913 C  CA  A PRO   A 136 ? 0.1541 0.1653 0.2531 -0.0099 0.0002  0.0359  136 PRO   A CA  
2914 C  CA  B PRO   A 136 ? 0.1650 0.1665 0.2132 -0.0055 -0.0045 0.0013  136 PRO   A CA  
2915 C  C   A PRO   A 136 ? 0.1402 0.1586 0.2415 -0.0032 0.0034  0.0307  136 PRO   A C   
2916 C  C   B PRO   A 136 ? 0.1584 0.1689 0.2000 -0.0030 -0.0007 0.0019  136 PRO   A C   
2917 O  O   A PRO   A 136 ? 0.1362 0.1562 0.2310 -0.0064 0.0003  0.0311  136 PRO   A O   
2918 O  O   B PRO   A 136 ? 0.1550 0.1580 0.1822 0.0033  0.0080  0.0039  136 PRO   A O   
2919 C  CB  A PRO   A 136 ? 0.1674 0.1629 0.2739 -0.0087 0.0011  0.0352  136 PRO   A CB  
2920 C  CB  B PRO   A 136 ? 0.1704 0.1638 0.2221 -0.0032 -0.0073 -0.0008 136 PRO   A CB  
2921 C  CG  A PRO   A 136 ? 0.1766 0.1699 0.2840 -0.0088 -0.0028 0.0384  136 PRO   A CG  
2922 C  CG  B PRO   A 136 ? 0.1788 0.1649 0.2368 0.0001  -0.0131 0.0065  136 PRO   A CG  
2923 C  CD  A PRO   A 136 ? 0.1726 0.1723 0.2635 -0.0074 -0.0045 0.0475  136 PRO   A CD  
2924 C  CD  B PRO   A 136 ? 0.1726 0.1606 0.2305 -0.0004 -0.0116 0.0120  136 PRO   A CD  
2939 N  N   A ILE   A 137 ? 0.1406 0.1640 0.2384 -0.0032 -0.0071 0.0380  137 ILE   A N   
2940 N  N   B ILE   A 137 ? 0.1592 0.1733 0.2075 -0.0078 -0.0018 0.0024  137 ILE   A N   
2941 C  CA  A ILE   A 137 ? 0.1449 0.1732 0.2300 -0.0110 -0.0170 0.0430  137 ILE   A CA  
2942 C  CA  B ILE   A 137 ? 0.1640 0.1805 0.2069 -0.0084 -0.0043 0.0055  137 ILE   A CA  
2943 C  C   A ILE   A 137 ? 0.1488 0.1776 0.2002 -0.0155 -0.0199 0.0414  137 ILE   A C   
2944 C  C   B ILE   A 137 ? 0.1606 0.1876 0.1982 -0.0130 -0.0017 0.0003  137 ILE   A C   
2945 O  O   A ILE   A 137 ? 0.1537 0.1697 0.2013 -0.0194 -0.0120 0.0374  137 ILE   A O   
2946 O  O   B ILE   A 137 ? 0.1585 0.1890 0.2012 -0.0135 0.0033  -0.0042 137 ILE   A O   
2947 C  CB  A ILE   A 137 ? 0.1497 0.1867 0.2517 -0.0119 -0.0329 0.0462  137 ILE   A CB  
2948 C  CB  B ILE   A 137 ? 0.1735 0.1783 0.2300 -0.0100 -0.0172 0.0207  137 ILE   A CB  
2949 C  CG1 A ILE   A 137 ? 0.1566 0.2073 0.2756 -0.0107 -0.0288 0.0613  137 ILE   A CG1 
2950 C  CG1 B ILE   A 137 ? 0.1838 0.1818 0.2463 -0.0058 -0.0291 0.0401  137 ILE   A CG1 
2951 C  CG2 A ILE   A 137 ? 0.1561 0.1856 0.2615 -0.0169 -0.0385 0.0234  137 ILE   A CG2 
2952 C  CG2 B ILE   A 137 ? 0.1766 0.1754 0.2424 -0.0096 -0.0192 0.0185  137 ILE   A CG2 
2953 C  CD1 A ILE   A 137 ? 0.1715 0.2203 0.2882 -0.0063 -0.0190 0.0692  137 ILE   A CD1 
2954 C  CD1 B ILE   A 137 ? 0.1912 0.1832 0.2613 -0.0065 -0.0317 0.0533  137 ILE   A CD1 
2977 N  N   A HIS   A 138 ? 0.1482 0.1924 0.2012 -0.0150 -0.0137 0.0341  138 HIS   A N   
2978 N  N   B HIS   A 138 ? 0.1598 0.1979 0.2015 -0.0145 0.0041  0.0035  138 HIS   A N   
2979 C  CA  A HIS   A 138 ? 0.1515 0.2011 0.1969 -0.0119 -0.0036 0.0259  138 HIS   A CA  
2980 C  CA  B HIS   A 138 ? 0.1597 0.1978 0.1961 -0.0140 0.0104  0.0097  138 HIS   A CA  
2981 C  C   A HIS   A 138 ? 0.1441 0.1914 0.1913 -0.0090 -0.0099 0.0285  138 HIS   A C   
2982 C  C   B HIS   A 138 ? 0.1521 0.1889 0.1935 -0.0114 0.0048  0.0225  138 HIS   A C   
2983 O  O   A HIS   A 138 ? 0.1547 0.1901 0.1892 -0.0091 -0.0022 0.0230  138 HIS   A O   
2984 O  O   B HIS   A 138 ? 0.1587 0.1887 0.1941 -0.0158 0.0103  0.0222  138 HIS   A O   
2985 C  CB  A HIS   A 138 ? 0.1708 0.2244 0.1946 -0.0145 -0.0177 0.0183  138 HIS   A CB  
2986 C  CB  B HIS   A 138 ? 0.1647 0.2081 0.1945 -0.0128 0.0074  -0.0008 138 HIS   A CB  
2987 C  CG  A HIS   A 138 ? 0.1912 0.2394 0.2046 -0.0223 -0.0170 0.0160  138 HIS   A CG  
2988 C  CG  B HIS   A 138 ? 0.1733 0.2154 0.2021 -0.0177 0.0057  -0.0069 138 HIS   A CG  
2989 N  ND1 A HIS   A 138 ? 0.2030 0.2494 0.2250 -0.0229 -0.0121 0.0040  138 HIS   A ND1 
2990 N  ND1 B HIS   A 138 ? 0.1797 0.2215 0.2181 -0.0163 0.0058  -0.0164 138 HIS   A ND1 
2991 C  CD2 A HIS   A 138 ? 0.2002 0.2492 0.2013 -0.0204 -0.0134 0.0166  138 HIS   A CD2 
2992 C  CD2 B HIS   A 138 ? 0.1759 0.2194 0.2005 -0.0161 0.0099  -0.0053 138 HIS   A CD2 
2993 C  CE1 A HIS   A 138 ? 0.2108 0.2577 0.2331 -0.0143 -0.0096 0.0047  138 HIS   A CE1 
2994 C  CE1 B HIS   A 138 ? 0.1830 0.2247 0.2232 -0.0110 0.0064  -0.0143 138 HIS   A CE1 
2995 N  NE2 A HIS   A 138 ? 0.2073 0.2576 0.2081 -0.0154 -0.0049 0.0092  138 HIS   A NE2 
2996 N  NE2 B HIS   A 138 ? 0.1796 0.2242 0.2086 -0.0125 0.0114  -0.0108 138 HIS   A NE2 
3011 N  N   . SER   A 139 ? 0.1416 0.1769 0.1939 -0.0056 -0.0008 0.0324  139 SER   A N   
3012 C  CA  . SER   A 139 ? 0.1372 0.1709 0.1963 -0.0096 0.0066  0.0292  139 SER   A CA  
3013 C  C   . SER   A 139 ? 0.1335 0.1554 0.1943 -0.0089 0.0093  0.0220  139 SER   A C   
3014 O  O   . SER   A 139 ? 0.1283 0.1535 0.2088 -0.0076 0.0055  0.0282  139 SER   A O   
3015 C  CB  . SER   A 139 ? 0.1348 0.1712 0.1927 -0.0107 -0.0021 0.0363  139 SER   A CB  
3016 O  OG  . SER   A 139 ? 0.1409 0.1712 0.2031 -0.0158 -0.0041 0.0400  139 SER   A OG  
3023 N  N   . LEU   A 140 ? 0.1311 0.1615 0.1850 -0.0088 0.0051  0.0348  140 LEU   A N   
3024 C  CA  . LEU   A 140 ? 0.1313 0.1577 0.1820 -0.0109 0.0023  0.0362  140 LEU   A CA  
3025 C  C   . LEU   A 140 ? 0.1283 0.1668 0.1948 -0.0179 -0.0020 0.0342  140 LEU   A C   
3026 O  O   . LEU   A 140 ? 0.1344 0.1666 0.2076 -0.0105 0.0028  0.0386  140 LEU   A O   
3027 C  CB  . LEU   A 140 ? 0.1327 0.1662 0.1917 -0.0141 0.0031  0.0326  140 LEU   A CB  
3028 C  CG  . LEU   A 140 ? 0.1351 0.1864 0.1982 -0.0216 0.0093  0.0362  140 LEU   A CG  
3029 C  CD1 . LEU   A 140 ? 0.1415 0.1855 0.2167 -0.0145 0.0091  0.0369  140 LEU   A CD1 
3030 C  CD2 . LEU   A 140 ? 0.1371 0.2004 0.2060 -0.0168 0.0113  0.0410  140 LEU   A CD2 
3042 N  N   . ARG   A 141 ? 0.1359 0.1723 0.2003 -0.0131 -0.0028 0.0307  141 ARG   A N   
3043 C  CA  . ARG   A 141 ? 0.1462 0.1817 0.2156 -0.0205 -0.0079 0.0144  141 ARG   A CA  
3044 C  C   . ARG   A 141 ? 0.1475 0.1669 0.2047 -0.0171 -0.0094 0.0134  141 ARG   A C   
3045 O  O   . ARG   A 141 ? 0.1476 0.1663 0.2204 -0.0174 0.0030  0.0162  141 ARG   A O   
3046 C  CB  . ARG   A 141 ? 0.1582 0.2064 0.2455 -0.0252 -0.0047 -0.0110 141 ARG   A CB  
3047 C  CG  . ARG   A 141 ? 0.1904 0.2410 0.2837 -0.0378 0.0139  -0.0206 141 ARG   A CG  
3048 C  CD  . ARG   A 141 ? 0.2240 0.2706 0.3198 -0.0491 0.0125  -0.0314 141 ARG   A CD  
3049 N  NE  . ARG   A 141 ? 0.2219 0.3049 0.3399 -0.0506 -0.0038 -0.0268 141 ARG   A NE  
3050 C  CZ  . ARG   A 141 ? 0.2257 0.3294 0.3464 -0.0701 0.0004  -0.0138 141 ARG   A CZ  
3051 N  NH1 . ARG   A 141 ? 0.2134 0.3319 0.3285 -0.0888 0.0308  -0.0285 141 ARG   A NH1 
3052 N  NH2 . ARG   A 141 ? 0.2377 0.3441 0.3716 -0.0630 -0.0152 0.0023  141 ARG   A NH2 
3066 N  N   . VAL   A 142 ? 0.1385 0.1617 0.1945 -0.0125 -0.0038 0.0104  142 VAL   A N   
3067 C  CA  . VAL   A 142 ? 0.1399 0.1559 0.1995 -0.0087 0.0121  0.0141  142 VAL   A CA  
3068 C  C   . VAL   A 142 ? 0.1287 0.1525 0.2016 -0.0164 0.0072  0.0188  142 VAL   A C   
3069 O  O   . VAL   A 142 ? 0.1330 0.1562 0.2058 -0.0039 0.0068  0.0130  142 VAL   A O   
3070 C  CB  . VAL   A 142 ? 0.1469 0.1667 0.1890 -0.0112 0.0166  0.0150  142 VAL   A CB  
3071 C  CG1 . VAL   A 142 ? 0.1465 0.1608 0.1946 -0.0173 0.0189  0.0118  142 VAL   A CG1 
3072 C  CG2 . VAL   A 142 ? 0.1618 0.1851 0.2115 -0.0076 0.0136  0.0142  142 VAL   A CG2 
3082 N  N   . CYS   A 143 ? 0.1347 0.1528 0.1955 -0.0182 0.0082  0.0125  143 CYS   A N   
3083 C  CA  . CYS   A 143 ? 0.1337 0.1505 0.2077 -0.0170 0.0138  0.0263  143 CYS   A CA  
3084 C  C   . CYS   A 143 ? 0.1332 0.1505 0.2167 -0.0111 0.0003  0.0297  143 CYS   A C   
3085 O  O   . CYS   A 143 ? 0.1309 0.1495 0.2086 -0.0055 0.0033  0.0313  143 CYS   A O   
3086 C  CB  . CYS   A 143 ? 0.1368 0.1570 0.2036 -0.0069 0.0136  0.0289  143 CYS   A CB  
3087 S  SG  . CYS   A 143 ? 0.1580 0.1650 0.1919 0.0030  0.0101  0.0191  143 CYS   A SG  
3093 N  N   . VAL   A 144 ? 0.1333 0.1562 0.2289 -0.0161 0.0044  0.0405  144 VAL   A N   
3094 C  CA  . VAL   A 144 ? 0.1401 0.1673 0.2594 -0.0174 0.0143  0.0470  144 VAL   A CA  
3095 C  C   . VAL   A 144 ? 0.1421 0.1570 0.2502 -0.0237 -0.0118 0.0402  144 VAL   A C   
3096 O  O   . VAL   A 144 ? 0.1643 0.1588 0.2541 -0.0101 -0.0129 0.0423  144 VAL   A O   
3097 C  CB  . VAL   A 144 ? 0.1652 0.1921 0.3229 -0.0079 0.0330  0.0491  144 VAL   A CB  
3098 C  CG1 . VAL   A 144 ? 0.1828 0.2090 0.3570 -0.0215 0.0131  0.0526  144 VAL   A CG1 
3099 C  CG2 . VAL   A 144 ? 0.1429 0.2000 0.3284 -0.0111 0.0424  0.0606  144 VAL   A CG2 
3109 N  N   . ASP   A 145 ? 0.1467 0.1518 0.2689 -0.0163 -0.0105 0.0324  145 ASP   A N   
3110 C  CA  . ASP   A 145 ? 0.1569 0.1551 0.2741 -0.0221 -0.0076 0.0190  145 ASP   A CA  
3111 C  C   . ASP   A 145 ? 0.1561 0.1508 0.2626 -0.0125 -0.0023 0.0094  145 ASP   A C   
3112 O  O   . ASP   A 145 ? 0.1717 0.1570 0.3146 -0.0145 -0.0085 -0.0210 145 ASP   A O   
3113 C  CB  . ASP   A 145 ? 0.1671 0.1856 0.2869 -0.0292 -0.0204 0.0186  145 ASP   A CB  
3114 C  CG  . ASP   A 145 ? 0.1833 0.2242 0.3200 -0.0495 -0.0328 0.0228  145 ASP   A CG  
3115 O  OD1 . ASP   A 145 ? 0.1786 0.2363 0.3362 -0.0577 -0.0190 0.0231  145 ASP   A OD1 
3116 O  OD2 . ASP   A 145 ? 0.2015 0.2485 0.3227 -0.0550 -0.0469 0.0290  145 ASP   A OD2 
3121 N  N   . THR   A 146 ? 0.1407 0.1454 0.2252 -0.0126 0.0058  0.0149  146 THR   A N   
3122 C  CA  . THR   A 146 ? 0.1382 0.1415 0.2239 -0.0089 0.0053  0.0113  146 THR   A CA  
3123 C  C   . THR   A 146 ? 0.1336 0.1375 0.2209 -0.0044 0.0136  0.0136  146 THR   A C   
3124 O  O   . THR   A 146 ? 0.1447 0.1549 0.2280 0.0025  0.0000  0.0177  146 THR   A O   
3125 C  CB  . THR   A 146 ? 0.1373 0.1428 0.2250 -0.0013 0.0084  0.0126  146 THR   A CB  
3126 O  OG1 . THR   A 146 ? 0.1360 0.1581 0.2234 0.0013  0.0047  0.0116  146 THR   A OG1 
3127 C  CG2 . THR   A 146 ? 0.1351 0.1434 0.2388 -0.0050 0.0116  0.0093  146 THR   A CG2 
3135 N  N   . VAL   A 147 ? 0.1313 0.1426 0.2138 -0.0041 0.0116  0.0216  147 VAL   A N   
3136 C  CA  . VAL   A 147 ? 0.1361 0.1448 0.2157 -0.0112 0.0262  0.0304  147 VAL   A CA  
3137 C  C   . VAL   A 147 ? 0.1339 0.1449 0.2293 -0.0155 0.0203  0.0354  147 VAL   A C   
3138 O  O   . VAL   A 147 ? 0.1387 0.1509 0.2411 -0.0169 0.0087  0.0373  147 VAL   A O   
3139 C  CB  . VAL   A 147 ? 0.1419 0.1457 0.2059 -0.0107 0.0223  0.0320  147 VAL   A CB  
3140 C  CG1 . VAL   A 147 ? 0.1682 0.1516 0.2089 -0.0029 0.0249  0.0342  147 VAL   A CG1 
3141 C  CG2 . VAL   A 147 ? 0.1510 0.1467 0.1971 -0.0091 0.0117  0.0217  147 VAL   A CG2 
3151 N  N   . ARG   A 148 ? 0.1349 0.1487 0.2385 -0.0166 0.0177  0.0486  148 ARG   A N   
3152 C  CA  . ARG   A 148 ? 0.1426 0.1515 0.2382 -0.0172 0.0052  0.0568  148 ARG   A CA  
3153 C  C   . ARG   A 148 ? 0.1506 0.1493 0.2418 -0.0183 0.0056  0.0687  148 ARG   A C   
3154 O  O   . ARG   A 148 ? 0.1809 0.1590 0.2550 -0.0234 0.0113  0.0552  148 ARG   A O   
3155 C  CB  . ARG   A 148 ? 0.1481 0.1544 0.2524 -0.0093 0.0151  0.0487  148 ARG   A CB  
3156 C  CG  . ARG   A 148 ? 0.1649 0.1542 0.2885 -0.0129 0.0363  0.0478  148 ARG   A CG  
3157 C  CD  . ARG   A 148 ? 0.1786 0.1510 0.3039 -0.0046 0.0461  0.0602  148 ARG   A CD  
3158 N  NE  . ARG   A 148 ? 0.1717 0.1577 0.2997 0.0092  0.0530  0.0589  148 ARG   A NE  
3159 C  CZ  . ARG   A 148 ? 0.1718 0.1440 0.2923 0.0000  0.0484  0.0461  148 ARG   A CZ  
3160 N  NH1 . ARG   A 148 ? 0.1785 0.1454 0.2901 -0.0123 0.0481  0.0242  148 ARG   A NH1 
3161 N  NH2 . ARG   A 148 ? 0.1637 0.1618 0.2945 0.0117  0.0504  0.0517  148 ARG   A NH2 
3175 N  N   . THR   A 149 ? 0.1536 0.1655 0.2278 -0.0194 -0.0038 0.0610  149 THR   A N   
3176 C  CA  . THR   A 149 ? 0.1527 0.1707 0.2270 -0.0159 0.0009  0.0548  149 THR   A CA  
3177 C  C   . THR   A 149 ? 0.1482 0.1669 0.2147 -0.0221 0.0037  0.0639  149 THR   A C   
3178 O  O   . THR   A 149 ? 0.1489 0.1764 0.2300 -0.0224 0.0033  0.0582  149 THR   A O   
3179 C  CB  . THR   A 149 ? 0.1557 0.1803 0.2284 -0.0167 0.0001  0.0488  149 THR   A CB  
3180 O  OG1 . THR   A 149 ? 0.1562 0.1669 0.2391 -0.0260 0.0001  0.0496  149 THR   A OG1 
3181 C  CG2 . THR   A 149 ? 0.1499 0.1933 0.2306 -0.0090 -0.0052 0.0394  149 THR   A CG2 
3189 N  N   . ASN   A 150 ? 0.1528 0.1764 0.2081 -0.0150 -0.0032 0.0744  150 ASN   A N   
3190 C  CA  . ASN   A 150 ? 0.1658 0.1852 0.2026 -0.0218 -0.0026 0.0639  150 ASN   A CA  
3191 C  C   . ASN   A 150 ? 0.1475 0.1736 0.1960 -0.0207 -0.0008 0.0574  150 ASN   A C   
3192 O  O   . ASN   A 150 ? 0.1574 0.1831 0.2238 -0.0179 -0.0129 0.0531  150 ASN   A O   
3193 C  CB  . ASN   A 150 ? 0.2098 0.2075 0.2326 -0.0284 0.0139  0.0829  150 ASN   A CB  
3194 C  CG  . ASN   A 150 ? 0.2669 0.2389 0.3031 -0.0268 0.0057  0.0797  150 ASN   A CG  
3195 O  OD1 . ASN   A 150 ? 0.2900 0.2418 0.3209 -0.0305 0.0101  0.0894  150 ASN   A OD1 
3196 N  ND2 . ASN   A 150 ? 0.2974 0.2630 0.3440 -0.0199 -0.0009 0.0768  150 ASN   A ND2 
3203 N  N   . VAL   A 151 ? 0.1514 0.1580 0.1975 -0.0235 -0.0009 0.0530  151 VAL   A N   
3204 C  CA  . VAL   A 151 ? 0.1561 0.1609 0.1888 -0.0236 0.0039  0.0536  151 VAL   A CA  
3205 C  C   . VAL   A 151 ? 0.1463 0.1567 0.1972 -0.0297 0.0041  0.0530  151 VAL   A C   
3206 O  O   . VAL   A 151 ? 0.1564 0.1625 0.2432 -0.0234 0.0038  0.0470  151 VAL   A O   
3207 C  CB  . VAL   A 151 ? 0.1835 0.1778 0.1991 -0.0097 0.0029  0.0476  151 VAL   A CB  
3208 C  CG1 . VAL   A 151 ? 0.1799 0.1989 0.2200 -0.0119 0.0062  0.0489  151 VAL   A CG1 
3209 C  CG2 . VAL   A 151 ? 0.1952 0.1726 0.1929 -0.0128 0.0198  0.0446  151 VAL   A CG2 
3219 N  N   . TYR   A 152 ? 0.1418 0.1619 0.1977 -0.0292 0.0013  0.0505  152 TYR   A N   
3220 C  CA  . TYR   A 152 ? 0.1469 0.1717 0.1815 -0.0263 0.0064  0.0473  152 TYR   A CA  
3221 C  C   . TYR   A 152 ? 0.1411 0.1635 0.1700 -0.0226 0.0141  0.0465  152 TYR   A C   
3222 O  O   . TYR   A 152 ? 0.1510 0.1576 0.1721 -0.0238 0.0161  0.0387  152 TYR   A O   
3223 C  CB  . TYR   A 152 ? 0.1676 0.1820 0.1905 -0.0251 0.0133  0.0593  152 TYR   A CB  
3224 C  CG  . TYR   A 152 ? 0.1721 0.2095 0.1854 -0.0295 0.0125  0.0624  152 TYR   A CG  
3225 C  CD1 . TYR   A 152 ? 0.1873 0.2346 0.1966 -0.0185 0.0199  0.0676  152 TYR   A CD1 
3226 C  CD2 . TYR   A 152 ? 0.1787 0.2222 0.1803 -0.0409 0.0070  0.0582  152 TYR   A CD2 
3227 C  CE1 . TYR   A 152 ? 0.2222 0.2485 0.2096 -0.0113 0.0146  0.0782  152 TYR   A CE1 
3228 C  CE2 . TYR   A 152 ? 0.2103 0.2378 0.1986 -0.0406 0.0123  0.0719  152 TYR   A CE2 
3229 C  CZ  . TYR   A 152 ? 0.2375 0.2444 0.2003 -0.0271 0.0104  0.0977  152 TYR   A CZ  
3230 O  OH  . TYR   A 152 ? 0.2701 0.2660 0.2461 -0.0222 0.0091  0.1099  152 TYR   A OH  
3240 N  N   . LEU   A 153 ? 0.1421 0.1549 0.1826 -0.0267 0.0149  0.0488  153 LEU   A N   
3241 C  CA  . LEU   A 153 ? 0.1331 0.1513 0.1953 -0.0156 0.0107  0.0434  153 LEU   A CA  
3242 C  C   . LEU   A 153 ? 0.1382 0.1560 0.1924 -0.0154 0.0206  0.0455  153 LEU   A C   
3243 O  O   . LEU   A 153 ? 0.1473 0.1685 0.2201 -0.0171 0.0372  0.0404  153 LEU   A O   
3244 C  CB  . LEU   A 153 ? 0.1294 0.1548 0.1984 -0.0129 0.0095  0.0462  153 LEU   A CB  
3245 C  CG  . LEU   A 153 ? 0.1366 0.1539 0.1941 -0.0161 0.0147  0.0364  153 LEU   A CG  
3246 C  CD1 . LEU   A 153 ? 0.1523 0.1617 0.1979 -0.0190 0.0019  0.0362  153 LEU   A CD1 
3247 C  CD2 . LEU   A 153 ? 0.1455 0.1611 0.2032 -0.0115 0.0218  0.0123  153 LEU   A CD2 
3259 N  N   . ALA   A 154 ? 0.1365 0.1538 0.1945 -0.0092 0.0235  0.0427  154 ALA   A N   
3260 C  CA  . ALA   A 154 ? 0.1465 0.1548 0.1972 -0.0036 0.0269  0.0423  154 ALA   A CA  
3261 C  C   . ALA   A 154 ? 0.1420 0.1520 0.1956 -0.0020 0.0227  0.0487  154 ALA   A C   
3262 O  O   . ALA   A 154 ? 0.1457 0.1719 0.2083 -0.0050 0.0203  0.0495  154 ALA   A O   
3263 C  CB  . ALA   A 154 ? 0.1616 0.1578 0.2108 0.0001  0.0212  0.0268  154 ALA   A CB  
3269 N  N   A VAL   A 155 ? 0.1308 0.1417 0.1726 0.0053  0.0225  0.0529  155 VAL   A N   
3270 N  N   B VAL   A 155 ? 0.1280 0.1354 0.1730 0.0040  0.0262  0.0518  155 VAL   A N   
3271 C  CA  A VAL   A 155 ? 0.1359 0.1554 0.1700 0.0040  0.0105  0.0503  155 VAL   A CA  
3272 C  CA  B VAL   A 155 ? 0.1320 0.1449 0.1709 0.0001  0.0181  0.0481  155 VAL   A CA  
3273 C  CA  T VAL   A 155 ? 0.2053 0.1926 0.2116 -0.0062 0.0141  0.0263  155 VAL   A CA  
3274 C  C   A VAL   A 155 ? 0.1467 0.1675 0.1817 0.0194  0.0024  0.0538  155 VAL   A C   
3275 C  C   B VAL   A 155 ? 0.1478 0.1582 0.1860 0.0098  0.0190  0.0491  155 VAL   A C   
3276 C  C   T VAL   A 155 ? 0.1961 0.1879 0.1953 -0.0015 0.0298  0.0409  155 VAL   A C   
3277 O  O   A VAL   A 155 ? 0.1499 0.1780 0.1808 0.0299  0.0087  0.0437  155 VAL   A O   
3278 O  O   B VAL   A 155 ? 0.1515 0.1679 0.1717 0.0207  0.0220  0.0396  155 VAL   A O   
3279 O  O   T VAL   A 155 ? 0.1914 0.1927 0.1836 0.0028  0.0308  0.0424  155 VAL   A O   
3280 C  CB  A VAL   A 155 ? 0.1351 0.1566 0.1755 -0.0023 -0.0020 0.0440  155 VAL   A CB  
3281 C  CB  B VAL   A 155 ? 0.1276 0.1432 0.1794 -0.0020 -0.0044 0.0381  155 VAL   A CB  
3282 C  CB  T VAL   A 155 ? 0.2132 0.1916 0.2270 -0.0102 0.0032  0.0194  155 VAL   A CB  
3283 C  CG1 A VAL   A 155 ? 0.1412 0.1572 0.1744 -0.0025 0.0020  0.0460  155 VAL   A CG1 
3284 C  CG1 B VAL   A 155 ? 0.1354 0.1436 0.1806 -0.0024 -0.0073 0.0366  155 VAL   A CG1 
3285 C  CG1 T VAL   A 155 ? 0.2173 0.1942 0.2284 -0.0102 -0.0040 0.0188  155 VAL   A CG1 
3286 C  CG2 A VAL   A 155 ? 0.1455 0.1614 0.1964 0.0004  -0.0095 0.0408  155 VAL   A CG2 
3287 C  CG2 B VAL   A 155 ? 0.1404 0.1477 0.2026 0.0064  -0.0115 0.0361  155 VAL   A CG2 
3288 C  CG2 T VAL   A 155 ? 0.2127 0.1895 0.2347 -0.0132 -0.0015 0.0148  155 VAL   A CG2 
3314 N  N   A PHE   A 156 ? 0.1623 0.1749 0.2014 0.0257  -0.0057 0.0681  156 PHE   A N   
3315 N  N   B PHE   A 156 ? 0.1673 0.1690 0.2287 0.0122  0.0222  0.0570  156 PHE   A N   
3316 N  N   T PHE   A 156 ? 0.1946 0.1800 0.2061 0.0024  0.0423  0.0524  156 PHE   A N   
3317 C  CA  A PHE   A 156 ? 0.1834 0.1860 0.2393 0.0375  -0.0063 0.0661  156 PHE   A CA  
3318 C  CA  B PHE   A 156 ? 0.1827 0.1813 0.2459 0.0211  0.0083  0.0588  156 PHE   A CA  
3319 C  CA  T PHE   A 156 ? 0.1978 0.1732 0.2013 0.0110  0.0444  0.0659  156 PHE   A CA  
3320 C  C   A PHE   A 156 ? 0.1891 0.1926 0.2398 0.0415  0.0081  0.0653  156 PHE   A C   
3321 C  C   B PHE   A 156 ? 0.1835 0.1828 0.2491 0.0255  0.0331  0.0618  156 PHE   A C   
3322 C  C   T PHE   A 156 ? 0.1851 0.1809 0.2075 0.0128  0.0455  0.0629  156 PHE   A C   
3323 O  O   A PHE   A 156 ? 0.1893 0.2023 0.2409 0.0371  0.0163  0.0648  156 PHE   A O   
3324 O  O   B PHE   A 156 ? 0.1824 0.1883 0.2532 0.0237  0.0495  0.0571  156 PHE   A O   
3325 O  O   T PHE   A 156 ? 0.1876 0.1897 0.2148 0.0132  0.0437  0.0475  156 PHE   A O   
3326 C  CB  A PHE   A 156 ? 0.1992 0.1921 0.2671 0.0339  -0.0109 0.0700  156 PHE   A CB  
3327 C  CB  B PHE   A 156 ? 0.1999 0.1959 0.2655 0.0150  -0.0212 0.0486  156 PHE   A CB  
3328 C  CB  T PHE   A 156 ? 0.2091 0.1573 0.1888 0.0131  0.0504  0.0802  156 PHE   A CB  
3329 C  CG  A PHE   A 156 ? 0.2174 0.1963 0.2877 0.0339  -0.0095 0.0611  156 PHE   A CG  
3330 C  CG  B PHE   A 156 ? 0.2207 0.2162 0.2975 0.0111  -0.0389 0.0290  156 PHE   A CG  
3331 C  CG  T PHE   A 156 ? 0.2221 0.1525 0.1849 0.0190  0.0484  0.0865  156 PHE   A CG  
3332 C  CD1 A PHE   A 156 ? 0.2245 0.2000 0.2903 0.0364  0.0000  0.0553  156 PHE   A CD1 
3333 C  CD1 B PHE   A 156 ? 0.2292 0.2293 0.3183 0.0113  -0.0421 0.0191  156 PHE   A CD1 
3334 C  CD1 T PHE   A 156 ? 0.2327 0.1611 0.2148 0.0262  0.0305  0.0721  156 PHE   A CD1 
3335 C  CD2 A PHE   A 156 ? 0.2237 0.2002 0.2937 0.0404  -0.0121 0.0632  156 PHE   A CD2 
3336 C  CD2 B PHE   A 156 ? 0.2287 0.2285 0.3140 0.0122  -0.0451 0.0175  156 PHE   A CD2 
3337 C  CD2 T PHE   A 156 ? 0.2266 0.1491 0.1872 0.0254  0.0533  0.0889  156 PHE   A CD2 
3338 C  CE1 A PHE   A 156 ? 0.2325 0.2014 0.2967 0.0376  0.0031  0.0497  156 PHE   A CE1 
3339 C  CE1 B PHE   A 156 ? 0.2326 0.2350 0.3260 0.0102  -0.0461 0.0108  156 PHE   A CE1 
3340 C  CE1 T PHE   A 156 ? 0.2397 0.1625 0.2260 0.0298  0.0227  0.0639  156 PHE   A CE1 
3341 C  CE2 A PHE   A 156 ? 0.2372 0.2058 0.3010 0.0411  -0.0100 0.0522  156 PHE   A CE2 
3342 C  CE2 B PHE   A 156 ? 0.2353 0.2360 0.3259 0.0126  -0.0486 0.0085  156 PHE   A CE2 
3343 C  CE2 T PHE   A 156 ? 0.2359 0.1544 0.2058 0.0260  0.0461  0.0736  156 PHE   A CE2 
3344 C  CZ  A PHE   A 156 ? 0.2388 0.2065 0.3036 0.0396  -0.0004 0.0483  156 PHE   A CZ  
3345 C  CZ  B PHE   A 156 ? 0.2367 0.2372 0.3273 0.0126  -0.0492 0.0081  156 PHE   A CZ  
3346 C  CZ  T PHE   A 156 ? 0.2394 0.1538 0.2206 0.0240  0.0344  0.0674  156 PHE   A CZ  
3374 N  N   A ASP   A 157 ? 0.1954 0.1934 0.2419 0.0453  0.0035  0.0570  157 ASP   A N   
3375 N  N   B ASP   A 157 ? 0.1905 0.1871 0.2627 0.0274  0.0260  0.0704  157 ASP   A N   
3376 N  N   T ASP   A 157 ? 0.1699 0.1832 0.2153 0.0129  0.0340  0.0714  157 ASP   A N   
3377 C  CA  A ASP   A 157 ? 0.2097 0.2075 0.2482 0.0441  0.0056  0.0465  157 ASP   A CA  
3378 C  CA  B ASP   A 157 ? 0.1975 0.1972 0.2603 0.0253  0.0202  0.0647  157 ASP   A CA  
3379 C  CA  T ASP   A 157 ? 0.1614 0.1940 0.2168 0.0147  0.0254  0.0670  157 ASP   A CA  
3380 C  C   A ASP   A 157 ? 0.2078 0.2233 0.2504 0.0428  0.0119  0.0460  157 ASP   A C   
3381 C  C   B ASP   A 157 ? 0.1797 0.2041 0.2476 0.0208  0.0260  0.0633  157 ASP   A C   
3382 C  C   T ASP   A 157 ? 0.1598 0.2098 0.2179 0.0163  0.0324  0.0662  157 ASP   A C   
3383 O  O   A ASP   A 157 ? 0.2064 0.2200 0.2447 0.0437  0.0145  0.0465  157 ASP   A O   
3384 O  O   B ASP   A 157 ? 0.1693 0.1983 0.2441 0.0226  0.0322  0.0720  157 ASP   A O   
3385 O  O   T ASP   A 157 ? 0.1548 0.2076 0.2196 0.0185  0.0370  0.0678  157 ASP   A O   
3386 C  CB  A ASP   A 157 ? 0.2240 0.2062 0.2555 0.0489  -0.0015 0.0371  157 ASP   A CB  
3387 C  CB  B ASP   A 157 ? 0.2184 0.2004 0.2702 0.0347  0.0072  0.0636  157 ASP   A CB  
3388 C  CB  T ASP   A 157 ? 0.1542 0.1893 0.2146 0.0209  0.0083  0.0616  157 ASP   A CB  
3389 C  CG  A ASP   A 157 ? 0.2383 0.2072 0.2765 0.0512  -0.0029 0.0234  157 ASP   A CG  
3390 C  CG  B ASP   A 157 ? 0.2381 0.2053 0.2835 0.0448  -0.0024 0.0549  157 ASP   A CG  
3391 C  CG  T ASP   A 157 ? 0.1437 0.1840 0.2199 0.0242  0.0044  0.0523  157 ASP   A CG  
3392 O  OD1 A ASP   A 157 ? 0.2556 0.2174 0.3023 0.0428  -0.0134 0.0125  157 ASP   A OD1 
3393 O  OD1 B ASP   A 157 ? 0.2563 0.2088 0.3129 0.0441  -0.0202 0.0436  157 ASP   A OD1 
3394 O  OD1 T ASP   A 157 ? 0.1468 0.1783 0.2480 0.0166  0.0009  0.0307  157 ASP   A OD1 
3395 O  OD2 A ASP   A 157 ? 0.2341 0.1985 0.2767 0.0554  0.0092  0.0213  157 ASP   A OD2 
3396 O  OD2 B ASP   A 157 ? 0.2349 0.2057 0.2727 0.0480  0.0075  0.0592  157 ASP   A OD2 
3397 O  OD2 T ASP   A 157 ? 0.1308 0.1857 0.2008 0.0338  0.0101  0.0625  157 ASP   A OD2 
3410 N  N   A LYS   A 158 ? 0.2112 0.2400 0.2609 0.0415  0.0182  0.0390  158 LYS   A N   
3411 N  N   B LYS   A 158 ? 0.1805 0.2190 0.2526 0.0186  0.0250  0.0534  158 LYS   A N   
3412 N  N   T LYS   A 158 ? 0.1701 0.2280 0.2282 0.0138  0.0347  0.0464  158 LYS   A N   
3413 C  CA  A LYS   A 158 ? 0.2088 0.2552 0.2814 0.0448  0.0311  0.0302  158 LYS   A CA  
3414 C  CA  B LYS   A 158 ? 0.1850 0.2346 0.2581 0.0191  0.0332  0.0425  158 LYS   A CA  
3415 C  CA  T LYS   A 158 ? 0.1802 0.2444 0.2516 0.0186  0.0366  0.0277  158 LYS   A CA  
3416 C  C   A LYS   A 158 ? 0.1916 0.2516 0.2663 0.0450  0.0214  0.0241  158 LYS   A C   
3417 C  C   B LYS   A 158 ? 0.1657 0.2311 0.2296 0.0184  0.0103  0.0345  158 LYS   A C   
3418 C  C   T LYS   A 158 ? 0.1759 0.2372 0.2411 0.0198  0.0222  0.0127  158 LYS   A C   
3419 O  O   A LYS   A 158 ? 0.1891 0.2565 0.2642 0.0432  0.0305  0.0176  158 LYS   A O   
3420 O  O   B LYS   A 158 ? 0.1555 0.2354 0.2213 0.0103  0.0108  0.0375  158 LYS   A O   
3421 O  O   T LYS   A 158 ? 0.1701 0.2351 0.2363 0.0182  0.0261  0.0014  158 LYS   A O   
3422 C  CB  A LYS   A 158 ? 0.2276 0.2690 0.3188 0.0447  0.0539  0.0342  158 LYS   A CB  
3423 C  CB  B LYS   A 158 ? 0.2089 0.2596 0.2934 0.0198  0.0519  0.0466  158 LYS   A CB  
3424 C  CB  T LYS   A 158 ? 0.2014 0.2630 0.2935 0.0189  0.0546  0.0277  158 LYS   A CB  
3425 C  CG  A LYS   A 158 ? 0.2475 0.2805 0.3559 0.0454  0.0649  0.0452  158 LYS   A CG  
3426 C  CG  B LYS   A 158 ? 0.2336 0.2825 0.3370 0.0217  0.0600  0.0561  158 LYS   A CG  
3427 C  CG  T LYS   A 158 ? 0.2245 0.2793 0.3373 0.0208  0.0602  0.0336  158 LYS   A CG  
3428 C  CD  A LYS   A 158 ? 0.2615 0.2880 0.3863 0.0464  0.0798  0.0584  158 LYS   A CD  
3429 C  CD  B LYS   A 158 ? 0.2532 0.3006 0.3768 0.0224  0.0694  0.0663  158 LYS   A CD  
3430 C  CD  T LYS   A 158 ? 0.2452 0.2921 0.3797 0.0269  0.0632  0.0408  158 LYS   A CD  
3431 C  CE  A LYS   A 158 ? 0.2707 0.2910 0.4043 0.0453  0.0915  0.0742  158 LYS   A CE  
3432 C  CE  B LYS   A 158 ? 0.2638 0.3119 0.4040 0.0254  0.0770  0.0788  158 LYS   A CE  
3433 C  CE  T LYS   A 158 ? 0.2602 0.3002 0.4091 0.0298  0.0646  0.0481  158 LYS   A CE  
3434 N  NZ  A LYS   A 158 ? 0.2737 0.2910 0.4143 0.0445  0.0997  0.0823  158 LYS   A NZ  
3435 N  NZ  B LYS   A 158 ? 0.2676 0.3174 0.4214 0.0243  0.0810  0.0875  158 LYS   A NZ  
3436 N  NZ  T LYS   A 158 ? 0.2680 0.3036 0.4251 0.0320  0.0660  0.0515  158 LYS   A NZ  
3476 N  N   A ASN   A 159 ? 0.1818 0.2379 0.2637 0.0372  0.0053  0.0257  159 ASN   A N   
3477 N  N   B ASN   A 159 ? 0.1674 0.2310 0.2200 0.0228  -0.0046 0.0281  159 ASN   A N   
3478 N  N   T ASN   A 159 ? 0.1818 0.2288 0.2476 0.0142  0.0097  0.0116  159 ASN   A N   
3479 C  CA  A ASN   A 159 ? 0.1760 0.2263 0.2530 0.0280  -0.0098 0.0323  159 ASN   A CA  
3480 C  CA  B ASN   A 159 ? 0.1694 0.2332 0.2162 0.0217  -0.0093 0.0314  159 ASN   A CA  
3481 C  CA  T ASN   A 159 ? 0.1952 0.2245 0.2505 0.0116  -0.0020 0.0150  159 ASN   A CA  
3482 C  C   A ASN   A 159 ? 0.1587 0.2137 0.2380 0.0191  -0.0022 0.0320  159 ASN   A C   
3483 C  C   B ASN   A 159 ? 0.1529 0.2265 0.2069 0.0132  -0.0129 0.0317  159 ASN   A C   
3484 C  C   T ASN   A 159 ? 0.2009 0.2231 0.2522 0.0093  0.0083  0.0101  159 ASN   A C   
3485 O  O   A ASN   A 159 ? 0.1469 0.2001 0.2378 0.0180  -0.0086 0.0135  159 ASN   A O   
3486 O  O   B ASN   A 159 ? 0.1557 0.2321 0.2109 0.0148  -0.0196 0.0281  159 ASN   A O   
3487 O  O   T ASN   A 159 ? 0.1998 0.2145 0.2542 0.0092  0.0109  -0.0016 159 ASN   A O   
3488 C  CB  A ASN   A 159 ? 0.1874 0.2306 0.2709 0.0266  -0.0193 0.0385  159 ASN   A CB  
3489 C  CB  B ASN   A 159 ? 0.1916 0.2455 0.2408 0.0274  -0.0097 0.0316  159 ASN   A CB  
3490 C  CB  T ASN   A 159 ? 0.2032 0.2253 0.2651 0.0122  -0.0137 0.0247  159 ASN   A CB  
3491 C  CG  A ASN   A 159 ? 0.2026 0.2411 0.2982 0.0247  -0.0193 0.0357  159 ASN   A CG  
3492 C  CG  B ASN   A 159 ? 0.2119 0.2624 0.2758 0.0205  -0.0015 0.0222  159 ASN   A CG  
3493 C  CG  T ASN   A 159 ? 0.2135 0.2304 0.2851 0.0142  -0.0177 0.0266  159 ASN   A CG  
3494 O  OD1 A ASN   A 159 ? 0.2139 0.2554 0.3192 0.0257  -0.0059 0.0300  159 ASN   A OD1 
3495 O  OD1 B ASN   A 159 ? 0.2231 0.2737 0.2948 0.0179  0.0056  0.0112  159 ASN   A OD1 
3496 O  OD1 T ASN   A 159 ? 0.2213 0.2418 0.3046 0.0171  -0.0070 0.0192  159 ASN   A OD1 
3497 N  ND2 A ASN   A 159 ? 0.2070 0.2431 0.3060 0.0242  -0.0254 0.0350  159 ASN   A ND2 
3498 N  ND2 B ASN   A 159 ? 0.2157 0.2681 0.2848 0.0164  -0.0064 0.0247  159 ASN   A ND2 
3499 N  ND2 T ASN   A 159 ? 0.2169 0.2314 0.2893 0.0151  -0.0249 0.0300  159 ASN   A ND2 
3518 N  N   A LEU   A 160 ? 0.1541 0.2107 0.2257 0.0136  0.0039  0.0530  160 LEU   A N   
3519 N  N   B LEU   A 160 ? 0.1416 0.2177 0.2046 0.0027  -0.0083 0.0476  160 LEU   A N   
3520 N  N   T LEU   A 160 ? 0.2071 0.2269 0.2548 0.0079  0.0111  0.0182  160 LEU   A N   
3521 C  CA  A LEU   A 160 ? 0.1575 0.2125 0.2196 0.0044  0.0152  0.0706  160 LEU   A CA  
3522 C  CA  B LEU   A 160 ? 0.1360 0.2127 0.1963 -0.0062 0.0075  0.0701  160 LEU   A CA  
3523 C  CA  T LEU   A 160 ? 0.2171 0.2322 0.2566 0.0034  0.0162  0.0269  160 LEU   A CA  
3524 C  C   A LEU   A 160 ? 0.1404 0.2132 0.2054 -0.0040 0.0188  0.0856  160 LEU   A C   
3525 C  C   B LEU   A 160 ? 0.1269 0.2173 0.1884 0.0005  0.0144  0.0773  160 LEU   A C   
3526 O  O   A LEU   A 160 ? 0.1274 0.2064 0.2051 -0.0147 0.0129  0.0912  160 LEU   A O   
3527 O  O   B LEU   A 160 ? 0.1268 0.2139 0.1988 -0.0060 0.0152  0.0816  160 LEU   A O   
3528 C  CB  A LEU   A 160 ? 0.1703 0.2168 0.2264 0.0020  0.0196  0.0724  160 LEU   A CB  
3529 C  CB  B LEU   A 160 ? 0.1425 0.2115 0.1934 -0.0122 0.0119  0.0719  160 LEU   A CB  
3530 C  CB  T LEU   A 160 ? 0.2237 0.2399 0.2572 -0.0017 0.0216  0.0347  160 LEU   A CB  
3531 C  CG  A LEU   A 160 ? 0.1858 0.2227 0.2525 0.0018  0.0232  0.0540  160 LEU   A CG  
3532 C  CG  B LEU   A 160 ? 0.1498 0.2209 0.2107 -0.0233 0.0199  0.0634  160 LEU   A CG  
3533 C  CG  T LEU   A 160 ? 0.2315 0.2474 0.2658 -0.0061 0.0270  0.0311  160 LEU   A CG  
3534 C  CD1 A LEU   A 160 ? 0.1934 0.2254 0.2652 -0.0017 0.0232  0.0447  160 LEU   A CD1 
3535 C  CD1 B LEU   A 160 ? 0.1595 0.2282 0.2301 -0.0219 0.0208  0.0619  160 LEU   A CD1 
3536 C  CD1 T LEU   A 160 ? 0.2368 0.2514 0.2715 -0.0079 0.0274  0.0280  160 LEU   A CD1 
3537 C  CD2 A LEU   A 160 ? 0.1903 0.2242 0.2604 0.0026  0.0304  0.0479  160 LEU   A CD2 
3538 C  CD2 B LEU   A 160 ? 0.1526 0.2229 0.2189 -0.0291 0.0269  0.0528  160 LEU   A CD2 
3539 C  CD2 T LEU   A 160 ? 0.2336 0.2490 0.2671 -0.0080 0.0329  0.0291  160 LEU   A CD2 
3572 N  N   A TYR   A 161 ? 0.1482 0.2244 0.2367 -0.0022 0.0273  0.0761  161 TYR   A N   
3573 N  N   B TYR   A 161 ? 0.1342 0.2252 0.1955 0.0078  0.0270  0.0749  161 TYR   A N   
3574 C  CA  A TYR   A 161 ? 0.1470 0.2371 0.2346 -0.0052 0.0256  0.0723  161 TYR   A CA  
3575 C  CA  B TYR   A 161 ? 0.1489 0.2316 0.1990 0.0079  0.0270  0.0757  161 TYR   A CA  
3576 C  C   A TYR   A 161 ? 0.1466 0.2678 0.2434 -0.0092 0.0224  0.0770  161 TYR   A C   
3577 C  C   B TYR   A 161 ? 0.1555 0.2508 0.2182 0.0049  0.0287  0.0722  161 TYR   A C   
3578 O  O   A TYR   A 161 ? 0.1443 0.2704 0.2272 -0.0130 0.0210  0.0755  161 TYR   A O   
3579 O  O   B TYR   A 161 ? 0.1514 0.2495 0.2058 -0.0038 0.0368  0.0752  161 TYR   A O   
3580 C  CB  A TYR   A 161 ? 0.1563 0.2265 0.2382 -0.0060 0.0318  0.0691  161 TYR   A CB  
3581 C  CB  B TYR   A 161 ? 0.1636 0.2212 0.1947 0.0075  0.0270  0.0726  161 TYR   A CB  
3582 C  CG  A TYR   A 161 ? 0.1511 0.2089 0.2351 -0.0013 0.0220  0.0530  161 TYR   A CG  
3583 C  CG  B TYR   A 161 ? 0.1674 0.2057 0.1961 0.0070  0.0291  0.0575  161 TYR   A CG  
3584 C  CD1 A TYR   A 161 ? 0.1462 0.1973 0.2415 -0.0012 0.0170  0.0413  161 TYR   A CD1 
3585 C  CD1 B TYR   A 161 ? 0.1694 0.1945 0.2045 0.0043  0.0268  0.0469  161 TYR   A CD1 
3586 C  CD2 A TYR   A 161 ? 0.1487 0.2018 0.2300 0.0070  0.0161  0.0462  161 TYR   A CD2 
3587 C  CD2 B TYR   A 161 ? 0.1702 0.2000 0.2008 0.0096  0.0329  0.0557  161 TYR   A CD2 
3588 C  CE1 A TYR   A 161 ? 0.1446 0.1837 0.2231 0.0030  -0.0004 0.0387  161 TYR   A CE1 
3589 C  CE1 B TYR   A 161 ? 0.1754 0.1924 0.2112 0.0050  0.0215  0.0439  161 TYR   A CE1 
3590 C  CE2 A TYR   A 161 ? 0.1504 0.1876 0.2236 0.0004  0.0068  0.0481  161 TYR   A CE2 
3591 C  CE2 B TYR   A 161 ? 0.1755 0.1939 0.2101 0.0015  0.0307  0.0544  161 TYR   A CE2 
3592 C  CZ  A TYR   A 161 ? 0.1543 0.1777 0.2139 -0.0037 -0.0011 0.0442  161 TYR   A CZ  
3593 C  CZ  B TYR   A 161 ? 0.1848 0.1905 0.2208 0.0003  0.0262  0.0487  161 TYR   A CZ  
3594 O  OH  A TYR   A 161 ? 0.1653 0.1630 0.2106 -0.0086 -0.0030 0.0486  161 TYR   A OH  
3595 O  OH  B TYR   A 161 ? 0.1985 0.1895 0.2500 -0.0014 0.0198  0.0431  161 TYR   A OH  
3614 N  N   A ASP   A 162 ? 0.1418 0.2938 0.2567 -0.0098 0.0327  0.0886  162 ASP   A N   
3615 N  N   B ASP   A 162 ? 0.1651 0.2700 0.2405 0.0059  0.0311  0.0701  162 ASP   A N   
3616 C  CA  A ASP   A 162 ? 0.1382 0.3270 0.2723 -0.0113 0.0405  0.0765  162 ASP   A CA  
3617 C  CA  B ASP   A 162 ? 0.1765 0.2942 0.2550 -0.0007 0.0352  0.0610  162 ASP   A CA  
3618 C  C   A ASP   A 162 ? 0.1249 0.3418 0.2577 -0.0180 0.0263  0.0799  162 ASP   A C   
3619 C  C   B ASP   A 162 ? 0.1779 0.3032 0.2489 -0.0105 0.0356  0.0712  162 ASP   A C   
3620 O  O   A ASP   A 162 ? 0.1276 0.3469 0.2632 -0.0166 0.0194  0.0689  162 ASP   A O   
3621 O  O   B ASP   A 162 ? 0.1792 0.3019 0.2517 -0.0175 0.0399  0.0716  162 ASP   A O   
3622 C  CB  A ASP   A 162 ? 0.1501 0.3457 0.3136 -0.0032 0.0527  0.0518  162 ASP   A CB  
3623 C  CB  B ASP   A 162 ? 0.1861 0.3107 0.2773 0.0038  0.0395  0.0380  162 ASP   A CB  
3624 C  CG  A ASP   A 162 ? 0.1637 0.3641 0.3487 0.0019  0.0625  0.0392  162 ASP   A CG  
3625 C  CG  B ASP   A 162 ? 0.1966 0.3274 0.2978 0.0056  0.0431  0.0241  162 ASP   A CG  
3626 O  OD1 A ASP   A 162 ? 0.1717 0.3682 0.3533 -0.0118 0.0678  0.0422  162 ASP   A OD1 
3627 O  OD1 B ASP   A 162 ? 0.2050 0.3306 0.2989 0.0000  0.0439  0.0261  162 ASP   A OD1 
3628 O  OD2 A ASP   A 162 ? 0.1736 0.3736 0.3770 0.0173  0.0584  0.0292  162 ASP   A OD2 
3629 O  OD2 B ASP   A 162 ? 0.2019 0.3387 0.3146 0.0133  0.0404  0.0147  162 ASP   A OD2 
3638 N  N   A LYS   A 163 ? 0.1348 0.3568 0.2549 -0.0121 0.0099  0.0775  163 LYS   A N   
3639 N  N   B LYS   A 163 ? 0.1857 0.3139 0.2553 -0.0072 0.0196  0.0701  163 LYS   A N   
3640 C  CA  A LYS   A 163 ? 0.1520 0.3685 0.2573 -0.0110 0.0013  0.0727  163 LYS   A CA  
3641 C  CA  B LYS   A 163 ? 0.1973 0.3252 0.2628 -0.0044 0.0078  0.0656  163 LYS   A CA  
3642 C  C   A LYS   A 163 ? 0.1485 0.3593 0.2228 -0.0188 0.0095  0.0768  163 LYS   A C   
3643 C  C   B LYS   A 163 ? 0.1860 0.3202 0.2445 -0.0051 0.0099  0.0623  163 LYS   A C   
3644 O  O   A LYS   A 163 ? 0.1467 0.3660 0.2052 -0.0274 0.0152  0.0719  163 LYS   A O   
3645 O  O   B LYS   A 163 ? 0.1839 0.3269 0.2347 -0.0074 0.0098  0.0620  163 LYS   A O   
3646 C  CB  A LYS   A 163 ? 0.1884 0.3884 0.3001 0.0039  -0.0106 0.0663  163 LYS   A CB  
3647 C  CB  B LYS   A 163 ? 0.2260 0.3420 0.3013 0.0021  -0.0032 0.0583  163 LYS   A CB  
3648 C  CG  A LYS   A 163 ? 0.2245 0.4061 0.3589 0.0070  -0.0083 0.0573  163 LYS   A CG  
3649 C  CG  B LYS   A 163 ? 0.2543 0.3579 0.3470 0.0038  -0.0099 0.0513  163 LYS   A CG  
3650 C  CD  A LYS   A 163 ? 0.2606 0.4214 0.4233 0.0066  -0.0095 0.0490  163 LYS   A CD  
3651 C  CD  B LYS   A 163 ? 0.2795 0.3716 0.3937 0.0036  -0.0147 0.0424  163 LYS   A CD  
3652 C  CE  A LYS   A 163 ? 0.2961 0.4322 0.4742 0.0035  -0.0053 0.0470  163 LYS   A CE  
3653 C  CE  B LYS   A 163 ? 0.2991 0.3811 0.4319 0.0030  -0.0144 0.0371  163 LYS   A CE  
3654 N  NZ  A LYS   A 163 ? 0.3074 0.4384 0.5050 0.0011  -0.0026 0.0470  163 LYS   A NZ  
3655 N  NZ  B LYS   A 163 ? 0.3084 0.3860 0.4527 0.0016  -0.0134 0.0343  163 LYS   A NZ  
3682 N  N   A LEU   A 164 ? 0.1351 0.3350 0.2018 -0.0253 0.0068  0.0759  164 LEU   A N   
3683 N  N   B LEU   A 164 ? 0.1736 0.3046 0.2305 -0.0061 0.0125  0.0556  164 LEU   A N   
3684 C  CA  A LEU   A 164 ? 0.1452 0.3102 0.1910 -0.0361 0.0169  0.0695  164 LEU   A CA  
3685 C  CA  B LEU   A 164 ? 0.1699 0.2886 0.2121 -0.0103 0.0200  0.0464  164 LEU   A CA  
3686 C  C   A LEU   A 164 ? 0.1555 0.3060 0.1838 -0.0388 0.0113  0.0621  164 LEU   A C   
3687 C  C   B LEU   A 164 ? 0.1725 0.2869 0.2131 -0.0192 0.0177  0.0425  164 LEU   A C   
3688 O  O   A LEU   A 164 ? 0.1579 0.3095 0.1895 -0.0416 0.0333  0.0520  164 LEU   A O   
3689 O  O   B LEU   A 164 ? 0.1734 0.2872 0.2064 -0.0285 0.0237  0.0442  164 LEU   A O   
3690 C  CB  A LEU   A 164 ? 0.1450 0.2914 0.1884 -0.0377 0.0266  0.0690  164 LEU   A CB  
3691 C  CB  B LEU   A 164 ? 0.1681 0.2748 0.1980 -0.0051 0.0289  0.0404  164 LEU   A CB  
3692 C  CG  A LEU   A 164 ? 0.1510 0.2781 0.1970 -0.0307 0.0128  0.0681  164 LEU   A CG  
3693 C  CG  B LEU   A 164 ? 0.1706 0.2642 0.1991 0.0015  0.0264  0.0355  164 LEU   A CG  
3694 C  CD1 A LEU   A 164 ? 0.1360 0.2676 0.1961 -0.0239 -0.0038 0.0776  164 LEU   A CD1 
3695 C  CD1 B LEU   A 164 ? 0.1657 0.2610 0.2038 0.0058  0.0250  0.0319  164 LEU   A CD1 
3696 C  CD2 A LEU   A 164 ? 0.1660 0.2794 0.2020 -0.0344 0.0232  0.0605  164 LEU   A CD2 
3697 C  CD2 B LEU   A 164 ? 0.1732 0.2607 0.1915 -0.0028 0.0339  0.0324  164 LEU   A CD2 
3720 N  N   A VAL   A 165 ? 0.1516 0.2956 0.1660 -0.0373 0.0069  0.0676  165 VAL   A N   
3721 N  N   B VAL   A 165 ? 0.1693 0.2842 0.2144 -0.0178 0.0144  0.0390  165 VAL   A N   
3722 C  CA  A VAL   A 165 ? 0.1637 0.2889 0.1511 -0.0431 0.0090  0.0710  165 VAL   A CA  
3723 C  CA  B VAL   A 165 ? 0.1733 0.2857 0.2132 -0.0155 0.0134  0.0364  165 VAL   A CA  
3724 C  C   A VAL   A 165 ? 0.1572 0.3073 0.1553 -0.0353 0.0103  0.0660  165 VAL   A C   
3725 C  C   B VAL   A 165 ? 0.1642 0.2909 0.2076 -0.0151 0.0152  0.0318  165 VAL   A C   
3726 O  O   A VAL   A 165 ? 0.1536 0.3091 0.1448 -0.0352 0.0208  0.0618  165 VAL   A O   
3727 O  O   B VAL   A 165 ? 0.1601 0.2917 0.1890 -0.0148 0.0191  0.0304  165 VAL   A O   
3728 C  CB  A VAL   A 165 ? 0.1870 0.2740 0.1585 -0.0495 0.0104  0.0618  165 VAL   A CB  
3729 C  CB  B VAL   A 165 ? 0.1864 0.2851 0.2198 -0.0131 0.0097  0.0303  165 VAL   A CB  
3730 C  CG1 A VAL   A 165 ? 0.1917 0.2729 0.1551 -0.0540 0.0204  0.0464  165 VAL   A CG1 
3731 C  CG1 B VAL   A 165 ? 0.1886 0.2873 0.2235 -0.0124 0.0105  0.0247  165 VAL   A CG1 
3732 C  CG2 A VAL   A 165 ? 0.1964 0.2717 0.1678 -0.0466 -0.0005 0.0712  165 VAL   A CG2 
3733 C  CG2 B VAL   A 165 ? 0.1922 0.2848 0.2265 -0.0129 0.0061  0.0290  165 VAL   A CG2 
3752 N  N   A SER   A 166 ? 0.1496 0.3205 0.1760 -0.0284 0.0137  0.0535  166 SER   A N   
3753 N  N   B SER   A 166 ? 0.1558 0.2948 0.2260 -0.0172 0.0221  0.0310  166 SER   A N   
3754 C  CA  A SER   A 166 ? 0.1535 0.3333 0.1967 -0.0274 0.0164  0.0490  166 SER   A CA  
3755 C  CA  B SER   A 166 ? 0.1582 0.2995 0.2353 -0.0220 0.0231  0.0308  166 SER   A CA  
3756 C  C   A SER   A 166 ? 0.1554 0.3443 0.2090 -0.0226 0.0099  0.0432  166 SER   A C   
3757 C  C   B SER   A 166 ? 0.1704 0.3058 0.2280 -0.0347 0.0265  0.0332  166 SER   A C   
3758 O  O   A SER   A 166 ? 0.1679 0.3605 0.2323 -0.0350 0.0300  0.0193  166 SER   A O   
3759 O  O   B SER   A 166 ? 0.1773 0.3127 0.2322 -0.0481 0.0406  0.0247  166 SER   A O   
3760 C  CB  A SER   A 166 ? 0.1634 0.3338 0.2135 -0.0224 0.0153  0.0527  166 SER   A CB  
3761 C  CB  B SER   A 166 ? 0.1547 0.2971 0.2545 -0.0143 0.0148  0.0306  166 SER   A CB  
3762 O  OG  A SER   A 166 ? 0.1750 0.3349 0.2267 -0.0162 0.0182  0.0615  166 SER   A OG  
3763 O  OG  B SER   A 166 ? 0.1566 0.2962 0.2684 -0.0066 0.0029  0.0343  166 SER   A OG  
3774 N  N   A SER   A 167 ? 0.1558 0.3334 0.1728 -0.0032 -0.0051 0.0635  167 SER   A N   
3775 N  N   B SER   A 167 ? 0.1813 0.3045 0.2352 -0.0294 0.0202  0.0399  167 SER   A N   
3776 C  CA  A SER   A 167 ? 0.1742 0.3255 0.1837 0.0011  -0.0085 0.0480  167 SER   A CA  
3777 C  CA  B SER   A 167 ? 0.1929 0.3057 0.2440 -0.0209 0.0202  0.0404  167 SER   A CA  
3778 C  C   A SER   A 167 ? 0.1864 0.3184 0.1977 0.0083  0.0097  0.0440  167 SER   A C   
3779 C  C   B SER   A 167 ? 0.1873 0.3128 0.2437 -0.0057 0.0270  0.0397  167 SER   A C   
3780 O  O   A SER   A 167 ? 0.2055 0.3296 0.2118 0.0140  -0.0059 0.0340  167 SER   A O   
3781 O  O   B SER   A 167 ? 0.1994 0.3192 0.2546 0.0030  0.0120  0.0328  167 SER   A O   
3782 C  CB  A SER   A 167 ? 0.1697 0.3226 0.1886 -0.0039 -0.0018 0.0402  167 SER   A CB  
3783 C  CB  B SER   A 167 ? 0.2094 0.3032 0.2629 -0.0216 0.0121  0.0318  167 SER   A CB  
3784 O  OG  A SER   A 167 ? 0.1669 0.3202 0.2098 -0.0149 0.0178  0.0339  167 SER   A OG  
3785 O  OG  B SER   A 167 ? 0.2220 0.3042 0.2799 -0.0218 0.0059  0.0297  167 SER   A OG  
3796 N  N   A PHE   A 168 ? 0.1750 0.2993 0.1981 0.0085  0.0211  0.0479  168 PHE   A N   
3797 N  N   B PHE   A 168 ? 0.1735 0.3128 0.2371 -0.0003 0.0352  0.0440  168 PHE   A N   
3798 C  CA  A PHE   A 168 ? 0.1804 0.2937 0.2238 0.0070  0.0232  0.0402  168 PHE   A CA  
3799 C  CA  B PHE   A 168 ? 0.1672 0.3128 0.2326 0.0010  0.0422  0.0426  168 PHE   A CA  
3800 C  C   A PHE   A 168 ? 0.1950 0.2969 0.2705 0.0074  0.0498  0.0291  168 PHE   A C   
3801 C  C   B PHE   A 168 ? 0.1742 0.3195 0.2457 0.0002  0.0526  0.0330  168 PHE   A C   
3802 O  O   A PHE   A 168 ? 0.2055 0.2996 0.3136 -0.0025 0.0640  0.0396  168 PHE   A O   
3803 O  O   B PHE   A 168 ? 0.1573 0.3203 0.2271 -0.0009 0.0643  0.0309  168 PHE   A O   
3804 C  CB  A PHE   A 168 ? 0.1783 0.2892 0.2020 0.0015  0.0084  0.0342  168 PHE   A CB  
3805 C  CB  B PHE   A 168 ? 0.1648 0.3071 0.2288 -0.0020 0.0362  0.0475  168 PHE   A CB  
3806 C  CG  A PHE   A 168 ? 0.1734 0.2876 0.1870 -0.0044 -0.0050 0.0248  168 PHE   A CG  
3807 C  CG  B PHE   A 168 ? 0.1639 0.3000 0.2311 -0.0006 0.0244  0.0586  168 PHE   A CG  
3808 C  CD1 A PHE   A 168 ? 0.1756 0.2914 0.1907 -0.0124 -0.0055 0.0224  168 PHE   A CD1 
3809 C  CD1 B PHE   A 168 ? 0.1666 0.2987 0.2373 -0.0009 0.0273  0.0670  168 PHE   A CD1 
3810 C  CD2 A PHE   A 168 ? 0.1678 0.2837 0.1904 -0.0084 -0.0064 0.0182  168 PHE   A CD2 
3811 C  CD2 B PHE   A 168 ? 0.1618 0.2941 0.2298 0.0008  0.0122  0.0680  168 PHE   A CD2 
3812 C  CE1 A PHE   A 168 ? 0.1658 0.2860 0.1911 -0.0178 -0.0081 0.0160  168 PHE   A CE1 
3813 C  CE1 B PHE   A 168 ? 0.1637 0.2937 0.2372 -0.0034 0.0254  0.0794  168 PHE   A CE1 
3814 C  CE2 A PHE   A 168 ? 0.1685 0.2782 0.1996 -0.0177 -0.0074 0.0163  168 PHE   A CE2 
3815 C  CE2 B PHE   A 168 ? 0.1596 0.2888 0.2258 -0.0021 0.0040  0.0821  168 PHE   A CE2 
3816 C  CZ  A PHE   A 168 ? 0.1651 0.2816 0.1966 -0.0196 -0.0093 0.0148  168 PHE   A CZ  
3817 C  CZ  B PHE   A 168 ? 0.1623 0.2895 0.2323 -0.0070 0.0167  0.0810  168 PHE   A CZ  
3836 N  N   A LEU   A 169 ? 0.2208 0.2984 0.2984 0.0050  0.0468  0.0051  169 LEU   A N   
3837 N  N   B LEU   A 169 ? 0.1987 0.3264 0.2842 0.0065  0.0427  0.0255  169 LEU   A N   
3838 C  CA  A LEU   A 169 ? 0.2485 0.2997 0.3314 0.0030  0.0374  0.0031  169 LEU   A CA  
3839 C  CA  B LEU   A 169 ? 0.2288 0.3374 0.3176 0.0090  0.0288  0.0139  169 LEU   A CA  
3840 C  C   A LEU   A 169 ? 0.2411 0.2915 0.3395 -0.0007 0.0420  0.0240  169 LEU   A C   
3841 C  C   B LEU   A 169 ? 0.2458 0.3438 0.3408 0.0109  0.0244  -0.0005 169 LEU   A C   
3842 O  O   A LEU   A 169 ? 0.2425 0.2934 0.3418 0.0082  0.0366  0.0177  169 LEU   A O   
3843 O  O   B LEU   A 169 ? 0.2501 0.3468 0.3504 0.0125  0.0148  -0.0065 169 LEU   A O   
3844 C  CB  A LEU   A 169 ? 0.2784 0.3110 0.3377 0.0022  0.0365  -0.0214 169 LEU   A CB  
3845 C  CB  B LEU   A 169 ? 0.2397 0.3428 0.3232 0.0116  0.0194  0.0180  169 LEU   A CB  
3846 C  CG  A LEU   A 169 ? 0.3052 0.3223 0.3493 -0.0024 0.0357  -0.0514 169 LEU   A CG  
3847 C  CG  B LEU   A 169 ? 0.2488 0.3491 0.3193 0.0126  0.0123  0.0207  169 LEU   A CG  
3848 C  CD1 A LEU   A 169 ? 0.3150 0.3247 0.3540 -0.0034 0.0313  -0.0631 169 LEU   A CD1 
3849 C  CD1 B LEU   A 169 ? 0.2524 0.3534 0.3190 0.0154  0.0143  0.0173  169 LEU   A CD1 
3850 C  CD2 A LEU   A 169 ? 0.3138 0.3281 0.3483 -0.0075 0.0378  -0.0620 169 LEU   A CD2 
3851 C  CD2 B LEU   A 169 ? 0.2535 0.3504 0.3207 0.0101  0.0064  0.0247  169 LEU   A CD2 
3852 O  OXT A LEU   A 169 ? 0.2290 0.2899 0.3335 -0.0094 0.0541  0.0391  169 LEU   A OXT 
3853 O  OXT B LEU   A 169 ? 0.2575 0.3474 0.3524 0.0071  0.0258  -0.0036 169 LEU   A OXT 
3876 N  N   A SER   B 1   ? 0.3773 0.3424 0.3248 -0.1015 -0.0670 0.0498  1   SER   B N   
3877 N  N   B SER   B 1   ? 0.3381 0.3283 0.3307 -0.0887 -0.0490 0.0329  1   SER   B N   
3878 C  CA  A SER   B 1   ? 0.3713 0.3495 0.3405 -0.1063 -0.0720 0.0404  1   SER   B CA  
3879 C  CA  B SER   B 1   ? 0.3325 0.3322 0.3351 -0.0920 -0.0523 0.0302  1   SER   B CA  
3880 C  C   A SER   B 1   ? 0.3482 0.3534 0.3288 -0.1096 -0.0796 0.0553  1   SER   B C   
3881 C  C   B SER   B 1   ? 0.3152 0.3335 0.3212 -0.0939 -0.0617 0.0481  1   SER   B C   
3882 O  O   A SER   B 1   ? 0.3570 0.3568 0.3101 -0.1037 -0.0735 0.0540  1   SER   B O   
3883 O  O   B SER   B 1   ? 0.3203 0.3356 0.3107 -0.0901 -0.0576 0.0435  1   SER   B O   
3884 C  CB  A SER   B 1   ? 0.3842 0.3500 0.3548 -0.1069 -0.0661 0.0195  1   SER   B CB  
3885 C  CB  B SER   B 1   ? 0.3406 0.3324 0.3434 -0.0923 -0.0441 0.0122  1   SER   B CB  
3886 O  OG  A SER   B 1   ? 0.3969 0.3574 0.4010 -0.1050 -0.0610 0.0105  1   SER   B OG  
3887 O  OG  B SER   B 1   ? 0.3483 0.3370 0.3726 -0.0923 -0.0404 0.0028  1   SER   B OG  
3902 N  N   A MET   B 2   ? 0.3226 0.3514 0.3333 -0.1118 -0.0828 0.0866  2   MET   B N   
3903 N  N   B MET   B 2   ? 0.2963 0.3310 0.3139 -0.0953 -0.0692 0.0822  2   MET   B N   
3904 C  CA  A MET   B 2   ? 0.3056 0.3550 0.3546 -0.0954 -0.0827 0.1063  2   MET   B CA  
3905 C  CA  B MET   B 2   ? 0.2822 0.3320 0.3151 -0.0846 -0.0768 0.1092  2   MET   B CA  
3906 C  C   A MET   B 2   ? 0.2703 0.3382 0.3207 -0.0787 -0.0948 0.1318  2   MET   B C   
3907 C  C   B MET   B 2   ? 0.2586 0.3216 0.3006 -0.0798 -0.0884 0.1310  2   MET   B C   
3908 O  O   A MET   B 2   ? 0.2681 0.3521 0.3307 -0.0632 -0.1047 0.1312  2   MET   B O   
3909 O  O   B MET   B 2   ? 0.2542 0.3261 0.3019 -0.0748 -0.0944 0.1308  2   MET   B O   
3910 C  CB  A MET   B 2   ? 0.3341 0.3843 0.4423 -0.0793 -0.0605 0.0830  2   MET   B CB  
3911 C  CB  B MET   B 2   ? 0.2984 0.3497 0.3519 -0.0677 -0.0668 0.1034  2   MET   B CB  
3912 C  CG  A MET   B 2   ? 0.3609 0.4110 0.5197 -0.0613 -0.0375 0.0673  2   MET   B CG  
3913 C  CG  B MET   B 2   ? 0.3136 0.3659 0.3748 -0.0493 -0.0569 0.1088  2   MET   B CG  
3914 S  SD  A MET   B 2   ? 0.3864 0.4364 0.5982 -0.0444 -0.0215 0.0555  2   MET   B SD  
3915 S  SD  B MET   B 2   ? 0.3286 0.3831 0.3944 -0.0314 -0.0520 0.1151  2   MET   B SD  
3916 C  CE  A MET   B 2   ? 0.3902 0.4424 0.6034 -0.0435 -0.0170 0.0560  2   MET   B CE  
3917 C  CE  B MET   B 2   ? 0.3321 0.3871 0.4018 -0.0299 -0.0490 0.1080  2   MET   B CE  
3936 N  N   . VAL   B 3   ? 0.2410 0.3063 0.2976 -0.0811 -0.0918 0.1425  3   VAL   B N   
3937 C  CA  . VAL   B 3   ? 0.2234 0.2705 0.2986 -0.0741 -0.0849 0.1287  3   VAL   B CA  
3938 C  C   . VAL   B 3   ? 0.2015 0.2633 0.2621 -0.0665 -0.0735 0.1141  3   VAL   B C   
3939 O  O   . VAL   B 3   ? 0.1985 0.2828 0.2679 -0.0705 -0.0773 0.1220  3   VAL   B O   
3940 C  CB  . VAL   B 3   ? 0.2406 0.2594 0.3547 -0.0735 -0.0725 0.1073  3   VAL   B CB  
3941 C  CG1 . VAL   B 3   ? 0.2491 0.2479 0.3784 -0.0812 -0.0688 0.1032  3   VAL   B CG1 
3942 C  CG2 . VAL   B 3   ? 0.2409 0.2631 0.3715 -0.0701 -0.0587 0.1124  3   VAL   B CG2 
3953 N  N   . ASN   B 4   ? 0.1914 0.2334 0.2280 -0.0643 -0.0576 0.0849  4   ASN   B N   
3954 C  CA  . ASN   B 4   ? 0.1942 0.2259 0.1881 -0.0630 -0.0499 0.0515  4   ASN   B CA  
3955 C  C   . ASN   B 4   ? 0.1974 0.2414 0.1785 -0.0635 -0.0374 0.0386  4   ASN   B C   
3956 O  O   . ASN   B 4   ? 0.1984 0.2419 0.2002 -0.0605 -0.0343 0.0173  4   ASN   B O   
3957 C  CB  . ASN   B 4   ? 0.1974 0.2185 0.1835 -0.0532 -0.0610 0.0355  4   ASN   B CB  
3958 C  CG  . ASN   B 4   ? 0.1979 0.1999 0.1756 -0.0562 -0.0620 0.0335  4   ASN   B CG  
3959 O  OD1 . ASN   B 4   ? 0.2081 0.1823 0.1738 -0.0505 -0.0579 0.0355  4   ASN   B OD1 
3960 N  ND2 . ASN   B 4   ? 0.2183 0.2086 0.1792 -0.0351 -0.0379 0.0346  4   ASN   B ND2 
3967 N  N   . SER   B 5   ? 0.2105 0.2622 0.1876 -0.0674 -0.0295 0.0374  5   SER   B N   
3968 C  CA  . SER   B 5   ? 0.2384 0.2949 0.2057 -0.0595 -0.0201 0.0407  5   SER   B CA  
3969 C  C   . SER   B 5   ? 0.2621 0.3053 0.2418 -0.0772 0.0085  0.0363  5   SER   B C   
3970 O  O   . SER   B 5   ? 0.2822 0.2986 0.3119 -0.0688 0.0470  0.0289  5   SER   B O   
3971 C  CB  . SER   B 5   ? 0.2560 0.3096 0.2345 -0.0447 -0.0129 0.0545  5   SER   B CB  
3972 O  OG  . SER   B 5   ? 0.2759 0.3315 0.2879 -0.0319 -0.0088 0.0582  5   SER   B OG  
3978 N  N   . PHE   B 6   ? 0.2827 0.3278 0.2235 -0.0860 0.0198  0.0404  6   PHE   B N   
3979 C  CA  . PHE   B 6   ? 0.2969 0.3376 0.2011 -0.1062 0.0294  0.0230  6   PHE   B CA  
3980 C  C   . PHE   B 6   ? 0.3524 0.3800 0.2510 -0.1168 0.0614  -0.0103 6   PHE   B C   
3981 O  O   . PHE   B 6   ? 0.3660 0.4113 0.2835 -0.1061 0.0530  -0.0250 6   PHE   B O   
3982 C  CB  . PHE   B 6   ? 0.2649 0.3115 0.1753 -0.0958 0.0060  0.0209  6   PHE   B CB  
3983 C  CG  . PHE   B 6   ? 0.2338 0.2762 0.1703 -0.0882 -0.0128 0.0257  6   PHE   B CG  
3984 C  CD1 . PHE   B 6   ? 0.2361 0.2468 0.1588 -0.0826 -0.0189 0.0228  6   PHE   B CD1 
3985 C  CD2 . PHE   B 6   ? 0.2124 0.2730 0.1715 -0.0719 -0.0160 0.0530  6   PHE   B CD2 
3986 C  CE1 . PHE   B 6   ? 0.2264 0.2253 0.1809 -0.0725 -0.0284 0.0199  6   PHE   B CE1 
3987 C  CE2 . PHE   B 6   ? 0.2114 0.2580 0.2064 -0.0639 -0.0104 0.0506  6   PHE   B CE2 
3988 C  CZ  . PHE   B 6   ? 0.2141 0.2331 0.1959 -0.0650 -0.0220 0.0321  6   PHE   B CZ  
3998 N  N   . SER   B 7   ? 0.3935 0.3747 0.2799 -0.1424 0.0990  -0.0369 7   SER   B N   
3999 C  CA  . SER   B 7   ? 0.4352 0.3968 0.3443 -0.1453 0.1292  -0.0490 7   SER   B CA  
4000 C  C   . SER   B 7   ? 0.4329 0.3681 0.3198 -0.1496 0.1443  -0.0718 7   SER   B C   
4001 O  O   . SER   B 7   ? 0.4413 0.3619 0.3329 -0.1546 0.1387  -0.0874 7   SER   B O   
4002 C  CB  . SER   B 7   ? 0.4673 0.4384 0.4271 -0.1442 0.1482  -0.0352 7   SER   B CB  
4003 O  OG  . SER   B 7   ? 0.4770 0.4551 0.4918 -0.1444 0.1536  -0.0235 7   SER   B OG  
4009 N  N   . GLY   B 8   ? 0.4289 0.3532 0.3148 -0.1356 0.1543  -0.0794 8   GLY   B N   
4010 C  CA  . GLY   B 8   ? 0.4150 0.3322 0.3098 -0.1241 0.1526  -0.0850 8   GLY   B CA  
4011 C  C   . GLY   B 8   ? 0.3916 0.2993 0.2956 -0.1174 0.1502  -0.0832 8   GLY   B C   
4012 O  O   . GLY   B 8   ? 0.4015 0.3062 0.3350 -0.1035 0.1504  -0.0928 8   GLY   B O   
4016 N  N   . TYR   B 9   ? 0.3707 0.2711 0.2683 -0.1052 0.1201  -0.0923 9   TYR   B N   
4017 C  CA  . TYR   B 9   ? 0.3497 0.2396 0.2373 -0.0911 0.0883  -0.0762 9   TYR   B CA  
4018 C  C   . TYR   B 9   ? 0.3463 0.2360 0.2302 -0.0830 0.0620  -0.0639 9   TYR   B C   
4019 O  O   . TYR   B 9   ? 0.3567 0.2548 0.2688 -0.0829 0.0654  -0.0469 9   TYR   B O   
4020 C  CB  . TYR   B 9   ? 0.3364 0.2153 0.2516 -0.0827 0.0786  -0.0736 9   TYR   B CB  
4021 C  CG  . TYR   B 9   ? 0.3212 0.1995 0.2527 -0.0875 0.0686  -0.0713 9   TYR   B CG  
4022 C  CD1 . TYR   B 9   ? 0.3200 0.2008 0.2694 -0.1001 0.0712  -0.0595 9   TYR   B CD1 
4023 C  CD2 . TYR   B 9   ? 0.3084 0.2004 0.2404 -0.0814 0.0540  -0.0693 9   TYR   B CD2 
4024 C  CE1 . TYR   B 9   ? 0.3166 0.2116 0.2657 -0.0996 0.0703  -0.0709 9   TYR   B CE1 
4025 C  CE2 . TYR   B 9   ? 0.3075 0.2007 0.2459 -0.0794 0.0564  -0.0651 9   TYR   B CE2 
4026 C  CZ  . TYR   B 9   ? 0.3098 0.2126 0.2543 -0.0905 0.0663  -0.0756 9   TYR   B CZ  
4027 O  OH  . TYR   B 9   ? 0.3075 0.2206 0.2714 -0.0985 0.0645  -0.0865 9   TYR   B OH  
4037 N  N   . LEU   B 10  ? 0.3293 0.2137 0.2201 -0.0830 0.0384  -0.0561 10  LEU   B N   
4038 C  CA  . LEU   B 10  ? 0.3284 0.2089 0.2136 -0.0919 -0.0022 -0.0479 10  LEU   B CA  
4039 C  C   . LEU   B 10  ? 0.3109 0.2116 0.2186 -0.0916 -0.0216 -0.0406 10  LEU   B C   
4040 O  O   . LEU   B 10  ? 0.2929 0.2167 0.2262 -0.0818 -0.0172 -0.0282 10  LEU   B O   
4041 C  CB  . LEU   B 10  ? 0.3486 0.2049 0.2355 -0.0941 -0.0231 -0.0253 10  LEU   B CB  
4042 C  CG  . LEU   B 10  ? 0.3718 0.2127 0.2701 -0.0861 -0.0519 -0.0074 10  LEU   B CG  
4043 C  CD1 . LEU   B 10  ? 0.3889 0.2195 0.2889 -0.0781 -0.0481 -0.0033 10  LEU   B CD1 
4044 C  CD2 . LEU   B 10  ? 0.3797 0.2193 0.3031 -0.0825 -0.0504 0.0150  10  LEU   B CD2 
4056 N  N   . LYS   B 11  ? 0.3226 0.2371 0.2274 -0.0872 -0.0343 -0.0233 11  LYS   B N   
4057 C  CA  . LYS   B 11  ? 0.3373 0.2638 0.2662 -0.0744 -0.0446 -0.0305 11  LYS   B CA  
4058 C  C   . LYS   B 11  ? 0.3131 0.2389 0.2690 -0.0920 -0.0403 -0.0416 11  LYS   B C   
4059 O  O   . LYS   B 11  ? 0.3271 0.2560 0.3055 -0.1064 -0.0379 -0.0719 11  LYS   B O   
4060 C  CB  . LYS   B 11  ? 0.3743 0.3129 0.3432 -0.0466 -0.0481 -0.0337 11  LYS   B CB  
4061 C  CG  . LYS   B 11  ? 0.4062 0.3458 0.4188 -0.0285 -0.0475 -0.0361 11  LYS   B CG  
4062 C  CD  . LYS   B 11  ? 0.4300 0.3676 0.4821 -0.0183 -0.0473 -0.0389 11  LYS   B CD  
4063 C  CE  . LYS   B 11  ? 0.4473 0.3835 0.5279 -0.0150 -0.0494 -0.0415 11  LYS   B CE  
4064 N  NZ  . LYS   B 11  ? 0.4567 0.3925 0.5501 -0.0147 -0.0535 -0.0420 11  LYS   B NZ  
4078 N  N   . LEU   B 12  ? 0.2755 0.2129 0.2701 -0.0790 -0.0393 -0.0353 12  LEU   B N   
4079 C  CA  . LEU   B 12  ? 0.2558 0.1923 0.2795 -0.0636 -0.0340 -0.0284 12  LEU   B CA  
4080 C  C   . LEU   B 12  ? 0.2405 0.1947 0.2839 -0.0675 -0.0484 -0.0218 12  LEU   B C   
4081 O  O   . LEU   B 12  ? 0.2384 0.1971 0.3025 -0.0773 -0.0621 -0.0162 12  LEU   B O   
4082 C  CB  . LEU   B 12  ? 0.2537 0.1721 0.2754 -0.0469 -0.0278 -0.0298 12  LEU   B CB  
4083 C  CG  . LEU   B 12  ? 0.2516 0.1602 0.2732 -0.0515 -0.0181 -0.0292 12  LEU   B CG  
4084 C  CD1 . LEU   B 12  ? 0.2620 0.1645 0.2675 -0.0338 -0.0157 -0.0120 12  LEU   B CD1 
4085 C  CD2 . LEU   B 12  ? 0.2582 0.1678 0.2852 -0.0508 -0.0097 -0.0337 12  LEU   B CD2 
4097 N  N   . THR   B 13  ? 0.2318 0.1985 0.2899 -0.0658 -0.0515 -0.0296 13  THR   B N   
4098 C  CA  . THR   B 13  ? 0.2315 0.2080 0.2767 -0.0689 -0.0670 -0.0153 13  THR   B CA  
4099 C  C   . THR   B 13  ? 0.2753 0.2316 0.2951 -0.0823 -0.0841 -0.0111 13  THR   B C   
4100 O  O   . THR   B 13  ? 0.2963 0.2289 0.3123 -0.0833 -0.0533 -0.0167 13  THR   B O   
4101 C  CB  . THR   B 13  ? 0.2087 0.2007 0.2703 -0.0570 -0.0577 -0.0118 13  THR   B CB  
4102 O  OG1 . THR   B 13  ? 0.1974 0.1937 0.2888 -0.0468 -0.0445 -0.0108 13  THR   B OG1 
4103 C  CG2 . THR   B 13  ? 0.2088 0.2054 0.2778 -0.0494 -0.0429 0.0020  13  THR   B CG2 
4111 N  N   A ASP   B 14  ? 0.2853 0.2469 0.2956 -0.0922 -0.1158 -0.0004 14  ASP   B N   
4112 N  N   B ASP   B 14  ? 0.2836 0.2447 0.3010 -0.0834 -0.0936 0.0009  14  ASP   B N   
4113 C  CA  A ASP   B 14  ? 0.2987 0.2625 0.3268 -0.0906 -0.1162 0.0199  14  ASP   B CA  
4114 C  CA  B ASP   B 14  ? 0.2929 0.2568 0.3193 -0.0803 -0.0906 0.0150  14  ASP   B CA  
4115 C  C   A ASP   B 14  ? 0.2891 0.2431 0.2830 -0.0911 -0.1042 0.0240  14  ASP   B C   
4116 C  C   B ASP   B 14  ? 0.2813 0.2399 0.2799 -0.0829 -0.0932 0.0190  14  ASP   B C   
4117 O  O   A ASP   B 14  ? 0.3166 0.2533 0.2829 -0.0897 -0.0991 0.0324  14  ASP   B O   
4118 O  O   B ASP   B 14  ? 0.2988 0.2462 0.2774 -0.0822 -0.0913 0.0213  14  ASP   B O   
4119 C  CB  A ASP   B 14  ? 0.3195 0.2978 0.4088 -0.0860 -0.1238 0.0192  14  ASP   B CB  
4120 C  CB  B ASP   B 14  ? 0.3116 0.2848 0.3782 -0.0733 -0.0846 0.0170  14  ASP   B CB  
4121 C  CG  A ASP   B 14  ? 0.3430 0.3285 0.4880 -0.0776 -0.1188 0.0051  14  ASP   B CG  
4122 C  CG  B ASP   B 14  ? 0.3297 0.3091 0.4341 -0.0653 -0.0757 0.0109  14  ASP   B CG  
4123 O  OD1 A ASP   B 14  ? 0.3554 0.3349 0.5084 -0.0787 -0.1205 -0.0067 14  ASP   B OD1 
4124 O  OD1 B ASP   B 14  ? 0.3391 0.3189 0.4480 -0.0637 -0.0717 0.0069  14  ASP   B OD1 
4125 O  OD2 A ASP   B 14  ? 0.3465 0.3429 0.5240 -0.0730 -0.1121 0.0059  14  ASP   B OD2 
4126 O  OD2 B ASP   B 14  ? 0.3326 0.3173 0.4558 -0.0635 -0.0736 0.0104  14  ASP   B OD2 
4135 N  N   . ASN   B 15  ? 0.2523 0.2178 0.2577 -0.0779 -0.0954 0.0269  15  ASN   B N   
4136 C  CA  . ASN   B 15  ? 0.2041 0.1837 0.2492 -0.0534 -0.0703 0.0107  15  ASN   B CA  
4137 C  C   . ASN   B 15  ? 0.1855 0.1657 0.2343 -0.0347 -0.0545 0.0021  15  ASN   B C   
4138 O  O   . ASN   B 15  ? 0.1794 0.1563 0.2495 -0.0297 -0.0534 -0.0085 15  ASN   B O   
4139 C  CB  . ASN   B 15  ? 0.1951 0.1781 0.2691 -0.0291 -0.0659 0.0118  15  ASN   B CB  
4140 C  CG  . ASN   B 15  ? 0.1783 0.1725 0.2726 -0.0307 -0.0411 0.0153  15  ASN   B CG  
4141 O  OD1 . ASN   B 15  ? 0.1813 0.1984 0.3049 -0.0507 -0.0499 0.0213  15  ASN   B OD1 
4142 N  ND2 . ASN   B 15  ? 0.1732 0.1501 0.2665 -0.0156 -0.0118 -0.0030 15  ASN   B ND2 
4150 N  N   . VAL   B 16  ? 0.1872 0.1608 0.2295 -0.0370 -0.0570 -0.0008 16  VAL   B N   
4151 C  CA  . VAL   B 16  ? 0.1835 0.1623 0.2114 -0.0331 -0.0472 -0.0211 16  VAL   B CA  
4152 C  C   . VAL   B 16  ? 0.1848 0.1776 0.2132 -0.0446 -0.0433 -0.0143 16  VAL   B C   
4153 O  O   . VAL   B 16  ? 0.1894 0.1888 0.2354 -0.0397 -0.0400 -0.0305 16  VAL   B O   
4154 C  CB  . VAL   B 16  ? 0.1881 0.1563 0.2248 -0.0187 -0.0340 -0.0282 16  VAL   B CB  
4155 C  CG1 . VAL   B 16  ? 0.1925 0.1485 0.2211 -0.0020 -0.0310 -0.0214 16  VAL   B CG1 
4156 C  CG2 . VAL   B 16  ? 0.1878 0.1622 0.2533 -0.0110 -0.0305 -0.0295 16  VAL   B CG2 
4166 N  N   . TYR   B 17  ? 0.1932 0.1843 0.2058 -0.0456 -0.0386 -0.0147 17  TYR   B N   
4167 C  CA  . TYR   B 17  ? 0.2013 0.1933 0.2097 -0.0567 -0.0392 0.0055  17  TYR   B CA  
4168 C  C   . TYR   B 17  ? 0.1957 0.1644 0.2080 -0.0539 -0.0217 -0.0069 17  TYR   B C   
4169 O  O   . TYR   B 17  ? 0.1883 0.1707 0.2087 -0.0433 -0.0257 -0.0326 17  TYR   B O   
4170 C  CB  . TYR   B 17  ? 0.2384 0.2436 0.2414 -0.0424 -0.0452 0.0368  17  TYR   B CB  
4171 C  CG  . TYR   B 17  ? 0.2718 0.2985 0.2965 -0.0352 -0.0675 0.0511  17  TYR   B CG  
4172 C  CD1 . TYR   B 17  ? 0.2914 0.3187 0.3357 -0.0334 -0.0746 0.0597  17  TYR   B CD1 
4173 C  CD2 . TYR   B 17  ? 0.2939 0.3242 0.3270 -0.0270 -0.0837 0.0575  17  TYR   B CD2 
4174 C  CE1 . TYR   B 17  ? 0.3098 0.3429 0.3582 -0.0241 -0.0873 0.0566  17  TYR   B CE1 
4175 C  CE2 . TYR   B 17  ? 0.3117 0.3449 0.3535 -0.0154 -0.0953 0.0641  17  TYR   B CE2 
4176 C  CZ  . TYR   B 17  ? 0.3223 0.3577 0.3737 -0.0138 -0.0977 0.0609  17  TYR   B CZ  
4177 O  OH  . TYR   B 17  ? 0.3374 0.3716 0.3910 -0.0053 -0.1021 0.0622  17  TYR   B OH  
4187 N  N   . ILE   B 18  ? 0.2063 0.1653 0.2040 -0.0443 -0.0109 -0.0203 18  ILE   B N   
4188 C  CA  . ILE   B 18  ? 0.2101 0.1619 0.2072 -0.0468 -0.0033 -0.0253 18  ILE   B CA  
4189 C  C   . ILE   B 18  ? 0.2194 0.1686 0.2039 -0.0575 -0.0006 -0.0350 18  ILE   B C   
4190 O  O   . ILE   B 18  ? 0.2360 0.1854 0.2189 -0.0485 0.0048  -0.0431 18  ILE   B O   
4191 C  CB  . ILE   B 18  ? 0.2144 0.1596 0.2141 -0.0477 -0.0018 -0.0234 18  ILE   B CB  
4192 C  CG1 . ILE   B 18  ? 0.2154 0.1621 0.2274 -0.0477 0.0032  -0.0142 18  ILE   B CG1 
4193 C  CG2 . ILE   B 18  ? 0.2208 0.1678 0.2199 -0.0509 -0.0115 -0.0129 18  ILE   B CG2 
4194 C  CD1 . ILE   B 18  ? 0.2223 0.1905 0.2466 -0.0424 -0.0140 0.0091  18  ILE   B CD1 
4206 N  N   . LYS   B 19  ? 0.2219 0.1667 0.2082 -0.0397 0.0341  -0.0441 19  LYS   B N   
4207 C  CA  . LYS   B 19  ? 0.2293 0.1723 0.2423 -0.0419 0.0325  -0.0526 19  LYS   B CA  
4208 C  C   . LYS   B 19  ? 0.2094 0.1683 0.2590 -0.0382 0.0353  -0.0611 19  LYS   B C   
4209 O  O   . LYS   B 19  ? 0.1990 0.1739 0.2307 -0.0269 0.0317  -0.0498 19  LYS   B O   
4210 C  CB  . LYS   B 19  ? 0.2552 0.1952 0.2592 -0.0426 0.0485  -0.0476 19  LYS   B CB  
4211 C  CG  . LYS   B 19  ? 0.2849 0.2222 0.2847 -0.0498 0.0567  -0.0477 19  LYS   B CG  
4212 C  CD  . LYS   B 19  ? 0.3146 0.2517 0.2881 -0.0567 0.0704  -0.0508 19  LYS   B CD  
4213 C  CE  . LYS   B 19  ? 0.3428 0.2770 0.3090 -0.0581 0.0672  -0.0509 19  LYS   B CE  
4214 N  NZ  . LYS   B 19  ? 0.3561 0.2896 0.3099 -0.0629 0.0720  -0.0472 19  LYS   B NZ  
4228 N  N   . ASN   B 20  ? 0.2071 0.1835 0.2931 -0.0318 0.0491  -0.0771 20  ASN   B N   
4229 C  CA  . ASN   B 20  ? 0.2090 0.1981 0.3217 -0.0231 0.0524  -0.0971 20  ASN   B CA  
4230 C  C   . ASN   B 20  ? 0.2093 0.2154 0.3237 -0.0268 0.0611  -0.1069 20  ASN   B C   
4231 O  O   . ASN   B 20  ? 0.2266 0.2502 0.3431 -0.0416 0.0671  -0.1025 20  ASN   B O   
4232 C  CB  . ASN   B 20  ? 0.2370 0.2056 0.3515 0.0035  0.0379  -0.1023 20  ASN   B CB  
4233 C  CG  . ASN   B 20  ? 0.2617 0.2158 0.3769 0.0372  0.0361  -0.1094 20  ASN   B CG  
4234 O  OD1 . ASN   B 20  ? 0.2936 0.2423 0.4031 0.0530  0.0372  -0.1060 20  ASN   B OD1 
4235 N  ND2 . ASN   B 20  ? 0.2499 0.2167 0.3725 0.0411  0.0194  -0.1060 20  ASN   B ND2 
4242 N  N   . ALA   B 21  ? 0.2048 0.2003 0.3158 -0.0305 0.0590  -0.0843 21  ALA   B N   
4243 C  CA  . ALA   B 21  ? 0.2171 0.2034 0.3202 -0.0310 0.0464  -0.0665 21  ALA   B CA  
4244 C  C   . ALA   B 21  ? 0.2152 0.1792 0.3048 -0.0244 0.0506  -0.0498 21  ALA   B C   
4245 O  O   . ALA   B 21  ? 0.2198 0.1704 0.3008 -0.0337 0.0440  -0.0424 21  ALA   B O   
4246 C  CB  . ALA   B 21  ? 0.2347 0.2285 0.3276 -0.0369 0.0517  -0.0515 21  ALA   B CB  
4252 N  N   . ASP   B 22  ? 0.2040 0.1694 0.2842 -0.0223 0.0454  -0.0408 22  ASP   B N   
4253 C  CA  . ASP   B 22  ? 0.1977 0.1624 0.2710 -0.0121 0.0328  -0.0302 22  ASP   B CA  
4254 C  C   . ASP   B 22  ? 0.1888 0.1559 0.2282 -0.0169 0.0226  -0.0171 22  ASP   B C   
4255 O  O   . ASP   B 22  ? 0.1910 0.1624 0.2368 -0.0132 0.0094  -0.0144 22  ASP   B O   
4256 C  CB  . ASP   B 22  ? 0.2050 0.1737 0.3046 -0.0072 0.0303  -0.0153 22  ASP   B CB  
4257 C  CG  . ASP   B 22  ? 0.2027 0.1951 0.3519 -0.0012 0.0121  -0.0186 22  ASP   B CG  
4258 O  OD1 . ASP   B 22  ? 0.2120 0.1835 0.3426 -0.0030 -0.0018 -0.0156 22  ASP   B OD1 
4259 O  OD2 . ASP   B 22  ? 0.2119 0.2227 0.4124 0.0102  -0.0088 -0.0276 22  ASP   B OD2 
4264 N  N   . ILE   B 23  ? 0.1914 0.1484 0.2036 -0.0137 0.0061  0.0087  23  ILE   B N   
4265 C  CA  . ILE   B 23  ? 0.1799 0.1469 0.1869 -0.0125 0.0025  0.0018  23  ILE   B CA  
4266 C  C   . ILE   B 23  ? 0.1715 0.1495 0.1795 -0.0068 -0.0125 -0.0013 23  ILE   B C   
4267 O  O   . ILE   B 23  ? 0.1632 0.1521 0.1736 -0.0118 -0.0079 0.0057  23  ILE   B O   
4268 C  CB  . ILE   B 23  ? 0.1770 0.1560 0.1967 -0.0198 0.0008  0.0097  23  ILE   B CB  
4269 C  CG1 . ILE   B 23  ? 0.1802 0.1648 0.1960 -0.0125 0.0055  0.0275  23  ILE   B CG1 
4270 C  CG2 . ILE   B 23  ? 0.1796 0.1755 0.1991 -0.0176 0.0029  0.0063  23  ILE   B CG2 
4271 C  CD1 . ILE   B 23  ? 0.1897 0.1841 0.2076 -0.0095 0.0054  0.0184  23  ILE   B CD1 
4283 N  N   . VAL   B 24  ? 0.1746 0.1497 0.1968 -0.0089 -0.0091 0.0005  24  VAL   B N   
4284 C  CA  . VAL   B 24  ? 0.1705 0.1583 0.2179 -0.0083 -0.0185 -0.0017 24  VAL   B CA  
4285 C  C   . VAL   B 24  ? 0.1703 0.1634 0.2201 -0.0142 -0.0064 0.0050  24  VAL   B C   
4286 O  O   . VAL   B 24  ? 0.1668 0.1678 0.2204 -0.0214 -0.0029 0.0135  24  VAL   B O   
4287 C  CB  . VAL   B 24  ? 0.1808 0.1704 0.2245 -0.0010 -0.0246 -0.0008 24  VAL   B CB  
4288 C  CG1 . VAL   B 24  ? 0.1752 0.1765 0.2463 -0.0106 -0.0307 0.0078  24  VAL   B CG1 
4289 C  CG2 . VAL   B 24  ? 0.1935 0.1968 0.2313 0.0074  -0.0196 -0.0074 24  VAL   B CG2 
4299 N  N   . GLU   B 25  ? 0.1884 0.1769 0.2311 -0.0116 0.0059  0.0004  25  GLU   B N   
4300 C  CA  . GLU   B 25  ? 0.2027 0.2014 0.2505 0.0020  0.0180  -0.0101 25  GLU   B CA  
4301 C  C   . GLU   B 25  ? 0.1954 0.1943 0.2086 -0.0105 0.0145  -0.0025 25  GLU   B C   
4302 O  O   . GLU   B 25  ? 0.2006 0.2056 0.2162 -0.0111 0.0146  0.0035  25  GLU   B O   
4303 C  CB  . GLU   B 25  ? 0.2432 0.2451 0.3195 0.0285  0.0276  -0.0166 25  GLU   B CB  
4304 C  CG  . GLU   B 25  ? 0.2874 0.3080 0.4270 0.0376  0.0196  -0.0186 25  GLU   B CG  
4305 C  CD  . GLU   B 25  ? 0.3252 0.3717 0.5162 0.0352  0.0101  -0.0206 25  GLU   B CD  
4306 O  OE1 . GLU   B 25  ? 0.3530 0.3939 0.5400 0.0391  0.0114  -0.0185 25  GLU   B OE1 
4307 O  OE2 . GLU   B 25  ? 0.3508 0.3835 0.5408 0.0334  0.0001  -0.0265 25  GLU   B OE2 
4314 N  N   . GLU   B 26  ? 0.1937 0.1855 0.1946 -0.0281 0.0102  -0.0016 26  GLU   B N   
4315 C  CA  . GLU   B 26  ? 0.1963 0.1988 0.1968 -0.0418 -0.0047 -0.0000 26  GLU   B CA  
4316 C  C   . GLU   B 26  ? 0.1791 0.1956 0.1900 -0.0317 0.0099  0.0122  26  GLU   B C   
4317 O  O   . GLU   B 26  ? 0.1951 0.2120 0.1868 -0.0322 0.0049  0.0154  26  GLU   B O   
4318 C  CB  . GLU   B 26  ? 0.2312 0.2198 0.2115 -0.0502 0.0023  0.0186  26  GLU   B CB  
4319 C  CG  . GLU   B 26  ? 0.2741 0.2566 0.2768 -0.0561 0.0175  -0.0034 26  GLU   B CG  
4320 C  CD  . GLU   B 26  ? 0.2969 0.2769 0.2917 -0.0764 0.0297  -0.0378 26  GLU   B CD  
4321 O  OE1 . GLU   B 26  ? 0.3147 0.2612 0.3120 -0.0842 0.0694  -0.0349 26  GLU   B OE1 
4322 O  OE2 . GLU   B 26  ? 0.3032 0.3156 0.3360 -0.0708 0.0228  -0.0297 26  GLU   B OE2 
4329 N  N   . ALA   B 27  ? 0.1643 0.1769 0.1823 -0.0288 0.0101  0.0138  27  ALA   B N   
4330 C  CA  . ALA   B 27  ? 0.1612 0.1764 0.1899 -0.0212 -0.0002 0.0257  27  ALA   B CA  
4331 C  C   . ALA   B 27  ? 0.1624 0.1872 0.2146 -0.0159 0.0117  0.0404  27  ALA   B C   
4332 O  O   . ALA   B 27  ? 0.1676 0.1943 0.2286 -0.0042 0.0150  0.0458  27  ALA   B O   
4333 C  CB  . ALA   B 27  ? 0.1686 0.1601 0.1928 -0.0199 -0.0008 0.0203  27  ALA   B CB  
4339 N  N   . LYS   B 28  ? 0.1616 0.2106 0.2547 -0.0220 0.0206  0.0608  28  LYS   B N   
4340 C  CA  . LYS   B 28  ? 0.1796 0.2490 0.2900 -0.0130 0.0509  0.0868  28  LYS   B CA  
4341 C  C   . LYS   B 28  ? 0.2005 0.2633 0.2782 -0.0086 0.0562  0.0754  28  LYS   B C   
4342 O  O   . LYS   B 28  ? 0.2218 0.2634 0.2873 -0.0123 0.0590  0.0653  28  LYS   B O   
4343 C  CB  . LYS   B 28  ? 0.2021 0.2843 0.3503 0.0011  0.0751  0.1122  28  LYS   B CB  
4344 C  CG  . LYS   B 28  ? 0.2351 0.3314 0.3977 0.0071  0.0841  0.1332  28  LYS   B CG  
4345 C  CD  . LYS   B 28  ? 0.2931 0.3925 0.4621 0.0110  0.0973  0.1354  28  LYS   B CD  
4346 C  CE  . LYS   B 28  ? 0.3473 0.4412 0.5164 0.0146  0.1001  0.1412  28  LYS   B CE  
4347 N  NZ  . LYS   B 28  ? 0.3764 0.4642 0.5384 0.0182  0.0973  0.1452  28  LYS   B NZ  
4361 N  N   . LYS   B 29  ? 0.2177 0.2926 0.2709 0.0055  0.0613  0.0674  29  LYS   B N   
4362 C  CA  . LYS   B 29  ? 0.2634 0.3296 0.2995 0.0088  0.0652  0.0618  29  LYS   B CA  
4363 C  C   . LYS   B 29  ? 0.2590 0.3273 0.2625 0.0067  0.0442  0.0705  29  LYS   B C   
4364 O  O   . LYS   B 29  ? 0.2789 0.3452 0.2670 0.0139  0.0425  0.0759  29  LYS   B O   
4365 C  CB  . LYS   B 29  ? 0.3224 0.3709 0.3865 0.0116  0.0739  0.0480  29  LYS   B CB  
4366 C  CG  . LYS   B 29  ? 0.3730 0.4042 0.4815 0.0130  0.0815  0.0406  29  LYS   B CG  
4367 C  CD  . LYS   B 29  ? 0.4173 0.4295 0.5536 0.0130  0.0918  0.0340  29  LYS   B CD  
4368 C  CE  . LYS   B 29  ? 0.4523 0.4503 0.6021 0.0133  0.1011  0.0283  29  LYS   B CE  
4369 N  NZ  . LYS   B 29  ? 0.4706 0.4568 0.6329 0.0134  0.1043  0.0240  29  LYS   B NZ  
4383 N  N   . VAL   B 30  ? 0.2284 0.3032 0.2431 -0.0084 0.0258  0.0685  30  VAL   B N   
4384 C  CA  . VAL   B 30  ? 0.2123 0.2877 0.2638 -0.0242 -0.0073 0.0728  30  VAL   B CA  
4385 C  C   . VAL   B 30  ? 0.1911 0.2821 0.2529 -0.0247 -0.0019 0.0870  30  VAL   B C   
4386 O  O   . VAL   B 30  ? 0.2023 0.2964 0.2509 -0.0177 -0.0047 0.0961  30  VAL   B O   
4387 C  CB  . VAL   B 30  ? 0.2175 0.2809 0.3067 -0.0410 -0.0312 0.0728  30  VAL   B CB  
4388 C  CG1 . VAL   B 30  ? 0.2255 0.2874 0.3058 -0.0398 -0.0263 0.0686  30  VAL   B CG1 
4389 C  CG2 . VAL   B 30  ? 0.2293 0.2814 0.3294 -0.0513 -0.0394 0.0596  30  VAL   B CG2 
4399 N  N   . LYS   B 31  ? 0.1795 0.2532 0.2811 -0.0368 -0.0048 0.0931  31  LYS   B N   
4400 C  CA  . LYS   B 31  ? 0.1669 0.2488 0.3103 -0.0441 -0.0087 0.1011  31  LYS   B CA  
4401 C  C   . LYS   B 31  ? 0.1651 0.2090 0.2681 -0.0389 -0.0268 0.0868  31  LYS   B C   
4402 O  O   . LYS   B 31  ? 0.1711 0.2208 0.2752 -0.0324 -0.0248 0.1035  31  LYS   B O   
4403 C  CB  . LYS   B 31  ? 0.1868 0.2942 0.3630 -0.0425 0.0213  0.1127  31  LYS   B CB  
4404 C  CG  . LYS   B 31  ? 0.2227 0.3379 0.4100 -0.0444 0.0318  0.1076  31  LYS   B CG  
4405 C  CD  . LYS   B 31  ? 0.2713 0.3870 0.4635 -0.0439 0.0233  0.0909  31  LYS   B CD  
4406 C  CE  . LYS   B 31  ? 0.3058 0.4195 0.5125 -0.0443 0.0116  0.0768  31  LYS   B CE  
4407 N  NZ  . LYS   B 31  ? 0.3325 0.4407 0.5268 -0.0402 -0.0003 0.0691  31  LYS   B NZ  
4421 N  N   . PRO   B 32  ? 0.1801 0.1673 0.2087 -0.0359 -0.0434 0.0524  32  PRO   B N   
4422 C  CA  . PRO   B 32  ? 0.1942 0.1638 0.1723 -0.0368 -0.0409 0.0327  32  PRO   B CA  
4423 C  C   . PRO   B 32  ? 0.2045 0.1531 0.1739 -0.0438 -0.0565 0.0389  32  PRO   B C   
4424 O  O   . PRO   B 32  ? 0.2189 0.1590 0.1984 -0.0464 -0.0687 0.0368  32  PRO   B O   
4425 C  CB  . PRO   B 32  ? 0.2055 0.1582 0.1720 -0.0418 -0.0323 0.0195  32  PRO   B CB  
4426 C  CG  . PRO   B 32  ? 0.2207 0.1493 0.1710 -0.0325 -0.0496 0.0287  32  PRO   B CG  
4427 C  CD  . PRO   B 32  ? 0.2033 0.1530 0.2011 -0.0237 -0.0619 0.0280  32  PRO   B CD  
4435 N  N   . THR   B 33  ? 0.2060 0.1462 0.1662 -0.0392 -0.0505 0.0305  33  THR   B N   
4436 C  CA  . THR   B 33  ? 0.2119 0.1499 0.1617 -0.0418 -0.0448 0.0320  33  THR   B CA  
4437 C  C   . THR   B 33  ? 0.2115 0.1400 0.1596 -0.0416 -0.0491 0.0189  33  THR   B C   
4438 O  O   . THR   B 33  ? 0.2277 0.1436 0.1758 -0.0473 -0.0603 0.0233  33  THR   B O   
4439 C  CB  . THR   B 33  ? 0.2204 0.1615 0.1622 -0.0284 -0.0506 0.0333  33  THR   B CB  
4440 O  OG1 . THR   B 33  ? 0.2090 0.1668 0.1756 -0.0284 -0.0482 0.0386  33  THR   B OG1 
4441 C  CG2 . THR   B 33  ? 0.2438 0.1695 0.1740 -0.0194 -0.0469 0.0296  33  THR   B CG2 
4449 N  N   . VAL   B 34  ? 0.1951 0.1392 0.1475 -0.0399 -0.0434 0.0200  34  VAL   B N   
4450 C  CA  . VAL   B 34  ? 0.1780 0.1359 0.1444 -0.0289 -0.0320 0.0077  34  VAL   B CA  
4451 C  C   . VAL   B 34  ? 0.1611 0.1325 0.1381 -0.0318 -0.0239 0.0081  34  VAL   B C   
4452 O  O   . VAL   B 34  ? 0.1788 0.1383 0.1404 -0.0308 -0.0340 0.0070  34  VAL   B O   
4453 C  CB  . VAL   B 34  ? 0.1838 0.1443 0.1679 -0.0116 -0.0286 0.0073  34  VAL   B CB  
4454 C  CG1 . VAL   B 34  ? 0.1806 0.1554 0.1735 -0.0134 -0.0134 0.0019  34  VAL   B CG1 
4455 C  CG2 . VAL   B 34  ? 0.1912 0.1502 0.1970 -0.0141 -0.0298 0.0135  34  VAL   B CG2 
4465 N  N   . VAL   B 35  ? 0.1513 0.1282 0.1322 -0.0267 -0.0138 0.0066  35  VAL   B N   
4466 C  CA  . VAL   B 35  ? 0.1458 0.1311 0.1271 -0.0219 -0.0110 0.0094  35  VAL   B CA  
4467 C  C   . VAL   B 35  ? 0.1375 0.1263 0.1322 -0.0189 -0.0121 0.0109  35  VAL   B C   
4468 O  O   . VAL   B 35  ? 0.1438 0.1296 0.1358 -0.0220 -0.0051 0.0017  35  VAL   B O   
4469 C  CB  . VAL   B 35  ? 0.1457 0.1448 0.1386 -0.0196 -0.0037 0.0019  35  VAL   B CB  
4470 C  CG1 . VAL   B 35  ? 0.1449 0.1577 0.1573 -0.0205 -0.0025 0.0067  35  VAL   B CG1 
4471 C  CG2 . VAL   B 35  ? 0.1547 0.1442 0.1681 -0.0115 0.0006  0.0022  35  VAL   B CG2 
4481 N  N   . VAL   B 36  ? 0.1354 0.1288 0.1350 -0.0223 -0.0144 0.0072  36  VAL   B N   
4482 C  CA  . VAL   B 36  ? 0.1335 0.1186 0.1297 -0.0179 -0.0063 0.0058  36  VAL   B CA  
4483 C  C   . VAL   B 36  ? 0.1323 0.1224 0.1265 -0.0152 -0.0057 -0.0020 36  VAL   B C   
4484 O  O   . VAL   B 36  ? 0.1400 0.1383 0.1416 -0.0118 -0.0052 -0.0071 36  VAL   B O   
4485 C  CB  . VAL   B 36  ? 0.1370 0.1265 0.1336 -0.0161 -0.0089 0.0011  36  VAL   B CB  
4486 C  CG1 . VAL   B 36  ? 0.1381 0.1364 0.1445 -0.0179 -0.0018 0.0019  36  VAL   B CG1 
4487 C  CG2 . VAL   B 36  ? 0.1477 0.1323 0.1371 -0.0162 -0.0188 0.0037  36  VAL   B CG2 
4497 N  N   . ASN   B 37  ? 0.1340 0.1235 0.1269 -0.0035 -0.0045 0.0045  37  ASN   B N   
4498 C  CA  . ASN   B 37  ? 0.1388 0.1290 0.1266 0.0007  -0.0105 0.0090  37  ASN   B CA  
4499 C  C   . ASN   B 37  ? 0.1412 0.1314 0.1283 0.0011  -0.0125 0.0055  37  ASN   B C   
4500 O  O   . ASN   B 37  ? 0.1432 0.1359 0.1456 0.0023  -0.0020 0.0057  37  ASN   B O   
4501 C  CB  . ASN   B 37  ? 0.1387 0.1288 0.1220 -0.0049 -0.0129 0.0058  37  ASN   B CB  
4502 C  CG  . ASN   B 37  ? 0.1435 0.1305 0.1429 -0.0045 -0.0110 0.0064  37  ASN   B CG  
4503 O  OD1 . ASN   B 37  ? 0.1506 0.1370 0.1572 0.0056  -0.0205 0.0039  37  ASN   B OD1 
4504 N  ND2 . ASN   B 37  ? 0.1485 0.1298 0.1397 -0.0014 -0.0220 0.0038  37  ASN   B ND2 
4511 N  N   . ALA   B 38  ? 0.1467 0.1302 0.1354 0.0066  0.0031  0.0082  38  ALA   B N   
4512 C  CA  . ALA   B 38  ? 0.1574 0.1365 0.1397 0.0009  -0.0017 0.0118  38  ALA   B CA  
4513 C  C   . ALA   B 38  ? 0.1515 0.1276 0.1368 -0.0008 -0.0023 0.0107  38  ALA   B C   
4514 O  O   . ALA   B 38  ? 0.1641 0.1417 0.1479 0.0030  -0.0070 0.0097  38  ALA   B O   
4515 C  CB  . ALA   B 38  ? 0.1814 0.1385 0.1522 -0.0092 0.0043  0.0081  38  ALA   B CB  
4521 N  N   . ALA   B 39  ? 0.1502 0.1320 0.1379 0.0066  -0.0077 0.0089  39  ALA   B N   
4522 C  CA  . ALA   B 39  ? 0.1577 0.1356 0.1362 0.0030  -0.0142 0.0058  39  ALA   B CA  
4523 C  C   . ALA   B 39  ? 0.1639 0.1417 0.1269 0.0095  -0.0100 0.0084  39  ALA   B C   
4524 O  O   . ALA   B 39  ? 0.1710 0.1505 0.1551 -0.0032 -0.0037 0.0123  39  ALA   B O   
4525 C  CB  . ALA   B 39  ? 0.1569 0.1437 0.1573 -0.0100 -0.0029 0.0000  39  ALA   B CB  
4531 N  N   . ASN   B 40  ? 0.1703 0.1660 0.1278 0.0001  -0.0035 -0.0055 40  ASN   B N   
4532 C  CA  . ASN   B 40  ? 0.1759 0.1717 0.1370 0.0025  -0.0103 -0.0065 40  ASN   B CA  
4533 C  C   . ASN   B 40  ? 0.1802 0.1730 0.1193 0.0101  -0.0111 0.0036  40  ASN   B C   
4534 O  O   . ASN   B 40  ? 0.1727 0.1646 0.1299 0.0094  -0.0100 0.0053  40  ASN   B O   
4535 C  CB  . ASN   B 40  ? 0.1869 0.1670 0.1571 0.0118  -0.0157 0.0103  40  ASN   B CB  
4536 C  CG  . ASN   B 40  ? 0.1923 0.1739 0.1850 0.0049  -0.0283 0.0204  40  ASN   B CG  
4537 O  OD1 . ASN   B 40  ? 0.1930 0.1709 0.2701 0.0027  -0.0373 0.0247  40  ASN   B OD1 
4538 N  ND2 . ASN   B 40  ? 0.1922 0.1741 0.1904 0.0041  -0.0249 0.0170  40  ASN   B ND2 
4545 N  N   . VAL   B 41  ? 0.1872 0.1745 0.1322 0.0142  0.0030  -0.0012 41  VAL   B N   
4546 C  CA  . VAL   B 41  ? 0.1956 0.1886 0.1328 0.0080  0.0009  -0.0071 41  VAL   B CA  
4547 C  C   . VAL   B 41  ? 0.1948 0.1844 0.1228 0.0137  -0.0058 -0.0038 41  VAL   B C   
4548 O  O   . VAL   B 41  ? 0.1929 0.1813 0.1374 0.0146  -0.0096 -0.0064 41  VAL   B O   
4549 C  CB  . VAL   B 41  ? 0.2094 0.2074 0.1652 -0.0040 0.0201  -0.0220 41  VAL   B CB  
4550 C  CG1 . VAL   B 41  ? 0.2070 0.2088 0.1834 -0.0074 0.0295  -0.0242 41  VAL   B CG1 
4551 C  CG2 . VAL   B 41  ? 0.2257 0.2298 0.1734 -0.0145 0.0212  -0.0177 41  VAL   B CG2 
4561 N  N   . TYR   B 42  ? 0.2007 0.1844 0.1258 0.0158  -0.0202 0.0049  42  TYR   B N   
4562 C  CA  . TYR   B 42  ? 0.2046 0.1866 0.1334 0.0203  -0.0255 -0.0108 42  TYR   B CA  
4563 C  C   . TYR   B 42  ? 0.1854 0.1717 0.1448 0.0216  -0.0233 -0.0112 42  TYR   B C   
4564 O  O   . TYR   B 42  ? 0.1849 0.1780 0.1768 0.0140  -0.0266 -0.0142 42  TYR   B O   
4565 C  CB  . TYR   B 42  ? 0.2254 0.2103 0.1588 0.0157  -0.0353 -0.0019 42  TYR   B CB  
4566 C  CG  . TYR   B 42  ? 0.2248 0.2231 0.1467 0.0003  -0.0352 0.0109  42  TYR   B CG  
4567 C  CD1 . TYR   B 42  ? 0.2223 0.2245 0.1155 -0.0053 -0.0142 0.0071  42  TYR   B CD1 
4568 C  CD2 . TYR   B 42  ? 0.2368 0.2297 0.1838 -0.0015 -0.0160 0.0181  42  TYR   B CD2 
4569 C  CE1 . TYR   B 42  ? 0.2366 0.2357 0.1261 -0.0026 -0.0124 0.0089  42  TYR   B CE1 
4570 C  CE2 . TYR   B 42  ? 0.2401 0.2424 0.1813 0.0002  0.0128  0.0342  42  TYR   B CE2 
4571 C  CZ  . TYR   B 42  ? 0.2522 0.2558 0.1582 0.0137  0.0161  0.0202  42  TYR   B CZ  
4572 O  OH  . TYR   B 42  ? 0.2799 0.2770 0.1937 0.0335  0.0217  0.0272  42  TYR   B OH  
4582 N  N   . LEU   B 43  ? 0.1745 0.1553 0.1323 0.0093  -0.0195 -0.0124 43  LEU   B N   
4583 C  CA  . LEU   B 43  ? 0.1748 0.1574 0.1233 0.0021  -0.0161 -0.0039 43  LEU   B CA  
4584 C  C   . LEU   B 43  ? 0.1809 0.1596 0.1234 0.0001  -0.0136 0.0046  43  LEU   B C   
4585 O  O   . LEU   B 43  ? 0.1738 0.1606 0.1622 0.0052  -0.0255 0.0098  43  LEU   B O   
4586 C  CB  . LEU   B 43  ? 0.1697 0.1502 0.1478 0.0021  -0.0244 -0.0052 43  LEU   B CB  
4587 C  CG  . LEU   B 43  ? 0.1733 0.1473 0.1592 -0.0012 -0.0272 -0.0105 43  LEU   B CG  
4588 C  CD1 . LEU   B 43  ? 0.1783 0.1511 0.1903 -0.0022 -0.0469 -0.0118 43  LEU   B CD1 
4589 C  CD2 . LEU   B 43  ? 0.1682 0.1468 0.1739 -0.0063 -0.0273 -0.0037 43  LEU   B CD2 
4601 N  N   . LYS   B 44  ? 0.1739 0.1603 0.1433 0.0086  -0.0110 -0.0019 44  LYS   B N   
4602 C  CA  . LYS   B 44  ? 0.1877 0.1687 0.1389 0.0108  -0.0127 0.0049  44  LYS   B CA  
4603 C  C   . LYS   B 44  ? 0.1769 0.1592 0.1390 0.0145  -0.0193 0.0045  44  LYS   B C   
4604 O  O   . LYS   B 44  ? 0.1945 0.1552 0.1745 0.0010  -0.0081 0.0011  44  LYS   B O   
4605 C  CB  . LYS   B 44  ? 0.2193 0.1828 0.1636 0.0231  -0.0269 0.0026  44  LYS   B CB  
4606 C  CG  . LYS   B 44  ? 0.2579 0.2063 0.2041 0.0128  -0.0607 0.0077  44  LYS   B CG  
4607 C  CD  . LYS   B 44  ? 0.2933 0.2297 0.2814 -0.0057 -0.0745 0.0027  44  LYS   B CD  
4608 C  CE  . LYS   B 44  ? 0.3274 0.2555 0.3393 -0.0149 -0.0823 0.0163  44  LYS   B CE  
4609 N  NZ  . LYS   B 44  ? 0.3371 0.2642 0.3663 -0.0158 -0.0949 0.0335  44  LYS   B NZ  
4623 N  N   . HIS   B 45  ? 0.1657 0.1629 0.1433 0.0042  -0.0188 0.0100  45  HIS   B N   
4624 C  CA  . HIS   B 45  ? 0.1695 0.1570 0.1506 0.0059  -0.0138 0.0016  45  HIS   B CA  
4625 C  C   . HIS   B 45  ? 0.1933 0.1749 0.1892 0.0200  -0.0183 -0.0051 45  HIS   B C   
4626 O  O   . HIS   B 45  ? 0.2056 0.2065 0.2237 0.0419  -0.0017 -0.0001 45  HIS   B O   
4627 C  CB  . HIS   B 45  ? 0.1659 0.1617 0.1564 -0.0000 -0.0121 -0.0065 45  HIS   B CB  
4628 C  CG  . HIS   B 45  ? 0.1674 0.1557 0.1430 -0.0038 -0.0172 -0.0016 45  HIS   B CG  
4629 N  ND1 . HIS   B 45  ? 0.1650 0.1496 0.1533 -0.0017 -0.0202 -0.0023 45  HIS   B ND1 
4630 C  CD2 . HIS   B 45  ? 0.1766 0.1592 0.1583 -0.0088 -0.0215 -0.0007 45  HIS   B CD2 
4631 C  CE1 . HIS   B 45  ? 0.1816 0.1428 0.1391 -0.0045 -0.0278 -0.0072 45  HIS   B CE1 
4632 N  NE2 . HIS   B 45  ? 0.1881 0.1495 0.1451 -0.0008 -0.0252 -0.0098 45  HIS   B NE2 
4640 N  N   A GLY   B 46  ? 0.2038 0.1699 0.2237 0.0224  -0.0444 0.0026  46  GLY   B N   
4641 N  N   B GLY   B 46  ? 0.2016 0.1786 0.2119 0.0194  -0.0349 0.0037  46  GLY   B N   
4642 C  CA  A GLY   B 46  ? 0.2165 0.1870 0.2696 0.0194  -0.0488 0.0030  46  GLY   B CA  
4643 C  CA  B GLY   B 46  ? 0.2110 0.1931 0.2409 0.0170  -0.0395 0.0091  46  GLY   B CA  
4644 C  C   A GLY   B 46  ? 0.2150 0.2032 0.3136 0.0256  -0.0482 0.0031  46  GLY   B C   
4645 C  C   B GLY   B 46  ? 0.2131 0.2077 0.2726 0.0205  -0.0392 0.0157  46  GLY   B C   
4646 O  O   A GLY   B 46  ? 0.2211 0.2165 0.3992 0.0276  -0.0326 -0.0248 46  GLY   B O   
4647 O  O   B GLY   B 46  ? 0.2210 0.2189 0.3013 0.0205  -0.0308 0.0197  46  GLY   B O   
4654 N  N   . GLY   B 47  ? 0.2087 0.2126 0.2777 0.0141  -0.0317 0.0055  47  GLY   B N   
4655 C  CA  . GLY   B 47  ? 0.1992 0.1912 0.2445 0.0037  -0.0215 0.0035  47  GLY   B CA  
4656 C  C   . GLY   B 47  ? 0.1826 0.1675 0.2009 0.0046  -0.0033 0.0085  47  GLY   B C   
4657 O  O   . GLY   B 47  ? 0.1974 0.1484 0.2034 0.0009  -0.0110 0.0151  47  GLY   B O   
4662 N  N   . GLY   B 48  ? 0.1630 0.1567 0.1966 0.0045  -0.0092 0.0164  48  GLY   B N   
4663 C  CA  . GLY   B 48  ? 0.1610 0.1511 0.1954 -0.0022 -0.0140 0.0150  48  GLY   B CA  
4664 C  C   . GLY   B 48  ? 0.1554 0.1496 0.1821 -0.0004 -0.0018 0.0117  48  GLY   B C   
4665 O  O   . GLY   B 48  ? 0.1499 0.1487 0.2070 0.0006  -0.0124 0.0066  48  GLY   B O   
4669 N  N   . VAL   B 49  ? 0.1599 0.1530 0.1727 0.0094  -0.0052 0.0096  49  VAL   B N   
4670 C  CA  . VAL   B 49  ? 0.1595 0.1582 0.1627 0.0098  -0.0157 -0.0040 49  VAL   B CA  
4671 C  C   . VAL   B 49  ? 0.1526 0.1489 0.1434 0.0123  -0.0154 0.0009  49  VAL   B C   
4672 O  O   . VAL   B 49  ? 0.1576 0.1525 0.1614 0.0038  -0.0026 -0.0011 49  VAL   B O   
4673 C  CB  . VAL   B 49  ? 0.1611 0.1767 0.1860 0.0027  -0.0247 -0.0010 49  VAL   B CB  
4674 C  CG1 . VAL   B 49  ? 0.1612 0.1860 0.1855 0.0085  -0.0287 -0.0039 49  VAL   B CG1 
4675 C  CG2 . VAL   B 49  ? 0.1754 0.1887 0.2107 -0.0068 -0.0359 -0.0051 49  VAL   B CG2 
4685 N  N   . ALA   B 50  ? 0.1450 0.1462 0.1509 0.0025  -0.0091 0.0051  50  ALA   B N   
4686 C  CA  . ALA   B 50  ? 0.1455 0.1391 0.1487 0.0060  -0.0094 0.0011  50  ALA   B CA  
4687 C  C   . ALA   B 50  ? 0.1532 0.1463 0.1438 0.0022  -0.0070 0.0020  50  ALA   B C   
4688 O  O   . ALA   B 50  ? 0.1545 0.1424 0.1452 0.0032  -0.0038 -0.0008 50  ALA   B O   
4689 C  CB  . ALA   B 50  ? 0.1499 0.1382 0.1531 -0.0020 -0.0082 0.0079  50  ALA   B CB  
4695 N  N   . GLY   B 51  ? 0.1518 0.1550 0.1560 0.0099  -0.0157 0.0084  51  GLY   B N   
4696 C  CA  . GLY   B 51  ? 0.1552 0.1600 0.1694 0.0188  -0.0243 0.0009  51  GLY   B CA  
4697 C  C   . GLY   B 51  ? 0.1524 0.1521 0.1729 0.0161  -0.0171 0.0030  51  GLY   B C   
4698 O  O   . GLY   B 51  ? 0.1582 0.1646 0.1957 0.0042  -0.0166 -0.0026 51  GLY   B O   
4702 N  N   . ALA   B 52  ? 0.1501 0.1481 0.1690 0.0153  -0.0083 0.0068  52  ALA   B N   
4703 C  CA  . ALA   B 52  ? 0.1599 0.1566 0.1735 0.0137  -0.0019 -0.0025 52  ALA   B CA  
4704 C  C   . ALA   B 52  ? 0.1500 0.1536 0.1587 0.0056  -0.0025 -0.0009 52  ALA   B C   
4705 O  O   . ALA   B 52  ? 0.1475 0.1599 0.1776 0.0067  0.0011  0.0004  52  ALA   B O   
4706 C  CB  . ALA   B 52  ? 0.1765 0.1587 0.1766 0.0082  -0.0011 -0.0049 52  ALA   B CB  
4712 N  N   . LEU   B 53  ? 0.1436 0.1502 0.1569 0.0186  -0.0013 0.0001  53  LEU   B N   
4713 C  CA  . LEU   B 53  ? 0.1450 0.1581 0.1535 0.0128  -0.0046 -0.0042 53  LEU   B CA  
4714 C  C   . LEU   B 53  ? 0.1494 0.1506 0.1498 0.0104  -0.0001 0.0031  53  LEU   B C   
4715 O  O   . LEU   B 53  ? 0.1554 0.1566 0.1642 -0.0004 0.0037  0.0107  53  LEU   B O   
4716 C  CB  . LEU   B 53  ? 0.1473 0.1633 0.1722 0.0091  -0.0027 0.0127  53  LEU   B CB  
4717 C  CG  . LEU   B 53  ? 0.1419 0.1726 0.1621 0.0020  -0.0001 0.0098  53  LEU   B CG  
4718 C  CD1 . LEU   B 53  ? 0.1532 0.1857 0.1887 0.0101  -0.0046 -0.0001 53  LEU   B CD1 
4719 C  CD2 . LEU   B 53  ? 0.1600 0.2023 0.1873 -0.0092 -0.0088 -0.0147 53  LEU   B CD2 
4731 N  N   . ASN   B 54  ? 0.1470 0.1428 0.1502 0.0024  0.0011  0.0011  54  ASN   B N   
4732 C  CA  . ASN   B 54  ? 0.1512 0.1544 0.1574 0.0029  -0.0032 -0.0017 54  ASN   B CA  
4733 C  C   . ASN   B 54  ? 0.1500 0.1592 0.1726 0.0025  0.0026  0.0008  54  ASN   B C   
4734 O  O   . ASN   B 54  ? 0.1445 0.1620 0.1814 -0.0051 0.0033  -0.0020 54  ASN   B O   
4735 C  CB  . ASN   B 54  ? 0.1599 0.1699 0.1676 0.0079  0.0033  -0.0047 54  ASN   B CB  
4736 C  CG  . ASN   B 54  ? 0.1587 0.1722 0.1746 0.0058  -0.0138 -0.0009 54  ASN   B CG  
4737 O  OD1 . ASN   B 54  ? 0.1578 0.1681 0.1858 0.0014  -0.0154 -0.0147 54  ASN   B OD1 
4738 N  ND2 . ASN   B 54  ? 0.1702 0.1887 0.2050 0.0008  -0.0367 0.0083  54  ASN   B ND2 
4745 N  N   . LYS   B 55  ? 0.1473 0.1635 0.1978 0.0075  0.0048  0.0057  55  LYS   B N   
4746 C  CA  . LYS   B 55  ? 0.1555 0.1725 0.2182 0.0115  0.0010  -0.0017 55  LYS   B CA  
4747 C  C   . LYS   B 55  ? 0.1533 0.1682 0.2185 0.0098  0.0081  -0.0126 55  LYS   B C   
4748 O  O   . LYS   B 55  ? 0.1449 0.1846 0.2314 0.0061  0.0057  -0.0105 55  LYS   B O   
4749 C  CB  . LYS   B 55  ? 0.1701 0.1901 0.2664 0.0275  0.0136  0.0047  55  LYS   B CB  
4750 C  CG  . LYS   B 55  ? 0.2078 0.2188 0.3504 0.0396  0.0321  0.0166  55  LYS   B CG  
4751 C  CD  . LYS   B 55  ? 0.2462 0.2434 0.4197 0.0481  0.0467  0.0292  55  LYS   B CD  
4752 C  CE  . LYS   B 55  ? 0.2724 0.2649 0.4866 0.0468  0.0602  0.0363  55  LYS   B CE  
4753 N  NZ  . LYS   B 55  ? 0.2795 0.2797 0.5203 0.0426  0.0484  0.0474  55  LYS   B NZ  
4767 N  N   . ALA   B 56  ? 0.1492 0.1769 0.1982 0.0057  0.0048  -0.0144 56  ALA   B N   
4768 C  CA  . ALA   B 56  ? 0.1622 0.1957 0.1923 0.0025  0.0076  -0.0129 56  ALA   B CA  
4769 C  C   . ALA   B 56  ? 0.1649 0.1889 0.1840 0.0028  0.0135  -0.0083 56  ALA   B C   
4770 O  O   . ALA   B 56  ? 0.1773 0.1992 0.1963 0.0036  0.0267  -0.0040 56  ALA   B O   
4771 C  CB  . ALA   B 56  ? 0.1691 0.2155 0.1943 -0.0090 0.0007  -0.0114 56  ALA   B CB  
4777 N  N   . THR   B 57  ? 0.1562 0.1789 0.1945 -0.0021 0.0191  -0.0061 57  THR   B N   
4778 C  CA  . THR   B 57  ? 0.1638 0.1804 0.1869 -0.0056 0.0207  -0.0007 57  THR   B CA  
4779 C  C   . THR   B 57  ? 0.1625 0.1914 0.2106 -0.0021 0.0212  0.0025  57  THR   B C   
4780 O  O   . THR   B 57  ? 0.1721 0.1922 0.2191 -0.0202 0.0152  -0.0010 57  THR   B O   
4781 C  CB  . THR   B 57  ? 0.1693 0.1649 0.1661 -0.0067 0.0143  0.0028  57  THR   B CB  
4782 O  OG1 . THR   B 57  ? 0.1673 0.1640 0.1825 -0.0080 0.0138  -0.0016 57  THR   B OG1 
4783 C  CG2 . THR   B 57  ? 0.1661 0.1688 0.1683 -0.0070 0.0177  -0.0005 57  THR   B CG2 
4791 N  N   . ASN   B 58  ? 0.1487 0.2076 0.2328 -0.0131 0.0078  -0.0108 58  ASN   B N   
4792 C  CA  . ASN   B 58  ? 0.1713 0.2502 0.2749 -0.0258 0.0354  -0.0065 58  ASN   B CA  
4793 C  C   . ASN   B 58  ? 0.1575 0.2276 0.2318 -0.0179 0.0015  -0.0124 58  ASN   B C   
4794 O  O   . ASN   B 58  ? 0.1648 0.2352 0.2433 -0.0181 -0.0012 -0.0268 58  ASN   B O   
4795 C  CB  . ASN   B 58  ? 0.2656 0.3281 0.4040 -0.0421 0.0822  0.0123  58  ASN   B CB  
4796 C  CG  . ASN   B 58  ? 0.3832 0.4106 0.5549 -0.0443 0.1023  0.0362  58  ASN   B CG  
4797 O  OD1 . ASN   B 58  ? 0.4080 0.4268 0.6098 -0.0454 0.1058  0.0427  58  ASN   B OD1 
4798 N  ND2 . ASN   B 58  ? 0.4588 0.4588 0.6049 -0.0453 0.1118  0.0424  58  ASN   B ND2 
4805 N  N   . ASN   B 59  ? 0.1574 0.2109 0.2106 -0.0082 -0.0058 -0.0045 59  ASN   B N   
4806 C  CA  . ASN   B 59  ? 0.1615 0.2111 0.2020 -0.0095 -0.0164 0.0082  59  ASN   B CA  
4807 C  C   . ASN   B 59  ? 0.1532 0.2018 0.1910 -0.0144 -0.0149 -0.0068 59  ASN   B C   
4808 O  O   . ASN   B 59  ? 0.1543 0.2008 0.1906 -0.0160 -0.0083 -0.0096 59  ASN   B O   
4809 C  CB  . ASN   B 59  ? 0.1726 0.2299 0.2167 -0.0064 -0.0263 0.0064  59  ASN   B CB  
4810 C  CG  . ASN   B 59  ? 0.1790 0.2404 0.2333 -0.0022 -0.0427 0.0072  59  ASN   B CG  
4811 O  OD1 . ASN   B 59  ? 0.1791 0.2433 0.2343 -0.0021 -0.0285 0.0282  59  ASN   B OD1 
4812 N  ND2 . ASN   B 59  ? 0.1868 0.2498 0.2393 -0.0092 -0.0490 -0.0063 59  ASN   B ND2 
4819 N  N   . ALA   B 60  ? 0.1553 0.1890 0.1982 -0.0172 -0.0051 -0.0021 60  ALA   B N   
4820 C  CA  . ALA   B 60  ? 0.1652 0.1803 0.1948 -0.0176 -0.0079 0.0012  60  ALA   B CA  
4821 C  C   . ALA   B 60  ? 0.1653 0.1677 0.1705 -0.0159 -0.0073 -0.0015 60  ALA   B C   
4822 O  O   . ALA   B 60  ? 0.1680 0.1640 0.1857 -0.0236 0.0045  -0.0106 60  ALA   B O   
4823 C  CB  . ALA   B 60  ? 0.1807 0.1765 0.2219 -0.0181 0.0047  0.0036  60  ALA   B CB  
4829 N  N   . MET   B 61  ? 0.1562 0.1557 0.1670 -0.0116 -0.0035 0.0021  61  MET   B N   
4830 C  CA  . MET   B 61  ? 0.1496 0.1527 0.1641 -0.0124 -0.0115 0.0005  61  MET   B CA  
4831 C  C   . MET   B 61  ? 0.1587 0.1488 0.1568 -0.0120 -0.0125 0.0008  61  MET   B C   
4832 O  O   . MET   B 61  ? 0.1606 0.1490 0.1508 -0.0054 -0.0112 -0.0120 61  MET   B O   
4833 C  CB  . MET   B 61  ? 0.1434 0.1544 0.1609 -0.0062 -0.0094 0.0005  61  MET   B CB  
4834 C  CG  . MET   B 61  ? 0.1424 0.1527 0.1546 -0.0039 -0.0123 -0.0010 61  MET   B CG  
4835 S  SD  . MET   B 61  ? 0.1484 0.1556 0.1713 -0.0043 -0.0091 -0.0107 61  MET   B SD  
4836 C  CE  . MET   B 61  ? 0.1553 0.1703 0.1993 0.0016  -0.0077 -0.0277 61  MET   B CE  
4846 N  N   . GLN   B 62  ? 0.1559 0.1613 0.1571 -0.0087 -0.0228 0.0030  62  GLN   B N   
4847 C  CA  . GLN   B 62  ? 0.1552 0.1646 0.1656 -0.0051 -0.0270 -0.0065 62  GLN   B CA  
4848 C  C   . GLN   B 62  ? 0.1569 0.1666 0.1646 -0.0074 -0.0308 -0.0126 62  GLN   B C   
4849 O  O   . GLN   B 62  ? 0.1688 0.1621 0.1760 -0.0021 -0.0322 -0.0101 62  GLN   B O   
4850 C  CB  . GLN   B 62  ? 0.1606 0.1658 0.1710 0.0038  -0.0201 0.0016  62  GLN   B CB  
4851 C  CG  . GLN   B 62  ? 0.1686 0.1680 0.1676 0.0031  -0.0257 0.0004  62  GLN   B CG  
4852 C  CD  . GLN   B 62  ? 0.1690 0.1646 0.1604 0.0037  -0.0228 0.0078  62  GLN   B CD  
4853 O  OE1 . GLN   B 62  ? 0.1698 0.1662 0.1729 -0.0007 -0.0294 -0.0047 62  GLN   B OE1 
4854 N  NE2 . GLN   B 62  ? 0.1682 0.1664 0.1620 0.0033  -0.0233 -0.0093 62  GLN   B NE2 
4863 N  N   . VAL   B 63  ? 0.1575 0.1688 0.1891 -0.0088 -0.0316 -0.0147 63  VAL   B N   
4864 C  CA  . VAL   B 63  ? 0.1701 0.1722 0.2164 -0.0165 -0.0341 -0.0057 63  VAL   B CA  
4865 C  C   . VAL   B 63  ? 0.1705 0.1597 0.1949 -0.0234 -0.0384 -0.0157 63  VAL   B C   
4866 O  O   . VAL   B 63  ? 0.1832 0.1597 0.2025 -0.0180 -0.0471 -0.0126 63  VAL   B O   
4867 C  CB  . VAL   B 63  ? 0.1713 0.1850 0.2487 -0.0198 -0.0296 -0.0112 63  VAL   B CB  
4868 C  CG1 . VAL   B 63  ? 0.1803 0.1908 0.2523 -0.0334 -0.0243 -0.0147 63  VAL   B CG1 
4869 C  CG2 . VAL   B 63  ? 0.1631 0.2005 0.2602 -0.0165 -0.0385 -0.0141 63  VAL   B CG2 
4879 N  N   . GLU   B 64  ? 0.1677 0.1555 0.1828 -0.0147 -0.0266 -0.0097 64  GLU   B N   
4880 C  CA  . GLU   B 64  ? 0.1708 0.1495 0.1822 -0.0149 -0.0309 -0.0012 64  GLU   B CA  
4881 C  C   . GLU   B 64  ? 0.1652 0.1487 0.1598 -0.0066 -0.0283 -0.0077 64  GLU   B C   
4882 O  O   . GLU   B 64  ? 0.1713 0.1603 0.1604 -0.0084 -0.0303 -0.0177 64  GLU   B O   
4883 C  CB  . GLU   B 64  ? 0.1695 0.1542 0.1787 -0.0171 -0.0266 0.0020  64  GLU   B CB  
4884 C  CG  . GLU   B 64  ? 0.1733 0.1609 0.1661 -0.0228 -0.0289 -0.0108 64  GLU   B CG  
4885 C  CD  . GLU   B 64  ? 0.1783 0.1752 0.1740 -0.0327 -0.0313 -0.0037 64  GLU   B CD  
4886 O  OE1 . GLU   B 64  ? 0.1766 0.1867 0.1897 -0.0351 -0.0205 -0.0272 64  GLU   B OE1 
4887 O  OE2 . GLU   B 64  ? 0.1903 0.1874 0.1722 -0.0398 -0.0408 0.0002  64  GLU   B OE2 
4894 N  N   . SER   B 65  ? 0.1662 0.1445 0.1578 -0.0098 -0.0189 -0.0128 65  SER   B N   
4895 C  CA  . SER   B 65  ? 0.1661 0.1427 0.1581 -0.0001 -0.0238 -0.0113 65  SER   B CA  
4896 C  C   . SER   B 65  ? 0.1674 0.1465 0.1571 -0.0007 -0.0279 -0.0138 65  SER   B C   
4897 O  O   . SER   B 65  ? 0.1714 0.1580 0.1577 -0.0027 -0.0267 -0.0195 65  SER   B O   
4898 C  CB  . SER   B 65  ? 0.1653 0.1507 0.1517 -0.0107 -0.0216 -0.0123 65  SER   B CB  
4899 O  OG  . SER   B 65  ? 0.1683 0.1484 0.1627 -0.0124 -0.0165 -0.0163 65  SER   B OG  
4905 N  N   . ASP   B 66  ? 0.1783 0.1542 0.1599 -0.0017 -0.0323 -0.0139 66  ASP   B N   
4906 C  CA  . ASP   B 66  ? 0.1840 0.1663 0.1560 0.0044  -0.0373 -0.0114 66  ASP   B CA  
4907 C  C   . ASP   B 66  ? 0.1921 0.1668 0.1539 0.0008  -0.0276 -0.0157 66  ASP   B C   
4908 O  O   . ASP   B 66  ? 0.1943 0.1709 0.1646 0.0041  -0.0288 -0.0187 66  ASP   B O   
4909 C  CB  . ASP   B 66  ? 0.1974 0.1806 0.1774 0.0149  -0.0451 -0.0135 66  ASP   B CB  
4910 C  CG  . ASP   B 66  ? 0.2241 0.1968 0.2036 0.0210  -0.0596 -0.0031 66  ASP   B CG  
4911 O  OD1 . ASP   B 66  ? 0.2523 0.1882 0.1939 0.0118  -0.0573 0.0065  66  ASP   B OD1 
4912 O  OD2 . ASP   B 66  ? 0.2383 0.2191 0.2653 0.0390  -0.0557 -0.0018 66  ASP   B OD2 
4917 N  N   . ASP   B 67  ? 0.1837 0.1603 0.1468 -0.0046 -0.0269 -0.0213 67  ASP   B N   
4918 C  CA  . ASP   B 67  ? 0.1999 0.1577 0.1565 -0.0044 -0.0361 -0.0106 67  ASP   B CA  
4919 C  C   . ASP   B 67  ? 0.1943 0.1560 0.1723 0.0000  -0.0333 -0.0197 67  ASP   B C   
4920 O  O   . ASP   B 67  ? 0.1965 0.1620 0.1841 -0.0002 -0.0194 -0.0260 67  ASP   B O   
4921 C  CB  . ASP   B 67  ? 0.2235 0.1632 0.1730 -0.0088 -0.0445 -0.0053 67  ASP   B CB  
4922 C  CG  . ASP   B 67  ? 0.2569 0.1696 0.1939 -0.0117 -0.0646 -0.0073 67  ASP   B CG  
4923 O  OD1 . ASP   B 67  ? 0.2781 0.1784 0.2067 -0.0144 -0.0622 -0.0114 67  ASP   B OD1 
4924 O  OD2 . ASP   B 67  ? 0.2709 0.1762 0.2108 -0.0012 -0.0713 -0.0022 67  ASP   B OD2 
4929 N  N   . TYR   B 68  ? 0.1855 0.1556 0.1626 0.0002  -0.0436 -0.0242 68  TYR   B N   
4930 C  CA  . TYR   B 68  ? 0.1810 0.1726 0.1826 0.0067  -0.0413 -0.0300 68  TYR   B CA  
4931 C  C   . TYR   B 68  ? 0.1770 0.1689 0.1759 0.0010  -0.0312 -0.0382 68  TYR   B C   
4932 O  O   . TYR   B 68  ? 0.1835 0.1808 0.1884 0.0087  -0.0282 -0.0525 68  TYR   B O   
4933 C  CB  . TYR   B 68  ? 0.1793 0.1907 0.1935 0.0123  -0.0461 -0.0427 68  TYR   B CB  
4934 C  CG  . TYR   B 68  ? 0.1907 0.2125 0.2022 0.0170  -0.0375 -0.0680 68  TYR   B CG  
4935 C  CD1 . TYR   B 68  ? 0.1946 0.2178 0.2350 0.0008  -0.0342 -0.0653 68  TYR   B CD1 
4936 C  CD2 . TYR   B 68  ? 0.1952 0.2349 0.2209 0.0197  -0.0505 -0.0604 68  TYR   B CD2 
4937 C  CE1 . TYR   B 68  ? 0.2009 0.2328 0.2555 0.0017  -0.0340 -0.0668 68  TYR   B CE1 
4938 C  CE2 . TYR   B 68  ? 0.2000 0.2394 0.2287 0.0196  -0.0393 -0.0766 68  TYR   B CE2 
4939 C  CZ  . TYR   B 68  ? 0.1972 0.2402 0.2522 0.0076  -0.0367 -0.0726 68  TYR   B CZ  
4940 O  OH  . TYR   B 68  ? 0.1882 0.2601 0.2776 0.0066  -0.0307 -0.0490 68  TYR   B OH  
4950 N  N   . ILE   B 69  ? 0.1770 0.1639 0.1683 0.0067  -0.0320 -0.0342 69  ILE   B N   
4951 C  CA  . ILE   B 69  ? 0.1844 0.1748 0.1776 0.0003  -0.0262 -0.0337 69  ILE   B CA  
4952 C  C   . ILE   B 69  ? 0.1836 0.1717 0.1756 0.0058  -0.0334 -0.0294 69  ILE   B C   
4953 O  O   . ILE   B 69  ? 0.1883 0.1813 0.1657 0.0048  -0.0151 -0.0342 69  ILE   B O   
4954 C  CB  . ILE   B 69  ? 0.1908 0.1743 0.1976 -0.0028 -0.0043 -0.0271 69  ILE   B CB  
4955 C  CG1 . ILE   B 69  ? 0.1888 0.1737 0.2120 -0.0041 0.0042  -0.0253 69  ILE   B CG1 
4956 C  CG2 . ILE   B 69  ? 0.2041 0.1819 0.2111 -0.0013 -0.0041 -0.0179 69  ILE   B CG2 
4957 C  CD1 . ILE   B 69  ? 0.1846 0.1765 0.2301 -0.0150 0.0146  -0.0244 69  ILE   B CD1 
4969 N  N   . ALA   B 70  ? 0.1794 0.1693 0.1777 0.0064  -0.0361 -0.0262 70  ALA   B N   
4970 C  CA  . ALA   B 70  ? 0.1830 0.1697 0.1619 0.0011  -0.0422 -0.0233 70  ALA   B CA  
4971 C  C   . ALA   B 70  ? 0.1924 0.1651 0.1779 -0.0031 -0.0393 -0.0387 70  ALA   B C   
4972 O  O   . ALA   B 70  ? 0.1965 0.1691 0.1825 0.0060  -0.0395 -0.0384 70  ALA   B O   
4973 C  CB  . ALA   B 70  ? 0.1862 0.1874 0.1642 0.0000  -0.0355 -0.0253 70  ALA   B CB  
4979 N  N   . THR   B 71  ? 0.1970 0.1702 0.1855 0.0043  -0.0453 -0.0337 71  THR   B N   
4980 C  CA  . THR   B 71  ? 0.2100 0.1729 0.2076 0.0101  -0.0699 -0.0342 71  THR   B CA  
4981 C  C   . THR   B 71  ? 0.2044 0.1796 0.2317 0.0280  -0.0626 -0.0517 71  THR   B C   
4982 O  O   . THR   B 71  ? 0.2129 0.1862 0.2703 0.0336  -0.0551 -0.0606 71  THR   B O   
4983 C  CB  . THR   B 71  ? 0.2399 0.1902 0.2418 -0.0005 -0.0757 -0.0086 71  THR   B CB  
4984 O  OG1 . THR   B 71  ? 0.2538 0.2165 0.2775 -0.0198 -0.0765 0.0142  71  THR   B OG1 
4985 C  CG2 . THR   B 71  ? 0.2556 0.1865 0.2697 0.0051  -0.0704 0.0022  71  THR   B CG2 
4993 N  N   . ASN   B 72  ? 0.1925 0.1842 0.2273 0.0169  -0.0637 -0.0674 72  ASN   B N   
4994 C  CA  . ASN   B 72  ? 0.1907 0.1971 0.2354 0.0175  -0.0524 -0.0703 72  ASN   B CA  
4995 C  C   . ASN   B 72  ? 0.1924 0.2057 0.2439 0.0051  -0.0331 -0.0682 72  ASN   B C   
4996 O  O   . ASN   B 72  ? 0.1932 0.2190 0.2710 0.0066  -0.0146 -0.0687 72  ASN   B O   
4997 C  CB  . ASN   B 72  ? 0.1941 0.2052 0.2429 0.0146  -0.0637 -0.0611 72  ASN   B CB  
4998 C  CG  . ASN   B 72  ? 0.2117 0.2197 0.2535 0.0303  -0.0533 -0.0363 72  ASN   B CG  
4999 O  OD1 . ASN   B 72  ? 0.2309 0.2363 0.2497 0.0178  -0.0398 -0.0358 72  ASN   B OD1 
5000 N  ND2 . ASN   B 72  ? 0.2240 0.2270 0.2951 0.0477  -0.0451 -0.0069 72  ASN   B ND2 
5007 N  N   . GLY   B 73  ? 0.1956 0.2045 0.2205 0.0016  -0.0313 -0.0692 73  GLY   B N   
5008 C  CA  . GLY   B 73  ? 0.1936 0.2115 0.1991 -0.0022 -0.0199 -0.0567 73  GLY   B CA  
5009 C  C   . GLY   B 73  ? 0.1887 0.2078 0.1604 0.0047  -0.0227 -0.0446 73  GLY   B C   
5010 O  O   . GLY   B 73  ? 0.1823 0.1912 0.1716 0.0068  -0.0187 -0.0337 73  GLY   B O   
5014 N  N   . PRO   B 74  ? 0.1906 0.2168 0.1505 0.0021  -0.0315 -0.0410 74  PRO   B N   
5015 C  CA  . PRO   B 74  ? 0.1820 0.2169 0.1365 0.0041  -0.0201 -0.0230 74  PRO   B CA  
5016 C  C   . PRO   B 74  ? 0.1716 0.2018 0.1335 0.0063  -0.0139 -0.0125 74  PRO   B C   
5017 O  O   . PRO   B 74  ? 0.1772 0.2036 0.1787 0.0084  -0.0044 -0.0273 74  PRO   B O   
5018 C  CB  . PRO   B 74  ? 0.1968 0.2329 0.1512 0.0018  -0.0158 -0.0193 74  PRO   B CB  
5019 C  CG  . PRO   B 74  ? 0.2159 0.2445 0.1755 0.0034  -0.0131 -0.0160 74  PRO   B CG  
5020 C  CD  . PRO   B 74  ? 0.2151 0.2332 0.1675 0.0065  -0.0115 -0.0262 74  PRO   B CD  
5028 N  N   . LEU   B 75  ? 0.1651 0.1917 0.1282 0.0058  -0.0183 -0.0129 75  LEU   B N   
5029 C  CA  . LEU   B 75  ? 0.1712 0.1926 0.1333 0.0020  -0.0151 -0.0010 75  LEU   B CA  
5030 C  C   . LEU   B 75  ? 0.1769 0.2027 0.1398 0.0021  -0.0057 0.0009  75  LEU   B C   
5031 O  O   . LEU   B 75  ? 0.1961 0.2136 0.1450 -0.0061 -0.0063 -0.0015 75  LEU   B O   
5032 C  CB  . LEU   B 75  ? 0.1838 0.1925 0.1227 -0.0083 -0.0186 0.0062  75  LEU   B CB  
5033 C  CG  . LEU   B 75  ? 0.2152 0.2070 0.1487 -0.0283 -0.0073 0.0095  75  LEU   B CG  
5034 C  CD1 . LEU   B 75  ? 0.2435 0.2214 0.1533 -0.0345 0.0169  0.0012  75  LEU   B CD1 
5035 C  CD2 . LEU   B 75  ? 0.2499 0.2216 0.2185 -0.0212 0.0075  0.0158  75  LEU   B CD2 
5047 N  N   . LYS   B 76  ? 0.1732 0.2217 0.1595 -0.0006 0.0005  0.0099  76  LYS   B N   
5048 C  CA  . LYS   B 76  ? 0.1870 0.2291 0.1860 -0.0087 0.0214  0.0085  76  LYS   B CA  
5049 C  C   . LYS   B 76  ? 0.1830 0.2135 0.1645 -0.0038 0.0184  0.0248  76  LYS   B C   
5050 O  O   . LYS   B 76  ? 0.1825 0.1911 0.1654 -0.0041 0.0071  0.0175  76  LYS   B O   
5051 C  CB  . LYS   B 76  ? 0.2047 0.2355 0.2364 -0.0128 0.0396  -0.0193 76  LYS   B CB  
5052 C  CG  . LYS   B 76  ? 0.2153 0.2547 0.2785 -0.0025 0.0335  -0.0268 76  LYS   B CG  
5053 C  CD  . LYS   B 76  ? 0.2162 0.2643 0.3056 0.0035  0.0313  -0.0367 76  LYS   B CD  
5054 C  CE  . LYS   B 76  ? 0.2185 0.2788 0.3544 0.0045  0.0223  -0.0456 76  LYS   B CE  
5055 N  NZ  . LYS   B 76  ? 0.2195 0.2840 0.3694 0.0045  0.0069  -0.0660 76  LYS   B NZ  
5069 N  N   . VAL   B 77  ? 0.1937 0.2224 0.1748 0.0026  0.0170  0.0296  77  VAL   B N   
5070 C  CA  . VAL   B 77  ? 0.1942 0.2111 0.1910 0.0094  0.0209  0.0548  77  VAL   B CA  
5071 C  C   . VAL   B 77  ? 0.1787 0.1874 0.1854 0.0160  0.0276  0.0397  77  VAL   B C   
5072 O  O   . VAL   B 77  ? 0.1825 0.1855 0.1848 0.0277  0.0364  0.0319  77  VAL   B O   
5073 C  CB  . VAL   B 77  ? 0.2081 0.2217 0.2257 0.0100  0.0308  0.0680  77  VAL   B CB  
5074 C  CG1 . VAL   B 77  ? 0.2076 0.2159 0.2503 0.0075  0.0284  0.0812  77  VAL   B CG1 
5075 C  CG2 . VAL   B 77  ? 0.2218 0.2384 0.2466 0.0058  0.0095  0.0680  77  VAL   B CG2 
5085 N  N   . GLY   B 78  ? 0.1709 0.1758 0.1785 0.0066  0.0252  0.0291  78  GLY   B N   
5086 C  CA  . GLY   B 78  ? 0.1712 0.1759 0.1749 0.0032  0.0291  0.0245  78  GLY   B CA  
5087 C  C   . GLY   B 78  ? 0.1611 0.1665 0.1718 0.0099  0.0217  0.0196  78  GLY   B C   
5088 O  O   . GLY   B 78  ? 0.1621 0.1656 0.1828 0.0137  0.0146  0.0257  78  GLY   B O   
5092 N  N   . GLY   B 79  ? 0.1554 0.1694 0.1666 0.0078  0.0184  0.0187  79  GLY   B N   
5093 C  CA  . GLY   B 79  ? 0.1594 0.1588 0.1598 0.0139  0.0138  0.0141  79  GLY   B CA  
5094 C  C   . GLY   B 79  ? 0.1507 0.1520 0.1569 0.0071  0.0085  0.0082  79  GLY   B C   
5095 O  O   . GLY   B 79  ? 0.1580 0.1460 0.1706 0.0076  0.0172  0.0176  79  GLY   B O   
5099 N  N   . SER   B 80  ? 0.1477 0.1490 0.1641 0.0066  0.0169  0.0091  80  SER   B N   
5100 C  CA  . SER   B 80  ? 0.1432 0.1505 0.1615 0.0048  0.0004  0.0064  80  SER   B CA  
5101 C  C   . SER   B 80  ? 0.1477 0.1415 0.1542 0.0073  -0.0048 0.0061  80  SER   B C   
5102 O  O   . SER   B 80  ? 0.1575 0.1430 0.1790 0.0069  0.0066  0.0022  80  SER   B O   
5103 C  CB  . SER   B 80  ? 0.1469 0.1479 0.1627 -0.0022 0.0045  0.0140  80  SER   B CB  
5104 O  OG  . SER   B 80  ? 0.1535 0.1618 0.1845 -0.0045 -0.0114 0.0116  80  SER   B OG  
5110 N  N   . CYS   B 81  ? 0.1434 0.1322 0.1617 -0.0036 -0.0108 0.0001  81  CYS   B N   
5111 C  CA  . CYS   B 81  ? 0.1512 0.1283 0.1606 0.0055  -0.0165 0.0041  81  CYS   B CA  
5112 C  C   . CYS   B 81  ? 0.1484 0.1332 0.1359 -0.0024 -0.0103 0.0021  81  CYS   B C   
5113 O  O   . CYS   B 81  ? 0.1645 0.1325 0.1535 0.0052  -0.0024 -0.0042 81  CYS   B O   
5114 C  CB  . CYS   B 81  ? 0.1665 0.1394 0.1627 0.0003  -0.0154 0.0026  81  CYS   B CB  
5115 S  SG  . CYS   B 81  ? 0.1644 0.1610 0.1557 -0.0052 -0.0242 -0.0068 81  CYS   B SG  
5121 N  N   . VAL   B 82  ? 0.1512 0.1334 0.1546 -0.0033 -0.0155 0.0022  82  VAL   B N   
5122 C  CA  . VAL   B 82  ? 0.1578 0.1350 0.1433 -0.0130 -0.0128 0.0117  82  VAL   B CA  
5123 C  C   . VAL   B 82  ? 0.1645 0.1273 0.1521 -0.0064 -0.0024 -0.0031 82  VAL   B C   
5124 O  O   . VAL   B 82  ? 0.1696 0.1282 0.1916 -0.0060 -0.0108 -0.0141 82  VAL   B O   
5125 C  CB  . VAL   B 82  ? 0.1673 0.1519 0.1614 -0.0079 -0.0108 0.0096  82  VAL   B CB  
5126 C  CG1 . VAL   B 82  ? 0.1877 0.1745 0.1747 0.0024  -0.0111 0.0200  82  VAL   B CG1 
5127 C  CG2 . VAL   B 82  ? 0.1710 0.1681 0.1764 -0.0122 -0.0276 0.0193  82  VAL   B CG2 
5137 N  N   . LEU   B 83  ? 0.1492 0.1241 0.1552 -0.0146 -0.0164 -0.0101 83  LEU   B N   
5138 C  CA  . LEU   B 83  ? 0.1537 0.1298 0.1518 -0.0152 -0.0178 -0.0046 83  LEU   B CA  
5139 C  C   . LEU   B 83  ? 0.1517 0.1288 0.1563 -0.0213 -0.0178 -0.0008 83  LEU   B C   
5140 O  O   . LEU   B 83  ? 0.1565 0.1389 0.1408 -0.0232 -0.0164 0.0023  83  LEU   B O   
5141 C  CB  . LEU   B 83  ? 0.1594 0.1451 0.1413 -0.0187 -0.0229 -0.0117 83  LEU   B CB  
5142 C  CG  . LEU   B 83  ? 0.1771 0.1670 0.1488 -0.0209 -0.0095 -0.0051 83  LEU   B CG  
5143 C  CD1 . LEU   B 83  ? 0.1893 0.1721 0.1541 -0.0141 -0.0208 -0.0030 83  LEU   B CD1 
5144 C  CD2 . LEU   B 83  ? 0.1954 0.1689 0.1571 -0.0117 -0.0154 -0.0176 83  LEU   B CD2 
5156 N  N   . SER   B 84  ? 0.1593 0.1411 0.1686 -0.0236 -0.0210 0.0032  84  SER   B N   
5157 C  CA  . SER   B 84  ? 0.1594 0.1640 0.1568 -0.0270 -0.0186 0.0165  84  SER   B CA  
5158 C  C   . SER   B 84  ? 0.1519 0.1756 0.1199 -0.0236 -0.0135 0.0179  84  SER   B C   
5159 O  O   . SER   B 84  ? 0.1597 0.1660 0.1252 -0.0214 -0.0146 0.0038  84  SER   B O   
5160 C  CB  . SER   B 84  ? 0.1775 0.1683 0.1954 -0.0312 0.0058  0.0150  84  SER   B CB  
5161 O  OG  . SER   B 84  ? 0.1729 0.1787 0.2331 -0.0392 0.0075  0.0248  84  SER   B OG  
5167 N  N   . GLY   B 85  ? 0.1546 0.1936 0.1377 -0.0303 -0.0166 0.0200  85  GLY   B N   
5168 C  CA  . GLY   B 85  ? 0.1555 0.2002 0.1546 -0.0361 -0.0130 -0.0097 85  GLY   B CA  
5169 C  C   . GLY   B 85  ? 0.1560 0.1886 0.1419 -0.0461 -0.0060 0.0043  85  GLY   B C   
5170 O  O   . GLY   B 85  ? 0.1641 0.1883 0.1536 -0.0506 0.0099  -0.0077 85  GLY   B O   
5174 N  N   . HIS   B 86  ? 0.1552 0.1751 0.1533 -0.0329 -0.0135 0.0161  86  HIS   B N   
5175 C  CA  . HIS   B 86  ? 0.1597 0.1741 0.1535 -0.0349 -0.0152 0.0157  86  HIS   B CA  
5176 C  C   . HIS   B 86  ? 0.1587 0.1853 0.1522 -0.0444 -0.0067 0.0302  86  HIS   B C   
5177 O  O   . HIS   B 86  ? 0.1712 0.1991 0.1580 -0.0374 0.0100  0.0249  86  HIS   B O   
5178 C  CB  . HIS   B 86  ? 0.1681 0.1781 0.1635 -0.0247 -0.0210 0.0041  86  HIS   B CB  
5179 C  CG  . HIS   B 86  ? 0.1681 0.1837 0.1622 -0.0153 -0.0176 0.0114  86  HIS   B CG  
5180 N  ND1 . HIS   B 86  ? 0.1762 0.2028 0.1796 -0.0250 -0.0317 -0.0006 86  HIS   B ND1 
5181 C  CD2 . HIS   B 86  ? 0.1708 0.1850 0.1588 -0.0062 -0.0199 0.0069  86  HIS   B CD2 
5182 C  CE1 . HIS   B 86  ? 0.1873 0.2012 0.1689 -0.0133 -0.0124 -0.0173 86  HIS   B CE1 
5183 N  NE2 . HIS   B 86  ? 0.1804 0.1917 0.1510 -0.0004 -0.0146 -0.0022 86  HIS   B NE2 
5191 N  N   . ASN   B 87  ? 0.1591 0.1860 0.1592 -0.0353 -0.0012 0.0199  87  ASN   B N   
5192 C  CA  . ASN   B 87  ? 0.1665 0.2024 0.1667 -0.0367 0.0189  0.0198  87  ASN   B CA  
5193 C  C   . ASN   B 87  ? 0.1829 0.1894 0.1517 -0.0296 0.0326  0.0163  87  ASN   B C   
5194 O  O   . ASN   B 87  ? 0.2094 0.2001 0.1906 -0.0221 0.0513  0.0094  87  ASN   B O   
5195 C  CB  . ASN   B 87  ? 0.1724 0.2423 0.1997 -0.0304 0.0238  0.0156  87  ASN   B CB  
5196 C  CG  . ASN   B 87  ? 0.1784 0.2610 0.2024 0.0011  0.0307  0.0309  87  ASN   B CG  
5197 O  OD1 . ASN   B 87  ? 0.1710 0.2491 0.1907 0.0051  0.0436  0.0451  87  ASN   B OD1 
5198 N  ND2 . ASN   B 87  ? 0.2097 0.2723 0.2401 0.0118  0.0365  0.0353  87  ASN   B ND2 
5205 N  N   . LEU   B 88  ? 0.1679 0.1754 0.1400 -0.0336 0.0128  0.0090  88  LEU   B N   
5206 C  CA  . LEU   B 88  ? 0.1829 0.1743 0.1462 -0.0333 0.0073  -0.0017 88  LEU   B CA  
5207 C  C   . LEU   B 88  ? 0.1797 0.1626 0.1490 -0.0370 0.0017  0.0004  88  LEU   B C   
5208 O  O   . LEU   B 88  ? 0.2085 0.1697 0.1760 -0.0246 -0.0267 -0.0057 88  LEU   B O   
5209 C  CB  . LEU   B 88  ? 0.1980 0.1799 0.1661 -0.0416 -0.0070 0.0072  88  LEU   B CB  
5210 C  CG  . LEU   B 88  ? 0.2369 0.2067 0.1920 -0.0331 -0.0276 0.0176  88  LEU   B CG  
5211 C  CD1 . LEU   B 88  ? 0.2498 0.2351 0.2062 -0.0434 -0.0216 0.0365  88  LEU   B CD1 
5212 C  CD2 . LEU   B 88  ? 0.2747 0.2304 0.2585 0.0015  -0.0439 0.0063  88  LEU   B CD2 
5224 N  N   . ALA   B 89  ? 0.1670 0.1620 0.1411 -0.0390 0.0172  -0.0025 89  ALA   B N   
5225 C  CA  . ALA   B 89  ? 0.1649 0.1546 0.1275 -0.0397 0.0076  0.0066  89  ALA   B CA  
5226 C  C   . ALA   B 89  ? 0.1801 0.1594 0.1282 -0.0438 0.0074  0.0044  89  ALA   B C   
5227 O  O   . ALA   B 89  ? 0.1595 0.1697 0.1683 -0.0418 0.0095  -0.0240 89  ALA   B O   
5228 C  CB  . ALA   B 89  ? 0.1575 0.1550 0.1410 -0.0347 0.0046  0.0108  89  ALA   B CB  
5234 N  N   . LYS   B 90  ? 0.2129 0.1485 0.1334 -0.0510 -0.0102 0.0120  90  LYS   B N   
5235 C  CA  . LYS   B 90  ? 0.2234 0.1473 0.1274 -0.0485 -0.0143 0.0130  90  LYS   B CA  
5236 C  C   . LYS   B 90  ? 0.1992 0.1450 0.1429 -0.0430 -0.0130 0.0049  90  LYS   B C   
5237 O  O   . LYS   B 90  ? 0.2036 0.1556 0.1639 -0.0550 -0.0079 0.0055  90  LYS   B O   
5238 C  CB  . LYS   B 90  ? 0.2425 0.1532 0.1579 -0.0394 -0.0068 0.0199  90  LYS   B CB  
5239 C  CG  . LYS   B 90  ? 0.2462 0.1658 0.1666 -0.0281 0.0235  0.0179  90  LYS   B CG  
5240 C  CD  . LYS   B 90  ? 0.2745 0.1874 0.2041 -0.0172 0.0459  -0.0081 90  LYS   B CD  
5241 C  CE  . LYS   B 90  ? 0.2866 0.2006 0.2536 -0.0222 0.0681  -0.0149 90  LYS   B CE  
5242 N  NZ  . LYS   B 90  ? 0.2987 0.1934 0.2455 -0.0385 0.0890  -0.0154 90  LYS   B NZ  
5256 N  N   . HIS   B 91  ? 0.1734 0.1333 0.1345 -0.0321 -0.0160 0.0100  91  HIS   B N   
5257 C  CA  . HIS   B 91  ? 0.1609 0.1367 0.1378 -0.0254 -0.0136 0.0034  91  HIS   B CA  
5258 C  C   . HIS   B 91  ? 0.1525 0.1373 0.1281 -0.0292 -0.0025 0.0038  91  HIS   B C   
5259 O  O   . HIS   B 91  ? 0.1666 0.1415 0.1336 -0.0304 -0.0215 0.0049  91  HIS   B O   
5260 C  CB  . HIS   B 91  ? 0.1810 0.1413 0.1759 -0.0117 -0.0029 0.0187  91  HIS   B CB  
5261 C  CG  . HIS   B 91  ? 0.2208 0.1545 0.2456 0.0022  0.0216  0.0304  91  HIS   B CG  
5262 N  ND1 . HIS   B 91  ? 0.2501 0.1630 0.3033 -0.0007 0.0275  0.0173  91  HIS   B ND1 
5263 C  CD2 . HIS   B 91  ? 0.2336 0.1820 0.2954 0.0133  0.0146  0.0596  91  HIS   B CD2 
5264 C  CE1 . HIS   B 91  ? 0.2544 0.1769 0.3218 0.0138  0.0309  0.0198  91  HIS   B CE1 
5265 N  NE2 . HIS   B 91  ? 0.2481 0.1884 0.3267 0.0237  0.0248  0.0618  91  HIS   B NE2 
5273 N  N   . CYS   B 92  ? 0.1476 0.1365 0.1303 -0.0264 -0.0140 0.0079  92  CYS   B N   
5274 C  CA  . CYS   B 92  ? 0.1443 0.1358 0.1228 -0.0229 -0.0056 0.0065  92  CYS   B CA  
5275 C  C   . CYS   B 92  ? 0.1439 0.1288 0.1193 -0.0148 -0.0061 0.0028  92  CYS   B C   
5276 O  O   . CYS   B 92  ? 0.1510 0.1348 0.1402 -0.0180 -0.0059 -0.0040 92  CYS   B O   
5277 C  CB  . CYS   B 92  ? 0.1460 0.1364 0.1392 -0.0185 -0.0084 -0.0013 92  CYS   B CB  
5278 S  SG  . CYS   B 92  ? 0.1478 0.1395 0.1344 -0.0127 -0.0122 0.0062  92  CYS   B SG  
5284 N  N   . LEU   B 93  ? 0.1363 0.1312 0.1239 -0.0143 -0.0073 -0.0028 93  LEU   B N   
5285 C  CA  . LEU   B 93  ? 0.1354 0.1321 0.1237 -0.0060 -0.0110 0.0059  93  LEU   B CA  
5286 C  C   . LEU   B 93  ? 0.1298 0.1293 0.1199 -0.0025 -0.0071 0.0116  93  LEU   B C   
5287 O  O   . LEU   B 93  ? 0.1403 0.1246 0.1420 -0.0079 -0.0074 0.0028  93  LEU   B O   
5288 C  CB  . LEU   B 93  ? 0.1415 0.1322 0.1375 -0.0011 -0.0020 0.0055  93  LEU   B CB  
5289 C  CG  . LEU   B 93  ? 0.1427 0.1390 0.1599 -0.0019 -0.0062 0.0176  93  LEU   B CG  
5290 C  CD1 . LEU   B 93  ? 0.1420 0.1488 0.1631 0.0052  -0.0023 0.0031  93  LEU   B CD1 
5291 C  CD2 . LEU   B 93  ? 0.1431 0.1383 0.1678 -0.0065 -0.0115 0.0051  93  LEU   B CD2 
5303 N  N   . HIS   B 94  ? 0.1387 0.1271 0.1183 -0.0075 -0.0135 0.0102  94  HIS   B N   
5304 C  CA  . HIS   B 94  ? 0.1430 0.1242 0.1225 0.0005  -0.0116 0.0035  94  HIS   B CA  
5305 C  C   . HIS   B 94  ? 0.1381 0.1285 0.1325 -0.0036 -0.0077 0.0086  94  HIS   B C   
5306 O  O   . HIS   B 94  ? 0.1395 0.1364 0.1766 -0.0074 0.0113  -0.0098 94  HIS   B O   
5307 C  CB  . HIS   B 94  ? 0.1395 0.1289 0.1312 -0.0004 -0.0134 0.0055  94  HIS   B CB  
5308 C  CG  . HIS   B 94  ? 0.1453 0.1269 0.1331 -0.0060 -0.0262 0.0023  94  HIS   B CG  
5309 N  ND1 . HIS   B 94  ? 0.1454 0.1319 0.1371 -0.0056 -0.0256 0.0003  94  HIS   B ND1 
5310 C  CD2 . HIS   B 94  ? 0.1434 0.1315 0.1378 -0.0060 -0.0187 0.0059  94  HIS   B CD2 
5311 C  CE1 . HIS   B 94  ? 0.1489 0.1322 0.1424 -0.0105 -0.0201 0.0038  94  HIS   B CE1 
5312 N  NE2 . HIS   B 94  ? 0.1436 0.1367 0.1475 -0.0196 -0.0210 0.0011  94  HIS   B NE2 
5320 N  N   . VAL   B 95  ? 0.1340 0.1266 0.1411 -0.0006 -0.0056 0.0034  95  VAL   B N   
5321 C  CA  . VAL   B 95  ? 0.1342 0.1333 0.1406 -0.0048 0.0014  0.0147  95  VAL   B CA  
5322 C  C   . VAL   B 95  ? 0.1451 0.1329 0.1427 -0.0015 0.0079  0.0102  95  VAL   B C   
5323 O  O   . VAL   B 95  ? 0.1476 0.1298 0.1657 0.0067  -0.0001 0.0167  95  VAL   B O   
5324 C  CB  . VAL   B 95  ? 0.1384 0.1311 0.1508 -0.0079 -0.0060 0.0116  95  VAL   B CB  
5325 C  CG1 . VAL   B 95  ? 0.1469 0.1546 0.1696 -0.0124 -0.0067 0.0213  95  VAL   B CG1 
5326 C  CG2 . VAL   B 95  ? 0.1482 0.1301 0.1440 -0.0045 -0.0064 0.0079  95  VAL   B CG2 
5336 N  N   . VAL   B 96  ? 0.1527 0.1390 0.1467 0.0061  0.0050  0.0138  96  VAL   B N   
5337 C  CA  . VAL   B 96  ? 0.1615 0.1466 0.1386 0.0065  -0.0004 0.0230  96  VAL   B CA  
5338 C  C   . VAL   B 96  ? 0.1666 0.1514 0.1471 0.0086  0.0096  0.0180  96  VAL   B C   
5339 O  O   . VAL   B 96  ? 0.1705 0.1561 0.1721 0.0013  0.0228  0.0077  96  VAL   B O   
5340 C  CB  . VAL   B 96  ? 0.1665 0.1640 0.1412 0.0080  0.0030  0.0197  96  VAL   B CB  
5341 C  CG1 . VAL   B 96  ? 0.1663 0.1806 0.1590 0.0150  0.0107  0.0066  96  VAL   B CG1 
5342 C  CG2 . VAL   B 96  ? 0.1715 0.1700 0.1519 0.0038  0.0098  0.0117  96  VAL   B CG2 
5352 N  N   . GLY   B 97  ? 0.1730 0.1515 0.1473 0.0058  0.0046  0.0246  97  GLY   B N   
5353 C  CA  . GLY   B 97  ? 0.1905 0.1554 0.1604 0.0055  0.0088  0.0277  97  GLY   B CA  
5354 C  C   . GLY   B 97  ? 0.2102 0.1697 0.1736 0.0128  0.0124  0.0305  97  GLY   B C   
5355 O  O   . GLY   B 97  ? 0.2238 0.1748 0.1682 0.0063  0.0051  0.0149  97  GLY   B O   
5359 N  N   . PRO   B 98  ? 0.2269 0.1777 0.1983 0.0177  0.0411  0.0422  98  PRO   B N   
5360 C  CA  . PRO   B 98  ? 0.2439 0.1950 0.2089 0.0287  0.0526  0.0401  98  PRO   B CA  
5361 C  C   . PRO   B 98  ? 0.2583 0.1941 0.1812 0.0456  0.0608  0.0628  98  PRO   B C   
5362 O  O   . PRO   B 98  ? 0.2473 0.1870 0.1975 0.0396  0.0605  0.0568  98  PRO   B O   
5363 C  CB  . PRO   B 98  ? 0.2334 0.2045 0.2220 0.0229  0.0633  0.0406  98  PRO   B CB  
5364 C  CG  . PRO   B 98  ? 0.2265 0.1934 0.2208 0.0184  0.0509  0.0658  98  PRO   B CG  
5365 C  CD  . PRO   B 98  ? 0.2136 0.1819 0.2230 0.0193  0.0518  0.0570  98  PRO   B CD  
5373 N  N   . ASN   B 99  ? 0.2736 0.2177 0.1812 0.0629  0.0651  0.0419  99  ASN   B N   
5374 C  CA  . ASN   B 99  ? 0.2973 0.2326 0.1925 0.0746  0.0585  0.0677  99  ASN   B CA  
5375 C  C   . ASN   B 99  ? 0.3265 0.2712 0.2370 0.0733  0.0749  0.1053  99  ASN   B C   
5376 O  O   . ASN   B 99  ? 0.3370 0.2804 0.2450 0.0814  0.0709  0.1096  99  ASN   B O   
5377 C  CB  . ASN   B 99  ? 0.3074 0.2266 0.1934 0.0735  0.0454  0.0575  99  ASN   B CB  
5378 C  CG  . ASN   B 99  ? 0.3137 0.2326 0.2097 0.0670  0.0390  0.0500  99  ASN   B CG  
5379 O  OD1 . ASN   B 99  ? 0.3160 0.2293 0.2354 0.0714  0.0452  0.0590  99  ASN   B OD1 
5380 N  ND2 . ASN   B 99  ? 0.3117 0.2347 0.2187 0.0683  0.0112  0.0345  99  ASN   B ND2 
5387 N  N   A VAL   B 100 ? 0.3447 0.2855 0.2803 0.0577  0.0788  0.1309  100 VAL   B N   
5388 N  N   B VAL   B 100 ? 0.3473 0.2862 0.2824 0.0600  0.0669  0.1192  100 VAL   B N   
5389 C  CA  A VAL   B 100 ? 0.3711 0.3036 0.3378 0.0415  0.0714  0.1479  100 VAL   B CA  
5390 C  CA  B VAL   B 100 ? 0.3726 0.3019 0.3299 0.0466  0.0542  0.1291  100 VAL   B CA  
5391 C  C   A VAL   B 100 ? 0.3929 0.3112 0.3283 0.0475  0.0655  0.1642  100 VAL   B C   
5392 C  C   B VAL   B 100 ? 0.3927 0.3090 0.3282 0.0495  0.0513  0.1499  100 VAL   B C   
5393 O  O   A VAL   B 100 ? 0.4012 0.3242 0.3364 0.0467  0.0754  0.1568  100 VAL   B O   
5394 O  O   B VAL   B 100 ? 0.3977 0.3152 0.3324 0.0481  0.0540  0.1435  100 VAL   B O   
5395 C  CB  A VAL   B 100 ? 0.3775 0.3143 0.4035 0.0176  0.0694  0.1494  100 VAL   B CB  
5396 C  CB  B VAL   B 100 ? 0.3784 0.3102 0.3759 0.0304  0.0461  0.1200  100 VAL   B CB  
5397 C  CG1 A VAL   B 100 ? 0.3827 0.3192 0.4317 0.0141  0.0654  0.1457  100 VAL   B CG1 
5398 C  CG1 B VAL   B 100 ? 0.3818 0.3134 0.3938 0.0267  0.0425  0.1158  100 VAL   B CG1 
5399 C  CG2 A VAL   B 100 ? 0.3764 0.3172 0.4213 0.0057  0.0719  0.1562  100 VAL   B CG2 
5400 C  CG2 B VAL   B 100 ? 0.3790 0.3131 0.3914 0.0235  0.0439  0.1184  100 VAL   B CG2 
5419 N  N   . ASN   B 101 ? 0.4076 0.3128 0.3293 0.0553  0.0464  0.1656  101 ASN   B N   
5420 C  CA  . ASN   B 101 ? 0.4436 0.3265 0.3391 0.0611  0.0218  0.1665  101 ASN   B CA  
5421 C  C   . ASN   B 101 ? 0.4869 0.3698 0.3441 0.0567  0.0111  0.1716  101 ASN   B C   
5422 O  O   . ASN   B 101 ? 0.4912 0.3816 0.3641 0.0600  0.0150  0.1476  101 ASN   B O   
5423 C  CB  . ASN   B 101 ? 0.4385 0.3043 0.3614 0.0603  0.0236  0.1449  101 ASN   B CB  
5424 C  CG  . ASN   B 101 ? 0.4322 0.2822 0.3708 0.0654  0.0226  0.1417  101 ASN   B CG  
5425 O  OD1 . ASN   B 101 ? 0.4321 0.2792 0.3927 0.0562  0.0352  0.1338  101 ASN   B OD1 
5426 N  ND2 . ASN   B 101 ? 0.4275 0.2755 0.3645 0.0718  0.0193  0.1274  101 ASN   B ND2 
5434 N  N   . LYS   B 102 ? 0.5231 0.4094 0.3696 0.0419  0.0144  0.1664  102 LYS   B N   
5435 C  CA  . LYS   B 102 ? 0.5566 0.4544 0.3992 0.0232  0.0220  0.1372  102 LYS   B CA  
5436 C  C   . LYS   B 102 ? 0.5530 0.4605 0.3801 0.0200  0.0274  0.1465  102 LYS   B C   
5437 O  O   . LYS   B 102 ? 0.5616 0.4663 0.3944 0.0194  0.0121  0.1435  102 LYS   B O   
5438 C  CB  . LYS   B 102 ? 0.5890 0.4907 0.4646 0.0084  0.0331  0.0880  102 LYS   B CB  
5439 C  CG  . LYS   B 102 ? 0.6163 0.5225 0.5274 -0.0049 0.0453  0.0407  102 LYS   B CG  
5440 C  CD  . LYS   B 102 ? 0.6387 0.5482 0.5949 -0.0145 0.0576  0.0021  102 LYS   B CD  
5441 C  CE  . LYS   B 102 ? 0.6558 0.5665 0.6449 -0.0221 0.0659  -0.0252 102 LYS   B CE  
5442 N  NZ  . LYS   B 102 ? 0.6635 0.5764 0.6745 -0.0253 0.0682  -0.0399 102 LYS   B NZ  
5456 N  N   . GLY   B 103 ? 0.5371 0.4577 0.3800 0.0183  0.0485  0.1425  103 GLY   B N   
5457 C  CA  . GLY   B 103 ? 0.5174 0.4515 0.3890 0.0191  0.0671  0.1217  103 GLY   B CA  
5458 C  C   . GLY   B 103 ? 0.4930 0.4399 0.3912 0.0207  0.0835  0.0981  103 GLY   B C   
5459 O  O   . GLY   B 103 ? 0.4967 0.4450 0.3929 0.0214  0.0900  0.1027  103 GLY   B O   
5463 N  N   A GLU   B 104 ? 0.4780 0.4299 0.3822 0.0233  0.0984  0.0831  104 GLU   B N   
5464 N  N   B GLU   B 104 ? 0.4768 0.4297 0.3895 0.0190  0.0773  0.0784  104 GLU   B N   
5465 C  CA  A GLU   B 104 ? 0.4609 0.4185 0.3690 0.0292  0.1076  0.0639  104 GLU   B CA  
5466 C  CA  B GLU   B 104 ? 0.4591 0.4180 0.3823 0.0188  0.0689  0.0547  104 GLU   B CA  
5467 C  C   A GLU   B 104 ? 0.4580 0.4156 0.3769 0.0143  0.1468  0.0701  104 GLU   B C   
5468 C  C   B GLU   B 104 ? 0.4530 0.4148 0.3931 0.0125  0.0833  0.0491  104 GLU   B C   
5469 O  O   A GLU   B 104 ? 0.4591 0.4196 0.3917 0.0106  0.1491  0.0715  104 GLU   B O   
5470 O  O   B GLU   B 104 ? 0.4539 0.4165 0.3999 0.0109  0.0840  0.0482  104 GLU   B O   
5471 C  CB  A GLU   B 104 ? 0.4489 0.4073 0.3569 0.0507  0.0736  0.0309  104 GLU   B CB  
5472 C  CB  B GLU   B 104 ? 0.4486 0.4080 0.3677 0.0248  0.0452  0.0316  104 GLU   B CB  
5473 C  CG  A GLU   B 104 ? 0.4364 0.3971 0.3376 0.0733  0.0399  -0.0029 104 GLU   B CG  
5474 C  CG  B GLU   B 104 ? 0.4393 0.3994 0.3519 0.0315  0.0219  0.0082  104 GLU   B CG  
5475 C  CD  A GLU   B 104 ? 0.4245 0.3865 0.3124 0.0957  0.0095  -0.0262 104 GLU   B CD  
5476 C  CD  B GLU   B 104 ? 0.4319 0.3915 0.3359 0.0377  0.0019  -0.0081 104 GLU   B CD  
5477 O  OE1 A GLU   B 104 ? 0.4137 0.3751 0.2688 0.1106  0.0140  -0.0377 104 GLU   B OE1 
5478 O  OE1 B GLU   B 104 ? 0.4272 0.3858 0.3161 0.0406  0.0015  -0.0125 104 GLU   B OE1 
5479 O  OE2 A GLU   B 104 ? 0.4231 0.3871 0.3024 0.1001  -0.0149 -0.0396 104 GLU   B OE2 
5480 O  OE2 B GLU   B 104 ? 0.4306 0.3905 0.3286 0.0394  -0.0129 -0.0174 104 GLU   B OE2 
5493 N  N   A ASP   B 105 ? 0.4506 0.4070 0.3582 0.0050  0.1785  0.0716  105 ASP   B N   
5494 N  N   B ASP   B 105 ? 0.4447 0.4086 0.3848 0.0085  0.0951  0.0430  105 ASP   B N   
5495 C  CA  A ASP   B 105 ? 0.4464 0.4013 0.3715 -0.0034 0.1986  0.0572  105 ASP   B CA  
5496 C  CA  B ASP   B 105 ? 0.4386 0.4032 0.3937 0.0042  0.1026  0.0310  105 ASP   B CA  
5497 C  C   A ASP   B 105 ? 0.4277 0.3748 0.3302 -0.0176 0.2093  0.0598  105 ASP   B C   
5498 C  C   B ASP   B 105 ? 0.4271 0.3895 0.3679 -0.0020 0.1078  0.0268  105 ASP   B C   
5499 O  O   A ASP   B 105 ? 0.4147 0.3691 0.3161 -0.0166 0.1995  0.0638  105 ASP   B O   
5500 O  O   B ASP   B 105 ? 0.4263 0.3876 0.3540 -0.0016 0.1125  0.0300  105 ASP   B O   
5501 C  CB  A ASP   B 105 ? 0.4624 0.4206 0.4469 0.0043  0.1948  0.0324  105 ASP   B CB  
5502 C  CB  B ASP   B 105 ? 0.4431 0.4110 0.4306 0.0074  0.1026  0.0208  105 ASP   B CB  
5503 C  CG  A ASP   B 105 ? 0.4746 0.4370 0.5182 0.0085  0.1950  0.0142  105 ASP   B CG  
5504 C  CG  B ASP   B 105 ? 0.4470 0.4174 0.4684 0.0085  0.1050  0.0139  105 ASP   B CG  
5505 O  OD1 A ASP   B 105 ? 0.4746 0.4398 0.5305 0.0053  0.2048  0.0164  105 ASP   B OD1 
5506 O  OD1 B ASP   B 105 ? 0.4471 0.4198 0.4770 0.0065  0.1075  0.0147  105 ASP   B OD1 
5507 O  OD2 A ASP   B 105 ? 0.4812 0.4458 0.5534 0.0139  0.1877  0.0005  105 ASP   B OD2 
5508 O  OD2 B ASP   B 105 ? 0.4480 0.4196 0.4818 0.0097  0.1064  0.0100  105 ASP   B OD2 
5517 N  N   A ILE   B 106 ? 0.4176 0.3529 0.3327 -0.0299 0.2046  0.0552  106 ILE   B N   
5518 N  N   B ILE   B 106 ? 0.4153 0.3761 0.3586 -0.0066 0.1034  0.0211  106 ILE   B N   
5519 C  CA  A ILE   B 106 ? 0.3991 0.3257 0.3520 -0.0479 0.1989  0.0468  106 ILE   B CA  
5520 C  CA  B ILE   B 106 ? 0.4004 0.3618 0.3599 -0.0121 0.1001  0.0137  106 ILE   B CA  
5521 C  C   A ILE   B 106 ? 0.3667 0.3150 0.3487 -0.0419 0.1912  0.0341  106 ILE   B C   
5522 C  C   B ILE   B 106 ? 0.3774 0.3518 0.3528 -0.0085 0.0982  0.0066  106 ILE   B C   
5523 O  O   A ILE   B 106 ? 0.3547 0.2948 0.3503 -0.0485 0.1935  0.0356  106 ILE   B O   
5524 O  O   B ILE   B 106 ? 0.3740 0.3443 0.3490 -0.0105 0.0970  0.0047  106 ILE   B O   
5525 C  CB  A ILE   B 106 ? 0.4148 0.3133 0.3808 -0.0657 0.1889  0.0467  106 ILE   B CB  
5526 C  CB  B ILE   B 106 ? 0.4079 0.3591 0.3699 -0.0200 0.0979  0.0124  106 ILE   B CB  
5527 C  CG1 A ILE   B 106 ? 0.4213 0.3122 0.3872 -0.0611 0.1792  0.0359  106 ILE   B CG1 
5528 C  CG1 B ILE   B 106 ? 0.4102 0.3577 0.3732 -0.0205 0.0943  0.0101  106 ILE   B CG1 
5529 C  CG2 A ILE   B 106 ? 0.4200 0.3101 0.3982 -0.0780 0.1891  0.0526  106 ILE   B CG2 
5530 C  CG2 B ILE   B 106 ? 0.4112 0.3603 0.3779 -0.0236 0.0984  0.0127  106 ILE   B CG2 
5531 C  CD1 A ILE   B 106 ? 0.4237 0.3129 0.3811 -0.0575 0.1773  0.0326  106 ILE   B CD1 
5532 C  CD1 B ILE   B 106 ? 0.4112 0.3570 0.3741 -0.0201 0.0922  0.0088  106 ILE   B CD1 
5555 N  N   A GLN   B 107 ? 0.3484 0.3265 0.3595 -0.0338 0.1744  0.0280  107 GLN   B N   
5556 N  N   B GLN   B 107 ? 0.3590 0.3508 0.3594 -0.0051 0.0958  0.0052  107 GLN   B N   
5557 C  CA  A GLN   B 107 ? 0.3300 0.3374 0.3753 -0.0249 0.1445  0.0233  107 GLN   B CA  
5558 C  CA  B GLN   B 107 ? 0.3412 0.3489 0.3687 -0.0018 0.0886  0.0083  107 GLN   B CA  
5559 C  C   A GLN   B 107 ? 0.2945 0.3142 0.3374 -0.0141 0.1221  0.0154  107 GLN   B C   
5560 C  C   B GLN   B 107 ? 0.3055 0.3227 0.3336 0.0014  0.0935  0.0098  107 GLN   B C   
5561 O  O   A GLN   B 107 ? 0.2843 0.3153 0.3626 -0.0104 0.0977  -0.0057 107 GLN   B O   
5562 O  O   B GLN   B 107 ? 0.3019 0.3251 0.3444 0.0037  0.0804  -0.0012 107 GLN   B O   
5563 C  CB  A GLN   B 107 ? 0.3596 0.3742 0.4486 -0.0205 0.1139  0.0228  107 GLN   B CB  
5564 C  CB  B GLN   B 107 ? 0.3622 0.3730 0.4243 -0.0000 0.0703  0.0089  107 GLN   B CB  
5565 C  CG  A GLN   B 107 ? 0.3889 0.4064 0.5161 -0.0150 0.0781  0.0227  107 GLN   B CG  
5566 C  CG  B GLN   B 107 ? 0.3815 0.3938 0.4753 0.0021  0.0500  0.0101  107 GLN   B CG  
5567 C  CD  A GLN   B 107 ? 0.4104 0.4307 0.5692 -0.0130 0.0531  0.0244  107 GLN   B CD  
5568 C  CD  B GLN   B 107 ? 0.3960 0.4093 0.5167 0.0026  0.0353  0.0115  107 GLN   B CD  
5569 O  OE1 A GLN   B 107 ? 0.4190 0.4402 0.5887 -0.0129 0.0481  0.0216  107 GLN   B OE1 
5570 O  OE1 B GLN   B 107 ? 0.4014 0.4149 0.5301 0.0023  0.0327  0.0108  107 GLN   B OE1 
5571 N  NE2 A GLN   B 107 ? 0.4180 0.4382 0.5865 -0.0099 0.0426  0.0284  107 GLN   B NE2 
5572 N  NE2 B GLN   B 107 ? 0.4013 0.4143 0.5315 0.0041  0.0292  0.0135  107 GLN   B NE2 
5589 N  N   . LEU   B 108 ? 0.2737 0.2949 0.3036 0.0096  0.1052  0.0191  108 LEU   B N   
5590 C  CA  . LEU   B 108 ? 0.2417 0.2613 0.2570 0.0263  0.0823  0.0329  108 LEU   B CA  
5591 C  C   . LEU   B 108 ? 0.2013 0.2142 0.2438 0.0240  0.0552  0.0351  108 LEU   B C   
5592 O  O   . LEU   B 108 ? 0.1920 0.1986 0.2276 0.0248  0.0435  0.0337  108 LEU   B O   
5593 C  CB  . LEU   B 108 ? 0.2536 0.2817 0.2459 0.0280  0.0843  0.0473  108 LEU   B CB  
5594 C  CG  . LEU   B 108 ? 0.2681 0.3102 0.2534 0.0310  0.0756  0.0240  108 LEU   B CG  
5595 C  CD1 . LEU   B 108 ? 0.2794 0.3207 0.2445 0.0240  0.0729  0.0223  108 LEU   B CD1 
5596 C  CD2 . LEU   B 108 ? 0.2782 0.3239 0.2611 0.0403  0.0585  0.0040  108 LEU   B CD2 
5609 N  N   . LEU   B 109 ? 0.1851 0.1862 0.2434 0.0152  0.0442  0.0251  109 LEU   B N   
5610 C  CA  . LEU   B 109 ? 0.1617 0.1574 0.2463 0.0056  0.0406  0.0345  109 LEU   B CA  
5611 C  C   . LEU   B 109 ? 0.1549 0.1384 0.2457 0.0024  0.0352  0.0252  109 LEU   B C   
5612 O  O   . LEU   B 109 ? 0.1514 0.1362 0.2459 0.0039  0.0333  0.0347  109 LEU   B O   
5613 C  CB  . LEU   B 109 ? 0.1700 0.1487 0.2511 0.0027  0.0324  0.0430  109 LEU   B CB  
5614 C  CG  . LEU   B 109 ? 0.1681 0.1452 0.2543 0.0014  0.0250  0.0287  109 LEU   B CG  
5615 C  CD1 . LEU   B 109 ? 0.1634 0.1568 0.2409 0.0083  0.0260  0.0303  109 LEU   B CD1 
5616 C  CD2 . LEU   B 109 ? 0.1810 0.1503 0.2699 0.0047  0.0228  0.0244  109 LEU   B CD2 
5628 N  N   . LYS   B 110 ? 0.1490 0.1407 0.2445 -0.0057 0.0264  0.0218  110 LYS   B N   
5629 C  CA  . LYS   B 110 ? 0.1492 0.1410 0.2441 -0.0025 0.0232  0.0222  110 LYS   B CA  
5630 C  C   . LYS   B 110 ? 0.1443 0.1392 0.2266 -0.0012 0.0286  0.0143  110 LYS   B C   
5631 O  O   . LYS   B 110 ? 0.1427 0.1403 0.2241 -0.0025 0.0256  0.0104  110 LYS   B O   
5632 C  CB  . LYS   B 110 ? 0.1465 0.1418 0.2662 -0.0030 0.0329  0.0184  110 LYS   B CB  
5633 C  CG  . LYS   B 110 ? 0.1476 0.1413 0.2830 -0.0072 0.0195  0.0199  110 LYS   B CG  
5634 C  CD  . LYS   B 110 ? 0.1550 0.1430 0.2917 -0.0106 0.0137  0.0159  110 LYS   B CD  
5635 C  CE  . LYS   B 110 ? 0.1493 0.1535 0.3101 -0.0046 0.0184  0.0083  110 LYS   B CE  
5636 N  NZ  . LYS   B 110 ? 0.1488 0.1673 0.3110 -0.0021 0.0077  0.0062  110 LYS   B NZ  
5650 N  N   . SER   B 111 ? 0.1464 0.1412 0.2443 -0.0040 0.0281  0.0167  111 SER   B N   
5651 C  CA  . SER   B 111 ? 0.1547 0.1465 0.2285 0.0041  0.0238  0.0216  111 SER   B CA  
5652 C  C   . SER   B 111 ? 0.1506 0.1392 0.2143 -0.0004 0.0204  0.0106  111 SER   B C   
5653 O  O   . SER   B 111 ? 0.1457 0.1400 0.2227 -0.0020 0.0102  0.0099  111 SER   B O   
5654 C  CB  . SER   B 111 ? 0.1681 0.1654 0.2375 0.0074  0.0400  0.0290  111 SER   B CB  
5655 O  OG  . SER   B 111 ? 0.1802 0.1928 0.2488 0.0111  0.0409  0.0342  111 SER   B OG  
5661 N  N   . ALA   B 112 ? 0.1432 0.1442 0.2211 0.0058  0.0268  0.0206  112 ALA   B N   
5662 C  CA  . ALA   B 112 ? 0.1430 0.1457 0.2037 0.0024  0.0148  0.0048  112 ALA   B CA  
5663 C  C   . ALA   B 112 ? 0.1342 0.1397 0.2001 0.0013  0.0108  0.0023  112 ALA   B C   
5664 O  O   . ALA   B 112 ? 0.1342 0.1411 0.2145 -0.0042 0.0091  0.0012  112 ALA   B O   
5665 C  CB  . ALA   B 112 ? 0.1435 0.1502 0.2068 0.0056  0.0106  0.0125  112 ALA   B CB  
5671 N  N   . TYR   B 113 ? 0.1322 0.1300 0.2149 -0.0009 0.0106  0.0097  113 TYR   B N   
5672 C  CA  . TYR   B 113 ? 0.1263 0.1293 0.2049 0.0000  0.0096  -0.0016 113 TYR   B CA  
5673 C  C   . TYR   B 113 ? 0.1286 0.1243 0.1963 -0.0067 0.0065  0.0042  113 TYR   B C   
5674 O  O   . TYR   B 113 ? 0.1349 0.1296 0.1882 -0.0070 0.0046  0.0008  113 TYR   B O   
5675 C  CB  . TYR   B 113 ? 0.1375 0.1208 0.2144 -0.0059 0.0165  -0.0005 113 TYR   B CB  
5676 C  CG  . TYR   B 113 ? 0.1381 0.1251 0.2195 -0.0079 0.0083  0.0108  113 TYR   B CG  
5677 C  CD1 . TYR   B 113 ? 0.1421 0.1269 0.2327 -0.0073 0.0137  0.0225  113 TYR   B CD1 
5678 C  CD2 . TYR   B 113 ? 0.1473 0.1257 0.2151 -0.0056 0.0049  0.0161  113 TYR   B CD2 
5679 C  CE1 . TYR   B 113 ? 0.1463 0.1292 0.2309 -0.0029 0.0248  0.0139  113 TYR   B CE1 
5680 C  CE2 . TYR   B 113 ? 0.1552 0.1218 0.2242 0.0003  0.0097  0.0178  113 TYR   B CE2 
5681 C  CZ  . TYR   B 113 ? 0.1432 0.1287 0.2348 0.0023  0.0109  0.0157  113 TYR   B CZ  
5682 O  OH  . TYR   B 113 ? 0.1494 0.1225 0.2649 0.0082  0.0226  0.0058  113 TYR   B OH  
5692 N  N   . GLU   B 114 ? 0.1271 0.1216 0.2093 -0.0040 0.0102  0.0080  114 GLU   B N   
5693 C  CA  . GLU   B 114 ? 0.1274 0.1211 0.2088 0.0017  0.0105  0.0020  114 GLU   B CA  
5694 C  C   . GLU   B 114 ? 0.1325 0.1229 0.1949 -0.0013 0.0093  0.0068  114 GLU   B C   
5695 O  O   . GLU   B 114 ? 0.1298 0.1237 0.2044 0.0005  0.0008  0.0046  114 GLU   B O   
5696 C  CB  . GLU   B 114 ? 0.1287 0.1296 0.2112 -0.0033 0.0158  0.0091  114 GLU   B CB  
5697 C  CG  . GLU   B 114 ? 0.1368 0.1269 0.2122 -0.0014 0.0109  0.0076  114 GLU   B CG  
5698 C  CD  . GLU   B 114 ? 0.1342 0.1288 0.2192 -0.0037 0.0114  0.0062  114 GLU   B CD  
5699 O  OE1 . GLU   B 114 ? 0.1328 0.1410 0.2257 -0.0067 0.0176  0.0053  114 GLU   B OE1 
5700 O  OE2 . GLU   B 114 ? 0.1357 0.1466 0.2496 -0.0168 0.0139  0.0107  114 GLU   B OE2 
5707 N  N   . ASN   B 115 ? 0.1323 0.1186 0.1934 -0.0049 0.0035  0.0056  115 ASN   B N   
5708 C  CA  . ASN   B 115 ? 0.1366 0.1258 0.1757 -0.0103 -0.0024 0.0110  115 ASN   B CA  
5709 C  C   . ASN   B 115 ? 0.1326 0.1222 0.1830 -0.0130 -0.0075 -0.0013 115 ASN   B C   
5710 O  O   . ASN   B 115 ? 0.1419 0.1244 0.1938 -0.0143 0.0003  0.0055  115 ASN   B O   
5711 C  CB  . ASN   B 115 ? 0.1427 0.1404 0.1810 -0.0128 -0.0046 0.0038  115 ASN   B CB  
5712 C  CG  . ASN   B 115 ? 0.1543 0.1425 0.1756 0.0012  -0.0009 0.0011  115 ASN   B CG  
5713 O  OD1 . ASN   B 115 ? 0.1937 0.1547 0.1988 -0.0046 0.0115  -0.0064 115 ASN   B OD1 
5714 N  ND2 . ASN   B 115 ? 0.1480 0.1490 0.1791 -0.0025 0.0077  0.0044  115 ASN   B ND2 
5721 N  N   . PHE   B 116 ? 0.1308 0.1275 0.1733 -0.0061 -0.0010 0.0047  116 PHE   B N   
5722 C  CA  . PHE   B 116 ? 0.1374 0.1263 0.1794 -0.0088 -0.0055 0.0013  116 PHE   B CA  
5723 C  C   . PHE   B 116 ? 0.1347 0.1181 0.1742 -0.0104 -0.0019 -0.0013 116 PHE   B C   
5724 O  O   . PHE   B 116 ? 0.1392 0.1284 0.1836 -0.0057 -0.0068 0.0107  116 PHE   B O   
5725 C  CB  . PHE   B 116 ? 0.1322 0.1230 0.1746 -0.0080 -0.0146 0.0081  116 PHE   B CB  
5726 C  CG  . PHE   B 116 ? 0.1261 0.1227 0.1750 -0.0133 -0.0071 0.0104  116 PHE   B CG  
5727 C  CD1 . PHE   B 116 ? 0.1364 0.1287 0.1939 -0.0063 -0.0064 0.0028  116 PHE   B CD1 
5728 C  CD2 . PHE   B 116 ? 0.1392 0.1268 0.1689 -0.0077 -0.0024 -0.0013 116 PHE   B CD2 
5729 C  CE1 . PHE   B 116 ? 0.1384 0.1336 0.1834 -0.0063 -0.0155 0.0072  116 PHE   B CE1 
5730 C  CE2 . PHE   B 116 ? 0.1371 0.1252 0.1788 -0.0023 -0.0065 0.0026  116 PHE   B CE2 
5731 C  CZ  . PHE   B 116 ? 0.1280 0.1367 0.1785 -0.0058 -0.0146 0.0050  116 PHE   B CZ  
5741 N  N   . ASN   B 117 ? 0.1300 0.1212 0.1922 -0.0069 -0.0047 0.0096  117 ASN   B N   
5742 C  CA  . ASN   B 117 ? 0.1403 0.1260 0.1906 -0.0049 -0.0129 -0.0011 117 ASN   B CA  
5743 C  C   . ASN   B 117 ? 0.1443 0.1270 0.1966 -0.0050 -0.0134 0.0067  117 ASN   B C   
5744 O  O   . ASN   B 117 ? 0.1534 0.1338 0.2277 -0.0071 -0.0331 0.0164  117 ASN   B O   
5745 C  CB  . ASN   B 117 ? 0.1388 0.1286 0.1955 -0.0006 -0.0083 -0.0005 117 ASN   B CB  
5746 C  CG  . ASN   B 117 ? 0.1375 0.1248 0.2145 -0.0019 -0.0061 -0.0046 117 ASN   B CG  
5747 O  OD1 . ASN   B 117 ? 0.1589 0.1280 0.2274 -0.0127 -0.0019 -0.0050 117 ASN   B OD1 
5748 N  ND2 . ASN   B 117 ? 0.1423 0.1314 0.2018 -0.0019 -0.0039 -0.0011 117 ASN   B ND2 
5755 N  N   . GLN   B 118 ? 0.1425 0.1190 0.1940 -0.0098 -0.0128 0.0020  118 GLN   B N   
5756 C  CA  . GLN   B 118 ? 0.1460 0.1262 0.2205 0.0008  -0.0166 -0.0037 118 GLN   B CA  
5757 C  C   . GLN   B 118 ? 0.1495 0.1228 0.2170 0.0015  -0.0096 -0.0053 118 GLN   B C   
5758 O  O   . GLN   B 118 ? 0.1724 0.1224 0.2458 -0.0081 0.0009  0.0018  118 GLN   B O   
5759 C  CB  . GLN   B 118 ? 0.1486 0.1282 0.2241 0.0010  -0.0179 0.0037  118 GLN   B CB  
5760 C  CG  . GLN   B 118 ? 0.1606 0.1320 0.2192 0.0045  -0.0118 -0.0038 118 GLN   B CG  
5761 C  CD  . GLN   B 118 ? 0.1637 0.1227 0.2183 -0.0002 -0.0140 -0.0135 118 GLN   B CD  
5762 O  OE1 . GLN   B 118 ? 0.1701 0.1245 0.2354 0.0030  -0.0039 -0.0006 118 GLN   B OE1 
5763 N  NE2 . GLN   B 118 ? 0.1732 0.1282 0.2214 -0.0022 -0.0122 0.0006  118 GLN   B NE2 
5772 N  N   . HIS   B 119 ? 0.1523 0.1277 0.1843 -0.0094 -0.0168 0.0101  119 HIS   B N   
5773 C  CA  . HIS   B 119 ? 0.1607 0.1395 0.1717 -0.0060 -0.0207 0.0060  119 HIS   B CA  
5774 C  C   . HIS   B 119 ? 0.1630 0.1385 0.1664 -0.0046 -0.0268 0.0095  119 HIS   B C   
5775 O  O   . HIS   B 119 ? 0.1699 0.1385 0.1908 -0.0279 -0.0240 0.0119  119 HIS   B O   
5776 C  CB  . HIS   B 119 ? 0.1634 0.1487 0.1715 -0.0028 -0.0207 0.0043  119 HIS   B CB  
5777 C  CG  . HIS   B 119 ? 0.1672 0.1721 0.1900 0.0087  -0.0410 -0.0066 119 HIS   B CG  
5778 N  ND1 . HIS   B 119 ? 0.1791 0.1879 0.2261 0.0027  -0.0475 -0.0256 119 HIS   B ND1 
5779 C  CD2 . HIS   B 119 ? 0.1822 0.1905 0.1973 0.0360  -0.0484 -0.0112 119 HIS   B CD2 
5780 C  CE1 . HIS   B 119 ? 0.1972 0.2050 0.2267 0.0157  -0.0531 -0.0349 119 HIS   B CE1 
5781 N  NE2 . HIS   B 119 ? 0.2005 0.2125 0.2168 0.0295  -0.0480 -0.0259 119 HIS   B NE2 
5789 N  N   . GLU   B 120 ? 0.1873 0.1429 0.1693 -0.0113 -0.0398 0.0182  120 GLU   B N   
5790 C  CA  . GLU   B 120 ? 0.2155 0.1598 0.1771 -0.0070 -0.0475 0.0334  120 GLU   B CA  
5791 C  C   . GLU   B 120 ? 0.1910 0.1483 0.1727 -0.0179 -0.0412 0.0303  120 GLU   B C   
5792 O  O   . GLU   B 120 ? 0.1825 0.1587 0.1807 -0.0179 -0.0412 0.0185  120 GLU   B O   
5793 C  CB  . GLU   B 120 ? 0.2833 0.1987 0.2507 0.0105  -0.0807 0.0541  120 GLU   B CB  
5794 C  CG  . GLU   B 120 ? 0.3465 0.2816 0.3558 0.0259  -0.1040 0.0755  120 GLU   B CG  
5795 C  CD  . GLU   B 120 ? 0.3967 0.3577 0.4652 0.0332  -0.1110 0.0892  120 GLU   B CD  
5796 O  OE1 . GLU   B 120 ? 0.4199 0.3828 0.5009 0.0282  -0.1087 0.1003  120 GLU   B OE1 
5797 O  OE2 . GLU   B 120 ? 0.4170 0.3915 0.5181 0.0361  -0.1090 0.0824  120 GLU   B OE2 
5804 N  N   . VAL   B 121 ? 0.1818 0.1469 0.1751 -0.0234 -0.0307 0.0281  121 VAL   B N   
5805 C  CA  . VAL   B 121 ? 0.1793 0.1568 0.1499 -0.0186 -0.0303 0.0187  121 VAL   B CA  
5806 C  C   . VAL   B 121 ? 0.1681 0.1495 0.1530 -0.0257 -0.0188 0.0135  121 VAL   B C   
5807 O  O   . VAL   B 121 ? 0.1752 0.1483 0.1734 -0.0348 -0.0291 0.0074  121 VAL   B O   
5808 C  CB  . VAL   B 121 ? 0.2054 0.1916 0.1549 -0.0098 -0.0231 0.0225  121 VAL   B CB  
5809 C  CG1 . VAL   B 121 ? 0.2109 0.2019 0.1786 -0.0211 -0.0191 0.0197  121 VAL   B CG1 
5810 C  CG2 . VAL   B 121 ? 0.2306 0.2196 0.1560 0.0030  -0.0224 0.0091  121 VAL   B CG2 
5820 N  N   . LEU   B 122 ? 0.1633 0.1425 0.1436 -0.0178 -0.0265 0.0099  122 LEU   B N   
5821 C  CA  . LEU   B 122 ? 0.1538 0.1522 0.1379 -0.0198 -0.0256 0.0134  122 LEU   B CA  
5822 C  C   . LEU   B 122 ? 0.1522 0.1403 0.1415 -0.0270 -0.0191 0.0066  122 LEU   B C   
5823 O  O   . LEU   B 122 ? 0.1601 0.1408 0.1772 -0.0370 -0.0283 0.0008  122 LEU   B O   
5824 C  CB  . LEU   B 122 ? 0.1730 0.1600 0.1669 -0.0080 -0.0305 0.0171  122 LEU   B CB  
5825 C  CG  . LEU   B 122 ? 0.1611 0.1658 0.1801 -0.0177 -0.0120 0.0168  122 LEU   B CG  
5826 C  CD1 . LEU   B 122 ? 0.1651 0.1850 0.1906 -0.0259 -0.0234 0.0102  122 LEU   B CD1 
5827 C  CD2 . LEU   B 122 ? 0.1659 0.1669 0.1534 -0.0128 -0.0133 0.0019  122 LEU   B CD2 
5839 N  N   . LEU   B 123 ? 0.1552 0.1299 0.1355 -0.0236 -0.0182 0.0108  123 LEU   B N   
5840 C  CA  . LEU   B 123 ? 0.1539 0.1292 0.1450 -0.0260 -0.0204 0.0051  123 LEU   B CA  
5841 C  C   . LEU   B 123 ? 0.1446 0.1263 0.1368 -0.0293 -0.0175 0.0012  123 LEU   B C   
5842 O  O   . LEU   B 123 ? 0.1537 0.1343 0.1410 -0.0346 -0.0179 0.0041  123 LEU   B O   
5843 C  CB  . LEU   B 123 ? 0.1573 0.1333 0.1607 -0.0274 -0.0132 -0.0043 123 LEU   B CB  
5844 C  CG  . LEU   B 123 ? 0.1557 0.1419 0.1668 -0.0190 -0.0100 0.0078  123 LEU   B CG  
5845 C  CD1 . LEU   B 123 ? 0.1684 0.1400 0.1797 -0.0191 -0.0097 -0.0068 123 LEU   B CD1 
5846 C  CD2 . LEU   B 123 ? 0.1611 0.1528 0.1803 -0.0186 -0.0007 0.0194  123 LEU   B CD2 
5858 N  N   . ALA   B 124 ? 0.1416 0.1301 0.1437 -0.0193 -0.0109 0.0007  124 ALA   B N   
5859 C  CA  . ALA   B 124 ? 0.1338 0.1297 0.1579 -0.0149 -0.0110 -0.0037 124 ALA   B CA  
5860 C  C   . ALA   B 124 ? 0.1346 0.1266 0.1534 -0.0187 -0.0119 -0.0020 124 ALA   B C   
5861 O  O   . ALA   B 124 ? 0.1489 0.1269 0.1618 -0.0153 -0.0152 -0.0015 124 ALA   B O   
5862 C  CB  . ALA   B 124 ? 0.1449 0.1384 0.1688 -0.0082 -0.0004 -0.0071 124 ALA   B CB  
5868 N  N   . PRO   B 125 ? 0.1451 0.1280 0.1493 -0.0133 -0.0157 0.0113  125 PRO   B N   
5869 C  CA  . PRO   B 125 ? 0.1541 0.1297 0.1689 -0.0167 -0.0153 0.0153  125 PRO   B CA  
5870 C  C   . PRO   B 125 ? 0.1435 0.1300 0.1804 -0.0156 -0.0093 0.0058  125 PRO   B C   
5871 O  O   . PRO   B 125 ? 0.1474 0.1255 0.1987 -0.0098 -0.0047 0.0148  125 PRO   B O   
5872 C  CB  . PRO   B 125 ? 0.1544 0.1535 0.1791 -0.0193 -0.0246 0.0312  125 PRO   B CB  
5873 C  CG  . PRO   B 125 ? 0.1571 0.1591 0.1617 -0.0305 -0.0260 0.0126  125 PRO   B CG  
5874 C  CD  . PRO   B 125 ? 0.1557 0.1395 0.1483 -0.0272 -0.0162 0.0049  125 PRO   B CD  
5882 N  N   . LEU   B 126 ? 0.1497 0.1210 0.2092 -0.0133 0.0063  0.0116  126 LEU   B N   
5883 C  CA  . LEU   B 126 ? 0.1580 0.1309 0.2097 -0.0114 0.0212  0.0187  126 LEU   B CA  
5884 C  C   . LEU   B 126 ? 0.1524 0.1387 0.2205 0.0002  0.0270  0.0257  126 LEU   B C   
5885 O  O   . LEU   B 126 ? 0.1761 0.1673 0.2334 0.0195  0.0003  -0.0012 126 LEU   B O   
5886 C  CB  . LEU   B 126 ? 0.1745 0.1337 0.2323 -0.0193 0.0268  0.0168  126 LEU   B CB  
5887 C  CG  . LEU   B 126 ? 0.1881 0.1462 0.2510 -0.0275 0.0192  -0.0109 126 LEU   B CG  
5888 C  CD1 . LEU   B 126 ? 0.2021 0.1576 0.2972 -0.0205 0.0163  -0.0169 126 LEU   B CD1 
5889 C  CD2 . LEU   B 126 ? 0.1892 0.1546 0.2539 -0.0313 0.0123  -0.0184 126 LEU   B CD2 
5901 N  N   . LEU   B 127 ? 0.1500 0.1290 0.2277 0.0035  0.0265  0.0147  127 LEU   B N   
5902 C  CA  . LEU   B 127 ? 0.1518 0.1410 0.2303 -0.0002 0.0315  0.0227  127 LEU   B CA  
5903 C  C   . LEU   B 127 ? 0.1455 0.1386 0.2310 0.0008  0.0206  0.0277  127 LEU   B C   
5904 O  O   . LEU   B 127 ? 0.1515 0.1395 0.2445 -0.0150 0.0131  0.0258  127 LEU   B O   
5905 C  CB  . LEU   B 127 ? 0.1645 0.1361 0.2426 -0.0002 0.0328  0.0258  127 LEU   B CB  
5906 C  CG  . LEU   B 127 ? 0.1728 0.1381 0.2518 0.0003  0.0304  0.0194  127 LEU   B CG  
5907 C  CD1 . LEU   B 127 ? 0.1777 0.1322 0.2624 0.0047  0.0191  0.0120  127 LEU   B CD1 
5908 C  CD2 . LEU   B 127 ? 0.1795 0.1487 0.2664 -0.0146 0.0264  0.0249  127 LEU   B CD2 
5920 N  N   . SER   B 128 ? 0.1499 0.1401 0.2288 0.0055  0.0036  0.0249  128 SER   B N   
5921 C  CA  . SER   B 128 ? 0.1660 0.1439 0.2256 0.0097  -0.0091 0.0301  128 SER   B CA  
5922 C  C   . SER   B 128 ? 0.1803 0.1513 0.2579 0.0069  -0.0281 0.0265  128 SER   B C   
5923 O  O   . SER   B 128 ? 0.1935 0.1522 0.2908 0.0036  -0.0210 0.0392  128 SER   B O   
5924 C  CB  . SER   B 128 ? 0.1772 0.1433 0.2314 0.0072  -0.0011 0.0405  128 SER   B CB  
5925 O  OG  . SER   B 128 ? 0.1812 0.1597 0.2292 0.0097  0.0138  0.0390  128 SER   B OG  
5931 N  N   . ALA   B 129 ? 0.1921 0.1520 0.2910 0.0248  -0.0157 0.0085  129 ALA   B N   
5932 C  CA  . ALA   B 129 ? 0.2052 0.1608 0.2997 0.0327  -0.0106 0.0044  129 ALA   B CA  
5933 C  C   . ALA   B 129 ? 0.1946 0.1523 0.2793 0.0241  0.0056  0.0102  129 ALA   B C   
5934 O  O   . ALA   B 129 ? 0.1873 0.1556 0.2705 0.0180  0.0018  0.0082  129 ALA   B O   
5935 C  CB  . ALA   B 129 ? 0.2251 0.1882 0.3407 0.0368  0.0009  0.0023  129 ALA   B CB  
5941 N  N   . GLY   B 130 ? 0.1929 0.1522 0.2757 0.0283  0.0077  0.0057  130 GLY   B N   
5942 C  CA  . GLY   B 130 ? 0.1930 0.1598 0.2840 0.0259  0.0178  0.0042  130 GLY   B CA  
5943 C  C   . GLY   B 130 ? 0.1939 0.1659 0.2789 0.0155  0.0171  0.0125  130 GLY   B C   
5944 O  O   . GLY   B 130 ? 0.2051 0.1771 0.2937 0.0150  0.0120  0.0222  130 GLY   B O   
5948 N  N   . ILE   B 131 ? 0.1908 0.1787 0.2839 0.0275  0.0191  0.0083  131 ILE   B N   
5949 C  CA  . ILE   B 131 ? 0.2150 0.1930 0.2888 0.0261  0.0049  0.0192  131 ILE   B CA  
5950 C  C   . ILE   B 131 ? 0.2292 0.1811 0.2466 0.0173  0.0056  0.0223  131 ILE   B C   
5951 O  O   . ILE   B 131 ? 0.2569 0.2001 0.2567 0.0175  -0.0102 0.0298  131 ILE   B O   
5952 C  CB  . ILE   B 131 ? 0.2152 0.2246 0.3233 0.0219  -0.0140 0.0319  131 ILE   B CB  
5953 C  CG1 . ILE   B 131 ? 0.2161 0.2460 0.3436 -0.0044 -0.0140 0.0338  131 ILE   B CG1 
5954 C  CG2 . ILE   B 131 ? 0.2149 0.2411 0.3447 0.0326  -0.0116 0.0217  131 ILE   B CG2 
5955 C  CD1 . ILE   B 131 ? 0.2227 0.2656 0.3638 -0.0198 -0.0213 0.0355  131 ILE   B CD1 
5967 N  N   . PHE   B 132 ? 0.2136 0.1647 0.2377 0.0113  0.0228  0.0273  132 PHE   B N   
5968 C  CA  . PHE   B 132 ? 0.2225 0.1681 0.2456 0.0067  0.0393  0.0189  132 PHE   B CA  
5969 C  C   . PHE   B 132 ? 0.2407 0.1843 0.2707 0.0135  0.0502  0.0180  132 PHE   B C   
5970 O  O   . PHE   B 132 ? 0.2571 0.2099 0.2887 0.0079  0.0649  0.0235  132 PHE   B O   
5971 C  CB  . PHE   B 132 ? 0.2027 0.1671 0.2231 0.0107  0.0397  0.0223  132 PHE   B CB  
5972 C  CG  . PHE   B 132 ? 0.1967 0.1703 0.2101 0.0109  0.0301  0.0252  132 PHE   B CG  
5973 C  CD1 . PHE   B 132 ? 0.2025 0.1741 0.2369 0.0097  0.0215  0.0216  132 PHE   B CD1 
5974 C  CD2 . PHE   B 132 ? 0.1983 0.1773 0.1812 0.0225  0.0249  0.0234  132 PHE   B CD2 
5975 C  CE1 . PHE   B 132 ? 0.2137 0.1826 0.2385 0.0013  0.0102  0.0144  132 PHE   B CE1 
5976 C  CE2 . PHE   B 132 ? 0.2103 0.1807 0.1872 0.0200  0.0104  0.0160  132 PHE   B CE2 
5977 C  CZ  . PHE   B 132 ? 0.2145 0.1831 0.2175 0.0040  -0.0016 0.0179  132 PHE   B CZ  
5987 N  N   . GLY   B 133 ? 0.2385 0.1783 0.2756 0.0035  0.0344  0.0423  133 GLY   B N   
5988 C  CA  . GLY   B 133 ? 0.2514 0.1895 0.2893 -0.0149 0.0385  0.0460  133 GLY   B CA  
5989 C  C   . GLY   B 133 ? 0.2593 0.1941 0.2885 -0.0299 0.0438  0.0531  133 GLY   B C   
5990 O  O   . GLY   B 133 ? 0.2799 0.2021 0.3208 -0.0407 0.0467  0.0612  133 GLY   B O   
5994 N  N   . ALA   B 134 ? 0.2389 0.1955 0.2764 -0.0262 0.0441  0.0396  134 ALA   B N   
5995 C  CA  . ALA   B 134 ? 0.2309 0.1952 0.2804 -0.0137 0.0535  0.0274  134 ALA   B CA  
5996 C  C   . ALA   B 134 ? 0.2369 0.1834 0.2872 -0.0086 0.0472  0.0362  134 ALA   B C   
5997 O  O   . ALA   B 134 ? 0.2384 0.2028 0.2995 -0.0004 0.0448  0.0288  134 ALA   B O   
5998 C  CB  . ALA   B 134 ? 0.2278 0.1981 0.2903 -0.0072 0.0414  0.0232  134 ALA   B CB  
6004 N  N   . ASP   B 135 ? 0.2479 0.1737 0.2895 -0.0106 0.0264  0.0455  135 ASP   B N   
6005 C  CA  . ASP   B 135 ? 0.2616 0.1657 0.3089 -0.0098 0.0069  0.0432  135 ASP   B CA  
6006 C  C   . ASP   B 135 ? 0.2437 0.1547 0.2910 0.0012  0.0053  0.0389  135 ASP   B C   
6007 O  O   . ASP   B 135 ? 0.2332 0.1494 0.2968 -0.0013 0.0079  0.0355  135 ASP   B O   
6008 C  CB  . ASP   B 135 ? 0.2956 0.1786 0.3433 -0.0359 0.0022  0.0422  135 ASP   B CB  
6009 C  CG  . ASP   B 135 ? 0.3228 0.1789 0.3874 -0.0611 -0.0026 0.0359  135 ASP   B CG  
6010 O  OD1 . ASP   B 135 ? 0.3302 0.1645 0.3838 -0.0423 -0.0096 0.0362  135 ASP   B OD1 
6011 O  OD2 . ASP   B 135 ? 0.3441 0.2136 0.4379 -0.0792 -0.0041 0.0151  135 ASP   B OD2 
6016 N  N   . PRO   B 136 ? 0.2331 0.1585 0.2937 0.0154  -0.0125 0.0335  136 PRO   B N   
6017 C  CA  . PRO   B 136 ? 0.2111 0.1485 0.2921 0.0166  -0.0127 0.0182  136 PRO   B CA  
6018 C  C   . PRO   B 136 ? 0.1890 0.1386 0.3076 0.0144  -0.0108 0.0156  136 PRO   B C   
6019 O  O   . PRO   B 136 ? 0.1695 0.1351 0.2967 0.0084  -0.0000 0.0143  136 PRO   B O   
6020 C  CB  . PRO   B 136 ? 0.2223 0.1705 0.3094 0.0266  -0.0201 0.0043  136 PRO   B CB  
6021 C  CG  . PRO   B 136 ? 0.2416 0.1775 0.3304 0.0293  -0.0117 0.0073  136 PRO   B CG  
6022 C  CD  . PRO   B 136 ? 0.2422 0.1709 0.3140 0.0371  -0.0082 0.0180  136 PRO   B CD  
6030 N  N   . ILE   B 137 ? 0.1998 0.1340 0.3204 0.0154  -0.0107 0.0082  137 ILE   B N   
6031 C  CA  . ILE   B 137 ? 0.2050 0.1291 0.3245 -0.0036 -0.0009 0.0073  137 ILE   B CA  
6032 C  C   . ILE   B 137 ? 0.1978 0.1311 0.3158 -0.0105 0.0157  0.0240  137 ILE   B C   
6033 O  O   . ILE   B 137 ? 0.1902 0.1344 0.3017 -0.0165 0.0086  0.0191  137 ILE   B O   
6034 C  CB  . ILE   B 137 ? 0.2288 0.1381 0.3693 -0.0032 -0.0021 0.0074  137 ILE   B CB  
6035 C  CG1 . ILE   B 137 ? 0.2545 0.1571 0.4153 0.0075  0.0076  0.0004  137 ILE   B CG1 
6036 C  CG2 . ILE   B 137 ? 0.2274 0.1402 0.3789 -0.0249 -0.0049 0.0089  137 ILE   B CG2 
6037 C  CD1 . ILE   B 137 ? 0.2744 0.1794 0.4536 0.0205  0.0099  0.0029  137 ILE   B CD1 
6049 N  N   . HIS   B 138 ? 0.2011 0.1351 0.3222 -0.0090 0.0280  0.0267  138 HIS   B N   
6050 C  CA  . HIS   B 138 ? 0.2124 0.1446 0.3183 -0.0088 0.0401  0.0307  138 HIS   B CA  
6051 C  C   . HIS   B 138 ? 0.1971 0.1425 0.3005 -0.0072 0.0323  0.0343  138 HIS   B C   
6052 O  O   . HIS   B 138 ? 0.1845 0.1505 0.3177 -0.0021 0.0391  0.0356  138 HIS   B O   
6053 C  CB  . HIS   B 138 ? 0.2413 0.1531 0.3309 -0.0074 0.0592  0.0305  138 HIS   B CB  
6054 C  CG  . HIS   B 138 ? 0.2692 0.1746 0.3338 -0.0117 0.0817  0.0439  138 HIS   B CG  
6055 N  ND1 . HIS   B 138 ? 0.2815 0.1908 0.3501 -0.0073 0.0996  0.0365  138 HIS   B ND1 
6056 C  CD2 . HIS   B 138 ? 0.2861 0.1858 0.3345 -0.0121 0.0895  0.0391  138 HIS   B CD2 
6057 C  CE1 . HIS   B 138 ? 0.2888 0.1934 0.3471 -0.0055 0.1077  0.0352  138 HIS   B CE1 
6058 N  NE2 . HIS   B 138 ? 0.2952 0.1831 0.3308 -0.0036 0.1025  0.0298  138 HIS   B NE2 
6066 N  N   . SER   B 139 ? 0.1920 0.1334 0.2953 -0.0033 0.0278  0.0218  139 SER   B N   
6067 C  CA  . SER   B 139 ? 0.1854 0.1272 0.2728 -0.0073 0.0251  0.0082  139 SER   B CA  
6068 C  C   . SER   B 139 ? 0.1638 0.1235 0.2654 -0.0071 0.0153  0.0081  139 SER   B C   
6069 O  O   . SER   B 139 ? 0.1562 0.1278 0.2622 0.0026  0.0056  0.0153  139 SER   B O   
6070 C  CB  . SER   B 139 ? 0.1882 0.1281 0.2790 -0.0023 0.0082  0.0088  139 SER   B CB  
6071 O  OG  . SER   B 139 ? 0.1894 0.1306 0.2758 -0.0023 -0.0010 0.0149  139 SER   B OG  
6077 N  N   . LEU   B 140 ? 0.1627 0.1169 0.2536 -0.0122 0.0157  0.0053  140 LEU   B N   
6078 C  CA  . LEU   B 140 ? 0.1572 0.1219 0.2613 -0.0024 0.0144  0.0051  140 LEU   B CA  
6079 C  C   . LEU   B 140 ? 0.1531 0.1235 0.2733 -0.0050 0.0028  -0.0018 140 LEU   B C   
6080 O  O   . LEU   B 140 ? 0.1507 0.1301 0.2631 -0.0049 -0.0025 0.0024  140 LEU   B O   
6081 C  CB  . LEU   B 140 ? 0.1560 0.1203 0.2729 -0.0106 0.0151  0.0036  140 LEU   B CB  
6082 C  CG  . LEU   B 140 ? 0.1669 0.1262 0.2706 -0.0126 0.0076  0.0058  140 LEU   B CG  
6083 C  CD1 . LEU   B 140 ? 0.1762 0.1329 0.2842 -0.0101 0.0192  -0.0002 140 LEU   B CD1 
6084 C  CD2 . LEU   B 140 ? 0.1858 0.1403 0.2848 -0.0112 0.0005  -0.0072 140 LEU   B CD2 
6096 N  N   . ARG   B 141 ? 0.1477 0.1235 0.2949 -0.0130 0.0078  -0.0032 141 ARG   B N   
6097 C  CA  . ARG   B 141 ? 0.1476 0.1269 0.3226 -0.0148 0.0245  -0.0017 141 ARG   B CA  
6098 C  C   . ARG   B 141 ? 0.1448 0.1277 0.3074 -0.0157 0.0114  -0.0003 141 ARG   B C   
6099 O  O   . ARG   B 141 ? 0.1514 0.1281 0.3039 -0.0131 0.0026  -0.0126 141 ARG   B O   
6100 C  CB  . ARG   B 141 ? 0.1656 0.1397 0.3446 -0.0197 0.0268  -0.0082 141 ARG   B CB  
6101 C  CG  . ARG   B 141 ? 0.1916 0.1652 0.3455 -0.0202 0.0294  -0.0124 141 ARG   B CG  
6102 C  CD  . ARG   B 141 ? 0.2343 0.1854 0.3375 -0.0170 0.0140  -0.0241 141 ARG   B CD  
6103 N  NE  . ARG   B 141 ? 0.2626 0.1818 0.3309 -0.0301 0.0174  -0.0269 141 ARG   B NE  
6104 C  CZ  . ARG   B 141 ? 0.2841 0.1675 0.3056 -0.0302 0.0294  -0.0332 141 ARG   B CZ  
6105 N  NH1 . ARG   B 141 ? 0.2947 0.1600 0.2950 -0.0319 0.0275  -0.0316 141 ARG   B NH1 
6106 N  NH2 . ARG   B 141 ? 0.3014 0.1776 0.3147 -0.0160 0.0178  -0.0265 141 ARG   B NH2 
6120 N  N   . VAL   B 142 ? 0.1458 0.1234 0.2977 -0.0100 0.0127  0.0021  142 VAL   B N   
6121 C  CA  . VAL   B 142 ? 0.1397 0.1275 0.2952 -0.0057 0.0160  -0.0012 142 VAL   B CA  
6122 C  C   . VAL   B 142 ? 0.1378 0.1259 0.2895 -0.0041 0.0082  -0.0009 142 VAL   B C   
6123 O  O   . VAL   B 142 ? 0.1483 0.1235 0.2953 -0.0015 0.0119  -0.0007 142 VAL   B O   
6124 C  CB  . VAL   B 142 ? 0.1544 0.1397 0.3032 -0.0021 0.0218  0.0132  142 VAL   B CB  
6125 C  CG1 . VAL   B 142 ? 0.1516 0.1380 0.2996 0.0065  0.0287  0.0052  142 VAL   B CG1 
6126 C  CG2 . VAL   B 142 ? 0.1762 0.1421 0.3105 0.0019  0.0183  0.0199  142 VAL   B CG2 
6136 N  N   . CYS   B 143 ? 0.1377 0.1307 0.2637 -0.0021 0.0052  0.0131  143 CYS   B N   
6137 C  CA  . CYS   B 143 ? 0.1360 0.1272 0.2615 -0.0047 0.0041  -0.0030 143 CYS   B CA  
6138 C  C   . CYS   B 143 ? 0.1331 0.1293 0.2607 -0.0086 0.0024  -0.0051 143 CYS   B C   
6139 O  O   . CYS   B 143 ? 0.1411 0.1332 0.2597 -0.0051 -0.0037 -0.0056 143 CYS   B O   
6140 C  CB  . CYS   B 143 ? 0.1427 0.1369 0.2599 -0.0085 -0.0009 -0.0017 143 CYS   B CB  
6141 S  SG  . CYS   B 143 ? 0.1461 0.1491 0.2545 -0.0078 0.0022  0.0046  143 CYS   B SG  
6147 N  N   . VAL   B 144 ? 0.1386 0.1306 0.2875 -0.0127 -0.0025 -0.0182 144 VAL   B N   
6148 C  CA  . VAL   B 144 ? 0.1487 0.1375 0.3115 -0.0168 -0.0087 -0.0196 144 VAL   B CA  
6149 C  C   . VAL   B 144 ? 0.1434 0.1416 0.3152 -0.0134 -0.0105 -0.0048 144 VAL   B C   
6150 O  O   . VAL   B 144 ? 0.1529 0.1597 0.3298 -0.0046 -0.0176 0.0201  144 VAL   B O   
6151 C  CB  . VAL   B 144 ? 0.1713 0.1513 0.3558 -0.0194 -0.0161 -0.0330 144 VAL   B CB  
6152 C  CG1 . VAL   B 144 ? 0.1946 0.1878 0.3825 -0.0073 -0.0146 -0.0203 144 VAL   B CG1 
6153 C  CG2 . VAL   B 144 ? 0.1850 0.1543 0.3456 -0.0097 -0.0259 -0.0400 144 VAL   B CG2 
6163 N  N   . ASP   B 145 ? 0.1455 0.1316 0.3222 -0.0104 -0.0039 -0.0191 145 ASP   B N   
6164 C  CA  . ASP   B 145 ? 0.1443 0.1355 0.3522 -0.0090 0.0127  -0.0151 145 ASP   B CA  
6165 C  C   . ASP   B 145 ? 0.1426 0.1374 0.3363 -0.0075 0.0076  -0.0112 145 ASP   B C   
6166 O  O   . ASP   B 145 ? 0.1417 0.1549 0.3881 -0.0152 0.0137  -0.0235 145 ASP   B O   
6167 C  CB  . ASP   B 145 ? 0.1544 0.1509 0.4020 -0.0133 0.0299  -0.0132 145 ASP   B CB  
6168 C  CG  . ASP   B 145 ? 0.1715 0.1478 0.4539 -0.0231 0.0349  -0.0145 145 ASP   B CG  
6169 O  OD1 . ASP   B 145 ? 0.1754 0.1471 0.4542 -0.0260 0.0018  -0.0250 145 ASP   B OD1 
6170 O  OD2 . ASP   B 145 ? 0.1975 0.1529 0.4919 -0.0299 0.0587  -0.0029 145 ASP   B OD2 
6175 N  N   . THR   B 146 ? 0.1345 0.1275 0.2795 -0.0099 -0.0036 -0.0008 146 THR   B N   
6176 C  CA  . THR   B 146 ? 0.1395 0.1275 0.2583 -0.0139 0.0094  -0.0038 146 THR   B CA  
6177 C  C   . THR   B 146 ? 0.1427 0.1298 0.2591 -0.0086 0.0060  0.0025  146 THR   B C   
6178 O  O   . THR   B 146 ? 0.1459 0.1269 0.2567 -0.0075 0.0017  0.0026  146 THR   B O   
6179 C  CB  . THR   B 146 ? 0.1449 0.1268 0.2668 -0.0064 0.0172  0.0039  146 THR   B CB  
6180 O  OG1 . THR   B 146 ? 0.1497 0.1283 0.2648 -0.0061 0.0235  0.0107  146 THR   B OG1 
6181 C  CG2 . THR   B 146 ? 0.1557 0.1361 0.2586 -0.0055 0.0161  -0.0004 146 THR   B CG2 
6189 N  N   . VAL   B 147 ? 0.1444 0.1330 0.2458 -0.0083 0.0099  0.0055  147 VAL   B N   
6190 C  CA  . VAL   B 147 ? 0.1421 0.1291 0.2360 -0.0104 -0.0096 0.0016  147 VAL   B CA  
6191 C  C   . VAL   B 147 ? 0.1429 0.1297 0.2391 -0.0191 -0.0125 -0.0010 147 VAL   B C   
6192 O  O   . VAL   B 147 ? 0.1540 0.1403 0.2454 -0.0197 -0.0325 -0.0075 147 VAL   B O   
6193 C  CB  . VAL   B 147 ? 0.1476 0.1428 0.2232 -0.0114 -0.0122 0.0016  147 VAL   B CB  
6194 C  CG1 . VAL   B 147 ? 0.1477 0.1511 0.2128 -0.0156 -0.0047 -0.0008 147 VAL   B CG1 
6195 C  CG2 . VAL   B 147 ? 0.1497 0.1409 0.2357 -0.0166 0.0007  0.0019  147 VAL   B CG2 
6205 N  N   . ARG   B 148 ? 0.1472 0.1322 0.2290 -0.0116 -0.0219 -0.0099 148 ARG   B N   
6206 C  CA  . ARG   B 148 ? 0.1498 0.1422 0.2257 -0.0079 -0.0303 -0.0066 148 ARG   B CA  
6207 C  C   . ARG   B 148 ? 0.1535 0.1517 0.2184 -0.0108 -0.0345 -0.0058 148 ARG   B C   
6208 O  O   . ARG   B 148 ? 0.1705 0.1834 0.2307 -0.0285 -0.0444 0.0027  148 ARG   B O   
6209 C  CB  . ARG   B 148 ? 0.1570 0.1492 0.2228 -0.0057 -0.0349 -0.0133 148 ARG   B CB  
6210 C  CG  . ARG   B 148 ? 0.1532 0.1610 0.2422 -0.0101 -0.0303 -0.0304 148 ARG   B CG  
6211 C  CD  . ARG   B 148 ? 0.1575 0.1789 0.2565 0.0035  -0.0327 -0.0300 148 ARG   B CD  
6212 N  NE  . ARG   B 148 ? 0.1619 0.1805 0.2490 0.0184  -0.0322 -0.0298 148 ARG   B NE  
6213 C  CZ  . ARG   B 148 ? 0.1597 0.1740 0.2285 0.0127  -0.0244 -0.0215 148 ARG   B CZ  
6214 N  NH1 . ARG   B 148 ? 0.1520 0.1796 0.2396 -0.0040 -0.0001 -0.0176 148 ARG   B NH1 
6215 N  NH2 . ARG   B 148 ? 0.1774 0.1559 0.2232 0.0154  -0.0156 -0.0161 148 ARG   B NH2 
6229 N  N   . THR   B 149 ? 0.1558 0.1399 0.2086 -0.0119 -0.0321 -0.0015 149 THR   B N   
6230 C  CA  . THR   B 149 ? 0.1642 0.1460 0.2013 -0.0164 -0.0298 0.0059  149 THR   B CA  
6231 C  C   . THR   B 149 ? 0.1645 0.1455 0.1873 -0.0167 -0.0392 -0.0006 149 THR   B C   
6232 O  O   . THR   B 149 ? 0.1701 0.1405 0.2103 -0.0250 -0.0201 0.0035  149 THR   B O   
6233 C  CB  . THR   B 149 ? 0.1639 0.1412 0.2018 -0.0180 -0.0263 0.0020  149 THR   B CB  
6234 O  OG1 . THR   B 149 ? 0.1639 0.1494 0.1967 -0.0246 -0.0301 0.0075  149 THR   B OG1 
6235 C  CG2 . THR   B 149 ? 0.1711 0.1453 0.2274 -0.0146 -0.0220 0.0038  149 THR   B CG2 
6243 N  N   . ASN   B 150 ? 0.1688 0.1466 0.1834 -0.0199 -0.0412 0.0004  150 ASN   B N   
6244 C  CA  . ASN   B 150 ? 0.1785 0.1640 0.1735 -0.0266 -0.0365 -0.0002 150 ASN   B CA  
6245 C  C   . ASN   B 150 ? 0.1678 0.1574 0.1789 -0.0213 -0.0244 -0.0038 150 ASN   B C   
6246 O  O   . ASN   B 150 ? 0.1730 0.1527 0.1966 -0.0305 -0.0429 0.0020  150 ASN   B O   
6247 C  CB  . ASN   B 150 ? 0.2044 0.1957 0.1774 -0.0331 -0.0486 0.0135  150 ASN   B CB  
6248 C  CG  . ASN   B 150 ? 0.2280 0.2390 0.2217 -0.0253 -0.0557 0.0261  150 ASN   B CG  
6249 O  OD1 . ASN   B 150 ? 0.2343 0.2525 0.2339 -0.0337 -0.0658 0.0126  150 ASN   B OD1 
6250 N  ND2 . ASN   B 150 ? 0.2406 0.2602 0.2619 -0.0137 -0.0609 0.0682  150 ASN   B ND2 
6257 N  N   . VAL   B 151 ? 0.1616 0.1564 0.1790 -0.0240 -0.0295 -0.0029 151 VAL   B N   
6258 C  CA  . VAL   B 151 ? 0.1609 0.1529 0.1769 -0.0268 -0.0262 -0.0023 151 VAL   B CA  
6259 C  C   . VAL   B 151 ? 0.1644 0.1439 0.1796 -0.0333 -0.0257 -0.0039 151 VAL   B C   
6260 O  O   . VAL   B 151 ? 0.1722 0.1519 0.2077 -0.0290 -0.0252 -0.0120 151 VAL   B O   
6261 C  CB  . VAL   B 151 ? 0.1803 0.1676 0.1924 -0.0104 -0.0252 -0.0039 151 VAL   B CB  
6262 C  CG1 . VAL   B 151 ? 0.1839 0.1731 0.2199 -0.0173 -0.0197 -0.0083 151 VAL   B CG1 
6263 C  CG2 . VAL   B 151 ? 0.1916 0.1819 0.1813 0.0026  -0.0199 0.0124  151 VAL   B CG2 
6273 N  N   . TYR   B 152 ? 0.1611 0.1349 0.1776 -0.0278 -0.0264 -0.0075 152 TYR   B N   
6274 C  CA  . TYR   B 152 ? 0.1691 0.1512 0.1598 -0.0339 -0.0193 -0.0102 152 TYR   B CA  
6275 C  C   . TYR   B 152 ? 0.1627 0.1369 0.1485 -0.0268 -0.0168 -0.0080 152 TYR   B C   
6276 O  O   . TYR   B 152 ? 0.1664 0.1409 0.1634 -0.0291 -0.0178 -0.0022 152 TYR   B O   
6277 C  CB  . TYR   B 152 ? 0.1806 0.1699 0.1612 -0.0382 -0.0129 -0.0016 152 TYR   B CB  
6278 C  CG  . TYR   B 152 ? 0.1934 0.1800 0.1604 -0.0451 -0.0191 0.0050  152 TYR   B CG  
6279 C  CD1 . TYR   B 152 ? 0.2046 0.1923 0.1573 -0.0425 -0.0247 0.0151  152 TYR   B CD1 
6280 C  CD2 . TYR   B 152 ? 0.2138 0.1991 0.1653 -0.0444 -0.0155 -0.0008 152 TYR   B CD2 
6281 C  CE1 . TYR   B 152 ? 0.2224 0.2133 0.1738 -0.0396 -0.0352 0.0273  152 TYR   B CE1 
6282 C  CE2 . TYR   B 152 ? 0.2243 0.2211 0.1723 -0.0457 -0.0263 -0.0128 152 TYR   B CE2 
6283 C  CZ  . TYR   B 152 ? 0.2318 0.2362 0.1671 -0.0435 -0.0477 0.0203  152 TYR   B CZ  
6284 O  OH  . TYR   B 152 ? 0.2573 0.2740 0.2065 -0.0332 -0.0546 0.0246  152 TYR   B OH  
6294 N  N   . LEU   B 153 ? 0.1596 0.1357 0.1676 -0.0270 -0.0170 -0.0024 153 LEU   B N   
6295 C  CA  . LEU   B 153 ? 0.1629 0.1317 0.1582 -0.0207 -0.0072 -0.0079 153 LEU   B CA  
6296 C  C   . LEU   B 153 ? 0.1693 0.1301 0.1690 -0.0272 -0.0078 -0.0167 153 LEU   B C   
6297 O  O   . LEU   B 153 ? 0.1770 0.1502 0.1851 -0.0190 -0.0070 -0.0305 153 LEU   B O   
6298 C  CB  . LEU   B 153 ? 0.1632 0.1243 0.1832 -0.0295 -0.0095 -0.0026 153 LEU   B CB  
6299 C  CG  . LEU   B 153 ? 0.1607 0.1400 0.2092 -0.0278 -0.0117 0.0001  153 LEU   B CG  
6300 C  CD1 . LEU   B 153 ? 0.1672 0.1538 0.2121 -0.0325 -0.0030 0.0119  153 LEU   B CD1 
6301 C  CD2 . LEU   B 153 ? 0.1577 0.1572 0.2096 -0.0316 0.0033  0.0096  153 LEU   B CD2 
6313 N  N   . ALA   B 154 ? 0.1561 0.1335 0.1821 -0.0124 -0.0161 -0.0063 154 ALA   B N   
6314 C  CA  . ALA   B 154 ? 0.1661 0.1440 0.2055 -0.0058 -0.0158 -0.0199 154 ALA   B CA  
6315 C  C   . ALA   B 154 ? 0.1794 0.1489 0.2164 0.0002  -0.0223 -0.0281 154 ALA   B C   
6316 O  O   . ALA   B 154 ? 0.2098 0.1494 0.2221 0.0054  -0.0074 -0.0114 154 ALA   B O   
6317 C  CB  . ALA   B 154 ? 0.1657 0.1593 0.2254 -0.0051 -0.0037 -0.0268 154 ALA   B CB  
6323 N  N   . VAL   B 155 ? 0.1502 0.1405 0.2335 -0.0074 0.0013  -0.0254 155 VAL   B N   
6324 C  CA  . VAL   B 155 ? 0.1469 0.1396 0.2501 -0.0039 -0.0128 -0.0122 155 VAL   B CA  
6325 C  C   . VAL   B 155 ? 0.1451 0.1369 0.2470 -0.0053 -0.0073 -0.0306 155 VAL   B C   
6326 O  O   . VAL   B 155 ? 0.1651 0.1571 0.2874 0.0077  -0.0102 -0.0496 155 VAL   B O   
6327 C  CB  . VAL   B 155 ? 0.1512 0.1524 0.2816 -0.0073 -0.0227 -0.0002 155 VAL   B CB  
6328 C  CG1 . VAL   B 155 ? 0.1605 0.1464 0.2856 -0.0113 -0.0116 -0.0048 155 VAL   B CG1 
6329 C  CG2 . VAL   B 155 ? 0.1471 0.1592 0.3041 -0.0040 -0.0202 0.0341  155 VAL   B CG2 
6339 N  N   . PHE   B 156 ? 0.1342 0.1454 0.2655 0.0017  -0.0053 -0.0237 156 PHE   B N   
6340 C  CA  . PHE   B 156 ? 0.1451 0.1510 0.3009 0.0038  -0.0050 -0.0228 156 PHE   B CA  
6341 C  C   . PHE   B 156 ? 0.1447 0.1597 0.3343 0.0100  -0.0090 -0.0449 156 PHE   B C   
6342 O  O   . PHE   B 156 ? 0.1694 0.1850 0.3648 0.0225  -0.0004 -0.0554 156 PHE   B O   
6343 C  CB  . PHE   B 156 ? 0.1530 0.1525 0.2865 0.0012  -0.0090 -0.0132 156 PHE   B CB  
6344 C  CG  . PHE   B 156 ? 0.1512 0.1726 0.2932 0.0023  -0.0101 0.0087  156 PHE   B CG  
6345 C  CD1 . PHE   B 156 ? 0.1544 0.1918 0.3226 0.0093  -0.0052 0.0366  156 PHE   B CD1 
6346 C  CD2 . PHE   B 156 ? 0.1574 0.1832 0.2969 0.0090  -0.0161 0.0165  156 PHE   B CD2 
6347 C  CE1 . PHE   B 156 ? 0.1565 0.2067 0.3446 0.0043  -0.0057 0.0361  156 PHE   B CE1 
6348 C  CE2 . PHE   B 156 ? 0.1646 0.2028 0.3248 0.0131  -0.0224 0.0156  156 PHE   B CE2 
6349 C  CZ  . PHE   B 156 ? 0.1536 0.2084 0.3458 0.0172  -0.0235 0.0215  156 PHE   B CZ  
6359 N  N   . ASP   B 157 ? 0.1453 0.1573 0.3589 0.0111  -0.0268 -0.0236 157 ASP   B N   
6360 C  CA  . ASP   B 157 ? 0.1590 0.1635 0.3952 0.0124  -0.0220 -0.0299 157 ASP   B CA  
6361 C  C   . ASP   B 157 ? 0.1600 0.1619 0.4035 0.0077  -0.0173 -0.0555 157 ASP   B C   
6362 O  O   . ASP   B 157 ? 0.1452 0.1589 0.3943 0.0075  -0.0174 -0.0470 157 ASP   B O   
6363 C  CB  . ASP   B 157 ? 0.1893 0.1779 0.4042 0.0010  -0.0440 -0.0123 157 ASP   B CB  
6364 C  CG  . ASP   B 157 ? 0.2318 0.1892 0.4314 0.0001  -0.0345 -0.0224 157 ASP   B CG  
6365 O  OD1 . ASP   B 157 ? 0.2389 0.1887 0.4480 0.0069  -0.0273 -0.0209 157 ASP   B OD1 
6366 O  OD2 . ASP   B 157 ? 0.2611 0.2120 0.4546 0.0007  -0.0238 -0.0242 157 ASP   B OD2 
6371 N  N   . LYS   B 158 ? 0.1618 0.1882 0.4118 0.0112  -0.0028 -0.0880 158 LYS   B N   
6372 C  CA  . LYS   B 158 ? 0.1800 0.2100 0.4182 0.0062  0.0033  -0.1091 158 LYS   B CA  
6373 C  C   . LYS   B 158 ? 0.1825 0.1925 0.4340 0.0037  -0.0059 -0.0950 158 LYS   B C   
6374 O  O   . LYS   B 158 ? 0.1817 0.1949 0.4384 -0.0051 0.0001  -0.0972 158 LYS   B O   
6375 C  CB  . LYS   B 158 ? 0.2082 0.2577 0.4150 0.0036  0.0116  -0.1336 158 LYS   B CB  
6376 C  CG  . LYS   B 158 ? 0.2450 0.3126 0.4285 -0.0004 0.0152  -0.1382 158 LYS   B CG  
6377 C  CD  . LYS   B 158 ? 0.2693 0.3649 0.4390 -0.0021 0.0242  -0.1333 158 LYS   B CD  
6378 C  CE  . LYS   B 158 ? 0.2872 0.4064 0.4500 -0.0014 0.0238  -0.1290 158 LYS   B CE  
6379 N  NZ  . LYS   B 158 ? 0.2910 0.4285 0.4504 -0.0052 0.0211  -0.1290 158 LYS   B NZ  
6393 N  N   . ASN   B 159 ? 0.1824 0.1777 0.4553 0.0059  -0.0243 -0.0747 159 ASN   B N   
6394 C  CA  . ASN   B 159 ? 0.1947 0.1705 0.4685 0.0154  -0.0380 -0.0622 159 ASN   B CA  
6395 C  C   . ASN   B 159 ? 0.1797 0.1560 0.4606 0.0120  -0.0492 -0.0502 159 ASN   B C   
6396 O  O   . ASN   B 159 ? 0.1842 0.1474 0.4780 -0.0018 -0.0570 -0.0365 159 ASN   B O   
6397 C  CB  . ASN   B 159 ? 0.2180 0.1875 0.4857 0.0203  -0.0413 -0.0549 159 ASN   B CB  
6398 C  CG  . ASN   B 159 ? 0.2468 0.2112 0.5068 0.0230  -0.0489 -0.0610 159 ASN   B CG  
6399 O  OD1 . ASN   B 159 ? 0.2602 0.2209 0.5005 0.0290  -0.0454 -0.0684 159 ASN   B OD1 
6400 N  ND2 . ASN   B 159 ? 0.2491 0.2169 0.5173 0.0275  -0.0550 -0.0555 159 ASN   B ND2 
6407 N  N   . LEU   B 160 ? 0.1655 0.1527 0.4362 0.0074  -0.0498 -0.0454 160 LEU   B N   
6408 C  CA  . LEU   B 160 ? 0.1599 0.1561 0.3931 0.0099  -0.0434 -0.0285 160 LEU   B CA  
6409 C  C   . LEU   B 160 ? 0.1593 0.1481 0.3814 0.0020  -0.0272 -0.0320 160 LEU   B C   
6410 O  O   . LEU   B 160 ? 0.1529 0.1503 0.3758 -0.0028 -0.0336 -0.0176 160 LEU   B O   
6411 C  CB  . LEU   B 160 ? 0.1620 0.1661 0.3696 0.0040  -0.0389 -0.0228 160 LEU   B CB  
6412 C  CG  . LEU   B 160 ? 0.1652 0.1763 0.3409 0.0077  -0.0415 -0.0073 160 LEU   B CG  
6413 C  CD1 . LEU   B 160 ? 0.1834 0.1930 0.3382 -0.0038 -0.0346 -0.0045 160 LEU   B CD1 
6414 C  CD2 . LEU   B 160 ? 0.1677 0.1841 0.3264 0.0161  -0.0325 -0.0123 160 LEU   B CD2 
6426 N  N   . TYR   B 161 ? 0.1535 0.1546 0.3800 -0.0056 0.0006  -0.0461 161 TYR   B N   
6427 C  CA  . TYR   B 161 ? 0.1683 0.1545 0.3632 -0.0151 0.0154  -0.0538 161 TYR   B CA  
6428 C  C   . TYR   B 161 ? 0.1750 0.1530 0.3552 -0.0142 0.0139  -0.0435 161 TYR   B C   
6429 O  O   . TYR   B 161 ? 0.1780 0.1557 0.3391 -0.0204 0.0074  -0.0375 161 TYR   B O   
6430 C  CB  . TYR   B 161 ? 0.1849 0.1642 0.3589 -0.0276 0.0305  -0.0695 161 TYR   B CB  
6431 C  CG  . TYR   B 161 ? 0.2115 0.1718 0.3484 -0.0350 0.0444  -0.0744 161 TYR   B CG  
6432 C  CD1 . TYR   B 161 ? 0.2215 0.1717 0.3437 -0.0505 0.0492  -0.0743 161 TYR   B CD1 
6433 C  CD2 . TYR   B 161 ? 0.2340 0.1856 0.3324 -0.0325 0.0441  -0.0778 161 TYR   B CD2 
6434 C  CE1 . TYR   B 161 ? 0.2421 0.1937 0.3402 -0.0524 0.0521  -0.0695 161 TYR   B CE1 
6435 C  CE2 . TYR   B 161 ? 0.2551 0.2045 0.3390 -0.0374 0.0521  -0.0742 161 TYR   B CE2 
6436 C  CZ  . TYR   B 161 ? 0.2607 0.2060 0.3411 -0.0537 0.0466  -0.0674 161 TYR   B CZ  
6437 O  OH  . TYR   B 161 ? 0.2904 0.2260 0.3644 -0.0557 0.0474  -0.0653 161 TYR   B OH  
6447 N  N   . ASP   B 162 ? 0.1772 0.1512 0.3753 -0.0125 0.0004  -0.0599 162 ASP   B N   
6448 C  CA  . ASP   B 162 ? 0.1850 0.1572 0.3856 -0.0082 -0.0003 -0.0585 162 ASP   B CA  
6449 C  C   . ASP   B 162 ? 0.1801 0.1489 0.3814 -0.0119 -0.0100 -0.0388 162 ASP   B C   
6450 O  O   . ASP   B 162 ? 0.1814 0.1564 0.3832 -0.0128 -0.0312 -0.0291 162 ASP   B O   
6451 C  CB  . ASP   B 162 ? 0.2022 0.1734 0.4023 -0.0076 -0.0046 -0.0824 162 ASP   B CB  
6452 C  CG  . ASP   B 162 ? 0.2107 0.2043 0.4258 0.0040  -0.0027 -0.0955 162 ASP   B CG  
6453 O  OD1 . ASP   B 162 ? 0.2142 0.2203 0.4159 -0.0072 0.0139  -0.0894 162 ASP   B OD1 
6454 O  OD2 . ASP   B 162 ? 0.2205 0.2264 0.4517 0.0248  -0.0030 -0.0952 162 ASP   B OD2 
6459 N  N   . LYS   B 163 ? 0.1755 0.1368 0.3716 -0.0091 -0.0328 -0.0289 163 LYS   B N   
6460 C  CA  . LYS   B 163 ? 0.1884 0.1492 0.3700 -0.0132 -0.0223 -0.0141 163 LYS   B CA  
6461 C  C   . LYS   B 163 ? 0.1617 0.1434 0.3438 -0.0164 -0.0280 -0.0032 163 LYS   B C   
6462 O  O   . LYS   B 163 ? 0.1585 0.1544 0.3638 -0.0239 -0.0330 -0.0030 163 LYS   B O   
6463 C  CB  . LYS   B 163 ? 0.2298 0.1825 0.3981 -0.0134 -0.0240 0.0006  163 LYS   B CB  
6464 C  CG  . LYS   B 163 ? 0.3022 0.2567 0.4376 -0.0161 -0.0127 0.0071  163 LYS   B CG  
6465 C  CD  . LYS   B 163 ? 0.3658 0.3142 0.4900 -0.0239 -0.0076 0.0044  163 LYS   B CD  
6466 C  CE  . LYS   B 163 ? 0.4217 0.3719 0.5220 -0.0298 0.0012  0.0025  163 LYS   B CE  
6467 N  NZ  . LYS   B 163 ? 0.4533 0.3976 0.5438 -0.0328 0.0055  -0.0028 163 LYS   B NZ  
6481 N  N   . LEU   B 164 ? 0.1466 0.1361 0.3171 -0.0120 -0.0242 -0.0074 164 LEU   B N   
6482 C  CA  . LEU   B 164 ? 0.1500 0.1392 0.3092 -0.0159 -0.0271 0.0010  164 LEU   B CA  
6483 C  C   . LEU   B 164 ? 0.1584 0.1371 0.3098 -0.0168 -0.0333 -0.0007 164 LEU   B C   
6484 O  O   . LEU   B 164 ? 0.1623 0.1637 0.3292 -0.0163 -0.0391 0.0022  164 LEU   B O   
6485 C  CB  . LEU   B 164 ? 0.1475 0.1341 0.2967 -0.0147 -0.0233 -0.0000 164 LEU   B CB  
6486 C  CG  . LEU   B 164 ? 0.1585 0.1495 0.3006 -0.0153 -0.0126 0.0018  164 LEU   B CG  
6487 C  CD1 . LEU   B 164 ? 0.1625 0.1514 0.2948 -0.0172 -0.0204 -0.0091 164 LEU   B CD1 
6488 C  CD2 . LEU   B 164 ? 0.1748 0.1820 0.3170 -0.0142 0.0033  -0.0030 164 LEU   B CD2 
6500 N  N   . VAL   B 165 ? 0.1939 0.1500 0.3268 -0.0223 -0.0386 -0.0137 165 VAL   B N   
6501 C  CA  . VAL   B 165 ? 0.2338 0.1654 0.3329 -0.0327 -0.0629 -0.0155 165 VAL   B CA  
6502 C  C   . VAL   B 165 ? 0.2622 0.1749 0.3629 -0.0422 -0.0983 -0.0095 165 VAL   B C   
6503 O  O   . VAL   B 165 ? 0.2833 0.1890 0.3805 -0.0507 -0.1112 0.0024  165 VAL   B O   
6504 C  CB  . VAL   B 165 ? 0.2615 0.1813 0.3326 -0.0212 -0.0302 -0.0211 165 VAL   B CB  
6505 C  CG1 . VAL   B 165 ? 0.2790 0.1870 0.3452 -0.0213 -0.0174 -0.0164 165 VAL   B CG1 
6506 C  CG2 . VAL   B 165 ? 0.2631 0.1819 0.3209 -0.0159 -0.0172 -0.0194 165 VAL   B CG2 
6516 N  N   . SER   B 166 ? 0.2695 0.1635 0.3984 -0.0388 -0.1010 -0.0309 166 SER   B N   
6517 C  CA  . SER   B 166 ? 0.2610 0.1627 0.4486 -0.0392 -0.0861 -0.0337 166 SER   B CA  
6518 C  C   . SER   B 166 ? 0.2464 0.1756 0.4710 -0.0442 -0.0771 -0.0050 166 SER   B C   
6519 O  O   . SER   B 166 ? 0.2491 0.1939 0.4986 -0.0591 -0.0811 -0.0258 166 SER   B O   
6520 C  CB  . SER   B 166 ? 0.2594 0.1736 0.4706 -0.0329 -0.0754 -0.0472 166 SER   B CB  
6521 O  OG  . SER   B 166 ? 0.2439 0.1742 0.4790 -0.0262 -0.0733 -0.0345 166 SER   B OG  
6527 N  N   . SER   B 167 ? 0.2208 0.1697 0.4430 -0.0454 -0.0842 0.0371  167 SER   B N   
6528 C  CA  . SER   B 167 ? 0.2100 0.1784 0.4260 -0.0416 -0.0601 0.0376  167 SER   B CA  
6529 C  C   . SER   B 167 ? 0.2076 0.1872 0.4006 -0.0524 -0.0529 0.0557  167 SER   B C   
6530 O  O   . SER   B 167 ? 0.2064 0.2014 0.4002 -0.0576 -0.0500 0.0499  167 SER   B O   
6531 C  CB  . SER   B 167 ? 0.1959 0.1868 0.4299 -0.0353 -0.0322 0.0272  167 SER   B CB  
6532 O  OG  . SER   B 167 ? 0.1880 0.1938 0.4239 -0.0233 -0.0133 0.0301  167 SER   B OG  
6538 N  N   . PHE   B 168 ? 0.2080 0.1827 0.3814 -0.0484 -0.0415 0.0605  168 PHE   B N   
6539 C  CA  . PHE   B 168 ? 0.2087 0.1799 0.3493 -0.0486 -0.0362 0.0349  168 PHE   B CA  
6540 C  C   . PHE   B 168 ? 0.1858 0.1688 0.3021 -0.0284 -0.0188 0.0145  168 PHE   B C   
6541 O  O   . PHE   B 168 ? 0.2064 0.1617 0.2972 -0.0056 -0.0145 0.0026  168 PHE   B O   
6542 C  CB  . PHE   B 168 ? 0.2230 0.1832 0.3577 -0.0578 -0.0467 0.0418  168 PHE   B CB  
6543 C  CG  . PHE   B 168 ? 0.2452 0.1649 0.3394 -0.0586 -0.0500 0.0198  168 PHE   B CG  
6544 C  CD1 . PHE   B 168 ? 0.2737 0.1693 0.3454 -0.0518 -0.0498 0.0154  168 PHE   B CD1 
6545 C  CD2 . PHE   B 168 ? 0.2323 0.1607 0.3292 -0.0522 -0.0492 0.0304  168 PHE   B CD2 
6546 C  CE1 . PHE   B 168 ? 0.2850 0.1786 0.3292 -0.0376 -0.0415 0.0208  168 PHE   B CE1 
6547 C  CE2 . PHE   B 168 ? 0.2609 0.1698 0.3289 -0.0359 -0.0548 0.0216  168 PHE   B CE2 
6548 C  CZ  . PHE   B 168 ? 0.2765 0.1676 0.3267 -0.0262 -0.0509 0.0334  168 PHE   B CZ  
6558 N  N   . LEU   B 169 ? 0.1934 0.1780 0.2978 -0.0070 0.0010  0.0019  169 LEU   B N   
6559 C  CA  . LEU   B 169 ? 0.2195 0.2140 0.3165 -0.0073 0.0081  -0.0276 169 LEU   B CA  
6560 C  C   . LEU   B 169 ? 0.2473 0.2378 0.3732 0.0049  0.0080  -0.0530 169 LEU   B C   
6561 O  O   . LEU   B 169 ? 0.2636 0.2548 0.4192 0.0061  0.0058  -0.0712 169 LEU   B O   
6562 C  CB  . LEU   B 169 ? 0.2371 0.2532 0.3206 -0.0121 0.0048  -0.0061 169 LEU   B CB  
6563 C  CG  . LEU   B 169 ? 0.2691 0.2902 0.3462 -0.0068 0.0070  0.0006  169 LEU   B CG  
6564 C  CD1 . LEU   B 169 ? 0.2848 0.3067 0.3458 -0.0067 0.0030  0.0169  169 LEU   B CD1 
6565 C  CD2 . LEU   B 169 ? 0.2594 0.2995 0.3447 0.0028  0.0230  -0.0118 169 LEU   B CD2 
6566 O  OXT . LEU   B 169 ? 0.2619 0.2500 0.3791 0.0260  0.0162  -0.0545 169 LEU   B OXT 
6578 C  C1  T TFA   C .   ? 0.1390 0.1520 0.1362 -0.0036 0.0293  0.0150  201 TFA   A C1  
6579 C  C2  T TFA   C .   ? 0.1624 0.1755 0.1714 -0.0174 0.0226  -0.0033 201 TFA   A C2  
6580 O  O   T TFA   C .   ? 0.1170 0.1322 0.1219 -0.0076 0.0236  0.0242  201 TFA   A O   
6581 F  F1  T TFA   C .   ? 0.1701 0.1799 0.2005 -0.0129 0.0134  -0.0078 201 TFA   A F1  
6582 F  F2  T TFA   C .   ? 0.1736 0.1805 0.1646 -0.0209 0.0298  0.0037  201 TFA   A F2  
6583 F  F3  T TFA   C .   ? 0.1695 0.1946 0.1912 -0.0294 0.0294  -0.0200 201 TFA   A F3  
6584 O  OXT T TFA   C .   ? 0.1394 0.1456 0.1314 0.0259  0.0315  0.0203  201 TFA   A OXT 
6585 N  N2  B A1A84 D .   ? 0.2067 0.2217 0.2222 -0.0050 -0.0241 0.0075  202 A1A84 A N2  
6586 C  C3  B A1A84 D .   ? 0.2500 0.2803 0.2573 0.0097  -0.0149 -0.0111 202 A1A84 A C3  
6587 C  C6  B A1A84 D .   ? 0.2046 0.2293 0.2178 -0.0046 -0.0191 0.0125  202 A1A84 A C6  
6588 C  C9  B A1A84 D .   ? 0.1828 0.2148 0.2003 -0.0027 -0.0188 0.0229  202 A1A84 A C9  
6589 C  C1  B A1A84 D .   ? 0.2501 0.2772 0.2508 0.0163  -0.0211 -0.0009 202 A1A84 A C1  
6590 C  C10 B A1A84 D .   ? 0.1673 0.2090 0.1927 -0.0053 -0.0112 0.0383  202 A1A84 A C10 
6591 C  C11 B A1A84 D .   ? 0.1514 0.1947 0.1884 -0.0113 -0.0259 0.0462  202 A1A84 A C11 
6592 C  C2  B A1A84 D .   ? 0.2533 0.2823 0.2585 0.0126  -0.0172 -0.0091 202 A1A84 A C2  
6593 C  C4  B A1A84 D .   ? 0.2415 0.2703 0.2498 0.0020  -0.0122 -0.0103 202 A1A84 A C4  
6594 C  C5  B A1A84 D .   ? 0.2491 0.2756 0.2531 0.0037  -0.0057 -0.0188 202 A1A84 A C5  
6595 C  C7  B A1A84 D .   ? 0.2026 0.2159 0.2148 0.0002  -0.0266 0.0160  202 A1A84 A C7  
6596 C  C8  B A1A84 D .   ? 0.1763 0.2009 0.1899 -0.0018 -0.0265 0.0285  202 A1A84 A C8  
6597 N  N1  B A1A84 D .   ? 0.2205 0.2505 0.2331 -0.0038 -0.0176 0.0035  202 A1A84 A N1  
6598 N  N3  B A1A84 D .   ? 0.1933 0.2067 0.1996 0.0012  -0.0266 0.0255  202 A1A84 A N3  
6599 N  N4  B A1A84 D .   ? 0.1538 0.1862 0.1792 -0.0043 -0.0297 0.0437  202 A1A84 A N4  
6600 O  O1  B A1A84 D .   ? 0.2505 0.2789 0.2571 0.0009  -0.0048 -0.0171 202 A1A84 A O1  
6613 CL CL  B CL    E .   ? 0.2007 0.1733 0.2669 -0.0109 -0.0411 0.0264  203 CL    A CL  
6614 O  O   . HOH   F .   ? 0.3973 0.8110 0.4609 -0.1223 0.0022  0.1289  301 HOH   A O   
6615 O  O   . HOH   F .   ? 0.2432 0.2349 0.3964 -0.0145 -0.0333 0.0422  302 HOH   A O   
6616 O  O   . HOH   F .   ? 0.4521 0.3817 0.4823 -0.0411 0.1164  -0.0416 303 HOH   A O   
6617 O  O   . HOH   F .   ? 0.6239 0.4738 0.3050 0.1835  -0.1414 0.0394  304 HOH   A O   
6618 O  O   . HOH   F .   ? 0.2280 0.2518 0.2491 -0.0238 0.0527  0.0460  305 HOH   A O   
6619 O  O   B HOH   F .   ? 0.3997 0.2983 0.3734 -0.0272 0.0206  0.0074  306 HOH   A O   
6620 O  O   . HOH   F .   ? 0.6090 0.6887 0.5673 -0.1326 -0.1226 -0.1209 307 HOH   A O   
6621 O  O   . HOH   F .   ? 0.2979 0.5466 0.6109 0.1143  0.0810  0.1307  308 HOH   A O   
6622 O  O   . HOH   F .   ? 0.7257 0.5951 0.5044 -0.1162 0.0303  0.2336  309 HOH   A O   
6623 O  O   . HOH   F .   ? 0.6224 0.4584 0.6099 -0.0988 0.1893  0.1541  310 HOH   A O   
6624 O  O   . HOH   F .   ? 0.2903 0.6488 0.6122 -0.0759 -0.0834 0.2569  311 HOH   A O   
6625 O  O   . HOH   F .   ? 0.1853 0.3809 0.3227 0.0621  -0.0033 0.0325  312 HOH   A O   
6626 O  O   . HOH   F .   ? 0.5075 0.4870 0.5445 -0.0518 0.1307  0.2454  313 HOH   A O   
6627 O  O   . HOH   F .   ? 0.1839 0.1797 0.2166 0.0189  -0.0292 0.0246  314 HOH   A O   
6628 O  O   . HOH   F .   ? 0.2829 0.5967 0.3681 0.0061  -0.0536 0.0624  315 HOH   A O   
6629 O  O   . HOH   F .   ? 0.3600 0.3367 0.3029 -0.1271 0.0047  0.0856  316 HOH   A O   
6630 O  O   . HOH   F .   ? 0.2216 0.1959 0.3490 -0.0523 0.0169  -0.0213 317 HOH   A O   
6631 O  O   . HOH   F .   ? 0.6325 0.3444 0.3975 -0.1191 -0.0959 0.0252  318 HOH   A O   
6632 O  O   . HOH   F .   ? 0.2990 0.3404 0.1698 -0.0448 0.0400  0.0417  319 HOH   A O   
6633 O  O   . HOH   F .   ? 0.6490 0.5595 0.3678 -0.0392 -0.0445 0.1104  320 HOH   A O   
6634 O  O   . HOH   F .   ? 0.1537 0.4267 0.2443 0.0017  0.0238  0.0730  321 HOH   A O   
6635 O  O   . HOH   F .   ? 0.4968 0.2145 0.5187 0.0555  -0.0103 -0.0192 322 HOH   A O   
6636 O  O   . HOH   F .   ? 0.4921 0.5088 0.6284 0.1741  0.1105  -0.1056 323 HOH   A O   
6637 O  O   . HOH   F .   ? 0.6218 0.4870 0.5356 -0.0634 -0.0097 0.0045  324 HOH   A O   
6638 O  O   . HOH   F .   ? 0.6296 0.6241 0.4660 -0.0247 0.0500  -0.0912 325 HOH   A O   
6639 O  O   B HOH   F .   ? 0.4489 0.3983 0.4838 -0.0810 0.0611  0.0015  326 HOH   A O   
6640 O  O   . HOH   F .   ? 0.4937 0.2697 0.3092 -0.1177 0.0566  0.0381  327 HOH   A O   
6641 O  O   . HOH   F .   ? 0.3496 0.3753 0.4442 -0.0817 0.1479  0.0159  328 HOH   A O   
6642 O  O   . HOH   F .   ? 0.1599 0.1562 0.2447 -0.0203 0.0076  0.0103  329 HOH   A O   
6643 O  O   . HOH   F .   ? 0.2025 0.3506 0.4003 -0.0257 0.0341  -0.0943 330 HOH   A O   
6644 O  O   . HOH   F .   ? 0.5281 0.5412 0.5022 0.0563  0.2515  -0.0406 331 HOH   A O   
6645 O  O   . HOH   F .   ? 0.3208 0.2853 0.4294 -0.0543 -0.1298 0.1236  332 HOH   A O   
6646 O  O   . HOH   F .   ? 0.6296 0.6140 0.4152 0.2144  -0.0080 -0.0356 333 HOH   A O   
6647 O  O   . HOH   F .   ? 0.2429 0.4130 0.3658 0.0942  -0.0788 -0.0088 334 HOH   A O   
6648 O  O   . HOH   F .   ? 0.3302 0.4614 0.2495 -0.0151 0.0626  0.0236  335 HOH   A O   
6649 O  O   . HOH   F .   ? 0.5542 0.1939 0.4512 0.0179  -0.1430 0.0515  336 HOH   A O   
6650 O  O   . HOH   F .   ? 0.2369 0.2168 0.2872 0.0356  0.0271  0.0551  337 HOH   A O   
6651 O  O   A HOH   F .   ? 0.1967 0.2667 0.4067 -0.0071 0.0785  0.1436  338 HOH   A O   
6652 O  O   B HOH   F .   ? 0.2487 0.1893 0.2533 -0.0010 -0.0081 0.0258  339 HOH   A O   
6653 O  O   . HOH   F .   ? 0.2114 0.4297 0.4261 -0.0346 -0.0651 0.1698  340 HOH   A O   
6654 O  O   . HOH   F .   ? 0.2686 0.2282 0.2458 -0.0303 0.0163  -0.0055 341 HOH   A O   
6655 O  O   . HOH   F .   ? 0.5337 0.4314 0.4778 -0.1760 -0.0883 0.2310  342 HOH   A O   
6656 O  O   . HOH   F .   ? 0.5175 0.5014 0.3160 -0.1081 0.1584  0.0554  343 HOH   A O   
6657 O  O   . HOH   F .   ? 0.2083 0.1967 0.4542 0.0180  0.1228  -0.0165 344 HOH   A O   
6658 O  O   . HOH   F .   ? 0.1560 0.2100 0.2155 0.0050  -0.0092 0.0431  345 HOH   A O   
6659 O  O   . HOH   F .   ? 0.3087 0.3229 0.5101 -0.0705 -0.1008 -0.0702 346 HOH   A O   
6660 O  O   . HOH   F .   ? 0.2290 0.1834 0.2658 0.0005  -0.0615 -0.0111 347 HOH   A O   
6661 O  O   . HOH   F .   ? 0.1841 0.2494 0.2984 -0.0251 0.0569  0.0608  348 HOH   A O   
6662 O  O   . HOH   F .   ? 0.2702 0.3766 0.3655 -0.0875 -0.0494 -0.0366 349 HOH   A O   
6663 O  O   . HOH   F .   ? 0.1403 0.1331 0.1495 -0.0030 0.0148  0.0094  350 HOH   A O   
6664 O  O   . HOH   F .   ? 0.3448 0.6798 0.4153 -0.0773 0.0109  0.1599  351 HOH   A O   
6665 O  O   . HOH   F .   ? 0.2261 0.1770 0.2493 0.0358  -0.0412 0.0023  352 HOH   A O   
6666 O  O   A HOH   F .   ? 0.1812 0.2658 0.2077 0.0178  0.0329  0.0267  353 HOH   A O   
6667 O  O   . HOH   F .   ? 0.3246 0.3447 0.2298 -0.0503 -0.0684 0.0420  354 HOH   A O   
6668 O  O   . HOH   F .   ? 0.3347 0.2905 0.3446 -0.0860 -0.0046 -0.0056 355 HOH   A O   
6669 O  O   . HOH   F .   ? 0.2104 0.1706 0.1636 -0.0082 0.0194  0.0229  356 HOH   A O   
6670 O  O   . HOH   F .   ? 0.3937 0.2154 0.2808 0.1047  0.0653  0.0348  357 HOH   A O   
6671 O  O   . HOH   F .   ? 0.3259 0.3831 0.2310 -0.1271 -0.0114 -0.0618 358 HOH   A O   
6672 O  O   . HOH   F .   ? 0.1563 0.1353 0.2511 -0.0105 0.0161  -0.0085 359 HOH   A O   
6673 O  O   . HOH   F .   ? 0.1563 0.1970 0.2593 0.0017  -0.0047 0.0191  360 HOH   A O   
6674 O  O   . HOH   F .   ? 0.3886 0.7113 0.5076 -0.0808 -0.1274 0.0591  361 HOH   A O   
6675 O  O   . HOH   F .   ? 0.2106 0.2622 0.3656 0.0160  0.0895  -0.0680 362 HOH   A O   
6676 O  O   . HOH   F .   ? 0.3914 0.4472 0.4395 0.2209  0.0487  0.0203  363 HOH   A O   
6677 O  O   . HOH   F .   ? 0.3296 0.4382 0.3586 -0.0647 -0.0543 0.1093  364 HOH   A O   
6678 O  O   . HOH   F .   ? 0.2522 0.4015 0.3483 -0.0412 0.0644  0.0067  365 HOH   A O   
6679 O  O   A HOH   F .   ? 0.1401 0.1960 0.1958 0.0429  0.0320  0.0435  366 HOH   A O   
6680 O  O   . HOH   F .   ? 0.5094 0.5824 0.5740 0.0829  -0.0537 0.1788  367 HOH   A O   
6681 O  O   . HOH   F .   ? 0.1543 0.1603 0.1595 -0.0092 -0.0094 -0.0051 368 HOH   A O   
6682 O  O   . HOH   F .   ? 0.1637 0.1778 0.2835 0.0047  -0.0394 -0.0404 369 HOH   A O   
6683 O  O   . HOH   F .   ? 0.1813 0.2284 0.1948 -0.0280 -0.0047 0.0681  370 HOH   A O   
6684 O  O   . HOH   F .   ? 0.2619 0.4460 0.3367 0.0530  0.0786  0.2045  371 HOH   A O   
6685 O  O   . HOH   F .   ? 0.4356 0.2643 0.3818 -0.1413 0.1757  -0.0715 372 HOH   A O   
6686 O  O   . HOH   F .   ? 0.1884 0.1892 0.2476 -0.0337 0.0058  0.0366  373 HOH   A O   
6687 O  O   . HOH   F .   ? 0.1965 0.1986 0.1837 -0.0002 0.0110  0.0150  374 HOH   A O   
6688 O  O   . HOH   F .   ? 0.3372 0.6929 0.3123 0.1421  0.0746  -0.0640 375 HOH   A O   
6689 O  O   T HOH   F .   ? 0.1180 0.1126 0.2531 -0.0129 0.0044  0.0475  376 HOH   A O   
6690 O  O   . HOH   F .   ? 0.5965 0.4144 0.3534 -0.0206 -0.0177 0.1596  377 HOH   A O   
6691 O  O   . HOH   F .   ? 0.4115 0.2573 0.4562 -0.1247 0.0812  0.0514  378 HOH   A O   
6692 O  O   . HOH   F .   ? 0.1784 0.1829 0.2533 -0.0256 0.0090  0.0405  379 HOH   A O   
6693 O  O   . HOH   F .   ? 0.2718 0.3621 0.3136 -0.0404 0.0829  -0.0514 380 HOH   A O   
6694 O  O   A HOH   F .   ? 0.3172 0.1641 0.1852 0.0152  0.0278  0.0065  381 HOH   A O   
6695 O  O   . HOH   F .   ? 0.3169 0.2953 0.2320 0.0337  0.0834  0.0156  382 HOH   A O   
6696 O  O   . HOH   F .   ? 0.5934 0.5430 0.7195 -0.0425 -0.0018 0.1418  383 HOH   A O   
6697 O  O   . HOH   F .   ? 0.3219 0.2577 0.4761 -0.0653 -0.0363 0.0267  384 HOH   A O   
6698 O  O   . HOH   F .   ? 0.2244 0.2493 0.5139 0.0071  0.0023  -0.0710 385 HOH   A O   
6699 O  O   . HOH   F .   ? 0.1908 0.2875 0.2723 0.0397  0.0457  0.0939  386 HOH   A O   
6700 O  O   . HOH   F .   ? 0.2579 0.2161 0.1886 -0.0651 -0.0028 0.0430  387 HOH   A O   
6701 O  O   . HOH   F .   ? 0.2118 0.2205 0.2932 -0.0179 -0.0370 0.0871  388 HOH   A O   
6702 O  O   . HOH   F .   ? 0.2013 0.2416 0.2571 -0.0370 -0.0543 0.0617  389 HOH   A O   
6703 O  O   . HOH   F .   ? 0.1592 0.1801 0.1833 0.0173  -0.0200 -0.0316 390 HOH   A O   
6704 O  O   . HOH   F .   ? 0.3382 0.2842 0.3115 -0.0179 -0.0378 0.1065  391 HOH   A O   
6705 O  O   . HOH   F .   ? 0.1862 0.1974 0.3857 0.0331  0.0955  0.1047  392 HOH   A O   
6706 O  O   A HOH   F .   ? 0.1769 0.1736 0.2603 -0.0013 -0.0389 0.0237  393 HOH   A O   
6707 O  O   . HOH   F .   ? 0.3586 0.3653 0.2602 -0.0592 -0.0506 0.0263  394 HOH   A O   
6708 O  O   A HOH   F .   ? 0.1946 0.1792 0.3083 -0.0186 0.0475  -0.0095 395 HOH   A O   
6709 O  O   B HOH   F .   ? 0.1753 0.2008 0.4207 -0.0102 -0.0093 0.0370  396 HOH   A O   
6710 O  O   . HOH   F .   ? 0.2568 0.4112 0.3327 -0.0355 0.0843  -0.0783 397 HOH   A O   
6711 O  O   . HOH   F .   ? 0.3743 0.6096 0.5765 0.1263  0.1773  0.0392  398 HOH   A O   
6712 O  O   . HOH   F .   ? 0.7923 0.3960 0.6158 -0.0502 -0.1330 0.0733  399 HOH   A O   
6713 O  O   . HOH   F .   ? 0.2650 0.1895 0.2678 -0.0065 0.0103  0.0305  400 HOH   A O   
6714 O  O   . HOH   F .   ? 0.1386 0.1470 0.1888 -0.0035 -0.0175 0.0059  401 HOH   A O   
6715 O  O   A HOH   F .   ? 0.2237 0.2545 0.2044 0.0686  0.0605  0.0453  402 HOH   A O   
6716 O  O   . HOH   F .   ? 0.4213 0.4758 0.3743 0.2044  0.0197  -0.0620 403 HOH   A O   
6717 O  O   . HOH   F .   ? 0.1712 0.1919 0.2055 0.0017  -0.0260 0.0120  404 HOH   A O   
6718 O  O   . HOH   F .   ? 0.3271 0.3807 0.3599 -0.1527 0.0877  -0.0201 405 HOH   A O   
6719 O  O   . HOH   F .   ? 0.5886 0.5951 0.5141 0.0322  0.1276  0.0314  406 HOH   A O   
6720 O  O   . HOH   F .   ? 0.5771 0.2930 0.5208 0.0855  -0.0679 -0.0134 407 HOH   A O   
6721 O  O   . HOH   F .   ? 0.4777 0.4103 0.6511 0.1368  0.1771  -0.1242 408 HOH   A O   
6722 O  O   . HOH   F .   ? 0.1605 0.1744 0.3290 -0.0052 -0.0058 0.0296  409 HOH   A O   
6723 O  O   . HOH   F .   ? 0.5252 0.5270 0.2021 -0.0019 0.0872  0.0948  410 HOH   A O   
6724 O  O   . HOH   F .   ? 0.2494 0.3000 0.3393 -0.0096 -0.0108 -0.0810 411 HOH   A O   
6725 O  O   . HOH   F .   ? 0.3347 0.4016 0.4070 -0.0925 0.1518  -0.0113 412 HOH   A O   
6726 O  O   . HOH   F .   ? 0.3113 0.2822 0.2295 -0.0838 -0.0887 0.0393  413 HOH   A O   
6727 O  O   A HOH   F .   ? 0.1947 0.2326 0.2600 0.0224  -0.0014 0.0617  414 HOH   A O   
6728 O  O   . HOH   F .   ? 0.1942 0.2626 0.4117 -0.0037 -0.0280 0.0293  415 HOH   A O   
6729 O  O   . HOH   F .   ? 0.1811 0.1447 0.1651 -0.0219 0.0169  0.0034  416 HOH   A O   
6730 O  O   . HOH   F .   ? 0.2294 0.1807 0.3278 0.0049  -0.0369 0.0099  417 HOH   A O   
6731 O  O   . HOH   F .   ? 0.2119 0.3135 0.2663 -0.0166 -0.0543 0.0534  418 HOH   A O   
6732 O  O   . HOH   F .   ? 0.2384 0.2181 0.2817 -0.0553 -0.0083 0.0626  419 HOH   A O   
6733 O  O   . HOH   F .   ? 0.4813 0.5097 0.3993 0.1537  -0.1007 -0.1568 420 HOH   A O   
6734 O  O   . HOH   F .   ? 0.2919 0.5995 0.1801 -0.0243 0.0529  0.0243  421 HOH   A O   
6735 O  O   . HOH   F .   ? 0.3425 0.1375 0.1991 0.0008  -0.0445 0.0115  422 HOH   A O   
6736 O  O   . HOH   F .   ? 0.3040 0.3704 0.7148 -0.0206 0.0838  -0.0623 423 HOH   A O   
6737 O  O   . HOH   F .   ? 0.1655 0.2127 0.2736 -0.0128 -0.0030 0.0416  424 HOH   A O   
6738 O  O   . HOH   F .   ? 0.2357 0.4060 0.2607 0.1517  0.0000  0.0216  425 HOH   A O   
6739 O  O   . HOH   F .   ? 0.6300 0.4040 0.4813 0.1459  -0.0909 0.1395  426 HOH   A O   
6740 O  O   . HOH   F .   ? 0.2078 0.1951 0.3570 0.0238  -0.0725 0.0307  427 HOH   A O   
6741 O  O   . HOH   F .   ? 0.4104 0.2431 0.5980 -0.0951 -0.2104 0.1268  428 HOH   A O   
6742 O  O   . HOH   F .   ? 0.4718 0.7031 0.3408 -0.1111 -0.0195 0.1710  429 HOH   A O   
6743 O  O   . HOH   F .   ? 0.6127 0.7252 0.4624 0.1041  0.2916  -0.0502 430 HOH   A O   
6744 O  O   . HOH   F .   ? 0.5949 0.6648 0.7019 -0.1199 -0.1100 -0.0610 431 HOH   A O   
6745 O  O   . HOH   F .   ? 0.9633 0.9555 0.8093 -0.0306 -0.0479 -0.0315 432 HOH   A O   
6746 O  O   . HOH   F .   ? 0.3533 0.2943 0.1965 -0.0914 0.0101  0.0792  433 HOH   A O   
6747 O  O   . HOH   F .   ? 0.2629 0.3986 0.5137 -0.0100 0.0858  -0.1784 434 HOH   A O   
6748 O  O   . HOH   F .   ? 0.5557 0.4497 0.4395 -0.0458 -0.1506 0.0291  435 HOH   A O   
6749 O  O   A HOH   F .   ? 0.5521 0.4941 0.3045 -0.1257 -0.0089 0.1586  436 HOH   A O   
6750 O  O   . HOH   F .   ? 0.5842 0.8707 0.4677 0.2161  -0.0909 0.1986  437 HOH   A O   
6751 O  O   . HOH   F .   ? 0.2668 0.1661 0.2895 0.0048  -0.0009 0.0148  438 HOH   A O   
6752 O  O   . HOH   F .   ? 0.1915 0.2276 0.4888 -0.0219 -0.0845 0.0564  439 HOH   A O   
6753 O  O   . HOH   F .   ? 0.1843 0.1609 0.1797 -0.0089 0.0004  -0.0061 440 HOH   A O   
6754 O  O   . HOH   F .   ? 0.6818 0.3842 0.5410 0.0573  0.1016  0.1687  441 HOH   A O   
6755 O  O   . HOH   F .   ? 0.6827 0.6512 0.7048 -0.1363 -0.0222 -0.1297 442 HOH   A O   
6756 O  O   . HOH   F .   ? 0.3896 0.3794 0.2976 0.2233  -0.0661 -0.0471 443 HOH   A O   
6757 O  O   . HOH   F .   ? 0.5886 0.7125 0.6572 -0.1298 0.0567  -0.0100 444 HOH   A O   
6758 O  O   B HOH   F .   ? 0.3927 0.2494 0.3238 0.1087  -0.1023 0.0346  445 HOH   A O   
6759 O  O   A HOH   F .   ? 0.4076 0.2190 0.2891 -0.0396 0.0344  0.0553  446 HOH   A O   
6760 O  O   A HOH   F .   ? 0.2708 0.2064 0.2398 -0.0254 0.0341  -0.0219 447 HOH   A O   
6761 O  O   . HOH   F .   ? 0.4737 0.5230 0.5081 -0.1174 -0.1072 -0.1328 448 HOH   A O   
6762 O  O   . HOH   F .   ? 0.2184 0.2778 0.2682 0.0059  -0.0185 -0.0346 449 HOH   A O   
6763 O  O   . HOH   F .   ? 0.2163 0.2168 0.2911 0.0030  0.0080  0.0157  450 HOH   A O   
6764 O  O   . HOH   F .   ? 0.6326 0.3960 0.6371 0.0414  0.1186  -0.1205 451 HOH   A O   
6765 O  O   . HOH   F .   ? 0.7302 0.6384 0.6935 0.0604  -0.1174 -0.0221 452 HOH   A O   
6766 O  O   . HOH   F .   ? 0.6582 0.5876 0.7555 0.0658  -0.1096 0.1857  453 HOH   A O   
6767 O  O   . HOH   F .   ? 0.6499 0.6347 0.4824 -0.0882 0.0895  0.1330  454 HOH   A O   
6768 O  O   . HOH   F .   ? 0.5140 0.4205 0.3867 0.0072  0.0973  0.0405  455 HOH   A O   
6769 O  O   . HOH   F .   ? 0.4753 0.5070 0.4872 0.0067  -0.0038 0.0866  456 HOH   A O   
6770 O  O   . HOH   F .   ? 0.4045 0.3324 0.4104 0.0359  0.0475  0.0335  457 HOH   A O   
6771 O  O   . HOH   F .   ? 0.3895 0.4411 0.4235 0.2046  -0.0295 0.0844  458 HOH   A O   
6772 O  O   . HOH   F .   ? 0.6710 0.7581 0.4653 0.1421  -0.0732 -0.0610 459 HOH   A O   
6773 O  O   . HOH   F .   ? 0.2724 0.2690 0.3861 -0.0384 0.0352  -0.0737 460 HOH   A O   
6774 O  O   . HOH   F .   ? 0.4008 0.5559 0.5778 -0.1438 0.1573  -0.1177 461 HOH   A O   
6775 O  O   B HOH   F .   ? 0.2214 0.3669 0.3906 0.0306  0.0676  0.0362  462 HOH   A O   
6776 O  O   . HOH   F .   ? 0.3854 0.4695 0.4679 0.0275  -0.0730 0.0860  463 HOH   A O   
6777 O  O   . HOH   F .   ? 0.2694 0.4478 0.5278 0.0575  -0.0113 -0.1913 464 HOH   A O   
6778 O  O   . HOH   F .   ? 0.2795 0.2836 0.3648 -0.0925 0.0531  -0.0102 465 HOH   A O   
6779 O  O   . HOH   F .   ? 0.6320 0.3461 0.7312 0.1235  0.0278  0.2045  466 HOH   A O   
6780 O  O   . HOH   F .   ? 0.2513 0.1836 0.2682 0.0231  -0.0886 -0.0303 467 HOH   A O   
6781 O  O   A HOH   F .   ? 0.2777 0.2618 0.4870 0.1030  -0.1656 -0.1031 468 HOH   A O   
6782 O  O   . HOH   F .   ? 0.3929 0.6412 0.3936 -0.1045 -0.0882 0.2361  469 HOH   A O   
6783 O  O   . HOH   F .   ? 0.4043 0.4633 0.4339 -0.1321 0.0053  0.0155  470 HOH   A O   
6784 O  O   . HOH   F .   ? 0.3861 0.5312 0.4107 0.0611  -0.0510 -0.0919 471 HOH   A O   
6785 O  O   . HOH   F .   ? 0.5909 0.4883 0.4991 0.0276  0.1406  0.0390  472 HOH   A O   
6786 O  O   . HOH   F .   ? 0.7439 0.6901 0.6981 0.1041  0.1861  0.2127  473 HOH   A O   
6787 O  O   . HOH   F .   ? 0.3728 0.2782 0.3953 0.0334  0.1056  0.0000  474 HOH   A O   
6788 O  O   . HOH   F .   ? 0.5368 0.5236 0.4400 0.0470  -0.0617 -0.0414 475 HOH   A O   
6789 O  O   . HOH   F .   ? 0.4484 0.4379 0.5027 -0.1982 -0.0368 -0.0361 476 HOH   A O   
6790 O  O   . HOH   F .   ? 0.3831 0.5168 0.2725 0.0242  -0.0028 -0.0019 477 HOH   A O   
6791 O  O   . HOH   F .   ? 0.5768 0.4130 0.4394 0.0108  -0.0240 -0.1096 478 HOH   A O   
6792 O  O   . HOH   F .   ? 0.6317 0.6081 0.6141 -0.1669 -0.1378 -0.0137 479 HOH   A O   
6793 O  O   . HOH   F .   ? 0.7249 0.6089 0.7005 -0.0528 0.0360  -0.0927 480 HOH   A O   
6794 O  O   . HOH   F .   ? 0.4207 0.5116 0.3136 -0.0450 -0.0435 -0.0178 481 HOH   A O   
6795 O  O   . HOH   F .   ? 0.7962 0.3961 0.3291 -0.0392 -0.1327 0.0412  482 HOH   A O   
6796 O  O   . HOH   F .   ? 0.2557 0.2557 0.2504 0.0283  -0.0082 -0.0012 483 HOH   A O   
6797 O  O   . HOH   F .   ? 0.3137 0.4218 0.4915 0.0072  0.1464  0.1189  484 HOH   A O   
6798 O  O   . HOH   F .   ? 0.4741 0.2893 0.3535 -0.0726 -0.1338 0.0579  485 HOH   A O   
6799 O  O   . HOH   F .   ? 0.5817 0.3973 0.4249 -0.0314 0.1481  -0.0204 486 HOH   A O   
6800 O  O   . HOH   F .   ? 0.6868 0.6941 0.4950 -0.0910 0.1394  0.1915  487 HOH   A O   
6801 O  O   . HOH   F .   ? 0.2653 0.5317 0.3680 0.1063  0.0910  0.2460  488 HOH   A O   
6802 O  O   . HOH   F .   ? 0.6263 0.6147 0.7151 0.1064  0.2427  -0.1155 489 HOH   A O   
6803 O  O   . HOH   F .   ? 0.2453 0.2448 0.6991 0.0021  -0.1304 0.0294  490 HOH   A O   
6804 O  O   . HOH   F .   ? 0.4579 0.3467 0.5219 -0.0562 0.0292  0.1476  491 HOH   A O   
6805 O  O   . HOH   F .   ? 0.5438 0.5515 0.6443 0.0627  -0.1122 0.1297  492 HOH   A O   
6806 O  O   . HOH   F .   ? 0.4586 0.3912 0.2558 -0.0626 0.1379  -0.0506 493 HOH   A O   
6807 O  O   . HOH   F .   ? 0.6312 0.4928 0.5090 -0.0823 -0.1182 -0.0720 494 HOH   A O   
6808 O  O   . HOH   F .   ? 0.4732 0.3207 0.4844 -0.0367 0.2247  0.0467  495 HOH   A O   
6809 O  O   . HOH   F .   ? 0.3217 0.2311 0.5798 0.0205  0.0440  0.1177  496 HOH   A O   
6810 O  O   . HOH   F .   ? 0.2675 0.3781 0.5425 -0.0058 0.0970  -0.0741 497 HOH   A O   
6811 O  O   . HOH   F .   ? 0.6700 0.6275 0.4524 0.1594  -0.1460 -0.0383 498 HOH   A O   
6812 O  O   . HOH   F .   ? 0.6603 0.2420 0.3991 -0.0740 0.1119  0.0362  499 HOH   A O   
6813 O  O   B HOH   F .   ? 0.5037 0.1768 0.2829 0.0254  0.0291  0.0545  500 HOH   A O   
6814 O  O   . HOH   F .   ? 0.3000 0.4736 0.3202 -0.0044 -0.0375 -0.0915 501 HOH   A O   
6815 O  O   B HOH   F .   ? 0.2509 0.3976 0.3594 -0.0225 0.0367  0.0456  502 HOH   A O   
6816 O  O   . HOH   F .   ? 0.2791 0.3855 0.3541 0.0944  -0.0480 0.0517  503 HOH   A O   
6817 O  O   . HOH   F .   ? 0.3761 0.7983 0.5685 -0.0913 -0.0375 0.2096  504 HOH   A O   
6818 O  O   . HOH   F .   ? 0.2715 0.4597 0.5048 0.0367  -0.0737 0.0012  505 HOH   A O   
6819 O  O   . HOH   F .   ? 0.5604 0.8083 0.5365 0.0877  -0.0646 0.0666  506 HOH   A O   
6820 O  O   . HOH   F .   ? 0.6417 0.4891 0.5242 0.1739  -0.0022 0.1681  507 HOH   A O   
6821 O  O   . HOH   F .   ? 0.5748 0.6647 0.5551 0.3117  0.0471  0.1695  508 HOH   A O   
6822 O  O   . HOH   F .   ? 0.2984 0.2412 0.4772 0.0185  0.0279  0.0641  509 HOH   A O   
6823 O  O   T HOH   F .   ? 0.1240 0.1224 0.2207 -0.0178 -0.0132 0.0288  510 HOH   A O   
6824 O  O   A HOH   F .   ? 0.4043 0.7111 0.3120 0.2279  -0.0201 -0.0459 511 HOH   A O   
6825 O  O   . HOH   F .   ? 0.5785 0.6277 0.4246 -0.0847 -0.0347 -0.1286 512 HOH   A O   
6826 O  O   . HOH   F .   ? 0.2865 0.7364 0.4338 0.0410  0.0603  -0.0874 513 HOH   A O   
6827 O  O   . HOH   F .   ? 0.4691 0.7352 0.5342 -0.0532 -0.0699 0.0551  514 HOH   A O   
6828 O  O   . HOH   F .   ? 0.4736 0.4821 0.5433 0.1183  -0.0125 0.1820  515 HOH   A O   
6829 O  O   . HOH   F .   ? 0.2603 0.4798 0.6468 0.0007  -0.0634 0.2940  516 HOH   A O   
6830 O  O   . HOH   G .   ? 0.2371 0.2351 0.3374 0.0208  0.0833  0.0437  201 HOH   B O   
6831 O  O   . HOH   G .   ? 0.5074 0.3711 0.4164 0.0030  0.0083  -0.1625 202 HOH   B O   
6832 O  O   . HOH   G .   ? 0.3856 0.3132 0.7054 -0.0530 0.0191  -0.0389 203 HOH   B O   
6833 O  O   . HOH   G .   ? 0.3156 0.6954 0.3399 0.0791  0.0198  0.2252  204 HOH   B O   
6834 O  O   . HOH   G .   ? 0.7308 0.3083 0.4450 0.1168  0.0849  0.0051  205 HOH   B O   
6835 O  O   . HOH   G .   ? 0.5377 0.6319 0.4499 0.3101  -0.1298 -0.0073 206 HOH   B O   
6836 O  O   . HOH   G .   ? 0.3231 0.2349 0.5537 -0.0018 0.1978  0.0420  207 HOH   B O   
6837 O  O   . HOH   G .   ? 0.3476 0.3966 0.5258 -0.0868 0.0128  -0.1426 208 HOH   B O   
6838 O  O   . HOH   G .   ? 0.3210 0.5847 0.5188 -0.0111 0.1733  -0.1948 209 HOH   B O   
6839 O  O   . HOH   G .   ? 0.4380 0.5288 0.2746 0.0215  -0.0522 -0.1568 210 HOH   B O   
6840 O  O   . HOH   G .   ? 0.2001 0.2266 0.3086 -0.0029 0.0355  -0.0244 211 HOH   B O   
6841 O  O   . HOH   G .   ? 0.1701 0.2005 0.2969 -0.0183 -0.0081 0.0144  212 HOH   B O   
6842 O  O   . HOH   G .   ? 0.4183 0.3825 0.3696 0.0093  -0.1081 0.0640  213 HOH   B O   
6843 O  O   . HOH   G .   ? 0.2810 0.2835 0.6574 0.0468  -0.0920 0.0568  214 HOH   B O   
6844 O  O   . HOH   G .   ? 0.4083 0.5467 0.3802 0.2406  -0.0396 0.0224  215 HOH   B O   
6845 O  O   . HOH   G .   ? 0.3049 0.2050 0.5872 0.0140  0.1950  0.0798  216 HOH   B O   
6846 O  O   . HOH   G .   ? 0.6311 0.6234 0.5967 0.1311  0.0411  0.0322  217 HOH   B O   
6847 O  O   . HOH   G .   ? 0.4645 0.6868 0.4057 0.2202  0.0390  0.0100  218 HOH   B O   
6848 O  O   . HOH   G .   ? 0.3613 0.5567 0.5743 0.2526  0.0369  -0.0299 219 HOH   B O   
6849 O  O   . HOH   G .   ? 0.7217 0.4619 0.2937 -0.0925 0.0486  0.0348  220 HOH   B O   
6850 O  O   . HOH   G .   ? 0.4527 0.4023 0.6624 -0.0376 -0.1491 -0.0928 221 HOH   B O   
6851 O  O   . HOH   G .   ? 0.3368 0.3498 0.4372 0.0677  -0.0111 0.0365  222 HOH   B O   
6852 O  O   . HOH   G .   ? 0.2279 0.2295 0.4126 -0.0418 0.0078  -0.0612 223 HOH   B O   
6853 O  O   . HOH   G .   ? 0.4173 0.4801 0.3913 0.0353  0.0822  -0.1387 224 HOH   B O   
6854 O  O   . HOH   G .   ? 0.5796 0.3004 0.3976 -0.1766 0.0082  0.0239  225 HOH   B O   
6855 O  O   . HOH   G .   ? 0.1790 0.2165 0.3521 -0.0182 0.0152  -0.0083 226 HOH   B O   
6856 O  O   . HOH   G .   ? 0.5168 0.3996 0.6223 0.0478  -0.0919 0.2609  227 HOH   B O   
6857 O  O   . HOH   G .   ? 0.5079 0.2143 0.3058 -0.0113 -0.1040 0.0016  228 HOH   B O   
6858 O  O   . HOH   G .   ? 0.2442 0.1869 0.2797 -0.0320 0.0980  -0.0106 229 HOH   B O   
6859 O  O   . HOH   G .   ? 0.3756 0.1825 0.2017 0.0181  -0.0780 -0.0128 230 HOH   B O   
6860 O  O   . HOH   G .   ? 0.4207 0.2947 0.3973 0.1038  -0.0187 -0.0382 231 HOH   B O   
6861 O  O   . HOH   G .   ? 0.6719 0.6419 0.3340 0.0187  0.0188  0.0720  232 HOH   B O   
6862 O  O   . HOH   G .   ? 0.3628 0.2511 0.4415 0.0300  -0.0602 -0.1336 233 HOH   B O   
6863 O  O   . HOH   G .   ? 0.2159 0.2703 0.3437 -0.0575 0.0235  -0.0198 234 HOH   B O   
6864 O  O   . HOH   G .   ? 0.1491 0.1523 0.1564 -0.0145 -0.0098 -0.0070 235 HOH   B O   
6865 O  O   . HOH   G .   ? 0.2800 0.2585 0.3214 0.0318  0.0139  -0.0939 236 HOH   B O   
6866 O  O   . HOH   G .   ? 0.3338 0.4103 0.6643 0.0036  0.0847  0.0036  237 HOH   B O   
6867 O  O   . HOH   G .   ? 0.2179 0.3853 0.2670 -0.0557 -0.0189 0.0537  238 HOH   B O   
6868 O  O   . HOH   G .   ? 0.3734 0.3036 0.2147 0.0261  0.0624  0.0429  239 HOH   B O   
6869 O  O   . HOH   G .   ? 0.2100 0.1409 0.3440 0.0072  -0.0542 -0.0165 240 HOH   B O   
6870 O  O   . HOH   G .   ? 0.3963 0.4235 0.5526 -0.1579 -0.0058 0.0978  241 HOH   B O   
6871 O  O   . HOH   G .   ? 0.7553 0.5233 0.5043 0.2209  -0.0609 -0.1226 242 HOH   B O   
6872 O  O   . HOH   G .   ? 0.1642 0.1536 0.2670 -0.0052 0.0107  -0.0109 243 HOH   B O   
6873 O  O   . HOH   G .   ? 0.2230 0.2042 0.2133 -0.0341 -0.0469 0.0224  244 HOH   B O   
6874 O  O   . HOH   G .   ? 0.5109 0.3165 0.4052 -0.2273 -0.0158 0.0242  245 HOH   B O   
6875 O  O   . HOH   G .   ? 0.3354 0.2903 0.3394 -0.0279 0.0219  -0.0605 246 HOH   B O   
6876 O  O   . HOH   G .   ? 0.3282 0.1810 0.6426 -0.0313 -0.1052 -0.0288 247 HOH   B O   
6877 O  O   . HOH   G .   ? 0.3246 0.4241 0.2744 -0.1137 -0.0351 -0.0555 248 HOH   B O   
6878 O  O   . HOH   G .   ? 0.1542 0.1359 0.1696 0.0009  -0.0117 0.0069  249 HOH   B O   
6879 O  O   . HOH   G .   ? 0.2461 0.2176 0.2683 0.0699  -0.0779 -0.0593 250 HOH   B O   
6880 O  O   . HOH   G .   ? 0.2363 0.3808 0.3270 -0.0531 -0.0757 -0.0481 251 HOH   B O   
6881 O  O   . HOH   G .   ? 0.2973 0.3492 0.3054 -0.1018 0.0172  -0.0090 252 HOH   B O   
6882 O  O   . HOH   G .   ? 0.2840 0.2278 0.3102 0.0766  0.0828  0.0022  253 HOH   B O   
6883 O  O   . HOH   G .   ? 0.3400 0.4135 0.2343 0.0183  0.0876  0.0325  254 HOH   B O   
6884 O  O   . HOH   G .   ? 0.3057 0.2204 0.2017 0.0225  -0.0215 -0.0075 255 HOH   B O   
6885 O  O   . HOH   G .   ? 0.4669 0.4313 0.2959 0.0126  -0.0126 -0.0558 256 HOH   B O   
6886 O  O   . HOH   G .   ? 0.2441 0.5529 0.6115 0.1389  -0.0536 -0.0916 257 HOH   B O   
6887 O  O   . HOH   G .   ? 0.2112 0.1596 0.2256 -0.0281 -0.0389 0.0211  258 HOH   B O   
6888 O  O   . HOH   G .   ? 0.2176 0.3298 0.2336 -0.0583 0.0241  0.0460  259 HOH   B O   
6889 O  O   . HOH   G .   ? 0.1446 0.1681 0.2257 -0.0058 0.0038  0.0168  260 HOH   B O   
6890 O  O   . HOH   G .   ? 0.1733 0.1724 0.3337 -0.0280 -0.0140 0.0072  261 HOH   B O   
6891 O  O   . HOH   G .   ? 0.2771 0.4805 0.6447 -0.0201 0.0431  -0.1106 262 HOH   B O   
6892 O  O   . HOH   G .   ? 0.3589 0.4967 0.3408 -0.0445 -0.1189 0.0828  263 HOH   B O   
6893 O  O   . HOH   G .   ? 0.2123 0.1993 0.3652 -0.0008 -0.0483 -0.0332 264 HOH   B O   
6894 O  O   . HOH   G .   ? 0.4134 0.2694 0.4580 -0.0412 -0.1414 -0.0488 265 HOH   B O   
6895 O  O   . HOH   G .   ? 0.2554 0.2829 0.2607 -0.0382 -0.0852 0.0249  266 HOH   B O   
6896 O  O   . HOH   G .   ? 0.1978 0.1941 0.1752 -0.0512 -0.0455 0.0115  267 HOH   B O   
6897 O  O   . HOH   G .   ? 0.2487 0.2243 0.2038 0.0041  -0.0113 -0.0086 268 HOH   B O   
6898 O  O   . HOH   G .   ? 0.4951 0.3786 0.3748 -0.1458 0.0798  -0.1263 269 HOH   B O   
6899 O  O   . HOH   G .   ? 0.2758 0.3864 0.4215 0.0327  0.1546  0.0292  270 HOH   B O   
6900 O  O   . HOH   G .   ? 0.2222 0.4650 0.5090 -0.0467 -0.0431 -0.1469 271 HOH   B O   
6901 O  O   . HOH   G .   ? 0.3638 0.3979 0.4552 0.1329  -0.0517 -0.1173 272 HOH   B O   
6902 O  O   . HOH   G .   ? 0.1860 0.1496 0.3579 -0.0082 -0.0181 -0.0143 273 HOH   B O   
6903 O  O   . HOH   G .   ? 0.2180 0.1640 0.2327 -0.0329 -0.0169 0.0146  274 HOH   B O   
6904 O  O   . HOH   G .   ? 0.2772 0.2061 0.2991 -0.0671 0.0251  -0.0314 275 HOH   B O   
6905 O  O   . HOH   G .   ? 0.2895 0.2163 0.5420 0.0092  0.0832  0.0540  276 HOH   B O   
6906 O  O   . HOH   G .   ? 0.2564 0.3794 0.2564 0.1412  -0.0462 -0.0643 277 HOH   B O   
6907 O  O   . HOH   G .   ? 0.2397 0.2561 0.2391 -0.0288 -0.0715 -0.0426 278 HOH   B O   
6908 O  O   . HOH   G .   ? 0.2694 0.6986 0.2382 0.0936  -0.0365 -0.0616 279 HOH   B O   
6909 O  O   . HOH   G .   ? 0.5211 0.6721 0.2754 0.0307  -0.0808 0.0054  280 HOH   B O   
6910 O  O   . HOH   G .   ? 0.2902 0.7213 0.7295 0.1473  -0.0828 -0.0958 281 HOH   B O   
6911 O  O   . HOH   G .   ? 0.1815 0.2185 0.2982 0.0211  -0.0015 0.0143  282 HOH   B O   
6912 O  O   . HOH   G .   ? 0.4853 0.4814 0.5590 0.1059  0.0407  0.0718  283 HOH   B O   
6913 O  O   . HOH   G .   ? 0.2946 0.4797 0.4920 -0.1093 -0.1226 0.0680  284 HOH   B O   
6914 O  O   . HOH   G .   ? 0.1753 0.1589 0.1990 0.0030  0.0061  0.0066  285 HOH   B O   
6915 O  O   . HOH   G .   ? 0.2480 0.3505 0.3479 -0.0615 0.0638  -0.1305 286 HOH   B O   
6916 O  O   . HOH   G .   ? 0.1708 0.1575 0.3671 -0.0113 0.0072  -0.0129 287 HOH   B O   
6917 O  O   . HOH   G .   ? 0.2458 0.2744 0.2960 0.0005  -0.0751 0.0259  288 HOH   B O   
6918 O  O   . HOH   G .   ? 0.3600 0.2694 0.2283 0.0276  -0.0858 -0.0214 289 HOH   B O   
6919 O  O   . HOH   G .   ? 0.1678 0.2073 0.1660 -0.0099 -0.0168 0.0068  290 HOH   B O   
6920 O  O   . HOH   G .   ? 0.5063 0.5031 0.4870 0.0439  -0.1414 0.0448  291 HOH   B O   
6921 O  O   . HOH   G .   ? 0.3929 0.2310 0.4354 -0.1082 -0.2229 0.0974  292 HOH   B O   
6922 O  O   . HOH   G .   ? 0.1885 0.3651 0.4954 0.0417  0.0053  -0.1733 293 HOH   B O   
6923 O  O   . HOH   G .   ? 0.3429 0.3061 0.3134 -0.0416 0.0281  -0.1421 294 HOH   B O   
6924 O  O   . HOH   G .   ? 0.5843 0.5953 0.5493 0.2617  -0.0257 0.0056  295 HOH   B O   
6925 O  O   . HOH   G .   ? 0.5550 0.3596 0.3179 0.2449  0.1052  0.0904  296 HOH   B O   
6926 O  O   . HOH   G .   ? 0.5233 0.3914 0.2288 0.1297  -0.1006 0.0455  297 HOH   B O   
6927 O  O   . HOH   G .   ? 0.4387 0.5277 0.2592 0.0139  0.0894  0.0966  298 HOH   B O   
6928 O  O   . HOH   G .   ? 0.4002 0.4066 0.3800 -0.1837 0.1131  -0.0149 299 HOH   B O   
6929 O  O   . HOH   G .   ? 0.4677 0.6624 0.3801 0.1614  -0.0959 0.1132  300 HOH   B O   
6930 O  O   . HOH   G .   ? 0.1642 0.1588 0.3281 0.0098  0.0078  0.0004  301 HOH   B O   
6931 O  O   . HOH   G .   ? 0.1897 0.1650 0.2444 0.0046  0.0043  0.0140  302 HOH   B O   
6932 O  O   . HOH   G .   ? 0.3356 0.1907 0.3629 0.0661  0.1208  0.0482  303 HOH   B O   
6933 O  O   . HOH   G .   ? 0.3201 0.3269 0.5103 -0.0443 -0.1004 0.1385  304 HOH   B O   
6934 O  O   . HOH   G .   ? 0.1995 0.1688 0.3537 0.0282  -0.0951 0.0019  305 HOH   B O   
6935 O  O   . HOH   G .   ? 0.4973 0.2967 0.2322 -0.1821 0.0638  -0.0258 306 HOH   B O   
6936 O  O   . HOH   G .   ? 0.2258 0.1759 0.2650 -0.0278 -0.0290 -0.0021 307 HOH   B O   
6937 O  O   . HOH   G .   ? 0.2011 0.2864 0.6367 0.0416  -0.0322 -0.1324 308 HOH   B O   
6938 O  O   . HOH   G .   ? 0.2314 0.2005 0.1899 -0.0075 0.0193  0.0111  309 HOH   B O   
6939 O  O   . HOH   G .   ? 0.3006 0.2999 0.3994 -0.0629 0.1359  -0.1037 310 HOH   B O   
6940 O  O   . HOH   G .   ? 0.2611 0.1610 0.2559 -0.0197 -0.0278 0.0342  311 HOH   B O   
6941 O  O   . HOH   G .   ? 0.1694 0.1901 0.3116 -0.0272 -0.0172 0.0105  312 HOH   B O   
6942 O  O   . HOH   G .   ? 0.1655 0.1739 0.2997 -0.0197 -0.0105 -0.0059 313 HOH   B O   
6943 O  O   . HOH   G .   ? 0.4769 0.2614 0.3322 0.0059  -0.0166 0.0914  314 HOH   B O   
6944 O  O   . HOH   G .   ? 0.4197 0.2479 0.2727 0.1635  0.1039  0.0458  315 HOH   B O   
6945 O  O   . HOH   G .   ? 0.2340 0.3259 0.4957 -0.0196 -0.0592 -0.0055 316 HOH   B O   
6946 O  O   . HOH   G .   ? 0.1802 0.2850 0.2320 -0.0128 -0.0106 0.0627  317 HOH   B O   
6947 O  O   . HOH   G .   ? 0.2183 0.5109 0.4956 -0.0714 -0.0207 -0.0385 318 HOH   B O   
6948 O  O   . HOH   G .   ? 0.2281 0.2349 0.5700 -0.0469 -0.0004 0.1423  319 HOH   B O   
6949 O  O   . HOH   G .   ? 0.5081 0.3974 0.2688 -0.0071 -0.0563 -0.0620 320 HOH   B O   
6950 O  O   . HOH   G .   ? 0.4903 0.5211 0.2244 0.1827  -0.0991 -0.0298 321 HOH   B O   
6951 O  O   . HOH   G .   ? 0.5087 0.4153 0.4971 0.0630  0.0443  0.0490  322 HOH   B O   
6952 O  O   . HOH   G .   ? 0.4616 0.3203 0.5234 0.1167  0.2409  0.1624  323 HOH   B O   
6953 O  O   . HOH   G .   ? 0.4974 0.3557 0.4309 -0.0673 0.0212  0.1190  324 HOH   B O   
6954 O  O   . HOH   G .   ? 0.3308 0.2342 0.2575 0.0220  -0.0306 0.0411  325 HOH   B O   
6955 O  O   . HOH   G .   ? 0.1958 0.1909 0.3040 0.0241  0.0429  0.0236  326 HOH   B O   
6956 O  O   . HOH   G .   ? 0.3821 0.4400 0.8381 -0.0294 -0.1132 0.2251  327 HOH   B O   
6957 O  O   . HOH   G .   ? 0.2805 0.2047 0.4465 -0.0032 -0.0027 0.0528  328 HOH   B O   
6958 O  O   . HOH   G .   ? 0.1887 0.2890 0.3404 0.0390  -0.0138 -0.0744 329 HOH   B O   
6959 O  O   . HOH   G .   ? 0.5819 0.4910 0.7178 0.1397  -0.0670 0.2144  330 HOH   B O   
6960 O  O   . HOH   G .   ? 0.3048 0.3140 0.5589 -0.0759 -0.1678 0.1623  331 HOH   B O   
6961 O  O   . HOH   G .   ? 0.6440 0.4491 0.5099 0.0558  0.1734  0.0123  332 HOH   B O   
6962 O  O   . HOH   G .   ? 0.8627 0.2278 0.3344 0.0472  -0.0845 -0.0031 333 HOH   B O   
6963 O  O   . HOH   G .   ? 0.5549 0.3841 0.4052 0.0487  0.1321  0.1734  334 HOH   B O   
6964 O  O   . HOH   G .   ? 0.5974 0.5600 0.5755 -0.1116 -0.0565 0.1775  335 HOH   B O   
6965 O  O   . HOH   G .   ? 0.1848 0.1536 0.2431 0.0105  -0.0258 0.0118  336 HOH   B O   
6966 O  O   . HOH   G .   ? 0.5719 0.4464 0.6302 -0.0696 -0.0796 -0.1132 337 HOH   B O   
6967 O  O   . HOH   G .   ? 0.5362 0.3768 0.5024 0.0331  0.0926  -0.1427 338 HOH   B O   
6968 O  O   . HOH   G .   ? 0.4775 0.3035 0.3199 0.0507  -0.1218 -0.0788 339 HOH   B O   
6969 O  O   . HOH   G .   ? 0.7600 0.6312 0.3367 0.0036  -0.0586 0.1206  340 HOH   B O   
6970 O  O   . HOH   G .   ? 0.4645 0.7555 0.4264 -0.0493 -0.0832 0.2253  341 HOH   B O   
6971 O  O   . HOH   G .   ? 0.2594 0.5055 0.6669 -0.0625 -0.1217 0.0093  342 HOH   B O   
6972 O  O   . HOH   G .   ? 0.2811 0.1887 0.4120 0.0301  -0.1067 -0.0368 343 HOH   B O   
6973 O  O   . HOH   G .   ? 0.3676 0.6016 0.4194 -0.1039 -0.0828 -0.0817 344 HOH   B O   
6974 O  O   . HOH   G .   ? 0.2148 0.1933 0.3251 -0.0102 0.0572  -0.0091 345 HOH   B O   
6975 O  O   . HOH   G .   ? 0.5075 0.5370 0.3869 -0.0036 -0.1211 0.0206  346 HOH   B O   
6976 O  O   . HOH   G .   ? 0.4860 0.5855 0.5626 -0.1204 0.0628  0.1217  347 HOH   B O   
6977 O  O   . HOH   G .   ? 0.4387 0.5666 0.6021 0.0026  -0.1155 0.0845  348 HOH   B O   
6978 O  O   . HOH   G .   ? 0.2514 0.6484 0.3323 0.1615  -0.0675 -0.1503 349 HOH   B O   
6979 O  O   . HOH   G .   ? 0.3010 0.2266 0.4933 -0.0214 -0.0966 -0.0356 350 HOH   B O   
6980 O  O   . HOH   G .   ? 0.4362 0.5797 0.6551 0.0169  0.0070  -0.0805 351 HOH   B O   
6981 O  O   . HOH   G .   ? 0.2264 0.4502 0.4926 0.0478  0.0366  0.0162  352 HOH   B O   
6982 O  O   . HOH   G .   ? 0.3520 0.4481 0.4985 -0.1276 0.0217  -0.0640 353 HOH   B O   
6983 O  O   . HOH   G .   ? 0.3681 0.2172 0.3321 -0.0572 0.0112  -0.0748 354 HOH   B O   
6984 O  O   . HOH   G .   ? 0.3517 0.2673 0.3336 -0.0719 -0.0034 -0.0552 355 HOH   B O   
6985 O  O   . HOH   G .   ? 0.5385 0.3700 0.4347 0.0483  0.1405  -0.0814 356 HOH   B O   
6986 O  O   . HOH   G .   ? 0.4957 0.3059 0.5471 -0.1053 0.1225  0.0774  357 HOH   B O   
6987 O  O   . HOH   G .   ? 0.4868 0.5374 0.4943 0.1638  -0.1231 0.1597  358 HOH   B O   
6988 O  O   . HOH   G .   ? 0.5345 0.3551 0.5140 -0.0213 -0.1428 -0.0406 359 HOH   B O   
6989 O  O   . HOH   G .   ? 0.4830 0.4220 0.6606 0.0119  0.0778  0.1266  360 HOH   B O   
6990 O  O   . HOH   G .   ? 0.4225 0.6229 0.2930 0.1912  0.0061  0.0158  361 HOH   B O   
6991 O  O   . HOH   G .   ? 0.2432 0.3817 0.7116 -0.0828 -0.0801 -0.0741 362 HOH   B O   
6992 O  O   . HOH   G .   ? 0.5409 0.5246 0.5937 -0.0494 0.0136  0.0782  363 HOH   B O   
6993 O  O   . HOH   G .   ? 0.6484 0.2296 0.3795 -0.0302 -0.0102 0.0782  364 HOH   B O   
6994 O  O   . HOH   G .   ? 0.5190 0.5418 0.4832 -0.1109 -0.0079 -0.1114 365 HOH   B O   
6995 O  O   . HOH   G .   ? 0.4899 0.3170 0.5438 -0.1384 -0.0323 0.0148  366 HOH   B O   
6996 O  O   . HOH   G .   ? 0.6103 0.4679 0.4213 0.1171  0.0323  0.0803  367 HOH   B O   
6997 O  O   . HOH   G .   ? 0.4739 0.3762 0.5301 0.1351  -0.1198 0.0115  368 HOH   B O   
6998 O  O   . HOH   G .   ? 0.5283 0.5736 0.3689 0.1361  -0.1473 0.0769  369 HOH   B O   
6999 O  O   . HOH   G .   ? 0.3787 0.5724 0.4869 0.2208  0.0786  0.1411  370 HOH   B O   
7000 O  O   . HOH   G .   ? 0.5721 0.3957 0.3236 -0.0645 -0.1044 -0.0717 371 HOH   B O   
7001 O  O   . HOH   G .   ? 0.8292 0.7465 0.5484 0.2470  -0.1390 0.0133  372 HOH   B O   
7002 O  O   . HOH   G .   ? 0.3902 0.3485 0.4039 0.0805  -0.1231 -0.0745 373 HOH   B O   
7003 O  O   . HOH   G .   ? 0.4637 0.4825 0.4715 -0.0612 -0.0408 0.0295  374 HOH   B O   
7004 O  O   . HOH   G .   ? 0.4536 0.7000 0.5937 0.1419  0.0534  0.2659  375 HOH   B O   
7005 O  O   . HOH   G .   ? 0.5669 0.7211 0.4329 -0.1400 0.0208  -0.1399 376 HOH   B O   
7006 O  O   . HOH   G .   ? 0.2382 0.4335 0.4393 0.0139  -0.0308 -0.1009 377 HOH   B O   
7007 O  O   . HOH   G .   ? 0.3703 0.4924 0.5032 0.1383  0.0031  0.0092  378 HOH   B O   
7008 O  O   . HOH   G .   ? 0.3552 0.5685 0.2288 -0.0432 0.0225  0.0069  379 HOH   B O   
7009 O  O   . HOH   G .   ? 0.7913 0.3937 0.4918 -0.1079 -0.0874 0.0017  380 HOH   B O   
7010 O  O   . HOH   G .   ? 0.4886 0.6972 0.6264 -0.0235 0.2031  0.1175  381 HOH   B O   
7011 O  O   . HOH   G .   ? 0.3166 0.2610 0.3006 0.0064  0.0307  0.0137  382 HOH   B O   
7012 O  O   . HOH   G .   ? 0.4506 0.7745 0.5466 0.0360  0.1643  0.0243  383 HOH   B O   
7013 O  O   . HOH   G .   ? 0.6720 0.4615 0.3980 0.1121  0.1018  -0.0405 384 HOH   B O   
7014 O  O   . HOH   G .   ? 0.5389 0.5351 0.4461 0.0516  -0.0663 -0.0215 385 HOH   B O   
7015 O  O   . HOH   G .   ? 0.8045 0.5750 0.4674 0.2121  -0.0157 -0.0113 386 HOH   B O   
7016 O  O   . HOH   G .   ? 0.2563 0.4223 0.4266 -0.0777 -0.1120 -0.0138 387 HOH   B O   
7017 O  O   . HOH   G .   ? 0.6360 0.4796 0.5543 -0.0912 0.1154  -0.0461 388 HOH   B O   
7018 O  O   . HOH   G .   ? 0.5303 0.4096 0.3554 -0.0074 0.0697  -0.0351 389 HOH   B O   
7019 O  O   . HOH   G .   ? 0.4839 0.3300 0.4531 -0.1752 -0.0220 0.0734  390 HOH   B O   
7020 O  O   . HOH   G .   ? 0.3931 0.2233 0.3476 0.0505  -0.0324 0.0288  391 HOH   B O   
7021 O  O   . HOH   G .   ? 0.5733 0.4533 0.4968 0.0863  0.1250  0.1003  392 HOH   B O   
7022 O  O   . HOH   G .   ? 0.2558 0.3909 0.7302 -0.1074 -0.0610 -0.0497 393 HOH   B O   
7023 O  O   . HOH   G .   ? 0.3902 0.2217 0.5550 -0.0209 0.0661  0.0700  394 HOH   B O   
7024 O  O   . HOH   G .   ? 0.4314 0.6280 0.4283 0.1161  0.0317  -0.0997 395 HOH   B O   
7025 O  O   . HOH   G .   ? 0.3494 0.3892 0.4237 0.0176  0.0462  -0.0830 396 HOH   B O   
7026 O  O   . HOH   G .   ? 0.2114 0.2875 0.6245 -0.0723 -0.0817 0.0578  397 HOH   B O   
7027 O  O   . HOH   G .   ? 0.4682 0.4399 0.5140 0.0380  0.1094  0.1372  398 HOH   B O   
7028 O  O   . HOH   G .   ? 0.5812 0.4028 0.3068 -0.2480 -0.0625 0.0990  399 HOH   B O   
7029 O  O   . HOH   G .   ? 0.6011 0.6658 0.6676 0.0624  -0.1443 0.2241  400 HOH   B O   
7030 O  O   . HOH   G .   ? 0.5862 0.5919 0.3765 0.2107  -0.0391 -0.0569 401 HOH   B O   
# 
